data_9CR1
# 
_entry.id   9CR1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CR1         pdb_00009cr1 10.2210/pdb9cr1/pdb 
WWPDB D_1000283893 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CR1 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-20 
_pdbx_database_status.SG_entry                        N 
_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           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mlemieux@ualberta.ca     'M. Joanne' Lemieux ?  'principal investigator/group leader' 0000-0003-4745-9153 
3 john.vederas@ualberta.ca John        Vederas C. 'principal investigator/group leader' 0000-0002-2996-0326 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, P.'      1 0000-0002-0434-6346 
'Lamer, T.'     2 0000-0002-1511-4540 
'Vederas, J.C.' 3 0000-0002-2996-0326 
'Lemieux, M.J.' 4 0000-0003-4745-9153 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            300 
_citation.language                  ? 
_citation.page_first                107896 
_citation.page_last                 107896 
_citation.title                     
;Discovery, characterization, and structure of a cofactor-independent histidine racemase from the oral pathogen Fusobacterium nucleatum.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.107896 
_citation.pdbx_database_id_PubMed   39424140 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lamer, T.'        1 ? 
primary 'Chen, P.'         2 ? 
primary 'Venter, M.J.'     3 ? 
primary 'van Belkum, M.J.' 4 ? 
primary 'Wijewardane, A.'  5 ? 
primary 'Wu, C.'           6 ? 
primary 'Lemieux, M.J.'    7 ? 
primary 'Vederas, J.C.'    8 ? 
# 
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 'Histidine racemase' 31087.467 4  ? C67S ? ? 
2 non-polymer syn 'SULFATE ION'        96.063    8  ? ?    ? ? 
3 water       nat water                18.015    74 ? ?    ? ? 
# 
_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       
;MDRKVQVLDFIKINPAGNITILIDNFDIYDKNIPKLSEEIMKETNLYAEQVGFIKDSHLQMMGGEFSGNASRAFASLLAF
RDKDFSKQKNYNITCSGESKVLDVDVRNDGAKNKFLAKIKMPKFLSLEEINVDEYKLGLVRFSGINHFIFNIKENKETSF
ENIIDLVKKYLSNEEYSAFGIMFFDSDNLSMKPYVYVKEVGSGVYENSCASGTTALGYYLKKCKNLDRAKIVQPNGWLEY
IIENDEMYIDGPVEIIAEGKIYIGKHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDRKVQVLDFIKINPAGNITILIDNFDIYDKNIPKLSEEIMKETNLYAEQVGFIKDSHLQMMGGEFSGNASRAFASLLAF
RDKDFSKQKNYNITCSGESKVLDVDVRNDGAKNKFLAKIKMPKFLSLEEINVDEYKLGLVRFSGINHFIFNIKENKETSF
ENIIDLVKKYLSNEEYSAFGIMFFDSDNLSMKPYVYVKEVGSGVYENSCASGTTALGYYLKKCKNLDRAKIVQPNGWLEY
IIENDEMYIDGPVEIIAEGKIYIGKHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 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   ASP n 
1 3   ARG n 
1 4   LYS n 
1 5   VAL n 
1 6   GLN n 
1 7   VAL n 
1 8   LEU n 
1 9   ASP n 
1 10  PHE n 
1 11  ILE n 
1 12  LYS n 
1 13  ILE n 
1 14  ASN n 
1 15  PRO n 
1 16  ALA n 
1 17  GLY n 
1 18  ASN n 
1 19  ILE n 
1 20  THR n 
1 21  ILE n 
1 22  LEU n 
1 23  ILE n 
1 24  ASP n 
1 25  ASN n 
1 26  PHE n 
1 27  ASP n 
1 28  ILE n 
1 29  TYR n 
1 30  ASP n 
1 31  LYS n 
1 32  ASN n 
1 33  ILE n 
1 34  PRO n 
1 35  LYS n 
1 36  LEU n 
1 37  SER n 
1 38  GLU n 
1 39  GLU n 
1 40  ILE n 
1 41  MET n 
1 42  LYS n 
1 43  GLU n 
1 44  THR n 
1 45  ASN n 
1 46  LEU n 
1 47  TYR n 
1 48  ALA n 
1 49  GLU n 
1 50  GLN n 
1 51  VAL n 
1 52  GLY n 
1 53  PHE n 
1 54  ILE n 
1 55  LYS n 
1 56  ASP n 
1 57  SER n 
1 58  HIS n 
1 59  LEU n 
1 60  GLN n 
1 61  MET n 
1 62  MET n 
1 63  GLY n 
1 64  GLY n 
1 65  GLU n 
1 66  PHE n 
1 67  SER n 
1 68  GLY n 
1 69  ASN n 
1 70  ALA n 
1 71  SER n 
1 72  ARG n 
1 73  ALA n 
1 74  PHE n 
1 75  ALA n 
1 76  SER n 
1 77  LEU n 
1 78  LEU n 
1 79  ALA n 
1 80  PHE n 
1 81  ARG n 
1 82  ASP n 
1 83  LYS n 
1 84  ASP n 
1 85  PHE n 
1 86  SER n 
1 87  LYS n 
1 88  GLN n 
1 89  LYS n 
1 90  ASN n 
1 91  TYR n 
1 92  ASN n 
1 93  ILE n 
1 94  THR n 
1 95  CYS n 
1 96  SER n 
1 97  GLY n 
1 98  GLU n 
1 99  SER n 
1 100 LYS n 
1 101 VAL n 
1 102 LEU n 
1 103 ASP n 
1 104 VAL n 
1 105 ASP n 
1 106 VAL n 
1 107 ARG n 
1 108 ASN n 
1 109 ASP n 
1 110 GLY n 
1 111 ALA n 
1 112 LYS n 
1 113 ASN n 
1 114 LYS n 
1 115 PHE n 
1 116 LEU n 
1 117 ALA n 
1 118 LYS n 
1 119 ILE n 
1 120 LYS n 
1 121 MET n 
1 122 PRO n 
1 123 LYS n 
1 124 PHE n 
1 125 LEU n 
1 126 SER n 
1 127 LEU n 
1 128 GLU n 
1 129 GLU n 
1 130 ILE n 
1 131 ASN n 
1 132 VAL n 
1 133 ASP n 
1 134 GLU n 
1 135 TYR n 
1 136 LYS n 
1 137 LEU n 
1 138 GLY n 
1 139 LEU n 
1 140 VAL n 
1 141 ARG n 
1 142 PHE n 
1 143 SER n 
1 144 GLY n 
1 145 ILE n 
1 146 ASN n 
1 147 HIS n 
1 148 PHE n 
1 149 ILE n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 LYS n 
1 154 GLU n 
1 155 ASN n 
1 156 LYS n 
1 157 GLU n 
1 158 THR n 
1 159 SER n 
1 160 PHE n 
1 161 GLU n 
1 162 ASN n 
1 163 ILE n 
1 164 ILE n 
1 165 ASP n 
1 166 LEU n 
1 167 VAL n 
1 168 LYS n 
1 169 LYS n 
1 170 TYR n 
1 171 LEU n 
1 172 SER n 
1 173 ASN n 
1 174 GLU n 
1 175 GLU n 
1 176 TYR n 
1 177 SER n 
1 178 ALA n 
1 179 PHE n 
1 180 GLY n 
1 181 ILE n 
1 182 MET n 
1 183 PHE n 
1 184 PHE n 
1 185 ASP n 
1 186 SER n 
1 187 ASP n 
1 188 ASN n 
1 189 LEU n 
1 190 SER n 
1 191 MET n 
1 192 LYS n 
1 193 PRO n 
1 194 TYR n 
1 195 VAL n 
1 196 TYR n 
1 197 VAL n 
1 198 LYS n 
1 199 GLU n 
1 200 VAL n 
1 201 GLY n 
1 202 SER n 
1 203 GLY n 
1 204 VAL n 
1 205 TYR n 
1 206 GLU n 
1 207 ASN n 
1 208 SER n 
1 209 CYS n 
1 210 ALA n 
1 211 SER n 
1 212 GLY n 
1 213 THR n 
1 214 THR n 
1 215 ALA n 
1 216 LEU n 
1 217 GLY n 
1 218 TYR n 
1 219 TYR n 
1 220 LEU n 
1 221 LYS n 
1 222 LYS n 
1 223 CYS n 
1 224 LYS n 
1 225 ASN n 
1 226 LEU n 
1 227 ASP n 
1 228 ARG n 
1 229 ALA n 
1 230 LYS n 
1 231 ILE n 
1 232 VAL n 
1 233 GLN n 
1 234 PRO n 
1 235 ASN n 
1 236 GLY n 
1 237 TRP n 
1 238 LEU n 
1 239 GLU n 
1 240 TYR n 
1 241 ILE n 
1 242 ILE n 
1 243 GLU n 
1 244 ASN n 
1 245 ASP n 
1 246 GLU n 
1 247 MET n 
1 248 TYR n 
1 249 ILE n 
1 250 ASP n 
1 251 GLY n 
1 252 PRO n 
1 253 VAL n 
1 254 GLU n 
1 255 ILE n 
1 256 ILE n 
1 257 ALA n 
1 258 GLU n 
1 259 GLY n 
1 260 LYS n 
1 261 ILE n 
1 262 TYR n 
1 263 ILE n 
1 264 GLY n 
1 265 LYS n 
1 266 HIS n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS 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                   271 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FN1732 
_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      'Fusobacterium nucleatum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     851 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  HIS 58  58  58  HIS HIS A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 MET 121 121 121 MET MET A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 MET 191 191 191 MET MET A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 CYS 223 223 223 CYS CYS A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 TRP 237 237 237 TRP TRP A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 MET 247 247 247 MET MET A . n 
A 1 248 TYR 248 248 248 TYR TYR A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 HIS 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 HIS 269 269 ?   ?   ?   A . n 
A 1 270 HIS 270 270 ?   ?   ?   A . n 
A 1 271 HIS 271 271 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   3   ARG ARG B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   GLN 6   6   6   GLN GLN B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   ASP 9   9   9   ASP ASP B . n 
B 1 10  PHE 10  10  10  PHE PHE B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  ILE 13  13  13  ILE ILE B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  THR 20  20  20  THR THR B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  ASN 25  25  25  ASN ASN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  TYR 29  29  29  TYR TYR B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  SER 37  37  37  SER SER B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  GLN 50  50  50  GLN GLN B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  PHE 53  53  53  PHE PHE B . n 
B 1 54  ILE 54  54  54  ILE ILE B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  HIS 58  58  58  HIS HIS B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  MET 62  62  62  MET MET B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  SER 71  71  71  SER SER B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  PHE 85  85  85  PHE PHE B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  GLN 88  88  88  GLN GLN B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  THR 94  94  94  THR THR B . n 
B 1 95  CYS 95  95  95  CYS CYS B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 PHE 115 115 115 PHE PHE B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 ILE 119 119 119 ILE ILE B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 MET 121 121 121 MET MET B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 PHE 124 124 124 PHE PHE B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 GLU 128 128 128 GLU GLU B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 TYR 135 135 135 TYR TYR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 SER 143 143 143 SER SER B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 HIS 147 147 147 HIS HIS B . n 
B 1 148 PHE 148 148 148 PHE PHE B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 PHE 160 160 160 PHE PHE B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 ASP 165 165 165 ASP ASP B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 ASN 173 173 173 ASN ASN B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 TYR 176 176 176 TYR TYR B . n 
B 1 177 SER 177 177 177 SER SER B . n 
B 1 178 ALA 178 178 178 ALA ALA B . n 
B 1 179 PHE 179 179 179 PHE PHE B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 MET 182 182 182 MET MET B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ASN 188 188 188 ASN ASN B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 MET 191 191 191 MET MET B . n 
B 1 192 LYS 192 192 192 LYS LYS B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 GLY 203 203 203 GLY GLY B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 TYR 205 205 205 TYR TYR B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 ASN 207 207 207 ASN ASN B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 SER 211 211 211 SER SER B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 TYR 218 218 218 TYR TYR B . n 
B 1 219 TYR 219 219 219 TYR TYR B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 LYS 222 222 222 LYS LYS B . n 
B 1 223 CYS 223 223 223 CYS CYS B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ASN 225 225 225 ASN ASN B . n 
B 1 226 LEU 226 226 226 LEU LEU B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 ALA 229 229 229 ALA ALA B . n 
B 1 230 LYS 230 230 230 LYS LYS B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 TRP 237 237 237 TRP TRP B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ILE 242 242 242 ILE ILE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 GLU 246 246 246 GLU GLU B . n 
B 1 247 MET 247 247 247 MET MET B . n 
B 1 248 TYR 248 248 248 TYR TYR B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 GLY 259 259 259 GLY GLY B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 TYR 262 262 262 TYR TYR B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 HIS 266 266 ?   ?   ?   B . n 
B 1 267 HIS 267 267 ?   ?   ?   B . n 
B 1 268 HIS 268 268 ?   ?   ?   B . n 
B 1 269 HIS 269 269 ?   ?   ?   B . n 
B 1 270 HIS 270 270 ?   ?   ?   B . n 
B 1 271 HIS 271 271 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ASP 2   2   2   ASP ASP C . n 
C 1 3   ARG 3   3   3   ARG ARG C . n 
C 1 4   LYS 4   4   4   LYS LYS C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   GLN 6   6   6   GLN GLN C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   ASP 9   9   9   ASP ASP C . n 
C 1 10  PHE 10  10  10  PHE PHE C . n 
C 1 11  ILE 11  11  11  ILE ILE C . n 
C 1 12  LYS 12  12  12  LYS LYS C . n 
C 1 13  ILE 13  13  13  ILE ILE C . n 
C 1 14  ASN 14  14  14  ASN ASN C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  ALA 16  16  16  ALA ALA C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  ASN 18  18  18  ASN ASN C . n 
C 1 19  ILE 19  19  19  ILE ILE C . n 
C 1 20  THR 20  20  20  THR THR C . n 
C 1 21  ILE 21  21  21  ILE ILE C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  ILE 23  23  23  ILE ILE C . n 
C 1 24  ASP 24  24  24  ASP ASP C . n 
C 1 25  ASN 25  25  25  ASN ASN C . n 
C 1 26  PHE 26  26  26  PHE PHE C . n 
C 1 27  ASP 27  27  27  ASP ASP C . n 
C 1 28  ILE 28  28  28  ILE ILE C . n 
C 1 29  TYR 29  29  29  TYR TYR C . n 
C 1 30  ASP 30  30  30  ASP ASP C . n 
C 1 31  LYS 31  31  31  LYS LYS C . n 
C 1 32  ASN 32  32  32  ASN ASN C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  PRO 34  34  34  PRO PRO C . n 
C 1 35  LYS 35  35  35  LYS LYS C . n 
C 1 36  LEU 36  36  36  LEU LEU C . n 
C 1 37  SER 37  37  37  SER SER C . n 
C 1 38  GLU 38  38  38  GLU GLU C . n 
C 1 39  GLU 39  39  39  GLU GLU C . n 
C 1 40  ILE 40  40  40  ILE ILE C . n 
C 1 41  MET 41  41  41  MET MET C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  GLU 43  43  43  GLU GLU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  ASN 45  45  45  ASN ASN C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  TYR 47  47  47  TYR TYR C . n 
C 1 48  ALA 48  48  48  ALA ALA C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  GLN 50  50  50  GLN GLN C . n 
C 1 51  VAL 51  51  51  VAL VAL C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  PHE 53  53  53  PHE PHE C . n 
C 1 54  ILE 54  54  54  ILE ILE C . n 
C 1 55  LYS 55  55  55  LYS LYS C . n 
C 1 56  ASP 56  56  56  ASP ASP C . n 
C 1 57  SER 57  57  57  SER SER C . n 
C 1 58  HIS 58  58  58  HIS HIS C . n 
C 1 59  LEU 59  59  59  LEU LEU C . n 
C 1 60  GLN 60  60  60  GLN GLN C . n 
C 1 61  MET 61  61  61  MET MET C . n 
C 1 62  MET 62  62  62  MET MET C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  GLU 65  65  65  GLU GLU C . n 
C 1 66  PHE 66  66  66  PHE PHE C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  ASN 69  69  69  ASN ASN C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  SER 71  71  71  SER SER C . n 
C 1 72  ARG 72  72  72  ARG ARG C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  PHE 74  74  74  PHE PHE C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  PHE 80  80  80  PHE PHE C . n 
C 1 81  ARG 81  81  81  ARG ARG C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  LYS 83  83  83  LYS LYS C . n 
C 1 84  ASP 84  84  84  ASP ASP C . n 
C 1 85  PHE 85  85  85  PHE PHE C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  GLN 88  88  88  GLN GLN C . n 
C 1 89  LYS 89  89  89  LYS LYS C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  TYR 91  91  91  TYR TYR C . n 
C 1 92  ASN 92  92  92  ASN ASN C . n 
C 1 93  ILE 93  93  93  ILE ILE C . n 
C 1 94  THR 94  94  94  THR THR C . n 
C 1 95  CYS 95  95  95  CYS CYS C . n 
C 1 96  SER 96  96  96  SER SER C . n 
C 1 97  GLY 97  97  97  GLY GLY C . n 
C 1 98  GLU 98  98  98  GLU GLU C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 LYS 100 100 100 LYS LYS C . n 
C 1 101 VAL 101 101 101 VAL VAL C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 VAL 104 104 104 VAL VAL C . n 
C 1 105 ASP 105 105 105 ASP ASP C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 ARG 107 107 107 ARG ARG C . n 
C 1 108 ASN 108 108 108 ASN ASN C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 GLY 110 110 110 GLY GLY C . n 
C 1 111 ALA 111 111 111 ALA ALA C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 ASN 113 113 113 ASN ASN C . n 
C 1 114 LYS 114 114 114 LYS LYS C . n 
C 1 115 PHE 115 115 115 PHE PHE C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 ALA 117 117 117 ALA ALA C . n 
C 1 118 LYS 118 118 118 LYS LYS C . n 
C 1 119 ILE 119 119 119 ILE ILE C . n 
C 1 120 LYS 120 120 120 LYS LYS C . n 
C 1 121 MET 121 121 121 MET MET C . n 
C 1 122 PRO 122 122 122 PRO PRO C . n 
C 1 123 LYS 123 123 123 LYS LYS C . n 
C 1 124 PHE 124 124 124 PHE PHE C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 SER 126 126 126 SER SER C . n 
C 1 127 LEU 127 127 127 LEU LEU C . n 
C 1 128 GLU 128 128 128 GLU GLU C . n 
C 1 129 GLU 129 129 129 GLU GLU C . n 
C 1 130 ILE 130 130 130 ILE ILE C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 ASP 133 133 133 ASP ASP C . n 
C 1 134 GLU 134 134 134 GLU GLU C . n 
C 1 135 TYR 135 135 135 TYR TYR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 LEU 137 137 137 LEU LEU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 VAL 140 140 140 VAL VAL C . n 
C 1 141 ARG 141 141 141 ARG ARG C . n 
C 1 142 PHE 142 142 142 PHE PHE C . n 
C 1 143 SER 143 143 143 SER SER C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 ILE 145 145 145 ILE ILE C . n 
C 1 146 ASN 146 146 146 ASN ASN C . n 
C 1 147 HIS 147 147 147 HIS HIS C . n 
C 1 148 PHE 148 148 148 PHE PHE C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 ASN 151 151 151 ASN ASN C . n 
C 1 152 ILE 152 152 152 ILE ILE C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 GLU 154 154 154 GLU GLU C . n 
C 1 155 ASN 155 155 155 ASN ASN C . n 
C 1 156 LYS 156 156 156 LYS LYS C . n 
C 1 157 GLU 157 157 157 GLU GLU C . n 
C 1 158 THR 158 158 158 THR THR C . n 
C 1 159 SER 159 159 159 SER SER C . n 
C 1 160 PHE 160 160 160 PHE PHE C . n 
C 1 161 GLU 161 161 161 GLU GLU C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 ILE 163 163 163 ILE ILE C . n 
C 1 164 ILE 164 164 164 ILE ILE C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 VAL 167 167 167 VAL VAL C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 LYS 169 169 169 LYS LYS C . n 
C 1 170 TYR 170 170 170 TYR TYR C . n 
C 1 171 LEU 171 171 171 LEU LEU C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 ASN 173 173 173 ASN ASN C . n 
C 1 174 GLU 174 174 174 GLU GLU C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 TYR 176 176 176 TYR TYR C . n 
C 1 177 SER 177 177 177 SER SER C . n 
C 1 178 ALA 178 178 178 ALA ALA C . n 
C 1 179 PHE 179 179 179 PHE PHE C . n 
C 1 180 GLY 180 180 180 GLY GLY C . n 
C 1 181 ILE 181 181 181 ILE ILE C . n 
C 1 182 MET 182 182 182 MET MET C . n 
C 1 183 PHE 183 183 183 PHE PHE C . n 
C 1 184 PHE 184 184 184 PHE PHE C . n 
C 1 185 ASP 185 185 185 ASP ASP C . n 
C 1 186 SER 186 186 186 SER SER C . n 
C 1 187 ASP 187 187 187 ASP ASP C . n 
C 1 188 ASN 188 188 188 ASN ASN C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 MET 191 191 191 MET MET C . n 
C 1 192 LYS 192 192 192 LYS LYS C . n 
C 1 193 PRO 193 193 193 PRO PRO C . n 
C 1 194 TYR 194 194 194 TYR TYR C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 TYR 196 196 196 TYR TYR C . n 
C 1 197 VAL 197 197 197 VAL VAL C . n 
C 1 198 LYS 198 198 198 LYS LYS C . n 
C 1 199 GLU 199 199 199 GLU GLU C . n 
C 1 200 VAL 200 200 200 VAL VAL C . n 
C 1 201 GLY 201 201 201 GLY GLY C . n 
C 1 202 SER 202 202 202 SER SER C . n 
C 1 203 GLY 203 203 203 GLY GLY C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
C 1 205 TYR 205 205 205 TYR TYR C . n 
C 1 206 GLU 206 206 206 GLU GLU C . n 
C 1 207 ASN 207 207 207 ASN ASN C . n 
C 1 208 SER 208 208 208 SER SER C . n 
C 1 209 CYS 209 209 209 CYS CYS C . n 
C 1 210 ALA 210 210 210 ALA ALA C . n 
C 1 211 SER 211 211 211 SER SER C . n 
C 1 212 GLY 212 212 212 GLY GLY C . n 
C 1 213 THR 213 213 213 THR THR C . n 
C 1 214 THR 214 214 214 THR THR C . n 
C 1 215 ALA 215 215 215 ALA ALA C . n 
C 1 216 LEU 216 216 216 LEU LEU C . n 
C 1 217 GLY 217 217 217 GLY GLY C . n 
C 1 218 TYR 218 218 218 TYR TYR C . n 
C 1 219 TYR 219 219 219 TYR TYR C . n 
C 1 220 LEU 220 220 220 LEU LEU C . n 
C 1 221 LYS 221 221 221 LYS LYS C . n 
C 1 222 LYS 222 222 222 LYS LYS C . n 
C 1 223 CYS 223 223 223 CYS CYS C . n 
C 1 224 LYS 224 224 224 LYS LYS C . n 
C 1 225 ASN 225 225 225 ASN ASN C . n 
C 1 226 LEU 226 226 226 LEU LEU C . n 
C 1 227 ASP 227 227 227 ASP ASP C . n 
C 1 228 ARG 228 228 228 ARG ARG C . n 
C 1 229 ALA 229 229 229 ALA ALA C . n 
C 1 230 LYS 230 230 230 LYS LYS C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 VAL 232 232 232 VAL VAL C . n 
C 1 233 GLN 233 233 233 GLN GLN C . n 
C 1 234 PRO 234 234 234 PRO PRO C . n 
C 1 235 ASN 235 235 235 ASN ASN C . n 
C 1 236 GLY 236 236 236 GLY GLY C . n 
C 1 237 TRP 237 237 237 TRP TRP C . n 
C 1 238 LEU 238 238 238 LEU LEU C . n 
C 1 239 GLU 239 239 239 GLU GLU C . n 
C 1 240 TYR 240 240 240 TYR TYR C . n 
C 1 241 ILE 241 241 241 ILE ILE C . n 
C 1 242 ILE 242 242 242 ILE ILE C . n 
C 1 243 GLU 243 243 243 GLU GLU C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASP 245 245 245 ASP ASP C . n 
C 1 246 GLU 246 246 246 GLU GLU C . n 
C 1 247 MET 247 247 247 MET MET C . n 
C 1 248 TYR 248 248 248 TYR TYR C . n 
C 1 249 ILE 249 249 249 ILE ILE C . n 
C 1 250 ASP 250 250 250 ASP ASP C . n 
C 1 251 GLY 251 251 251 GLY GLY C . n 
C 1 252 PRO 252 252 252 PRO PRO C . n 
C 1 253 VAL 253 253 253 VAL VAL C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ILE 255 255 255 ILE ILE C . n 
C 1 256 ILE 256 256 256 ILE ILE C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 GLU 258 258 258 GLU GLU C . n 
C 1 259 GLY 259 259 259 GLY GLY C . n 
C 1 260 LYS 260 260 260 LYS LYS C . n 
C 1 261 ILE 261 261 261 ILE ILE C . n 
C 1 262 TYR 262 262 262 TYR TYR C . n 
C 1 263 ILE 263 263 263 ILE ILE C . n 
C 1 264 GLY 264 264 264 GLY GLY C . n 
C 1 265 LYS 265 265 265 LYS LYS C . n 
C 1 266 HIS 266 266 ?   ?   ?   C . n 
C 1 267 HIS 267 267 ?   ?   ?   C . n 
C 1 268 HIS 268 268 ?   ?   ?   C . n 
C 1 269 HIS 269 269 ?   ?   ?   C . n 
C 1 270 HIS 270 270 ?   ?   ?   C . n 
C 1 271 HIS 271 271 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ASP 2   2   ?   ?   ?   D . n 
D 1 3   ARG 3   3   3   ARG ARG D . n 
D 1 4   LYS 4   4   4   LYS LYS D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   GLN 6   6   6   GLN GLN D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   ASP 9   9   9   ASP ASP D . n 
D 1 10  PHE 10  10  10  PHE PHE D . n 
D 1 11  ILE 11  11  11  ILE ILE D . n 
D 1 12  LYS 12  12  12  LYS LYS D . n 
D 1 13  ILE 13  13  13  ILE ILE D . n 
D 1 14  ASN 14  14  14  ASN ASN D . n 
D 1 15  PRO 15  15  15  PRO PRO D . n 
D 1 16  ALA 16  16  16  ALA ALA D . n 
D 1 17  GLY 17  17  17  GLY GLY D . n 
D 1 18  ASN 18  18  18  ASN ASN D . n 
D 1 19  ILE 19  19  19  ILE ILE D . n 
D 1 20  THR 20  20  20  THR THR D . n 
D 1 21  ILE 21  21  21  ILE ILE D . n 
D 1 22  LEU 22  22  22  LEU LEU D . n 
D 1 23  ILE 23  23  23  ILE ILE D . n 
D 1 24  ASP 24  24  24  ASP ASP D . n 
D 1 25  ASN 25  25  25  ASN ASN D . n 
D 1 26  PHE 26  26  26  PHE PHE D . n 
D 1 27  ASP 27  27  27  ASP ASP D . n 
D 1 28  ILE 28  28  28  ILE ILE D . n 
D 1 29  TYR 29  29  29  TYR TYR D . n 
D 1 30  ASP 30  30  30  ASP ASP D . n 
D 1 31  LYS 31  31  31  LYS LYS D . n 
D 1 32  ASN 32  32  32  ASN ASN D . n 
D 1 33  ILE 33  33  33  ILE ILE D . n 
D 1 34  PRO 34  34  34  PRO PRO D . n 
D 1 35  LYS 35  35  35  LYS LYS D . n 
D 1 36  LEU 36  36  36  LEU LEU D . n 
D 1 37  SER 37  37  37  SER SER D . n 
D 1 38  GLU 38  38  38  GLU GLU D . n 
D 1 39  GLU 39  39  39  GLU GLU D . n 
D 1 40  ILE 40  40  40  ILE ILE D . n 
D 1 41  MET 41  41  41  MET MET D . n 
D 1 42  LYS 42  42  42  LYS LYS D . n 
D 1 43  GLU 43  43  43  GLU GLU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  ASN 45  45  45  ASN ASN D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  TYR 47  47  47  TYR TYR D . n 
D 1 48  ALA 48  48  48  ALA ALA D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  GLN 50  50  50  GLN GLN D . n 
D 1 51  VAL 51  51  51  VAL VAL D . n 
D 1 52  GLY 52  52  52  GLY GLY D . n 
D 1 53  PHE 53  53  53  PHE PHE D . n 
D 1 54  ILE 54  54  54  ILE ILE D . n 
D 1 55  LYS 55  55  55  LYS LYS D . n 
D 1 56  ASP 56  56  56  ASP ASP D . n 
D 1 57  SER 57  57  57  SER SER D . n 
D 1 58  HIS 58  58  58  HIS HIS D . n 
D 1 59  LEU 59  59  59  LEU LEU D . n 
D 1 60  GLN 60  60  60  GLN GLN D . n 
D 1 61  MET 61  61  61  MET MET D . n 
D 1 62  MET 62  62  62  MET MET D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  GLY 64  64  64  GLY GLY D . n 
D 1 65  GLU 65  65  65  GLU GLU D . n 
D 1 66  PHE 66  66  66  PHE PHE D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  GLY 68  68  68  GLY GLY D . n 
D 1 69  ASN 69  69  69  ASN ASN D . n 
D 1 70  ALA 70  70  70  ALA ALA D . n 
D 1 71  SER 71  71  71  SER SER D . n 
D 1 72  ARG 72  72  72  ARG ARG D . n 
D 1 73  ALA 73  73  73  ALA ALA D . n 
D 1 74  PHE 74  74  74  PHE PHE D . n 
D 1 75  ALA 75  75  75  ALA ALA D . n 
D 1 76  SER 76  76  76  SER SER D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  ALA 79  79  79  ALA ALA D . n 
D 1 80  PHE 80  80  80  PHE PHE D . n 
D 1 81  ARG 81  81  81  ARG ARG D . n 
D 1 82  ASP 82  82  82  ASP ASP D . n 
D 1 83  LYS 83  83  83  LYS LYS D . n 
D 1 84  ASP 84  84  84  ASP ASP D . n 
D 1 85  PHE 85  85  85  PHE PHE D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  LYS 87  87  87  LYS LYS D . n 
D 1 88  GLN 88  88  88  GLN GLN D . n 
D 1 89  LYS 89  89  89  LYS LYS D . n 
D 1 90  ASN 90  90  90  ASN ASN D . n 
D 1 91  TYR 91  91  91  TYR TYR D . n 
D 1 92  ASN 92  92  92  ASN ASN D . n 
D 1 93  ILE 93  93  93  ILE ILE D . n 
D 1 94  THR 94  94  94  THR THR D . n 
D 1 95  CYS 95  95  95  CYS CYS D . n 
D 1 96  SER 96  96  96  SER SER D . n 
D 1 97  GLY 97  97  97  GLY GLY D . n 
D 1 98  GLU 98  98  98  GLU GLU D . n 
D 1 99  SER 99  99  99  SER SER D . n 
D 1 100 LYS 100 100 100 LYS LYS D . n 
D 1 101 VAL 101 101 101 VAL VAL D . n 
D 1 102 LEU 102 102 102 LEU LEU D . n 
D 1 103 ASP 103 103 103 ASP ASP D . n 
D 1 104 VAL 104 104 104 VAL VAL D . n 
D 1 105 ASP 105 105 105 ASP ASP D . n 
D 1 106 VAL 106 106 106 VAL VAL D . n 
D 1 107 ARG 107 107 107 ARG ARG D . n 
D 1 108 ASN 108 108 108 ASN ASN D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 GLY 110 110 110 GLY GLY D . n 
D 1 111 ALA 111 111 111 ALA ALA D . n 
D 1 112 LYS 112 112 112 LYS LYS D . n 
D 1 113 ASN 113 113 113 ASN ASN D . n 
D 1 114 LYS 114 114 114 LYS LYS D . n 
D 1 115 PHE 115 115 115 PHE PHE D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 ALA 117 117 117 ALA ALA D . n 
D 1 118 LYS 118 118 118 LYS LYS D . n 
D 1 119 ILE 119 119 119 ILE ILE D . n 
D 1 120 LYS 120 120 120 LYS LYS D . n 
D 1 121 MET 121 121 121 MET MET D . n 
D 1 122 PRO 122 122 122 PRO PRO D . n 
D 1 123 LYS 123 123 123 LYS LYS D . n 
D 1 124 PHE 124 124 124 PHE PHE D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 SER 126 126 126 SER SER D . n 
D 1 127 LEU 127 127 127 LEU LEU D . n 
D 1 128 GLU 128 128 128 GLU GLU D . n 
D 1 129 GLU 129 129 129 GLU GLU D . n 
D 1 130 ILE 130 130 130 ILE ILE D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 VAL 132 132 132 VAL VAL D . n 
D 1 133 ASP 133 133 133 ASP ASP D . n 
D 1 134 GLU 134 134 134 GLU GLU D . n 
D 1 135 TYR 135 135 135 TYR TYR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 LEU 137 137 137 LEU LEU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 VAL 140 140 140 VAL VAL D . n 
D 1 141 ARG 141 141 141 ARG ARG D . n 
D 1 142 PHE 142 142 142 PHE PHE D . n 
D 1 143 SER 143 143 143 SER SER D . n 
D 1 144 GLY 144 144 144 GLY GLY D . n 
D 1 145 ILE 145 145 145 ILE ILE D . n 
D 1 146 ASN 146 146 146 ASN ASN D . n 
D 1 147 HIS 147 147 147 HIS HIS D . n 
D 1 148 PHE 148 148 148 PHE PHE D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 PHE 150 150 150 PHE PHE D . n 
D 1 151 ASN 151 151 151 ASN ASN D . n 
D 1 152 ILE 152 152 152 ILE ILE D . n 
D 1 153 LYS 153 153 153 LYS LYS D . n 
D 1 154 GLU 154 154 154 GLU GLU D . n 
D 1 155 ASN 155 155 155 ASN ASN D . n 
D 1 156 LYS 156 156 156 LYS LYS D . n 
D 1 157 GLU 157 157 157 GLU GLU D . n 
D 1 158 THR 158 158 158 THR THR D . n 
D 1 159 SER 159 159 159 SER SER D . n 
D 1 160 PHE 160 160 160 PHE PHE D . n 
D 1 161 GLU 161 161 161 GLU GLU D . n 
D 1 162 ASN 162 162 162 ASN ASN D . n 
D 1 163 ILE 163 163 163 ILE ILE D . n 
D 1 164 ILE 164 164 164 ILE ILE D . n 
D 1 165 ASP 165 165 165 ASP ASP D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 VAL 167 167 167 VAL VAL D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 LYS 169 169 169 LYS LYS D . n 
D 1 170 TYR 170 170 170 TYR TYR D . n 
D 1 171 LEU 171 171 171 LEU LEU D . n 
D 1 172 SER 172 172 172 SER SER D . n 
D 1 173 ASN 173 173 173 ASN ASN D . n 
D 1 174 GLU 174 174 174 GLU GLU D . n 
D 1 175 GLU 175 175 175 GLU GLU D . n 
D 1 176 TYR 176 176 176 TYR TYR D . n 
D 1 177 SER 177 177 177 SER SER D . n 
D 1 178 ALA 178 178 178 ALA ALA D . n 
D 1 179 PHE 179 179 179 PHE PHE D . n 
D 1 180 GLY 180 180 180 GLY GLY D . n 
D 1 181 ILE 181 181 181 ILE ILE D . n 
D 1 182 MET 182 182 182 MET MET D . n 
D 1 183 PHE 183 183 183 PHE PHE D . n 
D 1 184 PHE 184 184 184 PHE PHE D . n 
D 1 185 ASP 185 185 185 ASP ASP D . n 
D 1 186 SER 186 186 186 SER SER D . n 
D 1 187 ASP 187 187 187 ASP ASP D . n 
D 1 188 ASN 188 188 188 ASN ASN D . n 
D 1 189 LEU 189 189 189 LEU LEU D . n 
D 1 190 SER 190 190 190 SER SER D . n 
D 1 191 MET 191 191 191 MET MET D . n 
D 1 192 LYS 192 192 192 LYS LYS D . n 
D 1 193 PRO 193 193 193 PRO PRO D . n 
D 1 194 TYR 194 194 194 TYR TYR D . n 
D 1 195 VAL 195 195 195 VAL VAL D . n 
D 1 196 TYR 196 196 196 TYR TYR D . n 
D 1 197 VAL 197 197 197 VAL VAL D . n 
D 1 198 LYS 198 198 198 LYS LYS D . n 
D 1 199 GLU 199 199 199 GLU GLU D . n 
D 1 200 VAL 200 200 200 VAL VAL D . n 
D 1 201 GLY 201 201 201 GLY GLY D . n 
D 1 202 SER 202 202 202 SER SER D . n 
D 1 203 GLY 203 203 203 GLY GLY D . n 
D 1 204 VAL 204 204 204 VAL VAL D . n 
D 1 205 TYR 205 205 205 TYR TYR D . n 
D 1 206 GLU 206 206 206 GLU GLU D . n 
D 1 207 ASN 207 207 207 ASN ASN D . n 
D 1 208 SER 208 208 208 SER SER D . n 
D 1 209 CYS 209 209 209 CYS CYS D . n 
D 1 210 ALA 210 210 210 ALA ALA D . n 
D 1 211 SER 211 211 211 SER SER D . n 
D 1 212 GLY 212 212 212 GLY GLY D . n 
D 1 213 THR 213 213 213 THR THR D . n 
D 1 214 THR 214 214 214 THR THR D . n 
D 1 215 ALA 215 215 215 ALA ALA D . n 
D 1 216 LEU 216 216 216 LEU LEU D . n 
D 1 217 GLY 217 217 217 GLY GLY D . n 
D 1 218 TYR 218 218 218 TYR TYR D . n 
D 1 219 TYR 219 219 219 TYR TYR D . n 
D 1 220 LEU 220 220 220 LEU LEU D . n 
D 1 221 LYS 221 221 221 LYS LYS D . n 
D 1 222 LYS 222 222 222 LYS LYS D . n 
D 1 223 CYS 223 223 223 CYS CYS D . n 
D 1 224 LYS 224 224 224 LYS LYS D . n 
D 1 225 ASN 225 225 225 ASN ASN D . n 
D 1 226 LEU 226 226 226 LEU LEU D . n 
D 1 227 ASP 227 227 227 ASP ASP D . n 
D 1 228 ARG 228 228 228 ARG ARG D . n 
D 1 229 ALA 229 229 229 ALA ALA D . n 
D 1 230 LYS 230 230 230 LYS LYS D . n 
D 1 231 ILE 231 231 231 ILE ILE D . n 
D 1 232 VAL 232 232 232 VAL VAL D . n 
D 1 233 GLN 233 233 233 GLN GLN D . n 
D 1 234 PRO 234 234 234 PRO PRO D . n 
D 1 235 ASN 235 235 235 ASN ASN D . n 
D 1 236 GLY 236 236 236 GLY GLY D . n 
D 1 237 TRP 237 237 237 TRP TRP D . n 
D 1 238 LEU 238 238 238 LEU LEU D . n 
D 1 239 GLU 239 239 239 GLU GLU D . n 
D 1 240 TYR 240 240 240 TYR TYR D . n 
D 1 241 ILE 241 241 241 ILE ILE D . n 
D 1 242 ILE 242 242 242 ILE ILE D . n 
D 1 243 GLU 243 243 243 GLU GLU D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASP 245 245 245 ASP ASP D . n 
D 1 246 GLU 246 246 246 GLU GLU D . n 
D 1 247 MET 247 247 247 MET MET D . n 
D 1 248 TYR 248 248 248 TYR TYR D . n 
D 1 249 ILE 249 249 249 ILE ILE D . n 
D 1 250 ASP 250 250 250 ASP ASP D . n 
D 1 251 GLY 251 251 251 GLY GLY D . n 
D 1 252 PRO 252 252 252 PRO PRO D . n 
D 1 253 VAL 253 253 253 VAL VAL D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ILE 255 255 255 ILE ILE D . n 
D 1 256 ILE 256 256 256 ILE ILE D . n 
D 1 257 ALA 257 257 257 ALA ALA D . n 
D 1 258 GLU 258 258 258 GLU GLU D . n 
D 1 259 GLY 259 259 259 GLY GLY D . n 
D 1 260 LYS 260 260 260 LYS LYS D . n 
D 1 261 ILE 261 261 261 ILE ILE D . n 
D 1 262 TYR 262 262 262 TYR TYR D . n 
D 1 263 ILE 263 263 263 ILE ILE D . n 
D 1 264 GLY 264 264 264 GLY GLY D . n 
D 1 265 LYS 265 265 265 LYS LYS D . n 
D 1 266 HIS 266 266 ?   ?   ?   D . n 
D 1 267 HIS 267 267 ?   ?   ?   D . n 
D 1 268 HIS 268 268 ?   ?   ?   D . n 
D 1 269 HIS 269 269 ?   ?   ?   D . n 
D 1 270 HIS 270 270 ?   ?   ?   D . n 
D 1 271 HIS 271 271 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SO4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SO4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 SO4 1  301 2  SO4 SO4 A . 
F 2 SO4 1  302 8  SO4 SO4 A . 
G 2 SO4 1  301 1  SO4 SO4 B . 
H 2 SO4 1  302 7  SO4 SO4 B . 
I 2 SO4 1  301 4  SO4 SO4 C . 
J 2 SO4 1  302 6  SO4 SO4 C . 
K 2 SO4 1  301 3  SO4 SO4 D . 
L 2 SO4 1  302 5  SO4 SO4 D . 
M 3 HOH 1  401 55 HOH HOH A . 
M 3 HOH 2  402 56 HOH HOH A . 
M 3 HOH 3  403 27 HOH HOH A . 
M 3 HOH 4  404 20 HOH HOH A . 
M 3 HOH 5  405 45 HOH HOH A . 
M 3 HOH 6  406 28 HOH HOH A . 
M 3 HOH 7  407 5  HOH HOH A . 
M 3 HOH 8  408 34 HOH HOH A . 
M 3 HOH 9  409 69 HOH HOH A . 
M 3 HOH 10 410 25 HOH HOH A . 
M 3 HOH 11 411 67 HOH HOH A . 
M 3 HOH 12 412 44 HOH HOH A . 
M 3 HOH 13 413 59 HOH HOH A . 
M 3 HOH 14 414 29 HOH HOH A . 
M 3 HOH 15 415 22 HOH HOH A . 
M 3 HOH 16 416 31 HOH HOH A . 
M 3 HOH 17 417 68 HOH HOH A . 
M 3 HOH 18 418 2  HOH HOH A . 
M 3 HOH 19 419 10 HOH HOH A . 
M 3 HOH 20 420 48 HOH HOH A . 
M 3 HOH 21 421 70 HOH HOH A . 
M 3 HOH 22 422 37 HOH HOH A . 
M 3 HOH 23 423 50 HOH HOH A . 
M 3 HOH 24 424 23 HOH HOH A . 
M 3 HOH 25 425 7  HOH HOH A . 
M 3 HOH 26 426 52 HOH HOH A . 
M 3 HOH 27 427 60 HOH HOH A . 
M 3 HOH 28 428 47 HOH HOH A . 
N 3 HOH 1  401 40 HOH HOH B . 
N 3 HOH 2  402 64 HOH HOH B . 
N 3 HOH 3  403 53 HOH HOH B . 
N 3 HOH 4  404 33 HOH HOH B . 
N 3 HOH 5  405 9  HOH HOH B . 
N 3 HOH 6  406 63 HOH HOH B . 
N 3 HOH 7  407 13 HOH HOH B . 
N 3 HOH 8  408 36 HOH HOH B . 
N 3 HOH 9  409 15 HOH HOH B . 
N 3 HOH 10 410 42 HOH HOH B . 
N 3 HOH 11 411 8  HOH HOH B . 
N 3 HOH 12 412 72 HOH HOH B . 
N 3 HOH 13 413 66 HOH HOH B . 
N 3 HOH 14 414 65 HOH HOH B . 
N 3 HOH 15 415 32 HOH HOH B . 
N 3 HOH 16 416 11 HOH HOH B . 
N 3 HOH 17 417 4  HOH HOH B . 
N 3 HOH 18 418 62 HOH HOH B . 
N 3 HOH 19 419 14 HOH HOH B . 
O 3 HOH 1  401 3  HOH HOH C . 
O 3 HOH 2  402 19 HOH HOH C . 
O 3 HOH 3  403 61 HOH HOH C . 
O 3 HOH 4  404 41 HOH HOH C . 
O 3 HOH 5  405 1  HOH HOH C . 
O 3 HOH 6  406 57 HOH HOH C . 
O 3 HOH 7  407 43 HOH HOH C . 
O 3 HOH 8  408 16 HOH HOH C . 
O 3 HOH 9  409 49 HOH HOH C . 
O 3 HOH 10 410 58 HOH HOH C . 
O 3 HOH 11 411 30 HOH HOH C . 
O 3 HOH 12 412 54 HOH HOH C . 
P 3 HOH 1  401 21 HOH HOH D . 
P 3 HOH 2  402 17 HOH HOH D . 
P 3 HOH 3  403 46 HOH HOH D . 
P 3 HOH 4  404 6  HOH HOH D . 
P 3 HOH 5  405 35 HOH HOH D . 
P 3 HOH 6  406 71 HOH HOH D . 
P 3 HOH 7  407 26 HOH HOH D . 
P 3 HOH 8  408 38 HOH HOH D . 
P 3 HOH 9  409 12 HOH HOH D . 
P 3 HOH 10 410 39 HOH HOH D . 
P 3 HOH 11 411 24 HOH HOH D . 
P 3 HOH 12 412 51 HOH HOH D . 
P 3 HOH 13 413 18 HOH HOH D . 
P 3 HOH 14 414 73 HOH HOH D . 
P 3 HOH 15 415 74 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   89.98 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CR1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.144 
_cell.length_a_esd                 ? 
_cell.length_b                     149.607 
_cell.length_b_esd                 ? 
_cell.length_c                     138.232 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9CR1 
_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                   9CR1 
_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             3.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.99 
_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              7.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES sodium pH 7.5, 2% v/v Polyethylene glycol 400, 2.0 M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   7.0-8.0 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93.15 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CR1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_reflns.d_resolution_low                               37.58 
_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                                     49178 
_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                           97.35 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.28 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.069 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.049 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.50 2.65  ? ? ? ? ? ? 5042 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.448 ? ? 1 1 0.892 ? ? ? ? 0.316 ? ? ? ? ? ? ? ? ? 
2.65 2.84  ? ? ? ? ? ? 4749 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.352 ? ? 2 1 0.908 ? ? ? ? 0.249 ? ? ? ? ? ? ? ? ? 
2.84 3.06  ? ? ? ? ? ? 4057 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.257 ? ? 3 1 0.947 ? ? ? ? 0.182 ? ? ? ? ? ? ? ? ? 
3.06 3.35  ? ? ? ? ? ? 3923 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.119 ? ? 4 1 0.985 ? ? ? ? 0.084 ? ? ? ? ? ? ? ? ? 
3.35 3.74  ? ? ? ? ? ? 3624 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.084 ? ? 5 1 0.989 ? ? ? ? 0.06  ? ? ? ? ? ? ? ? ? 
3.74 4.32  ? ? ? ? ? ? 3029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.066 ? ? 6 1 0.992 ? ? ? ? 0.047 ? ? ? ? ? ? ? ? ? 
4.32 5.27  ? ? ? ? ? ? 2334 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.062 ? ? 7 1 0.989 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? ? 
5.27 7.39  ? ? ? ? ? ? 1617 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.058 ? ? 8 1 0.993 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? ? 
7.39 37.58 ? ? ? ? ? ? 953  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.048 ? ? 9 1 0.992 ? ? ? ? 0.034 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9CR1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             37.58 
_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                     49177 
_refine.ls_number_reflns_R_free                  2339 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.38 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2557 
_refine.ls_R_factor_R_free                       0.2967 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2537 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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                 41.56 
_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                            0.44 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        37.58 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               8564 
_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        8450 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 8638  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.612  ? 11611 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.167 ? 3249  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 1249  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 1488  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.50 2.55  . . 132 2573 92.00 . . . . 0.5533 . . . . . . . . . . . 0.5447 
'X-RAY DIFFRACTION' 2.55 2.61  . . 171 2753 98.00 . . . . 0.4850 . . . . . . . . . . . 0.4925 
'X-RAY DIFFRACTION' 2.61 2.67  . . 131 2775 98.00 . . . . 0.4633 . . . . . . . . . . . 0.4977 
'X-RAY DIFFRACTION' 2.67 2.74  . . 101 2814 99.00 . . . . 0.4512 . . . . . . . . . . . 0.4890 
'X-RAY DIFFRACTION' 2.74 2.81  . . 112 2779 98.00 . . . . 0.4114 . . . . . . . . . . . 0.4474 
'X-RAY DIFFRACTION' 2.81 2.89  . . 136 2780 98.00 . . . . 0.4078 . . . . . . . . . . . 0.4446 
'X-RAY DIFFRACTION' 2.89 2.99  . . 153 2772 97.00 . . . . 0.3850 . . . . . . . . . . . 0.4170 
'X-RAY DIFFRACTION' 2.99 3.09  . . 159 2489 90.00 . . . . 0.3818 . . . . . . . . . . . 0.3695 
'X-RAY DIFFRACTION' 3.09 3.22  . . 149 2708 97.00 . . . . 0.3598 . . . . . . . . . . . 0.3923 
'X-RAY DIFFRACTION' 3.22 3.36  . . 127 2836 99.00 . . . . 0.3035 . . . . . . . . . . . 0.3310 
'X-RAY DIFFRACTION' 3.36 3.54  . . 135 2797 99.00 . . . . 0.2881 . . . . . . . . . . . 0.3282 
'X-RAY DIFFRACTION' 3.54 3.76  . . 134 2846 99.00 . . . . 0.2663 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 3.76 4.05  . . 121 2803 99.00 . . . . 0.2319 . . . . . . . . . . . 0.3261 
'X-RAY DIFFRACTION' 4.05 4.46  . . 142 2814 99.00 . . . . 0.1995 . . . . . . . . . . . 0.2507 
'X-RAY DIFFRACTION' 4.46 5.10  . . 103 2840 99.00 . . . . 0.1717 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 5.10 6.42  . . 153 2639 93.00 . . . . 0.2142 . . . . . . . . . . . 0.2993 
'X-RAY DIFFRACTION' 6.43 37.58 . . 180 2820 99.00 . . . . 0.1752 . . . . . . . . . . . 0.2031 
# 
_struct.entry_id                     9CR1 
_struct.title                        'Crystal structure of histidine racemase (HisR) of Fusobacterium nucleatum (C67S)' 
_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        9CR1 
_struct_keywords.text            
;D-Histidine, racemase, stereochemistry, cofactor-independent, lanthionine, Fusobacterium nucleatum, staphylopine, CntK, Staphylococcus aureus, ISOMERASE
;
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8RI81_FUSNN 
_struct_ref.pdbx_db_accession          Q8RI81 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDRKVQVLDFIKINPAGNITILIDNFDIYDKNIPKLSEEIMKETNLYAEQVGFIKDSHLQMMGGEFCGNASRAFASLLAF
RDKDFSKQKNYNITCSGESKVLDVDVRNDGAKNKFLAKIKMPKFLSLEEINVDEYKLGLVRFSGINHFIFNIKENKETSF
ENIIDLVKKYLSNEEYSAFGIMFFDSDNLSMKPYVYVKEVGSGVYENSCASGTTALGYYLKKCKNLDRAKIVQPNGWLEY
IIENDEMYIDGPVEIIAEGKIYIGK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CR1 A 1 ? 265 ? Q8RI81 1 ? 265 ? 1 265 
2 1 9CR1 B 1 ? 265 ? Q8RI81 1 ? 265 ? 1 265 
3 1 9CR1 C 1 ? 265 ? Q8RI81 1 ? 265 ? 1 265 
4 1 9CR1 D 1 ? 265 ? Q8RI81 1 ? 265 ? 1 265 
# 
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 9CR1 SER A 67  ? UNP Q8RI81 CYS 67 'engineered mutation' 67  1  
1 9CR1 HIS A 266 ? UNP Q8RI81 ?   ?  'expression tag'      266 2  
1 9CR1 HIS A 267 ? UNP Q8RI81 ?   ?  'expression tag'      267 3  
1 9CR1 HIS A 268 ? UNP Q8RI81 ?   ?  'expression tag'      268 4  
1 9CR1 HIS A 269 ? UNP Q8RI81 ?   ?  'expression tag'      269 5  
1 9CR1 HIS A 270 ? UNP Q8RI81 ?   ?  'expression tag'      270 6  
1 9CR1 HIS A 271 ? UNP Q8RI81 ?   ?  'expression tag'      271 7  
2 9CR1 SER B 67  ? UNP Q8RI81 CYS 67 'engineered mutation' 67  8  
2 9CR1 HIS B 266 ? UNP Q8RI81 ?   ?  'expression tag'      266 9  
2 9CR1 HIS B 267 ? UNP Q8RI81 ?   ?  'expression tag'      267 10 
2 9CR1 HIS B 268 ? UNP Q8RI81 ?   ?  'expression tag'      268 11 
2 9CR1 HIS B 269 ? UNP Q8RI81 ?   ?  'expression tag'      269 12 
2 9CR1 HIS B 270 ? UNP Q8RI81 ?   ?  'expression tag'      270 13 
2 9CR1 HIS B 271 ? UNP Q8RI81 ?   ?  'expression tag'      271 14 
3 9CR1 SER C 67  ? UNP Q8RI81 CYS 67 'engineered mutation' 67  15 
3 9CR1 HIS C 266 ? UNP Q8RI81 ?   ?  'expression tag'      266 16 
3 9CR1 HIS C 267 ? UNP Q8RI81 ?   ?  'expression tag'      267 17 
3 9CR1 HIS C 268 ? UNP Q8RI81 ?   ?  'expression tag'      268 18 
3 9CR1 HIS C 269 ? UNP Q8RI81 ?   ?  'expression tag'      269 19 
3 9CR1 HIS C 270 ? UNP Q8RI81 ?   ?  'expression tag'      270 20 
3 9CR1 HIS C 271 ? UNP Q8RI81 ?   ?  'expression tag'      271 21 
4 9CR1 SER D 67  ? UNP Q8RI81 CYS 67 'engineered mutation' 67  22 
4 9CR1 HIS D 266 ? UNP Q8RI81 ?   ?  'expression tag'      266 23 
4 9CR1 HIS D 267 ? UNP Q8RI81 ?   ?  'expression tag'      267 24 
4 9CR1 HIS D 268 ? UNP Q8RI81 ?   ?  'expression tag'      268 25 
4 9CR1 HIS D 269 ? UNP Q8RI81 ?   ?  'expression tag'      269 26 
4 9CR1 HIS D 270 ? UNP Q8RI81 ?   ?  'expression tag'      270 27 
4 9CR1 HIS D 271 ? UNP Q8RI81 ?   ?  'expression tag'      271 28 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 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)' 3160  ? 
1 MORE         -72   ? 
1 'SSA (A^2)'  23650 ? 
2 'ABSA (A^2)' 3270  ? 
2 MORE         -71   ? 
2 'SSA (A^2)'  23600 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,I,J,M,O 
2 1 B,D,G,H,K,L,N,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 32  ? LYS A 42  ? ASN A 32  LYS A 42  1 ? 11 
HELX_P HELX_P2  AA2 SER A 67  ? ARG A 81  ? SER A 67  ARG A 81  1 ? 15 
HELX_P HELX_P3  AA3 SER A 159 ? LEU A 171 ? SER A 159 LEU A 171 1 ? 13 
HELX_P HELX_P4  AA4 SER A 172 ? GLU A 174 ? SER A 172 GLU A 174 5 ? 3  
HELX_P HELX_P5  AA5 CYS A 209 ? ASN A 225 ? CYS A 209 ASN A 225 1 ? 17 
HELX_P HELX_P6  AA6 ASN B 32  ? LYS B 42  ? ASN B 32  LYS B 42  1 ? 11 
HELX_P HELX_P7  AA7 SER B 67  ? ARG B 81  ? SER B 67  ARG B 81  1 ? 15 
HELX_P HELX_P8  AA8 SER B 159 ? LEU B 171 ? SER B 159 LEU B 171 1 ? 13 
HELX_P HELX_P9  AA9 SER B 172 ? GLU B 174 ? SER B 172 GLU B 174 5 ? 3  
HELX_P HELX_P10 AB1 CYS B 209 ? ASN B 225 ? CYS B 209 ASN B 225 1 ? 17 
HELX_P HELX_P11 AB2 ASN C 32  ? LYS C 42  ? ASN C 32  LYS C 42  1 ? 11 
HELX_P HELX_P12 AB3 SER C 67  ? ASP C 82  ? SER C 67  ASP C 82  1 ? 16 
HELX_P HELX_P13 AB4 SER C 159 ? LEU C 171 ? SER C 159 LEU C 171 1 ? 13 
HELX_P HELX_P14 AB5 SER C 172 ? GLU C 174 ? SER C 172 GLU C 174 5 ? 3  
HELX_P HELX_P15 AB6 CYS C 209 ? LYS C 224 ? CYS C 209 LYS C 224 1 ? 16 
HELX_P HELX_P16 AB7 ASN D 32  ? LYS D 42  ? ASN D 32  LYS D 42  1 ? 11 
HELX_P HELX_P17 AB8 SER D 67  ? ARG D 81  ? SER D 67  ARG D 81  1 ? 15 
HELX_P HELX_P18 AB9 SER D 159 ? LEU D 171 ? SER D 159 LEU D 171 1 ? 13 
HELX_P HELX_P19 AC1 CYS D 209 ? LYS D 224 ? CYS D 209 LYS D 224 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 21 ? 
AA2 ? 5  ? 
AA3 ? 21 ? 
AA4 ? 6  ? 
AA5 ? 6  ? 
AA6 ? 6  ? 
AA7 ? 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  ? anti-parallel 
AA1 1  10 ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? anti-parallel 
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  10 ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 21 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 11 21 ? anti-parallel 
AA1 12 13 ? parallel      
AA1 13 14 ? anti-parallel 
AA1 14 15 ? parallel      
AA1 15 16 ? anti-parallel 
AA1 16 17 ? anti-parallel 
AA1 17 20 ? anti-parallel 
AA1 17 21 ? anti-parallel 
AA1 18 19 ? anti-parallel 
AA1 19 20 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? parallel      
AA2 4  5  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 1  10 ? anti-parallel 
AA3 2  3  ? parallel      
AA3 3  4  ? anti-parallel 
AA3 4  5  ? parallel      
AA3 5  6  ? anti-parallel 
AA3 6  7  ? anti-parallel 
AA3 7  10 ? anti-parallel 
AA3 8  9  ? anti-parallel 
AA3 9  10 ? anti-parallel 
AA3 10 21 ? anti-parallel 
AA3 11 12 ? anti-parallel 
AA3 11 21 ? anti-parallel 
AA3 12 13 ? parallel      
AA3 13 14 ? anti-parallel 
AA3 14 15 ? parallel      
AA3 15 16 ? anti-parallel 
AA3 16 17 ? anti-parallel 
AA3 17 20 ? anti-parallel 
AA3 17 21 ? anti-parallel 
AA3 18 19 ? anti-parallel 
AA3 19 20 ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? parallel      
AA4 4  5  ? anti-parallel 
AA4 5  6  ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA5 2  3  ? anti-parallel 
AA5 3  4  ? parallel      
AA5 4  5  ? anti-parallel 
AA5 5  6  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? parallel      
AA6 4  5  ? anti-parallel 
AA6 5  6  ? anti-parallel 
AA7 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  VAL A 5   ? PRO A 15  ? VAL A 5   PRO A 15  
AA1 2  THR A 20  ? ASP A 24  ? THR A 20  ASP A 24  
AA1 3  GLN A 50  ? LYS A 55  ? GLN A 50  LYS A 55  
AA1 4  HIS A 58  ? MET A 61  ? HIS A 58  MET A 61  
AA1 5  GLN A 88  ? CYS A 95  ? GLN A 88  CYS A 95  
AA1 6  LEU A 102 ? ASN A 108 ? LEU A 102 ASN A 108 
AA1 7  LYS A 114 ? MET A 121 ? LYS A 114 MET A 121 
AA1 8  ARG A 228 ? GLN A 233 ? ARG A 228 GLN A 233 
AA1 9  GLY A 236 ? ILE A 242 ? GLY A 236 ILE A 242 
AA1 10 MET A 247 ? GLY A 264 ? MET A 247 GLY A 264 
AA1 11 LYS C 4   ? PRO C 15  ? LYS C 4   PRO C 15  
AA1 12 THR C 20  ? ASP C 24  ? THR C 20  ASP C 24  
AA1 13 GLN C 50  ? LYS C 55  ? GLN C 50  LYS C 55  
AA1 14 HIS C 58  ? MET C 61  ? HIS C 58  MET C 61  
AA1 15 GLN C 88  ? CYS C 95  ? GLN C 88  CYS C 95  
AA1 16 LEU C 102 ? ASN C 108 ? LEU C 102 ASN C 108 
AA1 17 LYS C 114 ? LYS C 120 ? LYS C 114 LYS C 120 
AA1 18 ARG C 228 ? GLN C 233 ? ARG C 228 GLN C 233 
AA1 19 GLY C 236 ? GLU C 243 ? GLY C 236 GLU C 243 
AA1 20 GLU C 246 ? ASP C 250 ? GLU C 246 ASP C 250 
AA1 21 PRO C 252 ? LYS C 265 ? PRO C 252 LYS C 265 
AA2 1  SER A 126 ? VAL A 132 ? SER A 126 VAL A 132 
AA2 2  TYR A 135 ? ARG A 141 ? TYR A 135 ARG A 141 
AA2 3  ILE A 145 ? ASN A 151 ? ILE A 145 ASN A 151 
AA2 4  ALA A 178 ? ASP A 185 ? ALA A 178 ASP A 185 
AA2 5  SER A 190 ? VAL A 197 ? SER A 190 VAL A 197 
AA3 1  VAL B 5   ? PRO B 15  ? VAL B 5   PRO B 15  
AA3 2  THR B 20  ? ASP B 24  ? THR B 20  ASP B 24  
AA3 3  GLN B 50  ? LYS B 55  ? GLN B 50  LYS B 55  
AA3 4  HIS B 58  ? MET B 61  ? HIS B 58  MET B 61  
AA3 5  GLN B 88  ? CYS B 95  ? GLN B 88  CYS B 95  
AA3 6  LEU B 102 ? ASN B 108 ? LEU B 102 ASN B 108 
AA3 7  LYS B 114 ? LYS B 120 ? LYS B 114 LYS B 120 
AA3 8  ARG B 228 ? GLN B 233 ? ARG B 228 GLN B 233 
AA3 9  GLY B 236 ? ILE B 242 ? GLY B 236 ILE B 242 
AA3 10 MET B 247 ? GLY B 264 ? MET B 247 GLY B 264 
AA3 11 VAL D 5   ? PRO D 15  ? VAL D 5   PRO D 15  
AA3 12 THR D 20  ? ASP D 24  ? THR D 20  ASP D 24  
AA3 13 GLN D 50  ? LYS D 55  ? GLN D 50  LYS D 55  
AA3 14 HIS D 58  ? MET D 61  ? HIS D 58  MET D 61  
AA3 15 GLN D 88  ? CYS D 95  ? GLN D 88  CYS D 95  
AA3 16 GLU D 98  ? ASN D 108 ? GLU D 98  ASN D 108 
AA3 17 LYS D 114 ? LYS D 120 ? LYS D 114 LYS D 120 
AA3 18 ARG D 228 ? GLN D 233 ? ARG D 228 GLN D 233 
AA3 19 GLY D 236 ? ILE D 242 ? GLY D 236 ILE D 242 
AA3 20 MET D 247 ? ASP D 250 ? MET D 247 ASP D 250 
AA3 21 PRO D 252 ? GLY D 264 ? PRO D 252 GLY D 264 
AA4 1  SER B 126 ? VAL B 132 ? SER B 126 VAL B 132 
AA4 2  TYR B 135 ? ARG B 141 ? TYR B 135 ARG B 141 
AA4 3  ILE B 145 ? ASN B 151 ? ILE B 145 ASN B 151 
AA4 4  ALA B 178 ? ASP B 185 ? ALA B 178 ASP B 185 
AA4 5  SER B 190 ? VAL B 197 ? SER B 190 VAL B 197 
AA4 6  SER B 202 ? TYR B 205 ? SER B 202 TYR B 205 
AA5 1  SER C 126 ? VAL C 132 ? SER C 126 VAL C 132 
AA5 2  TYR C 135 ? ARG C 141 ? TYR C 135 ARG C 141 
AA5 3  ASN C 146 ? ASN C 151 ? ASN C 146 ASN C 151 
AA5 4  ALA C 178 ? ASP C 185 ? ALA C 178 ASP C 185 
AA5 5  SER C 190 ? VAL C 197 ? SER C 190 VAL C 197 
AA5 6  SER C 202 ? TYR C 205 ? SER C 202 TYR C 205 
AA6 1  SER D 126 ? GLU D 128 ? SER D 126 GLU D 128 
AA6 2  GLY D 138 ? ARG D 141 ? GLY D 138 ARG D 141 
AA6 3  ASN D 146 ? ASN D 151 ? ASN D 146 ASN D 151 
AA6 4  ALA D 178 ? ASP D 185 ? ALA D 178 ASP D 185 
AA6 5  SER D 190 ? VAL D 197 ? SER D 190 VAL D 197 
AA6 6  SER D 202 ? TYR D 205 ? SER D 202 TYR D 205 
AA7 1  ASN D 131 ? VAL D 132 ? ASN D 131 VAL D 132 
AA7 2  TYR D 135 ? LYS D 136 ? TYR D 135 LYS D 136 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N ILE A 13  ? N ILE A 13  O THR A 20  ? O THR A 20  
AA1 1  10 N ASN A 14  ? N ASN A 14  O GLU A 254 ? O GLU A 254 
AA1 2  3  N ILE A 23  ? N ILE A 23  O GLY A 52  ? O GLY A 52  
AA1 3  4  N LYS A 55  ? N LYS A 55  O HIS A 58  ? O HIS A 58  
AA1 4  5  N LEU A 59  ? N LEU A 59  O THR A 94  ? O THR A 94  
AA1 5  6  N ILE A 93  ? N ILE A 93  O LEU A 102 ? O LEU A 102 
AA1 6  7  N ARG A 107 ? N ARG A 107 O LEU A 116 ? O LEU A 116 
AA1 7  10 N MET A 121 ? N MET A 121 O MET A 247 ? O MET A 247 
AA1 8  9  N GLN A 233 ? N GLN A 233 O GLY A 236 ? O GLY A 236 
AA1 9  10 N ILE A 241 ? N ILE A 241 O TYR A 248 ? O TYR A 248 
AA1 10 21 N GLU A 258 ? N GLU A 258 O LYS C 260 ? O LYS C 260 
AA1 11 12 N ILE C 13  ? N ILE C 13  O THR C 20  ? O THR C 20  
AA1 11 21 N LYS C 12  ? N LYS C 12  O ALA C 257 ? O ALA C 257 
AA1 12 13 N ILE C 21  ? N ILE C 21  O GLY C 52  ? O GLY C 52  
AA1 13 14 N PHE C 53  ? N PHE C 53  O GLN C 60  ? O GLN C 60  
AA1 14 15 N LEU C 59  ? N LEU C 59  O THR C 94  ? O THR C 94  
AA1 15 16 N TYR C 91  ? N TYR C 91  O VAL C 104 ? O VAL C 104 
AA1 16 17 N ARG C 107 ? N ARG C 107 O LEU C 116 ? O LEU C 116 
AA1 17 20 N ILE C 119 ? N ILE C 119 O ILE C 249 ? O ILE C 249 
AA1 17 21 N PHE C 115 ? N PHE C 115 O VAL C 253 ? O VAL C 253 
AA1 18 19 N ILE C 231 ? N ILE C 231 O LEU C 238 ? O LEU C 238 
AA1 19 20 N GLU C 239 ? N GLU C 239 O ASP C 250 ? O ASP C 250 
AA2 1  2  N ILE A 130 ? N ILE A 130 O LEU A 137 ? O LEU A 137 
AA2 2  3  N GLY A 138 ? N GLY A 138 O ILE A 149 ? O ILE A 149 
AA2 3  4  N PHE A 148 ? N PHE A 148 O GLY A 180 ? O GLY A 180 
AA2 4  5  N PHE A 183 ? N PHE A 183 O LYS A 192 ? O LYS A 192 
AA3 1  2  N ILE B 11  ? N ILE B 11  O LEU B 22  ? O LEU B 22  
AA3 1  10 N ASN B 14  ? N ASN B 14  O GLU B 254 ? O GLU B 254 
AA3 2  3  N ILE B 23  ? N ILE B 23  O GLY B 52  ? O GLY B 52  
AA3 3  4  N LYS B 55  ? N LYS B 55  O HIS B 58  ? O HIS B 58  
AA3 4  5  N LEU B 59  ? N LEU B 59  O THR B 94  ? O THR B 94  
AA3 5  6  N TYR B 91  ? N TYR B 91  O VAL B 104 ? O VAL B 104 
AA3 6  7  N ARG B 107 ? N ARG B 107 O LEU B 116 ? O LEU B 116 
AA3 7  10 N PHE B 115 ? N PHE B 115 O VAL B 253 ? O VAL B 253 
AA3 8  9  N ILE B 231 ? N ILE B 231 O LEU B 238 ? O LEU B 238 
AA3 9  10 N ILE B 241 ? N ILE B 241 O TYR B 248 ? O TYR B 248 
AA3 10 21 N GLU B 258 ? N GLU B 258 O LYS D 260 ? O LYS D 260 
AA3 11 12 N ILE D 11  ? N ILE D 11  O LEU D 22  ? O LEU D 22  
AA3 11 21 N GLN D 6   ? N GLN D 6   O ILE D 263 ? O ILE D 263 
AA3 12 13 N ILE D 23  ? N ILE D 23  O GLY D 52  ? O GLY D 52  
AA3 13 14 N PHE D 53  ? N PHE D 53  O GLN D 60  ? O GLN D 60  
AA3 14 15 N LEU D 59  ? N LEU D 59  O THR D 94  ? O THR D 94  
AA3 15 16 N ILE D 93  ? N ILE D 93  O LEU D 102 ? O LEU D 102 
AA3 16 17 N ARG D 107 ? N ARG D 107 O LEU D 116 ? O LEU D 116 
AA3 17 20 N ILE D 119 ? N ILE D 119 O ILE D 249 ? O ILE D 249 
AA3 17 21 N PHE D 115 ? N PHE D 115 O VAL D 253 ? O VAL D 253 
AA3 18 19 N ILE D 231 ? N ILE D 231 O LEU D 238 ? O LEU D 238 
AA3 19 20 N GLU D 239 ? N GLU D 239 O ASP D 250 ? O ASP D 250 
AA4 1  2  N ILE B 130 ? N ILE B 130 O LEU B 137 ? O LEU B 137 
AA4 2  3  N GLY B 138 ? N GLY B 138 O ILE B 149 ? O ILE B 149 
AA4 3  4  N PHE B 148 ? N PHE B 148 O MET B 182 ? O MET B 182 
AA4 4  5  N PHE B 183 ? N PHE B 183 O LYS B 192 ? O LYS B 192 
AA4 5  6  N VAL B 195 ? N VAL B 195 O VAL B 204 ? O VAL B 204 
AA5 1  2  N ILE C 130 ? N ILE C 130 O LEU C 137 ? O LEU C 137 
AA5 2  3  N VAL C 140 ? N VAL C 140 O HIS C 147 ? O HIS C 147 
AA5 3  4  N PHE C 150 ? N PHE C 150 O PHE C 184 ? O PHE C 184 
AA5 4  5  N ILE C 181 ? N ILE C 181 O TYR C 194 ? O TYR C 194 
AA5 5  6  N VAL C 195 ? N VAL C 195 O VAL C 204 ? O VAL C 204 
AA6 1  2  N GLU D 128 ? N GLU D 128 O LEU D 139 ? O LEU D 139 
AA6 2  3  N GLY D 138 ? N GLY D 138 O ILE D 149 ? O ILE D 149 
AA6 3  4  N PHE D 148 ? N PHE D 148 O MET D 182 ? O MET D 182 
AA6 4  5  N ILE D 181 ? N ILE D 181 O TYR D 194 ? O TYR D 194 
AA6 5  6  N VAL D 195 ? N VAL D 195 O VAL D 204 ? O VAL D 204 
AA7 1  2  N VAL D 132 ? N VAL D 132 O TYR D 135 ? O TYR D 135 
# 
_pdbx_entry_details.entry_id                   9CR1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 HA   A LYS 120 ? ? O  A HOH 404 ? ? 1.13 
2  1 HE   D ARG 72  ? ? O  D HOH 401 ? ? 1.16 
3  1 H    C SER 186 ? ? O  C HOH 403 ? ? 1.23 
4  1 HB3  B ASP 109 ? ? O  B HOH 402 ? ? 1.24 
5  1 HG12 A ILE 255 ? ? O  A HOH 406 ? ? 1.25 
6  1 HA2  A GLY 217 ? ? O  A HOH 402 ? ? 1.25 
7  1 HG11 D VAL 51  ? ? O  D HOH 403 ? ? 1.42 
8  1 HH21 D ARG 72  ? ? O  D HOH 401 ? ? 1.43 
9  1 HG2  A MET 41  ? ? O  A HOH 407 ? ? 1.45 
10 1 HA   D SER 37  ? ? O  D HOH 403 ? ? 1.45 
11 1 HB2  D ASN 69  ? ? O  D HOH 406 ? ? 1.45 
12 1 H    D VAL 51  ? ? O  D HOH 404 ? ? 1.46 
13 1 HA   A LYS 260 ? ? O  A HOH 403 ? ? 1.51 
14 1 H    D ILE 145 ? ? O  D HOH 402 ? ? 1.56 
15 1 HZ2  B LYS 120 ? ? O  B HOH 404 ? ? 1.56 
16 1 HD21 B ASN 235 ? ? O  B HOH 403 ? ? 1.57 
17 1 H    C SER 86  ? ? O  C HOH 407 ? ? 1.57 
18 1 H    A PHE 148 ? ? O  A GLY 180 ? ? 1.59 
19 1 O    A PRO 252 ? ? O  A HOH 401 ? ? 1.80 
20 1 NE   D ARG 72  ? ? O  D HOH 401 ? ? 1.80 
21 1 O    A GLY 217 ? ? O  A HOH 402 ? ? 1.81 
22 1 O    A LEU 8   ? ? O  A HOH 403 ? ? 1.81 
23 1 O    A MET 247 ? ? O  A HOH 404 ? ? 1.82 
24 1 N    D ILE 145 ? ? O  D HOH 402 ? ? 1.84 
25 1 N    B PHE 183 ? ? O  B HOH 401 ? ? 1.84 
26 1 O    B LYS 114 ? ? O  B HOH 402 ? ? 1.85 
27 1 ND2  B ASN 207 ? ? O  B HOH 403 ? ? 1.85 
28 1 NZ   B LYS 120 ? ? O  B HOH 404 ? ? 1.85 
29 1 OD1  C ASN 69  ? ? O  C HOH 401 ? ? 1.86 
30 1 CB   B ASP 109 ? ? O  B HOH 402 ? ? 1.87 
31 1 OE2  A GLU 129 ? ? O  A HOH 405 ? ? 1.87 
32 1 O    A ASN 113 ? ? O  A HOH 406 ? ? 1.88 
33 1 CA   A LYS 120 ? ? O  A HOH 404 ? ? 1.88 
34 1 O    B PRO 252 ? ? O  B HOH 405 ? ? 1.89 
35 1 N    A PRO 252 ? ? O  A HOH 401 ? ? 1.89 
36 1 OE1  B GLU 129 ? ? O  B HOH 406 ? ? 1.90 
37 1 O3   C SO4 301 ? ? O  C HOH 401 ? ? 1.90 
38 1 O    A ALA 48  ? ? O  A HOH 407 ? ? 1.90 
39 1 C    B LYS 114 ? ? O  B HOH 402 ? ? 1.91 
40 1 SG   B CYS 223 ? ? O  B HOH 417 ? ? 1.91 
41 1 O    C GLY 64  ? ? O  C HOH 402 ? ? 1.92 
42 1 CA   A GLY 217 ? ? O  A HOH 402 ? ? 1.92 
43 1 O    A GLY 259 ? ? O  A HOH 403 ? ? 1.93 
44 1 CG   B ASN 207 ? ? O  B HOH 403 ? ? 1.93 
45 1 N    C SER 186 ? ? O  C HOH 403 ? ? 1.93 
46 1 CG1  A ILE 255 ? ? O  A HOH 406 ? ? 1.94 
47 1 OD1  A ASN 235 ? ? O  A HOH 408 ? ? 1.94 
48 1 O    A HOH 419 ? ? O  A HOH 425 ? ? 1.94 
49 1 OE2  B GLU 98  ? ? O  B HOH 404 ? ? 1.96 
50 1 OD2  B ASP 27  ? ? O  B HOH 407 ? ? 1.96 
51 1 OG   D SER 37  ? ? O  D HOH 403 ? ? 1.97 
52 1 NH2  D ARG 72  ? ? O  D HOH 401 ? ? 1.97 
53 1 O    C ASN 207 ? ? O  C HOH 404 ? ? 1.97 
54 1 C    C GLY 64  ? ? O  C HOH 402 ? ? 1.98 
55 1 NE1  A TRP 237 ? ? O  A HOH 409 ? ? 1.98 
56 1 OD2  A ASP 27  ? ? O  A HOH 410 ? ? 1.99 
57 1 OD2  A ASP 105 ? ? O  A HOH 411 ? ? 2.02 
58 1 N    A GLY 97  ? ? O  A HOH 412 ? ? 2.02 
59 1 O    A HIS 147 ? ? O  A HOH 413 ? ? 2.03 
60 1 N    B PRO 252 ? ? O  B HOH 405 ? ? 2.05 
61 1 CA   D GLY 144 ? ? O  D HOH 402 ? ? 2.06 
62 1 O    D ILE 40  ? ? O  D LEU 46  ? ? 2.06 
63 1 N    D VAL 51  ? ? O  D HOH 404 ? ? 2.07 
64 1 CE2  A TRP 237 ? ? O  A HOH 409 ? ? 2.07 
65 1 C    A HIS 147 ? ? O  A HOH 413 ? ? 2.07 
66 1 OD1  B ASN 207 ? ? O  B HOH 403 ? ? 2.08 
67 1 N    A GLU 206 ? ? O  A HOH 414 ? ? 2.08 
68 1 ND2  B ASN 235 ? ? O  B HOH 403 ? ? 2.08 
69 1 O    A GLY 97  ? ? O  A HOH 415 ? ? 2.09 
70 1 C    A GLY 217 ? ? O  A HOH 402 ? ? 2.10 
71 1 C    D GLY 144 ? ? O  D HOH 402 ? ? 2.10 
72 1 C    C ASN 235 ? ? O  C HOH 404 ? ? 2.10 
73 1 O    C ASN 235 ? ? O  C HOH 404 ? ? 2.10 
74 1 N    D GLY 201 ? ? O  D HOH 405 ? ? 2.11 
75 1 O    C ILE 23  ? ? O  C HOH 405 ? ? 2.11 
76 1 C    D VAL 200 ? ? O  D HOH 405 ? ? 2.11 
77 1 O4   C SO4 302 ? ? O  C HOH 406 ? ? 2.11 
78 1 CA   D SER 37  ? ? O  D HOH 403 ? ? 2.11 
79 1 N    C GLU 65  ? ? O  C HOH 402 ? ? 2.12 
80 1 OH   B TYR 194 ? ? O1 B SO4 302 ? ? 2.13 
81 1 O    A ALA 79  ? ? O  A HOH 416 ? ? 2.13 
82 1 N    B ASP 109 ? ? O  B HOH 402 ? ? 2.13 
83 1 CG   A MET 41  ? ? O  A HOH 407 ? ? 2.14 
84 1 O    D ALA 16  ? ? OG D SER 208 ? ? 2.14 
85 1 O1   D SO4 301 ? ? O  D HOH 406 ? ? 2.14 
86 1 C    B MET 182 ? ? O  B HOH 401 ? ? 2.15 
87 1 CA   D GLN 50  ? ? O  D HOH 404 ? ? 2.15 
88 1 N    A PHE 148 ? ? O  A HOH 413 ? ? 2.15 
89 1 CD   A PRO 252 ? ? O  A HOH 401 ? ? 2.16 
90 1 NH1  B ARG 141 ? ? O  B HOH 408 ? ? 2.16 
91 1 CG1  D VAL 51  ? ? O  D HOH 403 ? ? 2.17 
92 1 CD   A GLU 129 ? ? O  A HOH 405 ? ? 2.17 
93 1 CZ   D ARG 72  ? ? O  D HOH 401 ? ? 2.17 
94 1 CE   A MET 41  ? ? O  A HOH 407 ? ? 2.17 
95 1 O    A PRO 193 ? ? O  A HOH 414 ? ? 2.17 
96 1 CA   A PHE 148 ? ? O  A HOH 413 ? ? 2.18 
97 1 OE2  A GLU 154 ? ? O  A HOH 417 ? ? 2.19 
98 1 CA   B ASP 109 ? ? O  B HOH 402 ? ? 2.19 
# 
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 ASP A 27  ? ? -57.41  105.92  
2  1 ASN A 45  ? ? -137.05 -155.11 
3  1 ALA A 48  ? ? -175.07 142.49  
4  1 ASP A 56  ? ? 49.84   -122.38 
5  1 SER A 86  ? ? -113.25 -93.93  
6  1 PRO A 122 ? ? -48.62  156.15  
7  1 ASP A 133 ? ? 55.27   -119.07 
8  1 ASN A 173 ? ? -101.02 47.06   
9  1 SER A 208 ? ? -170.21 148.68  
10 1 ASP B 27  ? ? -54.93  107.43  
11 1 ASN B 45  ? ? -105.74 -161.97 
12 1 ASP B 56  ? ? 52.79   -128.70 
13 1 SER B 86  ? ? -106.64 -75.60  
14 1 LYS B 87  ? ? -121.93 -61.66  
15 1 SER B 126 ? ? -171.05 142.19  
16 1 ASP B 133 ? ? 44.66   -125.90 
17 1 LYS B 224 ? ? -151.65 -0.97   
18 1 ILE B 256 ? ? -96.22  -63.23  
19 1 ASN C 45  ? ? -120.81 -162.16 
20 1 ASP C 56  ? ? 58.97   -119.01 
21 1 SER C 86  ? ? -103.47 -80.99  
22 1 ASP C 133 ? ? 34.58   -105.39 
23 1 ASN C 225 ? ? 70.26   36.23   
24 1 ASP D 56  ? ? 59.94   -118.25 
25 1 SER D 86  ? ? -119.49 -81.31  
26 1 LYS D 89  ? ? -170.79 136.57  
27 1 ASP D 133 ? ? 50.55   -117.29 
28 1 LEU D 171 ? ? -68.17  2.56    
29 1 ALA D 229 ? ? -173.13 142.09  
30 1 ILE D 256 ? ? -90.80  -60.56  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ASP 2   ? A ASP 2   
3  1 Y 1 A HIS 266 ? A HIS 266 
4  1 Y 1 A HIS 267 ? A HIS 267 
5  1 Y 1 A HIS 268 ? A HIS 268 
6  1 Y 1 A HIS 269 ? A HIS 269 
7  1 Y 1 A HIS 270 ? A HIS 270 
8  1 Y 1 A HIS 271 ? A HIS 271 
9  1 Y 1 B MET 1   ? B MET 1   
10 1 Y 1 B ASP 2   ? B ASP 2   
11 1 Y 1 B HIS 266 ? B HIS 266 
12 1 Y 1 B HIS 267 ? B HIS 267 
13 1 Y 1 B HIS 268 ? B HIS 268 
14 1 Y 1 B HIS 269 ? B HIS 269 
15 1 Y 1 B HIS 270 ? B HIS 270 
16 1 Y 1 B HIS 271 ? B HIS 271 
17 1 Y 1 C MET 1   ? C MET 1   
18 1 Y 1 C HIS 266 ? C HIS 266 
19 1 Y 1 C HIS 267 ? C HIS 267 
20 1 Y 1 C HIS 268 ? C HIS 268 
21 1 Y 1 C HIS 269 ? C HIS 269 
22 1 Y 1 C HIS 270 ? C HIS 270 
23 1 Y 1 C HIS 271 ? C HIS 271 
24 1 Y 1 D MET 1   ? D MET 1   
25 1 Y 1 D ASP 2   ? D ASP 2   
26 1 Y 1 D HIS 266 ? D HIS 266 
27 1 Y 1 D HIS 267 ? D HIS 267 
28 1 Y 1 D HIS 268 ? D HIS 268 
29 1 Y 1 D HIS 269 ? D HIS 269 
30 1 Y 1 D HIS 270 ? D HIS 270 
31 1 Y 1 D HIS 271 ? D HIS 271 
# 
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 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Canadian Institutes of Health Research (CIHR)'                     Canada ? 1 
'Natural Sciences and Engineering Research Council (NSERC, Canada)' Canada ? 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-Q8RI81-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CR1 
_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]   0.013861 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   -0.000005 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006684 
_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]   0.007234 
_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 
H 
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    . ARG A 1 3   ? -9.120  4.027   35.860  1.00 122.92 ? 3   ARG A N    1 
ATOM   2     C CA   . ARG A 1 3   ? -9.063  4.331   37.287  1.00 126.92 ? 3   ARG A CA   1 
ATOM   3     C C    . ARG A 1 3   ? -8.121  5.505   37.557  1.00 124.95 ? 3   ARG A C    1 
ATOM   4     O O    . ARG A 1 3   ? -7.449  5.999   36.648  1.00 126.30 ? 3   ARG A O    1 
ATOM   5     C CB   . ARG A 1 3   ? -8.614  3.104   38.080  1.00 127.39 ? 3   ARG A CB   1 
ATOM   6     C CG   . ARG A 1 3   ? -9.700  2.050   38.283  1.00 130.09 ? 3   ARG A CG   1 
ATOM   7     C CD   . ARG A 1 3   ? -10.948 2.622   38.960  1.00 134.75 ? 3   ARG A CD   1 
ATOM   8     N NE   . ARG A 1 3   ? -10.631 3.667   39.928  1.00 137.37 ? 3   ARG A NE   1 
ATOM   9     C CZ   . ARG A 1 3   ? -10.802 3.560   41.240  1.00 135.41 ? 3   ARG A CZ   1 
ATOM   10    N NH1  . ARG A 1 3   ? -11.287 2.457   41.789  1.00 135.40 ? 3   ARG A NH1  1 
ATOM   11    N NH2  . ARG A 1 3   ? -10.479 4.587   42.021  1.00 131.98 ? 3   ARG A NH2  1 
ATOM   12    H H    . ARG A 1 3   ? -8.411  3.650   35.553  1.00 147.51 ? 3   ARG A H    1 
ATOM   13    H HA   . ARG A 1 3   ? -9.949  4.577   37.594  1.00 152.30 ? 3   ARG A HA   1 
ATOM   14    H HB2  . ARG A 1 3   ? -7.880  2.681   37.607  1.00 152.87 ? 3   ARG A HB2  1 
ATOM   15    H HB3  . ARG A 1 3   ? -8.320  3.394   38.958  1.00 152.87 ? 3   ARG A HB3  1 
ATOM   16    H HG2  . ARG A 1 3   ? -9.962  1.694   37.420  1.00 156.11 ? 3   ARG A HG2  1 
ATOM   17    H HG3  . ARG A 1 3   ? -9.353  1.339   38.844  1.00 156.11 ? 3   ARG A HG3  1 
ATOM   18    H HD2  . ARG A 1 3   ? -11.528 3.006   38.283  1.00 161.70 ? 3   ARG A HD2  1 
ATOM   19    H HD3  . ARG A 1 3   ? -11.410 1.909   39.428  1.00 161.70 ? 3   ARG A HD3  1 
ATOM   20    H HE   . ARG A 1 3   ? -10.311 4.406   39.627  1.00 164.84 ? 3   ARG A HE   1 
ATOM   21    H HH11 . ARG A 1 3   ? -11.500 1.788   41.292  1.00 162.48 ? 3   ARG A HH11 1 
ATOM   22    H HH12 . ARG A 1 3   ? -11.389 2.410   42.641  1.00 162.48 ? 3   ARG A HH12 1 
ATOM   23    H HH21 . ARG A 1 3   ? -10.165 5.309   41.675  1.00 158.38 ? 3   ARG A HH21 1 
ATOM   24    H HH22 . ARG A 1 3   ? -10.585 4.530   42.873  1.00 158.38 ? 3   ARG A HH22 1 
ATOM   25    N N    . LYS A 1 4   ? -8.079  5.947   38.812  1.00 122.84 ? 4   LYS A N    1 
ATOM   26    C CA   . LYS A 1 4   ? -7.269  7.091   39.200  1.00 120.35 ? 4   LYS A CA   1 
ATOM   27    C C    . LYS A 1 4   ? -5.858  6.635   39.553  1.00 116.80 ? 4   LYS A C    1 
ATOM   28    O O    . LYS A 1 4   ? -5.679  5.691   40.330  1.00 117.11 ? 4   LYS A O    1 
ATOM   29    C CB   . LYS A 1 4   ? -7.881  7.824   40.397  1.00 122.44 ? 4   LYS A CB   1 
ATOM   30    C CG   . LYS A 1 4   ? -9.395  7.758   40.496  1.00 124.38 ? 4   LYS A CG   1 
ATOM   31    C CD   . LYS A 1 4   ? -10.067 8.534   39.375  1.00 123.58 ? 4   LYS A CD   1 
ATOM   32    C CE   . LYS A 1 4   ? -11.581 8.395   39.445  1.00 123.72 ? 4   LYS A CE   1 
ATOM   33    N NZ   . LYS A 1 4   ? -12.113 8.751   40.793  1.00 121.56 ? 4   LYS A NZ   1 
ATOM   34    H H    . LYS A 1 4   ? -8.517  5.594   39.462  1.00 147.41 ? 4   LYS A H    1 
ATOM   35    H HA   . LYS A 1 4   ? -7.225  7.708   38.453  1.00 144.42 ? 4   LYS A HA   1 
ATOM   36    H HB2  . LYS A 1 4   ? -7.521  7.436   41.210  1.00 146.92 ? 4   LYS A HB2  1 
ATOM   37    H HB3  . LYS A 1 4   ? -7.636  8.761   40.340  1.00 146.92 ? 4   LYS A HB3  1 
ATOM   38    H HG2  . LYS A 1 4   ? -9.680  6.833   40.438  1.00 149.25 ? 4   LYS A HG2  1 
ATOM   39    H HG3  . LYS A 1 4   ? -9.678  8.140   41.342  1.00 149.25 ? 4   LYS A HG3  1 
ATOM   40    H HD2  . LYS A 1 4   ? -9.841  9.474   39.452  1.00 148.30 ? 4   LYS A HD2  1 
ATOM   41    H HD3  . LYS A 1 4   ? -9.767  8.190   38.519  1.00 148.30 ? 4   LYS A HD3  1 
ATOM   42    H HE2  . LYS A 1 4   ? -11.986 8.988   38.793  1.00 148.46 ? 4   LYS A HE2  1 
ATOM   43    H HE3  . LYS A 1 4   ? -11.826 7.476   39.255  1.00 148.46 ? 4   LYS A HE3  1 
ATOM   44    H HZ1  . LYS A 1 4   ? -11.848 9.571   41.018  1.00 145.87 ? 4   LYS A HZ1  1 
ATOM   45    H HZ2  . LYS A 1 4   ? -13.002 8.728   40.785  1.00 145.87 ? 4   LYS A HZ2  1 
ATOM   46    H HZ3  . LYS A 1 4   ? -11.814 8.174   41.400  1.00 145.87 ? 4   LYS A HZ3  1 
ATOM   47    N N    . VAL A 1 5   ? -4.864  7.314   38.990  1.00 111.79 ? 5   VAL A N    1 
ATOM   48    C CA   . VAL A 1 5   ? -3.464  7.082   39.321  1.00 105.51 ? 5   VAL A CA   1 
ATOM   49    C C    . VAL A 1 5   ? -3.064  8.094   40.386  1.00 101.66 ? 5   VAL A C    1 
ATOM   50    O O    . VAL A 1 5   ? -3.193  9.307   40.184  1.00 100.87 ? 5   VAL A O    1 
ATOM   51    C CB   . VAL A 1 5   ? -2.559  7.200   38.084  1.00 102.18 ? 5   VAL A CB   1 
ATOM   52    C CG1  . VAL A 1 5   ? -1.233  6.490   38.341  1.00 94.97  ? 5   VAL A CG1  1 
ATOM   53    C CG2  . VAL A 1 5   ? -3.262  6.644   36.853  1.00 101.09 ? 5   VAL A CG2  1 
ATOM   54    H H    . VAL A 1 5   ? -4.979  7.928   38.398  1.00 134.15 ? 5   VAL A H    1 
ATOM   55    H HA   . VAL A 1 5   ? -3.364  6.189   39.685  1.00 126.61 ? 5   VAL A HA   1 
ATOM   56    H HB   . VAL A 1 5   ? -2.369  8.135   37.909  1.00 122.61 ? 5   VAL A HB   1 
ATOM   57    H HG11 . VAL A 1 5   ? -0.672  6.577   37.554  1.00 113.96 ? 5   VAL A HG11 1 
ATOM   58    H HG12 . VAL A 1 5   ? -0.798  6.900   39.105  1.00 113.96 ? 5   VAL A HG12 1 
ATOM   59    H HG13 . VAL A 1 5   ? -1.406  5.553   38.522  1.00 113.96 ? 5   VAL A HG13 1 
ATOM   60    H HG21 . VAL A 1 5   ? -2.612  6.529   36.143  1.00 121.31 ? 5   VAL A HG21 1 
ATOM   61    H HG22 . VAL A 1 5   ? -3.662  5.788   37.077  1.00 121.31 ? 5   VAL A HG22 1 
ATOM   62    H HG23 . VAL A 1 5   ? -3.951  7.267   36.574  1.00 121.31 ? 5   VAL A HG23 1 
ATOM   63    N N    . GLN A 1 6   ? -2.579  7.599   41.520  1.00 102.02 ? 6   GLN A N    1 
ATOM   64    C CA   . GLN A 1 6   ? -2.123  8.457   42.603  1.00 97.27  ? 6   GLN A CA   1 
ATOM   65    C C    . GLN A 1 6   ? -0.627  8.705   42.461  1.00 90.38  ? 6   GLN A C    1 
ATOM   66    O O    . GLN A 1 6   ? 0.160   7.757   42.365  1.00 88.98  ? 6   GLN A O    1 
ATOM   67    C CB   . GLN A 1 6   ? -2.434  7.823   43.958  1.00 101.50 ? 6   GLN A CB   1 
ATOM   68    C CG   . GLN A 1 6   ? -2.400  8.803   45.112  1.00 98.75  ? 6   GLN A CG   1 
ATOM   69    C CD   . GLN A 1 6   ? -2.994  8.224   46.375  1.00 105.65 ? 6   GLN A CD   1 
ATOM   70    O OE1  . GLN A 1 6   ? -2.994  7.009   46.574  1.00 108.78 ? 6   GLN A OE1  1 
ATOM   71    N NE2  . GLN A 1 6   ? -3.510  9.091   47.238  1.00 106.42 ? 6   GLN A NE2  1 
ATOM   72    H H    . GLN A 1 6   ? -2.504  6.759   41.687  1.00 122.43 ? 6   GLN A H    1 
ATOM   73    H HA   . GLN A 1 6   ? -2.581  9.311   42.559  1.00 116.73 ? 6   GLN A HA   1 
ATOM   74    H HB2  . GLN A 1 6   ? -3.323  7.436   43.924  1.00 121.81 ? 6   GLN A HB2  1 
ATOM   75    H HB3  . GLN A 1 6   ? -1.778  7.132   44.136  1.00 121.81 ? 6   GLN A HB3  1 
ATOM   76    H HG2  . GLN A 1 6   ? -1.479  9.046   45.296  1.00 118.50 ? 6   GLN A HG2  1 
ATOM   77    H HG3  . GLN A 1 6   ? -2.909  9.593   44.873  1.00 118.50 ? 6   GLN A HG3  1 
ATOM   78    H HE21 . GLN A 1 6   ? -3.494  9.933   47.064  1.00 127.71 ? 6   GLN A HE21 1 
ATOM   79    H HE22 . GLN A 1 6   ? -3.861  8.811   47.972  1.00 127.71 ? 6   GLN A HE22 1 
ATOM   80    N N    . VAL A 1 7   ? -0.244  9.979   42.446  1.00 85.17  ? 7   VAL A N    1 
ATOM   81    C CA   . VAL A 1 7   ? 1.146   10.386  42.290  1.00 82.13  ? 7   VAL A CA   1 
ATOM   82    C C    . VAL A 1 7   ? 1.675   10.807  43.654  1.00 82.12  ? 7   VAL A C    1 
ATOM   83    O O    . VAL A 1 7   ? 1.158   11.750  44.268  1.00 83.13  ? 7   VAL A O    1 
ATOM   84    C CB   . VAL A 1 7   ? 1.284   11.524  41.266  1.00 83.30  ? 7   VAL A CB   1 
ATOM   85    C CG1  . VAL A 1 7   ? 2.753   11.844  41.028  1.00 82.70  ? 7   VAL A CG1  1 
ATOM   86    C CG2  . VAL A 1 7   ? 0.586   11.163  39.963  1.00 81.25  ? 7   VAL A CG2  1 
ATOM   87    H H    . VAL A 1 7   ? -0.786  10.641  42.527  1.00 102.20 ? 7   VAL A H    1 
ATOM   88    H HA   . VAL A 1 7   ? 1.670   9.630   41.980  1.00 98.56  ? 7   VAL A HA   1 
ATOM   89    H HB   . VAL A 1 7   ? 0.855   12.320  41.619  1.00 99.97  ? 7   VAL A HB   1 
ATOM   90    H HG11 . VAL A 1 7   ? 2.822   12.502  40.318  1.00 99.25  ? 7   VAL A HG11 1 
ATOM   91    H HG12 . VAL A 1 7   ? 3.136   12.199  41.846  1.00 99.25  ? 7   VAL A HG12 1 
ATOM   92    H HG13 . VAL A 1 7   ? 3.216   11.031  40.772  1.00 99.25  ? 7   VAL A HG13 1 
ATOM   93    H HG21 . VAL A 1 7   ? 0.954   11.705  39.248  1.00 97.50  ? 7   VAL A HG21 1 
ATOM   94    H HG22 . VAL A 1 7   ? 0.734   10.223  39.776  1.00 97.50  ? 7   VAL A HG22 1 
ATOM   95    H HG23 . VAL A 1 7   ? -0.364  11.337  40.055  1.00 97.50  ? 7   VAL A HG23 1 
ATOM   96    N N    . LEU A 1 8   ? 2.708   10.113  44.122  1.00 78.53  ? 8   LEU A N    1 
ATOM   97    C CA   . LEU A 1 8   ? 3.320   10.381  45.412  1.00 74.31  ? 8   LEU A CA   1 
ATOM   98    C C    . LEU A 1 8   ? 4.739   10.907  45.234  1.00 74.87  ? 8   LEU A C    1 
ATOM   99    O O    . LEU A 1 8   ? 5.395   10.632  44.224  1.00 76.61  ? 8   LEU A O    1 
ATOM   100   C CB   . LEU A 1 8   ? 3.363   9.120   46.275  1.00 77.59  ? 8   LEU A CB   1 
ATOM   101   C CG   . LEU A 1 8   ? 2.238   8.102   46.103  1.00 78.98  ? 8   LEU A CG   1 
ATOM   102   C CD1  . LEU A 1 8   ? 2.452   6.922   47.042  1.00 78.22  ? 8   LEU A CD1  1 
ATOM   103   C CD2  . LEU A 1 8   ? 0.891   8.748   46.351  1.00 83.95  ? 8   LEU A CD2  1 
ATOM   104   H H    . LEU A 1 8   ? 3.080   9.465   43.696  1.00 94.23  ? 8   LEU A H    1 
ATOM   105   H HA   . LEU A 1 8   ? 2.797   11.057  45.870  1.00 89.17  ? 8   LEU A HA   1 
ATOM   106   H HB2  . LEU A 1 8   ? 4.192   8.656   46.079  1.00 93.11  ? 8   LEU A HB2  1 
ATOM   107   H HB3  . LEU A 1 8   ? 3.349   9.398   47.204  1.00 93.11  ? 8   LEU A HB3  1 
ATOM   108   H HG   . LEU A 1 8   ? 2.243   7.769   45.192  1.00 94.77  ? 8   LEU A HG   1 
ATOM   109   H HD11 . LEU A 1 8   ? 1.734   6.282   46.913  1.00 93.86  ? 8   LEU A HD11 1 
ATOM   110   H HD12 . LEU A 1 8   ? 3.305   6.508   46.839  1.00 93.86  ? 8   LEU A HD12 1 
ATOM   111   H HD13 . LEU A 1 8   ? 2.449   7.243   47.958  1.00 93.86  ? 8   LEU A HD13 1 
ATOM   112   H HD21 . LEU A 1 8   ? 0.211   8.057   46.386  1.00 100.74 ? 8   LEU A HD21 1 
ATOM   113   H HD22 . LEU A 1 8   ? 0.920   9.226   47.195  1.00 100.74 ? 8   LEU A HD22 1 
ATOM   114   H HD23 . LEU A 1 8   ? 0.699   9.365   45.628  1.00 100.74 ? 8   LEU A HD23 1 
ATOM   115   N N    . ASP A 1 9   ? 5.202   11.663  46.223  1.00 72.47  ? 9   ASP A N    1 
ATOM   116   C CA   . ASP A 1 9   ? 6.568   12.166  46.248  1.00 71.11  ? 9   ASP A CA   1 
ATOM   117   C C    . ASP A 1 9   ? 7.426   11.183  47.032  1.00 70.08  ? 9   ASP A C    1 
ATOM   118   O O    . ASP A 1 9   ? 7.148   10.911  48.204  1.00 74.80  ? 9   ASP A O    1 
ATOM   119   C CB   . ASP A 1 9   ? 6.611   13.560  46.866  1.00 73.48  ? 9   ASP A CB   1 
ATOM   120   C CG   . ASP A 1 9   ? 5.762   14.557  46.094  1.00 79.05  ? 9   ASP A CG   1 
ATOM   121   O OD1  . ASP A 1 9   ? 6.277   15.147  45.119  1.00 78.91  ? 9   ASP A OD1  1 
ATOM   122   O OD2  . ASP A 1 9   ? 4.575   14.743  46.448  1.00 82.84  ? 9   ASP A OD2  1 
ATOM   123   H H    . ASP A 1 9   ? 4.734   11.903  46.904  1.00 86.96  ? 9   ASP A H    1 
ATOM   124   H HA   . ASP A 1 9   ? 6.922   12.233  45.347  1.00 85.34  ? 9   ASP A HA   1 
ATOM   125   H HB2  . ASP A 1 9   ? 6.274   13.516  47.774  1.00 88.17  ? 9   ASP A HB2  1 
ATOM   126   H HB3  . ASP A 1 9   ? 7.526   13.880  46.867  1.00 88.17  ? 9   ASP A HB3  1 
ATOM   127   N N    . PHE A 1 10  ? 8.455   10.646  46.386  1.00 67.24  ? 10  PHE A N    1 
ATOM   128   C CA   . PHE A 1 10  ? 9.289   9.612   46.971  1.00 69.47  ? 10  PHE A CA   1 
ATOM   129   C C    . PHE A 1 10  ? 10.735  10.073  47.061  1.00 67.54  ? 10  PHE A C    1 
ATOM   130   O O    . PHE A 1 10  ? 11.185  10.931  46.300  1.00 64.50  ? 10  PHE A O    1 
ATOM   131   C CB   . PHE A 1 10  ? 9.213   8.298   46.151  1.00 70.23  ? 10  PHE A CB   1 
ATOM   132   C CG   . PHE A 1 10  ? 10.232  8.207   45.038  1.00 72.37  ? 10  PHE A CG   1 
ATOM   133   C CD1  . PHE A 1 10  ? 11.498  7.686   45.276  1.00 70.85  ? 10  PHE A CD1  1 
ATOM   134   C CD2  . PHE A 1 10  ? 9.919   8.632   43.751  1.00 72.11  ? 10  PHE A CD2  1 
ATOM   135   C CE1  . PHE A 1 10  ? 12.435  7.605   44.259  1.00 70.98  ? 10  PHE A CE1  1 
ATOM   136   C CE2  . PHE A 1 10  ? 10.852  8.553   42.726  1.00 71.91  ? 10  PHE A CE2  1 
ATOM   137   C CZ   . PHE A 1 10  ? 12.112  8.038   42.983  1.00 73.45  ? 10  PHE A CZ   1 
ATOM   138   H H    . PHE A 1 10  ? 8.693   10.872  45.591  1.00 80.69  ? 10  PHE A H    1 
ATOM   139   H HA   . PHE A 1 10  ? 8.978   9.432   47.872  1.00 83.37  ? 10  PHE A HA   1 
ATOM   140   H HB2  . PHE A 1 10  ? 9.363   7.550   46.750  1.00 84.27  ? 10  PHE A HB2  1 
ATOM   141   H HB3  . PHE A 1 10  ? 8.332   8.232   45.751  1.00 84.27  ? 10  PHE A HB3  1 
ATOM   142   H HD1  . PHE A 1 10  ? 11.719  7.388   46.129  1.00 85.02  ? 10  PHE A HD1  1 
ATOM   143   H HD2  . PHE A 1 10  ? 9.073   8.975   43.574  1.00 86.54  ? 10  PHE A HD2  1 
ATOM   144   H HE1  . PHE A 1 10  ? 13.281  7.260   44.433  1.00 85.18  ? 10  PHE A HE1  1 
ATOM   145   H HE2  . PHE A 1 10  ? 10.633  8.845   41.871  1.00 86.30  ? 10  PHE A HE2  1 
ATOM   146   H HZ   . PHE A 1 10  ? 12.740  7.982   42.300  1.00 88.15  ? 10  PHE A HZ   1 
ATOM   147   N N    . ILE A 1 11  ? 11.452  9.495   48.024  1.00 73.45  ? 11  ILE A N    1 
ATOM   148   C CA   . ILE A 1 11  ? 12.904  9.588   48.108  1.00 70.59  ? 11  ILE A CA   1 
ATOM   149   C C    . ILE A 1 11  ? 13.408  8.193   48.447  1.00 69.90  ? 11  ILE A C    1 
ATOM   150   O O    . ILE A 1 11  ? 12.966  7.598   49.436  1.00 70.71  ? 11  ILE A O    1 
ATOM   151   C CB   . ILE A 1 11  ? 13.377  10.601  49.161  1.00 67.82  ? 11  ILE A CB   1 
ATOM   152   C CG1  . ILE A 1 11  ? 12.643  11.932  49.002  1.00 68.35  ? 11  ILE A CG1  1 
ATOM   153   C CG2  . ILE A 1 11  ? 14.886  10.806  49.038  1.00 67.98  ? 11  ILE A CG2  1 
ATOM   154   C CD1  . ILE A 1 11  ? 11.422  12.076  49.886  1.00 68.69  ? 11  ILE A CD1  1 
ATOM   155   H H    . ILE A 1 11  ? 11.106  9.029   48.659  1.00 88.14  ? 11  ILE A H    1 
ATOM   156   H HA   . ILE A 1 11  ? 13.268  9.867   47.253  1.00 84.71  ? 11  ILE A HA   1 
ATOM   157   H HB   . ILE A 1 11  ? 13.173  10.250  50.042  1.00 81.39  ? 11  ILE A HB   1 
ATOM   158   H HG12 . ILE A 1 11  ? 13.254  12.652  49.223  1.00 82.02  ? 11  ILE A HG12 1 
ATOM   159   H HG13 . ILE A 1 11  ? 12.351  12.016  48.081  1.00 82.02  ? 11  ILE A HG13 1 
ATOM   160   H HG21 . ILE A 1 11  ? 15.168  11.474  49.682  1.00 81.57  ? 11  ILE A HG21 1 
ATOM   161   H HG22 . ILE A 1 11  ? 15.335  9.965   49.216  1.00 81.57  ? 11  ILE A HG22 1 
ATOM   162   H HG23 . ILE A 1 11  ? 15.091  11.107  48.138  1.00 81.57  ? 11  ILE A HG23 1 
ATOM   163   H HD11 . ILE A 1 11  ? 11.048  12.963  49.764  1.00 82.43  ? 11  ILE A HD11 1 
ATOM   164   H HD12 . ILE A 1 11  ? 10.769  11.405  49.635  1.00 82.43  ? 11  ILE A HD12 1 
ATOM   165   H HD13 . ILE A 1 11  ? 11.686  11.952  50.811  1.00 82.43  ? 11  ILE A HD13 1 
ATOM   166   N N    . LYS A 1 12  ? 14.296  7.655   47.618  1.00 69.16  ? 12  LYS A N    1 
ATOM   167   C CA   . LYS A 1 12  ? 14.886  6.345   47.855  1.00 68.27  ? 12  LYS A CA   1 
ATOM   168   C C    . LYS A 1 12  ? 16.273  6.539   48.443  1.00 71.01  ? 12  LYS A C    1 
ATOM   169   O O    . LYS A 1 12  ? 17.063  7.341   47.932  1.00 72.79  ? 12  LYS A O    1 
ATOM   170   C CB   . LYS A 1 12  ? 14.965  5.527   46.570  1.00 71.11  ? 12  LYS A CB   1 
ATOM   171   C CG   . LYS A 1 12  ? 15.177  4.044   46.814  1.00 72.01  ? 12  LYS A CG   1 
ATOM   172   C CD   . LYS A 1 12  ? 14.725  3.212   45.621  1.00 74.47  ? 12  LYS A CD   1 
ATOM   173   C CE   . LYS A 1 12  ? 15.510  1.908   45.529  1.00 72.43  ? 12  LYS A CE   1 
ATOM   174   N NZ   . LYS A 1 12  ? 14.648  0.758   45.141  1.00 75.65  ? 12  LYS A NZ   1 
ATOM   175   H H    . LYS A 1 12  ? 14.577  8.038   46.901  1.00 83.00  ? 12  LYS A H    1 
ATOM   176   H HA   . LYS A 1 12  ? 14.338  5.848   48.482  1.00 81.93  ? 12  LYS A HA   1 
ATOM   177   H HB2  . LYS A 1 12  ? 14.135  5.633   46.079  1.00 85.33  ? 12  LYS A HB2  1 
ATOM   178   H HB3  . LYS A 1 12  ? 15.709  5.851   46.038  1.00 85.33  ? 12  LYS A HB3  1 
ATOM   179   H HG2  . LYS A 1 12  ? 16.121  3.874   46.964  1.00 86.41  ? 12  LYS A HG2  1 
ATOM   180   H HG3  . LYS A 1 12  ? 14.664  3.769   47.590  1.00 86.41  ? 12  LYS A HG3  1 
ATOM   181   H HD2  . LYS A 1 12  ? 13.784  2.996   45.716  1.00 89.37  ? 12  LYS A HD2  1 
ATOM   182   H HD3  . LYS A 1 12  ? 14.870  3.714   44.804  1.00 89.37  ? 12  LYS A HD3  1 
ATOM   183   H HE2  . LYS A 1 12  ? 16.207  2.002   44.861  1.00 86.92  ? 12  LYS A HE2  1 
ATOM   184   H HE3  . LYS A 1 12  ? 15.904  1.712   46.393  1.00 86.92  ? 12  LYS A HE3  1 
ATOM   185   H HZ1  . LYS A 1 12  ? 15.135  0.014   45.095  1.00 90.78  ? 12  LYS A HZ1  1 
ATOM   186   H HZ2  . LYS A 1 12  ? 14.277  0.910   44.347  1.00 90.78  ? 12  LYS A HZ2  1 
ATOM   187   H HZ3  . LYS A 1 12  ? 14.003  0.644   45.744  1.00 90.78  ? 12  LYS A HZ3  1 
ATOM   188   N N    . ILE A 1 13  ? 16.563  5.808   49.514  1.00 70.72  ? 13  ILE A N    1 
ATOM   189   C CA   . ILE A 1 13  ? 17.784  5.984   50.289  1.00 69.95  ? 13  ILE A CA   1 
ATOM   190   C C    . ILE A 1 13  ? 18.316  4.607   50.652  1.00 69.75  ? 13  ILE A C    1 
ATOM   191   O O    . ILE A 1 13  ? 17.539  3.684   50.920  1.00 70.60  ? 13  ILE A O    1 
ATOM   192   C CB   . ILE A 1 13  ? 17.527  6.830   51.553  1.00 70.05  ? 13  ILE A CB   1 
ATOM   193   C CG1  . ILE A 1 13  ? 16.599  8.003   51.233  1.00 69.97  ? 13  ILE A CG1  1 
ATOM   194   C CG2  . ILE A 1 13  ? 18.841  7.326   52.131  1.00 69.77  ? 13  ILE A CG2  1 
ATOM   195   C CD1  . ILE A 1 13  ? 16.139  8.784   52.453  1.00 70.06  ? 13  ILE A CD1  1 
ATOM   196   H H    . ILE A 1 13  ? 16.054  5.186   49.818  1.00 84.86  ? 13  ILE A H    1 
ATOM   197   H HA   . ILE A 1 13  ? 18.453  6.438   49.753  1.00 83.94  ? 13  ILE A HA   1 
ATOM   198   H HB   . ILE A 1 13  ? 17.092  6.269   52.214  1.00 84.05  ? 13  ILE A HB   1 
ATOM   199   H HG12 . ILE A 1 13  ? 17.067  8.619   50.648  1.00 83.97  ? 13  ILE A HG12 1 
ATOM   200   H HG13 . ILE A 1 13  ? 15.808  7.661   50.788  1.00 83.97  ? 13  ILE A HG13 1 
ATOM   201   H HG21 . ILE A 1 13  ? 18.659  7.835   52.937  1.00 83.72  ? 13  ILE A HG21 1 
ATOM   202   H HG22 . ILE A 1 13  ? 19.402  6.564   52.341  1.00 83.72  ? 13  ILE A HG22 1 
ATOM   203   H HG23 . ILE A 1 13  ? 19.281  7.891   51.476  1.00 83.72  ? 13  ILE A HG23 1 
ATOM   204   H HD11 . ILE A 1 13  ? 15.492  9.452   52.176  1.00 84.08  ? 13  ILE A HD11 1 
ATOM   205   H HD12 . ILE A 1 13  ? 15.732  8.171   53.086  1.00 84.08  ? 13  ILE A HD12 1 
ATOM   206   H HD13 . ILE A 1 13  ? 16.907  9.216   52.859  1.00 84.08  ? 13  ILE A HD13 1 
ATOM   207   N N    . ASN A 1 14  ? 19.643  4.467   50.652  1.00 71.11  ? 14  ASN A N    1 
ATOM   208   C CA   . ASN A 1 14  ? 20.307  3.233   51.060  1.00 70.75  ? 14  ASN A CA   1 
ATOM   209   C C    . ASN A 1 14  ? 20.981  3.432   52.411  1.00 71.15  ? 14  ASN A C    1 
ATOM   210   O O    . ASN A 1 14  ? 22.175  3.765   52.473  1.00 71.14  ? 14  ASN A O    1 
ATOM   211   C CB   . ASN A 1 14  ? 21.332  2.795   50.011  1.00 72.72  ? 14  ASN A CB   1 
ATOM   212   C CG   . ASN A 1 14  ? 22.112  1.565   50.442  1.00 73.21  ? 14  ASN A CG   1 
ATOM   213   O OD1  . ASN A 1 14  ? 21.570  0.670   51.091  1.00 72.61  ? 14  ASN A OD1  1 
ATOM   214   N ND2  . ASN A 1 14  ? 23.389  1.511   50.076  1.00 74.60  ? 14  ASN A ND2  1 
ATOM   215   H H    . ASN A 1 14  ? 20.189  5.087   50.413  1.00 85.33  ? 14  ASN A H    1 
ATOM   216   H HA   . ASN A 1 14  ? 19.637  2.538   51.156  1.00 84.90  ? 14  ASN A HA   1 
ATOM   217   H HB2  . ASN A 1 14  ? 20.870  2.585   49.184  1.00 87.26  ? 14  ASN A HB2  1 
ATOM   218   H HB3  . ASN A 1 14  ? 21.964  3.516   49.863  1.00 87.26  ? 14  ASN A HB3  1 
ATOM   219   H HD21 . ASN A 1 14  ? 23.872  0.835   50.297  1.00 89.52  ? 14  ASN A HD21 1 
ATOM   220   H HD22 . ASN A 1 14  ? 23.733  2.154   49.619  1.00 89.52  ? 14  ASN A HD22 1 
ATOM   221   N N    . PRO A 1 15  ? 20.265  3.245   53.524  1.00 73.17  ? 15  PRO A N    1 
ATOM   222   C CA   . PRO A 1 15  ? 20.939  3.234   54.830  1.00 70.77  ? 15  PRO A CA   1 
ATOM   223   C C    . PRO A 1 15  ? 21.599  1.893   55.105  1.00 71.69  ? 15  PRO A C    1 
ATOM   224   O O    . PRO A 1 15  ? 20.946  0.954   55.571  1.00 73.91  ? 15  PRO A O    1 
ATOM   225   C CB   . PRO A 1 15  ? 19.802  3.522   55.816  1.00 73.13  ? 15  PRO A CB   1 
ATOM   226   C CG   . PRO A 1 15  ? 18.585  2.959   55.146  1.00 73.11  ? 15  PRO A CG   1 
ATOM   227   C CD   . PRO A 1 15  ? 18.799  3.105   53.650  1.00 71.90  ? 15  PRO A CD   1 
ATOM   228   H HA   . PRO A 1 15  ? 21.596  3.944   54.892  1.00 84.93  ? 15  PRO A HA   1 
ATOM   229   H HB2  . PRO A 1 15  ? 19.973  3.078   56.662  1.00 87.76  ? 15  PRO A HB2  1 
ATOM   230   H HB3  . PRO A 1 15  ? 19.715  4.478   55.955  1.00 87.76  ? 15  PRO A HB3  1 
ATOM   231   H HG2  . PRO A 1 15  ? 18.487  2.024   55.385  1.00 87.73  ? 15  PRO A HG2  1 
ATOM   232   H HG3  . PRO A 1 15  ? 17.802  3.457   55.427  1.00 87.73  ? 15  PRO A HG3  1 
ATOM   233   H HD2  . PRO A 1 15  ? 18.486  2.317   53.179  1.00 86.28  ? 15  PRO A HD2  1 
ATOM   234   H HD3  . PRO A 1 15  ? 18.347  3.894   53.313  1.00 86.28  ? 15  PRO A HD3  1 
ATOM   235   N N    . ALA A 1 16  ? 22.889  1.793   54.810  1.00 71.42  ? 16  ALA A N    1 
ATOM   236   C CA   . ALA A 1 16  ? 23.666  0.577   55.033  1.00 73.96  ? 16  ALA A CA   1 
ATOM   237   C C    . ALA A 1 16  ? 22.908  -0.666  54.569  1.00 75.30  ? 16  ALA A C    1 
ATOM   238   O O    . ALA A 1 16  ? 22.802  -1.669  55.275  1.00 75.82  ? 16  ALA A O    1 
ATOM   239   C CB   . ALA A 1 16  ? 24.063  0.453   56.502  1.00 72.69  ? 16  ALA A CB   1 
ATOM   240   H H    . ALA A 1 16  ? 23.351  2.433   54.469  1.00 85.70  ? 16  ALA A H    1 
ATOM   241   H HA   . ALA A 1 16  ? 24.474  0.638   54.500  1.00 88.75  ? 16  ALA A HA   1 
ATOM   242   H HB1  . ALA A 1 16  ? 24.576  -0.361  56.622  1.00 87.23  ? 16  ALA A HB1  1 
ATOM   243   H HB2  . ALA A 1 16  ? 24.599  1.222   56.750  1.00 87.23  ? 16  ALA A HB2  1 
ATOM   244   H HB3  . ALA A 1 16  ? 23.259  0.421   57.044  1.00 87.23  ? 16  ALA A HB3  1 
ATOM   245   N N    . GLY A 1 17  ? 22.373  -0.590  53.350  1.00 76.75  ? 17  GLY A N    1 
ATOM   246   C CA   . GLY A 1 17  ? 21.725  -1.717  52.716  1.00 76.00  ? 17  GLY A CA   1 
ATOM   247   C C    . GLY A 1 17  ? 20.248  -1.877  53.020  1.00 77.76  ? 17  GLY A C    1 
ATOM   248   O O    . GLY A 1 17  ? 19.549  -2.565  52.269  1.00 79.01  ? 17  GLY A O    1 
ATOM   249   H H    . GLY A 1 17  ? 22.378  0.121   52.867  1.00 92.09  ? 17  GLY A H    1 
ATOM   250   H HA2  . GLY A 1 17  ? 21.818  -1.625  51.755  1.00 91.20  ? 17  GLY A HA2  1 
ATOM   251   H HA3  . GLY A 1 17  ? 22.172  -2.529  53.000  1.00 91.20  ? 17  GLY A HA3  1 
ATOM   252   N N    . ASN A 1 18  ? 19.750  -1.271  54.096  1.00 75.27  ? 18  ASN A N    1 
ATOM   253   C CA   . ASN A 1 18  ? 18.342  -1.392  54.490  1.00 77.47  ? 18  ASN A CA   1 
ATOM   254   C C    . ASN A 1 18  ? 17.527  -0.416  53.639  1.00 76.05  ? 18  ASN A C    1 
ATOM   255   O O    . ASN A 1 18  ? 17.120  0.661   54.080  1.00 76.76  ? 18  ASN A O    1 
ATOM   256   C CB   . ASN A 1 18  ? 18.202  -1.122  55.983  1.00 77.16  ? 18  ASN A CB   1 
ATOM   257   C CG   . ASN A 1 18  ? 16.885  -1.629  56.574  1.00 76.81  ? 18  ASN A CG   1 
ATOM   258   O OD1  . ASN A 1 18  ? 16.510  -1.228  57.675  1.00 78.04  ? 18  ASN A OD1  1 
ATOM   259   N ND2  . ASN A 1 18  ? 16.193  -2.510  55.858  1.00 77.57  ? 18  ASN A ND2  1 
ATOM   260   H H    . ASN A 1 18  ? 20.213  -0.775  54.625  1.00 90.32  ? 18  ASN A H    1 
ATOM   261   H HA   . ASN A 1 18  ? 18.015  -2.287  54.310  1.00 92.96  ? 18  ASN A HA   1 
ATOM   262   H HB2  . ASN A 1 18  ? 18.927  -1.566  56.451  1.00 92.59  ? 18  ASN A HB2  1 
ATOM   263   H HB3  . ASN A 1 18  ? 18.247  -0.165  56.134  1.00 92.59  ? 18  ASN A HB3  1 
ATOM   264   H HD21 . ASN A 1 18  ? 16.491  -2.773  55.095  1.00 93.08  ? 18  ASN A HD21 1 
ATOM   265   H HD22 . ASN A 1 18  ? 15.448  -2.817  56.157  1.00 93.08  ? 18  ASN A HD22 1 
ATOM   266   N N    . ILE A 1 19  ? 17.273  -0.821  52.392  1.00 77.24  ? 19  ILE A N    1 
ATOM   267   C CA   . ILE A 1 19  ? 16.670  0.061   51.396  1.00 76.70  ? 19  ILE A CA   1 
ATOM   268   C C    . ILE A 1 19  ? 15.371  0.653   51.930  1.00 75.18  ? 19  ILE A C    1 
ATOM   269   O O    . ILE A 1 19  ? 14.443  -0.077  52.298  1.00 73.73  ? 19  ILE A O    1 
ATOM   270   C CB   . ILE A 1 19  ? 16.417  -0.678  50.070  1.00 79.93  ? 19  ILE A CB   1 
ATOM   271   C CG1  . ILE A 1 19  ? 17.740  -1.145  49.455  1.00 78.27  ? 19  ILE A CG1  1 
ATOM   272   C CG2  . ILE A 1 19  ? 15.671  0.219   49.079  1.00 76.67  ? 19  ILE A CG2  1 
ATOM   273   C CD1  . ILE A 1 19  ? 18.700  -0.011  49.145  1.00 79.92  ? 19  ILE A CD1  1 
ATOM   274   H H    . ILE A 1 19  ? 17.444  -1.611  52.097  1.00 92.69  ? 19  ILE A H    1 
ATOM   275   H HA   . ILE A 1 19  ? 17.287  0.791   51.234  1.00 92.04  ? 19  ILE A HA   1 
ATOM   276   H HB   . ILE A 1 19  ? 15.868  -1.454  50.263  1.00 95.92  ? 19  ILE A HB   1 
ATOM   277   H HG12 . ILE A 1 19  ? 18.180  -1.744  50.078  1.00 93.93  ? 19  ILE A HG12 1 
ATOM   278   H HG13 . ILE A 1 19  ? 17.551  -1.610  48.625  1.00 93.93  ? 19  ILE A HG13 1 
ATOM   279   H HG21 . ILE A 1 19  ? 15.623  -0.230  48.220  1.00 92.01  ? 19  ILE A HG21 1 
ATOM   280   H HG22 . ILE A 1 19  ? 14.776  0.386   49.415  1.00 92.01  ? 19  ILE A HG22 1 
ATOM   281   H HG23 . ILE A 1 19  ? 16.151  1.057   48.988  1.00 92.01  ? 19  ILE A HG23 1 
ATOM   282   H HD11 . ILE A 1 19  ? 19.539  -0.384  48.832  1.00 95.90  ? 19  ILE A HD11 1 
ATOM   283   H HD12 . ILE A 1 19  ? 18.312  0.552   48.456  1.00 95.90  ? 19  ILE A HD12 1 
ATOM   284   H HD13 . ILE A 1 19  ? 18.848  0.507   49.951  1.00 95.90  ? 19  ILE A HD13 1 
ATOM   285   N N    . THR A 1 20  ? 15.298  1.984   51.957  1.00 73.66  ? 20  THR A N    1 
ATOM   286   C CA   . THR A 1 20  ? 14.177  2.716   52.517  1.00 74.01  ? 20  THR A CA   1 
ATOM   287   C C    . THR A 1 20  ? 13.654  3.706   51.487  1.00 72.13  ? 20  THR A C    1 
ATOM   288   O O    . THR A 1 20  ? 14.430  4.379   50.802  1.00 70.52  ? 20  THR A O    1 
ATOM   289   C CB   . THR A 1 20  ? 14.594  3.467   53.796  1.00 74.04  ? 20  THR A CB   1 
ATOM   290   O OG1  . THR A 1 20  ? 15.223  2.553   54.708  1.00 74.67  ? 20  THR A OG1  1 
ATOM   291   C CG2  . THR A 1 20  ? 13.384  4.105   54.471  1.00 74.00  ? 20  THR A CG2  1 
ATOM   292   H H    . THR A 1 20  ? 15.912  2.499   51.644  1.00 88.39  ? 20  THR A H    1 
ATOM   293   H HA   . THR A 1 20  ? 13.461  2.101   52.740  1.00 88.81  ? 20  THR A HA   1 
ATOM   294   H HB   . THR A 1 20  ? 15.217  4.173   53.563  1.00 88.85  ? 20  THR A HB   1 
ATOM   295   H HG1  . THR A 1 20  ? 14.696  1.926   54.896  1.00 89.60  ? 20  THR A HG1  1 
ATOM   296   H HG21 . THR A 1 20  ? 13.643  4.486   55.325  1.00 88.80  ? 20  THR A HG21 1 
ATOM   297   H HG22 . THR A 1 20  ? 13.022  4.808   53.909  1.00 88.80  ? 20  THR A HG22 1 
ATOM   298   H HG23 . THR A 1 20  ? 12.697  3.437   54.620  1.00 88.80  ? 20  THR A HG23 1 
ATOM   299   N N    . ILE A 1 21  ? 12.330  3.775   51.369  1.00 71.17  ? 21  ILE A N    1 
ATOM   300   C CA   . ILE A 1 21  ? 11.655  4.796   50.577  1.00 72.34  ? 21  ILE A CA   1 
ATOM   301   C C    . ILE A 1 21  ? 10.866  5.671   51.541  1.00 73.67  ? 21  ILE A C    1 
ATOM   302   O O    . ILE A 1 21  ? 10.164  5.157   52.420  1.00 73.17  ? 21  ILE A O    1 
ATOM   303   C CB   . ILE A 1 21  ? 10.726  4.185   49.515  1.00 73.51  ? 21  ILE A CB   1 
ATOM   304   C CG1  . ILE A 1 21  ? 11.514  3.307   48.542  1.00 74.38  ? 21  ILE A CG1  1 
ATOM   305   C CG2  . ILE A 1 21  ? 10.003  5.288   48.749  1.00 74.39  ? 21  ILE A CG2  1 
ATOM   306   C CD1  . ILE A 1 21  ? 10.638  2.477   47.636  1.00 74.70  ? 21  ILE A CD1  1 
ATOM   307   H H    . ILE A 1 21  ? 11.789  3.226   51.750  1.00 85.41  ? 21  ILE A H    1 
ATOM   308   H HA   . ILE A 1 21  ? 12.316  5.335   50.116  1.00 86.82  ? 21  ILE A HA   1 
ATOM   309   H HB   . ILE A 1 21  ? 10.073  3.630   49.970  1.00 88.21  ? 21  ILE A HB   1 
ATOM   310   H HG12 . ILE A 1 21  ? 12.065  3.877   47.983  1.00 89.26  ? 21  ILE A HG12 1 
ATOM   311   H HG13 . ILE A 1 21  ? 12.074  2.700   49.052  1.00 89.26  ? 21  ILE A HG13 1 
ATOM   312   H HG21 . ILE A 1 21  ? 9.400   4.884   48.106  1.00 89.27  ? 21  ILE A HG21 1 
ATOM   313   H HG22 . ILE A 1 21  ? 9.502   5.832   49.376  1.00 89.27  ? 21  ILE A HG22 1 
ATOM   314   H HG23 . ILE A 1 21  ? 10.660  5.835   48.288  1.00 89.27  ? 21  ILE A HG23 1 
ATOM   315   H HD11 . ILE A 1 21  ? 11.202  1.960   47.039  1.00 89.64  ? 21  ILE A HD11 1 
ATOM   316   H HD12 . ILE A 1 21  ? 10.097  1.883   48.177  1.00 89.64  ? 21  ILE A HD12 1 
ATOM   317   H HD13 . ILE A 1 21  ? 10.067  3.069   47.121  1.00 89.64  ? 21  ILE A HD13 1 
ATOM   318   N N    . LEU A 1 22  ? 10.981  6.986   51.381  1.00 72.30  ? 22  LEU A N    1 
ATOM   319   C CA   . LEU A 1 22  ? 10.243  7.948   52.187  1.00 69.36  ? 22  LEU A CA   1 
ATOM   320   C C    . LEU A 1 22  ? 9.256   8.689   51.296  1.00 72.36  ? 22  LEU A C    1 
ATOM   321   O O    . LEU A 1 22  ? 9.640   9.234   50.256  1.00 72.48  ? 22  LEU A O    1 
ATOM   322   C CB   . LEU A 1 22  ? 11.196  8.928   52.868  1.00 71.07  ? 22  LEU A CB   1 
ATOM   323   C CG   . LEU A 1 22  ? 12.223  8.279   53.802  1.00 73.88  ? 22  LEU A CG   1 
ATOM   324   C CD1  . LEU A 1 22  ? 13.194  9.316   54.355  1.00 71.86  ? 22  LEU A CD1  1 
ATOM   325   C CD2  . LEU A 1 22  ? 11.532  7.520   54.933  1.00 68.18  ? 22  LEU A CD2  1 
ATOM   326   H H    . LEU A 1 22  ? 11.495  7.352   50.797  1.00 86.75  ? 22  LEU A H    1 
ATOM   327   H HA   . LEU A 1 22  ? 9.741   7.488   52.878  1.00 83.24  ? 22  LEU A HA   1 
ATOM   328   H HB2  . LEU A 1 22  ? 11.686  9.407   52.182  1.00 85.28  ? 22  LEU A HB2  1 
ATOM   329   H HB3  . LEU A 1 22  ? 10.672  9.550   53.396  1.00 85.28  ? 22  LEU A HB3  1 
ATOM   330   H HG   . LEU A 1 22  ? 12.741  7.637   53.291  1.00 88.66  ? 22  LEU A HG   1 
ATOM   331   H HD11 . LEU A 1 22  ? 13.833  8.873   54.935  1.00 86.23  ? 22  LEU A HD11 1 
ATOM   332   H HD12 . LEU A 1 22  ? 13.657  9.741   53.616  1.00 86.23  ? 22  LEU A HD12 1 
ATOM   333   H HD13 . LEU A 1 22  ? 12.695  9.979   54.858  1.00 86.23  ? 22  LEU A HD13 1 
ATOM   334   H HD21 . LEU A 1 22  ? 12.198  7.239   55.579  1.00 81.82  ? 22  LEU A HD21 1 
ATOM   335   H HD22 . LEU A 1 22  ? 10.886  8.106   55.358  1.00 81.82  ? 22  LEU A HD22 1 
ATOM   336   H HD23 . LEU A 1 22  ? 11.082  6.744   54.563  1.00 81.82  ? 22  LEU A HD23 1 
ATOM   337   N N    . ILE A 1 23  ? 7.989   8.694   51.696  1.00 73.47  ? 23  ILE A N    1 
ATOM   338   C CA   . ILE A 1 23  ? 6.926   9.360   50.952  1.00 72.90  ? 23  ILE A CA   1 
ATOM   339   C C    . ILE A 1 23  ? 6.671   10.707  51.612  1.00 74.12  ? 23  ILE A C    1 
ATOM   340   O O    . ILE A 1 23  ? 6.380   10.777  52.812  1.00 73.11  ? 23  ILE A O    1 
ATOM   341   C CB   . ILE A 1 23  ? 5.649   8.507   50.909  1.00 73.82  ? 23  ILE A CB   1 
ATOM   342   C CG1  . ILE A 1 23  ? 5.744   7.485   49.777  1.00 76.37  ? 23  ILE A CG1  1 
ATOM   343   C CG2  . ILE A 1 23  ? 4.419   9.381   50.717  1.00 74.79  ? 23  ILE A CG2  1 
ATOM   344   C CD1  . ILE A 1 23  ? 6.921   6.543   49.909  1.00 78.99  ? 23  ILE A CD1  1 
ATOM   345   H H    . ILE A 1 23  ? 7.714   8.309   52.414  1.00 88.16  ? 23  ILE A H    1 
ATOM   346   H HA   . ILE A 1 23  ? 7.215   9.513   50.038  1.00 87.48  ? 23  ILE A HA   1 
ATOM   347   H HB   . ILE A 1 23  ? 5.567   8.042   51.756  1.00 88.58  ? 23  ILE A HB   1 
ATOM   348   H HG12 . ILE A 1 23  ? 4.935   6.950   49.771  1.00 91.65  ? 23  ILE A HG12 1 
ATOM   349   H HG13 . ILE A 1 23  ? 5.836   7.958   48.936  1.00 91.65  ? 23  ILE A HG13 1 
ATOM   350   H HG21 . ILE A 1 23  ? 3.674   8.822   50.447  1.00 89.75  ? 23  ILE A HG21 1 
ATOM   351   H HG22 . ILE A 1 23  ? 4.213   9.824   51.555  1.00 89.75  ? 23  ILE A HG22 1 
ATOM   352   H HG23 . ILE A 1 23  ? 4.604   10.041  50.031  1.00 89.75  ? 23  ILE A HG23 1 
ATOM   353   H HD11 . ILE A 1 23  ? 6.813   5.813   49.279  1.00 94.78  ? 23  ILE A HD11 1 
ATOM   354   H HD12 . ILE A 1 23  ? 7.738   7.029   49.716  1.00 94.78  ? 23  ILE A HD12 1 
ATOM   355   H HD13 . ILE A 1 23  ? 6.948   6.196   50.815  1.00 94.78  ? 23  ILE A HD13 1 
ATOM   356   N N    . ASP A 1 24  ? 6.775   11.776  50.828  1.00 75.57  ? 24  ASP A N    1 
ATOM   357   C CA   . ASP A 1 24  ? 6.652   13.145  51.306  1.00 75.07  ? 24  ASP A CA   1 
ATOM   358   C C    . ASP A 1 24  ? 5.326   13.743  50.856  1.00 75.45  ? 24  ASP A C    1 
ATOM   359   O O    . ASP A 1 24  ? 4.718   13.300  49.877  1.00 73.79  ? 24  ASP A O    1 
ATOM   360   C CB   . ASP A 1 24  ? 7.817   13.996  50.784  1.00 72.71  ? 24  ASP A CB   1 
ATOM   361   C CG   . ASP A 1 24  ? 8.117   15.191  51.664  1.00 74.60  ? 24  ASP A CG   1 
ATOM   362   O OD1  . ASP A 1 24  ? 7.465   15.356  52.720  1.00 76.25  ? 24  ASP A OD1  1 
ATOM   363   O OD2  . ASP A 1 24  ? 9.016   15.972  51.287  1.00 75.12  ? 24  ASP A OD2  1 
ATOM   364   H H    . ASP A 1 24  ? 6.922   11.730  49.982  1.00 90.69  ? 24  ASP A H    1 
ATOM   365   H HA   . ASP A 1 24  ? 6.671   13.158  52.276  1.00 90.09  ? 24  ASP A HA   1 
ATOM   366   H HB2  . ASP A 1 24  ? 8.616   13.447  50.743  1.00 87.26  ? 24  ASP A HB2  1 
ATOM   367   H HB3  . ASP A 1 24  ? 7.595   14.325  49.899  1.00 87.26  ? 24  ASP A HB3  1 
ATOM   368   N N    . ASN A 1 25  ? 4.875   14.759  51.591  1.00 74.76  ? 25  ASN A N    1 
ATOM   369   C CA   . ASN A 1 25  ? 3.663   15.494  51.239  1.00 75.71  ? 25  ASN A CA   1 
ATOM   370   C C    . ASN A 1 25  ? 2.441   14.583  51.210  1.00 75.99  ? 25  ASN A C    1 
ATOM   371   O O    . ASN A 1 25  ? 1.528   14.767  50.402  1.00 80.32  ? 25  ASN A O    1 
ATOM   372   C CB   . ASN A 1 25  ? 3.848   16.208  49.897  1.00 77.88  ? 25  ASN A CB   1 
ATOM   373   C CG   . ASN A 1 25  ? 5.079   17.107  49.886  1.00 77.39  ? 25  ASN A CG   1 
ATOM   374   O OD1  . ASN A 1 25  ? 5.999   16.921  49.089  1.00 74.70  ? 25  ASN A OD1  1 
ATOM   375   N ND2  . ASN A 1 25  ? 5.103   18.080  50.785  1.00 84.64  ? 25  ASN A ND2  1 
ATOM   376   H H    . ASN A 1 25  ? 5.258   15.044  52.306  1.00 89.71  ? 25  ASN A H    1 
ATOM   377   H HA   . ASN A 1 25  ? 3.491   16.166  51.917  1.00 90.86  ? 25  ASN A HA   1 
ATOM   378   H HB2  . ASN A 1 25  ? 3.952   15.545  49.196  1.00 93.45  ? 25  ASN A HB2  1 
ATOM   379   H HB3  . ASN A 1 25  ? 3.070   16.759  49.720  1.00 93.45  ? 25  ASN A HB3  1 
ATOM   380   H HD21 . ASN A 1 25  ? 4.447   18.175  51.333  1.00 101.57 ? 25  ASN A HD21 1 
ATOM   381   H HD22 . ASN A 1 25  ? 5.775   18.615  50.821  1.00 101.57 ? 25  ASN A HD22 1 
ATOM   382   N N    . PHE A 1 26  ? 2.414   13.602  52.102  1.00 78.29  ? 26  PHE A N    1 
ATOM   383   C CA   . PHE A 1 26  ? 1.346   12.617  52.193  1.00 81.67  ? 26  PHE A CA   1 
ATOM   384   C C    . PHE A 1 26  ? 0.825   12.595  53.621  1.00 82.16  ? 26  PHE A C    1 
ATOM   385   O O    . PHE A 1 26  ? 1.593   12.785  54.569  1.00 80.64  ? 26  PHE A O    1 
ATOM   386   C CB   . PHE A 1 26  ? 1.868   11.236  51.773  1.00 79.93  ? 26  PHE A CB   1 
ATOM   387   C CG   . PHE A 1 26  ? 0.800   10.191  51.632  1.00 82.39  ? 26  PHE A CG   1 
ATOM   388   C CD1  . PHE A 1 26  ? 0.095   10.048  50.447  1.00 84.85  ? 26  PHE A CD1  1 
ATOM   389   C CD2  . PHE A 1 26  ? 0.517   9.336   52.679  1.00 84.90  ? 26  PHE A CD2  1 
ATOM   390   C CE1  . PHE A 1 26  ? -0.882  9.078   50.320  1.00 87.23  ? 26  PHE A CE1  1 
ATOM   391   C CE2  . PHE A 1 26  ? -0.456  8.364   52.557  1.00 88.17  ? 26  PHE A CE2  1 
ATOM   392   C CZ   . PHE A 1 26  ? -1.156  8.234   51.378  1.00 86.71  ? 26  PHE A CZ   1 
ATOM   393   H H    . PHE A 1 26  ? 3.029   13.481  52.690  1.00 93.95  ? 26  PHE A H    1 
ATOM   394   H HA   . PHE A 1 26  ? 0.603   12.845  51.613  1.00 98.00  ? 26  PHE A HA   1 
ATOM   395   H HB2  . PHE A 1 26  ? 2.312   11.320  50.914  1.00 95.92  ? 26  PHE A HB2  1 
ATOM   396   H HB3  . PHE A 1 26  ? 2.497   10.925  52.443  1.00 95.92  ? 26  PHE A HB3  1 
ATOM   397   H HD1  . PHE A 1 26  ? 0.280   10.611  49.730  1.00 101.83 ? 26  PHE A HD1  1 
ATOM   398   H HD2  . PHE A 1 26  ? 0.989   9.415   53.477  1.00 101.88 ? 26  PHE A HD2  1 
ATOM   399   H HE1  . PHE A 1 26  ? -1.354  8.994   49.523  1.00 104.67 ? 26  PHE A HE1  1 
ATOM   400   H HE2  . PHE A 1 26  ? -0.639  7.796   53.271  1.00 105.80 ? 26  PHE A HE2  1 
ATOM   401   H HZ   . PHE A 1 26  ? -1.812  7.580   51.294  1.00 104.05 ? 26  PHE A HZ   1 
ATOM   402   N N    . ASP A 1 27  ? -0.484  12.388  53.772  1.00 84.37  ? 27  ASP A N    1 
ATOM   403   C CA   . ASP A 1 27  ? -1.070  12.244  55.100  1.00 85.83  ? 27  ASP A CA   1 
ATOM   404   C C    . ASP A 1 27  ? -0.395  11.094  55.836  1.00 86.24  ? 27  ASP A C    1 
ATOM   405   O O    . ASP A 1 27  ? -0.644  9.924   55.525  1.00 87.28  ? 27  ASP A O    1 
ATOM   406   C CB   . ASP A 1 27  ? -2.577  12.003  55.017  1.00 85.19  ? 27  ASP A CB   1 
ATOM   407   C CG   . ASP A 1 27  ? -3.195  11.737  56.375  1.00 92.43  ? 27  ASP A CG   1 
ATOM   408   O OD1  . ASP A 1 27  ? -2.764  12.368  57.368  1.00 93.06  ? 27  ASP A OD1  1 
ATOM   409   O OD2  . ASP A 1 27  ? -4.114  10.896  56.452  1.00 96.63  ? 27  ASP A OD2  1 
ATOM   410   H H    . ASP A 1 27  ? -1.047  12.329  53.125  1.00 101.24 ? 27  ASP A H    1 
ATOM   411   H HA   . ASP A 1 27  ? -0.935  13.066  55.597  1.00 103.00 ? 27  ASP A HA   1 
ATOM   412   H HB2  . ASP A 1 27  ? -3.004  12.788  54.640  1.00 102.23 ? 27  ASP A HB2  1 
ATOM   413   H HB3  . ASP A 1 27  ? -2.744  11.232  54.453  1.00 102.23 ? 27  ASP A HB3  1 
ATOM   414   N N    . ILE A 1 28  ? 0.461   11.413  56.811  1.00 86.06  ? 28  ILE A N    1 
ATOM   415   C CA   . ILE A 1 28  ? 1.233   10.382  57.494  1.00 88.26  ? 28  ILE A CA   1 
ATOM   416   C C    . ILE A 1 28  ? 0.341   9.425   58.270  1.00 88.75  ? 28  ILE A C    1 
ATOM   417   O O    . ILE A 1 28  ? 0.786   8.337   58.655  1.00 88.23  ? 28  ILE A O    1 
ATOM   418   C CB   . ILE A 1 28  ? 2.284   11.033  58.421  1.00 87.32  ? 28  ILE A CB   1 
ATOM   419   C CG1  . ILE A 1 28  ? 1.619   11.804  59.561  1.00 87.91  ? 28  ILE A CG1  1 
ATOM   420   C CG2  . ILE A 1 28  ? 3.186   11.974  57.619  1.00 84.39  ? 28  ILE A CG2  1 
ATOM   421   C CD1  . ILE A 1 28  ? 2.496   11.936  60.797  1.00 87.12  ? 28  ILE A CD1  1 
ATOM   422   H H    . ILE A 1 28  ? 0.609   12.212  57.090  1.00 103.28 ? 28  ILE A H    1 
ATOM   423   H HA   . ILE A 1 28  ? 1.702   9.861   56.823  1.00 105.91 ? 28  ILE A HA   1 
ATOM   424   H HB   . ILE A 1 28  ? 2.818   10.320  58.806  1.00 104.79 ? 28  ILE A HB   1 
ATOM   425   H HG12 . ILE A 1 28  ? 1.406   12.698  59.252  1.00 105.50 ? 28  ILE A HG12 1 
ATOM   426   H HG13 . ILE A 1 28  ? 0.808   11.340  59.821  1.00 105.50 ? 28  ILE A HG13 1 
ATOM   427   H HG21 . ILE A 1 28  ? 3.906   12.284  58.190  1.00 101.27 ? 28  ILE A HG21 1 
ATOM   428   H HG22 . ILE A 1 28  ? 3.550   11.492  56.860  1.00 101.27 ? 28  ILE A HG22 1 
ATOM   429   H HG23 . ILE A 1 28  ? 2.660   12.729  57.311  1.00 101.27 ? 28  ILE A HG23 1 
ATOM   430   H HD11 . ILE A 1 28  ? 2.075   12.549  61.420  1.00 104.55 ? 28  ILE A HD11 1 
ATOM   431   H HD12 . ILE A 1 28  ? 2.596   11.063  61.209  1.00 104.55 ? 28  ILE A HD12 1 
ATOM   432   H HD13 . ILE A 1 28  ? 3.365   12.278  60.533  1.00 104.55 ? 28  ILE A HD13 1 
ATOM   433   N N    . TYR A 1 29  ? -0.910  9.808   58.517  1.00 89.73  ? 29  TYR A N    1 
ATOM   434   C CA   . TYR A 1 29  ? -1.867  8.968   59.222  1.00 91.68  ? 29  TYR A CA   1 
ATOM   435   C C    . TYR A 1 29  ? -2.946  8.430   58.290  1.00 92.22  ? 29  TYR A C    1 
ATOM   436   O O    . TYR A 1 29  ? -4.050  8.109   58.742  1.00 96.91  ? 29  TYR A O    1 
ATOM   437   C CB   . TYR A 1 29  ? -2.499  9.747   60.375  1.00 92.40  ? 29  TYR A CB   1 
ATOM   438   C CG   . TYR A 1 29  ? -1.498  10.264  61.383  1.00 92.50  ? 29  TYR A CG   1 
ATOM   439   C CD1  . TYR A 1 29  ? -0.644  9.394   62.052  1.00 94.95  ? 29  TYR A CD1  1 
ATOM   440   C CD2  . TYR A 1 29  ? -1.405  11.619  61.669  1.00 92.66  ? 29  TYR A CD2  1 
ATOM   441   C CE1  . TYR A 1 29  ? 0.276   9.860   62.975  1.00 97.21  ? 29  TYR A CE1  1 
ATOM   442   C CE2  . TYR A 1 29  ? -0.491  12.094  62.594  1.00 91.49  ? 29  TYR A CE2  1 
ATOM   443   C CZ   . TYR A 1 29  ? 0.347   11.212  63.242  1.00 94.36  ? 29  TYR A CZ   1 
ATOM   444   O OH   . TYR A 1 29  ? 1.257   11.685  64.160  1.00 96.21  ? 29  TYR A OH   1 
ATOM   445   H H    . TYR A 1 29  ? -1.233  10.568  58.278  1.00 107.67 ? 29  TYR A H    1 
ATOM   446   H HA   . TYR A 1 29  ? -1.397  8.208   59.599  1.00 110.01 ? 29  TYR A HA   1 
ATOM   447   H HB2  . TYR A 1 29  ? -2.974  10.511  60.012  1.00 110.88 ? 29  TYR A HB2  1 
ATOM   448   H HB3  . TYR A 1 29  ? -3.117  9.164   60.844  1.00 110.88 ? 29  TYR A HB3  1 
ATOM   449   H HD1  . TYR A 1 29  ? -0.691  8.482   61.875  1.00 111.19 ? 29  TYR A HD1  1 
ATOM   450   H HD2  . TYR A 1 29  ? -1.967  12.217  61.232  1.00 113.94 ? 29  TYR A HD2  1 
ATOM   451   H HE1  . TYR A 1 29  ? 0.842   9.266   63.413  1.00 109.79 ? 29  TYR A HE1  1 
ATOM   452   H HE2  . TYR A 1 29  ? -0.443  13.005  62.777  1.00 116.65 ? 29  TYR A HE2  1 
ATOM   453   H HH   . TYR A 1 29  ? 1.705   11.048  64.474  1.00 115.45 ? 29  TYR A HH   1 
ATOM   454   N N    . ASP A 1 30  ? -2.651  8.332   56.996  1.00 91.83  ? 30  ASP A N    1 
ATOM   455   C CA   . ASP A 1 30  ? -3.615  7.779   56.055  1.00 95.72  ? 30  ASP A CA   1 
ATOM   456   C C    . ASP A 1 30  ? -3.884  6.315   56.380  1.00 94.83  ? 30  ASP A C    1 
ATOM   457   O O    . ASP A 1 30  ? -2.990  5.580   56.812  1.00 93.21  ? 30  ASP A O    1 
ATOM   458   C CB   . ASP A 1 30  ? -3.098  7.923   54.623  1.00 96.59  ? 30  ASP A CB   1 
ATOM   459   C CG   . ASP A 1 30  ? -4.134  7.520   53.583  1.00 97.98  ? 30  ASP A CG   1 
ATOM   460   O OD1  . ASP A 1 30  ? -4.227  6.314   53.272  1.00 101.56 ? 30  ASP A OD1  1 
ATOM   461   O OD2  . ASP A 1 30  ? -4.851  8.407   53.071  1.00 96.34  ? 30  ASP A OD2  1 
ATOM   462   H H    . ASP A 1 30  ? -1.906  8.576   56.643  1.00 110.19 ? 30  ASP A H    1 
ATOM   463   H HA   . ASP A 1 30  ? -4.451  8.266   56.118  1.00 114.87 ? 30  ASP A HA   1 
ATOM   464   H HB2  . ASP A 1 30  ? -2.858  8.849   54.464  1.00 115.91 ? 30  ASP A HB2  1 
ATOM   465   H HB3  . ASP A 1 30  ? -2.320  7.354   54.508  1.00 115.91 ? 30  ASP A HB3  1 
ATOM   466   N N    . LYS A 1 31  ? -5.134  5.895   56.174  1.00 97.02  ? 31  LYS A N    1 
ATOM   467   C CA   . LYS A 1 31  ? -5.525  4.531   56.515  1.00 96.35  ? 31  LYS A CA   1 
ATOM   468   C C    . LYS A 1 31  ? -4.868  3.514   55.585  1.00 94.48  ? 31  LYS A C    1 
ATOM   469   O O    . LYS A 1 31  ? -4.473  2.428   56.026  1.00 93.16  ? 31  LYS A O    1 
ATOM   470   C CB   . LYS A 1 31  ? -7.054  4.406   56.474  1.00 96.81  ? 31  LYS A CB   1 
ATOM   471   C CG   . LYS A 1 31  ? -7.622  3.954   55.132  1.00 97.85  ? 31  LYS A CG   1 
ATOM   472   C CD   . LYS A 1 31  ? -8.987  4.582   54.821  1.00 100.08 ? 31  LYS A CD   1 
ATOM   473   C CE   . LYS A 1 31  ? -9.317  4.431   53.338  1.00 99.45  ? 31  LYS A CE   1 
ATOM   474   N NZ   . LYS A 1 31  ? -10.597 5.084   52.949  1.00 102.26 ? 31  LYS A NZ   1 
ATOM   475   H H    . LYS A 1 31  ? -5.766  6.375   55.842  1.00 116.43 ? 31  LYS A H    1 
ATOM   476   H HA   . LYS A 1 31  ? -5.232  4.332   57.418  1.00 115.62 ? 31  LYS A HA   1 
ATOM   477   H HB2  . LYS A 1 31  ? -7.328  3.757   57.140  1.00 116.17 ? 31  LYS A HB2  1 
ATOM   478   H HB3  . LYS A 1 31  ? -7.439  5.273   56.676  1.00 116.17 ? 31  LYS A HB3  1 
ATOM   479   H HG2  . LYS A 1 31  ? -7.008  4.209   54.426  1.00 117.42 ? 31  LYS A HG2  1 
ATOM   480   H HG3  . LYS A 1 31  ? -7.732  2.990   55.143  1.00 117.42 ? 31  LYS A HG3  1 
ATOM   481   H HD2  . LYS A 1 31  ? -9.676  4.136   55.338  1.00 120.10 ? 31  LYS A HD2  1 
ATOM   482   H HD3  . LYS A 1 31  ? -8.968  5.527   55.039  1.00 120.10 ? 31  LYS A HD3  1 
ATOM   483   H HE2  . LYS A 1 31  ? -8.606  4.834   52.815  1.00 119.34 ? 31  LYS A HE2  1 
ATOM   484   H HE3  . LYS A 1 31  ? -9.389  3.487   53.126  1.00 119.34 ? 31  LYS A HE3  1 
ATOM   485   H HZ1  . LYS A 1 31  ? -10.747 4.966   52.080  1.00 122.72 ? 31  LYS A HZ1  1 
ATOM   486   H HZ2  . LYS A 1 31  ? -11.271 4.731   53.410  1.00 122.72 ? 31  LYS A HZ2  1 
ATOM   487   H HZ3  . LYS A 1 31  ? -10.557 5.957   53.119  1.00 122.72 ? 31  LYS A HZ3  1 
ATOM   488   N N    . ASN A 1 32  ? -4.723  3.851   54.303  1.00 95.84  ? 32  ASN A N    1 
ATOM   489   C CA   . ASN A 1 32  ? -4.268  2.894   53.299  1.00 94.66  ? 32  ASN A CA   1 
ATOM   490   C C    . ASN A 1 32  ? -2.755  2.713   53.293  1.00 93.04  ? 32  ASN A C    1 
ATOM   491   O O    . ASN A 1 32  ? -2.254  1.901   52.497  1.00 90.16  ? 32  ASN A O    1 
ATOM   492   C CB   . ASN A 1 32  ? -4.729  3.334   51.904  1.00 92.66  ? 32  ASN A CB   1 
ATOM   493   C CG   . ASN A 1 32  ? -6.237  3.420   51.782  1.00 95.22  ? 32  ASN A CG   1 
ATOM   494   O OD1  . ASN A 1 32  ? -6.779  4.453   51.389  1.00 95.76  ? 32  ASN A OD1  1 
ATOM   495   N ND2  . ASN A 1 32  ? -6.922  2.329   52.105  1.00 95.46  ? 32  ASN A ND2  1 
ATOM   496   H H    . ASN A 1 32  ? -4.884  4.635   53.989  1.00 115.01 ? 32  ASN A H    1 
ATOM   497   H HA   . ASN A 1 32  ? -4.672  2.034   53.494  1.00 113.59 ? 32  ASN A HA   1 
ATOM   498   H HB2  . ASN A 1 32  ? -4.362  4.212   51.713  1.00 111.19 ? 32  ASN A HB2  1 
ATOM   499   H HB3  . ASN A 1 32  ? -4.411  2.692   51.250  1.00 111.19 ? 32  ASN A HB3  1 
ATOM   500   H HD21 . ASN A 1 32  ? -7.780  2.329   52.052  1.00 114.56 ? 32  ASN A HD21 1 
ATOM   501   H HD22 . ASN A 1 32  ? -6.507  1.623   52.368  1.00 114.56 ? 32  ASN A HD22 1 
ATOM   502   N N    . ILE A 1 33  ? -2.041  3.445   54.184  1.00 92.88  ? 33  ILE A N    1 
ATOM   503   C CA   . ILE A 1 33  ? -0.580  3.359   54.192  1.00 89.83  ? 33  ILE A CA   1 
ATOM   504   C C    . ILE A 1 33  ? -0.060  1.932   54.055  1.00 88.94  ? 33  ILE A C    1 
ATOM   505   O O    . ILE A 1 33  ? 0.850   1.713   53.254  1.00 86.85  ? 33  ILE A O    1 
ATOM   506   C CB   . ILE A 1 33  ? -0.032  4.085   55.430  1.00 88.72  ? 33  ILE A CB   1 
ATOM   507   C CG1  . ILE A 1 33  ? 0.116   5.579   55.166  1.00 88.83  ? 33  ILE A CG1  1 
ATOM   508   C CG2  . ILE A 1 33  ? 1.297   3.461   55.879  1.00 84.05  ? 33  ILE A CG2  1 
ATOM   509   C CD1  . ILE A 1 33  ? 0.602   6.390   56.350  1.00 86.89  ? 33  ILE A CD1  1 
ATOM   510   H H    . ILE A 1 33  ? -2.377  3.977   54.770  1.00 111.46 ? 33  ILE A H    1 
ATOM   511   H HA   . ILE A 1 33  ? -0.260  3.834   53.409  1.00 107.79 ? 33  ILE A HA   1 
ATOM   512   H HB   . ILE A 1 33  ? -0.672  3.978   56.151  1.00 106.46 ? 33  ILE A HB   1 
ATOM   513   H HG12 . ILE A 1 33  ? 0.755   5.703   54.447  1.00 106.59 ? 33  ILE A HG12 1 
ATOM   514   H HG13 . ILE A 1 33  ? -0.749  5.933   54.906  1.00 106.59 ? 33  ILE A HG13 1 
ATOM   515   H HG21 . ILE A 1 33  ? 1.707   4.036   56.544  1.00 100.86 ? 33  ILE A HG21 1 
ATOM   516   H HG22 . ILE A 1 33  ? 1.123   2.586   56.260  1.00 100.86 ? 33  ILE A HG22 1 
ATOM   517   H HG23 . ILE A 1 33  ? 1.882   3.376   55.109  1.00 100.86 ? 33  ILE A HG23 1 
ATOM   518   H HD11 . ILE A 1 33  ? 0.434   7.330   56.179  1.00 104.26 ? 33  ILE A HD11 1 
ATOM   519   H HD12 . ILE A 1 33  ? 0.122   6.108   57.144  1.00 104.26 ? 33  ILE A HD12 1 
ATOM   520   H HD13 . ILE A 1 33  ? 1.553   6.240   56.467  1.00 104.26 ? 33  ILE A HD13 1 
ATOM   521   N N    . PRO A 1 34  ? -0.551  0.956   54.819  1.00 90.33  ? 34  PRO A N    1 
ATOM   522   C CA   . PRO A 1 34  ? 0.039   -0.383  54.719  1.00 88.32  ? 34  PRO A CA   1 
ATOM   523   C C    . PRO A 1 34  ? -0.218  -1.033  53.373  1.00 88.18  ? 34  PRO A C    1 
ATOM   524   O O    . PRO A 1 34  ? 0.620   -1.814  52.910  1.00 87.01  ? 34  PRO A O    1 
ATOM   525   C CB   . PRO A 1 34  ? -0.630  -1.160  55.864  1.00 86.98  ? 34  PRO A CB   1 
ATOM   526   C CG   . PRO A 1 34  ? -1.605  -0.226  56.524  1.00 88.63  ? 34  PRO A CG   1 
ATOM   527   C CD   . PRO A 1 34  ? -1.754  0.993   55.667  1.00 88.53  ? 34  PRO A CD   1 
ATOM   528   H HA   . PRO A 1 34  ? 0.993   -0.345  54.886  1.00 105.98 ? 34  PRO A HA   1 
ATOM   529   H HB2  . PRO A 1 34  ? -1.092  -1.932  55.502  1.00 104.38 ? 34  PRO A HB2  1 
ATOM   530   H HB3  . PRO A 1 34  ? 0.047   -1.446  56.497  1.00 104.38 ? 34  PRO A HB3  1 
ATOM   531   H HG2  . PRO A 1 34  ? -2.460  -0.675  56.616  1.00 106.35 ? 34  PRO A HG2  1 
ATOM   532   H HG3  . PRO A 1 34  ? -1.264  0.020   57.398  1.00 106.35 ? 34  PRO A HG3  1 
ATOM   533   H HD2  . PRO A 1 34  ? -2.558  0.941   55.128  1.00 106.24 ? 34  PRO A HD2  1 
ATOM   534   H HD3  . PRO A 1 34  ? -1.770  1.798   56.209  1.00 106.24 ? 34  PRO A HD3  1 
ATOM   535   N N    . LYS A 1 35  ? -1.343  -0.727  52.722  1.00 89.21  ? 35  LYS A N    1 
ATOM   536   C CA   . LYS A 1 35  ? -1.638  -1.339  51.430  1.00 89.62  ? 35  LYS A CA   1 
ATOM   537   C C    . LYS A 1 35  ? -0.722  -0.794  50.339  1.00 89.23  ? 35  LYS A C    1 
ATOM   538   O O    . LYS A 1 35  ? -0.093  -1.563  49.604  1.00 88.35  ? 35  LYS A O    1 
ATOM   539   C CB   . LYS A 1 35  ? -3.107  -1.113  51.067  1.00 91.60  ? 35  LYS A CB   1 
ATOM   540   C CG   . LYS A 1 35  ? -4.063  -2.105  51.719  1.00 95.30  ? 35  LYS A CG   1 
ATOM   541   C CD   . LYS A 1 35  ? -5.322  -2.310  50.883  1.00 100.79 ? 35  LYS A CD   1 
ATOM   542   C CE   . LYS A 1 35  ? -5.685  -3.788  50.773  1.00 104.74 ? 35  LYS A CE   1 
ATOM   543   N NZ   . LYS A 1 35  ? -6.726  -4.034  49.731  1.00 104.40 ? 35  LYS A NZ   1 
ATOM   544   H H    . LYS A 1 35  ? -1.941  -0.176  53.003  1.00 107.05 ? 35  LYS A H    1 
ATOM   545   H HA   . LYS A 1 35  ? -1.488  -2.295  51.496  1.00 107.55 ? 35  LYS A HA   1 
ATOM   546   H HB2  . LYS A 1 35  ? -3.366  -0.223  51.352  1.00 109.92 ? 35  LYS A HB2  1 
ATOM   547   H HB3  . LYS A 1 35  ? -3.207  -1.195  50.105  1.00 109.92 ? 35  LYS A HB3  1 
ATOM   548   H HG2  . LYS A 1 35  ? -3.619  -2.962  51.814  1.00 114.36 ? 35  LYS A HG2  1 
ATOM   549   H HG3  . LYS A 1 35  ? -4.327  -1.769  52.589  1.00 114.36 ? 35  LYS A HG3  1 
ATOM   550   H HD2  . LYS A 1 35  ? -6.064  -1.844  51.301  1.00 120.95 ? 35  LYS A HD2  1 
ATOM   551   H HD3  . LYS A 1 35  ? -5.174  -1.964  49.989  1.00 120.95 ? 35  LYS A HD3  1 
ATOM   552   H HE2  . LYS A 1 35  ? -4.892  -4.294  50.534  1.00 125.68 ? 35  LYS A HE2  1 
ATOM   553   H HE3  . LYS A 1 35  ? -6.030  -4.096  51.625  1.00 125.68 ? 35  LYS A HE3  1 
ATOM   554   H HZ1  . LYS A 1 35  ? -6.917  -4.902  49.690  1.00 125.28 ? 35  LYS A HZ1  1 
ATOM   555   H HZ2  . LYS A 1 35  ? -7.468  -3.584  49.930  1.00 125.28 ? 35  LYS A HZ2  1 
ATOM   556   H HZ3  . LYS A 1 35  ? -6.431  -3.765  48.936  1.00 125.28 ? 35  LYS A HZ3  1 
ATOM   557   N N    . LEU A 1 36  ? -0.638  0.531   50.203  1.00 89.12  ? 36  LEU A N    1 
ATOM   558   C CA   . LEU A 1 36  ? 0.241   1.085   49.181  1.00 87.77  ? 36  LEU A CA   1 
ATOM   559   C C    . LEU A 1 36  ? 1.710   0.902   49.542  1.00 87.56  ? 36  LEU A C    1 
ATOM   560   O O    . LEU A 1 36  ? 2.556   0.873   48.643  1.00 88.85  ? 36  LEU A O    1 
ATOM   561   C CB   . LEU A 1 36  ? -0.063  2.564   48.943  1.00 86.91  ? 36  LEU A CB   1 
ATOM   562   C CG   . LEU A 1 36  ? -0.033  3.530   50.119  1.00 87.37  ? 36  LEU A CG   1 
ATOM   563   C CD1  . LEU A 1 36  ? 0.643   4.836   49.735  1.00 84.89  ? 36  LEU A CD1  1 
ATOM   564   C CD2  . LEU A 1 36  ? -1.446  3.805   50.598  1.00 91.38  ? 36  LEU A CD2  1 
ATOM   565   H H    . LEU A 1 36  ? -1.066  1.108   50.676  1.00 106.95 ? 36  LEU A H    1 
ATOM   566   H HA   . LEU A 1 36  ? 0.072   0.623   48.345  1.00 105.33 ? 36  LEU A HA   1 
ATOM   567   H HB2  . LEU A 1 36  ? 0.588   2.894   48.303  1.00 104.29 ? 36  LEU A HB2  1 
ATOM   568   H HB3  . LEU A 1 36  ? -0.955  2.619   48.567  1.00 104.29 ? 36  LEU A HB3  1 
ATOM   569   H HG   . LEU A 1 36  ? 0.475   3.129   50.841  1.00 104.84 ? 36  LEU A HG   1 
ATOM   570   H HD11 . LEU A 1 36  ? 0.641   5.430   50.502  1.00 101.87 ? 36  LEU A HD11 1 
ATOM   571   H HD12 . LEU A 1 36  ? 1.555   4.650   49.463  1.00 101.87 ? 36  LEU A HD12 1 
ATOM   572   H HD13 . LEU A 1 36  ? 0.154   5.241   49.002  1.00 101.87 ? 36  LEU A HD13 1 
ATOM   573   H HD21 . LEU A 1 36  ? -1.413  4.123   51.513  1.00 109.66 ? 36  LEU A HD21 1 
ATOM   574   H HD22 . LEU A 1 36  ? -1.848  4.479   50.027  1.00 109.66 ? 36  LEU A HD22 1 
ATOM   575   H HD23 . LEU A 1 36  ? -1.960  2.983   50.551  1.00 109.66 ? 36  LEU A HD23 1 
ATOM   576   N N    . SER A 1 37  ? 2.029   0.754   50.830  1.00 87.65  ? 37  SER A N    1 
ATOM   577   C CA   . SER A 1 37  ? 3.419   0.552   51.228  1.00 88.65  ? 37  SER A CA   1 
ATOM   578   C C    . SER A 1 37  ? 3.966   -0.759  50.674  1.00 87.12  ? 37  SER A C    1 
ATOM   579   O O    . SER A 1 37  ? 5.077   -0.797  50.126  1.00 86.51  ? 37  SER A O    1 
ATOM   580   C CB   . SER A 1 37  ? 3.535   0.586   52.753  1.00 85.59  ? 37  SER A CB   1 
ATOM   581   O OG   . SER A 1 37  ? 3.748   1.909   53.210  1.00 82.09  ? 37  SER A OG   1 
ATOM   582   H H    . SER A 1 37  ? 1.468   0.766   51.481  1.00 105.18 ? 37  SER A H    1 
ATOM   583   H HA   . SER A 1 37  ? 3.955   1.275   50.869  1.00 106.38 ? 37  SER A HA   1 
ATOM   584   H HB2  . SER A 1 37  ? 2.714   0.246   53.141  1.00 102.70 ? 37  SER A HB2  1 
ATOM   585   H HB3  . SER A 1 37  ? 4.285   0.034   53.026  1.00 102.70 ? 37  SER A HB3  1 
ATOM   586   H HG   . SER A 1 37  ? 3.112   2.402   52.968  1.00 98.51  ? 37  SER A HG   1 
ATOM   587   N N    . GLU A 1 38  ? 3.208   -1.853  50.815  1.00 85.88  ? 38  GLU A N    1 
ATOM   588   C CA   . GLU A 1 38  ? 3.655   -3.110  50.223  1.00 89.74  ? 38  GLU A CA   1 
ATOM   589   C C    . GLU A 1 38  ? 3.752   -3.005  48.706  1.00 87.87  ? 38  GLU A C    1 
ATOM   590   O O    . GLU A 1 38  ? 4.610   -3.650  48.091  1.00 85.17  ? 38  GLU A O    1 
ATOM   591   C CB   . GLU A 1 38  ? 2.722   -4.254  50.619  1.00 87.49  ? 38  GLU A CB   1 
ATOM   592   C CG   . GLU A 1 38  ? 1.247   -3.980  50.405  1.00 88.07  ? 38  GLU A CG   1 
ATOM   593   C CD   . GLU A 1 38  ? 0.440   -5.249  50.201  1.00 92.93  ? 38  GLU A CD   1 
ATOM   594   O OE1  . GLU A 1 38  ? 0.630   -6.214  50.976  1.00 96.13  ? 38  GLU A OE1  1 
ATOM   595   O OE2  . GLU A 1 38  ? -0.383  -5.282  49.265  1.00 98.96  ? 38  GLU A OE2  1 
ATOM   596   H H    . GLU A 1 38  ? 2.458   -1.890  51.234  1.00 103.06 ? 38  GLU A H    1 
ATOM   597   H HA   . GLU A 1 38  ? 4.536   -3.320  50.571  1.00 107.69 ? 38  GLU A HA   1 
ATOM   598   H HB2  . GLU A 1 38  ? 2.952   -5.035  50.092  1.00 104.98 ? 38  GLU A HB2  1 
ATOM   599   H HB3  . GLU A 1 38  ? 2.849   -4.441  51.563  1.00 104.98 ? 38  GLU A HB3  1 
ATOM   600   H HG2  . GLU A 1 38  ? 0.894   -3.521  51.184  1.00 105.68 ? 38  GLU A HG2  1 
ATOM   601   H HG3  . GLU A 1 38  ? 1.140   -3.425  49.617  1.00 105.68 ? 38  GLU A HG3  1 
ATOM   602   N N    . GLU A 1 39  ? 2.888   -2.196  48.086  1.00 87.70  ? 39  GLU A N    1 
ATOM   603   C CA   . GLU A 1 39  ? 2.991   -1.972  46.648  1.00 88.59  ? 39  GLU A CA   1 
ATOM   604   C C    . GLU A 1 39  ? 4.275   -1.231  46.300  1.00 85.75  ? 39  GLU A C    1 
ATOM   605   O O    . GLU A 1 39  ? 4.978   -1.603  45.356  1.00 88.87  ? 39  GLU A O    1 
ATOM   606   C CB   . GLU A 1 39  ? 1.774   -1.195  46.153  1.00 90.07  ? 39  GLU A CB   1 
ATOM   607   C CG   . GLU A 1 39  ? 0.529   -2.046  45.974  1.00 92.96  ? 39  GLU A CG   1 
ATOM   608   C CD   . GLU A 1 39  ? 0.601   -2.930  44.742  1.00 101.29 ? 39  GLU A CD   1 
ATOM   609   O OE1  . GLU A 1 39  ? 1.219   -2.506  43.736  1.00 98.78  ? 39  GLU A OE1  1 
ATOM   610   O OE2  . GLU A 1 39  ? 0.036   -4.046  44.777  1.00 104.12 ? 39  GLU A OE2  1 
ATOM   611   H H    . GLU A 1 39  ? 2.246   -1.773  48.470  1.00 105.24 ? 39  GLU A H    1 
ATOM   612   H HA   . GLU A 1 39  ? 3.004   -2.830  46.195  1.00 106.31 ? 39  GLU A HA   1 
ATOM   613   H HB2  . GLU A 1 39  ? 1.566   -0.500  46.797  1.00 108.08 ? 39  GLU A HB2  1 
ATOM   614   H HB3  . GLU A 1 39  ? 1.987   -0.798  45.294  1.00 108.08 ? 39  GLU A HB3  1 
ATOM   615   H HG2  . GLU A 1 39  ? 0.423   -2.619  46.749  1.00 111.54 ? 39  GLU A HG2  1 
ATOM   616   H HG3  . GLU A 1 39  ? -0.242  -1.465  45.882  1.00 111.54 ? 39  GLU A HG3  1 
ATOM   617   N N    . ILE A 1 40  ? 4.600   -0.186  47.063  1.00 85.02  ? 40  ILE A N    1 
ATOM   618   C CA   . ILE A 1 40  ? 5.816   0.577   46.825  1.00 86.12  ? 40  ILE A CA   1 
ATOM   619   C C    . ILE A 1 40  ? 7.060   -0.298  46.933  1.00 84.98  ? 40  ILE A C    1 
ATOM   620   O O    . ILE A 1 40  ? 8.102   0.046   46.369  1.00 84.82  ? 40  ILE A O    1 
ATOM   621   C CB   . ILE A 1 40  ? 5.886   1.764   47.816  1.00 86.28  ? 40  ILE A CB   1 
ATOM   622   C CG1  . ILE A 1 40  ? 4.739   2.764   47.589  1.00 85.45  ? 40  ILE A CG1  1 
ATOM   623   C CG2  . ILE A 1 40  ? 7.240   2.486   47.733  1.00 83.13  ? 40  ILE A CG2  1 
ATOM   624   C CD1  . ILE A 1 40  ? 4.183   2.805   46.188  1.00 87.74  ? 40  ILE A CD1  1 
ATOM   625   H H    . ILE A 1 40  ? 4.131   0.099   47.725  1.00 102.03 ? 40  ILE A H    1 
ATOM   626   H HA   . ILE A 1 40  ? 5.787   0.932   45.922  1.00 103.35 ? 40  ILE A HA   1 
ATOM   627   H HB   . ILE A 1 40  ? 5.790   1.389   48.705  1.00 103.54 ? 40  ILE A HB   1 
ATOM   628   H HG12 . ILE A 1 40  ? 4.008   2.530   48.183  1.00 102.55 ? 40  ILE A HG12 1 
ATOM   629   H HG13 . ILE A 1 40  ? 5.064   3.654   47.797  1.00 102.55 ? 40  ILE A HG13 1 
ATOM   630   H HG21 . ILE A 1 40  ? 7.245   3.221   48.366  1.00 99.76  ? 40  ILE A HG21 1 
ATOM   631   H HG22 . ILE A 1 40  ? 7.946   1.857   47.949  1.00 99.76  ? 40  ILE A HG22 1 
ATOM   632   H HG23 . ILE A 1 40  ? 7.363   2.824   46.832  1.00 99.76  ? 40  ILE A HG23 1 
ATOM   633   H HD11 . ILE A 1 40  ? 3.469   3.462   46.150  1.00 105.29 ? 40  ILE A HD11 1 
ATOM   634   H HD12 . ILE A 1 40  ? 4.892   3.052   45.573  1.00 105.29 ? 40  ILE A HD12 1 
ATOM   635   H HD13 . ILE A 1 40  ? 3.837   1.928   45.959  1.00 105.29 ? 40  ILE A HD13 1 
ATOM   636   N N    . MET A 1 41  ? 6.981   -1.429  47.644  1.00 85.65  ? 41  MET A N    1 
ATOM   637   C CA   . MET A 1 41  ? 8.168   -2.213  47.968  1.00 84.66  ? 41  MET A CA   1 
ATOM   638   C C    . MET A 1 41  ? 8.439   -3.367  47.011  1.00 83.69  ? 41  MET A C    1 
ATOM   639   O O    . MET A 1 41  ? 9.580   -3.838  46.950  1.00 85.54  ? 41  MET A O    1 
ATOM   640   C CB   . MET A 1 41  ? 8.052   -2.803  49.379  1.00 85.19  ? 41  MET A CB   1 
ATOM   641   C CG   . MET A 1 41  ? 8.149   -1.807  50.512  1.00 83.47  ? 41  MET A CG   1 
ATOM   642   S SD   . MET A 1 41  ? 7.391   -2.494  51.986  1.00 88.28  ? 41  MET A SD   1 
ATOM   643   C CE   . MET A 1 41  ? 8.800   -3.302  52.748  1.00 82.79  ? 41  MET A CE   1 
ATOM   644   H H    . MET A 1 41  ? 6.248   -1.760  47.948  1.00 102.78 ? 41  MET A H    1 
ATOM   645   H HA   . MET A 1 41  ? 8.923   -1.605  47.944  1.00 101.60 ? 41  MET A HA   1 
ATOM   646   H HB2  . MET A 1 41  ? 7.191   -3.244  49.456  1.00 102.23 ? 41  MET A HB2  1 
ATOM   647   H HB3  . MET A 1 41  ? 8.766   -3.448  49.500  1.00 102.23 ? 41  MET A HB3  1 
ATOM   648   H HG2  . MET A 1 41  ? 9.081   -1.615  50.700  1.00 100.16 ? 41  MET A HG2  1 
ATOM   649   H HG3  . MET A 1 41  ? 7.683   -0.991  50.272  1.00 100.16 ? 41  MET A HG3  1 
ATOM   650   H HE1  . MET A 1 41  ? 8.565   -3.556  53.655  1.00 99.35  ? 41  MET A HE1  1 
ATOM   651   H HE2  . MET A 1 41  ? 9.029   -4.091  52.232  1.00 99.35  ? 41  MET A HE2  1 
ATOM   652   H HE3  . MET A 1 41  ? 9.549   -2.686  52.761  1.00 99.35  ? 41  MET A HE3  1 
ATOM   653   N N    . LYS A 1 42  ? 7.428   -3.848  46.290  1.00 85.44  ? 42  LYS A N    1 
ATOM   654   C CA   . LYS A 1 42  ? 7.603   -5.005  45.428  1.00 84.58  ? 42  LYS A CA   1 
ATOM   655   C C    . LYS A 1 42  ? 8.708   -4.755  44.402  1.00 83.89  ? 42  LYS A C    1 
ATOM   656   O O    . LYS A 1 42  ? 9.058   -3.612  44.081  1.00 84.47  ? 42  LYS A O    1 
ATOM   657   C CB   . LYS A 1 42  ? 6.297   -5.334  44.703  1.00 84.63  ? 42  LYS A CB   1 
ATOM   658   C CG   . LYS A 1 42  ? 5.436   -6.432  45.340  1.00 86.71  ? 42  LYS A CG   1 
ATOM   659   C CD   . LYS A 1 42  ? 6.205   -7.732  45.641  1.00 88.72  ? 42  LYS A CD   1 
ATOM   660   C CE   . LYS A 1 42  ? 6.769   -8.389  44.387  1.00 88.01  ? 42  LYS A CE   1 
ATOM   661   N NZ   . LYS A 1 42  ? 5.777   -9.277  43.720  1.00 90.28  ? 42  LYS A NZ   1 
ATOM   662   H H    . LYS A 1 42  ? 6.632   -3.521  46.285  1.00 102.53 ? 42  LYS A H    1 
ATOM   663   H HA   . LYS A 1 42  ? 7.856   -5.769  45.969  1.00 101.49 ? 42  LYS A HA   1 
ATOM   664   H HB2  . LYS A 1 42  ? 5.758   -4.529  44.670  1.00 101.56 ? 42  LYS A HB2  1 
ATOM   665   H HB3  . LYS A 1 42  ? 6.514   -5.625  43.803  1.00 101.56 ? 42  LYS A HB3  1 
ATOM   666   H HG2  . LYS A 1 42  ? 5.077   -6.101  46.178  1.00 104.04 ? 42  LYS A HG2  1 
ATOM   667   H HG3  . LYS A 1 42  ? 4.712   -6.652  44.733  1.00 104.04 ? 42  LYS A HG3  1 
ATOM   668   H HD2  . LYS A 1 42  ? 6.946   -7.531  46.233  1.00 106.46 ? 42  LYS A HD2  1 
ATOM   669   H HD3  . LYS A 1 42  ? 5.604   -8.364  46.065  1.00 106.46 ? 42  LYS A HD3  1 
ATOM   670   H HE2  . LYS A 1 42  ? 7.028   -7.699  43.756  1.00 105.60 ? 42  LYS A HE2  1 
ATOM   671   H HE3  . LYS A 1 42  ? 7.540   -8.925  44.628  1.00 105.60 ? 42  LYS A HE3  1 
ATOM   672   H HZ1  . LYS A 1 42  ? 6.142   -9.655  43.001  1.00 108.34 ? 42  LYS A HZ1  1 
ATOM   673   H HZ2  . LYS A 1 42  ? 5.515   -9.916  44.281  1.00 108.34 ? 42  LYS A HZ2  1 
ATOM   674   H HZ3  . LYS A 1 42  ? 5.066   -8.804  43.468  1.00 108.34 ? 42  LYS A HZ3  1 
ATOM   675   N N    . GLU A 1 43  ? 9.266   -5.855  43.884  1.00 84.64  ? 43  GLU A N    1 
ATOM   676   C CA   . GLU A 1 43  ? 10.230  -5.748  42.792  1.00 90.49  ? 43  GLU A CA   1 
ATOM   677   C C    . GLU A 1 43  ? 9.577   -5.208  41.525  1.00 86.67  ? 43  GLU A C    1 
ATOM   678   O O    . GLU A 1 43  ? 10.236  -4.526  40.731  1.00 84.68  ? 43  GLU A O    1 
ATOM   679   C CB   . GLU A 1 43  ? 10.879  -7.107  42.520  1.00 91.42  ? 43  GLU A CB   1 
ATOM   680   C CG   . GLU A 1 43  ? 10.078  -8.021  41.608  1.00 95.08  ? 43  GLU A CG   1 
ATOM   681   C CD   . GLU A 1 43  ? 10.773  -9.354  41.360  1.00 100.77 ? 43  GLU A CD   1 
ATOM   682   O OE1  . GLU A 1 43  ? 12.021  -9.376  41.317  1.00 103.88 ? 43  GLU A OE1  1 
ATOM   683   O OE2  . GLU A 1 43  ? 10.069  -10.377 41.206  1.00 104.79 ? 43  GLU A OE2  1 
ATOM   684   H H    . GLU A 1 43  ? 9.104   -6.659  44.143  1.00 101.57 ? 43  GLU A H    1 
ATOM   685   H HA   . GLU A 1 43  ? 10.932  -5.133  43.057  1.00 108.59 ? 43  GLU A HA   1 
ATOM   686   H HB2  . GLU A 1 43  ? 11.741  -6.958  42.101  1.00 109.70 ? 43  GLU A HB2  1 
ATOM   687   H HB3  . GLU A 1 43  ? 10.996  -7.567  43.366  1.00 109.70 ? 43  GLU A HB3  1 
ATOM   688   H HG2  . GLU A 1 43  ? 9.217   -8.202  42.017  1.00 114.09 ? 43  GLU A HG2  1 
ATOM   689   H HG3  . GLU A 1 43  ? 9.952   -7.583  40.751  1.00 114.09 ? 43  GLU A HG3  1 
ATOM   690   N N    . THR A 1 44  ? 8.294   -5.503  41.320  1.00 85.78  ? 44  THR A N    1 
ATOM   691   C CA   . THR A 1 44  ? 7.532   -5.012  40.178  1.00 82.94  ? 44  THR A CA   1 
ATOM   692   C C    . THR A 1 44  ? 7.151   -3.544  40.311  1.00 82.65  ? 44  THR A C    1 
ATOM   693   O O    . THR A 1 44  ? 6.331   -3.052  39.526  1.00 83.96  ? 44  THR A O    1 
ATOM   694   C CB   . THR A 1 44  ? 6.271   -5.857  39.995  1.00 82.90  ? 44  THR A CB   1 
ATOM   695   O OG1  . THR A 1 44  ? 5.396   -5.661  41.112  1.00 88.41  ? 44  THR A OG1  1 
ATOM   696   C CG2  . THR A 1 44  ? 6.632   -7.331  39.894  1.00 85.82  ? 44  THR A CG2  1 
ATOM   697   H H    . THR A 1 44  ? 7.831   -6.002  41.846  1.00 102.94 ? 44  THR A H    1 
ATOM   698   H HA   . THR A 1 44  ? 8.075   -5.104  39.380  1.00 99.52  ? 44  THR A HA   1 
ATOM   699   H HB   . THR A 1 44  ? 5.819   -5.593  39.178  1.00 99.48  ? 44  THR A HB   1 
ATOM   700   H HG1  . THR A 1 44  ? 5.757   -5.949  41.814  1.00 106.09 ? 44  THR A HG1  1 
ATOM   701   H HG21 . THR A 1 44  ? 5.829   -7.862  39.772  1.00 102.99 ? 44  THR A HG21 1 
ATOM   702   H HG22 . THR A 1 44  ? 7.223   -7.477  39.139  1.00 102.99 ? 44  THR A HG22 1 
ATOM   703   H HG23 . THR A 1 44  ? 7.079   -7.620  40.705  1.00 102.99 ? 44  THR A HG23 1 
ATOM   704   N N    . ASN A 1 45  ? 7.714   -2.857  41.297  1.00 82.45  ? 45  ASN A N    1 
ATOM   705   C CA   . ASN A 1 45  ? 7.579   -1.413  41.470  1.00 80.95  ? 45  ASN A CA   1 
ATOM   706   C C    . ASN A 1 45  ? 8.973   -0.906  41.833  1.00 79.88  ? 45  ASN A C    1 
ATOM   707   O O    . ASN A 1 45  ? 9.984   -1.532  41.490  1.00 78.55  ? 45  ASN A O    1 
ATOM   708   C CB   . ASN A 1 45  ? 6.501   -1.104  42.520  1.00 81.53  ? 45  ASN A CB   1 
ATOM   709   C CG   . ASN A 1 45  ? 5.849   0.245   42.305  1.00 82.29  ? 45  ASN A CG   1 
ATOM   710   O OD1  . ASN A 1 45  ? 6.146   1.202   43.011  1.00 81.62  ? 45  ASN A OD1  1 
ATOM   711   N ND2  . ASN A 1 45  ? 4.961   0.330   41.320  1.00 87.65  ? 45  ASN A ND2  1 
ATOM   712   H H    . ASN A 1 45  ? 8.201   -3.219  41.906  1.00 98.94  ? 45  ASN A H    1 
ATOM   713   H HA   . ASN A 1 45  ? 7.300   -0.996  40.640  1.00 97.14  ? 45  ASN A HA   1 
ATOM   714   H HB2  . ASN A 1 45  ? 5.810   -1.783  42.472  1.00 97.84  ? 45  ASN A HB2  1 
ATOM   715   H HB3  . ASN A 1 45  ? 6.907   -1.105  43.401  1.00 97.84  ? 45  ASN A HB3  1 
ATOM   716   H HD21 . ASN A 1 45  ? 4.783   -0.362  40.841  1.00 105.18 ? 45  ASN A HD21 1 
ATOM   717   H HD22 . ASN A 1 45  ? 4.565   1.076   41.161  1.00 105.18 ? 45  ASN A HD22 1 
ATOM   718   N N    . LEU A 1 46  ? 9.058   0.234   42.523  1.00 79.25  ? 46  LEU A N    1 
ATOM   719   C CA   . LEU A 1 46  ? 10.315  0.585   43.175  1.00 76.36  ? 46  LEU A CA   1 
ATOM   720   C C    . LEU A 1 46  ? 10.594  -0.469  44.241  1.00 81.50  ? 46  LEU A C    1 
ATOM   721   O O    . LEU A 1 46  ? 9.692   -0.882  44.973  1.00 84.37  ? 46  LEU A O    1 
ATOM   722   C CB   . LEU A 1 46  ? 10.250  1.980   43.795  1.00 76.96  ? 46  LEU A CB   1 
ATOM   723   C CG   . LEU A 1 46  ? 11.401  2.944   43.479  1.00 76.82  ? 46  LEU A CG   1 
ATOM   724   C CD1  . LEU A 1 46  ? 11.526  3.156   41.965  1.00 75.77  ? 46  LEU A CD1  1 
ATOM   725   C CD2  . LEU A 1 46  ? 11.223  4.299   44.161  1.00 72.64  ? 46  LEU A CD2  1 
ATOM   726   H H    . LEU A 1 46  ? 8.420   0.803   42.625  1.00 95.10  ? 46  LEU A H    1 
ATOM   727   H HA   . LEU A 1 46  ? 11.041  0.610   42.532  1.00 91.63  ? 46  LEU A HA   1 
ATOM   728   H HB2  . LEU A 1 46  ? 9.434   2.404   43.485  1.00 92.36  ? 46  LEU A HB2  1 
ATOM   729   H HB3  . LEU A 1 46  ? 10.225  1.876   44.759  1.00 92.36  ? 46  LEU A HB3  1 
ATOM   730   H HG   . LEU A 1 46  ? 12.216  2.543   43.820  1.00 92.18  ? 46  LEU A HG   1 
ATOM   731   H HD11 . LEU A 1 46  ? 12.262  3.763   41.791  1.00 90.93  ? 46  LEU A HD11 1 
ATOM   732   H HD12 . LEU A 1 46  ? 11.693  2.301   41.539  1.00 90.93  ? 46  LEU A HD12 1 
ATOM   733   H HD13 . LEU A 1 46  ? 10.698  3.536   41.630  1.00 90.93  ? 46  LEU A HD13 1 
ATOM   734   H HD21 . LEU A 1 46  ? 11.968  4.872   43.923  1.00 87.17  ? 46  LEU A HD21 1 
ATOM   735   H HD22 . LEU A 1 46  ? 10.391  4.696   43.861  1.00 87.17  ? 46  LEU A HD22 1 
ATOM   736   H HD23 . LEU A 1 46  ? 11.200  4.168   45.122  1.00 87.17  ? 46  LEU A HD23 1 
ATOM   737   N N    . TYR A 1 47  ? 11.829  -0.951  44.299  1.00 84.00  ? 47  TYR A N    1 
ATOM   738   C CA   . TYR A 1 47  ? 12.166  -1.929  45.328  1.00 85.37  ? 47  TYR A CA   1 
ATOM   739   C C    . TYR A 1 47  ? 12.327  -1.229  46.673  1.00 77.98  ? 47  TYR A C    1 
ATOM   740   O O    . TYR A 1 47  ? 12.569  -0.024  46.742  1.00 72.10  ? 47  TYR A O    1 
ATOM   741   C CB   . TYR A 1 47  ? 13.436  -2.692  44.948  1.00 83.79  ? 47  TYR A CB   1 
ATOM   742   C CG   . TYR A 1 47  ? 13.782  -3.800  45.908  1.00 85.21  ? 47  TYR A CG   1 
ATOM   743   C CD1  . TYR A 1 47  ? 12.970  -4.917  46.029  1.00 88.46  ? 47  TYR A CD1  1 
ATOM   744   C CD2  . TYR A 1 47  ? 14.913  -3.720  46.705  1.00 86.30  ? 47  TYR A CD2  1 
ATOM   745   C CE1  . TYR A 1 47  ? 13.281  -5.932  46.917  1.00 92.37  ? 47  TYR A CE1  1 
ATOM   746   C CE2  . TYR A 1 47  ? 15.231  -4.725  47.601  1.00 92.04  ? 47  TYR A CE2  1 
ATOM   747   C CZ   . TYR A 1 47  ? 14.416  -5.830  47.703  1.00 93.47  ? 47  TYR A CZ   1 
ATOM   748   O OH   . TYR A 1 47  ? 14.744  -6.827  48.601  1.00 93.12  ? 47  TYR A OH   1 
ATOM   749   H H    . TYR A 1 47  ? 12.472  -0.735  43.771  1.00 100.80 ? 47  TYR A H    1 
ATOM   750   H HA   . TYR A 1 47  ? 11.456  -2.584  45.415  1.00 102.44 ? 47  TYR A HA   1 
ATOM   751   H HB2  . TYR A 1 47  ? 13.312  -3.087  44.071  1.00 100.54 ? 47  TYR A HB2  1 
ATOM   752   H HB3  . TYR A 1 47  ? 14.181  -2.071  44.930  1.00 100.54 ? 47  TYR A HB3  1 
ATOM   753   H HD1  . TYR A 1 47  ? 12.204  -4.985  45.506  1.00 103.56 ? 47  TYR A HD1  1 
ATOM   754   H HD2  . TYR A 1 47  ? 15.469  -2.977  46.637  1.00 106.15 ? 47  TYR A HD2  1 
ATOM   755   H HE1  . TYR A 1 47  ? 12.731  -6.679  46.985  1.00 110.45 ? 47  TYR A HE1  1 
ATOM   756   H HE2  . TYR A 1 47  ? 15.991  -4.655  48.132  1.00 110.85 ? 47  TYR A HE2  1 
ATOM   757   H HH   . TYR A 1 47  ? 14.199  -7.463  48.536  1.00 111.75 ? 47  TYR A HH   1 
ATOM   758   N N    . ALA A 1 48  ? 12.167  -1.999  47.752  1.00 84.99  ? 48  ALA A N    1 
ATOM   759   C CA   . ALA A 1 48  ? 12.353  -1.469  49.097  1.00 80.92  ? 48  ALA A CA   1 
ATOM   760   C C    . ALA A 1 48  ? 12.238  -2.547  50.167  1.00 80.88  ? 48  ALA A C    1 
ATOM   761   O O    . ALA A 1 48  ? 11.407  -3.456  50.057  1.00 80.06  ? 48  ALA A O    1 
ATOM   762   C CB   . ALA A 1 48  ? 11.334  -0.360  49.387  1.00 78.60  ? 48  ALA A CB   1 
ATOM   763   H H    . ALA A 1 48  ? 11.951  -2.831  47.728  1.00 101.99 ? 48  ALA A H    1 
ATOM   764   H HA   . ALA A 1 48  ? 13.250  -1.101  49.141  1.00 97.10  ? 48  ALA A HA   1 
ATOM   765   H HB1  . ALA A 1 48  ? 11.333  -0.173  50.339  1.00 94.32  ? 48  ALA A HB1  1 
ATOM   766   H HB2  . ALA A 1 48  ? 11.585  0.437   48.894  1.00 94.32  ? 48  ALA A HB2  1 
ATOM   767   H HB3  . ALA A 1 48  ? 10.454  -0.658  49.107  1.00 94.32  ? 48  ALA A HB3  1 
ATOM   768   N N    . GLU A 1 49  ? 13.072  -2.438  51.205  1.00 81.44  ? 49  GLU A N    1 
ATOM   769   C CA   . GLU A 1 49  ? 12.969  -3.267  52.400  1.00 79.78  ? 49  GLU A CA   1 
ATOM   770   C C    . GLU A 1 49  ? 12.062  -2.652  53.457  1.00 77.91  ? 49  GLU A C    1 
ATOM   771   O O    . GLU A 1 49  ? 11.541  -3.380  54.305  1.00 77.52  ? 49  GLU A O    1 
ATOM   772   C CB   . GLU A 1 49  ? 14.366  -3.514  52.979  1.00 79.33  ? 49  GLU A CB   1 
ATOM   773   C CG   . GLU A 1 49  ? 15.266  -4.338  52.048  1.00 84.23  ? 49  GLU A CG   1 
ATOM   774   C CD   . GLU A 1 49  ? 16.492  -4.908  52.746  1.00 87.89  ? 49  GLU A CD   1 
ATOM   775   O OE1  . GLU A 1 49  ? 17.119  -4.182  53.544  1.00 93.97  ? 49  GLU A OE1  1 
ATOM   776   O OE2  . GLU A 1 49  ? 16.837  -6.079  52.485  1.00 83.44  ? 49  GLU A OE2  1 
ATOM   777   H H    . GLU A 1 49  ? 13.721  -1.876  51.239  1.00 97.73  ? 49  GLU A H    1 
ATOM   778   H HA   . GLU A 1 49  ? 12.596  -4.132  52.168  1.00 95.73  ? 49  GLU A HA   1 
ATOM   779   H HB2  . GLU A 1 49  ? 14.798  -2.659  53.133  1.00 95.20  ? 49  GLU A HB2  1 
ATOM   780   H HB3  . GLU A 1 49  ? 14.279  -3.998  53.815  1.00 95.20  ? 49  GLU A HB3  1 
ATOM   781   H HG2  . GLU A 1 49  ? 14.753  -5.081  51.692  1.00 101.08 ? 49  GLU A HG2  1 
ATOM   782   H HG3  . GLU A 1 49  ? 15.572  -3.770  51.324  1.00 101.08 ? 49  GLU A HG3  1 
ATOM   783   N N    . GLN A 1 50  ? 11.846  -1.341  53.406  1.00 79.63  ? 50  GLN A N    1 
ATOM   784   C CA   . GLN A 1 50  ? 10.908  -0.666  54.295  1.00 80.31  ? 50  GLN A CA   1 
ATOM   785   C C    . GLN A 1 50  ? 10.557  0.682   53.678  1.00 76.56  ? 50  GLN A C    1 
ATOM   786   O O    . GLN A 1 50  ? 11.199  1.140   52.730  1.00 73.44  ? 50  GLN A O    1 
ATOM   787   C CB   . GLN A 1 50  ? 11.483  -0.497  55.711  1.00 76.76  ? 50  GLN A CB   1 
ATOM   788   C CG   . GLN A 1 50  ? 12.750  0.354   55.783  1.00 78.55  ? 50  GLN A CG   1 
ATOM   789   C CD   . GLN A 1 50  ? 13.563  0.151   57.061  1.00 78.78  ? 50  GLN A CD   1 
ATOM   790   O OE1  . GLN A 1 50  ? 14.665  0.684   57.194  1.00 82.57  ? 50  GLN A OE1  1 
ATOM   791   N NE2  . GLN A 1 50  ? 13.020  -0.612  57.999  1.00 76.53  ? 50  GLN A NE2  1 
ATOM   792   H H    . GLN A 1 50  ? 12.239  -0.810  52.855  1.00 95.56  ? 50  GLN A H    1 
ATOM   793   H HA   . GLN A 1 50  ? 10.098  -1.196  54.366  1.00 96.38  ? 50  GLN A HA   1 
ATOM   794   H HB2  . GLN A 1 50  ? 10.813  -0.071  56.268  1.00 92.11  ? 50  GLN A HB2  1 
ATOM   795   H HB3  . GLN A 1 50  ? 11.699  -1.374  56.064  1.00 92.11  ? 50  GLN A HB3  1 
ATOM   796   H HG2  . GLN A 1 50  ? 13.321  0.127   55.032  1.00 94.27  ? 50  GLN A HG2  1 
ATOM   797   H HG3  . GLN A 1 50  ? 12.500  1.290   55.739  1.00 94.27  ? 50  GLN A HG3  1 
ATOM   798   H HE21 . GLN A 1 50  ? 12.246  -0.965  57.872  1.00 91.83  ? 50  GLN A HE21 1 
ATOM   799   H HE22 . GLN A 1 50  ? 13.442  -0.753  58.735  1.00 91.83  ? 50  GLN A HE22 1 
ATOM   800   N N    . VAL A 1 51  ? 9.523   1.315   54.229  1.00 79.30  ? 51  VAL A N    1 
ATOM   801   C CA   . VAL A 1 51  ? 9.013   2.574   53.695  1.00 75.97  ? 51  VAL A CA   1 
ATOM   802   C C    . VAL A 1 51  ? 8.418   3.385   54.837  1.00 78.61  ? 51  VAL A C    1 
ATOM   803   O O    . VAL A 1 51  ? 7.818   2.834   55.766  1.00 78.74  ? 51  VAL A O    1 
ATOM   804   C CB   . VAL A 1 51  ? 7.975   2.326   52.579  1.00 77.12  ? 51  VAL A CB   1 
ATOM   805   C CG1  . VAL A 1 51  ? 6.958   1.288   53.008  1.00 81.68  ? 51  VAL A CG1  1 
ATOM   806   C CG2  . VAL A 1 51  ? 7.274   3.624   52.197  1.00 78.03  ? 51  VAL A CG2  1 
ATOM   807   H H    . VAL A 1 51  ? 9.096   1.031   54.919  1.00 95.16  ? 51  VAL A H    1 
ATOM   808   H HA   . VAL A 1 51  ? 9.750   3.083   53.323  1.00 91.17  ? 51  VAL A HA   1 
ATOM   809   H HB   . VAL A 1 51  ? 8.442   1.990   51.798  1.00 92.54  ? 51  VAL A HB   1 
ATOM   810   H HG11 . VAL A 1 51  ? 6.249   1.249   52.347  1.00 98.02  ? 51  VAL A HG11 1 
ATOM   811   H HG12 . VAL A 1 51  ? 7.396   0.425   53.074  1.00 98.02  ? 51  VAL A HG12 1 
ATOM   812   H HG13 . VAL A 1 51  ? 6.593   1.541   53.870  1.00 98.02  ? 51  VAL A HG13 1 
ATOM   813   H HG21 . VAL A 1 51  ? 6.819   3.499   51.349  1.00 93.64  ? 51  VAL A HG21 1 
ATOM   814   H HG22 . VAL A 1 51  ? 6.632   3.851   52.887  1.00 93.64  ? 51  VAL A HG22 1 
ATOM   815   H HG23 . VAL A 1 51  ? 7.936   4.329   52.116  1.00 93.64  ? 51  VAL A HG23 1 
ATOM   816   N N    . GLY A 1 52  ? 8.595   4.708   54.761  1.00 77.08  ? 52  GLY A N    1 
ATOM   817   C CA   . GLY A 1 52  ? 8.064   5.603   55.764  1.00 78.53  ? 52  GLY A CA   1 
ATOM   818   C C    . GLY A 1 52  ? 7.470   6.841   55.123  1.00 73.96  ? 52  GLY A C    1 
ATOM   819   O O    . GLY A 1 52  ? 7.681   7.116   53.942  1.00 74.83  ? 52  GLY A O    1 
ATOM   820   H H    . GLY A 1 52  ? 9.024   5.104   54.130  1.00 92.49  ? 52  GLY A H    1 
ATOM   821   H HA2  . GLY A 1 52  ? 7.372   5.152   56.272  1.00 94.23  ? 52  GLY A HA2  1 
ATOM   822   H HA3  . GLY A 1 52  ? 8.773   5.875   56.369  1.00 94.23  ? 52  GLY A HA3  1 
ATOM   823   N N    . PHE A 1 53  ? 6.724   7.589   55.932  1.00 76.74  ? 53  PHE A N    1 
ATOM   824   C CA   . PHE A 1 53  ? 5.989   8.768   55.480  1.00 75.86  ? 53  PHE A CA   1 
ATOM   825   C C    . PHE A 1 53  ? 6.351   9.926   56.400  1.00 76.42  ? 53  PHE A C    1 
ATOM   826   O O    . PHE A 1 53  ? 5.974   9.927   57.576  1.00 80.29  ? 53  PHE A O    1 
ATOM   827   C CB   . PHE A 1 53  ? 4.480   8.499   55.474  1.00 76.19  ? 53  PHE A CB   1 
ATOM   828   C CG   . PHE A 1 53  ? 4.072   7.357   54.570  1.00 76.08  ? 53  PHE A CG   1 
ATOM   829   C CD1  . PHE A 1 53  ? 4.371   6.046   54.906  1.00 76.15  ? 53  PHE A CD1  1 
ATOM   830   C CD2  . PHE A 1 53  ? 3.394   7.598   53.381  1.00 77.96  ? 53  PHE A CD2  1 
ATOM   831   C CE1  . PHE A 1 53  ? 4.001   4.997   54.076  1.00 80.62  ? 53  PHE A CE1  1 
ATOM   832   C CE2  . PHE A 1 53  ? 3.022   6.550   52.549  1.00 78.54  ? 53  PHE A CE2  1 
ATOM   833   C CZ   . PHE A 1 53  ? 3.326   5.251   52.897  1.00 76.95  ? 53  PHE A CZ   1 
ATOM   834   H H    . PHE A 1 53  ? 6.625   7.429   56.771  1.00 92.09  ? 53  PHE A H    1 
ATOM   835   H HA   . PHE A 1 53  ? 6.256   9.006   54.579  1.00 91.03  ? 53  PHE A HA   1 
ATOM   836   H HB2  . PHE A 1 53  ? 4.199   8.279   56.375  1.00 91.42  ? 53  PHE A HB2  1 
ATOM   837   H HB3  . PHE A 1 53  ? 4.022   9.297   55.168  1.00 91.42  ? 53  PHE A HB3  1 
ATOM   838   H HD1  . PHE A 1 53  ? 4.825   5.868   55.698  1.00 91.38  ? 53  PHE A HD1  1 
ATOM   839   H HD2  . PHE A 1 53  ? 3.188   8.472   53.140  1.00 93.55  ? 53  PHE A HD2  1 
ATOM   840   H HE1  . PHE A 1 53  ? 4.209   4.122   54.314  1.00 96.74  ? 53  PHE A HE1  1 
ATOM   841   H HE2  . PHE A 1 53  ? 2.568   6.725   51.757  1.00 94.25  ? 53  PHE A HE2  1 
ATOM   842   H HZ   . PHE A 1 53  ? 3.077   4.549   52.341  1.00 92.35  ? 53  PHE A HZ   1 
ATOM   843   N N    . ILE A 1 54  ? 7.080   10.905  55.870  1.00 75.26  ? 54  ILE A N    1 
ATOM   844   C CA   . ILE A 1 54  ? 7.646   11.975  56.678  1.00 77.88  ? 54  ILE A CA   1 
ATOM   845   C C    . ILE A 1 54  ? 6.729   13.189  56.650  1.00 79.46  ? 54  ILE A C    1 
ATOM   846   O O    . ILE A 1 54  ? 5.985   13.422  55.688  1.00 76.64  ? 54  ILE A O    1 
ATOM   847   C CB   . ILE A 1 54  ? 9.067   12.354  56.205  1.00 77.86  ? 54  ILE A CB   1 
ATOM   848   C CG1  . ILE A 1 54  ? 9.106   12.604  54.694  1.00 74.44  ? 54  ILE A CG1  1 
ATOM   849   C CG2  . ILE A 1 54  ? 10.059  11.252  56.570  1.00 75.39  ? 54  ILE A CG2  1 
ATOM   850   C CD1  . ILE A 1 54  ? 10.419  13.215  54.209  1.00 73.15  ? 54  ILE A CD1  1 
ATOM   851   H H    . ILE A 1 54  ? 7.263   10.970  55.032  1.00 90.31  ? 54  ILE A H    1 
ATOM   852   H HA   . ILE A 1 54  ? 7.696   11.663  57.595  1.00 93.46  ? 54  ILE A HA   1 
ATOM   853   H HB   . ILE A 1 54  ? 9.315   13.176  56.657  1.00 93.44  ? 54  ILE A HB   1 
ATOM   854   H HG12 . ILE A 1 54  ? 8.984   11.759  54.234  1.00 89.33  ? 54  ILE A HG12 1 
ATOM   855   H HG13 . ILE A 1 54  ? 8.390   13.215  54.461  1.00 89.33  ? 54  ILE A HG13 1 
ATOM   856   H HG21 . ILE A 1 54  ? 10.951  11.531  56.311  1.00 90.47  ? 54  ILE A HG21 1 
ATOM   857   H HG22 . ILE A 1 54  ? 10.025  11.101  57.528  1.00 90.47  ? 54  ILE A HG22 1 
ATOM   858   H HG23 . ILE A 1 54  ? 9.817   10.440  56.098  1.00 90.47  ? 54  ILE A HG23 1 
ATOM   859   H HD11 . ILE A 1 54  ? 10.338  13.431  53.267  1.00 87.78  ? 54  ILE A HD11 1 
ATOM   860   H HD12 . ILE A 1 54  ? 10.601  14.020  54.719  1.00 87.78  ? 54  ILE A HD12 1 
ATOM   861   H HD13 . ILE A 1 54  ? 11.134  12.572  54.340  1.00 87.78  ? 54  ILE A HD13 1 
ATOM   862   N N    . LYS A 1 55  ? 6.767   13.959  57.739  1.00 83.21  ? 55  LYS A N    1 
ATOM   863   C CA   . LYS A 1 55  ? 6.009   15.204  57.855  1.00 83.53  ? 55  LYS A CA   1 
ATOM   864   C C    . LYS A 1 55  ? 6.794   16.128  58.768  1.00 84.02  ? 55  LYS A C    1 
ATOM   865   O O    . LYS A 1 55  ? 7.004   15.797  59.936  1.00 84.35  ? 55  LYS A O    1 
ATOM   866   C CB   . LYS A 1 55  ? 4.609   14.965  58.413  1.00 82.39  ? 55  LYS A CB   1 
ATOM   867   C CG   . LYS A 1 55  ? 3.941   16.241  58.904  1.00 84.15  ? 55  LYS A CG   1 
ATOM   868   C CD   . LYS A 1 55  ? 2.429   16.135  58.837  1.00 87.81  ? 55  LYS A CD   1 
ATOM   869   C CE   . LYS A 1 55  ? 1.793   17.455  58.418  1.00 88.34  ? 55  LYS A CE   1 
ATOM   870   N NZ   . LYS A 1 55  ? 0.476   17.225  57.753  1.00 91.26  ? 55  LYS A NZ   1 
ATOM   871   H H    . LYS A 1 55  ? 7.234   13.777  58.438  1.00 99.85  ? 55  LYS A H    1 
ATOM   872   H HA   . LYS A 1 55  ? 5.913   15.611  56.980  1.00 100.23 ? 55  LYS A HA   1 
ATOM   873   H HB2  . LYS A 1 55  ? 4.052   14.584  57.716  1.00 98.86  ? 55  LYS A HB2  1 
ATOM   874   H HB3  . LYS A 1 55  ? 4.669   14.351  59.162  1.00 98.86  ? 55  LYS A HB3  1 
ATOM   875   H HG2  . LYS A 1 55  ? 4.195   16.404  59.826  1.00 100.98 ? 55  LYS A HG2  1 
ATOM   876   H HG3  . LYS A 1 55  ? 4.220   16.985  58.347  1.00 100.98 ? 55  LYS A HG3  1 
ATOM   877   H HD2  . LYS A 1 55  ? 2.183   15.459  58.186  1.00 105.37 ? 55  LYS A HD2  1 
ATOM   878   H HD3  . LYS A 1 55  ? 2.085   15.894  59.711  1.00 105.37 ? 55  LYS A HD3  1 
ATOM   879   H HE2  . LYS A 1 55  ? 1.649   18.008  59.202  1.00 106.01 ? 55  LYS A HE2  1 
ATOM   880   H HE3  . LYS A 1 55  ? 2.378   17.912  57.793  1.00 106.01 ? 55  LYS A HE3  1 
ATOM   881   H HZ1  . LYS A 1 55  ? 0.584   16.713  57.033  1.00 109.51 ? 55  LYS A HZ1  1 
ATOM   882   H HZ2  . LYS A 1 55  ? -0.082  16.819  58.315  1.00 109.51 ? 55  LYS A HZ2  1 
ATOM   883   H HZ3  . LYS A 1 55  ? 0.121   18.002  57.504  1.00 109.51 ? 55  LYS A HZ3  1 
ATOM   884   N N    . ASP A 1 56  ? 7.225   17.274  58.249  1.00 88.48  ? 56  ASP A N    1 
ATOM   885   C CA   . ASP A 1 56  ? 8.135   18.132  59.014  1.00 89.59  ? 56  ASP A CA   1 
ATOM   886   C C    . ASP A 1 56  ? 9.281   17.268  59.522  1.00 81.57  ? 56  ASP A C    1 
ATOM   887   O O    . ASP A 1 56  ? 9.965   16.608  58.728  1.00 84.26  ? 56  ASP A O    1 
ATOM   888   C CB   . ASP A 1 56  ? 7.385   18.832  60.144  1.00 89.68  ? 56  ASP A CB   1 
ATOM   889   C CG   . ASP A 1 56  ? 6.114   19.519  59.659  1.00 98.62  ? 56  ASP A CG   1 
ATOM   890   O OD1  . ASP A 1 56  ? 6.181   20.318  58.696  1.00 96.17  ? 56  ASP A OD1  1 
ATOM   891   O OD2  . ASP A 1 56  ? 5.039   19.250  60.239  1.00 106.66 ? 56  ASP A OD2  1 
ATOM   892   H H    . ASP A 1 56  ? 7.011   17.574  57.472  1.00 106.17 ? 56  ASP A H    1 
ATOM   893   H HA   . ASP A 1 56  ? 8.503   18.842  58.464  1.00 107.51 ? 56  ASP A HA   1 
ATOM   894   H HB2  . ASP A 1 56  ? 7.137   18.176  60.814  1.00 107.61 ? 56  ASP A HB2  1 
ATOM   895   H HB3  . ASP A 1 56  ? 7.961   19.506  60.537  1.00 107.61 ? 56  ASP A HB3  1 
ATOM   896   N N    . SER A 1 57  ? 9.502   17.217  60.829  1.00 86.61  ? 57  SER A N    1 
ATOM   897   C CA   . SER A 1 57  ? 10.635  16.471  61.361  1.00 84.81  ? 57  SER A CA   1 
ATOM   898   C C    . SER A 1 57  ? 10.262  15.080  61.865  1.00 80.41  ? 57  SER A C    1 
ATOM   899   O O    . SER A 1 57  ? 11.097  14.427  62.499  1.00 79.67  ? 57  SER A O    1 
ATOM   900   C CB   . SER A 1 57  ? 11.303  17.265  62.482  1.00 78.98  ? 57  SER A CB   1 
ATOM   901   O OG   . SER A 1 57  ? 10.606  17.072  63.693  1.00 87.74  ? 57  SER A OG   1 
ATOM   902   H HA   . SER A 1 57  ? 11.278  16.354  60.644  1.00 101.77 ? 57  SER A HA   1 
ATOM   903   H HB2  . SER A 1 57  ? 12.217  16.960  62.588  1.00 94.77  ? 57  SER A HB2  1 
ATOM   904   H HB3  . SER A 1 57  ? 11.292  18.208  62.255  1.00 94.77  ? 57  SER A HB3  1 
ATOM   905   H HG   . SER A 1 57  ? 10.755  16.301  63.990  1.00 105.29 ? 57  SER A HG   1 
ATOM   906   N N    . HIS A 1 58  ? 9.045   14.605  61.598  1.00 80.83  ? 58  HIS A N    1 
ATOM   907   C CA   . HIS A 1 58  ? 8.610   13.282  62.024  1.00 81.27  ? 58  HIS A CA   1 
ATOM   908   C C    . HIS A 1 58  ? 8.731   12.276  60.883  1.00 79.56  ? 58  HIS A C    1 
ATOM   909   O O    . HIS A 1 58  ? 8.651   12.635  59.708  1.00 78.61  ? 58  HIS A O    1 
ATOM   910   C CB   . HIS A 1 58  ? 7.164   13.326  62.525  1.00 80.18  ? 58  HIS A CB   1 
ATOM   911   C CG   . HIS A 1 58  ? 6.641   11.996  62.972  1.00 80.40  ? 58  HIS A CG   1 
ATOM   912   N ND1  . HIS A 1 58  ? 7.292   11.220  63.907  1.00 81.76  ? 58  HIS A ND1  1 
ATOM   913   C CD2  . HIS A 1 58  ? 5.538   11.300  62.607  1.00 81.00  ? 58  HIS A CD2  1 
ATOM   914   C CE1  . HIS A 1 58  ? 6.610   10.105  64.103  1.00 83.60  ? 58  HIS A CE1  1 
ATOM   915   N NE2  . HIS A 1 58  ? 5.543   10.128  63.324  1.00 85.85  ? 58  HIS A NE2  1 
ATOM   916   H H    . HIS A 1 58  ? 8.445   15.041  61.163  1.00 97.00  ? 58  HIS A H    1 
ATOM   917   H HA   . HIS A 1 58  ? 9.179   12.978  62.749  1.00 97.52  ? 58  HIS A HA   1 
ATOM   918   H HB2  . HIS A 1 58  ? 7.114   13.933  63.280  1.00 96.22  ? 58  HIS A HB2  1 
ATOM   919   H HB3  . HIS A 1 58  ? 6.594   13.643  61.807  1.00 96.22  ? 58  HIS A HB3  1 
ATOM   920   H HD1  . HIS A 1 58  ? 8.027   11.428  64.300  1.00 98.11  ? 58  HIS A HD1  1 
ATOM   921   H HD2  . HIS A 1 58  ? 4.897   11.566  61.987  1.00 97.20  ? 58  HIS A HD2  1 
ATOM   922   H HE1  . HIS A 1 58  ? 6.842   9.421   64.689  1.00 100.32 ? 58  HIS A HE1  1 
ATOM   923   H HE2  . HIS A 1 58  ? 4.948   9.509   63.274  1.00 103.02 ? 58  HIS A HE2  1 
ATOM   924   N N    . LEU A 1 59  ? 8.933   11.008  61.251  1.00 80.13  ? 59  LEU A N    1 
ATOM   925   C CA   . LEU A 1 59  ? 8.965   9.888   60.312  1.00 78.60  ? 59  LEU A CA   1 
ATOM   926   C C    . LEU A 1 59  ? 7.944   8.864   60.791  1.00 78.46  ? 59  LEU A C    1 
ATOM   927   O O    . LEU A 1 59  ? 8.120   8.263   61.855  1.00 78.86  ? 59  LEU A O    1 
ATOM   928   C CB   . LEU A 1 59  ? 10.361  9.266   60.222  1.00 75.19  ? 59  LEU A CB   1 
ATOM   929   C CG   . LEU A 1 59  ? 10.486  7.891   59.563  1.00 75.66  ? 59  LEU A CG   1 
ATOM   930   C CD1  . LEU A 1 59  ? 9.757   7.846   58.222  1.00 73.72  ? 59  LEU A CD1  1 
ATOM   931   C CD2  . LEU A 1 59  ? 11.957  7.515   59.383  1.00 75.50  ? 59  LEU A CD2  1 
ATOM   932   H H    . LEU A 1 59  ? 9.058   10.765  62.067  1.00 96.15  ? 59  LEU A H    1 
ATOM   933   H HA   . LEU A 1 59  ? 8.720   10.195  59.425  1.00 94.32  ? 59  LEU A HA   1 
ATOM   934   H HB2  . LEU A 1 59  ? 10.923  9.872   59.714  1.00 90.22  ? 59  LEU A HB2  1 
ATOM   935   H HB3  . LEU A 1 59  ? 10.703  9.176   61.125  1.00 90.22  ? 59  LEU A HB3  1 
ATOM   936   H HG   . LEU A 1 59  ? 10.068  7.236   60.144  1.00 90.80  ? 59  LEU A HG   1 
ATOM   937   H HD11 . LEU A 1 59  ? 10.087  7.092   57.709  1.00 88.46  ? 59  LEU A HD11 1 
ATOM   938   H HD12 . LEU A 1 59  ? 8.806   7.746   58.383  1.00 88.46  ? 59  LEU A HD12 1 
ATOM   939   H HD13 . LEU A 1 59  ? 9.927   8.672   57.743  1.00 88.46  ? 59  LEU A HD13 1 
ATOM   940   H HD21 . LEU A 1 59  ? 12.010  6.636   58.977  1.00 90.60  ? 59  LEU A HD21 1 
ATOM   941   H HD22 . LEU A 1 59  ? 12.383  8.171   58.810  1.00 90.60  ? 59  LEU A HD22 1 
ATOM   942   H HD23 . LEU A 1 59  ? 12.388  7.504   60.252  1.00 90.60  ? 59  LEU A HD23 1 
ATOM   943   N N    . GLN A 1 60  ? 6.866   8.688   60.025  1.00 77.33  ? 60  GLN A N    1 
ATOM   944   C CA   . GLN A 1 60  ? 5.790   7.754   60.360  1.00 76.60  ? 60  GLN A CA   1 
ATOM   945   C C    . GLN A 1 60  ? 6.009   6.496   59.526  1.00 79.52  ? 60  GLN A C    1 
ATOM   946   O O    . GLN A 1 60  ? 5.681   6.458   58.337  1.00 80.18  ? 60  GLN A O    1 
ATOM   947   C CB   . GLN A 1 60  ? 4.423   8.380   60.100  1.00 79.35  ? 60  GLN A CB   1 
ATOM   948   C CG   . GLN A 1 60  ? 3.223   7.596   60.647  1.00 79.11  ? 60  GLN A CG   1 
ATOM   949   C CD   . GLN A 1 60  ? 3.392   7.150   62.089  1.00 84.05  ? 60  GLN A CD   1 
ATOM   950   O OE1  . GLN A 1 60  ? 3.388   7.966   63.014  1.00 79.66  ? 60  GLN A OE1  1 
ATOM   951   N NE2  . GLN A 1 60  ? 3.533   5.844   62.288  1.00 84.21  ? 60  GLN A NE2  1 
ATOM   952   H H    . GLN A 1 60  ? 6.733   9.108   59.287  1.00 92.80  ? 60  GLN A H    1 
ATOM   953   H HA   . GLN A 1 60  ? 5.834   7.520   61.300  1.00 91.92  ? 60  GLN A HA   1 
ATOM   954   H HB2  . GLN A 1 60  ? 4.406   9.258   60.513  1.00 95.22  ? 60  GLN A HB2  1 
ATOM   955   H HB3  . GLN A 1 60  ? 4.302   8.461   59.141  1.00 95.22  ? 60  GLN A HB3  1 
ATOM   956   H HG2  . GLN A 1 60  ? 2.435   8.160   60.602  1.00 94.94  ? 60  GLN A HG2  1 
ATOM   957   H HG3  . GLN A 1 60  ? 3.095   6.803   60.104  1.00 94.94  ? 60  GLN A HG3  1 
ATOM   958   H HE21 . GLN A 1 60  ? 3.525   5.304   61.619  1.00 101.05 ? 60  GLN A HE21 1 
ATOM   959   H HE22 . GLN A 1 60  ? 3.632   5.539   63.086  1.00 101.05 ? 60  GLN A HE22 1 
ATOM   960   N N    . MET A 1 61  ? 6.587   5.473   60.148  1.00 79.06  ? 61  MET A N    1 
ATOM   961   C CA   . MET A 1 61  ? 6.800   4.212   59.458  1.00 79.06  ? 61  MET A CA   1 
ATOM   962   C C    . MET A 1 61  ? 5.459   3.555   59.142  1.00 80.26  ? 61  MET A C    1 
ATOM   963   O O    . MET A 1 61  ? 4.435   3.826   59.778  1.00 82.43  ? 61  MET A O    1 
ATOM   964   C CB   . MET A 1 61  ? 7.660   3.271   60.300  1.00 79.25  ? 61  MET A CB   1 
ATOM   965   C CG   . MET A 1 61  ? 9.082   3.758   60.540  1.00 76.74  ? 61  MET A CG   1 
ATOM   966   S SD   . MET A 1 61  ? 10.033  4.080   59.042  1.00 86.93  ? 61  MET A SD   1 
ATOM   967   C CE   . MET A 1 61  ? 10.447  2.419   58.524  1.00 81.06  ? 61  MET A CE   1 
ATOM   968   H H    . MET A 1 61  ? 6.861   5.485   60.963  1.00 94.88  ? 61  MET A H    1 
ATOM   969   H HA   . MET A 1 61  ? 7.278   4.378   58.631  1.00 94.87  ? 61  MET A HA   1 
ATOM   970   H HB2  . MET A 1 61  ? 7.239   3.161   61.167  1.00 95.10  ? 61  MET A HB2  1 
ATOM   971   H HB3  . MET A 1 61  ? 7.716   2.416   59.847  1.00 95.10  ? 61  MET A HB3  1 
ATOM   972   H HG2  . MET A 1 61  ? 9.044   4.585   61.045  1.00 92.09  ? 61  MET A HG2  1 
ATOM   973   H HG3  . MET A 1 61  ? 9.558   3.082   61.047  1.00 92.09  ? 61  MET A HG3  1 
ATOM   974   H HE1  . MET A 1 61  ? 10.964  2.464   57.704  1.00 97.27  ? 61  MET A HE1  1 
ATOM   975   H HE2  . MET A 1 61  ? 10.969  1.992   59.221  1.00 97.27  ? 61  MET A HE2  1 
ATOM   976   H HE3  . MET A 1 61  ? 9.628   1.922   58.372  1.00 97.27  ? 61  MET A HE3  1 
ATOM   977   N N    . MET A 1 62  ? 5.482   2.661   58.149  1.00 79.94  ? 62  MET A N    1 
ATOM   978   C CA   . MET A 1 62  ? 4.242   2.097   57.630  1.00 81.37  ? 62  MET A CA   1 
ATOM   979   C C    . MET A 1 62  ? 3.410   1.439   58.723  1.00 83.17  ? 62  MET A C    1 
ATOM   980   O O    . MET A 1 62  ? 2.175   1.475   58.663  1.00 84.14  ? 62  MET A O    1 
ATOM   981   C CB   . MET A 1 62  ? 4.553   1.085   56.526  1.00 80.33  ? 62  MET A CB   1 
ATOM   982   C CG   . MET A 1 62  ? 5.723   0.166   56.831  1.00 85.24  ? 62  MET A CG   1 
ATOM   983   S SD   . MET A 1 62  ? 5.833   -1.216  55.680  1.00 94.35  ? 62  MET A SD   1 
ATOM   984   C CE   . MET A 1 62  ? 7.601   -1.237  55.383  1.00 82.59  ? 62  MET A CE   1 
ATOM   985   H H    . MET A 1 62  ? 6.195   2.371   57.765  1.00 95.93  ? 62  MET A H    1 
ATOM   986   H HA   . MET A 1 62  ? 3.721   2.818   57.243  1.00 97.64  ? 62  MET A HA   1 
ATOM   987   H HB2  . MET A 1 62  ? 3.771   0.529   56.387  1.00 96.40  ? 62  MET A HB2  1 
ATOM   988   H HB3  . MET A 1 62  ? 4.764   1.570   55.713  1.00 96.40  ? 62  MET A HB3  1 
ATOM   989   H HG2  . MET A 1 62  ? 6.548   0.673   56.773  1.00 102.28 ? 62  MET A HG2  1 
ATOM   990   H HG3  . MET A 1 62  ? 5.618   -0.195  57.725  1.00 102.28 ? 62  MET A HG3  1 
ATOM   991   H HE1  . MET A 1 62  ? 7.808   -1.953  54.762  1.00 99.11  ? 62  MET A HE1  1 
ATOM   992   H HE2  . MET A 1 62  ? 7.869   -0.385  55.006  1.00 99.11  ? 62  MET A HE2  1 
ATOM   993   H HE3  . MET A 1 62  ? 8.061   -1.386  56.224  1.00 99.11  ? 62  MET A HE3  1 
ATOM   994   N N    . GLY A 1 63  ? 4.057   0.840   59.722  1.00 83.77  ? 63  GLY A N    1 
ATOM   995   C CA   . GLY A 1 63  ? 3.334   0.154   60.774  1.00 85.62  ? 63  GLY A CA   1 
ATOM   996   C C    . GLY A 1 63  ? 3.584   0.692   62.168  1.00 82.67  ? 63  GLY A C    1 
ATOM   997   O O    . GLY A 1 63  ? 3.519   -0.055  63.147  1.00 84.67  ? 63  GLY A O    1 
ATOM   998   H H    . GLY A 1 63  ? 4.912   0.821   59.808  1.00 100.52 ? 63  GLY A H    1 
ATOM   999   H HA2  . GLY A 1 63  ? 2.383   0.223   60.595  1.00 102.74 ? 63  GLY A HA2  1 
ATOM   1000  H HA3  . GLY A 1 63  ? 3.589   -0.782  60.768  1.00 102.74 ? 63  GLY A HA3  1 
ATOM   1001  N N    . GLY A 1 64  ? 3.871   1.985   62.274  1.00 83.80  ? 64  GLY A N    1 
ATOM   1002  C CA   . GLY A 1 64  ? 4.104   2.605   63.563  1.00 80.87  ? 64  GLY A CA   1 
ATOM   1003  C C    . GLY A 1 64  ? 5.328   2.081   64.284  1.00 80.90  ? 64  GLY A C    1 
ATOM   1004  O O    . GLY A 1 64  ? 5.527   2.358   65.469  1.00 83.67  ? 64  GLY A O    1 
ATOM   1005  H H    . GLY A 1 64  ? 3.937   2.525   61.607  1.00 100.56 ? 64  GLY A H    1 
ATOM   1006  H HA2  . GLY A 1 64  ? 4.217   3.560   63.437  1.00 97.04  ? 64  GLY A HA2  1 
ATOM   1007  H HA3  . GLY A 1 64  ? 3.333   2.450   64.131  1.00 97.04  ? 64  GLY A HA3  1 
ATOM   1008  N N    . GLU A 1 65  ? 6.157   1.321   63.582  1.00 83.15  ? 65  GLU A N    1 
ATOM   1009  C CA   . GLU A 1 65  ? 7.363   0.766   64.174  1.00 81.74  ? 65  GLU A CA   1 
ATOM   1010  C C    . GLU A 1 65  ? 8.473   1.809   64.204  1.00 83.39  ? 65  GLU A C    1 
ATOM   1011  O O    . GLU A 1 65  ? 8.507   2.734   63.387  1.00 90.18  ? 65  GLU A O    1 
ATOM   1012  C CB   . GLU A 1 65  ? 7.825   -0.461  63.381  1.00 86.53  ? 65  GLU A CB   1 
ATOM   1013  C CG   . GLU A 1 65  ? 8.403   -0.144  62.000  1.00 86.38  ? 65  GLU A CG   1 
ATOM   1014  C CD   . GLU A 1 65  ? 7.447   -0.477  60.861  1.00 92.63  ? 65  GLU A CD   1 
ATOM   1015  O OE1  . GLU A 1 65  ? 6.223   -0.322  61.058  1.00 92.92  ? 65  GLU A OE1  1 
ATOM   1016  O OE2  . GLU A 1 65  ? 7.916   -0.889  59.773  1.00 87.64  ? 65  GLU A OE2  1 
ATOM   1017  H H    . GLU A 1 65  ? 6.042   1.111   62.756  1.00 99.78  ? 65  GLU A H    1 
ATOM   1018  H HA   . GLU A 1 65  ? 7.181   0.491   65.086  1.00 98.09  ? 65  GLU A HA   1 
ATOM   1019  H HB2  . GLU A 1 65  ? 8.514   -0.916  63.890  1.00 103.83 ? 65  GLU A HB2  1 
ATOM   1020  H HB3  . GLU A 1 65  ? 7.065   -1.050  63.252  1.00 103.83 ? 65  GLU A HB3  1 
ATOM   1021  H HG2  . GLU A 1 65  ? 8.605   0.804   61.953  1.00 103.66 ? 65  GLU A HG2  1 
ATOM   1022  H HG3  . GLU A 1 65  ? 9.213   -0.662  61.871  1.00 103.66 ? 65  GLU A HG3  1 
ATOM   1023  N N    . PHE A 1 66  ? 9.395   1.646   65.148  1.00 78.96  ? 66  PHE A N    1 
ATOM   1024  C CA   . PHE A 1 66  ? 10.627  2.422   65.149  1.00 79.35  ? 66  PHE A CA   1 
ATOM   1025  C C    . PHE A 1 66  ? 11.682  1.689   64.326  1.00 78.86  ? 66  PHE A C    1 
ATOM   1026  O O    . PHE A 1 66  ? 11.839  0.470   64.439  1.00 82.35  ? 66  PHE A O    1 
ATOM   1027  C CB   . PHE A 1 66  ? 11.141  2.653   66.569  1.00 79.45  ? 66  PHE A CB   1 
ATOM   1028  C CG   . PHE A 1 66  ? 12.543  3.200   66.617  1.00 78.59  ? 66  PHE A CG   1 
ATOM   1029  C CD1  . PHE A 1 66  ? 12.808  4.502   66.223  1.00 76.94  ? 66  PHE A CD1  1 
ATOM   1030  C CD2  . PHE A 1 66  ? 13.598  2.407   67.042  1.00 75.65  ? 66  PHE A CD2  1 
ATOM   1031  C CE1  . PHE A 1 66  ? 14.097  5.002   66.257  1.00 77.40  ? 66  PHE A CE1  1 
ATOM   1032  C CE2  . PHE A 1 66  ? 14.889  2.901   67.077  1.00 73.33  ? 66  PHE A CE2  1 
ATOM   1033  C CZ   . PHE A 1 66  ? 15.139  4.199   66.685  1.00 76.06  ? 66  PHE A CZ   1 
ATOM   1034  H H    . PHE A 1 66  ? 9.328   1.090   65.800  1.00 94.75  ? 66  PHE A H    1 
ATOM   1035  H HA   . PHE A 1 66  ? 10.460  3.293   64.757  1.00 95.23  ? 66  PHE A HA   1 
ATOM   1036  H HB2  . PHE A 1 66  ? 10.559  3.289   67.013  1.00 95.33  ? 66  PHE A HB2  1 
ATOM   1037  H HB3  . PHE A 1 66  ? 11.135  1.808   67.046  1.00 95.33  ? 66  PHE A HB3  1 
ATOM   1038  H HD1  . PHE A 1 66  ? 12.111  5.045   65.932  1.00 92.32  ? 66  PHE A HD1  1 
ATOM   1039  H HD2  . PHE A 1 66  ? 13.435  1.530   67.306  1.00 90.78  ? 66  PHE A HD2  1 
ATOM   1040  H HE1  . PHE A 1 66  ? 14.263  5.878   65.993  1.00 92.88  ? 66  PHE A HE1  1 
ATOM   1041  H HE2  . PHE A 1 66  ? 15.587  2.358   67.364  1.00 87.99  ? 66  PHE A HE2  1 
ATOM   1042  H HZ   . PHE A 1 66  ? 16.006  4.534   66.708  1.00 91.28  ? 66  PHE A HZ   1 
ATOM   1043  N N    . SER A 1 67  ? 12.396  2.436   63.488  1.00 77.10  ? 67  SER A N    1 
ATOM   1044  C CA   . SER A 1 67  ? 13.478  1.884   62.682  1.00 77.98  ? 67  SER A CA   1 
ATOM   1045  C C    . SER A 1 67  ? 14.678  2.809   62.779  1.00 74.20  ? 67  SER A C    1 
ATOM   1046  O O    . SER A 1 67  ? 14.608  3.966   62.353  1.00 73.22  ? 67  SER A O    1 
ATOM   1047  C CB   . SER A 1 67  ? 13.056  1.713   61.223  1.00 75.21  ? 67  SER A CB   1 
ATOM   1048  O OG   . SER A 1 67  ? 14.169  1.344   60.427  1.00 75.13  ? 67  SER A OG   1 
ATOM   1049  H H    . SER A 1 67  ? 12.270  3.278   63.368  1.00 92.52  ? 67  SER A H    1 
ATOM   1050  H HA   . SER A 1 67  ? 13.725  1.014   63.032  1.00 93.58  ? 67  SER A HA   1 
ATOM   1051  H HB2  . SER A 1 67  ? 12.382  1.018   61.166  1.00 90.25  ? 67  SER A HB2  1 
ATOM   1052  H HB3  . SER A 1 67  ? 12.697  2.552   60.896  1.00 90.25  ? 67  SER A HB3  1 
ATOM   1053  H HG   . SER A 1 67  ? 14.487  0.615   60.698  1.00 90.16  ? 67  SER A HG   1 
ATOM   1054  N N    . GLY A 1 68  ? 15.777  2.301   63.338  1.00 74.69  ? 68  GLY A N    1 
ATOM   1055  C CA   . GLY A 1 68  ? 16.986  3.101   63.415  1.00 71.11  ? 68  GLY A CA   1 
ATOM   1056  C C    . GLY A 1 68  ? 17.549  3.428   62.047  1.00 72.43  ? 68  GLY A C    1 
ATOM   1057  O O    . GLY A 1 68  ? 17.969  4.558   61.795  1.00 72.85  ? 68  GLY A O    1 
ATOM   1058  H H    . GLY A 1 68  ? 15.843  1.511   63.673  1.00 89.63  ? 68  GLY A H    1 
ATOM   1059  H HA2  . GLY A 1 68  ? 16.791  3.934   63.872  1.00 85.33  ? 68  GLY A HA2  1 
ATOM   1060  H HA3  . GLY A 1 68  ? 17.660  2.616   63.915  1.00 85.33  ? 68  GLY A HA3  1 
ATOM   1061  N N    . ASN A 1 69  ? 17.549  2.448   61.139  1.00 74.66  ? 69  ASN A N    1 
ATOM   1062  C CA   . ASN A 1 69  ? 18.082  2.676   59.799  1.00 71.48  ? 69  ASN A CA   1 
ATOM   1063  C C    . ASN A 1 69  ? 17.252  3.708   59.041  1.00 71.54  ? 69  ASN A C    1 
ATOM   1064  O O    . ASN A 1 69  ? 17.802  4.575   58.350  1.00 68.90  ? 69  ASN A O    1 
ATOM   1065  C CB   . ASN A 1 69  ? 18.126  1.358   59.026  1.00 72.31  ? 69  ASN A CB   1 
ATOM   1066  C CG   . ASN A 1 69  ? 19.447  0.626   59.190  1.00 71.94  ? 69  ASN A CG   1 
ATOM   1067  O OD1  . ASN A 1 69  ? 20.483  1.237   59.460  1.00 68.91  ? 69  ASN A OD1  1 
ATOM   1068  N ND2  . ASN A 1 69  ? 19.415  -0.694  59.017  1.00 73.50  ? 69  ASN A ND2  1 
ATOM   1069  H H    . ASN A 1 69  ? 17.250  1.653   61.274  1.00 89.59  ? 69  ASN A H    1 
ATOM   1070  H HA   . ASN A 1 69  ? 18.988  3.016   59.877  1.00 85.77  ? 69  ASN A HA   1 
ATOM   1071  H HB2  . ASN A 1 69  ? 17.419  0.778   59.350  1.00 86.78  ? 69  ASN A HB2  1 
ATOM   1072  H HB3  . ASN A 1 69  ? 17.999  1.541   58.082  1.00 86.78  ? 69  ASN A HB3  1 
ATOM   1073  H HD21 . ASN A 1 69  ? 20.136  -1.155  59.098  1.00 88.20  ? 69  ASN A HD21 1 
ATOM   1074  H HD22 . ASN A 1 69  ? 18.674  -1.085  58.824  1.00 88.20  ? 69  ASN A HD22 1 
ATOM   1075  N N    . ALA A 1 70  ? 15.923  3.632   59.162  1.00 71.55  ? 70  ALA A N    1 
ATOM   1076  C CA   . ALA A 1 70  ? 15.067  4.603   58.490  1.00 71.11  ? 70  ALA A CA   1 
ATOM   1077  C C    . ALA A 1 70  ? 15.244  6.000   59.074  1.00 72.25  ? 70  ALA A C    1 
ATOM   1078  O O    . ALA A 1 70  ? 15.272  6.990   58.335  1.00 69.98  ? 70  ALA A O    1 
ATOM   1079  C CB   . ALA A 1 70  ? 13.606  4.165   58.584  1.00 72.80  ? 70  ALA A CB   1 
ATOM   1080  H H    . ALA A 1 70  ? 15.502  3.038   59.620  1.00 85.86  ? 70  ALA A H    1 
ATOM   1081  H HA   . ALA A 1 70  ? 15.313  4.637   57.552  1.00 85.33  ? 70  ALA A HA   1 
ATOM   1082  H HB1  . ALA A 1 70  ? 13.059  4.775   58.064  1.00 87.35  ? 70  ALA A HB1  1 
ATOM   1083  H HB2  . ALA A 1 70  ? 13.522  3.265   58.233  1.00 87.35  ? 70  ALA A HB2  1 
ATOM   1084  H HB3  . ALA A 1 70  ? 13.330  4.185   59.514  1.00 87.35  ? 70  ALA A HB3  1 
ATOM   1085  N N    . SER A 1 71  ? 15.356  6.105   60.398  1.00 71.63  ? 71  SER A N    1 
ATOM   1086  C CA   . SER A 1 71  ? 15.559  7.415   61.009  1.00 71.01  ? 71  SER A CA   1 
ATOM   1087  C C    . SER A 1 71  ? 16.882  8.027   60.565  1.00 67.92  ? 71  SER A C    1 
ATOM   1088  O O    . SER A 1 71  ? 16.984  9.247   60.389  1.00 69.84  ? 71  SER A O    1 
ATOM   1089  C CB   . SER A 1 71  ? 15.499  7.296   62.532  1.00 72.01  ? 71  SER A CB   1 
ATOM   1090  O OG   . SER A 1 71  ? 14.218  6.851   62.954  1.00 70.20  ? 71  SER A OG   1 
ATOM   1091  H H    . SER A 1 71  ? 15.320  5.449   60.952  1.00 85.96  ? 71  SER A H    1 
ATOM   1092  H HA   . SER A 1 71  ? 14.845  8.010   60.730  1.00 85.21  ? 71  SER A HA   1 
ATOM   1093  H HB2  . SER A 1 71  ? 16.167  6.657   62.825  1.00 86.41  ? 71  SER A HB2  1 
ATOM   1094  H HB3  . SER A 1 71  ? 15.676  8.165   62.924  1.00 86.41  ? 71  SER A HB3  1 
ATOM   1095  H HG   . SER A 1 71  ? 14.044  6.106   62.608  1.00 84.24  ? 71  SER A HG   1 
ATOM   1096  N N    . ARG A 1 72  ? 17.907  7.197   60.370  1.00 67.85  ? 72  ARG A N    1 
ATOM   1097  C CA   . ARG A 1 72  ? 19.184  7.705   59.879  1.00 69.31  ? 72  ARG A CA   1 
ATOM   1098  C C    . ARG A 1 72  ? 19.076  8.141   58.421  1.00 72.07  ? 72  ARG A C    1 
ATOM   1099  O O    . ARG A 1 72  ? 19.711  9.120   58.009  1.00 70.25  ? 72  ARG A O    1 
ATOM   1100  C CB   . ARG A 1 72  ? 20.266  6.639   60.040  1.00 70.82  ? 72  ARG A CB   1 
ATOM   1101  C CG   . ARG A 1 72  ? 20.464  6.154   61.465  1.00 72.50  ? 72  ARG A CG   1 
ATOM   1102  C CD   . ARG A 1 72  ? 21.153  4.795   61.464  1.00 71.60  ? 72  ARG A CD   1 
ATOM   1103  N NE   . ARG A 1 72  ? 22.387  4.864   60.693  1.00 73.62  ? 72  ARG A NE   1 
ATOM   1104  C CZ   . ARG A 1 72  ? 22.618  4.197   59.571  1.00 75.25  ? 72  ARG A CZ   1 
ATOM   1105  N NH1  . ARG A 1 72  ? 21.759  3.308   59.099  1.00 74.88  ? 72  ARG A NH1  1 
ATOM   1106  N NH2  . ARG A 1 72  ? 23.739  4.431   58.899  1.00 75.75  ? 72  ARG A NH2  1 
ATOM   1107  H H    . ARG A 1 72  ? 17.889  6.349   60.513  1.00 81.42  ? 72  ARG A H    1 
ATOM   1108  H HA   . ARG A 1 72  ? 19.440  8.477   60.408  1.00 83.17  ? 72  ARG A HA   1 
ATOM   1109  H HB2  . ARG A 1 72  ? 20.026  5.870   59.500  1.00 84.98  ? 72  ARG A HB2  1 
ATOM   1110  H HB3  . ARG A 1 72  ? 21.110  7.007   59.736  1.00 84.98  ? 72  ARG A HB3  1 
ATOM   1111  H HG2  . ARG A 1 72  ? 21.019  6.784   61.950  1.00 87.00  ? 72  ARG A HG2  1 
ATOM   1112  H HG3  . ARG A 1 72  ? 19.603  6.066   61.902  1.00 87.00  ? 72  ARG A HG3  1 
ATOM   1113  H HD2  . ARG A 1 72  ? 21.369  4.537   62.374  1.00 85.92  ? 72  ARG A HD2  1 
ATOM   1114  H HD3  . ARG A 1 72  ? 20.570  4.133   61.060  1.00 85.92  ? 72  ARG A HD3  1 
ATOM   1115  H HE   . ARG A 1 72  ? 23.012  5.376   60.987  1.00 88.34  ? 72  ARG A HE   1 
ATOM   1116  H HH11 . ARG A 1 72  ? 21.027  3.151   59.523  1.00 89.86  ? 72  ARG A HH11 1 
ATOM   1117  H HH12 . ARG A 1 72  ? 21.931  2.888   58.369  1.00 89.86  ? 72  ARG A HH12 1 
ATOM   1118  H HH21 . ARG A 1 72  ? 24.303  5.010   59.193  1.00 90.90  ? 72  ARG A HH21 1 
ATOM   1119  H HH22 . ARG A 1 72  ? 23.901  4.004   58.170  1.00 90.90  ? 72  ARG A HH22 1 
ATOM   1120  N N    . ALA A 1 73  ? 18.282  7.422   57.623  1.00 69.10  ? 73  ALA A N    1 
ATOM   1121  C CA   . ALA A 1 73  ? 18.031  7.847   56.251  1.00 69.88  ? 73  ALA A CA   1 
ATOM   1122  C C    . ALA A 1 73  ? 17.331  9.200   56.221  1.00 70.23  ? 73  ALA A C    1 
ATOM   1123  O O    . ALA A 1 73  ? 17.709  10.095  55.457  1.00 71.99  ? 73  ALA A O    1 
ATOM   1124  C CB   . ALA A 1 73  ? 17.189  6.795   55.529  1.00 70.22  ? 73  ALA A CB   1 
ATOM   1125  H H    . ALA A 1 73  ? 17.884  6.695   57.851  1.00 82.92  ? 73  ALA A H    1 
ATOM   1126  H HA   . ALA A 1 73  ? 18.878  7.932   55.786  1.00 83.86  ? 73  ALA A HA   1 
ATOM   1127  H HB1  . ALA A 1 73  ? 17.043  7.081   54.613  1.00 84.26  ? 73  ALA A HB1  1 
ATOM   1128  H HB2  . ALA A 1 73  ? 17.664  5.949   55.539  1.00 84.26  ? 73  ALA A HB2  1 
ATOM   1129  H HB3  . ALA A 1 73  ? 16.339  6.702   55.986  1.00 84.26  ? 73  ALA A HB3  1 
ATOM   1130  N N    . PHE A 1 74  ? 16.296  9.360   57.048  1.00 69.83  ? 74  PHE A N    1 
ATOM   1131  C CA   . PHE A 1 74  ? 15.597  10.638  57.144  1.00 71.34  ? 74  PHE A CA   1 
ATOM   1132  C C    . PHE A 1 74  ? 16.535  11.755  57.579  1.00 71.52  ? 74  PHE A C    1 
ATOM   1133  O O    . PHE A 1 74  ? 16.438  12.884  57.084  1.00 70.00  ? 74  PHE A O    1 
ATOM   1134  C CB   . PHE A 1 74  ? 14.434  10.508  58.131  1.00 73.22  ? 74  PHE A CB   1 
ATOM   1135  C CG   . PHE A 1 74  ? 13.557  11.728  58.219  1.00 73.84  ? 74  PHE A CG   1 
ATOM   1136  C CD1  . PHE A 1 74  ? 13.455  12.609  57.159  1.00 71.55  ? 74  PHE A CD1  1 
ATOM   1137  C CD2  . PHE A 1 74  ? 12.823  11.980  59.365  1.00 75.87  ? 74  PHE A CD2  1 
ATOM   1138  C CE1  . PHE A 1 74  ? 12.642  13.721  57.242  1.00 73.94  ? 74  PHE A CE1  1 
ATOM   1139  C CE2  . PHE A 1 74  ? 12.009  13.091  59.453  1.00 76.90  ? 74  PHE A CE2  1 
ATOM   1140  C CZ   . PHE A 1 74  ? 11.918  13.962  58.386  1.00 76.70  ? 74  PHE A CZ   1 
ATOM   1141  H H    . PHE A 1 74  ? 15.981  8.747   57.562  1.00 83.79  ? 74  PHE A H    1 
ATOM   1142  H HA   . PHE A 1 74  ? 15.242  10.870  56.272  1.00 85.61  ? 74  PHE A HA   1 
ATOM   1143  H HB2  . PHE A 1 74  ? 13.875  9.764   57.855  1.00 87.86  ? 74  PHE A HB2  1 
ATOM   1144  H HB3  . PHE A 1 74  ? 14.795  10.341  59.015  1.00 87.86  ? 74  PHE A HB3  1 
ATOM   1145  H HD1  . PHE A 1 74  ? 13.939  12.450  56.381  1.00 85.86  ? 74  PHE A HD1  1 
ATOM   1146  H HD2  . PHE A 1 74  ? 12.878  11.394  60.084  1.00 91.04  ? 74  PHE A HD2  1 
ATOM   1147  H HE1  . PHE A 1 74  ? 12.585  14.309  56.524  1.00 88.73  ? 74  PHE A HE1  1 
ATOM   1148  H HE2  . PHE A 1 74  ? 11.523  13.253  60.229  1.00 92.28  ? 74  PHE A HE2  1 
ATOM   1149  H HZ   . PHE A 1 74  ? 11.368  14.710  58.440  1.00 92.04  ? 74  PHE A HZ   1 
ATOM   1150  N N    . ALA A 1 75  ? 17.436  11.472  58.522  1.00 70.22  ? 75  ALA A N    1 
ATOM   1151  C CA   . ALA A 1 75  ? 18.361  12.506  58.971  1.00 71.95  ? 75  ALA A CA   1 
ATOM   1152  C C    . ALA A 1 75  ? 19.352  12.860  57.869  1.00 71.16  ? 75  ALA A C    1 
ATOM   1153  O O    . ALA A 1 75  ? 19.706  14.032  57.694  1.00 70.78  ? 75  ALA A O    1 
ATOM   1154  C CB   . ALA A 1 75  ? 19.096  12.053  60.232  1.00 70.59  ? 75  ALA A CB   1 
ATOM   1155  H H    . ALA A 1 75  ? 17.528  10.709  58.907  1.00 84.27  ? 75  ALA A H    1 
ATOM   1156  H HA   . ALA A 1 75  ? 17.856  13.303  59.197  1.00 86.34  ? 75  ALA A HA   1 
ATOM   1157  H HB1  . ALA A 1 75  ? 19.705  12.754  60.512  1.00 84.70  ? 75  ALA A HB1  1 
ATOM   1158  H HB2  . ALA A 1 75  ? 18.447  11.880  60.931  1.00 84.70  ? 75  ALA A HB2  1 
ATOM   1159  H HB3  . ALA A 1 75  ? 19.592  11.243  60.034  1.00 84.70  ? 75  ALA A HB3  1 
ATOM   1160  N N    . SER A 1 76  ? 19.810  11.860  57.113  1.00 72.29  ? 76  SER A N    1 
ATOM   1161  C CA   . SER A 1 76  ? 20.700  12.142  55.994  1.00 69.48  ? 76  SER A CA   1 
ATOM   1162  C C    . SER A 1 76  ? 19.975  12.902  54.893  1.00 74.41  ? 76  SER A C    1 
ATOM   1163  O O    . SER A 1 76  ? 20.609  13.640  54.128  1.00 74.56  ? 76  SER A O    1 
ATOM   1164  C CB   . SER A 1 76  ? 21.285  10.842  55.449  1.00 70.12  ? 76  SER A CB   1 
ATOM   1165  O OG   . SER A 1 76  ? 22.094  10.201  56.416  1.00 69.84  ? 76  SER A OG   1 
ATOM   1166  H H    . SER A 1 76  ? 19.623  11.028  57.226  1.00 86.75  ? 76  SER A H    1 
ATOM   1167  H HA   . SER A 1 76  ? 21.437  12.689  56.305  1.00 83.38  ? 76  SER A HA   1 
ATOM   1168  H HB2  . SER A 1 76  ? 20.559  10.248  55.203  1.00 84.14  ? 76  SER A HB2  1 
ATOM   1169  H HB3  . SER A 1 76  ? 21.827  11.044  54.670  1.00 84.14  ? 76  SER A HB3  1 
ATOM   1170  H HG   . SER A 1 76  ? 21.632  9.999   57.088  1.00 83.81  ? 76  SER A HG   1 
ATOM   1171  N N    . LEU A 1 77  ? 18.652  12.744  54.799  1.00 75.89  ? 77  LEU A N    1 
ATOM   1172  C CA   . LEU A 1 77  ? 17.897  13.468  53.780  1.00 77.20  ? 77  LEU A CA   1 
ATOM   1173  C C    . LEU A 1 77  ? 17.764  14.941  54.143  1.00 74.80  ? 77  LEU A C    1 
ATOM   1174  O O    . LEU A 1 77  ? 17.801  15.809  53.262  1.00 76.00  ? 77  LEU A O    1 
ATOM   1175  C CB   . LEU A 1 77  ? 16.517  12.838  53.599  1.00 75.98  ? 77  LEU A CB   1 
ATOM   1176  C CG   . LEU A 1 77  ? 15.563  13.555  52.646  1.00 71.06  ? 77  LEU A CG   1 
ATOM   1177  C CD1  . LEU A 1 77  ? 16.227  13.784  51.307  1.00 71.81  ? 77  LEU A CD1  1 
ATOM   1178  C CD2  . LEU A 1 77  ? 14.276  12.762  52.475  1.00 72.26  ? 77  LEU A CD2  1 
ATOM   1179  H H    . LEU A 1 77  ? 18.178  12.233  55.303  1.00 91.07  ? 77  LEU A H    1 
ATOM   1180  H HA   . LEU A 1 77  ? 18.370  13.402  52.936  1.00 92.64  ? 77  LEU A HA   1 
ATOM   1181  H HB2  . LEU A 1 77  ? 16.639  11.938  53.256  1.00 91.18  ? 77  LEU A HB2  1 
ATOM   1182  H HB3  . LEU A 1 77  ? 16.084  12.807  54.466  1.00 91.18  ? 77  LEU A HB3  1 
ATOM   1183  H HG   . LEU A 1 77  ? 15.333  14.419  53.022  1.00 85.27  ? 77  LEU A HG   1 
ATOM   1184  H HD11 . LEU A 1 77  ? 15.567  14.124  50.681  1.00 86.16  ? 77  LEU A HD11 1 
ATOM   1185  H HD12 . LEU A 1 77  ? 16.943  14.429  51.415  1.00 86.16  ? 77  LEU A HD12 1 
ATOM   1186  H HD13 . LEU A 1 77  ? 16.586  12.943  50.984  1.00 86.16  ? 77  LEU A HD13 1 
ATOM   1187  H HD21 . LEU A 1 77  ? 13.688  13.242  51.871  1.00 86.71  ? 77  LEU A HD21 1 
ATOM   1188  H HD22 . LEU A 1 77  ? 14.489  11.891  52.107  1.00 86.71  ? 77  LEU A HD22 1 
ATOM   1189  H HD23 . LEU A 1 77  ? 13.851  12.661  53.341  1.00 86.71  ? 77  LEU A HD23 1 
ATOM   1190  N N    . LEU A 1 78  ? 17.599  15.242  55.433  1.00 73.50  ? 78  LEU A N    1 
ATOM   1191  C CA   . LEU A 1 78  ? 17.503  16.632  55.858  1.00 71.68  ? 78  LEU A CA   1 
ATOM   1192  C C    . LEU A 1 78  ? 18.821  17.366  55.669  1.00 73.01  ? 78  LEU A C    1 
ATOM   1193  O O    . LEU A 1 78  ? 18.818  18.570  55.385  1.00 73.19  ? 78  LEU A O    1 
ATOM   1194  C CB   . LEU A 1 78  ? 17.067  16.701  57.324  1.00 75.79  ? 78  LEU A CB   1 
ATOM   1195  C CG   . LEU A 1 78  ? 15.661  16.180  57.631  1.00 75.29  ? 78  LEU A CG   1 
ATOM   1196  C CD1  . LEU A 1 78  ? 15.525  15.861  59.112  1.00 69.06  ? 78  LEU A CD1  1 
ATOM   1197  C CD2  . LEU A 1 78  ? 14.598  17.181  57.188  1.00 67.03  ? 78  LEU A CD2  1 
ATOM   1198  H H    . LEU A 1 78  ? 17.541  14.667  56.069  1.00 88.20  ? 78  LEU A H    1 
ATOM   1199  H HA   . LEU A 1 78  ? 16.830  17.078  55.321  1.00 86.01  ? 78  LEU A HA   1 
ATOM   1200  H HB2  . LEU A 1 78  ? 17.689  16.174  57.850  1.00 90.95  ? 78  LEU A HB2  1 
ATOM   1201  H HB3  . LEU A 1 78  ? 17.097  17.629  57.605  1.00 90.95  ? 78  LEU A HB3  1 
ATOM   1202  H HG   . LEU A 1 78  ? 15.514  15.361  57.132  1.00 90.35  ? 78  LEU A HG   1 
ATOM   1203  H HD11 . LEU A 1 78  ? 14.624  15.545  59.286  1.00 82.87  ? 78  LEU A HD11 1 
ATOM   1204  H HD12 . LEU A 1 78  ? 16.168  15.174  59.348  1.00 82.87  ? 78  LEU A HD12 1 
ATOM   1205  H HD13 . LEU A 1 78  ? 15.697  16.666  59.626  1.00 82.87  ? 78  LEU A HD13 1 
ATOM   1206  H HD21 . LEU A 1 78  ? 13.722  16.827  57.406  1.00 80.43  ? 78  LEU A HD21 1 
ATOM   1207  H HD22 . LEU A 1 78  ? 14.741  18.020  57.654  1.00 80.43  ? 78  LEU A HD22 1 
ATOM   1208  H HD23 . LEU A 1 78  ? 14.672  17.317  56.231  1.00 80.43  ? 78  LEU A HD23 1 
ATOM   1209  N N    . ALA A 1 79  ? 19.946  16.669  55.829  1.00 72.93  ? 79  ALA A N    1 
ATOM   1210  C CA   . ALA A 1 79  ? 21.233  17.276  55.520  1.00 74.05  ? 79  ALA A CA   1 
ATOM   1211  C C    . ALA A 1 79  ? 21.369  17.505  54.025  1.00 73.80  ? 79  ALA A C    1 
ATOM   1212  O O    . ALA A 1 79  ? 21.843  18.562  53.591  1.00 74.08  ? 79  ALA A O    1 
ATOM   1213  C CB   . ALA A 1 79  ? 22.371  16.393  56.029  1.00 74.59  ? 79  ALA A CB   1 
ATOM   1214  H H    . ALA A 1 79  ? 19.989  15.857  56.110  1.00 87.52  ? 79  ALA A H    1 
ATOM   1215  H HA   . ALA A 1 79  ? 21.297  18.131  55.974  1.00 88.86  ? 79  ALA A HA   1 
ATOM   1216  H HB1  . ALA A 1 79  ? 23.218  16.813  55.812  1.00 89.51  ? 79  ALA A HB1  1 
ATOM   1217  H HB2  . ALA A 1 79  ? 22.288  16.293  56.990  1.00 89.51  ? 79  ALA A HB2  1 
ATOM   1218  H HB3  . ALA A 1 79  ? 22.312  15.525  55.601  1.00 89.51  ? 79  ALA A HB3  1 
ATOM   1219  N N    . PHE A 1 80  ? 20.956  16.513  53.225  1.00 73.78  ? 80  PHE A N    1 
ATOM   1220  C CA   . PHE A 1 80  ? 20.986  16.630  51.772  1.00 71.99  ? 80  PHE A CA   1 
ATOM   1221  C C    . PHE A 1 80  ? 20.230  17.860  51.294  1.00 73.26  ? 80  PHE A C    1 
ATOM   1222  O O    . PHE A 1 80  ? 20.611  18.467  50.285  1.00 73.09  ? 80  PHE A O    1 
ATOM   1223  C CB   . PHE A 1 80  ? 20.397  15.356  51.155  1.00 72.55  ? 80  PHE A CB   1 
ATOM   1224  C CG   . PHE A 1 80  ? 20.726  15.160  49.701  1.00 70.15  ? 80  PHE A CG   1 
ATOM   1225  C CD1  . PHE A 1 80  ? 22.043  15.026  49.286  1.00 70.44  ? 80  PHE A CD1  1 
ATOM   1226  C CD2  . PHE A 1 80  ? 19.717  15.091  48.749  1.00 69.56  ? 80  PHE A CD2  1 
ATOM   1227  C CE1  . PHE A 1 80  ? 22.348  14.841  47.945  1.00 71.40  ? 80  PHE A CE1  1 
ATOM   1228  C CE2  . PHE A 1 80  ? 20.019  14.906  47.410  1.00 69.66  ? 80  PHE A CE2  1 
ATOM   1229  C CZ   . PHE A 1 80  ? 21.335  14.780  47.010  1.00 69.51  ? 80  PHE A CZ   1 
ATOM   1230  H H    . PHE A 1 80  ? 20.653  15.758  53.505  1.00 88.54  ? 80  PHE A H    1 
ATOM   1231  H HA   . PHE A 1 80  ? 21.904  16.720  51.472  1.00 86.39  ? 80  PHE A HA   1 
ATOM   1232  H HB2  . PHE A 1 80  ? 20.740  14.590  51.640  1.00 87.06  ? 80  PHE A HB2  1 
ATOM   1233  H HB3  . PHE A 1 80  ? 19.430  15.393  51.234  1.00 87.06  ? 80  PHE A HB3  1 
ATOM   1234  H HD1  . PHE A 1 80  ? 22.729  15.061  49.913  1.00 84.52  ? 80  PHE A HD1  1 
ATOM   1235  H HD2  . PHE A 1 80  ? 18.829  15.171  49.013  1.00 83.46  ? 80  PHE A HD2  1 
ATOM   1236  H HE1  . PHE A 1 80  ? 23.234  14.759  47.677  1.00 85.68  ? 80  PHE A HE1  1 
ATOM   1237  H HE2  . PHE A 1 80  ? 19.336  14.867  46.780  1.00 83.59  ? 80  PHE A HE2  1 
ATOM   1238  H HZ   . PHE A 1 80  ? 21.539  14.653  46.111  1.00 83.41  ? 80  PHE A HZ   1 
ATOM   1239  N N    . ARG A 1 81  ? 19.169  18.246  52.001  1.00 72.15  ? 81  ARG A N    1 
ATOM   1240  C CA   . ARG A 1 81  ? 18.317  19.350  51.589  1.00 73.78  ? 81  ARG A CA   1 
ATOM   1241  C C    . ARG A 1 81  ? 18.603  20.643  52.350  1.00 73.52  ? 81  ARG A C    1 
ATOM   1242  O O    . ARG A 1 81  ? 17.883  21.628  52.161  1.00 75.92  ? 81  ARG A O    1 
ATOM   1243  C CB   . ARG A 1 81  ? 16.845  18.972  51.765  1.00 72.84  ? 81  ARG A CB   1 
ATOM   1244  C CG   . ARG A 1 81  ? 16.411  17.756  50.972  1.00 71.86  ? 81  ARG A CG   1 
ATOM   1245  C CD   . ARG A 1 81  ? 14.914  17.497  51.099  1.00 69.38  ? 81  ARG A CD   1 
ATOM   1246  N NE   . ARG A 1 81  ? 14.403  16.781  49.935  1.00 76.64  ? 81  ARG A NE   1 
ATOM   1247  C CZ   . ARG A 1 81  ? 13.188  16.256  49.840  1.00 74.10  ? 81  ARG A CZ   1 
ATOM   1248  N NH1  . ARG A 1 81  ? 12.326  16.325  50.838  1.00 65.54  ? 81  ARG A NH1  1 
ATOM   1249  N NH2  . ARG A 1 81  ? 12.826  15.656  48.708  1.00 72.72  ? 81  ARG A NH2  1 
ATOM   1250  H H    . ARG A 1 81  ? 18.921  17.874  52.735  1.00 86.58  ? 81  ARG A H    1 
ATOM   1251  H HA   . ARG A 1 81  ? 18.481  19.518  50.648  1.00 88.54  ? 81  ARG A HA   1 
ATOM   1252  H HB2  . ARG A 1 81  ? 16.685  18.783  52.703  1.00 87.41  ? 81  ARG A HB2  1 
ATOM   1253  H HB3  . ARG A 1 81  ? 16.298  19.719  51.479  1.00 87.41  ? 81  ARG A HB3  1 
ATOM   1254  H HG2  . ARG A 1 81  ? 16.615  17.896  50.035  1.00 86.23  ? 81  ARG A HG2  1 
ATOM   1255  H HG3  . ARG A 1 81  ? 16.882  16.975  51.301  1.00 86.23  ? 81  ARG A HG3  1 
ATOM   1256  H HD2  . ARG A 1 81  ? 14.746  16.958  51.888  1.00 83.25  ? 81  ARG A HD2  1 
ATOM   1257  H HD3  . ARG A 1 81  ? 14.445  18.343  51.168  1.00 83.25  ? 81  ARG A HD3  1 
ATOM   1258  H HE   . ARG A 1 81  ? 14.928  16.693  49.260  1.00 91.97  ? 81  ARG A HE   1 
ATOM   1259  H HH11 . ARG A 1 81  ? 12.546  16.717  51.571  1.00 78.65  ? 81  ARG A HH11 1 
ATOM   1260  H HH12 . ARG A 1 81  ? 11.543  15.977  50.755  1.00 78.65  ? 81  ARG A HH12 1 
ATOM   1261  H HH21 . ARG A 1 81  ? 13.377  15.612  48.049  1.00 87.27  ? 81  ARG A HH21 1 
ATOM   1262  H HH22 . ARG A 1 81  ? 12.041  15.312  48.635  1.00 87.27  ? 81  ARG A HH22 1 
ATOM   1263  N N    . ASP A 1 82  ? 19.630  20.666  53.201  1.00 74.07  ? 82  ASP A N    1 
ATOM   1264  C CA   . ASP A 1 82  ? 19.910  21.803  54.072  1.00 73.72  ? 82  ASP A CA   1 
ATOM   1265  C C    . ASP A 1 82  ? 20.983  22.676  53.435  1.00 73.12  ? 82  ASP A C    1 
ATOM   1266  O O    . ASP A 1 82  ? 22.118  22.228  53.234  1.00 72.88  ? 82  ASP A O    1 
ATOM   1267  C CB   . ASP A 1 82  ? 20.355  21.325  55.456  1.00 76.69  ? 82  ASP A CB   1 
ATOM   1268  C CG   . ASP A 1 82  ? 20.768  22.470  56.380  1.00 75.86  ? 82  ASP A CG   1 
ATOM   1269  O OD1  . ASP A 1 82  ? 20.182  23.575  56.302  1.00 75.96  ? 82  ASP A OD1  1 
ATOM   1270  O OD2  . ASP A 1 82  ? 21.681  22.251  57.202  1.00 74.94  ? 82  ASP A OD2  1 
ATOM   1271  H H    . ASP A 1 82  ? 20.189  20.019  53.292  1.00 88.89  ? 82  ASP A H    1 
ATOM   1272  H HA   . ASP A 1 82  ? 19.107  22.337  54.173  1.00 88.46  ? 82  ASP A HA   1 
ATOM   1273  H HB2  . ASP A 1 82  ? 19.621  20.851  55.877  1.00 92.03  ? 82  ASP A HB2  1 
ATOM   1274  H HB3  . ASP A 1 82  ? 21.117  20.733  55.355  1.00 92.03  ? 82  ASP A HB3  1 
ATOM   1275  N N    . LYS A 1 83  ? 20.621  23.924  53.124  1.00 72.91  ? 83  LYS A N    1 
ATOM   1276  C CA   . LYS A 1 83  ? 21.580  24.843  52.525  1.00 73.11  ? 83  LYS A CA   1 
ATOM   1277  C C    . LYS A 1 83  ? 22.806  25.033  53.407  1.00 77.14  ? 83  LYS A C    1 
ATOM   1278  O O    . LYS A 1 83  ? 23.896  25.322  52.895  1.00 76.35  ? 83  LYS A O    1 
ATOM   1279  C CB   . LYS A 1 83  ? 20.912  26.193  52.274  1.00 76.32  ? 83  LYS A CB   1 
ATOM   1280  C CG   . LYS A 1 83  ? 20.564  26.939  53.556  1.00 74.73  ? 83  LYS A CG   1 
ATOM   1281  C CD   . LYS A 1 83  ? 19.844  28.250  53.274  1.00 78.01  ? 83  LYS A CD   1 
ATOM   1282  C CE   . LYS A 1 83  ? 18.967  28.670  54.452  1.00 82.34  ? 83  LYS A CE   1 
ATOM   1283  N NZ   . LYS A 1 83  ? 18.483  27.513  55.271  1.00 86.01  ? 83  LYS A NZ   1 
ATOM   1284  H H    . LYS A 1 83  ? 19.837  24.255  53.249  1.00 87.49  ? 83  LYS A H    1 
ATOM   1285  H HA   . LYS A 1 83  ? 21.871  24.476  51.676  1.00 87.72  ? 83  LYS A HA   1 
ATOM   1286  H HB2  . LYS A 1 83  ? 21.516  26.751  51.759  1.00 91.58  ? 83  LYS A HB2  1 
ATOM   1287  H HB3  . LYS A 1 83  ? 20.090  26.050  51.780  1.00 91.58  ? 83  LYS A HB3  1 
ATOM   1288  H HG2  . LYS A 1 83  ? 19.983  26.385  54.100  1.00 89.68  ? 83  LYS A HG2  1 
ATOM   1289  H HG3  . LYS A 1 83  ? 21.380  27.140  54.041  1.00 89.68  ? 83  LYS A HG3  1 
ATOM   1290  H HD2  . LYS A 1 83  ? 20.498  28.948  53.115  1.00 93.61  ? 83  LYS A HD2  1 
ATOM   1291  H HD3  . LYS A 1 83  ? 19.277  28.144  52.494  1.00 93.61  ? 83  LYS A HD3  1 
ATOM   1292  H HE2  . LYS A 1 83  ? 19.480  29.253  55.034  1.00 98.81  ? 83  LYS A HE2  1 
ATOM   1293  H HE3  . LYS A 1 83  ? 18.190  29.141  54.113  1.00 98.81  ? 83  LYS A HE3  1 
ATOM   1294  H HZ1  . LYS A 1 83  ? 17.948  27.802  55.920  1.00 103.21 ? 83  LYS A HZ1  1 
ATOM   1295  H HZ2  . LYS A 1 83  ? 18.032  26.944  54.756  1.00 103.21 ? 83  LYS A HZ2  1 
ATOM   1296  H HZ3  . LYS A 1 83  ? 19.175  27.087  55.635  1.00 103.21 ? 83  LYS A HZ3  1 
ATOM   1297  N N    . ASP A 1 84  ? 22.644  24.889  54.729  1.00 77.64  ? 84  ASP A N    1 
ATOM   1298  C CA   . ASP A 1 84  ? 23.688  25.200  55.695  1.00 76.30  ? 84  ASP A CA   1 
ATOM   1299  C C    . ASP A 1 84  ? 24.582  24.010  56.027  1.00 78.77  ? 84  ASP A C    1 
ATOM   1300  O O    . ASP A 1 84  ? 25.616  24.196  56.682  1.00 77.75  ? 84  ASP A O    1 
ATOM   1301  C CB   . ASP A 1 84  ? 23.067  25.718  57.006  1.00 78.34  ? 84  ASP A CB   1 
ATOM   1302  C CG   . ASP A 1 84  ? 22.265  27.007  56.821  1.00 77.93  ? 84  ASP A CG   1 
ATOM   1303  O OD1  . ASP A 1 84  ? 22.872  28.076  56.583  1.00 72.01  ? 84  ASP A OD1  1 
ATOM   1304  O OD2  . ASP A 1 84  ? 21.019  26.955  56.940  1.00 79.08  ? 84  ASP A OD2  1 
ATOM   1305  H H    . ASP A 1 84  ? 21.918  24.606  55.093  1.00 93.17  ? 84  ASP A H    1 
ATOM   1306  H HA   . ASP A 1 84  ? 24.242  25.900  55.317  1.00 91.56  ? 84  ASP A HA   1 
ATOM   1307  H HB2  . ASP A 1 84  ? 22.468  25.042  57.360  1.00 94.01  ? 84  ASP A HB2  1 
ATOM   1308  H HB3  . ASP A 1 84  ? 23.777  25.897  57.641  1.00 94.01  ? 84  ASP A HB3  1 
ATOM   1309  N N    . PHE A 1 85  ? 24.215  22.798  55.612  1.00 79.98  ? 85  PHE A N    1 
ATOM   1310  C CA   . PHE A 1 85  ? 25.047  21.642  55.909  1.00 80.56  ? 85  PHE A CA   1 
ATOM   1311  C C    . PHE A 1 85  ? 26.401  21.781  55.228  1.00 83.33  ? 85  PHE A C    1 
ATOM   1312  O O    . PHE A 1 85  ? 26.481  22.056  54.028  1.00 83.47  ? 85  PHE A O    1 
ATOM   1313  C CB   . PHE A 1 85  ? 24.373  20.354  55.451  1.00 79.28  ? 85  PHE A CB   1 
ATOM   1314  C CG   . PHE A 1 85  ? 25.182  19.119  55.740  1.00 83.77  ? 85  PHE A CG   1 
ATOM   1315  C CD1  . PHE A 1 85  ? 25.131  18.513  56.988  1.00 80.50  ? 85  PHE A CD1  1 
ATOM   1316  C CD2  . PHE A 1 85  ? 26.006  18.572  54.767  1.00 82.28  ? 85  PHE A CD2  1 
ATOM   1317  C CE1  . PHE A 1 85  ? 25.879  17.380  57.253  1.00 80.58  ? 85  PHE A CE1  1 
ATOM   1318  C CE2  . PHE A 1 85  ? 26.759  17.437  55.029  1.00 83.00  ? 85  PHE A CE2  1 
ATOM   1319  C CZ   . PHE A 1 85  ? 26.695  16.843  56.272  1.00 81.62  ? 85  PHE A CZ   1 
ATOM   1320  H H    . PHE A 1 85  ? 23.500  22.625  55.165  1.00 95.98  ? 85  PHE A H    1 
ATOM   1321  H HA   . PHE A 1 85  ? 25.175  21.590  56.869  1.00 96.67  ? 85  PHE A HA   1 
ATOM   1322  H HB2  . PHE A 1 85  ? 23.523  20.266  55.908  1.00 95.13  ? 85  PHE A HB2  1 
ATOM   1323  H HB3  . PHE A 1 85  ? 24.231  20.399  54.492  1.00 95.13  ? 85  PHE A HB3  1 
ATOM   1324  H HD1  . PHE A 1 85  ? 24.588  18.872  57.652  1.00 96.59  ? 85  PHE A HD1  1 
ATOM   1325  H HD2  . PHE A 1 85  ? 26.055  18.972  53.929  1.00 98.73  ? 85  PHE A HD2  1 
ATOM   1326  H HE1  . PHE A 1 85  ? 25.834  16.979  58.091  1.00 96.70  ? 85  PHE A HE1  1 
ATOM   1327  H HE2  . PHE A 1 85  ? 27.305  17.078  54.368  1.00 99.60  ? 85  PHE A HE2  1 
ATOM   1328  H HZ   . PHE A 1 85  ? 27.199  16.083  56.451  1.00 97.94  ? 85  PHE A HZ   1 
ATOM   1329  N N    . SER A 1 86  ? 27.469  21.591  56.005  1.00 86.18  ? 86  SER A N    1 
ATOM   1330  C CA   . SER A 1 86  ? 28.819  21.600  55.469  1.00 94.48  ? 86  SER A CA   1 
ATOM   1331  C C    . SER A 1 86  ? 29.367  20.197  55.611  1.00 95.85  ? 86  SER A C    1 
ATOM   1332  O O    . SER A 1 86  ? 29.137  19.347  54.726  1.00 103.31 ? 86  SER A O    1 
ATOM   1333  C CB   . SER A 1 86  ? 29.667  22.669  56.173  1.00 89.97  ? 86  SER A CB   1 
ATOM   1334  O OG   . SER A 1 86  ? 29.525  22.570  57.576  1.00 95.61  ? 86  SER A OG   1 
ATOM   1335  H H    . SER A 1 86  ? 27.433  21.454  56.854  1.00 103.42 ? 86  SER A H    1 
ATOM   1336  H HA   . SER A 1 86  ? 28.785  21.822  54.525  1.00 113.37 ? 86  SER A HA   1 
ATOM   1337  H HB2  . SER A 1 86  ? 30.599  22.539  55.938  1.00 107.97 ? 86  SER A HB2  1 
ATOM   1338  H HB3  . SER A 1 86  ? 29.373  23.548  55.885  1.00 107.97 ? 86  SER A HB3  1 
ATOM   1339  H HG   . SER A 1 86  ? 29.983  23.164  57.954  1.00 114.73 ? 86  SER A HG   1 
ATOM   1340  N N    . LYS A 1 87  ? 30.087  19.877  56.685  1.00 89.67  ? 87  LYS A N    1 
ATOM   1341  C CA   . LYS A 1 87  ? 30.591  18.531  56.930  1.00 90.71  ? 87  LYS A CA   1 
ATOM   1342  C C    . LYS A 1 87  ? 29.822  17.793  58.014  1.00 90.82  ? 87  LYS A C    1 
ATOM   1343  O O    . LYS A 1 87  ? 29.566  16.596  57.869  1.00 89.21  ? 87  LYS A O    1 
ATOM   1344  C CB   . LYS A 1 87  ? 32.077  18.588  57.314  1.00 95.52  ? 87  LYS A CB   1 
ATOM   1345  C CG   . LYS A 1 87  ? 32.629  17.332  58.002  1.00 99.06  ? 87  LYS A CG   1 
ATOM   1346  C CD   . LYS A 1 87  ? 32.380  16.064  57.187  1.00 97.68  ? 87  LYS A CD   1 
ATOM   1347  C CE   . LYS A 1 87  ? 33.614  15.162  57.144  1.00 96.89  ? 87  LYS A CE   1 
ATOM   1348  N NZ   . LYS A 1 87  ? 34.544  15.517  56.028  1.00 103.74 ? 87  LYS A NZ   1 
ATOM   1349  H H    . LYS A 1 87  ? 30.300  20.438  57.300  1.00 107.60 ? 87  LYS A H    1 
ATOM   1350  H HA   . LYS A 1 87  ? 30.517  18.014  56.113  1.00 108.86 ? 87  LYS A HA   1 
ATOM   1351  H HB2  . LYS A 1 87  ? 32.595  18.727  56.506  1.00 114.63 ? 87  LYS A HB2  1 
ATOM   1352  H HB3  . LYS A 1 87  ? 32.206  19.332  57.923  1.00 114.63 ? 87  LYS A HB3  1 
ATOM   1353  H HG2  . LYS A 1 87  ? 33.586  17.429  58.121  1.00 118.88 ? 87  LYS A HG2  1 
ATOM   1354  H HG3  . LYS A 1 87  ? 32.196  17.225  58.864  1.00 118.88 ? 87  LYS A HG3  1 
ATOM   1355  H HD2  . LYS A 1 87  ? 31.652  15.564  57.589  1.00 117.22 ? 87  LYS A HD2  1 
ATOM   1356  H HD3  . LYS A 1 87  ? 32.151  16.310  56.277  1.00 117.22 ? 87  LYS A HD3  1 
ATOM   1357  H HE2  . LYS A 1 87  ? 34.099  15.248  57.979  1.00 116.27 ? 87  LYS A HE2  1 
ATOM   1358  H HE3  . LYS A 1 87  ? 33.330  14.243  57.018  1.00 116.27 ? 87  LYS A HE3  1 
ATOM   1359  H HZ1  . LYS A 1 87  ? 35.248  14.972  56.034  1.00 124.49 ? 87  LYS A HZ1  1 
ATOM   1360  H HZ2  . LYS A 1 87  ? 34.126  15.439  55.247  1.00 124.49 ? 87  LYS A HZ2  1 
ATOM   1361  H HZ3  . LYS A 1 87  ? 34.827  16.355  56.123  1.00 124.49 ? 87  LYS A HZ3  1 
ATOM   1362  N N    . GLN A 1 88  ? 29.439  18.480  59.093  1.00 84.67  ? 88  GLN A N    1 
ATOM   1363  C CA   . GLN A 1 88  ? 28.768  17.865  60.230  1.00 80.94  ? 88  GLN A CA   1 
ATOM   1364  C C    . GLN A 1 88  ? 27.619  18.747  60.695  1.00 78.94  ? 88  GLN A C    1 
ATOM   1365  O O    . GLN A 1 88  ? 27.717  19.977  60.666  1.00 79.81  ? 88  GLN A O    1 
ATOM   1366  C CB   . GLN A 1 88  ? 29.747  17.641  61.394  1.00 82.75  ? 88  GLN A CB   1 
ATOM   1367  C CG   . GLN A 1 88  ? 29.178  16.865  62.570  1.00 77.99  ? 88  GLN A CG   1 
ATOM   1368  C CD   . GLN A 1 88  ? 28.342  17.728  63.500  1.00 81.81  ? 88  GLN A CD   1 
ATOM   1369  O OE1  . GLN A 1 88  ? 27.221  17.365  63.858  1.00 81.35  ? 88  GLN A OE1  1 
ATOM   1370  N NE2  . GLN A 1 88  ? 28.883  18.881  63.893  1.00 83.52  ? 88  GLN A NE2  1 
ATOM   1371  H H    . GLN A 1 88  ? 29.562  19.326  59.188  1.00 101.60 ? 88  GLN A H    1 
ATOM   1372  H HA   . GLN A 1 88  ? 28.398  17.010  59.959  1.00 97.13  ? 88  GLN A HA   1 
ATOM   1373  H HB2  . GLN A 1 88  ? 30.512  17.146  61.061  1.00 99.30  ? 88  GLN A HB2  1 
ATOM   1374  H HB3  . GLN A 1 88  ? 30.032  18.507  61.727  1.00 99.30  ? 88  GLN A HB3  1 
ATOM   1375  H HG2  . GLN A 1 88  ? 28.613  16.152  62.234  1.00 93.59  ? 88  GLN A HG2  1 
ATOM   1376  H HG3  . GLN A 1 88  ? 29.910  16.492  63.086  1.00 93.59  ? 88  GLN A HG3  1 
ATOM   1377  H HE21 . GLN A 1 88  ? 29.668  19.102  63.621  1.00 100.23 ? 88  GLN A HE21 1 
ATOM   1378  H HE22 . GLN A 1 88  ? 28.448  19.403  64.420  1.00 100.23 ? 88  GLN A HE22 1 
ATOM   1379  N N    . LYS A 1 89  ? 26.532  18.113  61.132  1.00 75.89  ? 89  LYS A N    1 
ATOM   1380  C CA   . LYS A 1 89  ? 25.399  18.842  61.689  1.00 76.04  ? 89  LYS A CA   1 
ATOM   1381  C C    . LYS A 1 89  ? 24.429  17.882  62.367  1.00 76.93  ? 89  LYS A C    1 
ATOM   1382  O O    . LYS A 1 89  ? 24.036  16.870  61.779  1.00 78.99  ? 89  LYS A O    1 
ATOM   1383  C CB   . LYS A 1 89  ? 24.681  19.645  60.602  1.00 76.03  ? 89  LYS A CB   1 
ATOM   1384  C CG   . LYS A 1 89  ? 23.429  20.367  61.081  1.00 74.68  ? 89  LYS A CG   1 
ATOM   1385  C CD   . LYS A 1 89  ? 23.483  21.846  60.723  1.00 76.58  ? 89  LYS A CD   1 
ATOM   1386  C CE   . LYS A 1 89  ? 22.110  22.498  60.807  1.00 76.07  ? 89  LYS A CE   1 
ATOM   1387  N NZ   . LYS A 1 89  ? 22.212  23.990  60.873  1.00 78.01  ? 89  LYS A NZ   1 
ATOM   1388  H H    . LYS A 1 89  ? 26.428  17.259  61.115  1.00 91.06  ? 89  LYS A H    1 
ATOM   1389  H HA   . LYS A 1 89  ? 25.724  19.469  62.354  1.00 91.24  ? 89  LYS A HA   1 
ATOM   1390  H HB2  . LYS A 1 89  ? 25.292  20.314  60.256  1.00 91.24  ? 89  LYS A HB2  1 
ATOM   1391  H HB3  . LYS A 1 89  ? 24.417  19.038  59.892  1.00 91.24  ? 89  LYS A HB3  1 
ATOM   1392  H HG2  . LYS A 1 89  ? 22.648  19.977  60.657  1.00 89.62  ? 89  LYS A HG2  1 
ATOM   1393  H HG3  . LYS A 1 89  ? 23.358  20.287  62.045  1.00 89.62  ? 89  LYS A HG3  1 
ATOM   1394  H HD2  . LYS A 1 89  ? 24.074  22.303  61.341  1.00 91.90  ? 89  LYS A HD2  1 
ATOM   1395  H HD3  . LYS A 1 89  ? 23.811  21.944  59.816  1.00 91.90  ? 89  LYS A HD3  1 
ATOM   1396  H HE2  . LYS A 1 89  ? 21.595  22.263  60.019  1.00 91.28  ? 89  LYS A HE2  1 
ATOM   1397  H HE3  . LYS A 1 89  ? 21.656  22.188  61.606  1.00 91.28  ? 89  LYS A HE3  1 
ATOM   1398  H HZ1  . LYS A 1 89  ? 22.674  24.232  61.594  1.00 93.62  ? 89  LYS A HZ1  1 
ATOM   1399  H HZ2  . LYS A 1 89  ? 21.399  24.349  60.916  1.00 93.62  ? 89  LYS A HZ2  1 
ATOM   1400  H HZ3  . LYS A 1 89  ? 22.626  24.299  60.148  1.00 93.62  ? 89  LYS A HZ3  1 
ATOM   1401  N N    . ASN A 1 90  ? 24.041  18.192  63.601  1.00 77.89  ? 90  ASN A N    1 
ATOM   1402  C CA   . ASN A 1 90  ? 23.082  17.375  64.333  1.00 77.25  ? 90  ASN A CA   1 
ATOM   1403  C C    . ASN A 1 90  ? 21.664  17.776  63.949  1.00 76.74  ? 90  ASN A C    1 
ATOM   1404  O O    . ASN A 1 90  ? 21.341  18.968  63.886  1.00 77.31  ? 90  ASN A O    1 
ATOM   1405  C CB   . ASN A 1 90  ? 23.286  17.537  65.836  1.00 77.28  ? 90  ASN A CB   1 
ATOM   1406  C CG   . ASN A 1 90  ? 24.271  16.530  66.401  1.00 81.78  ? 90  ASN A CG   1 
ATOM   1407  O OD1  . ASN A 1 90  ? 23.886  15.579  67.093  1.00 82.64  ? 90  ASN A OD1  1 
ATOM   1408  N ND2  . ASN A 1 90  ? 25.553  16.733  66.112  1.00 81.80  ? 90  ASN A ND2  1 
ATOM   1409  H H    . ASN A 1 90  ? 24.321  18.876  64.039  1.00 93.46  ? 90  ASN A H    1 
ATOM   1410  H HA   . ASN A 1 90  ? 23.212  16.441  64.107  1.00 92.70  ? 90  ASN A HA   1 
ATOM   1411  H HB2  . ASN A 1 90  ? 23.629  18.426  66.015  1.00 92.74  ? 90  ASN A HB2  1 
ATOM   1412  H HB3  . ASN A 1 90  ? 22.436  17.412  66.286  1.00 92.74  ? 90  ASN A HB3  1 
ATOM   1413  H HD21 . ASN A 1 90  ? 26.152  16.191  66.409  1.00 98.16  ? 90  ASN A HD21 1 
ATOM   1414  H HD22 . ASN A 1 90  ? 25.784  17.406  65.629  1.00 98.16  ? 90  ASN A HD22 1 
ATOM   1415  N N    . TYR A 1 91  ? 20.819  16.783  63.689  1.00 75.30  ? 91  TYR A N    1 
ATOM   1416  C CA   . TYR A 1 91  ? 19.436  17.012  63.294  1.00 75.62  ? 91  TYR A CA   1 
ATOM   1417  C C    . TYR A 1 91  ? 18.510  16.309  64.273  1.00 76.44  ? 91  TYR A C    1 
ATOM   1418  O O    . TYR A 1 91  ? 18.685  15.118  64.556  1.00 81.34  ? 91  TYR A O    1 
ATOM   1419  C CB   . TYR A 1 91  ? 19.181  16.513  61.872  1.00 75.32  ? 91  TYR A CB   1 
ATOM   1420  C CG   . TYR A 1 91  ? 19.835  17.361  60.805  1.00 74.09  ? 91  TYR A CG   1 
ATOM   1421  C CD1  . TYR A 1 91  ? 19.262  18.557  60.391  1.00 71.70  ? 91  TYR A CD1  1 
ATOM   1422  C CD2  . TYR A 1 91  ? 21.028  16.969  60.218  1.00 74.91  ? 91  TYR A CD2  1 
ATOM   1423  C CE1  . TYR A 1 91  ? 19.859  19.337  59.423  1.00 75.05  ? 91  TYR A CE1  1 
ATOM   1424  C CE2  . TYR A 1 91  ? 21.631  17.740  59.246  1.00 78.02  ? 91  TYR A CE2  1 
ATOM   1425  C CZ   . TYR A 1 91  ? 21.042  18.919  58.845  1.00 76.85  ? 91  TYR A CZ   1 
ATOM   1426  O OH   . TYR A 1 91  ? 21.655  19.682  57.871  1.00 75.11  ? 91  TYR A OH   1 
ATOM   1427  H H    . TYR A 1 91  ? 21.029  15.951  63.737  1.00 90.36  ? 91  TYR A H    1 
ATOM   1428  H HA   . TYR A 1 91  ? 19.245  17.962  63.322  1.00 90.74  ? 91  TYR A HA   1 
ATOM   1429  H HB2  . TYR A 1 91  ? 19.530  15.612  61.790  1.00 90.38  ? 91  TYR A HB2  1 
ATOM   1430  H HB3  . TYR A 1 91  ? 18.225  16.514  61.708  1.00 90.38  ? 91  TYR A HB3  1 
ATOM   1431  H HD1  . TYR A 1 91  ? 18.461  18.836  60.774  1.00 86.04  ? 91  TYR A HD1  1 
ATOM   1432  H HD2  . TYR A 1 91  ? 21.428  16.173  60.483  1.00 89.89  ? 91  TYR A HD2  1 
ATOM   1433  H HE1  . TYR A 1 91  ? 19.468  20.139  59.161  1.00 90.06  ? 91  TYR A HE1  1 
ATOM   1434  H HE2  . TYR A 1 91  ? 22.433  17.464  58.863  1.00 93.62  ? 91  TYR A HE2  1 
ATOM   1435  H HH   . TYR A 1 91  ? 21.240  20.406  57.770  1.00 90.13  ? 91  TYR A HH   1 
ATOM   1436  N N    . ASN A 1 92  ? 17.530  17.046  64.787  1.00 75.27  ? 92  ASN A N    1 
ATOM   1437  C CA   . ASN A 1 92  ? 16.560  16.507  65.732  1.00 79.77  ? 92  ASN A CA   1 
ATOM   1438  C C    . ASN A 1 92  ? 15.327  16.038  64.971  1.00 75.82  ? 92  ASN A C    1 
ATOM   1439  O O    . ASN A 1 92  ? 14.764  16.789  64.167  1.00 74.45  ? 92  ASN A O    1 
ATOM   1440  C CB   . ASN A 1 92  ? 16.175  17.562  66.771  1.00 79.52  ? 92  ASN A CB   1 
ATOM   1441  C CG   . ASN A 1 92  ? 17.280  17.820  67.786  1.00 80.85  ? 92  ASN A CG   1 
ATOM   1442  O OD1  . ASN A 1 92  ? 17.922  16.893  68.277  1.00 82.15  ? 92  ASN A OD1  1 
ATOM   1443  N ND2  . ASN A 1 92  ? 17.499  19.086  68.107  1.00 85.40  ? 92  ASN A ND2  1 
ATOM   1444  H H    . ASN A 1 92  ? 17.405  17.876  64.601  1.00 90.33  ? 92  ASN A H    1 
ATOM   1445  H HA   . ASN A 1 92  ? 16.945  15.750  66.201  1.00 95.72  ? 92  ASN A HA   1 
ATOM   1446  H HB2  . ASN A 1 92  ? 15.983  18.398  66.317  1.00 95.42  ? 92  ASN A HB2  1 
ATOM   1447  H HB3  . ASN A 1 92  ? 15.389  17.259  67.253  1.00 95.42  ? 92  ASN A HB3  1 
ATOM   1448  H HD21 . ASN A 1 92  ? 17.028  19.709  67.747  1.00 102.48 ? 92  ASN A HD21 1 
ATOM   1449  H HD22 . ASN A 1 92  ? 18.112  19.286  68.676  1.00 102.48 ? 92  ASN A HD22 1 
ATOM   1450  N N    . ILE A 1 93  ? 14.910  14.796  65.224  1.00 77.39  ? 93  ILE A N    1 
ATOM   1451  C CA   . ILE A 1 93  ? 13.781  14.192  64.530  1.00 80.15  ? 93  ILE A CA   1 
ATOM   1452  C C    . ILE A 1 93  ? 12.986  13.344  65.516  1.00 81.05  ? 93  ILE A C    1 
ATOM   1453  O O    . ILE A 1 93  ? 13.415  13.085  66.640  1.00 81.99  ? 93  ILE A O    1 
ATOM   1454  C CB   . ILE A 1 93  ? 14.221  13.328  63.324  1.00 80.31  ? 93  ILE A CB   1 
ATOM   1455  C CG1  . ILE A 1 93  ? 15.294  12.319  63.745  1.00 82.54  ? 93  ILE A CG1  1 
ATOM   1456  C CG2  . ILE A 1 93  ? 14.742  14.200  62.186  1.00 74.97  ? 93  ILE A CG2  1 
ATOM   1457  C CD1  . ILE A 1 93  ? 15.055  10.914  63.225  1.00 77.51  ? 93  ILE A CD1  1 
ATOM   1458  H H    . ILE A 1 93  ? 15.275  14.278  65.805  1.00 92.87  ? 93  ILE A H    1 
ATOM   1459  H HA   . ILE A 1 93  ? 13.204  14.901  64.206  1.00 96.19  ? 93  ILE A HA   1 
ATOM   1460  H HB   . ILE A 1 93  ? 13.440  12.845  63.010  1.00 96.37  ? 93  ILE A HB   1 
ATOM   1461  H HG12 . ILE A 1 93  ? 16.152  12.617  63.405  1.00 99.05  ? 93  ILE A HG12 1 
ATOM   1462  H HG13 . ILE A 1 93  ? 15.317  12.275  64.713  1.00 99.05  ? 93  ILE A HG13 1 
ATOM   1463  H HG21 . ILE A 1 93  ? 14.988  13.631  61.440  1.00 89.97  ? 93  ILE A HG21 1 
ATOM   1464  H HG22 . ILE A 1 93  ? 14.045  14.817  61.916  1.00 89.97  ? 93  ILE A HG22 1 
ATOM   1465  H HG23 . ILE A 1 93  ? 15.518  14.692  62.496  1.00 89.97  ? 93  ILE A HG23 1 
ATOM   1466  H HD11 . ILE A 1 93  ? 15.770  10.337  63.536  1.00 93.02  ? 93  ILE A HD11 1 
ATOM   1467  H HD12 . ILE A 1 93  ? 14.203  10.594  63.560  1.00 93.02  ? 93  ILE A HD12 1 
ATOM   1468  H HD13 . ILE A 1 93  ? 15.043  10.934  62.255  1.00 93.02  ? 93  ILE A HD13 1 
ATOM   1469  N N    . THR A 1 94  ? 11.808  12.913  65.072  1.00 83.03  ? 94  THR A N    1 
ATOM   1470  C CA   . THR A 1 94  ? 10.963  12.000  65.825  1.00 80.93  ? 94  THR A CA   1 
ATOM   1471  C C    . THR A 1 94  ? 10.548  10.847  64.917  1.00 83.16  ? 94  THR A C    1 
ATOM   1472  O O    . THR A 1 94  ? 10.420  11.009  63.698  1.00 80.31  ? 94  THR A O    1 
ATOM   1473  C CB   . THR A 1 94  ? 9.719   12.706  66.379  1.00 81.49  ? 94  THR A CB   1 
ATOM   1474  O OG1  . THR A 1 94  ? 8.716   12.777  65.359  1.00 83.99  ? 94  THR A OG1  1 
ATOM   1475  C CG2  . THR A 1 94  ? 10.066  14.112  66.853  1.00 86.88  ? 94  THR A CG2  1 
ATOM   1476  H H    . THR A 1 94  ? 11.470  13.144  64.316  1.00 99.64  ? 94  THR A H    1 
ATOM   1477  H HA   . THR A 1 94  ? 11.456  11.638  66.578  1.00 97.12  ? 94  THR A HA   1 
ATOM   1478  H HB   . THR A 1 94  ? 9.375   12.208  67.137  1.00 97.78  ? 94  THR A HB   1 
ATOM   1479  H HG1  . THR A 1 94  ? 8.033   13.166  65.655  1.00 100.79 ? 94  THR A HG1  1 
ATOM   1480  H HG21 . THR A 1 94  ? 9.328   14.481  67.364  1.00 104.26 ? 94  THR A HG21 1 
ATOM   1481  H HG22 . THR A 1 94  ? 10.856  14.087  67.415  1.00 104.26 ? 94  THR A HG22 1 
ATOM   1482  H HG23 . THR A 1 94  ? 10.239  14.686  66.091  1.00 104.26 ? 94  THR A HG23 1 
ATOM   1483  N N    . CYS A 1 95  ? 10.340  9.680   65.526  1.00 85.14  ? 95  CYS A N    1 
ATOM   1484  C CA   . CYS A 1 95  ? 9.969   8.472   64.808  1.00 80.68  ? 95  CYS A CA   1 
ATOM   1485  C C    . CYS A 1 95  ? 8.896   7.729   65.586  1.00 79.99  ? 95  CYS A C    1 
ATOM   1486  O O    . CYS A 1 95  ? 8.905   7.721   66.818  1.00 85.19  ? 95  CYS A O    1 
ATOM   1487  C CB   . CYS A 1 95  ? 11.184  7.555   64.593  1.00 81.97  ? 95  CYS A CB   1 
ATOM   1488  S SG   . CYS A 1 95  ? 10.894  6.162   63.470  1.00 67.56  ? 95  CYS A SG   1 
ATOM   1489  H H    . CYS A 1 95  ? 10.410  9.565   66.376  1.00 102.17 ? 95  CYS A H    1 
ATOM   1490  H HA   . CYS A 1 95  ? 9.606   8.710   63.940  1.00 96.81  ? 95  CYS A HA   1 
ATOM   1491  H HB2  . CYS A 1 95  ? 11.907  8.085   64.221  1.00 98.36  ? 95  CYS A HB2  1 
ATOM   1492  H HB3  . CYS A 1 95  ? 11.449  7.189   65.451  1.00 98.36  ? 95  CYS A HB3  1 
ATOM   1493  H HG   . CYS A 1 95  ? 11.923  5.563   63.317  1.00 81.07  ? 95  CYS A HG   1 
ATOM   1494  N N    . SER A 1 96  ? 7.971   7.107   64.857  1.00 83.21  ? 96  SER A N    1 
ATOM   1495  C CA   . SER A 1 96  ? 6.952   6.283   65.494  1.00 82.08  ? 96  SER A CA   1 
ATOM   1496  C C    . SER A 1 96  ? 7.602   5.082   66.171  1.00 78.72  ? 96  SER A C    1 
ATOM   1497  O O    . SER A 1 96  ? 8.418   4.377   65.569  1.00 79.68  ? 96  SER A O    1 
ATOM   1498  C CB   . SER A 1 96  ? 5.928   5.825   64.452  1.00 81.49  ? 96  SER A CB   1 
ATOM   1499  O OG   . SER A 1 96  ? 6.566   5.340   63.287  1.00 77.74  ? 96  SER A OG   1 
ATOM   1500  H H    . SER A 1 96  ? 7.913   7.148   64.000  1.00 99.85  ? 96  SER A H    1 
ATOM   1501  H HA   . SER A 1 96  ? 6.485   6.798   66.169  1.00 98.50  ? 96  SER A HA   1 
ATOM   1502  H HB2  . SER A 1 96  ? 5.387   5.115   64.833  1.00 97.79  ? 96  SER A HB2  1 
ATOM   1503  H HB3  . SER A 1 96  ? 5.365   6.578   64.212  1.00 97.79  ? 96  SER A HB3  1 
ATOM   1504  H HG   . SER A 1 96  ? 7.055   4.684   63.479  1.00 93.29  ? 96  SER A HG   1 
ATOM   1505  N N    . GLY A 1 97  ? 7.241   4.856   67.436  1.00 83.02  ? 97  GLY A N    1 
ATOM   1506  C CA   . GLY A 1 97  ? 7.812   3.783   68.224  1.00 80.60  ? 97  GLY A CA   1 
ATOM   1507  C C    . GLY A 1 97  ? 8.862   4.218   69.225  1.00 78.86  ? 97  GLY A C    1 
ATOM   1508  O O    . GLY A 1 97  ? 9.225   3.422   70.102  1.00 79.14  ? 97  GLY A O    1 
ATOM   1509  H H    . GLY A 1 97  ? 6.656   5.323   67.859  1.00 99.63  ? 97  GLY A H    1 
ATOM   1510  H HA2  . GLY A 1 97  ? 7.100   3.345   68.715  1.00 96.72  ? 97  GLY A HA2  1 
ATOM   1511  H HA3  . GLY A 1 97  ? 8.224   3.142   67.624  1.00 96.72  ? 97  GLY A HA3  1 
ATOM   1512  N N    . GLU A 1 98  ? 9.375   5.438   69.105  1.00 79.06  ? 98  GLU A N    1 
ATOM   1513  C CA   . GLU A 1 98  ? 10.265  6.038   70.088  1.00 81.63  ? 98  GLU A CA   1 
ATOM   1514  C C    . GLU A 1 98  ? 9.609   7.324   70.567  1.00 87.31  ? 98  GLU A C    1 
ATOM   1515  O O    . GLU A 1 98  ? 9.177   8.145   69.750  1.00 86.37  ? 98  GLU A O    1 
ATOM   1516  C CB   . GLU A 1 98  ? 11.647  6.326   69.503  1.00 83.69  ? 98  GLU A CB   1 
ATOM   1517  C CG   . GLU A 1 98  ? 12.578  7.085   70.443  1.00 87.38  ? 98  GLU A CG   1 
ATOM   1518  C CD   . GLU A 1 98  ? 13.045  6.246   71.617  1.00 92.93  ? 98  GLU A CD   1 
ATOM   1519  O OE1  . GLU A 1 98  ? 13.694  5.208   71.374  1.00 92.25  ? 98  GLU A OE1  1 
ATOM   1520  O OE2  . GLU A 1 98  ? 12.761  6.623   72.776  1.00 94.45  ? 98  GLU A OE2  1 
ATOM   1521  H H    . GLU A 1 98  ? 9.214   5.956   68.437  1.00 94.87  ? 98  GLU A H    1 
ATOM   1522  H HA   . GLU A 1 98  ? 10.395  5.437   70.838  1.00 97.96  ? 98  GLU A HA   1 
ATOM   1523  H HB2  . GLU A 1 98  ? 12.073  5.482   69.285  1.00 100.43 ? 98  GLU A HB2  1 
ATOM   1524  H HB3  . GLU A 1 98  ? 11.539  6.860   68.700  1.00 100.43 ? 98  GLU A HB3  1 
ATOM   1525  H HG2  . GLU A 1 98  ? 13.362  7.370   69.948  1.00 104.85 ? 98  GLU A HG2  1 
ATOM   1526  H HG3  . GLU A 1 98  ? 12.108  7.858   70.795  1.00 104.85 ? 98  GLU A HG3  1 
ATOM   1527  N N    . SER A 1 99  ? 9.531   7.493   71.884  1.00 89.80  ? 99  SER A N    1 
ATOM   1528  C CA   . SER A 1 99  ? 8.875   8.656   72.457  1.00 91.40  ? 99  SER A CA   1 
ATOM   1529  C C    . SER A 1 99  ? 9.795   9.859   72.576  1.00 95.15  ? 99  SER A C    1 
ATOM   1530  O O    . SER A 1 99  ? 9.303   10.989  72.669  1.00 100.16 ? 99  SER A O    1 
ATOM   1531  C CB   . SER A 1 99  ? 8.320   8.314   73.842  1.00 93.36  ? 99  SER A CB   1 
ATOM   1532  O OG   . SER A 1 99  ? 9.249   7.535   74.575  1.00 95.15  ? 99  SER A OG   1 
ATOM   1533  H H    . SER A 1 99  ? 9.851   6.945   72.465  1.00 107.76 ? 99  SER A H    1 
ATOM   1534  H HA   . SER A 1 99  ? 8.131   8.906   71.887  1.00 109.68 ? 99  SER A HA   1 
ATOM   1535  H HB2  . SER A 1 99  ? 8.146   9.137   74.325  1.00 112.03 ? 99  SER A HB2  1 
ATOM   1536  H HB3  . SER A 1 99  ? 7.498   7.811   73.737  1.00 112.03 ? 99  SER A HB3  1 
ATOM   1537  H HG   . SER A 1 99  ? 8.931   7.343   75.328  1.00 114.18 ? 99  SER A HG   1 
ATOM   1538  N N    . LYS A 1 100 ? 11.106  9.650   72.573  1.00 93.60  ? 100 LYS A N    1 
ATOM   1539  C CA   . LYS A 1 100 ? 12.049  10.741  72.767  1.00 97.43  ? 100 LYS A CA   1 
ATOM   1540  C C    . LYS A 1 100 ? 12.493  11.314  71.423  1.00 95.19  ? 100 LYS A C    1 
ATOM   1541  O O    . LYS A 1 100 ? 12.578  10.606  70.414  1.00 98.31  ? 100 LYS A O    1 
ATOM   1542  C CB   . LYS A 1 100 ? 13.276  10.272  73.552  1.00 100.11 ? 100 LYS A CB   1 
ATOM   1543  C CG   . LYS A 1 100 ? 13.220  10.455  75.085  1.00 108.04 ? 100 LYS A CG   1 
ATOM   1544  C CD   . LYS A 1 100 ? 12.475  11.710  75.567  1.00 107.83 ? 100 LYS A CD   1 
ATOM   1545  C CE   . LYS A 1 100 ? 12.992  12.994  74.923  1.00 108.95 ? 100 LYS A CE   1 
ATOM   1546  N NZ   . LYS A 1 100 ? 12.002  14.112  75.037  1.00 110.47 ? 100 LYS A NZ   1 
ATOM   1547  H H    . LYS A 1 100 ? 11.475  8.881   72.460  1.00 112.32 ? 100 LYS A H    1 
ATOM   1548  H HA   . LYS A 1 100 ? 11.614  11.444  73.275  1.00 116.92 ? 100 LYS A HA   1 
ATOM   1549  H HB2  . LYS A 1 100 ? 13.400  9.325   73.382  1.00 120.13 ? 100 LYS A HB2  1 
ATOM   1550  H HB3  . LYS A 1 100 ? 14.046  10.770  73.234  1.00 120.13 ? 100 LYS A HB3  1 
ATOM   1551  H HG2  . LYS A 1 100 ? 12.770  9.686   75.469  1.00 129.64 ? 100 LYS A HG2  1 
ATOM   1552  H HG3  . LYS A 1 100 ? 14.128  10.510  75.421  1.00 129.64 ? 100 LYS A HG3  1 
ATOM   1553  H HD2  . LYS A 1 100 ? 11.535  11.623  75.346  1.00 129.39 ? 100 LYS A HD2  1 
ATOM   1554  H HD3  . LYS A 1 100 ? 12.585  11.792  76.527  1.00 129.39 ? 100 LYS A HD3  1 
ATOM   1555  H HE2  . LYS A 1 100 ? 13.811  13.267  75.366  1.00 130.74 ? 100 LYS A HE2  1 
ATOM   1556  H HE3  . LYS A 1 100 ? 13.162  12.834  73.981  1.00 130.74 ? 100 LYS A HE3  1 
ATOM   1557  H HZ1  . LYS A 1 100 ? 11.235  13.880  74.651  1.00 132.57 ? 100 LYS A HZ1  1 
ATOM   1558  H HZ2  . LYS A 1 100 ? 12.318  14.841  74.637  1.00 132.57 ? 100 LYS A HZ2  1 
ATOM   1559  H HZ3  . LYS A 1 100 ? 11.849  14.297  75.895  1.00 132.57 ? 100 LYS A HZ3  1 
ATOM   1560  N N    . VAL A 1 101 ? 12.767  12.621  71.421  1.00 93.43  ? 101 VAL A N    1 
ATOM   1561  C CA   . VAL A 1 101 ? 13.370  13.251  70.258  1.00 88.57  ? 101 VAL A CA   1 
ATOM   1562  C C    . VAL A 1 101 ? 14.750  12.653  70.034  1.00 87.07  ? 101 VAL A C    1 
ATOM   1563  O O    . VAL A 1 101 ? 15.535  12.478  70.976  1.00 89.59  ? 101 VAL A O    1 
ATOM   1564  C CB   . VAL A 1 101 ? 13.442  14.776  70.462  1.00 88.08  ? 101 VAL A CB   1 
ATOM   1565  C CG1  . VAL A 1 101 ? 14.442  15.411  69.502  1.00 87.47  ? 101 VAL A CG1  1 
ATOM   1566  C CG2  . VAL A 1 101 ? 12.056  15.389  70.291  1.00 87.48  ? 101 VAL A CG2  1 
ATOM   1567  H H    . VAL A 1 101 ? 12.613  13.156  72.077  1.00 112.11 ? 101 VAL A H    1 
ATOM   1568  H HA   . VAL A 1 101 ? 12.828  13.080  69.472  1.00 106.28 ? 101 VAL A HA   1 
ATOM   1569  H HB   . VAL A 1 101 ? 13.751  14.959  71.363  1.00 105.70 ? 101 VAL A HB   1 
ATOM   1570  H HG11 . VAL A 1 101 ? 14.431  16.373  69.627  1.00 104.97 ? 101 VAL A HG11 1 
ATOM   1571  H HG12 . VAL A 1 101 ? 15.327  15.063  69.692  1.00 104.97 ? 101 VAL A HG12 1 
ATOM   1572  H HG13 . VAL A 1 101 ? 14.188  15.193  68.592  1.00 104.97 ? 101 VAL A HG13 1 
ATOM   1573  H HG21 . VAL A 1 101 ? 12.117  16.348  70.422  1.00 104.97 ? 101 VAL A HG21 1 
ATOM   1574  H HG22 . VAL A 1 101 ? 11.735  15.197  69.395  1.00 104.97 ? 101 VAL A HG22 1 
ATOM   1575  H HG23 . VAL A 1 101 ? 11.456  15.002  70.947  1.00 104.97 ? 101 VAL A HG23 1 
ATOM   1576  N N    . LEU A 1 102 ? 15.055  12.338  68.779  1.00 83.04  ? 102 LEU A N    1 
ATOM   1577  C CA   . LEU A 1 102 ? 16.310  11.689  68.423  1.00 84.19  ? 102 LEU A CA   1 
ATOM   1578  C C    . LEU A 1 102 ? 17.264  12.721  67.837  1.00 82.09  ? 102 LEU A C    1 
ATOM   1579  O O    . LEU A 1 102 ? 16.958  13.347  66.816  1.00 83.42  ? 102 LEU A O    1 
ATOM   1580  C CB   . LEU A 1 102 ? 16.079  10.551  67.431  1.00 83.58  ? 102 LEU A CB   1 
ATOM   1581  C CG   . LEU A 1 102 ? 15.314  9.352   67.995  1.00 84.83  ? 102 LEU A CG   1 
ATOM   1582  C CD1  . LEU A 1 102 ? 14.228  8.914   67.016  1.00 83.40  ? 102 LEU A CD1  1 
ATOM   1583  C CD2  . LEU A 1 102 ? 16.263  8.205   68.320  1.00 81.48  ? 102 LEU A CD2  1 
ATOM   1584  H H    . LEU A 1 102 ? 14.542  12.493  68.107  1.00 99.64  ? 102 LEU A H    1 
ATOM   1585  H HA   . LEU A 1 102 ? 16.713  11.320  69.225  1.00 101.03 ? 102 LEU A HA   1 
ATOM   1586  H HB2  . LEU A 1 102 ? 15.569  10.895  66.681  1.00 100.30 ? 102 LEU A HB2  1 
ATOM   1587  H HB3  . LEU A 1 102 ? 16.942  10.229  67.126  1.00 100.30 ? 102 LEU A HB3  1 
ATOM   1588  H HG   . LEU A 1 102 ? 14.883  9.608   68.826  1.00 101.79 ? 102 LEU A HG   1 
ATOM   1589  H HD11 . LEU A 1 102 ? 13.755  8.153   67.388  1.00 100.08 ? 102 LEU A HD11 1 
ATOM   1590  H HD12 . LEU A 1 102 ? 13.612  9.651   66.877  1.00 100.08 ? 102 LEU A HD12 1 
ATOM   1591  H HD13 . LEU A 1 102 ? 14.642  8.667   66.174  1.00 100.08 ? 102 LEU A HD13 1 
ATOM   1592  H HD21 . LEU A 1 102 ? 15.750  7.462   68.676  1.00 97.78  ? 102 LEU A HD21 1 
ATOM   1593  H HD22 . LEU A 1 102 ? 16.719  7.933   67.509  1.00 97.78  ? 102 LEU A HD22 1 
ATOM   1594  H HD23 . LEU A 1 102 ? 16.909  8.506   68.978  1.00 97.78  ? 102 LEU A HD23 1 
ATOM   1595  N N    . ASP A 1 103 ? 18.416  12.886  68.484  1.00 81.30  ? 103 ASP A N    1 
ATOM   1596  C CA   . ASP A 1 103 ? 19.453  13.807  68.027  1.00 83.54  ? 103 ASP A CA   1 
ATOM   1597  C C    . ASP A 1 103 ? 20.444  13.020  67.180  1.00 85.50  ? 103 ASP A C    1 
ATOM   1598  O O    . ASP A 1 103 ? 21.362  12.385  67.705  1.00 85.35  ? 103 ASP A O    1 
ATOM   1599  C CB   . ASP A 1 103 ? 20.131  14.471  69.219  1.00 86.13  ? 103 ASP A CB   1 
ATOM   1600  C CG   . ASP A 1 103 ? 21.261  15.391  68.809  1.00 92.22  ? 103 ASP A CG   1 
ATOM   1601  O OD1  . ASP A 1 103 ? 21.001  16.365  68.068  1.00 94.00  ? 103 ASP A OD1  1 
ATOM   1602  O OD2  . ASP A 1 103 ? 22.409  15.137  69.231  1.00 93.30  ? 103 ASP A OD2  1 
ATOM   1603  H H    . ASP A 1 103 ? 18.625  12.466  69.205  1.00 97.56  ? 103 ASP A H    1 
ATOM   1604  H HA   . ASP A 1 103 ? 19.060  14.499  67.472  1.00 100.24 ? 103 ASP A HA   1 
ATOM   1605  H HB2  . ASP A 1 103 ? 19.475  14.998  69.702  1.00 103.35 ? 103 ASP A HB2  1 
ATOM   1606  H HB3  . ASP A 1 103 ? 20.497  13.784  69.797  1.00 103.35 ? 103 ASP A HB3  1 
ATOM   1607  N N    . VAL A 1 104 ? 20.258  13.060  65.858  1.00 82.32  ? 104 VAL A N    1 
ATOM   1608  C CA   . VAL A 1 104 ? 21.067  12.285  64.923  1.00 80.44  ? 104 VAL A CA   1 
ATOM   1609  C C    . VAL A 1 104 ? 22.267  13.116  64.487  1.00 77.85  ? 104 VAL A C    1 
ATOM   1610  O O    . VAL A 1 104 ? 22.116  14.255  64.030  1.00 75.41  ? 104 VAL A O    1 
ATOM   1611  C CB   . VAL A 1 104 ? 20.235  11.852  63.702  1.00 81.05  ? 104 VAL A CB   1 
ATOM   1612  C CG1  . VAL A 1 104 ? 20.879  10.652  63.008  1.00 77.22  ? 104 VAL A CG1  1 
ATOM   1613  C CG2  . VAL A 1 104 ? 18.799  11.538  64.107  1.00 80.12  ? 104 VAL A CG2  1 
ATOM   1614  H H    . VAL A 1 104 ? 19.656  13.540  65.474  1.00 98.78  ? 104 VAL A H    1 
ATOM   1615  H HA   . VAL A 1 104 ? 21.393  11.492  65.377  1.00 96.53  ? 104 VAL A HA   1 
ATOM   1616  H HB   . VAL A 1 104 ? 20.210  12.586  63.069  1.00 97.26  ? 104 VAL A HB   1 
ATOM   1617  H HG11 . VAL A 1 104 ? 20.382  10.451  62.199  1.00 92.66  ? 104 VAL A HG11 1 
ATOM   1618  H HG12 . VAL A 1 104 ? 21.797  10.872  62.786  1.00 92.66  ? 104 VAL A HG12 1 
ATOM   1619  H HG13 . VAL A 1 104 ? 20.856  9.891   63.608  1.00 92.66  ? 104 VAL A HG13 1 
ATOM   1620  H HG21 . VAL A 1 104 ? 18.365  11.059  63.384  1.00 96.15  ? 104 VAL A HG21 1 
ATOM   1621  H HG22 . VAL A 1 104 ? 18.810  10.991  64.908  1.00 96.15  ? 104 VAL A HG22 1 
ATOM   1622  H HG23 . VAL A 1 104 ? 18.331  12.370  64.281  1.00 96.15  ? 104 VAL A HG23 1 
ATOM   1623  N N    . ASP A 1 105 ? 23.459  12.536  64.612  1.00 76.51  ? 105 ASP A N    1 
ATOM   1624  C CA   . ASP A 1 105 ? 24.701  13.179  64.195  1.00 76.19  ? 105 ASP A CA   1 
ATOM   1625  C C    . ASP A 1 105 ? 25.017  12.744  62.769  1.00 76.76  ? 105 ASP A C    1 
ATOM   1626  O O    . ASP A 1 105 ? 25.431  11.602  62.537  1.00 73.81  ? 105 ASP A O    1 
ATOM   1627  C CB   . ASP A 1 105 ? 25.833  12.811  65.150  1.00 75.94  ? 105 ASP A CB   1 
ATOM   1628  C CG   . ASP A 1 105 ? 27.174  13.383  64.722  1.00 78.76  ? 105 ASP A CG   1 
ATOM   1629  O OD1  . ASP A 1 105 ? 27.204  14.247  63.818  1.00 79.46  ? 105 ASP A OD1  1 
ATOM   1630  O OD2  . ASP A 1 105 ? 28.203  12.965  65.304  1.00 78.95  ? 105 ASP A OD2  1 
ATOM   1631  H H    . ASP A 1 105 ? 23.576  11.751  64.943  1.00 91.82  ? 105 ASP A H    1 
ATOM   1632  H HA   . ASP A 1 105 ? 24.592  14.143  64.205  1.00 91.42  ? 105 ASP A HA   1 
ATOM   1633  H HB2  . ASP A 1 105 ? 25.627  13.158  66.032  1.00 91.13  ? 105 ASP A HB2  1 
ATOM   1634  H HB3  . ASP A 1 105 ? 25.916  11.845  65.184  1.00 91.13  ? 105 ASP A HB3  1 
ATOM   1635  N N    . VAL A 1 106 ? 24.825  13.655  61.814  1.00 77.08  ? 106 VAL A N    1 
ATOM   1636  C CA   . VAL A 1 106 ? 25.024  13.376  60.395  1.00 75.32  ? 106 VAL A CA   1 
ATOM   1637  C C    . VAL A 1 106 ? 26.324  14.029  59.948  1.00 75.32  ? 106 VAL A C    1 
ATOM   1638  O O    . VAL A 1 106 ? 26.573  15.204  60.243  1.00 75.97  ? 106 VAL A O    1 
ATOM   1639  C CB   . VAL A 1 106 ? 23.837  13.882  59.557  1.00 75.24  ? 106 VAL A CB   1 
ATOM   1640  C CG1  . VAL A 1 106 ? 24.117  13.703  58.059  1.00 75.81  ? 106 VAL A CG1  1 
ATOM   1641  C CG2  . VAL A 1 106 ? 22.554  13.167  59.963  1.00 73.39  ? 106 VAL A CG2  1 
ATOM   1642  H H    . VAL A 1 106 ? 24.572  14.462  61.970  1.00 92.49  ? 106 VAL A H    1 
ATOM   1643  H HA   . VAL A 1 106 ? 25.104  12.418  60.267  1.00 90.39  ? 106 VAL A HA   1 
ATOM   1644  H HB   . VAL A 1 106 ? 23.715  14.830  59.723  1.00 90.28  ? 106 VAL A HB   1 
ATOM   1645  H HG11 . VAL A 1 106 ? 23.289  13.813  57.567  1.00 90.97  ? 106 VAL A HG11 1 
ATOM   1646  H HG12 . VAL A 1 106 ? 24.761  14.372  57.776  1.00 90.97  ? 106 VAL A HG12 1 
ATOM   1647  H HG13 . VAL A 1 106 ? 24.477  12.815  57.908  1.00 90.97  ? 106 VAL A HG13 1 
ATOM   1648  H HG21 . VAL A 1 106 ? 21.826  13.486  59.407  1.00 88.07  ? 106 VAL A HG21 1 
ATOM   1649  H HG22 . VAL A 1 106 ? 22.672  12.213  59.838  1.00 88.07  ? 106 VAL A HG22 1 
ATOM   1650  H HG23 . VAL A 1 106 ? 22.368  13.359  60.895  1.00 88.07  ? 106 VAL A HG23 1 
ATOM   1651  N N    . ARG A 1 107 ? 27.149  13.271  59.231  1.00 76.42  ? 107 ARG A N    1 
ATOM   1652  C CA   . ARG A 1 107 ? 28.404  13.768  58.685  1.00 80.09  ? 107 ARG A CA   1 
ATOM   1653  C C    . ARG A 1 107 ? 28.533  13.344  57.227  1.00 79.34  ? 107 ARG A C    1 
ATOM   1654  O O    . ARG A 1 107 ? 27.917  12.371  56.784  1.00 77.22  ? 107 ARG A O    1 
ATOM   1655  C CB   . ARG A 1 107 ? 29.603  13.252  59.498  1.00 78.25  ? 107 ARG A CB   1 
ATOM   1656  C CG   . ARG A 1 107 ? 29.610  13.697  60.954  1.00 77.50  ? 107 ARG A CG   1 
ATOM   1657  C CD   . ARG A 1 107 ? 29.876  12.522  61.902  1.00 72.40  ? 107 ARG A CD   1 
ATOM   1658  N NE   . ARG A 1 107 ? 28.751  11.602  62.025  1.00 72.75  ? 107 ARG A NE   1 
ATOM   1659  C CZ   . ARG A 1 107 ? 28.866  10.282  62.108  1.00 70.40  ? 107 ARG A CZ   1 
ATOM   1660  N NH1  . ARG A 1 107 ? 30.036  9.675   61.955  1.00 66.15  ? 107 ARG A NH1  1 
ATOM   1661  N NH2  . ARG A 1 107 ? 27.788  9.555   62.390  1.00 73.69  ? 107 ARG A NH2  1 
ATOM   1662  H H    . ARG A 1 107 ? 26.999  12.445  59.044  1.00 91.70  ? 107 ARG A H    1 
ATOM   1663  H HA   . ARG A 1 107 ? 28.411  14.738  58.712  1.00 96.11  ? 107 ARG A HA   1 
ATOM   1664  H HB2  . ARG A 1 107 ? 29.590  12.282  59.487  1.00 93.89  ? 107 ARG A HB2  1 
ATOM   1665  H HB3  . ARG A 1 107 ? 30.419  13.577  59.087  1.00 93.89  ? 107 ARG A HB3  1 
ATOM   1666  H HG2  . ARG A 1 107 ? 30.308  14.357  61.084  1.00 93.00  ? 107 ARG A HG2  1 
ATOM   1667  H HG3  . ARG A 1 107 ? 28.747  14.078  61.177  1.00 93.00  ? 107 ARG A HG3  1 
ATOM   1668  H HD2  . ARG A 1 107 ? 30.636  12.019  61.571  1.00 86.88  ? 107 ARG A HD2  1 
ATOM   1669  H HD3  . ARG A 1 107 ? 30.070  12.872  62.786  1.00 86.88  ? 107 ARG A HD3  1 
ATOM   1670  H HE   . ARG A 1 107 ? 27.959  11.937  62.044  1.00 87.30  ? 107 ARG A HE   1 
ATOM   1671  H HH11 . ARG A 1 107 ? 30.743  10.139  61.797  1.00 79.38  ? 107 ARG A HH11 1 
ATOM   1672  H HH12 . ARG A 1 107 ? 30.087  8.819   62.013  1.00 79.38  ? 107 ARG A HH12 1 
ATOM   1673  H HH21 . ARG A 1 107 ? 27.030  9.941   62.515  1.00 88.42  ? 107 ARG A HH21 1 
ATOM   1674  H HH22 . ARG A 1 107 ? 27.849  8.699   62.446  1.00 88.42  ? 107 ARG A HH22 1 
ATOM   1675  N N    . ASN A 1 108 ? 29.342  14.094  56.477  1.00 83.03  ? 108 ASN A N    1 
ATOM   1676  C CA   . ASN A 1 108 ? 29.571  13.787  55.072  1.00 82.74  ? 108 ASN A CA   1 
ATOM   1677  C C    . ASN A 1 108 ? 30.490  12.580  54.949  1.00 84.95  ? 108 ASN A C    1 
ATOM   1678  O O    . ASN A 1 108 ? 31.443  12.426  55.717  1.00 87.81  ? 108 ASN A O    1 
ATOM   1679  C CB   . ASN A 1 108 ? 30.187  14.982  54.349  1.00 85.19  ? 108 ASN A CB   1 
ATOM   1680  C CG   . ASN A 1 108 ? 31.005  14.573  53.130  1.00 89.75  ? 108 ASN A CG   1 
ATOM   1681  O OD1  . ASN A 1 108 ? 32.224  14.430  53.206  1.00 92.77  ? 108 ASN A OD1  1 
ATOM   1682  N ND2  . ASN A 1 108 ? 30.330  14.387  51.996  1.00 86.08  ? 108 ASN A ND2  1 
ATOM   1683  H H    . ASN A 1 108 ? 29.768  14.785  56.761  1.00 99.63  ? 108 ASN A H    1 
ATOM   1684  H HA   . ASN A 1 108 ? 28.725  13.583  54.643  1.00 99.29  ? 108 ASN A HA   1 
ATOM   1685  H HB2  . ASN A 1 108 ? 29.477  15.572  54.051  1.00 102.23 ? 108 ASN A HB2  1 
ATOM   1686  H HB3  . ASN A 1 108 ? 30.774  15.453  54.961  1.00 102.23 ? 108 ASN A HB3  1 
ATOM   1687  H HD21 . ASN A 1 108 ? 29.477  14.499  51.979  1.00 103.29 ? 108 ASN A HD21 1 
ATOM   1688  H HD22 . ASN A 1 108 ? 30.747  14.155  51.280  1.00 103.29 ? 108 ASN A HD22 1 
ATOM   1689  N N    . ASP A 1 109 ? 30.205  11.718  53.976  1.00 84.45  ? 109 ASP A N    1 
ATOM   1690  C CA   . ASP A 1 109 ? 30.969  10.492  53.757  1.00 84.53  ? 109 ASP A CA   1 
ATOM   1691  C C    . ASP A 1 109 ? 31.449  10.443  52.300  1.00 86.57  ? 109 ASP A C    1 
ATOM   1692  O O    . ASP A 1 109 ? 31.201  9.493   51.569  1.00 85.87  ? 109 ASP A O    1 
ATOM   1693  C CB   . ASP A 1 109 ? 30.151  9.250   54.094  1.00 83.91  ? 109 ASP A CB   1 
ATOM   1694  C CG   . ASP A 1 109 ? 31.018  8.016   54.299  1.00 85.54  ? 109 ASP A CG   1 
ATOM   1695  O OD1  . ASP A 1 109 ? 32.185  8.164   54.704  1.00 87.54  ? 109 ASP A OD1  1 
ATOM   1696  O OD2  . ASP A 1 109 ? 30.517  6.887   54.059  1.00 86.83  ? 109 ASP A OD2  1 
ATOM   1697  H H    . ASP A 1 109 ? 29.559  11.824  53.418  1.00 101.34 ? 109 ASP A H    1 
ATOM   1698  H HA   . ASP A 1 109 ? 31.746  10.513  54.337  1.00 101.43 ? 109 ASP A HA   1 
ATOM   1699  H HB2  . ASP A 1 109 ? 29.656  9.409   54.913  1.00 100.69 ? 109 ASP A HB2  1 
ATOM   1700  H HB3  . ASP A 1 109 ? 29.536  9.068   53.366  1.00 100.69 ? 109 ASP A HB3  1 
ATOM   1701  N N    . GLY A 1 110 ? 32.156  11.492  51.884  1.00 90.01  ? 110 GLY A N    1 
ATOM   1702  C CA   . GLY A 1 110 ? 32.668  11.577  50.529  1.00 89.62  ? 110 GLY A CA   1 
ATOM   1703  C C    . GLY A 1 110 ? 31.825  12.447  49.620  1.00 92.73  ? 110 GLY A C    1 
ATOM   1704  O O    . GLY A 1 110 ? 31.931  13.676  49.650  1.00 100.64 ? 110 GLY A O    1 
ATOM   1705  H H    . GLY A 1 110 ? 32.352  12.171  52.375  1.00 108.02 ? 110 GLY A H    1 
ATOM   1706  H HA2  . GLY A 1 110 ? 33.565  11.945  50.551  1.00 107.54 ? 110 GLY A HA2  1 
ATOM   1707  H HA3  . GLY A 1 110 ? 32.702  10.686  50.147  1.00 107.54 ? 110 GLY A HA3  1 
ATOM   1708  N N    . ALA A 1 111 ? 30.982  11.815  48.809  1.00 91.40  ? 111 ALA A N    1 
ATOM   1709  C CA   . ALA A 1 111 ? 30.130  12.538  47.878  1.00 89.30  ? 111 ALA A CA   1 
ATOM   1710  C C    . ALA A 1 111 ? 29.016  13.282  48.612  1.00 84.17  ? 111 ALA A C    1 
ATOM   1711  O O    . ALA A 1 111 ? 28.697  12.999  49.771  1.00 81.99  ? 111 ALA A O    1 
ATOM   1712  C CB   . ALA A 1 111 ? 29.522  11.573  46.858  1.00 87.78  ? 111 ALA A CB   1 
ATOM   1713  H H    . ALA A 1 111 ? 30.885  10.961  48.779  1.00 109.67 ? 111 ALA A H    1 
ATOM   1714  H HA   . ALA A 1 111 ? 30.665  13.194  47.405  1.00 107.16 ? 111 ALA A HA   1 
ATOM   1715  H HB1  . ALA A 1 111 ? 28.950  10.942  47.322  1.00 105.33 ? 111 ALA A HB1  1 
ATOM   1716  H HB2  . ALA A 1 111 ? 29.002  12.080  46.214  1.00 105.33 ? 111 ALA A HB2  1 
ATOM   1717  H HB3  . ALA A 1 111 ? 30.238  11.100  46.405  1.00 105.33 ? 111 ALA A HB3  1 
ATOM   1718  N N    . LYS A 1 112 ? 28.411  14.245  47.902  1.00 81.12  ? 112 LYS A N    1 
ATOM   1719  C CA   . LYS A 1 112 ? 27.351  15.055  48.491  1.00 75.72  ? 112 LYS A CA   1 
ATOM   1720  C C    . LYS A 1 112 ? 26.099  14.241  48.793  1.00 73.87  ? 112 LYS A C    1 
ATOM   1721  O O    . LYS A 1 112 ? 25.293  14.645  49.639  1.00 76.00  ? 112 LYS A O    1 
ATOM   1722  C CB   . LYS A 1 112 ? 26.966  16.210  47.564  1.00 78.71  ? 112 LYS A CB   1 
ATOM   1723  C CG   . LYS A 1 112 ? 28.115  17.022  47.022  1.00 82.94  ? 112 LYS A CG   1 
ATOM   1724  C CD   . LYS A 1 112 ? 27.927  18.492  47.355  1.00 87.52  ? 112 LYS A CD   1 
ATOM   1725  C CE   . LYS A 1 112 ? 29.256  19.231  47.342  1.00 91.94  ? 112 LYS A CE   1 
ATOM   1726  N NZ   . LYS A 1 112 ? 29.141  20.579  47.971  1.00 94.12  ? 112 LYS A NZ   1 
ATOM   1727  H H    . LYS A 1 112 ? 28.597  14.443  47.086  1.00 97.35  ? 112 LYS A H    1 
ATOM   1728  H HA   . LYS A 1 112 ? 27.700  15.419  49.320  1.00 90.86  ? 112 LYS A HA   1 
ATOM   1729  H HB2  . LYS A 1 112 ? 26.488  15.844  46.804  1.00 94.45  ? 112 LYS A HB2  1 
ATOM   1730  H HB3  . LYS A 1 112 ? 26.391  16.817  48.056  1.00 94.45  ? 112 LYS A HB3  1 
ATOM   1731  H HG2  . LYS A 1 112 ? 28.945  16.718  47.422  1.00 99.53  ? 112 LYS A HG2  1 
ATOM   1732  H HG3  . LYS A 1 112 ? 28.156  16.925  46.058  1.00 99.53  ? 112 LYS A HG3  1 
ATOM   1733  H HD2  . LYS A 1 112 ? 27.343  18.900  46.696  1.00 105.03 ? 112 LYS A HD2  1 
ATOM   1734  H HD3  . LYS A 1 112 ? 27.538  18.576  48.239  1.00 105.03 ? 112 LYS A HD3  1 
ATOM   1735  H HE2  . LYS A 1 112 ? 29.912  18.718  47.839  1.00 110.32 ? 112 LYS A HE2  1 
ATOM   1736  H HE3  . LYS A 1 112 ? 29.550  19.346  46.425  1.00 110.32 ? 112 LYS A HE3  1 
ATOM   1737  H HZ1  . LYS A 1 112 ? 29.931  20.988  47.960  1.00 112.95 ? 112 LYS A HZ1  1 
ATOM   1738  H HZ2  . LYS A 1 112 ? 28.553  21.075  47.523  1.00 112.95 ? 112 LYS A HZ2  1 
ATOM   1739  H HZ3  . LYS A 1 112 ? 28.869  20.500  48.814  1.00 112.95 ? 112 LYS A HZ3  1 
ATOM   1740  N N    . ASN A 1 113 ? 25.889  13.139  48.078  1.00 74.71  ? 113 ASN A N    1 
ATOM   1741  C CA   . ASN A 1 113 ? 24.766  12.256  48.354  1.00 73.23  ? 113 ASN A CA   1 
ATOM   1742  C C    . ASN A 1 113 ? 25.093  11.201  49.405  1.00 75.34  ? 113 ASN A C    1 
ATOM   1743  O O    . ASN A 1 113 ? 24.178  10.529  49.896  1.00 74.67  ? 113 ASN A O    1 
ATOM   1744  C CB   . ASN A 1 113 ? 24.297  11.574  47.061  1.00 74.57  ? 113 ASN A CB   1 
ATOM   1745  C CG   . ASN A 1 113 ? 25.280  10.544  46.559  1.00 73.47  ? 113 ASN A CG   1 
ATOM   1746  O OD1  . ASN A 1 113 ? 26.478  10.810  46.473  1.00 73.85  ? 113 ASN A OD1  1 
ATOM   1747  N ND2  . ASN A 1 113 ? 24.781  9.360   46.228  1.00 75.70  ? 113 ASN A ND2  1 
ATOM   1748  H H    . ASN A 1 113 ? 26.386  12.882  47.426  1.00 89.65  ? 113 ASN A H    1 
ATOM   1749  H HA   . ASN A 1 113 ? 24.024  12.785  48.687  1.00 87.88  ? 113 ASN A HA   1 
ATOM   1750  H HB2  . ASN A 1 113 ? 23.453  11.127  47.228  1.00 89.49  ? 113 ASN A HB2  1 
ATOM   1751  H HB3  . ASN A 1 113 ? 24.186  12.246  46.371  1.00 89.49  ? 113 ASN A HB3  1 
ATOM   1752  H HD21 . ASN A 1 113 ? 25.301  8.740   45.936  1.00 90.84  ? 113 ASN A HD21 1 
ATOM   1753  H HD22 . ASN A 1 113 ? 23.937  9.212   46.305  1.00 90.84  ? 113 ASN A HD22 1 
ATOM   1754  N N    . LYS A 1 114 ? 26.364  11.062  49.780  1.00 76.08  ? 114 LYS A N    1 
ATOM   1755  C CA   . LYS A 1 114 ? 26.803  10.080  50.762  1.00 75.96  ? 114 LYS A CA   1 
ATOM   1756  C C    . LYS A 1 114 ? 27.007  10.744  52.116  1.00 76.65  ? 114 LYS A C    1 
ATOM   1757  O O    . LYS A 1 114 ? 27.490  11.876  52.206  1.00 80.58  ? 114 LYS A O    1 
ATOM   1758  C CB   . LYS A 1 114 ? 28.093  9.404   50.297  1.00 79.89  ? 114 LYS A CB   1 
ATOM   1759  C CG   . LYS A 1 114 ? 27.845  8.124   49.501  1.00 80.19  ? 114 LYS A CG   1 
ATOM   1760  C CD   . LYS A 1 114 ? 28.999  7.779   48.572  1.00 84.76  ? 114 LYS A CD   1 
ATOM   1761  C CE   . LYS A 1 114 ? 30.006  6.857   49.249  1.00 91.21  ? 114 LYS A CE   1 
ATOM   1762  N NZ   . LYS A 1 114 ? 31.408  7.245   48.911  1.00 96.77  ? 114 LYS A NZ   1 
ATOM   1763  H H    . LYS A 1 114 ? 27.007  11.540  49.469  1.00 91.30  ? 114 LYS A H    1 
ATOM   1764  H HA   . LYS A 1 114 ? 26.123  9.397   50.870  1.00 91.15  ? 114 LYS A HA   1 
ATOM   1765  H HB2  . LYS A 1 114 ? 28.583  10.019  49.729  1.00 95.87  ? 114 LYS A HB2  1 
ATOM   1766  H HB3  . LYS A 1 114 ? 28.625  9.174   51.074  1.00 95.87  ? 114 LYS A HB3  1 
ATOM   1767  H HG2  . LYS A 1 114 ? 27.726  7.385   50.118  1.00 96.22  ? 114 LYS A HG2  1 
ATOM   1768  H HG3  . LYS A 1 114 ? 27.048  8.237   48.960  1.00 96.22  ? 114 LYS A HG3  1 
ATOM   1769  H HD2  . LYS A 1 114 ? 28.654  7.328   47.785  1.00 101.71 ? 114 LYS A HD2  1 
ATOM   1770  H HD3  . LYS A 1 114 ? 29.458  8.594   48.313  1.00 101.71 ? 114 LYS A HD3  1 
ATOM   1771  H HE2  . LYS A 1 114 ? 29.897  6.912   50.211  1.00 109.45 ? 114 LYS A HE2  1 
ATOM   1772  H HE3  . LYS A 1 114 ? 29.860  5.946   48.950  1.00 109.45 ? 114 LYS A HE3  1 
ATOM   1773  H HZ1  . LYS A 1 114 ? 31.982  6.704   49.324  1.00 116.12 ? 114 LYS A HZ1  1 
ATOM   1774  H HZ2  . LYS A 1 114 ? 31.537  7.185   48.032  1.00 116.12 ? 114 LYS A HZ2  1 
ATOM   1775  H HZ3  . LYS A 1 114 ? 31.563  8.082   49.169  1.00 116.12 ? 114 LYS A HZ3  1 
ATOM   1776  N N    . PHE A 1 115 ? 26.623  10.033  53.173  1.00 77.96  ? 115 PHE A N    1 
ATOM   1777  C CA   . PHE A 1 115 ? 26.635  10.564  54.529  1.00 76.97  ? 115 PHE A CA   1 
ATOM   1778  C C    . PHE A 1 115 ? 27.030  9.458   55.508  1.00 75.98  ? 115 PHE A C    1 
ATOM   1779  O O    . PHE A 1 115 ? 27.180  8.291   55.140  1.00 73.59  ? 115 PHE A O    1 
ATOM   1780  C CB   . PHE A 1 115 ? 25.262  11.126  54.937  1.00 74.37  ? 115 PHE A CB   1 
ATOM   1781  C CG   . PHE A 1 115 ? 24.784  12.275  54.092  1.00 74.77  ? 115 PHE A CG   1 
ATOM   1782  C CD1  . PHE A 1 115 ? 24.063  12.052  52.926  1.00 76.98  ? 115 PHE A CD1  1 
ATOM   1783  C CD2  . PHE A 1 115 ? 25.024  13.580  54.482  1.00 75.12  ? 115 PHE A CD2  1 
ATOM   1784  C CE1  . PHE A 1 115 ? 23.611  13.112  52.160  1.00 73.92  ? 115 PHE A CE1  1 
ATOM   1785  C CE2  . PHE A 1 115 ? 24.574  14.643  53.721  1.00 73.05  ? 115 PHE A CE2  1 
ATOM   1786  C CZ   . PHE A 1 115 ? 23.865  14.407  52.558  1.00 74.08  ? 115 PHE A CZ   1 
ATOM   1787  H H    . PHE A 1 115 ? 26.345  9.220   53.126  1.00 93.56  ? 115 PHE A H    1 
ATOM   1788  H HA   . PHE A 1 115 ? 27.298  11.272  54.553  1.00 92.37  ? 115 PHE A HA   1 
ATOM   1789  H HB2  . PHE A 1 115 ? 24.604  10.417  54.867  1.00 89.24  ? 115 PHE A HB2  1 
ATOM   1790  H HB3  . PHE A 1 115 ? 25.315  11.439  55.854  1.00 89.24  ? 115 PHE A HB3  1 
ATOM   1791  H HD1  . PHE A 1 115 ? 23.883  11.180  52.657  1.00 92.37  ? 115 PHE A HD1  1 
ATOM   1792  H HD2  . PHE A 1 115 ? 25.494  13.744  55.267  1.00 90.15  ? 115 PHE A HD2  1 
ATOM   1793  H HE1  . PHE A 1 115 ? 23.135  12.950  51.377  1.00 88.70  ? 115 PHE A HE1  1 
ATOM   1794  H HE2  . PHE A 1 115 ? 24.749  15.515  53.991  1.00 87.66  ? 115 PHE A HE2  1 
ATOM   1795  H HZ   . PHE A 1 115 ? 23.559  15.120  52.046  1.00 88.89  ? 115 PHE A HZ   1 
ATOM   1796  N N    . LEU A 1 116 ? 27.192  9.830   56.776  1.00 80.01  ? 116 LEU A N    1 
ATOM   1797  C CA   . LEU A 1 116 ? 27.347  8.880   57.877  1.00 76.38  ? 116 LEU A CA   1 
ATOM   1798  C C    . LEU A 1 116 ? 26.457  9.377   59.003  1.00 73.42  ? 116 LEU A C    1 
ATOM   1799  O O    . LEU A 1 116 ? 26.613  10.517  59.447  1.00 75.37  ? 116 LEU A O    1 
ATOM   1800  C CB   . LEU A 1 116 ? 28.803  8.765   58.334  1.00 74.23  ? 116 LEU A CB   1 
ATOM   1801  C CG   . LEU A 1 116 ? 29.662  7.748   57.580  1.00 80.41  ? 116 LEU A CG   1 
ATOM   1802  C CD1  . LEU A 1 116 ? 31.134  8.138   57.661  1.00 84.43  ? 116 LEU A CD1  1 
ATOM   1803  C CD2  . LEU A 1 116 ? 29.466  6.342   58.112  1.00 79.38  ? 116 LEU A CD2  1 
ATOM   1804  H H    . LEU A 1 116 ? 27.215  10.651  57.032  1.00 96.01  ? 116 LEU A H    1 
ATOM   1805  H HA   . LEU A 1 116 ? 27.069  7.992   57.603  1.00 91.65  ? 116 LEU A HA   1 
ATOM   1806  H HB2  . LEU A 1 116 ? 29.223  9.633   58.227  1.00 89.07  ? 116 LEU A HB2  1 
ATOM   1807  H HB3  . LEU A 1 116 ? 28.807  8.508   59.269  1.00 89.07  ? 116 LEU A HB3  1 
ATOM   1808  H HG   . LEU A 1 116 ? 29.384  7.749   56.651  1.00 96.50  ? 116 LEU A HG   1 
ATOM   1809  H HD11 . LEU A 1 116 ? 31.666  7.453   57.226  1.00 101.32 ? 116 LEU A HD11 1 
ATOM   1810  H HD12 . LEU A 1 116 ? 31.261  8.989   57.213  1.00 101.32 ? 116 LEU A HD12 1 
ATOM   1811  H HD13 . LEU A 1 116 ? 31.390  8.213   58.594  1.00 101.32 ? 116 LEU A HD13 1 
ATOM   1812  H HD21 . LEU A 1 116 ? 30.150  6.157   58.774  1.00 95.26  ? 116 LEU A HD21 1 
ATOM   1813  H HD22 . LEU A 1 116 ? 28.587  6.278   58.517  1.00 95.26  ? 116 LEU A HD22 1 
ATOM   1814  H HD23 . LEU A 1 116 ? 29.538  5.714   57.376  1.00 95.26  ? 116 LEU A HD23 1 
ATOM   1815  N N    . ALA A 1 117 ? 25.516  8.545   59.446  1.00 74.04  ? 117 ALA A N    1 
ATOM   1816  C CA   . ALA A 1 117 ? 24.513  8.948   60.422  1.00 73.06  ? 117 ALA A CA   1 
ATOM   1817  C C    . ALA A 1 117 ? 24.606  8.070   61.660  1.00 77.52  ? 117 ALA A C    1 
ATOM   1818  O O    . ALA A 1 117 ? 24.604  6.839   61.551  1.00 78.76  ? 117 ALA A O    1 
ATOM   1819  C CB   . ALA A 1 117 ? 23.098  8.864   59.835  1.00 72.41  ? 117 ALA A CB   1 
ATOM   1820  H H    . ALA A 1 117 ? 25.439  7.728   59.189  1.00 88.85  ? 117 ALA A H    1 
ATOM   1821  H HA   . ALA A 1 117 ? 24.689  9.864   60.686  1.00 87.67  ? 117 ALA A HA   1 
ATOM   1822  H HB1  . ALA A 1 117 ? 22.453  9.031   60.540  1.00 86.89  ? 117 ALA A HB1  1 
ATOM   1823  H HB2  . ALA A 1 117 ? 23.006  9.531   59.137  1.00 86.89  ? 117 ALA A HB2  1 
ATOM   1824  H HB3  . ALA A 1 117 ? 22.962  7.977   59.466  1.00 86.89  ? 117 ALA A HB3  1 
ATOM   1825  N N    . LYS A 1 118 ? 24.682  8.707   62.832  1.00 75.19  ? 118 LYS A N    1 
ATOM   1826  C CA   . LYS A 1 118 ? 24.687  8.039   64.127  1.00 76.74  ? 118 LYS A CA   1 
ATOM   1827  C C    . LYS A 1 118 ? 23.410  8.408   64.875  1.00 77.49  ? 118 LYS A C    1 
ATOM   1828  O O    . LYS A 1 118 ? 22.958  9.556   64.818  1.00 79.09  ? 118 LYS A O    1 
ATOM   1829  C CB   . LYS A 1 118 ? 25.925  8.440   64.943  1.00 77.79  ? 118 LYS A CB   1 
ATOM   1830  C CG   . LYS A 1 118 ? 25.855  8.123   66.439  1.00 78.25  ? 118 LYS A CG   1 
ATOM   1831  C CD   . LYS A 1 118 ? 27.132  7.430   66.943  1.00 80.40  ? 118 LYS A CD   1 
ATOM   1832  C CE   . LYS A 1 118 ? 28.362  8.326   66.825  1.00 80.93  ? 118 LYS A CE   1 
ATOM   1833  N NZ   . LYS A 1 118 ? 28.304  9.500   67.738  1.00 82.21  ? 118 LYS A NZ   1 
ATOM   1834  H H    . LYS A 1 118 ? 24.732  9.563   62.900  1.00 90.23  ? 118 LYS A H    1 
ATOM   1835  H HA   . LYS A 1 118 ? 24.711  7.076   64.014  1.00 92.09  ? 118 LYS A HA   1 
ATOM   1836  H HB2  . LYS A 1 118 ? 26.693  7.969   64.583  1.00 93.35  ? 118 LYS A HB2  1 
ATOM   1837  H HB3  . LYS A 1 118 ? 26.051  9.397   64.856  1.00 93.35  ? 118 LYS A HB3  1 
ATOM   1838  H HG2  . LYS A 1 118 ? 25.743  8.949   66.935  1.00 93.90  ? 118 LYS A HG2  1 
ATOM   1839  H HG3  . LYS A 1 118 ? 25.105  7.531   66.605  1.00 93.90  ? 118 LYS A HG3  1 
ATOM   1840  H HD2  . LYS A 1 118 ? 27.019  7.195   67.877  1.00 96.48  ? 118 LYS A HD2  1 
ATOM   1841  H HD3  . LYS A 1 118 ? 27.290  6.631   66.416  1.00 96.48  ? 118 LYS A HD3  1 
ATOM   1842  H HE2  . LYS A 1 118 ? 29.153  7.811   67.049  1.00 97.12  ? 118 LYS A HE2  1 
ATOM   1843  H HE3  . LYS A 1 118 ? 28.428  8.656   65.915  1.00 97.12  ? 118 LYS A HE3  1 
ATOM   1844  H HZ1  . LYS A 1 118 ? 28.248  9.226   68.583  1.00 98.65  ? 118 LYS A HZ1  1 
ATOM   1845  H HZ2  . LYS A 1 118 ? 29.037  9.996   67.643  1.00 98.65  ? 118 LYS A HZ2  1 
ATOM   1846  H HZ3  . LYS A 1 118 ? 27.591  9.998   67.548  1.00 98.65  ? 118 LYS A HZ3  1 
ATOM   1847  N N    . ILE A 1 119 ? 22.835  7.435   65.582  1.00 77.15  ? 119 ILE A N    1 
ATOM   1848  C CA   . ILE A 1 119 ? 21.535  7.603   66.228  1.00 78.24  ? 119 ILE A CA   1 
ATOM   1849  C C    . ILE A 1 119 ? 21.521  6.809   67.530  1.00 77.03  ? 119 ILE A C    1 
ATOM   1850  O O    . ILE A 1 119 ? 22.087  5.715   67.612  1.00 77.85  ? 119 ILE A O    1 
ATOM   1851  C CB   . ILE A 1 119 ? 20.397  7.162   65.278  1.00 76.15  ? 119 ILE A CB   1 
ATOM   1852  C CG1  . ILE A 1 119 ? 19.027  7.483   65.872  1.00 76.78  ? 119 ILE A CG1  1 
ATOM   1853  C CG2  . ILE A 1 119 ? 20.517  5.669   64.966  1.00 75.37  ? 119 ILE A CG2  1 
ATOM   1854  C CD1  . ILE A 1 119 ? 17.862  6.876   65.100  1.00 74.24  ? 119 ILE A CD1  1 
ATOM   1855  H H    . ILE A 1 119 ? 23.184  6.658   65.704  1.00 92.58  ? 119 ILE A H    1 
ATOM   1856  H HA   . ILE A 1 119 ? 21.407  8.537   66.459  1.00 93.89  ? 119 ILE A HA   1 
ATOM   1857  H HB   . ILE A 1 119 ? 20.486  7.661   64.451  1.00 91.38  ? 119 ILE A HB   1 
ATOM   1858  H HG12 . ILE A 1 119 ? 18.993  7.139   66.778  1.00 92.13  ? 119 ILE A HG12 1 
ATOM   1859  H HG13 . ILE A 1 119 ? 18.908  8.445   65.877  1.00 92.13  ? 119 ILE A HG13 1 
ATOM   1860  H HG21 . ILE A 1 119 ? 19.941  5.456   64.216  1.00 90.45  ? 119 ILE A HG21 1 
ATOM   1861  H HG22 . ILE A 1 119 ? 21.439  5.466   64.744  1.00 90.45  ? 119 ILE A HG22 1 
ATOM   1862  H HG23 . ILE A 1 119 ? 20.245  5.161   65.747  1.00 90.45  ? 119 ILE A HG23 1 
ATOM   1863  H HD11 . ILE A 1 119 ? 17.035  7.278   65.409  1.00 89.09  ? 119 ILE A HD11 1 
ATOM   1864  H HD12 . ILE A 1 119 ? 17.982  7.054   64.154  1.00 89.09  ? 119 ILE A HD12 1 
ATOM   1865  H HD13 . ILE A 1 119 ? 17.843  5.919   65.256  1.00 89.09  ? 119 ILE A HD13 1 
ATOM   1866  N N    . LYS A 1 120 ? 20.863  7.366   68.550  1.00 79.57  ? 120 LYS A N    1 
ATOM   1867  C CA   . LYS A 1 120 ? 20.710  6.674   69.824  1.00 76.60  ? 120 LYS A CA   1 
ATOM   1868  C C    . LYS A 1 120 ? 19.672  5.567   69.699  1.00 78.56  ? 120 LYS A C    1 
ATOM   1869  O O    . LYS A 1 120 ? 18.552  5.808   69.236  1.00 80.17  ? 120 LYS A O    1 
ATOM   1870  C CB   . LYS A 1 120 ? 20.277  7.647   70.920  1.00 80.77  ? 120 LYS A CB   1 
ATOM   1871  C CG   . LYS A 1 120 ? 19.728  6.968   72.193  1.00 86.70  ? 120 LYS A CG   1 
ATOM   1872  C CD   . LYS A 1 120 ? 18.203  6.779   72.149  1.00 86.97  ? 120 LYS A CD   1 
ATOM   1873  C CE   . LYS A 1 120 ? 17.627  6.457   73.534  1.00 92.79  ? 120 LYS A CE   1 
ATOM   1874  N NZ   . LYS A 1 120 ? 16.264  5.840   73.461  1.00 89.93  ? 120 LYS A NZ   1 
ATOM   1875  H H    . LYS A 1 120 ? 20.497  8.144   68.526  1.00 95.49  ? 120 LYS A H    1 
ATOM   1876  H HA   . LYS A 1 120 ? 21.564  6.286   70.073  1.00 91.92  ? 120 LYS A HA   1 
ATOM   1877  H HB2  . LYS A 1 120 ? 21.045  8.180   71.180  1.00 96.92  ? 120 LYS A HB2  1 
ATOM   1878  H HB3  . LYS A 1 120 ? 19.579  8.219   70.568  1.00 96.92  ? 120 LYS A HB3  1 
ATOM   1879  H HG2  . LYS A 1 120 ? 20.136  6.093   72.288  1.00 104.05 ? 120 LYS A HG2  1 
ATOM   1880  H HG3  . LYS A 1 120 ? 19.940  7.519   72.963  1.00 104.05 ? 120 LYS A HG3  1 
ATOM   1881  H HD2  . LYS A 1 120 ? 17.788  7.596   71.830  1.00 104.36 ? 120 LYS A HD2  1 
ATOM   1882  H HD3  . LYS A 1 120 ? 17.989  6.045   71.553  1.00 104.36 ? 120 LYS A HD3  1 
ATOM   1883  H HE2  . LYS A 1 120 ? 18.216  5.832   73.985  1.00 111.35 ? 120 LYS A HE2  1 
ATOM   1884  H HE3  . LYS A 1 120 ? 17.558  7.277   74.047  1.00 111.35 ? 120 LYS A HE3  1 
ATOM   1885  H HZ1  . LYS A 1 120 ? 15.962  5.670   74.281  1.00 107.92 ? 120 LYS A HZ1  1 
ATOM   1886  H HZ2  . LYS A 1 120 ? 16.299  5.078   73.002  1.00 107.92 ? 120 LYS A HZ2  1 
ATOM   1887  H HZ3  . LYS A 1 120 ? 15.700  6.395   73.055  1.00 107.92 ? 120 LYS A HZ3  1 
ATOM   1888  N N    . MET A 1 121 ? 20.024  4.358   70.160  1.00 78.97  ? 121 MET A N    1 
ATOM   1889  C CA   . MET A 1 121 ? 19.114  3.228   70.011  1.00 80.02  ? 121 MET A CA   1 
ATOM   1890  C C    . MET A 1 121 ? 18.458  2.875   71.339  1.00 80.89  ? 121 MET A C    1 
ATOM   1891  O O    . MET A 1 121 ? 19.091  2.994   72.393  1.00 81.66  ? 121 MET A O    1 
ATOM   1892  C CB   . MET A 1 121 ? 19.853  1.999   69.466  1.00 79.84  ? 121 MET A CB   1 
ATOM   1893  C CG   . MET A 1 121 ? 20.428  2.187   68.063  1.00 77.23  ? 121 MET A CG   1 
ATOM   1894  S SD   . MET A 1 121 ? 19.182  2.517   66.794  1.00 78.73  ? 121 MET A SD   1 
ATOM   1895  C CE   . MET A 1 121 ? 18.145  1.058   66.901  1.00 76.41  ? 121 MET A CE   1 
ATOM   1896  H H    . MET A 1 121 ? 20.768  4.178   70.551  1.00 94.77  ? 121 MET A H    1 
ATOM   1897  H HA   . MET A 1 121 ? 18.421  3.466   69.376  1.00 96.02  ? 121 MET A HA   1 
ATOM   1898  H HB2  . MET A 1 121 ? 20.590  1.791   70.061  1.00 95.81  ? 121 MET A HB2  1 
ATOM   1899  H HB3  . MET A 1 121 ? 19.233  1.254   69.432  1.00 95.81  ? 121 MET A HB3  1 
ATOM   1900  H HG2  . MET A 1 121 ? 21.042  2.938   68.076  1.00 92.68  ? 121 MET A HG2  1 
ATOM   1901  H HG3  . MET A 1 121 ? 20.900  1.378   67.809  1.00 92.68  ? 121 MET A HG3  1 
ATOM   1902  H HE1  . MET A 1 121 ? 17.458  1.107   66.218  1.00 91.70  ? 121 MET A HE1  1 
ATOM   1903  H HE2  . MET A 1 121 ? 18.693  0.270   66.763  1.00 91.70  ? 121 MET A HE2  1 
ATOM   1904  H HE3  . MET A 1 121 ? 17.735  1.026   67.780  1.00 91.70  ? 121 MET A HE3  1 
ATOM   1905  N N    . PRO A 1 122 ? 17.182  2.458   71.322  1.00 81.69  ? 122 PRO A N    1 
ATOM   1906  C CA   . PRO A 1 122 ? 16.517  2.076   72.577  1.00 79.99  ? 122 PRO A CA   1 
ATOM   1907  C C    . PRO A 1 122 ? 17.339  1.124   73.433  1.00 81.19  ? 122 PRO A C    1 
ATOM   1908  O O    . PRO A 1 122 ? 18.208  0.411   72.923  1.00 77.42  ? 122 PRO A O    1 
ATOM   1909  C CB   . PRO A 1 122 ? 15.216  1.403   72.109  1.00 77.43  ? 122 PRO A CB   1 
ATOM   1910  C CG   . PRO A 1 122 ? 15.099  1.664   70.627  1.00 81.32  ? 122 PRO A CG   1 
ATOM   1911  C CD   . PRO A 1 122 ? 16.241  2.528   70.187  1.00 81.20  ? 122 PRO A CD   1 
ATOM   1912  H HA   . PRO A 1 122 ? 16.313  2.876   73.087  1.00 95.98  ? 122 PRO A HA   1 
ATOM   1913  H HB2  . PRO A 1 122 ? 15.264  0.450   72.284  1.00 92.92  ? 122 PRO A HB2  1 
ATOM   1914  H HB3  . PRO A 1 122 ? 14.463  1.789   72.583  1.00 92.92  ? 122 PRO A HB3  1 
ATOM   1915  H HG2  . PRO A 1 122 ? 15.125  0.816   70.156  1.00 97.58  ? 122 PRO A HG2  1 
ATOM   1916  H HG3  . PRO A 1 122 ? 14.258  2.114   70.453  1.00 97.58  ? 122 PRO A HG3  1 
ATOM   1917  H HD2  . PRO A 1 122 ? 16.648  2.176   69.380  1.00 97.44  ? 122 PRO A HD2  1 
ATOM   1918  H HD3  . PRO A 1 122 ? 15.946  3.440   70.040  1.00 97.44  ? 122 PRO A HD3  1 
ATOM   1919  N N    . LYS A 1 123 ? 17.071  1.115   74.739  1.00 82.51  ? 123 LYS A N    1 
ATOM   1920  C CA   . LYS A 1 123 ? 17.713  0.182   75.654  1.00 82.30  ? 123 LYS A CA   1 
ATOM   1921  C C    . LYS A 1 123 ? 16.974  -1.155  75.655  1.00 82.70  ? 123 LYS A C    1 
ATOM   1922  O O    . LYS A 1 123 ? 15.788  -1.241  75.317  1.00 81.95  ? 123 LYS A O    1 
ATOM   1923  C CB   . LYS A 1 123 ? 17.745  0.741   77.073  1.00 85.35  ? 123 LYS A CB   1 
ATOM   1924  C CG   . LYS A 1 123 ? 18.928  1.650   77.382  1.00 91.48  ? 123 LYS A CG   1 
ATOM   1925  C CD   . LYS A 1 123 ? 20.248  0.888   77.391  1.00 94.22  ? 123 LYS A CD   1 
ATOM   1926  C CE   . LYS A 1 123 ? 21.435  1.845   77.282  1.00 97.74  ? 123 LYS A CE   1 
ATOM   1927  N NZ   . LYS A 1 123 ? 22.745  1.143   77.411  1.00 96.47  ? 123 LYS A NZ   1 
ATOM   1928  H H    . LYS A 1 123 ? 16.514  1.647   75.122  1.00 99.01  ? 123 LYS A H    1 
ATOM   1929  H HA   . LYS A 1 123 ? 18.628  0.038   75.364  1.00 98.76  ? 123 LYS A HA   1 
ATOM   1930  H HB2  . LYS A 1 123 ? 16.936  1.257   77.218  1.00 102.42 ? 123 LYS A HB2  1 
ATOM   1931  H HB3  . LYS A 1 123 ? 17.780  -0.003  77.695  1.00 102.42 ? 123 LYS A HB3  1 
ATOM   1932  H HG2  . LYS A 1 123 ? 18.984  2.342   76.705  1.00 109.78 ? 123 LYS A HG2  1 
ATOM   1933  H HG3  . LYS A 1 123 ? 18.803  2.050   78.257  1.00 109.78 ? 123 LYS A HG3  1 
ATOM   1934  H HD2  . LYS A 1 123 ? 20.329  0.392   78.221  1.00 113.07 ? 123 LYS A HD2  1 
ATOM   1935  H HD3  . LYS A 1 123 ? 20.275  0.278   76.637  1.00 113.07 ? 123 LYS A HD3  1 
ATOM   1936  H HE2  . LYS A 1 123 ? 21.411  2.283   76.417  1.00 117.29 ? 123 LYS A HE2  1 
ATOM   1937  H HE3  . LYS A 1 123 ? 21.376  2.506   77.990  1.00 117.29 ? 123 LYS A HE3  1 
ATOM   1938  H HZ1  . LYS A 1 123 ? 23.399  1.660   77.098  1.00 115.77 ? 123 LYS A HZ1  1 
ATOM   1939  H HZ2  . LYS A 1 123 ? 22.909  0.957   78.265  1.00 115.77 ? 123 LYS A HZ2  1 
ATOM   1940  H HZ3  . LYS A 1 123 ? 22.731  0.383   76.947  1.00 115.77 ? 123 LYS A HZ3  1 
ATOM   1941  N N    . PHE A 1 124 ? 17.687  -2.205  76.054  1.00 84.41  ? 124 PHE A N    1 
ATOM   1942  C CA   . PHE A 1 124 ? 17.094  -3.531  76.139  1.00 87.24  ? 124 PHE A CA   1 
ATOM   1943  C C    . PHE A 1 124 ? 16.336  -3.687  77.450  1.00 86.81  ? 124 PHE A C    1 
ATOM   1944  O O    . PHE A 1 124 ? 16.633  -3.023  78.448  1.00 90.80  ? 124 PHE A O    1 
ATOM   1945  C CB   . PHE A 1 124 ? 18.164  -4.623  76.021  1.00 88.54  ? 124 PHE A CB   1 
ATOM   1946  C CG   . PHE A 1 124 ? 19.152  -4.637  77.155  1.00 84.35  ? 124 PHE A CG   1 
ATOM   1947  C CD1  . PHE A 1 124 ? 18.859  -5.291  78.340  1.00 90.11  ? 124 PHE A CD1  1 
ATOM   1948  C CD2  . PHE A 1 124 ? 20.376  -3.998  77.033  1.00 82.15  ? 124 PHE A CD2  1 
ATOM   1949  C CE1  . PHE A 1 124 ? 19.762  -5.299  79.390  1.00 85.60  ? 124 PHE A CE1  1 
ATOM   1950  C CE2  . PHE A 1 124 ? 21.286  -4.007  78.072  1.00 87.45  ? 124 PHE A CE2  1 
ATOM   1951  C CZ   . PHE A 1 124 ? 20.980  -4.658  79.254  1.00 84.42  ? 124 PHE A CZ   1 
ATOM   1952  H H    . PHE A 1 124 ? 18.516  -2.173  76.281  1.00 101.30 ? 124 PHE A H    1 
ATOM   1953  H HA   . PHE A 1 124 ? 16.471  -3.652  75.405  1.00 104.68 ? 124 PHE A HA   1 
ATOM   1954  H HB2  . PHE A 1 124 ? 17.725  -5.487  76.001  1.00 106.25 ? 124 PHE A HB2  1 
ATOM   1955  H HB3  . PHE A 1 124 ? 18.661  -4.483  75.199  1.00 106.25 ? 124 PHE A HB3  1 
ATOM   1956  H HD1  . PHE A 1 124 ? 18.044  -5.730  78.432  1.00 108.13 ? 124 PHE A HD1  1 
ATOM   1957  H HD2  . PHE A 1 124 ? 20.588  -3.558  76.241  1.00 98.59  ? 124 PHE A HD2  1 
ATOM   1958  H HE1  . PHE A 1 124 ? 19.551  -5.735  80.184  1.00 102.72 ? 124 PHE A HE1  1 
ATOM   1959  H HE2  . PHE A 1 124 ? 22.105  -3.576  77.977  1.00 104.94 ? 124 PHE A HE2  1 
ATOM   1960  H HZ   . PHE A 1 124 ? 21.591  -4.663  79.954  1.00 101.30 ? 124 PHE A HZ   1 
ATOM   1961  N N    . LEU A 1 125 ? 15.349  -4.582  77.442  1.00 89.54  ? 125 LEU A N    1 
ATOM   1962  C CA   . LEU A 1 125 ? 14.567  -4.848  78.644  1.00 91.95  ? 125 LEU A CA   1 
ATOM   1963  C C    . LEU A 1 125 ? 15.121  -6.005  79.462  1.00 90.64  ? 125 LEU A C    1 
ATOM   1964  O O    . LEU A 1 125 ? 14.901  -6.057  80.676  1.00 92.59  ? 125 LEU A O    1 
ATOM   1965  C CB   . LEU A 1 125 ? 13.114  -5.152  78.275  1.00 92.61  ? 125 LEU A CB   1 
ATOM   1966  C CG   . LEU A 1 125 ? 12.389  -4.078  77.465  1.00 96.70  ? 125 LEU A CG   1 
ATOM   1967  C CD1  . LEU A 1 125 ? 11.152  -4.661  76.800  1.00 100.48 ? 125 LEU A CD1  1 
ATOM   1968  C CD2  . LEU A 1 125 ? 12.025  -2.903  78.351  1.00 94.98  ? 125 LEU A CD2  1 
ATOM   1969  H H    . LEU A 1 125 ? 15.116  -5.046  76.757  1.00 107.45 ? 125 LEU A H    1 
ATOM   1970  H HA   . LEU A 1 125 ? 14.577  -4.052  79.199  1.00 110.34 ? 125 LEU A HA   1 
ATOM   1971  H HB2  . LEU A 1 125 ? 13.100  -5.966  77.748  1.00 111.13 ? 125 LEU A HB2  1 
ATOM   1972  H HB3  . LEU A 1 125 ? 12.613  -5.279  79.096  1.00 111.13 ? 125 LEU A HB3  1 
ATOM   1973  H HG   . LEU A 1 125 ? 12.978  -3.752  76.766  1.00 116.04 ? 125 LEU A HG   1 
ATOM   1974  H HD11 . LEU A 1 125 ? 10.710  -3.964  76.289  1.00 120.58 ? 125 LEU A HD11 1 
ATOM   1975  H HD12 . LEU A 1 125 ? 11.421  -5.383  76.210  1.00 120.58 ? 125 LEU A HD12 1 
ATOM   1976  H HD13 . LEU A 1 125 ? 10.554  -4.998  77.485  1.00 120.58 ? 125 LEU A HD13 1 
ATOM   1977  H HD21 . LEU A 1 125 ? 11.567  -2.234  77.817  1.00 113.98 ? 125 LEU A HD21 1 
ATOM   1978  H HD22 . LEU A 1 125 ? 11.443  -3.212  79.063  1.00 113.98 ? 125 LEU A HD22 1 
ATOM   1979  H HD23 . LEU A 1 125 ? 12.836  -2.527  78.727  1.00 113.98 ? 125 LEU A HD23 1 
ATOM   1980  N N    . SER A 1 126 ? 15.821  -6.941  78.825  1.00 91.66  ? 126 SER A N    1 
ATOM   1981  C CA   . SER A 1 126 ? 16.411  -8.067  79.531  1.00 88.74  ? 126 SER A CA   1 
ATOM   1982  C C    . SER A 1 126 ? 17.485  -8.685  78.650  1.00 90.42  ? 126 SER A C    1 
ATOM   1983  O O    . SER A 1 126 ? 17.409  -8.626  77.421  1.00 91.61  ? 126 SER A O    1 
ATOM   1984  C CB   . SER A 1 126 ? 15.358  -9.117  79.900  1.00 92.54  ? 126 SER A CB   1 
ATOM   1985  O OG   . SER A 1 126 ? 15.127  -9.990  78.810  1.00 93.93  ? 126 SER A OG   1 
ATOM   1986  H H    . SER A 1 126 ? 15.968  -6.943  77.978  1.00 110.00 ? 126 SER A H    1 
ATOM   1987  H HA   . SER A 1 126 ? 16.826  -7.754  80.349  1.00 106.49 ? 126 SER A HA   1 
ATOM   1988  H HB2  . SER A 1 126 ? 15.676  -9.632  80.658  1.00 111.06 ? 126 SER A HB2  1 
ATOM   1989  H HB3  . SER A 1 126 ? 14.529  -8.668  80.128  1.00 111.06 ? 126 SER A HB3  1 
ATOM   1990  H HG   . SER A 1 126 ? 14.534  -10.551 79.012  1.00 112.72 ? 126 SER A HG   1 
ATOM   1991  N N    . LEU A 1 127 ? 18.484  -9.280  79.296  1.00 90.57  ? 127 LEU A N    1 
ATOM   1992  C CA   . LEU A 1 127 ? 19.586  -9.953  78.615  1.00 92.50  ? 127 LEU A CA   1 
ATOM   1993  C C    . LEU A 1 127 ? 19.766  -11.317 79.266  1.00 94.84  ? 127 LEU A C    1 
ATOM   1994  O O    . LEU A 1 127 ? 20.176  -11.403 80.429  1.00 96.54  ? 127 LEU A O    1 
ATOM   1995  C CB   . LEU A 1 127 ? 20.867  -9.127  78.695  1.00 91.70  ? 127 LEU A CB   1 
ATOM   1996  C CG   . LEU A 1 127 ? 22.122  -9.678  78.022  1.00 94.67  ? 127 LEU A CG   1 
ATOM   1997  C CD1  . LEU A 1 127 ? 21.798  -10.513 76.794  1.00 90.23  ? 127 LEU A CD1  1 
ATOM   1998  C CD2  . LEU A 1 127 ? 23.066  -8.535  77.644  1.00 94.72  ? 127 LEU A CD2  1 
ATOM   1999  H H    . LEU A 1 127 ? 18.547  -9.308  80.153  1.00 108.68 ? 127 LEU A H    1 
ATOM   2000  H HA   . LEU A 1 127 ? 19.370  -10.082 77.678  1.00 111.00 ? 127 LEU A HA   1 
ATOM   2001  H HB2  . LEU A 1 127 ? 20.688  -8.266  78.286  1.00 110.04 ? 127 LEU A HB2  1 
ATOM   2002  H HB3  . LEU A 1 127 ? 21.084  -9.010  79.633  1.00 110.04 ? 127 LEU A HB3  1 
ATOM   2003  H HG   . LEU A 1 127 ? 22.566  -10.264 78.656  1.00 113.60 ? 127 LEU A HG   1 
ATOM   2004  H HD11 . LEU A 1 127 ? 22.609  -10.646 76.279  1.00 108.28 ? 127 LEU A HD11 1 
ATOM   2005  H HD12 . LEU A 1 127 ? 21.443  -11.370 77.080  1.00 108.28 ? 127 LEU A HD12 1 
ATOM   2006  H HD13 . LEU A 1 127 ? 21.139  -10.044 76.258  1.00 108.28 ? 127 LEU A HD13 1 
ATOM   2007  H HD21 . LEU A 1 127 ? 23.876  -8.908  77.263  1.00 113.66 ? 127 LEU A HD21 1 
ATOM   2008  H HD22 . LEU A 1 127 ? 22.626  -7.964  76.995  1.00 113.66 ? 127 LEU A HD22 1 
ATOM   2009  H HD23 . LEU A 1 127 ? 23.279  -8.026  78.442  1.00 113.66 ? 127 LEU A HD23 1 
ATOM   2010  N N    . GLU A 1 128 ? 19.445  -12.376 78.525  1.00 95.41  ? 128 GLU A N    1 
ATOM   2011  C CA   . GLU A 1 128 ? 19.560  -13.740 79.013  1.00 97.96  ? 128 GLU A CA   1 
ATOM   2012  C C    . GLU A 1 128 ? 20.479  -14.549 78.107  1.00 95.83  ? 128 GLU A C    1 
ATOM   2013  O O    . GLU A 1 128 ? 20.525  -14.339 76.891  1.00 97.45  ? 128 GLU A O    1 
ATOM   2014  C CB   . GLU A 1 128 ? 18.192  -14.438 79.086  1.00 99.68  ? 128 GLU A CB   1 
ATOM   2015  C CG   . GLU A 1 128 ? 17.031  -13.540 79.476  1.00 102.28 ? 128 GLU A CG   1 
ATOM   2016  C CD   . GLU A 1 128 ? 15.773  -14.328 79.799  1.00 104.49 ? 128 GLU A CD   1 
ATOM   2017  O OE1  . GLU A 1 128 ? 15.600  -15.432 79.240  1.00 104.29 ? 128 GLU A OE1  1 
ATOM   2018  O OE2  . GLU A 1 128 ? 14.957  -13.846 80.613  1.00 105.99 ? 128 GLU A OE2  1 
ATOM   2019  H H    . GLU A 1 128 ? 19.153  -12.324 77.717  1.00 114.49 ? 128 GLU A H    1 
ATOM   2020  H HA   . GLU A 1 128 ? 19.942  -13.717 79.904  1.00 117.55 ? 128 GLU A HA   1 
ATOM   2021  H HB2  . GLU A 1 128 ? 17.991  -14.810 78.213  1.00 119.61 ? 128 GLU A HB2  1 
ATOM   2022  H HB3  . GLU A 1 128 ? 18.245  -15.147 79.745  1.00 119.61 ? 128 GLU A HB3  1 
ATOM   2023  H HG2  . GLU A 1 128 ? 17.276  -13.028 80.262  1.00 122.74 ? 128 GLU A HG2  1 
ATOM   2024  H HG3  . GLU A 1 128 ? 16.831  -12.942 78.739  1.00 122.74 ? 128 GLU A HG3  1 
ATOM   2025  N N    . GLU A 1 129 ? 21.213  -15.476 78.715  1.00 98.23  ? 129 GLU A N    1 
ATOM   2026  C CA   . GLU A 1 129 ? 21.990  -16.489 78.006  1.00 95.23  ? 129 GLU A CA   1 
ATOM   2027  C C    . GLU A 1 129 ? 21.261  -17.811 78.205  1.00 95.15  ? 129 GLU A C    1 
ATOM   2028  O O    . GLU A 1 129 ? 21.180  -18.314 79.331  1.00 98.70  ? 129 GLU A O    1 
ATOM   2029  C CB   . GLU A 1 129 ? 23.420  -16.553 78.527  1.00 97.42  ? 129 GLU A CB   1 
ATOM   2030  C CG   . GLU A 1 129 ? 24.311  -17.509 77.759  1.00 99.55  ? 129 GLU A CG   1 
ATOM   2031  C CD   . GLU A 1 129 ? 25.774  -17.119 77.832  1.00 105.46 ? 129 GLU A CD   1 
ATOM   2032  O OE1  . GLU A 1 129 ? 26.131  -16.291 78.701  1.00 107.21 ? 129 GLU A OE1  1 
ATOM   2033  O OE2  . GLU A 1 129 ? 26.566  -17.640 77.019  1.00 106.61 ? 129 GLU A OE2  1 
ATOM   2034  H H    . GLU A 1 129 ? 21.279  -15.542 79.570  1.00 117.87 ? 129 GLU A H    1 
ATOM   2035  H HA   . GLU A 1 129 ? 22.036  -16.282 77.059  1.00 114.28 ? 129 GLU A HA   1 
ATOM   2036  H HB2  . GLU A 1 129 ? 23.814  -15.668 78.467  1.00 116.91 ? 129 GLU A HB2  1 
ATOM   2037  H HB3  . GLU A 1 129 ? 23.402  -16.845 79.452  1.00 116.91 ? 129 GLU A HB3  1 
ATOM   2038  H HG2  . GLU A 1 129 ? 24.218  -18.399 78.132  1.00 119.46 ? 129 GLU A HG2  1 
ATOM   2039  H HG3  . GLU A 1 129 ? 24.046  -17.510 76.826  1.00 119.46 ? 129 GLU A HG3  1 
ATOM   2040  N N    . ILE A 1 130 ? 20.728  -18.367 77.120  1.00 95.38  ? 130 ILE A N    1 
ATOM   2041  C CA   . ILE A 1 130 ? 19.832  -19.512 77.196  1.00 95.89  ? 130 ILE A CA   1 
ATOM   2042  C C    . ILE A 1 130 ? 20.455  -20.706 76.491  1.00 96.53  ? 130 ILE A C    1 
ATOM   2043  O O    . ILE A 1 130 ? 21.155  -20.566 75.484  1.00 100.51 ? 130 ILE A O    1 
ATOM   2044  C CB   . ILE A 1 130 ? 18.450  -19.184 76.585  1.00 93.99  ? 130 ILE A CB   1 
ATOM   2045  C CG1  . ILE A 1 130 ? 18.596  -18.714 75.139  1.00 97.91  ? 130 ILE A CG1  1 
ATOM   2046  C CG2  . ILE A 1 130 ? 17.748  -18.110 77.402  1.00 97.59  ? 130 ILE A CG2  1 
ATOM   2047  C CD1  . ILE A 1 130 ? 17.290  -18.701 74.364  1.00 97.57  ? 130 ILE A CD1  1 
ATOM   2048  H H    . ILE A 1 130 ? 20.874  -18.093 76.318  1.00 114.46 ? 130 ILE A H    1 
ATOM   2049  H HA   . ILE A 1 130 ? 19.717  -19.754 78.128  1.00 115.07 ? 130 ILE A HA   1 
ATOM   2050  H HB   . ILE A 1 130 ? 17.920  -19.996 76.600  1.00 112.79 ? 130 ILE A HB   1 
ATOM   2051  H HG12 . ILE A 1 130 ? 18.948  -17.810 75.139  1.00 117.49 ? 130 ILE A HG12 1 
ATOM   2052  H HG13 . ILE A 1 130 ? 19.208  -19.308 74.678  1.00 117.49 ? 130 ILE A HG13 1 
ATOM   2053  H HG21 . ILE A 1 130 ? 16.882  -17.927 77.005  1.00 117.11 ? 130 ILE A HG21 1 
ATOM   2054  H HG22 . ILE A 1 130 ? 17.634  -18.427 78.311  1.00 117.11 ? 130 ILE A HG22 1 
ATOM   2055  H HG23 . ILE A 1 130 ? 18.289  -17.305 77.398  1.00 117.11 ? 130 ILE A HG23 1 
ATOM   2056  H HD11 . ILE A 1 130 ? 17.461  -18.386 73.462  1.00 117.08 ? 130 ILE A HD11 1 
ATOM   2057  H HD12 . ILE A 1 130 ? 16.931  -19.602 74.337  1.00 117.08 ? 130 ILE A HD12 1 
ATOM   2058  H HD13 . ILE A 1 130 ? 16.664  -18.109 74.808  1.00 117.08 ? 130 ILE A HD13 1 
ATOM   2059  N N    . ASN A 1 131 ? 20.191  -21.894 77.037  1.00 98.61  ? 131 ASN A N    1 
ATOM   2060  C CA   . ASN A 1 131 ? 20.598  -23.166 76.449  1.00 96.93  ? 131 ASN A CA   1 
ATOM   2061  C C    . ASN A 1 131 ? 19.334  -23.867 75.963  1.00 99.49  ? 131 ASN A C    1 
ATOM   2062  O O    . ASN A 1 131 ? 18.494  -24.270 76.776  1.00 96.83  ? 131 ASN A O    1 
ATOM   2063  C CB   . ASN A 1 131 ? 21.347  -24.031 77.463  1.00 98.72  ? 131 ASN A CB   1 
ATOM   2064  C CG   . ASN A 1 131 ? 22.855  -23.920 77.327  1.00 100.39 ? 131 ASN A CG   1 
ATOM   2065  O OD1  . ASN A 1 131 ? 23.490  -23.107 77.995  1.00 104.56 ? 131 ASN A OD1  1 
ATOM   2066  N ND2  . ASN A 1 131 ? 23.435  -24.746 76.465  1.00 102.60 ? 131 ASN A ND2  1 
ATOM   2067  H H    . ASN A 1 131 ? 19.762  -21.989 77.776  1.00 118.33 ? 131 ASN A H    1 
ATOM   2068  H HA   . ASN A 1 131 ? 21.189  -23.007 75.697  1.00 116.31 ? 131 ASN A HA   1 
ATOM   2069  H HB2  . ASN A 1 131 ? 21.104  -23.749 78.359  1.00 118.47 ? 131 ASN A HB2  1 
ATOM   2070  H HB3  . ASN A 1 131 ? 21.100  -24.959 77.330  1.00 118.47 ? 131 ASN A HB3  1 
ATOM   2071  H HD21 . ASN A 1 131 ? 22.959  -25.306 76.019  1.00 123.12 ? 131 ASN A HD21 1 
ATOM   2072  H HD22 . ASN A 1 131 ? 24.287  -24.722 76.353  1.00 123.12 ? 131 ASN A HD22 1 
ATOM   2073  N N    . VAL A 1 132 ? 19.195  -24.003 74.646  1.00 103.08 ? 132 VAL A N    1 
ATOM   2074  C CA   . VAL A 1 132 ? 18.037  -24.639 74.027  1.00 102.64 ? 132 VAL A CA   1 
ATOM   2075  C C    . VAL A 1 132 ? 18.502  -25.945 73.405  1.00 105.45 ? 132 VAL A C    1 
ATOM   2076  O O    . VAL A 1 132 ? 19.333  -25.941 72.489  1.00 105.95 ? 132 VAL A O    1 
ATOM   2077  C CB   . VAL A 1 132 ? 17.386  -23.732 72.972  1.00 107.22 ? 132 VAL A CB   1 
ATOM   2078  C CG1  . VAL A 1 132 ? 16.589  -24.556 71.975  1.00 110.91 ? 132 VAL A CG1  1 
ATOM   2079  C CG2  . VAL A 1 132 ? 16.502  -22.706 73.648  1.00 106.90 ? 132 VAL A CG2  1 
ATOM   2080  H H    . VAL A 1 132 ? 19.776  -23.726 74.076  1.00 123.70 ? 132 VAL A H    1 
ATOM   2081  H HA   . VAL A 1 132 ? 17.377  -24.837 74.710  1.00 123.16 ? 132 VAL A HA   1 
ATOM   2082  H HB   . VAL A 1 132 ? 18.080  -23.265 72.482  1.00 128.67 ? 132 VAL A HB   1 
ATOM   2083  H HG11 . VAL A 1 132 ? 15.976  -23.973 71.501  1.00 133.09 ? 132 VAL A HG11 1 
ATOM   2084  H HG12 . VAL A 1 132 ? 17.202  -24.971 71.347  1.00 133.09 ? 132 VAL A HG12 1 
ATOM   2085  H HG13 . VAL A 1 132 ? 16.093  -25.239 72.453  1.00 133.09 ? 132 VAL A HG13 1 
ATOM   2086  H HG21 . VAL A 1 132 ? 16.111  -22.132 72.971  1.00 128.28 ? 132 VAL A HG21 1 
ATOM   2087  H HG22 . VAL A 1 132 ? 15.802  -23.165 74.137  1.00 128.28 ? 132 VAL A HG22 1 
ATOM   2088  H HG23 . VAL A 1 132 ? 17.041  -22.178 74.258  1.00 128.28 ? 132 VAL A HG23 1 
ATOM   2089  N N    . ASP A 1 133 ? 17.957  -27.060 73.892  1.00 109.89 ? 133 ASP A N    1 
ATOM   2090  C CA   . ASP A 1 133 ? 18.376  -28.375 73.418  1.00 107.84 ? 133 ASP A CA   1 
ATOM   2091  C C    . ASP A 1 133 ? 19.884  -28.499 73.590  1.00 106.21 ? 133 ASP A C    1 
ATOM   2092  O O    . ASP A 1 133 ? 20.389  -28.406 74.715  1.00 108.61 ? 133 ASP A O    1 
ATOM   2093  C CB   . ASP A 1 133 ? 17.938  -28.576 71.972  1.00 112.03 ? 133 ASP A CB   1 
ATOM   2094  C CG   . ASP A 1 133 ? 16.426  -28.673 71.838  1.00 117.10 ? 133 ASP A CG   1 
ATOM   2095  O OD1  . ASP A 1 133 ? 15.737  -28.749 72.881  1.00 118.80 ? 133 ASP A OD1  1 
ATOM   2096  O OD2  . ASP A 1 133 ? 15.931  -28.676 70.690  1.00 117.72 ? 133 ASP A OD2  1 
ATOM   2097  H H    . ASP A 1 133 ? 17.344  -27.081 74.496  1.00 131.87 ? 133 ASP A H    1 
ATOM   2098  H HA   . ASP A 1 133 ? 17.956  -29.085 73.929  1.00 129.41 ? 133 ASP A HA   1 
ATOM   2099  H HB2  . ASP A 1 133 ? 18.240  -27.823 71.440  1.00 134.44 ? 133 ASP A HB2  1 
ATOM   2100  H HB3  . ASP A 1 133 ? 18.324  -29.399 71.633  1.00 134.44 ? 133 ASP A HB3  1 
ATOM   2101  N N    . GLU A 1 134 ? 20.616  -28.693 72.497  1.00 106.48 ? 134 GLU A N    1 
ATOM   2102  C CA   . GLU A 1 134 ? 22.068  -28.808 72.551  1.00 107.53 ? 134 GLU A CA   1 
ATOM   2103  C C    . GLU A 1 134 ? 22.762  -27.612 71.903  1.00 106.66 ? 134 GLU A C    1 
ATOM   2104  O O    . GLU A 1 134 ? 23.863  -27.743 71.360  1.00 107.38 ? 134 GLU A O    1 
ATOM   2105  C CB   . GLU A 1 134 ? 22.528  -30.106 71.890  1.00 113.00 ? 134 GLU A CB   1 
ATOM   2106  C CG   . GLU A 1 134 ? 21.931  -30.345 70.514  1.00 111.62 ? 134 GLU A CG   1 
ATOM   2107  C CD   . GLU A 1 134 ? 22.687  -31.404 69.736  1.00 115.05 ? 134 GLU A CD   1 
ATOM   2108  O OE1  . GLU A 1 134 ? 23.756  -31.848 70.211  1.00 117.29 ? 134 GLU A OE1  1 
ATOM   2109  O OE2  . GLU A 1 134 ? 22.213  -31.794 68.647  1.00 116.73 ? 134 GLU A OE2  1 
ATOM   2110  H H    . GLU A 1 134 ? 20.289  -28.762 71.705  1.00 127.78 ? 134 GLU A H    1 
ATOM   2111  H HA   . GLU A 1 134 ? 22.335  -28.833 73.483  1.00 129.03 ? 134 GLU A HA   1 
ATOM   2112  H HB2  . GLU A 1 134 ? 23.492  -30.080 71.793  1.00 135.60 ? 134 GLU A HB2  1 
ATOM   2113  H HB3  . GLU A 1 134 ? 22.271  -30.850 72.456  1.00 135.60 ? 134 GLU A HB3  1 
ATOM   2114  H HG2  . GLU A 1 134 ? 21.012  -30.641 70.613  1.00 133.95 ? 134 GLU A HG2  1 
ATOM   2115  H HG3  . GLU A 1 134 ? 21.960  -29.519 70.006  1.00 133.95 ? 134 GLU A HG3  1 
ATOM   2116  N N    . TYR A 1 135 ? 22.130  -26.442 71.957  1.00 103.88 ? 135 TYR A N    1 
ATOM   2117  C CA   . TYR A 1 135 ? 22.701  -25.217 71.426  1.00 101.31 ? 135 TYR A CA   1 
ATOM   2118  C C    . TYR A 1 135 ? 22.656  -24.124 72.485  1.00 100.08 ? 135 TYR A C    1 
ATOM   2119  O O    . TYR A 1 135 ? 21.671  -23.998 73.219  1.00 99.13  ? 135 TYR A O    1 
ATOM   2120  C CB   . TYR A 1 135 ? 21.946  -24.742 70.178  1.00 103.09 ? 135 TYR A CB   1 
ATOM   2121  C CG   . TYR A 1 135 ? 21.912  -25.732 69.033  1.00 105.77 ? 135 TYR A CG   1 
ATOM   2122  C CD1  . TYR A 1 135 ? 23.072  -26.076 68.352  1.00 106.58 ? 135 TYR A CD1  1 
ATOM   2123  C CD2  . TYR A 1 135 ? 20.717  -26.310 68.625  1.00 107.43 ? 135 TYR A CD2  1 
ATOM   2124  C CE1  . TYR A 1 135 ? 23.046  -26.976 67.303  1.00 109.05 ? 135 TYR A CE1  1 
ATOM   2125  C CE2  . TYR A 1 135 ? 20.680  -27.212 67.576  1.00 109.78 ? 135 TYR A CE2  1 
ATOM   2126  C CZ   . TYR A 1 135 ? 21.847  -27.540 66.919  1.00 110.81 ? 135 TYR A CZ   1 
ATOM   2127  O OH   . TYR A 1 135 ? 21.815  -28.435 65.874  1.00 111.98 ? 135 TYR A OH   1 
ATOM   2128  H H    . TYR A 1 135 ? 21.352  -26.335 72.307  1.00 124.65 ? 135 TYR A H    1 
ATOM   2129  H HA   . TYR A 1 135 ? 23.628  -25.377 71.186  1.00 121.57 ? 135 TYR A HA   1 
ATOM   2130  H HB2  . TYR A 1 135 ? 21.027  -24.555 70.428  1.00 123.71 ? 135 TYR A HB2  1 
ATOM   2131  H HB3  . TYR A 1 135 ? 22.371  -23.934 69.851  1.00 123.71 ? 135 TYR A HB3  1 
ATOM   2132  H HD1  . TYR A 1 135 ? 23.882  -25.694 68.607  1.00 127.90 ? 135 TYR A HD1  1 
ATOM   2133  H HD2  . TYR A 1 135 ? 19.928  -26.088 69.064  1.00 128.92 ? 135 TYR A HD2  1 
ATOM   2134  H HE1  . TYR A 1 135 ? 23.832  -27.200 66.859  1.00 130.86 ? 135 TYR A HE1  1 
ATOM   2135  H HE2  . TYR A 1 135 ? 19.873  -27.594 67.316  1.00 131.74 ? 135 TYR A HE2  1 
ATOM   2136  H HH   . TYR A 1 135 ? 21.027  -28.691 65.740  1.00 134.37 ? 135 TYR A HH   1 
ATOM   2137  N N    . LYS A 1 136 ? 23.730  -23.342 72.565  1.00 100.09 ? 136 LYS A N    1 
ATOM   2138  C CA   . LYS A 1 136 ? 23.740  -22.102 73.329  1.00 96.16  ? 136 LYS A CA   1 
ATOM   2139  C C    . LYS A 1 136 ? 23.214  -21.000 72.419  1.00 99.98  ? 136 LYS A C    1 
ATOM   2140  O O    . LYS A 1 136 ? 23.668  -20.861 71.275  1.00 98.38  ? 136 LYS A O    1 
ATOM   2141  C CB   . LYS A 1 136 ? 25.156  -21.785 73.825  1.00 95.35  ? 136 LYS A CB   1 
ATOM   2142  C CG   . LYS A 1 136 ? 25.369  -20.391 74.455  1.00 102.60 ? 136 LYS A CG   1 
ATOM   2143  C CD   . LYS A 1 136 ? 25.255  -19.244 73.451  1.00 101.59 ? 136 LYS A CD   1 
ATOM   2144  C CE   . LYS A 1 136 ? 25.290  -17.882 74.129  1.00 98.89  ? 136 LYS A CE   1 
ATOM   2145  N NZ   . LYS A 1 136 ? 25.570  -16.849 73.095  1.00 100.78 ? 136 LYS A NZ   1 
ATOM   2146  H H    . LYS A 1 136 ? 24.478  -23.512 72.177  1.00 120.11 ? 136 LYS A H    1 
ATOM   2147  H HA   . LYS A 1 136 ? 23.175  -22.168 74.115  1.00 115.40 ? 136 LYS A HA   1 
ATOM   2148  H HB2  . LYS A 1 136 ? 25.394  -22.441 74.499  1.00 114.42 ? 136 LYS A HB2  1 
ATOM   2149  H HB3  . LYS A 1 136 ? 25.761  -21.851 73.070  1.00 114.42 ? 136 LYS A HB3  1 
ATOM   2150  H HG2  . LYS A 1 136 ? 24.699  -20.251 75.142  1.00 123.12 ? 136 LYS A HG2  1 
ATOM   2151  H HG3  . LYS A 1 136 ? 26.257  -20.355 74.845  1.00 123.12 ? 136 LYS A HG3  1 
ATOM   2152  H HD2  . LYS A 1 136 ? 25.997  -19.290 72.828  1.00 121.90 ? 136 LYS A HD2  1 
ATOM   2153  H HD3  . LYS A 1 136 ? 24.415  -19.322 72.972  1.00 121.90 ? 136 LYS A HD3  1 
ATOM   2154  H HE2  . LYS A 1 136 ? 24.433  -17.693 74.542  1.00 118.67 ? 136 LYS A HE2  1 
ATOM   2155  H HE3  . LYS A 1 136 ? 25.993  -17.861 74.797  1.00 118.67 ? 136 LYS A HE3  1 
ATOM   2156  H HZ1  . LYS A 1 136 ? 25.584  -16.041 73.467  1.00 120.94 ? 136 LYS A HZ1  1 
ATOM   2157  H HZ2  . LYS A 1 136 ? 26.359  -17.005 72.714  1.00 120.94 ? 136 LYS A HZ2  1 
ATOM   2158  H HZ3  . LYS A 1 136 ? 24.939  -16.867 72.468  1.00 120.94 ? 136 LYS A HZ3  1 
ATOM   2159  N N    . LEU A 1 137 ? 22.336  -20.149 72.957  1.00 98.56  ? 137 LEU A N    1 
ATOM   2160  C CA   . LEU A 1 137 ? 21.881  -18.965 72.243  1.00 96.51  ? 137 LEU A CA   1 
ATOM   2161  C C    . LEU A 1 137 ? 21.930  -17.748 73.159  1.00 96.05  ? 137 LEU A C    1 
ATOM   2162  O O    . LEU A 1 137 ? 21.835  -17.867 74.385  1.00 94.47  ? 137 LEU A O    1 
ATOM   2163  C CB   . LEU A 1 137 ? 20.451  -19.131 71.728  1.00 96.77  ? 137 LEU A CB   1 
ATOM   2164  C CG   . LEU A 1 137 ? 20.143  -20.152 70.637  1.00 96.86  ? 137 LEU A CG   1 
ATOM   2165  C CD1  . LEU A 1 137 ? 20.673  -21.531 70.930  1.00 99.84  ? 137 LEU A CD1  1 
ATOM   2166  C CD2  . LEU A 1 137 ? 18.619  -20.206 70.450  1.00 100.64 ? 137 LEU A CD2  1 
ATOM   2167  H H    . LEU A 1 137 ? 21.991  -20.241 73.739  1.00 118.27 ? 137 LEU A H    1 
ATOM   2168  H HA   . LEU A 1 137 ? 22.473  -18.811 71.490  1.00 115.81 ? 137 LEU A HA   1 
ATOM   2169  H HB2  . LEU A 1 137 ? 19.900  -19.376 72.488  1.00 116.12 ? 137 LEU A HB2  1 
ATOM   2170  H HB3  . LEU A 1 137 ? 20.172  -18.271 71.378  1.00 116.12 ? 137 LEU A HB3  1 
ATOM   2171  H HG   . LEU A 1 137 ? 20.588  -19.870 69.823  1.00 116.23 ? 137 LEU A HG   1 
ATOM   2172  H HD11 . LEU A 1 137 ? 20.098  -22.188 70.507  1.00 119.80 ? 137 LEU A HD11 1 
ATOM   2173  H HD12 . LEU A 1 137 ? 21.574  -21.605 70.578  1.00 119.80 ? 137 LEU A HD12 1 
ATOM   2174  H HD13 . LEU A 1 137 ? 20.681  -21.669 71.891  1.00 119.80 ? 137 LEU A HD13 1 
ATOM   2175  H HD21 . LEU A 1 137 ? 18.412  -20.807 69.718  1.00 120.77 ? 137 LEU A HD21 1 
ATOM   2176  H HD22 . LEU A 1 137 ? 18.212  -20.530 71.269  1.00 120.77 ? 137 LEU A HD22 1 
ATOM   2177  H HD23 . LEU A 1 137 ? 18.293  -19.315 70.249  1.00 120.77 ? 137 LEU A HD23 1 
ATOM   2178  N N    . GLY A 1 138 ? 22.068  -16.573 72.549  1.00 90.20  ? 138 GLY A N    1 
ATOM   2179  C CA   . GLY A 1 138 ? 21.889  -15.313 73.242  1.00 93.22  ? 138 GLY A CA   1 
ATOM   2180  C C    . GLY A 1 138 ? 20.477  -14.805 73.020  1.00 91.69  ? 138 GLY A C    1 
ATOM   2181  O O    . GLY A 1 138 ? 19.886  -15.019 71.964  1.00 89.21  ? 138 GLY A O    1 
ATOM   2182  H H    . GLY A 1 138 ? 22.269  -16.484 71.718  1.00 108.25 ? 138 GLY A H    1 
ATOM   2183  H HA2  . GLY A 1 138 ? 22.037  -15.434 74.194  1.00 111.87 ? 138 GLY A HA2  1 
ATOM   2184  H HA3  . GLY A 1 138 ? 22.520  -14.657 72.906  1.00 111.87 ? 138 GLY A HA3  1 
ATOM   2185  N N    . LEU A 1 139 ? 19.929  -14.133 74.031  1.00 90.92  ? 139 LEU A N    1 
ATOM   2186  C CA   . LEU A 1 139 ? 18.555  -13.641 73.966  1.00 89.12  ? 139 LEU A CA   1 
ATOM   2187  C C    . LEU A 1 139 ? 18.498  -12.233 74.533  1.00 89.42  ? 139 LEU A C    1 
ATOM   2188  O O    . LEU A 1 139 ? 18.862  -12.012 75.691  1.00 88.30  ? 139 LEU A O    1 
ATOM   2189  C CB   . LEU A 1 139 ? 17.606  -14.568 74.729  1.00 92.99  ? 139 LEU A CB   1 
ATOM   2190  C CG   . LEU A 1 139 ? 16.114  -14.342 74.498  1.00 92.93  ? 139 LEU A CG   1 
ATOM   2191  C CD1  . LEU A 1 139 ? 15.301  -15.550 74.948  1.00 96.10  ? 139 LEU A CD1  1 
ATOM   2192  C CD2  . LEU A 1 139 ? 15.657  -13.101 75.234  1.00 92.54  ? 139 LEU A CD2  1 
ATOM   2193  H H    . LEU A 1 139 ? 20.334  -13.949 74.767  1.00 109.11 ? 139 LEU A H    1 
ATOM   2194  H HA   . LEU A 1 139 ? 18.274  -13.600 73.039  1.00 106.94 ? 139 LEU A HA   1 
ATOM   2195  H HB2  . LEU A 1 139 ? 17.802  -15.481 74.467  1.00 111.59 ? 139 LEU A HB2  1 
ATOM   2196  H HB3  . LEU A 1 139 ? 17.770  -14.453 75.678  1.00 111.59 ? 139 LEU A HB3  1 
ATOM   2197  H HG   . LEU A 1 139 ? 15.960  -14.218 73.549  1.00 111.52 ? 139 LEU A HG   1 
ATOM   2198  H HD11 . LEU A 1 139 ? 14.358  -15.353 74.841  1.00 115.32 ? 139 LEU A HD11 1 
ATOM   2199  H HD12 . LEU A 1 139 ? 15.544  -16.314 74.402  1.00 115.32 ? 139 LEU A HD12 1 
ATOM   2200  H HD13 . LEU A 1 139 ? 15.497  -15.733 75.880  1.00 115.32 ? 139 LEU A HD13 1 
ATOM   2201  H HD21 . LEU A 1 139 ? 14.731  -13.214 75.499  1.00 111.05 ? 139 LEU A HD21 1 
ATOM   2202  H HD22 . LEU A 1 139 ? 16.213  -12.976 76.018  1.00 111.05 ? 139 LEU A HD22 1 
ATOM   2203  H HD23 . LEU A 1 139 ? 15.741  -12.335 74.644  1.00 111.05 ? 139 LEU A HD23 1 
ATOM   2204  N N    . VAL A 1 140 ? 18.037  -11.288 73.717  1.00 89.29  ? 140 VAL A N    1 
ATOM   2205  C CA   . VAL A 1 140 ? 17.903  -9.889  74.108  1.00 87.74  ? 140 VAL A CA   1 
ATOM   2206  C C    . VAL A 1 140 ? 16.469  -9.470  73.811  1.00 88.82  ? 140 VAL A C    1 
ATOM   2207  O O    . VAL A 1 140 ? 16.042  -9.490  72.650  1.00 88.73  ? 140 VAL A O    1 
ATOM   2208  C CB   . VAL A 1 140 ? 18.894  -8.975  73.368  1.00 86.13  ? 140 VAL A CB   1 
ATOM   2209  C CG1  . VAL A 1 140 ? 19.092  -7.678  74.147  1.00 86.45  ? 140 VAL A CG1  1 
ATOM   2210  C CG2  . VAL A 1 140 ? 20.233  -9.668  73.147  1.00 85.21  ? 140 VAL A CG2  1 
ATOM   2211  H H    . VAL A 1 140 ? 17.787  -11.439 72.907  1.00 107.15 ? 140 VAL A H    1 
ATOM   2212  H HA   . VAL A 1 140 ? 18.070  -9.802  75.060  1.00 105.29 ? 140 VAL A HA   1 
ATOM   2213  H HB   . VAL A 1 140 ? 18.525  -8.766  72.495  1.00 103.35 ? 140 VAL A HB   1 
ATOM   2214  H HG11 . VAL A 1 140 ? 19.677  -7.092  73.642  1.00 103.74 ? 140 VAL A HG11 1 
ATOM   2215  H HG12 . VAL A 1 140 ? 18.230  -7.252  74.276  1.00 103.74 ? 140 VAL A HG12 1 
ATOM   2216  H HG13 . VAL A 1 140 ? 19.491  -7.884  75.007  1.00 103.74 ? 140 VAL A HG13 1 
ATOM   2217  H HG21 . VAL A 1 140 ? 20.696  -9.235  72.413  1.00 102.25 ? 140 VAL A HG21 1 
ATOM   2218  H HG22 . VAL A 1 140 ? 20.761  -9.599  73.958  1.00 102.25 ? 140 VAL A HG22 1 
ATOM   2219  H HG23 . VAL A 1 140 ? 20.075  -10.601 72.934  1.00 102.25 ? 140 VAL A HG23 1 
ATOM   2220  N N    . ARG A 1 141 ? 15.728  -9.095  74.851  1.00 88.02  ? 141 ARG A N    1 
ATOM   2221  C CA   . ARG A 1 141 ? 14.324  -8.728  74.714  1.00 89.70  ? 141 ARG A CA   1 
ATOM   2222  C C    . ARG A 1 141 ? 14.203  -7.211  74.641  1.00 92.20  ? 141 ARG A C    1 
ATOM   2223  O O    . ARG A 1 141 ? 14.683  -6.499  75.531  1.00 91.51  ? 141 ARG A O    1 
ATOM   2224  C CB   . ARG A 1 141 ? 13.499  -9.277  75.876  1.00 91.81  ? 141 ARG A CB   1 
ATOM   2225  C CG   . ARG A 1 141 ? 13.865  -10.708 76.243  1.00 93.78  ? 141 ARG A CG   1 
ATOM   2226  C CD   . ARG A 1 141 ? 12.767  -11.414 77.040  1.00 91.10  ? 141 ARG A CD   1 
ATOM   2227  N NE   . ARG A 1 141 ? 12.002  -12.322 76.192  1.00 93.21  ? 141 ARG A NE   1 
ATOM   2228  C CZ   . ARG A 1 141 ? 11.909  -13.634 76.365  1.00 93.91  ? 141 ARG A CZ   1 
ATOM   2229  N NH1  . ARG A 1 141 ? 12.500  -14.244 77.380  1.00 91.57  ? 141 ARG A NH1  1 
ATOM   2230  N NH2  . ARG A 1 141 ? 11.204  -14.353 75.496  1.00 101.33 ? 141 ARG A NH2  1 
ATOM   2231  H H    . ARG A 1 141 ? 16.022  -9.044  75.657  1.00 105.62 ? 141 ARG A H    1 
ATOM   2232  H HA   . ARG A 1 141 ? 13.976  -9.101  73.888  1.00 107.64 ? 141 ARG A HA   1 
ATOM   2233  H HB2  . ARG A 1 141 ? 13.646  -8.721  76.656  1.00 110.17 ? 141 ARG A HB2  1 
ATOM   2234  H HB3  . ARG A 1 141 ? 12.561  -9.262  75.630  1.00 110.17 ? 141 ARG A HB3  1 
ATOM   2235  H HG2  . ARG A 1 141 ? 14.018  -11.214 75.430  1.00 112.54 ? 141 ARG A HG2  1 
ATOM   2236  H HG3  . ARG A 1 141 ? 14.670  -10.699 76.784  1.00 112.54 ? 141 ARG A HG3  1 
ATOM   2237  H HD2  . ARG A 1 141 ? 13.169  -11.930 77.756  1.00 109.32 ? 141 ARG A HD2  1 
ATOM   2238  H HD3  . ARG A 1 141 ? 12.159  -10.754 77.408  1.00 109.32 ? 141 ARG A HD3  1 
ATOM   2239  H HE   . ARG A 1 141 ? 11.577  -11.980 75.527  1.00 111.85 ? 141 ARG A HE   1 
ATOM   2240  H HH11 . ARG A 1 141 ? 12.958  -13.789 77.948  1.00 109.89 ? 141 ARG A HH11 1 
ATOM   2241  H HH12 . ARG A 1 141 ? 12.425  -15.096 77.472  1.00 109.89 ? 141 ARG A HH12 1 
ATOM   2242  H HH21 . ARG A 1 141 ? 10.815  -13.966 74.834  1.00 121.59 ? 141 ARG A HH21 1 
ATOM   2243  H HH22 . ARG A 1 141 ? 11.136  -15.204 75.597  1.00 121.59 ? 141 ARG A HH22 1 
ATOM   2244  N N    . PHE A 1 142 ? 13.574  -6.727  73.579  1.00 97.14  ? 142 PHE A N    1 
ATOM   2245  C CA   . PHE A 1 142 ? 13.284  -5.316  73.398  1.00 100.73 ? 142 PHE A CA   1 
ATOM   2246  C C    . PHE A 1 142 ? 11.775  -5.102  73.463  1.00 105.30 ? 142 PHE A C    1 
ATOM   2247  O O    . PHE A 1 142 ? 10.994  -6.039  73.652  1.00 103.95 ? 142 PHE A O    1 
ATOM   2248  C CB   . PHE A 1 142 ? 13.854  -4.816  72.072  1.00 94.93  ? 142 PHE A CB   1 
ATOM   2249  C CG   . PHE A 1 142 ? 15.354  -4.730  72.050  1.00 89.12  ? 142 PHE A CG   1 
ATOM   2250  C CD1  . PHE A 1 142 ? 16.007  -3.614  72.547  1.00 89.43  ? 142 PHE A CD1  1 
ATOM   2251  C CD2  . PHE A 1 142 ? 16.111  -5.764  71.525  1.00 88.32  ? 142 PHE A CD2  1 
ATOM   2252  C CE1  . PHE A 1 142 ? 17.389  -3.531  72.522  1.00 86.68  ? 142 PHE A CE1  1 
ATOM   2253  C CE2  . PHE A 1 142 ? 17.493  -5.688  71.497  1.00 85.78  ? 142 PHE A CE2  1 
ATOM   2254  C CZ   . PHE A 1 142 ? 18.132  -4.569  71.996  1.00 83.65  ? 142 PHE A CZ   1 
ATOM   2255  H H    . PHE A 1 142 ? 13.296  -7.215  72.928  1.00 116.57 ? 142 PHE A H    1 
ATOM   2256  H HA   . PHE A 1 142 ? 13.701  -4.809  74.113  1.00 120.88 ? 142 PHE A HA   1 
ATOM   2257  H HB2  . PHE A 1 142 ? 13.583  -5.425  71.368  1.00 113.92 ? 142 PHE A HB2  1 
ATOM   2258  H HB3  . PHE A 1 142 ? 13.504  -3.929  71.897  1.00 113.92 ? 142 PHE A HB3  1 
ATOM   2259  H HD1  . PHE A 1 142 ? 15.511  -2.912  72.901  1.00 107.32 ? 142 PHE A HD1  1 
ATOM   2260  H HD2  . PHE A 1 142 ? 15.686  -6.519  71.187  1.00 105.99 ? 142 PHE A HD2  1 
ATOM   2261  H HE1  . PHE A 1 142 ? 17.816  -2.777  72.859  1.00 104.01 ? 142 PHE A HE1  1 
ATOM   2262  H HE2  . PHE A 1 142 ? 17.991  -6.389  71.143  1.00 102.94 ? 142 PHE A HE2  1 
ATOM   2263  H HZ   . PHE A 1 142 ? 19.061  -4.514  71.977  1.00 100.38 ? 142 PHE A HZ   1 
ATOM   2264  N N    . SER A 1 143 ? 11.367  -3.847  73.305  1.00 112.52 ? 143 SER A N    1 
ATOM   2265  C CA   . SER A 1 143 ? 9.951   -3.497  73.229  1.00 113.42 ? 143 SER A CA   1 
ATOM   2266  C C    . SER A 1 143 ? 9.497   -3.696  71.789  1.00 118.71 ? 143 SER A C    1 
ATOM   2267  O O    . SER A 1 143 ? 9.758   -2.861  70.921  1.00 116.38 ? 143 SER A O    1 
ATOM   2268  C CB   . SER A 1 143 ? 9.728   -2.065  73.697  1.00 119.34 ? 143 SER A CB   1 
ATOM   2269  O OG   . SER A 1 143 ? 10.312  -1.851  74.971  1.00 119.70 ? 143 SER A OG   1 
ATOM   2270  H H    . SER A 1 143 ? 11.896  -3.173  73.238  1.00 135.02 ? 143 SER A H    1 
ATOM   2271  H HA   . SER A 1 143 ? 9.433   -4.084  73.803  1.00 136.11 ? 143 SER A HA   1 
ATOM   2272  H HB2  . SER A 1 143 ? 10.134  -1.458  73.059  1.00 143.21 ? 143 SER A HB2  1 
ATOM   2273  H HB3  . SER A 1 143 ? 8.775   -1.897  73.755  1.00 143.21 ? 143 SER A HB3  1 
ATOM   2274  H HG   . SER A 1 143 ? 10.199  -1.053  75.209  1.00 143.65 ? 143 SER A HG   1 
ATOM   2275  N N    . GLY A 1 144 ? 8.832   -4.820  71.528  1.00 119.30 ? 144 GLY A N    1 
ATOM   2276  C CA   . GLY A 1 144 ? 8.309   -5.096  70.207  1.00 117.27 ? 144 GLY A CA   1 
ATOM   2277  C C    . GLY A 1 144 ? 8.872   -6.344  69.561  1.00 115.94 ? 144 GLY A C    1 
ATOM   2278  O O    . GLY A 1 144 ? 8.131   -7.125  68.957  1.00 117.93 ? 144 GLY A O    1 
ATOM   2279  H H    . GLY A 1 144 ? 8.674   -5.437  72.105  1.00 143.15 ? 144 GLY A H    1 
ATOM   2280  H HA2  . GLY A 1 144 ? 7.346   -5.200  70.267  1.00 140.73 ? 144 GLY A HA2  1 
ATOM   2281  H HA3  . GLY A 1 144 ? 8.509   -4.344  69.627  1.00 140.73 ? 144 GLY A HA3  1 
ATOM   2282  N N    . ILE A 1 145 ? 10.180  -6.551  69.684  1.00 112.17 ? 145 ILE A N    1 
ATOM   2283  C CA   . ILE A 1 145 ? 10.865  -7.651  69.017  1.00 114.85 ? 145 ILE A CA   1 
ATOM   2284  C C    . ILE A 1 145 ? 11.873  -8.263  69.980  1.00 114.93 ? 145 ILE A C    1 
ATOM   2285  O O    . ILE A 1 145 ? 12.488  -7.559  70.787  1.00 113.80 ? 145 ILE A O    1 
ATOM   2286  C CB   . ILE A 1 145 ? 11.556  -7.173  67.716  1.00 115.03 ? 145 ILE A CB   1 
ATOM   2287  C CG1  . ILE A 1 145 ? 12.345  -8.316  67.081  1.00 111.00 ? 145 ILE A CG1  1 
ATOM   2288  C CG2  . ILE A 1 145 ? 12.432  -5.955  68.009  1.00 111.97 ? 145 ILE A CG2  1 
ATOM   2289  C CD1  . ILE A 1 145 ? 13.185  -7.893  65.897  1.00 110.46 ? 145 ILE A CD1  1 
ATOM   2290  H H    . ILE A 1 145 ? 10.701  -6.058  70.158  1.00 134.60 ? 145 ILE A H    1 
ATOM   2291  H HA   . ILE A 1 145 ? 10.221  -8.340  68.788  1.00 137.82 ? 145 ILE A HA   1 
ATOM   2292  H HB   . ILE A 1 145 ? 10.881  -6.902  67.074  1.00 138.04 ? 145 ILE A HB   1 
ATOM   2293  H HG12 . ILE A 1 145 ? 12.941  -8.690  67.748  1.00 133.20 ? 145 ILE A HG12 1 
ATOM   2294  H HG13 . ILE A 1 145 ? 11.721  -8.993  66.776  1.00 133.20 ? 145 ILE A HG13 1 
ATOM   2295  H HG21 . ILE A 1 145 ? 12.636  -5.504  67.174  1.00 134.37 ? 145 ILE A HG21 1 
ATOM   2296  H HG22 . ILE A 1 145 ? 11.951  -5.355  68.600  1.00 134.37 ? 145 ILE A HG22 1 
ATOM   2297  H HG23 . ILE A 1 145 ? 13.252  -6.251  68.433  1.00 134.37 ? 145 ILE A HG23 1 
ATOM   2298  H HD11 . ILE A 1 145 ? 13.794  -8.613  65.669  1.00 132.55 ? 145 ILE A HD11 1 
ATOM   2299  H HD12 . ILE A 1 145 ? 12.600  -7.705  65.146  1.00 132.55 ? 145 ILE A HD12 1 
ATOM   2300  H HD13 . ILE A 1 145 ? 13.687  -7.098  66.133  1.00 132.55 ? 145 ILE A HD13 1 
ATOM   2301  N N    . ASN A 1 146 ? 12.041  -9.581  69.890  1.00 105.64 ? 146 ASN A N    1 
ATOM   2302  C CA   . ASN A 1 146 ? 13.008  -10.322 70.685  1.00 101.44 ? 146 ASN A CA   1 
ATOM   2303  C C    . ASN A 1 146 ? 14.109  -10.837 69.768  1.00 97.05  ? 146 ASN A C    1 
ATOM   2304  O O    . ASN A 1 146 ? 13.847  -11.659 68.883  1.00 97.89  ? 146 ASN A O    1 
ATOM   2305  C CB   . ASN A 1 146 ? 12.336  -11.487 71.423  1.00 102.30 ? 146 ASN A CB   1 
ATOM   2306  C CG   . ASN A 1 146 ? 11.229  -11.025 72.363  1.00 101.07 ? 146 ASN A CG   1 
ATOM   2307  O OD1  . ASN A 1 146 ? 11.386  -10.047 73.096  1.00 96.87  ? 146 ASN A OD1  1 
ATOM   2308  N ND2  . ASN A 1 146 ? 10.102  -11.730 72.343  1.00 105.20 ? 146 ASN A ND2  1 
ATOM   2309  H H    . ASN A 1 146 ? 11.589  -10.081 69.356  1.00 126.76 ? 146 ASN A H    1 
ATOM   2310  H HA   . ASN A 1 146 ? 13.405  -9.730  71.342  1.00 121.73 ? 146 ASN A HA   1 
ATOM   2311  H HB2  . ASN A 1 146 ? 11.945  -12.091 70.772  1.00 122.76 ? 146 ASN A HB2  1 
ATOM   2312  H HB3  . ASN A 1 146 ? 13.002  -11.955 71.950  1.00 122.76 ? 146 ASN A HB3  1 
ATOM   2313  H HD21 . ASN A 1 146 ? 9.447   -11.510 72.855  1.00 126.24 ? 146 ASN A HD21 1 
ATOM   2314  H HD22 . ASN A 1 146 ? 10.028  -12.407 71.818  1.00 126.24 ? 146 ASN A HD22 1 
ATOM   2315  N N    . HIS A 1 147 ? 15.327  -10.345 69.972  1.00 91.80  ? 147 HIS A N    1 
ATOM   2316  C CA   . HIS A 1 147 ? 16.479  -10.780 69.201  1.00 87.34  ? 147 HIS A CA   1 
ATOM   2317  C C    . HIS A 1 147 ? 17.135  -11.992 69.849  1.00 88.50  ? 147 HIS A C    1 
ATOM   2318  O O    . HIS A 1 147 ? 17.299  -12.045 71.069  1.00 89.28  ? 147 HIS A O    1 
ATOM   2319  C CB   . HIS A 1 147 ? 17.506  -9.656  69.096  1.00 88.04  ? 147 HIS A CB   1 
ATOM   2320  C CG   . HIS A 1 147 ? 17.137  -8.579  68.125  1.00 89.94  ? 147 HIS A CG   1 
ATOM   2321  N ND1  . HIS A 1 147 ? 16.361  -8.809  67.010  1.00 87.51  ? 147 HIS A ND1  1 
ATOM   2322  C CD2  . HIS A 1 147 ? 17.447  -7.261  68.103  1.00 87.15  ? 147 HIS A CD2  1 
ATOM   2323  C CE1  . HIS A 1 147 ? 16.216  -7.680  66.341  1.00 88.21  ? 147 HIS A CE1  1 
ATOM   2324  N NE2  . HIS A 1 147 ? 16.860  -6.725  66.986  1.00 87.58  ? 147 HIS A NE2  1 
ATOM   2325  H H    . HIS A 1 147 ? 15.512  -9.747  70.562  1.00 110.15 ? 147 HIS A H    1 
ATOM   2326  H HA   . HIS A 1 147 ? 16.185  -11.028 68.310  1.00 104.81 ? 147 HIS A HA   1 
ATOM   2327  H HB2  . HIS A 1 147 ? 17.607  -9.245  69.968  1.00 105.65 ? 147 HIS A HB2  1 
ATOM   2328  H HB3  . HIS A 1 147 ? 18.352  -10.034 68.808  1.00 105.65 ? 147 HIS A HB3  1 
ATOM   2329  H HD1  . HIS A 1 147 ? 16.025  -9.568  66.784  1.00 105.01 ? 147 HIS A HD1  1 
ATOM   2330  H HD2  . HIS A 1 147 ? 17.962  -6.805  68.729  1.00 104.58 ? 147 HIS A HD2  1 
ATOM   2331  H HE1  . HIS A 1 147 ? 15.740  -7.575  65.550  1.00 105.85 ? 147 HIS A HE1  1 
ATOM   2332  N N    . PHE A 1 148 ? 17.519  -12.959 69.021  1.00 90.27  ? 148 PHE A N    1 
ATOM   2333  C CA   . PHE A 1 148 ? 18.283  -14.120 69.456  1.00 89.14  ? 148 PHE A CA   1 
ATOM   2334  C C    . PHE A 1 148 ? 19.658  -14.085 68.803  1.00 87.79  ? 148 PHE A C    1 
ATOM   2335  O O    . PHE A 1 148 ? 19.777  -13.822 67.602  1.00 87.08  ? 148 PHE A O    1 
ATOM   2336  C CB   . PHE A 1 148 ? 17.570  -15.423 69.096  1.00 89.24  ? 148 PHE A CB   1 
ATOM   2337  C CG   . PHE A 1 148 ? 16.372  -15.717 69.952  1.00 92.53  ? 148 PHE A CG   1 
ATOM   2338  C CD1  . PHE A 1 148 ? 15.194  -15.006 69.786  1.00 93.54  ? 148 PHE A CD1  1 
ATOM   2339  C CD2  . PHE A 1 148 ? 16.421  -16.706 70.922  1.00 93.22  ? 148 PHE A CD2  1 
ATOM   2340  C CE1  . PHE A 1 148 ? 14.090  -15.276 70.570  1.00 95.42  ? 148 PHE A CE1  1 
ATOM   2341  C CE2  . PHE A 1 148 ? 15.320  -16.980 71.707  1.00 91.37  ? 148 PHE A CE2  1 
ATOM   2342  C CZ   . PHE A 1 148 ? 14.153  -16.264 71.532  1.00 94.95  ? 148 PHE A CZ   1 
ATOM   2343  H H    . PHE A 1 148 ? 17.342  -12.964 68.180  1.00 108.33 ? 148 PHE A H    1 
ATOM   2344  H HA   . PHE A 1 148 ? 18.392  -14.098 70.420  1.00 106.97 ? 148 PHE A HA   1 
ATOM   2345  H HB2  . PHE A 1 148 ? 17.269  -15.369 68.175  1.00 107.09 ? 148 PHE A HB2  1 
ATOM   2346  H HB3  . PHE A 1 148 ? 18.194  -16.159 69.199  1.00 107.09 ? 148 PHE A HB3  1 
ATOM   2347  H HD1  . PHE A 1 148 ? 15.147  -14.339 69.139  1.00 112.25 ? 148 PHE A HD1  1 
ATOM   2348  H HD2  . PHE A 1 148 ? 17.206  -17.190 71.045  1.00 111.87 ? 148 PHE A HD2  1 
ATOM   2349  H HE1  . PHE A 1 148 ? 13.304  -14.792 70.450  1.00 114.50 ? 148 PHE A HE1  1 
ATOM   2350  H HE2  . PHE A 1 148 ? 15.364  -17.647 72.354  1.00 109.64 ? 148 PHE A HE2  1 
ATOM   2351  H HZ   . PHE A 1 148 ? 13.410  -16.447 72.061  1.00 113.94 ? 148 PHE A HZ   1 
ATOM   2352  N N    . ILE A 1 149 ? 20.692  -14.356 69.593  1.00 88.00  ? 149 ILE A N    1 
ATOM   2353  C CA   . ILE A 1 149 ? 22.073  -14.336 69.122  1.00 86.41  ? 149 ILE A CA   1 
ATOM   2354  C C    . ILE A 1 149 ? 22.548  -15.780 69.025  1.00 85.67  ? 149 ILE A C    1 
ATOM   2355  O O    . ILE A 1 149 ? 22.776  -16.437 70.048  1.00 92.69  ? 149 ILE A O    1 
ATOM   2356  C CB   . ILE A 1 149 ? 22.988  -13.522 70.047  1.00 85.29  ? 149 ILE A CB   1 
ATOM   2357  C CG1  . ILE A 1 149 ? 22.315  -12.214 70.464  1.00 88.04  ? 149 ILE A CG1  1 
ATOM   2358  C CG2  . ILE A 1 149 ? 24.325  -13.264 69.363  1.00 85.59  ? 149 ILE A CG2  1 
ATOM   2359  C CD1  . ILE A 1 149 ? 22.269  -11.158 69.386  1.00 85.88  ? 149 ILE A CD1  1 
ATOM   2360  H H    . ILE A 1 149 ? 20.617  -14.559 70.425  1.00 105.61 ? 149 ILE A H    1 
ATOM   2361  H HA   . ILE A 1 149 ? 22.096  -13.940 68.237  1.00 103.70 ? 149 ILE A HA   1 
ATOM   2362  H HB   . ILE A 1 149 ? 23.150  -14.036 70.853  1.00 102.35 ? 149 ILE A HB   1 
ATOM   2363  H HG12 . ILE A 1 149 ? 21.401  -12.407 70.724  1.00 105.65 ? 149 ILE A HG12 1 
ATOM   2364  H HG13 . ILE A 1 149 ? 22.803  -11.843 71.216  1.00 105.65 ? 149 ILE A HG13 1 
ATOM   2365  H HG21 . ILE A 1 149 ? 24.808  -12.585 69.861  1.00 102.71 ? 149 ILE A HG21 1 
ATOM   2366  H HG22 . ILE A 1 149 ? 24.835  -14.088 69.347  1.00 102.71 ? 149 ILE A HG22 1 
ATOM   2367  H HG23 . ILE A 1 149 ? 24.163  -12.957 68.458  1.00 102.71 ? 149 ILE A HG23 1 
ATOM   2368  H HD11 . ILE A 1 149 ? 21.680  -10.442 69.671  1.00 103.05 ? 149 ILE A HD11 1 
ATOM   2369  H HD12 . ILE A 1 149 ? 23.164  -10.813 69.244  1.00 103.05 ? 149 ILE A HD12 1 
ATOM   2370  H HD13 . ILE A 1 149 ? 21.934  -11.557 68.568  1.00 103.05 ? 149 ILE A HD13 1 
ATOM   2371  N N    . PHE A 1 150 ? 22.700  -16.279 67.801  1.00 85.83  ? 150 PHE A N    1 
ATOM   2372  C CA   . PHE A 1 150 ? 23.252  -17.607 67.558  1.00 85.05  ? 150 PHE A CA   1 
ATOM   2373  C C    . PHE A 1 150 ? 24.676  -17.428 67.044  1.00 82.81  ? 150 PHE A C    1 
ATOM   2374  O O    . PHE A 1 150 ? 24.883  -16.931 65.933  1.00 84.92  ? 150 PHE A O    1 
ATOM   2375  C CB   . PHE A 1 150 ? 22.397  -18.394 66.572  1.00 84.52  ? 150 PHE A CB   1 
ATOM   2376  C CG   . PHE A 1 150 ? 22.893  -19.793 66.332  1.00 90.22  ? 150 PHE A CG   1 
ATOM   2377  C CD1  . PHE A 1 150 ? 23.854  -20.035 65.364  1.00 85.32  ? 150 PHE A CD1  1 
ATOM   2378  C CD2  . PHE A 1 150 ? 22.412  -20.865 67.078  1.00 92.68  ? 150 PHE A CD2  1 
ATOM   2379  C CE1  . PHE A 1 150 ? 24.326  -21.312 65.135  1.00 85.02  ? 150 PHE A CE1  1 
ATOM   2380  C CE2  . PHE A 1 150 ? 22.880  -22.152 66.847  1.00 92.79  ? 150 PHE A CE2  1 
ATOM   2381  C CZ   . PHE A 1 150 ? 23.838  -22.372 65.872  1.00 93.03  ? 150 PHE A CZ   1 
ATOM   2382  H H    . PHE A 1 150 ? 22.486  -15.857 67.083  1.00 103.00 ? 150 PHE A H    1 
ATOM   2383  H HA   . PHE A 1 150 ? 23.277  -18.107 68.389  1.00 102.06 ? 150 PHE A HA   1 
ATOM   2384  H HB2  . PHE A 1 150 ? 21.494  -18.455 66.920  1.00 101.43 ? 150 PHE A HB2  1 
ATOM   2385  H HB3  . PHE A 1 150 ? 22.394  -17.930 65.720  1.00 101.43 ? 150 PHE A HB3  1 
ATOM   2386  H HD1  . PHE A 1 150 ? 24.186  -19.327 64.861  1.00 102.38 ? 150 PHE A HD1  1 
ATOM   2387  H HD2  . PHE A 1 150 ? 21.772  -20.719 67.736  1.00 111.21 ? 150 PHE A HD2  1 
ATOM   2388  H HE1  . PHE A 1 150 ? 24.974  -21.457 64.483  1.00 102.02 ? 150 PHE A HE1  1 
ATOM   2389  H HE2  . PHE A 1 150 ? 22.550  -22.864 67.346  1.00 111.35 ? 150 PHE A HE2  1 
ATOM   2390  H HZ   . PHE A 1 150 ? 24.153  -23.232 65.714  1.00 111.64 ? 150 PHE A HZ   1 
ATOM   2391  N N    . ASN A 1 151 ? 25.652  -17.821 67.858  1.00 85.64  ? 151 ASN A N    1 
ATOM   2392  C CA   . ASN A 1 151 ? 27.065  -17.710 67.512  1.00 85.27  ? 151 ASN A CA   1 
ATOM   2393  C C    . ASN A 1 151 ? 27.467  -18.955 66.732  1.00 88.60  ? 151 ASN A C    1 
ATOM   2394  O O    . ASN A 1 151 ? 27.486  -20.062 67.283  1.00 88.48  ? 151 ASN A O    1 
ATOM   2395  C CB   . ASN A 1 151 ? 27.911  -17.548 68.773  1.00 89.14  ? 151 ASN A CB   1 
ATOM   2396  C CG   . ASN A 1 151 ? 29.379  -17.311 68.466  1.00 89.60  ? 151 ASN A CG   1 
ATOM   2397  O OD1  . ASN A 1 151 ? 29.952  -17.946 67.580  1.00 92.36  ? 151 ASN A OD1  1 
ATOM   2398  N ND2  . ASN A 1 151 ? 29.996  -16.398 69.204  1.00 89.68  ? 151 ASN A ND2  1 
ATOM   2399  H H    . ASN A 1 151 ? 25.517  -18.164 68.635  1.00 102.77 ? 151 ASN A H    1 
ATOM   2400  H HA   . ASN A 1 151 ? 27.205  -16.933 66.949  1.00 102.32 ? 151 ASN A HA   1 
ATOM   2401  H HB2  . ASN A 1 151 ? 27.584  -16.788 69.278  1.00 106.97 ? 151 ASN A HB2  1 
ATOM   2402  H HB3  . ASN A 1 151 ? 27.843  -18.356 69.306  1.00 106.97 ? 151 ASN A HB3  1 
ATOM   2403  H HD21 . ASN A 1 151 ? 30.828  -16.227 69.070  1.00 107.62 ? 151 ASN A HD21 1 
ATOM   2404  H HD22 . ASN A 1 151 ? 29.564  -15.978 69.818  1.00 107.62 ? 151 ASN A HD22 1 
ATOM   2405  N N    . ILE A 1 152 ? 27.803  -18.770 65.452  1.00 90.02  ? 152 ILE A N    1 
ATOM   2406  C CA   . ILE A 1 152 ? 28.107  -19.900 64.578  1.00 88.15  ? 152 ILE A CA   1 
ATOM   2407  C C    . ILE A 1 152 ? 29.272  -20.708 65.134  1.00 91.25  ? 152 ILE A C    1 
ATOM   2408  O O    . ILE A 1 152 ? 29.189  -21.934 65.282  1.00 91.70  ? 152 ILE A O    1 
ATOM   2409  C CB   . ILE A 1 152 ? 28.407  -19.399 63.156  1.00 87.96  ? 152 ILE A CB   1 
ATOM   2410  C CG1  . ILE A 1 152 ? 27.133  -19.318 62.311  1.00 87.26  ? 152 ILE A CG1  1 
ATOM   2411  C CG2  . ILE A 1 152 ? 29.410  -20.317 62.458  1.00 90.39  ? 152 ILE A CG2  1 
ATOM   2412  C CD1  . ILE A 1 152 ? 25.957  -18.700 63.021  1.00 86.26  ? 152 ILE A CD1  1 
ATOM   2413  H H    . ILE A 1 152 ? 27.861  -18.002 65.069  1.00 108.02 ? 152 ILE A H    1 
ATOM   2414  H HA   . ILE A 1 152 ? 27.331  -20.481 64.545  1.00 105.78 ? 152 ILE A HA   1 
ATOM   2415  H HB   . ILE A 1 152 ? 28.784  -18.509 63.243  1.00 105.55 ? 152 ILE A HB   1 
ATOM   2416  H HG12 . ILE A 1 152 ? 27.316  -18.781 61.524  1.00 104.71 ? 152 ILE A HG12 1 
ATOM   2417  H HG13 . ILE A 1 152 ? 26.878  -20.216 62.047  1.00 104.71 ? 152 ILE A HG13 1 
ATOM   2418  H HG21 . ILE A 1 152 ? 29.425  -20.107 61.511  1.00 108.47 ? 152 ILE A HG21 1 
ATOM   2419  H HG22 . ILE A 1 152 ? 30.289  -20.175 62.842  1.00 108.47 ? 152 ILE A HG22 1 
ATOM   2420  H HG23 . ILE A 1 152 ? 29.137  -21.239 62.587  1.00 108.47 ? 152 ILE A HG23 1 
ATOM   2421  H HD11 . ILE A 1 152 ? 25.193  -18.694 62.423  1.00 103.51 ? 152 ILE A HD11 1 
ATOM   2422  H HD12 . ILE A 1 152 ? 25.754  -19.224 63.812  1.00 103.51 ? 152 ILE A HD12 1 
ATOM   2423  H HD13 . ILE A 1 152 ? 26.184  -17.792 63.276  1.00 103.51 ? 152 ILE A HD13 1 
ATOM   2424  N N    . LYS A 1 153 ? 30.386  -20.034 65.432  1.00 93.53  ? 153 LYS A N    1 
ATOM   2425  C CA   . LYS A 1 153 ? 31.590  -20.742 65.855  1.00 93.76  ? 153 LYS A CA   1 
ATOM   2426  C C    . LYS A 1 153 ? 31.391  -21.405 67.212  1.00 94.79  ? 153 LYS A C    1 
ATOM   2427  O O    . LYS A 1 153 ? 31.727  -22.581 67.393  1.00 95.10  ? 153 LYS A O    1 
ATOM   2428  C CB   . LYS A 1 153 ? 32.775  -19.776 65.894  1.00 96.11  ? 153 LYS A CB   1 
ATOM   2429  C CG   . LYS A 1 153 ? 33.719  -19.890 64.699  1.00 98.40  ? 153 LYS A CG   1 
ATOM   2430  C CD   . LYS A 1 153 ? 32.959  -19.897 63.378  1.00 97.90  ? 153 LYS A CD   1 
ATOM   2431  C CE   . LYS A 1 153 ? 33.831  -19.397 62.229  1.00 101.16 ? 153 LYS A CE   1 
ATOM   2432  N NZ   . LYS A 1 153 ? 33.774  -20.286 61.027  1.00 102.87 ? 153 LYS A NZ   1 
ATOM   2433  H H    . LYS A 1 153 ? 30.468  -19.178 65.397  1.00 112.24 ? 153 LYS A H    1 
ATOM   2434  H HA   . LYS A 1 153 ? 31.787  -21.437 65.209  1.00 112.51 ? 153 LYS A HA   1 
ATOM   2435  H HB2  . LYS A 1 153 ? 32.435  -18.868 65.914  1.00 115.34 ? 153 LYS A HB2  1 
ATOM   2436  H HB3  . LYS A 1 153 ? 33.293  -19.954 66.695  1.00 115.34 ? 153 LYS A HB3  1 
ATOM   2437  H HG2  . LYS A 1 153 ? 34.325  -19.133 64.696  1.00 118.07 ? 153 LYS A HG2  1 
ATOM   2438  H HG3  . LYS A 1 153 ? 34.221  -20.718 64.765  1.00 118.07 ? 153 LYS A HG3  1 
ATOM   2439  H HD2  . LYS A 1 153 ? 32.677  -20.803 63.175  1.00 117.48 ? 153 LYS A HD2  1 
ATOM   2440  H HD3  . LYS A 1 153 ? 32.185  -19.317 63.450  1.00 117.48 ? 153 LYS A HD3  1 
ATOM   2441  H HE2  . LYS A 1 153 ? 33.527  -18.515 61.963  1.00 121.40 ? 153 LYS A HE2  1 
ATOM   2442  H HE3  . LYS A 1 153 ? 34.753  -19.354 62.527  1.00 121.40 ? 153 LYS A HE3  1 
ATOM   2443  H HZ1  . LYS A 1 153 ? 34.287  -19.956 60.380  1.00 123.44 ? 153 LYS A HZ1  1 
ATOM   2444  H HZ2  . LYS A 1 153 ? 34.064  -21.101 61.238  1.00 123.44 ? 153 LYS A HZ2  1 
ATOM   2445  H HZ3  . LYS A 1 153 ? 32.937  -20.345 60.731  1.00 123.44 ? 153 LYS A HZ3  1 
ATOM   2446  N N    . GLU A 1 154 ? 30.840  -20.668 68.179  1.00 95.71  ? 154 GLU A N    1 
ATOM   2447  C CA   . GLU A 1 154 ? 30.680  -21.196 69.529  1.00 92.98  ? 154 GLU A CA   1 
ATOM   2448  C C    . GLU A 1 154 ? 29.709  -22.368 69.598  1.00 94.56  ? 154 GLU A C    1 
ATOM   2449  O O    . GLU A 1 154 ? 29.613  -23.002 70.655  1.00 94.98  ? 154 GLU A O    1 
ATOM   2450  C CB   . GLU A 1 154 ? 30.205  -20.090 70.476  1.00 87.45  ? 154 GLU A CB   1 
ATOM   2451  C CG   . GLU A 1 154 ? 31.313  -19.211 71.046  1.00 90.90  ? 154 GLU A CG   1 
ATOM   2452  C CD   . GLU A 1 154 ? 30.898  -18.500 72.330  1.00 98.81  ? 154 GLU A CD   1 
ATOM   2453  O OE1  . GLU A 1 154 ? 29.686  -18.244 72.512  1.00 98.66  ? 154 GLU A OE1  1 
ATOM   2454  O OE2  . GLU A 1 154 ? 31.782  -18.195 73.162  1.00 100.85 ? 154 GLU A OE2  1 
ATOM   2455  H H    . GLU A 1 154 ? 30.553  -19.863 68.077  1.00 114.85 ? 154 GLU A H    1 
ATOM   2456  H HA   . GLU A 1 154 ? 31.546  -21.507 69.836  1.00 111.57 ? 154 GLU A HA   1 
ATOM   2457  H HB2  . GLU A 1 154 ? 29.596  -19.511 69.991  1.00 104.94 ? 154 GLU A HB2  1 
ATOM   2458  H HB3  . GLU A 1 154 ? 29.746  -20.502 71.224  1.00 104.94 ? 154 GLU A HB3  1 
ATOM   2459  H HG2  . GLU A 1 154 ? 32.084  -19.765 71.245  1.00 109.08 ? 154 GLU A HG2  1 
ATOM   2460  H HG3  . GLU A 1 154 ? 31.550  -18.536 70.392  1.00 109.08 ? 154 GLU A HG3  1 
ATOM   2461  N N    . ASN A 1 155 ? 28.989  -22.665 68.521  1.00 94.35  ? 155 ASN A N    1 
ATOM   2462  C CA   . ASN A 1 155 ? 28.036  -23.763 68.490  1.00 95.74  ? 155 ASN A CA   1 
ATOM   2463  C C    . ASN A 1 155 ? 28.506  -24.842 67.523  1.00 100.01 ? 155 ASN A C    1 
ATOM   2464  O O    . ASN A 1 155 ? 29.451  -24.659 66.751  1.00 104.38 ? 155 ASN A O    1 
ATOM   2465  C CB   . ASN A 1 155 ? 26.639  -23.268 68.088  1.00 94.52  ? 155 ASN A CB   1 
ATOM   2466  C CG   . ASN A 1 155 ? 25.806  -22.845 69.280  1.00 96.27  ? 155 ASN A CG   1 
ATOM   2467  O OD1  . ASN A 1 155 ? 24.975  -23.606 69.782  1.00 96.27  ? 155 ASN A OD1  1 
ATOM   2468  N ND2  . ASN A 1 155 ? 26.028  -21.625 69.745  1.00 94.70  ? 155 ASN A ND2  1 
ATOM   2469  H H    . ASN A 1 155 ? 29.039  -22.232 67.779  1.00 113.22 ? 155 ASN A H    1 
ATOM   2470  H HA   . ASN A 1 155 ? 27.978  -24.150 69.378  1.00 114.89 ? 155 ASN A HA   1 
ATOM   2471  H HB2  . ASN A 1 155 ? 26.731  -22.504 67.499  1.00 113.42 ? 155 ASN A HB2  1 
ATOM   2472  H HB3  . ASN A 1 155 ? 26.169  -23.984 67.632  1.00 113.42 ? 155 ASN A HB3  1 
ATOM   2473  H HD21 . ASN A 1 155 ? 26.619  -21.123 69.372  1.00 113.64 ? 155 ASN A HD21 1 
ATOM   2474  H HD22 . ASN A 1 155 ? 25.582  -21.335 70.421  1.00 113.64 ? 155 ASN A HD22 1 
ATOM   2475  N N    . LYS A 1 156 ? 27.822  -25.981 67.572  1.00 103.60 ? 156 LYS A N    1 
ATOM   2476  C CA   . LYS A 1 156 ? 28.128  -27.083 66.678  1.00 107.50 ? 156 LYS A CA   1 
ATOM   2477  C C    . LYS A 1 156 ? 27.524  -26.838 65.297  1.00 108.44 ? 156 LYS A C    1 
ATOM   2478  O O    . LYS A 1 156 ? 26.605  -26.033 65.124  1.00 105.00 ? 156 LYS A O    1 
ATOM   2479  C CB   . LYS A 1 156 ? 27.603  -28.398 67.254  1.00 108.33 ? 156 LYS A CB   1 
ATOM   2480  C CG   . LYS A 1 156 ? 26.086  -28.498 67.294  1.00 108.73 ? 156 LYS A CG   1 
ATOM   2481  C CD   . LYS A 1 156 ? 25.633  -29.821 67.897  1.00 110.79 ? 156 LYS A CD   1 
ATOM   2482  C CE   . LYS A 1 156 ? 25.394  -30.874 66.825  1.00 111.22 ? 156 LYS A CE   1 
ATOM   2483  N NZ   . LYS A 1 156 ? 24.174  -31.688 67.102  1.00 112.70 ? 156 LYS A NZ   1 
ATOM   2484  H H    . LYS A 1 156 ? 27.174  -26.137 68.116  1.00 124.33 ? 156 LYS A H    1 
ATOM   2485  H HA   . LYS A 1 156 ? 29.090  -27.160 66.577  1.00 129.01 ? 156 LYS A HA   1 
ATOM   2486  H HB2  . LYS A 1 156 ? 27.932  -29.129 66.708  1.00 130.00 ? 156 LYS A HB2  1 
ATOM   2487  H HB3  . LYS A 1 156 ? 27.929  -28.490 68.163  1.00 130.00 ? 156 LYS A HB3  1 
ATOM   2488  H HG2  . LYS A 1 156 ? 25.730  -27.777 67.837  1.00 130.48 ? 156 LYS A HG2  1 
ATOM   2489  H HG3  . LYS A 1 156 ? 25.736  -28.437 66.391  1.00 130.48 ? 156 LYS A HG3  1 
ATOM   2490  H HD2  . LYS A 1 156 ? 26.318  -30.150 68.500  1.00 132.94 ? 156 LYS A HD2  1 
ATOM   2491  H HD3  . LYS A 1 156 ? 24.803  -29.685 68.380  1.00 132.94 ? 156 LYS A HD3  1 
ATOM   2492  H HE2  . LYS A 1 156 ? 25.278  -30.436 65.967  1.00 133.47 ? 156 LYS A HE2  1 
ATOM   2493  H HE3  . LYS A 1 156 ? 26.156  -31.474 66.790  1.00 133.47 ? 156 LYS A HE3  1 
ATOM   2494  H HZ1  . LYS A 1 156 ? 23.467  -31.155 67.187  1.00 135.25 ? 156 LYS A HZ1  1 
ATOM   2495  H HZ2  . LYS A 1 156 ? 24.029  -32.256 66.432  1.00 135.25 ? 156 LYS A HZ2  1 
ATOM   2496  H HZ3  . LYS A 1 156 ? 24.281  -32.150 67.855  1.00 135.25 ? 156 LYS A HZ3  1 
ATOM   2497  N N    . GLU A 1 157 ? 28.060  -27.553 64.307  1.00 117.07 ? 157 GLU A N    1 
ATOM   2498  C CA   . GLU A 1 157 ? 27.564  -27.454 62.940  1.00 115.18 ? 157 GLU A CA   1 
ATOM   2499  C C    . GLU A 1 157 ? 26.056  -27.663 62.906  1.00 112.47 ? 157 GLU A C    1 
ATOM   2500  O O    . GLU A 1 157 ? 25.512  -28.517 63.610  1.00 113.74 ? 157 GLU A O    1 
ATOM   2501  C CB   . GLU A 1 157 ? 28.265  -28.490 62.051  1.00 120.49 ? 157 GLU A CB   1 
ATOM   2502  C CG   . GLU A 1 157 ? 27.575  -28.785 60.720  1.00 121.32 ? 157 GLU A CG   1 
ATOM   2503  C CD   . GLU A 1 157 ? 27.754  -27.672 59.704  1.00 127.75 ? 157 GLU A CD   1 
ATOM   2504  O OE1  . GLU A 1 157 ? 28.743  -26.918 59.821  1.00 130.69 ? 157 GLU A OE1  1 
ATOM   2505  O OE2  . GLU A 1 157 ? 26.908  -27.545 58.792  1.00 127.00 ? 157 GLU A OE2  1 
ATOM   2506  H H    . GLU A 1 157 ? 28.713  -28.104 64.403  1.00 140.49 ? 157 GLU A H    1 
ATOM   2507  H HA   . GLU A 1 157 ? 27.757  -26.572 62.586  1.00 138.21 ? 157 GLU A HA   1 
ATOM   2508  H HB2  . GLU A 1 157 ? 29.156  -28.166 61.850  1.00 144.58 ? 157 GLU A HB2  1 
ATOM   2509  H HB3  . GLU A 1 157 ? 28.318  -29.326 62.541  1.00 144.58 ? 157 GLU A HB3  1 
ATOM   2510  H HG2  . GLU A 1 157 ? 27.950  -29.597 60.344  1.00 145.59 ? 157 GLU A HG2  1 
ATOM   2511  H HG3  . GLU A 1 157 ? 26.625  -28.899 60.876  1.00 145.59 ? 157 GLU A HG3  1 
ATOM   2512  N N    . THR A 1 158 ? 25.385  -26.883 62.066  1.00 111.81 ? 158 THR A N    1 
ATOM   2513  C CA   . THR A 1 158 ? 23.945  -27.008 61.914  1.00 110.65 ? 158 THR A CA   1 
ATOM   2514  C C    . THR A 1 158 ? 23.488  -26.129 60.762  1.00 109.47 ? 158 THR A C    1 
ATOM   2515  O O    . THR A 1 158 ? 24.196  -25.213 60.333  1.00 109.52 ? 158 THR A O    1 
ATOM   2516  C CB   . THR A 1 158 ? 23.199  -26.614 63.193  1.00 109.24 ? 158 THR A CB   1 
ATOM   2517  O OG1  . THR A 1 158 ? 21.798  -26.509 62.908  1.00 107.09 ? 158 THR A OG1  1 
ATOM   2518  C CG2  . THR A 1 158 ? 23.713  -25.278 63.725  1.00 107.03 ? 158 THR A CG2  1 
ATOM   2519  H H    . THR A 1 158 ? 25.743  -26.275 61.573  1.00 134.16 ? 158 THR A H    1 
ATOM   2520  H HA   . THR A 1 158 ? 23.737  -27.931 61.700  1.00 132.77 ? 158 THR A HA   1 
ATOM   2521  H HB   . THR A 1 158 ? 23.343  -27.287 63.878  1.00 131.09 ? 158 THR A HB   1 
ATOM   2522  H HG1  . THR A 1 158 ? 21.354  -26.576 63.618  1.00 128.51 ? 158 THR A HG1  1 
ATOM   2523  H HG21 . THR A 1 158 ? 23.346  -25.109 64.607  1.00 128.44 ? 158 THR A HG21 1 
ATOM   2524  H HG22 . THR A 1 158 ? 24.681  -25.295 63.784  1.00 128.44 ? 158 THR A HG22 1 
ATOM   2525  H HG23 . THR A 1 158 ? 23.447  -24.560 63.130  1.00 128.44 ? 158 THR A HG23 1 
ATOM   2526  N N    . SER A 1 159 ? 22.291  -26.423 60.270  1.00 105.27 ? 159 SER A N    1 
ATOM   2527  C CA   . SER A 1 159 ? 21.647  -25.592 59.269  1.00 105.14 ? 159 SER A CA   1 
ATOM   2528  C C    . SER A 1 159 ? 20.869  -24.482 59.959  1.00 102.98 ? 159 SER A C    1 
ATOM   2529  O O    . SER A 1 159 ? 20.223  -24.710 60.991  1.00 103.94 ? 159 SER A O    1 
ATOM   2530  C CB   . SER A 1 159 ? 20.708  -26.420 58.394  1.00 107.02 ? 159 SER A CB   1 
ATOM   2531  O OG   . SER A 1 159 ? 19.379  -26.342 58.874  1.00 106.70 ? 159 SER A OG   1 
ATOM   2532  H H    . SER A 1 159 ? 21.828  -27.108 60.504  1.00 126.32 ? 159 SER A H    1 
ATOM   2533  H HA   . SER A 1 159 ? 22.318  -25.196 58.691  1.00 126.16 ? 159 SER A HA   1 
ATOM   2534  H HB2  . SER A 1 159 ? 20.737  -26.078 57.487  1.00 128.42 ? 159 SER A HB2  1 
ATOM   2535  H HB3  . SER A 1 159 ? 20.996  -27.346 58.409  1.00 128.42 ? 159 SER A HB3  1 
ATOM   2536  H HG   . SER A 1 159 ? 18.869  -26.795 58.383  1.00 128.04 ? 159 SER A HG   1 
ATOM   2537  N N    . PHE A 1 160 ? 20.960  -23.272 59.388  1.00 100.09 ? 160 PHE A N    1 
ATOM   2538  C CA   . PHE A 1 160 ? 20.153  -22.158 59.869  1.00 100.22 ? 160 PHE A CA   1 
ATOM   2539  C C    . PHE A 1 160 ? 18.721  -22.598 60.117  1.00 102.62 ? 160 PHE A C    1 
ATOM   2540  O O    . PHE A 1 160 ? 18.128  -22.303 61.158  1.00 103.24 ? 160 PHE A O    1 
ATOM   2541  C CB   . PHE A 1 160 ? 20.184  -21.023 58.839  1.00 101.59 ? 160 PHE A CB   1 
ATOM   2542  C CG   . PHE A 1 160 ? 21.420  -20.174 58.897  1.00 96.14  ? 160 PHE A CG   1 
ATOM   2543  C CD1  . PHE A 1 160 ? 22.602  -20.677 59.417  1.00 95.06  ? 160 PHE A CD1  1 
ATOM   2544  C CD2  . PHE A 1 160 ? 21.400  -18.872 58.433  1.00 93.42  ? 160 PHE A CD2  1 
ATOM   2545  C CE1  . PHE A 1 160 ? 23.738  -19.899 59.473  1.00 90.85  ? 160 PHE A CE1  1 
ATOM   2546  C CE2  . PHE A 1 160 ? 22.533  -18.088 58.488  1.00 95.03  ? 160 PHE A CE2  1 
ATOM   2547  C CZ   . PHE A 1 160 ? 23.704  -18.603 59.008  1.00 92.94  ? 160 PHE A CZ   1 
ATOM   2548  H H    . PHE A 1 160 ? 21.478  -23.078 58.729  1.00 120.10 ? 160 PHE A H    1 
ATOM   2549  H HA   . PHE A 1 160 ? 20.525  -21.828 60.702  1.00 120.26 ? 160 PHE A HA   1 
ATOM   2550  H HB2  . PHE A 1 160 ? 20.133  -21.409 57.950  1.00 121.90 ? 160 PHE A HB2  1 
ATOM   2551  H HB3  . PHE A 1 160 ? 19.421  -20.444 58.993  1.00 121.90 ? 160 PHE A HB3  1 
ATOM   2552  H HD1  . PHE A 1 160 ? 22.628  -21.552 59.732  1.00 114.08 ? 160 PHE A HD1  1 
ATOM   2553  H HD2  . PHE A 1 160 ? 20.614  -18.521 58.081  1.00 112.10 ? 160 PHE A HD2  1 
ATOM   2554  H HE1  . PHE A 1 160 ? 24.526  -20.248 59.823  1.00 109.03 ? 160 PHE A HE1  1 
ATOM   2555  H HE2  . PHE A 1 160 ? 22.509  -17.213 58.173  1.00 114.03 ? 160 PHE A HE2  1 
ATOM   2556  H HZ   . PHE A 1 160 ? 24.469  -18.074 59.045  1.00 111.53 ? 160 PHE A HZ   1 
ATOM   2557  N N    . GLU A 1 161 ? 18.152  -23.337 59.159  1.00 104.82 ? 161 GLU A N    1 
ATOM   2558  C CA   . GLU A 1 161 ? 16.735  -23.680 59.206  1.00 105.51 ? 161 GLU A CA   1 
ATOM   2559  C C    . GLU A 1 161 ? 16.393  -24.432 60.484  1.00 104.88 ? 161 GLU A C    1 
ATOM   2560  O O    . GLU A 1 161 ? 15.340  -24.197 61.088  1.00 106.90 ? 161 GLU A O    1 
ATOM   2561  C CB   . GLU A 1 161 ? 16.360  -24.514 57.975  1.00 104.45 ? 161 GLU A CB   1 
ATOM   2562  C CG   . GLU A 1 161 ? 16.669  -23.871 56.614  1.00 107.04 ? 161 GLU A CG   1 
ATOM   2563  C CD   . GLU A 1 161 ? 18.160  -23.768 56.318  1.00 106.19 ? 161 GLU A CD   1 
ATOM   2564  O OE1  . GLU A 1 161 ? 18.955  -24.361 57.088  1.00 105.46 ? 161 GLU A OE1  1 
ATOM   2565  O OE2  . GLU A 1 161 ? 18.538  -23.078 55.351  1.00 98.70  ? 161 GLU A OE2  1 
ATOM   2566  H H    . GLU A 1 161 ? 18.566  -23.649 58.473  1.00 125.78 ? 161 GLU A H    1 
ATOM   2567  H HA   . GLU A 1 161 ? 16.213  -22.862 59.190  1.00 126.61 ? 161 GLU A HA   1 
ATOM   2568  H HB2  . GLU A 1 161 ? 16.848  -25.352 58.015  1.00 125.34 ? 161 GLU A HB2  1 
ATOM   2569  H HB3  . GLU A 1 161 ? 15.406  -24.685 58.003  1.00 125.34 ? 161 GLU A HB3  1 
ATOM   2570  H HG2  . GLU A 1 161 ? 16.264  -24.406 55.914  1.00 128.45 ? 161 GLU A HG2  1 
ATOM   2571  H HG3  . GLU A 1 161 ? 16.301  -22.973 56.600  1.00 128.45 ? 161 GLU A HG3  1 
ATOM   2572  N N    . ASN A 1 162 ? 17.270  -25.342 60.911  1.00 102.55 ? 162 ASN A N    1 
ATOM   2573  C CA   . ASN A 1 162 ? 17.059  -26.044 62.172  1.00 105.54 ? 162 ASN A CA   1 
ATOM   2574  C C    . ASN A 1 162 ? 16.936  -25.065 63.332  1.00 105.33 ? 162 ASN A C    1 
ATOM   2575  O O    . ASN A 1 162 ? 16.159  -25.292 64.267  1.00 107.71 ? 162 ASN A O    1 
ATOM   2576  C CB   . ASN A 1 162 ? 18.208  -27.024 62.407  1.00 105.80 ? 162 ASN A CB   1 
ATOM   2577  C CG   . ASN A 1 162 ? 18.031  -27.845 63.665  1.00 106.34 ? 162 ASN A CG   1 
ATOM   2578  O OD1  . ASN A 1 162 ? 18.958  -27.982 64.461  1.00 106.79 ? 162 ASN A OD1  1 
ATOM   2579  N ND2  . ASN A 1 162 ? 16.842  -28.410 63.845  1.00 109.62 ? 162 ASN A ND2  1 
ATOM   2580  H H    . ASN A 1 162 ? 17.987  -25.568 60.493  1.00 123.07 ? 162 ASN A H    1 
ATOM   2581  H HA   . ASN A 1 162 ? 16.232  -26.550 62.125  1.00 126.66 ? 162 ASN A HA   1 
ATOM   2582  H HB2  . ASN A 1 162 ? 18.261  -27.635 61.656  1.00 126.96 ? 162 ASN A HB2  1 
ATOM   2583  H HB3  . ASN A 1 162 ? 19.037  -26.526 62.489  1.00 126.96 ? 162 ASN A HB3  1 
ATOM   2584  H HD21 . ASN A 1 162 ? 16.694  -28.886 64.545  1.00 131.54 ? 162 ASN A HD21 1 
ATOM   2585  H HD22 . ASN A 1 162 ? 16.221  -28.299 63.260  1.00 131.54 ? 162 ASN A HD22 1 
ATOM   2586  N N    . ILE A 1 163 ? 17.690  -23.964 63.285  1.00 106.14 ? 163 ILE A N    1 
ATOM   2587  C CA   . ILE A 1 163 ? 17.674  -23.004 64.381  1.00 104.89 ? 163 ILE A CA   1 
ATOM   2588  C C    . ILE A 1 163 ? 16.421  -22.139 64.320  1.00 106.73 ? 163 ILE A C    1 
ATOM   2589  O O    . ILE A 1 163 ? 15.776  -21.892 65.345  1.00 108.01 ? 163 ILE A O    1 
ATOM   2590  C CB   . ILE A 1 163 ? 18.945  -22.138 64.351  1.00 97.97  ? 163 ILE A CB   1 
ATOM   2591  C CG1  . ILE A 1 163 ? 20.149  -22.913 63.809  1.00 99.63  ? 163 ILE A CG1  1 
ATOM   2592  C CG2  . ILE A 1 163 ? 19.266  -21.619 65.741  1.00 99.04  ? 163 ILE A CG2  1 
ATOM   2593  C CD1  . ILE A 1 163 ? 20.449  -24.197 64.541  1.00 104.09 ? 163 ILE A CD1  1 
ATOM   2594  H H    . ILE A 1 163 ? 18.213  -23.754 62.636  1.00 127.37 ? 163 ILE A H    1 
ATOM   2595  H HA   . ILE A 1 163 ? 17.663  -23.497 65.216  1.00 125.86 ? 163 ILE A HA   1 
ATOM   2596  H HB   . ILE A 1 163 ? 18.767  -21.394 63.755  1.00 117.57 ? 163 ILE A HB   1 
ATOM   2597  H HG12 . ILE A 1 163 ? 19.979  -23.138 62.881  1.00 119.56 ? 163 ILE A HG12 1 
ATOM   2598  H HG13 . ILE A 1 163 ? 20.935  -22.348 63.875  1.00 119.56 ? 163 ILE A HG13 1 
ATOM   2599  H HG21 . ILE A 1 163 ? 20.067  -21.074 65.698  1.00 118.84 ? 163 ILE A HG21 1 
ATOM   2600  H HG22 . ILE A 1 163 ? 18.521  -21.087 66.060  1.00 118.84 ? 163 ILE A HG22 1 
ATOM   2601  H HG23 . ILE A 1 163 ? 19.412  -22.373 66.334  1.00 118.84 ? 163 ILE A HG23 1 
ATOM   2602  H HD11 . ILE A 1 163 ? 21.222  -24.619 64.135  1.00 124.91 ? 163 ILE A HD11 1 
ATOM   2603  H HD12 . ILE A 1 163 ? 20.634  -23.995 65.472  1.00 124.91 ? 163 ILE A HD12 1 
ATOM   2604  H HD13 . ILE A 1 163 ? 19.680  -24.785 64.477  1.00 124.91 ? 163 ILE A HD13 1 
ATOM   2605  N N    . ILE A 1 164 ? 16.062  -21.652 63.126  1.00 110.04 ? 164 ILE A N    1 
ATOM   2606  C CA   . ILE A 1 164 ? 14.847  -20.856 62.994  1.00 107.22 ? 164 ILE A CA   1 
ATOM   2607  C C    . ILE A 1 164 ? 13.653  -21.633 63.531  1.00 109.74 ? 164 ILE A C    1 
ATOM   2608  O O    . ILE A 1 164 ? 12.764  -21.070 64.181  1.00 109.04 ? 164 ILE A O    1 
ATOM   2609  C CB   . ILE A 1 164 ? 14.626  -20.436 61.529  1.00 112.68 ? 164 ILE A CB   1 
ATOM   2610  C CG1  . ILE A 1 164 ? 15.950  -20.065 60.856  1.00 110.39 ? 164 ILE A CG1  1 
ATOM   2611  C CG2  . ILE A 1 164 ? 13.647  -19.264 61.472  1.00 112.57 ? 164 ILE A CG2  1 
ATOM   2612  C CD1  . ILE A 1 164 ? 15.796  -19.503 59.451  1.00 105.40 ? 164 ILE A CD1  1 
ATOM   2613  H H    . ILE A 1 164 ? 16.499  -21.767 62.394  1.00 132.05 ? 164 ILE A H    1 
ATOM   2614  H HA   . ILE A 1 164 ? 14.952  -20.048 63.521  1.00 128.67 ? 164 ILE A HA   1 
ATOM   2615  H HB   . ILE A 1 164 ? 14.251  -21.190 61.047  1.00 135.21 ? 164 ILE A HB   1 
ATOM   2616  H HG12 . ILE A 1 164 ? 16.394  -19.393 61.395  1.00 132.47 ? 164 ILE A HG12 1 
ATOM   2617  H HG13 . ILE A 1 164 ? 16.502  -20.861 60.796  1.00 132.47 ? 164 ILE A HG13 1 
ATOM   2618  H HG21 . ILE A 1 164 ? 13.242  -19.233 60.591  1.00 135.08 ? 164 ILE A HG21 1 
ATOM   2619  H HG22 . ILE A 1 164 ? 12.962  -19.391 62.147  1.00 135.08 ? 164 ILE A HG22 1 
ATOM   2620  H HG23 . ILE A 1 164 ? 14.131  -18.440 61.643  1.00 135.08 ? 164 ILE A HG23 1 
ATOM   2621  H HD11 . ILE A 1 164 ? 16.334  -20.030 58.840  1.00 126.48 ? 164 ILE A HD11 1 
ATOM   2622  H HD12 . ILE A 1 164 ? 14.862  -19.549 59.194  1.00 126.48 ? 164 ILE A HD12 1 
ATOM   2623  H HD13 . ILE A 1 164 ? 16.095  -18.581 59.446  1.00 126.48 ? 164 ILE A HD13 1 
ATOM   2624  N N    . ASP A 1 165 ? 13.614  -22.940 63.263  1.00 112.88 ? 165 ASP A N    1 
ATOM   2625  C CA   . ASP A 1 165 ? 12.553  -23.777 63.808  1.00 114.68 ? 165 ASP A CA   1 
ATOM   2626  C C    . ASP A 1 165 ? 12.709  -23.946 65.313  1.00 113.15 ? 165 ASP A C    1 
ATOM   2627  O O    . ASP A 1 165 ? 11.728  -23.836 66.058  1.00 114.30 ? 165 ASP A O    1 
ATOM   2628  C CB   . ASP A 1 165 ? 12.553  -25.139 63.114  1.00 117.90 ? 165 ASP A CB   1 
ATOM   2629  C CG   . ASP A 1 165 ? 11.705  -25.152 61.858  1.00 117.43 ? 165 ASP A CG   1 
ATOM   2630  O OD1  . ASP A 1 165 ? 11.671  -24.118 61.159  1.00 117.35 ? 165 ASP A OD1  1 
ATOM   2631  O OD2  . ASP A 1 165 ? 11.073  -26.190 61.575  1.00 118.40 ? 165 ASP A OD2  1 
ATOM   2632  H H    . ASP A 1 165 ? 14.183  -23.359 62.773  1.00 135.46 ? 165 ASP A H    1 
ATOM   2633  H HA   . ASP A 1 165 ? 11.698  -23.352 63.638  1.00 137.61 ? 165 ASP A HA   1 
ATOM   2634  H HB2  . ASP A 1 165 ? 13.462  -25.369 62.865  1.00 141.47 ? 165 ASP A HB2  1 
ATOM   2635  H HB3  . ASP A 1 165 ? 12.198  -25.806 63.723  1.00 141.47 ? 165 ASP A HB3  1 
ATOM   2636  N N    . LEU A 1 166 ? 13.933  -24.210 65.780  1.00 111.03 ? 166 LEU A N    1 
ATOM   2637  C CA   . LEU A 1 166 ? 14.152  -24.414 67.209  1.00 110.25 ? 166 LEU A CA   1 
ATOM   2638  C C    . LEU A 1 166 ? 13.754  -23.177 68.004  1.00 109.75 ? 166 LEU A C    1 
ATOM   2639  O O    . LEU A 1 166 ? 13.078  -23.276 69.034  1.00 109.84 ? 166 LEU A O    1 
ATOM   2640  C CB   . LEU A 1 166 ? 15.615  -24.767 67.472  1.00 111.28 ? 166 LEU A CB   1 
ATOM   2641  C CG   . LEU A 1 166 ? 15.991  -26.247 67.394  1.00 113.54 ? 166 LEU A CG   1 
ATOM   2642  C CD1  . LEU A 1 166 ? 17.501  -26.410 67.550  1.00 112.83 ? 166 LEU A CD1  1 
ATOM   2643  C CD2  . LEU A 1 166 ? 15.257  -27.072 68.440  1.00 115.72 ? 166 LEU A CD2  1 
ATOM   2644  H H    . LEU A 1 166 ? 14.641  -24.274 65.296  1.00 133.23 ? 166 LEU A H    1 
ATOM   2645  H HA   . LEU A 1 166 ? 13.604  -25.159 67.503  1.00 132.30 ? 166 LEU A HA   1 
ATOM   2646  H HB2  . LEU A 1 166 ? 16.158  -24.301 66.818  1.00 133.54 ? 166 LEU A HB2  1 
ATOM   2647  H HB3  . LEU A 1 166 ? 15.840  -24.464 68.366  1.00 133.54 ? 166 LEU A HB3  1 
ATOM   2648  H HG   . LEU A 1 166 ? 15.725  -26.586 66.525  1.00 136.25 ? 166 LEU A HG   1 
ATOM   2649  H HD11 . LEU A 1 166 ? 17.723  -27.353 67.501  1.00 135.40 ? 166 LEU A HD11 1 
ATOM   2650  H HD12 . LEU A 1 166 ? 17.946  -25.928 66.837  1.00 135.40 ? 166 LEU A HD12 1 
ATOM   2651  H HD13 . LEU A 1 166 ? 17.770  -26.051 68.410  1.00 135.40 ? 166 LEU A HD13 1 
ATOM   2652  H HD21 . LEU A 1 166 ? 15.622  -27.971 68.446  1.00 138.87 ? 166 LEU A HD21 1 
ATOM   2653  H HD22 . LEU A 1 166 ? 15.379  -26.660 69.309  1.00 138.87 ? 166 LEU A HD22 1 
ATOM   2654  H HD23 . LEU A 1 166 ? 14.314  -27.099 68.216  1.00 138.87 ? 166 LEU A HD23 1 
ATOM   2655  N N    . VAL A 1 167 ? 14.179  -21.998 67.546  1.00 111.23 ? 167 VAL A N    1 
ATOM   2656  C CA   . VAL A 1 167 ? 13.751  -20.759 68.190  1.00 110.28 ? 167 VAL A CA   1 
ATOM   2657  C C    . VAL A 1 167 ? 12.230  -20.702 68.230  1.00 112.39 ? 167 VAL A C    1 
ATOM   2658  O O    . VAL A 1 167 ? 11.622  -20.640 69.303  1.00 114.54 ? 167 VAL A O    1 
ATOM   2659  C CB   . VAL A 1 167 ? 14.346  -19.539 67.467  1.00 104.25 ? 167 VAL A CB   1 
ATOM   2660  C CG1  . VAL A 1 167 ? 13.806  -18.251 68.062  1.00 101.99 ? 167 VAL A CG1  1 
ATOM   2661  C CG2  . VAL A 1 167 ? 15.865  -19.566 67.557  1.00 102.18 ? 167 VAL A CG2  1 
ATOM   2662  H H    . VAL A 1 167 ? 14.707  -21.891 66.876  1.00 133.48 ? 167 VAL A H    1 
ATOM   2663  H HA   . VAL A 1 167 ? 14.080  -20.747 69.102  1.00 132.33 ? 167 VAL A HA   1 
ATOM   2664  H HB   . VAL A 1 167 ? 14.090  -19.571 66.532  1.00 125.11 ? 167 VAL A HB   1 
ATOM   2665  H HG11 . VAL A 1 167 ? 14.370  -17.513 67.781  1.00 122.39 ? 167 VAL A HG11 1 
ATOM   2666  H HG12 . VAL A 1 167 ? 12.899  -18.113 67.747  1.00 122.39 ? 167 VAL A HG12 1 
ATOM   2667  H HG13 . VAL A 1 167 ? 13.813  -18.322 69.029  1.00 122.39 ? 167 VAL A HG13 1 
ATOM   2668  H HG21 . VAL A 1 167 ? 16.223  -18.799 67.083  1.00 122.62 ? 167 VAL A HG21 1 
ATOM   2669  H HG22 . VAL A 1 167 ? 16.126  -19.531 68.490  1.00 122.62 ? 167 VAL A HG22 1 
ATOM   2670  H HG23 . VAL A 1 167 ? 16.190  -20.386 67.153  1.00 122.62 ? 167 VAL A HG23 1 
ATOM   2671  N N    . LYS A 1 168 ? 11.595  -20.778 67.058  1.00 112.72 ? 168 LYS A N    1 
ATOM   2672  C CA   . LYS A 1 168 ? 10.140  -20.793 66.960  1.00 114.24 ? 168 LYS A CA   1 
ATOM   2673  C C    . LYS A 1 168 ? 9.517   -21.732 67.987  1.00 114.80 ? 168 LYS A C    1 
ATOM   2674  O O    . LYS A 1 168 ? 8.394   -21.499 68.447  1.00 114.69 ? 168 LYS A O    1 
ATOM   2675  C CB   . LYS A 1 168 ? 9.711   -21.205 65.548  1.00 109.65 ? 168 LYS A CB   1 
ATOM   2676  C CG   . LYS A 1 168 ? 9.648   -20.057 64.552  1.00 109.84 ? 168 LYS A CG   1 
ATOM   2677  C CD   . LYS A 1 168 ? 9.178   -20.538 63.181  1.00 113.66 ? 168 LYS A CD   1 
ATOM   2678  C CE   . LYS A 1 168 ? 8.451   -19.442 62.410  1.00 113.56 ? 168 LYS A CE   1 
ATOM   2679  N NZ   . LYS A 1 168 ? 7.481   -20.008 61.427  1.00 115.83 ? 168 LYS A NZ   1 
ATOM   2680  H H    . LYS A 1 168 ? 11.992  -20.823 66.296  1.00 135.26 ? 168 LYS A H    1 
ATOM   2681  H HA   . LYS A 1 168 ? 9.811   -19.899 67.141  1.00 137.09 ? 168 LYS A HA   1 
ATOM   2682  H HB2  . LYS A 1 168 ? 10.347  -21.854 65.208  1.00 131.58 ? 168 LYS A HB2  1 
ATOM   2683  H HB3  . LYS A 1 168 ? 8.827   -21.601 65.597  1.00 131.58 ? 168 LYS A HB3  1 
ATOM   2684  H HG2  . LYS A 1 168 ? 9.023   -19.388 64.872  1.00 131.81 ? 168 LYS A HG2  1 
ATOM   2685  H HG3  . LYS A 1 168 ? 10.530  -19.667 64.453  1.00 131.81 ? 168 LYS A HG3  1 
ATOM   2686  H HD2  . LYS A 1 168 ? 9.947   -20.816 62.659  1.00 136.39 ? 168 LYS A HD2  1 
ATOM   2687  H HD3  . LYS A 1 168 ? 8.567   -21.283 63.296  1.00 136.39 ? 168 LYS A HD3  1 
ATOM   2688  H HE2  . LYS A 1 168 ? 7.961   -18.883 63.034  1.00 136.27 ? 168 LYS A HE2  1 
ATOM   2689  H HE3  . LYS A 1 168 ? 9.099   -18.909 61.925  1.00 136.27 ? 168 LYS A HE3  1 
ATOM   2690  H HZ1  . LYS A 1 168 ? 7.074   -19.349 60.987  1.00 138.99 ? 168 LYS A HZ1  1 
ATOM   2691  H HZ2  . LYS A 1 168 ? 6.867   -20.494 61.851  1.00 138.99 ? 168 LYS A HZ2  1 
ATOM   2692  H HZ3  . LYS A 1 168 ? 7.907   -20.526 60.842  1.00 138.99 ? 168 LYS A HZ3  1 
ATOM   2693  N N    . LYS A 1 169 ? 10.237  -22.798 68.352  1.00 118.25 ? 169 LYS A N    1 
ATOM   2694  C CA   . LYS A 1 169 ? 9.753   -23.695 69.396  1.00 117.10 ? 169 LYS A CA   1 
ATOM   2695  C C    . LYS A 1 169 ? 9.909   -23.066 70.777  1.00 118.50 ? 169 LYS A C    1 
ATOM   2696  O O    . LYS A 1 169 ? 9.050   -23.248 71.647  1.00 120.98 ? 169 LYS A O    1 
ATOM   2697  C CB   . LYS A 1 169 ? 10.496  -25.029 69.334  1.00 118.70 ? 169 LYS A CB   1 
ATOM   2698  C CG   . LYS A 1 169 ? 9.668   -26.207 68.821  1.00 121.80 ? 169 LYS A CG   1 
ATOM   2699  C CD   . LYS A 1 169 ? 8.467   -26.530 69.715  1.00 124.49 ? 169 LYS A CD   1 
ATOM   2700  C CE   . LYS A 1 169 ? 8.868   -26.876 71.142  1.00 128.08 ? 169 LYS A CE   1 
ATOM   2701  N NZ   . LYS A 1 169 ? 7.683   -26.903 72.054  1.00 127.10 ? 169 LYS A NZ   1 
ATOM   2702  H H    . LYS A 1 169 ? 10.997  -23.019 68.014  1.00 141.90 ? 169 LYS A H    1 
ATOM   2703  H HA   . LYS A 1 169 ? 8.810   -23.868 69.244  1.00 140.51 ? 169 LYS A HA   1 
ATOM   2704  H HB2  . LYS A 1 169 ? 11.257  -24.929 68.741  1.00 142.44 ? 169 LYS A HB2  1 
ATOM   2705  H HB3  . LYS A 1 169 ? 10.799  -25.254 70.228  1.00 142.44 ? 169 LYS A HB3  1 
ATOM   2706  H HG2  . LYS A 1 169 ? 9.333   -25.995 67.936  1.00 146.15 ? 169 LYS A HG2  1 
ATOM   2707  H HG3  . LYS A 1 169 ? 10.232  -26.996 68.782  1.00 146.15 ? 169 LYS A HG3  1 
ATOM   2708  H HD2  . LYS A 1 169 ? 7.881   -25.758 69.748  1.00 149.38 ? 169 LYS A HD2  1 
ATOM   2709  H HD3  . LYS A 1 169 ? 7.993   -27.291 69.345  1.00 149.38 ? 169 LYS A HD3  1 
ATOM   2710  H HE2  . LYS A 1 169 ? 9.283   -27.752 71.155  1.00 153.69 ? 169 LYS A HE2  1 
ATOM   2711  H HE3  . LYS A 1 169 ? 9.491   -26.209 71.471  1.00 153.69 ? 169 LYS A HE3  1 
ATOM   2712  H HZ1  . LYS A 1 169 ? 7.941   -27.101 72.883  1.00 152.53 ? 169 LYS A HZ1  1 
ATOM   2713  H HZ2  . LYS A 1 169 ? 7.283   -26.108 72.058  1.00 152.53 ? 169 LYS A HZ2  1 
ATOM   2714  H HZ3  . LYS A 1 169 ? 7.101   -27.518 71.779  1.00 152.53 ? 169 LYS A HZ3  1 
ATOM   2715  N N    . TYR A 1 170 ? 11.001  -22.327 70.999  1.00 115.01 ? 170 TYR A N    1 
ATOM   2716  C CA   . TYR A 1 170 ? 11.215  -21.687 72.296  1.00 112.91 ? 170 TYR A CA   1 
ATOM   2717  C C    . TYR A 1 170 ? 10.091  -20.709 72.615  1.00 115.42 ? 170 TYR A C    1 
ATOM   2718  O O    . TYR A 1 170 ? 9.573   -20.694 73.738  1.00 120.43 ? 170 TYR A O    1 
ATOM   2719  C CB   . TYR A 1 170 ? 12.572  -20.977 72.307  1.00 109.43 ? 170 TYR A CB   1 
ATOM   2720  C CG   . TYR A 1 170 ? 12.978  -20.360 73.632  1.00 107.84 ? 170 TYR A CG   1 
ATOM   2721  C CD1  . TYR A 1 170 ? 12.397  -19.180 74.083  1.00 108.19 ? 170 TYR A CD1  1 
ATOM   2722  C CD2  . TYR A 1 170 ? 13.963  -20.945 74.421  1.00 105.15 ? 170 TYR A CD2  1 
ATOM   2723  C CE1  . TYR A 1 170 ? 12.772  -18.612 75.291  1.00 103.11 ? 170 TYR A CE1  1 
ATOM   2724  C CE2  . TYR A 1 170 ? 14.345  -20.381 75.626  1.00 97.82  ? 170 TYR A CE2  1 
ATOM   2725  C CZ   . TYR A 1 170 ? 13.747  -19.216 76.054  1.00 97.91  ? 170 TYR A CZ   1 
ATOM   2726  O OH   . TYR A 1 170 ? 14.124  -18.647 77.247  1.00 101.04 ? 170 TYR A OH   1 
ATOM   2727  H H    . TYR A 1 170 ? 11.623  -22.182 70.423  1.00 138.01 ? 170 TYR A H    1 
ATOM   2728  H HA   . TYR A 1 170 ? 11.226  -22.367 72.988  1.00 135.49 ? 170 TYR A HA   1 
ATOM   2729  H HB2  . TYR A 1 170 ? 13.256  -21.623 72.069  1.00 131.32 ? 170 TYR A HB2  1 
ATOM   2730  H HB3  . TYR A 1 170 ? 12.548  -20.263 71.652  1.00 131.32 ? 170 TYR A HB3  1 
ATOM   2731  H HD1  . TYR A 1 170 ? 11.745  -18.764 73.566  1.00 129.82 ? 170 TYR A HD1  1 
ATOM   2732  H HD2  . TYR A 1 170 ? 14.372  -21.730 74.134  1.00 126.19 ? 170 TYR A HD2  1 
ATOM   2733  H HE1  . TYR A 1 170 ? 12.368  -17.827 75.584  1.00 123.73 ? 170 TYR A HE1  1 
ATOM   2734  H HE2  . TYR A 1 170 ? 15.002  -20.787 76.144  1.00 117.38 ? 170 TYR A HE2  1 
ATOM   2735  H HH   . TYR A 1 170 ? 14.740  -19.098 77.599  1.00 121.24 ? 170 TYR A HH   1 
ATOM   2736  N N    . LEU A 1 171 ? 9.701   -19.884 71.643  1.00 115.10 ? 171 LEU A N    1 
ATOM   2737  C CA   . LEU A 1 171 ? 8.615   -18.935 71.828  1.00 120.98 ? 171 LEU A CA   1 
ATOM   2738  C C    . LEU A 1 171 ? 7.244   -19.557 71.568  1.00 124.50 ? 171 LEU A C    1 
ATOM   2739  O O    . LEU A 1 171 ? 6.282   -18.827 71.299  1.00 128.63 ? 171 LEU A O    1 
ATOM   2740  C CB   . LEU A 1 171 ? 8.809   -17.717 70.919  1.00 121.00 ? 171 LEU A CB   1 
ATOM   2741  C CG   . LEU A 1 171 ? 10.214  -17.143 70.766  1.00 116.84 ? 171 LEU A CG   1 
ATOM   2742  C CD1  . LEU A 1 171 ? 10.870  -17.708 69.513  1.00 112.50 ? 171 LEU A CD1  1 
ATOM   2743  C CD2  . LEU A 1 171 ? 10.201  -15.622 70.704  1.00 117.59 ? 171 LEU A CD2  1 
ATOM   2744  H H    . LEU A 1 171 ? 10.057  -19.858 70.861  1.00 138.12 ? 171 LEU A H    1 
ATOM   2745  H HA   . LEU A 1 171 ? 8.638   -18.628 72.748  1.00 145.17 ? 171 LEU A HA   1 
ATOM   2746  H HB2  . LEU A 1 171 ? 8.513   -17.966 70.030  1.00 145.20 ? 171 LEU A HB2  1 
ATOM   2747  H HB3  . LEU A 1 171 ? 8.253   -17.002 71.266  1.00 145.20 ? 171 LEU A HB3  1 
ATOM   2748  H HG   . LEU A 1 171 ? 10.734  -17.397 71.545  1.00 140.21 ? 171 LEU A HG   1 
ATOM   2749  H HD11 . LEU A 1 171 ? 11.764  -17.341 69.431  1.00 135.00 ? 171 LEU A HD11 1 
ATOM   2750  H HD12 . LEU A 1 171 ? 10.915  -18.674 69.588  1.00 135.00 ? 171 LEU A HD12 1 
ATOM   2751  H HD13 . LEU A 1 171 ? 10.339  -17.461 68.740  1.00 135.00 ? 171 LEU A HD13 1 
ATOM   2752  H HD21 . LEU A 1 171 ? 11.111  -15.302 70.605  1.00 141.11 ? 171 LEU A HD21 1 
ATOM   2753  H HD22 . LEU A 1 171 ? 9.667   -15.341 69.944  1.00 141.11 ? 171 LEU A HD22 1 
ATOM   2754  H HD23 . LEU A 1 171 ? 9.816   -15.276 71.524  1.00 141.11 ? 171 LEU A HD23 1 
ATOM   2755  N N    . SER A 1 172 ? 7.136   -20.886 71.631  1.00 122.68 ? 172 SER A N    1 
ATOM   2756  C CA   . SER A 1 172 ? 5.843   -21.531 71.420  1.00 126.90 ? 172 SER A CA   1 
ATOM   2757  C C    . SER A 1 172 ? 4.831   -21.072 72.465  1.00 132.81 ? 172 SER A C    1 
ATOM   2758  O O    . SER A 1 172 ? 3.707   -20.682 72.129  1.00 134.81 ? 172 SER A O    1 
ATOM   2759  C CB   . SER A 1 172 ? 6.004   -23.051 71.451  1.00 126.66 ? 172 SER A CB   1 
ATOM   2760  O OG   . SER A 1 172 ? 6.195   -23.522 72.772  1.00 128.17 ? 172 SER A OG   1 
ATOM   2761  H H    . SER A 1 172 ? 7.785   -21.427 71.791  1.00 147.22 ? 172 SER A H    1 
ATOM   2762  H HA   . SER A 1 172 ? 5.507   -21.284 70.544  1.00 152.29 ? 172 SER A HA   1 
ATOM   2763  H HB2  . SER A 1 172 ? 5.203   -23.459 71.085  1.00 151.99 ? 172 SER A HB2  1 
ATOM   2764  H HB3  . SER A 1 172 ? 6.775   -23.296 70.916  1.00 151.99 ? 172 SER A HB3  1 
ATOM   2765  H HG   . SER A 1 172 ? 6.290   -24.357 72.769  1.00 153.80 ? 172 SER A HG   1 
ATOM   2766  N N    . ASN A 1 173 ? 5.215   -21.108 73.736  1.00 133.90 ? 173 ASN A N    1 
ATOM   2767  C CA   . ASN A 1 173 ? 4.364   -20.640 74.833  1.00 134.95 ? 173 ASN A CA   1 
ATOM   2768  C C    . ASN A 1 173 ? 4.782   -19.248 75.294  1.00 135.55 ? 173 ASN A C    1 
ATOM   2769  O O    . ASN A 1 173 ? 4.926   -18.978 76.486  1.00 135.97 ? 173 ASN A O    1 
ATOM   2770  C CB   . ASN A 1 173 ? 4.403   -21.636 75.986  1.00 136.76 ? 173 ASN A CB   1 
ATOM   2771  C CG   . ASN A 1 173 ? 3.639   -22.913 75.680  1.00 139.56 ? 173 ASN A CG   1 
ATOM   2772  O OD1  . ASN A 1 173 ? 3.994   -23.659 74.766  1.00 138.33 ? 173 ASN A OD1  1 
ATOM   2773  N ND2  . ASN A 1 173 ? 2.581   -23.169 76.443  1.00 141.47 ? 173 ASN A ND2  1 
ATOM   2774  H H    . ASN A 1 173 ? 5.979   -21.404 73.997  1.00 160.67 ? 173 ASN A H    1 
ATOM   2775  H HA   . ASN A 1 173 ? 3.448   -20.588 74.518  1.00 161.94 ? 173 ASN A HA   1 
ATOM   2776  H HB2  . ASN A 1 173 ? 5.326   -21.874 76.167  1.00 164.11 ? 173 ASN A HB2  1 
ATOM   2777  H HB3  . ASN A 1 173 ? 4.005   -21.228 76.771  1.00 164.11 ? 173 ASN A HB3  1 
ATOM   2778  H HD21 . ASN A 1 173 ? 2.362   -22.623 77.071  1.00 169.76 ? 173 ASN A HD21 1 
ATOM   2779  H HD22 . ASN A 1 173 ? 2.116   -23.879 76.309  1.00 169.76 ? 173 ASN A HD22 1 
ATOM   2780  N N    . GLU A 1 174 ? 4.986   -18.346 74.338  1.00 134.22 ? 174 GLU A N    1 
ATOM   2781  C CA   . GLU A 1 174 ? 5.368   -16.968 74.634  1.00 134.73 ? 174 GLU A CA   1 
ATOM   2782  C C    . GLU A 1 174 ? 4.838   -16.093 73.509  1.00 134.38 ? 174 GLU A C    1 
ATOM   2783  O O    . GLU A 1 174 ? 5.155   -16.329 72.339  1.00 132.95 ? 174 GLU A O    1 
ATOM   2784  C CB   . GLU A 1 174 ? 6.888   -16.834 74.777  1.00 133.72 ? 174 GLU A CB   1 
ATOM   2785  C CG   . GLU A 1 174 ? 7.472   -15.496 74.341  1.00 134.95 ? 174 GLU A CG   1 
ATOM   2786  C CD   . GLU A 1 174 ? 6.937   -14.318 75.134  1.00 135.26 ? 174 GLU A CD   1 
ATOM   2787  O OE1  . GLU A 1 174 ? 6.057   -14.524 75.997  1.00 137.62 ? 174 GLU A OE1  1 
ATOM   2788  O OE2  . GLU A 1 174 ? 7.397   -13.181 74.887  1.00 132.02 ? 174 GLU A OE2  1 
ATOM   2789  H H    . GLU A 1 174 ? 4.908   -18.509 73.497  1.00 161.07 ? 174 GLU A H    1 
ATOM   2790  H HA   . GLU A 1 174 ? 4.968   -16.678 75.468  1.00 161.67 ? 174 GLU A HA   1 
ATOM   2791  H HB2  . GLU A 1 174 ? 7.118   -16.960 75.711  1.00 160.47 ? 174 GLU A HB2  1 
ATOM   2792  H HB3  . GLU A 1 174 ? 7.307   -17.522 74.236  1.00 160.47 ? 174 GLU A HB3  1 
ATOM   2793  H HG2  . GLU A 1 174 ? 8.434   -15.521 74.459  1.00 161.94 ? 174 GLU A HG2  1 
ATOM   2794  H HG3  . GLU A 1 174 ? 7.255   -15.349 73.407  1.00 161.94 ? 174 GLU A HG3  1 
ATOM   2795  N N    . GLU A 1 175 ? 4.031   -15.096 73.860  1.00 136.67 ? 175 GLU A N    1 
ATOM   2796  C CA   . GLU A 1 175 ? 3.414   -14.235 72.861  1.00 135.75 ? 175 GLU A CA   1 
ATOM   2797  C C    . GLU A 1 175 ? 4.379   -13.132 72.447  1.00 134.43 ? 175 GLU A C    1 
ATOM   2798  O O    . GLU A 1 175 ? 4.966   -12.453 73.296  1.00 135.06 ? 175 GLU A O    1 
ATOM   2799  C CB   . GLU A 1 175 ? 2.120   -13.633 73.404  1.00 135.29 ? 175 GLU A CB   1 
ATOM   2800  C CG   . GLU A 1 175 ? 1.011   -14.646 73.615  1.00 135.78 ? 175 GLU A CG   1 
ATOM   2801  C CD   . GLU A 1 175 ? 0.595   -15.332 72.330  1.00 134.68 ? 175 GLU A CD   1 
ATOM   2802  O OE1  . GLU A 1 175 ? 0.778   -14.732 71.249  1.00 135.20 ? 175 GLU A OE1  1 
ATOM   2803  O OE2  . GLU A 1 175 ? 0.087   -16.471 72.401  1.00 130.88 ? 175 GLU A OE2  1 
ATOM   2804  H H    . GLU A 1 175 ? 3.826   -14.898 74.671  1.00 164.00 ? 175 GLU A H    1 
ATOM   2805  H HA   . GLU A 1 175 ? 3.198   -14.760 72.074  1.00 162.91 ? 175 GLU A HA   1 
ATOM   2806  H HB2  . GLU A 1 175 ? 2.306   -13.216 74.260  1.00 162.35 ? 175 GLU A HB2  1 
ATOM   2807  H HB3  . GLU A 1 175 ? 1.798   -12.969 72.775  1.00 162.35 ? 175 GLU A HB3  1 
ATOM   2808  H HG2  . GLU A 1 175 ? 1.319   -15.328 74.233  1.00 162.94 ? 175 GLU A HG2  1 
ATOM   2809  H HG3  . GLU A 1 175 ? 0.235   -14.194 73.980  1.00 162.94 ? 175 GLU A HG3  1 
ATOM   2810  N N    . TYR A 1 176 ? 4.534   -12.955 71.138  1.00 131.97 ? 176 TYR A N    1 
ATOM   2811  C CA   . TYR A 1 176 ? 5.436   -11.957 70.589  1.00 131.68 ? 176 TYR A CA   1 
ATOM   2812  C C    . TYR A 1 176 ? 4.858   -11.448 69.277  1.00 129.41 ? 176 TYR A C    1 
ATOM   2813  O O    . TYR A 1 176 ? 4.057   -12.122 68.625  1.00 129.05 ? 176 TYR A O    1 
ATOM   2814  C CB   . TYR A 1 176 ? 6.838   -12.534 70.358  1.00 129.49 ? 176 TYR A CB   1 
ATOM   2815  C CG   . TYR A 1 176 ? 6.848   -13.687 69.378  1.00 127.72 ? 176 TYR A CG   1 
ATOM   2816  C CD1  . TYR A 1 176 ? 6.973   -13.464 68.013  1.00 124.85 ? 176 TYR A CD1  1 
ATOM   2817  C CD2  . TYR A 1 176 ? 6.716   -14.997 69.817  1.00 128.58 ? 176 TYR A CD2  1 
ATOM   2818  C CE1  . TYR A 1 176 ? 6.971   -14.514 67.116  1.00 123.74 ? 176 TYR A CE1  1 
ATOM   2819  C CE2  . TYR A 1 176 ? 6.717   -16.053 68.926  1.00 126.74 ? 176 TYR A CE2  1 
ATOM   2820  C CZ   . TYR A 1 176 ? 6.846   -15.806 67.577  1.00 124.68 ? 176 TYR A CZ   1 
ATOM   2821  O OH   . TYR A 1 176 ? 6.848   -16.856 66.688  1.00 123.23 ? 176 TYR A OH   1 
ATOM   2822  H H    . TYR A 1 176 ? 4.119   -13.411 70.538  1.00 158.37 ? 176 TYR A H    1 
ATOM   2823  H HA   . TYR A 1 176 ? 5.509   -11.212 71.206  1.00 158.01 ? 176 TYR A HA   1 
ATOM   2824  H HB2  . TYR A 1 176 ? 7.411   -11.836 70.005  1.00 155.39 ? 176 TYR A HB2  1 
ATOM   2825  H HB3  . TYR A 1 176 ? 7.189   -12.856 71.203  1.00 155.39 ? 176 TYR A HB3  1 
ATOM   2826  H HD1  . TYR A 1 176 ? 7.060   -12.594 67.698  1.00 149.82 ? 176 TYR A HD1  1 
ATOM   2827  H HD2  . TYR A 1 176 ? 6.626   -15.167 70.727  1.00 154.30 ? 176 TYR A HD2  1 
ATOM   2828  H HE1  . TYR A 1 176 ? 7.053   -14.349 66.204  1.00 148.49 ? 176 TYR A HE1  1 
ATOM   2829  H HE2  . TYR A 1 176 ? 6.631   -16.926 69.236  1.00 152.08 ? 176 TYR A HE2  1 
ATOM   2830  H HH   . TYR A 1 176 ? 6.771   -17.583 67.102  1.00 147.88 ? 176 TYR A HH   1 
ATOM   2831  N N    . SER A 1 177 ? 5.279   -10.243 68.895  1.00 128.83 ? 177 SER A N    1 
ATOM   2832  C CA   . SER A 1 177 ? 4.910   -9.685  67.601  1.00 129.07 ? 177 SER A CA   1 
ATOM   2833  C C    . SER A 1 177 ? 5.910   -10.049 66.513  1.00 127.93 ? 177 SER A C    1 
ATOM   2834  O O    . SER A 1 177 ? 5.522   -10.204 65.349  1.00 130.86 ? 177 SER A O    1 
ATOM   2835  C CB   . SER A 1 177 ? 4.792   -8.163  67.699  1.00 127.63 ? 177 SER A CB   1 
ATOM   2836  O OG   . SER A 1 177 ? 4.073   -7.786  68.860  1.00 125.74 ? 177 SER A OG   1 
ATOM   2837  H H    . SER A 1 177 ? 5.780   -9.730  69.370  1.00 154.59 ? 177 SER A H    1 
ATOM   2838  H HA   . SER A 1 177 ? 4.042   -10.031 67.340  1.00 154.89 ? 177 SER A HA   1 
ATOM   2839  H HB2  . SER A 1 177 ? 5.681   -7.780  67.741  1.00 153.16 ? 177 SER A HB2  1 
ATOM   2840  H HB3  . SER A 1 177 ? 4.323   -7.832  66.917  1.00 153.16 ? 177 SER A HB3  1 
ATOM   2841  H HG   . SER A 1 177 ? 3.989   -6.951  68.888  1.00 150.88 ? 177 SER A HG   1 
ATOM   2842  N N    . ALA A 1 178 ? 7.183   -10.195 66.870  1.00 123.77 ? 178 ALA A N    1 
ATOM   2843  C CA   . ALA A 1 178 ? 8.230   -10.562 65.927  1.00 120.71 ? 178 ALA A CA   1 
ATOM   2844  C C    . ALA A 1 178 ? 9.489   -10.876 66.720  1.00 116.03 ? 178 ALA A C    1 
ATOM   2845  O O    . ALA A 1 178 ? 9.638   -10.456 67.871  1.00 114.76 ? 178 ALA A O    1 
ATOM   2846  C CB   . ALA A 1 178 ? 8.493   -9.448  64.910  1.00 120.24 ? 178 ALA A CB   1 
ATOM   2847  H H    . ALA A 1 178 ? 7.471   -10.084 67.673  1.00 148.52 ? 178 ALA A H    1 
ATOM   2848  H HA   . ALA A 1 178 ? 7.966   -11.358 65.439  1.00 144.85 ? 178 ALA A HA   1 
ATOM   2849  H HB1  . ALA A 1 178 ? 9.211   -9.723  64.319  1.00 144.28 ? 178 ALA A HB1  1 
ATOM   2850  H HB2  . ALA A 1 178 ? 7.685   -9.291  64.397  1.00 144.28 ? 178 ALA A HB2  1 
ATOM   2851  H HB3  . ALA A 1 178 ? 8.745   -8.640  65.384  1.00 144.28 ? 178 ALA A HB3  1 
ATOM   2852  N N    . PHE A 1 179 ? 10.389  -11.627 66.092  1.00 113.61 ? 179 PHE A N    1 
ATOM   2853  C CA   . PHE A 1 179 ? 11.667  -11.974 66.695  1.00 109.77 ? 179 PHE A CA   1 
ATOM   2854  C C    . PHE A 1 179 ? 12.739  -11.957 65.616  1.00 105.43 ? 179 PHE A C    1 
ATOM   2855  O O    . PHE A 1 179 ? 12.447  -11.918 64.417  1.00 106.72 ? 179 PHE A O    1 
ATOM   2856  C CB   . PHE A 1 179 ? 11.614  -13.342 67.394  1.00 107.89 ? 179 PHE A CB   1 
ATOM   2857  C CG   . PHE A 1 179 ? 11.397  -14.501 66.460  1.00 109.82 ? 179 PHE A CG   1 
ATOM   2858  C CD1  . PHE A 1 179 ? 12.469  -15.133 65.850  1.00 104.63 ? 179 PHE A CD1  1 
ATOM   2859  C CD2  . PHE A 1 179 ? 10.119  -14.969 66.202  1.00 114.34 ? 179 PHE A CD2  1 
ATOM   2860  C CE1  . PHE A 1 179 ? 12.269  -16.202 64.995  1.00 106.94 ? 179 PHE A CE1  1 
ATOM   2861  C CE2  . PHE A 1 179 ? 9.915   -16.038 65.348  1.00 113.55 ? 179 PHE A CE2  1 
ATOM   2862  C CZ   . PHE A 1 179 ? 10.989  -16.655 64.746  1.00 109.77 ? 179 PHE A CZ   1 
ATOM   2863  H H    . PHE A 1 179 ? 10.279  -11.952 65.303  1.00 136.33 ? 179 PHE A H    1 
ATOM   2864  H HA   . PHE A 1 179 ? 11.897  -11.309 67.363  1.00 131.73 ? 179 PHE A HA   1 
ATOM   2865  H HB2  . PHE A 1 179 ? 12.455  -13.488 67.854  1.00 129.46 ? 179 PHE A HB2  1 
ATOM   2866  H HB3  . PHE A 1 179 ? 10.883  -13.337 68.031  1.00 129.46 ? 179 PHE A HB3  1 
ATOM   2867  H HD1  . PHE A 1 179 ? 13.334  -14.834 66.018  1.00 125.55 ? 179 PHE A HD1  1 
ATOM   2868  H HD2  . PHE A 1 179 ? 9.390   -14.559 66.608  1.00 137.21 ? 179 PHE A HD2  1 
ATOM   2869  H HE1  . PHE A 1 179 ? 12.996  -16.615 64.588  1.00 128.33 ? 179 PHE A HE1  1 
ATOM   2870  H HE2  . PHE A 1 179 ? 9.051   -16.341 65.182  1.00 136.26 ? 179 PHE A HE2  1 
ATOM   2871  H HZ   . PHE A 1 179 ? 10.852  -17.374 64.172  1.00 131.72 ? 179 PHE A HZ   1 
ATOM   2872  N N    . GLY A 1 180 ? 13.995  -11.983 66.057  1.00 98.82  ? 180 GLY A N    1 
ATOM   2873  C CA   . GLY A 1 180 ? 15.115  -11.999 65.140  1.00 96.53  ? 180 GLY A CA   1 
ATOM   2874  C C    . GLY A 1 180 ? 16.248  -12.892 65.597  1.00 92.70  ? 180 GLY A C    1 
ATOM   2875  O O    . GLY A 1 180 ? 16.596  -12.904 66.779  1.00 93.91  ? 180 GLY A O    1 
ATOM   2876  H H    . GLY A 1 180 ? 14.219  -11.992 66.887  1.00 118.58 ? 180 GLY A H    1 
ATOM   2877  H HA2  . GLY A 1 180 ? 14.812  -12.314 64.274  1.00 115.83 ? 180 GLY A HA2  1 
ATOM   2878  H HA3  . GLY A 1 180 ? 15.460  -11.097 65.045  1.00 115.83 ? 180 GLY A HA3  1 
ATOM   2879  N N    . ILE A 1 181 ? 16.825  -13.655 64.673  1.00 93.54  ? 181 ILE A N    1 
ATOM   2880  C CA   . ILE A 1 181 ? 18.009  -14.462 64.938  1.00 89.78  ? 181 ILE A CA   1 
ATOM   2881  C C    . ILE A 1 181 ? 19.184  -13.795 64.237  1.00 88.81  ? 181 ILE A C    1 
ATOM   2882  O O    . ILE A 1 181 ? 19.161  -13.601 63.013  1.00 88.17  ? 181 ILE A O    1 
ATOM   2883  C CB   . ILE A 1 181 ? 17.841  -15.910 64.460  1.00 92.00  ? 181 ILE A CB   1 
ATOM   2884  C CG1  . ILE A 1 181 ? 16.694  -16.587 65.201  1.00 94.36  ? 181 ILE A CG1  1 
ATOM   2885  C CG2  . ILE A 1 181 ? 19.130  -16.688 64.679  1.00 90.95  ? 181 ILE A CG2  1 
ATOM   2886  C CD1  . ILE A 1 181 ? 15.395  -16.537 64.453  1.00 98.86  ? 181 ILE A CD1  1 
ATOM   2887  H H    . ILE A 1 181 ? 16.539  -13.722 63.864  1.00 112.25 ? 181 ILE A H    1 
ATOM   2888  H HA   . ILE A 1 181 ? 18.177  -14.477 65.893  1.00 107.74 ? 181 ILE A HA   1 
ATOM   2889  H HB   . ILE A 1 181 ? 17.634  -15.895 63.513  1.00 110.40 ? 181 ILE A HB   1 
ATOM   2890  H HG12 . ILE A 1 181 ? 16.920  -17.519 65.345  1.00 113.24 ? 181 ILE A HG12 1 
ATOM   2891  H HG13 . ILE A 1 181 ? 16.565  -16.142 66.053  1.00 113.24 ? 181 ILE A HG13 1 
ATOM   2892  H HG21 . ILE A 1 181 ? 18.959  -17.631 64.528  1.00 109.13 ? 181 ILE A HG21 1 
ATOM   2893  H HG22 . ILE A 1 181 ? 19.801  -16.370 64.054  1.00 109.13 ? 181 ILE A HG22 1 
ATOM   2894  H HG23 . ILE A 1 181 ? 19.433  -16.548 65.590  1.00 109.13 ? 181 ILE A HG23 1 
ATOM   2895  H HD11 . ILE A 1 181 ? 14.827  -17.262 64.757  1.00 118.64 ? 181 ILE A HD11 1 
ATOM   2896  H HD12 . ILE A 1 181 ? 14.965  -15.685 64.624  1.00 118.64 ? 181 ILE A HD12 1 
ATOM   2897  H HD13 . ILE A 1 181 ? 15.574  -16.633 63.504  1.00 118.64 ? 181 ILE A HD13 1 
ATOM   2898  N N    . MET A 1 182 ? 20.203  -13.440 65.009  1.00 87.10  ? 182 MET A N    1 
ATOM   2899  C CA   . MET A 1 182 ? 21.414  -12.817 64.483  1.00 84.26  ? 182 MET A CA   1 
ATOM   2900  C C    . MET A 1 182 ? 22.490  -13.895 64.424  1.00 84.02  ? 182 MET A C    1 
ATOM   2901  O O    . MET A 1 182 ? 23.149  -14.190 65.424  1.00 85.30  ? 182 MET A O    1 
ATOM   2902  C CB   . MET A 1 182 ? 21.828  -11.633 65.349  1.00 83.25  ? 182 MET A CB   1 
ATOM   2903  C CG   . MET A 1 182 ? 20.667  -10.726 65.737  1.00 84.24  ? 182 MET A CG   1 
ATOM   2904  S SD   . MET A 1 182 ? 19.616  -10.266 64.334  1.00 88.26  ? 182 MET A SD   1 
ATOM   2905  C CE   . MET A 1 182 ? 20.654  -9.081  63.510  1.00 80.25  ? 182 MET A CE   1 
ATOM   2906  H H    . MET A 1 182 ? 20.218  -13.552 65.862  1.00 104.52 ? 182 MET A H    1 
ATOM   2907  H HA   . MET A 1 182 ? 21.251  -12.480 63.588  1.00 101.11 ? 182 MET A HA   1 
ATOM   2908  H HB2  . MET A 1 182 ? 22.229  -11.969 66.166  1.00 99.90  ? 182 MET A HB2  1 
ATOM   2909  H HB3  . MET A 1 182 ? 22.472  -11.098 64.859  1.00 99.90  ? 182 MET A HB3  1 
ATOM   2910  H HG2  . MET A 1 182 ? 20.113  -11.186 66.386  1.00 101.09 ? 182 MET A HG2  1 
ATOM   2911  H HG3  . MET A 1 182 ? 21.022  -9.910  66.123  1.00 101.09 ? 182 MET A HG3  1 
ATOM   2912  H HE1  . MET A 1 182 ? 20.095  -8.453  63.027  1.00 96.30  ? 182 MET A HE1  1 
ATOM   2913  H HE2  . MET A 1 182 ? 21.184  -8.610  64.173  1.00 96.30  ? 182 MET A HE2  1 
ATOM   2914  H HE3  . MET A 1 182 ? 21.237  -9.548  62.891  1.00 96.30  ? 182 MET A HE3  1 
ATOM   2915  N N    . PHE A 1 183 ? 22.646  -14.500 63.249  1.00 84.51  ? 183 PHE A N    1 
ATOM   2916  C CA   . PHE A 1 183 ? 23.674  -15.510 63.032  1.00 83.53  ? 183 PHE A CA   1 
ATOM   2917  C C    . PHE A 1 183 ? 25.029  -14.823 62.935  1.00 80.33  ? 183 PHE A C    1 
ATOM   2918  O O    . PHE A 1 183 ? 25.324  -14.148 61.944  1.00 81.13  ? 183 PHE A O    1 
ATOM   2919  C CB   . PHE A 1 183 ? 23.364  -16.303 61.769  1.00 87.43  ? 183 PHE A CB   1 
ATOM   2920  C CG   . PHE A 1 183 ? 22.069  -17.061 61.835  1.00 88.96  ? 183 PHE A CG   1 
ATOM   2921  C CD1  . PHE A 1 183 ? 22.010  -18.301 62.450  1.00 86.47  ? 183 PHE A CD1  1 
ATOM   2922  C CD2  . PHE A 1 183 ? 20.912  -16.534 61.279  1.00 90.61  ? 183 PHE A CD2  1 
ATOM   2923  C CE1  . PHE A 1 183 ? 20.822  -19.006 62.508  1.00 88.46  ? 183 PHE A CE1  1 
ATOM   2924  C CE2  . PHE A 1 183 ? 19.720  -17.234 61.335  1.00 92.83  ? 183 PHE A CE2  1 
ATOM   2925  C CZ   . PHE A 1 183 ? 19.676  -18.473 61.952  1.00 94.69  ? 183 PHE A CZ   1 
ATOM   2926  H H    . PHE A 1 183 ? 22.163  -14.340 62.556  1.00 101.41 ? 183 PHE A H    1 
ATOM   2927  H HA   . PHE A 1 183 ? 23.693  -16.129 63.779  1.00 100.23 ? 183 PHE A HA   1 
ATOM   2928  H HB2  . PHE A 1 183 ? 23.309  -15.688 61.021  1.00 104.91 ? 183 PHE A HB2  1 
ATOM   2929  H HB3  . PHE A 1 183 ? 24.076  -16.944 61.621  1.00 104.91 ? 183 PHE A HB3  1 
ATOM   2930  H HD1  . PHE A 1 183 ? 22.778  -18.664 62.829  1.00 103.76 ? 183 PHE A HD1  1 
ATOM   2931  H HD2  . PHE A 1 183 ? 20.938  -15.703 60.864  1.00 108.73 ? 183 PHE A HD2  1 
ATOM   2932  H HE1  . PHE A 1 183 ? 20.795  -19.839 62.921  1.00 106.15 ? 183 PHE A HE1  1 
ATOM   2933  H HE2  . PHE A 1 183 ? 18.949  -16.873 60.960  1.00 111.39 ? 183 PHE A HE2  1 
ATOM   2934  H HZ   . PHE A 1 183 ? 18.876  -18.945 61.991  1.00 113.63 ? 183 PHE A HZ   1 
ATOM   2935  N N    . PHE A 1 184 ? 25.856  -15.001 63.959  1.00 80.86  ? 184 PHE A N    1 
ATOM   2936  C CA   . PHE A 1 184 ? 27.076  -14.228 64.141  1.00 82.90  ? 184 PHE A CA   1 
ATOM   2937  C C    . PHE A 1 184 ? 28.291  -15.100 63.867  1.00 82.18  ? 184 PHE A C    1 
ATOM   2938  O O    . PHE A 1 184 ? 28.403  -16.204 64.410  1.00 84.54  ? 184 PHE A O    1 
ATOM   2939  C CB   . PHE A 1 184 ? 27.121  -13.660 65.563  1.00 81.15  ? 184 PHE A CB   1 
ATOM   2940  C CG   . PHE A 1 184 ? 28.457  -13.124 65.966  1.00 82.39  ? 184 PHE A CG   1 
ATOM   2941  C CD1  . PHE A 1 184 ? 28.983  -12.005 65.348  1.00 84.10  ? 184 PHE A CD1  1 
ATOM   2942  C CD2  . PHE A 1 184 ? 29.186  -13.734 66.976  1.00 85.91  ? 184 PHE A CD2  1 
ATOM   2943  C CE1  . PHE A 1 184 ? 30.215  -11.506 65.724  1.00 88.18  ? 184 PHE A CE1  1 
ATOM   2944  C CE2  . PHE A 1 184 ? 30.418  -13.242 67.355  1.00 86.46  ? 184 PHE A CE2  1 
ATOM   2945  C CZ   . PHE A 1 184 ? 30.934  -12.126 66.728  1.00 87.39  ? 184 PHE A CZ   1 
ATOM   2946  H H    . PHE A 1 184 ? 25.727  -15.582 64.579  1.00 97.04  ? 184 PHE A H    1 
ATOM   2947  H HA   . PHE A 1 184 ? 27.104  -13.494 63.508  1.00 99.48  ? 184 PHE A HA   1 
ATOM   2948  H HB2  . PHE A 1 184 ? 26.481  -12.934 65.628  1.00 97.39  ? 184 PHE A HB2  1 
ATOM   2949  H HB3  . PHE A 1 184 ? 26.886  -14.365 66.187  1.00 97.39  ? 184 PHE A HB3  1 
ATOM   2950  H HD1  . PHE A 1 184 ? 28.503  -11.584 64.672  1.00 100.91 ? 184 PHE A HD1  1 
ATOM   2951  H HD2  . PHE A 1 184 ? 28.840  -14.484 67.403  1.00 103.09 ? 184 PHE A HD2  1 
ATOM   2952  H HE1  . PHE A 1 184 ? 30.561  -10.754 65.301  1.00 105.82 ? 184 PHE A HE1  1 
ATOM   2953  H HE2  . PHE A 1 184 ? 30.899  -13.661 68.031  1.00 103.75 ? 184 PHE A HE2  1 
ATOM   2954  H HZ   . PHE A 1 184 ? 31.764  -11.791 66.981  1.00 104.87 ? 184 PHE A HZ   1 
ATOM   2955  N N    . ASP A 1 185 ? 29.195  -14.598 63.025  1.00 82.02  ? 185 ASP A N    1 
ATOM   2956  C CA   . ASP A 1 185 ? 30.435  -15.285 62.677  1.00 87.08  ? 185 ASP A CA   1 
ATOM   2957  C C    . ASP A 1 185 ? 31.601  -14.516 63.290  1.00 88.48  ? 185 ASP A C    1 
ATOM   2958  O O    . ASP A 1 185 ? 31.883  -13.380 62.891  1.00 85.61  ? 185 ASP A O    1 
ATOM   2959  C CB   . ASP A 1 185 ? 30.589  -15.405 61.162  1.00 87.63  ? 185 ASP A CB   1 
ATOM   2960  C CG   . ASP A 1 185 ? 31.730  -16.323 60.764  1.00 93.37  ? 185 ASP A CG   1 
ATOM   2961  O OD1  . ASP A 1 185 ? 32.741  -16.369 61.494  1.00 96.59  ? 185 ASP A OD1  1 
ATOM   2962  O OD2  . ASP A 1 185 ? 31.617  -17.000 59.721  1.00 100.55 ? 185 ASP A OD2  1 
ATOM   2963  H H    . ASP A 1 185 ? 29.108  -13.838 62.632  1.00 98.42  ? 185 ASP A H    1 
ATOM   2964  H HA   . ASP A 1 185 ? 30.424  -16.178 63.055  1.00 104.50 ? 185 ASP A HA   1 
ATOM   2965  H HB2  . ASP A 1 185 ? 29.769  -15.765 60.788  1.00 105.16 ? 185 ASP A HB2  1 
ATOM   2966  H HB3  . ASP A 1 185 ? 30.766  -14.527 60.791  1.00 105.16 ? 185 ASP A HB3  1 
ATOM   2967  N N    . SER A 1 186 ? 32.286  -15.149 64.248  1.00 91.29  ? 186 SER A N    1 
ATOM   2968  C CA   . SER A 1 186 ? 33.343  -14.467 64.987  1.00 92.04  ? 186 SER A CA   1 
ATOM   2969  C C    . SER A 1 186 ? 34.591  -14.272 64.136  1.00 94.15  ? 186 SER A C    1 
ATOM   2970  O O    . SER A 1 186 ? 35.288  -13.259 64.272  1.00 95.93  ? 186 SER A O    1 
ATOM   2971  C CB   . SER A 1 186 ? 33.689  -15.259 66.248  1.00 91.85  ? 186 SER A CB   1 
ATOM   2972  O OG   . SER A 1 186 ? 32.521  -15.683 66.929  1.00 94.83  ? 186 SER A OG   1 
ATOM   2973  H H    . SER A 1 186 ? 32.157  -15.966 64.485  1.00 109.55 ? 186 SER A H    1 
ATOM   2974  H HA   . SER A 1 186 ? 33.017  -13.591 65.248  1.00 110.45 ? 186 SER A HA   1 
ATOM   2975  H HB2  . SER A 1 186 ? 34.206  -16.040 65.995  1.00 110.22 ? 186 SER A HB2  1 
ATOM   2976  H HB3  . SER A 1 186 ? 34.209  -14.694 66.840  1.00 110.22 ? 186 SER A HB3  1 
ATOM   2977  H HG   . SER A 1 186 ? 32.239  -15.067 67.426  1.00 113.79 ? 186 SER A HG   1 
ATOM   2978  N N    . ASP A 1 187 ? 34.900  -15.237 63.268  1.00 92.88  ? 187 ASP A N    1 
ATOM   2979  C CA   . ASP A 1 187 ? 36.094  -15.126 62.435  1.00 96.83  ? 187 ASP A CA   1 
ATOM   2980  C C    . ASP A 1 187 ? 36.099  -13.831 61.634  1.00 97.83  ? 187 ASP A C    1 
ATOM   2981  O O    . ASP A 1 187 ? 37.169  -13.285 61.341  1.00 100.17 ? 187 ASP A O    1 
ATOM   2982  C CB   . ASP A 1 187 ? 36.182  -16.319 61.482  1.00 99.22  ? 187 ASP A CB   1 
ATOM   2983  C CG   . ASP A 1 187 ? 36.614  -17.593 62.173  1.00 102.34 ? 187 ASP A CG   1 
ATOM   2984  O OD1  . ASP A 1 187 ? 36.746  -17.588 63.415  1.00 102.46 ? 187 ASP A OD1  1 
ATOM   2985  O OD2  . ASP A 1 187 ? 36.817  -18.606 61.470  1.00 105.47 ? 187 ASP A OD2  1 
ATOM   2986  H H    . ASP A 1 187 ? 34.442  -15.954 63.144  1.00 111.45 ? 187 ASP A H    1 
ATOM   2987  H HA   . ASP A 1 187 ? 36.873  -15.134 63.012  1.00 116.19 ? 187 ASP A HA   1 
ATOM   2988  H HB2  . ASP A 1 187 ? 35.310  -16.473 61.087  1.00 119.06 ? 187 ASP A HB2  1 
ATOM   2989  H HB3  . ASP A 1 187 ? 36.830  -16.121 60.787  1.00 119.06 ? 187 ASP A HB3  1 
ATOM   2990  N N    . ASN A 1 188 ? 34.920  -13.335 61.271  1.00 94.81  ? 188 ASN A N    1 
ATOM   2991  C CA   . ASN A 1 188 ? 34.778  -12.183 60.401  1.00 93.66  ? 188 ASN A CA   1 
ATOM   2992  C C    . ASN A 1 188 ? 34.127  -10.991 61.081  1.00 90.83  ? 188 ASN A C    1 
ATOM   2993  O O    . ASN A 1 188 ? 34.191  -9.882  60.536  1.00 89.54  ? 188 ASN A O    1 
ATOM   2994  C CB   . ASN A 1 188 ? 33.940  -12.562 59.168  1.00 89.86  ? 188 ASN A CB   1 
ATOM   2995  C CG   . ASN A 1 188 ? 34.390  -11.856 57.913  1.00 97.81  ? 188 ASN A CG   1 
ATOM   2996  O OD1  . ASN A 1 188 ? 35.500  -11.328 57.845  1.00 103.08 ? 188 ASN A OD1  1 
ATOM   2997  N ND2  . ASN A 1 188 ? 33.528  -11.846 56.901  1.00 97.90  ? 188 ASN A ND2  1 
ATOM   2998  H H    . ASN A 1 188 ? 34.167  -13.662 61.526  1.00 113.77 ? 188 ASN A H    1 
ATOM   2999  H HA   . ASN A 1 188 ? 35.657  -11.908 60.098  1.00 112.39 ? 188 ASN A HA   1 
ATOM   3000  H HB2  . ASN A 1 188 ? 34.014  -13.517 59.017  1.00 107.83 ? 188 ASN A HB2  1 
ATOM   3001  H HB3  . ASN A 1 188 ? 33.014  -12.323 59.330  1.00 107.83 ? 188 ASN A HB3  1 
ATOM   3002  H HD21 . ASN A 1 188 ? 32.762  -12.229 56.984  1.00 117.48 ? 188 ASN A HD21 1 
ATOM   3003  H HD22 . ASN A 1 188 ? 33.736  -11.456 56.162  1.00 117.48 ? 188 ASN A HD22 1 
ATOM   3004  N N    . LEU A 1 189 ? 33.523  -11.175 62.255  1.00 90.82  ? 189 LEU A N    1 
ATOM   3005  C CA   . LEU A 1 189 ? 32.674  -10.153 62.861  1.00 89.23  ? 189 LEU A CA   1 
ATOM   3006  C C    . LEU A 1 189 ? 31.574  -9.748  61.879  1.00 84.35  ? 189 LEU A C    1 
ATOM   3007  O O    . LEU A 1 189 ? 31.365  -8.569  61.584  1.00 80.73  ? 189 LEU A O    1 
ATOM   3008  C CB   . LEU A 1 189 ? 33.497  -8.949  63.311  1.00 91.04  ? 189 LEU A CB   1 
ATOM   3009  C CG   . LEU A 1 189 ? 34.009  -8.979  64.758  1.00 91.69  ? 189 LEU A CG   1 
ATOM   3010  C CD1  . LEU A 1 189 ? 32.860  -9.005  65.762  1.00 87.31  ? 189 LEU A CD1  1 
ATOM   3011  C CD2  . LEU A 1 189 ? 34.935  -10.171 64.990  1.00 93.90  ? 189 LEU A CD2  1 
ATOM   3012  H H    . LEU A 1 189 ? 33.590  -11.892 62.724  1.00 108.99 ? 189 LEU A H    1 
ATOM   3013  H HA   . LEU A 1 189 ? 32.250  -10.517 63.654  1.00 107.08 ? 189 LEU A HA   1 
ATOM   3014  H HB2  . LEU A 1 189 ? 34.274  -8.882  62.734  1.00 109.25 ? 189 LEU A HB2  1 
ATOM   3015  H HB3  . LEU A 1 189 ? 32.946  -8.156  63.220  1.00 109.25 ? 189 LEU A HB3  1 
ATOM   3016  H HG   . LEU A 1 189 ? 34.516  -8.165  64.908  1.00 110.03 ? 189 LEU A HG   1 
ATOM   3017  H HD11 . LEU A 1 189 ? 33.195  -8.740  66.633  1.00 104.77 ? 189 LEU A HD11 1 
ATOM   3018  H HD12 . LEU A 1 189 ? 32.172  -8.386  65.470  1.00 104.77 ? 189 LEU A HD12 1 
ATOM   3019  H HD13 . LEU A 1 189 ? 32.499  -9.904  65.806  1.00 104.77 ? 189 LEU A HD13 1 
ATOM   3020  H HD21 . LEU A 1 189 ? 35.288  -10.127 65.892  1.00 112.68 ? 189 LEU A HD21 1 
ATOM   3021  H HD22 . LEU A 1 189 ? 34.429  -10.991 64.873  1.00 112.68 ? 189 LEU A HD22 1 
ATOM   3022  H HD23 . LEU A 1 189 ? 35.661  -10.137 64.348  1.00 112.68 ? 189 LEU A HD23 1 
ATOM   3023  N N    . SER A 1 190 ? 30.883  -10.755 61.352  1.00 82.37  ? 190 SER A N    1 
ATOM   3024  C CA   . SER A 1 190 ? 29.766  -10.587 60.436  1.00 81.78  ? 190 SER A CA   1 
ATOM   3025  C C    . SER A 1 190 ? 28.480  -11.058 61.105  1.00 80.48  ? 190 SER A C    1 
ATOM   3026  O O    . SER A 1 190 ? 28.495  -11.702 62.158  1.00 83.78  ? 190 SER A O    1 
ATOM   3027  C CB   . SER A 1 190 ? 30.008  -11.362 59.133  1.00 85.17  ? 190 SER A CB   1 
ATOM   3028  O OG   . SER A 1 190 ? 30.552  -12.650 59.378  1.00 82.99  ? 190 SER A OG   1 
ATOM   3029  H H    . SER A 1 190 ? 31.053  -11.581 61.521  1.00 98.84  ? 190 SER A H    1 
ATOM   3030  H HA   . SER A 1 190 ? 29.671  -9.648  60.211  1.00 98.13  ? 190 SER A HA   1 
ATOM   3031  H HB2  . SER A 1 190 ? 29.162  -11.464 58.669  1.00 102.20 ? 190 SER A HB2  1 
ATOM   3032  H HB3  . SER A 1 190 ? 30.629  -10.860 58.582  1.00 102.20 ? 190 SER A HB3  1 
ATOM   3033  H HG   . SER A 1 190 ? 30.690  -13.047 58.650  1.00 99.59  ? 190 SER A HG   1 
ATOM   3034  N N    . MET A 1 191 ? 27.354  -10.739 60.473  1.00 79.26  ? 191 MET A N    1 
ATOM   3035  C CA   . MET A 1 191 ? 26.054  -11.067 61.043  1.00 82.00  ? 191 MET A CA   1 
ATOM   3036  C C    . MET A 1 191 ? 25.025  -11.160 59.928  1.00 80.46  ? 191 MET A C    1 
ATOM   3037  O O    . MET A 1 191 ? 24.886  -10.225 59.136  1.00 79.90  ? 191 MET A O    1 
ATOM   3038  C CB   . MET A 1 191 ? 25.638  -10.009 62.069  1.00 78.09  ? 191 MET A CB   1 
ATOM   3039  C CG   . MET A 1 191 ? 24.251  -10.199 62.650  1.00 79.22  ? 191 MET A CG   1 
ATOM   3040  S SD   . MET A 1 191 ? 23.848  -8.889  63.823  1.00 83.82  ? 191 MET A SD   1 
ATOM   3041  C CE   . MET A 1 191 ? 23.451  -7.544  62.707  1.00 76.04  ? 191 MET A CE   1 
ATOM   3042  H H    . MET A 1 191 ? 27.317  -10.334 59.715  1.00 95.12  ? 191 MET A H    1 
ATOM   3043  H HA   . MET A 1 191 ? 26.106  -11.928 61.487  1.00 98.41  ? 191 MET A HA   1 
ATOM   3044  H HB2  . MET A 1 191 ? 26.268  -10.031 62.806  1.00 93.70  ? 191 MET A HB2  1 
ATOM   3045  H HB3  . MET A 1 191 ? 25.658  -9.139  61.641  1.00 93.70  ? 191 MET A HB3  1 
ATOM   3046  H HG2  . MET A 1 191 ? 23.597  -10.182 61.934  1.00 95.07  ? 191 MET A HG2  1 
ATOM   3047  H HG3  . MET A 1 191 ? 24.210  -11.050 63.115  1.00 95.07  ? 191 MET A HG3  1 
ATOM   3048  H HE1  . MET A 1 191 ? 23.157  -6.779  63.226  1.00 91.25  ? 191 MET A HE1  1 
ATOM   3049  H HE2  . MET A 1 191 ? 24.243  -7.313  62.196  1.00 91.25  ? 191 MET A HE2  1 
ATOM   3050  H HE3  . MET A 1 191 ? 22.743  -7.829  62.108  1.00 91.25  ? 191 MET A HE3  1 
ATOM   3051  N N    . LYS A 1 192 ? 24.306  -12.286 59.876  1.00 81.93  ? 192 LYS A N    1 
ATOM   3052  C CA   . LYS A 1 192 ? 23.214  -12.479 58.931  1.00 84.10  ? 192 LYS A CA   1 
ATOM   3053  C C    . LYS A 1 192 ? 21.894  -12.239 59.655  1.00 82.10  ? 192 LYS A C    1 
ATOM   3054  O O    . LYS A 1 192 ? 21.417  -13.130 60.376  1.00 84.31  ? 192 LYS A O    1 
ATOM   3055  C CB   . LYS A 1 192 ? 23.257  -13.891 58.339  1.00 87.45  ? 192 LYS A CB   1 
ATOM   3056  C CG   . LYS A 1 192 ? 24.116  -14.022 57.086  1.00 90.14  ? 192 LYS A CG   1 
ATOM   3057  C CD   . LYS A 1 192 ? 25.005  -15.264 57.131  1.00 100.80 ? 192 LYS A CD   1 
ATOM   3058  C CE   . LYS A 1 192 ? 26.329  -14.990 57.850  1.00 101.97 ? 192 LYS A CE   1 
ATOM   3059  N NZ   . LYS A 1 192 ? 27.273  -16.147 57.775  1.00 101.38 ? 192 LYS A NZ   1 
ATOM   3060  H H    . LYS A 1 192 ? 24.437  -12.962 60.390  1.00 98.32  ? 192 LYS A H    1 
ATOM   3061  H HA   . LYS A 1 192 ? 23.295  -11.840 58.206  1.00 100.92 ? 192 LYS A HA   1 
ATOM   3062  H HB2  . LYS A 1 192 ? 23.617  -14.496 59.006  1.00 104.94 ? 192 LYS A HB2  1 
ATOM   3063  H HB3  . LYS A 1 192 ? 22.353  -14.156 58.105  1.00 104.94 ? 192 LYS A HB3  1 
ATOM   3064  H HG2  . LYS A 1 192 ? 23.539  -14.090 56.309  1.00 108.17 ? 192 LYS A HG2  1 
ATOM   3065  H HG3  . LYS A 1 192 ? 24.687  -13.242 57.008  1.00 108.17 ? 192 LYS A HG3  1 
ATOM   3066  H HD2  . LYS A 1 192 ? 24.543  -15.972 57.606  1.00 120.96 ? 192 LYS A HD2  1 
ATOM   3067  H HD3  . LYS A 1 192 ? 25.205  -15.548 56.225  1.00 120.96 ? 192 LYS A HD3  1 
ATOM   3068  H HE2  . LYS A 1 192 ? 26.759  -14.223 57.440  1.00 122.36 ? 192 LYS A HE2  1 
ATOM   3069  H HE3  . LYS A 1 192 ? 26.149  -14.808 58.786  1.00 122.36 ? 192 LYS A HE3  1 
ATOM   3070  H HZ1  . LYS A 1 192 ? 28.032  -15.948 58.195  1.00 121.65 ? 192 LYS A HZ1  1 
ATOM   3071  H HZ2  . LYS A 1 192 ? 26.909  -16.862 58.159  1.00 121.65 ? 192 LYS A HZ2  1 
ATOM   3072  H HZ3  . LYS A 1 192 ? 27.454  -16.337 56.924  1.00 121.65 ? 192 LYS A HZ3  1 
ATOM   3073  N N    . PRO A 1 193 ? 21.264  -11.074 59.505  1.00 82.90  ? 193 PRO A N    1 
ATOM   3074  C CA   . PRO A 1 193 ? 20.034  -10.808 60.264  1.00 86.38  ? 193 PRO A CA   1 
ATOM   3075  C C    . PRO A 1 193 ? 18.852  -11.585 59.702  1.00 89.53  ? 193 PRO A C    1 
ATOM   3076  O O    . PRO A 1 193 ? 18.625  -11.612 58.490  1.00 94.54  ? 193 PRO A O    1 
ATOM   3077  C CB   . PRO A 1 193 ? 19.834  -9.294  60.122  1.00 85.03  ? 193 PRO A CB   1 
ATOM   3078  C CG   . PRO A 1 193 ? 20.673  -8.870  58.960  1.00 83.74  ? 193 PRO A CG   1 
ATOM   3079  C CD   . PRO A 1 193 ? 21.617  -9.979  58.582  1.00 83.57  ? 193 PRO A CD   1 
ATOM   3080  H HA   . PRO A 1 193 ? 20.158  -11.036 61.198  1.00 103.65 ? 193 PRO A HA   1 
ATOM   3081  H HB2  . PRO A 1 193 ? 18.898  -9.103  59.956  1.00 102.03 ? 193 PRO A HB2  1 
ATOM   3082  H HB3  . PRO A 1 193 ? 20.124  -8.850  60.934  1.00 102.03 ? 193 PRO A HB3  1 
ATOM   3083  H HG2  . PRO A 1 193 ? 20.089  -8.666  58.213  1.00 100.49 ? 193 PRO A HG2  1 
ATOM   3084  H HG3  . PRO A 1 193 ? 21.177  -8.080  59.212  1.00 100.49 ? 193 PRO A HG3  1 
ATOM   3085  H HD2  . PRO A 1 193 ? 21.479  -10.249 57.661  1.00 100.28 ? 193 PRO A HD2  1 
ATOM   3086  H HD3  . PRO A 1 193 ? 22.538  -9.704  58.713  1.00 100.28 ? 193 PRO A HD3  1 
ATOM   3087  N N    . TYR A 1 194 ? 18.104  -12.220 60.598  1.00 92.34  ? 194 TYR A N    1 
ATOM   3088  C CA   . TYR A 1 194 ? 16.862  -12.903 60.273  1.00 93.95  ? 194 TYR A CA   1 
ATOM   3089  C C    . TYR A 1 194 ? 15.726  -12.228 61.027  1.00 97.51  ? 194 TYR A C    1 
ATOM   3090  O O    . TYR A 1 194 ? 15.898  -11.809 62.177  1.00 97.37  ? 194 TYR A O    1 
ATOM   3091  C CB   . TYR A 1 194 ? 16.927  -14.384 60.645  1.00 95.82  ? 194 TYR A CB   1 
ATOM   3092  C CG   . TYR A 1 194 ? 15.657  -15.150 60.352  1.00 100.69 ? 194 TYR A CG   1 
ATOM   3093  C CD1  . TYR A 1 194 ? 14.591  -15.135 61.241  1.00 103.88 ? 194 TYR A CD1  1 
ATOM   3094  C CD2  . TYR A 1 194 ? 15.528  -15.895 59.189  1.00 104.68 ? 194 TYR A CD2  1 
ATOM   3095  C CE1  . TYR A 1 194 ? 13.430  -15.835 60.978  1.00 109.00 ? 194 TYR A CE1  1 
ATOM   3096  C CE2  . TYR A 1 194 ? 14.369  -16.600 58.916  1.00 110.10 ? 194 TYR A CE2  1 
ATOM   3097  C CZ   . TYR A 1 194 ? 13.324  -16.567 59.814  1.00 111.19 ? 194 TYR A CZ   1 
ATOM   3098  O OH   . TYR A 1 194 ? 12.167  -17.269 59.556  1.00 113.16 ? 194 TYR A OH   1 
ATOM   3099  H H    . TYR A 1 194 ? 18.306  -12.270 61.433  1.00 110.81 ? 194 TYR A H    1 
ATOM   3100  H HA   . TYR A 1 194 ? 16.688  -12.844 59.321  1.00 112.74 ? 194 TYR A HA   1 
ATOM   3101  H HB2  . TYR A 1 194 ? 17.645  -14.799 60.142  1.00 114.99 ? 194 TYR A HB2  1 
ATOM   3102  H HB3  . TYR A 1 194 ? 17.103  -14.458 61.596  1.00 114.99 ? 194 TYR A HB3  1 
ATOM   3103  H HD1  . TYR A 1 194 ? 14.659  -14.645 62.029  1.00 124.66 ? 194 TYR A HD1  1 
ATOM   3104  H HD2  . TYR A 1 194 ? 16.232  -15.920 58.582  1.00 125.62 ? 194 TYR A HD2  1 
ATOM   3105  H HE1  . TYR A 1 194 ? 12.723  -15.814 61.582  1.00 130.81 ? 194 TYR A HE1  1 
ATOM   3106  H HE2  . TYR A 1 194 ? 14.296  -17.094 58.131  1.00 132.12 ? 194 TYR A HE2  1 
ATOM   3107  H HH   . TYR A 1 194 ? 12.238  -17.680 58.827  1.00 135.79 ? 194 TYR A HH   1 
ATOM   3108  N N    . VAL A 1 195 ? 14.564  -12.134 60.385  1.00 100.71 ? 195 VAL A N    1 
ATOM   3109  C CA   . VAL A 1 195 ? 13.410  -11.502 61.011  1.00 104.31 ? 195 VAL A CA   1 
ATOM   3110  C C    . VAL A 1 195 ? 12.124  -12.190 60.573  1.00 108.77 ? 195 VAL A C    1 
ATOM   3111  O O    . VAL A 1 195 ? 11.737  -12.126 59.401  1.00 111.47 ? 195 VAL A O    1 
ATOM   3112  C CB   . VAL A 1 195 ? 13.365  -9.996  60.685  1.00 101.44 ? 195 VAL A CB   1 
ATOM   3113  C CG1  . VAL A 1 195 ? 11.946  -9.461  60.816  1.00 105.23 ? 195 VAL A CG1  1 
ATOM   3114  C CG2  . VAL A 1 195 ? 14.318  -9.224  61.586  1.00 96.34  ? 195 VAL A CG2  1 
ATOM   3115  H H    . VAL A 1 195 ? 14.421  -12.427 59.589  1.00 120.85 ? 195 VAL A H    1 
ATOM   3116  H HA   . VAL A 1 195 ? 13.486  -11.613 61.972  1.00 125.17 ? 195 VAL A HA   1 
ATOM   3117  H HB   . VAL A 1 195 ? 13.650  -9.866  59.767  1.00 121.73 ? 195 VAL A HB   1 
ATOM   3118  H HG11 . VAL A 1 195 ? 11.976  -8.493  60.867  1.00 126.28 ? 195 VAL A HG11 1 
ATOM   3119  H HG12 . VAL A 1 195 ? 11.432  -9.736  60.040  1.00 126.28 ? 195 VAL A HG12 1 
ATOM   3120  H HG13 . VAL A 1 195 ? 11.545  -9.823  61.622  1.00 126.28 ? 195 VAL A HG13 1 
ATOM   3121  H HG21 . VAL A 1 195 ? 14.234  -8.277  61.397  1.00 115.61 ? 195 VAL A HG21 1 
ATOM   3122  H HG22 . VAL A 1 195 ? 14.088  -9.399  62.512  1.00 115.61 ? 195 VAL A HG22 1 
ATOM   3123  H HG23 . VAL A 1 195 ? 15.226  -9.517  61.409  1.00 115.61 ? 195 VAL A HG23 1 
ATOM   3124  N N    . TYR A 1 196 ? 11.459  -12.856 61.513  1.00 111.61 ? 196 TYR A N    1 
ATOM   3125  C CA   . TYR A 1 196 ? 10.097  -13.337 61.330  1.00 115.47 ? 196 TYR A CA   1 
ATOM   3126  C C    . TYR A 1 196 ? 9.150   -12.322 61.962  1.00 119.82 ? 196 TYR A C    1 
ATOM   3127  O O    . TYR A 1 196 ? 9.445   -11.756 63.020  1.00 119.53 ? 196 TYR A O    1 
ATOM   3128  C CB   . TYR A 1 196 ? 9.907   -14.725 61.960  1.00 115.49 ? 196 TYR A CB   1 
ATOM   3129  C CG   . TYR A 1 196 ? 8.471   -15.237 61.975  1.00 120.01 ? 196 TYR A CG   1 
ATOM   3130  C CD1  . TYR A 1 196 ? 7.472   -14.593 62.699  1.00 119.83 ? 196 TYR A CD1  1 
ATOM   3131  C CD2  . TYR A 1 196 ? 8.127   -16.397 61.295  1.00 123.88 ? 196 TYR A CD2  1 
ATOM   3132  C CE1  . TYR A 1 196 ? 6.181   -15.044 62.711  1.00 123.31 ? 196 TYR A CE1  1 
ATOM   3133  C CE2  . TYR A 1 196 ? 6.815   -16.874 61.314  1.00 127.60 ? 196 TYR A CE2  1 
ATOM   3134  C CZ   . TYR A 1 196 ? 5.853   -16.189 62.025  1.00 126.56 ? 196 TYR A CZ   1 
ATOM   3135  O OH   . TYR A 1 196 ? 4.562   -16.666 62.040  1.00 129.68 ? 196 TYR A OH   1 
ATOM   3136  H H    . TYR A 1 196 ? 11.786  -13.045 62.285  1.00 133.93 ? 196 TYR A H    1 
ATOM   3137  H HA   . TYR A 1 196 ? 9.888   -13.428 60.387  1.00 138.56 ? 196 TYR A HA   1 
ATOM   3138  H HB2  . TYR A 1 196 ? 10.438  -15.365 61.460  1.00 138.59 ? 196 TYR A HB2  1 
ATOM   3139  H HB3  . TYR A 1 196 ? 10.212  -14.689 62.880  1.00 138.59 ? 196 TYR A HB3  1 
ATOM   3140  H HD1  . TYR A 1 196 ? 7.689   -13.834 63.190  1.00 148.65 ? 196 TYR A HD1  1 
ATOM   3141  H HD2  . TYR A 1 196 ? 8.778   -16.863 60.822  1.00 143.80 ? 196 TYR A HD2  1 
ATOM   3142  H HE1  . TYR A 1 196 ? 5.528   -14.578 63.182  1.00 153.12 ? 196 TYR A HE1  1 
ATOM   3143  H HE2  . TYR A 1 196 ? 6.591   -17.649 60.849  1.00 147.98 ? 196 TYR A HE2  1 
ATOM   3144  H HH   . TYR A 1 196 ? 4.075   -16.164 62.505  1.00 155.61 ? 196 TYR A HH   1 
ATOM   3145  N N    . VAL A 1 197 ? 8.001   -12.112 61.321  1.00 125.03 ? 197 VAL A N    1 
ATOM   3146  C CA   . VAL A 1 197 ? 6.911   -11.338 61.899  1.00 129.92 ? 197 VAL A CA   1 
ATOM   3147  C C    . VAL A 1 197 ? 5.612   -12.106 61.690  1.00 136.30 ? 197 VAL A C    1 
ATOM   3148  O O    . VAL A 1 197 ? 5.483   -12.922 60.773  1.00 135.91 ? 197 VAL A O    1 
ATOM   3149  C CB   . VAL A 1 197 ? 6.812   -9.919  61.299  1.00 131.08 ? 197 VAL A CB   1 
ATOM   3150  C CG1  . VAL A 1 197 ? 8.199   -9.302  61.179  1.00 124.49 ? 197 VAL A CG1  1 
ATOM   3151  C CG2  . VAL A 1 197 ? 6.111   -9.943  59.953  1.00 136.53 ? 197 VAL A CG2  1 
ATOM   3152  H H    . VAL A 1 197 ? 7.828   -12.415 60.535  1.00 150.03 ? 197 VAL A H    1 
ATOM   3153  H HA   . VAL A 1 197 ? 7.057   -11.243 62.853  1.00 155.90 ? 197 VAL A HA   1 
ATOM   3154  H HB   . VAL A 1 197 ? 6.282   -9.365  61.893  1.00 157.30 ? 197 VAL A HB   1 
ATOM   3155  H HG11 . VAL A 1 197 ? 8.116   -8.407  60.814  1.00 149.39 ? 197 VAL A HG11 1 
ATOM   3156  H HG12 . VAL A 1 197 ? 8.605   -9.264  62.059  1.00 149.39 ? 197 VAL A HG12 1 
ATOM   3157  H HG13 . VAL A 1 197 ? 8.739   -9.851  60.589  1.00 149.39 ? 197 VAL A HG13 1 
ATOM   3158  H HG21 . VAL A 1 197 ? 6.090   -9.044  59.591  1.00 163.83 ? 197 VAL A HG21 1 
ATOM   3159  H HG22 . VAL A 1 197 ? 6.598   -10.530 59.354  1.00 163.83 ? 197 VAL A HG22 1 
ATOM   3160  H HG23 . VAL A 1 197 ? 5.206   -10.272 60.074  1.00 163.83 ? 197 VAL A HG23 1 
ATOM   3161  N N    . LYS A 1 198 ? 4.638   -11.831 62.560  1.00 147.93 ? 198 LYS A N    1 
ATOM   3162  C CA   . LYS A 1 198 ? 3.375   -12.562 62.517  1.00 148.36 ? 198 LYS A CA   1 
ATOM   3163  C C    . LYS A 1 198 ? 2.624   -12.291 61.219  1.00 153.74 ? 198 LYS A C    1 
ATOM   3164  O O    . LYS A 1 198 ? 2.132   -13.221 60.569  1.00 149.54 ? 198 LYS A O    1 
ATOM   3165  C CB   . LYS A 1 198 ? 2.520   -12.187 63.732  1.00 151.31 ? 198 LYS A CB   1 
ATOM   3166  C CG   . LYS A 1 198 ? 1.089   -11.779 63.404  1.00 151.96 ? 198 LYS A CG   1 
ATOM   3167  C CD   . LYS A 1 198 ? 0.283   -11.482 64.669  1.00 152.05 ? 198 LYS A CD   1 
ATOM   3168  C CE   . LYS A 1 198 ? 0.724   -10.185 65.329  1.00 151.09 ? 198 LYS A CE   1 
ATOM   3169  N NZ   . LYS A 1 198 ? 1.623   -10.434 66.492  1.00 146.42 ? 198 LYS A NZ   1 
ATOM   3170  H H    . LYS A 1 198 ? 4.685   -11.234 63.177  1.00 177.51 ? 198 LYS A H    1 
ATOM   3171  H HA   . LYS A 1 198 ? 3.560   -13.513 62.558  1.00 178.03 ? 198 LYS A HA   1 
ATOM   3172  H HB2  . LYS A 1 198 ? 2.477   -12.953 64.325  1.00 181.58 ? 198 LYS A HB2  1 
ATOM   3173  H HB3  . LYS A 1 198 ? 2.940   -11.440 64.186  1.00 181.58 ? 198 LYS A HB3  1 
ATOM   3174  H HG2  . LYS A 1 198 ? 1.101   -10.979 62.856  1.00 182.35 ? 198 LYS A HG2  1 
ATOM   3175  H HG3  . LYS A 1 198 ? 0.651   -12.501 62.926  1.00 182.35 ? 198 LYS A HG3  1 
ATOM   3176  H HD2  . LYS A 1 198 ? -0.656  -11.402 64.439  1.00 182.46 ? 198 LYS A HD2  1 
ATOM   3177  H HD3  . LYS A 1 198 ? 0.408   -12.204 65.305  1.00 182.46 ? 198 LYS A HD3  1 
ATOM   3178  H HE2  . LYS A 1 198 ? 1.206   -9.645  64.683  1.00 181.31 ? 198 LYS A HE2  1 
ATOM   3179  H HE3  . LYS A 1 198 ? -0.057  -9.705  65.646  1.00 181.31 ? 198 LYS A HE3  1 
ATOM   3180  H HZ1  . LYS A 1 198 ? 1.199   -10.920 67.105  1.00 175.70 ? 198 LYS A HZ1  1 
ATOM   3181  H HZ2  . LYS A 1 198 ? 2.349   -10.875 66.226  1.00 175.70 ? 198 LYS A HZ2  1 
ATOM   3182  H HZ3  . LYS A 1 198 ? 1.871   -9.661  66.856  1.00 175.70 ? 198 LYS A HZ3  1 
ATOM   3183  N N    . GLU A 1 199 ? 2.522   -11.018 60.827  1.00 150.01 ? 199 GLU A N    1 
ATOM   3184  C CA   . GLU A 1 199 ? 1.734   -10.665 59.650  1.00 148.65 ? 199 GLU A CA   1 
ATOM   3185  C C    . GLU A 1 199 ? 2.259   -11.383 58.410  1.00 145.66 ? 199 GLU A C    1 
ATOM   3186  O O    . GLU A 1 199 ? 1.547   -12.176 57.784  1.00 149.08 ? 199 GLU A O    1 
ATOM   3187  C CB   . GLU A 1 199 ? 1.741   -9.148  59.443  1.00 149.70 ? 199 GLU A CB   1 
ATOM   3188  C CG   . GLU A 1 199 ? 1.441   -8.315  60.692  1.00 152.02 ? 199 GLU A CG   1 
ATOM   3189  C CD   . GLU A 1 199 ? 0.106   -8.642  61.351  1.00 153.01 ? 199 GLU A CD   1 
ATOM   3190  O OE1  . GLU A 1 199 ? -0.298  -9.821  61.363  1.00 152.88 ? 199 GLU A OE1  1 
ATOM   3191  O OE2  . GLU A 1 199 ? -0.541  -7.712  61.876  1.00 153.60 ? 199 GLU A OE2  1 
ATOM   3192  H H    . GLU A 1 199 ? 2.895   -10.351 61.221  1.00 180.01 ? 199 GLU A H    1 
ATOM   3193  H HA   . GLU A 1 199 ? 0.816   -10.940 59.797  1.00 178.38 ? 199 GLU A HA   1 
ATOM   3194  H HB2  . GLU A 1 199 ? 2.620   -8.887  59.125  1.00 179.64 ? 199 GLU A HB2  1 
ATOM   3195  H HB3  . GLU A 1 199 ? 1.069   -8.927  58.779  1.00 179.64 ? 199 GLU A HB3  1 
ATOM   3196  H HG2  . GLU A 1 199 ? 2.139   -8.473  61.347  1.00 182.43 ? 199 GLU A HG2  1 
ATOM   3197  H HG3  . GLU A 1 199 ? 1.425   -7.377  60.444  1.00 182.43 ? 199 GLU A HG3  1 
ATOM   3198  N N    . VAL A 1 200 ? 3.517   -11.118 58.044  1.00 145.37 ? 200 VAL A N    1 
ATOM   3199  C CA   . VAL A 1 200 ? 4.117   -11.790 56.894  1.00 138.83 ? 200 VAL A CA   1 
ATOM   3200  C C    . VAL A 1 200 ? 4.023   -13.301 57.038  1.00 135.24 ? 200 VAL A C    1 
ATOM   3201  O O    . VAL A 1 200 ? 3.883   -14.023 56.042  1.00 135.37 ? 200 VAL A O    1 
ATOM   3202  C CB   . VAL A 1 200 ? 5.585   -11.339 56.721  1.00 135.67 ? 200 VAL A CB   1 
ATOM   3203  C CG1  . VAL A 1 200 ? 6.257   -12.123 55.599  1.00 131.34 ? 200 VAL A CG1  1 
ATOM   3204  C CG2  . VAL A 1 200 ? 5.656   -9.845  56.457  1.00 139.91 ? 200 VAL A CG2  1 
ATOM   3205  H H    . VAL A 1 200 ? 4.036   -10.559 58.441  1.00 174.44 ? 200 VAL A H    1 
ATOM   3206  H HA   . VAL A 1 200 ? 3.625   -11.532 56.099  1.00 166.60 ? 200 VAL A HA   1 
ATOM   3207  H HB   . VAL A 1 200 ? 6.068   -11.521 57.542  1.00 162.81 ? 200 VAL A HB   1 
ATOM   3208  H HG11 . VAL A 1 200 ? 7.080   -11.673 55.348  1.00 157.61 ? 200 VAL A HG11 1 
ATOM   3209  H HG12 . VAL A 1 200 ? 6.453   -13.019 55.913  1.00 157.61 ? 200 VAL A HG12 1 
ATOM   3210  H HG13 . VAL A 1 200 ? 5.657   -12.162 54.837  1.00 157.61 ? 200 VAL A HG13 1 
ATOM   3211  H HG21 . VAL A 1 200 ? 6.580   -9.595  56.299  1.00 167.89 ? 200 VAL A HG21 1 
ATOM   3212  H HG22 . VAL A 1 200 ? 5.119   -9.636  55.677  1.00 167.89 ? 200 VAL A HG22 1 
ATOM   3213  H HG23 . VAL A 1 200 ? 5.313   -9.371  57.231  1.00 167.89 ? 200 VAL A HG23 1 
ATOM   3214  N N    . GLY A 1 201 ? 4.096   -13.808 58.265  1.00 138.11 ? 201 GLY A N    1 
ATOM   3215  C CA   . GLY A 1 201 ? 4.063   -15.244 58.471  1.00 133.26 ? 201 GLY A CA   1 
ATOM   3216  C C    . GLY A 1 201 ? 5.198   -15.979 57.798  1.00 127.65 ? 201 GLY A C    1 
ATOM   3217  O O    . GLY A 1 201 ? 5.030   -17.135 57.396  1.00 123.12 ? 201 GLY A O    1 
ATOM   3218  H H    . GLY A 1 201 ? 4.164   -13.343 58.986  1.00 165.73 ? 201 GLY A H    1 
ATOM   3219  H HA2  . GLY A 1 201 ? 4.108   -15.427 59.423  1.00 159.90 ? 201 GLY A HA2  1 
ATOM   3220  H HA3  . GLY A 1 201 ? 3.228   -15.594 58.121  1.00 159.90 ? 201 GLY A HA3  1 
ATOM   3221  N N    . SER A 1 202 ? 6.355   -15.337 57.664  1.00 120.44 ? 202 SER A N    1 
ATOM   3222  C CA   . SER A 1 202 ? 7.496   -15.941 56.993  1.00 120.47 ? 202 SER A CA   1 
ATOM   3223  C C    . SER A 1 202 ? 8.744   -15.142 57.339  1.00 119.28 ? 202 SER A C    1 
ATOM   3224  O O    . SER A 1 202 ? 8.665   -14.010 57.824  1.00 119.08 ? 202 SER A O    1 
ATOM   3225  C CB   . SER A 1 202 ? 7.293   -15.993 55.474  1.00 119.35 ? 202 SER A CB   1 
ATOM   3226  O OG   . SER A 1 202 ? 6.711   -17.222 55.075  1.00 117.62 ? 202 SER A OG   1 
ATOM   3227  H H    . SER A 1 202 ? 6.504   -14.542 57.956  1.00 144.54 ? 202 SER A H    1 
ATOM   3228  H HA   . SER A 1 202 ? 7.615   -16.849 57.315  1.00 144.56 ? 202 SER A HA   1 
ATOM   3229  H HB2  . SER A 1 202 ? 6.705   -15.267 55.211  1.00 143.22 ? 202 SER A HB2  1 
ATOM   3230  H HB3  . SER A 1 202 ? 8.154   -15.897 55.038  1.00 143.22 ? 202 SER A HB3  1 
ATOM   3231  H HG   . SER A 1 202 ? 5.966   -17.323 55.450  1.00 141.15 ? 202 SER A HG   1 
ATOM   3232  N N    . GLY A 1 203 ? 9.905   -15.751 57.072  1.00 116.22 ? 203 GLY A N    1 
ATOM   3233  C CA   . GLY A 1 203 ? 11.167  -15.138 57.418  1.00 114.28 ? 203 GLY A CA   1 
ATOM   3234  C C    . GLY A 1 203 ? 11.666  -14.159 56.374  1.00 107.69 ? 203 GLY A C    1 
ATOM   3235  O O    . GLY A 1 203 ? 11.191  -14.117 55.240  1.00 112.59 ? 203 GLY A O    1 
ATOM   3236  H H    . GLY A 1 203 ? 9.977   -16.519 56.690  1.00 139.46 ? 203 GLY A H    1 
ATOM   3237  H HA2  . GLY A 1 203 ? 11.069  -14.661 58.257  1.00 137.14 ? 203 GLY A HA2  1 
ATOM   3238  H HA3  . GLY A 1 203 ? 11.837  -15.831 57.525  1.00 137.14 ? 203 GLY A HA3  1 
ATOM   3239  N N    . VAL A 1 204 ? 12.647  -13.354 56.780  1.00 105.14 ? 204 VAL A N    1 
ATOM   3240  C CA   . VAL A 1 204 ? 13.230  -12.344 55.903  1.00 103.33 ? 204 VAL A CA   1 
ATOM   3241  C C    . VAL A 1 204 ? 14.678  -12.090 56.305  1.00 100.90 ? 204 VAL A C    1 
ATOM   3242  O O    . VAL A 1 204 ? 14.947  -11.514 57.366  1.00 97.98  ? 204 VAL A O    1 
ATOM   3243  C CB   . VAL A 1 204 ? 12.418  -11.035 55.946  1.00 100.46 ? 204 VAL A CB   1 
ATOM   3244  C CG1  . VAL A 1 204 ? 13.204  -9.901  55.304  1.00 95.19  ? 204 VAL A CG1  1 
ATOM   3245  C CG2  . VAL A 1 204 ? 11.067  -11.208 55.268  1.00 103.65 ? 204 VAL A CG2  1 
ATOM   3246  H H    . VAL A 1 204 ? 12.995  -13.375 57.566  1.00 126.17 ? 204 VAL A H    1 
ATOM   3247  H HA   . VAL A 1 204 ? 13.222  -12.684 54.995  1.00 123.99 ? 204 VAL A HA   1 
ATOM   3248  H HB   . VAL A 1 204 ? 12.254  -10.802 56.873  1.00 120.55 ? 204 VAL A HB   1 
ATOM   3249  H HG11 . VAL A 1 204 ? 12.597  -9.174  55.095  1.00 114.23 ? 204 VAL A HG11 1 
ATOM   3250  H HG12 . VAL A 1 204 ? 13.884  -9.596  55.925  1.00 114.23 ? 204 VAL A HG12 1 
ATOM   3251  H HG13 . VAL A 1 204 ? 13.621  -10.227 54.491  1.00 114.23 ? 204 VAL A HG13 1 
ATOM   3252  H HG21 . VAL A 1 204 ? 10.649  -10.339 55.169  1.00 124.38 ? 204 VAL A HG21 1 
ATOM   3253  H HG22 . VAL A 1 204 ? 11.201  -11.612 54.396  1.00 124.38 ? 204 VAL A HG22 1 
ATOM   3254  H HG23 . VAL A 1 204 ? 10.510  -11.783 55.816  1.00 124.38 ? 204 VAL A HG23 1 
ATOM   3255  N N    . TYR A 1 205 ? 15.620  -12.513 55.463  1.00 96.48  ? 205 TYR A N    1 
ATOM   3256  C CA   . TYR A 1 205 ? 17.032  -12.202 55.668  1.00 93.84  ? 205 TYR A CA   1 
ATOM   3257  C C    . TYR A 1 205 ? 17.283  -10.788 55.155  1.00 91.09  ? 205 TYR A C    1 
ATOM   3258  O O    . TYR A 1 205 ? 17.181  -10.530 53.951  1.00 94.02  ? 205 TYR A O    1 
ATOM   3259  C CB   . TYR A 1 205 ? 17.918  -13.216 54.951  1.00 93.32  ? 205 TYR A CB   1 
ATOM   3260  C CG   . TYR A 1 205 ? 17.938  -14.587 55.592  1.00 96.11  ? 205 TYR A CG   1 
ATOM   3261  C CD1  . TYR A 1 205 ? 16.960  -15.526 55.295  1.00 97.22  ? 205 TYR A CD1  1 
ATOM   3262  C CD2  . TYR A 1 205 ? 18.942  -14.946 56.485  1.00 95.87  ? 205 TYR A CD2  1 
ATOM   3263  C CE1  . TYR A 1 205 ? 16.974  -16.784 55.872  1.00 98.19  ? 205 TYR A CE1  1 
ATOM   3264  C CE2  . TYR A 1 205 ? 18.966  -16.203 57.067  1.00 98.48  ? 205 TYR A CE2  1 
ATOM   3265  C CZ   . TYR A 1 205 ? 17.978  -17.118 56.755  1.00 99.85  ? 205 TYR A CZ   1 
ATOM   3266  O OH   . TYR A 1 205 ? 17.992  -18.370 57.331  1.00 101.20 ? 205 TYR A OH   1 
ATOM   3267  H H    . TYR A 1 205 ? 15.464  -12.985 54.761  1.00 115.77 ? 205 TYR A H    1 
ATOM   3268  H HA   . TYR A 1 205 ? 17.244  -12.241 56.613  1.00 112.61 ? 205 TYR A HA   1 
ATOM   3269  H HB2  . TYR A 1 205 ? 17.595  -13.321 54.043  1.00 111.99 ? 205 TYR A HB2  1 
ATOM   3270  H HB3  . TYR A 1 205 ? 18.828  -12.881 54.944  1.00 111.99 ? 205 TYR A HB3  1 
ATOM   3271  H HD1  . TYR A 1 205 ? 16.282  -15.305 54.698  1.00 116.66 ? 205 TYR A HD1  1 
ATOM   3272  H HD2  . TYR A 1 205 ? 19.608  -14.333 56.695  1.00 115.04 ? 205 TYR A HD2  1 
ATOM   3273  H HE1  . TYR A 1 205 ? 16.310  -17.401 55.664  1.00 117.83 ? 205 TYR A HE1  1 
ATOM   3274  H HE2  . TYR A 1 205 ? 19.642  -16.430 57.663  1.00 118.18 ? 205 TYR A HE2  1 
ATOM   3275  H HH   . TYR A 1 205 ? 17.331  -18.816 57.066  1.00 121.44 ? 205 TYR A HH   1 
ATOM   3276  N N    . GLU A 1 206 ? 17.609  -9.872  56.059  1.00 89.78  ? 206 GLU A N    1 
ATOM   3277  C CA   . GLU A 1 206 ? 17.726  -8.463  55.717  1.00 85.63  ? 206 GLU A CA   1 
ATOM   3278  C C    . GLU A 1 206 ? 19.132  -8.132  55.228  1.00 82.88  ? 206 GLU A C    1 
ATOM   3279  O O    . GLU A 1 206 ? 20.085  -8.887  55.434  1.00 80.21  ? 206 GLU A O    1 
ATOM   3280  C CB   . GLU A 1 206 ? 17.383  -7.589  56.925  1.00 91.11  ? 206 GLU A CB   1 
ATOM   3281  C CG   . GLU A 1 206 ? 15.978  -7.793  57.474  1.00 95.31  ? 206 GLU A CG   1 
ATOM   3282  C CD   . GLU A 1 206 ? 14.965  -6.872  56.821  1.00 94.02  ? 206 GLU A CD   1 
ATOM   3283  O OE1  . GLU A 1 206 ? 15.323  -6.209  55.825  1.00 94.21  ? 206 GLU A OE1  1 
ATOM   3284  O OE2  . GLU A 1 206 ? 13.813  -6.812  57.301  1.00 97.53  ? 206 GLU A OE2  1 
ATOM   3285  H H    . GLU A 1 206 ? 17.768  -10.044 56.887  1.00 107.74 ? 206 GLU A H    1 
ATOM   3286  H HA   . GLU A 1 206 ? 17.103  -8.261  55.001  1.00 102.76 ? 206 GLU A HA   1 
ATOM   3287  H HB2  . GLU A 1 206 ? 18.009  -7.789  57.639  1.00 109.32 ? 206 GLU A HB2  1 
ATOM   3288  H HB3  . GLU A 1 206 ? 17.464  -6.657  56.666  1.00 109.32 ? 206 GLU A HB3  1 
ATOM   3289  H HG2  . GLU A 1 206 ? 15.704  -8.709  57.310  1.00 114.38 ? 206 GLU A HG2  1 
ATOM   3290  H HG3  . GLU A 1 206 ? 15.980  -7.613  58.427  1.00 114.38 ? 206 GLU A HG3  1 
ATOM   3291  N N    . ASN A 1 207 ? 19.248  -6.983  54.561  1.00 85.48  ? 207 ASN A N    1 
ATOM   3292  C CA   . ASN A 1 207 ? 20.555  -6.496  54.138  1.00 81.40  ? 207 ASN A CA   1 
ATOM   3293  C C    . ASN A 1 207 ? 21.334  -5.919  55.308  1.00 81.49  ? 207 ASN A C    1 
ATOM   3294  O O    . ASN A 1 207 ? 22.570  -5.930  55.290  1.00 81.79  ? 207 ASN A O    1 
ATOM   3295  C CB   . ASN A 1 207 ? 20.397  -5.442  53.042  1.00 82.35  ? 207 ASN A CB   1 
ATOM   3296  C CG   . ASN A 1 207 ? 20.053  -6.053  51.696  1.00 87.11  ? 207 ASN A CG   1 
ATOM   3297  O OD1  . ASN A 1 207 ? 20.374  -7.214  51.427  1.00 85.13  ? 207 ASN A OD1  1 
ATOM   3298  N ND2  . ASN A 1 207 ? 19.397  -5.275  50.840  1.00 88.31  ? 207 ASN A ND2  1 
ATOM   3299  H H    . ASN A 1 207 ? 18.591  -6.473  54.344  1.00 102.58 ? 207 ASN A H    1 
ATOM   3300  H HA   . ASN A 1 207 ? 21.062  -7.234  53.764  1.00 97.68  ? 207 ASN A HA   1 
ATOM   3301  H HB2  . ASN A 1 207 ? 19.683  -4.833  53.287  1.00 98.82  ? 207 ASN A HB2  1 
ATOM   3302  H HB3  . ASN A 1 207 ? 21.230  -4.955  52.947  1.00 98.82  ? 207 ASN A HB3  1 
ATOM   3303  H HD21 . ASN A 1 207 ? 19.190  -4.470  51.062  1.00 105.97 ? 207 ASN A HD21 1 
ATOM   3304  H HD22 . ASN A 1 207 ? 19.180  -5.576  50.064  1.00 105.97 ? 207 ASN A HD22 1 
ATOM   3305  N N    . SER A 1 208 ? 20.630  -5.419  56.320  1.00 77.11  ? 208 SER A N    1 
ATOM   3306  C CA   . SER A 1 208 ? 21.232  -4.917  57.546  1.00 77.02  ? 208 SER A CA   1 
ATOM   3307  C C    . SER A 1 208 ? 20.112  -4.664  58.543  1.00 78.20  ? 208 SER A C    1 
ATOM   3308  O O    . SER A 1 208 ? 18.985  -4.334  58.156  1.00 80.75  ? 208 SER A O    1 
ATOM   3309  C CB   . SER A 1 208 ? 22.041  -3.641  57.297  1.00 75.01  ? 208 SER A CB   1 
ATOM   3310  O OG   . SER A 1 208 ? 21.229  -2.487  57.393  1.00 76.18  ? 208 SER A OG   1 
ATOM   3311  H H    . SER A 1 208 ? 19.772  -5.358  56.319  1.00 92.54  ? 208 SER A H    1 
ATOM   3312  H HA   . SER A 1 208 ? 21.837  -5.578  57.918  1.00 92.43  ? 208 SER A HA   1 
ATOM   3313  H HB2  . SER A 1 208 ? 22.748  -3.584  57.960  1.00 90.01  ? 208 SER A HB2  1 
ATOM   3314  H HB3  . SER A 1 208 ? 22.424  -3.682  56.407  1.00 90.01  ? 208 SER A HB3  1 
ATOM   3315  H HG   . SER A 1 208 ? 21.691  -1.799  57.259  1.00 91.42  ? 208 SER A HG   1 
ATOM   3316  N N    . CYS A 1 209 ? 20.429  -4.835  59.826  1.00 76.01  ? 209 CYS A N    1 
ATOM   3317  C CA   . CYS A 1 209 ? 19.451  -4.709  60.903  1.00 78.11  ? 209 CYS A CA   1 
ATOM   3318  C C    . CYS A 1 209 ? 20.058  -3.884  62.029  1.00 76.89  ? 209 CYS A C    1 
ATOM   3319  O O    . CYS A 1 209 ? 20.934  -4.369  62.756  1.00 76.23  ? 209 CYS A O    1 
ATOM   3320  C CB   . CYS A 1 209 ? 19.020  -6.082  61.421  1.00 77.37  ? 209 CYS A CB   1 
ATOM   3321  S SG   . CYS A 1 209 ? 17.691  -6.007  62.631  1.00 78.50  ? 209 CYS A SG   1 
ATOM   3322  H H    . CYS A 1 209 ? 21.221  -5.027  60.101  1.00 91.21  ? 209 CYS A H    1 
ATOM   3323  H HA   . CYS A 1 209 ? 18.673  -4.239  60.565  1.00 93.73  ? 209 CYS A HA   1 
ATOM   3324  H HB2  . CYS A 1 209 ? 18.711  -6.616  60.673  1.00 92.84  ? 209 CYS A HB2  1 
ATOM   3325  H HB3  . CYS A 1 209 ? 19.781  -6.511  61.843  1.00 92.84  ? 209 CYS A HB3  1 
ATOM   3326  H HG   . CYS A 1 209 ? 16.723  -5.516  62.118  1.00 94.20  ? 209 CYS A HG   1 
ATOM   3327  N N    . ALA A 1 210 ? 19.574  -2.650  62.187  1.00 76.84  ? 210 ALA A N    1 
ATOM   3328  C CA   . ALA A 1 210 ? 20.123  -1.761  63.206  1.00 75.59  ? 210 ALA A CA   1 
ATOM   3329  C C    . ALA A 1 210 ? 19.848  -2.287  64.610  1.00 75.67  ? 210 ALA A C    1 
ATOM   3330  O O    . ALA A 1 210 ? 20.771  -2.422  65.424  1.00 75.40  ? 210 ALA A O    1 
ATOM   3331  C CB   . ALA A 1 210 ? 19.546  -0.357  63.030  1.00 73.75  ? 210 ALA A CB   1 
ATOM   3332  H H    . ALA A 1 210 ? 18.936  -2.309  61.723  1.00 92.20  ? 210 ALA A H    1 
ATOM   3333  H HA   . ALA A 1 210 ? 21.085  -1.711  63.093  1.00 90.70  ? 210 ALA A HA   1 
ATOM   3334  H HB1  . ALA A 1 210 ? 19.961  0.238   63.675  1.00 88.50  ? 210 ALA A HB1  1 
ATOM   3335  H HB2  . ALA A 1 210 ? 19.732  -0.049  62.129  1.00 88.50  ? 210 ALA A HB2  1 
ATOM   3336  H HB3  . ALA A 1 210 ? 18.588  -0.388  63.178  1.00 88.50  ? 210 ALA A HB3  1 
ATOM   3337  N N    . SER A 1 211 ? 18.582  -2.587  64.915  1.00 76.65  ? 211 SER A N    1 
ATOM   3338  C CA   . SER A 1 211 ? 18.246  -3.087  66.245  1.00 77.00  ? 211 SER A CA   1 
ATOM   3339  C C    . SER A 1 211 ? 18.968  -4.397  66.534  1.00 78.22  ? 211 SER A C    1 
ATOM   3340  O O    . SER A 1 211 ? 19.419  -4.633  67.661  1.00 80.22  ? 211 SER A O    1 
ATOM   3341  C CB   . SER A 1 211 ? 16.733  -3.269  66.374  1.00 77.04  ? 211 SER A CB   1 
ATOM   3342  O OG   . SER A 1 211 ? 16.248  -4.246  65.472  1.00 76.61  ? 211 SER A OG   1 
ATOM   3343  H H    . SER A 1 211 ? 17.914  -2.511  64.380  1.00 91.98  ? 211 SER A H    1 
ATOM   3344  H HA   . SER A 1 211 ? 18.526  -2.434  66.906  1.00 92.40  ? 211 SER A HA   1 
ATOM   3345  H HB2  . SER A 1 211 ? 16.527  -3.550  67.279  1.00 92.45  ? 211 SER A HB2  1 
ATOM   3346  H HB3  . SER A 1 211 ? 16.299  -2.423  66.182  1.00 92.45  ? 211 SER A HB3  1 
ATOM   3347  H HG   . SER A 1 211 ? 16.710  -4.945  65.529  1.00 91.94  ? 211 SER A HG   1 
ATOM   3348  N N    . GLY A 1 212 ? 19.082  -5.266  65.527  1.00 78.70  ? 212 GLY A N    1 
ATOM   3349  C CA   . GLY A 1 212 ? 19.799  -6.513  65.724  1.00 77.86  ? 212 GLY A CA   1 
ATOM   3350  C C    . GLY A 1 212 ? 21.260  -6.293  66.067  1.00 78.17  ? 212 GLY A C    1 
ATOM   3351  O O    . GLY A 1 212 ? 21.845  -7.048  66.849  1.00 80.79  ? 212 GLY A O    1 
ATOM   3352  H H    . GLY A 1 212 ? 18.758  -5.156  64.738  1.00 94.43  ? 212 GLY A H    1 
ATOM   3353  H HA2  . GLY A 1 212 ? 19.387  -7.009  66.449  1.00 93.42  ? 212 GLY A HA2  1 
ATOM   3354  H HA3  . GLY A 1 212 ? 19.753  -7.042  64.913  1.00 93.42  ? 212 GLY A HA3  1 
ATOM   3355  N N    . THR A 1 213 ? 21.872  -5.256  65.489  1.00 77.76  ? 213 THR A N    1 
ATOM   3356  C CA   . THR A 1 213 ? 23.267  -4.966  65.800  1.00 79.87  ? 213 THR A CA   1 
ATOM   3357  C C    . THR A 1 213 ? 23.432  -4.527  67.249  1.00 78.13  ? 213 THR A C    1 
ATOM   3358  O O    . THR A 1 213 ? 24.465  -4.809  67.867  1.00 79.93  ? 213 THR A O    1 
ATOM   3359  C CB   . THR A 1 213 ? 23.806  -3.890  64.855  1.00 78.56  ? 213 THR A CB   1 
ATOM   3360  O OG1  . THR A 1 213 ? 23.332  -4.140  63.525  1.00 73.95  ? 213 THR A OG1  1 
ATOM   3361  C CG2  . THR A 1 213 ? 25.331  -3.885  64.845  1.00 77.85  ? 213 THR A CG2  1 
ATOM   3362  H H    . THR A 1 213 ? 21.507  -4.718  64.927  1.00 93.31  ? 213 THR A H    1 
ATOM   3363  H HA   . THR A 1 213 ? 23.793  -5.770  65.664  1.00 95.84  ? 213 THR A HA   1 
ATOM   3364  H HB   . THR A 1 213 ? 23.500  -3.020  65.156  1.00 94.27  ? 213 THR A HB   1 
ATOM   3365  H HG1  . THR A 1 213 ? 23.539  -3.501  63.021  1.00 88.74  ? 213 THR A HG1  1 
ATOM   3366  H HG21 . THR A 1 213 ? 25.657  -3.206  64.234  1.00 93.42  ? 213 THR A HG21 1 
ATOM   3367  H HG22 . THR A 1 213 ? 25.667  -3.695  65.735  1.00 93.42  ? 213 THR A HG22 1 
ATOM   3368  H HG23 . THR A 1 213 ? 25.663  -4.751  64.561  1.00 93.42  ? 213 THR A HG23 1 
ATOM   3369  N N    . THR A 1 214 ? 22.434  -3.835  67.805  1.00 80.39  ? 214 THR A N    1 
ATOM   3370  C CA   . THR A 1 214 ? 22.493  -3.460  69.214  1.00 79.17  ? 214 THR A CA   1 
ATOM   3371  C C    . THR A 1 214 ? 22.383  -4.690  70.107  1.00 78.33  ? 214 THR A C    1 
ATOM   3372  O O    . THR A 1 214 ? 23.130  -4.825  71.085  1.00 81.70  ? 214 THR A O    1 
ATOM   3373  C CB   . THR A 1 214 ? 21.390  -2.455  69.547  1.00 78.31  ? 214 THR A CB   1 
ATOM   3374  O OG1  . THR A 1 214 ? 20.110  -3.089  69.432  1.00 76.17  ? 214 THR A OG1  1 
ATOM   3375  C CG2  . THR A 1 214 ? 21.452  -1.257  68.606  1.00 76.34  ? 214 THR A CG2  1 
ATOM   3376  H H    . THR A 1 214 ? 21.724  -3.575  67.393  1.00 96.46  ? 214 THR A H    1 
ATOM   3377  H HA   . THR A 1 214 ? 23.345  -3.030  69.388  1.00 95.00  ? 214 THR A HA   1 
ATOM   3378  H HB   . THR A 1 214 ? 21.508  -2.134  70.454  1.00 93.98  ? 214 THR A HB   1 
ATOM   3379  H HG1  . THR A 1 214 ? 19.990  -3.356  68.644  1.00 91.40  ? 214 THR A HG1  1 
ATOM   3380  H HG21 . THR A 1 214 ? 20.822  -0.578  68.891  1.00 91.60  ? 214 THR A HG21 1 
ATOM   3381  H HG22 . THR A 1 214 ? 22.346  -0.879  68.609  1.00 91.60  ? 214 THR A HG22 1 
ATOM   3382  H HG23 . THR A 1 214 ? 21.231  -1.533  67.703  1.00 91.60  ? 214 THR A HG23 1 
ATOM   3383  N N    . ALA A 1 215 ? 21.458  -5.598  69.788  1.00 79.34  ? 215 ALA A N    1 
ATOM   3384  C CA   . ALA A 1 215 ? 21.412  -6.882  70.483  1.00 82.45  ? 215 ALA A CA   1 
ATOM   3385  C C    . ALA A 1 215 ? 22.778  -7.557  70.442  1.00 82.53  ? 215 ALA A C    1 
ATOM   3386  O O    . ALA A 1 215 ? 23.339  -7.928  71.479  1.00 85.54  ? 215 ALA A O    1 
ATOM   3387  C CB   . ALA A 1 215 ? 20.346  -7.780  69.851  1.00 79.83  ? 215 ALA A CB   1 
ATOM   3388  H H    . ALA A 1 215 ? 20.855  -5.496  69.183  1.00 95.21  ? 215 ALA A H    1 
ATOM   3389  H HA   . ALA A 1 215 ? 21.167  -6.738  71.410  1.00 98.94  ? 215 ALA A HA   1 
ATOM   3390  H HB1  . ALA A 1 215 ? 20.357  -8.643  70.295  1.00 95.79  ? 215 ALA A HB1  1 
ATOM   3391  H HB2  . ALA A 1 215 ? 19.477  -7.363  69.960  1.00 95.79  ? 215 ALA A HB2  1 
ATOM   3392  H HB3  . ALA A 1 215 ? 20.545  -7.890  68.908  1.00 95.79  ? 215 ALA A HB3  1 
ATOM   3393  N N    . LEU A 1 216 ? 23.326  -7.723  69.238  1.00 82.25  ? 216 LEU A N    1 
ATOM   3394  C CA   . LEU A 1 216 ? 24.705  -8.176  69.092  1.00 83.34  ? 216 LEU A CA   1 
ATOM   3395  C C    . LEU A 1 216 ? 25.645  -7.343  69.956  1.00 87.25  ? 216 LEU A C    1 
ATOM   3396  O O    . LEU A 1 216 ? 26.494  -7.883  70.674  1.00 89.47  ? 216 LEU A O    1 
ATOM   3397  C CB   . LEU A 1 216 ? 25.103  -8.100  67.618  1.00 92.66  ? 216 LEU A CB   1 
ATOM   3398  C CG   . LEU A 1 216 ? 26.251  -8.954  67.082  1.00 93.66  ? 216 LEU A CG   1 
ATOM   3399  C CD1  . LEU A 1 216 ? 27.571  -8.475  67.675  1.00 97.76  ? 216 LEU A CD1  1 
ATOM   3400  C CD2  . LEU A 1 216 ? 26.031  -10.429 67.368  1.00 91.83  ? 216 LEU A CD2  1 
ATOM   3401  H H    . LEU A 1 216 ? 22.922  -7.579  68.492  1.00 98.70  ? 216 LEU A H    1 
ATOM   3402  H HA   . LEU A 1 216 ? 24.780  -9.099  69.381  1.00 100.01 ? 216 LEU A HA   1 
ATOM   3403  H HB2  . LEU A 1 216 ? 24.321  -8.345  67.099  1.00 111.19 ? 216 LEU A HB2  1 
ATOM   3404  H HB3  . LEU A 1 216 ? 25.346  -7.179  67.436  1.00 111.19 ? 216 LEU A HB3  1 
ATOM   3405  H HG   . LEU A 1 216 ? 26.289  -8.858  66.118  1.00 112.39 ? 216 LEU A HG   1 
ATOM   3406  H HD11 . LEU A 1 216 ? 28.291  -9.025  67.328  1.00 117.31 ? 216 LEU A HD11 1 
ATOM   3407  H HD12 . LEU A 1 216 ? 27.712  -7.549  67.425  1.00 117.31 ? 216 LEU A HD12 1 
ATOM   3408  H HD13 . LEU A 1 216 ? 27.531  -8.555  68.641  1.00 117.31 ? 216 LEU A HD13 1 
ATOM   3409  H HD21 . LEU A 1 216 ? 26.780  -10.934 67.013  1.00 110.19 ? 216 LEU A HD21 1 
ATOM   3410  H HD22 . LEU A 1 216 ? 25.969  -10.560 68.327  1.00 110.19 ? 216 LEU A HD22 1 
ATOM   3411  H HD23 . LEU A 1 216 ? 25.208  -10.715 66.941  1.00 110.19 ? 216 LEU A HD23 1 
ATOM   3412  N N    . GLY A 1 217 ? 25.489  -6.019  69.915  1.00 85.26  ? 217 GLY A N    1 
ATOM   3413  C CA   . GLY A 1 217 ? 26.382  -5.157  70.674  1.00 86.73  ? 217 GLY A CA   1 
ATOM   3414  C C    . GLY A 1 217 ? 26.257  -5.360  72.170  1.00 86.74  ? 217 GLY A C    1 
ATOM   3415  O O    . GLY A 1 217 ? 27.251  -5.586  72.865  1.00 89.40  ? 217 GLY A O    1 
ATOM   3416  H H    . GLY A 1 217 ? 24.885  -5.605  69.464  1.00 102.31 ? 217 GLY A H    1 
ATOM   3417  H HA2  . GLY A 1 217 ? 27.299  -5.340  70.417  1.00 104.08 ? 217 GLY A HA2  1 
ATOM   3418  H HA3  . GLY A 1 217 ? 26.178  -4.230  70.474  1.00 104.08 ? 217 GLY A HA3  1 
ATOM   3419  N N    . TYR A 1 218 ? 25.030  -5.271  72.690  1.00 84.98  ? 218 TYR A N    1 
ATOM   3420  C CA   . TYR A 1 218 ? 24.813  -5.520  74.110  1.00 88.03  ? 218 TYR A CA   1 
ATOM   3421  C C    . TYR A 1 218 ? 25.389  -6.869  74.519  1.00 90.53  ? 218 TYR A C    1 
ATOM   3422  O O    . TYR A 1 218 ? 25.980  -7.007  75.596  1.00 90.76  ? 218 TYR A O    1 
ATOM   3423  C CB   . TYR A 1 218 ? 23.318  -5.477  74.437  1.00 85.81  ? 218 TYR A CB   1 
ATOM   3424  C CG   . TYR A 1 218 ? 22.681  -4.110  74.356  1.00 83.09  ? 218 TYR A CG   1 
ATOM   3425  C CD1  . TYR A 1 218 ? 23.162  -3.046  75.111  1.00 84.08  ? 218 TYR A CD1  1 
ATOM   3426  C CD2  . TYR A 1 218 ? 21.585  -3.887  73.533  1.00 79.79  ? 218 TYR A CD2  1 
ATOM   3427  C CE1  . TYR A 1 218 ? 22.572  -1.797  75.039  1.00 82.24  ? 218 TYR A CE1  1 
ATOM   3428  C CE2  . TYR A 1 218 ? 20.990  -2.648  73.456  1.00 78.82  ? 218 TYR A CE2  1 
ATOM   3429  C CZ   . TYR A 1 218 ? 21.485  -1.608  74.209  1.00 81.32  ? 218 TYR A CZ   1 
ATOM   3430  O OH   . TYR A 1 218 ? 20.885  -0.375  74.122  1.00 84.14  ? 218 TYR A OH   1 
ATOM   3431  H H    . TYR A 1 218 ? 24.320  -5.072  72.247  1.00 101.98 ? 218 TYR A H    1 
ATOM   3432  H HA   . TYR A 1 218 ? 25.254  -4.820  74.618  1.00 105.64 ? 218 TYR A HA   1 
ATOM   3433  H HB2  . TYR A 1 218 ? 22.851  -6.052  73.810  1.00 102.97 ? 218 TYR A HB2  1 
ATOM   3434  H HB3  . TYR A 1 218 ? 23.193  -5.803  75.342  1.00 102.97 ? 218 TYR A HB3  1 
ATOM   3435  H HD1  . TYR A 1 218 ? 23.892  -3.176  75.672  1.00 100.90 ? 218 TYR A HD1  1 
ATOM   3436  H HD2  . TYR A 1 218 ? 21.246  -4.589  73.025  1.00 95.75  ? 218 TYR A HD2  1 
ATOM   3437  H HE1  . TYR A 1 218 ? 22.904  -1.091  75.545  1.00 98.68  ? 218 TYR A HE1  1 
ATOM   3438  H HE2  . TYR A 1 218 ? 20.258  -2.515  72.898  1.00 94.59  ? 218 TYR A HE2  1 
ATOM   3439  H HH   . TYR A 1 218 ? 20.252  -0.401  73.570  1.00 100.97 ? 218 TYR A HH   1 
ATOM   3440  N N    . TYR A 1 219 ? 25.226  -7.877  73.663  1.00 91.02  ? 219 TYR A N    1 
ATOM   3441  C CA   . TYR A 1 219 ? 25.644  -9.233  74.008  1.00 92.26  ? 219 TYR A CA   1 
ATOM   3442  C C    . TYR A 1 219 ? 27.160  -9.359  74.028  1.00 94.93  ? 219 TYR A C    1 
ATOM   3443  O O    . TYR A 1 219 ? 27.717  -10.030 74.902  1.00 98.84  ? 219 TYR A O    1 
ATOM   3444  C CB   . TYR A 1 219 ? 25.013  -10.212 73.016  1.00 93.25  ? 219 TYR A CB   1 
ATOM   3445  C CG   . TYR A 1 219 ? 25.667  -11.566 72.937  1.00 95.40  ? 219 TYR A CG   1 
ATOM   3446  C CD1  . TYR A 1 219 ? 25.417  -12.531 73.895  1.00 98.63  ? 219 TYR A CD1  1 
ATOM   3447  C CD2  . TYR A 1 219 ? 26.517  -11.886 71.885  1.00 96.25  ? 219 TYR A CD2  1 
ATOM   3448  C CE1  . TYR A 1 219 ? 26.009  -13.771 73.822  1.00 102.41 ? 219 TYR A CE1  1 
ATOM   3449  C CE2  . TYR A 1 219 ? 27.111  -13.126 71.799  1.00 97.58  ? 219 TYR A CE2  1 
ATOM   3450  C CZ   . TYR A 1 219 ? 26.853  -14.066 72.766  1.00 99.82  ? 219 TYR A CZ   1 
ATOM   3451  O OH   . TYR A 1 219 ? 27.447  -15.306 72.674  1.00 101.40 ? 219 TYR A OH   1 
ATOM   3452  H H    . TYR A 1 219 ? 24.878  -7.804  72.880  1.00 109.22 ? 219 TYR A H    1 
ATOM   3453  H HA   . TYR A 1 219 ? 25.330  -9.457  74.898  1.00 110.72 ? 219 TYR A HA   1 
ATOM   3454  H HB2  . TYR A 1 219 ? 24.088  -10.353 73.272  1.00 111.91 ? 219 TYR A HB2  1 
ATOM   3455  H HB3  . TYR A 1 219 ? 25.056  -9.819  72.130  1.00 111.91 ? 219 TYR A HB3  1 
ATOM   3456  H HD1  . TYR A 1 219 ? 24.841  -12.340 74.600  1.00 118.35 ? 219 TYR A HD1  1 
ATOM   3457  H HD2  . TYR A 1 219 ? 26.689  -11.251 71.228  1.00 115.50 ? 219 TYR A HD2  1 
ATOM   3458  H HE1  . TYR A 1 219 ? 25.842  -14.407 74.479  1.00 122.89 ? 219 TYR A HE1  1 
ATOM   3459  H HE2  . TYR A 1 219 ? 27.682  -13.325 71.092  1.00 117.09 ? 219 TYR A HE2  1 
ATOM   3460  H HH   . TYR A 1 219 ? 27.918  -15.348 71.980  1.00 121.68 ? 219 TYR A HH   1 
ATOM   3461  N N    . LEU A 1 220 ? 27.847  -8.716  73.082  1.00 96.47  ? 220 LEU A N    1 
ATOM   3462  C CA   . LEU A 1 220 ? 29.302  -8.755  73.082  1.00 98.52  ? 220 LEU A CA   1 
ATOM   3463  C C    . LEU A 1 220 ? 29.898  -7.883  74.179  1.00 98.63  ? 220 LEU A C    1 
ATOM   3464  O O    . LEU A 1 220 ? 31.043  -8.113  74.581  1.00 101.74 ? 220 LEU A O    1 
ATOM   3465  C CB   . LEU A 1 220 ? 29.854  -8.308  71.731  1.00 95.66  ? 220 LEU A CB   1 
ATOM   3466  C CG   . LEU A 1 220 ? 29.674  -9.243  70.538  1.00 92.66  ? 220 LEU A CG   1 
ATOM   3467  C CD1  . LEU A 1 220 ? 30.519  -8.727  69.374  1.00 93.68  ? 220 LEU A CD1  1 
ATOM   3468  C CD2  . LEU A 1 220 ? 30.044  -10.673 70.843  1.00 92.61  ? 220 LEU A CD2  1 
ATOM   3469  H H    . LEU A 1 220 ? 27.498  -8.259  72.442  1.00 115.76 ? 220 LEU A H    1 
ATOM   3470  H HA   . LEU A 1 220 ? 29.580  -9.673  73.229  1.00 118.23 ? 220 LEU A HA   1 
ATOM   3471  H HB2  . LEU A 1 220 ? 29.419  -7.473  71.498  1.00 114.79 ? 220 LEU A HB2  1 
ATOM   3472  H HB3  . LEU A 1 220 ? 30.808  -8.169  71.834  1.00 114.79 ? 220 LEU A HB3  1 
ATOM   3473  H HG   . LEU A 1 220 ? 28.733  -9.252  70.303  1.00 111.19 ? 220 LEU A HG   1 
ATOM   3474  H HD11 . LEU A 1 220 ? 30.400  -9.315  68.612  1.00 112.41 ? 220 LEU A HD11 1 
ATOM   3475  H HD12 . LEU A 1 220 ? 30.230  -7.829  69.148  1.00 112.41 ? 220 LEU A HD12 1 
ATOM   3476  H HD13 . LEU A 1 220 ? 31.452  -8.717  69.641  1.00 112.41 ? 220 LEU A HD13 1 
ATOM   3477  H HD21 . LEU A 1 220 ? 29.922  -11.208 70.043  1.00 111.14 ? 220 LEU A HD21 1 
ATOM   3478  H HD22 . LEU A 1 220 ? 30.972  -10.706 71.124  1.00 111.14 ? 220 LEU A HD22 1 
ATOM   3479  H HD23 . LEU A 1 220 ? 29.472  -11.003 71.553  1.00 111.14 ? 220 LEU A HD23 1 
ATOM   3480  N N    . LYS A 1 221 ? 29.156  -6.876  74.651  1.00 97.24  ? 221 LYS A N    1 
ATOM   3481  C CA   . LYS A 1 221 ? 29.617  -6.075  75.781  1.00 99.29  ? 221 LYS A CA   1 
ATOM   3482  C C    . LYS A 1 221 ? 29.624  -6.902  77.063  1.00 98.62  ? 221 LYS A C    1 
ATOM   3483  O O    . LYS A 1 221 ? 30.618  -6.917  77.797  1.00 102.09 ? 221 LYS A O    1 
ATOM   3484  C CB   . LYS A 1 221 ? 28.732  -4.834  75.933  1.00 94.56  ? 221 LYS A CB   1 
ATOM   3485  C CG   . LYS A 1 221 ? 28.956  -4.025  77.207  1.00 94.71  ? 221 LYS A CG   1 
ATOM   3486  C CD   . LYS A 1 221 ? 30.170  -3.105  77.107  1.00 95.58  ? 221 LYS A CD   1 
ATOM   3487  C CE   . LYS A 1 221 ? 30.453  -2.422  78.442  1.00 101.31 ? 221 LYS A CE   1 
ATOM   3488  N NZ   . LYS A 1 221 ? 31.913  -2.296  78.724  1.00 104.16 ? 221 LYS A NZ   1 
ATOM   3489  H H    . LYS A 1 221 ? 28.391  -6.640  74.337  1.00 116.68 ? 221 LYS A H    1 
ATOM   3490  H HA   . LYS A 1 221 ? 30.525  -5.776  75.614  1.00 119.15 ? 221 LYS A HA   1 
ATOM   3491  H HB2  . LYS A 1 221 ? 28.902  -4.245  75.181  1.00 113.47 ? 221 LYS A HB2  1 
ATOM   3492  H HB3  . LYS A 1 221 ? 27.805  -5.118  75.929  1.00 113.47 ? 221 LYS A HB3  1 
ATOM   3493  H HG2  . LYS A 1 221 ? 28.174  -3.475  77.375  1.00 113.65 ? 221 LYS A HG2  1 
ATOM   3494  H HG3  . LYS A 1 221 ? 29.099  -4.633  77.949  1.00 113.65 ? 221 LYS A HG3  1 
ATOM   3495  H HD2  . LYS A 1 221 ? 30.949  -3.625  76.858  1.00 114.69 ? 221 LYS A HD2  1 
ATOM   3496  H HD3  . LYS A 1 221 ? 30.001  -2.419  76.442  1.00 114.69 ? 221 LYS A HD3  1 
ATOM   3497  H HE2  . LYS A 1 221 ? 30.072  -1.530  78.429  1.00 121.58 ? 221 LYS A HE2  1 
ATOM   3498  H HE3  . LYS A 1 221 ? 30.053  -2.943  79.156  1.00 121.58 ? 221 LYS A HE3  1 
ATOM   3499  H HZ1  . LYS A 1 221 ? 32.038  -1.900  79.511  1.00 124.99 ? 221 LYS A HZ1  1 
ATOM   3500  H HZ2  . LYS A 1 221 ? 32.290  -3.102  78.744  1.00 124.99 ? 221 LYS A HZ2  1 
ATOM   3501  H HZ3  . LYS A 1 221 ? 32.305  -1.810  78.090  1.00 124.99 ? 221 LYS A HZ3  1 
ATOM   3502  N N    . LYS A 1 222 ? 28.523  -7.608  77.339  1.00 98.53  ? 222 LYS A N    1 
ATOM   3503  C CA   . LYS A 1 222 ? 28.395  -8.355  78.585  1.00 101.01 ? 222 LYS A CA   1 
ATOM   3504  C C    . LYS A 1 222 ? 29.187  -9.657  78.563  1.00 105.52 ? 222 LYS A C    1 
ATOM   3505  O O    . LYS A 1 222 ? 29.703  -10.073 79.605  1.00 108.93 ? 222 LYS A O    1 
ATOM   3506  C CB   . LYS A 1 222 ? 26.916  -8.645  78.866  1.00 97.30  ? 222 LYS A CB   1 
ATOM   3507  C CG   . LYS A 1 222 ? 26.561  -8.824  80.341  1.00 103.97 ? 222 LYS A CG   1 
ATOM   3508  C CD   . LYS A 1 222 ? 26.469  -10.302 80.724  1.00 110.52 ? 222 LYS A CD   1 
ATOM   3509  C CE   . LYS A 1 222 ? 25.451  -10.551 81.842  1.00 108.78 ? 222 LYS A CE   1 
ATOM   3510  N NZ   . LYS A 1 222 ? 24.910  -11.946 81.805  1.00 108.39 ? 222 LYS A NZ   1 
ATOM   3511  H H    . LYS A 1 222 ? 27.839  -7.669  76.821  1.00 118.24 ? 222 LYS A H    1 
ATOM   3512  H HA   . LYS A 1 222 ? 28.742  -7.813  79.310  1.00 121.21 ? 222 LYS A HA   1 
ATOM   3513  H HB2  . LYS A 1 222 ? 26.389  -7.905  78.528  1.00 116.76 ? 222 LYS A HB2  1 
ATOM   3514  H HB3  . LYS A 1 222 ? 26.672  -9.464  78.407  1.00 116.76 ? 222 LYS A HB3  1 
ATOM   3515  H HG2  . LYS A 1 222 ? 27.246  -8.410  80.889  1.00 124.76 ? 222 LYS A HG2  1 
ATOM   3516  H HG3  . LYS A 1 222 ? 25.701  -8.411  80.516  1.00 124.76 ? 222 LYS A HG3  1 
ATOM   3517  H HD2  . LYS A 1 222 ? 26.197  -10.816 79.948  1.00 132.63 ? 222 LYS A HD2  1 
ATOM   3518  H HD3  . LYS A 1 222 ? 27.337  -10.605 81.034  1.00 132.63 ? 222 LYS A HD3  1 
ATOM   3519  H HE2  . LYS A 1 222 ? 25.881  -10.415 82.701  1.00 130.54 ? 222 LYS A HE2  1 
ATOM   3520  H HE3  . LYS A 1 222 ? 24.709  -9.935  81.741  1.00 130.54 ? 222 LYS A HE3  1 
ATOM   3521  H HZ1  . LYS A 1 222 ? 24.322  -12.062 82.462  1.00 130.07 ? 222 LYS A HZ1  1 
ATOM   3522  H HZ2  . LYS A 1 222 ? 24.506  -12.095 81.026  1.00 130.07 ? 222 LYS A HZ2  1 
ATOM   3523  H HZ3  . LYS A 1 222 ? 25.573  -12.533 81.903  1.00 130.07 ? 222 LYS A HZ3  1 
ATOM   3524  N N    . CYS A 1 223 ? 29.314  -10.301 77.400  1.00 112.89 ? 223 CYS A N    1 
ATOM   3525  C CA   . CYS A 1 223 ? 29.939  -11.615 77.315  1.00 117.81 ? 223 CYS A CA   1 
ATOM   3526  C C    . CYS A 1 223 ? 31.398  -11.579 76.881  1.00 118.11 ? 223 CYS A C    1 
ATOM   3527  O O    . CYS A 1 223 ? 32.102  -12.581 77.053  1.00 119.33 ? 223 CYS A O    1 
ATOM   3528  C CB   . CYS A 1 223 ? 29.163  -12.507 76.337  1.00 110.96 ? 223 CYS A CB   1 
ATOM   3529  S SG   . CYS A 1 223 ? 28.102  -13.744 77.118  1.00 128.86 ? 223 CYS A SG   1 
ATOM   3530  H H    . CYS A 1 223 ? 29.043  -9.993  76.644  1.00 135.47 ? 223 CYS A H    1 
ATOM   3531  H HA   . CYS A 1 223 ? 29.905  -12.021 78.196  1.00 141.37 ? 223 CYS A HA   1 
ATOM   3532  H HB2  . CYS A 1 223 ? 28.597  -11.943 75.788  1.00 133.16 ? 223 CYS A HB2  1 
ATOM   3533  H HB3  . CYS A 1 223 ? 29.801  -12.980 75.780  1.00 133.16 ? 223 CYS A HB3  1 
ATOM   3534  H HG   . CYS A 1 223 ? 27.539  -14.371 76.263  1.00 154.64 ? 223 CYS A HG   1 
ATOM   3535  N N    . LYS A 1 224 ? 31.867  -10.468 76.314  1.00 115.10 ? 224 LYS A N    1 
ATOM   3536  C CA   . LYS A 1 224 ? 33.237  -10.381 75.827  1.00 114.51 ? 224 LYS A CA   1 
ATOM   3537  C C    . LYS A 1 224 ? 33.883  -9.026  76.083  1.00 107.76 ? 224 LYS A C    1 
ATOM   3538  O O    . LYS A 1 224 ? 35.015  -8.812  75.637  1.00 104.75 ? 224 LYS A O    1 
ATOM   3539  C CB   . LYS A 1 224 ? 33.284  -10.689 74.318  1.00 112.91 ? 224 LYS A CB   1 
ATOM   3540  C CG   . LYS A 1 224 ? 32.252  -11.717 73.868  1.00 113.24 ? 224 LYS A CG   1 
ATOM   3541  C CD   . LYS A 1 224 ? 32.558  -12.266 72.484  1.00 116.44 ? 224 LYS A CD   1 
ATOM   3542  C CE   . LYS A 1 224 ? 33.668  -13.300 72.519  1.00 111.09 ? 224 LYS A CE   1 
ATOM   3543  N NZ   . LYS A 1 224 ? 34.896  -12.784 71.852  1.00 116.60 ? 224 LYS A NZ   1 
ATOM   3544  H H    . LYS A 1 224 ? 31.408  -9.750  76.201  1.00 138.12 ? 224 LYS A H    1 
ATOM   3545  H HA   . LYS A 1 224 ? 33.771  -11.050 76.282  1.00 137.42 ? 224 LYS A HA   1 
ATOM   3546  H HB2  . LYS A 1 224 ? 33.119  -9.869  73.827  1.00 135.48 ? 224 LYS A HB2  1 
ATOM   3547  H HB3  . LYS A 1 224 ? 34.163  -11.036 74.099  1.00 135.48 ? 224 LYS A HB3  1 
ATOM   3548  H HG2  . LYS A 1 224 ? 32.247  -12.459 74.493  1.00 135.89 ? 224 LYS A HG2  1 
ATOM   3549  H HG3  . LYS A 1 224 ? 31.377  -11.300 73.841  1.00 135.89 ? 224 LYS A HG3  1 
ATOM   3550  H HD2  . LYS A 1 224 ? 31.762  -12.687 72.123  1.00 139.73 ? 224 LYS A HD2  1 
ATOM   3551  H HD3  . LYS A 1 224 ? 32.839  -11.539 71.906  1.00 139.73 ? 224 LYS A HD3  1 
ATOM   3552  H HE2  . LYS A 1 224 ? 33.884  -13.512 73.440  1.00 133.31 ? 224 LYS A HE2  1 
ATOM   3553  H HE3  . LYS A 1 224 ? 33.379  -14.101 72.053  1.00 133.31 ? 224 LYS A HE3  1 
ATOM   3554  H HZ1  . LYS A 1 224 ? 34.720  -12.583 71.003  1.00 139.92 ? 224 LYS A HZ1  1 
ATOM   3555  H HZ2  . LYS A 1 224 ? 35.184  -12.053 72.269  1.00 139.92 ? 224 LYS A HZ2  1 
ATOM   3556  H HZ3  . LYS A 1 224 ? 35.537  -13.401 71.875  1.00 139.92 ? 224 LYS A HZ3  1 
ATOM   3557  N N    . ASN A 1 225 ? 33.212  -8.110  76.780  1.00 107.34 ? 225 ASN A N    1 
ATOM   3558  C CA   . ASN A 1 225 ? 33.774  -6.798  77.096  1.00 111.16 ? 225 ASN A CA   1 
ATOM   3559  C C    . ASN A 1 225 ? 34.182  -6.062  75.821  1.00 109.18 ? 225 ASN A C    1 
ATOM   3560  O O    . ASN A 1 225 ? 35.311  -5.589  75.682  1.00 108.24 ? 225 ASN A O    1 
ATOM   3561  C CB   . ASN A 1 225 ? 34.957  -6.934  78.062  1.00 114.63 ? 225 ASN A CB   1 
ATOM   3562  C CG   . ASN A 1 225 ? 35.582  -5.594  78.424  1.00 115.31 ? 225 ASN A CG   1 
ATOM   3563  O OD1  . ASN A 1 225 ? 34.895  -4.573  78.501  1.00 114.39 ? 225 ASN A OD1  1 
ATOM   3564  N ND2  . ASN A 1 225 ? 36.893  -5.595  78.645  1.00 111.10 ? 225 ASN A ND2  1 
ATOM   3565  H H    . ASN A 1 225 ? 32.416  -8.227  77.086  1.00 128.81 ? 225 ASN A H    1 
ATOM   3566  H HA   . ASN A 1 225 ? 33.094  -6.262  77.534  1.00 133.39 ? 225 ASN A HA   1 
ATOM   3567  H HB2  . ASN A 1 225 ? 34.648  -7.352  78.882  1.00 137.56 ? 225 ASN A HB2  1 
ATOM   3568  H HB3  . ASN A 1 225 ? 35.641  -7.481  77.648  1.00 137.56 ? 225 ASN A HB3  1 
ATOM   3569  H HD21 . ASN A 1 225 ? 37.340  -6.327  78.580  1.00 133.32 ? 225 ASN A HD21 1 
ATOM   3570  H HD22 . ASN A 1 225 ? 37.295  -4.863  78.853  1.00 133.32 ? 225 ASN A HD22 1 
ATOM   3571  N N    . LEU A 1 226 ? 33.241  -5.968  74.878  1.00 107.45 ? 226 LEU A N    1 
ATOM   3572  C CA   . LEU A 1 226 ? 33.441  -5.265  73.611  1.00 101.64 ? 226 LEU A CA   1 
ATOM   3573  C C    . LEU A 1 226 ? 32.516  -4.053  73.577  1.00 99.02  ? 226 LEU A C    1 
ATOM   3574  O O    . LEU A 1 226 ? 31.292  -4.196  73.476  1.00 95.11  ? 226 LEU A O    1 
ATOM   3575  C CB   . LEU A 1 226 ? 33.179  -6.184  72.424  1.00 100.91 ? 226 LEU A CB   1 
ATOM   3576  C CG   . LEU A 1 226 ? 33.768  -5.744  71.083  1.00 99.94  ? 226 LEU A CG   1 
ATOM   3577  C CD1  . LEU A 1 226 ? 35.213  -5.285  71.208  1.00 100.12 ? 226 LEU A CD1  1 
ATOM   3578  C CD2  . LEU A 1 226 ? 33.656  -6.882  70.069  1.00 96.72  ? 226 LEU A CD2  1 
ATOM   3579  H H    . LEU A 1 226 ? 32.458  -6.314  74.953  1.00 128.94 ? 226 LEU A H    1 
ATOM   3580  H HA   . LEU A 1 226 ? 34.359  -4.954  73.562  1.00 121.96 ? 226 LEU A HA   1 
ATOM   3581  H HB2  . LEU A 1 226 ? 33.553  -7.055  72.629  1.00 121.10 ? 226 LEU A HB2  1 
ATOM   3582  H HB3  . LEU A 1 226 ? 32.219  -6.256  72.305  1.00 121.10 ? 226 LEU A HB3  1 
ATOM   3583  H HG   . LEU A 1 226 ? 33.261  -4.980  70.766  1.00 119.93 ? 226 LEU A HG   1 
ATOM   3584  H HD11 . LEU A 1 226 ? 35.613  -5.255  70.324  1.00 120.14 ? 226 LEU A HD11 1 
ATOM   3585  H HD12 . LEU A 1 226 ? 35.231  -4.402  71.609  1.00 120.14 ? 226 LEU A HD12 1 
ATOM   3586  H HD13 . LEU A 1 226 ? 35.696  -5.912  71.768  1.00 120.14 ? 226 LEU A HD13 1 
ATOM   3587  H HD21 . LEU A 1 226 ? 34.212  -6.676  69.301  1.00 116.06 ? 226 LEU A HD21 1 
ATOM   3588  H HD22 . LEU A 1 226 ? 33.957  -7.705  70.484  1.00 116.06 ? 226 LEU A HD22 1 
ATOM   3589  H HD23 . LEU A 1 226 ? 32.730  -6.969  69.793  1.00 116.06 ? 226 LEU A HD23 1 
ATOM   3590  N N    . ASP A 1 227 ? 33.110  -2.860  73.634  1.00 101.64 ? 227 ASP A N    1 
ATOM   3591  C CA   . ASP A 1 227 ? 32.336  -1.636  73.798  1.00 102.43 ? 227 ASP A CA   1 
ATOM   3592  C C    . ASP A 1 227 ? 31.744  -1.148  72.483  1.00 101.32 ? 227 ASP A C    1 
ATOM   3593  O O    . ASP A 1 227 ? 30.638  -0.593  72.469  1.00 100.80 ? 227 ASP A O    1 
ATOM   3594  C CB   . ASP A 1 227 ? 33.224  -0.550  74.413  1.00 109.60 ? 227 ASP A CB   1 
ATOM   3595  C CG   . ASP A 1 227 ? 32.432  0.622   74.946  1.00 116.10 ? 227 ASP A CG   1 
ATOM   3596  O OD1  . ASP A 1 227 ? 31.887  0.515   76.066  1.00 120.18 ? 227 ASP A OD1  1 
ATOM   3597  O OD2  . ASP A 1 227 ? 32.357  1.656   74.246  1.00 112.48 ? 227 ASP A OD2  1 
ATOM   3598  H H    . ASP A 1 227 ? 33.960  -2.735  73.580  1.00 121.97 ? 227 ASP A H    1 
ATOM   3599  H HA   . ASP A 1 227 ? 31.598  -1.815  74.401  1.00 122.92 ? 227 ASP A HA   1 
ATOM   3600  H HB2  . ASP A 1 227 ? 33.726  -0.932  75.149  1.00 131.52 ? 227 ASP A HB2  1 
ATOM   3601  H HB3  . ASP A 1 227 ? 33.832  -0.217  73.734  1.00 131.52 ? 227 ASP A HB3  1 
ATOM   3602  N N    . ARG A 1 228 ? 32.461  -1.329  71.377  1.00 97.08  ? 228 ARG A N    1 
ATOM   3603  C CA   . ARG A 1 228 ? 31.976  -0.880  70.080  1.00 92.68  ? 228 ARG A CA   1 
ATOM   3604  C C    . ARG A 1 228 ? 32.738  -1.607  68.981  1.00 91.90  ? 228 ARG A C    1 
ATOM   3605  O O    . ARG A 1 228 ? 33.930  -1.891  69.131  1.00 94.80  ? 228 ARG A O    1 
ATOM   3606  C CB   . ARG A 1 228 ? 32.119  0.643   69.913  1.00 93.42  ? 228 ARG A CB   1 
ATOM   3607  C CG   . ARG A 1 228 ? 33.528  1.196   70.104  1.00 95.23  ? 228 ARG A CG   1 
ATOM   3608  C CD   . ARG A 1 228 ? 34.183  1.591   68.794  1.00 96.39  ? 228 ARG A CD   1 
ATOM   3609  N NE   . ARG A 1 228 ? 33.673  2.826   68.206  1.00 96.04  ? 228 ARG A NE   1 
ATOM   3610  C CZ   . ARG A 1 228 ? 33.949  4.055   68.612  1.00 95.44  ? 228 ARG A CZ   1 
ATOM   3611  N NH1  . ARG A 1 228 ? 34.579  4.273   69.714  1.00 98.72  ? 228 ARG A NH1  1 
ATOM   3612  N NH2  . ARG A 1 228 ? 33.690  5.081   67.821  1.00 98.32  ? 228 ARG A NH2  1 
ATOM   3613  H H    . ARG A 1 228 ? 33.232  -1.709  71.353  1.00 116.49 ? 228 ARG A H    1 
ATOM   3614  H HA   . ARG A 1 228 ? 31.036  -1.107  69.998  1.00 111.22 ? 228 ARG A HA   1 
ATOM   3615  H HB2  . ARG A 1 228 ? 31.835  0.879   69.016  1.00 112.11 ? 228 ARG A HB2  1 
ATOM   3616  H HB3  . ARG A 1 228 ? 31.548  1.076   70.567  1.00 112.11 ? 228 ARG A HB3  1 
ATOM   3617  H HG2  . ARG A 1 228 ? 33.486  1.984   70.668  1.00 114.27 ? 228 ARG A HG2  1 
ATOM   3618  H HG3  . ARG A 1 228 ? 34.081  0.518   70.523  1.00 114.27 ? 228 ARG A HG3  1 
ATOM   3619  H HD2  . ARG A 1 228 ? 35.133  1.711   68.947  1.00 115.66 ? 228 ARG A HD2  1 
ATOM   3620  H HD3  . ARG A 1 228 ? 34.038  0.880   68.150  1.00 115.66 ? 228 ARG A HD3  1 
ATOM   3621  H HE   . ARG A 1 228 ? 33.145  2.748   67.532  1.00 115.25 ? 228 ARG A HE   1 
ATOM   3622  H HH11 . ARG A 1 228 ? 34.831  3.613   70.203  1.00 118.47 ? 228 ARG A HH11 1 
ATOM   3623  H HH12 . ARG A 1 228 ? 34.748  5.080   69.960  1.00 118.47 ? 228 ARG A HH12 1 
ATOM   3624  H HH21 . ARG A 1 228 ? 33.343  4.949   67.045  1.00 117.98 ? 228 ARG A HH21 1 
ATOM   3625  H HH22 . ARG A 1 228 ? 33.867  5.881   68.082  1.00 117.98 ? 228 ARG A HH22 1 
ATOM   3626  N N    . ALA A 1 229 ? 32.042  -1.911  67.889  1.00 87.73  ? 229 ALA A N    1 
ATOM   3627  C CA   . ALA A 1 229 ? 32.638  -2.660  66.794  1.00 86.02  ? 229 ALA A CA   1 
ATOM   3628  C C    . ALA A 1 229 ? 31.824  -2.433  65.531  1.00 82.61  ? 229 ALA A C    1 
ATOM   3629  O O    . ALA A 1 229 ? 30.683  -1.966  65.579  1.00 80.23  ? 229 ALA A O    1 
ATOM   3630  C CB   . ALA A 1 229 ? 32.714  -4.156  67.119  1.00 86.12  ? 229 ALA A CB   1 
ATOM   3631  H H    . ALA A 1 229 ? 31.221  -1.692  67.759  1.00 105.28 ? 229 ALA A H    1 
ATOM   3632  H HA   . ALA A 1 229 ? 33.536  -2.329  66.636  1.00 103.23 ? 229 ALA A HA   1 
ATOM   3633  H HB1  . ALA A 1 229 ? 31.818  -4.491  67.277  1.00 103.34 ? 229 ALA A HB1  1 
ATOM   3634  H HB2  . ALA A 1 229 ? 33.114  -4.622  66.368  1.00 103.34 ? 229 ALA A HB2  1 
ATOM   3635  H HB3  . ALA A 1 229 ? 33.258  -4.280  67.912  1.00 103.34 ? 229 ALA A HB3  1 
ATOM   3636  N N    . LYS A 1 230 ? 32.431  -2.778  64.398  1.00 83.20  ? 230 LYS A N    1 
ATOM   3637  C CA   . LYS A 1 230 ? 31.798  -2.666  63.089  1.00 79.95  ? 230 LYS A CA   1 
ATOM   3638  C C    . LYS A 1 230 ? 31.360  -4.052  62.631  1.00 75.84  ? 230 LYS A C    1 
ATOM   3639  O O    . LYS A 1 230 ? 32.201  -4.930  62.409  1.00 78.07  ? 230 LYS A O    1 
ATOM   3640  C CB   . LYS A 1 230 ? 32.757  -2.043  62.078  1.00 76.90  ? 230 LYS A CB   1 
ATOM   3641  C CG   . LYS A 1 230 ? 32.758  -0.525  62.083  1.00 78.30  ? 230 LYS A CG   1 
ATOM   3642  C CD   . LYS A 1 230 ? 33.688  0.020   61.006  1.00 85.27  ? 230 LYS A CD   1 
ATOM   3643  C CE   . LYS A 1 230 ? 34.720  0.987   61.576  1.00 85.74  ? 230 LYS A CE   1 
ATOM   3644  N NZ   . LYS A 1 230 ? 34.887  2.185   60.692  1.00 86.46  ? 230 LYS A NZ   1 
ATOM   3645  H H    . LYS A 1 230 ? 33.232  -3.089  64.362  1.00 99.84  ? 230 LYS A H    1 
ATOM   3646  H HA   . LYS A 1 230 ? 31.011  -2.102  63.154  1.00 95.94  ? 230 LYS A HA   1 
ATOM   3647  H HB2  . LYS A 1 230 ? 33.658  -2.340  62.280  1.00 92.27  ? 230 LYS A HB2  1 
ATOM   3648  H HB3  . LYS A 1 230 ? 32.503  -2.335  61.188  1.00 92.27  ? 230 LYS A HB3  1 
ATOM   3649  H HG2  . LYS A 1 230 ? 31.861  -0.200  61.909  1.00 93.96  ? 230 LYS A HG2  1 
ATOM   3650  H HG3  . LYS A 1 230 ? 33.066  -0.205  62.946  1.00 93.96  ? 230 LYS A HG3  1 
ATOM   3651  H HD2  . LYS A 1 230 ? 34.162  -0.717  60.590  1.00 102.33 ? 230 LYS A HD2  1 
ATOM   3652  H HD3  . LYS A 1 230 ? 33.164  0.495   60.342  1.00 102.33 ? 230 LYS A HD3  1 
ATOM   3653  H HE2  . LYS A 1 230 ? 34.429  1.290   62.450  1.00 102.88 ? 230 LYS A HE2  1 
ATOM   3654  H HE3  . LYS A 1 230 ? 35.577  0.538   61.649  1.00 102.88 ? 230 LYS A HE3  1 
ATOM   3655  H HZ1  . LYS A 1 230 ? 35.492  2.737   61.038  1.00 103.75 ? 230 LYS A HZ1  1 
ATOM   3656  H HZ2  . LYS A 1 230 ? 35.157  1.930   59.883  1.00 103.75 ? 230 LYS A HZ2  1 
ATOM   3657  H HZ3  . LYS A 1 230 ? 34.112  2.617   60.615  1.00 103.75 ? 230 LYS A HZ3  1 
ATOM   3658  N N    . ILE A 1 231 ? 30.053  -4.246  62.487  1.00 72.90  ? 231 ILE A N    1 
ATOM   3659  C CA   . ILE A 1 231 ? 29.482  -5.550  62.166  1.00 77.35  ? 231 ILE A CA   1 
ATOM   3660  C C    . ILE A 1 231 ? 29.087  -5.535  60.695  1.00 78.16  ? 231 ILE A C    1 
ATOM   3661  O O    . ILE A 1 231 ? 28.134  -4.852  60.301  1.00 75.65  ? 231 ILE A O    1 
ATOM   3662  C CB   . ILE A 1 231 ? 28.287  -5.871  63.071  1.00 77.95  ? 231 ILE A CB   1 
ATOM   3663  C CG1  . ILE A 1 231 ? 28.738  -6.681  64.292  1.00 82.34  ? 231 ILE A CG1  1 
ATOM   3664  C CG2  . ILE A 1 231 ? 27.224  -6.667  62.327  1.00 78.60  ? 231 ILE A CG2  1 
ATOM   3665  C CD1  . ILE A 1 231 ? 29.866  -6.054  65.075  1.00 80.92  ? 231 ILE A CD1  1 
ATOM   3666  H H    . ILE A 1 231 ? 29.465  -3.625  62.573  1.00 87.48  ? 231 ILE A H    1 
ATOM   3667  H HA   . ILE A 1 231 ? 30.154  -6.238  62.288  1.00 92.82  ? 231 ILE A HA   1 
ATOM   3668  H HB   . ILE A 1 231 ? 27.911  -5.023  63.355  1.00 93.53  ? 231 ILE A HB   1 
ATOM   3669  H HG12 . ILE A 1 231 ? 27.984  -6.780  64.894  1.00 98.81  ? 231 ILE A HG12 1 
ATOM   3670  H HG13 . ILE A 1 231 ? 29.040  -7.552  63.991  1.00 98.81  ? 231 ILE A HG13 1 
ATOM   3671  H HG21 . ILE A 1 231 ? 26.598  -7.036  62.969  1.00 94.32  ? 231 ILE A HG21 1 
ATOM   3672  H HG22 . ILE A 1 231 ? 26.758  -6.076  61.714  1.00 94.32  ? 231 ILE A HG22 1 
ATOM   3673  H HG23 . ILE A 1 231 ? 27.653  -7.383  61.834  1.00 94.32  ? 231 ILE A HG23 1 
ATOM   3674  H HD11 . ILE A 1 231 ? 29.976  -6.534  65.911  1.00 97.11  ? 231 ILE A HD11 1 
ATOM   3675  H HD12 . ILE A 1 231 ? 30.682  -6.107  64.553  1.00 97.11  ? 231 ILE A HD12 1 
ATOM   3676  H HD13 . ILE A 1 231 ? 29.649  -5.125  65.254  1.00 97.11  ? 231 ILE A HD13 1 
ATOM   3677  N N    . VAL A 1 232 ? 29.818  -6.291  59.879  1.00 77.62  ? 232 VAL A N    1 
ATOM   3678  C CA   . VAL A 1 232 ? 29.518  -6.387  58.456  1.00 79.64  ? 232 VAL A CA   1 
ATOM   3679  C C    . VAL A 1 232 ? 28.297  -7.278  58.269  1.00 78.79  ? 232 VAL A C    1 
ATOM   3680  O O    . VAL A 1 232 ? 28.161  -8.321  58.918  1.00 78.25  ? 232 VAL A O    1 
ATOM   3681  C CB   . VAL A 1 232 ? 30.733  -6.917  57.671  1.00 80.09  ? 232 VAL A CB   1 
ATOM   3682  C CG1  . VAL A 1 232 ? 32.018  -6.250  58.151  1.00 84.10  ? 232 VAL A CG1  1 
ATOM   3683  C CG2  . VAL A 1 232 ? 30.841  -8.425  57.784  1.00 78.98  ? 232 VAL A CG2  1 
ATOM   3684  H H    . VAL A 1 232 ? 30.495  -6.759  60.128  1.00 93.15  ? 232 VAL A H    1 
ATOM   3685  H HA   . VAL A 1 232 ? 29.312  -5.503  58.114  1.00 95.56  ? 232 VAL A HA   1 
ATOM   3686  H HB   . VAL A 1 232 ? 30.608  -6.698  56.734  1.00 96.11  ? 232 VAL A HB   1 
ATOM   3687  H HG11 . VAL A 1 232 ? 32.760  -6.576  57.619  1.00 100.92 ? 232 VAL A HG11 1 
ATOM   3688  H HG12 . VAL A 1 232 ? 31.933  -5.289  58.047  1.00 100.92 ? 232 VAL A HG12 1 
ATOM   3689  H HG13 . VAL A 1 232 ? 32.158  -6.470  59.085  1.00 100.92 ? 232 VAL A HG13 1 
ATOM   3690  H HG21 . VAL A 1 232 ? 31.638  -8.721  57.318  1.00 94.78  ? 232 VAL A HG21 1 
ATOM   3691  H HG22 . VAL A 1 232 ? 30.897  -8.669  58.722  1.00 94.78  ? 232 VAL A HG22 1 
ATOM   3692  H HG23 . VAL A 1 232 ? 30.055  -8.829  57.384  1.00 94.78  ? 232 VAL A HG23 1 
ATOM   3693  N N    . GLN A 1 233 ? 27.409  -6.876  57.374  1.00 78.61  ? 233 GLN A N    1 
ATOM   3694  C CA   . GLN A 1 233 ? 26.124  -7.522  57.153  1.00 79.36  ? 233 GLN A CA   1 
ATOM   3695  C C    . GLN A 1 233 ? 25.935  -7.766  55.670  1.00 80.34  ? 233 GLN A C    1 
ATOM   3696  O O    . GLN A 1 233 ? 26.718  -7.285  54.844  1.00 81.23  ? 233 GLN A O    1 
ATOM   3697  C CB   . GLN A 1 233 ? 25.008  -6.644  57.739  1.00 78.48  ? 233 GLN A CB   1 
ATOM   3698  C CG   . GLN A 1 233 ? 25.411  -6.087  59.111  1.00 80.53  ? 233 GLN A CG   1 
ATOM   3699  C CD   . GLN A 1 233 ? 24.245  -5.715  59.999  1.00 74.04  ? 233 GLN A CD   1 
ATOM   3700  O OE1  . GLN A 1 233 ? 23.126  -6.193  59.823  1.00 73.31  ? 233 GLN A OE1  1 
ATOM   3701  N NE2  . GLN A 1 233 ? 24.507  -4.853  60.969  1.00 70.48  ? 233 GLN A NE2  1 
ATOM   3702  H H    . GLN A 1 233 ? 27.535  -6.199  56.858  1.00 94.34  ? 233 GLN A H    1 
ATOM   3703  H HA   . GLN A 1 233 ? 26.086  -8.387  57.589  1.00 95.23  ? 233 GLN A HA   1 
ATOM   3704  H HB2  . GLN A 1 233 ? 24.837  -5.899  57.142  1.00 94.18  ? 233 GLN A HB2  1 
ATOM   3705  H HB3  . GLN A 1 233 ? 24.203  -7.175  57.846  1.00 94.18  ? 233 GLN A HB3  1 
ATOM   3706  H HG2  . GLN A 1 233 ? 25.932  -6.759  59.578  1.00 96.63  ? 233 GLN A HG2  1 
ATOM   3707  H HG3  . GLN A 1 233 ? 25.944  -5.288  58.977  1.00 96.63  ? 233 GLN A HG3  1 
ATOM   3708  H HE21 . GLN A 1 233 ? 25.303  -4.541  61.064  1.00 84.58  ? 233 GLN A HE21 1 
ATOM   3709  H HE22 . GLN A 1 233 ? 23.882  -4.605  61.505  1.00 84.58  ? 233 GLN A HE22 1 
ATOM   3710  N N    . PRO A 1 234 ? 24.910  -8.537  55.293  1.00 80.53  ? 234 PRO A N    1 
ATOM   3711  C CA   . PRO A 1 234 ? 24.850  -9.036  53.905  1.00 82.59  ? 234 PRO A CA   1 
ATOM   3712  C C    . PRO A 1 234 ? 25.115  -7.993  52.829  1.00 81.51  ? 234 PRO A C    1 
ATOM   3713  O O    . PRO A 1 234 ? 25.913  -8.249  51.919  1.00 81.47  ? 234 PRO A O    1 
ATOM   3714  C CB   . PRO A 1 234 ? 23.424  -9.607  53.815  1.00 81.56  ? 234 PRO A CB   1 
ATOM   3715  C CG   . PRO A 1 234 ? 23.117  -10.049 55.209  1.00 80.20  ? 234 PRO A CG   1 
ATOM   3716  C CD   . PRO A 1 234 ? 23.774  -9.020  56.106  1.00 80.50  ? 234 PRO A CD   1 
ATOM   3717  H HA   . PRO A 1 234 ? 25.503  -9.747  53.807  1.00 99.11  ? 234 PRO A HA   1 
ATOM   3718  H HB2  . PRO A 1 234 ? 22.807  -8.918  53.523  1.00 97.88  ? 234 PRO A HB2  1 
ATOM   3719  H HB3  . PRO A 1 234 ? 23.402  -10.355 53.198  1.00 97.88  ? 234 PRO A HB3  1 
ATOM   3720  H HG2  . PRO A 1 234 ? 22.157  -10.065 55.346  1.00 96.24  ? 234 PRO A HG2  1 
ATOM   3721  H HG3  . PRO A 1 234 ? 23.489  -10.931 55.364  1.00 96.24  ? 234 PRO A HG3  1 
ATOM   3722  H HD2  . PRO A 1 234 ? 23.161  -8.296  56.308  1.00 96.60  ? 234 PRO A HD2  1 
ATOM   3723  H HD3  . PRO A 1 234 ? 24.087  -9.429  56.929  1.00 96.60  ? 234 PRO A HD3  1 
ATOM   3724  N N    . ASN A 1 235 ? 24.478  -6.825  52.904  1.00 80.93  ? 235 ASN A N    1 
ATOM   3725  C CA   . ASN A 1 235 ? 24.610  -5.779  51.892  1.00 80.58  ? 235 ASN A CA   1 
ATOM   3726  C C    . ASN A 1 235 ? 24.845  -4.423  52.555  1.00 79.86  ? 235 ASN A C    1 
ATOM   3727  O O    . ASN A 1 235 ? 24.209  -3.418  52.234  1.00 81.38  ? 235 ASN A O    1 
ATOM   3728  C CB   . ASN A 1 235 ? 23.366  -5.730  51.001  1.00 83.75  ? 235 ASN A CB   1 
ATOM   3729  C CG   . ASN A 1 235 ? 23.628  -6.236  49.587  1.00 88.02  ? 235 ASN A CG   1 
ATOM   3730  O OD1  . ASN A 1 235 ? 24.723  -6.069  49.041  1.00 84.53  ? 235 ASN A OD1  1 
ATOM   3731  N ND2  . ASN A 1 235 ? 22.614  -6.848  48.981  1.00 89.14  ? 235 ASN A ND2  1 
ATOM   3732  H H    . ASN A 1 235 ? 23.951  -6.611  53.549  1.00 97.11  ? 235 ASN A H    1 
ATOM   3733  H HA   . ASN A 1 235 ? 25.383  -5.980  51.341  1.00 96.70  ? 235 ASN A HA   1 
ATOM   3734  H HB2  . ASN A 1 235 ? 22.675  -6.286  51.394  1.00 100.50 ? 235 ASN A HB2  1 
ATOM   3735  H HB3  . ASN A 1 235 ? 23.059  -4.812  50.938  1.00 100.50 ? 235 ASN A HB3  1 
ATOM   3736  H HD21 . ASN A 1 235 ? 21.862  -6.939  49.389  1.00 106.97 ? 235 ASN A HD21 1 
ATOM   3737  H HD22 . ASN A 1 235 ? 22.710  -7.151  48.183  1.00 106.97 ? 235 ASN A HD22 1 
ATOM   3738  N N    . GLY A 1 236 ? 25.777  -4.381  53.491  1.00 81.52  ? 236 GLY A N    1 
ATOM   3739  C CA   . GLY A 1 236 ? 26.067  -3.157  54.207  1.00 77.07  ? 236 GLY A CA   1 
ATOM   3740  C C    . GLY A 1 236 ? 26.784  -3.468  55.501  1.00 79.09  ? 236 GLY A C    1 
ATOM   3741  O O    . GLY A 1 236 ? 27.096  -4.619  55.808  1.00 80.83  ? 236 GLY A O    1 
ATOM   3742  H H    . GLY A 1 236 ? 26.259  -5.052  53.730  1.00 97.83  ? 236 GLY A H    1 
ATOM   3743  H HA2  . GLY A 1 236 ? 26.630  -2.582  53.665  1.00 92.49  ? 236 GLY A HA2  1 
ATOM   3744  H HA3  . GLY A 1 236 ? 25.241  -2.690  54.410  1.00 92.49  ? 236 GLY A HA3  1 
ATOM   3745  N N    . TRP A 1 237 ? 27.038  -2.407  56.265  1.00 78.61  ? 237 TRP A N    1 
ATOM   3746  C CA   . TRP A 1 237 ? 27.679  -2.564  57.562  1.00 76.17  ? 237 TRP A CA   1 
ATOM   3747  C C    . TRP A 1 237 ? 27.185  -1.486  58.515  1.00 77.54  ? 237 TRP A C    1 
ATOM   3748  O O    . TRP A 1 237 ? 26.807  -0.387  58.096  1.00 77.30  ? 237 TRP A O    1 
ATOM   3749  C CB   . TRP A 1 237 ? 29.211  -2.514  57.447  1.00 76.72  ? 237 TRP A CB   1 
ATOM   3750  C CG   . TRP A 1 237 ? 29.769  -1.177  57.055  1.00 76.49  ? 237 TRP A CG   1 
ATOM   3751  C CD1  . TRP A 1 237 ? 30.079  -0.757  55.800  1.00 76.88  ? 237 TRP A CD1  1 
ATOM   3752  C CD2  . TRP A 1 237 ? 30.096  -0.091  57.933  1.00 78.87  ? 237 TRP A CD2  1 
ATOM   3753  N NE1  . TRP A 1 237 ? 30.574  0.523   55.835  1.00 77.80  ? 237 TRP A NE1  1 
ATOM   3754  C CE2  . TRP A 1 237 ? 30.595  0.955   57.133  1.00 75.53  ? 237 TRP A CE2  1 
ATOM   3755  C CE3  . TRP A 1 237 ? 30.016  0.097   59.318  1.00 77.26  ? 237 TRP A CE3  1 
ATOM   3756  C CZ2  . TRP A 1 237 ? 31.010  2.173   57.669  1.00 77.86  ? 237 TRP A CZ2  1 
ATOM   3757  C CZ3  . TRP A 1 237 ? 30.424  1.308   59.847  1.00 76.75  ? 237 TRP A CZ3  1 
ATOM   3758  C CH2  . TRP A 1 237 ? 30.914  2.331   59.024  1.00 78.21  ? 237 TRP A CH2  1 
ATOM   3759  H H    . TRP A 1 237 ? 26.850  -1.595  56.054  1.00 94.33  ? 237 TRP A H    1 
ATOM   3760  H HA   . TRP A 1 237 ? 27.428  -3.423  57.936  1.00 91.40  ? 237 TRP A HA   1 
ATOM   3761  H HB2  . TRP A 1 237 ? 29.593  -2.748  58.308  1.00 92.07  ? 237 TRP A HB2  1 
ATOM   3762  H HB3  . TRP A 1 237 ? 29.491  -3.155  56.775  1.00 92.07  ? 237 TRP A HB3  1 
ATOM   3763  H HD1  . TRP A 1 237 ? 29.970  -1.265  55.028  1.00 92.26  ? 237 TRP A HD1  1 
ATOM   3764  H HE1  . TRP A 1 237 ? 30.830  0.978   55.152  1.00 93.37  ? 237 TRP A HE1  1 
ATOM   3765  H HE3  . TRP A 1 237 ? 29.694  -0.578  59.871  1.00 92.71  ? 237 TRP A HE3  1 
ATOM   3766  H HZ2  . TRP A 1 237 ? 31.339  2.852   57.126  1.00 93.43  ? 237 TRP A HZ2  1 
ATOM   3767  H HZ3  . TRP A 1 237 ? 30.373  1.446   60.765  1.00 92.10  ? 237 TRP A HZ3  1 
ATOM   3768  H HH2  . TRP A 1 237 ? 31.179  3.135   59.408  1.00 93.86  ? 237 TRP A HH2  1 
ATOM   3769  N N    . LEU A 1 238 ? 27.191  -1.822  59.804  1.00 76.68  ? 238 LEU A N    1 
ATOM   3770  C CA   . LEU A 1 238 ? 26.779  -0.913  60.859  1.00 74.44  ? 238 LEU A CA   1 
ATOM   3771  C C    . LEU A 1 238 ? 27.733  -1.062  62.037  1.00 78.26  ? 238 LEU A C    1 
ATOM   3772  O O    . LEU A 1 238 ? 28.192  -2.168  62.341  1.00 76.65  ? 238 LEU A O    1 
ATOM   3773  C CB   . LEU A 1 238 ? 25.344  -1.191  61.314  1.00 73.36  ? 238 LEU A CB   1 
ATOM   3774  C CG   . LEU A 1 238 ? 24.228  -0.890  60.317  1.00 72.73  ? 238 LEU A CG   1 
ATOM   3775  C CD1  . LEU A 1 238 ? 22.896  -1.405  60.852  1.00 73.57  ? 238 LEU A CD1  1 
ATOM   3776  C CD2  . LEU A 1 238 ? 24.144  0.592   60.013  1.00 69.72  ? 238 LEU A CD2  1 
ATOM   3777  H H    . LEU A 1 238 ? 27.436  -2.594  60.095  1.00 92.02  ? 238 LEU A H    1 
ATOM   3778  H HA   . LEU A 1 238 ? 26.822  0.001   60.539  1.00 89.32  ? 238 LEU A HA   1 
ATOM   3779  H HB2  . LEU A 1 238 ? 25.279  -2.133  61.535  1.00 88.03  ? 238 LEU A HB2  1 
ATOM   3780  H HB3  . LEU A 1 238 ? 25.171  -0.652  62.102  1.00 88.03  ? 238 LEU A HB3  1 
ATOM   3781  H HG   . LEU A 1 238 ? 24.424  -1.345  59.483  1.00 87.27  ? 238 LEU A HG   1 
ATOM   3782  H HD11 . LEU A 1 238 ? 22.203  -1.231  60.196  1.00 88.28  ? 238 LEU A HD11 1 
ATOM   3783  H HD12 . LEU A 1 238 ? 22.967  -2.359  61.013  1.00 88.28  ? 238 LEU A HD12 1 
ATOM   3784  H HD13 . LEU A 1 238 ? 22.689  -0.945  61.681  1.00 88.28  ? 238 LEU A HD13 1 
ATOM   3785  H HD21 . LEU A 1 238 ? 23.370  0.756   59.453  1.00 83.66  ? 238 LEU A HD21 1 
ATOM   3786  H HD22 . LEU A 1 238 ? 24.060  1.081   60.847  1.00 83.66  ? 238 LEU A HD22 1 
ATOM   3787  H HD23 . LEU A 1 238 ? 24.952  0.865   59.550  1.00 83.66  ? 238 LEU A HD23 1 
ATOM   3788  N N    . GLU A 1 239 ? 28.028  0.057   62.691  1.00 80.47  ? 239 GLU A N    1 
ATOM   3789  C CA   . GLU A 1 239 ? 28.854  0.085   63.890  1.00 79.70  ? 239 GLU A CA   1 
ATOM   3790  C C    . GLU A 1 239 ? 27.975  0.377   65.095  1.00 78.53  ? 239 GLU A C    1 
ATOM   3791  O O    . GLU A 1 239 ? 27.178  1.321   65.071  1.00 76.34  ? 239 GLU A O    1 
ATOM   3792  C CB   . GLU A 1 239 ? 29.955  1.142   63.779  1.00 80.16  ? 239 GLU A CB   1 
ATOM   3793  C CG   . GLU A 1 239 ? 30.991  1.070   64.887  1.00 83.84  ? 239 GLU A CG   1 
ATOM   3794  C CD   . GLU A 1 239 ? 31.963  2.236   64.854  1.00 86.52  ? 239 GLU A CD   1 
ATOM   3795  O OE1  . GLU A 1 239 ? 31.581  3.317   64.354  1.00 81.96  ? 239 GLU A OE1  1 
ATOM   3796  O OE2  . GLU A 1 239 ? 33.106  2.073   65.332  1.00 90.15  ? 239 GLU A OE2  1 
ATOM   3797  H H    . GLU A 1 239 ? 27.751  0.836   62.452  1.00 96.56  ? 239 GLU A H    1 
ATOM   3798  H HA   . GLU A 1 239 ? 29.275  -0.781  64.011  1.00 95.65  ? 239 GLU A HA   1 
ATOM   3799  H HB2  . GLU A 1 239 ? 30.417  1.023   62.934  1.00 96.19  ? 239 GLU A HB2  1 
ATOM   3800  H HB3  . GLU A 1 239 ? 29.546  2.021   63.813  1.00 96.19  ? 239 GLU A HB3  1 
ATOM   3801  H HG2  . GLU A 1 239 ? 30.538  1.081   65.745  1.00 100.61 ? 239 GLU A HG2  1 
ATOM   3802  H HG3  . GLU A 1 239 ? 31.501  0.251   64.791  1.00 100.61 ? 239 GLU A HG3  1 
ATOM   3803  N N    . TYR A 1 240 ? 28.114  -0.434  66.139  1.00 82.17  ? 240 TYR A N    1 
ATOM   3804  C CA   . TYR A 1 240 ? 27.430  -0.201  67.404  1.00 80.62  ? 240 TYR A CA   1 
ATOM   3805  C C    . TYR A 1 240 ? 28.396  0.466   68.373  1.00 86.28  ? 240 TYR A C    1 
ATOM   3806  O O    . TYR A 1 240 ? 29.583  0.124   68.420  1.00 87.80  ? 240 TYR A O    1 
ATOM   3807  C CB   . TYR A 1 240 ? 26.876  -1.501  68.000  1.00 82.48  ? 240 TYR A CB   1 
ATOM   3808  C CG   . TYR A 1 240 ? 27.867  -2.365  68.747  1.00 83.71  ? 240 TYR A CG   1 
ATOM   3809  C CD1  . TYR A 1 240 ? 28.207  -2.094  70.068  1.00 88.12  ? 240 TYR A CD1  1 
ATOM   3810  C CD2  . TYR A 1 240 ? 28.443  -3.470  68.139  1.00 83.34  ? 240 TYR A CD2  1 
ATOM   3811  C CE1  . TYR A 1 240 ? 29.108  -2.890  70.751  1.00 89.39  ? 240 TYR A CE1  1 
ATOM   3812  C CE2  . TYR A 1 240 ? 29.342  -4.270  68.813  1.00 86.17  ? 240 TYR A CE2  1 
ATOM   3813  C CZ   . TYR A 1 240 ? 29.672  -3.977  70.119  1.00 89.50  ? 240 TYR A CZ   1 
ATOM   3814  O OH   . TYR A 1 240 ? 30.566  -4.774  70.794  1.00 91.00  ? 240 TYR A OH   1 
ATOM   3815  H H    . TYR A 1 240 ? 28.608  -1.138  66.138  1.00 98.60  ? 240 TYR A H    1 
ATOM   3816  H HA   . TYR A 1 240 ? 26.671  0.387   67.263  1.00 96.75  ? 240 TYR A HA   1 
ATOM   3817  H HB2  . TYR A 1 240 ? 26.169  -1.271  68.623  1.00 98.97  ? 240 TYR A HB2  1 
ATOM   3818  H HB3  . TYR A 1 240 ? 26.517  -2.038  67.275  1.00 98.97  ? 240 TYR A HB3  1 
ATOM   3819  H HD1  . TYR A 1 240 ? 27.822  -1.365  70.498  1.00 105.75 ? 240 TYR A HD1  1 
ATOM   3820  H HD2  . TYR A 1 240 ? 28.218  -3.676  67.261  1.00 100.01 ? 240 TYR A HD2  1 
ATOM   3821  H HE1  . TYR A 1 240 ? 29.332  -2.693  71.632  1.00 107.27 ? 240 TYR A HE1  1 
ATOM   3822  H HE2  . TYR A 1 240 ? 29.725  -5.003  68.388  1.00 103.40 ? 240 TYR A HE2  1 
ATOM   3823  H HH   . TYR A 1 240 ? 30.675  -4.485  71.576  1.00 109.20 ? 240 TYR A HH   1 
ATOM   3824  N N    . ILE A 1 241 ? 27.873  1.416   69.148  1.00 87.15  ? 241 ILE A N    1 
ATOM   3825  C CA   . ILE A 1 241 ? 28.662  2.217   70.077  1.00 88.84  ? 241 ILE A CA   1 
ATOM   3826  C C    . ILE A 1 241 ? 27.925  2.264   71.404  1.00 90.56  ? 241 ILE A C    1 
ATOM   3827  O O    . ILE A 1 241 ? 26.762  2.680   71.457  1.00 89.26  ? 241 ILE A O    1 
ATOM   3828  C CB   . ILE A 1 241 ? 28.907  3.640   69.547  1.00 90.61  ? 241 ILE A CB   1 
ATOM   3829  C CG1  . ILE A 1 241 ? 30.157  3.634   68.647  1.00 93.50  ? 241 ILE A CG1  1 
ATOM   3830  C CG2  . ILE A 1 241 ? 29.046  4.631   70.678  1.00 90.86  ? 241 ILE A CG2  1 
ATOM   3831  C CD1  . ILE A 1 241 ? 30.567  4.983   68.114  1.00 92.12  ? 241 ILE A CD1  1 
ATOM   3832  H H    . ILE A 1 241 ? 27.038  1.620   69.151  1.00 104.58 ? 241 ILE A H    1 
ATOM   3833  H HA   . ILE A 1 241 ? 29.520  1.789   70.220  1.00 106.61 ? 241 ILE A HA   1 
ATOM   3834  H HB   . ILE A 1 241 ? 28.141  3.919   69.021  1.00 108.73 ? 241 ILE A HB   1 
ATOM   3835  H HG12 . ILE A 1 241 ? 30.903  3.286   69.161  1.00 112.20 ? 241 ILE A HG12 1 
ATOM   3836  H HG13 . ILE A 1 241 ? 29.983  3.060   67.884  1.00 112.20 ? 241 ILE A HG13 1 
ATOM   3837  H HG21 . ILE A 1 241 ? 29.417  5.457   70.331  1.00 109.03 ? 241 ILE A HG21 1 
ATOM   3838  H HG22 . ILE A 1 241 ? 28.170  4.797   71.062  1.00 109.03 ? 241 ILE A HG22 1 
ATOM   3839  H HG23 . ILE A 1 241 ? 29.637  4.259   71.352  1.00 109.03 ? 241 ILE A HG23 1 
ATOM   3840  H HD11 . ILE A 1 241 ? 31.068  4.859   67.293  1.00 110.55 ? 241 ILE A HD11 1 
ATOM   3841  H HD12 . ILE A 1 241 ? 29.771  5.508   67.939  1.00 110.55 ? 241 ILE A HD12 1 
ATOM   3842  H HD13 . ILE A 1 241 ? 31.119  5.429   68.775  1.00 110.55 ? 241 ILE A HD13 1 
ATOM   3843  N N    . ILE A 1 242 ? 28.603  1.856   72.472  1.00 96.91  ? 242 ILE A N    1 
ATOM   3844  C CA   . ILE A 1 242 ? 28.074  1.934   73.829  1.00 99.53  ? 242 ILE A CA   1 
ATOM   3845  C C    . ILE A 1 242 ? 28.913  2.951   74.589  1.00 104.48 ? 242 ILE A C    1 
ATOM   3846  O O    . ILE A 1 242 ? 30.140  2.817   74.674  1.00 103.91 ? 242 ILE A O    1 
ATOM   3847  C CB   . ILE A 1 242 ? 28.085  0.565   74.524  1.00 99.39  ? 242 ILE A CB   1 
ATOM   3848  C CG1  . ILE A 1 242 ? 27.523  -0.503  73.584  1.00 91.00  ? 242 ILE A CG1  1 
ATOM   3849  C CG2  . ILE A 1 242 ? 27.283  0.625   75.820  1.00 97.17  ? 242 ILE A CG2  1 
ATOM   3850  C CD1  . ILE A 1 242 ? 27.356  -1.864  74.218  1.00 90.14  ? 242 ILE A CD1  1 
ATOM   3851  H H    . ILE A 1 242 ? 29.394  1.522   72.434  1.00 116.29 ? 242 ILE A H    1 
ATOM   3852  H HA   . ILE A 1 242 ? 27.157  2.248   73.804  1.00 119.44 ? 242 ILE A HA   1 
ATOM   3853  H HB   . ILE A 1 242 ? 29.000  0.330   74.743  1.00 119.27 ? 242 ILE A HB   1 
ATOM   3854  H HG12 . ILE A 1 242 ? 26.650  -0.214  73.274  1.00 109.20 ? 242 ILE A HG12 1 
ATOM   3855  H HG13 . ILE A 1 242 ? 28.126  -0.601  72.831  1.00 109.20 ? 242 ILE A HG13 1 
ATOM   3856  H HG21 . ILE A 1 242 ? 27.435  -0.190  76.323  1.00 116.61 ? 242 ILE A HG21 1 
ATOM   3857  H HG22 . ILE A 1 242 ? 27.576  1.392   76.337  1.00 116.61 ? 242 ILE A HG22 1 
ATOM   3858  H HG23 . ILE A 1 242 ? 26.341  0.711   75.605  1.00 116.61 ? 242 ILE A HG23 1 
ATOM   3859  H HD11 . ILE A 1 242 ? 27.173  -2.516  73.523  1.00 108.16 ? 242 ILE A HD11 1 
ATOM   3860  H HD12 . ILE A 1 242 ? 28.175  -2.098  74.683  1.00 108.16 ? 242 ILE A HD12 1 
ATOM   3861  H HD13 . ILE A 1 242 ? 26.617  -1.832  74.845  1.00 108.16 ? 242 ILE A HD13 1 
ATOM   3862  N N    . GLU A 1 243 ? 28.256  3.971   75.136  1.00 110.56 ? 243 GLU A N    1 
ATOM   3863  C CA   . GLU A 1 243 ? 28.949  5.071   75.794  1.00 115.41 ? 243 GLU A CA   1 
ATOM   3864  C C    . GLU A 1 243 ? 28.083  5.597   76.927  1.00 116.07 ? 243 GLU A C    1 
ATOM   3865  O O    . GLU A 1 243 ? 26.906  5.902   76.717  1.00 114.99 ? 243 GLU A O    1 
ATOM   3866  C CB   . GLU A 1 243 ? 29.262  6.193   74.798  1.00 119.86 ? 243 GLU A CB   1 
ATOM   3867  C CG   . GLU A 1 243 ? 30.451  7.062   75.174  1.00 124.25 ? 243 GLU A CG   1 
ATOM   3868  C CD   . GLU A 1 243 ? 30.783  8.089   74.102  1.00 129.49 ? 243 GLU A CD   1 
ATOM   3869  O OE1  . GLU A 1 243 ? 29.887  8.877   73.729  1.00 128.62 ? 243 GLU A OE1  1 
ATOM   3870  O OE2  . GLU A 1 243 ? 31.940  8.108   73.630  1.00 130.03 ? 243 GLU A OE2  1 
ATOM   3871  H H    . GLU A 1 243 ? 27.399  4.048   75.138  1.00 132.68 ? 243 GLU A H    1 
ATOM   3872  H HA   . GLU A 1 243 ? 29.783  4.751   76.173  1.00 138.49 ? 243 GLU A HA   1 
ATOM   3873  H HB2  . GLU A 1 243 ? 29.454  5.794   73.935  1.00 143.83 ? 243 GLU A HB2  1 
ATOM   3874  H HB3  . GLU A 1 243 ? 28.487  6.772   74.732  1.00 143.83 ? 243 GLU A HB3  1 
ATOM   3875  H HG2  . GLU A 1 243 ? 30.248  7.538   75.995  1.00 149.10 ? 243 GLU A HG2  1 
ATOM   3876  H HG3  . GLU A 1 243 ? 31.229  6.497   75.302  1.00 149.10 ? 243 GLU A HG3  1 
ATOM   3877  N N    . ASN A 1 244 ? 28.671  5.711   78.119  1.00 111.57 ? 244 ASN A N    1 
ATOM   3878  C CA   . ASN A 1 244 ? 27.931  6.110   79.313  1.00 110.90 ? 244 ASN A CA   1 
ATOM   3879  C C    . ASN A 1 244 ? 26.661  5.276   79.458  1.00 108.91 ? 244 ASN A C    1 
ATOM   3880  O O    . ASN A 1 244 ? 25.583  5.788   79.770  1.00 109.72 ? 244 ASN A O    1 
ATOM   3881  C CB   . ASN A 1 244 ? 27.600  7.603   79.288  1.00 109.65 ? 244 ASN A CB   1 
ATOM   3882  C CG   . ASN A 1 244 ? 27.088  8.110   80.627  1.00 114.32 ? 244 ASN A CG   1 
ATOM   3883  O OD1  . ASN A 1 244 ? 25.884  8.108   80.886  1.00 114.93 ? 244 ASN A OD1  1 
ATOM   3884  N ND2  . ASN A 1 244 ? 28.005  8.542   81.487  1.00 113.20 ? 244 ASN A ND2  1 
ATOM   3885  H H    . ASN A 1 244 ? 29.506  5.561   78.261  1.00 133.89 ? 244 ASN A H    1 
ATOM   3886  H HA   . ASN A 1 244 ? 28.489  5.947   80.089  1.00 133.08 ? 244 ASN A HA   1 
ATOM   3887  H HB2  . ASN A 1 244 ? 28.401  8.102   79.064  1.00 131.58 ? 244 ASN A HB2  1 
ATOM   3888  H HB3  . ASN A 1 244 ? 26.913  7.764   78.623  1.00 131.58 ? 244 ASN A HB3  1 
ATOM   3889  H HD21 . ASN A 1 244 ? 28.838  8.525   81.272  1.00 135.84 ? 244 ASN A HD21 1 
ATOM   3890  H HD22 . ASN A 1 244 ? 27.766  8.839   82.258  1.00 135.84 ? 244 ASN A HD22 1 
ATOM   3891  N N    . ASP A 1 245 ? 26.790  3.973   79.221  1.00 106.46 ? 245 ASP A N    1 
ATOM   3892  C CA   . ASP A 1 245 ? 25.654  3.057   79.252  1.00 106.67 ? 245 ASP A CA   1 
ATOM   3893  C C    . ASP A 1 245 ? 24.528  3.557   78.345  1.00 104.55 ? 245 ASP A C    1 
ATOM   3894  O O    . ASP A 1 245 ? 23.359  3.619   78.733  1.00 108.02 ? 245 ASP A O    1 
ATOM   3895  C CB   . ASP A 1 245 ? 25.163  2.856   80.689  1.00 110.67 ? 245 ASP A CB   1 
ATOM   3896  C CG   . ASP A 1 245 ? 26.276  2.426   81.632  1.00 115.81 ? 245 ASP A CG   1 
ATOM   3897  O OD1  . ASP A 1 245 ? 27.361  2.055   81.137  1.00 120.82 ? 245 ASP A OD1  1 
ATOM   3898  O OD2  . ASP A 1 245 ? 26.072  2.461   82.865  1.00 114.08 ? 245 ASP A OD2  1 
ATOM   3899  H H    . ASP A 1 245 ? 27.538  3.590   79.037  1.00 127.75 ? 245 ASP A H    1 
ATOM   3900  H HA   . ASP A 1 245 ? 25.940  2.195   78.911  1.00 128.01 ? 245 ASP A HA   1 
ATOM   3901  H HB2  . ASP A 1 245 ? 24.795  3.691   81.018  1.00 132.81 ? 245 ASP A HB2  1 
ATOM   3902  H HB3  . ASP A 1 245 ? 24.480  2.167   80.696  1.00 132.81 ? 245 ASP A HB3  1 
ATOM   3903  N N    . GLU A 1 246 ? 24.892  3.917   77.114  1.00 102.22 ? 246 GLU A N    1 
ATOM   3904  C CA   . GLU A 1 246 ? 23.927  4.334   76.103  1.00 98.90  ? 246 GLU A CA   1 
ATOM   3905  C C    . GLU A 1 246 ? 24.341  3.746   74.763  1.00 92.71  ? 246 GLU A C    1 
ATOM   3906  O O    . GLU A 1 246 ? 25.513  3.826   74.384  1.00 93.16  ? 246 GLU A O    1 
ATOM   3907  C CB   . GLU A 1 246 ? 23.835  5.863   76.012  1.00 97.06  ? 246 GLU A CB   1 
ATOM   3908  C CG   . GLU A 1 246 ? 23.275  6.522   77.266  1.00 102.30 ? 246 GLU A CG   1 
ATOM   3909  C CD   . GLU A 1 246 ? 22.297  7.645   76.963  1.00 105.20 ? 246 GLU A CD   1 
ATOM   3910  O OE1  . GLU A 1 246 ? 21.090  7.356   76.815  1.00 105.75 ? 246 GLU A OE1  1 
ATOM   3911  O OE2  . GLU A 1 246 ? 22.736  8.815   76.880  1.00 105.37 ? 246 GLU A OE2  1 
ATOM   3912  H H    . GLU A 1 246 ? 25.707  3.928   76.838  1.00 122.67 ? 246 GLU A H    1 
ATOM   3913  H HA   . GLU A 1 246 ? 23.047  3.996   76.331  1.00 118.69 ? 246 GLU A HA   1 
ATOM   3914  H HB2  . GLU A 1 246 ? 24.724  6.220   75.862  1.00 116.48 ? 246 GLU A HB2  1 
ATOM   3915  H HB3  . GLU A 1 246 ? 23.254  6.096   75.271  1.00 116.48 ? 246 GLU A HB3  1 
ATOM   3916  H HG2  . GLU A 1 246 ? 22.808  5.853   77.791  1.00 122.76 ? 246 GLU A HG2  1 
ATOM   3917  H HG3  . GLU A 1 246 ? 24.008  6.894   77.780  1.00 122.76 ? 246 GLU A HG3  1 
ATOM   3918  N N    . MET A 1 247 ? 23.382  3.163   74.048  1.00 89.67  ? 247 MET A N    1 
ATOM   3919  C CA   . MET A 1 247 ? 23.667  2.489   72.787  1.00 86.62  ? 247 MET A CA   1 
ATOM   3920  C C    . MET A 1 247 ? 23.464  3.443   71.615  1.00 85.73  ? 247 MET A C    1 
ATOM   3921  O O    . MET A 1 247 ? 22.455  4.155   71.550  1.00 85.17  ? 247 MET A O    1 
ATOM   3922  C CB   . MET A 1 247 ? 22.779  1.255   72.621  1.00 82.74  ? 247 MET A CB   1 
ATOM   3923  C CG   . MET A 1 247 ? 22.954  0.535   71.283  1.00 83.82  ? 247 MET A CG   1 
ATOM   3924  S SD   . MET A 1 247 ? 24.600  -0.163  71.042  1.00 84.42  ? 247 MET A SD   1 
ATOM   3925  C CE   . MET A 1 247 ? 24.404  -1.763  71.825  1.00 79.98  ? 247 MET A CE   1 
ATOM   3926  H H    . MET A 1 247 ? 22.552  3.145   74.274  1.00 107.60 ? 247 MET A H    1 
ATOM   3927  H HA   . MET A 1 247 ? 24.592  2.198   72.796  1.00 103.94 ? 247 MET A HA   1 
ATOM   3928  H HB2  . MET A 1 247 ? 22.991  0.623   73.325  1.00 99.29  ? 247 MET A HB2  1 
ATOM   3929  H HB3  . MET A 1 247 ? 21.851  1.529   72.688  1.00 99.29  ? 247 MET A HB3  1 
ATOM   3930  H HG2  . MET A 1 247 ? 22.315  -0.193  71.234  1.00 100.58 ? 247 MET A HG2  1 
ATOM   3931  H HG3  . MET A 1 247 ? 22.793  1.167   70.564  1.00 100.58 ? 247 MET A HG3  1 
ATOM   3932  H HE1  . MET A 1 247 ? 25.183  -2.308  71.630  1.00 95.97  ? 247 MET A HE1  1 
ATOM   3933  H HE2  . MET A 1 247 ? 24.320  -1.638  72.783  1.00 95.97  ? 247 MET A HE2  1 
ATOM   3934  H HE3  . MET A 1 247 ? 23.606  -2.190  71.476  1.00 95.97  ? 247 MET A HE3  1 
ATOM   3935  N N    . TYR A 1 248 ? 24.412  3.437   70.686  1.00 84.45  ? 248 TYR A N    1 
ATOM   3936  C CA   . TYR A 1 248 ? 24.334  4.224   69.466  1.00 82.87  ? 248 TYR A CA   1 
ATOM   3937  C C    . TYR A 1 248 ? 24.738  3.346   68.293  1.00 80.85  ? 248 TYR A C    1 
ATOM   3938  O O    . TYR A 1 248 ? 25.637  2.508   68.415  1.00 78.82  ? 248 TYR A O    1 
ATOM   3939  C CB   . TYR A 1 248 ? 25.240  5.458   69.534  1.00 82.73  ? 248 TYR A CB   1 
ATOM   3940  C CG   . TYR A 1 248 ? 24.945  6.361   70.711  1.00 86.77  ? 248 TYR A CG   1 
ATOM   3941  C CD1  . TYR A 1 248 ? 23.992  7.364   70.620  1.00 84.29  ? 248 TYR A CD1  1 
ATOM   3942  C CD2  . TYR A 1 248 ? 25.623  6.208   71.912  1.00 89.64  ? 248 TYR A CD2  1 
ATOM   3943  C CE1  . TYR A 1 248 ? 23.718  8.187   71.694  1.00 85.95  ? 248 TYR A CE1  1 
ATOM   3944  C CE2  . TYR A 1 248 ? 25.360  7.028   72.990  1.00 90.13  ? 248 TYR A CE2  1 
ATOM   3945  C CZ   . TYR A 1 248 ? 24.405  8.015   72.876  1.00 87.88  ? 248 TYR A CZ   1 
ATOM   3946  O OH   . TYR A 1 248 ? 24.138  8.833   73.949  1.00 93.37  ? 248 TYR A OH   1 
ATOM   3947  H H    . TYR A 1 248 ? 25.132  2.971   70.744  1.00 101.33 ? 248 TYR A H    1 
ATOM   3948  H HA   . TYR A 1 248 ? 23.425  4.532   69.328  1.00 99.44  ? 248 TYR A HA   1 
ATOM   3949  H HB2  . TYR A 1 248 ? 26.162  5.166   69.608  1.00 99.27  ? 248 TYR A HB2  1 
ATOM   3950  H HB3  . TYR A 1 248 ? 25.121  5.978   68.724  1.00 99.27  ? 248 TYR A HB3  1 
ATOM   3951  H HD1  . TYR A 1 248 ? 23.528  7.483   69.823  1.00 101.14 ? 248 TYR A HD1  1 
ATOM   3952  H HD2  . TYR A 1 248 ? 26.267  5.541   71.991  1.00 107.57 ? 248 TYR A HD2  1 
ATOM   3953  H HE1  . TYR A 1 248 ? 23.074  8.854   71.620  1.00 103.14 ? 248 TYR A HE1  1 
ATOM   3954  H HE2  . TYR A 1 248 ? 25.824  6.914   73.789  1.00 108.16 ? 248 TYR A HE2  1 
ATOM   3955  H HH   . TYR A 1 248 ? 24.614  8.612   74.605  1.00 112.05 ? 248 TYR A HH   1 
ATOM   3956  N N    . ILE A 1 249 ? 24.070  3.539   67.157  1.00 79.01  ? 249 ILE A N    1 
ATOM   3957  C CA   . ILE A 1 249 ? 24.377  2.821   65.924  1.00 78.19  ? 249 ILE A CA   1 
ATOM   3958  C C    . ILE A 1 249 ? 24.760  3.846   64.866  1.00 77.44  ? 249 ILE A C    1 
ATOM   3959  O O    . ILE A 1 249 ? 23.952  4.717   64.514  1.00 76.94  ? 249 ILE A O    1 
ATOM   3960  C CB   . ILE A 1 249 ? 23.196  1.955   65.451  1.00 78.23  ? 249 ILE A CB   1 
ATOM   3961  C CG1  . ILE A 1 249 ? 23.194  0.613   66.193  1.00 73.24  ? 249 ILE A CG1  1 
ATOM   3962  C CG2  . ILE A 1 249 ? 23.253  1.738   63.937  1.00 75.96  ? 249 ILE A CG2  1 
ATOM   3963  C CD1  . ILE A 1 249 ? 24.150  -0.417  65.615  1.00 74.22  ? 249 ILE A CD1  1 
ATOM   3964  H H    . ILE A 1 249 ? 23.419  4.095   67.076  1.00 94.81  ? 249 ILE A H    1 
ATOM   3965  H HA   . ILE A 1 249 ? 25.138  2.238   66.074  1.00 93.82  ? 249 ILE A HA   1 
ATOM   3966  H HB   . ILE A 1 249 ? 22.371  2.424   65.657  1.00 93.88  ? 249 ILE A HB   1 
ATOM   3967  H HG12 . ILE A 1 249 ? 23.451  0.768   67.116  1.00 87.88  ? 249 ILE A HG12 1 
ATOM   3968  H HG13 . ILE A 1 249 ? 22.300  0.238   66.156  1.00 87.88  ? 249 ILE A HG13 1 
ATOM   3969  H HG21 . ILE A 1 249 ? 22.672  0.998   63.702  1.00 91.14  ? 249 ILE A HG21 1 
ATOM   3970  H HG22 . ILE A 1 249 ? 22.955  2.547   63.490  1.00 91.14  ? 249 ILE A HG22 1 
ATOM   3971  H HG23 . ILE A 1 249 ? 24.166  1.536   63.681  1.00 91.14  ? 249 ILE A HG23 1 
ATOM   3972  H HD11 . ILE A 1 249 ? 24.278  -1.128  66.262  1.00 89.06  ? 249 ILE A HD11 1 
ATOM   3973  H HD12 . ILE A 1 249 ? 23.770  -0.777  64.798  1.00 89.06  ? 249 ILE A HD12 1 
ATOM   3974  H HD13 . ILE A 1 249 ? 24.999  0.013   65.423  1.00 89.06  ? 249 ILE A HD13 1 
ATOM   3975  N N    . ASP A 1 250 ? 25.988  3.746   64.365  1.00 77.58  ? 250 ASP A N    1 
ATOM   3976  C CA   . ASP A 1 250 ? 26.477  4.573   63.272  1.00 76.28  ? 250 ASP A CA   1 
ATOM   3977  C C    . ASP A 1 250 ? 26.578  3.728   62.007  1.00 77.68  ? 250 ASP A C    1 
ATOM   3978  O O    . ASP A 1 250 ? 26.755  2.507   62.073  1.00 81.35  ? 250 ASP A O    1 
ATOM   3979  C CB   . ASP A 1 250 ? 27.847  5.182   63.600  1.00 77.33  ? 250 ASP A CB   1 
ATOM   3980  C CG   . ASP A 1 250 ? 28.200  6.354   62.695  1.00 78.79  ? 250 ASP A CG   1 
ATOM   3981  O OD1  . ASP A 1 250 ? 27.294  6.891   62.026  1.00 78.61  ? 250 ASP A OD1  1 
ATOM   3982  O OD2  . ASP A 1 250 ? 29.385  6.750   62.650  1.00 78.44  ? 250 ASP A OD2  1 
ATOM   3983  H H    . ASP A 1 250 ? 26.575  3.187   64.653  1.00 93.10  ? 250 ASP A H    1 
ATOM   3984  H HA   . ASP A 1 250 ? 25.860  5.304   63.112  1.00 91.53  ? 250 ASP A HA   1 
ATOM   3985  H HB2  . ASP A 1 250 ? 27.839  5.501   64.516  1.00 92.79  ? 250 ASP A HB2  1 
ATOM   3986  H HB3  . ASP A 1 250 ? 28.529  4.502   63.492  1.00 92.79  ? 250 ASP A HB3  1 
ATOM   3987  N N    . GLY A 1 251 ? 26.467  4.385   60.851  1.00 77.45  ? 251 GLY A N    1 
ATOM   3988  C CA   . GLY A 1 251 ? 26.607  3.709   59.580  1.00 76.49  ? 251 GLY A CA   1 
ATOM   3989  C C    . GLY A 1 251 ? 26.529  4.633   58.382  1.00 78.76  ? 251 GLY A C    1 
ATOM   3990  O O    . GLY A 1 251 ? 26.180  5.811   58.494  1.00 77.79  ? 251 GLY A O    1 
ATOM   3991  H H    . GLY A 1 251 ? 26.310  5.228   60.785  1.00 92.94  ? 251 GLY A H    1 
ATOM   3992  H HA2  . GLY A 1 251 ? 27.466  3.259   59.556  1.00 91.79  ? 251 GLY A HA2  1 
ATOM   3993  H HA3  . GLY A 1 251 ? 25.902  3.048   59.495  1.00 91.79  ? 251 GLY A HA3  1 
ATOM   3994  N N    . PRO A 1 252 ? 26.861  4.111   57.206  1.00 75.53  ? 252 PRO A N    1 
ATOM   3995  C CA   . PRO A 1 252 ? 26.735  4.915   55.985  1.00 78.21  ? 252 PRO A CA   1 
ATOM   3996  C C    . PRO A 1 252 ? 25.300  5.016   55.492  1.00 76.01  ? 252 PRO A C    1 
ATOM   3997  O O    . PRO A 1 252 ? 24.466  4.138   55.727  1.00 73.79  ? 252 PRO A O    1 
ATOM   3998  C CB   . PRO A 1 252 ? 27.607  4.177   54.961  1.00 73.97  ? 252 PRO A CB   1 
ATOM   3999  C CG   . PRO A 1 252 ? 28.204  3.015   55.646  1.00 77.22  ? 252 PRO A CG   1 
ATOM   4000  C CD   . PRO A 1 252 ? 27.671  2.883   57.027  1.00 77.77  ? 252 PRO A CD   1 
ATOM   4001  H HA   . PRO A 1 252 ? 27.092  5.805   56.139  1.00 93.85  ? 252 PRO A HA   1 
ATOM   4002  H HB2  . PRO A 1 252 ? 27.053  3.885   54.220  1.00 88.77  ? 252 PRO A HB2  1 
ATOM   4003  H HB3  . PRO A 1 252 ? 28.301  4.775   54.641  1.00 88.77  ? 252 PRO A HB3  1 
ATOM   4004  H HG2  . PRO A 1 252 ? 27.991  2.217   55.138  1.00 92.66  ? 252 PRO A HG2  1 
ATOM   4005  H HG3  . PRO A 1 252 ? 29.165  3.140   55.680  1.00 92.66  ? 252 PRO A HG3  1 
ATOM   4006  H HD2  . PRO A 1 252 ? 27.117  2.091   57.107  1.00 93.33  ? 252 PRO A HD2  1 
ATOM   4007  H HD3  . PRO A 1 252 ? 28.394  2.850   57.673  1.00 93.33  ? 252 PRO A HD3  1 
ATOM   4008  N N    . VAL A 1 253 ? 25.030  6.117   54.787  1.00 75.23  ? 253 VAL A N    1 
ATOM   4009  C CA   . VAL A 1 253 ? 23.733  6.379   54.177  1.00 73.90  ? 253 VAL A CA   1 
ATOM   4010  C C    . VAL A 1 253 ? 23.975  7.039   52.825  1.00 74.02  ? 253 VAL A C    1 
ATOM   4011  O O    . VAL A 1 253 ? 24.954  7.770   52.634  1.00 73.65  ? 253 VAL A O    1 
ATOM   4012  C CB   . VAL A 1 253 ? 22.842  7.265   55.070  1.00 72.39  ? 253 VAL A CB   1 
ATOM   4013  C CG1  . VAL A 1 253 ? 21.421  7.323   54.522  1.00 68.47  ? 253 VAL A CG1  1 
ATOM   4014  C CG2  . VAL A 1 253 ? 22.846  6.746   56.506  1.00 71.92  ? 253 VAL A CG2  1 
ATOM   4015  H H    . VAL A 1 253 ? 25.602  6.744   54.646  1.00 90.28  ? 253 VAL A H    1 
ATOM   4016  H HA   . VAL A 1 253 ? 23.265  5.542   54.034  1.00 88.68  ? 253 VAL A HA   1 
ATOM   4017  H HB   . VAL A 1 253 ? 23.198  8.168   55.073  1.00 86.87  ? 253 VAL A HB   1 
ATOM   4018  H HG11 . VAL A 1 253 ? 20.899  7.936   55.063  1.00 82.16  ? 253 VAL A HG11 1 
ATOM   4019  H HG12 . VAL A 1 253 ? 21.450  7.635   53.604  1.00 82.16  ? 253 VAL A HG12 1 
ATOM   4020  H HG13 . VAL A 1 253 ? 21.032  6.435   54.558  1.00 82.16  ? 253 VAL A HG13 1 
ATOM   4021  H HG21 . VAL A 1 253 ? 22.179  7.230   57.019  1.00 86.30  ? 253 VAL A HG21 1 
ATOM   4022  H HG22 . VAL A 1 253 ? 22.635  5.799   56.500  1.00 86.30  ? 253 VAL A HG22 1 
ATOM   4023  H HG23 . VAL A 1 253 ? 23.725  6.887   56.890  1.00 86.30  ? 253 VAL A HG23 1 
ATOM   4024  N N    . GLU A 1 254 ? 23.079  6.771   51.875  1.00 73.53  ? 254 GLU A N    1 
ATOM   4025  C CA   . GLU A 1 254 ? 23.240  7.297   50.522  1.00 73.58  ? 254 GLU A CA   1 
ATOM   4026  C C    . GLU A 1 254 ? 21.882  7.555   49.895  1.00 72.78  ? 254 GLU A C    1 
ATOM   4027  O O    . GLU A 1 254 ? 21.063  6.637   49.787  1.00 69.05  ? 254 GLU A O    1 
ATOM   4028  C CB   . GLU A 1 254 ? 24.050  6.340   49.650  1.00 71.20  ? 254 GLU A CB   1 
ATOM   4029  C CG   . GLU A 1 254 ? 24.507  6.973   48.344  1.00 76.02  ? 254 GLU A CG   1 
ATOM   4030  C CD   . GLU A 1 254 ? 25.264  6.008   47.451  1.00 77.86  ? 254 GLU A CD   1 
ATOM   4031  O OE1  . GLU A 1 254 ? 25.850  5.033   47.973  1.00 77.47  ? 254 GLU A OE1  1 
ATOM   4032  O OE2  . GLU A 1 254 ? 25.275  6.230   46.222  1.00 78.89  ? 254 GLU A OE2  1 
ATOM   4033  H H    . GLU A 1 254 ? 22.375  6.290   51.989  1.00 88.24  ? 254 GLU A H    1 
ATOM   4034  H HA   . GLU A 1 254 ? 23.705  8.147   50.581  1.00 88.29  ? 254 GLU A HA   1 
ATOM   4035  H HB2  . GLU A 1 254 ? 24.839  6.060   50.140  1.00 85.44  ? 254 GLU A HB2  1 
ATOM   4036  H HB3  . GLU A 1 254 ? 23.501  5.570   49.434  1.00 85.44  ? 254 GLU A HB3  1 
ATOM   4037  H HG2  . GLU A 1 254 ? 23.729  7.284   47.856  1.00 91.22  ? 254 GLU A HG2  1 
ATOM   4038  H HG3  . GLU A 1 254 ? 25.094  7.719   48.544  1.00 91.22  ? 254 GLU A HG3  1 
ATOM   4039  N N    . ILE A 1 255 ? 21.669  8.790   49.449  1.00 74.37  ? 255 ILE A N    1 
ATOM   4040  C CA   . ILE A 1 255 ? 20.432  9.170   48.776  1.00 71.86  ? 255 ILE A CA   1 
ATOM   4041  C C    . ILE A 1 255 ? 20.508  8.674   47.339  1.00 71.86  ? 255 ILE A C    1 
ATOM   4042  O O    . ILE A 1 255 ? 21.370  9.107   46.566  1.00 73.22  ? 255 ILE A O    1 
ATOM   4043  C CB   . ILE A 1 255 ? 20.212  10.688  48.831  1.00 72.14  ? 255 ILE A CB   1 
ATOM   4044  C CG1  . ILE A 1 255 ? 20.442  11.214  50.249  1.00 71.06  ? 255 ILE A CG1  1 
ATOM   4045  C CG2  . ILE A 1 255 ? 18.802  11.033  48.360  1.00 70.62  ? 255 ILE A CG2  1 
ATOM   4046  C CD1  . ILE A 1 255 ? 19.286  10.954  51.212  1.00 72.11  ? 255 ILE A CD1  1 
ATOM   4047  H H    . ILE A 1 255 ? 22.233  9.434   49.526  1.00 89.24  ? 255 ILE A H    1 
ATOM   4048  H HA   . ILE A 1 255 ? 19.678  8.744   49.215  1.00 86.23  ? 255 ILE A HA   1 
ATOM   4049  H HB   . ILE A 1 255 ? 20.853  11.111  48.239  1.00 86.56  ? 255 ILE A HB   1 
ATOM   4050  H HG12 . ILE A 1 255 ? 21.231  10.784  50.615  1.00 85.27  ? 255 ILE A HG12 1 
ATOM   4051  H HG13 . ILE A 1 255 ? 20.578  12.174  50.206  1.00 85.27  ? 255 ILE A HG13 1 
ATOM   4052  H HG21 . ILE A 1 255 ? 18.610  11.956  48.587  1.00 84.74  ? 255 ILE A HG21 1 
ATOM   4053  H HG22 . ILE A 1 255 ? 18.752  10.912  47.399  1.00 84.74  ? 255 ILE A HG22 1 
ATOM   4054  H HG23 . ILE A 1 255 ? 18.169  10.445  48.801  1.00 84.74  ? 255 ILE A HG23 1 
ATOM   4055  H HD11 . ILE A 1 255 ? 19.605  11.051  52.123  1.00 86.53  ? 255 ILE A HD11 1 
ATOM   4056  H HD12 . ILE A 1 255 ? 18.580  11.596  51.038  1.00 86.53  ? 255 ILE A HD12 1 
ATOM   4057  H HD13 . ILE A 1 255 ? 18.955  10.053  51.072  1.00 86.53  ? 255 ILE A HD13 1 
ATOM   4058  N N    . ILE A 1 256 ? 19.612  7.759   46.980  1.00 71.93  ? 256 ILE A N    1 
ATOM   4059  C CA   . ILE A 1 256 ? 19.658  7.100   45.680  1.00 72.38  ? 256 ILE A CA   1 
ATOM   4060  C C    . ILE A 1 256 ? 18.979  7.967   44.632  1.00 73.80  ? 256 ILE A C    1 
ATOM   4061  O O    . ILE A 1 256 ? 19.626  8.457   43.699  1.00 73.16  ? 256 ILE A O    1 
ATOM   4062  C CB   . ILE A 1 256 ? 18.990  5.713   45.745  1.00 73.65  ? 256 ILE A CB   1 
ATOM   4063  C CG1  . ILE A 1 256 ? 19.890  4.717   46.471  1.00 72.51  ? 256 ILE A CG1  1 
ATOM   4064  C CG2  . ILE A 1 256 ? 18.656  5.193   44.344  1.00 73.49  ? 256 ILE A CG2  1 
ATOM   4065  C CD1  . ILE A 1 256 ? 19.122  3.706   47.273  1.00 71.96  ? 256 ILE A CD1  1 
ATOM   4066  H H    . ILE A 1 256 ? 18.960  7.501   47.478  1.00 86.32  ? 256 ILE A H    1 
ATOM   4067  H HA   . ILE A 1 256 ? 20.588  6.993   45.424  1.00 86.86  ? 256 ILE A HA   1 
ATOM   4068  H HB   . ILE A 1 256 ? 18.162  5.811   46.241  1.00 88.38  ? 256 ILE A HB   1 
ATOM   4069  H HG12 . ILE A 1 256 ? 20.422  4.238   45.816  1.00 87.01  ? 256 ILE A HG12 1 
ATOM   4070  H HG13 . ILE A 1 256 ? 20.470  5.202   47.079  1.00 87.01  ? 256 ILE A HG13 1 
ATOM   4071  H HG21 . ILE A 1 256 ? 18.270  4.306   44.419  1.00 88.18  ? 256 ILE A HG21 1 
ATOM   4072  H HG22 . ILE A 1 256 ? 18.021  5.795   43.926  1.00 88.18  ? 256 ILE A HG22 1 
ATOM   4073  H HG23 . ILE A 1 256 ? 19.471  5.155   43.819  1.00 88.18  ? 256 ILE A HG23 1 
ATOM   4074  H HD11 . ILE A 1 256 ? 19.745  3.075   47.666  1.00 86.35  ? 256 ILE A HD11 1 
ATOM   4075  H HD12 . ILE A 1 256 ? 18.630  4.165   47.972  1.00 86.35  ? 256 ILE A HD12 1 
ATOM   4076  H HD13 . ILE A 1 256 ? 18.505  3.240   46.687  1.00 86.35  ? 256 ILE A HD13 1 
ATOM   4077  N N    . ALA A 1 257 ? 17.666  8.140   44.767  1.00 73.87  ? 257 ALA A N    1 
ATOM   4078  C CA   . ALA A 1 257 ? 16.867  8.764   43.726  1.00 71.19  ? 257 ALA A CA   1 
ATOM   4079  C C    . ALA A 1 257 ? 15.728  9.544   44.361  1.00 70.00  ? 257 ALA A C    1 
ATOM   4080  O O    . ALA A 1 257 ? 15.410  9.376   45.542  1.00 71.26  ? 257 ALA A O    1 
ATOM   4081  C CB   . ALA A 1 257 ? 16.321  7.717   42.749  1.00 72.84  ? 257 ALA A CB   1 
ATOM   4082  H H    . ALA A 1 257 ? 17.215  7.902   45.459  1.00 88.65  ? 257 ALA A H    1 
ATOM   4083  H HA   . ALA A 1 257 ? 17.424  9.390   43.237  1.00 85.42  ? 257 ALA A HA   1 
ATOM   4084  H HB1  . ALA A 1 257 ? 15.790  8.164   42.071  1.00 87.40  ? 257 ALA A HB1  1 
ATOM   4085  H HB2  . ALA A 1 257 ? 17.065  7.254   42.334  1.00 87.40  ? 257 ALA A HB2  1 
ATOM   4086  H HB3  . ALA A 1 257 ? 15.770  7.086   43.238  1.00 87.40  ? 257 ALA A HB3  1 
ATOM   4087  N N    . GLU A 1 258 ? 15.096  10.385  43.544  1.00 67.73  ? 258 GLU A N    1 
ATOM   4088  C CA   . GLU A 1 258 ? 14.105  11.337  44.018  1.00 67.55  ? 258 GLU A CA   1 
ATOM   4089  C C    . GLU A 1 258 ? 13.128  11.647  42.899  1.00 70.31  ? 258 GLU A C    1 
ATOM   4090  O O    . GLU A 1 258 ? 13.541  11.863  41.756  1.00 69.13  ? 258 GLU A O    1 
ATOM   4091  C CB   . GLU A 1 258 ? 14.788  12.624  44.490  1.00 70.93  ? 258 GLU A CB   1 
ATOM   4092  C CG   . GLU A 1 258 ? 13.987  13.460  45.456  1.00 73.76  ? 258 GLU A CG   1 
ATOM   4093  C CD   . GLU A 1 258 ? 14.714  14.734  45.840  1.00 75.45  ? 258 GLU A CD   1 
ATOM   4094  O OE1  . GLU A 1 258 ? 15.893  14.888  45.447  1.00 72.38  ? 258 GLU A OE1  1 
ATOM   4095  O OE2  . GLU A 1 258 ? 14.112  15.578  46.537  1.00 80.37  ? 258 GLU A OE2  1 
ATOM   4096  H H    . GLU A 1 258 ? 15.229  10.421  42.695  1.00 81.28  ? 258 GLU A H    1 
ATOM   4097  H HA   . GLU A 1 258 ? 13.601  10.953  44.753  1.00 81.06  ? 258 GLU A HA   1 
ATOM   4098  H HB2  . GLU A 1 258 ? 15.618  12.386  44.932  1.00 85.11  ? 258 GLU A HB2  1 
ATOM   4099  H HB3  . GLU A 1 258 ? 14.972  13.175  43.714  1.00 85.11  ? 258 GLU A HB3  1 
ATOM   4100  H HG2  . GLU A 1 258 ? 13.143  13.704  45.043  1.00 88.52  ? 258 GLU A HG2  1 
ATOM   4101  H HG3  . GLU A 1 258 ? 13.825  12.947  46.264  1.00 88.52  ? 258 GLU A HG3  1 
ATOM   4102  N N    . GLY A 1 259 ? 11.838  11.671  43.232  1.00 64.40  ? 259 GLY A N    1 
ATOM   4103  C CA   . GLY A 1 259 ? 10.843  12.075  42.265  1.00 70.73  ? 259 GLY A CA   1 
ATOM   4104  C C    . GLY A 1 259 ? 9.436   11.577  42.508  1.00 77.71  ? 259 GLY A C    1 
ATOM   4105  O O    . GLY A 1 259 ? 8.960   11.556  43.643  1.00 69.53  ? 259 GLY A O    1 
ATOM   4106  H H    . GLY A 1 259 ? 11.526  11.458  44.004  1.00 77.29  ? 259 GLY A H    1 
ATOM   4107  H HA2  . GLY A 1 259 ? 10.809  13.044  42.249  1.00 84.87  ? 259 GLY A HA2  1 
ATOM   4108  H HA3  . GLY A 1 259 ? 11.117  11.754  41.392  1.00 84.87  ? 259 GLY A HA3  1 
ATOM   4109  N N    . LYS A 1 260 ? 8.760   11.174  41.427  1.00 70.95  ? 260 LYS A N    1 
ATOM   4110  C CA   . LYS A 1 260 ? 7.351   10.815  41.464  1.00 74.25  ? 260 LYS A CA   1 
ATOM   4111  C C    . LYS A 1 260 ? 7.172   9.318   41.245  1.00 76.59  ? 260 LYS A C    1 
ATOM   4112  O O    . LYS A 1 260 ? 7.940   8.679   40.520  1.00 75.01  ? 260 LYS A O    1 
ATOM   4113  C CB   . LYS A 1 260 ? 6.564   11.592  40.402  1.00 71.57  ? 260 LYS A CB   1 
ATOM   4114  C CG   . LYS A 1 260 ? 6.767   13.101  40.457  1.00 73.78  ? 260 LYS A CG   1 
ATOM   4115  C CD   . LYS A 1 260 ? 5.594   13.803  41.132  1.00 76.13  ? 260 LYS A CD   1 
ATOM   4116  C CE   . LYS A 1 260 ? 6.031   15.108  41.790  1.00 77.43  ? 260 LYS A CE   1 
ATOM   4117  N NZ   . LYS A 1 260 ? 4.909   15.782  42.500  1.00 77.94  ? 260 LYS A NZ   1 
ATOM   4118  H H    . LYS A 1 260 ? 9.111   11.101  40.645  1.00 85.14  ? 260 LYS A H    1 
ATOM   4119  H HA   . LYS A 1 260 ? 6.988   11.031  42.337  1.00 89.10  ? 260 LYS A HA   1 
ATOM   4120  H HB2  . LYS A 1 260 ? 6.845   11.289  39.524  1.00 85.89  ? 260 LYS A HB2  1 
ATOM   4121  H HB3  . LYS A 1 260 ? 5.619   11.417  40.527  1.00 85.89  ? 260 LYS A HB3  1 
ATOM   4122  H HG2  . LYS A 1 260 ? 7.571   13.298  40.962  1.00 88.54  ? 260 LYS A HG2  1 
ATOM   4123  H HG3  . LYS A 1 260 ? 6.849   13.446  39.554  1.00 88.54  ? 260 LYS A HG3  1 
ATOM   4124  H HD2  . LYS A 1 260 ? 4.917   14.007  40.469  1.00 91.36  ? 260 LYS A HD2  1 
ATOM   4125  H HD3  . LYS A 1 260 ? 5.225   13.224  41.817  1.00 91.36  ? 260 LYS A HD3  1 
ATOM   4126  H HE2  . LYS A 1 260 ? 6.729   14.921  42.437  1.00 92.92  ? 260 LYS A HE2  1 
ATOM   4127  H HE3  . LYS A 1 260 ? 6.364   15.712  41.108  1.00 92.92  ? 260 LYS A HE3  1 
ATOM   4128  H HZ1  . LYS A 1 260 ? 5.194   16.540  42.870  1.00 93.52  ? 260 LYS A HZ1  1 
ATOM   4129  H HZ2  . LYS A 1 260 ? 4.254   15.969  41.927  1.00 93.52  ? 260 LYS A HZ2  1 
ATOM   4130  H HZ3  . LYS A 1 260 ? 4.590   15.251  43.139  1.00 93.52  ? 260 LYS A HZ3  1 
ATOM   4131  N N    . ILE A 1 261 ? 6.135   8.768   41.870  1.00 76.10  ? 261 ILE A N    1 
ATOM   4132  C CA   . ILE A 1 261 ? 5.820   7.348   41.788  1.00 77.51  ? 261 ILE A CA   1 
ATOM   4133  C C    . ILE A 1 261 ? 4.324   7.200   41.548  1.00 80.50  ? 261 ILE A C    1 
ATOM   4134  O O    . ILE A 1 261 ? 3.513   7.794   42.268  1.00 78.28  ? 261 ILE A O    1 
ATOM   4135  C CB   . ILE A 1 261 ? 6.266   6.614   43.065  1.00 76.17  ? 261 ILE A CB   1 
ATOM   4136  C CG1  . ILE A 1 261 ? 6.052   5.113   42.932  1.00 78.75  ? 261 ILE A CG1  1 
ATOM   4137  C CG2  . ILE A 1 261 ? 5.548   7.167   44.287  1.00 80.73  ? 261 ILE A CG2  1 
ATOM   4138  C CD1  . ILE A 1 261 ? 6.545   4.372   44.133  1.00 85.15  ? 261 ILE A CD1  1 
ATOM   4139  H H    . ILE A 1 261 ? 5.586   9.210   42.362  1.00 91.33  ? 261 ILE A H    1 
ATOM   4140  H HA   . ILE A 1 261 ? 6.273   6.945   41.031  1.00 93.02  ? 261 ILE A HA   1 
ATOM   4141  H HB   . ILE A 1 261 ? 7.216   6.769   43.181  1.00 91.40  ? 261 ILE A HB   1 
ATOM   4142  H HG12 . ILE A 1 261 ? 5.104   4.934   42.833  1.00 94.50  ? 261 ILE A HG12 1 
ATOM   4143  H HG13 . ILE A 1 261 ? 6.535   4.790   42.156  1.00 94.50  ? 261 ILE A HG13 1 
ATOM   4144  H HG21 . ILE A 1 261 ? 5.976   6.823   45.087  1.00 96.87  ? 261 ILE A HG21 1 
ATOM   4145  H HG22 . ILE A 1 261 ? 5.601   8.135   44.274  1.00 96.87  ? 261 ILE A HG22 1 
ATOM   4146  H HG23 . ILE A 1 261 ? 4.620   6.886   44.262  1.00 96.87  ? 261 ILE A HG23 1 
ATOM   4147  H HD11 . ILE A 1 261 ? 6.448   3.420   43.977  1.00 102.18 ? 261 ILE A HD11 1 
ATOM   4148  H HD12 . ILE A 1 261 ? 7.479   4.590   44.277  1.00 102.18 ? 261 ILE A HD12 1 
ATOM   4149  H HD13 . ILE A 1 261 ? 6.020   4.636   44.904  1.00 102.18 ? 261 ILE A HD13 1 
ATOM   4150  N N    . TYR A 1 262 ? 3.964   6.417   40.527  1.00 81.10  ? 262 TYR A N    1 
ATOM   4151  C CA   . TYR A 1 262 ? 2.586   6.304   40.056  1.00 84.38  ? 262 TYR A CA   1 
ATOM   4152  C C    . TYR A 1 262 ? 2.015   4.952   40.483  1.00 89.02  ? 262 TYR A C    1 
ATOM   4153  O O    . TYR A 1 262 ? 2.487   3.901   40.032  1.00 86.41  ? 262 TYR A O    1 
ATOM   4154  C CB   . TYR A 1 262 ? 2.523   6.475   38.536  1.00 80.68  ? 262 TYR A CB   1 
ATOM   4155  C CG   . TYR A 1 262 ? 3.260   7.696   38.012  1.00 80.62  ? 262 TYR A CG   1 
ATOM   4156  C CD1  . TYR A 1 262 ? 2.807   8.979   38.292  1.00 80.44  ? 262 TYR A CD1  1 
ATOM   4157  C CD2  . TYR A 1 262 ? 4.404   7.564   37.229  1.00 79.25  ? 262 TYR A CD2  1 
ATOM   4158  C CE1  . TYR A 1 262 ? 3.473   10.095  37.815  1.00 78.93  ? 262 TYR A CE1  1 
ATOM   4159  C CE2  . TYR A 1 262 ? 5.078   8.677   36.747  1.00 76.16  ? 262 TYR A CE2  1 
ATOM   4160  C CZ   . TYR A 1 262 ? 4.606   9.938   37.045  1.00 76.27  ? 262 TYR A CZ   1 
ATOM   4161  O OH   . TYR A 1 262 ? 5.266   11.048  36.575  1.00 78.41  ? 262 TYR A OH   1 
ATOM   4162  H H    . TYR A 1 262 ? 4.516   5.929   40.084  1.00 97.32  ? 262 TYR A H    1 
ATOM   4163  H HA   . TYR A 1 262 ? 2.050   6.997   40.474  1.00 101.26 ? 262 TYR A HA   1 
ATOM   4164  H HB2  . TYR A 1 262 ? 2.918   5.693   38.120  1.00 96.82  ? 262 TYR A HB2  1 
ATOM   4165  H HB3  . TYR A 1 262 ? 1.594   6.558   38.272  1.00 96.82  ? 262 TYR A HB3  1 
ATOM   4166  H HD1  . TYR A 1 262 ? 2.042   9.090   38.808  1.00 96.53  ? 262 TYR A HD1  1 
ATOM   4167  H HD2  . TYR A 1 262 ? 4.722   6.714   37.025  1.00 95.11  ? 262 TYR A HD2  1 
ATOM   4168  H HE1  . TYR A 1 262 ? 3.158   10.947  38.014  1.00 94.72  ? 262 TYR A HE1  1 
ATOM   4169  H HE2  . TYR A 1 262 ? 5.841   8.573   36.226  1.00 91.39  ? 262 TYR A HE2  1 
ATOM   4170  H HH   . TYR A 1 262 ? 5.939   10.815  36.129  1.00 94.10  ? 262 TYR A HH   1 
ATOM   4171  N N    . ILE A 1 263 ? 0.995   4.986   41.348  1.00 95.91  ? 263 ILE A N    1 
ATOM   4172  C CA   . ILE A 1 263 ? 0.281   3.805   41.822  1.00 98.20  ? 263 ILE A CA   1 
ATOM   4173  C C    . ILE A 1 263 ? -1.207  4.056   41.627  1.00 101.93 ? 263 ILE A C    1 
ATOM   4174  O O    . ILE A 1 263 ? -1.633  5.159   41.284  1.00 104.83 ? 263 ILE A O    1 
ATOM   4175  C CB   . ILE A 1 263 ? 0.618   3.494   43.303  1.00 102.25 ? 263 ILE A CB   1 
ATOM   4176  C CG1  . ILE A 1 263 ? 2.066   2.992   43.425  1.00 99.91  ? 263 ILE A CG1  1 
ATOM   4177  C CG2  . ILE A 1 263 ? -0.337  2.474   43.917  1.00 106.04 ? 263 ILE A CG2  1 
ATOM   4178  C CD1  . ILE A 1 263 ? 2.209   1.466   43.419  1.00 106.05 ? 263 ILE A CD1  1 
ATOM   4179  H H    . ILE A 1 263 ? 0.688   5.715   41.686  1.00 115.09 ? 263 ILE A H    1 
ATOM   4180  H HA   . ILE A 1 263 ? 0.523   3.027   41.295  1.00 117.83 ? 263 ILE A HA   1 
ATOM   4181  H HB   . ILE A 1 263 ? 0.514   4.324   43.795  1.00 122.70 ? 263 ILE A HB   1 
ATOM   4182  H HG12 . ILE A 1 263 ? 2.577   3.338   42.677  1.00 119.90 ? 263 ILE A HG12 1 
ATOM   4183  H HG13 . ILE A 1 263 ? 2.437   3.319   44.260  1.00 119.90 ? 263 ILE A HG13 1 
ATOM   4184  H HG21 . ILE A 1 263 ? 0.039   2.151   44.751  1.00 127.25 ? 263 ILE A HG21 1 
ATOM   4185  H HG22 . ILE A 1 263 ? -1.192  2.901   44.082  1.00 127.25 ? 263 ILE A HG22 1 
ATOM   4186  H HG23 . ILE A 1 263 ? -0.450  1.736   43.297  1.00 127.25 ? 263 ILE A HG23 1 
ATOM   4187  H HD11 . ILE A 1 263 ? 3.139   1.237   43.265  1.00 127.26 ? 263 ILE A HD11 1 
ATOM   4188  H HD12 . ILE A 1 263 ? 1.921   1.118   44.277  1.00 127.26 ? 263 ILE A HD12 1 
ATOM   4189  H HD13 . ILE A 1 263 ? 1.656   1.100   42.711  1.00 127.26 ? 263 ILE A HD13 1 
ATOM   4190  N N    . GLY A 1 264 ? -2.007  2.999   41.817  1.00 108.59 ? 264 GLY A N    1 
ATOM   4191  C CA   . GLY A 1 264 ? -3.449  3.131   41.772  1.00 113.86 ? 264 GLY A CA   1 
ATOM   4192  C C    . GLY A 1 264 ? -4.040  3.738   43.039  1.00 121.20 ? 264 GLY A C    1 
ATOM   4193  O O    . GLY A 1 264 ? -3.377  3.894   44.065  1.00 118.41 ? 264 GLY A O    1 
ATOM   4194  H H    . GLY A 1 264 ? -1.731  2.200   41.974  1.00 130.30 ? 264 GLY A H    1 
ATOM   4195  H HA2  . GLY A 1 264 ? -3.693  3.699   41.024  1.00 136.63 ? 264 GLY A HA2  1 
ATOM   4196  H HA3  . GLY A 1 264 ? -3.844  2.255   41.645  1.00 136.63 ? 264 GLY A HA3  1 
ATOM   4197  N N    . LYS A 1 265 ? -5.326  4.080   42.952  1.00 136.05 ? 265 LYS A N    1 
ATOM   4198  C CA   . LYS A 1 265 ? -6.040  4.712   44.059  1.00 136.08 ? 265 LYS A CA   1 
ATOM   4199  C C    . LYS A 1 265 ? -7.275  3.906   44.453  1.00 136.03 ? 265 LYS A C    1 
ATOM   4200  O O    . LYS A 1 265 ? -7.666  3.877   45.621  1.00 136.05 ? 265 LYS A O    1 
ATOM   4201  C CB   . LYS A 1 265 ? -6.453  6.141   43.684  1.00 132.04 ? 265 LYS A CB   1 
ATOM   4202  C CG   . LYS A 1 265 ? -7.013  6.968   44.838  1.00 128.60 ? 265 LYS A CG   1 
ATOM   4203  C CD   . LYS A 1 265 ? -6.435  8.380   44.834  1.00 125.02 ? 265 LYS A CD   1 
ATOM   4204  C CE   . LYS A 1 265 ? -7.280  9.340   45.659  1.00 125.27 ? 265 LYS A CE   1 
ATOM   4205  N NZ   . LYS A 1 265 ? -6.560  9.807   46.878  1.00 124.81 ? 265 LYS A NZ   1 
ATOM   4206  H H    . LYS A 1 265 ? -5.813  3.954   42.253  1.00 163.26 ? 265 LYS A H    1 
ATOM   4207  H HA   . LYS A 1 265 ? -5.449  4.755   44.827  1.00 163.30 ? 265 LYS A HA   1 
ATOM   4208  H HB2  . LYS A 1 265 ? -5.673  6.607   43.343  1.00 158.45 ? 265 LYS A HB2  1 
ATOM   4209  H HB3  . LYS A 1 265 ? -7.137  6.094   42.999  1.00 158.45 ? 265 LYS A HB3  1 
ATOM   4210  H HG2  . LYS A 1 265 ? -7.977  7.032   44.751  1.00 154.32 ? 265 LYS A HG2  1 
ATOM   4211  H HG3  . LYS A 1 265 ? -6.783  6.545   45.680  1.00 154.32 ? 265 LYS A HG3  1 
ATOM   4212  H HD2  . LYS A 1 265 ? -5.541  8.362   45.211  1.00 150.02 ? 265 LYS A HD2  1 
ATOM   4213  H HD3  . LYS A 1 265 ? -6.404  8.711   43.922  1.00 150.02 ? 265 LYS A HD3  1 
ATOM   4214  H HE2  . LYS A 1 265 ? -7.501  10.116  45.121  1.00 150.33 ? 265 LYS A HE2  1 
ATOM   4215  H HE3  . LYS A 1 265 ? -8.092  8.889   45.941  1.00 150.33 ? 265 LYS A HE3  1 
ATOM   4216  H HZ1  . LYS A 1 265 ? -6.350  9.113   47.393  1.00 149.78 ? 265 LYS A HZ1  1 
ATOM   4217  H HZ2  . LYS A 1 265 ? -5.813  10.232  46.646  1.00 149.78 ? 265 LYS A HZ2  1 
ATOM   4218  H HZ3  . LYS A 1 265 ? -7.077  10.365  47.341  1.00 149.78 ? 265 LYS A HZ3  1 
ATOM   4219  N N    . ARG B 1 3   ? -9.558  30.374  32.687  1.00 122.25 ? 3   ARG B N    1 
ATOM   4220  C CA   . ARG B 1 3   ? -8.800  30.250  31.447  1.00 121.71 ? 3   ARG B CA   1 
ATOM   4221  C C    . ARG B 1 3   ? -7.964  28.974  31.450  1.00 118.46 ? 3   ARG B C    1 
ATOM   4222  O O    . ARG B 1 3   ? -7.406  28.588  32.477  1.00 121.92 ? 3   ARG B O    1 
ATOM   4223  C CB   . ARG B 1 3   ? -7.899  31.470  31.246  1.00 121.93 ? 3   ARG B CB   1 
ATOM   4224  C CG   . ARG B 1 3   ? -8.658  32.762  30.990  1.00 130.49 ? 3   ARG B CG   1 
ATOM   4225  C CD   . ARG B 1 3   ? -7.718  33.935  30.740  1.00 135.88 ? 3   ARG B CD   1 
ATOM   4226  N NE   . ARG B 1 3   ? -8.452  35.184  30.560  1.00 142.09 ? 3   ARG B NE   1 
ATOM   4227  C CZ   . ARG B 1 3   ? -7.891  36.382  30.460  1.00 141.94 ? 3   ARG B CZ   1 
ATOM   4228  N NH1  . ARG B 1 3   ? -6.579  36.539  30.513  1.00 139.96 ? 3   ARG B NH1  1 
ATOM   4229  N NH2  . ARG B 1 3   ? -8.668  37.450  30.304  1.00 140.67 ? 3   ARG B NH2  1 
ATOM   4230  H HA   . ARG B 1 3   ? -9.417  30.207  30.699  1.00 146.05 ? 3   ARG B HA   1 
ATOM   4231  H HB2  . ARG B 1 3   ? -7.362  31.595  32.044  1.00 146.31 ? 3   ARG B HB2  1 
ATOM   4232  H HB3  . ARG B 1 3   ? -7.324  31.309  30.481  1.00 146.31 ? 3   ARG B HB3  1 
ATOM   4233  H HG2  . ARG B 1 3   ? -9.220  32.652  30.207  1.00 156.59 ? 3   ARG B HG2  1 
ATOM   4234  H HG3  . ARG B 1 3   ? -9.204  32.970  31.764  1.00 156.59 ? 3   ARG B HG3  1 
ATOM   4235  H HD2  . ARG B 1 3   ? -7.124  34.037  31.500  1.00 163.05 ? 3   ARG B HD2  1 
ATOM   4236  H HD3  . ARG B 1 3   ? -7.202  33.767  29.936  1.00 163.05 ? 3   ARG B HD3  1 
ATOM   4237  H HE   . ARG B 1 3   ? -9.309  35.140  30.516  1.00 170.51 ? 3   ARG B HE   1 
ATOM   4238  H HH11 . ARG B 1 3   ? -6.068  35.855  30.615  1.00 167.96 ? 3   ARG B HH11 1 
ATOM   4239  H HH12 . ARG B 1 3   ? -6.237  37.326  30.446  1.00 167.96 ? 3   ARG B HH12 1 
ATOM   4240  H HH21 . ARG B 1 3   ? -9.522  37.359  30.269  1.00 168.81 ? 3   ARG B HH21 1 
ATOM   4241  H HH22 . ARG B 1 3   ? -8.316  38.232  30.238  1.00 168.81 ? 3   ARG B HH22 1 
ATOM   4242  N N    . LYS B 1 4   ? -7.881  28.319  30.297  1.00 118.76 ? 4   LYS B N    1 
ATOM   4243  C CA   . LYS B 1 4   ? -7.069  27.119  30.161  1.00 116.66 ? 4   LYS B CA   1 
ATOM   4244  C C    . LYS B 1 4   ? -5.688  27.471  29.618  1.00 114.74 ? 4   LYS B C    1 
ATOM   4245  O O    . LYS B 1 4   ? -5.506  28.483  28.930  1.00 114.08 ? 4   LYS B O    1 
ATOM   4246  C CB   . LYS B 1 4   ? -7.739  26.098  29.241  1.00 117.03 ? 4   LYS B CB   1 
ATOM   4247  C CG   . LYS B 1 4   ? -8.898  25.318  29.869  1.00 119.49 ? 4   LYS B CG   1 
ATOM   4248  C CD   . LYS B 1 4   ? -8.611  24.836  31.293  1.00 120.37 ? 4   LYS B CD   1 
ATOM   4249  C CE   . LYS B 1 4   ? -7.310  24.049  31.389  1.00 119.46 ? 4   LYS B CE   1 
ATOM   4250  N NZ   . LYS B 1 4   ? -7.109  23.469  32.749  1.00 115.13 ? 4   LYS B NZ   1 
ATOM   4251  H H    . LYS B 1 4   ? -8.288  28.552  29.576  1.00 142.51 ? 4   LYS B H    1 
ATOM   4252  H HA   . LYS B 1 4   ? -6.964  26.709  31.034  1.00 139.99 ? 4   LYS B HA   1 
ATOM   4253  H HB2  . LYS B 1 4   ? -8.090  26.567  28.467  1.00 140.43 ? 4   LYS B HB2  1 
ATOM   4254  H HB3  . LYS B 1 4   ? -7.071  25.452  28.963  1.00 140.43 ? 4   LYS B HB3  1 
ATOM   4255  H HG2  . LYS B 1 4   ? -9.680  25.891  29.903  1.00 143.39 ? 4   LYS B HG2  1 
ATOM   4256  H HG3  . LYS B 1 4   ? -9.083  24.537  29.324  1.00 143.39 ? 4   LYS B HG3  1 
ATOM   4257  H HD2  . LYS B 1 4   ? -8.542  25.604  31.881  1.00 144.45 ? 4   LYS B HD2  1 
ATOM   4258  H HD3  . LYS B 1 4   ? -9.334  24.258  31.585  1.00 144.45 ? 4   LYS B HD3  1 
ATOM   4259  H HE2  . LYS B 1 4   ? -7.329  23.321  30.749  1.00 143.36 ? 4   LYS B HE2  1 
ATOM   4260  H HE3  . LYS B 1 4   ? -6.565  24.640  31.199  1.00 143.36 ? 4   LYS B HE3  1 
ATOM   4261  H HZ1  . LYS B 1 4   ? -6.254  23.252  32.864  1.00 138.16 ? 4   LYS B HZ1  1 
ATOM   4262  H HZ2  . LYS B 1 4   ? -7.343  24.061  33.371  1.00 138.16 ? 4   LYS B HZ2  1 
ATOM   4263  H HZ3  . LYS B 1 4   ? -7.608  22.738  32.845  1.00 138.16 ? 4   LYS B HZ3  1 
ATOM   4264  N N    . VAL B 1 5   ? -4.719  26.617  29.930  1.00 111.85 ? 5   VAL B N    1 
ATOM   4265  C CA   . VAL B 1 5   ? -3.323  26.823  29.567  1.00 105.90 ? 5   VAL B CA   1 
ATOM   4266  C C    . VAL B 1 5   ? -2.958  25.797  28.506  1.00 102.63 ? 5   VAL B C    1 
ATOM   4267  O O    . VAL B 1 5   ? -3.008  24.586  28.759  1.00 101.88 ? 5   VAL B O    1 
ATOM   4268  C CB   . VAL B 1 5   ? -2.399  26.700  30.789  1.00 102.61 ? 5   VAL B CB   1 
ATOM   4269  C CG1  . VAL B 1 5   ? -1.080  27.415  30.533  1.00 95.68  ? 5   VAL B CG1  1 
ATOM   4270  C CG2  . VAL B 1 5   ? -3.091  27.245  32.035  1.00 99.63  ? 5   VAL B CG2  1 
ATOM   4271  H H    . VAL B 1 5   ? -4.851  25.888  30.366  1.00 134.22 ? 5   VAL B H    1 
ATOM   4272  H HA   . VAL B 1 5   ? -3.218  27.709  29.187  1.00 127.08 ? 5   VAL B HA   1 
ATOM   4273  H HB   . VAL B 1 5   ? -2.201  25.764  30.946  1.00 123.13 ? 5   VAL B HB   1 
ATOM   4274  H HG11 . VAL B 1 5   ? -0.527  27.351  31.327  1.00 114.82 ? 5   VAL B HG11 1 
ATOM   4275  H HG12 . VAL B 1 5   ? -0.633  26.993  29.783  1.00 114.82 ? 5   VAL B HG12 1 
ATOM   4276  H HG13 . VAL B 1 5   ? -1.260  28.346  30.329  1.00 114.82 ? 5   VAL B HG13 1 
ATOM   4277  H HG21 . VAL B 1 5   ? -2.432  27.357  32.739  1.00 119.56 ? 5   VAL B HG21 1 
ATOM   4278  H HG22 . VAL B 1 5   ? -3.497  28.100  31.823  1.00 119.56 ? 5   VAL B HG22 1 
ATOM   4279  H HG23 . VAL B 1 5   ? -3.773  26.616  32.318  1.00 119.56 ? 5   VAL B HG23 1 
ATOM   4280  N N    . GLN B 1 6   ? -2.591  26.275  27.322  1.00 102.09 ? 6   GLN B N    1 
ATOM   4281  C CA   . GLN B 1 6   ? -2.125  25.389  26.265  1.00 97.81  ? 6   GLN B CA   1 
ATOM   4282  C C    . GLN B 1 6   ? -0.638  25.115  26.450  1.00 92.51  ? 6   GLN B C    1 
ATOM   4283  O O    . GLN B 1 6   ? 0.166   26.046  26.565  1.00 90.11  ? 6   GLN B O    1 
ATOM   4284  C CB   . GLN B 1 6   ? -2.394  25.998  24.892  1.00 100.24 ? 6   GLN B CB   1 
ATOM   4285  C CG   . GLN B 1 6   ? -2.388  24.962  23.779  1.00 98.98  ? 6   GLN B CG   1 
ATOM   4286  C CD   . GLN B 1 6   ? -2.987  25.474  22.488  1.00 99.64  ? 6   GLN B CD   1 
ATOM   4287  O OE1  . GLN B 1 6   ? -2.894  26.660  22.170  1.00 99.95  ? 6   GLN B OE1  1 
ATOM   4288  N NE2  . GLN B 1 6   ? -3.605  24.576  21.730  1.00 103.13 ? 6   GLN B NE2  1 
ATOM   4289  H H    . GLN B 1 6   ? -2.602  27.108  27.107  1.00 122.50 ? 6   GLN B H    1 
ATOM   4290  H HA   . GLN B 1 6   ? -2.605  24.547  26.311  1.00 117.37 ? 6   GLN B HA   1 
ATOM   4291  H HB2  . GLN B 1 6   ? -3.264  26.425  24.900  1.00 120.28 ? 6   GLN B HB2  1 
ATOM   4292  H HB3  . GLN B 1 6   ? -1.705  26.652  24.696  1.00 120.28 ? 6   GLN B HB3  1 
ATOM   4293  H HG2  . GLN B 1 6   ? -1.472  24.699  23.599  1.00 118.78 ? 6   GLN B HG2  1 
ATOM   4294  H HG3  . GLN B 1 6   ? -2.905  24.192  24.063  1.00 118.78 ? 6   GLN B HG3  1 
ATOM   4295  H HE21 . GLN B 1 6   ? -3.647  23.755  21.983  1.00 123.76 ? 6   GLN B HE21 1 
ATOM   4296  H HE22 . GLN B 1 6   ? -3.963  24.815  20.985  1.00 123.76 ? 6   GLN B HE22 1 
ATOM   4297  N N    . VAL B 1 7   ? -0.279  23.835  26.479  1.00 90.27  ? 7   VAL B N    1 
ATOM   4298  C CA   . VAL B 1 7   ? 1.079   23.389  26.767  1.00 86.88  ? 7   VAL B CA   1 
ATOM   4299  C C    . VAL B 1 7   ? 1.709   22.937  25.456  1.00 85.86  ? 7   VAL B C    1 
ATOM   4300  O O    . VAL B 1 7   ? 1.373   21.868  24.930  1.00 85.30  ? 7   VAL B O    1 
ATOM   4301  C CB   . VAL B 1 7   ? 1.093   22.261  27.806  1.00 86.61  ? 7   VAL B CB   1 
ATOM   4302  C CG1  . VAL B 1 7   ? 2.454   22.177  28.477  1.00 85.96  ? 7   VAL B CG1  1 
ATOM   4303  C CG2  . VAL B 1 7   ? -0.014  22.470  28.839  1.00 89.51  ? 7   VAL B CG2  1 
ATOM   4304  H H    . VAL B 1 7   ? -0.823  23.186  26.330  1.00 108.32 ? 7   VAL B H    1 
ATOM   4305  H HA   . VAL B 1 7   ? 1.595   24.136  27.109  1.00 104.26 ? 7   VAL B HA   1 
ATOM   4306  H HB   . VAL B 1 7   ? 0.926   21.416  27.360  1.00 103.93 ? 7   VAL B HB   1 
ATOM   4307  H HG11 . VAL B 1 7   ? 2.440   21.460  29.131  1.00 103.16 ? 7   VAL B HG11 1 
ATOM   4308  H HG12 . VAL B 1 7   ? 3.127   21.996  27.803  1.00 103.16 ? 7   VAL B HG12 1 
ATOM   4309  H HG13 . VAL B 1 7   ? 2.642   23.021  28.915  1.00 103.16 ? 7   VAL B HG13 1 
ATOM   4310  H HG21 . VAL B 1 7   ? 0.025   21.755  29.493  1.00 107.41 ? 7   VAL B HG21 1 
ATOM   4311  H HG22 . VAL B 1 7   ? 0.120   23.326  29.276  1.00 107.41 ? 7   VAL B HG22 1 
ATOM   4312  H HG23 . VAL B 1 7   ? -0.872  22.460  28.388  1.00 107.41 ? 7   VAL B HG23 1 
ATOM   4313  N N    . LEU B 1 8   ? 2.630   23.741  24.933  1.00 81.27  ? 8   LEU B N    1 
ATOM   4314  C CA   . LEU B 1 8   ? 3.287   23.459  23.669  1.00 79.32  ? 8   LEU B CA   1 
ATOM   4315  C C    . LEU B 1 8   ? 4.711   22.968  23.889  1.00 77.85  ? 8   LEU B C    1 
ATOM   4316  O O    . LEU B 1 8   ? 5.377   23.349  24.856  1.00 77.16  ? 8   LEU B O    1 
ATOM   4317  C CB   . LEU B 1 8   ? 3.327   24.703  22.781  1.00 83.24  ? 8   LEU B CB   1 
ATOM   4318  C CG   . LEU B 1 8   ? 2.127   25.641  22.754  1.00 83.94  ? 8   LEU B CG   1 
ATOM   4319  C CD1  . LEU B 1 8   ? 2.245   26.588  21.566  1.00 88.48  ? 8   LEU B CD1  1 
ATOM   4320  C CD2  . LEU B 1 8   ? 0.839   24.866  22.681  1.00 88.75  ? 8   LEU B CD2  1 
ATOM   4321  H H    . LEU B 1 8   ? 2.895   24.472  25.303  1.00 97.52  ? 8   LEU B H    1 
ATOM   4322  H HA   . LEU B 1 8   ? 2.787   22.762  23.214  1.00 95.19  ? 8   LEU B HA   1 
ATOM   4323  H HB2  . LEU B 1 8   ? 4.085   25.238  23.066  1.00 99.88  ? 8   LEU B HB2  1 
ATOM   4324  H HB3  . LEU B 1 8   ? 3.459   24.403  21.868  1.00 99.88  ? 8   LEU B HB3  1 
ATOM   4325  H HG   . LEU B 1 8   ? 2.110   26.160  23.573  1.00 100.72 ? 8   LEU B HG   1 
ATOM   4326  H HD11 . LEU B 1 8   ? 1.477   27.181  21.557  1.00 106.17 ? 8   LEU B HD11 1 
ATOM   4327  H HD12 . LEU B 1 8   ? 3.061   27.105  21.653  1.00 106.17 ? 8   LEU B HD12 1 
ATOM   4328  H HD13 . LEU B 1 8   ? 2.269   26.067  20.748  1.00 106.17 ? 8   LEU B HD13 1 
ATOM   4329  H HD21 . LEU B 1 8   ? 0.099   25.490  22.606  1.00 106.50 ? 8   LEU B HD21 1 
ATOM   4330  H HD22 . LEU B 1 8   ? 0.862   24.286  21.904  1.00 106.50 ? 8   LEU B HD22 1 
ATOM   4331  H HD23 . LEU B 1 8   ? 0.743   24.336  23.487  1.00 106.50 ? 8   LEU B HD23 1 
ATOM   4332  N N    . ASP B 1 9   ? 5.179   22.130  22.967  1.00 76.41  ? 9   ASP B N    1 
ATOM   4333  C CA   . ASP B 1 9   ? 6.559   21.665  22.966  1.00 74.95  ? 9   ASP B CA   1 
ATOM   4334  C C    . ASP B 1 9   ? 7.407   22.641  22.163  1.00 73.57  ? 9   ASP B C    1 
ATOM   4335  O O    . ASP B 1 9   ? 7.093   22.934  21.005  1.00 75.79  ? 9   ASP B O    1 
ATOM   4336  C CB   . ASP B 1 9   ? 6.657   20.261  22.375  1.00 77.53  ? 9   ASP B CB   1 
ATOM   4337  C CG   . ASP B 1 9   ? 5.671   19.288  23.006  1.00 81.57  ? 9   ASP B CG   1 
ATOM   4338  O OD1  . ASP B 1 9   ? 4.577   19.724  23.429  1.00 82.73  ? 9   ASP B OD1  1 
ATOM   4339  O OD2  . ASP B 1 9   ? 5.988   18.082  23.077  1.00 83.22  ? 9   ASP B OD2  1 
ATOM   4340  H H    . ASP B 1 9   ? 4.706   21.812  22.322  1.00 91.69  ? 9   ASP B H    1 
ATOM   4341  H HA   . ASP B 1 9   ? 6.896   21.627  23.875  1.00 89.94  ? 9   ASP B HA   1 
ATOM   4342  H HB2  . ASP B 1 9   ? 6.470   20.304  21.424  1.00 93.04  ? 9   ASP B HB2  1 
ATOM   4343  H HB3  . ASP B 1 9   ? 7.553   19.918  22.521  1.00 93.04  ? 9   ASP B HB3  1 
ATOM   4344  N N    . PHE B 1 10  ? 8.474   23.146  22.779  1.00 72.18  ? 10  PHE B N    1 
ATOM   4345  C CA   . PHE B 1 10  ? 9.315   24.158  22.165  1.00 71.09  ? 10  PHE B CA   1 
ATOM   4346  C C    . PHE B 1 10  ? 10.765  23.701  22.104  1.00 69.56  ? 10  PHE B C    1 
ATOM   4347  O O    . PHE B 1 10  ? 11.215  22.880  22.905  1.00 68.31  ? 10  PHE B O    1 
ATOM   4348  C CB   . PHE B 1 10  ? 9.246   25.497  22.931  1.00 72.08  ? 10  PHE B CB   1 
ATOM   4349  C CG   . PHE B 1 10  ? 10.233  25.599  24.072  1.00 73.57  ? 10  PHE B CG   1 
ATOM   4350  C CD1  . PHE B 1 10  ? 11.521  26.078  23.859  1.00 72.42  ? 10  PHE B CD1  1 
ATOM   4351  C CD2  . PHE B 1 10  ? 9.873   25.214  25.355  1.00 73.16  ? 10  PHE B CD2  1 
ATOM   4352  C CE1  . PHE B 1 10  ? 12.427  26.165  24.900  1.00 72.09  ? 10  PHE B CE1  1 
ATOM   4353  C CE2  . PHE B 1 10  ? 10.777  25.300  26.403  1.00 72.17  ? 10  PHE B CE2  1 
ATOM   4354  C CZ   . PHE B 1 10  ? 12.055  25.777  26.174  1.00 73.23  ? 10  PHE B CZ   1 
ATOM   4355  H H    . PHE B 1 10  ? 8.730   22.912  23.565  1.00 86.62  ? 10  PHE B H    1 
ATOM   4356  H HA   . PHE B 1 10  ? 9.005   24.298  21.256  1.00 85.31  ? 10  PHE B HA   1 
ATOM   4357  H HB2  . PHE B 1 10  ? 9.433   26.220  22.313  1.00 86.49  ? 10  PHE B HB2  1 
ATOM   4358  H HB3  . PHE B 1 10  ? 8.355   25.599  23.301  1.00 86.49  ? 10  PHE B HB3  1 
ATOM   4359  H HD1  . PHE B 1 10  ? 11.776  26.343  23.005  1.00 86.90  ? 10  PHE B HD1  1 
ATOM   4360  H HD2  . PHE B 1 10  ? 9.015   24.895  25.514  1.00 87.79  ? 10  PHE B HD2  1 
ATOM   4361  H HE1  . PHE B 1 10  ? 13.286  26.484  24.744  1.00 86.51  ? 10  PHE B HE1  1 
ATOM   4362  H HE2  . PHE B 1 10  ? 10.524  25.037  27.259  1.00 86.61  ? 10  PHE B HE2  1 
ATOM   4363  H HZ   . PHE B 1 10  ? 12.663  25.837  26.875  1.00 87.88  ? 10  PHE B HZ   1 
ATOM   4364  N N    . ILE B 1 11  ? 11.485  24.248  21.124  1.00 73.26  ? 11  ILE B N    1 
ATOM   4365  C CA   . ILE B 1 11  ? 12.935  24.146  21.034  1.00 70.39  ? 11  ILE B CA   1 
ATOM   4366  C C    . ILE B 1 11  ? 13.448  25.539  20.699  1.00 70.09  ? 11  ILE B C    1 
ATOM   4367  O O    . ILE B 1 11  ? 13.085  26.098  19.660  1.00 69.83  ? 11  ILE B O    1 
ATOM   4368  C CB   . ILE B 1 11  ? 13.397  23.138  19.968  1.00 71.34  ? 11  ILE B CB   1 
ATOM   4369  C CG1  . ILE B 1 11  ? 12.628  21.821  20.090  1.00 70.90  ? 11  ILE B CG1  1 
ATOM   4370  C CG2  . ILE B 1 11  ? 14.901  22.905  20.100  1.00 70.93  ? 11  ILE B CG2  1 
ATOM   4371  C CD1  . ILE B 1 11  ? 11.426  21.715  19.170  1.00 68.89  ? 11  ILE B CD1  1 
ATOM   4372  H H    . ILE B 1 11  ? 11.140  24.699  20.478  1.00 87.92  ? 11  ILE B H    1 
ATOM   4373  H HA   . ILE B 1 11  ? 13.300  23.859  21.886  1.00 84.47  ? 11  ILE B HA   1 
ATOM   4374  H HB   . ILE B 1 11  ? 13.208  23.506  19.091  1.00 85.61  ? 11  ILE B HB   1 
ATOM   4375  H HG12 . ILE B 1 11  ? 13.228  21.091  19.874  1.00 85.08  ? 11  ILE B HG12 1 
ATOM   4376  H HG13 . ILE B 1 11  ? 12.309  21.731  21.001  1.00 85.08  ? 11  ILE B HG13 1 
ATOM   4377  H HG21 . ILE B 1 11  ? 15.176  22.242  19.449  1.00 85.12  ? 11  ILE B HG21 1 
ATOM   4378  H HG22 . ILE B 1 11  ? 15.365  23.741  19.938  1.00 85.12  ? 11  ILE B HG22 1 
ATOM   4379  H HG23 . ILE B 1 11  ? 15.094  22.588  20.997  1.00 85.12  ? 11  ILE B HG23 1 
ATOM   4380  H HD11 . ILE B 1 11  ? 11.010  20.847  19.294  1.00 82.67  ? 11  ILE B HD11 1 
ATOM   4381  H HD12 . ILE B 1 11  ? 10.797  22.419  19.391  1.00 82.67  ? 11  ILE B HD12 1 
ATOM   4382  H HD13 . ILE B 1 11  ? 11.722  21.811  18.251  1.00 82.67  ? 11  ILE B HD13 1 
ATOM   4383  N N    . LYS B 1 12  ? 14.260  26.112  21.580  1.00 69.68  ? 12  LYS B N    1 
ATOM   4384  C CA   . LYS B 1 12  ? 14.845  27.427  21.357  1.00 70.32  ? 12  LYS B CA   1 
ATOM   4385  C C    . LYS B 1 12  ? 16.235  27.250  20.766  1.00 72.06  ? 12  LYS B C    1 
ATOM   4386  O O    . LYS B 1 12  ? 17.041  26.470  21.287  1.00 73.51  ? 12  LYS B O    1 
ATOM   4387  C CB   . LYS B 1 12  ? 14.919  28.238  22.649  1.00 70.68  ? 12  LYS B CB   1 
ATOM   4388  C CG   . LYS B 1 12  ? 15.453  29.644  22.439  1.00 72.39  ? 12  LYS B CG   1 
ATOM   4389  C CD   . LYS B 1 12  ? 15.130  30.552  23.613  1.00 77.36  ? 12  LYS B CD   1 
ATOM   4390  C CE   . LYS B 1 12  ? 15.285  32.014  23.221  1.00 79.01  ? 12  LYS B CE   1 
ATOM   4391  N NZ   . LYS B 1 12  ? 14.798  32.937  24.272  1.00 78.85  ? 12  LYS B NZ   1 
ATOM   4392  H H    . LYS B 1 12  ? 14.491  25.752  22.326  1.00 83.61  ? 12  LYS B H    1 
ATOM   4393  H HA   . LYS B 1 12  ? 14.294  27.924  20.733  1.00 84.38  ? 12  LYS B HA   1 
ATOM   4394  H HB2  . LYS B 1 12  ? 14.028  28.310  23.027  1.00 84.82  ? 12  LYS B HB2  1 
ATOM   4395  H HB3  . LYS B 1 12  ? 15.508  27.785  23.272  1.00 84.82  ? 12  LYS B HB3  1 
ATOM   4396  H HG2  . LYS B 1 12  ? 16.417  29.608  22.339  1.00 86.86  ? 12  LYS B HG2  1 
ATOM   4397  H HG3  . LYS B 1 12  ? 15.050  30.023  21.642  1.00 86.86  ? 12  LYS B HG3  1 
ATOM   4398  H HD2  . LYS B 1 12  ? 14.214  30.404  23.895  1.00 92.84  ? 12  LYS B HD2  1 
ATOM   4399  H HD3  . LYS B 1 12  ? 15.737  30.364  24.346  1.00 92.84  ? 12  LYS B HD3  1 
ATOM   4400  H HE2  . LYS B 1 12  ? 16.223  32.203  23.065  1.00 94.81  ? 12  LYS B HE2  1 
ATOM   4401  H HE3  . LYS B 1 12  ? 14.775  32.182  22.413  1.00 94.81  ? 12  LYS B HE3  1 
ATOM   4402  H HZ1  . LYS B 1 12  ? 14.886  33.780  24.001  1.00 94.62  ? 12  LYS B HZ1  1 
ATOM   4403  H HZ2  . LYS B 1 12  ? 15.268  32.822  25.019  1.00 94.62  ? 12  LYS B HZ2  1 
ATOM   4404  H HZ3  . LYS B 1 12  ? 13.939  32.777  24.443  1.00 94.62  ? 12  LYS B HZ3  1 
ATOM   4405  N N    . ILE B 1 13  ? 16.508  27.975  19.685  1.00 71.35  ? 13  ILE B N    1 
ATOM   4406  C CA   . ILE B 1 13  ? 17.717  27.797  18.889  1.00 69.57  ? 13  ILE B CA   1 
ATOM   4407  C C    . ILE B 1 13  ? 18.241  29.170  18.495  1.00 70.41  ? 13  ILE B C    1 
ATOM   4408  O O    . ILE B 1 13  ? 17.460  30.076  18.183  1.00 71.53  ? 13  ILE B O    1 
ATOM   4409  C CB   . ILE B 1 13  ? 17.443  26.941  17.634  1.00 70.85  ? 13  ILE B CB   1 
ATOM   4410  C CG1  . ILE B 1 13  ? 16.664  25.678  18.007  1.00 69.89  ? 13  ILE B CG1  1 
ATOM   4411  C CG2  . ILE B 1 13  ? 18.746  26.587  16.934  1.00 71.02  ? 13  ILE B CG2  1 
ATOM   4412  C CD1  . ILE B 1 13  ? 16.098  24.939  16.811  1.00 69.53  ? 13  ILE B CD1  1 
ATOM   4413  H H    . ILE B 1 13  ? 15.993  28.594  19.384  1.00 85.62  ? 13  ILE B H    1 
ATOM   4414  H HA   . ILE B 1 13  ? 18.393  27.352  19.424  1.00 83.48  ? 13  ILE B HA   1 
ATOM   4415  H HB   . ILE B 1 13  ? 16.901  27.463  17.022  1.00 85.01  ? 13  ILE B HB   1 
ATOM   4416  H HG12 . ILE B 1 13  ? 17.258  25.071  18.476  1.00 83.87  ? 13  ILE B HG12 1 
ATOM   4417  H HG13 . ILE B 1 13  ? 15.922  25.926  18.581  1.00 83.87  ? 13  ILE B HG13 1 
ATOM   4418  H HG21 . ILE B 1 13  ? 18.564  25.937  16.237  1.00 85.22  ? 13  ILE B HG21 1 
ATOM   4419  H HG22 . ILE B 1 13  ? 19.125  27.391  16.545  1.00 85.22  ? 13  ILE B HG22 1 
ATOM   4420  H HG23 . ILE B 1 13  ? 19.362  26.212  17.583  1.00 85.22  ? 13  ILE B HG23 1 
ATOM   4421  H HD11 . ILE B 1 13  ? 15.492  24.249  17.124  1.00 83.43  ? 13  ILE B HD11 1 
ATOM   4422  H HD12 . ILE B 1 13  ? 15.620  25.568  16.248  1.00 83.43  ? 13  ILE B HD12 1 
ATOM   4423  H HD13 . ILE B 1 13  ? 16.827  24.537  16.313  1.00 83.43  ? 13  ILE B HD13 1 
ATOM   4424  N N    . ASN B 1 14  ? 19.568  29.319  18.496  1.00 71.03  ? 14  ASN B N    1 
ATOM   4425  C CA   . ASN B 1 14  ? 20.227  30.558  18.091  1.00 73.05  ? 14  ASN B CA   1 
ATOM   4426  C C    . ASN B 1 14  ? 20.928  30.381  16.748  1.00 70.95  ? 14  ASN B C    1 
ATOM   4427  O O    . ASN B 1 14  ? 22.124  30.053  16.702  1.00 69.92  ? 14  ASN B O    1 
ATOM   4428  C CB   . ASN B 1 14  ? 21.226  31.005  19.162  1.00 70.57  ? 14  ASN B CB   1 
ATOM   4429  C CG   . ASN B 1 14  ? 22.015  32.231  18.744  1.00 72.43  ? 14  ASN B CG   1 
ATOM   4430  O OD1  . ASN B 1 14  ? 21.493  33.111  18.065  1.00 73.84  ? 14  ASN B OD1  1 
ATOM   4431  N ND2  . ASN B 1 14  ? 23.277  32.295  19.151  1.00 72.32  ? 14  ASN B ND2  1 
ATOM   4432  H H    . ASN B 1 14  ? 20.117  28.701  18.734  1.00 85.24  ? 14  ASN B H    1 
ATOM   4433  H HA   . ASN B 1 14  ? 19.547  31.240  17.975  1.00 87.67  ? 14  ASN B HA   1 
ATOM   4434  H HB2  . ASN B 1 14  ? 20.744  31.220  19.975  1.00 84.68  ? 14  ASN B HB2  1 
ATOM   4435  H HB3  . ASN B 1 14  ? 21.855  30.285  19.329  1.00 84.68  ? 14  ASN B HB3  1 
ATOM   4436  H HD21 . ASN B 1 14  ? 23.764  32.972  18.938  1.00 86.79  ? 14  ASN B HD21 1 
ATOM   4437  H HD22 . ASN B 1 14  ? 23.608  31.660  19.627  1.00 86.79  ? 14  ASN B HD22 1 
ATOM   4438  N N    . PRO B 1 15  ? 20.234  30.592  15.623  1.00 74.54  ? 15  PRO B N    1 
ATOM   4439  C CA   . PRO B 1 15  ? 20.919  30.575  14.320  1.00 70.83  ? 15  PRO B CA   1 
ATOM   4440  C C    . PRO B 1 15  ? 21.561  31.912  13.987  1.00 71.79  ? 15  PRO B C    1 
ATOM   4441  O O    . PRO B 1 15  ? 20.910  32.808  13.439  1.00 73.03  ? 15  PRO B O    1 
ATOM   4442  C CB   . PRO B 1 15  ? 19.792  30.232  13.339  1.00 72.25  ? 15  PRO B CB   1 
ATOM   4443  C CG   . PRO B 1 15  ? 18.564  30.817  13.982  1.00 71.93  ? 15  PRO B CG   1 
ATOM   4444  C CD   . PRO B 1 15  ? 18.769  30.718  15.483  1.00 74.24  ? 15  PRO B CD   1 
ATOM   4445  H HA   . PRO B 1 15  ? 21.592  29.877  14.297  1.00 85.00  ? 15  PRO B HA   1 
ATOM   4446  H HB2  . PRO B 1 15  ? 19.964  30.639  12.476  1.00 86.70  ? 15  PRO B HB2  1 
ATOM   4447  H HB3  . PRO B 1 15  ? 19.713  29.270  13.242  1.00 86.70  ? 15  PRO B HB3  1 
ATOM   4448  H HG2  . PRO B 1 15  ? 18.467  31.743  13.712  1.00 86.31  ? 15  PRO B HG2  1 
ATOM   4449  H HG3  . PRO B 1 15  ? 17.783  30.309  13.711  1.00 86.31  ? 15  PRO B HG3  1 
ATOM   4450  H HD2  . PRO B 1 15  ? 18.448  31.519  15.928  1.00 89.08  ? 15  PRO B HD2  1 
ATOM   4451  H HD3  . PRO B 1 15  ? 18.320  29.937  15.842  1.00 89.08  ? 15  PRO B HD3  1 
ATOM   4452  N N    . ALA B 1 16  ? 22.842  32.056  14.328  1.00 73.14  ? 16  ALA B N    1 
ATOM   4453  C CA   . ALA B 1 16  ? 23.610  33.266  14.039  1.00 72.51  ? 16  ALA B CA   1 
ATOM   4454  C C    . ALA B 1 16  ? 22.947  34.515  14.619  1.00 73.62  ? 16  ALA B C    1 
ATOM   4455  O O    . ALA B 1 16  ? 22.985  35.595  14.027  1.00 75.20  ? 16  ALA B O    1 
ATOM   4456  C CB   . ALA B 1 16  ? 23.828  33.419  12.532  1.00 74.08  ? 16  ALA B CB   1 
ATOM   4457  H H    . ALA B 1 16  ? 23.298  31.452  14.737  1.00 87.77  ? 16  ALA B H    1 
ATOM   4458  H HA   . ALA B 1 16  ? 24.476  33.183  14.469  1.00 87.01  ? 16  ALA B HA   1 
ATOM   4459  H HB1  . ALA B 1 16  ? 24.342  34.225  12.368  1.00 88.90  ? 16  ALA B HB1  1 
ATOM   4460  H HB2  . ALA B 1 16  ? 24.312  32.646  12.203  1.00 88.90  ? 16  ALA B HB2  1 
ATOM   4461  H HB3  . ALA B 1 16  ? 22.965  33.482  12.093  1.00 88.90  ? 16  ALA B HB3  1 
ATOM   4462  N N    . GLY B 1 17  ? 22.345  34.374  15.795  1.00 74.78  ? 17  GLY B N    1 
ATOM   4463  C CA   . GLY B 1 17  ? 21.725  35.484  16.482  1.00 76.95  ? 17  GLY B CA   1 
ATOM   4464  C C    . GLY B 1 17  ? 20.260  35.702  16.165  1.00 78.50  ? 17  GLY B C    1 
ATOM   4465  O O    . GLY B 1 17  ? 19.564  36.356  16.950  1.00 80.29  ? 17  GLY B O    1 
ATOM   4466  H H    . GLY B 1 17  ? 22.284  33.628  16.219  1.00 89.73  ? 17  GLY B H    1 
ATOM   4467  H HA2  . GLY B 1 17  ? 21.802  35.338  17.437  1.00 92.34  ? 17  GLY B HA2  1 
ATOM   4468  H HA3  . GLY B 1 17  ? 22.201  36.297  16.247  1.00 92.34  ? 17  GLY B HA3  1 
ATOM   4469  N N    . ASN B 1 18  ? 19.771  35.177  15.043  1.00 74.53  ? 18  ASN B N    1 
ATOM   4470  C CA   . ASN B 1 18  ? 18.363  35.300  14.652  1.00 77.90  ? 18  ASN B CA   1 
ATOM   4471  C C    . ASN B 1 18  ? 17.554  34.307  15.487  1.00 76.35  ? 18  ASN B C    1 
ATOM   4472  O O    . ASN B 1 18  ? 17.178  33.219  15.045  1.00 77.41  ? 18  ASN B O    1 
ATOM   4473  C CB   . ASN B 1 18  ? 18.217  35.059  13.153  1.00 79.63  ? 18  ASN B CB   1 
ATOM   4474  C CG   . ASN B 1 18  ? 16.811  35.339  12.634  1.00 79.00  ? 18  ASN B CG   1 
ATOM   4475  O OD1  . ASN B 1 18  ? 16.415  34.808  11.602  1.00 81.59  ? 18  ASN B OD1  1 
ATOM   4476  N ND2  . ASN B 1 18  ? 16.064  36.178  13.340  1.00 81.87  ? 18  ASN B ND2  1 
ATOM   4477  H H    . ASN B 1 18  ? 20.244  34.735  14.476  1.00 89.44  ? 18  ASN B H    1 
ATOM   4478  H HA   . ASN B 1 18  ? 18.035  36.192  14.847  1.00 93.48  ? 18  ASN B HA   1 
ATOM   4479  H HB2  . ASN B 1 18  ? 18.831  35.641  12.680  1.00 95.55  ? 18  ASN B HB2  1 
ATOM   4480  H HB3  . ASN B 1 18  ? 18.426  34.131  12.962  1.00 95.55  ? 18  ASN B HB3  1 
ATOM   4481  H HD21 . ASN B 1 18  ? 16.378  36.536  14.056  1.00 98.24  ? 18  ASN B HD21 1 
ATOM   4482  H HD22 . ASN B 1 18  ? 15.264  36.363  13.082  1.00 98.24  ? 18  ASN B HD22 1 
ATOM   4483  N N    . ILE B 1 19  ? 17.275  34.707  16.731  1.00 79.77  ? 19  ILE B N    1 
ATOM   4484  C CA   . ILE B 1 19  ? 16.670  33.792  17.692  1.00 77.50  ? 19  ILE B CA   1 
ATOM   4485  C C    . ILE B 1 19  ? 15.340  33.284  17.154  1.00 76.91  ? 19  ILE B C    1 
ATOM   4486  O O    . ILE B 1 19  ? 14.452  34.068  16.793  1.00 75.29  ? 19  ILE B O    1 
ATOM   4487  C CB   . ILE B 1 19  ? 16.477  34.481  19.051  1.00 80.19  ? 19  ILE B CB   1 
ATOM   4488  C CG1  . ILE B 1 19  ? 17.768  35.146  19.525  1.00 82.19  ? 19  ILE B CG1  1 
ATOM   4489  C CG2  . ILE B 1 19  ? 15.992  33.470  20.088  1.00 78.38  ? 19  ILE B CG2  1 
ATOM   4490  C CD1  . ILE B 1 19  ? 18.793  34.180  20.067  1.00 80.40  ? 19  ILE B CD1  1 
ATOM   4491  H H    . ILE B 1 19  ? 17.426  35.496  17.037  1.00 95.73  ? 19  ILE B H    1 
ATOM   4492  H HA   . ILE B 1 19  ? 17.269  33.038  17.810  1.00 93.00  ? 19  ILE B HA   1 
ATOM   4493  H HB   . ILE B 1 19  ? 15.807  35.174  18.941  1.00 96.22  ? 19  ILE B HB   1 
ATOM   4494  H HG12 . ILE B 1 19  ? 18.171  35.613  18.776  1.00 98.62  ? 19  ILE B HG12 1 
ATOM   4495  H HG13 . ILE B 1 19  ? 17.553  35.775  20.231  1.00 98.62  ? 19  ILE B HG13 1 
ATOM   4496  H HG21 . ILE B 1 19  ? 16.099  33.850  20.974  1.00 94.05  ? 19  ILE B HG21 1 
ATOM   4497  H HG22 . ILE B 1 19  ? 15.057  33.272  19.924  1.00 94.05  ? 19  ILE B HG22 1 
ATOM   4498  H HG23 . ILE B 1 19  ? 16.521  32.660  20.011  1.00 94.05  ? 19  ILE B HG23 1 
ATOM   4499  H HD11 . ILE B 1 19  ? 19.680  34.535  19.901  1.00 96.48  ? 19  ILE B HD11 1 
ATOM   4500  H HD12 . ILE B 1 19  ? 18.652  34.073  21.021  1.00 96.48  ? 19  ILE B HD12 1 
ATOM   4501  H HD13 . ILE B 1 19  ? 18.689  33.326  19.619  1.00 96.48  ? 19  ILE B HD13 1 
ATOM   4502  N N    . THR B 1 20  ? 15.192  31.965  17.105  1.00 74.40  ? 20  THR B N    1 
ATOM   4503  C CA   . THR B 1 20  ? 13.994  31.327  16.579  1.00 75.94  ? 20  THR B CA   1 
ATOM   4504  C C    . THR B 1 20  ? 13.562  30.224  17.532  1.00 74.66  ? 20  THR B C    1 
ATOM   4505  O O    . THR B 1 20  ? 14.398  29.496  18.079  1.00 74.63  ? 20  THR B O    1 
ATOM   4506  C CB   . THR B 1 20  ? 14.233  30.760  15.162  1.00 78.00  ? 20  THR B CB   1 
ATOM   4507  O OG1  . THR B 1 20  ? 13.092  29.998  14.741  1.00 77.83  ? 20  THR B OG1  1 
ATOM   4508  C CG2  . THR B 1 20  ? 15.466  29.872  15.126  1.00 74.76  ? 20  THR B CG2  1 
ATOM   4509  H H    . THR B 1 20  ? 15.787  31.407  17.378  1.00 89.27  ? 20  THR B H    1 
ATOM   4510  H HA   . THR B 1 20  ? 13.273  31.973  16.517  1.00 91.12  ? 20  THR B HA   1 
ATOM   4511  H HB   . THR B 1 20  ? 14.374  31.500  14.551  1.00 93.60  ? 20  THR B HB   1 
ATOM   4512  H HG1  . THR B 1 20  ? 13.219  29.693  13.969  1.00 93.39  ? 20  THR B HG1  1 
ATOM   4513  H HG21 . THR B 1 20  ? 15.643  29.588  14.215  1.00 89.71  ? 20  THR B HG21 1 
ATOM   4514  H HG22 . THR B 1 20  ? 16.235  30.359  15.459  1.00 89.71  ? 20  THR B HG22 1 
ATOM   4515  H HG23 . THR B 1 20  ? 15.326  29.088  15.679  1.00 89.71  ? 20  THR B HG23 1 
ATOM   4516  N N    . ILE B 1 21  ? 12.254  30.129  17.749  1.00 74.69  ? 21  ILE B N    1 
ATOM   4517  C CA   . ILE B 1 21  ? 11.648  29.065  18.537  1.00 74.08  ? 21  ILE B CA   1 
ATOM   4518  C C    . ILE B 1 21  ? 10.850  28.186  17.583  1.00 76.23  ? 21  ILE B C    1 
ATOM   4519  O O    . ILE B 1 21  ? 10.084  28.693  16.753  1.00 73.61  ? 21  ILE B O    1 
ATOM   4520  C CB   . ILE B 1 21  ? 10.757  29.628  19.655  1.00 74.64  ? 21  ILE B CB   1 
ATOM   4521  C CG1  . ILE B 1 21  ? 11.578  30.541  20.569  1.00 77.03  ? 21  ILE B CG1  1 
ATOM   4522  C CG2  . ILE B 1 21  ? 10.133  28.502  20.461  1.00 75.31  ? 21  ILE B CG2  1 
ATOM   4523  C CD1  . ILE B 1 21  ? 10.749  31.372  21.501  1.00 75.52  ? 21  ILE B CD1  1 
ATOM   4524  H H    . ILE B 1 21  ? 11.679  30.689  17.439  1.00 89.63  ? 21  ILE B H    1 
ATOM   4525  H HA   . ILE B 1 21  ? 12.340  28.527  18.953  1.00 88.89  ? 21  ILE B HA   1 
ATOM   4526  H HB   . ILE B 1 21  ? 10.044  30.146  19.248  1.00 89.57  ? 21  ILE B HB   1 
ATOM   4527  H HG12 . ILE B 1 21  ? 12.169  29.992  21.108  1.00 92.43  ? 21  ILE B HG12 1 
ATOM   4528  H HG13 . ILE B 1 21  ? 12.099  31.147  20.018  1.00 92.43  ? 21  ILE B HG13 1 
ATOM   4529  H HG21 . ILE B 1 21  ? 9.579   28.883  21.160  1.00 90.38  ? 21  ILE B HG21 1 
ATOM   4530  H HG22 . ILE B 1 21  ? 9.592   27.954  19.872  1.00 90.38  ? 21  ILE B HG22 1 
ATOM   4531  H HG23 . ILE B 1 21  ? 10.840  27.967  20.855  1.00 90.38  ? 21  ILE B HG23 1 
ATOM   4532  H HD11 . ILE B 1 21  ? 11.338  31.880  22.080  1.00 90.63  ? 21  ILE B HD11 1 
ATOM   4533  H HD12 . ILE B 1 21  ? 10.196  31.975  20.980  1.00 90.63  ? 21  ILE B HD12 1 
ATOM   4534  H HD13 . ILE B 1 21  ? 10.188  30.785  22.032  1.00 90.63  ? 21  ILE B HD13 1 
ATOM   4535  N N    . LEU B 1 22  ? 11.048  26.876  17.685  1.00 75.50  ? 22  LEU B N    1 
ATOM   4536  C CA   . LEU B 1 22  ? 10.325  25.896  16.893  1.00 72.43  ? 22  LEU B CA   1 
ATOM   4537  C C    . LEU B 1 22  ? 9.329   25.168  17.786  1.00 77.16  ? 22  LEU B C    1 
ATOM   4538  O O    . LEU B 1 22  ? 9.648   24.792  18.918  1.00 70.25  ? 22  LEU B O    1 
ATOM   4539  C CB   . LEU B 1 22  ? 11.299  24.909  16.249  1.00 72.29  ? 22  LEU B CB   1 
ATOM   4540  C CG   . LEU B 1 22  ? 11.869  25.320  14.886  1.00 75.05  ? 22  LEU B CG   1 
ATOM   4541  C CD1  . LEU B 1 22  ? 12.252  26.790  14.854  1.00 79.55  ? 22  LEU B CD1  1 
ATOM   4542  C CD2  . LEU B 1 22  ? 13.071  24.456  14.522  1.00 74.59  ? 22  LEU B CD2  1 
ATOM   4543  H H    . LEU B 1 22  ? 11.616  26.522  18.226  1.00 90.60  ? 22  LEU B H    1 
ATOM   4544  H HA   . LEU B 1 22  ? 9.828   26.330  16.182  1.00 86.91  ? 22  LEU B HA   1 
ATOM   4545  H HB2  . LEU B 1 22  ? 12.050  24.789  16.850  1.00 86.75  ? 22  LEU B HB2  1 
ATOM   4546  H HB3  . LEU B 1 22  ? 10.836  24.066  16.124  1.00 86.75  ? 22  LEU B HB3  1 
ATOM   4547  H HG   . LEU B 1 22  ? 11.175  25.185  14.221  1.00 90.06  ? 22  LEU B HG   1 
ATOM   4548  H HD11 . LEU B 1 22  ? 12.772  26.963  14.053  1.00 95.46  ? 22  LEU B HD11 1 
ATOM   4549  H HD12 . LEU B 1 22  ? 11.444  27.327  14.845  1.00 95.46  ? 22  LEU B HD12 1 
ATOM   4550  H HD13 . LEU B 1 22  ? 12.778  26.996  15.642  1.00 95.46  ? 22  LEU B HD13 1 
ATOM   4551  H HD21 . LEU B 1 22  ? 13.420  24.745  13.664  1.00 89.50  ? 22  LEU B HD21 1 
ATOM   4552  H HD22 . LEU B 1 22  ? 13.751  24.557  15.206  1.00 89.50  ? 22  LEU B HD22 1 
ATOM   4553  H HD23 . LEU B 1 22  ? 12.790  23.529  14.469  1.00 89.50  ? 22  LEU B HD23 1 
ATOM   4554  N N    . ILE B 1 23  ? 8.110   25.000  17.283  1.00 77.70  ? 23  ILE B N    1 
ATOM   4555  C CA   . ILE B 1 23  ? 7.018   24.383  18.027  1.00 76.37  ? 23  ILE B CA   1 
ATOM   4556  C C    . ILE B 1 23  ? 6.735   23.023  17.400  1.00 77.41  ? 23  ILE B C    1 
ATOM   4557  O O    . ILE B 1 23  ? 6.391   22.937  16.215  1.00 77.74  ? 23  ILE B O    1 
ATOM   4558  C CB   . ILE B 1 23  ? 5.755   25.259  18.025  1.00 77.31  ? 23  ILE B CB   1 
ATOM   4559  C CG1  . ILE B 1 23  ? 6.006   26.563  18.785  1.00 76.30  ? 23  ILE B CG1  1 
ATOM   4560  C CG2  . ILE B 1 23  ? 4.578   24.491  18.621  1.00 78.56  ? 23  ILE B CG2  1 
ATOM   4561  C CD1  . ILE B 1 23  ? 6.802   26.413  20.063  1.00 77.85  ? 23  ILE B CD1  1 
ATOM   4562  H H    . ILE B 1 23  ? 7.886   25.243  16.490  1.00 93.24  ? 23  ILE B H    1 
ATOM   4563  H HA   . ILE B 1 23  ? 7.295   24.250  18.947  1.00 91.65  ? 23  ILE B HA   1 
ATOM   4564  H HB   . ILE B 1 23  ? 5.537   25.486  17.108  1.00 92.77  ? 23  ILE B HB   1 
ATOM   4565  H HG12 . ILE B 1 23  ? 6.496   27.167  18.205  1.00 91.56  ? 23  ILE B HG12 1 
ATOM   4566  H HG13 . ILE B 1 23  ? 5.149   26.951  19.020  1.00 91.56  ? 23  ILE B HG13 1 
ATOM   4567  H HG21 . ILE B 1 23  ? 3.869   25.117  18.836  1.00 94.28  ? 23  ILE B HG21 1 
ATOM   4568  H HG22 . ILE B 1 23  ? 4.262   23.844  17.971  1.00 94.28  ? 23  ILE B HG22 1 
ATOM   4569  H HG23 . ILE B 1 23  ? 4.872   24.035  19.425  1.00 94.28  ? 23  ILE B HG23 1 
ATOM   4570  H HD11 . ILE B 1 23  ? 6.704   27.220  20.593  1.00 93.42  ? 23  ILE B HD11 1 
ATOM   4571  H HD12 . ILE B 1 23  ? 6.465   25.650  20.558  1.00 93.42  ? 23  ILE B HD12 1 
ATOM   4572  H HD13 . ILE B 1 23  ? 7.736   26.276  19.839  1.00 93.42  ? 23  ILE B HD13 1 
ATOM   4573  N N    . ASP B 1 24  ? 6.867   21.968  18.195  1.00 77.03  ? 24  ASP B N    1 
ATOM   4574  C CA   . ASP B 1 24  ? 6.664   20.599  17.748  1.00 80.44  ? 24  ASP B CA   1 
ATOM   4575  C C    . ASP B 1 24  ? 5.313   20.078  18.222  1.00 80.54  ? 24  ASP B C    1 
ATOM   4576  O O    . ASP B 1 24  ? 4.733   20.575  19.190  1.00 79.15  ? 24  ASP B O    1 
ATOM   4577  C CB   . ASP B 1 24  ? 7.789   19.703  18.275  1.00 79.87  ? 24  ASP B CB   1 
ATOM   4578  C CG   . ASP B 1 24  ? 7.954   18.438  17.468  1.00 80.19  ? 24  ASP B CG   1 
ATOM   4579  O OD1  . ASP B 1 24  ? 7.103   18.169  16.592  1.00 79.74  ? 24  ASP B OD1  1 
ATOM   4580  O OD2  . ASP B 1 24  ? 8.940   17.709  17.716  1.00 80.45  ? 24  ASP B OD2  1 
ATOM   4581  H H    . ASP B 1 24  ? 7.080   22.023  19.026  1.00 92.44  ? 24  ASP B H    1 
ATOM   4582  H HA   . ASP B 1 24  ? 6.673   20.566  16.779  1.00 96.53  ? 24  ASP B HA   1 
ATOM   4583  H HB2  . ASP B 1 24  ? 8.625   20.192  18.241  1.00 95.84  ? 24  ASP B HB2  1 
ATOM   4584  H HB3  . ASP B 1 24  ? 7.589   19.450  19.191  1.00 95.84  ? 24  ASP B HB3  1 
ATOM   4585  N N    . ASN B 1 25  ? 4.810   19.066  17.514  1.00 78.45  ? 25  ASN B N    1 
ATOM   4586  C CA   . ASN B 1 25  ? 3.580   18.375  17.899  1.00 78.86  ? 25  ASN B CA   1 
ATOM   4587  C C    . ASN B 1 25  ? 2.404   19.345  17.991  1.00 80.62  ? 25  ASN B C    1 
ATOM   4588  O O    . ASN B 1 25  ? 1.610   19.319  18.931  1.00 87.64  ? 25  ASN B O    1 
ATOM   4589  C CB   . ASN B 1 25  ? 3.792   17.629  19.213  1.00 84.47  ? 25  ASN B CB   1 
ATOM   4590  C CG   . ASN B 1 25  ? 5.130   16.907  19.264  1.00 84.24  ? 25  ASN B CG   1 
ATOM   4591  O OD1  . ASN B 1 25  ? 5.335   15.914  18.572  1.00 84.26  ? 25  ASN B OD1  1 
ATOM   4592  N ND2  . ASN B 1 25  ? 6.053   17.418  20.075  1.00 85.68  ? 25  ASN B ND2  1 
ATOM   4593  H H    . ASN B 1 25  ? 5.168   18.757  16.796  1.00 94.15  ? 25  ASN B H    1 
ATOM   4594  H HA   . ASN B 1 25  ? 3.353   17.729  17.212  1.00 94.63  ? 25  ASN B HA   1 
ATOM   4595  H HB2  . ASN B 1 25  ? 3.765   18.263  19.946  1.00 101.36 ? 25  ASN B HB2  1 
ATOM   4596  H HB3  . ASN B 1 25  ? 3.089   16.969  19.320  1.00 101.36 ? 25  ASN B HB3  1 
ATOM   4597  H HD21 . ASN B 1 25  ? 5.878   18.122  20.537  1.00 102.82 ? 25  ASN B HD21 1 
ATOM   4598  H HD22 . ASN B 1 25  ? 6.825   17.044  20.138  1.00 102.82 ? 25  ASN B HD22 1 
ATOM   4599  N N    . PHE B 1 26  ? 2.293   20.204  16.984  1.00 81.66  ? 26  PHE B N    1 
ATOM   4600  C CA   . PHE B 1 26  ? 1.245   21.212  16.889  1.00 85.42  ? 26  PHE B CA   1 
ATOM   4601  C C    . PHE B 1 26  ? 0.741   21.223  15.455  1.00 87.84  ? 26  PHE B C    1 
ATOM   4602  O O    . PHE B 1 26  ? 1.530   21.082  14.517  1.00 88.23  ? 26  PHE B O    1 
ATOM   4603  C CB   . PHE B 1 26  ? 1.782   22.595  17.299  1.00 86.00  ? 26  PHE B CB   1 
ATOM   4604  C CG   . PHE B 1 26  ? 0.714   23.633  17.539  1.00 86.34  ? 26  PHE B CG   1 
ATOM   4605  C CD1  . PHE B 1 26  ? 0.026   23.690  18.743  1.00 92.08  ? 26  PHE B CD1  1 
ATOM   4606  C CD2  . PHE B 1 26  ? 0.424   24.570  16.569  1.00 86.12  ? 26  PHE B CD2  1 
ATOM   4607  C CE1  . PHE B 1 26  ? -0.944  24.658  18.959  1.00 93.45  ? 26  PHE B CE1  1 
ATOM   4608  C CE2  . PHE B 1 26  ? -0.542  25.535  16.777  1.00 89.19  ? 26  PHE B CE2  1 
ATOM   4609  C CZ   . PHE B 1 26  ? -1.226  25.581  17.971  1.00 91.02  ? 26  PHE B CZ   1 
ATOM   4610  H H    . PHE B 1 26  ? 2.835   20.223  16.316  1.00 98.00  ? 26  PHE B H    1 
ATOM   4611  H HA   . PHE B 1 26  ? 0.499   21.005  17.473  1.00 102.51 ? 26  PHE B HA   1 
ATOM   4612  H HB2  . PHE B 1 26  ? 2.288   22.499  18.121  1.00 103.20 ? 26  PHE B HB2  1 
ATOM   4613  H HB3  . PHE B 1 26  ? 2.358   22.925  16.592  1.00 103.20 ? 26  PHE B HB3  1 
ATOM   4614  H HD1  . PHE B 1 26  ? 0.218   23.073  19.411  1.00 110.50 ? 26  PHE B HD1  1 
ATOM   4615  H HD2  . PHE B 1 26  ? 0.886   24.551  15.762  1.00 103.34 ? 26  PHE B HD2  1 
ATOM   4616  H HE1  . PHE B 1 26  ? -1.403  24.685  19.767  1.00 112.13 ? 26  PHE B HE1  1 
ATOM   4617  H HE2  . PHE B 1 26  ? -0.730  26.155  16.110  1.00 107.03 ? 26  PHE B HE2  1 
ATOM   4618  H HZ   . PHE B 1 26  ? -1.875  26.232  18.113  1.00 109.22 ? 26  PHE B HZ   1 
ATOM   4619  N N    . ASP B 1 27  ? -0.572  21.355  15.286  1.00 88.37  ? 27  ASP B N    1 
ATOM   4620  C CA   . ASP B 1 27  ? -1.138  21.507  13.952  1.00 88.01  ? 27  ASP B CA   1 
ATOM   4621  C C    . ASP B 1 27  ? -0.463  22.687  13.261  1.00 88.57  ? 27  ASP B C    1 
ATOM   4622  O O    . ASP B 1 27  ? -0.706  23.841  13.626  1.00 89.54  ? 27  ASP B O    1 
ATOM   4623  C CB   . ASP B 1 27  ? -2.647  21.707  14.020  1.00 87.15  ? 27  ASP B CB   1 
ATOM   4624  C CG   . ASP B 1 27  ? -3.230  22.136  12.697  1.00 92.10  ? 27  ASP B CG   1 
ATOM   4625  O OD1  . ASP B 1 27  ? -2.669  21.766  11.640  1.00 95.19  ? 27  ASP B OD1  1 
ATOM   4626  O OD2  . ASP B 1 27  ? -4.256  22.845  12.716  1.00 95.02  ? 27  ASP B OD2  1 
ATOM   4627  H H    . ASP B 1 27  ? -1.150  21.360  15.923  1.00 106.04 ? 27  ASP B H    1 
ATOM   4628  H HA   . ASP B 1 27  ? -0.985  20.703  13.431  1.00 105.61 ? 27  ASP B HA   1 
ATOM   4629  H HB2  . ASP B 1 27  ? -3.067  20.872  14.278  1.00 104.58 ? 27  ASP B HB2  1 
ATOM   4630  H HB3  . ASP B 1 27  ? -2.847  22.395  14.675  1.00 104.58 ? 27  ASP B HB3  1 
ATOM   4631  N N    . ILE B 1 28  ? 0.401   22.412  12.278  1.00 88.55  ? 28  ILE B N    1 
ATOM   4632  C CA   . ILE B 1 28  ? 1.168   23.477  11.641  1.00 89.82  ? 28  ILE B CA   1 
ATOM   4633  C C    . ILE B 1 28  ? 0.297   24.394  10.797  1.00 89.73  ? 28  ILE B C    1 
ATOM   4634  O O    . ILE B 1 28  ? 0.760   25.460  10.374  1.00 88.89  ? 28  ILE B O    1 
ATOM   4635  C CB   . ILE B 1 28  ? 2.311   22.891  10.785  1.00 88.84  ? 28  ILE B CB   1 
ATOM   4636  C CG1  . ILE B 1 28  ? 1.779   22.346  9.455   1.00 91.70  ? 28  ILE B CG1  1 
ATOM   4637  C CG2  . ILE B 1 28  ? 3.058   21.807  11.566  1.00 86.64  ? 28  ILE B CG2  1 
ATOM   4638  C CD1  . ILE B 1 28  ? 2.755   21.442  8.706   1.00 89.56  ? 28  ILE B CD1  1 
ATOM   4639  H H    . ILE B 1 28  ? 0.558   21.625  11.969  1.00 106.26 ? 28  ILE B H    1 
ATOM   4640  H HA   . ILE B 1 28  ? 1.572   24.017  12.338  1.00 107.79 ? 28  ILE B HA   1 
ATOM   4641  H HB   . ILE B 1 28  ? 2.934   23.605  10.581  1.00 106.61 ? 28  ILE B HB   1 
ATOM   4642  H HG12 . ILE B 1 28  ? 0.977   21.829  9.631   1.00 110.03 ? 28  ILE B HG12 1 
ATOM   4643  H HG13 . ILE B 1 28  ? 1.569   23.095  8.875   1.00 110.03 ? 28  ILE B HG13 1 
ATOM   4644  H HG21 . ILE B 1 28  ? 3.807   21.494  11.034  1.00 103.97 ? 28  ILE B HG21 1 
ATOM   4645  H HG22 . ILE B 1 28  ? 3.379   22.183  12.400  1.00 103.97 ? 28  ILE B HG22 1 
ATOM   4646  H HG23 . ILE B 1 28  ? 2.451   21.072  11.746  1.00 103.97 ? 28  ILE B HG23 1 
ATOM   4647  H HD11 . ILE B 1 28  ? 2.399   21.255  7.823   1.00 107.47 ? 28  ILE B HD11 1 
ATOM   4648  H HD12 . ILE B 1 28  ? 3.609   21.896  8.628   1.00 107.47 ? 28  ILE B HD12 1 
ATOM   4649  H HD13 . ILE B 1 28  ? 2.863   20.616  9.201   1.00 107.47 ? 28  ILE B HD13 1 
ATOM   4650  N N    . TYR B 1 29  ? -0.955  24.010  10.553  1.00 90.32  ? 29  TYR B N    1 
ATOM   4651  C CA   . TYR B 1 29  ? -1.907  24.824  9.808   1.00 92.23  ? 29  TYR B CA   1 
ATOM   4652  C C    . TYR B 1 29  ? -3.008  25.376  10.708  1.00 91.82  ? 29  TYR B C    1 
ATOM   4653  O O    . TYR B 1 29  ? -4.084  25.739  10.223  1.00 97.12  ? 29  TYR B O    1 
ATOM   4654  C CB   . TYR B 1 29  ? -2.504  24.006  8.661   1.00 93.54  ? 29  TYR B CB   1 
ATOM   4655  C CG   . TYR B 1 29  ? -1.459  23.451  7.714   1.00 95.19  ? 29  TYR B CG   1 
ATOM   4656  C CD1  . TYR B 1 29  ? -0.860  24.265  6.759   1.00 94.84  ? 29  TYR B CD1  1 
ATOM   4657  C CD2  . TYR B 1 29  ? -1.070  22.121  7.776   1.00 97.42  ? 29  TYR B CD2  1 
ATOM   4658  C CE1  . TYR B 1 29  ? 0.095   23.767  5.889   1.00 96.72  ? 29  TYR B CE1  1 
ATOM   4659  C CE2  . TYR B 1 29  ? -0.120  21.614  6.912   1.00 100.58 ? 29  TYR B CE2  1 
ATOM   4660  C CZ   . TYR B 1 29  ? 0.460   22.439  5.972   1.00 98.70  ? 29  TYR B CZ   1 
ATOM   4661  O OH   . TYR B 1 29  ? 1.408   21.930  5.115   1.00 106.52 ? 29  TYR B OH   1 
ATOM   4662  H H    . TYR B 1 29  ? -1.284  23.261  10.817  1.00 108.38 ? 29  TYR B H    1 
ATOM   4663  H HA   . TYR B 1 29  ? -1.441  25.581  9.420   1.00 110.67 ? 29  TYR B HA   1 
ATOM   4664  H HB2  . TYR B 1 29  ? -2.997  23.258  9.033   1.00 112.25 ? 29  TYR B HB2  1 
ATOM   4665  H HB3  . TYR B 1 29  ? -3.100  24.574  8.149   1.00 112.25 ? 29  TYR B HB3  1 
ATOM   4666  H HD1  . TYR B 1 29  ? -1.104  25.161  6.704   1.00 113.81 ? 29  TYR B HD1  1 
ATOM   4667  H HD2  . TYR B 1 29  ? -1.456  21.561  8.411   1.00 116.91 ? 29  TYR B HD2  1 
ATOM   4668  H HE1  . TYR B 1 29  ? 0.487   24.323  5.254   1.00 116.06 ? 29  TYR B HE1  1 
ATOM   4669  H HE2  . TYR B 1 29  ? 0.127   20.719  6.963   1.00 120.69 ? 29  TYR B HE2  1 
ATOM   4670  H HH   . TYR B 1 29  ? 1.716   21.211  5.422   1.00 127.82 ? 29  TYR B HH   1 
ATOM   4671  N N    . ASP B 1 30  ? -2.754  25.448  12.011  1.00 93.16  ? 30  ASP B N    1 
ATOM   4672  C CA   . ASP B 1 30  ? -3.717  26.007  12.950  1.00 95.85  ? 30  ASP B CA   1 
ATOM   4673  C C    . ASP B 1 30  ? -3.905  27.498  12.690  1.00 95.86  ? 30  ASP B C    1 
ATOM   4674  O O    . ASP B 1 30  ? -2.981  28.205  12.279  1.00 93.76  ? 30  ASP B O    1 
ATOM   4675  C CB   . ASP B 1 30  ? -3.249  25.764  14.385  1.00 92.97  ? 30  ASP B CB   1 
ATOM   4676  C CG   . ASP B 1 30  ? -4.330  26.061  15.417  1.00 94.95  ? 30  ASP B CG   1 
ATOM   4677  O OD1  . ASP B 1 30  ? -4.548  27.251  15.717  1.00 98.49  ? 30  ASP B OD1  1 
ATOM   4678  O OD2  . ASP B 1 30  ? -4.945  25.107  15.937  1.00 93.68  ? 30  ASP B OD2  1 
ATOM   4679  H H    . ASP B 1 30  ? -2.026  25.177  12.380  1.00 111.79 ? 30  ASP B H    1 
ATOM   4680  H HA   . ASP B 1 30  ? -4.579  25.575  12.842  1.00 115.02 ? 30  ASP B HA   1 
ATOM   4681  H HB2  . ASP B 1 30  ? -2.991  24.834  14.480  1.00 111.57 ? 30  ASP B HB2  1 
ATOM   4682  H HB3  . ASP B 1 30  ? -2.490  26.339  14.571  1.00 111.57 ? 30  ASP B HB3  1 
ATOM   4683  N N    . LYS B 1 31  ? -5.126  27.975  12.941  1.00 97.51  ? 31  LYS B N    1 
ATOM   4684  C CA   . LYS B 1 31  ? -5.476  29.350  12.604  1.00 100.26 ? 31  LYS B CA   1 
ATOM   4685  C C    . LYS B 1 31  ? -4.913  30.362  13.594  1.00 100.91 ? 31  LYS B C    1 
ATOM   4686  O O    . LYS B 1 31  ? -4.654  31.510  13.214  1.00 102.45 ? 31  LYS B O    1 
ATOM   4687  C CB   . LYS B 1 31  ? -6.997  29.493  12.530  1.00 104.70 ? 31  LYS B CB   1 
ATOM   4688  C CG   . LYS B 1 31  ? -7.667  28.492  11.604  1.00 109.96 ? 31  LYS B CG   1 
ATOM   4689  C CD   . LYS B 1 31  ? -9.069  28.943  11.217  1.00 118.20 ? 31  LYS B CD   1 
ATOM   4690  C CE   . LYS B 1 31  ? -9.810  27.857  10.448  1.00 121.53 ? 31  LYS B CE   1 
ATOM   4691  N NZ   . LYS B 1 31  ? -10.488 26.888  11.358  1.00 118.96 ? 31  LYS B NZ   1 
ATOM   4692  H H    . LYS B 1 31  ? -5.764  27.525  13.303  1.00 117.01 ? 31  LYS B H    1 
ATOM   4693  H HA   . LYS B 1 31  ? -5.101  29.554  11.732  1.00 120.32 ? 31  LYS B HA   1 
ATOM   4694  H HB2  . LYS B 1 31  ? -7.365  29.366  13.418  1.00 125.64 ? 31  LYS B HB2  1 
ATOM   4695  H HB3  . LYS B 1 31  ? -7.210  30.383  12.206  1.00 125.64 ? 31  LYS B HB3  1 
ATOM   4696  H HG2  . LYS B 1 31  ? -7.142  28.402  10.794  1.00 131.96 ? 31  LYS B HG2  1 
ATOM   4697  H HG3  . LYS B 1 31  ? -7.736  27.635  12.053  1.00 131.96 ? 31  LYS B HG3  1 
ATOM   4698  H HD2  . LYS B 1 31  ? -9.575  29.148  12.019  1.00 141.83 ? 31  LYS B HD2  1 
ATOM   4699  H HD3  . LYS B 1 31  ? -9.010  29.730  10.653  1.00 141.83 ? 31  LYS B HD3  1 
ATOM   4700  H HE2  . LYS B 1 31  ? -10.485 28.267  9.885   1.00 145.83 ? 31  LYS B HE2  1 
ATOM   4701  H HE3  . LYS B 1 31  ? -9.177  27.365  9.901   1.00 145.83 ? 31  LYS B HE3  1 
ATOM   4702  H HZ1  . LYS B 1 31  ? -11.083 27.313  11.866  1.00 142.75 ? 31  LYS B HZ1  1 
ATOM   4703  H HZ2  . LYS B 1 31  ? -10.908 26.265  10.882  1.00 142.75 ? 31  LYS B HZ2  1 
ATOM   4704  H HZ3  . LYS B 1 31  ? -9.889  26.494  11.885  1.00 142.75 ? 31  LYS B HZ3  1 
ATOM   4705  N N    . ASN B 1 32  ? -4.721  29.971  14.852  1.00 97.57  ? 32  ASN B N    1 
ATOM   4706  C CA   . ASN B 1 32  ? -4.221  30.877  15.877  1.00 97.48  ? 32  ASN B CA   1 
ATOM   4707  C C    . ASN B 1 32  ? -2.701  30.967  15.898  1.00 95.11  ? 32  ASN B C    1 
ATOM   4708  O O    . ASN B 1 32  ? -2.150  31.705  16.724  1.00 93.83  ? 32  ASN B O    1 
ATOM   4709  C CB   . ASN B 1 32  ? -4.732  30.442  17.255  1.00 99.48  ? 32  ASN B CB   1 
ATOM   4710  C CG   . ASN B 1 32  ? -6.234  30.611  17.400  1.00 102.09 ? 32  ASN B CG   1 
ATOM   4711  O OD1  . ASN B 1 32  ? -7.001  30.249  16.506  1.00 104.22 ? 32  ASN B OD1  1 
ATOM   4712  N ND2  . ASN B 1 32  ? -6.661  31.165  18.527  1.00 102.06 ? 32  ASN B ND2  1 
ATOM   4713  H H    . ASN B 1 32  ? -4.877  29.175  15.137  1.00 117.09 ? 32  ASN B H    1 
ATOM   4714  H HA   . ASN B 1 32  ? -4.565  31.766  15.700  1.00 116.97 ? 32  ASN B HA   1 
ATOM   4715  H HB2  . ASN B 1 32  ? -4.520  29.505  17.390  1.00 119.37 ? 32  ASN B HB2  1 
ATOM   4716  H HB3  . ASN B 1 32  ? -4.301  30.981  17.937  1.00 119.37 ? 32  ASN B HB3  1 
ATOM   4717  H HD21 . ASN B 1 32  ? -6.096  31.407  19.128  1.00 122.47 ? 32  ASN B HD21 1 
ATOM   4718  H HD22 . ASN B 1 32  ? -7.504  31.282  18.657  1.00 122.47 ? 32  ASN B HD22 1 
ATOM   4719  N N    . ILE B 1 33  ? -2.017  30.243  15.009  1.00 93.76  ? 33  ILE B N    1 
ATOM   4720  C CA   . ILE B 1 33  ? -0.554  30.298  14.964  1.00 91.74  ? 33  ILE B CA   1 
ATOM   4721  C C    . ILE B 1 33  ? -0.050  31.733  14.918  1.00 92.05  ? 33  ILE B C    1 
ATOM   4722  O O    . ILE B 1 33  ? 0.870   32.068  15.687  1.00 90.28  ? 33  ILE B O    1 
ATOM   4723  C CB   . ILE B 1 33  ? -0.031  29.445  13.797  1.00 90.14  ? 33  ILE B CB   1 
ATOM   4724  C CG1  . ILE B 1 33  ? 0.007   27.969  14.221  1.00 92.15  ? 33  ILE B CG1  1 
ATOM   4725  C CG2  . ILE B 1 33  ? 1.336   29.942  13.335  1.00 85.20  ? 33  ILE B CG2  1 
ATOM   4726  C CD1  . ILE B 1 33  ? 0.595   27.024  13.190  1.00 90.05  ? 33  ILE B CD1  1 
ATOM   4727  H H    . ILE B 1 33  ? -2.372  29.718  14.427  1.00 112.52 ? 33  ILE B H    1 
ATOM   4728  H HA   . ILE B 1 33  ? -0.217  29.897  15.780  1.00 110.09 ? 33  ILE B HA   1 
ATOM   4729  H HB   . ILE B 1 33  ? -0.633  29.530  13.041  1.00 108.17 ? 33  ILE B HB   1 
ATOM   4730  H HG12 . ILE B 1 33  ? 0.545   27.894  15.025  1.00 110.58 ? 33  ILE B HG12 1 
ATOM   4731  H HG13 . ILE B 1 33  ? -0.900  27.677  14.400  1.00 110.58 ? 33  ILE B HG13 1 
ATOM   4732  H HG21 . ILE B 1 33  ? 1.746   29.264  12.775  1.00 102.24 ? 33  ILE B HG21 1 
ATOM   4733  H HG22 . ILE B 1 33  ? 1.220   30.762  12.831  1.00 102.24 ? 33  ILE B HG22 1 
ATOM   4734  H HG23 . ILE B 1 33  ? 1.891   30.107  14.114  1.00 102.24 ? 33  ILE B HG23 1 
ATOM   4735  H HD11 . ILE B 1 33  ? 0.319   26.117  13.399  1.00 108.06 ? 33  ILE B HD11 1 
ATOM   4736  H HD12 . ILE B 1 33  ? 0.270   27.274  12.311  1.00 108.06 ? 33  ILE B HD12 1 
ATOM   4737  H HD13 . ILE B 1 33  ? 1.562   27.090  13.216  1.00 108.06 ? 33  ILE B HD13 1 
ATOM   4738  N N    . PRO B 1 34  ? -0.576  32.626  14.075  1.00 92.80  ? 34  PRO B N    1 
ATOM   4739  C CA   . PRO B 1 34  ? -0.041  33.997  14.032  1.00 91.52  ? 34  PRO B CA   1 
ATOM   4740  C C    . PRO B 1 34  ? -0.089  34.700  15.377  1.00 92.26  ? 34  PRO B C    1 
ATOM   4741  O O    . PRO B 1 34  ? 0.797   35.509  15.682  1.00 90.11  ? 34  PRO B O    1 
ATOM   4742  C CB   . PRO B 1 34  ? -0.938  34.696  12.995  1.00 93.50  ? 34  PRO B CB   1 
ATOM   4743  C CG   . PRO B 1 34  ? -1.504  33.571  12.158  1.00 95.26  ? 34  PRO B CG   1 
ATOM   4744  C CD   . PRO B 1 34  ? -1.701  32.441  13.136  1.00 93.19  ? 34  PRO B CD   1 
ATOM   4745  H HA   . PRO B 1 34  ? 0.872   33.985  13.706  1.00 109.82 ? 34  PRO B HA   1 
ATOM   4746  H HB2  . PRO B 1 34  ? -1.644  35.186  13.445  1.00 112.20 ? 34  PRO B HB2  1 
ATOM   4747  H HB3  . PRO B 1 34  ? -0.408  35.301  12.453  1.00 112.20 ? 34  PRO B HB3  1 
ATOM   4748  H HG2  . PRO B 1 34  ? -2.347  33.841  11.762  1.00 114.31 ? 34  PRO B HG2  1 
ATOM   4749  H HG3  . PRO B 1 34  ? -0.875  33.324  11.462  1.00 114.31 ? 34  PRO B HG3  1 
ATOM   4750  H HD2  . PRO B 1 34  ? -2.553  32.521  13.593  1.00 111.83 ? 34  PRO B HD2  1 
ATOM   4751  H HD3  . PRO B 1 34  ? -1.644  31.581  12.691  1.00 111.83 ? 34  PRO B HD3  1 
ATOM   4752  N N    . LYS B 1 35  ? -1.102  34.410  16.192  1.00 93.90  ? 35  LYS B N    1 
ATOM   4753  C CA   . LYS B 1 35  ? -1.280  35.058  17.484  1.00 92.66  ? 35  LYS B CA   1 
ATOM   4754  C C    . LYS B 1 35  ? -0.507  34.351  18.588  1.00 92.01  ? 35  LYS B C    1 
ATOM   4755  O O    . LYS B 1 35  ? 0.117   35.012  19.426  1.00 90.92  ? 35  LYS B O    1 
ATOM   4756  C CB   . LYS B 1 35  ? -2.772  35.113  17.832  1.00 95.50  ? 35  LYS B CB   1 
ATOM   4757  C CG   . LYS B 1 35  ? -3.709  34.978  16.629  1.00 99.97  ? 35  LYS B CG   1 
ATOM   4758  C CD   . LYS B 1 35  ? -5.176  34.898  17.049  1.00 104.67 ? 35  LYS B CD   1 
ATOM   4759  C CE   . LYS B 1 35  ? -5.699  36.246  17.530  1.00 108.82 ? 35  LYS B CE   1 
ATOM   4760  N NZ   . LYS B 1 35  ? -6.884  36.078  18.423  1.00 110.33 ? 35  LYS B NZ   1 
ATOM   4761  H H    . LYS B 1 35  ? -1.711  33.829  16.014  1.00 112.68 ? 35  LYS B H    1 
ATOM   4762  H HA   . LYS B 1 35  ? -0.954  35.970  17.433  1.00 111.19 ? 35  LYS B HA   1 
ATOM   4763  H HB2  . LYS B 1 35  ? -2.974  34.388  18.444  1.00 114.60 ? 35  LYS B HB2  1 
ATOM   4764  H HB3  . LYS B 1 35  ? -2.960  35.966  18.255  1.00 114.60 ? 35  LYS B HB3  1 
ATOM   4765  H HG2  . LYS B 1 35  ? -3.601  35.751  16.052  1.00 119.96 ? 35  LYS B HG2  1 
ATOM   4766  H HG3  . LYS B 1 35  ? -3.489  34.168  16.143  1.00 119.96 ? 35  LYS B HG3  1 
ATOM   4767  H HD2  . LYS B 1 35  ? -5.711  34.617  16.290  1.00 125.61 ? 35  LYS B HD2  1 
ATOM   4768  H HD3  . LYS B 1 35  ? -5.267  34.260  17.774  1.00 125.61 ? 35  LYS B HD3  1 
ATOM   4769  H HE2  . LYS B 1 35  ? -5.002  36.702  18.027  1.00 130.58 ? 35  LYS B HE2  1 
ATOM   4770  H HE3  . LYS B 1 35  ? -5.965  36.779  16.765  1.00 130.58 ? 35  LYS B HE3  1 
ATOM   4771  H HZ1  . LYS B 1 35  ? -7.173  36.873  18.697  1.00 132.40 ? 35  LYS B HZ1  1 
ATOM   4772  H HZ2  . LYS B 1 35  ? -7.540  35.667  17.984  1.00 132.40 ? 35  LYS B HZ2  1 
ATOM   4773  H HZ3  . LYS B 1 35  ? -6.663  35.590  19.134  1.00 132.40 ? 35  LYS B HZ3  1 
ATOM   4774  N N    . LEU B 1 36  ? -0.540  33.016  18.608  1.00 92.99  ? 36  LEU B N    1 
ATOM   4775  C CA   . LEU B 1 36  ? 0.292   32.270  19.545  1.00 90.78  ? 36  LEU B CA   1 
ATOM   4776  C C    . LEU B 1 36  ? 1.750   32.695  19.416  1.00 90.09  ? 36  LEU B C    1 
ATOM   4777  O O    . LEU B 1 36  ? 2.428   32.961  20.414  1.00 89.09  ? 36  LEU B O    1 
ATOM   4778  C CB   . LEU B 1 36  ? 0.157   30.770  19.294  1.00 90.52  ? 36  LEU B CB   1 
ATOM   4779  C CG   . LEU B 1 36  ? -1.185  30.100  19.578  1.00 94.46  ? 36  LEU B CG   1 
ATOM   4780  C CD1  . LEU B 1 36  ? -0.990  28.585  19.667  1.00 95.51  ? 36  LEU B CD1  1 
ATOM   4781  C CD2  . LEU B 1 36  ? -1.834  30.619  20.846  1.00 96.38  ? 36  LEU B CD2  1 
ATOM   4782  H H    . LEU B 1 36  ? -1.029  32.528  18.096  1.00 111.59 ? 36  LEU B H    1 
ATOM   4783  H HA   . LEU B 1 36  ? -0.011  32.451  20.449  1.00 108.94 ? 36  LEU B HA   1 
ATOM   4784  H HB2  . LEU B 1 36  ? 0.352   30.612  18.357  1.00 108.62 ? 36  LEU B HB2  1 
ATOM   4785  H HB3  . LEU B 1 36  ? 0.813   30.321  19.849  1.00 108.62 ? 36  LEU B HB3  1 
ATOM   4786  H HG   . LEU B 1 36  ? -1.790  30.311  18.850  1.00 113.36 ? 36  LEU B HG   1 
ATOM   4787  H HD11 . LEU B 1 36  ? -1.852  28.163  19.806  1.00 114.61 ? 36  LEU B HD11 1 
ATOM   4788  H HD12 . LEU B 1 36  ? -0.596  28.268  18.839  1.00 114.61 ? 36  LEU B HD12 1 
ATOM   4789  H HD13 . LEU B 1 36  ? -0.400  28.385  20.411  1.00 114.61 ? 36  LEU B HD13 1 
ATOM   4790  H HD21 . LEU B 1 36  ? -2.612  30.076  21.047  1.00 115.66 ? 36  LEU B HD21 1 
ATOM   4791  H HD22 . LEU B 1 36  ? -1.195  30.564  21.573  1.00 115.66 ? 36  LEU B HD22 1 
ATOM   4792  H HD23 . LEU B 1 36  ? -2.101  31.542  20.709  1.00 115.66 ? 36  LEU B HD23 1 
ATOM   4793  N N    . SER B 1 37  ? 2.245   32.768  18.177  1.00 90.31  ? 37  SER B N    1 
ATOM   4794  C CA   . SER B 1 37  ? 3.641   33.127  17.953  1.00 87.92  ? 37  SER B CA   1 
ATOM   4795  C C    . SER B 1 37  ? 3.951   34.510  18.510  1.00 88.77  ? 37  SER B C    1 
ATOM   4796  O O    . SER B 1 37  ? 5.043   34.740  19.041  1.00 88.28  ? 37  SER B O    1 
ATOM   4797  C CB   . SER B 1 37  ? 3.961   33.060  16.459  1.00 88.35  ? 37  SER B CB   1 
ATOM   4798  O OG   . SER B 1 37  ? 3.771   31.748  15.953  1.00 84.71  ? 37  SER B OG   1 
ATOM   4799  H H    . SER B 1 37  ? 1.797   32.616  17.459  1.00 108.38 ? 37  SER B H    1 
ATOM   4800  H HA   . SER B 1 37  ? 4.209   32.488  18.412  1.00 105.51 ? 37  SER B HA   1 
ATOM   4801  H HB2  . SER B 1 37  ? 3.373   33.668  15.984  1.00 106.02 ? 37  SER B HB2  1 
ATOM   4802  H HB3  . SER B 1 37  ? 4.886   33.319  16.323  1.00 106.02 ? 37  SER B HB3  1 
ATOM   4803  H HG   . SER B 1 37  ? 3.954   31.727  15.133  1.00 101.65 ? 37  SER B HG   1 
ATOM   4804  N N    . GLU B 1 38  ? 3.002   35.443  18.407  1.00 91.25  ? 38  GLU B N    1 
ATOM   4805  C CA   . GLU B 1 38  ? 3.235   36.779  18.949  1.00 92.93  ? 38  GLU B CA   1 
ATOM   4806  C C    . GLU B 1 38  ? 3.524   36.721  20.445  1.00 90.38  ? 38  GLU B C    1 
ATOM   4807  O O    . GLU B 1 38  ? 4.418   37.418  20.939  1.00 90.77  ? 38  GLU B O    1 
ATOM   4808  C CB   . GLU B 1 38  ? 2.034   37.682  18.675  1.00 93.58  ? 38  GLU B CB   1 
ATOM   4809  C CG   . GLU B 1 38  ? 2.272   39.140  19.040  1.00 99.67  ? 38  GLU B CG   1 
ATOM   4810  C CD   . GLU B 1 38  ? 1.246   40.074  18.423  1.00 106.61 ? 38  GLU B CD   1 
ATOM   4811  O OE1  . GLU B 1 38  ? 0.042   39.740  18.459  1.00 109.16 ? 38  GLU B OE1  1 
ATOM   4812  O OE2  . GLU B 1 38  ? 1.642   41.141  17.904  1.00 105.38 ? 38  GLU B OE2  1 
ATOM   4813  H H    . GLU B 1 38  ? 2.234   35.331  18.037  1.00 109.50 ? 38  GLU B H    1 
ATOM   4814  H HA   . GLU B 1 38  ? 4.006   37.163  18.503  1.00 111.52 ? 38  GLU B HA   1 
ATOM   4815  H HB2  . GLU B 1 38  ? 1.824   37.644  17.729  1.00 112.29 ? 38  GLU B HB2  1 
ATOM   4816  H HB3  . GLU B 1 38  ? 1.280   37.365  19.196  1.00 112.29 ? 38  GLU B HB3  1 
ATOM   4817  H HG2  . GLU B 1 38  ? 2.224   39.236  20.004  1.00 119.60 ? 38  GLU B HG2  1 
ATOM   4818  H HG3  . GLU B 1 38  ? 3.149   39.406  18.724  1.00 119.60 ? 38  GLU B HG3  1 
ATOM   4819  N N    . GLU B 1 39  ? 2.775   35.894  21.183  1.00 89.27  ? 39  GLU B N    1 
ATOM   4820  C CA   . GLU B 1 39  ? 3.027   35.754  22.613  1.00 88.73  ? 39  GLU B CA   1 
ATOM   4821  C C    . GLU B 1 39  ? 4.381   35.102  22.867  1.00 84.96  ? 39  GLU B C    1 
ATOM   4822  O O    . GLU B 1 39  ? 5.128   35.526  23.755  1.00 85.25  ? 39  GLU B O    1 
ATOM   4823  C CB   . GLU B 1 39  ? 1.915   34.937  23.272  1.00 88.54  ? 39  GLU B CB   1 
ATOM   4824  C CG   . GLU B 1 39  ? 0.514   35.539  23.176  1.00 90.63  ? 39  GLU B CG   1 
ATOM   4825  C CD   . GLU B 1 39  ? 0.364   36.850  23.933  1.00 97.69  ? 39  GLU B CD   1 
ATOM   4826  O OE1  . GLU B 1 39  ? 1.333   37.631  23.970  1.00 97.78  ? 39  GLU B OE1  1 
ATOM   4827  O OE2  . GLU B 1 39  ? -0.725  37.112  24.487  1.00 100.34 ? 39  GLU B OE2  1 
ATOM   4828  H H    . GLU B 1 39  ? 2.129   35.413  20.882  1.00 107.12 ? 39  GLU B H    1 
ATOM   4829  H HA   . GLU B 1 39  ? 3.027   36.637  23.015  1.00 106.48 ? 39  GLU B HA   1 
ATOM   4830  H HB2  . GLU B 1 39  ? 1.884   34.065  22.848  1.00 106.25 ? 39  GLU B HB2  1 
ATOM   4831  H HB3  . GLU B 1 39  ? 2.124   34.840  24.214  1.00 106.25 ? 39  GLU B HB3  1 
ATOM   4832  H HG2  . GLU B 1 39  ? 0.309   35.710  22.243  1.00 108.75 ? 39  GLU B HG2  1 
ATOM   4833  H HG3  . GLU B 1 39  ? -0.124  34.909  23.545  1.00 108.75 ? 39  GLU B HG3  1 
ATOM   4834  N N    . ILE B 1 40  ? 4.717   34.075  22.089  1.00 85.80  ? 40  ILE B N    1 
ATOM   4835  C CA   . ILE B 1 40  ? 5.979   33.375  22.282  1.00 86.04  ? 40  ILE B CA   1 
ATOM   4836  C C    . ILE B 1 40  ? 7.160   34.341  22.236  1.00 85.03  ? 40  ILE B C    1 
ATOM   4837  O O    . ILE B 1 40  ? 8.148   34.154  22.952  1.00 82.15  ? 40  ILE B O    1 
ATOM   4838  C CB   . ILE B 1 40  ? 6.127   32.266  21.220  1.00 84.45  ? 40  ILE B CB   1 
ATOM   4839  C CG1  . ILE B 1 40  ? 4.999   31.231  21.325  1.00 83.39  ? 40  ILE B CG1  1 
ATOM   4840  C CG2  . ILE B 1 40  ? 7.490   31.590  21.335  1.00 81.84  ? 40  ILE B CG2  1 
ATOM   4841  C CD1  . ILE B 1 40  ? 4.407   31.059  22.699  1.00 85.67  ? 40  ILE B CD1  1 
ATOM   4842  H H    . ILE B 1 40  ? 4.234   33.768  21.447  1.00 102.97 ? 40  ILE B H    1 
ATOM   4843  H HA   . ILE B 1 40  ? 5.970   32.966  23.161  1.00 103.25 ? 40  ILE B HA   1 
ATOM   4844  H HB   . ILE B 1 40  ? 6.061   32.687  20.348  1.00 101.35 ? 40  ILE B HB   1 
ATOM   4845  H HG12 . ILE B 1 40  ? 4.280   31.501  20.733  1.00 100.07 ? 40  ILE B HG12 1 
ATOM   4846  H HG13 . ILE B 1 40  ? 5.349   30.369  21.051  1.00 100.07 ? 40  ILE B HG13 1 
ATOM   4847  H HG21 . ILE B 1 40  ? 7.479   30.767  20.821  1.00 98.21  ? 40  ILE B HG21 1 
ATOM   4848  H HG22 . ILE B 1 40  ? 8.170   32.188  20.987  1.00 98.21  ? 40  ILE B HG22 1 
ATOM   4849  H HG23 . ILE B 1 40  ? 7.668   31.394  22.268  1.00 98.21  ? 40  ILE B HG23 1 
ATOM   4850  H HD11 . ILE B 1 40  ? 3.859   30.259  22.709  1.00 102.81 ? 40  ILE B HD11 1 
ATOM   4851  H HD12 . ILE B 1 40  ? 5.127   30.975  23.345  1.00 102.81 ? 40  ILE B HD12 1 
ATOM   4852  H HD13 . ILE B 1 40  ? 3.864   31.835  22.909  1.00 102.81 ? 40  ILE B HD13 1 
ATOM   4853  N N    . MET B 1 41  ? 7.085   35.379  21.400  1.00 85.76  ? 41  MET B N    1 
ATOM   4854  C CA   . MET B 1 41  ? 8.252   36.208  21.116  1.00 83.58  ? 41  MET B CA   1 
ATOM   4855  C C    . MET B 1 41  ? 8.481   37.318  22.133  1.00 83.45  ? 41  MET B C    1 
ATOM   4856  O O    . MET B 1 41  ? 9.622   37.773  22.290  1.00 82.81  ? 41  MET B O    1 
ATOM   4857  C CB   . MET B 1 41  ? 8.122   36.843  19.728  1.00 84.14  ? 41  MET B CB   1 
ATOM   4858  C CG   . MET B 1 41  ? 7.958   35.845  18.601  1.00 83.11  ? 41  MET B CG   1 
ATOM   4859  S SD   . MET B 1 41  ? 7.529   36.644  17.050  1.00 81.63  ? 41  MET B SD   1 
ATOM   4860  C CE   . MET B 1 41  ? 9.149   36.815  16.310  1.00 80.40  ? 41  MET B CE   1 
ATOM   4861  H H    . MET B 1 41  ? 6.370   35.622  20.988  1.00 102.92 ? 41  MET B H    1 
ATOM   4862  H HA   . MET B 1 41  ? 9.027   35.624  21.120  1.00 100.30 ? 41  MET B HA   1 
ATOM   4863  H HB2  . MET B 1 41  ? 7.345   37.422  19.724  1.00 100.97 ? 41  MET B HB2  1 
ATOM   4864  H HB3  . MET B 1 41  ? 8.923   37.360  19.548  1.00 100.97 ? 41  MET B HB3  1 
ATOM   4865  H HG2  . MET B 1 41  ? 8.792   35.366  18.475  1.00 99.73  ? 41  MET B HG2  1 
ATOM   4866  H HG3  . MET B 1 41  ? 7.249   35.222  18.827  1.00 99.73  ? 41  MET B HG3  1 
ATOM   4867  H HE1  . MET B 1 41  ? 9.095   37.444  15.573  1.00 96.48  ? 41  MET B HE1  1 
ATOM   4868  H HE2  . MET B 1 41  ? 9.769   37.143  16.980  1.00 96.48  ? 41  MET B HE2  1 
ATOM   4869  H HE3  . MET B 1 41  ? 9.441   35.949  15.985  1.00 96.48  ? 41  MET B HE3  1 
ATOM   4870  N N    . LYS B 1 42  ? 7.430   37.774  22.812  1.00 83.17  ? 42  LYS B N    1 
ATOM   4871  C CA   . LYS B 1 42  ? 7.573   38.862  23.765  1.00 80.47  ? 42  LYS B CA   1 
ATOM   4872  C C    . LYS B 1 42  ? 8.699   38.563  24.744  1.00 80.41  ? 42  LYS B C    1 
ATOM   4873  O O    . LYS B 1 42  ? 8.979   37.405  25.069  1.00 83.78  ? 42  LYS B O    1 
ATOM   4874  C CB   . LYS B 1 42  ? 6.266   39.072  24.527  1.00 82.18  ? 42  LYS B CB   1 
ATOM   4875  C CG   . LYS B 1 42  ? 5.156   39.695  23.702  1.00 87.42  ? 42  LYS B CG   1 
ATOM   4876  C CD   . LYS B 1 42  ? 4.031   40.196  24.598  1.00 87.57  ? 42  LYS B CD   1 
ATOM   4877  C CE   . LYS B 1 42  ? 2.669   40.011  23.944  1.00 91.89  ? 42  LYS B CE   1 
ATOM   4878  N NZ   . LYS B 1 42  ? 2.125   41.279  23.375  1.00 96.14  ? 42  LYS B NZ   1 
ATOM   4879  H H    . LYS B 1 42  ? 6.629   37.471  22.737  1.00 99.81  ? 42  LYS B H    1 
ATOM   4880  H HA   . LYS B 1 42  ? 7.786   39.681  23.292  1.00 96.57  ? 42  LYS B HA   1 
ATOM   4881  H HB2  . LYS B 1 42  ? 5.950   38.211  24.842  1.00 98.61  ? 42  LYS B HB2  1 
ATOM   4882  H HB3  . LYS B 1 42  ? 6.437   39.659  25.280  1.00 98.61  ? 42  LYS B HB3  1 
ATOM   4883  H HG2  . LYS B 1 42  ? 5.508   40.447  23.200  1.00 104.91 ? 42  LYS B HG2  1 
ATOM   4884  H HG3  . LYS B 1 42  ? 4.793   39.031  23.094  1.00 104.91 ? 42  LYS B HG3  1 
ATOM   4885  H HD2  . LYS B 1 42  ? 4.039   39.699  25.431  1.00 105.08 ? 42  LYS B HD2  1 
ATOM   4886  H HD3  . LYS B 1 42  ? 4.158   41.141  24.775  1.00 105.08 ? 42  LYS B HD3  1 
ATOM   4887  H HE2  . LYS B 1 42  ? 2.750   39.369  23.222  1.00 110.26 ? 42  LYS B HE2  1 
ATOM   4888  H HE3  . LYS B 1 42  ? 2.041   39.686  24.608  1.00 110.26 ? 42  LYS B HE3  1 
ATOM   4889  H HZ1  . LYS B 1 42  ? 1.336   41.127  22.993  1.00 115.37 ? 42  LYS B HZ1  1 
ATOM   4890  H HZ2  . LYS B 1 42  ? 2.023   41.883  24.020  1.00 115.37 ? 42  LYS B HZ2  1 
ATOM   4891  H HZ3  . LYS B 1 42  ? 2.684   41.602  22.763  1.00 115.37 ? 42  LYS B HZ3  1 
ATOM   4892  N N    . GLU B 1 43  ? 9.356   39.623  25.218  1.00 77.39  ? 43  GLU B N    1 
ATOM   4893  C CA   . GLU B 1 43  ? 10.358  39.435  26.260  1.00 85.74  ? 43  GLU B CA   1 
ATOM   4894  C C    . GLU B 1 43  ? 9.726   38.938  27.555  1.00 81.50  ? 43  GLU B C    1 
ATOM   4895  O O    . GLU B 1 43  ? 10.365  38.184  28.299  1.00 81.18  ? 43  GLU B O    1 
ATOM   4896  C CB   . GLU B 1 43  ? 11.124  40.734  26.497  1.00 87.52  ? 43  GLU B CB   1 
ATOM   4897  C CG   . GLU B 1 43  ? 10.523  41.636  27.550  1.00 89.33  ? 43  GLU B CG   1 
ATOM   4898  C CD   . GLU B 1 43  ? 11.170  43.003  27.555  1.00 94.92  ? 43  GLU B CD   1 
ATOM   4899  O OE1  . GLU B 1 43  ? 12.404  43.070  27.742  1.00 98.10  ? 43  GLU B OE1  1 
ATOM   4900  O OE2  . GLU B 1 43  ? 10.451  44.005  27.362  1.00 99.16  ? 43  GLU B OE2  1 
ATOM   4901  H H    . GLU B 1 43  ? 9.243   40.436  24.960  1.00 92.86  ? 43  GLU B H    1 
ATOM   4902  H HA   . GLU B 1 43  ? 10.998  38.769  25.964  1.00 102.90 ? 43  GLU B HA   1 
ATOM   4903  H HB2  . GLU B 1 43  ? 12.025  40.513  26.780  1.00 105.03 ? 43  GLU B HB2  1 
ATOM   4904  H HB3  . GLU B 1 43  ? 11.150  41.232  25.665  1.00 105.03 ? 43  GLU B HB3  1 
ATOM   4905  H HG2  . GLU B 1 43  ? 9.576   41.749  27.371  1.00 107.19 ? 43  GLU B HG2  1 
ATOM   4906  H HG3  . GLU B 1 43  ? 10.650  41.236  28.424  1.00 107.19 ? 43  GLU B HG3  1 
ATOM   4907  N N    . THR B 1 44  ? 8.479   39.337  27.840  1.00 80.53  ? 44  THR B N    1 
ATOM   4908  C CA   . THR B 1 44  ? 7.793   38.868  29.040  1.00 82.29  ? 44  THR B CA   1 
ATOM   4909  C C    . THR B 1 44  ? 7.461   37.383  28.980  1.00 78.80  ? 44  THR B C    1 
ATOM   4910  O O    . THR B 1 44  ? 7.113   36.799  30.011  1.00 78.58  ? 44  THR B O    1 
ATOM   4911  C CB   . THR B 1 44  ? 6.499   39.656  29.279  1.00 82.95  ? 44  THR B CB   1 
ATOM   4912  O OG1  . THR B 1 44  ? 5.440   39.095  28.490  1.00 87.06  ? 44  THR B OG1  1 
ATOM   4913  C CG2  . THR B 1 44  ? 6.675   41.124  28.922  1.00 85.51  ? 44  THR B CG2  1 
ATOM   4914  H H    . THR B 1 44  ? 8.015   39.875  27.355  1.00 96.64  ? 44  THR B H    1 
ATOM   4915  H HA   . THR B 1 44  ? 8.379   39.028  29.797  1.00 98.75  ? 44  THR B HA   1 
ATOM   4916  H HB   . THR B 1 44  ? 6.266   39.604  30.219  1.00 99.53  ? 44  THR B HB   1 
ATOM   4917  H HG1  . THR B 1 44  ? 4.728   39.520  28.621  1.00 104.47 ? 44  THR B HG1  1 
ATOM   4918  H HG21 . THR B 1 44  ? 5.964   41.650  29.320  1.00 102.62 ? 44  THR B HG21 1 
ATOM   4919  H HG22 . THR B 1 44  ? 7.528   41.446  29.252  1.00 102.62 ? 44  THR B HG22 1 
ATOM   4920  H HG23 . THR B 1 44  ? 6.648   41.236  27.958  1.00 102.62 ? 44  THR B HG23 1 
ATOM   4921  N N    . ASN B 1 45  ? 7.534   36.771  27.804  1.00 81.45  ? 45  ASN B N    1 
ATOM   4922  C CA   . ASN B 1 45  ? 7.440   35.337  27.626  1.00 79.75  ? 45  ASN B CA   1 
ATOM   4923  C C    . ASN B 1 45  ? 8.850   34.823  27.322  1.00 76.95  ? 45  ASN B C    1 
ATOM   4924  O O    . ASN B 1 45  ? 9.847   35.513  27.595  1.00 77.78  ? 45  ASN B O    1 
ATOM   4925  C CB   . ASN B 1 45  ? 6.424   35.039  26.523  1.00 79.63  ? 45  ASN B CB   1 
ATOM   4926  C CG   . ASN B 1 45  ? 6.002   33.587  26.497  1.00 81.98  ? 45  ASN B CG   1 
ATOM   4927  O OD1  . ASN B 1 45  ? 6.712   32.737  25.958  1.00 82.09  ? 45  ASN B OD1  1 
ATOM   4928  N ND2  . ASN B 1 45  ? 4.848   33.291  27.087  1.00 82.90  ? 45  ASN B ND2  1 
ATOM   4929  H H    . ASN B 1 45  ? 7.643   37.191  27.061  1.00 97.75  ? 45  ASN B H    1 
ATOM   4930  H HA   . ASN B 1 45  ? 7.112   34.911  28.434  1.00 95.70  ? 45  ASN B HA   1 
ATOM   4931  H HB2  . ASN B 1 45  ? 5.631   35.580  26.669  1.00 95.55  ? 45  ASN B HB2  1 
ATOM   4932  H HB3  . ASN B 1 45  ? 6.818   35.254  25.663  1.00 95.55  ? 45  ASN B HB3  1 
ATOM   4933  H HD21 . ASN B 1 45  ? 4.383   33.912  27.458  1.00 99.48  ? 45  ASN B HD21 1 
ATOM   4934  H HD22 . ASN B 1 45  ? 4.566   32.479  27.097  1.00 99.48  ? 45  ASN B HD22 1 
ATOM   4935  N N    . LEU B 1 46  ? 8.941   33.615  26.767  1.00 78.93  ? 46  LEU B N    1 
ATOM   4936  C CA   . LEU B 1 46  ? 10.165  33.230  26.079  1.00 75.04  ? 46  LEU B CA   1 
ATOM   4937  C C    . LEU B 1 46  ? 10.464  34.296  25.036  1.00 82.18  ? 46  LEU B C    1 
ATOM   4938  O O    . LEU B 1 46  ? 9.560   34.974  24.539  1.00 84.09  ? 46  LEU B O    1 
ATOM   4939  C CB   . LEU B 1 46  ? 10.019  31.854  25.436  1.00 76.67  ? 46  LEU B CB   1 
ATOM   4940  C CG   . LEU B 1 46  ? 11.274  30.979  25.440  1.00 78.08  ? 46  LEU B CG   1 
ATOM   4941  C CD1  . LEU B 1 46  ? 11.660  30.586  26.862  1.00 76.06  ? 46  LEU B CD1  1 
ATOM   4942  C CD2  . LEU B 1 46  ? 11.085  29.727  24.591  1.00 75.24  ? 46  LEU B CD2  1 
ATOM   4943  H H    . LEU B 1 46  ? 8.324   33.016  26.777  1.00 94.71  ? 46  LEU B H    1 
ATOM   4944  H HA   . LEU B 1 46  ? 10.909  33.160  26.697  1.00 90.05  ? 46  LEU B HA   1 
ATOM   4945  H HB2  . LEU B 1 46  ? 9.328   31.369  25.914  1.00 92.00  ? 46  LEU B HB2  1 
ATOM   4946  H HB3  . LEU B 1 46  ? 9.757   31.979  24.511  1.00 92.00  ? 46  LEU B HB3  1 
ATOM   4947  H HG   . LEU B 1 46  ? 11.998  31.497  25.054  1.00 93.69  ? 46  LEU B HG   1 
ATOM   4948  H HD11 . LEU B 1 46  ? 12.201  29.782  26.832  1.00 91.28  ? 46  LEU B HD11 1 
ATOM   4949  H HD12 . LEU B 1 46  ? 12.166  31.310  27.264  1.00 91.28  ? 46  LEU B HD12 1 
ATOM   4950  H HD13 . LEU B 1 46  ? 10.852  30.423  27.375  1.00 91.28  ? 46  LEU B HD13 1 
ATOM   4951  H HD21 . LEU B 1 46  ? 11.953  29.409  24.299  1.00 90.29  ? 46  LEU B HD21 1 
ATOM   4952  H HD22 . LEU B 1 46  ? 10.646  29.047  25.125  1.00 90.29  ? 46  LEU B HD22 1 
ATOM   4953  H HD23 . LEU B 1 46  ? 10.538  29.948  23.821  1.00 90.29  ? 46  LEU B HD23 1 
ATOM   4954  N N    . TYR B 1 47  ? 11.735  34.485  24.722  1.00 84.42  ? 47  TYR B N    1 
ATOM   4955  C CA   . TYR B 1 47  ? 12.142  35.551  23.818  1.00 82.42  ? 47  TYR B CA   1 
ATOM   4956  C C    . TYR B 1 47  ? 12.598  34.961  22.494  1.00 79.56  ? 47  TYR B C    1 
ATOM   4957  O O    . TYR B 1 47  ? 13.198  33.883  22.465  1.00 76.26  ? 47  TYR B O    1 
ATOM   4958  C CB   . TYR B 1 47  ? 13.254  36.391  24.445  1.00 82.62  ? 47  TYR B CB   1 
ATOM   4959  C CG   . TYR B 1 47  ? 13.650  37.553  23.587  1.00 83.75  ? 47  TYR B CG   1 
ATOM   4960  C CD1  . TYR B 1 47  ? 12.842  38.675  23.493  1.00 83.96  ? 47  TYR B CD1  1 
ATOM   4961  C CD2  . TYR B 1 47  ? 14.821  37.519  22.850  1.00 88.81  ? 47  TYR B CD2  1 
ATOM   4962  C CE1  . TYR B 1 47  ? 13.198  39.739  22.690  1.00 88.81  ? 47  TYR B CE1  1 
ATOM   4963  C CE2  . TYR B 1 47  ? 15.187  38.575  22.041  1.00 92.51  ? 47  TYR B CE2  1 
ATOM   4964  C CZ   . TYR B 1 47  ? 14.374  39.682  21.965  1.00 93.59  ? 47  TYR B CZ   1 
ATOM   4965  O OH   . TYR B 1 47  ? 14.747  40.733  21.159  1.00 100.23 ? 47  TYR B OH   1 
ATOM   4966  H H    . TYR B 1 47  ? 12.384  34.006  25.021  1.00 101.31 ? 47  TYR B H    1 
ATOM   4967  H HA   . TYR B 1 47  ? 11.390  36.135  23.634  1.00 98.91  ? 47  TYR B HA   1 
ATOM   4968  H HB2  . TYR B 1 47  ? 12.946  36.737  25.298  1.00 99.15  ? 47  TYR B HB2  1 
ATOM   4969  H HB3  . TYR B 1 47  ? 14.036  35.833  24.576  1.00 99.15  ? 47  TYR B HB3  1 
ATOM   4970  H HD1  . TYR B 1 47  ? 12.049  38.712  23.977  1.00 100.76 ? 47  TYR B HD1  1 
ATOM   4971  H HD2  . TYR B 1 47  ? 15.371  36.771  22.901  1.00 106.57 ? 47  TYR B HD2  1 
ATOM   4972  H HE1  . TYR B 1 47  ? 12.650  40.488  22.636  1.00 106.56 ? 47  TYR B HE1  1 
ATOM   4973  H HE2  . TYR B 1 47  ? 15.977  38.539  21.552  1.00 111.01 ? 47  TYR B HE2  1 
ATOM   4974  H HH   . TYR B 1 47  ? 15.472  40.556  20.774  1.00 120.28 ? 47  TYR B HH   1 
ATOM   4975  N N    . ALA B 1 48  ? 12.294  35.666  21.396  1.00 83.32  ? 48  ALA B N    1 
ATOM   4976  C CA   . ALA B 1 48  ? 12.700  35.221  20.070  1.00 81.41  ? 48  ALA B CA   1 
ATOM   4977  C C    . ALA B 1 48  ? 12.351  36.218  18.969  1.00 80.44  ? 48  ALA B C    1 
ATOM   4978  O O    . ALA B 1 48  ? 11.362  36.952  19.071  1.00 78.22  ? 48  ALA B O    1 
ATOM   4979  C CB   . ALA B 1 48  ? 12.046  33.870  19.743  1.00 78.07  ? 48  ALA B CB   1 
ATOM   4980  H H    . ALA B 1 48  ? 11.853  36.404  21.400  1.00 99.98  ? 48  ALA B H    1 
ATOM   4981  H HA   . ALA B 1 48  ? 13.665  35.131  20.082  1.00 97.69  ? 48  ALA B HA   1 
ATOM   4982  H HB1  . ALA B 1 48  ? 12.277  33.620  18.834  1.00 93.69  ? 48  ALA B HB1  1 
ATOM   4983  H HB2  . ALA B 1 48  ? 12.375  33.202  20.364  1.00 93.69  ? 48  ALA B HB2  1 
ATOM   4984  H HB3  . ALA B 1 48  ? 11.084  33.956  19.828  1.00 93.69  ? 48  ALA B HB3  1 
ATOM   4985  N N    . GLU B 1 49  ? 13.153  36.238  17.903  1.00 79.24  ? 49  GLU B N    1 
ATOM   4986  C CA   . GLU B 1 49  ? 12.843  37.024  16.718  1.00 81.92  ? 49  GLU B CA   1 
ATOM   4987  C C    . GLU B 1 49  ? 12.049  36.241  15.679  1.00 79.78  ? 49  GLU B C    1 
ATOM   4988  O O    . GLU B 1 49  ? 11.578  36.839  14.707  1.00 80.90  ? 49  GLU B O    1 
ATOM   4989  C CB   . GLU B 1 49  ? 14.132  37.549  16.070  1.00 78.80  ? 49  GLU B CB   1 
ATOM   4990  C CG   . GLU B 1 49  ? 15.189  38.024  17.063  1.00 84.28  ? 49  GLU B CG   1 
ATOM   4991  C CD   . GLU B 1 49  ? 16.390  38.666  16.379  1.00 86.92  ? 49  GLU B CD   1 
ATOM   4992  O OE1  . GLU B 1 49  ? 17.094  37.964  15.628  1.00 83.29  ? 49  GLU B OE1  1 
ATOM   4993  O OE2  . GLU B 1 49  ? 16.629  39.875  16.587  1.00 87.38  ? 49  GLU B OE2  1 
ATOM   4994  H H    . GLU B 1 49  ? 13.889  35.798  17.846  1.00 95.09  ? 49  GLU B H    1 
ATOM   4995  H HA   . GLU B 1 49  ? 12.315  37.791  16.989  1.00 98.30  ? 49  GLU B HA   1 
ATOM   4996  H HB2  . GLU B 1 49  ? 14.525  36.837  15.542  1.00 94.56  ? 49  GLU B HB2  1 
ATOM   4997  H HB3  . GLU B 1 49  ? 13.908  38.300  15.499  1.00 94.56  ? 49  GLU B HB3  1 
ATOM   4998  H HG2  . GLU B 1 49  ? 14.794  38.682  17.656  1.00 101.14 ? 49  GLU B HG2  1 
ATOM   4999  H HG3  . GLU B 1 49  ? 15.506  37.264  17.576  1.00 101.14 ? 49  GLU B HG3  1 
ATOM   5000  N N    . GLN B 1 50  ? 11.868  34.933  15.870  1.00 85.65  ? 50  GLN B N    1 
ATOM   5001  C CA   . GLN B 1 50  ? 11.202  34.093  14.883  1.00 83.46  ? 50  GLN B CA   1 
ATOM   5002  C C    . GLN B 1 50  ? 10.483  32.951  15.586  1.00 78.83  ? 50  GLN B C    1 
ATOM   5003  O O    . GLN B 1 50  ? 10.834  32.570  16.705  1.00 77.18  ? 50  GLN B O    1 
ATOM   5004  C CB   . GLN B 1 50  ? 12.200  33.516  13.872  1.00 80.44  ? 50  GLN B CB   1 
ATOM   5005  C CG   . GLN B 1 50  ? 12.086  34.061  12.476  1.00 81.76  ? 50  GLN B CG   1 
ATOM   5006  C CD   . GLN B 1 50  ? 13.404  33.980  11.734  1.00 85.03  ? 50  GLN B CD   1 
ATOM   5007  O OE1  . GLN B 1 50  ? 14.222  33.096  11.992  1.00 83.51  ? 50  GLN B OE1  1 
ATOM   5008  N NE2  . GLN B 1 50  ? 13.620  34.909  10.808  1.00 90.38  ? 50  GLN B NE2  1 
ATOM   5009  H H    . GLN B 1 50  ? 12.125  34.507  16.572  1.00 102.78 ? 50  GLN B H    1 
ATOM   5010  H HA   . GLN B 1 50  ? 10.545  34.631  14.415  1.00 100.15 ? 50  GLN B HA   1 
ATOM   5011  H HB2  . GLN B 1 50  ? 13.098  33.706  14.186  1.00 96.53  ? 50  GLN B HB2  1 
ATOM   5012  H HB3  . GLN B 1 50  ? 12.063  32.557  13.821  1.00 96.53  ? 50  GLN B HB3  1 
ATOM   5013  H HG2  . GLN B 1 50  ? 11.427  33.547  11.984  1.00 98.11  ? 50  GLN B HG2  1 
ATOM   5014  H HG3  . GLN B 1 50  ? 11.817  34.992  12.517  1.00 98.11  ? 50  GLN B HG3  1 
ATOM   5015  H HE21 . GLN B 1 50  ? 13.027  35.513  10.658  1.00 108.46 ? 50  GLN B HE21 1 
ATOM   5016  H HE22 . GLN B 1 50  ? 14.354  34.906  10.359  1.00 108.46 ? 50  GLN B HE22 1 
ATOM   5017  N N    . VAL B 1 51  ? 9.480   32.397  14.905  1.00 80.04  ? 51  VAL B N    1 
ATOM   5018  C CA   . VAL B 1 51  ? 8.713   31.266  15.422  1.00 77.55  ? 51  VAL B CA   1 
ATOM   5019  C C    . VAL B 1 51  ? 8.314   30.378  14.250  1.00 78.88  ? 51  VAL B C    1 
ATOM   5020  O O    . VAL B 1 51  ? 7.799   30.865  13.237  1.00 80.09  ? 51  VAL B O    1 
ATOM   5021  C CB   . VAL B 1 51  ? 7.464   31.726  16.199  1.00 79.94  ? 51  VAL B CB   1 
ATOM   5022  C CG1  . VAL B 1 51  ? 6.698   30.520  16.731  1.00 79.39  ? 51  VAL B CG1  1 
ATOM   5023  C CG2  . VAL B 1 51  ? 7.844   32.661  17.341  1.00 80.29  ? 51  VAL B CG2  1 
ATOM   5024  H H    . VAL B 1 51  ? 9.222   32.663  14.130  1.00 96.05  ? 51  VAL B H    1 
ATOM   5025  H HA   . VAL B 1 51  ? 9.275   30.751  16.021  1.00 93.06  ? 51  VAL B HA   1 
ATOM   5026  H HB   . VAL B 1 51  ? 6.885   32.216  15.594  1.00 95.93  ? 51  VAL B HB   1 
ATOM   5027  H HG11 . VAL B 1 51  ? 6.017   30.826  17.350  1.00 95.27  ? 51  VAL B HG11 1 
ATOM   5028  H HG12 . VAL B 1 51  ? 6.284   30.055  15.987  1.00 95.27  ? 51  VAL B HG12 1 
ATOM   5029  H HG13 . VAL B 1 51  ? 7.318   29.928  17.187  1.00 95.27  ? 51  VAL B HG13 1 
ATOM   5030  H HG21 . VAL B 1 51  ? 7.063   32.821  17.892  1.00 96.35  ? 51  VAL B HG21 1 
ATOM   5031  H HG22 . VAL B 1 51  ? 8.543   32.245  17.870  1.00 96.35  ? 51  VAL B HG22 1 
ATOM   5032  H HG23 . VAL B 1 51  ? 8.165   33.498  16.970  1.00 96.35  ? 51  VAL B HG23 1 
ATOM   5033  N N    . GLY B 1 52  ? 8.548   29.075  14.395  1.00 76.42  ? 52  GLY B N    1 
ATOM   5034  C CA   . GLY B 1 52  ? 8.175   28.121  13.368  1.00 77.79  ? 52  GLY B CA   1 
ATOM   5035  C C    . GLY B 1 52  ? 7.512   26.904  13.980  1.00 75.16  ? 52  GLY B C    1 
ATOM   5036  O O    . GLY B 1 52  ? 7.676   26.610  15.166  1.00 78.00  ? 52  GLY B O    1 
ATOM   5037  H H    . GLY B 1 52  ? 8.923   28.721  15.083  1.00 91.70  ? 52  GLY B H    1 
ATOM   5038  H HA2  . GLY B 1 52  ? 7.556   28.535  12.747  1.00 93.35  ? 52  GLY B HA2  1 
ATOM   5039  H HA3  . GLY B 1 52  ? 8.966   27.836  12.884  1.00 93.35  ? 52  GLY B HA3  1 
ATOM   5040  N N    . PHE B 1 53  ? 6.759   26.196  13.141  1.00 76.45  ? 53  PHE B N    1 
ATOM   5041  C CA   . PHE B 1 53  ? 5.987   25.029  13.554  1.00 75.24  ? 53  PHE B CA   1 
ATOM   5042  C C    . PHE B 1 53  ? 6.348   23.872  12.635  1.00 77.39  ? 53  PHE B C    1 
ATOM   5043  O O    . PHE B 1 53  ? 6.114   23.938  11.425  1.00 80.78  ? 53  PHE B O    1 
ATOM   5044  C CB   . PHE B 1 53  ? 4.485   25.328  13.522  1.00 76.72  ? 53  PHE B CB   1 
ATOM   5045  C CG   . PHE B 1 53  ? 4.079   26.451  14.442  1.00 77.51  ? 53  PHE B CG   1 
ATOM   5046  C CD1  . PHE B 1 53  ? 4.381   27.766  14.125  1.00 77.89  ? 53  PHE B CD1  1 
ATOM   5047  C CD2  . PHE B 1 53  ? 3.414   26.193  15.632  1.00 81.66  ? 53  PHE B CD2  1 
ATOM   5048  C CE1  . PHE B 1 53  ? 4.021   28.800  14.972  1.00 81.97  ? 53  PHE B CE1  1 
ATOM   5049  C CE2  . PHE B 1 53  ? 3.053   27.227  16.483  1.00 81.59  ? 53  PHE B CE2  1 
ATOM   5050  C CZ   . PHE B 1 53  ? 3.355   28.530  16.151  1.00 81.75  ? 53  PHE B CZ   1 
ATOM   5051  H H    . PHE B 1 53  ? 6.678   26.378  12.305  1.00 91.75  ? 53  PHE B H    1 
ATOM   5052  H HA   . PHE B 1 53  ? 6.218   24.773  14.461  1.00 90.29  ? 53  PHE B HA   1 
ATOM   5053  H HB2  . PHE B 1 53  ? 4.235   25.578  12.619  1.00 92.07  ? 53  PHE B HB2  1 
ATOM   5054  H HB3  . PHE B 1 53  ? 4.001   24.532  13.793  1.00 92.07  ? 53  PHE B HB3  1 
ATOM   5055  H HD1  . PHE B 1 53  ? 4.831   27.955  13.333  1.00 93.47  ? 53  PHE B HD1  1 
ATOM   5056  H HD2  . PHE B 1 53  ? 3.207   25.315  15.861  1.00 97.99  ? 53  PHE B HD2  1 
ATOM   5057  H HE1  . PHE B 1 53  ? 4.229   29.678  14.747  1.00 98.37  ? 53  PHE B HE1  1 
ATOM   5058  H HE2  . PHE B 1 53  ? 2.607   27.040  17.278  1.00 97.91  ? 53  PHE B HE2  1 
ATOM   5059  H HZ   . PHE B 1 53  ? 3.110   29.225  16.719  1.00 98.10  ? 53  PHE B HZ   1 
ATOM   5060  N N    . ILE B 1 54  ? 6.914   22.818  13.213  1.00 77.99  ? 54  ILE B N    1 
ATOM   5061  C CA   . ILE B 1 54  ? 7.585   21.766  12.464  1.00 79.40  ? 54  ILE B CA   1 
ATOM   5062  C C    . ILE B 1 54  ? 6.730   20.509  12.457  1.00 80.34  ? 54  ILE B C    1 
ATOM   5063  O O    . ILE B 1 54  ? 6.068   20.183  13.449  1.00 81.83  ? 54  ILE B O    1 
ATOM   5064  C CB   . ILE B 1 54  ? 8.979   21.477  13.055  1.00 78.85  ? 54  ILE B CB   1 
ATOM   5065  C CG1  . ILE B 1 54  ? 8.884   21.169  14.550  1.00 78.29  ? 54  ILE B CG1  1 
ATOM   5066  C CG2  . ILE B 1 54  ? 9.908   22.668  12.844  1.00 77.48  ? 54  ILE B CG2  1 
ATOM   5067  C CD1  . ILE B 1 54  ? 10.179  20.648  15.159  1.00 75.67  ? 54  ILE B CD1  1 
ATOM   5068  H H    . ILE B 1 54  ? 6.921   22.687  14.063  1.00 93.58  ? 54  ILE B H    1 
ATOM   5069  H HA   . ILE B 1 54  ? 7.684   22.054  11.543  1.00 95.28  ? 54  ILE B HA   1 
ATOM   5070  H HB   . ILE B 1 54  ? 9.337   20.702  12.595  1.00 94.61  ? 54  ILE B HB   1 
ATOM   5071  H HG12 . ILE B 1 54  ? 8.643   21.983  15.020  1.00 93.95  ? 54  ILE B HG12 1 
ATOM   5072  H HG13 . ILE B 1 54  ? 8.201   20.494  14.686  1.00 93.95  ? 54  ILE B HG13 1 
ATOM   5073  H HG21 . ILE B 1 54  ? 10.804  22.424  13.124  1.00 92.98  ? 54  ILE B HG21 1 
ATOM   5074  H HG22 . ILE B 1 54  ? 9.909   22.905  11.903  1.00 92.98  ? 54  ILE B HG22 1 
ATOM   5075  H HG23 . ILE B 1 54  ? 9.588   23.416  13.372  1.00 92.98  ? 54  ILE B HG23 1 
ATOM   5076  H HD11 . ILE B 1 54  ? 10.015  20.393  16.080  1.00 90.80  ? 54  ILE B HD11 1 
ATOM   5077  H HD12 . ILE B 1 54  ? 10.479  19.878  14.651  1.00 90.80  ? 54  ILE B HD12 1 
ATOM   5078  H HD13 . ILE B 1 54  ? 10.849  21.349  15.124  1.00 90.80  ? 54  ILE B HD13 1 
ATOM   5079  N N    . LYS B 1 55  ? 6.740   19.807  11.326  1.00 82.29  ? 55  LYS B N    1 
ATOM   5080  C CA   . LYS B 1 55  ? 6.083   18.512  11.199  1.00 84.29  ? 55  LYS B CA   1 
ATOM   5081  C C    . LYS B 1 55  ? 6.869   17.700  10.181  1.00 83.80  ? 55  LYS B C    1 
ATOM   5082  O O    . LYS B 1 55  ? 7.083   18.159  9.055   1.00 85.00  ? 55  LYS B O    1 
ATOM   5083  C CB   . LYS B 1 55  ? 4.620   18.656  10.766  1.00 85.77  ? 55  LYS B CB   1 
ATOM   5084  C CG   . LYS B 1 55  ? 3.929   17.323  10.494  1.00 86.79  ? 55  LYS B CG   1 
ATOM   5085  C CD   . LYS B 1 55  ? 2.634   17.179  11.288  1.00 93.73  ? 55  LYS B CD   1 
ATOM   5086  C CE   . LYS B 1 55  ? 1.416   17.521  10.434  1.00 98.10  ? 55  LYS B CE   1 
ATOM   5087  N NZ   . LYS B 1 55  ? 0.174   17.642  11.255  1.00 103.13 ? 55  LYS B NZ   1 
ATOM   5088  H H    . LYS B 1 55  ? 7.129   20.066  10.604  1.00 98.75  ? 55  LYS B H    1 
ATOM   5089  H HA   . LYS B 1 55  ? 6.087   18.050  12.052  1.00 101.15 ? 55  LYS B HA   1 
ATOM   5090  H HB2  . LYS B 1 55  ? 4.129   19.106  11.471  1.00 102.92 ? 55  LYS B HB2  1 
ATOM   5091  H HB3  . LYS B 1 55  ? 4.586   19.180  9.951   1.00 102.92 ? 55  LYS B HB3  1 
ATOM   5092  H HG2  . LYS B 1 55  ? 3.715   17.262  9.550   1.00 104.15 ? 55  LYS B HG2  1 
ATOM   5093  H HG3  . LYS B 1 55  ? 4.522   16.598  10.747  1.00 104.15 ? 55  LYS B HG3  1 
ATOM   5094  H HD2  . LYS B 1 55  ? 2.545   16.263  11.595  1.00 112.48 ? 55  LYS B HD2  1 
ATOM   5095  H HD3  . LYS B 1 55  ? 2.653   17.783  12.048  1.00 112.48 ? 55  LYS B HD3  1 
ATOM   5096  H HE2  . LYS B 1 55  ? 1.567   18.368  9.986   1.00 117.73 ? 55  LYS B HE2  1 
ATOM   5097  H HE3  . LYS B 1 55  ? 1.279   16.819  9.779   1.00 117.73 ? 55  LYS B HE3  1 
ATOM   5098  H HZ1  . LYS B 1 55  ? -0.518  17.841  10.733  1.00 123.75 ? 55  LYS B HZ1  1 
ATOM   5099  H HZ2  . LYS B 1 55  ? 0.009   16.873  11.673  1.00 123.75 ? 55  LYS B HZ2  1 
ATOM   5100  H HZ3  . LYS B 1 55  ? 0.273   18.285  11.863  1.00 123.75 ? 55  LYS B HZ3  1 
ATOM   5101  N N    . ASP B 1 56  ? 7.298   16.503  10.580  1.00 83.35  ? 56  ASP B N    1 
ATOM   5102  C CA   . ASP B 1 56  ? 8.132   15.629  9.743   1.00 86.52  ? 56  ASP B CA   1 
ATOM   5103  C C    . ASP B 1 56  ? 9.335   16.453  9.282   1.00 83.47  ? 56  ASP B C    1 
ATOM   5104  O O    . ASP B 1 56  ? 10.005  17.070  10.122  1.00 82.84  ? 56  ASP B O    1 
ATOM   5105  C CB   . ASP B 1 56  ? 7.285   15.032  8.626   1.00 86.03  ? 56  ASP B CB   1 
ATOM   5106  C CG   . ASP B 1 56  ? 6.032   14.341  9.138   1.00 90.23  ? 56  ASP B CG   1 
ATOM   5107  O OD1  . ASP B 1 56  ? 6.054   13.803  10.267  1.00 90.36  ? 56  ASP B OD1  1 
ATOM   5108  O OD2  . ASP B 1 56  ? 5.022   14.331  8.399   1.00 95.58  ? 56  ASP B OD2  1 
ATOM   5109  H H    . ASP B 1 56  ? 7.116   16.164  11.349  1.00 100.03 ? 56  ASP B H    1 
ATOM   5110  H HA   . ASP B 1 56  ? 8.468   14.900  10.288  1.00 103.83 ? 56  ASP B HA   1 
ATOM   5111  H HB2  . ASP B 1 56  ? 7.010   15.742  8.024   1.00 103.24 ? 56  ASP B HB2  1 
ATOM   5112  H HB3  . ASP B 1 56  ? 7.813   14.376  8.145   1.00 103.24 ? 56  ASP B HB3  1 
ATOM   5113  N N    . SER B 1 57  ? 9.642   16.495  7.990   1.00 87.30  ? 57  SER B N    1 
ATOM   5114  C CA   . SER B 1 57  ? 10.745  17.284  7.462   1.00 83.57  ? 57  SER B CA   1 
ATOM   5115  C C    . SER B 1 57  ? 10.325  18.700  7.077   1.00 82.65  ? 57  SER B C    1 
ATOM   5116  O O    . SER B 1 57  ? 11.124  19.430  6.479   1.00 85.45  ? 57  SER B O    1 
ATOM   5117  C CB   . SER B 1 57  ? 11.352  16.579  6.243   1.00 82.15  ? 57  SER B CB   1 
ATOM   5118  O OG   . SER B 1 57  ? 12.206  15.515  6.633   1.00 81.72  ? 57  SER B OG   1 
ATOM   5119  H H    . SER B 1 57  ? 9.212   16.063  7.383   1.00 104.76 ? 57  SER B H    1 
ATOM   5120  H HA   . SER B 1 57  ? 11.430  17.353  8.145   1.00 100.28 ? 57  SER B HA   1 
ATOM   5121  H HB2  . SER B 1 57  ? 10.633  16.221  5.699   1.00 98.57  ? 57  SER B HB2  1 
ATOM   5122  H HB3  . SER B 1 57  ? 11.866  17.223  5.732   1.00 98.57  ? 57  SER B HB3  1 
ATOM   5123  H HG   . SER B 1 57  ? 12.542  15.152  5.954   1.00 98.06  ? 57  SER B HG   1 
ATOM   5124  N N    . HIS B 1 58  ? 9.100   19.103  7.401   1.00 83.27  ? 58  HIS B N    1 
ATOM   5125  C CA   . HIS B 1 58  ? 8.568   20.395  6.995   1.00 83.67  ? 58  HIS B CA   1 
ATOM   5126  C C    . HIS B 1 58  ? 8.716   21.419  8.115   1.00 82.64  ? 58  HIS B C    1 
ATOM   5127  O O    . HIS B 1 58  ? 8.775   21.073  9.294   1.00 79.81  ? 58  HIS B O    1 
ATOM   5128  C CB   . HIS B 1 58  ? 7.095   20.268  6.598   1.00 81.20  ? 58  HIS B CB   1 
ATOM   5129  C CG   . HIS B 1 58  ? 6.468   21.562  6.188   1.00 81.78  ? 58  HIS B CG   1 
ATOM   5130  N ND1  . HIS B 1 58  ? 6.796   22.203  5.013   1.00 80.86  ? 58  HIS B ND1  1 
ATOM   5131  C CD2  . HIS B 1 58  ? 5.540   22.338  6.796   1.00 81.28  ? 58  HIS B CD2  1 
ATOM   5132  C CE1  . HIS B 1 58  ? 6.093   23.316  4.911   1.00 80.93  ? 58  HIS B CE1  1 
ATOM   5133  N NE2  . HIS B 1 58  ? 5.326   23.423  5.982   1.00 83.03  ? 58  HIS B NE2  1 
ATOM   5134  H H    . HIS B 1 58  ? 8.549   18.634  7.866   1.00 99.93  ? 58  HIS B H    1 
ATOM   5135  H HA   . HIS B 1 58  ? 9.067   20.720  6.230   1.00 100.40 ? 58  HIS B HA   1 
ATOM   5136  H HB2  . HIS B 1 58  ? 7.026   19.655  5.849   1.00 97.44  ? 58  HIS B HB2  1 
ATOM   5137  H HB3  . HIS B 1 58  ? 6.596   19.924  7.355   1.00 97.44  ? 58  HIS B HB3  1 
ATOM   5138  H HD1  . HIS B 1 58  ? 7.369   21.923  4.436   1.00 97.03  ? 58  HIS B HD1  1 
ATOM   5139  H HD2  . HIS B 1 58  ? 5.126   22.168  7.612   1.00 97.54  ? 58  HIS B HD2  1 
ATOM   5140  H HE1  . HIS B 1 58  ? 6.130   23.921  4.206   1.00 97.11  ? 58  HIS B HE1  1 
ATOM   5141  H HE2  . HIS B 1 58  ? 4.781   24.069  6.144   1.00 99.63  ? 58  HIS B HE2  1 
ATOM   5142  N N    . LEU B 1 59  ? 8.790   22.690  7.724   1.00 82.65  ? 59  LEU B N    1 
ATOM   5143  C CA   . LEU B 1 59  ? 8.850   23.817  8.650   1.00 79.98  ? 59  LEU B CA   1 
ATOM   5144  C C    . LEU B 1 59  ? 7.820   24.840  8.197   1.00 78.23  ? 59  LEU B C    1 
ATOM   5145  O O    . LEU B 1 59  ? 7.864   25.298  7.049   1.00 81.27  ? 59  LEU B O    1 
ATOM   5146  C CB   . LEU B 1 59  ? 10.250  24.437  8.687   1.00 77.53  ? 59  LEU B CB   1 
ATOM   5147  C CG   . LEU B 1 59  ? 10.364  25.844  9.270   1.00 75.65  ? 59  LEU B CG   1 
ATOM   5148  C CD1  . LEU B 1 59  ? 9.833   25.894  10.699  1.00 73.94  ? 59  LEU B CD1  1 
ATOM   5149  C CD2  . LEU B 1 59  ? 11.807  26.337  9.226   1.00 72.47  ? 59  LEU B CD2  1 
ATOM   5150  H H    . LEU B 1 59  ? 8.807   22.932  6.899   1.00 99.18  ? 59  LEU B H    1 
ATOM   5151  H HA   . LEU B 1 59  ? 8.633   23.522  9.548   1.00 95.98  ? 59  LEU B HA   1 
ATOM   5152  H HB2  . LEU B 1 59  ? 10.818  23.861  9.223   1.00 93.03  ? 59  LEU B HB2  1 
ATOM   5153  H HB3  . LEU B 1 59  ? 10.583  24.478  7.777   1.00 93.03  ? 59  LEU B HB3  1 
ATOM   5154  H HG   . LEU B 1 59  ? 9.823   26.440  8.728   1.00 90.78  ? 59  LEU B HG   1 
ATOM   5155  H HD11 . LEU B 1 59  ? 9.977   26.784  11.059  1.00 88.73  ? 59  LEU B HD11 1 
ATOM   5156  H HD12 . LEU B 1 59  ? 8.884   25.691  10.691  1.00 88.73  ? 59  LEU B HD12 1 
ATOM   5157  H HD13 . LEU B 1 59  ? 10.307  25.240  11.236  1.00 88.73  ? 59  LEU B HD13 1 
ATOM   5158  H HD21 . LEU B 1 59  ? 11.847  27.232  9.598   1.00 86.97  ? 59  LEU B HD21 1 
ATOM   5159  H HD22 . LEU B 1 59  ? 12.362  25.737  9.750   1.00 86.97  ? 59  LEU B HD22 1 
ATOM   5160  H HD23 . LEU B 1 59  ? 12.110  26.347  8.305   1.00 86.97  ? 59  LEU B HD23 1 
ATOM   5161  N N    . GLN B 1 60  ? 6.890   25.186  9.082   1.00 77.53  ? 60  GLN B N    1 
ATOM   5162  C CA   . GLN B 1 60  ? 5.815   26.133  8.771   1.00 75.54  ? 60  GLN B CA   1 
ATOM   5163  C C    . GLN B 1 60  ? 6.040   27.377  9.623   1.00 77.74  ? 60  GLN B C    1 
ATOM   5164  O O    . GLN B 1 60  ? 5.778   27.376  10.829  1.00 76.54  ? 60  GLN B O    1 
ATOM   5165  C CB   . GLN B 1 60  ? 4.444   25.521  9.025   1.00 78.18  ? 60  GLN B CB   1 
ATOM   5166  C CG   . GLN B 1 60  ? 3.273   26.360  8.502   1.00 75.63  ? 60  GLN B CG   1 
ATOM   5167  C CD   . GLN B 1 60  ? 3.319   26.585  6.995   1.00 81.56  ? 60  GLN B CD   1 
ATOM   5168  O OE1  . GLN B 1 60  ? 3.514   25.647  6.222   1.00 80.24  ? 60  GLN B OE1  1 
ATOM   5169  N NE2  . GLN B 1 60  ? 3.133   27.834  6.576   1.00 76.15  ? 60  GLN B NE2  1 
ATOM   5170  H H    . GLN B 1 60  ? 6.858   24.881  9.886   1.00 93.04  ? 60  GLN B H    1 
ATOM   5171  H HA   . GLN B 1 60  ? 5.864   26.379  7.834   1.00 90.65  ? 60  GLN B HA   1 
ATOM   5172  H HB2  . GLN B 1 60  ? 4.405   24.656  8.588   1.00 93.81  ? 60  GLN B HB2  1 
ATOM   5173  H HB3  . GLN B 1 60  ? 4.325   25.414  9.982   1.00 93.81  ? 60  GLN B HB3  1 
ATOM   5174  H HG2  . GLN B 1 60  ? 2.442   25.904  8.710   1.00 90.76  ? 60  GLN B HG2  1 
ATOM   5175  H HG3  . GLN B 1 60  ? 3.291   27.228  8.933   1.00 90.76  ? 60  GLN B HG3  1 
ATOM   5176  H HE21 . GLN B 1 60  ? 2.995   28.463  7.146   1.00 91.38  ? 60  GLN B HE21 1 
ATOM   5177  H HE22 . GLN B 1 60  ? 3.150   28.012  5.735   1.00 91.38  ? 60  GLN B HE22 1 
ATOM   5178  N N    . MET B 1 61  ? 6.524   28.440  8.987   1.00 75.31  ? 61  MET B N    1 
ATOM   5179  C CA   . MET B 1 61  ? 6.749   29.697  9.687   1.00 76.02  ? 61  MET B CA   1 
ATOM   5180  C C    . MET B 1 61  ? 5.417   30.379  9.980   1.00 78.07  ? 61  MET B C    1 
ATOM   5181  O O    . MET B 1 61  ? 4.437   30.224  9.245   1.00 79.19  ? 61  MET B O    1 
ATOM   5182  C CB   . MET B 1 61  ? 7.646   30.613  8.860   1.00 76.63  ? 61  MET B CB   1 
ATOM   5183  C CG   . MET B 1 61  ? 8.997   30.003  8.505   1.00 75.88  ? 61  MET B CG   1 
ATOM   5184  S SD   . MET B 1 61  ? 10.140  29.772  9.888   1.00 83.40  ? 61  MET B SD   1 
ATOM   5185  C CE   . MET B 1 61  ? 9.791   31.189  10.927  1.00 78.86  ? 61  MET B CE   1 
ATOM   5186  H H    . MET B 1 61  ? 6.730   28.458  8.152   1.00 90.37  ? 61  MET B H    1 
ATOM   5187  H HA   . MET B 1 61  ? 7.205   29.525  10.525  1.00 91.23  ? 61  MET B HA   1 
ATOM   5188  H HB2  . MET B 1 61  ? 7.192   30.827  8.030   1.00 91.95  ? 61  MET B HB2  1 
ATOM   5189  H HB3  . MET B 1 61  ? 7.813   31.424  9.365   1.00 91.95  ? 61  MET B HB3  1 
ATOM   5190  H HG2  . MET B 1 61  ? 8.843   29.131  8.110   1.00 91.06  ? 61  MET B HG2  1 
ATOM   5191  H HG3  . MET B 1 61  ? 9.435   30.585  7.864   1.00 91.06  ? 61  MET B HG3  1 
ATOM   5192  H HE1  . MET B 1 61  ? 10.384  31.171  11.695  1.00 94.64  ? 61  MET B HE1  1 
ATOM   5193  H HE2  . MET B 1 61  ? 9.937   32.000  10.415  1.00 94.64  ? 61  MET B HE2  1 
ATOM   5194  H HE3  . MET B 1 61  ? 8.868   31.145  11.221  1.00 94.64  ? 61  MET B HE3  1 
ATOM   5195  N N    . MET B 1 62  ? 5.393   31.142  11.076  1.00 79.16  ? 62  MET B N    1 
ATOM   5196  C CA   . MET B 1 62  ? 4.146   31.729  11.556  1.00 79.67  ? 62  MET B CA   1 
ATOM   5197  C C    . MET B 1 62  ? 3.380   32.432  10.441  1.00 80.72  ? 62  MET B C    1 
ATOM   5198  O O    . MET B 1 62  ? 2.144   32.382  10.400  1.00 81.97  ? 62  MET B O    1 
ATOM   5199  C CB   . MET B 1 62  ? 4.442   32.714  12.691  1.00 80.83  ? 62  MET B CB   1 
ATOM   5200  C CG   . MET B 1 62  ? 5.149   33.989  12.236  1.00 83.60  ? 62  MET B CG   1 
ATOM   5201  S SD   . MET B 1 62  ? 5.882   34.930  13.591  1.00 89.47  ? 62  MET B SD   1 
ATOM   5202  C CE   . MET B 1 62  ? 7.578   34.359  13.522  1.00 81.29  ? 62  MET B CE   1 
ATOM   5203  H H    . MET B 1 62  ? 6.082   31.332  11.556  1.00 95.00  ? 62  MET B H    1 
ATOM   5204  H HA   . MET B 1 62  ? 3.591   31.015  11.906  1.00 95.60  ? 62  MET B HA   1 
ATOM   5205  H HB2  . MET B 1 62  ? 3.604   32.973  13.104  1.00 96.99  ? 62  MET B HB2  1 
ATOM   5206  H HB3  . MET B 1 62  ? 5.012   32.277  13.342  1.00 96.99  ? 62  MET B HB3  1 
ATOM   5207  H HG2  . MET B 1 62  ? 5.861   33.750  11.621  1.00 100.32 ? 62  MET B HG2  1 
ATOM   5208  H HG3  . MET B 1 62  ? 4.506   34.562  11.791  1.00 100.32 ? 62  MET B HG3  1 
ATOM   5209  H HE1  . MET B 1 62  ? 8.009   34.546  14.371  1.00 97.55  ? 62  MET B HE1  1 
ATOM   5210  H HE2  . MET B 1 62  ? 7.584   33.404  13.352  1.00 97.55  ? 62  MET B HE2  1 
ATOM   5211  H HE3  . MET B 1 62  ? 8.040   34.825  12.807  1.00 97.55  ? 62  MET B HE3  1 
ATOM   5212  N N    . GLY B 1 63  ? 4.095   33.087  9.527   1.00 79.88  ? 63  GLY B N    1 
ATOM   5213  C CA   . GLY B 1 63  ? 3.447   33.856  8.484   1.00 81.44  ? 63  GLY B CA   1 
ATOM   5214  C C    . GLY B 1 63  ? 3.596   33.277  7.094   1.00 77.55  ? 63  GLY B C    1 
ATOM   5215  O O    . GLY B 1 63  ? 3.399   33.981  6.099   1.00 79.93  ? 63  GLY B O    1 
ATOM   5216  H H    . GLY B 1 63  ? 4.954   33.099  9.494   1.00 95.85  ? 63  GLY B H    1 
ATOM   5217  H HA2  . GLY B 1 63  ? 2.500   33.915  8.681   1.00 97.73  ? 63  GLY B HA2  1 
ATOM   5218  H HA3  . GLY B 1 63  ? 3.824   34.750  8.475   1.00 97.73  ? 63  GLY B HA3  1 
ATOM   5219  N N    . GLY B 1 64  ? 3.946   31.996  7.010   1.00 79.93  ? 64  GLY B N    1 
ATOM   5220  C CA   . GLY B 1 64  ? 4.112   31.336  5.733   1.00 80.14  ? 64  GLY B CA   1 
ATOM   5221  C C    . GLY B 1 64  ? 5.344   31.726  4.951   1.00 76.95  ? 64  GLY B C    1 
ATOM   5222  O O    . GLY B 1 64  ? 5.546   31.207  3.850   1.00 77.69  ? 64  GLY B O    1 
ATOM   5223  H H    . GLY B 1 64  ? 4.093   31.489  7.689   1.00 95.92  ? 64  GLY B H    1 
ATOM   5224  H HA2  . GLY B 1 64  ? 4.152   30.378  5.885   1.00 96.16  ? 64  GLY B HA2  1 
ATOM   5225  H HA3  . GLY B 1 64  ? 3.339   31.535  5.181   1.00 96.16  ? 64  GLY B HA3  1 
ATOM   5226  N N    . GLU B 1 65  ? 6.177   32.612  5.480   1.00 77.52  ? 65  GLU B N    1 
ATOM   5227  C CA   . GLU B 1 65  ? 7.364   33.052  4.768   1.00 77.18  ? 65  GLU B CA   1 
ATOM   5228  C C    . GLU B 1 65  ? 8.454   31.984  4.820   1.00 77.33  ? 65  GLU B C    1 
ATOM   5229  O O    . GLU B 1 65  ? 8.438   31.081  5.661   1.00 79.65  ? 65  GLU B O    1 
ATOM   5230  C CB   . GLU B 1 65  ? 7.884   34.366  5.363   1.00 79.52  ? 65  GLU B CB   1 
ATOM   5231  C CG   . GLU B 1 65  ? 8.627   34.229  6.698   1.00 82.08  ? 65  GLU B CG   1 
ATOM   5232  C CD   . GLU B 1 65  ? 7.696   34.112  7.905   1.00 83.84  ? 65  GLU B CD   1 
ATOM   5233  O OE1  . GLU B 1 65  ? 6.499   33.802  7.711   1.00 84.49  ? 65  GLU B OE1  1 
ATOM   5234  O OE2  . GLU B 1 65  ? 8.161   34.322  9.050   1.00 82.24  ? 65  GLU B OE2  1 
ATOM   5235  H H    . GLU B 1 65  ? 6.076   32.975  6.253   1.00 93.02  ? 65  GLU B H    1 
ATOM   5236  H HA   . GLU B 1 65  ? 7.143   33.206  3.836   1.00 92.62  ? 65  GLU B HA   1 
ATOM   5237  H HB2  . GLU B 1 65  ? 8.499   34.767  4.729   1.00 95.42  ? 65  GLU B HB2  1 
ATOM   5238  H HB3  . GLU B 1 65  ? 7.128   34.955  5.511   1.00 95.42  ? 65  GLU B HB3  1 
ATOM   5239  H HG2  . GLU B 1 65  ? 9.177   33.431  6.670   1.00 98.49  ? 65  GLU B HG2  1 
ATOM   5240  H HG3  . GLU B 1 65  ? 9.184   35.012  6.828   1.00 98.49  ? 65  GLU B HG3  1 
ATOM   5241  N N    . PHE B 1 66  ? 9.414   32.104  3.907   1.00 77.58  ? 66  PHE B N    1 
ATOM   5242  C CA   . PHE B 1 66  ? 10.632  31.308  3.956   1.00 78.05  ? 66  PHE B CA   1 
ATOM   5243  C C    . PHE B 1 66  ? 11.664  32.031  4.818   1.00 77.72  ? 66  PHE B C    1 
ATOM   5244  O O    . PHE B 1 66  ? 11.749  33.265  4.804   1.00 77.43  ? 66  PHE B O    1 
ATOM   5245  C CB   . PHE B 1 66  ? 11.188  31.068  2.555   1.00 75.89  ? 66  PHE B CB   1 
ATOM   5246  C CG   . PHE B 1 66  ? 12.572  30.480  2.545   1.00 76.40  ? 66  PHE B CG   1 
ATOM   5247  C CD1  . PHE B 1 66  ? 12.783  29.154  2.893   1.00 76.59  ? 66  PHE B CD1  1 
ATOM   5248  C CD2  . PHE B 1 66  ? 13.665  31.254  2.187   1.00 75.20  ? 66  PHE B CD2  1 
ATOM   5249  C CE1  . PHE B 1 66  ? 14.060  28.614  2.887   1.00 76.24  ? 66  PHE B CE1  1 
ATOM   5250  C CE2  . PHE B 1 66  ? 14.943  30.721  2.179   1.00 73.87  ? 66  PHE B CE2  1 
ATOM   5251  C CZ   . PHE B 1 66  ? 15.140  29.399  2.530   1.00 75.82  ? 66  PHE B CZ   1 
ATOM   5252  H H    . PHE B 1 66  ? 9.382   32.648  3.241   1.00 93.10  ? 66  PHE B H    1 
ATOM   5253  H HA   . PHE B 1 66  ? 10.446  30.440  4.345   1.00 93.66  ? 66  PHE B HA   1 
ATOM   5254  H HB2  . PHE B 1 66  ? 10.602  30.453  2.088   1.00 91.06  ? 66  PHE B HB2  1 
ATOM   5255  H HB3  . PHE B 1 66  ? 11.223  31.915  2.084   1.00 91.06  ? 66  PHE B HB3  1 
ATOM   5256  H HD1  . PHE B 1 66  ? 12.060  28.621  3.133   1.00 91.91  ? 66  PHE B HD1  1 
ATOM   5257  H HD2  . PHE B 1 66  ? 13.538  32.145  1.950   1.00 90.25  ? 66  PHE B HD2  1 
ATOM   5258  H HE1  . PHE B 1 66  ? 14.190  27.724  3.124   1.00 91.48  ? 66  PHE B HE1  1 
ATOM   5259  H HE2  . PHE B 1 66  ? 15.668  31.252  1.938   1.00 88.65  ? 66  PHE B HE2  1 
ATOM   5260  H HZ   . PHE B 1 66  ? 15.997  29.038  2.526   1.00 90.99  ? 66  PHE B HZ   1 
ATOM   5261  N N    . SER B 1 67  ? 12.435  31.258  5.584   1.00 76.96  ? 67  SER B N    1 
ATOM   5262  C CA   . SER B 1 67  ? 13.481  31.815  6.437   1.00 76.96  ? 67  SER B CA   1 
ATOM   5263  C C    . SER B 1 67  ? 14.695  30.898  6.383   1.00 72.34  ? 67  SER B C    1 
ATOM   5264  O O    . SER B 1 67  ? 14.655  29.781  6.905   1.00 71.99  ? 67  SER B O    1 
ATOM   5265  C CB   . SER B 1 67  ? 13.000  31.984  7.876   1.00 74.27  ? 67  SER B CB   1 
ATOM   5266  O OG   . SER B 1 67  ? 14.096  32.221  8.739   1.00 76.25  ? 67  SER B OG   1 
ATOM   5267  H H    . SER B 1 67  ? 12.369  30.402  5.626   1.00 92.36  ? 67  SER B H    1 
ATOM   5268  H HA   . SER B 1 67  ? 13.738  32.684  6.090   1.00 92.36  ? 67  SER B HA   1 
ATOM   5269  H HB2  . SER B 1 67  ? 12.392  32.739  7.921   1.00 89.12  ? 67  SER B HB2  1 
ATOM   5270  H HB3  . SER B 1 67  ? 12.545  31.175  8.156   1.00 89.12  ? 67  SER B HB3  1 
ATOM   5271  H HG   . SER B 1 67  ? 14.498  32.922  8.508   1.00 91.50  ? 67  SER B HG   1 
ATOM   5272  N N    . GLY B 1 68  ? 15.771  31.370  5.752   1.00 73.16  ? 68  GLY B N    1 
ATOM   5273  C CA   . GLY B 1 68  ? 16.974  30.566  5.671   1.00 69.65  ? 68  GLY B CA   1 
ATOM   5274  C C    . GLY B 1 68  ? 17.587  30.298  7.026   1.00 72.41  ? 68  GLY B C    1 
ATOM   5275  O O    . GLY B 1 68  ? 18.168  29.231  7.249   1.00 72.14  ? 68  GLY B O    1 
ATOM   5276  H H    . GLY B 1 68  ? 15.824  32.140  5.371   1.00 87.79  ? 68  GLY B H    1 
ATOM   5277  H HA2  . GLY B 1 68  ? 16.761  29.714  5.258   1.00 83.58  ? 68  GLY B HA2  1 
ATOM   5278  H HA3  . GLY B 1 68  ? 17.630  31.026  5.124   1.00 83.58  ? 68  GLY B HA3  1 
ATOM   5279  N N    . ASN B 1 69  ? 17.460  31.256  7.951   1.00 73.42  ? 69  ASN B N    1 
ATOM   5280  C CA   . ASN B 1 69  ? 17.991  31.076  9.297   1.00 70.40  ? 69  ASN B CA   1 
ATOM   5281  C C    . ASN B 1 69  ? 17.145  30.090  10.096  1.00 72.17  ? 69  ASN B C    1 
ATOM   5282  O O    . ASN B 1 69  ? 17.686  29.238  10.812  1.00 70.93  ? 69  ASN B O    1 
ATOM   5283  C CB   . ASN B 1 69  ? 18.061  32.426  10.008  1.00 71.74  ? 69  ASN B CB   1 
ATOM   5284  C CG   . ASN B 1 69  ? 19.472  33.010  10.034  1.00 73.30  ? 69  ASN B CG   1 
ATOM   5285  O OD1  . ASN B 1 69  ? 20.454  32.325  9.738   1.00 69.77  ? 69  ASN B OD1  1 
ATOM   5286  N ND2  . ASN B 1 69  ? 19.573  34.287  10.399  1.00 78.55  ? 69  ASN B ND2  1 
ATOM   5287  H H    . ASN B 1 69  ? 17.073  32.013  7.822   1.00 88.11  ? 69  ASN B H    1 
ATOM   5288  H HA   . ASN B 1 69  ? 18.890  30.718  9.237   1.00 84.48  ? 69  ASN B HA   1 
ATOM   5289  H HB2  . ASN B 1 69  ? 17.484  33.056  9.547   1.00 86.09  ? 69  ASN B HB2  1 
ATOM   5290  H HB3  . ASN B 1 69  ? 17.765  32.315  10.925  1.00 86.09  ? 69  ASN B HB3  1 
ATOM   5291  H HD21 . ASN B 1 69  ? 18.867  34.733  10.603  1.00 94.26  ? 69  ASN B HD21 1 
ATOM   5292  H HD22 . ASN B 1 69  ? 20.345  34.665  10.431  1.00 94.26  ? 69  ASN B HD22 1 
ATOM   5293  N N    . ALA B 1 70  ? 15.817  30.185  9.985   1.00 71.08  ? 70  ALA B N    1 
ATOM   5294  C CA   . ALA B 1 70  ? 14.954  29.206  10.637  1.00 70.12  ? 70  ALA B CA   1 
ATOM   5295  C C    . ALA B 1 70  ? 15.155  27.812  10.047  1.00 72.16  ? 70  ALA B C    1 
ATOM   5296  O O    . ALA B 1 70  ? 15.207  26.819  10.781  1.00 73.40  ? 70  ALA B O    1 
ATOM   5297  C CB   . ALA B 1 70  ? 13.492  29.632  10.518  1.00 70.80  ? 70  ALA B CB   1 
ATOM   5298  H H    . ALA B 1 70  ? 15.400  30.796  9.545   1.00 85.30  ? 70  ALA B H    1 
ATOM   5299  H HA   . ALA B 1 70  ? 15.181  29.169  11.579  1.00 84.15  ? 70  ALA B HA   1 
ATOM   5300  H HB1  . ALA B 1 70  ? 12.939  29.004  11.009  1.00 84.96  ? 70  ALA B HB1  1 
ATOM   5301  H HB2  . ALA B 1 70  ? 13.391  30.522  10.891  1.00 84.96  ? 70  ALA B HB2  1 
ATOM   5302  H HB3  . ALA B 1 70  ? 13.238  29.635  9.582   1.00 84.96  ? 70  ALA B HB3  1 
ATOM   5303  N N    . SER B 1 71  ? 15.263  27.713  8.720   1.00 71.06  ? 71  SER B N    1 
ATOM   5304  C CA   . SER B 1 71  ? 15.519  26.415  8.103   1.00 72.42  ? 71  SER B CA   1 
ATOM   5305  C C    . SER B 1 71  ? 16.856  25.845  8.565   1.00 69.67  ? 71  SER B C    1 
ATOM   5306  O O    . SER B 1 71  ? 16.992  24.632  8.758   1.00 71.21  ? 71  SER B O    1 
ATOM   5307  C CB   . SER B 1 71  ? 15.479  26.542  6.581   1.00 74.40  ? 71  SER B CB   1 
ATOM   5308  O OG   . SER B 1 71  ? 14.210  27.001  6.140   1.00 73.26  ? 71  SER B OG   1 
ATOM   5309  H H    . SER B 1 71  ? 15.193  28.369  8.168   1.00 85.28  ? 71  SER B H    1 
ATOM   5310  H HA   . SER B 1 71  ? 14.821  25.795  8.367   1.00 86.91  ? 71  SER B HA   1 
ATOM   5311  H HB2  . SER B 1 71  ? 16.158  27.175  6.300   1.00 89.27  ? 71  SER B HB2  1 
ATOM   5312  H HB3  . SER B 1 71  ? 15.653  25.672  6.187   1.00 89.27  ? 71  SER B HB3  1 
ATOM   5313  H HG   . SER B 1 71  ? 14.050  27.759  6.467   1.00 87.91  ? 71  SER B HG   1 
ATOM   5314  N N    . ARG B 1 72  ? 17.858  26.707  8.751   1.00 70.10  ? 72  ARG B N    1 
ATOM   5315  C CA   . ARG B 1 72  ? 19.138  26.251  9.283   1.00 70.46  ? 72  ARG B CA   1 
ATOM   5316  C C    . ARG B 1 72  ? 18.990  25.763  10.718  1.00 72.26  ? 72  ARG B C    1 
ATOM   5317  O O    . ARG B 1 72  ? 19.618  24.772  11.112  1.00 71.54  ? 72  ARG B O    1 
ATOM   5318  C CB   . ARG B 1 72  ? 20.167  27.383  9.203   1.00 73.09  ? 72  ARG B CB   1 
ATOM   5319  C CG   . ARG B 1 72  ? 20.794  27.576  7.826   1.00 69.48  ? 72  ARG B CG   1 
ATOM   5320  C CD   . ARG B 1 72  ? 21.226  29.022  7.568   1.00 68.77  ? 72  ARG B CD   1 
ATOM   5321  N NE   . ARG B 1 72  ? 21.459  29.788  8.786   1.00 69.25  ? 72  ARG B NE   1 
ATOM   5322  C CZ   . ARG B 1 72  ? 22.470  29.585  9.619   1.00 74.03  ? 72  ARG B CZ   1 
ATOM   5323  N NH1  . ARG B 1 72  ? 23.381  28.655  9.385   1.00 75.97  ? 72  ARG B NH1  1 
ATOM   5324  N NH2  . ARG B 1 72  ? 22.566  30.328  10.717  1.00 68.78  ? 72  ARG B NH2  1 
ATOM   5325  H H    . ARG B 1 72  ? 17.821  27.549  8.580   1.00 84.11  ? 72  ARG B H    1 
ATOM   5326  H HA   . ARG B 1 72  ? 19.460  25.512  8.744   1.00 84.55  ? 72  ARG B HA   1 
ATOM   5327  H HB2  . ARG B 1 72  ? 19.730  28.214  9.445   1.00 87.70  ? 72  ARG B HB2  1 
ATOM   5328  H HB3  . ARG B 1 72  ? 20.885  27.191  9.827   1.00 87.70  ? 72  ARG B HB3  1 
ATOM   5329  H HG2  . ARG B 1 72  ? 21.580  27.012  7.754   1.00 83.38  ? 72  ARG B HG2  1 
ATOM   5330  H HG3  . ARG B 1 72  ? 20.147  27.332  7.146   1.00 83.38  ? 72  ARG B HG3  1 
ATOM   5331  H HD2  . ARG B 1 72  ? 22.052  29.016  7.060   1.00 82.53  ? 72  ARG B HD2  1 
ATOM   5332  H HD3  . ARG B 1 72  ? 20.530  29.472  7.064   1.00 82.53  ? 72  ARG B HD3  1 
ATOM   5333  H HE   . ARG B 1 72  ? 20.902  30.415  8.977   1.00 83.10  ? 72  ARG B HE   1 
ATOM   5334  H HH11 . ARG B 1 72  ? 23.325  28.166  8.680   1.00 91.17  ? 72  ARG B HH11 1 
ATOM   5335  H HH12 . ARG B 1 72  ? 24.029  28.539  9.938   1.00 91.17  ? 72  ARG B HH12 1 
ATOM   5336  H HH21 . ARG B 1 72  ? 21.976  30.933  10.881  1.00 82.54  ? 72  ARG B HH21 1 
ATOM   5337  H HH22 . ARG B 1 72  ? 23.218  30.205  11.265  1.00 82.54  ? 72  ARG B HH22 1 
ATOM   5338  N N    . ALA B 1 73  ? 18.167  26.449  11.516  1.00 71.90  ? 73  ALA B N    1 
ATOM   5339  C CA   . ALA B 1 73  ? 17.922  26.010  12.885  1.00 69.46  ? 73  ALA B CA   1 
ATOM   5340  C C    . ALA B 1 73  ? 17.241  24.648  12.907  1.00 68.33  ? 73  ALA B C    1 
ATOM   5341  O O    . ALA B 1 73  ? 17.636  23.753  13.661  1.00 70.58  ? 73  ALA B O    1 
ATOM   5342  C CB   . ALA B 1 73  ? 17.069  27.047  13.615  1.00 71.85  ? 73  ALA B CB   1 
ATOM   5343  H H    . ALA B 1 73  ? 17.744  27.162  11.289  1.00 86.28  ? 73  ALA B H    1 
ATOM   5344  H HA   . ALA B 1 73  ? 18.770  25.933  13.348  1.00 83.35  ? 73  ALA B HA   1 
ATOM   5345  H HB1  . ALA B 1 73  ? 16.919  26.748  14.525  1.00 86.21  ? 73  ALA B HB1  1 
ATOM   5346  H HB2  . ALA B 1 73  ? 17.538  27.896  13.618  1.00 86.21  ? 73  ALA B HB2  1 
ATOM   5347  H HB3  . ALA B 1 73  ? 16.221  27.140  13.153  1.00 86.21  ? 73  ALA B HB3  1 
ATOM   5348  N N    . PHE B 1 74  ? 16.207  24.474  12.081  1.00 71.69  ? 74  PHE B N    1 
ATOM   5349  C CA   . PHE B 1 74  ? 15.517  23.188  12.006  1.00 73.88  ? 74  PHE B CA   1 
ATOM   5350  C C    . PHE B 1 74  ? 16.472  22.070  11.601  1.00 72.10  ? 74  PHE B C    1 
ATOM   5351  O O    . PHE B 1 74  ? 16.527  21.020  12.253  1.00 68.33  ? 74  PHE B O    1 
ATOM   5352  C CB   . PHE B 1 74  ? 14.352  23.277  11.017  1.00 73.18  ? 74  PHE B CB   1 
ATOM   5353  C CG   . PHE B 1 74  ? 13.497  22.040  10.975  1.00 74.07  ? 74  PHE B CG   1 
ATOM   5354  C CD1  . PHE B 1 74  ? 13.417  21.195  12.069  1.00 75.37  ? 74  PHE B CD1  1 
ATOM   5355  C CD2  . PHE B 1 74  ? 12.769  21.728  9.840   1.00 77.32  ? 74  PHE B CD2  1 
ATOM   5356  C CE1  . PHE B 1 74  ? 12.634  20.062  12.033  1.00 79.13  ? 74  PHE B CE1  1 
ATOM   5357  C CE2  . PHE B 1 74  ? 11.979  20.591  9.796   1.00 79.37  ? 74  PHE B CE2  1 
ATOM   5358  C CZ   . PHE B 1 74  ? 11.913  19.757  10.899  1.00 79.29  ? 74  PHE B CZ   1 
ATOM   5359  H H    . PHE B 1 74  ? 15.889  25.079  11.559  1.00 86.03  ? 74  PHE B H    1 
ATOM   5360  H HA   . PHE B 1 74  ? 15.160  22.978  12.883  1.00 88.66  ? 74  PHE B HA   1 
ATOM   5361  H HB2  . PHE B 1 74  ? 13.784  24.021  11.271  1.00 87.82  ? 74  PHE B HB2  1 
ATOM   5362  H HB3  . PHE B 1 74  ? 14.709  23.421  10.127  1.00 87.82  ? 74  PHE B HB3  1 
ATOM   5363  H HD1  . PHE B 1 74  ? 13.900  21.394  12.838  1.00 90.45  ? 74  PHE B HD1  1 
ATOM   5364  H HD2  . PHE B 1 74  ? 12.811  22.288  9.099   1.00 92.78  ? 74  PHE B HD2  1 
ATOM   5365  H HE1  . PHE B 1 74  ? 12.591  19.503  12.775  1.00 94.95  ? 74  PHE B HE1  1 
ATOM   5366  H HE2  . PHE B 1 74  ? 11.495  20.388  9.028   1.00 95.24  ? 74  PHE B HE2  1 
ATOM   5367  H HZ   . PHE B 1 74  ? 11.384  18.993  10.874  1.00 95.15  ? 74  PHE B HZ   1 
ATOM   5368  N N    . ALA B 1 75  ? 17.228  22.272  10.520  1.00 69.46  ? 75  ALA B N    1 
ATOM   5369  C CA   . ALA B 1 75  ? 18.171  21.248  10.083  1.00 71.07  ? 75  ALA B CA   1 
ATOM   5370  C C    . ALA B 1 75  ? 19.153  20.893  11.193  1.00 72.71  ? 75  ALA B C    1 
ATOM   5371  O O    . ALA B 1 75  ? 19.463  19.713  11.405  1.00 70.87  ? 75  ALA B O    1 
ATOM   5372  C CB   . ALA B 1 75  ? 18.923  21.720  8.837   1.00 71.35  ? 75  ALA B CB   1 
ATOM   5373  H H    . ALA B 1 75  ? 17.213  22.980  10.032  1.00 83.35  ? 75  ALA B H    1 
ATOM   5374  H HA   . ALA B 1 75  ? 17.674  20.448  9.850   1.00 85.28  ? 75  ALA B HA   1 
ATOM   5375  H HB1  . ALA B 1 75  ? 19.544  21.027  8.562   1.00 85.61  ? 75  ALA B HB1  1 
ATOM   5376  H HB2  . ALA B 1 75  ? 18.284  21.891  8.128   1.00 85.61  ? 75  ALA B HB2  1 
ATOM   5377  H HB3  . ALA B 1 75  ? 19.408  22.533  9.050   1.00 85.61  ? 75  ALA B HB3  1 
ATOM   5378  N N    . SER B 1 76  ? 19.655  21.901  11.914  1.00 68.99  ? 76  SER B N    1 
ATOM   5379  C CA   . SER B 1 76  ? 20.567  21.644  13.021  1.00 68.00  ? 76  SER B CA   1 
ATOM   5380  C C    . SER B 1 76  ? 19.872  20.945  14.178  1.00 73.93  ? 76  SER B C    1 
ATOM   5381  O O    . SER B 1 76  ? 20.541  20.273  14.975  1.00 72.43  ? 76  SER B O    1 
ATOM   5382  C CB   . SER B 1 76  ? 21.191  22.954  13.500  1.00 71.54  ? 76  SER B CB   1 
ATOM   5383  O OG   . SER B 1 76  ? 22.175  23.409  12.594  1.00 71.65  ? 76  SER B OG   1 
ATOM   5384  H H    . SER B 1 76  ? 19.482  22.733  11.780  1.00 82.79  ? 76  SER B H    1 
ATOM   5385  H HA   . SER B 1 76  ? 21.284  21.070  12.710  1.00 81.59  ? 76  SER B HA   1 
ATOM   5386  H HB2  . SER B 1 76  ? 20.495  23.626  13.572  1.00 85.85  ? 76  SER B HB2  1 
ATOM   5387  H HB3  . SER B 1 76  ? 21.603  22.808  14.366  1.00 85.85  ? 76  SER B HB3  1 
ATOM   5388  H HG   . SER B 1 76  ? 21.827  23.563  11.845  1.00 85.99  ? 76  SER B HG   1 
ATOM   5389  N N    . LEU B 1 77  ? 18.549  21.092  14.296  1.00 71.81  ? 77  LEU B N    1 
ATOM   5390  C CA   . LEU B 1 77  ? 17.821  20.353  15.323  1.00 68.38  ? 77  LEU B CA   1 
ATOM   5391  C C    . LEU B 1 77  ? 17.737  18.871  14.977  1.00 72.35  ? 77  LEU B C    1 
ATOM   5392  O O    . LEU B 1 77  ? 17.845  18.015  15.863  1.00 73.88  ? 77  LEU B O    1 
ATOM   5393  C CB   . LEU B 1 77  ? 16.423  20.941  15.495  1.00 68.34  ? 77  LEU B CB   1 
ATOM   5394  C CG   . LEU B 1 77  ? 15.461  20.136  16.372  1.00 67.73  ? 77  LEU B CG   1 
ATOM   5395  C CD1  . LEU B 1 77  ? 16.034  19.980  17.767  1.00 71.65  ? 77  LEU B CD1  1 
ATOM   5396  C CD2  . LEU B 1 77  ? 14.095  20.805  16.404  1.00 68.25  ? 77  LEU B CD2  1 
ATOM   5397  H H    . LEU B 1 77  ? 18.063  21.602  13.804  1.00 86.18  ? 77  LEU B H    1 
ATOM   5398  H HA   . LEU B 1 77  ? 18.291  20.441  16.167  1.00 82.05  ? 77  LEU B HA   1 
ATOM   5399  H HB2  . LEU B 1 77  ? 16.512  21.820  15.898  1.00 82.01  ? 77  LEU B HB2  1 
ATOM   5400  H HB3  . LEU B 1 77  ? 16.017  21.018  14.618  1.00 82.01  ? 77  LEU B HB3  1 
ATOM   5401  H HG   . LEU B 1 77  ? 15.343  19.248  16.001  1.00 81.28  ? 77  LEU B HG   1 
ATOM   5402  H HD11 . LEU B 1 77  ? 15.347  19.625  18.353  1.00 85.98  ? 77  LEU B HD11 1 
ATOM   5403  H HD12 . LEU B 1 77  ? 16.787  19.369  17.733  1.00 85.98  ? 77  LEU B HD12 1 
ATOM   5404  H HD13 . LEU B 1 77  ? 16.327  20.847  18.088  1.00 85.98  ? 77  LEU B HD13 1 
ATOM   5405  H HD21 . LEU B 1 77  ? 13.499  20.280  16.961  1.00 81.90  ? 77  LEU B HD21 1 
ATOM   5406  H HD22 . LEU B 1 77  ? 14.189  21.698  16.771  1.00 81.90  ? 77  LEU B HD22 1 
ATOM   5407  H HD23 . LEU B 1 77  ? 13.745  20.854  15.501  1.00 81.90  ? 77  LEU B HD23 1 
ATOM   5408  N N    . LEU B 1 78  ? 17.537  18.548  13.695  1.00 71.15  ? 78  LEU B N    1 
ATOM   5409  C CA   . LEU B 1 78  ? 17.469  17.147  13.289  1.00 71.60  ? 78  LEU B CA   1 
ATOM   5410  C C    . LEU B 1 78  ? 18.800  16.438  13.506  1.00 75.22  ? 78  LEU B C    1 
ATOM   5411  O O    . LEU B 1 78  ? 18.823  15.233  13.783  1.00 76.70  ? 78  LEU B O    1 
ATOM   5412  C CB   . LEU B 1 78  ? 17.049  17.041  11.823  1.00 74.39  ? 78  LEU B CB   1 
ATOM   5413  C CG   . LEU B 1 78  ? 15.663  17.587  11.484  1.00 74.83  ? 78  LEU B CG   1 
ATOM   5414  C CD1  . LEU B 1 78  ? 15.435  17.588  9.978   1.00 73.35  ? 78  LEU B CD1  1 
ATOM   5415  C CD2  . LEU B 1 78  ? 14.571  16.791  12.191  1.00 68.06  ? 78  LEU B CD2  1 
ATOM   5416  H H    . LEU B 1 78  ? 17.439  19.112  13.053  1.00 85.38  ? 78  LEU B H    1 
ATOM   5417  H HA   . LEU B 1 78  ? 16.797  16.702  13.827  1.00 85.92  ? 78  LEU B HA   1 
ATOM   5418  H HB2  . LEU B 1 78  ? 17.691  17.534  11.288  1.00 89.27  ? 78  LEU B HB2  1 
ATOM   5419  H HB3  . LEU B 1 78  ? 17.059  16.104  11.573  1.00 89.27  ? 78  LEU B HB3  1 
ATOM   5420  H HG   . LEU B 1 78  ? 15.611  18.504  11.797  1.00 89.79  ? 78  LEU B HG   1 
ATOM   5421  H HD11 . LEU B 1 78  ? 14.551  17.942  9.793   1.00 88.02  ? 78  LEU B HD11 1 
ATOM   5422  H HD12 . LEU B 1 78  ? 16.109  18.144  9.557   1.00 88.02  ? 78  LEU B HD12 1 
ATOM   5423  H HD13 . LEU B 1 78  ? 15.502  16.678  9.648   1.00 88.02  ? 78  LEU B HD13 1 
ATOM   5424  H HD21 . LEU B 1 78  ? 13.706  17.076  11.856  1.00 81.67  ? 78  LEU B HD21 1 
ATOM   5425  H HD22 . LEU B 1 78  ? 14.701  15.847  12.011  1.00 81.67  ? 78  LEU B HD22 1 
ATOM   5426  H HD23 . LEU B 1 78  ? 14.627  16.957  13.145  1.00 81.67  ? 78  LEU B HD23 1 
ATOM   5427  N N    . ALA B 1 79  ? 19.915  17.159  13.367  1.00 73.97  ? 79  ALA B N    1 
ATOM   5428  C CA   . ALA B 1 79  ? 21.209  16.578  13.707  1.00 75.19  ? 79  ALA B CA   1 
ATOM   5429  C C    . ALA B 1 79  ? 21.334  16.382  15.209  1.00 75.94  ? 79  ALA B C    1 
ATOM   5430  O O    . ALA B 1 79  ? 21.817  15.342  15.673  1.00 78.01  ? 79  ALA B O    1 
ATOM   5431  C CB   . ALA B 1 79  ? 22.339  17.473  13.197  1.00 75.51  ? 79  ALA B CB   1 
ATOM   5432  H H    . ALA B 1 79  ? 19.947  17.970  13.084  1.00 88.76  ? 79  ALA B H    1 
ATOM   5433  H HA   . ALA B 1 79  ? 21.291  15.715  13.272  1.00 90.23  ? 79  ALA B HA   1 
ATOM   5434  H HB1  . ALA B 1 79  ? 23.183  17.144  13.543  1.00 90.61  ? 79  ALA B HB1  1 
ATOM   5435  H HB2  . ALA B 1 79  ? 22.348  17.448  12.227  1.00 90.61  ? 79  ALA B HB2  1 
ATOM   5436  H HB3  . ALA B 1 79  ? 22.186  18.380  13.503  1.00 90.61  ? 79  ALA B HB3  1 
ATOM   5437  N N    . PHE B 1 80  ? 20.908  17.382  15.982  1.00 74.54  ? 80  PHE B N    1 
ATOM   5438  C CA   . PHE B 1 80  ? 20.925  17.290  17.436  1.00 73.50  ? 80  PHE B CA   1 
ATOM   5439  C C    . PHE B 1 80  ? 20.176  16.063  17.927  1.00 74.54  ? 80  PHE B C    1 
ATOM   5440  O O    . PHE B 1 80  ? 20.501  15.522  18.988  1.00 73.60  ? 80  PHE B O    1 
ATOM   5441  C CB   . PHE B 1 80  ? 20.317  18.576  18.013  1.00 71.87  ? 80  PHE B CB   1 
ATOM   5442  C CG   . PHE B 1 80  ? 20.549  18.766  19.481  1.00 72.58  ? 80  PHE B CG   1 
ATOM   5443  C CD1  . PHE B 1 80  ? 21.820  19.019  19.978  1.00 72.16  ? 80  PHE B CD1  1 
ATOM   5444  C CD2  . PHE B 1 80  ? 19.484  18.717  20.370  1.00 70.05  ? 80  PHE B CD2  1 
ATOM   5445  C CE1  . PHE B 1 80  ? 22.024  19.204  21.336  1.00 69.46  ? 80  PHE B CE1  1 
ATOM   5446  C CE2  . PHE B 1 80  ? 19.685  18.901  21.720  1.00 69.27  ? 80  PHE B CE2  1 
ATOM   5447  C CZ   . PHE B 1 80  ? 20.955  19.146  22.202  1.00 68.61  ? 80  PHE B CZ   1 
ATOM   5448  H H    . PHE B 1 80  ? 20.602  18.130  15.686  1.00 89.45  ? 80  PHE B H    1 
ATOM   5449  H HA   . PHE B 1 80  ? 21.837  17.211  17.756  1.00 88.19  ? 80  PHE B HA   1 
ATOM   5450  H HB2  . PHE B 1 80  ? 20.708  19.335  17.554  1.00 86.24  ? 80  PHE B HB2  1 
ATOM   5451  H HB3  . PHE B 1 80  ? 19.359  18.557  17.867  1.00 86.24  ? 80  PHE B HB3  1 
ATOM   5452  H HD1  . PHE B 1 80  ? 22.542  19.064  19.394  1.00 86.59  ? 80  PHE B HD1  1 
ATOM   5453  H HD2  . PHE B 1 80  ? 18.625  18.557  20.051  1.00 84.06  ? 80  PHE B HD2  1 
ATOM   5454  H HE1  . PHE B 1 80  ? 22.880  19.368  21.661  1.00 83.35  ? 80  PHE B HE1  1 
ATOM   5455  H HE2  . PHE B 1 80  ? 18.965  18.861  22.307  1.00 83.12  ? 80  PHE B HE2  1 
ATOM   5456  H HZ   . PHE B 1 80  ? 21.090  19.271  23.114  1.00 82.33  ? 80  PHE B HZ   1 
ATOM   5457  N N    . ARG B 1 81  ? 19.192  15.594  17.161  1.00 75.02  ? 81  ARG B N    1 
ATOM   5458  C CA   . ARG B 1 81  ? 18.336  14.489  17.568  1.00 74.49  ? 81  ARG B CA   1 
ATOM   5459  C C    . ARG B 1 81  ? 18.613  13.198  16.810  1.00 75.00  ? 81  ARG B C    1 
ATOM   5460  O O    . ARG B 1 81  ? 17.950  12.188  17.074  1.00 78.80  ? 81  ARG B O    1 
ATOM   5461  C CB   . ARG B 1 81  ? 16.862  14.877  17.380  1.00 73.34  ? 81  ARG B CB   1 
ATOM   5462  C CG   . ARG B 1 81  ? 16.334  15.833  18.420  1.00 68.76  ? 81  ARG B CG   1 
ATOM   5463  C CD   . ARG B 1 81  ? 14.893  16.244  18.143  1.00 66.38  ? 81  ARG B CD   1 
ATOM   5464  N NE   . ARG B 1 81  ? 14.337  17.014  19.255  1.00 75.08  ? 81  ARG B NE   1 
ATOM   5465  C CZ   . ARG B 1 81  ? 13.098  17.489  19.300  1.00 72.48  ? 81  ARG B CZ   1 
ATOM   5466  N NH1  . ARG B 1 81  ? 12.255  17.316  18.292  1.00 69.65  ? 81  ARG B NH1  1 
ATOM   5467  N NH2  . ARG B 1 81  ? 12.695  18.152  20.384  1.00 72.00  ? 81  ARG B NH2  1 
ATOM   5468  H H    . ARG B 1 81  ? 18.999  15.908  16.384  1.00 90.03  ? 81  ARG B H    1 
ATOM   5469  H HA   . ARG B 1 81  ? 18.493  14.316  18.509  1.00 89.39  ? 81  ARG B HA   1 
ATOM   5470  H HB2  . ARG B 1 81  ? 16.762  15.301  16.513  1.00 88.00  ? 81  ARG B HB2  1 
ATOM   5471  H HB3  . ARG B 1 81  ? 16.323  14.072  17.420  1.00 88.00  ? 81  ARG B HB3  1 
ATOM   5472  H HG2  . ARG B 1 81  ? 16.365  15.406  19.290  1.00 82.50  ? 81  ARG B HG2  1 
ATOM   5473  H HG3  . ARG B 1 81  ? 16.881  16.634  18.424  1.00 82.50  ? 81  ARG B HG3  1 
ATOM   5474  H HD2  . ARG B 1 81  ? 14.863  16.794  17.345  1.00 79.65  ? 81  ARG B HD2  1 
ATOM   5475  H HD3  . ARG B 1 81  ? 14.350  15.449  18.020  1.00 79.65  ? 81  ARG B HD3  1 
ATOM   5476  H HE   . ARG B 1 81  ? 14.849  17.171  19.928  1.00 90.10  ? 81  ARG B HE   1 
ATOM   5477  H HH11 . ARG B 1 81  ? 12.506  16.887  17.590  1.00 83.58  ? 81  ARG B HH11 1 
ATOM   5478  H HH12 . ARG B 1 81  ? 11.456  17.631  18.341  1.00 83.58  ? 81  ARG B HH12 1 
ATOM   5479  H HH21 . ARG B 1 81  ? 13.234  18.267  21.044  1.00 86.40  ? 81  ARG B HH21 1 
ATOM   5480  H HH22 . ARG B 1 81  ? 11.894  18.464  20.424  1.00 86.40  ? 81  ARG B HH22 1 
ATOM   5481  N N    . ASP B 1 82  ? 19.558  13.199  15.874  1.00 76.35  ? 82  ASP B N    1 
ATOM   5482  C CA   . ASP B 1 82  ? 19.870  12.017  15.081  1.00 76.93  ? 82  ASP B CA   1 
ATOM   5483  C C    . ASP B 1 82  ? 20.986  11.233  15.758  1.00 76.28  ? 82  ASP B C    1 
ATOM   5484  O O    . ASP B 1 82  ? 22.025  11.802  16.112  1.00 77.22  ? 82  ASP B O    1 
ATOM   5485  C CB   . ASP B 1 82  ? 20.288  12.417  13.665  1.00 78.73  ? 82  ASP B CB   1 
ATOM   5486  C CG   . ASP B 1 82  ? 20.623  11.217  12.786  1.00 80.63  ? 82  ASP B CG   1 
ATOM   5487  O OD1  . ASP B 1 82  ? 19.917  10.188  12.879  1.00 81.69  ? 82  ASP B OD1  1 
ATOM   5488  O OD2  . ASP B 1 82  ? 21.589  11.308  11.994  1.00 78.96  ? 82  ASP B OD2  1 
ATOM   5489  H H    . ASP B 1 82  ? 20.039  13.883  15.678  1.00 91.62  ? 82  ASP B H    1 
ATOM   5490  H HA   . ASP B 1 82  ? 19.087  11.449  15.017  1.00 92.32  ? 82  ASP B HA   1 
ATOM   5491  H HB2  . ASP B 1 82  ? 19.560  12.902  13.246  1.00 94.47  ? 82  ASP B HB2  1 
ATOM   5492  H HB3  . ASP B 1 82  ? 21.076  12.981  13.715  1.00 94.47  ? 82  ASP B HB3  1 
ATOM   5493  N N    . LYS B 1 83  ? 20.764  9.930   15.942  1.00 76.91  ? 83  LYS B N    1 
ATOM   5494  C CA   . LYS B 1 83  ? 21.784  9.086   16.551  1.00 77.61  ? 83  LYS B CA   1 
ATOM   5495  C C    . LYS B 1 83  ? 22.971  8.854   15.625  1.00 82.70  ? 83  LYS B C    1 
ATOM   5496  O O    . LYS B 1 83  ? 24.067  8.546   16.107  1.00 84.42  ? 83  LYS B O    1 
ATOM   5497  C CB   . LYS B 1 83  ? 21.179  7.741   16.948  1.00 78.70  ? 83  LYS B CB   1 
ATOM   5498  C CG   . LYS B 1 83  ? 21.027  6.772   15.775  1.00 81.63  ? 83  LYS B CG   1 
ATOM   5499  C CD   . LYS B 1 83  ? 19.696  6.025   15.826  1.00 82.00  ? 83  LYS B CD   1 
ATOM   5500  C CE   . LYS B 1 83  ? 19.573  5.007   14.699  1.00 80.90  ? 83  LYS B CE   1 
ATOM   5501  N NZ   . LYS B 1 83  ? 20.195  5.473   13.422  1.00 85.42  ? 83  LYS B NZ   1 
ATOM   5502  H H    . LYS B 1 83  ? 20.041  9.518   15.725  1.00 92.30  ? 83  LYS B H    1 
ATOM   5503  H HA   . LYS B 1 83  ? 22.109  9.524   17.354  1.00 93.13  ? 83  LYS B HA   1 
ATOM   5504  H HB2  . LYS B 1 83  ? 21.753  7.322   17.608  1.00 94.44  ? 83  LYS B HB2  1 
ATOM   5505  H HB3  . LYS B 1 83  ? 20.298  7.893   17.324  1.00 94.44  ? 83  LYS B HB3  1 
ATOM   5506  H HG2  . LYS B 1 83  ? 21.064  7.268   14.943  1.00 97.96  ? 83  LYS B HG2  1 
ATOM   5507  H HG3  . LYS B 1 83  ? 21.743  6.118   15.805  1.00 97.96  ? 83  LYS B HG3  1 
ATOM   5508  H HD2  . LYS B 1 83  ? 19.626  5.552   16.671  1.00 98.40  ? 83  LYS B HD2  1 
ATOM   5509  H HD3  . LYS B 1 83  ? 18.968  6.661   15.741  1.00 98.40  ? 83  LYS B HD3  1 
ATOM   5510  H HE2  . LYS B 1 83  ? 20.016  4.186   14.965  1.00 97.08  ? 83  LYS B HE2  1 
ATOM   5511  H HE3  . LYS B 1 83  ? 18.633  4.836   14.529  1.00 97.08  ? 83  LYS B HE3  1 
ATOM   5512  H HZ1  . LYS B 1 83  ? 19.862  5.014   12.736  1.00 102.50 ? 83  LYS B HZ1  1 
ATOM   5513  H HZ2  . LYS B 1 83  ? 20.026  6.338   13.300  1.00 102.50 ? 83  LYS B HZ2  1 
ATOM   5514  H HZ3  . LYS B 1 83  ? 21.076  5.352   13.451  1.00 102.50 ? 83  LYS B HZ3  1 
ATOM   5515  N N    . ASP B 1 84  ? 22.771  8.989   14.313  1.00 80.65  ? 84  ASP B N    1 
ATOM   5516  C CA   . ASP B 1 84  ? 23.799  8.702   13.326  1.00 81.40  ? 84  ASP B CA   1 
ATOM   5517  C C    . ASP B 1 84  ? 24.674  9.906   13.000  1.00 83.22  ? 84  ASP B C    1 
ATOM   5518  O O    . ASP B 1 84  ? 25.658  9.756   12.264  1.00 81.47  ? 84  ASP B O    1 
ATOM   5519  C CB   . ASP B 1 84  ? 23.152  8.192   12.029  1.00 83.85  ? 84  ASP B CB   1 
ATOM   5520  C CG   . ASP B 1 84  ? 22.577  6.791   12.168  1.00 82.40  ? 84  ASP B CG   1 
ATOM   5521  O OD1  . ASP B 1 84  ? 23.062  6.002   13.002  1.00 80.05  ? 84  ASP B OD1  1 
ATOM   5522  O OD2  . ASP B 1 84  ? 21.633  6.466   11.424  1.00 90.56  ? 84  ASP B OD2  1 
ATOM   5523  H H    . ASP B 1 84  ? 22.030  9.253   13.966  1.00 96.78  ? 84  ASP B H    1 
ATOM   5524  H HA   . ASP B 1 84  ? 24.373  8.003   13.676  1.00 97.68  ? 84  ASP B HA   1 
ATOM   5525  H HB2  . ASP B 1 84  ? 22.430  8.790   11.781  1.00 100.62 ? 84  ASP B HB2  1 
ATOM   5526  H HB3  . ASP B 1 84  ? 23.823  8.174   11.328  1.00 100.62 ? 84  ASP B HB3  1 
ATOM   5527  N N    . PHE B 1 85  ? 24.345  11.088  13.511  1.00 82.24  ? 85  PHE B N    1 
ATOM   5528  C CA   . PHE B 1 85  ? 25.157  12.265  13.236  1.00 80.86  ? 85  PHE B CA   1 
ATOM   5529  C C    . PHE B 1 85  ? 26.516  12.114  13.911  1.00 84.10  ? 85  PHE B C    1 
ATOM   5530  O O    . PHE B 1 85  ? 26.595  11.947  15.134  1.00 85.13  ? 85  PHE B O    1 
ATOM   5531  C CB   . PHE B 1 85  ? 24.454  13.527  13.718  1.00 80.56  ? 85  PHE B CB   1 
ATOM   5532  C CG   . PHE B 1 85  ? 25.217  14.790  13.428  1.00 85.99  ? 85  PHE B CG   1 
ATOM   5533  C CD1  . PHE B 1 85  ? 26.195  15.238  14.304  1.00 86.67  ? 85  PHE B CD1  1 
ATOM   5534  C CD2  . PHE B 1 85  ? 24.959  15.529  12.284  1.00 84.37  ? 85  PHE B CD2  1 
ATOM   5535  C CE1  . PHE B 1 85  ? 26.901  16.399  14.047  1.00 84.91  ? 85  PHE B CE1  1 
ATOM   5536  C CE2  . PHE B 1 85  ? 25.659  16.692  12.024  1.00 83.61  ? 85  PHE B CE2  1 
ATOM   5537  C CZ   . PHE B 1 85  ? 26.633  17.126  12.908  1.00 85.65  ? 85  PHE B CZ   1 
ATOM   5538  H H    . PHE B 1 85  ? 23.663  11.232  14.015  1.00 98.69  ? 85  PHE B H    1 
ATOM   5539  H HA   . PHE B 1 85  ? 25.290  12.346  12.278  1.00 97.03  ? 85  PHE B HA   1 
ATOM   5540  H HB2  . PHE B 1 85  ? 23.593  13.592  13.277  1.00 96.68  ? 85  PHE B HB2  1 
ATOM   5541  H HB3  . PHE B 1 85  ? 24.331  13.468  14.678  1.00 96.68  ? 85  PHE B HB3  1 
ATOM   5542  H HD1  . PHE B 1 85  ? 26.378  14.752  15.075  1.00 104.01 ? 85  PHE B HD1  1 
ATOM   5543  H HD2  . PHE B 1 85  ? 24.308  15.240  11.685  1.00 101.24 ? 85  PHE B HD2  1 
ATOM   5544  H HE1  . PHE B 1 85  ? 27.556  16.688  14.641  1.00 101.90 ? 85  PHE B HE1  1 
ATOM   5545  H HE2  . PHE B 1 85  ? 25.476  17.183  11.255  1.00 100.34 ? 85  PHE B HE2  1 
ATOM   5546  H HZ   . PHE B 1 85  ? 27.106  17.907  12.732  1.00 102.78 ? 85  PHE B HZ   1 
ATOM   5547  N N    . SER B 1 86  ? 27.580  12.158  13.107  1.00 85.03  ? 86  SER B N    1 
ATOM   5548  C CA   . SER B 1 86  ? 28.945  12.091  13.614  1.00 88.99  ? 86  SER B CA   1 
ATOM   5549  C C    . SER B 1 86  ? 29.598  13.471  13.518  1.00 92.60  ? 86  SER B C    1 
ATOM   5550  O O    . SER B 1 86  ? 29.743  14.165  14.533  1.00 97.77  ? 86  SER B O    1 
ATOM   5551  C CB   . SER B 1 86  ? 29.749  11.044  12.845  1.00 90.95  ? 86  SER B CB   1 
ATOM   5552  O OG   . SER B 1 86  ? 29.519  9.745   13.376  1.00 96.07  ? 86  SER B OG   1 
ATOM   5553  H H    . SER B 1 86  ? 27.534  12.227  12.251  1.00 102.03 ? 86  SER B H    1 
ATOM   5554  H HA   . SER B 1 86  ? 28.940  11.822  14.546  1.00 106.79 ? 86  SER B HA   1 
ATOM   5555  H HB2  . SER B 1 86  ? 29.478  11.057  11.914  1.00 109.14 ? 86  SER B HB2  1 
ATOM   5556  H HB3  . SER B 1 86  ? 30.693  11.253  12.919  1.00 109.14 ? 86  SER B HB3  1 
ATOM   5557  H HG   . SER B 1 86  ? 29.972  9.177   12.953  1.00 115.29 ? 86  SER B HG   1 
ATOM   5558  N N    . LYS B 1 87  ? 29.988  13.874  12.307  1.00 96.43  ? 87  LYS B N    1 
ATOM   5559  C CA   . LYS B 1 87  ? 30.511  15.221  12.081  1.00 94.58  ? 87  LYS B CA   1 
ATOM   5560  C C    . LYS B 1 87  ? 29.690  15.971  11.041  1.00 96.33  ? 87  LYS B C    1 
ATOM   5561  O O    . LYS B 1 87  ? 29.097  17.007  11.357  1.00 99.41  ? 87  LYS B O    1 
ATOM   5562  C CB   . LYS B 1 87  ? 31.987  15.157  11.657  1.00 98.88  ? 87  LYS B CB   1 
ATOM   5563  C CG   . LYS B 1 87  ? 32.572  16.470  11.136  1.00 104.70 ? 87  LYS B CG   1 
ATOM   5564  C CD   . LYS B 1 87  ? 32.064  17.678  11.923  1.00 103.80 ? 87  LYS B CD   1 
ATOM   5565  C CE   . LYS B 1 87  ? 33.125  18.756  12.072  1.00 104.39 ? 87  LYS B CE   1 
ATOM   5566  N NZ   . LYS B 1 87  ? 34.258  18.318  12.936  1.00 105.03 ? 87  LYS B NZ   1 
ATOM   5567  H H    . LYS B 1 87  ? 29.959  13.385  11.600  1.00 115.72 ? 87  LYS B H    1 
ATOM   5568  H HA   . LYS B 1 87  ? 30.464  15.713  12.915  1.00 113.50 ? 87  LYS B HA   1 
ATOM   5569  H HB2  . LYS B 1 87  ? 32.514  14.889  12.426  1.00 118.65 ? 87  LYS B HB2  1 
ATOM   5570  H HB3  . LYS B 1 87  ? 32.074  14.500  10.949  1.00 118.65 ? 87  LYS B HB3  1 
ATOM   5571  H HG2  . LYS B 1 87  ? 33.539  16.443  11.216  1.00 125.64 ? 87  LYS B HG2  1 
ATOM   5572  H HG3  . LYS B 1 87  ? 32.319  16.586  10.207  1.00 125.64 ? 87  LYS B HG3  1 
ATOM   5573  H HD2  . LYS B 1 87  ? 31.304  18.064  11.459  1.00 124.56 ? 87  LYS B HD2  1 
ATOM   5574  H HD3  . LYS B 1 87  ? 31.799  17.391  12.811  1.00 124.56 ? 87  LYS B HD3  1 
ATOM   5575  H HE2  . LYS B 1 87  ? 33.480  18.975  11.196  1.00 125.27 ? 87  LYS B HE2  1 
ATOM   5576  H HE3  . LYS B 1 87  ? 32.725  19.543  12.474  1.00 125.27 ? 87  LYS B HE3  1 
ATOM   5577  H HZ1  . LYS B 1 87  ? 34.857  18.972  13.007  1.00 126.04 ? 87  LYS B HZ1  1 
ATOM   5578  H HZ2  . LYS B 1 87  ? 33.959  18.110  13.748  1.00 126.04 ? 87  LYS B HZ2  1 
ATOM   5579  H HZ3  . LYS B 1 87  ? 34.652  17.602  12.582  1.00 126.04 ? 87  LYS B HZ3  1 
ATOM   5580  N N    . GLN B 1 88  ? 29.631  15.477  9.810   1.00 90.01  ? 88  GLN B N    1 
ATOM   5581  C CA   . GLN B 1 88  ? 28.856  16.095  8.745   1.00 87.36  ? 88  GLN B CA   1 
ATOM   5582  C C    . GLN B 1 88  ? 27.692  15.191  8.359   1.00 85.17  ? 88  GLN B C    1 
ATOM   5583  O O    . GLN B 1 88  ? 27.785  13.961  8.430   1.00 86.32  ? 88  GLN B O    1 
ATOM   5584  C CB   . GLN B 1 88  ? 29.744  16.378  7.521   1.00 88.49  ? 88  GLN B CB   1 
ATOM   5585  C CG   . GLN B 1 88  ? 29.698  15.318  6.444   1.00 90.14  ? 88  GLN B CG   1 
ATOM   5586  C CD   . GLN B 1 88  ? 28.667  15.629  5.382   1.00 89.11  ? 88  GLN B CD   1 
ATOM   5587  O OE1  . GLN B 1 88  ? 28.229  16.774  5.251   1.00 85.58  ? 88  GLN B OE1  1 
ATOM   5588  N NE2  . GLN B 1 88  ? 28.263  14.612  4.622   1.00 92.47  ? 88  GLN B NE2  1 
ATOM   5589  H H    . GLN B 1 88  ? 30.043  14.765  9.561   1.00 108.01 ? 88  GLN B H    1 
ATOM   5590  H HA   . GLN B 1 88  ? 28.488  16.939  9.048   1.00 104.83 ? 88  GLN B HA   1 
ATOM   5591  H HB2  . GLN B 1 88  ? 29.457  17.214  7.121   1.00 106.19 ? 88  GLN B HB2  1 
ATOM   5592  H HB3  . GLN B 1 88  ? 30.664  16.452  7.819   1.00 106.19 ? 88  GLN B HB3  1 
ATOM   5593  H HG2  . GLN B 1 88  ? 30.566  15.261  6.016   1.00 108.17 ? 88  GLN B HG2  1 
ATOM   5594  H HG3  . GLN B 1 88  ? 29.469  14.465  6.846   1.00 108.17 ? 88  GLN B HG3  1 
ATOM   5595  H HE21 . GLN B 1 88  ? 28.587  13.825  4.748   1.00 110.96 ? 88  GLN B HE21 1 
ATOM   5596  H HE22 . GLN B 1 88  ? 27.679  14.742  4.004   1.00 110.96 ? 88  GLN B HE22 1 
ATOM   5597  N N    . LYS B 1 89  ? 26.594  15.814  7.940   1.00 84.46  ? 89  LYS B N    1 
ATOM   5598  C CA   . LYS B 1 89  ? 25.446  15.069  7.441   1.00 81.57  ? 89  LYS B CA   1 
ATOM   5599  C C    . LYS B 1 89  ? 24.443  16.006  6.783   1.00 80.99  ? 89  LYS B C    1 
ATOM   5600  O O    . LYS B 1 89  ? 24.051  17.018  7.372   1.00 81.74  ? 89  LYS B O    1 
ATOM   5601  C CB   . LYS B 1 89  ? 24.777  14.288  8.573   1.00 83.01  ? 89  LYS B CB   1 
ATOM   5602  C CG   . LYS B 1 89  ? 23.534  13.525  8.141   1.00 81.03  ? 89  LYS B CG   1 
ATOM   5603  C CD   . LYS B 1 89  ? 23.544  12.100  8.680   1.00 82.73  ? 89  LYS B CD   1 
ATOM   5604  C CE   . LYS B 1 89  ? 22.526  11.234  7.948   1.00 83.76  ? 89  LYS B CE   1 
ATOM   5605  N NZ   . LYS B 1 89  ? 21.174  11.286  8.572   1.00 80.98  ? 89  LYS B NZ   1 
ATOM   5606  H H    . LYS B 1 89  ? 26.491  16.668  7.934   1.00 101.35 ? 89  LYS B H    1 
ATOM   5607  H HA   . LYS B 1 89  ? 25.749  14.432  6.776   1.00 97.88  ? 89  LYS B HA   1 
ATOM   5608  H HB2  . LYS B 1 89  ? 25.412  13.644  8.925   1.00 99.62  ? 89  LYS B HB2  1 
ATOM   5609  H HB3  . LYS B 1 89  ? 24.515  14.910  9.269   1.00 99.62  ? 89  LYS B HB3  1 
ATOM   5610  H HG2  . LYS B 1 89  ? 22.746  13.975  8.482   1.00 97.24  ? 89  LYS B HG2  1 
ATOM   5611  H HG3  . LYS B 1 89  ? 23.501  13.485  7.173   1.00 97.24  ? 89  LYS B HG3  1 
ATOM   5612  H HD2  . LYS B 1 89  ? 24.424  11.713  8.554   1.00 99.28  ? 89  LYS B HD2  1 
ATOM   5613  H HD3  . LYS B 1 89  ? 23.317  12.110  9.623   1.00 99.28  ? 89  LYS B HD3  1 
ATOM   5614  H HE2  . LYS B 1 89  ? 22.446  11.544  7.032   1.00 100.51 ? 89  LYS B HE2  1 
ATOM   5615  H HE3  . LYS B 1 89  ? 22.827  10.312  7.961   1.00 100.51 ? 89  LYS B HE3  1 
ATOM   5616  H HZ1  . LYS B 1 89  ? 20.874  12.124  8.578   1.00 97.18  ? 89  LYS B HZ1  1 
ATOM   5617  H HZ2  . LYS B 1 89  ? 21.213  10.987  9.409   1.00 97.18  ? 89  LYS B HZ2  1 
ATOM   5618  H HZ3  . LYS B 1 89  ? 20.606  10.779  8.110   1.00 97.18  ? 89  LYS B HZ3  1 
ATOM   5619  N N    . ASN B 1 90  ? 24.022  15.674  5.565   1.00 81.25  ? 90  ASN B N    1 
ATOM   5620  C CA   . ASN B 1 90  ? 23.035  16.457  4.838   1.00 80.50  ? 90  ASN B CA   1 
ATOM   5621  C C    . ASN B 1 90  ? 21.625  16.044  5.242   1.00 79.01  ? 90  ASN B C    1 
ATOM   5622  O O    . ASN B 1 90  ? 21.327  14.853  5.386   1.00 79.99  ? 90  ASN B O    1 
ATOM   5623  C CB   . ASN B 1 90  ? 23.218  16.274  3.332   1.00 80.96  ? 90  ASN B CB   1 
ATOM   5624  C CG   . ASN B 1 90  ? 24.262  17.215  2.750   1.00 81.51  ? 90  ASN B CG   1 
ATOM   5625  O OD1  . ASN B 1 90  ? 23.957  18.042  1.889   1.00 84.57  ? 90  ASN B OD1  1 
ATOM   5626  N ND2  . ASN B 1 90  ? 25.499  17.095  3.220   1.00 82.73  ? 90  ASN B ND2  1 
ATOM   5627  H H    . ASN B 1 90  ? 24.301  14.985  5.133   1.00 97.50  ? 90  ASN B H    1 
ATOM   5628  H HA   . ASN B 1 90  ? 23.147  17.396  5.050   1.00 96.60  ? 90  ASN B HA   1 
ATOM   5629  H HB2  . ASN B 1 90  ? 23.503  15.364  3.156   1.00 97.15  ? 90  ASN B HB2  1 
ATOM   5630  H HB3  . ASN B 1 90  ? 22.374  16.449  2.887   1.00 97.15  ? 90  ASN B HB3  1 
ATOM   5631  H HD21 . ASN B 1 90  ? 25.674  16.506  3.822   1.00 99.27  ? 90  ASN B HD21 1 
ATOM   5632  H HD22 . ASN B 1 90  ? 26.124  17.604  2.921   1.00 99.27  ? 90  ASN B HD22 1 
ATOM   5633  N N    . TYR B 1 91  ? 20.756  17.037  5.418   1.00 76.66  ? 91  TYR B N    1 
ATOM   5634  C CA   . TYR B 1 91  ? 19.378  16.810  5.830   1.00 77.08  ? 91  TYR B CA   1 
ATOM   5635  C C    . TYR B 1 91  ? 18.441  17.492  4.845   1.00 78.69  ? 91  TYR B C    1 
ATOM   5636  O O    . TYR B 1 91  ? 18.596  18.684  4.559   1.00 80.89  ? 91  TYR B O    1 
ATOM   5637  C CB   . TYR B 1 91  ? 19.132  17.340  7.244   1.00 80.53  ? 91  TYR B CB   1 
ATOM   5638  C CG   . TYR B 1 91  ? 19.829  16.539  8.319   1.00 76.77  ? 91  TYR B CG   1 
ATOM   5639  C CD1  . TYR B 1 91  ? 19.240  15.405  8.856   1.00 74.57  ? 91  TYR B CD1  1 
ATOM   5640  C CD2  . TYR B 1 91  ? 21.082  16.911  8.783   1.00 76.74  ? 91  TYR B CD2  1 
ATOM   5641  C CE1  . TYR B 1 91  ? 19.876  14.666  9.830   1.00 80.64  ? 91  TYR B CE1  1 
ATOM   5642  C CE2  . TYR B 1 91  ? 21.726  16.183  9.755   1.00 79.71  ? 91  TYR B CE2  1 
ATOM   5643  C CZ   . TYR B 1 91  ? 21.119  15.062  10.281  1.00 81.72  ? 91  TYR B CZ   1 
ATOM   5644  O OH   . TYR B 1 91  ? 21.765  14.331  11.258  1.00 79.75  ? 91  TYR B OH   1 
ATOM   5645  H H    . TYR B 1 91  ? 20.948  17.867  5.302   1.00 92.00  ? 91  TYR B H    1 
ATOM   5646  H HA   . TYR B 1 91  ? 19.190  15.859  5.820   1.00 92.49  ? 91  TYR B HA   1 
ATOM   5647  H HB2  . TYR B 1 91  ? 19.456  18.253  7.297   1.00 96.64  ? 91  TYR B HB2  1 
ATOM   5648  H HB3  . TYR B 1 91  ? 18.180  17.315  7.426   1.00 96.64  ? 91  TYR B HB3  1 
ATOM   5649  H HD1  . TYR B 1 91  ? 18.401  15.140  8.555   1.00 89.49  ? 91  TYR B HD1  1 
ATOM   5650  H HD2  . TYR B 1 91  ? 21.494  17.667  8.431   1.00 92.09  ? 91  TYR B HD2  1 
ATOM   5651  H HE1  . TYR B 1 91  ? 19.471  13.906  10.181  1.00 96.76  ? 91  TYR B HE1  1 
ATOM   5652  H HE2  . TYR B 1 91  ? 22.567  16.445  10.055  1.00 95.66  ? 91  TYR B HE2  1 
ATOM   5653  H HH   . TYR B 1 91  ? 21.284  13.685  11.498  1.00 95.71  ? 91  TYR B HH   1 
ATOM   5654  N N    . ASN B 1 92  ? 17.477  16.734  4.330   1.00 80.10  ? 92  ASN B N    1 
ATOM   5655  C CA   . ASN B 1 92  ? 16.485  17.254  3.399   1.00 81.70  ? 92  ASN B CA   1 
ATOM   5656  C C    . ASN B 1 92  ? 15.262  17.726  4.176   1.00 80.65  ? 92  ASN B C    1 
ATOM   5657  O O    . ASN B 1 92  ? 14.692  16.965  4.966   1.00 78.40  ? 92  ASN B O    1 
ATOM   5658  C CB   . ASN B 1 92  ? 16.081  16.180  2.387   1.00 79.50  ? 92  ASN B CB   1 
ATOM   5659  C CG   . ASN B 1 92  ? 17.124  15.974  1.301   1.00 83.55  ? 92  ASN B CG   1 
ATOM   5660  O OD1  . ASN B 1 92  ? 17.868  16.888  0.945   1.00 85.20  ? 92  ASN B OD1  1 
ATOM   5661  N ND2  . ASN B 1 92  ? 17.175  14.765  0.763   1.00 89.08  ? 92  ASN B ND2  1 
ATOM   5662  H H    . ASN B 1 92  ? 17.375  15.899  4.509   1.00 96.12  ? 92  ASN B H    1 
ATOM   5663  H HA   . ASN B 1 92  ? 16.856  18.006  2.912   1.00 98.05  ? 92  ASN B HA   1 
ATOM   5664  H HB2  . ASN B 1 92  ? 15.961  15.337  2.852   1.00 95.40  ? 92  ASN B HB2  1 
ATOM   5665  H HB3  . ASN B 1 92  ? 15.251  16.444  1.960   1.00 95.40  ? 92  ASN B HB3  1 
ATOM   5666  H HD21 . ASN B 1 92  ? 16.637  14.152  1.033   1.00 106.90 ? 92  ASN B HD21 1 
ATOM   5667  H HD22 . ASN B 1 92  ? 17.747  14.594  0.144   1.00 106.90 ? 92  ASN B HD22 1 
ATOM   5668  N N    . ILE B 1 93  ? 14.860  18.978  3.949   1.00 81.74  ? 93  ILE B N    1 
ATOM   5669  C CA   . ILE B 1 93  ? 13.727  19.574  4.644   1.00 83.87  ? 93  ILE B CA   1 
ATOM   5670  C C    . ILE B 1 93  ? 12.898  20.380  3.651   1.00 86.71  ? 93  ILE B C    1 
ATOM   5671  O O    . ILE B 1 93  ? 13.272  20.561  2.492   1.00 86.00  ? 93  ILE B O    1 
ATOM   5672  C CB   . ILE B 1 93  ? 14.168  20.470  5.824   1.00 84.35  ? 93  ILE B CB   1 
ATOM   5673  C CG1  . ILE B 1 93  ? 15.028  21.637  5.335   1.00 83.73  ? 93  ILE B CG1  1 
ATOM   5674  C CG2  . ILE B 1 93  ? 14.938  19.654  6.861   1.00 81.10  ? 93  ILE B CG2  1 
ATOM   5675  C CD1  . ILE B 1 93  ? 15.043  22.823  6.288   1.00 80.01  ? 93  ILE B CD1  1 
ATOM   5676  H H    . ILE B 1 93  ? 15.237  19.507  3.386   1.00 98.09  ? 93  ILE B H    1 
ATOM   5677  H HA   . ILE B 1 93  ? 13.167  18.862  4.991   1.00 100.65 ? 93  ILE B HA   1 
ATOM   5678  H HB   . ILE B 1 93  ? 13.367  20.829  6.235   1.00 101.22 ? 93  ILE B HB   1 
ATOM   5679  H HG12 . ILE B 1 93  ? 15.942  21.330  5.230   1.00 100.48 ? 93  ILE B HG12 1 
ATOM   5680  H HG13 . ILE B 1 93  ? 14.682  21.945  4.483   1.00 100.48 ? 93  ILE B HG13 1 
ATOM   5681  H HG21 . ILE B 1 93  ? 15.160  20.226  7.612   1.00 97.32  ? 93  ILE B HG21 1 
ATOM   5682  H HG22 . ILE B 1 93  ? 14.381  18.918  7.160   1.00 97.32  ? 93  ILE B HG22 1 
ATOM   5683  H HG23 . ILE B 1 93  ? 15.749  19.311  6.455   1.00 97.32  ? 93  ILE B HG23 1 
ATOM   5684  H HD11 . ILE B 1 93  ? 15.692  23.472  5.974   1.00 96.01  ? 93  ILE B HD11 1 
ATOM   5685  H HD12 . ILE B 1 93  ? 14.159  23.223  6.308   1.00 96.01  ? 93  ILE B HD12 1 
ATOM   5686  H HD13 . ILE B 1 93  ? 15.286  22.513  7.174   1.00 96.01  ? 93  ILE B HD13 1 
ATOM   5687  N N    . THR B 1 94  ? 11.757  20.869  4.130   1.00 91.33  ? 94  THR B N    1 
ATOM   5688  C CA   . THR B 1 94  ? 10.882  21.743  3.361   1.00 93.72  ? 94  THR B CA   1 
ATOM   5689  C C    . THR B 1 94  ? 10.397  22.864  4.272   1.00 92.62  ? 94  THR B C    1 
ATOM   5690  O O    . THR B 1 94  ? 10.079  22.628  5.442   1.00 89.36  ? 94  THR B O    1 
ATOM   5691  C CB   . THR B 1 94  ? 9.686   20.979  2.779   1.00 89.81  ? 94  THR B CB   1 
ATOM   5692  O OG1  . THR B 1 94  ? 8.639   20.901  3.754   1.00 96.90  ? 94  THR B OG1  1 
ATOM   5693  C CG2  . THR B 1 94  ? 10.094  19.573  2.370   1.00 93.26  ? 94  THR B CG2  1 
ATOM   5694  H H    . THR B 1 94  ? 11.461  20.704  4.921   1.00 109.60 ? 94  THR B H    1 
ATOM   5695  H HA   . THR B 1 94  ? 11.370  22.132  2.619   1.00 112.46 ? 94  THR B HA   1 
ATOM   5696  H HB   . THR B 1 94  ? 9.362   21.445  1.992   1.00 107.77 ? 94  THR B HB   1 
ATOM   5697  H HG1  . THR B 1 94  ? 8.011   20.426  3.463   1.00 116.29 ? 94  THR B HG1  1 
ATOM   5698  H HG21 . THR B 1 94  ? 9.386   19.160  1.850   1.00 111.91 ? 94  THR B HG21 1 
ATOM   5699  H HG22 . THR B 1 94  ? 10.901  19.605  1.833   1.00 111.91 ? 94  THR B HG22 1 
ATOM   5700  H HG23 . THR B 1 94  ? 10.261  19.034  3.159   1.00 111.91 ? 94  THR B HG23 1 
ATOM   5701  N N    . CYS B 1 95  ? 10.348  24.084  3.733   1.00 89.47  ? 95  CYS B N    1 
ATOM   5702  C CA   . CYS B 1 95  ? 9.937   25.261  4.485   1.00 85.61  ? 95  CYS B CA   1 
ATOM   5703  C C    . CYS B 1 95  ? 8.892   26.043  3.705   1.00 81.25  ? 95  CYS B C    1 
ATOM   5704  O O    . CYS B 1 95  ? 8.955   26.127  2.480   1.00 81.14  ? 95  CYS B O    1 
ATOM   5705  C CB   . CYS B 1 95  ? 11.140  26.169  4.802   1.00 83.45  ? 95  CYS B CB   1 
ATOM   5706  S SG   . CYS B 1 95  ? 10.737  27.635  5.785   1.00 77.61  ? 95  CYS B SG   1 
ATOM   5707  H H    . CYS B 1 95  ? 10.553  24.255  2.916   1.00 107.36 ? 95  CYS B H    1 
ATOM   5708  H HA   . CYS B 1 95  ? 9.535   24.979  5.322   1.00 102.73 ? 95  CYS B HA   1 
ATOM   5709  H HB2  . CYS B 1 95  ? 11.794  25.654  5.299   1.00 100.14 ? 95  CYS B HB2  1 
ATOM   5710  H HB3  . CYS B 1 95  ? 11.525  26.475  3.965   1.00 100.14 ? 95  CYS B HB3  1 
ATOM   5711  H HG   . CYS B 1 95  ? 9.953   28.310  5.176   1.00 93.13  ? 95  CYS B HG   1 
ATOM   5712  N N    . SER B 1 96  ? 7.936   26.619  4.430   1.00 83.52  ? 96  SER B N    1 
ATOM   5713  C CA   . SER B 1 96  ? 6.903   27.430  3.801   1.00 80.30  ? 96  SER B CA   1 
ATOM   5714  C C    . SER B 1 96  ? 7.523   28.613  3.063   1.00 78.90  ? 96  SER B C    1 
ATOM   5715  O O    . SER B 1 96  ? 8.414   29.296  3.580   1.00 76.49  ? 96  SER B O    1 
ATOM   5716  C CB   . SER B 1 96  ? 5.910   27.926  4.857   1.00 78.65  ? 96  SER B CB   1 
ATOM   5717  O OG   . SER B 1 96  ? 6.583   28.426  5.999   1.00 74.90  ? 96  SER B OG   1 
ATOM   5718  H H    . SER B 1 96  ? 7.865   26.555  5.284   1.00 100.23 ? 96  SER B H    1 
ATOM   5719  H HA   . SER B 1 96  ? 6.417   26.893  3.156   1.00 96.35  ? 96  SER B HA   1 
ATOM   5720  H HB2  . SER B 1 96  ? 5.372   28.636  4.474   1.00 94.38  ? 96  SER B HB2  1 
ATOM   5721  H HB3  . SER B 1 96  ? 5.342   27.187  5.125   1.00 94.38  ? 96  SER B HB3  1 
ATOM   5722  H HG   . SER B 1 96  ? 7.086   29.062  5.781   1.00 89.87  ? 96  SER B HG   1 
ATOM   5723  N N    . GLY B 1 97  ? 7.040   28.855  1.846   1.00 80.76  ? 97  GLY B N    1 
ATOM   5724  C CA   . GLY B 1 97  ? 7.564   29.911  1.006   1.00 80.14  ? 97  GLY B CA   1 
ATOM   5725  C C    . GLY B 1 97  ? 8.606   29.473  0.002   1.00 83.21  ? 97  GLY B C    1 
ATOM   5726  O O    . GLY B 1 97  ? 9.053   30.299  -0.804  1.00 81.39  ? 97  GLY B O    1 
ATOM   5727  H H    . GLY B 1 97  ? 6.398   28.411  1.485   1.00 96.91  ? 97  GLY B H    1 
ATOM   5728  H HA2  . GLY B 1 97  ? 6.829   30.309  0.515   1.00 96.17  ? 97  GLY B HA2  1 
ATOM   5729  H HA3  . GLY B 1 97  ? 7.967   30.586  1.574   1.00 96.17  ? 97  GLY B HA3  1 
ATOM   5730  N N    . GLU B 1 98  ? 9.013   28.210  0.032   1.00 87.26  ? 98  GLU B N    1 
ATOM   5731  C CA   . GLU B 1 98  ? 9.933   27.633  -0.933  1.00 85.65  ? 98  GLU B CA   1 
ATOM   5732  C C    . GLU B 1 98  ? 9.312   26.345  -1.452  1.00 89.14  ? 98  GLU B C    1 
ATOM   5733  O O    . GLU B 1 98  ? 8.779   25.544  -0.677  1.00 86.46  ? 98  GLU B O    1 
ATOM   5734  C CB   . GLU B 1 98  ? 11.304  27.351  -0.305  1.00 87.89  ? 98  GLU B CB   1 
ATOM   5735  C CG   . GLU B 1 98  ? 12.332  26.793  -1.276  1.00 90.42  ? 98  GLU B CG   1 
ATOM   5736  C CD   . GLU B 1 98  ? 12.760  27.804  -2.324  1.00 94.34  ? 98  GLU B CD   1 
ATOM   5737  O OE1  . GLU B 1 98  ? 12.834  29.007  -1.993  1.00 93.57  ? 98  GLU B OE1  1 
ATOM   5738  O OE2  . GLU B 1 98  ? 13.020  27.398  -3.478  1.00 96.51  ? 98  GLU B OE2  1 
ATOM   5739  H H    . GLU B 1 98  ? 8.759   27.646  0.629   1.00 104.72 ? 98  GLU B H    1 
ATOM   5740  H HA   . GLU B 1 98  ? 10.078  28.239  -1.675  1.00 102.78 ? 98  GLU B HA   1 
ATOM   5741  H HB2  . GLU B 1 98  ? 11.658  28.181  0.052   1.00 105.47 ? 98  GLU B HB2  1 
ATOM   5742  H HB3  . GLU B 1 98  ? 11.192  26.704  0.408   1.00 105.47 ? 98  GLU B HB3  1 
ATOM   5743  H HG2  . GLU B 1 98  ? 13.121  26.524  -0.780  1.00 108.50 ? 98  GLU B HG2  1 
ATOM   5744  H HG3  . GLU B 1 98  ? 11.951  26.029  -1.735  1.00 108.50 ? 98  GLU B HG3  1 
ATOM   5745  N N    . SER B 1 99  ? 9.368   26.157  -2.768  1.00 91.29  ? 99  SER B N    1 
ATOM   5746  C CA   . SER B 1 99  ? 8.747   24.998  -3.391  1.00 91.32  ? 99  SER B CA   1 
ATOM   5747  C C    . SER B 1 99  ? 9.696   23.820  -3.540  1.00 93.11  ? 99  SER B C    1 
ATOM   5748  O O    . SER B 1 99  ? 9.231   22.691  -3.731  1.00 97.74  ? 99  SER B O    1 
ATOM   5749  C CB   . SER B 1 99  ? 8.204   25.373  -4.771  1.00 93.51  ? 99  SER B CB   1 
ATOM   5750  O OG   . SER B 1 99  ? 9.249   25.858  -5.596  1.00 93.18  ? 99  SER B OG   1 
ATOM   5751  H H    . SER B 1 99  ? 9.761   26.688  -3.319  1.00 109.54 ? 99  SER B H    1 
ATOM   5752  H HA   . SER B 1 99  ? 8.003   24.713  -2.838  1.00 109.59 ? 99  SER B HA   1 
ATOM   5753  H HB2  . SER B 1 99  ? 7.813   24.587  -5.183  1.00 112.21 ? 99  SER B HB2  1 
ATOM   5754  H HB3  . SER B 1 99  ? 7.532   26.065  -4.671  1.00 112.21 ? 99  SER B HB3  1 
ATOM   5755  H HG   . SER B 1 99  ? 8.945   26.066  -6.351  1.00 111.81 ? 99  SER B HG   1 
ATOM   5756  N N    . LYS B 1 100 ? 11.002  24.049  -3.458  1.00 91.41  ? 100 LYS B N    1 
ATOM   5757  C CA   . LYS B 1 100 ? 11.989  23.000  -3.666  1.00 91.66  ? 100 LYS B CA   1 
ATOM   5758  C C    . LYS B 1 100 ? 12.490  22.473  -2.326  1.00 92.70  ? 100 LYS B C    1 
ATOM   5759  O O    . LYS B 1 100 ? 12.703  23.239  -1.380  1.00 91.06  ? 100 LYS B O    1 
ATOM   5760  C CB   . LYS B 1 100 ? 13.175  23.510  -4.489  1.00 97.26  ? 100 LYS B CB   1 
ATOM   5761  C CG   . LYS B 1 100 ? 13.148  23.183  -5.999  1.00 101.05 ? 100 LYS B CG   1 
ATOM   5762  C CD   . LYS B 1 100 ? 12.624  21.776  -6.352  1.00 102.68 ? 100 LYS B CD   1 
ATOM   5763  C CE   . LYS B 1 100 ? 13.276  20.667  -5.522  1.00 100.22 ? 100 LYS B CE   1 
ATOM   5764  N NZ   . LYS B 1 100 ? 12.482  19.395  -5.547  1.00 97.95  ? 100 LYS B NZ   1 
ATOM   5765  H H    . LYS B 1 100 ? 11.346  24.817  -3.280  1.00 109.69 ? 100 LYS B H    1 
ATOM   5766  H HA   . LYS B 1 100 ? 11.573  22.269  -4.150  1.00 109.99 ? 100 LYS B HA   1 
ATOM   5767  H HB2  . LYS B 1 100 ? 13.206  24.476  -4.407  1.00 116.72 ? 100 LYS B HB2  1 
ATOM   5768  H HB3  . LYS B 1 100 ? 13.985  23.120  -4.126  1.00 116.72 ? 100 LYS B HB3  1 
ATOM   5769  H HG2  . LYS B 1 100 ? 12.574  23.826  -6.443  1.00 121.26 ? 100 LYS B HG2  1 
ATOM   5770  H HG3  . LYS B 1 100 ? 14.052  23.251  -6.345  1.00 121.26 ? 100 LYS B HG3  1 
ATOM   5771  H HD2  . LYS B 1 100 ? 11.668  21.747  -6.191  1.00 123.22 ? 100 LYS B HD2  1 
ATOM   5772  H HD3  . LYS B 1 100 ? 12.809  21.597  -7.287  1.00 123.22 ? 100 LYS B HD3  1 
ATOM   5773  H HE2  . LYS B 1 100 ? 14.157  20.478  -5.880  1.00 120.26 ? 100 LYS B HE2  1 
ATOM   5774  H HE3  . LYS B 1 100 ? 13.347  20.959  -4.600  1.00 120.26 ? 100 LYS B HE3  1 
ATOM   5775  H HZ1  . LYS B 1 100 ? 12.874  18.781  -5.036  1.00 117.54 ? 100 LYS B HZ1  1 
ATOM   5776  H HZ2  . LYS B 1 100 ? 11.659  19.543  -5.241  1.00 117.54 ? 100 LYS B HZ2  1 
ATOM   5777  H HZ3  . LYS B 1 100 ? 12.428  19.085  -6.380  1.00 117.54 ? 100 LYS B HZ3  1 
ATOM   5778  N N    . VAL B 1 101 ? 12.674  21.155  -2.256  1.00 92.65  ? 101 VAL B N    1 
ATOM   5779  C CA   . VAL B 1 101 ? 13.305  20.545  -1.095  1.00 87.80  ? 101 VAL B CA   1 
ATOM   5780  C C    . VAL B 1 101 ? 14.681  21.157  -0.886  1.00 86.77  ? 101 VAL B C    1 
ATOM   5781  O O    . VAL B 1 101 ? 15.505  21.203  -1.809  1.00 89.39  ? 101 VAL B O    1 
ATOM   5782  C CB   . VAL B 1 101 ? 13.397  19.024  -1.285  1.00 84.93  ? 101 VAL B CB   1 
ATOM   5783  C CG1  . VAL B 1 101 ? 14.334  18.417  -0.242  1.00 89.04  ? 101 VAL B CG1  1 
ATOM   5784  C CG2  . VAL B 1 101 ? 12.013  18.398  -1.218  1.00 82.93  ? 101 VAL B CG2  1 
ATOM   5785  H H    . VAL B 1 101 ? 12.443  20.595  -2.867  1.00 111.18 ? 101 VAL B H    1 
ATOM   5786  H HA   . VAL B 1 101 ? 12.766  20.727  -0.309  1.00 105.36 ? 101 VAL B HA   1 
ATOM   5787  H HB   . VAL B 1 101 ? 13.765  18.831  -2.162  1.00 101.92 ? 101 VAL B HB   1 
ATOM   5788  H HG11 . VAL B 1 101 ? 14.176  17.462  -0.194  1.00 106.84 ? 101 VAL B HG11 1 
ATOM   5789  H HG12 . VAL B 1 101 ? 15.252  18.587  -0.505  1.00 106.84 ? 101 VAL B HG12 1 
ATOM   5790  H HG13 . VAL B 1 101 ? 14.155  18.827  0.619   1.00 106.84 ? 101 VAL B HG13 1 
ATOM   5791  H HG21 . VAL B 1 101 ? 12.094  17.439  -1.343  1.00 99.51  ? 101 VAL B HG21 1 
ATOM   5792  H HG22 . VAL B 1 101 ? 11.623  18.586  -0.350  1.00 99.51  ? 101 VAL B HG22 1 
ATOM   5793  H HG23 . VAL B 1 101 ? 11.460  18.777  -1.918  1.00 99.51  ? 101 VAL B HG23 1 
ATOM   5794  N N    . LEU B 1 102 ? 14.942  21.618  0.335   1.00 85.33  ? 102 LEU B N    1 
ATOM   5795  C CA   . LEU B 1 102 ? 16.209  22.251  0.676   1.00 85.09  ? 102 LEU B CA   1 
ATOM   5796  C C    . LEU B 1 102 ? 17.165  21.206  1.242   1.00 83.22  ? 102 LEU B C    1 
ATOM   5797  O O    . LEU B 1 102 ? 16.840  20.526  2.220   1.00 83.93  ? 102 LEU B O    1 
ATOM   5798  C CB   . LEU B 1 102 ? 15.992  23.376  1.687   1.00 85.62  ? 102 LEU B CB   1 
ATOM   5799  C CG   . LEU B 1 102 ? 15.029  24.482  1.252   1.00 86.94  ? 102 LEU B CG   1 
ATOM   5800  C CD1  . LEU B 1 102 ? 14.196  24.969  2.433   1.00 84.45  ? 102 LEU B CD1  1 
ATOM   5801  C CD2  . LEU B 1 102 ? 15.789  25.633  0.603   1.00 83.89  ? 102 LEU B CD2  1 
ATOM   5802  H H    . LEU B 1 102 ? 14.390  21.574  0.993   1.00 102.40 ? 102 LEU B H    1 
ATOM   5803  H HA   . LEU B 1 102 ? 16.606  22.626  -0.126  1.00 102.11 ? 102 LEU B HA   1 
ATOM   5804  H HB2  . LEU B 1 102 ? 15.636  22.988  2.501   1.00 102.75 ? 102 LEU B HB2  1 
ATOM   5805  H HB3  . LEU B 1 102 ? 16.849  23.793  1.866   1.00 102.75 ? 102 LEU B HB3  1 
ATOM   5806  H HG   . LEU B 1 102 ? 14.417  24.125  0.590   1.00 104.33 ? 102 LEU B HG   1 
ATOM   5807  H HD11 . LEU B 1 102 ? 13.598  25.670  2.130   1.00 101.35 ? 102 LEU B HD11 1 
ATOM   5808  H HD12 . LEU B 1 102 ? 13.682  24.226  2.785   1.00 101.35 ? 102 LEU B HD12 1 
ATOM   5809  H HD13 . LEU B 1 102 ? 14.790  25.314  3.118   1.00 101.35 ? 102 LEU B HD13 1 
ATOM   5810  H HD21 . LEU B 1 102 ? 15.156  26.316  0.331   1.00 100.67 ? 102 LEU B HD21 1 
ATOM   5811  H HD22 . LEU B 1 102 ? 16.415  26.001  1.247   1.00 100.67 ? 102 LEU B HD22 1 
ATOM   5812  H HD23 . LEU B 1 102 ? 16.269  25.299  -0.171  1.00 100.67 ? 102 LEU B HD23 1 
ATOM   5813  N N    . ASP B 1 103 ? 18.342  21.088  0.631   1.00 85.63  ? 103 ASP B N    1 
ATOM   5814  C CA   . ASP B 1 103 ? 19.363  20.127  1.045   1.00 84.44  ? 103 ASP B CA   1 
ATOM   5815  C C    . ASP B 1 103 ? 20.391  20.866  1.897   1.00 84.79  ? 103 ASP B C    1 
ATOM   5816  O O    . ASP B 1 103 ? 21.320  21.484  1.371   1.00 85.77  ? 103 ASP B O    1 
ATOM   5817  C CB   . ASP B 1 103 ? 20.004  19.478  -0.177  1.00 85.49  ? 103 ASP B CB   1 
ATOM   5818  C CG   . ASP B 1 103 ? 21.175  18.587  0.184   1.00 88.66  ? 103 ASP B CG   1 
ATOM   5819  O OD1  . ASP B 1 103 ? 21.098  17.896  1.221   1.00 88.33  ? 103 ASP B OD1  1 
ATOM   5820  O OD2  . ASP B 1 103 ? 22.173  18.578  -0.572  1.00 92.53  ? 103 ASP B OD2  1 
ATOM   5821  H H    . ASP B 1 103 ? 18.579  21.567  -0.043  1.00 102.76 ? 103 ASP B H    1 
ATOM   5822  H HA   . ASP B 1 103 ? 18.959  19.434  1.589   1.00 101.33 ? 103 ASP B HA   1 
ATOM   5823  H HB2  . ASP B 1 103 ? 19.341  18.934  -0.630  1.00 102.58 ? 103 ASP B HB2  1 
ATOM   5824  H HB3  . ASP B 1 103 ? 20.327  20.172  -0.772  1.00 102.58 ? 103 ASP B HB3  1 
ATOM   5825  N N    . VAL B 1 104 ? 20.226  20.791  3.220   1.00 84.20  ? 104 VAL B N    1 
ATOM   5826  C CA   . VAL B 1 104 ? 21.046  21.549  4.160   1.00 79.30  ? 104 VAL B CA   1 
ATOM   5827  C C    . VAL B 1 104 ? 22.235  20.705  4.596   1.00 76.29  ? 104 VAL B C    1 
ATOM   5828  O O    . VAL B 1 104 ? 22.070  19.556  5.025   1.00 75.04  ? 104 VAL B O    1 
ATOM   5829  C CB   . VAL B 1 104 ? 20.217  21.989  5.381   1.00 82.11  ? 104 VAL B CB   1 
ATOM   5830  C CG1  . VAL B 1 104 ? 20.949  23.077  6.166   1.00 74.26  ? 104 VAL B CG1  1 
ATOM   5831  C CG2  . VAL B 1 104 ? 18.832  22.461  4.957   1.00 80.57  ? 104 VAL B CG2  1 
ATOM   5832  H H    . VAL B 1 104 ? 19.633  20.298  3.602   1.00 101.05 ? 104 VAL B H    1 
ATOM   5833  H HA   . VAL B 1 104 ? 21.385  22.337  3.707   1.00 95.16  ? 104 VAL B HA   1 
ATOM   5834  H HB   . VAL B 1 104 ? 20.102  21.225  5.967   1.00 98.53  ? 104 VAL B HB   1 
ATOM   5835  H HG11 . VAL B 1 104 ? 20.432  23.298  6.956   1.00 89.11  ? 104 VAL B HG11 1 
ATOM   5836  H HG12 . VAL B 1 104 ? 21.823  22.745  6.425   1.00 89.11  ? 104 VAL B HG12 1 
ATOM   5837  H HG13 . VAL B 1 104 ? 21.046  23.861  5.604   1.00 89.11  ? 104 VAL B HG13 1 
ATOM   5838  H HG21 . VAL B 1 104 ? 18.405  22.901  5.709   1.00 96.69  ? 104 VAL B HG21 1 
ATOM   5839  H HG22 . VAL B 1 104 ? 18.922  23.082  4.218   1.00 96.69  ? 104 VAL B HG22 1 
ATOM   5840  H HG23 . VAL B 1 104 ? 18.308  21.693  4.682   1.00 96.69  ? 104 VAL B HG23 1 
ATOM   5841  N N    . ASP B 1 105 ? 23.433  21.287  4.505   1.00 75.11  ? 105 ASP B N    1 
ATOM   5842  C CA   . ASP B 1 105 ? 24.664  20.630  4.939   1.00 75.08  ? 105 ASP B CA   1 
ATOM   5843  C C    . ASP B 1 105 ? 24.961  21.044  6.375   1.00 76.94  ? 105 ASP B C    1 
ATOM   5844  O O    . ASP B 1 105 ? 25.298  22.204  6.641   1.00 73.87  ? 105 ASP B O    1 
ATOM   5845  C CB   . ASP B 1 105 ? 25.825  21.001  4.023   1.00 75.17  ? 105 ASP B CB   1 
ATOM   5846  C CG   . ASP B 1 105 ? 27.131  20.345  4.440   1.00 78.81  ? 105 ASP B CG   1 
ATOM   5847  O OD1  . ASP B 1 105 ? 27.087  19.409  5.270   1.00 79.07  ? 105 ASP B OD1  1 
ATOM   5848  O OD2  . ASP B 1 105 ? 28.200  20.762  3.933   1.00 77.39  ? 105 ASP B OD2  1 
ATOM   5849  H H    . ASP B 1 105 ? 23.559  22.077  4.189   1.00 90.13  ? 105 ASP B H    1 
ATOM   5850  H HA   . ASP B 1 105 ? 24.538  19.669  4.910   1.00 90.09  ? 105 ASP B HA   1 
ATOM   5851  H HB2  . ASP B 1 105 ? 25.620  20.713  3.119   1.00 90.21  ? 105 ASP B HB2  1 
ATOM   5852  H HB3  . ASP B 1 105 ? 25.951  21.962  4.044   1.00 90.21  ? 105 ASP B HB3  1 
ATOM   5853  N N    . VAL B 1 106 ? 24.839  20.097  7.300   1.00 78.68  ? 106 VAL B N    1 
ATOM   5854  C CA   . VAL B 1 106 ? 25.023  20.344  8.725   1.00 75.74  ? 106 VAL B CA   1 
ATOM   5855  C C    . VAL B 1 106 ? 26.341  19.713  9.149   1.00 76.29  ? 106 VAL B C    1 
ATOM   5856  O O    . VAL B 1 106 ? 26.632  18.564  8.792   1.00 77.03  ? 106 VAL B O    1 
ATOM   5857  C CB   . VAL B 1 106 ? 23.843  19.788  9.542   1.00 78.34  ? 106 VAL B CB   1 
ATOM   5858  C CG1  . VAL B 1 106 ? 24.094  19.954  11.036  1.00 75.50  ? 106 VAL B CG1  1 
ATOM   5859  C CG2  . VAL B 1 106 ? 22.544  20.482  9.122   1.00 76.18  ? 106 VAL B CG2  1 
ATOM   5860  H H    . VAL B 1 106 ? 24.644  19.279  7.120   1.00 94.41  ? 106 VAL B H    1 
ATOM   5861  H HA   . VAL B 1 106 ? 25.081  21.298  8.889   1.00 90.89  ? 106 VAL B HA   1 
ATOM   5862  H HB   . VAL B 1 106 ? 23.751  18.839  9.365   1.00 94.01  ? 106 VAL B HB   1 
ATOM   5863  H HG11 . VAL B 1 106 ? 23.271  19.774  11.517  1.00 90.60  ? 106 VAL B HG11 1 
ATOM   5864  H HG12 . VAL B 1 106 ? 24.782  19.327  11.312  1.00 90.60  ? 106 VAL B HG12 1 
ATOM   5865  H HG13 . VAL B 1 106 ? 24.386  20.863  11.208  1.00 90.60  ? 106 VAL B HG13 1 
ATOM   5866  H HG21 . VAL B 1 106 ? 21.817  20.149  9.671   1.00 91.42  ? 106 VAL B HG21 1 
ATOM   5867  H HG22 . VAL B 1 106 ? 22.643  21.439  9.247   1.00 91.42  ? 106 VAL B HG22 1 
ATOM   5868  H HG23 . VAL B 1 106 ? 22.370  20.287  8.188   1.00 91.42  ? 106 VAL B HG23 1 
ATOM   5869  N N    . ARG B 1 107 ? 27.141  20.471  9.895   1.00 76.15  ? 107 ARG B N    1 
ATOM   5870  C CA   . ARG B 1 107 ? 28.403  19.990  10.435  1.00 81.18  ? 107 ARG B CA   1 
ATOM   5871  C C    . ARG B 1 107 ? 28.503  20.355  11.911  1.00 82.07  ? 107 ARG B C    1 
ATOM   5872  O O    . ARG B 1 107 ? 27.980  21.381  12.355  1.00 76.56  ? 107 ARG B O    1 
ATOM   5873  C CB   . ARG B 1 107 ? 29.603  20.580  9.676   1.00 77.99  ? 107 ARG B CB   1 
ATOM   5874  C CG   . ARG B 1 107 ? 29.671  20.206  8.200   1.00 79.67  ? 107 ARG B CG   1 
ATOM   5875  C CD   . ARG B 1 107 ? 30.042  21.415  7.333   1.00 70.06  ? 107 ARG B CD   1 
ATOM   5876  N NE   . ARG B 1 107 ? 28.890  22.281  7.115   1.00 66.00  ? 107 ARG B NE   1 
ATOM   5877  C CZ   . ARG B 1 107 ? 28.955  23.593  6.939   1.00 68.14  ? 107 ARG B CZ   1 
ATOM   5878  N NH1  . ARG B 1 107 ? 30.113  24.233  6.922   1.00 66.71  ? 107 ARG B NH1  1 
ATOM   5879  N NH2  . ARG B 1 107 ? 27.828  24.281  6.767   1.00 72.66  ? 107 ARG B NH2  1 
ATOM   5880  H H    . ARG B 1 107 ? 26.968  21.286  10.106  1.00 91.38  ? 107 ARG B H    1 
ATOM   5881  H HA   . ARG B 1 107 ? 28.439  19.024  10.357  1.00 97.41  ? 107 ARG B HA   1 
ATOM   5882  H HB2  . ARG B 1 107 ? 29.556  21.547  9.730   1.00 93.60  ? 107 ARG B HB2  1 
ATOM   5883  H HB3  . ARG B 1 107 ? 30.418  20.262  10.095  1.00 93.60  ? 107 ARG B HB3  1 
ATOM   5884  H HG2  . ARG B 1 107 ? 30.344  19.520  8.072   1.00 95.60  ? 107 ARG B HG2  1 
ATOM   5885  H HG3  . ARG B 1 107 ? 28.804  19.879  7.911   1.00 95.60  ? 107 ARG B HG3  1 
ATOM   5886  H HD2  . ARG B 1 107 ? 30.733  21.930  7.778   1.00 84.07  ? 107 ARG B HD2  1 
ATOM   5887  H HD3  . ARG B 1 107 ? 30.362  21.107  6.471   1.00 84.07  ? 107 ARG B HD3  1 
ATOM   5888  H HE   . ARG B 1 107 ? 28.113  21.914  7.100   1.00 79.20  ? 107 ARG B HE   1 
ATOM   5889  H HH11 . ARG B 1 107 ? 30.846  23.797  7.027   1.00 80.05  ? 107 ARG B HH11 1 
ATOM   5890  H HH12 . ARG B 1 107 ? 30.131  25.085  6.806   1.00 80.05  ? 107 ARG B HH12 1 
ATOM   5891  H HH21 . ARG B 1 107 ? 27.070  23.873  6.772   1.00 87.20  ? 107 ARG B HH21 1 
ATOM   5892  H HH22 . ARG B 1 107 ? 27.857  25.132  6.652   1.00 87.20  ? 107 ARG B HH22 1 
ATOM   5893  N N    . ASN B 1 108 ? 29.176  19.498  12.672  1.00 85.20  ? 108 ASN B N    1 
ATOM   5894  C CA   . ASN B 1 108 ? 29.420  19.785  14.079  1.00 84.05  ? 108 ASN B CA   1 
ATOM   5895  C C    . ASN B 1 108 ? 30.355  20.982  14.201  1.00 85.11  ? 108 ASN B C    1 
ATOM   5896  O O    . ASN B 1 108 ? 31.304  21.130  13.427  1.00 87.45  ? 108 ASN B O    1 
ATOM   5897  C CB   . ASN B 1 108 ? 30.019  18.565  14.777  1.00 86.60  ? 108 ASN B CB   1 
ATOM   5898  C CG   . ASN B 1 108 ? 30.854  18.938  15.983  1.00 87.01  ? 108 ASN B CG   1 
ATOM   5899  O OD1  . ASN B 1 108 ? 32.069  19.111  15.879  1.00 87.49  ? 108 ASN B OD1  1 
ATOM   5900  N ND2  . ASN B 1 108 ? 30.206  19.070  17.136  1.00 84.68  ? 108 ASN B ND2  1 
ATOM   5901  H H    . ASN B 1 108 ? 29.500  18.750  12.399  1.00 102.24 ? 108 ASN B H    1 
ATOM   5902  H HA   . ASN B 1 108 ? 28.585  19.994  14.525  1.00 100.86 ? 108 ASN B HA   1 
ATOM   5903  H HB2  . ASN B 1 108 ? 29.300  17.986  15.077  1.00 103.92 ? 108 ASN B HB2  1 
ATOM   5904  H HB3  . ASN B 1 108 ? 30.588  18.089  14.152  1.00 103.92 ? 108 ASN B HB3  1 
ATOM   5905  H HD21 . ASN B 1 108 ? 29.356  18.945  17.168  1.00 101.61 ? 108 ASN B HD21 1 
ATOM   5906  H HD22 . ASN B 1 108 ? 30.637  19.282  17.849  1.00 101.61 ? 108 ASN B HD22 1 
ATOM   5907  N N    . ASP B 1 109 ? 30.076  21.850  15.176  1.00 82.82  ? 109 ASP B N    1 
ATOM   5908  C CA   . ASP B 1 109 ? 30.798  23.108  15.336  1.00 81.44  ? 109 ASP B CA   1 
ATOM   5909  C C    . ASP B 1 109 ? 31.435  23.215  16.719  1.00 83.36  ? 109 ASP B C    1 
ATOM   5910  O O    . ASP B 1 109 ? 31.577  24.312  17.263  1.00 82.17  ? 109 ASP B O    1 
ATOM   5911  C CB   . ASP B 1 109 ? 29.865  24.292  15.077  1.00 79.99  ? 109 ASP B CB   1 
ATOM   5912  C CG   . ASP B 1 109 ? 30.597  25.624  15.050  1.00 84.04  ? 109 ASP B CG   1 
ATOM   5913  O OD1  . ASP B 1 109 ? 31.806  25.633  14.735  1.00 81.36  ? 109 ASP B OD1  1 
ATOM   5914  O OD2  . ASP B 1 109 ? 29.962  26.660  15.355  1.00 88.50  ? 109 ASP B OD2  1 
ATOM   5915  H H    . ASP B 1 109 ? 29.462  21.728  15.766  1.00 99.38  ? 109 ASP B H    1 
ATOM   5916  H HA   . ASP B 1 109 ? 31.516  23.140  14.684  1.00 97.73  ? 109 ASP B HA   1 
ATOM   5917  H HB2  . ASP B 1 109 ? 29.432  24.170  14.218  1.00 95.99  ? 109 ASP B HB2  1 
ATOM   5918  H HB3  . ASP B 1 109 ? 29.200  24.329  15.782  1.00 95.99  ? 109 ASP B HB3  1 
ATOM   5919  N N    . GLY B 1 110 ? 31.832  22.081  17.291  1.00 84.17  ? 110 GLY B N    1 
ATOM   5920  C CA   . GLY B 1 110 ? 32.470  22.066  18.592  1.00 82.07  ? 110 GLY B CA   1 
ATOM   5921  C C    . GLY B 1 110 ? 31.701  21.248  19.606  1.00 83.75  ? 110 GLY B C    1 
ATOM   5922  O O    . GLY B 1 110 ? 31.906  20.037  19.729  1.00 84.33  ? 110 GLY B O    1 
ATOM   5923  H H    . GLY B 1 110 ? 31.739  21.302  16.938  1.00 101.00 ? 110 GLY B H    1 
ATOM   5924  H HA2  . GLY B 1 110 ? 33.360  21.689  18.507  1.00 98.49  ? 110 GLY B HA2  1 
ATOM   5925  H HA3  . GLY B 1 110 ? 32.542  22.974  18.924  1.00 98.49  ? 110 GLY B HA3  1 
ATOM   5926  N N    . ALA B 1 111 ? 30.809  21.903  20.339  1.00 84.48  ? 111 ALA B N    1 
ATOM   5927  C CA   . ALA B 1 111 ? 29.959  21.214  21.294  1.00 82.08  ? 111 ALA B CA   1 
ATOM   5928  C C    . ALA B 1 111 ? 28.853  20.451  20.570  1.00 78.89  ? 111 ALA B C    1 
ATOM   5929  O O    . ALA B 1 111 ? 28.518  20.731  19.416  1.00 79.19  ? 111 ALA B O    1 
ATOM   5930  C CB   . ALA B 1 111 ? 29.352  22.207  22.284  1.00 80.89  ? 111 ALA B CB   1 
ATOM   5931  H H    . ALA B 1 111 ? 30.678  22.752  20.300  1.00 101.38 ? 111 ALA B H    1 
ATOM   5932  H HA   . ALA B 1 111 ? 30.489  20.575  21.797  1.00 98.50  ? 111 ALA B HA   1 
ATOM   5933  H HB1  . ALA B 1 111 ? 28.798  21.723  22.917  1.00 97.07  ? 111 ALA B HB1  1 
ATOM   5934  H HB2  . ALA B 1 111 ? 30.067  22.664  22.753  1.00 97.07  ? 111 ALA B HB2  1 
ATOM   5935  H HB3  . ALA B 1 111 ? 28.813  22.849  21.796  1.00 97.07  ? 111 ALA B HB3  1 
ATOM   5936  N N    . LYS B 1 112 ? 28.281  19.473  21.273  1.00 80.50  ? 112 LYS B N    1 
ATOM   5937  C CA   . LYS B 1 112 ? 27.232  18.638  20.702  1.00 75.63  ? 112 LYS B CA   1 
ATOM   5938  C C    . LYS B 1 112 ? 25.939  19.402  20.451  1.00 71.24  ? 112 LYS B C    1 
ATOM   5939  O O    . LYS B 1 112 ? 25.005  18.828  19.880  1.00 70.25  ? 112 LYS B O    1 
ATOM   5940  C CB   . LYS B 1 112 ? 26.954  17.445  21.621  1.00 77.17  ? 112 LYS B CB   1 
ATOM   5941  C CG   . LYS B 1 112 ? 28.197  16.663  22.029  1.00 83.47  ? 112 LYS B CG   1 
ATOM   5942  C CD   . LYS B 1 112 ? 28.267  15.302  21.340  1.00 84.36  ? 112 LYS B CD   1 
ATOM   5943  C CE   . LYS B 1 112 ? 28.889  14.252  22.261  1.00 89.90  ? 112 LYS B CE   1 
ATOM   5944  N NZ   . LYS B 1 112 ? 29.430  13.080  21.509  1.00 91.97  ? 112 LYS B NZ   1 
ATOM   5945  H H    . LYS B 1 112 ? 28.484  19.274  22.085  1.00 96.60  ? 112 LYS B H    1 
ATOM   5946  H HA   . LYS B 1 112 ? 27.544  18.295  19.850  1.00 90.75  ? 112 LYS B HA   1 
ATOM   5947  H HB2  . LYS B 1 112 ? 26.532  17.770  22.432  1.00 92.61  ? 112 LYS B HB2  1 
ATOM   5948  H HB3  . LYS B 1 112 ? 26.359  16.832  21.161  1.00 92.61  ? 112 LYS B HB3  1 
ATOM   5949  H HG2  . LYS B 1 112 ? 28.987  17.168  21.782  1.00 100.16 ? 112 LYS B HG2  1 
ATOM   5950  H HG3  . LYS B 1 112 ? 28.182  16.517  22.988  1.00 100.16 ? 112 LYS B HG3  1 
ATOM   5951  H HD2  . LYS B 1 112 ? 27.372  15.012  21.105  1.00 101.23 ? 112 LYS B HD2  1 
ATOM   5952  H HD3  . LYS B 1 112 ? 28.814  15.372  20.542  1.00 101.23 ? 112 LYS B HD3  1 
ATOM   5953  H HE2  . LYS B 1 112 ? 29.619  14.656  22.755  1.00 107.88 ? 112 LYS B HE2  1 
ATOM   5954  H HE3  . LYS B 1 112 ? 28.212  13.929  22.876  1.00 107.88 ? 112 LYS B HE3  1 
ATOM   5955  H HZ1  . LYS B 1 112 ? 29.779  12.490  22.076  1.00 110.36 ? 112 LYS B HZ1  1 
ATOM   5956  H HZ2  . LYS B 1 112 ? 28.778  12.688  21.048  1.00 110.36 ? 112 LYS B HZ2  1 
ATOM   5957  H HZ3  . LYS B 1 112 ? 30.064  13.347  20.944  1.00 110.36 ? 112 LYS B HZ3  1 
ATOM   5958  N N    . ASN B 1 113 ? 25.851  20.662  20.874  1.00 72.20  ? 113 ASN B N    1 
ATOM   5959  C CA   . ASN B 1 113 ? 24.723  21.520  20.539  1.00 73.71  ? 113 ASN B CA   1 
ATOM   5960  C C    . ASN B 1 113 ? 25.110  22.640  19.581  1.00 73.48  ? 113 ASN B C    1 
ATOM   5961  O O    . ASN B 1 113 ? 24.260  23.474  19.245  1.00 72.49  ? 113 ASN B O    1 
ATOM   5962  C CB   . ASN B 1 113 ? 24.106  22.116  21.809  1.00 73.68  ? 113 ASN B CB   1 
ATOM   5963  C CG   . ASN B 1 113 ? 25.044  23.065  22.524  1.00 73.55  ? 113 ASN B CG   1 
ATOM   5964  O OD1  . ASN B 1 113 ? 26.231  22.779  22.683  1.00 74.67  ? 113 ASN B OD1  1 
ATOM   5965  N ND2  . ASN B 1 113 ? 24.514  24.201  22.963  1.00 73.08  ? 113 ASN B ND2  1 
ATOM   5966  H H    . ASN B 1 113 ? 26.444  21.047  21.365  1.00 86.64  ? 113 ASN B H    1 
ATOM   5967  H HA   . ASN B 1 113 ? 24.039  20.981  20.112  1.00 88.45  ? 113 ASN B HA   1 
ATOM   5968  H HB2  . ASN B 1 113 ? 23.305  22.608  21.571  1.00 88.41  ? 113 ASN B HB2  1 
ATOM   5969  H HB3  . ASN B 1 113 ? 23.884  21.396  22.421  1.00 88.41  ? 113 ASN B HB3  1 
ATOM   5970  H HD21 . ASN B 1 113 ? 25.005  24.773  23.375  1.00 87.70  ? 113 ASN B HD21 1 
ATOM   5971  H HD22 . ASN B 1 113 ? 23.679  24.364  22.835  1.00 87.70  ? 113 ASN B HD22 1 
ATOM   5972  N N    . LYS B 1 114 ? 26.363  22.678  19.132  1.00 73.65  ? 114 LYS B N    1 
ATOM   5973  C CA   . LYS B 1 114 ? 26.849  23.685  18.202  1.00 77.25  ? 114 LYS B CA   1 
ATOM   5974  C C    . LYS B 1 114 ? 26.983  23.081  16.810  1.00 76.41  ? 114 LYS B C    1 
ATOM   5975  O O    . LYS B 1 114 ? 27.504  21.972  16.648  1.00 76.83  ? 114 LYS B O    1 
ATOM   5976  C CB   . LYS B 1 114 ? 28.198  24.238  18.662  1.00 79.41  ? 114 LYS B CB   1 
ATOM   5977  C CG   . LYS B 1 114 ? 28.111  25.365  19.679  1.00 77.83  ? 114 LYS B CG   1 
ATOM   5978  C CD   . LYS B 1 114 ? 29.424  26.137  19.731  1.00 82.79  ? 114 LYS B CD   1 
ATOM   5979  C CE   . LYS B 1 114 ? 29.456  27.127  20.884  1.00 86.65  ? 114 LYS B CE   1 
ATOM   5980  N NZ   . LYS B 1 114 ? 28.097  27.421  21.417  1.00 86.31  ? 114 LYS B NZ   1 
ATOM   5981  H H    . LYS B 1 114 ? 26.967  22.111  19.362  1.00 88.38  ? 114 LYS B H    1 
ATOM   5982  H HA   . LYS B 1 114 ? 26.218  24.420  18.156  1.00 92.70  ? 114 LYS B HA   1 
ATOM   5983  H HB2  . LYS B 1 114 ? 28.703  23.516  19.069  1.00 95.30  ? 114 LYS B HB2  1 
ATOM   5984  H HB3  . LYS B 1 114 ? 28.671  24.579  17.888  1.00 95.30  ? 114 LYS B HB3  1 
ATOM   5985  H HG2  . LYS B 1 114 ? 27.402  25.977  19.426  1.00 93.39  ? 114 LYS B HG2  1 
ATOM   5986  H HG3  . LYS B 1 114 ? 27.933  24.997  20.558  1.00 93.39  ? 114 LYS B HG3  1 
ATOM   5987  H HD2  . LYS B 1 114 ? 30.158  25.513  19.847  1.00 99.34  ? 114 LYS B HD2  1 
ATOM   5988  H HD3  . LYS B 1 114 ? 29.537  26.631  18.904  1.00 99.34  ? 114 LYS B HD3  1 
ATOM   5989  H HE2  . LYS B 1 114 ? 29.989  26.757  21.605  1.00 103.98 ? 114 LYS B HE2  1 
ATOM   5990  H HE3  . LYS B 1 114 ? 29.847  27.960  20.577  1.00 103.98 ? 114 LYS B HE3  1 
ATOM   5991  H HZ1  . LYS B 1 114 ? 28.139  28.085  22.009  1.00 103.57 ? 114 LYS B HZ1  1 
ATOM   5992  H HZ2  . LYS B 1 114 ? 27.555  27.661  20.753  1.00 103.57 ? 114 LYS B HZ2  1 
ATOM   5993  H HZ3  . LYS B 1 114 ? 27.763  26.699  21.817  1.00 103.57 ? 114 LYS B HZ3  1 
ATOM   5994  N N    . PHE B 1 115 ? 26.515  23.818  15.806  1.00 77.61  ? 115 PHE B N    1 
ATOM   5995  C CA   . PHE B 1 115 ? 26.509  23.330  14.438  1.00 75.21  ? 115 PHE B CA   1 
ATOM   5996  C C    . PHE B 1 115 ? 26.823  24.465  13.475  1.00 74.19  ? 115 PHE B C    1 
ATOM   5997  O O    . PHE B 1 115 ? 26.758  25.645  13.827  1.00 71.10  ? 115 PHE B O    1 
ATOM   5998  C CB   . PHE B 1 115 ? 25.149  22.719  14.059  1.00 73.40  ? 115 PHE B CB   1 
ATOM   5999  C CG   . PHE B 1 115 ? 24.741  21.569  14.921  1.00 73.71  ? 115 PHE B CG   1 
ATOM   6000  C CD1  . PHE B 1 115 ? 25.191  20.291  14.648  1.00 76.93  ? 115 PHE B CD1  1 
ATOM   6001  C CD2  . PHE B 1 115 ? 23.904  21.763  16.007  1.00 76.30  ? 115 PHE B CD2  1 
ATOM   6002  C CE1  . PHE B 1 115 ? 24.816  19.227  15.444  1.00 76.66  ? 115 PHE B CE1  1 
ATOM   6003  C CE2  . PHE B 1 115 ? 23.525  20.703  16.805  1.00 73.72  ? 115 PHE B CE2  1 
ATOM   6004  C CZ   . PHE B 1 115 ? 23.981  19.436  16.525  1.00 74.30  ? 115 PHE B CZ   1 
ATOM   6005  H H    . PHE B 1 115 ? 26.193  24.610  15.897  1.00 93.13  ? 115 PHE B H    1 
ATOM   6006  H HA   . PHE B 1 115 ? 27.200  22.656  14.353  1.00 90.26  ? 115 PHE B HA   1 
ATOM   6007  H HB2  . PHE B 1 115 ? 24.467  23.404  14.138  1.00 88.08  ? 115 PHE B HB2  1 
ATOM   6008  H HB3  . PHE B 1 115 ? 25.195  22.401  13.144  1.00 88.08  ? 115 PHE B HB3  1 
ATOM   6009  H HD1  . PHE B 1 115 ? 25.751  20.146  13.920  1.00 92.32  ? 115 PHE B HD1  1 
ATOM   6010  H HD2  . PHE B 1 115 ? 23.594  22.618  16.201  1.00 91.56  ? 115 PHE B HD2  1 
ATOM   6011  H HE1  . PHE B 1 115 ? 25.126  18.371  15.253  1.00 91.99  ? 115 PHE B HE1  1 
ATOM   6012  H HE2  . PHE B 1 115 ? 22.962  20.846  17.531  1.00 88.46  ? 115 PHE B HE2  1 
ATOM   6013  H HZ   . PHE B 1 115 ? 23.728  18.721  17.063  1.00 89.16  ? 115 PHE B HZ   1 
ATOM   6014  N N    . LEU B 1 116 ? 27.179  24.076  12.248  1.00 77.42  ? 116 LEU B N    1 
ATOM   6015  C CA   . LEU B 1 116 ? 27.226  24.961  11.092  1.00 72.77  ? 116 LEU B CA   1 
ATOM   6016  C C    . LEU B 1 116 ? 26.224  24.436  10.073  1.00 72.72  ? 116 LEU B C    1 
ATOM   6017  O O    . LEU B 1 116 ? 26.231  23.241  9.758   1.00 76.31  ? 116 LEU B O    1 
ATOM   6018  C CB   . LEU B 1 116 ? 28.617  25.011  10.472  1.00 69.61  ? 116 LEU B CB   1 
ATOM   6019  C CG   . LEU B 1 116 ? 29.699  25.765  11.240  1.00 73.07  ? 116 LEU B CG   1 
ATOM   6020  C CD1  . LEU B 1 116 ? 31.011  25.711  10.470  1.00 68.26  ? 116 LEU B CD1  1 
ATOM   6021  C CD2  . LEU B 1 116 ? 29.290  27.201  11.506  1.00 73.33  ? 116 LEU B CD2  1 
ATOM   6022  H H    . LEU B 1 116 ? 27.407  23.269  12.058  1.00 92.91  ? 116 LEU B H    1 
ATOM   6023  H HA   . LEU B 1 116 ? 26.991  25.865  11.354  1.00 87.32  ? 116 LEU B HA   1 
ATOM   6024  H HB2  . LEU B 1 116 ? 28.930  24.099  10.369  1.00 83.53  ? 116 LEU B HB2  1 
ATOM   6025  H HB3  . LEU B 1 116 ? 28.541  25.436  9.604   1.00 83.53  ? 116 LEU B HB3  1 
ATOM   6026  H HG   . LEU B 1 116 ? 29.827  25.341  12.103  1.00 87.69  ? 116 LEU B HG   1 
ATOM   6027  H HD11 . LEU B 1 116 ? 31.698  26.165  10.983  1.00 81.92  ? 116 LEU B HD11 1 
ATOM   6028  H HD12 . LEU B 1 116 ? 31.260  24.783  10.334  1.00 81.92  ? 116 LEU B HD12 1 
ATOM   6029  H HD13 . LEU B 1 116 ? 30.893  26.151  9.613   1.00 81.92  ? 116 LEU B HD13 1 
ATOM   6030  H HD21 . LEU B 1 116 ? 30.060  27.777  11.380  1.00 88.00  ? 116 LEU B HD21 1 
ATOM   6031  H HD22 . LEU B 1 116 ? 28.587  27.449  10.885  1.00 88.00  ? 116 LEU B HD22 1 
ATOM   6032  H HD23 . LEU B 1 116 ? 28.967  27.274  12.417  1.00 88.00  ? 116 LEU B HD23 1 
ATOM   6033  N N    . ALA B 1 117 ? 25.367  25.316  9.561   1.00 71.48  ? 117 ALA B N    1 
ATOM   6034  C CA   . ALA B 1 117 ? 24.302  24.930  8.641   1.00 72.18  ? 117 ALA B CA   1 
ATOM   6035  C C    . ALA B 1 117 ? 24.430  25.737  7.358   1.00 76.44  ? 117 ALA B C    1 
ATOM   6036  O O    . ALA B 1 117 ? 24.437  26.973  7.401   1.00 76.05  ? 117 ALA B O    1 
ATOM   6037  C CB   . ALA B 1 117 ? 22.924  25.150  9.274   1.00 70.00  ? 117 ALA B CB   1 
ATOM   6038  H H    . ALA B 1 117 ? 25.384  26.158  9.735   1.00 85.78  ? 117 ALA B H    1 
ATOM   6039  H HA   . ALA B 1 117 ? 24.398  23.991  8.420   1.00 86.61  ? 117 ALA B HA   1 
ATOM   6040  H HB1  . ALA B 1 117 ? 22.239  24.900  8.633   1.00 84.00  ? 117 ALA B HB1  1 
ATOM   6041  H HB2  . ALA B 1 117 ? 22.850  24.599  10.069  1.00 84.00  ? 117 ALA B HB2  1 
ATOM   6042  H HB3  . ALA B 1 117 ? 22.830  26.086  9.510   1.00 84.00  ? 117 ALA B HB3  1 
ATOM   6043  N N    . LYS B 1 118 ? 24.524  25.037  6.225   1.00 73.39  ? 118 LYS B N    1 
ATOM   6044  C CA   . LYS B 1 118 ? 24.593  25.647  4.902   1.00 77.38  ? 118 LYS B CA   1 
ATOM   6045  C C    . LYS B 1 118 ? 23.333  25.291  4.121   1.00 77.52  ? 118 LYS B C    1 
ATOM   6046  O O    . LYS B 1 118 ? 22.962  24.114  4.039   1.00 76.27  ? 118 LYS B O    1 
ATOM   6047  C CB   . LYS B 1 118 ? 25.834  25.173  4.139   1.00 76.76  ? 118 LYS B CB   1 
ATOM   6048  C CG   . LYS B 1 118 ? 25.909  25.656  2.694   1.00 78.01  ? 118 LYS B CG   1 
ATOM   6049  C CD   . LYS B 1 118 ? 27.019  24.942  1.925   1.00 84.90  ? 118 LYS B CD   1 
ATOM   6050  C CE   . LYS B 1 118 ? 28.368  25.626  2.106   1.00 87.67  ? 118 LYS B CE   1 
ATOM   6051  N NZ   . LYS B 1 118 ? 29.205  25.516  0.869   1.00 103.16 ? 118 LYS B NZ   1 
ATOM   6052  H H    . LYS B 1 118 ? 24.551  24.178  6.200   1.00 88.07  ? 118 LYS B H    1 
ATOM   6053  H HA   . LYS B 1 118 ? 24.641  26.612  4.992   1.00 92.85  ? 118 LYS B HA   1 
ATOM   6054  H HB2  . LYS B 1 118 ? 26.623  25.499  4.599   1.00 92.11  ? 118 LYS B HB2  1 
ATOM   6055  H HB3  . LYS B 1 118 ? 25.836  24.203  4.125   1.00 92.11  ? 118 LYS B HB3  1 
ATOM   6056  H HG2  . LYS B 1 118 ? 25.066  25.475  2.251   1.00 93.61  ? 118 LYS B HG2  1 
ATOM   6057  H HG3  . LYS B 1 118 ? 26.094  26.608  2.683   1.00 93.61  ? 118 LYS B HG3  1 
ATOM   6058  H HD2  . LYS B 1 118 ? 27.096  24.030  2.247   1.00 101.89 ? 118 LYS B HD2  1 
ATOM   6059  H HD3  . LYS B 1 118 ? 26.803  24.943  0.979   1.00 101.89 ? 118 LYS B HD3  1 
ATOM   6060  H HE2  . LYS B 1 118 ? 28.229  26.566  2.298   1.00 105.21 ? 118 LYS B HE2  1 
ATOM   6061  H HE3  . LYS B 1 118 ? 28.847  25.205  2.837   1.00 105.21 ? 118 LYS B HE3  1 
ATOM   6062  H HZ1  . LYS B 1 118 ? 29.989  25.917  0.995   1.00 123.79 ? 118 LYS B HZ1  1 
ATOM   6063  H HZ2  . LYS B 1 118 ? 29.347  24.659  0.673   1.00 123.79 ? 118 LYS B HZ2  1 
ATOM   6064  H HZ3  . LYS B 1 118 ? 28.789  25.903  0.184   1.00 123.79 ? 118 LYS B HZ3  1 
ATOM   6065  N N    . ILE B 1 119 ? 22.700  26.301  3.524   1.00 78.20  ? 119 ILE B N    1 
ATOM   6066  C CA   . ILE B 1 119 ? 21.416  26.142  2.852   1.00 77.47  ? 119 ILE B CA   1 
ATOM   6067  C C    . ILE B 1 119 ? 21.427  26.932  1.553   1.00 78.57  ? 119 ILE B C    1 
ATOM   6068  O O    . ILE B 1 119 ? 22.043  27.998  1.460   1.00 79.19  ? 119 ILE B O    1 
ATOM   6069  C CB   . ILE B 1 119 ? 20.256  26.605  3.766   1.00 76.85  ? 119 ILE B CB   1 
ATOM   6070  C CG1  . ILE B 1 119 ? 18.904  26.362  3.100   1.00 77.33  ? 119 ILE B CG1  1 
ATOM   6071  C CG2  . ILE B 1 119 ? 20.415  28.085  4.131   1.00 74.66  ? 119 ILE B CG2  1 
ATOM   6072  C CD1  . ILE B 1 119 ? 17.718  26.726  3.984   1.00 76.74  ? 119 ILE B CD1  1 
ATOM   6073  H H    . ILE B 1 119 ? 23.003  27.105  3.496   1.00 93.84  ? 119 ILE B H    1 
ATOM   6074  H HA   . ILE B 1 119 ? 21.285  25.209  2.622   1.00 92.97  ? 119 ILE B HA   1 
ATOM   6075  H HB   . ILE B 1 119 ? 20.291  26.078  4.580   1.00 92.22  ? 119 ILE B HB   1 
ATOM   6076  H HG12 . ILE B 1 119 ? 18.851  26.899  2.295   1.00 92.79  ? 119 ILE B HG12 1 
ATOM   6077  H HG13 . ILE B 1 119 ? 18.830  25.421  2.876   1.00 92.79  ? 119 ILE B HG13 1 
ATOM   6078  H HG21 . ILE B 1 119 ? 19.780  28.308  4.829   1.00 89.59  ? 119 ILE B HG21 1 
ATOM   6079  H HG22 . ILE B 1 119 ? 21.319  28.237  4.445   1.00 89.59  ? 119 ILE B HG22 1 
ATOM   6080  H HG23 . ILE B 1 119 ? 20.243  28.624  3.343   1.00 89.59  ? 119 ILE B HG23 1 
ATOM   6081  H HD11 . ILE B 1 119 ? 16.906  26.383  3.581   1.00 92.08  ? 119 ILE B HD11 1 
ATOM   6082  H HD12 . ILE B 1 119 ? 17.845  26.330  4.861   1.00 92.08  ? 119 ILE B HD12 1 
ATOM   6083  H HD13 . ILE B 1 119 ? 17.667  27.692  4.062   1.00 92.08  ? 119 ILE B HD13 1 
ATOM   6084  N N    . LYS B 1 120 ? 20.740  26.394  0.540   1.00 82.96  ? 120 LYS B N    1 
ATOM   6085  C CA   . LYS B 1 120 ? 20.580  27.087  -0.733  1.00 79.19  ? 120 LYS B CA   1 
ATOM   6086  C C    . LYS B 1 120 ? 19.554  28.203  -0.590  1.00 80.53  ? 120 LYS B C    1 
ATOM   6087  O O    . LYS B 1 120 ? 18.431  27.967  -0.130  1.00 82.31  ? 120 LYS B O    1 
ATOM   6088  C CB   . LYS B 1 120 ? 20.122  26.125  -1.827  1.00 85.79  ? 120 LYS B CB   1 
ATOM   6089  C CG   . LYS B 1 120 ? 19.550  26.819  -3.084  1.00 91.02  ? 120 LYS B CG   1 
ATOM   6090  C CD   . LYS B 1 120 ? 18.037  27.083  -2.982  1.00 92.24  ? 120 LYS B CD   1 
ATOM   6091  C CE   . LYS B 1 120 ? 17.409  27.373  -4.359  1.00 95.14  ? 120 LYS B CE   1 
ATOM   6092  N NZ   . LYS B 1 120 ? 16.089  28.074  -4.243  1.00 92.16  ? 120 LYS B NZ   1 
ATOM   6093  H H    . LYS B 1 120 ? 20.357  25.625  0.569   1.00 99.55  ? 120 LYS B H    1 
ATOM   6094  H HA   . LYS B 1 120 ? 21.435  27.463  -0.991  1.00 95.02  ? 120 LYS B HA   1 
ATOM   6095  H HB2  . LYS B 1 120 ? 20.881  25.589  -2.106  1.00 102.95 ? 120 LYS B HB2  1 
ATOM   6096  H HB3  . LYS B 1 120 ? 19.427  25.553  -1.465  1.00 102.95 ? 120 LYS B HB3  1 
ATOM   6097  H HG2  . LYS B 1 120 ? 19.996  27.672  -3.205  1.00 109.23 ? 120 LYS B HG2  1 
ATOM   6098  H HG3  . LYS B 1 120 ? 19.704  26.252  -3.856  1.00 109.23 ? 120 LYS B HG3  1 
ATOM   6099  H HD2  . LYS B 1 120 ? 17.600  26.302  -2.608  1.00 110.69 ? 120 LYS B HD2  1 
ATOM   6100  H HD3  . LYS B 1 120 ? 17.885  27.853  -2.412  1.00 110.69 ? 120 LYS B HD3  1 
ATOM   6101  H HE2  . LYS B 1 120 ? 18.009  27.939  -4.869  1.00 114.17 ? 120 LYS B HE2  1 
ATOM   6102  H HE3  . LYS B 1 120 ? 17.266  26.535  -4.826  1.00 114.17 ? 120 LYS B HE3  1 
ATOM   6103  H HZ1  . LYS B 1 120 ? 16.194  28.855  -3.830  1.00 110.59 ? 120 LYS B HZ1  1 
ATOM   6104  H HZ2  . LYS B 1 120 ? 15.519  27.574  -3.777  1.00 110.59 ? 120 LYS B HZ2  1 
ATOM   6105  H HZ3  . LYS B 1 120 ? 15.750  28.219  -5.053  1.00 110.59 ? 120 LYS B HZ3  1 
ATOM   6106  N N    . MET B 1 121 ? 19.917  29.404  -1.029  1.00 83.38  ? 121 MET B N    1 
ATOM   6107  C CA   . MET B 1 121 ? 19.006  30.533  -0.903  1.00 84.38  ? 121 MET B CA   1 
ATOM   6108  C C    . MET B 1 121 ? 18.363  30.867  -2.245  1.00 86.72  ? 121 MET B C    1 
ATOM   6109  O O    . MET B 1 121 ? 18.924  30.569  -3.306  1.00 88.46  ? 121 MET B O    1 
ATOM   6110  C CB   . MET B 1 121 ? 19.750  31.759  -0.369  1.00 83.38  ? 121 MET B CB   1 
ATOM   6111  C CG   . MET B 1 121 ? 20.319  31.563  1.039   1.00 81.46  ? 121 MET B CG   1 
ATOM   6112  S SD   . MET B 1 121 ? 19.055  31.588  2.333   1.00 75.98  ? 121 MET B SD   1 
ATOM   6113  C CE   . MET B 1 121 ? 18.549  33.307  2.303   1.00 73.15  ? 121 MET B CE   1 
ATOM   6114  H H    . MET B 1 121 ? 20.672  29.587  -1.397  1.00 100.06 ? 121 MET B H    1 
ATOM   6115  H HA   . MET B 1 121 ? 18.304  30.311  -0.271  1.00 101.26 ? 121 MET B HA   1 
ATOM   6116  H HB2  . MET B 1 121 ? 20.490  31.958  -0.964  1.00 100.06 ? 121 MET B HB2  1 
ATOM   6117  H HB3  . MET B 1 121 ? 19.136  32.509  -0.340  1.00 100.06 ? 121 MET B HB3  1 
ATOM   6118  H HG2  . MET B 1 121 ? 20.769  30.704  1.080   1.00 97.75  ? 121 MET B HG2  1 
ATOM   6119  H HG3  . MET B 1 121 ? 20.950  32.276  1.225   1.00 97.75  ? 121 MET B HG3  1 
ATOM   6120  H HE1  . MET B 1 121 ? 17.935  33.468  3.038   1.00 87.78  ? 121 MET B HE1  1 
ATOM   6121  H HE2  . MET B 1 121 ? 19.333  33.869  2.398   1.00 87.78  ? 121 MET B HE2  1 
ATOM   6122  H HE3  . MET B 1 121 ? 18.109  33.492  1.459   1.00 87.78  ? 121 MET B HE3  1 
ATOM   6123  N N    . PRO B 1 122 ? 17.175  31.472  -2.231  1.00 87.20  ? 122 PRO B N    1 
ATOM   6124  C CA   . PRO B 1 122 ? 16.524  31.830  -3.497  1.00 85.07  ? 122 PRO B CA   1 
ATOM   6125  C C    . PRO B 1 122 ? 17.358  32.817  -4.301  1.00 86.65  ? 122 PRO B C    1 
ATOM   6126  O O    . PRO B 1 122 ? 18.236  33.508  -3.779  1.00 82.84  ? 122 PRO B O    1 
ATOM   6127  C CB   . PRO B 1 122 ? 15.190  32.454  -3.057  1.00 82.56  ? 122 PRO B CB   1 
ATOM   6128  C CG   . PRO B 1 122 ? 15.389  32.836  -1.620  1.00 86.93  ? 122 PRO B CG   1 
ATOM   6129  C CD   . PRO B 1 122 ? 16.356  31.830  -1.057  1.00 81.65  ? 122 PRO B CD   1 
ATOM   6130  H HA   . PRO B 1 122 ? 16.354  31.037  -4.030  1.00 102.08 ? 122 PRO B HA   1 
ATOM   6131  H HB2  . PRO B 1 122 ? 14.997  33.235  -3.599  1.00 99.08  ? 122 PRO B HB2  1 
ATOM   6132  H HB3  . PRO B 1 122 ? 14.477  31.803  -3.147  1.00 99.08  ? 122 PRO B HB3  1 
ATOM   6133  H HG2  . PRO B 1 122 ? 15.756  33.732  -1.567  1.00 104.31 ? 122 PRO B HG2  1 
ATOM   6134  H HG3  . PRO B 1 122 ? 14.541  32.797  -1.151  1.00 104.31 ? 122 PRO B HG3  1 
ATOM   6135  H HD2  . PRO B 1 122 ? 16.902  32.226  -0.360  1.00 97.98  ? 122 PRO B HD2  1 
ATOM   6136  H HD3  . PRO B 1 122 ? 15.887  31.054  -0.711  1.00 97.98  ? 122 PRO B HD3  1 
ATOM   6137  N N    . LYS B 1 123 ? 17.069  32.872  -5.599  1.00 92.61  ? 123 LYS B N    1 
ATOM   6138  C CA   . LYS B 1 123 ? 17.743  33.805  -6.486  1.00 91.16  ? 123 LYS B CA   1 
ATOM   6139  C C    . LYS B 1 123 ? 17.058  35.170  -6.444  1.00 92.69  ? 123 LYS B C    1 
ATOM   6140  O O    . LYS B 1 123 ? 15.871  35.293  -6.115  1.00 94.66  ? 123 LYS B O    1 
ATOM   6141  C CB   . LYS B 1 123 ? 17.748  33.298  -7.926  1.00 93.12  ? 123 LYS B CB   1 
ATOM   6142  C CG   . LYS B 1 123 ? 18.784  32.230  -8.256  1.00 101.95 ? 123 LYS B CG   1 
ATOM   6143  C CD   . LYS B 1 123 ? 20.091  32.402  -7.509  1.00 99.72  ? 123 LYS B CD   1 
ATOM   6144  C CE   . LYS B 1 123 ? 20.988  31.197  -7.723  1.00 103.47 ? 123 LYS B CE   1 
ATOM   6145  N NZ   . LYS B 1 123 ? 20.987  30.373  -6.481  1.00 101.63 ? 123 LYS B NZ   1 
ATOM   6146  H H    . LYS B 1 123 ? 16.483  32.377  -5.988  1.00 111.13 ? 123 LYS B H    1 
ATOM   6147  H HA   . LYS B 1 123 ? 18.663  33.897  -6.194  1.00 109.39 ? 123 LYS B HA   1 
ATOM   6148  H HB2  . LYS B 1 123 ? 16.876  32.920  -8.117  1.00 111.75 ? 123 LYS B HB2  1 
ATOM   6149  H HB3  . LYS B 1 123 ? 17.918  34.053  -8.512  1.00 111.75 ? 123 LYS B HB3  1 
ATOM   6150  H HG2  . LYS B 1 123 ? 18.423  31.360  -8.024  1.00 122.35 ? 123 LYS B HG2  1 
ATOM   6151  H HG3  . LYS B 1 123 ? 18.979  32.265  -9.206  1.00 122.35 ? 123 LYS B HG3  1 
ATOM   6152  H HD2  . LYS B 1 123 ? 20.551  33.191  -7.836  1.00 119.66 ? 123 LYS B HD2  1 
ATOM   6153  H HD3  . LYS B 1 123 ? 19.913  32.491  -6.560  1.00 119.66 ? 123 LYS B HD3  1 
ATOM   6154  H HE2  . LYS B 1 123 ? 20.652  30.661  -8.459  1.00 124.16 ? 123 LYS B HE2  1 
ATOM   6155  H HE3  . LYS B 1 123 ? 21.894  31.487  -7.910  1.00 124.16 ? 123 LYS B HE3  1 
ATOM   6156  H HZ1  . LYS B 1 123 ? 21.494  29.650  -6.595  1.00 121.96 ? 123 LYS B HZ1  1 
ATOM   6157  H HZ2  . LYS B 1 123 ? 21.310  30.848  -5.800  1.00 121.96 ? 123 LYS B HZ2  1 
ATOM   6158  H HZ3  . LYS B 1 123 ? 20.158  30.116  -6.286  1.00 121.96 ? 123 LYS B HZ3  1 
ATOM   6159  N N    . PHE B 1 124 ? 17.823  36.204  -6.789  1.00 91.40  ? 124 PHE B N    1 
ATOM   6160  C CA   . PHE B 1 124 ? 17.257  37.538  -6.927  1.00 92.60  ? 124 PHE B CA   1 
ATOM   6161  C C    . PHE B 1 124 ? 16.421  37.608  -8.198  1.00 89.45  ? 124 PHE B C    1 
ATOM   6162  O O    . PHE B 1 124 ? 16.659  36.880  -9.164  1.00 92.46  ? 124 PHE B O    1 
ATOM   6163  C CB   . PHE B 1 124 ? 18.358  38.608  -6.953  1.00 91.16  ? 124 PHE B CB   1 
ATOM   6164  C CG   . PHE B 1 124 ? 19.286  38.518  -8.136  1.00 85.14  ? 124 PHE B CG   1 
ATOM   6165  C CD1  . PHE B 1 124 ? 18.900  38.988  -9.382  1.00 94.07  ? 124 PHE B CD1  1 
ATOM   6166  C CD2  . PHE B 1 124 ? 20.554  37.973  -7.999  1.00 84.31  ? 124 PHE B CD2  1 
ATOM   6167  C CE1  . PHE B 1 124 ? 19.754  38.901  -10.477 1.00 85.57  ? 124 PHE B CE1  1 
ATOM   6168  C CE2  . PHE B 1 124 ? 21.413  37.888  -9.082  1.00 88.08  ? 124 PHE B CE2  1 
ATOM   6169  C CZ   . PHE B 1 124 ? 21.013  38.352  -10.324 1.00 83.36  ? 124 PHE B CZ   1 
ATOM   6170  H H    . PHE B 1 124 ? 18.667  36.157  -6.948  1.00 109.68 ? 124 PHE B H    1 
ATOM   6171  H HA   . PHE B 1 124 ? 16.690  37.735  -6.165  1.00 111.12 ? 124 PHE B HA   1 
ATOM   6172  H HB2  . PHE B 1 124 ? 17.940  39.483  -6.975  1.00 109.39 ? 124 PHE B HB2  1 
ATOM   6173  H HB3  . PHE B 1 124 ? 18.896  38.518  -6.151  1.00 109.39 ? 124 PHE B HB3  1 
ATOM   6174  H HD1  . PHE B 1 124 ? 18.058  39.367  -9.487  1.00 112.88 ? 124 PHE B HD1  1 
ATOM   6175  H HD2  . PHE B 1 124 ? 20.832  37.661  -7.168  1.00 101.17 ? 124 PHE B HD2  1 
ATOM   6176  H HE1  . PHE B 1 124 ? 19.478  39.211  -11.309 1.00 102.68 ? 124 PHE B HE1  1 
ATOM   6177  H HE2  . PHE B 1 124 ? 22.259  37.517  -8.976  1.00 105.69 ? 124 PHE B HE2  1 
ATOM   6178  H HZ   . PHE B 1 124 ? 21.589  38.296  -11.051 1.00 100.04 ? 124 PHE B HZ   1 
ATOM   6179  N N    . LEU B 1 125 ? 15.428  38.491  -8.192  1.00 90.61  ? 125 LEU B N    1 
ATOM   6180  C CA   . LEU B 1 125 ? 14.630  38.736  -9.385  1.00 95.90  ? 125 LEU B CA   1 
ATOM   6181  C C    . LEU B 1 125 ? 15.143  39.918  -10.200 1.00 92.92  ? 125 LEU B C    1 
ATOM   6182  O O    . LEU B 1 125 ? 14.743  40.072  -11.357 1.00 89.88  ? 125 LEU B O    1 
ATOM   6183  C CB   . LEU B 1 125 ? 13.167  38.977  -9.005  1.00 95.54  ? 125 LEU B CB   1 
ATOM   6184  C CG   . LEU B 1 125 ? 12.374  37.730  -8.614  1.00 97.94  ? 125 LEU B CG   1 
ATOM   6185  C CD1  . LEU B 1 125 ? 11.043  38.113  -7.984  1.00 99.91  ? 125 LEU B CD1  1 
ATOM   6186  C CD2  . LEU B 1 125 ? 12.154  36.835  -9.821  1.00 100.17 ? 125 LEU B CD2  1 
ATOM   6187  H H    . LEU B 1 125 ? 15.198  38.960  -7.509  1.00 108.73 ? 125 LEU B H    1 
ATOM   6188  H HA   . LEU B 1 125 ? 14.659  37.947  -9.948  1.00 115.08 ? 125 LEU B HA   1 
ATOM   6189  H HB2  . LEU B 1 125 ? 13.145  39.583  -8.248  1.00 114.65 ? 125 LEU B HB2  1 
ATOM   6190  H HB3  . LEU B 1 125 ? 12.717  39.379  -9.765  1.00 114.65 ? 125 LEU B HB3  1 
ATOM   6191  H HG   . LEU B 1 125 ? 12.884  37.230  -7.958  1.00 117.53 ? 125 LEU B HG   1 
ATOM   6192  H HD11 . LEU B 1 125 ? 10.560  37.305  -7.751  1.00 119.89 ? 125 LEU B HD11 1 
ATOM   6193  H HD12 . LEU B 1 125 ? 11.211  38.639  -7.186  1.00 119.89 ? 125 LEU B HD12 1 
ATOM   6194  H HD13 . LEU B 1 125 ? 10.530  38.633  -8.621  1.00 119.89 ? 125 LEU B HD13 1 
ATOM   6195  H HD21 . LEU B 1 125 ? 11.643  36.058  -9.549  1.00 120.21 ? 125 LEU B HD21 1 
ATOM   6196  H HD22 . LEU B 1 125 ? 11.666  37.331  -10.498 1.00 120.21 ? 125 LEU B HD22 1 
ATOM   6197  H HD23 . LEU B 1 125 ? 13.016  36.559  -10.171 1.00 120.21 ? 125 LEU B HD23 1 
ATOM   6198  N N    . SER B 1 126 ? 16.005  40.753  -9.623  1.00 95.08  ? 126 SER B N    1 
ATOM   6199  C CA   . SER B 1 126 ? 16.551  41.919  -10.302 1.00 87.77  ? 126 SER B CA   1 
ATOM   6200  C C    . SER B 1 126 ? 17.654  42.500  -9.431  1.00 90.24  ? 126 SER B C    1 
ATOM   6201  O O    . SER B 1 126 ? 17.537  42.508  -8.203  1.00 91.10  ? 126 SER B O    1 
ATOM   6202  C CB   . SER B 1 126 ? 15.473  42.979  -10.557 1.00 89.09  ? 126 SER B CB   1 
ATOM   6203  O OG   . SER B 1 126 ? 15.538  44.001  -9.570  1.00 91.96  ? 126 SER B OG   1 
ATOM   6204  H H    . SER B 1 126 ? 16.296  40.660  -8.819  1.00 114.09 ? 126 SER B H    1 
ATOM   6205  H HA   . SER B 1 126 ? 16.923  41.654  -11.158 1.00 105.32 ? 126 SER B HA   1 
ATOM   6206  H HB2  . SER B 1 126 ? 15.616  43.373  -11.431 1.00 106.91 ? 126 SER B HB2  1 
ATOM   6207  H HB3  . SER B 1 126 ? 14.599  42.559  -10.521 1.00 106.91 ? 126 SER B HB3  1 
ATOM   6208  H HG   . SER B 1 126 ? 14.949  44.581  -9.718  1.00 110.35 ? 126 SER B HG   1 
ATOM   6209  N N    . LEU B 1 127 ? 18.718  42.975  -10.071 1.00 87.24  ? 127 LEU B N    1 
ATOM   6210  C CA   . LEU B 1 127 ? 19.801  43.680  -9.396  1.00 88.29  ? 127 LEU B CA   1 
ATOM   6211  C C    . LEU B 1 127 ? 20.035  44.983  -10.143 1.00 94.71  ? 127 LEU B C    1 
ATOM   6212  O O    . LEU B 1 127 ? 20.363  44.968  -11.335 1.00 96.98  ? 127 LEU B O    1 
ATOM   6213  C CB   . LEU B 1 127 ? 21.074  42.836  -9.361  1.00 89.08  ? 127 LEU B CB   1 
ATOM   6214  C CG   . LEU B 1 127 ? 22.299  43.447  -8.687  1.00 92.10  ? 127 LEU B CG   1 
ATOM   6215  C CD1  . LEU B 1 127 ? 21.920  44.217  -7.435  1.00 89.97  ? 127 LEU B CD1  1 
ATOM   6216  C CD2  . LEU B 1 127 ? 23.316  42.359  -8.354  1.00 94.25  ? 127 LEU B CD2  1 
ATOM   6217  H H    . LEU B 1 127 ? 18.837  42.899  -10.919 1.00 104.69 ? 127 LEU B H    1 
ATOM   6218  H HA   . LEU B 1 127 ? 19.553  43.881  -8.480  1.00 105.95 ? 127 LEU B HA   1 
ATOM   6219  H HB2  . LEU B 1 127 ? 20.873  42.014  -8.887  1.00 106.90 ? 127 LEU B HB2  1 
ATOM   6220  H HB3  . LEU B 1 127 ? 21.326  42.638  -10.277 1.00 106.90 ? 127 LEU B HB3  1 
ATOM   6221  H HG   . LEU B 1 127 ? 22.706  44.076  -9.303  1.00 110.52 ? 127 LEU B HG   1 
ATOM   6222  H HD11 . LEU B 1 127 ? 22.714  44.353  -6.895  1.00 107.96 ? 127 LEU B HD11 1 
ATOM   6223  H HD12 . LEU B 1 127 ? 21.545  45.074  -7.692  1.00 107.96 ? 127 LEU B HD12 1 
ATOM   6224  H HD13 . LEU B 1 127 ? 21.265  43.706  -6.936  1.00 107.96 ? 127 LEU B HD13 1 
ATOM   6225  H HD21 . LEU B 1 127 ? 24.100  42.770  -7.956  1.00 113.09 ? 127 LEU B HD21 1 
ATOM   6226  H HD22 . LEU B 1 127 ? 22.917  41.735  -7.728  1.00 113.09 ? 127 LEU B HD22 1 
ATOM   6227  H HD23 . LEU B 1 127 ? 23.563  41.897  -9.170  1.00 113.09 ? 127 LEU B HD23 1 
ATOM   6228  N N    . GLU B 1 128 ? 19.847  46.105  -9.457  1.00 91.76  ? 128 GLU B N    1 
ATOM   6229  C CA   . GLU B 1 128 ? 19.989  47.407  -10.087 1.00 95.44  ? 128 GLU B CA   1 
ATOM   6230  C C    . GLU B 1 128 ? 20.530  48.400  -9.073  1.00 94.55  ? 128 GLU B C    1 
ATOM   6231  O O    . GLU B 1 128 ? 20.144  48.374  -7.902  1.00 93.58  ? 128 GLU B O    1 
ATOM   6232  C CB   . GLU B 1 128 ? 18.650  47.903  -10.648 1.00 98.47  ? 128 GLU B CB   1 
ATOM   6233  C CG   . GLU B 1 128 ? 17.584  48.153  -9.593  1.00 95.44  ? 128 GLU B CG   1 
ATOM   6234  C CD   . GLU B 1 128 ? 16.182  48.205  -10.176 1.00 100.04 ? 128 GLU B CD   1 
ATOM   6235  O OE1  . GLU B 1 128 ? 15.639  47.132  -10.513 1.00 102.37 ? 128 GLU B OE1  1 
ATOM   6236  O OE2  . GLU B 1 128 ? 15.620  49.318  -10.297 1.00 99.35  ? 128 GLU B OE2  1 
ATOM   6237  H H    . GLU B 1 128 ? 19.636  46.136  -8.624  1.00 110.11 ? 128 GLU B H    1 
ATOM   6238  H HA   . GLU B 1 128 ? 20.625  47.345  -10.816 1.00 114.53 ? 128 GLU B HA   1 
ATOM   6239  H HB2  . GLU B 1 128 ? 18.801  48.738  -11.117 1.00 118.17 ? 128 GLU B HB2  1 
ATOM   6240  H HB3  . GLU B 1 128 ? 18.305  47.235  -11.261 1.00 118.17 ? 128 GLU B HB3  1 
ATOM   6241  H HG2  . GLU B 1 128 ? 17.611  47.437  -8.940  1.00 114.52 ? 128 GLU B HG2  1 
ATOM   6242  H HG3  . GLU B 1 128 ? 17.761  49.003  -9.161  1.00 114.52 ? 128 GLU B HG3  1 
ATOM   6243  N N    . GLU B 1 129 ? 21.430  49.265  -9.532  1.00 97.90  ? 129 GLU B N    1 
ATOM   6244  C CA   . GLU B 1 129 ? 21.912  50.376  -8.726  1.00 96.01  ? 129 GLU B CA   1 
ATOM   6245  C C    . GLU B 1 129 ? 21.000  51.577  -8.942  1.00 95.89  ? 129 GLU B C    1 
ATOM   6246  O O    . GLU B 1 129 ? 20.739  51.969  -10.084 1.00 98.83  ? 129 GLU B O    1 
ATOM   6247  C CB   . GLU B 1 129 ? 23.351  50.737  -9.084  1.00 98.26  ? 129 GLU B CB   1 
ATOM   6248  C CG   . GLU B 1 129 ? 23.959  51.739  -8.122  1.00 103.30 ? 129 GLU B CG   1 
ATOM   6249  C CD   . GLU B 1 129 ? 25.460  51.604  -8.020  1.00 109.76 ? 129 GLU B CD   1 
ATOM   6250  O OE1  . GLU B 1 129 ? 25.938  50.544  -7.560  1.00 113.26 ? 129 GLU B OE1  1 
ATOM   6251  O OE2  . GLU B 1 129 ? 26.166  52.555  -8.415  1.00 112.14 ? 129 GLU B OE2  1 
ATOM   6252  H H    . GLU B 1 129 ? 21.780  49.228  -10.317 1.00 117.48 ? 129 GLU B H    1 
ATOM   6253  H HA   . GLU B 1 129 ? 21.897  50.127  -7.789  1.00 115.21 ? 129 GLU B HA   1 
ATOM   6254  H HB2  . GLU B 1 129 ? 23.892  49.933  -9.063  1.00 117.92 ? 129 GLU B HB2  1 
ATOM   6255  H HB3  . GLU B 1 129 ? 23.367  51.125  -9.973  1.00 117.92 ? 129 GLU B HB3  1 
ATOM   6256  H HG2  . GLU B 1 129 ? 23.759  52.637  -8.430  1.00 123.95 ? 129 GLU B HG2  1 
ATOM   6257  H HG3  . GLU B 1 129 ? 23.584  51.600  -7.239  1.00 123.95 ? 129 GLU B HG3  1 
ATOM   6258  N N    . ILE B 1 130 ? 20.520  52.151  -7.844  1.00 96.59  ? 130 ILE B N    1 
ATOM   6259  C CA   . ILE B 1 130 ? 19.598  53.275  -7.874  1.00 95.68  ? 130 ILE B CA   1 
ATOM   6260  C C    . ILE B 1 130 ? 20.286  54.484  -7.260  1.00 97.92  ? 130 ILE B C    1 
ATOM   6261  O O    . ILE B 1 130 ? 21.200  54.354  -6.439  1.00 97.91  ? 130 ILE B O    1 
ATOM   6262  C CB   . ILE B 1 130 ? 18.289  52.950  -7.125  1.00 96.97  ? 130 ILE B CB   1 
ATOM   6263  C CG1  . ILE B 1 130 ? 18.593  52.377  -5.740  1.00 95.11  ? 130 ILE B CG1  1 
ATOM   6264  C CG2  . ILE B 1 130 ? 17.457  51.958  -7.923  1.00 95.07  ? 130 ILE B CG2  1 
ATOM   6265  C CD1  . ILE B 1 130 ? 17.407  52.374  -4.801  1.00 95.77  ? 130 ILE B CD1  1 
ATOM   6266  H H    . ILE B 1 130 ? 20.721  51.898  -7.047  1.00 115.90 ? 130 ILE B H    1 
ATOM   6267  H HA   . ILE B 1 130 ? 19.379  53.489  -8.795  1.00 114.82 ? 130 ILE B HA   1 
ATOM   6268  H HB   . ILE B 1 130 ? 17.788  53.774  -7.020  1.00 116.37 ? 130 ILE B HB   1 
ATOM   6269  H HG12 . ILE B 1 130 ? 18.891  51.460  -5.841  1.00 114.13 ? 130 ILE B HG12 1 
ATOM   6270  H HG13 . ILE B 1 130 ? 19.292  52.910  -5.330  1.00 114.13 ? 130 ILE B HG13 1 
ATOM   6271  H HG21 . ILE B 1 130 ? 16.618  51.806  -7.461  1.00 114.08 ? 130 ILE B HG21 1 
ATOM   6272  H HG22 . ILE B 1 130 ? 17.287  52.325  -8.805  1.00 114.08 ? 130 ILE B HG22 1 
ATOM   6273  H HG23 . ILE B 1 130 ? 17.948  51.125  -8.001  1.00 114.08 ? 130 ILE B HG23 1 
ATOM   6274  H HD11 . ILE B 1 130 ? 17.694  52.054  -3.932  1.00 114.93 ? 130 ILE B HD11 1 
ATOM   6275  H HD12 . ILE B 1 130 ? 17.063  53.278  -4.724  1.00 114.93 ? 130 ILE B HD12 1 
ATOM   6276  H HD13 . ILE B 1 130 ? 16.722  51.789  -5.160  1.00 114.93 ? 130 ILE B HD13 1 
ATOM   6277  N N    . ASN B 1 131 ? 19.845  55.671  -7.676  1.00 99.34  ? 131 ASN B N    1 
ATOM   6278  C CA   . ASN B 1 131 ? 20.362  56.941  -7.169  1.00 98.26  ? 131 ASN B CA   1 
ATOM   6279  C C    . ASN B 1 131 ? 19.165  57.770  -6.711  1.00 98.07  ? 131 ASN B C    1 
ATOM   6280  O O    . ASN B 1 131 ? 18.431  58.316  -7.543  1.00 98.56  ? 131 ASN B O    1 
ATOM   6281  C CB   . ASN B 1 131 ? 21.174  57.677  -8.234  1.00 96.77  ? 131 ASN B CB   1 
ATOM   6282  C CG   . ASN B 1 131 ? 22.670  57.507  -8.049  1.00 98.95  ? 131 ASN B CG   1 
ATOM   6283  O OD1  . ASN B 1 131 ? 23.352  56.947  -8.903  1.00 104.13 ? 131 ASN B OD1  1 
ATOM   6284  N ND2  . ASN B 1 131 ? 23.186  57.992  -6.926  1.00 102.74 ? 131 ASN B ND2  1 
ATOM   6285  H H    . ASN B 1 131 ? 19.229  55.768  -8.269  1.00 119.20 ? 131 ASN B H    1 
ATOM   6286  H HA   . ASN B 1 131 ? 20.941  56.777  -6.408  1.00 117.92 ? 131 ASN B HA   1 
ATOM   6287  H HB2  . ASN B 1 131 ? 20.937  57.330  -9.108  1.00 116.13 ? 131 ASN B HB2  1 
ATOM   6288  H HB3  . ASN B 1 131 ? 20.971  58.625  -8.188  1.00 116.13 ? 131 ASN B HB3  1 
ATOM   6289  H HD21 . ASN B 1 131 ? 22.677  58.378  -6.351  1.00 123.29 ? 131 ASN B HD21 1 
ATOM   6290  H HD22 . ASN B 1 131 ? 24.030  57.920  -6.775  1.00 123.29 ? 131 ASN B HD22 1 
ATOM   6291  N N    . VAL B 1 132 ? 18.967  57.852  -5.395  1.00 99.28  ? 132 VAL B N    1 
ATOM   6292  C CA   . VAL B 1 132 ? 17.859  58.588  -4.797  1.00 98.50  ? 132 VAL B CA   1 
ATOM   6293  C C    . VAL B 1 132 ? 18.421  59.824  -4.116  1.00 101.21 ? 132 VAL B C    1 
ATOM   6294  O O    . VAL B 1 132 ? 19.388  59.727  -3.348  1.00 102.76 ? 132 VAL B O    1 
ATOM   6295  C CB   . VAL B 1 132 ? 17.083  57.723  -3.790  1.00 101.61 ? 132 VAL B CB   1 
ATOM   6296  C CG1  . VAL B 1 132 ? 16.439  58.595  -2.721  1.00 104.74 ? 132 VAL B CG1  1 
ATOM   6297  C CG2  . VAL B 1 132 ? 16.037  56.898  -4.508  1.00 103.52 ? 132 VAL B CG2  1 
ATOM   6298  H H    . VAL B 1 132 ? 19.478  57.477  -4.814  1.00 119.14 ? 132 VAL B H    1 
ATOM   6299  H HA   . VAL B 1 132 ? 17.248  58.867  -5.497  1.00 118.20 ? 132 VAL B HA   1 
ATOM   6300  H HB   . VAL B 1 132 ? 17.700  57.118  -3.350  1.00 121.93 ? 132 VAL B HB   1 
ATOM   6301  H HG11 . VAL B 1 132 ? 15.763  58.078  -2.257  1.00 125.68 ? 132 VAL B HG11 1 
ATOM   6302  H HG12 . VAL B 1 132 ? 17.122  58.883  -2.095  1.00 125.68 ? 132 VAL B HG12 1 
ATOM   6303  H HG13 . VAL B 1 132 ? 16.033  59.366  -3.146  1.00 125.68 ? 132 VAL B HG13 1 
ATOM   6304  H HG21 . VAL B 1 132 ? 15.580  56.337  -3.862  1.00 124.23 ? 132 VAL B HG21 1 
ATOM   6305  H HG22 . VAL B 1 132 ? 15.403  57.495  -4.935  1.00 124.23 ? 132 VAL B HG22 1 
ATOM   6306  H HG23 . VAL B 1 132 ? 16.474  56.347  -5.176  1.00 124.23 ? 132 VAL B HG23 1 
ATOM   6307  N N    . ASP B 1 133 ? 17.798  60.981  -4.374  1.00 103.36 ? 133 ASP B N    1 
ATOM   6308  C CA   . ASP B 1 133 ? 18.295  62.243  -3.833  1.00 100.95 ? 133 ASP B CA   1 
ATOM   6309  C C    . ASP B 1 133 ? 19.807  62.267  -4.028  1.00 100.53 ? 133 ASP B C    1 
ATOM   6310  O O    . ASP B 1 133 ? 20.280  62.053  -5.148  1.00 105.52 ? 133 ASP B O    1 
ATOM   6311  C CB   . ASP B 1 133 ? 17.853  62.399  -2.384  1.00 108.05 ? 133 ASP B CB   1 
ATOM   6312  C CG   . ASP B 1 133 ? 16.450  63.009  -2.278  1.00 111.03 ? 133 ASP B CG   1 
ATOM   6313  O OD1  . ASP B 1 133 ? 15.691  62.950  -3.277  1.00 115.72 ? 133 ASP B OD1  1 
ATOM   6314  O OD2  . ASP B 1 133 ? 16.114  63.549  -1.206  1.00 105.80 ? 133 ASP B OD2  1 
ATOM   6315  H H    . ASP B 1 133 ? 17.091  61.056  -4.857  1.00 124.03 ? 133 ASP B H    1 
ATOM   6316  H HA   . ASP B 1 133 ? 17.928  63.017  -4.288  1.00 121.14 ? 133 ASP B HA   1 
ATOM   6317  H HB2  . ASP B 1 133 ? 17.839  61.528  -1.958  1.00 129.66 ? 133 ASP B HB2  1 
ATOM   6318  H HB3  . ASP B 1 133 ? 18.474  62.984  -1.922  1.00 129.66 ? 133 ASP B HB3  1 
ATOM   6319  N N    . GLU B 1 134 ? 20.583  62.487  -2.968  1.00 103.44 ? 134 GLU B N    1 
ATOM   6320  C CA   . GLU B 1 134 ? 22.034  62.578  -3.086  1.00 102.67 ? 134 GLU B CA   1 
ATOM   6321  C C    . GLU B 1 134 ? 22.753  61.323  -2.591  1.00 103.42 ? 134 GLU B C    1 
ATOM   6322  O O    . GLU B 1 134 ? 23.875  61.414  -2.082  1.00 105.35 ? 134 GLU B O    1 
ATOM   6323  C CB   . GLU B 1 134 ? 22.549  63.812  -2.338  1.00 106.24 ? 134 GLU B CB   1 
ATOM   6324  C CG   . GLU B 1 134 ? 22.403  63.745  -0.824  1.00 108.07 ? 134 GLU B CG   1 
ATOM   6325  C CD   . GLU B 1 134 ? 21.071  64.288  -0.330  1.00 110.54 ? 134 GLU B CD   1 
ATOM   6326  O OE1  . GLU B 1 134 ? 20.055  64.061  -1.003  1.00 110.48 ? 134 GLU B OE1  1 
ATOM   6327  O OE2  . GLU B 1 134 ? 21.045  64.946  0.738   1.00 110.44 ? 134 GLU B OE2  1 
ATOM   6328  H H    . GLU B 1 134 ? 20.288  62.586  -2.166  1.00 124.13 ? 134 GLU B H    1 
ATOM   6329  H HA   . GLU B 1 134 ? 22.250  62.679  -4.026  1.00 123.21 ? 134 GLU B HA   1 
ATOM   6330  H HB2  . GLU B 1 134 ? 23.492  63.921  -2.536  1.00 127.49 ? 134 GLU B HB2  1 
ATOM   6331  H HB3  . GLU B 1 134 ? 22.054  64.587  -2.645  1.00 127.49 ? 134 GLU B HB3  1 
ATOM   6332  H HG2  . GLU B 1 134 ? 22.472  62.820  -0.541  1.00 129.68 ? 134 GLU B HG2  1 
ATOM   6333  H HG3  . GLU B 1 134 ? 23.109  64.270  -0.416  1.00 129.68 ? 134 GLU B HG3  1 
ATOM   6334  N N    . TYR B 1 135 ? 22.143  60.150  -2.737  1.00 100.98 ? 135 TYR B N    1 
ATOM   6335  C CA   . TYR B 1 135 ? 22.722  58.907  -2.248  1.00 101.85 ? 135 TYR B CA   1 
ATOM   6336  C C    . TYR B 1 135 ? 22.609  57.817  -3.307  1.00 103.33 ? 135 TYR B C    1 
ATOM   6337  O O    . TYR B 1 135 ? 21.627  57.762  -4.055  1.00 100.27 ? 135 TYR B O    1 
ATOM   6338  C CB   . TYR B 1 135 ? 22.029  58.452  -0.955  1.00 101.53 ? 135 TYR B CB   1 
ATOM   6339  C CG   . TYR B 1 135 ? 22.024  59.479  0.166   1.00 104.33 ? 135 TYR B CG   1 
ATOM   6340  C CD1  . TYR B 1 135 ? 23.146  59.675  0.963   1.00 104.35 ? 135 TYR B CD1  1 
ATOM   6341  C CD2  . TYR B 1 135 ? 20.892  60.240  0.434   1.00 105.68 ? 135 TYR B CD2  1 
ATOM   6342  C CE1  . TYR B 1 135 ? 23.143  60.607  1.989   1.00 106.13 ? 135 TYR B CE1  1 
ATOM   6343  C CE2  . TYR B 1 135 ? 20.880  61.173  1.456   1.00 107.50 ? 135 TYR B CE2  1 
ATOM   6344  C CZ   . TYR B 1 135 ? 22.006  61.354  2.230   1.00 108.04 ? 135 TYR B CZ   1 
ATOM   6345  O OH   . TYR B 1 135 ? 21.991  62.282  3.247   1.00 110.31 ? 135 TYR B OH   1 
ATOM   6346  H H    . TYR B 1 135 ? 21.382  60.049  -3.124  1.00 121.17 ? 135 TYR B H    1 
ATOM   6347  H HA   . TYR B 1 135 ? 23.666  59.043  -2.067  1.00 122.22 ? 135 TYR B HA   1 
ATOM   6348  H HB2  . TYR B 1 135 ? 21.105  58.241  -1.160  1.00 121.84 ? 135 TYR B HB2  1 
ATOM   6349  H HB3  . TYR B 1 135 ? 22.485  57.662  -0.624  1.00 121.84 ? 135 TYR B HB3  1 
ATOM   6350  H HD1  . TYR B 1 135 ? 23.912  59.173  0.804   1.00 125.22 ? 135 TYR B HD1  1 
ATOM   6351  H HD2  . TYR B 1 135 ? 20.129  60.120  -0.083  1.00 126.82 ? 135 TYR B HD2  1 
ATOM   6352  H HE1  . TYR B 1 135 ? 23.902  60.729  2.512   1.00 127.35 ? 135 TYR B HE1  1 
ATOM   6353  H HE2  . TYR B 1 135 ? 20.115  61.677  1.620   1.00 129.00 ? 135 TYR B HE2  1 
ATOM   6354  H HH   . TYR B 1 135 ? 21.248  62.674  3.267   1.00 132.37 ? 135 TYR B HH   1 
ATOM   6355  N N    . LYS B 1 136 ? 23.623  56.955  -3.371  1.00 103.12 ? 136 LYS B N    1 
ATOM   6356  C CA   . LYS B 1 136 ? 23.620  55.786  -4.246  1.00 97.02  ? 136 LYS B CA   1 
ATOM   6357  C C    . LYS B 1 136 ? 23.299  54.544  -3.421  1.00 97.57  ? 136 LYS B C    1 
ATOM   6358  O O    . LYS B 1 136 ? 23.943  54.289  -2.397  1.00 96.15  ? 136 LYS B O    1 
ATOM   6359  C CB   . LYS B 1 136 ? 24.966  55.639  -4.965  1.00 100.56 ? 136 LYS B CB   1 
ATOM   6360  C CG   . LYS B 1 136 ? 26.005  54.752  -4.279  1.00 105.94 ? 136 LYS B CG   1 
ATOM   6361  C CD   . LYS B 1 136 ? 27.251  54.565  -5.167  1.00 110.11 ? 136 LYS B CD   1 
ATOM   6362  C CE   . LYS B 1 136 ? 28.505  54.265  -4.341  1.00 110.46 ? 136 LYS B CE   1 
ATOM   6363  N NZ   . LYS B 1 136 ? 28.761  52.799  -4.172  1.00 105.70 ? 136 LYS B NZ   1 
ATOM   6364  H H    . LYS B 1 136 ? 24.341  57.028  -2.904  1.00 123.75 ? 136 LYS B H    1 
ATOM   6365  H HA   . LYS B 1 136 ? 22.935  55.881  -4.926  1.00 116.42 ? 136 LYS B HA   1 
ATOM   6366  H HB2  . LYS B 1 136 ? 24.800  55.258  -5.842  1.00 120.68 ? 136 LYS B HB2  1 
ATOM   6367  H HB3  . LYS B 1 136 ? 25.358  56.521  -5.055  1.00 120.68 ? 136 LYS B HB3  1 
ATOM   6368  H HG2  . LYS B 1 136 ? 26.282  55.165  -3.446  1.00 127.12 ? 136 LYS B HG2  1 
ATOM   6369  H HG3  . LYS B 1 136 ? 25.620  53.879  -4.104  1.00 127.12 ? 136 LYS B HG3  1 
ATOM   6370  H HD2  . LYS B 1 136 ? 27.102  53.822  -5.773  1.00 132.13 ? 136 LYS B HD2  1 
ATOM   6371  H HD3  . LYS B 1 136 ? 27.408  55.378  -5.672  1.00 132.13 ? 136 LYS B HD3  1 
ATOM   6372  H HE2  . LYS B 1 136 ? 29.275  54.653  -4.786  1.00 132.55 ? 136 LYS B HE2  1 
ATOM   6373  H HE3  . LYS B 1 136 ? 28.401  54.654  -3.458  1.00 132.55 ? 136 LYS B HE3  1 
ATOM   6374  H HZ1  . LYS B 1 136 ? 29.497  52.672  -3.687  1.00 126.84 ? 136 LYS B HZ1  1 
ATOM   6375  H HZ2  . LYS B 1 136 ? 28.073  52.415  -3.758  1.00 126.84 ? 136 LYS B HZ2  1 
ATOM   6376  H HZ3  . LYS B 1 136 ? 28.870  52.415  -4.967  1.00 126.84 ? 136 LYS B HZ3  1 
ATOM   6377  N N    . LEU B 1 137 ? 22.303  53.782  -3.866  1.00 97.80  ? 137 LEU B N    1 
ATOM   6378  C CA   . LEU B 1 137 ? 21.820  52.612  -3.149  1.00 96.20  ? 137 LEU B CA   1 
ATOM   6379  C C    . LEU B 1 137 ? 21.888  51.380  -4.044  1.00 98.10  ? 137 LEU B C    1 
ATOM   6380  O O    . LEU B 1 137 ? 21.918  51.476  -5.272  1.00 97.69  ? 137 LEU B O    1 
ATOM   6381  C CB   . LEU B 1 137 ? 20.367  52.797  -2.684  1.00 94.71  ? 137 LEU B CB   1 
ATOM   6382  C CG   . LEU B 1 137 ? 20.083  53.601  -1.416  1.00 92.07  ? 137 LEU B CG   1 
ATOM   6383  C CD1  . LEU B 1 137 ? 20.824  52.979  -0.252  1.00 89.31  ? 137 LEU B CD1  1 
ATOM   6384  C CD2  . LEU B 1 137 ? 20.452  55.061  -1.622  1.00 91.67  ? 137 LEU B CD2  1 
ATOM   6385  H H    . LEU B 1 137 ? 21.881  53.929  -4.600  1.00 117.36 ? 137 LEU B H    1 
ATOM   6386  H HA   . LEU B 1 137 ? 22.387  52.471  -2.375  1.00 115.43 ? 137 LEU B HA   1 
ATOM   6387  H HB2  . LEU B 1 137 ? 19.888  53.241  -3.402  1.00 113.66 ? 137 LEU B HB2  1 
ATOM   6388  H HB3  . LEU B 1 137 ? 19.996  51.913  -2.536  1.00 113.66 ? 137 LEU B HB3  1 
ATOM   6389  H HG   . LEU B 1 137 ? 19.136  53.583  -1.205  1.00 110.49 ? 137 LEU B HG   1 
ATOM   6390  H HD11 . LEU B 1 137 ? 20.540  53.410  0.570   1.00 107.17 ? 137 LEU B HD11 1 
ATOM   6391  H HD12 . LEU B 1 137 ? 20.619  52.032  -0.217  1.00 107.17 ? 137 LEU B HD12 1 
ATOM   6392  H HD13 . LEU B 1 137 ? 21.777  53.107  -0.379  1.00 107.17 ? 137 LEU B HD13 1 
ATOM   6393  H HD21 . LEU B 1 137 ? 20.118  55.580  -0.874  1.00 110.00 ? 137 LEU B HD21 1 
ATOM   6394  H HD22 . LEU B 1 137 ? 21.417  55.139  -1.674  1.00 110.00 ? 137 LEU B HD22 1 
ATOM   6395  H HD23 . LEU B 1 137 ? 20.050  55.375  -2.448  1.00 110.00 ? 137 LEU B HD23 1 
ATOM   6396  N N    . GLY B 1 138 ? 21.884  50.210  -3.419  1.00 103.94 ? 138 GLY B N    1 
ATOM   6397  C CA   . GLY B 1 138 ? 21.655  48.958  -4.102  1.00 98.10  ? 138 GLY B CA   1 
ATOM   6398  C C    . GLY B 1 138 ? 20.187  48.569  -4.002  1.00 97.16  ? 138 GLY B C    1 
ATOM   6399  O O    . GLY B 1 138 ? 19.450  49.065  -3.153  1.00 102.04 ? 138 GLY B O    1 
ATOM   6400  H H    . GLY B 1 138 ? 22.016  50.119  -2.574  1.00 124.73 ? 138 GLY B H    1 
ATOM   6401  H HA2  . GLY B 1 138 ? 21.895  49.044  -5.038  1.00 117.72 ? 138 GLY B HA2  1 
ATOM   6402  H HA3  . GLY B 1 138 ? 22.194  48.260  -3.701  1.00 117.72 ? 138 GLY B HA3  1 
ATOM   6403  N N    . LEU B 1 139 ? 19.765  47.659  -4.882  1.00 91.77  ? 139 LEU B N    1 
ATOM   6404  C CA   . LEU B 1 139 ? 18.357  47.254  -4.906  1.00 91.58  ? 139 LEU B CA   1 
ATOM   6405  C C    . LEU B 1 139 ? 18.264  45.846  -5.502  1.00 90.83  ? 139 LEU B C    1 
ATOM   6406  O O    . LEU B 1 139 ? 18.155  45.685  -6.717  1.00 90.23  ? 139 LEU B O    1 
ATOM   6407  C CB   . LEU B 1 139 ? 17.516  48.242  -5.686  1.00 93.42  ? 139 LEU B CB   1 
ATOM   6408  C CG   . LEU B 1 139 ? 16.034  47.926  -5.881  1.00 95.40  ? 139 LEU B CG   1 
ATOM   6409  C CD1  . LEU B 1 139 ? 15.421  47.308  -4.642  1.00 90.12  ? 139 LEU B CD1  1 
ATOM   6410  C CD2  . LEU B 1 139 ? 15.280  49.198  -6.286  1.00 97.74  ? 139 LEU B CD2  1 
ATOM   6411  H H    . LEU B 1 139 ? 20.263  47.269  -5.464  1.00 110.12 ? 139 LEU B H    1 
ATOM   6412  H HA   . LEU B 1 139 ? 18.029  47.205  -3.994  1.00 109.90 ? 139 LEU B HA   1 
ATOM   6413  H HB2  . LEU B 1 139 ? 17.561  49.095  -5.227  1.00 112.11 ? 139 LEU B HB2  1 
ATOM   6414  H HB3  . LEU B 1 139 ? 17.902  48.322  -6.573  1.00 112.11 ? 139 LEU B HB3  1 
ATOM   6415  H HG   . LEU B 1 139 ? 15.947  47.270  -6.590  1.00 114.48 ? 139 LEU B HG   1 
ATOM   6416  H HD11 . LEU B 1 139 ? 14.456  47.300  -4.738  1.00 108.14 ? 139 LEU B HD11 1 
ATOM   6417  H HD12 . LEU B 1 139 ? 15.751  46.402  -4.545  1.00 108.14 ? 139 LEU B HD12 1 
ATOM   6418  H HD13 . LEU B 1 139 ? 15.672  47.837  -3.869  1.00 108.14 ? 139 LEU B HD13 1 
ATOM   6419  H HD21 . LEU B 1 139 ? 14.346  48.979  -6.431  1.00 117.29 ? 139 LEU B HD21 1 
ATOM   6420  H HD22 . LEU B 1 139 ? 15.359  49.853  -5.575  1.00 117.29 ? 139 LEU B HD22 1 
ATOM   6421  H HD23 . LEU B 1 139 ? 15.668  49.549  -7.103  1.00 117.29 ? 139 LEU B HD23 1 
ATOM   6422  N N    . VAL B 1 140 ? 18.303  44.847  -4.628  1.00 91.60  ? 140 VAL B N    1 
ATOM   6423  C CA   . VAL B 1 140 ? 18.076  43.457  -5.001  1.00 88.59  ? 140 VAL B CA   1 
ATOM   6424  C C    . VAL B 1 140 ? 16.612  43.143  -4.727  1.00 90.78  ? 140 VAL B C    1 
ATOM   6425  O O    . VAL B 1 140 ? 16.150  43.249  -3.584  1.00 91.25  ? 140 VAL B O    1 
ATOM   6426  C CB   . VAL B 1 140 ? 18.999  42.504  -4.225  1.00 87.69  ? 140 VAL B CB   1 
ATOM   6427  C CG1  . VAL B 1 140 ? 19.071  41.151  -4.921  1.00 86.02  ? 140 VAL B CG1  1 
ATOM   6428  C CG2  . VAL B 1 140 ? 20.387  43.110  -4.066  1.00 86.15  ? 140 VAL B CG2  1 
ATOM   6429  H H    . VAL B 1 140 ? 18.464  44.952  -3.790  1.00 109.92 ? 140 VAL B H    1 
ATOM   6430  H HA   . VAL B 1 140 ? 18.252  43.341  -5.948  1.00 106.30 ? 140 VAL B HA   1 
ATOM   6431  H HB   . VAL B 1 140 ? 18.633  42.365  -3.338  1.00 105.23 ? 140 VAL B HB   1 
ATOM   6432  H HG11 . VAL B 1 140 ? 19.655  40.565  -4.414  1.00 103.23 ? 140 VAL B HG11 1 
ATOM   6433  H HG12 . VAL B 1 140 ? 18.180  40.771  -4.967  1.00 103.23 ? 140 VAL B HG12 1 
ATOM   6434  H HG13 . VAL B 1 140 ? 19.424  41.274  -5.816  1.00 103.23 ? 140 VAL B HG13 1 
ATOM   6435  H HG21 . VAL B 1 140 ? 21.023  42.400  -3.890  1.00 103.38 ? 140 VAL B HG21 1 
ATOM   6436  H HG22 . VAL B 1 140 ? 20.625  43.573  -4.885  1.00 103.38 ? 140 VAL B HG22 1 
ATOM   6437  H HG23 . VAL B 1 140 ? 20.375  43.735  -3.325  1.00 103.38 ? 140 VAL B HG23 1 
ATOM   6438  N N    . ARG B 1 141 ? 15.876  42.762  -5.766  1.00 90.98  ? 141 ARG B N    1 
ATOM   6439  C CA   . ARG B 1 141 ? 14.456  42.461  -5.646  1.00 93.33  ? 141 ARG B CA   1 
ATOM   6440  C C    . ARG B 1 141 ? 14.253  40.955  -5.542  1.00 93.14  ? 141 ARG B C    1 
ATOM   6441  O O    . ARG B 1 141 ? 14.749  40.196  -6.381  1.00 94.87  ? 141 ARG B O    1 
ATOM   6442  C CB   . ARG B 1 141 ? 13.680  43.020  -6.839  1.00 94.48  ? 141 ARG B CB   1 
ATOM   6443  C CG   . ARG B 1 141 ? 13.827  44.525  -7.019  1.00 98.34  ? 141 ARG B CG   1 
ATOM   6444  C CD   . ARG B 1 141 ? 12.773  45.099  -7.970  1.00 95.94  ? 141 ARG B CD   1 
ATOM   6445  N NE   . ARG B 1 141 ? 12.004  46.169  -7.343  1.00 99.50  ? 141 ARG B NE   1 
ATOM   6446  C CZ   . ARG B 1 141 ? 12.080  47.450  -7.678  1.00 102.87 ? 141 ARG B CZ   1 
ATOM   6447  N NH1  . ARG B 1 141 ? 12.868  47.867  -8.658  1.00 103.35 ? 141 ARG B NH1  1 
ATOM   6448  N NH2  . ARG B 1 141 ? 11.342  48.337  -7.016  1.00 106.33 ? 141 ARG B NH2  1 
ATOM   6449  H H    . ARG B 1 141 ? 16.184  42.670  -6.564  1.00 109.17 ? 141 ARG B H    1 
ATOM   6450  H HA   . ARG B 1 141 ? 14.109  42.868  -4.837  1.00 111.99 ? 141 ARG B HA   1 
ATOM   6451  H HB2  . ARG B 1 141 ? 14.002  42.593  -7.648  1.00 113.37 ? 141 ARG B HB2  1 
ATOM   6452  H HB3  . ARG B 1 141 ? 12.737  42.828  -6.715  1.00 113.37 ? 141 ARG B HB3  1 
ATOM   6453  H HG2  . ARG B 1 141 ? 13.725  44.960  -6.158  1.00 118.00 ? 141 ARG B HG2  1 
ATOM   6454  H HG3  . ARG B 1 141 ? 14.703  44.718  -7.387  1.00 118.00 ? 141 ARG B HG3  1 
ATOM   6455  H HD2  . ARG B 1 141 ? 13.214  45.461  -8.755  1.00 115.13 ? 141 ARG B HD2  1 
ATOM   6456  H HD3  . ARG B 1 141 ? 12.159  44.395  -8.230  1.00 115.13 ? 141 ARG B HD3  1 
ATOM   6457  H HE   . ARG B 1 141 ? 11.463  45.953  -6.711  1.00 119.39 ? 141 ARG B HE   1 
ATOM   6458  H HH11 . ARG B 1 141 ? 13.346  47.301  -9.094  1.00 124.02 ? 141 ARG B HH11 1 
ATOM   6459  H HH12 . ARG B 1 141 ? 12.900  48.702  -8.858  1.00 124.02 ? 141 ARG B HH12 1 
ATOM   6460  H HH21 . ARG B 1 141 ? 10.825  48.077  -6.380  1.00 127.59 ? 141 ARG B HH21 1 
ATOM   6461  H HH22 . ARG B 1 141 ? 11.382  49.171  -7.224  1.00 127.59 ? 141 ARG B HH22 1 
ATOM   6462  N N    . PHE B 1 142 ? 13.530  40.533  -4.512  1.00 98.61  ? 142 PHE B N    1 
ATOM   6463  C CA   . PHE B 1 142 ? 13.191  39.134  -4.306  1.00 102.77 ? 142 PHE B CA   1 
ATOM   6464  C C    . PHE B 1 142 ? 11.672  38.968  -4.384  1.00 105.98 ? 142 PHE B C    1 
ATOM   6465  O O    . PHE B 1 142 ? 10.935  39.911  -4.691  1.00 105.47 ? 142 PHE B O    1 
ATOM   6466  C CB   . PHE B 1 142 ? 13.735  38.633  -2.968  1.00 95.35  ? 142 PHE B CB   1 
ATOM   6467  C CG   . PHE B 1 142 ? 15.229  38.530  -2.921  1.00 89.91  ? 142 PHE B CG   1 
ATOM   6468  C CD1  . PHE B 1 142 ? 15.879  37.434  -3.461  1.00 87.69  ? 142 PHE B CD1  1 
ATOM   6469  C CD2  . PHE B 1 142 ? 15.984  39.533  -2.335  1.00 88.16  ? 142 PHE B CD2  1 
ATOM   6470  C CE1  . PHE B 1 142 ? 17.259  37.340  -3.419  1.00 88.03  ? 142 PHE B CE1  1 
ATOM   6471  C CE2  . PHE B 1 142 ? 17.364  39.445  -2.287  1.00 85.42  ? 142 PHE B CE2  1 
ATOM   6472  C CZ   . PHE B 1 142 ? 18.003  38.346  -2.829  1.00 86.36  ? 142 PHE B CZ   1 
ATOM   6473  H H    . PHE B 1 142 ? 13.216  41.054  -3.904  1.00 118.33 ? 142 PHE B H    1 
ATOM   6474  H HA   . PHE B 1 142 ? 13.602  38.613  -5.014  1.00 123.33 ? 142 PHE B HA   1 
ATOM   6475  H HB2  . PHE B 1 142 ? 13.459  39.248  -2.270  1.00 114.42 ? 142 PHE B HB2  1 
ATOM   6476  H HB3  . PHE B 1 142 ? 13.373  37.750  -2.796  1.00 114.42 ? 142 PHE B HB3  1 
ATOM   6477  H HD1  . PHE B 1 142 ? 15.384  36.754  -3.857  1.00 105.23 ? 142 PHE B HD1  1 
ATOM   6478  H HD2  . PHE B 1 142 ? 15.558  40.274  -1.969  1.00 105.78 ? 142 PHE B HD2  1 
ATOM   6479  H HE1  . PHE B 1 142 ? 17.686  36.600  -3.788  1.00 105.64 ? 142 PHE B HE1  1 
ATOM   6480  H HE2  . PHE B 1 142 ? 17.861  40.124  -1.890  1.00 102.51 ? 142 PHE B HE2  1 
ATOM   6481  H HZ   . PHE B 1 142 ? 18.930  38.283  -2.797  1.00 103.63 ? 142 PHE B HZ   1 
ATOM   6482  N N    . SER B 1 143 ? 11.207  37.757  -4.093  1.00 105.97 ? 143 SER B N    1 
ATOM   6483  C CA   . SER B 1 143 ? 9.780   37.457  -4.026  1.00 110.13 ? 143 SER B CA   1 
ATOM   6484  C C    . SER B 1 143 ? 9.330   37.694  -2.591  1.00 115.82 ? 143 SER B C    1 
ATOM   6485  O O    . SER B 1 143 ? 9.578   36.873  -1.706  1.00 115.15 ? 143 SER B O    1 
ATOM   6486  C CB   . SER B 1 143 ? 9.509   36.027  -4.476  1.00 112.36 ? 143 SER B CB   1 
ATOM   6487  O OG   . SER B 1 143 ? 10.391  35.649  -5.518  1.00 115.38 ? 143 SER B OG   1 
ATOM   6488  H H    . SER B 1 143 ? 11.709  37.078  -3.928  1.00 127.16 ? 143 SER B H    1 
ATOM   6489  H HA   . SER B 1 143 ? 9.287   38.053  -4.611  1.00 132.15 ? 143 SER B HA   1 
ATOM   6490  H HB2  . SER B 1 143 ? 9.636   35.430  -3.723  1.00 134.84 ? 143 SER B HB2  1 
ATOM   6491  H HB3  . SER B 1 143 ? 8.597   35.966  -4.798  1.00 134.84 ? 143 SER B HB3  1 
ATOM   6492  H HG   . SER B 1 143 ? 10.244  34.854  -5.744  1.00 138.46 ? 143 SER B HG   1 
ATOM   6493  N N    . GLY B 1 144 ? 8.681   38.831  -2.357  1.00 124.12 ? 144 GLY B N    1 
ATOM   6494  C CA   . GLY B 1 144 ? 8.201   39.165  -1.032  1.00 122.62 ? 144 GLY B CA   1 
ATOM   6495  C C    . GLY B 1 144 ? 8.999   40.258  -0.349  1.00 120.55 ? 144 GLY B C    1 
ATOM   6496  O O    . GLY B 1 144 ? 8.423   41.162  0.260   1.00 121.80 ? 144 GLY B O    1 
ATOM   6497  H H    . GLY B 1 144 ? 8.508   39.425  -2.954  1.00 148.94 ? 144 GLY B H    1 
ATOM   6498  H HA2  . GLY B 1 144 ? 7.280   39.462  -1.095  1.00 147.15 ? 144 GLY B HA2  1 
ATOM   6499  H HA3  . GLY B 1 144 ? 8.240   38.373  -0.473  1.00 147.15 ? 144 GLY B HA3  1 
ATOM   6500  N N    . ILE B 1 145 ? 10.326  40.186  -0.441  1.00 118.38 ? 145 ILE B N    1 
ATOM   6501  C CA   . ILE B 1 145 ? 11.215  41.163  0.175   1.00 119.03 ? 145 ILE B CA   1 
ATOM   6502  C C    . ILE B 1 145 ? 11.977  41.890  -0.921  1.00 119.26 ? 145 ILE B C    1 
ATOM   6503  O O    . ILE B 1 145 ? 12.306  41.325  -1.967  1.00 118.37 ? 145 ILE B O    1 
ATOM   6504  C CB   . ILE B 1 145 ? 12.182  40.482  1.175   1.00 120.04 ? 145 ILE B CB   1 
ATOM   6505  C CG1  . ILE B 1 145 ? 12.893  41.504  2.073   1.00 118.06 ? 145 ILE B CG1  1 
ATOM   6506  C CG2  . ILE B 1 145 ? 13.228  39.647  0.429   1.00 118.55 ? 145 ILE B CG2  1 
ATOM   6507  C CD1  . ILE B 1 145 ? 12.015  42.612  2.630   1.00 117.54 ? 145 ILE B CD1  1 
ATOM   6508  H H    . ILE B 1 145 ? 10.742  39.565  -0.865  1.00 142.05 ? 145 ILE B H    1 
ATOM   6509  H HA   . ILE B 1 145 ? 10.694  41.824  0.656   1.00 142.83 ? 145 ILE B HA   1 
ATOM   6510  H HB   . ILE B 1 145 ? 11.642  39.907  1.739   1.00 144.05 ? 145 ILE B HB   1 
ATOM   6511  H HG12 . ILE B 1 145 ? 13.275  41.032  2.829   1.00 141.68 ? 145 ILE B HG12 1 
ATOM   6512  H HG13 . ILE B 1 145 ? 13.596  41.926  1.555   1.00 141.68 ? 145 ILE B HG13 1 
ATOM   6513  H HG21 . ILE B 1 145 ? 13.806  39.213  1.076   1.00 142.26 ? 145 ILE B HG21 1 
ATOM   6514  H HG22 . ILE B 1 145 ? 12.774  38.980  -0.109  1.00 142.26 ? 145 ILE B HG22 1 
ATOM   6515  H HG23 . ILE B 1 145 ? 13.751  40.232  -0.141  1.00 142.26 ? 145 ILE B HG23 1 
ATOM   6516  H HD11 . ILE B 1 145 ? 12.551  43.182  3.203   1.00 141.05 ? 145 ILE B HD11 1 
ATOM   6517  H HD12 . ILE B 1 145 ? 11.654  43.130  1.893   1.00 141.05 ? 145 ILE B HD12 1 
ATOM   6518  H HD13 . ILE B 1 145 ? 11.292  42.216  3.141   1.00 141.05 ? 145 ILE B HD13 1 
ATOM   6519  N N    . ASN B 1 146 ? 12.249  43.171  -0.671  1.00 109.00 ? 146 ASN B N    1 
ATOM   6520  C CA   . ASN B 1 146 ? 13.041  44.012  -1.571  1.00 102.96 ? 146 ASN B CA   1 
ATOM   6521  C C    . ASN B 1 146 ? 14.138  44.664  -0.733  1.00 98.39  ? 146 ASN B C    1 
ATOM   6522  O O    . ASN B 1 146 ? 13.874  45.616  0.007   1.00 98.86  ? 146 ASN B O    1 
ATOM   6523  C CB   . ASN B 1 146 ? 12.178  45.063  -2.264  1.00 104.52 ? 146 ASN B CB   1 
ATOM   6524  C CG   . ASN B 1 146 ? 11.242  44.463  -3.302  1.00 106.83 ? 146 ASN B CG   1 
ATOM   6525  O OD1  . ASN B 1 146 ? 11.429  43.331  -3.752  1.00 104.30 ? 146 ASN B OD1  1 
ATOM   6526  N ND2  . ASN B 1 146 ? 10.226  45.225  -3.688  1.00 110.52 ? 146 ASN B ND2  1 
ATOM   6527  H H    . ASN B 1 146 ? 11.979  43.586  0.032   1.00 130.80 ? 146 ASN B H    1 
ATOM   6528  H HA   . ASN B 1 146 ? 13.448  43.459  -2.256  1.00 123.56 ? 146 ASN B HA   1 
ATOM   6529  H HB2  . ASN B 1 146 ? 11.637  45.516  -1.599  1.00 125.42 ? 146 ASN B HB2  1 
ATOM   6530  H HB3  . ASN B 1 146 ? 12.755  45.700  -2.713  1.00 125.42 ? 146 ASN B HB3  1 
ATOM   6531  H HD21 . ASN B 1 146 ? 10.127  46.011  -3.353  1.00 132.62 ? 146 ASN B HD21 1 
ATOM   6532  H HD22 . ASN B 1 146 ? 9.667   44.934  -4.273  1.00 132.62 ? 146 ASN B HD22 1 
ATOM   6533  N N    . HIS B 1 147 ? 15.361  44.157  -0.844  1.00 93.04  ? 147 HIS B N    1 
ATOM   6534  C CA   . HIS B 1 147 ? 16.472  44.655  -0.047  1.00 89.26  ? 147 HIS B CA   1 
ATOM   6535  C C    . HIS B 1 147 ? 17.148  45.839  -0.726  1.00 88.48  ? 147 HIS B C    1 
ATOM   6536  O O    . HIS B 1 147 ? 17.103  45.993  -1.948  1.00 91.72  ? 147 HIS B O    1 
ATOM   6537  C CB   . HIS B 1 147 ? 17.495  43.547  0.197   1.00 88.24  ? 147 HIS B CB   1 
ATOM   6538  C CG   . HIS B 1 147 ? 17.042  42.516  1.183   1.00 89.15  ? 147 HIS B CG   1 
ATOM   6539  N ND1  . HIS B 1 147 ? 16.715  42.827  2.485   1.00 89.01  ? 147 HIS B ND1  1 
ATOM   6540  C CD2  . HIS B 1 147 ? 16.853  41.182  1.055   1.00 87.84  ? 147 HIS B CD2  1 
ATOM   6541  C CE1  . HIS B 1 147 ? 16.348  41.727  3.118   1.00 89.56  ? 147 HIS B CE1  1 
ATOM   6542  N NE2  . HIS B 1 147 ? 16.423  40.715  2.273   1.00 88.01  ? 147 HIS B NE2  1 
ATOM   6543  H H    . HIS B 1 147 ? 15.573  43.518  -1.379  1.00 111.65 ? 147 HIS B H    1 
ATOM   6544  H HA   . HIS B 1 147 ? 16.134  44.958  0.810   1.00 107.11 ? 147 HIS B HA   1 
ATOM   6545  H HB2  . HIS B 1 147 ? 17.673  43.095  -0.643  1.00 105.89 ? 147 HIS B HB2  1 
ATOM   6546  H HB3  . HIS B 1 147 ? 18.311  43.945  0.539   1.00 105.89 ? 147 HIS B HB3  1 
ATOM   6547  H HD1  . HIS B 1 147 ? 16.745  43.613  2.832   1.00 106.81 ? 147 HIS B HD1  1 
ATOM   6548  H HD2  . HIS B 1 147 ? 16.989  40.676  0.287   1.00 105.41 ? 147 HIS B HD2  1 
ATOM   6549  H HE1  . HIS B 1 147 ? 16.082  41.674  4.008   1.00 107.47 ? 147 HIS B HE1  1 
ATOM   6550  N N    . PHE B 1 148 ? 17.773  46.684  0.092   1.00 90.38  ? 148 PHE B N    1 
ATOM   6551  C CA   . PHE B 1 148 ? 18.476  47.873  -0.377  1.00 90.08  ? 148 PHE B CA   1 
ATOM   6552  C C    . PHE B 1 148 ? 19.844  47.912  0.289   1.00 89.09  ? 148 PHE B C    1 
ATOM   6553  O O    . PHE B 1 148 ? 19.931  47.991  1.520   1.00 86.49  ? 148 PHE B O    1 
ATOM   6554  C CB   . PHE B 1 148 ? 17.700  49.155  -0.044  1.00 87.92  ? 148 PHE B CB   1 
ATOM   6555  C CG   . PHE B 1 148 ? 16.430  49.336  -0.830  1.00 87.89  ? 148 PHE B CG   1 
ATOM   6556  C CD1  . PHE B 1 148 ? 15.275  48.661  -0.474  1.00 89.51  ? 148 PHE B CD1  1 
ATOM   6557  C CD2  . PHE B 1 148 ? 16.385  50.209  -1.910  1.00 92.03  ? 148 PHE B CD2  1 
ATOM   6558  C CE1  . PHE B 1 148 ? 14.103  48.836  -1.185  1.00 89.91  ? 148 PHE B CE1  1 
ATOM   6559  C CE2  . PHE B 1 148 ? 15.214  50.390  -2.627  1.00 87.98  ? 148 PHE B CE2  1 
ATOM   6560  C CZ   . PHE B 1 148 ? 14.072  49.702  -2.262  1.00 92.85  ? 148 PHE B CZ   1 
ATOM   6561  H H    . PHE B 1 148 ? 17.804  46.586  0.945   1.00 108.46 ? 148 PHE B H    1 
ATOM   6562  H HA   . PHE B 1 148 ? 18.587  47.820  -1.339  1.00 108.10 ? 148 PHE B HA   1 
ATOM   6563  H HB2  . PHE B 1 148 ? 17.463  49.137  0.897   1.00 105.51 ? 148 PHE B HB2  1 
ATOM   6564  H HB3  . PHE B 1 148 ? 18.270  49.918  -0.227  1.00 105.51 ? 148 PHE B HB3  1 
ATOM   6565  H HD1  . PHE B 1 148 ? 15.288  48.081  0.253   1.00 107.41 ? 148 PHE B HD1  1 
ATOM   6566  H HD2  . PHE B 1 148 ? 17.150  50.678  -2.153  1.00 110.44 ? 148 PHE B HD2  1 
ATOM   6567  H HE1  . PHE B 1 148 ? 13.335  48.371  -0.940  1.00 107.89 ? 148 PHE B HE1  1 
ATOM   6568  H HE2  . PHE B 1 148 ? 15.197  50.973  -3.352  1.00 105.57 ? 148 PHE B HE2  1 
ATOM   6569  H HZ   . PHE B 1 148 ? 13.284  49.822  -2.741  1.00 111.42 ? 148 PHE B HZ   1 
ATOM   6570  N N    . ILE B 1 149 ? 20.905  47.861  -0.514  1.00 90.31  ? 149 ILE B N    1 
ATOM   6571  C CA   . ILE B 1 149 ? 22.258  48.010  0.010   1.00 87.56  ? 149 ILE B CA   1 
ATOM   6572  C C    . ILE B 1 149 ? 22.566  49.493  0.175   1.00 88.05  ? 149 ILE B C    1 
ATOM   6573  O O    . ILE B 1 149 ? 22.236  50.312  -0.694  1.00 91.79  ? 149 ILE B O    1 
ATOM   6574  C CB   . ILE B 1 149 ? 23.284  47.336  -0.919  1.00 88.56  ? 149 ILE B CB   1 
ATOM   6575  C CG1  . ILE B 1 149 ? 22.750  46.007  -1.455  1.00 89.34  ? 149 ILE B CG1  1 
ATOM   6576  C CG2  . ILE B 1 149 ? 24.607  47.142  -0.179  1.00 86.29  ? 149 ILE B CG2  1 
ATOM   6577  C CD1  . ILE B 1 149 ? 22.240  45.058  -0.384  1.00 88.64  ? 149 ILE B CD1  1 
ATOM   6578  H H    . ILE B 1 149 ? 20.866  47.741  -1.364  1.00 108.37 ? 149 ILE B H    1 
ATOM   6579  H HA   . ILE B 1 149 ? 22.307  47.579  0.877   1.00 105.07 ? 149 ILE B HA   1 
ATOM   6580  H HB   . ILE B 1 149 ? 23.437  47.916  -1.681  1.00 106.28 ? 149 ILE B HB   1 
ATOM   6581  H HG12 . ILE B 1 149 ? 22.014  46.191  -2.060  1.00 107.21 ? 149 ILE B HG12 1 
ATOM   6582  H HG13 . ILE B 1 149 ? 23.465  45.556  -1.931  1.00 107.21 ? 149 ILE B HG13 1 
ATOM   6583  H HG21 . ILE B 1 149 ? 25.217  46.646  -0.747  1.00 103.55 ? 149 ILE B HG21 1 
ATOM   6584  H HG22 . ILE B 1 149 ? 24.983  48.011  0.030   1.00 103.55 ? 149 ILE B HG22 1 
ATOM   6585  H HG23 . ILE B 1 149 ? 24.441  46.647  0.639   1.00 103.55 ? 149 ILE B HG23 1 
ATOM   6586  H HD11 . ILE B 1 149 ? 22.071  44.191  -0.785  1.00 106.37 ? 149 ILE B HD11 1 
ATOM   6587  H HD12 . ILE B 1 149 ? 22.911  44.976  0.311   1.00 106.37 ? 149 ILE B HD12 1 
ATOM   6588  H HD13 . ILE B 1 149 ? 21.419  45.415  -0.011  1.00 106.37 ? 149 ILE B HD13 1 
ATOM   6589  N N    . PHE B 1 150 ? 23.206  49.847  1.289   1.00 84.69  ? 150 PHE B N    1 
ATOM   6590  C CA   . PHE B 1 150 ? 23.632  51.221  1.560   1.00 83.97  ? 150 PHE B CA   1 
ATOM   6591  C C    . PHE B 1 150 ? 25.076  51.153  2.050   1.00 84.44  ? 150 PHE B C    1 
ATOM   6592  O O    . PHE B 1 150 ? 25.329  50.946  3.239   1.00 87.00  ? 150 PHE B O    1 
ATOM   6593  C CB   . PHE B 1 150 ? 22.723  51.899  2.573   1.00 85.53  ? 150 PHE B CB   1 
ATOM   6594  C CG   . PHE B 1 150 ? 23.083  53.334  2.850   1.00 87.22  ? 150 PHE B CG   1 
ATOM   6595  C CD1  . PHE B 1 150 ? 22.715  54.339  1.969   1.00 90.63  ? 150 PHE B CD1  1 
ATOM   6596  C CD2  . PHE B 1 150 ? 23.788  53.677  3.993   1.00 86.14  ? 150 PHE B CD2  1 
ATOM   6597  C CE1  . PHE B 1 150 ? 23.044  55.661  2.230   1.00 92.64  ? 150 PHE B CE1  1 
ATOM   6598  C CE2  . PHE B 1 150 ? 24.120  54.993  4.254   1.00 84.63  ? 150 PHE B CE2  1 
ATOM   6599  C CZ   . PHE B 1 150 ? 23.746  55.985  3.373   1.00 91.96  ? 150 PHE B CZ   1 
ATOM   6600  H H    . PHE B 1 150 ? 23.408  49.297  1.918   1.00 101.63 ? 150 PHE B H    1 
ATOM   6601  H HA   . PHE B 1 150 ? 23.600  51.736  0.738   1.00 100.76 ? 150 PHE B HA   1 
ATOM   6602  H HB2  . PHE B 1 150 ? 21.813  51.882  2.236   1.00 102.63 ? 150 PHE B HB2  1 
ATOM   6603  H HB3  . PHE B 1 150 ? 22.774  51.414  3.412   1.00 102.63 ? 150 PHE B HB3  1 
ATOM   6604  H HD1  . PHE B 1 150 ? 22.243  54.125  1.196   1.00 108.76 ? 150 PHE B HD1  1 
ATOM   6605  H HD2  . PHE B 1 150 ? 24.040  53.012  4.593   1.00 103.36 ? 150 PHE B HD2  1 
ATOM   6606  H HE1  . PHE B 1 150 ? 22.793  56.329  1.634   1.00 111.17 ? 150 PHE B HE1  1 
ATOM   6607  H HE2  . PHE B 1 150 ? 24.595  55.210  5.023   1.00 101.55 ? 150 PHE B HE2  1 
ATOM   6608  H HZ   . PHE B 1 150 ? 23.966  56.871  3.549   1.00 110.35 ? 150 PHE B HZ   1 
ATOM   6609  N N    . ASN B 1 151 ? 26.018  51.311  1.125   1.00 87.79  ? 151 ASN B N    1 
ATOM   6610  C CA   . ASN B 1 151 ? 27.435  51.377  1.469   1.00 87.98  ? 151 ASN B CA   1 
ATOM   6611  C C    . ASN B 1 151 ? 27.681  52.689  2.201   1.00 87.67  ? 151 ASN B C    1 
ATOM   6612  O O    . ASN B 1 151 ? 27.717  53.759  1.590   1.00 89.64  ? 151 ASN B O    1 
ATOM   6613  C CB   . ASN B 1 151 ? 28.296  51.270  0.218   1.00 89.50  ? 151 ASN B CB   1 
ATOM   6614  C CG   . ASN B 1 151 ? 29.747  50.973  0.538   1.00 93.08  ? 151 ASN B CG   1 
ATOM   6615  O OD1  . ASN B 1 151 ? 30.292  51.472  1.526   1.00 96.03  ? 151 ASN B OD1  1 
ATOM   6616  N ND2  . ASN B 1 151 ? 30.384  50.157  -0.298  1.00 94.21  ? 151 ASN B ND2  1 
ATOM   6617  H H    . ASN B 1 151 ? 25.861  51.383  0.283   1.00 105.35 ? 151 ASN B H    1 
ATOM   6618  H HA   . ASN B 1 151 ? 27.669  50.638  2.053   1.00 105.58 ? 151 ASN B HA   1 
ATOM   6619  H HB2  . ASN B 1 151 ? 27.958  50.553  -0.340  1.00 107.40 ? 151 ASN B HB2  1 
ATOM   6620  H HB3  . ASN B 1 151 ? 28.260  52.111  -0.265  1.00 107.40 ? 151 ASN B HB3  1 
ATOM   6621  H HD21 . ASN B 1 151 ? 31.209  49.958  -0.159  1.00 113.04 ? 151 ASN B HD21 1 
ATOM   6622  H HD22 . ASN B 1 151 ? 29.971  49.829  -0.977  1.00 113.04 ? 151 ASN B HD22 1 
ATOM   6623  N N    . ILE B 1 152 ? 27.847  52.609  3.522   1.00 91.25  ? 152 ILE B N    1 
ATOM   6624  C CA   . ILE B 1 152 ? 27.992  53.818  4.328   1.00 89.58  ? 152 ILE B CA   1 
ATOM   6625  C C    . ILE B 1 152 ? 29.238  54.588  3.914   1.00 92.25  ? 152 ILE B C    1 
ATOM   6626  O O    . ILE B 1 152 ? 29.200  55.809  3.711   1.00 94.84  ? 152 ILE B O    1 
ATOM   6627  C CB   . ILE B 1 152 ? 28.027  53.459  5.825   1.00 85.14  ? 152 ILE B CB   1 
ATOM   6628  C CG1  . ILE B 1 152 ? 26.643  53.001  6.285   1.00 84.08  ? 152 ILE B CG1  1 
ATOM   6629  C CG2  . ILE B 1 152 ? 28.517  54.644  6.645   1.00 88.30  ? 152 ILE B CG2  1 
ATOM   6630  C CD1  . ILE B 1 152 ? 26.637  52.348  7.647   1.00 85.78  ? 152 ILE B CD1  1 
ATOM   6631  H H    . ILE B 1 152 ? 27.880  51.875  3.970   1.00 109.49 ? 152 ILE B H    1 
ATOM   6632  H HA   . ILE B 1 152 ? 27.222  54.387  4.170   1.00 107.50 ? 152 ILE B HA   1 
ATOM   6633  H HB   . ILE B 1 152 ? 28.650  52.727  5.958   1.00 102.18 ? 152 ILE B HB   1 
ATOM   6634  H HG12 . ILE B 1 152 ? 26.056  53.772  6.324   1.00 100.90 ? 152 ILE B HG12 1 
ATOM   6635  H HG13 . ILE B 1 152 ? 26.300  52.356  5.646   1.00 100.90 ? 152 ILE B HG13 1 
ATOM   6636  H HG21 . ILE B 1 152 ? 28.283  54.502  7.576   1.00 105.96 ? 152 ILE B HG21 1 
ATOM   6637  H HG22 . ILE B 1 152 ? 29.480  54.714  6.554   1.00 105.96 ? 152 ILE B HG22 1 
ATOM   6638  H HG23 . ILE B 1 152 ? 28.093  55.452  6.317   1.00 105.96 ? 152 ILE B HG23 1 
ATOM   6639  H HD11 . ILE B 1 152 ? 27.292  51.632  7.657   1.00 102.94 ? 152 ILE B HD11 1 
ATOM   6640  H HD12 . ILE B 1 152 ? 26.864  53.013  8.316   1.00 102.94 ? 152 ILE B HD12 1 
ATOM   6641  H HD13 . ILE B 1 152 ? 25.753  51.991  7.823   1.00 102.94 ? 152 ILE B HD13 1 
ATOM   6642  N N    . LYS B 1 153 ? 30.364  53.884  3.780   1.00 92.32  ? 153 LYS B N    1 
ATOM   6643  C CA   . LYS B 1 153 ? 31.630  54.557  3.510   1.00 93.64  ? 153 LYS B CA   1 
ATOM   6644  C C    . LYS B 1 153 ? 31.613  55.251  2.155   1.00 94.98  ? 153 LYS B C    1 
ATOM   6645  O O    . LYS B 1 153 ? 32.138  56.362  2.013   1.00 94.37  ? 153 LYS B O    1 
ATOM   6646  C CB   . LYS B 1 153 ? 32.777  53.550  3.584   1.00 93.79  ? 153 LYS B CB   1 
ATOM   6647  C CG   . LYS B 1 153 ? 32.927  52.880  4.945   1.00 94.82  ? 153 LYS B CG   1 
ATOM   6648  C CD   . LYS B 1 153 ? 33.636  53.794  5.939   1.00 95.94  ? 153 LYS B CD   1 
ATOM   6649  C CE   . LYS B 1 153 ? 33.063  53.651  7.346   1.00 95.83  ? 153 LYS B CE   1 
ATOM   6650  N NZ   . LYS B 1 153 ? 34.121  53.727  8.401   1.00 97.17  ? 153 LYS B NZ   1 
ATOM   6651  H H    . LYS B 1 153 ? 30.419  53.028  3.841   1.00 110.78 ? 153 LYS B H    1 
ATOM   6652  H HA   . LYS B 1 153 ? 31.776  55.235  4.188   1.00 112.37 ? 153 LYS B HA   1 
ATOM   6653  H HB2  . LYS B 1 153 ? 32.622  52.853  2.928   1.00 112.55 ? 153 LYS B HB2  1 
ATOM   6654  H HB3  . LYS B 1 153 ? 33.608  54.011  3.389   1.00 112.55 ? 153 LYS B HB3  1 
ATOM   6655  H HG2  . LYS B 1 153 ? 32.049  52.667  5.298   1.00 113.78 ? 153 LYS B HG2  1 
ATOM   6656  H HG3  . LYS B 1 153 ? 33.451  52.069  4.848   1.00 113.78 ? 153 LYS B HG3  1 
ATOM   6657  H HD2  . LYS B 1 153 ? 34.578  53.565  5.970   1.00 115.12 ? 153 LYS B HD2  1 
ATOM   6658  H HD3  . LYS B 1 153 ? 33.529  54.716  5.659   1.00 115.12 ? 153 LYS B HD3  1 
ATOM   6659  H HE2  . LYS B 1 153 ? 32.427  54.367  7.504   1.00 115.00 ? 153 LYS B HE2  1 
ATOM   6660  H HE3  . LYS B 1 153 ? 32.621  52.791  7.424   1.00 115.00 ? 153 LYS B HE3  1 
ATOM   6661  H HZ1  . LYS B 1 153 ? 34.707  53.066  8.293   1.00 116.61 ? 153 LYS B HZ1  1 
ATOM   6662  H HZ2  . LYS B 1 153 ? 34.550  54.505  8.347   1.00 116.61 ? 153 LYS B HZ2  1 
ATOM   6663  H HZ3  . LYS B 1 153 ? 33.752  53.657  9.208   1.00 116.61 ? 153 LYS B HZ3  1 
ATOM   6664  N N    . GLU B 1 154 ? 31.012  54.618  1.149   1.00 95.47  ? 154 GLU B N    1 
ATOM   6665  C CA   . GLU B 1 154 ? 30.983  55.167  -0.200  1.00 97.56  ? 154 GLU B CA   1 
ATOM   6666  C C    . GLU B 1 154 ? 29.879  56.198  -0.400  1.00 98.58  ? 154 GLU B C    1 
ATOM   6667  O O    . GLU B 1 154 ? 29.587  56.551  -1.549  1.00 99.13  ? 154 GLU B O    1 
ATOM   6668  C CB   . GLU B 1 154 ? 30.819  54.038  -1.223  1.00 97.29  ? 154 GLU B CB   1 
ATOM   6669  C CG   . GLU B 1 154 ? 31.929  52.998  -1.182  1.00 99.60  ? 154 GLU B CG   1 
ATOM   6670  C CD   . GLU B 1 154 ? 32.056  52.217  -2.477  1.00 104.07 ? 154 GLU B CD   1 
ATOM   6671  O OE1  . GLU B 1 154 ? 31.167  52.345  -3.347  1.00 105.83 ? 154 GLU B OE1  1 
ATOM   6672  O OE2  . GLU B 1 154 ? 33.051  51.474  -2.625  1.00 105.44 ? 154 GLU B OE2  1 
ATOM   6673  H H    . GLU B 1 154 ? 30.611  53.861  1.226   1.00 114.56 ? 154 GLU B H    1 
ATOM   6674  H HA   . GLU B 1 154 ? 31.832  55.605  -0.367  1.00 117.07 ? 154 GLU B HA   1 
ATOM   6675  H HB2  . GLU B 1 154 ? 29.981  53.581  -1.051  1.00 116.75 ? 154 GLU B HB2  1 
ATOM   6676  H HB3  . GLU B 1 154 ? 30.810  54.424  -2.113  1.00 116.75 ? 154 GLU B HB3  1 
ATOM   6677  H HG2  . GLU B 1 154 ? 32.774  53.445  -1.018  1.00 119.52 ? 154 GLU B HG2  1 
ATOM   6678  H HG3  . GLU B 1 154 ? 31.744  52.367  -0.469  1.00 119.52 ? 154 GLU B HG3  1 
ATOM   6679  N N    . ASN B 1 155 ? 29.270  56.696  0.673   1.00 97.82  ? 155 ASN B N    1 
ATOM   6680  C CA   . ASN B 1 155 ? 28.176  57.647  0.562   1.00 100.08 ? 155 ASN B CA   1 
ATOM   6681  C C    . ASN B 1 155 ? 28.384  58.811  1.520   1.00 100.76 ? 155 ASN B C    1 
ATOM   6682  O O    . ASN B 1 155 ? 29.248  58.784  2.401   1.00 103.54 ? 155 ASN B O    1 
ATOM   6683  C CB   . ASN B 1 155 ? 26.822  56.972  0.832   1.00 97.75  ? 155 ASN B CB   1 
ATOM   6684  C CG   . ASN B 1 155 ? 26.030  56.740  -0.437  1.00 101.27 ? 155 ASN B CG   1 
ATOM   6685  O OD1  . ASN B 1 155 ? 26.601  56.583  -1.515  1.00 102.09 ? 155 ASN B OD1  1 
ATOM   6686  N ND2  . ASN B 1 155 ? 24.712  56.727  -0.320  1.00 102.78 ? 155 ASN B ND2  1 
ATOM   6687  H H    . ASN B 1 155 ? 29.478  56.494  1.483   1.00 117.39 ? 155 ASN B H    1 
ATOM   6688  H HA   . ASN B 1 155 ? 28.171  58.008  -0.339  1.00 120.09 ? 155 ASN B HA   1 
ATOM   6689  H HB2  . ASN B 1 155 ? 26.975  56.111  1.254   1.00 117.30 ? 155 ASN B HB2  1 
ATOM   6690  H HB3  . ASN B 1 155 ? 26.296  57.539  1.417   1.00 117.30 ? 155 ASN B HB3  1 
ATOM   6691  H HD21 . ASN B 1 155 ? 24.347  56.846  0.450   1.00 123.33 ? 155 ASN B HD21 1 
ATOM   6692  H HD22 . ASN B 1 155 ? 24.220  56.599  -1.013  1.00 123.33 ? 155 ASN B HD22 1 
ATOM   6693  N N    . LYS B 1 156 ? 27.575  59.849  1.323   1.00 104.44 ? 156 LYS B N    1 
ATOM   6694  C CA   . LYS B 1 156 ? 27.640  61.027  2.174   1.00 105.54 ? 156 LYS B CA   1 
ATOM   6695  C C    . LYS B 1 156 ? 27.222  60.674  3.595   1.00 105.32 ? 156 LYS B C    1 
ATOM   6696  O O    . LYS B 1 156 ? 26.338  59.842  3.813   1.00 103.17 ? 156 LYS B O    1 
ATOM   6697  C CB   . LYS B 1 156 ? 26.739  62.130  1.619   1.00 105.14 ? 156 LYS B CB   1 
ATOM   6698  C CG   . LYS B 1 156 ? 26.772  63.423  2.422   1.00 107.20 ? 156 LYS B CG   1 
ATOM   6699  C CD   . LYS B 1 156 ? 25.763  64.435  1.890   1.00 107.66 ? 156 LYS B CD   1 
ATOM   6700  C CE   . LYS B 1 156 ? 24.338  64.058  2.278   1.00 106.98 ? 156 LYS B CE   1 
ATOM   6701  N NZ   . LYS B 1 156 ? 23.481  65.258  2.507   1.00 107.39 ? 156 LYS B NZ   1 
ATOM   6702  H H    . LYS B 1 156 ? 26.980  59.893  0.703   1.00 125.33 ? 156 LYS B H    1 
ATOM   6703  H HA   . LYS B 1 156 ? 28.549  61.362  2.196   1.00 126.66 ? 156 LYS B HA   1 
ATOM   6704  H HB2  . LYS B 1 156 ? 27.023  62.337  0.715   1.00 126.17 ? 156 LYS B HB2  1 
ATOM   6705  H HB3  . LYS B 1 156 ? 25.823  61.810  1.615   1.00 126.17 ? 156 LYS B HB3  1 
ATOM   6706  H HG2  . LYS B 1 156 ? 26.554  63.233  3.348   1.00 128.64 ? 156 LYS B HG2  1 
ATOM   6707  H HG3  . LYS B 1 156 ? 27.657  63.815  2.364   1.00 128.64 ? 156 LYS B HG3  1 
ATOM   6708  H HD2  . LYS B 1 156 ? 25.958  65.310  2.260   1.00 129.19 ? 156 LYS B HD2  1 
ATOM   6709  H HD3  . LYS B 1 156 ? 25.817  64.465  0.922   1.00 129.19 ? 156 LYS B HD3  1 
ATOM   6710  H HE2  . LYS B 1 156 ? 23.941  63.536  1.564   1.00 128.37 ? 156 LYS B HE2  1 
ATOM   6711  H HE3  . LYS B 1 156 ? 24.357  63.540  3.098   1.00 128.37 ? 156 LYS B HE3  1 
ATOM   6712  H HZ1  . LYS B 1 156 ? 23.444  65.752  1.768   1.00 128.86 ? 156 LYS B HZ1  1 
ATOM   6713  H HZ2  . LYS B 1 156 ? 22.656  65.006  2.727   1.00 128.86 ? 156 LYS B HZ2  1 
ATOM   6714  H HZ3  . LYS B 1 156 ? 23.818  65.751  3.167   1.00 128.86 ? 156 LYS B HZ3  1 
ATOM   6715  N N    . GLU B 1 157 ? 27.872  61.313  4.565   1.00 107.65 ? 157 GLU B N    1 
ATOM   6716  C CA   . GLU B 1 157 ? 27.499  61.137  5.961   1.00 109.38 ? 157 GLU B CA   1 
ATOM   6717  C C    . GLU B 1 157 ? 26.023  61.456  6.154   1.00 106.49 ? 157 GLU B C    1 
ATOM   6718  O O    . GLU B 1 157 ? 25.507  62.441  5.619   1.00 106.71 ? 157 GLU B O    1 
ATOM   6719  C CB   . GLU B 1 157 ? 28.358  62.038  6.847   1.00 113.68 ? 157 GLU B CB   1 
ATOM   6720  C CG   . GLU B 1 157 ? 28.343  61.670  8.317   1.00 115.26 ? 157 GLU B CG   1 
ATOM   6721  C CD   . GLU B 1 157 ? 28.135  62.877  9.210   1.00 119.15 ? 157 GLU B CD   1 
ATOM   6722  O OE1  . GLU B 1 157 ? 28.770  63.924  8.956   1.00 118.63 ? 157 GLU B OE1  1 
ATOM   6723  O OE2  . GLU B 1 157 ? 27.334  62.778  10.165  1.00 121.65 ? 157 GLU B OE2  1 
ATOM   6724  H H    . GLU B 1 157 ? 28.530  61.852  4.439   1.00 129.19 ? 157 GLU B H    1 
ATOM   6725  H HA   . GLU B 1 157 ? 27.650  60.217  6.229   1.00 131.26 ? 157 GLU B HA   1 
ATOM   6726  H HB2  . GLU B 1 157 ? 29.277  61.987  6.541   1.00 136.41 ? 157 GLU B HB2  1 
ATOM   6727  H HB3  . GLU B 1 157 ? 28.033  62.949  6.769   1.00 136.41 ? 157 GLU B HB3  1 
ATOM   6728  H HG2  . GLU B 1 157 ? 27.619  61.045  8.481   1.00 138.31 ? 157 GLU B HG2  1 
ATOM   6729  H HG3  . GLU B 1 157 ? 29.192  61.264  8.552   1.00 138.31 ? 157 GLU B HG3  1 
ATOM   6730  N N    . THR B 1 158 ? 25.340  60.613  6.922   1.00 107.61 ? 158 THR B N    1 
ATOM   6731  C CA   . THR B 1 158 ? 23.907  60.770  7.125   1.00 107.13 ? 158 THR B CA   1 
ATOM   6732  C C    . THR B 1 158 ? 23.490  59.992  8.366   1.00 106.37 ? 158 THR B C    1 
ATOM   6733  O O    . THR B 1 158 ? 24.292  59.292  8.989   1.00 105.98 ? 158 THR B O    1 
ATOM   6734  C CB   . THR B 1 158 ? 23.112  60.286  5.908   1.00 105.30 ? 158 THR B CB   1 
ATOM   6735  O OG1  . THR B 1 158 ? 21.731  60.135  6.264   1.00 104.43 ? 158 THR B OG1  1 
ATOM   6736  C CG2  . THR B 1 158 ? 23.651  58.944  5.426   1.00 103.90 ? 158 THR B CG2  1 
ATOM   6737  H H    . THR B 1 158 ? 25.685  59.943  7.336   1.00 129.13 ? 158 THR B H    1 
ATOM   6738  H HA   . THR B 1 158 ? 23.731  61.713  7.271   1.00 128.56 ? 158 THR B HA   1 
ATOM   6739  H HB   . THR B 1 158 ? 23.192  60.933  5.189   1.00 126.37 ? 158 THR B HB   1 
ATOM   6740  H HG1  . THR B 1 158 ? 21.291  59.866  5.601   1.00 125.31 ? 158 THR B HG1  1 
ATOM   6741  H HG21 . THR B 1 158 ? 23.150  58.644  4.651   1.00 124.67 ? 158 THR B HG21 1 
ATOM   6742  H HG22 . THR B 1 158 ? 24.586  59.030  5.182   1.00 124.67 ? 158 THR B HG22 1 
ATOM   6743  H HG23 . THR B 1 158 ? 23.569  58.281  6.129   1.00 124.67 ? 158 THR B HG23 1 
ATOM   6744  N N    . SER B 1 159 ? 22.212  60.117  8.714   1.00 105.42 ? 159 SER B N    1 
ATOM   6745  C CA   . SER B 1 159 ? 21.608  59.363  9.800   1.00 106.49 ? 159 SER B CA   1 
ATOM   6746  C C    . SER B 1 159 ? 20.835  58.187  9.224   1.00 104.83 ? 159 SER B C    1 
ATOM   6747  O O    . SER B 1 159 ? 20.177  58.313  8.186   1.00 104.20 ? 159 SER B O    1 
ATOM   6748  C CB   . SER B 1 159 ? 20.666  60.241  10.624  1.00 107.25 ? 159 SER B CB   1 
ATOM   6749  O OG   . SER B 1 159 ? 19.404  60.360  9.988   1.00 108.58 ? 159 SER B OG   1 
ATOM   6750  H H    . SER B 1 159 ? 21.661  60.649  8.322   1.00 126.50 ? 159 SER B H    1 
ATOM   6751  H HA   . SER B 1 159 ? 22.301  59.031  10.392  1.00 127.79 ? 159 SER B HA   1 
ATOM   6752  H HB2  . SER B 1 159 ? 20.543  59.839  11.499  1.00 128.70 ? 159 SER B HB2  1 
ATOM   6753  H HB3  . SER B 1 159 ? 21.057  61.124  10.718  1.00 128.70 ? 159 SER B HB3  1 
ATOM   6754  H HG   . SER B 1 159 ? 18.899  60.856  10.442  1.00 130.30 ? 159 SER B HG   1 
ATOM   6755  N N    . PHE B 1 160 ? 20.920  57.042  9.902   1.00 107.74 ? 160 PHE B N    1 
ATOM   6756  C CA   . PHE B 1 160 ? 20.168  55.871  9.469   1.00 108.72 ? 160 PHE B CA   1 
ATOM   6757  C C    . PHE B 1 160 ? 18.709  56.223  9.207   1.00 107.55 ? 160 PHE B C    1 
ATOM   6758  O O    . PHE B 1 160 ? 18.138  55.808  8.195   1.00 104.56 ? 160 PHE B O    1 
ATOM   6759  C CB   . PHE B 1 160 ? 20.272  54.766  10.524  1.00 108.53 ? 160 PHE B CB   1 
ATOM   6760  C CG   . PHE B 1 160 ? 21.496  53.905  10.382  1.00 104.25 ? 160 PHE B CG   1 
ATOM   6761  C CD1  . PHE B 1 160 ? 22.661  54.412  9.824   1.00 104.35 ? 160 PHE B CD1  1 
ATOM   6762  C CD2  . PHE B 1 160 ? 21.482  52.588  10.803  1.00 101.58 ? 160 PHE B CD2  1 
ATOM   6763  C CE1  . PHE B 1 160 ? 23.785  53.623  9.690   1.00 101.04 ? 160 PHE B CE1  1 
ATOM   6764  C CE2  . PHE B 1 160 ? 22.604  51.793  10.672  1.00 104.28 ? 160 PHE B CE2  1 
ATOM   6765  C CZ   . PHE B 1 160 ? 23.756  52.311  10.114  1.00 103.16 ? 160 PHE B CZ   1 
ATOM   6766  H H    . PHE B 1 160 ? 21.400  56.921  10.605  1.00 129.29 ? 160 PHE B H    1 
ATOM   6767  H HA   . PHE B 1 160 ? 20.550  55.535  8.644   1.00 130.46 ? 160 PHE B HA   1 
ATOM   6768  H HB2  . PHE B 1 160 ? 20.299  55.176  11.403  1.00 130.24 ? 160 PHE B HB2  1 
ATOM   6769  H HB3  . PHE B 1 160 ? 19.495  54.190  10.450  1.00 130.24 ? 160 PHE B HB3  1 
ATOM   6770  H HD1  . PHE B 1 160 ? 22.684  55.296  9.536   1.00 125.23 ? 160 PHE B HD1  1 
ATOM   6771  H HD2  . PHE B 1 160 ? 20.708  52.234  11.179  1.00 121.89 ? 160 PHE B HD2  1 
ATOM   6772  H HE1  . PHE B 1 160 ? 24.560  53.974  9.315   1.00 121.25 ? 160 PHE B HE1  1 
ATOM   6773  H HE2  . PHE B 1 160 ? 22.583  50.908  10.958  1.00 125.14 ? 160 PHE B HE2  1 
ATOM   6774  H HZ   . PHE B 1 160 ? 24.512  51.776  10.025  1.00 123.79 ? 160 PHE B HZ   1 
ATOM   6775  N N    . GLU B 1 161 ? 18.102  57.015  10.096  1.00 107.49 ? 161 GLU B N    1 
ATOM   6776  C CA   . GLU B 1 161 ? 16.677  57.308  9.982   1.00 106.61 ? 161 GLU B CA   1 
ATOM   6777  C C    . GLU B 1 161 ? 16.364  58.078  8.705   1.00 105.81 ? 161 GLU B C    1 
ATOM   6778  O O    . GLU B 1 161 ? 15.335  57.837  8.062   1.00 106.34 ? 161 GLU B O    1 
ATOM   6779  C CB   . GLU B 1 161 ? 16.211  58.091  11.211  1.00 104.60 ? 161 GLU B CB   1 
ATOM   6780  C CG   . GLU B 1 161 ? 16.229  57.290  12.511  1.00 104.49 ? 161 GLU B CG   1 
ATOM   6781  C CD   . GLU B 1 161 ? 17.627  57.129  13.085  1.00 104.22 ? 161 GLU B CD   1 
ATOM   6782  O OE1  . GLU B 1 161 ? 18.421  58.089  13.003  1.00 104.81 ? 161 GLU B OE1  1 
ATOM   6783  O OE2  . GLU B 1 161 ? 17.934  56.039  13.612  1.00 103.32 ? 161 GLU B OE2  1 
ATOM   6784  H H    . GLU B 1 161 ? 18.490  57.390  10.766  1.00 128.99 ? 161 GLU B H    1 
ATOM   6785  H HA   . GLU B 1 161 ? 16.187  56.471  9.949   1.00 127.93 ? 161 GLU B HA   1 
ATOM   6786  H HB2  . GLU B 1 161 ? 16.794  58.856  11.330  1.00 125.52 ? 161 GLU B HB2  1 
ATOM   6787  H HB3  . GLU B 1 161 ? 15.300  58.388  11.062  1.00 125.52 ? 161 GLU B HB3  1 
ATOM   6788  H HG2  . GLU B 1 161 ? 15.685  57.747  13.171  1.00 125.39 ? 161 GLU B HG2  1 
ATOM   6789  H HG3  . GLU B 1 161 ? 15.871  56.404  12.341  1.00 125.39 ? 161 GLU B HG3  1 
ATOM   6790  N N    . ASN B 1 162 ? 17.236  59.013  8.322   1.00 102.86 ? 162 ASN B N    1 
ATOM   6791  C CA   . ASN B 1 162 ? 17.027  59.758  7.084   1.00 105.74 ? 162 ASN B CA   1 
ATOM   6792  C C    . ASN B 1 162 ? 17.001  58.833  5.874   1.00 105.68 ? 162 ASN B C    1 
ATOM   6793  O O    . ASN B 1 162 ? 16.253  59.077  4.921   1.00 106.38 ? 162 ASN B O    1 
ATOM   6794  C CB   . ASN B 1 162 ? 18.120  60.818  6.931   1.00 105.29 ? 162 ASN B CB   1 
ATOM   6795  C CG   . ASN B 1 162 ? 18.166  61.420  5.542   1.00 107.62 ? 162 ASN B CG   1 
ATOM   6796  O OD1  . ASN B 1 162 ? 17.137  61.576  4.882   1.00 110.18 ? 162 ASN B OD1  1 
ATOM   6797  N ND2  . ASN B 1 162 ? 19.366  61.771  5.092   1.00 108.36 ? 162 ASN B ND2  1 
ATOM   6798  H H    . ASN B 1 162 ? 17.946  59.231  8.756   1.00 123.43 ? 162 ASN B H    1 
ATOM   6799  H HA   . ASN B 1 162 ? 16.171  60.213  7.125   1.00 126.89 ? 162 ASN B HA   1 
ATOM   6800  H HB2  . ASN B 1 162 ? 17.955  61.535  7.563   1.00 126.35 ? 162 ASN B HB2  1 
ATOM   6801  H HB3  . ASN B 1 162 ? 18.982  60.410  7.110   1.00 126.35 ? 162 ASN B HB3  1 
ATOM   6802  H HD21 . ASN B 1 162 ? 20.062  61.652  5.584   1.00 130.03 ? 162 ASN B HD21 1 
ATOM   6803  H HD22 . ASN B 1 162 ? 19.448  62.117  4.310   1.00 130.03 ? 162 ASN B HD22 1 
ATOM   6804  N N    . ILE B 1 163 ? 17.796  57.764  5.899   1.00 107.17 ? 163 ILE B N    1 
ATOM   6805  C CA   . ILE B 1 163 ? 17.835  56.837  4.775   1.00 103.10 ? 163 ILE B CA   1 
ATOM   6806  C C    . ILE B 1 163 ? 16.589  55.959  4.752   1.00 103.96 ? 163 ILE B C    1 
ATOM   6807  O O    . ILE B 1 163 ? 16.056  55.654  3.682   1.00 104.82 ? 163 ILE B O    1 
ATOM   6808  C CB   . ILE B 1 163 ? 19.123  55.998  4.839   1.00 97.55  ? 163 ILE B CB   1 
ATOM   6809  C CG1  . ILE B 1 163 ? 20.353  56.910  4.902   1.00 98.52  ? 163 ILE B CG1  1 
ATOM   6810  C CG2  . ILE B 1 163 ? 19.219  55.067  3.649   1.00 95.07  ? 163 ILE B CG2  1 
ATOM   6811  C CD1  . ILE B 1 163 ? 20.417  57.952  3.798   1.00 102.76 ? 163 ILE B CD1  1 
ATOM   6812  H H    . ILE B 1 163 ? 18.317  57.556  6.550   1.00 128.60 ? 163 ILE B H    1 
ATOM   6813  H HA   . ILE B 1 163 ? 17.846  57.346  3.950   1.00 123.72 ? 163 ILE B HA   1 
ATOM   6814  H HB   . ILE B 1 163 ? 19.092  55.461  5.647   1.00 117.06 ? 163 ILE B HB   1 
ATOM   6815  H HG12 . ILE B 1 163 ? 20.347  57.381  5.751   1.00 118.23 ? 163 ILE B HG12 1 
ATOM   6816  H HG13 . ILE B 1 163 ? 21.150  56.361  4.834   1.00 118.23 ? 163 ILE B HG13 1 
ATOM   6817  H HG21 . ILE B 1 163 ? 20.046  54.563  3.708   1.00 114.08 ? 163 ILE B HG21 1 
ATOM   6818  H HG22 . ILE B 1 163 ? 18.461  54.463  3.658   1.00 114.08 ? 163 ILE B HG22 1 
ATOM   6819  H HG23 . ILE B 1 163 ? 19.211  55.595  2.834   1.00 114.08 ? 163 ILE B HG23 1 
ATOM   6820  H HD11 . ILE B 1 163 ? 21.227  58.475  3.903   1.00 123.31 ? 163 ILE B HD11 1 
ATOM   6821  H HD12 . ILE B 1 163 ? 20.423  57.502  2.939   1.00 123.31 ? 163 ILE B HD12 1 
ATOM   6822  H HD13 . ILE B 1 163 ? 19.640  58.530  3.864   1.00 123.31 ? 163 ILE B HD13 1 
ATOM   6823  N N    . ILE B 1 164 ? 16.106  55.527  5.920   1.00 105.81 ? 164 ILE B N    1 
ATOM   6824  C CA   . ILE B 1 164 ? 14.885  54.727  5.949   1.00 104.96 ? 164 ILE B CA   1 
ATOM   6825  C C    . ILE B 1 164 ? 13.718  55.531  5.387   1.00 107.72 ? 164 ILE B C    1 
ATOM   6826  O O    . ILE B 1 164 ? 12.837  54.989  4.708   1.00 105.50 ? 164 ILE B O    1 
ATOM   6827  C CB   . ILE B 1 164 ? 14.589  54.233  7.377   1.00 107.32 ? 164 ILE B CB   1 
ATOM   6828  C CG1  . ILE B 1 164 ? 15.881  53.832  8.092   1.00 106.77 ? 164 ILE B CG1  1 
ATOM   6829  C CG2  . ILE B 1 164 ? 13.617  53.049  7.325   1.00 108.57 ? 164 ILE B CG2  1 
ATOM   6830  C CD1  . ILE B 1 164 ? 15.668  53.008  9.343   1.00 102.13 ? 164 ILE B CD1  1 
ATOM   6831  H H    . ILE B 1 164 ? 16.458  55.681  6.690   1.00 126.97 ? 164 ILE B H    1 
ATOM   6832  H HA   . ILE B 1 164 ? 15.019  53.947  5.388   1.00 125.95 ? 164 ILE B HA   1 
ATOM   6833  H HB   . ILE B 1 164 ? 14.182  54.959  7.875   1.00 128.78 ? 164 ILE B HB   1 
ATOM   6834  H HG12 . ILE B 1 164 ? 16.423  53.306  7.482   1.00 128.12 ? 164 ILE B HG12 1 
ATOM   6835  H HG13 . ILE B 1 164 ? 16.357  54.637  8.348   1.00 128.12 ? 164 ILE B HG13 1 
ATOM   6836  H HG21 . ILE B 1 164 ? 13.135  52.999  8.165   1.00 130.28 ? 164 ILE B HG21 1 
ATOM   6837  H HG22 . ILE B 1 164 ? 12.994  53.184  6.593   1.00 130.28 ? 164 ILE B HG22 1 
ATOM   6838  H HG23 . ILE B 1 164 ? 14.122  52.233  7.183   1.00 130.28 ? 164 ILE B HG23 1 
ATOM   6839  H HD11 . ILE B 1 164 ? 16.427  52.417  9.465   1.00 122.55 ? 164 ILE B HD11 1 
ATOM   6840  H HD12 . ILE B 1 164 ? 15.587  53.604  10.103  1.00 122.55 ? 164 ILE B HD12 1 
ATOM   6841  H HD13 . ILE B 1 164 ? 14.856  52.487  9.243   1.00 122.55 ? 164 ILE B HD13 1 
ATOM   6842  N N    . ASP B 1 165 ? 13.696  56.838  5.658   1.00 113.07 ? 165 ASP B N    1 
ATOM   6843  C CA   . ASP B 1 165 ? 12.643  57.690  5.117   1.00 114.48 ? 165 ASP B CA   1 
ATOM   6844  C C    . ASP B 1 165 ? 12.787  57.836  3.608   1.00 116.70 ? 165 ASP B C    1 
ATOM   6845  O O    . ASP B 1 165 ? 11.805  57.715  2.867   1.00 122.15 ? 165 ASP B O    1 
ATOM   6846  C CB   . ASP B 1 165 ? 12.676  59.061  5.797   1.00 119.41 ? 165 ASP B CB   1 
ATOM   6847  C CG   . ASP B 1 165 ? 12.452  58.976  7.297   1.00 120.82 ? 165 ASP B CG   1 
ATOM   6848  O OD1  . ASP B 1 165 ? 12.283  57.850  7.814   1.00 119.76 ? 165 ASP B OD1  1 
ATOM   6849  O OD2  . ASP B 1 165 ? 12.446  60.037  7.959   1.00 117.22 ? 165 ASP B OD2  1 
ATOM   6850  H H    . ASP B 1 165 ? 14.272  57.248  6.147   1.00 135.69 ? 165 ASP B H    1 
ATOM   6851  H HA   . ASP B 1 165 ? 11.782  57.285  5.304   1.00 137.38 ? 165 ASP B HA   1 
ATOM   6852  H HB2  . ASP B 1 165 ? 13.542  59.469  5.645   1.00 143.29 ? 165 ASP B HB2  1 
ATOM   6853  H HB3  . ASP B 1 165 ? 11.976  59.618  5.420   1.00 143.29 ? 165 ASP B HB3  1 
ATOM   6854  N N    . LEU B 1 166 ? 14.008  58.095  3.132   1.00 109.48 ? 166 LEU B N    1 
ATOM   6855  C CA   . LEU B 1 166 ? 14.224  58.205  1.692   1.00 109.41 ? 166 LEU B CA   1 
ATOM   6856  C C    . LEU B 1 166 ? 13.800  56.928  0.980   1.00 107.31 ? 166 LEU B C    1 
ATOM   6857  O O    . LEU B 1 166 ? 13.192  56.979  -0.096  1.00 108.73 ? 166 LEU B O    1 
ATOM   6858  C CB   . LEU B 1 166 ? 15.690  58.518  1.396   1.00 109.63 ? 166 LEU B CB   1 
ATOM   6859  C CG   . LEU B 1 166 ? 16.041  59.998  1.222   1.00 112.66 ? 166 LEU B CG   1 
ATOM   6860  C CD1  . LEU B 1 166 ? 17.559  60.185  1.239   1.00 110.22 ? 166 LEU B CD1  1 
ATOM   6861  C CD2  . LEU B 1 166 ? 15.446  60.569  -0.058  1.00 110.36 ? 166 LEU B CD2  1 
ATOM   6862  H H    . LEU B 1 166 ? 14.713  58.209  3.612   1.00 131.38 ? 166 LEU B H    1 
ATOM   6863  H HA   . LEU B 1 166 ? 13.688  58.939  1.352   1.00 131.29 ? 166 LEU B HA   1 
ATOM   6864  H HB2  . LEU B 1 166 ? 16.225  58.181  2.132   1.00 131.56 ? 166 LEU B HB2  1 
ATOM   6865  H HB3  . LEU B 1 166 ? 15.935  58.067  0.574   1.00 131.56 ? 166 LEU B HB3  1 
ATOM   6866  H HG   . LEU B 1 166 ? 15.659  60.494  1.962   1.00 135.20 ? 166 LEU B HG   1 
ATOM   6867  H HD11 . LEU B 1 166 ? 17.762  61.127  1.124   1.00 132.26 ? 166 LEU B HD11 1 
ATOM   6868  H HD12 . LEU B 1 166 ? 17.906  59.873  2.089   1.00 132.26 ? 166 LEU B HD12 1 
ATOM   6869  H HD13 . LEU B 1 166 ? 17.948  59.672  0.514   1.00 132.26 ? 166 LEU B HD13 1 
ATOM   6870  H HD21 . LEU B 1 166 ? 15.228  61.503  0.085   1.00 132.43 ? 166 LEU B HD21 1 
ATOM   6871  H HD22 . LEU B 1 166 ? 16.096  60.486  -0.773  1.00 132.43 ? 166 LEU B HD22 1 
ATOM   6872  H HD23 . LEU B 1 166 ? 14.643  60.073  -0.281  1.00 132.43 ? 166 LEU B HD23 1 
ATOM   6873  N N    . VAL B 1 167 ? 14.112  55.770  1.564   1.00 107.04 ? 167 VAL B N    1 
ATOM   6874  C CA   . VAL B 1 167 ? 13.690  54.504  0.974   1.00 106.56 ? 167 VAL B CA   1 
ATOM   6875  C C    . VAL B 1 167 ? 12.170  54.441  0.905   1.00 109.98 ? 167 VAL B C    1 
ATOM   6876  O O    . VAL B 1 167 ? 11.591  54.135  -0.143  1.00 114.61 ? 167 VAL B O    1 
ATOM   6877  C CB   . VAL B 1 167 ? 14.266  53.319  1.769   1.00 102.75 ? 167 VAL B CB   1 
ATOM   6878  C CG1  . VAL B 1 167 ? 13.720  52.003  1.229   1.00 98.72  ? 167 VAL B CG1  1 
ATOM   6879  C CG2  . VAL B 1 167 ? 15.784  53.334  1.713   1.00 101.04 ? 167 VAL B CG2  1 
ATOM   6880  H H    . VAL B 1 167 ? 14.562  55.693  2.293   1.00 128.44 ? 167 VAL B H    1 
ATOM   6881  H HA   . VAL B 1 167 ? 14.037  54.453  0.070   1.00 127.87 ? 167 VAL B HA   1 
ATOM   6882  H HB   . VAL B 1 167 ? 13.996  53.398  2.697   1.00 123.29 ? 167 VAL B HB   1 
ATOM   6883  H HG11 . VAL B 1 167 ? 14.268  51.275  1.560   1.00 118.47 ? 167 VAL B HG11 1 
ATOM   6884  H HG12 . VAL B 1 167 ? 12.805  51.893  1.532   1.00 118.47 ? 167 VAL B HG12 1 
ATOM   6885  H HG13 . VAL B 1 167 ? 13.747  52.024  0.260   1.00 118.47 ? 167 VAL B HG13 1 
ATOM   6886  H HG21 . VAL B 1 167 ? 16.133  52.895  2.504   1.00 121.26 ? 167 VAL B HG21 1 
ATOM   6887  H HG22 . VAL B 1 167 ? 16.075  52.863  0.917   1.00 121.26 ? 167 VAL B HG22 1 
ATOM   6888  H HG23 . VAL B 1 167 ? 16.089  54.255  1.684   1.00 121.26 ? 167 VAL B HG23 1 
ATOM   6889  N N    . LYS B 1 168 ? 11.500  54.737  2.022   1.00 107.80 ? 168 LYS B N    1 
ATOM   6890  C CA   . LYS B 1 168 ? 10.041  54.729  2.028   1.00 110.38 ? 168 LYS B CA   1 
ATOM   6891  C C    . LYS B 1 168 ? 9.482   55.715  1.012   1.00 111.82 ? 168 LYS B C    1 
ATOM   6892  O O    . LYS B 1 168 ? 8.384   55.506  0.485   1.00 113.82 ? 168 LYS B O    1 
ATOM   6893  C CB   . LYS B 1 168 ? 9.521   55.026  3.440   1.00 114.28 ? 168 LYS B CB   1 
ATOM   6894  C CG   . LYS B 1 168 ? 9.067   56.460  3.693   1.00 115.23 ? 168 LYS B CG   1 
ATOM   6895  C CD   . LYS B 1 168 ? 7.577   56.647  3.412   1.00 116.59 ? 168 LYS B CD   1 
ATOM   6896  C CE   . LYS B 1 168 ? 7.189   58.121  3.447   1.00 119.56 ? 168 LYS B CE   1 
ATOM   6897  N NZ   . LYS B 1 168 ? 5.766   58.345  3.063   1.00 120.71 ? 168 LYS B NZ   1 
ATOM   6898  H H    . LYS B 1 168 ? 11.862  54.943  2.775   1.00 129.36 ? 168 LYS B H    1 
ATOM   6899  H HA   . LYS B 1 168 ? 9.721   53.846  1.785   1.00 132.45 ? 168 LYS B HA   1 
ATOM   6900  H HB2  . LYS B 1 168 ? 8.760   54.449  3.612   1.00 137.14 ? 168 LYS B HB2  1 
ATOM   6901  H HB3  . LYS B 1 168 ? 10.231  54.834  4.072   1.00 137.14 ? 168 LYS B HB3  1 
ATOM   6902  H HG2  . LYS B 1 168 ? 9.231   56.688  4.621   1.00 138.28 ? 168 LYS B HG2  1 
ATOM   6903  H HG3  . LYS B 1 168 ? 9.563   57.059  3.112   1.00 138.28 ? 168 LYS B HG3  1 
ATOM   6904  H HD2  . LYS B 1 168 ? 7.369   56.298  2.531   1.00 139.91 ? 168 LYS B HD2  1 
ATOM   6905  H HD3  . LYS B 1 168 ? 7.061   56.179  4.086   1.00 139.91 ? 168 LYS B HD3  1 
ATOM   6906  H HE2  . LYS B 1 168 ? 7.314   58.461  4.347   1.00 143.47 ? 168 LYS B HE2  1 
ATOM   6907  H HE3  . LYS B 1 168 ? 7.749   58.613  2.827   1.00 143.47 ? 168 LYS B HE3  1 
ATOM   6908  H HZ1  . LYS B 1 168 ? 5.573   59.213  3.102   1.00 144.85 ? 168 LYS B HZ1  1 
ATOM   6909  H HZ2  . LYS B 1 168 ? 5.626   58.056  2.233   1.00 144.85 ? 168 LYS B HZ2  1 
ATOM   6910  H HZ3  . LYS B 1 168 ? 5.228   57.904  3.617   1.00 144.85 ? 168 LYS B HZ3  1 
ATOM   6911  N N    . LYS B 1 169 ? 10.221  56.793  0.726   1.00 113.72 ? 169 LYS B N    1 
ATOM   6912  C CA   . LYS B 1 169 ? 9.826   57.704  -0.343  1.00 113.81 ? 169 LYS B CA   1 
ATOM   6913  C C    . LYS B 1 169 ? 9.925   57.028  -1.706  1.00 114.08 ? 169 LYS B C    1 
ATOM   6914  O O    . LYS B 1 169 ? 9.115   57.306  -2.598  1.00 116.94 ? 169 LYS B O    1 
ATOM   6915  C CB   . LYS B 1 169 ? 10.702  58.958  -0.319  1.00 112.98 ? 169 LYS B CB   1 
ATOM   6916  C CG   . LYS B 1 169 ? 10.004  60.238  0.142   1.00 114.96 ? 169 LYS B CG   1 
ATOM   6917  C CD   . LYS B 1 169 ? 8.766   60.588  -0.691  1.00 115.67 ? 169 LYS B CD   1 
ATOM   6918  C CE   . LYS B 1 169 ? 9.057   60.665  -2.187  1.00 119.24 ? 169 LYS B CE   1 
ATOM   6919  N NZ   . LYS B 1 169 ? 7.809   60.856  -2.989  1.00 117.49 ? 169 LYS B NZ   1 
ATOM   6920  H H    . LYS B 1 169 ? 10.946  57.015  1.133   1.00 136.47 ? 169 LYS B H    1 
ATOM   6921  H HA   . LYS B 1 169 ? 8.906   57.977  -0.198  1.00 136.58 ? 169 LYS B HA   1 
ATOM   6922  H HB2  . LYS B 1 169 ? 11.445  58.800  0.284   1.00 135.58 ? 169 LYS B HB2  1 
ATOM   6923  H HB3  . LYS B 1 169 ? 11.032  59.116  -1.218  1.00 135.58 ? 169 LYS B HB3  1 
ATOM   6924  H HG2  . LYS B 1 169 ? 9.721   60.128  1.063   1.00 137.95 ? 169 LYS B HG2  1 
ATOM   6925  H HG3  . LYS B 1 169 ? 10.627  60.978  0.073   1.00 137.95 ? 169 LYS B HG3  1 
ATOM   6926  H HD2  . LYS B 1 169 ? 8.090   59.906  -0.554  1.00 138.80 ? 169 LYS B HD2  1 
ATOM   6927  H HD3  . LYS B 1 169 ? 8.428   61.452  -0.408  1.00 138.80 ? 169 LYS B HD3  1 
ATOM   6928  H HE2  . LYS B 1 169 ? 9.646   61.416  -2.359  1.00 143.09 ? 169 LYS B HE2  1 
ATOM   6929  H HE3  . LYS B 1 169 ? 9.479   59.840  -2.473  1.00 143.09 ? 169 LYS B HE3  1 
ATOM   6930  H HZ1  . LYS B 1 169 ? 8.007   60.897  -3.855  1.00 140.98 ? 169 LYS B HZ1  1 
ATOM   6931  H HZ2  . LYS B 1 169 ? 7.252   60.176  -2.852  1.00 140.98 ? 169 LYS B HZ2  1 
ATOM   6932  H HZ3  . LYS B 1 169 ? 7.405   61.612  -2.748  1.00 140.98 ? 169 LYS B HZ3  1 
ATOM   6933  N N    . TYR B 1 170 ? 10.908  56.142  -1.883  1.00 112.92 ? 170 TYR B N    1 
ATOM   6934  C CA   . TYR B 1 170 ? 11.096  55.471  -3.166  1.00 112.46 ? 170 TYR B CA   1 
ATOM   6935  C C    . TYR B 1 170 ? 9.928   54.543  -3.476  1.00 114.47 ? 170 TYR B C    1 
ATOM   6936  O O    . TYR B 1 170 ? 9.399   54.547  -4.593  1.00 118.81 ? 170 TYR B O    1 
ATOM   6937  C CB   . TYR B 1 170 ? 12.417  54.697  -3.148  1.00 109.63 ? 170 TYR B CB   1 
ATOM   6938  C CG   . TYR B 1 170 ? 12.905  54.211  -4.495  1.00 105.13 ? 170 TYR B CG   1 
ATOM   6939  C CD1  . TYR B 1 170 ? 13.640  55.042  -5.331  1.00 101.30 ? 170 TYR B CD1  1 
ATOM   6940  C CD2  . TYR B 1 170 ? 12.649  52.915  -4.921  1.00 104.25 ? 170 TYR B CD2  1 
ATOM   6941  C CE1  . TYR B 1 170 ? 14.098  54.599  -6.558  1.00 99.55  ? 170 TYR B CE1  1 
ATOM   6942  C CE2  . TYR B 1 170 ? 13.101  52.463  -6.149  1.00 104.20 ? 170 TYR B CE2  1 
ATOM   6943  C CZ   . TYR B 1 170 ? 13.824  53.309  -6.963  1.00 100.29 ? 170 TYR B CZ   1 
ATOM   6944  O OH   . TYR B 1 170 ? 14.276  52.857  -8.182  1.00 97.54  ? 170 TYR B OH   1 
ATOM   6945  H H    . TYR B 1 170 ? 11.475  55.913  -1.278  1.00 135.51 ? 170 TYR B H    1 
ATOM   6946  H HA   . TYR B 1 170 ? 11.141  56.136  -3.871  1.00 134.94 ? 170 TYR B HA   1 
ATOM   6947  H HB2  . TYR B 1 170 ? 13.105  55.275  -2.783  1.00 131.56 ? 170 TYR B HB2  1 
ATOM   6948  H HB3  . TYR B 1 170 ? 12.305  53.916  -2.583  1.00 131.56 ? 170 TYR B HB3  1 
ATOM   6949  H HD1  . TYR B 1 170 ? 13.828  55.911  -5.060  1.00 121.56 ? 170 TYR B HD1  1 
ATOM   6950  H HD2  . TYR B 1 170 ? 12.167  52.340  -4.372  1.00 125.10 ? 170 TYR B HD2  1 
ATOM   6951  H HE1  . TYR B 1 170 ? 14.587  55.168  -7.108  1.00 119.46 ? 170 TYR B HE1  1 
ATOM   6952  H HE2  . TYR B 1 170 ? 12.917  51.594  -6.423  1.00 125.04 ? 170 TYR B HE2  1 
ATOM   6953  H HH   . TYR B 1 170 ? 14.028  52.063  -8.303  1.00 117.05 ? 170 TYR B HH   1 
ATOM   6954  N N    . LEU B 1 171 ? 9.508   53.744  -2.496  1.00 116.12 ? 171 LEU B N    1 
ATOM   6955  C CA   . LEU B 1 171 ? 8.422   52.793  -2.679  1.00 120.99 ? 171 LEU B CA   1 
ATOM   6956  C C    . LEU B 1 171 ? 7.040   53.433  -2.556  1.00 124.21 ? 171 LEU B C    1 
ATOM   6957  O O    . LEU B 1 171 ? 6.051   52.712  -2.377  1.00 127.67 ? 171 LEU B O    1 
ATOM   6958  C CB   . LEU B 1 171 ? 8.556   51.648  -1.670  1.00 120.14 ? 171 LEU B CB   1 
ATOM   6959  C CG   . LEU B 1 171 ? 9.950   51.037  -1.531  1.00 115.52 ? 171 LEU B CG   1 
ATOM   6960  C CD1  . LEU B 1 171 ? 10.599  51.442  -0.215  1.00 108.73 ? 171 LEU B CD1  1 
ATOM   6961  C CD2  . LEU B 1 171 ? 9.895   49.516  -1.651  1.00 116.37 ? 171 LEU B CD2  1 
ATOM   6962  H H    . LEU B 1 171 ? 9.844   53.738  -1.704  1.00 139.35 ? 171 LEU B H    1 
ATOM   6963  H HA   . LEU B 1 171 ? 8.493   52.419  -3.571  1.00 145.19 ? 171 LEU B HA   1 
ATOM   6964  H HB2  . LEU B 1 171 ? 8.301   51.983  -0.797  1.00 144.17 ? 171 LEU B HB2  1 
ATOM   6965  H HB3  . LEU B 1 171 ? 7.955   50.935  -1.940  1.00 144.17 ? 171 LEU B HB3  1 
ATOM   6966  H HG   . LEU B 1 171 ? 10.503  51.376  -2.253  1.00 138.62 ? 171 LEU B HG   1 
ATOM   6967  H HD11 . LEU B 1 171 ? 11.551  51.564  -0.356  1.00 130.48 ? 171 LEU B HD11 1 
ATOM   6968  H HD12 . LEU B 1 171 ? 10.201  52.272  0.091   1.00 130.48 ? 171 LEU B HD12 1 
ATOM   6969  H HD13 . LEU B 1 171 ? 10.449  50.742  0.440   1.00 130.48 ? 171 LEU B HD13 1 
ATOM   6970  H HD21 . LEU B 1 171 ? 10.791  49.158  -1.548  1.00 139.65 ? 171 LEU B HD21 1 
ATOM   6971  H HD22 . LEU B 1 171 ? 9.317   49.165  -0.955  1.00 139.65 ? 171 LEU B HD22 1 
ATOM   6972  H HD23 . LEU B 1 171 ? 9.543   49.280  -2.524  1.00 139.65 ? 171 LEU B HD23 1 
ATOM   6973  N N    . SER B 1 172 ? 6.946   54.760  -2.651  1.00 123.24 ? 172 SER B N    1 
ATOM   6974  C CA   . SER B 1 172 ? 5.655   55.436  -2.602  1.00 126.27 ? 172 SER B CA   1 
ATOM   6975  C C    . SER B 1 172 ? 4.798   55.177  -3.839  1.00 132.36 ? 172 SER B C    1 
ATOM   6976  O O    . SER B 1 172 ? 3.667   55.666  -3.894  1.00 131.72 ? 172 SER B O    1 
ATOM   6977  C CB   . SER B 1 172 ? 5.860   56.943  -2.432  1.00 123.93 ? 172 SER B CB   1 
ATOM   6978  O OG   . SER B 1 172 ? 6.923   57.215  -1.535  1.00 120.42 ? 172 SER B OG   1 
ATOM   6979  H H    . SER B 1 172 ? 7.618   55.289  -2.745  1.00 147.89 ? 172 SER B H    1 
ATOM   6980  H HA   . SER B 1 172 ? 5.169   55.108  -1.830  1.00 151.52 ? 172 SER B HA   1 
ATOM   6981  H HB2  . SER B 1 172 ? 6.070   57.332  -3.295  1.00 148.72 ? 172 SER B HB2  1 
ATOM   6982  H HB3  . SER B 1 172 ? 5.045   57.334  -2.081  1.00 148.72 ? 172 SER B HB3  1 
ATOM   6983  H HG   . SER B 1 172 ? 7.025   58.045  -1.454  1.00 144.51 ? 172 SER B HG   1 
ATOM   6984  N N    . ASN B 1 173 ? 5.307   54.443  -4.829  1.00 139.87 ? 173 ASN B N    1 
ATOM   6985  C CA   . ASN B 1 173 ? 4.525   54.048  -5.994  1.00 139.42 ? 173 ASN B CA   1 
ATOM   6986  C C    . ASN B 1 173 ? 4.657   52.556  -6.271  1.00 140.03 ? 173 ASN B C    1 
ATOM   6987  O O    . ASN B 1 173 ? 4.256   52.102  -7.351  1.00 140.45 ? 173 ASN B O    1 
ATOM   6988  C CB   . ASN B 1 173 ? 4.941   54.875  -7.229  1.00 141.31 ? 173 ASN B CB   1 
ATOM   6989  C CG   . ASN B 1 173 ? 6.119   54.281  -7.978  1.00 144.45 ? 173 ASN B CG   1 
ATOM   6990  O OD1  . ASN B 1 173 ? 6.018   53.208  -8.571  1.00 148.29 ? 173 ASN B OD1  1 
ATOM   6991  N ND2  . ASN B 1 173 ? 7.239   54.994  -7.979  1.00 144.23 ? 173 ASN B ND2  1 
ATOM   6992  H H    . ASN B 1 173 ? 6.118   54.157  -4.847  1.00 167.85 ? 173 ASN B H    1 
ATOM   6993  H HA   . ASN B 1 173 ? 3.587   54.235  -5.837  1.00 167.30 ? 173 ASN B HA   1 
ATOM   6994  H HB2  . ASN B 1 173 ? 4.191   54.922  -7.843  1.00 169.57 ? 173 ASN B HB2  1 
ATOM   6995  H HB3  . ASN B 1 173 ? 5.189   55.767  -6.941  1.00 169.57 ? 173 ASN B HB3  1 
ATOM   6996  H HD21 . ASN B 1 173 ? 7.268   55.750  -7.568  1.00 173.07 ? 173 ASN B HD21 1 
ATOM   6997  H HD22 . ASN B 1 173 ? 7.936   54.701  -8.389  1.00 173.07 ? 173 ASN B HD22 1 
ATOM   6998  N N    . GLU B 1 174 ? 5.171   51.783  -5.317  1.00 137.20 ? 174 GLU B N    1 
ATOM   6999  C CA   . GLU B 1 174 ? 5.469   50.372  -5.500  1.00 137.35 ? 174 GLU B CA   1 
ATOM   7000  C C    . GLU B 1 174 ? 4.736   49.543  -4.455  1.00 136.97 ? 174 GLU B C    1 
ATOM   7001  O O    . GLU B 1 174 ? 4.718   49.891  -3.270  1.00 134.49 ? 174 GLU B O    1 
ATOM   7002  C CB   . GLU B 1 174 ? 6.981   50.118  -5.394  1.00 135.14 ? 174 GLU B CB   1 
ATOM   7003  C CG   . GLU B 1 174 ? 7.543   49.170  -6.440  1.00 136.10 ? 174 GLU B CG   1 
ATOM   7004  C CD   . GLU B 1 174 ? 7.666   47.736  -5.941  1.00 138.22 ? 174 GLU B CD   1 
ATOM   7005  O OE1  . GLU B 1 174 ? 7.585   47.506  -4.713  1.00 136.18 ? 174 GLU B OE1  1 
ATOM   7006  O OE2  . GLU B 1 174 ? 7.847   46.833  -6.784  1.00 139.63 ? 174 GLU B OE2  1 
ATOM   7007  H H    . GLU B 1 174 ? 5.362   52.067  -4.528  1.00 164.64 ? 174 GLU B H    1 
ATOM   7008  H HA   . GLU B 1 174 ? 5.163   50.088  -6.376  1.00 164.83 ? 174 GLU B HA   1 
ATOM   7009  H HB2  . GLU B 1 174 ? 7.442   50.965  -5.491  1.00 162.16 ? 174 GLU B HB2  1 
ATOM   7010  H HB3  . GLU B 1 174 ? 7.168   49.735  -4.523  1.00 162.16 ? 174 GLU B HB3  1 
ATOM   7011  H HG2  . GLU B 1 174 ? 6.955   49.168  -7.211  1.00 163.33 ? 174 GLU B HG2  1 
ATOM   7012  H HG3  . GLU B 1 174 ? 8.427   49.473  -6.697  1.00 163.33 ? 174 GLU B HG3  1 
ATOM   7013  N N    . GLU B 1 175 ? 4.133   48.444  -4.904  1.00 138.15 ? 175 GLU B N    1 
ATOM   7014  C CA   . GLU B 1 175 ? 3.482   47.495  -4.007  1.00 135.55 ? 175 GLU B CA   1 
ATOM   7015  C C    . GLU B 1 175 ? 4.545   46.558  -3.444  1.00 135.26 ? 175 GLU B C    1 
ATOM   7016  O O    . GLU B 1 175 ? 5.074   45.703  -4.163  1.00 136.51 ? 175 GLU B O    1 
ATOM   7017  C CB   . GLU B 1 175 ? 2.398   46.713  -4.741  1.00 133.63 ? 175 GLU B CB   1 
ATOM   7018  C CG   . GLU B 1 175 ? 1.130   47.504  -5.015  1.00 135.61 ? 175 GLU B CG   1 
ATOM   7019  C CD   . GLU B 1 175 ? 0.514   48.090  -3.758  1.00 136.47 ? 175 GLU B CD   1 
ATOM   7020  O OE1  . GLU B 1 175 ? 0.399   47.358  -2.751  1.00 134.52 ? 175 GLU B OE1  1 
ATOM   7021  O OE2  . GLU B 1 175 ? 0.150   49.283  -3.778  1.00 136.83 ? 175 GLU B OE2  1 
ATOM   7022  H H    . GLU B 1 175 ? 4.087   48.224  -5.735  1.00 165.78 ? 175 GLU B H    1 
ATOM   7023  H HA   . GLU B 1 175 ? 3.063   47.975  -3.276  1.00 162.66 ? 175 GLU B HA   1 
ATOM   7024  H HB2  . GLU B 1 175 ? 2.752   46.421  -5.596  1.00 160.35 ? 175 GLU B HB2  1 
ATOM   7025  H HB3  . GLU B 1 175 ? 2.154   45.944  -4.203  1.00 160.35 ? 175 GLU B HB3  1 
ATOM   7026  H HG2  . GLU B 1 175 ? 1.339   48.237  -5.615  1.00 162.74 ? 175 GLU B HG2  1 
ATOM   7027  H HG3  . GLU B 1 175 ? 0.474   46.917  -5.424  1.00 162.74 ? 175 GLU B HG3  1 
ATOM   7028  N N    . TYR B 1 176 ? 4.864   46.720  -2.162  1.00 133.19 ? 176 TYR B N    1 
ATOM   7029  C CA   . TYR B 1 176 ? 5.873   45.913  -1.489  1.00 131.56 ? 176 TYR B CA   1 
ATOM   7030  C C    . TYR B 1 176 ? 5.277   45.335  -0.216  1.00 130.65 ? 176 TYR B C    1 
ATOM   7031  O O    . TYR B 1 176 ? 4.684   46.066  0.583   1.00 130.32 ? 176 TYR B O    1 
ATOM   7032  C CB   . TYR B 1 176 ? 7.122   46.743  -1.163  1.00 131.07 ? 176 TYR B CB   1 
ATOM   7033  C CG   . TYR B 1 176 ? 6.896   47.820  -0.122  1.00 129.14 ? 176 TYR B CG   1 
ATOM   7034  C CD1  . TYR B 1 176 ? 6.339   49.044  -0.470  1.00 129.02 ? 176 TYR B CD1  1 
ATOM   7035  C CD2  . TYR B 1 176 ? 7.238   47.611  1.209   1.00 125.67 ? 176 TYR B CD2  1 
ATOM   7036  C CE1  . TYR B 1 176 ? 6.129   50.029  0.477   1.00 127.25 ? 176 TYR B CE1  1 
ATOM   7037  C CE2  . TYR B 1 176 ? 7.031   48.591  2.162   1.00 125.36 ? 176 TYR B CE2  1 
ATOM   7038  C CZ   . TYR B 1 176 ? 6.477   49.798  1.791   1.00 126.92 ? 176 TYR B CZ   1 
ATOM   7039  O OH   . TYR B 1 176 ? 6.269   50.776  2.736   1.00 128.51 ? 176 TYR B OH   1 
ATOM   7040  H H    . TYR B 1 176 ? 4.500   47.307  -1.649  1.00 159.83 ? 176 TYR B H    1 
ATOM   7041  H HA   . TYR B 1 176 ? 6.139   45.179  -2.065  1.00 157.87 ? 176 TYR B HA   1 
ATOM   7042  H HB2  . TYR B 1 176 ? 7.811   46.149  -0.827  1.00 157.28 ? 176 TYR B HB2  1 
ATOM   7043  H HB3  . TYR B 1 176 ? 7.427   47.178  -1.975  1.00 157.28 ? 176 TYR B HB3  1 
ATOM   7044  H HD1  . TYR B 1 176 ? 6.104   49.204  -1.355  1.00 154.83 ? 176 TYR B HD1  1 
ATOM   7045  H HD2  . TYR B 1 176 ? 7.613   46.799  1.462   1.00 150.80 ? 176 TYR B HD2  1 
ATOM   7046  H HE1  . TYR B 1 176 ? 5.755   50.844  0.229   1.00 152.70 ? 176 TYR B HE1  1 
ATOM   7047  H HE2  . TYR B 1 176 ? 7.263   48.437  3.049   1.00 150.43 ? 176 TYR B HE2  1 
ATOM   7048  H HH   . TYR B 1 176 ? 6.513   50.502  3.491   1.00 154.22 ? 176 TYR B HH   1 
ATOM   7049  N N    . SER B 1 177 ? 5.425   44.019  -0.037  1.00 130.86 ? 177 SER B N    1 
ATOM   7050  C CA   . SER B 1 177 ? 4.993   43.391  1.206   1.00 129.66 ? 177 SER B CA   1 
ATOM   7051  C C    . SER B 1 177 ? 5.922   43.750  2.358   1.00 128.50 ? 177 SER B C    1 
ATOM   7052  O O    . SER B 1 177 ? 5.472   43.879  3.502   1.00 129.93 ? 177 SER B O    1 
ATOM   7053  C CB   . SER B 1 177 ? 4.928   41.874  1.033   1.00 127.56 ? 177 SER B CB   1 
ATOM   7054  O OG   . SER B 1 177 ? 3.860   41.502  0.180   1.00 126.98 ? 177 SER B OG   1 
ATOM   7055  H H    . SER B 1 177 ? 5.768   43.479  -0.612  1.00 157.03 ? 177 SER B H    1 
ATOM   7056  H HA   . SER B 1 177 ? 4.102   43.706  1.425   1.00 155.59 ? 177 SER B HA   1 
ATOM   7057  H HB2  . SER B 1 177 ? 5.762   41.566  0.645   1.00 153.07 ? 177 SER B HB2  1 
ATOM   7058  H HB3  . SER B 1 177 ? 4.794   41.464  1.902   1.00 153.07 ? 177 SER B HB3  1 
ATOM   7059  H HG   . SER B 1 177 ? 3.828   40.665  0.108   1.00 152.37 ? 177 SER B HG   1 
ATOM   7060  N N    . ALA B 1 178 ? 7.211   43.920  2.073   1.00 127.88 ? 178 ALA B N    1 
ATOM   7061  C CA   . ALA B 1 178 ? 8.208   44.278  3.073   1.00 125.64 ? 178 ALA B CA   1 
ATOM   7062  C C    . ALA B 1 178 ? 9.486   44.651  2.337   1.00 125.47 ? 178 ALA B C    1 
ATOM   7063  O O    . ALA B 1 178 ? 9.725   44.209  1.210   1.00 123.83 ? 178 ALA B O    1 
ATOM   7064  C CB   . ALA B 1 178 ? 8.458   43.138  4.059   1.00 124.69 ? 178 ALA B CB   1 
ATOM   7065  H H    . ALA B 1 178 ? 7.541   43.831  1.284   1.00 153.45 ? 178 ALA B H    1 
ATOM   7066  H HA   . ALA B 1 178 ? 7.906   45.047  3.582   1.00 150.77 ? 178 ALA B HA   1 
ATOM   7067  H HB1  . ALA B 1 178 ? 9.158   43.402  4.676   1.00 149.63 ? 178 ALA B HB1  1 
ATOM   7068  H HB2  . ALA B 1 178 ? 7.639   42.956  4.546   1.00 149.63 ? 178 ALA B HB2  1 
ATOM   7069  H HB3  . ALA B 1 178 ? 8.732   42.349  3.566   1.00 149.63 ? 178 ALA B HB3  1 
ATOM   7070  N N    . PHE B 1 179 ? 10.309  45.470  2.989   1.00 115.18 ? 179 PHE B N    1 
ATOM   7071  C CA   . PHE B 1 179 ? 11.591  45.881  2.429   1.00 109.77 ? 179 PHE B CA   1 
ATOM   7072  C C    . PHE B 1 179 ? 12.635  45.901  3.537   1.00 105.58 ? 179 PHE B C    1 
ATOM   7073  O O    . PHE B 1 179 ? 12.309  45.933  4.725   1.00 104.47 ? 179 PHE B O    1 
ATOM   7074  C CB   . PHE B 1 179 ? 11.495  47.254  1.735   1.00 104.93 ? 179 PHE B CB   1 
ATOM   7075  C CG   . PHE B 1 179 ? 11.535  48.429  2.674   1.00 103.94 ? 179 PHE B CG   1 
ATOM   7076  C CD1  . PHE B 1 179 ? 12.745  48.943  3.112   1.00 99.09  ? 179 PHE B CD1  1 
ATOM   7077  C CD2  . PHE B 1 179 ? 10.364  49.034  3.098   1.00 108.40 ? 179 PHE B CD2  1 
ATOM   7078  C CE1  . PHE B 1 179 ? 12.785  50.025  3.971   1.00 99.95  ? 179 PHE B CE1  1 
ATOM   7079  C CE2  . PHE B 1 179 ? 10.398  50.119  3.953   1.00 108.81 ? 179 PHE B CE2  1 
ATOM   7080  C CZ   . PHE B 1 179 ? 11.610  50.615  4.389   1.00 104.29 ? 179 PHE B CZ   1 
ATOM   7081  H H    . PHE B 1 179 ? 10.144  45.803  3.764   1.00 138.21 ? 179 PHE B H    1 
ATOM   7082  H HA   . PHE B 1 179 ? 11.879  45.236  1.765   1.00 131.73 ? 179 PHE B HA   1 
ATOM   7083  H HB2  . PHE B 1 179 ? 12.240  47.343  1.121   1.00 125.92 ? 179 PHE B HB2  1 
ATOM   7084  H HB3  . PHE B 1 179 ? 10.657  47.297  1.248   1.00 125.92 ? 179 PHE B HB3  1 
ATOM   7085  H HD1  . PHE B 1 179 ? 13.540  48.556  2.825   1.00 118.90 ? 179 PHE B HD1  1 
ATOM   7086  H HD2  . PHE B 1 179 ? 9.545   48.705  2.805   1.00 130.08 ? 179 PHE B HD2  1 
ATOM   7087  H HE1  . PHE B 1 179 ? 13.603  50.355  4.267   1.00 119.94 ? 179 PHE B HE1  1 
ATOM   7088  H HE2  . PHE B 1 179 ? 9.605   50.516  4.234   1.00 130.57 ? 179 PHE B HE2  1 
ATOM   7089  H HZ   . PHE B 1 179 ? 11.635  51.345  4.964   1.00 125.16 ? 179 PHE B HZ   1 
ATOM   7090  N N    . GLY B 1 180 ? 13.901  45.869  3.127   1.00 99.50  ? 180 GLY B N    1 
ATOM   7091  C CA   . GLY B 1 180 ? 15.003  45.880  4.066   1.00 92.80  ? 180 GLY B CA   1 
ATOM   7092  C C    . GLY B 1 180 ? 16.170  46.726  3.602   1.00 90.33  ? 180 GLY B C    1 
ATOM   7093  O O    . GLY B 1 180 ? 16.513  46.725  2.417   1.00 91.63  ? 180 GLY B O    1 
ATOM   7094  H H    . GLY B 1 180 ? 14.144  45.841  2.303   1.00 119.40 ? 180 GLY B H    1 
ATOM   7095  H HA2  . GLY B 1 180 ? 14.694  46.231  4.916   1.00 111.36 ? 180 GLY B HA2  1 
ATOM   7096  H HA3  . GLY B 1 180 ? 15.320  44.973  4.196   1.00 111.36 ? 180 GLY B HA3  1 
ATOM   7097  N N    . ILE B 1 181 ? 16.783  47.463  4.523   1.00 90.30  ? 181 ILE B N    1 
ATOM   7098  C CA   . ILE B 1 181 ? 17.947  48.291  4.230   1.00 86.92  ? 181 ILE B CA   1 
ATOM   7099  C C    . ILE B 1 181 ? 19.149  47.645  4.904   1.00 86.30  ? 181 ILE B C    1 
ATOM   7100  O O    . ILE B 1 181 ? 19.187  47.517  6.135   1.00 83.72  ? 181 ILE B O    1 
ATOM   7101  C CB   . ILE B 1 181 ? 17.759  49.736  4.712   1.00 88.27  ? 181 ILE B CB   1 
ATOM   7102  C CG1  . ILE B 1 181 ? 16.572  50.390  4.009   1.00 87.73  ? 181 ILE B CG1  1 
ATOM   7103  C CG2  . ILE B 1 181 ? 19.026  50.548  4.462   1.00 86.90  ? 181 ILE B CG2  1 
ATOM   7104  C CD1  . ILE B 1 181 ? 15.786  51.332  4.893   1.00 92.78  ? 181 ILE B CD1  1 
ATOM   7105  H H    . ILE B 1 181 ? 16.536  47.499  5.346   1.00 108.36 ? 181 ILE B H    1 
ATOM   7106  H HA   . ILE B 1 181 ? 18.096  48.308  3.272   1.00 104.30 ? 181 ILE B HA   1 
ATOM   7107  H HB   . ILE B 1 181 ? 17.581  49.713  5.665   1.00 105.92 ? 181 ILE B HB   1 
ATOM   7108  H HG12 . ILE B 1 181 ? 16.900  50.899  3.251   1.00 105.27 ? 181 ILE B HG12 1 
ATOM   7109  H HG13 . ILE B 1 181 ? 15.967  49.695  3.705   1.00 105.27 ? 181 ILE B HG13 1 
ATOM   7110  H HG21 . ILE B 1 181 ? 18.821  51.491  4.564   1.00 104.28 ? 181 ILE B HG21 1 
ATOM   7111  H HG22 . ILE B 1 181 ? 19.702  50.284  5.106   1.00 104.28 ? 181 ILE B HG22 1 
ATOM   7112  H HG23 . ILE B 1 181 ? 19.340  50.373  3.561   1.00 104.28 ? 181 ILE B HG23 1 
ATOM   7113  H HD11 . ILE B 1 181 ? 15.134  51.803  4.352   1.00 111.34 ? 181 ILE B HD11 1 
ATOM   7114  H HD12 . ILE B 1 181 ? 15.336  50.817  5.581   1.00 111.34 ? 181 ILE B HD12 1 
ATOM   7115  H HD13 . ILE B 1 181 ? 16.397  51.965  5.301   1.00 111.34 ? 181 ILE B HD13 1 
ATOM   7116  N N    . MET B 1 182 ? 20.127  47.236  4.102   1.00 83.15  ? 182 MET B N    1 
ATOM   7117  C CA   . MET B 1 182 ? 21.339  46.594  4.610   1.00 79.68  ? 182 MET B CA   1 
ATOM   7118  C C    . MET B 1 182 ? 22.426  47.659  4.689   1.00 84.07  ? 182 MET B C    1 
ATOM   7119  O O    . MET B 1 182 ? 23.175  47.885  3.737   1.00 83.87  ? 182 MET B O    1 
ATOM   7120  C CB   . MET B 1 182 ? 21.750  45.429  3.722   1.00 77.23  ? 182 MET B CB   1 
ATOM   7121  C CG   . MET B 1 182 ? 20.654  44.403  3.522   1.00 81.48  ? 182 MET B CG   1 
ATOM   7122  S SD   . MET B 1 182 ? 20.529  43.279  4.930   1.00 84.09  ? 182 MET B SD   1 
ATOM   7123  C CE   . MET B 1 182 ? 18.884  43.649  5.522   1.00 82.50  ? 182 MET B CE   1 
ATOM   7124  H H    . MET B 1 182 ? 20.113  47.319  3.246   1.00 99.78  ? 182 MET B H    1 
ATOM   7125  H HA   . MET B 1 182 ? 21.164  46.246  5.498   1.00 95.61  ? 182 MET B HA   1 
ATOM   7126  H HB2  . MET B 1 182 ? 21.997  45.773  2.849   1.00 92.68  ? 182 MET B HB2  1 
ATOM   7127  H HB3  . MET B 1 182 ? 22.508  44.979  4.127   1.00 92.68  ? 182 MET B HB3  1 
ATOM   7128  H HG2  . MET B 1 182 ? 19.804  44.858  3.419   1.00 97.77  ? 182 MET B HG2  1 
ATOM   7129  H HG3  . MET B 1 182 ? 20.847  43.878  2.730   1.00 97.77  ? 182 MET B HG3  1 
ATOM   7130  H HE1  . MET B 1 182 ? 18.689  43.085  6.287   1.00 99.00  ? 182 MET B HE1  1 
ATOM   7131  H HE2  . MET B 1 182 ? 18.844  44.583  5.781   1.00 99.00  ? 182 MET B HE2  1 
ATOM   7132  H HE3  . MET B 1 182 ? 18.246  43.475  4.812   1.00 99.00  ? 182 MET B HE3  1 
ATOM   7133  N N    . PHE B 1 183 ? 22.498  48.330  5.838   1.00 81.39  ? 183 PHE B N    1 
ATOM   7134  C CA   . PHE B 1 183 ? 23.552  49.306  6.088   1.00 83.20  ? 183 PHE B CA   1 
ATOM   7135  C C    . PHE B 1 183 ? 24.890  48.578  6.136   1.00 81.78  ? 183 PHE B C    1 
ATOM   7136  O O    . PHE B 1 183 ? 25.137  47.775  7.039   1.00 81.94  ? 183 PHE B O    1 
ATOM   7137  C CB   . PHE B 1 183 ? 23.279  50.054  7.387   1.00 86.49  ? 183 PHE B CB   1 
ATOM   7138  C CG   . PHE B 1 183 ? 21.983  50.815  7.384   1.00 89.97  ? 183 PHE B CG   1 
ATOM   7139  C CD1  . PHE B 1 183 ? 21.894  52.056  6.771   1.00 89.91  ? 183 PHE B CD1  1 
ATOM   7140  C CD2  . PHE B 1 183 ? 20.853  50.287  7.991   1.00 90.25  ? 183 PHE B CD2  1 
ATOM   7141  C CE1  . PHE B 1 183 ? 20.703  52.758  6.768   1.00 91.81  ? 183 PHE B CE1  1 
ATOM   7142  C CE2  . PHE B 1 183 ? 19.659  50.984  7.989   1.00 91.95  ? 183 PHE B CE2  1 
ATOM   7143  C CZ   . PHE B 1 183 ? 19.584  52.221  7.377   1.00 94.95  ? 183 PHE B CZ   1 
ATOM   7144  H H    . PHE B 1 183 ? 21.945  48.236  6.489   1.00 97.67  ? 183 PHE B H    1 
ATOM   7145  H HA   . PHE B 1 183 ? 23.576  49.959  5.371   1.00 99.84  ? 183 PHE B HA   1 
ATOM   7146  H HB2  . PHE B 1 183 ? 23.245  49.413  8.114   1.00 103.79 ? 183 PHE B HB2  1 
ATOM   7147  H HB3  . PHE B 1 183 ? 23.996  50.689  7.538   1.00 103.79 ? 183 PHE B HB3  1 
ATOM   7148  H HD1  . PHE B 1 183 ? 22.643  52.419  6.358   1.00 107.89 ? 183 PHE B HD1  1 
ATOM   7149  H HD2  . PHE B 1 183 ? 20.899  49.455  8.405   1.00 108.30 ? 183 PHE B HD2  1 
ATOM   7150  H HE1  . PHE B 1 183 ? 20.655  53.591  6.357   1.00 110.17 ? 183 PHE B HE1  1 
ATOM   7151  H HE2  . PHE B 1 183 ? 18.907  50.621  8.398   1.00 110.34 ? 183 PHE B HE2  1 
ATOM   7152  H HZ   . PHE B 1 183 ? 18.782  52.692  7.376   1.00 113.93 ? 183 PHE B HZ   1 
ATOM   7153  N N    . PHE B 1 184 ? 25.749  48.851  5.160   1.00 83.61  ? 184 PHE B N    1 
ATOM   7154  C CA   . PHE B 1 184 ? 26.974  48.095  4.942   1.00 83.52  ? 184 PHE B CA   1 
ATOM   7155  C C    . PHE B 1 184 ? 28.182  48.972  5.237   1.00 83.10  ? 184 PHE B C    1 
ATOM   7156  O O    . PHE B 1 184 ? 28.219  50.146  4.853   1.00 86.62  ? 184 PHE B O    1 
ATOM   7157  C CB   . PHE B 1 184 ? 27.013  47.572  3.501   1.00 82.63  ? 184 PHE B CB   1 
ATOM   7158  C CG   . PHE B 1 184 ? 28.323  46.958  3.103   1.00 83.54  ? 184 PHE B CG   1 
ATOM   7159  C CD1  . PHE B 1 184 ? 28.817  45.850  3.769   1.00 82.92  ? 184 PHE B CD1  1 
ATOM   7160  C CD2  . PHE B 1 184 ? 29.056  47.483  2.043   1.00 86.47  ? 184 PHE B CD2  1 
ATOM   7161  C CE1  . PHE B 1 184 ? 30.024  45.281  3.398   1.00 85.92  ? 184 PHE B CE1  1 
ATOM   7162  C CE2  . PHE B 1 184 ? 30.263  46.920  1.669   1.00 84.78  ? 184 PHE B CE2  1 
ATOM   7163  C CZ   . PHE B 1 184 ? 30.747  45.818  2.346   1.00 86.09  ? 184 PHE B CZ   1 
ATOM   7164  H H    . PHE B 1 184 ? 25.639  49.489  4.595   1.00 100.33 ? 184 PHE B H    1 
ATOM   7165  H HA   . PHE B 1 184 ? 27.020  47.336  5.544   1.00 100.22 ? 184 PHE B HA   1 
ATOM   7166  H HB2  . PHE B 1 184 ? 26.327  46.893  3.400   1.00 99.16  ? 184 PHE B HB2  1 
ATOM   7167  H HB3  . PHE B 1 184 ? 26.839  48.311  2.898   1.00 99.16  ? 184 PHE B HB3  1 
ATOM   7168  H HD1  . PHE B 1 184 ? 28.334  45.483  4.474   1.00 99.50  ? 184 PHE B HD1  1 
ATOM   7169  H HD2  . PHE B 1 184 ? 28.730  48.221  1.581   1.00 103.76 ? 184 PHE B HD2  1 
ATOM   7170  H HE1  . PHE B 1 184 ? 30.349  44.539  3.854   1.00 103.10 ? 184 PHE B HE1  1 
ATOM   7171  H HE2  . PHE B 1 184 ? 30.747  47.284  0.963   1.00 101.74 ? 184 PHE B HE2  1 
ATOM   7172  H HZ   . PHE B 1 184 ? 31.558  45.436  2.096   1.00 103.31 ? 184 PHE B HZ   1 
ATOM   7173  N N    . ASP B 1 185 ? 29.159  48.398  5.939   1.00 83.87  ? 185 ASP B N    1 
ATOM   7174  C CA   . ASP B 1 185 ? 30.420  49.063  6.236   1.00 84.39  ? 185 ASP B CA   1 
ATOM   7175  C C    . ASP B 1 185 ? 31.562  48.231  5.669   1.00 87.48  ? 185 ASP B C    1 
ATOM   7176  O O    . ASP B 1 185 ? 31.740  47.070  6.055   1.00 87.01  ? 185 ASP B O    1 
ATOM   7177  C CB   . ASP B 1 185 ? 30.609  49.261  7.739   1.00 85.52  ? 185 ASP B CB   1 
ATOM   7178  C CG   . ASP B 1 185 ? 31.901  49.988  8.069   1.00 91.42  ? 185 ASP B CG   1 
ATOM   7179  O OD1  . ASP B 1 185 ? 32.585  50.440  7.126   1.00 92.59  ? 185 ASP B OD1  1 
ATOM   7180  O OD2  . ASP B 1 185 ? 32.235  50.107  9.269   1.00 95.23  ? 185 ASP B OD2  1 
ATOM   7181  H H    . ASP B 1 185 ? 29.109  47.602  6.261   1.00 100.65 ? 185 ASP B H    1 
ATOM   7182  H HA   . ASP B 1 185 ? 30.425  49.934  5.810   1.00 101.27 ? 185 ASP B HA   1 
ATOM   7183  H HB2  . ASP B 1 185 ? 29.871  49.787  8.086   1.00 102.63 ? 185 ASP B HB2  1 
ATOM   7184  H HB3  . ASP B 1 185 ? 30.632  48.394  8.174   1.00 102.63 ? 185 ASP B HB3  1 
ATOM   7185  N N    . SER B 1 186 ? 32.340  48.834  4.767   1.00 87.96  ? 186 SER B N    1 
ATOM   7186  C CA   . SER B 1 186 ? 33.436  48.126  4.120   1.00 88.67  ? 186 SER B CA   1 
ATOM   7187  C C    . SER B 1 186 ? 34.662  48.013  5.013   1.00 89.51  ? 186 SER B C    1 
ATOM   7188  O O    . SER B 1 186 ? 35.385  47.015  4.935   1.00 91.97  ? 186 SER B O    1 
ATOM   7189  C CB   . SER B 1 186 ? 33.818  48.831  2.818   1.00 89.46  ? 186 SER B CB   1 
ATOM   7190  O OG   . SER B 1 186 ? 32.671  49.322  2.150   1.00 91.77  ? 186 SER B OG   1 
ATOM   7191  H H    . SER B 1 186 ? 32.252  49.652  4.515   1.00 105.55 ? 186 SER B H    1 
ATOM   7192  H HA   . SER B 1 186 ? 33.134  47.228  3.908   1.00 106.40 ? 186 SER B HA   1 
ATOM   7193  H HB2  . SER B 1 186 ? 34.405  49.575  3.024   1.00 107.35 ? 186 SER B HB2  1 
ATOM   7194  H HB3  . SER B 1 186 ? 34.274  48.200  2.240   1.00 107.35 ? 186 SER B HB3  1 
ATOM   7195  H HG   . SER B 1 186 ? 32.187  48.681  1.902   1.00 110.13 ? 186 SER B HG   1 
ATOM   7196  N N    . ASP B 1 187 ? 34.920  49.019  5.850   1.00 89.33  ? 187 ASP B N    1 
ATOM   7197  C CA   . ASP B 1 187 ? 36.056  48.947  6.763   1.00 93.16  ? 187 ASP B CA   1 
ATOM   7198  C C    . ASP B 1 187 ? 36.058  47.631  7.533   1.00 93.31  ? 187 ASP B C    1 
ATOM   7199  O O    . ASP B 1 187 ? 37.117  47.064  7.823   1.00 94.38  ? 187 ASP B O    1 
ATOM   7200  C CB   . ASP B 1 187 ? 36.024  50.121  7.743   1.00 96.03  ? 187 ASP B CB   1 
ATOM   7201  C CG   . ASP B 1 187 ? 36.352  51.443  7.086   1.00 93.97  ? 187 ASP B CG   1 
ATOM   7202  O OD1  . ASP B 1 187 ? 36.297  51.522  5.842   1.00 94.34  ? 187 ASP B OD1  1 
ATOM   7203  O OD2  . ASP B 1 187 ? 36.663  52.406  7.819   1.00 96.07  ? 187 ASP B OD2  1 
ATOM   7204  H H    . ASP B 1 187 ? 34.459  49.743  5.906   1.00 107.20 ? 187 ASP B H    1 
ATOM   7205  H HA   . ASP B 1 187 ? 36.874  49.007  6.245   1.00 111.80 ? 187 ASP B HA   1 
ATOM   7206  H HB2  . ASP B 1 187 ? 35.135  50.189  8.125   1.00 115.23 ? 187 ASP B HB2  1 
ATOM   7207  H HB3  . ASP B 1 187 ? 36.675  49.965  8.444   1.00 115.23 ? 187 ASP B HB3  1 
ATOM   7208  N N    . ASN B 1 188 ? 34.867  47.130  7.873   1.00 90.83  ? 188 ASN B N    1 
ATOM   7209  C CA   . ASN B 1 188 ? 34.709  45.965  8.732   1.00 92.04  ? 188 ASN B CA   1 
ATOM   7210  C C    . ASN B 1 188 ? 34.099  44.766  8.021   1.00 90.24  ? 188 ASN B C    1 
ATOM   7211  O O    . ASN B 1 188 ? 34.139  43.658  8.568   1.00 90.80  ? 188 ASN B O    1 
ATOM   7212  C CB   . ASN B 1 188 ? 33.823  46.328  9.936   1.00 88.18  ? 188 ASN B CB   1 
ATOM   7213  C CG   . ASN B 1 188 ? 34.318  45.728  11.235  1.00 99.02  ? 188 ASN B CG   1 
ATOM   7214  O OD1  . ASN B 1 188 ? 35.512  45.479  11.402  1.00 104.44 ? 188 ASN B OD1  1 
ATOM   7215  N ND2  . ASN B 1 188 ? 33.401  45.499  12.171  1.00 100.65 ? 188 ASN B ND2  1 
ATOM   7216  H H    . ASN B 1 188 ? 34.118  47.460  7.608   1.00 109.00 ? 188 ASN B H    1 
ATOM   7217  H HA   . ASN B 1 188 ? 35.582  45.700  9.060   1.00 110.45 ? 188 ASN B HA   1 
ATOM   7218  H HB2  . ASN B 1 188 ? 33.809  47.293  10.039  1.00 105.81 ? 188 ASN B HB2  1 
ATOM   7219  H HB3  . ASN B 1 188 ? 32.924  45.998  9.778   1.00 105.81 ? 188 ASN B HB3  1 
ATOM   7220  H HD21 . ASN B 1 188 ? 32.576  45.691  12.021  1.00 120.78 ? 188 ASN B HD21 1 
ATOM   7221  H HD22 . ASN B 1 188 ? 33.632  45.159  12.926  1.00 120.78 ? 188 ASN B HD22 1 
ATOM   7222  N N    . LEU B 1 189 ? 33.546  44.948  6.823   1.00 89.48  ? 189 LEU B N    1 
ATOM   7223  C CA   . LEU B 1 189 ? 32.710  43.929  6.195   1.00 89.02  ? 189 LEU B CA   1 
ATOM   7224  C C    . LEU B 1 189 ? 31.620  43.487  7.172   1.00 85.18  ? 189 LEU B C    1 
ATOM   7225  O O    . LEU B 1 189 ? 31.425  42.300  7.447   1.00 83.32  ? 189 LEU B O    1 
ATOM   7226  C CB   . LEU B 1 189 ? 33.545  42.744  5.718   1.00 91.13  ? 189 LEU B CB   1 
ATOM   7227  C CG   . LEU B 1 189 ? 34.092  42.767  4.284   1.00 92.76  ? 189 LEU B CG   1 
ATOM   7228  C CD1  . LEU B 1 189 ? 33.034  43.101  3.240   1.00 87.60  ? 189 LEU B CD1  1 
ATOM   7229  C CD2  . LEU B 1 189 ? 35.259  43.752  4.176   1.00 94.26  ? 189 LEU B CD2  1 
ATOM   7230  H H    . LEU B 1 189 ? 33.642  45.660  6.351   1.00 107.38 ? 189 LEU B H    1 
ATOM   7231  H HA   . LEU B 1 189 ? 32.284  44.306  5.410   1.00 106.82 ? 189 LEU B HA   1 
ATOM   7232  H HB2  . LEU B 1 189 ? 34.313  42.670  6.306   1.00 109.36 ? 189 LEU B HB2  1 
ATOM   7233  H HB3  . LEU B 1 189 ? 32.994  41.949  5.791   1.00 109.36 ? 189 LEU B HB3  1 
ATOM   7234  H HG   . LEU B 1 189 ? 34.401  41.870  4.085   1.00 111.31 ? 189 LEU B HG   1 
ATOM   7235  H HD11 . LEU B 1 189 ? 33.377  42.879  2.361   1.00 105.12 ? 189 LEU B HD11 1 
ATOM   7236  H HD12 . LEU B 1 189 ? 32.234  42.584  3.424   1.00 105.12 ? 189 LEU B HD12 1 
ATOM   7237  H HD13 . LEU B 1 189 ? 32.833  44.049  3.287   1.00 105.12 ? 189 LEU B HD13 1 
ATOM   7238  H HD21 . LEU B 1 189 ? 35.483  43.875  3.240   1.00 113.10 ? 189 LEU B HD21 1 
ATOM   7239  H HD22 . LEU B 1 189 ? 34.996  44.599  4.567   1.00 113.10 ? 189 LEU B HD22 1 
ATOM   7240  H HD23 . LEU B 1 189 ? 36.022  43.390  4.653   1.00 113.10 ? 189 LEU B HD23 1 
ATOM   7241  N N    . SER B 1 190 ? 30.919  44.472  7.723   1.00 83.68  ? 190 SER B N    1 
ATOM   7242  C CA   . SER B 1 190 ? 29.809  44.260  8.639   1.00 82.30  ? 190 SER B CA   1 
ATOM   7243  C C    . SER B 1 190 ? 28.534  44.827  8.025   1.00 82.24  ? 190 SER B C    1 
ATOM   7244  O O    . SER B 1 190 ? 28.566  45.575  7.043   1.00 83.99  ? 190 SER B O    1 
ATOM   7245  C CB   . SER B 1 190 ? 30.083  44.909  10.003  1.00 85.65  ? 190 SER B CB   1 
ATOM   7246  O OG   . SER B 1 190 ? 30.506  46.254  9.861   1.00 83.97  ? 190 SER B OG   1 
ATOM   7247  H H    . SER B 1 190 ? 31.076  45.305  7.575   1.00 100.41 ? 190 SER B H    1 
ATOM   7248  H HA   . SER B 1 190 ? 29.684  43.308  8.782   1.00 98.76  ? 190 SER B HA   1 
ATOM   7249  H HB2  . SER B 1 190 ? 29.268  44.891  10.528  1.00 102.78 ? 190 SER B HB2  1 
ATOM   7250  H HB3  . SER B 1 190 ? 30.780  44.408  10.454  1.00 102.78 ? 190 SER B HB3  1 
ATOM   7251  H HG   . SER B 1 190 ? 30.633  46.597  10.617  1.00 100.77 ? 190 SER B HG   1 
ATOM   7252  N N    . MET B 1 191 ? 27.400  44.469  8.625   1.00 77.51  ? 191 MET B N    1 
ATOM   7253  C CA   . MET B 1 191 ? 26.103  44.829  8.065   1.00 81.79  ? 191 MET B CA   1 
ATOM   7254  C C    . MET B 1 191 ? 25.074  44.952  9.176   1.00 79.31  ? 191 MET B C    1 
ATOM   7255  O O    . MET B 1 191 ? 24.960  44.059  10.019  1.00 79.73  ? 191 MET B O    1 
ATOM   7256  C CB   . MET B 1 191 ? 25.653  43.782  7.039   1.00 80.87  ? 191 MET B CB   1 
ATOM   7257  C CG   . MET B 1 191 ? 24.328  44.081  6.368   1.00 78.28  ? 191 MET B CG   1 
ATOM   7258  S SD   . MET B 1 191 ? 23.786  42.707  5.333   1.00 79.35  ? 191 MET B SD   1 
ATOM   7259  C CE   . MET B 1 191 ? 23.412  41.460  6.560   1.00 79.44  ? 191 MET B CE   1 
ATOM   7260  H H    . MET B 1 191 ? 27.357  44.018  9.355   1.00 93.01  ? 191 MET B H    1 
ATOM   7261  H HA   . MET B 1 191 ? 26.179  45.691  7.626   1.00 98.15  ? 191 MET B HA   1 
ATOM   7262  H HB2  . MET B 1 191 ? 26.326  43.723  6.343   1.00 97.04  ? 191 MET B HB2  1 
ATOM   7263  H HB3  . MET B 1 191 ? 25.566  42.927  7.489   1.00 97.04  ? 191 MET B HB3  1 
ATOM   7264  H HG2  . MET B 1 191 ? 23.652  44.237  7.046   1.00 93.94  ? 191 MET B HG2  1 
ATOM   7265  H HG3  . MET B 1 191 ? 24.422  44.867  5.807   1.00 93.94  ? 191 MET B HG3  1 
ATOM   7266  H HE1  . MET B 1 191 ? 22.943  40.727  6.132   1.00 95.33  ? 191 MET B HE1  1 
ATOM   7267  H HE2  . MET B 1 191 ? 24.241  41.141  6.948   1.00 95.33  ? 191 MET B HE2  1 
ATOM   7268  H HE3  . MET B 1 191 ? 22.853  41.853  7.249   1.00 95.33  ? 191 MET B HE3  1 
ATOM   7269  N N    . LYS B 1 192 ? 24.322  46.053  9.159   1.00 80.11  ? 192 LYS B N    1 
ATOM   7270  C CA   . LYS B 1 192 ? 23.247  46.304  10.115  1.00 81.23  ? 192 LYS B CA   1 
ATOM   7271  C C    . LYS B 1 192 ? 21.906  46.087  9.424   1.00 81.07  ? 192 LYS B C    1 
ATOM   7272  O O    . LYS B 1 192 ? 21.423  46.983  8.713   1.00 82.63  ? 192 LYS B O    1 
ATOM   7273  C CB   . LYS B 1 192 ? 23.346  47.733  10.660  1.00 82.51  ? 192 LYS B CB   1 
ATOM   7274  C CG   . LYS B 1 192 ? 23.523  47.825  12.163  1.00 85.38  ? 192 LYS B CG   1 
ATOM   7275  C CD   . LYS B 1 192 ? 22.181  47.705  12.874  1.00 92.17  ? 192 LYS B CD   1 
ATOM   7276  C CE   . LYS B 1 192 ? 22.299  48.022  14.362  1.00 91.26  ? 192 LYS B CE   1 
ATOM   7277  N NZ   . LYS B 1 192 ? 21.201  47.386  15.147  1.00 91.17  ? 192 LYS B NZ   1 
ATOM   7278  H H    . LYS B 1 192 ? 24.419  46.687  8.586   1.00 96.13  ? 192 LYS B H    1 
ATOM   7279  H HA   . LYS B 1 192 ? 23.318  45.685  10.858  1.00 97.47  ? 192 LYS B HA   1 
ATOM   7280  H HB2  . LYS B 1 192 ? 24.110  48.167  10.249  1.00 99.01  ? 192 LYS B HB2  1 
ATOM   7281  H HB3  . LYS B 1 192 ? 22.532  48.207  10.431  1.00 99.01  ? 192 LYS B HB3  1 
ATOM   7282  H HG2  . LYS B 1 192 ? 24.097  47.104  12.466  1.00 102.45 ? 192 LYS B HG2  1 
ATOM   7283  H HG3  . LYS B 1 192 ? 23.916  48.681  12.391  1.00 102.45 ? 192 LYS B HG3  1 
ATOM   7284  H HD2  . LYS B 1 192 ? 21.553  48.329  12.479  1.00 110.61 ? 192 LYS B HD2  1 
ATOM   7285  H HD3  . LYS B 1 192 ? 21.850  46.798  12.782  1.00 110.61 ? 192 LYS B HD3  1 
ATOM   7286  H HE2  . LYS B 1 192 ? 23.146  47.687  14.696  1.00 109.51 ? 192 LYS B HE2  1 
ATOM   7287  H HE3  . LYS B 1 192 ? 22.248  48.983  14.491  1.00 109.51 ? 192 LYS B HE3  1 
ATOM   7288  H HZ1  . LYS B 1 192 ? 21.338  47.508  16.017  1.00 109.41 ? 192 LYS B HZ1  1 
ATOM   7289  H HZ2  . LYS B 1 192 ? 20.419  47.748  14.924  1.00 109.41 ? 192 LYS B HZ2  1 
ATOM   7290  H HZ3  . LYS B 1 192 ? 21.174  46.513  14.978  1.00 109.41 ? 192 LYS B HZ3  1 
ATOM   7291  N N    . PRO B 1 193 ? 21.262  44.930  9.592   1.00 79.95  ? 193 PRO B N    1 
ATOM   7292  C CA   . PRO B 1 193 ? 20.027  44.666  8.837   1.00 84.00  ? 193 PRO B CA   1 
ATOM   7293  C C    . PRO B 1 193 ? 18.830  45.393  9.432   1.00 87.04  ? 193 PRO B C    1 
ATOM   7294  O O    . PRO B 1 193 ? 18.498  45.217  10.607  1.00 95.06  ? 193 PRO B O    1 
ATOM   7295  C CB   . PRO B 1 193 ? 19.862  43.142  8.932   1.00 84.10  ? 193 PRO B CB   1 
ATOM   7296  C CG   . PRO B 1 193 ? 20.928  42.642  9.865   1.00 82.64  ? 193 PRO B CG   1 
ATOM   7297  C CD   . PRO B 1 193 ? 21.634  43.813  10.476  1.00 83.11  ? 193 PRO B CD   1 
ATOM   7298  H HA   . PRO B 1 193 ? 20.140  44.938  7.912   1.00 100.80 ? 193 PRO B HA   1 
ATOM   7299  H HB2  . PRO B 1 193 ? 18.981  42.934  9.281   1.00 100.92 ? 193 PRO B HB2  1 
ATOM   7300  H HB3  . PRO B 1 193 ? 19.971  42.750  8.052   1.00 100.92 ? 193 PRO B HB3  1 
ATOM   7301  H HG2  . PRO B 1 193 ? 20.513  42.107  10.559  1.00 99.17  ? 193 PRO B HG2  1 
ATOM   7302  H HG3  . PRO B 1 193 ? 21.558  42.102  9.362   1.00 99.17  ? 193 PRO B HG3  1 
ATOM   7303  H HD2  . PRO B 1 193 ? 21.322  43.970  11.381  1.00 99.73  ? 193 PRO B HD2  1 
ATOM   7304  H HD3  . PRO B 1 193 ? 22.594  43.677  10.474  1.00 99.73  ? 193 PRO B HD3  1 
ATOM   7305  N N    . TYR B 1 194 ? 18.183  46.212  8.609   1.00 88.33  ? 194 TYR B N    1 
ATOM   7306  C CA   . TYR B 1 194 ? 16.888  46.802  8.920   1.00 91.49  ? 194 TYR B CA   1 
ATOM   7307  C C    . TYR B 1 194 ? 15.811  46.077  8.123   1.00 95.53  ? 194 TYR B C    1 
ATOM   7308  O O    . TYR B 1 194 ? 16.048  45.668  6.980   1.00 94.42  ? 194 TYR B O    1 
ATOM   7309  C CB   . TYR B 1 194 ? 16.877  48.293  8.584   1.00 91.83  ? 194 TYR B CB   1 
ATOM   7310  C CG   . TYR B 1 194 ? 15.616  49.012  8.998   1.00 97.46  ? 194 TYR B CG   1 
ATOM   7311  C CD1  . TYR B 1 194 ? 14.470  48.961  8.214   1.00 100.63 ? 194 TYR B CD1  1 
ATOM   7312  C CD2  . TYR B 1 194 ? 15.575  49.752  10.171  1.00 102.10 ? 194 TYR B CD2  1 
ATOM   7313  C CE1  . TYR B 1 194 ? 13.317  49.624  8.591   1.00 105.28 ? 194 TYR B CE1  1 
ATOM   7314  C CE2  . TYR B 1 194 ? 14.423  50.405  10.564  1.00 105.28 ? 194 TYR B CE2  1 
ATOM   7315  C CZ   . TYR B 1 194 ? 13.301  50.350  9.763   1.00 108.79 ? 194 TYR B CZ   1 
ATOM   7316  O OH   . TYR B 1 194 ? 12.159  51.017  10.146  1.00 113.51 ? 194 TYR B OH   1 
ATOM   7317  H H    . TYR B 1 194 ? 18.485  46.448  7.839   1.00 105.99 ? 194 TYR B H    1 
ATOM   7318  H HA   . TYR B 1 194 ? 16.695  46.710  9.866   1.00 109.78 ? 194 TYR B HA   1 
ATOM   7319  H HB2  . TYR B 1 194 ? 17.621  48.718  9.039   1.00 110.20 ? 194 TYR B HB2  1 
ATOM   7320  H HB3  . TYR B 1 194 ? 16.973  48.395  7.624   1.00 110.20 ? 194 TYR B HB3  1 
ATOM   7321  H HD1  . TYR B 1 194 ? 14.479  48.473  7.423   1.00 120.75 ? 194 TYR B HD1  1 
ATOM   7322  H HD2  . TYR B 1 194 ? 16.336  49.809  10.703  1.00 122.52 ? 194 TYR B HD2  1 
ATOM   7323  H HE1  . TYR B 1 194 ? 12.556  49.580  8.057   1.00 126.34 ? 194 TYR B HE1  1 
ATOM   7324  H HE2  . TYR B 1 194 ? 14.404  50.880  11.363  1.00 126.33 ? 194 TYR B HE2  1 
ATOM   7325  H HH   . TYR B 1 194 ? 12.292  51.422  10.870  1.00 136.22 ? 194 TYR B HH   1 
ATOM   7326  N N    . VAL B 1 195 ? 14.631  45.922  8.720   1.00 98.76  ? 195 VAL B N    1 
ATOM   7327  C CA   . VAL B 1 195 ? 13.532  45.209  8.082   1.00 102.15 ? 195 VAL B CA   1 
ATOM   7328  C C    . VAL B 1 195 ? 12.223  45.892  8.456   1.00 106.87 ? 195 VAL B C    1 
ATOM   7329  O O    . VAL B 1 195 ? 11.806  45.848  9.618   1.00 109.35 ? 195 VAL B O    1 
ATOM   7330  C CB   . VAL B 1 195 ? 13.496  43.724  8.477   1.00 100.74 ? 195 VAL B CB   1 
ATOM   7331  C CG1  . VAL B 1 195 ? 12.217  43.064  7.982   1.00 104.49 ? 195 VAL B CG1  1 
ATOM   7332  C CG2  . VAL B 1 195 ? 14.720  43.002  7.929   1.00 98.46  ? 195 VAL B CG2  1 
ATOM   7333  H H    . VAL B 1 195 ? 14.444  46.225  9.503   1.00 118.52 ? 195 VAL B H    1 
ATOM   7334  H HA   . VAL B 1 195 ? 13.631  45.280  7.119   1.00 122.58 ? 195 VAL B HA   1 
ATOM   7335  H HB   . VAL B 1 195 ? 13.509  43.657  9.445   1.00 120.88 ? 195 VAL B HB   1 
ATOM   7336  H HG11 . VAL B 1 195 ? 12.243  42.120  8.204   1.00 125.39 ? 195 VAL B HG11 1 
ATOM   7337  H HG12 . VAL B 1 195 ? 11.457  43.485  8.413   1.00 125.39 ? 195 VAL B HG12 1 
ATOM   7338  H HG13 . VAL B 1 195 ? 12.156  43.176  7.020   1.00 125.39 ? 195 VAL B HG13 1 
ATOM   7339  H HG21 . VAL B 1 195 ? 14.674  42.066  8.180   1.00 118.15 ? 195 VAL B HG21 1 
ATOM   7340  H HG22 . VAL B 1 195 ? 14.730  43.085  6.963   1.00 118.15 ? 195 VAL B HG22 1 
ATOM   7341  H HG23 . VAL B 1 195 ? 15.519  43.405  8.304   1.00 118.15 ? 195 VAL B HG23 1 
ATOM   7342  N N    . TYR B 1 196 ? 11.576  46.517  7.475   1.00 111.38 ? 196 TYR B N    1 
ATOM   7343  C CA   . TYR B 1 196 ? 10.215  47.019  7.596   1.00 112.84 ? 196 TYR B CA   1 
ATOM   7344  C C    . TYR B 1 196 ? 9.265   45.971  7.029   1.00 117.14 ? 196 TYR B C    1 
ATOM   7345  O O    . TYR B 1 196 ? 9.549   45.358  5.996   1.00 119.58 ? 196 TYR B O    1 
ATOM   7346  C CB   . TYR B 1 196 ? 10.060  48.358  6.858   1.00 113.22 ? 196 TYR B CB   1 
ATOM   7347  C CG   . TYR B 1 196 ? 8.694   49.024  6.999   1.00 120.30 ? 196 TYR B CG   1 
ATOM   7348  C CD1  . TYR B 1 196 ? 7.512   48.367  6.682   1.00 125.24 ? 196 TYR B CD1  1 
ATOM   7349  C CD2  . TYR B 1 196 ? 8.606   50.351  7.399   1.00 123.64 ? 196 TYR B CD2  1 
ATOM   7350  C CE1  . TYR B 1 196 ? 6.289   48.976  6.806   1.00 129.52 ? 196 TYR B CE1  1 
ATOM   7351  C CE2  . TYR B 1 196 ? 7.365   50.987  7.520   1.00 127.60 ? 196 TYR B CE2  1 
ATOM   7352  C CZ   . TYR B 1 196 ? 6.214   50.287  7.221   1.00 129.50 ? 196 TYR B CZ   1 
ATOM   7353  O OH   . TYR B 1 196 ? 5.004   50.929  7.346   1.00 131.63 ? 196 TYR B OH   1 
ATOM   7354  H H    . TYR B 1 196 ? 11.920  46.666  6.701   1.00 133.66 ? 196 TYR B H    1 
ATOM   7355  H HA   . TYR B 1 196 ? 9.985   47.179  8.525   1.00 135.41 ? 196 TYR B HA   1 
ATOM   7356  H HB2  . TYR B 1 196 ? 10.722  48.977  7.204   1.00 135.87 ? 196 TYR B HB2  1 
ATOM   7357  H HB3  . TYR B 1 196 ? 10.212  48.206  5.912   1.00 135.87 ? 196 TYR B HB3  1 
ATOM   7358  H HD1  . TYR B 1 196 ? 7.550   47.490  6.377   1.00 150.29 ? 196 TYR B HD1  1 
ATOM   7359  H HD2  . TYR B 1 196 ? 9.383   50.825  7.590   1.00 148.36 ? 196 TYR B HD2  1 
ATOM   7360  H HE1  . TYR B 1 196 ? 5.512   48.505  6.610   1.00 155.43 ? 196 TYR B HE1  1 
ATOM   7361  H HE2  . TYR B 1 196 ? 7.316   51.873  7.799   1.00 153.13 ? 196 TYR B HE2  1 
ATOM   7362  H HH   . TYR B 1 196 ? 5.126   51.733  7.558   1.00 157.95 ? 196 TYR B HH   1 
ATOM   7363  N N    . VAL B 1 197 ? 8.134   45.775  7.703   1.00 123.37 ? 197 VAL B N    1 
ATOM   7364  C CA   . VAL B 1 197 ? 7.020   45.002  7.166   1.00 127.94 ? 197 VAL B CA   1 
ATOM   7365  C C    . VAL B 1 197 ? 5.742   45.811  7.354   1.00 133.91 ? 197 VAL B C    1 
ATOM   7366  O O    . VAL B 1 197 ? 5.546   46.440  8.400   1.00 134.76 ? 197 VAL B O    1 
ATOM   7367  C CB   . VAL B 1 197 ? 6.912   43.617  7.834   1.00 127.57 ? 197 VAL B CB   1 
ATOM   7368  C CG1  . VAL B 1 197 ? 8.297   42.988  7.966   1.00 122.05 ? 197 VAL B CG1  1 
ATOM   7369  C CG2  . VAL B 1 197 ? 6.242   43.719  9.185   1.00 132.89 ? 197 VAL B CG2  1 
ATOM   7370  H H    . VAL B 1 197 ? 7.987   46.087  8.490   1.00 148.05 ? 197 VAL B H    1 
ATOM   7371  H HA   . VAL B 1 197 ? 7.150   44.860  6.215   1.00 153.53 ? 197 VAL B HA   1 
ATOM   7372  H HB   . VAL B 1 197 ? 6.364   43.043  7.276   1.00 153.08 ? 197 VAL B HB   1 
ATOM   7373  H HG11 . VAL B 1 197 ? 8.209   42.113  8.377   1.00 146.45 ? 197 VAL B HG11 1 
ATOM   7374  H HG12 . VAL B 1 197 ? 8.690   42.900  7.084   1.00 146.45 ? 197 VAL B HG12 1 
ATOM   7375  H HG13 . VAL B 1 197 ? 8.852   43.559  8.520   1.00 146.45 ? 197 VAL B HG13 1 
ATOM   7376  H HG21 . VAL B 1 197 ? 6.221   42.840  9.594   1.00 159.47 ? 197 VAL B HG21 1 
ATOM   7377  H HG22 . VAL B 1 197 ? 6.746   44.332  9.742   1.00 159.47 ? 197 VAL B HG22 1 
ATOM   7378  H HG23 . VAL B 1 197 ? 5.338   44.050  9.064   1.00 159.47 ? 197 VAL B HG23 1 
ATOM   7379  N N    . LYS B 1 198 ? 4.872   45.795  6.337   1.00 136.98 ? 198 LYS B N    1 
ATOM   7380  C CA   . LYS B 1 198 ? 3.702   46.667  6.352   1.00 138.40 ? 198 LYS B CA   1 
ATOM   7381  C C    . LYS B 1 198 ? 2.660   46.217  7.371   1.00 143.21 ? 198 LYS B C    1 
ATOM   7382  O O    . LYS B 1 198 ? 1.954   47.057  7.941   1.00 143.52 ? 198 LYS B O    1 
ATOM   7383  C CB   . LYS B 1 198 ? 3.077   46.729  4.957   1.00 138.81 ? 198 LYS B CB   1 
ATOM   7384  C CG   . LYS B 1 198 ? 3.407   48.000  4.188   1.00 136.71 ? 198 LYS B CG   1 
ATOM   7385  C CD   . LYS B 1 198 ? 3.403   47.762  2.685   1.00 141.75 ? 198 LYS B CD   1 
ATOM   7386  C CE   . LYS B 1 198 ? 2.623   48.843  1.950   1.00 143.14 ? 198 LYS B CE   1 
ATOM   7387  N NZ   . LYS B 1 198 ? 2.763   48.725  0.470   1.00 139.61 ? 198 LYS B NZ   1 
ATOM   7388  H H    . LYS B 1 198 ? 4.939   45.295  5.640   1.00 164.38 ? 198 LYS B H    1 
ATOM   7389  H HA   . LYS B 1 198 ? 3.991   47.559  6.599   1.00 166.08 ? 198 LYS B HA   1 
ATOM   7390  H HB2  . LYS B 1 198 ? 3.400   45.977  4.437   1.00 166.57 ? 198 LYS B HB2  1 
ATOM   7391  H HB3  . LYS B 1 198 ? 2.112   46.680  5.046   1.00 166.57 ? 198 LYS B HB3  1 
ATOM   7392  H HG2  . LYS B 1 198 ? 2.745   48.679  4.391   1.00 164.05 ? 198 LYS B HG2  1 
ATOM   7393  H HG3  . LYS B 1 198 ? 4.289   48.310  4.445   1.00 164.05 ? 198 LYS B HG3  1 
ATOM   7394  H HD2  . LYS B 1 198 ? 4.316   47.768  2.356   1.00 170.10 ? 198 LYS B HD2  1 
ATOM   7395  H HD3  . LYS B 1 198 ? 2.989   46.905  2.496   1.00 170.10 ? 198 LYS B HD3  1 
ATOM   7396  H HE2  . LYS B 1 198 ? 1.682   48.765  2.173   1.00 171.77 ? 198 LYS B HE2  1 
ATOM   7397  H HE3  . LYS B 1 198 ? 2.955   49.714  2.218   1.00 171.77 ? 198 LYS B HE3  1 
ATOM   7398  H HZ1  . LYS B 1 198 ? 2.460   47.934  0.197   1.00 167.54 ? 198 LYS B HZ1  1 
ATOM   7399  H HZ2  . LYS B 1 198 ? 3.618   48.802  0.238   1.00 167.54 ? 198 LYS B HZ2  1 
ATOM   7400  H HZ3  . LYS B 1 198 ? 2.295   49.367  0.068   1.00 167.54 ? 198 LYS B HZ3  1 
ATOM   7401  N N    . GLU B 1 199 ? 2.538   44.909  7.606   1.00 146.46 ? 199 GLU B N    1 
ATOM   7402  C CA   . GLU B 1 199 ? 1.603   44.419  8.614   1.00 147.05 ? 199 GLU B CA   1 
ATOM   7403  C C    . GLU B 1 199 ? 1.857   45.095  9.957   1.00 146.94 ? 199 GLU B C    1 
ATOM   7404  O O    . GLU B 1 199 ? 0.968   45.735  10.529  1.00 149.12 ? 199 GLU B O    1 
ATOM   7405  C CB   . GLU B 1 199 ? 1.721   42.898  8.743   1.00 148.42 ? 199 GLU B CB   1 
ATOM   7406  C CG   . GLU B 1 199 ? 0.607   42.241  9.548   1.00 150.59 ? 199 GLU B CG   1 
ATOM   7407  C CD   . GLU B 1 199 ? 0.779   42.419  11.046  1.00 151.83 ? 199 GLU B CD   1 
ATOM   7408  O OE1  . GLU B 1 199 ? 1.932   42.583  11.497  1.00 151.36 ? 199 GLU B OE1  1 
ATOM   7409  O OE2  . GLU B 1 199 ? -0.238  42.401  11.770  1.00 151.63 ? 199 GLU B OE2  1 
ATOM   7410  H H    . GLU B 1 199 ? 2.980   44.293  7.200   1.00 175.76 ? 199 GLU B H    1 
ATOM   7411  H HA   . GLU B 1 199 ? 0.698   44.625  8.332   1.00 176.46 ? 199 GLU B HA   1 
ATOM   7412  H HB2  . GLU B 1 199 ? 1.707   42.510  7.854   1.00 178.10 ? 199 GLU B HB2  1 
ATOM   7413  H HB3  . GLU B 1 199 ? 2.561   42.690  9.183   1.00 178.10 ? 199 GLU B HB3  1 
ATOM   7414  H HG2  . GLU B 1 199 ? -0.242  42.637  9.295   1.00 180.72 ? 199 GLU B HG2  1 
ATOM   7415  H HG3  . GLU B 1 199 ? 0.599   41.289  9.359   1.00 180.72 ? 199 GLU B HG3  1 
ATOM   7416  N N    . VAL B 1 200 ? 3.086   44.967  10.469  1.00 145.49 ? 200 VAL B N    1 
ATOM   7417  C CA   . VAL B 1 200 ? 3.414   45.498  11.790  1.00 145.43 ? 200 VAL B CA   1 
ATOM   7418  C C    . VAL B 1 200 ? 3.567   47.010  11.795  1.00 140.45 ? 200 VAL B C    1 
ATOM   7419  O O    . VAL B 1 200 ? 3.721   47.605  12.870  1.00 138.92 ? 200 VAL B O    1 
ATOM   7420  C CB   . VAL B 1 200 ? 4.711   44.865  12.332  1.00 142.12 ? 200 VAL B CB   1 
ATOM   7421  C CG1  . VAL B 1 200 ? 4.850   45.124  13.826  1.00 142.15 ? 200 VAL B CG1  1 
ATOM   7422  C CG2  . VAL B 1 200 ? 4.750   43.367  12.052  1.00 143.86 ? 200 VAL B CG2  1 
ATOM   7423  H H    . VAL B 1 200 ? 3.742   44.578  10.072  1.00 174.59 ? 200 VAL B H    1 
ATOM   7424  H HA   . VAL B 1 200 ? 2.686   45.269  12.388  1.00 174.51 ? 200 VAL B HA   1 
ATOM   7425  H HB   . VAL B 1 200 ? 5.463   45.275  11.877  1.00 170.54 ? 200 VAL B HB   1 
ATOM   7426  H HG11 . VAL B 1 200 ? 5.524   44.529  14.188  1.00 170.57 ? 200 VAL B HG11 1 
ATOM   7427  H HG12 . VAL B 1 200 ? 5.115   46.047  13.963  1.00 170.57 ? 200 VAL B HG12 1 
ATOM   7428  H HG13 . VAL B 1 200 ? 3.996   44.958  14.256  1.00 170.57 ? 200 VAL B HG13 1 
ATOM   7429  H HG21 . VAL B 1 200 ? 5.633   43.028  12.268  1.00 172.63 ? 200 VAL B HG21 1 
ATOM   7430  H HG22 . VAL B 1 200 ? 4.083   42.925  12.601  1.00 172.63 ? 200 VAL B HG22 1 
ATOM   7431  H HG23 . VAL B 1 200 ? 4.558   43.216  11.113  1.00 172.63 ? 200 VAL B HG23 1 
ATOM   7432  N N    . GLY B 1 201 ? 3.527   47.652  10.631  1.00 137.01 ? 201 GLY B N    1 
ATOM   7433  C CA   . GLY B 1 201 ? 3.624   49.098  10.577  1.00 135.73 ? 201 GLY B CA   1 
ATOM   7434  C C    . GLY B 1 201 ? 4.856   49.672  11.231  1.00 132.15 ? 201 GLY B C    1 
ATOM   7435  O O    . GLY B 1 201 ? 4.846   50.838  11.639  1.00 130.13 ? 201 GLY B O    1 
ATOM   7436  H H    . GLY B 1 201 ? 3.444   47.272  9.864   1.00 164.42 ? 201 GLY B H    1 
ATOM   7437  H HA2  . GLY B 1 201 ? 3.626   49.375  9.648   1.00 162.88 ? 201 GLY B HA2  1 
ATOM   7438  H HA3  . GLY B 1 201 ? 2.849   49.478  11.019  1.00 162.88 ? 201 GLY B HA3  1 
ATOM   7439  N N    . SER B 1 202 ? 5.924   48.887  11.346  1.00 130.80 ? 202 SER B N    1 
ATOM   7440  C CA   . SER B 1 202 ? 7.159   49.364  11.950  1.00 126.50 ? 202 SER B CA   1 
ATOM   7441  C C    . SER B 1 202 ? 8.287   48.413  11.580  1.00 123.05 ? 202 SER B C    1 
ATOM   7442  O O    . SER B 1 202 ? 8.056   47.258  11.214  1.00 122.48 ? 202 SER B O    1 
ATOM   7443  C CB   . SER B 1 202 ? 7.031   49.484  13.473  1.00 124.60 ? 202 SER B CB   1 
ATOM   7444  O OG   . SER B 1 202 ? 6.686   50.805  13.848  1.00 124.87 ? 202 SER B OG   1 
ATOM   7445  H H    . SER B 1 202 ? 5.956   48.070  11.080  1.00 156.96 ? 202 SER B H    1 
ATOM   7446  H HA   . SER B 1 202 ? 7.372   50.240  11.593  1.00 151.81 ? 202 SER B HA   1 
ATOM   7447  H HB2  . SER B 1 202 ? 6.339   48.877  13.780  1.00 149.52 ? 202 SER B HB2  1 
ATOM   7448  H HB3  . SER B 1 202 ? 7.880   49.252  13.880  1.00 149.52 ? 202 SER B HB3  1 
ATOM   7449  H HG   . SER B 1 202 ? 5.954   51.021  13.497  1.00 149.84 ? 202 SER B HG   1 
ATOM   7450  N N    . GLY B 1 203 ? 9.516   48.921  11.687  1.00 117.12 ? 203 GLY B N    1 
ATOM   7451  C CA   . GLY B 1 203 ? 10.701  48.180  11.324  1.00 113.36 ? 203 GLY B CA   1 
ATOM   7452  C C    . GLY B 1 203 ? 11.492  47.730  12.542  1.00 109.43 ? 203 GLY B C    1 
ATOM   7453  O O    . GLY B 1 203 ? 11.288  48.192  13.663  1.00 110.80 ? 203 GLY B O    1 
ATOM   7454  H H    . GLY B 1 203 ? 9.682   49.713  11.976  1.00 140.54 ? 203 GLY B H    1 
ATOM   7455  H HA2  . GLY B 1 203 ? 10.447  47.394  10.816  1.00 136.03 ? 203 GLY B HA2  1 
ATOM   7456  H HA3  . GLY B 1 203 ? 11.274  48.738  10.776  1.00 136.03 ? 203 GLY B HA3  1 
ATOM   7457  N N    . VAL B 1 204 ? 12.416  46.804  12.295  1.00 106.53 ? 204 VAL B N    1 
ATOM   7458  C CA   . VAL B 1 204 ? 13.218  46.200  13.351  1.00 103.69 ? 204 VAL B CA   1 
ATOM   7459  C C    . VAL B 1 204 ? 14.645  46.016  12.853  1.00 100.87 ? 204 VAL B C    1 
ATOM   7460  O O    . VAL B 1 204 ? 14.871  45.731  11.672  1.00 99.59  ? 204 VAL B O    1 
ATOM   7461  C CB   . VAL B 1 204 ? 12.627  44.849  13.807  1.00 102.47 ? 204 VAL B CB   1 
ATOM   7462  C CG1  . VAL B 1 204 ? 11.112  44.939  13.932  1.00 106.31 ? 204 VAL B CG1  1 
ATOM   7463  C CG2  . VAL B 1 204 ? 13.020  43.741  12.842  1.00 101.71 ? 204 VAL B CG2  1 
ATOM   7464  H H    . VAL B 1 204 ? 12.597  46.505  11.509  1.00 127.83 ? 204 VAL B H    1 
ATOM   7465  H HA   . VAL B 1 204 ? 13.241  46.804  14.110  1.00 124.43 ? 204 VAL B HA   1 
ATOM   7466  H HB   . VAL B 1 204 ? 12.988  44.632  14.681  1.00 122.97 ? 204 VAL B HB   1 
ATOM   7467  H HG11 . VAL B 1 204 ? 10.783  44.136  14.366  1.00 127.57 ? 204 VAL B HG11 1 
ATOM   7468  H HG12 . VAL B 1 204 ? 10.884  45.719  14.462  1.00 127.57 ? 204 VAL B HG12 1 
ATOM   7469  H HG13 . VAL B 1 204 ? 10.726  45.017  13.046  1.00 127.57 ? 204 VAL B HG13 1 
ATOM   7470  H HG21 . VAL B 1 204 ? 12.419  42.989  12.963  1.00 122.06 ? 204 VAL B HG21 1 
ATOM   7471  H HG22 . VAL B 1 204 ? 12.953  44.075  11.934  1.00 122.06 ? 204 VAL B HG22 1 
ATOM   7472  H HG23 . VAL B 1 204 ? 13.932  43.468  13.028  1.00 122.06 ? 204 VAL B HG23 1 
ATOM   7473  N N    . TYR B 1 205 ? 15.607  46.180  13.759  1.00 98.28  ? 205 TYR B N    1 
ATOM   7474  C CA   . TYR B 1 205 ? 17.018  45.916  13.481  1.00 95.52  ? 205 TYR B CA   1 
ATOM   7475  C C    . TYR B 1 205 ? 17.310  44.499  13.966  1.00 95.60  ? 205 TYR B C    1 
ATOM   7476  O O    . TYR B 1 205 ? 17.420  44.252  15.170  1.00 96.74  ? 205 TYR B O    1 
ATOM   7477  C CB   . TYR B 1 205 ? 17.912  46.943  14.166  1.00 91.98  ? 205 TYR B CB   1 
ATOM   7478  C CG   . TYR B 1 205 ? 17.877  48.316  13.529  1.00 95.82  ? 205 TYR B CG   1 
ATOM   7479  C CD1  . TYR B 1 205 ? 16.838  49.198  13.791  1.00 96.68  ? 205 TYR B CD1  1 
ATOM   7480  C CD2  . TYR B 1 205 ? 18.888  48.732  12.669  1.00 95.08  ? 205 TYR B CD2  1 
ATOM   7481  C CE1  . TYR B 1 205 ? 16.804  50.456  13.213  1.00 99.26  ? 205 TYR B CE1  1 
ATOM   7482  C CE2  . TYR B 1 205 ? 18.864  49.987  12.087  1.00 94.39  ? 205 TYR B CE2  1 
ATOM   7483  C CZ   . TYR B 1 205 ? 17.821  50.846  12.363  1.00 98.80  ? 205 TYR B CZ   1 
ATOM   7484  O OH   . TYR B 1 205 ? 17.791  52.096  11.782  1.00 101.14 ? 205 TYR B OH   1 
ATOM   7485  H H    . TYR B 1 205 ? 15.464  46.450  14.563  1.00 117.93 ? 205 TYR B H    1 
ATOM   7486  H HA   . TYR B 1 205 ? 17.184  45.968  12.527  1.00 114.62 ? 205 TYR B HA   1 
ATOM   7487  H HB2  . TYR B 1 205 ? 17.625  47.039  15.088  1.00 110.38 ? 205 TYR B HB2  1 
ATOM   7488  H HB3  . TYR B 1 205 ? 18.828  46.627  14.135  1.00 110.38 ? 205 TYR B HB3  1 
ATOM   7489  H HD1  . TYR B 1 205 ? 16.153  48.940  14.364  1.00 116.02 ? 205 TYR B HD1  1 
ATOM   7490  H HD2  . TYR B 1 205 ? 19.593  48.156  12.481  1.00 114.10 ? 205 TYR B HD2  1 
ATOM   7491  H HE1  . TYR B 1 205 ? 16.100  51.036  13.396  1.00 119.11 ? 205 TYR B HE1  1 
ATOM   7492  H HE2  . TYR B 1 205 ? 19.546  50.249  11.512  1.00 113.26 ? 205 TYR B HE2  1 
ATOM   7493  H HH   . TYR B 1 205 ? 18.476  52.210  11.311  1.00 121.37 ? 205 TYR B HH   1 
ATOM   7494  N N    . GLU B 1 206 ? 17.430  43.566  13.027  1.00 94.48  ? 206 GLU B N    1 
ATOM   7495  C CA   . GLU B 1 206 ? 17.598  42.166  13.379  1.00 90.81  ? 206 GLU B CA   1 
ATOM   7496  C C    . GLU B 1 206 ? 19.025  41.883  13.841  1.00 86.95  ? 206 GLU B C    1 
ATOM   7497  O O    . GLU B 1 206 ? 19.972  42.602  13.510  1.00 84.21  ? 206 GLU B O    1 
ATOM   7498  C CB   . GLU B 1 206 ? 17.266  41.268  12.188  1.00 98.16  ? 206 GLU B CB   1 
ATOM   7499  C CG   . GLU B 1 206 ? 15.855  41.424  11.648  1.00 103.96 ? 206 GLU B CG   1 
ATOM   7500  C CD   . GLU B 1 206 ? 15.179  40.085  11.410  1.00 110.33 ? 206 GLU B CD   1 
ATOM   7501  O OE1  . GLU B 1 206 ? 15.623  39.346  10.498  1.00 104.63 ? 206 GLU B OE1  1 
ATOM   7502  O OE2  . GLU B 1 206 ? 14.213  39.769  12.139  1.00 106.85 ? 206 GLU B OE2  1 
ATOM   7503  H H    . GLU B 1 206 ? 17.418  43.720  12.181  1.00 113.37 ? 206 GLU B H    1 
ATOM   7504  H HA   . GLU B 1 206 ? 16.993  41.955  14.108  1.00 108.97 ? 206 GLU B HA   1 
ATOM   7505  H HB2  . GLU B 1 206 ? 17.880  41.475  11.466  1.00 117.80 ? 206 GLU B HB2  1 
ATOM   7506  H HB3  . GLU B 1 206 ? 17.374  40.343  12.460  1.00 117.80 ? 206 GLU B HB3  1 
ATOM   7507  H HG2  . GLU B 1 206 ? 15.323  41.921  12.289  1.00 124.75 ? 206 GLU B HG2  1 
ATOM   7508  H HG3  . GLU B 1 206 ? 15.889  41.900  10.804  1.00 124.75 ? 206 GLU B HG3  1 
ATOM   7509  N N    . ASN B 1 207 ? 19.168  40.808  14.619  1.00 88.05  ? 207 ASN B N    1 
ATOM   7510  C CA   . ASN B 1 207 ? 20.493  40.337  15.003  1.00 83.98  ? 207 ASN B CA   1 
ATOM   7511  C C    . ASN B 1 207 ? 21.237  39.727  13.823  1.00 82.06  ? 207 ASN B C    1 
ATOM   7512  O O    . ASN B 1 207 ? 22.468  39.635  13.862  1.00 81.47  ? 207 ASN B O    1 
ATOM   7513  C CB   . ASN B 1 207 ? 20.377  39.316  16.135  1.00 83.55  ? 207 ASN B CB   1 
ATOM   7514  C CG   . ASN B 1 207 ? 20.100  39.968  17.482  1.00 86.76  ? 207 ASN B CG   1 
ATOM   7515  O OD1  . ASN B 1 207 ? 20.475  41.118  17.715  1.00 85.79  ? 207 ASN B OD1  1 
ATOM   7516  N ND2  . ASN B 1 207 ? 19.446  39.233  18.374  1.00 86.33  ? 207 ASN B ND2  1 
ATOM   7517  H H    . ASN B 1 207 ? 18.519  40.340  14.934  1.00 105.65 ? 207 ASN B H    1 
ATOM   7518  H HA   . ASN B 1 207 ? 21.014  41.085  15.334  1.00 100.77 ? 207 ASN B HA   1 
ATOM   7519  H HB2  . ASN B 1 207 ? 19.647  38.707  15.940  1.00 100.26 ? 207 ASN B HB2  1 
ATOM   7520  H HB3  . ASN B 1 207 ? 21.210  38.824  16.205  1.00 100.26 ? 207 ASN B HB3  1 
ATOM   7521  H HD21 . ASN B 1 207 ? 19.202  38.432  18.176  1.00 103.59 ? 207 ASN B HD21 1 
ATOM   7522  H HD22 . ASN B 1 207 ? 19.266  39.558  19.150  1.00 103.59 ? 207 ASN B HD22 1 
ATOM   7523  N N    . SER B 1 208 ? 20.517  39.315  12.780  1.00 81.78  ? 208 SER B N    1 
ATOM   7524  C CA   . SER B 1 208 ? 21.104  38.756  11.570  1.00 78.98  ? 208 SER B CA   1 
ATOM   7525  C C    . SER B 1 208 ? 19.989  38.577  10.549  1.00 81.68  ? 208 SER B C    1 
ATOM   7526  O O    . SER B 1 208 ? 18.824  38.389  10.915  1.00 83.24  ? 208 SER B O    1 
ATOM   7527  C CB   . SER B 1 208 ? 21.813  37.427  11.850  1.00 76.33  ? 208 SER B CB   1 
ATOM   7528  O OG   . SER B 1 208 ? 20.927  36.328  11.768  1.00 76.77  ? 208 SER B OG   1 
ATOM   7529  H H    . SER B 1 208 ? 19.658  39.351  12.751  1.00 98.13  ? 208 SER B H    1 
ATOM   7530  H HA   . SER B 1 208 ? 21.763  39.366  11.203  1.00 94.78  ? 208 SER B HA   1 
ATOM   7531  H HB2  . SER B 1 208 ? 22.520  37.307  11.196  1.00 91.60  ? 208 SER B HB2  1 
ATOM   7532  H HB3  . SER B 1 208 ? 22.190  37.457  12.743  1.00 91.60  ? 208 SER B HB3  1 
ATOM   7533  H HG   . SER B 1 208 ? 21.343  35.613  11.911  1.00 92.12  ? 208 SER B HG   1 
ATOM   7534  N N    . CYS B 1 209 ? 20.355  38.655  9.266   1.00 81.20  ? 209 CYS B N    1 
ATOM   7535  C CA   . CYS B 1 209 ? 19.393  38.561  8.167   1.00 77.80  ? 209 CYS B CA   1 
ATOM   7536  C C    . CYS B 1 209 ? 20.028  37.746  7.044   1.00 80.61  ? 209 CYS B C    1 
ATOM   7537  O O    . CYS B 1 209 ? 20.840  38.269  6.270   1.00 80.65  ? 209 CYS B O    1 
ATOM   7538  C CB   . CYS B 1 209 ? 18.980  39.944  7.676   1.00 79.33  ? 209 CYS B CB   1 
ATOM   7539  S SG   . CYS B 1 209 ? 17.593  39.952  6.507   1.00 83.91  ? 209 CYS B SG   1 
ATOM   7540  H H    . CYS B 1 209 ? 21.167  38.765  9.005   1.00 97.44  ? 209 CYS B H    1 
ATOM   7541  H HA   . CYS B 1 209 ? 18.604  38.089  8.478   1.00 93.35  ? 209 CYS B HA   1 
ATOM   7542  H HB2  . CYS B 1 209 ? 18.720  40.478  8.443   1.00 95.19  ? 209 CYS B HB2  1 
ATOM   7543  H HB3  . CYS B 1 209 ? 19.740  40.352  7.231   1.00 95.19  ? 209 CYS B HB3  1 
ATOM   7544  H HG   . CYS B 1 209 ? 17.343  41.086  6.204   1.00 100.69 ? 209 CYS B HG   1 
ATOM   7545  N N    . ALA B 1 210 ? 19.639  36.472  6.942   1.00 80.77  ? 210 ALA B N    1 
ATOM   7546  C CA   . ALA B 1 210 ? 20.219  35.606  5.920   1.00 77.05  ? 210 ALA B CA   1 
ATOM   7547  C C    . ALA B 1 210 ? 19.855  36.077  4.516   1.00 79.06  ? 210 ALA B C    1 
ATOM   7548  O O    . ALA B 1 210 ? 20.712  36.103  3.623   1.00 76.83  ? 210 ALA B O    1 
ATOM   7549  C CB   . ALA B 1 210 ? 19.760  34.165  6.134   1.00 73.27  ? 210 ALA B CB   1 
ATOM   7550  H H    . ALA B 1 210 ? 19.052  36.094  7.444   1.00 96.92  ? 210 ALA B H    1 
ATOM   7551  H HA   . ALA B 1 210 ? 21.185  35.633  6.004   1.00 92.45  ? 210 ALA B HA   1 
ATOM   7552  H HB1  . ALA B 1 210 ? 20.196  33.595  5.481   1.00 87.93  ? 210 ALA B HB1  1 
ATOM   7553  H HB2  . ALA B 1 210 ? 20.003  33.886  7.030   1.00 87.93  ? 210 ALA B HB2  1 
ATOM   7554  H HB3  . ALA B 1 210 ? 18.798  34.120  6.022   1.00 87.93  ? 210 ALA B HB3  1 
ATOM   7555  N N    . SER B 1 211 ? 18.589  36.444  4.295   1.00 80.10  ? 211 SER B N    1 
ATOM   7556  C CA   . SER B 1 211 ? 18.174  36.884  2.965   1.00 78.97  ? 211 SER B CA   1 
ATOM   7557  C C    . SER B 1 211 ? 18.875  38.178  2.573   1.00 81.27  ? 211 SER B C    1 
ATOM   7558  O O    . SER B 1 211 ? 19.303  38.341  1.424   1.00 80.57  ? 211 SER B O    1 
ATOM   7559  C CB   . SER B 1 211 ? 16.656  37.070  2.920   1.00 77.69  ? 211 SER B CB   1 
ATOM   7560  O OG   . SER B 1 211 ? 16.267  38.246  3.612   1.00 79.61  ? 211 SER B OG   1 
ATOM   7561  H H    . SER B 1 211 ? 17.965  36.448  4.887   1.00 96.12  ? 211 SER B H    1 
ATOM   7562  H HA   . SER B 1 211 ? 18.413  36.199  2.322   1.00 94.76  ? 211 SER B HA   1 
ATOM   7563  H HB2  . SER B 1 211 ? 16.375  37.141  1.995   1.00 93.23  ? 211 SER B HB2  1 
ATOM   7564  H HB3  . SER B 1 211 ? 16.233  36.304  3.338   1.00 93.23  ? 211 SER B HB3  1 
ATOM   7565  H HG   . SER B 1 211 ? 15.430  38.320  3.604   1.00 95.53  ? 211 SER B HG   1 
ATOM   7566  N N    . GLY B 1 212 ? 18.995  39.117  3.513   1.00 81.74  ? 212 GLY B N    1 
ATOM   7567  C CA   . GLY B 1 212 ? 19.696  40.355  3.228   1.00 80.66  ? 212 GLY B CA   1 
ATOM   7568  C C    . GLY B 1 212 ? 21.182  40.178  3.011   1.00 78.54  ? 212 GLY B C    1 
ATOM   7569  O O    . GLY B 1 212 ? 21.808  41.027  2.368   1.00 79.26  ? 212 GLY B O    1 
ATOM   7570  H H    . GLY B 1 212 ? 18.682  39.057  4.311   1.00 98.09  ? 212 GLY B H    1 
ATOM   7571  H HA2  . GLY B 1 212 ? 19.321  40.753  2.426   1.00 96.79  ? 212 GLY B HA2  1 
ATOM   7572  H HA3  . GLY B 1 212 ? 19.571  40.966  3.971   1.00 96.79  ? 212 GLY B HA3  1 
ATOM   7573  N N    . THR B 1 213 ? 21.764  39.101  3.547   1.00 78.81  ? 213 THR B N    1 
ATOM   7574  C CA   . THR B 1 213 ? 23.172  38.821  3.291   1.00 80.15  ? 213 THR B CA   1 
ATOM   7575  C C    . THR B 1 213 ? 23.381  38.330  1.865   1.00 79.90  ? 213 THR B C    1 
ATOM   7576  O O    . THR B 1 213 ? 24.422  38.609  1.258   1.00 80.81  ? 213 THR B O    1 
ATOM   7577  C CB   . THR B 1 213 ? 23.699  37.789  4.289   1.00 79.52  ? 213 THR B CB   1 
ATOM   7578  O OG1  . THR B 1 213 ? 23.161  38.065  5.589   1.00 74.40  ? 213 THR B OG1  1 
ATOM   7579  C CG2  . THR B 1 213 ? 25.224  37.821  4.362   1.00 78.13  ? 213 THR B CG2  1 
ATOM   7580  H H    . THR B 1 213 ? 21.370  38.528  4.052   1.00 94.57  ? 213 THR B H    1 
ATOM   7581  H HA   . THR B 1 213 ? 23.683  39.637  3.414   1.00 96.18  ? 213 THR B HA   1 
ATOM   7582  H HB   . THR B 1 213 ? 23.430  36.903  4.000   1.00 95.43  ? 213 THR B HB   1 
ATOM   7583  H HG1  . THR B 1 213 ? 23.352  37.440  6.117   1.00 89.28  ? 213 THR B HG1  1 
ATOM   7584  H HG21 . THR B 1 213 ? 25.539  37.167  5.005   1.00 93.75  ? 213 THR B HG21 1 
ATOM   7585  H HG22 . THR B 1 213 ? 25.602  37.616  3.492   1.00 93.75  ? 213 THR B HG22 1 
ATOM   7586  H HG23 . THR B 1 213 ? 25.524  38.702  4.636   1.00 93.75  ? 213 THR B HG23 1 
ATOM   7587  N N    . THR B 1 214 ? 22.412  37.588  1.319   1.00 79.84  ? 214 THR B N    1 
ATOM   7588  C CA   . THR B 1 214 ? 22.481  37.207  -0.087  1.00 79.77  ? 214 THR B CA   1 
ATOM   7589  C C    . THR B 1 214 ? 22.332  38.431  -0.983  1.00 80.27  ? 214 THR B C    1 
ATOM   7590  O O    . THR B 1 214 ? 23.014  38.546  -2.008  1.00 81.25  ? 214 THR B O    1 
ATOM   7591  C CB   . THR B 1 214 ? 21.407  36.167  -0.412  1.00 79.02  ? 214 THR B CB   1 
ATOM   7592  O OG1  . THR B 1 214 ? 20.107  36.750  -0.258  1.00 77.53  ? 214 THR B OG1  1 
ATOM   7593  C CG2  . THR B 1 214 ? 21.535  34.956  0.507   1.00 76.34  ? 214 THR B CG2  1 
ATOM   7594  H H    . THR B 1 214 ? 21.718  37.298  1.736   1.00 95.80  ? 214 THR B H    1 
ATOM   7595  H HA   . THR B 1 214 ? 23.344  36.800  -0.261  1.00 95.73  ? 214 THR B HA   1 
ATOM   7596  H HB   . THR B 1 214 ? 21.517  35.867  -1.327  1.00 94.82  ? 214 THR B HB   1 
ATOM   7597  H HG1  . THR B 1 214 ? 19.998  37.004  0.535   1.00 93.03  ? 214 THR B HG1  1 
ATOM   7598  H HG21 . THR B 1 214 ? 20.902  34.271  0.242   1.00 91.61  ? 214 THR B HG21 1 
ATOM   7599  H HG22 . THR B 1 214 ? 22.433  34.593  0.454   1.00 91.61  ? 214 THR B HG22 1 
ATOM   7600  H HG23 . THR B 1 214 ? 21.354  35.215  1.424   1.00 91.61  ? 214 THR B HG23 1 
ATOM   7601  N N    . ALA B 1 215 ? 21.444  39.357  -0.613  1.00 80.11  ? 215 ALA B N    1 
ATOM   7602  C CA   . ALA B 1 215 ? 21.376  40.635  -1.317  1.00 83.74  ? 215 ALA B CA   1 
ATOM   7603  C C    . ALA B 1 215 ? 22.733  41.328  -1.293  1.00 82.73  ? 215 ALA B C    1 
ATOM   7604  O O    . ALA B 1 215 ? 23.256  41.744  -2.332  1.00 85.20  ? 215 ALA B O    1 
ATOM   7605  C CB   . ALA B 1 215 ? 20.304  41.528  -0.690  1.00 79.75  ? 215 ALA B CB   1 
ATOM   7606  H H    . ALA B 1 215 ? 20.881  39.271  0.032   1.00 96.13  ? 215 ALA B H    1 
ATOM   7607  H HA   . ALA B 1 215 ? 21.126  40.476  -2.240  1.00 100.49 ? 215 ALA B HA   1 
ATOM   7608  H HB1  . ALA B 1 215 ? 20.271  42.369  -1.173  1.00 95.70  ? 215 ALA B HB1  1 
ATOM   7609  H HB2  . ALA B 1 215 ? 19.446  41.079  -0.748  1.00 95.70  ? 215 ALA B HB2  1 
ATOM   7610  H HB3  . ALA B 1 215 ? 20.531  41.689  0.239   1.00 95.70  ? 215 ALA B HB3  1 
ATOM   7611  N N    . LEU B 1 216 ? 23.318  41.462  -0.102  1.00 81.35  ? 216 LEU B N    1 
ATOM   7612  C CA   . LEU B 1 216 ? 24.689  41.945  0.014   1.00 82.20  ? 216 LEU B CA   1 
ATOM   7613  C C    . LEU B 1 216 ? 25.629  41.107  -0.844  1.00 83.29  ? 216 LEU B C    1 
ATOM   7614  O O    . LEU B 1 216 ? 26.450  41.646  -1.593  1.00 86.78  ? 216 LEU B O    1 
ATOM   7615  C CB   . LEU B 1 216 ? 25.110  41.916  1.486   1.00 85.00  ? 216 LEU B CB   1 
ATOM   7616  C CG   . LEU B 1 216 ? 26.356  42.655  1.971   1.00 86.01  ? 216 LEU B CG   1 
ATOM   7617  C CD1  . LEU B 1 216 ? 27.614  42.125  1.291   1.00 90.67  ? 216 LEU B CD1  1 
ATOM   7618  C CD2  . LEU B 1 216 ? 26.223  44.154  1.748   1.00 87.68  ? 216 LEU B CD2  1 
ATOM   7619  H H    . LEU B 1 216 ? 22.942  41.281  0.650   1.00 97.62  ? 216 LEU B H    1 
ATOM   7620  H HA   . LEU B 1 216 ? 24.744  42.862  -0.296  1.00 98.63  ? 216 LEU B HA   1 
ATOM   7621  H HB2  . LEU B 1 216 ? 24.371  42.282  1.997   1.00 102.00 ? 216 LEU B HB2  1 
ATOM   7622  H HB3  . LEU B 1 216 ? 25.247  40.985  1.721   1.00 102.00 ? 216 LEU B HB3  1 
ATOM   7623  H HG   . LEU B 1 216 ? 26.447  42.499  2.924   1.00 103.21 ? 216 LEU B HG   1 
ATOM   7624  H HD11 . LEU B 1 216 ? 28.391  42.541  1.696   1.00 108.81 ? 216 LEU B HD11 1 
ATOM   7625  H HD12 . LEU B 1 216 ? 27.655  41.163  1.409   1.00 108.81 ? 216 LEU B HD12 1 
ATOM   7626  H HD13 . LEU B 1 216 ? 27.577  42.341  0.346   1.00 108.81 ? 216 LEU B HD13 1 
ATOM   7627  H HD21 . LEU B 1 216 ? 27.053  44.586  2.003   1.00 105.21 ? 216 LEU B HD21 1 
ATOM   7628  H HD22 . LEU B 1 216 ? 26.038  44.319  0.811   1.00 105.21 ? 216 LEU B HD22 1 
ATOM   7629  H HD23 . LEU B 1 216 ? 25.494  44.490  2.294   1.00 105.21 ? 216 LEU B HD23 1 
ATOM   7630  N N    . GLY B 1 217 ? 25.506  39.782  -0.763  1.00 82.70  ? 217 GLY B N    1 
ATOM   7631  C CA   . GLY B 1 217 ? 26.383  38.920  -1.540  1.00 85.69  ? 217 GLY B CA   1 
ATOM   7632  C C    . GLY B 1 217 ? 26.264  39.156  -3.033  1.00 87.35  ? 217 GLY B C    1 
ATOM   7633  O O    . GLY B 1 217 ? 27.266  39.349  -3.727  1.00 88.12  ? 217 GLY B O    1 
ATOM   7634  H H    . GLY B 1 217 ? 24.933  39.367  -0.274  1.00 99.24  ? 217 GLY B H    1 
ATOM   7635  H HA2  . GLY B 1 217 ? 27.303  39.082  -1.278  1.00 102.83 ? 217 GLY B HA2  1 
ATOM   7636  H HA3  . GLY B 1 217 ? 26.162  37.993  -1.360  1.00 102.83 ? 217 GLY B HA3  1 
ATOM   7637  N N    . TYR B 1 218 ? 25.033  39.136  -3.551  1.00 85.53  ? 218 TYR B N    1 
ATOM   7638  C CA   . TYR B 1 218 ? 24.823  39.391  -4.971  1.00 86.39  ? 218 TYR B CA   1 
ATOM   7639  C C    . TYR B 1 218 ? 25.412  40.740  -5.375  1.00 90.14  ? 218 TYR B C    1 
ATOM   7640  O O    . TYR B 1 218 ? 26.116  40.852  -6.386  1.00 91.62  ? 218 TYR B O    1 
ATOM   7641  C CB   . TYR B 1 218 ? 23.328  39.353  -5.303  1.00 86.11  ? 218 TYR B CB   1 
ATOM   7642  C CG   . TYR B 1 218 ? 22.677  37.989  -5.236  1.00 84.15  ? 218 TYR B CG   1 
ATOM   7643  C CD1  . TYR B 1 218 ? 23.187  36.910  -5.950  1.00 84.26  ? 218 TYR B CD1  1 
ATOM   7644  C CD2  . TYR B 1 218 ? 21.537  37.786  -4.470  1.00 82.69  ? 218 TYR B CD2  1 
ATOM   7645  C CE1  . TYR B 1 218 ? 22.586  35.664  -5.887  1.00 81.53  ? 218 TYR B CE1  1 
ATOM   7646  C CE2  . TYR B 1 218 ? 20.930  36.549  -4.404  1.00 82.61  ? 218 TYR B CE2  1 
ATOM   7647  C CZ   . TYR B 1 218 ? 21.456  35.493  -5.113  1.00 83.58  ? 218 TYR B CZ   1 
ATOM   7648  O OH   . TYR B 1 218 ? 20.848  34.262  -5.040  1.00 87.47  ? 218 TYR B OH   1 
ATOM   7649  H H    . TYR B 1 218 ? 24.314  38.979  -3.105  1.00 102.64 ? 218 TYR B H    1 
ATOM   7650  H HA   . TYR B 1 218 ? 25.266  38.692  -5.477  1.00 103.66 ? 218 TYR B HA   1 
ATOM   7651  H HB2  . TYR B 1 218 ? 22.862  39.926  -4.674  1.00 103.33 ? 218 TYR B HB2  1 
ATOM   7652  H HB3  . TYR B 1 218 ? 23.208  39.686  -6.206  1.00 103.33 ? 218 TYR B HB3  1 
ATOM   7653  H HD1  . TYR B 1 218 ? 23.945  37.027  -6.477  1.00 101.11 ? 218 TYR B HD1  1 
ATOM   7654  H HD2  . TYR B 1 218 ? 21.176  38.497  -3.992  1.00 99.22  ? 218 TYR B HD2  1 
ATOM   7655  H HE1  . TYR B 1 218 ? 22.940  34.948  -6.363  1.00 97.83  ? 218 TYR B HE1  1 
ATOM   7656  H HE2  . TYR B 1 218 ? 20.169  36.429  -3.883  1.00 99.13  ? 218 TYR B HE2  1 
ATOM   7657  H HH   . TYR B 1 218 ? 20.187  34.299  -4.522  1.00 104.97 ? 218 TYR B HH   1 
ATOM   7658  N N    . TYR B 1 219 ? 25.118  41.782  -4.595  1.00 87.82  ? 219 TYR B N    1 
ATOM   7659  C CA   . TYR B 1 219 ? 25.576  43.129  -4.927  1.00 89.52  ? 219 TYR B CA   1 
ATOM   7660  C C    . TYR B 1 219 ? 27.094  43.219  -4.911  1.00 91.36  ? 219 TYR B C    1 
ATOM   7661  O O    . TYR B 1 219 ? 27.689  43.905  -5.749  1.00 94.50  ? 219 TYR B O    1 
ATOM   7662  C CB   . TYR B 1 219 ? 24.944  44.123  -3.946  1.00 92.20  ? 219 TYR B CB   1 
ATOM   7663  C CG   . TYR B 1 219 ? 25.533  45.517  -3.904  1.00 95.44  ? 219 TYR B CG   1 
ATOM   7664  C CD1  . TYR B 1 219 ? 25.015  46.536  -4.694  1.00 96.24  ? 219 TYR B CD1  1 
ATOM   7665  C CD2  . TYR B 1 219 ? 26.575  45.827  -3.036  1.00 96.89  ? 219 TYR B CD2  1 
ATOM   7666  C CE1  . TYR B 1 219 ? 25.538  47.819  -4.642  1.00 97.56  ? 219 TYR B CE1  1 
ATOM   7667  C CE2  . TYR B 1 219 ? 27.104  47.105  -2.978  1.00 99.41  ? 219 TYR B CE2  1 
ATOM   7668  C CZ   . TYR B 1 219 ? 26.582  48.097  -3.780  1.00 98.51  ? 219 TYR B CZ   1 
ATOM   7669  O OH   . TYR B 1 219 ? 27.113  49.367  -3.716  1.00 99.51  ? 219 TYR B OH   1 
ATOM   7670  H H    . TYR B 1 219 ? 24.657  41.736  -3.870  1.00 105.39 ? 219 TYR B H    1 
ATOM   7671  H HA   . TYR B 1 219 ? 25.289  43.363  -5.824  1.00 107.42 ? 219 TYR B HA   1 
ATOM   7672  H HB2  . TYR B 1 219 ? 24.007  44.220  -4.179  1.00 110.64 ? 219 TYR B HB2  1 
ATOM   7673  H HB3  . TYR B 1 219 ? 25.027  43.755  -3.052  1.00 110.64 ? 219 TYR B HB3  1 
ATOM   7674  H HD1  . TYR B 1 219 ? 24.306  46.354  -5.268  1.00 116.27 ? 219 TYR B HD1  1 
ATOM   7675  H HD2  . TYR B 1 219 ? 26.922  45.163  -2.485  1.00 115.49 ? 219 TYR B HD2  1 
ATOM   7676  H HE1  . TYR B 1 219 ? 25.187  48.489  -5.184  1.00 119.29 ? 219 TYR B HE1  1 
ATOM   7677  H HE2  . TYR B 1 219 ? 27.809  47.293  -2.401  1.00 117.07 ? 219 TYR B HE2  1 
ATOM   7678  H HH   . TYR B 1 219 ? 26.709  49.874  -4.250  1.00 119.41 ? 219 TYR B HH   1 
ATOM   7679  N N    . LEU B 1 220 ? 27.742  42.535  -3.972  1.00 94.20  ? 220 LEU B N    1 
ATOM   7680  C CA   . LEU B 1 220 ? 29.196  42.571  -3.921  1.00 95.10  ? 220 LEU B CA   1 
ATOM   7681  C C    . LEU B 1 220 ? 29.833  41.729  -5.016  1.00 93.24  ? 220 LEU B C    1 
ATOM   7682  O O    . LEU B 1 220 ? 30.986  41.981  -5.379  1.00 94.56  ? 220 LEU B O    1 
ATOM   7683  C CB   . LEU B 1 220 ? 29.705  42.089  -2.563  1.00 91.10  ? 220 LEU B CB   1 
ATOM   7684  C CG   . LEU B 1 220 ? 29.645  43.074  -1.396  1.00 89.36  ? 220 LEU B CG   1 
ATOM   7685  C CD1  . LEU B 1 220 ? 30.496  42.535  -0.236  1.00 90.65  ? 220 LEU B CD1  1 
ATOM   7686  C CD2  . LEU B 1 220 ? 30.093  44.472  -1.767  1.00 86.71  ? 220 LEU B CD2  1 
ATOM   7687  H H    . LEU B 1 220 ? 27.369  42.053  -3.366  1.00 113.04 ? 220 LEU B H    1 
ATOM   7688  H HA   . LEU B 1 220 ? 29.479  43.492  -4.031  1.00 114.12 ? 220 LEU B HA   1 
ATOM   7689  H HB2  . LEU B 1 220 ? 29.178  41.316  -2.305  1.00 109.32 ? 220 LEU B HB2  1 
ATOM   7690  H HB3  . LEU B 1 220 ? 30.635  41.835  -2.668  1.00 109.32 ? 220 LEU B HB3  1 
ATOM   7691  H HG   . LEU B 1 220 ? 28.717  43.155  -1.124  1.00 107.23 ? 220 LEU B HG   1 
ATOM   7692  H HD11 . LEU B 1 220 ? 30.417  43.138  0.520   1.00 108.78 ? 220 LEU B HD11 1 
ATOM   7693  H HD12 . LEU B 1 220 ? 30.175  41.653  0.008   1.00 108.78 ? 220 LEU B HD12 1 
ATOM   7694  H HD13 . LEU B 1 220 ? 31.422  42.482  -0.522  1.00 108.78 ? 220 LEU B HD13 1 
ATOM   7695  H HD21 . LEU B 1 220 ? 30.228  44.986  -0.955  1.00 104.05 ? 220 LEU B HD21 1 
ATOM   7696  H HD22 . LEU B 1 220 ? 30.923  44.416  -2.265  1.00 104.05 ? 220 LEU B HD22 1 
ATOM   7697  H HD23 . LEU B 1 220 ? 29.407  44.889  -2.312  1.00 104.05 ? 220 LEU B HD23 1 
ATOM   7698  N N    . LYS B 1 221 ? 29.114  40.730  -5.534  1.00 95.59  ? 221 LYS B N    1 
ATOM   7699  C CA   . LYS B 1 221 ? 29.648  39.927  -6.629  1.00 95.88  ? 221 LYS B CA   1 
ATOM   7700  C C    . LYS B 1 221 ? 29.641  40.712  -7.935  1.00 97.25  ? 221 LYS B C    1 
ATOM   7701  O O    . LYS B 1 221 ? 30.576  40.603  -8.737  1.00 99.97  ? 221 LYS B O    1 
ATOM   7702  C CB   . LYS B 1 221 ? 28.844  38.635  -6.774  1.00 92.68  ? 221 LYS B CB   1 
ATOM   7703  C CG   . LYS B 1 221 ? 29.292  37.736  -7.929  1.00 93.83  ? 221 LYS B CG   1 
ATOM   7704  C CD   . LYS B 1 221 ? 30.791  37.456  -7.887  1.00 96.05  ? 221 LYS B CD   1 
ATOM   7705  C CE   . LYS B 1 221 ? 31.230  36.542  -9.026  1.00 101.63 ? 221 LYS B CE   1 
ATOM   7706  N NZ   . LYS B 1 221 ? 30.256  35.445  -9.298  1.00 100.61 ? 221 LYS B NZ   1 
ATOM   7707  H H    . LYS B 1 221 ? 28.327  40.501  -5.273  1.00 114.71 ? 221 LYS B H    1 
ATOM   7708  H HA   . LYS B 1 221 ? 30.566  39.686  -6.425  1.00 115.06 ? 221 LYS B HA   1 
ATOM   7709  H HB2  . LYS B 1 221 ? 28.930  38.124  -5.954  1.00 111.22 ? 221 LYS B HB2  1 
ATOM   7710  H HB3  . LYS B 1 221 ? 27.914  38.865  -6.925  1.00 111.22 ? 221 LYS B HB3  1 
ATOM   7711  H HG2  . LYS B 1 221 ? 28.824  36.888  -7.873  1.00 112.60 ? 221 LYS B HG2  1 
ATOM   7712  H HG3  . LYS B 1 221 ? 29.089  38.172  -8.771  1.00 112.60 ? 221 LYS B HG3  1 
ATOM   7713  H HD2  . LYS B 1 221 ? 31.275  38.293  -7.967  1.00 115.26 ? 221 LYS B HD2  1 
ATOM   7714  H HD3  . LYS B 1 221 ? 31.012  37.022  -7.048  1.00 115.26 ? 221 LYS B HD3  1 
ATOM   7715  H HE2  . LYS B 1 221 ? 31.322  37.068  -9.836  1.00 121.96 ? 221 LYS B HE2  1 
ATOM   7716  H HE3  . LYS B 1 221 ? 32.080  36.136  -8.796  1.00 121.96 ? 221 LYS B HE3  1 
ATOM   7717  H HZ1  . LYS B 1 221 ? 30.592  34.882  -9.900  1.00 120.73 ? 221 LYS B HZ1  1 
ATOM   7718  H HZ2  . LYS B 1 221 ? 30.084  34.998  -8.548  1.00 120.73 ? 221 LYS B HZ2  1 
ATOM   7719  H HZ3  . LYS B 1 221 ? 29.496  35.784  -9.613  1.00 120.73 ? 221 LYS B HZ3  1 
ATOM   7720  N N    . LYS B 1 222 ? 28.598  41.513  -8.165  1.00 96.35  ? 222 LYS B N    1 
ATOM   7721  C CA   . LYS B 1 222 ? 28.522  42.305  -9.386  1.00 97.47  ? 222 LYS B CA   1 
ATOM   7722  C C    . LYS B 1 222 ? 29.358  43.575  -9.284  1.00 98.91  ? 222 LYS B C    1 
ATOM   7723  O O    . LYS B 1 222 ? 30.008  43.967  -10.256 1.00 100.92 ? 222 LYS B O    1 
ATOM   7724  C CB   . LYS B 1 222 ? 27.063  42.649  -9.691  1.00 97.11  ? 222 LYS B CB   1 
ATOM   7725  C CG   . LYS B 1 222 ? 26.804  43.105  -11.118 1.00 103.56 ? 222 LYS B CG   1 
ATOM   7726  C CD   . LYS B 1 222 ? 26.551  41.922  -12.045 1.00 106.54 ? 222 LYS B CD   1 
ATOM   7727  C CE   . LYS B 1 222 ? 25.898  42.363  -13.348 1.00 108.33 ? 222 LYS B CE   1 
ATOM   7728  N NZ   . LYS B 1 222 ? 24.543  41.764  -13.522 1.00 109.02 ? 222 LYS B NZ   1 
ATOM   7729  H H    . LYS B 1 222 ? 27.930  41.614  -7.633  1.00 115.62 ? 222 LYS B H    1 
ATOM   7730  H HA   . LYS B 1 222 ? 28.869  41.779  -10.124 1.00 116.96 ? 222 LYS B HA   1 
ATOM   7731  H HB2  . LYS B 1 222 ? 26.521  41.860  -9.533  1.00 116.53 ? 222 LYS B HB2  1 
ATOM   7732  H HB3  . LYS B 1 222 ? 26.786  43.366  -9.100  1.00 116.53 ? 222 LYS B HB3  1 
ATOM   7733  H HG2  . LYS B 1 222 ? 26.022  43.678  -11.135 1.00 124.27 ? 222 LYS B HG2  1 
ATOM   7734  H HG3  . LYS B 1 222 ? 27.577  43.590  -11.446 1.00 124.27 ? 222 LYS B HG3  1 
ATOM   7735  H HD2  . LYS B 1 222 ? 27.396  41.495  -12.258 1.00 127.84 ? 222 LYS B HD2  1 
ATOM   7736  H HD3  . LYS B 1 222 ? 25.961  41.290  -11.607 1.00 127.84 ? 222 LYS B HD3  1 
ATOM   7737  H HE2  . LYS B 1 222 ? 25.804  43.329  -13.347 1.00 129.99 ? 222 LYS B HE2  1 
ATOM   7738  H HE3  . LYS B 1 222 ? 26.451  42.084  -14.094 1.00 129.99 ? 222 LYS B HE3  1 
ATOM   7739  H HZ1  . LYS B 1 222 ? 24.185  42.038  -14.290 1.00 130.82 ? 222 LYS B HZ1  1 
ATOM   7740  H HZ2  . LYS B 1 222 ? 24.602  40.876  -13.531 1.00 130.82 ? 222 LYS B HZ2  1 
ATOM   7741  H HZ3  . LYS B 1 222 ? 24.012  42.011  -12.852 1.00 130.82 ? 222 LYS B HZ3  1 
ATOM   7742  N N    . CYS B 1 223 ? 29.375  44.215  -8.119  1.00 99.51  ? 223 CYS B N    1 
ATOM   7743  C CA   . CYS B 1 223 ? 30.003  45.520  -7.953  1.00 101.38 ? 223 CYS B CA   1 
ATOM   7744  C C    . CYS B 1 223 ? 31.443  45.454  -7.456  1.00 101.95 ? 223 CYS B C    1 
ATOM   7745  O O    . CYS B 1 223 ? 32.085  46.505  -7.329  1.00 100.90 ? 223 CYS B O    1 
ATOM   7746  C CB   . CYS B 1 223 ? 29.184  46.381  -6.981  1.00 98.57  ? 223 CYS B CB   1 
ATOM   7747  S SG   . CYS B 1 223 ? 27.640  47.021  -7.658  1.00 108.87 ? 223 CYS B SG   1 
ATOM   7748  H H    . CYS B 1 223 ? 29.024  43.907  -7.397  1.00 119.41 ? 223 CYS B H    1 
ATOM   7749  H HA   . CYS B 1 223 ? 30.011  45.953  -8.822  1.00 121.66 ? 223 CYS B HA   1 
ATOM   7750  H HB2  . CYS B 1 223 ? 28.961  45.842  -6.206  1.00 118.29 ? 223 CYS B HB2  1 
ATOM   7751  H HB3  . CYS B 1 223 ? 29.723  47.141  -6.714  1.00 118.29 ? 223 CYS B HB3  1 
ATOM   7752  H HG   . CYS B 1 223 ? 27.130  47.746  -6.849  1.00 130.64 ? 223 CYS B HG   1 
ATOM   7753  N N    . LYS B 1 224 ? 31.962  44.265  -7.162  1.00 104.71 ? 224 LYS B N    1 
ATOM   7754  C CA   . LYS B 1 224 ? 33.321  44.153  -6.645  1.00 103.33 ? 224 LYS B CA   1 
ATOM   7755  C C    . LYS B 1 224 ? 33.989  42.830  -6.996  1.00 102.30 ? 224 LYS B C    1 
ATOM   7756  O O    . LYS B 1 224 ? 35.155  42.642  -6.637  1.00 100.16 ? 224 LYS B O    1 
ATOM   7757  C CB   . LYS B 1 224 ? 33.318  44.350  -5.111  1.00 98.91  ? 224 LYS B CB   1 
ATOM   7758  C CG   . LYS B 1 224 ? 33.561  45.794  -4.657  1.00 98.15  ? 224 LYS B CG   1 
ATOM   7759  C CD   . LYS B 1 224 ? 33.610  45.922  -3.138  1.00 101.37 ? 224 LYS B CD   1 
ATOM   7760  C CE   . LYS B 1 224 ? 35.013  46.263  -2.633  1.00 102.32 ? 224 LYS B CE   1 
ATOM   7761  N NZ   . LYS B 1 224 ? 35.283  45.686  -1.272  1.00 99.54  ? 224 LYS B NZ   1 
ATOM   7762  H H    . LYS B 1 224 ? 31.552  43.514  -7.253  1.00 125.65 ? 224 LYS B H    1 
ATOM   7763  H HA   . LYS B 1 224 ? 33.861  44.862  -7.028  1.00 123.99 ? 224 LYS B HA   1 
ATOM   7764  H HB2  . LYS B 1 224 ? 32.454  44.075  -4.766  1.00 118.70 ? 224 LYS B HB2  1 
ATOM   7765  H HB3  . LYS B 1 224 ? 34.018  43.800  -4.726  1.00 118.70 ? 224 LYS B HB3  1 
ATOM   7766  H HG2  . LYS B 1 224 ? 34.409  46.101  -5.013  1.00 117.78 ? 224 LYS B HG2  1 
ATOM   7767  H HG3  . LYS B 1 224 ? 32.841  46.356  -4.984  1.00 117.78 ? 224 LYS B HG3  1 
ATOM   7768  H HD2  . LYS B 1 224 ? 33.008  46.630  -2.858  1.00 121.65 ? 224 LYS B HD2  1 
ATOM   7769  H HD3  . LYS B 1 224 ? 33.341  45.081  -2.737  1.00 121.65 ? 224 LYS B HD3  1 
ATOM   7770  H HE2  . LYS B 1 224 ? 35.669  45.903  -3.250  1.00 122.79 ? 224 LYS B HE2  1 
ATOM   7771  H HE3  . LYS B 1 224 ? 35.105  47.227  -2.577  1.00 122.79 ? 224 LYS B HE3  1 
ATOM   7772  H HZ1  . LYS B 1 224 ? 36.122  45.857  -1.030  1.00 119.45 ? 224 LYS B HZ1  1 
ATOM   7773  H HZ2  . LYS B 1 224 ? 34.730  46.045  -0.674  1.00 119.45 ? 224 LYS B HZ2  1 
ATOM   7774  H HZ3  . LYS B 1 224 ? 35.160  44.804  -1.285  1.00 119.45 ? 224 LYS B HZ3  1 
ATOM   7775  N N    . ASN B 1 225 ? 33.314  41.919  -7.691  1.00 109.83 ? 225 ASN B N    1 
ATOM   7776  C CA   . ASN B 1 225 ? 33.826  40.579  -7.967  1.00 111.92 ? 225 ASN B CA   1 
ATOM   7777  C C    . ASN B 1 225 ? 34.255  39.883  -6.674  1.00 111.46 ? 225 ASN B C    1 
ATOM   7778  O O    . ASN B 1 225 ? 35.420  39.535  -6.473  1.00 110.11 ? 225 ASN B O    1 
ATOM   7779  C CB   . ASN B 1 225 ? 34.986  40.617  -8.967  1.00 115.26 ? 225 ASN B CB   1 
ATOM   7780  C CG   . ASN B 1 225 ? 35.529  39.228  -9.281  1.00 120.57 ? 225 ASN B CG   1 
ATOM   7781  O OD1  . ASN B 1 225 ? 34.869  38.218  -9.019  1.00 118.87 ? 225 ASN B OD1  1 
ATOM   7782  N ND2  . ASN B 1 225 ? 36.732  39.172  -9.838  1.00 115.78 ? 225 ASN B ND2  1 
ATOM   7783  H H    . ASN B 1 225 ? 32.533  42.057  -8.024  1.00 131.79 ? 225 ASN B H    1 
ATOM   7784  H HA   . ASN B 1 225 ? 33.106  40.065  -8.363  1.00 134.31 ? 225 ASN B HA   1 
ATOM   7785  H HB2  . ASN B 1 225 ? 34.676  41.014  -9.797  1.00 138.31 ? 225 ASN B HB2  1 
ATOM   7786  H HB3  . ASN B 1 225 ? 35.709  41.146  -8.595  1.00 138.31 ? 225 ASN B HB3  1 
ATOM   7787  H HD21 . ASN B 1 225 ? 37.164  39.897  -10.003 1.00 138.94 ? 225 ASN B HD21 1 
ATOM   7788  H HD22 . ASN B 1 225 ? 37.081  38.410  -10.033 1.00 138.94 ? 225 ASN B HD22 1 
ATOM   7789  N N    . LEU B 1 226 ? 33.280  39.683  -5.791  1.00 104.90 ? 226 LEU B N    1 
ATOM   7790  C CA   . LEU B 1 226 ? 33.480  38.979  -4.526  1.00 101.21 ? 226 LEU B CA   1 
ATOM   7791  C C    . LEU B 1 226 ? 32.476  37.835  -4.462  1.00 97.20  ? 226 LEU B C    1 
ATOM   7792  O O    . LEU B 1 226 ? 31.272  38.066  -4.292  1.00 94.89  ? 226 LEU B O    1 
ATOM   7793  C CB   . LEU B 1 226 ? 33.319  39.925  -3.342  1.00 99.11  ? 226 LEU B CB   1 
ATOM   7794  C CG   . LEU B 1 226 ? 33.919  39.445  -2.020  1.00 99.13  ? 226 LEU B CG   1 
ATOM   7795  C CD1  . LEU B 1 226 ? 35.421  39.250  -2.126  1.00 98.66  ? 226 LEU B CD1  1 
ATOM   7796  C CD2  . LEU B 1 226 ? 33.576  40.432  -0.912  1.00 94.19  ? 226 LEU B CD2  1 
ATOM   7797  H H    . LEU B 1 226 ? 32.472  39.952  -5.906  1.00 125.88 ? 226 LEU B H    1 
ATOM   7798  H HA   . LEU B 1 226 ? 34.376  38.607  -4.496  1.00 121.45 ? 226 LEU B HA   1 
ATOM   7799  H HB2  . LEU B 1 226 ? 33.749  40.765  -3.565  1.00 118.94 ? 226 LEU B HB2  1 
ATOM   7800  H HB3  . LEU B 1 226 ? 32.371  40.066  -3.194  1.00 118.94 ? 226 LEU B HB3  1 
ATOM   7801  H HG   . LEU B 1 226 ? 33.538  38.581  -1.797  1.00 118.95 ? 226 LEU B HG   1 
ATOM   7802  H HD11 . LEU B 1 226 ? 35.790  39.146  -1.235  1.00 118.39 ? 226 LEU B HD11 1 
ATOM   7803  H HD12 . LEU B 1 226 ? 35.601  38.456  -2.653  1.00 118.39 ? 226 LEU B HD12 1 
ATOM   7804  H HD13 . LEU B 1 226 ? 35.810  40.028  -2.557  1.00 118.39 ? 226 LEU B HD13 1 
ATOM   7805  H HD21 . LEU B 1 226 ? 33.973  40.125  -0.082  1.00 113.03 ? 226 LEU B HD21 1 
ATOM   7806  H HD22 . LEU B 1 226 ? 33.931  41.304  -1.146  1.00 113.03 ? 226 LEU B HD22 1 
ATOM   7807  H HD23 . LEU B 1 226 ? 32.612  40.481  -0.820  1.00 113.03 ? 226 LEU B HD23 1 
ATOM   7808  N N    . ASP B 1 227 ? 32.971  36.601  -4.597  1.00 95.75  ? 227 ASP B N    1 
ATOM   7809  C CA   . ASP B 1 227 ? 32.087  35.447  -4.672  1.00 96.62  ? 227 ASP B CA   1 
ATOM   7810  C C    . ASP B 1 227 ? 31.669  34.927  -3.304  1.00 96.89  ? 227 ASP B C    1 
ATOM   7811  O O    . ASP B 1 227 ? 30.633  34.260  -3.200  1.00 95.62  ? 227 ASP B O    1 
ATOM   7812  C CB   . ASP B 1 227 ? 32.759  34.312  -5.453  1.00 108.37 ? 227 ASP B CB   1 
ATOM   7813  C CG   . ASP B 1 227 ? 34.239  34.169  -5.129  1.00 111.86 ? 227 ASP B CG   1 
ATOM   7814  O OD1  . ASP B 1 227 ? 34.904  35.209  -4.920  1.00 111.95 ? 227 ASP B OD1  1 
ATOM   7815  O OD2  . ASP B 1 227 ? 34.736  33.023  -5.090  1.00 106.49 ? 227 ASP B OD2  1 
ATOM   7816  H H    . ASP B 1 227 ? 33.808  36.412  -4.647  1.00 114.90 ? 227 ASP B H    1 
ATOM   7817  H HA   . ASP B 1 227 ? 31.286  35.713  -5.149  1.00 115.95 ? 227 ASP B HA   1 
ATOM   7818  H HB2  . ASP B 1 227 ? 32.322  33.475  -5.233  1.00 130.04 ? 227 ASP B HB2  1 
ATOM   7819  H HB3  . ASP B 1 227 ? 32.676  34.490  -6.403  1.00 130.04 ? 227 ASP B HB3  1 
ATOM   7820  N N    . ARG B 1 228 ? 32.446  35.203  -2.259  1.00 94.26  ? 228 ARG B N    1 
ATOM   7821  C CA   . ARG B 1 228 ? 32.100  34.726  -0.930  1.00 93.50  ? 228 ARG B CA   1 
ATOM   7822  C C    . ARG B 1 228 ? 32.811  35.569  0.116   1.00 91.63  ? 228 ARG B C    1 
ATOM   7823  O O    . ARG B 1 228 ? 33.951  35.993  -0.094  1.00 94.72  ? 228 ARG B O    1 
ATOM   7824  C CB   . ARG B 1 228 ? 32.468  33.246  -0.760  1.00 94.07  ? 228 ARG B CB   1 
ATOM   7825  C CG   . ARG B 1 228 ? 33.954  32.986  -0.611  1.00 94.60  ? 228 ARG B CG   1 
ATOM   7826  C CD   . ARG B 1 228 ? 34.246  31.495  -0.592  1.00 95.71  ? 228 ARG B CD   1 
ATOM   7827  N NE   . ARG B 1 228 ? 33.731  30.845  0.606   1.00 92.31  ? 228 ARG B NE   1 
ATOM   7828  C CZ   . ARG B 1 228 ? 33.935  29.570  0.908   1.00 94.64  ? 228 ARG B CZ   1 
ATOM   7829  N NH1  . ARG B 1 228 ? 34.644  28.780  0.120   1.00 94.05  ? 228 ARG B NH1  1 
ATOM   7830  N NH2  . ARG B 1 228 ? 33.416  29.077  2.028   1.00 96.41  ? 228 ARG B NH2  1 
ATOM   7831  H H    . ARG B 1 228 ? 33.173  35.662  -2.297  1.00 113.11 ? 228 ARG B H    1 
ATOM   7832  H HA   . ARG B 1 228 ? 31.145  34.827  -0.795  1.00 112.20 ? 228 ARG B HA   1 
ATOM   7833  H HB2  . ARG B 1 228 ? 32.029  32.908  0.037   1.00 112.89 ? 228 ARG B HB2  1 
ATOM   7834  H HB3  . ARG B 1 228 ? 32.161  32.759  -1.540  1.00 112.89 ? 228 ARG B HB3  1 
ATOM   7835  H HG2  . ARG B 1 228 ? 34.428  33.383  -1.359  1.00 113.52 ? 228 ARG B HG2  1 
ATOM   7836  H HG3  . ARG B 1 228 ? 34.268  33.371  0.222   1.00 113.52 ? 228 ARG B HG3  1 
ATOM   7837  H HD2  . ARG B 1 228 ? 33.829  31.080  -1.364  1.00 114.86 ? 228 ARG B HD2  1 
ATOM   7838  H HD3  . ARG B 1 228 ? 35.206  31.359  -0.621  1.00 114.86 ? 228 ARG B HD3  1 
ATOM   7839  H HE   . ARG B 1 228 ? 33.266  31.318  1.153   1.00 110.77 ? 228 ARG B HE   1 
ATOM   7840  H HH11 . ARG B 1 228 ? 34.985  29.090  -0.606  1.00 112.86 ? 228 ARG B HH11 1 
ATOM   7841  H HH12 . ARG B 1 228 ? 34.764  27.955  0.334   1.00 112.86 ? 228 ARG B HH12 1 
ATOM   7842  H HH21 . ARG B 1 228 ? 32.955  29.584  2.547   1.00 115.69 ? 228 ARG B HH21 1 
ATOM   7843  H HH22 . ARG B 1 228 ? 33.542  28.251  2.233   1.00 115.69 ? 228 ARG B HH22 1 
ATOM   7844  N N    . ALA B 1 229 ? 32.134  35.796  1.236   1.00 86.57  ? 229 ALA B N    1 
ATOM   7845  C CA   . ALA B 1 229 ? 32.693  36.600  2.310   1.00 87.75  ? 229 ALA B CA   1 
ATOM   7846  C C    . ALA B 1 229 ? 31.892  36.347  3.577   1.00 83.04  ? 229 ALA B C    1 
ATOM   7847  O O    . ALA B 1 229 ? 30.731  35.932  3.530   1.00 80.79  ? 229 ALA B O    1 
ATOM   7848  C CB   . ALA B 1 229 ? 32.687  38.090  1.953   1.00 87.43  ? 229 ALA B CB   1 
ATOM   7849  H H    . ALA B 1 229 ? 31.345  35.494  1.397   1.00 103.88 ? 229 ALA B H    1 
ATOM   7850  H HA   . ALA B 1 229 ? 33.610  36.328  2.472   1.00 105.30 ? 229 ALA B HA   1 
ATOM   7851  H HB1  . ALA B 1 229 ? 33.077  38.591  2.686   1.00 104.92 ? 229 ALA B HB1  1 
ATOM   7852  H HB2  . ALA B 1 229 ? 33.208  38.223  1.146   1.00 104.92 ? 229 ALA B HB2  1 
ATOM   7853  H HB3  . ALA B 1 229 ? 31.771  38.376  1.806   1.00 104.92 ? 229 ALA B HB3  1 
ATOM   7854  N N    . LYS B 1 230 ? 32.536  36.604  4.713   1.00 83.21  ? 230 LYS B N    1 
ATOM   7855  C CA   . LYS B 1 230 ? 31.918  36.468  6.030   1.00 80.33  ? 230 LYS B CA   1 
ATOM   7856  C C    . LYS B 1 230 ? 31.427  37.839  6.479   1.00 76.14  ? 230 LYS B C    1 
ATOM   7857  O O    . LYS B 1 230 ? 32.231  38.747  6.714   1.00 76.34  ? 230 LYS B O    1 
ATOM   7858  C CB   . LYS B 1 230 ? 32.909  35.879  7.030   1.00 77.51  ? 230 LYS B CB   1 
ATOM   7859  C CG   . LYS B 1 230 ? 32.639  34.425  7.352   1.00 80.28  ? 230 LYS B CG   1 
ATOM   7860  C CD   . LYS B 1 230 ? 33.858  33.749  7.962   1.00 88.21  ? 230 LYS B CD   1 
ATOM   7861  C CE   . LYS B 1 230 ? 33.689  32.231  7.962   1.00 89.44  ? 230 LYS B CE   1 
ATOM   7862  N NZ   . LYS B 1 230 ? 34.892  31.510  8.473   1.00 89.98  ? 230 LYS B NZ   1 
ATOM   7863  H H    . LYS B 1 230 ? 33.354  36.867  4.748   1.00 99.85  ? 230 LYS B H    1 
ATOM   7864  H HA   . LYS B 1 230 ? 31.153  35.874  5.972   1.00 96.40  ? 230 LYS B HA   1 
ATOM   7865  H HB2  . LYS B 1 230 ? 33.803  35.942  6.660   1.00 93.01  ? 230 LYS B HB2  1 
ATOM   7866  H HB3  . LYS B 1 230 ? 32.856  36.382  7.857   1.00 93.01  ? 230 LYS B HB3  1 
ATOM   7867  H HG2  . LYS B 1 230 ? 31.910  34.368  7.988   1.00 96.33  ? 230 LYS B HG2  1 
ATOM   7868  H HG3  . LYS B 1 230 ? 32.407  33.954  6.537   1.00 96.33  ? 230 LYS B HG3  1 
ATOM   7869  H HD2  . LYS B 1 230 ? 34.646  33.971  7.443   1.00 105.85 ? 230 LYS B HD2  1 
ATOM   7870  H HD3  . LYS B 1 230 ? 33.969  34.047  8.879   1.00 105.85 ? 230 LYS B HD3  1 
ATOM   7871  H HE2  . LYS B 1 230 ? 32.937  31.998  8.529   1.00 107.33 ? 230 LYS B HE2  1 
ATOM   7872  H HE3  . LYS B 1 230 ? 33.525  31.932  7.054   1.00 107.33 ? 230 LYS B HE3  1 
ATOM   7873  H HZ1  . LYS B 1 230 ? 34.750  30.632  8.457   1.00 107.98 ? 230 LYS B HZ1  1 
ATOM   7874  H HZ2  . LYS B 1 230 ? 35.598  31.698  7.964   1.00 107.98 ? 230 LYS B HZ2  1 
ATOM   7875  H HZ3  . LYS B 1 230 ? 35.065  31.761  9.309   1.00 107.98 ? 230 LYS B HZ3  1 
ATOM   7876  N N    . ILE B 1 231 ? 30.111  37.986  6.599   1.00 75.45  ? 231 ILE B N    1 
ATOM   7877  C CA   . ILE B 1 231 ? 29.479  39.281  6.819   1.00 78.05  ? 231 ILE B CA   1 
ATOM   7878  C C    . ILE B 1 231 ? 29.111  39.385  8.293   1.00 77.84  ? 231 ILE B C    1 
ATOM   7879  O O    . ILE B 1 231 ? 28.143  38.762  8.747   1.00 74.76  ? 231 ILE B O    1 
ATOM   7880  C CB   . ILE B 1 231 ? 28.242  39.469  5.930   1.00 78.94  ? 231 ILE B CB   1 
ATOM   7881  C CG1  . ILE B 1 231 ? 28.641  39.602  4.455   1.00 82.32  ? 231 ILE B CG1  1 
ATOM   7882  C CG2  . ILE B 1 231 ? 27.441  40.691  6.381   1.00 77.37  ? 231 ILE B CG2  1 
ATOM   7883  C CD1  . ILE B 1 231 ? 29.787  40.561  4.185   1.00 83.39  ? 231 ILE B CD1  1 
ATOM   7884  H H    . ILE B 1 231 ? 29.551  37.334  6.554   1.00 90.54  ? 231 ILE B H    1 
ATOM   7885  H HA   . ILE B 1 231 ? 30.119  39.980  6.613   1.00 93.66  ? 231 ILE B HA   1 
ATOM   7886  H HB   . ILE B 1 231 ? 27.685  38.680  6.021   1.00 94.73  ? 231 ILE B HB   1 
ATOM   7887  H HG12 . ILE B 1 231 ? 28.911  38.728  4.130   1.00 98.78  ? 231 ILE B HG12 1 
ATOM   7888  H HG13 . ILE B 1 231 ? 27.873  39.919  3.956   1.00 98.78  ? 231 ILE B HG13 1 
ATOM   7889  H HG21 . ILE B 1 231 ? 26.835  40.952  5.670   1.00 92.84  ? 231 ILE B HG21 1 
ATOM   7890  H HG22 . ILE B 1 231 ? 26.937  40.462  7.178   1.00 92.84  ? 231 ILE B HG22 1 
ATOM   7891  H HG23 . ILE B 1 231 ? 28.055  41.417  6.576   1.00 92.84  ? 231 ILE B HG23 1 
ATOM   7892  H HD11 . ILE B 1 231 ? 29.792  40.789  3.243   1.00 100.06 ? 231 ILE B HD11 1 
ATOM   7893  H HD12 . ILE B 1 231 ? 29.661  41.361  4.719   1.00 100.06 ? 231 ILE B HD12 1 
ATOM   7894  H HD13 . ILE B 1 231 ? 30.622  40.131  4.426   1.00 100.06 ? 231 ILE B HD13 1 
ATOM   7895  N N    . VAL B 1 232 ? 29.883  40.190  9.033   1.00 79.74  ? 232 VAL B N    1 
ATOM   7896  C CA   . VAL B 1 232 ? 29.599  40.416  10.444  1.00 77.84  ? 232 VAL B CA   1 
ATOM   7897  C C    . VAL B 1 232 ? 28.268  41.138  10.590  1.00 76.85  ? 232 VAL B C    1 
ATOM   7898  O O    . VAL B 1 232 ? 27.930  42.033  9.808   1.00 79.71  ? 232 VAL B O    1 
ATOM   7899  C CB   . VAL B 1 232 ? 30.745  41.216  11.085  1.00 80.62  ? 232 VAL B CB   1 
ATOM   7900  C CG1  . VAL B 1 232 ? 30.240  42.036  12.261  1.00 82.19  ? 232 VAL B CG1  1 
ATOM   7901  C CG2  . VAL B 1 232 ? 31.869  40.286  11.528  1.00 82.15  ? 232 VAL B CG2  1 
ATOM   7902  H H    . VAL B 1 232 ? 30.572  40.612  8.739   1.00 95.68  ? 232 VAL B H    1 
ATOM   7903  H HA   . VAL B 1 232 ? 29.530  39.562  10.900  1.00 93.41  ? 232 VAL B HA   1 
ATOM   7904  H HB   . VAL B 1 232 ? 31.101  41.829  10.422  1.00 96.74  ? 232 VAL B HB   1 
ATOM   7905  H HG11 . VAL B 1 232 ? 31.000  42.351  12.776  1.00 98.62  ? 232 VAL B HG11 1 
ATOM   7906  H HG12 . VAL B 1 232 ? 29.733  42.791  11.925  1.00 98.62  ? 232 VAL B HG12 1 
ATOM   7907  H HG13 . VAL B 1 232 ? 29.674  41.477  12.816  1.00 98.62  ? 232 VAL B HG13 1 
ATOM   7908  H HG21 . VAL B 1 232 ? 32.583  40.815  11.916  1.00 98.59  ? 232 VAL B HG21 1 
ATOM   7909  H HG22 . VAL B 1 232 ? 31.522  39.664  12.187  1.00 98.59  ? 232 VAL B HG22 1 
ATOM   7910  H HG23 . VAL B 1 232 ? 32.199  39.800  10.757  1.00 98.59  ? 232 VAL B HG23 1 
ATOM   7911  N N    . GLN B 1 233 ? 27.504  40.755  11.607  1.00 78.08  ? 233 GLN B N    1 
ATOM   7912  C CA   . GLN B 1 233 ? 26.188  41.339  11.853  1.00 79.43  ? 233 GLN B CA   1 
ATOM   7913  C C    . GLN B 1 233 ? 26.044  41.620  13.344  1.00 78.64  ? 233 GLN B C    1 
ATOM   7914  O O    . GLN B 1 233 ? 26.929  41.250  14.125  1.00 78.66  ? 233 GLN B O    1 
ATOM   7915  C CB   . GLN B 1 233 ? 25.107  40.404  11.320  1.00 77.54  ? 233 GLN B CB   1 
ATOM   7916  C CG   . GLN B 1 233 ? 25.407  39.960  9.889   1.00 81.39  ? 233 GLN B CG   1 
ATOM   7917  C CD   . GLN B 1 233 ? 24.178  39.559  9.105   1.00 76.65  ? 233 GLN B CD   1 
ATOM   7918  O OE1  . GLN B 1 233 ? 23.088  40.093  9.303   1.00 78.59  ? 233 GLN B OE1  1 
ATOM   7919  N NE2  . GLN B 1 233 ? 24.354  38.612  8.196   1.00 71.62  ? 233 GLN B NE2  1 
ATOM   7920  H H    . GLN B 1 233 ? 27.727  40.150  12.176  1.00 93.69  ? 233 GLN B H    1 
ATOM   7921  H HA   . GLN B 1 233 ? 26.081  42.186  11.393  1.00 95.32  ? 233 GLN B HA   1 
ATOM   7922  H HB2  . GLN B 1 233 ? 25.061  39.615  11.882  1.00 93.05  ? 233 GLN B HB2  1 
ATOM   7923  H HB3  . GLN B 1 233 ? 24.253  40.865  11.325  1.00 93.05  ? 233 GLN B HB3  1 
ATOM   7924  H HG2  . GLN B 1 233 ? 25.831  40.694  9.418   1.00 97.68  ? 233 GLN B HG2  1 
ATOM   7925  H HG3  . GLN B 1 233 ? 26.002  39.195  9.918   1.00 97.68  ? 233 GLN B HG3  1 
ATOM   7926  H HE21 . GLN B 1 233 ? 25.132  38.266  8.082   1.00 85.94  ? 233 GLN B HE21 1 
ATOM   7927  H HE22 . GLN B 1 233 ? 23.689  38.344  7.720   1.00 85.94  ? 233 GLN B HE22 1 
ATOM   7928  N N    . PRO B 1 234 ? 24.970  42.289  13.777  1.00 79.53  ? 234 PRO B N    1 
ATOM   7929  C CA   . PRO B 1 234 ? 24.925  42.749  15.179  1.00 82.46  ? 234 PRO B CA   1 
ATOM   7930  C C    . PRO B 1 234 ? 25.208  41.665  16.209  1.00 81.52  ? 234 PRO B C    1 
ATOM   7931  O O    . PRO B 1 234 ? 26.064  41.857  17.083  1.00 83.53  ? 234 PRO B O    1 
ATOM   7932  C CB   . PRO B 1 234 ? 23.499  43.311  15.312  1.00 82.49  ? 234 PRO B CB   1 
ATOM   7933  C CG   . PRO B 1 234 ? 23.130  43.731  13.916  1.00 83.59  ? 234 PRO B CG   1 
ATOM   7934  C CD   . PRO B 1 234 ? 23.778  42.711  13.011  1.00 78.28  ? 234 PRO B CD   1 
ATOM   7935  H HA   . PRO B 1 234 ? 25.572  43.463  15.292  1.00 98.95  ? 234 PRO B HA   1 
ATOM   7936  H HB2  . PRO B 1 234 ? 22.900  42.623  15.639  1.00 98.99  ? 234 PRO B HB2  1 
ATOM   7937  H HB3  . PRO B 1 234 ? 23.496  44.069  15.917  1.00 98.99  ? 234 PRO B HB3  1 
ATOM   7938  H HG2  . PRO B 1 234 ? 22.166  43.722  13.813  1.00 100.31 ? 234 PRO B HG2  1 
ATOM   7939  H HG3  . PRO B 1 234 ? 23.475  44.620  13.737  1.00 100.31 ? 234 PRO B HG3  1 
ATOM   7940  H HD2  . PRO B 1 234 ? 23.183  41.961  12.856  1.00 93.94  ? 234 PRO B HD2  1 
ATOM   7941  H HD3  . PRO B 1 234 ? 24.034  43.112  12.166  1.00 93.94  ? 234 PRO B HD3  1 
ATOM   7942  N N    . ASN B 1 235 ? 24.513  40.528  16.136  1.00 80.66  ? 235 ASN B N    1 
ATOM   7943  C CA   . ASN B 1 235 ? 24.640  39.480  17.145  1.00 82.52  ? 235 ASN B CA   1 
ATOM   7944  C C    . ASN B 1 235 ? 24.935  38.127  16.504  1.00 79.93  ? 235 ASN B C    1 
ATOM   7945  O O    . ASN B 1 235 ? 24.493  37.084  17.000  1.00 79.28  ? 235 ASN B O    1 
ATOM   7946  C CB   . ASN B 1 235 ? 23.375  39.397  18.003  1.00 83.85  ? 235 ASN B CB   1 
ATOM   7947  C CG   . ASN B 1 235 ? 23.633  39.729  19.462  1.00 88.44  ? 235 ASN B CG   1 
ATOM   7948  O OD1  . ASN B 1 235 ? 24.617  39.271  20.054  1.00 85.79  ? 235 ASN B OD1  1 
ATOM   7949  N ND2  . ASN B 1 235 ? 22.745  40.520  20.055  1.00 89.59  ? 235 ASN B ND2  1 
ATOM   7950  H H    . ASN B 1 235 ? 23.959  40.341  15.506  1.00 96.80  ? 235 ASN B H    1 
ATOM   7951  H HA   . ASN B 1 235 ? 25.385  39.700  17.724  1.00 99.02  ? 235 ASN B HA   1 
ATOM   7952  H HB2  . ASN B 1 235 ? 22.720  40.027  17.664  1.00 100.62 ? 235 ASN B HB2  1 
ATOM   7953  H HB3  . ASN B 1 235 ? 23.021  38.495  17.958  1.00 100.62 ? 235 ASN B HB3  1 
ATOM   7954  H HD21 . ASN B 1 235 ? 22.069  40.814  19.613  1.00 107.51 ? 235 ASN B HD21 1 
ATOM   7955  H HD22 . ASN B 1 235 ? 22.846  40.737  20.881  1.00 107.51 ? 235 ASN B HD22 1 
ATOM   7956  N N    . GLY B 1 236 ? 25.685  38.126  15.411  1.00 80.53  ? 236 GLY B N    1 
ATOM   7957  C CA   . GLY B 1 236 ? 26.036  36.884  14.757  1.00 76.07  ? 236 GLY B CA   1 
ATOM   7958  C C    . GLY B 1 236 ? 26.882  37.168  13.539  1.00 77.81  ? 236 GLY B C    1 
ATOM   7959  O O    . GLY B 1 236 ? 27.396  38.275  13.362  1.00 79.26  ? 236 GLY B O    1 
ATOM   7960  H H    . GLY B 1 236 ? 26.000  38.830  15.032  1.00 96.64  ? 236 GLY B H    1 
ATOM   7961  H HA2  . GLY B 1 236 ? 26.538  36.320  15.366  1.00 91.29  ? 236 GLY B HA2  1 
ATOM   7962  H HA3  . GLY B 1 236 ? 25.233  36.416  14.482  1.00 91.29  ? 236 GLY B HA3  1 
ATOM   7963  N N    . TRP B 1 237 ? 27.017  36.153  12.690  1.00 78.54  ? 237 TRP B N    1 
ATOM   7964  C CA   . TRP B 1 237 ? 27.716  36.323  11.425  1.00 75.53  ? 237 TRP B CA   1 
ATOM   7965  C C    . TRP B 1 237 ? 27.270  35.231  10.466  1.00 75.70  ? 237 TRP B C    1 
ATOM   7966  O O    . TRP B 1 237 ? 26.981  34.102  10.877  1.00 75.82  ? 237 TRP B O    1 
ATOM   7967  C CB   . TRP B 1 237 ? 29.238  36.293  11.612  1.00 75.97  ? 237 TRP B CB   1 
ATOM   7968  C CG   . TRP B 1 237 ? 29.775  34.970  12.058  1.00 75.72  ? 237 TRP B CG   1 
ATOM   7969  C CD1  . TRP B 1 237 ? 30.047  34.586  13.332  1.00 75.10  ? 237 TRP B CD1  1 
ATOM   7970  C CD2  . TRP B 1 237 ? 30.112  33.855  11.222  1.00 78.01  ? 237 TRP B CD2  1 
ATOM   7971  N NE1  . TRP B 1 237 ? 30.528  33.299  13.347  1.00 74.30  ? 237 TRP B NE1  1 
ATOM   7972  C CE2  . TRP B 1 237 ? 30.578  32.828  12.065  1.00 75.01  ? 237 TRP B CE2  1 
ATOM   7973  C CE3  . TRP B 1 237 ? 30.061  33.626  9.844   1.00 74.86  ? 237 TRP B CE3  1 
ATOM   7974  C CZ2  . TRP B 1 237 ? 30.993  31.591  11.577  1.00 75.28  ? 237 TRP B CZ2  1 
ATOM   7975  C CZ3  . TRP B 1 237 ? 30.468  32.398  9.362   1.00 75.92  ? 237 TRP B CZ3  1 
ATOM   7976  C CH2  . TRP B 1 237 ? 30.930  31.396  10.226  1.00 76.46  ? 237 TRP B CH2  1 
ATOM   7977  H H    . TRP B 1 237 ? 26.713  35.360  12.825  1.00 94.24  ? 237 TRP B H    1 
ATOM   7978  H HA   . TRP B 1 237 ? 27.478  37.179  11.037  1.00 90.64  ? 237 TRP B HA   1 
ATOM   7979  H HB2  . TRP B 1 237 ? 29.659  36.511  10.765  1.00 91.16  ? 237 TRP B HB2  1 
ATOM   7980  H HB3  . TRP B 1 237 ? 29.481  36.950  12.282  1.00 91.16  ? 237 TRP B HB3  1 
ATOM   7981  H HD1  . TRP B 1 237 ? 29.924  35.117  14.085  1.00 90.12  ? 237 TRP B HD1  1 
ATOM   7982  H HE1  . TRP B 1 237 ? 30.761  32.860  14.050  1.00 89.16  ? 237 TRP B HE1  1 
ATOM   7983  H HE3  . TRP B 1 237 ? 29.760  34.288  9.263   1.00 89.83  ? 237 TRP B HE3  1 
ATOM   7984  H HZ2  . TRP B 1 237 ? 31.300  30.925  12.148  1.00 90.34  ? 237 TRP B HZ2  1 
ATOM   7985  H HZ3  . TRP B 1 237 ? 30.436  32.233  8.448   1.00 91.10  ? 237 TRP B HZ3  1 
ATOM   7986  H HH2  . TRP B 1 237 ? 31.199  30.579  9.871   1.00 91.76  ? 237 TRP B HH2  1 
ATOM   7987  N N    . LEU B 1 238 ? 27.216  35.588  9.182   1.00 75.91  ? 238 LEU B N    1 
ATOM   7988  C CA   . LEU B 1 238 ? 26.821  34.666  8.130   1.00 73.05  ? 238 LEU B CA   1 
ATOM   7989  C C    . LEU B 1 238 ? 27.776  34.816  6.955   1.00 77.57  ? 238 LEU B C    1 
ATOM   7990  O O    . LEU B 1 238 ? 28.173  35.931  6.603   1.00 77.71  ? 238 LEU B O    1 
ATOM   7991  C CB   . LEU B 1 238 ? 25.382  34.921  7.670   1.00 72.39  ? 238 LEU B CB   1 
ATOM   7992  C CG   . LEU B 1 238 ? 24.297  34.826  8.741   1.00 72.32  ? 238 LEU B CG   1 
ATOM   7993  C CD1  . LEU B 1 238 ? 22.987  35.416  8.237   1.00 72.22  ? 238 LEU B CD1  1 
ATOM   7994  C CD2  . LEU B 1 238 ? 24.103  33.381  9.190   1.00 70.97  ? 238 LEU B CD2  1 
ATOM   7995  H H    . LEU B 1 238 ? 27.408  36.375  8.895   1.00 91.09  ? 238 LEU B H    1 
ATOM   7996  H HA   . LEU B 1 238 ? 26.876  33.754  8.456   1.00 87.65  ? 238 LEU B HA   1 
ATOM   7997  H HB2  . LEU B 1 238 ? 25.339  35.816  7.300   1.00 86.87  ? 238 LEU B HB2  1 
ATOM   7998  H HB3  . LEU B 1 238 ? 25.165  34.268  6.986   1.00 86.87  ? 238 LEU B HB3  1 
ATOM   7999  H HG   . LEU B 1 238 ? 24.577  35.342  9.513   1.00 86.78  ? 238 LEU B HG   1 
ATOM   8000  H HD11 . LEU B 1 238 ? 22.342  35.417  8.961   1.00 86.67  ? 238 LEU B HD11 1 
ATOM   8001  H HD12 . LEU B 1 238 ? 23.146  36.323  7.933   1.00 86.67  ? 238 LEU B HD12 1 
ATOM   8002  H HD13 . LEU B 1 238 ? 22.659  34.874  7.502   1.00 86.67  ? 238 LEU B HD13 1 
ATOM   8003  H HD21 . LEU B 1 238 ? 23.351  33.338  9.801   1.00 85.16  ? 238 LEU B HD21 1 
ATOM   8004  H HD22 . LEU B 1 238 ? 23.928  32.829  8.412   1.00 85.16  ? 238 LEU B HD22 1 
ATOM   8005  H HD23 . LEU B 1 238 ? 24.910  33.078  9.636   1.00 85.16  ? 238 LEU B HD23 1 
ATOM   8006  N N    . GLU B 1 239 ? 28.142  33.687  6.356   1.00 78.50  ? 239 GLU B N    1 
ATOM   8007  C CA   . GLU B 1 239 ? 28.989  33.663  5.171   1.00 81.01  ? 239 GLU B CA   1 
ATOM   8008  C C    . GLU B 1 239 ? 28.117  33.388  3.952   1.00 80.18  ? 239 GLU B C    1 
ATOM   8009  O O    . GLU B 1 239 ? 27.405  32.380  3.912   1.00 78.88  ? 239 GLU B O    1 
ATOM   8010  C CB   . GLU B 1 239 ? 30.080  32.601  5.301   1.00 81.07  ? 239 GLU B CB   1 
ATOM   8011  C CG   . GLU B 1 239 ? 31.075  32.594  4.149   1.00 85.47  ? 239 GLU B CG   1 
ATOM   8012  C CD   . GLU B 1 239 ? 32.033  31.419  4.214   1.00 88.09  ? 239 GLU B CD   1 
ATOM   8013  O OE1  . GLU B 1 239 ? 31.632  30.350  4.720   1.00 83.63  ? 239 GLU B OE1  1 
ATOM   8014  O OE2  . GLU B 1 239 ? 33.186  31.562  3.757   1.00 93.22  ? 239 GLU B OE2  1 
ATOM   8015  H H    . GLU B 1 239 ? 27.906  32.905  6.624   1.00 94.20  ? 239 GLU B H    1 
ATOM   8016  H HA   . GLU B 1 239 ? 29.417  34.526  5.060   1.00 97.22  ? 239 GLU B HA   1 
ATOM   8017  H HB2  . GLU B 1 239 ? 30.576  32.763  6.119   1.00 97.28  ? 239 GLU B HB2  1 
ATOM   8018  H HB3  . GLU B 1 239 ? 29.662  31.726  5.335   1.00 97.28  ? 239 GLU B HB3  1 
ATOM   8019  H HG2  . GLU B 1 239 ? 30.589  32.540  3.311   1.00 102.56 ? 239 GLU B HG2  1 
ATOM   8020  H HG3  . GLU B 1 239 ? 31.598  33.411  4.177   1.00 102.56 ? 239 GLU B HG3  1 
ATOM   8021  N N    . TYR B 1 240 ? 28.161  34.287  2.971   1.00 81.34  ? 240 TYR B N    1 
ATOM   8022  C CA   . TYR B 1 240 ? 27.486  34.065  1.699   1.00 84.10  ? 240 TYR B CA   1 
ATOM   8023  C C    . TYR B 1 240 ? 28.452  33.380  0.742   1.00 88.94  ? 240 TYR B C    1 
ATOM   8024  O O    . TYR B 1 240 ? 29.639  33.716  0.692   1.00 88.70  ? 240 TYR B O    1 
ATOM   8025  C CB   . TYR B 1 240 ? 26.961  35.375  1.101   1.00 84.14  ? 240 TYR B CB   1 
ATOM   8026  C CG   . TYR B 1 240 ? 27.954  36.206  0.313   1.00 84.66  ? 240 TYR B CG   1 
ATOM   8027  C CD1  . TYR B 1 240 ? 28.246  35.912  -1.015  1.00 89.29  ? 240 TYR B CD1  1 
ATOM   8028  C CD2  . TYR B 1 240 ? 28.574  37.306  0.888   1.00 85.20  ? 240 TYR B CD2  1 
ATOM   8029  C CE1  . TYR B 1 240 ? 29.146  36.676  -1.734  1.00 90.08  ? 240 TYR B CE1  1 
ATOM   8030  C CE2  . TYR B 1 240 ? 29.473  38.076  0.176   1.00 86.59  ? 240 TYR B CE2  1 
ATOM   8031  C CZ   . TYR B 1 240 ? 29.754  37.760  -1.134  1.00 91.41  ? 240 TYR B CZ   1 
ATOM   8032  O OH   . TYR B 1 240 ? 30.647  38.528  -1.848  1.00 92.65  ? 240 TYR B OH   1 
ATOM   8033  H H    . TYR B 1 240 ? 28.578  35.037  3.020   1.00 97.61  ? 240 TYR B H    1 
ATOM   8034  H HA   . TYR B 1 240 ? 26.713  33.493  1.829   1.00 100.92 ? 240 TYR B HA   1 
ATOM   8035  H HB2  . TYR B 1 240 ? 26.230  35.161  0.500   1.00 100.96 ? 240 TYR B HB2  1 
ATOM   8036  H HB3  . TYR B 1 240 ? 26.640  35.931  1.829   1.00 100.96 ? 240 TYR B HB3  1 
ATOM   8037  H HD1  . TYR B 1 240 ? 27.829  35.190  -1.426  1.00 107.15 ? 240 TYR B HD1  1 
ATOM   8038  H HD2  . TYR B 1 240 ? 28.381  37.528  1.770   1.00 102.24 ? 240 TYR B HD2  1 
ATOM   8039  H HE1  . TYR B 1 240 ? 29.340  36.461  -2.618  1.00 108.10 ? 240 TYR B HE1  1 
ATOM   8040  H HE2  . TYR B 1 240 ? 29.886  38.805  0.580   1.00 103.91 ? 240 TYR B HE2  1 
ATOM   8041  H HH   . TYR B 1 240 ? 30.701  38.247  -2.637  1.00 111.18 ? 240 TYR B HH   1 
ATOM   8042  N N    . ILE B 1 241 ? 27.938  32.406  -0.003  1.00 97.62  ? 241 ILE B N    1 
ATOM   8043  C CA   . ILE B 1 241 ? 28.727  31.628  -0.947  1.00 99.14  ? 241 ILE B CA   1 
ATOM   8044  C C    . ILE B 1 241 ? 28.016  31.648  -2.293  1.00 104.02 ? 241 ILE B C    1 
ATOM   8045  O O    . ILE B 1 241 ? 26.831  31.308  -2.379  1.00 105.25 ? 241 ILE B O    1 
ATOM   8046  C CB   . ILE B 1 241 ? 28.940  30.179  -0.461  1.00 99.34  ? 241 ILE B CB   1 
ATOM   8047  C CG1  . ILE B 1 241 ? 30.153  30.121  0.472   1.00 101.46 ? 241 ILE B CG1  1 
ATOM   8048  C CG2  . ILE B 1 241 ? 29.082  29.238  -1.648  1.00 105.85 ? 241 ILE B CG2  1 
ATOM   8049  C CD1  . ILE B 1 241 ? 30.620  28.717  0.820   1.00 110.77 ? 241 ILE B CD1  1 
ATOM   8050  H H    . ILE B 1 241 ? 27.111  32.171  0.024   1.00 117.15 ? 241 ILE B H    1 
ATOM   8051  H HA   . ILE B 1 241 ? 29.598  32.041  -1.057  1.00 118.97 ? 241 ILE B HA   1 
ATOM   8052  H HB   . ILE B 1 241 ? 28.164  29.888  0.044   1.00 119.21 ? 241 ILE B HB   1 
ATOM   8053  H HG12 . ILE B 1 241 ? 30.894  30.577  0.044   1.00 121.75 ? 241 ILE B HG12 1 
ATOM   8054  H HG13 . ILE B 1 241 ? 29.924  30.566  1.303   1.00 121.75 ? 241 ILE B HG13 1 
ATOM   8055  H HG21 . ILE B 1 241 ? 29.389  28.374  -1.331  1.00 127.02 ? 241 ILE B HG21 1 
ATOM   8056  H HG22 . ILE B 1 241 ? 28.219  29.143  -2.081  1.00 127.02 ? 241 ILE B HG22 1 
ATOM   8057  H HG23 . ILE B 1 241 ? 29.726  29.610  -2.271  1.00 127.02 ? 241 ILE B HG23 1 
ATOM   8058  H HD11 . ILE B 1 241 ? 31.008  28.724  1.708   1.00 132.93 ? 241 ILE B HD11 1 
ATOM   8059  H HD12 . ILE B 1 241 ? 29.858  28.116  0.796   1.00 132.93 ? 241 ILE B HD12 1 
ATOM   8060  H HD13 . ILE B 1 241 ? 31.283  28.435  0.171   1.00 132.93 ? 241 ILE B HD13 1 
ATOM   8061  N N    . ILE B 1 242 ? 28.739  32.036  -3.339  1.00 97.73  ? 242 ILE B N    1 
ATOM   8062  C CA   . ILE B 1 242 ? 28.243  31.998  -4.711  1.00 99.97  ? 242 ILE B CA   1 
ATOM   8063  C C    . ILE B 1 242 ? 29.072  30.967  -5.463  1.00 100.06 ? 242 ILE B C    1 
ATOM   8064  O O    . ILE B 1 242 ? 30.297  31.104  -5.576  1.00 97.81  ? 242 ILE B O    1 
ATOM   8065  C CB   . ILE B 1 242 ? 28.310  33.378  -5.383  1.00 99.79  ? 242 ILE B CB   1 
ATOM   8066  C CG1  . ILE B 1 242 ? 27.693  34.435  -4.462  1.00 94.07  ? 242 ILE B CG1  1 
ATOM   8067  C CG2  . ILE B 1 242 ? 27.604  33.338  -6.732  1.00 93.83  ? 242 ILE B CG2  1 
ATOM   8068  C CD1  . ILE B 1 242 ? 27.210  35.681  -5.175  1.00 91.06  ? 242 ILE B CD1  1 
ATOM   8069  H H    . ILE B 1 242 ? 29.544  32.335  -3.277  1.00 117.27 ? 242 ILE B H    1 
ATOM   8070  H HA   . ILE B 1 242 ? 27.315  31.713  -4.717  1.00 119.96 ? 242 ILE B HA   1 
ATOM   8071  H HB   . ILE B 1 242 ? 29.238  33.614  -5.537  1.00 119.75 ? 242 ILE B HB   1 
ATOM   8072  H HG12 . ILE B 1 242 ? 26.931  34.043  -4.008  1.00 112.88 ? 242 ILE B HG12 1 
ATOM   8073  H HG13 . ILE B 1 242 ? 28.361  34.708  -3.813  1.00 112.88 ? 242 ILE B HG13 1 
ATOM   8074  H HG21 . ILE B 1 242 ? 27.852  34.125  -7.242  1.00 112.60 ? 242 ILE B HG21 1 
ATOM   8075  H HG22 . ILE B 1 242 ? 27.875  32.537  -7.207  1.00 112.60 ? 242 ILE B HG22 1 
ATOM   8076  H HG23 . ILE B 1 242 ? 26.645  33.328  -6.587  1.00 112.60 ? 242 ILE B HG23 1 
ATOM   8077  H HD11 . ILE B 1 242 ? 27.058  36.381  -4.520  1.00 109.27 ? 242 ILE B HD11 1 
ATOM   8078  H HD12 . ILE B 1 242 ? 27.886  35.964  -5.810  1.00 109.27 ? 242 ILE B HD12 1 
ATOM   8079  H HD13 . ILE B 1 242 ? 26.383  35.478  -5.640  1.00 109.27 ? 242 ILE B HD13 1 
ATOM   8080  N N    . GLU B 1 243 ? 28.407  29.936  -5.972  1.00 101.67 ? 243 GLU B N    1 
ATOM   8081  C CA   . GLU B 1 243 ? 29.097  28.791  -6.562  1.00 109.79 ? 243 GLU B CA   1 
ATOM   8082  C C    . GLU B 1 243 ? 28.264  28.293  -7.734  1.00 113.43 ? 243 GLU B C    1 
ATOM   8083  O O    . GLU B 1 243 ? 27.168  27.762  -7.532  1.00 113.58 ? 243 GLU B O    1 
ATOM   8084  C CB   . GLU B 1 243 ? 29.303  27.693  -5.521  1.00 115.32 ? 243 GLU B CB   1 
ATOM   8085  C CG   . GLU B 1 243 ? 30.041  26.464  -6.016  1.00 115.56 ? 243 GLU B CG   1 
ATOM   8086  C CD   . GLU B 1 243 ? 29.867  25.275  -5.083  1.00 124.54 ? 243 GLU B CD   1 
ATOM   8087  O OE1  . GLU B 1 243 ? 29.498  25.484  -3.903  1.00 121.20 ? 243 GLU B OE1  1 
ATOM   8088  O OE2  . GLU B 1 243 ? 30.096  24.130  -5.528  1.00 126.25 ? 243 GLU B OE2  1 
ATOM   8089  H H    . GLU B 1 243 ? 27.549  29.873  -5.989  1.00 122.00 ? 243 GLU B H    1 
ATOM   8090  H HA   . GLU B 1 243 ? 29.963  29.066  -6.901  1.00 131.75 ? 243 GLU B HA   1 
ATOM   8091  H HB2  . GLU B 1 243 ? 29.816  28.062  -4.785  1.00 138.38 ? 243 GLU B HB2  1 
ATOM   8092  H HB3  . GLU B 1 243 ? 28.433  27.402  -5.206  1.00 138.38 ? 243 GLU B HB3  1 
ATOM   8093  H HG2  . GLU B 1 243 ? 29.697  26.216  -6.889  1.00 138.67 ? 243 GLU B HG2  1 
ATOM   8094  H HG3  . GLU B 1 243 ? 30.988  26.664  -6.078  1.00 138.67 ? 243 GLU B HG3  1 
ATOM   8095  N N    . ASN B 1 244 ? 28.784  28.462  -8.949  1.00 109.42 ? 244 ASN B N    1 
ATOM   8096  C CA   . ASN B 1 244 ? 28.067  28.079  -10.164 1.00 111.83 ? 244 ASN B CA   1 
ATOM   8097  C C    . ASN B 1 244 ? 26.731  28.816  -10.251 1.00 110.48 ? 244 ASN B C    1 
ATOM   8098  O O    . ASN B 1 244 ? 25.672  28.216  -10.451 1.00 112.23 ? 244 ASN B O    1 
ATOM   8099  C CB   . ASN B 1 244 ? 27.866  26.564  -10.225 1.00 113.56 ? 244 ASN B CB   1 
ATOM   8100  C CG   . ASN B 1 244 ? 29.165  25.809  -10.455 1.00 117.04 ? 244 ASN B CG   1 
ATOM   8101  O OD1  . ASN B 1 244 ? 29.416  24.781  -9.824  1.00 114.47 ? 244 ASN B OD1  1 
ATOM   8102  N ND2  . ASN B 1 244 ? 29.996  26.314  -11.364 1.00 117.61 ? 244 ASN B ND2  1 
ATOM   8103  H H    . ASN B 1 244 ? 29.560  28.801  -9.098  1.00 131.30 ? 244 ASN B H    1 
ATOM   8104  H HA   . ASN B 1 244 ? 28.598  28.337  -10.934 1.00 134.20 ? 244 ASN B HA   1 
ATOM   8105  H HB2  . ASN B 1 244 ? 27.487  26.261  -9.385  1.00 136.27 ? 244 ASN B HB2  1 
ATOM   8106  H HB3  . ASN B 1 244 ? 27.263  26.354  -10.955 1.00 136.27 ? 244 ASN B HB3  1 
ATOM   8107  H HD21 . ASN B 1 244 ? 29.786  27.032  -11.787 1.00 141.13 ? 244 ASN B HD21 1 
ATOM   8108  H HD22 . ASN B 1 244 ? 30.744  25.921  -11.529 1.00 141.13 ? 244 ASN B HD22 1 
ATOM   8109  N N    . ASP B 1 245 ? 26.789  30.137  -10.099 1.00 108.59 ? 245 ASP B N    1 
ATOM   8110  C CA   . ASP B 1 245 ? 25.592  30.970  -10.112 1.00 110.18 ? 245 ASP B CA   1 
ATOM   8111  C C    . ASP B 1 245 ? 24.534  30.424  -9.152  1.00 107.10 ? 245 ASP B C    1 
ATOM   8112  O O    . ASP B 1 245 ? 23.334  30.473  -9.420  1.00 106.72 ? 245 ASP B O    1 
ATOM   8113  C CB   . ASP B 1 245 ? 25.029  31.092  -11.532 1.00 113.13 ? 245 ASP B CB   1 
ATOM   8114  C CG   . ASP B 1 245 ? 26.015  31.719  -12.511 1.00 122.49 ? 245 ASP B CG   1 
ATOM   8115  O OD1  . ASP B 1 245 ? 26.956  32.404  -12.059 1.00 128.65 ? 245 ASP B OD1  1 
ATOM   8116  O OD2  . ASP B 1 245 ? 25.849  31.525  -13.736 1.00 126.29 ? 245 ASP B OD2  1 
ATOM   8117  H H    . ASP B 1 245 ? 27.519  30.578  -9.986  1.00 130.31 ? 245 ASP B H    1 
ATOM   8118  H HA   . ASP B 1 245 ? 25.832  31.859  -9.808  1.00 132.22 ? 245 ASP B HA   1 
ATOM   8119  H HB2  . ASP B 1 245 ? 24.805  30.206  -11.860 1.00 135.75 ? 245 ASP B HB2  1 
ATOM   8120  H HB3  . ASP B 1 245 ? 24.235  31.648  -11.511 1.00 135.75 ? 245 ASP B HB3  1 
ATOM   8121  N N    . GLU B 1 246 ? 24.983  29.886  -8.020  1.00 104.18 ? 246 GLU B N    1 
ATOM   8122  C CA   . GLU B 1 246 ? 24.086  29.427  -6.965  1.00 102.88 ? 246 GLU B CA   1 
ATOM   8123  C C    . GLU B 1 246 ? 24.509  30.046  -5.641  1.00 94.27  ? 246 GLU B C    1 
ATOM   8124  O O    . GLU B 1 246 ? 25.702  30.122  -5.329  1.00 94.76  ? 246 GLU B O    1 
ATOM   8125  C CB   . GLU B 1 246 ? 24.065  27.894  -6.862  1.00 100.76 ? 246 GLU B CB   1 
ATOM   8126  C CG   . GLU B 1 246 ? 23.239  27.211  -7.962  1.00 103.32 ? 246 GLU B CG   1 
ATOM   8127  C CD   . GLU B 1 246 ? 21.747  27.154  -7.652  1.00 103.60 ? 246 GLU B CD   1 
ATOM   8128  O OE1  . GLU B 1 246 ? 21.301  27.852  -6.713  1.00 103.22 ? 246 GLU B OE1  1 
ATOM   8129  O OE2  . GLU B 1 246 ? 21.020  26.415  -8.347  1.00 100.82 ? 246 GLU B OE2  1 
ATOM   8130  H H    . GLU B 1 246 ? 25.816  29.775  -7.839  1.00 125.02 ? 246 GLU B H    1 
ATOM   8131  H HA   . GLU B 1 246 ? 23.181  29.717  -7.158  1.00 123.46 ? 246 GLU B HA   1 
ATOM   8132  H HB2  . GLU B 1 246 ? 24.976  27.565  -6.928  1.00 120.91 ? 246 GLU B HB2  1 
ATOM   8133  H HB3  . GLU B 1 246 ? 23.684  27.644  -6.006  1.00 120.91 ? 246 GLU B HB3  1 
ATOM   8134  H HG2  . GLU B 1 246 ? 23.352  27.703  -8.790  1.00 123.98 ? 246 GLU B HG2  1 
ATOM   8135  H HG3  . GLU B 1 246 ? 23.554  26.300  -8.071  1.00 123.98 ? 246 GLU B HG3  1 
ATOM   8136  N N    . MET B 1 247 ? 23.520  30.495  -4.871  1.00 91.80  ? 247 MET B N    1 
ATOM   8137  C CA   . MET B 1 247 ? 23.743  31.273  -3.658  1.00 91.99  ? 247 MET B CA   1 
ATOM   8138  C C    . MET B 1 247 ? 23.472  30.403  -2.440  1.00 89.72  ? 247 MET B C    1 
ATOM   8139  O O    . MET B 1 247 ? 22.364  29.879  -2.280  1.00 88.06  ? 247 MET B O    1 
ATOM   8140  C CB   . MET B 1 247 ? 22.844  32.513  -3.642  1.00 89.19  ? 247 MET B CB   1 
ATOM   8141  C CG   . MET B 1 247 ? 22.946  33.380  -2.383  1.00 84.48  ? 247 MET B CG   1 
ATOM   8142  S SD   . MET B 1 247 ? 24.631  33.704  -1.837  1.00 84.28  ? 247 MET B SD   1 
ATOM   8143  C CE   . MET B 1 247 ? 24.914  35.338  -2.505  1.00 83.44  ? 247 MET B CE   1 
ATOM   8144  H H    . MET B 1 247 ? 22.687  30.357  -5.038  1.00 110.16 ? 247 MET B H    1 
ATOM   8145  H HA   . MET B 1 247 ? 24.669  31.561  -3.633  1.00 110.39 ? 247 MET B HA   1 
ATOM   8146  H HB2  . MET B 1 247 ? 23.082  33.072  -4.398  1.00 107.03 ? 247 MET B HB2  1 
ATOM   8147  H HB3  . MET B 1 247 ? 21.922  32.223  -3.720  1.00 107.03 ? 247 MET B HB3  1 
ATOM   8148  H HG2  . MET B 1 247 ? 22.526  34.236  -2.561  1.00 101.38 ? 247 MET B HG2  1 
ATOM   8149  H HG3  . MET B 1 247 ? 22.485  32.930  -1.658  1.00 101.38 ? 247 MET B HG3  1 
ATOM   8150  H HE1  . MET B 1 247 ? 25.806  35.630  -2.258  1.00 100.13 ? 247 MET B HE1  1 
ATOM   8151  H HE2  . MET B 1 247 ? 24.833  35.304  -3.471  1.00 100.13 ? 247 MET B HE2  1 
ATOM   8152  H HE3  . MET B 1 247 ? 24.254  35.948  -2.139  1.00 100.13 ? 247 MET B HE3  1 
ATOM   8153  N N    . TYR B 1 248 ? 24.483  30.253  -1.588  1.00 89.49  ? 248 TYR B N    1 
ATOM   8154  C CA   . TYR B 1 248 ? 24.366  29.507  -0.347  1.00 85.59  ? 248 TYR B CA   1 
ATOM   8155  C C    . TYR B 1 248 ? 24.714  30.424  0.816   1.00 84.17  ? 248 TYR B C    1 
ATOM   8156  O O    . TYR B 1 248 ? 25.572  31.306  0.698   1.00 83.08  ? 248 TYR B O    1 
ATOM   8157  C CB   . TYR B 1 248 ? 25.285  28.280  -0.338  1.00 85.03  ? 248 TYR B CB   1 
ATOM   8158  C CG   . TYR B 1 248 ? 25.032  27.322  -1.481  1.00 88.13  ? 248 TYR B CG   1 
ATOM   8159  C CD1  . TYR B 1 248 ? 23.919  26.495  -1.486  1.00 86.40  ? 248 TYR B CD1  1 
ATOM   8160  C CD2  . TYR B 1 248 ? 25.911  27.247  -2.554  1.00 91.92  ? 248 TYR B CD2  1 
ATOM   8161  C CE1  . TYR B 1 248 ? 23.683  25.619  -2.530  1.00 88.38  ? 248 TYR B CE1  1 
ATOM   8162  C CE2  . TYR B 1 248 ? 25.688  26.375  -3.601  1.00 90.04  ? 248 TYR B CE2  1 
ATOM   8163  C CZ   . TYR B 1 248 ? 24.572  25.566  -3.584  1.00 87.12  ? 248 TYR B CZ   1 
ATOM   8164  O OH   . TYR B 1 248 ? 24.341  24.697  -4.624  1.00 90.29  ? 248 TYR B OH   1 
ATOM   8165  H H    . TYR B 1 248 ? 25.267  30.584  -1.715  1.00 107.38 ? 248 TYR B H    1 
ATOM   8166  H HA   . TYR B 1 248 ? 23.456  29.192  -0.235  1.00 102.71 ? 248 TYR B HA   1 
ATOM   8167  H HB2  . TYR B 1 248 ? 26.205  28.578  -0.399  1.00 102.04 ? 248 TYR B HB2  1 
ATOM   8168  H HB3  . TYR B 1 248 ? 25.148  27.794  0.491   1.00 102.04 ? 248 TYR B HB3  1 
ATOM   8169  H HD1  . TYR B 1 248 ? 23.321  26.529  -0.774  1.00 103.68 ? 248 TYR B HD1  1 
ATOM   8170  H HD2  . TYR B 1 248 ? 26.662  27.795  -2.568  1.00 110.31 ? 248 TYR B HD2  1 
ATOM   8171  H HE1  . TYR B 1 248 ? 22.932  25.072  -2.522  1.00 106.06 ? 248 TYR B HE1  1 
ATOM   8172  H HE2  . TYR B 1 248 ? 26.286  26.333  -4.312  1.00 108.04 ? 248 TYR B HE2  1 
ATOM   8173  H HH   . TYR B 1 248 ? 24.950  24.769  -5.198  1.00 108.35 ? 248 TYR B HH   1 
ATOM   8174  N N    . ILE B 1 249 ? 24.033  30.215  1.941   1.00 81.29  ? 249 ILE B N    1 
ATOM   8175  C CA   . ILE B 1 249 ? 24.299  30.938  3.179   1.00 77.77  ? 249 ILE B CA   1 
ATOM   8176  C C    . ILE B 1 249 ? 24.707  29.914  4.230   1.00 77.51  ? 249 ILE B C    1 
ATOM   8177  O O    . ILE B 1 249 ? 23.927  29.010  4.560   1.00 74.00  ? 249 ILE B O    1 
ATOM   8178  C CB   . ILE B 1 249 ? 23.083  31.761  3.639   1.00 76.48  ? 249 ILE B CB   1 
ATOM   8179  C CG1  . ILE B 1 249 ? 23.052  33.112  2.910   1.00 75.32  ? 249 ILE B CG1  1 
ATOM   8180  C CG2  . ILE B 1 249 ? 23.109  31.956  5.149   1.00 78.04  ? 249 ILE B CG2  1 
ATOM   8181  C CD1  . ILE B 1 249 ? 23.984  34.159  3.493   1.00 75.17  ? 249 ILE B CD1  1 
ATOM   8182  H H    . ILE B 1 249 ? 23.395  29.643  2.011   1.00 97.55  ? 249 ILE B H    1 
ATOM   8183  H HA   . ILE B 1 249 ? 25.039  31.551  3.045   1.00 93.32  ? 249 ILE B HA   1 
ATOM   8184  H HB   . ILE B 1 249 ? 22.276  31.272  3.414   1.00 91.78  ? 249 ILE B HB   1 
ATOM   8185  H HG12 . ILE B 1 249 ? 23.310  32.971  1.986   1.00 90.39  ? 249 ILE B HG12 1 
ATOM   8186  H HG13 . ILE B 1 249 ? 22.150  33.466  2.952   1.00 90.39  ? 249 ILE B HG13 1 
ATOM   8187  H HG21 . ILE B 1 249 ? 22.500  32.674  5.385   1.00 93.65  ? 249 ILE B HG21 1 
ATOM   8188  H HG22 . ILE B 1 249 ? 22.831  31.132  5.579   1.00 93.65  ? 249 ILE B HG22 1 
ATOM   8189  H HG23 . ILE B 1 249 ? 24.011  32.184  5.423   1.00 93.65  ? 249 ILE B HG23 1 
ATOM   8190  H HD11 . ILE B 1 249 ? 24.090  34.880  2.852   1.00 90.21  ? 249 ILE B HD11 1 
ATOM   8191  H HD12 . ILE B 1 249 ? 23.600  34.502  4.315   1.00 90.21  ? 249 ILE B HD12 1 
ATOM   8192  H HD13 . ILE B 1 249 ? 24.844  33.750  3.676   1.00 90.21  ? 249 ILE B HD13 1 
ATOM   8193  N N    . ASP B 1 250 ? 25.929  30.046  4.737   1.00 77.71  ? 250 ASP B N    1 
ATOM   8194  C CA   . ASP B 1 250 ? 26.446  29.223  5.818   1.00 77.10  ? 250 ASP B CA   1 
ATOM   8195  C C    . ASP B 1 250 ? 26.512  30.061  7.089   1.00 77.16  ? 250 ASP B C    1 
ATOM   8196  O O    . ASP B 1 250 ? 26.682  31.283  7.036   1.00 79.99  ? 250 ASP B O    1 
ATOM   8197  C CB   . ASP B 1 250 ? 27.834  28.670  5.480   1.00 76.98  ? 250 ASP B CB   1 
ATOM   8198  C CG   . ASP B 1 250 ? 28.210  27.464  6.332   1.00 77.01  ? 250 ASP B CG   1 
ATOM   8199  O OD1  . ASP B 1 250 ? 27.435  27.087  7.238   1.00 76.41  ? 250 ASP B OD1  1 
ATOM   8200  O OD2  . ASP B 1 250 ? 29.290  26.881  6.096   1.00 77.52  ? 250 ASP B OD2  1 
ATOM   8201  H H    . ASP B 1 250 ? 26.498  30.628  4.458   1.00 93.26  ? 250 ASP B H    1 
ATOM   8202  H HA   . ASP B 1 250 ? 25.860  28.465  5.971   1.00 92.52  ? 250 ASP B HA   1 
ATOM   8203  H HB2  . ASP B 1 250 ? 27.848  28.396  4.550   1.00 92.38  ? 250 ASP B HB2  1 
ATOM   8204  H HB3  . ASP B 1 250 ? 28.496  29.362  5.632   1.00 92.38  ? 250 ASP B HB3  1 
ATOM   8205  N N    . GLY B 1 251 ? 26.374  29.400  8.243   1.00 73.47  ? 251 GLY B N    1 
ATOM   8206  C CA   . GLY B 1 251 ? 26.430  30.090  9.523   1.00 75.79  ? 251 GLY B CA   1 
ATOM   8207  C C    . GLY B 1 251 ? 26.295  29.174  10.726  1.00 72.58  ? 251 GLY B C    1 
ATOM   8208  O O    . GLY B 1 251 ? 25.851  28.026  10.614  1.00 73.45  ? 251 GLY B O    1 
ATOM   8209  H H    . GLY B 1 251 ? 26.248  28.551  8.305   1.00 88.16  ? 251 GLY B H    1 
ATOM   8210  H HA2  . GLY B 1 251 ? 27.279  30.554  9.594   1.00 90.95  ? 251 GLY B HA2  1 
ATOM   8211  H HA3  . GLY B 1 251 ? 25.711  30.740  9.561   1.00 90.95  ? 251 GLY B HA3  1 
ATOM   8212  N N    . PRO B 1 252 ? 26.718  29.647  11.890  1.00 71.82  ? 252 PRO B N    1 
ATOM   8213  C CA   . PRO B 1 252 ? 26.626  28.810  13.085  1.00 75.61  ? 252 PRO B CA   1 
ATOM   8214  C C    . PRO B 1 252 ? 25.201  28.732  13.617  1.00 72.59  ? 252 PRO B C    1 
ATOM   8215  O O    . PRO B 1 252 ? 24.401  29.664  13.487  1.00 71.24  ? 252 PRO B O    1 
ATOM   8216  C CB   . PRO B 1 252 ? 27.544  29.489  14.106  1.00 69.62  ? 252 PRO B CB   1 
ATOM   8217  C CG   . PRO B 1 252 ? 28.192  30.603  13.421  1.00 76.64  ? 252 PRO B CG   1 
ATOM   8218  C CD   . PRO B 1 252 ? 27.641  30.765  12.030  1.00 73.93  ? 252 PRO B CD   1 
ATOM   8219  H HA   . PRO B 1 252 ? 26.964  27.922  12.893  1.00 90.73  ? 252 PRO B HA   1 
ATOM   8220  H HB2  . PRO B 1 252 ? 27.015  29.810  14.852  1.00 83.54  ? 252 PRO B HB2  1 
ATOM   8221  H HB3  . PRO B 1 252 ? 28.205  28.851  14.418  1.00 83.54  ? 252 PRO B HB3  1 
ATOM   8222  H HG2  . PRO B 1 252 ? 28.031  31.412  13.931  1.00 91.96  ? 252 PRO B HG2  1 
ATOM   8223  H HG3  . PRO B 1 252 ? 29.144  30.424  13.375  1.00 91.96  ? 252 PRO B HG3  1 
ATOM   8224  H HD2  . PRO B 1 252 ? 27.172  31.609  11.942  1.00 88.72  ? 252 PRO B HD2  1 
ATOM   8225  H HD3  . PRO B 1 252 ? 28.350  30.708  11.370  1.00 88.72  ? 252 PRO B HD3  1 
ATOM   8226  N N    . VAL B 1 253 ? 24.880  27.586  14.216  1.00 72.49  ? 253 VAL B N    1 
ATOM   8227  C CA   . VAL B 1 253 ? 23.603  27.373  14.876  1.00 74.38  ? 253 VAL B CA   1 
ATOM   8228  C C    . VAL B 1 253 ? 23.881  26.727  16.226  1.00 73.34  ? 253 VAL B C    1 
ATOM   8229  O O    . VAL B 1 253 ? 24.785  25.891  16.351  1.00 72.12  ? 253 VAL B O    1 
ATOM   8230  C CB   . VAL B 1 253 ? 22.660  26.498  14.030  1.00 71.23  ? 253 VAL B CB   1 
ATOM   8231  C CG1  . VAL B 1 253 ? 21.355  26.249  14.779  1.00 69.77  ? 253 VAL B CG1  1 
ATOM   8232  C CG2  . VAL B 1 253 ? 22.385  27.159  12.691  1.00 71.70  ? 253 VAL B CG2  1 
ATOM   8233  H H    . VAL B 1 253 ? 25.402  26.904  14.251  1.00 86.98  ? 253 VAL B H    1 
ATOM   8234  H HA   . VAL B 1 253 ? 23.161  28.224  15.023  1.00 89.26  ? 253 VAL B HA   1 
ATOM   8235  H HB   . VAL B 1 253 ? 23.085  25.643  13.864  1.00 85.47  ? 253 VAL B HB   1 
ATOM   8236  H HG11 . VAL B 1 253 ? 20.739  25.781  14.194  1.00 83.72  ? 253 VAL B HG11 1 
ATOM   8237  H HG12 . VAL B 1 253 ? 21.540  25.711  15.564  1.00 83.72  ? 253 VAL B HG12 1 
ATOM   8238  H HG13 . VAL B 1 253 ? 20.975  27.102  15.044  1.00 83.72  ? 253 VAL B HG13 1 
ATOM   8239  H HG21 . VAL B 1 253 ? 21.759  26.612  12.191  1.00 86.03  ? 253 VAL B HG21 1 
ATOM   8240  H HG22 . VAL B 1 253 ? 22.006  28.038  12.844  1.00 86.03  ? 253 VAL B HG22 1 
ATOM   8241  H HG23 . VAL B 1 253 ? 23.219  27.238  12.201  1.00 86.03  ? 253 VAL B HG23 1 
ATOM   8242  N N    . GLU B 1 254 ? 23.110  27.121  17.236  1.00 74.17  ? 254 GLU B N    1 
ATOM   8243  C CA   . GLU B 1 254 ? 23.278  26.590  18.582  1.00 72.57  ? 254 GLU B CA   1 
ATOM   8244  C C    . GLU B 1 254 ? 21.918  26.299  19.187  1.00 71.54  ? 254 GLU B C    1 
ATOM   8245  O O    . GLU B 1 254 ? 21.052  27.178  19.224  1.00 69.60  ? 254 GLU B O    1 
ATOM   8246  C CB   . GLU B 1 254 ? 24.048  27.572  19.477  1.00 73.56  ? 254 GLU B CB   1 
ATOM   8247  C CG   . GLU B 1 254 ? 24.547  26.969  20.779  1.00 76.81  ? 254 GLU B CG   1 
ATOM   8248  C CD   . GLU B 1 254 ? 24.984  28.026  21.775  1.00 82.03  ? 254 GLU B CD   1 
ATOM   8249  O OE1  . GLU B 1 254 ? 25.540  29.057  21.333  1.00 82.23  ? 254 GLU B OE1  1 
ATOM   8250  O OE2  . GLU B 1 254 ? 24.769  27.830  22.993  1.00 80.63  ? 254 GLU B OE2  1 
ATOM   8251  H H    . GLU B 1 254 ? 22.478  27.700  17.164  1.00 89.00  ? 254 GLU B H    1 
ATOM   8252  H HA   . GLU B 1 254 ? 23.775  25.758  18.534  1.00 87.08  ? 254 GLU B HA   1 
ATOM   8253  H HB2  . GLU B 1 254 ? 24.820  27.896  18.988  1.00 88.27  ? 254 GLU B HB2  1 
ATOM   8254  H HB3  . GLU B 1 254 ? 23.462  28.312  19.700  1.00 88.27  ? 254 GLU B HB3  1 
ATOM   8255  H HG2  . GLU B 1 254 ? 23.833  26.451  21.183  1.00 92.17  ? 254 GLU B HG2  1 
ATOM   8256  H HG3  . GLU B 1 254 ? 25.308  26.397  20.593  1.00 92.17  ? 254 GLU B HG3  1 
ATOM   8257  N N    . ILE B 1 255 ? 21.737  25.067  19.658  1.00 73.47  ? 255 ILE B N    1 
ATOM   8258  C CA   . ILE B 1 255 ? 20.523  24.683  20.370  1.00 71.14  ? 255 ILE B CA   1 
ATOM   8259  C C    . ILE B 1 255 ? 20.626  25.208  21.793  1.00 73.29  ? 255 ILE B C    1 
ATOM   8260  O O    . ILE B 1 255 ? 21.578  24.890  22.514  1.00 75.06  ? 255 ILE B O    1 
ATOM   8261  C CB   . ILE B 1 255 ? 20.322  23.161  20.359  1.00 72.96  ? 255 ILE B CB   1 
ATOM   8262  C CG1  . ILE B 1 255 ? 20.398  22.625  18.931  1.00 69.89  ? 255 ILE B CG1  1 
ATOM   8263  C CG2  . ILE B 1 255 ? 18.985  22.806  21.004  1.00 70.75  ? 255 ILE B CG2  1 
ATOM   8264  C CD1  . ILE B 1 255 ? 19.250  23.067  18.059  1.00 70.02  ? 255 ILE B CD1  1 
ATOM   8265  H H    . ILE B 1 255 ? 22.310  24.430  19.577  1.00 88.16  ? 255 ILE B H    1 
ATOM   8266  H HA   . ILE B 1 255 ? 19.755  25.088  19.937  1.00 85.37  ? 255 ILE B HA   1 
ATOM   8267  H HB   . ILE B 1 255 ? 21.034  22.749  20.873  1.00 87.55  ? 255 ILE B HB   1 
ATOM   8268  H HG12 . ILE B 1 255 ? 21.219  22.940  18.522  1.00 83.87  ? 255 ILE B HG12 1 
ATOM   8269  H HG13 . ILE B 1 255 ? 20.392  21.656  18.961  1.00 83.87  ? 255 ILE B HG13 1 
ATOM   8270  H HG21 . ILE B 1 255 ? 18.787  21.874  20.825  1.00 84.90  ? 255 ILE B HG21 1 
ATOM   8271  H HG22 . ILE B 1 255 ? 19.047  22.954  21.960  1.00 84.90  ? 255 ILE B HG22 1 
ATOM   8272  H HG23 . ILE B 1 255 ? 18.293  23.370  20.625  1.00 84.90  ? 255 ILE B HG23 1 
ATOM   8273  H HD11 . ILE B 1 255 ? 19.391  22.733  17.159  1.00 84.03  ? 255 ILE B HD11 1 
ATOM   8274  H HD12 . ILE B 1 255 ? 18.424  22.708  18.419  1.00 84.03  ? 255 ILE B HD12 1 
ATOM   8275  H HD13 . ILE B 1 255 ? 19.214  24.036  18.051  1.00 84.03  ? 255 ILE B HD13 1 
ATOM   8276  N N    . ILE B 1 256 ? 19.640  26.001  22.205  1.00 72.16  ? 256 ILE B N    1 
ATOM   8277  C CA   . ILE B 1 256 ? 19.685  26.666  23.501  1.00 74.93  ? 256 ILE B CA   1 
ATOM   8278  C C    . ILE B 1 256 ? 18.919  25.868  24.548  1.00 74.93  ? 256 ILE B C    1 
ATOM   8279  O O    . ILE B 1 256 ? 19.498  25.406  25.537  1.00 72.68  ? 256 ILE B O    1 
ATOM   8280  C CB   . ILE B 1 256 ? 19.125  28.100  23.398  1.00 76.56  ? 256 ILE B CB   1 
ATOM   8281  C CG1  . ILE B 1 256 ? 20.143  29.023  22.729  1.00 76.10  ? 256 ILE B CG1  1 
ATOM   8282  C CG2  . ILE B 1 256 ? 18.737  28.625  24.778  1.00 72.71  ? 256 ILE B CG2  1 
ATOM   8283  C CD1  . ILE B 1 256 ? 19.524  30.258  22.118  1.00 72.98  ? 256 ILE B CD1  1 
ATOM   8284  H H    . ILE B 1 256 ? 18.931  26.170  21.748  1.00 86.60  ? 256 ILE B H    1 
ATOM   8285  H HA   . ILE B 1 256 ? 20.611  26.700  23.788  1.00 89.92  ? 256 ILE B HA   1 
ATOM   8286  H HB   . ILE B 1 256 ? 18.327  28.077  22.846  1.00 91.87  ? 256 ILE B HB   1 
ATOM   8287  H HG12 . ILE B 1 256 ? 20.788  29.311  23.393  1.00 91.32  ? 256 ILE B HG12 1 
ATOM   8288  H HG13 . ILE B 1 256 ? 20.592  28.535  22.021  1.00 91.32  ? 256 ILE B HG13 1 
ATOM   8289  H HG21 . ILE B 1 256 ? 18.671  29.592  24.741  1.00 87.25  ? 256 ILE B HG21 1 
ATOM   8290  H HG22 . ILE B 1 256 ? 17.882  28.245  25.032  1.00 87.25  ? 256 ILE B HG22 1 
ATOM   8291  H HG23 . ILE B 1 256 ? 19.419  28.365  25.418  1.00 87.25  ? 256 ILE B HG23 1 
ATOM   8292  H HD11 . ILE B 1 256 ? 20.193  30.960  22.080  1.00 87.58  ? 256 ILE B HD11 1 
ATOM   8293  H HD12 . ILE B 1 256 ? 19.215  30.047  21.224  1.00 87.58  ? 256 ILE B HD12 1 
ATOM   8294  H HD13 . ILE B 1 256 ? 18.778  30.542  22.669  1.00 87.58  ? 256 ILE B HD13 1 
ATOM   8295  N N    . ALA B 1 257 ? 17.612  25.718  24.348  1.00 74.15  ? 257 ALA B N    1 
ATOM   8296  C CA   . ALA B 1 257 ? 16.739  25.145  25.360  1.00 71.96  ? 257 ALA B CA   1 
ATOM   8297  C C    . ALA B 1 257 ? 15.686  24.272  24.696  1.00 70.83  ? 257 ALA B C    1 
ATOM   8298  O O    . ALA B 1 257 ? 15.528  24.269  23.473  1.00 70.86  ? 257 ALA B O    1 
ATOM   8299  C CB   . ALA B 1 257 ? 16.065  26.238  26.196  1.00 73.27  ? 257 ALA B CB   1 
ATOM   8300  H H    . ALA B 1 257 ? 17.205  25.945  23.625  1.00 88.98  ? 257 ALA B H    1 
ATOM   8301  H HA   . ALA B 1 257 ? 17.270  24.581  25.945  1.00 86.35  ? 257 ALA B HA   1 
ATOM   8302  H HB1  . ALA B 1 257 ? 15.495  25.821  26.861  1.00 87.92  ? 257 ALA B HB1  1 
ATOM   8303  H HB2  . ALA B 1 257 ? 16.750  26.769  26.633  1.00 87.92  ? 257 ALA B HB2  1 
ATOM   8304  H HB3  . ALA B 1 257 ? 15.534  26.801  25.611  1.00 87.92  ? 257 ALA B HB3  1 
ATOM   8305  N N    . GLU B 1 258 ? 14.942  23.544  25.528  1.00 70.60  ? 258 GLU B N    1 
ATOM   8306  C CA   . GLU B 1 258 ? 13.992  22.551  25.042  1.00 69.63  ? 258 GLU B CA   1 
ATOM   8307  C C    . GLU B 1 258 ? 13.026  22.211  26.161  1.00 71.79  ? 258 GLU B C    1 
ATOM   8308  O O    . GLU B 1 258 ? 13.453  22.020  27.303  1.00 72.43  ? 258 GLU B O    1 
ATOM   8309  C CB   . GLU B 1 258 ? 14.736  21.298  24.566  1.00 71.36  ? 258 GLU B CB   1 
ATOM   8310  C CG   . GLU B 1 258 ? 13.853  20.216  23.965  1.00 74.96  ? 258 GLU B CG   1 
ATOM   8311  C CD   . GLU B 1 258 ? 14.653  19.080  23.343  1.00 75.98  ? 258 GLU B CD   1 
ATOM   8312  O OE1  . GLU B 1 258 ? 15.904  19.132  23.358  1.00 75.78  ? 258 GLU B OE1  1 
ATOM   8313  O OE2  . GLU B 1 258 ? 14.028  18.129  22.831  1.00 79.28  ? 258 GLU B OE2  1 
ATOM   8314  H H    . GLU B 1 258 ? 14.970  23.608  26.385  1.00 84.72  ? 258 GLU B H    1 
ATOM   8315  H HA   . GLU B 1 258 ? 13.478  22.911  24.303  1.00 83.55  ? 258 GLU B HA   1 
ATOM   8316  H HB2  . GLU B 1 258 ? 15.377  21.561  23.886  1.00 85.63  ? 258 GLU B HB2  1 
ATOM   8317  H HB3  . GLU B 1 258 ? 15.198  20.908  25.324  1.00 85.63  ? 258 GLU B HB3  1 
ATOM   8318  H HG2  . GLU B 1 258 ? 13.293  19.841  24.662  1.00 89.95  ? 258 GLU B HG2  1 
ATOM   8319  H HG3  . GLU B 1 258 ? 13.300  20.608  23.271  1.00 89.95  ? 258 GLU B HG3  1 
ATOM   8320  N N    . GLY B 1 259 ? 11.736  22.153  25.837  1.00 63.93  ? 259 GLY B N    1 
ATOM   8321  C CA   . GLY B 1 259 ? 10.750  21.734  26.807  1.00 70.69  ? 259 GLY B CA   1 
ATOM   8322  C C    . GLY B 1 259 ? 9.336   22.210  26.564  1.00 73.60  ? 259 GLY B C    1 
ATOM   8323  O O    . GLY B 1 259 ? 8.879   22.260  25.423  1.00 69.40  ? 259 GLY B O    1 
ATOM   8324  H H    . GLY B 1 259 ? 11.415  22.352  25.064  1.00 76.72  ? 259 GLY B H    1 
ATOM   8325  H HA2  . GLY B 1 259 ? 10.731  20.764  26.825  1.00 84.83  ? 259 GLY B HA2  1 
ATOM   8326  H HA3  . GLY B 1 259 ? 11.021  22.060  27.680  1.00 84.83  ? 259 GLY B HA3  1 
ATOM   8327  N N    . LYS B 1 260 ? 8.636   22.564  27.646  1.00 75.51  ? 260 LYS B N    1 
ATOM   8328  C CA   . LYS B 1 260 ? 7.232   22.947  27.596  1.00 77.55  ? 260 LYS B CA   1 
ATOM   8329  C C    . LYS B 1 260 ? 7.085   24.450  27.801  1.00 77.91  ? 260 LYS B C    1 
ATOM   8330  O O    . LYS B 1 260 ? 7.822   25.055  28.587  1.00 76.80  ? 260 LYS B O    1 
ATOM   8331  C CB   . LYS B 1 260 ? 6.425   22.203  28.666  1.00 73.28  ? 260 LYS B CB   1 
ATOM   8332  C CG   . LYS B 1 260 ? 6.629   20.696  28.677  1.00 76.30  ? 260 LYS B CG   1 
ATOM   8333  C CD   . LYS B 1 260 ? 5.782   20.012  27.612  1.00 80.82  ? 260 LYS B CD   1 
ATOM   8334  C CE   . LYS B 1 260 ? 5.979   18.502  27.622  1.00 78.93  ? 260 LYS B CE   1 
ATOM   8335  N NZ   . LYS B 1 260 ? 4.888   17.797  26.893  1.00 80.78  ? 260 LYS B NZ   1 
ATOM   8336  H H    . LYS B 1 260 ? 8.966   22.588  28.439  1.00 90.62  ? 260 LYS B H    1 
ATOM   8337  H HA   . LYS B 1 260 ? 6.873   22.725  26.722  1.00 93.06  ? 260 LYS B HA   1 
ATOM   8338  H HB2  . LYS B 1 260 ? 6.685   22.540  29.538  1.00 87.94  ? 260 LYS B HB2  1 
ATOM   8339  H HB3  . LYS B 1 260 ? 5.482   22.370  28.513  1.00 87.94  ? 260 LYS B HB3  1 
ATOM   8340  H HG2  . LYS B 1 260 ? 7.561   20.496  28.500  1.00 91.56  ? 260 LYS B HG2  1 
ATOM   8341  H HG3  . LYS B 1 260 ? 6.372   20.343  29.543  1.00 91.56  ? 260 LYS B HG3  1 
ATOM   8342  H HD2  . LYS B 1 260 ? 4.845   20.198  27.779  1.00 96.99  ? 260 LYS B HD2  1 
ATOM   8343  H HD3  . LYS B 1 260 ? 6.035   20.346  26.737  1.00 96.99  ? 260 LYS B HD3  1 
ATOM   8344  H HE2  . LYS B 1 260 ? 6.821   18.286  27.192  1.00 94.72  ? 260 LYS B HE2  1 
ATOM   8345  H HE3  . LYS B 1 260 ? 5.985   18.186  28.539  1.00 94.72  ? 260 LYS B HE3  1 
ATOM   8346  H HZ1  . LYS B 1 260 ? 5.023   16.918  26.921  1.00 96.93  ? 260 LYS B HZ1  1 
ATOM   8347  H HZ2  . LYS B 1 260 ? 4.103   17.981  27.269  1.00 96.93  ? 260 LYS B HZ2  1 
ATOM   8348  H HZ3  . LYS B 1 260 ? 4.871   18.060  26.043  1.00 96.93  ? 260 LYS B HZ3  1 
ATOM   8349  N N    . ILE B 1 261 ? 6.123   25.045  27.098  1.00 76.04  ? 261 ILE B N    1 
ATOM   8350  C CA   . ILE B 1 261 ? 5.784   26.454  27.245  1.00 77.79  ? 261 ILE B CA   1 
ATOM   8351  C C    . ILE B 1 261 ? 4.301   26.563  27.571  1.00 81.44  ? 261 ILE B C    1 
ATOM   8352  O O    . ILE B 1 261 ? 3.478   25.816  27.029  1.00 79.25  ? 261 ILE B O    1 
ATOM   8353  C CB   . ILE B 1 261 ? 6.134   27.258  25.978  1.00 78.81  ? 261 ILE B CB   1 
ATOM   8354  C CG1  . ILE B 1 261 ? 6.015   28.759  26.246  1.00 82.02  ? 261 ILE B CG1  1 
ATOM   8355  C CG2  . ILE B 1 261 ? 5.235   26.861  24.823  1.00 81.89  ? 261 ILE B CG2  1 
ATOM   8356  C CD1  . ILE B 1 261 ? 6.655   29.612  25.166  1.00 85.92  ? 261 ILE B CD1  1 
ATOM   8357  H H    . ILE B 1 261 ? 5.641   24.639  26.513  1.00 91.25  ? 261 ILE B H    1 
ATOM   8358  H HA   . ILE B 1 261 ? 6.284   26.830  27.986  1.00 93.35  ? 261 ILE B HA   1 
ATOM   8359  H HB   . ILE B 1 261 ? 7.052   27.054  25.740  1.00 94.57  ? 261 ILE B HB   1 
ATOM   8360  H HG12 . ILE B 1 261 ? 5.075   28.995  26.295  1.00 98.42  ? 261 ILE B HG12 1 
ATOM   8361  H HG13 . ILE B 1 261 ? 6.453   28.964  27.087  1.00 98.42  ? 261 ILE B HG13 1 
ATOM   8362  H HG21 . ILE B 1 261 ? 5.637   27.159  23.993  1.00 98.27  ? 261 ILE B HG21 1 
ATOM   8363  H HG22 . ILE B 1 261 ? 5.137   25.896  24.815  1.00 98.27  ? 261 ILE B HG22 1 
ATOM   8364  H HG23 . ILE B 1 261 ? 4.367   27.280  24.940  1.00 98.27  ? 261 ILE B HG23 1 
ATOM   8365  H HD11 . ILE B 1 261 ? 6.348   30.527  25.262  1.00 103.10 ? 261 ILE B HD11 1 
ATOM   8366  H HD12 . ILE B 1 261 ? 7.620   29.575  25.265  1.00 103.10 ? 261 ILE B HD12 1 
ATOM   8367  H HD13 . ILE B 1 261 ? 6.399   29.267  24.296  1.00 103.10 ? 261 ILE B HD13 1 
ATOM   8368  N N    . TYR B 1 262 ? 3.964   27.488  28.468  1.00 84.29  ? 262 TYR B N    1 
ATOM   8369  C CA   . TYR B 1 262 ? 2.604   27.664  28.964  1.00 85.64  ? 262 TYR B CA   1 
ATOM   8370  C C    . TYR B 1 262 ? 2.059   28.995  28.464  1.00 89.29  ? 262 TYR B C    1 
ATOM   8371  O O    . TYR B 1 262 ? 2.594   30.056  28.806  1.00 88.76  ? 262 TYR B O    1 
ATOM   8372  C CB   . TYR B 1 262 ? 2.577   27.605  30.489  1.00 81.73  ? 262 TYR B CB   1 
ATOM   8373  C CG   . TYR B 1 262 ? 3.224   26.359  31.044  1.00 81.08  ? 262 TYR B CG   1 
ATOM   8374  C CD1  . TYR B 1 262 ? 2.626   25.117  30.884  1.00 81.84  ? 262 TYR B CD1  1 
ATOM   8375  C CD2  . TYR B 1 262 ? 4.439   26.419  31.720  1.00 80.82  ? 262 TYR B CD2  1 
ATOM   8376  C CE1  . TYR B 1 262 ? 3.213   23.972  31.383  1.00 79.92  ? 262 TYR B CE1  1 
ATOM   8377  C CE2  . TYR B 1 262 ? 5.036   25.274  32.225  1.00 76.80  ? 262 TYR B CE2  1 
ATOM   8378  C CZ   . TYR B 1 262 ? 4.417   24.056  32.051  1.00 76.80  ? 262 TYR B CZ   1 
ATOM   8379  O OH   . TYR B 1 262 ? 5.001   22.915  32.546  1.00 80.36  ? 262 TYR B OH   1 
ATOM   8380  H H    . TYR B 1 262 ? 4.525   28.041  28.813  1.00 101.15 ? 262 TYR B H    1 
ATOM   8381  H HA   . TYR B 1 262 ? 2.036   26.959  28.616  1.00 102.77 ? 262 TYR B HA   1 
ATOM   8382  H HB2  . TYR B 1 262 ? 3.053   28.372  30.843  1.00 98.07  ? 262 TYR B HB2  1 
ATOM   8383  H HB3  . TYR B 1 262 ? 1.654   27.620  30.788  1.00 98.07  ? 262 TYR B HB3  1 
ATOM   8384  H HD1  . TYR B 1 262 ? 1.815   25.056  30.433  1.00 98.21  ? 262 TYR B HD1  1 
ATOM   8385  H HD2  . TYR B 1 262 ? 4.857   27.241  31.836  1.00 96.99  ? 262 TYR B HD2  1 
ATOM   8386  H HE1  . TYR B 1 262 ? 2.799   23.147  31.270  1.00 95.91  ? 262 TYR B HE1  1 
ATOM   8387  H HE2  . TYR B 1 262 ? 5.847   25.328  32.676  1.00 92.16  ? 262 TYR B HE2  1 
ATOM   8388  H HH   . TYR B 1 262 ? 5.735   23.102  32.909  1.00 96.43  ? 262 TYR B HH   1 
ATOM   8389  N N    . ILE B 1 263 ? 0.995   28.932  27.662  1.00 92.50  ? 263 ILE B N    1 
ATOM   8390  C CA   . ILE B 1 263 ? 0.399   30.100  27.027  1.00 93.28  ? 263 ILE B CA   1 
ATOM   8391  C C    . ILE B 1 263 ? -1.111  30.033  27.204  1.00 98.79  ? 263 ILE B C    1 
ATOM   8392  O O    . ILE B 1 263 ? -1.690  28.956  27.373  1.00 101.00 ? 263 ILE B O    1 
ATOM   8393  C CB   . ILE B 1 263 ? 0.785   30.177  25.531  1.00 96.86  ? 263 ILE B CB   1 
ATOM   8394  C CG1  . ILE B 1 263 ? 2.242   30.638  25.391  1.00 93.09  ? 263 ILE B CG1  1 
ATOM   8395  C CG2  . ILE B 1 263 ? -0.165  31.089  24.762  1.00 100.40 ? 263 ILE B CG2  1 
ATOM   8396  C CD1  . ILE B 1 263 ? 2.410   32.143  25.230  1.00 91.46  ? 263 ILE B CD1  1 
ATOM   8397  H H    . ILE B 1 263 ? 0.590   28.199  27.467  1.00 111.00 ? 263 ILE B H    1 
ATOM   8398  H HA   . ILE B 1 263 ? 0.709   30.908  27.464  1.00 111.94 ? 263 ILE B HA   1 
ATOM   8399  H HB   . ILE B 1 263 ? 0.704   29.290  25.146  1.00 116.24 ? 263 ILE B HB   1 
ATOM   8400  H HG12 . ILE B 1 263 ? 2.730   30.371  26.186  1.00 111.71 ? 263 ILE B HG12 1 
ATOM   8401  H HG13 . ILE B 1 263 ? 2.628   30.214  24.608  1.00 111.71 ? 263 ILE B HG13 1 
ATOM   8402  H HG21 . ILE B 1 263 ? 0.212   31.271  23.887  1.00 120.48 ? 263 ILE B HG21 1 
ATOM   8403  H HG22 . ILE B 1 263 ? -1.021  30.644  24.667  1.00 120.48 ? 263 ILE B HG22 1 
ATOM   8404  H HG23 . ILE B 1 263 ? -0.275  31.917  25.254  1.00 120.48 ? 263 ILE B HG23 1 
ATOM   8405  H HD11 . ILE B 1 263 ? 3.352   32.364  25.293  1.00 109.76 ? 263 ILE B HD11 1 
ATOM   8406  H HD12 . ILE B 1 263 ? 2.065   32.408  24.363  1.00 109.76 ? 263 ILE B HD12 1 
ATOM   8407  H HD13 . ILE B 1 263 ? 1.916   32.592  25.934  1.00 109.76 ? 263 ILE B HD13 1 
ATOM   8408  N N    . GLY B 1 264 ? -1.748  31.201  27.180  1.00 106.44 ? 264 GLY B N    1 
ATOM   8409  C CA   . GLY B 1 264 ? -3.194  31.241  27.306  1.00 109.12 ? 264 GLY B CA   1 
ATOM   8410  C C    . GLY B 1 264 ? -3.870  30.573  26.122  1.00 113.27 ? 264 GLY B C    1 
ATOM   8411  O O    . GLY B 1 264 ? -3.408  30.663  24.983  1.00 114.30 ? 264 GLY B O    1 
ATOM   8412  H H    . GLY B 1 264 ? -1.371  31.969  27.094  1.00 127.73 ? 264 GLY B H    1 
ATOM   8413  H HA2  . GLY B 1 264 ? -3.463  30.782  28.117  1.00 130.95 ? 264 GLY B HA2  1 
ATOM   8414  H HA3  . GLY B 1 264 ? -3.491  32.163  27.352  1.00 130.95 ? 264 GLY B HA3  1 
ATOM   8415  N N    . LYS B 1 265 ? -4.980  29.895  26.401  1.00 116.15 ? 265 LYS B N    1 
ATOM   8416  C CA   . LYS B 1 265 ? -5.718  29.163  25.377  1.00 117.29 ? 265 LYS B CA   1 
ATOM   8417  C C    . LYS B 1 265 ? -6.838  30.021  24.798  1.00 119.31 ? 265 LYS B C    1 
ATOM   8418  O O    . LYS B 1 265 ? -7.044  31.159  25.220  1.00 117.90 ? 265 LYS B O    1 
ATOM   8419  C CB   . LYS B 1 265 ? -6.293  27.868  25.960  1.00 119.23 ? 265 LYS B CB   1 
ATOM   8420  C CG   . LYS B 1 265 ? -6.316  26.695  24.990  1.00 115.64 ? 265 LYS B CG   1 
ATOM   8421  C CD   . LYS B 1 265 ? -7.659  26.581  24.279  1.00 121.67 ? 265 LYS B CD   1 
ATOM   8422  C CE   . LYS B 1 265 ? -7.846  25.200  23.666  1.00 119.31 ? 265 LYS B CE   1 
ATOM   8423  N NZ   . LYS B 1 265 ? -6.670  24.793  22.845  1.00 114.18 ? 265 LYS B NZ   1 
ATOM   8424  H H    . LYS B 1 265 ? -5.330  29.844  27.185  1.00 139.38 ? 265 LYS B H    1 
ATOM   8425  H HA   . LYS B 1 265 ? -5.115  28.927  24.655  1.00 140.74 ? 265 LYS B HA   1 
ATOM   8426  H HB2  . LYS B 1 265 ? -5.755  27.607  26.723  1.00 143.07 ? 265 LYS B HB2  1 
ATOM   8427  H HB3  . LYS B 1 265 ? -7.207  28.035  26.239  1.00 143.07 ? 265 LYS B HB3  1 
ATOM   8428  H HG2  . LYS B 1 265 ? -5.626  26.819  24.320  1.00 138.77 ? 265 LYS B HG2  1 
ATOM   8429  H HG3  . LYS B 1 265 ? -6.160  25.872  25.479  1.00 138.77 ? 265 LYS B HG3  1 
ATOM   8430  H HD2  . LYS B 1 265 ? -8.375  26.732  24.916  1.00 146.00 ? 265 LYS B HD2  1 
ATOM   8431  H HD3  . LYS B 1 265 ? -7.703  27.239  23.567  1.00 146.00 ? 265 LYS B HD3  1 
ATOM   8432  H HE2  . LYS B 1 265 ? -7.961  24.548  24.375  1.00 143.17 ? 265 LYS B HE2  1 
ATOM   8433  H HE3  . LYS B 1 265 ? -8.628  25.208  23.093  1.00 143.17 ? 265 LYS B HE3  1 
ATOM   8434  H HZ1  . LYS B 1 265 ? -6.509  25.406  22.220  1.00 137.01 ? 265 LYS B HZ1  1 
ATOM   8435  H HZ2  . LYS B 1 265 ? -5.951  24.713  23.363  1.00 137.01 ? 265 LYS B HZ2  1 
ATOM   8436  H HZ3  . LYS B 1 265 ? -6.831  24.013  22.449  1.00 137.01 ? 265 LYS B HZ3  1 
ATOM   8437  N N    . ASP C 1 2   ? 37.981  14.537  45.508  1.00 135.82 ? 2   ASP C N    1 
ATOM   8438  C CA   . ASP C 1 2   ? 37.494  13.386  44.756  1.00 137.05 ? 2   ASP C CA   1 
ATOM   8439  C C    . ASP C 1 2   ? 36.097  12.984  45.227  1.00 135.45 ? 2   ASP C C    1 
ATOM   8440  O O    . ASP C 1 2   ? 35.891  11.872  45.712  1.00 139.93 ? 2   ASP C O    1 
ATOM   8441  C CB   . ASP C 1 2   ? 38.460  12.208  44.898  1.00 138.51 ? 2   ASP C CB   1 
ATOM   8442  C CG   . ASP C 1 2   ? 38.176  11.095  43.904  1.00 138.39 ? 2   ASP C CG   1 
ATOM   8443  O OD1  . ASP C 1 2   ? 38.089  11.384  42.690  1.00 137.57 ? 2   ASP C OD1  1 
ATOM   8444  O OD2  . ASP C 1 2   ? 38.041  9.931   44.337  1.00 135.26 ? 2   ASP C OD2  1 
ATOM   8445  H H    . ASP C 1 2   ? 38.457  14.328  46.193  1.00 162.99 ? 2   ASP C H    1 
ATOM   8446  H HA   . ASP C 1 2   ? 37.440  13.617  43.815  1.00 164.46 ? 2   ASP C HA   1 
ATOM   8447  H HB2  . ASP C 1 2   ? 39.365  12.521  44.747  1.00 166.21 ? 2   ASP C HB2  1 
ATOM   8448  H HB3  . ASP C 1 2   ? 38.380  11.840  45.792  1.00 166.21 ? 2   ASP C HB3  1 
ATOM   8449  N N    . ARG C 1 3   ? 35.140  13.900  45.083  1.00 131.44 ? 3   ARG C N    1 
ATOM   8450  C CA   . ARG C 1 3   ? 33.754  13.643  45.468  1.00 123.30 ? 3   ARG C CA   1 
ATOM   8451  C C    . ARG C 1 3   ? 32.856  14.478  44.569  1.00 123.39 ? 3   ARG C C    1 
ATOM   8452  O O    . ARG C 1 3   ? 32.919  15.710  44.596  1.00 124.75 ? 3   ARG C O    1 
ATOM   8453  C CB   . ARG C 1 3   ? 33.522  13.957  46.954  1.00 120.96 ? 3   ARG C CB   1 
ATOM   8454  C CG   . ARG C 1 3   ? 33.315  15.427  47.316  1.00 124.39 ? 3   ARG C CG   1 
ATOM   8455  C CD   . ARG C 1 3   ? 34.533  16.279  47.003  1.00 129.01 ? 3   ARG C CD   1 
ATOM   8456  N NE   . ARG C 1 3   ? 35.704  15.881  47.776  1.00 132.32 ? 3   ARG C NE   1 
ATOM   8457  C CZ   . ARG C 1 3   ? 36.886  16.479  47.711  1.00 135.10 ? 3   ARG C CZ   1 
ATOM   8458  N NH1  . ARG C 1 3   ? 37.094  17.512  46.911  1.00 136.82 ? 3   ARG C NH1  1 
ATOM   8459  N NH2  . ARG C 1 3   ? 37.885  16.029  48.467  1.00 136.47 ? 3   ARG C NH2  1 
ATOM   8460  H H    . ARG C 1 3   ? 35.270  14.687  44.762  1.00 157.73 ? 3   ARG C H    1 
ATOM   8461  H HA   . ARG C 1 3   ? 33.536  12.708  45.330  1.00 147.96 ? 3   ARG C HA   1 
ATOM   8462  H HB2  . ARG C 1 3   ? 32.730  13.478  47.242  1.00 145.16 ? 3   ARG C HB2  1 
ATOM   8463  H HB3  . ARG C 1 3   ? 34.296  13.648  47.451  1.00 145.16 ? 3   ARG C HB3  1 
ATOM   8464  H HG2  . ARG C 1 3   ? 32.565  15.776  46.809  1.00 149.27 ? 3   ARG C HG2  1 
ATOM   8465  H HG3  . ARG C 1 3   ? 33.134  15.497  48.266  1.00 149.27 ? 3   ARG C HG3  1 
ATOM   8466  H HD2  . ARG C 1 3   ? 34.750  16.190  46.061  1.00 154.82 ? 3   ARG C HD2  1 
ATOM   8467  H HD3  . ARG C 1 3   ? 34.335  17.206  47.211  1.00 154.82 ? 3   ARG C HD3  1 
ATOM   8468  H HE   . ARG C 1 3   ? 35.622  15.213  48.312  1.00 158.78 ? 3   ARG C HE   1 
ATOM   8469  H HH11 . ARG C 1 3   ? 36.455  17.810  46.419  1.00 164.19 ? 3   ARG C HH11 1 
ATOM   8470  H HH12 . ARG C 1 3   ? 37.868  17.885  46.883  1.00 164.19 ? 3   ARG C HH12 1 
ATOM   8471  H HH21 . ARG C 1 3   ? 37.759  15.358  48.990  1.00 163.77 ? 3   ARG C HH21 1 
ATOM   8472  H HH22 . ARG C 1 3   ? 38.655  16.409  48.432  1.00 163.77 ? 3   ARG C HH22 1 
ATOM   8473  N N    . LYS C 1 4   ? 32.035  13.812  43.762  1.00 120.66 ? 4   LYS C N    1 
ATOM   8474  C CA   . LYS C 1 4   ? 31.245  14.488  42.744  1.00 114.08 ? 4   LYS C CA   1 
ATOM   8475  C C    . LYS C 1 4   ? 29.990  13.676  42.466  1.00 109.77 ? 4   LYS C C    1 
ATOM   8476  O O    . LYS C 1 4   ? 30.079  12.485  42.156  1.00 108.68 ? 4   LYS C O    1 
ATOM   8477  C CB   . LYS C 1 4   ? 32.062  14.674  41.454  1.00 120.06 ? 4   LYS C CB   1 
ATOM   8478  C CG   . LYS C 1 4   ? 32.805  13.419  40.989  1.00 126.43 ? 4   LYS C CG   1 
ATOM   8479  C CD   . LYS C 1 4   ? 34.234  13.729  40.533  1.00 128.85 ? 4   LYS C CD   1 
ATOM   8480  C CE   . LYS C 1 4   ? 35.017  12.449  40.250  1.00 130.22 ? 4   LYS C CE   1 
ATOM   8481  N NZ   . LYS C 1 4   ? 36.474  12.580  40.546  1.00 132.32 ? 4   LYS C NZ   1 
ATOM   8482  H H    . LYS C 1 4   ? 31.919  12.960  43.786  1.00 144.79 ? 4   LYS C H    1 
ATOM   8483  H HA   . LYS C 1 4   ? 30.973  15.360  43.068  1.00 136.90 ? 4   LYS C HA   1 
ATOM   8484  H HB2  . LYS C 1 4   ? 31.459  14.939  40.741  1.00 144.07 ? 4   LYS C HB2  1 
ATOM   8485  H HB3  . LYS C 1 4   ? 32.723  15.368  41.603  1.00 144.07 ? 4   LYS C HB3  1 
ATOM   8486  H HG2  . LYS C 1 4   ? 32.853  12.787  41.724  1.00 151.72 ? 4   LYS C HG2  1 
ATOM   8487  H HG3  . LYS C 1 4   ? 32.328  13.025  40.242  1.00 151.72 ? 4   LYS C HG3  1 
ATOM   8488  H HD2  . LYS C 1 4   ? 34.205  14.256  39.719  1.00 154.63 ? 4   LYS C HD2  1 
ATOM   8489  H HD3  . LYS C 1 4   ? 34.695  14.222  41.230  1.00 154.63 ? 4   LYS C HD3  1 
ATOM   8490  H HE2  . LYS C 1 4   ? 34.663  11.734  40.802  1.00 156.26 ? 4   LYS C HE2  1 
ATOM   8491  H HE3  . LYS C 1 4   ? 34.923  12.222  39.312  1.00 156.26 ? 4   LYS C HE3  1 
ATOM   8492  H HZ1  . LYS C 1 4   ? 36.593  12.785  41.404  1.00 158.78 ? 4   LYS C HZ1  1 
ATOM   8493  H HZ2  . LYS C 1 4   ? 36.830  13.222  40.044  1.00 158.78 ? 4   LYS C HZ2  1 
ATOM   8494  H HZ3  . LYS C 1 4   ? 36.890  11.813  40.373  1.00 158.78 ? 4   LYS C HZ3  1 
ATOM   8495  N N    . VAL C 1 5   ? 28.829  14.320  42.579  1.00 100.32 ? 5   VAL C N    1 
ATOM   8496  C CA   . VAL C 1 5   ? 27.544  13.660  42.376  1.00 94.55  ? 5   VAL C CA   1 
ATOM   8497  C C    . VAL C 1 5   ? 27.055  13.959  40.965  1.00 92.76  ? 5   VAL C C    1 
ATOM   8498  O O    . VAL C 1 5   ? 27.084  15.111  40.512  1.00 83.38  ? 5   VAL C O    1 
ATOM   8499  C CB   . VAL C 1 5   ? 26.509  14.104  43.426  1.00 88.31  ? 5   VAL C CB   1 
ATOM   8500  C CG1  . VAL C 1 5   ? 27.051  13.887  44.840  1.00 87.58  ? 5   VAL C CG1  1 
ATOM   8501  C CG2  . VAL C 1 5   ? 26.114  15.559  43.214  1.00 88.04  ? 5   VAL C CG2  1 
ATOM   8502  H H    . VAL C 1 5   ? 28.761  15.154  42.776  1.00 120.39 ? 5   VAL C H    1 
ATOM   8503  H HA   . VAL C 1 5   ? 27.667  12.702  42.457  1.00 113.46 ? 5   VAL C HA   1 
ATOM   8504  H HB   . VAL C 1 5   ? 25.711  13.562  43.325  1.00 105.97 ? 5   VAL C HB   1 
ATOM   8505  H HG11 . VAL C 1 5   ? 26.365  14.128  45.482  1.00 105.09 ? 5   VAL C HG11 1 
ATOM   8506  H HG12 . VAL C 1 5   ? 27.290  12.953  44.946  1.00 105.09 ? 5   VAL C HG12 1 
ATOM   8507  H HG13 . VAL C 1 5   ? 27.834  14.445  44.967  1.00 105.09 ? 5   VAL C HG13 1 
ATOM   8508  H HG21 . VAL C 1 5   ? 25.661  15.883  44.008  1.00 105.64 ? 5   VAL C HG21 1 
ATOM   8509  H HG22 . VAL C 1 5   ? 26.915  16.083  43.053  1.00 105.64 ? 5   VAL C HG22 1 
ATOM   8510  H HG23 . VAL C 1 5   ? 25.522  15.617  42.448  1.00 105.64 ? 5   VAL C HG23 1 
ATOM   8511  N N    . GLN C 1 6   ? 26.608  12.920  40.270  1.00 88.92  ? 6   GLN C N    1 
ATOM   8512  C CA   . GLN C 1 6   ? 26.071  13.021  38.920  1.00 85.87  ? 6   GLN C CA   1 
ATOM   8513  C C    . GLN C 1 6   ? 24.561  12.839  38.984  1.00 86.15  ? 6   GLN C C    1 
ATOM   8514  O O    . GLN C 1 6   ? 24.074  11.875  39.585  1.00 89.00  ? 6   GLN C O    1 
ATOM   8515  C CB   . GLN C 1 6   ? 26.709  11.968  38.015  1.00 88.25  ? 6   GLN C CB   1 
ATOM   8516  C CG   . GLN C 1 6   ? 26.652  12.305  36.544  1.00 94.26  ? 6   GLN C CG   1 
ATOM   8517  C CD   . GLN C 1 6   ? 27.611  11.470  35.719  1.00 93.51  ? 6   GLN C CD   1 
ATOM   8518  O OE1  . GLN C 1 6   ? 28.290  10.584  36.240  1.00 98.22  ? 6   GLN C OE1  1 
ATOM   8519  N NE2  . GLN C 1 6   ? 27.674  11.753  34.424  1.00 93.00  ? 6   GLN C NE2  1 
ATOM   8520  H H    . GLN C 1 6   ? 26.606  12.115  40.572  1.00 106.70 ? 6   GLN C H    1 
ATOM   8521  H HA   . GLN C 1 6   ? 26.257  13.894  38.541  1.00 103.05 ? 6   GLN C HA   1 
ATOM   8522  H HB2  . GLN C 1 6   ? 27.643  11.872  38.259  1.00 105.90 ? 6   GLN C HB2  1 
ATOM   8523  H HB3  . GLN C 1 6   ? 26.245  11.126  38.142  1.00 105.90 ? 6   GLN C HB3  1 
ATOM   8524  H HG2  . GLN C 1 6   ? 25.754  12.143  36.216  1.00 113.11 ? 6   GLN C HG2  1 
ATOM   8525  H HG3  . GLN C 1 6   ? 26.886  13.239  36.424  1.00 113.11 ? 6   GLN C HG3  1 
ATOM   8526  H HE21 . GLN C 1 6   ? 27.186  12.380  34.097  1.00 111.60 ? 6   GLN C HE21 1 
ATOM   8527  H HE22 . GLN C 1 6   ? 28.203  11.308  33.913  1.00 111.60 ? 6   GLN C HE22 1 
ATOM   8528  N N    . VAL C 1 7   ? 23.825  13.769  38.379  1.00 84.55  ? 7   VAL C N    1 
ATOM   8529  C CA   . VAL C 1 7   ? 22.369  13.824  38.494  1.00 82.81  ? 7   VAL C CA   1 
ATOM   8530  C C    . VAL C 1 7   ? 21.770  13.491  37.137  1.00 78.32  ? 7   VAL C C    1 
ATOM   8531  O O    . VAL C 1 7   ? 21.942  14.243  36.168  1.00 83.94  ? 7   VAL C O    1 
ATOM   8532  C CB   . VAL C 1 7   ? 21.886  15.194  38.990  1.00 78.71  ? 7   VAL C CB   1 
ATOM   8533  C CG1  . VAL C 1 7   ? 20.394  15.157  39.311  1.00 76.08  ? 7   VAL C CG1  1 
ATOM   8534  C CG2  . VAL C 1 7   ? 22.687  15.626  40.212  1.00 77.40  ? 7   VAL C CG2  1 
ATOM   8535  H H    . VAL C 1 7   ? 24.153  14.392  37.885  1.00 101.46 ? 7   VAL C H    1 
ATOM   8536  H HA   . VAL C 1 7   ? 22.078  13.150  39.129  1.00 99.38  ? 7   VAL C HA   1 
ATOM   8537  H HB   . VAL C 1 7   ? 22.024  15.849  38.288  1.00 94.46  ? 7   VAL C HB   1 
ATOM   8538  H HG11 . VAL C 1 7   ? 20.115  16.032  39.623  1.00 91.30  ? 7   VAL C HG11 1 
ATOM   8539  H HG12 . VAL C 1 7   ? 19.904  14.920  38.508  1.00 91.30  ? 7   VAL C HG12 1 
ATOM   8540  H HG13 . VAL C 1 7   ? 20.235  14.494  40.001  1.00 91.30  ? 7   VAL C HG13 1 
ATOM   8541  H HG21 . VAL C 1 7   ? 22.360  16.488  40.515  1.00 92.88  ? 7   VAL C HG21 1 
ATOM   8542  H HG22 . VAL C 1 7   ? 22.576  14.965  40.912  1.00 92.88  ? 7   VAL C HG22 1 
ATOM   8543  H HG23 . VAL C 1 7   ? 23.623  15.695  39.967  1.00 92.88  ? 7   VAL C HG23 1 
ATOM   8544  N N    . LEU C 1 8   ? 21.056  12.371  37.070  1.00 76.85  ? 8   LEU C N    1 
ATOM   8545  C CA   . LEU C 1 8   ? 20.475  11.876  35.836  1.00 74.54  ? 8   LEU C CA   1 
ATOM   8546  C C    . LEU C 1 8   ? 18.955  11.857  35.939  1.00 74.46  ? 8   LEU C C    1 
ATOM   8547  O O    . LEU C 1 8   ? 18.382  11.800  37.031  1.00 80.01  ? 8   LEU C O    1 
ATOM   8548  C CB   . LEU C 1 8   ? 20.993  10.465  35.521  1.00 75.31  ? 8   LEU C CB   1 
ATOM   8549  C CG   . LEU C 1 8   ? 22.386  10.345  34.901  1.00 81.59  ? 8   LEU C CG   1 
ATOM   8550  C CD1  . LEU C 1 8   ? 23.395  11.237  35.590  1.00 83.20  ? 8   LEU C CD1  1 
ATOM   8551  C CD2  . LEU C 1 8   ? 22.869  8.895   34.936  1.00 82.66  ? 8   LEU C CD2  1 
ATOM   8552  H H    . LEU C 1 8   ? 20.892  11.869  37.749  1.00 92.22  ? 8   LEU C H    1 
ATOM   8553  H HA   . LEU C 1 8   ? 20.715  12.468  35.106  1.00 89.45  ? 8   LEU C HA   1 
ATOM   8554  H HB2  . LEU C 1 8   ? 21.011  9.964   36.352  1.00 90.37  ? 8   LEU C HB2  1 
ATOM   8555  H HB3  . LEU C 1 8   ? 20.372  10.054  34.900  1.00 90.37  ? 8   LEU C HB3  1 
ATOM   8556  H HG   . LEU C 1 8   ? 22.321  10.635  33.978  1.00 97.91  ? 8   LEU C HG   1 
ATOM   8557  H HD11 . LEU C 1 8   ? 24.287  10.988  35.301  1.00 99.84  ? 8   LEU C HD11 1 
ATOM   8558  H HD12 . LEU C 1 8   ? 23.216  12.160  35.351  1.00 99.84  ? 8   LEU C HD12 1 
ATOM   8559  H HD13 . LEU C 1 8   ? 23.314  11.123  36.550  1.00 99.84  ? 8   LEU C HD13 1 
ATOM   8560  H HD21 . LEU C 1 8   ? 23.831  8.880   34.814  1.00 99.20  ? 8   LEU C HD21 1 
ATOM   8561  H HD22 . LEU C 1 8   ? 22.638  8.506   35.793  1.00 99.20  ? 8   LEU C HD22 1 
ATOM   8562  H HD23 . LEU C 1 8   ? 22.437  8.402   34.221  1.00 99.20  ? 8   LEU C HD23 1 
ATOM   8563  N N    . ASP C 1 9   ? 18.309  11.920  34.778  1.00 74.41  ? 9   ASP C N    1 
ATOM   8564  C CA   . ASP C 1 9   ? 16.864  11.775  34.672  1.00 75.45  ? 9   ASP C CA   1 
ATOM   8565  C C    . ASP C 1 9   ? 16.526  10.319  34.381  1.00 75.09  ? 9   ASP C C    1 
ATOM   8566  O O    . ASP C 1 9   ? 17.010  9.749   33.397  1.00 75.10  ? 9   ASP C O    1 
ATOM   8567  C CB   . ASP C 1 9   ? 16.307  12.661  33.559  1.00 76.01  ? 9   ASP C CB   1 
ATOM   8568  C CG   . ASP C 1 9   ? 16.787  14.093  33.653  1.00 80.98  ? 9   ASP C CG   1 
ATOM   8569  O OD1  . ASP C 1 9   ? 17.713  14.376  34.449  1.00 81.53  ? 9   ASP C OD1  1 
ATOM   8570  O OD2  . ASP C 1 9   ? 16.227  14.940  32.922  1.00 82.22  ? 9   ASP C OD2  1 
ATOM   8571  H H    . ASP C 1 9   ? 18.696  12.049  34.021  1.00 89.29  ? 9   ASP C H    1 
ATOM   8572  H HA   . ASP C 1 9   ? 16.454  12.040  35.510  1.00 90.54  ? 9   ASP C HA   1 
ATOM   8573  H HB2  . ASP C 1 9   ? 16.589  12.305  32.702  1.00 91.21  ? 9   ASP C HB2  1 
ATOM   8574  H HB3  . ASP C 1 9   ? 15.338  12.665  33.615  1.00 91.21  ? 9   ASP C HB3  1 
ATOM   8575  N N    . PHE C 1 10  ? 15.673  9.732   35.212  1.00 73.98  ? 10  PHE C N    1 
ATOM   8576  C CA   . PHE C 1 10  ? 15.370  8.311   35.144  1.00 72.90  ? 10  PHE C CA   1 
ATOM   8577  C C    . PHE C 1 10  ? 13.872  8.082   34.997  1.00 72.22  ? 10  PHE C C    1 
ATOM   8578  O O    . PHE C 1 10  ? 13.053  8.890   35.444  1.00 71.88  ? 10  PHE C O    1 
ATOM   8579  C CB   . PHE C 1 10  ? 15.891  7.577   36.403  1.00 73.54  ? 10  PHE C CB   1 
ATOM   8580  C CG   . PHE C 1 10  ? 14.890  7.504   37.531  1.00 73.16  ? 10  PHE C CG   1 
ATOM   8581  C CD1  . PHE C 1 10  ? 13.973  6.466   37.598  1.00 73.02  ? 10  PHE C CD1  1 
ATOM   8582  C CD2  . PHE C 1 10  ? 14.873  8.464   38.528  1.00 74.63  ? 10  PHE C CD2  1 
ATOM   8583  C CE1  . PHE C 1 10  ? 13.056  6.396   38.625  1.00 72.88  ? 10  PHE C CE1  1 
ATOM   8584  C CE2  . PHE C 1 10  ? 13.958  8.398   39.563  1.00 72.88  ? 10  PHE C CE2  1 
ATOM   8585  C CZ   . PHE C 1 10  ? 13.048  7.361   39.607  1.00 74.53  ? 10  PHE C CZ   1 
ATOM   8586  H H    . PHE C 1 10  ? 15.250  10.145  35.836  1.00 88.78  ? 10  PHE C H    1 
ATOM   8587  H HA   . PHE C 1 10  ? 15.799  7.932   34.360  1.00 87.48  ? 10  PHE C HA   1 
ATOM   8588  H HB2  . PHE C 1 10  ? 16.126  6.668   36.158  1.00 88.25  ? 10  PHE C HB2  1 
ATOM   8589  H HB3  . PHE C 1 10  ? 16.674  8.045   36.734  1.00 88.25  ? 10  PHE C HB3  1 
ATOM   8590  H HD1  . PHE C 1 10  ? 13.977  5.808   36.941  1.00 87.63  ? 10  PHE C HD1  1 
ATOM   8591  H HD2  . PHE C 1 10  ? 15.485  9.164   38.501  1.00 89.56  ? 10  PHE C HD2  1 
ATOM   8592  H HE1  . PHE C 1 10  ? 12.443  5.697   38.654  1.00 87.45  ? 10  PHE C HE1  1 
ATOM   8593  H HE2  . PHE C 1 10  ? 13.956  9.049   40.226  1.00 87.45  ? 10  PHE C HE2  1 
ATOM   8594  H HZ   . PHE C 1 10  ? 12.429  7.315   40.300  1.00 89.44  ? 10  PHE C HZ   1 
ATOM   8595  N N    . ILE C 1 11  ? 13.527  6.964   34.365  1.00 73.22  ? 11  ILE C N    1 
ATOM   8596  C CA   . ILE C 1 11  ? 12.156  6.478   34.269  1.00 72.12  ? 11  ILE C CA   1 
ATOM   8597  C C    . ILE C 1 11  ? 12.194  4.989   34.572  1.00 71.97  ? 11  ILE C C    1 
ATOM   8598  O O    . ILE C 1 11  ? 12.917  4.238   33.903  1.00 73.86  ? 11  ILE C O    1 
ATOM   8599  C CB   . ILE C 1 11  ? 11.546  6.730   32.882  1.00 73.20  ? 11  ILE C CB   1 
ATOM   8600  C CG1  . ILE C 1 11  ? 11.605  8.212   32.519  1.00 71.20  ? 11  ILE C CG1  1 
ATOM   8601  C CG2  . ILE C 1 11  ? 10.099  6.243   32.842  1.00 74.44  ? 11  ILE C CG2  1 
ATOM   8602  C CD1  . ILE C 1 11  ? 12.662  8.543   31.486  1.00 74.51  ? 11  ILE C CD1  1 
ATOM   8603  H H    . ILE C 1 11  ? 14.092  6.452   33.968  1.00 87.87  ? 11  ILE C H    1 
ATOM   8604  H HA   . ILE C 1 11  ? 11.599  6.924   34.926  1.00 86.54  ? 11  ILE C HA   1 
ATOM   8605  H HB   . ILE C 1 11  ? 12.070  6.234   32.234  1.00 87.84  ? 11  ILE C HB   1 
ATOM   8606  H HG12 . ILE C 1 11  ? 10.744  8.479   32.159  1.00 85.44  ? 11  ILE C HG12 1 
ATOM   8607  H HG13 . ILE C 1 11  ? 11.803  8.722   33.320  1.00 85.44  ? 11  ILE C HG13 1 
ATOM   8608  H HG21 . ILE C 1 11  ? 9.706   6.489   31.990  1.00 89.33  ? 11  ILE C HG21 1 
ATOM   8609  H HG22 . ILE C 1 11  ? 10.087  5.279   32.946  1.00 89.33  ? 11  ILE C HG22 1 
ATOM   8610  H HG23 . ILE C 1 11  ? 9.605   6.659   33.566  1.00 89.33  ? 11  ILE C HG23 1 
ATOM   8611  H HD11 . ILE C 1 11  ? 12.640  9.496   31.306  1.00 89.41  ? 11  ILE C HD11 1 
ATOM   8612  H HD12 . ILE C 1 11  ? 13.532  8.292   31.833  1.00 89.41  ? 11  ILE C HD12 1 
ATOM   8613  H HD13 . ILE C 1 11  ? 12.474  8.049   30.673  1.00 89.41  ? 11  ILE C HD13 1 
ATOM   8614  N N    . LYS C 1 12  ? 11.433  4.561   35.575  1.00 70.00  ? 12  LYS C N    1 
ATOM   8615  C CA   . LYS C 1 12  ? 11.361  3.151   35.940  1.00 71.48  ? 12  LYS C CA   1 
ATOM   8616  C C    . LYS C 1 12  ? 10.069  2.563   35.387  1.00 72.27  ? 12  LYS C C    1 
ATOM   8617  O O    . LYS C 1 12  ? 8.976   3.044   35.707  1.00 73.98  ? 12  LYS C O    1 
ATOM   8618  C CB   . LYS C 1 12  ? 11.426  2.945   37.452  1.00 72.35  ? 12  LYS C CB   1 
ATOM   8619  C CG   . LYS C 1 12  ? 11.294  1.472   37.841  1.00 75.01  ? 12  LYS C CG   1 
ATOM   8620  C CD   . LYS C 1 12  ? 11.930  1.182   39.186  1.00 78.86  ? 12  LYS C CD   1 
ATOM   8621  C CE   . LYS C 1 12  ? 12.574  -0.199  39.220  1.00 79.02  ? 12  LYS C CE   1 
ATOM   8622  N NZ   . LYS C 1 12  ? 13.105  -0.490  40.584  1.00 76.77  ? 12  LYS C NZ   1 
ATOM   8623  H H    . LYS C 1 12  ? 10.945  5.074   36.063  1.00 84.00  ? 12  LYS C H    1 
ATOM   8624  H HA   . LYS C 1 12  ? 12.119  2.691   35.544  1.00 85.78  ? 12  LYS C HA   1 
ATOM   8625  H HB2  . LYS C 1 12  ? 12.279  3.270   37.781  1.00 86.83  ? 12  LYS C HB2  1 
ATOM   8626  H HB3  . LYS C 1 12  ? 10.701  3.434   37.871  1.00 86.83  ? 12  LYS C HB3  1 
ATOM   8627  H HG2  . LYS C 1 12  ? 10.354  1.238   37.893  1.00 90.02  ? 12  LYS C HG2  1 
ATOM   8628  H HG3  . LYS C 1 12  ? 11.735  0.925   37.173  1.00 90.02  ? 12  LYS C HG3  1 
ATOM   8629  H HD2  . LYS C 1 12  ? 12.618  1.842   39.364  1.00 94.63  ? 12  LYS C HD2  1 
ATOM   8630  H HD3  . LYS C 1 12  ? 11.250  1.217   39.876  1.00 94.63  ? 12  LYS C HD3  1 
ATOM   8631  H HE2  . LYS C 1 12  ? 11.913  -0.872  38.996  1.00 94.83  ? 12  LYS C HE2  1 
ATOM   8632  H HE3  . LYS C 1 12  ? 13.309  -0.232  38.588  1.00 94.83  ? 12  LYS C HE3  1 
ATOM   8633  H HZ1  . LYS C 1 12  ? 13.431  -1.318  40.613  1.00 92.13  ? 12  LYS C HZ1  1 
ATOM   8634  H HZ2  . LYS C 1 12  ? 13.756  0.083   40.786  1.00 92.13  ? 12  LYS C HZ2  1 
ATOM   8635  H HZ3  . LYS C 1 12  ? 12.455  -0.414  41.187  1.00 92.13  ? 12  LYS C HZ3  1 
ATOM   8636  N N    . ILE C 1 13  ? 10.197  1.524   34.565  1.00 72.42  ? 13  ILE C N    1 
ATOM   8637  C CA   . ILE C 1 13  ? 9.076   0.915   33.863  1.00 73.65  ? 13  ILE C CA   1 
ATOM   8638  C C    . ILE C 1 13  ? 9.085   -0.578  34.161  1.00 75.77  ? 13  ILE C C    1 
ATOM   8639  O O    . ILE C 1 13  ? 10.128  -1.162  34.478  1.00 73.97  ? 13  ILE C O    1 
ATOM   8640  C CB   . ILE C 1 13  ? 9.152   1.170   32.346  1.00 71.84  ? 13  ILE C CB   1 
ATOM   8641  C CG1  . ILE C 1 13  ? 9.165   2.673   32.050  1.00 73.05  ? 13  ILE C CG1  1 
ATOM   8642  C CG2  . ILE C 1 13  ? 7.980   0.526   31.630  1.00 73.30  ? 13  ILE C CG2  1 
ATOM   8643  C CD1  . ILE C 1 13  ? 10.120  3.077   30.940  1.00 74.45  ? 13  ILE C CD1  1 
ATOM   8644  H H    . ILE C 1 13  ? 10.949  1.144   34.393  1.00 86.90  ? 13  ILE C H    1 
ATOM   8645  H HA   . ILE C 1 13  ? 8.242   1.287   34.189  1.00 88.39  ? 13  ILE C HA   1 
ATOM   8646  H HB   . ILE C 1 13  ? 9.978   0.775   32.025  1.00 86.21  ? 13  ILE C HB   1 
ATOM   8647  H HG12 . ILE C 1 13  ? 8.272   2.946   31.785  1.00 87.66  ? 13  ILE C HG12 1 
ATOM   8648  H HG13 . ILE C 1 13  ? 9.430   3.146   32.854  1.00 87.66  ? 13  ILE C HG13 1 
ATOM   8649  H HG21 . ILE C 1 13  ? 7.915   0.895   30.736  1.00 87.97  ? 13  ILE C HG21 1 
ATOM   8650  H HG22 . ILE C 1 13  ? 8.127   -0.432  31.583  1.00 87.97  ? 13  ILE C HG22 1 
ATOM   8651  H HG23 . ILE C 1 13  ? 7.167   0.712   32.125  1.00 87.97  ? 13  ILE C HG23 1 
ATOM   8652  H HD11 . ILE C 1 13  ? 10.086  4.040   30.828  1.00 89.34  ? 13  ILE C HD11 1 
ATOM   8653  H HD12 . ILE C 1 13  ? 11.019  2.803   31.182  1.00 89.34  ? 13  ILE C HD12 1 
ATOM   8654  H HD13 . ILE C 1 13  ? 9.851   2.639   30.118  1.00 89.34  ? 13  ILE C HD13 1 
ATOM   8655  N N    . ASN C 1 14  ? 7.906   -1.198  34.063  1.00 75.68  ? 14  ASN C N    1 
ATOM   8656  C CA   . ASN C 1 14  ? 7.731   -2.625  34.315  1.00 76.74  ? 14  ASN C CA   1 
ATOM   8657  C C    . ASN C 1 14  ? 7.137   -3.289  33.078  1.00 77.76  ? 14  ASN C C    1 
ATOM   8658  O O    . ASN C 1 14  ? 5.917   -3.511  33.005  1.00 77.09  ? 14  ASN C O    1 
ATOM   8659  C CB   . ASN C 1 14  ? 6.839   -2.866  35.531  1.00 75.64  ? 14  ASN C CB   1 
ATOM   8660  C CG   . ASN C 1 14  ? 6.535   -4.333  35.738  1.00 76.47  ? 14  ASN C CG   1 
ATOM   8661  O OD1  . ASN C 1 14  ? 7.314   -5.197  35.336  1.00 76.77  ? 14  ASN C OD1  1 
ATOM   8662  N ND2  . ASN C 1 14  ? 5.398   -4.625  36.370  1.00 77.18  ? 14  ASN C ND2  1 
ATOM   8663  H H    . ASN C 1 14  ? 7.175   -0.799  33.846  1.00 90.82  ? 14  ASN C H    1 
ATOM   8664  H HA   . ASN C 1 14  ? 8.604   -3.016  34.476  1.00 92.08  ? 14  ASN C HA   1 
ATOM   8665  H HB2  . ASN C 1 14  ? 7.287   -2.536  36.325  1.00 90.76  ? 14  ASN C HB2  1 
ATOM   8666  H HB3  . ASN C 1 14  ? 5.998   -2.399  35.406  1.00 90.76  ? 14  ASN C HB3  1 
ATOM   8667  H HD21 . ASN C 1 14  ? 4.880   -3.993  36.637  1.00 92.62  ? 14  ASN C HD21 1 
ATOM   8668  H HD22 . ASN C 1 14  ? 5.183   -5.445  36.511  1.00 92.62  ? 14  ASN C HD22 1 
ATOM   8669  N N    . PRO C 1 15  ? 7.971   -3.627  32.083  1.00 78.94  ? 15  PRO C N    1 
ATOM   8670  C CA   . PRO C 1 15  ? 7.462   -4.360  30.916  1.00 77.12  ? 15  PRO C CA   1 
ATOM   8671  C C    . PRO C 1 15  ? 7.368   -5.852  31.181  1.00 77.75  ? 15  PRO C C    1 
ATOM   8672  O O    . PRO C 1 15  ? 8.331   -6.591  30.957  1.00 77.98  ? 15  PRO C O    1 
ATOM   8673  C CB   . PRO C 1 15  ? 8.498   -4.044  29.832  1.00 76.33  ? 15  PRO C CB   1 
ATOM   8674  C CG   . PRO C 1 15  ? 9.779   -3.896  30.598  1.00 76.59  ? 15  PRO C CG   1 
ATOM   8675  C CD   . PRO C 1 15  ? 9.413   -3.328  31.963  1.00 78.74  ? 15  PRO C CD   1 
ATOM   8676  H HA   . PRO C 1 15  ? 6.596   -4.020  30.642  1.00 92.54  ? 15  PRO C HA   1 
ATOM   8677  H HB2  . PRO C 1 15  ? 8.550   -4.774  29.195  1.00 91.59  ? 15  PRO C HB2  1 
ATOM   8678  H HB3  . PRO C 1 15  ? 8.264   -3.221  29.374  1.00 91.59  ? 15  PRO C HB3  1 
ATOM   8679  H HG2  . PRO C 1 15  ? 10.200  -4.765  30.693  1.00 91.91  ? 15  PRO C HG2  1 
ATOM   8680  H HG3  . PRO C 1 15  ? 10.370  -3.290  30.124  1.00 91.91  ? 15  PRO C HG3  1 
ATOM   8681  H HD2  . PRO C 1 15  ? 9.916   -3.767  32.666  1.00 94.48  ? 15  PRO C HD2  1 
ATOM   8682  H HD3  . PRO C 1 15  ? 9.570   -2.371  31.992  1.00 94.48  ? 15  PRO C HD3  1 
ATOM   8683  N N    . ALA C 1 16  ? 6.215   -6.303  31.673  1.00 78.91  ? 16  ALA C N    1 
ATOM   8684  C CA   . ALA C 1 16  ? 5.972   -7.719  31.940  1.00 84.98  ? 16  ALA C CA   1 
ATOM   8685  C C    . ALA C 1 16  ? 7.037   -8.308  32.866  1.00 84.81  ? 16  ALA C C    1 
ATOM   8686  O O    . ALA C 1 16  ? 7.560   -9.401  32.635  1.00 85.72  ? 16  ALA C O    1 
ATOM   8687  C CB   . ALA C 1 16  ? 5.890   -8.513  30.633  1.00 77.23  ? 16  ALA C CB   1 
ATOM   8688  H H    . ALA C 1 16  ? 5.545   -5.798  31.863  1.00 94.69  ? 16  ALA C H    1 
ATOM   8689  H HA   . ALA C 1 16  ? 5.120   -7.796  32.399  1.00 101.97 ? 16  ALA C HA   1 
ATOM   8690  H HB1  . ALA C 1 16  ? 5.686   -9.439  30.838  1.00 92.68  ? 16  ALA C HB1  1 
ATOM   8691  H HB2  . ALA C 1 16  ? 5.191   -8.136  30.077  1.00 92.68  ? 16  ALA C HB2  1 
ATOM   8692  H HB3  . ALA C 1 16  ? 6.744   -8.456  30.175  1.00 92.68  ? 16  ALA C HB3  1 
ATOM   8693  N N    . GLY C 1 17  ? 7.356   -7.573  33.928  1.00 79.34  ? 17  GLY C N    1 
ATOM   8694  C CA   . GLY C 1 17  ? 8.296   -8.042  34.922  1.00 82.57  ? 17  GLY C CA   1 
ATOM   8695  C C    . GLY C 1 17  ? 9.758   -7.841  34.591  1.00 84.40  ? 17  GLY C C    1 
ATOM   8696  O O    . GLY C 1 17  ? 10.607  -8.082  35.457  1.00 84.90  ? 17  GLY C O    1 
ATOM   8697  H H    . GLY C 1 17  ? 7.035   -6.792  34.091  1.00 95.20  ? 17  GLY C H    1 
ATOM   8698  H HA2  . GLY C 1 17  ? 8.119   -7.579  35.755  1.00 99.09  ? 17  GLY C HA2  1 
ATOM   8699  H HA3  . GLY C 1 17  ? 8.155   -8.993  35.053  1.00 99.09  ? 17  GLY C HA3  1 
ATOM   8700  N N    . ASN C 1 18  ? 10.087  -7.406  33.373  1.00 82.67  ? 18  ASN C N    1 
ATOM   8701  C CA   . ASN C 1 18  ? 11.475  -7.164  32.972  1.00 81.75  ? 18  ASN C CA   1 
ATOM   8702  C C    . ASN C 1 18  ? 11.835  -5.718  33.312  1.00 81.58  ? 18  ASN C C    1 
ATOM   8703  O O    . ASN C 1 18  ? 11.920  -4.840  32.449  1.00 77.93  ? 18  ASN C O    1 
ATOM   8704  C CB   . ASN C 1 18  ? 11.653  -7.460  31.487  1.00 83.13  ? 18  ASN C CB   1 
ATOM   8705  C CG   . ASN C 1 18  ? 13.093  -7.766  31.117  1.00 83.72  ? 18  ASN C CG   1 
ATOM   8706  O OD1  . ASN C 1 18  ? 13.969  -7.836  31.980  1.00 88.79  ? 18  ASN C OD1  1 
ATOM   8707  N ND2  . ASN C 1 18  ? 13.344  -7.948  29.830  1.00 80.58  ? 18  ASN C ND2  1 
ATOM   8708  H H    . ASN C 1 18  ? 9.515   -7.243  32.751  1.00 99.21  ? 18  ASN C H    1 
ATOM   8709  H HA   . ASN C 1 18  ? 12.062  -7.748  33.477  1.00 98.10  ? 18  ASN C HA   1 
ATOM   8710  H HB2  . ASN C 1 18  ? 11.113  -8.230  31.252  1.00 99.75  ? 18  ASN C HB2  1 
ATOM   8711  H HB3  . ASN C 1 18  ? 11.370  -6.687  30.974  1.00 99.75  ? 18  ASN C HB3  1 
ATOM   8712  H HD21 . ASN C 1 18  ? 12.707  -7.890  29.255  1.00 96.69  ? 18  ASN C HD21 1 
ATOM   8713  H HD22 . ASN C 1 18  ? 14.144  -8.124  29.568  1.00 96.69  ? 18  ASN C HD22 1 
ATOM   8714  N N    . ILE C 1 19  ? 12.072  -5.481  34.609  1.00 85.24  ? 19  ILE C N    1 
ATOM   8715  C CA   . ILE C 1 19  ? 12.236  -4.125  35.121  1.00 76.66  ? 19  ILE C CA   1 
ATOM   8716  C C    . ILE C 1 19  ? 13.301  -3.388  34.321  1.00 76.83  ? 19  ILE C C    1 
ATOM   8717  O O    . ILE C 1 19  ? 14.435  -3.858  34.178  1.00 76.87  ? 19  ILE C O    1 
ATOM   8718  C CB   . ILE C 1 19  ? 12.588  -4.161  36.618  1.00 81.30  ? 19  ILE C CB   1 
ATOM   8719  C CG1  . ILE C 1 19  ? 11.547  -4.968  37.398  1.00 81.69  ? 19  ILE C CG1  1 
ATOM   8720  C CG2  . ILE C 1 19  ? 12.693  -2.745  37.182  1.00 76.43  ? 19  ILE C CG2  1 
ATOM   8721  C CD1  . ILE C 1 19  ? 10.113  -4.724  36.961  1.00 81.56  ? 19  ILE C CD1  1 
ATOM   8722  H H    . ILE C 1 19  ? 12.142  -6.093  35.210  1.00 102.29 ? 19  ILE C H    1 
ATOM   8723  H HA   . ILE C 1 19  ? 11.397  -3.652  35.011  1.00 91.99  ? 19  ILE C HA   1 
ATOM   8724  H HB   . ILE C 1 19  ? 13.450  -4.597  36.712  1.00 97.56  ? 19  ILE C HB   1 
ATOM   8725  H HG12 . ILE C 1 19  ? 11.734  -5.912  37.279  1.00 98.03  ? 19  ILE C HG12 1 
ATOM   8726  H HG13 . ILE C 1 19  ? 11.612  -4.733  38.337  1.00 98.03  ? 19  ILE C HG13 1 
ATOM   8727  H HG21 . ILE C 1 19  ? 12.818  -2.796  38.143  1.00 91.72  ? 19  ILE C HG21 1 
ATOM   8728  H HG22 . ILE C 1 19  ? 13.450  -2.297  36.774  1.00 91.72  ? 19  ILE C HG22 1 
ATOM   8729  H HG23 . ILE C 1 19  ? 11.876  -2.263  36.980  1.00 91.72  ? 19  ILE C HG23 1 
ATOM   8730  H HD11 . ILE C 1 19  ? 9.512   -5.081  37.634  1.00 97.87  ? 19  ILE C HD11 1 
ATOM   8731  H HD12 . ILE C 1 19  ? 9.970   -3.769  36.863  1.00 97.87  ? 19  ILE C HD12 1 
ATOM   8732  H HD13 . ILE C 1 19  ? 9.961   -5.169  36.113  1.00 97.87  ? 19  ILE C HD13 1 
ATOM   8733  N N    . THR C 1 20  ? 12.935  -2.211  33.812  1.00 76.51  ? 20  THR C N    1 
ATOM   8734  C CA   . THR C 1 20  ? 13.778  -1.411  32.939  1.00 73.32  ? 20  THR C CA   1 
ATOM   8735  C C    . THR C 1 20  ? 13.917  -0.011  33.514  1.00 72.79  ? 20  THR C C    1 
ATOM   8736  O O    . THR C 1 20  ? 12.955  0.551   34.048  1.00 72.21  ? 20  THR C O    1 
ATOM   8737  C CB   . THR C 1 20  ? 13.182  -1.333  31.523  1.00 76.38  ? 20  THR C CB   1 
ATOM   8738  O OG1  . THR C 1 20  ? 12.590  -2.597  31.179  1.00 76.84  ? 20  THR C OG1  1 
ATOM   8739  C CG2  . THR C 1 20  ? 14.244  -0.979  30.490  1.00 76.93  ? 20  THR C CG2  1 
ATOM   8740  H H    . THR C 1 20  ? 12.172  -1.846  33.967  1.00 91.81  ? 20  THR C H    1 
ATOM   8741  H HA   . THR C 1 20  ? 14.662  -1.806  32.882  1.00 87.98  ? 20  THR C HA   1 
ATOM   8742  H HB   . THR C 1 20  ? 12.506  -0.638  31.506  1.00 91.65  ? 20  THR C HB   1 
ATOM   8743  H HG1  . THR C 1 20  ? 12.993  -3.220  31.573  1.00 92.21  ? 20  THR C HG1  1 
ATOM   8744  H HG21 . THR C 1 20  ? 15.041  -0.648  30.933  1.00 92.31  ? 20  THR C HG21 1 
ATOM   8745  H HG22 . THR C 1 20  ? 13.909  -0.294  29.890  1.00 92.31  ? 20  THR C HG22 1 
ATOM   8746  H HG23 . THR C 1 20  ? 14.477  -1.765  29.970  1.00 92.31  ? 20  THR C HG23 1 
ATOM   8747  N N    . ILE C 1 21  ? 15.124  0.539   33.420  1.00 73.12  ? 21  ILE C N    1 
ATOM   8748  C CA   . ILE C 1 21  ? 15.388  1.938   33.735  1.00 74.80  ? 21  ILE C CA   1 
ATOM   8749  C C    . ILE C 1 21  ? 15.847  2.611   32.443  1.00 73.73  ? 21  ILE C C    1 
ATOM   8750  O O    . ILE C 1 21  ? 16.815  2.160   31.811  1.00 71.69  ? 21  ILE C O    1 
ATOM   8751  C CB   . ILE C 1 21  ? 16.447  2.100   34.838  1.00 72.23  ? 21  ILE C CB   1 
ATOM   8752  C CG1  . ILE C 1 21  ? 15.957  1.539   36.184  1.00 77.09  ? 21  ILE C CG1  1 
ATOM   8753  C CG2  . ILE C 1 21  ? 16.847  3.569   34.984  1.00 70.07  ? 21  ILE C CG2  1 
ATOM   8754  C CD1  . ILE C 1 21  ? 14.521  1.881   36.559  1.00 76.35  ? 21  ILE C CD1  1 
ATOM   8755  H H    . ILE C 1 21  ? 15.825  0.109   33.168  1.00 87.75  ? 21  ILE C H    1 
ATOM   8756  H HA   . ILE C 1 21  ? 14.570  2.358   34.043  1.00 89.76  ? 21  ILE C HA   1 
ATOM   8757  H HB   . ILE C 1 21  ? 17.225  1.586   34.571  1.00 86.68  ? 21  ILE C HB   1 
ATOM   8758  H HG12 . ILE C 1 21  ? 16.024  0.572   36.153  1.00 92.51  ? 21  ILE C HG12 1 
ATOM   8759  H HG13 . ILE C 1 21  ? 16.529  1.889   36.885  1.00 92.51  ? 21  ILE C HG13 1 
ATOM   8760  H HG21 . ILE C 1 21  ? 17.491  3.651   35.704  1.00 84.09  ? 21  ILE C HG21 1 
ATOM   8761  H HG22 . ILE C 1 21  ? 17.241  3.874   34.151  1.00 84.09  ? 21  ILE C HG22 1 
ATOM   8762  H HG23 . ILE C 1 21  ? 16.056  4.093   35.186  1.00 84.09  ? 21  ILE C HG23 1 
ATOM   8763  H HD11 . ILE C 1 21  ? 14.336  1.539   37.447  1.00 91.62  ? 21  ILE C HD11 1 
ATOM   8764  H HD12 . ILE C 1 21  ? 14.412  2.845   36.547  1.00 91.62  ? 21  ILE C HD12 1 
ATOM   8765  H HD13 . ILE C 1 21  ? 13.921  1.473   35.916  1.00 91.62  ? 21  ILE C HD13 1 
ATOM   8766  N N    . LEU C 1 22  ? 15.149  3.671   32.048  1.00 72.76  ? 22  LEU C N    1 
ATOM   8767  C CA   . LEU C 1 22  ? 15.533  4.491   30.907  1.00 72.81  ? 22  LEU C CA   1 
ATOM   8768  C C    . LEU C 1 22  ? 16.092  5.809   31.426  1.00 74.89  ? 22  LEU C C    1 
ATOM   8769  O O    . LEU C 1 22  ? 15.472  6.460   32.276  1.00 71.82  ? 22  LEU C O    1 
ATOM   8770  C CB   . LEU C 1 22  ? 14.341  4.740   29.987  1.00 72.44  ? 22  LEU C CB   1 
ATOM   8771  C CG   . LEU C 1 22  ? 13.620  3.485   29.492  1.00 73.16  ? 22  LEU C CG   1 
ATOM   8772  C CD1  . LEU C 1 22  ? 12.375  3.855   28.697  1.00 73.60  ? 22  LEU C CD1  1 
ATOM   8773  C CD2  . LEU C 1 22  ? 14.551  2.622   28.651  1.00 73.29  ? 22  LEU C CD2  1 
ATOM   8774  H H    . LEU C 1 22  ? 14.431  3.941   32.436  1.00 87.31  ? 22  LEU C H    1 
ATOM   8775  H HA   . LEU C 1 22  ? 16.219  4.043   30.389  1.00 87.37  ? 22  LEU C HA   1 
ATOM   8776  H HB2  . LEU C 1 22  ? 13.691  5.276   30.468  1.00 86.93  ? 22  LEU C HB2  1 
ATOM   8777  H HB3  . LEU C 1 22  ? 14.654  5.221   29.205  1.00 86.93  ? 22  LEU C HB3  1 
ATOM   8778  H HG   . LEU C 1 22  ? 13.342  2.964   30.262  1.00 87.79  ? 22  LEU C HG   1 
ATOM   8779  H HD11 . LEU C 1 22  ? 11.862  3.051   28.521  1.00 88.32  ? 22  LEU C HD11 1 
ATOM   8780  H HD12 . LEU C 1 22  ? 11.844  4.480   29.216  1.00 88.32  ? 22  LEU C HD12 1 
ATOM   8781  H HD13 . LEU C 1 22  ? 12.645  4.266   27.861  1.00 88.32  ? 22  LEU C HD13 1 
ATOM   8782  H HD21 . LEU C 1 22  ? 14.047  1.881   28.281  1.00 87.94  ? 22  LEU C HD21 1 
ATOM   8783  H HD22 . LEU C 1 22  ? 14.920  3.162   27.934  1.00 87.94  ? 22  LEU C HD22 1 
ATOM   8784  H HD23 . LEU C 1 22  ? 15.266  2.287   29.215  1.00 87.94  ? 22  LEU C HD23 1 
ATOM   8785  N N    . ILE C 1 23  ? 17.271  6.181   30.942  1.00 76.27  ? 23  ILE C N    1 
ATOM   8786  C CA   . ILE C 1 23  ? 17.891  7.458   31.277  1.00 76.60  ? 23  ILE C CA   1 
ATOM   8787  C C    . ILE C 1 23  ? 17.625  8.430   30.137  1.00 76.00  ? 23  ILE C C    1 
ATOM   8788  O O    . ILE C 1 23  ? 17.771  8.079   28.957  1.00 78.54  ? 23  ILE C O    1 
ATOM   8789  C CB   . ILE C 1 23  ? 19.402  7.306   31.530  1.00 77.78  ? 23  ILE C CB   1 
ATOM   8790  C CG1  . ILE C 1 23  ? 19.669  6.245   32.601  1.00 74.70  ? 23  ILE C CG1  1 
ATOM   8791  C CG2  . ILE C 1 23  ? 20.005  8.644   31.949  1.00 77.01  ? 23  ILE C CG2  1 
ATOM   8792  C CD1  . ILE C 1 23  ? 18.671  6.234   33.746  1.00 76.12  ? 23  ILE C CD1  1 
ATOM   8793  H H    . ILE C 1 23  ? 17.742  5.701   30.406  1.00 91.53  ? 23  ILE C H    1 
ATOM   8794  H HA   . ILE C 1 23  ? 17.489  7.805   32.088  1.00 91.91  ? 23  ILE C HA   1 
ATOM   8795  H HB   . ILE C 1 23  ? 19.819  7.016   30.704  1.00 93.34  ? 23  ILE C HB   1 
ATOM   8796  H HG12 . ILE C 1 23  ? 19.643  5.370   32.182  1.00 89.64  ? 23  ILE C HG12 1 
ATOM   8797  H HG13 . ILE C 1 23  ? 20.548  6.405   32.981  1.00 89.64  ? 23  ILE C HG13 1 
ATOM   8798  H HG21 . ILE C 1 23  ? 20.953  8.524   32.118  1.00 92.41  ? 23  ILE C HG21 1 
ATOM   8799  H HG22 . ILE C 1 23  ? 19.876  9.286   31.233  1.00 92.41  ? 23  ILE C HG22 1 
ATOM   8800  H HG23 . ILE C 1 23  ? 19.562  8.953   32.754  1.00 92.41  ? 23  ILE C HG23 1 
ATOM   8801  H HD11 . ILE C 1 23  ? 18.949  5.574   34.401  1.00 91.35  ? 23  ILE C HD11 1 
ATOM   8802  H HD12 . ILE C 1 23  ? 18.647  7.114   34.152  1.00 91.35  ? 23  ILE C HD12 1 
ATOM   8803  H HD13 . ILE C 1 23  ? 17.795  6.006   33.398  1.00 91.35  ? 23  ILE C HD13 1 
ATOM   8804  N N    . ASP C 1 24  ? 17.241  9.654   30.486  1.00 78.27  ? 24  ASP C N    1 
ATOM   8805  C CA   . ASP C 1 24  ? 16.850  10.676  29.526  1.00 75.24  ? 24  ASP C CA   1 
ATOM   8806  C C    . ASP C 1 24  ? 17.885  11.793  29.489  1.00 73.83  ? 24  ASP C C    1 
ATOM   8807  O O    . ASP C 1 24  ? 18.541  12.090  30.491  1.00 74.77  ? 24  ASP C O    1 
ATOM   8808  C CB   . ASP C 1 24  ? 15.481  11.256  29.893  1.00 74.04  ? 24  ASP C CB   1 
ATOM   8809  C CG   . ASP C 1 24  ? 14.608  11.512  28.686  1.00 75.94  ? 24  ASP C CG   1 
ATOM   8810  O OD1  . ASP C 1 24  ? 15.037  11.209  27.556  1.00 79.23  ? 24  ASP C OD1  1 
ATOM   8811  O OD2  . ASP C 1 24  ? 13.483  12.019  28.866  1.00 81.15  ? 24  ASP C OD2  1 
ATOM   8812  H H    . ASP C 1 24  ? 17.198  9.924   31.301  1.00 93.93  ? 24  ASP C H    1 
ATOM   8813  H HA   . ASP C 1 24  ? 16.799  10.287  28.638  1.00 90.28  ? 24  ASP C HA   1 
ATOM   8814  H HB2  . ASP C 1 24  ? 15.017  10.629  30.470  1.00 88.85  ? 24  ASP C HB2  1 
ATOM   8815  H HB3  . ASP C 1 24  ? 15.609  12.099  30.355  1.00 88.85  ? 24  ASP C HB3  1 
ATOM   8816  N N    . ASN C 1 25  ? 18.030  12.405  28.316  1.00 73.68  ? 25  ASN C N    1 
ATOM   8817  C CA   . ASN C 1 25  ? 18.848  13.606  28.147  1.00 70.68  ? 25  ASN C CA   1 
ATOM   8818  C C    . ASN C 1 25  ? 20.318  13.355  28.464  1.00 69.99  ? 25  ASN C C    1 
ATOM   8819  O O    . ASN C 1 25  ? 21.035  14.259  28.899  1.00 71.62  ? 25  ASN C O    1 
ATOM   8820  C CB   . ASN C 1 25  ? 18.302  14.748  29.008  1.00 71.95  ? 25  ASN C CB   1 
ATOM   8821  C CG   . ASN C 1 25  ? 16.842  15.035  28.731  1.00 75.36  ? 25  ASN C CG   1 
ATOM   8822  O OD1  . ASN C 1 25  ? 16.009  15.022  29.640  1.00 72.84  ? 25  ASN C OD1  1 
ATOM   8823  N ND2  . ASN C 1 25  ? 16.521  15.282  27.466  1.00 75.34  ? 25  ASN C ND2  1 
ATOM   8824  H H    . ASN C 1 25  ? 17.658  12.139  27.588  1.00 88.42  ? 25  ASN C H    1 
ATOM   8825  H HA   . ASN C 1 25  ? 18.808  13.873  27.215  1.00 84.81  ? 25  ASN C HA   1 
ATOM   8826  H HB2  . ASN C 1 25  ? 18.390  14.510  29.944  1.00 86.34  ? 25  ASN C HB2  1 
ATOM   8827  H HB3  . ASN C 1 25  ? 18.808  15.555  28.822  1.00 86.34  ? 25  ASN C HB3  1 
ATOM   8828  H HD21 . ASN C 1 25  ? 17.130  15.273  26.858  1.00 90.40  ? 25  ASN C HD21 1 
ATOM   8829  H HD22 . ASN C 1 25  ? 15.705  15.450  27.255  1.00 90.40  ? 25  ASN C HD22 1 
ATOM   8830  N N    . PHE C 1 26  ? 20.780  12.133  28.235  1.00 71.54  ? 26  PHE C N    1 
ATOM   8831  C CA   . PHE C 1 26  ? 22.163  11.747  28.464  1.00 75.11  ? 26  PHE C CA   1 
ATOM   8832  C C    . PHE C 1 26  ? 22.826  11.427  27.129  1.00 76.40  ? 26  PHE C C    1 
ATOM   8833  O O    . PHE C 1 26  ? 22.156  11.072  26.155  1.00 76.58  ? 26  PHE C O    1 
ATOM   8834  C CB   . PHE C 1 26  ? 22.236  10.537  29.404  1.00 74.61  ? 26  PHE C CB   1 
ATOM   8835  C CG   . PHE C 1 26  ? 23.575  10.354  30.058  1.00 73.47  ? 26  PHE C CG   1 
ATOM   8836  C CD1  . PHE C 1 26  ? 23.917  11.084  31.182  1.00 77.85  ? 26  PHE C CD1  1 
ATOM   8837  C CD2  . PHE C 1 26  ? 24.493  9.450   29.550  1.00 77.86  ? 26  PHE C CD2  1 
ATOM   8838  C CE1  . PHE C 1 26  ? 25.148  10.919  31.785  1.00 79.20  ? 26  PHE C CE1  1 
ATOM   8839  C CE2  . PHE C 1 26  ? 25.727  9.282   30.148  1.00 79.60  ? 26  PHE C CE2  1 
ATOM   8840  C CZ   . PHE C 1 26  ? 26.053  10.016  31.267  1.00 83.83  ? 26  PHE C CZ   1 
ATOM   8841  H H    . PHE C 1 26  ? 20.294  11.489  27.937  1.00 85.84  ? 26  PHE C H    1 
ATOM   8842  H HA   . PHE C 1 26  ? 22.655  12.474  28.877  1.00 90.14  ? 26  PHE C HA   1 
ATOM   8843  H HB2  . PHE C 1 26  ? 21.578  10.650  30.107  1.00 89.53  ? 26  PHE C HB2  1 
ATOM   8844  H HB3  . PHE C 1 26  ? 22.044  9.735   28.894  1.00 89.53  ? 26  PHE C HB3  1 
ATOM   8845  H HD1  . PHE C 1 26  ? 23.310  11.693  31.535  1.00 93.42  ? 26  PHE C HD1  1 
ATOM   8846  H HD2  . PHE C 1 26  ? 24.275  8.950   28.797  1.00 93.43  ? 26  PHE C HD2  1 
ATOM   8847  H HE1  . PHE C 1 26  ? 25.367  11.417  32.540  1.00 95.04  ? 26  PHE C HE1  1 
ATOM   8848  H HE2  . PHE C 1 26  ? 26.336  8.675   29.795  1.00 95.53  ? 26  PHE C HE2  1 
ATOM   8849  H HZ   . PHE C 1 26  ? 26.882  9.902   31.673  1.00 100.59 ? 26  PHE C HZ   1 
ATOM   8850  N N    . ASP C 1 27  ? 24.148  11.577  27.085  1.00 76.35  ? 27  ASP C N    1 
ATOM   8851  C CA   . ASP C 1 27  ? 24.927  11.216  25.905  1.00 76.24  ? 27  ASP C CA   1 
ATOM   8852  C C    . ASP C 1 27  ? 24.900  9.702   25.745  1.00 81.28  ? 27  ASP C C    1 
ATOM   8853  O O    . ASP C 1 27  ? 25.542  8.979   26.515  1.00 82.64  ? 27  ASP C O    1 
ATOM   8854  C CB   . ASP C 1 27  ? 26.353  11.737  26.042  1.00 78.52  ? 27  ASP C CB   1 
ATOM   8855  C CG   . ASP C 1 27  ? 27.265  11.267  24.922  1.00 86.59  ? 27  ASP C CG   1 
ATOM   8856  O OD1  . ASP C 1 27  ? 26.770  10.752  23.890  1.00 83.48  ? 27  ASP C OD1  1 
ATOM   8857  O OD2  . ASP C 1 27  ? 28.494  11.420  25.077  1.00 91.82  ? 27  ASP C OD2  1 
ATOM   8858  H H    . ASP C 1 27  ? 24.620  11.890  27.732  1.00 91.62  ? 27  ASP C H    1 
ATOM   8859  H HA   . ASP C 1 27  ? 24.538  11.618  25.113  1.00 91.49  ? 27  ASP C HA   1 
ATOM   8860  H HB2  . ASP C 1 27  ? 26.337  12.707  26.028  1.00 94.23  ? 27  ASP C HB2  1 
ATOM   8861  H HB3  . ASP C 1 27  ? 26.724  11.424  26.882  1.00 94.23  ? 27  ASP C HB3  1 
ATOM   8862  N N    . ILE C 1 28  ? 24.138  9.220   24.748  1.00 79.30  ? 28  ILE C N    1 
ATOM   8863  C CA   . ILE C 1 28  ? 23.913  7.780   24.598  1.00 77.46  ? 28  ILE C CA   1 
ATOM   8864  C C    . ILE C 1 28  ? 25.129  7.047   24.089  1.00 81.11  ? 28  ILE C C    1 
ATOM   8865  O O    . ILE C 1 28  ? 25.064  5.821   23.915  1.00 82.35  ? 28  ILE C O    1 
ATOM   8866  C CB   . ILE C 1 28  ? 22.709  7.532   23.657  1.00 79.08  ? 28  ILE C CB   1 
ATOM   8867  C CG1  . ILE C 1 28  ? 23.141  7.639   22.197  1.00 78.23  ? 28  ILE C CG1  1 
ATOM   8868  C CG2  . ILE C 1 28  ? 21.575  8.519   23.971  1.00 77.10  ? 28  ILE C CG2  1 
ATOM   8869  C CD1  . ILE C 1 28  ? 21.996  7.618   21.195  1.00 75.65  ? 28  ILE C CD1  1 
ATOM   8870  H H    . ILE C 1 28  ? 23.746  9.704   24.155  1.00 95.16  ? 28  ILE C H    1 
ATOM   8871  H HA   . ILE C 1 28  ? 23.707  7.405   25.468  1.00 92.95  ? 28  ILE C HA   1 
ATOM   8872  H HB   . ILE C 1 28  ? 22.380  6.632   23.806  1.00 94.90  ? 28  ILE C HB   1 
ATOM   8873  H HG12 . ILE C 1 28  ? 23.619  8.475   22.076  1.00 93.87  ? 28  ILE C HG12 1 
ATOM   8874  H HG13 . ILE C 1 28  ? 23.723  6.891   21.991  1.00 93.87  ? 28  ILE C HG13 1 
ATOM   8875  H HG21 . ILE C 1 28  ? 20.749  8.183   23.588  1.00 92.52  ? 28  ILE C HG21 1 
ATOM   8876  H HG22 . ILE C 1 28  ? 21.484  8.599   24.934  1.00 92.52  ? 28  ILE C HG22 1 
ATOM   8877  H HG23 . ILE C 1 28  ? 21.791  9.382   23.586  1.00 92.52  ? 28  ILE C HG23 1 
ATOM   8878  H HD11 . ILE C 1 28  ? 22.360  7.524   20.301  1.00 90.78  ? 28  ILE C HD11 1 
ATOM   8879  H HD12 . ILE C 1 28  ? 21.415  6.867   21.396  1.00 90.78  ? 28  ILE C HD12 1 
ATOM   8880  H HD13 . ILE C 1 28  ? 21.500  8.448   21.265  1.00 90.78  ? 28  ILE C HD13 1 
ATOM   8881  N N    . TYR C 1 29  ? 26.229  7.741   23.844  1.00 81.64  ? 29  TYR C N    1 
ATOM   8882  C CA   . TYR C 1 29  ? 27.477  7.137   23.413  1.00 81.76  ? 29  TYR C CA   1 
ATOM   8883  C C    . TYR C 1 29  ? 28.599  7.464   24.396  1.00 86.01  ? 29  TYR C C    1 
ATOM   8884  O O    . TYR C 1 29  ? 29.752  7.656   24.008  1.00 86.58  ? 29  TYR C O    1 
ATOM   8885  C CB   . TYR C 1 29  ? 27.839  7.596   22.003  1.00 83.50  ? 29  TYR C CB   1 
ATOM   8886  C CG   . TYR C 1 29  ? 26.880  7.123   20.928  1.00 80.77  ? 29  TYR C CG   1 
ATOM   8887  C CD1  . TYR C 1 29  ? 26.521  5.783   20.828  1.00 81.17  ? 29  TYR C CD1  1 
ATOM   8888  C CD2  . TYR C 1 29  ? 26.338  8.016   20.008  1.00 77.45  ? 29  TYR C CD2  1 
ATOM   8889  C CE1  . TYR C 1 29  ? 25.645  5.345   19.843  1.00 79.19  ? 29  TYR C CE1  1 
ATOM   8890  C CE2  . TYR C 1 29  ? 25.464  7.585   19.020  1.00 78.74  ? 29  TYR C CE2  1 
ATOM   8891  C CZ   . TYR C 1 29  ? 25.121  6.250   18.944  1.00 79.11  ? 29  TYR C CZ   1 
ATOM   8892  O OH   . TYR C 1 29  ? 24.250  5.819   17.963  1.00 74.85  ? 29  TYR C OH   1 
ATOM   8893  H H    . TYR C 1 29  ? 26.278  8.596   23.924  1.00 97.97  ? 29  TYR C H    1 
ATOM   8894  H HA   . TYR C 1 29  ? 27.369  6.173   23.394  1.00 98.11  ? 29  TYR C HA   1 
ATOM   8895  H HB2  . TYR C 1 29  ? 27.845  8.566   21.985  1.00 100.20 ? 29  TYR C HB2  1 
ATOM   8896  H HB3  . TYR C 1 29  ? 28.719  7.254   21.783  1.00 100.20 ? 29  TYR C HB3  1 
ATOM   8897  H HD1  . TYR C 1 29  ? 26.873  5.170   21.432  1.00 97.40  ? 29  TYR C HD1  1 
ATOM   8898  H HD2  . TYR C 1 29  ? 26.566  8.917   20.056  1.00 92.94  ? 29  TYR C HD2  1 
ATOM   8899  H HE1  . TYR C 1 29  ? 25.413  4.446   19.791  1.00 95.02  ? 29  TYR C HE1  1 
ATOM   8900  H HE2  . TYR C 1 29  ? 25.110  8.194   18.412  1.00 94.49  ? 29  TYR C HE2  1 
ATOM   8901  H HH   . TYR C 1 29  ? 23.996  6.471   17.498  1.00 89.82  ? 29  TYR C HH   1 
ATOM   8902  N N    . ASP C 1 30  ? 28.268  7.527   25.685  1.00 85.83  ? 30  ASP C N    1 
ATOM   8903  C CA   . ASP C 1 30  ? 29.260  7.765   26.728  1.00 88.52  ? 30  ASP C CA   1 
ATOM   8904  C C    . ASP C 1 30  ? 30.027  6.483   27.023  1.00 89.54  ? 30  ASP C C    1 
ATOM   8905  O O    . ASP C 1 30  ? 29.449  5.393   27.059  1.00 89.33  ? 30  ASP C O    1 
ATOM   8906  C CB   . ASP C 1 30  ? 28.576  8.271   28.002  1.00 92.87  ? 30  ASP C CB   1 
ATOM   8907  C CG   . ASP C 1 30  ? 29.501  9.099   28.887  1.00 90.95  ? 30  ASP C CG   1 
ATOM   8908  O OD1  . ASP C 1 30  ? 30.224  8.510   29.716  1.00 90.51  ? 30  ASP C OD1  1 
ATOM   8909  O OD2  . ASP C 1 30  ? 29.489  10.344  28.768  1.00 94.35  ? 30  ASP C OD2  1 
ATOM   8910  H H    . ASP C 1 30  ? 27.467  7.433   25.984  1.00 103.00 ? 30  ASP C H    1 
ATOM   8911  H HA   . ASP C 1 30  ? 29.891  8.441   26.434  1.00 106.23 ? 30  ASP C HA   1 
ATOM   8912  H HB2  . ASP C 1 30  ? 27.822  8.828   27.755  1.00 111.45 ? 30  ASP C HB2  1 
ATOM   8913  H HB3  . ASP C 1 30  ? 28.271  7.509   28.519  1.00 111.45 ? 30  ASP C HB3  1 
ATOM   8914  N N    . LYS C 1 31  ? 31.342  6.615   27.223  1.00 91.36  ? 31  LYS C N    1 
ATOM   8915  C CA   . LYS C 1 31  ? 32.142  5.452   27.594  1.00 93.81  ? 31  LYS C CA   1 
ATOM   8916  C C    . LYS C 1 31  ? 31.657  4.860   28.911  1.00 90.59  ? 31  LYS C C    1 
ATOM   8917  O O    . LYS C 1 31  ? 31.623  3.635   29.073  1.00 90.62  ? 31  LYS C O    1 
ATOM   8918  C CB   . LYS C 1 31  ? 33.624  5.835   27.686  1.00 97.24  ? 31  LYS C CB   1 
ATOM   8919  C CG   . LYS C 1 31  ? 34.465  4.935   28.598  1.00 101.13 ? 31  LYS C CG   1 
ATOM   8920  C CD   . LYS C 1 31  ? 35.787  5.603   29.007  1.00 105.62 ? 31  LYS C CD   1 
ATOM   8921  C CE   . LYS C 1 31  ? 36.530  4.804   30.081  1.00 110.71 ? 31  LYS C CE   1 
ATOM   8922  N NZ   . LYS C 1 31  ? 36.163  3.355   30.102  1.00 109.61 ? 31  LYS C NZ   1 
ATOM   8923  H H    . LYS C 1 31  ? 31.782  7.350   27.152  1.00 109.63 ? 31  LYS C H    1 
ATOM   8924  H HA   . LYS C 1 31  ? 32.055  4.776   26.904  1.00 112.57 ? 31  LYS C HA   1 
ATOM   8925  H HB2  . LYS C 1 31  ? 34.009  5.791   26.797  1.00 116.69 ? 31  LYS C HB2  1 
ATOM   8926  H HB3  . LYS C 1 31  ? 33.687  6.739   28.031  1.00 116.69 ? 31  LYS C HB3  1 
ATOM   8927  H HG2  . LYS C 1 31  ? 33.963  4.739   29.405  1.00 121.36 ? 31  LYS C HG2  1 
ATOM   8928  H HG3  . LYS C 1 31  ? 34.674  4.111   28.130  1.00 121.36 ? 31  LYS C HG3  1 
ATOM   8929  H HD2  . LYS C 1 31  ? 36.363  5.672   28.229  1.00 126.75 ? 31  LYS C HD2  1 
ATOM   8930  H HD3  . LYS C 1 31  ? 35.601  6.486   29.362  1.00 126.75 ? 31  LYS C HD3  1 
ATOM   8931  H HE2  . LYS C 1 31  ? 37.484  4.866   29.916  1.00 132.85 ? 31  LYS C HE2  1 
ATOM   8932  H HE3  . LYS C 1 31  ? 36.319  5.176   30.952  1.00 132.85 ? 31  LYS C HE3  1 
ATOM   8933  H HZ1  . LYS C 1 31  ? 36.630  2.932   30.730  1.00 131.53 ? 31  LYS C HZ1  1 
ATOM   8934  H HZ2  . LYS C 1 31  ? 35.295  3.264   30.278  1.00 131.53 ? 31  LYS C HZ2  1 
ATOM   8935  H HZ3  . LYS C 1 31  ? 36.338  2.985   29.312  1.00 131.53 ? 31  LYS C HZ3  1 
ATOM   8936  N N    . ASN C 1 32  ? 31.300  5.717   29.871  1.00 91.05  ? 32  ASN C N    1 
ATOM   8937  C CA   . ASN C 1 32  ? 30.910  5.278   31.203  1.00 90.05  ? 32  ASN C CA   1 
ATOM   8938  C C    . ASN C 1 32  ? 29.526  4.649   31.246  1.00 87.69  ? 32  ASN C C    1 
ATOM   8939  O O    . ASN C 1 32  ? 29.093  4.234   32.327  1.00 87.16  ? 32  ASN C O    1 
ATOM   8940  C CB   . ASN C 1 32  ? 30.964  6.468   32.165  1.00 92.49  ? 32  ASN C CB   1 
ATOM   8941  C CG   . ASN C 1 32  ? 32.335  7.118   32.215  1.00 94.49  ? 32  ASN C CG   1 
ATOM   8942  O OD1  . ASN C 1 32  ? 33.339  6.454   32.473  1.00 97.26  ? 32  ASN C OD1  1 
ATOM   8943  N ND2  . ASN C 1 32  ? 32.383  8.420   31.960  1.00 95.09  ? 32  ASN C ND2  1 
ATOM   8944  H H    . ASN C 1 32  ? 31.277  6.571   29.769  1.00 109.26 ? 32  ASN C H    1 
ATOM   8945  H HA   . ASN C 1 32  ? 31.542  4.608   31.506  1.00 108.05 ? 32  ASN C HA   1 
ATOM   8946  H HB2  . ASN C 1 32  ? 30.324  7.137   31.877  1.00 110.99 ? 32  ASN C HB2  1 
ATOM   8947  H HB3  . ASN C 1 32  ? 30.744  6.162   33.059  1.00 110.99 ? 32  ASN C HB3  1 
ATOM   8948  H HD21 . ASN C 1 32  ? 31.661  8.850   31.779  1.00 114.10 ? 32  ASN C HD21 1 
ATOM   8949  H HD22 . ASN C 1 32  ? 33.137  8.834   31.976  1.00 114.10 ? 32  ASN C HD22 1 
ATOM   8950  N N    . ILE C 1 33  ? 28.830  4.556   30.112  1.00 89.51  ? 33  ILE C N    1 
ATOM   8951  C CA   . ILE C 1 33  ? 27.487  3.972   30.114  1.00 87.75  ? 33  ILE C CA   1 
ATOM   8952  C C    . ILE C 1 33  ? 27.473  2.597   30.774  1.00 86.03  ? 33  ILE C C    1 
ATOM   8953  O O    . ILE C 1 33  ? 26.660  2.382   31.684  1.00 83.81  ? 33  ILE C O    1 
ATOM   8954  C CB   . ILE C 1 33  ? 26.913  3.957   28.684  1.00 83.34  ? 33  ILE C CB   1 
ATOM   8955  C CG1  . ILE C 1 33  ? 26.431  5.372   28.327  1.00 85.05  ? 33  ILE C CG1  1 
ATOM   8956  C CG2  . ILE C 1 33  ? 25.825  2.899   28.559  1.00 81.89  ? 33  ILE C CG2  1 
ATOM   8957  C CD1  . ILE C 1 33  ? 25.141  5.446   27.533  1.00 82.62  ? 33  ILE C CD1  1 
ATOM   8958  H H    . ILE C 1 33  ? 29.106  4.818   29.341  1.00 107.41 ? 33  ILE C H    1 
ATOM   8959  H HA   . ILE C 1 33  ? 26.913  4.552   30.639  1.00 105.30 ? 33  ILE C HA   1 
ATOM   8960  H HB   . ILE C 1 33  ? 27.600  3.712   28.045  1.00 100.01 ? 33  ILE C HB   1 
ATOM   8961  H HG12 . ILE C 1 33  ? 26.291  5.863   29.151  1.00 102.06 ? 33  ILE C HG12 1 
ATOM   8962  H HG13 . ILE C 1 33  ? 27.120  5.803   27.797  1.00 102.06 ? 33  ILE C HG13 1 
ATOM   8963  H HG21 . ILE C 1 33  ? 25.382  3.001   27.702  1.00 98.27  ? 33  ILE C HG21 1 
ATOM   8964  H HG22 . ILE C 1 33  ? 26.232  2.020   28.618  1.00 98.27  ? 33  ILE C HG22 1 
ATOM   8965  H HG23 . ILE C 1 33  ? 25.186  3.016   29.278  1.00 98.27  ? 33  ILE C HG23 1 
ATOM   8966  H HD11 . ILE C 1 33  ? 24.957  6.373   27.316  1.00 99.14  ? 33  ILE C HD11 1 
ATOM   8967  H HD12 . ILE C 1 33  ? 25.241  4.929   26.719  1.00 99.14  ? 33  ILE C HD12 1 
ATOM   8968  H HD13 . ILE C 1 33  ? 24.419  5.083   28.070  1.00 99.14  ? 33  ILE C HD13 1 
ATOM   8969  N N    . PRO C 1 34  ? 28.311  1.635   30.375  1.00 84.29  ? 34  PRO C N    1 
ATOM   8970  C CA   . PRO C 1 34  ? 28.299  0.328   31.055  1.00 86.45  ? 34  PRO C CA   1 
ATOM   8971  C C    . PRO C 1 34  ? 28.417  0.404   32.571  1.00 88.33  ? 34  PRO C C    1 
ATOM   8972  O O    . PRO C 1 34  ? 27.641  -0.245  33.284  1.00 84.80  ? 34  PRO C O    1 
ATOM   8973  C CB   . PRO C 1 34  ? 29.506  -0.390  30.431  1.00 86.20  ? 34  PRO C CB   1 
ATOM   8974  C CG   . PRO C 1 34  ? 29.626  0.188   29.073  1.00 85.12  ? 34  PRO C CG   1 
ATOM   8975  C CD   . PRO C 1 34  ? 29.142  1.625   29.155  1.00 86.94  ? 34  PRO C CD   1 
ATOM   8976  H HA   . PRO C 1 34  ? 27.478  -0.135  30.825  1.00 103.74 ? 34  PRO C HA   1 
ATOM   8977  H HB2  . PRO C 1 34  ? 30.303  -0.216  30.956  1.00 103.44 ? 34  PRO C HB2  1 
ATOM   8978  H HB3  . PRO C 1 34  ? 29.339  -1.345  30.390  1.00 103.44 ? 34  PRO C HB3  1 
ATOM   8979  H HG2  . PRO C 1 34  ? 30.554  0.158   28.791  1.00 102.14 ? 34  PRO C HG2  1 
ATOM   8980  H HG3  . PRO C 1 34  ? 29.076  -0.321  28.457  1.00 102.14 ? 34  PRO C HG3  1 
ATOM   8981  H HD2  . PRO C 1 34  ? 29.890  2.236   29.241  1.00 104.33 ? 34  PRO C HD2  1 
ATOM   8982  H HD3  . PRO C 1 34  ? 28.613  1.856   28.375  1.00 104.33 ? 34  PRO C HD3  1 
ATOM   8983  N N    . LYS C 1 35  ? 29.378  1.178   33.085  1.00 91.07  ? 35  LYS C N    1 
ATOM   8984  C CA   . LYS C 1 35  ? 29.558  1.265   34.530  1.00 88.97  ? 35  LYS C CA   1 
ATOM   8985  C C    . LYS C 1 35  ? 28.373  1.954   35.196  1.00 85.38  ? 35  LYS C C    1 
ATOM   8986  O O    . LYS C 1 35  ? 27.964  1.568   36.297  1.00 85.68  ? 35  LYS C O    1 
ATOM   8987  C CB   . LYS C 1 35  ? 30.858  2.003   34.853  1.00 91.80  ? 35  LYS C CB   1 
ATOM   8988  C CG   . LYS C 1 35  ? 31.765  1.268   35.836  1.00 97.19  ? 35  LYS C CG   1 
ATOM   8989  C CD   . LYS C 1 35  ? 32.270  -0.049  35.254  1.00 99.50  ? 35  LYS C CD   1 
ATOM   8990  C CE   . LYS C 1 35  ? 33.585  -0.473  35.895  1.00 102.99 ? 35  LYS C CE   1 
ATOM   8991  N NZ   . LYS C 1 35  ? 33.760  -1.954  35.895  1.00 110.88 ? 35  LYS C NZ   1 
ATOM   8992  H H    . LYS C 1 35  ? 29.928  1.653   32.625  1.00 109.28 ? 35  LYS C H    1 
ATOM   8993  H HA   . LYS C 1 35  ? 29.625  0.367   34.890  1.00 106.76 ? 35  LYS C HA   1 
ATOM   8994  H HB2  . LYS C 1 35  ? 31.356  2.128   34.030  1.00 110.16 ? 35  LYS C HB2  1 
ATOM   8995  H HB3  . LYS C 1 35  ? 30.637  2.864   35.242  1.00 110.16 ? 35  LYS C HB3  1 
ATOM   8996  H HG2  . LYS C 1 35  ? 32.532  1.825   36.043  1.00 116.63 ? 35  LYS C HG2  1 
ATOM   8997  H HG3  . LYS C 1 35  ? 31.268  1.073   36.646  1.00 116.63 ? 35  LYS C HG3  1 
ATOM   8998  H HD2  . LYS C 1 35  ? 31.614  -0.745  35.414  1.00 119.40 ? 35  LYS C HD2  1 
ATOM   8999  H HD3  . LYS C 1 35  ? 32.416  0.056   34.300  1.00 119.40 ? 35  LYS C HD3  1 
ATOM   9000  H HE2  . LYS C 1 35  ? 34.322  -0.082  35.400  1.00 123.59 ? 35  LYS C HE2  1 
ATOM   9001  H HE3  . LYS C 1 35  ? 33.604  -0.167  36.815  1.00 123.59 ? 35  LYS C HE3  1 
ATOM   9002  H HZ1  . LYS C 1 35  ? 34.538  -2.169  36.272  1.00 133.05 ? 35  LYS C HZ1  1 
ATOM   9003  H HZ2  . LYS C 1 35  ? 33.101  -2.338  36.354  1.00 133.05 ? 35  LYS C HZ2  1 
ATOM   9004  H HZ3  . LYS C 1 35  ? 33.748  -2.262  35.061  1.00 133.05 ? 35  LYS C HZ3  1 
ATOM   9005  N N    . LEU C 1 36  ? 27.816  2.983   34.553  1.00 83.90  ? 36  LEU C N    1 
ATOM   9006  C CA   . LEU C 1 36  ? 26.638  3.638   35.106  1.00 83.69  ? 36  LEU C CA   1 
ATOM   9007  C C    . LEU C 1 36  ? 25.455  2.679   35.154  1.00 83.21  ? 36  LEU C C    1 
ATOM   9008  O O    . LEU C 1 36  ? 24.691  2.669   36.124  1.00 85.33  ? 36  LEU C O    1 
ATOM   9009  C CB   . LEU C 1 36  ? 26.281  4.873   34.281  1.00 85.62  ? 36  LEU C CB   1 
ATOM   9010  C CG   . LEU C 1 36  ? 27.233  6.068   34.331  1.00 87.45  ? 36  LEU C CG   1 
ATOM   9011  C CD1  . LEU C 1 36  ? 26.585  7.269   33.637  1.00 88.65  ? 36  LEU C CD1  1 
ATOM   9012  C CD2  . LEU C 1 36  ? 27.629  6.419   35.753  1.00 87.25  ? 36  LEU C CD2  1 
ATOM   9013  H H    . LEU C 1 36  ? 28.098  3.312   33.810  1.00 100.68 ? 36  LEU C H    1 
ATOM   9014  H HA   . LEU C 1 36  ? 26.838  3.929   36.010  1.00 100.43 ? 36  LEU C HA   1 
ATOM   9015  H HB2  . LEU C 1 36  ? 26.224  4.601   33.352  1.00 102.74 ? 36  LEU C HB2  1 
ATOM   9016  H HB3  . LEU C 1 36  ? 25.418  5.193   34.587  1.00 102.74 ? 36  LEU C HB3  1 
ATOM   9017  H HG   . LEU C 1 36  ? 28.050  5.834   33.864  1.00 104.94 ? 36  LEU C HG   1 
ATOM   9018  H HD11 . LEU C 1 36  ? 26.394  7.037   32.715  1.00 106.39 ? 36  LEU C HD11 1 
ATOM   9019  H HD12 . LEU C 1 36  ? 25.762  7.494   34.098  1.00 106.39 ? 36  LEU C HD12 1 
ATOM   9020  H HD13 . LEU C 1 36  ? 27.197  8.021   33.669  1.00 106.39 ? 36  LEU C HD13 1 
ATOM   9021  H HD21 . LEU C 1 36  ? 28.095  7.269   35.750  1.00 104.70 ? 36  LEU C HD21 1 
ATOM   9022  H HD22 . LEU C 1 36  ? 26.829  6.482   36.297  1.00 104.70 ? 36  LEU C HD22 1 
ATOM   9023  H HD23 . LEU C 1 36  ? 28.211  5.724   36.099  1.00 104.70 ? 36  LEU C HD23 1 
ATOM   9024  N N    . SER C 1 37  ? 25.285  1.863   34.111  1.00 82.85  ? 37  SER C N    1 
ATOM   9025  C CA   . SER C 1 37  ? 24.194  0.894   34.110  1.00 83.13  ? 37  SER C CA   1 
ATOM   9026  C C    . SER C 1 37  ? 24.385  -0.139  35.212  1.00 82.61  ? 37  SER C C    1 
ATOM   9027  O O    . SER C 1 37  ? 23.416  -0.570  35.848  1.00 81.22  ? 37  SER C O    1 
ATOM   9028  C CB   . SER C 1 37  ? 24.102  0.210   32.746  1.00 81.89  ? 37  SER C CB   1 
ATOM   9029  O OG   . SER C 1 37  ? 23.921  1.157   31.707  1.00 85.14  ? 37  SER C OG   1 
ATOM   9030  H H    . SER C 1 37  ? 25.779  1.851   33.407  1.00 99.42  ? 37  SER C H    1 
ATOM   9031  H HA   . SER C 1 37  ? 23.358  1.359   34.268  1.00 99.76  ? 37  SER C HA   1 
ATOM   9032  H HB2  . SER C 1 37  ? 24.924  -0.280  32.584  1.00 98.27  ? 37  SER C HB2  1 
ATOM   9033  H HB3  . SER C 1 37  ? 23.348  -0.399  32.750  1.00 98.27  ? 37  SER C HB3  1 
ATOM   9034  H HG   . SER C 1 37  ? 24.569  1.691   31.690  1.00 102.17 ? 37  SER C HG   1 
ATOM   9035  N N    . GLU C 1 38  ? 25.634  -0.539  35.460  1.00 82.85  ? 38  GLU C N    1 
ATOM   9036  C CA   . GLU C 1 38  ? 25.904  -1.554  36.473  1.00 84.31  ? 38  GLU C CA   1 
ATOM   9037  C C    . GLU C 1 38  ? 25.490  -1.074  37.858  1.00 83.58  ? 38  GLU C C    1 
ATOM   9038  O O    . GLU C 1 38  ? 24.816  -1.797  38.603  1.00 81.33  ? 38  GLU C O    1 
ATOM   9039  C CB   . GLU C 1 38  ? 27.387  -1.924  36.450  1.00 87.83  ? 38  GLU C CB   1 
ATOM   9040  C CG   . GLU C 1 38  ? 27.660  -3.394  36.700  1.00 91.34  ? 38  GLU C CG   1 
ATOM   9041  C CD   . GLU C 1 38  ? 28.941  -3.631  37.480  1.00 92.53  ? 38  GLU C CD   1 
ATOM   9042  O OE1  . GLU C 1 38  ? 29.823  -2.744  37.480  1.00 92.61  ? 38  GLU C OE1  1 
ATOM   9043  O OE2  . GLU C 1 38  ? 29.065  -4.713  38.095  1.00 99.92  ? 38  GLU C OE2  1 
ATOM   9044  H H    . GLU C 1 38  ? 26.334  -0.242  35.059  1.00 99.43  ? 38  GLU C H    1 
ATOM   9045  H HA   . GLU C 1 38  ? 25.388  -2.349  36.267  1.00 101.17 ? 38  GLU C HA   1 
ATOM   9046  H HB2  . GLU C 1 38  ? 27.749  -1.700  35.579  1.00 105.40 ? 38  GLU C HB2  1 
ATOM   9047  H HB3  . GLU C 1 38  ? 27.844  -1.417  37.140  1.00 105.40 ? 38  GLU C HB3  1 
ATOM   9048  H HG2  . GLU C 1 38  ? 26.925  -3.769  37.210  1.00 109.61 ? 38  GLU C HG2  1 
ATOM   9049  H HG3  . GLU C 1 38  ? 27.739  -3.850  35.848  1.00 109.61 ? 38  GLU C HG3  1 
ATOM   9050  N N    . GLU C 1 39  ? 25.888  0.148   38.225  1.00 82.89  ? 39  GLU C N    1 
ATOM   9051  C CA   . GLU C 1 39  ? 25.546  0.661   39.549  1.00 86.94  ? 39  GLU C CA   1 
ATOM   9052  C C    . GLU C 1 39  ? 24.049  0.922   39.670  1.00 82.75  ? 39  GLU C C    1 
ATOM   9053  O O    . GLU C 1 39  ? 23.454  0.679   40.725  1.00 81.70  ? 39  GLU C O    1 
ATOM   9054  C CB   . GLU C 1 39  ? 26.333  1.938   39.840  1.00 89.14  ? 39  GLU C CB   1 
ATOM   9055  C CG   . GLU C 1 39  ? 27.085  1.916   41.167  1.00 100.34 ? 39  GLU C CG   1 
ATOM   9056  C CD   . GLU C 1 39  ? 27.941  3.156   41.380  1.00 110.96 ? 39  GLU C CD   1 
ATOM   9057  O OE1  . GLU C 1 39  ? 27.390  4.207   41.775  1.00 110.69 ? 39  GLU C OE1  1 
ATOM   9058  O OE2  . GLU C 1 39  ? 29.169  3.080   41.156  1.00 115.22 ? 39  GLU C OE2  1 
ATOM   9059  H H    . GLU C 1 39  ? 26.346  0.687   37.736  1.00 99.47  ? 39  GLU C H    1 
ATOM   9060  H HA   . GLU C 1 39  ? 25.793  -0.003  40.211  1.00 104.33 ? 39  GLU C HA   1 
ATOM   9061  H HB2  . GLU C 1 39  ? 26.985  2.069   39.133  1.00 106.96 ? 39  GLU C HB2  1 
ATOM   9062  H HB3  . GLU C 1 39  ? 25.715  2.686   39.863  1.00 106.96 ? 39  GLU C HB3  1 
ATOM   9063  H HG2  . GLU C 1 39  ? 26.443  1.867   41.893  1.00 120.41 ? 39  GLU C HG2  1 
ATOM   9064  H HG3  . GLU C 1 39  ? 27.669  1.142   41.186  1.00 120.41 ? 39  GLU C HG3  1 
ATOM   9065  N N    . ILE C 1 40  ? 23.422  1.414   38.600  1.00 79.67  ? 40  ILE C N    1 
ATOM   9066  C CA   . ILE C 1 40  ? 21.998  1.719   38.657  1.00 78.14  ? 40  ILE C CA   1 
ATOM   9067  C C    . ILE C 1 40  ? 21.176  0.453   38.845  1.00 79.02  ? 40  ILE C C    1 
ATOM   9068  O O    . ILE C 1 40  ? 20.052  0.514   39.347  1.00 77.66  ? 40  ILE C O    1 
ATOM   9069  C CB   . ILE C 1 40  ? 21.558  2.481   37.390  1.00 82.05  ? 40  ILE C CB   1 
ATOM   9070  C CG1  . ILE C 1 40  ? 22.119  3.909   37.410  1.00 83.19  ? 40  ILE C CG1  1 
ATOM   9071  C CG2  . ILE C 1 40  ? 20.033  2.498   37.263  1.00 82.05  ? 40  ILE C CG2  1 
ATOM   9072  C CD1  . ILE C 1 40  ? 21.644  4.792   36.241  1.00 86.35  ? 40  ILE C CD1  1 
ATOM   9073  H H    . ILE C 1 40  ? 23.794  1.577   37.842  1.00 95.61  ? 40  ILE C H    1 
ATOM   9074  H HA   . ILE C 1 40  ? 21.845  2.292   39.425  1.00 93.77  ? 40  ILE C HA   1 
ATOM   9075  H HB   . ILE C 1 40  ? 21.917  2.018   36.617  1.00 98.46  ? 40  ILE C HB   1 
ATOM   9076  H HG12 . ILE C 1 40  ? 21.842  4.339   38.235  1.00 99.82  ? 40  ILE C HG12 1 
ATOM   9077  H HG13 . ILE C 1 40  ? 23.087  3.862   37.369  1.00 99.82  ? 40  ILE C HG13 1 
ATOM   9078  H HG21 . ILE C 1 40  ? 19.788  2.991   36.465  1.00 98.47  ? 40  ILE C HG21 1 
ATOM   9079  H HG22 . ILE C 1 40  ? 19.711  1.585   37.199  1.00 98.47  ? 40  ILE C HG22 1 
ATOM   9080  H HG23 . ILE C 1 40  ? 19.655  2.927   38.047  1.00 98.47  ? 40  ILE C HG23 1 
ATOM   9081  H HD11 . ILE C 1 40  ? 22.089  5.653   36.295  1.00 103.62 ? 40  ILE C HD11 1 
ATOM   9082  H HD12 . ILE C 1 40  ? 21.868  4.356   35.404  1.00 103.62 ? 40  ILE C HD12 1 
ATOM   9083  H HD13 . ILE C 1 40  ? 20.684  4.912   36.305  1.00 103.62 ? 40  ILE C HD13 1 
ATOM   9084  N N    . MET C 1 41  ? 21.700  -0.703  38.435  1.00 80.40  ? 41  MET C N    1 
ATOM   9085  C CA   . MET C 1 41  ? 20.920  -1.936  38.474  1.00 80.06  ? 41  MET C CA   1 
ATOM   9086  C C    . MET C 1 41  ? 20.951  -2.619  39.836  1.00 81.10  ? 41  MET C C    1 
ATOM   9087  O O    . MET C 1 41  ? 20.101  -3.477  40.105  1.00 80.41  ? 41  MET C O    1 
ATOM   9088  C CB   . MET C 1 41  ? 21.427  -2.908  37.397  1.00 80.75  ? 41  MET C CB   1 
ATOM   9089  C CG   . MET C 1 41  ? 20.698  -2.800  36.069  1.00 80.07  ? 41  MET C CG   1 
ATOM   9090  S SD   . MET C 1 41  ? 21.395  -3.779  34.706  1.00 86.83  ? 41  MET C SD   1 
ATOM   9091  C CE   . MET C 1 41  ? 23.158  -3.701  35.041  1.00 82.34  ? 41  MET C CE   1 
ATOM   9092  H H    . MET C 1 41  ? 22.500  -0.798  38.133  1.00 96.48  ? 41  MET C H    1 
ATOM   9093  H HA   . MET C 1 41  ? 19.997  -1.719  38.268  1.00 96.07  ? 41  MET C HA   1 
ATOM   9094  H HB2  . MET C 1 41  ? 22.365  -2.728  37.233  1.00 96.90  ? 41  MET C HB2  1 
ATOM   9095  H HB3  . MET C 1 41  ? 21.315  -3.816  37.721  1.00 96.90  ? 41  MET C HB3  1 
ATOM   9096  H HG2  . MET C 1 41  ? 19.783  -3.098  36.198  1.00 96.09  ? 41  MET C HG2  1 
ATOM   9097  H HG3  . MET C 1 41  ? 20.708  -1.871  35.790  1.00 96.09  ? 41  MET C HG3  1 
ATOM   9098  H HE1  . MET C 1 41  ? 23.637  -4.118  34.308  1.00 98.80  ? 41  MET C HE1  1 
ATOM   9099  H HE2  . MET C 1 41  ? 23.423  -2.772  35.124  1.00 98.80  ? 41  MET C HE2  1 
ATOM   9100  H HE3  . MET C 1 41  ? 23.344  -4.172  35.868  1.00 98.80  ? 41  MET C HE3  1 
ATOM   9101  N N    . LYS C 1 42  ? 21.890  -2.253  40.703  1.00 82.66  ? 42  LYS C N    1 
ATOM   9102  C CA   . LYS C 1 42  ? 22.021  -2.941  41.978  1.00 83.26  ? 42  LYS C CA   1 
ATOM   9103  C C    . LYS C 1 42  ? 20.733  -2.847  42.791  1.00 82.69  ? 42  LYS C C    1 
ATOM   9104  O O    . LYS C 1 42  ? 19.925  -1.928  42.622  1.00 80.93  ? 42  LYS C O    1 
ATOM   9105  C CB   . LYS C 1 42  ? 23.177  -2.354  42.786  1.00 80.30  ? 42  LYS C CB   1 
ATOM   9106  C CG   . LYS C 1 42  ? 24.548  -2.587  42.191  1.00 80.40  ? 42  LYS C CG   1 
ATOM   9107  C CD   . LYS C 1 42  ? 25.620  -1.965  43.070  1.00 87.66  ? 42  LYS C CD   1 
ATOM   9108  C CE   . LYS C 1 42  ? 26.974  -1.941  42.378  1.00 91.63  ? 42  LYS C CE   1 
ATOM   9109  N NZ   . LYS C 1 42  ? 28.087  -1.863  43.373  1.00 93.95  ? 42  LYS C NZ   1 
ATOM   9110  H H    . LYS C 1 42  ? 22.456  -1.618  40.577  1.00 99.19  ? 42  LYS C H    1 
ATOM   9111  H HA   . LYS C 1 42  ? 22.205  -3.878  41.808  1.00 99.91  ? 42  LYS C HA   1 
ATOM   9112  H HB2  . LYS C 1 42  ? 23.048  -1.395  42.856  1.00 96.37  ? 42  LYS C HB2  1 
ATOM   9113  H HB3  . LYS C 1 42  ? 23.170  -2.754  43.670  1.00 96.37  ? 42  LYS C HB3  1 
ATOM   9114  H HG2  . LYS C 1 42  ? 24.716  -3.540  42.126  1.00 96.48  ? 42  LYS C HG2  1 
ATOM   9115  H HG3  . LYS C 1 42  ? 24.594  -2.181  41.311  1.00 96.48  ? 42  LYS C HG3  1 
ATOM   9116  H HD2  . LYS C 1 42  ? 25.370  -1.051  43.281  1.00 105.20 ? 42  LYS C HD2  1 
ATOM   9117  H HD3  . LYS C 1 42  ? 25.705  -2.482  43.886  1.00 105.20 ? 42  LYS C HD3  1 
ATOM   9118  H HE2  . LYS C 1 42  ? 27.084  -2.751  41.857  1.00 109.95 ? 42  LYS C HE2  1 
ATOM   9119  H HE3  . LYS C 1 42  ? 27.026  -1.164  41.799  1.00 109.95 ? 42  LYS C HE3  1 
ATOM   9120  H HZ1  . LYS C 1 42  ? 28.871  -1.850  42.952  1.00 112.74 ? 42  LYS C HZ1  1 
ATOM   9121  H HZ2  . LYS C 1 42  ? 28.009  -1.123  43.861  1.00 112.74 ? 42  LYS C HZ2  1 
ATOM   9122  H HZ3  . LYS C 1 42  ? 28.062  -2.570  43.913  1.00 112.74 ? 42  LYS C HZ3  1 
ATOM   9123  N N    . GLU C 1 43  ? 20.547  -3.833  43.677  1.00 83.02  ? 43  GLU C N    1 
ATOM   9124  C CA   . GLU C 1 43  ? 19.462  -3.781  44.650  1.00 86.28  ? 43  GLU C CA   1 
ATOM   9125  C C    . GLU C 1 43  ? 19.711  -2.699  45.692  1.00 84.52  ? 43  GLU C C    1 
ATOM   9126  O O    . GLU C 1 43  ? 18.754  -2.141  46.241  1.00 82.97  ? 43  GLU C O    1 
ATOM   9127  C CB   . GLU C 1 43  ? 19.303  -5.149  45.324  1.00 90.32  ? 43  GLU C CB   1 
ATOM   9128  C CG   . GLU C 1 43  ? 18.106  -5.275  46.273  1.00 93.45  ? 43  GLU C CG   1 
ATOM   9129  C CD   . GLU C 1 43  ? 18.450  -5.970  47.596  1.00 97.62  ? 43  GLU C CD   1 
ATOM   9130  O OE1  . GLU C 1 43  ? 19.644  -6.229  47.854  1.00 96.35  ? 43  GLU C OE1  1 
ATOM   9131  O OE2  . GLU C 1 43  ? 17.527  -6.253  48.396  1.00 96.11  ? 43  GLU C OE2  1 
ATOM   9132  H H    . GLU C 1 43  ? 21.035  -4.539  43.733  1.00 99.62  ? 43  GLU C H    1 
ATOM   9133  H HA   . GLU C 1 43  ? 18.631  -3.575  44.194  1.00 103.54 ? 43  GLU C HA   1 
ATOM   9134  H HB2  . GLU C 1 43  ? 19.196  -5.821  44.632  1.00 108.39 ? 43  GLU C HB2  1 
ATOM   9135  H HB3  . GLU C 1 43  ? 20.103  -5.331  45.842  1.00 108.39 ? 43  GLU C HB3  1 
ATOM   9136  H HG2  . GLU C 1 43  ? 17.775  -4.387  46.481  1.00 112.14 ? 43  GLU C HG2  1 
ATOM   9137  H HG3  . GLU C 1 43  ? 17.412  -5.794  45.837  1.00 112.14 ? 43  GLU C HG3  1 
ATOM   9138  N N    . THR C 1 44  ? 20.982  -2.399  45.983  1.00 84.00  ? 44  THR C N    1 
ATOM   9139  C CA   . THR C 1 44  ? 21.351  -1.295  46.866  1.00 81.60  ? 44  THR C CA   1 
ATOM   9140  C C    . THR C 1 44  ? 21.232  0.067   46.185  1.00 80.75  ? 44  THR C C    1 
ATOM   9141  O O    . THR C 1 44  ? 21.545  1.086   46.808  1.00 80.28  ? 44  THR C O    1 
ATOM   9142  C CB   . THR C 1 44  ? 22.781  -1.497  47.389  1.00 77.80  ? 44  THR C CB   1 
ATOM   9143  O OG1  . THR C 1 44  ? 23.698  -1.678  46.303  1.00 87.11  ? 44  THR C OG1  1 
ATOM   9144  C CG2  . THR C 1 44  ? 22.854  -2.728  48.274  1.00 84.45  ? 44  THR C CG2  1 
ATOM   9145  H H    . THR C 1 44  ? 21.659  -2.831  45.675  1.00 100.80 ? 44  THR C H    1 
ATOM   9146  H HA   . THR C 1 44  ? 20.755  -1.294  47.632  1.00 97.92  ? 44  THR C HA   1 
ATOM   9147  H HB   . THR C 1 44  ? 23.033  -0.712  47.900  1.00 93.36  ? 44  THR C HB   1 
ATOM   9148  H HG1  . THR C 1 44  ? 23.487  -2.359  45.859  1.00 104.53 ? 44  THR C HG1  1 
ATOM   9149  H HG21 . THR C 1 44  ? 23.754  -2.834  48.621  1.00 101.34 ? 44  THR C HG21 1 
ATOM   9150  H HG22 . THR C 1 44  ? 22.238  -2.639  49.017  1.00 101.34 ? 44  THR C HG22 1 
ATOM   9151  H HG23 . THR C 1 44  ? 22.619  -3.518  47.763  1.00 101.34 ? 44  THR C HG23 1 
ATOM   9152  N N    . ASN C 1 45  ? 20.780  0.107   44.931  1.00 81.43  ? 45  ASN C N    1 
ATOM   9153  C CA   . ASN C 1 45  ? 20.495  1.343   44.202  1.00 78.84  ? 45  ASN C CA   1 
ATOM   9154  C C    . ASN C 1 45  ? 19.023  1.325   43.794  1.00 76.44  ? 45  ASN C C    1 
ATOM   9155  O O    . ASN C 1 45  ? 18.229  0.562   44.357  1.00 82.36  ? 45  ASN C O    1 
ATOM   9156  C CB   . ASN C 1 45  ? 21.397  1.466   42.971  1.00 79.21  ? 45  ASN C CB   1 
ATOM   9157  C CG   . ASN C 1 45  ? 21.682  2.916   42.594  1.00 79.55  ? 45  ASN C CG   1 
ATOM   9158  O OD1  . ASN C 1 45  ? 21.010  3.490   41.731  1.00 71.34  ? 45  ASN C OD1  1 
ATOM   9159  N ND2  . ASN C 1 45  ? 22.694  3.508   43.226  1.00 79.86  ? 45  ASN C ND2  1 
ATOM   9160  H H    . ASN C 1 45  ? 20.624  -0.596  44.461  1.00 97.71  ? 45  ASN C H    1 
ATOM   9161  H HA   . ASN C 1 45  ? 20.673  2.118   44.758  1.00 94.61  ? 45  ASN C HA   1 
ATOM   9162  H HB2  . ASN C 1 45  ? 22.245  1.032   43.154  1.00 95.06  ? 45  ASN C HB2  1 
ATOM   9163  H HB3  . ASN C 1 45  ? 20.962  1.040   42.216  1.00 95.06  ? 45  ASN C HB3  1 
ATOM   9164  H HD21 . ASN C 1 45  ? 22.893  4.325   43.048  1.00 95.83  ? 45  ASN C HD21 1 
ATOM   9165  H HD22 . ASN C 1 45  ? 23.148  3.072   43.813  1.00 95.83  ? 45  ASN C HD22 1 
ATOM   9166  N N    . LEU C 1 46  ? 18.638  2.156   42.829  1.00 81.04  ? 46  LEU C N    1 
ATOM   9167  C CA   . LEU C 1 46  ? 17.391  1.917   42.115  1.00 77.59  ? 46  LEU C CA   1 
ATOM   9168  C C    . LEU C 1 46  ? 17.464  0.524   41.512  1.00 79.11  ? 46  LEU C C    1 
ATOM   9169  O O    . LEU C 1 46  ? 18.461  0.170   40.884  1.00 83.69  ? 46  LEU C O    1 
ATOM   9170  C CB   . LEU C 1 46  ? 17.190  2.963   41.024  1.00 74.54  ? 46  LEU C CB   1 
ATOM   9171  C CG   . LEU C 1 46  ? 15.740  3.312   40.671  1.00 75.08  ? 46  LEU C CG   1 
ATOM   9172  C CD1  . LEU C 1 46  ? 15.048  3.997   41.845  1.00 76.75  ? 46  LEU C CD1  1 
ATOM   9173  C CD2  . LEU C 1 46  ? 15.670  4.188   39.427  1.00 72.88  ? 46  LEU C CD2  1 
ATOM   9174  H H    . LEU C 1 46  ? 19.073  2.853   42.574  1.00 97.25  ? 46  LEU C H    1 
ATOM   9175  H HA   . LEU C 1 46  ? 16.630  1.983   42.713  1.00 93.11  ? 46  LEU C HA   1 
ATOM   9176  H HB2  . LEU C 1 46  ? 17.618  3.784   41.312  1.00 89.45  ? 46  LEU C HB2  1 
ATOM   9177  H HB3  . LEU C 1 46  ? 17.610  2.637   40.213  1.00 89.45  ? 46  LEU C HB3  1 
ATOM   9178  H HG   . LEU C 1 46  ? 15.267  2.487   40.479  1.00 90.09  ? 46  LEU C HG   1 
ATOM   9179  H HD11 . LEU C 1 46  ? 14.211  4.380   41.539  1.00 92.10  ? 46  LEU C HD11 1 
ATOM   9180  H HD12 . LEU C 1 46  ? 14.877  3.341   42.539  1.00 92.10  ? 46  LEU C HD12 1 
ATOM   9181  H HD13 . LEU C 1 46  ? 15.626  4.697   42.188  1.00 92.10  ? 46  LEU C HD13 1 
ATOM   9182  H HD21 . LEU C 1 46  ? 14.748  4.243   39.131  1.00 87.46  ? 46  LEU C HD21 1 
ATOM   9183  H HD22 . LEU C 1 46  ? 16.001  5.074   39.646  1.00 87.46  ? 46  LEU C HD22 1 
ATOM   9184  H HD23 . LEU C 1 46  ? 16.218  3.793   38.731  1.00 87.46  ? 46  LEU C HD23 1 
ATOM   9185  N N    . TYR C 1 47  ? 16.442  -0.292  41.717  1.00 79.71  ? 47  TYR C N    1 
ATOM   9186  C CA   . TYR C 1 47  ? 16.525  -1.660  41.209  1.00 81.87  ? 47  TYR C CA   1 
ATOM   9187  C C    . TYR C 1 47  ? 16.174  -1.697  39.726  1.00 76.47  ? 47  TYR C C    1 
ATOM   9188  O O    . TYR C 1 47  ? 15.383  -0.888  39.235  1.00 73.78  ? 47  TYR C O    1 
ATOM   9189  C CB   . TYR C 1 47  ? 15.608  -2.590  41.994  1.00 81.78  ? 47  TYR C CB   1 
ATOM   9190  C CG   . TYR C 1 47  ? 16.074  -4.034  42.031  1.00 88.40  ? 47  TYR C CG   1 
ATOM   9191  C CD1  . TYR C 1 47  ? 17.397  -4.378  41.763  1.00 87.98  ? 47  TYR C CD1  1 
ATOM   9192  C CD2  . TYR C 1 47  ? 15.185  -5.057  42.338  1.00 95.75  ? 47  TYR C CD2  1 
ATOM   9193  C CE1  . TYR C 1 47  ? 17.817  -5.695  41.796  1.00 92.50  ? 47  TYR C CE1  1 
ATOM   9194  C CE2  . TYR C 1 47  ? 15.597  -6.378  42.378  1.00 97.53  ? 47  TYR C CE2  1 
ATOM   9195  C CZ   . TYR C 1 47  ? 16.914  -6.690  42.108  1.00 98.79  ? 47  TYR C CZ   1 
ATOM   9196  O OH   . TYR C 1 47  ? 17.331  -8.001  42.148  1.00 106.97 ? 47  TYR C OH   1 
ATOM   9197  H H    . TYR C 1 47  ? 15.716  -0.089  42.132  1.00 95.65  ? 47  TYR C H    1 
ATOM   9198  H HA   . TYR C 1 47  ? 17.431  -1.990  41.313  1.00 98.24  ? 47  TYR C HA   1 
ATOM   9199  H HB2  . TYR C 1 47  ? 15.555  -2.274  42.910  1.00 98.14  ? 47  TYR C HB2  1 
ATOM   9200  H HB3  . TYR C 1 47  ? 14.727  -2.575  41.587  1.00 98.14  ? 47  TYR C HB3  1 
ATOM   9201  H HD1  . TYR C 1 47  ? 18.009  -3.709  41.557  1.00 105.57 ? 47  TYR C HD1  1 
ATOM   9202  H HD2  . TYR C 1 47  ? 14.297  -4.850  42.519  1.00 114.90 ? 47  TYR C HD2  1 
ATOM   9203  H HE1  . TYR C 1 47  ? 18.703  -5.908  41.610  1.00 111.00 ? 47  TYR C HE1  1 
ATOM   9204  H HE2  . TYR C 1 47  ? 14.990  -7.051  42.586  1.00 117.04 ? 47  TYR C HE2  1 
ATOM   9205  H HH   . TYR C 1 47  ? 16.700  -8.496  42.399  1.00 128.37 ? 47  TYR C HH   1 
ATOM   9206  N N    . ALA C 1 48  ? 16.780  -2.644  39.011  1.00 78.06  ? 48  ALA C N    1 
ATOM   9207  C CA   . ALA C 1 48  ? 16.567  -2.775  37.576  1.00 81.11  ? 48  ALA C CA   1 
ATOM   9208  C C    . ALA C 1 48  ? 17.175  -4.080  37.085  1.00 80.59  ? 48  ALA C C    1 
ATOM   9209  O O    . ALA C 1 48  ? 18.160  -4.570  37.644  1.00 81.39  ? 48  ALA C O    1 
ATOM   9210  C CB   . ALA C 1 48  ? 17.189  -1.603  36.803  1.00 75.96  ? 48  ALA C CB   1 
ATOM   9211  H H    . ALA C 1 48  ? 17.323  -3.225  39.339  1.00 93.67  ? 48  ALA C H    1 
ATOM   9212  H HA   . ALA C 1 48  ? 15.612  -2.798  37.410  1.00 97.33  ? 48  ALA C HA   1 
ATOM   9213  H HB1  . ALA C 1 48  ? 16.813  -1.580  35.909  1.00 91.15  ? 48  ALA C HB1  1 
ATOM   9214  H HB2  . ALA C 1 48  ? 16.988  -0.776  37.268  1.00 91.15  ? 48  ALA C HB2  1 
ATOM   9215  H HB3  . ALA C 1 48  ? 18.149  -1.731  36.755  1.00 91.15  ? 48  ALA C HB3  1 
ATOM   9216  N N    . GLU C 1 49  ? 16.576  -4.627  36.022  1.00 77.73  ? 49  GLU C N    1 
ATOM   9217  C CA   . GLU C 1 49  ? 17.136  -5.759  35.299  1.00 78.51  ? 49  GLU C CA   1 
ATOM   9218  C C    . GLU C 1 49  ? 17.871  -5.346  34.031  1.00 76.84  ? 49  GLU C C    1 
ATOM   9219  O O    . GLU C 1 49  ? 18.675  -6.126  33.512  1.00 76.68  ? 49  GLU C O    1 
ATOM   9220  C CB   . GLU C 1 49  ? 16.025  -6.749  34.929  1.00 81.18  ? 49  GLU C CB   1 
ATOM   9221  C CG   . GLU C 1 49  ? 15.419  -7.470  36.115  1.00 84.73  ? 49  GLU C CG   1 
ATOM   9222  C CD   . GLU C 1 49  ? 14.422  -8.540  35.705  1.00 90.49  ? 49  GLU C CD   1 
ATOM   9223  O OE1  . GLU C 1 49  ? 14.640  -9.195  34.658  1.00 94.54  ? 49  GLU C OE1  1 
ATOM   9224  O OE2  . GLU C 1 49  ? 13.420  -8.721  36.433  1.00 93.13  ? 49  GLU C OE2  1 
ATOM   9225  H H    . GLU C 1 49  ? 15.828  -4.351  35.698  1.00 93.28  ? 49  GLU C H    1 
ATOM   9226  H HA   . GLU C 1 49  ? 17.766  -6.221  35.875  1.00 94.21  ? 49  GLU C HA   1 
ATOM   9227  H HB2  . GLU C 1 49  ? 15.313  -6.263  34.484  1.00 97.41  ? 49  GLU C HB2  1 
ATOM   9228  H HB3  . GLU C 1 49  ? 16.393  -7.419  34.332  1.00 97.41  ? 49  GLU C HB3  1 
ATOM   9229  H HG2  . GLU C 1 49  ? 16.128  -7.899  36.620  1.00 101.67 ? 49  GLU C HG2  1 
ATOM   9230  H HG3  . GLU C 1 49  ? 14.956  -6.827  36.674  1.00 101.67 ? 49  GLU C HG3  1 
ATOM   9231  N N    . GLN C 1 50  ? 17.619  -4.144  33.524  1.00 74.78  ? 50  GLN C N    1 
ATOM   9232  C CA   . GLN C 1 50  ? 18.262  -3.665  32.310  1.00 77.31  ? 50  GLN C CA   1 
ATOM   9233  C C    . GLN C 1 50  ? 18.119  -2.154  32.262  1.00 76.28  ? 50  GLN C C    1 
ATOM   9234  O O    . GLN C 1 50  ? 17.193  -1.587  32.845  1.00 74.84  ? 50  GLN C O    1 
ATOM   9235  C CB   . GLN C 1 50  ? 17.646  -4.300  31.066  1.00 74.05  ? 50  GLN C CB   1 
ATOM   9236  C CG   . GLN C 1 50  ? 16.217  -3.868  30.809  1.00 74.94  ? 50  GLN C CG   1 
ATOM   9237  C CD   . GLN C 1 50  ? 15.586  -4.609  29.645  1.00 78.71  ? 50  GLN C CD   1 
ATOM   9238  O OE1  . GLN C 1 50  ? 16.273  -5.271  28.865  1.00 77.22  ? 50  GLN C OE1  1 
ATOM   9239  N NE2  . GLN C 1 50  ? 14.269  -4.495  29.520  1.00 80.73  ? 50  GLN C NE2  1 
ATOM   9240  H H    . GLN C 1 50  ? 17.071  -3.579  33.870  1.00 89.74  ? 50  GLN C H    1 
ATOM   9241  H HA   . GLN C 1 50  ? 19.206  -3.887  32.325  1.00 92.77  ? 50  GLN C HA   1 
ATOM   9242  H HB2  . GLN C 1 50  ? 18.175  -4.051  30.293  1.00 88.87  ? 50  GLN C HB2  1 
ATOM   9243  H HB3  . GLN C 1 50  ? 17.650  -5.264  31.173  1.00 88.87  ? 50  GLN C HB3  1 
ATOM   9244  H HG2  . GLN C 1 50  ? 15.686  -4.044  31.601  1.00 89.93  ? 50  GLN C HG2  1 
ATOM   9245  H HG3  . GLN C 1 50  ? 16.205  -2.920  30.604  1.00 89.93  ? 50  GLN C HG3  1 
ATOM   9246  H HE21 . GLN C 1 50  ? 13.823  -4.021  30.082  1.00 96.88  ? 50  GLN C HE21 1 
ATOM   9247  H HE22 . GLN C 1 50  ? 13.862  -4.896  28.877  1.00 96.88  ? 50  GLN C HE22 1 
ATOM   9248  N N    . VAL C 1 51  ? 19.045  -1.507  31.563  1.00 77.37  ? 51  VAL C N    1 
ATOM   9249  C CA   . VAL C 1 51  ? 19.113  -0.050  31.509  1.00 78.61  ? 51  VAL C CA   1 
ATOM   9250  C C    . VAL C 1 51  ? 19.155  0.387   30.053  1.00 76.38  ? 51  VAL C C    1 
ATOM   9251  O O    . VAL C 1 51  ? 19.829  -0.234  29.223  1.00 76.13  ? 51  VAL C O    1 
ATOM   9252  C CB   . VAL C 1 51  ? 20.338  0.488   32.282  1.00 79.81  ? 51  VAL C CB   1 
ATOM   9253  C CG1  . VAL C 1 51  ? 20.755  1.864   31.780  1.00 76.16  ? 51  VAL C CG1  1 
ATOM   9254  C CG2  . VAL C 1 51  ? 20.034  0.529   33.773  1.00 77.06  ? 51  VAL C CG2  1 
ATOM   9255  H H    . VAL C 1 51  ? 19.657  -1.897  31.103  1.00 92.84  ? 51  VAL C H    1 
ATOM   9256  H HA   . VAL C 1 51  ? 18.311  0.323   31.909  1.00 94.33  ? 51  VAL C HA   1 
ATOM   9257  H HB   . VAL C 1 51  ? 21.085  -0.112  32.130  1.00 95.77  ? 51  VAL C HB   1 
ATOM   9258  H HG11 . VAL C 1 51  ? 21.508  2.177   32.306  1.00 91.40  ? 51  VAL C HG11 1 
ATOM   9259  H HG12 . VAL C 1 51  ? 21.009  1.796   30.846  1.00 91.40  ? 51  VAL C HG12 1 
ATOM   9260  H HG13 . VAL C 1 51  ? 20.008  2.475   31.876  1.00 91.40  ? 51  VAL C HG13 1 
ATOM   9261  H HG21 . VAL C 1 51  ? 20.815  0.859   34.245  1.00 92.48  ? 51  VAL C HG21 1 
ATOM   9262  H HG22 . VAL C 1 51  ? 19.281  1.120   33.926  1.00 92.48  ? 51  VAL C HG22 1 
ATOM   9263  H HG23 . VAL C 1 51  ? 19.819  -0.367  34.076  1.00 92.48  ? 51  VAL C HG23 1 
ATOM   9264  N N    . GLY C 1 52  ? 18.435  1.471   29.748  1.00 75.79  ? 52  GLY C N    1 
ATOM   9265  C CA   . GLY C 1 52  ? 18.445  2.047   28.424  1.00 74.95  ? 52  GLY C CA   1 
ATOM   9266  C C    . GLY C 1 52  ? 18.733  3.537   28.489  1.00 74.67  ? 52  GLY C C    1 
ATOM   9267  O O    . GLY C 1 52  ? 18.675  4.159   29.556  1.00 78.67  ? 52  GLY C O    1 
ATOM   9268  H H    . GLY C 1 52  ? 17.931  1.888   30.306  1.00 90.95  ? 52  GLY C H    1 
ATOM   9269  H HA2  . GLY C 1 52  ? 19.130  1.620   27.885  1.00 89.93  ? 52  GLY C HA2  1 
ATOM   9270  H HA3  . GLY C 1 52  ? 17.582  1.914   28.001  1.00 89.93  ? 52  GLY C HA3  1 
ATOM   9271  N N    . PHE C 1 53  ? 19.045  4.100   27.323  1.00 75.92  ? 53  PHE C N    1 
ATOM   9272  C CA   . PHE C 1 53  ? 19.412  5.507   27.200  1.00 78.95  ? 53  PHE C CA   1 
ATOM   9273  C C    . PHE C 1 53  ? 18.698  6.093   25.991  1.00 79.16  ? 53  PHE C C    1 
ATOM   9274  O O    . PHE C 1 53  ? 18.890  5.622   24.866  1.00 78.26  ? 53  PHE C O    1 
ATOM   9275  C CB   . PHE C 1 53  ? 20.929  5.661   27.064  1.00 79.85  ? 53  PHE C CB   1 
ATOM   9276  C CG   . PHE C 1 53  ? 21.684  5.316   28.312  1.00 77.56  ? 53  PHE C CG   1 
ATOM   9277  C CD1  . PHE C 1 53  ? 22.015  4.001   28.598  1.00 74.86  ? 53  PHE C CD1  1 
ATOM   9278  C CD2  . PHE C 1 53  ? 22.056  6.308   29.204  1.00 78.36  ? 53  PHE C CD2  1 
ATOM   9279  C CE1  . PHE C 1 53  ? 22.705  3.685   29.750  1.00 79.04  ? 53  PHE C CE1  1 
ATOM   9280  C CE2  . PHE C 1 53  ? 22.747  5.997   30.361  1.00 79.53  ? 53  PHE C CE2  1 
ATOM   9281  C CZ   . PHE C 1 53  ? 23.072  4.684   30.632  1.00 82.79  ? 53  PHE C CZ   1 
ATOM   9282  H H    . PHE C 1 53  ? 19.050  3.677   26.574  1.00 91.11  ? 53  PHE C H    1 
ATOM   9283  H HA   . PHE C 1 53  ? 19.121  5.993   27.987  1.00 94.74  ? 53  PHE C HA   1 
ATOM   9284  H HB2  . PHE C 1 53  ? 21.241  5.075   26.357  1.00 95.82  ? 53  PHE C HB2  1 
ATOM   9285  H HB3  . PHE C 1 53  ? 21.130  6.584   26.842  1.00 95.82  ? 53  PHE C HB3  1 
ATOM   9286  H HD1  . PHE C 1 53  ? 21.769  3.326   28.008  1.00 89.84  ? 53  PHE C HD1  1 
ATOM   9287  H HD2  . PHE C 1 53  ? 21.838  7.194   29.023  1.00 94.03  ? 53  PHE C HD2  1 
ATOM   9288  H HE1  . PHE C 1 53  ? 22.924  2.800   29.933  1.00 94.85  ? 53  PHE C HE1  1 
ATOM   9289  H HE2  . PHE C 1 53  ? 22.992  6.671   30.954  1.00 95.43  ? 53  PHE C HE2  1 
ATOM   9290  H HZ   . PHE C 1 53  ? 23.538  4.471   31.409  1.00 99.35  ? 53  PHE C HZ   1 
ATOM   9291  N N    . ILE C 1 54  ? 17.891  7.131   26.224  1.00 86.54  ? 54  ILE C N    1 
ATOM   9292  C CA   . ILE C 1 54  ? 16.972  7.663   25.224  1.00 84.44  ? 54  ILE C CA   1 
ATOM   9293  C C    . ILE C 1 54  ? 17.618  8.819   24.469  1.00 82.19  ? 54  ILE C C    1 
ATOM   9294  O O    . ILE C 1 54  ? 18.428  9.581   25.007  1.00 85.16  ? 54  ILE C O    1 
ATOM   9295  C CB   . ILE C 1 54  ? 15.654  8.105   25.901  1.00 82.68  ? 54  ILE C CB   1 
ATOM   9296  C CG1  . ILE C 1 54  ? 14.674  6.932   26.007  1.00 83.67  ? 54  ILE C CG1  1 
ATOM   9297  C CG2  . ILE C 1 54  ? 15.009  9.262   25.148  1.00 88.09  ? 54  ILE C CG2  1 
ATOM   9298  C CD1  . ILE C 1 54  ? 13.523  7.186   26.965  1.00 80.52  ? 54  ILE C CD1  1 
ATOM   9299  H H    . ILE C 1 54  ? 17.859  7.553   26.974  1.00 103.84 ? 54  ILE C H    1 
ATOM   9300  H HA   . ILE C 1 54  ? 16.786  6.967   24.574  1.00 101.33 ? 54  ILE C HA   1 
ATOM   9301  H HB   . ILE C 1 54  ? 15.875  8.406   26.796  1.00 99.22  ? 54  ILE C HB   1 
ATOM   9302  H HG12 . ILE C 1 54  ? 14.298  6.759   25.130  1.00 100.41 ? 54  ILE C HG12 1 
ATOM   9303  H HG13 . ILE C 1 54  ? 15.156  6.151   26.322  1.00 100.41 ? 54  ILE C HG13 1 
ATOM   9304  H HG21 . ILE C 1 54  ? 14.118  9.411   25.501  1.00 105.71 ? 54  ILE C HG21 1 
ATOM   9305  H HG22 . ILE C 1 54  ? 15.550  10.058  25.270  1.00 105.71 ? 54  ILE C HG22 1 
ATOM   9306  H HG23 . ILE C 1 54  ? 14.959  9.037   24.206  1.00 105.71 ? 54  ILE C HG23 1 
ATOM   9307  H HD11 . ILE C 1 54  ? 13.027  6.361   27.087  1.00 96.62  ? 54  ILE C HD11 1 
ATOM   9308  H HD12 . ILE C 1 54  ? 13.881  7.486   27.816  1.00 96.62  ? 54  ILE C HD12 1 
ATOM   9309  H HD13 . ILE C 1 54  ? 12.945  7.868   26.590  1.00 96.62  ? 54  ILE C HD13 1 
ATOM   9310  N N    . LYS C 1 55  ? 17.243  8.950   23.198  1.00 80.40  ? 55  LYS C N    1 
ATOM   9311  C CA   . LYS C 1 55  ? 17.611  10.118  22.410  1.00 79.70  ? 55  LYS C CA   1 
ATOM   9312  C C    . LYS C 1 55  ? 16.569  10.246  21.312  1.00 78.95  ? 55  LYS C C    1 
ATOM   9313  O O    . LYS C 1 55  ? 16.570  9.448   20.367  1.00 80.20  ? 55  LYS C O    1 
ATOM   9314  C CB   . LYS C 1 55  ? 19.012  9.976   21.832  1.00 77.55  ? 55  LYS C CB   1 
ATOM   9315  C CG   . LYS C 1 55  ? 19.363  11.066  20.841  1.00 79.68  ? 55  LYS C CG   1 
ATOM   9316  C CD   . LYS C 1 55  ? 20.831  11.434  20.908  1.00 81.40  ? 55  LYS C CD   1 
ATOM   9317  C CE   . LYS C 1 55  ? 21.336  11.902  19.551  1.00 69.98  ? 55  LYS C CE   1 
ATOM   9318  N NZ   . LYS C 1 55  ? 22.397  12.937  19.700  1.00 74.44  ? 55  LYS C NZ   1 
ATOM   9319  H H    . LYS C 1 55  ? 16.773  8.372   22.769  1.00 96.48  ? 55  LYS C H    1 
ATOM   9320  H HA   . LYS C 1 55  ? 17.598  10.914  22.965  1.00 95.64  ? 55  LYS C HA   1 
ATOM   9321  H HB2  . LYS C 1 55  ? 19.656  10.013  22.556  1.00 93.06  ? 55  LYS C HB2  1 
ATOM   9322  H HB3  . LYS C 1 55  ? 19.077  9.124   21.373  1.00 93.06  ? 55  LYS C HB3  1 
ATOM   9323  H HG2  . LYS C 1 55  ? 19.168  10.757  19.942  1.00 95.62  ? 55  LYS C HG2  1 
ATOM   9324  H HG3  . LYS C 1 55  ? 18.841  11.859  21.039  1.00 95.62  ? 55  LYS C HG3  1 
ATOM   9325  H HD2  . LYS C 1 55  ? 20.955  12.153  21.547  1.00 97.68  ? 55  LYS C HD2  1 
ATOM   9326  H HD3  . LYS C 1 55  ? 21.347  10.658  21.178  1.00 97.68  ? 55  LYS C HD3  1 
ATOM   9327  H HE2  . LYS C 1 55  ? 21.709  11.147  19.068  1.00 83.98  ? 55  LYS C HE2  1 
ATOM   9328  H HE3  . LYS C 1 55  ? 20.601  12.286  19.048  1.00 83.98  ? 55  LYS C HE3  1 
ATOM   9329  H HZ1  . LYS C 1 55  ? 23.087  12.603  20.153  1.00 89.33  ? 55  LYS C HZ1  1 
ATOM   9330  H HZ2  . LYS C 1 55  ? 22.678  13.203  18.899  1.00 89.33  ? 55  LYS C HZ2  1 
ATOM   9331  H HZ3  . LYS C 1 55  ? 22.076  13.640  20.142  1.00 89.33  ? 55  LYS C HZ3  1 
ATOM   9332  N N    . ASP C 1 56  ? 15.667  11.215  21.447  1.00 77.84  ? 56  ASP C N    1 
ATOM   9333  C CA   . ASP C 1 56  ? 14.590  11.431  20.476  1.00 79.72  ? 56  ASP C CA   1 
ATOM   9334  C C    . ASP C 1 56  ? 13.777  10.144  20.416  1.00 79.36  ? 56  ASP C C    1 
ATOM   9335  O O    . ASP C 1 56  ? 13.232  9.736   21.457  1.00 77.95  ? 56  ASP C O    1 
ATOM   9336  C CB   . ASP C 1 56  ? 15.207  11.899  19.156  1.00 77.46  ? 56  ASP C CB   1 
ATOM   9337  C CG   . ASP C 1 56  ? 14.157  12.308  18.129  1.00 80.94  ? 56  ASP C CG   1 
ATOM   9338  O OD1  . ASP C 1 56  ? 12.984  12.500  18.512  1.00 83.32  ? 56  ASP C OD1  1 
ATOM   9339  O OD2  . ASP C 1 56  ? 14.506  12.439  16.935  1.00 81.31  ? 56  ASP C OD2  1 
ATOM   9340  H H    . ASP C 1 56  ? 15.655  11.771  22.103  1.00 93.41  ? 56  ASP C H    1 
ATOM   9341  H HA   . ASP C 1 56  ? 14.001  12.132  20.796  1.00 95.66  ? 56  ASP C HA   1 
ATOM   9342  H HB2  . ASP C 1 56  ? 15.775  12.666  19.327  1.00 92.96  ? 56  ASP C HB2  1 
ATOM   9343  H HB3  . ASP C 1 56  ? 15.731  11.176  18.778  1.00 92.96  ? 56  ASP C HB3  1 
ATOM   9344  N N    . SER C 1 57  ? 13.681  9.472   19.271  1.00 78.65  ? 57  SER C N    1 
ATOM   9345  C CA   . SER C 1 57  ? 12.904  8.249   19.145  1.00 78.92  ? 57  SER C CA   1 
ATOM   9346  C C    . SER C 1 57  ? 13.764  6.990   19.157  1.00 73.90  ? 57  SER C C    1 
ATOM   9347  O O    . SER C 1 57  ? 13.269  5.912   18.806  1.00 74.52  ? 57  SER C O    1 
ATOM   9348  C CB   . SER C 1 57  ? 12.073  8.291   17.861  1.00 78.79  ? 57  SER C CB   1 
ATOM   9349  O OG   . SER C 1 57  ? 12.858  8.748   16.774  1.00 84.14  ? 57  SER C OG   1 
ATOM   9350  H H    . SER C 1 57  ? 14.066  9.712   18.540  1.00 94.38  ? 57  SER C H    1 
ATOM   9351  H HA   . SER C 1 57  ? 12.298  8.196   19.901  1.00 94.70  ? 57  SER C HA   1 
ATOM   9352  H HB2  . SER C 1 57  ? 11.749  7.398   17.664  1.00 94.54  ? 57  SER C HB2  1 
ATOM   9353  H HB3  . SER C 1 57  ? 11.325  8.895   17.988  1.00 94.54  ? 57  SER C HB3  1 
ATOM   9354  H HG   . SER C 1 57  ? 12.391  8.780   16.076  1.00 100.97 ? 57  SER C HG   1 
ATOM   9355  N N    . HIS C 1 58  ? 15.028  7.096   19.567  1.00 75.74  ? 58  HIS C N    1 
ATOM   9356  C CA   . HIS C 1 58  ? 15.947  5.969   19.615  1.00 74.05  ? 58  HIS C CA   1 
ATOM   9357  C C    . HIS C 1 58  ? 16.182  5.521   21.050  1.00 77.17  ? 58  HIS C C    1 
ATOM   9358  O O    . HIS C 1 58  ? 16.224  6.336   21.973  1.00 75.93  ? 58  HIS C O    1 
ATOM   9359  C CB   . HIS C 1 58  ? 17.292  6.336   18.974  1.00 70.90  ? 58  HIS C CB   1 
ATOM   9360  C CG   . HIS C 1 58  ? 18.355  5.297   19.157  1.00 76.44  ? 58  HIS C CG   1 
ATOM   9361  N ND1  . HIS C 1 58  ? 18.301  4.065   18.541  1.00 79.10  ? 58  HIS C ND1  1 
ATOM   9362  C CD2  . HIS C 1 58  ? 19.498  5.306   19.885  1.00 75.82  ? 58  HIS C CD2  1 
ATOM   9363  C CE1  . HIS C 1 58  ? 19.367  3.361   18.878  1.00 78.35  ? 58  HIS C CE1  1 
ATOM   9364  N NE2  . HIS C 1 58  ? 20.109  4.090   19.693  1.00 77.36  ? 58  HIS C NE2  1 
ATOM   9365  H H    . HIS C 1 58  ? 15.382  7.834   19.829  1.00 90.88  ? 58  HIS C H    1 
ATOM   9366  H HA   . HIS C 1 58  ? 15.558  5.226   19.129  1.00 88.86  ? 58  HIS C HA   1 
ATOM   9367  H HB2  . HIS C 1 58  ? 17.160  6.459   18.021  1.00 85.08  ? 58  HIS C HB2  1 
ATOM   9368  H HB3  . HIS C 1 58  ? 17.612  7.160   19.374  1.00 85.08  ? 58  HIS C HB3  1 
ATOM   9369  H HD1  . HIS C 1 58  ? 17.673  3.797   18.020  1.00 94.91  ? 58  HIS C HD1  1 
ATOM   9370  H HD2  . HIS C 1 58  ? 19.811  6.004   20.415  1.00 90.99  ? 58  HIS C HD2  1 
ATOM   9371  H HE1  . HIS C 1 58  ? 19.563  2.498   18.590  1.00 94.02  ? 58  HIS C HE1  1 
ATOM   9372  H HE2  . HIS C 1 58  ? 20.854  3.844   20.046  1.00 92.83  ? 58  HIS C HE2  1 
ATOM   9373  N N    . LEU C 1 59  ? 16.348  4.212   21.220  1.00 78.86  ? 59  LEU C N    1 
ATOM   9374  C CA   . LEU C 1 59  ? 16.661  3.597   22.502  1.00 74.89  ? 59  LEU C CA   1 
ATOM   9375  C C    . LEU C 1 59  ? 17.993  2.874   22.366  1.00 76.60  ? 59  LEU C C    1 
ATOM   9376  O O    . LEU C 1 59  ? 18.139  1.990   21.514  1.00 78.94  ? 59  LEU C O    1 
ATOM   9377  C CB   . LEU C 1 59  ? 15.553  2.631   22.923  1.00 74.23  ? 59  LEU C CB   1 
ATOM   9378  C CG   . LEU C 1 59  ? 15.911  1.561   23.955  1.00 73.29  ? 59  LEU C CG   1 
ATOM   9379  C CD1  . LEU C 1 59  ? 16.382  2.200   25.245  1.00 75.20  ? 59  LEU C CD1  1 
ATOM   9380  C CD2  . LEU C 1 59  ? 14.706  0.663   24.198  1.00 73.67  ? 59  LEU C CD2  1 
ATOM   9381  H H    . LEU C 1 59  ? 16.282  3.640   20.581  1.00 94.63  ? 59  LEU C H    1 
ATOM   9382  H HA   . LEU C 1 59  ? 16.746  4.275   23.191  1.00 89.86  ? 59  LEU C HA   1 
ATOM   9383  H HB2  . LEU C 1 59  ? 14.830  3.155   23.301  1.00 89.08  ? 59  LEU C HB2  1 
ATOM   9384  H HB3  . LEU C 1 59  ? 15.247  2.165   22.129  1.00 89.08  ? 59  LEU C HB3  1 
ATOM   9385  H HG   . LEU C 1 59  ? 16.638  1.014   23.619  1.00 87.95  ? 59  LEU C HG   1 
ATOM   9386  H HD11 . LEU C 1 59  ? 16.512  1.506   25.911  1.00 90.24  ? 59  LEU C HD11 1 
ATOM   9387  H HD12 . LEU C 1 59  ? 17.218  2.663   25.082  1.00 90.24  ? 59  LEU C HD12 1 
ATOM   9388  H HD13 . LEU C 1 59  ? 15.709  2.829   25.550  1.00 90.24  ? 59  LEU C HD13 1 
ATOM   9389  H HD21 . LEU C 1 59  ? 14.947  -0.021  24.843  1.00 88.40  ? 59  LEU C HD21 1 
ATOM   9390  H HD22 . LEU C 1 59  ? 13.976  1.201   24.544  1.00 88.40  ? 59  LEU C HD22 1 
ATOM   9391  H HD23 . LEU C 1 59  ? 14.444  0.251   23.360  1.00 88.40  ? 59  LEU C HD23 1 
ATOM   9392  N N    . GLN C 1 60  ? 18.963  3.257   23.193  1.00 78.30  ? 60  GLN C N    1 
ATOM   9393  C CA   . GLN C 1 60  ? 20.305  2.679   23.168  1.00 78.08  ? 60  GLN C CA   1 
ATOM   9394  C C    . GLN C 1 60  ? 20.488  1.850   24.434  1.00 77.27  ? 60  GLN C C    1 
ATOM   9395  O O    . GLN C 1 60  ? 20.740  2.396   25.511  1.00 76.64  ? 60  GLN C O    1 
ATOM   9396  C CB   . GLN C 1 60  ? 21.365  3.773   23.062  1.00 74.87  ? 60  GLN C CB   1 
ATOM   9397  C CG   . GLN C 1 60  ? 22.786  3.253   22.931  1.00 76.45  ? 60  GLN C CG   1 
ATOM   9398  C CD   . GLN C 1 60  ? 23.087  2.764   21.538  1.00 76.17  ? 60  GLN C CD   1 
ATOM   9399  O OE1  . GLN C 1 60  ? 22.210  2.749   20.676  1.00 77.27  ? 60  GLN C OE1  1 
ATOM   9400  N NE2  . GLN C 1 60  ? 24.332  2.364   21.301  1.00 77.76  ? 60  GLN C NE2  1 
ATOM   9401  H H    . GLN C 1 60  ? 18.865  3.865   23.793  1.00 93.95  ? 60  GLN C H    1 
ATOM   9402  H HA   . GLN C 1 60  ? 20.388  2.092   22.400  1.00 93.70  ? 60  GLN C HA   1 
ATOM   9403  H HB2  . GLN C 1 60  ? 21.175  4.314   22.279  1.00 89.84  ? 60  GLN C HB2  1 
ATOM   9404  H HB3  . GLN C 1 60  ? 21.324  4.321   23.861  1.00 89.84  ? 60  GLN C HB3  1 
ATOM   9405  H HG2  . GLN C 1 60  ? 23.407  3.968   23.141  1.00 91.74  ? 60  GLN C HG2  1 
ATOM   9406  H HG3  . GLN C 1 60  ? 22.912  2.513   23.545  1.00 91.74  ? 60  GLN C HG3  1 
ATOM   9407  H HE21 . GLN C 1 60  ? 24.919  2.393   21.929  1.00 93.31  ? 60  GLN C HE21 1 
ATOM   9408  H HE22 . GLN C 1 60  ? 24.550  2.077   20.521  1.00 93.31  ? 60  GLN C HE22 1 
ATOM   9409  N N    . MET C 1 61  ? 20.366  0.532   24.301  1.00 75.40  ? 61  MET C N    1 
ATOM   9410  C CA   . MET C 1 61  ? 20.540  -0.353  25.444  1.00 79.07  ? 61  MET C CA   1 
ATOM   9411  C C    . MET C 1 61  ? 21.998  -0.362  25.897  1.00 82.71  ? 61  MET C C    1 
ATOM   9412  O O    . MET C 1 61  ? 22.920  -0.057  25.131  1.00 80.90  ? 61  MET C O    1 
ATOM   9413  C CB   . MET C 1 61  ? 20.089  -1.773  25.105  1.00 81.55  ? 61  MET C CB   1 
ATOM   9414  C CG   . MET C 1 61  ? 18.638  -1.875  24.659  1.00 82.78  ? 61  MET C CG   1 
ATOM   9415  S SD   . MET C 1 61  ? 17.463  -1.200  25.857  1.00 81.27  ? 61  MET C SD   1 
ATOM   9416  C CE   . MET C 1 61  ? 17.436  -2.486  27.102  1.00 79.34  ? 61  MET C CE   1 
ATOM   9417  H H    . MET C 1 61  ? 20.183  0.128   23.564  1.00 90.48  ? 61  MET C H    1 
ATOM   9418  H HA   . MET C 1 61  ? 19.985  -0.035  26.173  1.00 94.88  ? 61  MET C HA   1 
ATOM   9419  H HB2  . MET C 1 61  ? 20.644  -2.111  24.384  1.00 97.87  ? 61  MET C HB2  1 
ATOM   9420  H HB3  . MET C 1 61  ? 20.195  -2.329  25.893  1.00 97.87  ? 61  MET C HB3  1 
ATOM   9421  H HG2  . MET C 1 61  ? 18.530  -1.384  23.829  1.00 99.34  ? 61  MET C HG2  1 
ATOM   9422  H HG3  . MET C 1 61  ? 18.418  -2.810  24.522  1.00 99.34  ? 61  MET C HG3  1 
ATOM   9423  H HE1  . MET C 1 61  ? 16.821  -2.230  27.807  1.00 95.20  ? 61  MET C HE1  1 
ATOM   9424  H HE2  . MET C 1 61  ? 17.143  -3.315  26.693  1.00 95.20  ? 61  MET C HE2  1 
ATOM   9425  H HE3  . MET C 1 61  ? 18.329  -2.593  27.465  1.00 95.20  ? 61  MET C HE3  1 
ATOM   9426  N N    . MET C 1 62  ? 22.194  -0.753  27.165  1.00 81.07  ? 62  MET C N    1 
ATOM   9427  C CA   . MET C 1 62  ? 23.471  -0.550  27.836  1.00 81.38  ? 62  MET C CA   1 
ATOM   9428  C C    . MET C 1 62  ? 24.633  -1.238  27.134  1.00 80.46  ? 62  MET C C    1 
ATOM   9429  O O    . MET C 1 62  ? 25.789  -0.873  27.382  1.00 81.05  ? 62  MET C O    1 
ATOM   9430  C CB   . MET C 1 62  ? 23.391  -1.043  29.291  1.00 81.94  ? 62  MET C CB   1 
ATOM   9431  C CG   . MET C 1 62  ? 22.411  -2.197  29.547  1.00 85.72  ? 62  MET C CG   1 
ATOM   9432  S SD   . MET C 1 62  ? 22.733  -3.132  31.065  1.00 83.32  ? 62  MET C SD   1 
ATOM   9433  C CE   . MET C 1 62  ? 24.386  -3.753  30.727  1.00 87.42  ? 62  MET C CE   1 
ATOM   9434  H H    . MET C 1 62  ? 21.600  -1.138  27.653  1.00 97.28  ? 62  MET C H    1 
ATOM   9435  H HA   . MET C 1 62  ? 23.644  0.405   27.846  1.00 97.65  ? 62  MET C HA   1 
ATOM   9436  H HB2  . MET C 1 62  ? 24.272  -1.348  29.558  1.00 98.33  ? 62  MET C HB2  1 
ATOM   9437  H HB3  . MET C 1 62  ? 23.115  -0.299  29.850  1.00 98.33  ? 62  MET C HB3  1 
ATOM   9438  H HG2  . MET C 1 62  ? 21.514  -1.832  29.613  1.00 102.87 ? 62  MET C HG2  1 
ATOM   9439  H HG3  . MET C 1 62  ? 22.463  -2.818  28.804  1.00 102.87 ? 62  MET C HG3  1 
ATOM   9440  H HE1  . MET C 1 62  ? 24.589  -4.466  31.351  1.00 104.90 ? 62  MET C HE1  1 
ATOM   9441  H HE2  . MET C 1 62  ? 24.416  -4.090  29.818  1.00 104.90 ? 62  MET C HE2  1 
ATOM   9442  H HE3  . MET C 1 62  ? 25.023  -3.029  30.832  1.00 104.90 ? 62  MET C HE3  1 
ATOM   9443  N N    . GLY C 1 63  ? 24.365  -2.213  26.270  1.00 82.55  ? 63  GLY C N    1 
ATOM   9444  C CA   . GLY C 1 63  ? 25.435  -2.917  25.592  1.00 83.63  ? 63  GLY C CA   1 
ATOM   9445  C C    . GLY C 1 63  ? 25.397  -2.814  24.081  1.00 85.37  ? 63  GLY C C    1 
ATOM   9446  O O    . GLY C 1 63  ? 26.338  -3.232  23.398  1.00 88.17  ? 63  GLY C O    1 
ATOM   9447  H H    . GLY C 1 63  ? 23.574  -2.480  26.063  1.00 99.06  ? 63  GLY C H    1 
ATOM   9448  H HA2  . GLY C 1 63  ? 26.285  -2.559  25.893  1.00 100.36 ? 63  GLY C HA2  1 
ATOM   9449  H HA3  . GLY C 1 63  ? 25.388  -3.857  25.827  1.00 100.36 ? 63  GLY C HA3  1 
ATOM   9450  N N    . GLY C 1 64  ? 24.304  -2.274  23.546  1.00 85.25  ? 64  GLY C N    1 
ATOM   9451  C CA   . GLY C 1 64  ? 24.118  -2.222  22.111  1.00 84.90  ? 64  GLY C CA   1 
ATOM   9452  C C    . GLY C 1 64  ? 23.317  -3.367  21.545  1.00 83.41  ? 64  GLY C C    1 
ATOM   9453  O O    . GLY C 1 64  ? 23.564  -3.780  20.404  1.00 84.65  ? 64  GLY C O    1 
ATOM   9454  H H    . GLY C 1 64  ? 23.657  -1.932  23.998  1.00 102.30 ? 64  GLY C H    1 
ATOM   9455  H HA2  . GLY C 1 64  ? 23.659  -1.397  21.885  1.00 101.88 ? 64  GLY C HA2  1 
ATOM   9456  H HA3  . GLY C 1 64  ? 24.988  -2.227  21.683  1.00 101.88 ? 64  GLY C HA3  1 
ATOM   9457  N N    . GLU C 1 65  ? 22.366  -3.898  22.313  1.00 80.97  ? 65  GLU C N    1 
ATOM   9458  C CA   . GLU C 1 65  ? 21.638  -5.105  21.964  1.00 80.46  ? 65  GLU C CA   1 
ATOM   9459  C C    . GLU C 1 65  ? 20.144  -4.823  21.991  1.00 76.89  ? 65  GLU C C    1 
ATOM   9460  O O    . GLU C 1 65  ? 19.669  -3.972  22.745  1.00 79.45  ? 65  GLU C O    1 
ATOM   9461  C CB   . GLU C 1 65  ? 21.981  -6.266  22.923  1.00 78.33  ? 65  GLU C CB   1 
ATOM   9462  C CG   . GLU C 1 65  ? 21.669  -6.040  24.405  1.00 86.27  ? 65  GLU C CG   1 
ATOM   9463  C CD   . GLU C 1 65  ? 22.416  -4.862  24.998  1.00 84.48  ? 65  GLU C CD   1 
ATOM   9464  O OE1  . GLU C 1 65  ? 23.180  -4.219  24.259  1.00 87.87  ? 65  GLU C OE1  1 
ATOM   9465  O OE2  . GLU C 1 65  ? 22.227  -4.579  26.197  1.00 81.07  ? 65  GLU C OE2  1 
ATOM   9466  H H    . GLU C 1 65  ? 22.121  -3.563  23.066  1.00 97.16  ? 65  GLU C H    1 
ATOM   9467  H HA   . GLU C 1 65  ? 21.871  -5.381  21.064  1.00 96.55  ? 65  GLU C HA   1 
ATOM   9468  H HB2  . GLU C 1 65  ? 21.480  -7.048  22.642  1.00 93.99  ? 65  GLU C HB2  1 
ATOM   9469  H HB3  . GLU C 1 65  ? 22.933  -6.441  22.856  1.00 93.99  ? 65  GLU C HB3  1 
ATOM   9470  H HG2  . GLU C 1 65  ? 20.719  -5.871  24.504  1.00 103.52 ? 65  GLU C HG2  1 
ATOM   9471  H HG3  . GLU C 1 65  ? 21.919  -6.833  24.904  1.00 103.52 ? 65  GLU C HG3  1 
ATOM   9472  N N    . PHE C 1 66  ? 19.408  -5.547  21.161  1.00 77.12  ? 66  PHE C N    1 
ATOM   9473  C CA   . PHE C 1 66  ? 17.974  -5.344  21.071  1.00 76.10  ? 66  PHE C CA   1 
ATOM   9474  C C    . PHE C 1 66  ? 17.269  -5.983  22.259  1.00 73.14  ? 66  PHE C C    1 
ATOM   9475  O O    . PHE C 1 66  ? 17.682  -7.023  22.779  1.00 73.76  ? 66  PHE C O    1 
ATOM   9476  C CB   . PHE C 1 66  ? 17.438  -5.936  19.772  1.00 77.42  ? 66  PHE C CB   1 
ATOM   9477  C CG   . PHE C 1 66  ? 15.953  -5.846  19.635  1.00 75.81  ? 66  PHE C CG   1 
ATOM   9478  C CD1  . PHE C 1 66  ? 15.324  -4.617  19.526  1.00 78.01  ? 66  PHE C CD1  1 
ATOM   9479  C CD2  . PHE C 1 66  ? 15.182  -6.993  19.625  1.00 71.85  ? 66  PHE C CD2  1 
ATOM   9480  C CE1  . PHE C 1 66  ? 13.952  -4.536  19.400  1.00 77.65  ? 66  PHE C CE1  1 
ATOM   9481  C CE2  . PHE C 1 66  ? 13.813  -6.915  19.498  1.00 74.34  ? 66  PHE C CE2  1 
ATOM   9482  C CZ   . PHE C 1 66  ? 13.194  -5.687  19.387  1.00 76.37  ? 66  PHE C CZ   1 
ATOM   9483  H H    . PHE C 1 66  ? 19.715  -6.159  20.641  1.00 92.54  ? 66  PHE C H    1 
ATOM   9484  H HA   . PHE C 1 66  ? 17.779  -4.394  21.076  1.00 91.32  ? 66  PHE C HA   1 
ATOM   9485  H HB2  . PHE C 1 66  ? 17.834  -5.459  19.026  1.00 92.91  ? 66  PHE C HB2  1 
ATOM   9486  H HB3  . PHE C 1 66  ? 17.682  -6.874  19.733  1.00 92.91  ? 66  PHE C HB3  1 
ATOM   9487  H HD1  . PHE C 1 66  ? 15.831  -3.838  19.537  1.00 93.61  ? 66  PHE C HD1  1 
ATOM   9488  H HD2  . PHE C 1 66  ? 15.591  -7.824  19.704  1.00 86.22  ? 66  PHE C HD2  1 
ATOM   9489  H HE1  . PHE C 1 66  ? 13.539  -3.706  19.326  1.00 93.18  ? 66  PHE C HE1  1 
ATOM   9490  H HE2  . PHE C 1 66  ? 13.303  -7.693  19.488  1.00 89.21  ? 66  PHE C HE2  1 
ATOM   9491  H HZ   . PHE C 1 66  ? 12.269  -5.636  19.302  1.00 91.65  ? 66  PHE C HZ   1 
ATOM   9492  N N    . SER C 1 67  ? 16.192  -5.334  22.697  1.00 72.80  ? 67  SER C N    1 
ATOM   9493  C CA   . SER C 1 67  ? 15.329  -5.868  23.748  1.00 74.59  ? 67  SER C CA   1 
ATOM   9494  C C    . SER C 1 67  ? 13.891  -5.507  23.402  1.00 72.28  ? 67  SER C C    1 
ATOM   9495  O O    . SER C 1 67  ? 13.532  -4.326  23.388  1.00 73.56  ? 67  SER C O    1 
ATOM   9496  C CB   . SER C 1 67  ? 15.712  -5.321  25.121  1.00 74.55  ? 67  SER C CB   1 
ATOM   9497  O OG   . SER C 1 67  ? 14.681  -5.561  26.068  1.00 74.99  ? 67  SER C OG   1 
ATOM   9498  H H    . SER C 1 67  ? 15.936  -4.570  22.395  1.00 87.36  ? 67  SER C H    1 
ATOM   9499  H HA   . SER C 1 67  ? 15.412  -6.834  23.772  1.00 89.51  ? 67  SER C HA   1 
ATOM   9500  H HB2  . SER C 1 67  ? 16.524  -5.759  25.420  1.00 89.46  ? 67  SER C HB2  1 
ATOM   9501  H HB3  . SER C 1 67  ? 15.859  -4.364  25.049  1.00 89.46  ? 67  SER C HB3  1 
ATOM   9502  H HG   . SER C 1 67  ? 14.548  -6.386  26.145  1.00 89.99  ? 67  SER C HG   1 
ATOM   9503  N N    . GLY C 1 68  ? 13.073  -6.520  23.119  1.00 73.99  ? 68  GLY C N    1 
ATOM   9504  C CA   . GLY C 1 68  ? 11.669  -6.263  22.855  1.00 73.43  ? 68  GLY C CA   1 
ATOM   9505  C C    . GLY C 1 68  ? 10.953  -5.658  24.046  1.00 73.52  ? 68  GLY C C    1 
ATOM   9506  O O    . GLY C 1 68  ? 10.109  -4.772  23.891  1.00 73.39  ? 68  GLY C O    1 
ATOM   9507  H H    . GLY C 1 68  ? 13.304  -7.348  23.075  1.00 88.78  ? 68  GLY C H    1 
ATOM   9508  H HA2  . GLY C 1 68  ? 11.591  -5.649  22.108  1.00 88.12  ? 68  GLY C HA2  1 
ATOM   9509  H HA3  . GLY C 1 68  ? 11.228  -7.096  22.626  1.00 88.12  ? 68  GLY C HA3  1 
ATOM   9510  N N    . ASN C 1 69  ? 11.276  -6.129  25.254  1.00 73.49  ? 69  ASN C N    1 
ATOM   9511  C CA   . ASN C 1 69  ? 10.641  -5.587  26.451  1.00 74.83  ? 69  ASN C CA   1 
ATOM   9512  C C    . ASN C 1 69  ? 10.985  -4.112  26.630  1.00 73.46  ? 69  ASN C C    1 
ATOM   9513  O O    . ASN C 1 69  ? 10.099  -3.276  26.852  1.00 71.14  ? 69  ASN C O    1 
ATOM   9514  C CB   . ASN C 1 69  ? 11.065  -6.388  27.683  1.00 74.36  ? 69  ASN C CB   1 
ATOM   9515  C CG   . ASN C 1 69  ? 10.245  -7.661  27.865  1.00 80.49  ? 69  ASN C CG   1 
ATOM   9516  O OD1  . ASN C 1 69  ? 10.796  -8.762  27.978  1.00 84.13  ? 69  ASN C OD1  1 
ATOM   9517  N ND2  . ASN C 1 69  ? 8.922   -7.515  27.892  1.00 78.98  ? 69  ASN C ND2  1 
ATOM   9518  H H    . ASN C 1 69  ? 11.851  -6.751  25.403  1.00 88.19  ? 69  ASN C H    1 
ATOM   9519  H HA   . ASN C 1 69  ? 9.679   -5.669  26.357  1.00 89.79  ? 69  ASN C HA   1 
ATOM   9520  H HB2  . ASN C 1 69  ? 11.997  -6.641  27.591  1.00 89.23  ? 69  ASN C HB2  1 
ATOM   9521  H HB3  . ASN C 1 69  ? 10.947  -5.839  28.474  1.00 89.23  ? 69  ASN C HB3  1 
ATOM   9522  H HD21 . ASN C 1 69  ? 8.575   -6.732  27.809  1.00 94.78  ? 69  ASN C HD21 1 
ATOM   9523  H HD22 . ASN C 1 69  ? 8.415   -8.202  27.993  1.00 94.78  ? 69  ASN C HD22 1 
ATOM   9524  N N    . ALA C 1 70  ? 12.275  -3.771  26.537  1.00 72.81  ? 70  ALA C N    1 
ATOM   9525  C CA   . ALA C 1 70  ? 12.683  -2.377  26.682  1.00 71.00  ? 70  ALA C CA   1 
ATOM   9526  C C    . ALA C 1 70  ? 11.996  -1.499  25.645  1.00 69.95  ? 70  ALA C C    1 
ATOM   9527  O O    . ALA C 1 70  ? 11.430  -0.454  25.979  1.00 72.86  ? 70  ALA C O    1 
ATOM   9528  C CB   . ALA C 1 70  ? 14.202  -2.254  26.564  1.00 72.31  ? 70  ALA C CB   1 
ATOM   9529  H H    . ALA C 1 70  ? 12.921  -4.321  26.392  1.00 87.37  ? 70  ALA C H    1 
ATOM   9530  H HA   . ALA C 1 70  ? 12.426  -2.069  27.565  1.00 85.20  ? 70  ALA C HA   1 
ATOM   9531  H HB1  . ALA C 1 70  ? 14.454  -1.325  26.680  1.00 86.77  ? 70  ALA C HB1  1 
ATOM   9532  H HB2  . ALA C 1 70  ? 14.617  -2.798  27.252  1.00 86.77  ? 70  ALA C HB2  1 
ATOM   9533  H HB3  . ALA C 1 70  ? 14.477  -2.564  25.687  1.00 86.77  ? 70  ALA C HB3  1 
ATOM   9534  N N    . SER C 1 71  ? 12.035  -1.909  24.374  1.00 71.74  ? 71  SER C N    1 
ATOM   9535  C CA   . SER C 1 71  ? 11.372  -1.135  23.327  1.00 72.96  ? 71  SER C CA   1 
ATOM   9536  C C    . SER C 1 71  ? 9.892   -0.950  23.642  1.00 69.61  ? 71  SER C C    1 
ATOM   9537  O O    . SER C 1 71  ? 9.352   0.155   23.507  1.00 68.77  ? 71  SER C O    1 
ATOM   9538  C CB   . SER C 1 71  ? 11.557  -1.819  21.973  1.00 74.70  ? 71  SER C CB   1 
ATOM   9539  O OG   . SER C 1 71  ? 12.930  -1.911  21.628  1.00 72.50  ? 71  SER C OG   1 
ATOM   9540  H H    . SER C 1 71  ? 12.433  -2.619  24.097  1.00 86.09  ? 71  SER C H    1 
ATOM   9541  H HA   . SER C 1 71  ? 11.782  -0.257  23.275  1.00 87.56  ? 71  SER C HA   1 
ATOM   9542  H HB2  . SER C 1 71  ? 11.183  -2.713  22.019  1.00 89.64  ? 71  SER C HB2  1 
ATOM   9543  H HB3  . SER C 1 71  ? 11.096  -1.301  21.294  1.00 89.64  ? 71  SER C HB3  1 
ATOM   9544  H HG   . SER C 1 71  ? 13.340  -2.368  22.202  1.00 87.00  ? 71  SER C HG   1 
ATOM   9545  N N    . ARG C 1 72  ? 9.221   -2.021  24.070  1.00 70.82  ? 72  ARG C N    1 
ATOM   9546  C CA   . ARG C 1 72  ? 7.840   -1.899  24.529  1.00 72.81  ? 72  ARG C CA   1 
ATOM   9547  C C    . ARG C 1 72  ? 7.721   -0.899  25.674  1.00 72.15  ? 72  ARG C C    1 
ATOM   9548  O O    . ARG C 1 72  ? 6.730   -0.162  25.766  1.00 73.04  ? 72  ARG C O    1 
ATOM   9549  C CB   . ARG C 1 72  ? 7.310   -3.269  24.963  1.00 76.58  ? 72  ARG C CB   1 
ATOM   9550  C CG   . ARG C 1 72  ? 7.094   -4.248  23.817  1.00 73.57  ? 72  ARG C CG   1 
ATOM   9551  C CD   . ARG C 1 72  ? 7.051   -5.700  24.296  1.00 76.29  ? 72  ARG C CD   1 
ATOM   9552  N NE   . ARG C 1 72  ? 6.905   -5.842  25.741  1.00 76.71  ? 72  ARG C NE   1 
ATOM   9553  C CZ   . ARG C 1 72  ? 5.748   -5.792  26.389  1.00 79.53  ? 72  ARG C CZ   1 
ATOM   9554  N NH1  . ARG C 1 72  ? 4.609   -5.569  25.755  1.00 80.29  ? 72  ARG C NH1  1 
ATOM   9555  N NH2  . ARG C 1 72  ? 5.734   -5.972  27.707  1.00 78.70  ? 72  ARG C NH2  1 
ATOM   9556  H H    . ARG C 1 72  ? 9.539   -2.819  24.105  1.00 84.99  ? 72  ARG C H    1 
ATOM   9557  H HA   . ARG C 1 72  ? 7.295   -1.579  23.792  1.00 87.37  ? 72  ARG C HA   1 
ATOM   9558  H HB2  . ARG C 1 72  ? 7.948   -3.668  25.575  1.00 91.90  ? 72  ARG C HB2  1 
ATOM   9559  H HB3  . ARG C 1 72  ? 6.457   -3.144  25.408  1.00 91.90  ? 72  ARG C HB3  1 
ATOM   9560  H HG2  . ARG C 1 72  ? 6.250   -4.048  23.383  1.00 88.29  ? 72  ARG C HG2  1 
ATOM   9561  H HG3  . ARG C 1 72  ? 7.822   -4.161  23.183  1.00 88.29  ? 72  ARG C HG3  1 
ATOM   9562  H HD2  . ARG C 1 72  ? 6.296   -6.144  23.878  1.00 91.55  ? 72  ARG C HD2  1 
ATOM   9563  H HD3  . ARG C 1 72  ? 7.877   -6.138  24.038  1.00 91.55  ? 72  ARG C HD3  1 
ATOM   9564  H HE   . ARG C 1 72  ? 7.618   -5.967  26.205  1.00 92.05  ? 72  ARG C HE   1 
ATOM   9565  H HH11 . ARG C 1 72  ? 4.607   -5.453  24.903  1.00 96.35  ? 72  ARG C HH11 1 
ATOM   9566  H HH12 . ARG C 1 72  ? 3.871   -5.540  26.195  1.00 96.35  ? 72  ARG C HH12 1 
ATOM   9567  H HH21 . ARG C 1 72  ? 6.468   -6.120  28.128  1.00 94.44  ? 72  ARG C HH21 1 
ATOM   9568  H HH22 . ARG C 1 72  ? 4.990   -5.942  28.137  1.00 94.44  ? 72  ARG C HH22 1 
ATOM   9569  N N    . ALA C 1 73  ? 8.711   -0.867  26.569  1.00 73.33  ? 73  ALA C N    1 
ATOM   9570  C CA   . ALA C 1 73  ? 8.677   0.105   27.658  1.00 71.87  ? 73  ALA C CA   1 
ATOM   9571  C C    . ALA C 1 73  ? 8.896   1.520   27.133  1.00 70.68  ? 73  ALA C C    1 
ATOM   9572  O O    . ALA C 1 73  ? 8.186   2.452   27.526  1.00 70.62  ? 73  ALA C O    1 
ATOM   9573  C CB   . ALA C 1 73  ? 9.728   -0.246  28.708  1.00 70.88  ? 73  ALA C CB   1 
ATOM   9574  H H    . ALA C 1 73  ? 9.398   -1.385  26.567  1.00 87.99  ? 73  ALA C H    1 
ATOM   9575  H HA   . ALA C 1 73  ? 7.806   0.071   28.085  1.00 86.24  ? 73  ALA C HA   1 
ATOM   9576  H HB1  . ALA C 1 73  ? 9.708   0.421   29.411  1.00 85.06  ? 73  ALA C HB1  1 
ATOM   9577  H HB2  . ALA C 1 73  ? 9.526   -1.121  29.077  1.00 85.06  ? 73  ALA C HB2  1 
ATOM   9578  H HB3  . ALA C 1 73  ? 10.602  -0.258  28.288  1.00 85.06  ? 73  ALA C HB3  1 
ATOM   9579  N N    . PHE C 1 74  ? 9.867   1.693   26.233  1.00 71.55  ? 74  PHE C N    1 
ATOM   9580  C CA   . PHE C 1 74  ? 10.112  3.001   25.632  1.00 73.68  ? 74  PHE C CA   1 
ATOM   9581  C C    . PHE C 1 74  ? 8.869   3.525   24.923  1.00 71.38  ? 74  PHE C C    1 
ATOM   9582  O O    . PHE C 1 74  ? 8.449   4.666   25.146  1.00 72.55  ? 74  PHE C O    1 
ATOM   9583  C CB   . PHE C 1 74  ? 11.290  2.907   24.660  1.00 72.02  ? 74  PHE C CB   1 
ATOM   9584  C CG   . PHE C 1 74  ? 11.655  4.211   24.013  1.00 71.92  ? 74  PHE C CG   1 
ATOM   9585  C CD1  . PHE C 1 74  ? 11.348  5.420   24.619  1.00 73.30  ? 74  PHE C CD1  1 
ATOM   9586  C CD2  . PHE C 1 74  ? 12.313  4.229   22.799  1.00 75.83  ? 74  PHE C CD2  1 
ATOM   9587  C CE1  . PHE C 1 74  ? 11.681  6.619   24.015  1.00 73.16  ? 74  PHE C CE1  1 
ATOM   9588  C CE2  . PHE C 1 74  ? 12.650  5.424   22.195  1.00 76.14  ? 74  PHE C CE2  1 
ATOM   9589  C CZ   . PHE C 1 74  ? 12.335  6.621   22.808  1.00 74.37  ? 74  PHE C CZ   1 
ATOM   9590  H H    . PHE C 1 74  ? 10.394  1.073   25.956  1.00 85.86  ? 74  PHE C H    1 
ATOM   9591  H HA   . PHE C 1 74  ? 10.342  3.633   26.331  1.00 88.42  ? 74  PHE C HA   1 
ATOM   9592  H HB2  . PHE C 1 74  ? 12.069  2.590   25.144  1.00 86.43  ? 74  PHE C HB2  1 
ATOM   9593  H HB3  . PHE C 1 74  ? 11.062  2.281   23.954  1.00 86.43  ? 74  PHE C HB3  1 
ATOM   9594  H HD1  . PHE C 1 74  ? 10.912  5.424   25.441  1.00 87.96  ? 74  PHE C HD1  1 
ATOM   9595  H HD2  . PHE C 1 74  ? 12.531  3.426   22.383  1.00 91.00  ? 74  PHE C HD2  1 
ATOM   9596  H HE1  . PHE C 1 74  ? 11.462  7.424   24.427  1.00 87.79  ? 74  PHE C HE1  1 
ATOM   9597  H HE2  . PHE C 1 74  ? 13.090  5.423   21.375  1.00 91.37  ? 74  PHE C HE2  1 
ATOM   9598  H HZ   . PHE C 1 74  ? 12.565  7.426   22.404  1.00 89.24  ? 74  PHE C HZ   1 
ATOM   9599  N N    . ALA C 1 75  ? 8.272   2.708   24.054  1.00 71.34  ? 75  ALA C N    1 
ATOM   9600  C CA   . ALA C 1 75  ? 7.075   3.148   23.344  1.00 72.56  ? 75  ALA C CA   1 
ATOM   9601  C C    . ALA C 1 75  ? 5.963   3.509   24.322  1.00 73.85  ? 75  ALA C C    1 
ATOM   9602  O O    . ALA C 1 75  ? 5.288   4.532   24.160  1.00 74.84  ? 75  ALA C O    1 
ATOM   9603  C CB   . ALA C 1 75  ? 6.607   2.062   22.377  1.00 73.17  ? 75  ALA C CB   1 
ATOM   9604  H H    . ALA C 1 75  ? 8.534   1.912   23.862  1.00 85.61  ? 75  ALA C H    1 
ATOM   9605  H HA   . ALA C 1 75  ? 7.290   3.938   22.824  1.00 87.07  ? 75  ALA C HA   1 
ATOM   9606  H HB1  . ALA C 1 75  ? 5.811   2.371   21.917  1.00 87.80  ? 75  ALA C HB1  1 
ATOM   9607  H HB2  . ALA C 1 75  ? 7.312   1.886   21.735  1.00 87.80  ? 75  ALA C HB2  1 
ATOM   9608  H HB3  . ALA C 1 75  ? 6.408   1.257   22.879  1.00 87.80  ? 75  ALA C HB3  1 
ATOM   9609  N N    . SER C 1 76  ? 5.764   2.685   25.353  1.00 72.46  ? 76  SER C N    1 
ATOM   9610  C CA   . SER C 1 76  ? 4.752   3.002   26.356  1.00 75.17  ? 76  SER C CA   1 
ATOM   9611  C C    . SER C 1 76  ? 5.035   4.352   27.003  1.00 75.20  ? 76  SER C C    1 
ATOM   9612  O O    . SER C 1 76  ? 4.108   5.114   27.311  1.00 74.06  ? 76  SER C O    1 
ATOM   9613  C CB   . SER C 1 76  ? 4.700   1.895   27.408  1.00 74.54  ? 76  SER C CB   1 
ATOM   9614  O OG   . SER C 1 76  ? 4.275   0.680   26.824  1.00 74.86  ? 76  SER C OG   1 
ATOM   9615  H H    . SER C 1 76  ? 6.193   1.953   25.491  1.00 86.95  ? 76  SER C H    1 
ATOM   9616  H HA   . SER C 1 76  ? 3.882   3.049   25.930  1.00 90.21  ? 76  SER C HA   1 
ATOM   9617  H HB2  . SER C 1 76  ? 5.585   1.774   27.786  1.00 89.45  ? 76  SER C HB2  1 
ATOM   9618  H HB3  . SER C 1 76  ? 4.074   2.149   28.105  1.00 89.45  ? 76  SER C HB3  1 
ATOM   9619  H HG   . SER C 1 76  ? 4.819   0.440   26.231  1.00 89.83  ? 76  SER C HG   1 
ATOM   9620  N N    . LEU C 1 77  ? 6.313   4.670   27.209  1.00 74.07  ? 77  LEU C N    1 
ATOM   9621  C CA   . LEU C 1 77  ? 6.670   5.966   27.774  1.00 73.34  ? 77  LEU C CA   1 
ATOM   9622  C C    . LEU C 1 77  ? 6.291   7.089   26.820  1.00 74.45  ? 77  LEU C C    1 
ATOM   9623  O O    . LEU C 1 77  ? 5.728   8.108   27.234  1.00 73.54  ? 77  LEU C O    1 
ATOM   9624  C CB   . LEU C 1 77  ? 8.165   6.002   28.087  1.00 73.22  ? 77  LEU C CB   1 
ATOM   9625  C CG   . LEU C 1 77  ? 8.709   7.335   28.595  1.00 72.94  ? 77  LEU C CG   1 
ATOM   9626  C CD1  . LEU C 1 77  ? 7.945   7.779   29.833  1.00 73.64  ? 77  LEU C CD1  1 
ATOM   9627  C CD2  . LEU C 1 77  ? 10.203  7.221   28.869  1.00 70.69  ? 77  LEU C CD2  1 
ATOM   9628  H H    . LEU C 1 77  ? 6.982   4.159   27.033  1.00 88.89  ? 77  LEU C H    1 
ATOM   9629  H HA   . LEU C 1 77  ? 6.188   6.097   28.605  1.00 88.01  ? 77  LEU C HA   1 
ATOM   9630  H HB2  . LEU C 1 77  ? 8.348   5.338   28.770  1.00 87.87  ? 77  LEU C HB2  1 
ATOM   9631  H HB3  . LEU C 1 77  ? 8.650   5.785   27.275  1.00 87.87  ? 77  LEU C HB3  1 
ATOM   9632  H HG   . LEU C 1 77  ? 8.587   8.019   27.918  1.00 87.53  ? 77  LEU C HG   1 
ATOM   9633  H HD11 . LEU C 1 77  ? 8.383   8.557   30.213  1.00 88.36  ? 77  LEU C HD11 1 
ATOM   9634  H HD12 . LEU C 1 77  ? 7.035   8.002   29.580  1.00 88.36  ? 77  LEU C HD12 1 
ATOM   9635  H HD13 . LEU C 1 77  ? 7.941   7.054   30.478  1.00 88.36  ? 77  LEU C HD13 1 
ATOM   9636  H HD21 . LEU C 1 77  ? 10.532  8.076   29.186  1.00 84.83  ? 77  LEU C HD21 1 
ATOM   9637  H HD22 . LEU C 1 77  ? 10.349  6.539   29.543  1.00 84.83  ? 77  LEU C HD22 1 
ATOM   9638  H HD23 . LEU C 1 77  ? 10.656  6.976   28.047  1.00 84.83  ? 77  LEU C HD23 1 
ATOM   9639  N N    . LEU C 1 78  ? 6.599   6.920   25.531  1.00 75.38  ? 78  LEU C N    1 
ATOM   9640  C CA   . LEU C 1 78  ? 6.196   7.917   24.545  1.00 73.78  ? 78  LEU C CA   1 
ATOM   9641  C C    . LEU C 1 78  ? 4.696   8.172   24.616  1.00 76.36  ? 78  LEU C C    1 
ATOM   9642  O O    . LEU C 1 78  ? 4.249   9.323   24.559  1.00 77.98  ? 78  LEU C O    1 
ATOM   9643  C CB   . LEU C 1 78  ? 6.598   7.462   23.143  1.00 76.57  ? 78  LEU C CB   1 
ATOM   9644  C CG   . LEU C 1 78  ? 8.093   7.468   22.824  1.00 74.54  ? 78  LEU C CG   1 
ATOM   9645  C CD1  . LEU C 1 78  ? 8.343   6.828   21.462  1.00 72.71  ? 78  LEU C CD1  1 
ATOM   9646  C CD2  . LEU C 1 78  ? 8.658   8.879   22.862  1.00 73.00  ? 78  LEU C CD2  1 
ATOM   9647  H H    . LEU C 1 78  ? 7.031   6.250   25.210  1.00 90.45  ? 78  LEU C H    1 
ATOM   9648  H HA   . LEU C 1 78  ? 6.657   8.751   24.729  1.00 88.54  ? 78  LEU C HA   1 
ATOM   9649  H HB2  . LEU C 1 78  ? 6.285   6.552   23.022  1.00 91.88  ? 78  LEU C HB2  1 
ATOM   9650  H HB3  . LEU C 1 78  ? 6.167   8.049   22.502  1.00 91.88  ? 78  LEU C HB3  1 
ATOM   9651  H HG   . LEU C 1 78  ? 8.559   6.950   23.498  1.00 89.45  ? 78  LEU C HG   1 
ATOM   9652  H HD11 . LEU C 1 78  ? 9.295   6.845   21.274  1.00 87.25  ? 78  LEU C HD11 1 
ATOM   9653  H HD12 . LEU C 1 78  ? 8.027   5.911   21.481  1.00 87.25  ? 78  LEU C HD12 1 
ATOM   9654  H HD13 . LEU C 1 78  ? 7.864   7.329   20.784  1.00 87.25  ? 78  LEU C HD13 1 
ATOM   9655  H HD21 . LEU C 1 78  ? 9.568   8.864   22.526  1.00 87.60  ? 78  LEU C HD21 1 
ATOM   9656  H HD22 . LEU C 1 78  ? 8.109   9.454   22.307  1.00 87.60  ? 78  LEU C HD22 1 
ATOM   9657  H HD23 . LEU C 1 78  ? 8.650   9.197   23.779  1.00 87.60  ? 78  LEU C HD23 1 
ATOM   9658  N N    . ALA C 1 79  ? 3.902   7.105   24.750  1.00 75.72  ? 79  ALA C N    1 
ATOM   9659  C CA   . ALA C 1 79  ? 2.462   7.270   24.908  1.00 77.67  ? 79  ALA C CA   1 
ATOM   9660  C C    . ALA C 1 79  ? 2.122   7.938   26.232  1.00 77.02  ? 79  ALA C C    1 
ATOM   9661  O O    . ALA C 1 79  ? 1.155   8.704   26.311  1.00 78.19  ? 79  ALA C O    1 
ATOM   9662  C CB   . ALA C 1 79  ? 1.762   5.915   24.811  1.00 81.33  ? 79  ALA C CB   1 
ATOM   9663  H H    . ALA C 1 79  ? 4.171   6.288   24.753  1.00 90.86  ? 79  ALA C H    1 
ATOM   9664  H HA   . ALA C 1 79  ? 2.133   7.831   24.189  1.00 93.20  ? 79  ALA C HA   1 
ATOM   9665  H HB1  . ALA C 1 79  ? 0.808   6.043   24.933  1.00 97.59  ? 79  ALA C HB1  1 
ATOM   9666  H HB2  . ALA C 1 79  ? 1.935   5.532   23.937  1.00 97.59  ? 79  ALA C HB2  1 
ATOM   9667  H HB3  . ALA C 1 79  ? 2.109   5.330   25.503  1.00 97.59  ? 79  ALA C HB3  1 
ATOM   9668  N N    . PHE C 1 80  ? 2.901   7.658   27.278  1.00 79.40  ? 80  PHE C N    1 
ATOM   9669  C CA   . PHE C 1 80  ? 2.660   8.286   28.573  1.00 79.01  ? 80  PHE C CA   1 
ATOM   9670  C C    . PHE C 1 80  ? 2.830   9.798   28.492  1.00 77.22  ? 80  PHE C C    1 
ATOM   9671  O O    . PHE C 1 80  ? 2.112   10.549  29.163  1.00 78.04  ? 80  PHE C O    1 
ATOM   9672  C CB   . PHE C 1 80  ? 3.611   7.689   29.613  1.00 76.07  ? 80  PHE C CB   1 
ATOM   9673  C CG   . PHE C 1 80  ? 3.306   8.093   31.023  1.00 78.53  ? 80  PHE C CG   1 
ATOM   9674  C CD1  . PHE C 1 80  ? 2.102   7.746   31.615  1.00 82.13  ? 80  PHE C CD1  1 
ATOM   9675  C CD2  . PHE C 1 80  ? 4.231   8.806   31.767  1.00 76.98  ? 80  PHE C CD2  1 
ATOM   9676  C CE1  . PHE C 1 80  ? 1.822   8.111   32.918  1.00 77.03  ? 80  PHE C CE1  1 
ATOM   9677  C CE2  . PHE C 1 80  ? 3.955   9.173   33.066  1.00 77.89  ? 80  PHE C CE2  1 
ATOM   9678  C CZ   . PHE C 1 80  ? 2.749   8.826   33.642  1.00 77.04  ? 80  PHE C CZ   1 
ATOM   9679  H H    . PHE C 1 80  ? 3.568   7.115   27.264  1.00 95.27  ? 80  PHE C H    1 
ATOM   9680  H HA   . PHE C 1 80  ? 1.750   8.105   28.853  1.00 94.81  ? 80  PHE C HA   1 
ATOM   9681  H HB2  . PHE C 1 80  ? 3.557   6.722   29.565  1.00 91.29  ? 80  PHE C HB2  1 
ATOM   9682  H HB3  . PHE C 1 80  ? 4.514   7.981   29.412  1.00 91.29  ? 80  PHE C HB3  1 
ATOM   9683  H HD1  . PHE C 1 80  ? 1.474   7.261   31.129  1.00 98.56  ? 80  PHE C HD1  1 
ATOM   9684  H HD2  . PHE C 1 80  ? 5.046   9.041   31.386  1.00 92.38  ? 80  PHE C HD2  1 
ATOM   9685  H HE1  . PHE C 1 80  ? 1.010   7.875   33.305  1.00 92.43  ? 80  PHE C HE1  1 
ATOM   9686  H HE2  . PHE C 1 80  ? 4.582   9.654   33.556  1.00 93.46  ? 80  PHE C HE2  1 
ATOM   9687  H HZ   . PHE C 1 80  ? 2.563   9.075   34.518  1.00 92.45  ? 80  PHE C HZ   1 
ATOM   9688  N N    . ARG C 1 81  ? 3.767   10.264  27.673  1.00 77.38  ? 81  ARG C N    1 
ATOM   9689  C CA   . ARG C 1 81  ? 4.076   11.684  27.568  1.00 77.56  ? 81  ARG C CA   1 
ATOM   9690  C C    . ARG C 1 81  ? 3.341   12.374  26.428  1.00 82.08  ? 81  ARG C C    1 
ATOM   9691  O O    . ARG C 1 81  ? 3.455   13.597  26.290  1.00 83.54  ? 81  ARG C O    1 
ATOM   9692  C CB   . ARG C 1 81  ? 5.584   11.879  27.391  1.00 76.00  ? 81  ARG C CB   1 
ATOM   9693  C CG   . ARG C 1 81  ? 6.413   11.159  28.432  1.00 76.52  ? 81  ARG C CG   1 
ATOM   9694  C CD   . ARG C 1 81  ? 7.874   11.578  28.392  1.00 73.61  ? 81  ARG C CD   1 
ATOM   9695  N NE   . ARG C 1 81  ? 8.404   11.738  29.741  1.00 80.58  ? 81  ARG C NE   1 
ATOM   9696  C CZ   . ARG C 1 81  ? 9.677   11.574  30.077  1.00 80.79  ? 81  ARG C CZ   1 
ATOM   9697  N NH1  . ARG C 1 81  ? 10.593  11.262  29.176  1.00 79.43  ? 81  ARG C NH1  1 
ATOM   9698  N NH2  . ARG C 1 81  ? 10.037  11.726  31.351  1.00 82.13  ? 81  ARG C NH2  1 
ATOM   9699  H H    . ARG C 1 81  ? 4.246   9.768   27.158  1.00 92.85  ? 81  ARG C H    1 
ATOM   9700  H HA   . ARG C 1 81  ? 3.808   12.116  28.394  1.00 93.07  ? 81  ARG C HA   1 
ATOM   9701  H HB2  . ARG C 1 81  ? 5.843   11.541  26.520  1.00 91.20  ? 81  ARG C HB2  1 
ATOM   9702  H HB3  . ARG C 1 81  ? 5.787   12.826  27.453  1.00 91.20  ? 81  ARG C HB3  1 
ATOM   9703  H HG2  . ARG C 1 81  ? 6.064   11.362  29.314  1.00 91.82  ? 81  ARG C HG2  1 
ATOM   9704  H HG3  . ARG C 1 81  ? 6.368   10.203  28.270  1.00 91.82  ? 81  ARG C HG3  1 
ATOM   9705  H HD2  . ARG C 1 81  ? 8.393   10.898  27.936  1.00 88.33  ? 81  ARG C HD2  1 
ATOM   9706  H HD3  . ARG C 1 81  ? 7.954   12.425  27.927  1.00 88.33  ? 81  ARG C HD3  1 
ATOM   9707  H HE   . ARG C 1 81  ? 7.852   11.955  30.364  1.00 96.70  ? 81  ARG C HE   1 
ATOM   9708  H HH11 . ARG C 1 81  ? 10.368  11.161  28.352  1.00 95.31  ? 81  ARG C HH11 1 
ATOM   9709  H HH12 . ARG C 1 81  ? 11.413  11.160  29.414  1.00 95.31  ? 81  ARG C HH12 1 
ATOM   9710  H HH21 . ARG C 1 81  ? 9.448   11.928  31.944  1.00 98.56  ? 81  ARG C HH21 1 
ATOM   9711  H HH22 . ARG C 1 81  ? 10.860  11.622  31.581  1.00 98.56  ? 81  ARG C HH22 1 
ATOM   9712  N N    . ASP C 1 82  ? 2.599   11.630  25.612  1.00 81.12  ? 82  ASP C N    1 
ATOM   9713  C CA   . ASP C 1 82  ? 1.834   12.209  24.512  1.00 84.74  ? 82  ASP C CA   1 
ATOM   9714  C C    . ASP C 1 82  ? 0.491   12.693  25.044  1.00 87.70  ? 82  ASP C C    1 
ATOM   9715  O O    . ASP C 1 82  ? -0.393  11.885  25.347  1.00 88.55  ? 82  ASP C O    1 
ATOM   9716  C CB   . ASP C 1 82  ? 1.642   11.183  23.402  1.00 85.99  ? 82  ASP C CB   1 
ATOM   9717  C CG   . ASP C 1 82  ? 1.002   11.776  22.163  1.00 88.12  ? 82  ASP C CG   1 
ATOM   9718  O OD1  . ASP C 1 82  ? -0.077  12.398  22.277  1.00 90.77  ? 82  ASP C OD1  1 
ATOM   9719  O OD2  . ASP C 1 82  ? 1.577   11.613  21.069  1.00 90.54  ? 82  ASP C OD2  1 
ATOM   9720  H H    . ASP C 1 82  ? 2.521   10.776  25.675  1.00 97.34  ? 82  ASP C H    1 
ATOM   9721  H HA   . ASP C 1 82  ? 2.316   12.969  24.149  1.00 101.68 ? 82  ASP C HA   1 
ATOM   9722  H HB2  . ASP C 1 82  ? 2.507   10.823  23.150  1.00 103.19 ? 82  ASP C HB2  1 
ATOM   9723  H HB3  . ASP C 1 82  ? 1.069   10.471  23.725  1.00 103.19 ? 82  ASP C HB3  1 
ATOM   9724  N N    . LYS C 1 83  ? 0.328   14.013  25.145  1.00 90.48  ? 83  LYS C N    1 
ATOM   9725  C CA   . LYS C 1 83  ? -0.927  14.569  25.636  1.00 93.16  ? 83  LYS C CA   1 
ATOM   9726  C C    . LYS C 1 83  ? -2.112  14.180  24.762  1.00 95.60  ? 83  LYS C C    1 
ATOM   9727  O O    . LYS C 1 83  ? -3.258  14.271  25.215  1.00 96.52  ? 83  LYS C O    1 
ATOM   9728  C CB   . LYS C 1 83  ? -0.825  16.097  25.722  1.00 93.75  ? 83  LYS C CB   1 
ATOM   9729  C CG   . LYS C 1 83  ? -0.559  16.780  24.386  1.00 98.24  ? 83  LYS C CG   1 
ATOM   9730  C CD   . LYS C 1 83  ? -1.331  18.088  24.255  1.00 95.83  ? 83  LYS C CD   1 
ATOM   9731  C CE   . LYS C 1 83  ? -0.476  19.280  24.656  1.00 92.59  ? 83  LYS C CE   1 
ATOM   9732  N NZ   . LYS C 1 83  ? -1.196  20.575  24.463  1.00 95.09  ? 83  LYS C NZ   1 
ATOM   9733  H H    . LYS C 1 83  ? 0.923   14.599  24.939  1.00 108.58 ? 83  LYS C H    1 
ATOM   9734  H HA   . LYS C 1 83  ? -1.089  14.226  26.529  1.00 111.80 ? 83  LYS C HA   1 
ATOM   9735  H HB2  . LYS C 1 83  ? -1.662  16.444  26.069  1.00 112.50 ? 83  LYS C HB2  1 
ATOM   9736  H HB3  . LYS C 1 83  ? -0.097  16.326  26.321  1.00 112.50 ? 83  LYS C HB3  1 
ATOM   9737  H HG2  . LYS C 1 83  ? 0.387   16.977  24.310  1.00 117.88 ? 83  LYS C HG2  1 
ATOM   9738  H HG3  . LYS C 1 83  ? -0.834  16.191  23.665  1.00 117.88 ? 83  LYS C HG3  1 
ATOM   9739  H HD2  . LYS C 1 83  ? -1.608  18.208  23.333  1.00 114.99 ? 83  LYS C HD2  1 
ATOM   9740  H HD3  . LYS C 1 83  ? -2.109  18.062  24.835  1.00 114.99 ? 83  LYS C HD3  1 
ATOM   9741  H HE2  . LYS C 1 83  ? -0.239  19.202  25.593  1.00 111.11 ? 83  LYS C HE2  1 
ATOM   9742  H HE3  . LYS C 1 83  ? 0.326   19.295  24.111  1.00 111.11 ? 83  LYS C HE3  1 
ATOM   9743  H HZ1  . LYS C 1 83  ? -1.936  20.589  24.957  1.00 114.11 ? 83  LYS C HZ1  1 
ATOM   9744  H HZ2  . LYS C 1 83  ? -0.673  21.253  24.706  1.00 114.11 ? 83  LYS C HZ2  1 
ATOM   9745  H HZ3  . LYS C 1 83  ? -1.418  20.675  23.607  1.00 114.11 ? 83  LYS C HZ3  1 
ATOM   9746  N N    . ASP C 1 84  ? -1.864  13.749  23.526  1.00 100.52 ? 84  ASP C N    1 
ATOM   9747  C CA   . ASP C 1 84  ? -2.922  13.413  22.584  1.00 102.31 ? 84  ASP C CA   1 
ATOM   9748  C C    . ASP C 1 84  ? -3.171  11.912  22.479  1.00 96.65  ? 84  ASP C C    1 
ATOM   9749  O O    . ASP C 1 84  ? -3.968  11.486  21.637  1.00 94.56  ? 84  ASP C O    1 
ATOM   9750  C CB   . ASP C 1 84  ? -2.593  13.984  21.200  1.00 100.02 ? 84  ASP C CB   1 
ATOM   9751  C CG   . ASP C 1 84  ? -2.746  15.494  21.140  1.00 104.51 ? 84  ASP C CG   1 
ATOM   9752  O OD1  . ASP C 1 84  ? -3.811  16.001  21.555  1.00 106.30 ? 84  ASP C OD1  1 
ATOM   9753  O OD2  . ASP C 1 84  ? -1.802  16.175  20.685  1.00 106.62 ? 84  ASP C OD2  1 
ATOM   9754  H H    . ASP C 1 84  ? -1.073  13.642  23.206  1.00 120.62 ? 84  ASP C H    1 
ATOM   9755  H HA   . ASP C 1 84  ? -3.745  13.823  22.894  1.00 122.78 ? 84  ASP C HA   1 
ATOM   9756  H HB2  . ASP C 1 84  ? -1.675  13.766  20.978  1.00 120.02 ? 84  ASP C HB2  1 
ATOM   9757  H HB3  . ASP C 1 84  ? -3.195  13.594  20.546  1.00 120.02 ? 84  ASP C HB3  1 
ATOM   9758  N N    . PHE C 1 85  ? -2.513  11.104  23.307  1.00 95.50  ? 85  PHE C N    1 
ATOM   9759  C CA   . PHE C 1 85  ? -2.790  9.672   23.334  1.00 95.54  ? 85  PHE C CA   1 
ATOM   9760  C C    . PHE C 1 85  ? -4.128  9.431   24.023  1.00 99.17  ? 85  PHE C C    1 
ATOM   9761  O O    . PHE C 1 85  ? -4.335  9.867   25.160  1.00 99.94  ? 85  PHE C O    1 
ATOM   9762  C CB   . PHE C 1 85  ? -1.672  8.924   24.053  1.00 88.81  ? 85  PHE C CB   1 
ATOM   9763  C CG   . PHE C 1 85  ? -1.873  7.436   24.104  1.00 89.87  ? 85  PHE C CG   1 
ATOM   9764  C CD1  . PHE C 1 85  ? -2.634  6.858   25.107  1.00 92.70  ? 85  PHE C CD1  1 
ATOM   9765  C CD2  . PHE C 1 85  ? -1.298  6.614   23.149  1.00 87.73  ? 85  PHE C CD2  1 
ATOM   9766  C CE1  . PHE C 1 85  ? -2.821  5.487   25.154  1.00 93.59  ? 85  PHE C CE1  1 
ATOM   9767  C CE2  . PHE C 1 85  ? -1.480  5.242   23.191  1.00 86.23  ? 85  PHE C CE2  1 
ATOM   9768  C CZ   . PHE C 1 85  ? -2.243  4.679   24.195  1.00 90.63  ? 85  PHE C CZ   1 
ATOM   9769  H H    . PHE C 1 85  ? -1.907  11.359  23.861  1.00 114.60 ? 85  PHE C H    1 
ATOM   9770  H HA   . PHE C 1 85  ? -2.837  9.335   22.426  1.00 114.64 ? 85  PHE C HA   1 
ATOM   9771  H HB2  . PHE C 1 85  ? -0.836  9.094   23.591  1.00 106.57 ? 85  PHE C HB2  1 
ATOM   9772  H HB3  . PHE C 1 85  ? -1.617  9.247   24.966  1.00 106.57 ? 85  PHE C HB3  1 
ATOM   9773  H HD1  . PHE C 1 85  ? -3.025  7.397   25.756  1.00 111.24 ? 85  PHE C HD1  1 
ATOM   9774  H HD2  . PHE C 1 85  ? -0.784  6.988   22.471  1.00 105.27 ? 85  PHE C HD2  1 
ATOM   9775  H HE1  . PHE C 1 85  ? -3.336  5.111   25.831  1.00 112.31 ? 85  PHE C HE1  1 
ATOM   9776  H HE2  . PHE C 1 85  ? -1.089  4.700   22.544  1.00 103.48 ? 85  PHE C HE2  1 
ATOM   9777  H HZ   . PHE C 1 85  ? -2.367  3.758   24.225  1.00 108.76 ? 85  PHE C HZ   1 
ATOM   9778  N N    . SER C 1 86  ? -5.037  8.740   23.337  1.00 101.32 ? 86  SER C N    1 
ATOM   9779  C CA   . SER C 1 86  ? -6.366  8.478   23.879  1.00 107.45 ? 86  SER C CA   1 
ATOM   9780  C C    . SER C 1 86  ? -6.465  7.038   24.370  1.00 110.22 ? 86  SER C C    1 
ATOM   9781  O O    . SER C 1 86  ? -6.336  6.777   25.571  1.00 111.56 ? 86  SER C O    1 
ATOM   9782  C CB   . SER C 1 86  ? -7.435  8.766   22.823  1.00 107.61 ? 86  SER C CB   1 
ATOM   9783  O OG   . SER C 1 86  ? -8.741  8.640   23.360  1.00 113.60 ? 86  SER C OG   1 
ATOM   9784  H H    . SER C 1 86  ? -4.907  8.413   22.553  1.00 121.59 ? 86  SER C H    1 
ATOM   9785  H HA   . SER C 1 86  ? -6.529  9.064   24.635  1.00 128.94 ? 86  SER C HA   1 
ATOM   9786  H HB2  . SER C 1 86  ? -7.317  9.672   22.497  1.00 129.13 ? 86  SER C HB2  1 
ATOM   9787  H HB3  . SER C 1 86  ? -7.334  8.135   22.094  1.00 129.13 ? 86  SER C HB3  1 
ATOM   9788  H HG   . SER C 1 86  ? -8.842  9.176   23.998  1.00 136.31 ? 86  SER C HG   1 
ATOM   9789  N N    . LYS C 1 87  ? -6.695  6.099   23.451  1.00 101.74 ? 87  LYS C N    1 
ATOM   9790  C CA   . LYS C 1 87  ? -6.768  4.683   23.785  1.00 99.03  ? 87  LYS C CA   1 
ATOM   9791  C C    . LYS C 1 87  ? -5.856  3.812   22.935  1.00 94.31  ? 87  LYS C C    1 
ATOM   9792  O O    . LYS C 1 87  ? -5.536  2.695   23.357  1.00 94.66  ? 87  LYS C O    1 
ATOM   9793  C CB   . LYS C 1 87  ? -8.210  4.165   23.648  1.00 100.10 ? 87  LYS C CB   1 
ATOM   9794  C CG   . LYS C 1 87  ? -9.276  5.131   24.156  1.00 102.63 ? 87  LYS C CG   1 
ATOM   9795  C CD   . LYS C 1 87  ? -10.654 4.893   23.517  1.00 103.29 ? 87  LYS C CD   1 
ATOM   9796  C CE   . LYS C 1 87  ? -10.604 4.777   21.993  1.00 104.54 ? 87  LYS C CE   1 
ATOM   9797  N NZ   . LYS C 1 87  ? -9.624  5.712   21.367  1.00 104.91 ? 87  LYS C NZ   1 
ATOM   9798  H H    . LYS C 1 87  ? -6.814  6.264   22.615  1.00 122.09 ? 87  LYS C H    1 
ATOM   9799  H HA   . LYS C 1 87  ? -6.510  4.570   24.713  1.00 118.83 ? 87  LYS C HA   1 
ATOM   9800  H HB2  . LYS C 1 87  ? -8.391  3.996   22.710  1.00 120.12 ? 87  LYS C HB2  1 
ATOM   9801  H HB3  . LYS C 1 87  ? -8.294  3.343   24.155  1.00 120.12 ? 87  LYS C HB3  1 
ATOM   9802  H HG2  . LYS C 1 87  ? -9.369  5.023   25.115  1.00 123.16 ? 87  LYS C HG2  1 
ATOM   9803  H HG3  . LYS C 1 87  ? -9.004  6.039   23.950  1.00 123.16 ? 87  LYS C HG3  1 
ATOM   9804  H HD2  . LYS C 1 87  ? -11.024 4.067   23.865  1.00 123.94 ? 87  LYS C HD2  1 
ATOM   9805  H HD3  . LYS C 1 87  ? -11.236 5.637   23.739  1.00 123.94 ? 87  LYS C HD3  1 
ATOM   9806  H HE2  . LYS C 1 87  ? -10.348 3.873   21.754  1.00 125.45 ? 87  LYS C HE2  1 
ATOM   9807  H HE3  . LYS C 1 87  ? -11.481 4.980   21.632  1.00 125.45 ? 87  LYS C HE3  1 
ATOM   9808  H HZ1  . LYS C 1 87  ? -9.853  6.554   21.541  1.00 125.89 ? 87  LYS C HZ1  1 
ATOM   9809  H HZ2  . LYS C 1 87  ? -9.608  5.592   20.486  1.00 125.89 ? 87  LYS C HZ2  1 
ATOM   9810  H HZ3  . LYS C 1 87  ? -8.809  5.562   21.693  1.00 125.89 ? 87  LYS C HZ3  1 
ATOM   9811  N N    . GLN C 1 88  ? -5.431  4.276   21.764  1.00 91.71  ? 88  GLN C N    1 
ATOM   9812  C CA   . GLN C 1 88  ? -4.515  3.526   20.918  1.00 88.19  ? 88  GLN C CA   1 
ATOM   9813  C C    . GLN C 1 88  ? -3.782  4.507   20.013  1.00 85.65  ? 88  GLN C C    1 
ATOM   9814  O O    . GLN C 1 88  ? -4.369  5.486   19.546  1.00 84.62  ? 88  GLN C O    1 
ATOM   9815  C CB   . GLN C 1 88  ? -5.248  2.479   20.072  1.00 85.42  ? 88  GLN C CB   1 
ATOM   9816  C CG   . GLN C 1 88  ? -4.329  1.642   19.197  1.00 85.09  ? 88  GLN C CG   1 
ATOM   9817  C CD   . GLN C 1 88  ? -4.035  2.293   17.855  1.00 88.10  ? 88  GLN C CD   1 
ATOM   9818  O OE1  . GLN C 1 88  ? -4.765  3.179   17.400  1.00 90.15  ? 88  GLN C OE1  1 
ATOM   9819  N NE2  . GLN C 1 88  ? -2.957  1.855   17.215  1.00 87.71  ? 88  GLN C NE2  1 
ATOM   9820  H H    . GLN C 1 88  ? -5.663  5.036   21.434  1.00 110.05 ? 88  GLN C H    1 
ATOM   9821  H HA   . GLN C 1 88  ? -3.868  3.065   21.474  1.00 105.83 ? 88  GLN C HA   1 
ATOM   9822  H HB2  . GLN C 1 88  ? -5.722  1.876   20.666  1.00 102.51 ? 88  GLN C HB2  1 
ATOM   9823  H HB3  . GLN C 1 88  ? -5.878  2.934   19.491  1.00 102.51 ? 88  GLN C HB3  1 
ATOM   9824  H HG2  . GLN C 1 88  ? -3.486  1.513   19.658  1.00 102.11 ? 88  GLN C HG2  1 
ATOM   9825  H HG3  . GLN C 1 88  ? -4.750  0.784   19.028  1.00 102.11 ? 88  GLN C HG3  1 
ATOM   9826  H HE21 . GLN C 1 88  ? -2.472  1.237   17.563  1.00 105.25 ? 88  GLN C HE21 1 
ATOM   9827  H HE22 . GLN C 1 88  ? -2.745  2.189   16.451  1.00 105.25 ? 88  GLN C HE22 1 
ATOM   9828  N N    . LYS C 1 89  ? -2.503  4.235   19.771  1.00 84.34  ? 89  LYS C N    1 
ATOM   9829  C CA   . LYS C 1 89  ? -1.679  5.074   18.913  1.00 83.35  ? 89  LYS C CA   1 
ATOM   9830  C C    . LYS C 1 89  ? -0.408  4.309   18.584  1.00 82.31  ? 89  LYS C C    1 
ATOM   9831  O O    . LYS C 1 89  ? 0.173   3.660   19.457  1.00 81.48  ? 89  LYS C O    1 
ATOM   9832  C CB   . LYS C 1 89  ? -1.341  6.407   19.590  1.00 82.38  ? 89  LYS C CB   1 
ATOM   9833  C CG   . LYS C 1 89  ? -0.914  7.508   18.619  1.00 82.75  ? 89  LYS C CG   1 
ATOM   9834  C CD   . LYS C 1 89  ? -0.517  8.786   19.360  1.00 87.30  ? 89  LYS C CD   1 
ATOM   9835  C CE   . LYS C 1 89  ? -0.738  10.034  18.504  1.00 85.33  ? 89  LYS C CE   1 
ATOM   9836  N NZ   . LYS C 1 89  ? 0.524   10.802  18.280  1.00 82.12  ? 89  LYS C NZ   1 
ATOM   9837  H H    . LYS C 1 89  ? -2.084  3.558   20.098  1.00 101.21 ? 89  LYS C H    1 
ATOM   9838  H HA   . LYS C 1 89  ? -2.152  5.269   18.089  1.00 100.02 ? 89  LYS C HA   1 
ATOM   9839  H HB2  . LYS C 1 89  ? -2.126  6.722   20.065  1.00 98.86  ? 89  LYS C HB2  1 
ATOM   9840  H HB3  . LYS C 1 89  ? -0.611  6.264   20.212  1.00 98.86  ? 89  LYS C HB3  1 
ATOM   9841  H HG2  . LYS C 1 89  ? -0.150  7.204   18.104  1.00 99.31  ? 89  LYS C HG2  1 
ATOM   9842  H HG3  . LYS C 1 89  ? -1.652  7.717   18.025  1.00 99.31  ? 89  LYS C HG3  1 
ATOM   9843  H HD2  . LYS C 1 89  ? -1.055  8.870   20.163  1.00 104.76 ? 89  LYS C HD2  1 
ATOM   9844  H HD3  . LYS C 1 89  ? 0.423   8.742   19.593  1.00 104.76 ? 89  LYS C HD3  1 
ATOM   9845  H HE2  . LYS C 1 89  ? -1.087  9.768   17.638  1.00 102.40 ? 89  LYS C HE2  1 
ATOM   9846  H HE3  . LYS C 1 89  ? -1.371  10.618  18.951  1.00 102.40 ? 89  LYS C HE3  1 
ATOM   9847  H HZ1  . LYS C 1 89  ? 1.122   10.290  17.864  1.00 98.54  ? 89  LYS C HZ1  1 
ATOM   9848  H HZ2  . LYS C 1 89  ? 0.359   11.519  17.779  1.00 98.54  ? 89  LYS C HZ2  1 
ATOM   9849  H HZ3  . LYS C 1 89  ? 0.862   11.065  19.059  1.00 98.54  ? 89  LYS C HZ3  1 
ATOM   9850  N N    . ASN C 1 90  ? 0.009   4.377   17.326  1.00 80.54  ? 90  ASN C N    1 
ATOM   9851  C CA   . ASN C 1 90  ? 1.223   3.708   16.885  1.00 80.41  ? 90  ASN C CA   1 
ATOM   9852  C C    . ASN C 1 90  ? 2.412   4.649   17.003  1.00 78.80  ? 90  ASN C C    1 
ATOM   9853  O O    . ASN C 1 90  ? 2.319   5.836   16.670  1.00 79.26  ? 90  ASN C O    1 
ATOM   9854  C CB   . ASN C 1 90  ? 1.085   3.228   15.444  1.00 84.08  ? 90  ASN C CB   1 
ATOM   9855  C CG   . ASN C 1 90  ? 0.428   1.873   15.349  1.00 85.99  ? 90  ASN C CG   1 
ATOM   9856  O OD1  . ASN C 1 90  ? -0.791  1.756   15.467  1.00 88.81  ? 90  ASN C OD1  1 
ATOM   9857  N ND2  . ASN C 1 90  ? 1.232   0.837   15.135  1.00 87.22  ? 90  ASN C ND2  1 
ATOM   9858  H H    . ASN C 1 90  ? -0.399  4.808   16.704  1.00 96.64  ? 90  ASN C H    1 
ATOM   9859  H HA   . ASN C 1 90  ? 1.384   2.934   17.448  1.00 96.49  ? 90  ASN C HA   1 
ATOM   9860  H HB2  . ASN C 1 90  ? 0.543   3.861   14.949  1.00 100.90 ? 90  ASN C HB2  1 
ATOM   9861  H HB3  . ASN C 1 90  ? 1.967   3.164   15.045  1.00 100.90 ? 90  ASN C HB3  1 
ATOM   9862  H HD21 . ASN C 1 90  ? 2.080   0.959   15.059  1.00 104.66 ? 90  ASN C HD21 1 
ATOM   9863  H HD22 . ASN C 1 90  ? 0.905   0.044   15.073  1.00 104.66 ? 90  ASN C HD22 1 
ATOM   9864  N N    . TYR C 1 91  ? 3.533   4.108   17.471  1.00 78.23  ? 91  TYR C N    1 
ATOM   9865  C CA   . TYR C 1 91  ? 4.739   4.889   17.699  1.00 81.38  ? 91  TYR C CA   1 
ATOM   9866  C C    . TYR C 1 91  ? 5.904   4.241   16.972  1.00 79.77  ? 91  TYR C C    1 
ATOM   9867  O O    . TYR C 1 91  ? 6.095   3.022   17.052  1.00 81.22  ? 91  TYR C O    1 
ATOM   9868  C CB   . TYR C 1 91  ? 5.040   5.008   19.191  1.00 77.19  ? 91  TYR C CB   1 
ATOM   9869  C CG   . TYR C 1 91  ? 4.059   5.891   19.920  1.00 77.41  ? 91  TYR C CG   1 
ATOM   9870  C CD1  . TYR C 1 91  ? 2.896   5.364   20.467  1.00 78.11  ? 91  TYR C CD1  1 
ATOM   9871  C CD2  . TYR C 1 91  ? 4.287   7.254   20.053  1.00 76.76  ? 91  TYR C CD2  1 
ATOM   9872  C CE1  . TYR C 1 91  ? 1.992   6.169   21.129  1.00 80.59  ? 91  TYR C CE1  1 
ATOM   9873  C CE2  . TYR C 1 91  ? 3.389   8.067   20.715  1.00 77.28  ? 91  TYR C CE2  1 
ATOM   9874  C CZ   . TYR C 1 91  ? 2.243   7.521   21.249  1.00 80.75  ? 91  TYR C CZ   1 
ATOM   9875  O OH   . TYR C 1 91  ? 1.347   8.327   21.907  1.00 83.23  ? 91  TYR C OH   1 
ATOM   9876  H H    . TYR C 1 91  ? 3.619   3.275   17.667  1.00 93.88  ? 91  TYR C H    1 
ATOM   9877  H HA   . TYR C 1 91  ? 4.621   5.781   17.338  1.00 97.65  ? 91  TYR C HA   1 
ATOM   9878  H HB2  . TYR C 1 91  ? 5.004   4.125   19.591  1.00 92.63  ? 91  TYR C HB2  1 
ATOM   9879  H HB3  . TYR C 1 91  ? 5.926   5.387   19.304  1.00 92.63  ? 91  TYR C HB3  1 
ATOM   9880  H HD1  . TYR C 1 91  ? 2.724   4.454   20.386  1.00 93.74  ? 91  TYR C HD1  1 
ATOM   9881  H HD2  . TYR C 1 91  ? 5.058   7.626   19.690  1.00 92.11  ? 91  TYR C HD2  1 
ATOM   9882  H HE1  . TYR C 1 91  ? 1.217   5.803   21.491  1.00 96.71  ? 91  TYR C HE1  1 
ATOM   9883  H HE2  . TYR C 1 91  ? 3.557   8.978   20.800  1.00 92.74  ? 91  TYR C HE2  1 
ATOM   9884  H HH   . TYR C 1 91  ? 1.587   9.130   21.851  1.00 99.87  ? 91  TYR C HH   1 
ATOM   9885  N N    . ASN C 1 92  ? 6.680   5.062   16.274  1.00 77.98  ? 92  ASN C N    1 
ATOM   9886  C CA   . ASN C 1 92  ? 7.821   4.601   15.496  1.00 82.45  ? 92  ASN C CA   1 
ATOM   9887  C C    . ASN C 1 92  ? 9.100   4.913   16.260  1.00 81.42  ? 92  ASN C C    1 
ATOM   9888  O O    . ASN C 1 92  ? 9.404   6.084   16.515  1.00 84.41  ? 92  ASN C O    1 
ATOM   9889  C CB   . ASN C 1 92  ? 7.829   5.264   14.125  1.00 83.73  ? 92  ASN C CB   1 
ATOM   9890  C CG   . ASN C 1 92  ? 7.161   4.413   13.073  1.00 89.01  ? 92  ASN C CG   1 
ATOM   9891  O OD1  . ASN C 1 92  ? 5.933   4.375   12.965  1.00 89.40  ? 92  ASN C OD1  1 
ATOM   9892  N ND2  . ASN C 1 92  ? 7.972   3.702   12.293  1.00 94.40  ? 92  ASN C ND2  1 
ATOM   9893  H H    . ASN C 1 92  ? 6.562   5.913   16.235  1.00 93.57  ? 92  ASN C H    1 
ATOM   9894  H HA   . ASN C 1 92  ? 7.771   3.640   15.372  1.00 98.94  ? 92  ASN C HA   1 
ATOM   9895  H HB2  . ASN C 1 92  ? 7.354   6.108   14.177  1.00 100.48 ? 92  ASN C HB2  1 
ATOM   9896  H HB3  . ASN C 1 92  ? 8.747   5.417   13.852  1.00 100.48 ? 92  ASN C HB3  1 
ATOM   9897  H HD21 . ASN C 1 92  ? 8.824   3.745   12.405  1.00 113.27 ? 92  ASN C HD21 1 
ATOM   9898  H HD22 . ASN C 1 92  ? 7.645   3.200   11.676  1.00 113.27 ? 92  ASN C HD22 1 
ATOM   9899  N N    . ILE C 1 93  ? 9.838   3.871   16.632  1.00 81.64  ? 93  ILE C N    1 
ATOM   9900  C CA   . ILE C 1 93  ? 11.038  4.009   17.426  1.00 81.06  ? 93  ILE C CA   1 
ATOM   9901  C C    . ILE C 1 93  ? 12.141  3.149   16.813  1.00 79.89  ? 93  ILE C C    1 
ATOM   9902  O O    . ILE C 1 93  ? 11.923  2.408   15.858  1.00 81.31  ? 93  ILE C O    1 
ATOM   9903  C CB   . ILE C 1 93  ? 10.813  3.638   18.907  1.00 81.06  ? 93  ILE C CB   1 
ATOM   9904  C CG1  . ILE C 1 93  ? 10.296  2.204   19.043  1.00 80.82  ? 93  ILE C CG1  1 
ATOM   9905  C CG2  . ILE C 1 93  ? 9.839   4.607   19.569  1.00 78.26  ? 93  ILE C CG2  1 
ATOM   9906  C CD1  . ILE C 1 93  ? 10.807  1.486   20.285  1.00 78.26  ? 93  ILE C CD1  1 
ATOM   9907  H H    . ILE C 1 93  ? 9.652   3.056   16.428  1.00 97.96  ? 93  ILE C H    1 
ATOM   9908  H HA   . ILE C 1 93  ? 11.323  4.935   17.387  1.00 97.27  ? 93  ILE C HA   1 
ATOM   9909  H HB   . ILE C 1 93  ? 11.671  3.701   19.355  1.00 97.27  ? 93  ILE C HB   1 
ATOM   9910  H HG12 . ILE C 1 93  ? 9.327   2.224   19.089  1.00 96.99  ? 93  ILE C HG12 1 
ATOM   9911  H HG13 . ILE C 1 93  ? 10.580  1.695   18.267  1.00 96.99  ? 93  ILE C HG13 1 
ATOM   9912  H HG21 . ILE C 1 93  ? 9.725   4.355   20.498  1.00 93.91  ? 93  ILE C HG21 1 
ATOM   9913  H HG22 . ILE C 1 93  ? 10.201  5.506   19.512  1.00 93.91  ? 93  ILE C HG22 1 
ATOM   9914  H HG23 . ILE C 1 93  ? 8.988   4.564   19.107  1.00 93.91  ? 93  ILE C HG23 1 
ATOM   9915  H HD11 . ILE C 1 93  ? 10.440  0.589   20.304  1.00 93.91  ? 93  ILE C HD11 1 
ATOM   9916  H HD12 . ILE C 1 93  ? 11.776  1.446   20.250  1.00 93.91  ? 93  ILE C HD12 1 
ATOM   9917  H HD13 . ILE C 1 93  ? 10.524  1.977   21.072  1.00 93.91  ? 93  ILE C HD13 1 
ATOM   9918  N N    . THR C 1 94  ? 13.336  3.256   17.390  1.00 76.72  ? 94  THR C N    1 
ATOM   9919  C CA   . THR C 1 94  ? 14.476  2.448   16.997  1.00 77.93  ? 94  THR C CA   1 
ATOM   9920  C C    . THR C 1 94  ? 15.163  1.917   18.247  1.00 80.29  ? 94  THR C C    1 
ATOM   9921  O O    . THR C 1 94  ? 15.043  2.480   19.340  1.00 77.63  ? 94  THR C O    1 
ATOM   9922  C CB   . THR C 1 94  ? 15.472  3.248   16.146  1.00 81.00  ? 94  THR C CB   1 
ATOM   9923  O OG1  . THR C 1 94  ? 16.322  4.028   16.997  1.00 76.05  ? 94  THR C OG1  1 
ATOM   9924  C CG2  . THR C 1 94  ? 14.736  4.170   15.189  1.00 84.05  ? 94  THR C CG2  1 
ATOM   9925  H H    . THR C 1 94  ? 13.511  3.805   18.028  1.00 92.06  ? 94  THR C H    1 
ATOM   9926  H HA   . THR C 1 94  ? 14.173  1.693   16.469  1.00 93.52  ? 94  THR C HA   1 
ATOM   9927  H HB   . THR C 1 94  ? 16.014  2.635   15.626  1.00 97.20  ? 94  THR C HB   1 
ATOM   9928  H HG1  . THR C 1 94  ? 15.950  4.758   17.184  1.00 91.26  ? 94  THR C HG1  1 
ATOM   9929  H HG21 . THR C 1 94  ? 15.357  4.539   14.541  1.00 100.86 ? 94  THR C HG21 1 
ATOM   9930  H HG22 . THR C 1 94  ? 14.046  3.677   14.718  1.00 100.86 ? 94  THR C HG22 1 
ATOM   9931  H HG23 . THR C 1 94  ? 14.324  4.898   15.680  1.00 100.86 ? 94  THR C HG23 1 
ATOM   9932  N N    . CYS C 1 95  ? 15.889  0.816   18.073  1.00 79.78  ? 95  CYS C N    1 
ATOM   9933  C CA   . CYS C 1 95  ? 16.569  0.163   19.180  1.00 79.75  ? 95  CYS C CA   1 
ATOM   9934  C C    . CYS C 1 95  ? 17.936  -0.330  18.734  1.00 81.45  ? 95  CYS C C    1 
ATOM   9935  O O    . CYS C 1 95  ? 18.085  -0.868  17.633  1.00 77.82  ? 95  CYS C O    1 
ATOM   9936  C CB   . CYS C 1 95  ? 15.752  -1.017  19.722  1.00 80.10  ? 95  CYS C CB   1 
ATOM   9937  S SG   . CYS C 1 95  ? 16.273  -1.560  21.360  1.00 82.67  ? 95  CYS C SG   1 
ATOM   9938  H H    . CYS C 1 95  ? 16.002  0.427   17.314  1.00 95.74  ? 95  CYS C H    1 
ATOM   9939  H HA   . CYS C 1 95  ? 16.700  0.807   19.893  1.00 95.70  ? 95  CYS C HA   1 
ATOM   9940  H HB2  . CYS C 1 95  ? 14.820  -0.752  19.779  1.00 96.12  ? 95  CYS C HB2  1 
ATOM   9941  H HB3  . CYS C 1 95  ? 15.847  -1.768  19.115  1.00 96.12  ? 95  CYS C HB3  1 
ATOM   9942  H HG   . CYS C 1 95  ? 15.562  -2.458  21.718  1.00 99.19  ? 95  CYS C HG   1 
ATOM   9943  N N    . SER C 1 96  ? 18.926  -0.152  19.608  1.00 81.63  ? 96  SER C N    1 
ATOM   9944  C CA   . SER C 1 96  ? 20.272  -0.636  19.329  1.00 81.74  ? 96  SER C CA   1 
ATOM   9945  C C    . SER C 1 96  ? 20.243  -2.131  19.035  1.00 81.29  ? 96  SER C C    1 
ATOM   9946  O O    . SER C 1 96  ? 19.614  -2.905  19.760  1.00 78.54  ? 96  SER C O    1 
ATOM   9947  C CB   . SER C 1 96  ? 21.187  -0.345  20.517  1.00 78.77  ? 96  SER C CB   1 
ATOM   9948  O OG   . SER C 1 96  ? 20.891  -1.199  21.606  1.00 79.92  ? 96  SER C OG   1 
ATOM   9949  H H    . SER C 1 96  ? 18.843  0.245   20.367  1.00 97.96  ? 96  SER C H    1 
ATOM   9950  H HA   . SER C 1 96  ? 20.628  -0.179  18.552  1.00 98.08  ? 96  SER C HA   1 
ATOM   9951  H HB2  . SER C 1 96  ? 22.108  -0.486  20.247  1.00 94.52  ? 96  SER C HB2  1 
ATOM   9952  H HB3  . SER C 1 96  ? 21.059  0.576   20.794  1.00 94.52  ? 96  SER C HB3  1 
ATOM   9953  H HG   . SER C 1 96  ? 21.416  -1.046  22.243  1.00 95.91  ? 96  SER C HG   1 
ATOM   9954  N N    . GLY C 1 97  ? 20.921  -2.535  17.967  1.00 82.99  ? 97  GLY C N    1 
ATOM   9955  C CA   . GLY C 1 97  ? 20.935  -3.919  17.556  1.00 81.08  ? 97  GLY C CA   1 
ATOM   9956  C C    . GLY C 1 97  ? 19.787  -4.331  16.666  1.00 85.57  ? 97  GLY C C    1 
ATOM   9957  O O    . GLY C 1 97  ? 19.598  -5.534  16.444  1.00 87.73  ? 97  GLY C O    1 
ATOM   9958  H H    . GLY C 1 97  ? 21.384  -2.015  17.462  1.00 99.60  ? 97  GLY C H    1 
ATOM   9959  H HA2  . GLY C 1 97  ? 21.759  -4.091  17.074  1.00 97.30  ? 97  GLY C HA2  1 
ATOM   9960  H HA3  . GLY C 1 97  ? 20.910  -4.478  18.348  1.00 97.30  ? 97  GLY C HA3  1 
ATOM   9961  N N    . GLU C 1 98  ? 19.020  -3.379  16.144  1.00 86.55  ? 98  GLU C N    1 
ATOM   9962  C CA   . GLU C 1 98  ? 17.888  -3.643  15.260  1.00 85.82  ? 98  GLU C CA   1 
ATOM   9963  C C    . GLU C 1 98  ? 17.979  -2.671  14.093  1.00 86.31  ? 98  GLU C C    1 
ATOM   9964  O O    . GLU C 1 98  ? 17.792  -1.463  14.272  1.00 84.04  ? 98  GLU C O    1 
ATOM   9965  C CB   . GLU C 1 98  ? 16.562  -3.490  16.010  1.00 85.87  ? 98  GLU C CB   1 
ATOM   9966  C CG   . GLU C 1 98  ? 15.315  -3.913  15.236  1.00 88.15  ? 98  GLU C CG   1 
ATOM   9967  C CD   . GLU C 1 98  ? 15.544  -5.142  14.379  1.00 94.48  ? 98  GLU C CD   1 
ATOM   9968  O OE1  . GLU C 1 98  ? 16.246  -5.022  13.344  1.00 95.44  ? 98  GLU C OE1  1 
ATOM   9969  O OE2  . GLU C 1 98  ? 15.016  -6.220  14.733  1.00 91.68  ? 98  GLU C OE2  1 
ATOM   9970  H H    . GLU C 1 98  ? 19.139  -2.540  16.293  1.00 103.86 ? 98  GLU C H    1 
ATOM   9971  H HA   . GLU C 1 98  ? 17.936  -4.548  14.914  1.00 102.99 ? 98  GLU C HA   1 
ATOM   9972  H HB2  . GLU C 1 98  ? 16.602  -4.033  16.812  1.00 103.04 ? 98  GLU C HB2  1 
ATOM   9973  H HB3  . GLU C 1 98  ? 16.452  -2.556  16.246  1.00 103.04 ? 98  GLU C HB3  1 
ATOM   9974  H HG2  . GLU C 1 98  ? 14.606  -4.114  15.866  1.00 105.78 ? 98  GLU C HG2  1 
ATOM   9975  H HG3  . GLU C 1 98  ? 15.044  -3.187  14.653  1.00 105.78 ? 98  GLU C HG3  1 
ATOM   9976  N N    . SER C 1 99  ? 18.265  -3.199  12.901  1.00 91.48  ? 99  SER C N    1 
ATOM   9977  C CA   . SER C 1 99  ? 18.498  -2.350  11.741  1.00 92.44  ? 99  SER C CA   1 
ATOM   9978  C C    . SER C 1 99  ? 17.222  -1.726  11.198  1.00 91.14  ? 99  SER C C    1 
ATOM   9979  O O    . SER C 1 99  ? 17.296  -0.722  10.482  1.00 88.00  ? 99  SER C O    1 
ATOM   9980  C CB   . SER C 1 99  ? 19.161  -3.160  10.627  1.00 91.76  ? 99  SER C CB   1 
ATOM   9981  O OG   . SER C 1 99  ? 18.207  -4.005  10.003  1.00 91.26  ? 99  SER C OG   1 
ATOM   9982  H H    . SER C 1 99  ? 18.328  -4.042  12.742  1.00 109.77 ? 99  SER C H    1 
ATOM   9983  H HA   . SER C 1 99  ? 19.094  -1.634  12.010  1.00 110.93 ? 99  SER C HA   1 
ATOM   9984  H HB2  . SER C 1 99  ? 19.528  -2.552  9.966   1.00 110.11 ? 99  SER C HB2  1 
ATOM   9985  H HB3  . SER C 1 99  ? 19.869  -3.704  11.006  1.00 110.11 ? 99  SER C HB3  1 
ATOM   9986  H HG   . SER C 1 99  ? 18.575  -4.457  9.398   1.00 109.51 ? 99  SER C HG   1 
ATOM   9987  N N    . LYS C 1 100 ? 16.065  -2.299  11.503  1.00 93.98  ? 100 LYS C N    1 
ATOM   9988  C CA   . LYS C 1 100 ? 14.800  -1.838  10.958  1.00 92.16  ? 100 LYS C CA   1 
ATOM   9989  C C    . LYS C 1 100 ? 14.023  -1.046  11.998  1.00 92.57  ? 100 LYS C C    1 
ATOM   9990  O O    . LYS C 1 100 ? 14.068  -1.333  13.196  1.00 93.39  ? 100 LYS C O    1 
ATOM   9991  C CB   . LYS C 1 100 ? 13.959  -3.018  10.471  1.00 101.61 ? 100 LYS C CB   1 
ATOM   9992  C CG   . LYS C 1 100 ? 14.286  -3.442  9.042   1.00 107.10 ? 100 LYS C CG   1 
ATOM   9993  C CD   . LYS C 1 100 ? 13.227  -4.361  8.462   1.00 109.03 ? 100 LYS C CD   1 
ATOM   9994  C CE   . LYS C 1 100 ? 13.234  -4.362  6.932   1.00 110.88 ? 100 LYS C CE   1 
ATOM   9995  N NZ   . LYS C 1 100 ? 14.444  -3.747  6.316   1.00 114.48 ? 100 LYS C NZ   1 
ATOM   9996  H H    . LYS C 1 100 ? 15.988  -2.971  12.035  1.00 112.78 ? 100 LYS C H    1 
ATOM   9997  H HA   . LYS C 1 100 ? 14.973  -1.253  10.204  1.00 110.59 ? 100 LYS C HA   1 
ATOM   9998  H HB2  . LYS C 1 100 ? 14.118  -3.778  11.053  1.00 121.93 ? 100 LYS C HB2  1 
ATOM   9999  H HB3  . LYS C 1 100 ? 13.022  -2.768  10.501  1.00 121.93 ? 100 LYS C HB3  1 
ATOM   10000 H HG2  . LYS C 1 100 ? 14.343  -2.654  8.481   1.00 128.52 ? 100 LYS C HG2  1 
ATOM   10001 H HG3  . LYS C 1 100 ? 15.133  -3.916  9.037   1.00 128.52 ? 100 LYS C HG3  1 
ATOM   10002 H HD2  . LYS C 1 100 ? 13.392  -5.268  8.765   1.00 130.84 ? 100 LYS C HD2  1 
ATOM   10003 H HD3  . LYS C 1 100 ? 12.352  -4.065  8.759   1.00 130.84 ? 100 LYS C HD3  1 
ATOM   10004 H HE2  . LYS C 1 100 ? 13.185  -5.280  6.623   1.00 133.05 ? 100 LYS C HE2  1 
ATOM   10005 H HE3  . LYS C 1 100 ? 12.463  -3.865  6.619   1.00 133.05 ? 100 LYS C HE3  1 
ATOM   10006 H HZ1  . LYS C 1 100 ? 14.399  -3.807  5.430   1.00 137.38 ? 100 LYS C HZ1  1 
ATOM   10007 H HZ2  . LYS C 1 100 ? 14.499  -2.888  6.545   1.00 137.38 ? 100 LYS C HZ2  1 
ATOM   10008 H HZ3  . LYS C 1 100 ? 15.176  -4.167  6.598   1.00 137.38 ? 100 LYS C HZ3  1 
ATOM   10009 N N    . VAL C 1 101 ? 13.303  -0.034  11.515  1.00 90.06  ? 101 VAL C N    1 
ATOM   10010 C CA   . VAL C 1 101 ? 12.467  0.776   12.387  1.00 86.76  ? 101 VAL C CA   1 
ATOM   10011 C C    . VAL C 1 101 ? 11.356  -0.086  12.972  1.00 85.49  ? 101 VAL C C    1 
ATOM   10012 O O    . VAL C 1 101 ? 10.834  -0.997  12.315  1.00 89.70  ? 101 VAL C O    1 
ATOM   10013 C CB   . VAL C 1 101 ? 11.911  1.971   11.595  1.00 84.12  ? 101 VAL C CB   1 
ATOM   10014 C CG1  . VAL C 1 101 ? 10.752  2.577   12.318  1.00 87.32  ? 101 VAL C CG1  1 
ATOM   10015 C CG2  . VAL C 1 101 ? 13.002  3.013   11.365  1.00 77.08  ? 101 VAL C CG2  1 
ATOM   10016 H H    . VAL C 1 101 ? 13.283  0.201   10.688  1.00 108.07 ? 101 VAL C H    1 
ATOM   10017 H HA   . VAL C 1 101 ? 12.992  1.119   13.127  1.00 104.11 ? 101 VAL C HA   1 
ATOM   10018 H HB   . VAL C 1 101 ? 11.603  1.660   10.730  1.00 100.94 ? 101 VAL C HB   1 
ATOM   10019 H HG11 . VAL C 1 101 ? 10.601  3.472   11.978  1.00 104.78 ? 101 VAL C HG11 1 
ATOM   10020 H HG12 . VAL C 1 101 ? 9.965   2.029   12.168  1.00 104.78 ? 101 VAL C HG12 1 
ATOM   10021 H HG13 . VAL C 1 101 ? 10.954  2.613   13.266  1.00 104.78 ? 101 VAL C HG13 1 
ATOM   10022 H HG21 . VAL C 1 101 ? 12.636  3.742   10.840  1.00 92.49  ? 101 VAL C HG21 1 
ATOM   10023 H HG22 . VAL C 1 101 ? 13.308  3.345   12.223  1.00 92.49  ? 101 VAL C HG22 1 
ATOM   10024 H HG23 . VAL C 1 101 ? 13.739  2.599   10.888  1.00 92.49  ? 101 VAL C HG23 1 
ATOM   10025 N N    . LEU C 1 102 ? 10.992  0.194   14.223  1.00 87.62  ? 102 LEU C N    1 
ATOM   10026 C CA   . LEU C 1 102 ? 10.047  -0.629  14.971  1.00 85.66  ? 102 LEU C CA   1 
ATOM   10027 C C    . LEU C 1 102 ? 8.759   0.152   15.202  1.00 85.98  ? 102 LEU C C    1 
ATOM   10028 O O    . LEU C 1 102 ? 8.714   1.056   16.045  1.00 85.83  ? 102 LEU C O    1 
ATOM   10029 C CB   . LEU C 1 102 ? 10.657  -1.078  16.299  1.00 84.45  ? 102 LEU C CB   1 
ATOM   10030 C CG   . LEU C 1 102 ? 11.737  -2.155  16.194  1.00 86.49  ? 102 LEU C CG   1 
ATOM   10031 C CD1  . LEU C 1 102 ? 12.888  -1.853  17.149  1.00 82.30  ? 102 LEU C CD1  1 
ATOM   10032 C CD2  . LEU C 1 102 ? 11.155  -3.536  16.463  1.00 85.40  ? 102 LEU C CD2  1 
ATOM   10033 H H    . LEU C 1 102 ? 11.286  0.869   14.667  1.00 105.14 ? 102 LEU C H    1 
ATOM   10034 H HA   . LEU C 1 102 ? 9.828   -1.410  14.438  1.00 102.79 ? 102 LEU C HA   1 
ATOM   10035 H HB2  . LEU C 1 102 ? 11.058  -0.306  16.727  1.00 101.34 ? 102 LEU C HB2  1 
ATOM   10036 H HB3  . LEU C 1 102 ? 9.946   -1.434  16.855  1.00 101.34 ? 102 LEU C HB3  1 
ATOM   10037 H HG   . LEU C 1 102 ? 12.091  -2.157  15.291  1.00 103.79 ? 102 LEU C HG   1 
ATOM   10038 H HD11 . LEU C 1 102 ? 13.535  -2.574  17.102  1.00 98.76  ? 102 LEU C HD11 1 
ATOM   10039 H HD12 . LEU C 1 102 ? 13.305  -1.017  16.887  1.00 98.76  ? 102 LEU C HD12 1 
ATOM   10040 H HD13 . LEU C 1 102 ? 12.539  -1.779  18.051  1.00 98.76  ? 102 LEU C HD13 1 
ATOM   10041 H HD21 . LEU C 1 102 ? 11.851  -4.201  16.343  1.00 102.48 ? 102 LEU C HD21 1 
ATOM   10042 H HD22 . LEU C 1 102 ? 10.822  -3.567  17.374  1.00 102.48 ? 102 LEU C HD22 1 
ATOM   10043 H HD23 . LEU C 1 102 ? 10.430  -3.700  15.840  1.00 102.48 ? 102 LEU C HD23 1 
ATOM   10044 N N    . ASP C 1 103 ? 7.715   -0.206  14.455  1.00 87.72  ? 103 ASP C N    1 
ATOM   10045 C CA   . ASP C 1 103 ? 6.380   0.350   14.654  1.00 85.30  ? 103 ASP C CA   1 
ATOM   10046 C C    . ASP C 1 103 ? 5.727   -0.383  15.819  1.00 88.54  ? 103 ASP C C    1 
ATOM   10047 O O    . ASP C 1 103 ? 5.466   -1.589  15.734  1.00 94.22  ? 103 ASP C O    1 
ATOM   10048 C CB   . ASP C 1 103 ? 5.559   0.212   13.377  1.00 87.26  ? 103 ASP C CB   1 
ATOM   10049 C CG   . ASP C 1 103 ? 4.249   0.974   13.438  1.00 89.19  ? 103 ASP C CG   1 
ATOM   10050 O OD1  . ASP C 1 103 ? 4.021   1.703   14.425  1.00 90.15  ? 103 ASP C OD1  1 
ATOM   10051 O OD2  . ASP C 1 103 ? 3.443   0.839   12.495  1.00 87.41  ? 103 ASP C OD2  1 
ATOM   10052 H H    . ASP C 1 103 ? 7.757   -0.779  13.816  1.00 105.26 ? 103 ASP C H    1 
ATOM   10053 H HA   . ASP C 1 103 ? 6.440   1.293   14.874  1.00 102.36 ? 103 ASP C HA   1 
ATOM   10054 H HB2  . ASP C 1 103 ? 6.073   0.559   12.631  1.00 104.71 ? 103 ASP C HB2  1 
ATOM   10055 H HB3  . ASP C 1 103 ? 5.354   -0.725  13.232  1.00 104.71 ? 103 ASP C HB3  1 
ATOM   10056 N N    . VAL C 1 104 ? 5.471   0.335   16.913  1.00 85.99  ? 104 VAL C N    1 
ATOM   10057 C CA   . VAL C 1 104 ? 4.941   -0.250  18.140  1.00 84.61  ? 104 VAL C CA   1 
ATOM   10058 C C    . VAL C 1 104 ? 3.502   0.207   18.319  1.00 83.20  ? 104 VAL C C    1 
ATOM   10059 O O    . VAL C 1 104 ? 3.207   1.405   18.228  1.00 83.29  ? 104 VAL C O    1 
ATOM   10060 C CB   . VAL C 1 104 ? 5.792   0.137   19.364  1.00 83.90  ? 104 VAL C CB   1 
ATOM   10061 C CG1  . VAL C 1 104 ? 5.419   -0.725  20.564  1.00 80.50  ? 104 VAL C CG1  1 
ATOM   10062 C CG2  . VAL C 1 104 ? 7.272   0.008   19.046  1.00 83.70  ? 104 VAL C CG2  1 
ATOM   10063 H H    . VAL C 1 104 ? 5.601   1.183   16.967  1.00 103.18 ? 104 VAL C H    1 
ATOM   10064 H HA   . VAL C 1 104 ? 4.944   -1.216  18.053  1.00 101.53 ? 104 VAL C HA   1 
ATOM   10065 H HB   . VAL C 1 104 ? 5.614   1.063   19.590  1.00 100.67 ? 104 VAL C HB   1 
ATOM   10066 H HG11 . VAL C 1 104 ? 5.991   -0.490  21.311  1.00 96.60  ? 104 VAL C HG11 1 
ATOM   10067 H HG12 . VAL C 1 104 ? 4.491   -0.561  20.795  1.00 96.60  ? 104 VAL C HG12 1 
ATOM   10068 H HG13 . VAL C 1 104 ? 5.542   -1.659  20.333  1.00 96.60  ? 104 VAL C HG13 1 
ATOM   10069 H HG21 . VAL C 1 104 ? 7.777   0.050   19.874  1.00 100.44 ? 104 VAL C HG21 1 
ATOM   10070 H HG22 . VAL C 1 104 ? 7.428   -0.842  18.606  1.00 100.44 ? 104 VAL C HG22 1 
ATOM   10071 H HG23 . VAL C 1 104 ? 7.534   0.736   18.462  1.00 100.44 ? 104 VAL C HG23 1 
ATOM   10072 N N    . ASP C 1 105 ? 2.613   -0.743  18.589  1.00 83.82  ? 105 ASP C N    1 
ATOM   10073 C CA   . ASP C 1 105 ? 1.185   -0.476  18.774  1.00 84.50  ? 105 ASP C CA   1 
ATOM   10074 C C    . ASP C 1 105 ? 0.911   -0.403  20.272  1.00 81.94  ? 105 ASP C C    1 
ATOM   10075 O O    . ASP C 1 105 ? 0.853   -1.426  20.956  1.00 84.60  ? 105 ASP C O    1 
ATOM   10076 C CB   . ASP C 1 105 ? 0.347   -1.555  18.105  1.00 85.74  ? 105 ASP C CB   1 
ATOM   10077 C CG   . ASP C 1 105 ? -1.144  -1.334  18.296  1.00 87.76  ? 105 ASP C CG   1 
ATOM   10078 O OD1  . ASP C 1 105 ? -1.522  -0.317  18.915  1.00 89.41  ? 105 ASP C OD1  1 
ATOM   10079 O OD2  . ASP C 1 105 ? -1.939  -2.181  17.832  1.00 87.34  ? 105 ASP C OD2  1 
ATOM   10080 H H    . ASP C 1 105 ? 2.817   -1.575  18.674  1.00 100.58 ? 105 ASP C H    1 
ATOM   10081 H HA   . ASP C 1 105 ? 0.961   0.380   18.376  1.00 101.40 ? 105 ASP C HA   1 
ATOM   10082 H HB2  . ASP C 1 105 ? 0.531   -1.556  17.153  1.00 102.90 ? 105 ASP C HB2  1 
ATOM   10083 H HB3  . ASP C 1 105 ? 0.575   -2.416  18.488  1.00 102.90 ? 105 ASP C HB3  1 
ATOM   10084 N N    . VAL C 1 106 ? 0.714   0.815   20.779  1.00 85.41  ? 106 VAL C N    1 
ATOM   10085 C CA   . VAL C 1 106 ? 0.481   1.057   22.198  1.00 84.48  ? 106 VAL C CA   1 
ATOM   10086 C C    . VAL C 1 106 ? -1.002  1.318   22.421  1.00 85.31  ? 106 VAL C C    1 
ATOM   10087 O O    . VAL C 1 106 ? -1.637  2.060   21.661  1.00 84.28  ? 106 VAL C O    1 
ATOM   10088 C CB   . VAL C 1 106 ? 1.326   2.239   22.711  1.00 82.38  ? 106 VAL C CB   1 
ATOM   10089 C CG1  . VAL C 1 106 ? 1.028   2.514   24.184  1.00 86.36  ? 106 VAL C CG1  1 
ATOM   10090 C CG2  . VAL C 1 106 ? 2.807   1.967   22.505  1.00 78.94  ? 106 VAL C CG2  1 
ATOM   10091 H H    . VAL C 1 106 ? 0.713   1.534   20.306  1.00 102.50 ? 106 VAL C H    1 
ATOM   10092 H HA   . VAL C 1 106 ? 0.731   0.262   22.696  1.00 101.38 ? 106 VAL C HA   1 
ATOM   10093 H HB   . VAL C 1 106 ? 1.093   3.033   22.204  1.00 98.85  ? 106 VAL C HB   1 
ATOM   10094 H HG11 . VAL C 1 106 ? 1.710   3.104   24.540  1.00 103.64 ? 106 VAL C HG11 1 
ATOM   10095 H HG12 . VAL C 1 106 ? 0.157   2.935   24.256  1.00 103.64 ? 106 VAL C HG12 1 
ATOM   10096 H HG13 . VAL C 1 106 ? 1.031   1.674   24.669  1.00 103.64 ? 106 VAL C HG13 1 
ATOM   10097 H HG21 . VAL C 1 106 ? 3.318   2.707   22.870  1.00 94.73  ? 106 VAL C HG21 1 
ATOM   10098 H HG22 . VAL C 1 106 ? 3.043   1.145   22.961  1.00 94.73  ? 106 VAL C HG22 1 
ATOM   10099 H HG23 . VAL C 1 106 ? 2.982   1.881   21.555  1.00 94.73  ? 106 VAL C HG23 1 
ATOM   10100 N N    . ARG C 1 107 ? -1.556  0.712   23.470  1.00 88.14  ? 107 ARG C N    1 
ATOM   10101 C CA   . ARG C 1 107 ? -2.959  0.883   23.816  1.00 89.65  ? 107 ARG C CA   1 
ATOM   10102 C C    . ARG C 1 107 ? -3.091  0.993   25.328  1.00 92.69  ? 107 ARG C C    1 
ATOM   10103 O O    . ARG C 1 107 ? -2.248  0.496   26.079  1.00 88.91  ? 107 ARG C O    1 
ATOM   10104 C CB   . ARG C 1 107 ? -3.816  -0.280  23.296  1.00 89.14  ? 107 ARG C CB   1 
ATOM   10105 C CG   . ARG C 1 107 ? -3.470  -0.734  21.885  1.00 86.27  ? 107 ARG C CG   1 
ATOM   10106 C CD   . ARG C 1 107 ? -4.054  -2.108  21.583  1.00 84.53  ? 107 ARG C CD   1 
ATOM   10107 N NE   . ARG C 1 107 ? -3.281  -3.187  22.189  1.00 87.72  ? 107 ARG C NE   1 
ATOM   10108 C CZ   . ARG C 1 107 ? -2.039  -3.506  21.849  1.00 86.68  ? 107 ARG C CZ   1 
ATOM   10109 N NH1  . ARG C 1 107 ? -1.383  -2.834  20.918  1.00 88.84  ? 107 ARG C NH1  1 
ATOM   10110 N NH2  . ARG C 1 107 ? -1.442  -4.528  22.455  1.00 84.37  ? 107 ARG C NH2  1 
ATOM   10111 H H    . ARG C 1 107 ? -1.130  0.188   24.003  1.00 105.77 ? 107 ARG C H    1 
ATOM   10112 H HA   . ARG C 1 107 ? -3.293  1.704   23.422  1.00 107.59 ? 107 ARG C HA   1 
ATOM   10113 H HB2  . ARG C 1 107 ? -3.698  -1.041  23.886  1.00 106.97 ? 107 ARG C HB2  1 
ATOM   10114 H HB3  . ARG C 1 107 ? -4.746  -0.003  23.295  1.00 106.97 ? 107 ARG C HB3  1 
ATOM   10115 H HG2  . ARG C 1 107 ? -3.833  -0.101  21.245  1.00 103.52 ? 107 ARG C HG2  1 
ATOM   10116 H HG3  . ARG C 1 107 ? -2.506  -0.785  21.791  1.00 103.52 ? 107 ARG C HG3  1 
ATOM   10117 H HD2  . ARG C 1 107 ? -4.958  -2.152  21.932  1.00 101.43 ? 107 ARG C HD2  1 
ATOM   10118 H HD3  . ARG C 1 107 ? -4.062  -2.246  20.623  1.00 101.43 ? 107 ARG C HD3  1 
ATOM   10119 H HE   . ARG C 1 107 ? -3.657  -3.648  22.811  1.00 105.26 ? 107 ARG C HE   1 
ATOM   10120 H HH11 . ARG C 1 107 ? -1.762  -2.173  20.517  1.00 106.61 ? 107 ARG C HH11 1 
ATOM   10121 H HH12 . ARG C 1 107 ? -0.579  -3.058  20.712  1.00 106.61 ? 107 ARG C HH12 1 
ATOM   10122 H HH21 . ARG C 1 107 ? -1.861  -4.974  23.060  1.00 101.24 ? 107 ARG C HH21 1 
ATOM   10123 H HH22 . ARG C 1 107 ? -0.637  -4.744  22.242  1.00 101.24 ? 107 ARG C HH22 1 
ATOM   10124 N N    . ASN C 1 108 ? -4.155  1.663   25.766  1.00 105.41 ? 108 ASN C N    1 
ATOM   10125 C CA   . ASN C 1 108 ? -4.426  1.805   27.189  1.00 103.57 ? 108 ASN C CA   1 
ATOM   10126 C C    . ASN C 1 108 ? -4.732  0.444   27.805  1.00 102.54 ? 108 ASN C C    1 
ATOM   10127 O O    . ASN C 1 108 ? -5.287  -0.447  27.158  1.00 105.60 ? 108 ASN C O    1 
ATOM   10128 C CB   . ASN C 1 108 ? -5.593  2.766   27.408  1.00 109.05 ? 108 ASN C CB   1 
ATOM   10129 C CG   . ASN C 1 108 ? -6.011  2.857   28.863  1.00 112.57 ? 108 ASN C CG   1 
ATOM   10130 O OD1  . ASN C 1 108 ? -6.394  1.859   29.471  1.00 115.25 ? 108 ASN C OD1  1 
ATOM   10131 N ND2  . ASN C 1 108 ? -5.947  4.059   29.426  1.00 112.21 ? 108 ASN C ND2  1 
ATOM   10132 H H    . ASN C 1 108 ? -4.734  2.044   25.257  1.00 126.49 ? 108 ASN C H    1 
ATOM   10133 H HA   . ASN C 1 108 ? -3.650  2.172   27.640  1.00 124.28 ? 108 ASN C HA   1 
ATOM   10134 H HB2  . ASN C 1 108 ? -5.333  3.653   27.115  1.00 130.87 ? 108 ASN C HB2  1 
ATOM   10135 H HB3  . ASN C 1 108 ? -6.357  2.458   26.895  1.00 130.87 ? 108 ASN C HB3  1 
ATOM   10136 H HD21 . ASN C 1 108 ? -5.678  4.735   28.967  1.00 134.65 ? 108 ASN C HD21 1 
ATOM   10137 H HD22 . ASN C 1 108 ? -6.173  4.161   30.249  1.00 134.65 ? 108 ASN C HD22 1 
ATOM   10138 N N    . ASP C 1 109 ? -4.366  0.292   29.080  1.00 97.09  ? 109 ASP C N    1 
ATOM   10139 C CA   . ASP C 1 109 ? -4.489  -0.981  29.782  1.00 97.85  ? 109 ASP C CA   1 
ATOM   10140 C C    . ASP C 1 109 ? -5.191  -0.841  31.131  1.00 98.29  ? 109 ASP C C    1 
ATOM   10141 O O    . ASP C 1 109 ? -5.184  -1.788  31.926  1.00 96.92  ? 109 ASP C O    1 
ATOM   10142 C CB   . ASP C 1 109 ? -3.096  -1.608  29.955  1.00 95.29  ? 109 ASP C CB   1 
ATOM   10143 C CG   . ASP C 1 109 ? -3.129  -2.923  30.712  1.00 94.25  ? 109 ASP C CG   1 
ATOM   10144 O OD1  . ASP C 1 109 ? -4.180  -3.601  30.691  1.00 93.77  ? 109 ASP C OD1  1 
ATOM   10145 O OD2  . ASP C 1 109 ? -2.101  -3.270  31.335  1.00 96.16  ? 109 ASP C OD2  1 
ATOM   10146 H H    . ASP C 1 109 ? -4.038  0.923   29.564  1.00 116.51 ? 109 ASP C H    1 
ATOM   10147 H HA   . ASP C 1 109 ? -5.028  -1.590  29.254  1.00 117.42 ? 109 ASP C HA   1 
ATOM   10148 H HB2  . ASP C 1 109 ? -2.716  -1.777  29.079  1.00 114.34 ? 109 ASP C HB2  1 
ATOM   10149 H HB3  . ASP C 1 109 ? -2.532  -0.992  30.448  1.00 114.34 ? 109 ASP C HB3  1 
ATOM   10150 N N    . GLY C 1 110 ? -5.809  0.301   31.409  1.00 101.27 ? 110 GLY C N    1 
ATOM   10151 C CA   . GLY C 1 110 ? -6.603  0.438   32.613  1.00 100.85 ? 110 GLY C CA   1 
ATOM   10152 C C    . GLY C 1 110 ? -6.450  1.772   33.308  1.00 101.36 ? 110 GLY C C    1 
ATOM   10153 O O    . GLY C 1 110 ? -7.325  2.189   34.073  1.00 105.95 ? 110 GLY C O    1 
ATOM   10154 H H    . GLY C 1 110 ? -5.782  1.005   30.917  1.00 121.52 ? 110 GLY C H    1 
ATOM   10155 H HA2  . GLY C 1 110 ? -7.540  0.326   32.386  1.00 121.02 ? 110 GLY C HA2  1 
ATOM   10156 H HA3  . GLY C 1 110 ? -6.346  -0.256  33.240  1.00 121.02 ? 110 GLY C HA3  1 
ATOM   10157 N N    . ALA C 1 111 ? -5.339  2.450   33.056  1.00 98.34  ? 111 ALA C N    1 
ATOM   10158 C CA   . ALA C 1 111 ? -5.067  3.739   33.675  1.00 95.72  ? 111 ALA C CA   1 
ATOM   10159 C C    . ALA C 1 111 ? -4.016  4.451   32.835  1.00 93.70  ? 111 ALA C C    1 
ATOM   10160 O O    . ALA C 1 111 ? -3.571  3.943   31.802  1.00 94.41  ? 111 ALA C O    1 
ATOM   10161 C CB   . ALA C 1 111 ? -4.616  3.568   35.127  1.00 93.65  ? 111 ALA C CB   1 
ATOM   10162 H H    . ALA C 1 111 ? -4.720  2.182   32.522  1.00 118.01 ? 111 ALA C H    1 
ATOM   10163 H HA   . ALA C 1 111 ? -5.875  4.275   33.672  1.00 114.87 ? 111 ALA C HA   1 
ATOM   10164 H HB1  . ALA C 1 111 ? -4.455  4.443   35.513  1.00 112.38 ? 111 ALA C HB1  1 
ATOM   10165 H HB2  . ALA C 1 111 ? -5.313  3.111   35.623  1.00 112.38 ? 111 ALA C HB2  1 
ATOM   10166 H HB3  . ALA C 1 111 ? -3.800  3.044   35.145  1.00 112.38 ? 111 ALA C HB3  1 
ATOM   10167 N N    . LYS C 1 112 ? -3.614  5.636   33.294  1.00 89.91  ? 112 LYS C N    1 
ATOM   10168 C CA   . LYS C 1 112 ? -2.704  6.454   32.504  1.00 87.21  ? 112 LYS C CA   1 
ATOM   10169 C C    . LYS C 1 112 ? -1.283  5.908   32.520  1.00 86.56  ? 112 LYS C C    1 
ATOM   10170 O O    . LYS C 1 112 ? -0.498  6.237   31.626  1.00 85.23  ? 112 LYS C O    1 
ATOM   10171 C CB   . LYS C 1 112 ? -2.705  7.901   33.007  1.00 89.97  ? 112 LYS C CB   1 
ATOM   10172 C CG   . LYS C 1 112 ? -4.080  8.570   33.215  1.00 93.54  ? 112 LYS C CG   1 
ATOM   10173 C CD   . LYS C 1 112 ? -5.215  7.990   32.377  1.00 96.05  ? 112 LYS C CD   1 
ATOM   10174 C CE   . LYS C 1 112 ? -6.569  8.227   33.069  1.00 100.58 ? 112 LYS C CE   1 
ATOM   10175 N NZ   . LYS C 1 112 ? -7.641  7.327   32.552  1.00 102.32 ? 112 LYS C NZ   1 
ATOM   10176 H H    . LYS C 1 112 ? -3.850  5.981   34.046  1.00 107.89 ? 112 LYS C H    1 
ATOM   10177 H HA   . LYS C 1 112 ? -3.019  6.461   31.587  1.00 104.65 ? 112 LYS C HA   1 
ATOM   10178 H HB2  . LYS C 1 112 ? -2.249  7.920   33.863  1.00 107.96 ? 112 LYS C HB2  1 
ATOM   10179 H HB3  . LYS C 1 112 ? -2.223  8.441   32.362  1.00 107.96 ? 112 LYS C HB3  1 
ATOM   10180 H HG2  . LYS C 1 112 ? -4.330  8.474   34.147  1.00 112.25 ? 112 LYS C HG2  1 
ATOM   10181 H HG3  . LYS C 1 112 ? -4.002  9.509   32.986  1.00 112.25 ? 112 LYS C HG3  1 
ATOM   10182 H HD2  . LYS C 1 112 ? -5.232  8.422   31.509  1.00 115.25 ? 112 LYS C HD2  1 
ATOM   10183 H HD3  . LYS C 1 112 ? -5.085  7.035   32.270  1.00 115.25 ? 112 LYS C HD3  1 
ATOM   10184 H HE2  . LYS C 1 112 ? -6.472  8.063   34.020  1.00 120.69 ? 112 LYS C HE2  1 
ATOM   10185 H HE3  . LYS C 1 112 ? -6.847  9.144   32.917  1.00 120.69 ? 112 LYS C HE3  1 
ATOM   10186 H HZ1  . LYS C 1 112 ? -8.409  7.499   32.968  1.00 122.78 ? 112 LYS C HZ1  1 
ATOM   10187 H HZ2  . LYS C 1 112 ? -7.750  7.456   31.678  1.00 122.78 ? 112 LYS C HZ2  1 
ATOM   10188 H HZ3  . LYS C 1 112 ? -7.419  6.477   32.694  1.00 122.78 ? 112 LYS C HZ3  1 
ATOM   10189 N N    . ASN C 1 113 ? -0.936  5.085   33.506  1.00 87.09  ? 113 ASN C N    1 
ATOM   10190 C CA   . ASN C 1 113 ? 0.396   4.506   33.603  1.00 84.30  ? 113 ASN C CA   1 
ATOM   10191 C C    . ASN C 1 113 ? 0.459   3.072   33.094  1.00 85.56  ? 113 ASN C C    1 
ATOM   10192 O O    . ASN C 1 113 ? 1.545   2.479   33.086  1.00 81.48  ? 113 ASN C O    1 
ATOM   10193 C CB   . ASN C 1 113 ? 0.888   4.553   35.052  1.00 82.42  ? 113 ASN C CB   1 
ATOM   10194 C CG   . ASN C 1 113 ? 0.049   3.698   35.977  1.00 85.82  ? 113 ASN C CG   1 
ATOM   10195 O OD1  . ASN C 1 113 ? -1.171  3.614   35.830  1.00 88.42  ? 113 ASN C OD1  1 
ATOM   10196 N ND2  . ASN C 1 113 ? 0.701   3.059   36.941  1.00 85.08  ? 113 ASN C ND2  1 
ATOM   10197 H H    . ASN C 1 113 ? -1.465  4.844   34.139  1.00 104.51 ? 113 ASN C H    1 
ATOM   10198 H HA   . ASN C 1 113 ? 1.001   5.040   33.064  1.00 101.17 ? 113 ASN C HA   1 
ATOM   10199 H HB2  . ASN C 1 113 ? 1.801   4.227   35.088  1.00 98.90  ? 113 ASN C HB2  1 
ATOM   10200 H HB3  . ASN C 1 113 ? 0.850   5.468   35.371  1.00 98.90  ? 113 ASN C HB3  1 
ATOM   10201 H HD21 . ASN C 1 113 ? 1.553   3.144   37.013  1.00 102.10 ? 113 ASN C HD21 1 
ATOM   10202 H HD22 . ASN C 1 113 ? 0.270   2.560   37.493  1.00 102.10 ? 113 ASN C HD22 1 
ATOM   10203 N N    . LYS C 1 114 ? -0.664  2.506   32.658  1.00 85.62  ? 114 LYS C N    1 
ATOM   10204 C CA   . LYS C 1 114 ? -0.733  1.116   32.223  1.00 87.38  ? 114 LYS C CA   1 
ATOM   10205 C C    . LYS C 1 114 ? -0.971  1.059   30.721  1.00 89.46  ? 114 LYS C C    1 
ATOM   10206 O O    . LYS C 1 114 ? -1.831  1.779   30.197  1.00 91.81  ? 114 LYS C O    1 
ATOM   10207 C CB   . LYS C 1 114 ? -1.833  0.367   32.978  1.00 91.70  ? 114 LYS C CB   1 
ATOM   10208 C CG   . LYS C 1 114 ? -1.512  0.121   34.452  1.00 89.39  ? 114 LYS C CG   1 
ATOM   10209 C CD   . LYS C 1 114 ? -2.625  -0.651  35.156  1.00 93.76  ? 114 LYS C CD   1 
ATOM   10210 C CE   . LYS C 1 114 ? -2.203  -2.082  35.481  1.00 98.79  ? 114 LYS C CE   1 
ATOM   10211 N NZ   . LYS C 1 114 ? -3.002  -2.670  36.602  1.00 109.86 ? 114 LYS C NZ   1 
ATOM   10212 H H    . LYS C 1 114 ? -1.417  2.919   32.603  1.00 102.74 ? 114 LYS C H    1 
ATOM   10213 H HA   . LYS C 1 114 ? 0.112   0.674   32.404  1.00 104.85 ? 114 LYS C HA   1 
ATOM   10214 H HB2  . LYS C 1 114 ? -2.650  0.888   32.936  1.00 110.04 ? 114 LYS C HB2  1 
ATOM   10215 H HB3  . LYS C 1 114 ? -1.968  -0.496  32.556  1.00 110.04 ? 114 LYS C HB3  1 
ATOM   10216 H HG2  . LYS C 1 114 ? -0.695  -0.397  34.520  1.00 107.26 ? 114 LYS C HG2  1 
ATOM   10217 H HG3  . LYS C 1 114 ? -1.402  0.973   34.902  1.00 107.26 ? 114 LYS C HG3  1 
ATOM   10218 H HD2  . LYS C 1 114 ? -2.848  -0.204  35.987  1.00 112.51 ? 114 LYS C HD2  1 
ATOM   10219 H HD3  . LYS C 1 114 ? -3.404  -0.687  34.579  1.00 112.51 ? 114 LYS C HD3  1 
ATOM   10220 H HE2  . LYS C 1 114 ? -2.331  -2.637  34.696  1.00 118.55 ? 114 LYS C HE2  1 
ATOM   10221 H HE3  . LYS C 1 114 ? -1.269  -2.086  35.741  1.00 118.55 ? 114 LYS C HE3  1 
ATOM   10222 H HZ1  . LYS C 1 114 ? -2.732  -3.502  36.764  1.00 131.83 ? 114 LYS C HZ1  1 
ATOM   10223 H HZ2  . LYS C 1 114 ? -2.895  -2.183  37.340  1.00 131.83 ? 114 LYS C HZ2  1 
ATOM   10224 H HZ3  . LYS C 1 114 ? -3.865  -2.683  36.387  1.00 131.83 ? 114 LYS C HZ3  1 
ATOM   10225 N N    . PHE C 1 115 ? -0.225  0.197   30.039  1.00 86.42  ? 115 PHE C N    1 
ATOM   10226 C CA   . PHE C 1 115 ? -0.284  0.121   28.591  1.00 87.72  ? 115 PHE C CA   1 
ATOM   10227 C C    . PHE C 1 115 ? -0.110  -1.317  28.128  1.00 85.38  ? 115 PHE C C    1 
ATOM   10228 O O    . PHE C 1 115 ? 0.493   -2.144  28.815  1.00 82.95  ? 115 PHE C O    1 
ATOM   10229 C CB   . PHE C 1 115 ? 0.803   0.996   27.944  1.00 84.28  ? 115 PHE C CB   1 
ATOM   10230 C CG   . PHE C 1 115 ? 0.669   2.465   28.239  1.00 82.75  ? 115 PHE C CG   1 
ATOM   10231 C CD1  . PHE C 1 115 ? -0.391  3.195   27.729  1.00 85.16  ? 115 PHE C CD1  1 
ATOM   10232 C CD2  . PHE C 1 115 ? 1.612   3.116   29.014  1.00 83.68  ? 115 PHE C CD2  1 
ATOM   10233 C CE1  . PHE C 1 115 ? -0.514  4.545   27.993  1.00 82.98  ? 115 PHE C CE1  1 
ATOM   10234 C CE2  . PHE C 1 115 ? 1.493   4.469   29.281  1.00 84.92  ? 115 PHE C CE2  1 
ATOM   10235 C CZ   . PHE C 1 115 ? 0.430   5.184   28.767  1.00 83.02  ? 115 PHE C CZ   1 
ATOM   10236 H H    . PHE C 1 115 ? 0.326   -0.358  30.398  1.00 103.70 ? 115 PHE C H    1 
ATOM   10237 H HA   . PHE C 1 115 ? -1.157  0.424   28.298  1.00 105.27 ? 115 PHE C HA   1 
ATOM   10238 H HB2  . PHE C 1 115 ? 1.669   0.708   28.272  1.00 101.14 ? 115 PHE C HB2  1 
ATOM   10239 H HB3  . PHE C 1 115 ? 0.759   0.884   26.982  1.00 101.14 ? 115 PHE C HB3  1 
ATOM   10240 H HD1  . PHE C 1 115 ? -1.028  2.770   27.202  1.00 102.19 ? 115 PHE C HD1  1 
ATOM   10241 H HD2  . PHE C 1 115 ? 2.332   2.640   29.359  1.00 100.42 ? 115 PHE C HD2  1 
ATOM   10242 H HE1  . PHE C 1 115 ? -1.235  5.022   27.649  1.00 99.58  ? 115 PHE C HE1  1 
ATOM   10243 H HE2  . PHE C 1 115 ? 2.130   4.897   29.807  1.00 101.90 ? 115 PHE C HE2  1 
ATOM   10244 H HZ   . PHE C 1 115 ? 0.352   6.094   28.943  1.00 99.63  ? 115 PHE C HZ   1 
ATOM   10245 N N    . LEU C 1 116 ? -0.659  -1.603  26.954  1.00 88.08  ? 116 LEU C N    1 
ATOM   10246 C CA   . LEU C 1 116 ? -0.403  -2.839  26.224  1.00 85.89  ? 116 LEU C CA   1 
ATOM   10247 C C    . LEU C 1 116 ? 0.346   -2.466  24.950  1.00 83.71  ? 116 LEU C C    1 
ATOM   10248 O O    . LEU C 1 116 ? -0.154  -1.669  24.147  1.00 85.96  ? 116 LEU C O    1 
ATOM   10249 C CB   . LEU C 1 116 ? -1.702  -3.570  25.897  1.00 84.20  ? 116 LEU C CB   1 
ATOM   10250 C CG   . LEU C 1 116 ? -2.333  -4.376  27.030  1.00 85.96  ? 116 LEU C CG   1 
ATOM   10251 C CD1  . LEU C 1 116 ? -3.692  -4.914  26.597  1.00 82.12  ? 116 LEU C CD1  1 
ATOM   10252 C CD2  . LEU C 1 116 ? -1.427  -5.512  27.474  1.00 85.87  ? 116 LEU C CD2  1 
ATOM   10253 H H    . LEU C 1 116 ? -1.204  -1.078  26.545  1.00 105.69 ? 116 LEU C H    1 
ATOM   10254 H HA   . LEU C 1 116 ? 0.142   -3.439  26.757  1.00 103.07 ? 116 LEU C HA   1 
ATOM   10255 H HB2  . LEU C 1 116 ? -2.356  -2.911  25.618  1.00 101.03 ? 116 LEU C HB2  1 
ATOM   10256 H HB3  . LEU C 1 116 ? -1.525  -4.189  25.172  1.00 101.03 ? 116 LEU C HB3  1 
ATOM   10257 H HG   . LEU C 1 116 ? -2.458  -3.791  27.794  1.00 103.15 ? 116 LEU C HG   1 
ATOM   10258 H HD11 . LEU C 1 116 ? -4.080  -5.418  27.329  1.00 98.54  ? 116 LEU C HD11 1 
ATOM   10259 H HD12 . LEU C 1 116 ? -4.268  -4.168  26.366  1.00 98.54  ? 116 LEU C HD12 1 
ATOM   10260 H HD13 . LEU C 1 116 ? -3.572  -5.490  25.825  1.00 98.54  ? 116 LEU C HD13 1 
ATOM   10261 H HD21 . LEU C 1 116 ? -1.915  -6.085  28.085  1.00 103.05 ? 116 LEU C HD21 1 
ATOM   10262 H HD22 . LEU C 1 116 ? -1.151  -6.019  26.694  1.00 103.05 ? 116 LEU C HD22 1 
ATOM   10263 H HD23 . LEU C 1 116 ? -0.649  -5.140  27.919  1.00 103.05 ? 116 LEU C HD23 1 
ATOM   10264 N N    . ALA C 1 117 ? 1.539   -3.029  24.768  1.00 83.43  ? 117 ALA C N    1 
ATOM   10265 C CA   . ALA C 1 117 ? 2.420   -2.657  23.666  1.00 83.24  ? 117 ALA C CA   1 
ATOM   10266 C C    . ALA C 1 117 ? 2.765   -3.888  22.844  1.00 82.96  ? 117 ALA C C    1 
ATOM   10267 O O    . ALA C 1 117 ? 3.302   -4.863  23.378  1.00 83.36  ? 117 ALA C O    1 
ATOM   10268 C CB   . ALA C 1 117 ? 3.698   -1.994  24.191  1.00 80.19  ? 117 ALA C CB   1 
ATOM   10269 H H    . ALA C 1 117 ? 1.865   -3.639  25.279  1.00 100.12 ? 117 ALA C H    1 
ATOM   10270 H HA   . ALA C 1 117 ? 1.953   -2.034  23.088  1.00 99.89  ? 117 ALA C HA   1 
ATOM   10271 H HB1  . ALA C 1 117 ? 4.264   -1.759  23.439  1.00 96.22  ? 117 ALA C HB1  1 
ATOM   10272 H HB2  . ALA C 1 117 ? 3.459   -1.196  24.688  1.00 96.22  ? 117 ALA C HB2  1 
ATOM   10273 H HB3  . ALA C 1 117 ? 4.162   -2.618  24.771  1.00 96.22  ? 117 ALA C HB3  1 
ATOM   10274 N N    . LYS C 1 118 ? 2.473   -3.833  21.545  1.00 83.95  ? 118 LYS C N    1 
ATOM   10275 C CA   . LYS C 1 118 ? 2.800   -4.898  20.606  1.00 84.68  ? 118 LYS C CA   1 
ATOM   10276 C C    . LYS C 1 118 ? 3.934   -4.448  19.692  1.00 82.69  ? 118 LYS C C    1 
ATOM   10277 O O    . LYS C 1 118 ? 3.931   -3.320  19.191  1.00 82.72  ? 118 LYS C O    1 
ATOM   10278 C CB   . LYS C 1 118 ? 1.574   -5.284  19.776  1.00 86.91  ? 118 LYS C CB   1 
ATOM   10279 C CG   . LYS C 1 118 ? 1.888   -5.918  18.433  1.00 89.37  ? 118 LYS C CG   1 
ATOM   10280 C CD   . LYS C 1 118 ? 0.795   -6.901  17.995  1.00 92.13  ? 118 LYS C CD   1 
ATOM   10281 C CE   . LYS C 1 118 ? -0.587  -6.250  17.946  1.00 95.91  ? 118 LYS C CE   1 
ATOM   10282 N NZ   . LYS C 1 118 ? -0.924  -5.704  16.590  1.00 95.61  ? 118 LYS C NZ   1 
ATOM   10283 H H    . LYS C 1 118 ? 2.073   -3.167  21.176  1.00 100.74 ? 118 LYS C H    1 
ATOM   10284 H HA   . LYS C 1 118 ? 3.098   -5.684  21.089  1.00 101.61 ? 118 LYS C HA   1 
ATOM   10285 H HB2  . LYS C 1 118 ? 1.047   -5.921  20.284  1.00 104.30 ? 118 LYS C HB2  1 
ATOM   10286 H HB3  . LYS C 1 118 ? 1.053   -4.483  19.606  1.00 104.30 ? 118 LYS C HB3  1 
ATOM   10287 H HG2  . LYS C 1 118 ? 1.959   -5.224  17.760  1.00 107.24 ? 118 LYS C HG2  1 
ATOM   10288 H HG3  . LYS C 1 118 ? 2.725   -6.405  18.497  1.00 107.24 ? 118 LYS C HG3  1 
ATOM   10289 H HD2  . LYS C 1 118 ? 1.003   -7.233  17.107  1.00 110.56 ? 118 LYS C HD2  1 
ATOM   10290 H HD3  . LYS C 1 118 ? 0.759   -7.638  18.624  1.00 110.56 ? 118 LYS C HD3  1 
ATOM   10291 H HE2  . LYS C 1 118 ? -1.256  -6.913  18.177  1.00 115.09 ? 118 LYS C HE2  1 
ATOM   10292 H HE3  . LYS C 1 118 ? -0.613  -5.516  18.579  1.00 115.09 ? 118 LYS C HE3  1 
ATOM   10293 H HZ1  . LYS C 1 118 ? -1.731  -5.328  16.605  1.00 114.73 ? 118 LYS C HZ1  1 
ATOM   10294 H HZ2  . LYS C 1 118 ? -0.324  -5.091  16.350  1.00 114.73 ? 118 LYS C HZ2  1 
ATOM   10295 H HZ3  . LYS C 1 118 ? -0.923  -6.360  15.988  1.00 114.73 ? 118 LYS C HZ3  1 
ATOM   10296 N N    . ILE C 1 119 ? 4.899   -5.345  19.472  1.00 83.81  ? 119 ILE C N    1 
ATOM   10297 C CA   . ILE C 1 119 ? 6.127   -5.027  18.754  1.00 80.31  ? 119 ILE C CA   1 
ATOM   10298 C C    . ILE C 1 119 ? 6.489   -6.200  17.856  1.00 85.49  ? 119 ILE C C    1 
ATOM   10299 O O    . ILE C 1 119 ? 6.201   -7.357  18.171  1.00 86.97  ? 119 ILE C O    1 
ATOM   10300 C CB   . ILE C 1 119 ? 7.285   -4.706  19.735  1.00 83.32  ? 119 ILE C CB   1 
ATOM   10301 C CG1  . ILE C 1 119 ? 8.382   -3.910  19.026  1.00 81.77  ? 119 ILE C CG1  1 
ATOM   10302 C CG2  . ILE C 1 119 ? 7.837   -5.995  20.364  1.00 83.74  ? 119 ILE C CG2  1 
ATOM   10303 C CD1  . ILE C 1 119 ? 9.658   -3.759  19.840  1.00 81.37  ? 119 ILE C CD1  1 
ATOM   10304 H H    . ILE C 1 119 ? 4.860   -6.162  19.737  1.00 100.58 ? 119 ILE C H    1 
ATOM   10305 H HA   . ILE C 1 119 ? 5.979   -4.254  18.186  1.00 96.37  ? 119 ILE C HA   1 
ATOM   10306 H HB   . ILE C 1 119 ? 6.936   -4.155  20.454  1.00 99.98  ? 119 ILE C HB   1 
ATOM   10307 H HG12 . ILE C 1 119 ? 8.611   -4.363  18.200  1.00 98.12  ? 119 ILE C HG12 1 
ATOM   10308 H HG13 . ILE C 1 119 ? 8.047   -3.020  18.835  1.00 98.12  ? 119 ILE C HG13 1 
ATOM   10309 H HG21 . ILE C 1 119 ? 8.491   -5.760  21.041  1.00 100.49 ? 119 ILE C HG21 1 
ATOM   10310 H HG22 . ILE C 1 119 ? 7.106   -6.488  20.767  1.00 100.49 ? 119 ILE C HG22 1 
ATOM   10311 H HG23 . ILE C 1 119 ? 8.256   -6.530  19.671  1.00 100.49 ? 119 ILE C HG23 1 
ATOM   10312 H HD11 . ILE C 1 119 ? 10.260  -3.157  19.375  1.00 97.64  ? 119 ILE C HD11 1 
ATOM   10313 H HD12 . ILE C 1 119 ? 9.436   -3.396  20.712  1.00 97.64  ? 119 ILE C HD12 1 
ATOM   10314 H HD13 . ILE C 1 119 ? 10.073  -4.630  19.941  1.00 97.64  ? 119 ILE C HD13 1 
ATOM   10315 N N    . LYS C 1 120 ? 7.127   -5.892  16.726  1.00 87.58  ? 120 LYS C N    1 
ATOM   10316 C CA   . LYS C 1 120 ? 7.632   -6.925  15.830  1.00 85.01  ? 120 LYS C CA   1 
ATOM   10317 C C    . LYS C 1 120 ? 8.982   -7.430  16.328  1.00 83.02  ? 120 LYS C C    1 
ATOM   10318 O O    . LYS C 1 120 ? 9.882   -6.637  16.620  1.00 81.34  ? 120 LYS C O    1 
ATOM   10319 C CB   . LYS C 1 120 ? 7.768   -6.385  14.404  1.00 88.26  ? 120 LYS C CB   1 
ATOM   10320 C CG   . LYS C 1 120 ? 8.270   -7.415  13.394  1.00 86.51  ? 120 LYS C CG   1 
ATOM   10321 C CD   . LYS C 1 120 ? 8.147   -6.912  11.966  1.00 89.92  ? 120 LYS C CD   1 
ATOM   10322 C CE   . LYS C 1 120 ? 6.704   -6.573  11.613  1.00 95.28  ? 120 LYS C CE   1 
ATOM   10323 N NZ   . LYS C 1 120 ? 6.427   -6.681  10.151  1.00 90.52  ? 120 LYS C NZ   1 
ATOM   10324 H H    . LYS C 1 120 ? 7.279   -5.089  16.457  1.00 105.10 ? 120 LYS C H    1 
ATOM   10325 H HA   . LYS C 1 120 ? 7.007   -7.667  15.814  1.00 102.02 ? 120 LYS C HA   1 
ATOM   10326 H HB2  . LYS C 1 120 ? 6.899   -6.077  14.104  1.00 105.91 ? 120 LYS C HB2  1 
ATOM   10327 H HB3  . LYS C 1 120 ? 8.398   -5.647  14.410  1.00 105.91 ? 120 LYS C HB3  1 
ATOM   10328 H HG2  . LYS C 1 120 ? 9.205   -7.606  13.569  1.00 103.82 ? 120 LYS C HG2  1 
ATOM   10329 H HG3  . LYS C 1 120 ? 7.744   -8.226  13.476  1.00 103.82 ? 120 LYS C HG3  1 
ATOM   10330 H HD2  . LYS C 1 120 ? 8.683   -6.110  11.861  1.00 107.91 ? 120 LYS C HD2  1 
ATOM   10331 H HD3  . LYS C 1 120 ? 8.457   -7.599  11.356  1.00 107.91 ? 120 LYS C HD3  1 
ATOM   10332 H HE2  . LYS C 1 120 ? 6.113   -7.186  12.077  1.00 114.34 ? 120 LYS C HE2  1 
ATOM   10333 H HE3  . LYS C 1 120 ? 6.518   -5.661  11.887  1.00 114.34 ? 120 LYS C HE3  1 
ATOM   10334 H HZ1  . LYS C 1 120 ? 6.324   -5.870  9.800   1.00 108.63 ? 120 LYS C HZ1  1 
ATOM   10335 H HZ2  . LYS C 1 120 ? 7.104   -7.089  9.742   1.00 108.63 ? 120 LYS C HZ2  1 
ATOM   10336 H HZ3  . LYS C 1 120 ? 5.683   -7.151  10.016  1.00 108.63 ? 120 LYS C HZ3  1 
ATOM   10337 N N    . MET C 1 121 ? 9.127   -8.761  16.418  1.00 81.58  ? 121 MET C N    1 
ATOM   10338 C CA   . MET C 1 121 ? 10.372  -9.312  16.933  1.00 82.61  ? 121 MET C CA   1 
ATOM   10339 C C    . MET C 1 121 ? 11.245  -9.837  15.798  1.00 83.00  ? 121 MET C C    1 
ATOM   10340 O O    . MET C 1 121 ? 10.733  -10.250 14.750  1.00 86.04  ? 121 MET C O    1 
ATOM   10341 C CB   . MET C 1 121 ? 10.104  -10.457 17.914  1.00 83.48  ? 121 MET C CB   1 
ATOM   10342 C CG   . MET C 1 121 ? 9.398   -10.070 19.213  1.00 86.15  ? 121 MET C CG   1 
ATOM   10343 S SD   . MET C 1 121 ? 10.177  -8.828  20.273  1.00 86.60  ? 121 MET C SD   1 
ATOM   10344 C CE   . MET C 1 121 ? 11.878  -9.380  20.282  1.00 80.70  ? 121 MET C CE   1 
ATOM   10345 H H    . MET C 1 121 ? 8.534   -9.342  16.192  1.00 97.90  ? 121 MET C H    1 
ATOM   10346 H HA   . MET C 1 121 ? 10.846  -8.613  17.410  1.00 99.13  ? 121 MET C HA   1 
ATOM   10347 H HB2  . MET C 1 121 ? 9.546   -11.113 17.468  1.00 100.17 ? 121 MET C HB2  1 
ATOM   10348 H HB3  . MET C 1 121 ? 10.955  -10.854 18.156  1.00 100.17 ? 121 MET C HB3  1 
ATOM   10349 H HG2  . MET C 1 121 ? 8.522   -9.724  18.981  1.00 103.38 ? 121 MET C HG2  1 
ATOM   10350 H HG3  . MET C 1 121 ? 9.307   -10.873 19.749  1.00 103.38 ? 121 MET C HG3  1 
ATOM   10351 H HE1  . MET C 1 121 ? 12.404  -8.773  20.826  1.00 96.84  ? 121 MET C HE1  1 
ATOM   10352 H HE2  . MET C 1 121 ? 11.917  -10.275 20.652  1.00 96.84  ? 121 MET C HE2  1 
ATOM   10353 H HE3  . MET C 1 121 ? 12.213  -9.383  19.372  1.00 96.84  ? 121 MET C HE3  1 
ATOM   10354 N N    . PRO C 1 122 ? 12.568  -9.818  15.968  1.00 82.02  ? 122 PRO C N    1 
ATOM   10355 C CA   . PRO C 1 122 ? 13.445  -10.476 14.990  1.00 85.43  ? 122 PRO C CA   1 
ATOM   10356 C C    . PRO C 1 122 ? 12.996  -11.894 14.659  1.00 89.49  ? 122 PRO C C    1 
ATOM   10357 O O    . PRO C 1 122 ? 12.501  -12.631 15.515  1.00 89.21  ? 122 PRO C O    1 
ATOM   10358 C CB   . PRO C 1 122 ? 14.815  -10.467 15.686  1.00 79.67  ? 122 PRO C CB   1 
ATOM   10359 C CG   . PRO C 1 122 ? 14.561  -9.932  17.101  1.00 79.65  ? 122 PRO C CG   1 
ATOM   10360 C CD   . PRO C 1 122 ? 13.363  -9.045  16.935  1.00 82.45  ? 122 PRO C CD   1 
ATOM   10361 H HA   . PRO C 1 122 ? 13.476  -9.956  14.172  1.00 102.52 ? 122 PRO C HA   1 
ATOM   10362 H HB2  . PRO C 1 122 ? 15.172  -11.369 15.717  1.00 95.61  ? 122 PRO C HB2  1 
ATOM   10363 H HB3  . PRO C 1 122 ? 15.423  -9.886  15.202  1.00 95.61  ? 122 PRO C HB3  1 
ATOM   10364 H HG2  . PRO C 1 122 ? 14.374  -10.665 17.708  1.00 95.58  ? 122 PRO C HG2  1 
ATOM   10365 H HG3  . PRO C 1 122 ? 15.330  -9.430  17.413  1.00 95.58  ? 122 PRO C HG3  1 
ATOM   10366 H HD2  . PRO C 1 122 ? 12.888  -8.932  17.773  1.00 98.94  ? 122 PRO C HD2  1 
ATOM   10367 H HD3  . PRO C 1 122 ? 13.612  -8.179  16.575  1.00 98.94  ? 122 PRO C HD3  1 
ATOM   10368 N N    . LYS C 1 123 ? 13.180  -12.271 13.400  1.00 84.50  ? 123 LYS C N    1 
ATOM   10369 C CA   . LYS C 1 123 ? 12.890  -13.622 12.956  1.00 90.75  ? 123 LYS C CA   1 
ATOM   10370 C C    . LYS C 1 123 ? 13.991  -14.571 13.415  1.00 91.15  ? 123 LYS C C    1 
ATOM   10371 O O    . LYS C 1 123 ? 15.114  -14.160 13.731  1.00 85.91  ? 123 LYS C O    1 
ATOM   10372 C CB   . LYS C 1 123 ? 12.759  -13.664 11.434  1.00 86.85  ? 123 LYS C CB   1 
ATOM   10373 C CG   . LYS C 1 123 ? 14.098  -13.715 10.712  1.00 89.84  ? 123 LYS C CG   1 
ATOM   10374 C CD   . LYS C 1 123 ? 14.068  -13.045 9.329   1.00 94.17  ? 123 LYS C CD   1 
ATOM   10375 C CE   . LYS C 1 123 ? 12.707  -13.135 8.647   1.00 93.77  ? 123 LYS C CE   1 
ATOM   10376 N NZ   . LYS C 1 123 ? 12.821  -12.995 7.163   1.00 97.84  ? 123 LYS C NZ   1 
ATOM   10377 H H    . LYS C 1 123 ? 13.476  -11.756 12.778  1.00 101.41 ? 123 LYS C H    1 
ATOM   10378 H HA   . LYS C 1 123 ? 12.050  -13.922 13.338  1.00 108.90 ? 123 LYS C HA   1 
ATOM   10379 H HB2  . LYS C 1 123 ? 12.256  -14.455 11.185  1.00 104.22 ? 123 LYS C HB2  1 
ATOM   10380 H HB3  . LYS C 1 123 ? 12.292  -12.867 11.139  1.00 104.22 ? 123 LYS C HB3  1 
ATOM   10381 H HG2  . LYS C 1 123 ? 14.763  -13.258 11.250  1.00 107.81 ? 123 LYS C HG2  1 
ATOM   10382 H HG3  . LYS C 1 123 ? 14.353  -14.643 10.588  1.00 107.81 ? 123 LYS C HG3  1 
ATOM   10383 H HD2  . LYS C 1 123 ? 14.289  -12.105 9.430   1.00 113.00 ? 123 LYS C HD2  1 
ATOM   10384 H HD3  . LYS C 1 123 ? 14.718  -13.479 8.755   1.00 113.00 ? 123 LYS C HD3  1 
ATOM   10385 H HE2  . LYS C 1 123 ? 12.308  -13.997 8.842   1.00 112.52 ? 123 LYS C HE2  1 
ATOM   10386 H HE3  . LYS C 1 123 ? 12.136  -12.423 8.977   1.00 112.52 ? 123 LYS C HE3  1 
ATOM   10387 H HZ1  . LYS C 1 123 ? 12.014  -13.034 6.791   1.00 117.41 ? 123 LYS C HZ1  1 
ATOM   10388 H HZ2  . LYS C 1 123 ? 13.196  -12.214 6.959   1.00 117.41 ? 123 LYS C HZ2  1 
ATOM   10389 H HZ3  . LYS C 1 123 ? 13.324  -13.652 6.834   1.00 117.41 ? 123 LYS C HZ3  1 
ATOM   10390 N N    . PHE C 1 124 ? 13.660  -15.860 13.447  1.00 91.56  ? 124 PHE C N    1 
ATOM   10391 C CA   . PHE C 1 124 ? 14.639  -16.866 13.827  1.00 95.82  ? 124 PHE C CA   1 
ATOM   10392 C C    . PHE C 1 124 ? 15.566  -17.165 12.657  1.00 95.93  ? 124 PHE C C    1 
ATOM   10393 O O    . PHE C 1 124 ? 15.192  -17.032 11.491  1.00 97.55  ? 124 PHE C O    1 
ATOM   10394 C CB   . PHE C 1 124 ? 13.962  -18.158 14.307  1.00 98.41  ? 124 PHE C CB   1 
ATOM   10395 C CG   . PHE C 1 124 ? 13.095  -18.827 13.276  1.00 96.95  ? 124 PHE C CG   1 
ATOM   10396 C CD1  . PHE C 1 124 ? 13.643  -19.650 12.305  1.00 97.74  ? 124 PHE C CD1  1 
ATOM   10397 C CD2  . PHE C 1 124 ? 11.722  -18.654 13.299  1.00 100.24 ? 124 PHE C CD2  1 
ATOM   10398 C CE1  . PHE C 1 124 ? 12.837  -20.269 11.366  1.00 97.72  ? 124 PHE C CE1  1 
ATOM   10399 C CE2  . PHE C 1 124 ? 10.913  -19.273 12.363  1.00 103.55 ? 124 PHE C CE2  1 
ATOM   10400 C CZ   . PHE C 1 124 ? 11.469  -20.080 11.400  1.00 103.84 ? 124 PHE C CZ   1 
ATOM   10401 H H    . PHE C 1 124 ? 12.882  -16.171 13.254  1.00 109.87 ? 124 PHE C H    1 
ATOM   10402 H HA   . PHE C 1 124 ? 15.170  -16.531 14.566  1.00 114.99 ? 124 PHE C HA   1 
ATOM   10403 H HB2  . PHE C 1 124 ? 14.650  -18.790 14.566  1.00 118.10 ? 124 PHE C HB2  1 
ATOM   10404 H HB3  . PHE C 1 124 ? 13.400  -17.947 15.069  1.00 118.10 ? 124 PHE C HB3  1 
ATOM   10405 H HD1  . PHE C 1 124 ? 14.563  -19.787 12.284  1.00 120.28 ? 124 PHE C HD1  1 
ATOM   10406 H HD2  . PHE C 1 124 ? 11.338  -18.114 13.952  1.00 117.28 ? 124 PHE C HD2  1 
ATOM   10407 H HE1  . PHE C 1 124 ? 13.216  -20.812 10.713  1.00 124.27 ? 124 PHE C HE1  1 
ATOM   10408 H HE2  . PHE C 1 124 ? 9.992   -19.143 12.385  1.00 117.26 ? 124 PHE C HE2  1 
ATOM   10409 H HZ   . PHE C 1 124 ? 10.925  -20.498 10.772  1.00 124.61 ? 124 PHE C HZ   1 
ATOM   10410 N N    . LEU C 1 125 ? 16.791  -17.561 12.989  1.00 100.05 ? 125 LEU C N    1 
ATOM   10411 C CA   . LEU C 1 125 ? 17.768  -17.980 11.993  1.00 100.03 ? 125 LEU C CA   1 
ATOM   10412 C C    . LEU C 1 125 ? 17.770  -19.485 11.772  1.00 102.42 ? 125 LEU C C    1 
ATOM   10413 O O    . LEU C 1 125 ? 18.169  -19.939 10.692  1.00 101.75 ? 125 LEU C O    1 
ATOM   10414 C CB   . LEU C 1 125 ? 19.164  -17.514 12.401  1.00 99.45  ? 125 LEU C CB   1 
ATOM   10415 C CG   . LEU C 1 125 ? 19.231  -16.112 13.008  1.00 104.26 ? 125 LEU C CG   1 
ATOM   10416 C CD1  . LEU C 1 125 ? 20.685  -15.703 13.242  1.00 106.69 ? 125 LEU C CD1  1 
ATOM   10417 C CD2  . LEU C 1 125 ? 18.521  -15.090 12.128  1.00 102.54 ? 125 LEU C CD2  1 
ATOM   10418 H H    . LEU C 1 125 ? 17.084  -17.597 13.796  1.00 120.06 ? 125 LEU C H    1 
ATOM   10419 H HA   . LEU C 1 125 ? 17.558  -17.560 11.144  1.00 120.04 ? 125 LEU C HA   1 
ATOM   10420 H HB2  . LEU C 1 125 ? 19.512  -18.133 13.062  1.00 119.33 ? 125 LEU C HB2  1 
ATOM   10421 H HB3  . LEU C 1 125 ? 19.729  -17.517 11.613  1.00 119.33 ? 125 LEU C HB3  1 
ATOM   10422 H HG   . LEU C 1 125 ? 18.774  -16.124 13.863  1.00 125.11 ? 125 LEU C HG   1 
ATOM   10423 H HD11 . LEU C 1 125 ? 20.706  -14.802 13.601  1.00 128.02 ? 125 LEU C HD11 1 
ATOM   10424 H HD12 . LEU C 1 125 ? 21.089  -16.320 13.871  1.00 128.02 ? 125 LEU C HD12 1 
ATOM   10425 H HD13 . LEU C 1 125 ? 21.161  -15.733 12.397  1.00 128.02 ? 125 LEU C HD13 1 
ATOM   10426 H HD21 . LEU C 1 125 ? 18.679  -14.202 12.484  1.00 123.05 ? 125 LEU C HD21 1 
ATOM   10427 H HD22 . LEU C 1 125 ? 18.872  -15.151 11.226  1.00 123.05 ? 125 LEU C HD22 1 
ATOM   10428 H HD23 . LEU C 1 125 ? 17.570  -15.281 12.126  1.00 123.05 ? 125 LEU C HD23 1 
ATOM   10429 N N    . SER C 1 126 ? 17.337  -20.262 12.765  1.00 104.30 ? 126 SER C N    1 
ATOM   10430 C CA   . SER C 1 126 ? 17.215  -21.708 12.638  1.00 104.38 ? 126 SER C CA   1 
ATOM   10431 C C    . SER C 1 126 ? 16.077  -22.187 13.528  1.00 101.26 ? 126 SER C C    1 
ATOM   10432 O O    . SER C 1 126 ? 15.795  -21.595 14.572  1.00 103.69 ? 126 SER C O    1 
ATOM   10433 C CB   . SER C 1 126 ? 18.515  -22.434 13.030  1.00 104.51 ? 126 SER C CB   1 
ATOM   10434 O OG   . SER C 1 126 ? 19.660  -21.732 12.581  1.00 108.07 ? 126 SER C OG   1 
ATOM   10435 H H    . SER C 1 126 ? 17.104  -19.966 13.538  1.00 125.15 ? 126 SER C H    1 
ATOM   10436 H HA   . SER C 1 126 ? 17.009  -21.927 11.716  1.00 125.25 ? 126 SER C HA   1 
ATOM   10437 H HB2  . SER C 1 126 ? 18.552  -22.508 13.997  1.00 125.42 ? 126 SER C HB2  1 
ATOM   10438 H HB3  . SER C 1 126 ? 18.512  -23.317 12.630  1.00 125.42 ? 126 SER C HB3  1 
ATOM   10439 H HG   . SER C 1 126 ? 19.709  -20.987 12.966  1.00 129.69 ? 126 SER C HG   1 
ATOM   10440 N N    . LEU C 1 127 ? 15.418  -23.258 13.098  1.00 101.23 ? 127 LEU C N    1 
ATOM   10441 C CA   . LEU C 1 127 ? 14.384  -23.924 13.884  1.00 103.40 ? 127 LEU C CA   1 
ATOM   10442 C C    . LEU C 1 127 ? 14.542  -25.419 13.658  1.00 104.43 ? 127 LEU C C    1 
ATOM   10443 O O    . LEU C 1 127 ? 14.559  -25.875 12.511  1.00 103.80 ? 127 LEU C O    1 
ATOM   10444 C CB   . LEU C 1 127 ? 12.976  -23.457 13.482  1.00 105.88 ? 127 LEU C CB   1 
ATOM   10445 C CG   . LEU C 1 127 ? 11.777  -24.121 14.164  1.00 108.17 ? 127 LEU C CG   1 
ATOM   10446 C CD1  . LEU C 1 127 ? 10.571  -23.172 14.160  1.00 107.35 ? 127 LEU C CD1  1 
ATOM   10447 C CD2  . LEU C 1 127 ? 11.396  -25.430 13.499  1.00 106.91 ? 127 LEU C CD2  1 
ATOM   10448 H H    . LEU C 1 127 ? 15.556  -23.629 12.335  1.00 121.48 ? 127 LEU C H    1 
ATOM   10449 H HA   . LEU C 1 127 ? 14.489  -23.727 14.828  1.00 124.08 ? 127 LEU C HA   1 
ATOM   10450 H HB2  . LEU C 1 127 ? 12.914  -22.508 13.673  1.00 127.05 ? 127 LEU C HB2  1 
ATOM   10451 H HB3  . LEU C 1 127 ? 12.875  -23.612 12.530  1.00 127.05 ? 127 LEU C HB3  1 
ATOM   10452 H HG   . LEU C 1 127 ? 12.030  -24.319 15.080  1.00 129.81 ? 127 LEU C HG   1 
ATOM   10453 H HD11 . LEU C 1 127 ? 9.835   -23.594 14.629  1.00 128.82 ? 127 LEU C HD11 1 
ATOM   10454 H HD12 . LEU C 1 127 ? 10.817  -22.346 14.606  1.00 128.82 ? 127 LEU C HD12 1 
ATOM   10455 H HD13 . LEU C 1 127 ? 10.317  -22.989 13.242  1.00 128.82 ? 127 LEU C HD13 1 
ATOM   10456 H HD21 . LEU C 1 127 ? 10.612  -25.792 13.941  1.00 128.30 ? 127 LEU C HD21 1 
ATOM   10457 H HD22 . LEU C 1 127 ? 11.201  -25.264 12.564  1.00 128.30 ? 127 LEU C HD22 1 
ATOM   10458 H HD23 . LEU C 1 127 ? 12.136  -26.051 13.578  1.00 128.30 ? 127 LEU C HD23 1 
ATOM   10459 N N    . GLU C 1 128 ? 14.647  -26.178 14.743  1.00 107.68 ? 128 GLU C N    1 
ATOM   10460 C CA   . GLU C 1 128 ? 14.991  -27.591 14.648  1.00 108.78 ? 128 GLU C CA   1 
ATOM   10461 C C    . GLU C 1 128 ? 14.565  -28.286 15.931  1.00 112.12 ? 128 GLU C C    1 
ATOM   10462 O O    . GLU C 1 128 ? 14.459  -27.664 16.991  1.00 113.02 ? 128 GLU C O    1 
ATOM   10463 C CB   . GLU C 1 128 ? 16.493  -27.786 14.403  1.00 106.50 ? 128 GLU C CB   1 
ATOM   10464 C CG   . GLU C 1 128 ? 17.357  -26.730 15.088  1.00 110.10 ? 128 GLU C CG   1 
ATOM   10465 C CD   . GLU C 1 128 ? 18.794  -26.732 14.601  1.00 110.46 ? 128 GLU C CD   1 
ATOM   10466 O OE1  . GLU C 1 128 ? 19.251  -27.788 14.104  1.00 108.41 ? 128 GLU C OE1  1 
ATOM   10467 O OE2  . GLU C 1 128 ? 19.460  -25.675 14.716  1.00 110.13 ? 128 GLU C OE2  1 
ATOM   10468 H H    . GLU C 1 128 ? 14.523  -25.898 15.547  1.00 129.21 ? 128 GLU C H    1 
ATOM   10469 H HA   . GLU C 1 128 ? 14.506  -27.992 13.909  1.00 130.54 ? 128 GLU C HA   1 
ATOM   10470 H HB2  . GLU C 1 128 ? 16.756  -28.655 14.746  1.00 127.80 ? 128 GLU C HB2  1 
ATOM   10471 H HB3  . GLU C 1 128 ? 16.664  -27.740 13.450  1.00 127.80 ? 128 GLU C HB3  1 
ATOM   10472 H HG2  . GLU C 1 128 ? 16.982  -25.853 14.910  1.00 132.12 ? 128 GLU C HG2  1 
ATOM   10473 H HG3  . GLU C 1 128 ? 17.364  -26.900 16.043  1.00 132.12 ? 128 GLU C HG3  1 
ATOM   10474 N N    . GLU C 1 129 ? 14.330  -29.594 15.825  1.00 115.67 ? 129 GLU C N    1 
ATOM   10475 C CA   . GLU C 1 129 ? 14.031  -30.433 16.981  1.00 121.18 ? 129 GLU C CA   1 
ATOM   10476 C C    . GLU C 1 129 ? 15.275  -31.255 17.311  1.00 128.73 ? 129 GLU C C    1 
ATOM   10477 O O    . GLU C 1 129 ? 15.688  -32.113 16.526  1.00 128.18 ? 129 GLU C O    1 
ATOM   10478 C CB   . GLU C 1 129 ? 12.828  -31.338 16.724  1.00 116.98 ? 129 GLU C CB   1 
ATOM   10479 C CG   . GLU C 1 129 ? 12.296  -32.004 17.992  1.00 126.89 ? 129 GLU C CG   1 
ATOM   10480 C CD   . GLU C 1 129 ? 10.785  -31.926 18.117  1.00 123.70 ? 129 GLU C CD   1 
ATOM   10481 O OE1  . GLU C 1 129 ? 10.093  -32.637 17.357  1.00 124.25 ? 129 GLU C OE1  1 
ATOM   10482 O OE2  . GLU C 1 129 ? 10.293  -31.165 18.982  1.00 125.69 ? 129 GLU C OE2  1 
ATOM   10483 H H    . GLU C 1 129 ? 14.338  -30.024 15.080  1.00 138.80 ? 129 GLU C H    1 
ATOM   10484 H HA   . GLU C 1 129 ? 13.819  -29.864 17.738  1.00 145.41 ? 129 GLU C HA   1 
ATOM   10485 H HB2  . GLU C 1 129 ? 12.111  -30.807 16.342  1.00 140.38 ? 129 GLU C HB2  1 
ATOM   10486 H HB3  . GLU C 1 129 ? 13.088  -32.039 16.105  1.00 140.38 ? 129 GLU C HB3  1 
ATOM   10487 H HG2  . GLU C 1 129 ? 12.547  -32.941 17.985  1.00 152.27 ? 129 GLU C HG2  1 
ATOM   10488 H HG3  . GLU C 1 129 ? 12.682  -31.563 18.765  1.00 152.27 ? 129 GLU C HG3  1 
ATOM   10489 N N    . ILE C 1 130 ? 15.875  -30.972 18.466  1.00 145.41 ? 130 ILE C N    1 
ATOM   10490 C CA   . ILE C 1 130 ? 16.999  -31.734 18.982  1.00 143.50 ? 130 ILE C CA   1 
ATOM   10491 C C    . ILE C 1 130 ? 16.461  -32.816 19.908  1.00 146.92 ? 130 ILE C C    1 
ATOM   10492 O O    . ILE C 1 130 ? 15.366  -32.717 20.452  1.00 149.69 ? 130 ILE C O    1 
ATOM   10493 C CB   . ILE C 1 130 ? 17.977  -30.788 19.711  1.00 143.44 ? 130 ILE C CB   1 
ATOM   10494 C CG1  . ILE C 1 130 ? 19.130  -30.353 18.794  1.00 145.96 ? 130 ILE C CG1  1 
ATOM   10495 C CG2  . ILE C 1 130 ? 18.569  -31.426 20.950  1.00 146.63 ? 130 ILE C CG2  1 
ATOM   10496 C CD1  . ILE C 1 130 ? 18.690  -29.823 17.455  1.00 145.74 ? 130 ILE C CD1  1 
ATOM   10497 H H    . ILE C 1 130 ? 15.641  -30.323 18.980  1.00 174.49 ? 130 ILE C H    1 
ATOM   10498 H HA   . ILE C 1 130 ? 17.476  -32.178 18.264  1.00 172.19 ? 130 ILE C HA   1 
ATOM   10499 H HB   . ILE C 1 130 ? 17.450  -30.014 19.968  1.00 172.13 ? 130 ILE C HB   1 
ATOM   10500 H HG12 . ILE C 1 130 ? 19.631  -29.650 19.238  1.00 175.15 ? 130 ILE C HG12 1 
ATOM   10501 H HG13 . ILE C 1 130 ? 19.704  -31.118 18.633  1.00 175.15 ? 130 ILE C HG13 1 
ATOM   10502 H HG21 . ILE C 1 130 ? 19.205  -30.811 21.349  1.00 175.96 ? 130 ILE C HG21 1 
ATOM   10503 H HG22 . ILE C 1 130 ? 17.856  -31.618 21.579  1.00 175.96 ? 130 ILE C HG22 1 
ATOM   10504 H HG23 . ILE C 1 130 ? 19.018  -32.248 20.698  1.00 175.96 ? 130 ILE C HG23 1 
ATOM   10505 H HD11 . ILE C 1 130 ? 19.391  -29.259 17.093  1.00 174.90 ? 130 ILE C HD11 1 
ATOM   10506 H HD12 . ILE C 1 130 ? 18.526  -30.570 16.858  1.00 174.90 ? 130 ILE C HD12 1 
ATOM   10507 H HD13 . ILE C 1 130 ? 17.876  -29.308 17.571  1.00 174.90 ? 130 ILE C HD13 1 
ATOM   10508 N N    . ASN C 1 131 ? 17.242  -33.890 20.072  1.00 147.45 ? 131 ASN C N    1 
ATOM   10509 C CA   . ASN C 1 131 ? 16.875  -35.016 20.947  1.00 147.64 ? 131 ASN C CA   1 
ATOM   10510 C C    . ASN C 1 131 ? 18.121  -35.414 21.738  1.00 147.35 ? 131 ASN C C    1 
ATOM   10511 O O    . ASN C 1 131 ? 18.920  -36.227 21.264  1.00 149.20 ? 131 ASN C O    1 
ATOM   10512 C CB   . ASN C 1 131 ? 16.325  -36.194 20.125  1.00 150.04 ? 131 ASN C CB   1 
ATOM   10513 C CG   . ASN C 1 131 ? 14.811  -36.209 20.060  1.00 150.08 ? 131 ASN C CG   1 
ATOM   10514 O OD1  . ASN C 1 131 ? 14.164  -37.094 20.617  1.00 153.74 ? 131 ASN C OD1  1 
ATOM   10515 N ND2  . ASN C 1 131 ? 14.237  -35.237 19.359  1.00 149.20 ? 131 ASN C ND2  1 
ATOM   10516 H H    . ASN C 1 131 ? 18.002  -33.993 19.682  1.00 176.94 ? 131 ASN C H    1 
ATOM   10517 H HA   . ASN C 1 131 ? 16.193  -34.726 21.573  1.00 177.16 ? 131 ASN C HA   1 
ATOM   10518 H HB2  . ASN C 1 131 ? 16.664  -36.132 19.219  1.00 180.05 ? 131 ASN C HB2  1 
ATOM   10519 H HB3  . ASN C 1 131 ? 16.616  -37.025 20.532  1.00 180.05 ? 131 ASN C HB3  1 
ATOM   10520 H HD21 . ASN C 1 131 ? 14.723  -34.641 18.972  1.00 179.04 ? 131 ASN C HD21 1 
ATOM   10521 H HD22 . ASN C 1 131 ? 13.381  -35.203 19.292  1.00 179.04 ? 131 ASN C HD22 1 
ATOM   10522 N N    . VAL C 1 132 ? 18.290  -34.831 22.939  1.00 149.29 ? 132 VAL C N    1 
ATOM   10523 C CA   . VAL C 1 132 ? 19.438  -35.142 23.783  1.00 150.19 ? 132 VAL C CA   1 
ATOM   10524 C C    . VAL C 1 132 ? 19.084  -36.300 24.702  1.00 150.70 ? 132 VAL C C    1 
ATOM   10525 O O    . VAL C 1 132 ? 17.958  -36.388 25.210  1.00 148.73 ? 132 VAL C O    1 
ATOM   10526 C CB   . VAL C 1 132 ? 19.889  -33.921 24.609  1.00 151.07 ? 132 VAL C CB   1 
ATOM   10527 C CG1  . VAL C 1 132 ? 20.027  -32.683 23.732  1.00 149.57 ? 132 VAL C CG1  1 
ATOM   10528 C CG2  . VAL C 1 132 ? 18.952  -33.684 25.794  1.00 148.15 ? 132 VAL C CG2  1 
ATOM   10529 H H    . VAL C 1 132 ? 17.750  -34.254 23.278  1.00 179.15 ? 132 VAL C H    1 
ATOM   10530 H HA   . VAL C 1 132 ? 20.171  -35.407 23.206  1.00 180.23 ? 132 VAL C HA   1 
ATOM   10531 H HB   . VAL C 1 132 ? 20.769  -34.104 24.974  1.00 181.29 ? 132 VAL C HB   1 
ATOM   10532 H HG11 . VAL C 1 132 ? 20.319  -31.939 24.281  1.00 179.49 ? 132 VAL C HG11 1 
ATOM   10533 H HG12 . VAL C 1 132 ? 20.682  -32.859 23.038  1.00 179.49 ? 132 VAL C HG12 1 
ATOM   10534 H HG13 . VAL C 1 132 ? 19.167  -32.483 23.332  1.00 179.49 ? 132 VAL C HG13 1 
ATOM   10535 H HG21 . VAL C 1 132 ? 19.077  -32.778 26.120  1.00 177.78 ? 132 VAL C HG21 1 
ATOM   10536 H HG22 . VAL C 1 132 ? 18.035  -33.806 25.502  1.00 177.78 ? 132 VAL C HG22 1 
ATOM   10537 H HG23 . VAL C 1 132 ? 19.163  -34.319 26.496  1.00 177.78 ? 132 VAL C HG23 1 
ATOM   10538 N N    . ASP C 1 133 ? 20.068  -37.178 24.938  1.00 154.63 ? 133 ASP C N    1 
ATOM   10539 C CA   . ASP C 1 133 ? 19.903  -38.373 25.763  1.00 152.17 ? 133 ASP C CA   1 
ATOM   10540 C C    . ASP C 1 133 ? 18.504  -38.954 25.609  1.00 153.20 ? 133 ASP C C    1 
ATOM   10541 O O    . ASP C 1 133 ? 18.193  -39.559 24.578  1.00 159.64 ? 133 ASP C O    1 
ATOM   10542 C CB   . ASP C 1 133 ? 20.216  -38.052 27.227  1.00 154.05 ? 133 ASP C CB   1 
ATOM   10543 C CG   . ASP C 1 133 ? 21.688  -37.734 27.449  1.00 157.60 ? 133 ASP C CG   1 
ATOM   10544 O OD1  . ASP C 1 133 ? 22.245  -36.905 26.698  1.00 155.31 ? 133 ASP C OD1  1 
ATOM   10545 O OD2  . ASP C 1 133 ? 22.288  -38.313 28.383  1.00 161.91 ? 133 ASP C OD2  1 
ATOM   10546 H H    . ASP C 1 133 ? 20.864  -37.098 24.620  1.00 185.55 ? 133 ASP C H    1 
ATOM   10547 H HA   . ASP C 1 133 ? 20.528  -39.055 25.472  1.00 182.60 ? 133 ASP C HA   1 
ATOM   10548 H HB2  . ASP C 1 133 ? 19.697  -37.280 27.500  1.00 184.86 ? 133 ASP C HB2  1 
ATOM   10549 H HB3  . ASP C 1 133 ? 19.987  -38.818 27.776  1.00 184.86 ? 133 ASP C HB3  1 
ATOM   10550 N N    . GLU C 1 134 ? 17.652  -38.768 26.615  1.00 145.99 ? 134 GLU C N    1 
ATOM   10551 C CA   . GLU C 1 134 ? 16.300  -39.316 26.582  1.00 144.39 ? 134 GLU C CA   1 
ATOM   10552 C C    . GLU C 1 134 ? 15.239  -38.316 26.145  1.00 141.81 ? 134 GLU C C    1 
ATOM   10553 O O    . GLU C 1 134 ? 14.147  -38.731 25.743  1.00 138.99 ? 134 GLU C O    1 
ATOM   10554 C CB   . GLU C 1 134 ? 15.921  -39.866 27.966  1.00 145.50 ? 134 GLU C CB   1 
ATOM   10555 C CG   . GLU C 1 134 ? 14.665  -40.718 27.973  1.00 148.14 ? 134 GLU C CG   1 
ATOM   10556 C CD   . GLU C 1 134 ? 14.681  -41.769 29.069  1.00 147.29 ? 134 GLU C CD   1 
ATOM   10557 O OE1  . GLU C 1 134 ? 14.384  -41.415 30.231  1.00 146.61 ? 134 GLU C OE1  1 
ATOM   10558 O OE2  . GLU C 1 134 ? 14.983  -42.945 28.767  1.00 145.71 ? 134 GLU C OE2  1 
ATOM   10559 H H    . GLU C 1 134 ? 17.835  -38.326 27.330  1.00 175.20 ? 134 GLU C H    1 
ATOM   10560 H HA   . GLU C 1 134 ? 16.285  -40.049 25.947  1.00 173.26 ? 134 GLU C HA   1 
ATOM   10561 H HB2  . GLU C 1 134 ? 16.651  -40.414 28.293  1.00 174.60 ? 134 GLU C HB2  1 
ATOM   10562 H HB3  . GLU C 1 134 ? 15.772  -39.118 28.567  1.00 174.60 ? 134 GLU C HB3  1 
ATOM   10563 H HG2  . GLU C 1 134 ? 13.894  -40.147 28.116  1.00 177.77 ? 134 GLU C HG2  1 
ATOM   10564 H HG3  . GLU C 1 134 ? 14.587  -41.174 27.121  1.00 177.77 ? 134 GLU C HG3  1 
ATOM   10565 N N    . TYR C 1 135 ? 15.537  -37.026 26.193  1.00 144.21 ? 135 TYR C N    1 
ATOM   10566 C CA   . TYR C 1 135 ? 14.549  -35.975 26.022  1.00 141.22 ? 135 TYR C CA   1 
ATOM   10567 C C    . TYR C 1 135 ? 14.683  -35.314 24.657  1.00 140.60 ? 135 TYR C C    1 
ATOM   10568 O O    . TYR C 1 135 ? 15.720  -35.409 23.993  1.00 142.24 ? 135 TYR C O    1 
ATOM   10569 C CB   . TYR C 1 135 ? 14.699  -34.937 27.142  1.00 137.21 ? 135 TYR C CB   1 
ATOM   10570 C CG   . TYR C 1 135 ? 14.690  -35.568 28.522  1.00 138.97 ? 135 TYR C CG   1 
ATOM   10571 C CD1  . TYR C 1 135 ? 13.538  -36.156 29.022  1.00 140.52 ? 135 TYR C CD1  1 
ATOM   10572 C CD2  . TYR C 1 135 ? 15.830  -35.579 29.319  1.00 140.55 ? 135 TYR C CD2  1 
ATOM   10573 C CE1  . TYR C 1 135 ? 13.514  -36.735 30.279  1.00 141.56 ? 135 TYR C CE1  1 
ATOM   10574 C CE2  . TYR C 1 135 ? 15.819  -36.155 30.581  1.00 137.99 ? 135 TYR C CE2  1 
ATOM   10575 C CZ   . TYR C 1 135 ? 14.659  -36.737 31.053  1.00 140.44 ? 135 TYR C CZ   1 
ATOM   10576 O OH   . TYR C 1 135 ? 14.637  -37.310 32.303  1.00 144.64 ? 135 TYR C OH   1 
ATOM   10577 H H    . TYR C 1 135 ? 16.331  -36.726 26.329  1.00 173.05 ? 135 TYR C H    1 
ATOM   10578 H HA   . TYR C 1 135 ? 13.656  -36.352 26.062  1.00 169.47 ? 135 TYR C HA   1 
ATOM   10579 H HB2  . TYR C 1 135 ? 15.541  -34.469 27.029  1.00 164.65 ? 135 TYR C HB2  1 
ATOM   10580 H HB3  . TYR C 1 135 ? 13.961  -34.309 27.093  1.00 164.65 ? 135 TYR C HB3  1 
ATOM   10581 H HD1  . TYR C 1 135 ? 12.767  -36.163 28.503  1.00 168.62 ? 135 TYR C HD1  1 
ATOM   10582 H HD2  . TYR C 1 135 ? 16.614  -35.193 29.001  1.00 168.66 ? 135 TYR C HD2  1 
ATOM   10583 H HE1  . TYR C 1 135 ? 12.732  -37.120 30.602  1.00 169.88 ? 135 TYR C HE1  1 
ATOM   10584 H HE2  . TYR C 1 135 ? 16.587  -36.148 31.105  1.00 165.59 ? 135 TYR C HE2  1 
ATOM   10585 H HH   . TYR C 1 135 ? 13.858  -37.562 32.490  1.00 173.57 ? 135 TYR C HH   1 
ATOM   10586 N N    . LYS C 1 136 ? 13.600  -34.661 24.227  1.00 140.98 ? 136 LYS C N    1 
ATOM   10587 C CA   . LYS C 1 136 ? 13.590  -33.860 23.010  1.00 140.85 ? 136 LYS C CA   1 
ATOM   10588 C C    . LYS C 1 136 ? 13.356  -32.395 23.367  1.00 136.68 ? 136 LYS C C    1 
ATOM   10589 O O    . LYS C 1 136 ? 12.790  -32.068 24.413  1.00 133.81 ? 136 LYS C O    1 
ATOM   10590 C CB   . LYS C 1 136 ? 12.526  -34.347 22.011  1.00 139.30 ? 136 LYS C CB   1 
ATOM   10591 C CG   . LYS C 1 136 ? 11.081  -34.218 22.474  1.00 137.38 ? 136 LYS C CG   1 
ATOM   10592 C CD   . LYS C 1 136 ? 10.059  -34.319 21.319  1.00 133.96 ? 136 LYS C CD   1 
ATOM   10593 C CE   . LYS C 1 136 ? 10.434  -35.357 20.260  1.00 135.30 ? 136 LYS C CE   1 
ATOM   10594 N NZ   . LYS C 1 136 ? 10.255  -36.761 20.726  1.00 144.55 ? 136 LYS C NZ   1 
ATOM   10595 H H    . LYS C 1 136 ? 12.843  -34.671 24.636  1.00 169.17 ? 136 LYS C H    1 
ATOM   10596 H HA   . LYS C 1 136 ? 14.451  -33.931 22.570  1.00 169.03 ? 136 LYS C HA   1 
ATOM   10597 H HB2  . LYS C 1 136 ? 12.614  -33.830 21.195  1.00 167.16 ? 136 LYS C HB2  1 
ATOM   10598 H HB3  . LYS C 1 136 ? 12.687  -35.286 21.827  1.00 167.16 ? 136 LYS C HB3  1 
ATOM   10599 H HG2  . LYS C 1 136 ? 10.888  -34.930 23.105  1.00 164.86 ? 136 LYS C HG2  1 
ATOM   10600 H HG3  . LYS C 1 136 ? 10.963  -33.355 22.901  1.00 164.86 ? 136 LYS C HG3  1 
ATOM   10601 H HD2  . LYS C 1 136 ? 9.196   -34.568 21.685  1.00 160.75 ? 136 LYS C HD2  1 
ATOM   10602 H HD3  . LYS C 1 136 ? 9.997   -33.457 20.879  1.00 160.75 ? 136 LYS C HD3  1 
ATOM   10603 H HE2  . LYS C 1 136 ? 9.872   -35.228 19.480  1.00 162.35 ? 136 LYS C HE2  1 
ATOM   10604 H HE3  . LYS C 1 136 ? 11.367  -35.239 20.020  1.00 162.35 ? 136 LYS C HE3  1 
ATOM   10605 H HZ1  . LYS C 1 136 ? 10.483  -37.328 20.079  1.00 173.46 ? 136 LYS C HZ1  1 
ATOM   10606 H HZ2  . LYS C 1 136 ? 10.767  -36.914 21.437  1.00 173.46 ? 136 LYS C HZ2  1 
ATOM   10607 H HZ3  . LYS C 1 136 ? 9.404   -36.903 20.947  1.00 173.46 ? 136 LYS C HZ3  1 
ATOM   10608 N N    . LEU C 1 137 ? 13.803  -31.513 22.477  1.00 136.51 ? 137 LEU C N    1 
ATOM   10609 C CA   . LEU C 1 137 ? 13.829  -30.082 22.755  1.00 135.77 ? 137 LEU C CA   1 
ATOM   10610 C C    . LEU C 1 137 ? 13.973  -29.341 21.434  1.00 132.22 ? 137 LEU C C    1 
ATOM   10611 O O    . LEU C 1 137 ? 14.798  -29.720 20.597  1.00 130.71 ? 137 LEU C O    1 
ATOM   10612 C CB   . LEU C 1 137 ? 14.977  -29.727 23.708  1.00 132.78 ? 137 LEU C CB   1 
ATOM   10613 C CG   . LEU C 1 137 ? 16.328  -30.293 23.272  1.00 141.24 ? 137 LEU C CG   1 
ATOM   10614 C CD1  . LEU C 1 137 ? 17.457  -29.374 23.718  1.00 138.97 ? 137 LEU C CD1  1 
ATOM   10615 C CD2  . LEU C 1 137 ? 16.542  -31.699 23.827  1.00 142.46 ? 137 LEU C CD2  1 
ATOM   10616 H H    . LEU C 1 137 ? 14.101  -31.721 21.697  1.00 163.81 ? 137 LEU C H    1 
ATOM   10617 H HA   . LEU C 1 137 ? 12.996  -29.809 23.172  1.00 162.92 ? 137 LEU C HA   1 
ATOM   10618 H HB2  . LEU C 1 137 ? 15.059  -28.762 23.752  1.00 159.33 ? 137 LEU C HB2  1 
ATOM   10619 H HB3  . LEU C 1 137 ? 14.774  -30.084 24.587  1.00 159.33 ? 137 LEU C HB3  1 
ATOM   10620 H HG   . LEU C 1 137 ? 16.341  -30.352 22.304  1.00 169.48 ? 137 LEU C HG   1 
ATOM   10621 H HD11 . LEU C 1 137 ? 18.303  -29.752 23.431  1.00 166.77 ? 137 LEU C HD11 1 
ATOM   10622 H HD12 . LEU C 1 137 ? 17.331  -28.501 23.314  1.00 166.77 ? 137 LEU C HD12 1 
ATOM   10623 H HD13 . LEU C 1 137 ? 17.439  -29.298 24.684  1.00 166.77 ? 137 LEU C HD13 1 
ATOM   10624 H HD21 . LEU C 1 137 ? 17.406  -32.027 23.533  1.00 170.96 ? 137 LEU C HD21 1 
ATOM   10625 H HD22 . LEU C 1 137 ? 16.514  -31.664 24.796  1.00 170.96 ? 137 LEU C HD22 1 
ATOM   10626 H HD23 . LEU C 1 137 ? 15.838  -32.280 23.497  1.00 170.96 ? 137 LEU C HD23 1 
ATOM   10627 N N    . GLY C 1 138 ? 13.163  -28.300 21.249  1.00 120.89 ? 138 GLY C N    1 
ATOM   10628 C CA   . GLY C 1 138 ? 13.122  -27.583 19.994  1.00 118.11 ? 138 GLY C CA   1 
ATOM   10629 C C    . GLY C 1 138 ? 13.996  -26.349 19.959  1.00 113.32 ? 138 GLY C C    1 
ATOM   10630 O O    . GLY C 1 138 ? 13.583  -25.275 20.411  1.00 117.15 ? 138 GLY C O    1 
ATOM   10631 H H    . GLY C 1 138 ? 12.625  -27.991 21.846  1.00 145.07 ? 138 GLY C H    1 
ATOM   10632 H HA2  . GLY C 1 138 ? 13.413  -28.176 19.284  1.00 141.73 ? 138 GLY C HA2  1 
ATOM   10633 H HA3  . GLY C 1 138 ? 12.208  -27.306 19.820  1.00 141.73 ? 138 GLY C HA3  1 
ATOM   10634 N N    . LEU C 1 139 ? 15.206  -26.487 19.419  1.00 113.75 ? 139 LEU C N    1 
ATOM   10635 C CA   . LEU C 1 139 ? 16.098  -25.346 19.274  1.00 107.96 ? 139 LEU C CA   1 
ATOM   10636 C C    . LEU C 1 139 ? 15.516  -24.334 18.295  1.00 106.84 ? 139 LEU C C    1 
ATOM   10637 O O    . LEU C 1 139 ? 15.136  -24.682 17.174  1.00 106.53 ? 139 LEU C O    1 
ATOM   10638 C CB   . LEU C 1 139 ? 17.468  -25.807 18.782  1.00 107.44 ? 139 LEU C CB   1 
ATOM   10639 C CG   . LEU C 1 139 ? 18.633  -25.580 19.744  1.00 113.99 ? 139 LEU C CG   1 
ATOM   10640 C CD1  . LEU C 1 139 ? 19.726  -26.617 19.486  1.00 117.96 ? 139 LEU C CD1  1 
ATOM   10641 C CD2  . LEU C 1 139 ? 19.176  -24.163 19.644  1.00 111.14 ? 139 LEU C CD2  1 
ATOM   10642 H H    . LEU C 1 139 ? 15.531  -27.229 19.130  1.00 136.50 ? 139 LEU C H    1 
ATOM   10643 H HA   . LEU C 1 139 ? 16.206  -24.919 20.138  1.00 129.55 ? 139 LEU C HA   1 
ATOM   10644 H HB2  . LEU C 1 139 ? 17.422  -26.760 18.605  1.00 128.93 ? 139 LEU C HB2  1 
ATOM   10645 H HB3  . LEU C 1 139 ? 17.673  -25.328 17.963  1.00 128.93 ? 139 LEU C HB3  1 
ATOM   10646 H HG   . LEU C 1 139 ? 18.318  -25.689 20.654  1.00 136.79 ? 139 LEU C HG   1 
ATOM   10647 H HD11 . LEU C 1 139 ? 20.593  -26.187 19.560  1.00 141.56 ? 139 LEU C HD11 1 
ATOM   10648 H HD12 . LEU C 1 139 ? 19.652  -27.325 20.145  1.00 141.56 ? 139 LEU C HD12 1 
ATOM   10649 H HD13 . LEU C 1 139 ? 19.613  -26.981 18.594  1.00 141.56 ? 139 LEU C HD13 1 
ATOM   10650 H HD21 . LEU C 1 139 ? 20.015  -24.111 20.129  1.00 133.38 ? 139 LEU C HD21 1 
ATOM   10651 H HD22 . LEU C 1 139 ? 19.320  -23.945 18.710  1.00 133.38 ? 139 LEU C HD22 1 
ATOM   10652 H HD23 . LEU C 1 139 ? 18.532  -23.550 20.032  1.00 133.38 ? 139 LEU C HD23 1 
ATOM   10653 N N    . VAL C 1 140 ? 15.448  -23.076 18.720  1.00 104.51 ? 140 VAL C N    1 
ATOM   10654 C CA   . VAL C 1 140 ? 15.094  -21.954 17.860  1.00 103.92 ? 140 VAL C CA   1 
ATOM   10655 C C    . VAL C 1 140 ? 16.233  -20.951 18.001  1.00 103.49 ? 140 VAL C C    1 
ATOM   10656 O O    . VAL C 1 140 ? 16.261  -20.178 18.965  1.00 104.56 ? 140 VAL C O    1 
ATOM   10657 C CB   . VAL C 1 140 ? 13.742  -21.333 18.233  1.00 97.70  ? 140 VAL C CB   1 
ATOM   10658 C CG1  . VAL C 1 140 ? 13.578  -19.975 17.570  1.00 95.74  ? 140 VAL C CG1  1 
ATOM   10659 C CG2  . VAL C 1 140 ? 12.591  -22.243 17.814  1.00 101.80 ? 140 VAL C CG2  1 
ATOM   10660 H H    . VAL C 1 140 ? 15.608  -22.841 19.532  1.00 125.41 ? 140 VAL C H    1 
ATOM   10661 H HA   . VAL C 1 140 ? 15.044  -22.243 16.935  1.00 124.71 ? 140 VAL C HA   1 
ATOM   10662 H HB   . VAL C 1 140 ? 13.718  -21.220 19.197  1.00 117.24 ? 140 VAL C HB   1 
ATOM   10663 H HG11 . VAL C 1 140 ? 12.718  -19.603 17.821  1.00 114.89 ? 140 VAL C HG11 1 
ATOM   10664 H HG12 . VAL C 1 140 ? 14.291  -19.389 17.868  1.00 114.89 ? 140 VAL C HG12 1 
ATOM   10665 H HG13 . VAL C 1 140 ? 13.622  -20.087 16.607  1.00 114.89 ? 140 VAL C HG13 1 
ATOM   10666 H HG21 . VAL C 1 140 ? 11.754  -21.842 18.095  1.00 122.16 ? 140 VAL C HG21 1 
ATOM   10667 H HG22 . VAL C 1 140 ? 12.603  -22.344 16.850  1.00 122.16 ? 140 VAL C HG22 1 
ATOM   10668 H HG23 . VAL C 1 140 ? 12.703  -23.108 18.238  1.00 122.16 ? 140 VAL C HG23 1 
ATOM   10669 N N    . ARG C 1 141 ? 17.171  -20.963 17.058  1.00 102.80 ? 141 ARG C N    1 
ATOM   10670 C CA   . ARG C 1 141 ? 18.350  -20.118 17.145  1.00 104.43 ? 141 ARG C CA   1 
ATOM   10671 C C    . ARG C 1 141 ? 18.029  -18.678 16.749  1.00 104.06 ? 141 ARG C C    1 
ATOM   10672 O O    . ARG C 1 141 ? 17.042  -18.396 16.059  1.00 102.00 ? 141 ARG C O    1 
ATOM   10673 C CB   . ARG C 1 141 ? 19.466  -20.665 16.255  1.00 104.75 ? 141 ARG C CB   1 
ATOM   10674 C CG   . ARG C 1 141 ? 19.904  -22.070 16.614  1.00 108.23 ? 141 ARG C CG   1 
ATOM   10675 C CD   . ARG C 1 141 ? 21.157  -22.512 15.847  1.00 112.91 ? 141 ARG C CD   1 
ATOM   10676 N NE   . ARG C 1 141 ? 22.054  -23.197 16.763  1.00 117.45 ? 141 ARG C NE   1 
ATOM   10677 C CZ   . ARG C 1 141 ? 21.791  -24.366 17.334  1.00 116.84 ? 141 ARG C CZ   1 
ATOM   10678 N NH1  . ARG C 1 141 ? 20.775  -25.119 16.941  1.00 115.29 ? 141 ARG C NH1  1 
ATOM   10679 N NH2  . ARG C 1 141 ? 22.544  -24.773 18.352  1.00 122.25 ? 141 ARG C NH2  1 
ATOM   10680 H H    . ARG C 1 141 ? 17.145  -21.456 16.354  1.00 123.36 ? 141 ARG C H    1 
ATOM   10681 H HA   . ARG C 1 141 ? 18.664  -20.111 18.063  1.00 125.32 ? 141 ARG C HA   1 
ATOM   10682 H HB2  . ARG C 1 141 ? 19.154  -20.678 15.337  1.00 125.70 ? 141 ARG C HB2  1 
ATOM   10683 H HB3  . ARG C 1 141 ? 20.240  -20.085 16.333  1.00 125.70 ? 141 ARG C HB3  1 
ATOM   10684 H HG2  . ARG C 1 141 ? 20.104  -22.108 17.562  1.00 129.88 ? 141 ARG C HG2  1 
ATOM   10685 H HG3  . ARG C 1 141 ? 19.189  -22.690 16.401  1.00 129.88 ? 141 ARG C HG3  1 
ATOM   10686 H HD2  . ARG C 1 141 ? 20.911  -23.119 15.133  1.00 135.50 ? 141 ARG C HD2  1 
ATOM   10687 H HD3  . ARG C 1 141 ? 21.611  -21.736 15.482  1.00 135.50 ? 141 ARG C HD3  1 
ATOM   10688 H HE   . ARG C 1 141 ? 22.805  -22.821 16.947  1.00 140.94 ? 141 ARG C HE   1 
ATOM   10689 H HH11 . ARG C 1 141 ? 20.266  -24.854 16.300  1.00 138.35 ? 141 ARG C HH11 1 
ATOM   10690 H HH12 . ARG C 1 141 ? 20.624  -25.873 17.326  1.00 138.35 ? 141 ARG C HH12 1 
ATOM   10691 H HH21 . ARG C 1 141 ? 23.191  -24.281 18.631  1.00 146.70 ? 141 ARG C HH21 1 
ATOM   10692 H HH22 . ARG C 1 141 ? 22.384  -25.528 18.730  1.00 146.70 ? 141 ARG C HH22 1 
ATOM   10693 N N    . PHE C 1 142 ? 18.874  -17.757 17.222  1.00 109.66 ? 142 PHE C N    1 
ATOM   10694 C CA   . PHE C 1 142 ? 18.775  -16.342 16.883  1.00 106.62 ? 142 PHE C CA   1 
ATOM   10695 C C    . PHE C 1 142 ? 20.177  -15.746 16.840  1.00 107.54 ? 142 PHE C C    1 
ATOM   10696 O O    . PHE C 1 142 ? 21.133  -16.326 17.361  1.00 110.47 ? 142 PHE C O    1 
ATOM   10697 C CB   . PHE C 1 142 ? 17.947  -15.535 17.901  1.00 101.98 ? 142 PHE C CB   1 
ATOM   10698 C CG   . PHE C 1 142 ? 16.478  -15.823 17.879  1.00 98.85  ? 142 PHE C CG   1 
ATOM   10699 C CD1  . PHE C 1 142 ? 15.955  -16.835 18.660  1.00 98.42  ? 142 PHE C CD1  1 
ATOM   10700 C CD2  . PHE C 1 142 ? 15.612  -15.057 17.113  1.00 96.77  ? 142 PHE C CD2  1 
ATOM   10701 C CE1  . PHE C 1 142 ? 14.601  -17.092 18.665  1.00 97.33  ? 142 PHE C CE1  1 
ATOM   10702 C CE2  . PHE C 1 142 ? 14.251  -15.320 17.106  1.00 96.03  ? 142 PHE C CE2  1 
ATOM   10703 C CZ   . PHE C 1 142 ? 13.746  -16.343 17.881  1.00 96.79  ? 142 PHE C CZ   1 
ATOM   10704 H H    . PHE C 1 142 ? 19.527  -17.935 17.752  1.00 131.59 ? 142 PHE C H    1 
ATOM   10705 H HA   . PHE C 1 142 ? 18.351  -16.279 16.013  1.00 127.95 ? 142 PHE C HA   1 
ATOM   10706 H HB2  . PHE C 1 142 ? 18.271  -15.738 18.792  1.00 122.38 ? 142 PHE C HB2  1 
ATOM   10707 H HB3  . PHE C 1 142 ? 18.062  -14.591 17.713  1.00 122.38 ? 142 PHE C HB3  1 
ATOM   10708 H HD1  . PHE C 1 142 ? 16.522  -17.349 19.189  1.00 118.10 ? 142 PHE C HD1  1 
ATOM   10709 H HD2  . PHE C 1 142 ? 15.949  -14.359 16.598  1.00 116.13 ? 142 PHE C HD2  1 
ATOM   10710 H HE1  . PHE C 1 142 ? 14.262  -17.774 19.199  1.00 116.80 ? 142 PHE C HE1  1 
ATOM   10711 H HE2  . PHE C 1 142 ? 13.680  -14.808 16.581  1.00 115.24 ? 142 PHE C HE2  1 
ATOM   10712 H HZ   . PHE C 1 142 ? 12.834  -16.528 17.875  1.00 116.15 ? 142 PHE C HZ   1 
ATOM   10713 N N    . SER C 1 143 ? 20.283  -14.555 16.251  1.00 107.67 ? 143 SER C N    1 
ATOM   10714 C CA   . SER C 1 143 ? 21.537  -13.808 16.275  1.00 109.44 ? 143 SER C CA   1 
ATOM   10715 C C    . SER C 1 143 ? 21.795  -13.256 17.671  1.00 111.11 ? 143 SER C C    1 
ATOM   10716 O O    . SER C 1 143 ? 21.352  -12.149 17.992  1.00 111.52 ? 143 SER C O    1 
ATOM   10717 C CB   . SER C 1 143 ? 21.500  -12.666 15.257  1.00 106.58 ? 143 SER C CB   1 
ATOM   10718 O OG   . SER C 1 143 ? 20.228  -12.046 15.250  1.00 103.22 ? 143 SER C OG   1 
ATOM   10719 H H    . SER C 1 143 ? 19.644  -14.160 15.832  1.00 129.20 ? 143 SER C H    1 
ATOM   10720 H HA   . SER C 1 143 ? 22.267  -14.401 16.035  1.00 131.33 ? 143 SER C HA   1 
ATOM   10721 H HB2  . SER C 1 143 ? 22.172  -12.008 15.495  1.00 127.89 ? 143 SER C HB2  1 
ATOM   10722 H HB3  . SER C 1 143 ? 21.684  -13.023 14.374  1.00 127.89 ? 143 SER C HB3  1 
ATOM   10723 H HG   . SER C 1 143 ? 20.082  -11.681 15.992  1.00 123.86 ? 143 SER C HG   1 
ATOM   10724 N N    . GLY C 1 144 ? 22.499  -14.013 18.506  1.00 113.77 ? 144 GLY C N    1 
ATOM   10725 C CA   . GLY C 1 144 ? 22.757  -13.591 19.866  1.00 116.22 ? 144 GLY C CA   1 
ATOM   10726 C C    . GLY C 1 144 ? 22.588  -14.710 20.870  1.00 121.38 ? 144 GLY C C    1 
ATOM   10727 O O    . GLY C 1 144 ? 23.545  -15.086 21.558  1.00 125.58 ? 144 GLY C O    1 
ATOM   10728 H H    . GLY C 1 144 ? 22.837  -14.777 18.303  1.00 136.52 ? 144 GLY C H    1 
ATOM   10729 H HA2  . GLY C 1 144 ? 23.666  -13.259 19.930  1.00 139.47 ? 144 GLY C HA2  1 
ATOM   10730 H HA3  . GLY C 1 144 ? 22.143  -12.877 20.100  1.00 139.47 ? 144 GLY C HA3  1 
ATOM   10731 N N    . ILE C 1 145 ? 21.379  -15.263 20.954  1.00 125.57 ? 145 ILE C N    1 
ATOM   10732 C CA   . ILE C 1 145 ? 21.062  -16.345 21.876  1.00 131.16 ? 145 ILE C CA   1 
ATOM   10733 C C    . ILE C 1 145 ? 20.350  -17.454 21.113  1.00 129.15 ? 145 ILE C C    1 
ATOM   10734 O O    . ILE C 1 145 ? 19.629  -17.202 20.143  1.00 126.11 ? 145 ILE C O    1 
ATOM   10735 C CB   . ILE C 1 145 ? 20.195  -15.843 23.057  1.00 132.46 ? 145 ILE C CB   1 
ATOM   10736 C CG1  . ILE C 1 145 ? 19.845  -17.002 23.997  1.00 128.95 ? 145 ILE C CG1  1 
ATOM   10737 C CG2  . ILE C 1 145 ? 18.932  -15.164 22.531  1.00 131.69 ? 145 ILE C CG2  1 
ATOM   10738 C CD1  . ILE C 1 145 ? 19.257  -16.566 25.328  1.00 124.62 ? 145 ILE C CD1  1 
ATOM   10739 H H    . ILE C 1 145 ? 20.709  -15.020 20.472  1.00 150.68 ? 145 ILE C H    1 
ATOM   10740 H HA   . ILE C 1 145 ? 21.884  -16.715 22.235  1.00 157.39 ? 145 ILE C HA   1 
ATOM   10741 H HB   . ILE C 1 145 ? 20.705  -15.191 23.563  1.00 158.95 ? 145 ILE C HB   1 
ATOM   10742 H HG12 . ILE C 1 145 ? 19.193  -17.570 23.559  1.00 154.74 ? 145 ILE C HG12 1 
ATOM   10743 H HG13 . ILE C 1 145 ? 20.653  -17.505 24.182  1.00 154.74 ? 145 ILE C HG13 1 
ATOM   10744 H HG21 . ILE C 1 145 ? 18.381  -14.895 23.283  1.00 158.03 ? 145 ILE C HG21 1 
ATOM   10745 H HG22 . ILE C 1 145 ? 19.186  -14.384 22.012  1.00 158.03 ? 145 ILE C HG22 1 
ATOM   10746 H HG23 . ILE C 1 145 ? 18.447  -15.790 21.972  1.00 158.03 ? 145 ILE C HG23 1 
ATOM   10747 H HD11 . ILE C 1 145 ? 18.969  -17.352 25.818  1.00 149.55 ? 145 ILE C HD11 1 
ATOM   10748 H HD12 . ILE C 1 145 ? 19.936  -16.093 25.833  1.00 149.55 ? 145 ILE C HD12 1 
ATOM   10749 H HD13 . ILE C 1 145 ? 18.500  -15.983 25.163  1.00 149.55 ? 145 ILE C HD13 1 
ATOM   10750 N N    . ASN C 1 146 ? 20.564  -18.695 21.553  1.00 120.34 ? 146 ASN C N    1 
ATOM   10751 C CA   . ASN C 1 146 ? 19.877  -19.862 21.005  1.00 114.92 ? 146 ASN C CA   1 
ATOM   10752 C C    . ASN C 1 146 ? 18.975  -20.433 22.093  1.00 111.06 ? 146 ASN C C    1 
ATOM   10753 O O    . ASN C 1 146 ? 19.463  -20.925 23.116  1.00 109.94 ? 146 ASN C O    1 
ATOM   10754 C CB   . ASN C 1 146 ? 20.867  -20.919 20.511  1.00 115.31 ? 146 ASN C CB   1 
ATOM   10755 C CG   . ASN C 1 146 ? 22.176  -20.324 20.040  1.00 119.61 ? 146 ASN C CG   1 
ATOM   10756 O OD1  . ASN C 1 146 ? 22.231  -19.646 19.013  1.00 116.11 ? 146 ASN C OD1  1 
ATOM   10757 N ND2  . ASN C 1 146 ? 23.243  -20.579 20.791  1.00 123.73 ? 146 ASN C ND2  1 
ATOM   10758 H H    . ASN C 1 146 ? 21.116  -18.889 22.183  1.00 144.40 ? 146 ASN C H    1 
ATOM   10759 H HA   . ASN C 1 146 ? 19.333  -19.584 20.252  1.00 137.91 ? 146 ASN C HA   1 
ATOM   10760 H HB2  . ASN C 1 146 ? 21.061  -21.534 21.236  1.00 138.37 ? 146 ASN C HB2  1 
ATOM   10761 H HB3  . ASN C 1 146 ? 20.471  -21.399 19.767  1.00 138.37 ? 146 ASN C HB3  1 
ATOM   10762 H HD21 . ASN C 1 146 ? 23.164  -21.059 21.501  1.00 148.48 ? 146 ASN C HD21 1 
ATOM   10763 H HD22 . ASN C 1 146 ? 24.011  -20.264 20.568  1.00 148.48 ? 146 ASN C HD22 1 
ATOM   10764 N N    . HIS C 1 147 ? 17.665  -20.372 21.872  1.00 107.02 ? 147 HIS C N    1 
ATOM   10765 C CA   . HIS C 1 147 ? 16.687  -20.825 22.851  1.00 103.69 ? 147 HIS C CA   1 
ATOM   10766 C C    . HIS C 1 147 ? 16.358  -22.294 22.643  1.00 104.17 ? 147 HIS C C    1 
ATOM   10767 O O    . HIS C 1 147 ? 16.228  -22.763 21.512  1.00 107.99 ? 147 HIS C O    1 
ATOM   10768 C CB   . HIS C 1 147 ? 15.413  -19.985 22.755  1.00 103.30 ? 147 HIS C CB   1 
ATOM   10769 C CG   . HIS C 1 147 ? 15.600  -18.556 23.167  1.00 104.04 ? 147 HIS C CG   1 
ATOM   10770 N ND1  . HIS C 1 147 ? 15.028  -18.027 24.306  1.00 102.11 ? 147 HIS C ND1  1 
ATOM   10771 C CD2  . HIS C 1 147 ? 16.301  -17.547 22.597  1.00 106.50 ? 147 HIS C CD2  1 
ATOM   10772 C CE1  . HIS C 1 147 ? 15.365  -16.755 24.415  1.00 99.17  ? 147 HIS C CE1  1 
ATOM   10773 N NE2  . HIS C 1 147 ? 16.138  -16.439 23.392  1.00 102.93 ? 147 HIS C NE2  1 
ATOM   10774 H H    . HIS C 1 147 ? 17.313  -20.067 21.149  1.00 128.42 ? 147 HIS C H    1 
ATOM   10775 H HA   . HIS C 1 147 ? 17.056  -20.726 23.742  1.00 124.42 ? 147 HIS C HA   1 
ATOM   10776 H HB2  . HIS C 1 147 ? 15.104  -19.990 21.835  1.00 123.97 ? 147 HIS C HB2  1 
ATOM   10777 H HB3  . HIS C 1 147 ? 14.738  -20.374 23.333  1.00 123.97 ? 147 HIS C HB3  1 
ATOM   10778 H HD1  . HIS C 1 147 ? 14.530  -18.459 24.858  1.00 122.54 ? 147 HIS C HD1  1 
ATOM   10779 H HD2  . HIS C 1 147 ? 16.800  -17.596 21.813  1.00 127.81 ? 147 HIS C HD2  1 
ATOM   10780 H HE1  . HIS C 1 147 ? 15.103  -16.179 25.097  1.00 119.00 ? 147 HIS C HE1  1 
ATOM   10781 N N    . PHE C 1 148 ? 16.223  -23.016 23.750  1.00 104.89 ? 148 PHE C N    1 
ATOM   10782 C CA   . PHE C 1 148 ? 16.018  -24.465 23.753  1.00 105.20 ? 148 PHE C CA   1 
ATOM   10783 C C    . PHE C 1 148 ? 14.646  -24.742 24.365  1.00 106.81 ? 148 PHE C C    1 
ATOM   10784 O O    . PHE C 1 148 ? 14.505  -24.749 25.590  1.00 109.95 ? 148 PHE C O    1 
ATOM   10785 C CB   . PHE C 1 148 ? 17.133  -25.164 24.534  1.00 104.19 ? 148 PHE C CB   1 
ATOM   10786 C CG   . PHE C 1 148 ? 18.458  -25.217 23.812  1.00 105.39 ? 148 PHE C CG   1 
ATOM   10787 C CD1  . PHE C 1 148 ? 19.203  -24.072 23.587  1.00 103.32 ? 148 PHE C CD1  1 
ATOM   10788 C CD2  . PHE C 1 148 ? 18.960  -26.430 23.377  1.00 109.29 ? 148 PHE C CD2  1 
ATOM   10789 C CE1  . PHE C 1 148 ? 20.420  -24.142 22.928  1.00 110.11 ? 148 PHE C CE1  1 
ATOM   10790 C CE2  . PHE C 1 148 ? 20.172  -26.509 22.719  1.00 110.78 ? 148 PHE C CE2  1 
ATOM   10791 C CZ   . PHE C 1 148 ? 20.903  -25.360 22.493  1.00 112.25 ? 148 PHE C CZ   1 
ATOM   10792 H H    . PHE C 1 148 ? 16.246  -22.679 24.540  1.00 125.86 ? 148 PHE C H    1 
ATOM   10793 H HA   . PHE C 1 148 ? 16.021  -24.800 22.842  1.00 126.24 ? 148 PHE C HA   1 
ATOM   10794 H HB2  . PHE C 1 148 ? 17.271  -24.689 25.369  1.00 125.03 ? 148 PHE C HB2  1 
ATOM   10795 H HB3  . PHE C 1 148 ? 16.859  -26.078 24.714  1.00 125.03 ? 148 PHE C HB3  1 
ATOM   10796 H HD1  . PHE C 1 148 ? 18.884  -23.249 23.881  1.00 123.99 ? 148 PHE C HD1  1 
ATOM   10797 H HD2  . PHE C 1 148 ? 18.473  -27.208 23.530  1.00 131.15 ? 148 PHE C HD2  1 
ATOM   10798 H HE1  . PHE C 1 148 ? 20.911  -23.367 22.777  1.00 132.13 ? 148 PHE C HE1  1 
ATOM   10799 H HE2  . PHE C 1 148 ? 20.494  -27.331 22.429  1.00 132.93 ? 148 PHE C HE2  1 
ATOM   10800 H HZ   . PHE C 1 148 ? 21.720  -25.406 22.050  1.00 134.70 ? 148 PHE C HZ   1 
ATOM   10801 N N    . ILE C 1 149 ? 13.632  -24.955 23.520  1.00 110.38 ? 149 ILE C N    1 
ATOM   10802 C CA   . ILE C 1 149 ? 12.292  -25.244 24.024  1.00 108.60 ? 149 ILE C CA   1 
ATOM   10803 C C    . ILE C 1 149 ? 12.268  -26.649 24.626  1.00 111.59 ? 149 ILE C C    1 
ATOM   10804 O O    . ILE C 1 149 ? 12.951  -27.567 24.153  1.00 118.75 ? 149 ILE C O    1 
ATOM   10805 C CB   . ILE C 1 149 ? 11.242  -25.112 22.903  1.00 105.07 ? 149 ILE C CB   1 
ATOM   10806 C CG1  . ILE C 1 149 ? 11.394  -23.787 22.151  1.00 104.46 ? 149 ILE C CG1  1 
ATOM   10807 C CG2  . ILE C 1 149 ? 9.830   -25.241 23.472  1.00 102.52 ? 149 ILE C CG2  1 
ATOM   10808 C CD1  . ILE C 1 149 ? 11.365  -22.541 23.038  1.00 100.96 ? 149 ILE C CD1  1 
ATOM   10809 H H    . ILE C 1 149 ? 13.695  -24.939 22.662  1.00 132.45 ? 149 ILE C H    1 
ATOM   10810 H HA   . ILE C 1 149 ? 12.073  -24.601 24.716  1.00 130.32 ? 149 ILE C HA   1 
ATOM   10811 H HB   . ILE C 1 149 ? 11.393  -25.833 22.272  1.00 126.08 ? 149 ILE C HB   1 
ATOM   10812 H HG12 . ILE C 1 149 ? 12.244  -23.794 21.684  1.00 125.35 ? 149 ILE C HG12 1 
ATOM   10813 H HG13 . ILE C 1 149 ? 10.667  -23.709 21.514  1.00 125.35 ? 149 ILE C HG13 1 
ATOM   10814 H HG21 . ILE C 1 149 ? 9.189   -25.019 22.779  1.00 123.02 ? 149 ILE C HG21 1 
ATOM   10815 H HG22 . ILE C 1 149 ? 9.692   -26.153 23.770  1.00 123.02 ? 149 ILE C HG22 1 
ATOM   10816 H HG23 . ILE C 1 149 ? 9.734   -24.630 24.220  1.00 123.02 ? 149 ILE C HG23 1 
ATOM   10817 H HD11 . ILE C 1 149 ? 11.336  -21.752 22.474  1.00 121.15 ? 149 ILE C HD11 1 
ATOM   10818 H HD12 . ILE C 1 149 ? 10.577  -22.574 23.603  1.00 121.15 ? 149 ILE C HD12 1 
ATOM   10819 H HD13 . ILE C 1 149 ? 12.165  -22.525 23.587  1.00 121.15 ? 149 ILE C HD13 1 
ATOM   10820 N N    . PHE C 1 150 ? 11.475  -26.821 25.686  1.00 110.56 ? 150 PHE C N    1 
ATOM   10821 C CA   . PHE C 1 150 ? 11.270  -28.126 26.315  1.00 113.57 ? 150 PHE C CA   1 
ATOM   10822 C C    . PHE C 1 150 ? 9.809   -28.211 26.739  1.00 116.05 ? 150 PHE C C    1 
ATOM   10823 O O    . PHE C 1 150 ? 9.385   -27.495 27.652  1.00 115.32 ? 150 PHE C O    1 
ATOM   10824 C CB   . PHE C 1 150 ? 12.201  -28.333 27.519  1.00 113.08 ? 150 PHE C CB   1 
ATOM   10825 C CG   . PHE C 1 150 ? 12.009  -29.656 28.233  1.00 122.30 ? 150 PHE C CG   1 
ATOM   10826 C CD1  . PHE C 1 150 ? 10.831  -29.938 28.912  1.00 122.19 ? 150 PHE C CD1  1 
ATOM   10827 C CD2  . PHE C 1 150 ? 13.016  -30.607 28.242  1.00 125.86 ? 150 PHE C CD2  1 
ATOM   10828 C CE1  . PHE C 1 150 ? 10.656  -31.146 29.565  1.00 122.46 ? 150 PHE C CE1  1 
ATOM   10829 C CE2  . PHE C 1 150 ? 12.842  -31.819 28.894  1.00 128.03 ? 150 PHE C CE2  1 
ATOM   10830 C CZ   . PHE C 1 150 ? 11.665  -32.084 29.558  1.00 126.73 ? 150 PHE C CZ   1 
ATOM   10831 H H    . PHE C 1 150 ? 11.038  -26.184 26.065  1.00 132.68 ? 150 PHE C H    1 
ATOM   10832 H HA   . PHE C 1 150 ? 11.454  -28.827 25.670  1.00 136.28 ? 150 PHE C HA   1 
ATOM   10833 H HB2  . PHE C 1 150 ? 13.120  -28.295 27.211  1.00 135.69 ? 150 PHE C HB2  1 
ATOM   10834 H HB3  . PHE C 1 150 ? 12.037  -27.625 28.162  1.00 135.69 ? 150 PHE C HB3  1 
ATOM   10835 H HD1  . PHE C 1 150 ? 10.148  -29.307 28.927  1.00 146.63 ? 150 PHE C HD1  1 
ATOM   10836 H HD2  . PHE C 1 150 ? 13.818  -30.431 27.806  1.00 151.03 ? 150 PHE C HD2  1 
ATOM   10837 H HE1  . PHE C 1 150 ? 9.859   -31.324 30.009  1.00 146.96 ? 150 PHE C HE1  1 
ATOM   10838 H HE2  . PHE C 1 150 ? 13.521  -32.454 28.882  1.00 153.64 ? 150 PHE C HE2  1 
ATOM   10839 H HZ   . PHE C 1 150 ? 11.551  -32.894 30.000  1.00 152.08 ? 150 PHE C HZ   1 
ATOM   10840 N N    . ASN C 1 151 ? 9.045   -29.089 26.091  1.00 117.30 ? 151 ASN C N    1 
ATOM   10841 C CA   . ASN C 1 151 ? 7.667   -29.359 26.490  1.00 118.41 ? 151 ASN C CA   1 
ATOM   10842 C C    . ASN C 1 151 ? 7.670   -30.414 27.592  1.00 124.27 ? 151 ASN C C    1 
ATOM   10843 O O    . ASN C 1 151 ? 8.122   -31.544 27.373  1.00 126.79 ? 151 ASN C O    1 
ATOM   10844 C CB   . ASN C 1 151 ? 6.842   -29.830 25.293  1.00 121.01 ? 151 ASN C CB   1 
ATOM   10845 C CG   . ASN C 1 151 ? 5.349   -29.723 25.536  1.00 124.91 ? 151 ASN C CG   1 
ATOM   10846 O OD1  . ASN C 1 151 ? 4.877   -29.914 26.656  1.00 129.16 ? 151 ASN C OD1  1 
ATOM   10847 N ND2  . ASN C 1 151 ? 4.598   -29.412 24.485  1.00 121.90 ? 151 ASN C ND2  1 
ATOM   10848 H H    . ASN C 1 151 ? 9.305   -29.546 25.410  1.00 140.76 ? 151 ASN C H    1 
ATOM   10849 H HA   . ASN C 1 151 ? 7.261   -28.547 26.831  1.00 142.09 ? 151 ASN C HA   1 
ATOM   10850 H HB2  . ASN C 1 151 ? 7.061   -29.284 24.522  1.00 145.21 ? 151 ASN C HB2  1 
ATOM   10851 H HB3  . ASN C 1 151 ? 7.051   -30.760 25.111  1.00 145.21 ? 151 ASN C HB3  1 
ATOM   10852 H HD21 . ASN C 1 151 ? 3.745   -29.339 24.572  1.00 146.27 ? 151 ASN C HD21 1 
ATOM   10853 H HD22 . ASN C 1 151 ? 4.964   -29.283 23.718  1.00 146.27 ? 151 ASN C HD22 1 
ATOM   10854 N N    . ILE C 1 152 ? 7.170   -30.049 28.774  1.00 121.64 ? 152 ILE C N    1 
ATOM   10855 C CA   . ILE C 1 152 ? 7.256   -30.970 29.899  1.00 123.38 ? 152 ILE C CA   1 
ATOM   10856 C C    . ILE C 1 152 ? 6.138   -32.015 29.836  1.00 130.19 ? 152 ILE C C    1 
ATOM   10857 O O    . ILE C 1 152 ? 6.326   -33.158 30.265  1.00 128.76 ? 152 ILE C O    1 
ATOM   10858 C CB   . ILE C 1 152 ? 7.216   -30.216 31.237  1.00 116.40 ? 152 ILE C CB   1 
ATOM   10859 C CG1  . ILE C 1 152 ? 7.991   -28.902 31.162  1.00 117.62 ? 152 ILE C CG1  1 
ATOM   10860 C CG2  . ILE C 1 152 ? 7.810   -31.084 32.340  1.00 116.06 ? 152 ILE C CG2  1 
ATOM   10861 C CD1  . ILE C 1 152 ? 7.828   -28.006 32.406  1.00 103.07 ? 152 ILE C CD1  1 
ATOM   10862 H H    . ILE C 1 152 ? 6.789   -29.297 28.943  1.00 145.97 ? 152 ILE C H    1 
ATOM   10863 H HA   . ILE C 1 152 ? 8.110   -31.427 29.841  1.00 148.06 ? 152 ILE C HA   1 
ATOM   10864 H HB   . ILE C 1 152 ? 6.287   -30.016 31.431  1.00 139.68 ? 152 ILE C HB   1 
ATOM   10865 H HG12 . ILE C 1 152 ? 8.935   -29.102 31.065  1.00 141.14 ? 152 ILE C HG12 1 
ATOM   10866 H HG13 . ILE C 1 152 ? 7.678   -28.399 30.394  1.00 141.14 ? 152 ILE C HG13 1 
ATOM   10867 H HG21 . ILE C 1 152 ? 7.766   -30.601 33.180  1.00 139.27 ? 152 ILE C HG21 1 
ATOM   10868 H HG22 . ILE C 1 152 ? 7.299   -31.906 32.405  1.00 139.27 ? 152 ILE C HG22 1 
ATOM   10869 H HG23 . ILE C 1 152 ? 8.733   -31.285 32.122  1.00 139.27 ? 152 ILE C HG23 1 
ATOM   10870 H HD11 . ILE C 1 152 ? 8.330   -27.187 32.273  1.00 123.68 ? 152 ILE C HD11 1 
ATOM   10871 H HD12 . ILE C 1 152 ? 6.888   -27.802 32.527  1.00 123.68 ? 152 ILE C HD12 1 
ATOM   10872 H HD13 . ILE C 1 152 ? 8.167   -28.479 33.182  1.00 123.68 ? 152 ILE C HD13 1 
ATOM   10873 N N    . LYS C 1 153 ? 4.962   -31.649 29.317  1.00 134.32 ? 153 LYS C N    1 
ATOM   10874 C CA   . LYS C 1 153 ? 3.897   -32.633 29.150  1.00 138.68 ? 153 LYS C CA   1 
ATOM   10875 C C    . LYS C 1 153 ? 4.270   -33.676 28.103  1.00 142.48 ? 153 LYS C C    1 
ATOM   10876 O O    . LYS C 1 153 ? 3.803   -34.818 28.177  1.00 144.33 ? 153 LYS C O    1 
ATOM   10877 C CB   . LYS C 1 153 ? 2.591   -31.925 28.780  1.00 140.04 ? 153 LYS C CB   1 
ATOM   10878 C CG   . LYS C 1 153 ? 1.432   -32.845 28.417  1.00 143.12 ? 153 LYS C CG   1 
ATOM   10879 C CD   . LYS C 1 153 ? 0.517   -32.189 27.378  1.00 144.79 ? 153 LYS C CD   1 
ATOM   10880 C CE   . LYS C 1 153 ? -0.465  -33.188 26.782  1.00 146.37 ? 153 LYS C CE   1 
ATOM   10881 N NZ   . LYS C 1 153 ? -1.759  -32.546 26.409  1.00 145.93 ? 153 LYS C NZ   1 
ATOM   10882 H H    . LYS C 1 153 ? 4.762   -30.853 29.059  1.00 161.19 ? 153 LYS C H    1 
ATOM   10883 H HA   . LYS C 1 153 ? 3.751   -33.098 29.989  1.00 166.41 ? 153 LYS C HA   1 
ATOM   10884 H HB2  . LYS C 1 153 ? 2.308   -31.388 29.537  1.00 168.05 ? 153 LYS C HB2  1 
ATOM   10885 H HB3  . LYS C 1 153 ? 2.758   -31.354 28.014  1.00 168.05 ? 153 LYS C HB3  1 
ATOM   10886 H HG2  . LYS C 1 153 ? 1.780   -33.670 28.043  1.00 171.74 ? 153 LYS C HG2  1 
ATOM   10887 H HG3  . LYS C 1 153 ? 0.909   -33.034 29.211  1.00 171.74 ? 153 LYS C HG3  1 
ATOM   10888 H HD2  . LYS C 1 153 ? 0.009   -31.479 27.800  1.00 173.75 ? 153 LYS C HD2  1 
ATOM   10889 H HD3  . LYS C 1 153 ? 1.057   -31.828 26.658  1.00 173.75 ? 153 LYS C HD3  1 
ATOM   10890 H HE2  . LYS C 1 153 ? -0.078  -33.578 25.982  1.00 175.65 ? 153 LYS C HE2  1 
ATOM   10891 H HE3  . LYS C 1 153 ? -0.649  -33.883 27.434  1.00 175.65 ? 153 LYS C HE3  1 
ATOM   10892 H HZ1  . LYS C 1 153 ? -2.309  -33.151 26.059  1.00 175.11 ? 153 LYS C HZ1  1 
ATOM   10893 H HZ2  . LYS C 1 153 ? -2.141  -32.189 27.129  1.00 175.11 ? 153 LYS C HZ2  1 
ATOM   10894 H HZ3  . LYS C 1 153 ? -1.617  -31.903 25.809  1.00 175.11 ? 153 LYS C HZ3  1 
ATOM   10895 N N    . GLU C 1 154 ? 5.114   -33.313 27.136  1.00 137.32 ? 154 GLU C N    1 
ATOM   10896 C CA   . GLU C 1 154 ? 5.515   -34.214 26.063  1.00 139.71 ? 154 GLU C CA   1 
ATOM   10897 C C    . GLU C 1 154 ? 6.893   -34.825 26.300  1.00 137.43 ? 154 GLU C C    1 
ATOM   10898 O O    . GLU C 1 154 ? 7.585   -35.189 25.344  1.00 141.60 ? 154 GLU C O    1 
ATOM   10899 C CB   . GLU C 1 154 ? 5.487   -33.477 24.724  1.00 147.25 ? 154 GLU C CB   1 
ATOM   10900 C CG   . GLU C 1 154 ? 4.175   -32.767 24.430  1.00 145.88 ? 154 GLU C CG   1 
ATOM   10901 C CD   . GLU C 1 154 ? 2.985   -33.706 24.456  1.00 151.96 ? 154 GLU C CD   1 
ATOM   10902 O OE1  . GLU C 1 154 ? 3.098   -34.832 23.927  1.00 151.45 ? 154 GLU C OE1  1 
ATOM   10903 O OE2  . GLU C 1 154 ? 1.938   -33.319 25.009  1.00 153.56 ? 154 GLU C OE2  1 
ATOM   10904 H H    . GLU C 1 154 ? 5.473   -32.534 27.081  1.00 164.78 ? 154 GLU C H    1 
ATOM   10905 H HA   . GLU C 1 154 ? 4.877   -34.943 26.022  1.00 167.65 ? 154 GLU C HA   1 
ATOM   10906 H HB2  . GLU C 1 154 ? 6.190   -32.809 24.723  1.00 176.70 ? 154 GLU C HB2  1 
ATOM   10907 H HB3  . GLU C 1 154 ? 5.640   -34.120 24.013  1.00 176.70 ? 154 GLU C HB3  1 
ATOM   10908 H HG2  . GLU C 1 154 ? 4.030   -32.080 25.099  1.00 175.06 ? 154 GLU C HG2  1 
ATOM   10909 H HG3  . GLU C 1 154 ? 4.223   -32.366 23.548  1.00 175.06 ? 154 GLU C HG3  1 
ATOM   10910 N N    . ASN C 1 155 ? 7.304   -34.952 27.559  1.00 136.45 ? 155 ASN C N    1 
ATOM   10911 C CA   . ASN C 1 155 ? 8.599   -35.531 27.883  1.00 136.93 ? 155 ASN C CA   1 
ATOM   10912 C C    . ASN C 1 155 ? 8.479   -36.330 29.171  1.00 140.63 ? 155 ASN C C    1 
ATOM   10913 O O    . ASN C 1 155 ? 7.624   -36.052 30.015  1.00 141.09 ? 155 ASN C O    1 
ATOM   10914 C CB   . ASN C 1 155 ? 9.676   -34.452 28.030  1.00 135.01 ? 155 ASN C CB   1 
ATOM   10915 C CG   . ASN C 1 155 ? 10.504  -34.281 26.773  1.00 135.26 ? 155 ASN C CG   1 
ATOM   10916 O OD1  . ASN C 1 155 ? 11.597  -34.835 26.657  1.00 136.71 ? 155 ASN C OD1  1 
ATOM   10917 N ND2  . ASN C 1 155 ? 9.984   -33.513 25.822  1.00 132.12 ? 155 ASN C ND2  1 
ATOM   10918 H H    . ASN C 1 155 ? 6.847   -34.708 28.245  1.00 163.74 ? 155 ASN C H    1 
ATOM   10919 H HA   . ASN C 1 155 ? 8.867   -36.137 27.175  1.00 164.31 ? 155 ASN C HA   1 
ATOM   10920 H HB2  . ASN C 1 155 ? 9.250   -33.604 28.227  1.00 162.01 ? 155 ASN C HB2  1 
ATOM   10921 H HB3  . ASN C 1 155 ? 10.275  -34.699 28.752  1.00 162.01 ? 155 ASN C HB3  1 
ATOM   10922 H HD21 . ASN C 1 155 ? 9.216   -33.144 25.940  1.00 158.55 ? 155 ASN C HD21 1 
ATOM   10923 H HD22 . ASN C 1 155 ? 10.415  -33.385 25.090  1.00 158.55 ? 155 ASN C HD22 1 
ATOM   10924 N N    . LYS C 1 156 ? 9.347   -37.328 29.311  1.00 142.24 ? 156 LYS C N    1 
ATOM   10925 C CA   . LYS C 1 156 ? 9.339   -38.166 30.496  1.00 143.47 ? 156 LYS C CA   1 
ATOM   10926 C C    . LYS C 1 156 ? 9.659   -37.332 31.736  1.00 147.50 ? 156 LYS C C    1 
ATOM   10927 O O    . LYS C 1 156 ? 10.055  -36.165 31.657  1.00 147.38 ? 156 LYS C O    1 
ATOM   10928 C CB   . LYS C 1 156 ? 10.343  -39.307 30.343  1.00 147.80 ? 156 LYS C CB   1 
ATOM   10929 C CG   . LYS C 1 156 ? 10.004  -40.281 29.222  1.00 152.18 ? 156 LYS C CG   1 
ATOM   10930 C CD   . LYS C 1 156 ? 11.064  -41.367 29.086  1.00 155.43 ? 156 LYS C CD   1 
ATOM   10931 C CE   . LYS C 1 156 ? 10.732  -42.333 27.954  1.00 158.26 ? 156 LYS C CE   1 
ATOM   10932 N NZ   . LYS C 1 156 ? 11.781  -43.380 27.781  1.00 158.32 ? 156 LYS C NZ   1 
ATOM   10933 H H    . LYS C 1 156 ? 9.948   -37.538 28.732  1.00 170.69 ? 156 LYS C H    1 
ATOM   10934 H HA   . LYS C 1 156 ? 8.458   -38.554 30.615  1.00 172.17 ? 156 LYS C HA   1 
ATOM   10935 H HB2  . LYS C 1 156 ? 11.216  -38.930 30.154  1.00 177.36 ? 156 LYS C HB2  1 
ATOM   10936 H HB3  . LYS C 1 156 ? 10.371  -39.810 31.173  1.00 177.36 ? 156 LYS C HB3  1 
ATOM   10937 H HG2  . LYS C 1 156 ? 9.154   -40.708 29.412  1.00 182.61 ? 156 LYS C HG2  1 
ATOM   10938 H HG3  . LYS C 1 156 ? 9.952   -39.799 28.382  1.00 182.61 ? 156 LYS C HG3  1 
ATOM   10939 H HD2  . LYS C 1 156 ? 11.922  -40.956 28.894  1.00 186.51 ? 156 LYS C HD2  1 
ATOM   10940 H HD3  . LYS C 1 156 ? 11.115  -41.872 29.912  1.00 186.51 ? 156 LYS C HD3  1 
ATOM   10941 H HE2  . LYS C 1 156 ? 9.891   -42.776 28.150  1.00 189.91 ? 156 LYS C HE2  1 
ATOM   10942 H HE3  . LYS C 1 156 ? 10.660  -41.837 27.123  1.00 189.91 ? 156 LYS C HE3  1 
ATOM   10943 H HZ1  . LYS C 1 156 ? 11.557  -43.928 27.118  1.00 189.98 ? 156 LYS C HZ1  1 
ATOM   10944 H HZ2  . LYS C 1 156 ? 12.562  -42.999 27.590  1.00 189.98 ? 156 LYS C HZ2  1 
ATOM   10945 H HZ3  . LYS C 1 156 ? 11.865  -43.852 28.531  1.00 189.98 ? 156 LYS C HZ3  1 
ATOM   10946 N N    . GLU C 1 157 ? 9.471   -37.952 32.899  1.00 151.09 ? 157 GLU C N    1 
ATOM   10947 C CA   . GLU C 1 157 ? 9.768   -37.285 34.159  1.00 147.82 ? 157 GLU C CA   1 
ATOM   10948 C C    . GLU C 1 157 ? 11.229  -36.864 34.199  1.00 143.06 ? 157 GLU C C    1 
ATOM   10949 O O    . GLU C 1 157 ? 12.125  -37.653 33.882  1.00 139.95 ? 157 GLU C O    1 
ATOM   10950 C CB   . GLU C 1 157 ? 9.457   -38.211 35.331  1.00 154.75 ? 157 GLU C CB   1 
ATOM   10951 C CG   . GLU C 1 157 ? 7.993   -38.571 35.469  1.00 161.19 ? 157 GLU C CG   1 
ATOM   10952 C CD   . GLU C 1 157 ? 7.756   -39.613 36.546  1.00 171.59 ? 157 GLU C CD   1 
ATOM   10953 O OE1  . GLU C 1 157 ? 8.743   -40.202 37.037  1.00 172.82 ? 157 GLU C OE1  1 
ATOM   10954 O OE2  . GLU C 1 157 ? 6.581   -39.844 36.903  1.00 176.48 ? 157 GLU C OE2  1 
ATOM   10955 H H    . GLU C 1 157 ? 9.174   -38.754 32.984  1.00 181.32 ? 157 GLU C H    1 
ATOM   10956 H HA   . GLU C 1 157 ? 9.214   -36.493 34.241  1.00 177.39 ? 157 GLU C HA   1 
ATOM   10957 H HB2  . GLU C 1 157 ? 9.953   -39.036 35.214  1.00 185.70 ? 157 GLU C HB2  1 
ATOM   10958 H HB3  . GLU C 1 157 ? 9.731   -37.773 36.152  1.00 185.70 ? 157 GLU C HB3  1 
ATOM   10959 H HG2  . GLU C 1 157 ? 7.490   -37.775 35.704  1.00 193.43 ? 157 GLU C HG2  1 
ATOM   10960 H HG3  . GLU C 1 157 ? 7.673   -38.929 34.627  1.00 193.43 ? 157 GLU C HG3  1 
ATOM   10961 N N    . THR C 1 158 ? 11.470  -35.620 34.609  1.00 141.77 ? 158 THR C N    1 
ATOM   10962 C CA   . THR C 1 158 ? 12.819  -35.083 34.610  1.00 137.90 ? 158 THR C CA   1 
ATOM   10963 C C    . THR C 1 158 ? 12.965  -34.008 35.676  1.00 137.31 ? 158 THR C C    1 
ATOM   10964 O O    . THR C 1 158 ? 11.988  -33.556 36.278  1.00 139.45 ? 158 THR C O    1 
ATOM   10965 C CB   . THR C 1 158 ? 13.186  -34.473 33.252  1.00 137.52 ? 158 THR C CB   1 
ATOM   10966 O OG1  . THR C 1 158 ? 14.364  -33.668 33.400  1.00 133.12 ? 158 THR C OG1  1 
ATOM   10967 C CG2  . THR C 1 158 ? 12.042  -33.591 32.750  1.00 138.72 ? 158 THR C CG2  1 
ATOM   10968 H H    . THR C 1 158 ? 10.868  -35.073 34.890  1.00 170.13 ? 158 THR C H    1 
ATOM   10969 H HA   . THR C 1 158 ? 13.416  -35.817 34.822  1.00 165.49 ? 158 THR C HA   1 
ATOM   10970 H HB   . THR C 1 158 ? 13.348  -35.177 32.605  1.00 165.02 ? 158 THR C HB   1 
ATOM   10971 H HG1  . THR C 1 158 ? 14.574  -33.328 32.661  1.00 159.74 ? 158 THR C HG1  1 
ATOM   10972 H HG21 . THR C 1 158 ? 12.273  -33.205 31.891  1.00 166.46 ? 158 THR C HG21 1 
ATOM   10973 H HG22 . THR C 1 158 ? 11.235  -34.120 32.650  1.00 166.46 ? 158 THR C HG22 1 
ATOM   10974 H HG23 . THR C 1 158 ? 11.872  -32.875 33.382  1.00 166.46 ? 158 THR C HG23 1 
ATOM   10975 N N    . SER C 1 159 ? 14.212  -33.589 35.880  1.00 134.82 ? 159 SER C N    1 
ATOM   10976 C CA   . SER C 1 159 ? 14.558  -32.468 36.739  1.00 127.64 ? 159 SER C CA   1 
ATOM   10977 C C    . SER C 1 159 ? 14.981  -31.286 35.879  1.00 125.34 ? 159 SER C C    1 
ATOM   10978 O O    . SER C 1 159 ? 15.623  -31.465 34.838  1.00 126.43 ? 159 SER C O    1 
ATOM   10979 C CB   . SER C 1 159 ? 15.695  -32.834 37.693  1.00 125.90 ? 159 SER C CB   1 
ATOM   10980 O OG   . SER C 1 159 ? 16.422  -31.678 38.076  1.00 127.26 ? 159 SER C OG   1 
ATOM   10981 H H    . SER C 1 159 ? 14.899  -33.955 35.515  1.00 161.79 ? 159 SER C H    1 
ATOM   10982 H HA   . SER C 1 159 ? 13.786  -32.214 37.269  1.00 153.17 ? 159 SER C HA   1 
ATOM   10983 H HB2  . SER C 1 159 ? 15.322  -33.249 38.486  1.00 151.08 ? 159 SER C HB2  1 
ATOM   10984 H HB3  . SER C 1 159 ? 16.296  -33.451 37.247  1.00 151.08 ? 159 SER C HB3  1 
ATOM   10985 H HG   . SER C 1 159 ? 17.053  -31.892 38.587  1.00 152.71 ? 159 SER C HG   1 
ATOM   10986 N N    . PHE C 1 160 ? 14.624  -30.076 36.316  1.00 122.48 ? 160 PHE C N    1 
ATOM   10987 C CA   . PHE C 1 160 ? 15.057  -28.879 35.602  1.00 120.53 ? 160 PHE C CA   1 
ATOM   10988 C C    . PHE C 1 160 ? 16.578  -28.836 35.495  1.00 123.67 ? 160 PHE C C    1 
ATOM   10989 O O    . PHE C 1 160 ? 17.133  -28.571 34.422  1.00 122.45 ? 160 PHE C O    1 
ATOM   10990 C CB   . PHE C 1 160 ? 14.544  -27.624 36.311  1.00 115.23 ? 160 PHE C CB   1 
ATOM   10991 C CG   . PHE C 1 160 ? 13.178  -27.180 35.867  1.00 106.53 ? 160 PHE C CG   1 
ATOM   10992 C CD1  . PHE C 1 160 ? 12.209  -28.102 35.508  1.00 107.24 ? 160 PHE C CD1  1 
ATOM   10993 C CD2  . PHE C 1 160 ? 12.862  -25.833 35.822  1.00 103.19 ? 160 PHE C CD2  1 
ATOM   10994 C CE1  . PHE C 1 160 ? 10.954  -27.688 35.108  1.00 102.69 ? 160 PHE C CE1  1 
ATOM   10995 C CE2  . PHE C 1 160 ? 11.610  -25.413 35.424  1.00 102.12 ? 160 PHE C CE2  1 
ATOM   10996 C CZ   . PHE C 1 160 ? 10.654  -26.341 35.067  1.00 100.18 ? 160 PHE C CZ   1 
ATOM   10997 H H    . PHE C 1 160 ? 14.139  -29.926 37.011  1.00 146.97 ? 160 PHE C H    1 
ATOM   10998 H HA   . PHE C 1 160 ? 14.681  -28.897 34.708  1.00 144.64 ? 160 PHE C HA   1 
ATOM   10999 H HB2  . PHE C 1 160 ? 14.499  -27.802 37.263  1.00 138.27 ? 160 PHE C HB2  1 
ATOM   11000 H HB3  . PHE C 1 160 ? 15.161  -26.896 36.138  1.00 138.27 ? 160 PHE C HB3  1 
ATOM   11001 H HD1  . PHE C 1 160 ? 12.406  -29.011 35.537  1.00 128.69 ? 160 PHE C HD1  1 
ATOM   11002 H HD2  . PHE C 1 160 ? 13.502  -25.203 36.065  1.00 123.83 ? 160 PHE C HD2  1 
ATOM   11003 H HE1  . PHE C 1 160 ? 10.312  -28.315 34.867  1.00 123.23 ? 160 PHE C HE1  1 
ATOM   11004 H HE2  . PHE C 1 160 ? 11.410  -24.505 35.395  1.00 122.54 ? 160 PHE C HE2  1 
ATOM   11005 H HZ   . PHE C 1 160 ? 9.809   -26.060 34.799  1.00 120.22 ? 160 PHE C HZ   1 
ATOM   11006 N N    . GLU C 1 161 ? 17.272  -29.099 36.607  1.00 128.92 ? 161 GLU C N    1 
ATOM   11007 C CA   . GLU C 1 161 ? 18.728  -28.986 36.610  1.00 128.00 ? 161 GLU C CA   1 
ATOM   11008 C C    . GLU C 1 161 ? 19.363  -30.042 35.717  1.00 127.04 ? 161 GLU C C    1 
ATOM   11009 O O    . GLU C 1 161 ? 20.343  -29.761 35.018  1.00 127.96 ? 161 GLU C O    1 
ATOM   11010 C CB   . GLU C 1 161 ? 19.263  -29.098 38.036  1.00 132.33 ? 161 GLU C CB   1 
ATOM   11011 C CG   . GLU C 1 161 ? 20.766  -28.867 38.153  1.00 134.76 ? 161 GLU C CG   1 
ATOM   11012 C CD   . GLU C 1 161 ? 21.240  -27.634 37.398  1.00 136.28 ? 161 GLU C CD   1 
ATOM   11013 O OE1  . GLU C 1 161 ? 20.714  -26.528 37.658  1.00 131.37 ? 161 GLU C OE1  1 
ATOM   11014 O OE2  . GLU C 1 161 ? 22.137  -27.769 36.539  1.00 134.10 ? 161 GLU C OE2  1 
ATOM   11015 H H    . GLU C 1 161 ? 16.929  -29.340 37.357  1.00 154.71 ? 161 GLU C H    1 
ATOM   11016 H HA   . GLU C 1 161 ? 18.972  -28.112 36.268  1.00 153.60 ? 161 GLU C HA   1 
ATOM   11017 H HB2  . GLU C 1 161 ? 18.819  -28.436 38.588  1.00 158.80 ? 161 GLU C HB2  1 
ATOM   11018 H HB3  . GLU C 1 161 ? 19.074  -29.989 38.370  1.00 158.80 ? 161 GLU C HB3  1 
ATOM   11019 H HG2  . GLU C 1 161 ? 20.995  -28.752 39.088  1.00 161.70 ? 161 GLU C HG2  1 
ATOM   11020 H HG3  . GLU C 1 161 ? 21.232  -29.637 37.790  1.00 161.70 ? 161 GLU C HG3  1 
ATOM   11021 N N    . ASN C 1 162 ? 18.823  -31.262 35.731  1.00 128.82 ? 162 ASN C N    1 
ATOM   11022 C CA   . ASN C 1 162 ? 19.307  -32.300 34.827  1.00 126.12 ? 162 ASN C CA   1 
ATOM   11023 C C    . ASN C 1 162 ? 19.327  -31.797 33.388  1.00 126.29 ? 162 ASN C C    1 
ATOM   11024 O O    . ASN C 1 162 ? 20.356  -31.862 32.705  1.00 126.09 ? 162 ASN C O    1 
ATOM   11025 C CB   . ASN C 1 162 ? 18.428  -33.545 34.956  1.00 124.01 ? 162 ASN C CB   1 
ATOM   11026 C CG   . ASN C 1 162 ? 19.035  -34.757 34.290  1.00 126.60 ? 162 ASN C CG   1 
ATOM   11027 O OD1  . ASN C 1 162 ? 20.252  -34.941 34.304  1.00 128.53 ? 162 ASN C OD1  1 
ATOM   11028 N ND2  . ASN C 1 162 ? 18.189  -35.595 33.702  1.00 129.15 ? 162 ASN C ND2  1 
ATOM   11029 H H    . ASN C 1 162 ? 18.184  -31.511 36.250  1.00 154.58 ? 162 ASN C H    1 
ATOM   11030 H HA   . ASN C 1 162 ? 20.213  -32.545 35.073  1.00 151.34 ? 162 ASN C HA   1 
ATOM   11031 H HB2  . ASN C 1 162 ? 18.304  -33.749 35.897  1.00 148.82 ? 162 ASN C HB2  1 
ATOM   11032 H HB3  . ASN C 1 162 ? 17.569  -33.371 34.539  1.00 148.82 ? 162 ASN C HB3  1 
ATOM   11033 H HD21 . ASN C 1 162 ? 17.344  -35.433 33.714  1.00 154.98 ? 162 ASN C HD21 1 
ATOM   11034 H HD22 . ASN C 1 162 ? 18.485  -36.300 33.309  1.00 154.98 ? 162 ASN C HD22 1 
ATOM   11035 N N    . ILE C 1 163 ? 18.193  -31.272 32.920  1.00 125.32 ? 163 ILE C N    1 
ATOM   11036 C CA   . ILE C 1 163 ? 18.113  -30.748 31.559  1.00 125.39 ? 163 ILE C CA   1 
ATOM   11037 C C    . ILE C 1 163 ? 19.159  -29.663 31.347  1.00 124.28 ? 163 ILE C C    1 
ATOM   11038 O O    . ILE C 1 163 ? 19.927  -29.693 30.378  1.00 123.21 ? 163 ILE C O    1 
ATOM   11039 C CB   . ILE C 1 163 ? 16.696  -30.214 31.277  1.00 124.08 ? 163 ILE C CB   1 
ATOM   11040 C CG1  . ILE C 1 163 ? 15.681  -31.352 31.292  1.00 122.37 ? 163 ILE C CG1  1 
ATOM   11041 C CG2  . ILE C 1 163 ? 16.665  -29.452 29.958  1.00 118.25 ? 163 ILE C CG2  1 
ATOM   11042 C CD1  . ILE C 1 163 ? 14.264  -30.873 31.479  1.00 123.54 ? 163 ILE C CD1  1 
ATOM   11043 H H    . ILE C 1 163 ? 17.462  -31.209 33.368  1.00 150.39 ? 163 ILE C H    1 
ATOM   11044 H HA   . ILE C 1 163 ? 18.297  -31.471 30.940  1.00 150.47 ? 163 ILE C HA   1 
ATOM   11045 H HB   . ILE C 1 163 ? 16.453  -29.595 31.982  1.00 148.89 ? 163 ILE C HB   1 
ATOM   11046 H HG12 . ILE C 1 163 ? 15.728  -31.827 30.448  1.00 146.85 ? 163 ILE C HG12 1 
ATOM   11047 H HG13 . ILE C 1 163 ? 15.893  -31.953 32.023  1.00 146.85 ? 163 ILE C HG13 1 
ATOM   11048 H HG21 . ILE C 1 163 ? 15.742  -29.286 29.710  1.00 141.90 ? 163 ILE C HG21 1 
ATOM   11049 H HG22 . ILE C 1 163 ? 17.134  -28.610 30.068  1.00 141.90 ? 163 ILE C HG22 1 
ATOM   11050 H HG23 . ILE C 1 163 ? 17.100  -29.986 29.274  1.00 141.90 ? 163 ILE C HG23 1 
ATOM   11051 H HD11 . ILE C 1 163 ? 13.665  -31.635 31.442  1.00 148.25 ? 163 ILE C HD11 1 
ATOM   11052 H HD12 . ILE C 1 163 ? 14.189  -30.436 32.341  1.00 148.25 ? 163 ILE C HD12 1 
ATOM   11053 H HD13 . ILE C 1 163 ? 14.046  -30.247 30.771  1.00 148.25 ? 163 ILE C HD13 1 
ATOM   11054 N N    . ILE C 1 164 ? 19.184  -28.673 32.242  1.00 124.14 ? 164 ILE C N    1 
ATOM   11055 C CA   . ILE C 1 164 ? 20.115  -27.554 32.107  1.00 122.93 ? 164 ILE C CA   1 
ATOM   11056 C C    . ILE C 1 164 ? 21.528  -28.071 31.875  1.00 124.41 ? 164 ILE C C    1 
ATOM   11057 O O    . ILE C 1 164 ? 22.245  -27.602 30.982  1.00 122.73 ? 164 ILE C O    1 
ATOM   11058 C CB   . ILE C 1 164 ? 20.044  -26.649 33.350  1.00 120.71 ? 164 ILE C CB   1 
ATOM   11059 C CG1  . ILE C 1 164 ? 18.776  -25.792 33.312  1.00 117.60 ? 164 ILE C CG1  1 
ATOM   11060 C CG2  . ILE C 1 164 ? 21.279  -25.769 33.442  1.00 119.95 ? 164 ILE C CG2  1 
ATOM   11061 C CD1  . ILE C 1 164 ? 18.282  -25.365 34.679  1.00 116.51 ? 164 ILE C CD1  1 
ATOM   11062 H H    . ILE C 1 164 ? 18.674  -28.626 32.933  1.00 148.96 ? 164 ILE C H    1 
ATOM   11063 H HA   . ILE C 1 164 ? 19.858  -27.027 31.334  1.00 147.51 ? 164 ILE C HA   1 
ATOM   11064 H HB   . ILE C 1 164 ? 20.011  -27.215 34.137  1.00 144.85 ? 164 ILE C HB   1 
ATOM   11065 H HG12 . ILE C 1 164 ? 18.959  -24.988 32.800  1.00 141.13 ? 164 ILE C HG12 1 
ATOM   11066 H HG13 . ILE C 1 164 ? 18.069  -26.301 32.887  1.00 141.13 ? 164 ILE C HG13 1 
ATOM   11067 H HG21 . ILE C 1 164 ? 21.098  -25.034 34.049  1.00 143.94 ? 164 ILE C HG21 1 
ATOM   11068 H HG22 . ILE C 1 164 ? 22.020  -26.298 33.775  1.00 143.94 ? 164 ILE C HG22 1 
ATOM   11069 H HG23 . ILE C 1 164 ? 21.488  -25.425 32.559  1.00 143.94 ? 164 ILE C HG23 1 
ATOM   11070 H HD11 . ILE C 1 164 ? 18.075  -26.156 35.201  1.00 139.81 ? 164 ILE C HD11 1 
ATOM   11071 H HD12 . ILE C 1 164 ? 18.976  -24.850 35.119  1.00 139.81 ? 164 ILE C HD12 1 
ATOM   11072 H HD13 . ILE C 1 164 ? 17.485  -24.822 34.571  1.00 139.81 ? 164 ILE C HD13 1 
ATOM   11073 N N    . ASP C 1 165 ? 21.948  -29.050 32.678  1.00 125.47 ? 165 ASP C N    1 
ATOM   11074 C CA   . ASP C 1 165 ? 23.274  -29.629 32.499  1.00 126.13 ? 165 ASP C CA   1 
ATOM   11075 C C    . ASP C 1 165 ? 23.397  -30.291 31.133  1.00 126.40 ? 165 ASP C C    1 
ATOM   11076 O O    . ASP C 1 165 ? 24.366  -30.057 30.401  1.00 127.12 ? 165 ASP C O    1 
ATOM   11077 C CB   . ASP C 1 165 ? 23.559  -30.634 33.613  1.00 127.42 ? 165 ASP C CB   1 
ATOM   11078 C CG   . ASP C 1 165 ? 25.020  -31.031 33.675  1.00 128.54 ? 165 ASP C CG   1 
ATOM   11079 O OD1  . ASP C 1 165 ? 25.881  -30.129 33.589  1.00 130.11 ? 165 ASP C OD1  1 
ATOM   11080 O OD2  . ASP C 1 165 ? 25.306  -32.241 33.803  1.00 128.04 ? 165 ASP C OD2  1 
ATOM   11081 H H    . ASP C 1 165 ? 21.490  -29.390 33.322  1.00 150.56 ? 165 ASP C H    1 
ATOM   11082 H HA   . ASP C 1 165 ? 23.936  -28.922 32.555  1.00 151.36 ? 165 ASP C HA   1 
ATOM   11083 H HB2  . ASP C 1 165 ? 23.318  -30.240 34.466  1.00 152.90 ? 165 ASP C HB2  1 
ATOM   11084 H HB3  . ASP C 1 165 ? 23.036  -31.436 33.459  1.00 152.90 ? 165 ASP C HB3  1 
ATOM   11085 N N    . LEU C 1 166 ? 22.416  -31.123 30.771  1.00 127.86 ? 166 LEU C N    1 
ATOM   11086 C CA   . LEU C 1 166 ? 22.460  -31.806 29.482  1.00 125.74 ? 166 LEU C CA   1 
ATOM   11087 C C    . LEU C 1 166 ? 22.629  -30.814 28.338  1.00 123.58 ? 166 LEU C C    1 
ATOM   11088 O O    . LEU C 1 166 ? 23.408  -31.053 27.408  1.00 124.54 ? 166 LEU C O    1 
ATOM   11089 C CB   . LEU C 1 166 ? 21.190  -32.634 29.282  1.00 128.30 ? 166 LEU C CB   1 
ATOM   11090 C CG   . LEU C 1 166 ? 20.989  -33.864 30.168  1.00 133.56 ? 166 LEU C CG   1 
ATOM   11091 C CD1  . LEU C 1 166 ? 19.611  -34.476 29.910  1.00 137.96 ? 166 LEU C CD1  1 
ATOM   11092 C CD2  . LEU C 1 166 ? 22.079  -34.900 29.949  1.00 138.96 ? 166 LEU C CD2  1 
ATOM   11093 H H    . LEU C 1 166 ? 21.724  -31.306 31.248  1.00 153.43 ? 166 LEU C H    1 
ATOM   11094 H HA   . LEU C 1 166 ? 23.219  -32.410 29.476  1.00 150.89 ? 166 LEU C HA   1 
ATOM   11095 H HB2  . LEU C 1 166 ? 20.431  -32.051 29.438  1.00 153.96 ? 166 LEU C HB2  1 
ATOM   11096 H HB3  . LEU C 1 166 ? 21.184  -32.948 28.364  1.00 153.96 ? 166 LEU C HB3  1 
ATOM   11097 H HG   . LEU C 1 166 ? 21.041  -33.586 31.096  1.00 160.27 ? 166 LEU C HG   1 
ATOM   11098 H HD11 . LEU C 1 166 ? 19.498  -35.253 30.481  1.00 165.55 ? 166 LEU C HD11 1 
ATOM   11099 H HD12 . LEU C 1 166 ? 18.929  -33.816 30.111  1.00 165.55 ? 166 LEU C HD12 1 
ATOM   11100 H HD13 . LEU C 1 166 ? 19.552  -34.740 28.978  1.00 165.55 ? 166 LEU C HD13 1 
ATOM   11101 H HD21 . LEU C 1 166 ? 21.862  -35.699 30.455  1.00 166.76 ? 166 LEU C HD21 1 
ATOM   11102 H HD22 . LEU C 1 166 ? 22.128  -35.111 29.003  1.00 166.76 ? 166 LEU C HD22 1 
ATOM   11103 H HD23 . LEU C 1 166 ? 22.926  -34.537 30.251  1.00 166.76 ? 166 LEU C HD23 1 
ATOM   11104 N N    . VAL C 1 167 ? 21.906  -29.693 28.390  1.00 125.76 ? 167 VAL C N    1 
ATOM   11105 C CA   . VAL C 1 167 ? 22.004  -28.700 27.325  1.00 125.25 ? 167 VAL C CA   1 
ATOM   11106 C C    . VAL C 1 167 ? 23.363  -28.018 27.361  1.00 128.68 ? 167 VAL C C    1 
ATOM   11107 O O    . VAL C 1 167 ? 23.996  -27.819 26.322  1.00 131.82 ? 167 VAL C O    1 
ATOM   11108 C CB   . VAL C 1 167 ? 20.856  -27.680 27.435  1.00 117.52 ? 167 VAL C CB   1 
ATOM   11109 C CG1  . VAL C 1 167 ? 21.039  -26.551 26.429  1.00 112.82 ? 167 VAL C CG1  1 
ATOM   11110 C CG2  . VAL C 1 167 ? 19.515  -28.367 27.233  1.00 115.96 ? 167 VAL C CG2  1 
ATOM   11111 H H    . VAL C 1 167 ? 21.360  -29.488 29.022  1.00 150.91 ? 167 VAL C H    1 
ATOM   11112 H HA   . VAL C 1 167 ? 21.917  -29.155 26.473  1.00 150.30 ? 167 VAL C HA   1 
ATOM   11113 H HB   . VAL C 1 167 ? 20.868  -27.291 28.324  1.00 141.02 ? 167 VAL C HB   1 
ATOM   11114 H HG11 . VAL C 1 167 ? 20.286  -25.943 26.495  1.00 135.39 ? 167 VAL C HG11 1 
ATOM   11115 H HG12 . VAL C 1 167 ? 21.863  -26.080 26.629  1.00 135.39 ? 167 VAL C HG12 1 
ATOM   11116 H HG13 . VAL C 1 167 ? 21.082  -26.928 25.536  1.00 135.39 ? 167 VAL C HG13 1 
ATOM   11117 H HG21 . VAL C 1 167 ? 18.808  -27.707 27.305  1.00 139.16 ? 167 VAL C HG21 1 
ATOM   11118 H HG22 . VAL C 1 167 ? 19.499  -28.775 26.353  1.00 139.16 ? 167 VAL C HG22 1 
ATOM   11119 H HG23 . VAL C 1 167 ? 19.403  -29.048 27.915  1.00 139.16 ? 167 VAL C HG23 1 
ATOM   11120 N N    . LYS C 1 168 ? 23.835  -27.652 28.554  1.00 123.94 ? 168 LYS C N    1 
ATOM   11121 C CA   . LYS C 1 168 ? 25.147  -27.024 28.663  1.00 126.11 ? 168 LYS C CA   1 
ATOM   11122 C C    . LYS C 1 168 ? 26.236  -27.900 28.057  1.00 129.11 ? 168 LYS C C    1 
ATOM   11123 O O    . LYS C 1 168 ? 27.237  -27.384 27.549  1.00 131.73 ? 168 LYS C O    1 
ATOM   11124 C CB   . LYS C 1 168 ? 25.459  -26.718 30.129  1.00 126.69 ? 168 LYS C CB   1 
ATOM   11125 C CG   . LYS C 1 168 ? 24.725  -25.499 30.672  1.00 124.56 ? 168 LYS C CG   1 
ATOM   11126 C CD   . LYS C 1 168 ? 24.516  -25.583 32.180  1.00 126.72 ? 168 LYS C CD   1 
ATOM   11127 C CE   . LYS C 1 168 ? 25.729  -25.073 32.951  1.00 126.46 ? 168 LYS C CE   1 
ATOM   11128 N NZ   . LYS C 1 168 ? 26.800  -26.108 33.052  1.00 131.57 ? 168 LYS C NZ   1 
ATOM   11129 H H    . LYS C 1 168 ? 23.423  -27.755 29.301  1.00 148.73 ? 168 LYS C H    1 
ATOM   11130 H HA   . LYS C 1 168 ? 25.137  -26.184 28.178  1.00 151.33 ? 168 LYS C HA   1 
ATOM   11131 H HB2  . LYS C 1 168 ? 25.202  -27.482 30.668  1.00 152.03 ? 168 LYS C HB2  1 
ATOM   11132 H HB3  . LYS C 1 168 ? 26.411  -26.554 30.218  1.00 152.03 ? 168 LYS C HB3  1 
ATOM   11133 H HG2  . LYS C 1 168 ? 25.245  -24.702 30.482  1.00 149.47 ? 168 LYS C HG2  1 
ATOM   11134 H HG3  . LYS C 1 168 ? 23.855  -25.435 30.248  1.00 149.47 ? 168 LYS C HG3  1 
ATOM   11135 H HD2  . LYS C 1 168 ? 23.750  -25.042 32.428  1.00 152.05 ? 168 LYS C HD2  1 
ATOM   11136 H HD3  . LYS C 1 168 ? 24.364  -26.508 32.431  1.00 152.05 ? 168 LYS C HD3  1 
ATOM   11137 H HE2  . LYS C 1 168 ? 26.097  -24.300 32.494  1.00 151.75 ? 168 LYS C HE2  1 
ATOM   11138 H HE3  . LYS C 1 168 ? 25.458  -24.829 33.849  1.00 151.75 ? 168 LYS C HE3  1 
ATOM   11139 H HZ1  . LYS C 1 168 ? 26.482  -26.836 33.455  1.00 157.89 ? 168 LYS C HZ1  1 
ATOM   11140 H HZ2  . LYS C 1 168 ? 27.086  -26.330 32.239  1.00 157.89 ? 168 LYS C HZ2  1 
ATOM   11141 H HZ3  . LYS C 1 168 ? 27.485  -25.793 33.523  1.00 157.89 ? 168 LYS C HZ3  1 
ATOM   11142 N N    . LYS C 1 169 ? 26.063  -29.222 28.095  1.00 128.96 ? 169 LYS C N    1 
ATOM   11143 C CA   . LYS C 1 169 ? 27.046  -30.107 27.477  1.00 135.14 ? 169 LYS C CA   1 
ATOM   11144 C C    . LYS C 1 169 ? 26.945  -30.075 25.959  1.00 137.63 ? 169 LYS C C    1 
ATOM   11145 O O    . LYS C 1 169 ? 27.967  -30.193 25.274  1.00 138.64 ? 169 LYS C O    1 
ATOM   11146 C CB   . LYS C 1 169 ? 26.866  -31.530 28.004  1.00 133.64 ? 169 LYS C CB   1 
ATOM   11147 C CG   . LYS C 1 169 ? 27.983  -32.522 27.630  1.00 140.64 ? 169 LYS C CG   1 
ATOM   11148 C CD   . LYS C 1 169 ? 29.393  -31.978 27.842  1.00 142.15 ? 169 LYS C CD   1 
ATOM   11149 C CE   . LYS C 1 169 ? 30.357  -32.519 26.778  1.00 142.66 ? 169 LYS C CE   1 
ATOM   11150 N NZ   . LYS C 1 169 ? 31.442  -31.541 26.474  1.00 144.34 ? 169 LYS C NZ   1 
ATOM   11151 H H    . LYS C 1 169 ? 25.398  -29.624 28.466  1.00 154.75 ? 169 LYS C H    1 
ATOM   11152 H HA   . LYS C 1 169 ? 27.938  -29.813 27.718  1.00 162.17 ? 169 LYS C HA   1 
ATOM   11153 H HB2  . LYS C 1 169 ? 26.826  -31.493 28.973  1.00 160.37 ? 169 LYS C HB2  1 
ATOM   11154 H HB3  . LYS C 1 169 ? 26.036  -31.884 27.650  1.00 160.37 ? 169 LYS C HB3  1 
ATOM   11155 H HG2  . LYS C 1 169 ? 27.889  -33.318 28.178  1.00 168.77 ? 169 LYS C HG2  1 
ATOM   11156 H HG3  . LYS C 1 169 ? 27.894  -32.753 26.692  1.00 168.77 ? 169 LYS C HG3  1 
ATOM   11157 H HD2  . LYS C 1 169 ? 29.379  -31.010 27.779  1.00 170.58 ? 169 LYS C HD2  1 
ATOM   11158 H HD3  . LYS C 1 169 ? 29.717  -32.249 28.715  1.00 170.58 ? 169 LYS C HD3  1 
ATOM   11159 H HE2  . LYS C 1 169 ? 30.766  -33.337 27.102  1.00 171.20 ? 169 LYS C HE2  1 
ATOM   11160 H HE3  . LYS C 1 169 ? 29.867  -32.694 25.960  1.00 171.20 ? 169 LYS C HE3  1 
ATOM   11161 H HZ1  . LYS C 1 169 ? 31.106  -30.719 26.422  1.00 173.21 ? 169 LYS C HZ1  1 
ATOM   11162 H HZ2  . LYS C 1 169 ? 32.058  -31.561 27.116  1.00 173.21 ? 169 LYS C HZ2  1 
ATOM   11163 H HZ3  . LYS C 1 169 ? 31.827  -31.745 25.698  1.00 173.21 ? 169 LYS C HZ3  1 
ATOM   11164 N N    . TYR C 1 170 ? 25.733  -29.923 25.423  1.00 137.19 ? 170 TYR C N    1 
ATOM   11165 C CA   . TYR C 1 170 ? 25.569  -29.665 23.999  1.00 137.65 ? 170 TYR C CA   1 
ATOM   11166 C C    . TYR C 1 170 ? 26.440  -28.488 23.574  1.00 141.81 ? 170 TYR C C    1 
ATOM   11167 O O    . TYR C 1 170 ? 27.279  -28.607 22.675  1.00 146.21 ? 170 TYR C O    1 
ATOM   11168 C CB   . TYR C 1 170 ? 24.090  -29.397 23.693  1.00 139.61 ? 170 TYR C CB   1 
ATOM   11169 C CG   . TYR C 1 170 ? 23.705  -29.407 22.222  1.00 143.00 ? 170 TYR C CG   1 
ATOM   11170 C CD1  . TYR C 1 170 ? 24.544  -28.864 21.258  1.00 147.20 ? 170 TYR C CD1  1 
ATOM   11171 C CD2  . TYR C 1 170 ? 22.492  -29.942 21.804  1.00 144.60 ? 170 TYR C CD2  1 
ATOM   11172 C CE1  . TYR C 1 170 ? 24.194  -28.865 19.917  1.00 146.70 ? 170 TYR C CE1  1 
ATOM   11173 C CE2  . TYR C 1 170 ? 22.133  -29.948 20.466  1.00 146.85 ? 170 TYR C CE2  1 
ATOM   11174 C CZ   . TYR C 1 170 ? 22.990  -29.406 19.528  1.00 146.60 ? 170 TYR C CZ   1 
ATOM   11175 O OH   . TYR C 1 170 ? 22.650  -29.402 18.195  1.00 146.24 ? 170 TYR C OH   1 
ATOM   11176 H H    . TYR C 1 170 ? 24.995  -29.964 25.863  1.00 164.63 ? 170 TYR C H    1 
ATOM   11177 H HA   . TYR C 1 170 ? 25.841  -30.445 23.490  1.00 165.19 ? 170 TYR C HA   1 
ATOM   11178 H HB2  . TYR C 1 170 ? 23.560  -30.081 24.133  1.00 167.54 ? 170 TYR C HB2  1 
ATOM   11179 H HB3  . TYR C 1 170 ? 23.860  -28.523 24.045  1.00 167.54 ? 170 TYR C HB3  1 
ATOM   11180 H HD1  . TYR C 1 170 ? 25.357  -28.493 21.517  1.00 176.64 ? 170 TYR C HD1  1 
ATOM   11181 H HD2  . TYR C 1 170 ? 21.911  -30.303 22.434  1.00 173.52 ? 170 TYR C HD2  1 
ATOM   11182 H HE1  . TYR C 1 170 ? 24.770  -28.502 19.283  1.00 176.04 ? 170 TYR C HE1  1 
ATOM   11183 H HE2  . TYR C 1 170 ? 21.320  -30.314 20.202  1.00 176.22 ? 170 TYR C HE2  1 
ATOM   11184 H HH   . TYR C 1 170 ? 21.881  -29.723 18.093  1.00 175.49 ? 170 TYR C HH   1 
ATOM   11185 N N    . LEU C 1 171 ? 26.257  -27.341 24.227  1.00 139.74 ? 171 LEU C N    1 
ATOM   11186 C CA   . LEU C 1 171 ? 26.895  -26.100 23.810  1.00 138.98 ? 171 LEU C CA   1 
ATOM   11187 C C    . LEU C 1 171 ? 28.412  -26.123 23.965  1.00 141.45 ? 171 LEU C C    1 
ATOM   11188 O O    . LEU C 1 171 ? 29.062  -25.136 23.602  1.00 141.36 ? 171 LEU C O    1 
ATOM   11189 C CB   . LEU C 1 171 ? 26.320  -24.926 24.604  1.00 135.31 ? 171 LEU C CB   1 
ATOM   11190 C CG   . LEU C 1 171 ? 24.875  -24.506 24.324  1.00 129.63 ? 171 LEU C CG   1 
ATOM   11191 C CD1  . LEU C 1 171 ? 24.636  -24.248 22.843  1.00 130.85 ? 171 LEU C CD1  1 
ATOM   11192 C CD2  . LEU C 1 171 ? 23.895  -25.541 24.853  1.00 127.61 ? 171 LEU C CD2  1 
ATOM   11193 H H    . LEU C 1 171 ? 25.762  -27.257 24.925  1.00 167.68 ? 171 LEU C H    1 
ATOM   11194 H HA   . LEU C 1 171 ? 26.697  -25.958 22.871  1.00 166.78 ? 171 LEU C HA   1 
ATOM   11195 H HB2  . LEU C 1 171 ? 26.364  -25.158 25.545  1.00 162.37 ? 171 LEU C HB2  1 
ATOM   11196 H HB3  . LEU C 1 171 ? 26.875  -24.151 24.427  1.00 162.37 ? 171 LEU C HB3  1 
ATOM   11197 H HG   . LEU C 1 171 ? 24.715  -23.670 24.790  1.00 155.55 ? 171 LEU C HG   1 
ATOM   11198 H HD11 . LEU C 1 171 ? 23.746  -23.879 22.726  1.00 157.01 ? 171 LEU C HD11 1 
ATOM   11199 H HD12 . LEU C 1 171 ? 25.299  -23.618 22.520  1.00 157.01 ? 171 LEU C HD12 1 
ATOM   11200 H HD13 . LEU C 1 171 ? 24.712  -25.086 22.360  1.00 157.01 ? 171 LEU C HD13 1 
ATOM   11201 H HD21 . LEU C 1 171 ? 22.990  -25.243 24.668  1.00 153.13 ? 171 LEU C HD21 1 
ATOM   11202 H HD22 . LEU C 1 171 ? 24.061  -26.388 24.411  1.00 153.13 ? 171 LEU C HD22 1 
ATOM   11203 H HD23 . LEU C 1 171 ? 24.022  -25.636 25.810  1.00 153.13 ? 171 LEU C HD23 1 
ATOM   11204 N N    . SER C 1 172 ? 28.995  -27.205 24.487  1.00 143.01 ? 172 SER C N    1 
ATOM   11205 C CA   . SER C 1 172 ? 30.446  -27.258 24.632  1.00 143.86 ? 172 SER C CA   1 
ATOM   11206 C C    . SER C 1 172 ? 31.136  -27.106 23.281  1.00 149.42 ? 172 SER C C    1 
ATOM   11207 O O    . SER C 1 172 ? 32.053  -26.290 23.127  1.00 149.09 ? 172 SER C O    1 
ATOM   11208 C CB   . SER C 1 172 ? 30.857  -28.569 25.302  1.00 141.81 ? 172 SER C CB   1 
ATOM   11209 O OG   . SER C 1 172 ? 30.912  -29.627 24.363  1.00 145.40 ? 172 SER C OG   1 
ATOM   11210 H H    . SER C 1 172 ? 28.579  -27.907 24.758  1.00 171.61 ? 172 SER C H    1 
ATOM   11211 H HA   . SER C 1 172 ? 30.731  -26.527 25.202  1.00 172.63 ? 172 SER C HA   1 
ATOM   11212 H HB2  . SER C 1 172 ? 31.734  -28.456 25.701  1.00 170.18 ? 172 SER C HB2  1 
ATOM   11213 H HB3  . SER C 1 172 ? 30.206  -28.789 25.986  1.00 170.18 ? 172 SER C HB3  1 
ATOM   11214 H HG   . SER C 1 172 ? 30.158  -29.738 24.010  1.00 174.48 ? 172 SER C HG   1 
ATOM   11215 N N    . ASN C 1 173 ? 30.701  -27.879 22.285  1.00 155.23 ? 173 ASN C N    1 
ATOM   11216 C CA   . ASN C 1 173 ? 31.313  -27.853 20.963  1.00 154.91 ? 173 ASN C CA   1 
ATOM   11217 C C    . ASN C 1 173 ? 30.797  -26.722 20.082  1.00 156.27 ? 173 ASN C C    1 
ATOM   11218 O O    . ASN C 1 173 ? 31.182  -26.653 18.909  1.00 160.72 ? 173 ASN C O    1 
ATOM   11219 C CB   . ASN C 1 173 ? 31.080  -29.192 20.256  1.00 157.86 ? 173 ASN C CB   1 
ATOM   11220 C CG   . ASN C 1 173 ? 29.608  -29.526 20.109  1.00 160.58 ? 173 ASN C CG   1 
ATOM   11221 O OD1  . ASN C 1 173 ? 28.923  -28.997 19.233  1.00 158.33 ? 173 ASN C OD1  1 
ATOM   11222 N ND2  . ASN C 1 173 ? 29.112  -30.405 20.972  1.00 162.21 ? 173 ASN C ND2  1 
ATOM   11223 H H    . ASN C 1 173 ? 30.046  -28.432 22.354  1.00 186.27 ? 173 ASN C H    1 
ATOM   11224 H HA   . ASN C 1 173 ? 32.268  -27.727 21.073  1.00 185.89 ? 173 ASN C HA   1 
ATOM   11225 H HB2  . ASN C 1 173 ? 31.470  -29.152 19.368  1.00 189.42 ? 173 ASN C HB2  1 
ATOM   11226 H HB3  . ASN C 1 173 ? 31.499  -29.899 20.770  1.00 189.42 ? 173 ASN C HB3  1 
ATOM   11227 H HD21 . ASN C 1 173 ? 29.620  -30.751 21.573  1.00 194.65 ? 173 ASN C HD21 1 
ATOM   11228 H HD22 . ASN C 1 173 ? 28.282  -30.627 20.930  1.00 194.65 ? 173 ASN C HD22 1 
ATOM   11229 N N    . GLU C 1 174 ? 29.945  -25.842 20.606  1.00 150.34 ? 174 GLU C N    1 
ATOM   11230 C CA   . GLU C 1 174 ? 29.426  -24.705 19.855  1.00 147.19 ? 174 GLU C CA   1 
ATOM   11231 C C    . GLU C 1 174 ? 29.720  -23.429 20.630  1.00 145.07 ? 174 GLU C C    1 
ATOM   11232 O O    . GLU C 1 174 ? 29.300  -23.291 21.784  1.00 143.30 ? 174 GLU C O    1 
ATOM   11233 C CB   . GLU C 1 174 ? 27.922  -24.841 19.612  1.00 143.91 ? 174 GLU C CB   1 
ATOM   11234 C CG   . GLU C 1 174 ? 27.463  -26.245 19.282  1.00 145.57 ? 174 GLU C CG   1 
ATOM   11235 C CD   . GLU C 1 174 ? 26.091  -26.258 18.644  1.00 142.08 ? 174 GLU C CD   1 
ATOM   11236 O OE1  . GLU C 1 174 ? 25.333  -25.287 18.850  1.00 136.91 ? 174 GLU C OE1  1 
ATOM   11237 O OE2  . GLU C 1 174 ? 25.773  -27.234 17.934  1.00 146.16 ? 174 GLU C OE2  1 
ATOM   11238 H H    . GLU C 1 174 ? 29.648  -25.886 21.411  1.00 180.41 ? 174 GLU C H    1 
ATOM   11239 H HA   . GLU C 1 174 ? 29.875  -24.659 18.997  1.00 176.62 ? 174 GLU C HA   1 
ATOM   11240 H HB2  . GLU C 1 174 ? 27.453  -24.560 20.414  1.00 172.69 ? 174 GLU C HB2  1 
ATOM   11241 H HB3  . GLU C 1 174 ? 27.677  -24.270 18.867  1.00 172.69 ? 174 GLU C HB3  1 
ATOM   11242 H HG2  . GLU C 1 174 ? 28.090  -26.648 18.661  1.00 174.68 ? 174 GLU C HG2  1 
ATOM   11243 H HG3  . GLU C 1 174 ? 27.423  -26.768 20.098  1.00 174.68 ? 174 GLU C HG3  1 
ATOM   11244 N N    . GLU C 1 175 ? 30.436  -22.502 19.999  1.00 141.68 ? 175 GLU C N    1 
ATOM   11245 C CA   . GLU C 1 175 ? 30.708  -21.211 20.621  1.00 141.77 ? 175 GLU C CA   1 
ATOM   11246 C C    . GLU C 1 175 ? 29.396  -20.482 20.882  1.00 141.44 ? 175 GLU C C    1 
ATOM   11247 O O    . GLU C 1 175 ? 28.625  -20.218 19.954  1.00 141.51 ? 175 GLU C O    1 
ATOM   11248 C CB   . GLU C 1 175 ? 31.624  -20.380 19.726  1.00 141.29 ? 175 GLU C CB   1 
ATOM   11249 C CG   . GLU C 1 175 ? 31.867  -18.949 20.204  1.00 142.99 ? 175 GLU C CG   1 
ATOM   11250 C CD   . GLU C 1 175 ? 31.827  -18.801 21.715  1.00 142.22 ? 175 GLU C CD   1 
ATOM   11251 O OE1  . GLU C 1 175 ? 32.706  -19.370 22.397  1.00 143.14 ? 175 GLU C OE1  1 
ATOM   11252 O OE2  . GLU C 1 175 ? 30.911  -18.116 22.218  1.00 141.40 ? 175 GLU C OE2  1 
ATOM   11253 H H    . GLU C 1 175 ? 30.775  -22.596 19.214  1.00 170.01 ? 175 GLU C H    1 
ATOM   11254 H HA   . GLU C 1 175 ? 31.163  -21.344 21.468  1.00 170.12 ? 175 GLU C HA   1 
ATOM   11255 H HB2  . GLU C 1 175 ? 32.487  -20.821 19.676  1.00 169.54 ? 175 GLU C HB2  1 
ATOM   11256 H HB3  . GLU C 1 175 ? 31.226  -20.329 18.843  1.00 169.54 ? 175 GLU C HB3  1 
ATOM   11257 H HG2  . GLU C 1 175 ? 32.742  -18.662 19.900  1.00 171.59 ? 175 GLU C HG2  1 
ATOM   11258 H HG3  . GLU C 1 175 ? 31.181  -18.374 19.831  1.00 171.59 ? 175 GLU C HG3  1 
ATOM   11259 N N    . TYR C 1 176 ? 29.144  -20.161 22.150  1.00 141.27 ? 176 TYR C N    1 
ATOM   11260 C CA   . TYR C 1 176 ? 27.888  -19.550 22.569  1.00 139.18 ? 176 TYR C CA   1 
ATOM   11261 C C    . TYR C 1 176 ? 28.192  -18.433 23.553  1.00 136.45 ? 176 TYR C C    1 
ATOM   11262 O O    . TYR C 1 176 ? 28.763  -18.680 24.619  1.00 136.06 ? 176 TYR C O    1 
ATOM   11263 C CB   . TYR C 1 176 ? 26.950  -20.591 23.198  1.00 138.97 ? 176 TYR C CB   1 
ATOM   11264 C CG   . TYR C 1 176 ? 27.462  -21.219 24.483  1.00 137.88 ? 176 TYR C CG   1 
ATOM   11265 C CD1  . TYR C 1 176 ? 28.691  -21.866 24.524  1.00 134.96 ? 176 TYR C CD1  1 
ATOM   11266 C CD2  . TYR C 1 176 ? 26.714  -21.165 25.656  1.00 137.90 ? 176 TYR C CD2  1 
ATOM   11267 C CE1  . TYR C 1 176 ? 29.164  -22.434 25.689  1.00 131.50 ? 176 TYR C CE1  1 
ATOM   11268 C CE2  . TYR C 1 176 ? 27.180  -21.733 26.827  1.00 136.52 ? 176 TYR C CE2  1 
ATOM   11269 C CZ   . TYR C 1 176 ? 28.406  -22.366 26.838  1.00 135.00 ? 176 TYR C CZ   1 
ATOM   11270 O OH   . TYR C 1 176 ? 28.876  -22.934 28.000  1.00 133.54 ? 176 TYR C OH   1 
ATOM   11271 H H    . TYR C 1 176 ? 29.696  -20.290 22.797  1.00 169.52 ? 176 TYR C H    1 
ATOM   11272 H HA   . TYR C 1 176 ? 27.442  -19.163 21.800  1.00 167.02 ? 176 TYR C HA   1 
ATOM   11273 H HB2  . TYR C 1 176 ? 26.105  -20.160 23.401  1.00 166.77 ? 176 TYR C HB2  1 
ATOM   11274 H HB3  . TYR C 1 176 ? 26.813  -21.307 22.559  1.00 166.77 ? 176 TYR C HB3  1 
ATOM   11275 H HD1  . TYR C 1 176 ? 29.205  -21.917 23.751  1.00 165.47 ? 176 TYR C HD1  1 
ATOM   11276 H HD2  . TYR C 1 176 ? 25.887  -20.739 25.651  1.00 161.95 ? 176 TYR C HD2  1 
ATOM   11277 H HE1  . TYR C 1 176 ? 29.990  -22.861 25.700  1.00 163.82 ? 176 TYR C HE1  1 
ATOM   11278 H HE2  . TYR C 1 176 ? 26.670  -21.689 27.604  1.00 157.80 ? 176 TYR C HE2  1 
ATOM   11279 H HH   . TYR C 1 176 ? 29.619  -23.301 27.860  1.00 160.25 ? 176 TYR C HH   1 
ATOM   11280 N N    . SER C 1 177 ? 27.827  -17.203 23.185  1.00 139.43 ? 177 SER C N    1 
ATOM   11281 C CA   . SER C 1 177 ? 27.890  -16.098 24.132  1.00 137.47 ? 177 SER C CA   1 
ATOM   11282 C C    . SER C 1 177 ? 26.812  -16.212 25.201  1.00 139.82 ? 177 SER C C    1 
ATOM   11283 O O    . SER C 1 177 ? 26.965  -15.640 26.284  1.00 137.87 ? 177 SER C O    1 
ATOM   11284 C CB   . SER C 1 177 ? 27.756  -14.766 23.394  1.00 132.74 ? 177 SER C CB   1 
ATOM   11285 O OG   . SER C 1 177 ? 27.233  -13.759 24.242  1.00 126.89 ? 177 SER C OG   1 
ATOM   11286 H H    . SER C 1 177 ? 27.542  -16.988 22.402  1.00 167.32 ? 177 SER C H    1 
ATOM   11287 H HA   . SER C 1 177 ? 28.755  -16.105 24.570  1.00 164.97 ? 177 SER C HA   1 
ATOM   11288 H HB2  . SER C 1 177 ? 28.632  -14.490 23.082  1.00 159.29 ? 177 SER C HB2  1 
ATOM   11289 H HB3  . SER C 1 177 ? 27.157  -14.883 22.640  1.00 159.29 ? 177 SER C HB3  1 
ATOM   11290 H HG   . SER C 1 177 ? 27.171  -13.033 23.822  1.00 152.27 ? 177 SER C HG   1 
ATOM   11291 N N    . ALA C 1 178 ? 25.736  -16.944 24.922  1.00 152.87 ? 178 ALA C N    1 
ATOM   11292 C CA   . ALA C 1 178 ? 24.642  -17.128 25.868  1.00 149.83 ? 178 ALA C CA   1 
ATOM   11293 C C    . ALA C 1 178 ? 23.684  -18.162 25.291  1.00 149.99 ? 178 ALA C C    1 
ATOM   11294 O O    . ALA C 1 178 ? 23.785  -18.549 24.124  1.00 151.78 ? 178 ALA C O    1 
ATOM   11295 C CB   . ALA C 1 178 ? 23.918  -15.810 26.153  1.00 145.70 ? 178 ALA C CB   1 
ATOM   11296 H H    . ALA C 1 178 ? 25.614  -17.353 24.175  1.00 183.44 ? 178 ALA C H    1 
ATOM   11297 H HA   . ALA C 1 178 ? 24.995  -17.470 26.704  1.00 179.79 ? 178 ALA C HA   1 
ATOM   11298 H HB1  . ALA C 1 178 ? 23.193  -15.976 26.776  1.00 174.83 ? 178 ALA C HB1  1 
ATOM   11299 H HB2  . ALA C 1 178 ? 24.547  -15.180 26.538  1.00 174.83 ? 178 ALA C HB2  1 
ATOM   11300 H HB3  . ALA C 1 178 ? 23.564  -15.457 25.321  1.00 174.83 ? 178 ALA C HB3  1 
ATOM   11301 N N    . PHE C 1 179 ? 22.751  -18.609 26.130  1.00 129.83 ? 179 PHE C N    1 
ATOM   11302 C CA   . PHE C 1 179 ? 21.729  -19.558 25.706  1.00 122.91 ? 179 PHE C CA   1 
ATOM   11303 C C    . PHE C 1 179 ? 20.601  -19.548 26.727  1.00 116.85 ? 179 PHE C C    1 
ATOM   11304 O O    . PHE C 1 179 ? 20.776  -19.118 27.869  1.00 116.60 ? 179 PHE C O    1 
ATOM   11305 C CB   . PHE C 1 179 ? 22.311  -20.970 25.530  1.00 118.39 ? 179 PHE C CB   1 
ATOM   11306 C CG   . PHE C 1 179 ? 22.392  -21.768 26.800  1.00 116.07 ? 179 PHE C CG   1 
ATOM   11307 C CD1  . PHE C 1 179 ? 21.287  -22.458 27.275  1.00 113.11 ? 179 PHE C CD1  1 
ATOM   11308 C CD2  . PHE C 1 179 ? 23.577  -21.844 27.509  1.00 119.02 ? 179 PHE C CD2  1 
ATOM   11309 C CE1  . PHE C 1 179 ? 21.359  -23.191 28.442  1.00 109.89 ? 179 PHE C CE1  1 
ATOM   11310 C CE2  . PHE C 1 179 ? 23.657  -22.582 28.673  1.00 116.13 ? 179 PHE C CE2  1 
ATOM   11311 C CZ   . PHE C 1 179 ? 22.546  -23.255 29.141  1.00 112.12 ? 179 PHE C CZ   1 
ATOM   11312 H H    . PHE C 1 179 ? 22.689  -18.374 26.955  1.00 155.80 ? 179 PHE C H    1 
ATOM   11313 H HA   . PHE C 1 179 ? 21.361  -19.279 24.853  1.00 147.50 ? 179 PHE C HA   1 
ATOM   11314 H HB2  . PHE C 1 179 ? 21.750  -21.461 24.909  1.00 142.07 ? 179 PHE C HB2  1 
ATOM   11315 H HB3  . PHE C 1 179 ? 23.210  -20.893 25.174  1.00 142.07 ? 179 PHE C HB3  1 
ATOM   11316 H HD1  . PHE C 1 179 ? 20.487  -22.427 26.801  1.00 135.73 ? 179 PHE C HD1  1 
ATOM   11317 H HD2  . PHE C 1 179 ? 24.329  -21.393 27.199  1.00 142.83 ? 179 PHE C HD2  1 
ATOM   11318 H HE1  . PHE C 1 179 ? 20.609  -23.642 28.757  1.00 131.88 ? 179 PHE C HE1  1 
ATOM   11319 H HE2  . PHE C 1 179 ? 24.459  -22.627 29.142  1.00 139.36 ? 179 PHE C HE2  1 
ATOM   11320 H HZ   . PHE C 1 179 ? 22.597  -23.751 29.926  1.00 134.55 ? 179 PHE C HZ   1 
ATOM   11321 N N    . GLY C 1 180 ? 19.437  -20.029 26.293  1.00 114.17 ? 180 GLY C N    1 
ATOM   11322 C CA   . GLY C 1 180 ? 18.263  -20.037 27.138  1.00 108.87 ? 180 GLY C CA   1 
ATOM   11323 C C    . GLY C 1 180 ? 17.497  -21.336 26.987  1.00 105.80 ? 180 GLY C C    1 
ATOM   11324 O O    . GLY C 1 180 ? 17.669  -22.079 26.019  1.00 105.21 ? 180 GLY C O    1 
ATOM   11325 H H    . GLY C 1 180 ? 19.308  -20.356 25.508  1.00 137.01 ? 180 GLY C H    1 
ATOM   11326 H HA2  . GLY C 1 180 ? 18.527  -19.937 28.066  1.00 130.64 ? 180 GLY C HA2  1 
ATOM   11327 H HA3  . GLY C 1 180 ? 17.680  -19.302 26.894  1.00 130.64 ? 180 GLY C HA3  1 
ATOM   11328 N N    . ILE C 1 181 ? 16.641  -21.596 27.974  1.00 104.14 ? 181 ILE C N    1 
ATOM   11329 C CA   . ILE C 1 181 ? 15.858  -22.826 28.041  1.00 102.06 ? 181 ILE C CA   1 
ATOM   11330 C C    . ILE C 1 181 ? 14.444  -22.466 28.463  1.00 99.84  ? 181 ILE C C    1 
ATOM   11331 O O    . ILE C 1 181 ? 14.230  -21.988 29.582  1.00 99.41  ? 181 ILE C O    1 
ATOM   11332 C CB   . ILE C 1 181 ? 16.469  -23.849 29.024  1.00 101.65 ? 181 ILE C CB   1 
ATOM   11333 C CG1  . ILE C 1 181 ? 17.825  -24.331 28.501  1.00 102.73 ? 181 ILE C CG1  1 
ATOM   11334 C CG2  . ILE C 1 181 ? 15.517  -25.015 29.233  1.00 101.11 ? 181 ILE C CG2  1 
ATOM   11335 C CD1  . ILE C 1 181 ? 18.566  -25.254 29.448  1.00 109.27 ? 181 ILE C CD1  1 
ATOM   11336 H H    . ILE C 1 181 ? 16.493  -21.062 28.631  1.00 124.96 ? 181 ILE C H    1 
ATOM   11337 H HA   . ILE C 1 181 ? 15.818  -23.231 27.160  1.00 122.47 ? 181 ILE C HA   1 
ATOM   11338 H HB   . ILE C 1 181 ? 16.608  -23.417 29.881  1.00 121.99 ? 181 ILE C HB   1 
ATOM   11339 H HG12 . ILE C 1 181 ? 17.683  -24.813 27.671  1.00 123.27 ? 181 ILE C HG12 1 
ATOM   11340 H HG13 . ILE C 1 181 ? 18.389  -23.557 28.343  1.00 123.27 ? 181 ILE C HG13 1 
ATOM   11341 H HG21 . ILE C 1 181 ? 15.969  -25.703 29.747  1.00 121.33 ? 181 ILE C HG21 1 
ATOM   11342 H HG22 . ILE C 1 181 ? 14.735  -24.702 29.713  1.00 121.33 ? 181 ILE C HG22 1 
ATOM   11343 H HG23 . ILE C 1 181 ? 15.255  -25.367 28.368  1.00 121.33 ? 181 ILE C HG23 1 
ATOM   11344 H HD11 . ILE C 1 181 ? 19.477  -25.364 29.133  1.00 131.13 ? 181 ILE C HD11 1 
ATOM   11345 H HD12 . ILE C 1 181 ? 18.568  -24.862 30.335  1.00 131.13 ? 181 ILE C HD12 1 
ATOM   11346 H HD13 . ILE C 1 181 ? 18.117  -26.114 29.467  1.00 131.13 ? 181 ILE C HD13 1 
ATOM   11347 N N    . MET C 1 182 ? 13.483  -22.693 27.570  1.00 99.48  ? 182 MET C N    1 
ATOM   11348 C CA   . MET C 1 182 ? 12.082  -22.361 27.813  1.00 97.26  ? 182 MET C CA   1 
ATOM   11349 C C    . MET C 1 182 ? 11.388  -23.608 28.356  1.00 99.60  ? 182 MET C C    1 
ATOM   11350 O O    . MET C 1 182 ? 11.023  -24.508 27.596  1.00 104.00 ? 182 MET C O    1 
ATOM   11351 C CB   . MET C 1 182 ? 11.411  -21.876 26.531  1.00 100.25 ? 182 MET C CB   1 
ATOM   11352 C CG   . MET C 1 182 ? 11.695  -20.433 26.109  1.00 93.74  ? 182 MET C CG   1 
ATOM   11353 S SD   . MET C 1 182 ? 11.839  -19.218 27.432  1.00 95.71  ? 182 MET C SD   1 
ATOM   11354 C CE   . MET C 1 182 ? 13.616  -18.993 27.511  1.00 98.54  ? 182 MET C CE   1 
ATOM   11355 H H    . MET C 1 182 ? 13.622  -23.047 26.798  1.00 119.37 ? 182 MET C H    1 
ATOM   11356 H HA   . MET C 1 182 ? 12.036  -21.649 28.470  1.00 116.71 ? 182 MET C HA   1 
ATOM   11357 H HB2  . MET C 1 182 ? 11.706  -22.447 25.804  1.00 120.30 ? 182 MET C HB2  1 
ATOM   11358 H HB3  . MET C 1 182 ? 10.451  -21.955 26.646  1.00 120.30 ? 182 MET C HB3  1 
ATOM   11359 H HG2  . MET C 1 182 ? 12.533  -20.421 25.621  1.00 112.49 ? 182 MET C HG2  1 
ATOM   11360 H HG3  . MET C 1 182 ? 10.971  -20.140 25.534  1.00 112.49 ? 182 MET C HG3  1 
ATOM   11361 H HE1  . MET C 1 182 ? 13.834  -18.472 28.300  1.00 118.24 ? 182 MET C HE1  1 
ATOM   11362 H HE2  . MET C 1 182 ? 14.042  -19.863 27.561  1.00 118.24 ? 182 MET C HE2  1 
ATOM   11363 H HE3  . MET C 1 182 ? 13.911  -18.525 26.714  1.00 118.24 ? 182 MET C HE3  1 
ATOM   11364 N N    . PHE C 1 183 ? 11.210  -23.667 29.675  1.00 100.89 ? 183 PHE C N    1 
ATOM   11365 C CA   . PHE C 1 183 ? 10.510  -24.779 30.321  1.00 100.18 ? 183 PHE C CA   1 
ATOM   11366 C C    . PHE C 1 183 ? 9.012   -24.558 30.153  1.00 100.41 ? 183 PHE C C    1 
ATOM   11367 O O    . PHE C 1 183 ? 8.398   -23.791 30.897  1.00 101.57 ? 183 PHE C O    1 
ATOM   11368 C CB   . PHE C 1 183 ? 10.895  -24.878 31.792  1.00 99.06  ? 183 PHE C CB   1 
ATOM   11369 C CG   . PHE C 1 183 ? 12.305  -25.339 32.017  1.00 99.51  ? 183 PHE C CG   1 
ATOM   11370 C CD1  . PHE C 1 183 ? 12.634  -26.679 31.900  1.00 103.59 ? 183 PHE C CD1  1 
ATOM   11371 C CD2  . PHE C 1 183 ? 13.303  -24.433 32.331  1.00 99.40  ? 183 PHE C CD2  1 
ATOM   11372 C CE1  . PHE C 1 183 ? 13.931  -27.108 32.097  1.00 106.20 ? 183 PHE C CE1  1 
ATOM   11373 C CE2  . PHE C 1 183 ? 14.603  -24.854 32.529  1.00 101.61 ? 183 PHE C CE2  1 
ATOM   11374 C CZ   . PHE C 1 183 ? 14.917  -26.194 32.415  1.00 106.70 ? 183 PHE C CZ   1 
ATOM   11375 H H    . PHE C 1 183 ? 11.488  -23.068 30.226  1.00 121.07 ? 183 PHE C H    1 
ATOM   11376 H HA   . PHE C 1 183 ? 10.753  -25.613 29.888  1.00 120.22 ? 183 PHE C HA   1 
ATOM   11377 H HB2  . PHE C 1 183 ? 10.802  -24.002 32.199  1.00 118.87 ? 183 PHE C HB2  1 
ATOM   11378 H HB3  . PHE C 1 183 ? 10.304  -25.511 32.228  1.00 118.87 ? 183 PHE C HB3  1 
ATOM   11379 H HD1  . PHE C 1 183 ? 11.973  -27.297 31.687  1.00 124.31 ? 183 PHE C HD1  1 
ATOM   11380 H HD2  . PHE C 1 183 ? 13.096  -23.529 32.410  1.00 119.28 ? 183 PHE C HD2  1 
ATOM   11381 H HE1  . PHE C 1 183 ? 14.141  -28.010 32.016  1.00 127.44 ? 183 PHE C HE1  1 
ATOM   11382 H HE2  . PHE C 1 183 ? 15.266  -24.236 32.739  1.00 121.94 ? 183 PHE C HE2  1 
ATOM   11383 H HZ   . PHE C 1 183 ? 15.791  -26.480 32.552  1.00 128.04 ? 183 PHE C HZ   1 
ATOM   11384 N N    . PHE C 1 184 ? 8.416   -25.245 29.183  1.00 105.06 ? 184 PHE C N    1 
ATOM   11385 C CA   . PHE C 1 184 ? 7.055   -24.973 28.739  1.00 106.02 ? 184 PHE C CA   1 
ATOM   11386 C C    . PHE C 1 184 ? 6.102   -26.052 29.235  1.00 107.58 ? 184 PHE C C    1 
ATOM   11387 O O    . PHE C 1 184 ? 6.347   -27.246 29.037  1.00 107.67 ? 184 PHE C O    1 
ATOM   11388 C CB   . PHE C 1 184 ? 7.009   -24.880 27.209  1.00 103.23 ? 184 PHE C CB   1 
ATOM   11389 C CG   . PHE C 1 184 ? 5.626   -24.944 26.634  1.00 105.27 ? 184 PHE C CG   1 
ATOM   11390 C CD1  . PHE C 1 184 ? 4.623   -24.120 27.117  1.00 103.04 ? 184 PHE C CD1  1 
ATOM   11391 C CD2  . PHE C 1 184 ? 5.330   -25.826 25.603  1.00 106.94 ? 184 PHE C CD2  1 
ATOM   11392 C CE1  . PHE C 1 184 ? 3.348   -24.178 26.586  1.00 106.23 ? 184 PHE C CE1  1 
ATOM   11393 C CE2  . PHE C 1 184 ? 4.056   -25.888 25.068  1.00 103.04 ? 184 PHE C CE2  1 
ATOM   11394 C CZ   . PHE C 1 184 ? 3.065   -25.061 25.559  1.00 104.60 ? 184 PHE C CZ   1 
ATOM   11395 H H    . PHE C 1 184 ? 8.791   -25.891 28.757  1.00 126.07 ? 184 PHE C H    1 
ATOM   11396 H HA   . PHE C 1 184 ? 6.755   -24.133 29.120  1.00 127.22 ? 184 PHE C HA   1 
ATOM   11397 H HB2  . PHE C 1 184 ? 7.403   -24.037 26.937  1.00 123.88 ? 184 PHE C HB2  1 
ATOM   11398 H HB3  . PHE C 1 184 ? 7.517   -25.619 26.838  1.00 123.88 ? 184 PHE C HB3  1 
ATOM   11399 H HD1  . PHE C 1 184 ? 4.809   -23.523 27.805  1.00 123.65 ? 184 PHE C HD1  1 
ATOM   11400 H HD2  . PHE C 1 184 ? 5.996   -26.382 25.268  1.00 128.33 ? 184 PHE C HD2  1 
ATOM   11401 H HE1  . PHE C 1 184 ? 2.680   -23.623 26.919  1.00 127.47 ? 184 PHE C HE1  1 
ATOM   11402 H HE2  . PHE C 1 184 ? 3.868   -26.484 24.380  1.00 123.65 ? 184 PHE C HE2  1 
ATOM   11403 H HZ   . PHE C 1 184 ? 2.208   -25.097 25.199  1.00 125.52 ? 184 PHE C HZ   1 
ATOM   11404 N N    . ASP C 1 185 ? 5.011   -25.621 29.867  1.00 107.17 ? 185 ASP C N    1 
ATOM   11405 C CA   . ASP C 1 185 ? 3.955   -26.498 30.362  1.00 108.88 ? 185 ASP C CA   1 
ATOM   11406 C C    . ASP C 1 185 ? 2.696   -26.231 29.547  1.00 111.43 ? 185 ASP C C    1 
ATOM   11407 O O    . ASP C 1 185 ? 2.123   -25.139 29.628  1.00 112.57 ? 185 ASP C O    1 
ATOM   11408 C CB   . ASP C 1 185 ? 3.715   -26.252 31.853  1.00 113.07 ? 185 ASP C CB   1 
ATOM   11409 C CG   . ASP C 1 185 ? 2.440   -26.909 32.377  1.00 117.32 ? 185 ASP C CG   1 
ATOM   11410 O OD1  . ASP C 1 185 ? 1.418   -26.957 31.662  1.00 118.21 ? 185 ASP C OD1  1 
ATOM   11411 O OD2  . ASP C 1 185 ? 2.452   -27.360 33.541  1.00 122.93 ? 185 ASP C OD2  1 
ATOM   11412 H H    . ASP C 1 185 ? 4.856   -24.790 30.027  1.00 128.60 ? 185 ASP C H    1 
ATOM   11413 H HA   . ASP C 1 185 ? 4.201   -27.429 30.246  1.00 130.66 ? 185 ASP C HA   1 
ATOM   11414 H HB2  . ASP C 1 185 ? 4.463   -26.613 32.355  1.00 135.68 ? 185 ASP C HB2  1 
ATOM   11415 H HB3  . ASP C 1 185 ? 3.643   -25.297 32.007  1.00 135.68 ? 185 ASP C HB3  1 
ATOM   11416 N N    . SER C 1 186 ? 2.253   -27.240 28.790  1.00 112.24 ? 186 SER C N    1 
ATOM   11417 C CA   . SER C 1 186 ? 1.126   -27.046 27.884  1.00 113.18 ? 186 SER C CA   1 
ATOM   11418 C C    . SER C 1 186 ? -0.196  -26.899 28.628  1.00 116.16 ? 186 SER C C    1 
ATOM   11419 O O    . SER C 1 186 ? -1.100  -26.206 28.147  1.00 116.84 ? 186 SER C O    1 
ATOM   11420 C CB   . SER C 1 186 ? 1.038   -28.215 26.904  1.00 118.37 ? 186 SER C CB   1 
ATOM   11421 O OG   . SER C 1 186 ? 0.051   -29.148 27.311  1.00 124.74 ? 186 SER C OG   1 
ATOM   11422 H H    . SER C 1 186 ? 2.585   -28.034 28.783  1.00 134.69 ? 186 SER C H    1 
ATOM   11423 H HA   . SER C 1 186 ? 1.278   -26.228 27.385  1.00 135.81 ? 186 SER C HA   1 
ATOM   11424 H HB2  . SER C 1 186 ? 0.806   -27.873 26.026  1.00 142.05 ? 186 SER C HB2  1 
ATOM   11425 H HB3  . SER C 1 186 ? 1.899   -28.661 26.868  1.00 142.05 ? 186 SER C HB3  1 
ATOM   11426 H HG   . SER C 1 186 ? -0.018  -29.760 26.740  1.00 149.68 ? 186 SER C HG   1 
ATOM   11427 N N    . ASP C 1 187 ? -0.335  -27.542 29.789  1.00 117.36 ? 187 ASP C N    1 
ATOM   11428 C CA   . ASP C 1 187 ? -1.611  -27.520 30.497  1.00 118.36 ? 187 ASP C CA   1 
ATOM   11429 C C    . ASP C 1 187 ? -2.001  -26.102 30.901  1.00 122.93 ? 187 ASP C C    1 
ATOM   11430 O O    . ASP C 1 187 ? -3.164  -25.704 30.752  1.00 123.23 ? 187 ASP C O    1 
ATOM   11431 C CB   . ASP C 1 187 ? -1.544  -28.424 31.729  1.00 115.30 ? 187 ASP C CB   1 
ATOM   11432 C CG   . ASP C 1 187 ? -1.276  -29.878 31.377  1.00 119.04 ? 187 ASP C CG   1 
ATOM   11433 O OD1  . ASP C 1 187 ? -1.886  -30.388 30.414  1.00 122.36 ? 187 ASP C OD1  1 
ATOM   11434 O OD2  . ASP C 1 187 ? -0.456  -30.514 32.070  1.00 118.92 ? 187 ASP C OD2  1 
ATOM   11435 H H    . ASP C 1 187 ? 0.286   -27.991 30.182  1.00 140.83 ? 187 ASP C H    1 
ATOM   11436 H HA   . ASP C 1 187 ? -2.299  -27.862 29.904  1.00 142.04 ? 187 ASP C HA   1 
ATOM   11437 H HB2  . ASP C 1 187 ? -0.827  -28.119 32.307  1.00 138.35 ? 187 ASP C HB2  1 
ATOM   11438 H HB3  . ASP C 1 187 ? -2.391  -28.381 32.199  1.00 138.35 ? 187 ASP C HB3  1 
ATOM   11439 N N    . ASN C 1 188 ? -1.048  -25.327 31.419  1.00 129.52 ? 188 ASN C N    1 
ATOM   11440 C CA   . ASN C 1 188 ? -1.311  -23.975 31.895  1.00 130.18 ? 188 ASN C CA   1 
ATOM   11441 C C    . ASN C 1 188 ? -0.701  -22.906 30.997  1.00 127.93 ? 188 ASN C C    1 
ATOM   11442 O O    . ASN C 1 188 ? -0.743  -21.720 31.345  1.00 127.87 ? 188 ASN C O    1 
ATOM   11443 C CB   . ASN C 1 188 ? -0.788  -23.810 33.326  1.00 126.42 ? 188 ASN C CB   1 
ATOM   11444 C CG   . ASN C 1 188 ? 0.633   -24.319 33.490  1.00 127.15 ? 188 ASN C CG   1 
ATOM   11445 O OD1  . ASN C 1 188 ? 1.439   -24.250 32.562  1.00 129.57 ? 188 ASN C OD1  1 
ATOM   11446 N ND2  . ASN C 1 188 ? 0.946   -24.839 34.672  1.00 128.38 ? 188 ASN C ND2  1 
ATOM   11447 H H    . ASN C 1 188 ? -0.228  -25.569 31.506  1.00 155.42 ? 188 ASN C H    1 
ATOM   11448 H HA   . ASN C 1 188 ? -2.271  -23.838 31.905  1.00 156.22 ? 188 ASN C HA   1 
ATOM   11449 H HB2  . ASN C 1 188 ? -0.798  -22.868 33.560  1.00 151.70 ? 188 ASN C HB2  1 
ATOM   11450 H HB3  . ASN C 1 188 ? -1.358  -24.309 33.931  1.00 151.70 ? 188 ASN C HB3  1 
ATOM   11451 H HD21 . ASN C 1 188 ? 0.356   -24.873 35.296  1.00 154.06 ? 188 ASN C HD21 1 
ATOM   11452 H HD22 . ASN C 1 188 ? 1.739   -25.140 34.813  1.00 154.06 ? 188 ASN C HD22 1 
ATOM   11453 N N    . LEU C 1 189 ? -0.138  -23.293 29.850  1.00 117.27 ? 189 LEU C N    1 
ATOM   11454 C CA   . LEU C 1 189 ? 0.512   -22.343 28.948  1.00 110.19 ? 189 LEU C CA   1 
ATOM   11455 C C    . LEU C 1 189 ? 1.538   -21.497 29.696  1.00 107.68 ? 189 LEU C C    1 
ATOM   11456 O O    . LEU C 1 189 ? 1.730   -20.314 29.397  1.00 101.95 ? 189 LEU C O    1 
ATOM   11457 C CB   . LEU C 1 189 ? -0.524  -21.460 28.249  1.00 106.70 ? 189 LEU C CB   1 
ATOM   11458 C CG   . LEU C 1 189 ? -1.183  -22.095 27.019  1.00 109.41 ? 189 LEU C CG   1 
ATOM   11459 C CD1  . LEU C 1 189 ? -2.659  -21.727 26.937  1.00 108.12 ? 189 LEU C CD1  1 
ATOM   11460 C CD2  . LEU C 1 189 ? -0.453  -21.690 25.745  1.00 100.88 ? 189 LEU C CD2  1 
ATOM   11461 H H    . LEU C 1 189 ? -0.120  -24.107 29.572  1.00 140.72 ? 189 LEU C H    1 
ATOM   11462 H HA   . LEU C 1 189 ? 0.988   -22.837 28.262  1.00 132.23 ? 189 LEU C HA   1 
ATOM   11463 H HB2  . LEU C 1 189 ? -1.228  -21.251 28.882  1.00 128.04 ? 189 LEU C HB2  1 
ATOM   11464 H HB3  . LEU C 1 189 ? -0.087  -20.645 27.958  1.00 128.04 ? 189 LEU C HB3  1 
ATOM   11465 H HG   . LEU C 1 189 ? -1.125  -23.060 27.103  1.00 131.29 ? 189 LEU C HG   1 
ATOM   11466 H HD11 . LEU C 1 189 ? -3.041  -22.129 26.140  1.00 129.74 ? 189 LEU C HD11 1 
ATOM   11467 H HD12 . LEU C 1 189 ? -3.113  -22.061 27.726  1.00 129.74 ? 189 LEU C HD12 1 
ATOM   11468 H HD13 . LEU C 1 189 ? -2.742  -20.761 26.892  1.00 129.74 ? 189 LEU C HD13 1 
ATOM   11469 H HD21 . LEU C 1 189 ? -0.877  -22.121 24.987  1.00 121.05 ? 189 LEU C HD21 1 
ATOM   11470 H HD22 . LEU C 1 189 ? -0.500  -20.726 25.647  1.00 121.05 ? 189 LEU C HD22 1 
ATOM   11471 H HD23 . LEU C 1 189 ? 0.474   -21.971 25.808  1.00 121.05 ? 189 LEU C HD23 1 
ATOM   11472 N N    . SER C 1 190 ? 2.198   -22.099 30.677  1.00 108.61 ? 190 SER C N    1 
ATOM   11473 C CA   . SER C 1 190 ? 3.224   -21.429 31.452  1.00 104.41 ? 190 SER C CA   1 
ATOM   11474 C C    . SER C 1 190 ? 4.597   -21.652 30.824  1.00 101.54 ? 190 SER C C    1 
ATOM   11475 O O    . SER C 1 190 ? 4.786   -22.507 29.958  1.00 103.60 ? 190 SER C O    1 
ATOM   11476 C CB   . SER C 1 190 ? 3.215   -21.932 32.896  1.00 108.49 ? 190 SER C CB   1 
ATOM   11477 O OG   . SER C 1 190 ? 4.090   -23.035 33.054  1.00 108.15 ? 190 SER C OG   1 
ATOM   11478 H H    . SER C 1 190 ? 2.065   -22.915 30.916  1.00 130.34 ? 190 SER C H    1 
ATOM   11479 H HA   . SER C 1 190 ? 3.044   -20.476 31.462  1.00 125.29 ? 190 SER C HA   1 
ATOM   11480 H HB2  . SER C 1 190 ? 3.503   -21.215 33.482  1.00 130.19 ? 190 SER C HB2  1 
ATOM   11481 H HB3  . SER C 1 190 ? 2.315   -22.209 33.128  1.00 130.19 ? 190 SER C HB3  1 
ATOM   11482 H HG   . SER C 1 190 ? 4.081   -23.297 33.852  1.00 129.78 ? 190 SER C HG   1 
ATOM   11483 N N    . MET C 1 191 ? 5.571   -20.877 31.289  1.00 99.34  ? 191 MET C N    1 
ATOM   11484 C CA   . MET C 1 191 ? 6.916   -20.925 30.724  1.00 96.21  ? 191 MET C CA   1 
ATOM   11485 C C    . MET C 1 191 ? 7.889   -20.317 31.717  1.00 97.92  ? 191 MET C C    1 
ATOM   11486 O O    . MET C 1 191 ? 7.724   -19.156 32.108  1.00 95.14  ? 191 MET C O    1 
ATOM   11487 C CB   . MET C 1 191 ? 6.954   -20.169 29.406  1.00 93.24  ? 191 MET C CB   1 
ATOM   11488 C CG   . MET C 1 191 ? 8.062   -20.595 28.476  1.00 97.24  ? 191 MET C CG   1 
ATOM   11489 S SD   . MET C 1 191 ? 8.409   -19.315 27.263  1.00 92.08  ? 191 MET C SD   1 
ATOM   11490 C CE   . MET C 1 191 ? 9.082   -18.031 28.307  1.00 92.01  ? 191 MET C CE   1 
ATOM   11491 H H    . MET C 1 191 ? 5.478   -20.313 31.931  1.00 119.21 ? 191 MET C H    1 
ATOM   11492 H HA   . MET C 1 191 ? 7.166   -21.850 30.568  1.00 115.45 ? 191 MET C HA   1 
ATOM   11493 H HB2  . MET C 1 191 ? 6.113   -20.310 28.944  1.00 111.89 ? 191 MET C HB2  1 
ATOM   11494 H HB3  . MET C 1 191 ? 7.076   -19.226 29.594  1.00 111.89 ? 191 MET C HB3  1 
ATOM   11495 H HG2  . MET C 1 191 ? 8.869   -20.761 28.988  1.00 116.69 ? 191 MET C HG2  1 
ATOM   11496 H HG3  . MET C 1 191 ? 7.797   -21.401 28.005  1.00 116.69 ? 191 MET C HG3  1 
ATOM   11497 H HE1  . MET C 1 191 ? 9.630   -17.440 27.767  1.00 110.42 ? 191 MET C HE1  1 
ATOM   11498 H HE2  . MET C 1 191 ? 8.351   -17.532 28.705  1.00 110.42 ? 191 MET C HE2  1 
ATOM   11499 H HE3  . MET C 1 191 ? 9.621   -18.439 29.002  1.00 110.42 ? 191 MET C HE3  1 
ATOM   11500 N N    . LYS C 1 192 ? 8.897   -21.094 32.127  1.00 95.10  ? 192 LYS C N    1 
ATOM   11501 C CA   . LYS C 1 192 ? 9.919   -20.606 33.044  1.00 96.07  ? 192 LYS C CA   1 
ATOM   11502 C C    . LYS C 1 192 ? 11.166  -20.266 32.238  1.00 95.00  ? 192 LYS C C    1 
ATOM   11503 O O    . LYS C 1 192 ? 11.894  -21.181 31.814  1.00 94.41  ? 192 LYS C O    1 
ATOM   11504 C CB   . LYS C 1 192 ? 10.238  -21.654 34.116  1.00 99.41  ? 192 LYS C CB   1 
ATOM   11505 C CG   . LYS C 1 192 ? 9.345   -21.586 35.352  1.00 98.70  ? 192 LYS C CG   1 
ATOM   11506 C CD   . LYS C 1 192 ? 7.900   -21.291 34.973  1.00 101.96 ? 192 LYS C CD   1 
ATOM   11507 C CE   . LYS C 1 192 ? 6.938   -21.636 36.099  1.00 105.70 ? 192 LYS C CE   1 
ATOM   11508 N NZ   . LYS C 1 192 ? 5.566   -21.129 35.801  1.00 110.95 ? 192 LYS C NZ   1 
ATOM   11509 H H    . LYS C 1 192 ? 9.007   -21.911 31.883  1.00 114.12 ? 192 LYS C H    1 
ATOM   11510 H HA   . LYS C 1 192 ? 9.599   -19.806 33.489  1.00 115.28 ? 192 LYS C HA   1 
ATOM   11511 H HB2  . LYS C 1 192 ? 10.134  -22.536 33.726  1.00 119.29 ? 192 LYS C HB2  1 
ATOM   11512 H HB3  . LYS C 1 192 ? 11.154  -21.527 34.409  1.00 119.29 ? 192 LYS C HB3  1 
ATOM   11513 H HG2  . LYS C 1 192 ? 9.372   -22.438 35.816  1.00 118.44 ? 192 LYS C HG2  1 
ATOM   11514 H HG3  . LYS C 1 192 ? 9.658   -20.879 35.937  1.00 118.44 ? 192 LYS C HG3  1 
ATOM   11515 H HD2  . LYS C 1 192 ? 7.808   -20.346 34.774  1.00 122.36 ? 192 LYS C HD2  1 
ATOM   11516 H HD3  . LYS C 1 192 ? 7.659   -21.818 34.195  1.00 122.36 ? 192 LYS C HD3  1 
ATOM   11517 H HE2  . LYS C 1 192 ? 6.893   -22.600 36.202  1.00 126.84 ? 192 LYS C HE2  1 
ATOM   11518 H HE3  . LYS C 1 192 ? 7.245   -21.228 36.923  1.00 126.84 ? 192 LYS C HE3  1 
ATOM   11519 H HZ1  . LYS C 1 192 ? 5.262   -21.496 35.050  1.00 133.14 ? 192 LYS C HZ1  1 
ATOM   11520 H HZ2  . LYS C 1 192 ? 5.013   -21.336 36.468  1.00 133.14 ? 192 LYS C HZ2  1 
ATOM   11521 H HZ3  . LYS C 1 192 ? 5.583   -20.244 35.705  1.00 133.14 ? 192 LYS C HZ3  1 
ATOM   11522 N N    . PRO C 1 193 ? 11.454  -18.986 31.981  1.00 92.51  ? 193 PRO C N    1 
ATOM   11523 C CA   . PRO C 1 193 ? 12.617  -18.656 31.147  1.00 95.31  ? 193 PRO C CA   1 
ATOM   11524 C C    . PRO C 1 193 ? 13.934  -18.764 31.896  1.00 93.49  ? 193 PRO C C    1 
ATOM   11525 O O    . PRO C 1 193 ? 14.329  -17.844 32.618  1.00 95.11  ? 193 PRO C O    1 
ATOM   11526 C CB   . PRO C 1 193 ? 12.348  -17.208 30.703  1.00 94.06  ? 193 PRO C CB   1 
ATOM   11527 C CG   . PRO C 1 193 ? 10.951  -16.870 31.180  1.00 93.87  ? 193 PRO C CG   1 
ATOM   11528 C CD   . PRO C 1 193 ? 10.669  -17.790 32.332  1.00 96.10  ? 193 PRO C CD   1 
ATOM   11529 H HA   . PRO C 1 193 ? 12.637  -19.237 30.370  1.00 114.37 ? 193 PRO C HA   1 
ATOM   11530 H HB2  . PRO C 1 193 ? 13.001  -16.617 31.109  1.00 112.88 ? 193 PRO C HB2  1 
ATOM   11531 H HB3  . PRO C 1 193 ? 12.403  -17.149 29.736  1.00 112.88 ? 193 PRO C HB3  1 
ATOM   11532 H HG2  . PRO C 1 193 ? 10.919  -15.944 31.466  1.00 112.64 ? 193 PRO C HG2  1 
ATOM   11533 H HG3  . PRO C 1 193 ? 10.316  -17.018 30.461  1.00 112.64 ? 193 PRO C HG3  1 
ATOM   11534 H HD2  . PRO C 1 193 ? 10.975  -17.405 33.168  1.00 115.32 ? 193 PRO C HD2  1 
ATOM   11535 H HD3  . PRO C 1 193 ? 9.723   -17.998 32.390  1.00 115.32 ? 193 PRO C HD3  1 
ATOM   11536 N N    . TYR C 1 194 ? 14.630  -19.881 31.722  1.00 93.03  ? 194 TYR C N    1 
ATOM   11537 C CA   . TYR C 1 194 ? 15.974  -20.048 32.256  1.00 97.54  ? 194 TYR C CA   1 
ATOM   11538 C C    . TYR C 1 194 ? 16.988  -19.518 31.248  1.00 100.71 ? 194 TYR C C    1 
ATOM   11539 O O    . TYR C 1 194 ? 16.893  -19.818 30.051  1.00 104.19 ? 194 TYR C O    1 
ATOM   11540 C CB   . TYR C 1 194 ? 16.256  -21.516 32.570  1.00 101.80 ? 194 TYR C CB   1 
ATOM   11541 C CG   . TYR C 1 194 ? 17.701  -21.798 32.919  1.00 104.90 ? 194 TYR C CG   1 
ATOM   11542 C CD1  . TYR C 1 194 ? 18.625  -22.112 31.931  1.00 107.28 ? 194 TYR C CD1  1 
ATOM   11543 C CD2  . TYR C 1 194 ? 18.140  -21.759 34.238  1.00 106.40 ? 194 TYR C CD2  1 
ATOM   11544 C CE1  . TYR C 1 194 ? 19.945  -22.374 32.243  1.00 109.07 ? 194 TYR C CE1  1 
ATOM   11545 C CE2  . TYR C 1 194 ? 19.460  -22.020 34.558  1.00 106.87 ? 194 TYR C CE2  1 
ATOM   11546 C CZ   . TYR C 1 194 ? 20.357  -22.326 33.555  1.00 109.52 ? 194 TYR C CZ   1 
ATOM   11547 O OH   . TYR C 1 194 ? 21.673  -22.588 33.862  1.00 111.14 ? 194 TYR C OH   1 
ATOM   11548 H H    . TYR C 1 194 ? 14.339  -20.567 31.292  1.00 111.64 ? 194 TYR C H    1 
ATOM   11549 H HA   . TYR C 1 194 ? 16.062  -19.544 33.080  1.00 117.05 ? 194 TYR C HA   1 
ATOM   11550 H HB2  . TYR C 1 194 ? 15.712  -21.783 33.327  1.00 122.16 ? 194 TYR C HB2  1 
ATOM   11551 H HB3  . TYR C 1 194 ? 16.030  -22.051 31.793  1.00 122.16 ? 194 TYR C HB3  1 
ATOM   11552 H HD1  . TYR C 1 194 ? 18.350  -22.147 31.044  1.00 128.74 ? 194 TYR C HD1  1 
ATOM   11553 H HD2  . TYR C 1 194 ? 17.537  -21.553 34.915  1.00 127.68 ? 194 TYR C HD2  1 
ATOM   11554 H HE1  . TYR C 1 194 ? 20.552  -22.580 31.569  1.00 130.88 ? 194 TYR C HE1  1 
ATOM   11555 H HE2  . TYR C 1 194 ? 19.741  -21.990 35.444  1.00 128.24 ? 194 TYR C HE2  1 
ATOM   11556 H HH   . TYR C 1 194 ? 21.834  -22.360 34.655  1.00 133.37 ? 194 TYR C HH   1 
ATOM   11557 N N    . VAL C 1 195 ? 17.962  -18.751 31.736  1.00 101.04 ? 195 VAL C N    1 
ATOM   11558 C CA   . VAL C 1 195 ? 18.992  -18.157 30.898  1.00 103.38 ? 195 VAL C CA   1 
ATOM   11559 C C    . VAL C 1 195 ? 20.351  -18.445 31.522  1.00 107.46 ? 195 VAL C C    1 
ATOM   11560 O O    . VAL C 1 195 ? 20.468  -18.721 32.718  1.00 109.51 ? 195 VAL C O    1 
ATOM   11561 C CB   . VAL C 1 195 ? 18.790  -16.637 30.720  1.00 102.53 ? 195 VAL C CB   1 
ATOM   11562 C CG1  . VAL C 1 195 ? 19.514  -16.142 29.479  1.00 102.33 ? 195 VAL C CG1  1 
ATOM   11563 C CG2  . VAL C 1 195 ? 17.307  -16.299 30.636  1.00 100.68 ? 195 VAL C CG2  1 
ATOM   11564 H H    . VAL C 1 195 ? 18.045  -18.557 32.570  1.00 121.25 ? 195 VAL C H    1 
ATOM   11565 H HA   . VAL C 1 195 ? 18.970  -18.570 30.020  1.00 124.06 ? 195 VAL C HA   1 
ATOM   11566 H HB   . VAL C 1 195 ? 19.162  -16.183 31.492  1.00 123.04 ? 195 VAL C HB   1 
ATOM   11567 H HG11 . VAL C 1 195 ? 19.367  -15.188 29.386  1.00 122.80 ? 195 VAL C HG11 1 
ATOM   11568 H HG12 . VAL C 1 195 ? 20.463  -16.323 29.574  1.00 122.80 ? 195 VAL C HG12 1 
ATOM   11569 H HG13 . VAL C 1 195 ? 19.166  -16.608 28.703  1.00 122.80 ? 195 VAL C HG13 1 
ATOM   11570 H HG21 . VAL C 1 195 ? 17.209  -15.343 30.503  1.00 120.81 ? 195 VAL C HG21 1 
ATOM   11571 H HG22 . VAL C 1 195 ? 16.915  -16.779 29.890  1.00 120.81 ? 195 VAL C HG22 1 
ATOM   11572 H HG23 . VAL C 1 195 ? 16.876  -16.564 31.463  1.00 120.81 ? 195 VAL C HG23 1 
ATOM   11573 N N    . TYR C 1 196 ? 21.387  -18.379 30.689  1.00 110.15 ? 196 TYR C N    1 
ATOM   11574 C CA   . TYR C 1 196 ? 22.749  -18.644 31.129  1.00 114.98 ? 196 TYR C CA   1 
ATOM   11575 C C    . TYR C 1 196 ? 23.710  -17.799 30.308  1.00 119.79 ? 196 TYR C C    1 
ATOM   11576 O O    . TYR C 1 196 ? 23.473  -17.536 29.126  1.00 122.55 ? 196 TYR C O    1 
ATOM   11577 C CB   . TYR C 1 196 ? 23.099  -20.133 30.995  1.00 113.22 ? 196 TYR C CB   1 
ATOM   11578 C CG   . TYR C 1 196 ? 24.460  -20.507 31.544  1.00 117.77 ? 196 TYR C CG   1 
ATOM   11579 C CD1  . TYR C 1 196 ? 24.624  -20.848 32.884  1.00 117.28 ? 196 TYR C CD1  1 
ATOM   11580 C CD2  . TYR C 1 196 ? 25.580  -20.527 30.721  1.00 119.18 ? 196 TYR C CD2  1 
ATOM   11581 C CE1  . TYR C 1 196 ? 25.867  -21.193 33.388  1.00 117.41 ? 196 TYR C CE1  1 
ATOM   11582 C CE2  . TYR C 1 196 ? 26.827  -20.871 31.217  1.00 121.47 ? 196 TYR C CE2  1 
ATOM   11583 C CZ   . TYR C 1 196 ? 26.964  -21.203 32.551  1.00 120.85 ? 196 TYR C CZ   1 
ATOM   11584 O OH   . TYR C 1 196 ? 28.200  -21.547 33.050  1.00 121.20 ? 196 TYR C OH   1 
ATOM   11585 H H    . TYR C 1 196 ? 21.324  -18.180 29.854  1.00 132.18 ? 196 TYR C H    1 
ATOM   11586 H HA   . TYR C 1 196 ? 22.846  -18.390 32.060  1.00 137.98 ? 196 TYR C HA   1 
ATOM   11587 H HB2  . TYR C 1 196 ? 22.436  -20.651 31.478  1.00 135.86 ? 196 TYR C HB2  1 
ATOM   11588 H HB3  . TYR C 1 196 ? 23.086  -20.370 30.055  1.00 135.86 ? 196 TYR C HB3  1 
ATOM   11589 H HD1  . TYR C 1 196 ? 23.887  -20.843 33.450  1.00 140.74 ? 196 TYR C HD1  1 
ATOM   11590 H HD2  . TYR C 1 196 ? 25.491  -20.306 29.822  1.00 143.02 ? 196 TYR C HD2  1 
ATOM   11591 H HE1  . TYR C 1 196 ? 25.961  -21.418 34.286  1.00 140.90 ? 196 TYR C HE1  1 
ATOM   11592 H HE2  . TYR C 1 196 ? 27.568  -20.878 30.655  1.00 145.77 ? 196 TYR C HE2  1 
ATOM   11593 H HH   . TYR C 1 196 ? 28.141  -21.718 33.870  1.00 145.44 ? 196 TYR C HH   1 
ATOM   11594 N N    . VAL C 1 197 ? 24.794  -17.369 30.950  1.00 121.38 ? 197 VAL C N    1 
ATOM   11595 C CA   . VAL C 1 197 ? 25.833  -16.578 30.301  1.00 126.18 ? 197 VAL C CA   1 
ATOM   11596 C C    . VAL C 1 197 ? 27.190  -17.098 30.756  1.00 126.49 ? 197 VAL C C    1 
ATOM   11597 O O    . VAL C 1 197 ? 27.402  -17.354 31.946  1.00 124.60 ? 197 VAL C O    1 
ATOM   11598 C CB   . VAL C 1 197 ? 25.693  -15.074 30.617  1.00 126.60 ? 197 VAL C CB   1 
ATOM   11599 C CG1  . VAL C 1 197 ? 26.396  -14.239 29.552  1.00 128.64 ? 197 VAL C CG1  1 
ATOM   11600 C CG2  . VAL C 1 197 ? 24.227  -14.683 30.727  1.00 124.51 ? 197 VAL C CG2  1 
ATOM   11601 H H    . VAL C 1 197 ? 24.953  -17.528 31.780  1.00 145.65 ? 197 VAL C H    1 
ATOM   11602 H HA   . VAL C 1 197 ? 25.764  -16.692 29.340  1.00 151.42 ? 197 VAL C HA   1 
ATOM   11603 H HB   . VAL C 1 197 ? 26.115  -14.891 31.471  1.00 151.92 ? 197 VAL C HB   1 
ATOM   11604 H HG11 . VAL C 1 197 ? 26.298  -13.299 29.772  1.00 154.36 ? 197 VAL C HG11 1 
ATOM   11605 H HG12 . VAL C 1 197 ? 27.335  -14.479 29.532  1.00 154.36 ? 197 VAL C HG12 1 
ATOM   11606 H HG13 . VAL C 1 197 ? 25.990  -14.421 28.690  1.00 154.36 ? 197 VAL C HG13 1 
ATOM   11607 H HG21 . VAL C 1 197 ? 24.159  -13.716 30.761  1.00 149.41 ? 197 VAL C HG21 1 
ATOM   11608 H HG22 . VAL C 1 197 ? 23.751  -15.022 29.953  1.00 149.41 ? 197 VAL C HG22 1 
ATOM   11609 H HG23 . VAL C 1 197 ? 23.858  -15.069 31.537  1.00 149.41 ? 197 VAL C HG23 1 
ATOM   11610 N N    . LYS C 1 198 ? 28.112  -17.256 29.801  1.00 129.40 ? 198 LYS C N    1 
ATOM   11611 C CA   . LYS C 1 198 ? 29.445  -17.748 30.138  1.00 131.04 ? 198 LYS C CA   1 
ATOM   11612 C C    . LYS C 1 198 ? 30.146  -16.813 31.116  1.00 131.21 ? 198 LYS C C    1 
ATOM   11613 O O    . LYS C 1 198 ? 30.801  -17.269 32.061  1.00 130.26 ? 198 LYS C O    1 
ATOM   11614 C CB   . LYS C 1 198 ? 30.281  -17.917 28.868  1.00 132.37 ? 198 LYS C CB   1 
ATOM   11615 C CG   . LYS C 1 198 ? 31.460  -18.874 29.015  1.00 132.32 ? 198 LYS C CG   1 
ATOM   11616 C CD   . LYS C 1 198 ? 32.688  -18.182 29.602  1.00 133.18 ? 198 LYS C CD   1 
ATOM   11617 C CE   . LYS C 1 198 ? 33.953  -18.540 28.828  1.00 133.61 ? 198 LYS C CE   1 
ATOM   11618 N NZ   . LYS C 1 198 ? 35.193  -18.140 29.555  1.00 133.15 ? 198 LYS C NZ   1 
ATOM   11619 H H    . LYS C 1 198 ? 27.992  -17.087 28.966  1.00 155.28 ? 198 LYS C H    1 
ATOM   11620 H HA   . LYS C 1 198 ? 29.359  -18.617 30.559  1.00 157.25 ? 198 LYS C HA   1 
ATOM   11621 H HB2  . LYS C 1 198 ? 29.709  -18.262 28.164  1.00 158.84 ? 198 LYS C HB2  1 
ATOM   11622 H HB3  . LYS C 1 198 ? 30.636  -17.051 28.612  1.00 158.84 ? 198 LYS C HB3  1 
ATOM   11623 H HG2  . LYS C 1 198 ? 31.210  -19.600 29.607  1.00 158.78 ? 198 LYS C HG2  1 
ATOM   11624 H HG3  . LYS C 1 198 ? 31.698  -19.224 28.142  1.00 158.78 ? 198 LYS C HG3  1 
ATOM   11625 H HD2  . LYS C 1 198 ? 32.566  -17.220 29.559  1.00 159.81 ? 198 LYS C HD2  1 
ATOM   11626 H HD3  . LYS C 1 198 ? 32.804  -18.461 30.523  1.00 159.81 ? 198 LYS C HD3  1 
ATOM   11627 H HE2  . LYS C 1 198 ? 33.981  -19.500 28.690  1.00 160.33 ? 198 LYS C HE2  1 
ATOM   11628 H HE3  . LYS C 1 198 ? 33.943  -18.082 27.973  1.00 160.33 ? 198 LYS C HE3  1 
ATOM   11629 H HZ1  . LYS C 1 198 ? 35.911  -18.362 29.078  1.00 159.78 ? 198 LYS C HZ1  1 
ATOM   11630 H HZ2  . LYS C 1 198 ? 35.196  -17.260 29.690  1.00 159.78 ? 198 LYS C HZ2  1 
ATOM   11631 H HZ3  . LYS C 1 198 ? 35.231  -18.553 30.343  1.00 159.78 ? 198 LYS C HZ3  1 
ATOM   11632 N N    . GLU C 1 199 ? 30.022  -15.499 30.906  1.00 131.99 ? 199 GLU C N    1 
ATOM   11633 C CA   . GLU C 1 199 ? 30.634  -14.542 31.823  1.00 132.36 ? 199 GLU C CA   1 
ATOM   11634 C C    . GLU C 1 199 ? 30.050  -14.680 33.224  1.00 131.47 ? 199 GLU C C    1 
ATOM   11635 O O    . GLU C 1 199 ? 30.785  -14.723 34.218  1.00 131.54 ? 199 GLU C O    1 
ATOM   11636 C CB   . GLU C 1 199 ? 30.444  -13.114 31.301  1.00 135.47 ? 199 GLU C CB   1 
ATOM   11637 C CG   . GLU C 1 199 ? 31.470  -12.685 30.263  1.00 139.17 ? 199 GLU C CG   1 
ATOM   11638 C CD   . GLU C 1 199 ? 32.251  -11.442 30.669  1.00 139.84 ? 199 GLU C CD   1 
ATOM   11639 O OE1  . GLU C 1 199 ? 31.775  -10.685 31.544  1.00 140.91 ? 199 GLU C OE1  1 
ATOM   11640 O OE2  . GLU C 1 199 ? 33.343  -11.218 30.110  1.00 139.99 ? 199 GLU C OE2  1 
ATOM   11641 H H    . GLU C 1 199 ? 29.594  -15.144 30.250  1.00 158.39 ? 199 GLU C H    1 
ATOM   11642 H HA   . GLU C 1 199 ? 31.587  -14.720 31.869  1.00 158.83 ? 199 GLU C HA   1 
ATOM   11643 H HB2  . GLU C 1 199 ? 29.567  -13.049 30.892  1.00 162.56 ? 199 GLU C HB2  1 
ATOM   11644 H HB3  . GLU C 1 199 ? 30.507  -12.500 32.049  1.00 162.56 ? 199 GLU C HB3  1 
ATOM   11645 H HG2  . GLU C 1 199 ? 32.104  -13.406 30.132  1.00 167.01 ? 199 GLU C HG2  1 
ATOM   11646 H HG3  . GLU C 1 199 ? 31.012  -12.489 29.431  1.00 167.01 ? 199 GLU C HG3  1 
ATOM   11647 N N    . VAL C 1 200 ? 28.719  -14.748 33.323  1.00 129.58 ? 200 VAL C N    1 
ATOM   11648 C CA   . VAL C 1 200 ? 28.074  -14.871 34.626  1.00 125.05 ? 200 VAL C CA   1 
ATOM   11649 C C    . VAL C 1 200 ? 28.420  -16.203 35.279  1.00 125.07 ? 200 VAL C C    1 
ATOM   11650 O O    . VAL C 1 200 ? 28.505  -16.296 36.510  1.00 118.07 ? 200 VAL C O    1 
ATOM   11651 C CB   . VAL C 1 200 ? 26.550  -14.695 34.473  1.00 120.81 ? 200 VAL C CB   1 
ATOM   11652 C CG1  . VAL C 1 200 ? 25.833  -15.045 35.766  1.00 118.28 ? 200 VAL C CG1  1 
ATOM   11653 C CG2  . VAL C 1 200 ? 26.218  -13.272 34.038  1.00 119.22 ? 200 VAL C CG2  1 
ATOM   11654 H H    . VAL C 1 200 ? 28.176  -14.725 32.657  1.00 155.49 ? 200 VAL C H    1 
ATOM   11655 H HA   . VAL C 1 200 ? 28.406  -14.166 35.204  1.00 150.06 ? 200 VAL C HA   1 
ATOM   11656 H HB   . VAL C 1 200 ? 26.235  -15.303 33.785  1.00 144.98 ? 200 VAL C HB   1 
ATOM   11657 H HG11 . VAL C 1 200 ? 24.930  -14.691 35.733  1.00 141.93 ? 200 VAL C HG11 1 
ATOM   11658 H HG12 . VAL C 1 200 ? 25.806  -16.010 35.862  1.00 141.93 ? 200 VAL C HG12 1 
ATOM   11659 H HG13 . VAL C 1 200 ? 26.315  -14.652 36.511  1.00 141.93 ? 200 VAL C HG13 1 
ATOM   11660 H HG21 . VAL C 1 200 ? 27.044  -12.789 33.881  1.00 143.06 ? 200 VAL C HG21 1 
ATOM   11661 H HG22 . VAL C 1 200 ? 25.694  -13.305 33.222  1.00 143.06 ? 200 VAL C HG22 1 
ATOM   11662 H HG23 . VAL C 1 200 ? 25.709  -12.838 34.741  1.00 143.06 ? 200 VAL C HG23 1 
ATOM   11663 N N    . GLY C 1 201 ? 28.629  -17.247 34.481  1.00 122.04 ? 201 GLY C N    1 
ATOM   11664 C CA   . GLY C 1 201 ? 28.919  -18.556 35.027  1.00 119.95 ? 201 GLY C CA   1 
ATOM   11665 C C    . GLY C 1 201 ? 27.786  -19.191 35.795  1.00 117.98 ? 201 GLY C C    1 
ATOM   11666 O O    . GLY C 1 201 ? 28.005  -20.195 36.479  1.00 119.94 ? 201 GLY C O    1 
ATOM   11667 H H    . GLY C 1 201 ? 28.608  -17.218 33.622  1.00 146.45 ? 201 GLY C H    1 
ATOM   11668 H HA2  . GLY C 1 201 ? 29.152  -19.151 34.298  1.00 143.94 ? 201 GLY C HA2  1 
ATOM   11669 H HA3  . GLY C 1 201 ? 29.677  -18.480 35.627  1.00 143.94 ? 201 GLY C HA3  1 
ATOM   11670 N N    . SER C 1 202 ? 26.580  -18.640 35.701  1.00 116.70 ? 202 SER C N    1 
ATOM   11671 C CA   . SER C 1 202 ? 25.437  -19.153 36.439  1.00 113.26 ? 202 SER C CA   1 
ATOM   11672 C C    . SER C 1 202 ? 24.168  -18.744 35.708  1.00 112.40 ? 202 SER C C    1 
ATOM   11673 O O    . SER C 1 202 ? 24.177  -17.839 34.869  1.00 114.76 ? 202 SER C O    1 
ATOM   11674 C CB   . SER C 1 202 ? 25.422  -18.631 37.878  1.00 115.64 ? 202 SER C CB   1 
ATOM   11675 O OG   . SER C 1 202 ? 25.742  -17.252 37.912  1.00 114.89 ? 202 SER C OG   1 
ATOM   11676 H H    . SER C 1 202 ? 26.398  -17.958 35.210  1.00 140.04 ? 202 SER C H    1 
ATOM   11677 H HA   . SER C 1 202 ? 25.476  -20.121 36.467  1.00 135.91 ? 202 SER C HA   1 
ATOM   11678 H HB2  . SER C 1 202 ? 24.536  -18.759 38.252  1.00 138.77 ? 202 SER C HB2  1 
ATOM   11679 H HB3  . SER C 1 202 ? 26.077  -19.121 38.399  1.00 138.77 ? 202 SER C HB3  1 
ATOM   11680 H HG   . SER C 1 202 ? 25.751  -16.978 38.706  1.00 137.87 ? 202 SER C HG   1 
ATOM   11681 N N    . GLY C 1 203 ? 23.071  -19.417 36.050  1.00 111.80 ? 203 GLY C N    1 
ATOM   11682 C CA   . GLY C 1 203 ? 21.798  -19.184 35.407  1.00 109.58 ? 203 GLY C CA   1 
ATOM   11683 C C    . GLY C 1 203 ? 20.851  -18.348 36.255  1.00 104.74 ? 203 GLY C C    1 
ATOM   11684 O O    . GLY C 1 203 ? 21.057  -18.124 37.442  1.00 108.67 ? 203 GLY C O    1 
ATOM   11685 H H    . GLY C 1 203 ? 23.046  -20.021 36.662  1.00 134.17 ? 203 GLY C H    1 
ATOM   11686 H HA2  . GLY C 1 203 ? 21.945  -18.719 34.569  1.00 131.50 ? 203 GLY C HA2  1 
ATOM   11687 H HA3  . GLY C 1 203 ? 21.372  -20.036 35.226  1.00 131.50 ? 203 GLY C HA3  1 
ATOM   11688 N N    . VAL C 1 204 ? 19.794  -17.874 35.601  1.00 101.50 ? 204 VAL C N    1 
ATOM   11689 C CA   . VAL C 1 204 ? 18.739  -17.122 36.266  1.00 100.27 ? 204 VAL C CA   1 
ATOM   11690 C C    . VAL C 1 204 ? 17.423  -17.452 35.576  1.00 99.39  ? 204 VAL C C    1 
ATOM   11691 O O    . VAL C 1 204 ? 17.380  -17.689 34.367  1.00 100.53 ? 204 VAL C O    1 
ATOM   11692 C CB   . VAL C 1 204 ? 19.003  -15.598 36.246  1.00 100.38 ? 204 VAL C CB   1 
ATOM   11693 C CG1  . VAL C 1 204 ? 20.462  -15.293 36.560  1.00 103.39 ? 204 VAL C CG1  1 
ATOM   11694 C CG2  . VAL C 1 204 ? 18.603  -15.002 34.904  1.00 97.16  ? 204 VAL C CG2  1 
ATOM   11695 H H    . VAL C 1 204 ? 19.664  -17.978 34.757  1.00 121.81 ? 204 VAL C H    1 
ATOM   11696 H HA   . VAL C 1 204 ? 18.690  -17.402 37.193  1.00 120.32 ? 204 VAL C HA   1 
ATOM   11697 H HB   . VAL C 1 204 ? 18.460  -15.182 36.933  1.00 120.46 ? 204 VAL C HB   1 
ATOM   11698 H HG11 . VAL C 1 204 ? 20.573  -14.333 36.645  1.00 124.07 ? 204 VAL C HG11 1 
ATOM   11699 H HG12 . VAL C 1 204 ? 20.703  -15.729 37.392  1.00 124.07 ? 204 VAL C HG12 1 
ATOM   11700 H HG13 . VAL C 1 204 ? 21.017  -15.628 35.838  1.00 124.07 ? 204 VAL C HG13 1 
ATOM   11701 H HG21 . VAL C 1 204 ? 19.032  -14.138 34.802  1.00 116.59 ? 204 VAL C HG21 1 
ATOM   11702 H HG22 . VAL C 1 204 ? 18.890  -15.599 34.195  1.00 116.59 ? 204 VAL C HG22 1 
ATOM   11703 H HG23 . VAL C 1 204 ? 17.639  -14.898 34.879  1.00 116.59 ? 204 VAL C HG23 1 
ATOM   11704 N N    . TYR C 1 205 ? 16.346  -17.466 36.353  1.00 96.73  ? 205 TYR C N    1 
ATOM   11705 C CA   . TYR C 1 205 ? 14.999  -17.711 35.839  1.00 94.17  ? 205 TYR C CA   1 
ATOM   11706 C C    . TYR C 1 205 ? 14.317  -16.351 35.745  1.00 95.34  ? 205 TYR C C    1 
ATOM   11707 O O    . TYR C 1 205 ? 13.792  -15.837 36.735  1.00 94.98  ? 205 TYR C O    1 
ATOM   11708 C CB   . TYR C 1 205 ? 14.234  -18.676 36.735  1.00 97.11  ? 205 TYR C CB   1 
ATOM   11709 C CG   . TYR C 1 205 ? 14.876  -20.045 36.862  1.00 103.79 ? 205 TYR C CG   1 
ATOM   11710 C CD1  . TYR C 1 205 ? 16.183  -20.184 37.317  1.00 103.09 ? 205 TYR C CD1  1 
ATOM   11711 C CD2  . TYR C 1 205 ? 14.172  -21.198 36.533  1.00 105.95 ? 205 TYR C CD2  1 
ATOM   11712 C CE1  . TYR C 1 205 ? 16.772  -21.427 37.439  1.00 104.23 ? 205 TYR C CE1  1 
ATOM   11713 C CE2  . TYR C 1 205 ? 14.754  -22.449 36.652  1.00 107.89 ? 205 TYR C CE2  1 
ATOM   11714 C CZ   . TYR C 1 205 ? 16.055  -22.557 37.106  1.00 111.12 ? 205 TYR C CZ   1 
ATOM   11715 O OH   . TYR C 1 205 ? 16.641  -23.798 37.229  1.00 118.31 ? 205 TYR C OH   1 
ATOM   11716 H H    . TYR C 1 205 ? 16.368  -17.334 37.203  1.00 116.07 ? 205 TYR C H    1 
ATOM   11717 H HA   . TYR C 1 205 ? 15.043  -18.111 34.956  1.00 113.01 ? 205 TYR C HA   1 
ATOM   11718 H HB2  . TYR C 1 205 ? 14.176  -18.294 37.625  1.00 116.54 ? 205 TYR C HB2  1 
ATOM   11719 H HB3  . TYR C 1 205 ? 13.344  -18.800 36.369  1.00 116.54 ? 205 TYR C HB3  1 
ATOM   11720 H HD1  . TYR C 1 205 ? 16.670  -19.425 37.544  1.00 123.71 ? 205 TYR C HD1  1 
ATOM   11721 H HD2  . TYR C 1 205 ? 13.296  -21.129 36.229  1.00 127.14 ? 205 TYR C HD2  1 
ATOM   11722 H HE1  . TYR C 1 205 ? 17.647  -21.502 37.744  1.00 125.08 ? 205 TYR C HE1  1 
ATOM   11723 H HE2  . TYR C 1 205 ? 14.273  -23.212 36.428  1.00 129.47 ? 205 TYR C HE2  1 
ATOM   11724 H HH   . TYR C 1 205 ? 16.095  -24.397 37.006  1.00 141.97 ? 205 TYR C HH   1 
ATOM   11725 N N    . GLU C 1 206 ? 14.342  -15.761 34.552  1.00 95.13  ? 206 GLU C N    1 
ATOM   11726 C CA   . GLU C 1 206 ? 13.868  -14.397 34.384  1.00 93.46  ? 206 GLU C CA   1 
ATOM   11727 C C    . GLU C 1 206 ? 12.373  -14.307 34.681  1.00 90.10  ? 206 GLU C C    1 
ATOM   11728 O O    . GLU C 1 206 ? 11.639  -15.298 34.653  1.00 89.59  ? 206 GLU C O    1 
ATOM   11729 C CB   . GLU C 1 206 ? 14.152  -13.899 32.964  1.00 94.03  ? 206 GLU C CB   1 
ATOM   11730 C CG   . GLU C 1 206 ? 15.564  -14.182 32.463  1.00 96.93  ? 206 GLU C CG   1 
ATOM   11731 C CD   . GLU C 1 206 ? 16.541  -13.047 32.747  1.00 96.89  ? 206 GLU C CD   1 
ATOM   11732 O OE1  . GLU C 1 206 ? 16.096  -11.948 33.148  1.00 94.35  ? 206 GLU C OE1  1 
ATOM   11733 O OE2  . GLU C 1 206 ? 17.761  -13.255 32.562  1.00 96.88  ? 206 GLU C OE2  1 
ATOM   11734 H H    . GLU C 1 206 ? 14.628  -16.130 33.830  1.00 114.15 ? 206 GLU C H    1 
ATOM   11735 H HA   . GLU C 1 206 ? 14.336  -13.818 35.005  1.00 112.16 ? 206 GLU C HA   1 
ATOM   11736 H HB2  . GLU C 1 206 ? 13.533  -14.332 32.355  1.00 112.84 ? 206 GLU C HB2  1 
ATOM   11737 H HB3  . GLU C 1 206 ? 14.021  -12.938 32.942  1.00 112.84 ? 206 GLU C HB3  1 
ATOM   11738 H HG2  . GLU C 1 206 ? 15.899  -14.980 32.901  1.00 116.31 ? 206 GLU C HG2  1 
ATOM   11739 H HG3  . GLU C 1 206 ? 15.536  -14.317 31.503  1.00 116.31 ? 206 GLU C HG3  1 
ATOM   11740 N N    . ASN C 1 207 ? 11.928  -13.088 34.982  1.00 90.69  ? 207 ASN C N    1 
ATOM   11741 C CA   . ASN C 1 207 ? 10.501  -12.855 35.164  1.00 90.73  ? 207 ASN C CA   1 
ATOM   11742 C C    . ASN C 1 207 ? 9.770   -12.851 33.832  1.00 92.10  ? 207 ASN C C    1 
ATOM   11743 O O    . ASN C 1 207 ? 8.571   -13.147 33.784  1.00 92.78  ? 207 ASN C O    1 
ATOM   11744 C CB   . ASN C 1 207 ? 10.273  -11.535 35.890  1.00 93.76  ? 207 ASN C CB   1 
ATOM   11745 C CG   . ASN C 1 207 ? 10.873  -11.527 37.272  1.00 91.12  ? 207 ASN C CG   1 
ATOM   11746 O OD1  . ASN C 1 207 ? 10.331  -12.130 38.198  1.00 93.83  ? 207 ASN C OD1  1 
ATOM   11747 N ND2  . ASN C 1 207 ? 12.007  -10.855 37.418  1.00 90.82  ? 207 ASN C ND2  1 
ATOM   11748 H H    . ASN C 1 207 ? 12.423  -12.392 35.084  1.00 108.83 ? 207 ASN C H    1 
ATOM   11749 H HA   . ASN C 1 207 ? 10.135  -13.566 35.713  1.00 108.87 ? 207 ASN C HA   1 
ATOM   11750 H HB2  . ASN C 1 207 ? 10.682  -10.817 35.381  1.00 112.51 ? 207 ASN C HB2  1 
ATOM   11751 H HB3  . ASN C 1 207 ? 9.319   -11.380 35.975  1.00 112.51 ? 207 ASN C HB3  1 
ATOM   11752 H HD21 . ASN C 1 207 ? 12.390  -10.820 38.188  1.00 108.99 ? 207 ASN C HD21 1 
ATOM   11753 H HD22 . ASN C 1 207 ? 12.360  -10.455 36.744  1.00 108.99 ? 207 ASN C HD22 1 
ATOM   11754 N N    . SER C 1 208 ? 10.469  -12.515 32.750  1.00 90.77  ? 208 SER C N    1 
ATOM   11755 C CA   . SER C 1 208 ? 9.894   -12.557 31.414  1.00 90.33  ? 208 SER C CA   1 
ATOM   11756 C C    . SER C 1 208 ? 11.022  -12.555 30.396  1.00 89.53  ? 208 SER C C    1 
ATOM   11757 O O    . SER C 1 208 ? 12.099  -12.006 30.645  1.00 89.12  ? 208 SER C O    1 
ATOM   11758 C CB   . SER C 1 208 ? 8.961   -11.371 31.151  1.00 90.18  ? 208 SER C CB   1 
ATOM   11759 O OG   . SER C 1 208 ? 7.696   -11.583 31.745  1.00 102.00 ? 208 SER C OG   1 
ATOM   11760 H H    . SER C 1 208 ? 11.288  -12.255 32.766  1.00 108.92 ? 208 SER C H    1 
ATOM   11761 H HA   . SER C 1 208 ? 9.384   -13.376 31.318  1.00 108.39 ? 208 SER C HA   1 
ATOM   11762 H HB2  . SER C 1 208 ? 9.356   -10.569 31.529  1.00 108.22 ? 208 SER C HB2  1 
ATOM   11763 H HB3  . SER C 1 208 ? 8.846   -11.265 30.194  1.00 108.22 ? 208 SER C HB3  1 
ATOM   11764 H HG   . SER C 1 208 ? 7.193   -10.928 31.590  1.00 122.40 ? 208 SER C HG   1 
ATOM   11765 N N    . CYS C 1 209 ? 10.755  -13.163 29.243  1.00 89.23  ? 209 CYS C N    1 
ATOM   11766 C CA   . CYS C 1 209 ? 11.677  -13.147 28.110  1.00 90.80  ? 209 CYS C CA   1 
ATOM   11767 C C    . CYS C 1 209 ? 10.849  -13.051 26.834  1.00 85.96  ? 209 CYS C C    1 
ATOM   11768 O O    . CYS C 1 209 ? 10.225  -14.034 26.421  1.00 84.38  ? 209 CYS C O    1 
ATOM   11769 C CB   . CYS C 1 209 ? 12.561  -14.396 28.100  1.00 91.62  ? 209 CYS C CB   1 
ATOM   11770 S SG   . CYS C 1 209 ? 14.104  -14.219 27.165  1.00 93.15  ? 209 CYS C SG   1 
ATOM   11771 H H    . CYS C 1 209 ? 10.031  -13.601 29.090  1.00 107.08 ? 209 CYS C H    1 
ATOM   11772 H HA   . CYS C 1 209 ? 12.250  -12.367 28.164  1.00 108.96 ? 209 CYS C HA   1 
ATOM   11773 H HB2  . CYS C 1 209 ? 12.796  -14.615 29.015  1.00 109.95 ? 209 CYS C HB2  1 
ATOM   11774 H HB3  . CYS C 1 209 ? 12.060  -15.126 27.703  1.00 109.95 ? 209 CYS C HB3  1 
ATOM   11775 H HG   . CYS C 1 209 ? 14.703  -15.258 27.200  1.00 111.78 ? 209 CYS C HG   1 
ATOM   11776 N N    . ALA C 1 210 ? 10.839  -11.868 26.213  1.00 88.37  ? 210 ALA C N    1 
ATOM   11777 C CA   . ALA C 1 210 ? 10.089  -11.692 24.972  1.00 88.08  ? 210 ALA C CA   1 
ATOM   11778 C C    . ALA C 1 210 ? 10.684  -12.527 23.844  1.00 86.55  ? 210 ALA C C    1 
ATOM   11779 O O    . ALA C 1 210 ? 9.947   -13.130 23.053  1.00 84.24  ? 210 ALA C O    1 
ATOM   11780 C CB   . ALA C 1 210 ? 10.055  -10.216 24.580  1.00 82.46  ? 210 ALA C CB   1 
ATOM   11781 H H    . ALA C 1 210 ? 11.253  -11.164 26.485  1.00 106.05 ? 210 ALA C H    1 
ATOM   11782 H HA   . ALA C 1 210 ? 9.176   -11.986 25.118  1.00 105.69 ? 210 ALA C HA   1 
ATOM   11783 H HB1  . ALA C 1 210 ? 9.546   -10.118 23.760  1.00 98.95  ? 210 ALA C HB1  1 
ATOM   11784 H HB2  . ALA C 1 210 ? 9.634   -9.709  25.292  1.00 98.95  ? 210 ALA C HB2  1 
ATOM   11785 H HB3  . ALA C 1 210 ? 10.963  -9.903  24.445  1.00 98.95  ? 210 ALA C HB3  1 
ATOM   11786 N N    . SER C 1 211 ? 12.016  -12.578 23.759  1.00 87.74  ? 211 SER C N    1 
ATOM   11787 C CA   . SER C 1 211 ? 12.657  -13.389 22.727  1.00 85.41  ? 211 SER C CA   1 
ATOM   11788 C C    . SER C 1 211 ? 12.460  -14.881 22.981  1.00 90.80  ? 211 SER C C    1 
ATOM   11789 O O    . SER C 1 211 ? 12.525  -15.684 22.045  1.00 89.99  ? 211 SER C O    1 
ATOM   11790 C CB   . SER C 1 211 ? 14.146  -13.065 22.653  1.00 86.83  ? 211 SER C CB   1 
ATOM   11791 O OG   . SER C 1 211 ? 14.873  -13.815 23.614  1.00 96.72  ? 211 SER C OG   1 
ATOM   11792 H H    . SER C 1 211 ? 12.560  -12.160 24.278  1.00 105.29 ? 211 SER C H    1 
ATOM   11793 H HA   . SER C 1 211 ? 12.256  -13.171 21.871  1.00 102.50 ? 211 SER C HA   1 
ATOM   11794 H HB2  . SER C 1 211 ? 14.473  -13.285 21.767  1.00 104.20 ? 211 SER C HB2  1 
ATOM   11795 H HB3  . SER C 1 211 ? 14.273  -12.120 22.829  1.00 104.20 ? 211 SER C HB3  1 
ATOM   11796 H HG   . SER C 1 211 ? 15.693  -13.644 23.551  1.00 116.07 ? 211 SER C HG   1 
ATOM   11797 N N    . GLY C 1 212 ? 12.244  -15.279 24.235  1.00 90.83  ? 212 GLY C N    1 
ATOM   11798 C CA   . GLY C 1 212 ? 11.983  -16.671 24.560  1.00 90.51  ? 212 GLY C CA   1 
ATOM   11799 C C    . GLY C 1 212 ? 10.552  -17.075 24.261  1.00 87.76  ? 212 GLY C C    1 
ATOM   11800 O O    . GLY C 1 212 ? 10.296  -18.177 23.766  1.00 87.79  ? 212 GLY C O    1 
ATOM   11801 H H    . GLY C 1 212 ? 12.245  -14.754 24.917  1.00 109.00 ? 212 GLY C H    1 
ATOM   11802 H HA2  . GLY C 1 212 ? 12.575  -17.239 24.043  1.00 108.61 ? 212 GLY C HA2  1 
ATOM   11803 H HA3  . GLY C 1 212 ? 12.150  -16.818 25.504  1.00 108.61 ? 212 GLY C HA3  1 
ATOM   11804 N N    . THR C 1 213 ? 9.606   -16.184 24.571  1.00 87.74  ? 213 THR C N    1 
ATOM   11805 C CA   . THR C 1 213 ? 8.229   -16.386 24.130  1.00 87.53  ? 213 THR C CA   1 
ATOM   11806 C C    . THR C 1 213 ? 8.146   -16.455 22.611  1.00 89.98  ? 213 THR C C    1 
ATOM   11807 O O    . THR C 1 213 ? 7.319   -17.195 22.063  1.00 86.72  ? 213 THR C O    1 
ATOM   11808 C CB   . THR C 1 213 ? 7.341   -15.258 24.659  1.00 86.76  ? 213 THR C CB   1 
ATOM   11809 O OG1  . THR C 1 213 ? 7.708   -14.951 26.012  1.00 89.34  ? 213 THR C OG1  1 
ATOM   11810 C CG2  . THR C 1 213 ? 5.876   -15.659 24.615  1.00 88.97  ? 213 THR C CG2  1 
ATOM   11811 H H    . THR C 1 213 ? 9.735   -15.468 25.028  1.00 105.29 ? 213 THR C H    1 
ATOM   11812 H HA   . THR C 1 213 ? 7.898   -17.222 24.493  1.00 105.03 ? 213 THR C HA   1 
ATOM   11813 H HB   . THR C 1 213 ? 7.457   -14.471 24.104  1.00 104.11 ? 213 THR C HB   1 
ATOM   11814 H HG1  . THR C 1 213 ? 7.228   -14.328 26.306  1.00 107.21 ? 213 THR C HG1  1 
ATOM   11815 H HG21 . THR C 1 213 ? 5.324   -14.937 24.953  1.00 106.76 ? 213 THR C HG21 1 
ATOM   11816 H HG22 . THR C 1 213 ? 5.613   -15.857 23.703  1.00 106.76 ? 213 THR C HG22 1 
ATOM   11817 H HG23 . THR C 1 213 ? 5.731   -16.447 25.162  1.00 106.76 ? 213 THR C HG23 1 
ATOM   11818 N N    . THR C 1 214 ? 8.989   -15.689 21.916  1.00 88.32  ? 214 THR C N    1 
ATOM   11819 C CA   . THR C 1 214 ? 9.053   -15.775 20.462  1.00 85.95  ? 214 THR C CA   1 
ATOM   11820 C C    . THR C 1 214 ? 9.518   -17.161 20.029  1.00 90.46  ? 214 THR C C    1 
ATOM   11821 O O    . THR C 1 214 ? 8.887   -17.807 19.186  1.00 90.68  ? 214 THR C O    1 
ATOM   11822 C CB   . THR C 1 214 ? 9.987   -14.686 19.928  1.00 85.72  ? 214 THR C CB   1 
ATOM   11823 O OG1  . THR C 1 214 ? 9.289   -13.434 19.846  1.00 84.12  ? 214 THR C OG1  1 
ATOM   11824 C CG2  . THR C 1 214 ? 10.488  -15.030 18.554  1.00 92.08  ? 214 THR C CG2  1 
ATOM   11825 H H    . THR C 1 214 ? 9.530   -15.116 22.262  1.00 105.98 ? 214 THR C H    1 
ATOM   11826 H HA   . THR C 1 214 ? 8.172   -15.625 20.084  1.00 103.13 ? 214 THR C HA   1 
ATOM   11827 H HB   . THR C 1 214 ? 10.742  -14.609 20.532  1.00 102.87 ? 214 THR C HB   1 
ATOM   11828 H HG1  . THR C 1 214 ? 9.803   -12.838 19.553  1.00 100.94 ? 214 THR C HG1  1 
ATOM   11829 H HG21 . THR C 1 214 ? 11.078  -14.331 18.231  1.00 110.50 ? 214 THR C HG21 1 
ATOM   11830 H HG22 . THR C 1 214 ? 10.977  -15.867 18.579  1.00 110.50 ? 214 THR C HG22 1 
ATOM   11831 H HG23 . THR C 1 214 ? 9.741   -15.120 17.941  1.00 110.50 ? 214 THR C HG23 1 
ATOM   11832 N N    . ALA C 1 215 ? 10.641  -17.626 20.584  1.00 89.77  ? 215 ALA C N    1 
ATOM   11833 C CA   . ALA C 1 215 ? 11.137  -18.960 20.252  1.00 91.31  ? 215 ALA C CA   1 
ATOM   11834 C C    . ALA C 1 215 ? 10.063  -20.011 20.498  1.00 91.52  ? 215 ALA C C    1 
ATOM   11835 O O    . ALA C 1 215 ? 9.810   -20.873 19.650  1.00 90.72  ? 215 ALA C O    1 
ATOM   11836 C CB   . ALA C 1 215 ? 12.390  -19.270 21.071  1.00 95.11  ? 215 ALA C CB   1 
ATOM   11837 H H    . ALA C 1 215 ? 11.127  -17.194 21.147  1.00 107.72 ? 215 ALA C H    1 
ATOM   11838 H HA   . ALA C 1 215 ? 11.378  -18.983 19.313  1.00 109.58 ? 215 ALA C HA   1 
ATOM   11839 H HB1  . ALA C 1 215 ? 12.685  -20.172 20.868  1.00 114.13 ? 215 ALA C HB1  1 
ATOM   11840 H HB2  . ALA C 1 215 ? 13.085  -18.635 20.838  1.00 114.13 ? 215 ALA C HB2  1 
ATOM   11841 H HB3  . ALA C 1 215 ? 12.178  -19.196 22.015  1.00 114.13 ? 215 ALA C HB3  1 
ATOM   11842 N N    . LEU C 1 216 ? 9.426   -19.955 21.669  1.00 91.13  ? 216 LEU C N    1 
ATOM   11843 C CA   . LEU C 1 216 ? 8.307   -20.847 21.961  1.00 91.11  ? 216 LEU C CA   1 
ATOM   11844 C C    . LEU C 1 216 ? 7.259   -20.779 20.858  1.00 92.63  ? 216 LEU C C    1 
ATOM   11845 O O    . LEU C 1 216 ? 6.805   -21.811 20.353  1.00 93.81  ? 216 LEU C O    1 
ATOM   11846 C CB   . LEU C 1 216 ? 7.706   -20.470 23.315  1.00 90.98  ? 216 LEU C CB   1 
ATOM   11847 C CG   . LEU C 1 216 ? 6.533   -21.214 23.956  1.00 94.02  ? 216 LEU C CG   1 
ATOM   11848 C CD1  . LEU C 1 216 ? 5.246   -21.057 23.155  1.00 95.57  ? 216 LEU C CD1  1 
ATOM   11849 C CD2  . LEU C 1 216 ? 6.858   -22.693 24.176  1.00 92.85  ? 216 LEU C CD2  1 
ATOM   11850 H H    . LEU C 1 216 ? 9.621   -19.413 22.308  1.00 109.36 ? 216 LEU C H    1 
ATOM   11851 H HA   . LEU C 1 216 ? 8.622   -21.762 22.013  1.00 109.33 ? 216 LEU C HA   1 
ATOM   11852 H HB2  . LEU C 1 216 ? 8.428   -20.532 23.960  1.00 109.17 ? 216 LEU C HB2  1 
ATOM   11853 H HB3  . LEU C 1 216 ? 7.410   -19.550 23.235  1.00 109.17 ? 216 LEU C HB3  1 
ATOM   11854 H HG   . LEU C 1 216 ? 6.378   -20.812 24.825  1.00 112.83 ? 216 LEU C HG   1 
ATOM   11855 H HD11 . LEU C 1 216 ? 4.511   -21.440 23.658  1.00 114.69 ? 216 LEU C HD11 1 
ATOM   11856 H HD12 . LEU C 1 216 ? 5.084   -20.113 22.999  1.00 114.69 ? 216 LEU C HD12 1 
ATOM   11857 H HD13 . LEU C 1 216 ? 5.344   -21.519 22.307  1.00 114.69 ? 216 LEU C HD13 1 
ATOM   11858 H HD21 . LEU C 1 216 ? 6.086   -23.132 24.564  1.00 111.41 ? 216 LEU C HD21 1 
ATOM   11859 H HD22 . LEU C 1 216 ? 7.075   -23.099 23.322  1.00 111.41 ? 216 LEU C HD22 1 
ATOM   11860 H HD23 . LEU C 1 216 ? 7.616   -22.764 24.777  1.00 111.41 ? 216 LEU C HD23 1 
ATOM   11861 N N    . GLY C 1 217 ? 6.870   -19.564 20.465  1.00 92.99  ? 217 GLY C N    1 
ATOM   11862 C CA   . GLY C 1 217 ? 5.814   -19.419 19.476  1.00 89.43  ? 217 GLY C CA   1 
ATOM   11863 C C    . GLY C 1 217 ? 6.160   -20.077 18.157  1.00 94.91  ? 217 GLY C C    1 
ATOM   11864 O O    . GLY C 1 217 ? 5.345   -20.796 17.573  1.00 97.16  ? 217 GLY C O    1 
ATOM   11865 H H    . GLY C 1 217 ? 7.198   -18.823 20.753  1.00 111.59 ? 217 GLY C H    1 
ATOM   11866 H HA2  . GLY C 1 217 ? 5.000   -19.824 19.815  1.00 107.31 ? 217 GLY C HA2  1 
ATOM   11867 H HA3  . GLY C 1 217 ? 5.654   -18.476 19.314  1.00 107.31 ? 217 GLY C HA3  1 
ATOM   11868 N N    . TYR C 1 218 ? 7.375   -19.830 17.662  1.00 94.43  ? 218 TYR C N    1 
ATOM   11869 C CA   . TYR C 1 218 ? 7.804   -20.458 16.419  1.00 92.02  ? 218 TYR C CA   1 
ATOM   11870 C C    . TYR C 1 218 ? 7.653   -21.974 16.498  1.00 95.43  ? 218 TYR C C    1 
ATOM   11871 O O    . TYR C 1 218 ? 7.038   -22.599 15.628  1.00 97.82  ? 218 TYR C O    1 
ATOM   11872 C CB   . TYR C 1 218 ? 9.256   -20.091 16.110  1.00 91.75  ? 218 TYR C CB   1 
ATOM   11873 C CG   . TYR C 1 218 ? 9.481   -18.641 15.744  1.00 93.38  ? 218 TYR C CG   1 
ATOM   11874 C CD1  . TYR C 1 218 ? 8.627   -17.973 14.871  1.00 90.06  ? 218 TYR C CD1  1 
ATOM   11875 C CD2  . TYR C 1 218 ? 10.559  -17.940 16.268  1.00 94.00  ? 218 TYR C CD2  1 
ATOM   11876 C CE1  . TYR C 1 218 ? 8.840   -16.644 14.540  1.00 87.88  ? 218 TYR C CE1  1 
ATOM   11877 C CE2  . TYR C 1 218 ? 10.781  -16.619 15.936  1.00 93.41  ? 218 TYR C CE2  1 
ATOM   11878 C CZ   . TYR C 1 218 ? 9.919   -15.973 15.078  1.00 93.27  ? 218 TYR C CZ   1 
ATOM   11879 O OH   . TYR C 1 218 ? 10.152  -14.652 14.766  1.00 91.22  ? 218 TYR C OH   1 
ATOM   11880 H H    . TYR C 1 218 ? 7.958   -19.311 18.023  1.00 113.31 ? 218 TYR C H    1 
ATOM   11881 H HA   . TYR C 1 218 ? 7.250   -20.125 15.696  1.00 110.42 ? 218 TYR C HA   1 
ATOM   11882 H HB2  . TYR C 1 218 ? 9.794   -20.280 16.894  1.00 110.10 ? 218 TYR C HB2  1 
ATOM   11883 H HB3  . TYR C 1 218 ? 9.557   -20.630 15.362  1.00 110.10 ? 218 TYR C HB3  1 
ATOM   11884 H HD1  . TYR C 1 218 ? 7.902   -18.425 14.505  1.00 108.06 ? 218 TYR C HD1  1 
ATOM   11885 H HD2  . TYR C 1 218 ? 11.142  -18.368 16.853  1.00 112.81 ? 218 TYR C HD2  1 
ATOM   11886 H HE1  . TYR C 1 218 ? 8.259   -16.208 13.960  1.00 105.46 ? 218 TYR C HE1  1 
ATOM   11887 H HE2  . TYR C 1 218 ? 11.511  -16.166 16.292  1.00 112.09 ? 218 TYR C HE2  1 
ATOM   11888 H HH   . TYR C 1 218 ? 10.835  -14.377 15.170  1.00 109.47 ? 218 TYR C HH   1 
ATOM   11889 N N    . TYR C 1 219 ? 8.212   -22.583 17.549  1.00 94.94  ? 219 TYR C N    1 
ATOM   11890 C CA   . TYR C 1 219 ? 8.136   -24.033 17.689  1.00 96.95  ? 219 TYR C CA   1 
ATOM   11891 C C    . TYR C 1 219 ? 6.694   -24.506 17.819  1.00 99.03  ? 219 TYR C C    1 
ATOM   11892 O O    . TYR C 1 219 ? 6.351   -25.586 17.327  1.00 99.85  ? 219 TYR C O    1 
ATOM   11893 C CB   . TYR C 1 219 ? 8.969   -24.479 18.895  1.00 99.05  ? 219 TYR C CB   1 
ATOM   11894 C CG   . TYR C 1 219 ? 8.486   -25.745 19.572  1.00 104.67 ? 219 TYR C CG   1 
ATOM   11895 C CD1  . TYR C 1 219 ? 7.517   -25.696 20.573  1.00 103.12 ? 219 TYR C CD1  1 
ATOM   11896 C CD2  . TYR C 1 219 ? 9.011   -26.985 19.227  1.00 105.83 ? 219 TYR C CD2  1 
ATOM   11897 C CE1  . TYR C 1 219 ? 7.073   -26.847 21.196  1.00 105.08 ? 219 TYR C CE1  1 
ATOM   11898 C CE2  . TYR C 1 219 ? 8.575   -28.143 19.845  1.00 109.09 ? 219 TYR C CE2  1 
ATOM   11899 C CZ   . TYR C 1 219 ? 7.607   -28.069 20.828  1.00 112.21 ? 219 TYR C CZ   1 
ATOM   11900 O OH   . TYR C 1 219 ? 7.168   -29.218 21.449  1.00 117.44 ? 219 TYR C OH   1 
ATOM   11901 H H    . TYR C 1 219 ? 8.633   -22.183 18.183  1.00 113.93 ? 219 TYR C H    1 
ATOM   11902 H HA   . TYR C 1 219 ? 8.510   -24.453 16.899  1.00 116.35 ? 219 TYR C HA   1 
ATOM   11903 H HB2  . TYR C 1 219 ? 9.879   -24.637 18.598  1.00 118.86 ? 219 TYR C HB2  1 
ATOM   11904 H HB3  . TYR C 1 219 ? 8.955   -23.771 19.557  1.00 118.86 ? 219 TYR C HB3  1 
ATOM   11905 H HD1  . TYR C 1 219 ? 7.162   -24.874 20.826  1.00 123.75 ? 219 TYR C HD1  1 
ATOM   11906 H HD2  . TYR C 1 219 ? 9.667   -27.037 18.570  1.00 126.99 ? 219 TYR C HD2  1 
ATOM   11907 H HE1  . TYR C 1 219 ? 6.420   -26.801 21.857  1.00 126.09 ? 219 TYR C HE1  1 
ATOM   11908 H HE2  . TYR C 1 219 ? 8.931   -28.967 19.600  1.00 130.91 ? 219 TYR C HE2  1 
ATOM   11909 H HH   . TYR C 1 219 ? 7.553   -29.888 21.120  1.00 140.93 ? 219 TYR C HH   1 
ATOM   11910 N N    . LEU C 1 220 ? 5.835   -23.717 18.468  1.00 99.47  ? 220 LEU C N    1 
ATOM   11911 C CA   . LEU C 1 220 ? 4.441   -24.122 18.603  1.00 101.94 ? 220 LEU C CA   1 
ATOM   11912 C C    . LEU C 1 220 ? 3.697   -23.995 17.280  1.00 103.02 ? 220 LEU C C    1 
ATOM   11913 O O    . LEU C 1 220 ? 2.737   -24.736 17.037  1.00 105.69 ? 220 LEU C O    1 
ATOM   11914 C CB   . LEU C 1 220 ? 3.742   -23.290 19.677  1.00 99.02  ? 220 LEU C CB   1 
ATOM   11915 C CG   . LEU C 1 220 ? 3.895   -23.708 21.139  1.00 96.42  ? 220 LEU C CG   1 
ATOM   11916 C CD1  . LEU C 1 220 ? 2.942   -22.884 22.009  1.00 92.91  ? 220 LEU C CD1  1 
ATOM   11917 C CD2  . LEU C 1 220 ? 3.646   -25.187 21.362  1.00 93.41  ? 220 LEU C CD2  1 
ATOM   11918 H H    . LEU C 1 220 ? 6.032   -22.962 18.830  1.00 119.36 ? 220 LEU C H    1 
ATOM   11919 H HA   . LEU C 1 220 ? 4.416   -25.050 18.885  1.00 122.33 ? 220 LEU C HA   1 
ATOM   11920 H HB2  . LEU C 1 220 ? 4.081   -22.384 19.612  1.00 118.83 ? 220 LEU C HB2  1 
ATOM   11921 H HB3  . LEU C 1 220 ? 2.791   -23.303 19.484  1.00 118.83 ? 220 LEU C HB3  1 
ATOM   11922 H HG   . LEU C 1 220 ? 4.815   -23.542 21.399  1.00 115.71 ? 220 LEU C HG   1 
ATOM   11923 H HD11 . LEU C 1 220 ? 3.143   -23.051 22.943  1.00 111.50 ? 220 LEU C HD11 1 
ATOM   11924 H HD12 . LEU C 1 220 ? 3.065   -21.943 21.807  1.00 111.50 ? 220 LEU C HD12 1 
ATOM   11925 H HD13 . LEU C 1 220 ? 2.029   -23.148 21.814  1.00 111.50 ? 220 LEU C HD13 1 
ATOM   11926 H HD21 . LEU C 1 220 ? 3.550   -25.352 22.314  1.00 112.09 ? 220 LEU C HD21 1 
ATOM   11927 H HD22 . LEU C 1 220 ? 2.833   -25.444 20.899  1.00 112.09 ? 220 LEU C HD22 1 
ATOM   11928 H HD23 . LEU C 1 220 ? 4.398   -25.691 21.013  1.00 112.09 ? 220 LEU C HD23 1 
ATOM   11929 N N    . LYS C 1 221 ? 4.116   -23.065 16.417  1.00 102.01 ? 221 LYS C N    1 
ATOM   11930 C CA   . LYS C 1 221 ? 3.469   -22.927 15.116  1.00 102.81 ? 221 LYS C CA   1 
ATOM   11931 C C    . LYS C 1 221 ? 3.767   -24.121 14.218  1.00 102.45 ? 221 LYS C C    1 
ATOM   11932 O O    . LYS C 1 221 ? 2.940   -24.477 13.371  1.00 106.08 ? 221 LYS C O    1 
ATOM   11933 C CB   . LYS C 1 221 ? 3.911   -21.626 14.445  1.00 99.48  ? 221 LYS C CB   1 
ATOM   11934 C CG   . LYS C 1 221 ? 3.436   -21.458 13.000  1.00 102.53 ? 221 LYS C CG   1 
ATOM   11935 C CD   . LYS C 1 221 ? 1.914   -21.438 12.898  1.00 104.91 ? 221 LYS C CD   1 
ATOM   11936 C CE   . LYS C 1 221 ? 1.428   -21.639 11.461  1.00 106.49 ? 221 LYS C CE   1 
ATOM   11937 N NZ   . LYS C 1 221 ? 2.135   -22.735 10.732  1.00 100.58 ? 221 LYS C NZ   1 
ATOM   11938 H H    . LYS C 1 221 ? 4.760   -22.513 16.559  1.00 122.41 ? 221 LYS C H    1 
ATOM   11939 H HA   . LYS C 1 221 ? 2.509   -22.881 15.244  1.00 123.37 ? 221 LYS C HA   1 
ATOM   11940 H HB2  . LYS C 1 221 ? 3.560   -20.880 14.956  1.00 119.38 ? 221 LYS C HB2  1 
ATOM   11941 H HB3  . LYS C 1 221 ? 4.881   -21.596 14.439  1.00 119.38 ? 221 LYS C HB3  1 
ATOM   11942 H HG2  . LYS C 1 221 ? 3.775   -20.620 12.647  1.00 123.03 ? 221 LYS C HG2  1 
ATOM   11943 H HG3  . LYS C 1 221 ? 3.765   -22.199 12.467  1.00 123.03 ? 221 LYS C HG3  1 
ATOM   11944 H HD2  . LYS C 1 221 ? 1.549   -22.152 13.443  1.00 125.89 ? 221 LYS C HD2  1 
ATOM   11945 H HD3  . LYS C 1 221 ? 1.586   -20.580 13.211  1.00 125.89 ? 221 LYS C HD3  1 
ATOM   11946 H HE2  . LYS C 1 221 ? 0.483   -21.859 11.479  1.00 127.79 ? 221 LYS C HE2  1 
ATOM   11947 H HE3  . LYS C 1 221 ? 1.568   -20.817 10.965  1.00 127.79 ? 221 LYS C HE3  1 
ATOM   11948 H HZ1  . LYS C 1 221 ? 1.723   -22.904 9.961   1.00 120.69 ? 221 LYS C HZ1  1 
ATOM   11949 H HZ2  . LYS C 1 221 ? 2.976   -22.495 10.563  1.00 120.69 ? 221 LYS C HZ2  1 
ATOM   11950 H HZ3  . LYS C 1 221 ? 2.140   -23.475 11.226  1.00 120.69 ? 221 LYS C HZ3  1 
ATOM   11951 N N    . LYS C 1 222 ? 4.928   -24.754 14.390  1.00 104.76 ? 222 LYS C N    1 
ATOM   11952 C CA   . LYS C 1 222 ? 5.283   -25.940 13.618  1.00 105.58 ? 222 LYS C CA   1 
ATOM   11953 C C    . LYS C 1 222 ? 4.729   -27.210 14.255  1.00 108.41 ? 222 LYS C C    1 
ATOM   11954 O O    . LYS C 1 222 ? 4.121   -28.042 13.576  1.00 116.11 ? 222 LYS C O    1 
ATOM   11955 C CB   . LYS C 1 222 ? 6.806   -26.064 13.495  1.00 104.68 ? 222 LYS C CB   1 
ATOM   11956 C CG   . LYS C 1 222 ? 7.519   -24.772 13.163  1.00 107.03 ? 222 LYS C CG   1 
ATOM   11957 C CD   . LYS C 1 222 ? 7.613   -24.580 11.661  1.00 111.39 ? 222 LYS C CD   1 
ATOM   11958 C CE   . LYS C 1 222 ? 7.876   -23.131 11.319  1.00 111.50 ? 222 LYS C CE   1 
ATOM   11959 N NZ   . LYS C 1 222 ? 8.766   -23.026 10.140  1.00 109.44 ? 222 LYS C NZ   1 
ATOM   11960 H H    . LYS C 1 222 ? 5.532   -24.513 14.952  1.00 125.71 ? 222 LYS C H    1 
ATOM   11961 H HA   . LYS C 1 222 ? 4.911   -25.843 12.728  1.00 126.70 ? 222 LYS C HA   1 
ATOM   11962 H HB2  . LYS C 1 222 ? 7.159   -26.384 14.340  1.00 125.62 ? 222 LYS C HB2  1 
ATOM   11963 H HB3  . LYS C 1 222 ? 7.008   -26.699 12.790  1.00 125.62 ? 222 LYS C HB3  1 
ATOM   11964 H HG2  . LYS C 1 222 ? 7.027   -24.025 13.539  1.00 128.43 ? 222 LYS C HG2  1 
ATOM   11965 H HG3  . LYS C 1 222 ? 8.418   -24.795 13.527  1.00 128.43 ? 222 LYS C HG3  1 
ATOM   11966 H HD2  . LYS C 1 222 ? 8.341   -25.116 11.311  1.00 133.66 ? 222 LYS C HD2  1 
ATOM   11967 H HD3  . LYS C 1 222 ? 6.776   -24.847 11.248  1.00 133.66 ? 222 LYS C HD3  1 
ATOM   11968 H HE2  . LYS C 1 222 ? 7.037   -22.689 11.113  1.00 133.80 ? 222 LYS C HE2  1 
ATOM   11969 H HE3  . LYS C 1 222 ? 8.306   -22.694 12.070  1.00 133.80 ? 222 LYS C HE3  1 
ATOM   11970 H HZ1  . LYS C 1 222 ? 8.904   -22.170 9.938   1.00 131.33 ? 222 LYS C HZ1  1 
ATOM   11971 H HZ2  . LYS C 1 222 ? 9.549   -23.411 10.314  1.00 131.33 ? 222 LYS C HZ2  1 
ATOM   11972 H HZ3  . LYS C 1 222 ? 8.394   -23.431 9.440   1.00 131.33 ? 222 LYS C HZ3  1 
ATOM   11973 N N    . CYS C 1 223 ? 4.941   -27.366 15.560  1.00 112.02 ? 223 CYS C N    1 
ATOM   11974 C CA   . CYS C 1 223 ? 4.596   -28.591 16.271  1.00 118.92 ? 223 CYS C CA   1 
ATOM   11975 C C    . CYS C 1 223 ? 3.107   -28.704 16.572  1.00 122.01 ? 223 CYS C C    1 
ATOM   11976 O O    . CYS C 1 223 ? 2.625   -29.815 16.818  1.00 126.01 ? 223 CYS C O    1 
ATOM   11977 C CB   . CYS C 1 223 ? 5.415   -28.655 17.568  1.00 113.20 ? 223 CYS C CB   1 
ATOM   11978 S SG   . CYS C 1 223 ? 4.928   -29.919 18.750  1.00 136.56 ? 223 CYS C SG   1 
ATOM   11979 H H    . CYS C 1 223 ? 5.291   -26.765 16.066  1.00 134.42 ? 223 CYS C H    1 
ATOM   11980 H HA   . CYS C 1 223 ? 4.825   -29.362 15.728  1.00 142.71 ? 223 CYS C HA   1 
ATOM   11981 H HB2  . CYS C 1 223 ? 6.340   -28.824 17.333  1.00 135.85 ? 223 CYS C HB2  1 
ATOM   11982 H HB3  . CYS C 1 223 ? 5.337   -27.798 18.016  1.00 135.85 ? 223 CYS C HB3  1 
ATOM   11983 H HG   . CYS C 1 223 ? 5.709   -29.922 19.662  1.00 163.87 ? 223 CYS C HG   1 
ATOM   11984 N N    . LYS C 1 224 ? 2.371   -27.593 16.539  1.00 115.84 ? 224 LYS C N    1 
ATOM   11985 C CA   . LYS C 1 224 ? 0.936   -27.596 16.792  1.00 114.68 ? 224 LYS C CA   1 
ATOM   11986 C C    . LYS C 1 224 ? 0.124   -26.876 15.725  1.00 112.07 ? 224 LYS C C    1 
ATOM   11987 O O    . LYS C 1 224 ? -1.059  -27.195 15.572  1.00 112.64 ? 224 LYS C O    1 
ATOM   11988 C CB   . LYS C 1 224 ? 0.634   -26.952 18.159  1.00 116.48 ? 224 LYS C CB   1 
ATOM   11989 C CG   . LYS C 1 224 ? -0.727  -27.306 18.795  1.00 121.00 ? 224 LYS C CG   1 
ATOM   11990 C CD   . LYS C 1 224 ? -1.901  -26.676 18.040  1.00 122.54 ? 224 LYS C CD   1 
ATOM   11991 C CE   . LYS C 1 224 ? -3.066  -26.281 18.942  1.00 122.96 ? 224 LYS C CE   1 
ATOM   11992 N NZ   . LYS C 1 224 ? -4.100  -25.532 18.158  1.00 117.73 ? 224 LYS C NZ   1 
ATOM   11993 H H    . LYS C 1 224 ? 2.689   -26.812 16.370  1.00 139.02 ? 224 LYS C H    1 
ATOM   11994 H HA   . LYS C 1 224 ? 0.627   -28.515 16.825  1.00 137.62 ? 224 LYS C HA   1 
ATOM   11995 H HB2  . LYS C 1 224 ? 1.322   -27.232 18.783  1.00 139.77 ? 224 LYS C HB2  1 
ATOM   11996 H HB3  . LYS C 1 224 ? 0.657   -25.989 18.050  1.00 139.77 ? 224 LYS C HB3  1 
ATOM   11997 H HG2  . LYS C 1 224 ? -0.842  -28.269 18.784  1.00 145.20 ? 224 LYS C HG2  1 
ATOM   11998 H HG3  . LYS C 1 224 ? -0.745  -26.980 19.708  1.00 145.20 ? 224 LYS C HG3  1 
ATOM   11999 H HD2  . LYS C 1 224 ? -1.591  -25.875 17.589  1.00 147.05 ? 224 LYS C HD2  1 
ATOM   12000 H HD3  . LYS C 1 224 ? -2.234  -27.315 17.390  1.00 147.05 ? 224 LYS C HD3  1 
ATOM   12001 H HE2  . LYS C 1 224 ? -3.476  -27.079 19.313  1.00 147.56 ? 224 LYS C HE2  1 
ATOM   12002 H HE3  . LYS C 1 224 ? -2.745  -25.710 19.657  1.00 147.56 ? 224 LYS C HE3  1 
ATOM   12003 H HZ1  . LYS C 1 224 ? -4.787  -25.322 18.684  1.00 141.28 ? 224 LYS C HZ1  1 
ATOM   12004 H HZ2  . LYS C 1 224 ? -3.749  -24.784 17.828  1.00 141.28 ? 224 LYS C HZ2  1 
ATOM   12005 H HZ3  . LYS C 1 224 ? -4.395  -26.034 17.485  1.00 141.28 ? 224 LYS C HZ3  1 
ATOM   12006 N N    . ASN C 1 225 ? 0.717   -25.956 14.960  1.00 109.89 ? 225 ASN C N    1 
ATOM   12007 C CA   . ASN C 1 225 ? -0.032  -25.044 14.095  1.00 108.70 ? 225 ASN C CA   1 
ATOM   12008 C C    . ASN C 1 225 ? -0.796  -24.028 14.945  1.00 109.39 ? 225 ASN C C    1 
ATOM   12009 O O    . ASN C 1 225 ? -1.920  -23.640 14.620  1.00 110.77 ? 225 ASN C O    1 
ATOM   12010 C CB   . ASN C 1 225 ? -0.978  -25.798 13.159  1.00 109.15 ? 225 ASN C CB   1 
ATOM   12011 C CG   . ASN C 1 225 ? -1.686  -24.873 12.174  1.00 108.83 ? 225 ASN C CG   1 
ATOM   12012 O OD1  . ASN C 1 225 ? -1.053  -24.055 11.500  1.00 108.08 ? 225 ASN C OD1  1 
ATOM   12013 N ND2  . ASN C 1 225 ? -3.007  -24.995 12.094  1.00 109.39 ? 225 ASN C ND2  1 
ATOM   12014 H H    . ASN C 1 225 ? 1.569   -25.840 14.924  1.00 131.87 ? 225 ASN C H    1 
ATOM   12015 H HA   . ASN C 1 225 ? 0.591   -24.559 13.532  1.00 130.44 ? 225 ASN C HA   1 
ATOM   12016 H HB2  . ASN C 1 225 ? -0.468  -26.447 12.650  1.00 130.98 ? 225 ASN C HB2  1 
ATOM   12017 H HB3  . ASN C 1 225 ? -1.654  -26.248 13.688  1.00 130.98 ? 225 ASN C HB3  1 
ATOM   12018 H HD21 . ASN C 1 225 ? -3.416  -25.572 12.582  1.00 131.26 ? 225 ASN C HD21 1 
ATOM   12019 H HD22 . ASN C 1 225 ? -3.453  -24.496 11.553  1.00 131.26 ? 225 ASN C HD22 1 
ATOM   12020 N N    . LEU C 1 226 ? -0.178  -23.611 16.052  1.00 108.87 ? 226 LEU C N    1 
ATOM   12021 C CA   . LEU C 1 226 ? -0.731  -22.600 16.951  1.00 105.98 ? 226 LEU C CA   1 
ATOM   12022 C C    . LEU C 1 226 ? -0.155  -21.244 16.557  1.00 104.02 ? 226 LEU C C    1 
ATOM   12023 O O    . LEU C 1 226 ? 1.047   -21.002 16.713  1.00 103.21 ? 226 LEU C O    1 
ATOM   12024 C CB   . LEU C 1 226 ? -0.400  -22.941 18.402  1.00 108.13 ? 226 LEU C CB   1 
ATOM   12025 C CG   . LEU C 1 226 ? -1.097  -22.188 19.534  1.00 104.11 ? 226 LEU C CG   1 
ATOM   12026 C CD1  . LEU C 1 226 ? -2.525  -21.806 19.195  1.00 102.55 ? 226 LEU C CD1  1 
ATOM   12027 C CD2  . LEU C 1 226 ? -1.063  -23.036 20.816  1.00 107.30 ? 226 LEU C CD2  1 
ATOM   12028 H H    . LEU C 1 226 ? 0.587   -23.908 16.310  1.00 130.65 ? 226 LEU C H    1 
ATOM   12029 H HA   . LEU C 1 226 ? -1.696  -22.567 16.858  1.00 127.18 ? 226 LEU C HA   1 
ATOM   12030 H HB2  . LEU C 1 226 ? -0.608  -23.880 18.531  1.00 129.75 ? 226 LEU C HB2  1 
ATOM   12031 H HB3  . LEU C 1 226 ? 0.551   -22.792 18.522  1.00 129.75 ? 226 LEU C HB3  1 
ATOM   12032 H HG   . LEU C 1 226 ? -0.619  -21.357 19.678  1.00 124.93 ? 226 LEU C HG   1 
ATOM   12033 H HD11 . LEU C 1 226 ? -2.920  -21.356 19.958  1.00 123.06 ? 226 LEU C HD11 1 
ATOM   12034 H HD12 . LEU C 1 226 ? -2.519  -21.213 18.428  1.00 123.06 ? 226 LEU C HD12 1 
ATOM   12035 H HD13 . LEU C 1 226 ? -3.026  -22.610 18.988  1.00 123.06 ? 226 LEU C HD13 1 
ATOM   12036 H HD21 . LEU C 1 226 ? -1.512  -22.552 21.526  1.00 128.76 ? 226 LEU C HD21 1 
ATOM   12037 H HD22 . LEU C 1 226 ? -1.516  -23.877 20.650  1.00 128.76 ? 226 LEU C HD22 1 
ATOM   12038 H HD23 . LEU C 1 226 ? -0.139  -23.201 21.061  1.00 128.76 ? 226 LEU C HD23 1 
ATOM   12039 N N    . ASP C 1 227 ? -1.016  -20.355 16.054  1.00 103.43 ? 227 ASP C N    1 
ATOM   12040 C CA   . ASP C 1 227 ? -0.545  -19.073 15.545  1.00 100.52 ? 227 ASP C CA   1 
ATOM   12041 C C    . ASP C 1 227 ? -0.348  -18.042 16.652  1.00 100.43 ? 227 ASP C C    1 
ATOM   12042 O O    . ASP C 1 227 ? 0.525   -17.173 16.529  1.00 98.90  ? 227 ASP C O    1 
ATOM   12043 C CB   . ASP C 1 227 ? -1.525  -18.534 14.496  1.00 102.27 ? 227 ASP C CB   1 
ATOM   12044 C CG   . ASP C 1 227 ? -1.188  -18.991 13.082  1.00 107.45 ? 227 ASP C CG   1 
ATOM   12045 O OD1  . ASP C 1 227 ? -0.806  -20.167 12.903  1.00 104.93 ? 227 ASP C OD1  1 
ATOM   12046 O OD2  . ASP C 1 227 ? -1.310  -18.174 12.143  1.00 113.32 ? 227 ASP C OD2  1 
ATOM   12047 H H    . ASP C 1 227 ? -1.866  -20.472 15.998  1.00 124.11 ? 227 ASP C H    1 
ATOM   12048 H HA   . ASP C 1 227 ? 0.314   -19.210 15.115  1.00 120.62 ? 227 ASP C HA   1 
ATOM   12049 H HB2  . ASP C 1 227 ? -2.418  -18.848 14.708  1.00 122.73 ? 227 ASP C HB2  1 
ATOM   12050 H HB3  . ASP C 1 227 ? -1.503  -17.564 14.511  1.00 122.73 ? 227 ASP C HB3  1 
ATOM   12051 N N    . ARG C 1 228 ? -1.130  -18.111 17.728  1.00 100.07 ? 228 ARG C N    1 
ATOM   12052 C CA   . ARG C 1 228 ? -1.005  -17.147 18.813  1.00 97.65  ? 228 ARG C CA   1 
ATOM   12053 C C    . ARG C 1 228 ? -1.418  -17.794 20.127  1.00 99.56  ? 228 ARG C C    1 
ATOM   12054 O O    . ARG C 1 228 ? -2.195  -18.751 20.155  1.00 102.55 ? 228 ARG C O    1 
ATOM   12055 C CB   . ARG C 1 228 ? -1.855  -15.895 18.555  1.00 97.24  ? 228 ARG C CB   1 
ATOM   12056 C CG   . ARG C 1 228 ? -3.288  -16.003 19.058  1.00 99.10  ? 228 ARG C CG   1 
ATOM   12057 C CD   . ARG C 1 228 ? -4.154  -14.881 18.502  1.00 102.68 ? 228 ARG C CD   1 
ATOM   12058 N NE   . ARG C 1 228 ? -3.808  -13.586 19.076  1.00 102.40 ? 228 ARG C NE   1 
ATOM   12059 C CZ   . ARG C 1 228 ? -4.612  -12.531 19.085  1.00 103.21 ? 228 ARG C CZ   1 
ATOM   12060 N NH1  . ARG C 1 228 ? -5.823  -12.581 18.554  1.00 108.00 ? 228 ARG C NH1  1 
ATOM   12061 N NH2  . ARG C 1 228 ? -4.192  -11.400 19.642  1.00 102.21 ? 228 ARG C NH2  1 
ATOM   12062 H H    . ARG C 1 228 ? -1.739  -18.707 17.851  1.00 120.08 ? 228 ARG C H    1 
ATOM   12063 H HA   . ARG C 1 228 ? -0.075  -16.884 18.887  1.00 117.18 ? 228 ARG C HA   1 
ATOM   12064 H HB2  . ARG C 1 228 ? -1.441  -15.141 19.003  1.00 116.69 ? 228 ARG C HB2  1 
ATOM   12065 H HB3  . ARG C 1 228 ? -1.890  -15.735 17.599  1.00 116.69 ? 228 ARG C HB3  1 
ATOM   12066 H HG2  . ARG C 1 228 ? -3.666  -16.850 18.775  1.00 118.92 ? 228 ARG C HG2  1 
ATOM   12067 H HG3  . ARG C 1 228 ? -3.295  -15.943 20.026  1.00 118.92 ? 228 ARG C HG3  1 
ATOM   12068 H HD2  . ARG C 1 228 ? -4.030  -14.829 17.541  1.00 123.22 ? 228 ARG C HD2  1 
ATOM   12069 H HD3  . ARG C 1 228 ? -5.084  -15.065 18.706  1.00 123.22 ? 228 ARG C HD3  1 
ATOM   12070 H HE   . ARG C 1 228 ? -3.031  -13.500 19.434  1.00 122.89 ? 228 ARG C HE   1 
ATOM   12071 H HH11 . ARG C 1 228 ? -6.105  -13.308 18.192  1.00 129.60 ? 228 ARG C HH11 1 
ATOM   12072 H HH12 . ARG C 1 228 ? -6.328  -11.885 18.570  1.00 129.60 ? 228 ARG C HH12 1 
ATOM   12073 H HH21 . ARG C 1 228 ? -3.407  -11.358 19.991  1.00 122.66 ? 228 ARG C HH21 1 
ATOM   12074 H HH22 . ARG C 1 228 ? -4.705  -10.710 19.653  1.00 122.66 ? 228 ARG C HH22 1 
ATOM   12075 N N    . ALA C 1 229 ? -0.894  -17.247 21.221  1.00 96.61  ? 229 ALA C N    1 
ATOM   12076 C CA   . ALA C 1 229 ? -1.206  -17.748 22.551  1.00 99.05  ? 229 ALA C CA   1 
ATOM   12077 C C    . ALA C 1 229 ? -0.596  -16.816 23.586  1.00 97.28  ? 229 ALA C C    1 
ATOM   12078 O O    . ALA C 1 229 ? 0.432   -16.181 23.337  1.00 95.42  ? 229 ALA C O    1 
ATOM   12079 C CB   . ALA C 1 229 ? -0.684  -19.178 22.748  1.00 99.25  ? 229 ALA C CB   1 
ATOM   12080 H H    . ALA C 1 229 ? -0.351  -16.580 21.216  1.00 115.93 ? 229 ALA C H    1 
ATOM   12081 H HA   . ALA C 1 229 ? -2.168  -17.751 22.676  1.00 118.86 ? 229 ALA C HA   1 
ATOM   12082 H HB1  . ALA C 1 229 ? -0.896  -19.470 23.648  1.00 119.10 ? 229 ALA C HB1  1 
ATOM   12083 H HB2  . ALA C 1 229 ? -1.111  -19.761 22.101  1.00 119.10 ? 229 ALA C HB2  1 
ATOM   12084 H HB3  . ALA C 1 229 ? 0.277   -19.184 22.615  1.00 119.10 ? 229 ALA C HB3  1 
ATOM   12085 N N    . LYS C 1 230 ? -1.247  -16.740 24.745  1.00 99.59  ? 230 LYS C N    1 
ATOM   12086 C CA   . LYS C 1 230 ? -0.778  -15.938 25.868  1.00 96.11  ? 230 LYS C CA   1 
ATOM   12087 C C    . LYS C 1 230 ? -0.007  -16.847 26.819  1.00 94.76  ? 230 LYS C C    1 
ATOM   12088 O O    . LYS C 1 230 ? -0.569  -17.807 27.357  1.00 96.39  ? 230 LYS C O    1 
ATOM   12089 C CB   . LYS C 1 230 ? -1.950  -15.270 26.585  1.00 96.98  ? 230 LYS C CB   1 
ATOM   12090 C CG   . LYS C 1 230 ? -1.538  -14.332 27.713  1.00 102.97 ? 230 LYS C CG   1 
ATOM   12091 C CD   . LYS C 1 230 ? -2.752  -13.723 28.415  1.00 104.80 ? 230 LYS C CD   1 
ATOM   12092 C CE   . LYS C 1 230 ? -2.939  -14.286 29.823  1.00 102.38 ? 230 LYS C CE   1 
ATOM   12093 N NZ   . LYS C 1 230 ? -4.378  -14.353 30.219  1.00 107.60 ? 230 LYS C NZ   1 
ATOM   12094 H H    . LYS C 1 230 ? -1.982  -17.156 24.907  1.00 119.50 ? 230 LYS C H    1 
ATOM   12095 H HA   . LYS C 1 230 ? -0.182  -15.241 25.553  1.00 115.33 ? 230 LYS C HA   1 
ATOM   12096 H HB2  . LYS C 1 230 ? -2.453  -14.750 25.938  1.00 116.38 ? 230 LYS C HB2  1 
ATOM   12097 H HB3  . LYS C 1 230 ? -2.515  -15.960 26.967  1.00 116.38 ? 230 LYS C HB3  1 
ATOM   12098 H HG2  . LYS C 1 230 ? -1.023  -14.828 28.369  1.00 123.56 ? 230 LYS C HG2  1 
ATOM   12099 H HG3  . LYS C 1 230 ? -1.003  -13.609 27.349  1.00 123.56 ? 230 LYS C HG3  1 
ATOM   12100 H HD2  . LYS C 1 230 ? -2.632  -12.763 28.486  1.00 125.76 ? 230 LYS C HD2  1 
ATOM   12101 H HD3  . LYS C 1 230 ? -3.551  -13.921 27.902  1.00 125.76 ? 230 LYS C HD3  1 
ATOM   12102 H HE2  . LYS C 1 230 ? -2.574  -15.184 29.858  1.00 122.85 ? 230 LYS C HE2  1 
ATOM   12103 H HE3  . LYS C 1 230 ? -2.477  -13.715 30.457  1.00 122.85 ? 230 LYS C HE3  1 
ATOM   12104 H HZ1  . LYS C 1 230 ? -4.453  -14.687 31.040  1.00 129.12 ? 230 LYS C HZ1  1 
ATOM   12105 H HZ2  . LYS C 1 230 ? -4.736  -13.538 30.205  1.00 129.12 ? 230 LYS C HZ2  1 
ATOM   12106 H HZ3  . LYS C 1 230 ? -4.825  -14.874 29.653  1.00 129.12 ? 230 LYS C HZ3  1 
ATOM   12107 N N    . ILE C 1 231 ? 1.273   -16.548 27.022  1.00 92.86  ? 231 ILE C N    1 
ATOM   12108 C CA   . ILE C 1 231 ? 2.174   -17.408 27.781  1.00 93.64  ? 231 ILE C CA   1 
ATOM   12109 C C    . ILE C 1 231 ? 2.416   -16.754 29.135  1.00 93.88  ? 231 ILE C C    1 
ATOM   12110 O O    . ILE C 1 231 ? 3.075   -15.709 29.228  1.00 90.78  ? 231 ILE C O    1 
ATOM   12111 C CB   . ILE C 1 231 ? 3.494   -17.655 27.036  1.00 90.85  ? 231 ILE C CB   1 
ATOM   12112 C CG1  . ILE C 1 231 ? 3.225   -18.210 25.632  1.00 95.84  ? 231 ILE C CG1  1 
ATOM   12113 C CG2  . ILE C 1 231 ? 4.378   -18.599 27.830  1.00 90.02  ? 231 ILE C CG2  1 
ATOM   12114 C CD1  . ILE C 1 231 ? 2.982   -19.714 25.576  1.00 92.89  ? 231 ILE C CD1  1 
ATOM   12115 H H    . ILE C 1 231 ? 1.650   -15.835 26.723  1.00 111.43 ? 231 ILE C H    1 
ATOM   12116 H HA   . ILE C 1 231 ? 1.741   -18.263 27.931  1.00 112.37 ? 231 ILE C HA   1 
ATOM   12117 H HB   . ILE C 1 231 ? 3.957   -16.807 26.942  1.00 109.02 ? 231 ILE C HB   1 
ATOM   12118 H HG12 . ILE C 1 231 ? 2.436   -17.773 25.274  1.00 115.01 ? 231 ILE C HG12 1 
ATOM   12119 H HG13 . ILE C 1 231 ? 3.994   -18.017 25.072  1.00 115.01 ? 231 ILE C HG13 1 
ATOM   12120 H HG21 . ILE C 1 231 ? 5.093   -18.919 27.257  1.00 108.02 ? 231 ILE C HG21 1 
ATOM   12121 H HG22 . ILE C 1 231 ? 4.750   -18.122 28.588  1.00 108.02 ? 231 ILE C HG22 1 
ATOM   12122 H HG23 . ILE C 1 231 ? 3.844   -19.347 28.140  1.00 108.02 ? 231 ILE C HG23 1 
ATOM   12123 H HD11 . ILE C 1 231 ? 2.589   -19.939 24.718  1.00 111.47 ? 231 ILE C HD11 1 
ATOM   12124 H HD12 . ILE C 1 231 ? 3.829   -20.175 25.683  1.00 111.47 ? 231 ILE C HD12 1 
ATOM   12125 H HD13 . ILE C 1 231 ? 2.377   -19.963 26.292  1.00 111.47 ? 231 ILE C HD13 1 
ATOM   12126 N N    . VAL C 1 232 ? 1.887   -17.372 30.192  1.00 91.68  ? 232 VAL C N    1 
ATOM   12127 C CA   . VAL C 1 232 ? 2.123   -16.885 31.545  1.00 92.08  ? 232 VAL C CA   1 
ATOM   12128 C C    . VAL C 1 232 ? 3.539   -17.248 31.974  1.00 93.66  ? 232 VAL C C    1 
ATOM   12129 O O    . VAL C 1 232 ? 4.037   -18.346 31.686  1.00 92.95  ? 232 VAL C O    1 
ATOM   12130 C CB   . VAL C 1 232 ? 1.076   -17.467 32.508  1.00 93.79  ? 232 VAL C CB   1 
ATOM   12131 C CG1  . VAL C 1 232 ? 1.639   -17.566 33.917  1.00 97.16  ? 232 VAL C CG1  1 
ATOM   12132 C CG2  . VAL C 1 232 ? -0.186  -16.612 32.485  1.00 92.19  ? 232 VAL C CG2  1 
ATOM   12133 H H    . VAL C 1 232 ? 1.389   -18.073 30.150  1.00 110.02 ? 232 VAL C H    1 
ATOM   12134 H HA   . VAL C 1 232 ? 2.041   -15.918 31.558  1.00 110.50 ? 232 VAL C HA   1 
ATOM   12135 H HB   . VAL C 1 232 ? 0.842   -18.363 32.221  1.00 112.55 ? 232 VAL C HB   1 
ATOM   12136 H HG11 . VAL C 1 232 ? 0.912   -17.726 34.538  1.00 116.59 ? 232 VAL C HG11 1 
ATOM   12137 H HG12 . VAL C 1 232 ? 2.273   -18.300 33.953  1.00 116.59 ? 232 VAL C HG12 1 
ATOM   12138 H HG13 . VAL C 1 232 ? 2.085   -16.733 34.138  1.00 116.59 ? 232 VAL C HG13 1 
ATOM   12139 H HG21 . VAL C 1 232 ? -0.843  -17.003 33.082  1.00 110.63 ? 232 VAL C HG21 1 
ATOM   12140 H HG22 . VAL C 1 232 ? 0.036   -15.715 32.779  1.00 110.63 ? 232 VAL C HG22 1 
ATOM   12141 H HG23 . VAL C 1 232 ? -0.534  -16.588 31.580  1.00 110.63 ? 232 VAL C HG23 1 
ATOM   12142 N N    . GLN C 1 233 ? 4.189   -16.334 32.682  1.00 90.88  ? 233 GLN C N    1 
ATOM   12143 C CA   . GLN C 1 233 ? 5.595   -16.433 33.045  1.00 91.06  ? 233 GLN C CA   1 
ATOM   12144 C C    . GLN C 1 233 ? 5.768   -16.125 34.521  1.00 91.64  ? 233 GLN C C    1 
ATOM   12145 O O    . GLN C 1 233 ? 4.811   -15.749 35.207  1.00 91.01  ? 233 GLN C O    1 
ATOM   12146 C CB   . GLN C 1 233 ? 6.426   -15.475 32.174  1.00 91.16  ? 233 GLN C CB   1 
ATOM   12147 C CG   . GLN C 1 233 ? 7.018   -16.140 30.924  1.00 90.71  ? 233 GLN C CG   1 
ATOM   12148 C CD   . GLN C 1 233 ? 7.219   -15.179 29.761  1.00 91.17  ? 233 GLN C CD   1 
ATOM   12149 O OE1  . GLN C 1 233 ? 8.326   -14.683 29.532  1.00 88.75  ? 233 GLN C OE1  1 
ATOM   12150 N NE2  . GLN C 1 233 ? 6.152   -14.924 29.013  1.00 91.10  ? 233 GLN C NE2  1 
ATOM   12151 H H    . GLN C 1 233 ? 3.818   -15.616 32.976  1.00 109.05 ? 233 GLN C H    1 
ATOM   12152 H HA   . GLN C 1 233 ? 5.917   -17.336 32.899  1.00 109.28 ? 233 GLN C HA   1 
ATOM   12153 H HB2  . GLN C 1 233 ? 5.858   -14.745 31.882  1.00 109.39 ? 233 GLN C HB2  1 
ATOM   12154 H HB3  . GLN C 1 233 ? 7.162   -15.131 32.704  1.00 109.39 ? 233 GLN C HB3  1 
ATOM   12155 H HG2  . GLN C 1 233 ? 7.883   -16.518 31.149  1.00 108.85 ? 233 GLN C HG2  1 
ATOM   12156 H HG3  . GLN C 1 233 ? 6.417   -16.842 30.628  1.00 108.85 ? 233 GLN C HG3  1 
ATOM   12157 H HE21 . GLN C 1 233 ? 5.399   -15.295 29.197  1.00 109.31 ? 233 GLN C HE21 1 
ATOM   12158 H HE22 . GLN C 1 233 ? 6.215   -14.386 28.344  1.00 109.31 ? 233 GLN C HE22 1 
ATOM   12159 N N    . PRO C 1 234 ? 6.983   -16.302 35.057  1.00 90.72  ? 234 PRO C N    1 
ATOM   12160 C CA   . PRO C 1 234 ? 7.147   -16.210 36.521  1.00 90.93  ? 234 PRO C CA   1 
ATOM   12161 C C    . PRO C 1 234 ? 6.566   -14.952 37.149  1.00 92.79  ? 234 PRO C C    1 
ATOM   12162 O O    . PRO C 1 234 ? 5.896   -15.039 38.185  1.00 93.50  ? 234 PRO C O    1 
ATOM   12163 C CB   . PRO C 1 234 ? 8.673   -16.289 36.699  1.00 91.65  ? 234 PRO C CB   1 
ATOM   12164 C CG   . PRO C 1 234 ? 9.141   -17.094 35.535  1.00 91.26  ? 234 PRO C CG   1 
ATOM   12165 C CD   . PRO C 1 234 ? 8.232   -16.715 34.383  1.00 91.83  ? 234 PRO C CD   1 
ATOM   12166 H HA   . PRO C 1 234 ? 6.726   -16.983 36.929  1.00 109.11 ? 234 PRO C HA   1 
ATOM   12167 H HB2  . PRO C 1 234 ? 9.056   -15.398 36.685  1.00 109.98 ? 234 PRO C HB2  1 
ATOM   12168 H HB3  . PRO C 1 234 ? 8.888   -16.729 37.537  1.00 109.98 ? 234 PRO C HB3  1 
ATOM   12169 H HG2  . PRO C 1 234 ? 10.063  -16.873 35.333  1.00 109.51 ? 234 PRO C HG2  1 
ATOM   12170 H HG3  . PRO C 1 234 ? 9.063   -18.039 35.738  1.00 109.51 ? 234 PRO C HG3  1 
ATOM   12171 H HD2  . PRO C 1 234 ? 8.608   -15.981 33.873  1.00 110.19 ? 234 PRO C HD2  1 
ATOM   12172 H HD3  . PRO C 1 234 ? 8.075   -17.476 33.802  1.00 110.19 ? 234 PRO C HD3  1 
ATOM   12173 N N    . ASN C 1 235 ? 6.801   -13.780 36.557  1.00 92.85  ? 235 ASN C N    1 
ATOM   12174 C CA   . ASN C 1 235 ? 6.285   -12.521 37.084  1.00 91.18  ? 235 ASN C CA   1 
ATOM   12175 C C    . ASN C 1 235 ? 5.860   -11.619 35.923  1.00 88.30  ? 235 ASN C C    1 
ATOM   12176 O O    . ASN C 1 235 ? 6.359   -10.514 35.733  1.00 86.81  ? 235 ASN C O    1 
ATOM   12177 C CB   . ASN C 1 235 ? 7.326   -11.834 37.967  1.00 92.26  ? 235 ASN C CB   1 
ATOM   12178 C CG   . ASN C 1 235 ? 6.705   -11.096 39.140  1.00 92.96  ? 235 ASN C CG   1 
ATOM   12179 O OD1  . ASN C 1 235 ? 5.593   -10.568 39.044  1.00 90.20  ? 235 ASN C OD1  1 
ATOM   12180 N ND2  . ASN C 1 235 ? 7.422   -11.052 40.254  1.00 95.86  ? 235 ASN C ND2  1 
ATOM   12181 H H    . ASN C 1 235 ? 7.265   -13.690 35.838  1.00 111.42 ? 235 ASN C H    1 
ATOM   12182 H HA   . ASN C 1 235 ? 5.500   -12.709 37.622  1.00 109.42 ? 235 ASN C HA   1 
ATOM   12183 H HB2  . ASN C 1 235 ? 7.932   -12.503 38.321  1.00 110.71 ? 235 ASN C HB2  1 
ATOM   12184 H HB3  . ASN C 1 235 ? 7.818   -11.190 37.434  1.00 110.71 ? 235 ASN C HB3  1 
ATOM   12185 H HD21 . ASN C 1 235 ? 7.115   -10.646 40.948  1.00 115.04 ? 235 ASN C HD21 1 
ATOM   12186 H HD22 . ASN C 1 235 ? 8.195   -11.429 40.284  1.00 115.04 ? 235 ASN C HD22 1 
ATOM   12187 N N    . GLY C 1 236 ? 4.913   -12.099 35.137  1.00 91.51  ? 236 GLY C N    1 
ATOM   12188 C CA   . GLY C 1 236 ? 4.422   -11.364 33.987  1.00 89.28  ? 236 GLY C CA   1 
ATOM   12189 C C    . GLY C 1 236 ? 3.886   -12.317 32.941  1.00 88.04  ? 236 GLY C C    1 
ATOM   12190 O O    . GLY C 1 236 ? 4.048   -13.533 33.028  1.00 89.76  ? 236 GLY C O    1 
ATOM   12191 H H    . GLY C 1 236 ? 4.532   -12.861 35.250  1.00 109.81 ? 236 GLY C H    1 
ATOM   12192 H HA2  . GLY C 1 236 ? 3.710   -10.764 34.259  1.00 107.13 ? 236 GLY C HA2  1 
ATOM   12193 H HA3  . GLY C 1 236 ? 5.142   -10.844 33.597  1.00 107.13 ? 236 GLY C HA3  1 
ATOM   12194 N N    . TRP C 1 237 ? 3.233   -11.736 31.932  1.00 89.24  ? 237 TRP C N    1 
ATOM   12195 C CA   . TRP C 1 237 ? 2.698   -12.506 30.818  1.00 86.92  ? 237 TRP C CA   1 
ATOM   12196 C C    . TRP C 1 237 ? 2.937   -11.766 29.511  1.00 86.16  ? 237 TRP C C    1 
ATOM   12197 O O    . TRP C 1 237 ? 2.812   -10.540 29.445  1.00 82.46  ? 237 TRP C O    1 
ATOM   12198 C CB   . TRP C 1 237 ? 1.198   -12.790 30.999  1.00 86.94  ? 237 TRP C CB   1 
ATOM   12199 C CG   . TRP C 1 237 ? 0.312   -11.591 30.840  1.00 86.94  ? 237 TRP C CG   1 
ATOM   12200 C CD1  . TRP C 1 237 ? -0.214  -10.820 31.838  1.00 84.71  ? 237 TRP C CD1  1 
ATOM   12201 C CD2  . TRP C 1 237 ? -0.164  -11.032 29.610  1.00 87.34  ? 237 TRP C CD2  1 
ATOM   12202 N NE1  . TRP C 1 237 ? -0.983  -9.815  31.304  1.00 86.35  ? 237 TRP C NE1  1 
ATOM   12203 C CE2  . TRP C 1 237 ? -0.967  -9.923  29.937  1.00 88.87  ? 237 TRP C CE2  1 
ATOM   12204 C CE3  . TRP C 1 237 ? 0.017   -11.358 28.264  1.00 88.47  ? 237 TRP C CE3  1 
ATOM   12205 C CZ2  . TRP C 1 237 ? -1.590  -9.141  28.968  1.00 87.41  ? 237 TRP C CZ2  1 
ATOM   12206 C CZ3  . TRP C 1 237 ? -0.603  -10.582 27.303  1.00 89.33  ? 237 TRP C CZ3  1 
ATOM   12207 C CH2  . TRP C 1 237 ? -1.396  -9.486  27.659  1.00 88.11  ? 237 TRP C CH2  1 
ATOM   12208 H H    . TRP C 1 237 ? 3.088   -10.891 31.874  1.00 107.09 ? 237 TRP C H    1 
ATOM   12209 H HA   . TRP C 1 237 ? 3.166   -13.355 30.764  1.00 104.30 ? 237 TRP C HA   1 
ATOM   12210 H HB2  . TRP C 1 237 ? 0.926   -13.445 30.337  1.00 104.33 ? 237 TRP C HB2  1 
ATOM   12211 H HB3  . TRP C 1 237 ? 1.057   -13.142 31.892  1.00 104.33 ? 237 TRP C HB3  1 
ATOM   12212 H HD1  . TRP C 1 237 ? -0.071  -10.956 32.747  1.00 101.65 ? 237 TRP C HD1  1 
ATOM   12213 H HE1  . TRP C 1 237 ? -1.405  -9.216  31.754  1.00 103.62 ? 237 TRP C HE1  1 
ATOM   12214 H HE3  . TRP C 1 237 ? 0.545   -12.083 28.019  1.00 106.17 ? 237 TRP C HE3  1 
ATOM   12215 H HZ2  . TRP C 1 237 ? -2.117  -8.412  29.201  1.00 104.89 ? 237 TRP C HZ2  1 
ATOM   12216 H HZ3  . TRP C 1 237 ? -0.491  -10.793 26.404  1.00 107.20 ? 237 TRP C HZ3  1 
ATOM   12217 H HH2  . TRP C 1 237 ? -1.801  -8.982  26.991  1.00 105.73 ? 237 TRP C HH2  1 
ATOM   12218 N N    . LEU C 1 238 ? 3.287   -12.524 28.476  1.00 89.60  ? 238 LEU C N    1 
ATOM   12219 C CA   . LEU C 1 238 ? 3.466   -12.003 27.131  1.00 86.69  ? 238 LEU C CA   1 
ATOM   12220 C C    . LEU C 1 238 ? 2.686   -12.880 26.164  1.00 90.08  ? 238 LEU C C    1 
ATOM   12221 O O    . LEU C 1 238 ? 2.637   -14.104 26.326  1.00 90.63  ? 238 LEU C O    1 
ATOM   12222 C CB   . LEU C 1 238 ? 4.941   -11.974 26.727  1.00 86.08  ? 238 LEU C CB   1 
ATOM   12223 C CG   . LEU C 1 238 ? 5.874   -11.089 27.552  1.00 88.80  ? 238 LEU C CG   1 
ATOM   12224 C CD1  . LEU C 1 238 ? 7.305   -11.239 27.031  1.00 85.70  ? 238 LEU C CD1  1 
ATOM   12225 C CD2  . LEU C 1 238 ? 5.432   -9.632  27.530  1.00 83.64  ? 238 LEU C CD2  1 
ATOM   12226 H H    . LEU C 1 238 ? 3.429   -13.370 28.533  1.00 107.52 ? 238 LEU C H    1 
ATOM   12227 H HA   . LEU C 1 238 ? 3.129   -11.095 27.082  1.00 104.02 ? 238 LEU C HA   1 
ATOM   12228 H HB2  . LEU C 1 238 ? 5.284   -12.880 26.788  1.00 103.30 ? 238 LEU C HB2  1 
ATOM   12229 H HB3  . LEU C 1 238 ? 4.992   -11.661 25.810  1.00 103.30 ? 238 LEU C HB3  1 
ATOM   12230 H HG   . LEU C 1 238 ? 5.845   -11.371 28.479  1.00 106.56 ? 238 LEU C HG   1 
ATOM   12231 H HD11 . LEU C 1 238 ? 7.895   -10.682 27.563  1.00 102.84 ? 238 LEU C HD11 1 
ATOM   12232 H HD12 . LEU C 1 238 ? 7.573   -12.168 27.104  1.00 102.84 ? 238 LEU C HD12 1 
ATOM   12233 H HD13 . LEU C 1 238 ? 7.334   -10.959 26.102  1.00 102.84 ? 238 LEU C HD13 1 
ATOM   12234 H HD21 . LEU C 1 238 ? 6.129   -9.085  27.924  1.00 100.37 ? 238 LEU C HD21 1 
ATOM   12235 H HD22 . LEU C 1 238 ? 5.279   -9.363  26.611  1.00 100.37 ? 238 LEU C HD22 1 
ATOM   12236 H HD23 . LEU C 1 238 ? 4.613   -9.543  28.041  1.00 100.37 ? 238 LEU C HD23 1 
ATOM   12237 N N    . GLU C 1 239 ? 2.078   -12.255 25.160  1.00 90.67  ? 239 GLU C N    1 
ATOM   12238 C CA   . GLU C 1 239 ? 1.369   -12.970 24.110  1.00 90.76  ? 239 GLU C CA   1 
ATOM   12239 C C    . GLU C 1 239 ? 2.186   -12.923 22.827  1.00 90.77  ? 239 GLU C C    1 
ATOM   12240 O O    . GLU C 1 239 ? 2.743   -11.879 22.473  1.00 90.04  ? 239 GLU C O    1 
ATOM   12241 C CB   . GLU C 1 239 ? -0.022  -12.379 23.864  1.00 91.66  ? 239 GLU C CB   1 
ATOM   12242 C CG   . GLU C 1 239 ? -0.897  -13.265 22.984  1.00 96.71  ? 239 GLU C CG   1 
ATOM   12243 C CD   . GLU C 1 239 ? -2.230  -12.632 22.635  1.00 98.39  ? 239 GLU C CD   1 
ATOM   12244 O OE1  . GLU C 1 239 ? -2.287  -11.390 22.515  1.00 96.96  ? 239 GLU C OE1  1 
ATOM   12245 O OE2  . GLU C 1 239 ? -3.218  -13.382 22.475  1.00 99.43  ? 239 GLU C OE2  1 
ATOM   12246 H H    . GLU C 1 239 ? 2.063   -11.400 25.066  1.00 108.81 ? 239 GLU C H    1 
ATOM   12247 H HA   . GLU C 1 239 ? 1.252   -13.897 24.373  1.00 108.91 ? 239 GLU C HA   1 
ATOM   12248 H HB2  . GLU C 1 239 ? -0.472  -12.265 24.716  1.00 109.99 ? 239 GLU C HB2  1 
ATOM   12249 H HB3  . GLU C 1 239 ? 0.074   -11.520 23.422  1.00 109.99 ? 239 GLU C HB3  1 
ATOM   12250 H HG2  . GLU C 1 239 ? -0.427  -13.446 22.154  1.00 116.05 ? 239 GLU C HG2  1 
ATOM   12251 H HG3  . GLU C 1 239 ? -1.075  -14.095 23.452  1.00 116.05 ? 239 GLU C HG3  1 
ATOM   12252 N N    . TYR C 1 240 ? 2.266   -14.056 22.139  1.00 90.80  ? 240 TYR C N    1 
ATOM   12253 C CA   . TYR C 1 240 ? 2.909   -14.133 20.834  1.00 93.35  ? 240 TYR C CA   1 
ATOM   12254 C C    . TYR C 1 240 ? 1.835   -14.216 19.756  1.00 94.13  ? 240 TYR C C    1 
ATOM   12255 O O    . TYR C 1 240 ? 0.832   -14.922 19.911  1.00 94.15  ? 240 TYR C O    1 
ATOM   12256 C CB   . TYR C 1 240 ? 3.884   -15.322 20.755  1.00 92.32  ? 240 TYR C CB   1 
ATOM   12257 C CG   . TYR C 1 240 ? 3.304   -16.686 20.407  1.00 95.42  ? 240 TYR C CG   1 
ATOM   12258 C CD1  . TYR C 1 240 ? 2.734   -16.935 19.162  1.00 97.09  ? 240 TYR C CD1  1 
ATOM   12259 C CD2  . TYR C 1 240 ? 3.372   -17.738 21.311  1.00 93.62  ? 240 TYR C CD2  1 
ATOM   12260 C CE1  . TYR C 1 240 ? 2.217   -18.172 18.845  1.00 96.60  ? 240 TYR C CE1  1 
ATOM   12261 C CE2  . TYR C 1 240 ? 2.855   -18.981 20.999  1.00 94.59  ? 240 TYR C CE2  1 
ATOM   12262 C CZ   . TYR C 1 240 ? 2.285   -19.192 19.762  1.00 97.20  ? 240 TYR C CZ   1 
ATOM   12263 O OH   . TYR C 1 240 ? 1.773   -20.426 19.435  1.00 98.53  ? 240 TYR C OH   1 
ATOM   12264 H H    . TYR C 1 240 ? 1.950   -14.807 22.413  1.00 108.96 ? 240 TYR C H    1 
ATOM   12265 H HA   . TYR C 1 240 ? 3.437   -13.335 20.671  1.00 112.02 ? 240 TYR C HA   1 
ATOM   12266 H HB2  . TYR C 1 240 ? 4.547   -15.118 20.076  1.00 110.79 ? 240 TYR C HB2  1 
ATOM   12267 H HB3  . TYR C 1 240 ? 4.313   -15.412 21.621  1.00 110.79 ? 240 TYR C HB3  1 
ATOM   12268 H HD1  . TYR C 1 240 ? 2.703   -16.253 18.531  1.00 116.51 ? 240 TYR C HD1  1 
ATOM   12269 H HD2  . TYR C 1 240 ? 3.771   -17.604 22.140  1.00 112.34 ? 240 TYR C HD2  1 
ATOM   12270 H HE1  . TYR C 1 240 ? 1.824   -18.315 18.015  1.00 115.92 ? 240 TYR C HE1  1 
ATOM   12271 H HE2  . TYR C 1 240 ? 2.892   -19.672 21.620  1.00 113.51 ? 240 TYR C HE2  1 
ATOM   12272 H HH   . TYR C 1 240 ? 1.889   -20.963 20.071  1.00 118.24 ? 240 TYR C HH   1 
ATOM   12273 N N    . ILE C 1 241 ? 2.046   -13.483 18.666  1.00 94.46  ? 241 ILE C N    1 
ATOM   12274 C CA   . ILE C 1 241 ? 1.095   -13.426 17.561  1.00 97.04  ? 241 ILE C CA   1 
ATOM   12275 C C    . ILE C 1 241 ? 1.883   -13.554 16.264  1.00 96.30  ? 241 ILE C C    1 
ATOM   12276 O O    . ILE C 1 241 ? 2.652   -12.652 15.913  1.00 95.46  ? 241 ILE C O    1 
ATOM   12277 C CB   . ILE C 1 241 ? 0.265   -12.130 17.564  1.00 94.70  ? 241 ILE C CB   1 
ATOM   12278 C CG1  . ILE C 1 241 ? -0.251  -11.845 18.977  1.00 96.29  ? 241 ILE C CG1  1 
ATOM   12279 C CG2  . ILE C 1 241 ? -0.881  -12.240 16.568  1.00 99.40  ? 241 ILE C CG2  1 
ATOM   12280 C CD1  . ILE C 1 241 ? -1.180  -10.646 19.077  1.00 97.69  ? 241 ILE C CD1  1 
ATOM   12281 H H    . ILE C 1 241 ? 2.748   -13.001 18.541  1.00 113.35 ? 241 ILE C H    1 
ATOM   12282 H HA   . ILE C 1 241 ? 0.489   -14.181 17.622  1.00 116.44 ? 241 ILE C HA   1 
ATOM   12283 H HB   . ILE C 1 241 ? 0.830   -11.390 17.293  1.00 113.64 ? 241 ILE C HB   1 
ATOM   12284 H HG12 . ILE C 1 241 ? -0.740  -12.622 19.290  1.00 115.55 ? 241 ILE C HG12 1 
ATOM   12285 H HG13 . ILE C 1 241 ? 0.509   -11.676 19.555  1.00 115.55 ? 241 ILE C HG13 1 
ATOM   12286 H HG21 . ILE C 1 241 ? -1.381  -11.408 16.569  1.00 119.28 ? 241 ILE C HG21 1 
ATOM   12287 H HG22 . ILE C 1 241 ? -0.517  -12.406 15.684  1.00 119.28 ? 241 ILE C HG22 1 
ATOM   12288 H HG23 . ILE C 1 241 ? -1.459  -12.973 16.830  1.00 119.28 ? 241 ILE C HG23 1 
ATOM   12289 H HD11 . ILE C 1 241 ? -1.440  -10.525 20.004  1.00 117.23 ? 241 ILE C HD11 1 
ATOM   12290 H HD12 . ILE C 1 241 ? -0.714  -9.858  18.758  1.00 117.23 ? 241 ILE C HD12 1 
ATOM   12291 H HD13 . ILE C 1 241 ? -1.966  -10.809 18.532  1.00 117.23 ? 241 ILE C HD13 1 
ATOM   12292 N N    . ILE C 1 242 ? 1.696   -14.666 15.557  1.00 97.60  ? 242 ILE C N    1 
ATOM   12293 C CA   . ILE C 1 242 ? 2.323   -14.880 14.255  1.00 102.34 ? 242 ILE C CA   1 
ATOM   12294 C C    . ILE C 1 242 ? 1.336   -14.441 13.179  1.00 107.93 ? 242 ILE C C    1 
ATOM   12295 O O    . ILE C 1 242 ? 0.211   -14.946 13.111  1.00 107.74 ? 242 ILE C O    1 
ATOM   12296 C CB   . ILE C 1 242 ? 2.746   -16.344 14.059  1.00 100.39 ? 242 ILE C CB   1 
ATOM   12297 C CG1  . ILE C 1 242 ? 4.105   -16.571 14.731  1.00 93.50  ? 242 ILE C CG1  1 
ATOM   12298 C CG2  . ILE C 1 242 ? 2.761   -16.693 12.576  1.00 101.19 ? 242 ILE C CG2  1 
ATOM   12299 C CD1  . ILE C 1 242 ? 4.792   -17.866 14.354  1.00 97.11  ? 242 ILE C CD1  1 
ATOM   12300 H H    . ILE C 1 242 ? 1.203   -15.322 15.815  1.00 117.12 ? 242 ILE C H    1 
ATOM   12301 H HA   . ILE C 1 242 ? 3.120   -14.332 14.191  1.00 122.81 ? 242 ILE C HA   1 
ATOM   12302 H HB   . ILE C 1 242 ? 2.103   -16.937 14.481  1.00 120.47 ? 242 ILE C HB   1 
ATOM   12303 H HG12 . ILE C 1 242 ? 4.697   -15.844 14.481  1.00 112.20 ? 242 ILE C HG12 1 
ATOM   12304 H HG13 . ILE C 1 242 ? 3.976   -16.578 15.692  1.00 112.20 ? 242 ILE C HG13 1 
ATOM   12305 H HG21 . ILE C 1 242 ? 3.183   -17.558 12.459  1.00 121.42 ? 242 ILE C HG21 1 
ATOM   12306 H HG22 . ILE C 1 242 ? 1.848   -16.723 12.249  1.00 121.42 ? 242 ILE C HG22 1 
ATOM   12307 H HG23 . ILE C 1 242 ? 3.261   -16.013 12.097  1.00 121.42 ? 242 ILE C HG23 1 
ATOM   12308 H HD11 . ILE C 1 242 ? 5.497   -18.047 14.995  1.00 116.53 ? 242 ILE C HD11 1 
ATOM   12309 H HD12 . ILE C 1 242 ? 4.140   -18.584 14.367  1.00 116.53 ? 242 ILE C HD12 1 
ATOM   12310 H HD13 . ILE C 1 242 ? 5.169   -17.776 13.465  1.00 116.53 ? 242 ILE C HD13 1 
ATOM   12311 N N    . GLU C 1 243 ? 1.767   -13.518 12.324  1.00 111.33 ? 243 GLU C N    1 
ATOM   12312 C CA   . GLU C 1 243 ? 0.892   -12.906 11.334  1.00 119.90 ? 243 GLU C CA   1 
ATOM   12313 C C    . GLU C 1 243 ? 1.674   -12.662 10.054  1.00 122.12 ? 243 GLU C C    1 
ATOM   12314 O O    . GLU C 1 243 ? 2.730   -12.023 10.084  1.00 125.86 ? 243 GLU C O    1 
ATOM   12315 C CB   . GLU C 1 243 ? 0.320   -11.587 11.861  1.00 124.96 ? 243 GLU C CB   1 
ATOM   12316 C CG   . GLU C 1 243 ? -1.173  -11.422 11.670  1.00 132.20 ? 243 GLU C CG   1 
ATOM   12317 C CD   . GLU C 1 243 ? -1.673  -10.090 12.200  1.00 139.61 ? 243 GLU C CD   1 
ATOM   12318 O OE1  . GLU C 1 243 ? -1.349  -9.048  11.589  1.00 136.21 ? 243 GLU C OE1  1 
ATOM   12319 O OE2  . GLU C 1 243 ? -2.385  -10.085 13.228  1.00 137.24 ? 243 GLU C OE2  1 
ATOM   12320 H H    . GLU C 1 243 ? 2.575   -13.226 12.299  1.00 133.60 ? 243 GLU C H    1 
ATOM   12321 H HA   . GLU C 1 243 ? 0.159   -13.506 11.127  1.00 143.88 ? 243 GLU C HA   1 
ATOM   12322 H HB2  . GLU C 1 243 ? 0.500   -11.531 12.813  1.00 149.96 ? 243 GLU C HB2  1 
ATOM   12323 H HB3  . GLU C 1 243 ? 0.756   -10.854 11.398  1.00 149.96 ? 243 GLU C HB3  1 
ATOM   12324 H HG2  . GLU C 1 243 ? -1.381  -11.469 10.724  1.00 158.64 ? 243 GLU C HG2  1 
ATOM   12325 H HG3  . GLU C 1 243 ? -1.635  -12.130 12.146  1.00 158.64 ? 243 GLU C HG3  1 
ATOM   12326 N N    . ASN C 1 244 ? 1.154   -13.169 8.937   1.00 123.06 ? 244 ASN C N    1 
ATOM   12327 C CA   . ASN C 1 244 ? 1.798   -12.998 7.635   1.00 124.76 ? 244 ASN C CA   1 
ATOM   12328 C C    . ASN C 1 244 ? 3.257   -13.443 7.678   1.00 121.53 ? 244 ASN C C    1 
ATOM   12329 O O    . ASN C 1 244 ? 4.117   -12.874 7.002   1.00 119.04 ? 244 ASN C O    1 
ATOM   12330 C CB   . ASN C 1 244 ? 1.700   -11.545 7.160   1.00 127.62 ? 244 ASN C CB   1 
ATOM   12331 C CG   . ASN C 1 244 ? 0.406   -10.876 7.587   1.00 131.29 ? 244 ASN C CG   1 
ATOM   12332 O OD1  . ASN C 1 244 ? -0.663  -11.487 7.554   1.00 134.31 ? 244 ASN C OD1  1 
ATOM   12333 N ND2  . ASN C 1 244 ? 0.496   -9.612  7.988   1.00 129.05 ? 244 ASN C ND2  1 
ATOM   12334 H H    . ASN C 1 244 ? 0.423   -13.621 8.906   1.00 147.67 ? 244 ASN C H    1 
ATOM   12335 H HA   . ASN C 1 244 ? 1.337   -13.559 6.992   1.00 149.71 ? 244 ASN C HA   1 
ATOM   12336 H HB2  . ASN C 1 244 ? 2.438   -11.039 7.534   1.00 153.14 ? 244 ASN C HB2  1 
ATOM   12337 H HB3  . ASN C 1 244 ? 1.742   -11.526 6.191   1.00 153.14 ? 244 ASN C HB3  1 
ATOM   12338 H HD21 . ASN C 1 244 ? 1.260   -9.216  7.995   1.00 154.86 ? 244 ASN C HD21 1 
ATOM   12339 H HD22 . ASN C 1 244 ? -0.209  -9.189  8.240   1.00 154.86 ? 244 ASN C HD22 1 
ATOM   12340 N N    . ASP C 1 245 ? 3.545   -14.465 8.483   1.00 118.46 ? 245 ASP C N    1 
ATOM   12341 C CA   . ASP C 1 245 ? 4.912   -14.945 8.673   1.00 118.56 ? 245 ASP C CA   1 
ATOM   12342 C C    . ASP C 1 245 ? 5.785   -13.868 9.319   1.00 115.82 ? 245 ASP C C    1 
ATOM   12343 O O    . ASP C 1 245 ? 6.956   -13.696 8.973   1.00 115.05 ? 245 ASP C O    1 
ATOM   12344 C CB   . ASP C 1 245 ? 5.515   -15.416 7.349   1.00 121.11 ? 245 ASP C CB   1 
ATOM   12345 C CG   . ASP C 1 245 ? 6.327   -16.688 7.497   1.00 125.92 ? 245 ASP C CG   1 
ATOM   12346 O OD1  . ASP C 1 245 ? 5.836   -17.639 8.146   1.00 128.23 ? 245 ASP C OD1  1 
ATOM   12347 O OD2  . ASP C 1 245 ? 7.456   -16.738 6.966   1.00 126.86 ? 245 ASP C OD2  1 
ATOM   12348 H H    . ASP C 1 245 ? 2.958   -14.901 8.936   1.00 142.15 ? 245 ASP C H    1 
ATOM   12349 H HA   . ASP C 1 245 ? 4.893   -15.704 9.277   1.00 142.27 ? 245 ASP C HA   1 
ATOM   12350 H HB2  . ASP C 1 245 ? 4.798   -15.588 6.718   1.00 145.34 ? 245 ASP C HB2  1 
ATOM   12351 H HB3  . ASP C 1 245 ? 6.101   -14.724 7.004   1.00 145.34 ? 245 ASP C HB3  1 
ATOM   12352 N N    . GLU C 1 246 ? 5.208   -13.131 10.266  1.00 113.06 ? 246 GLU C N    1 
ATOM   12353 C CA   . GLU C 1 246 ? 5.927   -12.118 11.027  1.00 108.70 ? 246 GLU C CA   1 
ATOM   12354 C C    . GLU C 1 246 ? 5.541   -12.247 12.494  1.00 102.24 ? 246 GLU C C    1 
ATOM   12355 O O    . GLU C 1 246 ? 4.361   -12.398 12.825  1.00 101.43 ? 246 GLU C O    1 
ATOM   12356 C CB   . GLU C 1 246 ? 5.624   -10.707 10.509  1.00 105.04 ? 246 GLU C CB   1 
ATOM   12357 C CG   . GLU C 1 246 ? 5.804   -10.557 9.000   1.00 111.43 ? 246 GLU C CG   1 
ATOM   12358 C CD   . GLU C 1 246 ? 6.572   -9.307  8.617   1.00 106.70 ? 246 GLU C CD   1 
ATOM   12359 O OE1  . GLU C 1 246 ? 7.719   -9.143  9.084   1.00 103.87 ? 246 GLU C OE1  1 
ATOM   12360 O OE2  . GLU C 1 246 ? 6.029   -8.483  7.851   1.00 108.52 ? 246 GLU C OE2  1 
ATOM   12361 H H    . GLU C 1 246 ? 4.381   -13.203 10.489  1.00 135.67 ? 246 GLU C H    1 
ATOM   12362 H HA   . GLU C 1 246 ? 6.884   -12.256 10.951  1.00 130.44 ? 246 GLU C HA   1 
ATOM   12363 H HB2  . GLU C 1 246 ? 4.703   -10.488 10.721  1.00 126.05 ? 246 GLU C HB2  1 
ATOM   12364 H HB3  . GLU C 1 246 ? 6.223   -10.080 10.943  1.00 126.05 ? 246 GLU C HB3  1 
ATOM   12365 H HG2  . GLU C 1 246 ? 6.293   -11.324 8.663   1.00 133.72 ? 246 GLU C HG2  1 
ATOM   12366 H HG3  . GLU C 1 246 ? 4.930   -10.512 8.581   1.00 133.72 ? 246 GLU C HG3  1 
ATOM   12367 N N    . MET C 1 247 ? 6.541   -12.187 13.368  1.00 93.72  ? 247 MET C N    1 
ATOM   12368 C CA   . MET C 1 247 ? 6.361   -12.454 14.789  1.00 95.18  ? 247 MET C CA   1 
ATOM   12369 C C    . MET C 1 247 ? 6.148   -11.152 15.551  1.00 90.61  ? 247 MET C C    1 
ATOM   12370 O O    . MET C 1 247 ? 6.950   -10.219 15.435  1.00 89.44  ? 247 MET C O    1 
ATOM   12371 C CB   . MET C 1 247 ? 7.573   -13.205 15.353  1.00 90.73  ? 247 MET C CB   1 
ATOM   12372 C CG   . MET C 1 247 ? 7.484   -13.548 16.826  1.00 86.43  ? 247 MET C CG   1 
ATOM   12373 S SD   . MET C 1 247 ? 6.571   -15.067 17.185  1.00 91.04  ? 247 MET C SD   1 
ATOM   12374 C CE   . MET C 1 247 ? 4.981   -14.376 17.633  1.00 90.17  ? 247 MET C CE   1 
ATOM   12375 H H    . MET C 1 247 ? 7.351   -11.990 13.155  1.00 112.47 ? 247 MET C H    1 
ATOM   12376 H HA   . MET C 1 247 ? 5.574   -13.009 14.906  1.00 114.21 ? 247 MET C HA   1 
ATOM   12377 H HB2  . MET C 1 247 ? 7.672   -14.038 14.865  1.00 108.88 ? 247 MET C HB2  1 
ATOM   12378 H HB3  . MET C 1 247 ? 8.361   -12.653 15.229  1.00 108.88 ? 247 MET C HB3  1 
ATOM   12379 H HG2  . MET C 1 247 ? 8.383   -13.657 17.173  1.00 103.72 ? 247 MET C HG2  1 
ATOM   12380 H HG3  . MET C 1 247 ? 7.036   -12.821 17.286  1.00 103.72 ? 247 MET C HG3  1 
ATOM   12381 H HE1  . MET C 1 247 ? 4.360   -15.101 17.810  1.00 108.20 ? 247 MET C HE1  1 
ATOM   12382 H HE2  . MET C 1 247 ? 5.086   -13.830 18.428  1.00 108.20 ? 247 MET C HE2  1 
ATOM   12383 H HE3  . MET C 1 247 ? 4.654   -13.833 16.899  1.00 108.20 ? 247 MET C HE3  1 
ATOM   12384 N N    . TYR C 1 248 ? 5.072   -11.103 16.334  1.00 89.82  ? 248 TYR C N    1 
ATOM   12385 C CA   . TYR C 1 248 ? 4.772   -9.976  17.202  1.00 87.25  ? 248 TYR C CA   1 
ATOM   12386 C C    . TYR C 1 248 ? 4.746   -10.447 18.651  1.00 90.86  ? 248 TYR C C    1 
ATOM   12387 O O    . TYR C 1 248 ? 4.456   -11.615 18.941  1.00 90.99  ? 248 TYR C O    1 
ATOM   12388 C CB   . TYR C 1 248 ? 3.424   -9.338  16.849  1.00 89.11  ? 248 TYR C CB   1 
ATOM   12389 C CG   . TYR C 1 248 ? 3.381   -8.722  15.470  1.00 92.90  ? 248 TYR C CG   1 
ATOM   12390 C CD1  . TYR C 1 248 ? 3.034   -9.483  14.360  1.00 94.02  ? 248 TYR C CD1  1 
ATOM   12391 C CD2  . TYR C 1 248 ? 3.690   -7.381  15.276  1.00 89.21  ? 248 TYR C CD2  1 
ATOM   12392 C CE1  . TYR C 1 248 ? 2.994   -8.928  13.098  1.00 95.69  ? 248 TYR C CE1  1 
ATOM   12393 C CE2  . TYR C 1 248 ? 3.655   -6.818  14.011  1.00 93.16  ? 248 TYR C CE2  1 
ATOM   12394 C CZ   . TYR C 1 248 ? 3.306   -7.597  12.929  1.00 92.59  ? 248 TYR C CZ   1 
ATOM   12395 O OH   . TYR C 1 248 ? 3.265   -7.047  11.667  1.00 99.98  ? 248 TYR C OH   1 
ATOM   12396 H H    . TYR C 1 248 ? 4.487   -11.731 16.379  1.00 107.78 ? 248 TYR C H    1 
ATOM   12397 H HA   . TYR C 1 248 ? 5.460   -9.300  17.105  1.00 104.70 ? 248 TYR C HA   1 
ATOM   12398 H HB2  . TYR C 1 248 ? 2.736   -10.020 16.889  1.00 106.92 ? 248 TYR C HB2  1 
ATOM   12399 H HB3  . TYR C 1 248 ? 3.234   -8.637  17.491  1.00 106.92 ? 248 TYR C HB3  1 
ATOM   12400 H HD1  . TYR C 1 248 ? 2.824   -10.382 14.470  1.00 112.83 ? 248 TYR C HD1  1 
ATOM   12401 H HD2  . TYR C 1 248 ? 3.924   -6.854  16.006  1.00 107.05 ? 248 TYR C HD2  1 
ATOM   12402 H HE1  . TYR C 1 248 ? 2.758   -9.450  12.365  1.00 114.82 ? 248 TYR C HE1  1 
ATOM   12403 H HE2  . TYR C 1 248 ? 3.865   -5.920  13.893  1.00 111.79 ? 248 TYR C HE2  1 
ATOM   12404 H HH   . TYR C 1 248 ? 3.027   -7.627  11.108  1.00 119.98 ? 248 TYR C HH   1 
ATOM   12405 N N    . ILE C 1 249 ? 5.053   -9.531  19.565  1.00 89.41  ? 249 ILE C N    1 
ATOM   12406 C CA   . ILE C 1 249 ? 4.966   -9.794  20.995  1.00 85.25  ? 249 ILE C CA   1 
ATOM   12407 C C    . ILE C 1 249 ? 4.093   -8.711  21.607  1.00 84.61  ? 249 ILE C C    1 
ATOM   12408 O O    . ILE C 1 249 ? 4.400   -7.518  21.486  1.00 83.08  ? 249 ILE C O    1 
ATOM   12409 C CB   . ILE C 1 249 ? 6.346   -9.832  21.671  1.00 86.94  ? 249 ILE C CB   1 
ATOM   12410 C CG1  . ILE C 1 249 ? 7.158   -11.021 21.136  1.00 89.10  ? 249 ILE C CG1  1 
ATOM   12411 C CG2  . ILE C 1 249 ? 6.205   -9.909  23.193  1.00 86.67  ? 249 ILE C CG2  1 
ATOM   12412 C CD1  . ILE C 1 249 ? 6.608   -12.394 21.513  1.00 86.26  ? 249 ILE C CD1  1 
ATOM   12413 H H    . ILE C 1 249 ? 5.320   -8.736  19.375  1.00 107.30 ? 249 ILE C H    1 
ATOM   12414 H HA   . ILE C 1 249 ? 4.541   -10.654 21.140  1.00 102.30 ? 249 ILE C HA   1 
ATOM   12415 H HB   . ILE C 1 249 ? 6.818   -9.012  21.457  1.00 104.33 ? 249 ILE C HB   1 
ATOM   12416 H HG12 . ILE C 1 249 ? 7.176   -10.970 20.168  1.00 106.92 ? 249 ILE C HG12 1 
ATOM   12417 H HG13 . ILE C 1 249 ? 8.060   -10.961 21.488  1.00 106.92 ? 249 ILE C HG13 1 
ATOM   12418 H HG21 . ILE C 1 249 ? 7.088   -9.970  23.590  1.00 104.01 ? 249 ILE C HG21 1 
ATOM   12419 H HG22 . ILE C 1 249 ? 5.754   -9.110  23.509  1.00 104.01 ? 249 ILE C HG22 1 
ATOM   12420 H HG23 . ILE C 1 249 ? 5.684   -10.695 23.422  1.00 104.01 ? 249 ILE C HG23 1 
ATOM   12421 H HD11 . ILE C 1 249 ? 7.176   -13.079 21.127  1.00 103.52 ? 249 ILE C HD11 1 
ATOM   12422 H HD12 . ILE C 1 249 ? 6.600   -12.477 22.479  1.00 103.52 ? 249 ILE C HD12 1 
ATOM   12423 H HD13 . ILE C 1 249 ? 5.706   -12.479 21.166  1.00 103.52 ? 249 ILE C HD13 1 
ATOM   12424 N N    . ASP C 1 250 ? 3.004   -9.124  22.247  1.00 84.09  ? 250 ASP C N    1 
ATOM   12425 C CA   . ASP C 1 250 ? 2.129   -8.241  22.998  1.00 85.29  ? 250 ASP C CA   1 
ATOM   12426 C C    . ASP C 1 250 ? 2.323   -8.490  24.488  1.00 87.32  ? 250 ASP C C    1 
ATOM   12427 O O    . ASP C 1 250 ? 2.704   -9.587  24.909  1.00 88.71  ? 250 ASP C O    1 
ATOM   12428 C CB   . ASP C 1 250 ? 0.663   -8.465  22.622  1.00 85.67  ? 250 ASP C CB   1 
ATOM   12429 C CG   . ASP C 1 250 ? -0.183  -7.218  22.802  1.00 86.87  ? 250 ASP C CG   1 
ATOM   12430 O OD1  . ASP C 1 250 ? 0.342   -6.195  23.293  1.00 84.40  ? 250 ASP C OD1  1 
ATOM   12431 O OD2  . ASP C 1 250 ? -1.378  -7.256  22.447  1.00 92.63  ? 250 ASP C OD2  1 
ATOM   12432 H H    . ASP C 1 250 ? 2.745   -9.944  22.259  1.00 100.90 ? 250 ASP C H    1 
ATOM   12433 H HA   . ASP C 1 250 ? 2.347   -7.316  22.803  1.00 102.35 ? 250 ASP C HA   1 
ATOM   12434 H HB2  . ASP C 1 250 ? 0.612   -8.731  21.690  1.00 102.80 ? 250 ASP C HB2  1 
ATOM   12435 H HB3  . ASP C 1 250 ? 0.294   -9.163  23.186  1.00 102.80 ? 250 ASP C HB3  1 
ATOM   12436 N N    . GLY C 1 251 ? 2.053   -7.464  25.286  1.00 82.69  ? 251 GLY C N    1 
ATOM   12437 C CA   . GLY C 1 251 ? 2.198   -7.573  26.715  1.00 85.15  ? 251 GLY C CA   1 
ATOM   12438 C C    . GLY C 1 251 ? 1.949   -6.266  27.429  1.00 82.42  ? 251 GLY C C    1 
ATOM   12439 O O    . GLY C 1 251 ? 1.798   -5.209  26.809  1.00 82.12  ? 251 GLY C O    1 
ATOM   12440 H H    . GLY C 1 251 ? 1.785   -6.693  25.015  1.00 99.23  ? 251 GLY C H    1 
ATOM   12441 H HA2  . GLY C 1 251 ? 1.566   -8.228  27.051  1.00 102.18 ? 251 GLY C HA2  1 
ATOM   12442 H HA3  . GLY C 1 251 ? 3.098   -7.867  26.924  1.00 102.18 ? 251 GLY C HA3  1 
ATOM   12443 N N    . PRO C 1 252 ? 1.916   -6.313  28.759  1.00 84.31  ? 252 PRO C N    1 
ATOM   12444 C CA   . PRO C 1 252 ? 1.636   -5.107  29.538  1.00 81.31  ? 252 PRO C CA   1 
ATOM   12445 C C    . PRO C 1 252 ? 2.900   -4.385  29.967  1.00 78.99  ? 252 PRO C C    1 
ATOM   12446 O O    . PRO C 1 252 ? 3.956   -4.981  30.192  1.00 78.00  ? 252 PRO C O    1 
ATOM   12447 C CB   . PRO C 1 252 ? 0.876   -5.658  30.753  1.00 75.99  ? 252 PRO C CB   1 
ATOM   12448 C CG   . PRO C 1 252 ? 1.297   -7.123  30.856  1.00 77.40  ? 252 PRO C CG   1 
ATOM   12449 C CD   . PRO C 1 252 ? 2.107   -7.486  29.630  1.00 85.35  ? 252 PRO C CD   1 
ATOM   12450 H HA   . PRO C 1 252 ? 1.067   -4.496  29.045  1.00 97.57  ? 252 PRO C HA   1 
ATOM   12451 H HB2  . PRO C 1 252 ? 1.130   -5.168  31.550  1.00 91.18  ? 252 PRO C HB2  1 
ATOM   12452 H HB3  . PRO C 1 252 ? -0.080  -5.582  30.607  1.00 91.18  ? 252 PRO C HB3  1 
ATOM   12453 H HG2  . PRO C 1 252 ? 1.834   -7.241  31.656  1.00 92.88  ? 252 PRO C HG2  1 
ATOM   12454 H HG3  . PRO C 1 252 ? 0.502   -7.677  30.906  1.00 92.88  ? 252 PRO C HG3  1 
ATOM   12455 H HD2  . PRO C 1 252 ? 3.043   -7.605  29.854  1.00 102.42 ? 252 PRO C HD2  1 
ATOM   12456 H HD3  . PRO C 1 252 ? 1.761   -8.290  29.211  1.00 102.42 ? 252 PRO C HD3  1 
ATOM   12457 N N    . VAL C 1 253 ? 2.767   -3.067  30.084  1.00 79.13  ? 253 VAL C N    1 
ATOM   12458 C CA   . VAL C 1 253 ? 3.853   -2.190  30.499  1.00 79.48  ? 253 VAL C CA   1 
ATOM   12459 C C    . VAL C 1 253 ? 3.266   -1.147  31.439  1.00 79.62  ? 253 VAL C C    1 
ATOM   12460 O O    . VAL C 1 253 ? 2.355   -0.407  31.050  1.00 80.29  ? 253 VAL C O    1 
ATOM   12461 C CB   . VAL C 1 253 ? 4.535   -1.503  29.303  1.00 78.48  ? 253 VAL C CB   1 
ATOM   12462 C CG1  . VAL C 1 253 ? 5.877   -0.918  29.719  1.00 74.78  ? 253 VAL C CG1  1 
ATOM   12463 C CG2  . VAL C 1 253 ? 4.705   -2.478  28.147  1.00 78.16  ? 253 VAL C CG2  1 
ATOM   12464 H H    . VAL C 1 253 ? 2.034   -2.647  29.923  1.00 94.95  ? 253 VAL C H    1 
ATOM   12465 H HA   . VAL C 1 253 ? 4.522   -2.703  30.979  1.00 95.37  ? 253 VAL C HA   1 
ATOM   12466 H HB   . VAL C 1 253 ? 3.970   -0.776  28.998  1.00 94.18  ? 253 VAL C HB   1 
ATOM   12467 H HG11 . VAL C 1 253 ? 5.992   -0.055  29.289  1.00 89.74  ? 253 VAL C HG11 1 
ATOM   12468 H HG12 . VAL C 1 253 ? 5.891   -0.811  30.683  1.00 89.74  ? 253 VAL C HG12 1 
ATOM   12469 H HG13 . VAL C 1 253 ? 6.584   -1.521  29.442  1.00 89.74  ? 253 VAL C HG13 1 
ATOM   12470 H HG21 . VAL C 1 253 ? 5.267   -2.070  27.469  1.00 93.79  ? 253 VAL C HG21 1 
ATOM   12471 H HG22 . VAL C 1 253 ? 5.122   -3.290  28.476  1.00 93.79  ? 253 VAL C HG22 1 
ATOM   12472 H HG23 . VAL C 1 253 ? 3.833   -2.682  27.774  1.00 93.79  ? 253 VAL C HG23 1 
ATOM   12473 N N    . GLU C 1 254 ? 3.774   -1.086  32.667  1.00 77.06  ? 254 GLU C N    1 
ATOM   12474 C CA   . GLU C 1 254 ? 3.363   -0.083  33.636  1.00 77.54  ? 254 GLU C CA   1 
ATOM   12475 C C    . GLU C 1 254 ? 4.508   0.888   33.895  1.00 76.06  ? 254 GLU C C    1 
ATOM   12476 O O    . GLU C 1 254 ? 5.663   0.479   34.046  1.00 74.46  ? 254 GLU C O    1 
ATOM   12477 C CB   . GLU C 1 254 ? 2.935   -0.728  34.959  1.00 80.68  ? 254 GLU C CB   1 
ATOM   12478 C CG   . GLU C 1 254 ? 2.421   0.273   35.977  1.00 83.11  ? 254 GLU C CG   1 
ATOM   12479 C CD   . GLU C 1 254 ? 1.815   -0.389  37.196  1.00 87.02  ? 254 GLU C CD   1 
ATOM   12480 O OE1  . GLU C 1 254 ? 1.938   -1.628  37.310  1.00 90.22  ? 254 GLU C OE1  1 
ATOM   12481 O OE2  . GLU C 1 254 ? 1.220   0.326   38.033  1.00 86.21  ? 254 GLU C OE2  1 
ATOM   12482 H H    . GLU C 1 254 ? 4.370   -1.629  32.966  1.00 92.47  ? 254 GLU C H    1 
ATOM   12483 H HA   . GLU C 1 254 ? 2.609   0.412   33.279  1.00 93.05  ? 254 GLU C HA   1 
ATOM   12484 H HB2  . GLU C 1 254 ? 2.225   -1.364  34.782  1.00 96.81  ? 254 GLU C HB2  1 
ATOM   12485 H HB3  . GLU C 1 254 ? 3.699   -1.183  35.348  1.00 96.81  ? 254 GLU C HB3  1 
ATOM   12486 H HG2  . GLU C 1 254 ? 3.158   0.829   36.274  1.00 99.73  ? 254 GLU C HG2  1 
ATOM   12487 H HG3  . GLU C 1 254 ? 1.737   0.822   35.563  1.00 99.73  ? 254 GLU C HG3  1 
ATOM   12488 N N    . ILE C 1 255 ? 4.186   2.178   33.924  1.00 75.76  ? 255 ILE C N    1 
ATOM   12489 C CA   . ILE C 1 255 ? 5.151   3.203   34.316  1.00 76.36  ? 255 ILE C CA   1 
ATOM   12490 C C    . ILE C 1 255 ? 5.154   3.284   35.838  1.00 76.50  ? 255 ILE C C    1 
ATOM   12491 O O    . ILE C 1 255 ? 4.127   3.579   36.459  1.00 75.61  ? 255 ILE C O    1 
ATOM   12492 C CB   . ILE C 1 255 ? 4.815   4.563   33.691  1.00 78.71  ? 255 ILE C CB   1 
ATOM   12493 C CG1  . ILE C 1 255 ? 4.473   4.413   32.206  1.00 79.07  ? 255 ILE C CG1  1 
ATOM   12494 C CG2  . ILE C 1 255 ? 5.985   5.532   33.867  1.00 75.92  ? 255 ILE C CG2  1 
ATOM   12495 C CD1  . ILE C 1 255 ? 5.573   3.788   31.373  1.00 76.47  ? 255 ILE C CD1  1 
ATOM   12496 H H    . ILE C 1 255 ? 3.411   2.489   33.720  1.00 90.91  ? 255 ILE C H    1 
ATOM   12497 H HA   . ILE C 1 255 ? 6.035   2.947   34.010  1.00 91.63  ? 255 ILE C HA   1 
ATOM   12498 H HB   . ILE C 1 255 ? 4.038   4.919   34.148  1.00 94.45  ? 255 ILE C HB   1 
ATOM   12499 H HG12 . ILE C 1 255 ? 3.688   3.849   32.124  1.00 94.88  ? 255 ILE C HG12 1 
ATOM   12500 H HG13 . ILE C 1 255 ? 4.290   5.292   31.839  1.00 94.88  ? 255 ILE C HG13 1 
ATOM   12501 H HG21 . ILE C 1 255 ? 5.802   6.343   33.367  1.00 91.11  ? 255 ILE C HG21 1 
ATOM   12502 H HG22 . ILE C 1 255 ? 6.084   5.739   34.809  1.00 91.11  ? 255 ILE C HG22 1 
ATOM   12503 H HG23 . ILE C 1 255 ? 6.794   5.114   33.533  1.00 91.11  ? 255 ILE C HG23 1 
ATOM   12504 H HD11 . ILE C 1 255 ? 5.284   3.746   30.448  1.00 91.77  ? 255 ILE C HD11 1 
ATOM   12505 H HD12 . ILE C 1 255 ? 6.372   4.334   31.444  1.00 91.77  ? 255 ILE C HD12 1 
ATOM   12506 H HD13 . ILE C 1 255 ? 5.753   2.895   31.705  1.00 91.77  ? 255 ILE C HD13 1 
ATOM   12507 N N    . ILE C 1 256 ? 6.308   3.019   36.441  1.00 74.26  ? 256 ILE C N    1 
ATOM   12508 C CA   . ILE C 1 256 ? 6.404   2.930   37.894  1.00 74.94  ? 256 ILE C CA   1 
ATOM   12509 C C    . ILE C 1 256 ? 6.725   4.283   38.512  1.00 77.41  ? 256 ILE C C    1 
ATOM   12510 O O    . ILE C 1 256 ? 6.028   4.745   39.421  1.00 77.83  ? 256 ILE C O    1 
ATOM   12511 C CB   . ILE C 1 256 ? 7.456   1.868   38.286  1.00 76.84  ? 256 ILE C CB   1 
ATOM   12512 C CG1  . ILE C 1 256 ? 6.900   0.458   38.074  1.00 75.83  ? 256 ILE C CG1  1 
ATOM   12513 C CG2  . ILE C 1 256 ? 7.895   2.062   39.734  1.00 75.88  ? 256 ILE C CG2  1 
ATOM   12514 C CD1  . ILE C 1 256 ? 7.972   -0.611  37.987  1.00 73.61  ? 256 ILE C CD1  1 
ATOM   12515 H H    . ILE C 1 256 ? 7.052   2.886   36.031  1.00 89.11  ? 256 ILE C H    1 
ATOM   12516 H HA   . ILE C 1 256 ? 5.544   2.645   38.241  1.00 89.93  ? 256 ILE C HA   1 
ATOM   12517 H HB   . ILE C 1 256 ? 8.230   1.980   37.713  1.00 92.21  ? 256 ILE C HB   1 
ATOM   12518 H HG12 . ILE C 1 256 ? 6.320   0.236   38.818  1.00 90.99  ? 256 ILE C HG12 1 
ATOM   12519 H HG13 . ILE C 1 256 ? 6.397   0.442   37.245  1.00 90.99  ? 256 ILE C HG13 1 
ATOM   12520 H HG21 . ILE C 1 256 ? 8.324   1.250   40.046  1.00 91.05  ? 256 ILE C HG21 1 
ATOM   12521 H HG22 . ILE C 1 256 ? 8.519   2.803   39.779  1.00 91.05  ? 256 ILE C HG22 1 
ATOM   12522 H HG23 . ILE C 1 256 ? 7.115   2.254   40.278  1.00 91.05  ? 256 ILE C HG23 1 
ATOM   12523 H HD11 . ILE C 1 256 ? 7.580   -1.469  38.210  1.00 88.34  ? 256 ILE C HD11 1 
ATOM   12524 H HD12 . ILE C 1 256 ? 8.323   -0.632  37.083  1.00 88.34  ? 256 ILE C HD12 1 
ATOM   12525 H HD13 . ILE C 1 256 ? 8.681   -0.398  38.613  1.00 88.34  ? 256 ILE C HD13 1 
ATOM   12526 N N    . ALA C 1 257 ? 7.785   4.934   38.039  1.00 74.39  ? 257 ALA C N    1 
ATOM   12527 C CA   . ALA C 1 257 ? 8.255   6.160   38.665  1.00 73.36  ? 257 ALA C CA   1 
ATOM   12528 C C    . ALA C 1 257 ? 9.191   6.878   37.707  1.00 73.74  ? 257 ALA C C    1 
ATOM   12529 O O    . ALA C 1 257 ? 9.641   6.320   36.705  1.00 73.56  ? 257 ALA C O    1 
ATOM   12530 C CB   . ALA C 1 257 ? 8.957   5.863   39.994  1.00 76.25  ? 257 ALA C CB   1 
ATOM   12531 H H    . ALA C 1 257 ? 8.246   4.683   37.358  1.00 89.27  ? 257 ALA C H    1 
ATOM   12532 H HA   . ALA C 1 257 ? 7.496   6.741   38.833  1.00 88.02  ? 257 ALA C HA   1 
ATOM   12533 H HB1  . ALA C 1 257 ? 9.284   6.694   40.372  1.00 91.50  ? 257 ALA C HB1  1 
ATOM   12534 H HB2  . ALA C 1 257 ? 8.323   5.450   40.601  1.00 91.50  ? 257 ALA C HB2  1 
ATOM   12535 H HB3  . ALA C 1 257 ? 9.699   5.259   39.831  1.00 91.50  ? 257 ALA C HB3  1 
ATOM   12536 N N    . GLU C 1 258 ? 9.474   8.137   38.030  1.00 76.05  ? 258 GLU C N    1 
ATOM   12537 C CA   . GLU C 1 258 ? 10.411  8.933   37.252  1.00 75.19  ? 258 GLU C CA   1 
ATOM   12538 C C    . GLU C 1 258 ? 10.858  10.112  38.098  1.00 74.41  ? 258 GLU C C    1 
ATOM   12539 O O    . GLU C 1 258 ? 10.159  10.539  39.021  1.00 73.52  ? 258 GLU C O    1 
ATOM   12540 C CB   . GLU C 1 258 ? 9.791   9.407   35.933  1.00 72.22  ? 258 GLU C CB   1 
ATOM   12541 C CG   . GLU C 1 258 ? 8.886   10.620  36.053  1.00 75.87  ? 258 GLU C CG   1 
ATOM   12542 C CD   . GLU C 1 258 ? 8.257   11.006  34.722  1.00 79.33  ? 258 GLU C CD   1 
ATOM   12543 O OE1  . GLU C 1 258 ? 9.008   11.317  33.762  1.00 82.13  ? 258 GLU C OE1  1 
ATOM   12544 O OE2  . GLU C 1 258 ? 7.009   10.992  34.633  1.00 76.82  ? 258 GLU C OE2  1 
ATOM   12545 H H    . GLU C 1 258 ? 9.133   8.554   38.701  1.00 91.26  ? 258 GLU C H    1 
ATOM   12546 H HA   . GLU C 1 258 ? 11.192  8.399   37.038  1.00 90.22  ? 258 GLU C HA   1 
ATOM   12547 H HB2  . GLU C 1 258 ? 10.508  9.637   35.321  1.00 86.66  ? 258 GLU C HB2  1 
ATOM   12548 H HB3  . GLU C 1 258 ? 9.261   8.683   35.564  1.00 86.66  ? 258 GLU C HB3  1 
ATOM   12549 H HG2  . GLU C 1 258 ? 8.172   10.422  36.679  1.00 91.04  ? 258 GLU C HG2  1 
ATOM   12550 H HG3  . GLU C 1 258 ? 9.407   11.374  36.371  1.00 91.04  ? 258 GLU C HG3  1 
ATOM   12551 N N    . GLY C 1 259 ? 12.037  10.627  37.772  1.00 71.78  ? 259 GLY C N    1 
ATOM   12552 C CA   . GLY C 1 259 ? 12.597  11.742  38.503  1.00 70.27  ? 259 GLY C CA   1 
ATOM   12553 C C    . GLY C 1 259 ? 14.095  11.839  38.330  1.00 73.50  ? 259 GLY C C    1 
ATOM   12554 O O    . GLY C 1 259 ? 14.599  11.804  37.204  1.00 76.62  ? 259 GLY C O    1 
ATOM   12555 H H    . GLY C 1 259 ? 12.531  10.344  37.127  1.00 86.14  ? 259 GLY C H    1 
ATOM   12556 H HA2  . GLY C 1 259 ? 12.197  12.568  38.188  1.00 84.32  ? 259 GLY C HA2  1 
ATOM   12557 H HA3  . GLY C 1 259 ? 12.402  11.639  39.448  1.00 84.32  ? 259 GLY C HA3  1 
ATOM   12558 N N    . LYS C 1 260 ? 14.815  11.943  39.445  1.00 75.52  ? 260 LYS C N    1 
ATOM   12559 C CA   . LYS C 1 260 ? 16.256  12.127  39.439  1.00 73.84  ? 260 LYS C CA   1 
ATOM   12560 C C    . LYS C 1 260 ? 16.928  10.982  40.181  1.00 73.80  ? 260 LYS C C    1 
ATOM   12561 O O    . LYS C 1 260 ? 16.353  10.390  41.095  1.00 72.77  ? 260 LYS C O    1 
ATOM   12562 C CB   . LYS C 1 260 ? 16.638  13.464  40.085  1.00 71.82  ? 260 LYS C CB   1 
ATOM   12563 C CG   . LYS C 1 260 ? 16.064  14.681  39.371  1.00 75.81  ? 260 LYS C CG   1 
ATOM   12564 C CD   . LYS C 1 260 ? 16.802  14.967  38.071  1.00 75.75  ? 260 LYS C CD   1 
ATOM   12565 C CE   . LYS C 1 260 ? 16.147  16.101  37.287  1.00 77.93  ? 260 LYS C CE   1 
ATOM   12566 N NZ   . LYS C 1 260 ? 15.340  15.596  36.132  1.00 83.87  ? 260 LYS C NZ   1 
ATOM   12567 H H    . LYS C 1 260 ? 14.478  11.909  40.236  1.00 90.62  ? 260 LYS C H    1 
ATOM   12568 H HA   . LYS C 1 260 ? 16.584  12.123  38.526  1.00 88.61  ? 260 LYS C HA   1 
ATOM   12569 H HB2  . LYS C 1 260 ? 16.309  13.474  40.997  1.00 86.19  ? 260 LYS C HB2  1 
ATOM   12570 H HB3  . LYS C 1 260 ? 17.605  13.547  40.080  1.00 86.19  ? 260 LYS C HB3  1 
ATOM   12571 H HG2  . LYS C 1 260 ? 15.131  14.521  39.163  1.00 90.97  ? 260 LYS C HG2  1 
ATOM   12572 H HG3  . LYS C 1 260 ? 16.148  15.459  39.946  1.00 90.97  ? 260 LYS C HG3  1 
ATOM   12573 H HD2  . LYS C 1 260 ? 17.716  15.223  38.271  1.00 90.90  ? 260 LYS C HD2  1 
ATOM   12574 H HD3  . LYS C 1 260 ? 16.794  14.170  37.517  1.00 90.90  ? 260 LYS C HD3  1 
ATOM   12575 H HE2  . LYS C 1 260 ? 15.556  16.596  37.876  1.00 93.51  ? 260 LYS C HE2  1 
ATOM   12576 H HE3  . LYS C 1 260 ? 16.837  16.688  36.940  1.00 93.51  ? 260 LYS C HE3  1 
ATOM   12577 H HZ1  . LYS C 1 260 ? 15.212  16.249  35.541  1.00 100.64 ? 260 LYS C HZ1  1 
ATOM   12578 H HZ2  . LYS C 1 260 ? 15.766  14.925  35.733  1.00 100.64 ? 260 LYS C HZ2  1 
ATOM   12579 H HZ3  . LYS C 1 260 ? 14.548  15.306  36.418  1.00 100.64 ? 260 LYS C HZ3  1 
ATOM   12580 N N    . ILE C 1 261 ? 18.153  10.672  39.774  1.00 74.29  ? 261 ILE C N    1 
ATOM   12581 C CA   . ILE C 1 261 ? 18.975  9.659   40.422  1.00 75.49  ? 261 ILE C CA   1 
ATOM   12582 C C    . ILE C 1 261 ? 20.371  10.239  40.604  1.00 75.22  ? 261 ILE C C    1 
ATOM   12583 O O    . ILE C 1 261 ? 20.883  10.935  39.721  1.00 76.91  ? 261 ILE C O    1 
ATOM   12584 C CB   . ILE C 1 261 ? 19.012  8.349   39.607  1.00 76.49  ? 261 ILE C CB   1 
ATOM   12585 C CG1  . ILE C 1 261 ? 20.102  7.418   40.129  1.00 75.95  ? 261 ILE C CG1  1 
ATOM   12586 C CG2  . ILE C 1 261 ? 19.224  8.646   38.138  1.00 76.10  ? 261 ILE C CG2  1 
ATOM   12587 C CD1  . ILE C 1 261 ? 19.987  6.002   39.623  1.00 76.25  ? 261 ILE C CD1  1 
ATOM   12588 H H    . ILE C 1 261 ? 18.541  11.046  39.103  1.00 89.14  ? 261 ILE C H    1 
ATOM   12589 H HA   . ILE C 1 261 ? 18.615  9.448   41.298  1.00 90.59  ? 261 ILE C HA   1 
ATOM   12590 H HB   . ILE C 1 261 ? 18.156  7.904   39.713  1.00 91.78  ? 261 ILE C HB   1 
ATOM   12591 H HG12 . ILE C 1 261 ? 20.965  7.762   39.851  1.00 91.13  ? 261 ILE C HG12 1 
ATOM   12592 H HG13 . ILE C 1 261 ? 20.052  7.390   41.097  1.00 91.13  ? 261 ILE C HG13 1 
ATOM   12593 H HG21 . ILE C 1 261 ? 19.346  7.810   37.661  1.00 91.33  ? 261 ILE C HG21 1 
ATOM   12594 H HG22 . ILE C 1 261 ? 18.445  9.112   37.794  1.00 91.33  ? 261 ILE C HG22 1 
ATOM   12595 H HG23 . ILE C 1 261 ? 20.012  9.202   38.039  1.00 91.33  ? 261 ILE C HG23 1 
ATOM   12596 H HD11 . ILE C 1 261 ? 20.626  5.445   40.094  1.00 91.50  ? 261 ILE C HD11 1 
ATOM   12597 H HD12 . ILE C 1 261 ? 19.086  5.681   39.784  1.00 91.50  ? 261 ILE C HD12 1 
ATOM   12598 H HD13 . ILE C 1 261 ? 20.177  5.990   38.671  1.00 91.50  ? 261 ILE C HD13 1 
ATOM   12599 N N    . TYR C 1 262 ? 20.980  9.966   41.753  1.00 75.62  ? 262 TYR C N    1 
ATOM   12600 C CA   . TYR C 1 262 ? 22.268  10.544  42.117  1.00 78.88  ? 262 TYR C CA   1 
ATOM   12601 C C    . TYR C 1 262 ? 23.320  9.447   42.137  1.00 80.17  ? 262 TYR C C    1 
ATOM   12602 O O    . TYR C 1 262 ? 23.227  8.506   42.936  1.00 81.20  ? 262 TYR C O    1 
ATOM   12603 C CB   . TYR C 1 262 ? 22.195  11.239  43.477  1.00 74.55  ? 262 TYR C CB   1 
ATOM   12604 C CG   . TYR C 1 262 ? 20.997  12.145  43.624  1.00 73.02  ? 262 TYR C CG   1 
ATOM   12605 C CD1  . TYR C 1 262 ? 21.047  13.461  43.194  1.00 70.91  ? 262 TYR C CD1  1 
ATOM   12606 C CD2  . TYR C 1 262 ? 19.815  11.682  44.193  1.00 74.53  ? 262 TYR C CD2  1 
ATOM   12607 C CE1  . TYR C 1 262 ? 19.954  14.295  43.322  1.00 70.73  ? 262 TYR C CE1  1 
ATOM   12608 C CE2  . TYR C 1 262 ? 18.715  12.509  44.326  1.00 72.66  ? 262 TYR C CE2  1 
ATOM   12609 C CZ   . TYR C 1 262 ? 18.791  13.814  43.888  1.00 71.70  ? 262 TYR C CZ   1 
ATOM   12610 O OH   . TYR C 1 262 ? 17.706  14.653  44.012  1.00 70.80  ? 262 TYR C OH   1 
ATOM   12611 H H    . TYR C 1 262 ? 20.658  9.439   42.351  1.00 90.75  ? 262 TYR C H    1 
ATOM   12612 H HA   . TYR C 1 262 ? 22.522  11.199  41.449  1.00 94.66  ? 262 TYR C HA   1 
ATOM   12613 H HB2  . TYR C 1 262 ? 22.144  10.564  44.172  1.00 89.46  ? 262 TYR C HB2  1 
ATOM   12614 H HB3  . TYR C 1 262 ? 22.992  11.779  43.596  1.00 89.46  ? 262 TYR C HB3  1 
ATOM   12615 H HD1  . TYR C 1 262 ? 21.829  13.788  42.813  1.00 85.10  ? 262 TYR C HD1  1 
ATOM   12616 H HD2  . TYR C 1 262 ? 19.763  10.801  44.489  1.00 89.44  ? 262 TYR C HD2  1 
ATOM   12617 H HE1  . TYR C 1 262 ? 20.001  15.176  43.028  1.00 84.88  ? 262 TYR C HE1  1 
ATOM   12618 H HE2  . TYR C 1 262 ? 17.930  12.187  44.708  1.00 87.19  ? 262 TYR C HE2  1 
ATOM   12619 H HH   . TYR C 1 262 ? 17.067  14.245  44.373  1.00 84.96  ? 262 TYR C HH   1 
ATOM   12620 N N    . ILE C 1 263 ? 24.317  9.574   41.266  1.00 81.63  ? 263 ILE C N    1 
ATOM   12621 C CA   . ILE C 1 263 ? 25.394  8.600   41.147  1.00 87.06  ? 263 ILE C CA   1 
ATOM   12622 C C    . ILE C 1 263 ? 26.716  9.329   41.331  1.00 91.48  ? 263 ILE C C    1 
ATOM   12623 O O    . ILE C 1 263 ? 27.008  10.288  40.606  1.00 93.81  ? 263 ILE C O    1 
ATOM   12624 C CB   . ILE C 1 263 ? 25.367  7.874   39.795  1.00 88.03  ? 263 ILE C CB   1 
ATOM   12625 C CG1  . ILE C 1 263 ? 23.963  7.357   39.496  1.00 84.89  ? 263 ILE C CG1  1 
ATOM   12626 C CG2  . ILE C 1 263 ? 26.370  6.730   39.787  1.00 91.38  ? 263 ILE C CG2  1 
ATOM   12627 C CD1  . ILE C 1 263 ? 23.314  8.044   38.318  1.00 84.14  ? 263 ILE C CD1  1 
ATOM   12628 H H    . ILE C 1 263 ? 24.392  10.234  40.720  1.00 97.95  ? 263 ILE C H    1 
ATOM   12629 H HA   . ILE C 1 263 ? 25.302  7.943   41.855  1.00 104.48 ? 263 ILE C HA   1 
ATOM   12630 H HB   . ILE C 1 263 ? 25.615  8.507   39.102  1.00 105.64 ? 263 ILE C HB   1 
ATOM   12631 H HG12 . ILE C 1 263 ? 24.014  6.409   39.297  1.00 101.87 ? 263 ILE C HG12 1 
ATOM   12632 H HG13 . ILE C 1 263 ? 23.402  7.504   40.273  1.00 101.87 ? 263 ILE C HG13 1 
ATOM   12633 H HG21 . ILE C 1 263 ? 26.295  6.249   38.948  1.00 109.66 ? 263 ILE C HG21 1 
ATOM   12634 H HG22 . ILE C 1 263 ? 27.264  7.094   39.881  1.00 109.66 ? 263 ILE C HG22 1 
ATOM   12635 H HG23 . ILE C 1 263 ? 26.176  6.135   40.528  1.00 109.66 ? 263 ILE C HG23 1 
ATOM   12636 H HD11 . ILE C 1 263 ? 22.469  7.608   38.125  1.00 100.97 ? 263 ILE C HD11 1 
ATOM   12637 H HD12 . ILE C 1 263 ? 23.162  8.976   38.540  1.00 100.97 ? 263 ILE C HD12 1 
ATOM   12638 H HD13 . ILE C 1 263 ? 23.903  7.979   37.550  1.00 100.97 ? 263 ILE C HD13 1 
ATOM   12639 N N    . GLY C 1 264 ? 27.510  8.878   42.297  1.00 96.38  ? 264 GLY C N    1 
ATOM   12640 C CA   . GLY C 1 264 ? 28.850  9.402   42.440  1.00 104.01 ? 264 GLY C CA   1 
ATOM   12641 C C    . GLY C 1 264 ? 29.717  9.034   41.251  1.00 110.38 ? 264 GLY C C    1 
ATOM   12642 O O    . GLY C 1 264 ? 29.491  8.037   40.567  1.00 110.44 ? 264 GLY C O    1 
ATOM   12643 H H    . GLY C 1 264 ? 27.295  8.276   42.873  1.00 115.66 ? 264 GLY C H    1 
ATOM   12644 H HA2  . GLY C 1 264 ? 28.815  10.369  42.511  1.00 124.81 ? 264 GLY C HA2  1 
ATOM   12645 H HA3  . GLY C 1 264 ? 29.256  9.041   43.243  1.00 124.81 ? 264 GLY C HA3  1 
ATOM   12646 N N    . LYS C 1 265 ? 30.718  9.865   40.996  1.00 124.85 ? 265 LYS C N    1 
ATOM   12647 C CA   . LYS C 1 265 ? 31.640  9.642   39.881  1.00 130.33 ? 265 LYS C CA   1 
ATOM   12648 C C    . LYS C 1 265 ? 33.065  9.687   40.430  1.00 134.15 ? 265 LYS C C    1 
ATOM   12649 O O    . LYS C 1 265 ? 33.283  10.051  41.589  1.00 128.00 ? 265 LYS C O    1 
ATOM   12650 C CB   . LYS C 1 265 ? 31.414  10.681  38.782  1.00 122.85 ? 265 LYS C CB   1 
ATOM   12651 C CG   . LYS C 1 265 ? 32.514  10.766  37.732  1.00 127.62 ? 265 LYS C CG   1 
ATOM   12652 C CD   . LYS C 1 265 ? 32.610  9.503   36.887  1.00 131.07 ? 265 LYS C CD   1 
ATOM   12653 C CE   . LYS C 1 265 ? 34.057  9.194   36.514  1.00 132.33 ? 265 LYS C CE   1 
ATOM   12654 N NZ   . LYS C 1 265 ? 34.872  8.788   37.696  1.00 131.79 ? 265 LYS C NZ   1 
ATOM   12655 H H    . LYS C 1 265 ? 30.890  10.572  41.454  1.00 149.82 ? 265 LYS C H    1 
ATOM   12656 H HA   . LYS C 1 265 ? 31.493  8.780   39.461  1.00 156.39 ? 265 LYS C HA   1 
ATOM   12657 H HB2  . LYS C 1 265 ? 30.589  10.464  38.320  1.00 147.42 ? 265 LYS C HB2  1 
ATOM   12658 H HB3  . LYS C 1 265 ? 31.341  11.555  39.197  1.00 147.42 ? 265 LYS C HB3  1 
ATOM   12659 H HG2  . LYS C 1 265 ? 32.331  11.512  37.139  1.00 153.14 ? 265 LYS C HG2  1 
ATOM   12660 H HG3  . LYS C 1 265 ? 33.367  10.897  38.175  1.00 153.14 ? 265 LYS C HG3  1 
ATOM   12661 H HD2  . LYS C 1 265 ? 32.257  8.752   37.390  1.00 157.29 ? 265 LYS C HD2  1 
ATOM   12662 H HD3  . LYS C 1 265 ? 32.103  9.624   36.069  1.00 157.29 ? 265 LYS C HD3  1 
ATOM   12663 H HE2  . LYS C 1 265 ? 34.072  8.467   35.873  1.00 158.80 ? 265 LYS C HE2  1 
ATOM   12664 H HE3  . LYS C 1 265 ? 34.462  9.986   36.127  1.00 158.80 ? 265 LYS C HE3  1 
ATOM   12665 H HZ1  . LYS C 1 265 ? 35.691  8.555   37.435  1.00 158.14 ? 265 LYS C HZ1  1 
ATOM   12666 H HZ2  . LYS C 1 265 ? 34.934  9.464   38.271  1.00 158.14 ? 265 LYS C HZ2  1 
ATOM   12667 H HZ3  . LYS C 1 265 ? 34.492  8.095   38.104  1.00 158.14 ? 265 LYS C HZ3  1 
ATOM   12668 N N    . ARG D 1 3   ? 34.093  20.000  23.061  1.00 103.74 ? 3   ARG D N    1 
ATOM   12669 C CA   . ARG D 1 3   ? 33.635  20.361  24.401  1.00 107.10 ? 3   ARG D CA   1 
ATOM   12670 C C    . ARG D 1 3   ? 32.380  19.573  24.777  1.00 102.93 ? 3   ARG D C    1 
ATOM   12671 O O    . ARG D 1 3   ? 31.755  18.933  23.931  1.00 97.57  ? 3   ARG D O    1 
ATOM   12672 C CB   . ARG D 1 3   ? 33.365  21.865  24.485  1.00 111.25 ? 3   ARG D CB   1 
ATOM   12673 C CG   . ARG D 1 3   ? 34.491  22.727  23.928  1.00 119.84 ? 3   ARG D CG   1 
ATOM   12674 C CD   . ARG D 1 3   ? 34.138  24.214  23.948  1.00 125.30 ? 3   ARG D CD   1 
ATOM   12675 N NE   . ARG D 1 3   ? 35.202  25.015  24.543  1.00 127.89 ? 3   ARG D NE   1 
ATOM   12676 C CZ   . ARG D 1 3   ? 35.777  26.061  23.964  1.00 130.29 ? 3   ARG D CZ   1 
ATOM   12677 N NH1  . ARG D 1 3   ? 35.411  26.477  22.761  1.00 130.81 ? 3   ARG D NH1  1 
ATOM   12678 N NH2  . ARG D 1 3   ? 36.744  26.708  24.609  1.00 129.08 ? 3   ARG D NH2  1 
ATOM   12679 H H    . ARG D 1 3   ? 33.459  19.905  22.487  1.00 124.49 ? 3   ARG D H    1 
ATOM   12680 H HA   . ARG D 1 3   ? 34.328  20.145  25.044  1.00 128.52 ? 3   ARG D HA   1 
ATOM   12681 H HB2  . ARG D 1 3   ? 32.562  22.065  23.980  1.00 133.50 ? 3   ARG D HB2  1 
ATOM   12682 H HB3  . ARG D 1 3   ? 33.241  22.107  25.416  1.00 133.50 ? 3   ARG D HB3  1 
ATOM   12683 H HG2  . ARG D 1 3   ? 35.288  22.598  24.466  1.00 143.81 ? 3   ARG D HG2  1 
ATOM   12684 H HG3  . ARG D 1 3   ? 34.666  22.469  23.009  1.00 143.81 ? 3   ARG D HG3  1 
ATOM   12685 H HD2  . ARG D 1 3   ? 33.998  24.521  23.038  1.00 150.36 ? 3   ARG D HD2  1 
ATOM   12686 H HD3  . ARG D 1 3   ? 33.331  24.344  24.470  1.00 150.36 ? 3   ARG D HD3  1 
ATOM   12687 H HE   . ARG D 1 3   ? 35.476  24.793  25.327  1.00 153.47 ? 3   ARG D HE   1 
ATOM   12688 H HH11 . ARG D 1 3   ? 34.787  26.066  22.335  1.00 156.97 ? 3   ARG D HH11 1 
ATOM   12689 H HH12 . ARG D 1 3   ? 35.798  27.158  22.405  1.00 156.97 ? 3   ARG D HH12 1 
ATOM   12690 H HH21 . ARG D 1 3   ? 37.124  27.387  24.244  1.00 154.90 ? 3   ARG D HH21 1 
ATOM   12691 H HH22 . ARG D 1 3   ? 36.989  26.446  25.391  1.00 154.90 ? 3   ARG D HH22 1 
ATOM   12692 N N    . LYS D 1 4   ? 32.015  19.623  26.054  1.00 105.86 ? 4   LYS D N    1 
ATOM   12693 C CA   . LYS D 1 4   ? 30.909  18.841  26.593  1.00 101.08 ? 4   LYS D CA   1 
ATOM   12694 C C    . LYS D 1 4   ? 29.756  19.767  26.948  1.00 97.57  ? 4   LYS D C    1 
ATOM   12695 O O    . LYS D 1 4   ? 29.957  20.801  27.596  1.00 101.23 ? 4   LYS D O    1 
ATOM   12696 C CB   . LYS D 1 4   ? 31.356  18.045  27.822  1.00 101.03 ? 4   LYS D CB   1 
ATOM   12697 C CG   . LYS D 1 4   ? 30.355  17.008  28.352  1.00 104.84 ? 4   LYS D CG   1 
ATOM   12698 C CD   . LYS D 1 4   ? 29.490  16.366  27.268  1.00 102.14 ? 4   LYS D CD   1 
ATOM   12699 C CE   . LYS D 1 4   ? 30.305  15.546  26.281  1.00 100.14 ? 4   LYS D CE   1 
ATOM   12700 N NZ   . LYS D 1 4   ? 29.415  14.850  25.308  1.00 98.98  ? 4   LYS D NZ   1 
ATOM   12701 H H    . LYS D 1 4   ? 32.403  20.116  26.642  1.00 127.03 ? 4   LYS D H    1 
ATOM   12702 H HA   . LYS D 1 4   ? 30.594  18.215  25.922  1.00 121.29 ? 4   LYS D HA   1 
ATOM   12703 H HB2  . LYS D 1 4   ? 32.170  17.568  27.595  1.00 121.24 ? 4   LYS D HB2  1 
ATOM   12704 H HB3  . LYS D 1 4   ? 31.529  18.671  28.542  1.00 121.24 ? 4   LYS D HB3  1 
ATOM   12705 H HG2  . LYS D 1 4   ? 30.847  16.298  28.794  1.00 125.81 ? 4   LYS D HG2  1 
ATOM   12706 H HG3  . LYS D 1 4   ? 29.761  17.442  28.984  1.00 125.81 ? 4   LYS D HG3  1 
ATOM   12707 H HD2  . LYS D 1 4   ? 28.843  15.778  27.686  1.00 122.56 ? 4   LYS D HD2  1 
ATOM   12708 H HD3  . LYS D 1 4   ? 29.033  17.064  26.773  1.00 122.56 ? 4   LYS D HD3  1 
ATOM   12709 H HE2  . LYS D 1 4   ? 30.902  16.131  25.789  1.00 120.17 ? 4   LYS D HE2  1 
ATOM   12710 H HE3  . LYS D 1 4   ? 30.817  14.877  26.762  1.00 120.17 ? 4   LYS D HE3  1 
ATOM   12711 H HZ1  . LYS D 1 4   ? 29.013  15.446  24.783  1.00 118.78 ? 4   LYS D HZ1  1 
ATOM   12712 H HZ2  . LYS D 1 4   ? 29.893  14.295  24.802  1.00 118.78 ? 4   LYS D HZ2  1 
ATOM   12713 H HZ3  . LYS D 1 4   ? 28.795  14.382  25.743  1.00 118.78 ? 4   LYS D HZ3  1 
ATOM   12714 N N    . VAL D 1 5   ? 28.557  19.394  26.518  1.00 94.11  ? 5   VAL D N    1 
ATOM   12715 C CA   . VAL D 1 5   ? 27.357  20.152  26.841  1.00 91.36  ? 5   VAL D CA   1 
ATOM   12716 C C    . VAL D 1 5   ? 26.911  19.796  28.252  1.00 90.63  ? 5   VAL D C    1 
ATOM   12717 O O    . VAL D 1 5   ? 26.933  18.629  28.662  1.00 85.36  ? 5   VAL D O    1 
ATOM   12718 C CB   . VAL D 1 5   ? 26.247  19.875  25.810  1.00 85.48  ? 5   VAL D CB   1 
ATOM   12719 C CG1  . VAL D 1 5   ? 26.804  19.954  24.385  1.00 85.23  ? 5   VAL D CG1  1 
ATOM   12720 C CG2  . VAL D 1 5   ? 25.607  18.523  26.068  1.00 82.56  ? 5   VAL D CG2  1 
ATOM   12721 H H    . VAL D 1 5   ? 28.411  18.699  26.033  1.00 112.94 ? 5   VAL D H    1 
ATOM   12722 H HA   . VAL D 1 5   ? 27.560  21.100  26.812  1.00 109.63 ? 5   VAL D HA   1 
ATOM   12723 H HB   . VAL D 1 5   ? 25.559  20.552  25.898  1.00 102.58 ? 5   VAL D HB   1 
ATOM   12724 H HG11 . VAL D 1 5   ? 26.065  19.942  23.756  1.00 102.27 ? 5   VAL D HG11 1 
ATOM   12725 H HG12 . VAL D 1 5   ? 27.308  20.776  24.288  1.00 102.27 ? 5   VAL D HG12 1 
ATOM   12726 H HG13 . VAL D 1 5   ? 27.382  19.191  24.229  1.00 102.27 ? 5   VAL D HG13 1 
ATOM   12727 H HG21 . VAL D 1 5   ? 25.137  18.238  25.269  1.00 99.07  ? 5   VAL D HG21 1 
ATOM   12728 H HG22 . VAL D 1 5   ? 26.301  17.882  26.290  1.00 99.07  ? 5   VAL D HG22 1 
ATOM   12729 H HG23 . VAL D 1 5   ? 24.985  18.604  26.808  1.00 99.07  ? 5   VAL D HG23 1 
ATOM   12730 N N    . GLN D 1 6   ? 26.519  20.813  29.006  1.00 85.76  ? 6   GLN D N    1 
ATOM   12731 C CA   . GLN D 1 6   ? 25.978  20.661  30.348  1.00 81.77  ? 6   GLN D CA   1 
ATOM   12732 C C    . GLN D 1 6   ? 24.473  20.872  30.265  1.00 81.97  ? 6   GLN D C    1 
ATOM   12733 O O    . GLN D 1 6   ? 24.017  21.900  29.756  1.00 82.14  ? 6   GLN D O    1 
ATOM   12734 C CB   . GLN D 1 6   ? 26.631  21.658  31.302  1.00 85.31  ? 6   GLN D CB   1 
ATOM   12735 C CG   . GLN D 1 6   ? 26.141  21.561  32.728  1.00 88.67  ? 6   GLN D CG   1 
ATOM   12736 C CD   . GLN D 1 6   ? 27.227  21.881  33.734  1.00 86.21  ? 6   GLN D CD   1 
ATOM   12737 O OE1  . GLN D 1 6   ? 27.678  23.023  33.837  1.00 84.82  ? 6   GLN D OE1  1 
ATOM   12738 N NE2  . GLN D 1 6   ? 27.653  20.869  34.486  1.00 89.66  ? 6   GLN D NE2  1 
ATOM   12739 H H    . GLN D 1 6   ? 26.559  21.633  28.751  1.00 102.90 ? 6   GLN D H    1 
ATOM   12740 H HA   . GLN D 1 6   ? 26.145  19.769  30.691  1.00 98.12  ? 6   GLN D HA   1 
ATOM   12741 H HB2  . GLN D 1 6   ? 27.588  21.500  31.308  1.00 102.37 ? 6   GLN D HB2  1 
ATOM   12742 H HB3  . GLN D 1 6   ? 26.445  22.556  30.987  1.00 102.37 ? 6   GLN D HB3  1 
ATOM   12743 H HG2  . GLN D 1 6   ? 25.415  22.191  32.858  1.00 106.40 ? 6   GLN D HG2  1 
ATOM   12744 H HG3  . GLN D 1 6   ? 25.831  20.658  32.896  1.00 106.40 ? 6   GLN D HG3  1 
ATOM   12745 H HE21 . GLN D 1 6   ? 27.313  20.085  34.385  1.00 107.59 ? 6   GLN D HE21 1 
ATOM   12746 H HE22 . GLN D 1 6   ? 28.269  20.998  35.072  1.00 107.59 ? 6   GLN D HE22 1 
ATOM   12747 N N    . VAL D 1 7   ? 23.706  19.897  30.747  1.00 83.65  ? 7   VAL D N    1 
ATOM   12748 C CA   . VAL D 1 7   ? 22.251  19.894  30.624  1.00 81.94  ? 7   VAL D CA   1 
ATOM   12749 C C    . VAL D 1 7   ? 21.665  20.234  31.987  1.00 75.27  ? 7   VAL D C    1 
ATOM   12750 O O    . VAL D 1 7   ? 21.820  19.464  32.944  1.00 83.93  ? 7   VAL D O    1 
ATOM   12751 C CB   . VAL D 1 7   ? 21.722  18.544  30.118  1.00 77.98  ? 7   VAL D CB   1 
ATOM   12752 C CG1  . VAL D 1 7   ? 20.248  18.642  29.750  1.00 76.30  ? 7   VAL D CG1  1 
ATOM   12753 C CG2  . VAL D 1 7   ? 22.540  18.067  28.927  1.00 73.93  ? 7   VAL D CG2  1 
ATOM   12754 H H    . VAL D 1 7   ? 24.015  19.209  31.160  1.00 100.38 ? 7   VAL D H    1 
ATOM   12755 H HA   . VAL D 1 7   ? 21.983  20.581  29.994  1.00 98.33  ? 7   VAL D HA   1 
ATOM   12756 H HB   . VAL D 1 7   ? 21.808  17.890  30.829  1.00 93.57  ? 7   VAL D HB   1 
ATOM   12757 H HG11 . VAL D 1 7   ? 19.901  17.750  29.591  1.00 91.56  ? 7   VAL D HG11 1 
ATOM   12758 H HG12 . VAL D 1 7   ? 19.766  19.058  30.483  1.00 91.56  ? 7   VAL D HG12 1 
ATOM   12759 H HG13 . VAL D 1 7   ? 20.157  19.180  28.948  1.00 91.56  ? 7   VAL D HG13 1 
ATOM   12760 H HG21 . VAL D 1 7   ? 22.108  17.292  28.536  1.00 88.71  ? 7   VAL D HG21 1 
ATOM   12761 H HG22 . VAL D 1 7   ? 22.591  18.782  28.272  1.00 88.71  ? 7   VAL D HG22 1 
ATOM   12762 H HG23 . VAL D 1 7   ? 23.431  17.832  29.229  1.00 88.71  ? 7   VAL D HG23 1 
ATOM   12763 N N    . LEU D 1 8   ? 20.982  21.376  32.072  1.00 75.87  ? 8   LEU D N    1 
ATOM   12764 C CA   . LEU D 1 8   ? 20.437  21.877  33.326  1.00 76.15  ? 8   LEU D CA   1 
ATOM   12765 C C    . LEU D 1 8   ? 18.927  22.048  33.224  1.00 75.15  ? 8   LEU D C    1 
ATOM   12766 O O    . LEU D 1 8   ? 18.405  22.437  32.174  1.00 80.45  ? 8   LEU D O    1 
ATOM   12767 C CB   . LEU D 1 8   ? 21.081  23.218  33.704  1.00 76.74  ? 8   LEU D CB   1 
ATOM   12768 C CG   . LEU D 1 8   ? 22.607  23.292  33.636  1.00 78.12  ? 8   LEU D CG   1 
ATOM   12769 C CD1  . LEU D 1 8   ? 23.124  24.526  34.355  1.00 77.93  ? 8   LEU D CD1  1 
ATOM   12770 C CD2  . LEU D 1 8   ? 23.250  22.044  34.222  1.00 81.71  ? 8   LEU D CD2  1 
ATOM   12771 H H    . LEU D 1 8   ? 20.819  21.887  31.399  1.00 91.05  ? 8   LEU D H    1 
ATOM   12772 H HA   . LEU D 1 8   ? 20.616  21.232  34.028  1.00 91.38  ? 8   LEU D HA   1 
ATOM   12773 H HB2  . LEU D 1 8   ? 20.737  23.895  33.101  1.00 92.09  ? 8   LEU D HB2  1 
ATOM   12774 H HB3  . LEU D 1 8   ? 20.828  23.425  34.617  1.00 92.09  ? 8   LEU D HB3  1 
ATOM   12775 H HG   . LEU D 1 8   ? 22.860  23.350  32.701  1.00 93.74  ? 8   LEU D HG   1 
ATOM   12776 H HD11 . LEU D 1 8   ? 24.087  24.575  34.247  1.00 93.52  ? 8   LEU D HD11 1 
ATOM   12777 H HD12 . LEU D 1 8   ? 22.708  25.314  33.971  1.00 93.52  ? 8   LEU D HD12 1 
ATOM   12778 H HD13 . LEU D 1 8   ? 22.901  24.460  35.297  1.00 93.52  ? 8   LEU D HD13 1 
ATOM   12779 H HD21 . LEU D 1 8   ? 24.081  22.291  34.657  1.00 98.05  ? 8   LEU D HD21 1 
ATOM   12780 H HD22 . LEU D 1 8   ? 22.643  21.650  34.868  1.00 98.05  ? 8   LEU D HD22 1 
ATOM   12781 H HD23 . LEU D 1 8   ? 23.426  21.413  33.506  1.00 98.05  ? 8   LEU D HD23 1 
ATOM   12782 N N    . ASP D 1 9   ? 18.227  21.749  34.316  1.00 77.64  ? 9   ASP D N    1 
ATOM   12783 C CA   . ASP D 1 9   ? 16.789  21.964  34.377  1.00 78.94  ? 9   ASP D CA   1 
ATOM   12784 C C    . ASP D 1 9   ? 16.497  23.425  34.690  1.00 78.63  ? 9   ASP D C    1 
ATOM   12785 O O    . ASP D 1 9   ? 17.020  23.978  35.664  1.00 80.92  ? 9   ASP D O    1 
ATOM   12786 C CB   . ASP D 1 9   ? 16.155  21.074  35.443  1.00 77.79  ? 9   ASP D CB   1 
ATOM   12787 C CG   . ASP D 1 9   ? 16.307  19.602  35.141  1.00 84.33  ? 9   ASP D CG   1 
ATOM   12788 O OD1  . ASP D 1 9   ? 15.538  19.081  34.298  1.00 85.36  ? 9   ASP D OD1  1 
ATOM   12789 O OD2  . ASP D 1 9   ? 17.197  18.971  35.749  1.00 86.87  ? 9   ASP D OD2  1 
ATOM   12790 H H    . ASP D 1 9   ? 18.565  21.420  35.035  1.00 93.16  ? 9   ASP D H    1 
ATOM   12791 H HA   . ASP D 1 9   ? 16.398  21.739  33.519  1.00 94.73  ? 9   ASP D HA   1 
ATOM   12792 H HB2  . ASP D 1 9   ? 16.581  21.251  36.297  1.00 93.34  ? 9   ASP D HB2  1 
ATOM   12793 H HB3  . ASP D 1 9   ? 15.207  21.273  35.498  1.00 93.34  ? 9   ASP D HB3  1 
ATOM   12794 N N    . PHE D 1 10  ? 15.643  24.043  33.881  1.00 73.65  ? 10  PHE D N    1 
ATOM   12795 C CA   . PHE D 1 10  ? 15.337  25.457  34.013  1.00 73.80  ? 10  PHE D CA   1 
ATOM   12796 C C    . PHE D 1 10  ? 13.839  25.675  34.182  1.00 71.97  ? 10  PHE D C    1 
ATOM   12797 O O    . PHE D 1 10  ? 13.015  24.838  33.807  1.00 70.42  ? 10  PHE D O    1 
ATOM   12798 C CB   . PHE D 1 10  ? 15.830  26.247  32.787  1.00 74.22  ? 10  PHE D CB   1 
ATOM   12799 C CG   . PHE D 1 10  ? 14.835  26.299  31.660  1.00 73.99  ? 10  PHE D CG   1 
ATOM   12800 C CD1  . PHE D 1 10  ? 13.867  27.292  31.614  1.00 72.99  ? 10  PHE D CD1  1 
ATOM   12801 C CD2  . PHE D 1 10  ? 14.865  25.353  30.648  1.00 74.86  ? 10  PHE D CD2  1 
ATOM   12802 C CE1  . PHE D 1 10  ? 12.950  27.336  30.582  1.00 75.59  ? 10  PHE D CE1  1 
ATOM   12803 C CE2  . PHE D 1 10  ? 13.951  25.395  29.616  1.00 75.14  ? 10  PHE D CE2  1 
ATOM   12804 C CZ   . PHE D 1 10  ? 12.993  26.388  29.584  1.00 76.26  ? 10  PHE D CZ   1 
ATOM   12805 H H    . PHE D 1 10  ? 15.223  23.655  33.239  1.00 88.38  ? 10  PHE D H    1 
ATOM   12806 H HA   . PHE D 1 10  ? 15.778  25.795  34.807  1.00 88.56  ? 10  PHE D HA   1 
ATOM   12807 H HB2  . PHE D 1 10  ? 16.017  27.159  33.059  1.00 89.07  ? 10  PHE D HB2  1 
ATOM   12808 H HB3  . PHE D 1 10  ? 16.638  25.828  32.451  1.00 89.07  ? 10  PHE D HB3  1 
ATOM   12809 H HD1  . PHE D 1 10  ? 13.836  27.935  32.285  1.00 87.59  ? 10  PHE D HD1  1 
ATOM   12810 H HD2  . PHE D 1 10  ? 15.508  24.681  30.665  1.00 89.84  ? 10  PHE D HD2  1 
ATOM   12811 H HE1  . PHE D 1 10  ? 12.305  28.005  30.561  1.00 90.71  ? 10  PHE D HE1  1 
ATOM   12812 H HE2  . PHE D 1 10  ? 13.981  24.755  28.942  1.00 90.17  ? 10  PHE D HE2  1 
ATOM   12813 H HZ   . PHE D 1 10  ? 12.376  26.417  28.889  1.00 91.51  ? 10  PHE D HZ   1 
ATOM   12814 N N    . ILE D 1 11  ? 13.502  26.825  34.763  1.00 74.19  ? 11  ILE D N    1 
ATOM   12815 C CA   . ILE D 1 11  ? 12.137  27.339  34.779  1.00 72.99  ? 11  ILE D CA   1 
ATOM   12816 C C    . ILE D 1 11  ? 12.220  28.831  34.487  1.00 71.30  ? 11  ILE D C    1 
ATOM   12817 O O    . ILE D 1 11  ? 12.905  29.566  35.204  1.00 74.24  ? 11  ILE D O    1 
ATOM   12818 C CB   . ILE D 1 11  ? 11.424  27.097  36.119  1.00 71.51  ? 11  ILE D CB   1 
ATOM   12819 C CG1  . ILE D 1 11  ? 11.550  25.637  36.545  1.00 70.34  ? 11  ILE D CG1  1 
ATOM   12820 C CG2  . ILE D 1 11  ? 9.951   27.481  35.997  1.00 72.54  ? 11  ILE D CG2  1 
ATOM   12821 C CD1  . ILE D 1 11  ? 12.653  25.387  37.557  1.00 72.80  ? 11  ILE D CD1  1 
ATOM   12822 H H    . ILE D 1 11  ? 14.062  27.339  35.166  1.00 89.02  ? 11  ILE D H    1 
ATOM   12823 H HA   . ILE D 1 11  ? 11.617  26.903  34.085  1.00 87.58  ? 11  ILE D HA   1 
ATOM   12824 H HB   . ILE D 1 11  ? 11.847  27.649  36.794  1.00 85.81  ? 11  ILE D HB   1 
ATOM   12825 H HG12 . ILE D 1 11  ? 10.712  25.356  36.945  1.00 84.41  ? 11  ILE D HG12 1 
ATOM   12826 H HG13 . ILE D 1 11  ? 11.740  25.099  35.761  1.00 84.41  ? 11  ILE D HG13 1 
ATOM   12827 H HG21 . ILE D 1 11  ? 9.502   27.279  36.833  1.00 87.05  ? 11  ILE D HG21 1 
ATOM   12828 H HG22 . ILE D 1 11  ? 9.886   28.430  35.807  1.00 87.05  ? 11  ILE D HG22 1 
ATOM   12829 H HG23 . ILE D 1 11  ? 9.550   26.971  35.275  1.00 87.05  ? 11  ILE D HG23 1 
ATOM   12830 H HD11 . ILE D 1 11  ? 12.653  24.448  37.799  1.00 87.36  ? 11  ILE D HD11 1 
ATOM   12831 H HD12 . ILE D 1 11  ? 13.506  25.626  37.161  1.00 87.36  ? 11  ILE D HD12 1 
ATOM   12832 H HD13 . ILE D 1 11  ? 12.490  25.931  38.343  1.00 87.36  ? 11  ILE D HD13 1 
ATOM   12833 N N    . LYS D 1 12  ? 11.553  29.278  33.433  1.00 70.81  ? 12  LYS D N    1 
ATOM   12834 C CA   . LYS D 1 12  ? 11.465  30.696  33.105  1.00 72.71  ? 12  LYS D CA   1 
ATOM   12835 C C    . LYS D 1 12  ? 10.159  31.239  33.669  1.00 73.68  ? 12  LYS D C    1 
ATOM   12836 O O    . LYS D 1 12  ? 9.083   30.703  33.378  1.00 74.36  ? 12  LYS D O    1 
ATOM   12837 C CB   . LYS D 1 12  ? 11.535  30.941  31.599  1.00 71.29  ? 12  LYS D CB   1 
ATOM   12838 C CG   . LYS D 1 12  ? 11.409  32.410  31.215  1.00 71.57  ? 12  LYS D CG   1 
ATOM   12839 C CD   . LYS D 1 12  ? 11.957  32.677  29.820  1.00 76.12  ? 12  LYS D CD   1 
ATOM   12840 C CE   . LYS D 1 12  ? 12.548  34.078  29.719  1.00 77.75  ? 12  LYS D CE   1 
ATOM   12841 N NZ   . LYS D 1 12  ? 13.093  34.373  28.364  1.00 79.33  ? 12  LYS D NZ   1 
ATOM   12842 H H    . LYS D 1 12  ? 11.134  28.770  32.881  1.00 84.97  ? 12  LYS D H    1 
ATOM   12843 H HA   . LYS D 1 12  ? 12.212  31.168  33.505  1.00 87.25  ? 12  LYS D HA   1 
ATOM   12844 H HB2  . LYS D 1 12  ? 12.390  30.621  31.270  1.00 85.55  ? 12  LYS D HB2  1 
ATOM   12845 H HB3  . LYS D 1 12  ? 10.812  30.458  31.170  1.00 85.55  ? 12  LYS D HB3  1 
ATOM   12846 H HG2  . LYS D 1 12  ? 10.473  32.665  31.228  1.00 85.89  ? 12  LYS D HG2  1 
ATOM   12847 H HG3  . LYS D 1 12  ? 11.908  32.950  31.847  1.00 85.89  ? 12  LYS D HG3  1 
ATOM   12848 H HD2  . LYS D 1 12  ? 12.656  32.035  29.620  1.00 91.35  ? 12  LYS D HD2  1 
ATOM   12849 H HD3  . LYS D 1 12  ? 11.239  32.600  29.172  1.00 91.35  ? 12  LYS D HD3  1 
ATOM   12850 H HE2  . LYS D 1 12  ? 11.855  34.729  29.912  1.00 93.30  ? 12  LYS D HE2  1 
ATOM   12851 H HE3  . LYS D 1 12  ? 13.271  34.163  30.359  1.00 93.30  ? 12  LYS D HE3  1 
ATOM   12852 H HZ1  . LYS D 1 12  ? 12.446  34.317  27.756  1.00 95.20  ? 12  LYS D HZ1  1 
ATOM   12853 H HZ2  . LYS D 1 12  ? 13.733  33.789  28.159  1.00 95.20  ? 12  LYS D HZ2  1 
ATOM   12854 H HZ3  . LYS D 1 12  ? 13.436  35.194  28.346  1.00 95.20  ? 12  LYS D HZ3  1 
ATOM   12855 N N    . ILE D 1 13  ? 10.257  32.294  34.470  1.00 72.30  ? 13  ILE D N    1 
ATOM   12856 C CA   . ILE D 1 13  ? 9.113   32.848  35.179  1.00 74.68  ? 13  ILE D CA   1 
ATOM   12857 C C    . ILE D 1 13  ? 9.091   34.351  34.954  1.00 74.22  ? 13  ILE D C    1 
ATOM   12858 O O    . ILE D 1 13  ? 10.137  34.993  34.811  1.00 74.30  ? 13  ILE D O    1 
ATOM   12859 C CB   . ILE D 1 13  ? 9.160   32.515  36.686  1.00 73.69  ? 13  ILE D CB   1 
ATOM   12860 C CG1  . ILE D 1 13  ? 9.445   31.020  36.876  1.00 73.19  ? 13  ILE D CG1  1 
ATOM   12861 C CG2  . ILE D 1 13  ? 7.859   32.922  37.359  1.00 73.76  ? 13  ILE D CG2  1 
ATOM   12862 C CD1  . ILE D 1 13  ? 9.521   30.572  38.327  1.00 74.04  ? 13  ILE D CD1  1 
ATOM   12863 H H    . ILE D 1 13  ? 10.992  32.714  34.622  1.00 86.76  ? 13  ILE D H    1 
ATOM   12864 H HA   . ILE D 1 13  ? 8.293   32.477  34.817  1.00 89.61  ? 13  ILE D HA   1 
ATOM   12865 H HB   . ILE D 1 13  ? 9.878   33.017  37.102  1.00 88.43  ? 13  ILE D HB   1 
ATOM   12866 H HG12 . ILE D 1 13  ? 8.736   30.513  36.450  1.00 87.83  ? 13  ILE D HG12 1 
ATOM   12867 H HG13 . ILE D 1 13  ? 10.297  30.813  36.461  1.00 87.83  ? 13  ILE D HG13 1 
ATOM   12868 H HG21 . ILE D 1 13  ? 7.867   32.610  38.277  1.00 88.52  ? 13  ILE D HG21 1 
ATOM   12869 H HG22 . ILE D 1 13  ? 7.782   33.889  37.339  1.00 88.52  ? 13  ILE D HG22 1 
ATOM   12870 H HG23 . ILE D 1 13  ? 7.116   32.521  36.880  1.00 88.52  ? 13  ILE D HG23 1 
ATOM   12871 H HD11 . ILE D 1 13  ? 9.922   29.690  38.364  1.00 88.84  ? 13  ILE D HD11 1 
ATOM   12872 H HD12 . ILE D 1 13  ? 10.064  31.204  38.824  1.00 88.84  ? 13  ILE D HD12 1 
ATOM   12873 H HD13 . ILE D 1 13  ? 8.624   30.544  38.696  1.00 88.84  ? 13  ILE D HD13 1 
ATOM   12874 N N    . ASN D 1 14  ? 7.880   34.912  34.922  1.00 73.99  ? 14  ASN D N    1 
ATOM   12875 C CA   . ASN D 1 14  ? 7.678   36.339  34.694  1.00 78.35  ? 14  ASN D CA   1 
ATOM   12876 C C    . ASN D 1 14  ? 7.097   36.988  35.943  1.00 78.06  ? 14  ASN D C    1 
ATOM   12877 O O    . ASN D 1 14  ? 5.871   37.138  36.061  1.00 78.04  ? 14  ASN D O    1 
ATOM   12878 C CB   . ASN D 1 14  ? 6.758   36.564  33.492  1.00 75.64  ? 14  ASN D CB   1 
ATOM   12879 C CG   . ASN D 1 14  ? 6.440   38.025  33.275  1.00 76.10  ? 14  ASN D CG   1 
ATOM   12880 O OD1  . ASN D 1 14  ? 7.191   38.901  33.706  1.00 77.24  ? 14  ASN D OD1  1 
ATOM   12881 N ND2  . ASN D 1 14  ? 5.321   38.299  32.611  1.00 76.25  ? 14  ASN D ND2  1 
ATOM   12882 H H    . ASN D 1 14  ? 7.148   34.475  35.032  1.00 88.79  ? 14  ASN D H    1 
ATOM   12883 H HA   . ASN D 1 14  ? 8.538   36.751  34.518  1.00 94.02  ? 14  ASN D HA   1 
ATOM   12884 H HB2  . ASN D 1 14  ? 7.193   36.228  32.692  1.00 90.76  ? 14  ASN D HB2  1 
ATOM   12885 H HB3  . ASN D 1 14  ? 5.923   36.092  33.638  1.00 90.76  ? 14  ASN D HB3  1 
ATOM   12886 H HD21 . ASN D 1 14  ? 5.099   39.117  32.464  1.00 91.50  ? 14  ASN D HD21 1 
ATOM   12887 H HD22 . ASN D 1 14  ? 4.820   37.660  32.329  1.00 91.50  ? 14  ASN D HD22 1 
ATOM   12888 N N    . PRO D 1 15  ? 7.933   37.398  36.906  1.00 79.61  ? 15  PRO D N    1 
ATOM   12889 C CA   . PRO D 1 15  ? 7.410   38.096  38.088  1.00 77.89  ? 15  PRO D CA   1 
ATOM   12890 C C    . PRO D 1 15  ? 7.266   39.592  37.871  1.00 77.31  ? 15  PRO D C    1 
ATOM   12891 O O    . PRO D 1 15  ? 8.219   40.349  38.082  1.00 76.17  ? 15  PRO D O    1 
ATOM   12892 C CB   . PRO D 1 15  ? 8.460   37.788  39.162  1.00 79.88  ? 15  PRO D CB   1 
ATOM   12893 C CG   . PRO D 1 15  ? 9.745   37.712  38.381  1.00 78.77  ? 15  PRO D CG   1 
ATOM   12894 C CD   . PRO D 1 15  ? 9.391   37.179  36.995  1.00 78.98  ? 15  PRO D CD   1 
ATOM   12895 H HA   . PRO D 1 15  ? 6.552   37.725  38.348  1.00 93.46  ? 15  PRO D HA   1 
ATOM   12896 H HB2  . PRO D 1 15  ? 8.488   38.500  39.820  1.00 95.86  ? 15  PRO D HB2  1 
ATOM   12897 H HB3  . PRO D 1 15  ? 8.260   36.944  39.596  1.00 95.86  ? 15  PRO D HB3  1 
ATOM   12898 H HG2  . PRO D 1 15  ? 10.136  38.597  38.315  1.00 94.52  ? 15  PRO D HG2  1 
ATOM   12899 H HG3  . PRO D 1 15  ? 10.361  37.110  38.829  1.00 94.52  ? 15  PRO D HG3  1 
ATOM   12900 H HD2  . PRO D 1 15  ? 9.857   37.676  36.304  1.00 94.77  ? 15  PRO D HD2  1 
ATOM   12901 H HD3  . PRO D 1 15  ? 9.603   36.235  36.924  1.00 94.77  ? 15  PRO D HD3  1 
ATOM   12902 N N    . ALA D 1 16  ? 6.079   40.027  37.449  1.00 80.46  ? 16  ALA D N    1 
ATOM   12903 C CA   . ALA D 1 16  ? 5.786   41.441  37.219  1.00 84.21  ? 16  ALA D CA   1 
ATOM   12904 C C    . ALA D 1 16  ? 6.723   42.065  36.185  1.00 82.30  ? 16  ALA D C    1 
ATOM   12905 O O    . ALA D 1 16  ? 6.948   43.279  36.188  1.00 83.65  ? 16  ALA D O    1 
ATOM   12906 C CB   . ALA D 1 16  ? 5.844   42.237  38.528  1.00 77.82  ? 16  ALA D CB   1 
ATOM   12907 H H    . ALA D 1 16  ? 5.412   39.509  37.284  1.00 96.55  ? 16  ALA D H    1 
ATOM   12908 H HA   . ALA D 1 16  ? 4.886   41.502  36.863  1.00 101.05 ? 16  ALA D HA   1 
ATOM   12909 H HB1  . ALA D 1 16  ? 5.629   43.164  38.344  1.00 93.38  ? 16  ALA D HB1  1 
ATOM   12910 H HB2  . ALA D 1 16  ? 5.200   41.866  39.152  1.00 93.38  ? 16  ALA D HB2  1 
ATOM   12911 H HB3  . ALA D 1 16  ? 6.738   42.171  38.898  1.00 93.38  ? 16  ALA D HB3  1 
ATOM   12912 N N    . GLY D 1 17  ? 7.274   41.249  35.293  1.00 79.51  ? 17  GLY D N    1 
ATOM   12913 C CA   . GLY D 1 17  ? 8.186   41.737  34.279  1.00 81.02  ? 17  GLY D CA   1 
ATOM   12914 C C    . GLY D 1 17  ? 9.654   41.639  34.627  1.00 81.60  ? 17  GLY D C    1 
ATOM   12915 O O    . GLY D 1 17  ? 10.497  41.957  33.780  1.00 81.32  ? 17  GLY D O    1 
ATOM   12916 H H    . GLY D 1 17  ? 7.132   40.402  35.258  1.00 95.41  ? 17  GLY D H    1 
ATOM   12917 H HA2  . GLY D 1 17  ? 8.043   41.228  33.465  1.00 97.22  ? 17  GLY D HA2  1 
ATOM   12918 H HA3  . GLY D 1 17  ? 7.986   42.670  34.108  1.00 97.22  ? 17  GLY D HA3  1 
ATOM   12919 N N    . ASN D 1 18  ? 9.987   41.221  35.847  1.00 83.75  ? 18  ASN D N    1 
ATOM   12920 C CA   . ASN D 1 18  ? 11.376  41.015  36.262  1.00 83.00  ? 18  ASN D CA   1 
ATOM   12921 C C    . ASN D 1 18  ? 11.800  39.592  35.891  1.00 82.34  ? 18  ASN D C    1 
ATOM   12922 O O    . ASN D 1 18  ? 11.957  38.705  36.733  1.00 79.99  ? 18  ASN D O    1 
ATOM   12923 C CB   . ASN D 1 18  ? 11.520  41.267  37.758  1.00 79.14  ? 18  ASN D CB   1 
ATOM   12924 C CG   . ASN D 1 18  ? 12.956  41.572  38.183  1.00 81.21  ? 18  ASN D CG   1 
ATOM   12925 O OD1  . ASN D 1 18  ? 13.185  42.105  39.269  1.00 86.08  ? 18  ASN D OD1  1 
ATOM   12926 N ND2  . ASN D 1 18  ? 13.918  41.229  37.338  1.00 81.84  ? 18  ASN D ND2  1 
ATOM   12927 H H    . ASN D 1 18  ? 9.416   41.047  36.467  1.00 100.50 ? 18  ASN D H    1 
ATOM   12928 H HA   . ASN D 1 18  ? 11.947  41.641  35.791  1.00 99.60  ? 18  ASN D HA   1 
ATOM   12929 H HB2  . ASN D 1 18  ? 10.969  42.026  38.004  1.00 94.97  ? 18  ASN D HB2  1 
ATOM   12930 H HB3  . ASN D 1 18  ? 11.230  40.476  38.240  1.00 94.97  ? 18  ASN D HB3  1 
ATOM   12931 H HD21 . ASN D 1 18  ? 14.740  41.383  37.537  1.00 98.21  ? 18  ASN D HD21 1 
ATOM   12932 H HD22 . ASN D 1 18  ? 13.720  40.853  36.590  1.00 98.21  ? 18  ASN D HD22 1 
ATOM   12933 N N    . ILE D 1 19  ? 11.997  39.390  34.592  1.00 81.84  ? 19  ILE D N    1 
ATOM   12934 C CA   . ILE D 1 19  ? 12.238  38.066  34.027  1.00 77.67  ? 19  ILE D CA   1 
ATOM   12935 C C    . ILE D 1 19  ? 13.374  37.375  34.778  1.00 77.07  ? 19  ILE D C    1 
ATOM   12936 O O    . ILE D 1 19  ? 14.489  37.906  34.869  1.00 78.86  ? 19  ILE D O    1 
ATOM   12937 C CB   . ILE D 1 19  ? 12.547  38.139  32.521  1.00 79.73  ? 19  ILE D CB   1 
ATOM   12938 C CG1  . ILE D 1 19  ? 11.455  38.929  31.789  1.00 80.30  ? 19  ILE D CG1  1 
ATOM   12939 C CG2  . ILE D 1 19  ? 12.684  36.738  31.928  1.00 74.23  ? 19  ILE D CG2  1 
ATOM   12940 C CD1  . ILE D 1 19  ? 10.044  38.681  32.292  1.00 80.23  ? 19  ILE D CD1  1 
ATOM   12941 H H    . ILE D 1 19  ? 11.995  40.017  34.004  1.00 98.21  ? 19  ILE D H    1 
ATOM   12942 H HA   . ILE D 1 19  ? 11.433  37.539  34.148  1.00 93.21  ? 19  ILE D HA   1 
ATOM   12943 H HB   . ILE D 1 19  ? 13.392  38.601  32.408  1.00 95.68  ? 19  ILE D HB   1 
ATOM   12944 H HG12 . ILE D 1 19  ? 11.639  39.876  31.892  1.00 96.36  ? 19  ILE D HG12 1 
ATOM   12945 H HG13 . ILE D 1 19  ? 11.477  38.687  30.850  1.00 96.36  ? 19  ILE D HG13 1 
ATOM   12946 H HG21 . ILE D 1 19  ? 12.787  36.810  30.966  1.00 89.07  ? 19  ILE D HG21 1 
ATOM   12947 H HG22 . ILE D 1 19  ? 13.463  36.307  32.313  1.00 89.07  ? 19  ILE D HG22 1 
ATOM   12948 H HG23 . ILE D 1 19  ? 11.886  36.227  32.138  1.00 89.07  ? 19  ILE D HG23 1 
ATOM   12949 H HD11 . ILE D 1 19  ? 9.413   39.075  31.670  1.00 96.27  ? 19  ILE D HD11 1 
ATOM   12950 H HD12 . ILE D 1 19  ? 9.895   37.725  32.354  1.00 96.27  ? 19  ILE D HD12 1 
ATOM   12951 H HD13 . ILE D 1 19  ? 9.945   39.088  33.167  1.00 96.27  ? 19  ILE D HD13 1 
ATOM   12952 N N    . THR D 1 20  ? 13.096  36.191  35.324  1.00 76.68  ? 20  THR D N    1 
ATOM   12953 C CA   . THR D 1 20  ? 14.058  35.433  36.111  1.00 75.91  ? 20  THR D CA   1 
ATOM   12954 C C    . THR D 1 20  ? 13.995  33.971  35.696  1.00 74.01  ? 20  THR D C    1 
ATOM   12955 O O    . THR D 1 20  ? 12.937  33.463  35.314  1.00 74.92  ? 20  THR D O    1 
ATOM   12956 C CB   . THR D 1 20  ? 13.785  35.562  37.615  1.00 79.38  ? 20  THR D CB   1 
ATOM   12957 O OG1  . THR D 1 20  ? 14.525  34.568  38.337  1.00 80.21  ? 20  THR D OG1  1 
ATOM   12958 C CG2  . THR D 1 20  ? 12.300  35.381  37.907  1.00 81.41  ? 20  THR D CG2  1 
ATOM   12959 H H    . THR D 1 20  ? 12.335  35.799  35.250  1.00 92.02  ? 20  THR D H    1 
ATOM   12960 H HA   . THR D 1 20  ? 14.954  35.762  35.937  1.00 91.10  ? 20  THR D HA   1 
ATOM   12961 H HB   . THR D 1 20  ? 14.057  36.444  37.911  1.00 95.25  ? 20  THR D HB   1 
ATOM   12962 H HG1  . THR D 1 20  ? 14.365  34.631  39.159  1.00 96.26  ? 20  THR D HG1  1 
ATOM   12963 H HG21 . THR D 1 20  ? 12.144  35.410  38.864  1.00 97.69  ? 20  THR D HG21 1 
ATOM   12964 H HG22 . THR D 1 20  ? 11.789  36.088  37.483  1.00 97.69  ? 20  THR D HG22 1 
ATOM   12965 H HG23 . THR D 1 20  ? 11.996  34.525  37.566  1.00 97.69  ? 20  THR D HG23 1 
ATOM   12966 N N    . ILE D 1 21  ? 15.143  33.301  35.762  1.00 73.35  ? 21  ILE D N    1 
ATOM   12967 C CA   . ILE D 1 21  ? 15.256  31.888  35.423  1.00 75.86  ? 21  ILE D CA   1 
ATOM   12968 C C    . ILE D 1 21  ? 15.771  31.148  36.648  1.00 74.60  ? 21  ILE D C    1 
ATOM   12969 O O    . ILE D 1 21  ? 16.785  31.538  37.238  1.00 75.81  ? 21  ILE D O    1 
ATOM   12970 C CB   . ILE D 1 21  ? 16.187  31.657  34.222  1.00 76.42  ? 21  ILE D CB   1 
ATOM   12971 C CG1  . ILE D 1 21  ? 15.418  31.840  32.916  1.00 76.30  ? 21  ILE D CG1  1 
ATOM   12972 C CG2  . ILE D 1 21  ? 16.794  30.256  34.256  1.00 74.26  ? 21  ILE D CG2  1 
ATOM   12973 C CD1  . ILE D 1 21  ? 16.263  32.344  31.784  1.00 79.49  ? 21  ILE D CD1  1 
ATOM   12974 H H    . ILE D 1 21  ? 15.887  33.655  36.007  1.00 88.01  ? 21  ILE D H    1 
ATOM   12975 H HA   . ILE D 1 21  ? 14.378  31.545  35.196  1.00 91.03  ? 21  ILE D HA   1 
ATOM   12976 H HB   . ILE D 1 21  ? 16.903  32.310  34.276  1.00 91.71  ? 21  ILE D HB   1 
ATOM   12977 H HG12 . ILE D 1 21  ? 15.046  30.985  32.650  1.00 91.56  ? 21  ILE D HG12 1 
ATOM   12978 H HG13 . ILE D 1 21  ? 14.704  32.481  33.061  1.00 91.56  ? 21  ILE D HG13 1 
ATOM   12979 H HG21 . ILE D 1 21  ? 17.168  30.052  33.385  1.00 89.11  ? 21  ILE D HG21 1 
ATOM   12980 H HG22 . ILE D 1 21  ? 17.491  30.230  34.930  1.00 89.11  ? 21  ILE D HG22 1 
ATOM   12981 H HG23 . ILE D 1 21  ? 16.098  29.616  34.475  1.00 89.11  ? 21  ILE D HG23 1 
ATOM   12982 H HD11 . ILE D 1 21  ? 15.696  32.812  31.151  1.00 95.38  ? 21  ILE D HD11 1 
ATOM   12983 H HD12 . ILE D 1 21  ? 16.935  32.948  32.137  1.00 95.38  ? 21  ILE D HD12 1 
ATOM   12984 H HD13 . ILE D 1 21  ? 16.691  31.590  31.350  1.00 95.38  ? 21  ILE D HD13 1 
ATOM   12985 N N    . LEU D 1 22  ? 15.078  30.084  37.026  1.00 75.18  ? 22  LEU D N    1 
ATOM   12986 C CA   . LEU D 1 22  ? 15.456  29.265  38.163  1.00 73.66  ? 22  LEU D CA   1 
ATOM   12987 C C    . LEU D 1 22  ? 16.023  27.946  37.662  1.00 73.94  ? 22  LEU D C    1 
ATOM   12988 O O    . LEU D 1 22  ? 15.387  27.252  36.858  1.00 72.05  ? 22  LEU D O    1 
ATOM   12989 C CB   . LEU D 1 22  ? 14.250  29.022  39.076  1.00 74.09  ? 22  LEU D CB   1 
ATOM   12990 C CG   . LEU D 1 22  ? 13.620  30.281  39.678  1.00 73.61  ? 22  LEU D CG   1 
ATOM   12991 C CD1  . LEU D 1 22  ? 12.324  29.948  40.406  1.00 73.70  ? 22  LEU D CD1  1 
ATOM   12992 C CD2  . LEU D 1 22  ? 14.594  30.982  40.619  1.00 75.02  ? 22  LEU D CD2  1 
ATOM   12993 H H    . LEU D 1 22  ? 14.366  29.811  36.628  1.00 90.21  ? 22  LEU D H    1 
ATOM   12994 H HA   . LEU D 1 22  ? 16.144  29.711  38.681  1.00 88.40  ? 22  LEU D HA   1 
ATOM   12995 H HB2  . LEU D 1 22  ? 13.562  28.573  38.560  1.00 88.90  ? 22  LEU D HB2  1 
ATOM   12996 H HB3  . LEU D 1 22  ? 14.533  28.459  39.813  1.00 88.90  ? 22  LEU D HB3  1 
ATOM   12997 H HG   . LEU D 1 22  ? 13.409  30.893  38.956  1.00 88.34  ? 22  LEU D HG   1 
ATOM   12998 H HD11 . LEU D 1 22  ? 11.850  30.771  40.601  1.00 88.43  ? 22  LEU D HD11 1 
ATOM   12999 H HD12 . LEU D 1 22  ? 11.780  29.380  39.838  1.00 88.43  ? 22  LEU D HD12 1 
ATOM   13000 H HD13 . LEU D 1 22  ? 12.536  29.484  41.231  1.00 88.43  ? 22  LEU D HD13 1 
ATOM   13001 H HD21 . LEU D 1 22  ? 14.136  31.714  41.061  1.00 90.02  ? 22  LEU D HD21 1 
ATOM   13002 H HD22 . LEU D 1 22  ? 14.910  30.344  41.278  1.00 90.02  ? 22  LEU D HD22 1 
ATOM   13003 H HD23 . LEU D 1 22  ? 15.342  31.322  40.104  1.00 90.02  ? 22  LEU D HD23 1 
ATOM   13004 N N    . ILE D 1 23  ? 17.234  27.628  38.104  1.00 74.39  ? 23  ILE D N    1 
ATOM   13005 C CA   . ILE D 1 23  ? 17.858  26.342  37.814  1.00 75.01  ? 23  ILE D CA   1 
ATOM   13006 C C    . ILE D 1 23  ? 17.546  25.391  38.961  1.00 73.11  ? 23  ILE D C    1 
ATOM   13007 O O    . ILE D 1 23  ? 17.559  25.788  40.134  1.00 76.69  ? 23  ILE D O    1 
ATOM   13008 C CB   . ILE D 1 23  ? 19.376  26.498  37.614  1.00 76.96  ? 23  ILE D CB   1 
ATOM   13009 C CG1  . ILE D 1 23  ? 19.675  27.452  36.454  1.00 75.84  ? 23  ILE D CG1  1 
ATOM   13010 C CG2  . ILE D 1 23  ? 20.020  25.136  37.372  1.00 78.02  ? 23  ILE D CG2  1 
ATOM   13011 C CD1  . ILE D 1 23  ? 18.719  27.346  35.279  1.00 75.46  ? 23  ILE D CD1  1 
ATOM   13012 H H    . ILE D 1 23  ? 17.723  28.149  38.582  1.00 89.26  ? 23  ILE D H    1 
ATOM   13013 H HA   . ILE D 1 23  ? 17.486  25.980  36.994  1.00 90.02  ? 23  ILE D HA   1 
ATOM   13014 H HB   . ILE D 1 23  ? 19.752  26.881  38.422  1.00 92.36  ? 23  ILE D HB   1 
ATOM   13015 H HG12 . ILE D 1 23  ? 19.630  28.362  36.784  1.00 91.00  ? 23  ILE D HG12 1 
ATOM   13016 H HG13 . ILE D 1 23  ? 20.566  27.262  36.122  1.00 91.00  ? 23  ILE D HG13 1 
ATOM   13017 H HG21 . ILE D 1 23  ? 20.939  25.266  37.093  1.00 93.63  ? 23  ILE D HG21 1 
ATOM   13018 H HG22 . ILE D 1 23  ? 19.993  24.624  38.195  1.00 93.63  ? 23  ILE D HG22 1 
ATOM   13019 H HG23 . ILE D 1 23  ? 19.526  24.672  36.678  1.00 93.63  ? 23  ILE D HG23 1 
ATOM   13020 H HD11 . ILE D 1 23  ? 19.101  27.811  34.518  1.00 90.55  ? 23  ILE D HD11 1 
ATOM   13021 H HD12 . ILE D 1 23  ? 18.587  26.410  35.062  1.00 90.55  ? 23  ILE D HD12 1 
ATOM   13022 H HD13 . ILE D 1 23  ? 17.872  27.752  35.523  1.00 90.55  ? 23  ILE D HD13 1 
ATOM   13023 N N    . ASP D 1 24  ? 17.268  24.133  38.630  1.00 73.72  ? 24  ASP D N    1 
ATOM   13024 C CA   . ASP D 1 24  ? 16.880  23.121  39.603  1.00 72.73  ? 24  ASP D CA   1 
ATOM   13025 C C    . ASP D 1 24  ? 17.915  22.004  39.633  1.00 73.09  ? 24  ASP D C    1 
ATOM   13026 O O    . ASP D 1 24  ? 18.579  21.719  38.631  1.00 75.56  ? 24  ASP D O    1 
ATOM   13027 C CB   . ASP D 1 24  ? 15.497  22.535  39.266  1.00 71.23  ? 24  ASP D CB   1 
ATOM   13028 C CG   . ASP D 1 24  ? 14.644  22.295  40.497  1.00 75.91  ? 24  ASP D CG   1 
ATOM   13029 O OD1  . ASP D 1 24  ? 15.101  22.609  41.617  1.00 78.95  ? 24  ASP D OD1  1 
ATOM   13030 O OD2  . ASP D 1 24  ? 13.510  21.792  40.350  1.00 77.18  ? 24  ASP D OD2  1 
ATOM   13031 H H    . ASP D 1 24  ? 17.299  23.834  37.824  1.00 88.47  ? 24  ASP D H    1 
ATOM   13032 H HA   . ASP D 1 24  ? 16.839  23.520  40.486  1.00 87.27  ? 24  ASP D HA   1 
ATOM   13033 H HB2  . ASP D 1 24  ? 15.024  23.154  38.689  1.00 85.47  ? 24  ASP D HB2  1 
ATOM   13034 H HB3  . ASP D 1 24  ? 15.616  21.685  38.814  1.00 85.47  ? 24  ASP D HB3  1 
ATOM   13035 N N    . ASN D 1 25  ? 18.058  21.381  40.802  1.00 73.25  ? 25  ASN D N    1 
ATOM   13036 C CA   . ASN D 1 25  ? 18.867  20.171  40.957  1.00 71.07  ? 25  ASN D CA   1 
ATOM   13037 C C    . ASN D 1 25  ? 20.339  20.413  40.637  1.00 70.91  ? 25  ASN D C    1 
ATOM   13038 O O    . ASN D 1 25  ? 21.045  19.511  40.183  1.00 71.18  ? 25  ASN D O    1 
ATOM   13039 C CB   . ASN D 1 25  ? 18.305  19.041  40.088  1.00 70.44  ? 25  ASN D CB   1 
ATOM   13040 C CG   . ASN D 1 25  ? 16.869  18.699  40.440  1.00 73.33  ? 25  ASN D CG   1 
ATOM   13041 O OD1  . ASN D 1 25  ? 15.977  18.727  39.583  1.00 69.66  ? 25  ASN D OD1  1 
ATOM   13042 N ND2  . ASN D 1 25  ? 16.633  18.388  41.713  1.00 77.05  ? 25  ASN D ND2  1 
ATOM   13043 H H    . ASN D 1 25  ? 17.691  21.644  41.533  1.00 87.89  ? 25  ASN D H    1 
ATOM   13044 H HA   . ASN D 1 25  ? 18.830  19.895  41.886  1.00 85.29  ? 25  ASN D HA   1 
ATOM   13045 H HB2  . ASN D 1 25  ? 18.330  19.314  39.157  1.00 84.53  ? 25  ASN D HB2  1 
ATOM   13046 H HB3  . ASN D 1 25  ? 18.844  18.245  40.215  1.00 84.53  ? 25  ASN D HB3  1 
ATOM   13047 H HD21 . ASN D 1 25  ? 17.277  18.390  42.283  1.00 92.46  ? 25  ASN D HD21 1 
ATOM   13048 H HD22 . ASN D 1 25  ? 15.836  18.186  41.966  1.00 92.46  ? 25  ASN D HD22 1 
ATOM   13049 N N    . PHE D 1 26  ? 20.813  21.627  40.902  1.00 70.96  ? 26  PHE D N    1 
ATOM   13050 C CA   . PHE D 1 26  ? 22.194  22.020  40.664  1.00 75.27  ? 26  PHE D CA   1 
ATOM   13051 C C    . PHE D 1 26  ? 22.861  22.333  41.995  1.00 75.59  ? 26  PHE D C    1 
ATOM   13052 O O    . PHE D 1 26  ? 22.196  22.693  42.969  1.00 80.28  ? 26  PHE D O    1 
ATOM   13053 C CB   . PHE D 1 26  ? 22.254  23.246  39.731  1.00 76.85  ? 26  PHE D CB   1 
ATOM   13054 C CG   . PHE D 1 26  ? 23.574  23.423  39.040  1.00 75.16  ? 26  PHE D CG   1 
ATOM   13055 C CD1  . PHE D 1 26  ? 23.963  22.559  38.034  1.00 77.44  ? 26  PHE D CD1  1 
ATOM   13056 C CD2  . PHE D 1 26  ? 24.422  24.460  39.391  1.00 79.92  ? 26  PHE D CD2  1 
ATOM   13057 C CE1  . PHE D 1 26  ? 25.175  22.719  37.397  1.00 79.34  ? 26  PHE D CE1  1 
ATOM   13058 C CE2  . PHE D 1 26  ? 25.636  24.625  38.754  1.00 81.75  ? 26  PHE D CE2  1 
ATOM   13059 C CZ   . PHE D 1 26  ? 26.012  23.755  37.757  1.00 81.95  ? 26  PHE D CZ   1 
ATOM   13060 H H    . PHE D 1 26  ? 20.335  22.262  41.231  1.00 85.15  ? 26  PHE D H    1 
ATOM   13061 H HA   . PHE D 1 26  ? 22.687  21.298  40.244  1.00 90.32  ? 26  PHE D HA   1 
ATOM   13062 H HB2  . PHE D 1 26  ? 21.573  23.149  39.047  1.00 92.22  ? 26  PHE D HB2  1 
ATOM   13063 H HB3  . PHE D 1 26  ? 22.086  24.044  40.256  1.00 92.22  ? 26  PHE D HB3  1 
ATOM   13064 H HD1  . PHE D 1 26  ? 23.401  21.862  37.784  1.00 92.93  ? 26  PHE D HD1  1 
ATOM   13065 H HD2  . PHE D 1 26  ? 24.171  25.051  40.063  1.00 95.90  ? 26  PHE D HD2  1 
ATOM   13066 H HE1  . PHE D 1 26  ? 25.429  22.128  36.724  1.00 95.21  ? 26  PHE D HE1  1 
ATOM   13067 H HE2  . PHE D 1 26  ? 26.199  25.324  39.000  1.00 98.10  ? 26  PHE D HE2  1 
ATOM   13068 H HZ   . PHE D 1 26  ? 26.829  23.865  37.326  1.00 98.34  ? 26  PHE D HZ   1 
ATOM   13069 N N    . ASP D 1 27  ? 24.181  22.173  42.038  1.00 76.31  ? 27  ASP D N    1 
ATOM   13070 C CA   . ASP D 1 27  ? 24.960  22.532  43.220  1.00 77.57  ? 27  ASP D CA   1 
ATOM   13071 C C    . ASP D 1 27  ? 24.926  24.046  43.386  1.00 82.95  ? 27  ASP D C    1 
ATOM   13072 O O    . ASP D 1 27  ? 25.580  24.775  42.634  1.00 85.75  ? 27  ASP D O    1 
ATOM   13073 C CB   . ASP D 1 27  ? 26.385  22.016  43.071  1.00 77.61  ? 27  ASP D CB   1 
ATOM   13074 C CG   . ASP D 1 27  ? 27.303  22.501  44.175  1.00 82.81  ? 27  ASP D CG   1 
ATOM   13075 O OD1  . ASP D 1 27  ? 26.806  23.034  45.193  1.00 83.81  ? 27  ASP D OD1  1 
ATOM   13076 O OD2  . ASP D 1 27  ? 28.530  22.340  44.020  1.00 84.47  ? 27  ASP D OD2  1 
ATOM   13077 H H    . ASP D 1 27  ? 24.652  21.857  41.392  1.00 91.57  ? 27  ASP D H    1 
ATOM   13078 H HA   . ASP D 1 27  ? 24.575  22.127  44.013  1.00 93.09  ? 27  ASP D HA   1 
ATOM   13079 H HB2  . ASP D 1 27  ? 26.374  21.046  43.095  1.00 93.13  ? 27  ASP D HB2  1 
ATOM   13080 H HB3  . ASP D 1 27  ? 26.746  22.323  42.225  1.00 93.13  ? 27  ASP D HB3  1 
ATOM   13081 N N    . ILE D 1 28  ? 24.156  24.526  44.366  1.00 76.94  ? 28  ILE D N    1 
ATOM   13082 C CA   . ILE D 1 28  ? 23.922  25.957  44.510  1.00 76.73  ? 28  ILE D CA   1 
ATOM   13083 C C    . ILE D 1 28  ? 25.150  26.723  44.973  1.00 83.89  ? 28  ILE D C    1 
ATOM   13084 O O    . ILE D 1 28  ? 25.115  27.961  45.021  1.00 84.05  ? 28  ILE D O    1 
ATOM   13085 C CB   . ILE D 1 28  ? 22.755  26.218  45.490  1.00 81.62  ? 28  ILE D CB   1 
ATOM   13086 C CG1  . ILE D 1 28  ? 23.181  26.012  46.944  1.00 76.32  ? 28  ILE D CG1  1 
ATOM   13087 C CG2  . ILE D 1 28  ? 21.571  25.310  45.149  1.00 78.40  ? 28  ILE D CG2  1 
ATOM   13088 C CD1  . ILE D 1 28  ? 22.238  26.660  47.951  1.00 77.96  ? 28  ILE D CD1  1 
ATOM   13089 H H    . ILE D 1 28  ? 23.760  24.042  44.957  1.00 92.33  ? 28  ILE D H    1 
ATOM   13090 H HA   . ILE D 1 28  ? 23.677  26.301  43.637  1.00 92.07  ? 28  ILE D HA   1 
ATOM   13091 H HB   . ILE D 1 28  ? 22.488  27.145  45.391  1.00 97.94  ? 28  ILE D HB   1 
ATOM   13092 H HG12 . ILE D 1 28  ? 23.207  25.061  47.131  1.00 91.59  ? 28  ILE D HG12 1 
ATOM   13093 H HG13 . ILE D 1 28  ? 24.062  26.399  47.070  1.00 91.59  ? 28  ILE D HG13 1 
ATOM   13094 H HG21 . ILE D 1 28  ? 20.775  25.651  45.586  1.00 94.08  ? 28  ILE D HG21 1 
ATOM   13095 H HG22 . ILE D 1 28  ? 21.444  25.305  44.188  1.00 94.08  ? 28  ILE D HG22 1 
ATOM   13096 H HG23 . ILE D 1 28  ? 21.761  24.412  45.463  1.00 94.08  ? 28  ILE D HG23 1 
ATOM   13097 H HD11 . ILE D 1 28  ? 22.544  26.455  48.848  1.00 93.55  ? 28  ILE D HD11 1 
ATOM   13098 H HD12 . ILE D 1 28  ? 22.239  27.620  47.812  1.00 93.55  ? 28  ILE D HD12 1 
ATOM   13099 H HD13 . ILE D 1 28  ? 21.344  26.308  47.819  1.00 93.55  ? 28  ILE D HD13 1 
ATOM   13100 N N    . TYR D 1 29  ? 26.221  26.026  45.344  1.00 83.08  ? 29  TYR D N    1 
ATOM   13101 C CA   . TYR D 1 29  ? 27.466  26.654  45.771  1.00 82.25  ? 29  TYR D CA   1 
ATOM   13102 C C    . TYR D 1 29  ? 28.595  26.336  44.792  1.00 85.65  ? 29  TYR D C    1 
ATOM   13103 O O    . TYR D 1 29  ? 29.751  26.164  45.181  1.00 85.10  ? 29  TYR D O    1 
ATOM   13104 C CB   . TYR D 1 29  ? 27.836  26.215  47.182  1.00 84.02  ? 29  TYR D CB   1 
ATOM   13105 C CG   . TYR D 1 29  ? 26.863  26.685  48.245  1.00 81.23  ? 29  TYR D CG   1 
ATOM   13106 C CD1  . TYR D 1 29  ? 26.501  28.023  48.338  1.00 81.43  ? 29  TYR D CD1  1 
ATOM   13107 C CD2  . TYR D 1 29  ? 26.306  25.793  49.154  1.00 79.23  ? 29  TYR D CD2  1 
ATOM   13108 C CE1  . TYR D 1 29  ? 25.613  28.459  49.303  1.00 82.33  ? 29  TYR D CE1  1 
ATOM   13109 C CE2  . TYR D 1 29  ? 25.416  26.222  50.123  1.00 77.66  ? 29  TYR D CE2  1 
ATOM   13110 C CZ   . TYR D 1 29  ? 25.075  27.557  50.191  1.00 79.58  ? 29  TYR D CZ   1 
ATOM   13111 O OH   . TYR D 1 29  ? 24.193  28.001  51.152  1.00 81.54  ? 29  TYR D OH   1 
ATOM   13112 H H    . TYR D 1 29  ? 26.249  25.167  45.357  1.00 99.70  ? 29  TYR D H    1 
ATOM   13113 H HA   . TYR D 1 29  ? 27.344  27.616  45.787  1.00 98.71  ? 29  TYR D HA   1 
ATOM   13114 H HB2  . TYR D 1 29  ? 27.859  25.245  47.211  1.00 100.83 ? 29  TYR D HB2  1 
ATOM   13115 H HB3  . TYR D 1 29  ? 28.710  26.574  47.402  1.00 100.83 ? 29  TYR D HB3  1 
ATOM   13116 H HD1  . TYR D 1 29  ? 26.862  28.637  47.740  1.00 97.72  ? 29  TYR D HD1  1 
ATOM   13117 H HD2  . TYR D 1 29  ? 26.535  24.893  49.110  1.00 95.08  ? 29  TYR D HD2  1 
ATOM   13118 H HE1  . TYR D 1 29  ? 25.381  29.358  49.353  1.00 98.79  ? 29  TYR D HE1  1 
ATOM   13119 H HE2  . TYR D 1 29  ? 25.051  25.615  50.725  1.00 93.20  ? 29  TYR D HE2  1 
ATOM   13120 H HH   . TYR D 1 29  ? 23.922  27.354  51.614  1.00 97.84  ? 29  TYR D HH   1 
ATOM   13121 N N    . ASP D 1 30  ? 28.261  26.253  43.506  1.00 87.60  ? 30  ASP D N    1 
ATOM   13122 C CA   . ASP D 1 30  ? 29.251  25.975  42.475  1.00 89.67  ? 30  ASP D CA   1 
ATOM   13123 C C    . ASP D 1 30  ? 30.016  27.249  42.140  1.00 90.75  ? 30  ASP D C    1 
ATOM   13124 O O    . ASP D 1 30  ? 29.417  28.315  41.968  1.00 90.70  ? 30  ASP D O    1 
ATOM   13125 C CB   . ASP D 1 30  ? 28.569  25.412  41.228  1.00 89.60  ? 30  ASP D CB   1 
ATOM   13126 C CG   . ASP D 1 30  ? 29.557  24.876  40.214  1.00 94.59  ? 30  ASP D CG   1 
ATOM   13127 O OD1  . ASP D 1 30  ? 30.331  25.681  39.653  1.00 98.33  ? 30  ASP D OD1  1 
ATOM   13128 O OD2  . ASP D 1 30  ? 29.554  23.649  39.971  1.00 95.77  ? 30  ASP D OD2  1 
ATOM   13129 H H    . ASP D 1 30  ? 27.462  26.355  43.205  1.00 105.12 ? 30  ASP D H    1 
ATOM   13130 H HA   . ASP D 1 30  ? 29.885  25.315  42.794  1.00 107.60 ? 30  ASP D HA   1 
ATOM   13131 H HB2  . ASP D 1 30  ? 27.983  24.685  41.490  1.00 107.52 ? 30  ASP D HB2  1 
ATOM   13132 H HB3  . ASP D 1 30  ? 28.055  26.117  40.804  1.00 107.52 ? 30  ASP D HB3  1 
ATOM   13133 N N    . LYS D 1 31  ? 31.344  27.136  42.058  1.00 92.91  ? 31  LYS D N    1 
ATOM   13134 C CA   . LYS D 1 31  ? 32.167  28.306  41.768  1.00 94.61  ? 31  LYS D CA   1 
ATOM   13135 C C    . LYS D 1 31  ? 31.778  28.952  40.445  1.00 94.64  ? 31  LYS D C    1 
ATOM   13136 O O    . LYS D 1 31  ? 31.858  30.179  40.307  1.00 94.03  ? 31  LYS D O    1 
ATOM   13137 C CB   . LYS D 1 31  ? 33.647  27.911  41.752  1.00 96.00  ? 31  LYS D CB   1 
ATOM   13138 C CG   . LYS D 1 31  ? 34.613  29.075  41.543  1.00 100.68 ? 31  LYS D CG   1 
ATOM   13139 C CD   . LYS D 1 31  ? 34.934  29.299  40.066  1.00 101.31 ? 31  LYS D CD   1 
ATOM   13140 C CE   . LYS D 1 31  ? 36.081  30.291  39.890  1.00 104.83 ? 31  LYS D CE   1 
ATOM   13141 N NZ   . LYS D 1 31  ? 35.599  31.683  39.646  1.00 107.15 ? 31  LYS D NZ   1 
ATOM   13142 H H    . LYS D 1 31  ? 31.785  26.405  42.164  1.00 111.49 ? 31  LYS D H    1 
ATOM   13143 H HA   . LYS D 1 31  ? 32.037  28.962  42.470  1.00 113.53 ? 31  LYS D HA   1 
ATOM   13144 H HB2  . LYS D 1 31  ? 33.866  27.498  42.602  1.00 115.20 ? 31  LYS D HB2  1 
ATOM   13145 H HB3  . LYS D 1 31  ? 33.790  27.279  41.030  1.00 115.20 ? 31  LYS D HB3  1 
ATOM   13146 H HG2  . LYS D 1 31  ? 34.214  29.888  41.892  1.00 120.81 ? 31  LYS D HG2  1 
ATOM   13147 H HG3  . LYS D 1 31  ? 35.444  28.888  42.008  1.00 120.81 ? 31  LYS D HG3  1 
ATOM   13148 H HD2  . LYS D 1 31  ? 35.194  28.456  39.662  1.00 121.57 ? 31  LYS D HD2  1 
ATOM   13149 H HD3  . LYS D 1 31  ? 34.151  29.654  39.617  1.00 121.57 ? 31  LYS D HD3  1 
ATOM   13150 H HE2  . LYS D 1 31  ? 36.622  30.297  40.695  1.00 125.79 ? 31  LYS D HE2  1 
ATOM   13151 H HE3  . LYS D 1 31  ? 36.620  30.022  39.130  1.00 125.79 ? 31  LYS D HE3  1 
ATOM   13152 H HZ1  . LYS D 1 31  ? 36.292  32.232  39.547  1.00 128.59 ? 31  LYS D HZ1  1 
ATOM   13153 H HZ2  . LYS D 1 31  ? 35.103  31.708  38.908  1.00 128.59 ? 31  LYS D HZ2  1 
ATOM   13154 H HZ3  . LYS D 1 31  ? 35.108  31.960  40.335  1.00 128.59 ? 31  LYS D HZ3  1 
ATOM   13155 N N    . ASN D 1 32  ? 31.355  28.152  39.466  1.00 93.68  ? 32  ASN D N    1 
ATOM   13156 C CA   . ASN D 1 32  ? 31.014  28.653  38.141  1.00 92.78  ? 32  ASN D CA   1 
ATOM   13157 C C    . ASN D 1 32  ? 29.613  29.252  38.067  1.00 89.74  ? 32  ASN D C    1 
ATOM   13158 O O    . ASN D 1 32  ? 29.155  29.574  36.968  1.00 88.64  ? 32  ASN D O    1 
ATOM   13159 C CB   . ASN D 1 32  ? 31.142  27.526  37.110  1.00 94.91  ? 32  ASN D CB   1 
ATOM   13160 C CG   . ASN D 1 32  ? 32.491  26.827  37.167  1.00 97.12  ? 32  ASN D CG   1 
ATOM   13161 O OD1  . ASN D 1 32  ? 33.533  27.443  36.938  1.00 96.81  ? 32  ASN D OD1  1 
ATOM   13162 N ND2  . ASN D 1 32  ? 32.475  25.533  37.476  1.00 95.28  ? 32  ASN D ND2  1 
ATOM   13163 H H    . ASN D 1 32  ? 31.257  27.302  39.549  1.00 112.42 ? 32  ASN D H    1 
ATOM   13164 H HA   . ASN D 1 32  ? 31.646  29.352  37.910  1.00 111.34 ? 32  ASN D HA   1 
ATOM   13165 H HB2  . ASN D 1 32  ? 30.453  26.864  37.277  1.00 113.90 ? 32  ASN D HB2  1 
ATOM   13166 H HB3  . ASN D 1 32  ? 31.035  27.898  36.220  1.00 113.90 ? 32  ASN D HB3  1 
ATOM   13167 H HD21 . ASN D 1 32  ? 31.728  25.137  37.630  1.00 114.34 ? 32  ASN D HD21 1 
ATOM   13168 H HD22 . ASN D 1 32  ? 33.213  25.093  37.521  1.00 114.34 ? 32  ASN D HD22 1 
ATOM   13169 N N    . ILE D 1 33  ? 28.928  29.412  39.199  1.00 91.06  ? 33  ILE D N    1 
ATOM   13170 C CA   . ILE D 1 33  ? 27.577  29.972  39.175  1.00 89.16  ? 33  ILE D CA   1 
ATOM   13171 C C    . ILE D 1 33  ? 27.520  31.282  38.397  1.00 87.57  ? 33  ILE D C    1 
ATOM   13172 O O    . ILE D 1 33  ? 26.644  31.422  37.533  1.00 86.23  ? 33  ILE D O    1 
ATOM   13173 C CB   . ILE D 1 33  ? 27.040  30.116  40.611  1.00 86.96  ? 33  ILE D CB   1 
ATOM   13174 C CG1  . ILE D 1 33  ? 26.530  28.766  41.119  1.00 87.53  ? 33  ILE D CG1  1 
ATOM   13175 C CG2  . ILE D 1 33  ? 25.942  31.170  40.669  1.00 86.50  ? 33  ILE D CG2  1 
ATOM   13176 C CD1  . ILE D 1 33  ? 25.166  28.396  40.595  1.00 85.54  ? 33  ILE D CD1  1 
ATOM   13177 H H    . ILE D 1 33  ? 29.218  29.209  39.983  1.00 109.28 ? 33  ILE D H    1 
ATOM   13178 H HA   . ILE D 1 33  ? 27.004  29.336  38.719  1.00 106.99 ? 33  ILE D HA   1 
ATOM   13179 H HB   . ILE D 1 33  ? 27.766  30.406  41.186  1.00 104.35 ? 33  ILE D HB   1 
ATOM   13180 H HG12 . ILE D 1 33  ? 27.151  28.074  40.843  1.00 105.03 ? 33  ILE D HG12 1 
ATOM   13181 H HG13 . ILE D 1 33  ? 26.477  28.797  42.087  1.00 105.03 ? 33  ILE D HG13 1 
ATOM   13182 H HG21 . ILE D 1 33  ? 25.454  31.073  41.502  1.00 103.80 ? 33  ILE D HG21 1 
ATOM   13183 H HG22 . ILE D 1 33  ? 26.347  32.051  40.625  1.00 103.80 ? 33  ILE D HG22 1 
ATOM   13184 H HG23 . ILE D 1 33  ? 25.342  31.044  39.917  1.00 103.80 ? 33  ILE D HG23 1 
ATOM   13185 H HD11 . ILE D 1 33  ? 24.974  27.476  40.836  1.00 102.65 ? 33  ILE D HD11 1 
ATOM   13186 H HD12 . ILE D 1 33  ? 24.505  28.986  40.991  1.00 102.65 ? 33  ILE D HD12 1 
ATOM   13187 H HD13 . ILE D 1 33  ? 25.161  28.494  39.630  1.00 102.65 ? 33  ILE D HD13 1 
ATOM   13188 N N    . PRO D 1 34  ? 28.393  32.264  38.642  1.00 87.67  ? 34  PRO D N    1 
ATOM   13189 C CA   . PRO D 1 34  ? 28.258  33.544  37.920  1.00 88.14  ? 34  PRO D CA   1 
ATOM   13190 C C    . PRO D 1 34  ? 28.431  33.413  36.416  1.00 88.39  ? 34  PRO D C    1 
ATOM   13191 O O    . PRO D 1 34  ? 27.702  34.059  35.653  1.00 87.11  ? 34  PRO D O    1 
ATOM   13192 C CB   . PRO D 1 34  ? 29.359  34.420  38.544  1.00 89.34  ? 34  PRO D CB   1 
ATOM   13193 C CG   . PRO D 1 34  ? 29.701  33.757  39.854  1.00 88.24  ? 34  PRO D CG   1 
ATOM   13194 C CD   . PRO D 1 34  ? 29.494  32.287  39.623  1.00 89.93  ? 34  PRO D CD   1 
ATOM   13195 H HA   . PRO D 1 34  ? 27.390  33.931  38.111  1.00 105.76 ? 34  PRO D HA   1 
ATOM   13196 H HB2  . PRO D 1 34  ? 30.131  34.445  37.957  1.00 107.21 ? 34  PRO D HB2  1 
ATOM   13197 H HB3  . PRO D 1 34  ? 29.022  35.318  38.688  1.00 107.21 ? 34  PRO D HB3  1 
ATOM   13198 H HG2  . PRO D 1 34  ? 30.625  33.944  40.085  1.00 105.89 ? 34  PRO D HG2  1 
ATOM   13199 H HG3  . PRO D 1 34  ? 29.112  34.084  40.551  1.00 105.89 ? 34  PRO D HG3  1 
ATOM   13200 H HD2  . PRO D 1 34  ? 30.294  31.877  39.258  1.00 107.91 ? 34  PRO D HD2  1 
ATOM   13201 H HD3  . PRO D 1 34  ? 29.237  31.840  40.445  1.00 107.91 ? 34  PRO D HD3  1 
ATOM   13202 N N    . LYS D 1 35  ? 29.383  32.594  35.962  1.00 88.67  ? 35  LYS D N    1 
ATOM   13203 C CA   . LYS D 1 35  ? 29.595  32.433  34.527  1.00 88.22  ? 35  LYS D CA   1 
ATOM   13204 C C    . LYS D 1 35  ? 28.372  31.809  33.864  1.00 86.22  ? 35  LYS D C    1 
ATOM   13205 O O    . LYS D 1 35  ? 27.898  32.291  32.829  1.00 87.33  ? 35  LYS D O    1 
ATOM   13206 C CB   . LYS D 1 35  ? 30.843  31.588  34.273  1.00 87.24  ? 35  LYS D CB   1 
ATOM   13207 C CG   . LYS D 1 35  ? 31.917  32.284  33.439  1.00 91.95  ? 35  LYS D CG   1 
ATOM   13208 C CD   . LYS D 1 35  ? 32.215  33.693  33.945  1.00 93.97  ? 35  LYS D CD   1 
ATOM   13209 C CE   . LYS D 1 35  ? 33.678  34.061  33.756  1.00 97.47  ? 35  LYS D CE   1 
ATOM   13210 N NZ   . LYS D 1 35  ? 33.884  35.536  33.808  1.00 105.87 ? 35  LYS D NZ   1 
ATOM   13211 H H    . LYS D 1 35  ? 29.910  32.128  36.458  1.00 106.40 ? 35  LYS D H    1 
ATOM   13212 H HA   . LYS D 1 35  ? 29.742  33.305  34.129  1.00 105.86 ? 35  LYS D HA   1 
ATOM   13213 H HB2  . LYS D 1 35  ? 31.239  31.356  35.128  1.00 104.70 ? 35  LYS D HB2  1 
ATOM   13214 H HB3  . LYS D 1 35  ? 30.580  30.782  33.801  1.00 104.70 ? 35  LYS D HB3  1 
ATOM   13215 H HG2  . LYS D 1 35  ? 32.737  31.768  33.481  1.00 110.34 ? 35  LYS D HG2  1 
ATOM   13216 H HG3  . LYS D 1 35  ? 31.613  32.351  32.520  1.00 110.34 ? 35  LYS D HG3  1 
ATOM   13217 H HD2  . LYS D 1 35  ? 31.676  34.331  33.453  1.00 112.77 ? 35  LYS D HD2  1 
ATOM   13218 H HD3  . LYS D 1 35  ? 32.009  33.744  34.891  1.00 112.77 ? 35  LYS D HD3  1 
ATOM   13219 H HE2  . LYS D 1 35  ? 34.204  33.655  34.463  1.00 116.97 ? 35  LYS D HE2  1 
ATOM   13220 H HE3  . LYS D 1 35  ? 33.980  33.741  32.892  1.00 116.97 ? 35  LYS D HE3  1 
ATOM   13221 H HZ1  . LYS D 1 35  ? 34.746  35.727  33.702  1.00 127.04 ? 35  LYS D HZ1  1 
ATOM   13222 H HZ2  . LYS D 1 35  ? 33.419  35.931  33.159  1.00 127.04 ? 35  LYS D HZ2  1 
ATOM   13223 H HZ3  . LYS D 1 35  ? 33.611  35.855  34.593  1.00 127.04 ? 35  LYS D HZ3  1 
ATOM   13224 N N    . LEU D 1 36  ? 27.851  30.723  34.444  1.00 86.00  ? 36  LEU D N    1 
ATOM   13225 C CA   . LEU D 1 36  ? 26.604  30.158  33.941  1.00 86.04  ? 36  LEU D CA   1 
ATOM   13226 C C    . LEU D 1 36  ? 25.503  31.210  33.932  1.00 86.77  ? 36  LEU D C    1 
ATOM   13227 O O    . LEU D 1 36  ? 24.751  31.329  32.958  1.00 84.45  ? 36  LEU D O    1 
ATOM   13228 C CB   . LEU D 1 36  ? 26.175  28.964  34.792  1.00 85.82  ? 36  LEU D CB   1 
ATOM   13229 C CG   . LEU D 1 36  ? 27.191  27.850  35.025  1.00 86.84  ? 36  LEU D CG   1 
ATOM   13230 C CD1  . LEU D 1 36  ? 26.504  26.639  35.649  1.00 85.59  ? 36  LEU D CD1  1 
ATOM   13231 C CD2  . LEU D 1 36  ? 27.882  27.469  33.733  1.00 88.69  ? 36  LEU D CD2  1 
ATOM   13232 H H    . LEU D 1 36  ? 28.194  30.306  35.113  1.00 103.20 ? 36  LEU D H    1 
ATOM   13233 H HA   . LEU D 1 36  ? 26.749  29.843  33.035  1.00 103.25 ? 36  LEU D HA   1 
ATOM   13234 H HB2  . LEU D 1 36  ? 25.924  29.300  35.666  1.00 102.98 ? 36  LEU D HB2  1 
ATOM   13235 H HB3  . LEU D 1 36  ? 25.408  28.556  34.360  1.00 102.98 ? 36  LEU D HB3  1 
ATOM   13236 H HG   . LEU D 1 36  ? 27.873  28.165  35.639  1.00 104.20 ? 36  LEU D HG   1 
ATOM   13237 H HD11 . LEU D 1 36  ? 27.163  25.941  35.792  1.00 102.70 ? 36  LEU D HD11 1 
ATOM   13238 H HD12 . LEU D 1 36  ? 26.110  26.900  36.496  1.00 102.70 ? 36  LEU D HD12 1 
ATOM   13239 H HD13 . LEU D 1 36  ? 25.813  26.322  35.046  1.00 102.70 ? 36  LEU D HD13 1 
ATOM   13240 H HD21 . LEU D 1 36  ? 28.426  26.680  33.887  1.00 106.43 ? 36  LEU D HD21 1 
ATOM   13241 H HD22 . LEU D 1 36  ? 27.211  27.281  33.059  1.00 106.43 ? 36  LEU D HD22 1 
ATOM   13242 H HD23 . LEU D 1 36  ? 28.443  28.206  33.446  1.00 106.43 ? 36  LEU D HD23 1 
ATOM   13243 N N    . SER D 1 37  ? 25.397  31.986  35.014  1.00 87.22  ? 37  SER D N    1 
ATOM   13244 C CA   . SER D 1 37  ? 24.368  33.016  35.092  1.00 87.22  ? 37  SER D CA   1 
ATOM   13245 C C    . SER D 1 37  ? 24.479  33.987  33.924  1.00 85.36  ? 37  SER D C    1 
ATOM   13246 O O    . SER D 1 37  ? 23.467  34.366  33.322  1.00 82.74  ? 37  SER D O    1 
ATOM   13247 C CB   . SER D 1 37  ? 24.478  33.758  36.422  1.00 87.20  ? 37  SER D CB   1 
ATOM   13248 O OG   . SER D 1 37  ? 24.192  32.894  37.510  1.00 89.78  ? 37  SER D OG   1 
ATOM   13249 H H    . SER D 1 37  ? 25.904  31.935  35.708  1.00 104.66 ? 37  SER D H    1 
ATOM   13250 H HA   . SER D 1 37  ? 23.494  32.597  35.053  1.00 104.66 ? 37  SER D HA   1 
ATOM   13251 H HB2  . SER D 1 37  ? 25.381  34.098  36.519  1.00 104.64 ? 37  SER D HB2  1 
ATOM   13252 H HB3  . SER D 1 37  ? 23.844  34.492  36.427  1.00 104.64 ? 37  SER D HB3  1 
ATOM   13253 H HG   . SER D 1 37  ? 24.735  32.253  37.519  1.00 107.73 ? 37  SER D HG   1 
ATOM   13254 N N    . GLU D 1 38  ? 25.705  34.389  33.582  1.00 85.72  ? 38  GLU D N    1 
ATOM   13255 C CA   . GLU D 1 38  ? 25.895  35.338  32.492  1.00 87.72  ? 38  GLU D CA   1 
ATOM   13256 C C    . GLU D 1 38  ? 25.365  34.783  31.178  1.00 84.44  ? 38  GLU D C    1 
ATOM   13257 O O    . GLU D 1 38  ? 24.552  35.426  30.503  1.00 85.21  ? 38  GLU D O    1 
ATOM   13258 C CB   . GLU D 1 38  ? 27.375  35.692  32.356  1.00 90.41  ? 38  GLU D CB   1 
ATOM   13259 C CG   . GLU D 1 38  ? 27.620  37.133  31.946  1.00 95.25  ? 38  GLU D CG   1 
ATOM   13260 C CD   . GLU D 1 38  ? 29.054  37.392  31.533  1.00 97.55  ? 38  GLU D CD   1 
ATOM   13261 O OE1  . GLU D 1 38  ? 29.961  36.687  32.024  1.00 99.55  ? 38  GLU D OE1  1 
ATOM   13262 O OE2  . GLU D 1 38  ? 29.275  38.309  30.715  1.00 101.85 ? 38  GLU D OE2  1 
ATOM   13263 H H    . GLU D 1 38  ? 26.432  34.130  33.961  1.00 102.86 ? 38  GLU D H    1 
ATOM   13264 H HA   . GLU D 1 38  ? 25.404  36.148  32.701  1.00 105.27 ? 38  GLU D HA   1 
ATOM   13265 H HB2  . GLU D 1 38  ? 27.810  35.548  33.211  1.00 108.49 ? 38  GLU D HB2  1 
ATOM   13266 H HB3  . GLU D 1 38  ? 27.772  35.119  31.681  1.00 108.49 ? 38  GLU D HB3  1 
ATOM   13267 H HG2  . GLU D 1 38  ? 27.048  37.348  31.193  1.00 114.30 ? 38  GLU D HG2  1 
ATOM   13268 H HG3  . GLU D 1 38  ? 27.414  37.713  32.695  1.00 114.30 ? 38  GLU D HG3  1 
ATOM   13269 N N    . GLU D 1 39  ? 25.820  33.587  30.793  1.00 84.53  ? 39  GLU D N    1 
ATOM   13270 C CA   . GLU D 1 39  ? 25.410  33.023  29.511  1.00 88.93  ? 39  GLU D CA   1 
ATOM   13271 C C    . GLU D 1 39  ? 23.900  32.838  29.454  1.00 85.20  ? 39  GLU D C    1 
ATOM   13272 O O    . GLU D 1 39  ? 23.247  33.239  28.483  1.00 87.96  ? 39  GLU D O    1 
ATOM   13273 C CB   . GLU D 1 39  ? 26.125  31.693  29.264  1.00 88.34  ? 39  GLU D CB   1 
ATOM   13274 C CG   . GLU D 1 39  ? 26.906  31.644  27.951  1.00 98.29  ? 39  GLU D CG   1 
ATOM   13275 C CD   . GLU D 1 39  ? 27.623  30.320  27.741  1.00 104.43 ? 39  GLU D CD   1 
ATOM   13276 O OE1  . GLU D 1 39  ? 28.748  30.160  28.266  1.00 100.31 ? 39  GLU D OE1  1 
ATOM   13277 O OE2  . GLU D 1 39  ? 27.068  29.437  27.047  1.00 106.80 ? 39  GLU D OE2  1 
ATOM   13278 H H    . GLU D 1 39  ? 26.358  33.094  31.248  1.00 101.44 ? 39  GLU D H    1 
ATOM   13279 H HA   . GLU D 1 39  ? 25.668  33.636  28.805  1.00 106.72 ? 39  GLU D HA   1 
ATOM   13280 H HB2  . GLU D 1 39  ? 26.752  31.538  29.987  1.00 106.01 ? 39  GLU D HB2  1 
ATOM   13281 H HB3  . GLU D 1 39  ? 25.463  30.984  29.241  1.00 106.01 ? 39  GLU D HB3  1 
ATOM   13282 H HG2  . GLU D 1 39  ? 26.291  31.772  27.212  1.00 117.95 ? 39  GLU D HG2  1 
ATOM   13283 H HG3  . GLU D 1 39  ? 27.573  32.349  27.954  1.00 117.95 ? 39  GLU D HG3  1 
ATOM   13284 N N    . ILE D 1 40  ? 23.324  32.241  30.498  1.00 84.27  ? 40  ILE D N    1 
ATOM   13285 C CA   . ILE D 1 40  ? 21.889  31.983  30.498  1.00 83.87  ? 40  ILE D CA   1 
ATOM   13286 C C    . ILE D 1 40  ? 21.116  33.271  30.275  1.00 84.08  ? 40  ILE D C    1 
ATOM   13287 O O    . ILE D 1 40  ? 20.094  33.274  29.594  1.00 80.85  ? 40  ILE D O    1 
ATOM   13288 C CB   . ILE D 1 40  ? 21.454  31.298  31.808  1.00 84.69  ? 40  ILE D CB   1 
ATOM   13289 C CG1  . ILE D 1 40  ? 22.124  29.930  31.926  1.00 88.14  ? 40  ILE D CG1  1 
ATOM   13290 C CG2  . ILE D 1 40  ? 19.932  31.173  31.862  1.00 85.21  ? 40  ILE D CG2  1 
ATOM   13291 C CD1  . ILE D 1 40  ? 21.653  29.109  33.123  1.00 89.41  ? 40  ILE D CD1  1 
ATOM   13292 H H    . ILE D 1 40  ? 23.736  31.980  31.206  1.00 101.13 ? 40  ILE D H    1 
ATOM   13293 H HA   . ILE D 1 40  ? 21.696  31.378  29.765  1.00 100.64 ? 40  ILE D HA   1 
ATOM   13294 H HB   . ILE D 1 40  ? 21.737  31.843  32.559  1.00 101.63 ? 40  ILE D HB   1 
ATOM   13295 H HG12 . ILE D 1 40  ? 21.932  29.419  31.124  1.00 105.77 ? 40  ILE D HG12 1 
ATOM   13296 H HG13 . ILE D 1 40  ? 23.081  30.059  32.016  1.00 105.77 ? 40  ILE D HG13 1 
ATOM   13297 H HG21 . ILE D 1 40  ? 19.678  30.759  32.702  1.00 102.26 ? 40  ILE D HG21 1 
ATOM   13298 H HG22 . ILE D 1 40  ? 19.540  32.058  31.799  1.00 102.26 ? 40  ILE D HG22 1 
ATOM   13299 H HG23 . ILE D 1 40  ? 19.633  30.625  31.120  1.00 102.26 ? 40  ILE D HG23 1 
ATOM   13300 H HD11 . ILE D 1 40  ? 22.173  28.291  33.170  1.00 107.29 ? 40  ILE D HD11 1 
ATOM   13301 H HD12 . ILE D 1 40  ? 21.780  29.628  33.932  1.00 107.29 ? 40  ILE D HD12 1 
ATOM   13302 H HD13 . ILE D 1 40  ? 20.713  28.897  33.010  1.00 107.29 ? 40  ILE D HD13 1 
ATOM   13303 N N    . MET D 1 41  ? 21.567  34.377  30.873  1.00 85.95  ? 41  MET D N    1 
ATOM   13304 C CA   . MET D 1 41  ? 20.803  35.617  30.800  1.00 82.00  ? 41  MET D CA   1 
ATOM   13305 C C    . MET D 1 41  ? 20.885  36.286  29.436  1.00 83.52  ? 41  MET D C    1 
ATOM   13306 O O    . MET D 1 41  ? 20.006  37.091  29.101  1.00 82.28  ? 41  MET D O    1 
ATOM   13307 C CB   . MET D 1 41  ? 21.293  36.597  31.870  1.00 81.30  ? 41  MET D CB   1 
ATOM   13308 C CG   . MET D 1 41  ? 20.403  36.696  33.086  1.00 83.48  ? 41  MET D CG   1 
ATOM   13309 S SD   . MET D 1 41  ? 21.063  37.794  34.362  1.00 88.58  ? 41  MET D SD   1 
ATOM   13310 C CE   . MET D 1 41  ? 22.802  37.364  34.373  1.00 83.09  ? 41  MET D CE   1 
ATOM   13311 H H    . MET D 1 41  ? 22.300  34.432  31.319  1.00 103.14 ? 41  MET D H    1 
ATOM   13312 H HA   . MET D 1 41  ? 19.874  35.402  30.981  1.00 98.40  ? 41  MET D HA   1 
ATOM   13313 H HB2  . MET D 1 41  ? 22.170  36.310  32.172  1.00 97.56  ? 41  MET D HB2  1 
ATOM   13314 H HB3  . MET D 1 41  ? 21.351  37.481  31.476  1.00 97.56  ? 41  MET D HB3  1 
ATOM   13315 H HG2  . MET D 1 41  ? 19.538  37.041  32.814  1.00 100.17 ? 41  MET D HG2  1 
ATOM   13316 H HG3  . MET D 1 41  ? 20.302  35.813  33.475  1.00 100.17 ? 41  MET D HG3  1 
ATOM   13317 H HE1  . MET D 1 41  ? 23.256  37.906  35.036  1.00 99.70  ? 41  MET D HE1  1 
ATOM   13318 H HE2  . MET D 1 41  ? 22.893  36.424  34.594  1.00 99.70  ? 41  MET D HE2  1 
ATOM   13319 H HE3  . MET D 1 41  ? 23.175  37.535  33.494  1.00 99.70  ? 41  MET D HE3  1 
ATOM   13320 N N    . LYS D 1 42  ? 21.917  35.988  28.649  1.00 84.67  ? 42  LYS D N    1 
ATOM   13321 C CA   . LYS D 1 42  ? 22.117  36.690  27.389  1.00 84.95  ? 42  LYS D CA   1 
ATOM   13322 C C    . LYS D 1 42  ? 20.905  36.527  26.480  1.00 82.73  ? 42  LYS D C    1 
ATOM   13323 O O    . LYS D 1 42  ? 20.179  35.530  26.537  1.00 81.69  ? 42  LYS D O    1 
ATOM   13324 C CB   . LYS D 1 42  ? 23.378  36.176  26.692  1.00 84.33  ? 42  LYS D CB   1 
ATOM   13325 C CG   . LYS D 1 42  ? 24.662  36.774  27.261  1.00 88.22  ? 42  LYS D CG   1 
ATOM   13326 C CD   . LYS D 1 42  ? 25.909  36.264  26.549  1.00 92.27  ? 42  LYS D CD   1 
ATOM   13327 C CE   . LYS D 1 42  ? 26.996  35.878  27.553  1.00 95.34  ? 42  LYS D CE   1 
ATOM   13328 N NZ   . LYS D 1 42  ? 27.932  34.845  27.014  1.00 101.25 ? 42  LYS D NZ   1 
ATOM   13329 H H    . LYS D 1 42  ? 22.509  35.388  28.821  1.00 101.60 ? 42  LYS D H    1 
ATOM   13330 H HA   . LYS D 1 42  ? 22.233  37.637  27.563  1.00 101.94 ? 42  LYS D HA   1 
ATOM   13331 H HB2  . LYS D 1 42  ? 23.425  35.213  26.796  1.00 101.19 ? 42  LYS D HB2  1 
ATOM   13332 H HB3  . LYS D 1 42  ? 23.332  36.407  25.751  1.00 101.19 ? 42  LYS D HB3  1 
ATOM   13333 H HG2  . LYS D 1 42  ? 24.633  37.738  27.163  1.00 105.86 ? 42  LYS D HG2  1 
ATOM   13334 H HG3  . LYS D 1 42  ? 24.733  36.537  28.199  1.00 105.86 ? 42  LYS D HG3  1 
ATOM   13335 H HD2  . LYS D 1 42  ? 25.683  35.480  26.024  1.00 110.73 ? 42  LYS D HD2  1 
ATOM   13336 H HD3  . LYS D 1 42  ? 26.259  36.960  25.971  1.00 110.73 ? 42  LYS D HD3  1 
ATOM   13337 H HE2  . LYS D 1 42  ? 27.514  36.666  27.779  1.00 114.41 ? 42  LYS D HE2  1 
ATOM   13338 H HE3  . LYS D 1 42  ? 26.577  35.517  28.351  1.00 114.41 ? 42  LYS D HE3  1 
ATOM   13339 H HZ1  . LYS D 1 42  ? 28.534  34.627  27.632  1.00 121.49 ? 42  LYS D HZ1  1 
ATOM   13340 H HZ2  . LYS D 1 42  ? 27.479  34.115  26.781  1.00 121.49 ? 42  LYS D HZ2  1 
ATOM   13341 H HZ3  . LYS D 1 42  ? 28.355  35.163  26.298  1.00 121.49 ? 42  LYS D HZ3  1 
ATOM   13342 N N    . GLU D 1 43  ? 20.679  37.547  25.650  1.00 84.86  ? 43  GLU D N    1 
ATOM   13343 C CA   . GLU D 1 43  ? 19.584  37.520  24.686  1.00 86.44  ? 43  GLU D CA   1 
ATOM   13344 C C    . GLU D 1 43  ? 19.775  36.449  23.623  1.00 85.25  ? 43  GLU D C    1 
ATOM   13345 O O    . GLU D 1 43  ? 18.789  36.033  23.005  1.00 85.99  ? 43  GLU D O    1 
ATOM   13346 C CB   . GLU D 1 43  ? 19.442  38.909  24.054  1.00 86.93  ? 43  GLU D CB   1 
ATOM   13347 C CG   . GLU D 1 43  ? 18.268  39.077  23.113  1.00 92.79  ? 43  GLU D CG   1 
ATOM   13348 C CD   . GLU D 1 43  ? 18.637  39.887  21.874  1.00 98.36  ? 43  GLU D CD   1 
ATOM   13349 O OE1  . GLU D 1 43  ? 19.715  40.522  21.881  1.00 99.20  ? 43  GLU D OE1  1 
ATOM   13350 O OE2  . GLU D 1 43  ? 17.856  39.887  20.896  1.00 94.72  ? 43  GLU D OE2  1 
ATOM   13351 H H    . GLU D 1 43  ? 21.148  38.267  25.625  1.00 101.83 ? 43  GLU D H    1 
ATOM   13352 H HA   . GLU D 1 43  ? 18.752  37.313  25.139  1.00 103.73 ? 43  GLU D HA   1 
ATOM   13353 H HB2  . GLU D 1 43  ? 19.337  39.559  24.766  1.00 104.31 ? 43  GLU D HB2  1 
ATOM   13354 H HB3  . GLU D 1 43  ? 20.248  39.098  23.548  1.00 104.31 ? 43  GLU D HB3  1 
ATOM   13355 H HG2  . GLU D 1 43  ? 17.965  38.202  22.823  1.00 111.35 ? 43  GLU D HG2  1 
ATOM   13356 H HG3  . GLU D 1 43  ? 17.553  39.540  23.576  1.00 111.35 ? 43  GLU D HG3  1 
ATOM   13357 N N    . THR D 1 44  ? 21.010  35.991  23.407  1.00 84.86  ? 44  THR D N    1 
ATOM   13358 C CA   . THR D 1 44  ? 21.316  34.907  22.479  1.00 83.58  ? 44  THR D CA   1 
ATOM   13359 C C    . THR D 1 44  ? 21.299  33.533  23.152  1.00 81.46  ? 44  THR D C    1 
ATOM   13360 O O    . THR D 1 44  ? 21.976  32.601  22.702  1.00 80.51  ? 44  THR D O    1 
ATOM   13361 C CB   . THR D 1 44  ? 22.668  35.161  21.821  1.00 81.98  ? 44  THR D CB   1 
ATOM   13362 O OG1  . THR D 1 44  ? 23.636  35.550  22.801  1.00 85.74  ? 44  THR D OG1  1 
ATOM   13363 C CG2  . THR D 1 44  ? 22.547  36.283  20.799  1.00 82.96  ? 44  THR D CG2  1 
ATOM   13364 H H    . THR D 1 44  ? 21.708  36.304  23.800  1.00 101.83 ? 44  THR D H    1 
ATOM   13365 H HA   . THR D 1 44  ? 20.639  34.896  21.784  1.00 100.30 ? 44  THR D HA   1 
ATOM   13366 H HB   . THR D 1 44  ? 22.961  34.347  21.382  1.00 98.37  ? 44  THR D HB   1 
ATOM   13367 H HG1  . THR D 1 44  ? 23.425  36.292  23.135  1.00 102.89 ? 44  THR D HG1  1 
ATOM   13368 H HG21 . THR D 1 44  ? 23.415  36.473  20.410  1.00 99.55  ? 44  THR D HG21 1 
ATOM   13369 H HG22 . THR D 1 44  ? 21.935  36.024  20.092  1.00 99.55  ? 44  THR D HG22 1 
ATOM   13370 H HG23 . THR D 1 44  ? 22.211  37.086  21.227  1.00 99.55  ? 44  THR D HG23 1 
ATOM   13371 N N    . ASN D 1 45  ? 20.523  33.398  24.219  1.00 84.13  ? 45  ASN D N    1 
ATOM   13372 C CA   . ASN D 1 45  ? 20.319  32.177  25.006  1.00 81.04  ? 45  ASN D CA   1 
ATOM   13373 C C    . ASN D 1 45  ? 18.852  32.217  25.433  1.00 77.71  ? 45  ASN D C    1 
ATOM   13374 O O    . ASN D 1 45  ? 18.047  32.944  24.838  1.00 82.56  ? 45  ASN D O    1 
ATOM   13375 C CB   . ASN D 1 45  ? 21.329  32.140  26.166  1.00 81.90  ? 45  ASN D CB   1 
ATOM   13376 C CG   . ASN D 1 45  ? 21.929  30.744  26.382  1.00 85.52  ? 45  ASN D CG   1 
ATOM   13377 O OD1  . ASN D 1 45  ? 21.221  29.808  26.759  1.00 84.58  ? 45  ASN D OD1  1 
ATOM   13378 N ND2  . ASN D 1 45  ? 23.237  30.616  26.188  1.00 88.58  ? 45  ASN D ND2  1 
ATOM   13379 H H    . ASN D 1 45  ? 20.063  34.051  24.538  1.00 100.95 ? 45  ASN D H    1 
ATOM   13380 H HA   . ASN D 1 45  ? 20.470  31.379  24.475  1.00 97.25  ? 45  ASN D HA   1 
ATOM   13381 H HB2  . ASN D 1 45  ? 22.056  32.753  25.974  1.00 98.27  ? 45  ASN D HB2  1 
ATOM   13382 H HB3  . ASN D 1 45  ? 20.881  32.404  26.985  1.00 98.27  ? 45  ASN D HB3  1 
ATOM   13383 H HD21 . ASN D 1 45  ? 23.615  29.852  26.297  1.00 106.30 ? 45  ASN D HD21 1 
ATOM   13384 H HD22 . ASN D 1 45  ? 23.705  31.298  25.953  1.00 106.30 ? 45  ASN D HD22 1 
ATOM   13385 N N    . LEU D 1 46  ? 18.480  31.434  26.440  1.00 82.96  ? 46  LEU D N    1 
ATOM   13386 C CA   . LEU D 1 46  ? 17.260  31.772  27.169  1.00 83.06  ? 46  LEU D CA   1 
ATOM   13387 C C    . LEU D 1 46  ? 17.479  33.174  27.730  1.00 83.74  ? 46  LEU D C    1 
ATOM   13388 O O    . LEU D 1 46  ? 18.557  33.473  28.231  1.00 93.31  ? 46  LEU D O    1 
ATOM   13389 C CB   . LEU D 1 46  ? 16.997  30.749  28.270  1.00 85.13  ? 46  LEU D CB   1 
ATOM   13390 C CG   . LEU D 1 46  ? 15.544  30.360  28.542  1.00 85.89  ? 46  LEU D CG   1 
ATOM   13391 C CD1  . LEU D 1 46  ? 14.968  29.539  27.398  1.00 82.87  ? 46  LEU D CD1  1 
ATOM   13392 C CD2  . LEU D 1 46  ? 15.398  29.586  29.846  1.00 80.82  ? 46  LEU D CD2  1 
ATOM   13393 H H    . LEU D 1 46  ? 18.896  30.731  26.709  1.00 99.56  ? 46  LEU D H    1 
ATOM   13394 H HA   . LEU D 1 46  ? 16.471  31.755  26.606  1.00 99.67  ? 46  LEU D HA   1 
ATOM   13395 H HB2  . LEU D 1 46  ? 17.467  29.933  28.035  1.00 102.16 ? 46  LEU D HB2  1 
ATOM   13396 H HB3  . LEU D 1 46  ? 17.351  31.108  29.099  1.00 102.16 ? 46  LEU D HB3  1 
ATOM   13397 H HG   . LEU D 1 46  ? 15.038  31.184  28.620  1.00 103.06 ? 46  LEU D HG   1 
ATOM   13398 H HD11 . LEU D 1 46  ? 14.154  29.106  27.698  1.00 99.45  ? 46  LEU D HD11 1 
ATOM   13399 H HD12 . LEU D 1 46  ? 14.774  30.128  26.652  1.00 99.45  ? 46  LEU D HD12 1 
ATOM   13400 H HD13 . LEU D 1 46  ? 15.619  28.871  27.130  1.00 99.45  ? 46  LEU D HD13 1 
ATOM   13401 H HD21 . LEU D 1 46  ? 15.494  28.638  29.664  1.00 96.98  ? 46  LEU D HD21 1 
ATOM   13402 H HD22 . LEU D 1 46  ? 16.086  29.876  30.465  1.00 96.98  ? 46  LEU D HD22 1 
ATOM   13403 H HD23 . LEU D 1 46  ? 14.521  29.762  30.221  1.00 96.98  ? 46  LEU D HD23 1 
ATOM   13404 N N    . TYR D 1 47  ? 16.526  34.075  27.557  1.00 81.46  ? 47  TYR D N    1 
ATOM   13405 C CA   . TYR D 1 47  ? 16.725  35.474  27.962  1.00 83.77  ? 47  TYR D CA   1 
ATOM   13406 C C    . TYR D 1 47  ? 16.240  35.688  29.388  1.00 77.78  ? 47  TYR D C    1 
ATOM   13407 O O    . TYR D 1 47  ? 15.293  35.041  29.829  1.00 74.84  ? 47  TYR D O    1 
ATOM   13408 C CB   . TYR D 1 47  ? 15.986  36.363  26.955  1.00 80.06  ? 47  TYR D CB   1 
ATOM   13409 C CG   . TYR D 1 47  ? 16.131  37.863  27.015  1.00 83.84  ? 47  TYR D CG   1 
ATOM   13410 C CD1  . TYR D 1 47  ? 17.193  38.492  27.647  1.00 84.09  ? 47  TYR D CD1  1 
ATOM   13411 C CD2  . TYR D 1 47  ? 15.173  38.658  26.398  1.00 90.01  ? 47  TYR D CD2  1 
ATOM   13412 C CE1  . TYR D 1 47  ? 17.283  39.886  27.671  1.00 86.56  ? 47  TYR D CE1  1 
ATOM   13413 C CE2  . TYR D 1 47  ? 15.250  40.030  26.411  1.00 88.20  ? 47  TYR D CE2  1 
ATOM   13414 C CZ   . TYR D 1 47  ? 16.299  40.645  27.041  1.00 87.93  ? 47  TYR D CZ   1 
ATOM   13415 O OH   . TYR D 1 47  ? 16.348  42.021  27.036  1.00 96.29  ? 47  TYR D OH   1 
ATOM   13416 H HA   . TYR D 1 47  ? 17.662  35.726  27.963  1.00 100.52 ? 47  TYR D HA   1 
ATOM   13417 H HB2  . TYR D 1 47  ? 16.283  36.101  26.069  1.00 96.07  ? 47  TYR D HB2  1 
ATOM   13418 H HB3  . TYR D 1 47  ? 15.038  36.181  27.054  1.00 96.07  ? 47  TYR D HB3  1 
ATOM   13419 H HD1  . TYR D 1 47  ? 17.852  37.981  28.058  1.00 100.90 ? 47  TYR D HD1  1 
ATOM   13420 H HD2  . TYR D 1 47  ? 14.459  38.250  25.963  1.00 108.01 ? 47  TYR D HD2  1 
ATOM   13421 H HE1  . TYR D 1 47  ? 17.992  40.304  28.104  1.00 103.87 ? 47  TYR D HE1  1 
ATOM   13422 H HE2  . TYR D 1 47  ? 14.593  40.538  25.994  1.00 105.84 ? 47  TYR D HE2  1 
ATOM   13423 H HH   . TYR D 1 47  ? 15.667  42.331  26.655  1.00 115.54 ? 47  TYR D HH   1 
ATOM   13424 N N    . ALA D 1 48  ? 16.920  36.573  30.127  1.00 78.41  ? 48  ALA D N    1 
ATOM   13425 C CA   . ALA D 1 48  ? 16.506  36.837  31.507  1.00 80.04  ? 48  ALA D CA   1 
ATOM   13426 C C    . ALA D 1 48  ? 17.210  38.054  32.097  1.00 78.29  ? 48  ALA D C    1 
ATOM   13427 O O    . ALA D 1 48  ? 18.297  38.444  31.664  1.00 81.03  ? 48  ALA D O    1 
ATOM   13428 C CB   . ALA D 1 48  ? 16.768  35.620  32.418  1.00 76.47  ? 48  ALA D CB   1 
ATOM   13429 H H    . ALA D 1 48  ? 17.604  37.019  29.858  1.00 94.09  ? 48  ALA D H    1 
ATOM   13430 H HA   . ALA D 1 48  ? 15.560  37.047  31.472  1.00 96.06  ? 48  ALA D HA   1 
ATOM   13431 H HB1  . ALA D 1 48  ? 17.672  35.301  32.267  1.00 91.76  ? 48  ALA D HB1  1 
ATOM   13432 H HB2  . ALA D 1 48  ? 16.663  35.890  33.344  1.00 91.76  ? 48  ALA D HB2  1 
ATOM   13433 H HB3  . ALA D 1 48  ? 16.131  34.921  32.203  1.00 91.76  ? 48  ALA D HB3  1 
ATOM   13434 N N    . GLU D 1 49  ? 16.572  38.627  33.126  1.00 77.40  ? 49  GLU D N    1 
ATOM   13435 C CA   . GLU D 1 49  ? 17.141  39.721  33.908  1.00 79.76  ? 49  GLU D CA   1 
ATOM   13436 C C    . GLU D 1 49  ? 17.951  39.231  35.103  1.00 78.24  ? 49  GLU D C    1 
ATOM   13437 O O    . GLU D 1 49  ? 18.869  39.929  35.549  1.00 78.47  ? 49  GLU D O    1 
ATOM   13438 C CB   . GLU D 1 49  ? 16.020  40.646  34.389  1.00 79.80  ? 49  GLU D CB   1 
ATOM   13439 C CG   . GLU D 1 49  ? 15.043  41.057  33.290  1.00 81.84  ? 49  GLU D CG   1 
ATOM   13440 C CD   . GLU D 1 49  ? 14.435  42.432  33.523  1.00 85.69  ? 49  GLU D CD   1 
ATOM   13441 O OE1  . GLU D 1 49  ? 14.503  42.934  34.667  1.00 84.50  ? 49  GLU D OE1  1 
ATOM   13442 O OE2  . GLU D 1 49  ? 13.882  43.008  32.563  1.00 91.28  ? 49  GLU D OE2  1 
ATOM   13443 H H    . GLU D 1 49  ? 15.790  38.391  33.395  1.00 92.87  ? 49  GLU D H    1 
ATOM   13444 H HA   . GLU D 1 49  ? 17.736  40.239  33.343  1.00 95.71  ? 49  GLU D HA   1 
ATOM   13445 H HB2  . GLU D 1 49  ? 15.515  40.190  35.079  1.00 95.76  ? 49  GLU D HB2  1 
ATOM   13446 H HB3  . GLU D 1 49  ? 16.417  41.455  34.749  1.00 95.76  ? 49  GLU D HB3  1 
ATOM   13447 H HG2  . GLU D 1 49  ? 15.512  41.077  32.442  1.00 98.20  ? 49  GLU D HG2  1 
ATOM   13448 H HG3  . GLU D 1 49  ? 14.320  40.412  33.255  1.00 98.20  ? 49  GLU D HG3  1 
ATOM   13449 N N    . GLN D 1 50  ? 17.635  38.047  35.626  1.00 77.72  ? 50  GLN D N    1 
ATOM   13450 C CA   . GLN D 1 50  ? 18.350  37.471  36.755  1.00 80.55  ? 50  GLN D CA   1 
ATOM   13451 C C    . GLN D 1 50  ? 18.191  35.958  36.702  1.00 80.10  ? 50  GLN D C    1 
ATOM   13452 O O    . GLN D 1 50  ? 17.386  35.426  35.938  1.00 78.15  ? 50  GLN D O    1 
ATOM   13453 C CB   . GLN D 1 50  ? 17.823  38.013  38.083  1.00 76.80  ? 50  GLN D CB   1 
ATOM   13454 C CG   . GLN D 1 50  ? 16.431  37.494  38.422  1.00 79.72  ? 50  GLN D CG   1 
ATOM   13455 C CD   . GLN D 1 50  ? 15.666  38.411  39.363  1.00 80.35  ? 50  GLN D CD   1 
ATOM   13456 O OE1  . GLN D 1 50  ? 14.496  38.715  39.135  1.00 83.96  ? 50  GLN D OE1  1 
ATOM   13457 N NE2  . GLN D 1 50  ? 16.323  38.847  40.429  1.00 74.49  ? 50  GLN D NE2  1 
ATOM   13458 H H    . GLN D 1 50  ? 16.996  37.550  35.336  1.00 93.26  ? 50  GLN D H    1 
ATOM   13459 H HA   . GLN D 1 50  ? 19.292  37.691  36.684  1.00 96.66  ? 50  GLN D HA   1 
ATOM   13460 H HB2  . GLN D 1 50  ? 18.425  37.744  38.794  1.00 92.16  ? 50  GLN D HB2  1 
ATOM   13461 H HB3  . GLN D 1 50  ? 17.779  38.980  38.033  1.00 92.16  ? 50  GLN D HB3  1 
ATOM   13462 H HG2  . GLN D 1 50  ? 15.918  37.411  37.604  1.00 95.67  ? 50  GLN D HG2  1 
ATOM   13463 H HG3  . GLN D 1 50  ? 16.514  36.628  38.851  1.00 95.67  ? 50  GLN D HG3  1 
ATOM   13464 H HE21 . GLN D 1 50  ? 17.139  38.609  40.558  1.00 89.39  ? 50  GLN D HE21 1 
ATOM   13465 H HE22 . GLN D 1 50  ? 15.933  39.368  40.991  1.00 89.39  ? 50  GLN D HE22 1 
ATOM   13466 N N    . VAL D 1 51  ? 18.954  35.259  37.531  1.00 82.13  ? 51  VAL D N    1 
ATOM   13467 C CA   . VAL D 1 51  ? 18.894  33.798  37.556  1.00 85.96  ? 51  VAL D CA   1 
ATOM   13468 C C    . VAL D 1 51  ? 19.170  33.315  38.973  1.00 86.58  ? 51  VAL D C    1 
ATOM   13469 O O    . VAL D 1 51  ? 20.096  33.790  39.637  1.00 85.95  ? 51  VAL D O    1 
ATOM   13470 C CB   . VAL D 1 51  ? 19.873  33.172  36.538  1.00 85.61  ? 51  VAL D CB   1 
ATOM   13471 C CG1  . VAL D 1 51  ? 21.286  33.682  36.760  1.00 90.73  ? 51  VAL D CG1  1 
ATOM   13472 C CG2  . VAL D 1 51  ? 19.842  31.651  36.614  1.00 81.00  ? 51  VAL D CG2  1 
ATOM   13473 H H    . VAL D 1 51  ? 19.514  35.603  38.086  1.00 98.56  ? 51  VAL D H    1 
ATOM   13474 H HA   . VAL D 1 51  ? 17.997  33.509  37.326  1.00 103.15 ? 51  VAL D HA   1 
ATOM   13475 H HB   . VAL D 1 51  ? 19.593  33.437  35.648  1.00 102.73 ? 51  VAL D HB   1 
ATOM   13476 H HG11 . VAL D 1 51  ? 21.876  33.273  36.107  1.00 108.87 ? 51  VAL D HG11 1 
ATOM   13477 H HG12 . VAL D 1 51  ? 21.294  34.646  36.654  1.00 108.87 ? 51  VAL D HG12 1 
ATOM   13478 H HG13 . VAL D 1 51  ? 21.570  33.445  37.656  1.00 108.87 ? 51  VAL D HG13 1 
ATOM   13479 H HG21 . VAL D 1 51  ? 20.465  31.289  35.964  1.00 97.21  ? 51  VAL D HG21 1 
ATOM   13480 H HG22 . VAL D 1 51  ? 20.097  31.374  37.507  1.00 97.21  ? 51  VAL D HG22 1 
ATOM   13481 H HG23 . VAL D 1 51  ? 18.943  31.344  36.417  1.00 97.21  ? 51  VAL D HG23 1 
ATOM   13482 N N    . GLY D 1 52  ? 18.344  32.374  39.439  1.00 82.18  ? 52  GLY D N    1 
ATOM   13483 C CA   . GLY D 1 52  ? 18.487  31.795  40.753  1.00 77.02  ? 52  GLY D CA   1 
ATOM   13484 C C    . GLY D 1 52  ? 18.628  30.281  40.682  1.00 75.83  ? 52  GLY D C    1 
ATOM   13485 O O    . GLY D 1 52  ? 18.377  29.653  39.647  1.00 79.36  ? 52  GLY D O    1 
ATOM   13486 H H    . GLY D 1 52  ? 17.680  32.056  38.994  1.00 98.62  ? 52  GLY D H    1 
ATOM   13487 H HA2  . GLY D 1 52  ? 19.276  32.159  41.185  1.00 92.43  ? 52  GLY D HA2  1 
ATOM   13488 H HA3  . GLY D 1 52  ? 17.708  32.008  41.290  1.00 92.43  ? 52  GLY D HA3  1 
ATOM   13489 N N    . PHE D 1 53  ? 19.027  29.698  41.813  1.00 76.69  ? 53  PHE D N    1 
ATOM   13490 C CA   . PHE D 1 53  ? 19.311  28.271  41.913  1.00 76.03  ? 53  PHE D CA   1 
ATOM   13491 C C    . PHE D 1 53  ? 18.613  27.703  43.140  1.00 78.10  ? 53  PHE D C    1 
ATOM   13492 O O    . PHE D 1 53  ? 18.730  28.255  44.241  1.00 77.35  ? 53  PHE D O    1 
ATOM   13493 C CB   . PHE D 1 53  ? 20.822  28.028  41.977  1.00 76.58  ? 53  PHE D CB   1 
ATOM   13494 C CG   . PHE D 1 53  ? 21.565  28.550  40.779  1.00 80.13  ? 53  PHE D CG   1 
ATOM   13495 C CD1  . PHE D 1 53  ? 21.890  29.894  40.677  1.00 78.43  ? 53  PHE D CD1  1 
ATOM   13496 C CD2  . PHE D 1 53  ? 21.930  27.696  39.747  1.00 79.38  ? 53  PHE D CD2  1 
ATOM   13497 C CE1  . PHE D 1 53  ? 22.569  30.374  39.571  1.00 81.31  ? 53  PHE D CE1  1 
ATOM   13498 C CE2  . PHE D 1 53  ? 22.606  28.172  38.640  1.00 80.22  ? 53  PHE D CE2  1 
ATOM   13499 C CZ   . PHE D 1 53  ? 22.924  29.513  38.552  1.00 82.35  ? 53  PHE D CZ   1 
ATOM   13500 H H    . PHE D 1 53  ? 19.142  30.121  42.553  1.00 92.03  ? 53  PHE D H    1 
ATOM   13501 H HA   . PHE D 1 53  ? 18.960  27.804  41.138  1.00 91.23  ? 53  PHE D HA   1 
ATOM   13502 H HB2  . PHE D 1 53  ? 21.177  28.472  42.763  1.00 91.90  ? 53  PHE D HB2  1 
ATOM   13503 H HB3  . PHE D 1 53  ? 20.984  27.073  42.034  1.00 91.90  ? 53  PHE D HB3  1 
ATOM   13504 H HD1  . PHE D 1 53  ? 21.648  30.479  41.359  1.00 94.12  ? 53  PHE D HD1  1 
ATOM   13505 H HD2  . PHE D 1 53  ? 21.717  26.793  39.802  1.00 95.25  ? 53  PHE D HD2  1 
ATOM   13506 H HE1  . PHE D 1 53  ? 22.787  31.277  39.515  1.00 97.57  ? 53  PHE D HE1  1 
ATOM   13507 H HE2  . PHE D 1 53  ? 22.845  27.590  37.955  1.00 96.27  ? 53  PHE D HE2  1 
ATOM   13508 H HZ   . PHE D 1 53  ? 23.377  29.835  37.806  1.00 98.82  ? 53  PHE D HZ   1 
ATOM   13509 N N    . ILE D 1 54  ? 17.905  26.587  42.951  1.00 75.97  ? 54  ILE D N    1 
ATOM   13510 C CA   . ILE D 1 54  ? 16.959  26.071  43.936  1.00 77.57  ? 54  ILE D CA   1 
ATOM   13511 C C    . ILE D 1 54  ? 17.566  24.893  44.686  1.00 77.83  ? 54  ILE D C    1 
ATOM   13512 O O    . ILE D 1 54  ? 18.316  24.086  44.119  1.00 78.90  ? 54  ILE D O    1 
ATOM   13513 C CB   . ILE D 1 54  ? 15.639  25.657  43.250  1.00 77.26  ? 54  ILE D CB   1 
ATOM   13514 C CG1  . ILE D 1 54  ? 14.769  26.887  42.972  1.00 79.50  ? 54  ILE D CG1  1 
ATOM   13515 C CG2  . ILE D 1 54  ? 14.874  24.650  44.099  1.00 83.10  ? 54  ILE D CG2  1 
ATOM   13516 C CD1  . ILE D 1 54  ? 13.512  26.584  42.174  1.00 79.25  ? 54  ILE D CD1  1 
ATOM   13517 H H    . ILE D 1 54  ? 17.959  26.102  42.242  1.00 91.17  ? 54  ILE D H    1 
ATOM   13518 H HA   . ILE D 1 54  ? 16.782  26.768  44.586  1.00 93.08  ? 54  ILE D HA   1 
ATOM   13519 H HB   . ILE D 1 54  ? 15.864  25.237  42.405  1.00 92.71  ? 54  ILE D HB   1 
ATOM   13520 H HG12 . ILE D 1 54  ? 14.495  27.272  43.820  1.00 95.39  ? 54  ILE D HG12 1 
ATOM   13521 H HG13 . ILE D 1 54  ? 15.291  27.531  42.469  1.00 95.39  ? 54  ILE D HG13 1 
ATOM   13522 H HG21 . ILE D 1 54  ? 13.972  24.567  43.754  1.00 99.72  ? 54  ILE D HG21 1 
ATOM   13523 H HG22 . ILE D 1 54  ? 15.326  23.792  44.054  1.00 99.72  ? 54  ILE D HG22 1 
ATOM   13524 H HG23 . ILE D 1 54  ? 14.850  24.964  45.016  1.00 99.72  ? 54  ILE D HG23 1 
ATOM   13525 H HD11 . ILE D 1 54  ? 13.187  27.405  41.774  1.00 95.10  ? 54  ILE D HD11 1 
ATOM   13526 H HD12 . ILE D 1 54  ? 13.726  25.940  41.481  1.00 95.10  ? 54  ILE D HD12 1 
ATOM   13527 H HD13 . ILE D 1 54  ? 12.840  26.218  42.770  1.00 95.10  ? 54  ILE D HD13 1 
ATOM   13528 N N    . LYS D 1 55  ? 17.222  24.786  45.969  1.00 76.95  ? 55  LYS D N    1 
ATOM   13529 C CA   . LYS D 1 55  ? 17.577  23.620  46.773  1.00 79.99  ? 55  LYS D CA   1 
ATOM   13530 C C    . LYS D 1 55  ? 16.526  23.528  47.876  1.00 79.10  ? 55  LYS D C    1 
ATOM   13531 O O    . LYS D 1 55  ? 16.566  24.300  48.840  1.00 79.18  ? 55  LYS D O    1 
ATOM   13532 C CB   . LYS D 1 55  ? 18.981  23.740  47.341  1.00 78.31  ? 55  LYS D CB   1 
ATOM   13533 C CG   . LYS D 1 55  ? 19.438  22.512  48.104  1.00 77.80  ? 55  LYS D CG   1 
ATOM   13534 C CD   . LYS D 1 55  ? 20.878  22.667  48.569  1.00 80.12  ? 55  LYS D CD   1 
ATOM   13535 C CE   . LYS D 1 55  ? 21.204  21.706  49.695  1.00 72.58  ? 55  LYS D CE   1 
ATOM   13536 N NZ   . LYS D 1 55  ? 22.436  20.923  49.395  1.00 78.38  ? 55  LYS D NZ   1 
ATOM   13537 H H    . LYS D 1 55  ? 16.777  25.382  46.401  1.00 92.34  ? 55  LYS D H    1 
ATOM   13538 H HA   . LYS D 1 55  ? 17.546  22.818  46.229  1.00 95.99  ? 55  LYS D HA   1 
ATOM   13539 H HB2  . LYS D 1 55  ? 19.602  23.882  46.609  1.00 93.97  ? 55  LYS D HB2  1 
ATOM   13540 H HB3  . LYS D 1 55  ? 19.008  24.494  47.950  1.00 93.97  ? 55  LYS D HB3  1 
ATOM   13541 H HG2  . LYS D 1 55  ? 18.875  22.387  48.884  1.00 93.36  ? 55  LYS D HG2  1 
ATOM   13542 H HG3  . LYS D 1 55  ? 19.383  21.733  47.528  1.00 93.36  ? 55  LYS D HG3  1 
ATOM   13543 H HD2  . LYS D 1 55  ? 21.477  22.483  47.828  1.00 96.14  ? 55  LYS D HD2  1 
ATOM   13544 H HD3  . LYS D 1 55  ? 21.017  23.572  48.890  1.00 96.14  ? 55  LYS D HD3  1 
ATOM   13545 H HE2  . LYS D 1 55  ? 21.351  22.206  50.513  1.00 87.09  ? 55  LYS D HE2  1 
ATOM   13546 H HE3  . LYS D 1 55  ? 20.468  21.086  49.813  1.00 87.09  ? 55  LYS D HE3  1 
ATOM   13547 H HZ1  . LYS D 1 55  ? 23.127  21.473  49.285  1.00 94.06  ? 55  LYS D HZ1  1 
ATOM   13548 H HZ2  . LYS D 1 55  ? 22.614  20.366  50.066  1.00 94.06  ? 55  LYS D HZ2  1 
ATOM   13549 H HZ3  . LYS D 1 55  ? 22.322  20.450  48.650  1.00 94.06  ? 55  LYS D HZ3  1 
ATOM   13550 N N    . ASP D 1 56  ? 15.581  22.604  47.720  1.00 82.27  ? 56  ASP D N    1 
ATOM   13551 C CA   . ASP D 1 56  ? 14.478  22.424  48.671  1.00 83.88  ? 56  ASP D CA   1 
ATOM   13552 C C    . ASP D 1 56  ? 13.703  23.735  48.720  1.00 83.64  ? 56  ASP D C    1 
ATOM   13553 O O    . ASP D 1 56  ? 13.172  24.145  47.672  1.00 85.57  ? 56  ASP D O    1 
ATOM   13554 C CB   . ASP D 1 56  ? 15.046  21.939  49.999  1.00 79.73  ? 56  ASP D CB   1 
ATOM   13555 C CG   . ASP D 1 56  ? 13.972  21.399  50.944  1.00 87.17  ? 56  ASP D CG   1 
ATOM   13556 O OD1  . ASP D 1 56  ? 12.829  21.188  50.477  1.00 92.91  ? 56  ASP D OD1  1 
ATOM   13557 O OD2  . ASP D 1 56  ? 14.269  21.191  52.142  1.00 91.35  ? 56  ASP D OD2  1 
ATOM   13558 H H    . ASP D 1 56  ? 15.554  22.056  47.057  1.00 98.72  ? 56  ASP D H    1 
ATOM   13559 H HA   . ASP D 1 56  ? 13.877  21.741  48.333  1.00 100.65 ? 56  ASP D HA   1 
ATOM   13560 H HB2  . ASP D 1 56  ? 15.681  21.225  49.829  1.00 95.67  ? 56  ASP D HB2  1 
ATOM   13561 H HB3  . ASP D 1 56  ? 15.490  22.679  50.442  1.00 95.67  ? 56  ASP D HB3  1 
ATOM   13562 N N    . SER D 1 57  ? 13.618  24.418  49.862  1.00 82.37  ? 57  SER D N    1 
ATOM   13563 C CA   . SER D 1 57  ? 12.887  25.671  49.974  1.00 79.93  ? 57  SER D CA   1 
ATOM   13564 C C    . SER D 1 57  ? 13.791  26.897  49.903  1.00 74.07  ? 57  SER D C    1 
ATOM   13565 O O    . SER D 1 57  ? 13.326  28.011  50.177  1.00 77.30  ? 57  SER D O    1 
ATOM   13566 C CB   . SER D 1 57  ? 12.099  25.714  51.288  1.00 81.64  ? 57  SER D CB   1 
ATOM   13567 O OG   . SER D 1 57  ? 11.447  24.483  51.553  1.00 81.99  ? 57  SER D OG   1 
ATOM   13568 H H    . SER D 1 57  ? 13.984  24.167  50.598  1.00 98.84  ? 57  SER D H    1 
ATOM   13569 H HA   . SER D 1 57  ? 12.259  25.711  49.235  1.00 95.92  ? 57  SER D HA   1 
ATOM   13570 H HB2  . SER D 1 57  ? 12.713  25.904  52.014  1.00 97.96  ? 57  SER D HB2  1 
ATOM   13571 H HB3  . SER D 1 57  ? 11.430  26.414  51.228  1.00 97.96  ? 57  SER D HB3  1 
ATOM   13572 H HG   . SER D 1 57  ? 11.012  24.537  52.270  1.00 98.39  ? 57  SER D HG   1 
ATOM   13573 N N    . HIS D 1 58  ? 15.065  26.725  49.554  1.00 73.24  ? 58  HIS D N    1 
ATOM   13574 C CA   . HIS D 1 58  ? 16.016  27.827  49.511  1.00 75.27  ? 58  HIS D CA   1 
ATOM   13575 C C    . HIS D 1 58  ? 16.259  28.284  48.078  1.00 75.60  ? 58  HIS D C    1 
ATOM   13576 O O    . HIS D 1 58  ? 16.264  27.480  47.145  1.00 75.34  ? 58  HIS D O    1 
ATOM   13577 C CB   . HIS D 1 58  ? 17.346  27.425  50.157  1.00 71.19  ? 58  HIS D CB   1 
ATOM   13578 C CG   . HIS D 1 58  ? 18.403  28.479  50.058  1.00 77.26  ? 58  HIS D CG   1 
ATOM   13579 N ND1  . HIS D 1 58  ? 18.255  29.734  50.613  1.00 77.15  ? 58  HIS D ND1  1 
ATOM   13580 C CD2  . HIS D 1 58  ? 19.623  28.470  49.467  1.00 77.86  ? 58  HIS D CD2  1 
ATOM   13581 C CE1  . HIS D 1 58  ? 19.337  30.452  50.368  1.00 77.48  ? 58  HIS D CE1  1 
ATOM   13582 N NE2  . HIS D 1 58  ? 20.182  29.708  49.676  1.00 81.32  ? 58  HIS D NE2  1 
ATOM   13583 H H    . HIS D 1 58  ? 15.405  25.966  49.336  1.00 87.88  ? 58  HIS D H    1 
ATOM   13584 H HA   . HIS D 1 58  ? 15.648  28.578  50.003  1.00 90.33  ? 58  HIS D HA   1 
ATOM   13585 H HB2  . HIS D 1 58  ? 17.194  27.244  51.098  1.00 85.43  ? 58  HIS D HB2  1 
ATOM   13586 H HB3  . HIS D 1 58  ? 17.679  26.628  49.715  1.00 85.43  ? 58  HIS D HB3  1 
ATOM   13587 H HD2  . HIS D 1 58  ? 20.008  27.759  49.007  1.00 93.43  ? 58  HIS D HD2  1 
ATOM   13588 H HE1  . HIS D 1 58  ? 19.479  31.331  50.638  1.00 92.98  ? 58  HIS D HE1  1 
ATOM   13589 H HE2  . HIS D 1 58  ? 20.958  29.958  49.401  1.00 97.58  ? 58  HIS D HE2  1 
ATOM   13590 N N    . LEU D 1 59  ? 16.469  29.592  47.916  1.00 77.28  ? 59  LEU D N    1 
ATOM   13591 C CA   . LEU D 1 59  ? 16.725  30.210  46.619  1.00 73.99  ? 59  LEU D CA   1 
ATOM   13592 C C    . LEU D 1 59  ? 18.060  30.939  46.680  1.00 74.56  ? 59  LEU D C    1 
ATOM   13593 O O    . LEU D 1 59  ? 18.208  31.910  47.430  1.00 77.48  ? 59  LEU D O    1 
ATOM   13594 C CB   . LEU D 1 59  ? 15.602  31.178  46.242  1.00 72.31  ? 59  LEU D CB   1 
ATOM   13595 C CG   . LEU D 1 59  ? 15.887  32.166  45.110  1.00 74.42  ? 59  LEU D CG   1 
ATOM   13596 C CD1  . LEU D 1 59  ? 16.362  31.455  43.859  1.00 75.14  ? 59  LEU D CD1  1 
ATOM   13597 C CD2  . LEU D 1 59  ? 14.641  32.989  44.816  1.00 73.16  ? 59  LEU D CD2  1 
ATOM   13598 H H    . LEU D 1 59  ? 16.467  30.156  48.565  1.00 92.74  ? 59  LEU D H    1 
ATOM   13599 H HA   . LEU D 1 59  ? 16.781  29.522  45.938  1.00 88.79  ? 59  LEU D HA   1 
ATOM   13600 H HB2  . LEU D 1 59  ? 14.833  30.652  45.971  1.00 86.76  ? 59  LEU D HB2  1 
ATOM   13601 H HB3  . LEU D 1 59  ? 15.384  31.703  47.028  1.00 86.76  ? 59  LEU D HB3  1 
ATOM   13602 H HG   . LEU D 1 59  ? 16.600  32.762  45.389  1.00 89.31  ? 59  LEU D HG   1 
ATOM   13603 H HD11 . LEU D 1 59  ? 16.378  32.087  43.123  1.00 90.17  ? 59  LEU D HD11 1 
ATOM   13604 H HD12 . LEU D 1 59  ? 17.253  31.104  44.013  1.00 90.17  ? 59  LEU D HD12 1 
ATOM   13605 H HD13 . LEU D 1 59  ? 15.751  30.729  43.657  1.00 90.17  ? 59  LEU D HD13 1 
ATOM   13606 H HD21 . LEU D 1 59  ? 14.838  33.615  44.101  1.00 87.79  ? 59  LEU D HD21 1 
ATOM   13607 H HD22 . LEU D 1 59  ? 13.925  32.393  44.546  1.00 87.79  ? 59  LEU D HD22 1 
ATOM   13608 H HD23 . LEU D 1 59  ? 14.385  33.472  45.617  1.00 87.79  ? 59  LEU D HD23 1 
ATOM   13609 N N    . GLN D 1 60  ? 19.025  30.477  45.891  1.00 78.41  ? 60  GLN D N    1 
ATOM   13610 C CA   . GLN D 1 60  ? 20.364  31.062  45.864  1.00 77.91  ? 60  GLN D CA   1 
ATOM   13611 C C    . GLN D 1 60  ? 20.478  31.944  44.624  1.00 78.66  ? 60  GLN D C    1 
ATOM   13612 O O    . GLN D 1 60  ? 20.685  31.450  43.514  1.00 76.72  ? 60  GLN D O    1 
ATOM   13613 C CB   . GLN D 1 60  ? 21.433  29.974  45.865  1.00 76.31  ? 60  GLN D CB   1 
ATOM   13614 C CG   . GLN D 1 60  ? 22.843  30.504  46.061  1.00 78.93  ? 60  GLN D CG   1 
ATOM   13615 C CD   . GLN D 1 60  ? 23.032  31.134  47.423  1.00 75.60  ? 60  GLN D CD   1 
ATOM   13616 O OE1  . GLN D 1 60  ? 22.569  30.605  48.424  1.00 75.75  ? 60  GLN D OE1  1 
ATOM   13617 N NE2  . GLN D 1 60  ? 23.709  32.273  47.465  1.00 77.95  ? 60  GLN D NE2  1 
ATOM   13618 H H    . GLN D 1 60  ? 18.928  29.814  45.353  1.00 94.09  ? 60  GLN D H    1 
ATOM   13619 H HA   . GLN D 1 60  ? 20.483  31.617  46.650  1.00 93.49  ? 60  GLN D HA   1 
ATOM   13620 H HB2  . GLN D 1 60  ? 21.246  29.354  46.588  1.00 91.57  ? 60  GLN D HB2  1 
ATOM   13621 H HB3  . GLN D 1 60  ? 21.406  29.509  45.014  1.00 91.57  ? 60  GLN D HB3  1 
ATOM   13622 H HG2  . GLN D 1 60  ? 23.473  29.771  45.976  1.00 94.72  ? 60  GLN D HG2  1 
ATOM   13623 H HG3  . GLN D 1 60  ? 23.025  31.178  45.388  1.00 94.72  ? 60  GLN D HG3  1 
ATOM   13624 H HE21 . GLN D 1 60  ? 24.015  32.618  46.739  1.00 93.54  ? 60  GLN D HE21 1 
ATOM   13625 H HE22 . GLN D 1 60  ? 23.841  32.667  48.218  1.00 93.54  ? 60  GLN D HE22 1 
ATOM   13626 N N    . MET D 1 61  ? 20.337  33.250  44.814  1.00 77.33  ? 61  MET D N    1 
ATOM   13627 C CA   . MET D 1 61  ? 20.504  34.176  43.706  1.00 79.55  ? 61  MET D CA   1 
ATOM   13628 C C    . MET D 1 61  ? 21.943  34.129  43.197  1.00 83.38  ? 61  MET D C    1 
ATOM   13629 O O    . MET D 1 61  ? 22.869  33.709  43.901  1.00 81.87  ? 61  MET D O    1 
ATOM   13630 C CB   . MET D 1 61  ? 20.136  35.597  44.126  1.00 81.31  ? 61  MET D CB   1 
ATOM   13631 C CG   . MET D 1 61  ? 18.649  35.800  44.417  1.00 79.13  ? 61  MET D CG   1 
ATOM   13632 S SD   . MET D 1 61  ? 17.535  35.022  43.220  1.00 73.85  ? 61  MET D SD   1 
ATOM   13633 C CE   . MET D 1 61  ? 17.633  36.166  41.842  1.00 75.94  ? 61  MET D CE   1 
ATOM   13634 H H    . MET D 1 61  ? 20.147  33.621  45.566  1.00 92.79  ? 61  MET D H    1 
ATOM   13635 H HA   . MET D 1 61  ? 19.904  33.925  42.986  1.00 95.46  ? 61  MET D HA   1 
ATOM   13636 H HB2  . MET D 1 61  ? 20.626  35.818  44.933  1.00 97.57  ? 61  MET D HB2  1 
ATOM   13637 H HB3  . MET D 1 61  ? 20.381  36.205  43.411  1.00 97.57  ? 61  MET D HB3  1 
ATOM   13638 H HG2  . MET D 1 61  ? 18.450  35.424  45.289  1.00 94.95  ? 61  MET D HG2  1 
ATOM   13639 H HG3  . MET D 1 61  ? 18.461  36.752  44.416  1.00 94.95  ? 61  MET D HG3  1 
ATOM   13640 H HE1  . MET D 1 61  ? 17.049  35.856  41.132  1.00 91.13  ? 61  MET D HE1  1 
ATOM   13641 H HE2  . MET D 1 61  ? 17.352  37.045  42.141  1.00 91.13  ? 61  MET D HE2  1 
ATOM   13642 H HE3  . MET D 1 61  ? 18.549  36.201  41.525  1.00 91.13  ? 61  MET D HE3  1 
ATOM   13643 N N    . MET D 1 62  ? 22.123  34.588  41.952  1.00 84.65  ? 62  MET D N    1 
ATOM   13644 C CA   . MET D 1 62  ? 23.390  34.381  41.261  1.00 85.27  ? 62  MET D CA   1 
ATOM   13645 C C    . MET D 1 62  ? 24.558  35.037  41.986  1.00 84.78  ? 62  MET D C    1 
ATOM   13646 O O    . MET D 1 62  ? 25.700  34.585  41.847  1.00 86.17  ? 62  MET D O    1 
ATOM   13647 C CB   . MET D 1 62  ? 23.296  34.916  39.828  1.00 88.80  ? 62  MET D CB   1 
ATOM   13648 C CG   . MET D 1 62  ? 22.330  36.087  39.643  1.00 90.12  ? 62  MET D CG   1 
ATOM   13649 S SD   . MET D 1 62  ? 22.514  36.972  38.082  1.00 87.13  ? 62  MET D SD   1 
ATOM   13650 C CE   . MET D 1 62  ? 24.257  37.412  38.123  1.00 91.01  ? 62  MET D CE   1 
ATOM   13651 H H    . MET D 1 62  ? 21.533  35.016  41.496  1.00 101.57 ? 62  MET D H    1 
ATOM   13652 H HA   . MET D 1 62  ? 23.556  33.426  41.219  1.00 102.33 ? 62  MET D HA   1 
ATOM   13653 H HB2  . MET D 1 62  ? 24.176  35.217  39.553  1.00 106.56 ? 62  MET D HB2  1 
ATOM   13654 H HB3  . MET D 1 62  ? 22.996  34.197  39.250  1.00 106.56 ? 62  MET D HB3  1 
ATOM   13655 H HG2  . MET D 1 62  ? 21.422  35.748  39.682  1.00 108.15 ? 62  MET D HG2  1 
ATOM   13656 H HG3  . MET D 1 62  ? 22.477  36.725  40.360  1.00 108.15 ? 62  MET D HG3  1 
ATOM   13657 H HE1  . MET D 1 62  ? 24.467  37.941  37.338  1.00 109.21 ? 62  MET D HE1  1 
ATOM   13658 H HE2  . MET D 1 62  ? 24.434  37.926  38.926  1.00 109.21 ? 62  MET D HE2  1 
ATOM   13659 H HE3  . MET D 1 62  ? 24.787  36.600  38.126  1.00 109.21 ? 62  MET D HE3  1 
ATOM   13660 N N    . GLY D 1 63  ? 24.301  36.090  42.758  1.00 84.63  ? 63  GLY D N    1 
ATOM   13661 C CA   . GLY D 1 63  ? 25.374  36.789  43.440  1.00 86.32  ? 63  GLY D CA   1 
ATOM   13662 C C    . GLY D 1 63  ? 25.351  36.659  44.949  1.00 86.36  ? 63  GLY D C    1 
ATOM   13663 O O    . GLY D 1 63  ? 26.309  37.045  45.629  1.00 86.03  ? 63  GLY D O    1 
ATOM   13664 H H    . GLY D 1 63  ? 23.517  36.414  42.900  1.00 101.55 ? 63  GLY D H    1 
ATOM   13665 H HA2  . GLY D 1 63  ? 26.223  36.441  43.125  1.00 103.58 ? 63  GLY D HA2  1 
ATOM   13666 H HA3  . GLY D 1 63  ? 25.319  37.733  43.223  1.00 103.58 ? 63  GLY D HA3  1 
ATOM   13667 N N    . GLY D 1 64  ? 24.255  36.130  45.488  1.00 83.55  ? 64  GLY D N    1 
ATOM   13668 C CA   . GLY D 1 64  ? 24.092  36.032  46.925  1.00 84.08  ? 64  GLY D CA   1 
ATOM   13669 C C    . GLY D 1 64  ? 23.346  37.212  47.510  1.00 81.97  ? 64  GLY D C    1 
ATOM   13670 O O    . GLY D 1 64  ? 23.662  37.675  48.610  1.00 87.84  ? 64  GLY D O    1 
ATOM   13671 H H    . GLY D 1 64  ? 23.592  35.821  45.036  1.00 100.27 ? 64  GLY D H    1 
ATOM   13672 H HA2  . GLY D 1 64  ? 23.598  35.224  47.136  1.00 100.89 ? 64  GLY D HA2  1 
ATOM   13673 H HA3  . GLY D 1 64  ? 24.966  35.986  47.343  1.00 100.89 ? 64  GLY D HA3  1 
ATOM   13674 N N    . GLU D 1 65  ? 22.351  37.707  46.777  1.00 80.18  ? 65  GLU D N    1 
ATOM   13675 C CA   . GLU D 1 65  ? 21.610  38.902  47.145  1.00 79.99  ? 65  GLU D CA   1 
ATOM   13676 C C    . GLU D 1 65  ? 20.119  38.600  47.132  1.00 76.28  ? 65  GLU D C    1 
ATOM   13677 O O    . GLU D 1 65  ? 19.657  37.665  46.477  1.00 78.40  ? 65  GLU D O    1 
ATOM   13678 C CB   . GLU D 1 65  ? 21.926  40.086  46.206  1.00 77.21  ? 65  GLU D CB   1 
ATOM   13679 C CG   . GLU D 1 65  ? 21.644  39.876  44.710  1.00 86.31  ? 65  GLU D CG   1 
ATOM   13680 C CD   . GLU D 1 65  ? 22.363  38.677  44.131  1.00 84.34  ? 65  GLU D CD   1 
ATOM   13681 O OE1  . GLU D 1 65  ? 23.055  37.983  44.896  1.00 88.83  ? 65  GLU D OE1  1 
ATOM   13682 O OE2  . GLU D 1 65  ? 22.225  38.415  42.926  1.00 83.37  ? 65  GLU D OE2  1 
ATOM   13683 H H    . GLU D 1 65  ? 22.082  37.355  46.040  1.00 96.22  ? 65  GLU D H    1 
ATOM   13684 H HA   . GLU D 1 65  ? 21.854  39.166  48.046  1.00 95.98  ? 65  GLU D HA   1 
ATOM   13685 H HB2  . GLU D 1 65  ? 21.394  40.845  46.491  1.00 92.65  ? 65  GLU D HB2  1 
ATOM   13686 H HB3  . GLU D 1 65  ? 22.870  40.291  46.290  1.00 92.65  ? 65  GLU D HB3  1 
ATOM   13687 H HG2  . GLU D 1 65  ? 20.692  39.742  44.585  1.00 103.57 ? 65  GLU D HG2  1 
ATOM   13688 H HG3  . GLU D 1 65  ? 21.935  40.662  44.222  1.00 103.57 ? 65  GLU D HG3  1 
ATOM   13689 N N    . PHE D 1 66  ? 19.365  39.401  47.873  1.00 78.56  ? 66  PHE D N    1 
ATOM   13690 C CA   . PHE D 1 66  ? 17.936  39.170  48.003  1.00 78.56  ? 66  PHE D CA   1 
ATOM   13691 C C    . PHE D 1 66  ? 17.192  39.791  46.831  1.00 74.29  ? 66  PHE D C    1 
ATOM   13692 O O    . PHE D 1 66  ? 17.552  40.866  46.344  1.00 77.25  ? 66  PHE D O    1 
ATOM   13693 C CB   . PHE D 1 66  ? 17.416  39.748  49.321  1.00 78.27  ? 66  PHE D CB   1 
ATOM   13694 C CG   . PHE D 1 66  ? 15.918  39.688  49.462  1.00 76.52  ? 66  PHE D CG   1 
ATOM   13695 C CD1  . PHE D 1 66  ? 15.279  38.493  49.754  1.00 77.17  ? 66  PHE D CD1  1 
ATOM   13696 C CD2  . PHE D 1 66  ? 15.150  40.830  49.295  1.00 73.05  ? 66  PHE D CD2  1 
ATOM   13697 C CE1  . PHE D 1 66  ? 13.901  38.439  49.879  1.00 76.82  ? 66  PHE D CE1  1 
ATOM   13698 C CE2  . PHE D 1 66  ? 13.772  40.781  49.420  1.00 74.17  ? 66  PHE D CE2  1 
ATOM   13699 C CZ   . PHE D 1 66  ? 13.148  39.584  49.712  1.00 75.12  ? 66  PHE D CZ   1 
ATOM   13700 H H    . PHE D 1 66  ? 19.657  40.083  48.308  1.00 94.28  ? 66  PHE D H    1 
ATOM   13701 H HA   . PHE D 1 66  ? 17.761  38.216  48.005  1.00 94.27  ? 66  PHE D HA   1 
ATOM   13702 H HB2  . PHE D 1 66  ? 17.803  39.246  50.056  1.00 93.93  ? 66  PHE D HB2  1 
ATOM   13703 H HB3  . PHE D 1 66  ? 17.682  40.679  49.380  1.00 93.93  ? 66  PHE D HB3  1 
ATOM   13704 H HD1  . PHE D 1 66  ? 15.782  37.719  49.866  1.00 92.60  ? 66  PHE D HD1  1 
ATOM   13705 H HD2  . PHE D 1 66  ? 15.565  41.638  49.097  1.00 87.65  ? 66  PHE D HD2  1 
ATOM   13706 H HE1  . PHE D 1 66  ? 13.483  37.632  50.075  1.00 92.18  ? 66  PHE D HE1  1 
ATOM   13707 H HE2  . PHE D 1 66  ? 13.267  41.554  49.307  1.00 89.01  ? 66  PHE D HE2  1 
ATOM   13708 H HZ   . PHE D 1 66  ? 12.222  39.549  49.797  1.00 90.15  ? 66  PHE D HZ   1 
ATOM   13709 N N    . SER D 1 67  ? 16.155  39.098  46.371  1.00 72.06  ? 67  SER D N    1 
ATOM   13710 C CA   . SER D 1 67  ? 15.266  39.620  45.338  1.00 75.77  ? 67  SER D CA   1 
ATOM   13711 C C    . SER D 1 67  ? 13.844  39.241  45.725  1.00 73.55  ? 67  SER D C    1 
ATOM   13712 O O    . SER D 1 67  ? 13.500  38.055  45.754  1.00 75.75  ? 67  SER D O    1 
ATOM   13713 C CB   . SER D 1 67  ? 15.631  39.072  43.961  1.00 75.90  ? 67  SER D CB   1 
ATOM   13714 O OG   . SER D 1 67  ? 14.630  39.378  43.001  1.00 75.72  ? 67  SER D OG   1 
ATOM   13715 H H    . SER D 1 67  ? 15.943  38.311  46.645  1.00 86.47  ? 67  SER D H    1 
ATOM   13716 H HA   . SER D 1 67  ? 15.332  40.587  45.302  1.00 90.92  ? 67  SER D HA   1 
ATOM   13717 H HB2  . SER D 1 67  ? 16.469  39.469  43.678  1.00 91.08  ? 67  SER D HB2  1 
ATOM   13718 H HB3  . SER D 1 67  ? 15.724  38.108  44.022  1.00 91.08  ? 67  SER D HB3  1 
ATOM   13719 H HG   . SER D 1 67  ? 14.542  40.210  42.933  1.00 90.87  ? 67  SER D HG   1 
ATOM   13720 N N    . GLY D 1 68  ? 13.024  40.242  46.042  1.00 74.10  ? 68  GLY D N    1 
ATOM   13721 C CA   . GLY D 1 68  ? 11.622  39.977  46.301  1.00 75.04  ? 68  GLY D CA   1 
ATOM   13722 C C    . GLY D 1 68  ? 10.888  39.457  45.084  1.00 75.61  ? 68  GLY D C    1 
ATOM   13723 O O    . GLY D 1 68  ? 9.924   38.698  45.214  1.00 74.64  ? 68  GLY D O    1 
ATOM   13724 H H    . GLY D 1 68  ? 13.255  41.068  46.111  1.00 88.92  ? 68  GLY D H    1 
ATOM   13725 H HA2  . GLY D 1 68  ? 11.548  39.316  47.006  1.00 90.04  ? 68  GLY D HA2  1 
ATOM   13726 H HA3  . GLY D 1 68  ? 11.191  40.797  46.589  1.00 90.04  ? 68  GLY D HA3  1 
ATOM   13727 N N    . ASN D 1 69  ? 11.323  39.860  43.887  1.00 75.71  ? 69  ASN D N    1 
ATOM   13728 C CA   . ASN D 1 69  ? 10.709  39.345  42.669  1.00 77.48  ? 69  ASN D CA   1 
ATOM   13729 C C    . ASN D 1 69  ? 11.053  37.874  42.466  1.00 76.36  ? 69  ASN D C    1 
ATOM   13730 O O    . ASN D 1 69  ? 10.162  37.040  42.258  1.00 74.84  ? 69  ASN D O    1 
ATOM   13731 C CB   . ASN D 1 69  ? 11.157  40.173  41.463  1.00 75.72  ? 69  ASN D CB   1 
ATOM   13732 C CG   . ASN D 1 69  ? 10.281  41.394  41.239  1.00 79.88  ? 69  ASN D CG   1 
ATOM   13733 O OD1  . ASN D 1 69  ? 9.053   41.293  41.208  1.00 79.45  ? 69  ASN D OD1  1 
ATOM   13734 N ND2  . ASN D 1 69  ? 10.909  42.559  41.088  1.00 82.42  ? 69  ASN D ND2  1 
ATOM   13735 H H    . ASN D 1 69  ? 11.962  40.420  43.759  1.00 90.85  ? 69  ASN D H    1 
ATOM   13736 H HA   . ASN D 1 69  ? 9.746   39.426  42.747  1.00 92.97  ? 69  ASN D HA   1 
ATOM   13737 H HB2  . ASN D 1 69  ? 12.067  40.477  41.607  1.00 90.87  ? 69  ASN D HB2  1 
ATOM   13738 H HB3  . ASN D 1 69  ? 11.114  39.621  40.666  1.00 90.87  ? 69  ASN D HB3  1 
ATOM   13739 H HD21 . ASN D 1 69  ? 11.768  42.592  41.119  1.00 98.91  ? 69  ASN D HD21 1 
ATOM   13740 H HD22 . ASN D 1 69  ? 10.456  43.278  40.958  1.00 98.91  ? 69  ASN D HD22 1 
ATOM   13741 N N    . ALA D 1 70  ? 12.345  37.533  42.529  1.00 75.90  ? 70  ALA D N    1 
ATOM   13742 C CA   . ALA D 1 70  ? 12.746  36.135  42.392  1.00 73.27  ? 70  ALA D CA   1 
ATOM   13743 C C    . ALA D 1 70  ? 12.065  35.272  43.445  1.00 72.49  ? 70  ALA D C    1 
ATOM   13744 O O    . ALA D 1 70  ? 11.538  34.198  43.139  1.00 75.57  ? 70  ALA D O    1 
ATOM   13745 C CB   . ALA D 1 70  ? 14.266  36.009  42.500  1.00 71.92  ? 70  ALA D CB   1 
ATOM   13746 H H    . ALA D 1 70  ? 12.995  38.083  42.648  1.00 91.08  ? 70  ALA D H    1 
ATOM   13747 H HA   . ALA D 1 70  ? 12.480  35.819  41.514  1.00 87.93  ? 70  ALA D HA   1 
ATOM   13748 H HB1  . ALA D 1 70  ? 14.516  35.082  42.363  1.00 86.30  ? 70  ALA D HB1  1 
ATOM   13749 H HB2  . ALA D 1 70  ? 14.678  36.566  41.822  1.00 86.30  ? 70  ALA D HB2  1 
ATOM   13750 H HB3  . ALA D 1 70  ? 14.545  36.300  43.383  1.00 86.30  ? 70  ALA D HB3  1 
ATOM   13751 N N    . SER D 1 71  ? 12.067  35.729  44.697  1.00 76.53  ? 71  SER D N    1 
ATOM   13752 C CA   . SER D 1 71  ? 11.428  34.966  45.766  1.00 75.00  ? 71  SER D CA   1 
ATOM   13753 C C    . SER D 1 71  ? 9.948   34.745  45.475  1.00 74.35  ? 71  SER D C    1 
ATOM   13754 O O    . SER D 1 71  ? 9.421   33.647  45.694  1.00 72.01  ? 71  SER D O    1 
ATOM   13755 C CB   . SER D 1 71  ? 11.615  35.683  47.100  1.00 75.87  ? 71  SER D CB   1 
ATOM   13756 O OG   . SER D 1 71  ? 12.975  35.653  47.496  1.00 75.42  ? 71  SER D OG   1 
ATOM   13757 H H    . SER D 1 71  ? 12.426  36.468  44.951  1.00 91.84  ? 71  SER D H    1 
ATOM   13758 H HA   . SER D 1 71  ? 11.853  34.096  45.829  1.00 89.99  ? 71  SER D HA   1 
ATOM   13759 H HB2  . SER D 1 71  ? 11.333  36.607  47.005  1.00 91.04  ? 71  SER D HB2  1 
ATOM   13760 H HB3  . SER D 1 71  ? 11.078  35.240  47.776  1.00 91.04  ? 71  SER D HB3  1 
ATOM   13761 H HG   . SER D 1 71  ? 13.452  36.026  46.914  1.00 90.50  ? 71  SER D HG   1 
ATOM   13762 N N    . ARG D 1 72  ? 9.260   35.779  44.979  1.00 76.72  ? 72  ARG D N    1 
ATOM   13763 C CA   . ARG D 1 72  ? 7.865   35.612  44.587  1.00 76.39  ? 72  ARG D CA   1 
ATOM   13764 C C    . ARG D 1 72  ? 7.731   34.638  43.426  1.00 75.39  ? 72  ARG D C    1 
ATOM   13765 O O    . ARG D 1 72  ? 6.739   33.906  43.337  1.00 75.44  ? 72  ARG D O    1 
ATOM   13766 C CB   . ARG D 1 72  ? 7.257   36.963  44.215  1.00 77.76  ? 72  ARG D CB   1 
ATOM   13767 C CG   . ARG D 1 72  ? 6.982   37.881  45.412  1.00 77.51  ? 72  ARG D CG   1 
ATOM   13768 C CD   . ARG D 1 72  ? 6.720   39.315  44.944  1.00 77.45  ? 72  ARG D CD   1 
ATOM   13769 N NE   . ARG D 1 72  ? 5.757   39.360  43.849  1.00 78.33  ? 72  ARG D NE   1 
ATOM   13770 C CZ   . ARG D 1 72  ? 6.040   39.733  42.609  1.00 80.01  ? 72  ARG D CZ   1 
ATOM   13771 N NH1  . ARG D 1 72  ? 7.253   40.135  42.266  1.00 81.03  ? 72  ARG D NH1  1 
ATOM   13772 N NH2  . ARG D 1 72  ? 5.079   39.705  41.689  1.00 80.93  ? 72  ARG D NH2  1 
ATOM   13773 H H    . ARG D 1 72  ? 9.574   36.571  44.863  1.00 92.07  ? 72  ARG D H    1 
ATOM   13774 H HA   . ARG D 1 72  ? 7.367   35.258  45.340  1.00 91.67  ? 72  ARG D HA   1 
ATOM   13775 H HB2  . ARG D 1 72  ? 7.870   37.427  43.624  1.00 93.31  ? 72  ARG D HB2  1 
ATOM   13776 H HB3  . ARG D 1 72  ? 6.412   36.810  43.763  1.00 93.31  ? 72  ARG D HB3  1 
ATOM   13777 H HG2  . ARG D 1 72  ? 6.201   37.565  45.891  1.00 93.02  ? 72  ARG D HG2  1 
ATOM   13778 H HG3  . ARG D 1 72  ? 7.753   37.885  46.001  1.00 93.02  ? 72  ARG D HG3  1 
ATOM   13779 H HD2  . ARG D 1 72  ? 6.364   39.833  45.683  1.00 92.94  ? 72  ARG D HD2  1 
ATOM   13780 H HD3  . ARG D 1 72  ? 7.551   39.707  44.634  1.00 92.94  ? 72  ARG D HD3  1 
ATOM   13781 H HE   . ARG D 1 72  ? 4.947   39.128  44.021  1.00 94.00  ? 72  ARG D HE   1 
ATOM   13782 H HH11 . ARG D 1 72  ? 7.880   40.159  42.853  1.00 97.23  ? 72  ARG D HH11 1 
ATOM   13783 H HH12 . ARG D 1 72  ? 7.414   40.373  41.455  1.00 97.23  ? 72  ARG D HH12 1 
ATOM   13784 H HH21 . ARG D 1 72  ? 4.287   39.447  41.902  1.00 97.12  ? 72  ARG D HH21 1 
ATOM   13785 H HH22 . ARG D 1 72  ? 5.251   39.944  40.881  1.00 97.12  ? 72  ARG D HH22 1 
ATOM   13786 N N    . ALA D 1 73  ? 8.715   34.614  42.526  1.00 76.22  ? 73  ALA D N    1 
ATOM   13787 C CA   . ALA D 1 73  ? 8.683   33.654  41.428  1.00 73.94  ? 73  ALA D CA   1 
ATOM   13788 C C    . ALA D 1 73  ? 8.892   32.234  41.938  1.00 74.20  ? 73  ALA D C    1 
ATOM   13789 O O    . ALA D 1 73  ? 8.206   31.302  41.500  1.00 73.66  ? 73  ALA D O    1 
ATOM   13790 C CB   . ALA D 1 73  ? 9.746   34.018  40.393  1.00 75.23  ? 73  ALA D CB   1 
ATOM   13791 H H    . ALA D 1 73  ? 9.400   35.133  42.530  1.00 91.46  ? 73  ALA D H    1 
ATOM   13792 H HA   . ALA D 1 73  ? 7.816   33.694  40.995  1.00 88.72  ? 73  ALA D HA   1 
ATOM   13793 H HB1  . ALA D 1 73  ? 9.713   33.376  39.667  1.00 90.27  ? 73  ALA D HB1  1 
ATOM   13794 H HB2  . ALA D 1 73  ? 9.566   34.909  40.056  1.00 90.27  ? 73  ALA D HB2  1 
ATOM   13795 H HB3  . ALA D 1 73  ? 10.619  33.994  40.816  1.00 90.27  ? 73  ALA D HB3  1 
ATOM   13796 N N    . PHE D 1 74  ? 9.830   32.052  42.870  1.00 75.00  ? 74  PHE D N    1 
ATOM   13797 C CA   . PHE D 1 74  ? 10.044  30.742  43.475  1.00 76.11  ? 74  PHE D CA   1 
ATOM   13798 C C    . PHE D 1 74  ? 8.780   30.246  44.166  1.00 75.12  ? 74  PHE D C    1 
ATOM   13799 O O    . PHE D 1 74  ? 8.330   29.119  43.924  1.00 77.23  ? 74  PHE D O    1 
ATOM   13800 C CB   . PHE D 1 74  ? 11.214  30.815  44.460  1.00 74.21  ? 74  PHE D CB   1 
ATOM   13801 C CG   . PHE D 1 74  ? 11.568  29.495  45.098  1.00 77.13  ? 74  PHE D CG   1 
ATOM   13802 C CD1  . PHE D 1 74  ? 11.072  28.297  44.603  1.00 76.92  ? 74  PHE D CD1  1 
ATOM   13803 C CD2  . PHE D 1 74  ? 12.406  29.458  46.199  1.00 78.56  ? 74  PHE D CD2  1 
ATOM   13804 C CE1  . PHE D 1 74  ? 11.395  27.092  45.204  1.00 76.46  ? 74  PHE D CE1  1 
ATOM   13805 C CE2  . PHE D 1 74  ? 12.741  28.255  46.797  1.00 77.49  ? 74  PHE D CE2  1 
ATOM   13806 C CZ   . PHE D 1 74  ? 12.233  27.070  46.296  1.00 76.01  ? 74  PHE D CZ   1 
ATOM   13807 H H    . PHE D 1 74  ? 10.353  32.668  43.165  1.00 90.00  ? 74  PHE D H    1 
ATOM   13808 H HA   . PHE D 1 74  ? 10.271  30.103  42.782  1.00 91.33  ? 74  PHE D HA   1 
ATOM   13809 H HB2  . PHE D 1 74  ? 11.999  31.133  43.986  1.00 89.05  ? 74  PHE D HB2  1 
ATOM   13810 H HB3  . PHE D 1 74  ? 10.983  31.433  45.171  1.00 89.05  ? 74  PHE D HB3  1 
ATOM   13811 H HD1  . PHE D 1 74  ? 10.515  28.304  43.858  1.00 92.31  ? 74  PHE D HD1  1 
ATOM   13812 H HD2  . PHE D 1 74  ? 12.749  30.251  46.541  1.00 94.27  ? 74  PHE D HD2  1 
ATOM   13813 H HE1  . PHE D 1 74  ? 11.046  26.297  44.869  1.00 91.75  ? 74  PHE D HE1  1 
ATOM   13814 H HE2  . PHE D 1 74  ? 13.306  28.244  47.535  1.00 92.99  ? 74  PHE D HE2  1 
ATOM   13815 H HZ   . PHE D 1 74  ? 12.458  26.261  46.695  1.00 91.21  ? 74  PHE D HZ   1 
ATOM   13816 N N    . ALA D 1 75  ? 8.193   31.067  45.035  1.00 73.57  ? 75  ALA D N    1 
ATOM   13817 C CA   . ALA D 1 75  ? 6.987   30.641  45.737  1.00 78.08  ? 75  ALA D CA   1 
ATOM   13818 C C    . ALA D 1 75  ? 5.897   30.263  44.740  1.00 76.04  ? 75  ALA D C    1 
ATOM   13819 O O    . ALA D 1 75  ? 5.241   29.224  44.876  1.00 77.77  ? 75  ALA D O    1 
ATOM   13820 C CB   . ALA D 1 75  ? 6.505   31.739  46.686  1.00 75.42  ? 75  ALA D CB   1 
ATOM   13821 H H    . ALA D 1 75  ? 8.468   31.858  45.231  1.00 88.28  ? 75  ALA D H    1 
ATOM   13822 H HA   . ALA D 1 75  ? 7.193   29.862  46.277  1.00 93.69  ? 75  ALA D HA   1 
ATOM   13823 H HB1  . ALA D 1 75  ? 5.704   31.434  47.141  1.00 90.51  ? 75  ALA D HB1  1 
ATOM   13824 H HB2  . ALA D 1 75  ? 7.203   31.925  47.333  1.00 90.51  ? 75  ALA D HB2  1 
ATOM   13825 H HB3  . ALA D 1 75  ? 6.309   32.538  46.171  1.00 90.51  ? 75  ALA D HB3  1 
ATOM   13826 N N    . SER D 1 76  ? 5.702   31.092  43.709  1.00 76.31  ? 76  SER D N    1 
ATOM   13827 C CA   . SER D 1 76  ? 4.714   30.760  42.685  1.00 79.56  ? 76  SER D CA   1 
ATOM   13828 C C    . SER D 1 76  ? 5.012   29.402  42.063  1.00 77.28  ? 76  SER D C    1 
ATOM   13829 O O    . SER D 1 76  ? 4.092   28.637  41.751  1.00 78.84  ? 76  SER D O    1 
ATOM   13830 C CB   . SER D 1 76  ? 4.682   31.845  41.610  1.00 77.08  ? 76  SER D CB   1 
ATOM   13831 O OG   . SER D 1 76  ? 4.063   33.020  42.098  1.00 77.11  ? 76  SER D OG   1 
ATOM   13832 H H    . SER D 1 76  ? 6.118   31.834  43.585  1.00 91.57  ? 76  SER D H    1 
ATOM   13833 H HA   . SER D 1 76  ? 3.837   30.723  43.097  1.00 95.47  ? 76  SER D HA   1 
ATOM   13834 H HB2  . SER D 1 76  ? 5.591   32.054  41.346  1.00 92.49  ? 76  SER D HB2  1 
ATOM   13835 H HB3  . SER D 1 76  ? 4.181   31.518  40.847  1.00 92.49  ? 76  SER D HB3  1 
ATOM   13836 H HG   . SER D 1 76  ? 4.483   33.311  42.765  1.00 92.53  ? 76  SER D HG   1 
ATOM   13837 N N    . LEU D 1 77  ? 6.295   29.085  41.874  1.00 76.02  ? 77  LEU D N    1 
ATOM   13838 C CA   . LEU D 1 77  ? 6.665   27.785  41.319  1.00 76.95  ? 77  LEU D CA   1 
ATOM   13839 C C    . LEU D 1 77  ? 6.293   26.662  42.278  1.00 78.24  ? 77  LEU D C    1 
ATOM   13840 O O    . LEU D 1 77  ? 5.745   25.634  41.863  1.00 76.89  ? 77  LEU D O    1 
ATOM   13841 C CB   . LEU D 1 77  ? 8.161   27.754  41.009  1.00 75.79  ? 77  LEU D CB   1 
ATOM   13842 C CG   . LEU D 1 77  ? 8.707   26.427  40.487  1.00 71.85  ? 77  LEU D CG   1 
ATOM   13843 C CD1  . LEU D 1 77  ? 7.894   25.968  39.292  1.00 72.71  ? 77  LEU D CD1  1 
ATOM   13844 C CD2  . LEU D 1 77  ? 10.183  26.552  40.142  1.00 67.94  ? 77  LEU D CD2  1 
ATOM   13845 H H    . LEU D 1 77  ? 6.961   29.598  42.057  1.00 91.22  ? 77  LEU D H    1 
ATOM   13846 H HA   . LEU D 1 77  ? 6.183   27.649  40.488  1.00 92.34  ? 77  LEU D HA   1 
ATOM   13847 H HB2  . LEU D 1 77  ? 8.345   28.426  40.334  1.00 90.94  ? 77  LEU D HB2  1 
ATOM   13848 H HB3  . LEU D 1 77  ? 8.644   27.962  41.825  1.00 90.94  ? 77  LEU D HB3  1 
ATOM   13849 H HG   . LEU D 1 77  ? 8.631   25.749  41.177  1.00 86.22  ? 77  LEU D HG   1 
ATOM   13850 H HD11 . LEU D 1 77  ? 8.348   25.223  38.869  1.00 87.25  ? 77  LEU D HD11 1 
ATOM   13851 H HD12 . LEU D 1 77  ? 7.016   25.690  39.596  1.00 87.25  ? 77  LEU D HD12 1 
ATOM   13852 H HD13 . LEU D 1 77  ? 7.810   26.703  38.666  1.00 87.25  ? 77  LEU D HD13 1 
ATOM   13853 H HD21 . LEU D 1 77  ? 10.504  25.698  39.811  1.00 81.53  ? 77  LEU D HD21 1 
ATOM   13854 H HD22 . LEU D 1 77  ? 10.291  27.232  39.459  1.00 81.53  ? 77  LEU D HD22 1 
ATOM   13855 H HD23 . LEU D 1 77  ? 10.674  26.803  40.940  1.00 81.53  ? 77  LEU D HD23 1 
ATOM   13856 N N    . LEU D 1 78  ? 6.593   26.836  43.568  1.00 77.85  ? 78  LEU D N    1 
ATOM   13857 C CA   . LEU D 1 78  ? 6.191   25.839  44.554  1.00 76.72  ? 78  LEU D CA   1 
ATOM   13858 C C    . LEU D 1 78  ? 4.690   25.593  44.494  1.00 77.48  ? 78  LEU D C    1 
ATOM   13859 O O    . LEU D 1 78  ? 4.233   24.452  44.631  1.00 79.05  ? 78  LEU D O    1 
ATOM   13860 C CB   . LEU D 1 78  ? 6.601   26.293  45.951  1.00 80.01  ? 78  LEU D CB   1 
ATOM   13861 C CG   . LEU D 1 78  ? 8.099   26.402  46.230  1.00 77.29  ? 78  LEU D CG   1 
ATOM   13862 C CD1  . LEU D 1 78  ? 8.331   27.046  47.592  1.00 78.49  ? 78  LEU D CD1  1 
ATOM   13863 C CD2  . LEU D 1 78  ? 8.756   25.033  46.153  1.00 75.09  ? 78  LEU D CD2  1 
ATOM   13864 H H    . LEU D 1 78  ? 7.019   27.511  43.889  1.00 93.42  ? 78  LEU D H    1 
ATOM   13865 H HA   . LEU D 1 78  ? 6.647   25.004  44.363  1.00 92.06  ? 78  LEU D HA   1 
ATOM   13866 H HB2  . LEU D 1 78  ? 6.219   27.172  46.104  1.00 96.01  ? 78  LEU D HB2  1 
ATOM   13867 H HB3  . LEU D 1 78  ? 6.239   25.658  46.590  1.00 96.01  ? 78  LEU D HB3  1 
ATOM   13868 H HG   . LEU D 1 78  ? 8.514   26.963  45.557  1.00 92.75  ? 78  LEU D HG   1 
ATOM   13869 H HD11 . LEU D 1 78  ? 9.285   27.104  47.756  1.00 94.18  ? 78  LEU D HD11 1 
ATOM   13870 H HD12 . LEU D 1 78  ? 7.941   27.935  47.592  1.00 94.18  ? 78  LEU D HD12 1 
ATOM   13871 H HD13 . LEU D 1 78  ? 7.911   26.501  48.275  1.00 94.18  ? 78  LEU D HD13 1 
ATOM   13872 H HD21 . LEU D 1 78  ? 9.681   25.111  46.435  1.00 90.10  ? 78  LEU D HD21 1 
ATOM   13873 H HD22 . LEU D 1 78  ? 8.282   24.422  46.739  1.00 90.10  ? 78  LEU D HD22 1 
ATOM   13874 H HD23 . LEU D 1 78  ? 8.715   24.714  45.238  1.00 90.10  ? 78  LEU D HD23 1 
ATOM   13875 N N    . ALA D 1 79  ? 3.907   26.656  44.295  1.00 78.69  ? 79  ALA D N    1 
ATOM   13876 C CA   . ALA D 1 79  ? 2.467   26.498  44.152  1.00 80.13  ? 79  ALA D CA   1 
ATOM   13877 C C    . ALA D 1 79  ? 2.126   25.783  42.856  1.00 79.57  ? 79  ALA D C    1 
ATOM   13878 O O    . ALA D 1 79  ? 1.208   24.955  42.818  1.00 81.37  ? 79  ALA D O    1 
ATOM   13879 C CB   . ALA D 1 79  ? 1.784   27.862  44.202  1.00 82.64  ? 79  ALA D CB   1 
ATOM   13880 H H    . ALA D 1 79  ? 4.185   27.468  44.240  1.00 94.42  ? 79  ALA D H    1 
ATOM   13881 H HA   . ALA D 1 79  ? 2.133   25.966  44.892  1.00 96.15  ? 79  ALA D HA   1 
ATOM   13882 H HB1  . ALA D 1 79  ? 0.856   27.760  43.938  1.00 99.16  ? 79  ALA D HB1  1 
ATOM   13883 H HB2  . ALA D 1 79  ? 1.835   28.208  45.107  1.00 99.16  ? 79  ALA D HB2  1 
ATOM   13884 H HB3  . ALA D 1 79  ? 2.238   28.464  43.591  1.00 99.16  ? 79  ALA D HB3  1 
ATOM   13885 N N    . PHE D 1 80  ? 2.852   26.098  41.781  1.00 80.35  ? 80  PHE D N    1 
ATOM   13886 C CA   . PHE D 1 80  ? 2.623   25.442  40.500  1.00 78.23  ? 80  PHE D CA   1 
ATOM   13887 C C    . PHE D 1 80  ? 2.848   23.939  40.596  1.00 79.39  ? 80  PHE D C    1 
ATOM   13888 O O    . PHE D 1 80  ? 2.153   23.164  39.928  1.00 82.75  ? 80  PHE D O    1 
ATOM   13889 C CB   . PHE D 1 80  ? 3.543   26.061  39.445  1.00 78.67  ? 80  PHE D CB   1 
ATOM   13890 C CG   . PHE D 1 80  ? 3.201   25.678  38.033  1.00 79.86  ? 80  PHE D CG   1 
ATOM   13891 C CD1  . PHE D 1 80  ? 1.971   26.011  37.485  1.00 81.52  ? 80  PHE D CD1  1 
ATOM   13892 C CD2  . PHE D 1 80  ? 4.115   24.995  37.246  1.00 78.93  ? 80  PHE D CD2  1 
ATOM   13893 C CE1  . PHE D 1 80  ? 1.658   25.662  36.185  1.00 80.96  ? 80  PHE D CE1  1 
ATOM   13894 C CE2  . PHE D 1 80  ? 3.804   24.643  35.950  1.00 79.28  ? 80  PHE D CE2  1 
ATOM   13895 C CZ   . PHE D 1 80  ? 2.574   24.977  35.419  1.00 79.42  ? 80  PHE D CZ   1 
ATOM   13896 H H    . PHE D 1 80  ? 3.480   26.686  41.770  1.00 96.42  ? 80  PHE D H    1 
ATOM   13897 H HA   . PHE D 1 80  ? 1.704   25.583  40.224  1.00 93.87  ? 80  PHE D HA   1 
ATOM   13898 H HB2  . PHE D 1 80  ? 3.484   27.027  39.510  1.00 94.41  ? 80  PHE D HB2  1 
ATOM   13899 H HB3  . PHE D 1 80  ? 4.452   25.771  39.617  1.00 94.41  ? 80  PHE D HB3  1 
ATOM   13900 H HD1  . PHE D 1 80  ? 1.350   26.475  37.999  1.00 97.82  ? 80  PHE D HD1  1 
ATOM   13901 H HD2  . PHE D 1 80  ? 4.946   24.771  37.597  1.00 94.72  ? 80  PHE D HD2  1 
ATOM   13902 H HE1  . PHE D 1 80  ? 0.829   25.889  35.829  1.00 97.16  ? 80  PHE D HE1  1 
ATOM   13903 H HE2  . PHE D 1 80  ? 4.424   24.181  35.432  1.00 95.13  ? 80  PHE D HE2  1 
ATOM   13904 H HZ   . PHE D 1 80  ? 2.365   24.740  34.544  1.00 95.31  ? 80  PHE D HZ   1 
ATOM   13905 N N    . ARG D 1 81  ? 3.799   23.508  41.420  1.00 78.72  ? 81  ARG D N    1 
ATOM   13906 C CA   . ARG D 1 81  ? 4.150   22.101  41.541  1.00 77.28  ? 81  ARG D CA   1 
ATOM   13907 C C    . ARG D 1 81  ? 3.416   21.398  42.673  1.00 84.13  ? 81  ARG D C    1 
ATOM   13908 O O    . ARG D 1 81  ? 3.615   20.193  42.864  1.00 87.28  ? 81  ARG D O    1 
ATOM   13909 C CB   . ARG D 1 81  ? 5.663   21.962  41.745  1.00 75.22  ? 81  ARG D CB   1 
ATOM   13910 C CG   . ARG D 1 81  ? 6.477   22.600  40.629  1.00 77.80  ? 81  ARG D CG   1 
ATOM   13911 C CD   . ARG D 1 81  ? 7.918   22.115  40.603  1.00 74.56  ? 81  ARG D CD   1 
ATOM   13912 N NE   . ARG D 1 81  ? 8.436   22.096  39.242  1.00 75.51  ? 81  ARG D NE   1 
ATOM   13913 C CZ   . ARG D 1 81  ? 9.716   22.223  38.916  1.00 76.94  ? 81  ARG D CZ   1 
ATOM   13914 N NH1  . ARG D 1 81  ? 10.648  22.395  39.838  1.00 74.98  ? 81  ARG D NH1  1 
ATOM   13915 N NH2  . ARG D 1 81  ? 10.067  22.173  37.630  1.00 75.31  ? 81  ARG D NH2  1 
ATOM   13916 H H    . ARG D 1 81  ? 4.263   24.024  41.929  1.00 94.47  ? 81  ARG D H    1 
ATOM   13917 H HA   . ARG D 1 81  ? 3.913   21.649  40.717  1.00 92.74  ? 81  ARG D HA   1 
ATOM   13918 H HB2  . ARG D 1 81  ? 5.909   22.394  42.578  1.00 90.26  ? 81  ARG D HB2  1 
ATOM   13919 H HB3  . ARG D 1 81  ? 5.891   21.020  41.779  1.00 90.26  ? 81  ARG D HB3  1 
ATOM   13920 H HG2  . ARG D 1 81  ? 6.071   22.380  39.776  1.00 93.36  ? 81  ARG D HG2  1 
ATOM   13921 H HG3  . ARG D 1 81  ? 6.487   23.562  40.754  1.00 93.36  ? 81  ARG D HG3  1 
ATOM   13922 H HD2  . ARG D 1 81  ? 8.469   22.710  41.134  1.00 89.47  ? 81  ARG D HD2  1 
ATOM   13923 H HD3  . ARG D 1 81  ? 7.962   21.214  40.962  1.00 89.47  ? 81  ARG D HD3  1 
ATOM   13924 H HE   . ARG D 1 81  ? 7.871   21.995  38.602  1.00 90.61  ? 81  ARG D HE   1 
ATOM   13925 H HH11 . ARG D 1 81  ? 10.429  22.426  40.669  1.00 89.97  ? 81  ARG D HH11 1 
ATOM   13926 H HH12 . ARG D 1 81  ? 11.472  22.475  39.607  1.00 89.97  ? 81  ARG D HH12 1 
ATOM   13927 H HH21 . ARG D 1 81  ? 9.467   22.060  37.024  1.00 90.37  ? 81  ARG D HH21 1 
ATOM   13928 H HH22 . ARG D 1 81  ? 10.894  22.254  37.407  1.00 90.37  ? 81  ARG D HH22 1 
ATOM   13929 N N    . ASP D 1 82  ? 2.577   22.110  43.420  1.00 82.04  ? 82  ASP D N    1 
ATOM   13930 C CA   . ASP D 1 82  ? 1.804   21.521  44.508  1.00 85.46  ? 82  ASP D CA   1 
ATOM   13931 C C    . ASP D 1 82  ? 0.470   21.032  43.955  1.00 87.39  ? 82  ASP D C    1 
ATOM   13932 O O    . ASP D 1 82  ? -0.375  21.836  43.550  1.00 87.04  ? 82  ASP D O    1 
ATOM   13933 C CB   . ASP D 1 82  ? 1.595   22.538  45.625  1.00 87.81  ? 82  ASP D CB   1 
ATOM   13934 C CG   . ASP D 1 82  ? 1.017   21.917  46.874  1.00 87.04  ? 82  ASP D CG   1 
ATOM   13935 O OD1  . ASP D 1 82  ? 0.498   20.784  46.795  1.00 91.17  ? 82  ASP D OD1  1 
ATOM   13936 O OD2  . ASP D 1 82  ? 1.084   22.563  47.936  1.00 88.72  ? 82  ASP D OD2  1 
ATOM   13937 H H    . ASP D 1 82  ? 2.435   22.952  43.313  1.00 98.45  ? 82  ASP D H    1 
ATOM   13938 H HA   . ASP D 1 82  ? 2.284   20.759  44.869  1.00 102.55 ? 82  ASP D HA   1 
ATOM   13939 H HB2  . ASP D 1 82  ? 2.450   22.936  45.855  1.00 105.38 ? 82  ASP D HB2  1 
ATOM   13940 H HB3  . ASP D 1 82  ? 0.982   23.224  45.318  1.00 105.38 ? 82  ASP D HB3  1 
ATOM   13941 N N    . LYS D 1 83  ? 0.279   19.711  43.943  1.00 90.06  ? 83  LYS D N    1 
ATOM   13942 C CA   . LYS D 1 83  ? -0.977  19.153  43.459  1.00 92.33  ? 83  LYS D CA   1 
ATOM   13943 C C    . LYS D 1 83  ? -2.163  19.590  44.308  1.00 94.66  ? 83  LYS D C    1 
ATOM   13944 O O    . LYS D 1 83  ? -3.298  19.582  43.819  1.00 95.18  ? 83  LYS D O    1 
ATOM   13945 C CB   . LYS D 1 83  ? -0.894  17.622  43.424  1.00 92.30  ? 83  LYS D CB   1 
ATOM   13946 C CG   . LYS D 1 83  ? -1.032  16.943  44.781  1.00 96.50  ? 83  LYS D CG   1 
ATOM   13947 C CD   . LYS D 1 83  ? -1.082  15.416  44.657  1.00 94.76  ? 83  LYS D CD   1 
ATOM   13948 C CE   . LYS D 1 83  ? 0.237   14.839  44.146  1.00 92.59  ? 83  LYS D CE   1 
ATOM   13949 N NZ   . LYS D 1 83  ? 1.160   14.446  45.257  1.00 89.44  ? 83  LYS D NZ   1 
ATOM   13950 H H    . LYS D 1 83  ? 0.853   19.128  44.207  1.00 108.07 ? 83  LYS D H    1 
ATOM   13951 H HA   . LYS D 1 83  ? -1.128  19.463  42.553  1.00 110.80 ? 83  LYS D HA   1 
ATOM   13952 H HB2  . LYS D 1 83  ? -1.607  17.288  42.857  1.00 110.76 ? 83  LYS D HB2  1 
ATOM   13953 H HB3  . LYS D 1 83  ? -0.033  17.369  43.058  1.00 110.76 ? 83  LYS D HB3  1 
ATOM   13954 H HG2  . LYS D 1 83  ? -0.270  17.177  45.334  1.00 115.79 ? 83  LYS D HG2  1 
ATOM   13955 H HG3  . LYS D 1 83  ? -1.853  17.240  45.204  1.00 115.79 ? 83  LYS D HG3  1 
ATOM   13956 H HD2  . LYS D 1 83  ? -1.264  15.031  45.528  1.00 113.72 ? 83  LYS D HD2  1 
ATOM   13957 H HD3  . LYS D 1 83  ? -1.782  15.170  44.032  1.00 113.72 ? 83  LYS D HD3  1 
ATOM   13958 H HE2  . LYS D 1 83  ? 0.053   14.049  43.615  1.00 111.10 ? 83  LYS D HE2  1 
ATOM   13959 H HE3  . LYS D 1 83  ? 0.686   15.506  43.604  1.00 111.10 ? 83  LYS D HE3  1 
ATOM   13960 H HZ1  . LYS D 1 83  ? 1.919   14.123  44.922  1.00 107.33 ? 83  LYS D HZ1  1 
ATOM   13961 H HZ2  . LYS D 1 83  ? 1.346   15.155  45.763  1.00 107.33 ? 83  LYS D HZ2  1 
ATOM   13962 H HZ3  . LYS D 1 83  ? 0.778   13.822  45.763  1.00 107.33 ? 83  LYS D HZ3  1 
ATOM   13963 N N    . ASP D 1 84  ? -1.924  19.974  45.563  1.00 99.38  ? 84  ASP D N    1 
ATOM   13964 C CA   . ASP D 1 84  ? -2.991  20.307  46.497  1.00 99.95  ? 84  ASP D CA   1 
ATOM   13965 C C    . ASP D 1 84  ? -3.324  21.791  46.532  1.00 95.48  ? 84  ASP D C    1 
ATOM   13966 O O    . ASP D 1 84  ? -4.287  22.176  47.205  1.00 98.03  ? 84  ASP D O    1 
ATOM   13967 C CB   . ASP D 1 84  ? -2.614  19.841  47.908  1.00 98.52  ? 84  ASP D CB   1 
ATOM   13968 C CG   . ASP D 1 84  ? -2.621  18.333  48.040  1.00 103.65 ? 84  ASP D CG   1 
ATOM   13969 O OD1  . ASP D 1 84  ? -3.560  17.702  47.512  1.00 102.64 ? 84  ASP D OD1  1 
ATOM   13970 O OD2  . ASP D 1 84  ? -1.689  17.778  48.660  1.00 110.66 ? 84  ASP D OD2  1 
ATOM   13971 H H    . ASP D 1 84  ? -1.137  20.049  45.901  1.00 119.26 ? 84  ASP D H    1 
ATOM   13972 H HA   . ASP D 1 84  ? -3.794  19.835  46.226  1.00 119.94 ? 84  ASP D HA   1 
ATOM   13973 H HB2  . ASP D 1 84  ? -1.721  20.158  48.118  1.00 118.22 ? 84  ASP D HB2  1 
ATOM   13974 H HB3  . ASP D 1 84  ? -3.252  20.203  48.543  1.00 118.22 ? 84  ASP D HB3  1 
ATOM   13975 N N    . PHE D 1 85  ? -2.559  22.629  45.839  1.00 91.85  ? 85  PHE D N    1 
ATOM   13976 C CA   . PHE D 1 85  ? -2.915  24.036  45.735  1.00 93.63  ? 85  PHE D CA   1 
ATOM   13977 C C    . PHE D 1 85  ? -4.300  24.179  45.115  1.00 97.12  ? 85  PHE D C    1 
ATOM   13978 O O    . PHE D 1 85  ? -4.633  23.507  44.134  1.00 97.89  ? 85  PHE D O    1 
ATOM   13979 C CB   . PHE D 1 85  ? -1.879  24.781  44.894  1.00 90.66  ? 85  PHE D CB   1 
ATOM   13980 C CG   . PHE D 1 85  ? -2.060  26.268  44.890  1.00 90.22  ? 85  PHE D CG   1 
ATOM   13981 C CD1  . PHE D 1 85  ? -3.081  26.854  44.162  1.00 93.37  ? 85  PHE D CD1  1 
ATOM   13982 C CD2  . PHE D 1 85  ? -1.206  27.083  45.614  1.00 88.66  ? 85  PHE D CD2  1 
ATOM   13983 C CE1  . PHE D 1 85  ? -3.250  28.225  44.159  1.00 95.63  ? 85  PHE D CE1  1 
ATOM   13984 C CE2  . PHE D 1 85  ? -1.368  28.453  45.615  1.00 86.59  ? 85  PHE D CE2  1 
ATOM   13985 C CZ   . PHE D 1 85  ? -2.393  29.026  44.887  1.00 91.08  ? 85  PHE D CZ   1 
ATOM   13986 H H    . PHE D 1 85  ? -1.838  22.409  45.426  1.00 110.22 ? 85  PHE D H    1 
ATOM   13987 H HA   . PHE D 1 85  ? -2.928  24.439  46.617  1.00 112.36 ? 85  PHE D HA   1 
ATOM   13988 H HB2  . PHE D 1 85  ? -0.996  24.591  45.247  1.00 108.79 ? 85  PHE D HB2  1 
ATOM   13989 H HB3  . PHE D 1 85  ? -1.943  24.473  43.976  1.00 108.79 ? 85  PHE D HB3  1 
ATOM   13990 H HD1  . PHE D 1 85  ? -3.660  26.318  43.669  1.00 112.05 ? 85  PHE D HD1  1 
ATOM   13991 H HD2  . PHE D 1 85  ? -0.514  26.702  46.105  1.00 106.40 ? 85  PHE D HD2  1 
ATOM   13992 H HE1  . PHE D 1 85  ? -3.940  28.608  43.667  1.00 114.76 ? 85  PHE D HE1  1 
ATOM   13993 H HE2  . PHE D 1 85  ? -0.789  28.990  46.105  1.00 103.90 ? 85  PHE D HE2  1 
ATOM   13994 H HZ   . PHE D 1 85  ? -2.505  29.949  44.888  1.00 109.30 ? 85  PHE D HZ   1 
ATOM   13995 N N    . SER D 1 86  ? -5.111  25.063  45.696  1.00 95.90  ? 86  SER D N    1 
ATOM   13996 C CA   . SER D 1 86  ? -6.461  25.304  45.202  1.00 99.92  ? 86  SER D CA   1 
ATOM   13997 C C    . SER D 1 86  ? -6.623  26.759  44.778  1.00 103.87 ? 86  SER D C    1 
ATOM   13998 O O    . SER D 1 86  ? -6.532  27.079  43.587  1.00 105.75 ? 86  SER D O    1 
ATOM   13999 C CB   . SER D 1 86  ? -7.492  24.938  46.272  1.00 98.36  ? 86  SER D CB   1 
ATOM   14000 O OG   . SER D 1 86  ? -8.809  25.239  45.844  1.00 99.84  ? 86  SER D OG   1 
ATOM   14001 H H    . SER D 1 86  ? -4.899  25.538  46.381  1.00 115.08 ? 86  SER D H    1 
ATOM   14002 H HA   . SER D 1 86  ? -6.624  24.744  44.427  1.00 119.90 ? 86  SER D HA   1 
ATOM   14003 H HB2  . SER D 1 86  ? -7.430  23.988  46.455  1.00 118.03 ? 86  SER D HB2  1 
ATOM   14004 H HB3  . SER D 1 86  ? -7.301  25.444  47.077  1.00 118.03 ? 86  SER D HB3  1 
ATOM   14005 H HG   . SER D 1 86  ? -8.987  24.813  45.142  1.00 119.81 ? 86  SER D HG   1 
ATOM   14006 N N    . LYS D 1 87  ? -6.865  27.645  45.745  1.00 97.14  ? 87  LYS D N    1 
ATOM   14007 C CA   . LYS D 1 87  ? -6.989  29.073  45.495  1.00 92.93  ? 87  LYS D CA   1 
ATOM   14008 C C    . LYS D 1 87  ? -5.954  29.905  46.236  1.00 91.22  ? 87  LYS D C    1 
ATOM   14009 O O    . LYS D 1 87  ? -5.517  30.931  45.712  1.00 91.60  ? 87  LYS D O    1 
ATOM   14010 C CB   . LYS D 1 87  ? -8.393  29.566  45.888  1.00 94.65  ? 87  LYS D CB   1 
ATOM   14011 C CG   . LYS D 1 87  ? -9.544  28.735  45.323  1.00 97.44  ? 87  LYS D CG   1 
ATOM   14012 C CD   . LYS D 1 87  ? -10.763 28.755  46.249  1.00 96.15  ? 87  LYS D CD   1 
ATOM   14013 C CE   . LYS D 1 87  ? -11.612 27.495  46.090  1.00 98.85  ? 87  LYS D CE   1 
ATOM   14014 N NZ   . LYS D 1 87  ? -10.945 26.285  46.653  1.00 97.72  ? 87  LYS D NZ   1 
ATOM   14015 H H    . LYS D 1 87  ? -6.962  27.433  46.573  1.00 116.57 ? 87  LYS D H    1 
ATOM   14016 H HA   . LYS D 1 87  ? -6.876  29.235  44.546  1.00 111.52 ? 87  LYS D HA   1 
ATOM   14017 H HB2  . LYS D 1 87  ? -8.467  29.548  46.855  1.00 113.58 ? 87  LYS D HB2  1 
ATOM   14018 H HB3  . LYS D 1 87  ? -8.503  30.474  45.564  1.00 113.58 ? 87  LYS D HB3  1 
ATOM   14019 H HG2  . LYS D 1 87  ? -9.809  29.096  44.463  1.00 116.93 ? 87  LYS D HG2  1 
ATOM   14020 H HG3  . LYS D 1 87  ? -9.254  27.815  45.221  1.00 116.93 ? 87  LYS D HG3  1 
ATOM   14021 H HD2  . LYS D 1 87  ? -10.465 28.806  47.171  1.00 115.38 ? 87  LYS D HD2  1 
ATOM   14022 H HD3  . LYS D 1 87  ? -11.315 29.523  46.036  1.00 115.38 ? 87  LYS D HD3  1 
ATOM   14023 H HE2  . LYS D 1 87  ? -12.454 27.619  46.555  1.00 118.62 ? 87  LYS D HE2  1 
ATOM   14024 H HE3  . LYS D 1 87  ? -11.773 27.339  45.147  1.00 118.62 ? 87  LYS D HE3  1 
ATOM   14025 H HZ1  . LYS D 1 87  ? -10.167 26.148  46.244  1.00 117.26 ? 87  LYS D HZ1  1 
ATOM   14026 H HZ2  . LYS D 1 87  ? -11.463 25.571  46.536  1.00 117.26 ? 87  LYS D HZ2  1 
ATOM   14027 H HZ3  . LYS D 1 87  ? -10.799 26.396  47.524  1.00 117.26 ? 87  LYS D HZ3  1 
ATOM   14028 N N    . GLN D 1 88  ? -5.553  29.491  47.435  1.00 91.46  ? 88  GLN D N    1 
ATOM   14029 C CA   . GLN D 1 88  ? -4.552  30.188  48.229  1.00 86.98  ? 88  GLN D CA   1 
ATOM   14030 C C    . GLN D 1 88  ? -3.726  29.153  48.976  1.00 85.42  ? 88  GLN D C    1 
ATOM   14031 O O    . GLN D 1 88  ? -4.207  28.064  49.298  1.00 84.81  ? 88  GLN D O    1 
ATOM   14032 C CB   . GLN D 1 88  ? -5.196  31.171  49.227  1.00 86.99  ? 88  GLN D CB   1 
ATOM   14033 C CG   . GLN D 1 88  ? -4.207  32.013  50.046  1.00 85.29  ? 88  GLN D CG   1 
ATOM   14034 C CD   . GLN D 1 88  ? -3.592  31.269  51.236  1.00 86.73  ? 88  GLN D CD   1 
ATOM   14035 O OE1  . GLN D 1 88  ? -3.721  30.056  51.370  1.00 91.43  ? 88  GLN D OE1  1 
ATOM   14036 N NE2  . GLN D 1 88  ? -2.912  32.002  52.098  1.00 85.70  ? 88  GLN D NE2  1 
ATOM   14037 H H    . GLN D 1 88  ? -5.857  28.786  47.821  1.00 109.75 ? 88  GLN D H    1 
ATOM   14038 H HA   . GLN D 1 88  ? -3.966  30.698  47.648  1.00 104.38 ? 88  GLN D HA   1 
ATOM   14039 H HB2  . GLN D 1 88  ? -5.759  31.786  48.732  1.00 104.38 ? 88  GLN D HB2  1 
ATOM   14040 H HB3  . GLN D 1 88  ? -5.732  30.662  49.855  1.00 104.38 ? 88  GLN D HB3  1 
ATOM   14041 H HG2  . GLN D 1 88  ? -3.481  32.292  49.467  1.00 102.35 ? 88  GLN D HG2  1 
ATOM   14042 H HG3  . GLN D 1 88  ? -4.673  32.790  50.393  1.00 102.35 ? 88  GLN D HG3  1 
ATOM   14043 H HE21 . GLN D 1 88  ? -2.834  32.850  51.974  1.00 102.84 ? 88  GLN D HE21 1 
ATOM   14044 H HE22 . GLN D 1 88  ? -2.547  31.632  52.783  1.00 102.84 ? 88  GLN D HE22 1 
ATOM   14045 N N    . LYS D 1 89  ? -2.482  29.516  49.278  1.00 84.46  ? 89  LYS D N    1 
ATOM   14046 C CA   . LYS D 1 89  ? -1.625  28.701  50.126  1.00 83.58  ? 89  LYS D CA   1 
ATOM   14047 C C    . LYS D 1 89  ? -0.377  29.505  50.451  1.00 82.98  ? 89  LYS D C    1 
ATOM   14048 O O    . LYS D 1 89  ? 0.188   30.162  49.576  1.00 82.15  ? 89  LYS D O    1 
ATOM   14049 C CB   . LYS D 1 89  ? -1.250  27.377  49.452  1.00 84.77  ? 89  LYS D CB   1 
ATOM   14050 C CG   . LYS D 1 89  ? -0.442  26.443  50.345  1.00 82.47  ? 89  LYS D CG   1 
ATOM   14051 C CD   . LYS D 1 89  ? -0.350  25.043  49.755  1.00 84.72  ? 89  LYS D CD   1 
ATOM   14052 C CE   . LYS D 1 89  ? -1.003  24.014  50.665  1.00 85.20  ? 89  LYS D CE   1 
ATOM   14053 N NZ   . LYS D 1 89  ? -0.470  22.645  50.437  1.00 82.36  ? 89  LYS D NZ   1 
ATOM   14054 H H    . LYS D 1 89  ? -2.109  30.240  48.999  1.00 101.35 ? 89  LYS D H    1 
ATOM   14055 H HA   . LYS D 1 89  ? -2.087  28.490  50.952  1.00 100.30 ? 89  LYS D HA   1 
ATOM   14056 H HB2  . LYS D 1 89  ? -2.064  26.915  49.198  1.00 101.72 ? 89  LYS D HB2  1 
ATOM   14057 H HB3  . LYS D 1 89  ? -0.718  27.568  48.663  1.00 101.72 ? 89  LYS D HB3  1 
ATOM   14058 H HG2  . LYS D 1 89  ? 0.458   26.792  50.443  1.00 98.97  ? 89  LYS D HG2  1 
ATOM   14059 H HG3  . LYS D 1 89  ? -0.870  26.380  51.213  1.00 98.97  ? 89  LYS D HG3  1 
ATOM   14060 H HD2  . LYS D 1 89  ? -0.803  25.024  48.897  1.00 101.66 ? 89  LYS D HD2  1 
ATOM   14061 H HD3  . LYS D 1 89  ? 0.583   24.802  49.642  1.00 101.66 ? 89  LYS D HD3  1 
ATOM   14062 H HE2  . LYS D 1 89  ? -0.834  24.254  51.590  1.00 102.23 ? 89  LYS D HE2  1 
ATOM   14063 H HE3  . LYS D 1 89  ? -1.958  23.999  50.495  1.00 102.23 ? 89  LYS D HE3  1 
ATOM   14064 H HZ1  . LYS D 1 89  ? 0.406   22.629  50.594  1.00 98.84  ? 89  LYS D HZ1  1 
ATOM   14065 H HZ2  . LYS D 1 89  ? -0.872  22.067  50.981  1.00 98.84  ? 89  LYS D HZ2  1 
ATOM   14066 H HZ3  . LYS D 1 89  ? -0.617  22.397  49.594  1.00 98.84  ? 89  LYS D HZ3  1 
ATOM   14067 N N    . ASN D 1 90  ? 0.037   29.458  51.711  1.00 83.69  ? 90  ASN D N    1 
ATOM   14068 C CA   . ASN D 1 90  ? 1.254   30.126  52.142  1.00 82.40  ? 90  ASN D CA   1 
ATOM   14069 C C    . ASN D 1 90  ? 2.426   29.162  52.037  1.00 80.03  ? 90  ASN D C    1 
ATOM   14070 O O    . ASN D 1 90  ? 2.297   27.972  52.339  1.00 80.97  ? 90  ASN D O    1 
ATOM   14071 C CB   . ASN D 1 90  ? 1.115   30.630  53.575  1.00 81.52  ? 90  ASN D CB   1 
ATOM   14072 C CG   . ASN D 1 90  ? 0.234   31.856  53.674  1.00 85.05  ? 90  ASN D CG   1 
ATOM   14073 O OD1  . ASN D 1 90  ? -0.955  31.760  53.979  1.00 90.92  ? 90  ASN D OD1  1 
ATOM   14074 N ND2  . ASN D 1 90  ? 0.816   33.023  53.420  1.00 85.15  ? 90  ASN D ND2  1 
ATOM   14075 H H    . ASN D 1 90  ? -0.376  29.042  52.340  1.00 100.43 ? 90  ASN D H    1 
ATOM   14076 H HA   . ASN D 1 90  ? 1.429   30.893  51.575  1.00 98.89  ? 90  ASN D HA   1 
ATOM   14077 H HB2  . ASN D 1 90  ? 0.720   29.931  54.120  1.00 97.83  ? 90  ASN D HB2  1 
ATOM   14078 H HB3  . ASN D 1 90  ? 1.993   30.861  53.917  1.00 97.83  ? 90  ASN D HB3  1 
ATOM   14079 H HD21 . ASN D 1 90  ? 0.358   33.750  53.462  1.00 102.18 ? 90  ASN D HD21 1 
ATOM   14080 H HD22 . ASN D 1 90  ? 1.650   33.051  53.213  1.00 102.18 ? 90  ASN D HD22 1 
ATOM   14081 N N    . TYR D 1 91  ? 3.570   29.683  51.603  1.00 79.60  ? 91  TYR D N    1 
ATOM   14082 C CA   . TYR D 1 91  ? 4.771   28.882  51.415  1.00 81.21  ? 91  TYR D CA   1 
ATOM   14083 C C    . TYR D 1 91  ? 5.933   29.552  52.127  1.00 81.21  ? 91  TYR D C    1 
ATOM   14084 O O    . TYR D 1 91  ? 6.192   30.742  51.921  1.00 83.09  ? 91  TYR D O    1 
ATOM   14085 C CB   . TYR D 1 91  ? 5.084   28.704  49.931  1.00 79.31  ? 91  TYR D CB   1 
ATOM   14086 C CG   . TYR D 1 91  ? 4.078   27.835  49.213  1.00 79.57  ? 91  TYR D CG   1 
ATOM   14087 C CD1  . TYR D 1 91  ? 2.912   28.379  48.687  1.00 79.59  ? 91  TYR D CD1  1 
ATOM   14088 C CD2  . TYR D 1 91  ? 4.288   26.470  49.069  1.00 77.84  ? 91  TYR D CD2  1 
ATOM   14089 C CE1  . TYR D 1 91  ? 1.986   27.585  48.037  1.00 80.53  ? 91  TYR D CE1  1 
ATOM   14090 C CE2  . TYR D 1 91  ? 3.369   25.671  48.419  1.00 77.17  ? 91  TYR D CE2  1 
ATOM   14091 C CZ   . TYR D 1 91  ? 2.220   26.232  47.906  1.00 80.51  ? 91  TYR D CZ   1 
ATOM   14092 O OH   . TYR D 1 91  ? 1.303   25.439  47.258  1.00 82.43  ? 91  TYR D OH   1 
ATOM   14093 H H    . TYR D 1 91  ? 3.676   30.514  51.407  1.00 95.52  ? 91  TYR D H    1 
ATOM   14094 H HA   . TYR D 1 91  ? 4.643   28.004  51.807  1.00 97.45  ? 91  TYR D HA   1 
ATOM   14095 H HB2  . TYR D 1 91  ? 5.086   29.574  49.503  1.00 95.18  ? 91  TYR D HB2  1 
ATOM   14096 H HB3  . TYR D 1 91  ? 5.956   28.288  49.841  1.00 95.18  ? 91  TYR D HB3  1 
ATOM   14097 H HD1  . TYR D 1 91  ? 2.753   29.291  48.773  1.00 95.52  ? 91  TYR D HD1  1 
ATOM   14098 H HD2  . TYR D 1 91  ? 5.061   26.088  49.416  1.00 93.41  ? 91  TYR D HD2  1 
ATOM   14099 H HE1  . TYR D 1 91  ? 1.209   27.962  47.690  1.00 96.63  ? 91  TYR D HE1  1 
ATOM   14100 H HE2  . TYR D 1 91  ? 3.525   24.759  48.328  1.00 92.60  ? 91  TYR D HE2  1 
ATOM   14101 H HH   . TYR D 1 91  ? 1.565   24.641  47.254  1.00 98.91  ? 91  TYR D HH   1 
ATOM   14102 N N    . ASN D 1 92  ? 6.626   28.789  52.966  1.00 77.87  ? 92  ASN D N    1 
ATOM   14103 C CA   . ASN D 1 92  ? 7.794   29.289  53.677  1.00 80.57  ? 92  ASN D CA   1 
ATOM   14104 C C    . ASN D 1 92  ? 9.040   28.972  52.862  1.00 80.20  ? 92  ASN D C    1 
ATOM   14105 O O    . ASN D 1 92  ? 9.326   27.802  52.583  1.00 82.17  ? 92  ASN D O    1 
ATOM   14106 C CB   . ASN D 1 92  ? 7.871   28.676  55.071  1.00 83.20  ? 92  ASN D CB   1 
ATOM   14107 C CG   . ASN D 1 92  ? 6.973   29.389  56.065  1.00 81.53  ? 92  ASN D CG   1 
ATOM   14108 O OD1  . ASN D 1 92  ? 7.207   30.550  56.407  1.00 80.61  ? 92  ASN D OD1  1 
ATOM   14109 N ND2  . ASN D 1 92  ? 5.930   28.703  56.520  1.00 84.45  ? 92  ASN D ND2  1 
ATOM   14110 H H    . ASN D 1 92  ? 6.436   27.969  53.141  1.00 93.45  ? 92  ASN D H    1 
ATOM   14111 H HA   . ASN D 1 92  ? 7.736   30.252  53.778  1.00 96.68  ? 92  ASN D HA   1 
ATOM   14112 H HB2  . ASN D 1 92  ? 7.593   27.748  55.025  1.00 99.84  ? 92  ASN D HB2  1 
ATOM   14113 H HB3  . ASN D 1 92  ? 8.784   28.734  55.393  1.00 99.84  ? 92  ASN D HB3  1 
ATOM   14114 H HD21 . ASN D 1 92  ? 5.792   27.898  56.248  1.00 101.34 ? 92  ASN D HD21 1 
ATOM   14115 H HD22 . ASN D 1 92  ? 5.391   29.063  57.085  1.00 101.34 ? 92  ASN D HD22 1 
ATOM   14116 N N    . ILE D 1 93  ? 9.767   30.014  52.463  1.00 81.43  ? 93  ILE D N    1 
ATOM   14117 C CA   . ILE D 1 93  ? 10.975  29.860  51.671  1.00 81.95  ? 93  ILE D CA   1 
ATOM   14118 C C    . ILE D 1 93  ? 12.082  30.685  52.316  1.00 80.27  ? 93  ILE D C    1 
ATOM   14119 O O    . ILE D 1 93  ? 11.865  31.423  53.277  1.00 80.32  ? 93  ILE D O    1 
ATOM   14120 C CB   . ILE D 1 93  ? 10.772  30.268  50.193  1.00 81.00  ? 93  ILE D CB   1 
ATOM   14121 C CG1  . ILE D 1 93  ? 10.829  31.785  50.017  1.00 79.55  ? 93  ILE D CG1  1 
ATOM   14122 C CG2  . ILE D 1 93  ? 9.442   29.716  49.663  1.00 80.91  ? 93  ILE D CG2  1 
ATOM   14123 C CD1  . ILE D 1 93  ? 10.812  32.234  48.550  1.00 79.31  ? 93  ILE D CD1  1 
ATOM   14124 H H    . ILE D 1 93  ? 9.573   30.832  52.644  1.00 97.72  ? 93  ILE D H    1 
ATOM   14125 H HA   . ILE D 1 93  ? 11.247  28.929  51.684  1.00 98.34  ? 93  ILE D HA   1 
ATOM   14126 H HB   . ILE D 1 93  ? 11.500  29.882  49.680  1.00 97.20  ? 93  ILE D HB   1 
ATOM   14127 H HG12 . ILE D 1 93  ? 10.060  32.180  50.457  1.00 95.46  ? 93  ILE D HG12 1 
ATOM   14128 H HG13 . ILE D 1 93  ? 11.648  32.116  50.419  1.00 95.46  ? 93  ILE D HG13 1 
ATOM   14129 H HG21 . ILE D 1 93  ? 9.353   29.953  48.726  1.00 97.09  ? 93  ILE D HG21 1 
ATOM   14130 H HG22 . ILE D 1 93  ? 9.439   28.751  49.762  1.00 97.09  ? 93  ILE D HG22 1 
ATOM   14131 H HG23 . ILE D 1 93  ? 8.714   30.104  50.172  1.00 97.09  ? 93  ILE D HG23 1 
ATOM   14132 H HD11 . ILE D 1 93  ? 10.876  33.201  48.514  1.00 95.18  ? 93  ILE D HD11 1 
ATOM   14133 H HD12 . ILE D 1 93  ? 11.566  31.834  48.089  1.00 95.18  ? 93  ILE D HD12 1 
ATOM   14134 H HD13 . ILE D 1 93  ? 9.982   31.942  48.141  1.00 95.18  ? 93  ILE D HD13 1 
ATOM   14135 N N    . THR D 1 94  ? 13.283  30.546  51.762  1.00 79.89  ? 94  THR D N    1 
ATOM   14136 C CA   . THR D 1 94  ? 14.432  31.346  52.151  1.00 77.63  ? 94  THR D CA   1 
ATOM   14137 C C    . THR D 1 94  ? 15.127  31.836  50.889  1.00 80.29  ? 94  THR D C    1 
ATOM   14138 O O    . THR D 1 94  ? 14.959  31.272  49.805  1.00 73.60  ? 94  THR D O    1 
ATOM   14139 C CB   . THR D 1 94  ? 15.411  30.546  53.019  1.00 78.35  ? 94  THR D CB   1 
ATOM   14140 O OG1  . THR D 1 94  ? 15.988  29.492  52.233  1.00 76.99  ? 94  THR D OG1  1 
ATOM   14141 C CG2  . THR D 1 94  ? 14.697  29.956  54.220  1.00 80.90  ? 94  THR D CG2  1 
ATOM   14142 H H    . THR D 1 94  ? 13.459  29.978  51.140  1.00 95.87  ? 94  THR D H    1 
ATOM   14143 H HA   . THR D 1 94  ? 14.143  32.114  52.668  1.00 93.15  ? 94  THR D HA   1 
ATOM   14144 H HB   . THR D 1 94  ? 16.116  31.128  53.345  1.00 94.02  ? 94  THR D HB   1 
ATOM   14145 H HG1  . THR D 1 94  ? 16.511  29.035  52.704  1.00 92.39  ? 94  THR D HG1  1 
ATOM   14146 H HG21 . THR D 1 94  ? 15.334  29.512  54.800  1.00 97.08  ? 94  THR D HG21 1 
ATOM   14147 H HG22 . THR D 1 94  ? 14.253  30.659  54.720  1.00 97.08  ? 94  THR D HG22 1 
ATOM   14148 H HG23 . THR D 1 94  ? 14.033  29.311  53.928  1.00 97.08  ? 94  THR D HG23 1 
ATOM   14149 N N    . CYS D 1 95  ? 15.915  32.895  51.041  1.00 80.32  ? 95  CYS D N    1 
ATOM   14150 C CA   . CYS D 1 95  ? 16.631  33.473  49.916  1.00 74.95  ? 95  CYS D CA   1 
ATOM   14151 C C    . CYS D 1 95  ? 17.931  34.095  50.395  1.00 76.83  ? 95  CYS D C    1 
ATOM   14152 O O    . CYS D 1 95  ? 17.967  34.753  51.437  1.00 79.42  ? 95  CYS D O    1 
ATOM   14153 C CB   . CYS D 1 95  ? 15.782  34.530  49.204  1.00 79.46  ? 95  CYS D CB   1 
ATOM   14154 S SG   . CYS D 1 95  ? 16.686  35.426  47.907  1.00 82.31  ? 95  CYS D SG   1 
ATOM   14155 H H    . CYS D 1 95  ? 16.050  33.297  51.789  1.00 96.39  ? 95  CYS D H    1 
ATOM   14156 H HA   . CYS D 1 95  ? 16.851  32.768  49.288  1.00 89.94  ? 95  CYS D HA   1 
ATOM   14157 H HB2  . CYS D 1 95  ? 15.022  34.093  48.789  1.00 95.35  ? 95  CYS D HB2  1 
ATOM   14158 H HB3  . CYS D 1 95  ? 15.477  35.179  49.857  1.00 95.35  ? 95  CYS D HB3  1 
ATOM   14159 H HG   . CYS D 1 95  ? 17.559  36.073  48.415  1.00 98.78  ? 95  CYS D HG   1 
ATOM   14160 N N    . SER D 1 96  ? 18.993  33.894  49.616  1.00 78.10  ? 96  SER D N    1 
ATOM   14161 C CA   . SER D 1 96  ? 20.298  34.443  49.961  1.00 79.51  ? 96  SER D CA   1 
ATOM   14162 C C    . SER D 1 96  ? 20.206  35.945  50.190  1.00 81.91  ? 96  SER D C    1 
ATOM   14163 O O    . SER D 1 96  ? 19.554  36.667  49.431  1.00 81.94  ? 96  SER D O    1 
ATOM   14164 C CB   . SER D 1 96  ? 21.301  34.150  48.846  1.00 77.57  ? 96  SER D CB   1 
ATOM   14165 O OG   . SER D 1 96  ? 20.812  34.637  47.610  1.00 76.53  ? 96  SER D OG   1 
ATOM   14166 H H    . SER D 1 96  ? 18.983  33.443  48.883  1.00 93.72  ? 96  SER D H    1 
ATOM   14167 H HA   . SER D 1 96  ? 20.613  34.026  50.778  1.00 95.41  ? 96  SER D HA   1 
ATOM   14168 H HB2  . SER D 1 96  ? 22.141  34.589  49.051  1.00 93.08  ? 96  SER D HB2  1 
ATOM   14169 H HB3  . SER D 1 96  ? 21.434  33.192  48.781  1.00 93.08  ? 96  SER D HB3  1 
ATOM   14170 H HG   . SER D 1 96  ? 20.708  35.469  47.650  1.00 91.83  ? 96  SER D HG   1 
ATOM   14171 N N    . GLY D 1 97  ? 20.881  36.415  51.238  1.00 79.58  ? 97  GLY D N    1 
ATOM   14172 C CA   . GLY D 1 97  ? 20.854  37.815  51.590  1.00 80.61  ? 97  GLY D CA   1 
ATOM   14173 C C    . GLY D 1 97  ? 19.717  38.220  52.497  1.00 82.59  ? 97  GLY D C    1 
ATOM   14174 O O    . GLY D 1 97  ? 19.572  39.418  52.786  1.00 82.54  ? 97  GLY D O    1 
ATOM   14175 H H    . GLY D 1 97  ? 21.364  35.932  51.760  1.00 95.50  ? 97  GLY D H    1 
ATOM   14176 H HA2  . GLY D 1 97  ? 21.685  38.038  52.039  1.00 96.73  ? 97  GLY D HA2  1 
ATOM   14177 H HA3  . GLY D 1 97  ? 20.784  38.339  50.776  1.00 96.73  ? 97  GLY D HA3  1 
ATOM   14178 N N    . GLU D 1 98  ? 18.905  37.267  52.952  1.00 83.23  ? 98  GLU D N    1 
ATOM   14179 C CA   . GLU D 1 98  ? 17.816  37.522  53.891  1.00 87.13  ? 98  GLU D CA   1 
ATOM   14180 C C    . GLU D 1 98  ? 17.873  36.455  54.975  1.00 84.52  ? 98  GLU D C    1 
ATOM   14181 O O    . GLU D 1 98  ? 17.753  35.262  54.679  1.00 80.70  ? 98  GLU D O    1 
ATOM   14182 C CB   . GLU D 1 98  ? 16.459  37.508  53.181  1.00 86.99  ? 98  GLU D CB   1 
ATOM   14183 C CG   . GLU D 1 98  ? 15.275  37.750  54.105  1.00 91.78  ? 98  GLU D CG   1 
ATOM   14184 C CD   . GLU D 1 98  ? 15.341  39.102  54.782  1.00 95.30  ? 98  GLU D CD   1 
ATOM   14185 O OE1  . GLU D 1 98  ? 15.998  40.006  54.214  1.00 92.75  ? 98  GLU D OE1  1 
ATOM   14186 O OE2  . GLU D 1 98  ? 14.742  39.258  55.873  1.00 96.06  ? 98  GLU D OE2  1 
ATOM   14187 H H    . GLU D 1 98  ? 18.967  36.441  52.723  1.00 99.88  ? 98  GLU D H    1 
ATOM   14188 H HA   . GLU D 1 98  ? 17.928  38.392  54.305  1.00 104.56 ? 98  GLU D HA   1 
ATOM   14189 H HB2  . GLU D 1 98  ? 16.454  38.205  52.507  1.00 104.39 ? 98  GLU D HB2  1 
ATOM   14190 H HB3  . GLU D 1 98  ? 16.335  36.641  52.764  1.00 104.39 ? 98  GLU D HB3  1 
ATOM   14191 H HG2  . GLU D 1 98  ? 14.455  37.711  53.588  1.00 110.14 ? 98  GLU D HG2  1 
ATOM   14192 H HG3  . GLU D 1 98  ? 15.266  37.068  54.795  1.00 110.14 ? 98  GLU D HG3  1 
ATOM   14193 N N    . SER D 1 99  ? 18.055  36.882  56.224  1.00 88.92  ? 99  SER D N    1 
ATOM   14194 C CA   . SER D 1 99  ? 18.277  35.947  57.320  1.00 91.41  ? 99  SER D CA   1 
ATOM   14195 C C    . SER D 1 99  ? 16.995  35.351  57.879  1.00 90.61  ? 99  SER D C    1 
ATOM   14196 O O    . SER D 1 99  ? 17.042  34.262  58.460  1.00 89.34  ? 99  SER D O    1 
ATOM   14197 C CB   . SER D 1 99  ? 19.030  36.646  58.454  1.00 88.17  ? 99  SER D CB   1 
ATOM   14198 O OG   . SER D 1 99  ? 18.232  37.677  59.013  1.00 87.03  ? 99  SER D OG   1 
ATOM   14199 H H    . SER D 1 99  ? 18.053  37.708  56.461  1.00 106.71 ? 99  SER D H    1 
ATOM   14200 H HA   . SER D 1 99  ? 18.820  35.217  56.984  1.00 109.69 ? 99  SER D HA   1 
ATOM   14201 H HB2  . SER D 1 99  ? 19.239  35.997  59.144  1.00 105.80 ? 99  SER D HB2  1 
ATOM   14202 H HB3  . SER D 1 99  ? 19.847  37.032  58.103  1.00 105.80 ? 99  SER D HB3  1 
ATOM   14203 H HG   . SER D 1 99  ? 18.655  38.068  59.625  1.00 104.44 ? 99  SER D HG   1 
ATOM   14204 N N    . LYS D 1 100 ? 15.869  36.033  57.725  1.00 95.29  ? 100 LYS D N    1 
ATOM   14205 C CA   . LYS D 1 100 ? 14.601  35.560  58.250  1.00 91.29  ? 100 LYS D CA   1 
ATOM   14206 C C    . LYS D 1 100 ? 13.858  34.744  57.202  1.00 90.55  ? 100 LYS D C    1 
ATOM   14207 O O    . LYS D 1 100 ? 13.942  35.011  55.999  1.00 95.09  ? 100 LYS D O    1 
ATOM   14208 C CB   . LYS D 1 100 ? 13.738  36.738  58.702  1.00 101.21 ? 100 LYS D CB   1 
ATOM   14209 C CG   . LYS D 1 100 ? 13.853  37.061  60.188  1.00 109.38 ? 100 LYS D CG   1 
ATOM   14210 C CD   . LYS D 1 100 ? 13.255  38.426  60.519  1.00 107.77 ? 100 LYS D CD   1 
ATOM   14211 C CE   . LYS D 1 100 ? 13.203  38.651  62.017  1.00 115.10 ? 100 LYS D CE   1 
ATOM   14212 N NZ   . LYS D 1 100 ? 11.999  38.018  62.630  1.00 122.38 ? 100 LYS D NZ   1 
ATOM   14213 H H    . LYS D 1 100 ? 15.814  36.786  57.313  1.00 114.35 ? 100 LYS D H    1 
ATOM   14214 H HA   . LYS D 1 100 ? 14.763  34.988  59.017  1.00 109.55 ? 100 LYS D HA   1 
ATOM   14215 H HB2  . LYS D 1 100 ? 14.007  37.528  58.207  1.00 121.45 ? 100 LYS D HB2  1 
ATOM   14216 H HB3  . LYS D 1 100 ? 12.809  36.531  58.517  1.00 121.45 ? 100 LYS D HB3  1 
ATOM   14217 H HG2  . LYS D 1 100 ? 13.377  36.388  60.700  1.00 131.25 ? 100 LYS D HG2  1 
ATOM   14218 H HG3  . LYS D 1 100 ? 14.789  37.070  60.442  1.00 131.25 ? 100 LYS D HG3  1 
ATOM   14219 H HD2  . LYS D 1 100 ? 13.801  39.122  60.123  1.00 129.32 ? 100 LYS D HD2  1 
ATOM   14220 H HD3  . LYS D 1 100 ? 12.351  38.475  60.170  1.00 129.32 ? 100 LYS D HD3  1 
ATOM   14221 H HE2  . LYS D 1 100 ? 13.992  38.264  62.426  1.00 138.12 ? 100 LYS D HE2  1 
ATOM   14222 H HE3  . LYS D 1 100 ? 13.169  39.604  62.196  1.00 138.12 ? 100 LYS D HE3  1 
ATOM   14223 H HZ1  . LYS D 1 100 ? 11.992  38.164  63.508  1.00 146.86 ? 100 LYS D HZ1  1 
ATOM   14224 H HZ2  . LYS D 1 100 ? 11.259  38.362  62.274  1.00 146.86 ? 100 LYS D HZ2  1 
ATOM   14225 H HZ3  . LYS D 1 100 ? 12.009  37.140  62.483  1.00 146.86 ? 100 LYS D HZ3  1 
ATOM   14226 N N    . VAL D 1 101 ? 13.120  33.738  57.675  1.00 85.30  ? 101 VAL D N    1 
ATOM   14227 C CA   . VAL D 1 101 ? 12.315  32.913  56.784  1.00 87.09  ? 101 VAL D CA   1 
ATOM   14228 C C    . VAL D 1 101 ? 11.217  33.764  56.160  1.00 86.79  ? 101 VAL D C    1 
ATOM   14229 O O    . VAL D 1 101 ? 10.565  34.570  56.841  1.00 89.89  ? 101 VAL D O    1 
ATOM   14230 C CB   . VAL D 1 101 ? 11.731  31.712  57.548  1.00 84.14  ? 101 VAL D CB   1 
ATOM   14231 C CG1  . VAL D 1 101 ? 10.652  31.019  56.722  1.00 84.03  ? 101 VAL D CG1  1 
ATOM   14232 C CG2  . VAL D 1 101 ? 12.843  30.732  57.928  1.00 75.24  ? 101 VAL D CG2  1 
ATOM   14233 H H    . VAL D 1 101 ? 13.071  33.516  58.505  1.00 102.36 ? 101 VAL D H    1 
ATOM   14234 H HA   . VAL D 1 101 ? 12.876  32.570  56.071  1.00 104.51 ? 101 VAL D HA   1 
ATOM   14235 H HB   . VAL D 1 101 ? 11.317  32.031  58.365  1.00 100.97 ? 101 VAL D HB   1 
ATOM   14236 H HG11 . VAL D 1 101 ? 10.503  30.130  57.080  1.00 100.83 ? 101 VAL D HG11 1 
ATOM   14237 H HG12 . VAL D 1 101 ? 9.834   31.538  56.772  1.00 100.83 ? 101 VAL D HG12 1 
ATOM   14238 H HG13 . VAL D 1 101 ? 10.950  30.959  55.800  1.00 100.83 ? 101 VAL D HG13 1 
ATOM   14239 H HG21 . VAL D 1 101 ? 12.455  29.990  58.418  1.00 90.28  ? 101 VAL D HG21 1 
ATOM   14240 H HG22 . VAL D 1 101 ? 13.268  30.408  57.119  1.00 90.28  ? 101 VAL D HG22 1 
ATOM   14241 H HG23 . VAL D 1 101 ? 13.493  31.191  58.482  1.00 90.28  ? 101 VAL D HG23 1 
ATOM   14242 N N    . LEU D 1 102 ? 11.004  33.590  54.855  1.00 83.21  ? 102 LEU D N    1 
ATOM   14243 C CA   . LEU D 1 102 ? 10.056  34.401  54.097  1.00 84.37  ? 102 LEU D CA   1 
ATOM   14244 C C    . LEU D 1 102 ? 8.786   33.591  53.856  1.00 84.69  ? 102 LEU D C    1 
ATOM   14245 O O    . LEU D 1 102 ? 8.749   32.710  52.991  1.00 85.03  ? 102 LEU D O    1 
ATOM   14246 C CB   . LEU D 1 102 ? 10.671  34.860  52.776  1.00 85.27  ? 102 LEU D CB   1 
ATOM   14247 C CG   . LEU D 1 102 ? 11.864  35.811  52.873  1.00 88.09  ? 102 LEU D CG   1 
ATOM   14248 C CD1  . LEU D 1 102 ? 12.856  35.541  51.750  1.00 82.54  ? 102 LEU D CD1  1 
ATOM   14249 C CD2  . LEU D 1 102 ? 11.418  37.265  52.854  1.00 85.79  ? 102 LEU D CD2  1 
ATOM   14250 H H    . LEU D 1 102 ? 11.406  32.996  54.380  1.00 99.85  ? 102 LEU D H    1 
ATOM   14251 H HA   . LEU D 1 102 ? 9.823   35.179  54.628  1.00 101.24 ? 102 LEU D HA   1 
ATOM   14252 H HB2  . LEU D 1 102 ? 10.972  34.073  52.296  1.00 102.33 ? 102 LEU D HB2  1 
ATOM   14253 H HB3  . LEU D 1 102 ? 9.983   35.317  52.267  1.00 102.33 ? 102 LEU D HB3  1 
ATOM   14254 H HG   . LEU D 1 102 ? 12.312  35.655  53.719  1.00 105.71 ? 102 LEU D HG   1 
ATOM   14255 H HD11 . LEU D 1 102 ? 13.590  36.172  51.818  1.00 99.05  ? 102 LEU D HD11 1 
ATOM   14256 H HD12 . LEU D 1 102 ? 13.191  34.634  51.835  1.00 99.05  ? 102 LEU D HD12 1 
ATOM   14257 H HD13 . LEU D 1 102 ? 12.405  35.648  50.898  1.00 99.05  ? 102 LEU D HD13 1 
ATOM   14258 H HD21 . LEU D 1 102 ? 12.199  37.836  52.919  1.00 102.95 ? 102 LEU D HD21 1 
ATOM   14259 H HD22 . LEU D 1 102 ? 10.948  37.440  52.024  1.00 102.95 ? 102 LEU D HD22 1 
ATOM   14260 H HD23 . LEU D 1 102 ? 10.829  37.424  53.608  1.00 102.95 ? 102 LEU D HD23 1 
ATOM   14261 N N    . ASP D 1 103 ? 7.742   33.894  54.626  1.00 84.54  ? 103 ASP D N    1 
ATOM   14262 C CA   . ASP D 1 103 ? 6.419   33.337  54.374  1.00 86.45  ? 103 ASP D CA   1 
ATOM   14263 C C    . ASP D 1 103 ? 5.756   34.117  53.241  1.00 85.83  ? 103 ASP D C    1 
ATOM   14264 O O    . ASP D 1 103 ? 5.586   35.339  53.343  1.00 89.81  ? 103 ASP D O    1 
ATOM   14265 C CB   . ASP D 1 103 ? 5.561   33.387  55.635  1.00 84.43  ? 103 ASP D CB   1 
ATOM   14266 C CG   . ASP D 1 103 ? 4.288   32.572  55.499  1.00 88.23  ? 103 ASP D CG   1 
ATOM   14267 O OD1  . ASP D 1 103 ? 3.466   32.895  54.615  1.00 88.67  ? 103 ASP D OD1  1 
ATOM   14268 O OD2  . ASP D 1 103 ? 4.119   31.595  56.262  1.00 87.85  ? 103 ASP D OD2  1 
ATOM   14269 H H    . ASP D 1 103 ? 7.776   34.423  55.303  1.00 101.46 ? 103 ASP D H    1 
ATOM   14270 H HA   . ASP D 1 103 ? 6.505   32.407  54.109  1.00 103.73 ? 103 ASP D HA   1 
ATOM   14271 H HB2  . ASP D 1 103 ? 6.070   33.031  56.380  1.00 101.32 ? 103 ASP D HB2  1 
ATOM   14272 H HB3  . ASP D 1 103 ? 5.312   34.308  55.813  1.00 101.32 ? 103 ASP D HB3  1 
ATOM   14273 N N    . VAL D 1 104 ? 5.378   33.416  52.171  1.00 84.37  ? 104 VAL D N    1 
ATOM   14274 C CA   . VAL D 1 104 ? 4.839   34.031  50.963  1.00 83.06  ? 104 VAL D CA   1 
ATOM   14275 C C    . VAL D 1 104 ? 3.408   33.554  50.761  1.00 81.09  ? 104 VAL D C    1 
ATOM   14276 O O    . VAL D 1 104 ? 3.133   32.351  50.837  1.00 81.16  ? 104 VAL D O    1 
ATOM   14277 C CB   . VAL D 1 104 ? 5.692   33.696  49.725  1.00 84.13  ? 104 VAL D CB   1 
ATOM   14278 C CG1  . VAL D 1 104 ? 5.421   34.696  48.604  1.00 81.56  ? 104 VAL D CG1  1 
ATOM   14279 C CG2  . VAL D 1 104 ? 7.172   33.665  50.077  1.00 84.21  ? 104 VAL D CG2  1 
ATOM   14280 H H    . VAL D 1 104 ? 5.426   32.558  52.123  1.00 101.25 ? 104 VAL D H    1 
ATOM   14281 H HA   . VAL D 1 104 ? 4.826   34.993  51.086  1.00 99.67  ? 104 VAL D HA   1 
ATOM   14282 H HB   . VAL D 1 104 ? 5.447   32.813  49.407  1.00 100.95 ? 104 VAL D HB   1 
ATOM   14283 H HG11 . VAL D 1 104 ? 5.965   34.465  47.835  1.00 97.88  ? 104 VAL D HG11 1 
ATOM   14284 H HG12 . VAL D 1 104 ? 4.481   34.658  48.367  1.00 97.88  ? 104 VAL D HG12 1 
ATOM   14285 H HG13 . VAL D 1 104 ? 5.648   35.587  48.913  1.00 97.88  ? 104 VAL D HG13 1 
ATOM   14286 H HG21 . VAL D 1 104 ? 7.684   33.482  49.274  1.00 101.06 ? 104 VAL D HG21 1 
ATOM   14287 H HG22 . VAL D 1 104 ? 7.427   34.526  50.443  1.00 101.06 ? 104 VAL D HG22 1 
ATOM   14288 H HG23 . VAL D 1 104 ? 7.325   32.968  50.734  1.00 101.06 ? 104 VAL D HG23 1 
ATOM   14289 N N    . ASP D 1 105 ? 2.507   34.495  50.477  1.00 82.17  ? 105 ASP D N    1 
ATOM   14290 C CA   . ASP D 1 105 ? 1.087   34.210  50.281  1.00 82.96  ? 105 ASP D CA   1 
ATOM   14291 C C    . ASP D 1 105 ? 0.808   34.150  48.784  1.00 83.54  ? 105 ASP D C    1 
ATOM   14292 O O    . ASP D 1 105 ? 0.602   35.180  48.137  1.00 85.19  ? 105 ASP D O    1 
ATOM   14293 C CB   . ASP D 1 105 ? 0.228   35.272  50.963  1.00 83.21  ? 105 ASP D CB   1 
ATOM   14294 C CG   . ASP D 1 105 ? -1.259  34.965  50.887  1.00 85.55  ? 105 ASP D CG   1 
ATOM   14295 O OD1  . ASP D 1 105 ? -1.663  34.163  50.020  1.00 85.91  ? 105 ASP D OD1  1 
ATOM   14296 O OD2  . ASP D 1 105 ? -2.028  35.531  51.696  1.00 88.30  ? 105 ASP D OD2  1 
ATOM   14297 H H    . ASP D 1 105 ? 2.700   35.328  50.392  1.00 98.60  ? 105 ASP D H    1 
ATOM   14298 H HA   . ASP D 1 105 ? 0.881   33.343  50.665  1.00 99.55  ? 105 ASP D HA   1 
ATOM   14299 H HB2  . ASP D 1 105 ? 0.475   35.325  51.900  1.00 99.85  ? 105 ASP D HB2  1 
ATOM   14300 H HB3  . ASP D 1 105 ? 0.380   36.127  50.531  1.00 99.85  ? 105 ASP D HB3  1 
ATOM   14301 N N    . VAL D 1 106 ? 0.785   32.940  48.239  1.00 84.29  ? 106 VAL D N    1 
ATOM   14302 C CA   . VAL D 1 106 ? 0.509   32.726  46.825  1.00 83.66  ? 106 VAL D CA   1 
ATOM   14303 C C    . VAL D 1 106 ? -0.981  32.486  46.637  1.00 85.12  ? 106 VAL D C    1 
ATOM   14304 O O    . VAL D 1 106 ? -1.610  31.751  47.404  1.00 83.97  ? 106 VAL D O    1 
ATOM   14305 C CB   . VAL D 1 106 ? 1.332   31.544  46.276  1.00 83.36  ? 106 VAL D CB   1 
ATOM   14306 C CG1  . VAL D 1 106 ? 0.778   31.079  44.925  1.00 87.24  ? 106 VAL D CG1  1 
ATOM   14307 C CG2  . VAL D 1 106 ? 2.797   31.930  46.153  1.00 82.19  ? 106 VAL D CG2  1 
ATOM   14308 H H    . VAL D 1 106 ? 0.929   32.213  48.676  1.00 101.15 ? 106 VAL D H    1 
ATOM   14309 H HA   . VAL D 1 106 ? 0.756   33.525  46.333  1.00 100.39 ? 106 VAL D HA   1 
ATOM   14310 H HB   . VAL D 1 106 ? 1.265   30.801  46.897  1.00 100.03 ? 106 VAL D HB   1 
ATOM   14311 H HG11 . VAL D 1 106 ? 1.350   30.379  44.573  1.00 104.69 ? 106 VAL D HG11 1 
ATOM   14312 H HG12 . VAL D 1 106 ? -0.121  30.739  45.052  1.00 104.69 ? 106 VAL D HG12 1 
ATOM   14313 H HG13 . VAL D 1 106 ? 0.763   31.833  44.314  1.00 104.69 ? 106 VAL D HG13 1 
ATOM   14314 H HG21 . VAL D 1 106 ? 3.297   31.171  45.816  1.00 98.63  ? 106 VAL D HG21 1 
ATOM   14315 H HG22 . VAL D 1 106 ? 2.876   32.677  45.539  1.00 98.63  ? 106 VAL D HG22 1 
ATOM   14316 H HG23 . VAL D 1 106 ? 3.132   32.184  47.027  1.00 98.63  ? 106 VAL D HG23 1 
ATOM   14317 N N    . ARG D 1 107 ? -1.546  33.096  45.596  1.00 88.74  ? 107 ARG D N    1 
ATOM   14318 C CA   . ARG D 1 107 ? -2.944  32.902  45.241  1.00 88.45  ? 107 ARG D CA   1 
ATOM   14319 C C    . ARG D 1 107 ? -3.046  32.701  43.736  1.00 89.73  ? 107 ARG D C    1 
ATOM   14320 O O    . ARG D 1 107 ? -2.162  33.105  42.977  1.00 86.73  ? 107 ARG D O    1 
ATOM   14321 C CB   . ARG D 1 107 ? -3.809  34.091  45.676  1.00 87.59  ? 107 ARG D CB   1 
ATOM   14322 C CG   . ARG D 1 107 ? -3.673  34.471  47.142  1.00 88.18  ? 107 ARG D CG   1 
ATOM   14323 C CD   . ARG D 1 107 ? -4.074  35.924  47.370  1.00 85.58  ? 107 ARG D CD   1 
ATOM   14324 N NE   . ARG D 1 107 ? -3.126  36.848  46.757  1.00 86.22  ? 107 ARG D NE   1 
ATOM   14325 C CZ   . ARG D 1 107 ? -1.969  37.201  47.301  1.00 86.41  ? 107 ARG D CZ   1 
ATOM   14326 N NH1  . ARG D 1 107 ? -1.596  36.748  48.487  1.00 91.18  ? 107 ARG D NH1  1 
ATOM   14327 N NH2  . ARG D 1 107 ? -1.169  38.034  46.641  1.00 86.33  ? 107 ARG D NH2  1 
ATOM   14328 H H    . ARG D 1 107 ? -1.130  33.636  45.071  1.00 106.49 ? 107 ARG D H    1 
ATOM   14329 H HA   . ARG D 1 107 ? -3.283  32.107  45.681  1.00 106.14 ? 107 ARG D HA   1 
ATOM   14330 H HB2  . ARG D 1 107 ? -3.557  34.865  45.148  1.00 105.10 ? 107 ARG D HB2  1 
ATOM   14331 H HB3  . ARG D 1 107 ? -4.740  33.870  45.516  1.00 105.10 ? 107 ARG D HB3  1 
ATOM   14332 H HG2  . ARG D 1 107 ? -4.251  33.905  47.677  1.00 105.81 ? 107 ARG D HG2  1 
ATOM   14333 H HG3  . ARG D 1 107 ? -2.750  34.361  47.420  1.00 105.81 ? 107 ARG D HG3  1 
ATOM   14334 H HD2  . ARG D 1 107 ? -4.948  36.080  46.978  1.00 102.70 ? 107 ARG D HD2  1 
ATOM   14335 H HD3  . ARG D 1 107 ? -4.101  36.103  48.323  1.00 102.70 ? 107 ARG D HD3  1 
ATOM   14336 H HE   . ARG D 1 107 ? -3.331  37.186  45.994  1.00 103.47 ? 107 ARG D HE   1 
ATOM   14337 H HH11 . ARG D 1 107 ? -2.108  36.212  48.923  1.00 109.42 ? 107 ARG D HH11 1 
ATOM   14338 H HH12 . ARG D 1 107 ? -0.841  36.990  48.821  1.00 109.42 ? 107 ARG D HH12 1 
ATOM   14339 H HH21 . ARG D 1 107 ? -1.405  38.337  45.871  1.00 103.60 ? 107 ARG D HH21 1 
ATOM   14340 H HH22 . ARG D 1 107 ? -0.417  38.270  46.984  1.00 103.60 ? 107 ARG D HH22 1 
ATOM   14341 N N    . ASN D 1 108 ? -4.137  32.067  43.310  1.00 90.36  ? 108 ASN D N    1 
ATOM   14342 C CA   . ASN D 1 108 ? -4.371  31.845  41.890  1.00 91.82  ? 108 ASN D CA   1 
ATOM   14343 C C    . ASN D 1 108 ? -4.819  33.140  41.226  1.00 93.27  ? 108 ASN D C    1 
ATOM   14344 O O    . ASN D 1 108 ? -5.549  33.939  41.819  1.00 93.00  ? 108 ASN D O    1 
ATOM   14345 C CB   . ASN D 1 108 ? -5.421  30.757  41.671  1.00 93.47  ? 108 ASN D CB   1 
ATOM   14346 C CG   . ASN D 1 108 ? -5.379  30.182  40.259  1.00 97.17  ? 108 ASN D CG   1 
ATOM   14347 O OD1  . ASN D 1 108 ? -6.330  30.326  39.489  1.00 96.44  ? 108 ASN D OD1  1 
ATOM   14348 N ND2  . ASN D 1 108 ? -4.272  29.528  39.913  1.00 92.58  ? 108 ASN D ND2  1 
ATOM   14349 H H    . ASN D 1 108 ? -4.753  31.758  43.824  1.00 108.43 ? 108 ASN D H    1 
ATOM   14350 H HA   . ASN D 1 108 ? -3.547  31.548  41.473  1.00 110.18 ? 108 ASN D HA   1 
ATOM   14351 H HB2  . ASN D 1 108 ? -5.262  30.033  42.296  1.00 112.16 ? 108 ASN D HB2  1 
ATOM   14352 H HB3  . ASN D 1 108 ? -6.303  31.134  41.816  1.00 112.16 ? 108 ASN D HB3  1 
ATOM   14353 H HD21 . ASN D 1 108 ? -3.626  29.448  40.476  1.00 111.09 ? 108 ASN D HD21 1 
ATOM   14354 H HD22 . ASN D 1 108 ? -4.202  29.186  39.127  1.00 111.09 ? 108 ASN D HD22 1 
ATOM   14355 N N    . ASP D 1 109 ? -4.376  33.342  39.985  1.00 92.60  ? 109 ASP D N    1 
ATOM   14356 C CA   . ASP D 1 109 ? -4.641  34.568  39.240  1.00 94.58  ? 109 ASP D CA   1 
ATOM   14357 C C    . ASP D 1 109 ? -5.116  34.194  37.834  1.00 95.06  ? 109 ASP D C    1 
ATOM   14358 O O    . ASP D 1 109 ? -4.406  34.390  36.847  1.00 95.46  ? 109 ASP D O    1 
ATOM   14359 C CB   . ASP D 1 109 ? -3.396  35.458  39.199  1.00 93.61  ? 109 ASP D CB   1 
ATOM   14360 C CG   . ASP D 1 109 ? -3.671  36.821  38.599  1.00 92.81  ? 109 ASP D CG   1 
ATOM   14361 O OD1  . ASP D 1 109 ? -4.853  37.221  38.546  1.00 93.61  ? 109 ASP D OD1  1 
ATOM   14362 O OD2  . ASP D 1 109 ? -2.701  37.493  38.183  1.00 91.08  ? 109 ASP D OD2  1 
ATOM   14363 H H    . ASP D 1 109 ? -3.910  32.768  39.545  1.00 111.12 ? 109 ASP D H    1 
ATOM   14364 H HA   . ASP D 1 109 ? -5.356  35.059  39.675  1.00 113.49 ? 109 ASP D HA   1 
ATOM   14365 H HB2  . ASP D 1 109 ? -3.071  35.588  40.103  1.00 112.33 ? 109 ASP D HB2  1 
ATOM   14366 H HB3  . ASP D 1 109 ? -2.715  35.025  38.661  1.00 112.33 ? 109 ASP D HB3  1 
ATOM   14367 N N    . GLY D 1 110 ? -6.325  33.643  37.753  1.00 95.66  ? 110 GLY D N    1 
ATOM   14368 C CA   . GLY D 1 110 ? -6.930  33.336  36.474  1.00 97.43  ? 110 GLY D CA   1 
ATOM   14369 C C    . GLY D 1 110 ? -6.730  31.911  36.007  1.00 98.56  ? 110 GLY D C    1 
ATOM   14370 O O    . GLY D 1 110 ? -7.677  31.118  35.991  1.00 102.42 ? 110 GLY D O    1 
ATOM   14371 H H    . GLY D 1 110 ? -6.813  33.439  38.431  1.00 114.79 ? 110 GLY D H    1 
ATOM   14372 H HA2  . GLY D 1 110 ? -7.885  33.496  36.534  1.00 116.92 ? 110 GLY D HA2  1 
ATOM   14373 H HA3  . GLY D 1 110 ? -6.553  33.923  35.801  1.00 116.92 ? 110 GLY D HA3  1 
ATOM   14374 N N    . ALA D 1 111 ? -5.505  31.577  35.616  1.00 99.11  ? 111 ALA D N    1 
ATOM   14375 C CA   . ALA D 1 111 ? -5.164  30.265  35.089  1.00 98.24  ? 111 ALA D CA   1 
ATOM   14376 C C    . ALA D 1 111 ? -4.207  29.553  36.041  1.00 97.05  ? 111 ALA D C    1 
ATOM   14377 O O    . ALA D 1 111 ? -3.797  30.097  37.071  1.00 95.66  ? 111 ALA D O    1 
ATOM   14378 C CB   . ALA D 1 111 ? -4.552  30.393  33.694  1.00 98.86  ? 111 ALA D CB   1 
ATOM   14379 H H    . ALA D 1 111 ? -4.833  32.113  35.649  1.00 118.94 ? 111 ALA D H    1 
ATOM   14380 H HA   . ALA D 1 111 ? -5.974  29.736  35.021  1.00 117.89 ? 111 ALA D HA   1 
ATOM   14381 H HB1  . ALA D 1 111 ? -4.390  29.505  33.337  1.00 118.63 ? 111 ALA D HB1  1 
ATOM   14382 H HB2  . ALA D 1 111 ? -5.170  30.872  33.120  1.00 118.63 ? 111 ALA D HB2  1 
ATOM   14383 H HB3  . ALA D 1 111 ? -3.715  30.880  33.759  1.00 118.63 ? 111 ALA D HB3  1 
ATOM   14384 N N    . LYS D 1 112 ? -3.840  28.319  35.678  1.00 93.01  ? 112 LYS D N    1 
ATOM   14385 C CA   . LYS D 1 112 ? -2.989  27.527  36.559  1.00 90.45  ? 112 LYS D CA   1 
ATOM   14386 C C    . LYS D 1 112 ? -1.554  28.041  36.580  1.00 88.78  ? 112 LYS D C    1 
ATOM   14387 O O    . LYS D 1 112 ? -0.842  27.844  37.570  1.00 89.28  ? 112 LYS D O    1 
ATOM   14388 C CB   . LYS D 1 112 ? -2.995  26.051  36.145  1.00 93.37  ? 112 LYS D CB   1 
ATOM   14389 C CG   . LYS D 1 112 ? -4.253  25.553  35.441  1.00 99.86  ? 112 LYS D CG   1 
ATOM   14390 C CD   . LYS D 1 112 ? -5.525  25.836  36.228  1.00 102.91 ? 112 LYS D CD   1 
ATOM   14391 C CE   . LYS D 1 112 ? -6.674  26.197  35.284  1.00 107.30 ? 112 LYS D CE   1 
ATOM   14392 N NZ   . LYS D 1 112 ? -7.859  26.735  36.015  1.00 108.54 ? 112 LYS D NZ   1 
ATOM   14393 H H    . LYS D 1 112 ? -4.065  27.930  34.945  1.00 111.61 ? 112 LYS D H    1 
ATOM   14394 H HA   . LYS D 1 112 ? -3.356  27.591  37.455  1.00 108.54 ? 112 LYS D HA   1 
ATOM   14395 H HB2  . LYS D 1 112 ? -2.251  25.905  35.540  1.00 112.05 ? 112 LYS D HB2  1 
ATOM   14396 H HB3  . LYS D 1 112 ? -2.883  25.513  36.944  1.00 112.05 ? 112 LYS D HB3  1 
ATOM   14397 H HG2  . LYS D 1 112 ? -4.330  25.995  34.581  1.00 119.83 ? 112 LYS D HG2  1 
ATOM   14398 H HG3  . LYS D 1 112 ? -4.186  24.593  35.316  1.00 119.83 ? 112 LYS D HG3  1 
ATOM   14399 H HD2  . LYS D 1 112 ? -5.777  25.046  36.732  1.00 123.49 ? 112 LYS D HD2  1 
ATOM   14400 H HD3  . LYS D 1 112 ? -5.375  26.580  36.831  1.00 123.49 ? 112 LYS D HD3  1 
ATOM   14401 H HE2  . LYS D 1 112 ? -6.371  26.875  34.660  1.00 128.76 ? 112 LYS D HE2  1 
ATOM   14402 H HE3  . LYS D 1 112 ? -6.952  25.402  34.802  1.00 128.76 ? 112 LYS D HE3  1 
ATOM   14403 H HZ1  . LYS D 1 112 ? -8.162  26.129  36.592  1.00 130.25 ? 112 LYS D HZ1  1 
ATOM   14404 H HZ2  . LYS D 1 112 ? -8.508  26.933  35.438  1.00 130.25 ? 112 LYS D HZ2  1 
ATOM   14405 H HZ3  . LYS D 1 112 ? -7.633  27.471  36.460  1.00 130.25 ? 112 LYS D HZ3  1 
ATOM   14406 N N    . ASN D 1 113 ? -1.105  28.683  35.505  1.00 89.33  ? 113 ASN D N    1 
ATOM   14407 C CA   . ASN D 1 113 ? 0.260   29.182  35.429  1.00 86.67  ? 113 ASN D CA   1 
ATOM   14408 C C    . ASN D 1 113 ? 0.415   30.594  35.978  1.00 86.80  ? 113 ASN D C    1 
ATOM   14409 O O    . ASN D 1 113 ? 1.550   31.045  36.170  1.00 83.82  ? 113 ASN D O    1 
ATOM   14410 C CB   . ASN D 1 113 ? 0.750   29.158  33.979  1.00 84.43  ? 113 ASN D CB   1 
ATOM   14411 C CG   . ASN D 1 113 ? -0.047  30.084  33.086  1.00 88.09  ? 113 ASN D CG   1 
ATOM   14412 O OD1  . ASN D 1 113 ? -1.266  29.958  32.975  1.00 91.99  ? 113 ASN D OD1  1 
ATOM   14413 N ND2  . ASN D 1 113 ? 0.636   31.026  32.450  1.00 88.01  ? 113 ASN D ND2  1 
ATOM   14414 H H    . ASN D 1 113 ? -1.577  28.842  34.803  1.00 107.20 ? 113 ASN D H    1 
ATOM   14415 H HA   . ASN D 1 113 ? 0.828   28.594  35.951  1.00 104.01 ? 113 ASN D HA   1 
ATOM   14416 H HB2  . ASN D 1 113 ? 1.678   29.439  33.953  1.00 101.31 ? 113 ASN D HB2  1 
ATOM   14417 H HB3  . ASN D 1 113 ? 0.667   28.257  33.630  1.00 101.31 ? 113 ASN D HB3  1 
ATOM   14418 H HD21 . ASN D 1 113 ? 1.487   31.086  32.556  1.00 105.60 ? 113 ASN D HD21 1 
ATOM   14419 H HD22 . ASN D 1 113 ? 0.227   31.576  31.931  1.00 105.60 ? 113 ASN D HD22 1 
ATOM   14420 N N    . LYS D 1 114 ? -0.685  31.297  36.232  1.00 90.09  ? 114 LYS D N    1 
ATOM   14421 C CA   . LYS D 1 114 ? -0.649  32.677  36.698  1.00 88.87  ? 114 LYS D CA   1 
ATOM   14422 C C    . LYS D 1 114 ? -1.004  32.734  38.179  1.00 88.31  ? 114 LYS D C    1 
ATOM   14423 O O    . LYS D 1 114 ? -1.903  32.026  38.645  1.00 91.15  ? 114 LYS D O    1 
ATOM   14424 C CB   . LYS D 1 114 ? -1.610  33.550  35.884  1.00 89.86  ? 114 LYS D CB   1 
ATOM   14425 C CG   . LYS D 1 114 ? -1.241  33.663  34.407  1.00 87.64  ? 114 LYS D CG   1 
ATOM   14426 C CD   . LYS D 1 114 ? -2.469  33.859  33.517  1.00 95.05  ? 114 LYS D CD   1 
ATOM   14427 C CE   . LYS D 1 114 ? -2.378  33.010  32.246  1.00 102.71 ? 114 LYS D CE   1 
ATOM   14428 N NZ   . LYS D 1 114 ? -3.446  33.328  31.251  1.00 106.75 ? 114 LYS D NZ   1 
ATOM   14429 H H    . LYS D 1 114 ? -1.482  30.988  36.139  1.00 108.11 ? 114 LYS D H    1 
ATOM   14430 H HA   . LYS D 1 114 ? 0.245   33.036  36.590  1.00 106.65 ? 114 LYS D HA   1 
ATOM   14431 H HB2  . LYS D 1 114 ? -2.500  33.168  35.938  1.00 107.84 ? 114 LYS D HB2  1 
ATOM   14432 H HB3  . LYS D 1 114 ? -1.610  34.445  36.258  1.00 107.84 ? 114 LYS D HB3  1 
ATOM   14433 H HG2  . LYS D 1 114 ? -0.653  34.424  34.283  1.00 105.17 ? 114 LYS D HG2  1 
ATOM   14434 H HG3  . LYS D 1 114 ? -0.792  32.849  34.128  1.00 105.17 ? 114 LYS D HG3  1 
ATOM   14435 H HD2  . LYS D 1 114 ? -3.265  33.595  34.004  1.00 114.06 ? 114 LYS D HD2  1 
ATOM   14436 H HD3  . LYS D 1 114 ? -2.532  34.792  33.257  1.00 114.06 ? 114 LYS D HD3  1 
ATOM   14437 H HE2  . LYS D 1 114 ? -1.519  33.167  31.822  1.00 123.26 ? 114 LYS D HE2  1 
ATOM   14438 H HE3  . LYS D 1 114 ? -2.462  32.074  32.486  1.00 123.26 ? 114 LYS D HE3  1 
ATOM   14439 H HZ1  . LYS D 1 114 ? -3.380  34.177  30.993  1.00 128.09 ? 114 LYS D HZ1  1 
ATOM   14440 H HZ2  . LYS D 1 114 ? -3.364  32.802  30.537  1.00 128.09 ? 114 LYS D HZ2  1 
ATOM   14441 H HZ3  . LYS D 1 114 ? -4.249  33.198  31.614  1.00 128.09 ? 114 LYS D HZ3  1 
ATOM   14442 N N    . PHE D 1 115 ? -0.292  33.583  38.915  1.00 87.32  ? 115 PHE D N    1 
ATOM   14443 C CA   . PHE D 1 115 ? -0.411  33.631  40.363  1.00 88.22  ? 115 PHE D CA   1 
ATOM   14444 C C    . PHE D 1 115 ? -0.347  35.075  40.844  1.00 87.43  ? 115 PHE D C    1 
ATOM   14445 O O    . PHE D 1 115 ? -0.091  36.004  40.077  1.00 88.02  ? 115 PHE D O    1 
ATOM   14446 C CB   . PHE D 1 115 ? 0.702   32.815  41.044  1.00 84.46  ? 115 PHE D CB   1 
ATOM   14447 C CG   . PHE D 1 115 ? 0.605   31.333  40.817  1.00 83.37  ? 115 PHE D CG   1 
ATOM   14448 C CD1  . PHE D 1 115 ? -0.331  30.576  41.496  1.00 85.26  ? 115 PHE D CD1  1 
ATOM   14449 C CD2  . PHE D 1 115 ? 1.457   30.696  39.932  1.00 86.96  ? 115 PHE D CD2  1 
ATOM   14450 C CE1  . PHE D 1 115 ? -0.423  29.215  41.294  1.00 85.77  ? 115 PHE D CE1  1 
ATOM   14451 C CE2  . PHE D 1 115 ? 1.368   29.330  39.723  1.00 86.71  ? 115 PHE D CE2  1 
ATOM   14452 C CZ   . PHE D 1 115 ? 0.428   28.590  40.405  1.00 85.12  ? 115 PHE D CZ   1 
ATOM   14453 H H    . PHE D 1 115 ? 0.272   34.146  38.592  1.00 104.79 ? 115 PHE D H    1 
ATOM   14454 H HA   . PHE D 1 115 ? -1.275  33.267  40.608  1.00 105.86 ? 115 PHE D HA   1 
ATOM   14455 H HB2  . PHE D 1 115 ? 1.559   33.111  40.699  1.00 101.35 ? 115 PHE D HB2  1 
ATOM   14456 H HB3  . PHE D 1 115 ? 0.658   32.970  42.001  1.00 101.35 ? 115 PHE D HB3  1 
ATOM   14457 H HD1  . PHE D 1 115 ? -0.907  30.990  42.098  1.00 102.31 ? 115 PHE D HD1  1 
ATOM   14458 H HD2  . PHE D 1 115 ? 2.096   31.191  39.473  1.00 104.35 ? 115 PHE D HD2  1 
ATOM   14459 H HE1  . PHE D 1 115 ? -1.059  28.718  41.756  1.00 102.92 ? 115 PHE D HE1  1 
ATOM   14460 H HE2  . PHE D 1 115 ? 1.942   28.913  39.123  1.00 104.04 ? 115 PHE D HE2  1 
ATOM   14461 H HZ   . PHE D 1 115 ? 0.367   27.672  40.268  1.00 102.14 ? 115 PHE D HZ   1 
ATOM   14462 N N    . LEU D 1 116 ? -0.594  35.253  42.138  1.00 89.96  ? 116 LEU D N    1 
ATOM   14463 C CA   . LEU D 1 116 ? -0.400  36.530  42.819  1.00 90.89  ? 116 LEU D CA   1 
ATOM   14464 C C    . LEU D 1 116 ? 0.293   36.216  44.136  1.00 91.58  ? 116 LEU D C    1 
ATOM   14465 O O    . LEU D 1 116 ? -0.279  35.519  44.980  1.00 93.30  ? 116 LEU D O    1 
ATOM   14466 C CB   . LEU D 1 116 ? -1.724  37.253  43.060  1.00 90.88  ? 116 LEU D CB   1 
ATOM   14467 C CG   . LEU D 1 116 ? -2.333  38.055  41.911  1.00 92.23  ? 116 LEU D CG   1 
ATOM   14468 C CD1  . LEU D 1 116 ? -3.459  38.954  42.433  1.00 91.40  ? 116 LEU D CD1  1 
ATOM   14469 C CD2  . LEU D 1 116 ? -1.306  38.901  41.178  1.00 94.33  ? 116 LEU D CD2  1 
ATOM   14470 H H    . LEU D 1 116 ? -0.881  34.631  42.658  1.00 107.95 ? 116 LEU D H    1 
ATOM   14471 H HA   . LEU D 1 116 ? 0.154   37.120  42.285  1.00 109.07 ? 116 LEU D HA   1 
ATOM   14472 H HB2  . LEU D 1 116 ? -2.382  36.585  43.310  1.00 109.06 ? 116 LEU D HB2  1 
ATOM   14473 H HB3  . LEU D 1 116 ? -1.590  37.875  43.791  1.00 109.06 ? 116 LEU D HB3  1 
ATOM   14474 H HG   . LEU D 1 116 ? -2.688  37.419  41.270  1.00 110.68 ? 116 LEU D HG   1 
ATOM   14475 H HD11 . LEU D 1 116 ? -3.829  39.459  41.693  1.00 109.68 ? 116 LEU D HD11 1 
ATOM   14476 H HD12 . LEU D 1 116 ? -4.147  38.399  42.832  1.00 109.68 ? 116 LEU D HD12 1 
ATOM   14477 H HD13 . LEU D 1 116 ? -3.096  39.560  43.098  1.00 109.68 ? 116 LEU D HD13 1 
ATOM   14478 H HD21 . LEU D 1 116 ? -1.758  39.430  40.502  1.00 113.20 ? 116 LEU D HD21 1 
ATOM   14479 H HD22 . LEU D 1 116 ? -0.866  39.485  41.816  1.00 113.20 ? 116 LEU D HD22 1 
ATOM   14480 H HD23 . LEU D 1 116 ? -0.655  38.316  40.761  1.00 113.20 ? 116 LEU D HD23 1 
ATOM   14481 N N    . ALA D 1 117 ? 1.520   36.710  44.311  1.00 87.73  ? 117 ALA D N    1 
ATOM   14482 C CA   . ALA D 1 117 ? 2.361   36.337  45.443  1.00 87.11  ? 117 ALA D CA   1 
ATOM   14483 C C    . ALA D 1 117 ? 2.728   37.569  46.256  1.00 85.10  ? 117 ALA D C    1 
ATOM   14484 O O    . ALA D 1 117 ? 3.334   38.507  45.729  1.00 83.29  ? 117 ALA D O    1 
ATOM   14485 C CB   . ALA D 1 117 ? 3.628   35.619  44.967  1.00 82.65  ? 117 ALA D CB   1 
ATOM   14486 H H    . ALA D 1 117 ? 1.890   37.272  43.776  1.00 105.28 ? 117 ALA D H    1 
ATOM   14487 H HA   . ALA D 1 117 ? 1.854   35.745  46.021  1.00 104.53 ? 117 ALA D HA   1 
ATOM   14488 H HB1  . ALA D 1 117 ? 4.168   35.387  45.739  1.00 99.17  ? 117 ALA D HB1  1 
ATOM   14489 H HB2  . ALA D 1 117 ? 3.374   34.814  44.488  1.00 99.17  ? 117 ALA D HB2  1 
ATOM   14490 H HB3  . ALA D 1 117 ? 4.125   36.210  44.381  1.00 99.17  ? 117 ALA D HB3  1 
ATOM   14491 N N    . LYS D 1 118 ? 2.381   37.548  47.539  1.00 87.10  ? 118 LYS D N    1 
ATOM   14492 C CA   . LYS D 1 118 ? 2.719   38.608  48.478  1.00 83.91  ? 118 LYS D CA   1 
ATOM   14493 C C    . LYS D 1 118 ? 3.887   38.168  49.353  1.00 83.06  ? 118 LYS D C    1 
ATOM   14494 O O    . LYS D 1 118 ? 3.905   37.042  49.858  1.00 83.99  ? 118 LYS D O    1 
ATOM   14495 C CB   . LYS D 1 118 ? 1.510   38.956  49.348  1.00 85.22  ? 118 LYS D CB   1 
ATOM   14496 C CG   . LYS D 1 118 ? 1.791   40.027  50.390  1.00 88.99  ? 118 LYS D CG   1 
ATOM   14497 C CD   . LYS D 1 118 ? 0.503   40.548  51.011  1.00 92.32  ? 118 LYS D CD   1 
ATOM   14498 C CE   . LYS D 1 118 ? -0.109  39.593  52.027  1.00 95.44  ? 118 LYS D CE   1 
ATOM   14499 N NZ   . LYS D 1 118 ? -1.325  40.228  52.614  1.00 100.64 ? 118 LYS D NZ   1 
ATOM   14500 H H    . LYS D 1 118 ? 1.934   36.908  47.901  1.00 104.52 ? 118 LYS D H    1 
ATOM   14501 H HA   . LYS D 1 118 ? 2.987   39.406  47.995  1.00 100.69 ? 118 LYS D HA   1 
ATOM   14502 H HB2  . LYS D 1 118 ? 0.797   39.279  48.775  1.00 102.26 ? 118 LYS D HB2  1 
ATOM   14503 H HB3  . LYS D 1 118 ? 1.223   38.156  49.815  1.00 102.26 ? 118 LYS D HB3  1 
ATOM   14504 H HG2  . LYS D 1 118 ? 2.341   39.653  51.097  1.00 106.78 ? 118 LYS D HG2  1 
ATOM   14505 H HG3  . LYS D 1 118 ? 2.251   40.772  49.971  1.00 106.78 ? 118 LYS D HG3  1 
ATOM   14506 H HD2  . LYS D 1 118 ? 0.689   41.385  51.465  1.00 110.79 ? 118 LYS D HD2  1 
ATOM   14507 H HD3  . LYS D 1 118 ? -0.149  40.690  50.307  1.00 110.79 ? 118 LYS D HD3  1 
ATOM   14508 H HE2  . LYS D 1 118 ? -0.364  38.765  51.591  1.00 114.53 ? 118 LYS D HE2  1 
ATOM   14509 H HE3  . LYS D 1 118 ? 0.527   39.411  52.736  1.00 114.53 ? 118 LYS D HE3  1 
ATOM   14510 H HZ1  . LYS D 1 118 ? -1.666  39.704  53.248  1.00 120.77 ? 118 LYS D HZ1  1 
ATOM   14511 H HZ2  . LYS D 1 118 ? -1.114  41.015  52.973  1.00 120.77 ? 118 LYS D HZ2  1 
ATOM   14512 H HZ3  . LYS D 1 118 ? -1.938  40.354  51.982  1.00 120.77 ? 118 LYS D HZ3  1 
ATOM   14513 N N    . ILE D 1 119 ? 4.864   39.063  49.536  1.00 84.33  ? 119 ILE D N    1 
ATOM   14514 C CA   . ILE D 1 119 ? 6.068   38.762  50.302  1.00 83.67  ? 119 ILE D CA   1 
ATOM   14515 C C    . ILE D 1 119 ? 6.399   39.944  51.203  1.00 88.86  ? 119 ILE D C    1 
ATOM   14516 O O    . ILE D 1 119 ? 6.021   41.084  50.939  1.00 91.53  ? 119 ILE D O    1 
ATOM   14517 C CB   . ILE D 1 119 ? 7.265   38.434  49.377  1.00 83.62  ? 119 ILE D CB   1 
ATOM   14518 C CG1  . ILE D 1 119 ? 8.452   37.922  50.189  1.00 82.96  ? 119 ILE D CG1  1 
ATOM   14519 C CG2  . ILE D 1 119 ? 7.666   39.659  48.557  1.00 82.47  ? 119 ILE D CG2  1 
ATOM   14520 C CD1  . ILE D 1 119 ? 9.578   37.372  49.338  1.00 82.68  ? 119 ILE D CD1  1 
ATOM   14521 H H    . ILE D 1 119 ? 4.848   39.863  49.220  1.00 101.19 ? 119 ILE D H    1 
ATOM   14522 H HA   . ILE D 1 119 ? 5.901   37.997  50.875  1.00 100.40 ? 119 ILE D HA   1 
ATOM   14523 H HB   . ILE D 1 119 ? 6.987   37.733  48.766  1.00 100.35 ? 119 ILE D HB   1 
ATOM   14524 H HG12 . ILE D 1 119 ? 8.809   38.655  50.715  1.00 99.55  ? 119 ILE D HG12 1 
ATOM   14525 H HG13 . ILE D 1 119 ? 8.147   37.211  50.774  1.00 99.55  ? 119 ILE D HG13 1 
ATOM   14526 H HG21 . ILE D 1 119 ? 8.264   39.381  47.845  1.00 98.96  ? 119 ILE D HG21 1 
ATOM   14527 H HG22 . ILE D 1 119 ? 6.868   40.062  48.181  1.00 98.96  ? 119 ILE D HG22 1 
ATOM   14528 H HG23 . ILE D 1 119 ? 8.116   40.294  49.137  1.00 98.96  ? 119 ILE D HG23 1 
ATOM   14529 H HD11 . ILE D 1 119 ? 10.249  36.979  49.918  1.00 99.21  ? 119 ILE D HD11 1 
ATOM   14530 H HD12 . ILE D 1 119 ? 9.221   36.696  48.741  1.00 99.21  ? 119 ILE D HD12 1 
ATOM   14531 H HD13 . ILE D 1 119 ? 9.968   38.096  48.823  1.00 99.21  ? 119 ILE D HD13 1 
ATOM   14532 N N    . LYS D 1 120 ? 7.105   39.647  52.295  1.00 89.08  ? 120 LYS D N    1 
ATOM   14533 C CA   . LYS D 1 120 ? 7.586   40.669  53.222  1.00 90.28  ? 120 LYS D CA   1 
ATOM   14534 C C    . LYS D 1 120 ? 8.956   41.154  52.763  1.00 88.99  ? 120 LYS D C    1 
ATOM   14535 O O    . LYS D 1 120 ? 9.837   40.343  52.458  1.00 86.46  ? 120 LYS D O    1 
ATOM   14536 C CB   . LYS D 1 120 ? 7.665   40.115  54.647  1.00 92.57  ? 120 LYS D CB   1 
ATOM   14537 C CG   . LYS D 1 120 ? 8.187   41.100  55.690  1.00 97.61  ? 120 LYS D CG   1 
ATOM   14538 C CD   . LYS D 1 120 ? 9.241   40.463  56.602  1.00 100.49 ? 120 LYS D CD   1 
ATOM   14539 C CE   . LYS D 1 120 ? 10.462  39.980  55.815  1.00 99.08  ? 120 LYS D CE   1 
ATOM   14540 N NZ   . LYS D 1 120 ? 11.707  39.963  56.643  1.00 99.12  ? 120 LYS D NZ   1 
ATOM   14541 H H    . LYS D 1 120 ? 7.321   38.847  52.525  1.00 106.90 ? 120 LYS D H    1 
ATOM   14542 H HA   . LYS D 1 120 ? 6.973   41.421  53.228  1.00 108.34 ? 120 LYS D HA   1 
ATOM   14543 H HB2  . LYS D 1 120 ? 6.775   39.845  54.922  1.00 111.09 ? 120 LYS D HB2  1 
ATOM   14544 H HB3  . LYS D 1 120 ? 8.260   39.349  54.647  1.00 111.09 ? 120 LYS D HB3  1 
ATOM   14545 H HG2  . LYS D 1 120 ? 8.594   41.857  55.239  1.00 117.14 ? 120 LYS D HG2  1 
ATOM   14546 H HG3  . LYS D 1 120 ? 7.449   41.401  56.243  1.00 117.14 ? 120 LYS D HG3  1 
ATOM   14547 H HD2  . LYS D 1 120 ? 9.540   41.118  57.252  1.00 120.59 ? 120 LYS D HD2  1 
ATOM   14548 H HD3  . LYS D 1 120 ? 8.852   39.699  57.055  1.00 120.59 ? 120 LYS D HD3  1 
ATOM   14549 H HE2  . LYS D 1 120 ? 10.299  39.078  55.498  1.00 118.89 ? 120 LYS D HE2  1 
ATOM   14550 H HE3  . LYS D 1 120 ? 10.610  40.574  55.062  1.00 118.89 ? 120 LYS D HE3  1 
ATOM   14551 H HZ1  . LYS D 1 120 ? 12.392  39.671  56.157  1.00 118.94 ? 120 LYS D HZ1  1 
ATOM   14552 H HZ2  . LYS D 1 120 ? 11.599  39.424  57.343  1.00 118.94 ? 120 LYS D HZ2  1 
ATOM   14553 H HZ3  . LYS D 1 120 ? 11.889  40.784  56.935  1.00 118.94 ? 120 LYS D HZ3  1 
ATOM   14554 N N    . MET D 1 121 ? 9.132   42.471  52.712  1.00 88.08  ? 121 MET D N    1 
ATOM   14555 C CA   . MET D 1 121 ? 10.353  43.046  52.170  1.00 88.11  ? 121 MET D CA   1 
ATOM   14556 C C    . MET D 1 121 ? 11.252  43.570  53.280  1.00 87.44  ? 121 MET D C    1 
ATOM   14557 O O    . MET D 1 121 ? 10.781  43.906  54.369  1.00 88.51  ? 121 MET D O    1 
ATOM   14558 C CB   . MET D 1 121 ? 10.031  44.193  51.205  1.00 87.88  ? 121 MET D CB   1 
ATOM   14559 C CG   . MET D 1 121 ? 9.380   43.770  49.898  1.00 88.54  ? 121 MET D CG   1 
ATOM   14560 S SD   . MET D 1 121 ? 10.385  42.705  48.836  1.00 85.81  ? 121 MET D SD   1 
ATOM   14561 C CE   . MET D 1 121 ? 11.625  43.858  48.258  1.00 82.15  ? 121 MET D CE   1 
ATOM   14562 H H    . MET D 1 121 ? 8.558   43.050  52.987  1.00 105.69 ? 121 MET D H    1 
ATOM   14563 H HA   . MET D 1 121 ? 10.823  42.357  51.674  1.00 105.74 ? 121 MET D HA   1 
ATOM   14564 H HB2  . MET D 1 121 ? 9.423   44.805  51.648  1.00 105.46 ? 121 MET D HB2  1 
ATOM   14565 H HB3  . MET D 1 121 ? 10.858  44.650  50.983  1.00 105.46 ? 121 MET D HB3  1 
ATOM   14566 H HG2  . MET D 1 121 ? 8.566   43.285  50.105  1.00 106.25 ? 121 MET D HG2  1 
ATOM   14567 H HG3  . MET D 1 121 ? 9.170   44.569  49.389  1.00 106.25 ? 121 MET D HG3  1 
ATOM   14568 H HE1  . MET D 1 121 ? 12.270  43.381  47.713  1.00 98.58  ? 121 MET D HE1  1 
ATOM   14569 H HE2  . MET D 1 121 ? 11.193  44.549  47.731  1.00 98.58  ? 121 MET D HE2  1 
ATOM   14570 H HE3  . MET D 1 121 ? 12.069  44.255  49.024  1.00 98.58  ? 121 MET D HE3  1 
ATOM   14571 N N    . PRO D 1 122 ? 12.559  43.657  53.030  1.00 84.97  ? 122 PRO D N    1 
ATOM   14572 C CA   . PRO D 1 122 ? 13.459  44.228  54.038  1.00 86.84  ? 122 PRO D CA   1 
ATOM   14573 C C    . PRO D 1 122 ? 13.044  45.640  54.425  1.00 90.23  ? 122 PRO D C    1 
ATOM   14574 O O    . PRO D 1 122 ? 12.521  46.406  53.611  1.00 94.46  ? 122 PRO D O    1 
ATOM   14575 C CB   . PRO D 1 122 ? 14.832  44.215  53.347  1.00 86.40  ? 122 PRO D CB   1 
ATOM   14576 C CG   . PRO D 1 122 ? 14.560  43.964  51.899  1.00 84.36  ? 122 PRO D CG   1 
ATOM   14577 C CD   . PRO D 1 122 ? 13.292  43.166  51.849  1.00 84.31  ? 122 PRO D CD   1 
ATOM   14578 H HA   . PRO D 1 122 ? 13.485  43.667  54.829  1.00 104.21 ? 122 PRO D HA   1 
ATOM   14579 H HB2  . PRO D 1 122 ? 15.268  45.073  53.471  1.00 103.68 ? 122 PRO D HB2  1 
ATOM   14580 H HB3  . PRO D 1 122 ? 15.379  43.507  53.722  1.00 103.68 ? 122 PRO D HB3  1 
ATOM   14581 H HG2  . PRO D 1 122 ? 14.453  44.809  51.435  1.00 101.23 ? 122 PRO D HG2  1 
ATOM   14582 H HG3  . PRO D 1 122 ? 15.295  43.464  51.510  1.00 101.23 ? 122 PRO D HG3  1 
ATOM   14583 H HD2  . PRO D 1 122 ? 12.799  43.347  51.034  1.00 101.17 ? 122 PRO D HD2  1 
ATOM   14584 H HD3  . PRO D 1 122 ? 13.475  42.217  51.923  1.00 101.17 ? 122 PRO D HD3  1 
ATOM   14585 N N    . LYS D 1 123 ? 13.282  45.975  55.686  1.00 87.08  ? 123 LYS D N    1 
ATOM   14586 C CA   . LYS D 1 123 ? 12.969  47.300  56.195  1.00 93.12  ? 123 LYS D CA   1 
ATOM   14587 C C    . LYS D 1 123 ? 14.070  48.283  55.814  1.00 94.77  ? 123 LYS D C    1 
ATOM   14588 O O    . LYS D 1 123 ? 15.238  47.911  55.658  1.00 93.32  ? 123 LYS D O    1 
ATOM   14589 C CB   . LYS D 1 123 ? 12.797  47.262  57.716  1.00 90.52  ? 123 LYS D CB   1 
ATOM   14590 C CG   . LYS D 1 123 ? 14.099  47.367  58.498  1.00 92.11  ? 123 LYS D CG   1 
ATOM   14591 C CD   . LYS D 1 123 ? 14.014  46.731  59.893  1.00 95.43  ? 123 LYS D CD   1 
ATOM   14592 C CE   . LYS D 1 123 ? 12.615  46.811  60.499  1.00 96.91  ? 123 LYS D CE   1 
ATOM   14593 N NZ   . LYS D 1 123 ? 12.647  46.763  61.992  1.00 102.73 ? 123 LYS D NZ   1 
ATOM   14594 H H    . LYS D 1 123 ? 13.627  45.448  56.272  1.00 104.50 ? 123 LYS D H    1 
ATOM   14595 H HA   . LYS D 1 123 ? 12.136  47.613  55.810  1.00 111.74 ? 123 LYS D HA   1 
ATOM   14596 H HB2  . LYS D 1 123 ? 12.235  48.006  57.982  1.00 108.63 ? 123 LYS D HB2  1 
ATOM   14597 H HB3  . LYS D 1 123 ? 12.376  46.423  57.959  1.00 108.63 ? 123 LYS D HB3  1 
ATOM   14598 H HG2  . LYS D 1 123 ? 14.801  46.912  58.005  1.00 110.53 ? 123 LYS D HG2  1 
ATOM   14599 H HG3  . LYS D 1 123 ? 14.326  48.303  58.610  1.00 110.53 ? 123 LYS D HG3  1 
ATOM   14600 H HD2  . LYS D 1 123 ? 14.259  45.795  59.830  1.00 114.51 ? 123 LYS D HD2  1 
ATOM   14601 H HD3  . LYS D 1 123 ? 14.624  47.194  60.489  1.00 114.51 ? 123 LYS D HD3  1 
ATOM   14602 H HE2  . LYS D 1 123 ? 12.198  47.645  60.232  1.00 116.30 ? 123 LYS D HE2  1 
ATOM   14603 H HE3  . LYS D 1 123 ? 12.087  46.060  60.183  1.00 116.30 ? 123 LYS D HE3  1 
ATOM   14604 H HZ1  . LYS D 1 123 ? 11.819  46.801  62.316  1.00 123.27 ? 123 LYS D HZ1  1 
ATOM   14605 H HZ2  . LYS D 1 123 ? 13.029  46.006  62.264  1.00 123.27 ? 123 LYS D HZ2  1 
ATOM   14606 H HZ3  . LYS D 1 123 ? 13.113  47.452  62.309  1.00 123.27 ? 123 LYS D HZ3  1 
ATOM   14607 N N    . PHE D 1 124 ? 13.686  49.549  55.658  1.00 97.69  ? 124 PHE D N    1 
ATOM   14608 C CA   . PHE D 1 124 ? 14.646  50.576  55.283  1.00 96.08  ? 124 PHE D CA   1 
ATOM   14609 C C    . PHE D 1 124 ? 15.559  50.890  56.460  1.00 97.37  ? 124 PHE D C    1 
ATOM   14610 O O    . PHE D 1 124 ? 15.196  50.701  57.622  1.00 101.36 ? 124 PHE D O    1 
ATOM   14611 C CB   . PHE D 1 124 ? 13.932  51.846  54.806  1.00 97.82  ? 124 PHE D CB   1 
ATOM   14612 C CG   . PHE D 1 124 ? 13.190  52.579  55.887  1.00 97.30  ? 124 PHE D CG   1 
ATOM   14613 C CD1  . PHE D 1 124 ? 13.837  53.513  56.682  1.00 100.28 ? 124 PHE D CD1  1 
ATOM   14614 C CD2  . PHE D 1 124 ? 11.843  52.342  56.104  1.00 99.03  ? 124 PHE D CD2  1 
ATOM   14615 C CE1  . PHE D 1 124 ? 13.158  54.189  57.679  1.00 98.36  ? 124 PHE D CE1  1 
ATOM   14616 C CE2  . PHE D 1 124 ? 11.157  53.016  57.100  1.00 100.49 ? 124 PHE D CE2  1 
ATOM   14617 C CZ   . PHE D 1 124 ? 11.815  53.941  57.888  1.00 100.97 ? 124 PHE D CZ   1 
ATOM   14618 H H    . PHE D 1 124 ? 12.881  49.834  55.763  1.00 117.23 ? 124 PHE D H    1 
ATOM   14619 H HA   . PHE D 1 124 ? 15.191  50.260  54.545  1.00 115.29 ? 124 PHE D HA   1 
ATOM   14620 H HB2  . PHE D 1 124 ? 14.593  52.454  54.439  1.00 117.39 ? 124 PHE D HB2  1 
ATOM   14621 H HB3  . PHE D 1 124 ? 13.289  51.602  54.122  1.00 117.39 ? 124 PHE D HB3  1 
ATOM   14622 H HD1  . PHE D 1 124 ? 14.740  53.687  56.543  1.00 120.34 ? 124 PHE D HD1  1 
ATOM   14623 H HD2  . PHE D 1 124 ? 11.394  51.723  55.575  1.00 118.84 ? 124 PHE D HD2  1 
ATOM   14624 H HE1  . PHE D 1 124 ? 13.604  54.809  58.209  1.00 118.03 ? 124 PHE D HE1  1 
ATOM   14625 H HE2  . PHE D 1 124 ? 10.253  52.847  57.238  1.00 120.59 ? 124 PHE D HE2  1 
ATOM   14626 H HZ   . PHE D 1 124 ? 11.355  54.395  58.557  1.00 121.16 ? 124 PHE D HZ   1 
ATOM   14627 N N    . LEU D 1 125 ? 16.760  51.375  56.149  1.00 98.33  ? 125 LEU D N    1 
ATOM   14628 C CA   . LEU D 1 125 ? 17.706  51.779  57.179  1.00 100.83 ? 125 LEU D CA   1 
ATOM   14629 C C    . LEU D 1 125 ? 17.735  53.285  57.407  1.00 97.87  ? 125 LEU D C    1 
ATOM   14630 O O    . LEU D 1 125 ? 18.140  53.722  58.490  1.00 100.18 ? 125 LEU D O    1 
ATOM   14631 C CB   . LEU D 1 125 ? 19.117  51.301  56.824  1.00 100.39 ? 125 LEU D CB   1 
ATOM   14632 C CG   . LEU D 1 125 ? 19.293  49.814  56.525  1.00 101.46 ? 125 LEU D CG   1 
ATOM   14633 C CD1  . LEU D 1 125 ? 20.700  49.372  56.945  1.00 103.42 ? 125 LEU D CD1  1 
ATOM   14634 C CD2  . LEU D 1 125 ? 18.243  48.948  57.201  1.00 99.60  ? 125 LEU D CD2  1 
ATOM   14635 H H    . LEU D 1 125 ? 17.049  51.479  55.345  1.00 118.00 ? 125 LEU D H    1 
ATOM   14636 H HA   . LEU D 1 125 ? 17.453  51.356  58.015  1.00 120.99 ? 125 LEU D HA   1 
ATOM   14637 H HB2  . LEU D 1 125 ? 19.405  51.784  56.033  1.00 120.47 ? 125 LEU D HB2  1 
ATOM   14638 H HB3  . LEU D 1 125 ? 19.699  51.510  57.570  1.00 120.47 ? 125 LEU D HB3  1 
ATOM   14639 H HG   . LEU D 1 125 ? 19.179  49.683  55.571  1.00 121.76 ? 125 LEU D HG   1 
ATOM   14640 H HD11 . LEU D 1 125 ? 20.821  48.439  56.710  1.00 124.11 ? 125 LEU D HD11 1 
ATOM   14641 H HD12 . LEU D 1 125 ? 21.354  49.917  56.480  1.00 124.11 ? 125 LEU D HD12 1 
ATOM   14642 H HD13 . LEU D 1 125 ? 20.794  49.487  57.903  1.00 124.11 ? 125 LEU D HD13 1 
ATOM   14643 H HD21 . LEU D 1 125 ? 18.552  48.029  57.212  1.00 119.52 ? 125 LEU D HD21 1 
ATOM   14644 H HD22 . LEU D 1 125 ? 18.111  49.264  58.108  1.00 119.52 ? 125 LEU D HD22 1 
ATOM   14645 H HD23 . LEU D 1 125 ? 17.413  49.013  56.703  1.00 119.52 ? 125 LEU D HD23 1 
ATOM   14646 N N    . SER D 1 126 ? 17.330  54.083  56.420  1.00 100.76 ? 126 SER D N    1 
ATOM   14647 C CA   . SER D 1 126 ? 17.238  55.528  56.571  1.00 99.98  ? 126 SER D CA   1 
ATOM   14648 C C    . SER D 1 126 ? 16.170  56.051  55.622  1.00 97.85  ? 126 SER D C    1 
ATOM   14649 O O    . SER D 1 126 ? 15.932  55.481  54.556  1.00 98.03  ? 126 SER D O    1 
ATOM   14650 C CB   . SER D 1 126 ? 18.573  56.225  56.284  1.00 99.43  ? 126 SER D CB   1 
ATOM   14651 O OG   . SER D 1 126 ? 19.586  55.783  57.168  1.00 104.73 ? 126 SER D OG   1 
ATOM   14652 H H    . SER D 1 126 ? 17.099  53.804  55.640  1.00 120.91 ? 126 SER D H    1 
ATOM   14653 H HA   . SER D 1 126 ? 16.980  55.736  57.483  1.00 119.97 ? 126 SER D HA   1 
ATOM   14654 H HB2  . SER D 1 126 ? 18.842  56.025  55.374  1.00 119.32 ? 126 SER D HB2  1 
ATOM   14655 H HB3  . SER D 1 126 ? 18.457  57.182  56.393  1.00 119.32 ? 126 SER D HB3  1 
ATOM   14656 H HG   . SER D 1 126 ? 19.360  55.934  57.963  1.00 125.68 ? 126 SER D HG   1 
ATOM   14657 N N    . LEU D 1 127 ? 15.529  57.144  56.024  1.00 97.62  ? 127 LEU D N    1 
ATOM   14658 C CA   . LEU D 1 127 ? 14.513  57.806  55.213  1.00 100.11 ? 127 LEU D CA   1 
ATOM   14659 C C    . LEU D 1 127 ? 14.697  59.306  55.379  1.00 102.58 ? 127 LEU D C    1 
ATOM   14660 O O    . LEU D 1 127 ? 14.552  59.834  56.490  1.00 100.58 ? 127 LEU D O    1 
ATOM   14661 C CB   . LEU D 1 127 ? 13.104  57.379  55.627  1.00 100.76 ? 127 LEU D CB   1 
ATOM   14662 C CG   . LEU D 1 127 ? 11.960  57.901  54.758  1.00 103.67 ? 127 LEU D CG   1 
ATOM   14663 C CD1  . LEU D 1 127 ? 10.858  56.855  54.656  1.00 104.03 ? 127 LEU D CD1  1 
ATOM   14664 C CD2  . LEU D 1 127 ? 11.412  59.208  55.305  1.00 104.21 ? 127 LEU D CD2  1 
ATOM   14665 H H    . LEU D 1 127 ? 15.668  57.530  56.780  1.00 117.14 ? 127 LEU D H    1 
ATOM   14666 H HA   . LEU D 1 127 ? 14.629  57.575  54.278  1.00 120.13 ? 127 LEU D HA   1 
ATOM   14667 H HB2  . LEU D 1 127 ? 13.063  56.410  55.603  1.00 120.91 ? 127 LEU D HB2  1 
ATOM   14668 H HB3  . LEU D 1 127 ? 12.946  57.696  56.530  1.00 120.91 ? 127 LEU D HB3  1 
ATOM   14669 H HG   . LEU D 1 127 ? 12.298  58.078  53.866  1.00 124.40 ? 127 LEU D HG   1 
ATOM   14670 H HD11 . LEU D 1 127 ? 10.083  57.253  54.229  1.00 124.83 ? 127 LEU D HD11 1 
ATOM   14671 H HD12 . LEU D 1 127 ? 11.179  56.108  54.127  1.00 124.83 ? 127 LEU D HD12 1 
ATOM   14672 H HD13 . LEU D 1 127 ? 10.625  56.552  55.548  1.00 124.83 ? 127 LEU D HD13 1 
ATOM   14673 H HD21 . LEU D 1 127 ? 10.617  59.450  54.805  1.00 125.05 ? 127 LEU D HD21 1 
ATOM   14674 H HD22 . LEU D 1 127 ? 11.191  59.090  56.242  1.00 125.05 ? 127 LEU D HD22 1 
ATOM   14675 H HD23 . LEU D 1 127 ? 12.087  59.898  55.209  1.00 125.05 ? 127 LEU D HD23 1 
ATOM   14676 N N    . GLU D 1 128 ? 15.019  59.985  54.280  1.00 102.92 ? 128 GLU D N    1 
ATOM   14677 C CA   . GLU D 1 128 ? 15.357  61.400  54.286  1.00 103.85 ? 128 GLU D CA   1 
ATOM   14678 C C    . GLU D 1 128 ? 14.614  62.104  53.156  1.00 110.34 ? 128 GLU D C    1 
ATOM   14679 O O    . GLU D 1 128 ? 13.927  61.477  52.343  1.00 109.09 ? 128 GLU D O    1 
ATOM   14680 C CB   . GLU D 1 128 ? 16.871  61.593  54.138  1.00 103.22 ? 128 GLU D CB   1 
ATOM   14681 C CG   . GLU D 1 128 ? 17.478  62.596  55.092  1.00 106.98 ? 128 GLU D CG   1 
ATOM   14682 C CD   . GLU D 1 128 ? 18.981  62.708  54.923  1.00 107.49 ? 128 GLU D CD   1 
ATOM   14683 O OE1  . GLU D 1 128 ? 19.611  61.696  54.545  1.00 106.77 ? 128 GLU D OE1  1 
ATOM   14684 O OE2  . GLU D 1 128 ? 19.528  63.805  55.169  1.00 108.17 ? 128 GLU D OE2  1 
ATOM   14685 H H    . GLU D 1 128 ? 15.048  59.634  53.496  1.00 123.50 ? 128 GLU D H    1 
ATOM   14686 H HA   . GLU D 1 128 ? 15.069  61.792  55.125  1.00 124.62 ? 128 GLU D HA   1 
ATOM   14687 H HB2  . GLU D 1 128 ? 17.307  60.741  54.295  1.00 123.87 ? 128 GLU D HB2  1 
ATOM   14688 H HB3  . GLU D 1 128 ? 17.056  61.900  53.237  1.00 123.87 ? 128 GLU D HB3  1 
ATOM   14689 H HG2  . GLU D 1 128 ? 17.089  63.469  54.927  1.00 128.37 ? 128 GLU D HG2  1 
ATOM   14690 H HG3  . GLU D 1 128 ? 17.296  62.319  56.004  1.00 128.37 ? 128 GLU D HG3  1 
ATOM   14691 N N    . GLU D 1 129 ? 14.761  63.438  53.106  1.00 113.00 ? 129 GLU D N    1 
ATOM   14692 C CA   . GLU D 1 129 ? 14.171  64.267  52.051  1.00 115.35 ? 129 GLU D CA   1 
ATOM   14693 C C    . GLU D 1 129 ? 15.225  65.306  51.658  1.00 115.34 ? 129 GLU D C    1 
ATOM   14694 O O    . GLU D 1 129 ? 15.182  66.459  52.095  1.00 122.24 ? 129 GLU D O    1 
ATOM   14695 C CB   . GLU D 1 129 ? 12.867  64.920  52.506  1.00 117.78 ? 129 GLU D CB   1 
ATOM   14696 C CG   . GLU D 1 129 ? 12.175  65.730  51.420  1.00 123.13 ? 129 GLU D CG   1 
ATOM   14697 C CD   . GLU D 1 129 ? 10.835  66.291  51.866  1.00 129.81 ? 129 GLU D CD   1 
ATOM   14698 O OE1  . GLU D 1 129 ? 10.738  66.778  53.014  1.00 129.38 ? 129 GLU D OE1  1 
ATOM   14699 O OE2  . GLU D 1 129 ? 9.879   66.243  51.063  1.00 130.55 ? 129 GLU D OE2  1 
ATOM   14700 H H    . GLU D 1 129 ? 15.207  63.891  53.686  1.00 135.60 ? 129 GLU D H    1 
ATOM   14701 H HA   . GLU D 1 129 ? 13.973  63.715  51.278  1.00 138.42 ? 129 GLU D HA   1 
ATOM   14702 H HB2  . GLU D 1 129 ? 12.254  64.225  52.792  1.00 141.33 ? 129 GLU D HB2  1 
ATOM   14703 H HB3  . GLU D 1 129 ? 13.059  65.518  53.244  1.00 141.33 ? 129 GLU D HB3  1 
ATOM   14704 H HG2  . GLU D 1 129 ? 12.744  66.475  51.171  1.00 147.76 ? 129 GLU D HG2  1 
ATOM   14705 H HG3  . GLU D 1 129 ? 12.021  65.160  50.650  1.00 147.76 ? 129 GLU D HG3  1 
ATOM   14706 N N    . ILE D 1 130 ? 16.185  64.881  50.824  1.00 119.37 ? 130 ILE D N    1 
ATOM   14707 C CA   . ILE D 1 130 ? 17.250  65.777  50.399  1.00 120.55 ? 130 ILE D CA   1 
ATOM   14708 C C    . ILE D 1 130 ? 16.719  66.755  49.354  1.00 120.52 ? 130 ILE D C    1 
ATOM   14709 O O    . ILE D 1 130 ? 15.650  66.581  48.774  1.00 118.72 ? 130 ILE D O    1 
ATOM   14710 C CB   . ILE D 1 130 ? 18.455  64.984  49.864  1.00 122.14 ? 130 ILE D CB   1 
ATOM   14711 C CG1  . ILE D 1 130 ? 18.035  63.820  48.960  1.00 117.85 ? 130 ILE D CG1  1 
ATOM   14712 C CG2  . ILE D 1 130 ? 19.275  64.417  51.020  1.00 121.19 ? 130 ILE D CG2  1 
ATOM   14713 C CD1  . ILE D 1 130 ? 17.225  64.219  47.765  1.00 117.55 ? 130 ILE D CD1  1 
ATOM   14714 H H    . ILE D 1 130 ? 16.234  64.087  50.497  1.00 143.24 ? 130 ILE D H    1 
ATOM   14715 H HA   . ILE D 1 130 ? 17.547  66.295  51.164  1.00 144.66 ? 130 ILE D HA   1 
ATOM   14716 H HB   . ILE D 1 130 ? 18.979  65.611  49.342  1.00 146.57 ? 130 ILE D HB   1 
ATOM   14717 H HG12 . ILE D 1 130 ? 18.835  63.377  48.636  1.00 141.42 ? 130 ILE D HG12 1 
ATOM   14718 H HG13 . ILE D 1 130 ? 17.501  63.201  49.482  1.00 141.42 ? 130 ILE D HG13 1 
ATOM   14719 H HG21 . ILE D 1 130 ? 19.888  63.748  50.674  1.00 145.43 ? 130 ILE D HG21 1 
ATOM   14720 H HG22 . ILE D 1 130 ? 19.773  65.137  51.437  1.00 145.43 ? 130 ILE D HG22 1 
ATOM   14721 H HG23 . ILE D 1 130 ? 18.674  64.012  51.665  1.00 145.43 ? 130 ILE D HG23 1 
ATOM   14722 H HD11 . ILE D 1 130 ? 17.220  63.487  47.128  1.00 141.06 ? 130 ILE D HD11 1 
ATOM   14723 H HD12 . ILE D 1 130 ? 16.319  64.416  48.049  1.00 141.06 ? 130 ILE D HD12 1 
ATOM   14724 H HD13 . ILE D 1 130 ? 17.624  65.006  47.361  1.00 141.06 ? 130 ILE D HD13 1 
ATOM   14725 N N    . ASN D 1 131 ? 17.502  67.815  49.108  1.00 124.00 ? 131 ASN D N    1 
ATOM   14726 C CA   . ASN D 1 131 ? 17.117  68.870  48.158  1.00 123.34 ? 131 ASN D CA   1 
ATOM   14727 C C    . ASN D 1 131 ? 18.332  69.200  47.293  1.00 125.94 ? 131 ASN D C    1 
ATOM   14728 O O    . ASN D 1 131 ? 19.140  70.064  47.644  1.00 128.95 ? 131 ASN D O    1 
ATOM   14729 C CB   . ASN D 1 131 ? 16.596  70.107  48.886  1.00 122.27 ? 131 ASN D CB   1 
ATOM   14730 C CG   . ASN D 1 131 ? 15.172  69.937  49.375  1.00 122.68 ? 131 ASN D CG   1 
ATOM   14731 O OD1  . ASN D 1 131 ? 14.491  68.980  49.005  1.00 124.61 ? 131 ASN D OD1  1 
ATOM   14732 N ND2  . ASN D 1 131 ? 14.714  70.862  50.215  1.00 111.30 ? 131 ASN D ND2  1 
ATOM   14733 H H    . ASN D 1 131 ? 18.266  67.945  49.482  1.00 148.80 ? 131 ASN D H    1 
ATOM   14734 H HA   . ASN D 1 131 ? 16.417  68.528  47.580  1.00 148.00 ? 131 ASN D HA   1 
ATOM   14735 H HB2  . ASN D 1 131 ? 17.160  70.282  49.656  1.00 146.72 ? 131 ASN D HB2  1 
ATOM   14736 H HB3  . ASN D 1 131 ? 16.618  70.864  48.280  1.00 146.72 ? 131 ASN D HB3  1 
ATOM   14737 H HD21 . ASN D 1 131 ? 15.220  71.515  50.454  1.00 133.56 ? 131 ASN D HD21 1 
ATOM   14738 H HD22 . ASN D 1 131 ? 13.911  70.807  50.519  1.00 133.56 ? 131 ASN D HD22 1 
ATOM   14739 N N    . VAL D 1 132 ? 18.453  68.510  46.163  1.00 129.03 ? 132 VAL D N    1 
ATOM   14740 C CA   . VAL D 1 132 ? 19.559  68.744  45.241  1.00 133.01 ? 132 VAL D CA   1 
ATOM   14741 C C    . VAL D 1 132 ? 19.204  69.915  44.334  1.00 136.60 ? 132 VAL D C    1 
ATOM   14742 O O    . VAL D 1 132 ? 18.151  69.916  43.684  1.00 134.76 ? 132 VAL D O    1 
ATOM   14743 C CB   . VAL D 1 132 ? 19.865  67.479  44.423  1.00 132.48 ? 132 VAL D CB   1 
ATOM   14744 C CG1  . VAL D 1 132 ? 21.015  67.739  43.456  1.00 134.38 ? 132 VAL D CG1  1 
ATOM   14745 C CG2  . VAL D 1 132 ? 20.187  66.311  45.346  1.00 128.32 ? 132 VAL D CG2  1 
ATOM   14746 H H    . VAL D 1 132 ? 17.906  67.898  45.907  1.00 154.84 ? 132 VAL D H    1 
ATOM   14747 H HA   . VAL D 1 132 ? 20.353  68.977  45.747  1.00 159.61 ? 132 VAL D HA   1 
ATOM   14748 H HB   . VAL D 1 132 ? 19.082  67.242  43.903  1.00 158.97 ? 132 VAL D HB   1 
ATOM   14749 H HG11 . VAL D 1 132 ? 21.317  66.892  43.091  1.00 161.26 ? 132 VAL D HG11 1 
ATOM   14750 H HG12 . VAL D 1 132 ? 20.702  68.315  42.741  1.00 161.26 ? 132 VAL D HG12 1 
ATOM   14751 H HG13 . VAL D 1 132 ? 21.740  68.170  43.935  1.00 161.26 ? 132 VAL D HG13 1 
ATOM   14752 H HG21 . VAL D 1 132 ? 20.444  65.545  44.809  1.00 153.99 ? 132 VAL D HG21 1 
ATOM   14753 H HG22 . VAL D 1 132 ? 20.918  66.564  45.932  1.00 153.99 ? 132 VAL D HG22 1 
ATOM   14754 H HG23 . VAL D 1 132 ? 19.400  66.098  45.872  1.00 153.99 ? 132 VAL D HG23 1 
ATOM   14755 N N    . ASP D 1 133 ? 20.087  70.915  44.285  1.00 148.36 ? 133 ASP D N    1 
ATOM   14756 C CA   . ASP D 1 133 ? 19.843  72.120  43.501  1.00 150.34 ? 133 ASP D CA   1 
ATOM   14757 C C    . ASP D 1 133 ? 18.467  72.688  43.830  1.00 149.54 ? 133 ASP D C    1 
ATOM   14758 O O    . ASP D 1 133 ? 18.208  73.073  44.975  1.00 150.07 ? 133 ASP D O    1 
ATOM   14759 C CB   . ASP D 1 133 ? 19.979  71.821  42.008  1.00 149.79 ? 133 ASP D CB   1 
ATOM   14760 C CG   . ASP D 1 133 ? 21.411  71.530  41.602  1.00 155.26 ? 133 ASP D CG   1 
ATOM   14761 O OD1  . ASP D 1 133 ? 22.190  71.067  42.462  1.00 155.67 ? 133 ASP D OD1  1 
ATOM   14762 O OD2  . ASP D 1 133 ? 21.755  71.761  40.422  1.00 157.37 ? 133 ASP D OD2  1 
ATOM   14763 H H    . ASP D 1 133 ? 20.840  70.916  44.701  1.00 178.03 ? 133 ASP D H    1 
ATOM   14764 H HA   . ASP D 1 133 ? 20.504  72.796  43.721  1.00 180.40 ? 133 ASP D HA   1 
ATOM   14765 H HB2  . ASP D 1 133 ? 19.440  71.044  41.790  1.00 179.75 ? 133 ASP D HB2  1 
ATOM   14766 H HB3  . ASP D 1 133 ? 19.673  72.589  41.501  1.00 179.75 ? 133 ASP D HB3  1 
ATOM   14767 N N    . GLU D 1 134 ? 17.578  72.733  42.840  1.00 137.91 ? 134 GLU D N    1 
ATOM   14768 C CA   . GLU D 1 134 ? 16.240  73.286  43.010  1.00 134.33 ? 134 GLU D CA   1 
ATOM   14769 C C    . GLU D 1 134 ? 15.165  72.215  43.128  1.00 131.22 ? 134 GLU D C    1 
ATOM   14770 O O    . GLU D 1 134 ? 13.992  72.548  43.327  1.00 128.59 ? 134 GLU D O    1 
ATOM   14771 C CB   . GLU D 1 134 ? 15.911  74.215  41.835  1.00 136.97 ? 134 GLU D CB   1 
ATOM   14772 C CG   . GLU D 1 134 ? 15.936  73.516  40.480  1.00 135.52 ? 134 GLU D CG   1 
ATOM   14773 C CD   . GLU D 1 134 ? 17.035  74.025  39.558  1.00 134.15 ? 134 GLU D CD   1 
ATOM   14774 O OE1  . GLU D 1 134 ? 17.939  74.751  40.029  1.00 136.07 ? 134 GLU D OE1  1 
ATOM   14775 O OE2  . GLU D 1 134 ? 16.994  73.690  38.356  1.00 134.99 ? 134 GLU D OE2  1 
ATOM   14776 H H    . GLU D 1 134 ? 17.732  72.444  42.045  1.00 165.49 ? 134 GLU D H    1 
ATOM   14777 H HA   . GLU D 1 134 ? 16.223  73.810  43.826  1.00 161.20 ? 134 GLU D HA   1 
ATOM   14778 H HB2  . GLU D 1 134 ? 15.021  74.579  41.965  1.00 164.36 ? 134 GLU D HB2  1 
ATOM   14779 H HB3  . GLU D 1 134 ? 16.563  74.932  41.812  1.00 164.36 ? 134 GLU D HB3  1 
ATOM   14780 H HG2  . GLU D 1 134 ? 16.081  72.567  40.619  1.00 162.62 ? 134 GLU D HG2  1 
ATOM   14781 H HG3  . GLU D 1 134 ? 15.086  73.660  40.037  1.00 162.62 ? 134 GLU D HG3  1 
ATOM   14782 N N    . TYR D 1 135 ? 15.533  70.946  43.010  1.00 131.33 ? 135 TYR D N    1 
ATOM   14783 C CA   . TYR D 1 135 ? 14.584  69.843  43.031  1.00 127.19 ? 135 TYR D CA   1 
ATOM   14784 C C    . TYR D 1 135 ? 14.609  69.161  44.393  1.00 125.17 ? 135 TYR D C    1 
ATOM   14785 O O    . TYR D 1 135 ? 15.662  69.062  45.030  1.00 125.50 ? 135 TYR D O    1 
ATOM   14786 C CB   . TYR D 1 135 ? 14.914  68.837  41.928  1.00 124.56 ? 135 TYR D CB   1 
ATOM   14787 C CG   . TYR D 1 135 ? 15.272  69.473  40.598  1.00 128.28 ? 135 TYR D CG   1 
ATOM   14788 C CD1  . TYR D 1 135 ? 14.418  70.383  39.985  1.00 130.07 ? 135 TYR D CD1  1 
ATOM   14789 C CD2  . TYR D 1 135 ? 16.463  69.162  39.952  1.00 131.63 ? 135 TYR D CD2  1 
ATOM   14790 C CE1  . TYR D 1 135 ? 14.736  70.962  38.769  1.00 130.86 ? 135 TYR D CE1  1 
ATOM   14791 C CE2  . TYR D 1 135 ? 16.790  69.739  38.736  1.00 131.67 ? 135 TYR D CE2  1 
ATOM   14792 C CZ   . TYR D 1 135 ? 15.924  70.638  38.150  1.00 131.20 ? 135 TYR D CZ   1 
ATOM   14793 O OH   . TYR D 1 135 ? 16.247  71.214  36.944  1.00 133.10 ? 135 TYR D OH   1 
ATOM   14794 H H    . TYR D 1 135 ? 16.349  70.692  42.914  1.00 157.60 ? 135 TYR D H    1 
ATOM   14795 H HA   . TYR D 1 135 ? 13.686  70.177  42.882  1.00 152.63 ? 135 TYR D HA   1 
ATOM   14796 H HB2  . TYR D 1 135 ? 15.671  68.301  42.212  1.00 149.47 ? 135 TYR D HB2  1 
ATOM   14797 H HB3  . TYR D 1 135 ? 14.140  68.269  41.784  1.00 149.47 ? 135 TYR D HB3  1 
ATOM   14798 H HD1  . TYR D 1 135 ? 13.617  70.608  40.401  1.00 156.08 ? 135 TYR D HD1  1 
ATOM   14799 H HD2  . TYR D 1 135 ? 17.050  68.556  40.344  1.00 157.96 ? 135 TYR D HD2  1 
ATOM   14800 H HE1  . TYR D 1 135 ? 14.150  71.566  38.371  1.00 157.04 ? 135 TYR D HE1  1 
ATOM   14801 H HE2  . TYR D 1 135 ? 17.591  69.521  38.316  1.00 158.00 ? 135 TYR D HE2  1 
ATOM   14802 H HH   . TYR D 1 135 ? 15.642  71.746  36.708  1.00 159.72 ? 135 TYR D HH   1 
ATOM   14803 N N    . LYS D 1 136 ? 13.443  68.702  44.838  1.00 122.31 ? 136 LYS D N    1 
ATOM   14804 C CA   . LYS D 1 136 ? 13.303  67.983  46.100  1.00 121.47 ? 136 LYS D CA   1 
ATOM   14805 C C    . LYS D 1 136 ? 13.008  66.522  45.789  1.00 119.04 ? 136 LYS D C    1 
ATOM   14806 O O    . LYS D 1 136 ? 12.068  66.215  45.046  1.00 119.11 ? 136 LYS D O    1 
ATOM   14807 C CB   . LYS D 1 136 ? 12.207  68.602  46.970  1.00 122.90 ? 136 LYS D CB   1 
ATOM   14808 C CG   . LYS D 1 136 ? 10.866  67.880  46.967  1.00 125.52 ? 136 LYS D CG   1 
ATOM   14809 C CD   . LYS D 1 136 ? 9.801   68.617  47.804  1.00 127.22 ? 136 LYS D CD   1 
ATOM   14810 C CE   . LYS D 1 136 ? 10.371  69.254  49.067  1.00 125.84 ? 136 LYS D CE   1 
ATOM   14811 N NZ   . LYS D 1 136 ? 9.357   70.082  49.793  1.00 126.40 ? 136 LYS D NZ   1 
ATOM   14812 H H    . LYS D 1 136 ? 12.700  68.798  44.416  1.00 146.78 ? 136 LYS D H    1 
ATOM   14813 H HA   . LYS D 1 136 ? 14.133  68.027  46.600  1.00 145.77 ? 136 LYS D HA   1 
ATOM   14814 H HB2  . LYS D 1 136 ? 12.522  68.619  47.887  1.00 147.48 ? 136 LYS D HB2  1 
ATOM   14815 H HB3  . LYS D 1 136 ? 12.047  69.506  46.657  1.00 147.48 ? 136 LYS D HB3  1 
ATOM   14816 H HG2  . LYS D 1 136 ? 10.541  67.816  46.055  1.00 150.63 ? 136 LYS D HG2  1 
ATOM   14817 H HG3  . LYS D 1 136 ? 10.981  66.993  47.341  1.00 150.63 ? 136 LYS D HG3  1 
ATOM   14818 H HD2  . LYS D 1 136 ? 9.408   69.321  47.266  1.00 152.66 ? 136 LYS D HD2  1 
ATOM   14819 H HD3  . LYS D 1 136 ? 9.117   67.984  48.072  1.00 152.66 ? 136 LYS D HD3  1 
ATOM   14820 H HE2  . LYS D 1 136 ? 10.674  68.555  49.667  1.00 151.00 ? 136 LYS D HE2  1 
ATOM   14821 H HE3  . LYS D 1 136 ? 11.113  69.830  48.826  1.00 151.00 ? 136 LYS D HE3  1 
ATOM   14822 H HZ1  . LYS D 1 136 ? 9.721   70.437  50.524  1.00 151.68 ? 136 LYS D HZ1  1 
ATOM   14823 H HZ2  . LYS D 1 136 ? 9.067   70.739  49.267  1.00 151.68 ? 136 LYS D HZ2  1 
ATOM   14824 H HZ3  . LYS D 1 136 ? 8.665   69.576  50.032  1.00 151.68 ? 136 LYS D HZ3  1 
ATOM   14825 N N    . LEU D 1 137 ? 13.834  65.631  46.330  1.00 119.79 ? 137 LEU D N    1 
ATOM   14826 C CA   . LEU D 1 137 ? 13.766  64.208  46.053  1.00 115.23 ? 137 LEU D CA   1 
ATOM   14827 C C    . LEU D 1 137 ? 13.745  63.450  47.375  1.00 119.36 ? 137 LEU D C    1 
ATOM   14828 O O    . LEU D 1 137 ? 13.912  64.028  48.453  1.00 117.34 ? 137 LEU D O    1 
ATOM   14829 C CB   . LEU D 1 137 ? 14.956  63.749  45.200  1.00 111.68 ? 137 LEU D CB   1 
ATOM   14830 C CG   . LEU D 1 137 ? 15.082  64.195  43.744  1.00 113.67 ? 137 LEU D CG   1 
ATOM   14831 C CD1  . LEU D 1 137 ? 14.806  65.669  43.533  1.00 119.14 ? 137 LEU D CD1  1 
ATOM   14832 C CD2  . LEU D 1 137 ? 16.491  63.848  43.233  1.00 105.46 ? 137 LEU D CD2  1 
ATOM   14833 H H    . LEU D 1 137 ? 14.463  65.839  46.879  1.00 143.75 ? 137 LEU D H    1 
ATOM   14834 H HA   . LEU D 1 137 ? 12.950  64.010  45.568  1.00 138.28 ? 137 LEU D HA   1 
ATOM   14835 H HB2  . LEU D 1 137 ? 15.761  64.057  45.645  1.00 134.01 ? 137 LEU D HB2  1 
ATOM   14836 H HB3  . LEU D 1 137 ? 14.937  62.780  45.183  1.00 134.01 ? 137 LEU D HB3  1 
ATOM   14837 H HG   . LEU D 1 137 ? 14.405  63.723  43.233  1.00 136.41 ? 137 LEU D HG   1 
ATOM   14838 H HD11 . LEU D 1 137 ? 15.242  65.957  42.715  1.00 142.97 ? 137 LEU D HD11 1 
ATOM   14839 H HD12 . LEU D 1 137 ? 13.848  65.804  43.463  1.00 142.97 ? 137 LEU D HD12 1 
ATOM   14840 H HD13 . LEU D 1 137 ? 15.157  66.167  44.288  1.00 142.97 ? 137 LEU D HD13 1 
ATOM   14841 H HD21 . LEU D 1 137 ? 16.556  64.090  42.296  1.00 126.55 ? 137 LEU D HD21 1 
ATOM   14842 H HD22 . LEU D 1 137 ? 17.145  64.345  43.748  1.00 126.55 ? 137 LEU D HD22 1 
ATOM   14843 H HD23 . LEU D 1 137 ? 16.640  62.896  43.340  1.00 126.55 ? 137 LEU D HD23 1 
ATOM   14844 N N    . GLY D 1 138 ? 13.546  62.135  47.281  1.00 119.99 ? 138 GLY D N    1 
ATOM   14845 C CA   . GLY D 1 138 ? 13.544  61.266  48.434  1.00 112.27 ? 138 GLY D CA   1 
ATOM   14846 C C    . GLY D 1 138 ? 14.809  60.422  48.501  1.00 112.97 ? 138 GLY D C    1 
ATOM   14847 O O    . GLY D 1 138 ? 15.583  60.320  47.551  1.00 120.59 ? 138 GLY D O    1 
ATOM   14848 H H    . GLY D 1 138 ? 13.407  61.723  46.539  1.00 143.98 ? 138 GLY D H    1 
ATOM   14849 H HA2  . GLY D 1 138 ? 13.486  61.800  49.242  1.00 134.73 ? 138 GLY D HA2  1 
ATOM   14850 H HA3  . GLY D 1 138 ? 12.779  60.673  48.392  1.00 134.73 ? 138 GLY D HA3  1 
ATOM   14851 N N    . LEU D 1 139 ? 15.004  59.805  49.665  1.00 108.86 ? 139 LEU D N    1 
ATOM   14852 C CA   . LEU D 1 139 ? 16.196  58.993  49.899  1.00 104.74 ? 139 LEU D CA   1 
ATOM   14853 C C    . LEU D 1 139 ? 15.843  57.915  50.920  1.00 102.30 ? 139 LEU D C    1 
ATOM   14854 O O    . LEU D 1 139 ? 15.876  58.165  52.128  1.00 102.36 ? 139 LEU D O    1 
ATOM   14855 C CB   . LEU D 1 139 ? 17.355  59.859  50.374  1.00 104.72 ? 139 LEU D CB   1 
ATOM   14856 C CG   . LEU D 1 139 ? 18.739  59.263  50.132  1.00 104.91 ? 139 LEU D CG   1 
ATOM   14857 C CD1  . LEU D 1 139 ? 19.753  60.335  49.791  1.00 112.17 ? 139 LEU D CD1  1 
ATOM   14858 C CD2  . LEU D 1 139 ? 19.175  58.494  51.361  1.00 105.52 ? 139 LEU D CD2  1 
ATOM   14859 H H    . LEU D 1 139 ? 14.463  59.841  50.332  1.00 130.63 ? 139 LEU D H    1 
ATOM   14860 H HA   . LEU D 1 139 ? 16.450  58.553  49.073  1.00 125.69 ? 139 LEU D HA   1 
ATOM   14861 H HB2  . LEU D 1 139 ? 17.316  60.708  49.906  1.00 125.66 ? 139 LEU D HB2  1 
ATOM   14862 H HB3  . LEU D 1 139 ? 17.260  60.002  51.329  1.00 125.66 ? 139 LEU D HB3  1 
ATOM   14863 H HG   . LEU D 1 139 ? 18.696  58.659  49.375  1.00 125.90 ? 139 LEU D HG   1 
ATOM   14864 H HD11 . LEU D 1 139 ? 20.579  59.910  49.511  1.00 134.61 ? 139 LEU D HD11 1 
ATOM   14865 H HD12 . LEU D 1 139 ? 19.402  60.882  49.071  1.00 134.61 ? 139 LEU D HD12 1 
ATOM   14866 H HD13 . LEU D 1 139 ? 19.911  60.881  50.576  1.00 134.61 ? 139 LEU D HD13 1 
ATOM   14867 H HD21 . LEU D 1 139 ? 20.030  58.071  51.181  1.00 126.62 ? 139 LEU D HD21 1 
ATOM   14868 H HD22 . LEU D 1 139 ? 19.261  59.110  52.105  1.00 126.62 ? 139 LEU D HD22 1 
ATOM   14869 H HD23 . LEU D 1 139 ? 18.509  57.820  51.564  1.00 126.62 ? 139 LEU D HD23 1 
ATOM   14870 N N    . VAL D 1 140 ? 15.509  56.732  50.425  1.00 101.08 ? 140 VAL D N    1 
ATOM   14871 C CA   . VAL D 1 140 ? 15.255  55.559  51.251  1.00 98.46  ? 140 VAL D CA   1 
ATOM   14872 C C    . VAL D 1 140 ? 16.473  54.657  51.100  1.00 99.34  ? 140 VAL D C    1 
ATOM   14873 O O    . VAL D 1 140 ? 16.571  53.887  50.136  1.00 104.01 ? 140 VAL D O    1 
ATOM   14874 C CB   . VAL D 1 140 ? 13.965  54.834  50.845  1.00 97.06  ? 140 VAL D CB   1 
ATOM   14875 C CG1  . VAL D 1 140 ? 13.645  53.716  51.824  1.00 94.46  ? 140 VAL D CG1  1 
ATOM   14876 C CG2  . VAL D 1 140 ? 12.806  55.821  50.750  1.00 100.86 ? 140 VAL D CG2  1 
ATOM   14877 H H    . VAL D 1 140 ? 15.421  56.577  49.584  1.00 121.30 ? 140 VAL D H    1 
ATOM   14878 H HA   . VAL D 1 140 ? 15.173  55.827  52.179  1.00 118.15 ? 140 VAL D HA   1 
ATOM   14879 H HB   . VAL D 1 140 ? 14.093  54.435  49.970  1.00 116.48 ? 140 VAL D HB   1 
ATOM   14880 H HG11 . VAL D 1 140 ? 12.910  53.189  51.473  1.00 113.35 ? 140 VAL D HG11 1 
ATOM   14881 H HG12 . VAL D 1 140 ? 14.430  53.156  51.932  1.00 113.35 ? 140 VAL D HG12 1 
ATOM   14882 H HG13 . VAL D 1 140 ? 13.396  54.105  52.677  1.00 113.35 ? 140 VAL D HG13 1 
ATOM   14883 H HG21 . VAL D 1 140 ? 11.983  55.329  50.605  1.00 121.04 ? 140 VAL D HG21 1 
ATOM   14884 H HG22 . VAL D 1 140 ? 12.750  56.322  51.579  1.00 121.04 ? 140 VAL D HG22 1 
ATOM   14885 H HG23 . VAL D 1 140 ? 12.965  56.425  50.008  1.00 121.04 ? 140 VAL D HG23 1 
ATOM   14886 N N    . ARG D 1 141 ? 17.415  54.755  52.033  1.00 99.01  ? 141 ARG D N    1 
ATOM   14887 C CA   . ARG D 1 141 ? 18.610  53.926  51.968  1.00 102.53 ? 141 ARG D CA   1 
ATOM   14888 C C    . ARG D 1 141 ? 18.280  52.479  52.321  1.00 101.66 ? 141 ARG D C    1 
ATOM   14889 O O    . ARG D 1 141 ? 17.322  52.194  53.045  1.00 101.42 ? 141 ARG D O    1 
ATOM   14890 C CB   . ARG D 1 141 ? 19.687  54.457  52.914  1.00 104.29 ? 141 ARG D CB   1 
ATOM   14891 C CG   . ARG D 1 141 ? 20.339  55.747  52.443  1.00 106.94 ? 141 ARG D CG   1 
ATOM   14892 C CD   . ARG D 1 141 ? 21.809  55.815  52.838  1.00 114.15 ? 141 ARG D CD   1 
ATOM   14893 N NE   . ARG D 1 141 ? 22.547  56.784  52.033  1.00 120.19 ? 141 ARG D NE   1 
ATOM   14894 C CZ   . ARG D 1 141 ? 22.483  58.100  52.192  1.00 117.47 ? 141 ARG D CZ   1 
ATOM   14895 N NH1  . ARG D 1 141 ? 21.723  58.647  53.126  1.00 112.87 ? 141 ARG D NH1  1 
ATOM   14896 N NH2  . ARG D 1 141 ? 23.197  58.887  51.390  1.00 120.15 ? 141 ARG D NH2  1 
ATOM   14897 H H    . ARG D 1 141 ? 17.386  55.289  52.706  1.00 118.81 ? 141 ARG D H    1 
ATOM   14898 H HA   . ARG D 1 141 ? 18.965  53.948  51.066  1.00 123.04 ? 141 ARG D HA   1 
ATOM   14899 H HB2  . ARG D 1 141 ? 19.284  54.629  53.780  1.00 125.15 ? 141 ARG D HB2  1 
ATOM   14900 H HB3  . ARG D 1 141 ? 20.384  53.788  53.000  1.00 125.15 ? 141 ARG D HB3  1 
ATOM   14901 H HG2  . ARG D 1 141 ? 20.281  55.800  51.477  1.00 128.32 ? 141 ARG D HG2  1 
ATOM   14902 H HG3  . ARG D 1 141 ? 19.882  56.502  52.845  1.00 128.32 ? 141 ARG D HG3  1 
ATOM   14903 H HD2  . ARG D 1 141 ? 21.878  56.079  53.769  1.00 136.98 ? 141 ARG D HD2  1 
ATOM   14904 H HD3  . ARG D 1 141 ? 22.215  54.943  52.710  1.00 136.98 ? 141 ARG D HD3  1 
ATOM   14905 H HE   . ARG D 1 141 ? 23.059  56.481  51.412  1.00 144.22 ? 141 ARG D HE   1 
ATOM   14906 H HH11 . ARG D 1 141 ? 21.256  58.147  53.648  1.00 135.44 ? 141 ARG D HH11 1 
ATOM   14907 H HH12 . ARG D 1 141 ? 21.696  59.502  53.212  1.00 135.44 ? 141 ARG D HH12 1 
ATOM   14908 H HH21 . ARG D 1 141 ? 23.692  58.541  50.778  1.00 144.17 ? 141 ARG D HH21 1 
ATOM   14909 H HH22 . ARG D 1 141 ? 23.163  59.741  51.485  1.00 144.17 ? 141 ARG D HH22 1 
ATOM   14910 N N    . PHE D 1 142 ? 19.090  51.561  51.795  1.00 107.13 ? 142 PHE D N    1 
ATOM   14911 C CA   . PHE D 1 142 ? 18.922  50.137  52.036  1.00 104.93 ? 142 PHE D CA   1 
ATOM   14912 C C    . PHE D 1 142 ? 20.293  49.498  52.207  1.00 108.08 ? 142 PHE D C    1 
ATOM   14913 O O    . PHE D 1 142 ? 21.324  50.086  51.872  1.00 109.31 ? 142 PHE D O    1 
ATOM   14914 C CB   . PHE D 1 142 ? 18.166  49.451  50.891  1.00 101.09 ? 142 PHE D CB   1 
ATOM   14915 C CG   . PHE D 1 142 ? 16.682  49.664  50.927  1.00 97.59  ? 142 PHE D CG   1 
ATOM   14916 C CD1  . PHE D 1 142 ? 15.860  48.794  51.620  1.00 97.54  ? 142 PHE D CD1  1 
ATOM   14917 C CD2  . PHE D 1 142 ? 16.107  50.730  50.257  1.00 97.91  ? 142 PHE D CD2  1 
ATOM   14918 C CE1  . PHE D 1 142 ? 14.492  48.987  51.652  1.00 96.42  ? 142 PHE D CE1  1 
ATOM   14919 C CE2  . PHE D 1 142 ? 14.739  50.927  50.286  1.00 96.55  ? 142 PHE D CE2  1 
ATOM   14920 C CZ   . PHE D 1 142 ? 13.930  50.054  50.986  1.00 94.78  ? 142 PHE D CZ   1 
ATOM   14921 H H    . PHE D 1 142 ? 19.757  51.746  51.285  1.00 128.55 ? 142 PHE D H    1 
ATOM   14922 H HA   . PHE D 1 142 ? 18.415  50.016  52.855  1.00 125.91 ? 142 PHE D HA   1 
ATOM   14923 H HB2  . PHE D 1 142 ? 18.494  49.801  50.048  1.00 121.30 ? 142 PHE D HB2  1 
ATOM   14924 H HB3  . PHE D 1 142 ? 18.328  48.496  50.939  1.00 121.30 ? 142 PHE D HB3  1 
ATOM   14925 H HD1  . PHE D 1 142 ? 16.232  48.070  52.070  1.00 117.49 ? 142 PHE D HD1  1 
ATOM   14926 H HD2  . PHE D 1 142 ? 16.646  51.321  49.783  1.00 117.05 ? 142 PHE D HD2  1 
ATOM   14927 H HE1  . PHE D 1 142 ? 13.950  48.396  52.124  1.00 115.85 ? 142 PHE D HE1  1 
ATOM   14928 H HE2  . PHE D 1 142 ? 14.363  51.649  49.835  1.00 115.70 ? 142 PHE D HE2  1 
ATOM   14929 H HZ   . PHE D 1 142 ? 13.009  50.185  51.006  1.00 113.74 ? 142 PHE D HZ   1 
ATOM   14930 N N    . SER D 1 143 ? 20.296  48.271  52.727  1.00 109.07 ? 143 SER D N    1 
ATOM   14931 C CA   . SER D 1 143 ? 21.532  47.522  52.950  1.00 109.39 ? 143 SER D CA   1 
ATOM   14932 C C    . SER D 1 143 ? 22.012  46.963  51.614  1.00 110.44 ? 143 SER D C    1 
ATOM   14933 O O    . SER D 1 143 ? 21.804  45.796  51.275  1.00 111.37 ? 143 SER D O    1 
ATOM   14934 C CB   . SER D 1 143 ? 21.308  46.415  53.972  1.00 106.94 ? 143 SER D CB   1 
ATOM   14935 O OG   . SER D 1 143 ? 20.148  45.666  53.656  1.00 104.77 ? 143 SER D OG   1 
ATOM   14936 H H    . SER D 1 143 ? 19.586  47.846  52.962  1.00 130.89 ? 143 SER D H    1 
ATOM   14937 H HA   . SER D 1 143 ? 22.211  48.125  53.292  1.00 131.27 ? 143 SER D HA   1 
ATOM   14938 H HB2  . SER D 1 143 ? 22.077  45.823  53.969  1.00 128.32 ? 143 SER D HB2  1 
ATOM   14939 H HB3  . SER D 1 143 ? 21.199  46.813  54.850  1.00 128.32 ? 143 SER D HB3  1 
ATOM   14940 H HG   . SER D 1 143 ? 20.226  45.323  52.894  1.00 125.72 ? 143 SER D HG   1 
ATOM   14941 N N    . GLY D 1 144 ? 22.668  47.825  50.841  1.00 113.28 ? 144 GLY D N    1 
ATOM   14942 C CA   . GLY D 1 144 ? 23.166  47.436  49.539  1.00 116.01 ? 144 GLY D CA   1 
ATOM   14943 C C    . GLY D 1 144 ? 22.960  48.493  48.474  1.00 118.85 ? 144 GLY D C    1 
ATOM   14944 O O    . GLY D 1 144 ? 23.861  48.761  47.675  1.00 122.81 ? 144 GLY D O    1 
ATOM   14945 H H    . GLY D 1 144 ? 22.835  48.641  51.054  1.00 135.94 ? 144 GLY D H    1 
ATOM   14946 H HA2  . GLY D 1 144 ? 24.116  47.255  49.604  1.00 139.21 ? 144 GLY D HA2  1 
ATOM   14947 H HA3  . GLY D 1 144 ? 22.709  46.628  49.254  1.00 139.21 ? 144 GLY D HA3  1 
ATOM   14948 N N    . ILE D 1 145 ? 21.779  49.114  48.464  1.00 123.43 ? 145 ILE D N    1 
ATOM   14949 C CA   . ILE D 1 145 ? 21.410  50.099  47.455  1.00 125.48 ? 145 ILE D CA   1 
ATOM   14950 C C    . ILE D 1 145 ? 20.758  51.295  48.137  1.00 123.65 ? 145 ILE D C    1 
ATOM   14951 O O    . ILE D 1 145 ? 20.230  51.197  49.245  1.00 123.29 ? 145 ILE D O    1 
ATOM   14952 C CB   . ILE D 1 145 ? 20.461  49.488  46.393  1.00 129.37 ? 145 ILE D CB   1 
ATOM   14953 C CG1  . ILE D 1 145 ? 19.783  50.587  45.575  1.00 125.87 ? 145 ILE D CG1  1 
ATOM   14954 C CG2  . ILE D 1 145 ? 19.436  48.586  47.077  1.00 124.93 ? 145 ILE D CG2  1 
ATOM   14955 C CD1  . ILE D 1 145 ? 19.225  50.114  44.250  1.00 121.50 ? 145 ILE D CD1  1 
ATOM   14956 H H    . ILE D 1 145 ? 21.162  48.976  49.048  1.00 148.12 ? 145 ILE D H    1 
ATOM   14957 H HA   . ILE D 1 145 ? 22.207  50.423  47.007  1.00 150.58 ? 145 ILE D HA   1 
ATOM   14958 H HB   . ILE D 1 145 ? 20.983  48.951  45.776  1.00 155.24 ? 145 ILE D HB   1 
ATOM   14959 H HG12 . ILE D 1 145 ? 19.046  50.949  46.092  1.00 151.05 ? 145 ILE D HG12 1 
ATOM   14960 H HG13 . ILE D 1 145 ? 20.432  51.283  45.390  1.00 151.05 ? 145 ILE D HG13 1 
ATOM   14961 H HG21 . ILE D 1 145 ? 18.739  48.360  46.441  1.00 149.91 ? 145 ILE D HG21 1 
ATOM   14962 H HG22 . ILE D 1 145 ? 19.879  47.779  47.383  1.00 149.91 ? 145 ILE D HG22 1 
ATOM   14963 H HG23 . ILE D 1 145 ? 19.053  49.059  47.833  1.00 149.91 ? 145 ILE D HG23 1 
ATOM   14964 H HD11 . ILE D 1 145 ? 18.777  50.856  43.813  1.00 145.81 ? 145 ILE D HD11 1 
ATOM   14965 H HD12 . ILE D 1 145 ? 19.955  49.797  43.696  1.00 145.81 ? 145 ILE D HD12 1 
ATOM   14966 H HD13 . ILE D 1 145 ? 18.595  49.395  44.411  1.00 145.81 ? 145 ILE D HD13 1 
ATOM   14967 N N    . ASN D 1 146 ? 20.815  52.441  47.460  1.00 118.10 ? 146 ASN D N    1 
ATOM   14968 C CA   . ASN D 1 146 ? 20.181  53.674  47.917  1.00 114.16 ? 146 ASN D CA   1 
ATOM   14969 C C    . ASN D 1 146 ? 19.212  54.152  46.841  1.00 109.98 ? 146 ASN D C    1 
ATOM   14970 O O    . ASN D 1 146 ? 19.637  54.682  45.808  1.00 108.32 ? 146 ASN D O    1 
ATOM   14971 C CB   . ASN D 1 146 ? 21.225  54.747  48.224  1.00 115.48 ? 146 ASN D CB   1 
ATOM   14972 C CG   . ASN D 1 146 ? 22.405  54.206  49.005  1.00 121.87 ? 146 ASN D CG   1 
ATOM   14973 O OD1  . ASN D 1 146 ? 22.235  53.599  50.063  1.00 117.90 ? 146 ASN D OD1  1 
ATOM   14974 N ND2  . ASN D 1 146 ? 23.609  54.419  48.487  1.00 129.19 ? 146 ASN D ND2  1 
ATOM   14975 H H    . ASN D 1 146 ? 21.229  52.531  46.711  1.00 141.72 ? 146 ASN D H    1 
ATOM   14976 H HA   . ASN D 1 146 ? 19.676  53.491  48.725  1.00 136.99 ? 146 ASN D HA   1 
ATOM   14977 H HB2  . ASN D 1 146 ? 21.560  55.111  47.389  1.00 138.58 ? 146 ASN D HB2  1 
ATOM   14978 H HB3  . ASN D 1 146 ? 20.813  55.449  48.750  1.00 138.58 ? 146 ASN D HB3  1 
ATOM   14979 H HD21 . ASN D 1 146 ? 23.688  54.845  47.744  1.00 155.03 ? 146 ASN D HD21 1 
ATOM   14980 H HD22 . ASN D 1 146 ? 24.310  54.131  48.894  1.00 155.03 ? 146 ASN D HD22 1 
ATOM   14981 N N    . HIS D 1 147 ? 17.914  53.972  47.083  1.00 106.36 ? 147 HIS D N    1 
ATOM   14982 C CA   . HIS D 1 147 ? 16.889  54.426  46.154  1.00 100.59 ? 147 HIS D CA   1 
ATOM   14983 C C    . HIS D 1 147 ? 16.559  55.892  46.408  1.00 100.46 ? 147 HIS D C    1 
ATOM   14984 O O    . HIS D 1 147 ? 16.402  56.317  47.557  1.00 103.35 ? 147 HIS D O    1 
ATOM   14985 C CB   . HIS D 1 147 ? 15.610  53.595  46.287  1.00 96.43  ? 147 HIS D CB   1 
ATOM   14986 C CG   . HIS D 1 147 ? 15.784  52.149  45.949  1.00 98.68  ? 147 HIS D CG   1 
ATOM   14987 N ND1  . HIS D 1 147 ? 15.142  51.550  44.888  1.00 97.21  ? 147 HIS D ND1  1 
ATOM   14988 C CD2  . HIS D 1 147 ? 16.515  51.177  46.543  1.00 102.95 ? 147 HIS D CD2  1 
ATOM   14989 C CE1  . HIS D 1 147 ? 15.476  50.273  44.838  1.00 95.58  ? 147 HIS D CE1  1 
ATOM   14990 N NE2  . HIS D 1 147 ? 16.313  50.022  45.828  1.00 99.44  ? 147 HIS D NE2  1 
ATOM   14991 H H    . HIS D 1 147 ? 17.603  53.585  47.785  1.00 127.63 ? 147 HIS D H    1 
ATOM   14992 H HA   . HIS D 1 147 ? 17.224  54.327  45.249  1.00 120.71 ? 147 HIS D HA   1 
ATOM   14993 H HB2  . HIS D 1 147 ? 15.300  53.648  47.205  1.00 115.72 ? 147 HIS D HB2  1 
ATOM   14994 H HB3  . HIS D 1 147 ? 14.939  53.959  45.689  1.00 115.72 ? 147 HIS D HB3  1 
ATOM   14995 H HD2  . HIS D 1 147 ? 17.054  51.274  47.295  1.00 123.55 ? 147 HIS D HD2  1 
ATOM   14996 H HE1  . HIS D 1 147 ? 15.174  49.655  44.212  1.00 114.70 ? 147 HIS D HE1  1 
ATOM   14997 H HE2  . HIS D 1 147 ? 16.673  49.260  45.998  1.00 119.32 ? 147 HIS D HE2  1 
ATOM   14998 N N    . PHE D 1 148 ? 16.448  56.660  45.330  1.00 99.90  ? 148 PHE D N    1 
ATOM   14999 C CA   . PHE D 1 148 ? 15.991  58.040  45.385  1.00 100.26 ? 148 PHE D CA   1 
ATOM   15000 C C    . PHE D 1 148 ? 14.582  58.121  44.817  1.00 100.67 ? 148 PHE D C    1 
ATOM   15001 O O    . PHE D 1 148 ? 14.252  57.426  43.850  1.00 101.56 ? 148 PHE D O    1 
ATOM   15002 C CB   . PHE D 1 148 ? 16.923  58.962  44.605  1.00 99.46  ? 148 PHE D CB   1 
ATOM   15003 C CG   . PHE D 1 148 ? 18.282  59.108  45.222  1.00 101.07 ? 148 PHE D CG   1 
ATOM   15004 C CD1  . PHE D 1 148 ? 19.175  58.050  45.216  1.00 99.96  ? 148 PHE D CD1  1 
ATOM   15005 C CD2  . PHE D 1 148 ? 18.668  60.303  45.804  1.00 102.46 ? 148 PHE D CD2  1 
ATOM   15006 C CE1  . PHE D 1 148 ? 20.428  58.181  45.779  1.00 105.39 ? 148 PHE D CE1  1 
ATOM   15007 C CE2  . PHE D 1 148 ? 19.921  60.441  46.372  1.00 106.25 ? 148 PHE D CE2  1 
ATOM   15008 C CZ   . PHE D 1 148 ? 20.801  59.378  46.361  1.00 105.72 ? 148 PHE D CZ   1 
ATOM   15009 H H    . PHE D 1 148 ? 16.636  56.394  44.534  1.00 119.87 ? 148 PHE D H    1 
ATOM   15010 H HA   . PHE D 1 148 ? 15.975  58.346  46.305  1.00 120.32 ? 148 PHE D HA   1 
ATOM   15011 H HB2  . PHE D 1 148 ? 17.041  58.604  43.711  1.00 119.36 ? 148 PHE D HB2  1 
ATOM   15012 H HB3  . PHE D 1 148 ? 16.523  59.844  44.559  1.00 119.36 ? 148 PHE D HB3  1 
ATOM   15013 H HD1  . PHE D 1 148 ? 18.928  57.242  44.827  1.00 119.95 ? 148 PHE D HD1  1 
ATOM   15014 H HD2  . PHE D 1 148 ? 18.078  61.022  45.814  1.00 122.95 ? 148 PHE D HD2  1 
ATOM   15015 H HE1  . PHE D 1 148 ? 21.021  57.465  45.768  1.00 126.46 ? 148 PHE D HE1  1 
ATOM   15016 H HE2  . PHE D 1 148 ? 20.170  61.248  46.761  1.00 127.50 ? 148 PHE D HE2  1 
ATOM   15017 H HZ   . PHE D 1 148 ? 21.643  59.467  46.744  1.00 126.87 ? 148 PHE D HZ   1 
ATOM   15018 N N    . ILE D 1 149 ? 13.752  58.959  45.427  1.00 103.59 ? 149 ILE D N    1 
ATOM   15019 C CA   . ILE D 1 149 ? 12.376  59.166  44.998  1.00 103.13 ? 149 ILE D CA   1 
ATOM   15020 C C    . ILE D 1 149 ? 12.264  60.566  44.415  1.00 107.32 ? 149 ILE D C    1 
ATOM   15021 O O    . ILE D 1 149 ? 12.795  61.529  44.982  1.00 108.14 ? 149 ILE D O    1 
ATOM   15022 C CB   . ILE D 1 149 ? 11.372  58.985  46.153  1.00 107.05 ? 149 ILE D CB   1 
ATOM   15023 C CG1  . ILE D 1 149 ? 11.439  57.560  46.703  1.00 105.52 ? 149 ILE D CG1  1 
ATOM   15024 C CG2  . ILE D 1 149 ? 9.960   59.331  45.686  1.00 104.24 ? 149 ILE D CG2  1 
ATOM   15025 C CD1  . ILE D 1 149 ? 10.848  56.504  45.781  1.00 97.37  ? 149 ILE D CD1  1 
ATOM   15026 H H    . ILE D 1 149 ? 13.971  59.432  46.111  1.00 124.31 ? 149 ILE D H    1 
ATOM   15027 H HA   . ILE D 1 149 ? 12.163  58.514  44.311  1.00 123.75 ? 149 ILE D HA   1 
ATOM   15028 H HB   . ILE D 1 149 ? 11.611  59.592  46.871  1.00 128.47 ? 149 ILE D HB   1 
ATOM   15029 H HG12 . ILE D 1 149 ? 12.369  57.330  46.853  1.00 126.63 ? 149 ILE D HG12 1 
ATOM   15030 H HG13 . ILE D 1 149 ? 10.949  57.527  47.539  1.00 126.63 ? 149 ILE D HG13 1 
ATOM   15031 H HG21 . ILE D 1 149 ? 9.334   59.141  46.402  1.00 125.09 ? 149 ILE D HG21 1 
ATOM   15032 H HG22 . ILE D 1 149 ? 9.925   60.273  45.458  1.00 125.09 ? 149 ILE D HG22 1 
ATOM   15033 H HG23 . ILE D 1 149 ? 9.744   58.794  44.907  1.00 125.09 ? 149 ILE D HG23 1 
ATOM   15034 H HD11 . ILE D 1 149 ? 10.929  55.635  46.204  1.00 116.85 ? 149 ILE D HD11 1 
ATOM   15035 H HD12 . ILE D 1 149 ? 9.913   56.710  45.625  1.00 116.85 ? 149 ILE D HD12 1 
ATOM   15036 H HD13 . ILE D 1 149 ? 11.333  56.510  44.941  1.00 116.85 ? 149 ILE D HD13 1 
ATOM   15037 N N    . PHE D 1 150 ? 11.565  60.677  43.285  1.00 108.08 ? 150 PHE D N    1 
ATOM   15038 C CA   . PHE D 1 150 ? 11.270  61.963  42.663  1.00 108.39 ? 150 PHE D CA   1 
ATOM   15039 C C    . PHE D 1 150 ? 9.797   61.983  42.283  1.00 110.51 ? 150 PHE D C    1 
ATOM   15040 O O    . PHE D 1 150 ? 9.330   61.098  41.556  1.00 109.11 ? 150 PHE D O    1 
ATOM   15041 C CB   . PHE D 1 150 ? 12.148  62.202  41.432  1.00 108.11 ? 150 PHE D CB   1 
ATOM   15042 C CG   . PHE D 1 150 ? 11.736  63.401  40.623  1.00 114.65 ? 150 PHE D CG   1 
ATOM   15043 C CD1  . PHE D 1 150 ? 10.646  63.340  39.766  1.00 113.50 ? 150 PHE D CD1  1 
ATOM   15044 C CD2  . PHE D 1 150 ? 12.438  64.590  40.717  1.00 116.35 ? 150 PHE D CD2  1 
ATOM   15045 C CE1  . PHE D 1 150 ? 10.264  64.440  39.028  1.00 111.54 ? 150 PHE D CE1  1 
ATOM   15046 C CE2  . PHE D 1 150 ? 12.056  65.695  39.977  1.00 117.02 ? 150 PHE D CE2  1 
ATOM   15047 C CZ   . PHE D 1 150 ? 10.970  65.616  39.131  1.00 114.33 ? 150 PHE D CZ   1 
ATOM   15048 H H    . PHE D 1 150 ? 11.246  60.006  42.852  1.00 129.70 ? 150 PHE D H    1 
ATOM   15049 H HA   . PHE D 1 150 ? 11.439  62.678  43.296  1.00 130.07 ? 150 PHE D HA   1 
ATOM   15050 H HB2  . PHE D 1 150 ? 13.063  62.340  41.722  1.00 129.73 ? 150 PHE D HB2  1 
ATOM   15051 H HB3  . PHE D 1 150 ? 12.096  61.424  40.855  1.00 129.73 ? 150 PHE D HB3  1 
ATOM   15052 H HD1  . PHE D 1 150 ? 10.167  62.547  39.688  1.00 136.20 ? 150 PHE D HD1  1 
ATOM   15053 H HD2  . PHE D 1 150 ? 13.173  64.647  41.283  1.00 139.62 ? 150 PHE D HD2  1 
ATOM   15054 H HE1  . PHE D 1 150 ? 9.529   64.387  38.461  1.00 133.84 ? 150 PHE D HE1  1 
ATOM   15055 H HE2  . PHE D 1 150 ? 12.531  66.491  40.051  1.00 140.43 ? 150 PHE D HE2  1 
ATOM   15056 H HZ   . PHE D 1 150 ? 10.716  66.357  38.630  1.00 137.19 ? 150 PHE D HZ   1 
ATOM   15057 N N    . ASN D 1 151 ? 9.078   62.997  42.756  1.00 113.67 ? 151 ASN D N    1 
ATOM   15058 C CA   . ASN D 1 151 ? 7.681   63.214  42.404  1.00 118.20 ? 151 ASN D CA   1 
ATOM   15059 C C    . ASN D 1 151 ? 7.602   64.264  41.304  1.00 122.19 ? 151 ASN D C    1 
ATOM   15060 O O    . ASN D 1 151 ? 8.155   65.360  41.449  1.00 122.65 ? 151 ASN D O    1 
ATOM   15061 C CB   . ASN D 1 151 ? 6.877   63.662  43.625  1.00 119.73 ? 151 ASN D CB   1 
ATOM   15062 C CG   . ASN D 1 151 ? 5.382   63.602  43.389  1.00 123.71 ? 151 ASN D CG   1 
ATOM   15063 O OD1  . ASN D 1 151 ? 4.924   63.576  42.244  1.00 129.02 ? 151 ASN D OD1  1 
ATOM   15064 N ND2  . ASN D 1 151 ? 4.611   63.572  44.469  1.00 125.26 ? 151 ASN D ND2  1 
ATOM   15065 H H    . ASN D 1 151 ? 9.387   63.589  43.298  1.00 136.40 ? 151 ASN D H    1 
ATOM   15066 H HA   . ASN D 1 151 ? 7.292   62.389  42.074  1.00 141.84 ? 151 ASN D HA   1 
ATOM   15067 H HB2  . ASN D 1 151 ? 7.087   63.081  44.373  1.00 143.68 ? 151 ASN D HB2  1 
ATOM   15068 H HB3  . ASN D 1 151 ? 7.111   64.578  43.840  1.00 143.68 ? 151 ASN D HB3  1 
ATOM   15069 H HD21 . ASN D 1 151 ? 4.968   63.587  45.252  1.00 150.31 ? 151 ASN D HD21 1 
ATOM   15070 H HD22 . ASN D 1 151 ? 3.756   63.538  44.387  1.00 150.31 ? 151 ASN D HD22 1 
ATOM   15071 N N    . ILE D 1 152 ? 6.914   63.931  40.209  1.00 118.85 ? 152 ILE D N    1 
ATOM   15072 C CA   . ILE D 1 152 ? 6.899   64.813  39.047  1.00 117.17 ? 152 ILE D CA   1 
ATOM   15073 C C    . ILE D 1 152 ? 5.903   65.950  39.242  1.00 120.67 ? 152 ILE D C    1 
ATOM   15074 O O    . ILE D 1 152 ? 6.229   67.122  39.025  1.00 122.35 ? 152 ILE D O    1 
ATOM   15075 C CB   . ILE D 1 152 ? 6.596   64.009  37.765  1.00 113.06 ? 152 ILE D CB   1 
ATOM   15076 C CG1  . ILE D 1 152 ? 7.239   62.619  37.850  1.00 111.39 ? 152 ILE D CG1  1 
ATOM   15077 C CG2  . ILE D 1 152 ? 7.088   64.783  36.545  1.00 108.97 ? 152 ILE D CG2  1 
ATOM   15078 C CD1  . ILE D 1 152 ? 7.215   61.818  36.547  1.00 104.25 ? 152 ILE D CD1  1 
ATOM   15079 H H    . ILE D 1 152 ? 6.455   63.210  40.118  1.00 142.62 ? 152 ILE D H    1 
ATOM   15080 H HA   . ILE D 1 152 ? 7.781   65.205  38.951  1.00 140.60 ? 152 ILE D HA   1 
ATOM   15081 H HB   . ILE D 1 152 ? 5.638   63.886  37.680  1.00 135.68 ? 152 ILE D HB   1 
ATOM   15082 H HG12 . ILE D 1 152 ? 8.167   62.725  38.110  1.00 133.67 ? 152 ILE D HG12 1 
ATOM   15083 H HG13 . ILE D 1 152 ? 6.764   62.101  38.519  1.00 133.67 ? 152 ILE D HG13 1 
ATOM   15084 H HG21 . ILE D 1 152 ? 6.870   64.281  35.744  1.00 130.77 ? 152 ILE D HG21 1 
ATOM   15085 H HG22 . ILE D 1 152 ? 6.650   65.648  36.522  1.00 130.77 ? 152 ILE D HG22 1 
ATOM   15086 H HG23 . ILE D 1 152 ? 8.048   64.900  36.611  1.00 130.77 ? 152 ILE D HG23 1 
ATOM   15087 H HD11 . ILE D 1 152 ? 7.619   60.950  36.703  1.00 125.10 ? 152 ILE D HD11 1 
ATOM   15088 H HD12 . ILE D 1 152 ? 6.294   61.708  36.261  1.00 125.10 ? 152 ILE D HD12 1 
ATOM   15089 H HD13 . ILE D 1 152 ? 7.716   62.299  35.871  1.00 125.10 ? 152 ILE D HD13 1 
ATOM   15090 N N    . LYS D 1 153 ? 4.671   65.624  39.640  1.00 120.23 ? 153 LYS D N    1 
ATOM   15091 C CA   . LYS D 1 153 ? 3.685   66.666  39.912  1.00 124.57 ? 153 LYS D CA   1 
ATOM   15092 C C    . LYS D 1 153 ? 4.216   67.650  40.949  1.00 128.17 ? 153 LYS D C    1 
ATOM   15093 O O    . LYS D 1 153 ? 4.187   68.868  40.740  1.00 130.16 ? 153 LYS D O    1 
ATOM   15094 C CB   . LYS D 1 153 ? 2.372   66.040  40.391  1.00 123.92 ? 153 LYS D CB   1 
ATOM   15095 C CG   . LYS D 1 153 ? 1.167   66.991  40.446  1.00 125.15 ? 153 LYS D CG   1 
ATOM   15096 C CD   . LYS D 1 153 ? 1.186   67.953  41.651  1.00 127.46 ? 153 LYS D CD   1 
ATOM   15097 C CE   . LYS D 1 153 ? 1.269   67.241  42.999  1.00 130.06 ? 153 LYS D CE   1 
ATOM   15098 N NZ   . LYS D 1 153 ? 0.004   66.547  43.366  1.00 124.58 ? 153 LYS D NZ   1 
ATOM   15099 H H    . LYS D 1 153 ? 4.387   64.821  39.758  1.00 144.28 ? 153 LYS D H    1 
ATOM   15100 H HA   . LYS D 1 153 ? 3.504   67.150  39.091  1.00 149.48 ? 153 LYS D HA   1 
ATOM   15101 H HB2  . LYS D 1 153 ? 2.141   65.316  39.788  1.00 148.70 ? 153 LYS D HB2  1 
ATOM   15102 H HB3  . LYS D 1 153 ? 2.507   65.694  41.287  1.00 148.70 ? 153 LYS D HB3  1 
ATOM   15103 H HG2  . LYS D 1 153 ? 1.156   67.529  39.639  1.00 150.17 ? 153 LYS D HG2  1 
ATOM   15104 H HG3  . LYS D 1 153 ? 0.355   66.463  40.503  1.00 150.17 ? 153 LYS D HG3  1 
ATOM   15105 H HD2  . LYS D 1 153 ? 1.959   68.534  41.575  1.00 152.95 ? 153 LYS D HD2  1 
ATOM   15106 H HD3  . LYS D 1 153 ? 0.372   68.480  41.644  1.00 152.95 ? 153 LYS D HD3  1 
ATOM   15107 H HE2  . LYS D 1 153 ? 1.975   66.577  42.963  1.00 156.07 ? 153 LYS D HE2  1 
ATOM   15108 H HE3  . LYS D 1 153 ? 1.462   67.894  43.690  1.00 156.07 ? 153 LYS D HE3  1 
ATOM   15109 H HZ1  . LYS D 1 153 ? 0.098   66.136  44.150  1.00 149.49 ? 153 LYS D HZ1  1 
ATOM   15110 H HZ2  . LYS D 1 153 ? -0.660  67.136  43.428  1.00 149.49 ? 153 LYS D HZ2  1 
ATOM   15111 H HZ3  . LYS D 1 153 ? -0.203  65.942  42.746  1.00 149.49 ? 153 LYS D HZ3  1 
ATOM   15112 N N    . GLU D 1 154 ? 4.703   67.136  42.081  1.00 138.05 ? 154 GLU D N    1 
ATOM   15113 C CA   . GLU D 1 154 ? 5.175   68.015  43.145  1.00 136.11 ? 154 GLU D CA   1 
ATOM   15114 C C    . GLU D 1 154 ? 6.372   68.840  42.692  1.00 134.41 ? 154 GLU D C    1 
ATOM   15115 O O    . GLU D 1 154 ? 6.478   70.028  43.020  1.00 140.57 ? 154 GLU D O    1 
ATOM   15116 C CB   . GLU D 1 154 ? 5.532   67.194  44.384  1.00 143.24 ? 154 GLU D CB   1 
ATOM   15117 C CG   . GLU D 1 154 ? 4.349   66.506  45.040  1.00 145.26 ? 154 GLU D CG   1 
ATOM   15118 C CD   . GLU D 1 154 ? 3.458   67.469  45.798  1.00 155.48 ? 154 GLU D CD   1 
ATOM   15119 O OE1  . GLU D 1 154 ? 3.886   68.618  46.040  1.00 159.11 ? 154 GLU D OE1  1 
ATOM   15120 O OE2  . GLU D 1 154 ? 2.327   67.073  46.152  1.00 162.26 ? 154 GLU D OE2  1 
ATOM   15121 H H    . GLU D 1 154 ? 4.771   66.296  42.252  1.00 165.66 ? 154 GLU D H    1 
ATOM   15122 H HA   . GLU D 1 154 ? 4.459   68.626  43.382  1.00 163.32 ? 154 GLU D HA   1 
ATOM   15123 H HB2  . GLU D 1 154 ? 6.167   66.507  44.127  1.00 171.89 ? 154 GLU D HB2  1 
ATOM   15124 H HB3  . GLU D 1 154 ? 5.930   67.785  45.042  1.00 171.89 ? 154 GLU D HB3  1 
ATOM   15125 H HG2  . GLU D 1 154 ? 3.813   66.076  44.355  1.00 174.32 ? 154 GLU D HG2  1 
ATOM   15126 H HG3  . GLU D 1 154 ? 4.677   65.843  45.668  1.00 174.32 ? 154 GLU D HG3  1 
ATOM   15127 N N    . ASN D 1 155 ? 7.283   68.234  41.946  1.00 126.89 ? 155 ASN D N    1 
ATOM   15128 C CA   . ASN D 1 155 ? 8.459   68.935  41.458  1.00 127.03 ? 155 ASN D CA   1 
ATOM   15129 C C    . ASN D 1 155 ? 8.138   69.669  40.157  1.00 129.96 ? 155 ASN D C    1 
ATOM   15130 O O    . ASN D 1 155 ? 7.068   69.507  39.568  1.00 131.42 ? 155 ASN D O    1 
ATOM   15131 C CB   . ASN D 1 155 ? 9.615   67.958  41.261  1.00 124.65 ? 155 ASN D CB   1 
ATOM   15132 C CG   . ASN D 1 155 ? 10.955  68.577  41.593  1.00 124.39 ? 155 ASN D CG   1 
ATOM   15133 O OD1  . ASN D 1 155 ? 11.213  68.957  42.736  1.00 122.53 ? 155 ASN D OD1  1 
ATOM   15134 N ND2  . ASN D 1 155 ? 11.817  68.690  40.589  1.00 123.51 ? 155 ASN D ND2  1 
ATOM   15135 H H    . ASN D 1 155 ? 7.243   67.409  41.706  1.00 152.27 ? 155 ASN D H    1 
ATOM   15136 H HA   . ASN D 1 155 ? 8.736   69.594  42.114  1.00 152.43 ? 155 ASN D HA   1 
ATOM   15137 H HB2  . ASN D 1 155 ? 9.485   67.191  41.841  1.00 149.58 ? 155 ASN D HB2  1 
ATOM   15138 H HB3  . ASN D 1 155 ? 9.636   67.674  40.334  1.00 149.58 ? 155 ASN D HB3  1 
ATOM   15139 H HD21 . ASN D 1 155 ? 11.599  68.418  39.802  1.00 148.21 ? 155 ASN D HD21 1 
ATOM   15140 H HD22 . ASN D 1 155 ? 12.593  69.035  40.725  1.00 148.21 ? 155 ASN D HD22 1 
ATOM   15141 N N    . LYS D 1 156 ? 9.087   70.489  39.710  1.00 127.01 ? 156 LYS D N    1 
ATOM   15142 C CA   . LYS D 1 156 ? 8.893   71.337  38.547  1.00 126.65 ? 156 LYS D CA   1 
ATOM   15143 C C    . LYS D 1 156 ? 9.474   70.680  37.293  1.00 127.50 ? 156 LYS D C    1 
ATOM   15144 O O    . LYS D 1 156 ? 10.029  69.579  37.333  1.00 126.61 ? 156 LYS D O    1 
ATOM   15145 C CB   . LYS D 1 156 ? 9.523   72.712  38.785  1.00 127.65 ? 156 LYS D CB   1 
ATOM   15146 C CG   . LYS D 1 156 ? 9.012   73.448  40.028  1.00 133.06 ? 156 LYS D CG   1 
ATOM   15147 C CD   . LYS D 1 156 ? 7.535   73.182  40.297  1.00 133.84 ? 156 LYS D CD   1 
ATOM   15148 C CE   . LYS D 1 156 ? 7.027   73.952  41.518  1.00 126.66 ? 156 LYS D CE   1 
ATOM   15149 N NZ   . LYS D 1 156 ? 7.834   75.168  41.823  1.00 133.82 ? 156 LYS D NZ   1 
ATOM   15150 H H    . LYS D 1 156 ? 9.863   70.570  40.072  1.00 152.42 ? 156 LYS D H    1 
ATOM   15151 H HA   . LYS D 1 156 ? 7.940   71.451  38.407  1.00 151.98 ? 156 LYS D HA   1 
ATOM   15152 H HB2  . LYS D 1 156 ? 10.481  72.598  38.887  1.00 153.18 ? 156 LYS D HB2  1 
ATOM   15153 H HB3  . LYS D 1 156 ? 9.336   73.274  38.017  1.00 153.18 ? 156 LYS D HB3  1 
ATOM   15154 H HG2  . LYS D 1 156 ? 9.517   73.152  40.802  1.00 159.67 ? 156 LYS D HG2  1 
ATOM   15155 H HG3  . LYS D 1 156 ? 9.127   74.403  39.902  1.00 159.67 ? 156 LYS D HG3  1 
ATOM   15156 H HD2  . LYS D 1 156 ? 7.015   73.458  39.527  1.00 160.61 ? 156 LYS D HD2  1 
ATOM   15157 H HD3  . LYS D 1 156 ? 7.406   72.234  40.462  1.00 160.61 ? 156 LYS D HD3  1 
ATOM   15158 H HE2  . LYS D 1 156 ? 6.113   74.234  41.354  1.00 151.99 ? 156 LYS D HE2  1 
ATOM   15159 H HE3  . LYS D 1 156 ? 7.059   73.370  42.294  1.00 151.99 ? 156 LYS D HE3  1 
ATOM   15160 H HZ1  . LYS D 1 156 ? 7.447   75.634  42.475  1.00 160.58 ? 156 LYS D HZ1  1 
ATOM   15161 H HZ2  . LYS D 1 156 ? 8.652   74.932  42.083  1.00 160.58 ? 156 LYS D HZ2  1 
ATOM   15162 H HZ3  . LYS D 1 156 ? 7.898   75.681  41.099  1.00 160.58 ? 156 LYS D HZ3  1 
ATOM   15163 N N    . GLU D 1 157 ? 9.337   71.378  36.161  1.00 128.84 ? 157 GLU D N    1 
ATOM   15164 C CA   . GLU D 1 157 ? 9.801   70.855  34.882  1.00 128.69 ? 157 GLU D CA   1 
ATOM   15165 C C    . GLU D 1 157 ? 11.261  70.430  34.971  1.00 128.53 ? 157 GLU D C    1 
ATOM   15166 O O    . GLU D 1 157 ? 12.091  71.122  35.566  1.00 127.69 ? 157 GLU D O    1 
ATOM   15167 C CB   . GLU D 1 157 ? 9.637   71.907  33.782  1.00 130.50 ? 157 GLU D CB   1 
ATOM   15168 C CG   . GLU D 1 157 ? 9.143   71.350  32.448  1.00 135.28 ? 157 GLU D CG   1 
ATOM   15169 C CD   . GLU D 1 157 ? 10.269  71.078  31.456  1.00 136.19 ? 157 GLU D CD   1 
ATOM   15170 O OE1  . GLU D 1 157 ? 11.230  71.878  31.397  1.00 134.97 ? 157 GLU D OE1  1 
ATOM   15171 O OE2  . GLU D 1 157 ? 10.182  70.066  30.729  1.00 133.11 ? 157 GLU D OE2  1 
ATOM   15172 H H    . GLU D 1 157 ? 8.978   72.157  36.111  1.00 154.61 ? 157 GLU D H    1 
ATOM   15173 H HA   . GLU D 1 157 ? 9.266   70.080  34.648  1.00 154.43 ? 157 GLU D HA   1 
ATOM   15174 H HB2  . GLU D 1 157 ? 8.993   72.569  34.080  1.00 156.60 ? 157 GLU D HB2  1 
ATOM   15175 H HB3  . GLU D 1 157 ? 10.496  72.327  33.624  1.00 156.60 ? 157 GLU D HB3  1 
ATOM   15176 H HG2  . GLU D 1 157 ? 8.679   70.513  32.610  1.00 162.33 ? 157 GLU D HG2  1 
ATOM   15177 H HG3  . GLU D 1 157 ? 8.538   71.991  32.044  1.00 162.33 ? 157 GLU D HG3  1 
ATOM   15178 N N    . THR D 1 158 ? 11.569  69.292  34.353  1.00 127.85 ? 158 THR D N    1 
ATOM   15179 C CA   . THR D 1 158 ? 12.911  68.739  34.407  1.00 128.35 ? 158 THR D CA   1 
ATOM   15180 C C    . THR D 1 158 ? 13.076  67.698  33.310  1.00 134.85 ? 158 THR D C    1 
ATOM   15181 O O    . THR D 1 158 ? 12.122  67.328  32.623  1.00 134.76 ? 158 THR D O    1 
ATOM   15182 C CB   . THR D 1 158 ? 13.195  68.099  35.771  1.00 129.54 ? 158 THR D CB   1 
ATOM   15183 O OG1  . THR D 1 158 ? 14.430  67.375  35.711  1.00 129.01 ? 158 THR D OG1  1 
ATOM   15184 C CG2  . THR D 1 158 ? 12.067  67.137  36.142  1.00 129.01 ? 158 THR D CG2  1 
ATOM   15185 H H    . THR D 1 158 ? 11.013  68.821  33.895  1.00 153.42 ? 158 THR D H    1 
ATOM   15186 H HA   . THR D 1 158 ? 13.541  69.459  34.247  1.00 154.03 ? 158 THR D HA   1 
ATOM   15187 H HB   . THR D 1 158 ? 13.256  68.788  36.451  1.00 155.45 ? 158 THR D HB   1 
ATOM   15188 H HG1  . THR D 1 158 ? 14.602  67.038  36.461  1.00 154.81 ? 158 THR D HG1  1 
ATOM   15189 H HG21 . THR D 1 158 ? 12.264  66.707  36.989  1.00 154.81 ? 158 THR D HG21 1 
ATOM   15190 H HG22 . THR D 1 158 ? 11.231  67.622  36.222  1.00 154.81 ? 158 THR D HG22 1 
ATOM   15191 H HG23 . THR D 1 158 ? 11.973  66.456  35.458  1.00 154.81 ? 158 THR D HG23 1 
ATOM   15192 N N    . SER D 1 159 ? 14.310  67.223  33.166  1.00 135.30 ? 159 SER D N    1 
ATOM   15193 C CA   . SER D 1 159 ? 14.642  66.098  32.306  1.00 129.55 ? 159 SER D CA   1 
ATOM   15194 C C    . SER D 1 159 ? 15.122  64.943  33.175  1.00 129.38 ? 159 SER D C    1 
ATOM   15195 O O    . SER D 1 159 ? 15.809  65.158  34.180  1.00 133.13 ? 159 SER D O    1 
ATOM   15196 C CB   . SER D 1 159 ? 15.729  66.471  31.298  1.00 133.30 ? 159 SER D CB   1 
ATOM   15197 O OG   . SER D 1 159 ? 16.561  65.358  31.025  1.00 139.26 ? 159 SER D OG   1 
ATOM   15198 H H    . SER D 1 159 ? 14.994  67.550  33.572  1.00 162.37 ? 159 SER D H    1 
ATOM   15199 H HA   . SER D 1 159 ? 13.858  65.819  31.807  1.00 155.46 ? 159 SER D HA   1 
ATOM   15200 H HB2  . SER D 1 159 ? 15.309  66.762  30.474  1.00 159.96 ? 159 SER D HB2  1 
ATOM   15201 H HB3  . SER D 1 159 ? 16.269  67.187  31.666  1.00 159.96 ? 159 SER D HB3  1 
ATOM   15202 H HG   . SER D 1 159 ? 17.167  65.578  30.487  1.00 167.11 ? 159 SER D HG   1 
ATOM   15203 N N    . PHE D 1 160 ? 14.754  63.719  32.794  1.00 125.32 ? 160 PHE D N    1 
ATOM   15204 C CA   . PHE D 1 160 ? 15.209  62.553  33.544  1.00 120.08 ? 160 PHE D CA   1 
ATOM   15205 C C    . PHE D 1 160 ? 16.730  62.538  33.638  1.00 126.13 ? 160 PHE D C    1 
ATOM   15206 O O    . PHE D 1 160 ? 17.300  62.528  34.735  1.00 126.12 ? 160 PHE D O    1 
ATOM   15207 C CB   . PHE D 1 160 ? 14.699  61.269  32.891  1.00 113.35 ? 160 PHE D CB   1 
ATOM   15208 C CG   . PHE D 1 160 ? 13.312  60.880  33.310  1.00 104.10 ? 160 PHE D CG   1 
ATOM   15209 C CD1  . PHE D 1 160 ? 12.372  61.842  33.638  1.00 102.02 ? 160 PHE D CD1  1 
ATOM   15210 C CD2  . PHE D 1 160 ? 12.946  59.546  33.370  1.00 103.97 ? 160 PHE D CD2  1 
ATOM   15211 C CE1  . PHE D 1 160 ? 11.096  61.481  34.016  1.00 98.50  ? 160 PHE D CE1  1 
ATOM   15212 C CE2  . PHE D 1 160 ? 11.671  59.178  33.750  1.00 99.50  ? 160 PHE D CE2  1 
ATOM   15213 C CZ   . PHE D 1 160 ? 10.744  60.147  34.071  1.00 94.21  ? 160 PHE D CZ   1 
ATOM   15214 H H    . PHE D 1 160 ? 14.252  63.542  32.119  1.00 150.38 ? 160 PHE D H    1 
ATOM   15215 H HA   . PHE D 1 160 ? 14.841  62.595  34.441  1.00 144.10 ? 160 PHE D HA   1 
ATOM   15216 H HB2  . PHE D 1 160 ? 14.693  61.392  31.929  1.00 136.03 ? 160 PHE D HB2  1 
ATOM   15217 H HB3  . PHE D 1 160 ? 15.295  60.542  33.130  1.00 136.03 ? 160 PHE D HB3  1 
ATOM   15218 H HD1  . PHE D 1 160 ? 12.603  62.742  33.602  1.00 122.42 ? 160 PHE D HD1  1 
ATOM   15219 H HD2  . PHE D 1 160 ? 13.567  58.890  33.150  1.00 124.77 ? 160 PHE D HD2  1 
ATOM   15220 H HE1  . PHE D 1 160 ? 10.472  62.135  34.235  1.00 118.20 ? 160 PHE D HE1  1 
ATOM   15221 H HE2  . PHE D 1 160 ? 11.438  58.279  33.791  1.00 119.41 ? 160 PHE D HE2  1 
ATOM   15222 H HZ   . PHE D 1 160 ? 9.883   59.902  34.323  1.00 113.05 ? 160 PHE D HZ   1 
ATOM   15223 N N    . GLU D 1 161 ? 17.407  62.566  32.487  1.00 132.88 ? 161 GLU D N    1 
ATOM   15224 C CA   . GLU D 1 161 ? 18.866  62.523  32.482  1.00 132.38 ? 161 GLU D CA   1 
ATOM   15225 C C    . GLU D 1 161 ? 19.454  63.656  33.315  1.00 133.12 ? 161 GLU D C    1 
ATOM   15226 O O    . GLU D 1 161 ? 20.495  63.492  33.961  1.00 136.85 ? 161 GLU D O    1 
ATOM   15227 C CB   . GLU D 1 161 ? 19.392  62.587  31.050  1.00 133.64 ? 161 GLU D CB   1 
ATOM   15228 C CG   . GLU D 1 161 ? 20.903  62.435  30.945  1.00 136.35 ? 161 GLU D CG   1 
ATOM   15229 C CD   . GLU D 1 161 ? 21.399  61.096  31.467  1.00 137.31 ? 161 GLU D CD   1 
ATOM   15230 O OE1  . GLU D 1 161 ? 20.663  60.093  31.348  1.00 137.82 ? 161 GLU D OE1  1 
ATOM   15231 O OE2  . GLU D 1 161 ? 22.529  61.045  31.998  1.00 131.89 ? 161 GLU D OE2  1 
ATOM   15232 H H    . GLU D 1 161 ? 17.048  62.608  31.706  1.00 159.45 ? 161 GLU D H    1 
ATOM   15233 H HA   . GLU D 1 161 ? 19.152  61.681  32.870  1.00 158.85 ? 161 GLU D HA   1 
ATOM   15234 H HB2  . GLU D 1 161 ? 18.985  61.873  30.536  1.00 160.36 ? 161 GLU D HB2  1 
ATOM   15235 H HB3  . GLU D 1 161 ? 19.154  63.447  30.669  1.00 160.36 ? 161 GLU D HB3  1 
ATOM   15236 H HG2  . GLU D 1 161 ? 21.164  62.508  30.013  1.00 163.62 ? 161 GLU D HG2  1 
ATOM   15237 H HG3  . GLU D 1 161 ? 21.329  63.135  31.464  1.00 163.62 ? 161 GLU D HG3  1 
ATOM   15238 N N    . ASN D 1 162 ? 18.812  64.826  33.301  1.00 130.23 ? 162 ASN D N    1 
ATOM   15239 C CA   . ASN D 1 162 ? 19.283  65.938  34.124  1.00 130.93 ? 162 ASN D CA   1 
ATOM   15240 C C    . ASN D 1 162 ? 19.333  65.538  35.595  1.00 128.47 ? 162 ASN D C    1 
ATOM   15241 O O    . ASN D 1 162 ? 20.378  65.650  36.247  1.00 128.98 ? 162 ASN D O    1 
ATOM   15242 C CB   . ASN D 1 162 ? 18.381  67.156  33.905  1.00 131.74 ? 162 ASN D CB   1 
ATOM   15243 C CG   . ASN D 1 162 ? 18.450  68.151  35.041  1.00 132.01 ? 162 ASN D CG   1 
ATOM   15244 O OD1  . ASN D 1 162 ? 19.530  68.476  35.535  1.00 135.43 ? 162 ASN D OD1  1 
ATOM   15245 N ND2  . ASN D 1 162 ? 17.292  68.649  35.457  1.00 132.03 ? 162 ASN D ND2  1 
ATOM   15246 H H    . ASN D 1 162 ? 18.112  64.998  32.831  1.00 156.27 ? 162 ASN D H    1 
ATOM   15247 H HA   . ASN D 1 162 ? 20.182  66.183  33.856  1.00 157.12 ? 162 ASN D HA   1 
ATOM   15248 H HB2  . ASN D 1 162 ? 18.656  67.609  33.092  1.00 158.08 ? 162 ASN D HB2  1 
ATOM   15249 H HB3  . ASN D 1 162 ? 17.462  66.857  33.824  1.00 158.08 ? 162 ASN D HB3  1 
ATOM   15250 H HD21 . ASN D 1 162 ? 16.558  68.402  35.083  1.00 158.43 ? 162 ASN D HD21 1 
ATOM   15251 H HD22 . ASN D 1 162 ? 17.276  69.220  36.100  1.00 158.43 ? 162 ASN D HD22 1 
ATOM   15252 N N    . ILE D 1 163 ? 18.214  65.042  36.129  1.00 128.82 ? 163 ILE D N    1 
ATOM   15253 C CA   . ILE D 1 163 ? 18.183  64.588  37.518  1.00 127.84 ? 163 ILE D CA   1 
ATOM   15254 C C    . ILE D 1 163 ? 19.243  63.523  37.753  1.00 126.30 ? 163 ILE D C    1 
ATOM   15255 O O    . ILE D 1 163 ? 19.945  63.536  38.772  1.00 124.39 ? 163 ILE D O    1 
ATOM   15256 C CB   . ILE D 1 163 ? 16.778  64.065  37.874  1.00 122.28 ? 163 ILE D CB   1 
ATOM   15257 C CG1  . ILE D 1 163 ? 15.833  65.246  38.072  1.00 120.52 ? 163 ILE D CG1  1 
ATOM   15258 C CG2  . ILE D 1 163 ? 16.815  63.164  39.106  1.00 116.62 ? 163 ILE D CG2  1 
ATOM   15259 C CD1  . ILE D 1 163 ? 14.395  64.856  38.047  1.00 117.46 ? 163 ILE D CD1  1 
ATOM   15260 H H    . ILE D 1 163 ? 17.466  64.959  35.712  1.00 154.58 ? 163 ILE D H    1 
ATOM   15261 H HA   . ILE D 1 163 ? 18.383  65.344  38.092  1.00 153.41 ? 163 ILE D HA   1 
ATOM   15262 H HB   . ILE D 1 163 ? 16.452  63.523  37.139  1.00 146.74 ? 163 ILE D HB   1 
ATOM   15263 H HG12 . ILE D 1 163 ? 16.017  65.655  38.932  1.00 144.63 ? 163 ILE D HG12 1 
ATOM   15264 H HG13 . ILE D 1 163 ? 15.980  65.889  37.361  1.00 144.63 ? 163 ILE D HG13 1 
ATOM   15265 H HG21 . ILE D 1 163 ? 15.911  62.880  39.316  1.00 139.95 ? 163 ILE D HG21 1 
ATOM   15266 H HG22 . ILE D 1 163 ? 17.369  62.391  38.915  1.00 139.95 ? 163 ILE D HG22 1 
ATOM   15267 H HG23 . ILE D 1 163 ? 17.186  63.663  39.850  1.00 139.95 ? 163 ILE D HG23 1 
ATOM   15268 H HD11 . ILE D 1 163 ? 13.850  65.654  38.134  1.00 140.96 ? 163 ILE D HD11 1 
ATOM   15269 H HD12 . ILE D 1 163 ? 14.202  64.414  37.206  1.00 140.96 ? 163 ILE D HD12 1 
ATOM   15270 H HD13 . ILE D 1 163 ? 14.219  64.253  38.786  1.00 140.96 ? 163 ILE D HD13 1 
ATOM   15271 N N    . ILE D 1 164 ? 19.353  62.568  36.828  1.00 124.87 ? 164 ILE D N    1 
ATOM   15272 C CA   . ILE D 1 164 ? 20.307  61.472  36.985  1.00 122.76 ? 164 ILE D CA   1 
ATOM   15273 C C    . ILE D 1 164 ? 21.699  62.025  37.253  1.00 124.51 ? 164 ILE D C    1 
ATOM   15274 O O    . ILE D 1 164 ? 22.377  61.616  38.201  1.00 123.70 ? 164 ILE D O    1 
ATOM   15275 C CB   . ILE D 1 164 ? 20.275  60.552  35.747  1.00 124.11 ? 164 ILE D CB   1 
ATOM   15276 C CG1  . ILE D 1 164 ? 18.869  59.951  35.627  1.00 120.92 ? 164 ILE D CG1  1 
ATOM   15277 C CG2  . ILE D 1 164 ? 21.372  59.505  35.827  1.00 122.47 ? 164 ILE D CG2  1 
ATOM   15278 C CD1  . ILE D 1 164 ? 18.804  58.616  34.939  1.00 117.39 ? 164 ILE D CD1  1 
ATOM   15279 H H    . ILE D 1 164 ? 18.889  62.531  36.105  1.00 149.85 ? 164 ILE D H    1 
ATOM   15280 H HA   . ILE D 1 164 ? 20.051  60.938  37.753  1.00 147.31 ? 164 ILE D HA   1 
ATOM   15281 H HB   . ILE D 1 164 ? 20.456  61.060  34.940  1.00 148.93 ? 164 ILE D HB   1 
ATOM   15282 H HG12 . ILE D 1 164 ? 18.507  59.835  36.520  1.00 145.10 ? 164 ILE D HG12 1 
ATOM   15283 H HG13 . ILE D 1 164 ? 18.314  60.566  35.121  1.00 145.10 ? 164 ILE D HG13 1 
ATOM   15284 H HG21 . ILE D 1 164 ? 21.344  58.957  35.027  1.00 146.96 ? 164 ILE D HG21 1 
ATOM   15285 H HG22 . ILE D 1 164 ? 22.231  59.951  35.892  1.00 146.96 ? 164 ILE D HG22 1 
ATOM   15286 H HG23 . ILE D 1 164 ? 21.225  58.953  36.611  1.00 146.96 ? 164 ILE D HG23 1 
ATOM   15287 H HD11 . ILE D 1 164 ? 17.894  58.458  34.641  1.00 140.87 ? 164 ILE D HD11 1 
ATOM   15288 H HD12 . ILE D 1 164 ? 19.404  58.624  34.177  1.00 140.87 ? 164 ILE D HD12 1 
ATOM   15289 H HD13 . ILE D 1 164 ? 19.072  57.925  35.564  1.00 140.87 ? 164 ILE D HD13 1 
ATOM   15290 N N    . ASP D 1 165 ? 22.138  62.978  36.430  1.00 126.58 ? 165 ASP D N    1 
ATOM   15291 C CA   . ASP D 1 165 ? 23.448  63.580  36.644  1.00 125.59 ? 165 ASP D CA   1 
ATOM   15292 C C    . ASP D 1 165 ? 23.526  64.235  38.018  1.00 128.46 ? 165 ASP D C    1 
ATOM   15293 O O    . ASP D 1 165 ? 24.504  64.051  38.754  1.00 129.20 ? 165 ASP D O    1 
ATOM   15294 C CB   . ASP D 1 165 ? 23.746  64.602  35.548  1.00 126.22 ? 165 ASP D CB   1 
ATOM   15295 C CG   . ASP D 1 165 ? 25.131  65.204  35.679  1.00 128.09 ? 165 ASP D CG   1 
ATOM   15296 O OD1  . ASP D 1 165 ? 26.110  64.427  35.713  1.00 130.19 ? 165 ASP D OD1  1 
ATOM   15297 O OD2  . ASP D 1 165 ? 25.244  66.448  35.757  1.00 124.72 ? 165 ASP D OD2  1 
ATOM   15298 H H    . ASP D 1 165 ? 21.704  63.286  35.754  1.00 151.90 ? 165 ASP D H    1 
ATOM   15299 H HA   . ASP D 1 165 ? 24.123  62.884  36.596  1.00 150.72 ? 165 ASP D HA   1 
ATOM   15300 H HB2  . ASP D 1 165 ? 23.688  64.166  34.683  1.00 151.46 ? 165 ASP D HB2  1 
ATOM   15301 H HB3  . ASP D 1 165 ? 23.098  65.322  35.601  1.00 151.46 ? 165 ASP D HB3  1 
ATOM   15302 N N    . LEU D 1 166 ? 22.499  65.006  38.382  1.00 127.80 ? 166 LEU D N    1 
ATOM   15303 C CA   . LEU D 1 166 ? 22.488  65.660  39.686  1.00 126.31 ? 166 LEU D CA   1 
ATOM   15304 C C    . LEU D 1 166 ? 22.666  64.642  40.805  1.00 124.98 ? 166 LEU D C    1 
ATOM   15305 O O    . LEU D 1 166 ? 23.532  64.800  41.674  1.00 126.19 ? 166 LEU D O    1 
ATOM   15306 C CB   . LEU D 1 166 ? 21.186  66.436  39.872  1.00 127.82 ? 166 LEU D CB   1 
ATOM   15307 C CG   . LEU D 1 166 ? 20.889  67.556  38.877  1.00 132.97 ? 166 LEU D CG   1 
ATOM   15308 C CD1  . LEU D 1 166 ? 19.649  68.320  39.333  1.00 135.84 ? 166 LEU D CD1  1 
ATOM   15309 C CD2  . LEU D 1 166 ? 22.071  68.494  38.720  1.00 137.40 ? 166 LEU D CD2  1 
ATOM   15310 H H    . LEU D 1 166 ? 21.806  65.164  37.897  1.00 153.36 ? 166 LEU D H    1 
ATOM   15311 H HA   . LEU D 1 166 ? 23.225  66.291  39.725  1.00 151.57 ? 166 LEU D HA   1 
ATOM   15312 H HB2  . LEU D 1 166 ? 20.453  65.804  39.813  1.00 153.38 ? 166 LEU D HB2  1 
ATOM   15313 H HB3  . LEU D 1 166 ? 21.205  66.840  40.754  1.00 153.38 ? 166 LEU D HB3  1 
ATOM   15314 H HG   . LEU D 1 166 ? 20.722  67.169  38.003  1.00 159.57 ? 166 LEU D HG   1 
ATOM   15315 H HD11 . LEU D 1 166 ? 19.559  69.124  38.798  1.00 163.01 ? 166 LEU D HD11 1 
ATOM   15316 H HD12 . LEU D 1 166 ? 18.869  67.756  39.215  1.00 163.01 ? 166 LEU D HD12 1 
ATOM   15317 H HD13 . LEU D 1 166 ? 19.749  68.555  40.269  1.00 163.01 ? 166 LEU D HD13 1 
ATOM   15318 H HD21 . LEU D 1 166 ? 21.801  69.254  38.182  1.00 164.88 ? 166 LEU D HD21 1 
ATOM   15319 H HD22 . LEU D 1 166 ? 22.355  68.793  39.598  1.00 164.88 ? 166 LEU D HD22 1 
ATOM   15320 H HD23 . LEU D 1 166 ? 22.794  68.019  38.282  1.00 164.88 ? 166 LEU D HD23 1 
ATOM   15321 N N    . VAL D 1 167 ? 21.847  63.589  40.802  1.00 125.88 ? 167 VAL D N    1 
ATOM   15322 C CA   . VAL D 1 167 ? 21.975  62.546  41.816  1.00 125.33 ? 167 VAL D CA   1 
ATOM   15323 C C    . VAL D 1 167 ? 23.386  61.970  41.794  1.00 127.66 ? 167 VAL D C    1 
ATOM   15324 O O    . VAL D 1 167 ? 24.101  61.991  42.800  1.00 130.73 ? 167 VAL D O    1 
ATOM   15325 C CB   . VAL D 1 167 ? 20.916  61.452  41.603  1.00 116.88 ? 167 VAL D CB   1 
ATOM   15326 C CG1  . VAL D 1 167 ? 21.153  60.293  42.556  1.00 111.31 ? 167 VAL D CG1  1 
ATOM   15327 C CG2  . VAL D 1 167 ? 19.517  62.024  41.784  1.00 113.93 ? 167 VAL D CG2  1 
ATOM   15328 H H    . VAL D 1 167 ? 21.218  63.458  40.231  1.00 151.06 ? 167 VAL D H    1 
ATOM   15329 H HA   . VAL D 1 167 ? 21.823  62.940  42.689  1.00 150.39 ? 167 VAL D HA   1 
ATOM   15330 H HB   . VAL D 1 167 ? 20.986  61.114  40.696  1.00 140.26 ? 167 VAL D HB   1 
ATOM   15331 H HG11 . VAL D 1 167 ? 20.329  59.790  42.653  1.00 133.58 ? 167 VAL D HG11 1 
ATOM   15332 H HG12 . VAL D 1 167 ? 21.848  59.722  42.193  1.00 133.58 ? 167 VAL D HG12 1 
ATOM   15333 H HG13 . VAL D 1 167 ? 21.430  60.644  43.417  1.00 133.58 ? 167 VAL D HG13 1 
ATOM   15334 H HG21 . VAL D 1 167 ? 18.923  61.318  42.082  1.00 136.71 ? 167 VAL D HG21 1 
ATOM   15335 H HG22 . VAL D 1 167 ? 19.549  62.731  42.448  1.00 136.71 ? 167 VAL D HG22 1 
ATOM   15336 H HG23 . VAL D 1 167 ? 19.209  62.380  40.936  1.00 136.71 ? 167 VAL D HG23 1 
ATOM   15337 N N    . LYS D 1 168 ? 23.816  61.474  40.631  1.00 124.92 ? 168 LYS D N    1 
ATOM   15338 C CA   . LYS D 1 168 ? 25.143  60.876  40.529  1.00 126.87 ? 168 LYS D CA   1 
ATOM   15339 C C    . LYS D 1 168 ? 26.221  61.780  41.114  1.00 128.55 ? 168 LYS D C    1 
ATOM   15340 O O    . LYS D 1 168 ? 27.205  61.288  41.677  1.00 130.51 ? 168 LYS D O    1 
ATOM   15341 C CB   . LYS D 1 168 ? 25.471  60.564  39.066  1.00 127.64 ? 168 LYS D CB   1 
ATOM   15342 C CG   . LYS D 1 168 ? 24.541  59.564  38.407  1.00 123.63 ? 168 LYS D CG   1 
ATOM   15343 C CD   . LYS D 1 168 ? 24.727  59.568  36.896  1.00 125.96 ? 168 LYS D CD   1 
ATOM   15344 C CE   . LYS D 1 168 ? 26.165  59.237  36.505  1.00 129.53 ? 168 LYS D CE   1 
ATOM   15345 N NZ   . LYS D 1 168 ? 27.038  60.448  36.444  1.00 130.64 ? 168 LYS D NZ   1 
ATOM   15346 H H    . LYS D 1 168 ? 23.365  61.472  39.899  1.00 149.91 ? 168 LYS D H    1 
ATOM   15347 H HA   . LYS D 1 168 ? 25.141  60.043  41.027  1.00 152.25 ? 168 LYS D HA   1 
ATOM   15348 H HB2  . LYS D 1 168 ? 25.422  61.388  38.557  1.00 153.17 ? 168 LYS D HB2  1 
ATOM   15349 H HB3  . LYS D 1 168 ? 26.369  60.200  39.023  1.00 153.17 ? 168 LYS D HB3  1 
ATOM   15350 H HG2  . LYS D 1 168 ? 24.735  58.674  38.739  1.00 148.36 ? 168 LYS D HG2  1 
ATOM   15351 H HG3  . LYS D 1 168 ? 23.621  59.799  38.604  1.00 148.36 ? 168 LYS D HG3  1 
ATOM   15352 H HD2  . LYS D 1 168 ? 24.143  58.902  36.500  1.00 151.15 ? 168 LYS D HD2  1 
ATOM   15353 H HD3  . LYS D 1 168 ? 24.512  60.447  36.549  1.00 151.15 ? 168 LYS D HD3  1 
ATOM   15354 H HE2  . LYS D 1 168 ? 26.540  58.629  37.161  1.00 155.44 ? 168 LYS D HE2  1 
ATOM   15355 H HE3  . LYS D 1 168 ? 26.166  58.822  35.628  1.00 155.44 ? 168 LYS D HE3  1 
ATOM   15356 H HZ1  . LYS D 1 168 ? 27.223  60.731  37.268  1.00 156.77 ? 168 LYS D HZ1  1 
ATOM   15357 H HZ2  . LYS D 1 168 ? 27.800  60.253  36.028  1.00 156.77 ? 168 LYS D HZ2  1 
ATOM   15358 H HZ3  . LYS D 1 168 ? 26.626  61.100  36.000  1.00 156.77 ? 168 LYS D HZ3  1 
ATOM   15359 N N    . LYS D 1 169 ? 26.062  63.100  40.986  1.00 128.43 ? 169 LYS D N    1 
ATOM   15360 C CA   . LYS D 1 169 ? 27.007  64.024  41.601  1.00 132.12 ? 169 LYS D CA   1 
ATOM   15361 C C    . LYS D 1 169 ? 26.783  64.154  43.108  1.00 132.76 ? 169 LYS D C    1 
ATOM   15362 O O    . LYS D 1 169 ? 27.710  64.542  43.829  1.00 133.54 ? 169 LYS D O    1 
ATOM   15363 C CB   . LYS D 1 169 ? 26.917  65.403  40.945  1.00 133.63 ? 169 LYS D CB   1 
ATOM   15364 C CG   . LYS D 1 169 ? 27.906  65.684  39.785  1.00 134.75 ? 169 LYS D CG   1 
ATOM   15365 C CD   . LYS D 1 169 ? 29.229  64.916  39.850  1.00 138.78 ? 169 LYS D CD   1 
ATOM   15366 C CE   . LYS D 1 169 ? 29.977  65.160  41.155  1.00 142.12 ? 169 LYS D CE   1 
ATOM   15367 N NZ   . LYS D 1 169 ? 31.325  64.526  41.157  1.00 146.66 ? 169 LYS D NZ   1 
ATOM   15368 H H    . LYS D 1 169 ? 25.422  63.477  40.554  1.00 154.12 ? 169 LYS D H    1 
ATOM   15369 H HA   . LYS D 1 169 ? 27.907  63.693  41.452  1.00 158.54 ? 169 LYS D HA   1 
ATOM   15370 H HB2  . LYS D 1 169 ? 26.022  65.508  40.588  1.00 160.36 ? 169 LYS D HB2  1 
ATOM   15371 H HB3  . LYS D 1 169 ? 27.082  66.072  41.628  1.00 160.36 ? 169 LYS D HB3  1 
ATOM   15372 H HG2  . LYS D 1 169 ? 27.474  65.445  38.950  1.00 161.70 ? 169 LYS D HG2  1 
ATOM   15373 H HG3  . LYS D 1 169 ? 28.121  66.630  39.788  1.00 161.70 ? 169 LYS D HG3  1 
ATOM   15374 H HD2  . LYS D 1 169 ? 29.050  63.966  39.779  1.00 166.54 ? 169 LYS D HD2  1 
ATOM   15375 H HD3  . LYS D 1 169 ? 29.799  65.202  39.119  1.00 166.54 ? 169 LYS D HD3  1 
ATOM   15376 H HE2  . LYS D 1 169 ? 30.092  66.115  41.283  1.00 170.55 ? 169 LYS D HE2  1 
ATOM   15377 H HE3  . LYS D 1 169 ? 29.466  64.786  41.890  1.00 170.55 ? 169 LYS D HE3  1 
ATOM   15378 H HZ1  . LYS D 1 169 ? 31.824  64.869  40.506  1.00 176.00 ? 169 LYS D HZ1  1 
ATOM   15379 H HZ2  . LYS D 1 169 ? 31.728  64.670  41.937  1.00 176.00 ? 169 LYS D HZ2  1 
ATOM   15380 H HZ3  . LYS D 1 169 ? 31.248  63.648  41.030  1.00 176.00 ? 169 LYS D HZ3  1 
ATOM   15381 N N    . TYR D 1 170 ? 25.574  63.859  43.598  1.00 130.40 ? 170 TYR D N    1 
ATOM   15382 C CA   . TYR D 1 170 ? 25.386  63.683  45.035  1.00 130.92 ? 170 TYR D CA   1 
ATOM   15383 C C    . TYR D 1 170 ? 26.283  62.560  45.543  1.00 134.86 ? 170 TYR D C    1 
ATOM   15384 O O    . TYR D 1 170 ? 27.066  62.749  46.483  1.00 137.79 ? 170 TYR D O    1 
ATOM   15385 C CB   . TYR D 1 170 ? 23.910  63.394  45.345  1.00 130.19 ? 170 TYR D CB   1 
ATOM   15386 C CG   . TYR D 1 170 ? 23.536  63.438  46.826  1.00 132.72 ? 170 TYR D CG   1 
ATOM   15387 C CD1  . TYR D 1 170 ? 24.388  62.957  47.810  1.00 135.76 ? 170 TYR D CD1  1 
ATOM   15388 C CD2  . TYR D 1 170 ? 22.303  63.951  47.227  1.00 138.35 ? 170 TYR D CD2  1 
ATOM   15389 C CE1  . TYR D 1 170 ? 24.046  62.996  49.148  1.00 134.19 ? 170 TYR D CE1  1 
ATOM   15390 C CE2  . TYR D 1 170 ? 21.949  63.993  48.575  1.00 137.04 ? 170 TYR D CE2  1 
ATOM   15391 C CZ   . TYR D 1 170 ? 22.826  63.512  49.525  1.00 132.93 ? 170 TYR D CZ   1 
ATOM   15392 O OH   . TYR D 1 170 ? 22.472  63.550  50.852  1.00 132.28 ? 170 TYR D OH   1 
ATOM   15393 H H    . TYR D 1 170 ? 24.862  63.758  43.127  1.00 156.48 ? 170 TYR D H    1 
ATOM   15394 H HA   . TYR D 1 170 ? 25.623  64.503  45.496  1.00 157.10 ? 170 TYR D HA   1 
ATOM   15395 H HB2  . TYR D 1 170 ? 23.365  64.054  44.889  1.00 156.23 ? 170 TYR D HB2  1 
ATOM   15396 H HB3  . TYR D 1 170 ? 23.697  62.505  45.019  1.00 156.23 ? 170 TYR D HB3  1 
ATOM   15397 H HD1  . TYR D 1 170 ? 25.210  62.599  47.562  1.00 166.01 ? 170 TYR D HD1  1 
ATOM   15398 H HD2  . TYR D 1 170 ? 21.708  64.269  46.586  1.00 162.91 ? 170 TYR D HD2  1 
ATOM   15399 H HE1  . TYR D 1 170 ? 24.637  62.675  49.790  1.00 164.45 ? 170 TYR D HE1  1 
ATOM   15400 H HE2  . TYR D 1 170 ? 21.127  64.344  48.833  1.00 161.02 ? 170 TYR D HE2  1 
ATOM   15401 H HH   . TYR D 1 170 ? 22.963  63.032  51.295  1.00 158.73 ? 170 TYR D HH   1 
ATOM   15402 N N    . LEU D 1 171 ? 26.181  61.376  44.932  1.00 135.01 ? 171 LEU D N    1 
ATOM   15403 C CA   . LEU D 1 171 ? 26.910  60.208  45.407  1.00 136.44 ? 171 LEU D CA   1 
ATOM   15404 C C    . LEU D 1 171 ? 28.419  60.326  45.215  1.00 140.26 ? 171 LEU D C    1 
ATOM   15405 O O    . LEU D 1 171 ? 29.138  59.370  45.530  1.00 143.43 ? 171 LEU D O    1 
ATOM   15406 C CB   . LEU D 1 171 ? 26.406  58.952  44.695  1.00 134.93 ? 171 LEU D CB   1 
ATOM   15407 C CG   . LEU D 1 171 ? 24.931  58.555  44.777  1.00 128.30 ? 171 LEU D CG   1 
ATOM   15408 C CD1  . LEU D 1 171 ? 24.417  58.578  46.212  1.00 129.07 ? 171 LEU D CD1  1 
ATOM   15409 C CD2  . LEU D 1 171 ? 24.061  59.439  43.892  1.00 125.07 ? 171 LEU D CD2  1 
ATOM   15410 H H    . LEU D 1 171 ? 25.693  61.228  44.240  1.00 162.01 ? 171 LEU D H    1 
ATOM   15411 H HA   . LEU D 1 171 ? 26.739  60.110  46.356  1.00 163.72 ? 171 LEU D HA   1 
ATOM   15412 H HB2  . LEU D 1 171 ? 26.602  59.061  43.751  1.00 161.92 ? 171 LEU D HB2  1 
ATOM   15413 H HB3  . LEU D 1 171 ? 26.906  58.201  45.053  1.00 161.92 ? 171 LEU D HB3  1 
ATOM   15414 H HG   . LEU D 1 171 ? 24.861  57.643  44.452  1.00 153.97 ? 171 LEU D HG   1 
ATOM   15415 H HD11 . LEU D 1 171 ? 23.493  58.284  46.221  1.00 154.88 ? 171 LEU D HD11 1 
ATOM   15416 H HD12 . LEU D 1 171 ? 24.959  57.981  46.752  1.00 154.88 ? 171 LEU D HD12 1 
ATOM   15417 H HD13 . LEU D 1 171 ? 24.480  59.483  46.556  1.00 154.88 ? 171 LEU D HD13 1 
ATOM   15418 H HD21 . LEU D 1 171 ? 23.242  58.965  43.679  1.00 150.09 ? 171 LEU D HD21 1 
ATOM   15419 H HD22 . LEU D 1 171 ? 23.854  60.258  44.369  1.00 150.09 ? 171 LEU D HD22 1 
ATOM   15420 H HD23 . LEU D 1 171 ? 24.545  59.645  43.077  1.00 150.09 ? 171 LEU D HD23 1 
ATOM   15421 N N    . SER D 1 172 ? 28.915  61.456  44.704  1.00 139.80 ? 172 SER D N    1 
ATOM   15422 C CA   . SER D 1 172 ? 30.358  61.650  44.596  1.00 143.64 ? 172 SER D CA   1 
ATOM   15423 C C    . SER D 1 172 ? 31.044  61.435  45.939  1.00 149.39 ? 172 SER D C    1 
ATOM   15424 O O    . SER D 1 172 ? 32.147  60.879  46.003  1.00 150.55 ? 172 SER D O    1 
ATOM   15425 C CB   . SER D 1 172 ? 30.656  63.052  44.063  1.00 141.83 ? 172 SER D CB   1 
ATOM   15426 O OG   . SER D 1 172 ? 30.315  64.044  45.018  1.00 140.38 ? 172 SER D OG   1 
ATOM   15427 H H    . SER D 1 172 ? 28.443  62.116  44.419  1.00 167.77 ? 172 SER D H    1 
ATOM   15428 H HA   . SER D 1 172 ? 30.716  61.004  43.966  1.00 172.37 ? 172 SER D HA   1 
ATOM   15429 H HB2  . SER D 1 172 ? 31.604  63.118  43.865  1.00 170.20 ? 172 SER D HB2  1 
ATOM   15430 H HB3  . SER D 1 172 ? 30.138  63.199  43.257  1.00 170.20 ? 172 SER D HB3  1 
ATOM   15431 H HG   . SER D 1 172 ? 29.496  64.000  45.197  1.00 168.45 ? 172 SER D HG   1 
ATOM   15432 N N    . ASN D 1 173 ? 30.401  61.869  47.028  1.00 153.24 ? 173 ASN D N    1 
ATOM   15433 C CA   . ASN D 1 173 ? 30.986  61.722  48.356  1.00 152.80 ? 173 ASN D CA   1 
ATOM   15434 C C    . ASN D 1 173 ? 30.868  60.293  48.870  1.00 156.85 ? 173 ASN D C    1 
ATOM   15435 O O    . ASN D 1 173 ? 31.790  59.784  49.519  1.00 157.55 ? 173 ASN D O    1 
ATOM   15436 C CB   . ASN D 1 173 ? 30.307  62.680  49.337  1.00 152.67 ? 173 ASN D CB   1 
ATOM   15437 C CG   . ASN D 1 173 ? 30.094  64.059  48.755  1.00 154.38 ? 173 ASN D CG   1 
ATOM   15438 O OD1  . ASN D 1 173 ? 30.981  64.910  48.813  1.00 158.76 ? 173 ASN D OD1  1 
ATOM   15439 N ND2  . ASN D 1 173 ? 28.914  64.290  48.191  1.00 150.02 ? 173 ASN D ND2  1 
ATOM   15440 H H    . ASN D 1 173 ? 29.629  62.249  47.021  1.00 183.89 ? 173 ASN D H    1 
ATOM   15441 H HA   . ASN D 1 173 ? 31.927  61.951  48.301  1.00 183.36 ? 173 ASN D HA   1 
ATOM   15442 H HB2  . ASN D 1 173 ? 29.440  62.320  49.582  1.00 183.20 ? 173 ASN D HB2  1 
ATOM   15443 H HB3  . ASN D 1 173 ? 30.863  62.770  50.127  1.00 183.20 ? 173 ASN D HB3  1 
ATOM   15444 H HD21 . ASN D 1 173 ? 28.318  63.670  48.171  1.00 180.02 ? 173 ASN D HD21 1 
ATOM   15445 H HD22 . ASN D 1 173 ? 28.746  65.059  47.846  1.00 180.02 ? 173 ASN D HD22 1 
ATOM   15446 N N    . GLU D 1 174 ? 29.742  59.639  48.597  1.00 166.15 ? 174 GLU D N    1 
ATOM   15447 C CA   . GLU D 1 174 ? 29.450  58.323  49.143  1.00 163.04 ? 174 GLU D CA   1 
ATOM   15448 C C    . GLU D 1 174 ? 30.063  57.230  48.282  1.00 159.67 ? 174 GLU D C    1 
ATOM   15449 O O    . GLU D 1 174 ? 30.018  57.293  47.051  1.00 160.48 ? 174 GLU D O    1 
ATOM   15450 C CB   . GLU D 1 174 ? 27.937  58.121  49.236  1.00 164.70 ? 174 GLU D CB   1 
ATOM   15451 C CG   . GLU D 1 174 ? 27.505  56.722  49.633  1.00 164.18 ? 174 GLU D CG   1 
ATOM   15452 C CD   . GLU D 1 174 ? 26.089  56.692  50.172  1.00 163.22 ? 174 GLU D CD   1 
ATOM   15453 O OE1  . GLU D 1 174 ? 25.141  56.693  49.357  1.00 163.72 ? 174 GLU D OE1  1 
ATOM   15454 O OE2  . GLU D 1 174 ? 25.924  56.670  51.409  1.00 157.76 ? 174 GLU D OE2  1 
ATOM   15455 H H    . GLU D 1 174 ? 29.120  59.946  48.088  1.00 199.38 ? 174 GLU D H    1 
ATOM   15456 H HA   . GLU D 1 174 ? 29.835  58.251  50.030  1.00 195.65 ? 174 GLU D HA   1 
ATOM   15457 H HB2  . GLU D 1 174 ? 27.585  58.735  49.900  1.00 197.64 ? 174 GLU D HB2  1 
ATOM   15458 H HB3  . GLU D 1 174 ? 27.547  58.312  48.369  1.00 197.64 ? 174 GLU D HB3  1 
ATOM   15459 H HG2  . GLU D 1 174 ? 27.546  56.144  48.856  1.00 197.02 ? 174 GLU D HG2  1 
ATOM   15460 H HG3  . GLU D 1 174 ? 28.099  56.390  50.325  1.00 197.02 ? 174 GLU D HG3  1 
ATOM   15461 N N    . GLU D 1 175 ? 30.646  56.231  48.939  1.00 144.24 ? 175 GLU D N    1 
ATOM   15462 C CA   . GLU D 1 175 ? 31.104  55.023  48.262  1.00 137.42 ? 175 GLU D CA   1 
ATOM   15463 C C    . GLU D 1 175 ? 29.935  54.046  48.200  1.00 136.27 ? 175 GLU D C    1 
ATOM   15464 O O    . GLU D 1 175 ? 29.395  53.648  49.239  1.00 134.26 ? 175 GLU D O    1 
ATOM   15465 C CB   . GLU D 1 175 ? 32.300  54.404  48.977  1.00 128.43 ? 175 GLU D CB   1 
ATOM   15466 C CG   . GLU D 1 175 ? 32.597  52.950  48.595  1.00 126.27 ? 175 GLU D CG   1 
ATOM   15467 C CD   . GLU D 1 175 ? 32.516  52.674  47.096  1.00 123.69 ? 175 GLU D CD   1 
ATOM   15468 O OE1  . GLU D 1 175 ? 32.492  53.631  46.294  1.00 124.15 ? 175 GLU D OE1  1 
ATOM   15469 O OE2  . GLU D 1 175 ? 32.480  51.484  46.718  1.00 122.47 ? 175 GLU D OE2  1 
ATOM   15470 H H    . GLU D 1 175 ? 30.790  56.230  49.787  1.00 173.09 ? 175 GLU D H    1 
ATOM   15471 H HA   . GLU D 1 175 ? 31.391  55.237  47.360  1.00 164.91 ? 175 GLU D HA   1 
ATOM   15472 H HB2  . GLU D 1 175 ? 33.089  54.927  48.767  1.00 154.11 ? 175 GLU D HB2  1 
ATOM   15473 H HB3  . GLU D 1 175 ? 32.133  54.425  49.933  1.00 154.11 ? 175 GLU D HB3  1 
ATOM   15474 H HG2  . GLU D 1 175 ? 33.495  52.728  48.888  1.00 151.53 ? 175 GLU D HG2  1 
ATOM   15475 H HG3  . GLU D 1 175 ? 31.953  52.375  49.036  1.00 151.53 ? 175 GLU D HG3  1 
ATOM   15476 N N    . TYR D 1 176 ? 29.544  53.666  46.986  1.00 135.46 ? 176 TYR D N    1 
ATOM   15477 C CA   . TYR D 1 176 ? 28.348  52.864  46.783  1.00 132.11 ? 176 TYR D CA   1 
ATOM   15478 C C    . TYR D 1 176 ? 28.538  51.970  45.570  1.00 128.25 ? 176 TYR D C    1 
ATOM   15479 O O    . TYR D 1 176 ? 29.291  52.299  44.649  1.00 128.84 ? 176 TYR D O    1 
ATOM   15480 C CB   . TYR D 1 176 ? 27.114  53.756  46.597  1.00 135.55 ? 176 TYR D CB   1 
ATOM   15481 C CG   . TYR D 1 176 ? 27.015  54.372  45.219  1.00 133.21 ? 176 TYR D CG   1 
ATOM   15482 C CD1  . TYR D 1 176 ? 27.784  55.476  44.869  1.00 133.14 ? 176 TYR D CD1  1 
ATOM   15483 C CD2  . TYR D 1 176 ? 26.152  53.846  44.265  1.00 134.50 ? 176 TYR D CD2  1 
ATOM   15484 C CE1  . TYR D 1 176 ? 27.696  56.039  43.608  1.00 130.58 ? 176 TYR D CE1  1 
ATOM   15485 C CE2  . TYR D 1 176 ? 26.057  54.404  43.000  1.00 133.86 ? 176 TYR D CE2  1 
ATOM   15486 C CZ   . TYR D 1 176 ? 26.830  55.499  42.677  1.00 129.44 ? 176 TYR D CZ   1 
ATOM   15487 O OH   . TYR D 1 176 ? 26.742  56.060  41.424  1.00 125.94 ? 176 TYR D OH   1 
ATOM   15488 H H    . TYR D 1 176 ? 29.961  53.862  46.259  1.00 162.55 ? 176 TYR D H    1 
ATOM   15489 H HA   . TYR D 1 176 ? 28.205  52.291  47.553  1.00 158.54 ? 176 TYR D HA   1 
ATOM   15490 H HB2  . TYR D 1 176 ? 26.318  53.221  46.742  1.00 162.66 ? 176 TYR D HB2  1 
ATOM   15491 H HB3  . TYR D 1 176 ? 27.151  54.478  47.243  1.00 162.66 ? 176 TYR D HB3  1 
ATOM   15492 H HD1  . TYR D 1 176 ? 28.367  55.843  45.494  1.00 161.39 ? 176 TYR D HD1  1 
ATOM   15493 H HD2  . TYR D 1 176 ? 25.629  53.108  44.479  1.00 159.77 ? 176 TYR D HD2  1 
ATOM   15494 H HE1  . TYR D 1 176 ? 28.217  56.777  43.388  1.00 160.63 ? 176 TYR D HE1  1 
ATOM   15495 H HE2  . TYR D 1 176 ? 25.476  54.041  42.371  1.00 156.69 ? 176 TYR D HE2  1 
ATOM   15496 H HH   . TYR D 1 176 ? 27.264  56.715  41.365  1.00 151.12 ? 176 TYR D HH   1 
ATOM   15497 N N    . SER D 1 177 ? 27.842  50.834  45.580  1.00 130.25 ? 177 SER D N    1 
ATOM   15498 C CA   . SER D 1 177 ? 27.906  49.885  44.476  1.00 127.78 ? 177 SER D CA   1 
ATOM   15499 C C    . SER D 1 177 ? 26.807  50.107  43.446  1.00 132.47 ? 177 SER D C    1 
ATOM   15500 O O    . SER D 1 177 ? 26.998  49.781  42.269  1.00 130.84 ? 177 SER D O    1 
ATOM   15501 C CB   . SER D 1 177 ? 27.813  48.452  45.007  1.00 118.03 ? 177 SER D CB   1 
ATOM   15502 O OG   . SER D 1 177 ? 26.475  47.987  44.972  1.00 117.60 ? 177 SER D OG   1 
ATOM   15503 H H    . SER D 1 177 ? 27.322  50.589  46.221  1.00 156.31 ? 177 SER D H    1 
ATOM   15504 H HA   . SER D 1 177 ? 28.761  49.987  44.030  1.00 153.34 ? 177 SER D HA   1 
ATOM   15505 H HB2  . SER D 1 177 ? 28.362  47.875  44.455  1.00 141.63 ? 177 SER D HB2  1 
ATOM   15506 H HB3  . SER D 1 177 ? 28.129  48.434  45.924  1.00 141.63 ? 177 SER D HB3  1 
ATOM   15507 H HG   . SER D 1 177 ? 25.990  48.470  45.459  1.00 141.12 ? 177 SER D HG   1 
ATOM   15508 N N    . ALA D 1 178 ? 25.664  50.651  43.857  1.00 144.17 ? 178 ALA D N    1 
ATOM   15509 C CA   . ALA D 1 178 ? 24.553  50.891  42.946  1.00 140.54 ? 178 ALA D CA   1 
ATOM   15510 C C    . ALA D 1 178 ? 23.536  51.785  43.639  1.00 138.06 ? 178 ALA D C    1 
ATOM   15511 O O    . ALA D 1 178 ? 23.496  51.871  44.869  1.00 140.25 ? 178 ALA D O    1 
ATOM   15512 C CB   . ALA D 1 178 ? 23.898  49.580  42.498  1.00 136.53 ? 178 ALA D CB   1 
ATOM   15513 H H    . ALA D 1 178 ? 25.508  50.892  44.668  1.00 173.00 ? 178 ALA D H    1 
ATOM   15514 H HA   . ALA D 1 178 ? 24.880  51.357  42.160  1.00 168.65 ? 178 ALA D HA   1 
ATOM   15515 H HB1  . ALA D 1 178 ? 23.163  49.783  41.898  1.00 163.83 ? 178 ALA D HB1  1 
ATOM   15516 H HB2  . ALA D 1 178 ? 24.558  49.037  42.040  1.00 163.83 ? 178 ALA D HB2  1 
ATOM   15517 H HB3  . ALA D 1 178 ? 23.567  49.110  43.279  1.00 163.83 ? 178 ALA D HB3  1 
ATOM   15518 N N    . PHE D 1 179 ? 22.711  52.446  42.829  1.00 123.37 ? 179 PHE D N    1 
ATOM   15519 C CA   . PHE D 1 179 ? 21.659  53.316  43.336  1.00 117.35 ? 179 PHE D CA   1 
ATOM   15520 C C    . PHE D 1 179 ? 20.482  53.268  42.372  1.00 112.59 ? 179 PHE D C    1 
ATOM   15521 O O    . PHE D 1 179 ? 20.535  52.613  41.329  1.00 114.69 ? 179 PHE D O    1 
ATOM   15522 C CB   . PHE D 1 179 ? 22.183  54.743  43.539  1.00 114.22 ? 179 PHE D CB   1 
ATOM   15523 C CG   . PHE D 1 179 ? 22.147  55.593  42.302  1.00 110.90 ? 179 PHE D CG   1 
ATOM   15524 C CD1  . PHE D 1 179 ? 23.174  55.540  41.377  1.00 115.33 ? 179 PHE D CD1  1 
ATOM   15525 C CD2  . PHE D 1 179 ? 21.095  56.463  42.076  1.00 108.45 ? 179 PHE D CD2  1 
ATOM   15526 C CE1  . PHE D 1 179 ? 23.145  56.334  40.242  1.00 115.70 ? 179 PHE D CE1  1 
ATOM   15527 C CE2  . PHE D 1 179 ? 21.059  57.256  40.941  1.00 108.51 ? 179 PHE D CE2  1 
ATOM   15528 C CZ   . PHE D 1 179 ? 22.085  57.190  40.024  1.00 111.24 ? 179 PHE D CZ   1 
ATOM   15529 H H    . PHE D 1 179 ? 22.743  52.405  41.970  1.00 148.04 ? 179 PHE D H    1 
ATOM   15530 H HA   . PHE D 1 179 ? 21.354  52.983  44.195  1.00 140.81 ? 179 PHE D HA   1 
ATOM   15531 H HB2  . PHE D 1 179 ? 21.638  55.180  44.212  1.00 137.07 ? 179 PHE D HB2  1 
ATOM   15532 H HB3  . PHE D 1 179 ? 23.104  54.696  43.837  1.00 137.07 ? 179 PHE D HB3  1 
ATOM   15533 H HD1  . PHE D 1 179 ? 23.891  54.966  41.519  1.00 138.40 ? 179 PHE D HD1  1 
ATOM   15534 H HD2  . PHE D 1 179 ? 20.402  56.516  42.694  1.00 130.14 ? 179 PHE D HD2  1 
ATOM   15535 H HE1  . PHE D 1 179 ? 23.840  56.289  39.626  1.00 138.84 ? 179 PHE D HE1  1 
ATOM   15536 H HE2  . PHE D 1 179 ? 20.344  57.833  40.799  1.00 130.21 ? 179 PHE D HE2  1 
ATOM   15537 H HZ   . PHE D 1 179 ? 22.064  57.721  39.261  1.00 133.49 ? 179 PHE D HZ   1 
ATOM   15538 N N    . GLY D 1 180 ? 19.406  53.959  42.736  1.00 107.91 ? 180 GLY D N    1 
ATOM   15539 C CA   . GLY D 1 180 ? 18.208  53.968  41.919  1.00 104.82 ? 180 GLY D CA   1 
ATOM   15540 C C    . GLY D 1 180 ? 17.472  55.282  42.045  1.00 102.50 ? 180 GLY D C    1 
ATOM   15541 O O    . GLY D 1 180 ? 17.621  56.011  43.030  1.00 100.68 ? 180 GLY D O    1 
ATOM   15542 H H    . GLY D 1 180 ? 19.348  54.429  43.454  1.00 129.49 ? 180 GLY D H    1 
ATOM   15543 H HA2  . GLY D 1 180 ? 18.447  53.834  40.988  1.00 125.78 ? 180 GLY D HA2  1 
ATOM   15544 H HA3  . GLY D 1 180 ? 17.616  53.252  42.199  1.00 125.78 ? 180 GLY D HA3  1 
ATOM   15545 N N    . ILE D 1 181 ? 16.677  55.583  41.022  1.00 103.17 ? 181 ILE D N    1 
ATOM   15546 C CA   . ILE D 1 181 ? 15.848  56.783  40.978  1.00 98.36  ? 181 ILE D CA   1 
ATOM   15547 C C    . ILE D 1 181 ? 14.460  56.354  40.530  1.00 97.44  ? 181 ILE D C    1 
ATOM   15548 O O    . ILE D 1 181 ? 14.285  55.900  39.393  1.00 97.06  ? 181 ILE D O    1 
ATOM   15549 C CB   . ILE D 1 181 ? 16.414  57.856  40.036  1.00 98.60  ? 181 ILE D CB   1 
ATOM   15550 C CG1  . ILE D 1 181 ? 17.894  58.090  40.332  1.00 100.65 ? 181 ILE D CG1  1 
ATOM   15551 C CG2  . ILE D 1 181 ? 15.604  59.138  40.166  1.00 99.88  ? 181 ILE D CG2  1 
ATOM   15552 C CD1  . ILE D 1 181 ? 18.403  59.458  39.917  1.00 107.69 ? 181 ILE D CD1  1 
ATOM   15553 H H    . ILE D 1 181 ? 16.599  55.091  40.320  1.00 123.81 ? 181 ILE D H    1 
ATOM   15554 H HA   . ILE D 1 181 ? 15.786  57.162  41.869  1.00 118.03 ? 181 ILE D HA   1 
ATOM   15555 H HB   . ILE D 1 181 ? 16.343  57.547  39.119  1.00 118.32 ? 181 ILE D HB   1 
ATOM   15556 H HG12 . ILE D 1 181 ? 18.037  58.001  41.287  1.00 120.78 ? 181 ILE D HG12 1 
ATOM   15557 H HG13 . ILE D 1 181 ? 18.414  57.425  39.855  1.00 120.78 ? 181 ILE D HG13 1 
ATOM   15558 H HG21 . ILE D 1 181 ? 15.861  59.747  39.457  1.00 119.86 ? 181 ILE D HG21 1 
ATOM   15559 H HG22 . ILE D 1 181 ? 14.660  58.924  40.092  1.00 119.86 ? 181 ILE D HG22 1 
ATOM   15560 H HG23 . ILE D 1 181 ? 15.785  59.540  41.030  1.00 119.86 ? 181 ILE D HG23 1 
ATOM   15561 H HD11 . ILE D 1 181 ? 19.369  59.474  40.002  1.00 129.23 ? 181 ILE D HD11 1 
ATOM   15562 H HD12 . ILE D 1 181 ? 18.149  59.623  38.996  1.00 129.23 ? 181 ILE D HD12 1 
ATOM   15563 H HD13 . ILE D 1 181 ? 18.009  60.130  40.494  1.00 129.23 ? 181 ILE D HD13 1 
ATOM   15564 N N    . MET D 1 182 ? 13.478  56.494  41.415  1.00 97.08  ? 182 MET D N    1 
ATOM   15565 C CA   . MET D 1 182 ? 12.097  56.128  41.110  1.00 95.34  ? 182 MET D CA   1 
ATOM   15566 C C    . MET D 1 182 ? 11.382  57.381  40.617  1.00 96.09  ? 182 MET D C    1 
ATOM   15567 O O    . MET D 1 182 ? 10.893  58.185  41.412  1.00 102.09 ? 182 MET D O    1 
ATOM   15568 C CB   . MET D 1 182 ? 11.403  55.538  42.335  1.00 96.11  ? 182 MET D CB   1 
ATOM   15569 C CG   . MET D 1 182 ? 12.094  54.329  42.958  1.00 92.08  ? 182 MET D CG   1 
ATOM   15570 S SD   . MET D 1 182 ? 12.367  52.938  41.842  1.00 91.06  ? 182 MET D SD   1 
ATOM   15571 C CE   . MET D 1 182 ? 14.158  52.942  41.725  1.00 96.02  ? 182 MET D CE   1 
ATOM   15572 H H    . MET D 1 182 ? 13.588  56.802  42.210  1.00 116.50 ? 182 MET D H    1 
ATOM   15573 H HA   . MET D 1 182 ? 12.094  55.454  40.413  1.00 114.41 ? 182 MET D HA   1 
ATOM   15574 H HB2  . MET D 1 182 ? 11.350  56.225  43.017  1.00 115.33 ? 182 MET D HB2  1 
ATOM   15575 H HB3  . MET D 1 182 ? 10.511  55.259  42.075  1.00 115.33 ? 182 MET D HB3  1 
ATOM   15576 H HG2  . MET D 1 182 ? 12.962  54.609  43.290  1.00 110.50 ? 182 MET D HG2  1 
ATOM   15577 H HG3  . MET D 1 182 ? 11.547  54.007  43.692  1.00 110.50 ? 182 MET D HG3  1 
ATOM   15578 H HE1  . MET D 1 182 ? 14.436  52.248  41.107  1.00 115.23 ? 182 MET D HE1  1 
ATOM   15579 H HE2  . MET D 1 182 ? 14.452  53.809  41.403  1.00 115.23 ? 182 MET D HE2  1 
ATOM   15580 H HE3  . MET D 1 182 ? 14.533  52.772  42.604  1.00 115.23 ? 182 MET D HE3  1 
ATOM   15581 N N    . PHE D 1 183 ? 11.332  57.557  39.297  1.00 97.38  ? 183 PHE D N    1 
ATOM   15582 C CA   . PHE D 1 183 ? 10.604  58.667  38.680  1.00 98.01  ? 183 PHE D CA   1 
ATOM   15583 C C    . PHE D 1 183 ? 9.114   58.366  38.771  1.00 97.90  ? 183 PHE D C    1 
ATOM   15584 O O    . PHE D 1 183 ? 8.569   57.606  37.968  1.00 99.82  ? 183 PHE D O    1 
ATOM   15585 C CB   . PHE D 1 183 ? 11.052  58.858  37.237  1.00 97.50  ? 183 PHE D CB   1 
ATOM   15586 C CG   . PHE D 1 183 ? 12.479  59.305  37.105  1.00 97.61  ? 183 PHE D CG   1 
ATOM   15587 C CD1  . PHE D 1 183 ? 12.805  60.649  37.172  1.00 99.83  ? 183 PHE D CD1  1 
ATOM   15588 C CD2  . PHE D 1 183 ? 13.496  58.383  36.922  1.00 98.39  ? 183 PHE D CD2  1 
ATOM   15589 C CE1  . PHE D 1 183 ? 14.117  61.065  37.056  1.00 102.50 ? 183 PHE D CE1  1 
ATOM   15590 C CE2  . PHE D 1 183 ? 14.811  58.794  36.804  1.00 100.72 ? 183 PHE D CE2  1 
ATOM   15591 C CZ   . PHE D 1 183 ? 15.121  60.134  36.869  1.00 103.40 ? 183 PHE D CZ   1 
ATOM   15592 H H    . PHE D 1 183 ? 11.717  57.039  38.728  1.00 116.86 ? 183 PHE D H    1 
ATOM   15593 H HA   . PHE D 1 183 ? 10.785  59.491  39.159  1.00 117.61 ? 183 PHE D HA   1 
ATOM   15594 H HB2  . PHE D 1 183 ? 10.961  58.014  36.768  1.00 117.00 ? 183 PHE D HB2  1 
ATOM   15595 H HB3  . PHE D 1 183 ? 10.490  59.531  36.822  1.00 117.00 ? 183 PHE D HB3  1 
ATOM   15596 H HD1  . PHE D 1 183 ? 12.132  61.279  37.297  1.00 119.79 ? 183 PHE D HD1  1 
ATOM   15597 H HD2  . PHE D 1 183 ? 13.292  57.477  36.879  1.00 118.07 ? 183 PHE D HD2  1 
ATOM   15598 H HE1  . PHE D 1 183 ? 14.325  61.970  37.103  1.00 123.01 ? 183 PHE D HE1  1 
ATOM   15599 H HE2  . PHE D 1 183 ? 15.486  58.165  36.681  1.00 120.87 ? 183 PHE D HE2  1 
ATOM   15600 H HZ   . PHE D 1 183 ? 16.005  60.412  36.787  1.00 124.08 ? 183 PHE D HZ   1 
ATOM   15601 N N    . PHE D 1 184 ? 8.447   58.977  39.746  1.00 100.70 ? 184 PHE D N    1 
ATOM   15602 C CA   . PHE D 1 184 ? 7.112   58.572  40.170  1.00 104.54 ? 184 PHE D CA   1 
ATOM   15603 C C    . PHE D 1 184 ? 6.093   59.635  39.789  1.00 106.51 ? 184 PHE D C    1 
ATOM   15604 O O    . PHE D 1 184 ? 6.223   60.796  40.189  1.00 107.13 ? 184 PHE D O    1 
ATOM   15605 C CB   . PHE D 1 184 ? 7.091   58.331  41.681  1.00 101.71 ? 184 PHE D CB   1 
ATOM   15606 C CG   . PHE D 1 184 ? 5.749   58.546  42.318  1.00 101.20 ? 184 PHE D CG   1 
ATOM   15607 C CD1  . PHE D 1 184 ? 4.716   57.649  42.103  1.00 101.81 ? 184 PHE D CD1  1 
ATOM   15608 C CD2  . PHE D 1 184 ? 5.522   59.639  43.142  1.00 107.77 ? 184 PHE D CD2  1 
ATOM   15609 C CE1  . PHE D 1 184 ? 3.480   57.840  42.695  1.00 103.88 ? 184 PHE D CE1  1 
ATOM   15610 C CE2  . PHE D 1 184 ? 4.287   59.836  43.735  1.00 103.95 ? 184 PHE D CE2  1 
ATOM   15611 C CZ   . PHE D 1 184 ? 3.266   58.934  43.514  1.00 101.24 ? 184 PHE D CZ   1 
ATOM   15612 H H    . PHE D 1 184 ? 8.757   59.646  40.189  1.00 120.85 ? 184 PHE D H    1 
ATOM   15613 H HA   . PHE D 1 184 ? 6.866   57.757  39.705  1.00 125.44 ? 184 PHE D HA   1 
ATOM   15614 H HB2  . PHE D 1 184 ? 7.355   57.413  41.853  1.00 122.06 ? 184 PHE D HB2  1 
ATOM   15615 H HB3  . PHE D 1 184 ? 7.718   58.940  42.102  1.00 122.06 ? 184 PHE D HB3  1 
ATOM   15616 H HD1  . PHE D 1 184 ? 4.854   56.910  41.556  1.00 122.17 ? 184 PHE D HD1  1 
ATOM   15617 H HD2  . PHE D 1 184 ? 6.208   60.247  43.297  1.00 129.32 ? 184 PHE D HD2  1 
ATOM   15618 H HE1  . PHE D 1 184 ? 2.792   57.232  42.542  1.00 124.66 ? 184 PHE D HE1  1 
ATOM   15619 H HE2  . PHE D 1 184 ? 4.145   60.575  44.282  1.00 124.74 ? 184 PHE D HE2  1 
ATOM   15620 H HZ   . PHE D 1 184 ? 2.436   59.061  43.914  1.00 121.49 ? 184 PHE D HZ   1 
ATOM   15621 N N    . ASP D 1 185 ? 5.071   59.224  39.040  1.00 105.86 ? 185 ASP D N    1 
ATOM   15622 C CA   . ASP D 1 185 ? 3.973   60.096  38.641  1.00 108.03 ? 185 ASP D CA   1 
ATOM   15623 C C    . ASP D 1 185 ? 2.799   59.880  39.590  1.00 110.26 ? 185 ASP D C    1 
ATOM   15624 O O    . ASP D 1 185 ? 2.254   58.774  39.666  1.00 112.38 ? 185 ASP D O    1 
ATOM   15625 C CB   . ASP D 1 185 ? 3.557   59.815  37.198  1.00 114.50 ? 185 ASP D CB   1 
ATOM   15626 C CG   . ASP D 1 185 ? 2.377   60.662  36.748  1.00 121.89 ? 185 ASP D CG   1 
ATOM   15627 O OD1  . ASP D 1 185 ? 1.307   60.602  37.391  1.00 123.97 ? 185 ASP D OD1  1 
ATOM   15628 O OD2  . ASP D 1 185 ? 2.515   61.386  35.740  1.00 124.59 ? 185 ASP D OD2  1 
ATOM   15629 H H    . ASP D 1 185 ? 4.990   58.421  38.744  1.00 127.04 ? 185 ASP D H    1 
ATOM   15630 H HA   . ASP D 1 185 ? 4.253   61.022  38.705  1.00 129.64 ? 185 ASP D HA   1 
ATOM   15631 H HB2  . ASP D 1 185 ? 4.305   60.007  36.610  1.00 137.40 ? 185 ASP D HB2  1 
ATOM   15632 H HB3  . ASP D 1 185 ? 3.303   58.882  37.118  1.00 137.40 ? 185 ASP D HB3  1 
ATOM   15633 N N    . SER D 1 186 ? 2.399   60.943  40.292  1.00 114.34 ? 186 SER D N    1 
ATOM   15634 C CA   . SER D 1 186 ? 1.338   60.818  41.283  1.00 113.40 ? 186 SER D CA   1 
ATOM   15635 C C    . SER D 1 186 ? -0.040  60.699  40.642  1.00 117.86 ? 186 SER D C    1 
ATOM   15636 O O    . SER D 1 186 ? -0.954  60.132  41.249  1.00 115.92 ? 186 SER D O    1 
ATOM   15637 C CB   . SER D 1 186 ? 1.363   62.020  42.225  1.00 113.75 ? 186 SER D CB   1 
ATOM   15638 O OG   . SER D 1 186 ? 0.381   62.972  41.849  1.00 116.63 ? 186 SER D OG   1 
ATOM   15639 H H    . SER D 1 186 ? 2.724   61.736  40.213  1.00 137.21 ? 186 SER D H    1 
ATOM   15640 H HA   . SER D 1 186 ? 1.498   60.012  41.798  1.00 136.08 ? 186 SER D HA   1 
ATOM   15641 H HB2  . SER D 1 186 ? 1.181   61.718  43.129  1.00 136.50 ? 186 SER D HB2  1 
ATOM   15642 H HB3  . SER D 1 186 ? 2.239   62.436  42.184  1.00 136.50 ? 186 SER D HB3  1 
ATOM   15643 H HG   . SER D 1 186 ? 0.388   63.619  42.384  1.00 139.96 ? 186 SER D HG   1 
ATOM   15644 N N    . ASP D 1 187 ? -0.216  61.235  39.434  1.00 118.47 ? 187 ASP D N    1 
ATOM   15645 C CA   . ASP D 1 187 ? -1.525  61.183  38.790  1.00 122.88 ? 187 ASP D CA   1 
ATOM   15646 C C    . ASP D 1 187 ? -1.831  59.777  38.286  1.00 126.18 ? 187 ASP D C    1 
ATOM   15647 O O    . ASP D 1 187 ? -2.933  59.255  38.499  1.00 125.77 ? 187 ASP D O    1 
ATOM   15648 C CB   . ASP D 1 187 ? -1.586  62.191  37.641  1.00 123.49 ? 187 ASP D CB   1 
ATOM   15649 C CG   . ASP D 1 187 ? -0.992  63.539  38.012  1.00 123.14 ? 187 ASP D CG   1 
ATOM   15650 O OD1  . ASP D 1 187 ? -1.695  64.350  38.651  1.00 123.65 ? 187 ASP D OD1  1 
ATOM   15651 O OD2  . ASP D 1 187 ? 0.183   63.784  37.667  1.00 123.41 ? 187 ASP D OD2  1 
ATOM   15652 H H    . ASP D 1 187 ? 0.395   61.628  38.974  1.00 142.17 ? 187 ASP D H    1 
ATOM   15653 H HA   . ASP D 1 187 ? -2.203  61.426  39.440  1.00 147.46 ? 187 ASP D HA   1 
ATOM   15654 H HB2  . ASP D 1 187 ? -1.087  61.841  36.886  1.00 148.19 ? 187 ASP D HB2  1 
ATOM   15655 H HB3  . ASP D 1 187 ? -2.512  62.330  37.391  1.00 148.19 ? 187 ASP D HB3  1 
ATOM   15656 N N    . ASN D 1 188 ? -0.867  59.148  37.617  1.00 136.15 ? 188 ASN D N    1 
ATOM   15657 C CA   . ASN D 1 188 ? -1.033  57.802  37.088  1.00 131.16 ? 188 ASN D CA   1 
ATOM   15658 C C    . ASN D 1 188 ? -0.538  56.722  38.041  1.00 132.23 ? 188 ASN D C    1 
ATOM   15659 O O    . ASN D 1 188 ? -0.621  55.535  37.706  1.00 133.59 ? 188 ASN D O    1 
ATOM   15660 C CB   . ASN D 1 188 ? -0.294  57.666  35.746  1.00 129.53 ? 188 ASN D CB   1 
ATOM   15661 C CG   . ASN D 1 188 ? -0.246  58.968  34.962  1.00 143.14 ? 188 ASN D CG   1 
ATOM   15662 O OD1  . ASN D 1 188 ? -1.240  59.690  34.873  1.00 144.20 ? 188 ASN D OD1  1 
ATOM   15663 N ND2  . ASN D 1 188 ? 0.912   59.269  34.385  1.00 141.69 ? 188 ASN D ND2  1 
ATOM   15664 H H    . ASN D 1 188 ? -0.094  59.488  37.455  1.00 163.38 ? 188 ASN D H    1 
ATOM   15665 H HA   . ASN D 1 188 ? -1.979  57.653  36.930  1.00 157.40 ? 188 ASN D HA   1 
ATOM   15666 H HB2  . ASN D 1 188 ? 0.619   57.384  35.916  1.00 155.43 ? 188 ASN D HB2  1 
ATOM   15667 H HB3  . ASN D 1 188 ? -0.749  57.005  35.201  1.00 155.43 ? 188 ASN D HB3  1 
ATOM   15668 H HD21 . ASN D 1 188 ? 1.584   58.737  34.466  1.00 170.03 ? 188 ASN D HD21 1 
ATOM   15669 H HD22 . ASN D 1 188 ? 0.991   59.995  33.931  1.00 170.03 ? 188 ASN D HD22 1 
ATOM   15670 N N    . LEU D 1 189 ? -0.027  57.099  39.213  1.00 119.19 ? 189 LEU D N    1 
ATOM   15671 C CA   . LEU D 1 189 ? 0.621   56.150  40.116  1.00 113.49 ? 189 LEU D CA   1 
ATOM   15672 C C    . LEU D 1 189 ? 1.660   55.322  39.361  1.00 107.86 ? 189 LEU D C    1 
ATOM   15673 O O    . LEU D 1 189 ? 1.852   54.130  39.617  1.00 101.66 ? 189 LEU D O    1 
ATOM   15674 C CB   . LEU D 1 189 ? -0.410  55.254  40.801  1.00 112.20 ? 189 LEU D CB   1 
ATOM   15675 C CG   . LEU D 1 189 ? -1.345  55.988  41.763  1.00 108.55 ? 189 LEU D CG   1 
ATOM   15676 C CD1  . LEU D 1 189 ? -2.723  55.343  41.788  1.00 107.71 ? 189 LEU D CD1  1 
ATOM   15677 C CD2  . LEU D 1 189 ? -0.744  56.029  43.159  1.00 101.20 ? 189 LEU D CD2  1 
ATOM   15678 H H    . LEU D 1 189 ? -0.044  57.906  39.509  1.00 143.03 ? 189 LEU D H    1 
ATOM   15679 H HA   . LEU D 1 189 ? 1.084   56.644  40.811  1.00 136.19 ? 189 LEU D HA   1 
ATOM   15680 H HB2  . LEU D 1 189 ? -0.959  54.838  40.118  1.00 134.64 ? 189 LEU D HB2  1 
ATOM   15681 H HB3  . LEU D 1 189 ? 0.060   54.575  41.309  1.00 134.64 ? 189 LEU D HB3  1 
ATOM   15682 H HG   . LEU D 1 189 ? -1.457  56.900  41.454  1.00 130.25 ? 189 LEU D HG   1 
ATOM   15683 H HD11 . LEU D 1 189 ? -3.285  55.825  42.414  1.00 129.25 ? 189 LEU D HD11 1 
ATOM   15684 H HD12 . LEU D 1 189 ? -3.107  55.384  40.899  1.00 129.25 ? 189 LEU D HD12 1 
ATOM   15685 H HD13 . LEU D 1 189 ? -2.634  54.419  42.068  1.00 129.25 ? 189 LEU D HD13 1 
ATOM   15686 H HD21 . LEU D 1 189 ? -1.345  56.513  43.747  1.00 121.44 ? 189 LEU D HD21 1 
ATOM   15687 H HD22 . LEU D 1 189 ? -0.629  55.121  43.480  1.00 121.44 ? 189 LEU D HD22 1 
ATOM   15688 H HD23 . LEU D 1 189 ? 0.115   56.478  43.120  1.00 121.44 ? 189 LEU D HD23 1 
ATOM   15689 N N    . SER D 1 190 ? 2.329   55.967  38.410  1.00 109.77 ? 190 SER D N    1 
ATOM   15690 C CA   . SER D 1 190 ? 3.371   55.341  37.615  1.00 104.82 ? 190 SER D CA   1 
ATOM   15691 C C    . SER D 1 190 ? 4.725   55.511  38.290  1.00 101.26 ? 190 SER D C    1 
ATOM   15692 O O    . SER D 1 190 ? 4.948   56.447  39.060  1.00 101.52 ? 190 SER D O    1 
ATOM   15693 C CB   . SER D 1 190 ? 3.414   55.949  36.209  1.00 109.11 ? 190 SER D CB   1 
ATOM   15694 O OG   . SER D 1 190 ? 4.468   56.889  36.080  1.00 105.07 ? 190 SER D OG   1 
ATOM   15695 H H    . SER D 1 190 ? 2.192   56.790  38.204  1.00 131.72 ? 190 SER D H    1 
ATOM   15696 H HA   . SER D 1 190 ? 3.188   54.392  37.529  1.00 125.79 ? 190 SER D HA   1 
ATOM   15697 H HB2  . SER D 1 190 ? 3.549   55.237  35.564  1.00 130.94 ? 190 SER D HB2  1 
ATOM   15698 H HB3  . SER D 1 190 ? 2.571   56.397  36.036  1.00 130.94 ? 190 SER D HB3  1 
ATOM   15699 H HG   . SER D 1 190 ? 5.203   56.489  36.007  1.00 126.08 ? 190 SER D HG   1 
ATOM   15700 N N    . MET D 1 191 ? 5.634   54.593  37.986  1.00 97.45  ? 191 MET D N    1 
ATOM   15701 C CA   . MET D 1 191 ? 6.991   54.641  38.517  1.00 95.27  ? 191 MET D CA   1 
ATOM   15702 C C    . MET D 1 191 ? 7.922   54.075  37.460  1.00 95.17  ? 191 MET D C    1 
ATOM   15703 O O    . MET D 1 191 ? 7.770   52.915  37.062  1.00 91.73  ? 191 MET D O    1 
ATOM   15704 C CB   . MET D 1 191 ? 7.105   53.840  39.816  1.00 91.31  ? 191 MET D CB   1 
ATOM   15705 C CG   . MET D 1 191 ? 8.211   54.314  40.744  1.00 96.35  ? 191 MET D CG   1 
ATOM   15706 S SD   . MET D 1 191 ? 9.069   53.006  41.658  1.00 93.90  ? 191 MET D SD   1 
ATOM   15707 C CE   . MET D 1 191 ? 7.757   51.841  42.001  1.00 89.33  ? 191 MET D CE   1 
ATOM   15708 H H    . MET D 1 191 ? 5.489   53.922  37.467  1.00 116.93 ? 191 MET D H    1 
ATOM   15709 H HA   . MET D 1 191 ? 7.231   55.561  38.711  1.00 114.33 ? 191 MET D HA   1 
ATOM   15710 H HB2  . MET D 1 191 ? 6.266   53.908  40.297  1.00 109.56 ? 191 MET D HB2  1 
ATOM   15711 H HB3  . MET D 1 191 ? 7.285   52.913  39.593  1.00 109.56 ? 191 MET D HB3  1 
ATOM   15712 H HG2  . MET D 1 191 ? 8.876   54.782  40.215  1.00 115.63 ? 191 MET D HG2  1 
ATOM   15713 H HG3  . MET D 1 191 ? 7.823   54.917  41.398  1.00 115.63 ? 191 MET D HG3  1 
ATOM   15714 H HE1  . MET D 1 191 ? 8.122   51.091  42.496  1.00 107.20 ? 191 MET D HE1  1 
ATOM   15715 H HE2  . MET D 1 191 ? 7.072   52.283  42.527  1.00 107.20 ? 191 MET D HE2  1 
ATOM   15716 H HE3  . MET D 1 191 ? 7.382   51.532  41.161  1.00 107.20 ? 191 MET D HE3  1 
ATOM   15717 N N    . LYS D 1 192 ? 8.866   54.891  36.993  1.00 92.65  ? 192 LYS D N    1 
ATOM   15718 C CA   . LYS D 1 192 ? 9.885   54.420  36.064  1.00 94.96  ? 192 LYS D CA   1 
ATOM   15719 C C    . LYS D 1 192 ? 11.147  54.143  36.870  1.00 93.74  ? 192 LYS D C    1 
ATOM   15720 O O    . LYS D 1 192 ? 11.852  55.091  37.257  1.00 90.67  ? 192 LYS D O    1 
ATOM   15721 C CB   . LYS D 1 192 ? 10.153  55.452  34.966  1.00 94.43  ? 192 LYS D CB   1 
ATOM   15722 C CG   . LYS D 1 192 ? 9.405   55.173  33.673  1.00 95.26  ? 192 LYS D CG   1 
ATOM   15723 C CD   . LYS D 1 192 ? 7.899   55.361  33.839  1.00 96.15  ? 192 LYS D CD   1 
ATOM   15724 C CE   . LYS D 1 192 ? 7.113   54.435  32.908  1.00 104.39 ? 192 LYS D CE   1 
ATOM   15725 N NZ   . LYS D 1 192 ? 5.686   54.275  33.326  1.00 101.34 ? 192 LYS D NZ   1 
ATOM   15726 H H    . LYS D 1 192 ? 8.936   55.723  37.202  1.00 111.18 ? 192 LYS D H    1 
ATOM   15727 H HA   . LYS D 1 192 ? 9.587   53.604  35.632  1.00 113.95 ? 192 LYS D HA   1 
ATOM   15728 H HB2  . LYS D 1 192 ? 9.879   56.326  35.285  1.00 113.32 ? 192 LYS D HB2  1 
ATOM   15729 H HB3  . LYS D 1 192 ? 11.102  55.454  34.766  1.00 113.32 ? 192 LYS D HB3  1 
ATOM   15730 H HG2  . LYS D 1 192 ? 9.714   55.784  32.986  1.00 114.31 ? 192 LYS D HG2  1 
ATOM   15731 H HG3  . LYS D 1 192 ? 9.568   54.256  33.400  1.00 114.31 ? 192 LYS D HG3  1 
ATOM   15732 H HD2  . LYS D 1 192 ? 7.648   55.159  34.754  1.00 115.38 ? 192 LYS D HD2  1 
ATOM   15733 H HD3  . LYS D 1 192 ? 7.664   56.278  33.627  1.00 115.38 ? 192 LYS D HD3  1 
ATOM   15734 H HE2  . LYS D 1 192 ? 7.123   54.805  32.011  1.00 125.27 ? 192 LYS D HE2  1 
ATOM   15735 H HE3  . LYS D 1 192 ? 7.527   53.558  32.911  1.00 125.27 ? 192 LYS D HE3  1 
ATOM   15736 H HZ1  . LYS D 1 192 ? 5.263   53.731  32.762  1.00 121.61 ? 192 LYS D HZ1  1 
ATOM   15737 H HZ2  . LYS D 1 192 ? 5.645   53.929  34.145  1.00 121.61 ? 192 LYS D HZ2  1 
ATOM   15738 H HZ3  . LYS D 1 192 ? 5.277   55.066  33.325  1.00 121.61 ? 192 LYS D HZ3  1 
ATOM   15739 N N    . PRO D 1 193 ? 11.458  52.882  37.185  1.00 93.66  ? 193 PRO D N    1 
ATOM   15740 C CA   . PRO D 1 193 ? 12.617  52.613  38.048  1.00 96.29  ? 193 PRO D CA   1 
ATOM   15741 C C    . PRO D 1 193 ? 13.936  52.644  37.295  1.00 95.17  ? 193 PRO D C    1 
ATOM   15742 O O    . PRO D 1 193 ? 14.327  51.661  36.659  1.00 96.58  ? 193 PRO D O    1 
ATOM   15743 C CB   . PRO D 1 193 ? 12.326  51.218  38.620  1.00 91.87  ? 193 PRO D CB   1 
ATOM   15744 C CG   . PRO D 1 193 ? 11.360  50.589  37.683  1.00 91.53  ? 193 PRO D CG   1 
ATOM   15745 C CD   . PRO D 1 193 ? 10.686  51.664  36.870  1.00 93.36  ? 193 PRO D CD   1 
ATOM   15746 H HA   . PRO D 1 193 ? 12.647  53.258  38.772  1.00 115.55 ? 193 PRO D HA   1 
ATOM   15747 H HB2  . PRO D 1 193 ? 13.147  50.704  38.663  1.00 110.24 ? 193 PRO D HB2  1 
ATOM   15748 H HB3  . PRO D 1 193 ? 11.940  51.302  39.506  1.00 110.24 ? 193 PRO D HB3  1 
ATOM   15749 H HG2  . PRO D 1 193 ? 11.841  49.983  37.098  1.00 109.83 ? 193 PRO D HG2  1 
ATOM   15750 H HG3  . PRO D 1 193 ? 10.699  50.099  38.197  1.00 109.83 ? 193 PRO D HG3  1 
ATOM   15751 H HD2  . PRO D 1 193 ? 10.738  51.461  35.922  1.00 112.03 ? 193 PRO D HD2  1 
ATOM   15752 H HD3  . PRO D 1 193 ? 9.759   51.767  37.137  1.00 112.03 ? 193 PRO D HD3  1 
ATOM   15753 N N    . TYR D 1 194 ? 14.625  53.777  37.362  1.00 94.97  ? 194 TYR D N    1 
ATOM   15754 C CA   . TYR D 1 194 ? 15.982  53.867  36.851  1.00 99.31  ? 194 TYR D CA   1 
ATOM   15755 C C    . TYR D 1 194 ? 16.954  53.271  37.860  1.00 100.31 ? 194 TYR D C    1 
ATOM   15756 O O    . TYR D 1 194 ? 16.814  53.471  39.071  1.00 103.67 ? 194 TYR D O    1 
ATOM   15757 C CB   . TYR D 1 194 ? 16.363  55.319  36.568  1.00 104.49 ? 194 TYR D CB   1 
ATOM   15758 C CG   . TYR D 1 194 ? 17.835  55.506  36.269  1.00 107.81 ? 194 TYR D CG   1 
ATOM   15759 C CD1  . TYR D 1 194 ? 18.322  55.383  34.973  1.00 109.75 ? 194 TYR D CD1  1 
ATOM   15760 C CD2  . TYR D 1 194 ? 18.739  55.804  37.284  1.00 108.01 ? 194 TYR D CD2  1 
ATOM   15761 C CE1  . TYR D 1 194 ? 19.665  55.554  34.696  1.00 110.48 ? 194 TYR D CE1  1 
ATOM   15762 C CE2  . TYR D 1 194 ? 20.088  55.973  37.017  1.00 109.06 ? 194 TYR D CE2  1 
ATOM   15763 C CZ   . TYR D 1 194 ? 20.547  55.845  35.722  1.00 113.27 ? 194 TYR D CZ   1 
ATOM   15764 O OH   . TYR D 1 194 ? 21.885  56.020  35.449  1.00 114.77 ? 194 TYR D OH   1 
ATOM   15765 H H    . TYR D 1 194 ? 14.327  54.509  37.701  1.00 113.97 ? 194 TYR D H    1 
ATOM   15766 H HA   . TYR D 1 194 ? 16.046  53.374  36.018  1.00 119.17 ? 194 TYR D HA   1 
ATOM   15767 H HB2  . TYR D 1 194 ? 15.861  55.631  35.799  1.00 125.39 ? 194 TYR D HB2  1 
ATOM   15768 H HB3  . TYR D 1 194 ? 16.146  55.857  37.345  1.00 125.39 ? 194 TYR D HB3  1 
ATOM   15769 H HD1  . TYR D 1 194 ? 17.734  55.182  34.281  1.00 131.70 ? 194 TYR D HD1  1 
ATOM   15770 H HD2  . TYR D 1 194 ? 18.433  55.892  38.157  1.00 129.61 ? 194 TYR D HD2  1 
ATOM   15771 H HE1  . TYR D 1 194 ? 19.976  55.474  33.823  1.00 132.58 ? 194 TYR D HE1  1 
ATOM   15772 H HE2  . TYR D 1 194 ? 20.680  56.171  37.706  1.00 130.86 ? 194 TYR D HE2  1 
ATOM   15773 H HH   . TYR D 1 194 ? 22.025  55.927  34.626  1.00 137.73 ? 194 TYR D HH   1 
ATOM   15774 N N    . VAL D 1 195 ? 17.951  52.546  37.352  1.00 103.16 ? 195 VAL D N    1 
ATOM   15775 C CA   . VAL D 1 195 ? 18.959  51.899  38.180  1.00 104.53 ? 195 VAL D CA   1 
ATOM   15776 C C    . VAL D 1 195 ? 20.322  52.116  37.537  1.00 110.27 ? 195 VAL D C    1 
ATOM   15777 O O    . VAL D 1 195 ? 20.436  52.368  36.336  1.00 111.29 ? 195 VAL D O    1 
ATOM   15778 C CB   . VAL D 1 195 ? 18.671  50.391  38.364  1.00 101.41 ? 195 VAL D CB   1 
ATOM   15779 C CG1  . VAL D 1 195 ? 19.704  49.753  39.274  1.00 102.65 ? 195 VAL D CG1  1 
ATOM   15780 C CG2  . VAL D 1 195 ? 17.263  50.186  38.917  1.00 98.95  ? 195 VAL D CG2  1 
ATOM   15781 H H    . VAL D 1 195 ? 18.064  52.414  36.510  1.00 123.79 ? 195 VAL D H    1 
ATOM   15782 H HA   . VAL D 1 195 ? 18.977  52.308  39.059  1.00 125.43 ? 195 VAL D HA   1 
ATOM   15783 H HB   . VAL D 1 195 ? 18.726  49.953  37.500  1.00 121.69 ? 195 VAL D HB   1 
ATOM   15784 H HG11 . VAL D 1 195 ? 19.371  48.894  39.577  1.00 123.18 ? 195 VAL D HG11 1 
ATOM   15785 H HG12 . VAL D 1 195 ? 20.530  49.633  38.780  1.00 123.18 ? 195 VAL D HG12 1 
ATOM   15786 H HG13 . VAL D 1 195 ? 19.857  50.335  40.035  1.00 123.18 ? 195 VAL D HG13 1 
ATOM   15787 H HG21 . VAL D 1 195 ? 17.128  49.242  39.092  1.00 118.74 ? 195 VAL D HG21 1 
ATOM   15788 H HG22 . VAL D 1 195 ? 17.170  50.692  39.739  1.00 118.74 ? 195 VAL D HG22 1 
ATOM   15789 H HG23 . VAL D 1 195 ? 16.618  50.497  38.262  1.00 118.74 ? 195 VAL D HG23 1 
ATOM   15790 N N    . TYR D 1 196 ? 21.365  52.022  38.360  1.00 110.69 ? 196 TYR D N    1 
ATOM   15791 C CA   . TYR D 1 196 ? 22.726  52.291  37.920  1.00 114.68 ? 196 TYR D CA   1 
ATOM   15792 C C    . TYR D 1 196 ? 23.690  51.486  38.776  1.00 119.34 ? 196 TYR D C    1 
ATOM   15793 O O    . TYR D 1 196 ? 23.448  51.265  39.965  1.00 120.72 ? 196 TYR D O    1 
ATOM   15794 C CB   . TYR D 1 196 ? 23.043  53.791  38.007  1.00 112.97 ? 196 TYR D CB   1 
ATOM   15795 C CG   . TYR D 1 196 ? 24.399  54.196  37.470  1.00 117.49 ? 196 TYR D CG   1 
ATOM   15796 C CD1  . TYR D 1 196 ? 25.519  54.217  38.294  1.00 118.47 ? 196 TYR D CD1  1 
ATOM   15797 C CD2  . TYR D 1 196 ? 24.557  54.579  36.141  1.00 118.27 ? 196 TYR D CD2  1 
ATOM   15798 C CE1  . TYR D 1 196 ? 26.761  54.596  37.806  1.00 120.15 ? 196 TYR D CE1  1 
ATOM   15799 C CE2  . TYR D 1 196 ? 25.794  54.960  35.645  1.00 118.10 ? 196 TYR D CE2  1 
ATOM   15800 C CZ   . TYR D 1 196 ? 26.892  54.968  36.481  1.00 121.10 ? 196 TYR D CZ   1 
ATOM   15801 O OH   . TYR D 1 196 ? 28.119  55.348  35.983  1.00 120.18 ? 196 TYR D OH   1 
ATOM   15802 H H    . TYR D 1 196 ? 21.306  51.801  39.189  1.00 132.83 ? 196 TYR D H    1 
ATOM   15803 H HA   . TYR D 1 196 ? 22.843  52.008  36.999  1.00 137.62 ? 196 TYR D HA   1 
ATOM   15804 H HB2  . TYR D 1 196 ? 22.373  54.276  37.500  1.00 135.57 ? 196 TYR D HB2  1 
ATOM   15805 H HB3  . TYR D 1 196 ? 23.009  54.058  38.940  1.00 135.57 ? 196 TYR D HB3  1 
ATOM   15806 H HD1  . TYR D 1 196 ? 25.433  53.974  39.187  1.00 142.16 ? 196 TYR D HD1  1 
ATOM   15807 H HD2  . TYR D 1 196 ? 23.819  54.579  35.575  1.00 141.92 ? 196 TYR D HD2  1 
ATOM   15808 H HE1  . TYR D 1 196 ? 27.502  54.600  38.368  1.00 144.18 ? 196 TYR D HE1  1 
ATOM   15809 H HE2  . TYR D 1 196 ? 25.884  55.209  34.753  1.00 141.72 ? 196 TYR D HE2  1 
ATOM   15810 H HH   . TYR D 1 196 ? 28.050  55.548  35.170  1.00 144.21 ? 196 TYR D HH   1 
ATOM   15811 N N    . VAL D 1 197 ? 24.778  51.037  38.156  1.00 122.82 ? 197 VAL D N    1 
ATOM   15812 C CA   . VAL D 1 197 ? 25.827  50.295  38.847  1.00 125.62 ? 197 VAL D CA   1 
ATOM   15813 C C    . VAL D 1 197 ? 27.175  50.798  38.351  1.00 127.29 ? 197 VAL D C    1 
ATOM   15814 O O    . VAL D 1 197 ? 27.360  51.029  37.151  1.00 124.78 ? 197 VAL D O    1 
ATOM   15815 C CB   . VAL D 1 197 ? 25.701  48.773  38.626  1.00 123.76 ? 197 VAL D CB   1 
ATOM   15816 C CG1  . VAL D 1 197 ? 26.436  48.014  39.725  1.00 125.62 ? 197 VAL D CG1  1 
ATOM   15817 C CG2  . VAL D 1 197 ? 24.240  48.358  38.571  1.00 120.12 ? 197 VAL D CG2  1 
ATOM   15818 H H    . VAL D 1 197 ? 24.934  51.154  37.319  1.00 147.39 ? 197 VAL D H    1 
ATOM   15819 H HA   . VAL D 1 197 ? 25.760  50.466  39.799  1.00 150.73 ? 197 VAL D HA   1 
ATOM   15820 H HB   . VAL D 1 197 ? 26.109  48.545  37.775  1.00 148.52 ? 197 VAL D HB   1 
ATOM   15821 H HG11 . VAL D 1 197 ? 26.384  47.063  39.541  1.00 150.75 ? 197 VAL D HG11 1 
ATOM   15822 H HG12 . VAL D 1 197 ? 27.363  48.299  39.740  1.00 150.75 ? 197 VAL D HG12 1 
ATOM   15823 H HG13 . VAL D 1 197 ? 26.016  48.209  40.578  1.00 150.75 ? 197 VAL D HG13 1 
ATOM   15824 H HG21 . VAL D 1 197 ? 24.185  47.390  38.602  1.00 144.15 ? 197 VAL D HG21 1 
ATOM   15825 H HG22 . VAL D 1 197 ? 23.774  48.741  39.330  1.00 144.15 ? 197 VAL D HG22 1 
ATOM   15826 H HG23 . VAL D 1 197 ? 23.850  48.684  37.745  1.00 144.15 ? 197 VAL D HG23 1 
ATOM   15827 N N    . LYS D 1 198 ? 28.121  50.967  39.279  1.00 130.54 ? 198 LYS D N    1 
ATOM   15828 C CA   . LYS D 1 198 ? 29.449  51.441  38.902  1.00 130.82 ? 198 LYS D CA   1 
ATOM   15829 C C    . LYS D 1 198 ? 30.094  50.509  37.882  1.00 130.57 ? 198 LYS D C    1 
ATOM   15830 O O    . LYS D 1 198 ? 30.628  50.960  36.862  1.00 129.46 ? 198 LYS D O    1 
ATOM   15831 C CB   . LYS D 1 198 ? 30.334  51.573  40.144  1.00 133.23 ? 198 LYS D CB   1 
ATOM   15832 C CG   . LYS D 1 198 ? 31.582  52.428  39.939  1.00 135.64 ? 198 LYS D CG   1 
ATOM   15833 C CD   . LYS D 1 198 ? 32.710  51.637  39.282  1.00 136.84 ? 198 LYS D CD   1 
ATOM   15834 C CE   . LYS D 1 198 ? 34.032  52.395  39.338  1.00 138.53 ? 198 LYS D CE   1 
ATOM   15835 N NZ   . LYS D 1 198 ? 34.687  52.290  40.674  1.00 140.25 ? 198 LYS D NZ   1 
ATOM   15836 H H    . LYS D 1 198 ? 28.020  50.815  40.120  1.00 156.64 ? 198 LYS D H    1 
ATOM   15837 H HA   . LYS D 1 198 ? 29.364  52.320  38.499  1.00 156.98 ? 198 LYS D HA   1 
ATOM   15838 H HB2  . LYS D 1 198 ? 29.812  51.980  40.854  1.00 159.87 ? 198 LYS D HB2  1 
ATOM   15839 H HB3  . LYS D 1 198 ? 30.625  50.688  40.412  1.00 159.87 ? 198 LYS D HB3  1 
ATOM   15840 H HG2  . LYS D 1 198 ? 31.365  53.180  39.365  1.00 162.77 ? 198 LYS D HG2  1 
ATOM   15841 H HG3  . LYS D 1 198 ? 31.896  52.748  40.799  1.00 162.77 ? 198 LYS D HG3  1 
ATOM   15842 H HD2  . LYS D 1 198 ? 32.823  50.793  39.747  1.00 164.20 ? 198 LYS D HD2  1 
ATOM   15843 H HD3  . LYS D 1 198 ? 32.490  51.476  38.351  1.00 164.20 ? 198 LYS D HD3  1 
ATOM   15844 H HE2  . LYS D 1 198 ? 34.638  52.028  38.675  1.00 166.23 ? 198 LYS D HE2  1 
ATOM   15845 H HE3  . LYS D 1 198 ? 33.869  53.334  39.155  1.00 166.23 ? 198 LYS D HE3  1 
ATOM   15846 H HZ1  . LYS D 1 198 ? 34.854  51.437  40.865  1.00 168.29 ? 198 LYS D HZ1  1 
ATOM   15847 H HZ2  . LYS D 1 198 ? 35.454  52.741  40.673  1.00 168.29 ? 198 LYS D HZ2  1 
ATOM   15848 H HZ3  . LYS D 1 198 ? 34.154  52.628  41.301  1.00 168.29 ? 198 LYS D HZ3  1 
ATOM   15849 N N    . GLU D 1 199 ? 30.054  49.199  38.142  1.00 131.12 ? 199 GLU D N    1 
ATOM   15850 C CA   . GLU D 1 199 ? 30.683  48.250  37.229  1.00 131.20 ? 199 GLU D CA   1 
ATOM   15851 C C    . GLU D 1 199 ? 30.012  48.260  35.861  1.00 128.48 ? 199 GLU D C    1 
ATOM   15852 O O    . GLU D 1 199 ? 30.663  47.975  34.849  1.00 128.54 ? 199 GLU D O    1 
ATOM   15853 C CB   . GLU D 1 199 ? 30.652  46.844  37.830  1.00 131.04 ? 199 GLU D CB   1 
ATOM   15854 C CG   . GLU D 1 199 ? 31.859  46.519  38.698  1.00 132.88 ? 199 GLU D CG   1 
ATOM   15855 C CD   . GLU D 1 199 ? 32.404  45.123  38.454  1.00 132.42 ? 199 GLU D CD   1 
ATOM   15856 O OE1  . GLU D 1 199 ? 31.627  44.245  38.023  1.00 132.57 ? 199 GLU D OE1  1 
ATOM   15857 O OE2  . GLU D 1 199 ? 33.611  44.903  38.695  1.00 131.93 ? 199 GLU D OE2  1 
ATOM   15858 H H    . GLU D 1 199 ? 29.676  48.843  38.828  1.00 157.34 ? 199 GLU D H    1 
ATOM   15859 H HA   . GLU D 1 199 ? 31.612  48.502  37.107  1.00 157.44 ? 199 GLU D HA   1 
ATOM   15860 H HB2  . GLU D 1 199 ? 29.859  46.758  38.381  1.00 157.25 ? 199 GLU D HB2  1 
ATOM   15861 H HB3  . GLU D 1 199 ? 30.626  46.197  37.107  1.00 157.25 ? 199 GLU D HB3  1 
ATOM   15862 H HG2  . GLU D 1 199 ? 32.567  47.154  38.506  1.00 159.46 ? 199 GLU D HG2  1 
ATOM   15863 H HG3  . GLU D 1 199 ? 31.602  46.581  39.632  1.00 159.46 ? 199 GLU D HG3  1 
ATOM   15864 N N    . VAL D 1 200 ? 28.717  48.579  35.807  1.00 128.26 ? 200 VAL D N    1 
ATOM   15865 C CA   . VAL D 1 200 ? 28.045  48.708  34.518  1.00 124.85 ? 200 VAL D CA   1 
ATOM   15866 C C    . VAL D 1 200 ? 28.471  49.998  33.827  1.00 123.32 ? 200 VAL D C    1 
ATOM   15867 O O    . VAL D 1 200 ? 28.646  50.037  32.603  1.00 121.05 ? 200 VAL D O    1 
ATOM   15868 C CB   . VAL D 1 200 ? 26.517  48.646  34.704  1.00 121.02 ? 200 VAL D CB   1 
ATOM   15869 C CG1  . VAL D 1 200 ? 25.804  48.991  33.402  1.00 120.32 ? 200 VAL D CG1  1 
ATOM   15870 C CG2  . VAL D 1 200 ? 26.095  47.271  35.196  1.00 120.29 ? 200 VAL D CG2  1 
ATOM   15871 H H    . VAL D 1 200 ? 28.215  48.722  36.490  1.00 153.91 ? 200 VAL D H    1 
ATOM   15872 H HA   . VAL D 1 200 ? 28.309  47.963  33.956  1.00 149.82 ? 200 VAL D HA   1 
ATOM   15873 H HB   . VAL D 1 200 ? 26.258  49.299  35.372  1.00 145.22 ? 200 VAL D HB   1 
ATOM   15874 H HG11 . VAL D 1 200 ? 24.875  48.721  33.470  1.00 144.39 ? 200 VAL D HG11 1 
ATOM   15875 H HG12 . VAL D 1 200 ? 25.860  49.949  33.257  1.00 144.39 ? 200 VAL D HG12 1 
ATOM   15876 H HG13 . VAL D 1 200 ? 26.234  48.520  32.672  1.00 144.39 ? 200 VAL D HG13 1 
ATOM   15877 H HG21 . VAL D 1 200 ? 25.134  47.265  35.330  1.00 144.35 ? 200 VAL D HG21 1 
ATOM   15878 H HG22 . VAL D 1 200 ? 26.340  46.608  34.531  1.00 144.35 ? 200 VAL D HG22 1 
ATOM   15879 H HG23 . VAL D 1 200 ? 26.547  47.082  36.033  1.00 144.35 ? 200 VAL D HG23 1 
ATOM   15880 N N    . GLY D 1 201 ? 28.654  51.069  34.595  1.00 122.98 ? 201 GLY D N    1 
ATOM   15881 C CA   . GLY D 1 201 ? 28.979  52.354  34.016  1.00 121.49 ? 201 GLY D CA   1 
ATOM   15882 C C    . GLY D 1 201 ? 27.852  53.004  33.252  1.00 118.92 ? 201 GLY D C    1 
ATOM   15883 O O    . GLY D 1 201 ? 28.082  53.995  32.553  1.00 117.15 ? 201 GLY D O    1 
ATOM   15884 H H    . GLY D 1 201 ? 28.593  51.071  35.453  1.00 147.57 ? 201 GLY D H    1 
ATOM   15885 H HA2  . GLY D 1 201 ? 29.243  52.959  34.727  1.00 145.79 ? 201 GLY D HA2  1 
ATOM   15886 H HA3  . GLY D 1 201 ? 29.724  52.241  33.405  1.00 145.79 ? 201 GLY D HA3  1 
ATOM   15887 N N    . SER D 1 202 ? 26.638  52.474  33.365  1.00 117.39 ? 202 SER D N    1 
ATOM   15888 C CA   . SER D 1 202 ? 25.494  52.992  32.632  1.00 115.28 ? 202 SER D CA   1 
ATOM   15889 C C    . SER D 1 202 ? 24.230  52.549  33.350  1.00 113.54 ? 202 SER D C    1 
ATOM   15890 O O    . SER D 1 202 ? 24.224  51.554  34.080  1.00 114.66 ? 202 SER D O    1 
ATOM   15891 C CB   . SER D 1 202 ? 25.492  52.504  31.181  1.00 116.16 ? 202 SER D CB   1 
ATOM   15892 O OG   . SER D 1 202 ? 25.872  51.141  31.104  1.00 116.32 ? 202 SER D OG   1 
ATOM   15893 H H    . SER D 1 202 ? 26.450  51.803  33.869  1.00 140.87 ? 202 SER D H    1 
ATOM   15894 H HA   . SER D 1 202 ? 25.522  53.961  32.625  1.00 138.34 ? 202 SER D HA   1 
ATOM   15895 H HB2  . SER D 1 202 ? 24.598  52.603  30.817  1.00 139.40 ? 202 SER D HB2  1 
ATOM   15896 H HB3  . SER D 1 202 ? 26.120  53.037  30.668  1.00 139.40 ? 202 SER D HB3  1 
ATOM   15897 H HG   . SER D 1 202 ? 25.874  50.888  30.303  1.00 139.59 ? 202 SER D HG   1 
ATOM   15898 N N    . GLY D 1 203 ? 23.155  53.298  33.124  1.00 113.92 ? 203 GLY D N    1 
ATOM   15899 C CA   . GLY D 1 203 ? 21.885  53.025  33.753  1.00 110.11 ? 203 GLY D CA   1 
ATOM   15900 C C    . GLY D 1 203 ? 20.940  52.250  32.856  1.00 107.19 ? 203 GLY D C    1 
ATOM   15901 O O    . GLY D 1 203 ? 21.135  52.146  31.648  1.00 112.25 ? 203 GLY D O    1 
ATOM   15902 H H    . GLY D 1 203 ? 23.143  53.980  32.600  1.00 136.70 ? 203 GLY D H    1 
ATOM   15903 H HA2  . GLY D 1 203 ? 22.032  52.507  34.559  1.00 132.12 ? 203 GLY D HA2  1 
ATOM   15904 H HA3  . GLY D 1 203 ? 21.459  53.864  33.991  1.00 132.12 ? 203 GLY D HA3  1 
ATOM   15905 N N    . VAL D 1 204 ? 19.900  51.697  33.476  1.00 104.61 ? 204 VAL D N    1 
ATOM   15906 C CA   . VAL D 1 204 ? 18.872  50.952  32.762  1.00 102.92 ? 204 VAL D CA   1 
ATOM   15907 C C    . VAL D 1 204 ? 17.547  51.190  33.473  1.00 104.37 ? 204 VAL D C    1 
ATOM   15908 O O    . VAL D 1 204 ? 17.501  51.362  34.694  1.00 103.61 ? 204 VAL D O    1 
ATOM   15909 C CB   . VAL D 1 204 ? 19.198  49.441  32.687  1.00 103.34 ? 204 VAL D CB   1 
ATOM   15910 C CG1  . VAL D 1 204 ? 20.660  49.217  32.317  1.00 105.22 ? 204 VAL D CG1  1 
ATOM   15911 C CG2  . VAL D 1 204 ? 18.867  48.756  34.005  1.00 97.90  ? 204 VAL D CG2  1 
ATOM   15912 H H    . VAL D 1 204 ? 19.767  51.741  34.324  1.00 125.54 ? 204 VAL D H    1 
ATOM   15913 H HA   . VAL D 1 204 ? 18.805  51.287  31.854  1.00 123.50 ? 204 VAL D HA   1 
ATOM   15914 H HB   . VAL D 1 204 ? 18.650  49.042  31.993  1.00 124.01 ? 204 VAL D HB   1 
ATOM   15915 H HG11 . VAL D 1 204 ? 20.802  48.271  32.153  1.00 126.26 ? 204 VAL D HG11 1 
ATOM   15916 H HG12 . VAL D 1 204 ? 20.864  49.725  31.517  1.00 126.26 ? 204 VAL D HG12 1 
ATOM   15917 H HG13 . VAL D 1 204 ? 21.221  49.514  33.050  1.00 126.26 ? 204 VAL D HG13 1 
ATOM   15918 H HG21 . VAL D 1 204 ? 19.350  47.916  34.054  1.00 117.48 ? 204 VAL D HG21 1 
ATOM   15919 H HG22 . VAL D 1 204 ? 19.134  49.334  34.737  1.00 117.48 ? 204 VAL D HG22 1 
ATOM   15920 H HG23 . VAL D 1 204 ? 17.912  48.591  34.045  1.00 117.48 ? 204 VAL D HG23 1 
ATOM   15921 N N    . TYR D 1 205 ? 16.463  51.204  32.701  1.00 100.31 ? 205 TYR D N    1 
ATOM   15922 C CA   . TYR D 1 205 ? 15.116  51.387  33.234  1.00 98.88  ? 205 TYR D CA   1 
ATOM   15923 C C    . TYR D 1 205 ? 14.460  50.013  33.321  1.00 98.57  ? 205 TYR D C    1 
ATOM   15924 O O    . TYR D 1 205 ? 14.163  49.393  32.295  1.00 95.61  ? 205 TYR D O    1 
ATOM   15925 C CB   . TYR D 1 205 ? 14.307  52.342  32.361  1.00 101.81 ? 205 TYR D CB   1 
ATOM   15926 C CG   . TYR D 1 205 ? 14.849  53.761  32.332  1.00 109.74 ? 205 TYR D CG   1 
ATOM   15927 C CD1  . TYR D 1 205 ? 16.135  54.028  31.873  1.00 109.22 ? 205 TYR D CD1  1 
ATOM   15928 C CD2  . TYR D 1 205 ? 14.072  54.834  32.761  1.00 111.92 ? 205 TYR D CD2  1 
ATOM   15929 C CE1  . TYR D 1 205 ? 16.634  55.320  31.845  1.00 112.47 ? 205 TYR D CE1  1 
ATOM   15930 C CE2  . TYR D 1 205 ? 14.563  56.131  32.736  1.00 112.66 ? 205 TYR D CE2  1 
ATOM   15931 C CZ   . TYR D 1 205 ? 15.844  56.369  32.277  1.00 117.15 ? 205 TYR D CZ   1 
ATOM   15932 O OH   . TYR D 1 205 ? 16.331  57.658  32.249  1.00 117.86 ? 205 TYR D OH   1 
ATOM   15933 H H    . TYR D 1 205 ? 16.483  51.107  31.847  1.00 120.37 ? 205 TYR D H    1 
ATOM   15934 H HA   . TYR D 1 205 ? 15.161  51.769  34.125  1.00 118.66 ? 205 TYR D HA   1 
ATOM   15935 H HB2  . TYR D 1 205 ? 14.308  52.007  31.451  1.00 122.17 ? 205 TYR D HB2  1 
ATOM   15936 H HB3  . TYR D 1 205 ? 13.399  52.380  32.700  1.00 122.17 ? 205 TYR D HB3  1 
ATOM   15937 H HD1  . TYR D 1 205 ? 16.670  53.326  31.580  1.00 131.06 ? 205 TYR D HD1  1 
ATOM   15938 H HD2  . TYR D 1 205 ? 13.209  54.679  33.070  1.00 134.31 ? 205 TYR D HD2  1 
ATOM   15939 H HE1  . TYR D 1 205 ? 17.497  55.481  31.538  1.00 134.96 ? 205 TYR D HE1  1 
ATOM   15940 H HE2  . TYR D 1 205 ? 14.032  56.838  33.026  1.00 135.19 ? 205 TYR D HE2  1 
ATOM   15941 H HH   . TYR D 1 205 ? 15.739  58.194  32.510  1.00 141.44 ? 205 TYR D HH   1 
ATOM   15942 N N    . GLU D 1 206 ? 14.239  49.536  34.542  1.00 95.86  ? 206 GLU D N    1 
ATOM   15943 C CA   . GLU D 1 206 ? 13.765  48.177  34.741  1.00 93.99  ? 206 GLU D CA   1 
ATOM   15944 C C    . GLU D 1 206 ? 12.272  48.064  34.445  1.00 90.09  ? 206 GLU D C    1 
ATOM   15945 O O    . GLU D 1 206 ? 11.515  49.036  34.514  1.00 89.30  ? 206 GLU D O    1 
ATOM   15946 C CB   . GLU D 1 206 ? 14.040  47.713  36.176  1.00 95.36  ? 206 GLU D CB   1 
ATOM   15947 C CG   . GLU D 1 206 ? 15.256  46.809  36.320  1.00 96.14  ? 206 GLU D CG   1 
ATOM   15948 C CD   . GLU D 1 206 ? 16.562  47.583  36.265  1.00 99.79  ? 206 GLU D CD   1 
ATOM   15949 O OE1  . GLU D 1 206 ? 16.515  48.815  36.060  1.00 101.16 ? 206 GLU D OE1  1 
ATOM   15950 O OE2  . GLU D 1 206 ? 17.633  46.959  36.424  1.00 100.20 ? 206 GLU D OE2  1 
ATOM   15951 H H    . GLU D 1 206 ? 14.356  49.981  35.269  1.00 115.03 ? 206 GLU D H    1 
ATOM   15952 H HA   . GLU D 1 206 ? 14.239  47.591  34.131  1.00 112.79 ? 206 GLU D HA   1 
ATOM   15953 H HB2  . GLU D 1 206 ? 14.187  48.495  36.731  1.00 114.43 ? 206 GLU D HB2  1 
ATOM   15954 H HB3  . GLU D 1 206 ? 13.268  47.221  36.495  1.00 114.43 ? 206 GLU D HB3  1 
ATOM   15955 H HG2  . GLU D 1 206 ? 15.213  46.352  37.174  1.00 115.37 ? 206 GLU D HG2  1 
ATOM   15956 H HG3  . GLU D 1 206 ? 15.258  46.162  35.597  1.00 115.37 ? 206 GLU D HG3  1 
ATOM   15957 N N    . ASN D 1 207 ? 11.857  46.841  34.108  1.00 87.72  ? 207 ASN D N    1 
ATOM   15958 C CA   . ASN D 1 207 ? 10.435  46.561  33.956  1.00 88.06  ? 207 ASN D CA   1 
ATOM   15959 C C    . ASN D 1 207 ? 9.706   46.704  35.282  1.00 90.95  ? 207 ASN D C    1 
ATOM   15960 O O    . ASN D 1 207 ? 8.587   47.227  35.333  1.00 91.40  ? 207 ASN D O    1 
ATOM   15961 C CB   . ASN D 1 207 ? 10.240  45.157  33.398  1.00 90.70  ? 207 ASN D CB   1 
ATOM   15962 C CG   . ASN D 1 207 ? 10.836  44.997  32.028  1.00 86.23  ? 207 ASN D CG   1 
ATOM   15963 O OD1  . ASN D 1 207 ? 10.718  45.885  31.187  1.00 90.61  ? 207 ASN D OD1  1 
ATOM   15964 N ND2  . ASN D 1 207 ? 11.493  43.871  31.795  1.00 85.77  ? 207 ASN D ND2  1 
ATOM   15965 H H    . ASN D 1 207 ? 12.372  46.167  33.965  1.00 105.27 ? 207 ASN D H    1 
ATOM   15966 H HA   . ASN D 1 207 ? 10.055  47.196  33.328  1.00 105.67 ? 207 ASN D HA   1 
ATOM   15967 H HB2  . ASN D 1 207 ? 10.669  44.518  33.989  1.00 108.84 ? 207 ASN D HB2  1 
ATOM   15968 H HB3  . ASN D 1 207 ? 9.291   44.968  33.338  1.00 108.84 ? 207 ASN D HB3  1 
ATOM   15969 H HD21 . ASN D 1 207 ? 11.852  43.734  31.026  1.00 102.92 ? 207 ASN D HD21 1 
ATOM   15970 H HD22 . ASN D 1 207 ? 11.561  43.277  32.413  1.00 102.92 ? 207 ASN D HD22 1 
ATOM   15971 N N    . SER D 1 208 ? 10.322  46.232  36.367  1.00 89.56  ? 208 SER D N    1 
ATOM   15972 C CA   . SER D 1 208 ? 9.755   46.346  37.703  1.00 87.05  ? 208 SER D CA   1 
ATOM   15973 C C    . SER D 1 208 ? 10.888  46.430  38.714  1.00 87.73  ? 208 SER D C    1 
ATOM   15974 O O    . SER D 1 208 ? 12.006  45.970  38.465  1.00 86.05  ? 208 SER D O    1 
ATOM   15975 C CB   . SER D 1 208 ? 8.846   45.158  38.046  1.00 88.29  ? 208 SER D CB   1 
ATOM   15976 O OG   . SER D 1 208 ? 7.809   45.013  37.093  1.00 98.06  ? 208 SER D OG   1 
ATOM   15977 H H    . SER D 1 208 ? 11.084  45.834  36.352  1.00 107.48 ? 208 SER D H    1 
ATOM   15978 H HA   . SER D 1 208 ? 9.227   47.159  37.749  1.00 104.47 ? 208 SER D HA   1 
ATOM   15979 H HB2  . SER D 1 208 ? 9.379   44.348  38.056  1.00 105.95 ? 208 SER D HB2  1 
ATOM   15980 H HB3  . SER D 1 208 ? 8.451   45.307  38.919  1.00 105.95 ? 208 SER D HB3  1 
ATOM   15981 H HG   . SER D 1 208 ? 7.268   44.422  37.345  1.00 117.68 ? 208 SER D HG   1 
ATOM   15982 N N    . CYS D 1 209 ? 10.582  47.024  39.866  1.00 85.17  ? 209 CYS D N    1 
ATOM   15983 C CA   . CYS D 1 209 ? 11.529  47.113  40.976  1.00 88.53  ? 209 CYS D CA   1 
ATOM   15984 C C    . CYS D 1 209 ? 10.772  46.898  42.280  1.00 85.48  ? 209 CYS D C    1 
ATOM   15985 O O    . CYS D 1 209 ? 10.015  47.774  42.713  1.00 83.28  ? 209 CYS D O    1 
ATOM   15986 C CB   . CYS D 1 209 ? 12.248  48.463  40.982  1.00 89.14  ? 209 CYS D CB   1 
ATOM   15987 S SG   . CYS D 1 209 ? 13.868  48.444  41.803  1.00 92.34  ? 209 CYS D SG   1 
ATOM   15988 H H    . CYS D 1 209 ? 9.821   47.388  40.031  1.00 102.20 ? 209 CYS D H    1 
ATOM   15989 H HA   . CYS D 1 209 ? 12.188  46.407  40.888  1.00 106.23 ? 209 CYS D HA   1 
ATOM   15990 H HB2  . CYS D 1 209 ? 12.387  48.744  40.063  1.00 106.96 ? 209 CYS D HB2  1 
ATOM   15991 H HB3  . CYS D 1 209 ? 11.691  49.108  41.445  1.00 106.96 ? 209 CYS D HB3  1 
ATOM   15992 H HG   . CYS D 1 209 ? 14.373  49.527  41.696  1.00 110.81 ? 209 CYS D HG   1 
ATOM   15993 N N    . ALA D 1 210 ? 10.985  45.741  42.913  1.00 85.23  ? 210 ALA D N    1 
ATOM   15994 C CA   . ALA D 1 210 ? 10.329  45.462  44.187  1.00 86.84  ? 210 ALA D CA   1 
ATOM   15995 C C    . ALA D 1 210 ? 10.867  46.362  45.294  1.00 86.19  ? 210 ALA D C    1 
ATOM   15996 O O    . ALA D 1 210 ? 10.095  46.951  46.062  1.00 84.03  ? 210 ALA D O    1 
ATOM   15997 C CB   . ALA D 1 210 ? 10.509  43.990  44.561  1.00 84.05  ? 210 ALA D CB   1 
ATOM   15998 H H    . ALA D 1 210 ? 11.497  45.111  42.628  1.00 102.28 ? 210 ALA D H    1 
ATOM   15999 H HA   . ALA D 1 210 ? 9.379   45.635  44.091  1.00 104.21 ? 210 ALA D HA   1 
ATOM   16000 H HB1  . ALA D 1 210 ? 9.996   43.802  45.362  1.00 100.86 ? 210 ALA D HB1  1 
ATOM   16001 H HB2  . ALA D 1 210 ? 10.193  43.437  43.829  1.00 100.86 ? 210 ALA D HB2  1 
ATOM   16002 H HB3  . ALA D 1 210 ? 11.450  43.819  44.722  1.00 100.86 ? 210 ALA D HB3  1 
ATOM   16003 N N    . SER D 1 211 ? 12.194  46.476  45.400  1.00 87.11  ? 211 SER D N    1 
ATOM   16004 C CA   . SER D 1 211 ? 12.775  47.363  46.401  1.00 84.38  ? 211 SER D CA   1 
ATOM   16005 C C    . SER D 1 211 ? 12.445  48.822  46.116  1.00 87.21  ? 211 SER D C    1 
ATOM   16006 O O    . SER D 1 211 ? 12.299  49.616  47.051  1.00 89.07  ? 211 SER D O    1 
ATOM   16007 C CB   . SER D 1 211 ? 14.289  47.172  46.458  1.00 85.81  ? 211 SER D CB   1 
ATOM   16008 O OG   . SER D 1 211 ? 14.827  46.990  45.161  1.00 93.11  ? 211 SER D OG   1 
ATOM   16009 H H    . SER D 1 211 ? 12.766  46.057  44.913  1.00 104.53 ? 211 SER D H    1 
ATOM   16010 H HA   . SER D 1 211 ? 12.409  47.133  47.269  1.00 101.25 ? 211 SER D HA   1 
ATOM   16011 H HB2  . SER D 1 211 ? 14.691  47.958  46.859  1.00 102.97 ? 211 SER D HB2  1 
ATOM   16012 H HB3  . SER D 1 211 ? 14.488  46.388  46.994  1.00 102.97 ? 211 SER D HB3  1 
ATOM   16013 H HG   . SER D 1 211 ? 15.661  46.898  45.206  1.00 111.73 ? 211 SER D HG   1 
ATOM   16014 N N    . GLY D 1 212 ? 12.321  49.192  44.840  1.00 87.68  ? 212 GLY D N    1 
ATOM   16015 C CA   . GLY D 1 212 ? 11.995  50.570  44.509  1.00 86.88  ? 212 GLY D CA   1 
ATOM   16016 C C    . GLY D 1 212 ? 10.553  50.922  44.816  1.00 83.12  ? 212 GLY D C    1 
ATOM   16017 O O    . GLY D 1 212 ? 10.260  52.036  45.258  1.00 86.44  ? 212 GLY D O    1 
ATOM   16018 H H    . GLY D 1 212 ? 12.420  48.672  44.162  1.00 105.22 ? 212 GLY D H    1 
ATOM   16019 H HA2  . GLY D 1 212 ? 12.568  51.165  45.017  1.00 104.25 ? 212 GLY D HA2  1 
ATOM   16020 H HA3  . GLY D 1 212 ? 12.149  50.716  43.562  1.00 104.25 ? 212 GLY D HA3  1 
ATOM   16021 N N    . THR D 1 213 ? 9.630   49.990  44.567  1.00 83.18  ? 213 THR D N    1 
ATOM   16022 C CA   . THR D 1 213 ? 8.256   50.176  45.027  1.00 84.92  ? 213 THR D CA   1 
ATOM   16023 C C    . THR D 1 213 ? 8.202   50.262  46.550  1.00 89.65  ? 213 THR D C    1 
ATOM   16024 O O    . THR D 1 213 ? 7.444   51.060  47.116  1.00 88.63  ? 213 THR D O    1 
ATOM   16025 C CB   . THR D 1 213 ? 7.380   49.029  44.526  1.00 84.92  ? 213 THR D CB   1 
ATOM   16026 O OG1  . THR D 1 213 ? 7.707   48.739  43.162  1.00 86.38  ? 213 THR D OG1  1 
ATOM   16027 C CG2  . THR D 1 213 ? 5.907   49.392  44.623  1.00 88.21  ? 213 THR D CG2  1 
ATOM   16028 H H    . THR D 1 213 ? 9.771   49.255  44.143  1.00 99.81  ? 213 THR D H    1 
ATOM   16029 H HA   . THR D 1 213 ? 7.907   51.004  44.660  1.00 101.90 ? 213 THR D HA   1 
ATOM   16030 H HB   . THR D 1 213 ? 7.535   48.244  45.074  1.00 101.90 ? 213 THR D HB   1 
ATOM   16031 H HG1  . THR D 1 213 ? 7.259   48.081  42.894  1.00 103.65 ? 213 THR D HG1  1 
ATOM   16032 H HG21 . THR D 1 213 ? 5.362   48.655  44.304  1.00 105.86 ? 213 THR D HG21 1 
ATOM   16033 H HG22 . THR D 1 213 ? 5.672   49.581  45.545  1.00 105.86 ? 213 THR D HG22 1 
ATOM   16034 H HG23 . THR D 1 213 ? 5.722   50.177  44.083  1.00 105.86 ? 213 THR D HG23 1 
ATOM   16035 N N    . THR D 1 214 ? 9.002   49.439  47.231  1.00 87.84  ? 214 THR D N    1 
ATOM   16036 C CA   . THR D 1 214 ? 9.091   49.533  48.683  1.00 86.08  ? 214 THR D CA   1 
ATOM   16037 C C    . THR D 1 214 ? 9.572   50.913  49.106  1.00 90.09  ? 214 THR D C    1 
ATOM   16038 O O    . THR D 1 214 ? 9.030   51.505  50.048  1.00 92.20  ? 214 THR D O    1 
ATOM   16039 C CB   . THR D 1 214 ? 10.025  48.442  49.208  1.00 83.98  ? 214 THR D CB   1 
ATOM   16040 O OG1  . THR D 1 214 ? 9.314   47.199  49.308  1.00 83.24  ? 214 THR D OG1  1 
ATOM   16041 C CG2  . THR D 1 214 ? 10.561  48.799  50.570  1.00 92.64  ? 214 THR D CG2  1 
ATOM   16042 H H    . THR D 1 214 ? 9.494   48.827  46.881  1.00 105.40 ? 214 THR D H    1 
ATOM   16043 H HA   . THR D 1 214 ? 8.214   49.392  49.073  1.00 103.29 ? 214 THR D HA   1 
ATOM   16044 H HB   . THR D 1 214 ? 10.771  48.349  48.595  1.00 100.77 ? 214 THR D HB   1 
ATOM   16045 H HG1  . THR D 1 214 ? 9.825   46.598  49.596  1.00 99.89  ? 214 THR D HG1  1 
ATOM   16046 H HG21 . THR D 1 214 ? 11.151  48.098  50.889  1.00 111.17 ? 214 THR D HG21 1 
ATOM   16047 H HG22 . THR D 1 214 ? 11.057  49.631  50.524  1.00 111.17 ? 214 THR D HG22 1 
ATOM   16048 H HG23 . THR D 1 214 ? 9.829   48.903  51.198  1.00 111.17 ? 214 THR D HG23 1 
ATOM   16049 N N    . ALA D 1 215 ? 10.603  51.434  48.438  1.00 86.83  ? 215 ALA D N    1 
ATOM   16050 C CA   . ALA D 1 215 ? 11.108  52.758  48.782  1.00 92.36  ? 215 ALA D CA   1 
ATOM   16051 C C    . ALA D 1 215 ? 10.028  53.815  48.598  1.00 94.14  ? 215 ALA D C    1 
ATOM   16052 O O    . ALA D 1 215 ? 9.853   54.694  49.449  1.00 95.31  ? 215 ALA D O    1 
ATOM   16053 C CB   . ALA D 1 215 ? 12.331  53.091  47.928  1.00 90.57  ? 215 ALA D CB   1 
ATOM   16054 H H    . ALA D 1 215 ? 11.020  51.046  47.794  1.00 104.20 ? 215 ALA D H    1 
ATOM   16055 H HA   . ALA D 1 215 ? 11.381  52.760  49.713  1.00 110.83 ? 215 ALA D HA   1 
ATOM   16056 H HB1  . ALA D 1 215 ? 12.649  53.977  48.163  1.00 108.69 ? 215 ALA D HB1  1 
ATOM   16057 H HB2  . ALA D 1 215 ? 13.025  52.435  48.101  1.00 108.69 ? 215 ALA D HB2  1 
ATOM   16058 H HB3  . ALA D 1 215 ? 12.079  53.067  46.992  1.00 108.69 ? 215 ALA D HB3  1 
ATOM   16059 N N    . LEU D 1 216 ? 9.291   53.738  47.491  1.00 91.70  ? 216 LEU D N    1 
ATOM   16060 C CA   . LEU D 1 216 ? 8.219   54.695  47.245  1.00 94.08  ? 216 LEU D CA   1 
ATOM   16061 C C    . LEU D 1 216 ? 7.110   54.559  48.279  1.00 94.90  ? 216 LEU D C    1 
ATOM   16062 O O    . LEU D 1 216 ? 6.559   55.565  48.742  1.00 97.48  ? 216 LEU D O    1 
ATOM   16063 C CB   . LEU D 1 216 ? 7.680   54.499  45.831  1.00 90.04  ? 216 LEU D CB   1 
ATOM   16064 C CG   . LEU D 1 216 ? 6.387   55.221  45.474  1.00 92.24  ? 216 LEU D CG   1 
ATOM   16065 C CD1  . LEU D 1 216 ? 6.639   56.569  44.845  1.00 91.41  ? 216 LEU D CD1  1 
ATOM   16066 C CD2  . LEU D 1 216 ? 5.592   54.335  44.518  1.00 91.39  ? 216 LEU D CD2  1 
ATOM   16067 H H    . LEU D 1 216 ? 9.390   53.148  46.873  1.00 110.04 ? 216 LEU D H    1 
ATOM   16068 H HA   . LEU D 1 216 ? 8.570   55.597  47.313  1.00 112.89 ? 216 LEU D HA   1 
ATOM   16069 H HB2  . LEU D 1 216 ? 8.357   54.807  45.208  1.00 108.05 ? 216 LEU D HB2  1 
ATOM   16070 H HB3  . LEU D 1 216 ? 7.519   53.551  45.702  1.00 108.05 ? 216 LEU D HB3  1 
ATOM   16071 H HG   . LEU D 1 216 ? 5.881   55.387  46.285  1.00 110.69 ? 216 LEU D HG   1 
ATOM   16072 H HD11 . LEU D 1 216 ? 5.787   56.983  44.635  1.00 109.69 ? 216 LEU D HD11 1 
ATOM   16073 H HD12 . LEU D 1 216 ? 7.130   57.123  45.472  1.00 109.69 ? 216 LEU D HD12 1 
ATOM   16074 H HD13 . LEU D 1 216 ? 7.157   56.447  44.035  1.00 109.69 ? 216 LEU D HD13 1 
ATOM   16075 H HD21 . LEU D 1 216 ? 4.783   54.801  44.255  1.00 109.67 ? 216 LEU D HD21 1 
ATOM   16076 H HD22 . LEU D 1 216 ? 6.134   54.147  43.736  1.00 109.67 ? 216 LEU D HD22 1 
ATOM   16077 H HD23 . LEU D 1 216 ? 5.364   53.507  44.970  1.00 109.67 ? 216 LEU D HD23 1 
ATOM   16078 N N    . GLY D 1 217 ? 6.759   53.325  48.644  1.00 95.22  ? 217 GLY D N    1 
ATOM   16079 C CA   . GLY D 1 217 ? 5.745   53.133  49.668  1.00 95.34  ? 217 GLY D CA   1 
ATOM   16080 C C    . GLY D 1 217 ? 6.125   53.782  50.984  1.00 97.43  ? 217 GLY D C    1 
ATOM   16081 O O    . GLY D 1 217 ? 5.330   54.507  51.585  1.00 100.16 ? 217 GLY D O    1 
ATOM   16082 H H    . GLY D 1 217 ? 7.088   52.599  48.320  1.00 114.26 ? 217 GLY D H    1 
ATOM   16083 H HA2  . GLY D 1 217 ? 4.908   53.520  49.367  1.00 114.41 ? 217 GLY D HA2  1 
ATOM   16084 H HA3  . GLY D 1 217 ? 5.618   52.184  49.820  1.00 114.41 ? 217 GLY D HA3  1 
ATOM   16085 N N    . TYR D 1 218 ? 7.348   53.521  51.455  1.00 98.48  ? 218 TYR D N    1 
ATOM   16086 C CA   . TYR D 1 218 ? 7.829   54.172  52.669  1.00 99.51  ? 218 TYR D CA   1 
ATOM   16087 C C    . TYR D 1 218 ? 7.710   55.686  52.549  1.00 104.71 ? 218 TYR D C    1 
ATOM   16088 O O    . TYR D 1 218 ? 7.155   56.358  53.431  1.00 103.35 ? 218 TYR D O    1 
ATOM   16089 C CB   . TYR D 1 218 ? 9.285   53.789  52.946  1.00 97.08  ? 218 TYR D CB   1 
ATOM   16090 C CG   . TYR D 1 218 ? 9.527   52.347  53.337  1.00 98.01  ? 218 TYR D CG   1 
ATOM   16091 C CD1  . TYR D 1 218 ? 8.626   51.655  54.137  1.00 94.43  ? 218 TYR D CD1  1 
ATOM   16092 C CD2  . TYR D 1 218 ? 10.670  51.679  52.910  1.00 97.71  ? 218 TYR D CD2  1 
ATOM   16093 C CE1  . TYR D 1 218 ? 8.857   50.338  54.494  1.00 91.86  ? 218 TYR D CE1  1 
ATOM   16094 C CE2  . TYR D 1 218 ? 10.907  50.366  53.265  1.00 95.10  ? 218 TYR D CE2  1 
ATOM   16095 C CZ   . TYR D 1 218 ? 9.999   49.700  54.054  1.00 95.44  ? 218 TYR D CZ   1 
ATOM   16096 O OH   . TYR D 1 218 ? 10.242  48.388  54.400  1.00 91.64  ? 218 TYR D OH   1 
ATOM   16097 H H    . TYR D 1 218 ? 7.909   52.979  51.093  1.00 118.18 ? 218 TYR D H    1 
ATOM   16098 H HA   . TYR D 1 218 ? 7.289   53.865  53.414  1.00 119.42 ? 218 TYR D HA   1 
ATOM   16099 H HB2  . TYR D 1 218 ? 9.802   53.959  52.143  1.00 116.50 ? 218 TYR D HB2  1 
ATOM   16100 H HB3  . TYR D 1 218 ? 9.611   54.342  53.673  1.00 116.50 ? 218 TYR D HB3  1 
ATOM   16101 H HD1  . TYR D 1 218 ? 7.857   52.083  54.436  1.00 113.32 ? 218 TYR D HD1  1 
ATOM   16102 H HD2  . TYR D 1 218 ? 11.287  52.125  52.376  1.00 117.26 ? 218 TYR D HD2  1 
ATOM   16103 H HE1  . TYR D 1 218 ? 8.244   49.885  55.027  1.00 110.23 ? 218 TYR D HE1  1 
ATOM   16104 H HE2  . TYR D 1 218 ? 11.676  49.934  52.972  1.00 114.11 ? 218 TYR D HE2  1 
ATOM   16105 H HH   . TYR D 1 218 ? 10.963  48.129  54.055  1.00 109.97 ? 218 TYR D HH   1 
ATOM   16106 N N    . TYR D 1 219 ? 8.236   56.237  51.452  1.00 116.44 ? 219 TYR D N    1 
ATOM   16107 C CA   . TYR D 1 219 ? 8.221   57.680  51.249  1.00 114.63 ? 219 TYR D CA   1 
ATOM   16108 C C    . TYR D 1 219 ? 6.799   58.225  51.172  1.00 113.06 ? 219 TYR D C    1 
ATOM   16109 O O    . TYR D 1 219 ? 6.541   59.356  51.600  1.00 111.57 ? 219 TYR D O    1 
ATOM   16110 C CB   . TYR D 1 219 ? 8.996   58.009  49.971  1.00 118.46 ? 219 TYR D CB   1 
ATOM   16111 C CG   . TYR D 1 219 ? 9.506   59.423  49.899  1.00 127.68 ? 219 TYR D CG   1 
ATOM   16112 C CD1  . TYR D 1 219 ? 10.663  59.801  50.567  1.00 125.05 ? 219 TYR D CD1  1 
ATOM   16113 C CD2  . TYR D 1 219 ? 8.839   60.377  49.145  1.00 122.40 ? 219 TYR D CD2  1 
ATOM   16114 C CE1  . TYR D 1 219 ? 11.131  61.095  50.498  1.00 125.00 ? 219 TYR D CE1  1 
ATOM   16115 C CE2  . TYR D 1 219 ? 9.297   61.675  49.069  1.00 124.27 ? 219 TYR D CE2  1 
ATOM   16116 C CZ   . TYR D 1 219 ? 10.447  62.027  49.745  1.00 128.51 ? 219 TYR D CZ   1 
ATOM   16117 O OH   . TYR D 1 219 ? 10.912  63.321  49.671  1.00 128.62 ? 219 TYR D OH   1 
ATOM   16118 H H    . TYR D 1 219 ? 8.606   55.796  50.813  1.00 139.73 ? 219 TYR D H    1 
ATOM   16119 H HA   . TYR D 1 219 ? 8.655   58.118  51.997  1.00 137.56 ? 219 TYR D HA   1 
ATOM   16120 H HB2  . TYR D 1 219 ? 9.763   57.418  49.915  1.00 142.16 ? 219 TYR D HB2  1 
ATOM   16121 H HB3  . TYR D 1 219 ? 8.412   57.869  49.210  1.00 142.16 ? 219 TYR D HB3  1 
ATOM   16122 H HD1  . TYR D 1 219 ? 11.129  59.171  51.068  1.00 150.05 ? 219 TYR D HD1  1 
ATOM   16123 H HD2  . TYR D 1 219 ? 8.068   60.137  48.683  1.00 146.88 ? 219 TYR D HD2  1 
ATOM   16124 H HE1  . TYR D 1 219 ? 11.903  61.338  50.957  1.00 150.00 ? 219 TYR D HE1  1 
ATOM   16125 H HE2  . TYR D 1 219 ? 8.836   62.307  48.567  1.00 149.13 ? 219 TYR D HE2  1 
ATOM   16126 H HH   . TYR D 1 219 ? 10.367  63.797  49.245  1.00 154.34 ? 219 TYR D HH   1 
ATOM   16127 N N    . LEU D 1 220 ? 5.865   57.438  50.634  1.00 106.61 ? 220 LEU D N    1 
ATOM   16128 C CA   . LEU D 1 220 ? 4.483   57.886  50.516  1.00 105.54 ? 220 LEU D CA   1 
ATOM   16129 C C    . LEU D 1 220 ? 3.746   57.814  51.848  1.00 106.89 ? 220 LEU D C    1 
ATOM   16130 O O    . LEU D 1 220 ? 2.813   58.589  52.081  1.00 107.09 ? 220 LEU D O    1 
ATOM   16131 C CB   . LEU D 1 220 ? 3.748   57.048  49.468  1.00 99.15  ? 220 LEU D CB   1 
ATOM   16132 C CG   . LEU D 1 220 ? 3.967   57.358  47.989  1.00 98.66  ? 220 LEU D CG   1 
ATOM   16133 C CD1  . LEU D 1 220 ? 2.833   56.737  47.157  1.00 90.90  ? 220 LEU D CD1  1 
ATOM   16134 C CD2  . LEU D 1 220 ? 4.064   58.849  47.704  1.00 94.85  ? 220 LEU D CD2  1 
ATOM   16135 H H    . LEU D 1 220 ? 6.008   56.645  50.332  1.00 127.94 ? 220 LEU D H    1 
ATOM   16136 H HA   . LEU D 1 220 ? 4.479   58.809  50.219  1.00 126.64 ? 220 LEU D HA   1 
ATOM   16137 H HB2  . LEU D 1 220 ? 4.012   56.124  49.597  1.00 118.99 ? 220 LEU D HB2  1 
ATOM   16138 H HB3  . LEU D 1 220 ? 2.797   57.148  49.632  1.00 118.99 ? 220 LEU D HB3  1 
ATOM   16139 H HG   . LEU D 1 220 ? 4.818   56.972  47.729  1.00 118.39 ? 220 LEU D HG   1 
ATOM   16140 H HD11 . LEU D 1 220 ? 2.980   56.940  46.221  1.00 109.08 ? 220 LEU D HD11 1 
ATOM   16141 H HD12 . LEU D 1 220 ? 2.833   55.776  47.291  1.00 109.08 ? 220 LEU D HD12 1 
ATOM   16142 H HD13 . LEU D 1 220 ? 1.986   57.111  47.448  1.00 109.08 ? 220 LEU D HD13 1 
ATOM   16143 H HD21 . LEU D 1 220 ? 4.154   58.982  46.747  1.00 113.82 ? 220 LEU D HD21 1 
ATOM   16144 H HD22 . LEU D 1 220 ? 3.260   59.285  48.025  1.00 113.82 ? 220 LEU D HD22 1 
ATOM   16145 H HD23 . LEU D 1 220 ? 4.840   59.208  48.162  1.00 113.82 ? 220 LEU D HD23 1 
ATOM   16146 N N    . LYS D 1 221 ? 4.140   56.889  52.723  1.00 104.77 ? 221 LYS D N    1 
ATOM   16147 C CA   . LYS D 1 221 ? 3.503   56.738  54.027  1.00 107.25 ? 221 LYS D CA   1 
ATOM   16148 C C    . LYS D 1 221 ? 3.896   57.848  54.989  1.00 107.81 ? 221 LYS D C    1 
ATOM   16149 O O    . LYS D 1 221 ? 3.195   58.059  55.983  1.00 109.96 ? 221 LYS D O    1 
ATOM   16150 C CB   . LYS D 1 221 ? 3.856   55.358  54.590  1.00 104.04 ? 221 LYS D CB   1 
ATOM   16151 C CG   . LYS D 1 221 ? 3.154   54.930  55.884  1.00 104.17 ? 221 LYS D CG   1 
ATOM   16152 C CD   . LYS D 1 221 ? 1.649   55.115  55.869  1.00 108.32 ? 221 LYS D CD   1 
ATOM   16153 C CE   . LYS D 1 221 ? 1.120   55.217  57.301  1.00 111.23 ? 221 LYS D CE   1 
ATOM   16154 N NZ   . LYS D 1 221 ? 1.642   56.434  58.002  1.00 110.55 ? 221 LYS D NZ   1 
ATOM   16155 H H    . LYS D 1 221 ? 4.780   56.332  52.583  1.00 125.72 ? 221 LYS D H    1 
ATOM   16156 H HA   . LYS D 1 221 ? 2.537   56.778  53.941  1.00 128.70 ? 221 LYS D HA   1 
ATOM   16157 H HB2  . LYS D 1 221 ? 3.635   54.695  53.917  1.00 124.84 ? 221 LYS D HB2  1 
ATOM   16158 H HB3  . LYS D 1 221 ? 4.809   55.343  54.769  1.00 124.84 ? 221 LYS D HB3  1 
ATOM   16159 H HG2  . LYS D 1 221 ? 3.332   53.988  56.036  1.00 125.00 ? 221 LYS D HG2  1 
ATOM   16160 H HG3  . LYS D 1 221 ? 3.507   55.457  56.618  1.00 125.00 ? 221 LYS D HG3  1 
ATOM   16161 H HD2  . LYS D 1 221 ? 1.424   55.932  55.396  1.00 129.98 ? 221 LYS D HD2  1 
ATOM   16162 H HD3  . LYS D 1 221 ? 1.229   54.355  55.436  1.00 129.98 ? 221 LYS D HD3  1 
ATOM   16163 H HE2  . LYS D 1 221 ? 0.152   55.270  57.282  1.00 133.48 ? 221 LYS D HE2  1 
ATOM   16164 H HE3  . LYS D 1 221 ? 1.400   54.435  57.802  1.00 133.48 ? 221 LYS D HE3  1 
ATOM   16165 H HZ1  . LYS D 1 221 ? 2.511   56.340  58.169  1.00 132.66 ? 221 LYS D HZ1  1 
ATOM   16166 H HZ2  . LYS D 1 221 ? 1.521   57.154  57.493  1.00 132.66 ? 221 LYS D HZ2  1 
ATOM   16167 H HZ3  . LYS D 1 221 ? 1.211   56.550  58.773  1.00 132.66 ? 221 LYS D HZ3  1 
ATOM   16168 N N    . LYS D 1 222 ? 4.979   58.576  54.698  1.00 107.89 ? 222 LYS D N    1 
ATOM   16169 C CA   . LYS D 1 222 ? 5.371   59.730  55.495  1.00 104.72 ? 222 LYS D CA   1 
ATOM   16170 C C    . LYS D 1 222 ? 4.806   61.030  54.925  1.00 108.73 ? 222 LYS D C    1 
ATOM   16171 O O    . LYS D 1 222 ? 4.363   61.902  55.682  1.00 118.05 ? 222 LYS D O    1 
ATOM   16172 C CB   . LYS D 1 222 ? 6.897   59.856  55.581  1.00 104.04 ? 222 LYS D CB   1 
ATOM   16173 C CG   . LYS D 1 222 ? 7.711   58.561  55.730  1.00 109.30 ? 222 LYS D CG   1 
ATOM   16174 C CD   . LYS D 1 222 ? 7.006   57.464  56.508  1.00 110.04 ? 222 LYS D CD   1 
ATOM   16175 C CE   . LYS D 1 222 ? 8.008   56.388  56.942  1.00 109.52 ? 222 LYS D CE   1 
ATOM   16176 N NZ   . LYS D 1 222 ? 8.108   55.265  55.966  1.00 105.46 ? 222 LYS D NZ   1 
ATOM   16177 H H    . LYS D 1 222 ? 5.505   58.416  54.036  1.00 129.47 ? 222 LYS D H    1 
ATOM   16178 H HA   . LYS D 1 222 ? 5.035   59.597  56.395  1.00 125.66 ? 222 LYS D HA   1 
ATOM   16179 H HB2  . LYS D 1 222 ? 7.206   60.288  54.768  1.00 124.85 ? 222 LYS D HB2  1 
ATOM   16180 H HB3  . LYS D 1 222 ? 7.107   60.408  56.350  1.00 124.85 ? 222 LYS D HB3  1 
ATOM   16181 H HG2  . LYS D 1 222 ? 7.906   58.214  54.846  1.00 131.16 ? 222 LYS D HG2  1 
ATOM   16182 H HG3  . LYS D 1 222 ? 8.536   58.766  56.196  1.00 131.16 ? 222 LYS D HG3  1 
ATOM   16183 H HD2  . LYS D 1 222 ? 6.594   57.840  57.301  1.00 132.06 ? 222 LYS D HD2  1 
ATOM   16184 H HD3  . LYS D 1 222 ? 6.331   57.050  55.947  1.00 132.06 ? 222 LYS D HD3  1 
ATOM   16185 H HE2  . LYS D 1 222 ? 8.886   56.790  57.027  1.00 131.42 ? 222 LYS D HE2  1 
ATOM   16186 H HE3  . LYS D 1 222 ? 7.727   56.020  57.794  1.00 131.42 ? 222 LYS D HE3  1 
ATOM   16187 H HZ1  . LYS D 1 222 ? 8.369   55.572  55.173  1.00 126.55 ? 222 LYS D HZ1  1 
ATOM   16188 H HZ2  . LYS D 1 222 ? 8.700   54.665  56.252  1.00 126.55 ? 222 LYS D HZ2  1 
ATOM   16189 H HZ3  . LYS D 1 222 ? 7.317   54.868  55.876  1.00 126.55 ? 222 LYS D HZ3  1 
ATOM   16190 N N    . CYS D 1 223 ? 4.825   61.170  53.594  1.00 107.42 ? 223 CYS D N    1 
ATOM   16191 C CA   . CYS D 1 223 ? 4.403   62.404  52.939  1.00 111.15 ? 223 CYS D CA   1 
ATOM   16192 C C    . CYS D 1 223 ? 2.884   62.522  52.877  1.00 112.45 ? 223 CYS D C    1 
ATOM   16193 O O    . CYS D 1 223 ? 2.316   63.558  53.239  1.00 115.62 ? 223 CYS D O    1 
ATOM   16194 C CB   . CYS D 1 223 ? 4.979   62.460  51.517  1.00 112.52 ? 223 CYS D CB   1 
ATOM   16195 S SG   . CYS D 1 223 ? 6.715   62.937  51.368  1.00 125.44 ? 223 CYS D SG   1 
ATOM   16196 H H    . CYS D 1 223 ? 5.080   60.559  53.047  1.00 128.90 ? 223 CYS D H    1 
ATOM   16197 H HA   . CYS D 1 223 ? 4.746   63.152  53.451  1.00 133.38 ? 223 CYS D HA   1 
ATOM   16198 H HB2  . CYS D 1 223 ? 4.892   61.579  51.121  1.00 135.02 ? 223 CYS D HB2  1 
ATOM   16199 H HB3  . CYS D 1 223 ? 4.463   63.105  51.008  1.00 135.02 ? 223 CYS D HB3  1 
ATOM   16200 H HG   . CYS D 1 223 ? 7.370   62.271  52.122  1.00 150.53 ? 223 CYS D HG   1 
ATOM   16201 N N    . LYS D 1 224 ? 2.215   61.482  52.385  1.00 111.20 ? 224 LYS D N    1 
ATOM   16202 C CA   . LYS D 1 224 ? 0.764   61.456  52.246  1.00 112.52 ? 224 LYS D CA   1 
ATOM   16203 C C    . LYS D 1 224 ? 0.093   60.639  53.339  1.00 111.65 ? 224 LYS D C    1 
ATOM   16204 O O    . LYS D 1 224 ? -1.030  60.963  53.729  1.00 114.20 ? 224 LYS D O    1 
ATOM   16205 C CB   . LYS D 1 224 ? 0.394   60.895  50.857  1.00 117.02 ? 224 LYS D CB   1 
ATOM   16206 C CG   . LYS D 1 224 ? -1.066  61.075  50.378  1.00 121.87 ? 224 LYS D CG   1 
ATOM   16207 C CD   . LYS D 1 224 ? -2.058  60.362  51.291  1.00 121.10 ? 224 LYS D CD   1 
ATOM   16208 C CE   . LYS D 1 224 ? -3.388  60.041  50.623  1.00 122.28 ? 224 LYS D CE   1 
ATOM   16209 N NZ   . LYS D 1 224 ? -4.204  59.209  51.566  1.00 123.02 ? 224 LYS D NZ   1 
ATOM   16210 H H    . LYS D 1 224 ? 2.593   60.757  52.117  1.00 133.45 ? 224 LYS D H    1 
ATOM   16211 H HA   . LYS D 1 224 ? 0.405   62.356  52.299  1.00 135.02 ? 224 LYS D HA   1 
ATOM   16212 H HB2  . LYS D 1 224 ? 0.959   61.332  50.201  1.00 140.43 ? 224 LYS D HB2  1 
ATOM   16213 H HB3  . LYS D 1 224 ? 0.570   59.942  50.866  1.00 140.43 ? 224 LYS D HB3  1 
ATOM   16214 H HG2  . LYS D 1 224 ? -1.286  62.020  50.371  1.00 146.24 ? 224 LYS D HG2  1 
ATOM   16215 H HG3  . LYS D 1 224 ? -1.157  60.706  49.486  1.00 146.24 ? 224 LYS D HG3  1 
ATOM   16216 H HD2  . LYS D 1 224 ? -1.667  59.525  51.585  1.00 145.32 ? 224 LYS D HD2  1 
ATOM   16217 H HD3  . LYS D 1 224 ? -2.242  60.930  52.056  1.00 145.32 ? 224 LYS D HD3  1 
ATOM   16218 H HE2  . LYS D 1 224 ? -3.867  60.861  50.425  1.00 146.73 ? 224 LYS D HE2  1 
ATOM   16219 H HE3  . LYS D 1 224 ? -3.237  59.540  49.806  1.00 146.73 ? 224 LYS D HE3  1 
ATOM   16220 H HZ1  . LYS D 1 224 ? -4.994  59.022  51.202  1.00 147.62 ? 224 LYS D HZ1  1 
ATOM   16221 H HZ2  . LYS D 1 224 ? -3.781  58.447  51.744  1.00 147.62 ? 224 LYS D HZ2  1 
ATOM   16222 H HZ3  . LYS D 1 224 ? -4.334  59.652  52.327  1.00 147.62 ? 224 LYS D HZ3  1 
ATOM   16223 N N    . ASN D 1 225 ? 0.778   59.630  53.879  1.00 111.21 ? 225 ASN D N    1 
ATOM   16224 C CA   . ASN D 1 225 ? 0.190   58.660  54.794  1.00 111.79 ? 225 ASN D CA   1 
ATOM   16225 C C    . ASN D 1 225 ? -0.604  57.626  53.999  1.00 116.14 ? 225 ASN D C    1 
ATOM   16226 O O    . ASN D 1 225 ? -1.584  57.064  54.504  1.00 119.47 ? 225 ASN D O    1 
ATOM   16227 C CB   . ASN D 1 225 ? -0.700  59.331  55.841  1.00 112.15 ? 225 ASN D CB   1 
ATOM   16228 C CG   . ASN D 1 225 ? -1.138  58.366  56.937  1.00 112.17 ? 225 ASN D CG   1 
ATOM   16229 O OD1  . ASN D 1 225 ? -0.329  57.934  57.760  1.00 118.28 ? 225 ASN D OD1  1 
ATOM   16230 N ND2  . ASN D 1 225 ? -2.417  58.017  56.944  1.00 117.50 ? 225 ASN D ND2  1 
ATOM   16231 H H    . ASN D 1 225 ? 1.611   59.483  53.725  1.00 133.45 ? 225 ASN D H    1 
ATOM   16232 H HA   . ASN D 1 225 ? 0.900   58.214  55.282  1.00 134.15 ? 225 ASN D HA   1 
ATOM   16233 H HB2  . ASN D 1 225 ? -0.209  60.057  56.257  1.00 134.58 ? 225 ASN D HB2  1 
ATOM   16234 H HB3  . ASN D 1 225 ? -1.496  59.675  55.407  1.00 134.58 ? 225 ASN D HB3  1 
ATOM   16235 H HD21 . ASN D 1 225 ? -2.952  58.332  56.349  1.00 141.00 ? 225 ASN D HD21 1 
ATOM   16236 H HD22 . ASN D 1 225 ? -2.711  57.475  57.543  1.00 141.00 ? 225 ASN D HD22 1 
ATOM   16237 N N    . LEU D 1 226 ? -0.201  57.381  52.746  1.00 111.84 ? 226 LEU D N    1 
ATOM   16238 C CA   . LEU D 1 226 ? -0.803  56.325  51.936  1.00 111.28 ? 226 LEU D CA   1 
ATOM   16239 C C    . LEU D 1 226 ? -0.268  54.977  52.408  1.00 107.83 ? 226 LEU D C    1 
ATOM   16240 O O    . LEU D 1 226 ? 0.937   54.713  52.324  1.00 105.48 ? 226 LEU D O    1 
ATOM   16241 C CB   . LEU D 1 226 ? -0.497  56.537  50.457  1.00 110.78 ? 226 LEU D CB   1 
ATOM   16242 C CG   . LEU D 1 226 ? -1.530  56.079  49.422  1.00 107.26 ? 226 LEU D CG   1 
ATOM   16243 C CD1  . LEU D 1 226 ? -2.965  56.190  49.917  1.00 110.51 ? 226 LEU D CD1  1 
ATOM   16244 C CD2  . LEU D 1 226 ? -1.371  56.882  48.123  1.00 107.58 ? 226 LEU D CD2  1 
ATOM   16245 H H    . LEU D 1 226 ? 0.421   57.817  52.344  1.00 134.21 ? 226 LEU D H    1 
ATOM   16246 H HA   . LEU D 1 226 ? -1.767  56.341  52.044  1.00 133.54 ? 226 LEU D HA   1 
ATOM   16247 H HB2  . LEU D 1 226 ? -0.371  57.489  50.318  1.00 132.94 ? 226 LEU D HB2  1 
ATOM   16248 H HB3  . LEU D 1 226 ? 0.324   56.060  50.257  1.00 132.94 ? 226 LEU D HB3  1 
ATOM   16249 H HG   . LEU D 1 226 ? -1.364  55.139  49.253  1.00 128.71 ? 226 LEU D HG   1 
ATOM   16250 H HD11 . LEU D 1 226 ? -3.568  56.048  49.170  1.00 132.61 ? 226 LEU D HD11 1 
ATOM   16251 H HD12 . LEU D 1 226 ? -3.118  55.515  50.597  1.00 132.61 ? 226 LEU D HD12 1 
ATOM   16252 H HD13 . LEU D 1 226 ? -3.104  57.074  50.291  1.00 132.61 ? 226 LEU D HD13 1 
ATOM   16253 H HD21 . LEU D 1 226 ? -2.096  56.653  47.520  1.00 129.10 ? 226 LEU D HD21 1 
ATOM   16254 H HD22 . LEU D 1 226 ? -1.401  57.829  48.331  1.00 129.10 ? 226 LEU D HD22 1 
ATOM   16255 H HD23 . LEU D 1 226 ? -0.519  56.659  47.716  1.00 129.10 ? 226 LEU D HD23 1 
ATOM   16256 N N    . ASP D 1 227 ? -1.162  54.127  52.904  1.00 106.17 ? 227 ASP D N    1 
ATOM   16257 C CA   . ASP D 1 227 ? -0.771  52.854  53.497  1.00 107.10 ? 227 ASP D CA   1 
ATOM   16258 C C    . ASP D 1 227 ? -0.714  51.705  52.494  1.00 106.99 ? 227 ASP D C    1 
ATOM   16259 O O    . ASP D 1 227 ? -0.201  50.634  52.837  1.00 106.48 ? 227 ASP D O    1 
ATOM   16260 C CB   . ASP D 1 227 ? -1.736  52.493  54.638  1.00 105.62 ? 227 ASP D CB   1 
ATOM   16261 C CG   . ASP D 1 227 ? -1.452  53.275  55.915  1.00 111.48 ? 227 ASP D CG   1 
ATOM   16262 O OD1  . ASP D 1 227 ? -1.920  54.428  56.037  1.00 112.43 ? 227 ASP D OD1  1 
ATOM   16263 O OD2  . ASP D 1 227 ? -0.759  52.731  56.805  1.00 110.45 ? 227 ASP D OD2  1 
ATOM   16264 H H    . ASP D 1 227 ? -2.010  54.266  52.909  1.00 127.41 ? 227 ASP D H    1 
ATOM   16265 H HA   . ASP D 1 227 ? 0.118   52.949  53.873  1.00 128.52 ? 227 ASP D HA   1 
ATOM   16266 H HB2  . ASP D 1 227 ? -2.644  52.692  54.359  1.00 126.75 ? 227 ASP D HB2  1 
ATOM   16267 H HB3  . ASP D 1 227 ? -1.650  51.548  54.838  1.00 126.75 ? 227 ASP D HB3  1 
ATOM   16268 N N    . ARG D 1 228 ? -1.213  51.894  51.275  1.00 108.20 ? 228 ARG D N    1 
ATOM   16269 C CA   . ARG D 1 228 ? -1.112  50.870  50.239  1.00 108.79 ? 228 ARG D CA   1 
ATOM   16270 C C    . ARG D 1 228 ? -1.508  51.484  48.902  1.00 108.02 ? 228 ARG D C    1 
ATOM   16271 O O    . ARG D 1 228 ? -2.334  52.401  48.850  1.00 107.63 ? 228 ARG D O    1 
ATOM   16272 C CB   . ARG D 1 228 ? -2.001  49.656  50.551  1.00 109.50 ? 228 ARG D CB   1 
ATOM   16273 C CG   . ARG D 1 228 ? -3.477  49.914  50.322  1.00 115.82 ? 228 ARG D CG   1 
ATOM   16274 C CD   . ARG D 1 228 ? -4.351  48.664  50.428  1.00 125.02 ? 228 ARG D CD   1 
ATOM   16275 N NE   . ARG D 1 228 ? -5.670  49.059  50.911  1.00 134.50 ? 228 ARG D NE   1 
ATOM   16276 C CZ   . ARG D 1 228 ? -6.782  48.350  50.787  1.00 137.20 ? 228 ARG D CZ   1 
ATOM   16277 N NH1  . ARG D 1 228 ? -6.772  47.126  50.287  1.00 134.51 ? 228 ARG D NH1  1 
ATOM   16278 N NH2  . ARG D 1 228 ? -7.938  48.890  51.165  1.00 136.17 ? 228 ARG D NH2  1 
ATOM   16279 H H    . ARG D 1 228 ? -1.618  52.610  51.022  1.00 129.85 ? 228 ARG D H    1 
ATOM   16280 H HA   . ARG D 1 228 ? -0.192  50.567  50.177  1.00 130.55 ? 228 ARG D HA   1 
ATOM   16281 H HB2  . ARG D 1 228 ? -1.736  48.918  49.979  1.00 131.40 ? 228 ARG D HB2  1 
ATOM   16282 H HB3  . ARG D 1 228 ? -1.883  49.413  51.482  1.00 131.40 ? 228 ARG D HB3  1 
ATOM   16283 H HG2  . ARG D 1 228 ? -3.789  50.549  50.985  1.00 138.99 ? 228 ARG D HG2  1 
ATOM   16284 H HG3  . ARG D 1 228 ? -3.595  50.280  49.431  1.00 138.99 ? 228 ARG D HG3  1 
ATOM   16285 H HD2  . ARG D 1 228 ? -4.443  48.248  49.557  1.00 150.02 ? 228 ARG D HD2  1 
ATOM   16286 H HD3  . ARG D 1 228 ? -3.958  48.037  51.055  1.00 150.02 ? 228 ARG D HD3  1 
ATOM   16287 H HE   . ARG D 1 228 ? -5.730  49.818  51.311  1.00 161.39 ? 228 ARG D HE   1 
ATOM   16288 H HH11 . ARG D 1 228 ? -6.031  46.772  50.033  1.00 161.41 ? 228 ARG D HH11 1 
ATOM   16289 H HH12 . ARG D 1 228 ? -7.507  46.685  50.216  1.00 161.41 ? 228 ARG D HH12 1 
ATOM   16290 H HH21 . ARG D 1 228 ? -7.955  49.688  51.485  1.00 163.41 ? 228 ARG D HH21 1 
ATOM   16291 H HH22 . ARG D 1 228 ? -8.667  48.441  51.091  1.00 163.41 ? 228 ARG D HH22 1 
ATOM   16292 N N    . ALA D 1 229 ? -0.935  50.954  47.825  1.00 102.03 ? 229 ALA D N    1 
ATOM   16293 C CA   . ALA D 1 229 ? -1.256  51.450  46.494  1.00 101.91 ? 229 ALA D CA   1 
ATOM   16294 C C    . ALA D 1 229 ? -0.596  50.561  45.453  1.00 98.07  ? 229 ALA D C    1 
ATOM   16295 O O    . ALA D 1 229 ? 0.525   50.089  45.657  1.00 96.14  ? 229 ALA D O    1 
ATOM   16296 C CB   . ALA D 1 229 ? -0.793  52.903  46.320  1.00 101.21 ? 229 ALA D CB   1 
ATOM   16297 H H    . ALA D 1 229 ? -0.363  50.312  47.840  1.00 122.44 ? 229 ALA D H    1 
ATOM   16298 H HA   . ALA D 1 229 ? -2.216  51.410  46.360  1.00 122.30 ? 229 ALA D HA   1 
ATOM   16299 H HB1  . ALA D 1 229 ? -1.017  53.200  45.424  1.00 121.45 ? 229 ALA D HB1  1 
ATOM   16300 H HB2  . ALA D 1 229 ? -1.244  53.458  46.975  1.00 121.45 ? 229 ALA D HB2  1 
ATOM   16301 H HB3  . ALA D 1 229 ? 0.167   52.947  46.452  1.00 121.45 ? 229 ALA D HB3  1 
ATOM   16302 N N    . LYS D 1 230 ? -1.308  50.328  44.350  1.00 100.00 ? 230 LYS D N    1 
ATOM   16303 C CA   . LYS D 1 230 ? -0.745  49.619  43.211  1.00 97.80  ? 230 LYS D CA   1 
ATOM   16304 C C    . LYS D 1 230 ? 0.073   50.589  42.369  1.00 96.24  ? 230 LYS D C    1 
ATOM   16305 O O    . LYS D 1 230 ? -0.430  51.637  41.953  1.00 99.03  ? 230 LYS D O    1 
ATOM   16306 C CB   . LYS D 1 230 ? -1.857  49.004  42.358  1.00 97.59  ? 230 LYS D CB   1 
ATOM   16307 C CG   . LYS D 1 230 ? -2.541  47.806  42.991  1.00 103.00 ? 230 LYS D CG   1 
ATOM   16308 C CD   . LYS D 1 230 ? -3.843  47.469  42.270  1.00 106.02 ? 230 LYS D CD   1 
ATOM   16309 C CE   . LYS D 1 230 ? -3.594  46.997  40.842  1.00 106.62 ? 230 LYS D CE   1 
ATOM   16310 N NZ   . LYS D 1 230 ? -3.591  48.119  39.856  1.00 112.09 ? 230 LYS D NZ   1 
ATOM   16311 H H    . LYS D 1 230 ? -2.125  50.574  44.240  1.00 120.00 ? 230 LYS D H    1 
ATOM   16312 H HA   . LYS D 1 230 ? -0.172  48.902  43.524  1.00 117.35 ? 230 LYS D HA   1 
ATOM   16313 H HB2  . LYS D 1 230 ? -2.535  49.679  42.200  1.00 117.11 ? 230 LYS D HB2  1 
ATOM   16314 H HB3  . LYS D 1 230 ? -1.475  48.713  41.515  1.00 117.11 ? 230 LYS D HB3  1 
ATOM   16315 H HG2  . LYS D 1 230 ? -1.954  47.035  42.938  1.00 123.61 ? 230 LYS D HG2  1 
ATOM   16316 H HG3  . LYS D 1 230 ? -2.746  48.004  43.918  1.00 123.61 ? 230 LYS D HG3  1 
ATOM   16317 H HD2  . LYS D 1 230 ? -4.301  46.761  42.749  1.00 127.22 ? 230 LYS D HD2  1 
ATOM   16318 H HD3  . LYS D 1 230 ? -4.403  48.261  42.235  1.00 127.22 ? 230 LYS D HD3  1 
ATOM   16319 H HE2  . LYS D 1 230 ? -2.730  46.558  40.800  1.00 127.94 ? 230 LYS D HE2  1 
ATOM   16320 H HE3  . LYS D 1 230 ? -4.294  46.375  40.587  1.00 127.94 ? 230 LYS D HE3  1 
ATOM   16321 H HZ1  . LYS D 1 230 ? -3.506  47.798  39.030  1.00 134.51 ? 230 LYS D HZ1  1 
ATOM   16322 H HZ2  . LYS D 1 230 ? -4.353  48.575  39.912  1.00 134.51 ? 230 LYS D HZ2  1 
ATOM   16323 H HZ3  . LYS D 1 230 ? -2.912  48.669  40.023  1.00 134.51 ? 230 LYS D HZ3  1 
ATOM   16324 N N    . ILE D 1 231 ? 1.333   50.247  42.122  1.00 92.68  ? 231 ILE D N    1 
ATOM   16325 C CA   . ILE D 1 231 ? 2.249   51.129  41.409  1.00 93.64  ? 231 ILE D CA   1 
ATOM   16326 C C    . ILE D 1 231 ? 2.488   50.525  40.032  1.00 93.31  ? 231 ILE D C    1 
ATOM   16327 O O    . ILE D 1 231 ? 3.247   49.561  39.876  1.00 89.70  ? 231 ILE D O    1 
ATOM   16328 C CB   . ILE D 1 231 ? 3.565   51.342  42.168  1.00 92.28  ? 231 ILE D CB   1 
ATOM   16329 C CG1  . ILE D 1 231 ? 3.277   51.883  43.566  1.00 94.92  ? 231 ILE D CG1  1 
ATOM   16330 C CG2  . ILE D 1 231 ? 4.466   52.287  41.381  1.00 91.78  ? 231 ILE D CG2  1 
ATOM   16331 C CD1  . ILE D 1 231 ? 2.743   53.302  43.582  1.00 93.52  ? 231 ILE D CD1  1 
ATOM   16332 H H    . ILE D 1 231 ? 1.684   49.499  42.361  1.00 111.21 ? 231 ILE D H    1 
ATOM   16333 H HA   . ILE D 1 231 ? 1.821   51.991  41.292  1.00 112.37 ? 231 ILE D HA   1 
ATOM   16334 H HB   . ILE D 1 231 ? 4.024   50.493  42.264  1.00 110.73 ? 231 ILE D HB   1 
ATOM   16335 H HG12 . ILE D 1 231 ? 2.615   51.314  43.989  1.00 113.91 ? 231 ILE D HG12 1 
ATOM   16336 H HG13 . ILE D 1 231 ? 4.100   51.872  44.078  1.00 113.91 ? 231 ILE D HG13 1 
ATOM   16337 H HG21 . ILE D 1 231 ? 5.267   52.463  41.899  1.00 110.14 ? 231 ILE D HG21 1 
ATOM   16338 H HG22 . ILE D 1 231 ? 4.703   51.869  40.539  1.00 110.14 ? 231 ILE D HG22 1 
ATOM   16339 H HG23 . ILE D 1 231 ? 3.989   53.115  41.217  1.00 110.14 ? 231 ILE D HG23 1 
ATOM   16340 H HD11 . ILE D 1 231 ? 2.678   53.605  44.501  1.00 112.23 ? 231 ILE D HD11 1 
ATOM   16341 H HD12 . ILE D 1 231 ? 3.351   53.874  43.087  1.00 112.23 ? 231 ILE D HD12 1 
ATOM   16342 H HD13 . ILE D 1 231 ? 1.866   53.314  43.167  1.00 112.23 ? 231 ILE D HD13 1 
ATOM   16343 N N    . VAL D 1 232 ? 1.851   51.102  39.020  1.00 91.77  ? 232 VAL D N    1 
ATOM   16344 C CA   . VAL D 1 232 ? 2.094   50.685  37.648  1.00 91.64  ? 232 VAL D CA   1 
ATOM   16345 C C    . VAL D 1 232 ? 3.532   51.017  37.268  1.00 92.10  ? 232 VAL D C    1 
ATOM   16346 O O    . VAL D 1 232 ? 4.042   52.106  37.570  1.00 93.50  ? 232 VAL D O    1 
ATOM   16347 C CB   . VAL D 1 232 ? 1.092   51.361  36.698  1.00 92.81  ? 232 VAL D CB   1 
ATOM   16348 C CG1  . VAL D 1 232 ? 1.696   51.502  35.311  1.00 96.94  ? 232 VAL D CG1  1 
ATOM   16349 C CG2  . VAL D 1 232 ? -0.203  50.561  36.657  1.00 91.80  ? 232 VAL D CG2  1 
ATOM   16350 H H    . VAL D 1 232 ? 1.275   51.736  39.102  1.00 110.12 ? 232 VAL D H    1 
ATOM   16351 H HA   . VAL D 1 232 ? 1.972   49.726  37.578  1.00 109.97 ? 232 VAL D HA   1 
ATOM   16352 H HB   . VAL D 1 232 ? 0.885   52.252  37.021  1.00 111.37 ? 232 VAL D HB   1 
ATOM   16353 H HG11 . VAL D 1 232 ? 0.990   51.710  34.679  1.00 116.33 ? 232 VAL D HG11 1 
ATOM   16354 H HG12 . VAL D 1 232 ? 2.351   52.217  35.323  1.00 116.33 ? 232 VAL D HG12 1 
ATOM   16355 H HG13 . VAL D 1 232 ? 2.123   50.666  35.067  1.00 116.33 ? 232 VAL D HG13 1 
ATOM   16356 H HG21 . VAL D 1 232 ? -0.832  51.009  36.070  1.00 110.16 ? 232 VAL D HG21 1 
ATOM   16357 H HG22 . VAL D 1 232 ? -0.013  49.671  36.323  1.00 110.16 ? 232 VAL D HG22 1 
ATOM   16358 H HG23 . VAL D 1 232 ? -0.568  50.507  37.554  1.00 110.16 ? 232 VAL D HG23 1 
ATOM   16359 N N    . GLN D 1 233 ? 4.187   50.085  36.592  1.00 88.69  ? 233 GLN D N    1 
ATOM   16360 C CA   . GLN D 1 233 ? 5.585   50.188  36.201  1.00 89.94  ? 233 GLN D CA   1 
ATOM   16361 C C    . GLN D 1 233 ? 5.714   49.802  34.738  1.00 91.22  ? 233 GLN D C    1 
ATOM   16362 O O    . GLN D 1 233 ? 4.762   49.304  34.128  1.00 90.06  ? 233 GLN D O    1 
ATOM   16363 C CB   . GLN D 1 233 ? 6.454   49.295  37.102  1.00 89.12  ? 233 GLN D CB   1 
ATOM   16364 C CG   . GLN D 1 233 ? 6.807   49.964  38.446  1.00 90.44  ? 233 GLN D CG   1 
ATOM   16365 C CD   . GLN D 1 233 ? 7.417   49.012  39.467  1.00 88.69  ? 233 GLN D CD   1 
ATOM   16366 O OE1  . GLN D 1 233 ? 8.616   48.730  39.436  1.00 87.47  ? 233 GLN D OE1  1 
ATOM   16367 N NE2  . GLN D 1 233 ? 6.595   48.534  40.391  1.00 87.13  ? 233 GLN D NE2  1 
ATOM   16368 H H    . GLN D 1 233 ? 3.825   49.348  36.338  1.00 106.42 ? 233 GLN D H    1 
ATOM   16369 H HA   . GLN D 1 233 ? 5.904   51.099  36.297  1.00 107.94 ? 233 GLN D HA   1 
ATOM   16370 H HB2  . GLN D 1 233 ? 5.973   48.475  37.292  1.00 106.94 ? 233 GLN D HB2  1 
ATOM   16371 H HB3  . GLN D 1 233 ? 7.283   49.093  36.640  1.00 106.94 ? 233 GLN D HB3  1 
ATOM   16372 H HG2  . GLN D 1 233 ? 7.449   50.672  38.283  1.00 108.53 ? 233 GLN D HG2  1 
ATOM   16373 H HG3  . GLN D 1 233 ? 5.998   50.333  38.833  1.00 108.53 ? 233 GLN D HG3  1 
ATOM   16374 H HE21 . GLN D 1 233 ? 5.767   48.766  40.391  1.00 104.55 ? 233 GLN D HE21 1 
ATOM   16375 H HE22 . GLN D 1 233 ? 6.891   47.993  40.990  1.00 104.55 ? 233 GLN D HE22 1 
ATOM   16376 N N    . PRO D 1 234 ? 6.882   50.054  34.124  1.00 89.24  ? 234 PRO D N    1 
ATOM   16377 C CA   . PRO D 1 234 ? 6.994   49.890  32.667  1.00 90.54  ? 234 PRO D CA   1 
ATOM   16378 C C    . PRO D 1 234 ? 6.392   48.599  32.133  1.00 92.88  ? 234 PRO D C    1 
ATOM   16379 O O    . PRO D 1 234 ? 5.460   48.644  31.324  1.00 93.61  ? 234 PRO D O    1 
ATOM   16380 C CB   . PRO D 1 234 ? 8.511   49.948  32.431  1.00 89.33  ? 234 PRO D CB   1 
ATOM   16381 C CG   . PRO D 1 234 ? 9.006   50.867  33.513  1.00 89.35  ? 234 PRO D CG   1 
ATOM   16382 C CD   . PRO D 1 234 ? 8.125   50.588  34.722  1.00 90.75  ? 234 PRO D CD   1 
ATOM   16383 H HA   . PRO D 1 234 ? 6.557   50.634  32.224  1.00 108.65 ? 234 PRO D HA   1 
ATOM   16384 H HB2  . PRO D 1 234 ? 8.897   49.063  32.517  1.00 107.20 ? 234 PRO D HB2  1 
ATOM   16385 H HB3  . PRO D 1 234 ? 8.699   50.308  31.550  1.00 107.20 ? 234 PRO D HB3  1 
ATOM   16386 H HG2  . PRO D 1 234 ? 9.935   50.670  33.711  1.00 107.22 ? 234 PRO D HG2  1 
ATOM   16387 H HG3  . PRO D 1 234 ? 8.916   51.790  33.227  1.00 107.22 ? 234 PRO D HG3  1 
ATOM   16388 H HD2  . PRO D 1 234 ? 8.537   49.932  35.305  1.00 108.90 ? 234 PRO D HD2  1 
ATOM   16389 H HD3  . PRO D 1 234 ? 7.947   51.405  35.214  1.00 108.90 ? 234 PRO D HD3  1 
ATOM   16390 N N    . ASN D 1 235 ? 6.894   47.448  32.578  1.00 91.04  ? 235 ASN D N    1 
ATOM   16391 C CA   . ASN D 1 235 ? 6.417   46.170  32.062  1.00 88.69  ? 235 ASN D CA   1 
ATOM   16392 C C    . ASN D 1 235 ? 5.831   45.313  33.179  1.00 87.91  ? 235 ASN D C    1 
ATOM   16393 O O    . ASN D 1 235 ? 6.126   44.117  33.275  1.00 85.77  ? 235 ASN D O    1 
ATOM   16394 C CB   . ASN D 1 235 ? 7.558   45.428  31.358  1.00 90.03  ? 235 ASN D CB   1 
ATOM   16395 C CG   . ASN D 1 235 ? 7.214   45.043  29.930  1.00 89.53  ? 235 ASN D CG   1 
ATOM   16396 O OD1  . ASN D 1 235 ? 6.042   44.870  29.586  1.00 85.68  ? 235 ASN D OD1  1 
ATOM   16397 N ND2  . ASN D 1 235 ? 8.237   44.904  29.090  1.00 90.06  ? 235 ASN D ND2  1 
ATOM   16398 H H    . ASN D 1 235 ? 7.508   47.382  33.176  1.00 109.25 ? 235 ASN D H    1 
ATOM   16399 H HA   . ASN D 1 235 ? 5.713   46.332  31.415  1.00 106.43 ? 235 ASN D HA   1 
ATOM   16400 H HB2  . ASN D 1 235 ? 8.341   46.000  31.334  1.00 108.04 ? 235 ASN D HB2  1 
ATOM   16401 H HB3  . ASN D 1 235 ? 7.756   44.615  31.848  1.00 108.04 ? 235 ASN D HB3  1 
ATOM   16402 H HD21 . ASN D 1 235 ? 9.041   45.031  29.366  1.00 108.07 ? 235 ASN D HD21 1 
ATOM   16403 H HD22 . ASN D 1 235 ? 8.093   44.687  28.270  1.00 108.07 ? 235 ASN D HD22 1 
ATOM   16404 N N    . GLY D 1 236 ? 4.996   45.909  34.015  1.00 91.28  ? 236 GLY D N    1 
ATOM   16405 C CA   . GLY D 1 236 ? 4.382   45.187  35.109  1.00 86.43  ? 236 GLY D CA   1 
ATOM   16406 C C    . GLY D 1 236 ? 3.889   46.153  36.164  1.00 87.40  ? 236 GLY D C    1 
ATOM   16407 O O    . GLY D 1 236 ? 4.063   47.368  36.061  1.00 87.67  ? 236 GLY D O    1 
ATOM   16408 H H    . GLY D 1 236 ? 4.768   46.737  33.967  1.00 109.53 ? 236 GLY D H    1 
ATOM   16409 H HA2  . GLY D 1 236 ? 3.630   44.669  34.782  1.00 103.72 ? 236 GLY D HA2  1 
ATOM   16410 H HA3  . GLY D 1 236 ? 5.028   44.586  35.511  1.00 103.72 ? 236 GLY D HA3  1 
ATOM   16411 N N    . TRP D 1 237 ? 3.265   45.578  37.193  1.00 88.19  ? 237 TRP D N    1 
ATOM   16412 C CA   . TRP D 1 237 ? 2.750   46.355  38.310  1.00 86.89  ? 237 TRP D CA   1 
ATOM   16413 C C    . TRP D 1 237 ? 2.953   45.594  39.613  1.00 86.61  ? 237 TRP D C    1 
ATOM   16414 O O    . TRP D 1 237 ? 2.885   44.363  39.655  1.00 83.07  ? 237 TRP D O    1 
ATOM   16415 C CB   . TRP D 1 237 ? 1.263   46.696  38.124  1.00 85.63  ? 237 TRP D CB   1 
ATOM   16416 C CG   . TRP D 1 237 ? 0.333   45.519  38.212  1.00 85.64  ? 237 TRP D CG   1 
ATOM   16417 C CD1  . TRP D 1 237 ? -0.223  44.837  37.169  1.00 87.10  ? 237 TRP D CD1  1 
ATOM   16418 C CD2  . TRP D 1 237 ? -0.159  44.896  39.405  1.00 85.53  ? 237 TRP D CD2  1 
ATOM   16419 N NE1  . TRP D 1 237 ? -1.026  43.827  37.639  1.00 85.09  ? 237 TRP D NE1  1 
ATOM   16420 C CE2  . TRP D 1 237 ? -1.005  43.844  39.008  1.00 85.52  ? 237 TRP D CE2  1 
ATOM   16421 C CE3  . TRP D 1 237 ? 0.035   45.125  40.769  1.00 88.73  ? 237 TRP D CE3  1 
ATOM   16422 C CZ2  . TRP D 1 237 ? -1.652  43.022  39.925  1.00 87.61  ? 237 TRP D CZ2  1 
ATOM   16423 C CZ3  . TRP D 1 237 ? -0.609  44.307  41.679  1.00 86.91  ? 237 TRP D CZ3  1 
ATOM   16424 C CH2  . TRP D 1 237 ? -1.444  43.271  41.254  1.00 85.42  ? 237 TRP D CH2  1 
ATOM   16425 H H    . TRP D 1 237 ? 3.130   44.732  37.264  1.00 105.83 ? 237 TRP D H    1 
ATOM   16426 H HA   . TRP D 1 237 ? 3.249   47.185  38.376  1.00 104.27 ? 237 TRP D HA   1 
ATOM   16427 H HB2  . TRP D 1 237 ? 1.003   47.327  38.813  1.00 102.76 ? 237 TRP D HB2  1 
ATOM   16428 H HB3  . TRP D 1 237 ? 1.146   47.096  37.248  1.00 102.76 ? 237 TRP D HB3  1 
ATOM   16429 H HD1  . TRP D 1 237 ? -0.080  45.029  36.271  1.00 104.52 ? 237 TRP D HD1  1 
ATOM   16430 H HE1  . TRP D 1 237 ? -1.470  43.273  37.153  1.00 102.11 ? 237 TRP D HE1  1 
ATOM   16431 H HE3  . TRP D 1 237 ? 0.587   45.815  41.060  1.00 106.47 ? 237 TRP D HE3  1 
ATOM   16432 H HZ2  . TRP D 1 237 ? -2.206  42.329  39.645  1.00 105.13 ? 237 TRP D HZ2  1 
ATOM   16433 H HZ3  . TRP D 1 237 ? -0.484  44.449  42.590  1.00 104.28 ? 237 TRP D HZ3  1 
ATOM   16434 H HH2  . TRP D 1 237 ? -1.867  42.738  41.888  1.00 102.51 ? 237 TRP D HH2  1 
ATOM   16435 N N    . LEU D 1 238 ? 3.201   46.353  40.677  1.00 84.92  ? 238 LEU D N    1 
ATOM   16436 C CA   . LEU D 1 238 ? 3.373   45.818  42.020  1.00 88.01  ? 238 LEU D CA   1 
ATOM   16437 C C    . LEU D 1 238 ? 2.569   46.666  42.993  1.00 87.73  ? 238 LEU D C    1 
ATOM   16438 O O    . LEU D 1 238 ? 2.465   47.887  42.818  1.00 88.02  ? 238 LEU D O    1 
ATOM   16439 C CB   . LEU D 1 238 ? 4.848   45.799  42.429  1.00 87.63  ? 238 LEU D CB   1 
ATOM   16440 C CG   . LEU D 1 238 ? 5.775   44.824  41.698  1.00 86.39  ? 238 LEU D CG   1 
ATOM   16441 C CD1  . LEU D 1 238 ? 7.195   44.942  42.263  1.00 84.79  ? 238 LEU D CD1  1 
ATOM   16442 C CD2  . LEU D 1 238 ? 5.277   43.386  41.789  1.00 83.73  ? 238 LEU D CD2  1 
ATOM   16443 H H    . LEU D 1 238 ? 3.277   47.209  40.643  1.00 101.90 ? 238 LEU D H    1 
ATOM   16444 H HA   . LEU D 1 238 ? 3.043   44.906  42.059  1.00 105.62 ? 238 LEU D HA   1 
ATOM   16445 H HB2  . LEU D 1 238 ? 5.207   46.688  42.284  1.00 105.15 ? 238 LEU D HB2  1 
ATOM   16446 H HB3  . LEU D 1 238 ? 4.891   45.573  43.371  1.00 105.15 ? 238 LEU D HB3  1 
ATOM   16447 H HG   . LEU D 1 238 ? 5.787   45.055  40.756  1.00 103.66 ? 238 LEU D HG   1 
ATOM   16448 H HD11 . LEU D 1 238 ? 7.773   44.320  41.794  1.00 101.74 ? 238 LEU D HD11 1 
ATOM   16449 H HD12 . LEU D 1 238 ? 7.512   45.850  42.134  1.00 101.74 ? 238 LEU D HD12 1 
ATOM   16450 H HD13 . LEU D 1 238 ? 7.177   44.729  43.209  1.00 101.74 ? 238 LEU D HD13 1 
ATOM   16451 H HD21 . LEU D 1 238 ? 5.903   42.805  41.330  1.00 100.48 ? 238 LEU D HD21 1 
ATOM   16452 H HD22 . LEU D 1 238 ? 5.213   43.132  42.723  1.00 100.48 ? 238 LEU D HD22 1 
ATOM   16453 H HD23 . LEU D 1 238 ? 4.404   43.327  41.370  1.00 100.48 ? 238 LEU D HD23 1 
ATOM   16454 N N    . GLU D 1 239 ? 1.999   46.024  44.008  1.00 88.50  ? 239 GLU D N    1 
ATOM   16455 C CA   . GLU D 1 239 ? 1.250   46.716  45.046  1.00 94.34  ? 239 GLU D CA   1 
ATOM   16456 C C    . GLU D 1 239 ? 2.036   46.667  46.348  1.00 89.96  ? 239 GLU D C    1 
ATOM   16457 O O    . GLU D 1 239 ? 2.318   45.584  46.867  1.00 88.93  ? 239 GLU D O    1 
ATOM   16458 C CB   . GLU D 1 239 ? -0.134  46.103  45.254  1.00 94.86  ? 239 GLU D CB   1 
ATOM   16459 C CG   . GLU D 1 239 ? -0.889  46.750  46.416  1.00 95.09  ? 239 GLU D CG   1 
ATOM   16460 C CD   . GLU D 1 239 ? -2.377  46.469  46.388  1.00 97.34  ? 239 GLU D CD   1 
ATOM   16461 O OE1  . GLU D 1 239 ? -2.752  45.295  46.194  1.00 96.30  ? 239 GLU D OE1  1 
ATOM   16462 O OE2  . GLU D 1 239 ? -3.170  47.419  46.563  1.00 101.56 ? 239 GLU D OE2  1 
ATOM   16463 H H    . GLU D 1 239 ? 2.034   45.171  44.116  1.00 106.20 ? 239 GLU D H    1 
ATOM   16464 H HA   . GLU D 1 239 ? 1.139   47.642  44.777  1.00 113.21 ? 239 GLU D HA   1 
ATOM   16465 H HB2  . GLU D 1 239 ? -0.659  46.225  44.448  1.00 113.84 ? 239 GLU D HB2  1 
ATOM   16466 H HB3  . GLU D 1 239 ? -0.036  45.158  45.447  1.00 113.84 ? 239 GLU D HB3  1 
ATOM   16467 H HG2  . GLU D 1 239 ? -0.536  46.407  47.251  1.00 114.10 ? 239 GLU D HG2  1 
ATOM   16468 H HG3  . GLU D 1 239 ? -0.766  47.712  46.374  1.00 114.10 ? 239 GLU D HG3  1 
ATOM   16469 N N    . TYR D 1 240 ? 2.379   47.834  46.875  1.00 92.56  ? 240 TYR D N    1 
ATOM   16470 C CA   . TYR D 1 240 ? 2.971   47.953  48.203  1.00 97.84  ? 240 TYR D CA   1 
ATOM   16471 C C    . TYR D 1 240 ? 1.857   48.019  49.242  1.00 99.11  ? 240 TYR D C    1 
ATOM   16472 O O    . TYR D 1 240 ? 0.800   48.609  49.001  1.00 98.44  ? 240 TYR D O    1 
ATOM   16473 C CB   . TYR D 1 240 ? 3.893   49.182  48.269  1.00 95.96  ? 240 TYR D CB   1 
ATOM   16474 C CG   . TYR D 1 240 ? 3.268   50.493  48.715  1.00 100.43 ? 240 TYR D CG   1 
ATOM   16475 C CD1  . TYR D 1 240 ? 2.910   50.691  49.999  1.00 100.63 ? 240 TYR D CD1  1 
ATOM   16476 C CD2  . TYR D 1 240 ? 3.050   51.542  47.839  1.00 97.50  ? 240 TYR D CD2  1 
ATOM   16477 C CE1  . TYR D 1 240 ? 2.336   51.874  50.404  1.00 100.86 ? 240 TYR D CE1  1 
ATOM   16478 C CE2  . TYR D 1 240 ? 2.487   52.739  48.280  1.00 99.55  ? 240 TYR D CE2  1 
ATOM   16479 C CZ   . TYR D 1 240 ? 2.156   52.883  49.598  1.00 101.32 ? 240 TYR D CZ   1 
ATOM   16480 O OH   . TYR D 1 240 ? 1.598   54.033  50.106  1.00 105.14 ? 240 TYR D OH   1 
ATOM   16481 H H    . TYR D 1 240 ? 2.278   48.589  46.475  1.00 111.07 ? 240 TYR D H    1 
ATOM   16482 H HA   . TYR D 1 240 ? 3.521   47.182  48.410  1.00 117.41 ? 240 TYR D HA   1 
ATOM   16483 H HB2  . TYR D 1 240 ? 4.609   48.985  48.892  1.00 115.15 ? 240 TYR D HB2  1 
ATOM   16484 H HB3  . TYR D 1 240 ? 4.256   49.331  47.382  1.00 115.15 ? 240 TYR D HB3  1 
ATOM   16485 H HD1  . TYR D 1 240 ? 3.052   50.015  50.622  1.00 120.76 ? 240 TYR D HD1  1 
ATOM   16486 H HD2  . TYR D 1 240 ? 3.281   51.447  46.943  1.00 117.00 ? 240 TYR D HD2  1 
ATOM   16487 H HE1  . TYR D 1 240 ? 2.065   51.957  51.290  1.00 121.03 ? 240 TYR D HE1  1 
ATOM   16488 H HE2  . TYR D 1 240 ? 2.338   53.435  47.681  1.00 119.46 ? 240 TYR D HE2  1 
ATOM   16489 H HH   . TYR D 1 240 ? 1.530   54.612  49.501  1.00 126.16 ? 240 TYR D HH   1 
ATOM   16490 N N    . ILE D 1 241 ? 2.088   47.379  50.389  1.00 108.69 ? 241 ILE D N    1 
ATOM   16491 C CA   . ILE D 1 241 ? 1.097   47.357  51.461  1.00 104.94 ? 241 ILE D CA   1 
ATOM   16492 C C    . ILE D 1 241 ? 1.814   47.387  52.807  1.00 103.90 ? 241 ILE D C    1 
ATOM   16493 O O    . ILE D 1 241 ? 2.466   46.412  53.199  1.00 106.62 ? 241 ILE D O    1 
ATOM   16494 C CB   . ILE D 1 241 ? 0.197   46.119  51.368  1.00 103.29 ? 241 ILE D CB   1 
ATOM   16495 C CG1  . ILE D 1 241 ? 1.025   44.935  50.851  1.00 107.57 ? 241 ILE D CG1  1 
ATOM   16496 C CG2  . ILE D 1 241 ? -0.958  46.346  50.397  1.00 104.83 ? 241 ILE D CG2  1 
ATOM   16497 C CD1  . ILE D 1 241 ? 0.278   43.659  50.803  1.00 107.71 ? 241 ILE D CD1  1 
ATOM   16498 H H    . ILE D 1 241 ? 2.812   46.951  50.569  1.00 130.44 ? 241 ILE D H    1 
ATOM   16499 H HA   . ILE D 1 241 ? 0.540   48.147  51.382  1.00 125.92 ? 241 ILE D HA   1 
ATOM   16500 H HB   . ILE D 1 241 ? -0.159  45.942  52.253  1.00 123.94 ? 241 ILE D HB   1 
ATOM   16501 H HG12 . ILE D 1 241 ? 1.327   45.135  49.951  1.00 129.08 ? 241 ILE D HG12 1 
ATOM   16502 H HG13 . ILE D 1 241 ? 1.788   44.809  51.437  1.00 129.08 ? 241 ILE D HG13 1 
ATOM   16503 H HG21 . ILE D 1 241 ? -1.504  45.545  50.364  1.00 125.80 ? 241 ILE D HG21 1 
ATOM   16504 H HG22 . ILE D 1 241 ? -1.489  47.096  50.708  1.00 125.80 ? 241 ILE D HG22 1 
ATOM   16505 H HG23 . ILE D 1 241 ? -0.598  46.537  49.517  1.00 125.80 ? 241 ILE D HG23 1 
ATOM   16506 H HD11 . ILE D 1 241 ? 0.864   42.962  50.468  1.00 129.25 ? 241 ILE D HD11 1 
ATOM   16507 H HD12 . ILE D 1 241 ? -0.025  43.436  51.697  1.00 129.25 ? 241 ILE D HD12 1 
ATOM   16508 H HD13 . ILE D 1 241 ? -0.485  43.762  50.212  1.00 129.25 ? 241 ILE D HD13 1 
ATOM   16509 N N    . ILE D 1 242 ? 1.717   48.512  53.517  1.00 106.22 ? 242 ILE D N    1 
ATOM   16510 C CA   . ILE D 1 242 ? 2.301   48.674  54.843  1.00 107.36 ? 242 ILE D CA   1 
ATOM   16511 C C    . ILE D 1 242 ? 1.283   48.174  55.855  1.00 111.14 ? 242 ILE D C    1 
ATOM   16512 O O    . ILE D 1 242 ? 0.101   48.533  55.796  1.00 111.32 ? 242 ILE D O    1 
ATOM   16513 C CB   . ILE D 1 242 ? 2.653   50.136  55.137  1.00 107.29 ? 242 ILE D CB   1 
ATOM   16514 C CG1  . ILE D 1 242 ? 3.636   50.698  54.119  1.00 99.94  ? 242 ILE D CG1  1 
ATOM   16515 C CG2  . ILE D 1 242 ? 3.311   50.281  56.515  1.00 103.78 ? 242 ILE D CG2  1 
ATOM   16516 C CD1  . ILE D 1 242 ? 3.001   51.092  53.020  1.00 103.96 ? 242 ILE D CD1  1 
ATOM   16517 H H    . ILE D 1 242 ? 1.306   49.215  53.241  1.00 127.46 ? 242 ILE D H    1 
ATOM   16518 H HA   . ILE D 1 242 ? 3.115   48.150  54.898  1.00 128.84 ? 242 ILE D HA   1 
ATOM   16519 H HB   . ILE D 1 242 ? 1.814   50.622  55.097  1.00 128.75 ? 242 ILE D HB   1 
ATOM   16520 H HG12 . ILE D 1 242 ? 4.096   51.462  54.500  1.00 119.92 ? 242 ILE D HG12 1 
ATOM   16521 H HG13 . ILE D 1 242 ? 4.277   50.012  53.876  1.00 119.92 ? 242 ILE D HG13 1 
ATOM   16522 H HG21 . ILE D 1 242 ? 3.675   51.176  56.599  1.00 124.53 ? 242 ILE D HG21 1 
ATOM   16523 H HG22 . ILE D 1 242 ? 2.642   50.131  57.201  1.00 124.53 ? 242 ILE D HG22 1 
ATOM   16524 H HG23 . ILE D 1 242 ? 4.021   49.626  56.596  1.00 124.53 ? 242 ILE D HG23 1 
ATOM   16525 H HD11 . ILE D 1 242 ? 3.648   51.454  52.394  1.00 124.75 ? 242 ILE D HD11 1 
ATOM   16526 H HD12 . ILE D 1 242 ? 2.550   50.329  52.625  1.00 124.75 ? 242 ILE D HD12 1 
ATOM   16527 H HD13 . ILE D 1 242 ? 2.352   51.773  53.257  1.00 124.75 ? 242 ILE D HD13 1 
ATOM   16528 N N    . GLU D 1 243 ? 1.737   47.363  56.798  1.00 110.39 ? 243 GLU D N    1 
ATOM   16529 C CA   . GLU D 1 243 ? 0.820   46.733  57.740  1.00 117.05 ? 243 GLU D CA   1 
ATOM   16530 C C    . GLU D 1 243 ? 1.587   46.397  59.004  1.00 118.51 ? 243 GLU D C    1 
ATOM   16531 O O    . GLU D 1 243 ? 2.574   45.658  58.948  1.00 117.13 ? 243 GLU D O    1 
ATOM   16532 C CB   . GLU D 1 243 ? 0.205   45.480  57.120  1.00 117.70 ? 243 GLU D CB   1 
ATOM   16533 C CG   . GLU D 1 243 ? -0.889  44.854  57.951  1.00 120.62 ? 243 GLU D CG   1 
ATOM   16534 C CD   . GLU D 1 243 ? -0.970  43.355  57.752  1.00 124.46 ? 243 GLU D CD   1 
ATOM   16535 O OE1  . GLU D 1 243 ? -0.832  42.897  56.595  1.00 122.26 ? 243 GLU D OE1  1 
ATOM   16536 O OE2  . GLU D 1 243 ? -1.171  42.638  58.755  1.00 124.48 ? 243 GLU D OE2  1 
ATOM   16537 H H    . GLU D 1 243 ? 2.565   47.162  56.914  1.00 132.47 ? 243 GLU D H    1 
ATOM   16538 H HA   . GLU D 1 243 ? 0.107   47.348  57.973  1.00 140.46 ? 243 GLU D HA   1 
ATOM   16539 H HB2  . GLU D 1 243 ? -0.175  45.714  56.259  1.00 141.25 ? 243 GLU D HB2  1 
ATOM   16540 H HB3  . GLU D 1 243 ? 0.903   44.816  57.005  1.00 141.25 ? 243 GLU D HB3  1 
ATOM   16541 H HG2  . GLU D 1 243 ? -0.714  45.026  58.889  1.00 144.74 ? 243 GLU D HG2  1 
ATOM   16542 H HG3  . GLU D 1 243 ? -1.742  45.240  57.696  1.00 144.74 ? 243 GLU D HG3  1 
ATOM   16543 N N    . ASN D 1 244 ? 1.140   46.933  60.134  1.00 120.37 ? 244 ASN D N    1 
ATOM   16544 C CA   . ASN D 1 244 ? 1.793   46.711  61.415  1.00 124.49 ? 244 ASN D CA   1 
ATOM   16545 C C    . ASN D 1 244 ? 3.301   46.923  61.284  1.00 122.65 ? 244 ASN D C    1 
ATOM   16546 O O    . ASN D 1 244 ? 4.112   46.043  61.559  1.00 123.34 ? 244 ASN D O    1 
ATOM   16547 C CB   . ASN D 1 244 ? 1.483   45.305  61.938  1.00 125.39 ? 244 ASN D CB   1 
ATOM   16548 C CG   . ASN D 1 244 ? 0.086   44.834  61.568  1.00 126.58 ? 244 ASN D CG   1 
ATOM   16549 O OD1  . ASN D 1 244 ? -0.846  45.636  61.488  1.00 128.59 ? 244 ASN D OD1  1 
ATOM   16550 N ND2  . ASN D 1 244 ? -0.065  43.534  61.339  1.00 126.68 ? 244 ASN D ND2  1 
ATOM   16551 H H    . ASN D 1 244 ? 0.446   47.439  60.184  1.00 144.44 ? 244 ASN D H    1 
ATOM   16552 H HA   . ASN D 1 244 ? 1.454   47.355  62.057  1.00 149.39 ? 244 ASN D HA   1 
ATOM   16553 H HB2  . ASN D 1 244 ? 2.121   44.680  61.560  1.00 150.47 ? 244 ASN D HB2  1 
ATOM   16554 H HB3  . ASN D 1 244 ? 1.553   45.306  62.906  1.00 150.47 ? 244 ASN D HB3  1 
ATOM   16555 H HD21 . ASN D 1 244 ? 0.609   43.004  61.403  1.00 152.02 ? 244 ASN D HD21 1 
ATOM   16556 H HD22 . ASN D 1 244 ? -0.838  43.222  61.126  1.00 152.02 ? 244 ASN D HD22 1 
ATOM   16557 N N    . ASP D 1 245 ? 3.647   48.117  60.821  1.00 118.37 ? 245 ASP D N    1 
ATOM   16558 C CA   . ASP D 1 245 ? 5.035   48.508  60.562  1.00 118.76 ? 245 ASP D CA   1 
ATOM   16559 C C    . ASP D 1 245 ? 5.833   47.383  59.894  1.00 118.33 ? 245 ASP D C    1 
ATOM   16560 O O    . ASP D 1 245 ? 6.964   47.064  60.253  1.00 118.34 ? 245 ASP D O    1 
ATOM   16561 C CB   . ASP D 1 245 ? 5.736   48.967  61.847  1.00 124.46 ? 245 ASP D CB   1 
ATOM   16562 C CG   . ASP D 1 245 ? 5.659   47.931  62.976  1.00 127.74 ? 245 ASP D CG   1 
ATOM   16563 O OD1  . ASP D 1 245 ? 6.032   46.758  62.758  1.00 126.37 ? 245 ASP D OD1  1 
ATOM   16564 O OD2  . ASP D 1 245 ? 5.240   48.303  64.096  1.00 131.03 ? 245 ASP D OD2  1 
ATOM   16565 H H    . ASP D 1 245 ? 3.083   48.740  60.642  1.00 142.05 ? 245 ASP D H    1 
ATOM   16566 H HA   . ASP D 1 245 ? 5.007   49.254  59.943  1.00 142.52 ? 245 ASP D HA   1 
ATOM   16567 H HB2  . ASP D 1 245 ? 6.672   49.130  61.654  1.00 149.36 ? 245 ASP D HB2  1 
ATOM   16568 H HB3  . ASP D 1 245 ? 5.315   49.783  62.161  1.00 149.36 ? 245 ASP D HB3  1 
ATOM   16569 N N    . GLU D 1 246 ? 5.212   46.772  58.875  1.00 115.04 ? 246 GLU D N    1 
ATOM   16570 C CA   . GLU D 1 246 ? 5.869   45.769  58.036  1.00 110.97 ? 246 GLU D CA   1 
ATOM   16571 C C    . GLU D 1 246 ? 5.500   46.015  56.579  1.00 106.66 ? 246 GLU D C    1 
ATOM   16572 O O    . GLU D 1 246 ? 4.314   46.091  56.244  1.00 106.18 ? 246 GLU D O    1 
ATOM   16573 C CB   . GLU D 1 246 ? 5.468   44.338  58.444  1.00 111.03 ? 246 GLU D CB   1 
ATOM   16574 C CG   . GLU D 1 246 ? 5.844   43.953  59.868  1.00 115.46 ? 246 GLU D CG   1 
ATOM   16575 C CD   . GLU D 1 246 ? 6.657   42.671  59.938  1.00 116.23 ? 246 GLU D CD   1 
ATOM   16576 O OE1  . GLU D 1 246 ? 6.145   41.611  59.515  1.00 116.64 ? 246 GLU D OE1  1 
ATOM   16577 O OE2  . GLU D 1 246 ? 7.810   42.724  60.416  1.00 118.61 ? 246 GLU D OE2  1 
ATOM   16578 H H    . GLU D 1 246 ? 4.397   46.926  58.649  1.00 138.05 ? 246 GLU D H    1 
ATOM   16579 H HA   . GLU D 1 246 ? 6.830   45.856  58.132  1.00 133.16 ? 246 GLU D HA   1 
ATOM   16580 H HB2  . GLU D 1 246 ? 4.505   44.253  58.363  1.00 133.23 ? 246 GLU D HB2  1 
ATOM   16581 H HB3  . GLU D 1 246 ? 5.907   43.713  57.846  1.00 133.23 ? 246 GLU D HB3  1 
ATOM   16582 H HG2  . GLU D 1 246 ? 6.374   44.666  60.258  1.00 138.55 ? 246 GLU D HG2  1 
ATOM   16583 H HG3  . GLU D 1 246 ? 5.033   43.822  60.384  1.00 138.55 ? 246 GLU D HG3  1 
ATOM   16584 N N    . MET D 1 247 ? 6.515   46.152  55.725  1.00 100.20 ? 247 MET D N    1 
ATOM   16585 C CA   . MET D 1 247 ? 6.306   46.345  54.294  1.00 99.02  ? 247 MET D CA   1 
ATOM   16586 C C    . MET D 1 247 ? 6.068   45.010  53.601  1.00 96.09  ? 247 MET D C    1 
ATOM   16587 O O    . MET D 1 247 ? 6.724   44.010  53.903  1.00 96.35  ? 247 MET D O    1 
ATOM   16588 C CB   . MET D 1 247 ? 7.521   47.035  53.666  1.00 94.38  ? 247 MET D CB   1 
ATOM   16589 C CG   . MET D 1 247 ? 7.319   47.566  52.256  1.00 89.13  ? 247 MET D CG   1 
ATOM   16590 S SD   . MET D 1 247 ? 6.610   49.218  52.156  1.00 98.11  ? 247 MET D SD   1 
ATOM   16591 C CE   . MET D 1 247 ? 4.974   48.801  51.573  1.00 94.15  ? 247 MET D CE   1 
ATOM   16592 H H    . MET D 1 247 ? 7.344   46.135  55.954  1.00 120.24 ? 247 MET D H    1 
ATOM   16593 H HA   . MET D 1 247 ? 5.531   46.914  54.165  1.00 118.83 ? 247 MET D HA   1 
ATOM   16594 H HB2  . MET D 1 247 ? 7.766   47.789  54.225  1.00 113.26 ? 247 MET D HB2  1 
ATOM   16595 H HB3  . MET D 1 247 ? 8.250   46.397  53.632  1.00 113.26 ? 247 MET D HB3  1 
ATOM   16596 H HG2  . MET D 1 247 ? 8.181   47.593  51.811  1.00 106.96 ? 247 MET D HG2  1 
ATOM   16597 H HG3  . MET D 1 247 ? 6.722   46.964  51.784  1.00 106.96 ? 247 MET D HG3  1 
ATOM   16598 H HE1  . MET D 1 247 ? 4.456   49.616  51.474  1.00 112.98 ? 247 MET D HE1  1 
ATOM   16599 H HE2  . MET D 1 247 ? 5.048   48.351  50.717  1.00 112.98 ? 247 MET D HE2  1 
ATOM   16600 H HE3  . MET D 1 247 ? 4.548   48.215  52.219  1.00 112.98 ? 247 MET D HE3  1 
ATOM   16601 N N    . TYR D 1 248 ? 5.132   45.001  52.658  1.00 96.35  ? 248 TYR D N    1 
ATOM   16602 C CA   . TYR D 1 248 ? 4.845   43.812  51.864  1.00 94.44  ? 248 TYR D CA   1 
ATOM   16603 C C    . TYR D 1 248 ? 4.684   44.235  50.412  1.00 94.64  ? 248 TYR D C    1 
ATOM   16604 O O    . TYR D 1 248 ? 4.065   45.264  50.125  1.00 96.46  ? 248 TYR D O    1 
ATOM   16605 C CB   . TYR D 1 248 ? 3.586   43.098  52.335  1.00 97.67  ? 248 TYR D CB   1 
ATOM   16606 C CG   . TYR D 1 248 ? 3.632   42.637  53.780  1.00 99.01  ? 248 TYR D CG   1 
ATOM   16607 C CD1  . TYR D 1 248 ? 4.315   41.479  54.134  1.00 96.53  ? 248 TYR D CD1  1 
ATOM   16608 C CD2  . TYR D 1 248 ? 2.982   43.347  54.777  1.00 101.94 ? 248 TYR D CD2  1 
ATOM   16609 C CE1  . TYR D 1 248 ? 4.354   41.051  55.440  1.00 100.31 ? 248 TYR D CE1  1 
ATOM   16610 C CE2  . TYR D 1 248 ? 3.018   42.925  56.082  1.00 104.93 ? 248 TYR D CE2  1 
ATOM   16611 C CZ   . TYR D 1 248 ? 3.702   41.778  56.409  1.00 104.86 ? 248 TYR D CZ   1 
ATOM   16612 O OH   . TYR D 1 248 ? 3.740   41.350  57.718  1.00 108.98 ? 248 TYR D OH   1 
ATOM   16613 H H    . TYR D 1 248 ? 4.643   45.679  52.457  1.00 115.62 ? 248 TYR D H    1 
ATOM   16614 H HA   . TYR D 1 248 ? 5.582   43.186  51.936  1.00 113.33 ? 248 TYR D HA   1 
ATOM   16615 H HB2  . TYR D 1 248 ? 2.833   43.704  52.244  1.00 117.20 ? 248 TYR D HB2  1 
ATOM   16616 H HB3  . TYR D 1 248 ? 3.449   42.314  51.781  1.00 117.20 ? 248 TYR D HB3  1 
ATOM   16617 H HD1  . TYR D 1 248 ? 4.752   40.987  53.477  1.00 115.83 ? 248 TYR D HD1  1 
ATOM   16618 H HD2  . TYR D 1 248 ? 2.515   44.121  54.559  1.00 122.32 ? 248 TYR D HD2  1 
ATOM   16619 H HE1  . TYR D 1 248 ? 4.816   40.276  55.666  1.00 120.37 ? 248 TYR D HE1  1 
ATOM   16620 H HE2  . TYR D 1 248 ? 2.580   43.412  56.742  1.00 125.92 ? 248 TYR D HE2  1 
ATOM   16621 H HH   . TYR D 1 248 ? 3.368   41.915  58.216  1.00 130.77 ? 248 TYR D HH   1 
ATOM   16622 N N    . ILE D 1 249 ? 5.257   43.456  49.502  1.00 93.47  ? 249 ILE D N    1 
ATOM   16623 C CA   . ILE D 1 249 ? 5.151   43.705  48.068  1.00 86.45  ? 249 ILE D CA   1 
ATOM   16624 C C    . ILE D 1 249 ? 4.310   42.584  47.473  1.00 86.37  ? 249 ILE D C    1 
ATOM   16625 O O    . ILE D 1 249 ? 4.684   41.409  47.562  1.00 84.39  ? 249 ILE D O    1 
ATOM   16626 C CB   . ILE D 1 249 ? 6.540   43.788  47.408  1.00 88.11  ? 249 ILE D CB   1 
ATOM   16627 C CG1  . ILE D 1 249 ? 7.278   45.052  47.884  1.00 87.32  ? 249 ILE D CG1  1 
ATOM   16628 C CG2  . ILE D 1 249 ? 6.435   43.793  45.878  1.00 88.33  ? 249 ILE D CG2  1 
ATOM   16629 C CD1  . ILE D 1 249 ? 6.795   46.356  47.264  1.00 85.25  ? 249 ILE D CD1  1 
ATOM   16630 H H    . ILE D 1 249 ? 5.724   42.760  49.695  1.00 112.16 ? 249 ILE D H    1 
ATOM   16631 H HA   . ILE D 1 249 ? 4.693   44.545  47.908  1.00 103.74 ? 249 ILE D HA   1 
ATOM   16632 H HB   . ILE D 1 249 ? 7.039   43.001  47.675  1.00 105.73 ? 249 ILE D HB   1 
ATOM   16633 H HG12 . ILE D 1 249 ? 7.167   45.129  48.845  1.00 104.78 ? 249 ILE D HG12 1 
ATOM   16634 H HG13 . ILE D 1 249 ? 8.219   44.958  47.666  1.00 104.78 ? 249 ILE D HG13 1 
ATOM   16635 H HG21 . ILE D 1 249 ? 7.274   44.103  45.505  1.00 105.99 ? 249 ILE D HG21 1 
ATOM   16636 H HG22 . ILE D 1 249 ? 6.250   42.891  45.571  1.00 105.99 ? 249 ILE D HG22 1 
ATOM   16637 H HG23 . ILE D 1 249 ? 5.715   44.386  45.613  1.00 105.99 ? 249 ILE D HG23 1 
ATOM   16638 H HD11 . ILE D 1 249 ? 7.282   47.094  47.662  1.00 102.30 ? 249 ILE D HD11 1 
ATOM   16639 H HD12 . ILE D 1 249 ? 6.956   46.330  46.308  1.00 102.30 ? 249 ILE D HD12 1 
ATOM   16640 H HD13 . ILE D 1 249 ? 5.845   46.455  47.437  1.00 102.30 ? 249 ILE D HD13 1 
ATOM   16641 N N    . ASP D 1 250 ? 3.157   42.943  46.925  1.00 87.49  ? 250 ASP D N    1 
ATOM   16642 C CA   . ASP D 1 250 ? 2.276   42.048  46.191  1.00 88.53  ? 250 ASP D CA   1 
ATOM   16643 C C    . ASP D 1 250 ? 2.442   42.300  44.696  1.00 88.34  ? 250 ASP D C    1 
ATOM   16644 O O    . ASP D 1 250 ? 2.818   43.393  44.267  1.00 90.73  ? 250 ASP D O    1 
ATOM   16645 C CB   . ASP D 1 250 ? 0.818   42.266  46.606  1.00 89.54  ? 250 ASP D CB   1 
ATOM   16646 C CG   . ASP D 1 250 ? -0.046  41.035  46.381  1.00 85.74  ? 250 ASP D CG   1 
ATOM   16647 O OD1  . ASP D 1 250 ? 0.018   40.432  45.298  1.00 87.64  ? 250 ASP D OD1  1 
ATOM   16648 O OD2  . ASP D 1 250 ? -0.812  40.677  47.297  1.00 93.43  ? 250 ASP D OD2  1 
ATOM   16649 H H    . ASP D 1 250 ? 2.848   43.745  46.967  1.00 104.99 ? 250 ASP D H    1 
ATOM   16650 H HA   . ASP D 1 250 ? 2.501   41.124  46.383  1.00 106.24 ? 250 ASP D HA   1 
ATOM   16651 H HB2  . ASP D 1 250 ? 0.787   42.485  47.550  1.00 107.45 ? 250 ASP D HB2  1 
ATOM   16652 H HB3  . ASP D 1 250 ? 0.446   42.993  46.083  1.00 107.45 ? 250 ASP D HB3  1 
ATOM   16653 N N    . GLY D 1 251 ? 2.142   41.273  43.898  1.00 85.68  ? 251 GLY D N    1 
ATOM   16654 C CA   . GLY D 1 251 ? 2.193   41.402  42.459  1.00 86.46  ? 251 GLY D CA   1 
ATOM   16655 C C    . GLY D 1 251 ? 1.988   40.093  41.723  1.00 85.29  ? 251 GLY D C    1 
ATOM   16656 O O    . GLY D 1 251 ? 1.919   39.021  42.333  1.00 84.03  ? 251 GLY D O    1 
ATOM   16657 H H    . GLY D 1 251 ? 1.906   40.494  44.175  1.00 102.81 ? 251 GLY D H    1 
ATOM   16658 H HA2  . GLY D 1 251 ? 1.503   42.019  42.172  1.00 103.75 ? 251 GLY D HA2  1 
ATOM   16659 H HA3  . GLY D 1 251 ? 3.060   41.756  42.204  1.00 103.75 ? 251 GLY D HA3  1 
ATOM   16660 N N    . PRO D 1 252 ? 1.904   40.154  40.391  1.00 84.62  ? 252 PRO D N    1 
ATOM   16661 C CA   . PRO D 1 252 ? 1.665   38.940  39.607  1.00 83.92  ? 252 PRO D CA   1 
ATOM   16662 C C    . PRO D 1 252 ? 2.934   38.225  39.171  1.00 80.95  ? 252 PRO D C    1 
ATOM   16663 O O    . PRO D 1 252 ? 3.995   38.822  38.969  1.00 79.88  ? 252 PRO D O    1 
ATOM   16664 C CB   . PRO D 1 252 ? 0.900   39.454  38.376  1.00 79.11  ? 252 PRO D CB   1 
ATOM   16665 C CG   . PRO D 1 252 ? 0.966   40.973  38.428  1.00 82.54  ? 252 PRO D CG   1 
ATOM   16666 C CD   . PRO D 1 252 ? 1.896   41.360  39.545  1.00 84.58  ? 252 PRO D CD   1 
ATOM   16667 H HA   . PRO D 1 252 ? 1.112   38.328  40.119  1.00 100.71 ? 252 PRO D HA   1 
ATOM   16668 H HB2  . PRO D 1 252 ? 1.323   39.122  37.569  1.00 94.94  ? 252 PRO D HB2  1 
ATOM   16669 H HB3  . PRO D 1 252 ? -0.021  39.151  38.416  1.00 94.94  ? 252 PRO D HB3  1 
ATOM   16670 H HG2  . PRO D 1 252 ? 1.301   41.307  37.581  1.00 99.06  ? 252 PRO D HG2  1 
ATOM   16671 H HG3  . PRO D 1 252 ? 0.077   41.325  38.595  1.00 99.06  ? 252 PRO D HG3  1 
ATOM   16672 H HD2  . PRO D 1 252 ? 2.785   41.553  39.207  1.00 101.50 ? 252 PRO D HD2  1 
ATOM   16673 H HD3  . PRO D 1 252 ? 1.554   42.125  40.034  1.00 101.50 ? 252 PRO D HD3  1 
ATOM   16674 N N    . VAL D 1 253 ? 2.787   36.909  39.007  1.00 82.21  ? 253 VAL D N    1 
ATOM   16675 C CA   . VAL D 1 253 ? 3.859   36.023  38.569  1.00 81.55  ? 253 VAL D CA   1 
ATOM   16676 C C    . VAL D 1 253 ? 3.241   34.989  37.637  1.00 80.44  ? 253 VAL D C    1 
ATOM   16677 O O    . VAL D 1 253 ? 2.290   34.298  38.025  1.00 78.88  ? 253 VAL D O    1 
ATOM   16678 C CB   . VAL D 1 253 ? 4.558   35.322  39.744  1.00 81.00  ? 253 VAL D CB   1 
ATOM   16679 C CG1  . VAL D 1 253 ? 5.923   34.796  39.319  1.00 77.33  ? 253 VAL D CG1  1 
ATOM   16680 C CG2  . VAL D 1 253 ? 4.685   36.266  40.930  1.00 78.48  ? 253 VAL D CG2  1 
ATOM   16681 H H    . VAL D 1 253 ? 2.047   36.494  39.149  1.00 98.65  ? 253 VAL D H    1 
ATOM   16682 H HA   . VAL D 1 253 ? 4.524   36.533  38.081  1.00 97.86  ? 253 VAL D HA   1 
ATOM   16683 H HB   . VAL D 1 253 ? 4.020   34.564  40.022  1.00 97.20  ? 253 VAL D HB   1 
ATOM   16684 H HG11 . VAL D 1 253 ? 6.070   33.930  39.730  1.00 92.79  ? 253 VAL D HG11 1 
ATOM   16685 H HG12 . VAL D 1 253 ? 5.942   34.712  38.353  1.00 92.79  ? 253 VAL D HG12 1 
ATOM   16686 H HG13 . VAL D 1 253 ? 6.606   35.420  39.610  1.00 92.79  ? 253 VAL D HG13 1 
ATOM   16687 H HG21 . VAL D 1 253 ? 5.270   35.865  41.592  1.00 94.17  ? 253 VAL D HG21 1 
ATOM   16688 H HG22 . VAL D 1 253 ? 5.059   37.108  40.625  1.00 94.17  ? 253 VAL D HG22 1 
ATOM   16689 H HG23 . VAL D 1 253 ? 3.806   36.414  41.312  1.00 94.17  ? 253 VAL D HG23 1 
ATOM   16690 N N    . GLU D 1 254 ? 3.773   34.878  36.417  1.00 78.75  ? 254 GLU D N    1 
ATOM   16691 C CA   . GLU D 1 254 ? 3.331   33.883  35.450  1.00 77.15  ? 254 GLU D CA   1 
ATOM   16692 C C    . GLU D 1 254 ? 4.469   32.910  35.175  1.00 76.43  ? 254 GLU D C    1 
ATOM   16693 O O    . GLU D 1 254 ? 5.604   33.333  34.925  1.00 75.48  ? 254 GLU D O    1 
ATOM   16694 C CB   . GLU D 1 254 ? 2.879   34.540  34.140  1.00 81.48  ? 254 GLU D CB   1 
ATOM   16695 C CG   . GLU D 1 254 ? 2.431   33.535  33.082  1.00 84.61  ? 254 GLU D CG   1 
ATOM   16696 C CD   . GLU D 1 254 ? 1.898   34.189  31.815  1.00 88.53  ? 254 GLU D CD   1 
ATOM   16697 O OE1  . GLU D 1 254 ? 2.482   35.201  31.371  1.00 89.89  ? 254 GLU D OE1  1 
ATOM   16698 O OE2  . GLU D 1 254 ? 0.899   33.681  31.257  1.00 87.41  ? 254 GLU D OE2  1 
ATOM   16699 H H    . GLU D 1 254 ? 4.406   35.381  36.125  1.00 94.50  ? 254 GLU D H    1 
ATOM   16700 H HA   . GLU D 1 254 ? 2.582   33.390  35.818  1.00 92.58  ? 254 GLU D HA   1 
ATOM   16701 H HB2  . GLU D 1 254 ? 2.131   35.129  34.327  1.00 97.77  ? 254 GLU D HB2  1 
ATOM   16702 H HB3  . GLU D 1 254 ? 3.618   35.049  33.773  1.00 97.77  ? 254 GLU D HB3  1 
ATOM   16703 H HG2  . GLU D 1 254 ? 3.188   32.981  32.836  1.00 101.53 ? 254 GLU D HG2  1 
ATOM   16704 H HG3  . GLU D 1 254 ? 1.724   32.984  33.453  1.00 101.53 ? 254 GLU D HG3  1 
ATOM   16705 N N    . ILE D 1 255 ? 4.167   31.615  35.219  1.00 76.96  ? 255 ILE D N    1 
ATOM   16706 C CA   . ILE D 1 255 ? 5.129   30.590  34.827  1.00 76.38  ? 255 ILE D CA   1 
ATOM   16707 C C    . ILE D 1 255 ? 5.136   30.516  33.305  1.00 76.29  ? 255 ILE D C    1 
ATOM   16708 O O    . ILE D 1 255 ? 4.106   30.239  32.681  1.00 77.41  ? 255 ILE D O    1 
ATOM   16709 C CB   . ILE D 1 255 ? 4.784   29.229  35.448  1.00 78.72  ? 255 ILE D CB   1 
ATOM   16710 C CG1  . ILE D 1 255 ? 4.616   29.347  36.966  1.00 79.63  ? 255 ILE D CG1  1 
ATOM   16711 C CG2  . ILE D 1 255 ? 5.869   28.200  35.122  1.00 75.67  ? 255 ILE D CG2  1 
ATOM   16712 C CD1  . ILE D 1 255 ? 5.803   29.967  37.680  1.00 75.61  ? 255 ILE D CD1  1 
ATOM   16713 H H    . ILE D 1 255 ? 3.407   31.303  35.473  1.00 92.35  ? 255 ILE D H    1 
ATOM   16714 H HA   . ILE D 1 255 ? 6.015   30.839  35.136  1.00 91.66  ? 255 ILE D HA   1 
ATOM   16715 H HB   . ILE D 1 255 ? 3.943   28.935  35.065  1.00 94.46  ? 255 ILE D HB   1 
ATOM   16716 H HG12 . ILE D 1 255 ? 3.841   29.901  37.150  1.00 95.56  ? 255 ILE D HG12 1 
ATOM   16717 H HG13 . ILE D 1 255 ? 4.484   28.459  37.333  1.00 95.56  ? 255 ILE D HG13 1 
ATOM   16718 H HG21 . ILE D 1 255 ? 5.731   27.412  35.669  1.00 90.81  ? 255 ILE D HG21 1 
ATOM   16719 H HG22 . ILE D 1 255 ? 5.810   27.965  34.182  1.00 90.81  ? 255 ILE D HG22 1 
ATOM   16720 H HG23 . ILE D 1 255 ? 6.738   28.587  35.312  1.00 90.81  ? 255 ILE D HG23 1 
ATOM   16721 H HD11 . ILE D 1 255 ? 5.733   29.780  38.630  1.00 90.73  ? 255 ILE D HD11 1 
ATOM   16722 H HD12 . ILE D 1 255 ? 6.620   29.583  37.327  1.00 90.73  ? 255 ILE D HD12 1 
ATOM   16723 H HD13 . ILE D 1 255 ? 5.796   30.926  37.531  1.00 90.73  ? 255 ILE D HD13 1 
ATOM   16724 N N    . ILE D 1 256 ? 6.297   30.765  32.703  1.00 76.42  ? 256 ILE D N    1 
ATOM   16725 C CA   . ILE D 1 256 ? 6.400   30.887  31.253  1.00 74.97  ? 256 ILE D CA   1 
ATOM   16726 C C    . ILE D 1 256 ? 6.706   29.525  30.639  1.00 77.21  ? 256 ILE D C    1 
ATOM   16727 O O    . ILE D 1 256 ? 5.924   29.007  29.829  1.00 77.77  ? 256 ILE D O    1 
ATOM   16728 C CB   . ILE D 1 256 ? 7.469   31.925  30.863  1.00 76.42  ? 256 ILE D CB   1 
ATOM   16729 C CG1  . ILE D 1 256 ? 6.998   33.350  31.182  1.00 75.89  ? 256 ILE D CG1  1 
ATOM   16730 C CG2  . ILE D 1 256 ? 7.828   31.796  29.387  1.00 73.87  ? 256 ILE D CG2  1 
ATOM   16731 C CD1  . ILE D 1 256 ? 5.607   33.697  30.672  1.00 78.77  ? 256 ILE D CD1  1 
ATOM   16732 H H    . ILE D 1 256 ? 7.044   30.868  33.117  1.00 91.71  ? 256 ILE D H    1 
ATOM   16733 H HA   . ILE D 1 256 ? 5.544   31.181  30.903  1.00 89.97  ? 256 ILE D HA   1 
ATOM   16734 H HB   . ILE D 1 256 ? 8.263   31.747  31.391  1.00 91.70  ? 256 ILE D HB   1 
ATOM   16735 H HG12 . ILE D 1 256 ? 6.991   33.462  32.146  1.00 91.06  ? 256 ILE D HG12 1 
ATOM   16736 H HG13 . ILE D 1 256 ? 7.620   33.976  30.780  1.00 91.06  ? 256 ILE D HG13 1 
ATOM   16737 H HG21 . ILE D 1 256 ? 8.269   32.609  29.097  1.00 88.65  ? 256 ILE D HG21 1 
ATOM   16738 H HG22 . ILE D 1 256 ? 8.422   31.037  29.272  1.00 88.65  ? 256 ILE D HG22 1 
ATOM   16739 H HG23 . ILE D 1 256 ? 7.015   31.660  28.876  1.00 88.65  ? 256 ILE D HG23 1 
ATOM   16740 H HD11 . ILE D 1 256 ? 5.511   34.662  30.650  1.00 94.53  ? 256 ILE D HD11 1 
ATOM   16741 H HD12 . ILE D 1 256 ? 5.497   33.333  29.780  1.00 94.53  ? 256 ILE D HD12 1 
ATOM   16742 H HD13 . ILE D 1 256 ? 4.946   33.313  31.270  1.00 94.53  ? 256 ILE D HD13 1 
ATOM   16743 N N    . ALA D 1 257 ? 7.840   28.933  31.016  1.00 74.52  ? 257 ALA D N    1 
ATOM   16744 C CA   . ALA D 1 257 ? 8.273   27.680  30.406  1.00 73.65  ? 257 ALA D CA   1 
ATOM   16745 C C    . ALA D 1 257 ? 9.184   26.938  31.373  1.00 73.00  ? 257 ALA D C    1 
ATOM   16746 O O    . ALA D 1 257 ? 9.571   27.459  32.421  1.00 73.41  ? 257 ALA D O    1 
ATOM   16747 C CB   . ALA D 1 257 ? 8.989   27.932  29.076  1.00 77.07  ? 257 ALA D CB   1 
ATOM   16748 H H    . ALA D 1 257 ? 8.372   29.237  31.619  1.00 89.43  ? 257 ALA D H    1 
ATOM   16749 H HA   . ALA D 1 257 ? 7.493   27.127  30.245  1.00 88.38  ? 257 ALA D HA   1 
ATOM   16750 H HB1  . ALA D 1 257 ? 9.266   27.082  28.701  1.00 92.48  ? 257 ALA D HB1  1 
ATOM   16751 H HB2  . ALA D 1 257 ? 8.380   28.379  28.469  1.00 92.48  ? 257 ALA D HB2  1 
ATOM   16752 H HB3  . ALA D 1 257 ? 9.766   28.491  29.237  1.00 92.48  ? 257 ALA D HB3  1 
ATOM   16753 N N    . GLU D 1 258 ? 9.525   25.708  30.995  1.00 76.10  ? 258 GLU D N    1 
ATOM   16754 C CA   . GLU D 1 258 ? 10.399  24.873  31.807  1.00 75.17  ? 258 GLU D CA   1 
ATOM   16755 C C    . GLU D 1 258 ? 10.866  23.696  30.968  1.00 73.97  ? 258 GLU D C    1 
ATOM   16756 O O    . GLU D 1 258 ? 10.139  23.217  30.091  1.00 76.95  ? 258 GLU D O    1 
ATOM   16757 C CB   . GLU D 1 258 ? 9.688   24.381  33.075  1.00 72.13  ? 258 GLU D CB   1 
ATOM   16758 C CG   . GLU D 1 258 ? 8.743   23.211  32.853  1.00 75.58  ? 258 GLU D CG   1 
ATOM   16759 C CD   . GLU D 1 258 ? 8.094   22.733  34.146  1.00 77.59  ? 258 GLU D CD   1 
ATOM   16760 O OE1  . GLU D 1 258 ? 8.831   22.335  35.076  1.00 81.47  ? 258 GLU D OE1  1 
ATOM   16761 O OE2  . GLU D 1 258 ? 6.845   22.763  34.233  1.00 76.49  ? 258 GLU D OE2  1 
ATOM   16762 H H    . GLU D 1 258 ? 9.261   25.334  30.267  1.00 91.31  ? 258 GLU D H    1 
ATOM   16763 H HA   . GLU D 1 258 ? 11.179  25.383  32.075  1.00 90.20  ? 258 GLU D HA   1 
ATOM   16764 H HB2  . GLU D 1 258 ? 10.359  24.098  33.716  1.00 86.56  ? 258 GLU D HB2  1 
ATOM   16765 H HB3  . GLU D 1 258 ? 9.168   25.113  33.441  1.00 86.56  ? 258 GLU D HB3  1 
ATOM   16766 H HG2  . GLU D 1 258 ? 8.038   23.484  32.245  1.00 90.70  ? 258 GLU D HG2  1 
ATOM   16767 H HG3  . GLU D 1 258 ? 9.240   22.470  32.474  1.00 90.70  ? 258 GLU D HG3  1 
ATOM   16768 N N    . GLY D 1 259 ? 12.080  23.236  31.252  1.00 71.47  ? 259 GLY D N    1 
ATOM   16769 C CA   . GLY D 1 259 ? 12.636  22.103  30.544  1.00 73.05  ? 259 GLY D CA   1 
ATOM   16770 C C    . GLY D 1 259 ? 14.125  21.963  30.752  1.00 74.43  ? 259 GLY D C    1 
ATOM   16771 O O    . GLY D 1 259 ? 14.591  21.911  31.893  1.00 77.02  ? 259 GLY D O    1 
ATOM   16772 H H    . GLY D 1 259 ? 12.599  23.567  31.853  1.00 85.77  ? 259 GLY D H    1 
ATOM   16773 H HA2  . GLY D 1 259 ? 12.207  21.290  30.853  1.00 87.65  ? 259 GLY D HA2  1 
ATOM   16774 H HA3  . GLY D 1 259 ? 12.469  22.206  29.594  1.00 87.65  ? 259 GLY D HA3  1 
ATOM   16775 N N    . LYS D 1 260 ? 14.882  21.919  29.656  1.00 76.30  ? 260 LYS D N    1 
ATOM   16776 C CA   . LYS D 1 260 ? 16.314  21.672  29.700  1.00 75.41  ? 260 LYS D CA   1 
ATOM   16777 C C    . LYS D 1 260 ? 17.044  22.729  28.892  1.00 74.47  ? 260 LYS D C    1 
ATOM   16778 O O    . LYS D 1 260 ? 16.632  23.062  27.780  1.00 76.04  ? 260 LYS D O    1 
ATOM   16779 C CB   . LYS D 1 260 ? 16.649  20.282  29.146  1.00 74.54  ? 260 LYS D CB   1 
ATOM   16780 C CG   . LYS D 1 260 ? 16.019  19.140  29.923  1.00 78.46  ? 260 LYS D CG   1 
ATOM   16781 C CD   . LYS D 1 260 ? 16.911  18.707  31.068  1.00 77.10  ? 260 LYS D CD   1 
ATOM   16782 C CE   . LYS D 1 260 ? 16.261  17.607  31.897  1.00 81.59  ? 260 LYS D CE   1 
ATOM   16783 N NZ   . LYS D 1 260 ? 14.802  17.835  32.103  1.00 90.28  ? 260 LYS D NZ   1 
ATOM   16784 H H    . LYS D 1 260 ? 14.577  22.032  28.860  1.00 91.56  ? 260 LYS D H    1 
ATOM   16785 H HA   . LYS D 1 260 ? 16.621  21.726  30.619  1.00 90.49  ? 260 LYS D HA   1 
ATOM   16786 H HB2  . LYS D 1 260 ? 16.332  20.227  28.231  1.00 89.45  ? 260 LYS D HB2  1 
ATOM   16787 H HB3  . LYS D 1 260 ? 17.611  20.161  29.171  1.00 89.45  ? 260 LYS D HB3  1 
ATOM   16788 H HG2  . LYS D 1 260 ? 15.169  19.429  30.289  1.00 94.15  ? 260 LYS D HG2  1 
ATOM   16789 H HG3  . LYS D 1 260 ? 15.887  18.382  29.333  1.00 94.15  ? 260 LYS D HG3  1 
ATOM   16790 H HD2  . LYS D 1 260 ? 17.747  18.367  30.713  1.00 92.52  ? 260 LYS D HD2  1 
ATOM   16791 H HD3  . LYS D 1 260 ? 17.081  19.465  31.648  1.00 92.52  ? 260 LYS D HD3  1 
ATOM   16792 H HE2  . LYS D 1 260 ? 16.372  16.758  31.440  1.00 97.91  ? 260 LYS D HE2  1 
ATOM   16793 H HE3  . LYS D 1 260 ? 16.687  17.572  32.768  1.00 97.91  ? 260 LYS D HE3  1 
ATOM   16794 H HZ1  . LYS D 1 260 ? 14.368  17.747  31.331  1.00 108.33 ? 260 LYS D HZ1  1 
ATOM   16795 H HZ2  . LYS D 1 260 ? 14.480  17.243  32.684  1.00 108.33 ? 260 LYS D HZ2  1 
ATOM   16796 H HZ3  . LYS D 1 260 ? 14.664  18.655  32.420  1.00 108.33 ? 260 LYS D HZ3  1 
ATOM   16797 N N    . ILE D 1 261 ? 18.138  23.239  29.444  1.00 72.36  ? 261 ILE D N    1 
ATOM   16798 C CA   . ILE D 1 261 ? 18.993  24.206  28.768  1.00 75.74  ? 261 ILE D CA   1 
ATOM   16799 C C    . ILE D 1 261 ? 20.370  23.579  28.580  1.00 75.43  ? 261 ILE D C    1 
ATOM   16800 O O    . ILE D 1 261 ? 20.863  22.870  29.464  1.00 77.03  ? 261 ILE D O    1 
ATOM   16801 C CB   . ILE D 1 261 ? 19.072  25.530  29.557  1.00 75.74  ? 261 ILE D CB   1 
ATOM   16802 C CG1  . ILE D 1 261 ? 20.099  26.470  28.930  1.00 76.45  ? 261 ILE D CG1  1 
ATOM   16803 C CG2  . ILE D 1 261 ? 19.395  25.275  31.014  1.00 76.52  ? 261 ILE D CG2  1 
ATOM   16804 C CD1  . ILE D 1 261 ? 19.984  27.894  29.417  1.00 83.09  ? 261 ILE D CD1  1 
ATOM   16805 H H    . ILE D 1 261 ? 18.413  23.034  30.232  1.00 86.83  ? 261 ILE D H    1 
ATOM   16806 H HA   . ILE D 1 261 ? 18.638  24.407  27.888  1.00 90.88  ? 261 ILE D HA   1 
ATOM   16807 H HB   . ILE D 1 261 ? 18.201  25.955  29.512  1.00 90.89  ? 261 ILE D HB   1 
ATOM   16808 H HG12 . ILE D 1 261 ? 20.989  26.152  29.148  1.00 91.75  ? 261 ILE D HG12 1 
ATOM   16809 H HG13 . ILE D 1 261 ? 19.975  26.473  27.968  1.00 91.75  ? 261 ILE D HG13 1 
ATOM   16810 H HG21 . ILE D 1 261 ? 19.497  26.126  31.468  1.00 91.83  ? 261 ILE D HG21 1 
ATOM   16811 H HG22 . ILE D 1 261 ? 18.670  24.771  31.415  1.00 91.83  ? 261 ILE D HG22 1 
ATOM   16812 H HG23 . ILE D 1 261 ? 20.221  24.769  31.070  1.00 91.83  ? 261 ILE D HG23 1 
ATOM   16813 H HD11 . ILE D 1 261 ? 20.567  28.458  28.885  1.00 99.70  ? 261 ILE D HD11 1 
ATOM   16814 H HD12 . ILE D 1 261 ? 19.064  28.187  29.323  1.00 99.70  ? 261 ILE D HD12 1 
ATOM   16815 H HD13 . ILE D 1 261 ? 20.249  27.932  30.350  1.00 99.70  ? 261 ILE D HD13 1 
ATOM   16816 N N    . TYR D 1 262 ? 20.975  23.813  27.414  1.00 75.19  ? 262 TYR D N    1 
ATOM   16817 C CA   . TYR D 1 262 ? 22.258  23.219  27.058  1.00 76.24  ? 262 TYR D CA   1 
ATOM   16818 C C    . TYR D 1 262 ? 23.326  24.303  27.029  1.00 80.02  ? 262 TYR D C    1 
ATOM   16819 O O    . TYR D 1 262 ? 23.183  25.304  26.315  1.00 81.83  ? 262 TYR D O    1 
ATOM   16820 C CB   . TYR D 1 262 ? 22.189  22.512  25.701  1.00 73.82  ? 262 TYR D CB   1 
ATOM   16821 C CG   . TYR D 1 262 ? 20.998  21.599  25.555  1.00 72.12  ? 262 TYR D CG   1 
ATOM   16822 C CD1  . TYR D 1 262 ? 21.051  20.280  25.987  1.00 69.83  ? 262 TYR D CD1  1 
ATOM   16823 C CD2  . TYR D 1 262 ? 19.814  22.058  24.987  1.00 74.14  ? 262 TYR D CD2  1 
ATOM   16824 C CE1  . TYR D 1 262 ? 19.957  19.445  25.864  1.00 67.79  ? 262 TYR D CE1  1 
ATOM   16825 C CE2  . TYR D 1 262 ? 18.716  21.228  24.854  1.00 72.26  ? 262 TYR D CE2  1 
ATOM   16826 C CZ   . TYR D 1 262 ? 18.792  19.925  25.297  1.00 71.25  ? 262 TYR D CZ   1 
ATOM   16827 O OH   . TYR D 1 262 ? 17.700  19.097  25.172  1.00 70.66  ? 262 TYR D OH   1 
ATOM   16828 H H    . TYR D 1 262 ? 20.652  24.324  26.802  1.00 90.23  ? 262 TYR D H    1 
ATOM   16829 H HA   . TYR D 1 262 ? 22.497  22.567  27.735  1.00 91.49  ? 262 TYR D HA   1 
ATOM   16830 H HB2  . TYR D 1 262 ? 22.137  23.182  25.002  1.00 88.59  ? 262 TYR D HB2  1 
ATOM   16831 H HB3  . TYR D 1 262 ? 22.989  21.976  25.588  1.00 88.59  ? 262 TYR D HB3  1 
ATOM   16832 H HD1  . TYR D 1 262 ? 21.836  19.954  26.364  1.00 83.80  ? 262 TYR D HD1  1 
ATOM   16833 H HD2  . TYR D 1 262 ? 19.760  22.938  24.692  1.00 88.97  ? 262 TYR D HD2  1 
ATOM   16834 H HE1  . TYR D 1 262 ? 20.004  18.565  26.162  1.00 81.34  ? 262 TYR D HE1  1 
ATOM   16835 H HE2  . TYR D 1 262 ? 17.932  21.547  24.469  1.00 86.72  ? 262 TYR D HE2  1 
ATOM   16836 H HH   . TYR D 1 262 ? 17.074  19.502  24.786  1.00 84.80  ? 262 TYR D HH   1 
ATOM   16837 N N    . ILE D 1 263 ? 24.396  24.097  27.795  1.00 82.55  ? 263 ILE D N    1 
ATOM   16838 C CA   . ILE D 1 263 ? 25.503  25.040  27.879  1.00 88.11  ? 263 ILE D CA   1 
ATOM   16839 C C    . ILE D 1 263 ? 26.795  24.287  27.607  1.00 92.09  ? 263 ILE D C    1 
ATOM   16840 O O    . ILE D 1 263 ? 27.091  23.292  28.278  1.00 92.09  ? 263 ILE D O    1 
ATOM   16841 C CB   . ILE D 1 263 ? 25.574  25.733  29.251  1.00 89.13  ? 263 ILE D CB   1 
ATOM   16842 C CG1  . ILE D 1 263 ? 24.361  26.638  29.447  1.00 86.51  ? 263 ILE D CG1  1 
ATOM   16843 C CG2  . ILE D 1 263 ? 26.875  26.517  29.373  1.00 94.39  ? 263 ILE D CG2  1 
ATOM   16844 C CD1  . ILE D 1 263 ? 23.427  26.158  30.542  1.00 85.74  ? 263 ILE D CD1  1 
ATOM   16845 H H    . ILE D 1 263 ? 24.503  23.400  28.287  1.00 99.06  ? 263 ILE D H    1 
ATOM   16846 H HA   . ILE D 1 263 ? 25.390  25.716  27.193  1.00 105.73 ? 263 ILE D HA   1 
ATOM   16847 H HB   . ILE D 1 263 ? 25.561  25.059  29.949  1.00 106.96 ? 263 ILE D HB   1 
ATOM   16848 H HG12 . ILE D 1 263 ? 24.668  27.527  29.685  1.00 103.82 ? 263 ILE D HG12 1 
ATOM   16849 H HG13 . ILE D 1 263 ? 23.857  26.671  28.619  1.00 103.82 ? 263 ILE D HG13 1 
ATOM   16850 H HG21 . ILE D 1 263 ? 26.794  27.152  30.102  1.00 113.27 ? 263 ILE D HG21 1 
ATOM   16851 H HG22 . ILE D 1 263 ? 27.601  25.898  29.552  1.00 113.27 ? 263 ILE D HG22 1 
ATOM   16852 H HG23 . ILE D 1 263 ? 27.040  26.987  28.541  1.00 113.27 ? 263 ILE D HG23 1 
ATOM   16853 H HD11 . ILE D 1 263 ? 22.689  26.782  30.624  1.00 102.89 ? 263 ILE D HD11 1 
ATOM   16854 H HD12 . ILE D 1 263 ? 23.092  25.278  30.309  1.00 102.89 ? 263 ILE D HD12 1 
ATOM   16855 H HD13 . ILE D 1 263 ? 23.917  26.114  31.378  1.00 102.89 ? 263 ILE D HD13 1 
ATOM   16856 N N    . GLY D 1 264 ? 27.561  24.757  26.628  1.00 107.71 ? 264 GLY D N    1 
ATOM   16857 C CA   . GLY D 1 264 ? 28.875  24.195  26.400  1.00 112.41 ? 264 GLY D CA   1 
ATOM   16858 C C    . GLY D 1 264 ? 29.822  24.530  27.536  1.00 112.11 ? 264 GLY D C    1 
ATOM   16859 O O    . GLY D 1 264 ? 29.658  25.522  28.245  1.00 112.77 ? 264 GLY D O    1 
ATOM   16860 H H    . GLY D 1 264 ? 27.342  25.393  26.091  1.00 129.25 ? 264 GLY D H    1 
ATOM   16861 H HA2  . GLY D 1 264 ? 28.807  23.231  26.326  1.00 134.89 ? 264 GLY D HA2  1 
ATOM   16862 H HA3  . GLY D 1 264 ? 29.242  24.550  25.575  1.00 134.89 ? 264 GLY D HA3  1 
ATOM   16863 N N    . LYS D 1 265 ? 30.824  23.678  27.717  1.00 116.43 ? 265 LYS D N    1 
ATOM   16864 C CA   . LYS D 1 265 ? 31.816  23.897  28.766  1.00 126.57 ? 265 LYS D CA   1 
ATOM   16865 C C    . LYS D 1 265 ? 33.009  24.663  28.202  1.00 129.96 ? 265 LYS D C    1 
ATOM   16866 O O    . LYS D 1 265 ? 33.407  24.458  27.054  1.00 127.56 ? 265 LYS D O    1 
ATOM   16867 C CB   . LYS D 1 265 ? 32.267  22.570  29.376  1.00 125.19 ? 265 LYS D CB   1 
ATOM   16868 C CG   . LYS D 1 265 ? 33.450  22.681  30.342  1.00 129.93 ? 265 LYS D CG   1 
ATOM   16869 C CD   . LYS D 1 265 ? 33.200  23.684  31.463  1.00 129.97 ? 265 LYS D CD   1 
ATOM   16870 C CE   . LYS D 1 265 ? 34.514  24.147  32.096  1.00 129.71 ? 265 LYS D CE   1 
ATOM   16871 N NZ   . LYS D 1 265 ? 35.340  24.965  31.159  1.00 126.36 ? 265 LYS D NZ   1 
ATOM   16872 H H    . LYS D 1 265 ? 30.952  22.968  27.248  1.00 139.71 ? 265 LYS D H    1 
ATOM   16873 H HA   . LYS D 1 265 ? 31.424  24.420  29.483  1.00 151.88 ? 265 LYS D HA   1 
ATOM   16874 H HB2  . LYS D 1 265 ? 31.523  22.187  29.867  1.00 150.23 ? 265 LYS D HB2  1 
ATOM   16875 H HB3  . LYS D 1 265 ? 32.532  21.974  28.657  1.00 150.23 ? 265 LYS D HB3  1 
ATOM   16876 H HG2  . LYS D 1 265 ? 33.611  21.814  30.746  1.00 155.91 ? 265 LYS D HG2  1 
ATOM   16877 H HG3  . LYS D 1 265 ? 34.235  22.969  29.850  1.00 155.91 ? 265 LYS D HG3  1 
ATOM   16878 H HD2  . LYS D 1 265 ? 32.744  24.461  31.104  1.00 155.96 ? 265 LYS D HD2  1 
ATOM   16879 H HD3  . LYS D 1 265 ? 32.658  23.270  32.152  1.00 155.96 ? 265 LYS D HD3  1 
ATOM   16880 H HE2  . LYS D 1 265 ? 34.317  24.689  32.876  1.00 155.65 ? 265 LYS D HE2  1 
ATOM   16881 H HE3  . LYS D 1 265 ? 35.033  23.369  32.354  1.00 155.65 ? 265 LYS D HE3  1 
ATOM   16882 H HZ1  . LYS D 1 265 ? 35.591  24.470  30.463  1.00 151.63 ? 265 LYS D HZ1  1 
ATOM   16883 H HZ2  . LYS D 1 265 ? 34.868  25.659  30.864  1.00 151.63 ? 265 LYS D HZ2  1 
ATOM   16884 H HZ3  . LYS D 1 265 ? 36.066  25.265  31.577  1.00 151.63 ? 265 LYS D HZ3  1 
HETATM 16885 S S    . SO4 E 2 .   ? 15.991  -1.335  62.037  1.00 82.18  ? 301 SO4 A S    1 
HETATM 16886 O O1   . SO4 E 2 .   ? 16.952  -0.395  61.466  1.00 75.46  ? 301 SO4 A O1   1 
HETATM 16887 O O2   . SO4 E 2 .   ? 14.735  -1.282  61.289  1.00 78.20  ? 301 SO4 A O2   1 
HETATM 16888 O O3   . SO4 E 2 .   ? 16.527  -2.692  61.976  1.00 78.85  ? 301 SO4 A O3   1 
HETATM 16889 O O4   . SO4 E 2 .   ? 15.751  -0.973  63.428  1.00 77.30  ? 301 SO4 A O4   1 
HETATM 16890 S S    . SO4 F 2 .   ? 10.029  -19.358 57.090  1.00 124.30 ? 302 SO4 A S    1 
HETATM 16891 O O1   . SO4 F 2 .   ? 11.164  -19.267 56.175  1.00 119.70 ? 302 SO4 A O1   1 
HETATM 16892 O O2   . SO4 F 2 .   ? 8.788   -19.082 56.372  1.00 120.88 ? 302 SO4 A O2   1 
HETATM 16893 O O3   . SO4 F 2 .   ? 9.972   -20.710 57.648  1.00 119.06 ? 302 SO4 A O3   1 
HETATM 16894 O O4   . SO4 F 2 .   ? 10.188  -18.375 58.158  1.00 118.77 ? 302 SO4 A O4   1 
HETATM 16895 S S    . SO4 G 2 .   ? 15.970  35.284  7.258   1.00 85.66  ? 301 SO4 B S    1 
HETATM 16896 O O1   . SO4 G 2 .   ? 17.052  35.638  6.340   1.00 83.26  ? 301 SO4 B O1   1 
HETATM 16897 O O2   . SO4 G 2 .   ? 14.693  35.596  6.615   1.00 86.06  ? 301 SO4 B O2   1 
HETATM 16898 O O3   . SO4 G 2 .   ? 16.040  33.853  7.542   1.00 77.83  ? 301 SO4 B O3   1 
HETATM 16899 O O4   . SO4 G 2 .   ? 16.091  36.038  8.503   1.00 81.39  ? 301 SO4 B O4   1 
HETATM 16900 S S    . SO4 H 2 .   ? 9.531   52.632  11.766  1.00 126.44 ? 302 SO4 B S    1 
HETATM 16901 O O1   . SO4 H 2 .   ? 10.587  52.284  10.817  1.00 120.39 ? 302 SO4 B O1   1 
HETATM 16902 O O2   . SO4 H 2 .   ? 8.254   52.713  11.059  1.00 124.86 ? 302 SO4 B O2   1 
HETATM 16903 O O3   . SO4 H 2 .   ? 9.449   51.602  12.800  1.00 122.78 ? 302 SO4 B O3   1 
HETATM 16904 O O4   . SO4 H 2 .   ? 9.834   53.923  12.380  1.00 120.52 ? 302 SO4 B O4   1 
HETATM 16905 S S    . SO4 I 2 .   ? 14.104  -9.520  25.554  1.00 93.00  ? 301 SO4 C S    1 
HETATM 16906 O O1   . SO4 I 2 .   ? 15.448  -9.980  25.185  1.00 84.21  ? 301 SO4 C O1   1 
HETATM 16907 O O2   . SO4 I 2 .   ? 13.296  -9.480  24.331  1.00 86.63  ? 301 SO4 C O2   1 
HETATM 16908 O O3   . SO4 I 2 .   ? 13.491  -10.431 26.517  1.00 92.00  ? 301 SO4 C O3   1 
HETATM 16909 O O4   . SO4 I 2 .   ? 14.172  -8.192  26.170  1.00 76.96  ? 301 SO4 C O4   1 
HETATM 16910 S S    . SO4 J 2 .   ? 23.164  -22.765 37.185  1.00 112.45 ? 302 SO4 C S    1 
HETATM 16911 O O1   . SO4 J 2 .   ? 24.475  -22.550 36.575  1.00 110.85 ? 302 SO4 C O1   1 
HETATM 16912 O O2   . SO4 J 2 .   ? 22.148  -22.869 36.146  1.00 115.68 ? 302 SO4 C O2   1 
HETATM 16913 O O3   . SO4 J 2 .   ? 23.180  -24.005 37.957  1.00 113.90 ? 302 SO4 C O3   1 
HETATM 16914 O O4   . SO4 J 2 .   ? 22.838  -21.634 38.051  1.00 111.81 ? 302 SO4 C O4   1 
HETATM 16915 S S    . SO4 K 2 .   ? 14.161  43.179  43.559  1.00 91.32  ? 301 SO4 D S    1 
HETATM 16916 O O1   . SO4 K 2 .   ? 14.938  42.268  42.706  1.00 80.45  ? 301 SO4 D O1   1 
HETATM 16917 O O2   . SO4 K 2 .   ? 12.915  43.507  42.862  1.00 88.00  ? 301 SO4 D O2   1 
HETATM 16918 O O3   . SO4 K 2 .   ? 13.850  42.538  44.836  1.00 87.36  ? 301 SO4 D O3   1 
HETATM 16919 O O4   . SO4 K 2 .   ? 14.927  44.396  43.840  1.00 86.02  ? 301 SO4 D O4   1 
HETATM 16920 S S    . SO4 L 2 .   ? 22.659  56.812  31.703  1.00 119.44 ? 302 SO4 D S    1 
HETATM 16921 O O1   . SO4 L 2 .   ? 23.610  56.860  30.595  1.00 125.17 ? 302 SO4 D O1   1 
HETATM 16922 O O2   . SO4 L 2 .   ? 21.320  56.531  31.188  1.00 117.19 ? 302 SO4 D O2   1 
HETATM 16923 O O3   . SO4 L 2 .   ? 23.058  55.752  32.624  1.00 114.62 ? 302 SO4 D O3   1 
HETATM 16924 O O4   . SO4 L 2 .   ? 22.658  58.104  32.383  1.00 119.35 ? 302 SO4 D O4   1 
HETATM 16925 O O    . HOH M 3 .   ? 25.593  2.928   56.444  1.00 40.50  ? 401 HOH A O    1 
HETATM 16926 O O    . HOH M 3 .   ? 28.159  -5.530  71.305  1.00 40.50  ? 402 HOH A O    1 
HETATM 16927 O O    . HOH M 3 .   ? 7.114   11.043  43.843  1.00 40.50  ? 403 HOH A O    1 
HETATM 16928 O O    . HOH M 3 .   ? 21.828  5.793   71.051  1.00 40.50  ? 404 HOH A O    1 
HETATM 16929 O O    . HOH M 3 .   ? 25.708  -19.252 77.435  1.00 40.50  ? 405 HOH A O    1 
HETATM 16930 O O    . HOH M 3 .   ? 22.353  10.933  50.083  1.00 40.50  ? 406 HOH A O    1 
HETATM 16931 O O    . HOH M 3 .   ? 10.031  -2.643  51.082  1.00 40.50  ? 407 HOH A O    1 
HETATM 16932 O O    . HOH M 3 .   ? 25.218  -4.313  49.707  1.00 40.50  ? 408 HOH A O    1 
HETATM 16933 O O    . HOH M 3 .   ? 32.091  -0.412  56.708  1.00 40.50  ? 409 HOH A O    1 
HETATM 16934 O O    . HOH M 3 .   ? -5.147  12.160  55.318  1.00 40.50  ? 410 HOH A O    1 
HETATM 16935 O O    . HOH M 3 .   ? 29.067  13.458  67.060  1.00 40.50  ? 411 HOH A O    1 
HETATM 16936 O O    . HOH M 3 .   ? 5.375   4.999   66.672  1.00 40.50  ? 412 HOH A O    1 
HETATM 16937 O O    . HOH M 3 .   ? 19.148  -12.285 70.258  1.00 40.50  ? 413 HOH A O    1 
HETATM 16938 O O    . HOH M 3 .   ? 19.292  -11.008 56.511  1.00 40.50  ? 414 HOH A O    1 
HETATM 16939 O O    . HOH M 3 .   ? 11.226  3.997   70.282  1.00 40.50  ? 415 HOH A O    1 
HETATM 16940 O O    . HOH M 3 .   ? 23.465  18.701  52.221  1.00 40.50  ? 416 HOH A O    1 
HETATM 16941 O O    . HOH M 3 .   ? 33.563  -16.948 73.420  1.00 40.50  ? 417 HOH A O    1 
HETATM 16942 O O    . HOH M 3 .   ? 31.001  -17.385 65.693  1.00 40.50  ? 418 HOH A O    1 
HETATM 16943 O O    . HOH M 3 .   ? 29.252  8.736   71.240  1.00 40.50  ? 419 HOH A O    1 
HETATM 16944 O O    . HOH M 3 .   ? 3.228   12.529  47.812  1.00 40.50  ? 420 HOH A O    1 
HETATM 16945 O O    . HOH M 3 .   ? -1.747  -4.360  42.807  1.00 40.50  ? 421 HOH A O    1 
HETATM 16946 O O    . HOH M 3 .   ? 3.343   18.843  52.668  1.00 40.50  ? 422 HOH A O    1 
HETATM 16947 O O    . HOH M 3 .   ? 20.015  8.294   74.410  1.00 40.50  ? 423 HOH A O    1 
HETATM 16948 O O    . HOH M 3 .   ? 5.966   18.097  40.567  1.00 40.50  ? 424 HOH A O    1 
HETATM 16949 O O    . HOH M 3 .   ? 30.536  8.172   69.893  1.00 40.50  ? 425 HOH A O    1 
HETATM 16950 O O    . HOH M 3 .   ? -5.040  14.853  56.204  1.00 40.50  ? 426 HOH A O    1 
HETATM 16951 O O    . HOH M 3 .   ? 34.638  -0.486  56.697  1.00 40.50  ? 427 HOH A O    1 
HETATM 16952 O O    . HOH M 3 .   ? 3.277   15.722  34.343  1.00 40.50  ? 428 HOH A O    1 
HETATM 16953 O O    . HOH N 3 .   ? 21.010  49.198  5.185   1.00 40.50  ? 401 HOH B O    1 
HETATM 16954 O O    . HOH N 3 .   ? 28.759  23.227  16.136  1.00 40.50  ? 402 HOH B O    1 
HETATM 16955 O O    . HOH N 3 .   ? 21.056  39.718  19.139  1.00 40.50  ? 403 HOH B O    1 
HETATM 16956 O O    . HOH N 3 .   ? 14.462  28.715  -3.634  1.00 40.50  ? 404 HOH B O    1 
HETATM 16957 O O    . HOH N 3 .   ? 25.306  31.000  12.509  1.00 40.50  ? 405 HOH B O    1 
HETATM 16958 O O    . HOH N 3 .   ? 25.682  49.717  -9.246  1.00 40.50  ? 406 HOH B O    1 
HETATM 16959 O O    . HOH N 3 .   ? -5.037  21.406  13.799  1.00 40.50  ? 407 HOH B O    1 
HETATM 16960 O O    . HOH N 3 .   ? 13.392  48.644  -10.607 1.00 40.50  ? 408 HOH B O    1 
HETATM 16961 O O    . HOH N 3 .   ? 16.252  33.957  5.110   1.00 40.50  ? 409 HOH B O    1 
HETATM 16962 O O    . HOH N 3 .   ? 22.412  24.922  -7.408  1.00 40.50  ? 410 HOH B O    1 
HETATM 16963 O O    . HOH N 3 .   ? 18.519  9.752   15.142  1.00 40.50  ? 411 HOH B O    1 
HETATM 16964 O O    . HOH N 3 .   ? 12.336  35.397  6.034   1.00 40.50  ? 412 HOH B O    1 
HETATM 16965 O O    . HOH N 3 .   ? 15.052  54.345  -10.354 1.00 40.50  ? 413 HOH B O    1 
HETATM 16966 O O    . HOH N 3 .   ? 23.704  21.803  -0.100  1.00 40.50  ? 414 HOH B O    1 
HETATM 16967 O O    . HOH N 3 .   ? 18.422  11.511  8.000   1.00 40.50  ? 415 HOH B O    1 
HETATM 16968 O O    . HOH N 3 .   ? 29.015  40.742  16.717  1.00 40.50  ? 416 HOH B O    1 
HETATM 16969 O O    . HOH N 3 .   ? 28.034  48.381  -8.935  1.00 40.50  ? 417 HOH B O    1 
HETATM 16970 O O    . HOH N 3 .   ? -5.647  18.485  12.985  1.00 40.50  ? 418 HOH B O    1 
HETATM 16971 O O    . HOH N 3 .   ? 3.387   18.617  34.926  1.00 40.50  ? 419 HOH B O    1 
HETATM 16972 O O    . HOH O 3 .   ? 11.977  -9.294  26.641  1.00 40.50  ? 401 HOH C O    1 
HETATM 16973 O O    . HOH O 3 .   ? 21.711  -3.272  20.391  1.00 40.50  ? 402 HOH C O    1 
HETATM 16974 O O    . HOH O 3 .   ? 3.553   -28.563 28.245  1.00 40.50  ? 403 HOH C O    1 
HETATM 16975 O O    . HOH O 3 .   ? 7.776   -11.949 35.133  1.00 40.50  ? 404 HOH C O    1 
HETATM 16976 O O    . HOH O 3 .   ? 19.155  9.491   28.230  1.00 40.50  ? 405 HOH C O    1 
HETATM 16977 O O    . HOH O 3 .   ? 20.732  -21.715 38.099  1.00 40.50  ? 406 HOH C O    1 
HETATM 16978 O O    . HOH O 3 .   ? -5.560  7.277   21.685  1.00 40.50  ? 407 HOH C O    1 
HETATM 16979 O O    . HOH O 3 .   ? 20.762  -24.283 38.017  1.00 40.50  ? 408 HOH C O    1 
HETATM 16980 O O    . HOH O 3 .   ? 20.402  -3.371  31.386  1.00 40.50  ? 409 HOH C O    1 
HETATM 16981 O O    . HOH O 3 .   ? 5.315   11.146  23.518  1.00 40.50  ? 410 HOH C O    1 
HETATM 16982 O O    . HOH O 3 .   ? 3.003   -14.264 37.052  1.00 40.50  ? 411 HOH C O    1 
HETATM 16983 O O    . HOH O 3 .   ? 20.587  12.596  32.631  1.00 40.50  ? 412 HOH C O    1 
HETATM 16984 O O    . HOH P 3 .   ? 4.057   39.162  43.284  1.00 40.50  ? 401 HOH D O    1 
HETATM 16985 O O    . HOH P 3 .   ? 21.206  47.425  48.896  1.00 40.50  ? 402 HOH D O    1 
HETATM 16986 O O    . HOH P 3 .   ? 22.814  32.219  36.281  1.00 40.50  ? 403 HOH D O    1 
HETATM 16987 O O    . HOH P 3 .   ? 20.067  36.950  37.945  1.00 40.50  ? 404 HOH D O    1 
HETATM 16988 O O    . HOH P 3 .   ? 30.513  50.518  33.775  1.00 40.50  ? 405 HOH D O    1 
HETATM 16989 O O    . HOH P 3 .   ? 13.225  41.062  42.265  1.00 40.50  ? 406 HOH D O    1 
HETATM 16990 O O    . HOH P 3 .   ? 12.558  22.446  38.395  1.00 40.50  ? 407 HOH D O    1 
HETATM 16991 O O    . HOH P 3 .   ? -3.466  41.750  52.629  1.00 40.50  ? 408 HOH D O    1 
HETATM 16992 O O    . HOH P 3 .   ? 3.002   48.202  32.475  1.00 40.50  ? 409 HOH D O    1 
HETATM 16993 O O    . HOH P 3 .   ? -0.891  24.084  41.180  1.00 40.50  ? 410 HOH D O    1 
HETATM 16994 O O    . HOH P 3 .   ? 23.089  35.382  52.813  1.00 40.50  ? 411 HOH D O    1 
HETATM 16995 O O    . HOH P 3 .   ? 15.787  20.177  45.765  1.00 40.50  ? 412 HOH D O    1 
HETATM 16996 O O    . HOH P 3 .   ? 13.674  21.108  44.177  1.00 40.50  ? 413 HOH D O    1 
HETATM 16997 O O    . HOH P 3 .   ? -4.332  39.747  50.854  1.00 40.50  ? 414 HOH D O    1 
HETATM 16998 O O    . HOH P 3 .   ? 2.796   21.422  53.612  1.00 40.50  ? 415 HOH D O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ARG A 3   ? 1.2729 1.6400 1.7575 -0.1331 -0.3678 0.1069  3   ARG A N   
2     C CA  . ARG A 3   ? 1.2903 1.7166 1.8154 -0.1261 -0.3313 0.1133  3   ARG A CA  
3     C C   . ARG A 3   ? 1.2776 1.6980 1.7718 -0.0986 -0.2992 0.0972  3   ARG A C   
4     O O   . ARG A 3   ? 1.3290 1.6993 1.7707 -0.0867 -0.3037 0.0818  3   ARG A O   
5     C CB  . ARG A 3   ? 1.2988 1.7201 1.8213 -0.1433 -0.3217 0.1187  3   ARG A CB  
6     C CG  . ARG A 3   ? 1.3066 1.7566 1.8796 -0.1713 -0.3448 0.1399  3   ARG A CG  
7     C CD  . ARG A 3   ? 1.3113 1.8440 1.9645 -0.1702 -0.3384 0.1587  3   ARG A CD  
8     N NE  . ARG A 3   ? 1.3273 1.8997 1.9924 -0.1454 -0.2984 0.1544  3   ARG A NE  
9     C CZ  . ARG A 3   ? 1.2728 1.8960 1.9761 -0.1452 -0.2701 0.1659  3   ARG A CZ  
10    N NH1 . ARG A 3   ? 1.2542 1.8991 1.9914 -0.1691 -0.2751 0.1834  3   ARG A NH1 
11    N NH2 . ARG A 3   ? 1.2200 1.8698 1.9248 -0.1206 -0.2365 0.1600  3   ARG A NH2 
25    N N   . LYS A 4   ? 1.2240 1.6939 1.7495 -0.0890 -0.2671 0.1015  4   LYS A N   
26    C CA  . LYS A 4   ? 1.2011 1.6693 1.7023 -0.0643 -0.2376 0.0881  4   LYS A CA  
27    C C   . LYS A 4   ? 1.1851 1.6142 1.6384 -0.0638 -0.2186 0.0764  4   LYS A C   
28    O O   . LYS A 4   ? 1.1827 1.6209 1.6460 -0.0766 -0.2106 0.0830  4   LYS A O   
29    C CB  . LYS A 4   ? 1.1882 1.7234 1.7404 -0.0520 -0.2126 0.0979  4   LYS A CB  
30    C CG  . LYS A 4   ? 1.1714 1.7636 1.7908 -0.0593 -0.2270 0.1177  4   LYS A CG  
31    C CD  . LYS A 4   ? 1.1619 1.7488 1.7848 -0.0510 -0.2515 0.1157  4   LYS A CD  
32    C CE  . LYS A 4   ? 1.1196 1.7664 1.8147 -0.0596 -0.2682 0.1371  4   LYS A CE  
33    N NZ  . LYS A 4   ? 1.0519 1.7674 1.7994 -0.0495 -0.2377 0.1504  4   LYS A NZ  
47    N N   . VAL A 5   ? 1.1526 1.5394 1.5556 -0.0489 -0.2113 0.0598  5   VAL A N   
48    C CA  . VAL A 5   ? 1.0979 1.4523 1.4587 -0.0449 -0.1911 0.0487  5   VAL A CA  
49    C C   . VAL A 5   ? 1.0355 1.4209 1.4063 -0.0277 -0.1601 0.0452  5   VAL A C   
50    O O   . VAL A 5   ? 1.0238 1.4156 1.3931 -0.0114 -0.1553 0.0400  5   VAL A O   
51    C CB  . VAL A 5   ? 1.0972 1.3875 1.3977 -0.0391 -0.1999 0.0344  5   VAL A CB  
52    C CG1 . VAL A 5   ? 1.0295 1.2864 1.2924 -0.0409 -0.1852 0.0271  5   VAL A CG1 
53    C CG2 . VAL A 5   ? 1.0968 1.3571 1.3871 -0.0505 -0.2349 0.0373  5   VAL A CG2 
63    N N   . GLN A 6   ? 1.0326 1.4334 1.4103 -0.0312 -0.1404 0.0479  6   GLN A N   
64    C CA  . GLN A 6   ? 0.9635 1.3875 1.3450 -0.0159 -0.1124 0.0443  6   GLN A CA  
65    C C   . GLN A 6   ? 0.9062 1.2884 1.2394 -0.0081 -0.1001 0.0297  6   GLN A C   
66    O O   . GLN A 6   ? 0.9058 1.2595 1.2156 -0.0173 -0.1011 0.0271  6   GLN A O   
67    C CB  . GLN A 6   ? 0.9931 1.4562 1.4074 -0.0229 -0.0977 0.0560  6   GLN A CB  
68    C CG  . GLN A 6   ? 0.9437 1.4386 1.3699 -0.0058 -0.0720 0.0557  6   GLN A CG  
69    C CD  . GLN A 6   ? 1.0046 1.5423 1.4672 -0.0117 -0.0588 0.0700  6   GLN A CD  
70    O OE1 . GLN A 6   ? 1.0430 1.5784 1.5119 -0.0293 -0.0640 0.0774  6   GLN A OE1 
71    N NE2 . GLN A 6   ? 0.9950 1.5696 1.4790 0.0039  -0.0410 0.0744  6   GLN A NE2 
80    N N   . VAL A 7   ? 0.8460 1.2249 1.1651 0.0088  -0.0889 0.0211  7   VAL A N   
81    C CA  . VAL A 7   ? 0.8330 1.1765 1.1112 0.0163  -0.0772 0.0087  7   VAL A CA  
82    C C   . VAL A 7   ? 0.8238 1.1884 1.1080 0.0238  -0.0539 0.0078  7   VAL A C   
83    O O   . VAL A 7   ? 0.8223 1.2135 1.1229 0.0354  -0.0449 0.0092  7   VAL A O   
84    C CB  . VAL A 7   ? 0.8642 1.1829 1.1181 0.0283  -0.0826 0.0000  7   VAL A CB  
85    C CG1 . VAL A 7   ? 0.8819 1.1644 1.0960 0.0335  -0.0708 -0.0106 7   VAL A CG1 
86    C CG2 . VAL A 7   ? 0.8466 1.1455 1.0951 0.0220  -0.1077 0.0018  7   VAL A CG2 
96    N N   . LEU A 8   ? 0.7884 1.1385 1.0568 0.0183  -0.0448 0.0053  8   LEU A N   
97    C CA  . LEU A 8   ? 0.7299 1.0941 0.9995 0.0239  -0.0253 0.0042  8   LEU A CA  
98    C C   . LEU A 8   ? 0.7581 1.0918 0.9947 0.0301  -0.0170 -0.0066 8   LEU A C   
99    O O   . LEU A 8   ? 0.7988 1.1003 1.0117 0.0272  -0.0237 -0.0114 8   LEU A O   
100   C CB  . LEU A 8   ? 0.7633 1.1396 1.0453 0.0122  -0.0215 0.0117  8   LEU A CB  
101   C CG  . LEU A 8   ? 0.7662 1.1595 1.0750 -0.0016 -0.0348 0.0234  8   LEU A CG  
102   C CD1 . LEU A 8   ? 0.7520 1.1525 1.0674 -0.0126 -0.0287 0.0302  8   LEU A CD1 
103   C CD2 . LEU A 8   ? 0.8042 1.2372 1.1484 0.0037  -0.0353 0.0317  8   LEU A CD2 
115   N N   . ASP A 9   ? 0.7253 1.0683 0.9599 0.0388  -0.0026 -0.0095 9   ASP A N   
116   C CA  . ASP A 9   ? 0.7246 1.0437 0.9337 0.0429  0.0052  -0.0177 9   ASP A CA  
117   C C   . ASP A 9   ? 0.7126 1.0306 0.9197 0.0359  0.0119  -0.0161 9   ASP A C   
118   O O   . ASP A 9   ? 0.7608 1.1001 0.9813 0.0354  0.0190  -0.0114 9   ASP A O   
119   C CB  . ASP A 9   ? 0.7540 1.0789 0.9589 0.0555  0.0136  -0.0218 9   ASP A CB  
120   C CG  . ASP A 9   ? 0.8246 1.1491 1.0299 0.0642  0.0067  -0.0234 9   ASP A CG  
121   O OD1 . ASP A 9   ? 0.8068 1.1579 1.0335 0.0693  0.0059  -0.0180 9   ASP A OD1 
122   O OD2 . ASP A 9   ? 0.8883 1.1863 1.0728 0.0664  0.0025  -0.0293 9   ASP A OD2 
127   N N   . PHE A 10  ? 0.6912 0.9835 0.8801 0.0316  0.0104  -0.0194 10  PHE A N   
128   C CA  . PHE A 10  ? 0.7218 1.0102 0.9077 0.0256  0.0149  -0.0177 10  PHE A CA  
129   C C   . PHE A 10  ? 0.7075 0.9808 0.8779 0.0298  0.0229  -0.0231 10  PHE A C   
130   O O   . PHE A 10  ? 0.6781 0.9364 0.8362 0.0346  0.0233  -0.0277 10  PHE A O   
131   C CB  . PHE A 10  ? 0.7391 1.0106 0.9186 0.0168  0.0053  -0.0148 10  PHE A CB  
132   C CG  . PHE A 10  ? 0.7857 1.0245 0.9397 0.0193  0.0045  -0.0199 10  PHE A CG  
133   C CD1 . PHE A 10  ? 0.7737 1.0011 0.9170 0.0200  0.0121  -0.0211 10  PHE A CD1 
134   C CD2 . PHE A 10  ? 0.7934 1.0130 0.9336 0.0220  -0.0034 -0.0228 10  PHE A CD2 
135   C CE1 . PHE A 10  ? 0.7919 0.9918 0.9132 0.0241  0.0141  -0.0242 10  PHE A CE1 
136   C CE2 . PHE A 10  ? 0.8101 0.9983 0.9240 0.0257  -0.0017 -0.0265 10  PHE A CE2 
137   C CZ  . PHE A 10  ? 0.8352 1.0149 0.9407 0.0271  0.0081  -0.0269 10  PHE A CZ  
147   N N   . ILE A 11  ? 0.7801 1.0582 0.9525 0.0276  0.0288  -0.0215 11  ILE A N   
148   C CA  . ILE A 11  ? 0.7513 1.0171 0.9137 0.0293  0.0344  -0.0244 11  ILE A CA  
149   C C   . ILE A 11  ? 0.7439 1.0062 0.9057 0.0242  0.0347  -0.0209 11  ILE A C   
150   O O   . ILE A 11  ? 0.7467 1.0227 0.9173 0.0208  0.0351  -0.0170 11  ILE A O   
151   C CB  . ILE A 11  ? 0.7127 0.9873 0.8770 0.0337  0.0400  -0.0267 11  ILE A CB  
152   C CG1 . ILE A 11  ? 0.7187 0.9964 0.8819 0.0397  0.0390  -0.0298 11  ILE A CG1 
153   C CG2 . ILE A 11  ? 0.7207 0.9835 0.8786 0.0341  0.0435  -0.0286 11  ILE A CG2 
154   C CD1 . ILE A 11  ? 0.7128 1.0109 0.8863 0.0428  0.0400  -0.0271 11  ILE A CD1 
166   N N   . LYS A 12  ? 0.7450 0.9880 0.8949 0.0248  0.0352  -0.0217 12  LYS A N   
167   C CA  . LYS A 12  ? 0.7376 0.9731 0.8833 0.0223  0.0355  -0.0187 12  LYS A CA  
168   C C   . LYS A 12  ? 0.7707 1.0089 0.9186 0.0262  0.0427  -0.0193 12  LYS A C   
169   O O   . LYS A 12  ? 0.7953 1.0290 0.9412 0.0304  0.0471  -0.0213 12  LYS A O   
170   C CB  . LYS A 12  ? 0.7880 0.9977 0.9162 0.0227  0.0313  -0.0187 12  LYS A CB  
171   C CG  . LYS A 12  ? 0.8054 1.0043 0.9264 0.0196  0.0287  -0.0153 12  LYS A CG  
172   C CD  . LYS A 12  ? 0.8528 1.0233 0.9535 0.0180  0.0199  -0.0151 12  LYS A CD  
173   C CE  . LYS A 12  ? 0.8401 0.9885 0.9234 0.0206  0.0205  -0.0134 12  LYS A CE  
174   N NZ  . LYS A 12  ? 0.8927 1.0198 0.9619 0.0130  0.0073  -0.0108 12  LYS A NZ  
188   N N   . ILE A 13  ? 0.7629 1.0085 0.9156 0.0242  0.0433  -0.0165 13  ILE A N   
189   C CA  . ILE A 13  ? 0.7496 1.0009 0.9074 0.0270  0.0473  -0.0162 13  ILE A CA  
190   C C   . ILE A 13  ? 0.7504 0.9954 0.9045 0.0268  0.0468  -0.0127 13  ILE A C   
191   O O   . ILE A 13  ? 0.7635 1.0056 0.9135 0.0224  0.0430  -0.0102 13  ILE A O   
192   C CB  . ILE A 13  ? 0.7431 1.0100 0.9083 0.0262  0.0470  -0.0172 13  ILE A CB  
193   C CG1 . ILE A 13  ? 0.7406 1.0118 0.9063 0.0272  0.0466  -0.0202 13  ILE A CG1 
194   C CG2 . ILE A 13  ? 0.7371 1.0066 0.9071 0.0284  0.0480  -0.0175 13  ILE A CG2 
195   C CD1 . ILE A 13  ? 0.7373 1.0200 0.9048 0.0288  0.0469  -0.0212 13  ILE A CD1 
207   N N   . ASN A 14  ? 0.7674 1.0105 0.9239 0.0317  0.0503  -0.0117 14  ASN A N   
208   C CA  . ASN A 14  ? 0.7660 1.0032 0.9190 0.0340  0.0499  -0.0084 14  ASN A CA  
209   C C   . ASN A 14  ? 0.7630 1.0139 0.9265 0.0339  0.0484  -0.0071 14  ASN A C   
210   O O   . ASN A 14  ? 0.7576 1.0143 0.9312 0.0380  0.0502  -0.0058 14  ASN A O   
211   C CB  . ASN A 14  ? 0.7970 1.0215 0.9445 0.0421  0.0553  -0.0070 14  ASN A CB  
212   C CG  . ASN A 14  ? 0.8065 1.0247 0.9503 0.0471  0.0552  -0.0035 14  ASN A CG  
213   O OD1 . ASN A 14  ? 0.8036 1.0159 0.9395 0.0432  0.0499  -0.0024 14  ASN A OD1 
214   N ND2 . ASN A 14  ? 0.8215 1.0413 0.9716 0.0561  0.0616  -0.0008 14  ASN A ND2 
221   N N   . PRO A 15  ? 0.7874 1.0436 0.9490 0.0294  0.0448  -0.0065 15  PRO A N   
222   C CA  . PRO A 15  ? 0.7537 1.0165 0.9188 0.0302  0.0419  -0.0051 15  PRO A CA  
223   C C   . PRO A 15  ? 0.7699 1.0240 0.9299 0.0331  0.0403  -0.0013 15  PRO A C   
224   O O   . PRO A 15  ? 0.8039 1.0507 0.9535 0.0300  0.0385  0.0010  15  PRO A O   
225   C CB  . PRO A 15  ? 0.7835 1.0517 0.9435 0.0259  0.0409  -0.0053 15  PRO A CB  
226   C CG  . PRO A 15  ? 0.7857 1.0504 0.9417 0.0216  0.0423  -0.0039 15  PRO A CG  
227   C CD  . PRO A 15  ? 0.7726 1.0298 0.9294 0.0235  0.0435  -0.0061 15  PRO A CD  
235   N N   . ALA A 16  ? 0.7634 1.0185 0.9316 0.0394  0.0411  0.0001  16  ALA A N   
236   C CA  . ALA A 16  ? 0.7995 1.0468 0.9638 0.0451  0.0397  0.0038  16  ALA A CA  
237   C C   . ALA A 16  ? 0.8294 1.0571 0.9747 0.0442  0.0400  0.0048  16  ALA A C   
238   O O   . ALA A 16  ? 0.8427 1.0609 0.9772 0.0435  0.0361  0.0073  16  ALA A O   
239   C CB  . ALA A 16  ? 0.7814 1.0336 0.9470 0.0444  0.0328  0.0055  16  ALA A CB  
245   N N   . GLY A 17  ? 0.8527 1.0715 0.9918 0.0438  0.0434  0.0029  17  GLY A N   
246   C CA  . GLY A 17  ? 0.8576 1.0533 0.9767 0.0426  0.0413  0.0038  17  GLY A CA  
247   C C   . GLY A 17  ? 0.8822 1.0763 0.9959 0.0307  0.0365  0.0043  17  GLY A C   
248   O O   . GLY A 17  ? 0.9090 1.0845 1.0086 0.0271  0.0328  0.0049  17  GLY A O   
252   N N   . ASN A 18  ? 0.8412 1.0535 0.9652 0.0250  0.0360  0.0048  18  ASN A N   
253   C CA  . ASN A 18  ? 0.8679 1.0843 0.9913 0.0146  0.0337  0.0073  18  ASN A CA  
254   C C   . ASN A 18  ? 0.8444 1.0692 0.9758 0.0120  0.0347  0.0044  18  ASN A C   
255   O O   . ASN A 18  ? 0.8438 1.0867 0.9860 0.0114  0.0376  0.0029  18  ASN A O   
256   C CB  . ASN A 18  ? 0.8578 1.0883 0.9855 0.0127  0.0351  0.0095  18  ASN A CB  
257   C CG  . ASN A 18  ? 0.8530 1.0866 0.9788 0.0030  0.0347  0.0153  18  ASN A CG  
258   O OD1 . ASN A 18  ? 0.8637 1.1097 0.9919 0.0022  0.0383  0.0174  18  ASN A OD1 
259   N ND2 . ASN A 18  ? 0.8684 1.0896 0.9892 -0.0041 0.0304  0.0187  18  ASN A ND2 
266   N N   . ILE A 19  ? 0.8681 1.0762 0.9906 0.0113  0.0316  0.0036  19  ILE A N   
267   C CA  . ILE A 19  ? 0.8589 1.0700 0.9855 0.0106  0.0312  0.0004  19  ILE A CA  
268   C C   . ILE A 19  ? 0.8282 1.0598 0.9686 0.0031  0.0303  0.0025  19  ILE A C   
269   O O   . ILE A 19  ? 0.8087 1.0418 0.9508 -0.0056 0.0262  0.0080  19  ILE A O   
270   C CB  . ILE A 19  ? 0.9146 1.0988 1.0237 0.0098  0.0252  0.0000  19  ILE A CB  
271   C CG1 . ILE A 19  ? 0.9054 1.0694 0.9992 0.0210  0.0292  -0.0018 19  ILE A CG1 
272   C CG2 . ILE A 19  ? 0.8718 1.0578 0.9837 0.0085  0.0229  -0.0029 19  ILE A CG2 
273   C CD1 . ILE A 19  ? 0.9192 1.0948 1.0225 0.0300  0.0382  -0.0052 19  ILE A CD1 
285   N N   . THR A 20  ? 0.8002 1.0476 0.9508 0.0069  0.0344  -0.0012 20  THR A N   
286   C CA  . THR A 20  ? 0.7935 1.0617 0.9568 0.0039  0.0358  0.0005  20  THR A CA  
287   C C   . THR A 20  ? 0.7677 1.0380 0.9349 0.0059  0.0342  -0.0032 20  THR A C   
288   O O   . THR A 20  ? 0.7519 1.0138 0.9137 0.0118  0.0359  -0.0084 20  THR A O   
289   C CB  . THR A 20  ? 0.7882 1.0700 0.9550 0.0088  0.0420  -0.0006 20  THR A CB  
290   O OG1 . THR A 20  ? 0.8001 1.0766 0.9605 0.0080  0.0423  0.0024  20  THR A OG1 
291   C CG2 . THR A 20  ? 0.7779 1.0795 0.9542 0.0082  0.0455  0.0021  20  THR A CG2 
299   N N   . ILE A 21  ? 0.7483 1.0302 0.9258 0.0009  0.0308  0.0004  21  ILE A N   
300   C CA  . ILE A 21  ? 0.7594 1.0468 0.9425 0.0036  0.0287  -0.0024 21  ILE A CA  
301   C C   . ILE A 21  ? 0.7629 1.0760 0.9601 0.0069  0.0346  -0.0004 21  ILE A C   
302   O O   . ILE A 21  ? 0.7481 1.0767 0.9554 0.0027  0.0371  0.0065  21  ILE A O   
303   C CB  . ILE A 21  ? 0.7766 1.0557 0.9606 -0.0037 0.0177  0.0006  21  ILE A CB  
304   C CG1 . ILE A 21  ? 0.8054 1.0526 0.9681 -0.0045 0.0122  -0.0018 21  ILE A CG1 
305   C CG2 . ILE A 21  ? 0.7836 1.0690 0.9738 0.0001  0.0145  -0.0021 21  ILE A CG2 
306   C CD1 . ILE A 21  ? 0.8160 1.0481 0.9741 -0.0132 -0.0015 0.0017  21  ILE A CD1 
318   N N   . LEU A 22  ? 0.7451 1.0609 0.9409 0.0150  0.0375  -0.0060 22  LEU A N   
319   C CA  . LEU A 22  ? 0.6987 1.0341 0.9027 0.0214  0.0433  -0.0051 22  LEU A CA  
320   C C   . LEU A 22  ? 0.7316 1.0737 0.9439 0.0243  0.0390  -0.0057 22  LEU A C   
321   O O   . LEU A 22  ? 0.7415 1.0679 0.9446 0.0266  0.0345  -0.0113 22  LEU A O   
322   C CB  . LEU A 22  ? 0.7264 1.0556 0.9182 0.0295  0.0487  -0.0111 22  LEU A CB  
323   C CG  . LEU A 22  ? 0.7668 1.0896 0.9508 0.0275  0.0511  -0.0106 22  LEU A CG  
324   C CD1 . LEU A 22  ? 0.7477 1.0622 0.9204 0.0339  0.0526  -0.0164 22  LEU A CD1 
325   C CD2 . LEU A 22  ? 0.6884 1.0248 0.8774 0.0252  0.0557  -0.0033 22  LEU A CD2 
337   N N   . ILE A 23  ? 0.7319 1.0976 0.9620 0.0245  0.0406  0.0011  23  ILE A N   
338   C CA  . ILE A 23  ? 0.7169 1.0936 0.9594 0.0280  0.0357  0.0021  23  ILE A CA  
339   C C   . ILE A 23  ? 0.7297 1.1167 0.9700 0.0421  0.0443  -0.0008 23  ILE A C   
340   O O   . ILE A 23  ? 0.7105 1.1130 0.9544 0.0471  0.0544  0.0032  23  ILE A O   
341   C CB  . ILE A 23  ? 0.7125 1.1117 0.9806 0.0193  0.0309  0.0131  23  ILE A CB  
342   C CG1 . ILE A 23  ? 0.7524 1.1324 1.0169 0.0068  0.0166  0.0138  23  ILE A CG1 
343   C CG2 . ILE A 23  ? 0.7104 1.1333 0.9979 0.0270  0.0304  0.0166  23  ILE A CG2 
344   C CD1 . ILE A 23  ? 0.7998 1.1562 1.0451 0.0011  0.0172  0.0112  23  ILE A CD1 
356   N N   . ASP A 24  ? 0.7552 1.1303 0.9860 0.0493  0.0405  -0.0077 24  ASP A N   
357   C CA  . ASP A 24  ? 0.7514 1.1276 0.9735 0.0635  0.0467  -0.0120 24  ASP A CA  
358   C C   . ASP A 24  ? 0.7447 1.1391 0.9828 0.0712  0.0441  -0.0086 24  ASP A C   
359   O O   . ASP A 24  ? 0.7174 1.1166 0.9695 0.0648  0.0342  -0.0053 24  ASP A O   
360   C CB  . ASP A 24  ? 0.7393 1.0862 0.9373 0.0660  0.0440  -0.0217 24  ASP A CB  
361   C CG  . ASP A 24  ? 0.7710 1.1109 0.9525 0.0775  0.0501  -0.0265 24  ASP A CG  
362   O OD1 . ASP A 24  ? 0.7858 1.1411 0.9703 0.0857  0.0578  -0.0231 24  ASP A OD1 
363   O OD2 . ASP A 24  ? 0.7913 1.1081 0.9549 0.0785  0.0472  -0.0332 24  ASP A OD2 
368   N N   . ASN A 25  ? 0.7343 1.1374 0.9688 0.0860  0.0523  -0.0093 25  ASN A N   
369   C CA  . ASN A 25  ? 0.7358 1.1565 0.9845 0.0972  0.0511  -0.0063 25  ASN A CA  
370   C C   . ASN A 25  ? 0.7153 1.1714 1.0004 0.0912  0.0499  0.0062  25  ASN A C   
371   O O   . ASN A 25  ? 0.7595 1.2289 1.0633 0.0928  0.0414  0.0098  25  ASN A O   
372   C CB  . ASN A 25  ? 0.7744 1.1731 1.0114 0.0984  0.0394  -0.0135 25  ASN A CB  
373   C CG  . ASN A 25  ? 0.7908 1.1553 0.9945 0.1020  0.0403  -0.0241 25  ASN A CG  
374   O OD1 . ASN A 25  ? 0.7686 1.1100 0.9598 0.0929  0.0342  -0.0288 25  ASN A OD1 
375   N ND2 . ASN A 25  ? 0.8889 1.2494 1.0776 0.1155  0.0482  -0.0272 25  ASN A ND2 
382   N N   . PHE A 26  ? 0.7359 1.2070 1.0318 0.0837  0.0575  0.0137  26  PHE A N   
383   C CA  . PHE A 26  ? 0.7557 1.2600 1.0872 0.0746  0.0568  0.0275  26  PHE A CA  
384   C C   . PHE A 26  ? 0.7503 1.2805 1.0909 0.0835  0.0751  0.0363  26  PHE A C   
385   O O   . PHE A 26  ? 0.7448 1.2594 1.0598 0.0893  0.0854  0.0314  26  PHE A O   
386   C CB  . PHE A 26  ? 0.7375 1.2295 1.0701 0.0539  0.0470  0.0294  26  PHE A CB  
387   C CG  . PHE A 26  ? 0.7475 1.2676 1.1155 0.0407  0.0411  0.0435  26  PHE A CG  
388   C CD1 . PHE A 26  ? 0.7713 1.2956 1.1572 0.0337  0.0239  0.0465  26  PHE A CD1 
389   C CD2 . PHE A 26  ? 0.7678 1.3079 1.1501 0.0343  0.0513  0.0544  26  PHE A CD2 
390   C CE1 . PHE A 26  ? 0.7817 1.3309 1.2016 0.0194  0.0158  0.0604  26  PHE A CE1 
391   C CE2 . PHE A 26  ? 0.7892 1.3550 1.2057 0.0200  0.0451  0.0689  26  PHE A CE2 
392   C CZ  . PHE A 26  ? 0.7623 1.3332 1.1989 0.0119  0.0266  0.0721  26  PHE A CZ  
402   N N   . ASP A 27  ? 0.7530 1.3225 1.1300 0.0851  0.0791  0.0499  27  ASP A N   
403   C CA  . ASP A 27  ? 0.7585 1.3557 1.1469 0.0932  0.0987  0.0610  27  ASP A CA  
404   C C   . ASP A 27  ? 0.7703 1.3576 1.1490 0.0790  0.1030  0.0639  27  ASP A C   
405   O O   . ASP A 27  ? 0.7728 1.3702 1.1733 0.0600  0.0951  0.0727  27  ASP A O   
406   C CB  . ASP A 27  ? 0.7181 1.3636 1.1551 0.0932  0.1012  0.0782  27  ASP A CB  
407   C CG  . ASP A 27  ? 0.7951 1.4712 1.2458 0.1006  0.1239  0.0921  27  ASP A CG  
408   O OD1 . ASP A 27  ? 0.8183 1.4802 1.2372 0.1178  0.1401  0.0866  27  ASP A OD1 
409   O OD2 . ASP A 27  ? 0.8222 1.5351 1.3141 0.0892  0.1254  0.1092  27  ASP A OD2 
414   N N   . ILE A 28  ? 0.7869 1.3520 1.1311 0.0880  0.1139  0.0568  28  ILE A N   
415   C CA  . ILE A 28  ? 0.8241 1.3750 1.1543 0.0759  0.1163  0.0579  28  ILE A CA  
416   C C   . ILE A 28  ? 0.8108 1.3937 1.1676 0.0693  0.1278  0.0755  28  ILE A C   
417   O O   . ILE A 28  ? 0.8086 1.3829 1.1607 0.0554  0.1270  0.0793  28  ILE A O   
418   C CB  . ILE A 28  ? 0.8367 1.3570 1.1242 0.0883  0.1239  0.0470  28  ILE A CB  
419   C CG1 . ILE A 28  ? 0.8425 1.3760 1.1218 0.1095  0.1431  0.0518  28  ILE A CG1 
420   C CG2 . ILE A 28  ? 0.8175 1.3070 1.0819 0.0924  0.1119  0.0313  28  ILE A CG2 
421   C CD1 . ILE A 28  ? 0.8552 1.3610 1.0941 0.1173  0.1515  0.0463  28  ILE A CD1 
433   N N   . TYR A 29  ? 0.8013 1.4216 1.1864 0.0796  0.1390  0.0874  29  TYR A N   
434   C CA  . TYR A 29  ? 0.8036 1.4600 1.2197 0.0734  0.1518  0.1069  29  TYR A CA  
435   C C   . TYR A 29  ? 0.7821 1.4732 1.2487 0.0586  0.1401  0.1198  29  TYR A C   
436   O O   . TYR A 29  ? 0.8154 1.5481 1.3188 0.0579  0.1517  0.1383  29  TYR A O   
437   C CB  . TYR A 29  ? 0.8076 1.4838 1.2194 0.0976  0.1769  0.1136  29  TYR A CB  
438   C CG  . TYR A 29  ? 0.8389 1.4778 1.1977 0.1121  0.1868  0.1017  29  TYR A CG  
439   C CD1 . TYR A 29  ? 0.8840 1.5088 1.2149 0.1369  0.1940  0.0919  29  TYR A CD1 
440   C CD2 . TYR A 29  ? 0.8568 1.4720 1.1918 0.1010  0.1872  0.1005  29  TYR A CD2 
441   C CE1 . TYR A 29  ? 0.9419 1.5292 1.2226 0.1490  0.2000  0.0813  29  TYR A CE1 
442   C CE2 . TYR A 29  ? 0.8697 1.4499 1.1566 0.1136  0.1935  0.0900  29  TYR A CE2 
443   C CZ  . TYR A 29  ? 0.9199 1.4858 1.1797 0.1370  0.1992  0.0805  29  TYR A CZ  
444   O OH  . TYR A 29  ? 0.9726 1.5002 1.1828 0.1484  0.2025  0.0702  29  TYR A OH  
454   N N   . ASP A 30  ? 0.7820 1.4563 1.2508 0.0470  0.1172  0.1114  30  ASP A N   
455   C CA  . ASP A 30  ? 0.8080 1.5085 1.3204 0.0313  0.1016  0.1228  30  ASP A CA  
456   C C   . ASP A 30  ? 0.7863 1.4978 1.3189 0.0081  0.0996  0.1378  30  ASP A C   
457   O O   . ASP A 30  ? 0.7846 1.4675 1.2893 -0.0007 0.1004  0.1335  30  ASP A O   
458   C CB  . ASP A 30  ? 0.8335 1.5034 1.3330 0.0241  0.0769  0.1091  30  ASP A CB  
459   C CG  . ASP A 30  ? 0.8298 1.5227 1.3704 0.0102  0.0577  0.1196  30  ASP A CG  
460   O OD1 . ASP A 30  ? 0.8724 1.5615 1.4249 -0.0125 0.0445  0.1272  30  ASP A OD1 
461   O OD2 . ASP A 30  ? 0.7962 1.5086 1.3557 0.0219  0.0543  0.1203  30  ASP A OD2 
466   N N   . LYS A 31  ? 0.7834 1.5369 1.3661 -0.0022 0.0962  0.1564  31  LYS A N   
467   C CA  . LYS A 31  ? 0.7627 1.5296 1.3686 -0.0256 0.0943  0.1735  31  LYS A CA  
468   C C   . LYS A 31  ? 0.7577 1.4851 1.3470 -0.0489 0.0681  0.1665  31  LYS A C   
469   O O   . LYS A 31  ? 0.7503 1.4614 1.3280 -0.0642 0.0679  0.1710  31  LYS A O   
470   C CB  . LYS A 31  ? 0.7284 1.5530 1.3968 -0.0315 0.0959  0.1966  31  LYS A CB  
471   C CG  . LYS A 31  ? 0.7301 1.5587 1.4292 -0.0517 0.0649  0.2009  31  LYS A CG  
472   C CD  . LYS A 31  ? 0.7214 1.6047 1.4765 -0.0449 0.0644  0.2156  31  LYS A CD  
473   C CE  . LYS A 31  ? 0.7111 1.5852 1.4823 -0.0598 0.0298  0.2130  31  LYS A CE  
474   N NZ  . LYS A 31  ? 0.7114 1.6371 1.5371 -0.0524 0.0257  0.2263  31  LYS A NZ  
488   N N   . ASN A 32  ? 0.7832 1.4913 1.3670 -0.0504 0.0461  0.1553  32  ASN A N   
489   C CA  . ASN A 32  ? 0.7855 1.4566 1.3546 -0.0712 0.0202  0.1503  32  ASN A CA  
490   C C   . ASN A 32  ? 0.8005 1.4195 1.3152 -0.0679 0.0202  0.1320  32  ASN A C   
491   O O   . ASN A 32  ? 0.7822 1.3656 1.2780 -0.0822 0.0010  0.1269  32  ASN A O   
492   C CB  . ASN A 32  ? 0.7571 1.4253 1.3382 -0.0728 -0.0033 0.1461  32  ASN A CB  
493   C CG  . ASN A 32  ? 0.7527 1.4731 1.3922 -0.0782 -0.0082 0.1653  32  ASN A CG  
494   O OD1 . ASN A 32  ? 0.7470 1.4884 1.4032 -0.0634 -0.0086 0.1637  32  ASN A OD1 
495   N ND2 . ASN A 32  ? 0.7379 1.4796 1.4097 -0.0998 -0.0125 0.1843  32  ASN A ND2 
502   N N   . ILE A 33  ? 0.8084 1.4226 1.2982 -0.0490 0.0411  0.1231  33  ILE A N   
503   C CA  . ILE A 33  ? 0.8003 1.3694 1.2433 -0.0451 0.0409  0.1067  33  ILE A CA  
504   C C   . ILE A 33  ? 0.8033 1.3440 1.2319 -0.0644 0.0294  0.1087  33  ILE A C   
505   O O   . ILE A 33  ? 0.7993 1.3016 1.1990 -0.0664 0.0168  0.0964  33  ILE A O   
506   C CB  . ILE A 33  ? 0.7921 1.3635 1.2152 -0.0267 0.0639  0.1017  33  ILE A CB  
507   C CG1 . ILE A 33  ? 0.7969 1.3680 1.2101 -0.0060 0.0682  0.0899  33  ILE A CG1 
508   C CG2 . ILE A 33  ? 0.7579 1.2924 1.1434 -0.0295 0.0651  0.0931  33  ILE A CG2 
509   C CD1 . ILE A 33  ? 0.7807 1.3497 1.1709 0.0127  0.0882  0.0847  33  ILE A CD1 
521   N N   . PRO A 34  ? 0.8107 1.3662 1.2553 -0.0776 0.0342  0.1239  34  PRO A N   
522   C CA  . PRO A 34  ? 0.8031 1.3252 1.2275 -0.0944 0.0230  0.1246  34  PRO A CA  
523   C C   . PRO A 34  ? 0.8074 1.3088 1.2344 -0.1105 -0.0037 0.1246  34  PRO A C   
524   O O   . PRO A 34  ? 0.8171 1.2763 1.2124 -0.1170 -0.0154 0.1171  34  PRO A O   
525   C CB  . PRO A 34  ? 0.7709 1.3180 1.2159 -0.1050 0.0352  0.1433  34  PRO A CB  
526   C CG  . PRO A 34  ? 0.7644 1.3605 1.2425 -0.0930 0.0538  0.1531  34  PRO A CG  
527   C CD  . PRO A 34  ? 0.7589 1.3621 1.2428 -0.0789 0.0485  0.1426  34  PRO A CD  
535   N N   . LYS A 35  ? 0.7999 1.3278 1.2618 -0.1161 -0.0144 0.1328  35  LYS A N   
536   C CA  . LYS A 35  ? 0.8130 1.3176 1.2747 -0.1319 -0.0427 0.1330  35  LYS A CA  
537   C C   . LYS A 35  ? 0.8337 1.2985 1.2580 -0.1202 -0.0524 0.1133  35  LYS A C   
538   O O   . LYS A 35  ? 0.8481 1.2681 1.2406 -0.1276 -0.0680 0.1066  35  LYS A O   
539   C CB  . LYS A 35  ? 0.8072 1.3537 1.3194 -0.1408 -0.0528 0.1481  35  LYS A CB  
540   C CG  . LYS A 35  ? 0.8320 1.4073 1.3815 -0.1621 -0.0537 0.1707  35  LYS A CG  
541   C CD  . LYS A 35  ? 0.8800 1.4776 1.4720 -0.1792 -0.0777 0.1845  35  LYS A CD  
542   C CE  . LYS A 35  ? 0.9333 1.5146 1.5317 -0.2089 -0.0976 0.1986  35  LYS A CE  
543   N NZ  . LYS A 35  ? 0.9157 1.5049 1.5461 -0.2273 -0.1286 0.2088  35  LYS A NZ  
557   N N   . LEU A 36  ? 0.8274 1.3059 1.2530 -0.1013 -0.0430 0.1044  36  LEU A N   
558   C CA  . LEU A 36  ? 0.8343 1.2757 1.2249 -0.0905 -0.0505 0.0871  36  LEU A CA  
559   C C   . LEU A 36  ? 0.8560 1.2646 1.2064 -0.0824 -0.0395 0.0751  36  LEU A C   
560   O O   . LEU A 36  ? 0.8959 1.2661 1.2140 -0.0786 -0.0476 0.0635  36  LEU A O   
561   C CB  . LEU A 36  ? 0.8126 1.2753 1.2141 -0.0731 -0.0440 0.0814  36  LEU A CB  
562   C CG  . LEU A 36  ? 0.8048 1.2986 1.2162 -0.0566 -0.0191 0.0814  36  LEU A CG  
563   C CD1 . LEU A 36  ? 0.7857 1.2656 1.1742 -0.0375 -0.0135 0.0662  36  LEU A CD1 
564   C CD2 . LEU A 36  ? 0.8230 1.3677 1.2814 -0.0572 -0.0143 0.0970  36  LEU A CD2 
576   N N   . SER A 37  ? 0.8519 1.2746 1.2038 -0.0794 -0.0213 0.0786  37  SER A N   
577   C CA  . SER A 37  ? 0.8858 1.2797 1.2029 -0.0722 -0.0126 0.0685  37  SER A CA  
578   C C   . SER A 37  ? 0.8878 1.2419 1.1803 -0.0840 -0.0268 0.0675  37  SER A C   
579   O O   . SER A 37  ? 0.9019 1.2223 1.1627 -0.0767 -0.0286 0.0560  37  SER A O   
580   C CB  . SER A 37  ? 0.8379 1.2533 1.1607 -0.0675 0.0072  0.0737  37  SER A CB  
581   O OG  . SER A 37  ? 0.7886 1.2195 1.1110 -0.0498 0.0215  0.0669  37  SER A OG  
587   N N   . GLU A 38  ? 0.8668 1.2234 1.1728 -0.1019 -0.0366 0.0803  38  GLU A N   
588   C CA  . GLU A 38  ? 0.9393 1.2526 1.2177 -0.1130 -0.0524 0.0794  38  GLU A CA  
589   C C   . GLU A 38  ? 0.9328 1.2141 1.1918 -0.1120 -0.0708 0.0709  38  GLU A C   
590   O O   . GLU A 38  ? 0.9257 1.1626 1.1477 -0.1103 -0.0782 0.0634  38  GLU A O   
591   C CB  . GLU A 38  ? 0.9020 1.2228 1.1994 -0.1345 -0.0618 0.0959  38  GLU A CB  
592   C CG  . GLU A 38  ? 0.8824 1.2404 1.2234 -0.1459 -0.0703 0.1089  38  GLU A CG  
593   C CD  . GLU A 38  ? 0.9435 1.2921 1.2955 -0.1711 -0.0903 0.1234  38  GLU A CD  
594   O OE1 . GLU A 38  ? 0.9895 1.3290 1.3340 -0.1807 -0.0863 0.1307  38  GLU A OE1 
595   O OE2 . GLU A 38  ? 1.0148 1.3632 1.3819 -0.1818 -0.1113 0.1278  38  GLU A OE2 
602   N N   . GLU A 39  ? 0.9165 1.2180 1.1977 -0.1115 -0.0778 0.0721  39  GLU A N   
603   C CA  . GLU A 39  ? 0.9459 1.2152 1.2050 -0.1085 -0.0946 0.0634  39  GLU A CA  
604   C C   . GLU A 39  ? 0.9276 1.1753 1.1551 -0.0889 -0.0825 0.0480  39  GLU A C   
605   O O   . GLU A 39  ? 0.9940 1.1979 1.1849 -0.0854 -0.0909 0.0400  39  GLU A O   
606   C CB  . GLU A 39  ? 0.9438 1.2426 1.2357 -0.1110 -0.1044 0.0686  39  GLU A CB  
607   C CG  . GLU A 39  ? 0.9683 1.2766 1.2870 -0.1330 -0.1254 0.0837  39  GLU A CG  
608   C CD  . GLU A 39  ? 1.1029 1.3576 1.3880 -0.1434 -0.1526 0.0806  39  GLU A CD  
609   O OE1 . GLU A 39  ? 1.0722 1.3174 1.3636 -0.1635 -0.1693 0.0916  39  GLU A OE1 
610   O OE2 . GLU A 39  ? 1.1621 1.3817 1.4123 -0.1314 -0.1575 0.0675  39  GLU A OE2 
617   N N   . ILE A 40  ? 0.9045 1.1814 1.1446 -0.0759 -0.0626 0.0444  40  ILE A N   
618   C CA  . ILE A 40  ? 0.9321 1.1928 1.1474 -0.0593 -0.0510 0.0316  40  ILE A CA  
619   C C   . ILE A 40  ? 0.9388 1.1669 1.1232 -0.0570 -0.0471 0.0272  40  ILE A C   
620   O O   . ILE A 40  ? 0.9526 1.1579 1.1123 -0.0454 -0.0422 0.0178  40  ILE A O   
621   C CB  . ILE A 40  ? 0.9157 1.2125 1.1502 -0.0480 -0.0322 0.0302  40  ILE A CB  
622   C CG1 . ILE A 40  ? 0.8865 1.2126 1.1478 -0.0458 -0.0350 0.0333  40  ILE A CG1 
623   C CG2 . ILE A 40  ? 0.8889 1.1697 1.1000 -0.0335 -0.0206 0.0186  40  ILE A CG2 
624   C CD1 . ILE A 40  ? 0.9232 1.2312 1.1793 -0.0495 -0.0542 0.0318  40  ILE A CD1 
636   N N   . MET A 41  ? 0.9476 1.1734 1.1332 -0.0674 -0.0487 0.0346  41  MET A N   
637   C CA  . MET A 41  ? 0.9525 1.1524 1.1119 -0.0631 -0.0430 0.0311  41  MET A CA  
638   C C   . MET A 41  ? 0.9670 1.1193 1.0934 -0.0677 -0.0583 0.0298  41  MET A C   
639   O O   . MET A 41  ? 1.0083 1.1341 1.1076 -0.0588 -0.0531 0.0245  41  MET A O   
640   C CB  . MET A 41  ? 0.9481 1.1675 1.1214 -0.0698 -0.0349 0.0394  41  MET A CB  
641   C CG  . MET A 41  ? 0.9074 1.1634 1.1006 -0.0613 -0.0171 0.0393  41  MET A CG  
642   S SD  . MET A 41  ? 0.9529 1.2346 1.1666 -0.0728 -0.0109 0.0531  41  MET A SD  
643   C CE  . MET A 41  ? 0.9013 1.1577 1.0866 -0.0672 -0.0043 0.0494  41  MET A CE  
653   N N   . LYS A 42  ? 0.9929 1.1330 1.1203 -0.0808 -0.0776 0.0350  42  LYS A N   
654   C CA  . LYS A 42  ? 1.0111 1.1002 1.1023 -0.0859 -0.0945 0.0341  42  LYS A CA  
655   C C   . LYS A 42  ? 1.0274 1.0797 1.0802 -0.0683 -0.0909 0.0223  42  LYS A C   
656   O O   . LYS A 42  ? 1.0288 1.0945 1.0862 -0.0561 -0.0805 0.0157  42  LYS A O   
657   C CB  . LYS A 42  ? 1.0114 1.0934 1.1109 -0.1026 -0.1185 0.0410  42  LYS A CB  
658   C CG  . LYS A 42  ? 1.0306 1.1175 1.1463 -0.1242 -0.1306 0.0545  42  LYS A CG  
659   C CD  . LYS A 42  ? 1.0807 1.1280 1.1622 -0.1259 -0.1320 0.0547  42  LYS A CD  
660   C CE  . LYS A 42  ? 1.1107 1.0938 1.1393 -0.1200 -0.1471 0.0465  42  LYS A CE  
661   N NZ  . LYS A 42  ? 1.1532 1.1053 1.1719 -0.1400 -0.1766 0.0538  42  LYS A NZ  
675   N N   . GLU A 43  ? 1.0665 1.0701 1.0795 -0.0666 -0.0990 0.0203  43  GLU A N   
676   C CA  . GLU A 43  ? 1.1672 1.1312 1.1399 -0.0494 -0.0959 0.0107  43  GLU A CA  
677   C C   . GLU A 43  ? 1.1285 1.0749 1.0897 -0.0499 -0.1099 0.0075  43  GLU A C   
678   O O   . GLU A 43  ? 1.1145 1.0470 1.0561 -0.0344 -0.1015 -0.0001 43  GLU A O   
679   C CB  . GLU A 43  ? 1.2106 1.1230 1.1398 -0.0459 -0.1021 0.0099  43  GLU A CB  
680   C CG  . GLU A 43  ? 1.2831 1.1477 1.1818 -0.0577 -0.1289 0.0121  43  GLU A CG  
681   C CD  . GLU A 43  ? 1.3902 1.1985 1.2401 -0.0520 -0.1345 0.0107  43  GLU A CD  
682   O OE1 . GLU A 43  ? 1.4460 1.2220 1.2789 -0.0675 -0.1569 0.0159  43  GLU A OE1 
683   O OE2 . GLU A 43  ? 1.4522 1.2483 1.2809 -0.0317 -0.1170 0.0050  43  GLU A OE2 
690   N N   . THR A 44  ? 1.1129 1.0598 1.0865 -0.0677 -0.1316 0.0140  44  THR A N   
691   C CA  . THR A 44  ? 1.0843 1.0165 1.0504 -0.0701 -0.1488 0.0120  44  THR A CA  
692   C C   . THR A 44  ? 1.0527 1.0320 1.0555 -0.0657 -0.1387 0.0108  44  THR A C   
693   O O   . THR A 44  ? 1.0691 1.0458 1.0751 -0.0694 -0.1539 0.0109  44  THR A O   
694   C CB  . THR A 44  ? 1.0856 1.0060 1.0581 -0.0925 -0.1775 0.0211  44  THR A CB  
695   O OG1 . THR A 44  ? 1.1177 1.0954 1.1459 -0.1071 -0.1747 0.0317  44  THR A OG1 
696   C CG2 . THR A 44  ? 1.1533 1.0220 1.0856 -0.0976 -0.1890 0.0224  44  THR A CG2 
704   N N   . ASN A 45  ? 1.0283 1.0478 1.0567 -0.0579 -0.1153 0.0099  45  ASN A N   
705   C CA  . ASN A 45  ? 0.9871 1.0455 1.0430 -0.0503 -0.1030 0.0073  45  ASN A CA  
706   C C   . ASN A 45  ? 0.9755 1.0374 1.0221 -0.0340 -0.0792 0.0005  45  ASN A C   
707   O O   . ASN A 45  ? 0.9809 1.0090 0.9947 -0.0258 -0.0745 -0.0033 45  ASN A O   
708   C CB  . ASN A 45  ? 0.9604 1.0714 1.0661 -0.0618 -0.1027 0.0164  45  ASN A CB  
709   C CG  . ASN A 45  ? 0.9520 1.0928 1.0818 -0.0569 -0.1013 0.0152  45  ASN A CG  
710   O OD1 . ASN A 45  ? 0.9271 1.0991 1.0749 -0.0479 -0.0834 0.0130  45  ASN A OD1 
711   N ND2 . ASN A 45  ? 1.0248 1.1531 1.1525 -0.0624 -0.1215 0.0166  45  ASN A ND2 
718   N N   . LEU A 46  ? 0.9449 1.0466 1.0196 -0.0285 -0.0643 -0.0005 46  LEU A N   
719   C CA  . LEU A 46  ? 0.9054 1.0166 0.9792 -0.0174 -0.0439 -0.0043 46  LEU A CA  
720   C C   . LEU A 46  ? 0.9671 1.0835 1.0460 -0.0232 -0.0407 0.0006  46  LEU A C   
721   O O   . LEU A 46  ? 0.9894 1.1259 1.0902 -0.0355 -0.0466 0.0079  46  LEU A O   
722   C CB  . LEU A 46  ? 0.8913 1.0407 0.9922 -0.0123 -0.0318 -0.0059 46  LEU A CB  
723   C CG  . LEU A 46  ? 0.8948 1.0394 0.9846 0.0014  -0.0177 -0.0127 46  LEU A CG  
724   C CD1 . LEU A 46  ? 0.9030 1.0126 0.9634 0.0075  -0.0235 -0.0172 46  LEU A CD1 
725   C CD2 . LEU A 46  ? 0.8225 1.0009 0.9366 0.0048  -0.0088 -0.0140 46  LEU A CD2 
737   N N   . TYR A 47  ? 1.0119 1.1092 1.0704 -0.0143 -0.0316 -0.0024 47  TYR A N   
738   C CA  . TYR A 47  ? 1.0275 1.1277 1.0885 -0.0184 -0.0287 0.0020  47  TYR A CA  
739   C C   . TYR A 47  ? 0.9102 1.0517 1.0010 -0.0176 -0.0156 0.0036  47  TYR A C   
740   O O   . TYR A 47  ? 0.8251 0.9863 0.9280 -0.0106 -0.0066 -0.0002 47  TYR A O   
741   C CB  . TYR A 47  ? 1.0291 1.0956 1.0588 -0.0072 -0.0238 -0.0013 47  TYR A CB  
742   C CG  . TYR A 47  ? 1.0490 1.1121 1.0764 -0.0105 -0.0232 0.0031  47  TYR A CG  
743   C CD1 . TYR A 47  ? 1.0840 1.1599 1.1170 -0.0009 -0.0094 0.0021  47  TYR A CD1 
744   C CD2 . TYR A 47  ? 1.0710 1.1173 1.0908 -0.0239 -0.0376 0.0088  47  TYR A CD2 
745   C CE1 . TYR A 47  ? 1.1364 1.2077 1.1656 -0.0032 -0.0096 0.0061  47  TYR A CE1 
746   C CE2 . TYR A 47  ? 1.1472 1.1877 1.1623 -0.0271 -0.0372 0.0132  47  TYR A CE2 
747   C CZ  . TYR A 47  ? 1.1600 1.2126 1.1788 -0.0159 -0.0228 0.0115  47  TYR A CZ  
748   O OH  . TYR A 47  ? 1.1602 1.2055 1.1726 -0.0180 -0.0230 0.0157  47  TYR A OH  
758   N N   . ALA A 48  ? 0.9930 1.1440 1.0923 -0.0249 -0.0153 0.0095  48  ALA A N   
759   C CA  . ALA A 48  ? 0.9235 1.1071 1.0439 -0.0233 -0.0035 0.0112  48  ALA A CA  
760   C C   . ALA A 48  ? 0.9224 1.1070 1.0438 -0.0311 -0.0041 0.0183  48  ALA A C   
761   O O   . ALA A 48  ? 0.9158 1.0906 1.0356 -0.0433 -0.0147 0.0248  48  ALA A O   
762   C CB  . ALA A 48  ? 0.8744 1.0911 1.0210 -0.0261 -0.0013 0.0128  48  ALA A CB  
768   N N   . GLU A 49  ? 0.9254 1.1203 1.0488 -0.0247 0.0060  0.0175  49  GLU A N   
769   C CA  . GLU A 49  ? 0.9026 1.1015 1.0271 -0.0307 0.0074  0.0242  49  GLU A CA  
770   C C   . GLU A 49  ? 0.8601 1.0925 1.0075 -0.0355 0.0139  0.0297  49  GLU A C   
771   O O   . GLU A 49  ? 0.8527 1.0896 1.0031 -0.0441 0.0142  0.0380  49  GLU A O   
772   C CB  . GLU A 49  ? 0.9041 1.0938 1.0163 -0.0202 0.0135  0.0209  49  GLU A CB  
773   C CG  . GLU A 49  ? 0.9855 1.1413 1.0736 -0.0136 0.0089  0.0176  49  GLU A CG  
774   C CD  . GLU A 49  ? 1.0380 1.1853 1.1161 -0.0047 0.0129  0.0173  49  GLU A CD  
775   O OE1 . GLU A 49  ? 1.1319 1.2501 1.1885 -0.0033 0.0076  0.0188  49  GLU A OE1 
776   O OE2 . GLU A 49  ? 0.9708 1.1384 1.0611 0.0014  0.0201  0.0155  49  GLU A OE2 
783   N N   . GLN A 50  ? 0.8701 1.1241 1.0315 -0.0296 0.0197  0.0258  50  GLN A N   
784   C CA  . GLN A 50  ? 0.8620 1.1466 1.0429 -0.0312 0.0269  0.0308  50  GLN A CA  
785   C C   . GLN A 50  ? 0.8061 1.1050 0.9980 -0.0248 0.0286  0.0255  50  GLN A C   
786   O O   . GLN A 50  ? 0.7740 1.0592 0.9572 -0.0190 0.0257  0.0177  50  GLN A O   
787   C CB  . GLN A 50  ? 0.8160 1.1081 0.9923 -0.0251 0.0369  0.0312  50  GLN A CB  
788   C CG  . GLN A 50  ? 0.8436 1.1303 1.0108 -0.0129 0.0403  0.0216  50  GLN A CG  
789   C CD  . GLN A 50  ? 0.8511 1.1346 1.0077 -0.0083 0.0447  0.0220  50  GLN A CD  
790   O OE1 . GLN A 50  ? 0.9027 1.1811 1.0534 -0.0003 0.0450  0.0157  50  GLN A OE1 
791   N NE2 . GLN A 50  ? 0.8224 1.1085 0.9768 -0.0140 0.0473  0.0300  50  GLN A NE2 
800   N N   . VAL A 51  ? 0.8255 1.1516 1.0359 -0.0250 0.0342  0.0304  51  VAL A N   
801   C CA  . VAL A 51  ? 0.7751 1.1153 0.9963 -0.0184 0.0352  0.0265  51  VAL A CA  
802   C C   . VAL A 51  ? 0.7960 1.1626 1.0282 -0.0116 0.0472  0.0299  51  VAL A C   
803   O O   . VAL A 51  ? 0.7902 1.1709 1.0305 -0.0160 0.0531  0.0393  51  VAL A O   
804   C CB  . VAL A 51  ? 0.7844 1.1270 1.0188 -0.0269 0.0239  0.0305  51  VAL A CB  
805   C CG1 . VAL A 51  ? 0.8324 1.1879 1.0831 -0.0405 0.0207  0.0434  51  VAL A CG1 
806   C CG2 . VAL A 51  ? 0.7851 1.1464 1.0333 -0.0194 0.0254  0.0281  51  VAL A CG2 
816   N N   . GLY A 52  ? 0.7761 1.1467 1.0057 -0.0001 0.0513  0.0226  52  GLY A N   
817   C CA  . GLY A 52  ? 0.7866 1.1766 1.0205 0.0096  0.0625  0.0245  52  GLY A CA  
818   C C   . GLY A 52  ? 0.7229 1.1227 0.9647 0.0179  0.0621  0.0207  52  GLY A C   
819   O O   . GLY A 52  ? 0.7382 1.1265 0.9784 0.0168  0.0532  0.0151  52  GLY A O   
823   N N   . PHE A 53  ? 0.7496 1.1690 0.9972 0.0278  0.0724  0.0241  53  PHE A N   
824   C CA  . PHE A 53  ? 0.7317 1.1630 0.9875 0.0381  0.0733  0.0219  53  PHE A CA  
825   C C   . PHE A 53  ? 0.7478 1.1727 0.9832 0.0538  0.0827  0.0159  53  PHE A C   
826   O O   . PHE A 53  ? 0.7943 1.2298 1.0266 0.0604  0.0944  0.0214  53  PHE A O   
827   C CB  . PHE A 53  ? 0.7146 1.1789 1.0013 0.0359  0.0761  0.0343  53  PHE A CB  
828   C CG  . PHE A 53  ? 0.7060 1.1733 1.0115 0.0187  0.0635  0.0408  53  PHE A CG  
829   C CD1 . PHE A 53  ? 0.7097 1.1701 1.0137 0.0054  0.0617  0.0464  53  PHE A CD1 
830   C CD2 . PHE A 53  ? 0.7226 1.1956 1.0440 0.0161  0.0518  0.0412  53  PHE A CD2 
831   C CE1 . PHE A 53  ? 0.7631 1.2205 1.0796 -0.0105 0.0482  0.0521  53  PHE A CE1 
832   C CE2 . PHE A 53  ? 0.7266 1.1969 1.0608 0.0000  0.0375  0.0468  53  PHE A CE2 
833   C CZ  . PHE A 53  ? 0.7104 1.1720 1.0415 -0.0135 0.0356  0.0522  53  PHE A CZ  
843   N N   . ILE A 54  ? 0.7452 1.1501 0.9642 0.0596  0.0775  0.0052  54  ILE A N   
844   C CA  . ILE A 54  ? 0.7917 1.1816 0.9859 0.0720  0.0823  -0.0017 54  ILE A CA  
845   C C   . ILE A 54  ? 0.8086 1.2075 1.0031 0.0870  0.0870  -0.0025 54  ILE A C   
846   O O   . ILE A 54  ? 0.7632 1.1739 0.9748 0.0873  0.0829  -0.0011 54  ILE A O   
847   C CB  . ILE A 54  ? 0.8068 1.1685 0.9832 0.0685  0.0735  -0.0115 54  ILE A CB  
848   C CG1 . ILE A 54  ? 0.7627 1.1191 0.9467 0.0642  0.0648  -0.0152 54  ILE A CG1 
849   C CG2 . ILE A 54  ? 0.7796 1.1325 0.9524 0.0582  0.0711  -0.0104 54  ILE A CG2 
850   C CD1 . ILE A 54  ? 0.7601 1.0914 0.9279 0.0627  0.0589  -0.0234 54  ILE A CD1 
862   N N   . LYS A 55  ? 0.8660 1.2569 1.0387 0.1007  0.0952  -0.0048 55  LYS A N   
863   C CA  . LYS A 55  ? 0.8718 1.2650 1.0368 0.1186  0.1005  -0.0066 55  LYS A CA  
864   C C   . LYS A 55  ? 0.9011 1.2636 1.0277 0.1293  0.1014  -0.0148 55  LYS A C   
865   O O   . LYS A 55  ? 0.9123 1.2695 1.0233 0.1323  0.1082  -0.0125 55  LYS A O   
866   C CB  . LYS A 55  ? 0.8396 1.2662 1.0246 0.1277  0.1143  0.0050  55  LYS A CB  
867   C CG  . LYS A 55  ? 0.8676 1.2930 1.0367 0.1509  0.1235  0.0034  55  LYS A CG  
868   C CD  . LYS A 55  ? 0.8894 1.3555 1.0915 0.1593  0.1340  0.0155  55  LYS A CD  
869   C CE  . LYS A 55  ? 0.8979 1.3634 1.0951 0.1786  0.1344  0.0117  55  LYS A CE  
870   N NZ  . LYS A 55  ? 0.9062 1.4136 1.1476 0.1796  0.1360  0.0228  55  LYS A NZ  
884   N N   . ASP A 56  ? 0.9711 1.3106 1.0801 0.1345  0.0935  -0.0239 56  ASP A N   
885   C CA  . ASP A 56  ? 1.0094 1.3141 1.0807 0.1407  0.0897  -0.0320 56  ASP A CA  
886   C C   . ASP A 56  ? 0.9126 1.2071 0.9794 0.1271  0.0847  -0.0322 56  ASP A C   
887   O O   . ASP A 56  ? 0.9400 1.2374 1.0240 0.1116  0.0772  -0.0324 56  ASP A O   
888   C CB  . ASP A 56  ? 1.0202 1.3200 1.0672 0.1621  0.1011  -0.0310 56  ASP A CB  
889   C CG  . ASP A 56  ? 1.1238 1.4413 1.1819 0.1774  0.1080  -0.0284 56  ASP A CG  
890   O OD1 . ASP A 56  ? 1.0966 1.4036 1.1537 0.1781  0.0991  -0.0342 56  ASP A OD1 
891   O OD2 . ASP A 56  ? 1.2134 1.5566 1.2825 0.1890  0.1227  -0.0197 56  ASP A OD2 
896   N N   . SER A 57  ? 0.9887 1.2706 1.0314 0.1335  0.0888  -0.0318 57  SER A N   
897   C CA  . SER A 57  ? 0.9721 1.2420 1.0084 0.1218  0.0822  -0.0323 57  SER A CA  
898   C C   . SER A 57  ? 0.9037 1.1955 0.9559 0.1163  0.0910  -0.0232 57  SER A C   
899   O O   . SER A 57  ? 0.9009 1.1820 0.9442 0.1094  0.0867  -0.0229 57  SER A O   
900   C CB  . SER A 57  ? 0.9235 1.1585 0.9188 0.1302  0.0768  -0.0383 57  SER A CB  
901   O OG  . SER A 57  ? 1.0408 1.2760 1.0170 0.1434  0.0892  -0.0338 57  SER A OG  
906   N N   . HIS A 58  ? 0.8910 1.2130 0.9673 0.1184  0.1020  -0.0151 58  HIS A N   
907   C CA  . HIS A 58  ? 0.8839 1.2269 0.9769 0.1114  0.1101  -0.0049 58  HIS A CA  
908   C C   . HIS A 58  ? 0.8467 1.2050 0.9714 0.0938  0.1030  -0.0019 58  HIS A C   
909   O O   . HIS A 58  ? 0.8287 1.1906 0.9676 0.0905  0.0964  -0.0053 58  HIS A O   
910   C CB  . HIS A 58  ? 0.8588 1.2271 0.9606 0.1237  0.1271  0.0047  58  HIS A CB  
911   C CG  . HIS A 58  ? 0.8478 1.2386 0.9683 0.1152  0.1361  0.0171  58  HIS A CG  
912   N ND1 . HIS A 58  ? 0.8758 1.2523 0.9784 0.1105  0.1369  0.0189  58  HIS A ND1 
913   C CD2 . HIS A 58  ? 0.8323 1.2576 0.9878 0.1096  0.1433  0.0289  58  HIS A CD2 
914   C CE1 . HIS A 58  ? 0.8842 1.2840 1.0081 0.1025  0.1453  0.0313  58  HIS A CE1 
915   N NE2 . HIS A 58  ? 0.8914 1.3217 1.0488 0.1010  0.1490  0.0379  58  HIS A NE2 
924   N N   . LEU A 59  ? 0.8499 1.2132 0.9813 0.0834  0.1040  0.0043  59  LEU A N   
925   C CA  . LEU A 59  ? 0.8186 1.1927 0.9751 0.0676  0.0979  0.0083  59  LEU A CA  
926   C C   . LEU A 59  ? 0.8036 1.2007 0.9767 0.0631  0.1075  0.0212  59  LEU A C   
927   O O   . LEU A 59  ? 0.8146 1.2069 0.9748 0.0630  0.1134  0.0257  59  LEU A O   
928   C CB  . LEU A 59  ? 0.7853 1.1389 0.9325 0.0582  0.0878  0.0036  59  LEU A CB  
929   C CG  . LEU A 59  ? 0.7843 1.1423 0.9482 0.0439  0.0828  0.0084  59  LEU A CG  
930   C CD1 . LEU A 59  ? 0.7481 1.1187 0.9341 0.0385  0.0789  0.0098  59  LEU A CD1 
931   C CD2 . LEU A 59  ? 0.7924 1.1298 0.9463 0.0389  0.0736  0.0027  59  LEU A CD2 
943   N N   . GLN A 60  ? 0.7717 1.1933 0.9733 0.0590  0.1084  0.0278  60  GLN A N   
944   C CA  . GLN A 60  ? 0.7462 1.1938 0.9704 0.0525  0.1165  0.0422  60  GLN A CA  
945   C C   . GLN A 60  ? 0.7793 1.2240 1.0181 0.0335  0.1046  0.0452  60  GLN A C   
946   O O   . GLN A 60  ? 0.7800 1.2299 1.0365 0.0268  0.0947  0.0445  60  GLN A O   
947   C CB  . GLN A 60  ? 0.7626 1.2409 1.0115 0.0603  0.1239  0.0492  60  GLN A CB  
948   C CG  . GLN A 60  ? 0.7399 1.2508 1.0153 0.0557  0.1355  0.0666  60  GLN A CG  
949   C CD  . GLN A 60  ? 0.8109 1.3165 1.0663 0.0596  0.1497  0.0726  60  GLN A CD  
950   O OE1 . GLN A 60  ? 0.7649 1.2648 0.9972 0.0774  0.1622  0.0704  60  GLN A OE1 
951   N NE2 . GLN A 60  ? 0.8118 1.3156 1.0722 0.0435  0.1473  0.0803  60  GLN A NE2 
960   N N   . MET A 61  ? 0.7815 1.2137 1.0088 0.0257  0.1045  0.0482  61  MET A N   
961   C CA  . MET A 61  ? 0.7812 1.2058 1.0170 0.0091  0.0935  0.0514  61  MET A CA  
962   C C   . MET A 61  ? 0.7774 1.2282 1.0441 -0.0020 0.0939  0.0652  61  MET A C   
963   O O   . MET A 61  ? 0.7907 1.2684 1.0730 0.0027  0.1063  0.0751  61  MET A O   
964   C CB  . MET A 61  ? 0.7970 1.2020 1.0122 0.0048  0.0939  0.0524  61  MET A CB  
965   C CG  . MET A 61  ? 0.7824 1.1620 0.9714 0.0130  0.0898  0.0400  61  MET A CG  
966   S SD  . MET A 61  ? 0.9167 1.2801 1.1061 0.0112  0.0759  0.0282  61  MET A SD  
967   C CE  . MET A 61  ? 0.8477 1.1956 1.0367 -0.0028 0.0666  0.0323  61  MET A CE  
977   N N   . MET A 62  ? 0.7735 1.2153 1.0487 -0.0166 0.0798  0.0664  62  MET A N   
978   C CA  . MET A 62  ? 0.7739 1.2378 1.0800 -0.0293 0.0748  0.0789  62  MET A CA  
979   C C   . MET A 62  ? 0.7843 1.2707 1.1051 -0.0353 0.0869  0.0952  62  MET A C   
980   O O   . MET A 62  ? 0.7750 1.2939 1.1282 -0.0396 0.0902  0.1078  62  MET A O   
981   C CB  . MET A 62  ? 0.7698 1.2100 1.0725 -0.0445 0.0561  0.0773  62  MET A CB  
982   C CG  . MET A 62  ? 0.8521 1.2600 1.1265 -0.0481 0.0532  0.0729  62  MET A CG  
983   S SD  . MET A 62  ? 0.9791 1.3582 1.2476 -0.0657 0.0327  0.0745  62  MET A SD  
984   C CE  . MET A 62  ? 0.8550 1.1960 1.0872 -0.0553 0.0301  0.0589  62  MET A CE  
994   N N   . GLY A 63  ? 0.8045 1.2752 1.1030 -0.0354 0.0939  0.0964  63  GLY A N   
995   C CA  . GLY A 63  ? 0.8190 1.3070 1.1271 -0.0415 0.1063  0.1126  63  GLY A CA  
996   C C   . GLY A 63  ? 0.7886 1.2772 1.0753 -0.0255 0.1254  0.1124  63  GLY A C   
997   O O   . GLY A 63  ? 0.8178 1.3038 1.0955 -0.0296 0.1345  0.1222  63  GLY A O   
1001  N N   . GLY A 64  ? 0.8071 1.2952 1.0818 -0.0071 0.1308  0.1015  64  GLY A N   
1002  C CA  . GLY A 64  ? 0.7802 1.2634 1.0290 0.0098  0.1470  0.1001  64  GLY A CA  
1003  C C   . GLY A 64  ? 0.8043 1.2528 1.0168 0.0098  0.1436  0.0937  64  GLY A C   
1004  O O   . GLY A 64  ? 0.8509 1.2903 1.0377 0.0215  0.1555  0.0943  64  GLY A O   
1008  N N   . GLU A 65  ? 0.8412 1.2686 1.0496 -0.0021 0.1273  0.0878  65  GLU A N   
1009  C CA  . GLU A 65  ? 0.8441 1.2401 1.0216 -0.0019 0.1222  0.0821  65  GLU A CA  
1010  C C   . GLU A 65  ? 0.8787 1.2557 1.0339 0.0117  0.1171  0.0663  65  GLU A C   
1011  O O   . GLU A 65  ? 0.9599 1.3423 1.1243 0.0165  0.1127  0.0582  65  GLU A O   
1012  C CB  . GLU A 65  ? 0.9088 1.2890 1.0900 -0.0179 0.1073  0.0824  65  GLU A CB  
1013  C CG  . GLU A 65  ? 0.9076 1.2793 1.0953 -0.0191 0.0928  0.0707  65  GLU A CG  
1014  C CD  . GLU A 65  ? 0.9723 1.3591 1.1881 -0.0313 0.0859  0.0766  65  GLU A CD  
1015  O OE1 . GLU A 65  ? 0.9591 1.3738 1.1976 -0.0340 0.0941  0.0875  65  GLU A OE1 
1016  O OE2 . GLU A 65  ? 0.9150 1.2852 1.1297 -0.0376 0.0721  0.0709  65  GLU A OE2 
1023  N N   . PHE A 66  ? 0.8402 1.1939 0.9660 0.0170  0.1165  0.0627  66  PHE A N   
1024  C CA  . PHE A 66  ? 0.8584 1.1916 0.9651 0.0259  0.1073  0.0490  66  PHE A CA  
1025  C C   . PHE A 66  ? 0.8561 1.1743 0.9659 0.0171  0.0923  0.0436  66  PHE A C   
1026  O O   . PHE A 66  ? 0.9040 1.2136 1.0112 0.0084  0.0893  0.0493  66  PHE A O   
1027  C CB  . PHE A 66  ? 0.8773 1.1911 0.9502 0.0363  0.1113  0.0477  66  PHE A CB  
1028  C CG  . PHE A 66  ? 0.8800 1.1707 0.9353 0.0416  0.0977  0.0355  66  PHE A CG  
1029  C CD1 . PHE A 66  ? 0.8594 1.1494 0.9145 0.0492  0.0938  0.0260  66  PHE A CD1 
1030  C CD2 . PHE A 66  ? 0.8544 1.1248 0.8951 0.0385  0.0881  0.0344  66  PHE A CD2 
1031  C CE1 . PHE A 66  ? 0.8757 1.1465 0.9186 0.0518  0.0805  0.0166  66  PHE A CE1 
1032  C CE2 . PHE A 66  ? 0.8341 1.0876 0.8644 0.0425  0.0748  0.0248  66  PHE A CE2 
1033  C CZ  . PHE A 66  ? 0.8677 1.1221 0.9003 0.0483  0.0709  0.0164  66  PHE A CZ  
1043  N N   . SER A 67  ? 0.8337 1.1479 0.9480 0.0202  0.0838  0.0332  67  SER A N   
1044  C CA  . SER A 67  ? 0.8485 1.1493 0.9652 0.0153  0.0719  0.0281  67  SER A CA  
1045  C C   . SER A 67  ? 0.8076 1.0972 0.9145 0.0234  0.0652  0.0183  67  SER A C   
1046  O O   . SER A 67  ? 0.7917 1.0868 0.9034 0.0281  0.0653  0.0126  67  SER A O   
1047  C CB  . SER A 67  ? 0.8037 1.1127 0.9411 0.0082  0.0681  0.0278  67  SER A CB  
1048  O OG  . SER A 67  ? 0.8080 1.1025 0.9442 0.0070  0.0588  0.0222  67  SER A OG  
1054  N N   . GLY A 68  ? 0.8234 1.0971 0.9175 0.0244  0.0583  0.0170  68  GLY A N   
1055  C CA  . GLY A 68  ? 0.7826 1.0473 0.8720 0.0299  0.0497  0.0094  68  GLY A CA  
1056  C C   . GLY A 68  ? 0.7915 1.0610 0.8995 0.0279  0.0450  0.0046  68  GLY A C   
1057  O O   . GLY A 68  ? 0.7956 1.0659 0.9064 0.0312  0.0420  -0.0011 68  GLY A O   
1061  N N   . ASN A 69  ? 0.8162 1.0861 0.9343 0.0226  0.0445  0.0071  69  ASN A N   
1062  C CA  . ASN A 69  ? 0.7710 1.0423 0.9026 0.0221  0.0418  0.0033  69  ASN A CA  
1063  C C   . ASN A 69  ? 0.7655 1.0470 0.9056 0.0221  0.0457  0.0004  69  ASN A C   
1064  O O   . ASN A 69  ? 0.7298 1.0118 0.8761 0.0244  0.0438  -0.0045 69  ASN A O   
1065  C CB  . ASN A 69  ? 0.7835 1.0473 0.9168 0.0181  0.0406  0.0067  69  ASN A CB  
1066  C CG  . ASN A 69  ? 0.7836 1.0365 0.9132 0.0218  0.0354  0.0071  69  ASN A CG  
1067  O OD1 . ASN A 69  ? 0.7433 0.9982 0.8769 0.0266  0.0318  0.0043  69  ASN A OD1 
1068  N ND2 . ASN A 69  ? 0.8098 1.0508 0.9321 0.0196  0.0340  0.0111  69  ASN A ND2 
1075  N N   . ALA A 70  ? 0.7622 1.0526 0.9038 0.0194  0.0512  0.0041  70  ALA A N   
1076  C CA  . ALA A 70  ? 0.7501 1.0513 0.9005 0.0207  0.0543  0.0019  70  ALA A CA  
1077  C C   . ALA A 70  ? 0.7668 1.0685 0.9100 0.0285  0.0554  -0.0032 70  ALA A C   
1078  O O   . ALA A 70  ? 0.7364 1.0389 0.8838 0.0310  0.0542  -0.0081 70  ALA A O   
1079  C CB  . ALA A 70  ? 0.7645 1.0790 0.9224 0.0164  0.0596  0.0089  70  ALA A CB  
1085  N N   . SER A 71  ? 0.7653 1.0626 0.8939 0.0327  0.0570  -0.0023 71  SER A N   
1086  C CA  . SER A 71  ? 0.7639 1.0548 0.8793 0.0406  0.0560  -0.0075 71  SER A CA  
1087  C C   . SER A 71  ? 0.7276 1.0084 0.8446 0.0398  0.0464  -0.0134 71  SER A C   
1088  O O   . SER A 71  ? 0.7548 1.0311 0.8678 0.0433  0.0441  -0.0183 71  SER A O   
1089  C CB  . SER A 71  ? 0.7867 1.0690 0.8803 0.0457  0.0584  -0.0051 71  SER A CB  
1090  O OG  . SER A 71  ? 0.7597 1.0541 0.8536 0.0470  0.0699  0.0019  71  SER A OG  
1096  N N   . ARG A 72  ? 0.7258 1.0030 0.8493 0.0353  0.0410  -0.0120 72  ARG A N   
1097  C CA  . ARG A 72  ? 0.7431 1.0159 0.8743 0.0341  0.0333  -0.0152 72  ARG A CA  
1098  C C   . ARG A 72  ? 0.7717 1.0500 0.9168 0.0323  0.0360  -0.0171 72  ARG A C   
1099  O O   . ARG A 72  ? 0.7483 1.0237 0.8973 0.0322  0.0323  -0.0201 72  ARG A O   
1100  C CB  . ARG A 72  ? 0.7612 1.0317 0.8979 0.0320  0.0283  -0.0120 72  ARG A CB  
1101  C CG  . ARG A 72  ? 0.7907 1.0526 0.9115 0.0340  0.0241  -0.0099 72  ARG A CG  
1102  C CD  . ARG A 72  ? 0.7780 1.0386 0.9039 0.0327  0.0217  -0.0056 72  ARG A CD  
1103  N NE  . ARG A 72  ? 0.7961 1.0609 0.9402 0.0324  0.0168  -0.0058 72  ARG A NE  
1104  C CZ  . ARG A 72  ? 0.8112 1.0802 0.9677 0.0322  0.0212  -0.0040 72  ARG A CZ  
1105  N NH1 . ARG A 72  ? 0.8089 1.0756 0.9606 0.0309  0.0276  -0.0023 72  ARG A NH1 
1106  N NH2 . ARG A 72  ? 0.8100 1.0847 0.9836 0.0335  0.0191  -0.0032 72  ARG A NH2 
1120  N N   . ALA A 73  ? 0.7300 1.0141 0.8813 0.0302  0.0415  -0.0149 73  ALA A N   
1121  C CA  . ALA A 73  ? 0.7368 1.0224 0.8961 0.0294  0.0434  -0.0168 73  ALA A CA  
1122  C C   . ALA A 73  ? 0.7422 1.0291 0.8972 0.0329  0.0445  -0.0207 73  ALA A C   
1123  O O   . ALA A 73  ? 0.7652 1.0478 0.9223 0.0333  0.0431  -0.0239 73  ALA A O   
1124  C CB  . ALA A 73  ? 0.7391 1.0269 0.9019 0.0261  0.0462  -0.0136 73  ALA A CB  
1130  N N   . PHE A 74  ? 0.7377 1.0297 0.8857 0.0362  0.0479  -0.0198 74  PHE A N   
1131  C CA  . PHE A 74  ? 0.7592 1.0512 0.9003 0.0424  0.0495  -0.0233 74  PHE A CA  
1132  C C   . PHE A 74  ? 0.7701 1.0479 0.8996 0.0449  0.0434  -0.0281 74  PHE A C   
1133  O O   . PHE A 74  ? 0.7541 1.0258 0.8797 0.0476  0.0419  -0.0320 74  PHE A O   
1134  C CB  . PHE A 74  ? 0.7821 1.0828 0.9170 0.0477  0.0563  -0.0199 74  PHE A CB  
1135  C CG  . PHE A 74  ? 0.7919 1.0941 0.9196 0.0570  0.0599  -0.0226 74  PHE A CG  
1136  C CD1 . PHE A 74  ? 0.7625 1.0620 0.8940 0.0583  0.0572  -0.0267 74  PHE A CD1 
1137  C CD2 . PHE A 74  ? 0.8211 1.1257 0.9359 0.0659  0.0668  -0.0205 74  PHE A CD2 
1138  C CE1 . PHE A 74  ? 0.7956 1.0948 0.9189 0.0683  0.0601  -0.0292 74  PHE A CE1 
1139  C CE2 . PHE A 74  ? 0.8368 1.1418 0.9432 0.0771  0.0711  -0.0227 74  PHE A CE2 
1140  C CZ  . PHE A 74  ? 0.8336 1.1359 0.9448 0.0783  0.0671  -0.0273 74  PHE A CZ  
1150  N N   . ALA A 75  ? 0.7583 1.0289 0.8810 0.0435  0.0384  -0.0275 75  ALA A N   
1151  C CA  . ALA A 75  ? 0.7886 1.0441 0.9009 0.0439  0.0293  -0.0312 75  ALA A CA  
1152  C C   . ALA A 75  ? 0.7735 1.0287 0.9014 0.0376  0.0251  -0.0315 75  ALA A C   
1153  O O   . ALA A 75  ? 0.7740 1.0186 0.8967 0.0370  0.0197  -0.0345 75  ALA A O   
1154  C CB  . ALA A 75  ? 0.7775 1.0249 0.8796 0.0434  0.0226  -0.0298 75  ALA A CB  
1160  N N   . SER A 76  ? 0.7788 1.0438 0.9241 0.0333  0.0280  -0.0279 76  SER A N   
1161  C CA  . SER A 76  ? 0.7381 1.0040 0.8979 0.0291  0.0275  -0.0268 76  SER A CA  
1162  C C   . SER A 76  ? 0.8021 1.0655 0.9598 0.0306  0.0320  -0.0295 76  SER A C   
1163  O O   . SER A 76  ? 0.8037 1.0626 0.9666 0.0278  0.0310  -0.0294 76  SER A O   
1164  C CB  . SER A 76  ? 0.7387 1.0128 0.9126 0.0274  0.0312  -0.0222 76  SER A CB  
1165  O OG  . SER A 76  ? 0.7337 1.0095 0.9105 0.0266  0.0258  -0.0194 76  SER A OG  
1171  N N   . LEU A 77  ? 0.8218 1.0886 0.9732 0.0347  0.0368  -0.0309 77  LEU A N   
1172  C CA  . LEU A 77  ? 0.8400 1.1041 0.9891 0.0371  0.0394  -0.0334 77  LEU A CA  
1173  C C   . LEU A 77  ? 0.8179 1.0706 0.9535 0.0407  0.0354  -0.0377 77  LEU A C   
1174  O O   . LEU A 77  ? 0.8367 1.0811 0.9698 0.0406  0.0348  -0.0396 77  LEU A O   
1175  C CB  . LEU A 77  ? 0.8209 1.0948 0.9713 0.0399  0.0438  -0.0324 77  LEU A CB  
1176  C CG  . LEU A 77  ? 0.7597 1.0322 0.9081 0.0436  0.0447  -0.0347 77  LEU A CG  
1177  C CD1 . LEU A 77  ? 0.7721 1.0344 0.9218 0.0406  0.0441  -0.0353 77  LEU A CD1 
1178  C CD2 . LEU A 77  ? 0.7681 1.0537 0.9239 0.0442  0.0470  -0.0316 77  LEU A CD2 
1190  N N   . LEU A 78  ? 0.8072 1.0556 0.9300 0.0446  0.0325  -0.0393 78  LEU A N   
1191  C CA  . LEU A 78  ? 0.7960 1.0276 0.8999 0.0492  0.0275  -0.0438 78  LEU A CA  
1192  C C   . LEU A 78  ? 0.8171 1.0351 0.9217 0.0415  0.0186  -0.0440 78  LEU A C   
1193  O O   . LEU A 78  ? 0.8286 1.0308 0.9214 0.0424  0.0144  -0.0470 78  LEU A O   
1194  C CB  . LEU A 78  ? 0.8563 1.0822 0.9412 0.0566  0.0268  -0.0451 78  LEU A CB  
1195  C CG  . LEU A 78  ? 0.8453 1.0859 0.9296 0.0652  0.0371  -0.0433 78  LEU A CG  
1196  C CD1 . LEU A 78  ? 0.7733 1.0097 0.8410 0.0707  0.0385  -0.0422 78  LEU A CD1 
1197  C CD2 . LEU A 78  ? 0.7440 0.9824 0.8203 0.0749  0.0407  -0.0462 78  LEU A CD2 
1209  N N   . ALA A 79  ? 0.8092 1.0334 0.9285 0.0339  0.0153  -0.0399 79  ALA A N   
1210  C CA  . ALA A 79  ? 0.8226 1.0402 0.9509 0.0250  0.0077  -0.0375 79  ALA A CA  
1211  C C   . ALA A 79  ? 0.8143 1.0352 0.9546 0.0220  0.0143  -0.0355 79  ALA A C   
1212  O O   . ALA A 79  ? 0.8225 1.0316 0.9606 0.0174  0.0100  -0.0352 79  ALA A O   
1213  C CB  . ALA A 79  ? 0.8203 1.0482 0.9656 0.0191  0.0034  -0.0324 79  ALA A CB  
1219  N N   . PHE A 80  ? 0.8064 1.0403 0.9566 0.0245  0.0241  -0.0338 80  PHE A N   
1220  C CA  . PHE A 80  ? 0.7821 1.0153 0.9379 0.0236  0.0309  -0.0322 80  PHE A CA  
1221  C C   . PHE A 80  ? 0.8086 1.0269 0.9480 0.0268  0.0297  -0.0366 80  PHE A C   
1222  O O   . PHE A 80  ? 0.8090 1.0192 0.9488 0.0239  0.0317  -0.0350 80  PHE A O   
1223  C CB  . PHE A 80  ? 0.7843 1.0274 0.9449 0.0272  0.0389  -0.0311 80  PHE A CB  
1224  C CG  . PHE A 80  ? 0.7535 0.9936 0.9182 0.0267  0.0459  -0.0283 80  PHE A CG  
1225  C CD1 . PHE A 80  ? 0.7516 0.9949 0.9298 0.0229  0.0495  -0.0224 80  PHE A CD1 
1226  C CD2 . PHE A 80  ? 0.7514 0.9853 0.9061 0.0310  0.0490  -0.0308 80  PHE A CD2 
1227  C CE1 . PHE A 80  ? 0.7655 1.0038 0.9437 0.0245  0.0583  -0.0192 80  PHE A CE1 
1228  C CE2 . PHE A 80  ? 0.7561 0.9820 0.9086 0.0317  0.0552  -0.0284 80  PHE A CE2 
1229  C CZ  . PHE A 80  ? 0.7504 0.9776 0.9129 0.0292  0.0610  -0.0227 80  PHE A CZ  
1239  N N   . ARG A 81  ? 0.8012 1.0151 0.9251 0.0338  0.0271  -0.0416 81  ARG A N   
1240  C CA  . ARG A 81  ? 0.8319 1.0322 0.9393 0.0398  0.0261  -0.0460 81  ARG A CA  
1241  C C   . ARG A 81  ? 0.8416 1.0213 0.9305 0.0400  0.0170  -0.0492 81  ARG A C   
1242  O O   . ARG A 81  ? 0.8829 1.0479 0.9538 0.0468  0.0154  -0.0533 81  ARG A O   
1243  C CB  . ARG A 81  ? 0.8182 1.0282 0.9213 0.0496  0.0302  -0.0484 81  ARG A CB  
1244  C CG  . ARG A 81  ? 0.7956 1.0213 0.9135 0.0485  0.0361  -0.0454 81  ARG A CG  
1245  C CD  . ARG A 81  ? 0.7603 0.9975 0.8783 0.0564  0.0385  -0.0462 81  ARG A CD  
1246  N NE  . ARG A 81  ? 0.8474 1.0903 0.9742 0.0548  0.0400  -0.0442 81  ARG A NE  
1247  C CZ  . ARG A 81  ? 0.8083 1.0647 0.9424 0.0582  0.0406  -0.0426 81  ARG A CZ  
1248  N NH1 . ARG A 81  ? 0.6949 0.9645 0.8310 0.0643  0.0426  -0.0418 81  ARG A NH1 
1249  N NH2 . ARG A 81  ? 0.7894 1.0454 0.9282 0.0555  0.0388  -0.0411 81  ARG A NH2 
1263  N N   . ASP A 82  ? 0.8490 1.0251 0.9403 0.0330  0.0097  -0.0473 82  ASP A N   
1264  C CA  . ASP A 82  ? 0.8597 1.0118 0.9296 0.0326  -0.0020 -0.0504 82  ASP A CA  
1265  C C   . ASP A 82  ? 0.8549 0.9937 0.9295 0.0209  -0.0087 -0.0470 82  ASP A C   
1266  O O   . ASP A 82  ? 0.8401 0.9908 0.9383 0.0100  -0.0097 -0.0403 82  ASP A O   
1267  C CB  . ASP A 82  ? 0.8982 1.0508 0.9650 0.0316  -0.0089 -0.0502 82  ASP A CB  
1268  C CG  . ASP A 82  ? 0.9064 1.0286 0.9473 0.0302  -0.0240 -0.0534 82  ASP A CG  
1269  O OD1 . ASP A 82  ? 0.9238 1.0229 0.9394 0.0367  -0.0268 -0.0582 82  ASP A OD1 
1270  O OD2 . ASP A 82  ? 0.8947 1.0138 0.9387 0.0230  -0.0345 -0.0510 82  ASP A OD2 
1275  N N   . LYS A 83  ? 0.8676 0.9821 0.9204 0.0234  -0.0131 -0.0505 83  LYS A N   
1276  C CA  . LYS A 83  ? 0.8745 0.9735 0.9297 0.0111  -0.0198 -0.0463 83  LYS A CA  
1277  C C   . LYS A 83  ? 0.9253 1.0183 0.9872 -0.0016 -0.0338 -0.0422 83  LYS A C   
1278  O O   . LYS A 83  ? 0.9083 1.0033 0.9893 -0.0156 -0.0372 -0.0344 83  LYS A O   
1279  C CB  . LYS A 83  ? 0.9360 1.0039 0.9599 0.0170  -0.0246 -0.0518 83  LYS A CB  
1280  C CG  . LYS A 83  ? 0.9360 0.9766 0.9268 0.0241  -0.0369 -0.0584 83  LYS A CG  
1281  C CD  . LYS A 83  ? 0.9997 1.0075 0.9567 0.0328  -0.0409 -0.0640 83  LYS A CD  
1282  C CE  . LYS A 83  ? 1.0734 1.0606 0.9947 0.0495  -0.0454 -0.0720 83  LYS A CE  
1283  N NZ  . LYS A 83  ? 1.1078 1.1212 1.0390 0.0581  -0.0372 -0.0727 83  LYS A NZ  
1297  N N   . ASP A 84  ? 0.9393 1.0248 0.9859 0.0032  -0.0425 -0.0464 84  ASP A N   
1298  C CA  . ASP A 84  ? 0.9271 0.9995 0.9724 -0.0077 -0.0602 -0.0438 84  ASP A CA  
1299  C C   . ASP A 84  ? 0.9377 1.0392 1.0161 -0.0148 -0.0599 -0.0371 84  ASP A C   
1300  O O   . ASP A 84  ? 0.9242 1.0200 1.0100 -0.0261 -0.0757 -0.0328 84  ASP A O   
1301  C CB  . ASP A 84  ? 0.9769 1.0189 0.9807 0.0029  -0.0711 -0.0522 84  ASP A CB  
1302  C CG  . ASP A 84  ? 0.9956 1.0034 0.9621 0.0115  -0.0738 -0.0589 84  ASP A CG  
1303  O OD1 . ASP A 84  ? 0.9323 0.9143 0.8894 0.0009  -0.0867 -0.0573 84  ASP A OD1 
1304  O OD2 . ASP A 84  ? 1.0170 1.0238 0.9639 0.0293  -0.0634 -0.0652 84  ASP A OD2 
1309  N N   . PHE A 85  ? 0.9370 1.0676 1.0343 -0.0084 -0.0440 -0.0359 85  PHE A N   
1310  C CA  . PHE A 85  ? 0.9263 1.0822 1.0524 -0.0132 -0.0434 -0.0297 85  PHE A CA  
1311  C C   . PHE A 85  ? 0.9458 1.1148 1.1054 -0.0277 -0.0460 -0.0193 85  PHE A C   
1312  O O   . PHE A 85  ? 0.9422 1.1165 1.1128 -0.0304 -0.0358 -0.0155 85  PHE A O   
1313  C CB  . PHE A 85  ? 0.8984 1.0784 1.0354 -0.0039 -0.0261 -0.0302 85  PHE A CB  
1314  C CG  . PHE A 85  ? 0.9389 1.1420 1.1018 -0.0069 -0.0250 -0.0242 85  PHE A CG  
1315  C CD1 . PHE A 85  ? 0.9009 1.1028 1.0548 -0.0033 -0.0319 -0.0262 85  PHE A CD1 
1316  C CD2 . PHE A 85  ? 0.9026 1.1269 1.0967 -0.0118 -0.0165 -0.0161 85  PHE A CD2 
1317  C CE1 . PHE A 85  ? 0.8880 1.1093 1.0643 -0.0051 -0.0318 -0.0207 85  PHE A CE1 
1318  C CE2 . PHE A 85  ? 0.8973 1.1420 1.1143 -0.0124 -0.0153 -0.0105 85  PHE A CE2 
1319  C CZ  . PHE A 85  ? 0.8832 1.1263 1.0916 -0.0093 -0.0237 -0.0129 85  PHE A CZ  
1329  N N   . SER A 86  ? 0.9746 1.1492 1.1507 -0.0367 -0.0597 -0.0137 86  SER A N   
1330  C CA  . SER A 86  ? 1.0602 1.2542 1.2753 -0.0502 -0.0618 -0.0015 86  SER A CA  
1331  C C   . SER A 86  ? 1.0577 1.2826 1.3015 -0.0469 -0.0553 0.0039  86  SER A C   
1332  O O   . SER A 86  ? 1.1417 1.3857 1.3978 -0.0395 -0.0362 0.0056  86  SER A O   
1333  C CB  . SER A 86  ? 1.0100 1.1847 1.2239 -0.0650 -0.0859 0.0021  86  SER A CB  
1334  O OG  . SER A 86  ? 1.0951 1.2521 1.2855 -0.0618 -0.1027 -0.0041 86  SER A OG  
1340  N N   . LYS A 87  ? 0.9753 1.2036 1.2281 -0.0513 -0.0711 0.0066  87  LYS A N   
1341  C CA  . LYS A 87  ? 0.9717 1.2264 1.2486 -0.0467 -0.0666 0.0113  87  LYS A CA  
1342  C C   . LYS A 87  ? 0.9860 1.2300 1.2349 -0.0360 -0.0697 0.0025  87  LYS A C   
1343  O O   . LYS A 87  ? 0.9582 1.2182 1.2132 -0.0271 -0.0571 0.0025  87  LYS A O   
1344  C CB  . LYS A 87  ? 1.0151 1.2859 1.3284 -0.0591 -0.0823 0.0230  87  LYS A CB  
1345  C CG  . LYS A 87  ? 1.0475 1.3379 1.3785 -0.0539 -0.0856 0.0265  87  LYS A CG  
1346  C CD  . LYS A 87  ? 1.0184 1.3316 1.3614 -0.0414 -0.0617 0.0278  87  LYS A CD  
1347  C CE  . LYS A 87  ? 0.9837 1.3287 1.3690 -0.0411 -0.0612 0.0397  87  LYS A CE  
1348  N NZ  . LYS A 87  ? 1.0491 1.4185 1.4740 -0.0474 -0.0512 0.0526  87  LYS A NZ  
1362  N N   . GLN A 88  ? 0.9289 1.1436 1.1446 -0.0363 -0.0859 -0.0045 88  GLN A N   
1363  C CA  . GLN A 88  ? 0.8956 1.0976 1.0821 -0.0263 -0.0890 -0.0115 88  GLN A CA  
1364  C C   . GLN A 88  ? 0.8963 1.0658 1.0373 -0.0194 -0.0907 -0.0217 88  GLN A C   
1365  O O   . GLN A 88  ? 0.9193 1.0665 1.0465 -0.0253 -0.1015 -0.0234 88  GLN A O   
1366  C CB  . GLN A 88  ? 0.9185 1.1162 1.1095 -0.0318 -0.1107 -0.0079 88  GLN A CB  
1367  C CG  . GLN A 88  ? 0.8723 1.0574 1.0336 -0.0212 -0.1130 -0.0136 88  GLN A CG  
1368  C CD  . GLN A 88  ? 0.9508 1.0965 1.0612 -0.0155 -0.1216 -0.0230 88  GLN A CD  
1369  O OE1 . GLN A 88  ? 0.9570 1.0946 1.0392 -0.0030 -0.1093 -0.0291 88  GLN A OE1 
1370  N NE2 . GLN A 88  ? 0.9851 1.1053 1.0831 -0.0245 -0.1428 -0.0234 88  GLN A NE2 
1379  N N   . LYS A 89  ? 0.8664 1.0328 0.9841 -0.0064 -0.0797 -0.0277 89  LYS A N   
1380  C CA  . LYS A 89  ? 0.8920 1.0303 0.9667 0.0034  -0.0791 -0.0364 89  LYS A CA  
1381  C C   . LYS A 89  ? 0.9081 1.0497 0.9650 0.0163  -0.0676 -0.0394 89  LYS A C   
1382  O O   . LYS A 89  ? 0.9194 1.0862 0.9957 0.0191  -0.0519 -0.0370 89  LYS A O   
1383  C CB  . LYS A 89  ? 0.8933 1.0300 0.9656 0.0055  -0.0681 -0.0392 89  LYS A CB  
1384  C CG  . LYS A 89  ? 0.8986 1.0099 0.9291 0.0186  -0.0648 -0.0475 89  LYS A CG  
1385  C CD  . LYS A 89  ? 0.9371 1.0219 0.9507 0.0152  -0.0740 -0.0505 89  LYS A CD  
1386  C CE  . LYS A 89  ? 0.9481 1.0151 0.9271 0.0310  -0.0651 -0.0579 89  LYS A CE  
1387  N NZ  . LYS A 89  ? 0.9953 1.0244 0.9445 0.0299  -0.0789 -0.0621 89  LYS A NZ  
1401  N N   . ASN A 90  ? 0.9424 1.0564 0.9605 0.0240  -0.0754 -0.0442 90  ASN A N   
1402  C CA  . ASN A 90  ? 0.9406 1.0557 0.9389 0.0364  -0.0634 -0.0459 90  ASN A CA  
1403  C C   . ASN A 90  ? 0.9390 1.0544 0.9223 0.0480  -0.0463 -0.0499 90  ASN A C   
1404  O O   . ASN A 90  ? 0.9607 1.0544 0.9222 0.0519  -0.0500 -0.0546 90  ASN A O   
1405  C CB  . ASN A 90  ? 0.9645 1.0477 0.9242 0.0413  -0.0778 -0.0486 90  ASN A CB  
1406  C CG  . ASN A 90  ? 1.0139 1.1050 0.9883 0.0350  -0.0882 -0.0435 90  ASN A CG  
1407  O OD1 . ASN A 90  ? 1.0280 1.1212 0.9909 0.0421  -0.0812 -0.0424 90  ASN A OD1 
1408  N ND2 . ASN A 90  ? 1.0037 1.0999 1.0045 0.0217  -0.1049 -0.0396 90  ASN A ND2 
1415  N N   . TYR A 91  ? 0.9087 1.0480 0.9042 0.0533  -0.0286 -0.0475 91  TYR A N   
1416  C CA  . TYR A 91  ? 0.9126 1.0591 0.9015 0.0637  -0.0123 -0.0493 91  TYR A CA  
1417  C C   . TYR A 91  ? 0.9285 1.0768 0.8991 0.0748  -0.0010 -0.0477 91  TYR A C   
1418  O O   . TYR A 91  ? 0.9821 1.1440 0.9645 0.0712  0.0022  -0.0430 91  TYR A O   
1419  C CB  . TYR A 91  ? 0.8871 1.0628 0.9118 0.0581  -0.0017 -0.0463 91  TYR A CB  
1420  C CG  . TYR A 91  ? 0.8679 1.0408 0.9064 0.0500  -0.0083 -0.0475 91  TYR A CG  
1421  C CD1 . TYR A 91  ? 0.8470 1.0064 0.8708 0.0553  -0.0078 -0.0519 91  TYR A CD1 
1422  C CD2 . TYR A 91  ? 0.8657 1.0492 0.9314 0.0380  -0.0142 -0.0434 91  TYR A CD2 
1423  C CE1 . TYR A 91  ? 0.8875 1.0421 0.9219 0.0473  -0.0134 -0.0522 91  TYR A CE1 
1424  C CE2 . TYR A 91  ? 0.9013 1.0830 0.9800 0.0304  -0.0183 -0.0428 91  TYR A CE2 
1425  C CZ  . TYR A 91  ? 0.8971 1.0635 0.9595 0.0343  -0.0180 -0.0472 91  TYR A CZ  
1426  O OH  . TYR A 91  ? 0.8724 1.0352 0.9463 0.0261  -0.0217 -0.0458 91  TYR A OH  
1436  N N   . ASN A 92  ? 0.9284 1.0623 0.8694 0.0888  0.0058  -0.0508 92  ASN A N   
1437  C CA  . ASN A 92  ? 0.9909 1.1268 0.9131 0.1011  0.0195  -0.0478 92  ASN A CA  
1438  C C   . ASN A 92  ? 0.9214 1.0904 0.8692 0.1045  0.0381  -0.0433 92  ASN A C   
1439  O O   . ASN A 92  ? 0.8998 1.0743 0.8545 0.1083  0.0418  -0.0456 92  ASN A O   
1440  C CB  . ASN A 92  ? 1.0157 1.1165 0.8891 0.1171  0.0179  -0.0527 92  ASN A CB  
1441  C CG  . ASN A 92  ? 1.0553 1.1196 0.8972 0.1144  -0.0018 -0.0561 92  ASN A CG  
1442  O OD1 . ASN A 92  ? 1.0690 1.1361 0.9164 0.1073  -0.0072 -0.0527 92  ASN A OD1 
1443  N ND2 . ASN A 92  ? 1.1367 1.1643 0.9439 0.1201  -0.0141 -0.0626 92  ASN A ND2 
1450  N N   . ILE A 93  ? 0.9298 1.1195 0.8913 0.1025  0.0485  -0.0364 93  ILE A N   
1451  C CA  . ILE A 93  ? 0.9446 1.1669 0.9340 0.1026  0.0636  -0.0304 93  ILE A CA  
1452  C C   . ILE A 93  ? 0.9556 1.1868 0.9370 0.1088  0.0774  -0.0226 93  ILE A C   
1453  O O   . ILE A 93  ? 0.9827 1.1947 0.9377 0.1119  0.0751  -0.0222 93  ILE A O   
1454  C CB  . ILE A 93  ? 0.9273 1.1701 0.9540 0.0871  0.0598  -0.0281 93  ILE A CB  
1455  C CG1 . ILE A 93  ? 0.9566 1.1943 0.9853 0.0776  0.0519  -0.0261 93  ILE A CG1 
1456  C CG2 . ILE A 93  ? 0.8577 1.0962 0.8948 0.0825  0.0509  -0.0338 93  ILE A CG2 
1457  C CD1 . ILE A 93  ? 0.8770 1.1365 0.9317 0.0686  0.0574  -0.0193 93  ILE A CD1 
1469  N N   . THR A 94  ? 0.9632 1.2236 0.9680 0.1101  0.0914  -0.0157 94  THR A N   
1470  C CA  . THR A 94  ? 0.9309 1.2069 0.9373 0.1130  0.1062  -0.0056 94  THR A CA  
1471  C C   . THR A 94  ? 0.9357 1.2418 0.9821 0.0986  0.1087  0.0019  94  THR A C   
1472  O O   . THR A 94  ? 0.8871 1.2061 0.9584 0.0925  0.1041  -0.0001 94  THR A O   
1473  C CB  . THR A 94  ? 0.9399 1.2226 0.9336 0.1313  0.1229  -0.0018 94  THR A CB  
1474  O OG1 . THR A 94  ? 0.9492 1.2639 0.9780 0.1303  0.1295  0.0025  94  THR A OG1 
1475  C CG2 . THR A 94  ? 1.0324 1.2818 0.9869 0.1462  0.1174  -0.0116 94  THR A CG2 
1483  N N   . CYS A 95  ? 0.9574 1.2709 1.0065 0.0934  0.1153  0.0107  95  CYS A N   
1484  C CA  . CYS A 95  ? 0.8826 1.2187 0.9641 0.0788  0.1160  0.0186  95  CYS A CA  
1485  C C   . CYS A 95  ? 0.8665 1.2204 0.9524 0.0800  0.1321  0.0318  95  CYS A C   
1486  O O   . CYS A 95  ? 0.9459 1.2869 1.0042 0.0889  0.1402  0.0346  95  CYS A O   
1487  C CB  . CYS A 95  ? 0.9038 1.2255 0.9852 0.0662  0.1029  0.0158  95  CYS A CB  
1488  S SG  . CYS A 95  ? 0.7041 1.0438 0.8192 0.0487  0.0996  0.0228  95  CYS A SG  
1494  N N   . SER A 96  ? 0.8864 1.2686 1.0065 0.0708  0.1360  0.0408  96  SER A N   
1495  C CA  . SER A 96  ? 0.8615 1.2644 0.9929 0.0681  0.1505  0.0559  96  SER A CA  
1496  C C   . SER A 96  ? 0.8295 1.2156 0.9460 0.0586  0.1480  0.0598  96  SER A C   
1497  O O   . SER A 96  ? 0.8443 1.2185 0.9648 0.0463  0.1339  0.0556  96  SER A O   
1498  C CB  . SER A 96  ? 0.8290 1.2641 1.0031 0.0567  0.1503  0.0647  96  SER A CB  
1499  O OG  . SER A 96  ? 0.7804 1.2071 0.9664 0.0427  0.1329  0.0586  96  SER A OG  
1505  N N   . GLY A 97  ? 0.8915 1.2747 0.9882 0.0658  0.1623  0.0681  97  GLY A N   
1506  C CA  . GLY A 97  ? 0.8737 1.2379 0.9509 0.0590  0.1608  0.0723  97  GLY A CA  
1507  C C   . GLY A 97  ? 0.8783 1.2070 0.9111 0.0704  0.1563  0.0631  97  GLY A C   
1508  O O   . GLY A 97  ? 0.8950 1.2062 0.9057 0.0684  0.1574  0.0676  97  GLY A O   
1512  N N   . GLU A 98  ? 0.8902 1.2054 0.9082 0.0815  0.1495  0.0507  98  GLU A N   
1513  C CA  . GLU A 98  ? 0.9490 1.2292 0.9235 0.0932  0.1437  0.0422  98  GLU A CA  
1514  C C   . GLU A 98  ? 1.0285 1.3059 0.9829 0.1124  0.1552  0.0400  98  GLU A C   
1515  O O   . GLU A 98  ? 1.0051 1.2981 0.9786 0.1158  0.1558  0.0363  98  GLU A O   
1516  C CB  . GLU A 98  ? 0.9817 1.2433 0.9550 0.0875  0.1213  0.0293  98  GLU A CB  
1517  C CG  . GLU A 98  ? 1.0544 1.2798 0.9857 0.0981  0.1113  0.0205  98  GLU A CG  
1518  C CD  . GLU A 98  ? 1.1423 1.3450 1.0438 0.0986  0.1098  0.0246  98  GLU A CD  
1519  O OE1 . GLU A 98  ? 1.1293 1.3322 1.0435 0.0865  0.1007  0.0264  98  GLU A OE1 
1520  O OE2 . GLU A 98  ? 1.1812 1.3635 1.0439 0.1122  0.1179  0.0261  98  GLU A OE2 
1527  N N   . SER A 99  ? 1.0814 1.3363 0.9943 0.1262  0.1645  0.0424  99  SER A N   
1528  C CA  . SER A 99  ? 1.1131 1.3603 0.9994 0.1476  0.1775  0.0410  99  SER A CA  
1529  C C   . SER A 99  ? 1.1839 1.3947 1.0366 0.1567  0.1605  0.0257  99  SER A C   
1530  O O   . SER A 99  ? 1.2550 1.4596 1.0911 0.1731  0.1671  0.0219  99  SER A O   
1531  C CB  . SER A 99  ? 1.1534 1.3890 1.0047 0.1605  0.1969  0.0513  99  SER A CB  
1532  O OG  . SER A 99  ? 1.1950 1.4013 1.0191 0.1540  0.1863  0.0504  99  SER A OG  
1538  N N   . LYS A 100 ? 1.1757 1.3623 1.0185 0.1465  0.1385  0.0175  100 LYS A N   
1539  C CA  . LYS A 100 ? 1.2467 1.3972 1.0580 0.1525  0.1200  0.0044  100 LYS A CA  
1540  C C   . LYS A 100 ? 1.2026 1.3663 1.0477 0.1424  0.1063  -0.0034 100 LYS A C   
1541  O O   . LYS A 100 ? 1.2186 1.4103 1.1065 0.1272  0.1039  -0.0007 100 LYS A O   
1542  C CB  . LYS A 100 ? 1.3010 1.4183 1.0843 0.1473  0.1020  0.0009  100 LYS A CB  
1543  C CG  . LYS A 100 ? 1.4346 1.5125 1.1578 0.1638  0.1064  0.0017  100 LYS A CG  
1544  C CD  . LYS A 100 ? 1.4507 1.5097 1.1366 0.1858  0.1176  -0.0014 100 LYS A CD  
1545  C CE  . LYS A 100 ? 1.4702 1.5148 1.1546 0.1863  0.1001  -0.0137 100 LYS A CE  
1546  N NZ  . LYS A 100 ? 1.4989 1.5375 1.1610 0.2072  0.1153  -0.0152 100 LYS A NZ  
1560  N N   . VAL A 101 ? 1.1960 1.3359 1.0179 0.1514  0.0972  -0.0129 101 VAL A N   
1561  C CA  . VAL A 101 ? 1.1245 1.2694 0.9714 0.1416  0.0822  -0.0205 101 VAL A CA  
1562  C C   . VAL A 101 ? 1.1032 1.2418 0.9631 0.1249  0.0622  -0.0231 101 VAL A C   
1563  O O   . VAL A 101 ? 1.1539 1.2649 0.9852 0.1253  0.0508  -0.0248 101 VAL A O   
1564  C CB  . VAL A 101 ? 1.1403 1.2538 0.9526 0.1546  0.0751  -0.0297 101 VAL A CB  
1565  C CG1 . VAL A 101 ? 1.1287 1.2366 0.9583 0.1419  0.0547  -0.0375 101 VAL A CG1 
1566  C CG2 . VAL A 101 ? 1.1277 1.2563 0.9397 0.1709  0.0953  -0.0269 101 VAL A CG2 
1576  N N   . LEU A 102 ? 1.0296 1.1933 0.9321 0.1111  0.0578  -0.0232 102 LEU A N   
1577  C CA  . LEU A 102 ? 1.0378 1.2020 0.9591 0.0965  0.0420  -0.0240 102 LEU A CA  
1578  C C   . LEU A 102 ? 1.0139 1.1658 0.9392 0.0915  0.0249  -0.0316 102 LEU A C   
1579  O O   . LEU A 102 ? 1.0206 1.1847 0.9642 0.0901  0.0276  -0.0340 102 LEU A O   
1580  C CB  . LEU A 102 ? 1.0055 1.2024 0.9679 0.0854  0.0492  -0.0181 102 LEU A CB  
1581  C CG  . LEU A 102 ? 1.0176 1.2259 0.9795 0.0859  0.0629  -0.0090 102 LEU A CG  
1582  C CD1 . LEU A 102 ? 0.9780 1.2183 0.9726 0.0816  0.0762  -0.0032 102 LEU A CD1 
1583  C CD2 . LEU A 102 ? 0.9768 1.1787 0.9404 0.0774  0.0536  -0.0063 102 LEU A CD2 
1595  N N   . ASP A 103 ? 1.0177 1.1452 0.9262 0.0883  0.0066  -0.0346 103 ASP A N   
1596  C CA  . ASP A 103 ? 1.0480 1.1636 0.9624 0.0809  -0.0119 -0.0398 103 ASP A CA  
1597  C C   . ASP A 103 ? 1.0515 1.1897 1.0073 0.0668  -0.0185 -0.0363 103 ASP A C   
1598  O O   . ASP A 103 ? 1.0509 1.1841 1.0081 0.0621  -0.0299 -0.0340 103 ASP A O   
1599  C CB  . ASP A 103 ? 1.1077 1.1834 0.9813 0.0848  -0.0301 -0.0439 103 ASP A CB  
1600  C CG  . ASP A 103 ? 1.1862 1.2496 1.0683 0.0745  -0.0516 -0.0475 103 ASP A CG  
1601  O OD1 . ASP A 103 ? 1.2074 1.2703 1.0939 0.0743  -0.0503 -0.0509 103 ASP A OD1 
1602  O OD2 . ASP A 103 ? 1.2016 1.2562 1.0872 0.0663  -0.0703 -0.0462 103 ASP A OD2 
1607  N N   . VAL A 104 ? 0.9925 1.1545 0.9807 0.0614  -0.0111 -0.0357 104 VAL A N   
1608  C CA  . VAL A 104 ? 0.9490 1.1328 0.9747 0.0508  -0.0132 -0.0319 104 VAL A CA  
1609  C C   . VAL A 104 ? 0.9136 1.0920 0.9524 0.0426  -0.0288 -0.0334 104 VAL A C   
1610  O O   . VAL A 104 ? 0.8867 1.0573 0.9213 0.0424  -0.0307 -0.0371 104 VAL A O   
1611  C CB  . VAL A 104 ? 0.9405 1.1489 0.9902 0.0497  0.0025  -0.0300 104 VAL A CB  
1612  C CG1 . VAL A 104 ? 0.8765 1.1027 0.9548 0.0425  0.0034  -0.0252 104 VAL A CG1 
1613  C CG2 . VAL A 104 ? 0.9318 1.1448 0.9677 0.0579  0.0174  -0.0284 104 VAL A CG2 
1623  N N   . ASP A 105 ? 0.8893 1.0726 0.9453 0.0358  -0.0399 -0.0297 105 ASP A N   
1624  C CA  . ASP A 105 ? 0.8780 1.0622 0.9545 0.0265  -0.0544 -0.0282 105 ASP A CA  
1625  C C   . ASP A 105 ? 0.8633 1.0751 0.9781 0.0214  -0.0442 -0.0240 105 ASP A C   
1626  O O   . ASP A 105 ? 0.8142 1.0422 0.9482 0.0210  -0.0402 -0.0193 105 ASP A O   
1627  C CB  . ASP A 105 ? 0.8776 1.0539 0.9540 0.0230  -0.0727 -0.0251 105 ASP A CB  
1628  C CG  . ASP A 105 ? 0.9014 1.0845 1.0067 0.0119  -0.0881 -0.0210 105 ASP A CG  
1629  O OD1 . ASP A 105 ? 0.9044 1.0920 1.0226 0.0068  -0.0855 -0.0214 105 ASP A OD1 
1630  O OD2 . ASP A 105 ? 0.8997 1.0843 1.0159 0.0081  -0.1032 -0.0167 105 ASP A OD2 
1635  N N   . VAL A 106 ? 0.8643 1.0779 0.9864 0.0187  -0.0401 -0.0257 106 VAL A N   
1636  C CA  . VAL A 106 ? 0.8252 1.0599 0.9769 0.0154  -0.0292 -0.0222 106 VAL A CA  
1637  C C   . VAL A 106 ? 0.8155 1.0551 0.9913 0.0059  -0.0392 -0.0174 106 VAL A C   
1638  O O   . VAL A 106 ? 0.8324 1.0559 0.9984 0.0010  -0.0511 -0.0193 106 VAL A O   
1639  C CB  . VAL A 106 ? 0.8274 1.0610 0.9702 0.0193  -0.0165 -0.0264 106 VAL A CB  
1640  C CG1 . VAL A 106 ? 0.8210 1.0704 0.9892 0.0161  -0.0069 -0.0229 106 VAL A CG1 
1641  C CG2 . VAL A 106 ? 0.8093 1.0438 0.9355 0.0275  -0.0062 -0.0286 106 VAL A CG2 
1651  N N   . ARG A 107 ? 0.8119 1.0729 1.0188 0.0036  -0.0341 -0.0106 107 ARG A N   
1652  C CA  . ARG A 107 ? 0.8445 1.1171 1.0815 -0.0050 -0.0399 -0.0034 107 ARG A CA  
1653  C C   . ARG A 107 ? 0.8214 1.1124 1.0806 -0.0031 -0.0224 0.0012  107 ARG A C   
1654  O O   . ARG A 107 ? 0.7947 1.0902 1.0490 0.0045  -0.0094 -0.0004 107 ARG A O   
1655  C CB  . ARG A 107 ? 0.8119 1.0935 1.0676 -0.0082 -0.0540 0.0030  107 ARG A CB  
1656  C CG  . ARG A 107 ? 0.8184 1.0773 1.0490 -0.0102 -0.0741 -0.0010 107 ARG A CG  
1657  C CD  . ARG A 107 ? 0.7541 1.0151 0.9816 -0.0048 -0.0797 0.0004  107 ARG A CD  
1658  N NE  . ARG A 107 ? 0.7674 1.0244 0.9724 0.0052  -0.0652 -0.0045 107 ARG A NE  
1659  C CZ  . ARG A 107 ? 0.7319 0.9994 0.9436 0.0109  -0.0594 -0.0015 107 ARG A CZ  
1660  N NH1 . ARG A 107 ? 0.6621 0.9474 0.9039 0.0100  -0.0640 0.0061  107 ARG A NH1 
1661  N NH2 . ARG A 107 ? 0.7841 1.0437 0.9719 0.0178  -0.0492 -0.0054 107 ARG A NH2 
1675  N N   . ASN A 108 ? 0.8581 1.1570 1.1395 -0.0104 -0.0224 0.0073  108 ASN A N   
1676  C CA  . ASN A 108 ? 0.8435 1.1570 1.1432 -0.0078 -0.0051 0.0126  108 ASN A CA  
1677  C C   . ASN A 108 ? 0.8556 1.1908 1.1813 -0.0029 0.0002  0.0206  108 ASN A C   
1678  O O   . ASN A 108 ? 0.8819 1.2276 1.2268 -0.0064 -0.0119 0.0263  108 ASN A O   
1679  C CB  . ASN A 108 ? 0.8689 1.1840 1.1840 -0.0173 -0.0056 0.0183  108 ASN A CB  
1680  C CG  . ASN A 108 ? 0.9100 1.2461 1.2541 -0.0153 0.0104  0.0286  108 ASN A CG  
1681  O OD1 . ASN A 108 ? 0.9302 1.2870 1.3076 -0.0192 0.0077  0.0393  108 ASN A OD1 
1682  N ND2 . ASN A 108 ? 0.8698 1.2001 1.2006 -0.0083 0.0271  0.0259  108 ASN A ND2 
1689  N N   . ASP A 109 ? 0.8482 1.1879 1.1727 0.0061  0.0174  0.0212  109 ASP A N   
1690  C CA  . ASP A 109 ? 0.8376 1.1935 1.1806 0.0142  0.0247  0.0281  109 ASP A CA  
1691  C C   . ASP A 109 ? 0.8555 1.2208 1.2129 0.0189  0.0428  0.0352  109 ASP A C   
1692  O O   . ASP A 109 ? 0.8509 1.2129 1.1987 0.0296  0.0561  0.0348  109 ASP A O   
1693  C CB  . ASP A 109 ? 0.8408 1.1866 1.1607 0.0231  0.0274  0.0220  109 ASP A CB  
1694  C CG  . ASP A 109 ? 0.8521 1.2105 1.1876 0.0312  0.0289  0.0284  109 ASP A CG  
1695  O OD1 . ASP A 109 ? 0.8858 1.2356 1.2048 0.0399  0.0364  0.0259  109 ASP A OD1 
1696  O OD2 . ASP A 109 ? 0.8530 1.2290 1.2171 0.0288  0.0215  0.0364  109 ASP A OD2 
1701  N N   . GLY A 110 ? 0.8888 1.2638 1.2675 0.0107  0.0430  0.0423  110 GLY A N   
1702  C CA  . GLY A 110 ? 0.8765 1.2601 1.2685 0.0148  0.0614  0.0505  110 GLY A CA  
1703  C C   . GLY A 110 ? 0.9301 1.2944 1.2989 0.0121  0.0685  0.0453  110 GLY A C   
1704  O O   . GLY A 110 ? 1.0297 1.3910 1.4032 0.0008  0.0618  0.0466  110 GLY A O   
1708  N N   . ALA A 111 ? 0.9272 1.2759 1.2695 0.0223  0.0804  0.0394  111 ALA A N   
1709  C CA  . ALA A 111 ? 0.9152 1.2442 1.2336 0.0214  0.0866  0.0343  111 ALA A CA  
1710  C C   . ALA A 111 ? 0.8625 1.1758 1.1597 0.0144  0.0722  0.0234  111 ALA A C   
1711  O O   . ALA A 111 ? 0.8359 1.1499 1.1296 0.0129  0.0601  0.0184  111 ALA A O   
1712  C CB  . ALA A 111 ? 0.9088 1.2232 1.2031 0.0343  0.1002  0.0310  111 ALA A CB  
1718  N N   . LYS A 112 ? 0.8346 1.1322 1.1154 0.0117  0.0746  0.0201  112 LYS A N   
1719  C CA  . LYS A 112 ? 0.7782 1.0605 1.0383 0.0075  0.0627  0.0104  112 LYS A CA  
1720  C C   . LYS A 112 ? 0.7646 1.0390 1.0031 0.0146  0.0611  0.0013  112 LYS A C   
1721  O O   . LYS A 112 ? 0.7980 1.0658 1.0238 0.0130  0.0513  -0.0056 112 LYS A O   
1722  C CB  . LYS A 112 ? 0.8262 1.0921 1.0722 0.0048  0.0662  0.0092  112 LYS A CB  
1723  C CG  . LYS A 112 ? 0.8714 1.1430 1.1370 -0.0029 0.0706  0.0198  112 LYS A CG  
1724  C CD  . LYS A 112 ? 0.9373 1.1940 1.1942 -0.0129 0.0586  0.0173  112 LYS A CD  
1725  C CE  . LYS A 112 ? 0.9804 1.2477 1.2651 -0.0253 0.0565  0.0295  112 LYS A CE  
1726  N NZ  . LYS A 112 ? 1.0173 1.2669 1.2919 -0.0365 0.0397  0.0266  112 LYS A NZ  
1740  N N   . ASN A 113 ? 0.7775 1.0508 1.0104 0.0227  0.0708  0.0017  113 ASN A N   
1741  C CA  . ASN A 113 ? 0.7664 1.0336 0.9825 0.0274  0.0684  -0.0049 113 ASN A CA  
1742  C C   . ASN A 113 ? 0.7865 1.0647 1.0115 0.0286  0.0640  -0.0036 113 ASN A C   
1743  O O   . ASN A 113 ? 0.7832 1.0577 0.9962 0.0303  0.0605  -0.0081 113 ASN A O   
1744  C CB  . ASN A 113 ? 0.7930 1.0472 0.9933 0.0346  0.0778  -0.0054 113 ASN A CB  
1745  C CG  . ASN A 113 ? 0.7753 1.0333 0.9831 0.0412  0.0876  0.0012  113 ASN A CG  
1746  O OD1 . ASN A 113 ? 0.7695 1.0395 0.9969 0.0408  0.0932  0.0088  113 ASN A OD1 
1747  N ND2 . ASN A 113 ? 0.8122 1.0594 1.0045 0.0476  0.0895  -0.0008 113 ASN A ND2 
1754  N N   . LYS A 114 ? 0.7840 1.0760 1.0307 0.0273  0.0637  0.0033  114 LYS A N   
1755  C CA  . LYS A 114 ? 0.7765 1.0778 1.0317 0.0291  0.0587  0.0052  114 LYS A CA  
1756  C C   . LYS A 114 ? 0.7818 1.0877 1.0429 0.0219  0.0446  0.0040  114 LYS A C   
1757  O O   . LYS A 114 ? 0.8279 1.1356 1.0982 0.0151  0.0393  0.0058  114 LYS A O   
1758  C CB  . LYS A 114 ? 0.8152 1.1292 1.0910 0.0346  0.0668  0.0143  114 LYS A CB  
1759  C CG  . LYS A 114 ? 0.8269 1.1314 1.0885 0.0453  0.0772  0.0143  114 LYS A CG  
1760  C CD  . LYS A 114 ? 0.8774 1.1897 1.1534 0.0537  0.0907  0.0233  114 LYS A CD  
1761  C CE  . LYS A 114 ? 0.9476 1.2753 1.2428 0.0594  0.0892  0.0296  114 LYS A CE  
1762  N NZ  . LYS A 114 ? 0.9994 1.3498 1.3276 0.0613  0.0969  0.0413  114 LYS A NZ  
1776  N N   . PHE A 115 ? 0.8017 1.1063 1.0543 0.0234  0.0378  0.0010  115 PHE A N   
1777  C CA  . PHE A 115 ? 0.7911 1.0935 1.0399 0.0186  0.0242  -0.0014 115 PHE A CA  
1778  C C   . PHE A 115 ? 0.7764 1.0831 1.0274 0.0215  0.0187  0.0008  115 PHE A C   
1779  O O   . PHE A 115 ? 0.7438 1.0542 0.9979 0.0274  0.0256  0.0035  115 PHE A O   
1780  C CB  . PHE A 115 ? 0.7711 1.0599 0.9947 0.0186  0.0221  -0.0093 115 PHE A CB  
1781  C CG  . PHE A 115 ? 0.7804 1.0621 0.9983 0.0167  0.0255  -0.0122 115 PHE A CG  
1782  C CD1 . PHE A 115 ? 0.8111 1.0902 1.0234 0.0202  0.0359  -0.0136 115 PHE A CD1 
1783  C CD2 . PHE A 115 ? 0.7886 1.0625 1.0033 0.0115  0.0166  -0.0136 115 PHE A CD2 
1784  C CE1 . PHE A 115 ? 0.7776 1.0483 0.9826 0.0193  0.0380  -0.0163 115 PHE A CE1 
1785  C CE2 . PHE A 115 ? 0.7681 1.0326 0.9749 0.0103  0.0191  -0.0163 115 PHE A CE2 
1786  C CZ  . PHE A 115 ? 0.7828 1.0466 0.9852 0.0146  0.0302  -0.0176 115 PHE A CZ  
1796  N N   . LEU A 116 ? 0.8307 1.1330 1.0762 0.0182  0.0054  -0.0007 116 LEU A N   
1797  C CA  . LEU A 116 ? 0.7872 1.0880 1.0268 0.0211  -0.0014 0.0001  116 LEU A CA  
1798  C C   . LEU A 116 ? 0.7641 1.0490 0.9764 0.0203  -0.0087 -0.0061 116 LEU A C   
1799  O O   . LEU A 116 ? 0.7934 1.0700 1.0002 0.0160  -0.0184 -0.0082 116 LEU A O   
1800  C CB  . LEU A 116 ? 0.7483 1.0604 1.0116 0.0192  -0.0122 0.0069  116 LEU A CB  
1801  C CG  . LEU A 116 ? 0.8134 1.1418 1.1002 0.0251  -0.0037 0.0142  116 LEU A CG  
1802  C CD1 . LEU A 116 ? 0.8470 1.1935 1.1676 0.0214  -0.0123 0.0229  116 LEU A CD1 
1803  C CD2 . LEU A 116 ? 0.8060 1.1294 1.0807 0.0324  -0.0030 0.0141  116 LEU A CD2 
1815  N N   . ALA A 117 ? 0.7802 1.0591 0.9739 0.0246  -0.0037 -0.0083 117 ALA A N   
1816  C CA  . ALA A 117 ? 0.7814 1.0466 0.9480 0.0262  -0.0058 -0.0131 117 ALA A CA  
1817  C C   . ALA A 117 ? 0.8449 1.1028 0.9976 0.0290  -0.0114 -0.0115 117 ALA A C   
1818  O O   . ALA A 117 ? 0.8580 1.1203 1.0142 0.0309  -0.0066 -0.0082 117 ALA A O   
1819  C CB  . ALA A 117 ? 0.7760 1.0421 0.9333 0.0286  0.0072  -0.0157 117 ALA A CB  
1825  N N   . LYS A 118 ? 0.8272 1.0698 0.9599 0.0296  -0.0222 -0.0139 118 LYS A N   
1826  C CA  . LYS A 118 ? 0.8580 1.0880 0.9698 0.0330  -0.0283 -0.0129 118 LYS A CA  
1827  C C   . LYS A 118 ? 0.8829 1.0988 0.9627 0.0382  -0.0217 -0.0164 118 LYS A C   
1828  O O   . LYS A 118 ? 0.9090 1.1177 0.9783 0.0394  -0.0213 -0.0207 118 LYS A O   
1829  C CB  . LYS A 118 ? 0.8745 1.0949 0.9863 0.0307  -0.0482 -0.0120 118 LYS A CB  
1830  C CG  . LYS A 118 ? 0.8984 1.0968 0.9778 0.0351  -0.0574 -0.0126 118 LYS A CG  
1831  C CD  . LYS A 118 ? 0.9214 1.1208 1.0127 0.0339  -0.0729 -0.0080 118 LYS A CD  
1832  C CE  . LYS A 118 ? 0.9196 1.1227 1.0327 0.0270  -0.0911 -0.0065 118 LYS A CE  
1833  N NZ  . LYS A 118 ? 0.9550 1.1305 1.0381 0.0256  -0.1064 -0.0113 118 LYS A NZ  
1847  N N   . ILE A 119 ? 0.8855 1.0967 0.9490 0.0418  -0.0157 -0.0139 119 ILE A N   
1848  C CA  . ILE A 119 ? 0.9109 1.1140 0.9480 0.0477  -0.0050 -0.0147 119 ILE A CA  
1849  C C   . ILE A 119 ? 0.9095 1.0968 0.9206 0.0516  -0.0071 -0.0115 119 ILE A C   
1850  O O   . ILE A 119 ? 0.9166 1.1061 0.9353 0.0492  -0.0107 -0.0076 119 ILE A O   
1851  C CB  . ILE A 119 ? 0.8731 1.0951 0.9252 0.0464  0.0117  -0.0124 119 ILE A CB  
1852  C CG1 . ILE A 119 ? 0.8887 1.1082 0.9203 0.0528  0.0240  -0.0118 119 ILE A CG1 
1853  C CG2 . ILE A 119 ? 0.8562 1.0865 0.9212 0.0423  0.0151  -0.0069 119 ILE A CG2 
1854  C CD1 . ILE A 119 ? 0.8443 1.0839 0.8926 0.0502  0.0385  -0.0073 119 ILE A CD1 
1866  N N   . LYS A 120 ? 0.9589 1.1282 0.9363 0.0591  -0.0044 -0.0131 120 LYS A N   
1867  C CA  . LYS A 120 ? 0.9375 1.0887 0.8843 0.0642  -0.0039 -0.0097 120 LYS A CA  
1868  C C   . LYS A 120 ? 0.9557 1.1213 0.9078 0.0633  0.0141  -0.0026 120 LYS A C   
1869  O O   . LYS A 120 ? 0.9687 1.1491 0.9283 0.0644  0.0292  -0.0012 120 LYS A O   
1870  C CB  . LYS A 120 ? 1.0132 1.1378 0.9180 0.0744  -0.0044 -0.0132 120 LYS A CB  
1871  C CG  . LYS A 120 ? 1.1065 1.2130 0.9748 0.0821  0.0035  -0.0083 120 LYS A CG  
1872  C CD  . LYS A 120 ? 1.1054 1.2270 0.9720 0.0871  0.0286  -0.0028 120 LYS A CD  
1873  C CE  . LYS A 120 ? 1.2011 1.3003 1.0243 0.0974  0.0382  0.0021  120 LYS A CE  
1874  N NZ  . LYS A 120 ? 1.1544 1.2759 0.9867 0.0985  0.0630  0.0116  120 LYS A NZ  
1888  N N   . MET A 121 ? 0.9644 1.1244 0.9118 0.0611  0.0117  0.0024  121 MET A N   
1889  C CA  . MET A 121 ? 0.9719 1.1433 0.9251 0.0577  0.0265  0.0102  121 MET A CA  
1890  C C   . MET A 121 ? 1.0006 1.1547 0.9180 0.0639  0.0352  0.0157  121 MET A C   
1891  O O   . MET A 121 ? 1.0291 1.1576 0.9161 0.0697  0.0249  0.0139  121 MET A O   
1892  C CB  . MET A 121 ? 0.9618 1.1377 0.9340 0.0508  0.0199  0.0131  121 MET A CB  
1893  C CG  . MET A 121 ? 0.9113 1.1049 0.9183 0.0458  0.0152  0.0095  121 MET A CG  
1894  S SD  . MET A 121 ? 0.9147 1.1317 0.9450 0.0413  0.0301  0.0098  121 MET A SD  
1895  C CE  . MET A 121 ? 0.8853 1.1050 0.9131 0.0356  0.0414  0.0195  121 MET A CE  
1905  N N   . PRO A 122 ? 1.0055 1.1729 0.9255 0.0627  0.0538  0.0232  122 PRO A N   
1906  C CA  . PRO A 122 ? 1.0000 1.1525 0.8866 0.0688  0.0652  0.0305  122 PRO A CA  
1907  C C   . PRO A 122 ? 1.0314 1.1591 0.8943 0.0684  0.0548  0.0330  122 PRO A C   
1908  O O   . PRO A 122 ? 0.9779 1.1063 0.8575 0.0617  0.0422  0.0318  122 PRO A O   
1909  C CB  . PRO A 122 ? 0.9518 1.1300 0.8603 0.0620  0.0840  0.0408  122 PRO A CB  
1910  C CG  . PRO A 122 ? 0.9790 1.1828 0.9279 0.0544  0.0816  0.0371  122 PRO A CG  
1911  C CD  . PRO A 122 ? 0.9788 1.1751 0.9313 0.0570  0.0652  0.0255  122 PRO A CD  
1919  N N   . LYS A 123 ? 1.0698 1.1737 0.8915 0.0772  0.0603  0.0366  123 LYS A N   
1920  C CA  . LYS A 123 ? 1.0854 1.1625 0.8792 0.0778  0.0516  0.0401  123 LYS A CA  
1921  C C   . LYS A 123 ? 1.0857 1.1709 0.8855 0.0697  0.0655  0.0523  123 LYS A C   
1922  O O   . LYS A 123 ? 1.0634 1.1711 0.8794 0.0659  0.0844  0.0597  123 LYS A O   
1923  C CB  . LYS A 123 ? 1.1531 1.1957 0.8941 0.0912  0.0510  0.0389  123 LYS A CB  
1924  C CG  . LYS A 123 ? 1.2441 1.2634 0.9685 0.0969  0.0269  0.0278  123 LYS A CG  
1925  C CD  . LYS A 123 ? 1.2800 1.2890 1.0110 0.0915  0.0041  0.0261  123 LYS A CD  
1926  C CE  . LYS A 123 ? 1.3261 1.3262 1.0615 0.0925  -0.0209 0.0162  123 LYS A CE  
1927  N NZ  . LYS A 123 ? 1.3106 1.3020 1.0530 0.0892  -0.0436 0.0159  123 LYS A NZ  
1941  N N   . PHE A 124 ? 1.1182 1.1842 0.9049 0.0669  0.0549  0.0550  124 PHE A N   
1942  C CA  . PHE A 124 ? 1.1538 1.2203 0.9405 0.0585  0.0653  0.0668  124 PHE A CA  
1943  C C   . PHE A 124 ? 1.1683 1.2159 0.9141 0.0650  0.0810  0.0762  124 PHE A C   
1944  O O   . PHE A 124 ? 1.2400 1.2624 0.9475 0.0775  0.0778  0.0722  124 PHE A O   
1945  C CB  . PHE A 124 ? 1.1756 1.2264 0.9622 0.0543  0.0477  0.0661  124 PHE A CB  
1946  C CG  . PHE A 124 ? 1.1470 1.1633 0.8947 0.0640  0.0323  0.0628  124 PHE A CG  
1947  C CD1 . PHE A 124 ? 1.2430 1.2315 0.9491 0.0674  0.0382  0.0710  124 PHE A CD1 
1948  C CD2 . PHE A 124 ? 1.1190 1.1304 0.8721 0.0692  0.0111  0.0523  124 PHE A CD2 
1949  C CE1 . PHE A 124 ? 1.2106 1.1641 0.8778 0.0769  0.0221  0.0678  124 PHE A CE1 
1950  C CE2 . PHE A 124 ? 1.2080 1.1876 0.9270 0.0774  -0.0060 0.0498  124 PHE A CE2 
1951  C CZ  . PHE A 124 ? 1.1946 1.1439 0.8690 0.0817  -0.0012 0.0570  124 PHE A CZ  
1961  N N   . LEU A 125 ? 1.1972 1.2552 0.9499 0.0561  0.0978  0.0894  125 LEU A N   
1962  C CA  . LEU A 125 ? 1.2448 1.2875 0.9613 0.0612  0.1161  0.1012  125 LEU A CA  
1963  C C   . LEU A 125 ? 1.2511 1.2593 0.9336 0.0597  0.1085  0.1067  125 LEU A C   
1964  O O   . LEU A 125 ? 1.2992 1.2814 0.9373 0.0686  0.1176  0.1128  125 LEU A O   
1965  C CB  . LEU A 125 ? 1.2331 1.3081 0.9774 0.0517  0.1401  0.1153  125 LEU A CB  
1966  C CG  . LEU A 125 ? 1.2612 1.3725 1.0406 0.0534  0.1496  0.1120  125 LEU A CG  
1967  C CD1 . LEU A 125 ? 1.2841 1.4306 1.1032 0.0389  0.1654  0.1261  125 LEU A CD1 
1968  C CD2 . LEU A 125 ? 1.2523 1.3558 1.0007 0.0721  0.1626  0.1100  125 LEU A CD2 
1980  N N   . SER A 126 ? 1.2593 1.2646 0.9589 0.0499  0.0925  0.1051  126 SER A N   
1981  C CA  . SER A 126 ? 1.2443 1.2155 0.9121 0.0492  0.0832  0.1097  126 SER A CA  
1982  C C   . SER A 126 ? 1.2584 1.2286 0.9487 0.0442  0.0611  0.1024  126 SER A C   
1983  O O   . SER A 126 ? 1.2507 1.2479 0.9823 0.0364  0.0593  0.0989  126 SER A O   
1984  C CB  . SER A 126 ? 1.2960 1.2649 0.9553 0.0388  0.1020  0.1273  126 SER A CB  
1985  O OG  . SER A 126 ? 1.2957 1.2817 0.9915 0.0226  0.0993  0.1315  126 SER A OG  
1991  N N   . LEU A 127 ? 1.2809 1.2184 0.9418 0.0500  0.0445  0.1004  127 LEU A N   
1992  C CA  . LEU A 127 ? 1.3014 1.2345 0.9787 0.0487  0.0240  0.0948  127 LEU A CA  
1993  C C   . LEU A 127 ? 1.3529 1.2525 0.9982 0.0469  0.0200  0.1035  127 LEU A C   
1994  O O   . LEU A 127 ? 1.3987 1.2669 1.0023 0.0560  0.0138  0.1045  127 LEU A O   
1995  C CB  . LEU A 127 ? 1.2919 1.2214 0.9708 0.0602  0.0031  0.0820  127 LEU A CB  
1996  C CG  . LEU A 127 ? 1.3227 1.2522 1.0222 0.0620  -0.0175 0.0765  127 LEU A CG  
1997  C CD1 . LEU A 127 ? 1.2508 1.1966 0.9811 0.0519  -0.0117 0.0797  127 LEU A CD1 
1998  C CD2 . LEU A 127 ? 1.3099 1.2558 1.0331 0.0686  -0.0321 0.0651  127 LEU A CD2 
2010  N N   . GLU A 128 ? 1.3537 1.2564 1.0150 0.0353  0.0224  0.1098  128 GLU A N   
2011  C CA  . GLU A 128 ? 1.4069 1.2763 1.0388 0.0321  0.0184  0.1187  128 GLU A CA  
2012  C C   . GLU A 128 ? 1.3764 1.2403 1.0245 0.0324  0.0010  0.1137  128 GLU A C   
2013  O O   . GLU A 128 ? 1.3759 1.2650 1.0618 0.0285  -0.0004 0.1083  128 GLU A O   
2014  C CB  . GLU A 128 ? 1.4295 1.2999 1.0579 0.0165  0.0384  0.1341  128 GLU A CB  
2015  C CG  . GLU A 128 ? 1.4535 1.3467 1.0860 0.0144  0.0611  0.1400  128 GLU A CG  
2016  C CD  . GLU A 128 ? 1.4843 1.3760 1.1099 -0.0002 0.0807  0.1584  128 GLU A CD  
2017  O OE1 . GLU A 128 ? 1.4814 1.3657 1.1155 -0.0138 0.0764  0.1652  128 GLU A OE1 
2018  O OE2 . GLU A 128 ? 1.5065 1.4034 1.1174 0.0022  0.1004  0.1667  128 GLU A OE2 
2025  N N   . GLU A 129 ? 1.4290 1.2576 1.0456 0.0385  -0.0120 0.1159  129 GLU A N   
2026  C CA  . GLU A 129 ? 1.3934 1.2089 1.0161 0.0404  -0.0265 0.1140  129 GLU A CA  
2027  C C   . GLU A 129 ? 1.4105 1.1974 1.0075 0.0284  -0.0202 0.1269  129 GLU A C   
2028  O O   . GLU A 129 ? 1.4794 1.2351 1.0357 0.0299  -0.0196 0.1344  129 GLU A O   
2029  C CB  . GLU A 129 ? 1.4323 1.2293 1.0401 0.0575  -0.0478 0.1072  129 GLU A CB  
2030  C CG  . GLU A 129 ? 1.4597 1.2463 1.0763 0.0634  -0.0619 0.1048  129 GLU A CG  
2031  C CD  . GLU A 129 ? 1.5291 1.3208 1.1571 0.0808  -0.0815 0.0960  129 GLU A CD  
2032  O OE1 . GLU A 129 ? 1.5540 1.3466 1.1729 0.0872  -0.0880 0.0928  129 GLU A OE1 
2033  O OE2 . GLU A 129 ? 1.5368 1.3311 1.1827 0.0883  -0.0908 0.0929  129 GLU A OE2 
2040  N N   . ILE A 130 ? 1.4035 1.1985 1.0221 0.0162  -0.0164 0.1298  130 ILE A N   
2041  C CA  . ILE A 130 ? 1.4238 1.1957 1.0237 0.0002  -0.0096 0.1434  130 ILE A CA  
2042  C C   . ILE A 130 ? 1.4443 1.1877 1.0357 0.0017  -0.0248 0.1422  130 ILE A C   
2043  O O   . ILE A 130 ? 1.4830 1.2380 1.0979 0.0097  -0.0341 0.1321  130 ILE A O   
2044  C CB  . ILE A 130 ? 1.3798 1.1821 1.0094 -0.0185 0.0075  0.1505  130 ILE A CB  
2045  C CG1 . ILE A 130 ? 1.4059 1.2369 1.0772 -0.0191 0.0031  0.1404  130 ILE A CG1 
2046  C CG2 . ILE A 130 ? 1.4167 1.2428 1.0486 -0.0182 0.0249  0.1539  130 ILE A CG2 
2047  C CD1 . ILE A 130 ? 1.3849 1.2385 1.0838 -0.0389 0.0145  0.1482  130 ILE A CD1 
2059  N N   . ASN A 131 ? 1.4959 1.1998 1.0511 -0.0054 -0.0266 0.1532  131 ASN A N   
2060  C CA  . ASN A 131 ? 1.4919 1.1604 1.0305 -0.0057 -0.0400 0.1543  131 ASN A CA  
2061  C C   . ASN A 131 ? 1.5260 1.1873 1.0667 -0.0303 -0.0322 0.1667  131 ASN A C   
2062  O O   . ASN A 131 ? 1.5036 1.1515 1.0241 -0.0442 -0.0224 0.1807  131 ASN A O   
2063  C CB  . ASN A 131 ? 1.5455 1.1684 1.0372 0.0056  -0.0514 0.1574  131 ASN A CB  
2064  C CG  . ASN A 131 ? 1.5671 1.1868 1.0604 0.0303  -0.0686 0.1448  131 ASN A CG  
2065  O OD1 . ASN A 131 ? 1.6145 1.2480 1.1104 0.0434  -0.0719 0.1388  131 ASN A OD1 
2066  N ND2 . ASN A 131 ? 1.6022 1.2025 1.0935 0.0370  -0.0802 0.1413  131 ASN A ND2 
2073  N N   . VAL A 132 ? 1.5607 1.2305 1.1255 -0.0360 -0.0367 0.1623  132 VAL A N   
2074  C CA  . VAL A 132 ? 1.5553 1.2186 1.1258 -0.0603 -0.0335 0.1732  132 VAL A CA  
2075  C C   . VAL A 132 ? 1.6166 1.2311 1.1588 -0.0592 -0.0505 0.1727  132 VAL A C   
2076  O O   . VAL A 132 ? 1.6218 1.2333 1.1704 -0.0444 -0.0608 0.1605  132 VAL A O   
2077  C CB  . VAL A 132 ? 1.5829 1.2909 1.2002 -0.0689 -0.0265 0.1689  132 VAL A CB  
2078  C CG1 . VAL A 132 ? 1.6338 1.3255 1.2547 -0.0893 -0.0328 0.1758  132 VAL A CG1 
2079  C CG2 . VAL A 132 ? 1.5576 1.3066 1.1974 -0.0765 -0.0075 0.1751  132 VAL A CG2 
2089  N N   . ASP A 133 ? 1.6970 1.2718 1.2064 -0.0745 -0.0529 0.1866  133 ASP A N   
2090  C CA  . ASP A 133 ? 1.7011 1.2212 1.1753 -0.0732 -0.0701 0.1871  133 ASP A CA  
2091  C C   . ASP A 133 ? 1.6935 1.1949 1.1471 -0.0427 -0.0813 0.1745  133 ASP A C   
2092  O O   . ASP A 133 ? 1.7320 1.2277 1.1671 -0.0313 -0.0800 0.1755  133 ASP A O   
2093  C CB  . ASP A 133 ? 1.7485 1.2679 1.2403 -0.0842 -0.0771 0.1842  133 ASP A CB  
2094  C CG  . ASP A 133 ? 1.8027 1.3343 1.3124 -0.1167 -0.0701 0.1994  133 ASP A CG  
2095  O OD1 . ASP A 133 ? 1.8244 1.3603 1.3291 -0.1306 -0.0589 0.2137  133 ASP A OD1 
2096  O OD2 . ASP A 133 ? 1.8023 1.3392 1.3312 -0.1280 -0.0758 0.1977  133 ASP A OD2 
2101  N N   . GLU A 134 ? 1.6989 1.1912 1.1558 -0.0283 -0.0920 0.1634  134 GLU A N   
2102  C CA  . GLU A 134 ? 1.7205 1.2004 1.1646 0.0019  -0.1020 0.1525  134 GLU A CA  
2103  C C   . GLU A 134 ? 1.6787 1.2079 1.1661 0.0188  -0.0981 0.1390  134 GLU A C   
2104  O O   . GLU A 134 ? 1.6898 1.2132 1.1771 0.0419  -0.1061 0.1298  134 GLU A O   
2105  C CB  . GLU A 134 ? 1.8209 1.2448 1.2278 0.0101  -0.1171 0.1516  134 GLU A CB  
2106  C CG  . GLU A 134 ? 1.8034 1.2196 1.2181 -0.0018 -0.1197 0.1500  134 GLU A CG  
2107  C CD  . GLU A 134 ? 1.8762 1.2403 1.2549 0.0157  -0.1343 0.1448  134 GLU A CD  
2108  O OE1 . GLU A 134 ? 1.9198 1.2618 1.2748 0.0396  -0.1411 0.1416  134 GLU A OE1 
2109  O OE2 . GLU A 134 ? 1.9064 1.2499 1.2788 0.0065  -0.1395 0.1441  134 GLU A OE2 
2116  N N   . TYR A 135 ? 1.6147 1.1927 1.1394 0.0081  -0.0851 0.1384  135 TYR A N   
2117  C CA  . TYR A 135 ? 1.5528 1.1780 1.1186 0.0213  -0.0808 0.1267  135 TYR A CA  
2118  C C   . TYR A 135 ? 1.5203 1.1803 1.1020 0.0219  -0.0721 0.1267  135 TYR A C   
2119  O O   . TYR A 135 ? 1.5088 1.1725 1.0850 0.0050  -0.0625 0.1360  135 TYR A O   
2120  C CB  . TYR A 135 ? 1.5570 1.2065 1.1534 0.0086  -0.0747 0.1240  135 TYR A CB  
2121  C CG  . TYR A 135 ? 1.6093 1.2218 1.1875 0.0074  -0.0840 0.1233  135 TYR A CG  
2122  C CD1 . TYR A 135 ? 1.6280 1.2242 1.1975 0.0315  -0.0921 0.1144  135 TYR A CD1 
2123  C CD2 . TYR A 135 ? 1.6396 1.2332 1.2091 -0.0172 -0.0849 0.1320  135 TYR A CD2 
2124  C CE1 . TYR A 135 ? 1.6799 1.2370 1.2264 0.0328  -0.1003 0.1132  135 TYR A CE1 
2125  C CE2 . TYR A 135 ? 1.6899 1.2438 1.2375 -0.0185 -0.0959 0.1308  135 TYR A CE2 
2126  C CZ  . TYR A 135 ? 1.7145 1.2480 1.2478 0.0075  -0.1032 0.1209  135 TYR A CZ  
2127  O OH  . TYR A 135 ? 1.7535 1.2423 1.2589 0.0085  -0.1138 0.1193  135 TYR A OH  
2137  N N   . LYS A 136 ? 1.5061 1.1903 1.1067 0.0417  -0.0756 0.1171  136 LYS A N   
2138  C CA  . LYS A 136 ? 1.4383 1.1577 1.0578 0.0431  -0.0690 0.1145  136 LYS A CA  
2139  C C   . LYS A 136 ? 1.4580 1.2211 1.1198 0.0356  -0.0586 0.1092  136 LYS A C   
2140  O O   . LYS A 136 ? 1.4264 1.2015 1.1100 0.0426  -0.0611 0.1020  136 LYS A O   
2141  C CB  . LYS A 136 ? 1.4262 1.1495 1.0473 0.0660  -0.0808 0.1075  136 LYS A CB  
2142  C CG  . LYS A 136 ? 1.4991 1.2577 1.1416 0.0697  -0.0781 0.1026  136 LYS A CG  
2143  C CD  . LYS A 136 ? 1.4563 1.2594 1.1441 0.0674  -0.0704 0.0951  136 LYS A CD  
2144  C CE  . LYS A 136 ? 1.4076 1.2393 1.1103 0.0684  -0.0676 0.0912  136 LYS A CE  
2145  N NZ  . LYS A 136 ? 1.4040 1.2749 1.1502 0.0709  -0.0648 0.0829  136 LYS A NZ  
2159  N N   . LEU A 137 ? 1.4284 1.2156 1.1007 0.0239  -0.0465 0.1124  137 LEU A N   
2160  C CA  . LEU A 137 ? 1.3753 1.2050 1.0866 0.0190  -0.0371 0.1071  137 LEU A CA  
2161  C C   . LEU A 137 ? 1.3589 1.2130 1.0776 0.0235  -0.0315 0.1043  137 LEU A C   
2162  O O   . LEU A 137 ? 1.3535 1.1913 1.0445 0.0243  -0.0305 0.1098  137 LEU A O   
2163  C CB  . LEU A 137 ? 1.3734 1.2097 1.0937 -0.0026 -0.0263 0.1149  137 LEU A CB  
2164  C CG  . LEU A 137 ? 1.3833 1.1974 1.0995 -0.0115 -0.0321 0.1174  137 LEU A CG  
2165  C CD1 . LEU A 137 ? 1.4502 1.2158 1.1273 -0.0068 -0.0436 0.1214  137 LEU A CD1 
2166  C CD2 . LEU A 137 ? 1.4244 1.2485 1.1511 -0.0355 -0.0222 0.1279  137 LEU A CD2 
2178  N N   . GLY A 138 ? 1.2616 1.1514 1.0143 0.0268  -0.0283 0.0960  138 GLY A N   
2179  C CA  . GLY A 138 ? 1.2896 1.2025 1.0500 0.0287  -0.0219 0.0933  138 GLY A CA  
2180  C C   . GLY A 138 ? 1.2581 1.1928 1.0329 0.0137  -0.0052 0.0983  138 GLY A C   
2181  O O   . GLY A 138 ? 1.2167 1.1615 1.0112 0.0038  -0.0015 0.0995  138 GLY A O   
2185  N N   . LEU A 139 ? 1.2501 1.1908 1.0137 0.0131  0.0045  0.1017  139 LEU A N   
2186  C CA  . LEU A 139 ? 1.2152 1.1785 0.9923 0.0011  0.0221  0.1082  139 LEU A CA  
2187  C C   . LEU A 139 ? 1.2115 1.1942 0.9920 0.0095  0.0287  0.1028  139 LEU A C   
2188  O O   . LEU A 139 ? 1.2129 1.1783 0.9637 0.0187  0.0270  0.1028  139 LEU A O   
2189  C CB  . LEU A 139 ? 1.2788 1.2232 1.0312 -0.0105 0.0322  0.1234  139 LEU A CB  
2190  C CG  . LEU A 139 ? 1.2627 1.2327 1.0357 -0.0256 0.0502  0.1336  139 LEU A CG  
2191  C CD1 . LEU A 139 ? 1.3154 1.2655 1.0703 -0.0406 0.0567  0.1503  139 LEU A CD1 
2192  C CD2 . LEU A 139 ? 1.2506 1.2417 1.0239 -0.0181 0.0646  0.1331  139 LEU A CD2 
2204  N N   . VAL A 140 ? 1.1883 1.2031 1.0012 0.0069  0.0353  0.0982  140 VAL A N   
2205  C CA  . VAL A 140 ? 1.1614 1.1940 0.9782 0.0148  0.0416  0.0926  140 VAL A CA  
2206  C C   . VAL A 140 ? 1.1598 1.2191 0.9960 0.0055  0.0602  0.0996  140 VAL A C   
2207  O O   . VAL A 140 ? 1.1414 1.2210 1.0091 -0.0032 0.0612  0.0991  140 VAL A O   
2208  C CB  . VAL A 140 ? 1.1287 1.1755 0.9682 0.0230  0.0296  0.0791  140 VAL A CB  
2209  C CG1 . VAL A 140 ? 1.1358 1.1851 0.9639 0.0334  0.0299  0.0731  140 VAL A CG1 
2210  C CG2 . VAL A 140 ? 1.1238 1.1534 0.9604 0.0290  0.0115  0.0744  140 VAL A CG2 
2220  N N   . ARG A 141 ? 1.1562 1.2151 0.9729 0.0083  0.0750  0.1067  141 ARG A N   
2221  C CA  . ARG A 141 ? 1.1621 1.2485 0.9977 0.0012  0.0947  0.1158  141 ARG A CA  
2222  C C   . ARG A 141 ? 1.1835 1.2905 1.0293 0.0121  0.0999  0.1070  141 ARG A C   
2223  O O   . ARG A 141 ? 1.1892 1.2809 1.0067 0.0257  0.0986  0.1014  141 ARG A O   
2224  C CB  . ARG A 141 ? 1.2014 1.2765 1.0103 -0.0013 0.1112  0.1312  141 ARG A CB  
2225  C CG  . ARG A 141 ? 1.2447 1.2883 1.0303 -0.0087 0.1034  0.1386  141 ARG A CG  
2226  C CD  . ARG A 141 ? 1.2167 1.2566 0.9882 -0.0180 0.1221  0.1577  141 ARG A CD  
2227  N NE  . ARG A 141 ? 1.2293 1.2822 1.0301 -0.0384 0.1232  0.1685  141 ARG A NE  
2228  C CZ  . ARG A 141 ? 1.2509 1.2800 1.0372 -0.0510 0.1196  0.1795  141 ARG A CZ  
2229  N NH1 . ARG A 141 ? 1.2483 1.2400 0.9910 -0.0449 0.1163  0.1818  141 ARG A NH1 
2230  N NH2 . ARG A 141 ? 1.3317 1.3721 1.1461 -0.0704 0.1179  0.1884  141 ARG A NH2 
2244  N N   . PHE A 142 ? 1.2232 1.3613 1.1065 0.0062  0.1042  0.1058  142 PHE A N   
2245  C CA  . PHE A 142 ? 1.2578 1.4166 1.1530 0.0153  0.1105  0.0988  142 PHE A CA  
2246  C C   . PHE A 142 ? 1.3008 1.4874 1.2128 0.0114  0.1320  0.1112  142 PHE A C   
2247  O O   . PHE A 142 ? 1.2808 1.4717 1.1972 0.0001  0.1414  0.1256  142 PHE A O   
2248  C CB  . PHE A 142 ? 1.1698 1.3422 1.0950 0.0138  0.0973  0.0868  142 PHE A CB  
2249  C CG  . PHE A 142 ? 1.1069 1.2588 1.0204 0.0206  0.0784  0.0751  142 PHE A CG  
2250  C CD1 . PHE A 142 ? 1.1183 1.2628 1.0170 0.0331  0.0730  0.0656  142 PHE A CD1 
2251  C CD2 . PHE A 142 ? 1.0996 1.2391 1.0171 0.0149  0.0656  0.0742  142 PHE A CD2 
2252  C CE1 . PHE A 142 ? 1.0902 1.2196 0.9836 0.0380  0.0545  0.0566  142 PHE A CE1 
2253  C CE2 . PHE A 142 ? 1.0742 1.1995 0.9857 0.0223  0.0492  0.0650  142 PHE A CE2 
2254  C CZ  . PHE A 142 ? 1.0513 1.1736 0.9534 0.0329  0.0434  0.0567  142 PHE A CZ  
2264  N N   . SER A 143 ? 1.3823 1.5883 1.3046 0.0208  0.1396  0.1061  143 SER A N   
2265  C CA  . SER A 143 ? 1.3755 1.6136 1.3204 0.0193  0.1596  0.1172  143 SER A CA  
2266  C C   . SER A 143 ? 1.4182 1.6835 1.4089 0.0051  0.1534  0.1178  143 SER A C   
2267  O O   . SER A 143 ? 1.3795 1.6551 1.3872 0.0088  0.1455  0.1065  143 SER A O   
2268  C CB  . SER A 143 ? 1.4532 1.6962 1.3849 0.0379  0.1697  0.1112  143 SER A CB  
2269  O OG  . SER A 143 ? 1.4851 1.6949 1.3682 0.0516  0.1707  0.1083  143 SER A OG  
2275  N N   . GLY A 144 ? 1.4168 1.6906 1.4253 -0.0117 0.1558  0.1313  144 GLY A N   
2276  C CA  . GLY A 144 ? 1.3705 1.6663 1.4191 -0.0263 0.1485  0.1333  144 GLY A CA  
2277  C C   . GLY A 144 ? 1.3609 1.6354 1.4090 -0.0410 0.1311  0.1329  144 GLY A C   
2278  O O   . GLY A 144 ? 1.3751 1.6597 1.4461 -0.0580 0.1287  0.1433  144 GLY A O   
2282  N N   . ILE A 145 ? 1.3320 1.5759 1.3539 -0.0345 0.1181  0.1215  145 ILE A N   
2283  C CA  . ILE A 145 ? 1.3749 1.5957 1.3930 -0.0440 0.1013  0.1190  145 ILE A CA  
2284  C C   . ILE A 145 ? 1.3998 1.5868 1.3803 -0.0374 0.0962  0.1171  145 ILE A C   
2285  O O   . ILE A 145 ? 1.3949 1.5742 1.3547 -0.0230 0.0981  0.1104  145 ILE A O   
2286  C CB  . ILE A 145 ? 1.3715 1.5942 1.4051 -0.0409 0.0875  0.1046  145 ILE A CB  
2287  C CG1 . ILE A 145 ? 1.3329 1.5278 1.3568 -0.0469 0.0717  0.1019  145 ILE A CG1 
2288  C CG2 . ILE A 145 ? 1.3359 1.5587 1.3599 -0.0236 0.0868  0.0913  145 ILE A CG2 
2289  C CD1 . ILE A 145 ? 1.3235 1.5164 1.3570 -0.0410 0.0603  0.0884  145 ILE A CD1 
2301  N N   . ASN A 146 ? 1.2932 1.4574 1.2632 -0.0480 0.0880  0.1232  146 ASN A N   
2302  C CA  . ASN A 146 ? 1.2633 1.3930 1.1981 -0.0424 0.0808  0.1219  146 ASN A CA  
2303  C C   . ASN A 146 ? 1.2144 1.3249 1.1480 -0.0404 0.0624  0.1117  146 ASN A C   
2304  O O   . ASN A 146 ? 1.2243 1.3280 1.1670 -0.0520 0.0554  0.1149  146 ASN A O   
2305  C CB  . ASN A 146 ? 1.2847 1.3991 1.2032 -0.0547 0.0871  0.1385  146 ASN A CB  
2306  C CG  . ASN A 146 ? 1.2619 1.3967 1.1816 -0.0554 0.1085  0.1509  146 ASN A CG  
2307  O OD1 . ASN A 146 ? 1.2109 1.3512 1.1184 -0.0405 0.1172  0.1461  146 ASN A OD1 
2308  N ND2 . ASN A 146 ? 1.3061 1.4512 1.2400 -0.0726 0.1171  0.1677  146 ASN A ND2 
2315  N N   . HIS A 147 ? 1.1546 1.2561 1.0771 -0.0254 0.0544  0.0999  147 HIS A N   
2316  C CA  . HIS A 147 ? 1.1036 1.1894 1.0255 -0.0201 0.0391  0.0911  147 HIS A CA  
2317  C C   . HIS A 147 ? 1.1401 1.1911 1.0313 -0.0182 0.0309  0.0950  147 HIS A C   
2318  O O   . HIS A 147 ? 1.1624 1.2007 1.0292 -0.0132 0.0332  0.0985  147 HIS A O   
2319  C CB  . HIS A 147 ? 1.1064 1.2026 1.0361 -0.0056 0.0340  0.0784  147 HIS A CB  
2320  C CG  . HIS A 147 ? 1.1111 1.2356 1.0705 -0.0064 0.0381  0.0723  147 HIS A CG  
2321  N ND1 . HIS A 147 ? 1.0703 1.2052 1.0496 -0.0169 0.0398  0.0747  147 HIS A ND1 
2322  C CD2 . HIS A 147 ? 1.0663 1.2081 1.0368 0.0020  0.0393  0.0641  147 HIS A CD2 
2323  C CE1 . HIS A 147 ? 1.0641 1.2221 1.0653 -0.0140 0.0426  0.0680  147 HIS A CE1 
2324  N NE2 . HIS A 147 ? 1.0562 1.2188 1.0526 -0.0028 0.0428  0.0616  147 HIS A NE2 
2332  N N   . PHE A 148 ? 1.1695 1.2020 1.0585 -0.0210 0.0208  0.0943  148 PHE A N   
2333  C CA  . PHE A 148 ? 1.1766 1.1738 1.0366 -0.0166 0.0109  0.0965  148 PHE A CA  
2334  C C   . PHE A 148 ? 1.1599 1.1517 1.0241 -0.0015 -0.0008 0.0856  148 PHE A C   
2335  O O   . PHE A 148 ? 1.1403 1.1433 1.0249 -0.0007 -0.0024 0.0798  148 PHE A O   
2336  C CB  . PHE A 148 ? 1.1895 1.1633 1.0378 -0.0316 0.0085  0.1064  148 PHE A CB  
2337  C CG  . PHE A 148 ? 1.2336 1.2081 1.0740 -0.0463 0.0195  0.1204  148 PHE A CG  
2338  C CD1 . PHE A 148 ? 1.2268 1.2338 1.0935 -0.0570 0.0319  0.1257  148 PHE A CD1 
2339  C CD2 . PHE A 148 ? 1.2637 1.2071 1.0712 -0.0489 0.0181  0.1294  148 PHE A CD2 
2340  C CE1 . PHE A 148 ? 1.2502 1.2618 1.1134 -0.0698 0.0440  0.1405  148 PHE A CE1 
2341  C CE2 . PHE A 148 ? 1.2418 1.1868 1.0429 -0.0627 0.0301  0.1441  148 PHE A CE2 
2342  C CZ  . PHE A 148 ? 1.2655 1.2463 1.0959 -0.0731 0.0438  0.1501  148 PHE A CZ  
2352  N N   . ILE A 149 ? 1.1746 1.1494 1.0197 0.0109  -0.0088 0.0838  149 ILE A N   
2353  C CA  . ILE A 149 ? 1.1527 1.1258 1.0047 0.0267  -0.0195 0.0755  149 ILE A CA  
2354  C C   . ILE A 149 ? 1.1637 1.1006 0.9906 0.0308  -0.0285 0.0790  149 ILE A C   
2355  O O   . ILE A 149 ? 1.2700 1.1827 1.0692 0.0334  -0.0333 0.0839  149 ILE A O   
2356  C CB  . ILE A 149 ? 1.1352 1.1176 0.9879 0.0389  -0.0248 0.0709  149 ILE A CB  
2357  C CG1 . ILE A 149 ? 1.1578 1.1653 1.0221 0.0340  -0.0156 0.0693  149 ILE A CG1 
2358  C CG2 . ILE A 149 ? 1.1286 1.1215 1.0019 0.0533  -0.0338 0.0635  149 ILE A CG2 
2359  C CD1 . ILE A 149 ? 1.1087 1.1470 1.0072 0.0335  -0.0114 0.0623  149 ILE A CD1 
2371  N N   . PHE A 150 ? 1.1664 1.0959 0.9990 0.0323  -0.0310 0.0765  150 PHE A N   
2372  C CA  . PHE A 150 ? 1.1774 1.0698 0.9844 0.0395  -0.0400 0.0785  150 PHE A CA  
2373  C C   . PHE A 150 ? 1.1421 1.0419 0.9623 0.0607  -0.0457 0.0712  150 PHE A C   
2374  O O   . PHE A 150 ? 1.1556 1.0729 0.9982 0.0649  -0.0421 0.0657  150 PHE A O   
2375  C CB  . PHE A 150 ? 1.1807 1.0524 0.9783 0.0271  -0.0397 0.0818  150 PHE A CB  
2376  C CG  . PHE A 150 ? 1.2788 1.1055 1.0435 0.0345  -0.0497 0.0838  150 PHE A CG  
2377  C CD1 . PHE A 150 ? 1.2194 1.0377 0.9846 0.0523  -0.0537 0.0773  150 PHE A CD1 
2378  C CD2 . PHE A 150 ? 1.3329 1.1242 1.0643 0.0248  -0.0542 0.0928  150 PHE A CD2 
2379  C CE1 . PHE A 150 ? 1.2415 1.0156 0.9732 0.0619  -0.0625 0.0789  150 PHE A CE1 
2380  C CE2 . PHE A 150 ? 1.3608 1.1065 1.0584 0.0325  -0.0643 0.0944  150 PHE A CE2 
2381  C CZ  . PHE A 150 ? 1.3671 1.1036 1.0641 0.0519  -0.0686 0.0870  150 PHE A CZ  
2391  N N   . ASN A 151 ? 1.1865 1.0739 0.9936 0.0743  -0.0543 0.0719  151 ASN A N   
2392  C CA  . ASN A 151 ? 1.1732 1.0706 0.9960 0.0953  -0.0602 0.0673  151 ASN A CA  
2393  C C   . ASN A 151 ? 1.2334 1.0978 1.0353 0.1064  -0.0640 0.0682  151 ASN A C   
2394  O O   . ASN A 151 ? 1.2556 1.0830 1.0234 0.1084  -0.0711 0.0728  151 ASN A O   
2395  C CB  . ASN A 151 ? 1.2226 1.1222 1.0421 0.1050  -0.0699 0.0683  151 ASN A CB  
2396  C CG  . ASN A 151 ? 1.2140 1.1320 1.0585 0.1255  -0.0767 0.0652  151 ASN A CG  
2397  O OD1 . ASN A 151 ? 1.2513 1.1610 1.0971 0.1385  -0.0763 0.0647  151 ASN A OD1 
2398  N ND2 . ASN A 151 ? 1.2003 1.1427 1.0644 0.1289  -0.0831 0.0638  151 ASN A ND2 
2405  N N   . ILE A 152 ? 1.2422 1.1169 1.0612 0.1146  -0.0591 0.0638  152 ILE A N   
2406  C CA  . ILE A 152 ? 1.2382 1.0779 1.0331 0.1264  -0.0612 0.0640  152 ILE A CA  
2407  C C   . ILE A 152 ? 1.2885 1.1099 1.0685 0.1476  -0.0703 0.0662  152 ILE A C   
2408  O O   . ILE A 152 ? 1.3220 1.0989 1.0632 0.1509  -0.0769 0.0695  152 ILE A O   
2409  C CB  . ILE A 152 ? 1.2229 1.0799 1.0394 0.1351  -0.0528 0.0589  152 ILE A CB  
2410  C CG1 . ILE A 152 ? 1.2195 1.0672 1.0288 0.1164  -0.0479 0.0577  152 ILE A CG1 
2411  C CG2 . ILE A 152 ? 1.2674 1.0994 1.0675 0.1599  -0.0544 0.0586  152 ILE A CG2 
2412  C CD1 . ILE A 152 ? 1.1983 1.0626 1.0164 0.0921  -0.0461 0.0601  152 ILE A CD1 
2424  N N   . LYS A 153 ? 1.2959 1.1507 1.1071 0.1624  -0.0720 0.0649  153 LYS A N   
2425  C CA  . LYS A 153 ? 1.3051 1.1482 1.1090 0.1851  -0.0811 0.0675  153 LYS A CA  
2426  C C   . LYS A 153 ? 1.3384 1.1528 1.1102 0.1799  -0.0925 0.0718  153 LYS A C   
2427  O O   . LYS A 153 ? 1.3663 1.1421 1.1051 0.1917  -0.0998 0.0748  153 LYS A O   
2428  C CB  . LYS A 153 ? 1.3035 1.1940 1.1544 0.1989  -0.0816 0.0666  153 LYS A CB  
2429  C CG  . LYS A 153 ? 1.3218 1.2246 1.1922 0.2212  -0.0741 0.0662  153 LYS A CG  
2430  C CD  . LYS A 153 ? 1.3222 1.2141 1.1834 0.2152  -0.0612 0.0626  153 LYS A CD  
2431  C CE  . LYS A 153 ? 1.3428 1.2641 1.2368 0.2330  -0.0498 0.0620  153 LYS A CE  
2432  N NZ  . LYS A 153 ? 1.3866 1.2721 1.2499 0.2468  -0.0421 0.0608  153 LYS A NZ  
2446  N N   . GLU A 154 ? 1.3431 1.1727 1.1206 0.1634  -0.0938 0.0724  154 GLU A N   
2447  C CA  . GLU A 154 ? 1.3280 1.1309 1.0738 0.1592  -0.1035 0.0770  154 GLU A CA  
2448  C C   . GLU A 154 ? 1.3794 1.1340 1.0793 0.1475  -0.1030 0.0817  154 GLU A C   
2449  O O   . GLU A 154 ? 1.4053 1.1306 1.0730 0.1456  -0.1107 0.0866  154 GLU A O   
2450  C CB  . GLU A 154 ? 1.2458 1.0731 1.0038 0.1446  -0.1026 0.0766  154 GLU A CB  
2451  C CG  . GLU A 154 ? 1.2694 1.1279 1.0566 0.1563  -0.1121 0.0744  154 GLU A CG  
2452  C CD  . GLU A 154 ? 1.3720 1.2330 1.1493 0.1450  -0.1161 0.0752  154 GLU A CD  
2453  O OE1 . GLU A 154 ? 1.3760 1.2326 1.1402 0.1272  -0.1056 0.0761  154 GLU A OE1 
2454  O OE2 . GLU A 154 ? 1.3944 1.2610 1.1764 0.1547  -0.1300 0.0752  154 GLU A OE2 
2461  N N   . ASN A 155 ? 1.3820 1.1257 1.0770 0.1389  -0.0953 0.0808  155 ASN A N   
2462  C CA  . ASN A 155 ? 1.4287 1.1263 1.0827 0.1252  -0.0966 0.0861  155 ASN A CA  
2463  C C   . ASN A 155 ? 1.5028 1.1637 1.1333 0.1406  -0.1009 0.0848  155 ASN A C   
2464  O O   . ASN A 155 ? 1.5471 1.2228 1.1961 0.1615  -0.0993 0.0800  155 ASN A O   
2465  C CB  . ASN A 155 ? 1.4058 1.1158 1.0697 0.0992  -0.0867 0.0873  155 ASN A CB  
2466  C CG  . ASN A 155 ? 1.4256 1.1451 1.0870 0.0809  -0.0830 0.0930  155 ASN A CG  
2467  O OD1 . ASN A 155 ? 1.4457 1.1347 1.0774 0.0658  -0.0838 0.1010  155 ASN A OD1 
2468  N ND2 . ASN A 155 ? 1.3823 1.1426 1.0734 0.0825  -0.0787 0.0894  155 ASN A ND2 
2475  N N   . LYS A 156 ? 1.5794 1.1902 1.1669 0.1303  -0.1060 0.0901  156 LYS A N   
2476  C CA  . LYS A 156 ? 1.6545 1.2202 1.2099 0.1435  -0.1114 0.0891  156 LYS A CA  
2477  C C   . LYS A 156 ? 1.6624 1.2311 1.2267 0.1356  -0.1049 0.0850  156 LYS A C   
2478  O O   . LYS A 156 ? 1.6011 1.1986 1.1899 0.1144  -0.0979 0.0850  156 LYS A O   
2479  C CB  . LYS A 156 ? 1.7025 1.2085 1.2052 0.1337  -0.1214 0.0966  156 LYS A CB  
2480  C CG  . LYS A 156 ? 1.7143 1.2091 1.2079 0.1000  -0.1193 0.1030  156 LYS A CG  
2481  C CD  . LYS A 156 ? 1.7776 1.2124 1.2194 0.0896  -0.1296 0.1120  156 LYS A CD  
2482  C CE  . LYS A 156 ? 1.8135 1.1941 1.2184 0.0893  -0.1381 0.1117  156 LYS A CE  
2483  N NZ  . LYS A 156 ? 1.8560 1.1963 1.2299 0.0592  -0.1445 0.1225  156 LYS A NZ  
2497  N N   . GLU A 157 ? 1.7902 1.3264 1.3317 0.1545  -0.1076 0.0817  157 GLU A N   
2498  C CA  . GLU A 157 ? 1.7692 1.2976 1.3094 0.1500  -0.1034 0.0775  157 GLU A CA  
2499  C C   . GLU A 157 ? 1.7458 1.2554 1.2723 0.1164  -0.1072 0.0824  157 GLU A C   
2500  O O   . GLU A 157 ? 1.7845 1.2577 1.2795 0.1022  -0.1160 0.0897  157 GLU A O   
2501  C CB  . GLU A 157 ? 1.8664 1.3448 1.3668 0.1755  -0.1080 0.0747  157 GLU A CB  
2502  C CG  . GLU A 157 ? 1.8959 1.3411 1.3727 0.1684  -0.1091 0.0717  157 GLU A CG  
2503  C CD  . GLU A 157 ? 1.9503 1.4388 1.4650 0.1748  -0.0962 0.0652  157 GLU A CD  
2504  O OE1 . GLU A 157 ? 1.9597 1.4942 1.5117 0.1939  -0.0864 0.0628  157 GLU A OE1 
2505  O OE2 . GLU A 157 ? 1.9472 1.4234 1.4548 0.1601  -0.0968 0.0632  157 GLU A OE2 
2512  N N   . THR A 158 ? 1.7206 1.2555 1.2720 0.1035  -0.1009 0.0793  158 THR A N   
2513  C CA  . THR A 158 ? 1.7119 1.2348 1.2574 0.0717  -0.1049 0.0846  158 THR A CA  
2514  C C   . THR A 158 ? 1.6791 1.2287 1.2514 0.0658  -0.0988 0.0791  158 THR A C   
2515  O O   . THR A 158 ? 1.6571 1.2446 1.2595 0.0824  -0.0888 0.0721  158 THR A O   
2516  C CB  . THR A 158 ? 1.6784 1.2293 1.2430 0.0491  -0.1017 0.0925  158 THR A CB  
2517  O OG1 . THR A 158 ? 1.6479 1.2012 1.2199 0.0192  -0.1027 0.0982  158 THR A OG1 
2518  C CG2 . THR A 158 ? 1.6144 1.2274 1.2250 0.0575  -0.0898 0.0883  158 THR A CG2 
2526  N N   . SER A 159 ? 1.6365 1.1654 1.1978 0.0413  -0.1058 0.0830  159 SER A N   
2527  C CA  . SER A 159 ? 1.6183 1.1717 1.2047 0.0313  -0.1021 0.0792  159 SER A CA  
2528  C C   . SER A 159 ? 1.5558 1.1675 1.1893 0.0114  -0.0927 0.0830  159 SER A C   
2529  O O   . SER A 159 ? 1.5663 1.1815 1.2013 -0.0066 -0.0937 0.0922  159 SER A O   
2530  C CB  . SER A 159 ? 1.6699 1.1730 1.2233 0.0138  -0.1167 0.0822  159 SER A CB  
2531  O OG  . SER A 159 ? 1.6557 1.1725 1.2259 -0.0193 -0.1205 0.0920  159 SER A OG  
2537  N N   . PHE A 160 ? 1.4924 1.1482 1.1622 0.0164  -0.0828 0.0764  160 PHE A N   
2538  C CA  . PHE A 160 ? 1.4625 1.1707 1.1746 -0.0010 -0.0741 0.0791  160 PHE A CA  
2539  C C   . PHE A 160 ? 1.4972 1.1954 1.2065 -0.0312 -0.0807 0.0898  160 PHE A C   
2540  O O   . PHE A 160 ? 1.4903 1.2147 1.2175 -0.0452 -0.0747 0.0975  160 PHE A O   
2541  C CB  . PHE A 160 ? 1.4593 1.2001 1.2004 0.0045  -0.0669 0.0710  160 PHE A CB  
2542  C CG  . PHE A 160 ? 1.3726 1.1453 1.1348 0.0283  -0.0563 0.0634  160 PHE A CG  
2543  C CD1 . PHE A 160 ? 1.3681 1.1280 1.1159 0.0487  -0.0567 0.0623  160 PHE A CD1 
2544  C CD2 . PHE A 160 ? 1.3121 1.1275 1.1098 0.0298  -0.0470 0.0581  160 PHE A CD2 
2545  C CE1 . PHE A 160 ? 1.2960 1.0880 1.0680 0.0690  -0.0484 0.0570  160 PHE A CE1 
2546  C CE2 . PHE A 160 ? 1.3156 1.1603 1.1347 0.0493  -0.0384 0.0525  160 PHE A CE2 
2547  C CZ  . PHE A 160 ? 1.2963 1.1307 1.1043 0.0684  -0.0393 0.0524  160 PHE A CZ  
2557  N N   . GLU A 161 ? 1.5463 1.2046 1.2317 -0.0415 -0.0935 0.0913  161 GLU A N   
2558  C CA  . GLU A 161 ? 1.5555 1.2083 1.2451 -0.0726 -0.1016 0.1024  161 GLU A CA  
2559  C C   . GLU A 161 ? 1.5555 1.1963 1.2331 -0.0862 -0.1026 0.1147  161 GLU A C   
2560  O O   . GLU A 161 ? 1.5641 1.2318 1.2660 -0.1089 -0.0986 0.1256  161 GLU A O   
2561  C CB  . GLU A 161 ? 1.5706 1.1708 1.2274 -0.0795 -0.1195 0.1016  161 GLU A CB  
2562  C CG  . GLU A 161 ? 1.6013 1.2043 1.2616 -0.0654 -0.1192 0.0899  161 GLU A CG  
2563  C CD  . GLU A 161 ? 1.5984 1.1934 1.2429 -0.0311 -0.1110 0.0785  161 GLU A CD  
2564  O OE1 . GLU A 161 ? 1.6006 1.1799 1.2265 -0.0180 -0.1092 0.0794  161 GLU A OE1 
2565  O OE2 . GLU A 161 ? 1.4971 1.1033 1.1496 -0.0171 -0.1058 0.0695  161 GLU A OE2 
2572  N N   . ASN A 162 ? 1.5521 1.1527 1.1918 -0.0717 -0.1073 0.1138  162 ASN A N   
2573  C CA  . ASN A 162 ? 1.5998 1.1863 1.2241 -0.0822 -0.1077 0.1251  162 ASN A CA  
2574  C C   . ASN A 162 ? 1.5670 1.2085 1.2265 -0.0836 -0.0909 0.1284  162 ASN A C   
2575  O O   . ASN A 162 ? 1.5944 1.2414 1.2568 -0.1023 -0.0873 0.1411  162 ASN A O   
2576  C CB  . ASN A 162 ? 1.6344 1.1720 1.2136 -0.0604 -0.1147 0.1212  162 ASN A CB  
2577  C CG  . ASN A 162 ? 1.6566 1.1713 1.2127 -0.0704 -0.1169 0.1329  162 ASN A CG  
2578  O OD1 . ASN A 162 ? 1.6683 1.1784 1.2110 -0.0517 -0.1137 0.1305  162 ASN A OD1 
2579  N ND2 . ASN A 162 ? 1.7048 1.2041 1.2561 -0.1004 -0.1230 0.1463  162 ASN A ND2 
2586  N N   . ILE A 163 ? 1.5557 1.2366 1.2407 -0.0638 -0.0803 0.1176  163 ILE A N   
2587  C CA  . ILE A 163 ? 1.5153 1.2423 1.2276 -0.0624 -0.0660 0.1193  163 ILE A CA  
2588  C C   . ILE A 163 ? 1.5118 1.2815 1.2618 -0.0826 -0.0572 0.1251  163 ILE A C   
2589  O O   . ILE A 163 ? 1.5173 1.3082 1.2782 -0.0938 -0.0476 0.1346  163 ILE A O   
2590  C CB  . ILE A 163 ? 1.4151 1.1665 1.1409 -0.0355 -0.0602 0.1065  163 ILE A CB  
2591  C CG1 . ILE A 163 ? 1.4586 1.1718 1.1552 -0.0134 -0.0695 0.0994  163 ILE A CG1 
2592  C CG2 . ILE A 163 ? 1.4186 1.1932 1.1511 -0.0299 -0.0518 0.1086  163 ILE A CG2 
2593  C CD1 . ILE A 163 ? 1.5447 1.2106 1.1997 -0.0114 -0.0784 0.1057  163 ILE A CD1 
2605  N N   . ILE A 164 ? 1.5430 1.3256 1.3126 -0.0859 -0.0596 0.1197  164 ILE A N   
2606  C CA  . ILE A 164 ? 1.4815 1.3045 1.2880 -0.1042 -0.0527 0.1255  164 ILE A CA  
2607  C C   . ILE A 164 ? 1.5177 1.3307 1.3213 -0.1309 -0.0552 0.1427  164 ILE A C   
2608  O O   . ILE A 164 ? 1.4870 1.3376 1.3185 -0.1432 -0.0434 0.1522  164 ILE A O   
2609  C CB  . ILE A 164 ? 1.5445 1.3719 1.3648 -0.1047 -0.0591 0.1179  164 ILE A CB  
2610  C CG1 . ILE A 164 ? 1.5204 1.3418 1.3322 -0.0779 -0.0589 0.1026  164 ILE A CG1 
2611  C CG2 . ILE A 164 ? 1.5110 1.3908 1.3753 -0.1155 -0.0491 0.1206  164 ILE A CG2 
2612  C CD1 . ILE A 164 ? 1.4510 1.2786 1.2752 -0.0759 -0.0623 0.0946  164 ILE A CD1 
2624  N N   . ASP A 165 ? 1.5860 1.3474 1.3555 -0.1398 -0.0704 0.1479  165 ASP A N   
2625  C CA  . ASP A 165 ? 1.6149 1.3627 1.3797 -0.1666 -0.0740 0.1659  165 ASP A CA  
2626  C C   . ASP A 165 ? 1.5978 1.3492 1.3521 -0.1647 -0.0618 0.1742  165 ASP A C   
2627  O O   . ASP A 165 ? 1.5978 1.3739 1.3712 -0.1826 -0.0516 0.1889  165 ASP A O   
2628  C CB  . ASP A 165 ? 1.6898 1.3745 1.4152 -0.1760 -0.0955 0.1685  165 ASP A CB  
2629  C CG  . ASP A 165 ? 1.6805 1.3617 1.4197 -0.1931 -0.1092 0.1697  165 ASP A CG  
2630  O OD1 . ASP A 165 ? 1.6581 1.3743 1.4263 -0.1855 -0.1044 0.1605  165 ASP A OD1 
2631  O OD2 . ASP A 165 ? 1.7125 1.3540 1.4322 -0.2146 -0.1260 0.1800  165 ASP A OD2 
2636  N N   . LEU A 166 ? 1.5892 1.3164 1.3130 -0.1424 -0.0626 0.1656  166 LEU A N   
2637  C CA  . LEU A 166 ? 1.5858 1.3098 1.2933 -0.1391 -0.0534 0.1728  166 LEU A CA  
2638  C C   . LEU A 166 ? 1.5500 1.3291 1.2909 -0.1375 -0.0335 0.1749  166 LEU A C   
2639  O O   . LEU A 166 ? 1.5483 1.3361 1.2891 -0.1492 -0.0226 0.1887  166 LEU A O   
2640  C CB  . LEU A 166 ? 1.6204 1.3136 1.2943 -0.1126 -0.0593 0.1615  166 LEU A CB  
2641  C CG  . LEU A 166 ? 1.6862 1.3153 1.3125 -0.1132 -0.0753 0.1649  166 LEU A CG  
2642  C CD1 . LEU A 166 ? 1.6925 1.3007 1.2939 -0.0828 -0.0801 0.1526  166 LEU A CD1 
2643  C CD2 . LEU A 166 ? 1.7278 1.3353 1.3339 -0.1333 -0.0738 0.1826  166 LEU A CD2 
2655  N N   . VAL A 167 ? 1.5483 1.3628 1.3153 -0.1222 -0.0282 0.1616  167 VAL A N   
2656  C CA  . VAL A 167 ? 1.5096 1.3738 1.3066 -0.1201 -0.0105 0.1627  167 VAL A CA  
2657  C C   . VAL A 167 ? 1.5191 1.4085 1.3427 -0.1448 -0.0022 0.1786  167 VAL A C   
2658  O O   . VAL A 167 ? 1.5415 1.4442 1.3662 -0.1518 0.0117  0.1911  167 VAL A O   
2659  C CB  . VAL A 167 ? 1.4148 1.3097 1.2367 -0.1031 -0.0087 0.1466  167 VAL A CB  
2660  C CG1 . VAL A 167 ? 1.3608 1.3031 1.2112 -0.1017 0.0084  0.1478  167 VAL A CG1 
2661  C CG2 . VAL A 167 ? 1.4020 1.2777 1.2028 -0.0790 -0.0154 0.1336  167 VAL A CG2 
2671  N N   . LYS A 168 ? 1.5147 1.4091 1.3590 -0.1583 -0.0110 0.1793  168 LYS A N   
2672  C CA  . LYS A 168 ? 1.5155 1.4350 1.3901 -0.1833 -0.0065 0.1954  168 LYS A CA  
2673  C C   . LYS A 168 ? 1.5330 1.4365 1.3925 -0.2008 -0.0017 0.2151  168 LYS A C   
2674  O O   . LYS A 168 ? 1.5113 1.4478 1.3985 -0.2164 0.0115  0.2310  168 LYS A O   
2675  C CB  . LYS A 168 ? 1.4588 1.3647 1.3428 -0.1974 -0.0249 0.1943  168 LYS A CB  
2676  C CG  . LYS A 168 ? 1.4392 1.3793 1.3550 -0.1892 -0.0243 0.1824  168 LYS A CG  
2677  C CD  . LYS A 168 ? 1.4929 1.4134 1.4123 -0.2038 -0.0443 0.1821  168 LYS A CD  
2678  C CE  . LYS A 168 ? 1.4623 1.4276 1.4248 -0.2068 -0.0414 0.1797  168 LYS A CE  
2679  N NZ  . LYS A 168 ? 1.4911 1.4449 1.4649 -0.2307 -0.0600 0.1883  168 LYS A NZ  
2693  N N   . LYS A 169 ? 1.6082 1.4610 1.4238 -0.1977 -0.0115 0.2149  169 LYS A N   
2694  C CA  . LYS A 169 ? 1.6069 1.4397 1.4025 -0.2128 -0.0064 0.2334  169 LYS A CA  
2695  C C   . LYS A 169 ? 1.6193 1.4733 1.4098 -0.1995 0.0151  0.2363  169 LYS A C   
2696  O O   . LYS A 169 ? 1.6453 1.5111 1.4404 -0.2135 0.0295  0.2547  169 LYS A O   
2697  C CB  . LYS A 169 ? 1.6654 1.4331 1.4117 -0.2121 -0.0248 0.2318  169 LYS A CB  
2698  C CG  . LYS A 169 ? 1.7176 1.4530 1.4571 -0.2412 -0.0403 0.2465  169 LYS A CG  
2699  C CD  . LYS A 169 ? 1.7413 1.4931 1.4955 -0.2669 -0.0275 0.2716  169 LYS A CD  
2700  C CE  . LYS A 169 ? 1.8043 1.5377 1.5243 -0.2587 -0.0148 0.2784  169 LYS A CE  
2701  N NZ  . LYS A 169 ? 1.7759 1.5372 1.5163 -0.2797 0.0045  0.3027  169 LYS A NZ  
2715  N N   . TYR A 170 ? 1.5774 1.4352 1.3572 -0.1727 0.0174  0.2190  170 TYR A N   
2716  C CA  . TYR A 170 ? 1.5495 1.4216 1.3190 -0.1587 0.0349  0.2201  170 TYR A CA  
2717  C C   . TYR A 170 ? 1.5514 1.4758 1.3582 -0.1652 0.0562  0.2297  170 TYR A C   
2718  O O   . TYR A 170 ? 1.6156 1.5466 1.4137 -0.1679 0.0735  0.2433  170 TYR A O   
2719  C CB  . TYR A 170 ? 1.5102 1.3799 1.2679 -0.1306 0.0299  0.1994  170 TYR A CB  
2720  C CG  . TYR A 170 ? 1.4947 1.3693 1.2336 -0.1143 0.0425  0.1982  170 TYR A CG  
2721  C CD1 . TYR A 170 ? 1.4781 1.3936 1.2389 -0.1103 0.0609  0.1997  170 TYR A CD1 
2722  C CD2 . TYR A 170 ? 1.4879 1.3231 1.1844 -0.1015 0.0349  0.1951  170 TYR A CD2 
2723  C CE1 . TYR A 170 ? 1.4222 1.3359 1.1596 -0.0945 0.0710  0.1981  170 TYR A CE1 
2724  C CE2 . TYR A 170 ? 1.4020 1.2371 1.0775 -0.0865 0.0438  0.1937  170 TYR A CE2 
2725  C CZ  . TYR A 170 ? 1.3843 1.2571 1.0788 -0.0832 0.0616  0.1950  170 TYR A CZ  
2726  O OH  . TYR A 170 ? 1.4346 1.3017 1.1026 -0.0676 0.0692  0.1931  170 TYR A OH  
2736  N N   . LEU A 171 ? 1.5220 1.4828 1.3686 -0.1665 0.0559  0.2234  171 LEU A N   
2737  C CA  . LEU A 171 ? 1.5666 1.5785 1.4514 -0.1712 0.0752  0.2322  171 LEU A CA  
2738  C C   . LEU A 171 ? 1.5969 1.6239 1.5098 -0.1998 0.0777  0.2537  171 LEU A C   
2739  O O   . LEU A 171 ? 1.6198 1.6928 1.5748 -0.2060 0.0886  0.2604  171 LEU A O   
2740  C CB  . LEU A 171 ? 1.5460 1.5904 1.4609 -0.1590 0.0733  0.2159  171 LEU A CB  
2741  C CG  . LEU A 171 ? 1.5043 1.5349 1.4003 -0.1346 0.0649  0.1940  171 LEU A CG  
2742  C CD1 . LEU A 171 ? 1.4589 1.4641 1.3514 -0.1358 0.0431  0.1830  171 LEU A CD1 
2743  C CD2 . LEU A 171 ? 1.4927 1.5628 1.4125 -0.1197 0.0757  0.1839  171 LEU A CD2 
2755  N N   . SER A 172 ? 1.5936 1.5826 1.4852 -0.2176 0.0668  0.2651  172 SER A N   
2756  C CA  . SER A 172 ? 1.6337 1.6353 1.5528 -0.2475 0.0672  0.2875  172 SER A CA  
2757  C C   . SER A 172 ? 1.6872 1.7304 1.6284 -0.2519 0.0956  0.3071  172 SER A C   
2758  O O   . SER A 172 ? 1.6816 1.7700 1.6706 -0.2656 0.1037  0.3198  172 SER A O   
2759  C CB  . SER A 172 ? 1.6606 1.6070 1.5449 -0.2648 0.0503  0.2963  172 SER A CB  
2760  O OG  . SER A 172 ? 1.6986 1.6233 1.5479 -0.2614 0.0633  0.3063  172 SER A OG  
2766  N N   . ASN A 173 ? 1.7177 1.7458 1.6239 -0.2392 0.1112  0.3102  173 ASN A N   
2767  C CA  . ASN A 173 ? 1.7158 1.7781 1.6337 -0.2382 0.1412  0.3280  173 ASN A CA  
2768  C C   . ASN A 173 ? 1.7162 1.8028 1.6311 -0.2085 0.1570  0.3132  173 ASN A C   
2769  O O   . ASN A 173 ? 1.7332 1.8139 1.6190 -0.1941 0.1756  0.3167  173 ASN A O   
2770  C CB  . ASN A 173 ? 1.7649 1.7901 1.6411 -0.2447 0.1491  0.3437  173 ASN A CB  
2771  C CG  . ASN A 173 ? 1.8017 1.8123 1.6887 -0.2783 0.1393  0.3651  173 ASN A CG  
2772  O OD1 . ASN A 173 ? 1.7989 1.7775 1.6794 -0.2899 0.1124  0.3582  173 ASN A OD1 
2773  N ND2 . ASN A 173 ? 1.8134 1.8460 1.7159 -0.2939 0.1612  0.3920  173 ASN A ND2 
2780  N N   . GLU A 174 ? 1.6825 1.7931 1.6243 -0.1992 0.1486  0.2963  174 GLU A N   
2781  C CA  . GLU A 174 ? 1.6817 1.8144 1.6229 -0.1727 0.1605  0.2814  174 GLU A CA  
2782  C C   . GLU A 174 ? 1.6463 1.8223 1.6374 -0.1744 0.1575  0.2755  174 GLU A C   
2783  O O   . GLU A 174 ? 1.6271 1.7942 1.6301 -0.1815 0.1355  0.2651  174 GLU A O   
2784  C CB  . GLU A 174 ? 1.6964 1.7898 1.5947 -0.1516 0.1461  0.2588  174 GLU A CB  
2785  C CG  . GLU A 174 ? 1.7019 1.8148 1.6108 -0.1304 0.1440  0.2379  174 GLU A CG  
2786  C CD  . GLU A 174 ? 1.6934 1.8381 1.6078 -0.1155 0.1684  0.2410  174 GLU A CD  
2787  O OE1 . GLU A 174 ? 1.7201 1.8757 1.6330 -0.1208 0.1894  0.2602  174 GLU A OE1 
2788  O OE2 . GLU A 174 ? 1.6466 1.8040 1.5656 -0.0980 0.1671  0.2246  174 GLU A OE2 
2795  N N   . GLU A 175 ? 1.6518 1.8721 1.6690 -0.1665 0.1797  0.2822  175 GLU A N   
2796  C CA  . GLU A 175 ? 1.6096 1.8732 1.6752 -0.1675 0.1784  0.2786  175 GLU A CA  
2797  C C   . GLU A 175 ? 1.5976 1.8577 1.6525 -0.1441 0.1707  0.2528  175 GLU A C   
2798  O O   . GLU A 175 ? 1.6187 1.8695 1.6435 -0.1225 0.1811  0.2440  175 GLU A O   
2799  C CB  . GLU A 175 ? 1.5757 1.8895 1.6751 -0.1674 0.2061  0.2978  175 GLU A CB  
2800  C CG  . GLU A 175 ? 1.5688 1.8970 1.6932 -0.1941 0.2135  0.3262  175 GLU A CG  
2801  C CD  . GLU A 175 ? 1.5414 1.8740 1.7019 -0.2208 0.1888  0.3302  175 GLU A CD  
2802  O OE1 . GLU A 175 ? 1.5381 1.8809 1.7181 -0.2166 0.1735  0.3145  175 GLU A OE1 
2803  O OE2 . GLU A 175 ? 1.4946 1.8172 1.6611 -0.2460 0.1840  0.3492  175 GLU A OE2 
2810  N N   . TYR A 176 ? 1.5567 1.8224 1.6352 -0.1490 0.1518  0.2413  176 TYR A N   
2811  C CA  . TYR A 176 ? 1.5558 1.8190 1.6283 -0.1298 0.1433  0.2181  176 TYR A CA  
2812  C C   . TYR A 176 ? 1.5028 1.7958 1.6183 -0.1367 0.1345  0.2148  176 TYR A C   
2813  O O   . TYR A 176 ? 1.4860 1.7886 1.6287 -0.1581 0.1266  0.2270  176 TYR A O   
2814  C CB  . TYR A 176 ? 1.5558 1.7723 1.5919 -0.1246 0.1233  0.2024  176 TYR A CB  
2815  C CG  . TYR A 176 ? 1.5393 1.7337 1.5798 -0.1441 0.1027  0.2048  176 TYR A CG  
2816  C CD1 . TYR A 176 ? 1.4952 1.6932 1.5552 -0.1467 0.0867  0.1940  176 TYR A CD1 
2817  C CD2 . TYR A 176 ? 1.5660 1.7321 1.5873 -0.1594 0.0989  0.2181  176 TYR A CD2 
2818  C CE1 . TYR A 176 ? 1.4905 1.6627 1.5484 -0.1631 0.0672  0.1959  176 TYR A CE1 
2819  C CE2 . TYR A 176 ? 1.5516 1.6919 1.5719 -0.1768 0.0786  0.2201  176 TYR A CE2 
2820  C CZ  . TYR A 176 ? 1.5191 1.6617 1.5566 -0.1781 0.0627  0.2087  176 TYR A CZ  
2821  O OH  . TYR A 176 ? 1.5135 1.6248 1.5440 -0.1939 0.0418  0.2102  176 TYR A OH  
2831  N N   . SER A 177 ? 1.4899 1.7952 1.6097 -0.1190 0.1346  0.1985  177 SER A N   
2832  C CA  . SER A 177 ? 1.4742 1.8017 1.6283 -0.1226 0.1244  0.1923  177 SER A CA  
2833  C C   . SER A 177 ? 1.4747 1.7704 1.6155 -0.1239 0.1009  0.1764  177 SER A C   
2834  O O   . SER A 177 ? 1.5027 1.8035 1.6659 -0.1353 0.0873  0.1759  177 SER A O   
2835  C CB  . SER A 177 ? 1.4427 1.7989 1.6078 -0.1028 0.1371  0.1838  177 SER A CB  
2836  O OG  . SER A 177 ? 1.4110 1.7893 1.5772 -0.0955 0.1612  0.1966  177 SER A OG  
2842  N N   . ALA A 178 ? 1.4453 1.7077 1.5496 -0.1118 0.0957  0.1640  178 ALA A N   
2843  C CA  . ALA A 178 ? 1.4215 1.6536 1.5112 -0.1098 0.0762  0.1498  178 ALA A CA  
2844  C C   . ALA A 178 ? 1.3858 1.5857 1.4370 -0.0971 0.0744  0.1421  178 ALA A C   
2845  O O   . ALA A 178 ? 1.3736 1.5767 1.4101 -0.0866 0.0869  0.1434  178 ALA A O   
2846  C CB  . ALA A 178 ? 1.4048 1.6523 1.5114 -0.0996 0.0716  0.1353  178 ALA A CB  
2852  N N   . PHE A 179 ? 1.3719 1.5393 1.4054 -0.0972 0.0582  0.1344  179 PHE A N   
2853  C CA  . PHE A 179 ? 1.3444 1.4817 1.3448 -0.0844 0.0536  0.1268  179 PHE A CA  
2854  C C   . PHE A 179 ? 1.2959 1.4172 1.2926 -0.0756 0.0395  0.1123  179 PHE A C   
2855  O O   . PHE A 179 ? 1.3057 1.4309 1.3184 -0.0813 0.0325  0.1093  179 PHE A O   
2856  C CB  . PHE A 179 ? 1.3393 1.4461 1.3138 -0.0943 0.0509  0.1383  179 PHE A CB  
2857  C CG  . PHE A 179 ? 1.3727 1.4551 1.3447 -0.1095 0.0362  0.1425  179 PHE A CG  
2858  C CD1 . PHE A 179 ? 1.3258 1.3738 1.2757 -0.1021 0.0214  0.1327  179 PHE A CD1 
2859  C CD2 . PHE A 179 ? 1.4202 1.5130 1.4112 -0.1309 0.0367  0.1571  179 PHE A CD2 
2860  C CE1 . PHE A 179 ? 1.3677 1.3869 1.3087 -0.1146 0.0072  0.1361  179 PHE A CE1 
2861  C CE2 . PHE A 179 ? 1.4215 1.4866 1.4064 -0.1459 0.0204  0.1609  179 PHE A CE2 
2862  C CZ  . PHE A 179 ? 1.3960 1.4217 1.3529 -0.1372 0.0056  0.1498  179 PHE A CZ  
2872  N N   . GLY A 180 ? 1.2255 1.3286 1.2006 -0.0608 0.0355  0.1039  180 GLY A N   
2873  C CA  . GLY A 180 ? 1.2021 1.2915 1.1740 -0.0502 0.0245  0.0918  180 GLY A CA  
2874  C C   . GLY A 180 ? 1.1741 1.2308 1.1172 -0.0411 0.0163  0.0899  180 GLY A C   
2875  O O   . GLY A 180 ? 1.1965 1.2479 1.1237 -0.0354 0.0192  0.0920  180 GLY A O   
2879  N N   . ILE A 181 ? 1.1959 1.2285 1.1296 -0.0386 0.0056  0.0860  181 ILE A N   
2880  C CA  . ILE A 181 ? 1.1666 1.1694 1.0753 -0.0264 -0.0027 0.0832  181 ILE A CA  
2881  C C   . ILE A 181 ? 1.1473 1.1595 1.0677 -0.0092 -0.0052 0.0714  181 ILE A C   
2882  O O   . ILE A 181 ? 1.1343 1.1497 1.0659 -0.0086 -0.0065 0.0666  181 ILE A O   
2883  C CB  . ILE A 181 ? 1.2157 1.1794 1.1004 -0.0339 -0.0123 0.0885  181 ILE A CB  
2884  C CG1 . ILE A 181 ? 1.2517 1.2068 1.1269 -0.0530 -0.0099 0.1021  181 ILE A CG1 
2885  C CG2 . ILE A 181 ? 1.2210 1.1545 1.0800 -0.0178 -0.0205 0.0849  181 ILE A CG2 
2886  C CD1 . ILE A 181 ? 1.2982 1.2655 1.1927 -0.0721 -0.0091 0.1083  181 ILE A CD1 
2898  N N   . MET A 182 ? 1.1250 1.1415 1.0429 0.0043  -0.0062 0.0677  182 MET A N   
2899  C CA  . MET A 182 ? 1.0802 1.1086 1.0126 0.0202  -0.0088 0.0588  182 MET A CA  
2900  C C   . MET A 182 ? 1.0930 1.0932 1.0061 0.0329  -0.0174 0.0587  182 MET A C   
2901  O O   . MET A 182 ? 1.1164 1.1076 1.0169 0.0404  -0.0223 0.0603  182 MET A O   
2902  C CB  . MET A 182 ? 1.0547 1.1080 1.0003 0.0259  -0.0064 0.0554  182 MET A CB  
2903  C CG  . MET A 182 ? 1.0570 1.1315 1.0123 0.0149  0.0029  0.0573  182 MET A CG  
2904  S SD  . MET A 182 ? 1.0947 1.1864 1.0725 0.0045  0.0091  0.0559  182 MET A SD  
2905  C CE  . MET A 182 ? 0.9783 1.0909 0.9799 0.0169  0.0083  0.0454  182 MET A CE  
2915  N N   . PHE A 183 ? 1.1064 1.0901 1.0145 0.0364  -0.0197 0.0568  183 PHE A N   
2916  C CA  . PHE A 183 ? 1.1096 1.0655 0.9985 0.0516  -0.0265 0.0564  183 PHE A CA  
2917  C C   . PHE A 183 ? 1.0543 1.0329 0.9650 0.0701  -0.0261 0.0512  183 PHE A C   
2918  O O   . PHE A 183 ? 1.0515 1.0482 0.9829 0.0755  -0.0210 0.0466  183 PHE A O   
2919  C CB  . PHE A 183 ? 1.1737 1.1017 1.0464 0.0507  -0.0285 0.0558  183 PHE A CB  
2920  C CG  . PHE A 183 ? 1.2078 1.1117 1.0606 0.0307  -0.0320 0.0624  183 PHE A CG  
2921  C CD1 . PHE A 183 ? 1.1993 1.0663 1.0198 0.0280  -0.0394 0.0686  183 PHE A CD1 
2922  C CD2 . PHE A 183 ? 1.2189 1.1374 1.0864 0.0141  -0.0286 0.0632  183 PHE A CD2 
2923  C CE1 . PHE A 183 ? 1.2371 1.0825 1.0415 0.0075  -0.0432 0.0763  183 PHE A CE1 
2924  C CE2 . PHE A 183 ? 1.2576 1.1575 1.1120 -0.0058 -0.0329 0.0711  183 PHE A CE2 
2925  C CZ  . PHE A 183 ? 1.3037 1.1671 1.1270 -0.0099 -0.0401 0.0780  183 PHE A CZ  
2935  N N   . PHE A 184 ? 1.0629 1.0402 0.9694 0.0795  -0.0320 0.0529  184 PHE A N   
2936  C CA  . PHE A 184 ? 1.0710 1.0752 1.0035 0.0934  -0.0339 0.0499  184 PHE A CA  
2937  C C   . PHE A 184 ? 1.0690 1.0583 0.9953 0.1136  -0.0390 0.0509  184 PHE A C   
2938  O O   . PHE A 184 ? 1.1188 1.0771 1.0163 0.1178  -0.0459 0.0546  184 PHE A O   
2939  C CB  . PHE A 184 ? 1.0449 1.0599 0.9787 0.0893  -0.0390 0.0512  184 PHE A CB  
2940  C CG  . PHE A 184 ? 1.0469 1.0816 1.0019 0.1030  -0.0465 0.0499  184 PHE A CG  
2941  C CD1 . PHE A 184 ? 1.0457 1.1135 1.0361 0.1060  -0.0432 0.0463  184 PHE A CD1 
2942  C CD2 . PHE A 184 ? 1.1013 1.1211 1.0417 0.1120  -0.0579 0.0531  184 PHE A CD2 
2943  C CE1 . PHE A 184 ? 1.0830 1.1708 1.0968 0.1165  -0.0516 0.0467  184 PHE A CE1 
2944  C CE2 . PHE A 184 ? 1.0941 1.1335 1.0573 0.1236  -0.0673 0.0529  184 PHE A CE2 
2945  C CZ  . PHE A 184 ? 1.0814 1.1559 1.0830 0.1252  -0.0643 0.0501  184 PHE A CZ  
2955  N N   . ASP A 185 ? 1.0505 1.0621 1.0037 0.1266  -0.0349 0.0486  185 ASP A N   
2956  C CA  . ASP A 185 ? 1.1164 1.1217 1.0707 0.1489  -0.0371 0.0505  185 ASP A CA  
2957  C C   . ASP A 185 ? 1.1109 1.1509 1.0999 0.1580  -0.0424 0.0519  185 ASP A C   
2958  O O   . ASP A 185 ? 1.0517 1.1262 1.0750 0.1561  -0.0375 0.0503  185 ASP A O   
2959  C CB  . ASP A 185 ? 1.1235 1.1256 1.0804 0.1585  -0.0266 0.0485  185 ASP A CB  
2960  C CG  . ASP A 185 ? 1.2034 1.1913 1.1529 0.1838  -0.0267 0.0513  185 ASP A CG  
2961  O OD1 . ASP A 185 ? 1.2342 1.2366 1.1993 0.1958  -0.0332 0.0548  185 ASP A OD1 
2962  O OD2 . ASP A 185 ? 1.3109 1.2718 1.2378 0.1925  -0.0207 0.0503  185 ASP A OD2 
2967  N N   . SER A 186 ? 1.1533 1.1825 1.1328 0.1676  -0.0538 0.0555  186 SER A N   
2968  C CA  . SER A 186 ? 1.1423 1.2017 1.1531 0.1741  -0.0633 0.0576  186 SER A CA  
2969  C C   . SER A 186 ? 1.1473 1.2349 1.1949 0.1926  -0.0588 0.0605  186 SER A C   
2970  O O   . SER A 186 ? 1.1443 1.2691 1.2315 0.1923  -0.0620 0.0620  186 SER A O   
2971  C CB  . SER A 186 ? 1.1554 1.1919 1.1425 0.1795  -0.0783 0.0610  186 SER A CB  
2972  O OG  . SER A 186 ? 1.2167 1.2216 1.1647 0.1645  -0.0795 0.0601  186 SER A OG  
2978  N N   . ASP A 187 ? 1.1417 1.2112 1.1760 0.2092  -0.0515 0.0621  187 ASP A N   
2979  C CA  . ASP A 187 ? 1.1716 1.2679 1.2395 0.2296  -0.0441 0.0663  187 ASP A CA  
2980  C C   . ASP A 187 ? 1.1594 1.2931 1.2647 0.2218  -0.0330 0.0652  187 ASP A C   
2981  O O   . ASP A 187 ? 1.1626 1.3332 1.3103 0.2323  -0.0302 0.0705  187 ASP A O   
2982  C CB  . ASP A 187 ? 1.2228 1.2863 1.2609 0.2484  -0.0347 0.0669  187 ASP A CB  
2983  C CG  . ASP A 187 ? 1.2823 1.3143 1.2917 0.2634  -0.0457 0.0701  187 ASP A CG  
2984  O OD1 . ASP A 187 ? 1.2834 1.3167 1.2930 0.2577  -0.0608 0.0716  187 ASP A OD1 
2985  O OD2 . ASP A 187 ? 1.3407 1.3430 1.3235 0.2818  -0.0396 0.0709  187 ASP A OD2 
2990  N N   . ASN A 188 ? 1.1286 1.2539 1.2200 0.2033  -0.0267 0.0592  188 ASN A N   
2991  C CA  . ASN A 188 ? 1.0955 1.2487 1.2144 0.1959  -0.0154 0.0574  188 ASN A CA  
2992  C C   . ASN A 188 ? 1.0499 1.2202 1.1810 0.1739  -0.0214 0.0538  188 ASN A C   
2993  O O   . ASN A 188 ? 1.0152 1.2128 1.1743 0.1679  -0.0149 0.0531  188 ASN A O   
2994  C CB  . ASN A 188 ? 1.0652 1.1925 1.1565 0.1955  -0.0022 0.0534  188 ASN A CB  
2995  C CG  . ASN A 188 ? 1.1495 1.3003 1.2667 0.2028  0.0130  0.0545  188 ASN A CG  
2996  O OD1 . ASN A 188 ? 1.1914 1.3772 1.3479 0.2127  0.0157  0.0603  188 ASN A OD1 
2997  N ND2 . ASN A 188 ? 1.1644 1.2957 1.2598 0.1977  0.0224  0.0499  188 ASN A ND2 
3004  N N   . LEU A 189 ? 1.0628 1.2164 1.1717 0.1629  -0.0329 0.0519  189 LEU A N   
3005  C CA  . LEU A 189 ? 1.0398 1.2012 1.1494 0.1433  -0.0361 0.0479  189 LEU A CA  
3006  C C   . LEU A 189 ? 0.9815 1.1395 1.0841 0.1325  -0.0231 0.0433  189 LEU A C   
3007  O O   . LEU A 189 ? 0.9212 1.1015 1.0445 0.1238  -0.0191 0.0408  189 LEU A O   
3008  C CB  . LEU A 189 ? 1.0387 1.2345 1.1859 0.1411  -0.0439 0.0494  189 LEU A CB  
3009  C CG  . LEU A 189 ? 1.0486 1.2420 1.1931 0.1412  -0.0624 0.0516  189 LEU A CG  
3010  C CD1 . LEU A 189 ? 1.0140 1.1819 1.1215 0.1279  -0.0667 0.0476  189 LEU A CD1 
3011  C CD2 . LEU A 189 ? 1.0812 1.2647 1.2218 0.1589  -0.0691 0.0570  189 LEU A CD2 
3023  N N   . SER A 190 ? 0.9765 1.1044 1.0486 0.1333  -0.0179 0.0424  190 SER A N   
3024  C CA  . SER A 190 ? 0.9759 1.0947 1.0366 0.1231  -0.0086 0.0387  190 SER A CA  
3025  C C   . SER A 190 ? 0.9771 1.0725 1.0083 0.1079  -0.0123 0.0381  190 SER A C   
3026  O O   . SER A 190 ? 1.0298 1.1099 1.0435 0.1075  -0.0204 0.0409  190 SER A O   
3027  C CB  . SER A 190 ? 1.0288 1.1295 1.0776 0.1360  -0.0005 0.0390  190 SER A CB  
3028  O OG  . SER A 190 ? 1.0173 1.0920 1.0441 0.1497  -0.0054 0.0422  190 SER A OG  
3034  N N   . MET A 191 ? 0.9642 1.0570 0.9905 0.0955  -0.0063 0.0355  191 MET A N   
3035  C CA  . MET A 191 ? 1.0110 1.0883 1.0165 0.0796  -0.0081 0.0368  191 MET A CA  
3036  C C   . MET A 191 ? 0.9973 1.0645 0.9954 0.0707  -0.0030 0.0353  191 MET A C   
3037  O O   . MET A 191 ? 0.9777 1.0637 0.9944 0.0692  0.0030  0.0317  191 MET A O   
3038  C CB  . MET A 191 ? 0.9500 1.0494 0.9676 0.0697  -0.0087 0.0361  191 MET A CB  
3039  C CG  . MET A 191 ? 0.9730 1.0630 0.9740 0.0541  -0.0071 0.0389  191 MET A CG  
3040  S SD  . MET A 191 ? 1.0201 1.1336 1.0311 0.0474  -0.0056 0.0378  191 MET A SD  
3041  C CE  . MET A 191 ? 0.9036 1.0439 0.9417 0.0437  0.0021  0.0323  191 MET A CE  
3051  N N   . LYS A 192 ? 1.0357 1.0714 1.0060 0.0641  -0.0067 0.0384  192 LYS A N   
3052  C CA  . LYS A 192 ? 1.0705 1.0930 1.0318 0.0528  -0.0057 0.0381  192 LYS A CA  
3053  C C   . LYS A 192 ? 1.0414 1.0727 1.0052 0.0333  -0.0057 0.0420  192 LYS A C   
3054  O O   . LYS A 192 ? 1.0824 1.0940 1.0270 0.0253  -0.0101 0.0479  192 LYS A O   
3055  C CB  . LYS A 192 ? 1.1385 1.1176 1.0666 0.0570  -0.0116 0.0400  192 LYS A CB  
3056  C CG  . LYS A 192 ? 1.1781 1.1457 1.1010 0.0747  -0.0083 0.0358  192 LYS A CG  
3057  C CD  . LYS A 192 ? 1.3335 1.2676 1.2290 0.0913  -0.0126 0.0376  192 LYS A CD  
3058  C CE  . LYS A 192 ? 1.3340 1.2914 1.2489 0.1077  -0.0102 0.0383  192 LYS A CE  
3059  N NZ  . LYS A 192 ? 1.3446 1.2720 1.2354 0.1276  -0.0133 0.0401  192 LYS A NZ  
3073  N N   . PRO A 193 ? 1.0344 1.0944 1.0209 0.0258  -0.0001 0.0398  193 PRO A N   
3074  C CA  . PRO A 193 ? 1.0730 1.1450 1.0640 0.0100  0.0021  0.0447  193 PRO A CA  
3075  C C   . PRO A 193 ? 1.1224 1.1764 1.1030 -0.0050 -0.0017 0.0499  193 PRO A C   
3076  O O   . PRO A 193 ? 1.1886 1.2344 1.1691 -0.0061 -0.0043 0.0471  193 PRO A O   
3077  C CB  . PRO A 193 ? 1.0356 1.1418 1.0532 0.0099  0.0089  0.0401  193 PRO A CB  
3078  C CG  . PRO A 193 ? 1.0157 1.1241 1.0419 0.0209  0.0097  0.0335  193 PRO A CG  
3079  C CD  . PRO A 193 ? 1.0289 1.1099 1.0365 0.0320  0.0051  0.0336  193 PRO A CD  
3087  N N   . TYR A 194 ? 1.1636 1.2103 1.1346 -0.0169 -0.0027 0.0584  194 TYR A N   
3088  C CA  . TYR A 194 ? 1.1895 1.2242 1.1560 -0.0349 -0.0070 0.0661  194 TYR A CA  
3089  C C   . TYR A 194 ? 1.2173 1.2833 1.2044 -0.0473 0.0014  0.0728  194 TYR A C   
3090  O O   . TYR A 194 ? 1.2103 1.2905 1.1989 -0.0431 0.0088  0.0744  194 TYR A O   
3091  C CB  . TYR A 194 ? 1.2362 1.2323 1.1724 -0.0396 -0.0151 0.0728  194 TYR A CB  
3092  C CG  . TYR A 194 ? 1.3041 1.2857 1.2360 -0.0608 -0.0217 0.0824  194 TYR A CG  
3093  C CD1 . TYR A 194 ? 1.3346 1.3340 1.2785 -0.0769 -0.0163 0.0937  194 TYR A CD1 
3094  C CD2 . TYR A 194 ? 1.3710 1.3201 1.2863 -0.0648 -0.0337 0.0812  194 TYR A CD2 
3095  C CE1 . TYR A 194 ? 1.4023 1.3919 1.3474 -0.0981 -0.0231 0.1045  194 TYR A CE1 
3096  C CE2 . TYR A 194 ? 1.4456 1.3799 1.3578 -0.0863 -0.0429 0.0908  194 TYR A CE2 
3097  C CZ  . TYR A 194 ? 1.4459 1.4028 1.3759 -0.1038 -0.0378 0.1030  194 TYR A CZ  
3098  O OH  . TYR A 194 ? 1.4739 1.4196 1.4060 -0.1269 -0.0475 0.1145  194 TYR A OH  
3108  N N   . VAL A 195 ? 1.2497 1.3252 1.2516 -0.0615 -0.0001 0.0774  195 VAL A N   
3109  C CA  . VAL A 195 ? 1.2767 1.3850 1.3016 -0.0720 0.0091  0.0852  195 VAL A CA  
3110  C C   . VAL A 195 ? 1.3317 1.4366 1.3646 -0.0928 0.0027  0.0963  195 VAL A C   
3111  O O   . VAL A 195 ? 1.3642 1.4662 1.4051 -0.0980 -0.0058 0.0939  195 VAL A O   
3112  C CB  . VAL A 195 ? 1.2211 1.3629 1.2703 -0.0637 0.0167  0.0774  195 VAL A CB  
3113  C CG1 . VAL A 195 ? 1.2500 1.4230 1.3254 -0.0755 0.0233  0.0859  195 VAL A CG1 
3114  C CG2 . VAL A 195 ? 1.1545 1.3061 1.1998 -0.0481 0.0243  0.0710  195 VAL A CG2 
3124  N N   . TYR A 196 ? 1.3687 1.4730 1.3990 -0.1052 0.0061  0.1094  196 TYR A N   
3125  C CA  . TYR A 196 ? 1.4093 1.5215 1.4565 -0.1271 0.0025  0.1234  196 TYR A CA  
3126  C C   . TYR A 196 ? 1.4377 1.5974 1.5175 -0.1292 0.0184  0.1305  196 TYR A C   
3127  O O   . TYR A 196 ? 1.4304 1.6044 1.5069 -0.1180 0.0326  0.1297  196 TYR A O   
3128  C CB  . TYR A 196 ? 1.4268 1.5091 1.4523 -0.1408 -0.0027 0.1357  196 TYR A CB  
3129  C CG  . TYR A 196 ? 1.4728 1.5672 1.5197 -0.1660 -0.0052 0.1536  196 TYR A CG  
3130  C CD1 . TYR A 196 ? 1.4863 1.5462 1.5206 -0.1836 -0.0237 0.1599  196 TYR A CD1 
3131  C CD2 . TYR A 196 ? 1.4964 1.6352 1.5752 -0.1721 0.0107  0.1652  196 TYR A CD2 
3132  C CE1 . TYR A 196 ? 1.5185 1.5908 1.5760 -0.2090 -0.0279 0.1779  196 TYR A CE1 
3133  C CE2 . TYR A 196 ? 1.5299 1.6847 1.6338 -0.1950 0.0092  0.1832  196 TYR A CE2 
3134  C CZ  . TYR A 196 ? 1.5304 1.6529 1.6255 -0.2148 -0.0108 0.1900  196 TYR A CZ  
3135  O OH  . TYR A 196 ? 1.5549 1.6941 1.6781 -0.2402 -0.0144 0.2097  196 TYR A OH  
3145  N N   . VAL A 197 ? 1.4862 1.6685 1.5957 -0.1429 0.0153  0.1378  197 VAL A N   
3146  C CA  . VAL A 197 ? 1.5218 1.7498 1.6647 -0.1465 0.0304  0.1482  197 VAL A CA  
3147  C C   . VAL A 197 ? 1.5918 1.8290 1.7580 -0.1714 0.0239  0.1665  197 VAL A C   
3148  O O   . VAL A 197 ? 1.5974 1.8084 1.7580 -0.1851 0.0045  0.1676  197 VAL A O   
3149  C CB  . VAL A 197 ? 1.5191 1.7771 1.6844 -0.1340 0.0349  0.1380  197 VAL A CB  
3150  C CG1 . VAL A 197 ? 1.4487 1.6905 1.5909 -0.1132 0.0352  0.1196  197 VAL A CG1 
3151  C CG2 . VAL A 197 ? 1.5799 1.8416 1.7659 -0.1458 0.0197  0.1387  197 VAL A CG2 
3161  N N   . LYS A 198 ? 1.7181 1.9923 1.9101 -0.1770 0.0403  0.1817  198 LYS A N   
3162  C CA  . LYS A 198 ? 1.7094 1.9983 1.9292 -0.2020 0.0361  0.2025  198 LYS A CA  
3163  C C   . LYS A 198 ? 1.7620 2.0663 2.0133 -0.2126 0.0203  0.2028  198 LYS A C   
3164  O O   . LYS A 198 ? 1.7132 1.9997 1.9690 -0.2342 0.0009  0.2114  198 LYS A O   
3165  C CB  . LYS A 198 ? 1.7251 2.0557 1.9684 -0.2020 0.0609  0.2192  198 LYS A CB  
3166  C CG  . LYS A 198 ? 1.6990 2.0790 1.9956 -0.2143 0.0644  0.2348  198 LYS A CG  
3167  C CD  . LYS A 198 ? 1.6800 2.1001 1.9971 -0.2121 0.0922  0.2529  198 LYS A CD  
3168  C CE  . LYS A 198 ? 1.6661 2.1026 1.9722 -0.1830 0.1133  0.2409  198 LYS A CE  
3169  N NZ  . LYS A 198 ? 1.6318 2.0388 1.8926 -0.1708 0.1251  0.2367  198 LYS A NZ  
3183  N N   . GLU A 199 ? 1.6982 2.0323 1.9691 -0.1978 0.0266  0.1935  199 GLU A N   
3184  C CA  . GLU A 199 ? 1.6647 2.0163 1.9669 -0.2066 0.0122  0.1946  199 GLU A CA  
3185  C C   . GLU A 199 ? 1.6514 1.9552 1.9279 -0.2140 -0.0147 0.1845  199 GLU A C   
3186  O O   . GLU A 199 ? 1.6946 1.9880 1.9819 -0.2360 -0.0339 0.1949  199 GLU A O   
3187  C CB  . GLU A 199 ? 1.6619 2.0456 1.9804 -0.1859 0.0234  0.1836  199 GLU A CB  
3188  C CG  . GLU A 199 ? 1.6740 2.0962 2.0059 -0.1720 0.0512  0.1895  199 GLU A CG  
3189  C CD  . GLU A 199 ? 1.6606 2.1222 2.0310 -0.1871 0.0622  0.2142  199 GLU A CD  
3190  O OE1 . GLU A 199 ? 1.6615 2.1113 2.0361 -0.2097 0.0522  0.2283  199 GLU A OE1 
3191  O OE2 . GLU A 199 ? 1.6453 2.1495 2.0414 -0.1758 0.0817  0.2203  199 GLU A OE2 
3198  N N   . VAL A 200 ? 1.6698 1.9426 1.9109 -0.1956 -0.0166 0.1648  200 VAL A N   
3199  C CA  . VAL A 200 ? 1.6135 1.8375 1.8240 -0.1984 -0.0390 0.1547  200 VAL A CA  
3200  C C   . VAL A 200 ? 1.5874 1.7737 1.7773 -0.2175 -0.0528 0.1651  200 VAL A C   
3201  O O   . VAL A 200 ? 1.6055 1.7568 1.7811 -0.2296 -0.0757 0.1647  200 VAL A O   
3202  C CB  . VAL A 200 ? 1.5928 1.7927 1.7694 -0.1740 -0.0339 0.1346  200 VAL A CB  
3203  C CG1 . VAL A 200 ? 1.5676 1.7145 1.7083 -0.1741 -0.0540 0.1253  200 VAL A CG1 
3204  C CG2 . VAL A 200 ? 1.6293 1.8619 1.8247 -0.1573 -0.0233 0.1245  200 VAL A CG2 
3214  N N   . GLY A 201 ? 1.6250 1.8136 1.8090 -0.2205 -0.0399 0.1747  201 GLY A N   
3215  C CA  . GLY A 201 ? 1.5843 1.7338 1.7450 -0.2381 -0.0524 0.1847  201 GLY A CA  
3216  C C   . GLY A 201 ? 1.5500 1.6391 1.6609 -0.2298 -0.0679 0.1705  201 GLY A C   
3217  O O   . GLY A 201 ? 1.5135 1.5612 1.6032 -0.2460 -0.0872 0.1764  201 GLY A O   
3221  N N   . SER A 202 ? 1.4676 1.5498 1.5589 -0.2044 -0.0599 0.1527  202 SER A N   
3222  C CA  . SER A 202 ? 1.5005 1.5298 1.5469 -0.1925 -0.0716 0.1393  202 SER A CA  
3223  C C   . SER A 202 ? 1.4862 1.5237 1.5222 -0.1652 -0.0558 0.1245  202 SER A C   
3224  O O   . SER A 202 ? 1.4607 1.5410 1.5227 -0.1563 -0.0397 0.1224  202 SER A O   
3225  C CB  . SER A 202 ? 1.4970 1.5019 1.5357 -0.1961 -0.0916 0.1328  202 SER A CB  
3226  O OG  . SER A 202 ? 1.4938 1.4596 1.5158 -0.2178 -0.1133 0.1426  202 SER A OG  
3232  N N   . GLY A 203 ? 1.4746 1.4694 1.4717 -0.1516 -0.0613 0.1148  203 GLY A N   
3233  C CA  . GLY A 203 ? 1.4513 1.4518 1.4392 -0.1272 -0.0486 0.1026  203 GLY A CA  
3234  C C   . GLY A 203 ? 1.3630 1.3721 1.3568 -0.1120 -0.0474 0.0892  203 GLY A C   
3235  O O   . GLY A 203 ? 1.4282 1.4271 1.4227 -0.1178 -0.0585 0.0872  203 GLY A O   
3239  N N   . VAL A 204 ? 1.3237 1.3504 1.3208 -0.0927 -0.0344 0.0803  204 VAL A N   
3240  C CA  . VAL A 204 ? 1.2949 1.3321 1.2989 -0.0777 -0.0308 0.0684  204 VAL A CA  
3241  C C   . VAL A 204 ? 1.2682 1.3038 1.2618 -0.0568 -0.0223 0.0601  204 VAL A C   
3242  O O   . VAL A 204 ? 1.2184 1.2796 1.2247 -0.0520 -0.0120 0.0606  204 VAL A O   
3243  C CB  . VAL A 204 ? 1.2315 1.3141 1.2715 -0.0815 -0.0227 0.0689  204 VAL A CB  
3244  C CG1 . VAL A 204 ? 1.1588 1.2534 1.2046 -0.0645 -0.0165 0.0568  204 VAL A CG1 
3245  C CG2 . VAL A 204 ? 1.2663 1.3518 1.3202 -0.1001 -0.0334 0.0763  204 VAL A CG2 
3255  N N   . TYR A 205 ? 1.2301 1.2353 1.2003 -0.0437 -0.0268 0.0531  205 TYR A N   
3256  C CA  . TYR A 205 ? 1.1970 1.2051 1.1634 -0.0231 -0.0190 0.0460  205 TYR A CA  
3257  C C   . TYR A 205 ? 1.1439 1.1829 1.1342 -0.0150 -0.0105 0.0389  205 TYR A C   
3258  O O   . TYR A 205 ? 1.1851 1.2153 1.1721 -0.0127 -0.0129 0.0345  205 TYR A O   
3259  C CB  . TYR A 205 ? 1.2159 1.1809 1.1490 -0.0105 -0.0250 0.0428  205 TYR A CB  
3260  C CG  . TYR A 205 ? 1.2714 1.2031 1.1774 -0.0148 -0.0329 0.0490  205 TYR A CG  
3261  C CD1 . TYR A 205 ? 1.3016 1.2030 1.1893 -0.0318 -0.0454 0.0552  205 TYR A CD1 
3262  C CD2 . TYR A 205 ? 1.2719 1.2006 1.1701 -0.0023 -0.0293 0.0492  205 TYR A CD2 
3263  C CE1 . TYR A 205 ? 1.3342 1.2018 1.1948 -0.0367 -0.0532 0.0615  205 TYR A CE1 
3264  C CE2 . TYR A 205 ? 1.3254 1.2206 1.1959 -0.0056 -0.0369 0.0550  205 TYR A CE2 
3265  C CZ  . TYR A 205 ? 1.3597 1.2236 1.2107 -0.0229 -0.0484 0.0611  205 TYR A CZ  
3266  O OH  . TYR A 205 ? 1.3987 1.2263 1.2202 -0.0272 -0.0565 0.0674  205 TYR A OH  
3276  N N   . GLU A 206 ? 1.1097 1.1811 1.1206 -0.0107 -0.0015 0.0378  206 GLU A N   
3277  C CA  . GLU A 206 ? 1.0397 1.1405 1.0735 -0.0056 0.0057  0.0320  206 GLU A CA  
3278  C C   . GLU A 206 ? 1.0059 1.1047 1.0385 0.0120  0.0098  0.0256  206 GLU A C   
3279  O O   . GLU A 206 ? 0.9823 1.0644 1.0011 0.0220  0.0087  0.0260  206 GLU A O   
3280  C CB  . GLU A 206 ? 1.0919 1.2247 1.1450 -0.0092 0.0124  0.0340  206 GLU A CB  
3281  C CG  . GLU A 206 ? 1.1402 1.2819 1.1994 -0.0250 0.0120  0.0421  206 GLU A CG  
3282  C CD  . GLU A 206 ? 1.1100 1.2731 1.1894 -0.0314 0.0136  0.0414  206 GLU A CD  
3283  O OE1 . GLU A 206 ? 1.1107 1.2748 1.1940 -0.0246 0.0134  0.0343  206 GLU A OE1 
3284  O OE2 . GLU A 206 ? 1.1449 1.3242 1.2366 -0.0427 0.0156  0.0488  206 GLU A OE2 
3291  N N   . ASN A 207 ? 1.0275 1.1445 1.0760 0.0160  0.0149  0.0207  207 ASN A N   
3292  C CA  . ASN A 207 ? 0.9723 1.0943 1.0262 0.0312  0.0207  0.0164  207 ASN A CA  
3293  C C   . ASN A 207 ? 0.9603 1.1054 1.0305 0.0357  0.0237  0.0167  207 ASN A C   
3294  O O   . ASN A 207 ? 0.9621 1.1092 1.0364 0.0478  0.0259  0.0161  207 ASN A O   
3295  C CB  . ASN A 207 ? 0.9778 1.1094 1.0417 0.0327  0.0250  0.0120  207 ASN A CB  
3296  C CG  . ASN A 207 ? 1.0553 1.1570 1.0974 0.0337  0.0214  0.0107  207 ASN A CG  
3297  O OD1 . ASN A 207 ? 1.0481 1.1200 1.0665 0.0388  0.0177  0.0122  207 ASN A OD1 
3298  N ND2 . ASN A 207 ? 1.0675 1.1735 1.1142 0.0297  0.0215  0.0079  207 ASN A ND2 
3305  N N   . SER A 208 ? 0.8964 1.0583 0.9753 0.0266  0.0234  0.0182  208 SER A N   
3306  C CA  . SER A 208 ? 0.8871 1.0647 0.9747 0.0297  0.0238  0.0184  208 SER A CA  
3307  C C   . SER A 208 ? 0.8992 1.0858 0.9863 0.0194  0.0245  0.0213  208 SER A C   
3308  O O   . SER A 208 ? 0.9276 1.1209 1.0195 0.0113  0.0268  0.0219  208 SER A O   
3309  C CB  . SER A 208 ? 0.8485 1.0460 0.9556 0.0362  0.0269  0.0142  208 SER A CB  
3310  O OG  . SER A 208 ? 0.8546 1.0684 0.9715 0.0298  0.0296  0.0118  208 SER A OG  
3316  N N   . CYS A 209 ? 0.8736 1.0601 0.9544 0.0209  0.0227  0.0237  209 CYS A N   
3317  C CA  . CYS A 209 ? 0.9000 1.0922 0.9757 0.0135  0.0255  0.0277  209 CYS A CA  
3318  C C   . CYS A 209 ? 0.8818 1.0824 0.9571 0.0195  0.0247  0.0255  209 CYS A C   
3319  O O   . CYS A 209 ? 0.8802 1.0704 0.9457 0.0249  0.0191  0.0265  209 CYS A O   
3320  C CB  . CYS A 209 ? 0.9031 1.0760 0.9605 0.0075  0.0233  0.0349  209 CYS A CB  
3321  S SG  . CYS A 209 ? 0.9163 1.0977 0.9687 -0.0021 0.0301  0.0426  209 CYS A SG  
3327  N N   . ALA A 210 ? 0.8730 1.0897 0.9567 0.0189  0.0290  0.0226  210 ALA A N   
3328  C CA  . ALA A 210 ? 0.8575 1.0775 0.9370 0.0245  0.0263  0.0198  210 ALA A CA  
3329  C C   . ALA A 210 ? 0.8697 1.0781 0.9272 0.0244  0.0265  0.0247  210 ALA A C   
3330  O O   . ALA A 210 ? 0.8734 1.0713 0.9200 0.0299  0.0187  0.0241  210 ALA A O   
3331  C CB  . ALA A 210 ? 0.8264 1.0612 0.9145 0.0246  0.0310  0.0156  210 ALA A CB  
3337  N N   . SER A 211 ? 0.8836 1.0940 0.9347 0.0184  0.0352  0.0304  211 SER A N   
3338  C CA  . SER A 211 ? 0.8994 1.0983 0.9278 0.0184  0.0380  0.0365  211 SER A CA  
3339  C C   . SER A 211 ? 0.9263 1.1047 0.9410 0.0184  0.0304  0.0399  211 SER A C   
3340  O O   . SER A 211 ? 0.9636 1.1272 0.9572 0.0230  0.0266  0.0415  211 SER A O   
3341  C CB  . SER A 211 ? 0.8962 1.1050 0.9260 0.0109  0.0504  0.0444  211 SER A CB  
3342  O OG  . SER A 211 ? 0.8872 1.0959 0.9279 0.0009  0.0499  0.0492  211 SER A OG  
3348  N N   . GLY A 212 ? 0.9310 1.1049 0.9542 0.0143  0.0276  0.0410  212 GLY A N   
3349  C CA  . GLY A 212 ? 0.9326 1.0845 0.9411 0.0163  0.0201  0.0438  212 GLY A CA  
3350  C C   . GLY A 212 ? 0.9385 1.0858 0.9458 0.0276  0.0101  0.0389  212 GLY A C   
3351  O O   . GLY A 212 ? 0.9836 1.1130 0.9731 0.0318  0.0036  0.0416  212 GLY A O   
3355  N N   . THR A 213 ? 0.9212 1.0848 0.9486 0.0323  0.0081  0.0323  213 THR A N   
3356  C CA  . THR A 213 ? 0.9461 1.1099 0.9787 0.0415  -0.0023 0.0291  213 THR A CA  
3357  C C   . THR A 213 ? 0.9327 1.0887 0.9470 0.0441  -0.0080 0.0293  213 THR A C   
3358  O O   . THR A 213 ? 0.9606 1.1073 0.9692 0.0506  -0.0195 0.0297  213 THR A O   
3359  C CB  . THR A 213 ? 0.9139 1.0977 0.9734 0.0437  -0.0024 0.0237  213 THR A CB  
3360  O OG1 . THR A 213 ? 0.8503 1.0388 0.9206 0.0406  0.0050  0.0233  213 THR A OG1 
3361  C CG2 . THR A 213 ? 0.8992 1.0865 0.9721 0.0523  -0.0128 0.0231  213 THR A CG2 
3369  N N   . THR A 214 ? 0.9641 1.1224 0.9678 0.0403  -0.0006 0.0293  214 THR A N   
3370  C CA  . THR A 214 ? 0.9617 1.1064 0.9400 0.0442  -0.0049 0.0297  214 THR A CA  
3371  C C   . THR A 214 ? 0.9677 1.0898 0.9188 0.0445  -0.0058 0.0363  214 THR A C   
3372  O O   . THR A 214 ? 1.0224 1.1275 0.9543 0.0506  -0.0169 0.0364  214 THR A O   
3373  C CB  . THR A 214 ? 0.9512 1.1024 0.9220 0.0426  0.0060  0.0287  214 THR A CB  
3374  O OG1 . THR A 214 ? 0.9241 1.0785 0.8914 0.0361  0.0203  0.0354  214 THR A OG1 
3375  C CG2 . THR A 214 ? 0.9113 1.0821 0.9070 0.0421  0.0066  0.0222  214 THR A CG2 
3383  N N   . ALA A 215 ? 0.9821 1.1022 0.9303 0.0374  0.0045  0.0425  215 ALA A N   
3384  C CA  . ALA A 215 ? 1.0375 1.1342 0.9609 0.0364  0.0030  0.0496  215 ALA A CA  
3385  C C   . ALA A 215 ? 1.0430 1.1270 0.9657 0.0440  -0.0120 0.0478  215 ALA A C   
3386  O O   . ALA A 215 ? 1.0956 1.1597 0.9948 0.0497  -0.0209 0.0496  215 ALA A O   
3387  C CB  . ALA A 215 ? 1.0028 1.1002 0.9300 0.0255  0.0132  0.0566  215 ALA A CB  
3393  N N   . LEU A 216 ? 1.0275 1.1225 0.9751 0.0453  -0.0148 0.0447  216 LEU A N   
3394  C CA  . LEU A 216 ? 1.0410 1.1308 0.9949 0.0552  -0.0275 0.0432  216 LEU A CA  
3395  C C   . LEU A 216 ? 1.0894 1.1819 1.0438 0.0623  -0.0399 0.0399  216 LEU A C   
3396  O O   . LEU A 216 ? 1.1267 1.2042 1.0686 0.0695  -0.0522 0.0417  216 LEU A O   
3397  C CB  . LEU A 216 ? 1.1437 1.2501 1.1268 0.0571  -0.0252 0.0399  216 LEU A CB  
3398  C CG  . LEU A 216 ? 1.1561 1.2564 1.1460 0.0677  -0.0324 0.0407  216 LEU A CG  
3399  C CD1 . LEU A 216 ? 1.2011 1.3101 1.2032 0.0774  -0.0453 0.0395  216 LEU A CD1 
3400  C CD2 . LEU A 216 ? 1.1523 1.2227 1.1140 0.0682  -0.0340 0.0460  216 LEU A CD2 
3412  N N   . GLY A 217 ? 1.0545 1.1636 1.0213 0.0601  -0.0382 0.0352  217 GLY A N   
3413  C CA  . GLY A 217 ? 1.0730 1.1823 1.0400 0.0651  -0.0525 0.0320  217 GLY A CA  
3414  C C   . GLY A 217 ? 1.0950 1.1774 1.0233 0.0677  -0.0591 0.0343  217 GLY A C   
3415  O O   . GLY A 217 ? 1.1354 1.2056 1.0559 0.0742  -0.0757 0.0348  217 GLY A O   
3419  N N   . TYR A 218 ? 1.0843 1.1570 0.9877 0.0634  -0.0461 0.0362  218 TYR A N   
3420  C CA  . TYR A 218 ? 1.1465 1.1905 1.0078 0.0668  -0.0491 0.0394  218 TYR A CA  
3421  C C   . TYR A 218 ? 1.1903 1.2136 1.0359 0.0706  -0.0577 0.0444  218 TYR A C   
3422  O O   . TYR A 218 ? 1.2098 1.2099 1.0287 0.0769  -0.0713 0.0451  218 TYR A O   
3423  C CB  . TYR A 218 ? 1.1261 1.1669 0.9675 0.0619  -0.0290 0.0436  218 TYR A CB  
3424  C CG  . TYR A 218 ? 1.0855 1.1400 0.9315 0.0615  -0.0207 0.0391  218 TYR A CG  
3425  C CD1 . TYR A 218 ? 1.1077 1.1504 0.9366 0.0681  -0.0318 0.0335  218 TYR A CD1 
3426  C CD2 . TYR A 218 ? 1.0298 1.1065 0.8954 0.0550  -0.0032 0.0406  218 TYR A CD2 
3427  C CE1 . TYR A 218 ? 1.0815 1.1325 0.9106 0.0691  -0.0245 0.0291  218 TYR A CE1 
3428  C CE2 . TYR A 218 ? 1.0126 1.1009 0.8814 0.0564  0.0044  0.0366  218 TYR A CE2 
3429  C CZ  . TYR A 218 ? 1.0553 1.1299 0.9047 0.0639  -0.0057 0.0307  218 TYR A CZ  
3430  O OH  . TYR A 218 ? 1.0885 1.1709 0.9376 0.0665  0.0017  0.0265  218 TYR A OH  
3440  N N   . TYR A 219 ? 1.1903 1.2185 1.0495 0.0672  -0.0512 0.0479  219 TYR A N   
3441  C CA  . TYR A 219 ? 1.2201 1.2249 1.0606 0.0709  -0.0579 0.0532  219 TYR A CA  
3442  C C   . TYR A 219 ? 1.2495 1.2544 1.1029 0.0815  -0.0777 0.0507  219 TYR A C   
3443  O O   . TYR A 219 ? 1.3153 1.2960 1.1441 0.0881  -0.0898 0.0536  219 TYR A O   
3444  C CB  . TYR A 219 ? 1.2291 1.2358 1.0783 0.0641  -0.0465 0.0572  219 TYR A CB  
3445  C CG  . TYR A 219 ? 1.2669 1.2525 1.1054 0.0697  -0.0550 0.0608  219 TYR A CG  
3446  C CD1 . TYR A 219 ? 1.3311 1.2846 1.1317 0.0693  -0.0567 0.0674  219 TYR A CD1 
3447  C CD2 . TYR A 219 ? 1.2656 1.2617 1.1297 0.0763  -0.0603 0.0581  219 TYR A CD2 
3448  C CE1 . TYR A 219 ? 1.3907 1.3217 1.1787 0.0753  -0.0651 0.0706  219 TYR A CE1 
3449  C CE2 . TYR A 219 ? 1.2937 1.2684 1.1454 0.0838  -0.0675 0.0614  219 TYR A CE2 
3450  C CZ  . TYR A 219 ? 1.3459 1.2875 1.1593 0.0831  -0.0707 0.0673  219 TYR A CZ  
3451  O OH  . TYR A 219 ? 1.3791 1.2962 1.1775 0.0915  -0.0786 0.0704  219 TYR A OH  
3461  N N   . LEU A 220 ? 1.2466 1.2794 1.1393 0.0835  -0.0812 0.0462  220 LEU A N   
3462  C CA  . LEU A 220 ? 1.2640 1.3034 1.1761 0.0934  -0.0992 0.0456  220 LEU A CA  
3463  C C   . LEU A 220 ? 1.2705 1.3037 1.1732 0.0960  -0.1166 0.0434  220 LEU A C   
3464  O O   . LEU A 220 ? 1.3088 1.3392 1.2177 0.1041  -0.1353 0.0449  220 LEU A O   
3465  C CB  . LEU A 220 ? 1.2014 1.2737 1.1595 0.0945  -0.0958 0.0432  220 LEU A CB  
3466  C CG  . LEU A 220 ? 1.1588 1.2344 1.1274 0.0963  -0.0838 0.0450  220 LEU A CG  
3467  C CD1 . LEU A 220 ? 1.1469 1.2535 1.1590 0.1011  -0.0829 0.0434  220 LEU A CD1 
3468  C CD2 . LEU A 220 ? 1.1738 1.2242 1.1209 0.1047  -0.0894 0.0497  220 LEU A CD2 
3480  N N   . LYS A 221 ? 1.2589 1.2891 1.1466 0.0899  -0.1119 0.0401  221 LYS A N   
3481  C CA  . LYS A 221 ? 1.2966 1.3115 1.1646 0.0925  -0.1295 0.0377  221 LYS A CA  
3482  C C   . LYS A 221 ? 1.3163 1.2934 1.1376 0.0981  -0.1379 0.0415  221 LYS A C   
3483  O O   . LYS A 221 ? 1.3671 1.3310 1.1808 0.1044  -0.1605 0.0417  221 LYS A O   
3484  C CB  . LYS A 221 ? 1.2398 1.2560 1.0971 0.0867  -0.1202 0.0331  221 LYS A CB  
3485  C CG  . LYS A 221 ? 1.2621 1.2517 1.0848 0.0899  -0.1363 0.0302  221 LYS A CG  
3486  C CD  . LYS A 221 ? 1.2597 1.2615 1.1103 0.0897  -0.1598 0.0268  221 LYS A CD  
3487  C CE  . LYS A 221 ? 1.3574 1.3249 1.1672 0.0930  -0.1804 0.0241  221 LYS A CE  
3488  N NZ  . LYS A 221 ? 1.3865 1.3555 1.2157 0.0947  -0.2113 0.0251  221 LYS A NZ  
3502  N N   . LYS A 222 ? 1.3314 1.2907 1.1217 0.0953  -0.1205 0.0453  222 LYS A N   
3503  C CA  . LYS A 222 ? 1.3921 1.3127 1.1330 0.1000  -0.1254 0.0498  222 LYS A CA  
3504  C C   . LYS A 222 ? 1.4528 1.3625 1.1940 0.1063  -0.1363 0.0542  222 LYS A C   
3505  O O   . LYS A 222 ? 1.5166 1.3966 1.2256 0.1134  -0.1521 0.0563  222 LYS A O   
3506  C CB  . LYS A 222 ? 1.3593 1.2675 1.0703 0.0938  -0.1012 0.0544  222 LYS A CB  
3507  C CG  . LYS A 222 ? 1.4764 1.3443 1.1296 0.0983  -0.1024 0.0582  222 LYS A CG  
3508  C CD  . LYS A 222 ? 1.5768 1.4188 1.2038 0.0991  -0.1007 0.0663  222 LYS A CD  
3509  C CE  . LYS A 222 ? 1.5829 1.3933 1.1571 0.0985  -0.0861 0.0734  222 LYS A CE  
3510  N NZ  . LYS A 222 ? 1.5873 1.3834 1.1476 0.0929  -0.0748 0.0832  222 LYS A NZ  
3524  N N   . CYS A 223 ? 1.5285 1.4586 1.3023 0.1053  -0.1291 0.0555  223 CYS A N   
3525  C CA  . CYS A 223 ? 1.5967 1.5130 1.3664 0.1127  -0.1366 0.0599  223 CYS A CA  
3526  C C   . CYS A 223 ? 1.5816 1.5176 1.3883 0.1231  -0.1550 0.0584  223 CYS A C   
3527  O O   . CYS A 223 ? 1.6042 1.5259 1.4040 0.1330  -0.1656 0.0621  223 CYS A O   
3528  C CB  . CYS A 223 ? 1.5073 1.4263 1.2825 0.1069  -0.1178 0.0631  223 CYS A CB  
3529  S SG  . CYS A 223 ? 1.7656 1.6429 1.4877 0.1013  -0.1075 0.0714  223 CYS A SG  
3535  N N   . LYS A 224 ? 1.5192 1.4881 1.3658 0.1213  -0.1585 0.0542  224 LYS A N   
3536  C CA  . LYS A 224 ? 1.4894 1.4834 1.3782 0.1302  -0.1736 0.0549  224 LYS A CA  
3537  C C   . LYS A 224 ? 1.3894 1.4026 1.3023 0.1273  -0.1890 0.0518  224 LYS A C   
3538  O O   . LYS A 224 ? 1.3282 1.3683 1.2834 0.1326  -0.2010 0.0537  224 LYS A O   
3539  C CB  . LYS A 224 ? 1.4473 1.4690 1.3736 0.1315  -0.1579 0.0553  224 LYS A CB  
3540  C CG  . LYS A 224 ? 1.4661 1.4688 1.3676 0.1283  -0.1391 0.0568  224 LYS A CG  
3541  C CD  . LYS A 224 ? 1.4914 1.5113 1.4215 0.1343  -0.1291 0.0577  224 LYS A CD  
3542  C CE  . LYS A 224 ? 1.4255 1.4374 1.3581 0.1511  -0.1408 0.0620  224 LYS A CE  
3543  N NZ  . LYS A 224 ? 1.4660 1.5152 1.4489 0.1609  -0.1468 0.0629  224 LYS A NZ  
3557  N N   . ASN A 225 ? 1.3973 1.3969 1.2844 0.1194  -0.1891 0.0478  225 ASN A N   
3558  C CA  . ASN A 225 ? 1.4370 1.4470 1.3395 0.1157  -0.2061 0.0445  225 ASN A CA  
3559  C C   . ASN A 225 ? 1.3786 1.4320 1.3379 0.1113  -0.2003 0.0436  225 ASN A C   
3560  O O   . ASN A 225 ? 1.3471 1.4221 1.3433 0.1127  -0.2179 0.0457  225 ASN A O   
3561  C CB  . ASN A 225 ? 1.4872 1.4835 1.3847 0.1231  -0.2369 0.0473  225 ASN A CB  
3562  C CG  . ASN A 225 ? 1.4886 1.4919 1.4008 0.1176  -0.2585 0.0446  225 ASN A CG  
3563  O OD1 . ASN A 225 ? 1.4832 1.4813 1.3817 0.1096  -0.2523 0.0394  225 ASN A OD1 
3564  N ND2 . ASN A 225 ? 1.4220 1.4368 1.3626 0.1220  -0.2850 0.0488  225 ASN A ND2 
3571  N N   . LEU A 226 ? 1.3499 1.4162 1.3164 0.1057  -0.1755 0.0414  226 LEU A N   
3572  C CA  . LEU A 226 ? 1.2482 1.3516 1.2619 0.1013  -0.1663 0.0403  226 LEU A CA  
3573  C C   . LEU A 226 ? 1.2185 1.3216 1.2223 0.0912  -0.1574 0.0345  226 LEU A C   
3574  O O   . LEU A 226 ? 1.1804 1.2732 1.1603 0.0876  -0.1386 0.0324  226 LEU A O   
3575  C CB  . LEU A 226 ? 1.2293 1.3459 1.2591 0.1048  -0.1464 0.0424  226 LEU A CB  
3576  C CG  . LEU A 226 ? 1.1876 1.3417 1.2680 0.1052  -0.1394 0.0435  226 LEU A CG  
3577  C CD1 . LEU A 226 ? 1.1697 1.3462 1.2882 0.1092  -0.1593 0.0478  226 LEU A CD1 
3578  C CD2 . LEU A 226 ? 1.1439 1.3009 1.2301 0.1125  -0.1234 0.0460  226 LEU A CD2 
3590  N N   . ASP A 227 ? 1.2410 1.3561 1.2649 0.0866  -0.1713 0.0326  227 ASP A N   
3591  C CA  . ASP A 227 ? 1.2587 1.3667 1.2665 0.0788  -0.1672 0.0268  227 ASP A CA  
3592  C C   . ASP A 227 ? 1.2268 1.3609 1.2619 0.0733  -0.1462 0.0247  227 ASP A C   
3593  O O   . ASP A 227 ? 1.2298 1.3560 1.2443 0.0693  -0.1328 0.0203  227 ASP A O   
3594  C CB  . ASP A 227 ? 1.3486 1.4530 1.3627 0.0753  -0.1934 0.0257  227 ASP A CB  
3595  C CG  . ASP A 227 ? 1.4494 1.5319 1.4299 0.0703  -0.1933 0.0192  227 ASP A CG  
3596  O OD1 . ASP A 227 ? 1.5299 1.5767 1.4596 0.0743  -0.1964 0.0169  227 ASP A OD1 
3597  O OD2 . ASP A 227 ? 1.3906 1.4897 1.3934 0.0635  -0.1896 0.0165  227 ASP A OD2 
3602  N N   . ARG A 228 ? 1.1479 1.3126 1.2280 0.0741  -0.1427 0.0281  228 ARG A N   
3603  C CA  . ARG A 228 ? 1.0767 1.2638 1.1808 0.0696  -0.1238 0.0263  228 ARG A CA  
3604  C C   . ARG A 228 ? 1.0459 1.2581 1.1879 0.0753  -0.1173 0.0316  228 ARG A C   
3605  O O   . ARG A 228 ? 1.0710 1.2945 1.2364 0.0807  -0.1310 0.0370  228 ARG A O   
3606  C CB  . ARG A 228 ? 1.0781 1.2747 1.1969 0.0614  -0.1302 0.0232  228 ARG A CB  
3607  C CG  . ARG A 228 ? 1.0857 1.2963 1.2363 0.0594  -0.1529 0.0275  228 ARG A CG  
3608  C CD  . ARG A 228 ? 1.0716 1.3179 1.2728 0.0567  -0.1457 0.0317  228 ARG A CD  
3609  N NE  . ARG A 228 ? 1.0640 1.3153 1.2699 0.0477  -0.1386 0.0275  228 ARG A NE  
3610  C CZ  . ARG A 228 ? 1.0579 1.3038 1.2645 0.0392  -0.1544 0.0259  228 ARG A CZ  
3611  N NH1 . ARG A 228 ? 1.1079 1.3387 1.3044 0.0375  -0.1791 0.0270  228 ARG A NH1 
3612  N NH2 . ARG A 228 ? 1.0867 1.3424 1.3065 0.0319  -0.1467 0.0240  228 ARG A NH2 
3626  N N   . ALA A 229 ? 0.9890 1.2089 1.1356 0.0751  -0.0966 0.0305  229 ALA A N   
3627  C CA  . ALA A 229 ? 0.9524 1.1899 1.1262 0.0827  -0.0876 0.0350  229 ALA A CA  
3628  C C   . ALA A 229 ? 0.9048 1.1502 1.0838 0.0792  -0.0675 0.0321  229 ALA A C   
3629  O O   . ALA A 229 ? 0.8844 1.1203 1.0436 0.0716  -0.0602 0.0271  229 ALA A O   
3630  C CB  . ALA A 229 ? 0.9660 1.1859 1.1202 0.0923  -0.0878 0.0380  229 ALA A CB  
3636  N N   . LYS A 230 ? 0.8979 1.1602 1.1030 0.0860  -0.0587 0.0357  230 LYS A N   
3637  C CA  . LYS A 230 ? 0.8539 1.1211 1.0627 0.0846  -0.0407 0.0336  230 LYS A CA  
3638  C C   . LYS A 230 ? 0.8151 1.0639 1.0026 0.0919  -0.0313 0.0341  230 LYS A C   
3639  O O   . LYS A 230 ? 0.8407 1.0902 1.0354 0.1039  -0.0318 0.0388  230 LYS A O   
3640  C CB  . LYS A 230 ? 0.7929 1.0878 1.0410 0.0877  -0.0360 0.0377  230 LYS A CB  
3641  C CG  . LYS A 230 ? 0.8006 1.1094 1.0652 0.0765  -0.0400 0.0358  230 LYS A CG  
3642  C CD  . LYS A 230 ? 0.8666 1.2028 1.1705 0.0789  -0.0331 0.0417  230 LYS A CD  
3643  C CE  . LYS A 230 ? 0.8556 1.2115 1.1905 0.0727  -0.0493 0.0467  230 LYS A CE  
3644  N NZ  . LYS A 230 ? 0.8506 1.2242 1.2102 0.0650  -0.0427 0.0483  230 LYS A NZ  
3658  N N   . ILE A 231 ? 0.7922 1.0241 0.9537 0.0849  -0.0234 0.0300  231 ILE A N   
3659  C CA  . ILE A 231 ? 0.8643 1.0736 1.0011 0.0883  -0.0174 0.0307  231 ILE A CA  
3660  C C   . ILE A 231 ? 0.8728 1.0833 1.0137 0.0889  -0.0043 0.0291  231 ILE A C   
3661  O O   . ILE A 231 ? 0.8408 1.0538 0.9796 0.0793  0.0015  0.0254  231 ILE A O   
3662  C CB  . ILE A 231 ? 0.8888 1.0780 0.9948 0.0789  -0.0190 0.0293  231 ILE A CB  
3663  C CG1 . ILE A 231 ? 0.9556 1.1289 1.0441 0.0837  -0.0302 0.0326  231 ILE A CG1 
3664  C CG2 . ILE A 231 ? 0.9092 1.0810 0.9963 0.0747  -0.0099 0.0290  231 ILE A CG2 
3665  C CD1 . ILE A 231 ? 0.9274 1.1142 1.0331 0.0881  -0.0434 0.0337  231 ILE A CD1 
3677  N N   . VAL A 232 ? 0.8659 1.0729 1.0105 0.1016  0.0004  0.0320  232 VAL A N   
3678  C CA  . VAL A 232 ? 0.8941 1.0958 1.0360 0.1046  0.0124  0.0306  232 VAL A CA  
3679  C C   . VAL A 232 ? 0.9047 1.0762 1.0127 0.0983  0.0134  0.0284  232 VAL A C   
3680  O O   . VAL A 232 ? 0.9121 1.0625 0.9984 0.0995  0.0075  0.0303  232 VAL A O   
3681  C CB  . VAL A 232 ? 0.8948 1.1002 1.0482 0.1227  0.0183  0.0351  232 VAL A CB  
3682  C CG1 . VAL A 232 ? 0.9227 1.1598 1.1130 0.1279  0.0136  0.0399  232 VAL A CG1 
3683  C CG2 . VAL A 232 ? 0.8997 1.0758 1.0253 0.1334  0.0158  0.0370  232 VAL A CG2 
3693  N N   . GLN A 233 ? 0.9049 1.0734 1.0086 0.0910  0.0199  0.0251  233 GLN A N   
3694  C CA  . GLN A 233 ? 0.9312 1.0755 1.0087 0.0814  0.0192  0.0238  233 GLN A CA  
3695  C C   . GLN A 233 ? 0.9523 1.0811 1.0193 0.0860  0.0256  0.0220  233 GLN A C   
3696  O O   . GLN A 233 ? 0.9554 1.0949 1.0360 0.0961  0.0329  0.0217  233 GLN A O   
3697  C CB  . GLN A 233 ? 0.9139 1.0713 0.9967 0.0657  0.0181  0.0219  233 GLN A CB  
3698  C CG  . GLN A 233 ? 0.9310 1.1045 1.0242 0.0642  0.0129  0.0227  233 GLN A CG  
3699  C CD  . GLN A 233 ? 0.8506 1.0262 0.9363 0.0516  0.0119  0.0226  233 GLN A CD  
3700  O OE1 . GLN A 233 ? 0.8495 1.0138 0.9220 0.0430  0.0138  0.0240  233 GLN A OE1 
3701  N NE2 . GLN A 233 ? 0.7982 0.9878 0.8921 0.0508  0.0085  0.0217  233 GLN A NE2 
3710  N N   . PRO A 234 ? 0.9722 1.0739 1.0137 0.0785  0.0225  0.0217  234 PRO A N   
3711  C CA  . PRO A 234 ? 1.0134 1.0895 1.0352 0.0854  0.0257  0.0201  234 PRO A CA  
3712  C C   . PRO A 234 ? 0.9896 1.0808 1.0265 0.0902  0.0348  0.0172  234 PRO A C   
3713  O O   . PRO A 234 ? 0.9952 1.0756 1.0247 0.1057  0.0417  0.0175  234 PRO A O   
3714  C CB  . PRO A 234 ? 1.0152 1.0682 1.0156 0.0695  0.0179  0.0203  234 PRO A CB  
3715  C CG  . PRO A 234 ? 0.9974 1.0529 0.9970 0.0607  0.0119  0.0241  234 PRO A CG  
3716  C CD  . PRO A 234 ? 0.9798 1.0710 1.0079 0.0634  0.0156  0.0237  234 PRO A CD  
3724  N N   . ASN A 235 ? 0.9681 1.0827 1.0240 0.0786  0.0358  0.0149  235 ASN A N   
3725  C CA  . ASN A 235 ? 0.9557 1.0824 1.0237 0.0813  0.0437  0.0123  235 ASN A CA  
3726  C C   . ASN A 235 ? 0.9240 1.0868 1.0236 0.0760  0.0456  0.0118  235 ASN A C   
3727  O O   . ASN A 235 ? 0.9367 1.1106 1.0448 0.0683  0.0470  0.0090  235 ASN A O   
3728  C CB  . ASN A 235 ? 1.0073 1.1163 1.0586 0.0721  0.0407  0.0093  235 ASN A CB  
3729  C CG  . ASN A 235 ? 1.0799 1.1585 1.1059 0.0837  0.0447  0.0081  235 ASN A CG  
3730  O OD1 . ASN A 235 ? 1.0334 1.1152 1.0632 0.0988  0.0549  0.0091  235 ASN A OD1 
3731  N ND2 . ASN A 235 ? 1.1129 1.1614 1.1126 0.0766  0.0366  0.0066  235 ASN A ND2 
3738  N N   . GLY A 236 ? 0.9343 1.1133 1.0498 0.0806  0.0442  0.0146  236 GLY A N   
3739  C CA  . GLY A 236 ? 0.8597 1.0675 1.0012 0.0753  0.0429  0.0143  236 GLY A CA  
3740  C C   . GLY A 236 ? 0.8799 1.0959 1.0291 0.0775  0.0358  0.0173  236 GLY A C   
3741  O O   . GLY A 236 ? 0.9115 1.1124 1.0474 0.0840  0.0329  0.0199  236 GLY A O   
3745  N N   . TRP A 237 ? 0.8606 1.0976 1.0287 0.0722  0.0318  0.0169  237 TRP A N   
3746  C CA  . TRP A 237 ? 0.8258 1.0688 0.9994 0.0733  0.0224  0.0193  237 TRP A CA  
3747  C C   . TRP A 237 ? 0.8391 1.0913 1.0156 0.0630  0.0163  0.0164  237 TRP A C   
3748  O O   . TRP A 237 ? 0.8303 1.0918 1.0149 0.0575  0.0195  0.0135  237 TRP A O   
3749  C CB  . TRP A 237 ? 0.8191 1.0784 1.0177 0.0837  0.0217  0.0244  237 TRP A CB  
3750  C CG  . TRP A 237 ? 0.7990 1.0817 1.0256 0.0807  0.0238  0.0252  237 TRP A CG  
3751  C CD1 . TRP A 237 ? 0.7971 1.0877 1.0362 0.0846  0.0350  0.0267  237 TRP A CD1 
3752  C CD2 . TRP A 237 ? 0.8187 1.1165 1.0615 0.0729  0.0137  0.0251  237 TRP A CD2 
3753  N NE1 . TRP A 237 ? 0.7934 1.1049 1.0579 0.0786  0.0330  0.0282  237 TRP A NE1 
3754  C CE2 . TRP A 237 ? 0.7626 1.0779 1.0294 0.0711  0.0189  0.0270  237 TRP A CE2 
3755  C CE3 . TRP A 237 ? 0.8017 1.0963 1.0375 0.0675  0.0002  0.0238  237 TRP A CE3 
3756  C CZ2 . TRP A 237 ? 0.7813 1.1105 1.0664 0.0627  0.0097  0.0277  237 TRP A CZ2 
3757  C CZ3 . TRP A 237 ? 0.7861 1.0927 1.0372 0.0606  -0.0092 0.0237  237 TRP A CZ3 
3758  C CH2 . TRP A 237 ? 0.7908 1.1142 1.0668 0.0576  -0.0052 0.0256  237 TRP A CH2 
3769  N N   . LEU A 238 ? 0.8337 1.0801 0.9998 0.0617  0.0074  0.0174  238 LEU A N   
3770  C CA  . LEU A 238 ? 0.8058 1.0550 0.9674 0.0546  0.0011  0.0149  238 LEU A CA  
3771  C C   . LEU A 238 ? 0.8541 1.1026 1.0168 0.0582  -0.0117 0.0175  238 LEU A C   
3772  O O   . LEU A 238 ? 0.8389 1.0784 0.9949 0.0644  -0.0151 0.0209  238 LEU A O   
3773  C CB  . LEU A 238 ? 0.8044 1.0410 0.9420 0.0482  0.0049  0.0133  238 LEU A CB  
3774  C CG  . LEU A 238 ? 0.7959 1.0344 0.9331 0.0430  0.0145  0.0109  238 LEU A CG  
3775  C CD1 . LEU A 238 ? 0.8161 1.0451 0.9341 0.0368  0.0176  0.0123  238 LEU A CD1 
3776  C CD2 . LEU A 238 ? 0.7490 1.0009 0.8990 0.0404  0.0159  0.0070  238 LEU A CD2 
3788  N N   . GLU A 239 ? 0.8778 1.1329 1.0467 0.0544  -0.0202 0.0158  239 GLU A N   
3789  C CA  . GLU A 239 ? 0.8700 1.1214 1.0370 0.0563  -0.0357 0.0177  239 GLU A CA  
3790  C C   . GLU A 239 ? 0.8715 1.1050 1.0072 0.0525  -0.0397 0.0145  239 GLU A C   
3791  O O   . GLU A 239 ? 0.8465 1.0794 0.9748 0.0477  -0.0352 0.0104  239 GLU A O   
3792  C CB  . GLU A 239 ? 0.8604 1.1291 1.0562 0.0544  -0.0455 0.0192  239 GLU A CB  
3793  C CG  . GLU A 239 ? 0.9066 1.1732 1.1059 0.0565  -0.0646 0.0225  239 GLU A CG  
3794  C CD  . GLU A 239 ? 0.9256 1.2082 1.1536 0.0513  -0.0768 0.0247  239 GLU A CD  
3795  O OE1 . GLU A 239 ? 0.8649 1.1517 1.0974 0.0445  -0.0724 0.0215  239 GLU A OE1 
3796  O OE2 . GLU A 239 ? 0.9626 1.2534 1.2093 0.0535  -0.0919 0.0301  239 GLU A OE2 
3803  N N   . TYR A 240 ? 0.9297 1.1472 1.0450 0.0559  -0.0473 0.0167  240 TYR A N   
3804  C CA  . TYR A 240 ? 0.9277 1.1256 1.0100 0.0544  -0.0511 0.0148  240 TYR A CA  
3805  C C   . TYR A 240 ? 1.0022 1.1937 1.0822 0.0555  -0.0708 0.0143  240 TYR A C   
3806  O O   . TYR A 240 ? 1.0132 1.2112 1.1117 0.0589  -0.0831 0.0178  240 TYR A O   
3807  C CB  . TYR A 240 ? 0.9661 1.1458 1.0218 0.0567  -0.0468 0.0182  240 TYR A CB  
3808  C CG  . TYR A 240 ? 0.9878 1.1559 1.0368 0.0630  -0.0606 0.0220  240 TYR A CG  
3809  C CD1 . TYR A 240 ? 1.0571 1.2077 1.0835 0.0651  -0.0750 0.0217  240 TYR A CD1 
3810  C CD2 . TYR A 240 ? 0.9778 1.1493 1.0395 0.0681  -0.0597 0.0257  240 TYR A CD2 
3811  C CE1 . TYR A 240 ? 1.0792 1.2183 1.0991 0.0713  -0.0891 0.0252  240 TYR A CE1 
3812  C CE2 . TYR A 240 ? 1.0191 1.1800 1.0748 0.0753  -0.0725 0.0294  240 TYR A CE2 
3813  C CZ  . TYR A 240 ? 1.0729 1.2186 1.1090 0.0765  -0.0877 0.0292  240 TYR A CZ  
3814  O OH  . TYR A 240 ? 1.0978 1.2321 1.1275 0.0841  -0.1020 0.0330  240 TYR A OH  
3824  N N   . ILE A 241 ? 1.0258 1.2033 1.0822 0.0534  -0.0744 0.0103  241 ILE A N   
3825  C CA  . ILE A 241 ? 1.0542 1.2194 1.1021 0.0533  -0.0951 0.0088  241 ILE A CA  
3826  C C   . ILE A 241 ? 1.1024 1.2365 1.1019 0.0567  -0.0968 0.0067  241 ILE A C   
3827  O O   . ILE A 241 ? 1.0947 1.2227 1.0742 0.0569  -0.0825 0.0040  241 ILE A O   
3828  C CB  . ILE A 241 ? 1.0668 1.2425 1.1334 0.0475  -0.0997 0.0054  241 ILE A CB  
3829  C CG1 . ILE A 241 ? 1.0787 1.2814 1.1925 0.0448  -0.1064 0.0099  241 ILE A CG1 
3830  C CG2 . ILE A 241 ? 1.0881 1.2382 1.1258 0.0468  -0.1173 0.0017  241 ILE A CG2 
3831  C CD1 . ILE A 241 ? 1.0503 1.2639 1.1860 0.0374  -0.1125 0.0086  241 ILE A CD1 
3843  N N   . ILE A 242 ? 1.1958 1.3102 1.1762 0.0605  -0.1139 0.0086  242 ILE A N   
3844  C CA  . ILE A 242 ? 1.2575 1.3373 1.1869 0.0652  -0.1178 0.0070  242 ILE A CA  
3845  C C   . ILE A 242 ? 1.3304 1.3916 1.2479 0.0646  -0.1434 0.0038  242 ILE A C   
3846  O O   . ILE A 242 ? 1.3143 1.3807 1.2530 0.0631  -0.1642 0.0064  242 ILE A O   
3847  C CB  . ILE A 242 ? 1.2681 1.3324 1.1759 0.0704  -0.1176 0.0119  242 ILE A CB  
3848  C CG1 . ILE A 242 ? 1.1487 1.2326 1.0763 0.0688  -0.0973 0.0159  242 ILE A CG1 
3849  C CG2 . ILE A 242 ? 1.2704 1.2993 1.1224 0.0758  -0.1145 0.0113  242 ILE A CG2 
3850  C CD1 . ILE A 242 ? 1.1520 1.2178 1.0550 0.0727  -0.0949 0.0212  242 ILE A CD1 
3862  N N   . GLU A 243 ? 1.4262 1.4651 1.3096 0.0663  -0.1425 -0.0014 243 GLU A N   
3863  C CA  . GLU A 243 ? 1.5006 1.5165 1.3679 0.0648  -0.1677 -0.0052 243 GLU A CA  
3864  C C   . GLU A 243 ? 1.5437 1.5180 1.3483 0.0730  -0.1652 -0.0096 243 GLU A C   
3865  O O   . GLU A 243 ? 1.5343 1.5099 1.3248 0.0768  -0.1423 -0.0116 243 GLU A O   
3866  C CB  . GLU A 243 ? 1.5377 1.5751 1.4412 0.0562  -0.1709 -0.0077 243 GLU A CB  
3867  C CG  . GLU A 243 ? 1.5952 1.6208 1.5050 0.0498  -0.2027 -0.0083 243 GLU A CG  
3868  C CD  . GLU A 243 ? 1.6404 1.6896 1.5899 0.0398  -0.2040 -0.0089 243 GLU A CD  
3869  O OE1 . GLU A 243 ? 1.6352 1.6801 1.5715 0.0405  -0.1897 -0.0139 243 GLU A OE1 
3870  O OE2 . GLU A 243 ? 1.6245 1.6972 1.6189 0.0318  -0.2189 -0.0036 243 GLU A OE2 
3877  N N   . ASN A 244 ? 1.5118 1.4489 1.2785 0.0768  -0.1889 -0.0107 244 ASN A N   
3878  C CA  . ASN A 244 ? 1.5412 1.4321 1.2403 0.0874  -0.1870 -0.0143 244 ASN A CA  
3879  C C   . ASN A 244 ? 1.5220 1.4155 1.2007 0.0952  -0.1550 -0.0108 244 ASN A C   
3880  O O   . ASN A 244 ? 1.5486 1.4271 1.1931 0.1031  -0.1370 -0.0129 244 ASN A O   
3881  C CB  . ASN A 244 ? 1.5377 1.4112 1.2173 0.0880  -0.1904 -0.0213 244 ASN A CB  
3882  C CG  . ASN A 244 ? 1.6407 1.4584 1.2444 0.1009  -0.1944 -0.0255 244 ASN A CG  
3883  O OD1 . ASN A 244 ? 1.6620 1.4711 1.2339 0.1116  -0.1681 -0.0256 244 ASN A OD1 
3884  N ND2 . ASN A 244 ? 1.6493 1.4285 1.2233 0.1004  -0.2275 -0.0282 244 ASN A ND2 
3891  N N   . ASP A 245 ? 1.4771 1.3899 1.1779 0.0932  -0.1479 -0.0045 245 ASP A N   
3892  C CA  . ASP A 245 ? 1.4815 1.4006 1.1709 0.0972  -0.1191 0.0008  245 ASP A CA  
3893  C C   . ASP A 245 ? 1.4389 1.3852 1.1485 0.0955  -0.0930 0.0000  245 ASP A C   
3894  O O   . ASP A 245 ? 1.4949 1.4330 1.1762 0.1023  -0.0715 0.0020  245 ASP A O   
3895  C CB  . ASP A 245 ? 1.5693 1.4436 1.1921 0.1085  -0.1166 0.0025  245 ASP A CB  
3896  C CG  . ASP A 245 ? 1.6531 1.4959 1.2512 0.1108  -0.1452 0.0028  245 ASP A CG  
3897  O OD1 . ASP A 245 ? 1.6967 1.5586 1.3353 0.1038  -0.1638 0.0036  245 ASP A OD1 
3898  O OD2 . ASP A 245 ? 1.6661 1.4646 1.2038 0.1207  -0.1491 0.0028  245 ASP A OD2 
3903  N N   . GLU A 246 ? 1.3813 1.3611 1.1416 0.0869  -0.0948 -0.0022 246 GLU A N   
3904  C CA  . GLU A 246 ? 1.3217 1.3295 1.1067 0.0843  -0.0728 -0.0029 246 GLU A CA  
3905  C C   . GLU A 246 ? 1.2120 1.2578 1.0529 0.0748  -0.0703 -0.0006 246 GLU A C   
3906  O O   . GLU A 246 ? 1.2059 1.2602 1.0736 0.0700  -0.0884 -0.0017 246 GLU A O   
3907  C CB  . GLU A 246 ? 1.3043 1.3033 1.0804 0.0862  -0.0782 -0.0101 246 GLU A CB  
3908  C CG  . GLU A 246 ? 1.4046 1.3626 1.1197 0.0984  -0.0774 -0.0129 246 GLU A CG  
3909  C CD  . GLU A 246 ? 1.4440 1.4033 1.1500 0.1042  -0.0625 -0.0169 246 GLU A CD  
3910  O OE1 . GLU A 246 ? 1.4461 1.4205 1.1516 0.1091  -0.0360 -0.0127 246 GLU A OE1 
3911  O OE2 . GLU A 246 ? 1.4529 1.3979 1.1526 0.1038  -0.0778 -0.0236 246 GLU A OE2 
3918  N N   . MET A 247 ? 1.1602 1.2284 1.0183 0.0725  -0.0481 0.0031  247 MET A N   
3919  C CA  . MET A 247 ? 1.0966 1.1949 0.9997 0.0651  -0.0443 0.0054  247 MET A CA  
3920  C C   . MET A 247 ? 1.0676 1.1888 1.0009 0.0609  -0.0389 0.0013  247 MET A C   
3921  O O   . MET A 247 ? 1.0632 1.1859 0.9869 0.0631  -0.0263 -0.0007 247 MET A O   
3922  C CB  . MET A 247 ? 1.0451 1.1506 0.9482 0.0633  -0.0265 0.0122  247 MET A CB  
3923  C CG  . MET A 247 ? 1.0371 1.1677 0.9799 0.0567  -0.0221 0.0142  247 MET A CG  
3924  S SD  . MET A 247 ? 1.0376 1.1693 1.0008 0.0571  -0.0413 0.0148  247 MET A SD  
3925  C CE  . MET A 247 ? 0.9966 1.1084 0.9337 0.0591  -0.0391 0.0220  247 MET A CE  
3935  N N   . TYR A 248 ? 1.0334 1.1724 1.0028 0.0559  -0.0475 0.0006  248 TYR A N   
3936  C CA  . TYR A 248 ? 0.9963 1.1566 0.9956 0.0515  -0.0425 -0.0024 248 TYR A CA  
3937  C C   . TYR A 248 ? 0.9518 1.1342 0.9861 0.0478  -0.0378 0.0010  248 TYR A C   
3938  O O   . TYR A 248 ? 0.9233 1.1056 0.9659 0.0487  -0.0464 0.0043  248 TYR A O   
3939  C CB  . TYR A 248 ? 0.9944 1.1497 0.9992 0.0496  -0.0597 -0.0066 248 TYR A CB  
3940  C CG  . TYR A 248 ? 1.0690 1.1950 1.0329 0.0544  -0.0673 -0.0107 248 TYR A CG  
3941  C CD1 . TYR A 248 ? 1.0444 1.1652 0.9929 0.0574  -0.0575 -0.0150 248 TYR A CD1 
3942  C CD2 . TYR A 248 ? 1.1226 1.2232 1.0603 0.0574  -0.0850 -0.0104 248 TYR A CD2 
3943  C CE1 . TYR A 248 ? 1.0900 1.1797 0.9959 0.0643  -0.0637 -0.0189 248 TYR A CE1 
3944  C CE2 . TYR A 248 ? 1.1543 1.2222 1.0482 0.0632  -0.0927 -0.0145 248 TYR A CE2 
3945  C CZ  . TYR A 248 ? 1.1334 1.1952 1.0104 0.0671  -0.0813 -0.0188 248 TYR A CZ  
3946  O OH  . TYR A 248 ? 1.2314 1.2566 1.0598 0.0752  -0.0882 -0.0231 248 TYR A OH  
3956  N N   . ILE A 249 ? 0.9167 1.1161 0.9692 0.0448  -0.0245 0.0001  249 ILE A N   
3957  C CA  . ILE A 249 ? 0.8913 1.1075 0.9720 0.0424  -0.0192 0.0025  249 ILE A CA  
3958  C C   . ILE A 249 ? 0.8687 1.0995 0.9742 0.0397  -0.0194 -0.0005 249 ILE A C   
3959  O O   . ILE A 249 ? 0.8624 1.0957 0.9652 0.0382  -0.0125 -0.0039 249 ILE A O   
3960  C CB  . ILE A 249 ? 0.8922 1.1113 0.9690 0.0406  -0.0041 0.0051  249 ILE A CB  
3961  C CG1 . ILE A 249 ? 0.8388 1.0449 0.8989 0.0420  -0.0051 0.0102  249 ILE A CG1 
3962  C CG2 . ILE A 249 ? 0.8502 1.0837 0.9521 0.0383  0.0022  0.0051  249 ILE A CG2 
3963  C CD1 . ILE A 249 ? 0.8459 1.0536 0.9205 0.0438  -0.0097 0.0129  249 ILE A CD1 
3975  N N   . ASP A 250 ? 0.8590 1.0997 0.9890 0.0395  -0.0267 0.0017  250 ASP A N   
3976  C CA  . ASP A 250 ? 0.8288 1.0845 0.9849 0.0366  -0.0253 0.0010  250 ASP A CA  
3977  C C   . ASP A 250 ? 0.8366 1.1040 1.0107 0.0386  -0.0141 0.0039  250 ASP A C   
3978  O O   . ASP A 250 ? 0.8851 1.1493 1.0564 0.0426  -0.0127 0.0072  250 ASP A O   
3979  C CB  . ASP A 250 ? 0.8346 1.0951 1.0083 0.0347  -0.0411 0.0032  250 ASP A CB  
3980  C CG  . ASP A 250 ? 0.8419 1.1142 1.0374 0.0296  -0.0405 0.0027  250 ASP A CG  
3981  O OD1 . ASP A 250 ? 0.8419 1.1136 1.0315 0.0283  -0.0298 -0.0011 250 ASP A OD1 
3982  O OD2 . ASP A 250 ? 0.8261 1.1086 1.0457 0.0266  -0.0512 0.0070  250 ASP A OD2 
3987  N N   . GLY A 251 ? 0.8258 1.1028 1.0143 0.0366  -0.0066 0.0027  251 GLY A N   
3988  C CA  . GLY A 251 ? 0.8071 1.0909 1.0083 0.0396  0.0038  0.0051  251 GLY A CA  
3989  C C   . GLY A 251 ? 0.8290 1.1206 1.0428 0.0374  0.0110  0.0036  251 GLY A C   
3990  O O   . GLY A 251 ? 0.8176 1.1088 1.0291 0.0328  0.0087  0.0002  251 GLY A O   
3994  N N   . PRO A 252 ? 0.7834 1.0791 1.0073 0.0416  0.0201  0.0063  252 PRO A N   
3995  C CA  . PRO A 252 ? 0.8134 1.1131 1.0451 0.0403  0.0282  0.0053  252 PRO A CA  
3996  C C   . PRO A 252 ? 0.7952 1.0846 1.0083 0.0380  0.0339  0.0001  252 PRO A C   
3997  O O   . PRO A 252 ? 0.7751 1.0558 0.9729 0.0383  0.0348  -0.0009 252 PRO A O   
3998  C CB  . PRO A 252 ? 0.7542 1.0583 0.9981 0.0481  0.0368  0.0106  252 PRO A CB  
3999  C CG  . PRO A 252 ? 0.7954 1.0989 1.0397 0.0540  0.0325  0.0142  252 PRO A CG  
4000  C CD  . PRO A 252 ? 0.8094 1.1061 1.0395 0.0495  0.0219  0.0114  252 PRO A CD  
4008  N N   . VAL A 253 ? 0.7838 1.0748 0.9998 0.0352  0.0371  -0.0022 253 VAL A N   
4009  C CA  . VAL A 253 ? 0.7739 1.0576 0.9764 0.0336  0.0415  -0.0066 253 VAL A CA  
4010  C C   . VAL A 253 ? 0.7738 1.0567 0.9819 0.0346  0.0482  -0.0064 253 VAL A C   
4011  O O   . VAL A 253 ? 0.7618 1.0519 0.9845 0.0337  0.0485  -0.0037 253 VAL A O   
4012  C CB  . VAL A 253 ? 0.7581 1.0411 0.9513 0.0299  0.0366  -0.0108 253 VAL A CB  
4013  C CG1 . VAL A 253 ? 0.7133 0.9924 0.8958 0.0294  0.0410  -0.0138 253 VAL A CG1 
4014  C CG2 . VAL A 253 ? 0.7548 1.0369 0.9408 0.0299  0.0305  -0.0100 253 VAL A CG2 
4024  N N   . GLU A 254 ? 0.7748 1.0482 0.9708 0.0358  0.0531  -0.0086 254 GLU A N   
4025  C CA  . GLU A 254 ? 0.7775 1.0453 0.9729 0.0380  0.0599  -0.0085 254 GLU A CA  
4026  C C   . GLU A 254 ? 0.7755 1.0335 0.9562 0.0365  0.0595  -0.0130 254 GLU A C   
4027  O O   . GLU A 254 ? 0.7343 0.9848 0.9044 0.0365  0.0578  -0.0137 254 GLU A O   
4028  C CB  . GLU A 254 ? 0.7495 1.0114 0.9444 0.0452  0.0675  -0.0041 254 GLU A CB  
4029  C CG  . GLU A 254 ? 0.8122 1.0691 1.0071 0.0487  0.0766  -0.0022 254 GLU A CG  
4030  C CD  . GLU A 254 ? 0.8401 1.0883 1.0298 0.0589  0.0864  0.0024  254 GLU A CD  
4031  O OE1 . GLU A 254 ? 0.8322 1.0844 1.0269 0.0635  0.0861  0.0055  254 GLU A OE1 
4032  O OE2 . GLU A 254 ? 0.8614 1.0967 1.0395 0.0636  0.0947  0.0030  254 GLU A OE2 
4039  N N   . ILE A 255 ? 0.7960 1.0531 0.9765 0.0350  0.0600  -0.0153 255 ILE A N   
4040  C CA  . ILE A 255 ? 0.7711 1.0197 0.9394 0.0347  0.0588  -0.0192 255 ILE A CA  
4041  C C   . ILE A 255 ? 0.7803 1.0129 0.9370 0.0388  0.0639  -0.0183 255 ILE A C   
4042  O O   . ILE A 255 ? 0.7989 1.0268 0.9562 0.0418  0.0706  -0.0160 255 ILE A O   
4043  C CB  . ILE A 255 ? 0.7741 1.0239 0.9429 0.0331  0.0569  -0.0222 255 ILE A CB  
4044  C CG1 . ILE A 255 ? 0.7548 1.0147 0.9305 0.0305  0.0518  -0.0229 255 ILE A CG1 
4045  C CG2 . ILE A 255 ? 0.7601 1.0045 0.9185 0.0339  0.0541  -0.0260 255 ILE A CG2 
4046  C CD1 . ILE A 255 ? 0.7680 1.0332 0.9385 0.0308  0.0481  -0.0251 255 ILE A CD1 
4058  N N   . ILE A 256 ? 0.7886 1.0111 0.9334 0.0389  0.0604  -0.0192 256 ILE A N   
4059  C CA  . ILE A 256 ? 0.8075 1.0082 0.9346 0.0436  0.0630  -0.0187 256 ILE A CA  
4060  C C   . ILE A 256 ? 0.8334 1.0220 0.9488 0.0443  0.0616  -0.0217 256 ILE A C   
4061  O O   . ILE A 256 ? 0.8317 1.0090 0.9389 0.0490  0.0688  -0.0208 256 ILE A O   
4062  C CB  . ILE A 256 ? 0.8305 1.0207 0.9470 0.0419  0.0567  -0.0181 256 ILE A CB  
4063  C CG1 . ILE A 256 ? 0.8132 1.0072 0.9345 0.0442  0.0595  -0.0147 256 ILE A CG1 
4064  C CG2 . ILE A 256 ? 0.8465 1.0077 0.9380 0.0458  0.0549  -0.0191 256 ILE A CG2 
4065  C CD1 . ILE A 256 ? 0.8063 1.0012 0.9265 0.0384  0.0517  -0.0138 256 ILE A CD1 
4077  N N   . ALA A 257 ? 0.8337 1.0248 0.9484 0.0400  0.0528  -0.0243 257 ALA A N   
4078  C CA  . ALA A 257 ? 0.8085 0.9859 0.9104 0.0412  0.0485  -0.0271 257 ALA A CA  
4079  C C   . ALA A 257 ? 0.7838 0.9782 0.8977 0.0377  0.0419  -0.0291 257 ALA A C   
4080  O O   . ALA A 257 ? 0.7883 1.0023 0.9170 0.0344  0.0406  -0.0280 257 ALA A O   
4081  C CB  . ALA A 257 ? 0.8443 0.9975 0.9257 0.0418  0.0420  -0.0270 257 ALA A CB  
4087  N N   . GLU A 258 ? 0.7610 0.9463 0.8663 0.0399  0.0382  -0.0317 258 GLU A N   
4088  C CA  . GLU A 258 ? 0.7504 0.9505 0.8656 0.0399  0.0335  -0.0336 258 GLU A CA  
4089  C C   . GLU A 258 ? 0.7938 0.9801 0.8975 0.0419  0.0250  -0.0352 258 GLU A C   
4090  O O   . GLU A 258 ? 0.7934 0.9557 0.8776 0.0452  0.0260  -0.0365 258 GLU A O   
4091  C CB  . GLU A 258 ? 0.7906 0.9956 0.9087 0.0424  0.0396  -0.0354 258 GLU A CB  
4092  C CG  . GLU A 258 ? 0.8176 1.0396 0.9455 0.0440  0.0370  -0.0371 258 GLU A CG  
4093  C CD  . GLU A 258 ? 0.8410 1.0599 0.9658 0.0461  0.0406  -0.0393 258 GLU A CD  
4094  O OE1 . GLU A 258 ? 0.8070 1.0155 0.9278 0.0442  0.0454  -0.0382 258 GLU A OE1 
4095  O OE2 . GLU A 258 ? 0.9006 1.1266 1.0266 0.0497  0.0387  -0.0415 258 GLU A OE2 
4102  N N   . GLY A 259 ? 0.7097 0.9114 0.8259 0.0404  0.0168  -0.0344 259 GLY A N   
4103  C CA  . GLY A 259 ? 0.7952 0.9875 0.9046 0.0427  0.0066  -0.0355 259 GLY A CA  
4104  C C   . GLY A 259 ? 0.8715 1.0822 0.9990 0.0386  -0.0044 -0.0317 259 GLY A C   
4105  O O   . GLY A 259 ? 0.7512 0.9899 0.9006 0.0374  -0.0013 -0.0287 259 GLY A O   
4109  N N   . LYS A 260 ? 0.7945 0.9886 0.9126 0.0365  -0.0176 -0.0310 260 LYS A N   
4110  C CA  . LYS A 260 ? 0.8238 1.0355 0.9619 0.0318  -0.0309 -0.0261 260 LYS A CA  
4111  C C   . LYS A 260 ? 0.8573 1.0591 0.9936 0.0211  -0.0406 -0.0218 260 LYS A C   
4112  O O   . LYS A 260 ? 0.8571 1.0265 0.9664 0.0204  -0.0416 -0.0242 260 LYS A O   
4113  C CB  . LYS A 260 ? 0.7962 0.9965 0.9266 0.0368  -0.0431 -0.0280 260 LYS A CB  
4114  C CG  . LYS A 260 ? 0.8254 1.0272 0.9507 0.0478  -0.0351 -0.0328 260 LYS A CG  
4115  C CD  . LYS A 260 ? 0.8347 1.0702 0.9878 0.0528  -0.0373 -0.0297 260 LYS A CD  
4116  C CE  . LYS A 260 ? 0.8505 1.0914 1.0000 0.0631  -0.0246 -0.0340 260 LYS A CE  
4117  N NZ  . LYS A 260 ? 0.8388 1.1106 1.0118 0.0711  -0.0247 -0.0310 260 LYS A NZ  
4131  N N   . ILE A 261 ? 0.8327 1.0617 0.9972 0.0133  -0.0475 -0.0146 261 ILE A N   
4132  C CA  . ILE A 261 ? 0.8525 1.0740 1.0186 0.0010  -0.0587 -0.0089 261 ILE A CA  
4133  C C   . ILE A 261 ? 0.8759 1.1156 1.0670 -0.0065 -0.0762 -0.0015 261 ILE A C   
4134  O O   . ILE A 261 ? 0.8243 1.1025 1.0476 -0.0044 -0.0723 0.0033  261 ILE A O   
4135  C CB  . ILE A 261 ? 0.8253 1.0646 1.0041 -0.0040 -0.0469 -0.0050 261 ILE A CB  
4136  C CG1 . ILE A 261 ? 0.8642 1.0890 1.0390 -0.0169 -0.0587 0.0005  261 ILE A CG1 
4137  C CG2 . ILE A 261 ? 0.8570 1.1404 1.0699 -0.0026 -0.0382 0.0003  261 ILE A CG2 
4138  C CD1 . ILE A 261 ? 0.9383 1.1758 1.1211 -0.0211 -0.0475 0.0042  261 ILE A CD1 
4150  N N   . TYR A 262 ? 0.8983 1.1093 1.0739 -0.0146 -0.0960 -0.0002 262 TYR A N   
4151  C CA  . TYR A 262 ? 0.9288 1.1515 1.1259 -0.0226 -0.1174 0.0068  262 TYR A CA  
4152  C C   . TYR A 262 ? 0.9785 1.2097 1.1940 -0.0401 -0.1285 0.0170  262 TYR A C   
4153  O O   . TYR A 262 ? 0.9674 1.1612 1.1545 -0.0473 -0.1371 0.0157  262 TYR A O   
4154  C CB  . TYR A 262 ? 0.9075 1.0871 1.0709 -0.0197 -0.1356 0.0011  262 TYR A CB  
4155  C CG  . TYR A 262 ? 0.9211 1.0834 1.0586 -0.0034 -0.1240 -0.0087 262 TYR A CG  
4156  C CD1 . TYR A 262 ? 0.9024 1.0934 1.0605 0.0062  -0.1178 -0.0094 262 TYR A CD1 
4157  C CD2 . TYR A 262 ? 0.9344 1.0508 1.0261 0.0028  -0.1188 -0.0166 262 TYR A CD2 
4158  C CE1 . TYR A 262 ? 0.8978 1.0703 1.0309 0.0195  -0.1082 -0.0177 262 TYR A CE1 
4159  C CE2 . TYR A 262 ? 0.9075 1.0089 0.9772 0.0160  -0.1075 -0.0238 262 TYR A CE2 
4160  C CZ  . TYR A 262 ? 0.8930 1.0217 0.9833 0.0234  -0.1031 -0.0244 262 TYR A CZ  
4161  O OH  . TYR A 262 ? 0.9334 1.0449 1.0009 0.0351  -0.0929 -0.0310 262 TYR A OH  
4171  N N   . ILE A 263 ? 1.0343 1.3136 1.2962 -0.0463 -0.1277 0.0279  263 ILE A N   
4172  C CA  . ILE A 263 ? 1.0497 1.3444 1.3369 -0.0646 -0.1379 0.0404  263 ILE A CA  
4173  C C   . ILE A 263 ? 1.0713 1.4006 1.4010 -0.0714 -0.1543 0.0516  263 ILE A C   
4174  O O   . ILE A 263 ? 1.0998 1.4438 1.4395 -0.0598 -0.1548 0.0491  263 ILE A O   
4175  C CB  . ILE A 263 ? 1.0853 1.4094 1.3904 -0.0657 -0.1156 0.0453  263 ILE A CB  
4176  C CG1 . ILE A 263 ? 1.0814 1.3688 1.3461 -0.0618 -0.1045 0.0360  263 ILE A CG1 
4177  C CG2 . ILE A 263 ? 1.1128 1.4633 1.4531 -0.0844 -0.1237 0.0612  263 ILE A CG2 
4178  C CD1 . ILE A 263 ? 1.1721 1.4338 1.4235 -0.0774 -0.1156 0.0410  263 ILE A CD1 
4190  N N   . GLY A 264 ? 1.1430 1.4846 1.4982 -0.0908 -0.1692 0.0648  264 GLY A N   
4191  C CA  . GLY A 264 ? 1.1795 1.5622 1.5844 -0.0994 -0.1841 0.0787  264 GLY A CA  
4192  C C   . GLY A 264 ? 1.2350 1.6814 1.6887 -0.0927 -0.1612 0.0887  264 GLY A C   
4193  O O   . GLY A 264 ? 1.1978 1.6550 1.6463 -0.0843 -0.1354 0.0858  264 GLY A O   
4197  N N   . LYS A 265 ? 1.3932 1.8816 1.8945 -0.0955 -0.1717 0.1011  265 LYS A N   
4198  C CA  . LYS A 265 ? 1.3569 1.9076 1.9061 -0.0866 -0.1503 0.1122  265 LYS A CA  
4199  C C   . LYS A 265 ? 1.3224 1.9177 1.9285 -0.1063 -0.1602 0.1346  265 LYS A C   
4200  O O   . LYS A 265 ? 1.2959 1.9368 1.9365 -0.1050 -0.1388 0.1468  265 LYS A O   
4201  C CB  . LYS A 265 ? 1.2966 1.8652 1.8551 -0.0656 -0.1480 0.1072  265 LYS A CB  
4202  C CG  . LYS A 265 ? 1.2215 1.8469 1.8179 -0.0496 -0.1217 0.1155  265 LYS A CG  
4203  C CD  . LYS A 265 ? 1.1895 1.8034 1.7572 -0.0232 -0.1060 0.1002  265 LYS A CD  
4204  C CE  . LYS A 265 ? 1.1621 1.8297 1.7680 -0.0047 -0.0872 0.1090  265 LYS A CE  
4205  N NZ  . LYS A 265 ? 1.1618 1.8321 1.7484 0.0104  -0.0561 0.1033  265 LYS A NZ  
4219  N N   . ARG B 3   ? 1.2396 1.6131 1.7923 0.1228  0.4450  0.1572  3   ARG B N   
4220  C CA  . ARG B 3   ? 1.2241 1.6222 1.7781 0.1140  0.3968  0.1523  3   ARG B CA  
4221  C C   . ARG B 3   ? 1.2001 1.5881 1.7126 0.0846  0.3614  0.1331  3   ARG B C   
4222  O O   . ARG B 3   ? 1.2817 1.6165 1.7341 0.0733  0.3714  0.1156  3   ARG B O   
4223  C CB  . ARG B 3   ? 1.2566 1.6091 1.7669 0.1281  0.3986  0.1421  3   ARG B CB  
4224  C CG  . ARG B 3   ? 1.3461 1.7116 1.9003 0.1585  0.4280  0.1623  3   ARG B CG  
4225  C CD  . ARG B 3   ? 1.4460 1.7638 1.9530 0.1699  0.4272  0.1515  3   ARG B CD  
4226  N NE  . ARG B 3   ? 1.5098 1.8337 2.0552 0.2004  0.4584  0.1710  3   ARG B NE  
4227  C CZ  . ARG B 3   ? 1.5344 1.8140 2.0447 0.2153  0.4689  0.1658  3   ARG B CZ  
4228  N NH1 . ARG B 3   ? 1.5509 1.7789 1.9882 0.2018  0.4499  0.1422  3   ARG B NH1 
4229  N NH2 . ARG B 3   ? 1.5023 1.7897 2.0529 0.2445  0.4994  0.1859  3   ARG B NH2 
4242  N N   . LYS B 4   ? 1.1775 1.6143 1.7204 0.0719  0.3202  0.1372  4   LYS B N   
4243  C CA  . LYS B 4   ? 1.1664 1.5938 1.6723 0.0460  0.2864  0.1200  4   LYS B CA  
4244  C C   . LYS B 4   ? 1.1691 1.5646 1.6259 0.0439  0.2608  0.1026  4   LYS B C   
4245  O O   . LYS B 4   ? 1.1556 1.5563 1.6226 0.0591  0.2581  0.1075  4   LYS B O   
4246  C CB  . LYS B 4   ? 1.1319 1.6236 1.6911 0.0303  0.2571  0.1331  4   LYS B CB  
4247  C CG  . LYS B 4   ? 1.1408 1.6609 1.7384 0.0222  0.2747  0.1462  4   LYS B CG  
4248  C CD  . LYS B 4   ? 1.1879 1.6536 1.7321 0.0142  0.2988  0.1306  4   LYS B CD  
4249  C CE  . LYS B 4   ? 1.2132 1.6361 1.6898 -0.0049 0.2712  0.1060  4   LYS B CE  
4250  N NZ  . LYS B 4   ? 1.1910 1.5650 1.6185 -0.0152 0.2909  0.0936  4   LYS B NZ  
4264  N N   . VAL B 5   ? 1.1603 1.5237 1.5658 0.0252  0.2423  0.0836  5   VAL B N   
4265  C CA  . VAL B 5   ? 1.1119 1.4427 1.4691 0.0213  0.2196  0.0668  5   VAL B CA  
4266  C C   . VAL B 5   ? 1.0568 1.4185 1.4243 0.0049  0.1805  0.0640  5   VAL B C   
4267  O O   . VAL B 5   ? 1.0485 1.4129 1.4096 -0.0125 0.1704  0.0596  5   VAL B O   
4268  C CB  . VAL B 5   ? 1.1147 1.3808 1.4031 0.0134  0.2294  0.0487  5   VAL B CB  
4269  C CG1 . VAL B 5   ? 1.0529 1.2842 1.2983 0.0159  0.2159  0.0363  5   VAL B CG1 
4270  C CG2 . VAL B 5   ? 1.0907 1.3265 1.3684 0.0228  0.2716  0.0524  5   VAL B CG2 
4280  N N   . GLN B 6   ? 1.0392 1.4203 1.4193 0.0101  0.1599  0.0664  6   GLN B N   
4281  C CA  . GLN B 6   ? 0.9783 1.3794 1.3587 -0.0050 0.1247  0.0621  6   GLN B CA  
4282  C C   . GLN B 6   ? 0.9448 1.3017 1.2685 -0.0125 0.1114  0.0421  6   GLN B C   
4283  O O   . GLN B 6   ? 0.9330 1.2608 1.2298 -0.0027 0.1163  0.0356  6   GLN B O   
4284  C CB  . GLN B 6   ? 0.9844 1.4238 1.4004 0.0026  0.1085  0.0742  6   GLN B CB  
4285  C CG  . GLN B 6   ? 0.9556 1.4236 1.3816 -0.0153 0.0758  0.0750  6   GLN B CG  
4286  C CD  . GLN B 6   ? 0.9357 1.4472 1.4029 -0.0108 0.0605  0.0917  6   GLN B CD  
4287  O OE1 . GLN B 6   ? 0.9370 1.4485 1.4120 0.0065  0.0673  0.0974  6   GLN B OE1 
4288  N NE2 . GLN B 6   ? 0.9603 1.5069 1.4513 -0.0277 0.0387  0.1003  6   GLN B NE2 
4297  N N   . VAL B 7   ? 0.9236 1.2757 1.2305 -0.0300 0.0947  0.0337  7   VAL B N   
4298  C CA  . VAL B 7   ? 0.9100 1.2228 1.1684 -0.0376 0.0830  0.0173  7   VAL B CA  
4299  C C   . VAL B 7   ? 0.8919 1.2192 1.1510 -0.0436 0.0549  0.0137  7   VAL B C   
4300  O O   . VAL B 7   ? 0.8752 1.2210 1.1449 -0.0567 0.0401  0.0149  7   VAL B O   
4301  C CB  . VAL B 7   ? 0.9214 1.2123 1.1570 -0.0515 0.0868  0.0108  7   VAL B CB  
4302  C CG1 . VAL B 7   ? 0.9454 1.1899 1.1309 -0.0548 0.0823  -0.0028 7   VAL B CG1 
4303  C CG2 . VAL B 7   ? 0.9533 1.2449 1.2028 -0.0482 0.1151  0.0189  7   VAL B CG2 
4313  N N   . LEU B 8   ? 0.8424 1.1581 1.0872 -0.0352 0.0486  0.0092  8   LEU B N   
4314  C CA  . LEU B 8   ? 0.8154 1.1407 1.0578 -0.0390 0.0257  0.0057  8   LEU B CA  
4315  C C   . LEU B 8   ? 0.8206 1.1125 1.0249 -0.0441 0.0165  -0.0078 8   LEU B C   
4316  O O   . LEU B 8   ? 0.8302 1.0919 1.0096 -0.0411 0.0257  -0.0132 8   LEU B O   
4317  C CB  . LEU B 8   ? 0.8557 1.1947 1.1122 -0.0260 0.0245  0.0119  8   LEU B CB  
4318  C CG  . LEU B 8   ? 0.8436 1.2088 1.1369 -0.0140 0.0389  0.0271  8   LEU B CG  
4319  C CD1 . LEU B 8   ? 0.8915 1.2726 1.1976 -0.0045 0.0299  0.0335  8   LEU B CD1 
4320  C CD2 . LEU B 8   ? 0.8812 1.2812 1.2098 -0.0224 0.0376  0.0384  8   LEU B CD2 
4332  N N   . ASP B 9   ? 0.8025 1.0990 1.0018 -0.0521 -0.0016 -0.0120 9   ASP B N   
4333  C CA  . ASP B 9   ? 0.8025 1.0724 0.9729 -0.0547 -0.0104 -0.0223 9   ASP B CA  
4334  C C   . ASP B 9   ? 0.7865 1.0555 0.9535 -0.0452 -0.0148 -0.0234 9   ASP B C   
4335  O O   . ASP B 9   ? 0.8030 1.0925 0.9841 -0.0432 -0.0219 -0.0192 9   ASP B O   
4336  C CB  . ASP B 9   ? 0.8372 1.1072 1.0014 -0.0668 -0.0237 -0.0264 9   ASP B CB  
4337  C CG  . ASP B 9   ? 0.8848 1.1594 1.0550 -0.0781 -0.0205 -0.0240 9   ASP B CG  
4338  O OD1 . ASP B 9   ? 0.8862 1.1790 1.0780 -0.0767 -0.0101 -0.0159 9   ASP B OD1 
4339  O OD2 . ASP B 9   ? 0.9162 1.1755 1.0702 -0.0881 -0.0272 -0.0296 9   ASP B OD2 
4344  N N   . PHE B 10  ? 0.7837 1.0282 0.9307 -0.0408 -0.0116 -0.0280 10  PHE B N   
4345  C CA  . PHE B 10  ? 0.7721 1.0138 0.9152 -0.0327 -0.0141 -0.0285 10  PHE B CA  
4346  C C   . PHE B 10  ? 0.7646 0.9885 0.8899 -0.0353 -0.0229 -0.0346 10  PHE B C   
4347  O O   . PHE B 10  ? 0.7584 0.9660 0.8710 -0.0413 -0.0247 -0.0378 10  PHE B O   
4348  C CB  . PHE B 10  ? 0.7906 1.0199 0.9281 -0.0247 -0.0006 -0.0257 10  PHE B CB  
4349  C CG  . PHE B 10  ? 0.8295 1.0265 0.9392 -0.0285 0.0016  -0.0304 10  PHE B CG  
4350  C CD1 . PHE B 10  ? 0.8233 1.0081 0.9201 -0.0277 -0.0057 -0.0326 10  PHE B CD1 
4351  C CD2 . PHE B 10  ? 0.8349 1.0139 0.9309 -0.0342 0.0101  -0.0314 10  PHE B CD2 
4352  C CE1 . PHE B 10  ? 0.8364 0.9937 0.9090 -0.0336 -0.0070 -0.0346 10  PHE B CE1 
4353  C CE2 . PHE B 10  ? 0.8426 0.9901 0.9095 -0.0401 0.0093  -0.0344 10  PHE B CE2 
4354  C CZ  . PHE B 10  ? 0.8630 1.0006 0.9189 -0.0403 -0.0004 -0.0355 10  PHE B CZ  
4364  N N   . ILE B 11  ? 0.8097 1.0379 0.9361 -0.0302 -0.0280 -0.0349 11  ILE B N   
4365  C CA  . ILE B 11  ? 0.7815 0.9961 0.8968 -0.0299 -0.0336 -0.0380 11  ILE B CA  
4366  C C   . ILE B 11  ? 0.7781 0.9923 0.8928 -0.0231 -0.0313 -0.0356 11  ILE B C   
4367  O O   . ILE B 11  ? 0.7672 0.9955 0.8907 -0.0183 -0.0316 -0.0334 11  ILE B O   
4368  C CB  . ILE B 11  ? 0.7919 1.0106 0.9082 -0.0318 -0.0410 -0.0411 11  ILE B CB  
4369  C CG1 . ILE B 11  ? 0.7863 1.0055 0.9020 -0.0397 -0.0431 -0.0432 11  ILE B CG1 
4370  C CG2 . ILE B 11  ? 0.7931 0.9986 0.9034 -0.0304 -0.0441 -0.0422 11  ILE B CG2 
4371  C CD1 . ILE B 11  ? 0.7514 0.9895 0.8765 -0.0430 -0.0455 -0.0412 11  ILE B CD1 
4383  N N   . LYS B 12  ? 0.7830 0.9793 0.8851 -0.0241 -0.0300 -0.0352 12  LYS B N   
4384  C CA  . LYS B 12  ? 0.7943 0.9856 0.8919 -0.0200 -0.0282 -0.0329 12  LYS B CA  
4385  C C   . LYS B 12  ? 0.8154 1.0077 0.9148 -0.0207 -0.0362 -0.0328 12  LYS B C   
4386  O O   . LYS B 12  ? 0.8369 1.0222 0.9341 -0.0255 -0.0419 -0.0328 12  LYS B O   
4387  C CB  . LYS B 12  ? 0.8132 0.9806 0.8917 -0.0233 -0.0221 -0.0319 12  LYS B CB  
4388  C CG  . LYS B 12  ? 0.8408 0.9989 0.9107 -0.0205 -0.0196 -0.0296 12  LYS B CG  
4389  C CD  . LYS B 12  ? 0.9212 1.0510 0.9673 -0.0230 -0.0094 -0.0292 12  LYS B CD  
4390  C CE  . LYS B 12  ? 0.9479 1.0682 0.9860 -0.0181 -0.0035 -0.0269 12  LYS B CE  
4391  N NZ  . LYS B 12  ? 0.9655 1.0535 0.9771 -0.0189 0.0106  -0.0270 12  LYS B NZ  
4405  N N   . ILE B 13  ? 0.8017 1.0028 0.9064 -0.0154 -0.0359 -0.0316 13  ILE B N   
4406  C CA  . ILE B 13  ? 0.7759 0.9813 0.8860 -0.0146 -0.0403 -0.0309 13  ILE B CA  
4407  C C   . ILE B 13  ? 0.7883 0.9915 0.8953 -0.0122 -0.0385 -0.0277 13  ILE B C   
4408  O O   . ILE B 13  ? 0.8030 1.0074 0.9073 -0.0080 -0.0338 -0.0269 13  ILE B O   
4409  C CB  . ILE B 13  ? 0.7859 1.0032 0.9027 -0.0118 -0.0409 -0.0338 13  ILE B CB  
4410  C CG1 . ILE B 13  ? 0.7739 0.9911 0.8905 -0.0156 -0.0423 -0.0370 13  ILE B CG1 
4411  C CG2 . ILE B 13  ? 0.7866 1.0040 0.9077 -0.0101 -0.0414 -0.0332 13  ILE B CG2 
4412  C CD1 . ILE B 13  ? 0.7668 0.9916 0.8834 -0.0161 -0.0435 -0.0399 13  ILE B CD1 
4424  N N   . ASN B 14  ? 0.7962 0.9971 0.9057 -0.0149 -0.0420 -0.0247 14  ASN B N   
4425  C CA  . ASN B 14  ? 0.8235 1.0220 0.9302 -0.0147 -0.0409 -0.0211 14  ASN B CA  
4426  C C   . ASN B 14  ? 0.7889 0.9999 0.9068 -0.0103 -0.0395 -0.0203 14  ASN B C   
4427  O O   . ASN B 14  ? 0.7711 0.9859 0.8996 -0.0122 -0.0415 -0.0165 14  ASN B O   
4428  C CB  . ASN B 14  ? 0.7983 0.9843 0.8987 -0.0239 -0.0466 -0.0162 14  ASN B CB  
4429  C CG  . ASN B 14  ? 0.8238 1.0069 0.9213 -0.0263 -0.0464 -0.0118 14  ASN B CG  
4430  O OD1 . ASN B 14  ? 0.8443 1.0257 0.9355 -0.0211 -0.0403 -0.0131 14  ASN B OD1 
4431  N ND2 . ASN B 14  ? 0.8205 1.0037 0.9238 -0.0347 -0.0539 -0.0051 14  ASN B ND2 
4438  N N   . PRO B 15  ? 0.8331 1.0502 0.9490 -0.0047 -0.0356 -0.0226 15  PRO B N   
4439  C CA  . PRO B 15  ? 0.7829 1.0060 0.9023 -0.0016 -0.0323 -0.0220 15  PRO B CA  
4440  C C   . PRO B 15  ? 0.7971 1.0172 0.9134 -0.0020 -0.0303 -0.0175 15  PRO B C   
4441  O O   . PRO B 15  ? 0.8164 1.0345 0.9239 0.0010  -0.0284 -0.0170 15  PRO B O   
4442  C CB  . PRO B 15  ? 0.8016 1.0290 0.9146 0.0017  -0.0316 -0.0256 15  PRO B CB  
4443  C CG  . PRO B 15  ? 0.7984 1.0258 0.9087 0.0024  -0.0333 -0.0247 15  PRO B CG  
4444  C CD  . PRO B 15  ? 0.8299 1.0495 0.9412 -0.0014 -0.0343 -0.0246 15  PRO B CD  
4452  N N   . ALA B 16  ? 0.8111 1.0318 0.9362 -0.0062 -0.0313 -0.0127 16  ALA B N   
4453  C CA  . ALA B 16  ? 0.8046 1.0227 0.9279 -0.0091 -0.0298 -0.0075 16  ALA B CA  
4454  C C   . ALA B 16  ? 0.8293 1.0328 0.9351 -0.0115 -0.0309 -0.0072 16  ALA B C   
4455  O O   . ALA B 16  ? 0.8541 1.0519 0.9512 -0.0107 -0.0276 -0.0051 16  ALA B O   
4456  C CB  . ALA B 16  ? 0.8230 1.0460 0.9458 -0.0039 -0.0224 -0.0078 16  ALA B CB  
4462  N N   . GLY B 17  ? 0.8496 1.0436 0.9480 -0.0144 -0.0341 -0.0090 17  GLY B N   
4463  C CA  . GLY B 17  ? 0.8900 1.0645 0.9691 -0.0161 -0.0318 -0.0089 17  GLY B CA  
4464  C C   . GLY B 17  ? 0.9114 1.0854 0.9859 -0.0063 -0.0256 -0.0117 17  GLY B C   
4465  O O   . GLY B 17  ? 0.9443 1.1014 1.0051 -0.0055 -0.0209 -0.0118 17  GLY B O   
4469  N N   . ASN B 18  ? 0.8519 1.0430 0.9370 0.0008  -0.0251 -0.0128 18  ASN B N   
4470  C CA  . ASN B 18  ? 0.8924 1.0889 0.9787 0.0090  -0.0222 -0.0125 18  ASN B CA  
4471  C C   . ASN B 18  ? 0.8691 1.0702 0.9616 0.0084  -0.0230 -0.0155 18  ASN B C   
4472  O O   . ASN B 18  ? 0.8747 1.0900 0.9764 0.0085  -0.0267 -0.0178 18  ASN B O   
4473  C CB  . ASN B 18  ? 0.9079 1.1186 0.9990 0.0127  -0.0244 -0.0117 18  ASN B CB  
4474  C CG  . ASN B 18  ? 0.8960 1.1152 0.9906 0.0198  -0.0245 -0.0079 18  ASN B CG  
4475  O OD1 . ASN B 18  ? 0.9239 1.1551 1.0211 0.0201  -0.0293 -0.0073 18  ASN B OD1 
4476  N ND2 . ASN B 18  ? 0.9350 1.1466 1.0290 0.0251  -0.0189 -0.0042 18  ASN B ND2 
4483  N N   . ILE B 19  ? 0.9209 1.1059 1.0042 0.0067  -0.0185 -0.0156 19  ILE B N   
4484  C CA  . ILE B 19  ? 0.8912 1.0764 0.9771 0.0044  -0.0181 -0.0184 19  ILE B CA  
4485  C C   . ILE B 19  ? 0.8723 1.0767 0.9733 0.0108  -0.0170 -0.0172 19  ILE B C   
4486  O O   . ILE B 19  ? 0.8489 1.0572 0.9545 0.0187  -0.0117 -0.0122 19  ILE B O   
4487  C CB  . ILE B 19  ? 0.9400 1.0992 1.0075 0.0017  -0.0106 -0.0183 19  ILE B CB  
4488  C CG1 . ILE B 19  ? 0.9782 1.1168 1.0277 -0.0077 -0.0142 -0.0178 19  ILE B CG1 
4489  C CG2 . ILE B 19  ? 0.9179 1.0749 0.9851 -0.0025 -0.0101 -0.0213 19  ILE B CG2 
4490  C CD1 . ILE B 19  ? 0.9543 1.0949 1.0058 -0.0183 -0.0248 -0.0187 19  ILE B CD1 
4502  N N   . THR B 20  ? 0.8337 1.0500 0.9430 0.0069  -0.0225 -0.0204 20  THR B N   
4503  C CA  . THR B 20  ? 0.8423 1.0776 0.9654 0.0091  -0.0244 -0.0187 20  THR B CA  
4504  C C   . THR B 20  ? 0.8253 1.0605 0.9510 0.0037  -0.0243 -0.0218 20  THR B C   
4505  O O   . THR B 20  ? 0.8306 1.0561 0.9490 -0.0022 -0.0274 -0.0263 20  THR B O   
4506  C CB  . THR B 20  ? 0.8634 1.1113 0.9890 0.0074  -0.0326 -0.0195 20  THR B CB  
4507  O OG1 . THR B 20  ? 0.8524 1.1167 0.9880 0.0052  -0.0373 -0.0176 20  THR B OG1 
4508  C CG2 . THR B 20  ? 0.8270 1.0675 0.9461 0.0020  -0.0357 -0.0254 20  THR B CG2 
4516  N N   . ILE B 21  ? 0.8179 1.0644 0.9556 0.0061  -0.0204 -0.0180 21  ILE B N   
4517  C CA  . ILE B 21  ? 0.8079 1.0569 0.9498 0.0005  -0.0196 -0.0200 21  ILE B CA  
4518  C C   . ILE B 21  ? 0.8229 1.0946 0.9789 -0.0032 -0.0281 -0.0178 21  ILE B C   
4519  O O   . ILE B 21  ? 0.7794 1.0687 0.9487 0.0008  -0.0303 -0.0107 21  ILE B O   
4520  C CB  . ILE B 21  ? 0.8164 1.0588 0.9608 0.0046  -0.0061 -0.0163 21  ILE B CB  
4521  C CG1 . ILE B 21  ? 0.8641 1.0768 0.9858 0.0055  0.0015  -0.0188 21  ILE B CG1 
4522  C CG2 . ILE B 21  ? 0.8230 1.0676 0.9710 -0.0021 -0.0045 -0.0180 21  ILE B CG2 
4523  C CD1 . ILE B 21  ? 0.8511 1.0498 0.9687 0.0114  0.0186  -0.0152 21  ILE B CD1 
4535  N N   . LEU B 22  ? 0.8159 1.0855 0.9672 -0.0118 -0.0338 -0.0232 22  LEU B N   
4536  C CA  . LEU B 22  ? 0.7698 1.0545 0.9277 -0.0191 -0.0424 -0.0223 22  LEU B CA  
4537  C C   . LEU B 22  ? 0.8244 1.1153 0.9919 -0.0247 -0.0394 -0.0207 22  LEU B C   
4538  O O   . LEU B 22  ? 0.7448 1.0203 0.9042 -0.0264 -0.0337 -0.0249 22  LEU B O   
4539  C CB  . LEU B 22  ? 0.7776 1.0500 0.9191 -0.0250 -0.0491 -0.0299 22  LEU B CB  
4540  C CG  . LEU B 22  ? 0.8153 1.0875 0.9487 -0.0229 -0.0535 -0.0300 22  LEU B CG  
4541  C CD1 . LEU B 22  ? 0.8710 1.1437 1.0078 -0.0132 -0.0487 -0.0261 22  LEU B CD1 
4542  C CD2 . LEU B 22  ? 0.8209 1.0751 0.9380 -0.0253 -0.0537 -0.0376 22  LEU B CD2 
4554  N N   . ILE B 23  ? 0.8175 1.1317 1.0031 -0.0283 -0.0438 -0.0132 23  ILE B N   
4555  C CA  . ILE B 23  ? 0.7919 1.1176 0.9923 -0.0341 -0.0403 -0.0091 23  ILE B CA  
4556  C C   . ILE B 23  ? 0.8055 1.1353 1.0006 -0.0489 -0.0530 -0.0115 23  ILE B C   
4557  O O   . ILE B 23  ? 0.8047 1.1473 1.0019 -0.0544 -0.0648 -0.0074 23  ILE B O   
4558  C CB  . ILE B 23  ? 0.7847 1.1371 1.0157 -0.0272 -0.0345 0.0044  23  ILE B CB  
4559  C CG1 . ILE B 23  ? 0.7763 1.1162 1.0067 -0.0126 -0.0184 0.0058  23  ILE B CG1 
4560  C CG2 . ILE B 23  ? 0.7883 1.1577 1.0391 -0.0351 -0.0318 0.0103  23  ILE B CG2 
4561  C CD1 . ILE B 23  ? 0.8142 1.1230 1.0208 -0.0131 -0.0083 -0.0040 23  ILE B CD1 
4573  N N   . ASP B 24  ? 0.8090 1.1244 0.9935 -0.0564 -0.0509 -0.0177 24  ASP B N   
4574  C CA  . ASP B 24  ? 0.8570 1.1685 1.0308 -0.0713 -0.0609 -0.0212 24  ASP B CA  
4575  C C   . ASP B 24  ? 0.8452 1.1763 1.0388 -0.0811 -0.0607 -0.0137 24  ASP B C   
4576  O O   . ASP B 24  ? 0.8181 1.1590 1.0301 -0.0753 -0.0490 -0.0082 24  ASP B O   
4577  C CB  . ASP B 24  ? 0.8687 1.1489 1.0171 -0.0728 -0.0586 -0.0323 24  ASP B CB  
4578  C CG  . ASP B 24  ? 0.8839 1.1503 1.0125 -0.0850 -0.0677 -0.0378 24  ASP B CG  
4579  O OD1 . ASP B 24  ? 0.8729 1.1527 1.0041 -0.0957 -0.0772 -0.0336 24  ASP B OD1 
4580  O OD2 . ASP B 24  ? 0.9024 1.1428 1.0116 -0.0841 -0.0653 -0.0456 24  ASP B OD2 
4585  N N   . ASN B 25  ? 0.8192 1.1542 1.0075 -0.0971 -0.0731 -0.0131 25  ASN B N   
4586  C CA  . ASN B 25  ? 0.8124 1.1656 1.0183 -0.1103 -0.0751 -0.0058 25  ASN B CA  
4587  C C   . ASN B 25  ? 0.8079 1.2000 1.0552 -0.1047 -0.0714 0.0101  25  ASN B C   
4588  O O   . ASN B 25  ? 0.8849 1.2906 1.1544 -0.1046 -0.0607 0.0165  25  ASN B O   
4589  C CB  . ASN B 25  ? 0.8937 1.2265 1.0892 -0.1122 -0.0642 -0.0125 25  ASN B CB  
4590  C CG  . ASN B 25  ? 0.9155 1.2101 1.0753 -0.1116 -0.0650 -0.0261 25  ASN B CG  
4591  O OD1 . ASN B 25  ? 0.9278 1.2070 1.0666 -0.1229 -0.0741 -0.0313 25  ASN B OD1 
4592  N ND2 . ASN B 25  ? 0.9418 1.2197 1.0941 -0.0985 -0.0551 -0.0308 25  ASN B ND2 
4599  N N   . PHE B 26  ? 0.8119 1.2211 1.0698 -0.0995 -0.0794 0.0173  26  PHE B N   
4600  C CA  . PHE B 26  ? 0.8332 1.2799 1.1326 -0.0916 -0.0769 0.0346  26  PHE B CA  
4601  C C   . PHE B 26  ? 0.8544 1.3227 1.1604 -0.1026 -0.0986 0.0447  26  PHE B C   
4602  O O   . PHE B 26  ? 0.8768 1.3246 1.1509 -0.1067 -0.1094 0.0364  26  PHE B O   
4603  C CB  . PHE B 26  ? 0.8414 1.2814 1.1449 -0.0690 -0.0613 0.0342  26  PHE B CB  
4604  C CG  . PHE B 26  ? 0.8205 1.2929 1.1672 -0.0568 -0.0511 0.0517  26  PHE B CG  
4605  C CD1 . PHE B 26  ? 0.8837 1.3630 1.2519 -0.0516 -0.0319 0.0568  26  PHE B CD1 
4606  C CD2 . PHE B 26  ? 0.8046 1.2981 1.1695 -0.0495 -0.0590 0.0637  26  PHE B CD2 
4607  C CE1 . PHE B 26  ? 0.8779 1.3852 1.2874 -0.0379 -0.0188 0.0738  26  PHE B CE1 
4608  C CE2 . PHE B 26  ? 0.8196 1.3424 1.2268 -0.0359 -0.0483 0.0815  26  PHE B CE2 
4609  C CZ  . PHE B 26  ? 0.8326 1.3624 1.2633 -0.0294 -0.0271 0.0867  26  PHE B CZ  
4619  N N   . ASP B 27  ? 0.8341 1.3428 1.1806 -0.1083 -0.1049 0.0636  27  ASP B N   
4620  C CA  . ASP B 27  ? 0.8185 1.3511 1.1744 -0.1192 -0.1277 0.0770  27  ASP B CA  
4621  C C   . ASP B 27  ? 0.8309 1.3563 1.1781 -0.1030 -0.1277 0.0767  27  ASP B C   
4622  O O   . ASP B 27  ? 0.8278 1.3696 1.2046 -0.0833 -0.1149 0.0862  27  ASP B O   
4623  C CB  . ASP B 27  ? 0.7719 1.3556 1.1838 -0.1233 -0.1323 0.1015  27  ASP B CB  
4624  C CG  . ASP B 27  ? 0.8201 1.4320 1.2472 -0.1313 -0.1564 0.1192  27  ASP B CG  
4625  O OD1 . ASP B 27  ? 0.8805 1.4697 1.2664 -0.1449 -0.1747 0.1113  27  ASP B OD1 
4626  O OD2 . ASP B 27  ? 0.8248 1.4807 1.3050 -0.1238 -0.1563 0.1422  27  ASP B OD2 
4631  N N   . ILE B 28  ? 0.8540 1.3518 1.1588 -0.1108 -0.1399 0.0656  28  ILE B N   
4632  C CA  . ILE B 28  ? 0.8782 1.3647 1.1699 -0.0963 -0.1385 0.0635  28  ILE B CA  
4633  C C   . ILE B 28  ? 0.8553 1.3765 1.1774 -0.0941 -0.1515 0.0849  28  ILE B C   
4634  O O   . ILE B 28  ? 0.8474 1.3639 1.1663 -0.0796 -0.1484 0.0867  28  ILE B O   
4635  C CB  . ILE B 28  ? 0.8968 1.3437 1.1351 -0.1056 -0.1457 0.0468  28  ILE B CB  
4636  C CG1 . ILE B 28  ? 0.9372 1.3882 1.1586 -0.1283 -0.1706 0.0540  28  ILE B CG1 
4637  C CG2 . ILE B 28  ? 0.8880 1.3035 1.1003 -0.1095 -0.1353 0.0289  28  ILE B CG2 
4638  C CD1 . ILE B 28  ? 0.9441 1.3504 1.1083 -0.1411 -0.1748 0.0366  28  ILE B CD1 
4650  N N   . TYR B 29  ? 0.8405 1.3975 1.1936 -0.1085 -0.1666 0.1028  29  TYR B N   
4651  C CA  . TYR B 29  ? 0.8393 1.4356 1.2293 -0.1070 -0.1811 0.1275  29  TYR B CA  
4652  C C   . TYR B 29  ? 0.7989 1.4376 1.2524 -0.0931 -0.1678 0.1469  29  TYR B C   
4653  O O   . TYR B 29  ? 0.8375 1.5188 1.3338 -0.0959 -0.1816 0.1720  29  TYR B O   
4654  C CB  . TYR B 29  ? 0.8568 1.4632 1.2340 -0.1368 -0.2125 0.1368  29  TYR B CB  
4655  C CG  . TYR B 29  ? 0.9156 1.4752 1.2259 -0.1507 -0.2228 0.1179  29  TYR B CG  
4656  C CD1 . TYR B 29  ? 0.9239 1.4687 1.2108 -0.1440 -0.2282 0.1176  29  TYR B CD1 
4657  C CD2 . TYR B 29  ? 0.9679 1.4958 1.2379 -0.1697 -0.2250 0.1009  29  TYR B CD2 
4658  C CE1 . TYR B 29  ? 0.9830 1.4833 1.2086 -0.1559 -0.2342 0.1008  29  TYR B CE1 
4659  C CE2 . TYR B 29  ? 1.0434 1.5256 1.2524 -0.1806 -0.2305 0.0843  29  TYR B CE2 
4660  C CZ  . TYR B 29  ? 1.0313 1.5002 1.2186 -0.1735 -0.2344 0.0843  29  TYR B CZ  
4661  O OH  . TYR B 29  ? 1.1664 1.5882 1.2926 -0.1837 -0.2365 0.0680  29  TYR B OH  
4671  N N   . ASP B 30  ? 0.8177 1.4445 1.2775 -0.0782 -0.1408 0.1368  30  ASP B N   
4672  C CA  . ASP B 30  ? 0.8226 1.4819 1.3374 -0.0627 -0.1219 0.1533  30  ASP B CA  
4673  C C   . ASP B 30  ? 0.8086 1.4826 1.3512 -0.0388 -0.1140 0.1685  30  ASP B C   
4674  O O   . ASP B 30  ? 0.8016 1.4478 1.3131 -0.0286 -0.1124 0.1586  30  ASP B O   
4675  C CB  . ASP B 30  ? 0.7995 1.4315 1.3015 -0.0534 -0.0940 0.1363  30  ASP B CB  
4676  C CG  . ASP B 30  ? 0.7973 1.4590 1.3513 -0.0419 -0.0725 0.1521  30  ASP B CG  
4677  O OD1 . ASP B 30  ? 0.8314 1.5001 1.4105 -0.0185 -0.0541 0.1621  30  ASP B OD1 
4678  O OD2 . ASP B 30  ? 0.7721 1.4474 1.3401 -0.0559 -0.0720 0.1544  30  ASP B OD2 
4683  N N   . LYS B 31  ? 0.7944 1.5128 1.3977 -0.0294 -0.1079 0.1938  31  LYS B N   
4684  C CA  . LYS B 31  ? 0.8124 1.5489 1.4483 -0.0068 -0.1020 0.2128  31  LYS B CA  
4685  C C   . LYS B 31  ? 0.8340 1.5391 1.4609 0.0210  -0.0671 0.2024  31  LYS B C   
4686  O O   . LYS B 31  ? 0.8563 1.5536 1.4827 0.0387  -0.0623 0.2078  31  LYS B O   
4687  C CB  . LYS B 31  ? 0.8239 1.6210 1.5332 -0.0052 -0.1064 0.2462  31  LYS B CB  
4688  C CG  . LYS B 31  ? 0.8756 1.7063 1.5962 -0.0361 -0.1429 0.2595  31  LYS B CG  
4689  C CD  . LYS B 31  ? 0.9333 1.8280 1.7296 -0.0328 -0.1536 0.2981  31  LYS B CD  
4690  C CE  . LYS B 31  ? 0.9601 1.8890 1.7684 -0.0677 -0.1904 0.3123  31  LYS B CE  
4691  N NZ  . LYS B 31  ? 0.9115 1.8608 1.7475 -0.0798 -0.1809 0.3142  31  LYS B NZ  
4705  N N   . ASN B 32  ? 0.8024 1.4863 1.4187 0.0239  -0.0432 0.1881  32  ASN B N   
4706  C CA  . ASN B 32  ? 0.8176 1.4667 1.4194 0.0468  -0.0101 0.1782  32  ASN B CA  
4707  C C   . ASN B 32  ? 0.8265 1.4230 1.3643 0.0451  -0.0103 0.1513  32  ASN B C   
4708  O O   . ASN B 32  ? 0.8286 1.3907 1.3459 0.0604  0.0140  0.1414  32  ASN B O   
4709  C CB  . ASN B 32  ? 0.8385 1.4861 1.4550 0.0493  0.0161  0.1763  32  ASN B CB  
4710  C CG  . ASN B 32  ? 0.8309 1.5301 1.5178 0.0571  0.0251  0.2052  32  ASN B CG  
4711  O OD1 . ASN B 32  ? 0.8301 1.5754 1.5544 0.0454  0.0002  0.2245  32  ASN B OD1 
4712  N ND2 . ASN B 32  ? 0.8273 1.5182 1.5322 0.0763  0.0611  0.2094  32  ASN B ND2 
4719  N N   . ILE B 33  ? 0.8229 1.4113 1.3284 0.0264  -0.0363 0.1403  33  ILE B N   
4720  C CA  . ILE B 33  ? 0.8309 1.3737 1.2812 0.0251  -0.0365 0.1171  33  ILE B CA  
4721  C C   . ILE B 33  ? 0.8442 1.3672 1.2859 0.0454  -0.0232 0.1179  33  ILE B C   
4722  O O   . ILE B 33  ? 0.8454 1.3300 1.2547 0.0517  -0.0071 0.1020  33  ILE B O   
4723  C CB  . ILE B 33  ? 0.8207 1.3610 1.2432 0.0046  -0.0649 0.1096  33  ILE B CB  
4724  C CG1 . ILE B 33  ? 0.8527 1.3876 1.2611 -0.0147 -0.0703 0.0982  33  ILE B CG1 
4725  C CG2 . ILE B 33  ? 0.7847 1.2889 1.1638 0.0085  -0.0660 0.0944  33  ILE B CG2 
4726  C CD1 . ILE B 33  ? 0.8418 1.3644 1.2152 -0.0349 -0.0936 0.0882  33  ILE B CD1 
4738  N N   . PRO B 34  ? 0.8380 1.3829 1.3050 0.0554  -0.0297 0.1362  34  PRO B N   
4739  C CA  . PRO B 34  ? 0.8341 1.3549 1.2882 0.0742  -0.0164 0.1361  34  PRO B CA  
4740  C C   . PRO B 34  ? 0.8513 1.3482 1.3060 0.0918  0.0167  0.1330  34  PRO B C   
4741  O O   . PRO B 34  ? 0.8480 1.3063 1.2695 0.1003  0.0293  0.1220  34  PRO B O   
4742  C CB  . PRO B 34  ? 0.8345 1.3911 1.3270 0.0820  -0.0287 0.1616  34  PRO B CB  
4743  C CG  . PRO B 34  ? 0.8405 1.4317 1.3472 0.0600  -0.0580 0.1693  34  PRO B CG  
4744  C CD  . PRO B 34  ? 0.8133 1.4056 1.3219 0.0490  -0.0504 0.1594  34  PRO B CD  
4752  N N   . LYS B 35  ? 0.8539 1.3707 1.3432 0.0960  0.0319  0.1428  35  LYS B N   
4753  C CA  . LYS B 35  ? 0.8470 1.3385 1.3353 0.1125  0.0663  0.1412  35  LYS B CA  
4754  C C   . LYS B 35  ? 0.8650 1.3194 1.3114 0.1014  0.0759  0.1184  35  LYS B C   
4755  O O   . LYS B 35  ? 0.8771 1.2877 1.2897 0.1092  0.0964  0.1073  35  LYS B O   
4756  C CB  . LYS B 35  ? 0.8499 1.3807 1.3979 0.1237  0.0812  0.1645  35  LYS B CB  
4757  C CG  . LYS B 35  ? 0.8705 1.4581 1.4698 0.1208  0.0566  0.1890  35  LYS B CG  
4758  C CD  . LYS B 35  ? 0.8935 1.5255 1.5580 0.1298  0.0708  0.2136  35  LYS B CD  
4759  C CE  . LYS B 35  ? 0.9400 1.5644 1.6302 0.1603  0.1042  0.2288  35  LYS B CE  
4760  N NZ  . LYS B 35  ? 0.9337 1.5841 1.6744 0.1703  0.1308  0.2451  35  LYS B NZ  
4774  N N   . LEU B 36  ? 0.8727 1.3418 1.3187 0.0823  0.0605  0.1120  36  LEU B N   
4775  C CA  . LEU B 36  ? 0.8701 1.3043 1.2749 0.0706  0.0651  0.0911  36  LEU B CA  
4776  C C   . LEU B 36  ? 0.8910 1.2850 1.2470 0.0689  0.0599  0.0742  36  LEU B C   
4777  O O   . LEU B 36  ? 0.9030 1.2570 1.2249 0.0702  0.0751  0.0620  36  LEU B O   
4778  C CB  . LEU B 36  ? 0.8585 1.3136 1.2673 0.0496  0.0447  0.0871  36  LEU B CB  
4779  C CG  . LEU B 36  ? 0.8811 1.3740 1.3340 0.0454  0.0483  0.1017  36  LEU B CG  
4780  C CD1 . LEU B 36  ? 0.8992 1.3927 1.3369 0.0229  0.0326  0.0909  36  LEU B CD1 
4781  C CD2 . LEU B 36  ? 0.9040 1.3872 1.3708 0.0598  0.0820  0.1071  36  LEU B CD2 
4793  N N   . SER B 37  ? 0.8921 1.2959 1.2435 0.0647  0.0380  0.0743  37  SER B N   
4794  C CA  . SER B 37  ? 0.8867 1.2573 1.1967 0.0622  0.0324  0.0600  37  SER B CA  
4795  C C   . SER B 37  ? 0.9133 1.2521 1.2073 0.0774  0.0531  0.0599  37  SER B C   
4796  O O   . SER B 37  ? 0.9321 1.2341 1.1880 0.0737  0.0571  0.0463  37  SER B O   
4797  C CB  . SER B 37  ? 0.8864 1.2738 1.1968 0.0566  0.0087  0.0627  37  SER B CB  
4798  O OG  . SER B 37  ? 0.8318 1.2395 1.1472 0.0403  -0.0100 0.0607  37  SER B OG  
4804  N N   . GLU B 38  ? 0.9310 1.2826 1.2536 0.0940  0.0665  0.0759  38  GLU B N   
4805  C CA  . GLU B 38  ? 0.9704 1.2862 1.2744 0.1089  0.0889  0.0760  38  GLU B CA  
4806  C C   . GLU B 38  ? 0.9617 1.2374 1.2348 0.1066  0.1103  0.0641  38  GLU B C   
4807  O O   . GLU B 38  ? 0.9949 1.2269 1.2271 0.1064  0.1187  0.0540  38  GLU B O   
4808  C CB  . GLU B 38  ? 0.9580 1.2948 1.3027 0.1292  0.1029  0.0973  38  GLU B CB  
4809  C CG  . GLU B 38  ? 1.0556 1.3523 1.3790 0.1458  0.1259  0.0984  38  GLU B CG  
4810  C CD  . GLU B 38  ? 1.1217 1.4420 1.4869 0.1669  0.1343  0.1213  38  GLU B CD  
4811  O OE1 . GLU B 38  ? 1.1248 1.4837 1.5389 0.1741  0.1394  0.1379  38  GLU B OE1 
4812  O OE2 . GLU B 38  ? 1.1173 1.4183 1.4682 0.1763  0.1356  0.1242  38  GLU B OE2 
4819  N N   . GLU B 39  ? 0.9379 1.2263 1.2277 0.1032  0.1187  0.0657  39  GLU B N   
4820  C CA  . GLU B 39  ? 0.9556 1.2038 1.2119 0.0989  0.1381  0.0545  39  GLU B CA  
4821  C C   . GLU B 39  ? 0.9304 1.1536 1.1440 0.0803  0.1211  0.0365  39  GLU B C   
4822  O O   . GLU B 39  ? 0.9637 1.1411 1.1344 0.0765  0.1312  0.0264  39  GLU B O   
4823  C CB  . GLU B 39  ? 0.9364 1.2063 1.2215 0.0982  0.1500  0.0610  39  GLU B CB  
4824  C CG  . GLU B 39  ? 0.9373 1.2348 1.2714 0.1175  0.1703  0.0815  39  GLU B CG  
4825  C CD  . GLU B 39  ? 1.0472 1.3022 1.3625 0.1356  0.2043  0.0838  39  GLU B CD  
4826  O OE1 . GLU B 39  ? 1.0765 1.2902 1.3485 0.1356  0.2046  0.0737  39  GLU B OE1 
4827  O OE2 . GLU B 39  ? 1.0692 1.3307 1.4125 0.1497  0.2320  0.0963  39  GLU B OE2 
4834  N N   . ILE B 40  ? 0.9282 1.1795 1.1524 0.0682  0.0954  0.0334  40  ILE B N   
4835  C CA  . ILE B 40  ? 0.9489 1.1807 1.1396 0.0525  0.0800  0.0187  40  ILE B CA  
4836  C C   . ILE B 40  ? 0.9585 1.1571 1.1152 0.0529  0.0789  0.0122  40  ILE B C   
4837  O O   . ILE B 40  ? 0.9433 1.1118 1.0661 0.0422  0.0761  0.0020  40  ILE B O   
4838  C CB  . ILE B 40  ? 0.9117 1.1773 1.1199 0.0426  0.0549  0.0179  40  ILE B CB  
4839  C CG1 . ILE B 40  ? 0.8781 1.1740 1.1162 0.0382  0.0541  0.0240  40  ILE B CG1 
4840  C CG2 . ILE B 40  ? 0.8951 1.1414 1.0729 0.0294  0.0408  0.0047  40  ILE B CG2 
4841  C CD1 . ILE B 40  ? 0.9134 1.1939 1.1478 0.0387  0.0749  0.0237  40  ILE B CD1 
4853  N N   . MET B 41  ? 0.9631 1.1668 1.1287 0.0639  0.0798  0.0193  41  MET B N   
4854  C CA  . MET B 41  ? 0.9537 1.1317 1.0904 0.0620  0.0749  0.0139  41  MET B CA  
4855  C C   . MET B 41  ? 0.9794 1.1097 1.0817 0.0657  0.0953  0.0113  41  MET B C   
4856  O O   . MET B 41  ? 0.9918 1.0933 1.0612 0.0574  0.0901  0.0042  41  MET B O   
4857  C CB  . MET B 41  ? 0.9467 1.1472 1.1032 0.0709  0.0662  0.0226  41  MET B CB  
4858  C CG  . MET B 41  ? 0.9116 1.1525 1.0936 0.0651  0.0451  0.0250  41  MET B CG  
4859  S SD  . MET B 41  ? 0.8773 1.1430 1.0814 0.0755  0.0364  0.0383  41  MET B SD  
4860  C CE  . MET B 41  ? 0.8779 1.1260 1.0509 0.0661  0.0225  0.0279  41  MET B CE  
4870  N N   . LYS B 42  ? 0.9773 1.0973 1.0856 0.0773  0.1192  0.0175  42  LYS B N   
4871  C CA  . LYS B 42  ? 0.9734 1.0410 1.0432 0.0811  0.1419  0.0148  42  LYS B CA  
4872  C C   . LYS B 42  ? 1.0016 1.0301 1.0235 0.0618  0.1360  0.0016  42  LYS B C   
4873  O O   . LYS B 42  ? 1.0398 1.0805 1.0630 0.0492  0.1231  -0.0038 42  LYS B O   
4874  C CB  . LYS B 42  ? 0.9928 1.0541 1.0755 0.0948  0.1711  0.0222  42  LYS B CB  
4875  C CG  . LYS B 42  ? 1.0336 1.1261 1.1619 0.1163  0.1812  0.0387  42  LYS B CG  
4876  C CD  . LYS B 42  ? 1.0397 1.1136 1.1740 0.1322  0.2169  0.0465  42  LYS B CD  
4877  C CE  . LYS B 42  ? 1.0538 1.1831 1.2544 0.1487  0.2211  0.0655  42  LYS B CE  
4878  N NZ  . LYS B 42  ? 1.1012 1.2301 1.3216 0.1713  0.2361  0.0804  42  LYS B NZ  
4892  N N   . GLU B 43  ? 0.9940 0.9739 0.9724 0.0584  0.1447  -0.0024 43  GLU B N   
4893  C CA  . GLU B 43  ? 1.1295 1.0687 1.0597 0.0383  0.1390  -0.0125 43  GLU B CA  
4894  C C   . GLU B 43  ? 1.0899 1.0051 1.0016 0.0348  0.1564  -0.0156 43  GLU B C   
4895  O O   . GLU B 43  ? 1.0982 1.0000 0.9861 0.0171  0.1447  -0.0222 43  GLU B O   
4896  C CB  . GLU B 43  ? 1.1840 1.0731 1.0684 0.0332  0.1445  -0.0151 43  GLU B CB  
4897  C CG  . GLU B 43  ? 1.2393 1.0715 1.0834 0.0383  0.1759  -0.0160 43  GLU B CG  
4898  C CD  . GLU B 43  ? 1.3405 1.1244 1.1418 0.0350  0.1818  -0.0174 43  GLU B CD  
4899  O OE1 . GLU B 43  ? 1.3979 1.1624 1.1672 0.0141  0.1624  -0.0228 43  GLU B OE1 
4900  O OE2 . GLU B 43  ? 1.4001 1.1661 1.2014 0.0531  0.2055  -0.0119 43  GLU B OE2 
4907  N N   . THR B 44  ? 1.0754 0.9854 0.9990 0.0516  0.1847  -0.0096 44  THR B N   
4908  C CA  . THR B 44  ? 1.1104 0.9981 1.0181 0.0494  0.2049  -0.0118 44  THR B CA  
4909  C C   . THR B 44  ? 1.0395 0.9723 0.9822 0.0438  0.1907  -0.0114 44  THR B C   
4910  O O   . THR B 44  ? 1.0487 0.9630 0.9740 0.0370  0.2020  -0.0147 44  THR B O   
4911  C CB  . THR B 44  ? 1.1189 0.9944 1.0383 0.0713  0.2416  -0.0033 44  THR B CB  
4912  O OG1 . THR B 44  ? 1.1276 1.0659 1.1145 0.0862  0.2409  0.0082  44  THR B OG1 
4913  C CG2 . THR B 44  ? 1.1682 1.0122 1.0687 0.0823  0.2541  -0.0005 44  THR B CG2 
4921  N N   . ASN B 45  ? 1.0398 1.0274 1.0277 0.0459  0.1675  -0.0076 45  ASN B N   
4922  C CA  . ASN B 45  ? 0.9965 1.0225 1.0111 0.0376  0.1498  -0.0087 45  ASN B CA  
4923  C C   . ASN B 45  ? 0.9660 0.9928 0.9648 0.0216  0.1206  -0.0161 45  ASN B C   
4924  O O   . ASN B 45  ? 1.0002 0.9927 0.9623 0.0139  0.1164  -0.0206 45  ASN B O   
4925  C CB  . ASN B 45  ? 0.9564 1.0390 1.0302 0.0509  0.1470  0.0021  45  ASN B CB  
4926  C CG  . ASN B 45  ? 0.9661 1.0830 1.0658 0.0427  0.1355  0.0022  45  ASN B CG  
4927  O OD1 . ASN B 45  ? 0.9605 1.0951 1.0634 0.0319  0.1109  -0.0026 45  ASN B OD1 
4928  N ND2 . ASN B 45  ? 0.9691 1.0938 1.0868 0.0478  0.1548  0.0081  45  ASN B ND2 
4935  N N   . LEU B 46  ? 0.9693 1.0341 0.9955 0.0162  0.1012  -0.0166 46  LEU B N   
4936  C CA  . LEU B 46  ? 0.9166 0.9928 0.9419 0.0072  0.0758  -0.0205 46  LEU B CA  
4937  C C   . LEU B 46  ? 1.0021 1.0852 1.0353 0.0162  0.0732  -0.0169 46  LEU B C   
4938  O O   . LEU B 46  ? 1.0154 1.1108 1.0689 0.0304  0.0855  -0.0099 46  LEU B O   
4939  C CB  . LEU B 46  ? 0.9139 1.0293 0.9699 0.0038  0.0597  -0.0204 46  LEU B CB  
4940  C CG  . LEU B 46  ? 0.9362 1.0496 0.9808 -0.0092 0.0390  -0.0261 46  LEU B CG  
4941  C CD1 . LEU B 46  ? 0.9330 1.0125 0.9445 -0.0215 0.0409  -0.0301 46  LEU B CD1 
4942  C CD2 . LEU B 46  ? 0.8788 1.0278 0.9523 -0.0104 0.0257  -0.0260 46  LEU B CD2 
4954  N N   . TYR B 47  ? 1.0381 1.1133 1.0562 0.0081  0.0579  -0.0203 47  TYR B N   
4955  C CA  . TYR B 47  ? 1.0121 1.0880 1.0316 0.0144  0.0561  -0.0174 47  TYR B CA  
4956  C C   . TYR B 47  ? 0.9544 1.0676 1.0011 0.0146  0.0375  -0.0165 47  TYR B C   
4957  O O   . TYR B 47  ? 0.9071 1.0321 0.9582 0.0057  0.0238  -0.0201 47  TYR B O   
4958  C CB  . TYR B 47  ? 1.0418 1.0767 1.0208 0.0038  0.0549  -0.0209 47  TYR B CB  
4959  C CG  . TYR B 47  ? 1.0578 1.0893 1.0350 0.0095  0.0549  -0.0178 47  TYR B CG  
4960  C CD1 . TYR B 47  ? 1.0668 1.0832 1.0402 0.0229  0.0737  -0.0134 47  TYR B CD1 
4961  C CD2 . TYR B 47  ? 1.1167 1.1600 1.0975 0.0023  0.0374  -0.0182 47  TYR B CD2 
4962  C CE1 . TYR B 47  ? 1.1308 1.1422 1.1012 0.0281  0.0735  -0.0101 47  TYR B CE1 
4963  C CE2 . TYR B 47  ? 1.1657 1.2054 1.1439 0.0066  0.0377  -0.0151 47  TYR B CE2 
4964  C CZ  . TYR B 47  ? 1.1872 1.2100 1.1587 0.0190  0.0550  -0.0113 47  TYR B CZ  
4965  O OH  . TYR B 47  ? 1.2748 1.2916 1.2419 0.0230  0.0551  -0.0079 47  TYR B OH  
4975  N N   . ALA B 48  ? 0.9912 1.1203 1.0542 0.0252  0.0382  -0.0111 48  ALA B N   
4976  C CA  . ALA B 48  ? 0.9507 1.1095 1.0331 0.0250  0.0227  -0.0102 48  ALA B CA  
4977  C C   . ALA B 48  ? 0.9315 1.1001 1.0246 0.0360  0.0247  -0.0032 48  ALA B C   
4978  O O   . ALA B 48  ? 0.9016 1.0682 1.0021 0.0473  0.0377  0.0035  48  ALA B O   
4979  C CB  . ALA B 48  ? 0.8904 1.0793 0.9967 0.0234  0.0152  -0.0103 48  ALA B CB  
4985  N N   . GLU B 49  ? 0.9126 1.0912 1.0070 0.0334  0.0129  -0.0037 49  GLU B N   
4986  C CA  . GLU B 49  ? 0.9396 1.1295 1.0433 0.0422  0.0119  0.0033  49  GLU B CA  
4987  C C   . GLU B 49  ? 0.8930 1.1168 1.0216 0.0443  0.0022  0.0079  49  GLU B C   
4988  O O   . GLU B 49  ? 0.9002 1.1356 1.0382 0.0514  -0.0001 0.0160  49  GLU B O   
4989  C CB  . GLU B 49  ? 0.9086 1.0882 0.9971 0.0372  0.0057  0.0010  49  GLU B CB  
4990  C CG  . GLU B 49  ? 0.9967 1.1457 1.0600 0.0285  0.0090  -0.0038 49  GLU B CG  
4991  C CD  . GLU B 49  ? 1.0359 1.1779 1.0886 0.0235  0.0038  -0.0036 49  GLU B CD  
4992  O OE1 . GLU B 49  ? 0.9811 1.1406 1.0431 0.0190  -0.0056 -0.0053 49  GLU B OE1 
4993  O OE2 . GLU B 49  ? 1.0563 1.1734 1.0903 0.0240  0.0106  -0.0014 49  GLU B OE2 
5000  N N   . GLN B 50  ? 0.9598 1.1976 1.0969 0.0372  -0.0043 0.0037  50  GLN B N   
5001  C CA  . GLN B 50  ? 0.9171 1.1826 1.0714 0.0350  -0.0155 0.0072  50  GLN B CA  
5002  C C   . GLN B 50  ? 0.8508 1.1273 1.0169 0.0300  -0.0158 0.0055  50  GLN B C   
5003  O O   . GLN B 50  ? 0.8382 1.0996 0.9948 0.0261  -0.0100 -0.0009 50  GLN B O   
5004  C CB  . GLN B 50  ? 0.8823 1.1486 1.0253 0.0273  -0.0268 0.0015  50  GLN B CB  
5005  C CG  . GLN B 50  ? 0.8963 1.1711 1.0390 0.0299  -0.0334 0.0077  50  GLN B CG  
5006  C CD  . GLN B 50  ? 0.9476 1.2111 1.0721 0.0249  -0.0366 0.0014  50  GLN B CD  
5007  O OE1 . GLN B 50  ? 0.9324 1.1899 1.0506 0.0184  -0.0373 -0.0066 50  GLN B OE1 
5008  N NE2 . GLN B 50  ? 1.0188 1.2791 1.1362 0.0285  -0.0375 0.0062  50  GLN B NE2 
5017  N N   . VAL B 51  ? 0.8512 1.1535 1.0365 0.0284  -0.0238 0.0121  51  VAL B N   
5018  C CA  . VAL B 51  ? 0.8110 1.1265 1.0090 0.0218  -0.0255 0.0118  51  VAL B CA  
5019  C C   . VAL B 51  ? 0.8193 1.1549 1.0230 0.0123  -0.0419 0.0142  51  VAL B C   
5020  O O   . VAL B 51  ? 0.8262 1.1774 1.0394 0.0145  -0.0497 0.0238  51  VAL B O   
5021  C CB  . VAL B 51  ? 0.8296 1.1564 1.0513 0.0302  -0.0130 0.0217  51  VAL B CB  
5022  C CG1 . VAL B 51  ? 0.8135 1.1545 1.0486 0.0216  -0.0146 0.0216  51  VAL B CG1 
5023  C CG2 . VAL B 51  ? 0.8483 1.1467 1.0557 0.0385  0.0052  0.0186  51  VAL B CG2 
5033  N N   . GLY B 52  ? 0.7921 1.1243 0.9871 0.0010  -0.0476 0.0061  52  GLY B N   
5034  C CA  . GLY B 52  ? 0.8063 1.1501 0.9992 -0.0107 -0.0623 0.0070  52  GLY B CA  
5035  C C   . GLY B 52  ? 0.7684 1.1190 0.9684 -0.0208 -0.0643 0.0055  52  GLY B C   
5036  O O   . GLY B 52  ? 0.8078 1.1484 1.0075 -0.0195 -0.0545 0.0004  52  GLY B O   
5040  N N   . PHE B 53  ? 0.7785 1.1443 0.9821 -0.0327 -0.0781 0.0105  53  PHE B N   
5041  C CA  . PHE B 53  ? 0.7577 1.1323 0.9687 -0.0451 -0.0823 0.0109  53  PHE B CA  
5042  C C   . PHE B 53  ? 0.7994 1.1591 0.9821 -0.0608 -0.0949 0.0033  53  PHE B C   
5043  O O   . PHE B 53  ? 0.8435 1.2081 1.0178 -0.0681 -0.1078 0.0080  53  PHE B O   
5044  C CB  . PHE B 53  ? 0.7526 1.1628 0.9998 -0.0463 -0.0867 0.0279  53  PHE B CB  
5045  C CG  . PHE B 53  ? 0.7501 1.1708 1.0240 -0.0291 -0.0700 0.0357  53  PHE B CG  
5046  C CD1 . PHE B 53  ? 0.7548 1.1735 1.0310 -0.0147 -0.0649 0.0402  53  PHE B CD1 
5047  C CD2 . PHE B 53  ? 0.7940 1.2218 1.0868 -0.0277 -0.0575 0.0383  53  PHE B CD2 
5048  C CE1 . PHE B 53  ? 0.7993 1.2206 1.0947 0.0012  -0.0472 0.0468  53  PHE B CE1 
5049  C CE2 . PHE B 53  ? 0.7859 1.2166 1.0977 -0.0116 -0.0387 0.0449  53  PHE B CE2 
5050  C CZ  . PHE B 53  ? 0.7892 1.2154 1.1015 0.0030  -0.0333 0.0490  53  PHE B CZ  
5060  N N   . ILE B 54  ? 0.8198 1.1582 0.9852 -0.0662 -0.0906 -0.0080 54  ILE B N   
5061  C CA  . ILE B 54  ? 0.8572 1.1703 0.9895 -0.0769 -0.0963 -0.0180 54  ILE B CA  
5062  C C   . ILE B 54  ? 0.8700 1.1845 0.9980 -0.0950 -0.1052 -0.0174 54  ILE B C   
5063  O O   . ILE B 54  ? 0.8786 1.2051 1.0256 -0.0971 -0.1018 -0.0144 54  ILE B O   
5064  C CB  . ILE B 54  ? 0.8649 1.1502 0.9807 -0.0686 -0.0845 -0.0299 54  ILE B CB  
5065  C CG1 . ILE B 54  ? 0.8537 1.1388 0.9822 -0.0658 -0.0761 -0.0313 54  ILE B CG1 
5066  C CG2 . ILE B 54  ? 0.8485 1.1308 0.9646 -0.0545 -0.0781 -0.0301 54  ILE B CG2 
5067  C CD1 . ILE B 54  ? 0.8344 1.0932 0.9474 -0.0609 -0.0684 -0.0407 54  ILE B CD1 
5079  N N   . LYS B 55  ? 0.9092 1.2086 1.0089 -0.1094 -0.1161 -0.0204 55  LYS B N   
5080  C CA  . LYS B 55  ? 0.9419 1.2334 1.0273 -0.1296 -0.1252 -0.0217 55  LYS B CA  
5081  C C   . LYS B 55  ? 0.9647 1.2164 1.0028 -0.1387 -0.1269 -0.0327 55  LYS B C   
5082  O O   . LYS B 55  ? 0.9881 1.2333 1.0082 -0.1405 -0.1325 -0.0316 55  LYS B O   
5083  C CB  . LYS B 55  ? 0.9421 1.2674 1.0493 -0.1441 -0.1420 -0.0063 55  LYS B CB  
5084  C CG  . LYS B 55  ? 0.9646 1.2803 1.0529 -0.1694 -0.1544 -0.0067 55  LYS B CG  
5085  C CD  . LYS B 55  ? 1.0268 1.3793 1.1554 -0.1769 -0.1587 0.0061  55  LYS B CD  
5086  C CE  . LYS B 55  ? 1.0636 1.4512 1.2127 -0.1919 -0.1798 0.0246  55  LYS B CE  
5087  N NZ  . LYS B 55  ? 1.0952 1.5271 1.2961 -0.1938 -0.1802 0.0406  55  LYS B NZ  
5101  N N   . ASP B 56  ? 0.9762 1.1985 0.9923 -0.1440 -0.1205 -0.0429 56  ASP B N   
5102  C CA  . ASP B 56  ? 1.0469 1.2244 1.0162 -0.1500 -0.1165 -0.0544 56  ASP B CA  
5103  C C   . ASP B 56  ? 1.0134 1.1810 0.9771 -0.1322 -0.1055 -0.0583 56  ASP B C   
5104  O O   . ASP B 56  ? 0.9935 1.1721 0.9820 -0.1140 -0.0949 -0.0584 56  ASP B O   
5105  C CB  . ASP B 56  ? 1.0546 1.2210 0.9932 -0.1753 -0.1331 -0.0520 56  ASP B CB  
5106  C CG  . ASP B 56  ? 1.0974 1.2813 1.0495 -0.1939 -0.1454 -0.0453 56  ASP B CG  
5107  O OD1 . ASP B 56  ? 1.0944 1.2783 1.0606 -0.1898 -0.1369 -0.0482 56  ASP B OD1 
5108  O OD2 . ASP B 56  ? 1.1619 1.3595 1.1103 -0.2139 -0.1643 -0.0359 56  ASP B OD2 
5113  N N   . SER B 57  ? 1.0803 1.2262 1.0105 -0.1381 -0.1076 -0.0611 57  SER B N   
5114  C CA  . SER B 57  ? 1.0380 1.1748 0.9624 -0.1227 -0.0965 -0.0639 57  SER B CA  
5115  C C   . SER B 57  ? 1.0085 1.1774 0.9544 -0.1180 -0.1053 -0.0535 57  SER B C   
5116  O O   . SER B 57  ? 1.0490 1.2106 0.9871 -0.1082 -0.0982 -0.0547 57  SER B O   
5117  C CB  . SER B 57  ? 1.0528 1.1435 0.9249 -0.1309 -0.0904 -0.0728 57  SER B CB  
5118  O OG  . SER B 57  ? 1.0635 1.1212 0.9201 -0.1255 -0.0742 -0.0826 57  SER B OG  
5124  N N   . HIS B 58  ? 0.9954 1.1992 0.9694 -0.1242 -0.1194 -0.0424 58  HIS B N   
5125  C CA  . HIS B 58  ? 0.9832 1.2170 0.9787 -0.1199 -0.1285 -0.0303 58  HIS B CA  
5126  C C   . HIS B 58  ? 0.9473 1.2078 0.9848 -0.0999 -0.1189 -0.0258 58  HIS B C   
5127  O O   . HIS B 58  ? 0.9045 1.1688 0.9593 -0.0945 -0.1109 -0.0288 58  HIS B O   
5128  C CB  . HIS B 58  ? 0.9411 1.1988 0.9454 -0.1383 -0.1496 -0.0175 58  HIS B CB  
5129  C CG  . HIS B 58  ? 0.9288 1.2193 0.9592 -0.1330 -0.1597 -0.0022 58  HIS B CG  
5130  N ND1 . HIS B 58  ? 0.9286 1.2081 0.9355 -0.1339 -0.1650 0.0000  58  HIS B ND1 
5131  C CD2 . HIS B 58  ? 0.8930 1.2249 0.9705 -0.1258 -0.1637 0.0123  58  HIS B CD2 
5132  C CE1 . HIS B 58  ? 0.9075 1.2209 0.9465 -0.1275 -0.1737 0.0158  58  HIS B CE1 
5133  N NE2 . HIS B 58  ? 0.9085 1.2543 0.9918 -0.1216 -0.1722 0.0236  58  HIS B NE2 
5142  N N   . LEU B 59  ? 0.9388 1.2135 0.9879 -0.0898 -0.1195 -0.0187 59  LEU B N   
5143  C CA  . LEU B 59  ? 0.8866 1.1823 0.9699 -0.0722 -0.1108 -0.0135 59  LEU B CA  
5144  C C   . LEU B 59  ? 0.8473 1.1722 0.9527 -0.0710 -0.1216 0.0022  59  LEU B C   
5145  O O   . LEU B 59  ? 0.8925 1.2136 0.9818 -0.0744 -0.1299 0.0064  59  LEU B O   
5146  C CB  . LEU B 59  ? 0.8646 1.1425 0.9385 -0.0583 -0.0971 -0.0209 59  LEU B CB  
5147  C CG  . LEU B 59  ? 0.8277 1.1207 0.9260 -0.0427 -0.0902 -0.0147 59  LEU B CG  
5148  C CD1 . LEU B 59  ? 0.7922 1.0994 0.9177 -0.0374 -0.0845 -0.0122 59  LEU B CD1 
5149  C CD2 . LEU B 59  ? 0.7977 1.0719 0.8841 -0.0331 -0.0787 -0.0216 59  LEU B CD2 
5161  N N   . GLN B 60  ? 0.8170 1.1698 0.9591 -0.0660 -0.1206 0.0118  60  GLN B N   
5162  C CA  . GLN B 60  ? 0.7714 1.1558 0.9430 -0.0624 -0.1291 0.0297  60  GLN B CA  
5163  C C   . GLN B 60  ? 0.7896 1.1801 0.9841 -0.0413 -0.1130 0.0326  60  GLN B C   
5164  O O   . GLN B 60  ? 0.7656 1.1623 0.9803 -0.0345 -0.1013 0.0323  60  GLN B O   
5165  C CB  . GLN B 60  ? 0.7863 1.1994 0.9847 -0.0740 -0.1397 0.0412  60  GLN B CB  
5166  C CG  . GLN B 60  ? 0.7307 1.1803 0.9626 -0.0725 -0.1519 0.0633  60  GLN B CG  
5167  C CD  . GLN B 60  ? 0.8157 1.2600 1.0232 -0.0827 -0.1705 0.0690  60  GLN B CD  
5168  O OE1 . GLN B 60  ? 0.8177 1.2422 0.9889 -0.1020 -0.1828 0.0620  60  GLN B OE1 
5169  N NE2 . GLN B 60  ? 0.7370 1.1954 0.9610 -0.0701 -0.1721 0.0819  60  GLN B NE2 
5178  N N   . MET B 61  ? 0.7632 1.1478 0.9503 -0.0322 -0.1120 0.0354  61  MET B N   
5179  C CA  . MET B 61  ? 0.7669 1.1518 0.9698 -0.0136 -0.0971 0.0384  61  MET B CA  
5180  C C   . MET B 61  ? 0.7692 1.1852 1.0119 -0.0055 -0.0971 0.0566  61  MET B C   
5181  O O   . MET B 61  ? 0.7698 1.2105 1.0284 -0.0131 -0.1127 0.0705  61  MET B O   
5182  C CB  . MET B 61  ? 0.7872 1.1553 0.9690 -0.0076 -0.0963 0.0366  61  MET B CB  
5183  C CG  . MET B 61  ? 0.7990 1.1384 0.9458 -0.0138 -0.0937 0.0208  61  MET B CG  
5184  S SD  . MET B 61  ? 0.9020 1.2218 1.0450 -0.0075 -0.0765 0.0067  61  MET B SD  
5185  C CE  . MET B 61  ? 0.8351 1.1608 1.0006 0.0083  -0.0641 0.0145  61  MET B CE  
5195  N N   . MET B 62  ? 0.7787 1.1921 1.0371 0.0097  -0.0788 0.0575  62  MET B N   
5196  C CA  . MET B 62  ? 0.7628 1.2029 1.0614 0.0201  -0.0724 0.0744  62  MET B CA  
5197  C C   . MET B 62  ? 0.7614 1.2260 1.0797 0.0231  -0.0858 0.0937  62  MET B C   
5198  O O   . MET B 62  ? 0.7533 1.2518 1.1095 0.0233  -0.0914 0.1114  62  MET B O   
5199  C CB  . MET B 62  ? 0.7830 1.2047 1.0833 0.0374  -0.0484 0.0715  62  MET B CB  
5200  C CG  . MET B 62  ? 0.8298 1.2325 1.1141 0.0486  -0.0439 0.0718  62  MET B CG  
5201  S SD  . MET B 62  ? 0.9219 1.2883 1.1893 0.0617  -0.0179 0.0623  62  MET B SD  
5202  C CE  . MET B 62  ? 0.8421 1.1790 1.0676 0.0492  -0.0238 0.0419  62  MET B CE  
5212  N N   . GLY B 63  ? 0.7638 1.2128 1.0584 0.0250  -0.0916 0.0920  63  GLY B N   
5213  C CA  . GLY B 63  ? 0.7721 1.2404 1.0819 0.0287  -0.1045 0.1110  63  GLY B CA  
5214  C C   . GLY B 63  ? 0.7315 1.1993 1.0159 0.0102  -0.1288 0.1114  63  GLY B C   
5215  O O   . GLY B 63  ? 0.7602 1.2335 1.0432 0.0116  -0.1405 0.1241  63  GLY B O   
5219  N N   . GLY B 64  ? 0.7729 1.2304 1.0337 -0.0076 -0.1360 0.0978  64  GLY B N   
5220  C CA  . GLY B 64  ? 0.7892 1.2381 1.0176 -0.0270 -0.1565 0.0961  64  GLY B CA  
5221  C C   . GLY B 64  ? 0.7743 1.1895 0.9600 -0.0265 -0.1538 0.0846  64  GLY B C   
5222  O O   . GLY B 64  ? 0.7993 1.2009 0.9516 -0.0426 -0.1681 0.0822  64  GLY B O   
5226  N N   . GLU B 65  ? 0.7875 1.1868 0.9711 -0.0100 -0.1353 0.0778  65  GLU B N   
5227  C CA  . GLU B 65  ? 0.8051 1.1751 0.9524 -0.0092 -0.1312 0.0684  65  GLU B CA  
5228  C C   . GLU B 65  ? 0.8264 1.1700 0.9418 -0.0189 -0.1250 0.0484  65  GLU B C   
5229  O O   . GLU B 65  ? 0.8530 1.1979 0.9755 -0.0222 -0.1202 0.0402  65  GLU B O   
5230  C CB  . GLU B 65  ? 0.8344 1.1962 0.9908 0.0099  -0.1141 0.0689  65  GLU B CB  
5231  C CG  . GLU B 65  ? 0.8704 1.2189 1.0293 0.0168  -0.0952 0.0549  65  GLU B CG  
5232  C CD  . GLU B 65  ? 0.8750 1.2426 1.0678 0.0234  -0.0884 0.0601  65  GLU B CD  
5233  O OE1 . GLU B 65  ? 0.8663 1.2608 1.0832 0.0199  -0.0992 0.0730  65  GLU B OE1 
5234  O OE2 . GLU B 65  ? 0.8584 1.2135 1.0530 0.0309  -0.0724 0.0521  65  GLU B OE2 
5241  N N   . PHE B 66  ? 0.8495 1.1682 0.9301 -0.0226 -0.1238 0.0414  66  PHE B N   
5242  C CA  . PHE B 66  ? 0.8732 1.1654 0.9271 -0.0269 -0.1128 0.0240  66  PHE B CA  
5243  C C   . PHE B 66  ? 0.8688 1.1527 0.9315 -0.0128 -0.0948 0.0175  66  PHE B C   
5244  O O   . PHE B 66  ? 0.8621 1.1479 0.9321 -0.0027 -0.0910 0.0243  66  PHE B O   
5245  C CB  . PHE B 66  ? 0.8680 1.1355 0.8798 -0.0378 -0.1171 0.0202  66  PHE B CB  
5246  C CG  . PHE B 66  ? 0.8915 1.1315 0.8799 -0.0378 -0.1010 0.0044  66  PHE B CG  
5247  C CD1 . PHE B 66  ? 0.9001 1.1298 0.8803 -0.0448 -0.0973 -0.0061 66  PHE B CD1 
5248  C CD2 . PHE B 66  ? 0.8853 1.1102 0.8619 -0.0305 -0.0889 0.0016  66  PHE B CD2 
5249  C CE1 . PHE B 66  ? 0.9091 1.1150 0.8726 -0.0425 -0.0812 -0.0182 66  PHE B CE1 
5250  C CE2 . PHE B 66  ? 0.8805 1.0842 0.8422 -0.0295 -0.0731 -0.0103 66  PHE B CE2 
5251  C CZ  . PHE B 66  ? 0.9099 1.1047 0.8664 -0.0346 -0.0689 -0.0197 66  PHE B CZ  
5261  N N   . SER B 67  ? 0.8630 1.1369 0.9243 -0.0130 -0.0846 0.0054  67  SER B N   
5262  C CA  . SER B 67  ? 0.8634 1.1292 0.9316 -0.0032 -0.0702 0.0000  67  SER B CA  
5263  C C   . SER B 67  ? 0.8162 1.0639 0.8684 -0.0072 -0.0620 -0.0118 67  SER B C   
5264  O O   . SER B 67  ? 0.8115 1.0581 0.8658 -0.0115 -0.0617 -0.0178 67  SER B O   
5265  C CB  . SER B 67  ? 0.8166 1.0943 0.9110 0.0034  -0.0660 0.0016  67  SER B CB  
5266  O OG  . SER B 67  ? 0.8455 1.1113 0.9403 0.0080  -0.0547 -0.0049 67  SER B OG  
5272  N N   . GLY B 68  ? 0.8361 1.0697 0.8738 -0.0051 -0.0543 -0.0139 68  GLY B N   
5273  C CA  . GLY B 68  ? 0.8001 1.0184 0.8279 -0.0066 -0.0438 -0.0227 68  GLY B CA  
5274  C C   . GLY B 68  ? 0.8266 1.0492 0.8754 -0.0021 -0.0376 -0.0259 68  GLY B C   
5275  O O   . GLY B 68  ? 0.8260 1.0412 0.8738 -0.0037 -0.0324 -0.0319 68  GLY B O   
5279  N N   . ASN B 69  ? 0.8309 1.0624 0.8965 0.0032  -0.0379 -0.0215 69  ASN B N   
5280  C CA  . ASN B 69  ? 0.7871 1.0199 0.8680 0.0050  -0.0341 -0.0235 69  ASN B CA  
5281  C C   . ASN B 69  ? 0.8051 1.0436 0.8934 0.0022  -0.0388 -0.0261 69  ASN B C   
5282  O O   . ASN B 69  ? 0.7890 1.0238 0.8821 0.0008  -0.0364 -0.0301 69  ASN B O   
5283  C CB  . ASN B 69  ? 0.8016 1.0348 0.8895 0.0093  -0.0324 -0.0185 69  ASN B CB  
5284  C CG  . ASN B 69  ? 0.8238 1.0497 0.9114 0.0092  -0.0263 -0.0178 69  ASN B CG  
5285  O OD1 . ASN B 69  ? 0.7793 1.0034 0.8684 0.0075  -0.0222 -0.0202 69  ASN B OD1 
5286  N ND2 . ASN B 69  ? 0.8923 1.1134 0.9788 0.0109  -0.0249 -0.0134 69  ASN B ND2 
5293  N N   . ALA B 70  ? 0.7870 1.0356 0.8782 0.0013  -0.0455 -0.0224 70  ALA B N   
5294  C CA  . ALA B 70  ? 0.7701 1.0255 0.8687 -0.0030 -0.0497 -0.0241 70  ALA B CA  
5295  C C   . ALA B 70  ? 0.8034 1.0501 0.8883 -0.0105 -0.0516 -0.0305 70  ALA B C   
5296  O O   . ALA B 70  ? 0.8193 1.0625 0.9071 -0.0134 -0.0506 -0.0348 70  ALA B O   
5297  C CB  . ALA B 70  ? 0.7697 1.0416 0.8789 -0.0026 -0.0563 -0.0161 70  ALA B CB  
5303  N N   . SER B 71  ? 0.7982 1.0374 0.8644 -0.0143 -0.0536 -0.0311 71  SER B N   
5304  C CA  . SER B 71  ? 0.8277 1.0505 0.8736 -0.0217 -0.0526 -0.0380 71  SER B CA  
5305  C C   . SER B 71  ? 0.7966 1.0063 0.8443 -0.0168 -0.0407 -0.0437 71  SER B C   
5306  O O   . SER B 71  ? 0.8220 1.0203 0.8632 -0.0201 -0.0381 -0.0490 71  SER B O   
5307  C CB  . SER B 71  ? 0.8655 1.0766 0.8846 -0.0273 -0.0551 -0.0376 71  SER B CB  
5308  O OG  . SER B 71  ? 0.8460 1.0715 0.8659 -0.0330 -0.0690 -0.0297 71  SER B OG  
5314  N N   . ARG B 72  ? 0.7980 1.0096 0.8557 -0.0091 -0.0336 -0.0413 72  ARG B N   
5315  C CA  . ARG B 72  ? 0.8015 1.0068 0.8687 -0.0043 -0.0241 -0.0431 72  ARG B CA  
5316  C C   . ARG B 72  ? 0.8169 1.0281 0.9006 -0.0043 -0.0277 -0.0430 72  ARG B C   
5317  O O   . ARG B 72  ? 0.8092 1.0127 0.8964 -0.0033 -0.0233 -0.0451 72  ARG B O   
5318  C CB  . ARG B 72  ? 0.8303 1.0397 0.9070 0.0012  -0.0184 -0.0384 72  ARG B CB  
5319  C CG  . ARG B 72  ? 0.7937 0.9921 0.8542 0.0022  -0.0094 -0.0390 72  ARG B CG  
5320  C CD  . ARG B 72  ? 0.7813 0.9858 0.8459 0.0047  -0.0081 -0.0333 72  ARG B CD  
5321  N NE  . ARG B 72  ? 0.7766 0.9927 0.8619 0.0064  -0.0122 -0.0287 72  ARG B NE  
5322  C CZ  . ARG B 72  ? 0.8298 1.0497 0.9334 0.0076  -0.0092 -0.0262 72  ARG B CZ  
5323  N NH1 . ARG B 72  ? 0.8534 1.0698 0.9635 0.0102  -0.0005 -0.0267 72  ARG B NH1 
5324  N NH2 . ARG B 72  ? 0.7577 0.9834 0.8724 0.0060  -0.0149 -0.0222 72  ARG B NH2 
5338  N N   . ALA B 73  ? 0.8054 1.0282 0.8981 -0.0051 -0.0345 -0.0399 73  ALA B N   
5339  C CA  . ALA B 73  ? 0.7704 0.9953 0.8734 -0.0065 -0.0371 -0.0400 73  ALA B CA  
5340  C C   . ALA B 73  ? 0.7600 0.9799 0.8563 -0.0121 -0.0397 -0.0445 73  ALA B C   
5341  O O   . ALA B 73  ? 0.7898 1.0027 0.8892 -0.0128 -0.0384 -0.0463 73  ALA B O   
5342  C CB  . ALA B 73  ? 0.7954 1.0293 0.9051 -0.0058 -0.0401 -0.0361 73  ALA B CB  
5348  N N   . PHE B 74  ? 0.8049 1.0277 0.8912 -0.0174 -0.0444 -0.0453 74  PHE B N   
5349  C CA  . PHE B 74  ? 0.8381 1.0544 0.9146 -0.0256 -0.0480 -0.0493 74  PHE B CA  
5350  C C   . PHE B 74  ? 0.8276 1.0220 0.8898 -0.0255 -0.0408 -0.0550 74  PHE B C   
5351  O O   . PHE B 74  ? 0.7832 0.9683 0.8448 -0.0276 -0.0397 -0.0578 74  PHE B O   
5352  C CB  . PHE B 74  ? 0.8302 1.0534 0.8970 -0.0337 -0.0566 -0.0472 74  PHE B CB  
5353  C CG  . PHE B 74  ? 0.8467 1.0646 0.9032 -0.0456 -0.0627 -0.0499 74  PHE B CG  
5354  C CD1 . PHE B 74  ? 0.8620 1.0765 0.9252 -0.0473 -0.0610 -0.0524 74  PHE B CD1 
5355  C CD2 . PHE B 74  ? 0.8952 1.1097 0.9329 -0.0569 -0.0713 -0.0492 74  PHE B CD2 
5356  C CE1 . PHE B 74  ? 0.9152 1.1234 0.9678 -0.0595 -0.0664 -0.0547 74  PHE B CE1 
5357  C CE2 . PHE B 74  ? 0.9272 1.1353 0.9532 -0.0707 -0.0783 -0.0512 74  PHE B CE2 
5358  C CZ  . PHE B 74  ? 0.9245 1.1296 0.9586 -0.0717 -0.0751 -0.0542 74  PHE B CZ  
5368  N N   . ALA B 75  ? 0.8018 0.9857 0.8516 -0.0224 -0.0343 -0.0564 75  ALA B N   
5369  C CA  . ALA B 75  ? 0.8343 0.9950 0.8710 -0.0200 -0.0232 -0.0610 75  ALA B CA  
5370  C C   . ALA B 75  ? 0.8476 1.0094 0.9057 -0.0118 -0.0176 -0.0586 75  ALA B C   
5371  O O   . ALA B 75  ? 0.8314 0.9768 0.8844 -0.0112 -0.0123 -0.0613 75  ALA B O   
5372  C CB  . ALA B 75  ? 0.8458 0.9962 0.8688 -0.0162 -0.0138 -0.0615 75  ALA B CB  
5378  N N   . SER B 76  ? 0.7872 0.9664 0.8678 -0.0065 -0.0196 -0.0526 76  SER B N   
5379  C CA  . SER B 76  ? 0.7669 0.9489 0.8678 -0.0015 -0.0183 -0.0480 76  SER B CA  
5380  C C   . SER B 76  ? 0.8419 1.0229 0.9443 -0.0066 -0.0257 -0.0489 76  SER B C   
5381  O O   . SER B 76  ? 0.8211 0.9973 0.9336 -0.0038 -0.0248 -0.0458 76  SER B O   
5382  C CB  . SER B 76  ? 0.8006 0.9983 0.9192 0.0014  -0.0209 -0.0411 76  SER B CB  
5383  O OG  . SER B 76  ? 0.8007 0.9988 0.9230 0.0069  -0.0121 -0.0384 76  SER B OG  
5389  N N   . LEU B 77  ? 0.8161 1.0022 0.9103 -0.0139 -0.0327 -0.0516 77  LEU B N   
5390  C CA  . LEU B 77  ? 0.7734 0.9572 0.8675 -0.0197 -0.0377 -0.0527 77  LEU B CA  
5391  C C   . LEU B 77  ? 0.8351 0.9995 0.9143 -0.0231 -0.0346 -0.0577 77  LEU B C   
5392  O O   . LEU B 77  ? 0.8568 1.0125 0.9377 -0.0242 -0.0352 -0.0574 77  LEU B O   
5393  C CB  . LEU B 77  ? 0.7684 0.9657 0.8625 -0.0258 -0.0439 -0.0524 77  LEU B CB  
5394  C CG  . LEU B 77  ? 0.7617 0.9575 0.8544 -0.0334 -0.0474 -0.0536 77  LEU B CG  
5395  C CD1 . LEU B 77  ? 0.8111 1.0011 0.9102 -0.0317 -0.0470 -0.0512 77  LEU B CD1 
5396  C CD2 . LEU B 77  ? 0.7603 0.9737 0.8592 -0.0377 -0.0512 -0.0509 77  LEU B CD2 
5408  N N   . LEU B 78  ? 0.8297 0.9834 0.8902 -0.0259 -0.0313 -0.0623 78  LEU B N   
5409  C CA  . LEU B 78  ? 0.8510 0.9790 0.8903 -0.0304 -0.0268 -0.0679 78  LEU B CA  
5410  C C   . LEU B 78  ? 0.9006 1.0122 0.9453 -0.0197 -0.0155 -0.0665 78  LEU B C   
5411  O O   . LEU B 78  ? 0.9295 1.0206 0.9642 -0.0211 -0.0121 -0.0689 78  LEU B O   
5412  C CB  . LEU B 78  ? 0.9001 1.0147 0.9117 -0.0374 -0.0255 -0.0729 78  LEU B CB  
5413  C CG  . LEU B 78  ? 0.9014 1.0329 0.9088 -0.0493 -0.0387 -0.0719 78  LEU B CG  
5414  C CD1 . LEU B 78  ? 0.8975 1.0141 0.8752 -0.0568 -0.0391 -0.0750 78  LEU B CD1 
5415  C CD2 . LEU B 78  ? 0.8155 0.9486 0.8219 -0.0608 -0.0470 -0.0724 78  LEU B CD2 
5427  N N   . ALA B 79  ? 0.8759 0.9966 0.9380 -0.0089 -0.0093 -0.0613 79  ALA B N   
5428  C CA  . ALA B 79  ? 0.8889 1.0016 0.9664 0.0024  0.0003  -0.0560 79  ALA B CA  
5429  C C   . ALA B 79  ? 0.8888 1.0108 0.9858 0.0024  -0.0087 -0.0497 79  ALA B C   
5430  O O   . ALA B 79  ? 0.9186 1.0266 1.0190 0.0068  -0.0048 -0.0469 79  ALA B O   
5431  C CB  . ALA B 79  ? 0.8830 1.0077 0.9783 0.0121  0.0081  -0.0501 79  ALA B CB  
5437  N N   . PHE B 80  ? 0.8609 1.0034 0.9680 -0.0025 -0.0201 -0.0468 80  PHE B N   
5438  C CA  . PHE B 80  ? 0.8424 0.9896 0.9605 -0.0053 -0.0293 -0.0414 80  PHE B CA  
5439  C C   . PHE B 80  ? 0.8661 0.9965 0.9695 -0.0113 -0.0310 -0.0456 80  PHE B C   
5440  O O   . PHE B 80  ? 0.8539 0.9791 0.9636 -0.0113 -0.0351 -0.0403 80  PHE B O   
5441  C CB  . PHE B 80  ? 0.8153 0.9794 0.9361 -0.0112 -0.0379 -0.0404 80  PHE B CB  
5442  C CG  . PHE B 80  ? 0.8212 0.9873 0.9493 -0.0147 -0.0464 -0.0339 80  PHE B CG  
5443  C CD1 . PHE B 80  ? 0.8086 0.9793 0.9537 -0.0109 -0.0498 -0.0240 80  PHE B CD1 
5444  C CD2 . PHE B 80  ? 0.7940 0.9567 0.9109 -0.0231 -0.0512 -0.0367 80  PHE B CD2 
5445  C CE1 . PHE B 80  ? 0.7746 0.9436 0.9208 -0.0172 -0.0599 -0.0174 80  PHE B CE1 
5446  C CE2 . PHE B 80  ? 0.7855 0.9443 0.9021 -0.0278 -0.0581 -0.0313 80  PHE B CE2 
5447  C CZ  . PHE B 80  ? 0.7725 0.9330 0.9013 -0.0257 -0.0635 -0.0218 80  PHE B CZ  
5457  N N   . ARG B 81  ? 0.8825 1.0031 0.9650 -0.0179 -0.0287 -0.0541 81  ARG B N   
5458  C CA  . ARG B 81  ? 0.8862 0.9912 0.9528 -0.0267 -0.0311 -0.0584 81  ARG B CA  
5459  C C   . ARG B 81  ? 0.9088 0.9845 0.9564 -0.0251 -0.0215 -0.0630 81  ARG B C   
5460  O O   . ARG B 81  ? 0.9683 1.0265 0.9992 -0.0335 -0.0228 -0.0668 81  ARG B O   
5461  C CB  . ARG B 81  ? 0.8710 0.9872 0.9282 -0.0389 -0.0376 -0.0629 81  ARG B CB  
5462  C CG  . ARG B 81  ? 0.8014 0.9383 0.8727 -0.0414 -0.0443 -0.0588 81  ARG B CG  
5463  C CD  . ARG B 81  ? 0.7672 0.9187 0.8361 -0.0508 -0.0484 -0.0607 81  ARG B CD  
5464  N NE  . ARG B 81  ? 0.8689 1.0346 0.9493 -0.0521 -0.0506 -0.0568 81  ARG B NE  
5465  C CZ  . ARG B 81  ? 0.8287 1.0106 0.9146 -0.0578 -0.0521 -0.0555 81  ARG B CZ  
5466  N NH1 . ARG B 81  ? 0.7910 0.9812 0.8743 -0.0642 -0.0554 -0.0566 81  ARG B NH1 
5467  N NH2 . ARG B 81  ? 0.8176 1.0065 0.9114 -0.0573 -0.0500 -0.0520 81  ARG B NH2 
5481  N N   . ASP B 82  ? 0.9289 0.9958 0.9764 -0.0151 -0.0102 -0.0628 82  ASP B N   
5482  C CA  . ASP B 82  ? 0.9552 0.9878 0.9800 -0.0123 0.0030  -0.0676 82  ASP B CA  
5483  C C   . ASP B 82  ? 0.9452 0.9664 0.9867 0.0008  0.0106  -0.0597 82  ASP B C   
5484  O O   . ASP B 82  ? 0.9407 0.9806 1.0128 0.0122  0.0116  -0.0498 82  ASP B O   
5485  C CB  . ASP B 82  ? 0.9845 1.0095 0.9973 -0.0079 0.0144  -0.0712 82  ASP B CB  
5486  C CG  . ASP B 82  ? 1.0330 1.0151 1.0154 -0.0051 0.0316  -0.0771 82  ASP B CG  
5487  O OD1 . ASP B 82  ? 1.0639 1.0203 1.0198 -0.0152 0.0301  -0.0830 82  ASP B OD1 
5488  O OD2 . ASP B 82  ? 1.0151 0.9868 0.9983 0.0067  0.0481  -0.0758 82  ASP B OD2 
5493  N N   . LYS B 83  ? 0.9698 0.9606 0.9919 -0.0016 0.0150  -0.0628 83  LYS B N   
5494  C CA  . LYS B 83  ? 0.9778 0.9553 1.0156 0.0118  0.0226  -0.0538 83  LYS B CA  
5495  C C   . LYS B 83  ? 1.0452 1.0079 1.0891 0.0289  0.0434  -0.0505 83  LYS B C   
5496  O O   . LYS B 83  ? 1.0563 1.0220 1.1291 0.0441  0.0495  -0.0382 83  LYS B O   
5497  C CB  . LYS B 83  ? 1.0113 0.9559 1.0231 0.0045  0.0231  -0.0582 83  LYS B CB  
5498  C CG  . LYS B 83  ? 1.0762 0.9767 1.0487 0.0031  0.0398  -0.0683 83  LYS B CG  
5499  C CD  . LYS B 83  ? 1.1005 0.9790 1.0360 -0.0175 0.0321  -0.0783 83  LYS B CD  
5500  C CE  . LYS B 83  ? 1.1190 0.9465 1.0084 -0.0217 0.0479  -0.0883 83  LYS B CE  
5501  N NZ  . LYS B 83  ? 1.1818 1.0011 1.0625 -0.0133 0.0629  -0.0915 83  LYS B NZ  
5515  N N   . ASP B 84  ? 1.0334 0.9801 1.0509 0.0265  0.0548  -0.0601 84  ASP B N   
5516  C CA  . ASP B 84  ? 1.0506 0.9761 1.0662 0.0418  0.0789  -0.0587 84  ASP B CA  
5517  C C   . ASP B 84  ? 1.0516 1.0101 1.1002 0.0518  0.0820  -0.0509 84  ASP B C   
5518  O O   . ASP B 84  ? 1.0313 0.9777 1.0866 0.0665  0.1038  -0.0471 84  ASP B O   
5519  C CB  . ASP B 84  ? 1.1136 0.9971 1.0751 0.0319  0.0907  -0.0735 84  ASP B CB  
5520  C CG  . ASP B 84  ? 1.1221 0.9616 1.0471 0.0243  0.0943  -0.0804 84  ASP B CG  
5521  O OD1 . ASP B 84  ? 1.0895 0.9208 1.0311 0.0345  0.0980  -0.0729 84  ASP B OD1 
5522  O OD2 . ASP B 84  ? 1.2502 1.0621 1.1285 0.0069  0.0926  -0.0926 84  ASP B OD2 
5527  N N   . PHE B 85  ? 1.0197 1.0170 1.0879 0.0442  0.0628  -0.0481 85  PHE B N   
5528  C CA  . PHE B 85  ? 0.9825 1.0097 1.0800 0.0515  0.0647  -0.0405 85  PHE B CA  
5529  C C   . PHE B 85  ? 1.0031 1.0462 1.1462 0.0677  0.0697  -0.0235 85  PHE B C   
5530  O O   . PHE B 85  ? 1.0047 1.0615 1.1685 0.0665  0.0551  -0.0148 85  PHE B O   
5531  C CB  . PHE B 85  ? 0.9655 1.0254 1.0701 0.0393  0.0433  -0.0413 85  PHE B CB  
5532  C CG  . PHE B 85  ? 1.0165 1.1042 1.1467 0.0445  0.0441  -0.0342 85  PHE B CG  
5533  C CD1 . PHE B 85  ? 1.0028 1.1167 1.1736 0.0510  0.0381  -0.0196 85  PHE B CD1 
5534  C CD2 . PHE B 85  ? 1.0025 1.0888 1.1143 0.0412  0.0497  -0.0411 85  PHE B CD2 
5535  C CE1 . PHE B 85  ? 0.9648 1.1034 1.1581 0.0535  0.0382  -0.0126 85  PHE B CE1 
5536  C CE2 . PHE B 85  ? 0.9777 1.0877 1.1115 0.0451  0.0508  -0.0344 85  PHE B CE2 
5537  C CZ  . PHE B 85  ? 0.9810 1.1173 1.1559 0.0511  0.0454  -0.0204 85  PHE B CZ  
5547  N N   . SER B 86  ? 1.0104 1.0512 1.1690 0.0821  0.0905  -0.0175 86  SER B N   
5548  C CA  . SER B 86  ? 1.0368 1.0984 1.2459 0.0981  0.0962  0.0018  86  SER B CA  
5549  C C   . SER B 86  ? 1.0590 1.1593 1.3001 0.0979  0.0907  0.0107  86  SER B C   
5550  O O   . SER B 86  ? 1.1053 1.2370 1.3727 0.0914  0.0692  0.0204  86  SER B O   
5551  C CB  . SER B 86  ? 1.0718 1.1028 1.2812 0.1166  0.1271  0.0049  86  SER B CB  
5552  O OG  . SER B 86  ? 1.1502 1.1527 1.3475 0.1201  0.1293  0.0046  86  SER B OG  
5558  N N   . LYS B 87  ? 1.1113 1.2062 1.3463 0.1036  0.1102  0.0074  87  LYS B N   
5559  C CA  . LYS B 87  ? 1.0690 1.1967 1.3279 0.1014  0.1061  0.0141  87  LYS B CA  
5560  C C   . LYS B 87  ? 1.1086 1.2249 1.3267 0.0909  0.1079  -0.0018 87  LYS B C   
5561  O O   . LYS B 87  ? 1.1425 1.2782 1.3565 0.0783  0.0882  -0.0048 87  LYS B O   
5562  C CB  . LYS B 87  ? 1.1051 1.2452 1.4066 0.1192  0.1282  0.0304  87  LYS B CB  
5563  C CG  . LYS B 87  ? 1.1632 1.3309 1.4842 0.1172  0.1300  0.0361  87  LYS B CG  
5564  C CD  . LYS B 87  ? 1.1417 1.3373 1.4650 0.0998  0.0995  0.0359  87  LYS B CD  
5565  C CE  . LYS B 87  ? 1.1219 1.3553 1.4891 0.0996  0.0955  0.0526  87  LYS B CE  
5566  N NZ  . LYS B 87  ? 1.1035 1.3619 1.5254 0.1081  0.0920  0.0754  87  LYS B NZ  
5580  N N   . GLN B 88  ? 1.0507 1.1331 1.2360 0.0955  0.1311  -0.0115 88  GLN B N   
5581  C CA  . GLN B 88  ? 1.0363 1.1040 1.1789 0.0846  0.1322  -0.0254 88  GLN B CA  
5582  C C   . GLN B 88  ? 1.0395 1.0676 1.1289 0.0748  0.1314  -0.0412 88  GLN B C   
5583  O O   . GLN B 88  ? 1.0675 1.0666 1.1457 0.0809  0.1434  -0.0430 88  GLN B O   
5584  C CB  . GLN B 88  ? 1.0546 1.1121 1.1956 0.0942  0.1593  -0.0235 88  GLN B CB  
5585  C CG  . GLN B 88  ? 1.1075 1.1131 1.2043 0.0992  0.1865  -0.0337 88  GLN B CG  
5586  C CD  . GLN B 88  ? 1.1236 1.1015 1.1606 0.0833  0.1836  -0.0498 88  GLN B CD  
5587  O OE1 . GLN B 88  ? 1.0719 1.0724 1.1075 0.0730  0.1670  -0.0509 88  GLN B OE1 
5588  N NE2 . GLN B 88  ? 1.2005 1.1271 1.1858 0.0804  0.1989  -0.0615 88  GLN B NE2 
5597  N N   . LYS B 89  ? 1.0417 1.0686 1.0988 0.0591  0.1169  -0.0515 89  LYS B N   
5598  C CA  . LYS B 89  ? 1.0339 1.0257 1.0395 0.0462  0.1138  -0.0652 89  LYS B CA  
5599  C C   . LYS B 89  ? 1.0337 1.0314 1.0122 0.0307  0.0991  -0.0721 89  LYS B C   
5600  O O   . LYS B 89  ? 1.0240 1.0570 1.0249 0.0261  0.0799  -0.0679 89  LYS B O   
5601  C CB  . LYS B 89  ? 1.0504 1.0434 1.0603 0.0410  0.0984  -0.0659 89  LYS B CB  
5602  C CG  . LYS B 89  ? 1.0529 1.0133 1.0127 0.0248  0.0924  -0.0786 89  LYS B CG  
5603  C CD  . LYS B 89  ? 1.0867 1.0190 1.0378 0.0275  0.0989  -0.0802 89  LYS B CD  
5604  C CE  . LYS B 89  ? 1.1335 1.0225 1.0266 0.0109  0.0989  -0.0932 89  LYS B CE  
5605  N NZ  . LYS B 89  ? 1.0946 1.0000 0.9824 -0.0075 0.0727  -0.0961 89  LYS B NZ  
5619  N N   . ASN B 90  ? 1.0660 1.0267 0.9944 0.0224  0.1080  -0.0818 90  ASN B N   
5620  C CA  . ASN B 90  ? 1.0653 1.0285 0.9648 0.0067  0.0929  -0.0868 90  ASN B CA  
5621  C C   . ASN B 90  ? 1.0522 1.0155 0.9343 -0.0101 0.0704  -0.0916 90  ASN B C   
5622  O O   . ASN B 90  ? 1.0810 1.0164 0.9417 -0.0147 0.0734  -0.0970 90  ASN B O   
5623  C CB  . ASN B 90  ? 1.1021 1.0228 0.9513 0.0027  0.1110  -0.0938 90  ASN B CB  
5624  C CG  . ASN B 90  ? 1.1004 1.0314 0.9653 0.0139  0.1269  -0.0882 90  ASN B CG  
5625  O OD1 . ASN B 90  ? 1.1473 1.0767 0.9894 0.0057  0.1225  -0.0897 90  ASN B OD1 
5626  N ND2 . ASN B 90  ? 1.0984 1.0411 1.0037 0.0322  0.1447  -0.0803 90  ASN B ND2 
5633  N N   . TYR B 91  ? 1.0087 1.0032 0.9010 -0.0190 0.0488  -0.0888 91  TYR B N   
5634  C CA  . TYR B 91  ? 1.0136 1.0168 0.8983 -0.0344 0.0271  -0.0906 91  TYR B CA  
5635  C C   . TYR B 91  ? 1.0424 1.0470 0.9006 -0.0490 0.0135  -0.0911 91  TYR B C   
5636  O O   . TYR B 91  ? 1.0587 1.0844 0.9303 -0.0449 0.0105  -0.0861 91  TYR B O   
5637  C CB  . TYR B 91  ? 1.0283 1.0725 0.9591 -0.0297 0.0137  -0.0837 91  TYR B CB  
5638  C CG  . TYR B 91  ? 0.9739 1.0159 0.9271 -0.0196 0.0213  -0.0820 91  TYR B CG  
5639  C CD1 . TYR B 91  ? 0.9547 0.9819 0.8969 -0.0268 0.0172  -0.0857 91  TYR B CD1 
5640  C CD2 . TYR B 91  ? 0.9583 1.0134 0.9441 -0.0039 0.0316  -0.0753 91  TYR B CD2 
5641  C CE1 . TYR B 91  ? 1.0262 1.0499 0.9877 -0.0175 0.0234  -0.0829 91  TYR B CE1 
5642  C CE2 . TYR B 91  ? 0.9889 1.0434 0.9965 0.0048  0.0363  -0.0713 91  TYR B CE2 
5643  C CZ  . TYR B 91  ? 1.0241 1.0621 1.0189 -0.0014 0.0323  -0.0752 91  TYR B CZ  
5644  O OH  . TYR B 91  ? 0.9928 1.0289 1.0086 0.0075  0.0362  -0.0700 91  TYR B OH  
5654  N N   . ASN B 92  ? 1.0806 1.0621 0.9008 -0.0670 0.0043  -0.0960 92  ASN B N   
5655  C CA  . ASN B 92  ? 1.1091 1.0920 0.9033 -0.0839 -0.0126 -0.0943 92  ASN B CA  
5656  C C   . ASN B 92  ? 1.0712 1.0960 0.8970 -0.0911 -0.0363 -0.0867 92  ASN B C   
5657  O O   . ASN B 92  ? 1.0384 1.0674 0.8730 -0.0968 -0.0427 -0.0874 92  ASN B O   
5658  C CB  . ASN B 92  ? 1.1180 1.0516 0.8511 -0.1028 -0.0117 -0.1022 92  ASN B CB  
5659  C CG  . ASN B 92  ? 1.1980 1.0862 0.8903 -0.0979 0.0124  -0.1089 92  ASN B CG  
5660  O OD1 . ASN B 92  ? 1.2116 1.1096 0.9159 -0.0859 0.0222  -0.1058 92  ASN B OD1 
5661  N ND2 . ASN B 92  ? 1.3025 1.1380 0.9442 -0.1077 0.0235  -0.1179 92  ASN B ND2 
5668  N N   . ILE B 93  ? 1.0694 1.1240 0.9124 -0.0902 -0.0477 -0.0787 93  ILE B N   
5669  C CA  . ILE B 93  ? 1.0714 1.1670 0.9483 -0.0938 -0.0666 -0.0695 93  ILE B CA  
5670  C C   . ILE B 93  ? 1.1078 1.2141 0.9728 -0.1047 -0.0831 -0.0616 93  ILE B C   
5671  O O   . ILE B 93  ? 1.1186 1.2005 0.9485 -0.1090 -0.0800 -0.0637 93  ILE B O   
5672  C CB  . ILE B 93  ? 1.0506 1.1787 0.9757 -0.0754 -0.0616 -0.0649 93  ILE B CB  
5673  C CG1 . ILE B 93  ? 1.0400 1.1718 0.9697 -0.0635 -0.0534 -0.0624 93  ILE B CG1 
5674  C CG2 . ILE B 93  ? 1.0081 1.1274 0.9459 -0.0664 -0.0489 -0.0704 93  ILE B CG2 
5675  C CD1 . ILE B 93  ? 0.9679 1.1332 0.9388 -0.0513 -0.0553 -0.0552 93  ILE B CD1 
5687  N N   . THR B 94  ? 1.1440 1.2868 1.0394 -0.1086 -0.1001 -0.0513 94  THR B N   
5688  C CA  . THR B 94  ? 1.1676 1.3295 1.0639 -0.1164 -0.1176 -0.0397 94  THR B CA  
5689  C C   . THR B 94  ? 1.1217 1.3275 1.0701 -0.1027 -0.1211 -0.0288 94  THR B C   
5690  O O   . THR B 94  ? 1.0642 1.2881 1.0430 -0.0979 -0.1189 -0.0282 94  THR B O   
5691  C CB  . THR B 94  ? 1.1264 1.2850 1.0010 -0.1412 -0.1383 -0.0350 94  THR B CB  
5692  O OG1 . THR B 94  ? 1.1901 1.3856 1.1062 -0.1432 -0.1487 -0.0264 94  THR B OG1 
5693  C CG2 . THR B 94  ? 1.2021 1.3136 1.0279 -0.1546 -0.1314 -0.0482 94  THR B CG2 
5701  N N   . CYS B 95  ? 1.0751 1.2939 1.0305 -0.0965 -0.1252 -0.0202 95  CYS B N   
5702  C CA  . CYS B 95  ? 0.9998 1.2536 0.9993 -0.0821 -0.1258 -0.0097 95  CYS B CA  
5703  C C   . CYS B 95  ? 0.9351 1.2103 0.9419 -0.0879 -0.1440 0.0063  95  CYS B C   
5704  O O   . CYS B 95  ? 0.9501 1.2089 0.9240 -0.0979 -0.1526 0.0081  95  CYS B O   
5705  C CB  . CYS B 95  ? 0.9724 1.2198 0.9784 -0.0639 -0.1086 -0.0142 95  CYS B CB  
5706  S SG  . CYS B 95  ? 0.8727 1.1521 0.9240 -0.0465 -0.1058 -0.0032 95  CYS B SG  
5712  N N   . SER B 96  ? 0.9376 1.2485 0.9874 -0.0813 -0.1491 0.0189  96  SER B N   
5713  C CA  . SER B 96  ? 0.8824 1.2193 0.9492 -0.0837 -0.1659 0.0376  96  SER B CA  
5714  C C   . SER B 96  ? 0.8722 1.1992 0.9263 -0.0737 -0.1627 0.0405  96  SER B C   
5715  O O   . SER B 96  ? 0.8427 1.1616 0.9021 -0.0574 -0.1453 0.0339  96  SER B O   
5716  C CB  . SER B 96  ? 0.8309 1.2064 0.9511 -0.0729 -0.1648 0.0505  96  SER B CB  
5717  O OG  . SER B 96  ? 0.7792 1.1510 0.9155 -0.0541 -0.1436 0.0427  96  SER B OG  
5723  N N   . GLY B 97  ? 0.9020 1.2289 0.9377 -0.0853 -0.1807 0.0513  97  GLY B N   
5724  C CA  . GLY B 97  ? 0.9041 1.2188 0.9222 -0.0787 -0.1796 0.0550  97  GLY B CA  
5725  C C   . GLY B 97  ? 0.9758 1.2481 0.9378 -0.0887 -0.1748 0.0415  97  GLY B C   
5726  O O   . GLY B 97  ? 0.9637 1.2227 0.9059 -0.0856 -0.1740 0.0446  97  GLY B O   
5730  N N   . GLU B 98  ? 1.0440 1.2924 0.9792 -0.0998 -0.1696 0.0271  98  GLU B N   
5731  C CA  . GLU B 98  ? 1.0569 1.2610 0.9363 -0.1099 -0.1622 0.0143  98  GLU B CA  
5732  C C   . GLU B 98  ? 1.1180 1.3049 0.9641 -0.1343 -0.1765 0.0118  98  GLU B C   
5733  O O   . GLU B 98  ? 1.0731 1.2733 0.9386 -0.1388 -0.1798 0.0103  98  GLU B O   
5734  C CB  . GLU B 98  ? 1.0924 1.2768 0.9701 -0.0961 -0.1352 -0.0024 98  GLU B CB  
5735  C CG  . GLU B 98  ? 1.1575 1.2960 0.9820 -0.1030 -0.1221 -0.0148 98  GLU B CG  
5736  C CD  . GLU B 98  ? 1.2195 1.3447 1.0203 -0.1015 -0.1208 -0.0102 98  GLU B CD  
5737  O OE1 . GLU B 98  ? 1.1917 1.3401 1.0235 -0.0873 -0.1196 -0.0021 98  GLU B OE1 
5738  O OE2 . GLU B 98  ? 1.2770 1.3651 1.0247 -0.1151 -0.1200 -0.0147 98  GLU B OE2 
5745  N N   . SER B 99  ? 1.1740 1.3283 0.9662 -0.1516 -0.1850 0.0115  99  SER B N   
5746  C CA  . SER B 99  ? 1.1958 1.3273 0.9468 -0.1788 -0.2009 0.0100  99  SER B CA  
5747  C C   . SER B 99  ? 1.2510 1.3320 0.9548 -0.1839 -0.1803 -0.0106 99  SER B C   
5748  O O   . SER B 99  ? 1.3266 1.3868 1.0003 -0.2044 -0.1890 -0.0147 99  SER B O   
5749  C CB  . SER B 99  ? 1.2415 1.3596 0.9519 -0.1987 -0.2237 0.0220  99  SER B CB  
5750  O OG  . SER B 99  ? 1.2631 1.3447 0.9326 -0.1934 -0.2079 0.0143  99  SER B OG  
5756  N N   . LYS B 100 ? 1.2382 1.2989 0.9359 -0.1659 -0.1529 -0.0223 100 LYS B N   
5757  C CA  . LYS B 100 ? 1.2717 1.2837 0.9273 -0.1674 -0.1298 -0.0399 100 LYS B CA  
5758  C C   . LYS B 100 ? 1.2665 1.2927 0.9628 -0.1506 -0.1128 -0.0480 100 LYS B C   
5759  O O   . LYS B 100 ? 1.2159 1.2790 0.9651 -0.1312 -0.1079 -0.0438 100 LYS B O   
5760  C CB  . LYS B 100 ? 1.3641 1.3438 0.9877 -0.1588 -0.1084 -0.0462 100 LYS B CB  
5761  C CG  . LYS B 100 ? 1.4553 1.3825 1.0018 -0.1810 -0.1119 -0.0490 100 LYS B CG  
5762  C CD  . LYS B 100 ? 1.5057 1.3940 1.0018 -0.2056 -0.1191 -0.0563 100 LYS B CD  
5763  C CE  . LYS B 100 ? 1.4772 1.3494 0.9813 -0.1954 -0.0956 -0.0704 100 LYS B CE  
5764  N NZ  . LYS B 100 ? 1.4674 1.3157 0.9386 -0.2190 -0.1086 -0.0744 100 LYS B NZ  
5778  N N   . VAL B 101 ? 1.2867 1.2796 0.9541 -0.1590 -0.1040 -0.0594 101 VAL B N   
5779  C CA  . VAL B 101 ? 1.2133 1.2112 0.9114 -0.1434 -0.0860 -0.0674 101 VAL B CA  
5780  C C   . VAL B 101 ? 1.1943 1.1918 0.9107 -0.1198 -0.0610 -0.0713 101 VAL B C   
5781  O O   . VAL B 101 ? 1.2511 1.2143 0.9311 -0.1187 -0.0449 -0.0765 101 VAL B O   
5782  C CB  . VAL B 101 ? 1.2073 1.1589 0.8609 -0.1564 -0.0779 -0.0791 101 VAL B CB  
5783  C CG1 . VAL B 101 ? 1.2512 1.2003 0.9315 -0.1372 -0.0549 -0.0871 101 VAL B CG1 
5784  C CG2 . VAL B 101 ? 1.1818 1.1413 0.8278 -0.1801 -0.1041 -0.0740 101 VAL B CG2 
5794  N N   . LEU B 102 ? 1.1453 1.1798 0.9172 -0.1022 -0.0572 -0.0681 102 LEU B N   
5795  C CA  . LEU B 102 ? 1.1321 1.1727 0.9282 -0.0817 -0.0371 -0.0693 102 LEU B CA  
5796  C C   . LEU B 102 ? 1.1139 1.1350 0.9131 -0.0725 -0.0163 -0.0780 102 LEU B C   
5797  O O   . LEU B 102 ? 1.1127 1.1441 0.9320 -0.0721 -0.0203 -0.0792 102 LEU B O   
5798  C CB  . LEU B 102 ? 1.1055 1.1925 0.9552 -0.0697 -0.0453 -0.0603 102 LEU B CB  
5799  C CG  . LEU B 102 ? 1.1129 1.2227 0.9678 -0.0751 -0.0644 -0.0494 102 LEU B CG  
5800  C CD1 . LEU B 102 ? 1.0522 1.2026 0.9541 -0.0696 -0.0764 -0.0413 102 LEU B CD1 
5801  C CD2 . LEU B 102 ? 1.0767 1.1837 0.9272 -0.0667 -0.0560 -0.0463 102 LEU B CD2 
5813  N N   . ASP B 103 ? 1.1598 1.1532 0.9406 -0.0644 0.0068  -0.0828 103 ASP B N   
5814  C CA  . ASP B 103 ? 1.1496 1.1234 0.9353 -0.0532 0.0294  -0.0887 103 ASP B CA  
5815  C C   . ASP B 103 ? 1.1261 1.1316 0.9640 -0.0338 0.0390  -0.0826 103 ASP B C   
5816  O O   . ASP B 103 ? 1.1389 1.1413 0.9786 -0.0255 0.0539  -0.0805 103 ASP B O   
5817  C CB  . ASP B 103 ? 1.1979 1.1192 0.9310 -0.0561 0.0514  -0.0964 103 ASP B CB  
5818  C CG  . ASP B 103 ? 1.2411 1.1431 0.9845 -0.0405 0.0789  -0.1000 103 ASP B CG  
5819  O OD1 . ASP B 103 ? 1.2248 1.1376 0.9939 -0.0360 0.0759  -0.1000 103 ASP B OD1 
5820  O OD2 . ASP B 103 ? 1.3043 1.1803 1.0311 -0.0323 0.1042  -0.1018 103 ASP B OD2 
5825  N N   . VAL B 104 ? 1.0955 1.1299 0.9739 -0.0284 0.0302  -0.0793 104 VAL B N   
5826  C CA  . VAL B 104 ? 1.0071 1.0728 0.9332 -0.0143 0.0334  -0.0722 104 VAL B CA  
5827  C C   . VAL B 104 ? 0.9670 1.0224 0.9094 -0.0019 0.0528  -0.0724 104 VAL B C   
5828  O O   . VAL B 104 ? 0.9578 0.9985 0.8948 -0.0028 0.0547  -0.0762 104 VAL B O   
5829  C CB  . VAL B 104 ? 1.0211 1.1204 0.9782 -0.0161 0.0137  -0.0677 104 VAL B CB  
5830  C CG1 . VAL B 104 ? 0.8995 1.0268 0.8953 -0.0058 0.0142  -0.0602 104 VAL B CG1 
5831  C CG2 . VAL B 104 ? 1.0044 1.1114 0.9456 -0.0287 -0.0050 -0.0667 104 VAL B CG2 
5841  N N   . ASP B 105 ? 0.9415 1.0059 0.9063 0.0096  0.0670  -0.0667 105 ASP B N   
5842  C CA  . ASP B 105 ? 0.9333 0.9954 0.9239 0.0232  0.0852  -0.0626 105 ASP B CA  
5843  C C   . ASP B 105 ? 0.9287 1.0272 0.9675 0.0281  0.0728  -0.0537 105 ASP B C   
5844  O O   . ASP B 105 ? 0.8736 0.9976 0.9356 0.0293  0.0667  -0.0469 105 ASP B O   
5845  C CB  . ASP B 105 ? 0.9372 0.9906 0.9284 0.0319  0.1083  -0.0592 105 ASP B CB  
5846  C CG  . ASP B 105 ? 0.9712 1.0267 0.9965 0.0475  0.1283  -0.0518 105 ASP B CG  
5847  O OD1 . ASP B 105 ? 0.9707 1.0248 1.0088 0.0511  0.1256  -0.0512 105 ASP B OD1 
5848  O OD2 . ASP B 105 ? 0.9468 1.0061 0.9877 0.0564  0.1468  -0.0453 105 ASP B OD2 
5853  N N   . VAL B 106 ? 0.9474 1.0447 0.9973 0.0298  0.0688  -0.0537 106 VAL B N   
5854  C CA  . VAL B 106 ? 0.8881 1.0137 0.9759 0.0318  0.0554  -0.0457 106 VAL B CA  
5855  C C   . VAL B 106 ? 0.8837 1.0118 1.0030 0.0447  0.0689  -0.0366 106 VAL B C   
5856  O O   . VAL B 106 ? 0.9051 1.0080 1.0136 0.0511  0.0845  -0.0391 106 VAL B O   
5857  C CB  . VAL B 106 ? 0.9249 1.0490 1.0028 0.0230  0.0392  -0.0507 106 VAL B CB  
5858  C CG1 . VAL B 106 ? 0.8703 1.0170 0.9813 0.0246  0.0273  -0.0427 106 VAL B CG1 
5859  C CG2 . VAL B 106 ? 0.9040 1.0316 0.9589 0.0113  0.0258  -0.0564 106 VAL B CG2 
5869  N N   . ARG B 107 ? 0.8595 1.0167 1.0171 0.0480  0.0629  -0.0248 107 ARG B N   
5870  C CA  . ARG B 107 ? 0.9067 1.0746 1.1030 0.0591  0.0711  -0.0119 107 ARG B CA  
5871  C C   . ARG B 107 ? 0.9002 1.0933 1.1248 0.0542  0.0498  -0.0024 107 ARG B C   
5872  O O   . ARG B 107 ? 0.8273 1.0336 1.0479 0.0443  0.0338  -0.0036 107 ARG B O   
5873  C CB  . ARG B 107 ? 0.8556 1.0341 1.0737 0.0673  0.0880  -0.0030 107 ARG B CB  
5874  C CG  . ARG B 107 ? 0.8968 1.0457 1.0845 0.0727  0.1129  -0.0113 107 ARG B CG  
5875  C CD  . ARG B 107 ? 0.7727 0.9306 0.9588 0.0706  0.1193  -0.0096 107 ARG B CD  
5876  N NE  . ARG B 107 ? 0.7323 0.8887 0.8867 0.0573  0.1022  -0.0192 107 ARG B NE  
5877  C CZ  . ARG B 107 ? 0.7523 0.9256 0.9111 0.0520  0.0953  -0.0161 107 ARG B CZ  
5878  N NH1 . ARG B 107 ? 0.7167 0.9098 0.9082 0.0565  0.1031  -0.0043 107 ARG B NH1 
5879  N NH2 . ARG B 107 ? 0.8199 0.9902 0.9508 0.0417  0.0803  -0.0238 107 ARG B NH2 
5893  N N   . ASN B 108 ? 0.9299 1.1266 1.1807 0.0611  0.0503  0.0075  108 ASN B N   
5894  C CA  . ASN B 108 ? 0.8999 1.1178 1.1758 0.0554  0.0299  0.0185  108 ASN B CA  
5895  C C   . ASN B 108 ? 0.8942 1.1399 1.1997 0.0527  0.0247  0.0312  108 ASN B C   
5896  O O   . ASN B 108 ? 0.9141 1.1681 1.2406 0.0612  0.0404  0.0386  108 ASN B O   
5897  C CB  . ASN B 108 ? 0.9255 1.1407 1.2242 0.0639  0.0315  0.0287  108 ASN B CB  
5898  C CG  . ASN B 108 ? 0.9093 1.1513 1.2455 0.0602  0.0139  0.0471  108 ASN B CG  
5899  O OD1 . ASN B 108 ? 0.8954 1.1580 1.2708 0.0672  0.0191  0.0633  108 ASN B OD1 
5900  N ND2 . ASN B 108 ? 0.8841 1.1254 1.2078 0.0480  -0.0071 0.0456  108 ASN B ND2 
5907  N N   . ASP B 109 ? 0.8614 1.1190 1.1663 0.0400  0.0037  0.0338  109 ASP B N   
5908  C CA  . ASP B 109 ? 0.8305 1.1095 1.1543 0.0331  -0.0040 0.0441  109 ASP B CA  
5909  C C   . ASP B 109 ? 0.8415 1.1361 1.1897 0.0248  -0.0240 0.0598  109 ASP B C   
5910  O O   . ASP B 109 ? 0.8238 1.1271 1.1710 0.0120  -0.0383 0.0645  109 ASP B O   
5911  C CB  . ASP B 109 ? 0.8249 1.0975 1.1170 0.0234  -0.0095 0.0324  109 ASP B CB  
5912  C CG  . ASP B 109 ? 0.8660 1.1551 1.1719 0.0162  -0.0143 0.0415  109 ASP B CG  
5913  O OD1 . ASP B 109 ? 0.8411 1.1252 1.1250 0.0060  -0.0244 0.0362  109 ASP B OD1 
5914  O OD2 . ASP B 109 ? 0.9057 1.2120 1.2449 0.0208  -0.0072 0.0547  109 ASP B OD2 
5919  N N   . GLY B 110 ? 0.8451 1.1404 1.2126 0.0310  -0.0256 0.0685  110 GLY B N   
5920  C CA  . GLY B 110 ? 0.8064 1.1155 1.1965 0.0224  -0.0463 0.0854  110 GLY B CA  
5921  C C   . GLY B 110 ? 0.8407 1.1318 1.2098 0.0183  -0.0577 0.0806  110 GLY B C   
5922  O O   . GLY B 110 ? 0.8454 1.1316 1.2273 0.0286  -0.0525 0.0853  110 GLY B O   
5926  N N   . ALA B 111 ? 0.8651 1.1441 1.2008 0.0037  -0.0717 0.0715  111 ALA B N   
5927  C CA  . ALA B 111 ? 0.8492 1.1090 1.1605 -0.0015 -0.0808 0.0655  111 ALA B CA  
5928  C C   . ALA B 111 ? 0.8232 1.0642 1.1101 0.0071  -0.0652 0.0475  111 ALA B C   
5929  O O   . ALA B 111 ? 0.8302 1.0698 1.1088 0.0130  -0.0509 0.0372  111 ALA B O   
5930  C CB  . ALA B 111 ? 0.8472 1.0973 1.1290 -0.0195 -0.0969 0.0617  111 ALA B CB  
5936  N N   . LYS B 112 ? 0.8535 1.0786 1.1267 0.0059  -0.0694 0.0444  112 LYS B N   
5937  C CA  . LYS B 112 ? 0.8059 1.0121 1.0555 0.0110  -0.0572 0.0290  112 LYS B CA  
5938  C C   . LYS B 112 ? 0.7628 0.9625 0.9815 0.0032  -0.0566 0.0134  112 LYS B C   
5939  O O   . LYS B 112 ? 0.7608 0.9479 0.9604 0.0050  -0.0482 0.0013  112 LYS B O   
5940  C CB  . LYS B 112 ? 0.8330 1.0236 1.0756 0.0098  -0.0631 0.0309  112 LYS B CB  
5941  C CG  . LYS B 112 ? 0.8996 1.0969 1.1750 0.0179  -0.0659 0.0492  112 LYS B CG  
5942  C CD  . LYS B 112 ? 0.9151 1.0967 1.1934 0.0326  -0.0487 0.0466  112 LYS B CD  
5943  C CE  . LYS B 112 ? 0.9810 1.1578 1.2770 0.0370  -0.0560 0.0619  112 LYS B CE  
5944  N NZ  . LYS B 112 ? 1.0061 1.1712 1.3170 0.0555  -0.0361 0.0654  112 LYS B NZ  
5958  N N   . ASN B 113 ? 0.7744 0.9812 0.9876 -0.0060 -0.0654 0.0146  113 ASN B N   
5959  C CA  . ASN B 113 ? 0.8025 1.0057 0.9923 -0.0106 -0.0627 0.0025  113 ASN B CA  
5960  C C   . ASN B 113 ? 0.7935 1.0085 0.9898 -0.0079 -0.0572 0.0027  113 ASN B C   
5961  O O   . ASN B 113 ? 0.7871 1.0004 0.9668 -0.0106 -0.0552 -0.0051 113 ASN B O   
5962  C CB  . ASN B 113 ? 0.8114 1.0057 0.9823 -0.0227 -0.0735 0.0020  113 ASN B CB  
5963  C CG  . ASN B 113 ? 0.8063 1.0051 0.9833 -0.0309 -0.0847 0.0131  113 ASN B CG  
5964  O OD1 . ASN B 113 ? 0.8093 1.0180 1.0097 -0.0300 -0.0908 0.0258  113 ASN B OD1 
5965  N ND2 . ASN B 113 ? 0.8100 1.0005 0.9662 -0.0394 -0.0873 0.0095  113 ASN B ND2 
5972  N N   . LYS B 114 ? 0.7831 1.0105 1.0048 -0.0024 -0.0542 0.0126  114 LYS B N   
5973  C CA  . LYS B 114 ? 0.8226 1.0609 1.0516 -0.0001 -0.0479 0.0139  114 LYS B CA  
5974  C C   . LYS B 114 ? 0.8114 1.0481 1.0437 0.0116  -0.0306 0.0091  114 LYS B C   
5975  O O   . LYS B 114 ? 0.8132 1.0472 1.0589 0.0199  -0.0232 0.0127  114 LYS B O   
5976  C CB  . LYS B 114 ? 0.8357 1.0899 1.0917 -0.0041 -0.0558 0.0300  114 LYS B CB  
5977  C CG  . LYS B 114 ? 0.8209 1.0723 1.0638 -0.0189 -0.0710 0.0333  114 LYS B CG  
5978  C CD  . LYS B 114 ? 0.8699 1.1383 1.1373 -0.0246 -0.0774 0.0484  114 LYS B CD  
5979  C CE  . LYS B 114 ? 0.9276 1.1872 1.1775 -0.0424 -0.0945 0.0531  114 LYS B CE  
5980  N NZ  . LYS B 114 ? 0.9446 1.1800 1.1548 -0.0471 -0.0949 0.0392  114 LYS B NZ  
5994  N N   . PHE B 115 ? 0.8320 1.0673 1.0494 0.0122  -0.0236 0.0014  115 PHE B N   
5995  C CA  . PHE B 115 ? 0.8067 1.0342 1.0169 0.0205  -0.0076 -0.0047 115 PHE B CA  
5996  C C   . PHE B 115 ? 0.7921 1.0260 1.0008 0.0208  -0.0013 -0.0042 115 PHE B C   
5997  O O   . PHE B 115 ? 0.7504 0.9923 0.9586 0.0143  -0.0099 -0.0016 115 PHE B O   
5998  C CB  . PHE B 115 ? 0.7993 1.0102 0.9795 0.0184  -0.0066 -0.0178 115 PHE B CB  
5999  C CG  . PHE B 115 ? 0.8071 1.0089 0.9848 0.0171  -0.0115 -0.0194 115 PHE B CG  
6000  C CD1 . PHE B 115 ? 0.8511 1.0402 1.0318 0.0243  -0.0014 -0.0191 115 PHE B CD1 
6001  C CD2 . PHE B 115 ? 0.8418 1.0447 1.0125 0.0088  -0.0244 -0.0210 115 PHE B CD2 
6002  C CE1 . PHE B 115 ? 0.8525 1.0310 1.0292 0.0227  -0.0059 -0.0201 115 PHE B CE1 
6003  C CE2 . PHE B 115 ? 0.8136 1.0069 0.9804 0.0067  -0.0284 -0.0222 115 PHE B CE2 
6004  C CZ  . PHE B 115 ? 0.8240 1.0054 0.9938 0.0134  -0.0201 -0.0217 115 PHE B CZ  
6014  N N   . LEU B 116 ? 0.8369 1.0632 1.0416 0.0283  0.0152  -0.0067 116 LEU B N   
6015  C CA  . LEU B 116 ? 0.7824 1.0074 0.9751 0.0285  0.0235  -0.0093 116 LEU B CA  
6016  C C   . LEU B 116 ? 0.8007 1.0043 0.9582 0.0282  0.0297  -0.0217 116 LEU B C   
6017  O O   . LEU B 116 ? 0.8544 1.0417 1.0033 0.0324  0.0393  -0.0257 116 LEU B O   
6018  C CB  . LEU B 116 ? 0.7321 0.9644 0.9483 0.0360  0.0393  0.0000  116 LEU B CB  
6019  C CG  . LEU B 116 ? 0.7559 1.0127 1.0079 0.0334  0.0322  0.0147  116 LEU B CG  
6020  C CD1 . LEU B 116 ? 0.6832 0.9490 0.9615 0.0418  0.0509  0.0247  116 LEU B CD1 
6021  C CD2 . LEU B 116 ? 0.7609 1.0234 1.0020 0.0229  0.0190  0.0141  116 LEU B CD2 
6033  N N   . ALA B 117 ? 0.7925 0.9947 0.9288 0.0224  0.0239  -0.0266 117 ALA B N   
6034  C CA  . ALA B 117 ? 0.8185 1.0030 0.9210 0.0187  0.0246  -0.0362 117 ALA B CA  
6035  C C   . ALA B 117 ? 0.8805 1.0586 0.9652 0.0182  0.0320  -0.0369 117 ALA B C   
6036  O O   . ALA B 117 ? 0.8696 1.0600 0.9601 0.0165  0.0263  -0.0326 117 ALA B O   
6037  C CB  . ALA B 117 ? 0.7917 0.9819 0.8862 0.0115  0.0078  -0.0395 117 ALA B CB  
6043  N N   . LYS B 118 ? 0.8580 1.0131 0.9173 0.0189  0.0452  -0.0423 118 LYS B N   
6044  C CA  . LYS B 118 ? 0.9213 1.0635 0.9551 0.0169  0.0532  -0.0438 118 LYS B CA  
6045  C C   . LYS B 118 ? 0.9431 1.0660 0.9364 0.0072  0.0451  -0.0514 118 LYS B C   
6046  O O   . LYS B 118 ? 0.9393 1.0436 0.9149 0.0041  0.0470  -0.0576 118 LYS B O   
6047  C CB  . LYS B 118 ? 0.9191 1.0455 0.9518 0.0246  0.0780  -0.0428 118 LYS B CB  
6048  C CG  . LYS B 118 ? 0.9532 1.0590 0.9517 0.0215  0.0892  -0.0454 118 LYS B CG  
6049  C CD  . LYS B 118 ? 1.0504 1.1334 1.0422 0.0296  0.1180  -0.0459 118 LYS B CD  
6050  C CE  . LYS B 118 ? 1.0646 1.1698 1.0968 0.0385  0.1311  -0.0348 118 LYS B CE  
6051  N NZ  . LYS B 118 ? 1.2751 1.3560 1.2885 0.0432  0.1597  -0.0350 118 LYS B NZ  
6065  N N   . ILE B 119 ? 0.9555 1.0818 0.9338 0.0015  0.0355  -0.0498 119 ILE B N   
6066  C CA  . ILE B 119 ? 0.9610 1.0760 0.9065 -0.0095 0.0225  -0.0533 119 ILE B CA  
6067  C C   . ILE B 119 ? 0.9892 1.0907 0.9053 -0.0138 0.0249  -0.0518 119 ILE B C   
6068  O O   . ILE B 119 ? 0.9894 1.1010 0.9184 -0.0086 0.0295  -0.0465 119 ILE B O   
6069  C CB  . ILE B 119 ? 0.9381 1.0788 0.9030 -0.0125 0.0017  -0.0495 119 ILE B CB  
6070  C CG1 . ILE B 119 ? 0.9553 1.0896 0.8932 -0.0247 -0.0134 -0.0502 119 ILE B CG1 
6071  C CG2 . ILE B 119 ? 0.8961 1.0577 0.8829 -0.0072 -0.0024 -0.0420 119 ILE B CG2 
6072  C CD1 . ILE B 119 ? 0.9311 1.0922 0.8923 -0.0264 -0.0311 -0.0449 119 ILE B CD1 
6084  N N   . LYS B 120 ? 1.0674 1.1437 0.9409 -0.0250 0.0210  -0.0562 120 LYS B N   
6085  C CA  . LYS B 120 ? 1.0366 1.0967 0.8754 -0.0319 0.0197  -0.0541 120 LYS B CA  
6086  C C   . LYS B 120 ? 1.0410 1.1266 0.8920 -0.0350 -0.0026 -0.0454 120 LYS B C   
6087  O O   . LYS B 120 ? 1.0558 1.1562 0.9153 -0.0405 -0.0206 -0.0431 120 LYS B O   
6088  C CB  . LYS B 120 ? 1.1514 1.1728 0.9355 -0.0459 0.0201  -0.0608 120 LYS B CB  
6089  C CG  . LYS B 120 ? 1.2363 1.2424 0.9798 -0.0581 0.0094  -0.0568 120 LYS B CG  
6090  C CD  . LYS B 120 ? 1.2440 1.2706 0.9901 -0.0693 -0.0211 -0.0495 120 LYS B CD  
6091  C CE  . LYS B 120 ? 1.3054 1.3084 1.0010 -0.0857 -0.0339 -0.0454 120 LYS B CE  
6092  N NZ  . LYS B 120 ? 1.2514 1.2857 0.9646 -0.0919 -0.0633 -0.0326 120 LYS B NZ  
6106  N N   . MET B 121 ? 1.0756 1.1653 0.9273 -0.0314 -0.0003 -0.0395 121 MET B N   
6107  C CA  . MET B 121 ? 1.0767 1.1883 0.9411 -0.0317 -0.0188 -0.0299 121 MET B CA  
6108  C C   . MET B 121 ? 1.1258 1.2198 0.9493 -0.0430 -0.0294 -0.0255 121 MET B C   
6109  O O   . MET B 121 ? 1.1716 1.2341 0.9554 -0.0491 -0.0181 -0.0300 121 MET B O   
6110  C CB  . MET B 121 ? 1.0492 1.1767 0.9423 -0.0207 -0.0116 -0.0247 121 MET B CB  
6111  C CG  . MET B 121 ? 1.0054 1.1513 0.9383 -0.0118 -0.0055 -0.0267 121 MET B CG  
6112  S SD  . MET B 121 ? 0.9174 1.0898 0.8798 -0.0103 -0.0233 -0.0233 121 MET B SD  
6113  C CE  . MET B 121 ? 0.8749 1.0590 0.8456 -0.0057 -0.0315 -0.0125 121 MET B CE  
6123  N N   . PRO B 122 ? 1.1230 1.2356 0.9547 -0.0463 -0.0508 -0.0155 122 PRO B N   
6124  C CA  . PRO B 122 ? 1.1132 1.2114 0.9077 -0.0581 -0.0646 -0.0084 122 PRO B CA  
6125  C C   . PRO B 122 ? 1.1453 1.2269 0.9202 -0.0549 -0.0533 -0.0062 122 PRO B C   
6126  O O   . PRO B 122 ? 1.0863 1.1761 0.8852 -0.0428 -0.0389 -0.0067 122 PRO B O   
6127  C CB  . PRO B 122 ? 1.0606 1.1916 0.8848 -0.0570 -0.0876 0.0051  122 PRO B CB  
6128  C CG  . PRO B 122 ? 1.0905 1.2482 0.9641 -0.0414 -0.0801 0.0046  122 PRO B CG  
6129  C CD  . PRO B 122 ? 1.0266 1.1737 0.9021 -0.0393 -0.0627 -0.0091 122 PRO B CD  
6137  N N   . LYS B 123 ? 1.2449 1.3010 0.9729 -0.0678 -0.0607 -0.0029 123 LYS B N   
6138  C CA  . LYS B 123 ? 1.2412 1.2783 0.9443 -0.0670 -0.0513 0.0003  123 LYS B CA  
6139  C C   . LYS B 123 ? 1.2465 1.3059 0.9695 -0.0617 -0.0679 0.0155  123 LYS B C   
6140  O O   . LYS B 123 ? 1.2565 1.3400 1.0001 -0.0627 -0.0897 0.0253  123 LYS B O   
6141  C CB  . LYS B 123 ? 1.3023 1.2965 0.9395 -0.0843 -0.0512 -0.0027 123 LYS B CB  
6142  C CG  . LYS B 123 ? 1.4360 1.3950 1.0428 -0.0868 -0.0246 -0.0176 123 LYS B CG  
6143  C CD  . LYS B 123 ? 1.3916 1.3616 1.0357 -0.0695 0.0024  -0.0233 123 LYS B CD  
6144  C CE  . LYS B 123 ? 1.4566 1.3959 1.0788 -0.0698 0.0284  -0.0360 123 LYS B CE  
6145  N NZ  . LYS B 123 ? 1.4114 1.3741 1.0761 -0.0616 0.0294  -0.0410 123 LYS B NZ  
6159  N N   . PHE B 124 ? 1.2348 1.2855 0.9525 -0.0557 -0.0562 0.0183  124 PHE B N   
6160  C CA  . PHE B 124 ? 1.2425 1.3055 0.9703 -0.0509 -0.0696 0.0330  124 PHE B CA  
6161  C C   . PHE B 124 ? 1.2227 1.2686 0.9075 -0.0655 -0.0898 0.0430  124 PHE B C   
6162  O O   . PHE B 124 ? 1.2880 1.3016 0.9236 -0.0800 -0.0868 0.0366  124 PHE B O   
6163  C CB  . PHE B 124 ? 1.2260 1.2809 0.9567 -0.0422 -0.0511 0.0331  124 PHE B CB  
6164  C CG  . PHE B 124 ? 1.1778 1.1964 0.8606 -0.0509 -0.0352 0.0279  124 PHE B CG  
6165  C CD1 . PHE B 124 ? 1.3136 1.3088 0.9518 -0.0612 -0.0456 0.0362  124 PHE B CD1 
6166  C CD2 . PHE B 124 ? 1.1710 1.1784 0.8540 -0.0486 -0.0091 0.0160  124 PHE B CD2 
6167  C CE1 . PHE B 124 ? 1.2347 1.1922 0.8243 -0.0698 -0.0286 0.0310  124 PHE B CE1 
6168  C CE2 . PHE B 124 ? 1.2443 1.2175 0.8847 -0.0555 0.0093  0.0118  124 PHE B CE2 
6169  C CZ  . PHE B 124 ? 1.2099 1.1563 0.8012 -0.0664 0.0004  0.0185  124 PHE B CZ  
6179  N N   . LEU B 125 ? 1.2247 1.2906 0.9274 -0.0619 -0.1102 0.0596  125 LEU B N   
6180  C CA  . LEU B 125 ? 1.3082 1.3612 0.9742 -0.0754 -0.1326 0.0732  125 LEU B CA  
6181  C C   . LEU B 125 ? 1.2863 1.3180 0.9262 -0.0736 -0.1273 0.0803  125 LEU B C   
6182  O O   . LEU B 125 ? 1.2692 1.2799 0.8659 -0.0873 -0.1425 0.0896  125 LEU B O   
6183  C CB  . LEU B 125 ? 1.2793 1.3686 0.9822 -0.0729 -0.1599 0.0910  125 LEU B CB  
6184  C CG  . LEU B 125 ? 1.3002 1.4061 1.0150 -0.0827 -0.1732 0.0884  125 LEU B CG  
6185  C CD1 . LEU B 125 ? 1.2932 1.4427 1.0601 -0.0751 -0.1940 0.1070  125 LEU B CD1 
6186  C CD2 . LEU B 125 ? 1.3589 1.4335 1.0137 -0.1081 -0.1868 0.0867  125 LEU B CD2 
6198  N N   . SER B 126 ? 1.3050 1.3399 0.9676 -0.0587 -0.1073 0.0768  126 SER B N   
6199  C CA  . SER B 126 ? 1.2266 1.2412 0.8669 -0.0567 -0.1004 0.0833  126 SER B CA  
6200  C C   . SER B 126 ? 1.2466 1.2663 0.9158 -0.0430 -0.0756 0.0751  126 SER B C   
6201  O O   . SER B 126 ? 1.2333 1.2796 0.9485 -0.0315 -0.0731 0.0728  126 SER B O   
6202  C CB  . SER B 126 ? 1.2360 1.2631 0.8861 -0.0522 -0.1235 0.1049  126 SER B CB  
6203  O OG  . SER B 126 ? 1.2511 1.2975 0.9454 -0.0334 -0.1158 0.1096  126 SER B OG  
6209  N N   . LEU B 127 ? 1.2270 1.2203 0.8676 -0.0460 -0.0577 0.0715  127 LEU B N   
6210  C CA  . LEU B 127 ? 1.2314 1.2277 0.8957 -0.0364 -0.0364 0.0669  127 LEU B CA  
6211  C C   . LEU B 127 ? 1.3274 1.3036 0.9676 -0.0368 -0.0350 0.0774  127 LEU B C   
6212  O O   . LEU B 127 ? 1.3817 1.3284 0.9748 -0.0478 -0.0310 0.0779  127 LEU B O   
6213  C CB  . LEU B 127 ? 1.2462 1.2328 0.9056 -0.0400 -0.0114 0.0516  127 LEU B CB  
6214  C CG  . LEU B 127 ? 1.2736 1.2661 0.9596 -0.0332 0.0097  0.0482  127 LEU B CG  
6215  C CD1 . LEU B 127 ? 1.2238 1.2413 0.9532 -0.0220 0.0015  0.0533  127 LEU B CD1 
6216  C CD2 . LEU B 127 ? 1.2958 1.2911 0.9940 -0.0339 0.0302  0.0353  127 LEU B CD2 
6228  N N   . GLU B 128 ? 1.2767 1.2647 0.9450 -0.0254 -0.0376 0.0859  128 GLU B N   
6229  C CA  . GLU B 128 ? 1.3371 1.3051 0.9840 -0.0247 -0.0371 0.0971  128 GLU B CA  
6230  C C   . GLU B 128 ? 1.3134 1.2878 0.9911 -0.0143 -0.0253 0.0974  128 GLU B C   
6231  O O   . GLU B 128 ? 1.2810 1.2774 0.9972 -0.0045 -0.0281 0.0961  128 GLU B O   
6232  C CB  . GLU B 128 ? 1.3786 1.3472 1.0156 -0.0229 -0.0627 0.1148  128 GLU B CB  
6233  C CG  . GLU B 128 ? 1.3145 1.3133 0.9984 -0.0084 -0.0759 0.1232  128 GLU B CG  
6234  C CD  . GLU B 128 ? 1.3706 1.3786 1.0518 -0.0085 -0.1032 0.1413  128 GLU B CD  
6235  O OE1 . GLU B 128 ? 1.3997 1.4165 1.0734 -0.0186 -0.1168 0.1397  128 GLU B OE1 
6236  O OE2 . GLU B 128 ? 1.3605 1.3667 1.0476 0.0010  -0.1114 0.1582  128 GLU B OE2 
6243  N N   . GLU B 129 ? 1.3701 1.3223 1.0273 -0.0180 -0.0117 0.0989  129 GLU B N   
6244  C CA  . GLU B 129 ? 1.3402 1.2909 1.0168 -0.0113 -0.0025 0.1014  129 GLU B CA  
6245  C C   . GLU B 129 ? 1.3450 1.2845 1.0138 -0.0030 -0.0155 0.1176  129 GLU B C   
6246  O O   . GLU B 129 ? 1.4003 1.3202 1.0344 -0.0075 -0.0226 0.1272  129 GLU B O   
6247  C CB  . GLU B 129 ? 1.3797 1.3131 1.0407 -0.0206 0.0188  0.0965  129 GLU B CB  
6248  C CG  . GLU B 129 ? 1.4367 1.3694 1.1187 -0.0175 0.0278  0.0974  129 GLU B CG  
6249  C CD  . GLU B 129 ? 1.5166 1.4494 1.2045 -0.0275 0.0483  0.0899  129 GLU B CD  
6250  O OE1 . GLU B 129 ? 1.5466 1.4995 1.2574 -0.0291 0.0548  0.0803  129 GLU B OE1 
6251  O OE2 . GLU B 129 ? 1.5588 1.4722 1.2298 -0.0337 0.0581  0.0948  129 GLU B OE2 
6258  N N   . ILE B 130 ? 1.3403 1.2899 1.0396 0.0093  -0.0178 0.1212  130 ILE B N   
6259  C CA  . ILE B 130 ? 1.3321 1.2722 1.0311 0.0210  -0.0274 0.1374  130 ILE B CA  
6260  C C   . ILE B 130 ? 1.3677 1.2869 1.0660 0.0239  -0.0127 0.1377  130 ILE B C   
6261  O O   . ILE B 130 ? 1.3625 1.2843 1.0732 0.0190  0.0006  0.1259  130 ILE B O   
6262  C CB  . ILE B 130 ? 1.3281 1.2941 1.0622 0.0347  -0.0407 0.1434  130 ILE B CB  
6263  C CG1 . ILE B 130 ? 1.2877 1.2716 1.0545 0.0374  -0.0310 0.1296  130 ILE B CG1 
6264  C CG2 . ILE B 130 ? 1.3000 1.2828 1.0294 0.0297  -0.0596 0.1480  130 ILE B CG2 
6265  C CD1 . ILE B 130 ? 1.2782 1.2812 1.0795 0.0527  -0.0379 0.1360  130 ILE B CD1 
6277  N N   . ASN B 131 ? 1.3985 1.2954 1.0804 0.0309  -0.0161 0.1523  131 ASN B N   
6278  C CA  . ASN B 131 ? 1.3964 1.2662 1.0710 0.0335  -0.0032 0.1546  131 ASN B CA  
6279  C C   . ASN B 131 ? 1.3913 1.2554 1.0795 0.0530  -0.0092 0.1690  131 ASN B C   
6280  O O   . ASN B 131 ? 1.4050 1.2596 1.0802 0.0600  -0.0198 0.1855  131 ASN B O   
6281  C CB  . ASN B 131 ? 1.4007 1.2405 1.0357 0.0222  0.0032  0.1587  131 ASN B CB  
6282  C CG  . ASN B 131 ? 1.4312 1.2671 1.0613 0.0061  0.0202  0.1451  131 ASN B CG  
6283  O OD1 . ASN B 131 ? 1.5022 1.3389 1.1155 -0.0062 0.0247  0.1405  131 ASN B OD1 
6284  N ND2 . ASN B 131 ? 1.4762 1.3069 1.1206 0.0055  0.0302  0.1398  131 ASN B ND2 
6291  N N   . VAL B 132 ? 1.3966 1.2654 1.1103 0.0618  -0.0019 0.1638  132 VAL B N   
6292  C CA  . VAL B 132 ? 1.3835 1.2458 1.1133 0.0822  -0.0022 0.1764  132 VAL B CA  
6293  C C   . VAL B 132 ? 1.4371 1.2594 1.1492 0.0834  0.0148  0.1751  132 VAL B C   
6294  O O   . VAL B 132 ? 1.4601 1.2754 1.1689 0.0713  0.0256  0.1606  132 VAL B O   
6295  C CB  . VAL B 132 ? 1.3994 1.2930 1.1682 0.0918  -0.0049 0.1719  132 VAL B CB  
6296  C CG1 . VAL B 132 ? 1.4407 1.3166 1.2222 0.1098  0.0067  0.1780  132 VAL B CG1 
6297  C CG2 . VAL B 132 ? 1.4065 1.3335 1.1934 0.0964  -0.0243 0.1821  132 VAL B CG2 
6307  N N   . ASP B 133 ? 1.4771 1.2722 1.1778 0.0976  0.0166  0.1913  133 ASP B N   
6308  C CA  . ASP B 133 ? 1.4701 1.2192 1.1464 0.0981  0.0331  0.1912  133 ASP B CA  
6309  C C   . ASP B 133 ? 1.4780 1.2137 1.1280 0.0733  0.0395  0.1780  133 ASP B C   
6310  O O   . ASP B 133 ? 1.5446 1.2856 1.1791 0.0621  0.0332  0.1796  133 ASP B O   
6311  C CB  . ASP B 133 ? 1.5569 1.2980 1.2505 0.1099  0.0453  0.1865  133 ASP B CB  
6312  C CG  . ASP B 133 ? 1.5912 1.3259 1.3014 0.1375  0.0468  0.2052  133 ASP B CG  
6313  O OD1 . ASP B 133 ? 1.6580 1.3685 1.3702 0.1494  0.0626  0.2043  133 ASP B OD1 
6314  O OD2 . ASP B 133 ? 1.5154 1.2685 1.2361 0.1471  0.0325  0.2217  133 ASP B OD2 
6319  N N   . GLU B 134 ? 1.5220 1.2412 1.1671 0.0633  0.0518  0.1658  134 GLU B N   
6320  C CA  . GLU B 134 ? 1.5222 1.2312 1.1477 0.0391  0.0576  0.1562  134 GLU B CA  
6321  C C   . GLU B 134 ? 1.5113 1.2570 1.1610 0.0254  0.0555  0.1411  134 GLU B C   
6322  O O   . GLU B 134 ? 1.5401 1.2787 1.1842 0.0074  0.0622  0.1328  134 GLU B O   
6323  C CB  . GLU B 134 ? 1.5927 1.2533 1.1907 0.0328  0.0710  0.1555  134 GLU B CB  
6324  C CG  . GLU B 134 ? 1.6152 1.2681 1.2228 0.0347  0.0777  0.1466  134 GLU B CG  
6325  C CD  . GLU B 134 ? 1.6522 1.2851 1.2626 0.0605  0.0831  0.1554  134 GLU B CD  
6326  O OE1 . GLU B 134 ? 1.6386 1.2921 1.2671 0.0792  0.0755  0.1667  134 GLU B OE1 
6327  O OE2 . GLU B 134 ? 1.6689 1.2645 1.2629 0.0615  0.0955  0.1520  134 GLU B OE2 
6334  N N   . TYR B 135 ? 1.4582 1.2431 1.1353 0.0327  0.0458  0.1388  135 TYR B N   
6335  C CA  . TYR B 135 ? 1.4500 1.2687 1.1511 0.0225  0.0442  0.1254  135 TYR B CA  
6336  C C   . TYR B 135 ? 1.4556 1.3055 1.1650 0.0211  0.0352  0.1249  135 TYR B C   
6337  O O   . TYR B 135 ? 1.4160 1.2706 1.1231 0.0323  0.0256  0.1344  135 TYR B O   
6338  C CB  . TYR B 135 ? 1.4337 1.2644 1.1597 0.0325  0.0435  0.1201  135 TYR B CB  
6339  C CG  . TYR B 135 ? 1.4860 1.2798 1.1982 0.0342  0.0538  0.1199  135 TYR B CG  
6340  C CD1 . TYR B 135 ? 1.4942 1.2739 1.1969 0.0156  0.0599  0.1112  135 TYR B CD1 
6341  C CD2 . TYR B 135 ? 1.5119 1.2835 1.2199 0.0540  0.0577  0.1294  135 TYR B CD2 
6342  C CE1 . TYR B 135 ? 1.5368 1.2764 1.2191 0.0143  0.0689  0.1104  135 TYR B CE1 
6343  C CE2 . TYR B 135 ? 1.5548 1.2856 1.2442 0.0557  0.0701  0.1284  135 TYR B CE2 
6344  C CZ  . TYR B 135 ? 1.5732 1.2856 1.2462 0.0347  0.0753  0.1181  135 TYR B CZ  
6345  O OH  . TYR B 135 ? 1.6263 1.2917 1.2731 0.0337  0.0872  0.1166  135 TYR B OH  
6355  N N   . LYS B 136 ? 1.4437 1.3130 1.1615 0.0067  0.0384  0.1147  136 LYS B N   
6356  C CA  . LYS B 136 ? 1.3563 1.2509 1.0791 0.0041  0.0333  0.1114  136 LYS B CA  
6357  C C   . LYS B 136 ? 1.3421 1.2684 1.0969 0.0077  0.0285  0.1022  136 LYS B C   
6358  O O   . LYS B 136 ? 1.3157 1.2498 1.0879 0.0019  0.0338  0.0941  136 LYS B O   
6359  C CB  . LYS B 136 ? 1.4061 1.2984 1.1165 -0.0125 0.0438  0.1075  136 LYS B CB  
6360  C CG  . LYS B 136 ? 1.4577 1.3733 1.1941 -0.0226 0.0512  0.0967  136 LYS B CG  
6361  C CD  . LYS B 136 ? 1.5136 1.4292 1.2408 -0.0363 0.0639  0.0956  136 LYS B CD  
6362  C CE  . LYS B 136 ? 1.5032 1.4358 1.2580 -0.0480 0.0729  0.0905  136 LYS B CE  
6363  N NZ  . LYS B 136 ? 1.4234 1.3872 1.2056 -0.0469 0.0747  0.0824  136 LYS B NZ  
6377  N N   . LEU B 137 ? 1.3371 1.2807 1.0982 0.0159  0.0173  0.1043  137 LEU B N   
6378  C CA  . LEU B 137 ? 1.2978 1.2699 1.0873 0.0200  0.0116  0.0969  137 LEU B CA  
6379  C C   . LEU B 137 ? 1.3176 1.3063 1.1033 0.0139  0.0072  0.0922  137 LEU B C   
6380  O O   . LEU B 137 ? 1.3252 1.3024 1.0842 0.0093  0.0052  0.0970  137 LEU B O   
6381  C CB  . LEU B 137 ? 1.2720 1.2504 1.0763 0.0360  0.0018  0.1049  137 LEU B CB  
6382  C CG  . LEU B 137 ? 1.2392 1.2050 1.0542 0.0449  0.0083  0.1061  137 LEU B CG  
6383  C CD1 . LEU B 137 ? 1.1956 1.1710 1.0267 0.0371  0.0146  0.0928  137 LEU B CD1 
6384  C CD2 . LEU B 137 ? 1.2546 1.1845 1.0440 0.0448  0.0162  0.1134  137 LEU B CD2 
6396  N N   . GLY B 138 ? 1.3763 1.3882 1.1849 0.0132  0.0061  0.0827  138 GLY B N   
6397  C CA  . GLY B 138 ? 1.2990 1.3243 1.1041 0.0094  0.0006  0.0782  138 GLY B CA  
6398  C C   . GLY B 138 ? 1.2783 1.3186 1.0948 0.0181  -0.0160 0.0839  138 GLY B C   
6399  O O   . GLY B 138 ? 1.3317 1.3776 1.1679 0.0287  -0.0198 0.0890  138 GLY B O   
6403  N N   . LEU B 139 ? 1.2128 1.2582 1.0157 0.0127  -0.0250 0.0835  139 LEU B N   
6404  C CA  . LEU B 139 ? 1.2012 1.2633 1.0153 0.0180  -0.0432 0.0912  139 LEU B CA  
6405  C C   . LEU B 139 ? 1.1936 1.2620 0.9954 0.0074  -0.0493 0.0839  139 LEU B C   
6406  O O   . LEU B 139 ? 1.2022 1.2562 0.9701 -0.0016 -0.0560 0.0877  139 LEU B O   
6407  C CB  . LEU B 139 ? 1.2323 1.2850 1.0323 0.0228  -0.0556 0.1086  139 LEU B CB  
6408  C CG  . LEU B 139 ? 1.2461 1.3187 1.0599 0.0271  -0.0768 0.1215  139 LEU B CG  
6409  C CD1 . LEU B 139 ? 1.1565 1.2564 1.0111 0.0350  -0.0778 0.1176  139 LEU B CD1 
6410  C CD2 . LEU B 139 ? 1.2786 1.3440 1.0910 0.0372  -0.0856 0.1416  139 LEU B CD2 
6422  N N   . VAL B 140 ? 1.1896 1.2757 1.0152 0.0078  -0.0466 0.0736  140 VAL B N   
6423  C CA  . VAL B 140 ? 1.1527 1.2440 0.9692 -0.0012 -0.0524 0.0665  140 VAL B CA  
6424  C C   . VAL B 140 ? 1.1666 1.2799 1.0028 0.0022  -0.0722 0.0754  140 VAL B C   
6425  O O   . VAL B 140 ? 1.1541 1.2869 1.0261 0.0122  -0.0724 0.0764  140 VAL B O   
6426  C CB  . VAL B 140 ? 1.1344 1.2315 0.9661 -0.0026 -0.0376 0.0513  140 VAL B CB  
6427  C CG1 . VAL B 140 ? 1.1235 1.2129 0.9321 -0.0133 -0.0379 0.0430  140 VAL B CG1 
6428  C CG2 . VAL B 140 ? 1.1188 1.2045 0.9500 -0.0023 -0.0184 0.0469  140 VAL B CG2 
6438  N N   . ARG B 141 ? 1.1782 1.2879 0.9906 -0.0072 -0.0889 0.0826  141 ARG B N   
6439  C CA  . ARG B 141 ? 1.1934 1.3269 1.0257 -0.0065 -0.1103 0.0942  141 ARG B CA  
6440  C C   . ARG B 141 ? 1.1895 1.3300 1.0194 -0.0175 -0.1151 0.0840  141 ARG B C   
6441  O O   . ARG B 141 ? 1.2318 1.3501 1.0228 -0.0314 -0.1130 0.0754  141 ARG B O   
6442  C CB  . ARG B 141 ? 1.2178 1.3449 1.0270 -0.0121 -0.1302 0.1121  141 ARG B CB  
6443  C CG  . ARG B 141 ? 1.2703 1.3871 1.0789 -0.0011 -0.1261 0.1237  141 ARG B CG  
6444  C CD  . ARG B 141 ? 1.2424 1.3617 1.0413 -0.0032 -0.1498 0.1462  141 ARG B CD  
6445  N NE  . ARG B 141 ? 1.2680 1.4056 1.1068 0.0159  -0.1525 0.1629  141 ARG B NE  
6446  C CZ  . ARG B 141 ? 1.3182 1.4408 1.1497 0.0250  -0.1500 0.1749  141 ARG B CZ  
6447  N NH1 . ARG B 141 ? 1.3500 1.4409 1.1361 0.0159  -0.1463 0.1728  141 ARG B NH1 
6448  N NH2 . ARG B 141 ? 1.3443 1.4819 1.2137 0.0440  -0.1496 0.1896  141 ARG B NH2 
6462  N N   . PHE B 142 ? 1.2365 1.4046 1.1055 -0.0114 -0.1197 0.0849  142 PHE B N   
6463  C CA  . PHE B 142 ? 1.2860 1.4625 1.1563 -0.0215 -0.1257 0.0768  142 PHE B CA  
6464  C C   . PHE B 142 ? 1.3110 1.5141 1.2016 -0.0247 -0.1500 0.0932  142 PHE B C   
6465  O O   . PHE B 142 ? 1.2967 1.5111 1.1994 -0.0187 -0.1619 0.1114  142 PHE B O   
6466  C CB  . PHE B 142 ? 1.1793 1.3654 1.0782 -0.0135 -0.1092 0.0632  142 PHE B CB  
6467  C CG  . PHE B 142 ? 1.1232 1.2875 1.0056 -0.0134 -0.0878 0.0485  142 PHE B CG  
6468  C CD1 . PHE B 142 ? 1.1109 1.2563 0.9645 -0.0244 -0.0811 0.0364  142 PHE B CD1 
6469  C CD2 . PHE B 142 ? 1.0971 1.2590 0.9934 -0.0025 -0.0737 0.0478  142 PHE B CD2 
6470  C CE1 . PHE B 142 ? 1.1236 1.2527 0.9685 -0.0227 -0.0600 0.0254  142 PHE B CE1 
6471  C CE2 . PHE B 142 ? 1.0708 1.2174 0.9575 -0.0034 -0.0553 0.0369  142 PHE B CE2 
6472  C CZ  . PHE B 142 ? 1.0949 1.2274 0.9590 -0.0126 -0.0480 0.0265  142 PHE B CZ  
6482  N N   . SER B 143 ? 1.3053 1.5193 1.2018 -0.0342 -0.1572 0.0879  143 SER B N   
6483  C CA  . SER B 143 ? 1.3393 1.5835 1.2616 -0.0389 -0.1797 0.1035  143 SER B CA  
6484  C C   . SER B 143 ? 1.3831 1.6572 1.3603 -0.0216 -0.1709 0.1058  143 SER B C   
6485  O O   . SER B 143 ? 1.3695 1.6471 1.3584 -0.0215 -0.1608 0.0925  143 SER B O   
6486  C CB  . SER B 143 ? 1.3788 1.6156 1.2749 -0.0605 -0.1918 0.0966  143 SER B CB  
6487  O OG  . SER B 143 ? 1.4499 1.6462 1.2879 -0.0740 -0.1868 0.0853  143 SER B OG  
6493  N N   . GLY B 144 ? 1.4716 1.7640 1.4803 -0.0066 -0.1734 0.1230  144 GLY B N   
6494  C CA  . GLY B 144 ? 1.4289 1.7446 1.4856 0.0106  -0.1624 0.1265  144 GLY B CA  
6495  C C   . GLY B 144 ? 1.4067 1.7063 1.4674 0.0280  -0.1400 0.1208  144 GLY B C   
6496  O O   . GLY B 144 ? 1.4082 1.7196 1.4999 0.0447  -0.1341 0.1327  144 GLY B O   
6500  N N   . ILE B 145 ? 1.3991 1.6705 1.4283 0.0240  -0.1267 0.1035  145 ILE B N   
6501  C CA  . ILE B 145 ? 1.4135 1.6672 1.4418 0.0361  -0.1070 0.0974  145 ILE B CA  
6502  C C   . ILE B 145 ? 1.4365 1.6652 1.4296 0.0325  -0.1064 0.0986  145 ILE B C   
6503  O O   . ILE B 145 ? 1.4397 1.6568 1.4010 0.0186  -0.1140 0.0950  145 ILE B O   
6504  C CB  . ILE B 145 ? 1.4290 1.6747 1.4573 0.0343  -0.0913 0.0780  145 ILE B CB  
6505  C CG1 . ILE B 145 ? 1.4072 1.6383 1.4404 0.0455  -0.0735 0.0742  145 ILE B CG1 
6506  C CG2 . ILE B 145 ? 1.4272 1.6552 1.4220 0.0203  -0.0898 0.0645  145 ILE B CG2 
6507  C CD1 . ILE B 145 ? 1.3910 1.6277 1.4474 0.0613  -0.0700 0.0879  145 ILE B CD1 
6519  N N   . ASN B 146 ? 1.3096 1.5265 1.3054 0.0447  -0.0960 0.1038  146 ASN B N   
6520  C CA  . ASN B 146 ? 1.2524 1.4436 1.2161 0.0424  -0.0924 0.1050  146 ASN B CA  
6521  C C   . ASN B 146 ? 1.2011 1.3741 1.1632 0.0479  -0.0719 0.0945  146 ASN B C   
6522  O O   . ASN B 146 ? 1.2030 1.3727 1.1806 0.0606  -0.0641 0.1004  146 ASN B O   
6523  C CB  . ASN B 146 ? 1.2710 1.4636 1.2366 0.0501  -0.1035 0.1260  146 ASN B CB  
6524  C CG  . ASN B 146 ? 1.2972 1.5048 1.2571 0.0399  -0.1275 0.1383  146 ASN B CG  
6525  O OD1 . ASN B 146 ? 1.2716 1.4787 1.2126 0.0242  -0.1345 0.1290  146 ASN B OD1 
6526  N ND2 . ASN B 146 ? 1.3348 1.5542 1.3102 0.0482  -0.1405 0.1604  146 ASN B ND2 
6533  N N   . HIS B 147 ? 1.1438 1.3041 1.0872 0.0380  -0.0627 0.0800  147 HIS B N   
6534  C CA  . HIS B 147 ? 1.1004 1.2468 1.0441 0.0397  -0.0461 0.0710  147 HIS B CA  
6535  C C   . HIS B 147 ? 1.1063 1.2291 1.0264 0.0393  -0.0399 0.0758  147 HIS B C   
6536  O O   . HIS B 147 ? 1.1580 1.2722 1.0546 0.0345  -0.0462 0.0817  147 HIS B O   
6537  C CB  . HIS B 147 ? 1.0878 1.2357 1.0294 0.0300  -0.0389 0.0559  147 HIS B CB  
6538  C CG  . HIS B 147 ? 1.0851 1.2517 1.0506 0.0310  -0.0413 0.0497  147 HIS B CG  
6539  N ND1 . HIS B 147 ? 1.0740 1.2461 1.0618 0.0389  -0.0370 0.0497  147 HIS B ND1 
6540  C CD2 . HIS B 147 ? 1.0642 1.2419 1.0315 0.0245  -0.0467 0.0433  147 HIS B CD2 
6541  C CE1 . HIS B 147 ? 1.0704 1.2581 1.0742 0.0372  -0.0401 0.0440  147 HIS B CE1 
6542  N NE2 . HIS B 147 ? 1.0532 1.2450 1.0458 0.0286  -0.0463 0.0400  147 HIS B NE2 
6550  N N   . PHE B 148 ? 1.1338 1.2434 1.0570 0.0428  -0.0279 0.0735  148 PHE B N   
6551  C CA  . PHE B 148 ? 1.1454 1.2305 1.0469 0.0414  -0.0206 0.0777  148 PHE B CA  
6552  C C   . PHE B 148 ? 1.1358 1.2124 1.0367 0.0332  -0.0078 0.0673  148 PHE B C   
6553  O O   . PHE B 148 ? 1.0979 1.1749 1.0134 0.0352  -0.0033 0.0631  148 PHE B O   
6554  C CB  . PHE B 148 ? 1.1213 1.1938 1.0255 0.0544  -0.0197 0.0897  148 PHE B CB  
6555  C CG  . PHE B 148 ? 1.1170 1.1983 1.0241 0.0629  -0.0329 0.1048  148 PHE B CG  
6556  C CD1 . PHE B 148 ? 1.1201 1.2271 1.0539 0.0697  -0.0423 0.1093  148 PHE B CD1 
6557  C CD2 . PHE B 148 ? 1.1825 1.2472 1.0670 0.0636  -0.0368 0.1161  148 PHE B CD2 
6558  C CE1 . PHE B 148 ? 1.1185 1.2377 1.0599 0.0764  -0.0565 0.1260  148 PHE B CE1 
6559  C CE2 . PHE B 148 ? 1.1264 1.2008 1.0155 0.0708  -0.0515 0.1327  148 PHE B CE2 
6560  C CZ  . PHE B 148 ? 1.1684 1.2717 1.0878 0.0770  -0.0620 0.1383  148 PHE B CZ  
6570  N N   . ILE B 149 ? 1.1596 1.2282 1.0435 0.0232  -0.0021 0.0643  149 ILE B N   
6571  C CA  . ILE B 149 ? 1.1256 1.1888 1.0124 0.0144  0.0092  0.0581  149 ILE B CA  
6572  C C   . ILE B 149 ? 1.1447 1.1833 1.0174 0.0140  0.0147  0.0644  149 ILE B C   
6573  O O   . ILE B 149 ? 1.2042 1.2269 1.0565 0.0169  0.0134  0.0728  149 ILE B O   
6574  C CB  . ILE B 149 ? 1.1403 1.2062 1.0185 0.0048  0.0163  0.0537  149 ILE B CB  
6575  C CG1 . ILE B 149 ? 1.1455 1.2251 1.0241 0.0055  0.0106  0.0491  149 ILE B CG1 
6576  C CG2 . ILE B 149 ? 1.1037 1.1760 0.9990 -0.0034 0.0261  0.0485  149 ILE B CG2 
6577  C CD1 . ILE B 149 ? 1.1213 1.2208 1.0260 0.0095  0.0050  0.0431  149 ILE B CD1 
6589  N N   . PHE B 150 ? 1.1014 1.1343 0.9821 0.0091  0.0199  0.0611  150 PHE B N   
6590  C CA  . PHE B 150 ? 1.1072 1.1123 0.9708 0.0052  0.0257  0.0659  150 PHE B CA  
6591  C C   . PHE B 150 ? 1.1103 1.1175 0.9804 -0.0107 0.0313  0.0618  150 PHE B C   
6592  O O   . PHE B 150 ? 1.1377 1.1480 1.0200 -0.0153 0.0301  0.0576  150 PHE B O   
6593  C CB  . PHE B 150 ? 1.1329 1.1217 0.9950 0.0149  0.0253  0.0682  150 PHE B CB  
6594  C CG  . PHE B 150 ? 1.1743 1.1270 1.0125 0.0109  0.0324  0.0728  150 PHE B CG  
6595  C CD1 . PHE B 150 ? 1.2317 1.1630 1.0489 0.0171  0.0343  0.0821  150 PHE B CD1 
6596  C CD2 . PHE B 150 ? 1.1672 1.1046 1.0011 -0.0004 0.0362  0.0685  150 PHE B CD2 
6597  C CE1 . PHE B 150 ? 1.2780 1.1719 1.0701 0.0132  0.0417  0.0862  150 PHE B CE1 
6598  C CE2 . PHE B 150 ? 1.1698 1.0691 0.9765 -0.0063 0.0426  0.0723  150 PHE B CE2 
6599  C CZ  . PHE B 150 ? 1.2771 1.1539 1.0629 0.0010  0.0462  0.0808  150 PHE B CZ  
6609  N N   . ASN B 151 ? 1.1557 1.1619 1.0182 -0.0196 0.0373  0.0641  151 ASN B N   
6610  C CA  . ASN B 151 ? 1.1533 1.1640 1.0257 -0.0353 0.0430  0.0639  151 ASN B CA  
6611  C C   . ASN B 151 ? 1.1644 1.1465 1.0200 -0.0434 0.0435  0.0678  151 ASN B C   
6612  O O   . ASN B 151 ? 1.2059 1.1631 1.0368 -0.0451 0.0476  0.0736  151 ASN B O   
6613  C CB  . ASN B 151 ? 1.1723 1.1878 1.0405 -0.0415 0.0521  0.0667  151 ASN B CB  
6614  C CG  . ASN B 151 ? 1.2042 1.2367 1.0958 -0.0557 0.0586  0.0678  151 ASN B CG  
6615  O OD1 . ASN B 151 ? 1.2402 1.2694 1.1391 -0.0664 0.0553  0.0700  151 ASN B OD1 
6616  N ND2 . ASN B 151 ? 1.2088 1.2587 1.1119 -0.0564 0.0681  0.0672  151 ASN B ND2 
6623  N N   . ILE B 152 ? 1.2067 1.1885 1.0717 -0.0495 0.0392  0.0648  152 ILE B N   
6624  C CA  . ILE B 152 ? 1.2047 1.1523 1.0468 -0.0586 0.0395  0.0674  152 ILE B CA  
6625  C C   . ILE B 152 ? 1.2445 1.1826 1.0779 -0.0768 0.0438  0.0736  152 ILE B C   
6626  O O   . ILE B 152 ? 1.2987 1.2025 1.1022 -0.0805 0.0476  0.0780  152 ILE B O   
6627  C CB  . ILE B 152 ? 1.1457 1.0935 0.9959 -0.0649 0.0334  0.0628  152 ILE B CB  
6628  C CG1 . ILE B 152 ? 1.1316 1.0795 0.9837 -0.0463 0.0319  0.0578  152 ILE B CG1 
6629  C CG2 . ILE B 152 ? 1.2075 1.1175 1.0299 -0.0813 0.0336  0.0655  152 ILE B CG2 
6630  C CD1 . ILE B 152 ? 1.1477 1.1012 1.0104 -0.0513 0.0264  0.0524  152 ILE B CD1 
6642  N N   . LYS B 153 ? 1.2261 1.1946 1.0869 -0.0884 0.0441  0.0750  153 LYS B N   
6643  C CA  . LYS B 153 ? 1.2444 1.2094 1.1041 -0.1078 0.0480  0.0825  153 LYS B CA  
6644  C C   . LYS B 153 ? 1.2735 1.2234 1.1119 -0.1045 0.0576  0.0868  153 LYS B C   
6645  O O   . LYS B 153 ? 1.2811 1.2061 1.0985 -0.1177 0.0608  0.0928  153 LYS B O   
6646  C CB  . LYS B 153 ? 1.2186 1.2250 1.1200 -0.1174 0.0481  0.0853  153 LYS B CB  
6647  C CG  . LYS B 153 ? 1.2195 1.2410 1.1422 -0.1233 0.0367  0.0832  153 LYS B CG  
6648  C CD  . LYS B 153 ? 1.2442 1.2460 1.1549 -0.1469 0.0284  0.0891  153 LYS B CD  
6649  C CE  . LYS B 153 ? 1.2514 1.2383 1.1514 -0.1486 0.0171  0.0836  153 LYS B CE  
6650  N NZ  . LYS B 153 ? 1.2632 1.2553 1.1737 -0.1743 0.0048  0.0908  153 LYS B NZ  
6664  N N   . GLU B 154 ? 1.2752 1.2369 1.1152 -0.0887 0.0617  0.0843  154 GLU B N   
6665  C CA  . GLU B 154 ? 1.3143 1.2612 1.1314 -0.0861 0.0700  0.0887  154 GLU B CA  
6666  C C   . GLU B 154 ? 1.3512 1.2616 1.1327 -0.0756 0.0673  0.0909  154 GLU B C   
6667  O O   . GLU B 154 ? 1.3693 1.2672 1.1299 -0.0701 0.0713  0.0950  154 GLU B O   
6668  C CB  . GLU B 154 ? 1.2996 1.2698 1.1272 -0.0759 0.0750  0.0856  154 GLU B CB  
6669  C CG  . GLU B 154 ? 1.3056 1.3099 1.1688 -0.0832 0.0820  0.0847  154 GLU B CG  
6670  C CD  . GLU B 154 ? 1.3600 1.3735 1.2207 -0.0772 0.0936  0.0833  154 GLU B CD  
6671  O OE1 . GLU B 154 ? 1.3654 1.4024 1.2531 -0.0821 0.1044  0.0842  154 GLU B OE1 
6672  O OE2 . GLU B 154 ? 1.3932 1.3889 1.2243 -0.0681 0.0924  0.0821  154 GLU B OE2 
6679  N N   . ASN B 155 ? 1.3509 1.2419 1.1240 -0.0725 0.0615  0.0893  155 ASN B N   
6680  C CA  . ASN B 155 ? 1.4007 1.2572 1.1445 -0.0595 0.0611  0.0928  155 ASN B CA  
6681  C C   . ASN B 155 ? 1.4301 1.2479 1.1506 -0.0695 0.0629  0.0944  155 ASN B C   
6682  O O   . ASN B 155 ? 1.4623 1.2820 1.1896 -0.0872 0.0611  0.0922  155 ASN B O   
6683  C CB  . ASN B 155 ? 1.3633 1.2320 1.1188 -0.0389 0.0550  0.0895  155 ASN B CB  
6684  C CG  . ASN B 155 ? 1.4072 1.2830 1.1576 -0.0250 0.0527  0.0940  155 ASN B CG  
6685  O OD1 . ASN B 155 ? 1.4174 1.2996 1.1620 -0.0312 0.0558  0.0960  155 ASN B OD1 
6686  N ND2 . ASN B 155 ? 1.4264 1.3004 1.1782 -0.0070 0.0475  0.0966  155 ASN B ND2 
6693  N N   . LYS B 156 ? 1.4990 1.2794 1.1899 -0.0586 0.0663  0.0994  156 LYS B N   
6694  C CA  . LYS B 156 ? 1.5387 1.2724 1.1991 -0.0662 0.0706  0.1007  156 LYS B CA  
6695  C C   . LYS B 156 ? 1.5349 1.2653 1.2015 -0.0641 0.0681  0.0936  156 LYS B C   
6696  O O   . LYS B 156 ? 1.4927 1.2463 1.1810 -0.0472 0.0651  0.0902  156 LYS B O   
6697  C CB  . LYS B 156 ? 1.5570 1.2512 1.1868 -0.0504 0.0766  0.1086  156 LYS B CB  
6698  C CG  . LYS B 156 ? 1.6150 1.2519 1.2063 -0.0571 0.0841  0.1100  156 LYS B CG  
6699  C CD  . LYS B 156 ? 1.6420 1.2410 1.2076 -0.0366 0.0914  0.1192  156 LYS B CD  
6700  C CE  . LYS B 156 ? 1.6251 1.2319 1.2076 -0.0090 0.0922  0.1199  156 LYS B CE  
6701  N NZ  . LYS B 156 ? 1.6577 1.2118 1.2107 0.0077  0.1040  0.1276  156 LYS B NZ  
6715  N N   . GLU B 157 ? 1.5820 1.2814 1.2269 -0.0833 0.0692  0.0919  157 GLU B N   
6716  C CA  . GLU B 157 ? 1.6105 1.2953 1.2502 -0.0839 0.0682  0.0853  157 GLU B CA  
6717  C C   . GLU B 157 ? 1.5857 1.2466 1.2140 -0.0569 0.0766  0.0857  157 GLU B C   
6718  O O   . GLU B 157 ? 1.6076 1.2351 1.2118 -0.0456 0.0850  0.0923  157 GLU B O   
6719  C CB  . GLU B 157 ? 1.6911 1.3325 1.2956 -0.1106 0.0685  0.0850  157 GLU B CB  
6720  C CG  . GLU B 157 ? 1.7165 1.3475 1.3153 -0.1200 0.0642  0.0779  157 GLU B CG  
6721  C CD  . GLU B 157 ? 1.8080 1.3677 1.3513 -0.1283 0.0728  0.0766  157 GLU B CD  
6722  O OE1 . GLU B 157 ? 1.8242 1.3480 1.3353 -0.1451 0.0753  0.0812  157 GLU B OE1 
6723  O OE2 . GLU B 157 ? 1.8519 1.3888 1.3816 -0.1184 0.0784  0.0710  157 GLU B OE2 
6730  N N   . THR B 158 ? 1.5873 1.2663 1.2351 -0.0461 0.0749  0.0799  158 THR B N   
6731  C CA  . THR B 158 ? 1.5862 1.2514 1.2329 -0.0192 0.0836  0.0818  158 THR B CA  
6732  C C   . THR B 158 ? 1.5702 1.2431 1.2282 -0.0172 0.0833  0.0737  158 THR B C   
6733  O O   . THR B 158 ? 1.5563 1.2471 1.2234 -0.0358 0.0745  0.0672  158 THR B O   
6734  C CB  . THR B 158 ? 1.5408 1.2435 1.2168 0.0023  0.0798  0.0884  158 THR B CB  
6735  O OG1 . THR B 158 ? 1.5253 1.2288 1.2136 0.0270  0.0855  0.0910  158 THR B OG1 
6736  C CG2 . THR B 158 ? 1.4922 1.2514 1.2040 -0.0051 0.0673  0.0841  158 THR B CG2 
6744  N N   . SER B 159 ? 1.5621 1.2222 1.2211 0.0062  0.0936  0.0756  159 SER B N   
6745  C CA  . SER B 159 ? 1.5689 1.2372 1.2402 0.0122  0.0959  0.0691  159 SER B CA  
6746  C C   . SER B 159 ? 1.5126 1.2388 1.2317 0.0296  0.0880  0.0709  159 SER B C   
6747  O O   . SER B 159 ? 1.4941 1.2365 1.2286 0.0466  0.0873  0.0799  159 SER B O   
6748  C CB  . SER B 159 ? 1.6059 1.2209 1.2481 0.0271  0.1156  0.0706  159 SER B CB  
6749  O OG  . SER B 159 ? 1.6109 1.2388 1.2760 0.0570  0.1229  0.0806  159 SER B OG  
6755  N N   . PHE B 160 ? 1.5326 1.2881 1.2729 0.0238  0.0810  0.0631  160 PHE B N   
6756  C CA  . PHE B 160 ? 1.5139 1.3207 1.2962 0.0381  0.0737  0.0640  160 PHE B CA  
6757  C C   . PHE B 160 ? 1.4961 1.3008 1.2895 0.0651  0.0829  0.0734  160 PHE B C   
6758  O O   . PHE B 160 ? 1.4377 1.2772 1.2578 0.0768  0.0752  0.0806  160 PHE B O   
6759  C CB  . PHE B 160 ? 1.5008 1.3259 1.2971 0.0303  0.0692  0.0546  160 PHE B CB  
6760  C CG  . PHE B 160 ? 1.4323 1.2870 1.2416 0.0101  0.0552  0.0491  160 PHE B CG  
6761  C CD1 . PHE B 160 ? 1.4401 1.2881 1.2368 -0.0061 0.0511  0.0509  160 PHE B CD1 
6762  C CD2 . PHE B 160 ? 1.3780 1.2675 1.2139 0.0081  0.0473  0.0433  160 PHE B CD2 
6763  C CE1 . PHE B 160 ? 1.3824 1.2600 1.1966 -0.0227 0.0405  0.0480  160 PHE B CE1 
6764  C CE2 . PHE B 160 ? 1.3984 1.3148 1.2491 -0.0081 0.0362  0.0399  160 PHE B CE2 
6765  C CZ  . PHE B 160 ? 1.3887 1.3004 1.2305 -0.0228 0.0333  0.0428  160 PHE B CZ  
6775  N N   . GLU B 161 ? 1.5167 1.2787 1.2888 0.0746  0.1000  0.0746  161 GLU B N   
6776  C CA  . GLU B 161 ? 1.4995 1.2622 1.2889 0.1022  0.1112  0.0855  161 GLU B CA  
6777  C C   . GLU B 161 ? 1.4886 1.2513 1.2805 0.1148  0.1094  0.0994  161 GLU B C   
6778  O O   . GLU B 161 ? 1.4742 1.2677 1.2986 0.1339  0.1059  0.1111  161 GLU B O   
6779  C CB  . GLU B 161 ? 1.5017 1.2104 1.2622 0.1096  0.1342  0.0838  161 GLU B CB  
6780  C CG  . GLU B 161 ? 1.5011 1.2093 1.2599 0.1008  0.1373  0.0722  161 GLU B CG  
6781  C CD  . GLU B 161 ? 1.5133 1.2048 1.2419 0.0700  0.1276  0.0597  161 GLU B CD  
6782  O OE1 . GLU B 161 ? 1.5464 1.1981 1.2378 0.0567  0.1295  0.0592  161 GLU B OE1 
6783  O OE2 . GLU B 161 ? 1.4877 1.2069 1.2312 0.0586  0.1172  0.0517  161 GLU B OE2 
6790  N N   . ASN B 162 ? 1.4740 1.2025 1.2317 0.1031  0.1106  0.0994  162 ASN B N   
6791  C CA  . ASN B 162 ? 1.5121 1.2376 1.2679 0.1130  0.1082  0.1127  162 ASN B CA  
6792  C C   . ASN B 162 ? 1.4824 1.2633 1.2697 0.1120  0.0882  0.1166  162 ASN B C   
6793  O O   . ASN B 162 ? 1.4824 1.2762 1.2834 0.1273  0.0837  0.1307  162 ASN B O   
6794  C CB  . ASN B 162 ? 1.5366 1.2161 1.2480 0.0960  0.1122  0.1103  162 ASN B CB  
6795  C CG  . ASN B 162 ? 1.5669 1.2477 1.2744 0.1005  0.1062  0.1223  162 ASN B CG  
6796  O OD1 . ASN B 162 ? 1.5886 1.2823 1.3154 0.1223  0.1055  0.1361  162 ASN B OD1 
6797  N ND2 . ASN B 162 ? 1.5890 1.2564 1.2716 0.0791  0.1015  0.1183  162 ASN B ND2 
6804  N N   . ILE B 163 ? 1.4875 1.2993 1.2851 0.0939  0.0764  0.1052  163 ILE B N   
6805  C CA  . ILE B 163 ? 1.4130 1.2706 1.2338 0.0912  0.0598  0.1071  163 ILE B CA  
6806  C C   . ILE B 163 ? 1.3989 1.2946 1.2566 0.1070  0.0535  0.1125  163 ILE B C   
6807  O O   . ILE B 163 ? 1.3959 1.3180 1.2687 0.1131  0.0417  0.1220  163 ILE B O   
6808  C CB  . ILE B 163 ? 1.3373 1.2119 1.1572 0.0681  0.0524  0.0940  163 ILE B CB  
6809  C CG1 . ILE B 163 ? 1.3724 1.2116 1.1594 0.0508  0.0580  0.0909  163 ILE B CG1 
6810  C CG2 . ILE B 163 ? 1.2873 1.2008 1.1240 0.0650  0.0389  0.0951  163 ILE B CG2 
6811  C CD1 . ILE B 163 ? 1.4403 1.2580 1.2062 0.0538  0.0597  0.1014  163 ILE B CD1 
6823  N N   . ILE B 164 ? 1.4168 1.3155 1.2881 0.1121  0.0606  0.1071  164 ILE B N   
6824  C CA  . ILE B 164 ? 1.3813 1.3168 1.2899 0.1265  0.0557  0.1135  164 ILE B CA  
6825  C C   . ILE B 164 ? 1.4130 1.3460 1.3339 0.1488  0.0588  0.1330  164 ILE B C   
6826  O O   . ILE B 164 ? 1.3623 1.3327 1.3135 0.1573  0.0463  0.1441  164 ILE B O   
6827  C CB  . ILE B 164 ? 1.4089 1.3422 1.3264 0.1280  0.0659  0.1046  164 ILE B CB  
6828  C CG1 . ILE B 164 ? 1.4129 1.3343 1.3095 0.1056  0.0652  0.0877  164 ILE B CG1 
6829  C CG2 . ILE B 164 ? 1.3955 1.3762 1.3534 0.1353  0.0566  0.1079  164 ILE B CG2 
6830  C CD1 . ILE B 164 ? 1.3485 1.2765 1.2553 0.1032  0.0694  0.0784  164 ILE B CD1 
6842  N N   . ASP B 165 ? 1.5036 1.3917 1.4009 0.1579  0.0749  0.1386  165 ASP B N   
6843  C CA  . ASP B 165 ? 1.5191 1.4019 1.4287 0.1809  0.0792  0.1593  165 ASP B CA  
6844  C C   . ASP B 165 ? 1.5433 1.4408 1.4500 0.1774  0.0611  0.1699  165 ASP B C   
6845  O O   . ASP B 165 ? 1.5933 1.5197 1.5282 0.1905  0.0501  0.1873  165 ASP B O   
6846  C CB  . ASP B 165 ? 1.6115 1.4350 1.4904 0.1909  0.1032  0.1615  165 ASP B CB  
6847  C CG  . ASP B 165 ? 1.6378 1.4396 1.5131 0.1945  0.1231  0.1518  165 ASP B CG  
6848  O OD1 . ASP B 165 ? 1.6056 1.4407 1.5041 0.1894  0.1175  0.1437  165 ASP B OD1 
6849  O OD2 . ASP B 165 ? 1.6204 1.3679 1.4656 0.2018  0.1450  0.1522  165 ASP B OD2 
6854  N N   . LEU B 166 ? 1.4699 1.3475 1.3424 0.1587  0.0576  0.1607  166 LEU B N   
6855  C CA  . LEU B 166 ? 1.4686 1.3559 1.3325 0.1533  0.0421  0.1694  166 LEU B CA  
6856  C C   . LEU B 166 ? 1.4160 1.3542 1.3070 0.1487  0.0215  0.1712  166 LEU B C   
6857  O O   . LEU B 166 ? 1.4264 1.3804 1.3246 0.1540  0.0073  0.1868  166 LEU B O   
6858  C CB  . LEU B 166 ? 1.4926 1.3543 1.3186 0.1317  0.0437  0.1574  166 LEU B CB  
6859  C CG  . LEU B 166 ? 1.5594 1.3707 1.3506 0.1342  0.0555  0.1640  166 LEU B CG  
6860  C CD1 . LEU B 166 ? 1.5466 1.3359 1.3053 0.1097  0.0587  0.1502  166 LEU B CD1 
6861  C CD2 . LEU B 166 ? 1.5307 1.3424 1.3199 0.1452  0.0462  0.1835  166 LEU B CD2 
6873  N N   . VAL B 167 ? 1.4005 1.3623 1.3041 0.1377  0.0188  0.1560  167 VAL B N   
6874  C CA  . VAL B 167 ? 1.3724 1.3780 1.2984 0.1324  0.0006  0.1566  167 VAL B CA  
6875  C C   . VAL B 167 ? 1.3951 1.4268 1.3570 0.1509  -0.0063 0.1752  167 VAL B C   
6876  O O   . VAL B 167 ? 1.4429 1.4981 1.4138 0.1504  -0.0247 0.1881  167 VAL B O   
6877  C CB  . VAL B 167 ? 1.3160 1.3381 1.2498 0.1194  0.0017  0.1375  167 VAL B CB  
6878  C CG1 . VAL B 167 ? 1.2443 1.3073 1.1994 0.1146  -0.0157 0.1382  167 VAL B CG1 
6879  C CG2 . VAL B 167 ? 1.3105 1.3134 1.2153 0.1009  0.0063  0.1227  167 VAL B CG2 
6889  N N   . LYS B 168 ? 1.3621 1.3893 1.3446 0.1666  0.0087  0.1780  168 LYS B N   
6890  C CA  . LYS B 168 ? 1.3720 1.4265 1.3953 0.1859  0.0051  0.1980  168 LYS B CA  
6891  C C   . LYS B 168 ? 1.3923 1.4405 1.4158 0.1986  -0.0017 0.2213  168 LYS B C   
6892  O O   . LYS B 168 ? 1.3952 1.4771 1.4525 0.2081  -0.0160 0.2415  168 LYS B O   
6893  C CB  . LYS B 168 ? 1.4201 1.4620 1.4602 0.2018  0.0284  0.1966  168 LYS B CB  
6894  C CG  . LYS B 168 ? 1.4456 1.4514 1.4813 0.2239  0.0480  0.2110  168 LYS B CG  
6895  C CD  . LYS B 168 ? 1.4369 1.4729 1.5202 0.2475  0.0453  0.2382  168 LYS B CD  
6896  C CE  . LYS B 168 ? 1.4892 1.4870 1.5664 0.2707  0.0642  0.2548  168 LYS B CE  
6897  N NZ  . LYS B 168 ? 1.4756 1.5065 1.6044 0.2948  0.0601  0.2853  168 LYS B NZ  
6911  N N   . LYS B 169 ? 1.4428 1.4486 1.4295 0.1979  0.0072  0.2203  169 LYS B N   
6912  C CA  . LYS B 169 ? 1.4489 1.4456 1.4298 0.2074  -0.0011 0.2419  169 LYS B CA  
6913  C C   . LYS B 169 ? 1.4461 1.4686 1.4197 0.1911  -0.0287 0.2464  169 LYS B C   
6914  O O   . LYS B 169 ? 1.4731 1.5104 1.4597 0.1990  -0.0446 0.2694  169 LYS B O   
6915  C CB  . LYS B 169 ? 1.4711 1.4127 1.4089 0.2071  0.0152  0.2375  169 LYS B CB  
6916  C CG  . LYS B 169 ? 1.5047 1.4149 1.4482 0.2330  0.0347  0.2539  169 LYS B CG  
6917  C CD  . LYS B 169 ? 1.4948 1.4289 1.4712 0.2528  0.0218  0.2847  169 LYS B CD  
6918  C CE  . LYS B 169 ? 1.5455 1.4843 1.5007 0.2403  -0.0023 0.2941  169 LYS B CE  
6919  N NZ  . LYS B 169 ? 1.5017 1.4701 1.4922 0.2567  -0.0201 0.3259  169 LYS B NZ  
6933  N N   . TYR B 170 ? 1.4376 1.4640 1.3890 0.1682  -0.0343 0.2257  170 TYR B N   
6934  C CA  . TYR B 170 ? 1.4316 1.4740 1.3672 0.1511  -0.0569 0.2274  170 TYR B CA  
6935  C C   . TYR B 170 ? 1.4301 1.5180 1.4011 0.1523  -0.0780 0.2404  170 TYR B C   
6936  O O   . TYR B 170 ? 1.4824 1.5818 1.4502 0.1490  -0.0992 0.2577  170 TYR B O   
6937  C CB  . TYR B 170 ? 1.4076 1.4426 1.3153 0.1289  -0.0530 0.2021  170 TYR B CB  
6938  C CG  . TYR B 170 ? 1.3606 1.3959 1.2378 0.1104  -0.0685 0.2008  170 TYR B CG  
6939  C CD1 . TYR B 170 ? 1.3356 1.3388 1.1745 0.1043  -0.0657 0.2030  170 TYR B CD1 
6940  C CD2 . TYR B 170 ? 1.3383 1.4017 1.2209 0.0981  -0.0844 0.1967  170 TYR B CD2 
6941  C CE1 . TYR B 170 ? 1.3255 1.3246 1.1322 0.0871  -0.0771 0.2014  170 TYR B CE1 
6942  C CE2 . TYR B 170 ? 1.3515 1.4082 1.1995 0.0805  -0.0961 0.1946  170 TYR B CE2 
6943  C CZ  . TYR B 170 ? 1.3254 1.3498 1.1354 0.0754  -0.0917 0.1970  170 TYR B CZ  
6944  O OH  . TYR B 170 ? 1.3069 1.3207 1.0785 0.0577  -0.1008 0.1946  170 TYR B OH  
6954  N N   . LEU B 171 ? 1.4319 1.5450 1.4353 0.1554  -0.0735 0.2331  171 LEU B N   
6955  C CA  . LEU B 171 ? 1.4669 1.6245 1.5058 0.1544  -0.0928 0.2445  171 LEU B CA  
6956  C C   . LEU B 171 ? 1.4859 1.6642 1.5694 0.1773  -0.0956 0.2729  171 LEU B C   
6957  O O   . LEU B 171 ? 1.5028 1.7213 1.6266 0.1795  -0.1069 0.2834  171 LEU B O   
6958  C CB  . LEU B 171 ? 1.4446 1.6203 1.4998 0.1477  -0.0860 0.2253  171 LEU B CB  
6959  C CG  . LEU B 171 ? 1.4044 1.5607 1.4241 0.1290  -0.0785 0.1978  171 LEU B CG  
6960  C CD1 . LEU B 171 ? 1.3268 1.4600 1.3446 0.1355  -0.0532 0.1825  171 LEU B CD1 
6961  C CD2 . LEU B 171 ? 1.4044 1.5879 1.4294 0.1126  -0.0920 0.1875  171 LEU B CD2 
6973  N N   . SER B 172 ? 1.4839 1.6360 1.5627 0.1945  -0.0850 0.2868  172 SER B N   
6974  C CA  . SER B 172 ? 1.5013 1.6718 1.6245 0.2188  -0.0859 0.3167  172 SER B CA  
6975  C C   . SER B 172 ? 1.5615 1.7662 1.7012 0.2135  -0.1192 0.3429  172 SER B C   
6976  O O   . SER B 172 ? 1.5312 1.7589 1.7148 0.2330  -0.1240 0.3719  172 SER B O   
6977  C CB  . SER B 172 ? 1.4915 1.6182 1.5992 0.2383  -0.0647 0.3243  172 SER B CB  
6978  O OG  . SER B 172 ? 1.4715 1.5575 1.5465 0.2348  -0.0390 0.2981  172 SER B OG  
6984  N N   . ASN B 173 ? 1.6676 1.8745 1.7725 0.1874  -0.1418 0.3347  173 ASN B N   
6985  C CA  . ASN B 173 ? 1.6493 1.8858 1.7621 0.1766  -0.1763 0.3576  173 ASN B CA  
6986  C C   . ASN B 173 ? 1.6537 1.9118 1.7550 0.1497  -0.1945 0.3427  173 ASN B C   
6987  O O   . ASN B 173 ? 1.6580 1.9306 1.7478 0.1327  -0.2246 0.3561  173 ASN B O   
6988  C CB  . ASN B 173 ? 1.6984 1.9038 1.7669 0.1709  -0.1882 0.3681  173 ASN B CB  
6989  C CG  . ASN B 173 ? 1.7681 1.9466 1.7738 0.1426  -0.1937 0.3442  173 ASN B CG  
6990  O OD1 . ASN B 173 ? 1.8152 2.0106 1.8084 0.1208  -0.2149 0.3406  173 ASN B OD1 
6991  N ND2 . ASN B 173 ? 1.7935 1.9279 1.7585 0.1425  -0.1738 0.3287  173 ASN B ND2 
6998  N N   . GLU B 174 ? 1.6172 1.8758 1.7199 0.1450  -0.1777 0.3166  174 GLU B N   
6999  C CA  . GLU B 174 ? 1.6208 1.8913 1.7067 0.1203  -0.1899 0.2988  174 GLU B CA  
7000  C C   . GLU B 174 ? 1.5874 1.8948 1.7220 0.1250  -0.1862 0.2971  174 GLU B C   
7001  O O   . GLU B 174 ? 1.5479 1.8536 1.7084 0.1431  -0.1614 0.2912  174 GLU B O   
7002  C CB  . GLU B 174 ? 1.6219 1.8547 1.6580 0.1075  -0.1723 0.2669  174 GLU B CB  
7003  C CG  . GLU B 174 ? 1.6527 1.8758 1.6428 0.0800  -0.1888 0.2555  174 GLU B CG  
7004  C CD  . GLU B 174 ? 1.6725 1.9116 1.6675 0.0664  -0.1890 0.2366  174 GLU B CD  
7005  O OE1 . GLU B 174 ? 1.6313 1.8839 1.6592 0.0771  -0.1731 0.2277  174 GLU B OE1 
7006  O OE2 . GLU B 174 ? 1.7028 1.9375 1.6650 0.0444  -0.2044 0.2307  174 GLU B OE2 
7013  N N   . GLU B 175 ? 1.5895 1.9270 1.7326 0.1072  -0.2109 0.3024  175 GLU B N   
7014  C CA  . GLU B 175 ? 1.5311 1.9034 1.7157 0.1070  -0.2096 0.2996  175 GLU B CA  
7015  C C   . GLU B 175 ? 1.5443 1.8968 1.6983 0.0937  -0.1949 0.2655  175 GLU B C   
7016  O O   . GLU B 175 ? 1.5771 1.9184 1.6913 0.0706  -0.2077 0.2527  175 GLU B O   
7017  C CB  . GLU B 175 ? 1.4869 1.8984 1.6919 0.0910  -0.2437 0.3205  175 GLU B CB  
7018  C CG  . GLU B 175 ? 1.4839 1.9291 1.7397 0.1070  -0.2581 0.3587  175 GLU B CG  
7019  C CD  . GLU B 175 ? 1.4684 1.9329 1.7841 0.1372  -0.2323 0.3678  175 GLU B CD  
7020  O OE1 . GLU B 175 ? 1.4313 1.9103 1.7696 0.1378  -0.2186 0.3544  175 GLU B OE1 
7021  O OE2 . GLU B 175 ? 1.4664 1.9283 1.8042 0.1605  -0.2242 0.3883  175 GLU B OE2 
7028  N N   . TYR B 176 ? 1.5147 1.8605 1.6854 0.1081  -0.1675 0.2515  176 TYR B N   
7029  C CA  . TYR B 176 ? 1.5075 1.8361 1.6550 0.0980  -0.1527 0.2215  176 TYR B CA  
7030  C C   . TYR B 176 ? 1.4740 1.8271 1.6631 0.1056  -0.1418 0.2184  176 TYR B C   
7031  O O   . TYR B 176 ? 1.4558 1.8162 1.6796 0.1266  -0.1267 0.2293  176 TYR B O   
7032  C CB  . TYR B 176 ? 1.5257 1.8129 1.6413 0.1045  -0.1295 0.2051  176 TYR B CB  
7033  C CG  . TYR B 176 ? 1.4961 1.7746 1.6360 0.1282  -0.1066 0.2105  176 TYR B CG  
7034  C CD1 . TYR B 176 ? 1.4923 1.7663 1.6437 0.1452  -0.1059 0.2323  176 TYR B CD1 
7035  C CD2 . TYR B 176 ? 1.4520 1.7229 1.5999 0.1334  -0.0852 0.1941  176 TYR B CD2 
7036  C CE1 . TYR B 176 ? 1.4689 1.7284 1.6377 0.1674  -0.0821 0.2368  176 TYR B CE1 
7037  C CE2 . TYR B 176 ? 1.4484 1.7040 1.6107 0.1535  -0.0628 0.1982  176 TYR B CE2 
7038  C CZ  . TYR B 176 ? 1.4673 1.7159 1.6392 0.1708  -0.0601 0.2190  176 TYR B CZ  
7039  O OH  . TYR B 176 ? 1.4913 1.7185 1.6731 0.1913  -0.0350 0.2227  176 TYR B OH  
7049  N N   . SER B 177 ? 1.4752 1.8382 1.6586 0.0888  -0.1479 0.2037  177 SER B N   
7050  C CA  . SER B 177 ? 1.4427 1.8244 1.6594 0.0938  -0.1363 0.1979  177 SER B CA  
7051  C C   . SER B 177 ? 1.4417 1.7944 1.6465 0.1033  -0.1080 0.1780  177 SER B C   
7052  O O   . SER B 177 ? 1.4478 1.8075 1.6813 0.1164  -0.0916 0.1788  177 SER B O   
7053  C CB  . SER B 177 ? 1.4137 1.8099 1.6231 0.0718  -0.1514 0.1878  177 SER B CB  
7054  O OG  . SER B 177 ? 1.3903 1.8173 1.6169 0.0618  -0.1784 0.2087  177 SER B OG  
7060  N N   . ALA B 178 ? 1.4589 1.7785 1.6213 0.0960  -0.1021 0.1611  178 ALA B N   
7061  C CA  . ALA B 178 ? 1.4452 1.7361 1.5926 0.1012  -0.0790 0.1434  178 ALA B CA  
7062  C C   . ALA B 178 ? 1.4673 1.7280 1.5721 0.0924  -0.0780 0.1330  178 ALA B C   
7063  O O   . ALA B 178 ? 1.4536 1.7146 1.5369 0.0792  -0.0929 0.1328  178 ALA B O   
7064  C CB  . ALA B 178 ? 1.4294 1.7262 1.5822 0.0935  -0.0729 0.1265  178 ALA B CB  
7070  N N   . PHE B 179 ? 1.3510 1.5834 1.4418 0.0988  -0.0596 0.1245  179 PHE B N   
7071  C CA  . PHE B 179 ? 1.3040 1.5086 1.3583 0.0905  -0.0559 0.1151  179 PHE B CA  
7072  C C   . PHE B 179 ? 1.2606 1.4454 1.3054 0.0879  -0.0390 0.0982  179 PHE B C   
7073  O O   . PHE B 179 ? 1.2414 1.4259 1.3021 0.0952  -0.0285 0.0958  179 PHE B O   
7074  C CB  . PHE B 179 ? 1.2525 1.4394 1.2950 0.0996  -0.0550 0.1292  179 PHE B CB  
7075  C CG  . PHE B 179 ? 1.2470 1.4105 1.2919 0.1141  -0.0359 0.1312  179 PHE B CG  
7076  C CD1 . PHE B 179 ? 1.2047 1.3369 1.2232 0.1087  -0.0224 0.1183  179 PHE B CD1 
7077  C CD2 . PHE B 179 ? 1.2916 1.4628 1.3643 0.1324  -0.0310 0.1471  179 PHE B CD2 
7078  C CE1 . PHE B 179 ? 1.2266 1.3310 1.2400 0.1194  -0.0052 0.1196  179 PHE B CE1 
7079  C CE2 . PHE B 179 ? 1.3076 1.4501 1.3765 0.1459  -0.0106 0.1484  179 PHE B CE2 
7080  C CZ  . PHE B 179 ? 1.2734 1.3800 1.3093 0.1383  0.0018  0.1339  179 PHE B CZ  
7090  N N   . GLY B 180 ? 1.1982 1.3660 1.2163 0.0766  -0.0366 0.0876  180 GLY B N   
7091  C CA  . GLY B 180 ? 1.1217 1.2730 1.1313 0.0712  -0.0241 0.0739  180 GLY B CA  
7092  C C   . GLY B 180 ? 1.1076 1.2336 1.0908 0.0654  -0.0178 0.0716  180 GLY B C   
7093  O O   . GLY B 180 ? 1.1299 1.2543 1.0973 0.0596  -0.0235 0.0739  180 GLY B O   
7097  N N   . ILE B 181 ? 1.1171 1.2212 1.0928 0.0653  -0.0061 0.0675  181 ILE B N   
7098  C CA  . ILE B 181 ? 1.0900 1.1701 1.0423 0.0575  0.0001  0.0656  181 ILE B CA  
7099  C C   . ILE B 181 ? 1.0814 1.1630 1.0345 0.0443  0.0034  0.0535  181 ILE B C   
7100  O O   . ILE B 181 ? 1.0480 1.1255 1.0074 0.0433  0.0074  0.0484  181 ILE B O   
7101  C CB  . ILE B 181 ? 1.1218 1.1711 1.0609 0.0652  0.0100  0.0721  181 ILE B CB  
7102  C CG1 . ILE B 181 ? 1.1136 1.1632 1.0564 0.0804  0.0070  0.0869  181 ILE B CG1 
7103  C CG2 . ILE B 181 ? 1.1212 1.1454 1.0353 0.0539  0.0156  0.0699  181 ILE B CG2 
7104  C CD1 . ILE B 181 ? 1.1836 1.2127 1.1289 0.0952  0.0186  0.0937  181 ILE B CD1 
7116  N N   . MET B 182 ? 1.0420 1.1288 0.9886 0.0341  0.0023  0.0500  182 MET B N   
7117  C CA  . MET B 182 ? 0.9939 1.0865 0.9469 0.0224  0.0053  0.0416  182 MET B CA  
7118  C C   . MET B 182 ? 1.0616 1.1329 0.9997 0.0135  0.0120  0.0435  182 MET B C   
7119  O O   . MET B 182 ? 1.0631 1.1318 0.9919 0.0077  0.0149  0.0456  182 MET B O   
7120  C CB  . MET B 182 ? 0.9551 1.0662 0.9131 0.0179  0.0030  0.0374  182 MET B CB  
7121  C CG  . MET B 182 ? 0.9999 1.1285 0.9673 0.0238  -0.0050 0.0361  182 MET B CG  
7122  S SD  . MET B 182 ? 1.0200 1.1642 1.0110 0.0233  -0.0066 0.0280  182 MET B SD  
7123  C CE  . MET B 182 ? 0.9963 1.1427 0.9955 0.0353  -0.0112 0.0338  182 MET B CE  
7133  N N   . PHE B 183 ? 1.0353 1.0887 0.9686 0.0113  0.0149  0.0431  183 PHE B N   
7134  C CA  . PHE B 183 ? 1.0707 1.1021 0.9884 -0.0007 0.0196  0.0449  183 PHE B CA  
7135  C C   . PHE B 183 ? 1.0416 1.0914 0.9744 -0.0147 0.0185  0.0419  183 PHE B C   
7136  O O   . PHE B 183 ? 1.0339 1.0967 0.9827 -0.0190 0.0148  0.0376  183 PHE B O   
7137  C CB  . PHE B 183 ? 1.1260 1.1300 1.0302 -0.0019 0.0225  0.0443  183 PHE B CB  
7138  C CG  . PHE B 183 ? 1.1804 1.1651 1.0731 0.0142  0.0274  0.0489  183 PHE B CG  
7139  C CD1 . PHE B 183 ? 1.1957 1.1540 1.0665 0.0177  0.0327  0.0560  183 PHE B CD1 
7140  C CD2 . PHE B 183 ? 1.1766 1.1701 1.0825 0.0265  0.0275  0.0475  183 PHE B CD2 
7141  C CE1 . PHE B 183 ? 1.2276 1.1690 1.0917 0.0346  0.0382  0.0625  183 PHE B CE1 
7142  C CE2 . PHE B 183 ? 1.2044 1.1835 1.1059 0.0429  0.0336  0.0542  183 PHE B CE2 
7143  C CZ  . PHE B 183 ? 1.2576 1.2108 1.1391 0.0478  0.0390  0.0622  183 PHE B CZ  
7153  N N   . PHE B 184 ? 1.0656 1.1167 0.9945 -0.0212 0.0224  0.0454  184 PHE B N   
7154  C CA  . PHE B 184 ? 1.0506 1.1235 0.9992 -0.0311 0.0244  0.0448  184 PHE B CA  
7155  C C   . PHE B 184 ? 1.0501 1.1123 0.9950 -0.0474 0.0267  0.0503  184 PHE B C   
7156  O O   . PHE B 184 ? 1.1105 1.1486 1.0322 -0.0505 0.0301  0.0547  184 PHE B O   
7157  C CB  . PHE B 184 ? 1.0359 1.1198 0.9839 -0.0260 0.0298  0.0450  184 PHE B CB  
7158  C CG  . PHE B 184 ? 1.0354 1.1371 1.0017 -0.0343 0.0373  0.0461  184 PHE B CG  
7159  C CD1 . PHE B 184 ? 1.0105 1.1349 1.0051 -0.0360 0.0360  0.0434  184 PHE B CD1 
7160  C CD2 . PHE B 184 ? 1.0779 1.1733 1.0341 -0.0395 0.0470  0.0509  184 PHE B CD2 
7161  C CE1 . PHE B 184 ? 1.0354 1.1775 1.0516 -0.0413 0.0450  0.0465  184 PHE B CE1 
7162  C CE2 . PHE B 184 ? 1.0440 1.1567 1.0205 -0.0456 0.0571  0.0533  184 PHE B CE2 
7163  C CZ  . PHE B 184 ? 1.0419 1.1789 1.0503 -0.0458 0.0565  0.0516  184 PHE B CZ  
7173  N N   . ASP B 185 ? 1.0460 1.1263 1.0145 -0.0584 0.0238  0.0512  185 ASP B N   
7174  C CA  . ASP B 185 ? 1.0522 1.1298 1.0244 -0.0768 0.0236  0.0586  185 ASP B CA  
7175  C C   . ASP B 185 ? 1.0695 1.1796 1.0749 -0.0809 0.0292  0.0631  185 ASP B C   
7176  O O   . ASP B 185 ? 1.0462 1.1809 1.0789 -0.0775 0.0269  0.0614  185 ASP B O   
7177  C CB  . ASP B 185 ? 1.0704 1.1383 1.0408 -0.0893 0.0130  0.0591  185 ASP B CB  
7178  C CG  . ASP B 185 ? 1.1454 1.2100 1.1181 -0.1120 0.0096  0.0683  185 ASP B CG  
7179  O OD1 . ASP B 185 ? 1.1579 1.2266 1.1334 -0.1167 0.0171  0.0743  185 ASP B OD1 
7180  O OD2 . ASP B 185 ? 1.1970 1.2541 1.1673 -0.1265 -0.0011 0.0704  185 ASP B OD2 
7185  N N   . SER B 186 ? 1.0766 1.1854 1.0799 -0.0876 0.0382  0.0696  186 SER B N   
7186  C CA  . SER B 186 ? 1.0654 1.2032 1.1005 -0.0899 0.0483  0.0751  186 SER B CA  
7187  C C   . SER B 186 ? 1.0574 1.2173 1.1264 -0.1062 0.0422  0.0851  186 SER B C   
7188  O O   . SER B 186 ? 1.0656 1.2566 1.1723 -0.1039 0.0473  0.0894  186 SER B O   
7189  C CB  . SER B 186 ? 1.0841 1.2114 1.1036 -0.0917 0.0620  0.0792  186 SER B CB  
7190  O OG  . SER B 186 ? 1.1350 1.2353 1.1167 -0.0810 0.0626  0.0732  186 SER B OG  
7196  N N   . ASP B 187 ? 1.0651 1.2083 1.1209 -0.1232 0.0313  0.0899  187 ASP B N   
7197  C CA  . ASP B 187 ? 1.0967 1.2604 1.1827 -0.1422 0.0212  0.1012  187 ASP B CA  
7198  C C   . ASP B 187 ? 1.0790 1.2695 1.1969 -0.1360 0.0138  0.1002  187 ASP B C   
7199  O O   . ASP B 187 ? 1.0676 1.2907 1.2277 -0.1438 0.0111  0.1117  187 ASP B O   
7200  C CB  . ASP B 187 ? 1.1540 1.2858 1.2088 -0.1617 0.0073  0.1032  187 ASP B CB  
7201  C CG  . ASP B 187 ? 1.1445 1.2522 1.1736 -0.1730 0.0137  0.1079  187 ASP B CG  
7202  O OD1 . ASP B 187 ? 1.1493 1.2589 1.1763 -0.1622 0.0288  0.1069  187 ASP B OD1 
7203  O OD2 . ASP B 187 ? 1.1865 1.2699 1.1937 -0.1938 0.0034  0.1125  187 ASP B OD2 
7208  N N   . ASN B 188 ? 1.0579 1.2357 1.1576 -0.1217 0.0104  0.0879  188 ASN B N   
7209  C CA  . ASN B 188 ? 1.0599 1.2556 1.1815 -0.1167 0.0020  0.0857  188 ASN B CA  
7210  C C   . ASN B 188 ? 1.0291 1.2383 1.1612 -0.0950 0.0126  0.0772  188 ASN B C   
7211  O O   . ASN B 188 ? 1.0221 1.2499 1.1780 -0.0900 0.0084  0.0768  188 ASN B O   
7212  C CB  . ASN B 188 ? 1.0310 1.1982 1.1211 -0.1210 -0.0115 0.0788  188 ASN B CB  
7213  C CG  . ASN B 188 ? 1.1574 1.3379 1.2671 -0.1329 -0.0270 0.0845  188 ASN B CG  
7214  O OD1 . ASN B 188 ? 1.2054 1.4129 1.3498 -0.1449 -0.0322 0.0977  188 ASN B OD1 
7215  N ND2 . ASN B 188 ? 1.1914 1.3532 1.2796 -0.1298 -0.0346 0.0761  188 ASN B ND2 
7222  N N   . LEU B 189 ? 1.0298 1.2278 1.1424 -0.0833 0.0254  0.0711  189 LEU B N   
7223  C CA  . LEU B 189 ? 1.0239 1.2249 1.1334 -0.0652 0.0324  0.0614  189 LEU B CA  
7224  C C   . LEU B 189 ? 0.9812 1.1746 1.0807 -0.0598 0.0205  0.0531  189 LEU B C   
7225  O O   . LEU B 189 ? 0.9472 1.1550 1.0635 -0.0523 0.0194  0.0494  189 LEU B O   
7226  C CB  . LEU B 189 ? 1.0300 1.2582 1.1745 -0.0595 0.0438  0.0651  189 LEU B CB  
7227  C CG  . LEU B 189 ? 1.0502 1.2798 1.1944 -0.0553 0.0637  0.0675  189 LEU B CG  
7228  C CD1 . LEU B 189 ? 1.0075 1.2112 1.1098 -0.0471 0.0688  0.0581  189 LEU B CD1 
7229  C CD2 . LEU B 189 ? 1.0625 1.2987 1.2201 -0.0699 0.0674  0.0802  189 LEU B CD2 
7241  N N   . SER B 190 ? 0.9798 1.1483 1.0512 -0.0636 0.0130  0.0507  190 SER B N   
7242  C CA  . SER B 190 ? 0.9707 1.1275 1.0288 -0.0583 0.0046  0.0434  190 SER B CA  
7243  C C   . SER B 190 ? 0.9862 1.1227 1.0158 -0.0467 0.0083  0.0379  190 SER B C   
7244  O O   . SER B 190 ? 1.0166 1.1430 1.0317 -0.0454 0.0147  0.0403  190 SER B O   
7245  C CB  . SER B 190 ? 1.0212 1.1628 1.0704 -0.0733 -0.0062 0.0467  190 SER B CB  
7246  O OG  . SER B 190 ? 1.0138 1.1342 1.0426 -0.0847 -0.0051 0.0519  190 SER B OG  
7252  N N   . MET B 191 ? 0.9303 1.0614 0.9533 -0.0383 0.0039  0.0318  191 MET B N   
7253  C CA  . MET B 191 ? 0.9948 1.1136 0.9993 -0.0255 0.0063  0.0289  191 MET B CA  
7254  C C   . MET B 191 ? 0.9708 1.0763 0.9665 -0.0212 0.0025  0.0256  191 MET B C   
7255  O O   . MET B 191 ? 0.9685 1.0842 0.9768 -0.0219 -0.0019 0.0219  191 MET B O   
7256  C CB  . MET B 191 ? 0.9741 1.1111 0.9874 -0.0155 0.0083  0.0255  191 MET B CB  
7257  C CG  . MET B 191 ? 0.9491 1.0783 0.9470 -0.0042 0.0076  0.0252  191 MET B CG  
7258  S SD  . MET B 191 ? 0.9546 1.1021 0.9582 0.0025  0.0065  0.0210  191 MET B SD  
7259  C CE  . MET B 191 ? 0.9440 1.1063 0.9680 0.0037  0.0010  0.0149  191 MET B CE  
7269  N N   . LYS B 192 ? 0.9962 1.0775 0.9701 -0.0159 0.0059  0.0275  192 LYS B N   
7270  C CA  . LYS B 192 ? 1.0190 1.0840 0.9832 -0.0090 0.0070  0.0255  192 LYS B CA  
7271  C C   . LYS B 192 ? 1.0120 1.0866 0.9816 0.0078  0.0083  0.0265  192 LYS B C   
7272  O O   . LYS B 192 ? 1.0398 1.1023 0.9976 0.0152  0.0119  0.0319  192 LYS B O   
7273  C CB  . LYS B 192 ? 1.0575 1.0845 0.9930 -0.0142 0.0122  0.0284  192 LYS B CB  
7274  C CG  . LYS B 192 ? 1.1053 1.1111 1.0275 -0.0246 0.0112  0.0253  192 LYS B CG  
7275  C CD  . LYS B 192 ? 1.1963 1.1916 1.1142 -0.0113 0.0172  0.0223  192 LYS B CD  
7276  C CE  . LYS B 192 ? 1.2041 1.1663 1.0970 -0.0223 0.0194  0.0191  192 LYS B CE  
7277  N NZ  . LYS B 192 ? 1.2008 1.1644 1.0990 -0.0118 0.0241  0.0152  192 LYS B NZ  
7291  N N   . PRO B 193 ? 0.9845 1.0809 0.9722 0.0133  0.0045  0.0228  193 PRO B N   
7292  C CA  . PRO B 193 ? 1.0289 1.1386 1.0242 0.0263  0.0028  0.0258  193 PRO B CA  
7293  C C   . PRO B 193 ? 1.0733 1.1689 1.0650 0.0378  0.0083  0.0301  193 PRO B C   
7294  O O   . PRO B 193 ? 1.1767 1.2652 1.1698 0.0382  0.0120  0.0269  193 PRO B O   
7295  C CB  . PRO B 193 ? 1.0152 1.1506 1.0296 0.0252  -0.0031 0.0202  193 PRO B CB  
7296  C CG  . PRO B 193 ? 0.9956 1.1303 1.0139 0.0141  -0.0036 0.0149  193 PRO B CG  
7297  C CD  . PRO B 193 ? 1.0156 1.1250 1.0171 0.0068  0.0002  0.0171  193 PRO B CD  
7305  N N   . TYR B 194 ? 1.0930 1.1832 1.0798 0.0475  0.0099  0.0385  194 TYR B N   
7306  C CA  . TYR B 194 ? 1.1337 1.2173 1.1252 0.0625  0.0158  0.0459  194 TYR B CA  
7307  C C   . TYR B 194 ? 1.1669 1.2819 1.1810 0.0707  0.0068  0.0521  194 TYR B C   
7308  O O   . TYR B 194 ? 1.1481 1.2776 1.1619 0.0662  -0.0027 0.0533  194 TYR B O   
7309  C CB  . TYR B 194 ? 1.1543 1.2088 1.1261 0.0685  0.0235  0.0538  194 TYR B CB  
7310  C CG  . TYR B 194 ? 1.2276 1.2706 1.2047 0.0861  0.0335  0.0629  194 TYR B CG  
7311  C CD1 . TYR B 194 ? 1.2529 1.3186 1.2519 0.0999  0.0286  0.0749  194 TYR B CD1 
7312  C CD2 . TYR B 194 ? 1.3038 1.3118 1.2636 0.0885  0.0485  0.0606  194 TYR B CD2 
7313  C CE1 . TYR B 194 ? 1.3104 1.3690 1.3208 0.1179  0.0393  0.0858  194 TYR B CE1 
7314  C CE2 . TYR B 194 ? 1.3465 1.3416 1.3120 0.1066  0.0618  0.0695  194 TYR B CE2 
7315  C CZ  . TYR B 194 ? 1.3723 1.3949 1.3664 0.1224  0.0577  0.0828  194 TYR B CZ  
7316  O OH  . TYR B 194 ? 1.4315 1.4442 1.4372 0.1423  0.0725  0.0942  194 TYR B OH  
7326  N N   . VAL B 195 ? 1.1987 1.3228 1.2311 0.0816  0.0102  0.0568  195 VAL B N   
7327  C CA  . VAL B 195 ? 1.2225 1.3790 1.2798 0.0874  0.0000  0.0646  195 VAL B CA  
7328  C C   . VAL B 195 ? 1.2758 1.4334 1.3513 0.1047  0.0083  0.0776  195 VAL B C   
7329  O O   . VAL B 195 ? 1.3070 1.4581 1.3898 0.1099  0.0201  0.0753  195 VAL B O   
7330  C CB  . VAL B 195 ? 1.1924 1.3716 1.2635 0.0789  -0.0067 0.0557  195 VAL B CB  
7331  C CG1 . VAL B 195 ? 1.2209 1.4316 1.3178 0.0836  -0.0168 0.0651  195 VAL B CG1 
7332  C CG2 . VAL B 195 ? 1.1679 1.3481 1.2249 0.0644  -0.0137 0.0454  195 VAL B CG2 
7342  N N   . TYR B 196 ? 1.3280 1.4931 1.4109 0.1139  0.0029  0.0923  196 TYR B N   
7343  C CA  . TYR B 196 ? 1.3336 1.5099 1.4438 0.1319  0.0080  0.1091  196 TYR B CA  
7344  C C   . TYR B 196 ? 1.3633 1.5830 1.5046 0.1298  -0.0091 0.1175  196 TYR B C   
7345  O O   . TYR B 196 ? 1.3921 1.6257 1.5258 0.1177  -0.0269 0.1163  196 TYR B O   
7346  C CB  . TYR B 196 ? 1.3470 1.5061 1.4487 0.1434  0.0106  0.1232  196 TYR B CB  
7347  C CG  . TYR B 196 ? 1.4232 1.5917 1.5560 0.1652  0.0187  0.1434  196 TYR B CG  
7348  C CD1 . TYR B 196 ? 1.4580 1.6693 1.6313 0.1703  0.0070  0.1577  196 TYR B CD1 
7349  C CD2 . TYR B 196 ? 1.4808 1.6142 1.6026 0.1806  0.0382  0.1499  196 TYR B CD2 
7350  C CE1 . TYR B 196 ? 1.4964 1.7204 1.7045 0.1911  0.0150  0.1787  196 TYR B CE1 
7351  C CE2 . TYR B 196 ? 1.5180 1.6592 1.6712 0.2033  0.0486  0.1702  196 TYR B CE2 
7352  C CZ  . TYR B 196 ? 1.5106 1.6998 1.7100 0.2090  0.0368  0.1853  196 TYR B CZ  
7353  O OH  . TYR B 196 ? 1.5215 1.7219 1.7579 0.2325  0.0478  0.2079  196 TYR B OH  
7363  N N   . VAL B 197 ? 1.4248 1.6636 1.5992 0.1407  -0.0029 0.1265  197 VAL B N   
7364  C CA  . VAL B 197 ? 1.4566 1.7384 1.6661 0.1403  -0.0191 0.1399  197 VAL B CA  
7365  C C   . VAL B 197 ? 1.5156 1.8106 1.7619 0.1618  -0.0098 0.1624  197 VAL B C   
7366  O O   . VAL B 197 ? 1.5317 1.8065 1.7819 0.1759  0.0141  0.1621  197 VAL B O   
7367  C CB  . VAL B 197 ? 1.4421 1.7425 1.6624 0.1288  -0.0222 0.1286  197 VAL B CB  
7368  C CG1 . VAL B 197 ? 1.3910 1.6706 1.5756 0.1121  -0.0238 0.1061  197 VAL B CG1 
7369  C CG2 . VAL B 197 ? 1.5027 1.8019 1.7447 0.1410  -0.0015 0.1301  197 VAL B CG2 
7379  N N   . LYS B 198 ? 1.5349 1.8623 1.8075 0.1640  -0.0284 0.1829  198 LYS B N   
7380  C CA  . LYS B 198 ? 1.5349 1.8772 1.8466 0.1862  -0.0209 0.2084  198 LYS B CA  
7381  C C   . LYS B 198 ? 1.5727 1.9404 1.9281 0.1960  -0.0078 0.2156  198 LYS B C   
7382  O O   . LYS B 198 ? 1.5694 1.9332 1.9504 0.2184  0.0135  0.2297  198 LYS B O   
7383  C CB  . LYS B 198 ? 1.5243 1.8968 1.8531 0.1835  -0.0481 0.2307  198 LYS B CB  
7384  C CG  . LYS B 198 ? 1.5131 1.8600 1.8213 0.1931  -0.0478 0.2404  198 LYS B CG  
7385  C CD  . LYS B 198 ? 1.5753 1.9382 1.8722 0.1782  -0.0794 0.2505  198 LYS B CD  
7386  C CE  . LYS B 198 ? 1.5826 1.9542 1.9018 0.1950  -0.0860 0.2803  198 LYS B CE  
7387  N NZ  . LYS B 198 ? 1.5437 1.9209 1.8401 0.1786  -0.1165 0.2890  198 LYS B NZ  
7401  N N   . GLU B 199 ? 1.6028 1.9949 1.9672 0.1799  -0.0185 0.2067  199 GLU B N   
7402  C CA  . GLU B 199 ? 1.5895 2.0046 1.9932 0.1872  -0.0050 0.2122  199 GLU B CA  
7403  C C   . GLU B 199 ? 1.6057 1.9814 1.9959 0.2022  0.0300  0.2019  199 GLU B C   
7404  O O   . GLU B 199 ? 1.6216 2.0007 2.0436 0.2234  0.0514  0.2175  199 GLU B O   
7405  C CB  . GLU B 199 ? 1.6010 2.0359 2.0023 0.1647  -0.0201 0.1986  199 GLU B CB  
7406  C CG  . GLU B 199 ? 1.6022 2.0703 2.0494 0.1685  -0.0123 0.2081  199 GLU B CG  
7407  C CD  . GLU B 199 ? 1.6305 2.0692 2.0692 0.1786  0.0204  0.1950  199 GLU B CD  
7408  O OE1 . GLU B 199 ? 1.6547 2.0502 2.0461 0.1735  0.0296  0.1730  199 GLU B OE1 
7409  O OE2 . GLU B 199 ? 1.6081 2.0662 2.0869 0.1909  0.0368  0.2076  199 GLU B OE2 
7416  N N   . VAL B 200 ? 1.6168 1.9529 1.9584 0.1907  0.0365  0.1764  200 VAL B N   
7417  C CA  . VAL B 200 ? 1.6374 1.9312 1.9570 0.1993  0.0669  0.1646  200 VAL B CA  
7418  C C   . VAL B 200 ? 1.5929 1.8482 1.8952 0.2170  0.0855  0.1711  200 VAL B C   
7419  O O   . VAL B 200 ? 1.5942 1.8088 1.8755 0.2255  0.1128  0.1638  200 VAL B O   
7420  C CB  . VAL B 200 ? 1.6201 1.8856 1.8942 0.1792  0.0645  0.1375  200 VAL B CB  
7421  C CG1 . VAL B 200 ? 1.6397 1.8672 1.8940 0.1839  0.0926  0.1266  200 VAL B CG1 
7422  C CG2 . VAL B 200 ? 1.6274 1.9268 1.9117 0.1603  0.0425  0.1305  200 VAL B CG2 
7432  N N   . GLY B 201 ? 1.5454 1.8085 1.8519 0.2219  0.0717  0.1847  201 GLY B N   
7433  C CA  . GLY B 201 ? 1.5470 1.7728 1.8375 0.2392  0.0891  0.1925  201 GLY B CA  
7434  C C   . GLY B 201 ? 1.5405 1.7073 1.7733 0.2319  0.1040  0.1710  201 GLY B C   
7435  O O   . GLY B 201 ? 1.5346 1.6601 1.7498 0.2468  0.1271  0.1745  201 GLY B O   
7439  N N   . SER B 202 ? 1.5354 1.6962 1.7382 0.2088  0.0914  0.1497  202 SER B N   
7440  C CA  . SER B 202 ? 1.5155 1.6250 1.6661 0.1983  0.1015  0.1309  202 SER B CA  
7441  C C   . SER B 202 ? 1.4746 1.5945 1.6061 0.1737  0.0795  0.1143  202 SER B C   
7442  O O   . SER B 202 ? 1.4466 1.6061 1.6009 0.1651  0.0623  0.1135  202 SER B O   
7443  C CB  . SER B 202 ? 1.5078 1.5833 1.6432 0.2022  0.1282  0.1221  202 SER B CB  
7444  O OG  . SER B 202 ? 1.5296 1.5635 1.6514 0.2207  0.1541  0.1303  202 SER B OG  
7450  N N   . GLY B 203 ? 1.4260 1.5086 1.5154 0.1622  0.0811  0.1018  203 GLY B N   
7451  C CA  . GLY B 203 ? 1.3820 1.4711 1.4540 0.1408  0.0637  0.0879  203 GLY B CA  
7452  C C   . GLY B 203 ? 1.3474 1.4143 1.3962 0.1270  0.0699  0.0711  203 GLY B C   
7453  O O   . GLY B 203 ? 1.3801 1.4156 1.4142 0.1316  0.0886  0.0685  203 GLY B O   
7457  N N   . VAL B 204 ? 1.3071 1.3891 1.3513 0.1096  0.0542  0.0605  204 VAL B N   
7458  C CA  . VAL B 204 ? 1.2813 1.3497 1.3086 0.0949  0.0551  0.0467  204 VAL B CA  
7459  C C   . VAL B 204 ? 1.2517 1.3184 1.2624 0.0780  0.0426  0.0390  204 VAL B C   
7460  O O   . VAL B 204 ? 1.2247 1.3140 1.2452 0.0763  0.0306  0.0416  204 VAL B O   
7461  C CB  . VAL B 204 ? 1.2476 1.3461 1.2998 0.0932  0.0504  0.0434  204 VAL B CB  
7462  C CG1 . VAL B 204 ? 1.2817 1.3955 1.3621 0.1108  0.0601  0.0551  204 VAL B CG1 
7463  C CG2 . VAL B 204 ? 1.2215 1.3548 1.2884 0.0838  0.0308  0.0406  204 VAL B CG2 
7473  N N   . TYR B 205 ? 1.2366 1.2757 1.2219 0.0649  0.0456  0.0304  205 TYR B N   
7474  C CA  . TYR B 205 ? 1.2043 1.2452 1.1798 0.0480  0.0345  0.0245  205 TYR B CA  
7475  C C   . TYR B 205 ? 1.1927 1.2566 1.1830 0.0391  0.0255  0.0174  205 TYR B C   
7476  O O   . TYR B 205 ? 1.2157 1.2643 1.1956 0.0325  0.0287  0.0124  205 TYR B O   
7477  C CB  . TYR B 205 ? 1.1850 1.1840 1.1260 0.0367  0.0403  0.0221  205 TYR B CB  
7478  C CG  . TYR B 205 ? 1.2476 1.2221 1.1710 0.0429  0.0477  0.0288  205 TYR B CG  
7479  C CD1 . TYR B 205 ? 1.2695 1.2196 1.1843 0.0586  0.0631  0.0345  205 TYR B CD1 
7480  C CD2 . TYR B 205 ? 1.2407 1.2153 1.1567 0.0337  0.0409  0.0303  205 TYR B CD2 
7481  C CE1 . TYR B 205 ? 1.3162 1.2411 1.2140 0.0652  0.0704  0.0414  205 TYR B CE1 
7482  C CE2 . TYR B 205 ? 1.2462 1.1961 1.1439 0.0386  0.0476  0.0366  205 TYR B CE2 
7483  C CZ  . TYR B 205 ? 1.3140 1.2382 1.2019 0.0545  0.0618  0.0421  205 TYR B CZ  
7484  O OH  . TYR B 205 ? 1.3588 1.2561 1.2279 0.0604  0.0689  0.0493  205 TYR B OH  
7494  N N   . GLU B 206 ? 1.1606 1.2575 1.1716 0.0385  0.0149  0.0171  206 GLU B N   
7495  C CA  . GLU B 206 ? 1.1021 1.2202 1.1280 0.0322  0.0075  0.0111  206 GLU B CA  
7496  C C   . GLU B 206 ? 1.0580 1.1698 1.0760 0.0171  0.0023  0.0063  206 GLU B C   
7497  O O   . GLU B 206 ? 1.0308 1.1314 1.0375 0.0103  0.0017  0.0081  206 GLU B O   
7498  C CB  . GLU B 206 ? 1.1784 1.3278 1.2236 0.0357  -0.0009 0.0122  206 GLU B CB  
7499  C CG  . GLU B 206 ? 1.2432 1.4055 1.3012 0.0483  -0.0002 0.0197  206 GLU B CG  
7500  C CD  . GLU B 206 ? 1.3082 1.4983 1.3856 0.0477  -0.0082 0.0183  206 GLU B CD  
7501  O OE1 . GLU B 206 ? 1.2316 1.4344 1.3096 0.0419  -0.0166 0.0157  206 GLU B OE1 
7502  O OE2 . GLU B 206 ? 1.2577 1.4543 1.3477 0.0525  -0.0049 0.0199  206 GLU B OE2 
7509  N N   . ASN B 207 ? 1.0663 1.1867 1.0924 0.0114  -0.0021 0.0017  207 ASN B N   
7510  C CA  . ASN B 207 ? 1.0141 1.1359 1.0407 -0.0020 -0.0093 -0.0002 207 ASN B CA  
7511  C C   . ASN B 207 ? 0.9763 1.1219 1.0197 -0.0026 -0.0141 0.0005  207 ASN B C   
7512  O O   . ASN B 207 ? 0.9666 1.1149 1.0140 -0.0120 -0.0178 0.0021  207 ASN B O   
7513  C CB  . ASN B 207 ? 1.0066 1.1305 1.0374 -0.0068 -0.0128 -0.0041 207 ASN B CB  
7514  C CG  . ASN B 207 ? 1.0662 1.1580 1.0721 -0.0119 -0.0078 -0.0050 207 ASN B CG  
7515  O OD1 . ASN B 207 ? 1.0703 1.1357 1.0537 -0.0173 -0.0043 -0.0030 207 ASN B OD1 
7516  N ND2 . ASN B 207 ? 1.0611 1.1515 1.0674 -0.0114 -0.0064 -0.0082 207 ASN B ND2 
7523  N N   . SER B 208 ? 0.9643 1.1260 1.0168 0.0066  -0.0135 0.0002  208 SER B N   
7524  C CA  . SER B 208 ? 0.9208 1.0983 0.9818 0.0065  -0.0152 0.0002  208 SER B CA  
7525  C C   . SER B 208 ? 0.9517 1.1385 1.0131 0.0151  -0.0159 0.0009  208 SER B C   
7526  O O   . SER B 208 ? 0.9689 1.1596 1.0343 0.0204  -0.0170 0.0012  208 SER B O   
7527  C CB  . SER B 208 ? 0.8781 1.0686 0.9536 0.0018  -0.0184 -0.0032 208 SER B CB  
7528  O OG  . SER B 208 ? 0.8778 1.0791 0.9599 0.0061  -0.0206 -0.0072 208 SER B OG  
7534  N N   . CYS B 209 ? 0.9462 1.1363 1.0028 0.0153  -0.0153 0.0024  209 CYS B N   
7535  C CA  . CYS B 209 ? 0.9024 1.0989 0.9546 0.0204  -0.0186 0.0048  209 CYS B CA  
7536  C C   . CYS B 209 ? 0.9385 1.1389 0.9853 0.0163  -0.0180 0.0017  209 CYS B C   
7537  O O   . CYS B 209 ? 0.9448 1.1378 0.9818 0.0143  -0.0131 0.0035  209 CYS B O   
7538  C CB  . CYS B 209 ? 0.9289 1.1150 0.9703 0.0255  -0.0172 0.0122  209 CYS B CB  
7539  S SG  . CYS B 209 ? 0.9844 1.1804 1.0235 0.0316  -0.0252 0.0193  209 CYS B SG  
7545  N N   . ALA B 210 ? 0.9365 1.1453 0.9870 0.0149  -0.0215 -0.0029 210 ALA B N   
7546  C CA  . ALA B 210 ? 0.8936 1.0997 0.9341 0.0112  -0.0181 -0.0068 210 ALA B CA  
7547  C C   . ALA B 210 ? 0.9287 1.1275 0.9477 0.0103  -0.0200 -0.0032 210 ALA B C   
7548  O O   . ALA B 210 ? 0.9084 1.0970 0.9136 0.0077  -0.0122 -0.0042 210 ALA B O   
7549  C CB  . ALA B 210 ? 0.8429 1.0543 0.8869 0.0089  -0.0215 -0.0126 210 ALA B CB  
7555  N N   . SER B 211 ? 0.9411 1.1448 0.9575 0.0122  -0.0301 0.0023  211 SER B N   
7556  C CA  . SER B 211 ? 0.9363 1.1331 0.9312 0.0101  -0.0351 0.0078  211 SER B CA  
7557  C C   . SER B 211 ? 0.9722 1.1576 0.9582 0.0126  -0.0285 0.0125  211 SER B C   
7558  O O   . SER B 211 ? 0.9751 1.1479 0.9383 0.0085  -0.0256 0.0133  211 SER B O   
7559  C CB  . SER B 211 ? 0.9137 1.1230 0.9153 0.0123  -0.0489 0.0162  211 SER B CB  
7560  O OG  . SER B 211 ? 0.9314 1.1449 0.9485 0.0215  -0.0477 0.0236  211 SER B OG  
7566  N N   . GLY B 212 ? 0.9732 1.1594 0.9732 0.0180  -0.0253 0.0155  212 GLY B N   
7567  C CA  . GLY B 212 ? 0.9671 1.1401 0.9574 0.0188  -0.0188 0.0198  212 GLY B CA  
7568  C C   . GLY B 212 ? 0.9436 1.1102 0.9302 0.0129  -0.0079 0.0151  212 GLY B C   
7569  O O   . GLY B 212 ? 0.9610 1.1160 0.9346 0.0110  -0.0022 0.0188  212 GLY B O   
7573  N N   . THR B 213 ? 0.9399 1.1145 0.9400 0.0104  -0.0042 0.0084  213 THR B N   
7574  C CA  . THR B 213 ? 0.9566 1.1291 0.9596 0.0063  0.0074  0.0063  213 THR B CA  
7575  C C   . THR B 213 ? 0.9643 1.1267 0.9450 0.0039  0.0139  0.0044  213 THR B C   
7576  O O   . THR B 213 ? 0.9799 1.1353 0.9553 0.0015  0.0259  0.0059  213 THR B O   
7577  C CB  . THR B 213 ? 0.9371 1.1212 0.9631 0.0057  0.0092  0.0018  213 THR B CB  
7578  O OG1 . THR B 213 ? 0.8662 1.0557 0.9049 0.0069  0.0011  0.0024  213 THR B OG1 
7579  C CG2 . THR B 213 ? 0.9137 1.1010 0.9538 0.0023  0.0201  0.0041  213 THR B CG2 
7587  N N   . THR B 214 ? 0.9693 1.1291 0.9351 0.0034  0.0067  0.0016  214 THR B N   
7588  C CA  . THR B 214 ? 0.9845 1.1273 0.9191 -0.0012 0.0115  0.0000  214 THR B CA  
7589  C C   . THR B 214 ? 1.0021 1.1330 0.9148 -0.0026 0.0096  0.0072  214 THR B C   
7590  O O   . THR B 214 ? 1.0278 1.1420 0.9174 -0.0064 0.0205  0.0071  214 THR B O   
7591  C CB  . THR B 214 ? 0.9805 1.1212 0.9006 -0.0047 0.0009  -0.0037 214 THR B CB  
7592  O OG1 . THR B 214 ? 0.9575 1.1078 0.8803 -0.0036 -0.0165 0.0032  214 THR B OG1 
7593  C CG2 . THR B 214 ? 0.9367 1.0869 0.8771 -0.0033 0.0031  -0.0107 214 THR B CG2 
7601  N N   . ALA B 215 ? 0.9958 1.1332 0.9147 0.0012  -0.0028 0.0142  215 ALA B N   
7602  C CA  . ALA B 215 ? 1.0516 1.1771 0.9531 0.0014  -0.0041 0.0226  215 ALA B CA  
7603  C C   . ALA B 215 ? 1.0405 1.1587 0.9443 -0.0001 0.0111  0.0227  215 ALA B C   
7604  O O   . ALA B 215 ? 1.0851 1.1872 0.9651 -0.0042 0.0187  0.0250  215 ALA B O   
7605  C CB  . ALA B 215 ? 0.9938 1.1277 0.9086 0.0085  -0.0162 0.0308  215 ALA B CB  
7611  N N   . LEU B 216 ? 1.0101 1.1394 0.9415 0.0018  0.0150  0.0212  216 LEU B N   
7612  C CA  . LEU B 216 ? 1.0190 1.1460 0.9581 -0.0022 0.0280  0.0224  216 LEU B CA  
7613  C C   . LEU B 216 ? 1.0363 1.1596 0.9688 -0.0057 0.0427  0.0186  216 LEU B C   
7614  O O   . LEU B 216 ? 1.0877 1.2007 1.0088 -0.0095 0.0544  0.0219  216 LEU B O   
7615  C CB  . LEU B 216 ? 1.0399 1.1806 1.0091 -0.0022 0.0266  0.0214  216 LEU B CB  
7616  C CG  . LEU B 216 ? 1.0482 1.1895 1.0303 -0.0085 0.0338  0.0256  216 LEU B CG  
7617  C CD1 . LEU B 216 ? 1.1032 1.2494 1.0926 -0.0124 0.0485  0.0261  216 LEU B CD1 
7618  C CD2 . LEU B 216 ? 1.0811 1.2052 1.0450 -0.0104 0.0325  0.0319  216 LEU B CD2 
7630  N N   . GLY B 217 ? 1.0251 1.1541 0.9630 -0.0043 0.0440  0.0120  217 GLY B N   
7631  C CA  . GLY B 217 ? 1.0680 1.1894 0.9985 -0.0058 0.0613  0.0083  217 GLY B CA  
7632  C C   . GLY B 217 ? 1.1112 1.2077 1.0000 -0.0099 0.0675  0.0087  217 GLY B C   
7633  O O   . GLY B 217 ? 1.1269 1.2133 1.0080 -0.0122 0.0855  0.0104  217 GLY B O   
7637  N N   . TYR B 218 ? 1.1008 1.1870 0.9621 -0.0118 0.0526  0.0084  218 TYR B N   
7638  C CA  . TYR B 218 ? 1.1353 1.1952 0.9518 -0.0179 0.0547  0.0101  218 TYR B CA  
7639  C C   . TYR B 218 ? 1.1875 1.2399 0.9974 -0.0193 0.0611  0.0176  218 TYR B C   
7640  O O   . TYR B 218 ? 1.2217 1.2538 1.0056 -0.0238 0.0769  0.0178  218 TYR B O   
7641  C CB  . TYR B 218 ? 1.1401 1.1963 0.9354 -0.0208 0.0320  0.0127  218 TYR B CB  
7642  C CG  . TYR B 218 ? 1.1172 1.1736 0.9066 -0.0236 0.0253  0.0056  218 TYR B CG  
7643  C CD1 . TYR B 218 ? 1.1350 1.1690 0.8974 -0.0289 0.0401  -0.0026 218 TYR B CD1 
7644  C CD2 . TYR B 218 ? 1.0854 1.1617 0.8946 -0.0214 0.0057  0.0075  218 TYR B CD2 
7645  C CE1 . TYR B 218 ? 1.1050 1.1347 0.8579 -0.0329 0.0340  -0.0093 218 TYR B CE1 
7646  C CE2 . TYR B 218 ? 1.0864 1.1626 0.8898 -0.0258 -0.0011 0.0017  218 TYR B CE2 
7647  C CZ  . TYR B 218 ? 1.1167 1.1685 0.8906 -0.0322 0.0123  -0.0070 218 TYR B CZ  
7648  O OH  . TYR B 218 ? 1.1706 1.2181 0.9349 -0.0378 0.0056  -0.0131 218 TYR B OH  
7658  N N   . TYR B 219 ? 1.1471 1.2124 0.9774 -0.0157 0.0502  0.0239  219 TYR B N   
7659  C CA  . TYR B 219 ? 1.1749 1.2301 0.9964 -0.0177 0.0545  0.0315  219 TYR B CA  
7660  C C   . TYR B 219 ? 1.1928 1.2499 1.0286 -0.0208 0.0758  0.0313  219 TYR B C   
7661  O O   . TYR B 219 ? 1.2446 1.2856 1.0603 -0.0256 0.0868  0.0355  219 TYR B O   
7662  C CB  . TYR B 219 ? 1.1991 1.2644 1.0395 -0.0126 0.0404  0.0373  219 TYR B CB  
7663  C CG  . TYR B 219 ? 1.2442 1.2998 1.0823 -0.0147 0.0455  0.0444  219 TYR B CG  
7664  C CD1 . TYR B 219 ? 1.2425 1.3077 1.1065 -0.0176 0.0541  0.0443  219 TYR B CD1 
7665  C CD2 . TYR B 219 ? 1.2785 1.3148 1.0881 -0.0148 0.0400  0.0523  219 TYR B CD2 
7666  C CE1 . TYR B 219 ? 1.2646 1.3184 1.1237 -0.0220 0.0578  0.0509  219 TYR B CE1 
7667  C CE2 . TYR B 219 ? 1.3161 1.3401 1.1210 -0.0172 0.0451  0.0587  219 TYR B CE2 
7668  C CZ  . TYR B 219 ? 1.2941 1.3262 1.1228 -0.0215 0.0542  0.0575  219 TYR B CZ  
7669  O OH  . TYR B 219 ? 1.3141 1.3314 1.1354 -0.0264 0.0585  0.0639  219 TYR B OH  
7679  N N   . LEU B 220 ? 1.2098 1.2875 1.0819 -0.0186 0.0816  0.0278  220 LEU B N   
7680  C CA  . LEU B 220 ? 1.2115 1.2968 1.1050 -0.0216 0.1007  0.0305  220 LEU B CA  
7681  C C   . LEU B 220 ? 1.1982 1.2700 1.0745 -0.0221 0.1224  0.0271  220 LEU B C   
7682  O O   . LEU B 220 ? 1.2118 1.2840 1.0971 -0.0249 0.1418  0.0316  220 LEU B O   
7683  C CB  . LEU B 220 ? 1.1364 1.2490 1.0759 -0.0195 0.0984  0.0303  220 LEU B CB  
7684  C CG  . LEU B 220 ? 1.1046 1.2274 1.0632 -0.0223 0.0847  0.0353  220 LEU B CG  
7685  C CD1 . LEU B 220 ? 1.0983 1.2461 1.0998 -0.0237 0.0855  0.0371  220 LEU B CD1 
7686  C CD2 . LEU B 220 ? 1.0793 1.1900 1.0252 -0.0293 0.0879  0.0428  220 LEU B CD2 
7698  N N   . LYS B 221 ? 1.2408 1.2991 1.0920 -0.0202 0.1206  0.0196  221 LYS B N   
7699  C CA  . LYS B 221 ? 1.2607 1.2968 1.0855 -0.0214 0.1431  0.0153  221 LYS B CA  
7700  C C   . LYS B 221 ? 1.3036 1.3097 1.0816 -0.0283 0.1497  0.0184  221 LYS B C   
7701  O O   . LYS B 221 ? 1.3476 1.3382 1.1127 -0.0302 0.1751  0.0189  221 LYS B O   
7702  C CB  . LYS B 221 ? 1.2305 1.2555 1.0356 -0.0199 0.1378  0.0061  221 LYS B CB  
7703  C CG  . LYS B 221 ? 1.2684 1.2609 1.0360 -0.0219 0.1621  0.0001  221 LYS B CG  
7704  C CD  . LYS B 221 ? 1.2838 1.2840 1.0818 -0.0162 0.1930  0.0027  221 LYS B CD  
7705  C CE  . LYS B 221 ? 1.3800 1.3430 1.1384 -0.0164 0.2218  -0.0035 221 LYS B CE  
7706  N NZ  . LYS B 221 ? 1.3883 1.3262 1.1081 -0.0191 0.2131  -0.0139 221 LYS B NZ  
7720  N N   . LYS B 222 ? 1.3035 1.3008 1.0565 -0.0318 0.1281  0.0216  222 LYS B N   
7721  C CA  . LYS B 222 ? 1.3430 1.3107 1.0496 -0.0389 0.1312  0.0260  222 LYS B CA  
7722  C C   . LYS B 222 ? 1.3544 1.3276 1.0763 -0.0407 0.1394  0.0345  222 LYS B C   
7723  O O   . LYS B 222 ? 1.3961 1.3475 1.0910 -0.0463 0.1570  0.0372  222 LYS B O   
7724  C CB  . LYS B 222 ? 1.3517 1.3094 1.0285 -0.0415 0.1036  0.0288  222 LYS B CB  
7725  C CG  . LYS B 222 ? 1.4650 1.3864 1.0834 -0.0505 0.1039  0.0327  222 LYS B CG  
7726  C CD  . LYS B 222 ? 1.5273 1.4201 1.1005 -0.0577 0.1094  0.0249  222 LYS B CD  
7727  C CE  . LYS B 222 ? 1.5828 1.4398 1.0934 -0.0690 0.0988  0.0303  222 LYS B CE  
7728  N NZ  . LYS B 222 ? 1.6001 1.4533 1.0887 -0.0747 0.0712  0.0306  222 LYS B NZ  
7742  N N   . CYS B 223 ? 1.3401 1.3390 1.1018 -0.0374 0.1278  0.0386  223 CYS B N   
7743  C CA  . CYS B 223 ? 1.3601 1.3606 1.1314 -0.0413 0.1310  0.0471  223 CYS B CA  
7744  C C   . CYS B 223 ? 1.3471 1.3678 1.1587 -0.0435 0.1502  0.0498  223 CYS B C   
7745  O O   . CYS B 223 ? 1.3304 1.3526 1.1506 -0.0495 0.1538  0.0574  223 CYS B O   
7746  C CB  . CYS B 223 ? 1.3167 1.3268 1.1018 -0.0383 0.1079  0.0510  223 CYS B CB  
7747  S SG  . CYS B 223 ? 1.4684 1.4563 1.2118 -0.0360 0.0864  0.0552  223 CYS B SG  
7753  N N   . LYS B 224 ? 1.3681 1.4046 1.2057 -0.0391 0.1619  0.0452  224 LYS B N   
7754  C CA  . LYS B 224 ? 1.3272 1.3882 1.2106 -0.0404 0.1784  0.0508  224 LYS B CA  
7755  C C   . LYS B 224 ? 1.3088 1.3735 1.2046 -0.0345 0.2017  0.0472  224 LYS B C   
7756  O O   . LYS B 224 ? 1.2597 1.3475 1.1984 -0.0341 0.2174  0.0541  224 LYS B O   
7757  C CB  . LYS B 224 ? 1.2469 1.3374 1.1739 -0.0404 0.1600  0.0536  224 LYS B CB  
7758  C CG  . LYS B 224 ? 1.2355 1.3268 1.1669 -0.0495 0.1506  0.0619  224 LYS B CG  
7759  C CD  . LYS B 224 ? 1.2564 1.3709 1.2243 -0.0517 0.1338  0.0642  224 LYS B CD  
7760  C CE  . LYS B 224 ? 1.2477 1.3847 1.2554 -0.0619 0.1417  0.0750  224 LYS B CE  
7761  N NZ  . LYS B 224 ? 1.1892 1.3541 1.2389 -0.0624 0.1301  0.0768  224 LYS B NZ  
7775  N N   . ASN B 225 ? 1.4238 1.4654 1.2837 -0.0304 0.2050  0.0379  225 ASN B N   
7776  C CA  . ASN B 225 ? 1.4492 1.4877 1.3157 -0.0236 0.2275  0.0330  225 ASN B CA  
7777  C C   . ASN B 225 ? 1.4114 1.4867 1.3370 -0.0167 0.2237  0.0351  225 ASN B C   
7778  O O   . ASN B 225 ? 1.3742 1.4689 1.3406 -0.0129 0.2439  0.0420  225 ASN B O   
7779  C CB  . ASN B 225 ? 1.4982 1.5231 1.3579 -0.0247 0.2624  0.0376  225 ASN B CB  
7780  C CG  . ASN B 225 ? 1.5665 1.5833 1.4313 -0.0156 0.2901  0.0331  225 ASN B CG  
7781  O OD1 . ASN B 225 ? 1.5499 1.5605 1.4062 -0.0105 0.2823  0.0243  225 ASN B OD1 
7782  N ND2 . ASN B 225 ? 1.5013 1.5173 1.3805 -0.0133 0.3239  0.0398  225 ASN B ND2 
7789  N N   . LEU B 226 ? 1.3232 1.4084 1.2541 -0.0151 0.1973  0.0303  226 LEU B N   
7790  C CA  . LEU B 226 ? 1.2504 1.3658 1.2294 -0.0095 0.1896  0.0313  226 LEU B CA  
7791  C C   . LEU B 226 ? 1.2104 1.3136 1.1692 -0.0043 0.1811  0.0201  226 LEU B C   
7792  O O   . LEU B 226 ? 1.1910 1.2874 1.1269 -0.0068 0.1584  0.0153  226 LEU B O   
7793  C CB  . LEU B 226 ? 1.2071 1.3458 1.2130 -0.0145 0.1657  0.0371  226 LEU B CB  
7794  C CG  . LEU B 226 ? 1.1782 1.3501 1.2380 -0.0124 0.1599  0.0424  226 LEU B CG  
7795  C CD1 . LEU B 226 ? 1.1523 1.3437 1.2525 -0.0117 0.1824  0.0535  226 LEU B CD1 
7796  C CD2 . LEU B 226 ? 1.1080 1.2917 1.1790 -0.0197 0.1354  0.0462  226 LEU B CD2 
7808  N N   . ASP B 227 ? 1.1898 1.2901 1.1581 0.0031  0.2002  0.0171  227 ASP B N   
7809  C CA  . ASP B 227 ? 1.2152 1.2978 1.1583 0.0063  0.1952  0.0062  227 ASP B CA  
7810  C C   . ASP B 227 ? 1.1983 1.3067 1.1764 0.0099  0.1753  0.0053  227 ASP B C   
7811  O O   . ASP B 227 ? 1.1933 1.2905 1.1495 0.0096  0.1622  -0.0032 227 ASP B O   
7812  C CB  . ASP B 227 ? 1.3756 1.4355 1.3063 0.0128  0.2269  0.0025  227 ASP B CB  
7813  C CG  . ASP B 227 ? 1.3937 1.4782 1.3782 0.0209  0.2508  0.0134  227 ASP B CG  
7814  O OD1 . ASP B 227 ? 1.3911 1.4720 1.3903 0.0308  0.2705  0.0125  227 ASP B OD1 
7815  O OD2 . ASP B 227 ? 1.3087 1.4160 1.3215 0.0171  0.2498  0.0240  227 ASP B OD2 
7820  N N   . ARG B 228 ? 1.1366 1.2781 1.1667 0.0119  0.1722  0.0145  228 ARG B N   
7821  C CA  . ARG B 228 ? 1.1097 1.2729 1.1700 0.0142  0.1537  0.0142  228 ARG B CA  
7822  C C   . ARG B 228 ? 1.0611 1.2553 1.1652 0.0101  0.1437  0.0257  228 ARG B C   
7823  O O   . ARG B 228 ? 1.0881 1.2944 1.2164 0.0088  0.1578  0.0358  228 ARG B O   
7824  C CB  . ARG B 228 ? 1.1119 1.2745 1.1880 0.0235  0.1676  0.0118  228 ARG B CB  
7825  C CG  . ARG B 228 ? 1.0962 1.2790 1.2192 0.0300  0.1889  0.0237  228 ARG B CG  
7826  C CD  . ARG B 228 ? 1.1093 1.2849 1.2425 0.0415  0.2059  0.0213  228 ARG B CD  
7827  N NE  . ARG B 228 ? 1.0554 1.2448 1.2072 0.0431  0.1855  0.0195  228 ARG B NE  
7828  C CZ  . ARG B 228 ? 1.0810 1.2677 1.2471 0.0527  0.1950  0.0187  228 ARG B CZ  
7829  N NH1 . ARG B 228 ? 1.0796 1.2493 1.2445 0.0630  0.2260  0.0196  228 ARG B NH1 
7830  N NH2 . ARG B 228 ? 1.0948 1.2933 1.2751 0.0525  0.1746  0.0173  228 ARG B NH2 
7844  N N   . ALA B 229 ? 0.9904 1.1959 1.1029 0.0069  0.1198  0.0246  229 ALA B N   
7845  C CA  . ALA B 229 ? 0.9869 1.2152 1.1319 0.0001  0.1074  0.0346  229 ALA B CA  
7846  C C   . ALA B 229 ? 0.9233 1.1580 1.0737 -0.0009 0.0856  0.0309  229 ALA B C   
7847  O O   . ALA B 229 ? 0.9076 1.1290 1.0329 0.0023  0.0779  0.0210  229 ALA B O   
7848  C CB  . ALA B 229 ? 0.9913 1.2121 1.1187 -0.0087 0.1034  0.0382  229 ALA B CB  
7854  N N   . LYS B 230 ? 0.9081 1.1627 1.0909 -0.0068 0.0755  0.0399  230 LYS B N   
7855  C CA  . LYS B 230 ? 0.8689 1.1276 1.0558 -0.0098 0.0556  0.0378  230 LYS B CA  
7856  C C   . LYS B 230 ? 0.8257 1.0743 0.9930 -0.0192 0.0420  0.0380  230 LYS B C   
7857  O O   . LYS B 230 ? 0.8229 1.0769 1.0007 -0.0291 0.0399  0.0471  230 LYS B O   
7858  C CB  . LYS B 230 ? 0.8112 1.0935 1.0405 -0.0121 0.0516  0.0483  230 LYS B CB  
7859  C CG  . LYS B 230 ? 0.8419 1.1270 1.0812 -0.0026 0.0530  0.0439  230 LYS B CG  
7860  C CD  . LYS B 230 ? 0.9184 1.2285 1.2048 -0.0016 0.0551  0.0576  230 LYS B CD  
7861  C CE  . LYS B 230 ? 0.9321 1.2403 1.2261 0.0109  0.0631  0.0533  230 LYS B CE  
7862  N NZ  . LYS B 230 ? 0.9141 1.2472 1.2577 0.0148  0.0670  0.0688  230 LYS B NZ  
7876  N N   . ILE B 231 ? 0.8314 1.0645 0.9708 -0.0164 0.0334  0.0288  231 ILE B N   
7877  C CA  . ILE B 231 ? 0.8773 1.0950 0.9933 -0.0215 0.0250  0.0284  231 ILE B CA  
7878  C C   . ILE B 231 ? 0.8741 1.0904 0.9929 -0.0265 0.0107  0.0281  231 ILE B C   
7879  O O   . ILE B 231 ? 0.8378 1.0517 0.9509 -0.0209 0.0054  0.0214  231 ILE B O   
7880  C CB  . ILE B 231 ? 0.9041 1.1059 0.9894 -0.0141 0.0261  0.0212  231 ILE B CB  
7881  C CG1 . ILE B 231 ? 0.9528 1.1489 1.0260 -0.0123 0.0395  0.0221  231 ILE B CG1 
7882  C CG2 . ILE B 231 ? 0.8960 1.0822 0.9615 -0.0162 0.0174  0.0216  231 ILE B CG2 
7883  C CD1 . ILE B 231 ? 0.9640 1.1608 1.0436 -0.0201 0.0467  0.0307  231 ILE B CD1 
7895  N N   . VAL B 232 ? 0.8962 1.1121 1.0213 -0.0386 0.0048  0.0358  232 VAL B N   
7896  C CA  . VAL B 232 ? 0.8769 1.0843 0.9964 -0.0463 -0.0082 0.0358  232 VAL B CA  
7897  C C   . VAL B 232 ? 0.8831 1.0662 0.9705 -0.0417 -0.0098 0.0287  232 VAL B C   
7898  O O   . VAL B 232 ? 0.9299 1.0999 0.9988 -0.0389 -0.0043 0.0284  232 VAL B O   
7899  C CB  . VAL B 232 ? 0.9095 1.1172 1.0365 -0.0636 -0.0151 0.0465  232 VAL B CB  
7900  C CG1 . VAL B 232 ? 0.9473 1.1287 1.0467 -0.0736 -0.0256 0.0447  232 VAL B CG1 
7901  C CG2 . VAL B 232 ? 0.9069 1.1421 1.0725 -0.0685 -0.0193 0.0557  232 VAL B CG2 
7911  N N   . GLN B 233 ? 0.9027 1.0794 0.9844 -0.0404 -0.0163 0.0240  233 GLN B N   
7912  C CA  . GLN B 233 ? 0.9351 1.0911 0.9919 -0.0340 -0.0155 0.0187  233 GLN B CA  
7913  C C   . GLN B 233 ? 0.9355 1.0733 0.9793 -0.0428 -0.0221 0.0183  233 GLN B C   
7914  O O   . GLN B 233 ? 0.9303 1.0738 0.9846 -0.0545 -0.0299 0.0222  233 GLN B O   
7915  C CB  . GLN B 233 ? 0.9059 1.0728 0.9675 -0.0204 -0.0131 0.0125  233 GLN B CB  
7916  C CG  . GLN B 233 ? 0.9475 1.1282 1.0169 -0.0150 -0.0071 0.0126  233 GLN B CG  
7917  C CD  . GLN B 233 ? 0.8895 1.0719 0.9511 -0.0043 -0.0059 0.0081  233 GLN B CD  
7918  O OE1 . GLN B 233 ? 0.9208 1.0941 0.9711 0.0007  -0.0078 0.0078  233 GLN B OE1 
7919  N NE2 . GLN B 233 ? 0.8203 1.0134 0.8875 -0.0013 -0.0024 0.0057  233 GLN B NE2 
7928  N N   . PRO B 234 ? 0.9624 1.0766 0.9827 -0.0380 -0.0186 0.0148  234 PRO B N   
7929  C CA  . PRO B 234 ? 1.0157 1.1030 1.0143 -0.0485 -0.0219 0.0143  234 PRO B CA  
7930  C C   . PRO B 234 ? 0.9970 1.0937 1.0066 -0.0555 -0.0307 0.0135  234 PRO B C   
7931  O O   . PRO B 234 ? 1.0285 1.1148 1.0305 -0.0722 -0.0395 0.0178  234 PRO B O   
7932  C CB  . PRO B 234 ? 1.0297 1.0958 1.0087 -0.0358 -0.0123 0.0103  234 PRO B CB  
7933  C CG  . PRO B 234 ? 1.0387 1.1142 1.0232 -0.0238 -0.0064 0.0122  234 PRO B CG  
7934  C CD  . PRO B 234 ? 0.9512 1.0602 0.9628 -0.0233 -0.0110 0.0126  234 PRO B CD  
7942  N N   . ASN B 235 ? 0.9746 1.0896 1.0006 -0.0447 -0.0298 0.0089  235 ASN B N   
7943  C CA  . ASN B 235 ? 0.9936 1.1143 1.0273 -0.0501 -0.0374 0.0080  235 ASN B CA  
7944  C C   . ASN B 235 ? 0.9395 1.0926 1.0050 -0.0433 -0.0394 0.0079  235 ASN B C   
7945  O O   . ASN B 235 ? 0.9266 1.0864 0.9993 -0.0402 -0.0416 0.0045  235 ASN B O   
7946  C CB  . ASN B 235 ? 1.0227 1.1249 1.0383 -0.0450 -0.0325 0.0020  235 ASN B CB  
7947  C CG  . ASN B 235 ? 1.0996 1.1720 1.0886 -0.0601 -0.0374 0.0027  235 ASN B CG  
7948  O OD1 . ASN B 235 ? 1.0625 1.1398 1.0572 -0.0737 -0.0496 0.0074  235 ASN B OD1 
7949  N ND2 . ASN B 235 ? 1.1351 1.1750 1.0940 -0.0581 -0.0276 -0.0009 235 ASN B ND2 
7956  N N   . GLY B 236 ? 0.9357 1.1061 1.0181 -0.0411 -0.0370 0.0115  236 GLY B N   
7957  C CA  . GLY B 236 ? 0.8623 1.0574 0.9707 -0.0344 -0.0356 0.0114  236 GLY B CA  
7958  C C   . GLY B 236 ? 0.8765 1.0833 0.9968 -0.0327 -0.0292 0.0157  236 GLY B C   
7959  O O   . GLY B 236 ? 0.8999 1.0990 1.0125 -0.0396 -0.0287 0.0204  236 GLY B O   
7963  N N   . TRP B 237 ? 0.8751 1.0975 1.0114 -0.0242 -0.0230 0.0140  237 TRP B N   
7964  C CA  . TRP B 237 ? 0.8319 1.0622 0.9758 -0.0211 -0.0132 0.0170  237 TRP B CA  
7965  C C   . TRP B 237 ? 0.8323 1.0671 0.9769 -0.0104 -0.0048 0.0106  237 TRP B C   
7966  O O   . TRP B 237 ? 0.8301 1.0689 0.9819 -0.0070 -0.0068 0.0072  237 TRP B O   
7967  C CB  . TRP B 237 ? 0.8233 1.0688 0.9944 -0.0284 -0.0134 0.0281  237 TRP B CB  
7968  C CG  . TRP B 237 ? 0.8058 1.0672 1.0040 -0.0254 -0.0145 0.0315  237 TRP B CG  
7969  C CD1 . TRP B 237 ? 0.7928 1.0583 1.0023 -0.0324 -0.0269 0.0365  237 TRP B CD1 
7970  C CD2 . TRP B 237 ? 0.8260 1.0974 1.0405 -0.0147 -0.0019 0.0308  237 TRP B CD2 
7971  N NE1 . TRP B 237 ? 0.7691 1.0493 1.0047 -0.0256 -0.0237 0.0399  237 TRP B NE1 
7972  C CE2 . TRP B 237 ? 0.7761 1.0590 1.0149 -0.0141 -0.0072 0.0361  237 TRP B CE2 
7973  C CE3 . TRP B 237 ? 0.7897 1.0576 0.9969 -0.0059 0.0138  0.0262  237 TRP B CE3 
7974  C CZ2 . TRP B 237 ? 0.7706 1.0613 1.0285 -0.0034 0.0045  0.0371  237 TRP B CZ2 
7975  C CZ3 . TRP B 237 ? 0.7965 1.0695 1.0185 0.0033  0.0259  0.0261  237 TRP B CZ3 
7976  C CH2 . TRP B 237 ? 0.7910 1.0752 1.0391 0.0053  0.0220  0.0316  237 TRP B CH2 
7987  N N   . LEU B 238 ? 0.8402 1.0708 0.9732 -0.0065 0.0043  0.0092  238 LEU B N   
7988  C CA  . LEU B 238 ? 0.8075 1.0357 0.9322 0.0008  0.0125  0.0031  238 LEU B CA  
7989  C C   . LEU B 238 ? 0.8644 1.0924 0.9904 0.0021  0.0268  0.0066  238 LEU B C   
7990  O O   . LEU B 238 ? 0.8686 1.0940 0.9899 -0.0019 0.0288  0.0113  238 LEU B O   
7991  C CB  . LEU B 238 ? 0.8113 1.0288 0.9103 0.0034  0.0077  -0.0030 238 LEU B CB  
7992  C CG  . LEU B 238 ? 0.8108 1.0284 0.9086 0.0034  -0.0033 -0.0059 238 LEU B CG  
7993  C CD1 . LEU B 238 ? 0.8179 1.0292 0.8970 0.0062  -0.0074 -0.0074 238 LEU B CD1 
7994  C CD2 . LEU B 238 ? 0.7890 1.0116 0.8959 0.0050  -0.0047 -0.0104 238 LEU B CD2 
8006  N N   . GLU B 239 ? 0.8748 1.1025 1.0052 0.0075  0.0382  0.0042  239 GLU B N   
8007  C CA  . GLU B 239 ? 0.9089 1.1322 1.0371 0.0100  0.0562  0.0065  239 GLU B CA  
8008  C C   . GLU B 239 ? 0.9179 1.1200 1.0084 0.0119  0.0612  -0.0021 239 GLU B C   
8009  O O   . GLU B 239 ? 0.9082 1.1022 0.9866 0.0141  0.0591  -0.0093 239 GLU B O   
8010  C CB  . GLU B 239 ? 0.8964 1.1298 1.0541 0.0156  0.0692  0.0112  239 GLU B CB  
8011  C CG  . GLU B 239 ? 0.9527 1.1820 1.1126 0.0194  0.0920  0.0152  239 GLU B CG  
8012  C CD  . GLU B 239 ? 0.9736 1.2105 1.1630 0.0282  0.1082  0.0202  239 GLU B CD  
8013  O OE1 . GLU B 239 ? 0.9176 1.1512 1.1088 0.0326  0.1045  0.0157  239 GLU B OE1 
8014  O OE2 . GLU B 239 ? 1.0280 1.2738 1.2400 0.0312  0.1257  0.0296  239 GLU B OE2 
8021  N N   . TYR B 240 ? 0.9429 1.1347 1.0128 0.0094  0.0665  -0.0008 240 TYR B N   
8022  C CA  . TYR B 240 ? 0.9984 1.1677 1.0292 0.0090  0.0711  -0.0071 240 TYR B CA  
8023  C C   . TYR B 240 ? 1.0660 1.2226 1.0907 0.0121  0.0949  -0.0078 240 TYR B C   
8024  O O   . TYR B 240 ? 1.0524 1.2182 1.0996 0.0138  0.1087  -0.0006 240 TYR B O   
8025  C CB  . TYR B 240 ? 1.0093 1.1706 1.0169 0.0046  0.0640  -0.0044 240 TYR B CB  
8026  C CG  . TYR B 240 ? 1.0192 1.1749 1.0226 0.0026  0.0784  0.0013  240 TYR B CG  
8027  C CD1 . TYR B 240 ? 1.0944 1.2289 1.0692 0.0021  0.0946  -0.0011 240 TYR B CD1 
8028  C CD2 . TYR B 240 ? 1.0150 1.1832 1.0391 -0.0002 0.0759  0.0091  240 TYR B CD2 
8029  C CE1 . TYR B 240 ? 1.1078 1.2366 1.0783 -0.0001 0.1093  0.0044  240 TYR B CE1 
8030  C CE2 . TYR B 240 ? 1.0352 1.1988 1.0561 -0.0034 0.0889  0.0150  240 TYR B CE2 
8031  C CZ  . TYR B 240 ? 1.1107 1.2559 1.1065 -0.0028 0.1061  0.0128  240 TYR B CZ  
8032  O OH  . TYR B 240 ? 1.1293 1.2694 1.1215 -0.0063 0.1207  0.0190  240 TYR B OH  
8042  N N   . ILE B 241 ? 1.1938 1.3279 1.1876 0.0124  0.1006  -0.0159 241 ILE B N   
8043  C CA  . ILE B 241 ? 1.2248 1.3380 1.2042 0.0159  0.1262  -0.0184 241 ILE B CA  
8044  C C   . ILE B 241 ? 1.3167 1.3960 1.2394 0.0090  0.1281  -0.0248 241 ILE B C   
8045  O O   . ILE B 241 ? 1.3444 1.4137 1.2409 0.0031  0.1114  -0.0305 241 ILE B O   
8046  C CB  . ILE B 241 ? 1.2235 1.3344 1.2167 0.0226  0.1344  -0.0222 241 ILE B CB  
8047  C CG1 . ILE B 241 ? 1.2223 1.3619 1.2709 0.0304  0.1422  -0.0122 241 ILE B CG1 
8048  C CG2 . ILE B 241 ? 1.3320 1.4048 1.2850 0.0236  0.1569  -0.0296 241 ILE B CG2 
8049  C CD1 . ILE B 241 ? 1.3356 1.4718 1.4014 0.0395  0.1556  -0.0131 241 ILE B CD1 
8061  N N   . ILE B 242 ? 1.2494 1.3111 1.1527 0.0083  0.1479  -0.0229 242 ILE B N   
8062  C CA  . ILE B 242 ? 1.3104 1.3339 1.1540 0.0004  0.1528  -0.0285 242 ILE B CA  
8063  C C   . ILE B 242 ? 1.3282 1.3214 1.1523 0.0046  0.1847  -0.0333 242 ILE B C   
8064  O O   . ILE B 242 ? 1.2896 1.2886 1.1380 0.0122  0.2093  -0.0277 242 ILE B O   
8065  C CB  . ILE B 242 ? 1.3142 1.3352 1.1422 -0.0050 0.1504  -0.0224 242 ILE B CB  
8066  C CG1 . ILE B 242 ? 1.2222 1.2739 1.0780 -0.0059 0.1238  -0.0162 242 ILE B CG1 
8067  C CG2 . ILE B 242 ? 1.2739 1.2550 1.0363 -0.0155 0.1490  -0.0271 242 ILE B CG2 
8068  C CD1 . ILE B 242 ? 1.1965 1.2388 1.0245 -0.0125 0.1135  -0.0114 242 ILE B CD1 
8080  N N   . GLU B 243 ? 1.3743 1.3341 1.1545 -0.0005 0.1853  -0.0429 243 GLU B N   
8081  C CA  . GLU B 243 ? 1.4961 1.4211 1.2544 0.0046  0.2168  -0.0489 243 GLU B CA  
8082  C C   . GLU B 243 ? 1.5853 1.4584 1.2663 -0.0094 0.2157  -0.0587 243 GLU B C   
8083  O O   . GLU B 243 ? 1.5959 1.4628 1.2568 -0.0183 0.1930  -0.0640 243 GLU B O   
8084  C CB  . GLU B 243 ? 1.5484 1.4882 1.3449 0.0147  0.2196  -0.0502 243 GLU B CB  
8085  C CG  . GLU B 243 ? 1.5694 1.4729 1.3484 0.0230  0.2543  -0.0553 243 GLU B CG  
8086  C CD  . GLU B 243 ? 1.6739 1.5829 1.4753 0.0297  0.2507  -0.0584 243 GLU B CD  
8087  O OE1 . GLU B 243 ? 1.6036 1.5530 1.4483 0.0307  0.2254  -0.0541 243 GLU B OE1 
8088  O OE2 . GLU B 243 ? 1.7184 1.5876 1.4908 0.0336  0.2743  -0.0651 243 GLU B OE2 
8095  N N   . ASN B 244 ? 1.5619 1.3970 1.1984 -0.0129 0.2397  -0.0603 244 ASN B N   
8096  C CA  . ASN B 244 ? 1.6384 1.4180 1.1928 -0.0292 0.2388  -0.0688 244 ASN B CA  
8097  C C   . ASN B 244 ? 1.6241 1.4148 1.1588 -0.0446 0.1981  -0.0660 244 ASN B C   
8098  O O   . ASN B 244 ? 1.6655 1.4366 1.1622 -0.0580 0.1781  -0.0712 244 ASN B O   
8099  C CB  . ASN B 244 ? 1.6834 1.4253 1.2061 -0.0306 0.2501  -0.0795 244 ASN B CB  
8100  C CG  . ASN B 244 ? 1.7340 1.4513 1.2616 -0.0155 0.2960  -0.0818 244 ASN B CG  
8101  O OD1 . ASN B 244 ? 1.6938 1.4113 1.2442 -0.0052 0.3069  -0.0848 244 ASN B OD1 
8102  N ND2 . ASN B 244 ? 1.7553 1.4507 1.2626 -0.0134 0.3243  -0.0795 244 ASN B ND2 
8109  N N   . ASP B 245 ? 1.5803 1.4029 1.1429 -0.0428 0.1860  -0.0565 245 ASP B N   
8110  C CA  . ASP B 245 ? 1.5981 1.4363 1.1521 -0.0536 0.1494  -0.0508 245 ASP B CA  
8111  C C   . ASP B 245 ? 1.5424 1.4061 1.1208 -0.0552 0.1215  -0.0520 245 ASP B C   
8112  O O   . ASP B 245 ? 1.5475 1.4074 1.0998 -0.0682 0.0939  -0.0502 245 ASP B O   
8113  C CB  . ASP B 245 ? 1.6771 1.4678 1.1534 -0.0717 0.1442  -0.0522 245 ASP B CB  
8114  C CG  . ASP B 245 ? 1.8141 1.5776 1.2625 -0.0712 0.1717  -0.0505 245 ASP B CG  
8115  O OD1 . ASP B 245 ? 1.9333 1.6455 1.3095 -0.0854 0.1781  -0.0543 245 ASP B OD1 
8116  O OD2 . ASP B 245 ? 1.8366 1.6286 1.3331 -0.0582 0.1868  -0.0450 245 ASP B OD2 
8121  N N   . GLU B 246 ? 1.4792 1.3699 1.1093 -0.0425 0.1285  -0.0537 246 GLU B N   
8122  C CA  . GLU B 246 ? 1.4438 1.3619 1.1034 -0.0424 0.1047  -0.0542 246 GLU B CA  
8123  C C   . GLU B 246 ? 1.2953 1.2620 1.0244 -0.0287 0.1009  -0.0477 246 GLU B C   
8124  O O   . GLU B 246 ? 1.2883 1.2643 1.0479 -0.0177 0.1224  -0.0460 246 GLU B O   
8125  C CB  . GLU B 246 ? 1.4309 1.3242 1.0733 -0.0438 0.1150  -0.0641 246 GLU B CB  
8126  C CG  . GLU B 246 ? 1.5033 1.3491 1.0731 -0.0628 0.1080  -0.0705 246 GLU B CG  
8127  C CD  . GLU B 246 ? 1.5019 1.3647 1.0696 -0.0758 0.0711  -0.0676 246 GLU B CD  
8128  O OE1 . GLU B 246 ? 1.5267 1.3546 1.0407 -0.0933 0.0619  -0.0722 246 GLU B OE1 
8129  O OE2 . GLU B 246 ? 1.4340 1.3438 1.0530 -0.0693 0.0520  -0.0599 246 GLU B OE2 
8136  N N   . MET B 247 ? 1.2461 1.2428 0.9992 -0.0302 0.0736  -0.0432 247 MET B N   
8137  C CA  . MET B 247 ? 1.2164 1.2535 1.0252 -0.0203 0.0667  -0.0367 247 MET B CA  
8138  C C   . MET B 247 ? 1.1706 1.2266 1.0117 -0.0160 0.0600  -0.0399 247 MET B C   
8139  O O   . MET B 247 ? 1.1530 1.2092 0.9838 -0.0226 0.0428  -0.0422 247 MET B O   
8140  C CB  . MET B 247 ? 1.1748 1.2281 0.9861 -0.0235 0.0443  -0.0286 247 MET B CB  
8141  C CG  . MET B 247 ? 1.0872 1.1750 0.9476 -0.0148 0.0370  -0.0225 247 MET B CG  
8142  S SD  . MET B 247 ? 1.0694 1.1681 0.9648 -0.0060 0.0592  -0.0205 247 MET B SD  
8143  C CE  . MET B 247 ? 1.0635 1.1588 0.9480 -0.0079 0.0600  -0.0122 247 MET B CE  
8153  N N   . TYR B 248 ? 1.1490 1.2215 1.0296 -0.0059 0.0728  -0.0387 248 TYR B N   
8154  C CA  . TYR B 248 ? 1.0828 1.1734 0.9959 -0.0013 0.0670  -0.0403 248 TYR B CA  
8155  C C   . TYR B 248 ? 1.0389 1.1622 0.9968 0.0043  0.0597  -0.0329 248 TYR B C   
8156  O O   . TYR B 248 ? 1.0186 1.1487 0.9893 0.0070  0.0680  -0.0271 248 TYR B O   
8157  C CB  . TYR B 248 ? 1.0792 1.1555 0.9962 0.0048  0.0886  -0.0446 248 TYR B CB  
8158  C CG  . TYR B 248 ? 1.1492 1.1845 1.0150 -0.0013 0.0995  -0.0531 248 TYR B CG  
8159  C CD1 . TYR B 248 ? 1.1402 1.1622 0.9805 -0.0105 0.0853  -0.0593 248 TYR B CD1 
8160  C CD2 . TYR B 248 ? 1.2148 1.2223 1.0555 0.0006  0.1248  -0.0545 248 TYR B CD2 
8161  C CE1 . TYR B 248 ? 1.1972 1.1766 0.9843 -0.0191 0.0942  -0.0672 248 TYR B CE1 
8162  C CE2 . TYR B 248 ? 1.2241 1.1867 1.0102 -0.0065 0.1364  -0.0629 248 TYR B CE2 
8163  C CZ  . TYR B 248 ? 1.2017 1.1491 0.9592 -0.0171 0.1200  -0.0695 248 TYR B CZ  
8164  O OH  . TYR B 248 ? 1.2786 1.1764 0.9757 -0.0271 0.1303  -0.0781 248 TYR B OH  
8174  N N   . ILE B 249 ? 0.9898 1.1305 0.9683 0.0046  0.0444  -0.0330 249 ILE B N   
8175  C CA  . ILE B 249 ? 0.9248 1.0904 0.9397 0.0081  0.0371  -0.0271 249 ILE B CA  
8176  C C   . ILE B 249 ? 0.9101 1.0842 0.9506 0.0119  0.0391  -0.0284 249 ILE B C   
8177  O O   . ILE B 249 ? 0.8689 1.0395 0.9034 0.0101  0.0321  -0.0335 249 ILE B O   
8178  C CB  . ILE B 249 ? 0.9052 1.0812 0.9196 0.0053  0.0184  -0.0249 249 ILE B CB  
8179  C CG1 . ILE B 249 ? 0.8960 1.0686 0.8974 0.0042  0.0174  -0.0196 249 ILE B CG1 
8180  C CG2 . ILE B 249 ? 0.9089 1.1028 0.9536 0.0076  0.0111  -0.0223 249 ILE B CG2 
8181  C CD1 . ILE B 249 ? 0.8837 1.0660 0.9065 0.0063  0.0216  -0.0135 249 ILE B CD1 
8193  N N   . ASP B 250 ? 0.8992 1.0849 0.9687 0.0162  0.0477  -0.0224 250 ASP B N   
8194  C CA  . ASP B 250 ? 0.8781 1.0747 0.9765 0.0198  0.0476  -0.0202 250 ASP B CA  
8195  C C   . ASP B 250 ? 0.8646 1.0805 0.9867 0.0168  0.0336  -0.0139 250 ASP B C   
8196  O O   . ASP B 250 ? 0.8987 1.1193 1.0212 0.0136  0.0306  -0.0095 250 ASP B O   
8197  C CB  . ASP B 250 ? 0.8704 1.0670 0.9876 0.0267  0.0673  -0.0152 250 ASP B CB  
8198  C CG  . ASP B 250 ? 0.8614 1.0627 1.0018 0.0320  0.0690  -0.0135 250 ASP B CG  
8199  O OD1 . ASP B 250 ? 0.8529 1.0571 0.9933 0.0290  0.0542  -0.0167 250 ASP B OD1 
8200  O OD2 . ASP B 250 ? 0.8614 1.0632 1.0209 0.0398  0.0863  -0.0081 250 ASP B OD2 
8205  N N   . GLY B 251 ? 0.8103 1.0332 0.9480 0.0167  0.0254  -0.0136 251 GLY B N   
8206  C CA  . GLY B 251 ? 0.8305 1.0653 0.9840 0.0120  0.0124  -0.0082 251 GLY B CA  
8207  C C   . GLY B 251 ? 0.7844 1.0229 0.9505 0.0115  0.0045  -0.0081 251 GLY B C   
8208  O O   . GLY B 251 ? 0.7999 1.0311 0.9597 0.0147  0.0071  -0.0138 251 GLY B O   
8212  N N   . PRO B 252 ? 0.7668 1.0138 0.9481 0.0062  -0.0054 -0.0012 252 PRO B N   
8213  C CA  . PRO B 252 ? 0.8113 1.0596 1.0019 0.0044  -0.0138 -0.0001 252 PRO B CA  
8214  C C   . PRO B 252 ? 0.7830 1.0220 0.9529 0.0018  -0.0214 -0.0084 252 PRO B C   
8215  O O   . PRO B 252 ? 0.7727 1.0074 0.9267 -0.0002 -0.0237 -0.0116 252 PRO B O   
8216  C CB  . PRO B 252 ? 0.7266 0.9841 0.9345 -0.0035 -0.0235 0.0109  252 PRO B CB  
8217  C CG  . PRO B 252 ? 0.8129 1.0752 1.0237 -0.0057 -0.0189 0.0158  252 PRO B CG  
8218  C CD  . PRO B 252 ? 0.7870 1.0420 0.9800 0.0010  -0.0071 0.0078  252 PRO B CD  
8226  N N   . VAL B 253 ? 0.7821 1.0181 0.9539 0.0026  -0.0240 -0.0109 253 VAL B N   
8227  C CA  . VAL B 253 ? 0.8134 1.0426 0.9702 -0.0006 -0.0304 -0.0172 253 VAL B CA  
8228  C C   . VAL B 253 ? 0.7979 1.0256 0.9631 -0.0046 -0.0381 -0.0133 253 VAL B C   
8229  O O   . VAL B 253 ? 0.7758 1.0069 0.9575 -0.0020 -0.0370 -0.0081 253 VAL B O   
8230  C CB  . VAL B 253 ? 0.7797 1.0033 0.9234 0.0025  -0.0258 -0.0255 253 VAL B CB  
8231  C CG1 . VAL B 253 ? 0.7654 0.9861 0.8995 -0.0016 -0.0323 -0.0298 253 VAL B CG1 
8232  C CG2 . VAL B 253 ? 0.7897 1.0128 0.9216 0.0046  -0.0205 -0.0280 253 VAL B CG2 
8242  N N   . GLU B 254 ? 0.8146 1.0357 0.9678 -0.0106 -0.0449 -0.0149 254 GLU B N   
8243  C CA  . GLU B 254 ? 0.7959 1.0112 0.9502 -0.0165 -0.0530 -0.0114 254 GLU B CA  
8244  C C   . GLU B 254 ? 0.7915 0.9975 0.9293 -0.0189 -0.0534 -0.0184 254 GLU B C   
8245  O O   . GLU B 254 ? 0.7721 0.9745 0.8977 -0.0198 -0.0511 -0.0216 254 GLU B O   
8246  C CB  . GLU B 254 ? 0.8097 1.0219 0.9633 -0.0254 -0.0613 -0.0033 254 GLU B CB  
8247  C CG  . GLU B 254 ? 0.8521 1.0585 1.0078 -0.0332 -0.0721 0.0034  254 GLU B CG  
8248  C CD  . GLU B 254 ? 0.9262 1.1218 1.0689 -0.0463 -0.0820 0.0097  254 GLU B CD  
8249  O OE1 . GLU B 254 ? 0.9266 1.1262 1.0717 -0.0487 -0.0818 0.0133  254 GLU B OE1 
8250  O OE2 . GLU B 254 ? 0.9190 1.0991 1.0454 -0.0554 -0.0898 0.0110  254 GLU B OE2 
8257  N N   . ILE B 255 ? 0.8168 1.0189 0.9558 -0.0195 -0.0552 -0.0196 255 ILE B N   
8258  C CA  . ILE B 255 ? 0.7946 0.9883 0.9200 -0.0232 -0.0555 -0.0248 255 ILE B CA  
8259  C C   . ILE B 255 ? 0.8301 1.0110 0.9437 -0.0318 -0.0613 -0.0209 255 ILE B C   
8260  O O   . ILE B 255 ? 0.8527 1.0293 0.9700 -0.0366 -0.0694 -0.0141 255 ILE B O   
8261  C CB  . ILE B 255 ? 0.8179 1.0086 0.9455 -0.0222 -0.0551 -0.0274 255 ILE B CB  
8262  C CG1 . ILE B 255 ? 0.7756 0.9717 0.9082 -0.0155 -0.0487 -0.0312 255 ILE B CG1 
8263  C CG2 . ILE B 255 ? 0.7963 0.9806 0.9113 -0.0271 -0.0544 -0.0324 255 ILE B CG2 
8264  C CD1 . ILE B 255 ? 0.7783 0.9797 0.9025 -0.0153 -0.0452 -0.0370 255 ILE B CD1 
8276  N N   . ILE B 256 ? 0.8234 0.9965 0.9219 -0.0340 -0.0569 -0.0243 256 ILE B N   
8277  C CA  . ILE B 256 ? 0.8716 1.0250 0.9504 -0.0429 -0.0595 -0.0218 256 ILE B CA  
8278  C C   . ILE B 256 ? 0.8802 1.0205 0.9462 -0.0479 -0.0586 -0.0242 256 ILE B C   
8279  O O   . ILE B 256 ? 0.8591 0.9864 0.9160 -0.0562 -0.0668 -0.0201 256 ILE B O   
8280  C CB  . ILE B 256 ? 0.8988 1.0450 0.9652 -0.0414 -0.0516 -0.0235 256 ILE B CB  
8281  C CG1 . ILE B 256 ? 0.8894 1.0407 0.9614 -0.0409 -0.0548 -0.0194 256 ILE B CG1 
8282  C CG2 . ILE B 256 ? 0.8688 0.9869 0.9068 -0.0500 -0.0488 -0.0237 256 ILE B CG2 
8283  C CD1 . ILE B 256 ? 0.8523 1.0022 0.9185 -0.0351 -0.0457 -0.0214 256 ILE B CD1 
8295  N N   . ALA B 257 ? 0.8691 1.0134 0.9349 -0.0438 -0.0491 -0.0296 257 ALA B N   
8296  C CA  . ALA B 257 ? 0.8499 0.9814 0.9028 -0.0489 -0.0450 -0.0317 257 ALA B CA  
8297  C C   . ALA B 257 ? 0.8252 0.9735 0.8926 -0.0445 -0.0403 -0.0354 257 ALA B C   
8298  O O   . ALA B 257 ? 0.8141 0.9811 0.8972 -0.0382 -0.0401 -0.0366 257 ALA B O   
8299  C CB  . ALA B 257 ? 0.8801 0.9921 0.9117 -0.0513 -0.0346 -0.0323 257 ALA B CB  
8305  N N   . GLU B 258 ? 0.8279 0.9674 0.8873 -0.0498 -0.0369 -0.0368 258 GLU B N   
8306  C CA  . GLU B 258 ? 0.8069 0.9603 0.8783 -0.0494 -0.0347 -0.0394 258 GLU B CA  
8307  C C   . GLU B 258 ? 0.8418 0.9836 0.9022 -0.0556 -0.0268 -0.0397 258 GLU B C   
8308  O O   . GLU B 258 ? 0.8642 0.9830 0.9047 -0.0624 -0.0284 -0.0389 258 GLU B O   
8309  C CB  . GLU B 258 ? 0.8266 0.9815 0.9032 -0.0504 -0.0439 -0.0403 258 GLU B CB  
8310  C CG  . GLU B 258 ? 0.8668 1.0311 0.9503 -0.0526 -0.0430 -0.0435 258 GLU B CG  
8311  C CD  . GLU B 258 ? 0.8807 1.0408 0.9654 -0.0518 -0.0491 -0.0450 258 GLU B CD  
8312  O OE1 . GLU B 258 ? 0.8797 1.0340 0.9657 -0.0479 -0.0532 -0.0422 258 GLU B OE1 
8313  O OE2 . GLU B 258 ? 0.9220 1.0838 1.0065 -0.0555 -0.0489 -0.0481 258 GLU B OE2 
8320  N N   . GLY B 259 ? 0.7326 0.8903 0.8062 -0.0541 -0.0187 -0.0398 259 GLY B N   
8321  C CA  . GLY B 259 ? 0.8228 0.9728 0.8903 -0.0599 -0.0092 -0.0393 259 GLY B CA  
8322  C C   . GLY B 259 ? 0.8466 1.0166 0.9334 -0.0558 0.0033  -0.0359 259 GLY B C   
8323  O O   . GLY B 259 ? 0.7769 0.9735 0.8864 -0.0519 -0.0004 -0.0338 259 GLY B O   
8327  N N   . LYS B 260 ? 0.8784 1.0349 0.9559 -0.0569 0.0187  -0.0341 260 LYS B N   
8328  C CA  . LYS B 260 ? 0.8901 1.0661 0.9902 -0.0522 0.0339  -0.0285 260 LYS B CA  
8329  C C   . LYS B 260 ? 0.8986 1.0660 0.9955 -0.0414 0.0488  -0.0256 260 LYS B C   
8330  O O   . LYS B 260 ? 0.9060 1.0402 0.9718 -0.0424 0.0529  -0.0290 260 LYS B O   
8331  C CB  . LYS B 260 ? 0.8414 1.0077 0.9353 -0.0603 0.0454  -0.0276 260 LYS B CB  
8332  C CG  . LYS B 260 ? 0.8814 1.0469 0.9707 -0.0722 0.0322  -0.0309 260 LYS B CG  
8333  C CD  . LYS B 260 ? 0.9162 1.1174 1.0373 -0.0750 0.0253  -0.0273 260 LYS B CD  
8334  C CE  . LYS B 260 ? 0.8979 1.0920 1.0092 -0.0874 0.0136  -0.0312 260 LYS B CE  
8335  N NZ  . LYS B 260 ? 0.9030 1.1263 1.0399 -0.0949 0.0100  -0.0267 260 LYS B NZ  
8349  N N   . ILE B 261 ? 0.8550 1.0509 0.9834 -0.0318 0.0564  -0.0183 261 ILE B N   
8350  C CA  . ILE B 261 ? 0.8790 1.0678 1.0088 -0.0193 0.0738  -0.0138 261 ILE B CA  
8351  C C   . ILE B 261 ? 0.9102 1.1167 1.0675 -0.0134 0.0943  -0.0044 261 ILE B C   
8352  O O   . ILE B 261 ? 0.8596 1.1015 1.0500 -0.0166 0.0885  0.0017  261 ILE B O   
8353  C CB  . ILE B 261 ? 0.8806 1.0879 1.0258 -0.0102 0.0639  -0.0110 261 ILE B CB  
8354  C CG1 . ILE B 261 ? 0.9298 1.1193 1.0673 0.0024  0.0819  -0.0076 261 ILE B CG1 
8355  C CG2 . ILE B 261 ? 0.8910 1.1432 1.0774 -0.0082 0.0553  -0.0028 261 ILE B CG2 
8356  C CD1 . ILE B 261 ? 0.9756 1.1721 1.1167 0.0094  0.0715  -0.0067 261 ILE B CD1 
8368  N N   . TYR B 262 ? 0.9599 1.1402 1.1026 -0.0056 0.1191  -0.0027 262 TYR B N   
8369  C CA  . TYR B 262 ? 0.9651 1.1565 1.1322 0.0019  0.1446  0.0069  262 TYR B CA  
8370  C C   . TYR B 262 ? 0.9998 1.2024 1.1906 0.0207  0.1596  0.0168  262 TYR B C   
8371  O O   . TYR B 262 ? 1.0151 1.1818 1.1755 0.0276  0.1706  0.0129  262 TYR B O   
8372  C CB  . TYR B 262 ? 0.9440 1.0898 1.0715 -0.0036 0.1662  0.0015  262 TYR B CB  
8373  C CG  . TYR B 262 ? 0.9505 1.0801 1.0501 -0.0219 0.1504  -0.0076 262 TYR B CG  
8374  C CD1 . TYR B 262 ? 0.9422 1.1007 1.0668 -0.0307 0.1426  -0.0048 262 TYR B CD1 
8375  C CD2 . TYR B 262 ? 0.9791 1.0641 1.0277 -0.0311 0.1422  -0.0176 262 TYR B CD2 
8376  C CE1 . TYR B 262 ? 0.9323 1.0735 1.0309 -0.0463 0.1289  -0.0123 262 TYR B CE1 
8377  C CE2 . TYR B 262 ? 0.9403 1.0115 0.9663 -0.0466 0.1271  -0.0236 262 TYR B CE2 
8378  C CZ  . TYR B 262 ? 0.9230 1.0213 0.9736 -0.0532 0.1214  -0.0212 262 TYR B CZ  
8379  O OH  . TYR B 262 ? 0.9812 1.0634 1.0087 -0.0675 0.1072  -0.0265 262 TYR B OH  
8389  N N   . ILE B 263 ? 1.0062 1.2577 1.2506 0.0280  0.1591  0.0306  263 ILE B N   
8390  C CA  . ILE B 263 ? 0.9992 1.2698 1.2752 0.0467  0.1700  0.0434  263 ILE B CA  
8391  C C   . ILE B 263 ? 1.0407 1.3459 1.3671 0.0552  0.1901  0.0605  263 ILE B C   
8392  O O   . ILE B 263 ? 1.0542 1.3831 1.4002 0.0439  0.1858  0.0635  263 ILE B O   
8393  C CB  . ILE B 263 ? 1.0275 1.3299 1.3230 0.0467  0.1412  0.0464  263 ILE B CB  
8394  C CG1 . ILE B 263 ? 1.0071 1.2731 1.2569 0.0437  0.1293  0.0325  263 ILE B CG1 
8395  C CG2 . ILE B 263 ? 1.0452 1.3819 1.3877 0.0642  0.1485  0.0648  263 ILE B CG2 
8396  C CD1 . ILE B 263 ? 0.9954 1.2424 1.2374 0.0599  0.1428  0.0361  263 ILE B CD1 
8408  N N   . GLY B 264 ? 1.1295 1.4370 1.4777 0.0756  0.2133  0.0727  264 GLY B N   
8409  C CA  . GLY B 264 ? 1.1325 1.4772 1.5365 0.0865  0.2344  0.0924  264 GLY B CA  
8410  C C   . GLY B 264 ? 1.1436 1.5548 1.6053 0.0804  0.2073  0.1072  264 GLY B C   
8411  O O   . GLY B 264 ? 1.1494 1.5782 1.6152 0.0776  0.1794  0.1074  264 GLY B O   
8415  N N   . LYS B 265 ? 1.1541 1.6006 1.6584 0.0766  0.2159  0.1202  265 LYS B N   
8416  C CA  . LYS B 265 ? 1.1297 1.6389 1.6877 0.0664  0.1895  0.1357  265 LYS B CA  
8417  C C   . LYS B 265 ? 1.1175 1.6735 1.7421 0.0856  0.1992  0.1631  265 LYS B C   
8418  O O   . LYS B 265 ? 1.1043 1.6421 1.7332 0.1085  0.2291  0.1693  265 LYS B O   
8419  C CB  . LYS B 265 ? 1.1455 1.6700 1.7146 0.0482  0.1898  0.1361  265 LYS B CB  
8420  C CG  . LYS B 265 ? 1.0840 1.6440 1.6659 0.0249  0.1511  0.1371  265 LYS B CG  
8421  C CD  . LYS B 265 ? 1.1133 1.7406 1.7689 0.0239  0.1433  0.1648  265 LYS B CD  
8422  C CE  . LYS B 265 ? 1.0722 1.7269 1.7340 -0.0045 0.1108  0.1649  265 LYS B CE  
8423  N NZ  . LYS B 265 ? 1.0319 1.6619 1.6444 -0.0174 0.0794  0.1463  265 LYS B NZ  
8437  N N   . ASP C 2   ? 1.5266 1.9830 1.6511 -0.0401 -0.1569 -0.0852 2   ASP C N   
8438  C CA  . ASP C 2   ? 1.5431 1.9901 1.6740 -0.0162 -0.1523 -0.0801 2   ASP C CA  
8439  C C   . ASP C 2   ? 1.5590 1.9451 1.6423 -0.0105 -0.1491 -0.0666 2   ASP C C   
8440  O O   . ASP C 2   ? 1.6261 1.9938 1.6968 0.0088  -0.1643 -0.0604 2   ASP C O   
8441  C CB  . ASP C 2   ? 1.5395 2.0207 1.7024 0.0084  -0.1756 -0.0847 2   ASP C CB  
8442  C CG  . ASP C 2   ? 1.5338 2.0134 1.7109 0.0316  -0.1681 -0.0830 2   ASP C CG  
8443  O OD1 . ASP C 2   ? 1.5129 2.0062 1.7079 0.0265  -0.1453 -0.0874 2   ASP C OD1 
8444  O OD2 . ASP C 2   ? 1.5035 1.9650 1.6706 0.0543  -0.1851 -0.0772 2   ASP C OD2 
8449  N N   . ARG C 3   ? 1.5276 1.8820 1.5847 -0.0275 -0.1291 -0.0625 3   ARG C N   
8450  C CA  . ARG C 3   ? 1.4559 1.7566 1.4723 -0.0245 -0.1223 -0.0515 3   ARG C CA  
8451  C C   . ARG C 3   ? 1.4646 1.7485 1.4751 -0.0361 -0.0961 -0.0499 3   ARG C C   
8452  O O   . ARG C 3   ? 1.4836 1.7673 1.4890 -0.0560 -0.0864 -0.0536 3   ARG C O   
8453  C CB  . ARG C 3   ? 1.4491 1.7197 1.4273 -0.0343 -0.1341 -0.0478 3   ARG C CB  
8454  C CG  . ARG C 3   ? 1.5025 1.7610 1.4627 -0.0597 -0.1223 -0.0508 3   ARG C CG  
8455  C CD  . ARG C 3   ? 1.5360 1.8391 1.5268 -0.0740 -0.1242 -0.0616 3   ARG C CD  
8456  N NE  . ARG C 3   ? 1.5631 1.8966 1.5677 -0.0703 -0.1507 -0.0667 3   ARG C NE  
8457  C CZ  . ARG C 3   ? 1.5738 1.9516 1.6078 -0.0824 -0.1573 -0.0773 3   ARG C CZ  
8458  N NH1 . ARG C 3   ? 1.5848 1.9793 1.6345 -0.1007 -0.1382 -0.0839 3   ARG C NH1 
8459  N NH2 . ARG C 3   ? 1.5775 1.9829 1.6249 -0.0766 -0.1844 -0.0816 3   ARG C NH2 
8473  N N   . LYS C 4   ? 1.4352 1.7038 1.4455 -0.0236 -0.0860 -0.0447 4   LYS C N   
8474  C CA  . LYS C 4   ? 1.3565 1.6128 1.3653 -0.0313 -0.0640 -0.0434 4   LYS C CA  
8475  C C   . LYS C 4   ? 1.3176 1.5419 1.3112 -0.0185 -0.0581 -0.0351 4   LYS C C   
8476  O O   . LYS C 4   ? 1.2989 1.5284 1.3020 -0.0013 -0.0651 -0.0337 4   LYS C O   
8477  C CB  . LYS C 4   ? 1.4086 1.7024 1.4507 -0.0326 -0.0558 -0.0507 4   LYS C CB  
8478  C CG  . LYS C 4   ? 1.4700 1.7935 1.5403 -0.0128 -0.0656 -0.0543 4   LYS C CG  
8479  C CD  . LYS C 4   ? 1.4712 1.8461 1.5785 -0.0183 -0.0668 -0.0662 4   LYS C CD  
8480  C CE  . LYS C 4   ? 1.4684 1.8737 1.6057 0.0041  -0.0786 -0.0711 4   LYS C CE  
8481  N NZ  . LYS C 4   ? 1.4663 1.9224 1.6388 0.0021  -0.0905 -0.0826 4   LYS C NZ  
8495  N N   . VAL C 5   ? 1.2164 1.4079 1.1875 -0.0269 -0.0454 -0.0306 5   VAL C N   
8496  C CA  . VAL C 5   ? 1.1573 1.3198 1.1154 -0.0177 -0.0390 -0.0238 5   VAL C CA  
8497  C C   . VAL C 5   ? 1.1296 1.2946 1.1004 -0.0173 -0.0247 -0.0236 5   VAL C C   
8498  O O   . VAL C 5   ? 1.0097 1.1765 0.9819 -0.0295 -0.0147 -0.0259 5   VAL C O   
8499  C CB  . VAL C 5   ? 1.1002 1.2269 1.0282 -0.0258 -0.0340 -0.0200 5   VAL C CB  
8500  C CG1 . VAL C 5   ? 1.0992 1.2200 1.0084 -0.0287 -0.0486 -0.0202 5   VAL C CG1 
8501  C CG2 . VAL C 5   ? 1.1012 1.2192 1.0246 -0.0406 -0.0197 -0.0222 5   VAL C CG2 
8511  N N   . GLN C 6   ? 1.0799 1.2420 1.0567 -0.0037 -0.0245 -0.0207 6   GLN C N   
8512  C CA  . GLN C 6   ? 1.0388 1.2001 1.0239 -0.0020 -0.0133 -0.0199 6   GLN C CA  
8513  C C   . GLN C 6   ? 1.0575 1.1879 1.0278 0.0003  -0.0073 -0.0139 6   GLN C C   
8514  O O   . GLN C 6   ? 1.1015 1.2177 1.0625 0.0078  -0.0125 -0.0107 6   GLN C O   
8515  C CB  . GLN C 6   ? 1.0559 1.2378 1.0593 0.0109  -0.0172 -0.0225 6   GLN C CB  
8516  C CG  . GLN C 6   ? 1.1265 1.3158 1.1391 0.0087  -0.0061 -0.0243 6   GLN C CG  
8517  C CD  . GLN C 6   ? 1.1016 1.3173 1.1340 0.0185  -0.0081 -0.0300 6   GLN C CD  
8518  O OE1 . GLN C 6   ? 1.1538 1.3827 1.1956 0.0295  -0.0191 -0.0326 6   GLN C OE1 
8519  N NE2 . GLN C 6   ? 1.0914 1.3132 1.1288 0.0150  0.0024  -0.0324 6   GLN C NE2 
8528  N N   . VAL C 7   ? 1.0416 1.1612 1.0097 -0.0064 0.0035  -0.0128 7   VAL C N   
8529  C CA  . VAL C 7   ? 1.0311 1.1255 0.9899 -0.0054 0.0096  -0.0088 7   VAL C CA  
8530  C C   . VAL C 7   ? 0.9714 1.0654 0.9389 0.0010  0.0130  -0.0069 7   VAL C C   
8531  O O   . VAL C 7   ? 1.0400 1.1382 1.0113 -0.0030 0.0176  -0.0076 7   VAL C O   
8532  C CB  . VAL C 7   ? 0.9875 1.0668 0.9365 -0.0163 0.0176  -0.0095 7   VAL C CB  
8533  C CG1 . VAL C 7   ? 0.9634 1.0205 0.9069 -0.0138 0.0239  -0.0070 7   VAL C CG1 
8534  C CG2 . VAL C 7   ? 0.9736 1.0549 0.9122 -0.0250 0.0138  -0.0124 7   VAL C CG2 
8544  N N   . LEU C 8   ? 0.9554 1.0415 0.9230 0.0096  0.0105  -0.0044 8   LEU C N   
8545  C CA  . LEU C 8   ? 0.9245 1.0094 0.8984 0.0156  0.0116  -0.0030 8   LEU C CA  
8546  C C   . LEU C 8   ? 0.9298 0.9970 0.9022 0.0159  0.0154  -0.0004 8   LEU C C   
8547  O O   . LEU C 8   ? 1.0059 1.0620 0.9720 0.0134  0.0176  0.0000  8   LEU C O   
8548  C CB  . LEU C 8   ? 0.9306 1.0230 0.9078 0.0255  0.0049  -0.0038 8   LEU C CB  
8549  C CG  . LEU C 8   ? 0.9995 1.1145 0.9860 0.0282  0.0025  -0.0081 8   LEU C CG  
8550  C CD1 . LEU C 8   ? 1.0142 1.1437 1.0033 0.0206  0.0020  -0.0111 8   LEU C CD1 
8551  C CD2 . LEU C 8   ? 1.0110 1.1299 0.9999 0.0404  -0.0050 -0.0095 8   LEU C CD2 
8563  N N   . ASP C 9   ? 0.9280 0.9932 0.9060 0.0184  0.0164  0.0008  9   ASP C N   
8564  C CA  . ASP C 9   ? 0.9434 0.9975 0.9259 0.0199  0.0182  0.0023  9   ASP C CA  
8565  C C   . ASP C 9   ? 0.9391 0.9916 0.9223 0.0254  0.0139  0.0028  9   ASP C C   
8566  O O   . ASP C 9   ? 0.9375 0.9953 0.9207 0.0296  0.0100  0.0025  9   ASP C O   
8567  C CB  . ASP C 9   ? 0.9499 1.0011 0.9370 0.0200  0.0186  0.0036  9   ASP C CB  
8568  C CG  . ASP C 9   ? 1.0154 1.0639 0.9974 0.0143  0.0225  0.0034  9   ASP C CG  
8569  O OD1 . ASP C 9   ? 1.0227 1.0758 0.9991 0.0093  0.0246  0.0016  9   ASP C OD1 
8570  O OD2 . ASP C 9   ? 1.0339 1.0739 1.0161 0.0146  0.0225  0.0050  9   ASP C OD2 
8575  N N   . PHE C 10  ? 0.9285 0.9718 0.9106 0.0241  0.0160  0.0029  10  PHE C N   
8576  C CA  . PHE C 10  ? 0.9181 0.9551 0.8965 0.0271  0.0127  0.0032  10  PHE C CA  
8577  C C   . PHE C 10  ? 0.9083 0.9400 0.8959 0.0242  0.0158  0.0026  10  PHE C C   
8578  O O   . PHE C 10  ? 0.9010 0.9329 0.8972 0.0203  0.0218  0.0014  10  PHE C O   
8579  C CB  . PHE C 10  ? 0.9343 0.9622 0.8978 0.0265  0.0116  0.0038  10  PHE C CB  
8580  C CG  . PHE C 10  ? 0.9359 0.9503 0.8936 0.0192  0.0186  0.0037  10  PHE C CG  
8581  C CD1 . PHE C 10  ? 0.9390 0.9418 0.8938 0.0168  0.0203  0.0037  10  PHE C CD1 
8582  C CD2 . PHE C 10  ? 0.9566 0.9688 0.9102 0.0133  0.0246  0.0027  10  PHE C CD2 
8583  C CE1 . PHE C 10  ? 0.9429 0.9341 0.8921 0.0080  0.0292  0.0025  10  PHE C CE1 
8584  C CE2 . PHE C 10  ? 0.9409 0.9403 0.8878 0.0056  0.0334  0.0013  10  PHE C CE2 
8585  C CZ  . PHE C 10  ? 0.9656 0.9554 0.9109 0.0027  0.0363  0.0011  10  PHE C CZ  
8595  N N   . ILE C 11  ? 0.9226 0.9503 0.9093 0.0262  0.0117  0.0026  11  ILE C N   
8596  C CA  . ILE C 11  ? 0.9068 0.9309 0.9025 0.0219  0.0138  0.0010  11  ILE C CA  
8597  C C   . ILE C 11  ? 0.9145 0.9242 0.8957 0.0206  0.0123  0.0013  11  ILE C C   
8598  O O   . ILE C 11  ? 0.9427 0.9487 0.9149 0.0265  0.0059  0.0019  11  ILE C O   
8599  C CB  . ILE C 11  ? 0.9133 0.9454 0.9224 0.0243  0.0082  0.0005  11  ILE C CB  
8600  C CG1 . ILE C 11  ? 0.8823 0.9227 0.9003 0.0265  0.0082  0.0013  11  ILE C CG1 
8601  C CG2 . ILE C 11  ? 0.9242 0.9572 0.9471 0.0189  0.0093  -0.0022 11  ILE C CG2 
8602  C CD1 . ILE C 11  ? 0.9266 0.9690 0.9354 0.0308  0.0030  0.0032  11  ILE C CD1 
8614  N N   . LYS C 12  ? 0.8943 0.8938 0.8715 0.0127  0.0190  0.0003  12  LYS C N   
8615  C CA  . LYS C 12  ? 0.9258 0.9055 0.8846 0.0095  0.0183  0.0009  12  LYS C CA  
8616  C C   . LYS C 12  ? 0.9319 0.9118 0.9021 0.0022  0.0201  -0.0022 12  LYS C C   
8617  O O   . LYS C 12  ? 0.9448 0.9339 0.9323 -0.0056 0.0277  -0.0054 12  LYS C O   
8618  C CB  . LYS C 12  ? 0.9490 0.9117 0.8884 0.0031  0.0248  0.0022  12  LYS C CB  
8619  C CG  . LYS C 12  ? 0.9997 0.9355 0.9150 -0.0013 0.0239  0.0036  12  LYS C CG  
8620  C CD  . LYS C 12  ? 1.0656 0.9791 0.9515 -0.0028 0.0243  0.0071  12  LYS C CD  
8621  C CE  . LYS C 12  ? 1.0859 0.9722 0.9444 0.0028  0.0152  0.0105  12  LYS C CE  
8622  N NZ  . LYS C 12  ? 1.0766 0.9373 0.9030 0.0010  0.0136  0.0147  12  LYS C NZ  
8636  N N   . ILE C 13  ? 0.9397 0.9103 0.9015 0.0045  0.0132  -0.0021 13  ILE C N   
8637  C CA  . ILE C 13  ? 0.9518 0.9232 0.9235 -0.0029 0.0124  -0.0055 13  ILE C CA  
8638  C C   . ILE C 13  ? 0.9963 0.9398 0.9429 -0.0081 0.0125  -0.0052 13  ILE C C   
8639  O O   . ILE C 13  ? 0.9876 0.9125 0.9104 -0.0008 0.0090  -0.0021 13  ILE C O   
8640  C CB  . ILE C 13  ? 0.9209 0.9051 0.9037 0.0038  0.0029  -0.0064 13  ILE C CB  
8641  C CG1 . ILE C 13  ? 0.9224 0.9283 0.9250 0.0088  0.0021  -0.0058 13  ILE C CG1 
8642  C CG2 . ILE C 13  ? 0.9358 0.9211 0.9283 -0.0048 -0.0001 -0.0103 13  ILE C CG2 
8643  C CD1 . ILE C 13  ? 0.9404 0.9505 0.9378 0.0184  -0.0055 -0.0039 13  ILE C CD1 
8655  N N   . ASN C 14  ? 0.9944 0.9345 0.9467 -0.0208 0.0160  -0.0089 14  ASN C N   
8656  C CA  . ASN C 14  ? 1.0263 0.9362 0.9531 -0.0290 0.0172  -0.0091 14  ASN C CA  
8657  C C   . ASN C 14  ? 1.0369 0.9477 0.9698 -0.0330 0.0106  -0.0131 14  ASN C C   
8658  O O   . ASN C 14  ? 1.0211 0.9391 0.9687 -0.0474 0.0146  -0.0178 14  ASN C O   
8659  C CB  . ASN C 14  ? 1.0173 0.9172 0.9394 -0.0457 0.0302  -0.0108 14  ASN C CB  
8660  C CG  . ASN C 14  ? 1.0489 0.9143 0.9424 -0.0573 0.0321  -0.0111 14  ASN C CG  
8661  O OD1 . ASN C 14  ? 1.0692 0.9101 0.9377 -0.0490 0.0236  -0.0083 14  ASN C OD1 
8662  N ND2 . ASN C 14  ? 1.0580 0.9202 0.9544 -0.0768 0.0443  -0.0151 14  ASN C ND2 
8669  N N   . PRO C 15  ? 1.0577 0.9620 0.9798 -0.0213 0.0008  -0.0122 15  PRO C N   
8670  C CA  . PRO C 15  ? 1.0366 0.9360 0.9576 -0.0260 -0.0057 -0.0162 15  PRO C CA  
8671  C C   . PRO C 15  ? 1.0669 0.9293 0.9579 -0.0340 -0.0041 -0.0171 15  PRO C C   
8672  O O   . PRO C 15  ? 1.0866 0.9243 0.9518 -0.0235 -0.0085 -0.0156 15  PRO C O   
8673  C CB  . PRO C 15  ? 1.0258 0.9308 0.9436 -0.0102 -0.0142 -0.0154 15  PRO C CB  
8674  C CG  . PRO C 15  ? 1.0361 0.9335 0.9405 0.0024  -0.0121 -0.0111 15  PRO C CG  
8675  C CD  . PRO C 15  ? 1.0590 0.9620 0.9706 -0.0041 -0.0039 -0.0086 15  PRO C CD  
8683  N N   . ALA C 16  ? 1.0823 0.9397 0.9763 -0.0526 0.0027  -0.0202 16  ALA C N   
8684  C CA  . ALA C 16  ? 1.1823 1.0010 1.0454 -0.0642 0.0053  -0.0213 16  ALA C CA  
8685  C C   . ALA C 16  ? 1.2045 0.9869 1.0311 -0.0551 0.0067  -0.0152 16  ALA C C   
8686  O O   . ALA C 16  ? 1.2382 0.9849 1.0338 -0.0506 0.0021  -0.0145 16  ALA C O   
8687  C CB  . ALA C 16  ? 1.0909 0.8983 0.9452 -0.0647 -0.0038 -0.0255 16  ALA C CB  
8693  N N   . GLY C 17  ? 1.1315 0.9218 0.9611 -0.0517 0.0121  -0.0110 17  GLY C N   
8694  C CA  . GLY C 17  ? 1.1948 0.9523 0.9903 -0.0438 0.0116  -0.0050 17  GLY C CA  
8695  C C   . GLY C 17  ? 1.2187 0.9783 1.0098 -0.0196 0.0011  -0.0018 17  GLY C C   
8696  O O   . GLY C 17  ? 1.2400 0.9781 1.0079 -0.0107 -0.0017 0.0032  17  GLY C O   
8700  N N   . ASN C 18  ? 1.1815 0.9661 0.9936 -0.0092 -0.0049 -0.0050 18  ASN C N   
8701  C CA  . ASN C 18  ? 1.1674 0.9592 0.9796 0.0123  -0.0125 -0.0038 18  ASN C CA  
8702  C C   . ASN C 18  ? 1.1451 0.9725 0.9822 0.0171  -0.0108 -0.0018 18  ASN C C   
8703  O O   . ASN C 18  ? 1.0810 0.9382 0.9417 0.0212  -0.0121 -0.0040 18  ASN C O   
8704  C CB  . ASN C 18  ? 1.1816 0.9782 0.9986 0.0186  -0.0176 -0.0088 18  ASN C CB  
8705  C CG  . ASN C 18  ? 1.1942 0.9850 1.0019 0.0397  -0.0236 -0.0095 18  ASN C CG  
8706  O OD1 . ASN C 18  ? 1.2641 1.0469 1.0625 0.0506  -0.0261 -0.0060 18  ASN C OD1 
8707  N ND2 . ASN C 18  ? 1.1519 0.9474 0.9623 0.0455  -0.0260 -0.0147 18  ASN C ND2 
8714  N N   . ILE C 19  ? 1.1971 1.0172 1.0245 0.0161  -0.0081 0.0025  19  ILE C N   
8715  C CA  . ILE C 19  ? 1.0721 0.9210 0.9195 0.0167  -0.0048 0.0040  19  ILE C CA  
8716  C C   . ILE C 19  ? 1.0599 0.9350 0.9243 0.0319  -0.0106 0.0029  19  ILE C C   
8717  O O   . ILE C 19  ? 1.0662 0.9340 0.9204 0.0461  -0.0175 0.0031  19  ILE C O   
8718  C CB  . ILE C 19  ? 1.1442 0.9746 0.9702 0.0152  -0.0033 0.0087  19  ILE C CB  
8719  C CG1 . ILE C 19  ? 1.1668 0.9667 0.9705 -0.0022 0.0045  0.0095  19  ILE C CG1 
8720  C CG2 . ILE C 19  ? 1.0673 0.9250 0.9117 0.0140  0.0011  0.0093  19  ILE C CG2 
8721  C CD1 . ILE C 19  ? 1.1522 0.9684 0.9784 -0.0188 0.0143  0.0045  19  ILE C CD1 
8733  N N   . THR C 20  ? 1.0372 0.9422 0.9275 0.0289  -0.0076 0.0013  20  THR C N   
8734  C CA  . THR C 20  ? 0.9838 0.9128 0.8891 0.0392  -0.0110 -0.0001 20  THR C CA  
8735  C C   . THR C 20  ? 0.9649 0.9155 0.8853 0.0375  -0.0073 0.0016  20  THR C C   
8736  O O   . THR C 20  ? 0.9532 0.9081 0.8822 0.0275  -0.0013 0.0019  20  THR C O   
8737  C CB  . THR C 20  ? 1.0156 0.9542 0.9322 0.0367  -0.0124 -0.0034 20  THR C CB  
8738  O OG1 . THR C 20  ? 1.0338 0.9495 0.9363 0.0321  -0.0140 -0.0054 20  THR C OG1 
8739  C CG2 . THR C 20  ? 1.0169 0.9688 0.9371 0.0476  -0.0156 -0.0054 20  THR C CG2 
8747  N N   . ILE C 21  ? 0.9633 0.9277 0.8873 0.0470  -0.0101 0.0016  21  ILE C N   
8748  C CA  . ILE C 21  ? 0.9733 0.9581 0.9107 0.0453  -0.0070 0.0024  21  ILE C CA  
8749  C C   . ILE C 21  ? 0.9495 0.9528 0.8990 0.0493  -0.0080 0.0002  21  ILE C C   
8750  O O   . ILE C 21  ? 0.9238 0.9300 0.8702 0.0578  -0.0111 -0.0021 21  ILE C O   
8751  C CB  . ILE C 21  ? 0.9434 0.9284 0.8728 0.0497  -0.0094 0.0040  21  ILE C CB  
8752  C CG1 . ILE C 21  ? 1.0187 0.9807 0.9298 0.0438  -0.0081 0.0069  21  ILE C CG1 
8753  C CG2 . ILE C 21  ? 0.9046 0.9107 0.8471 0.0472  -0.0064 0.0038  21  ILE C CG2 
8754  C CD1 . ILE C 21  ? 1.0093 0.9670 0.9245 0.0304  0.0012  0.0069  21  ILE C CD1 
8766  N N   . LEU C 22  ? 0.9295 0.9435 0.8916 0.0434  -0.0050 0.0006  22  LEU C N   
8767  C CA  . LEU C 22  ? 0.9236 0.9507 0.8922 0.0451  -0.0056 -0.0004 22  LEU C CA  
8768  C C   . LEU C 22  ? 0.9439 0.9833 0.9184 0.0432  -0.0021 0.0007  22  LEU C C   
8769  O O   . LEU C 22  ? 0.9037 0.9421 0.8829 0.0382  0.0012  0.0022  22  LEU C O   
8770  C CB  . LEU C 22  ? 0.9171 0.9431 0.8922 0.0407  -0.0074 -0.0002 22  LEU C CB  
8771  C CG  . LEU C 22  ? 0.9322 0.9458 0.9017 0.0395  -0.0111 -0.0019 22  LEU C CG  
8772  C CD1 . LEU C 22  ? 0.9335 0.9498 0.9130 0.0344  -0.0150 -0.0020 22  LEU C CD1 
8773  C CD2 . LEU C 22  ? 0.9402 0.9479 0.8964 0.0460  -0.0135 -0.0045 22  LEU C CD2 
8785  N N   . ILE C 23  ? 0.9578 1.0083 0.9318 0.0464  -0.0018 -0.0009 23  ILE C N   
8786  C CA  . ILE C 23  ? 0.9568 1.0186 0.9349 0.0426  0.0016  -0.0007 23  ILE C CA  
8787  C C   . ILE C 23  ? 0.9487 1.0118 0.9273 0.0388  0.0032  0.0001  23  ILE C C   
8788  O O   . ILE C 23  ? 0.9828 1.0450 0.9565 0.0405  0.0020  -0.0012 23  ILE C O   
8789  C CB  . ILE C 23  ? 0.9670 1.0425 0.9459 0.0466  0.0012  -0.0038 23  ILE C CB  
8790  C CG1 . ILE C 23  ? 0.9313 1.0010 0.9060 0.0525  -0.0036 -0.0038 23  ILE C CG1 
8791  C CG2 . ILE C 23  ? 0.9523 1.0390 0.9348 0.0399  0.0049  -0.0040 23  ILE C CG2 
8792  C CD1 . ILE C 23  ? 0.9563 1.0109 0.9252 0.0477  -0.0031 -0.0002 23  ILE C CD1 
8804  N N   . ASP C 24  ? 0.9768 1.0388 0.9583 0.0335  0.0058  0.0022  24  ASP C N   
8805  C CA  . ASP C 24  ? 0.9409 0.9981 0.9197 0.0304  0.0057  0.0041  24  ASP C CA  
8806  C C   . ASP C 24  ? 0.9232 0.9854 0.8967 0.0247  0.0106  0.0036  24  ASP C C   
8807  O O   . ASP C 24  ? 0.9318 1.0013 0.9080 0.0221  0.0138  0.0021  24  ASP C O   
8808  C CB  . ASP C 24  ? 0.9260 0.9748 0.9125 0.0298  0.0045  0.0064  24  ASP C CB  
8809  C CG  . ASP C 24  ? 0.9529 0.9939 0.9384 0.0313  -0.0017 0.0086  24  ASP C CG  
8810  O OD1 . ASP C 24  ? 0.9991 1.0379 0.9735 0.0314  -0.0045 0.0087  24  ASP C OD1 
8811  O OD2 . ASP C 24  ? 1.0169 1.0538 1.0126 0.0326  -0.0041 0.0096  24  ASP C OD2 
8816  N N   . ASN C 25  ? 0.9265 0.9831 0.8900 0.0215  0.0110  0.0047  25  ASN C N   
8817  C CA  . ASN C 25  ? 0.8913 0.9478 0.8464 0.0133  0.0166  0.0046  25  ASN C CA  
8818  C C   . ASN C 25  ? 0.8747 0.9510 0.8335 0.0101  0.0221  -0.0006 25  ASN C C   
8819  O O   . ASN C 25  ? 0.8940 0.9753 0.8518 0.0022  0.0269  -0.0020 25  ASN C O   
8820  C CB  . ASN C 25  ? 0.9101 0.9569 0.8667 0.0103  0.0177  0.0070  25  ASN C CB  
8821  C CG  . ASN C 25  ? 0.9579 0.9891 0.9165 0.0154  0.0119  0.0108  25  ASN C CG  
8822  O OD1 . ASN C 25  ? 0.9222 0.9526 0.8926 0.0188  0.0116  0.0106  25  ASN C OD1 
8823  N ND2 . ASN C 25  ? 0.9654 0.9845 0.9125 0.0157  0.0073  0.0138  25  ASN C ND2 
8830  N N   . PHE C 26  ? 0.8887 0.9765 0.8529 0.0165  0.0209  -0.0043 26  PHE C N   
8831  C CA  . PHE C 26  ? 0.9237 1.0339 0.8964 0.0166  0.0246  -0.0104 26  PHE C CA  
8832  C C   . PHE C 26  ? 0.9400 1.0558 0.9071 0.0156  0.0300  -0.0148 26  PHE C C   
8833  O O   . PHE C 26  ? 0.9511 1.0520 0.9066 0.0176  0.0284  -0.0129 26  PHE C O   
8834  C CB  . PHE C 26  ? 0.9114 1.0287 0.8948 0.0270  0.0186  -0.0119 26  PHE C CB  
8835  C CG  . PHE C 26  ? 0.8850 1.0260 0.8807 0.0284  0.0188  -0.0175 26  PHE C CG  
8836  C CD1 . PHE C 26  ? 0.9371 1.0844 0.9365 0.0227  0.0176  -0.0172 26  PHE C CD1 
8837  C CD2 . PHE C 26  ? 0.9323 1.0895 0.9365 0.0359  0.0195  -0.0239 26  PHE C CD2 
8838  C CE1 . PHE C 26  ? 0.9420 1.1131 0.9542 0.0240  0.0153  -0.0227 26  PHE C CE1 
8839  C CE2 . PHE C 26  ? 0.9407 1.1232 0.9607 0.0389  0.0179  -0.0299 26  PHE C CE2 
8840  C CZ  . PHE C 26  ? 0.9901 1.1804 1.0145 0.0327  0.0148  -0.0290 26  PHE C CZ  
8850  N N   . ASP C 27  ? 0.9292 1.0672 0.9044 0.0115  0.0367  -0.0215 27  ASP C N   
8851  C CA  . ASP C 27  ? 0.9256 1.0731 0.8980 0.0101  0.0448  -0.0280 27  ASP C CA  
8852  C C   . ASP C 27  ? 0.9863 1.1368 0.9652 0.0246  0.0407  -0.0316 27  ASP C C   
8853  O O   . ASP C 27  ? 0.9916 1.1600 0.9884 0.0339  0.0374  -0.0359 27  ASP C O   
8854  C CB  . ASP C 27  ? 0.9407 1.1165 0.9263 0.0018  0.0537  -0.0359 27  ASP C CB  
8855  C CG  . ASP C 27  ? 1.0372 1.2281 1.0246 0.0009  0.0646  -0.0451 27  ASP C CG  
8856  O OD1 . ASP C 27  ? 1.0091 1.1826 0.9800 0.0037  0.0664  -0.0445 27  ASP C OD1 
8857  O OD2 . ASP C 27  ? 1.0871 1.3085 1.0930 -0.0033 0.0718  -0.0540 27  ASP C OD2 
8862  N N   . ILE C 28  ? 0.9734 1.1037 0.9359 0.0267  0.0398  -0.0296 28  ILE C N   
8863  C CA  . ILE C 28  ? 0.9511 1.0769 0.9152 0.0395  0.0353  -0.0323 28  ILE C CA  
8864  C C   . ILE C 28  ? 0.9880 1.1329 0.9609 0.0454  0.0432  -0.0430 28  ILE C C   
8865  O O   . ILE C 28  ? 1.0055 1.1449 0.9785 0.0570  0.0403  -0.0464 28  ILE C O   
8866  C CB  . ILE C 28  ? 0.9878 1.0861 0.9308 0.0381  0.0311  -0.0277 28  ILE C CB  
8867  C CG1 . ILE C 28  ? 0.9846 1.0781 0.9096 0.0318  0.0401  -0.0323 28  ILE C CG1 
8868  C CG2 . ILE C 28  ? 0.9698 1.0529 0.9069 0.0315  0.0248  -0.0184 28  ILE C CG2 
8869  C CD1 . ILE C 28  ? 0.9694 1.0349 0.8699 0.0281  0.0343  -0.0273 28  ILE C CD1 
8881  N N   . TYR C 29  ? 0.9847 1.1517 0.9657 0.0377  0.0536  -0.0492 29  TYR C N   
8882  C CA  . TYR C 29  ? 0.9729 1.1649 0.9688 0.0432  0.0630  -0.0615 29  TYR C CA  
8883  C C   . TYR C 29  ? 1.0053 1.2322 1.0304 0.0442  0.0632  -0.0668 29  TYR C C   
8884  O O   . TYR C 29  ? 0.9981 1.2532 1.0385 0.0403  0.0745  -0.0773 29  TYR C O   
8885  C CB  . TYR C 29  ? 1.0016 1.1908 0.9802 0.0308  0.0782  -0.0668 29  TYR C CB  
8886  C CG  . TYR C 29  ? 0.9880 1.1442 0.9367 0.0307  0.0770  -0.0634 29  TYR C CG  
8887  C CD1 . TYR C 29  ? 0.9969 1.1425 0.9446 0.0452  0.0712  -0.0657 29  TYR C CD1 
8888  C CD2 . TYR C 29  ? 0.9636 1.0966 0.8825 0.0158  0.0806  -0.0579 29  TYR C CD2 
8889  C CE1 . TYR C 29  ? 0.9911 1.1068 0.9108 0.0436  0.0691  -0.0633 29  TYR C CE1 
8890  C CE2 . TYR C 29  ? 0.9993 1.1024 0.8900 0.0154  0.0771  -0.0550 29  TYR C CE2 
8891  C CZ  . TYR C 29  ? 1.0060 1.1019 0.8981 0.0288  0.0715  -0.0580 29  TYR C CZ  
8892  O OH  . TYR C 29  ? 0.9714 1.0378 0.8349 0.0269  0.0672  -0.0557 29  TYR C OH  
8902  N N   . ASP C 30  ? 1.0007 1.2266 1.0339 0.0486  0.0507  -0.0604 30  ASP C N   
8903  C CA  . ASP C 30  ? 1.0160 1.2726 1.0749 0.0503  0.0470  -0.0648 30  ASP C CA  
8904  C C   . ASP C 30  ? 1.0156 1.2906 1.0959 0.0699  0.0414  -0.0728 30  ASP C C   
8905  O O   . ASP C 30  ? 1.0228 1.2769 1.0944 0.0836  0.0341  -0.0701 30  ASP C O   
8906  C CB  . ASP C 30  ? 1.0770 1.3208 1.1310 0.0474  0.0356  -0.0549 30  ASP C CB  
8907  C CG  . ASP C 30  ? 1.0376 1.3087 1.1094 0.0397  0.0343  -0.0583 30  ASP C CG  
8908  O OD1 . ASP C 30  ? 1.0187 1.3102 1.1101 0.0506  0.0252  -0.0625 30  ASP C OD1 
8909  O OD2 . ASP C 30  ? 1.0835 1.3535 1.1479 0.0225  0.0413  -0.0566 30  ASP C OD2 
8914  N N   . LYS C 31  ? 1.0160 1.3301 1.1250 0.0713  0.0444  -0.0832 31  LYS C N   
8915  C CA  . LYS C 31  ? 1.0324 1.3663 1.1656 0.0925  0.0367  -0.0913 31  LYS C CA  
8916  C C   . LYS C 31  ? 0.9991 1.3153 1.1275 0.1049  0.0169  -0.0825 31  LYS C C   
8917  O O   . LYS C 31  ? 1.0033 1.3082 1.1317 0.1239  0.0084  -0.0833 31  LYS C O   
8918  C CB  . LYS C 31  ? 1.0470 1.4311 1.2167 0.0907  0.0418  -0.1044 31  LYS C CB  
8919  C CG  . LYS C 31  ? 1.0782 1.4866 1.2776 0.1126  0.0262  -0.1103 31  LYS C CG  
8920  C CD  . LYS C 31  ? 1.1052 1.5656 1.3424 0.1067  0.0267  -0.1211 31  LYS C CD  
8921  C CE  . LYS C 31  ? 1.1532 1.6353 1.4180 0.1289  0.0058  -0.1249 31  LYS C CE  
8922  N NZ  . LYS C 31  ? 1.1515 1.6064 1.4068 0.1547  -0.0044 -0.1226 31  LYS C NZ  
8936  N N   . ASN C 32  ? 1.0089 1.3200 1.1306 0.0938  0.0102  -0.0744 32  ASN C N   
8937  C CA  . ASN C 32  ? 1.0041 1.2987 1.1185 0.1024  -0.0072 -0.0665 32  ASN C CA  
8938  C C   . ASN C 32  ? 0.9988 1.2491 1.0838 0.1056  -0.0107 -0.0563 32  ASN C C   
8939  O O   . ASN C 32  ? 1.0022 1.2335 1.0760 0.1109  -0.0231 -0.0494 32  ASN C O   
8940  C CB  . ASN C 32  ? 1.0328 1.3347 1.1467 0.0872  -0.0109 -0.0624 32  ASN C CB  
8941  C CG  . ASN C 32  ? 1.0330 1.3802 1.1769 0.0814  -0.0085 -0.0729 32  ASN C CG  
8942  O OD1 . ASN C 32  ? 1.0504 1.4254 1.2198 0.0957  -0.0167 -0.0809 32  ASN C OD1 
8943  N ND2 . ASN C 32  ? 1.0388 1.3936 1.1804 0.0604  0.0024  -0.0733 32  ASN C ND2 
8950  N N   . ILE C 33  ? 1.0320 1.2654 1.1034 0.1015  -0.0002 -0.0556 33  ILE C N   
8951  C CA  . ILE C 33  ? 1.0309 1.2257 1.0774 0.1028  -0.0036 -0.0470 33  ILE C CA  
8952  C C   . ILE C 33  ? 1.0161 1.1946 1.0582 0.1202  -0.0157 -0.0460 33  ILE C C   
8953  O O   . ILE C 33  ? 1.0016 1.1554 1.0275 0.1190  -0.0236 -0.0376 33  ILE C O   
8954  C CB  . ILE C 33  ? 0.9832 1.1658 1.0177 0.0973  0.0074  -0.0483 33  ILE C CB  
8955  C CG1 . ILE C 33  ? 1.0074 1.1894 1.0346 0.0787  0.0151  -0.0440 33  ILE C CG1 
8956  C CG2 . ILE C 33  ? 0.9826 1.1312 0.9976 0.1036  0.0024  -0.0435 33  ILE C CG2 
8957  C CD1 . ILE C 33  ? 0.9930 1.1470 0.9990 0.0722  0.0175  -0.0382 33  ILE C CD1 
8969  N N   . PRO C 34  ? 0.9869 1.1751 1.0406 0.1365  -0.0172 -0.0543 34  PRO C N   
8970  C CA  . PRO C 34  ? 1.0242 1.1908 1.0697 0.1541  -0.0303 -0.0524 34  PRO C CA  
8971  C C   . PRO C 34  ? 1.0503 1.2131 1.0928 0.1562  -0.0450 -0.0460 34  PRO C C   
8972  O O   . PRO C 34  ? 1.0251 1.1531 1.0438 0.1583  -0.0531 -0.0380 34  PRO C O   
8973  C CB  . PRO C 34  ? 1.0062 1.1954 1.0737 0.1718  -0.0289 -0.0649 34  PRO C CB  
8974  C CG  . PRO C 34  ? 0.9848 1.1906 1.0588 0.1615  -0.0111 -0.0719 34  PRO C CG  
8975  C CD  . PRO C 34  ? 1.0071 1.2194 1.0769 0.1391  -0.0051 -0.0657 34  PRO C CD  
8983  N N   . LYS C 35  ? 1.0665 1.2631 1.1307 0.1542  -0.0485 -0.0497 35  LYS C N   
8984  C CA  . LYS C 35  ? 1.0430 1.2355 1.1018 0.1558  -0.0639 -0.0441 35  LYS C CA  
8985  C C   . LYS C 35  ? 1.0146 1.1813 1.0482 0.1380  -0.0615 -0.0336 35  LYS C C   
8986  O O   . LYS C 35  ? 1.0341 1.1747 1.0468 0.1395  -0.0722 -0.0264 35  LYS C O   
8987  C CB  . LYS C 35  ? 1.0537 1.2913 1.1430 0.1555  -0.0680 -0.0516 35  LYS C CB  
8988  C CG  . LYS C 35  ? 1.1167 1.3614 1.2148 0.1742  -0.0889 -0.0533 35  LYS C CG  
8989  C CD  . LYS C 35  ? 1.1430 1.3861 1.2514 0.1984  -0.0929 -0.0600 35  LYS C CD  
8990  C CE  . LYS C 35  ? 1.1689 1.4404 1.3039 0.2181  -0.1115 -0.0668 35  LYS C CE  
8991  N NZ  . LYS C 35  ? 1.2790 1.5264 1.4074 0.2447  -0.1234 -0.0678 35  LYS C NZ  
9005  N N   . LEU C 36  ? 0.9937 1.1660 1.0281 0.1213  -0.0475 -0.0330 36  LEU C N   
9006  C CA  . LEU C 36  ? 1.0056 1.1547 1.0197 0.1063  -0.0441 -0.0245 36  LEU C CA  
9007  C C   . LEU C 36  ? 1.0200 1.1309 1.0107 0.1089  -0.0448 -0.0184 36  LEU C C   
9008  O O   . LEU C 36  ? 1.0610 1.1484 1.0326 0.1028  -0.0478 -0.0117 36  LEU C O   
9009  C CB  . LEU C 36  ? 1.0243 1.1846 1.0441 0.0908  -0.0301 -0.0254 36  LEU C CB  
9010  C CG  . LEU C 36  ? 1.0312 1.2233 1.0683 0.0815  -0.0268 -0.0304 36  LEU C CG  
9011  C CD1 . LEU C 36  ? 1.0491 1.2379 1.0814 0.0654  -0.0140 -0.0285 36  LEU C CD1 
9012  C CD2 . LEU C 36  ? 1.0282 1.2237 1.0632 0.0789  -0.0374 -0.0284 36  LEU C CD2 
9024  N N   . SER C 37  ? 1.0179 1.1216 1.0085 0.1164  -0.0410 -0.0213 37  SER C N   
9025  C CA  . SER C 37  ? 1.0407 1.1085 1.0093 0.1174  -0.0418 -0.0164 37  SER C CA  
9026  C C   . SER C 37  ? 1.0475 1.0919 0.9995 0.1280  -0.0547 -0.0129 37  SER C C   
9027  O O   . SER C 37  ? 1.0482 1.0608 0.9769 0.1221  -0.0559 -0.0064 37  SER C O   
9028  C CB  . SER C 37  ? 1.0256 1.0901 0.9959 0.1232  -0.0361 -0.0215 37  SER C CB  
9029  O OG  . SER C 37  ? 1.0578 1.1394 1.0379 0.1129  -0.0252 -0.0240 37  SER C OG  
9035  N N   . GLU C 38  ? 1.0418 1.1011 1.0052 0.1434  -0.0648 -0.0173 38  GLU C N   
9036  C CA  . GLU C 38  ? 1.0747 1.1087 1.0199 0.1559  -0.0800 -0.0135 38  GLU C CA  
9037  C C   . GLU C 38  ? 1.0771 1.0958 1.0027 0.1447  -0.0855 -0.0056 38  GLU C C   
9038  O O   . GLU C 38  ? 1.0719 1.0516 0.9668 0.1432  -0.0901 0.0012  38  GLU C O   
9039  C CB  . GLU C 38  ? 1.1035 1.1629 1.0709 0.1758  -0.0912 -0.0208 38  GLU C CB  
9040  C CG  . GLU C 38  ? 1.1632 1.1925 1.1148 0.1962  -0.1043 -0.0201 38  GLU C CG  
9041  C CD  . GLU C 38  ? 1.1686 1.2140 1.1330 0.2143  -0.1233 -0.0227 38  GLU C CD  
9042  O OE1 . GLU C 38  ? 1.1444 1.2347 1.1398 0.2131  -0.1240 -0.0287 38  GLU C OE1 
9043  O OE2 . GLU C 38  ? 1.2806 1.2927 1.2232 0.2295  -0.1384 -0.0187 38  GLU C OE2 
9050  N N   . GLU C 39  ? 1.0541 1.1010 0.9942 0.1353  -0.0840 -0.0068 39  GLU C N   
9051  C CA  . GLU C 39  ? 1.1172 1.1492 1.0369 0.1241  -0.0884 -0.0005 39  GLU C CA  
9052  C C   . GLU C 39  ? 1.0791 1.0854 0.9795 0.1072  -0.0752 0.0049  39  GLU C C   
9053  O O   . GLU C 39  ? 1.0854 1.0613 0.9574 0.1006  -0.0777 0.0108  39  GLU C O   
9054  C CB  . GLU C 39  ? 1.1264 1.1942 1.0662 0.1170  -0.0891 -0.0042 39  GLU C CB  
9055  C CG  . GLU C 39  ? 1.2729 1.3381 1.2015 0.1207  -0.1067 -0.0021 39  GLU C CG  
9056  C CD  . GLU C 39  ? 1.3875 1.4906 1.3380 0.1126  -0.1079 -0.0072 39  GLU C CD  
9057  O OE1 . GLU C 39  ? 1.3879 1.4880 1.3298 0.0949  -0.0989 -0.0053 39  GLU C OE1 
9058  O OE2 . GLU C 39  ? 1.4215 1.5578 1.3987 0.1239  -0.1175 -0.0140 39  GLU C OE2 
9065  N N   . ILE C 40  ? 1.0314 1.0494 0.9464 0.0999  -0.0613 0.0023  40  ILE C N   
9066  C CA  . ILE C 40  ? 1.0220 1.0216 0.9255 0.0852  -0.0496 0.0060  40  ILE C CA  
9067  C C   . ILE C 40  ? 1.0534 1.0162 0.9328 0.0863  -0.0506 0.0098  40  ILE C C   
9068  O O   . ILE C 40  ? 1.0477 0.9906 0.9124 0.0736  -0.0431 0.0131  40  ILE C O   
9069  C CB  . ILE C 40  ? 1.0578 1.0775 0.9823 0.0793  -0.0379 0.0025  40  ILE C CB  
9070  C CG1 . ILE C 40  ? 1.0574 1.1051 0.9983 0.0727  -0.0344 0.0000  40  ILE C CG1 
9071  C CG2 . ILE C 40  ? 1.0665 1.0679 0.9833 0.0681  -0.0283 0.0053  40  ILE C CG2 
9072  C CD1 . ILE C 40  ? 1.0879 1.1495 1.0436 0.0657  -0.0236 -0.0021 40  ILE C CD1 
9084  N N   . MET C 41  ? 1.0757 1.0283 0.9510 0.1008  -0.0587 0.0086  41  MET C N   
9085  C CA  . MET C 41  ? 1.0922 1.0069 0.9429 0.1008  -0.0588 0.0117  41  MET C CA  
9086  C C   . MET C 41  ? 1.1285 1.0075 0.9453 0.1013  -0.0682 0.0180  41  MET C C   
9087  O O   . MET C 41  ? 1.1408 0.9833 0.9312 0.0951  -0.0656 0.0216  41  MET C O   
9088  C CB  . MET C 41  ? 1.0992 1.0127 0.9562 0.1162  -0.0627 0.0072  41  MET C CB  
9089  C CG  . MET C 41  ? 1.0833 1.0057 0.9534 0.1100  -0.0514 0.0034  41  MET C CG  
9090  S SD  . MET C 41  ? 1.1660 1.0898 1.0435 0.1271  -0.0535 -0.0040 41  MET C SD  
9091  C CE  . MET C 41  ? 1.0948 1.0442 0.9894 0.1470  -0.0646 -0.0082 41  MET C CE  
9101  N N   . LYS C 42  ? 1.1463 1.0334 0.9609 0.1070  -0.0793 0.0193  42  LYS C N   
9102  C CA  . LYS C 42  ? 1.1786 1.0284 0.9564 0.1089  -0.0910 0.0257  42  LYS C CA  
9103  C C   . LYS C 42  ? 1.1912 1.0105 0.9401 0.0879  -0.0795 0.0307  42  LYS C C   
9104  O O   . LYS C 42  ? 1.1587 0.9945 0.9216 0.0729  -0.0644 0.0286  42  LYS C O   
9105  C CB  . LYS C 42  ? 1.1336 1.0018 0.9158 0.1156  -0.1052 0.0258  42  LYS C CB  
9106  C CG  . LYS C 42  ? 1.1155 1.0134 0.9258 0.1374  -0.1184 0.0202  42  LYS C CG  
9107  C CD  . LYS C 42  ? 1.1988 1.1171 1.0149 0.1415  -0.1333 0.0198  42  LYS C CD  
9108  C CE  . LYS C 42  ? 1.2216 1.1827 1.0772 0.1602  -0.1428 0.0114  42  LYS C CE  
9109  N NZ  . LYS C 42  ? 1.2480 1.2187 1.1029 0.1699  -0.1648 0.0118  42  LYS C NZ  
9123  N N   . GLU C 43  ? 1.2248 0.9976 0.9320 0.0873  -0.0866 0.0369  43  GLU C N   
9124  C CA  . GLU C 43  ? 1.2876 1.0286 0.9622 0.0664  -0.0756 0.0412  43  GLU C CA  
9125  C C   . GLU C 43  ? 1.2639 1.0149 0.9326 0.0577  -0.0760 0.0422  43  GLU C C   
9126  O O   . GLU C 43  ? 1.2500 0.9937 0.9086 0.0385  -0.0605 0.0421  43  GLU C O   
9127  C CB  . GLU C 43  ? 1.3742 1.0579 0.9998 0.0674  -0.0836 0.0480  43  GLU C CB  
9128  C CG  . GLU C 43  ? 1.4391 1.0850 1.0267 0.0432  -0.0693 0.0518  43  GLU C CG  
9129  C CD  . GLU C 43  ? 1.5282 1.1217 1.0592 0.0427  -0.0824 0.0602  43  GLU C CD  
9130  O OE1 . GLU C 43  ? 1.5155 1.1056 1.0396 0.0622  -0.1048 0.0633  43  GLU C OE1 
9131  O OE2 . GLU C 43  ? 1.5348 1.0898 1.0271 0.0224  -0.0705 0.0636  43  GLU C OE2 
9138  N N   . THR C 44  ? 1.2493 1.0174 0.9250 0.0713  -0.0934 0.0422  44  THR C N   
9139  C CA  . THR C 44  ? 1.2150 0.9971 0.8885 0.0633  -0.0954 0.0419  44  THR C CA  
9140  C C   . THR C 44  ? 1.1748 1.0033 0.8901 0.0567  -0.0820 0.0351  44  THR C C   
9141  O O   . THR C 44  ? 1.1639 1.0062 0.8803 0.0494  -0.0822 0.0336  44  THR C O   
9142  C CB  . THR C 44  ? 1.1673 0.9533 0.8355 0.0801  -0.1209 0.0436  44  THR C CB  
9143  O OG1 . THR C 44  ? 1.2599 1.0817 0.9681 0.0997  -0.1293 0.0384  44  THR C OG1 
9144  C CG2 . THR C 44  ? 1.2862 1.0182 0.9043 0.0855  -0.1359 0.0518  44  THR C CG2 
9152  N N   . ASN C 45  ? 1.1660 1.0156 0.9122 0.0585  -0.0709 0.0310  45  ASN C N   
9153  C CA  . ASN C 45  ? 1.1094 0.9957 0.8904 0.0515  -0.0576 0.0255  45  ASN C CA  
9154  C C   . ASN C 45  ? 1.0815 0.9583 0.8646 0.0391  -0.0393 0.0248  45  ASN C C   
9155  O O   . ASN C 45  ? 1.1770 1.0199 0.9323 0.0313  -0.0348 0.0280  45  ASN C O   
9156  C CB  . ASN C 45  ? 1.0900 1.0127 0.9071 0.0657  -0.0630 0.0207  45  ASN C CB  
9157  C CG  . ASN C 45  ? 1.0727 1.0319 0.9178 0.0597  -0.0562 0.0160  45  ASN C CG  
9158  O OD1 . ASN C 45  ? 0.9581 0.9306 0.8219 0.0540  -0.0434 0.0135  45  ASN C OD1 
9159  N ND2 . ASN C 45  ? 1.0712 1.0452 0.9179 0.0608  -0.0658 0.0148  45  ASN C ND2 
9166  N N   . LEU C 46  ? 1.1195 1.0251 0.9345 0.0365  -0.0291 0.0203  46  LEU C N   
9167  C CA  . LEU C 46  ? 1.0738 0.9761 0.8982 0.0299  -0.0167 0.0189  46  LEU C CA  
9168  C C   . LEU C 46  ? 1.1012 0.9870 0.9175 0.0390  -0.0235 0.0204  46  LEU C C   
9169  O O   . LEU C 46  ? 1.1525 1.0494 0.9781 0.0536  -0.0341 0.0194  46  LEU C O   
9170  C CB  . LEU C 46  ? 1.0127 0.9479 0.8716 0.0298  -0.0098 0.0146  46  LEU C CB  
9171  C CG  . LEU C 46  ? 1.0149 0.9516 0.8861 0.0191  0.0042  0.0124  46  LEU C CG  
9172  C CD1 . LEU C 46  ? 1.0427 0.9699 0.9035 0.0061  0.0151  0.0117  46  LEU C CD1 
9173  C CD2 . LEU C 46  ? 0.9676 0.9324 0.8691 0.0223  0.0064  0.0094  46  LEU C CD2 
9185  N N   . TYR C 47  ? 1.1239 0.9823 0.9224 0.0301  -0.0170 0.0219  47  TYR C N   
9186  C CA  . TYR C 47  ? 1.1627 0.9993 0.9485 0.0379  -0.0237 0.0232  47  TYR C CA  
9187  C C   . TYR C 47  ? 1.0784 0.9355 0.8918 0.0411  -0.0202 0.0188  47  TYR C C   
9188  O O   . TYR C 47  ? 1.0298 0.9078 0.8656 0.0326  -0.0104 0.0158  47  TYR C O   
9189  C CB  . TYR C 47  ? 1.1868 0.9821 0.9385 0.0251  -0.0181 0.0265  47  TYR C CB  
9190  C CG  . TYR C 47  ? 1.2926 1.0515 1.0148 0.0348  -0.0297 0.0302  47  TYR C CG  
9191  C CD1 . TYR C 47  ? 1.2852 1.0482 1.0093 0.0557  -0.0460 0.0309  47  TYR C CD1 
9192  C CD2 . TYR C 47  ? 1.4085 1.1282 1.1013 0.0228  -0.0239 0.0323  47  TYR C CD2 
9193  C CE1 . TYR C 47  ? 1.3632 1.0907 1.0606 0.0669  -0.0572 0.0338  47  TYR C CE1 
9194  C CE2 . TYR C 47  ? 1.4545 1.1350 1.1163 0.0318  -0.0346 0.0360  47  TYR C CE2 
9195  C CZ  . TYR C 47  ? 1.4686 1.1523 1.1327 0.0550  -0.0518 0.0368  47  TYR C CZ  
9196  O OH  . TYR C 47  ? 1.5960 1.2388 1.2297 0.0664  -0.0633 0.0400  47  TYR C OH  
9206  N N   . ALA C 48  ? 1.1021 0.9515 0.9123 0.0542  -0.0290 0.0181  48  ALA C N   
9207  C CA  . ALA C 48  ? 1.1288 0.9935 0.9594 0.0577  -0.0267 0.0136  48  ALA C CA  
9208  C C   . ALA C 48  ? 1.1341 0.9775 0.9503 0.0713  -0.0356 0.0129  48  ALA C C   
9209  O O   . ALA C 48  ? 1.1529 0.9841 0.9554 0.0842  -0.0460 0.0148  48  ALA C O   
9210  C CB  . ALA C 48  ? 1.0400 0.9448 0.9012 0.0633  -0.0262 0.0101  48  ALA C CB  
9216  N N   . GLU C 49  ? 1.0983 0.9371 0.9180 0.0689  -0.0321 0.0095  49  GLU C N   
9217  C CA  . GLU C 49  ? 1.1174 0.9388 0.9268 0.0822  -0.0385 0.0068  49  GLU C CA  
9218  C C   . GLU C 49  ? 1.0777 0.9300 0.9119 0.0933  -0.0388 0.0006  49  GLU C C   
9219  O O   . GLU C 49  ? 1.0798 0.9241 0.9096 0.1083  -0.0441 -0.0030 49  GLU C O   
9220  C CB  . GLU C 49  ? 1.1672 0.9583 0.9589 0.0709  -0.0344 0.0061  49  GLU C CB  
9221  C CG  . GLU C 49  ? 1.2360 0.9877 0.9956 0.0602  -0.0335 0.0114  49  GLU C CG  
9222  C CD  . GLU C 49  ? 1.3256 1.0460 1.0667 0.0482  -0.0294 0.0098  49  GLU C CD  
9223  O OE1 . GLU C 49  ? 1.3793 1.0932 1.1197 0.0561  -0.0325 0.0054  49  GLU C OE1 
9224  O OE2 . GLU C 49  ? 1.3700 1.0721 1.0966 0.0296  -0.0220 0.0121  49  GLU C OE2 
9231  N N   . GLN C 50  ? 1.0327 0.9177 0.8910 0.0861  -0.0327 -0.0009 50  GLN C N   
9232  C CA  . GLN C 50  ? 1.0494 0.9611 0.9269 0.0933  -0.0313 -0.0064 50  GLN C CA  
9233  C C   . GLN C 50  ? 1.0190 0.9619 0.9175 0.0850  -0.0262 -0.0055 50  GLN C C   
9234  O O   . GLN C 50  ? 1.0004 0.9428 0.9003 0.0727  -0.0225 -0.0019 50  GLN C O   
9235  C CB  . GLN C 50  ? 1.0135 0.9142 0.8860 0.0902  -0.0288 -0.0104 50  GLN C CB  
9236  C CG  . GLN C 50  ? 1.0229 0.9248 0.8996 0.0729  -0.0243 -0.0088 50  GLN C CG  
9237  C CD  . GLN C 50  ? 1.0779 0.9662 0.9466 0.0689  -0.0244 -0.0129 50  GLN C CD  
9238  O OE1 . GLN C 50  ? 1.0643 0.9448 0.9250 0.0790  -0.0259 -0.0176 50  GLN C OE1 
9239  N NE2 . GLN C 50  ? 1.1031 0.9895 0.9749 0.0539  -0.0226 -0.0120 50  GLN C NE2 
9248  N N   . VAL C 51  ? 1.0190 0.9877 0.9330 0.0915  -0.0251 -0.0094 51  VAL C N   
9249  C CA  . VAL C 51  ? 1.0203 1.0154 0.9510 0.0845  -0.0206 -0.0086 51  VAL C CA  
9250  C C   . VAL C 51  ? 0.9851 0.9934 0.9235 0.0830  -0.0162 -0.0126 51  VAL C C   
9251  O O   . VAL C 51  ? 0.9825 0.9912 0.9188 0.0914  -0.0160 -0.0179 51  VAL C O   
9252  C CB  . VAL C 51  ? 1.0264 1.0401 0.9659 0.0908  -0.0234 -0.0091 51  VAL C CB  
9253  C CG1 . VAL C 51  ? 0.9653 1.0071 0.9215 0.0853  -0.0179 -0.0110 51  VAL C CG1 
9254  C CG2 . VAL C 51  ? 0.9991 1.0002 0.9287 0.0867  -0.0269 -0.0038 51  VAL C CG2 
9264  N N   . GLY C 52  ? 0.9724 0.9896 0.9178 0.0725  -0.0127 -0.0103 52  GLY C N   
9265  C CA  . GLY C 52  ? 0.9578 0.9841 0.9057 0.0696  -0.0096 -0.0127 52  GLY C CA  
9266  C C   . GLY C 52  ? 0.9449 0.9894 0.9028 0.0639  -0.0059 -0.0110 52  GLY C C   
9267  O O   . GLY C 52  ? 0.9921 1.0413 0.9558 0.0609  -0.0057 -0.0080 52  GLY C O   
9271  N N   . PHE C 53  ? 0.9590 1.0105 0.9153 0.0615  -0.0025 -0.0132 53  PHE C N   
9272  C CA  . PHE C 53  ? 0.9914 1.0558 0.9524 0.0550  0.0017  -0.0120 53  PHE C CA  
9273  C C   . PHE C 53  ? 1.0000 1.0558 0.9518 0.0486  0.0014  -0.0101 53  PHE C C   
9274  O O   . PHE C 53  ? 0.9940 1.0446 0.9349 0.0494  0.0024  -0.0134 53  PHE C O   
9275  C CB  . PHE C 53  ? 0.9946 1.0781 0.9611 0.0579  0.0072  -0.0176 53  PHE C CB  
9276  C CG  . PHE C 53  ? 0.9584 1.0529 0.9356 0.0643  0.0047  -0.0189 53  PHE C CG  
9277  C CD1 . PHE C 53  ? 0.9260 1.0157 0.9028 0.0757  0.0003  -0.0217 53  PHE C CD1 
9278  C CD2 . PHE C 53  ? 0.9620 1.0684 0.9468 0.0590  0.0054  -0.0172 53  PHE C CD2 
9279  C CE1 . PHE C 53  ? 0.9741 1.0711 0.9579 0.0826  -0.0047 -0.0222 53  PHE C CE1 
9280  C CE2 . PHE C 53  ? 0.9714 1.0868 0.9635 0.0645  0.0009  -0.0182 53  PHE C CE2 
9281  C CZ  . PHE C 53  ? 1.0145 1.1252 1.0061 0.0767  -0.0050 -0.0204 53  PHE C CZ  
9291  N N   . ILE C 54  ? 1.0936 1.1463 1.0482 0.0428  -0.0004 -0.0051 54  ILE C N   
9292  C CA  . ILE C 54  ? 1.0735 1.1149 1.0200 0.0385  -0.0047 -0.0021 54  ILE C CA  
9293  C C   . ILE C 54  ? 1.0485 1.0901 0.9842 0.0328  -0.0004 -0.0013 54  ILE C C   
9294  O O   . ILE C 54  ? 1.0816 1.1329 1.0213 0.0299  0.0058  -0.0018 54  ILE C O   
9295  C CB  . ILE C 54  ? 1.0488 1.0861 1.0066 0.0373  -0.0098 0.0021  54  ILE C CB  
9296  C CG1 . ILE C 54  ? 1.0617 1.0934 1.0240 0.0391  -0.0151 0.0011  54  ILE C CG1 
9297  C CG2 . ILE C 54  ? 1.1214 1.1510 1.0746 0.0341  -0.0142 0.0060  54  ILE C CG2 
9298  C CD1 . ILE C 54  ? 1.0158 1.0491 0.9944 0.0374  -0.0164 0.0029  54  ILE C CD1 
9310  N N   . LYS C 55  ? 1.0359 1.0642 0.9549 0.0299  -0.0040 -0.0001 55  LYS C N   
9311  C CA  . LYS C 55  ? 1.0352 1.0556 0.9375 0.0228  -0.0011 0.0022  55  LYS C CA  
9312  C C   . LYS C 55  ? 1.0378 1.0382 0.9236 0.0215  -0.0117 0.0062  55  LYS C C   
9313  O O   . LYS C 55  ? 1.0611 1.0539 0.9323 0.0212  -0.0136 0.0035  55  LYS C O   
9314  C CB  . LYS C 55  ? 1.0088 1.0370 0.9007 0.0189  0.0104  -0.0037 55  LYS C CB  
9315  C CG  . LYS C 55  ? 1.0483 1.0632 0.9161 0.0086  0.0147  -0.0017 55  LYS C CG  
9316  C CD  . LYS C 55  ? 1.0642 1.0955 0.9331 0.0018  0.0294  -0.0075 55  LYS C CD  
9317  C CE  . LYS C 55  ? 0.9346 0.9514 0.7731 -0.0093 0.0372  -0.0088 55  LYS C CE  
9318  N NZ  . LYS C 55  ? 0.9889 1.0144 0.8252 -0.0211 0.0498  -0.0110 55  LYS C NZ  
9332  N N   . ASP C 56  ? 1.0260 1.0173 0.9143 0.0215  -0.0195 0.0121  56  ASP C N   
9333  C CA  . ASP C 56  ? 1.0600 1.0333 0.9356 0.0220  -0.0332 0.0164  56  ASP C CA  
9334  C C   . ASP C 56  ? 1.0503 1.0283 0.9367 0.0261  -0.0410 0.0136  56  ASP C C   
9335  O O   . ASP C 56  ? 1.0196 1.0107 0.9316 0.0301  -0.0413 0.0123  56  ASP C O   
9336  C CB  . ASP C 56  ? 1.0497 1.0037 0.8898 0.0146  -0.0316 0.0179  56  ASP C CB  
9337  C CG  . ASP C 56  ? 1.1078 1.0386 0.9291 0.0149  -0.0483 0.0237  56  ASP C CG  
9338  O OD1 . ASP C 56  ? 1.1307 1.0635 0.9714 0.0217  -0.0609 0.0267  56  ASP C OD1 
9339  O OD2 . ASP C 56  ? 1.1306 1.0413 0.9174 0.0084  -0.0490 0.0248  56  ASP C OD2 
9344  N N   . SER C 57  ? 1.0520 1.0183 0.9180 0.0239  -0.0464 0.0120  57  SER C N   
9345  C CA  . SER C 57  ? 1.0525 1.0203 0.9257 0.0257  -0.0540 0.0088  57  SER C CA  
9346  C C   . SER C 57  ? 0.9895 0.9609 0.8574 0.0260  -0.0440 0.0019  57  SER C C   
9347  O O   . SER C 57  ? 1.0003 0.9662 0.8649 0.0259  -0.0494 -0.0015 57  SER C O   
9348  C CB  . SER C 57  ? 1.0635 1.0135 0.9165 0.0231  -0.0696 0.0111  57  SER C CB  
9349  O OG  . SER C 57  ? 1.1491 1.0810 0.9668 0.0177  -0.0662 0.0123  57  SER C OG  
9355  N N   . HIS C 58  ? 1.0098 0.9900 0.8779 0.0268  -0.0301 -0.0009 58  HIS C N   
9356  C CA  . HIS C 58  ? 0.9875 0.9725 0.8536 0.0298  -0.0208 -0.0080 58  HIS C CA  
9357  C C   . HIS C 58  ? 1.0137 1.0140 0.9045 0.0358  -0.0166 -0.0092 58  HIS C C   
9358  O O   . HIS C 58  ? 0.9894 1.0003 0.8953 0.0359  -0.0147 -0.0058 58  HIS C O   
9359  C CB  . HIS C 58  ? 0.9523 0.9391 0.8025 0.0268  -0.0082 -0.0120 58  HIS C CB  
9360  C CG  . HIS C 58  ? 1.0175 1.0143 0.8724 0.0326  0.0022  -0.0205 58  HIS C CG  
9361  N ND1 . HIS C 58  ? 1.0589 1.0445 0.9019 0.0357  0.0017  -0.0263 58  HIS C ND1 
9362  C CD2 . HIS C 58  ? 0.9977 1.0145 0.8687 0.0368  0.0123  -0.0247 58  HIS C CD2 
9363  C CE1 . HIS C 58  ? 1.0426 1.0399 0.8945 0.0432  0.0115  -0.0337 58  HIS C CE1 
9364  N NE2 . HIS C 58  ? 1.0171 1.0350 0.8874 0.0442  0.0173  -0.0328 58  HIS C NE2 
9373  N N   . LEU C 59  ? 1.0356 1.0337 0.9269 0.0406  -0.0154 -0.0141 59  LEU C N   
9374  C CA  . LEU C 59  ? 0.9770 0.9837 0.8847 0.0469  -0.0124 -0.0153 59  LEU C CA  
9375  C C   . LEU C 59  ? 0.9986 1.0098 0.9022 0.0539  -0.0042 -0.0223 59  LEU C C   
9376  O O   . LEU C 59  ? 1.0369 1.0365 0.9261 0.0559  -0.0033 -0.0276 59  LEU C O   
9377  C CB  . LEU C 59  ? 0.9711 0.9671 0.8822 0.0466  -0.0196 -0.0146 59  LEU C CB  
9378  C CG  . LEU C 59  ? 0.9586 0.9520 0.8742 0.0529  -0.0172 -0.0168 59  LEU C CG  
9379  C CD1 . LEU C 59  ? 0.9731 0.9806 0.9036 0.0553  -0.0137 -0.0138 59  LEU C CD1 
9380  C CD2 . LEU C 59  ? 0.9685 0.9476 0.8829 0.0487  -0.0232 -0.0162 59  LEU C CD2 
9392  N N   . GLN C 60  ? 1.0097 1.0382 0.9270 0.0579  0.0014  -0.0232 60  GLN C N   
9393  C CA  . GLN C 60  ? 1.0022 1.0415 0.9230 0.0662  0.0085  -0.0307 60  GLN C CA  
9394  C C   . GLN C 60  ? 0.9879 1.0281 0.9198 0.0758  0.0044  -0.0305 60  GLN C C   
9395  O O   . GLN C 60  ? 0.9715 1.0239 0.9164 0.0760  0.0033  -0.0273 60  GLN C O   
9396  C CB  . GLN C 60  ? 0.9519 1.0126 0.8802 0.0624  0.0171  -0.0328 60  GLN C CB  
9397  C CG  . GLN C 60  ? 0.9631 1.0412 0.9004 0.0707  0.0253  -0.0425 60  GLN C CG  
9398  C CD  . GLN C 60  ? 0.9677 1.0379 0.8886 0.0703  0.0330  -0.0500 60  GLN C CD  
9399  O OE1 . GLN C 60  ? 0.9957 1.0446 0.8955 0.0636  0.0303  -0.0472 60  GLN C OE1 
9400  N NE2 . GLN C 60  ? 0.9787 1.0664 0.9095 0.0775  0.0425  -0.0603 60  GLN C NE2 
9409  N N   . MET C 61  ? 0.9727 0.9964 0.8959 0.0831  0.0017  -0.0339 61  MET C N   
9410  C CA  . MET C 61  ? 1.0199 1.0372 0.9471 0.0925  -0.0032 -0.0332 61  MET C CA  
9411  C C   . MET C 61  ? 1.0542 1.0924 0.9960 0.1039  -0.0006 -0.0383 61  MET C C   
9412  O O   . MET C 61  ? 1.0233 1.0790 0.9714 0.1058  0.0070  -0.0452 61  MET C O   
9413  C CB  . MET C 61  ? 1.0661 1.0559 0.9767 0.0973  -0.0064 -0.0359 61  MET C CB  
9414  C CG  . MET C 61  ? 1.0917 1.0632 0.9904 0.0853  -0.0102 -0.0322 61  MET C CG  
9415  S SD  . MET C 61  ? 1.0686 1.0419 0.9772 0.0749  -0.0148 -0.0230 61  MET C SD  
9416  C CE  . MET C 61  ? 1.0544 1.0056 0.9544 0.0810  -0.0185 -0.0217 61  MET C CE  
9426  N N   . MET C 62  ? 1.0327 1.0684 0.9792 0.1109  -0.0073 -0.0354 62  MET C N   
9427  C CA  . MET C 62  ? 1.0229 1.0822 0.9868 0.1203  -0.0085 -0.0387 62  MET C CA  
9428  C C   . MET C 62  ? 1.0049 1.0754 0.9768 0.1343  -0.0046 -0.0493 62  MET C C   
9429  O O   . MET C 62  ? 0.9958 1.0953 0.9883 0.1404  -0.0034 -0.0546 62  MET C O   
9430  C CB  . MET C 62  ? 1.0353 1.0823 0.9959 0.1262  -0.0189 -0.0332 62  MET C CB  
9431  C CG  . MET C 62  ? 1.1032 1.1125 1.0414 0.1273  -0.0240 -0.0291 62  MET C CG  
9432  S SD  . MET C 62  ? 1.0833 1.0717 1.0106 0.1389  -0.0364 -0.0248 62  MET C SD  
9433  C CE  . MET C 62  ? 1.1241 1.1302 1.0672 0.1619  -0.0400 -0.0347 62  MET C CE  
9443  N N   . GLY C 63  ? 1.0432 1.0927 1.0007 0.1392  -0.0023 -0.0537 63  GLY C N   
9444  C CA  . GLY C 63  ? 1.0516 1.1097 1.0163 0.1536  0.0029  -0.0653 63  GLY C CA  
9445  C C   . GLY C 63  ? 1.0769 1.1344 1.0323 0.1470  0.0152  -0.0723 63  GLY C C   
9446  O O   . GLY C 63  ? 1.1062 1.1748 1.0690 0.1569  0.0235  -0.0837 63  GLY C O   
9450  N N   . GLY C 64  ? 1.0857 1.1293 1.0242 0.1305  0.0163  -0.0661 64  GLY C N   
9451  C CA  . GLY C 64  ? 1.0893 1.1250 1.0114 0.1228  0.0254  -0.0713 64  GLY C CA  
9452  C C   . GLY C 64  ? 1.0906 1.0907 0.9878 0.1242  0.0221  -0.0726 64  GLY C C   
9453  O O   . GLY C 64  ? 1.1138 1.1054 0.9970 0.1247  0.0302  -0.0812 64  GLY C O   
9457  N N   . GLU C 65  ? 1.0695 1.0477 0.9592 0.1234  0.0112  -0.0650 65  GLU C N   
9458  C CA  . GLU C 65  ? 1.0824 1.0255 0.9492 0.1243  0.0072  -0.0665 65  GLU C CA  
9459  C C   . GLU C 65  ? 1.0456 0.9742 0.9016 0.1078  0.0000  -0.0577 65  GLU C C   
9460  O O   . GLU C 65  ? 1.0695 1.0111 0.9381 0.1006  -0.0039 -0.0495 65  GLU C O   
9461  C CB  . GLU C 65  ? 1.0611 0.9873 0.9276 0.1400  0.0011  -0.0672 65  GLU C CB  
9462  C CG  . GLU C 65  ? 1.1580 1.0861 1.0337 0.1394  -0.0079 -0.0573 65  GLU C CG  
9463  C CD  . GLU C 65  ? 1.1146 1.0797 1.0157 0.1401  -0.0064 -0.0551 65  GLU C CD  
9464  O OE1 . GLU C 65  ? 1.1452 1.1354 1.0580 0.1404  0.0021  -0.0613 65  GLU C OE1 
9465  O OE2 . GLU C 65  ? 1.0686 1.0360 0.9756 0.1389  -0.0130 -0.0476 65  GLU C OE2 
9472  N N   . PHE C 66  ? 1.0646 0.9671 0.8984 0.1019  -0.0017 -0.0604 66  PHE C N   
9473  C CA  . PHE C 66  ? 1.0576 0.9495 0.8843 0.0862  -0.0093 -0.0539 66  PHE C CA  
9474  C C   . PHE C 66  ? 1.0245 0.9016 0.8527 0.0850  -0.0160 -0.0485 66  PHE C C   
9475  O O   . PHE C 66  ? 1.0413 0.8996 0.8616 0.0951  -0.0163 -0.0509 66  PHE C O   
9476  C CB  . PHE C 66  ? 1.0903 0.9595 0.8919 0.0790  -0.0102 -0.0595 66  PHE C CB  
9477  C CG  . PHE C 66  ? 1.0746 0.9346 0.8713 0.0633  -0.0200 -0.0542 66  PHE C CG  
9478  C CD1 . PHE C 66  ? 1.0919 0.9713 0.9008 0.0538  -0.0244 -0.0478 66  PHE C CD1 
9479  C CD2 . PHE C 66  ? 1.0389 0.8711 0.8199 0.0581  -0.0250 -0.0563 66  PHE C CD2 
9480  C CE1 . PHE C 66  ? 1.0884 0.9636 0.8982 0.0410  -0.0344 -0.0442 66  PHE C CE1 
9481  C CE2 . PHE C 66  ? 1.0716 0.9002 0.8528 0.0427  -0.0341 -0.0529 66  PHE C CE2 
9482  C CZ  . PHE C 66  ? 1.0840 0.9362 0.8817 0.0350  -0.0392 -0.0471 66  PHE C CZ  
9492  N N   . SER C 67  ? 1.0147 0.8992 0.8523 0.0725  -0.0209 -0.0413 67  SER C N   
9493  C CA  . SER C 67  ? 1.0421 0.9125 0.8796 0.0667  -0.0251 -0.0367 67  SER C CA  
9494  C C   . SER C 67  ? 1.0108 0.8835 0.8522 0.0501  -0.0301 -0.0341 67  SER C C   
9495  O O   . SER C 67  ? 1.0135 0.9094 0.8720 0.0452  -0.0313 -0.0302 67  SER C O   
9496  C CB  . SER C 67  ? 1.0314 0.9163 0.8848 0.0713  -0.0240 -0.0309 67  SER C CB  
9497  O OG  . SER C 67  ? 1.0405 0.9149 0.8939 0.0612  -0.0262 -0.0261 67  SER C OG  
9503  N N   . GLY C 68  ? 1.0454 0.8941 0.8716 0.0416  -0.0337 -0.0369 68  GLY C N   
9504  C CA  . GLY C 68  ? 1.0339 0.8880 0.8682 0.0256  -0.0398 -0.0356 68  GLY C CA  
9505  C C   . GLY C 68  ? 1.0220 0.8924 0.8789 0.0191  -0.0388 -0.0300 68  GLY C C   
9506  O O   . GLY C 68  ? 1.0070 0.8984 0.8832 0.0115  -0.0425 -0.0281 68  GLY C O   
9510  N N   . ASN C 69  ? 1.0266 0.8859 0.8799 0.0224  -0.0339 -0.0276 69  ASN C N   
9511  C CA  . ASN C 69  ? 1.0336 0.9053 0.9042 0.0154  -0.0308 -0.0230 69  ASN C CA  
9512  C C   . ASN C 69  ? 0.9987 0.9012 0.8913 0.0210  -0.0294 -0.0194 69  ASN C C   
9513  O O   . ASN C 69  ? 0.9560 0.8776 0.8695 0.0132  -0.0296 -0.0178 69  ASN C O   
9514  C CB  . ASN C 69  ? 1.0406 0.8891 0.8955 0.0184  -0.0265 -0.0206 69  ASN C CB  
9515  C CG  . ASN C 69  ? 1.1349 0.9524 0.9708 0.0058  -0.0262 -0.0228 69  ASN C CG  
9516  O OD1 . ASN C 69  ? 1.2007 0.9856 1.0101 0.0116  -0.0267 -0.0238 69  ASN C OD1 
9517  N ND2 . ASN C 69  ? 1.1078 0.9352 0.9579 -0.0115 -0.0254 -0.0242 69  ASN C ND2 
9524  N N   . ALA C 70  ? 0.9899 0.8977 0.8789 0.0342  -0.0278 -0.0188 70  ALA C N   
9525  C CA  . ALA C 70  ? 0.9524 0.8863 0.8590 0.0380  -0.0259 -0.0158 70  ALA C CA  
9526  C C   . ALA C 70  ? 0.9307 0.8793 0.8478 0.0324  -0.0303 -0.0159 70  ALA C C   
9527  O O   . ALA C 70  ? 0.9558 0.9213 0.8911 0.0287  -0.0304 -0.0130 70  ALA C O   
9528  C CB  . ALA C 70  ? 0.9691 0.9076 0.8706 0.0513  -0.0234 -0.0170 70  ALA C CB  
9534  N N   . SER C 71  ? 0.9607 0.9007 0.8644 0.0322  -0.0345 -0.0196 71  SER C N   
9535  C CA  . SER C 71  ? 0.9716 0.9208 0.8799 0.0270  -0.0413 -0.0191 71  SER C CA  
9536  C C   . SER C 71  ? 0.9202 0.8774 0.8472 0.0170  -0.0469 -0.0181 71  SER C C   
9537  O O   . SER C 71  ? 0.8986 0.8722 0.8422 0.0158  -0.0511 -0.0154 71  SER C O   
9538  C CB  . SER C 71  ? 1.0067 0.9397 0.8919 0.0263  -0.0452 -0.0239 71  SER C CB  
9539  O OG  . SER C 71  ? 0.9846 0.9140 0.8560 0.0358  -0.0382 -0.0265 71  SER C OG  
9545  N N   . ARG C 72  ? 0.9401 0.8856 0.8652 0.0095  -0.0467 -0.0207 72  ARG C N   
9546  C CA  . ARG C 72  ? 0.9540 0.9111 0.9014 -0.0012 -0.0492 -0.0213 72  ARG C CA  
9547  C C   . ARG C 72  ? 0.9320 0.9075 0.9017 0.0007  -0.0425 -0.0178 72  ARG C C   
9548  O O   . ARG C 72  ? 0.9287 0.9231 0.9234 -0.0035 -0.0454 -0.0181 72  ARG C O   
9549  C CB  . ARG C 72  ? 1.0112 0.9495 0.9490 -0.0114 -0.0466 -0.0249 72  ARG C CB  
9550  C CG  . ARG C 72  ? 0.9859 0.9058 0.9038 -0.0168 -0.0542 -0.0297 72  ARG C CG  
9551  C CD  . ARG C 72  ? 1.0368 0.9278 0.9342 -0.0236 -0.0494 -0.0327 72  ARG C CD  
9552  N NE  . ARG C 72  ? 1.0408 0.9296 0.9442 -0.0272 -0.0398 -0.0302 72  ARG C NE  
9553  C CZ  . ARG C 72  ? 1.0661 0.9664 0.9893 -0.0412 -0.0368 -0.0316 72  ARG C CZ  
9554  N NH1 . ARG C 72  ? 1.0623 0.9816 1.0067 -0.0517 -0.0440 -0.0357 72  ARG C NH1 
9555  N NH2 . ARG C 72  ? 1.0586 0.9515 0.9800 -0.0450 -0.0264 -0.0295 72  ARG C NH2 
9569  N N   . ALA C 73  ? 0.9516 0.9216 0.9130 0.0074  -0.0340 -0.0152 73  ALA C N   
9570  C CA  . ALA C 73  ? 0.9226 0.9072 0.9009 0.0086  -0.0274 -0.0123 73  ALA C CA  
9571  C C   . ALA C 73  ? 0.8980 0.8997 0.8878 0.0149  -0.0307 -0.0098 73  ALA C C   
9572  O O   . ALA C 73  ? 0.8851 0.9019 0.8962 0.0132  -0.0298 -0.0092 73  ALA C O   
9573  C CB  . ALA C 73  ? 0.9191 0.8919 0.8823 0.0137  -0.0200 -0.0101 73  ALA C CB  
9579  N N   . PHE C 74  ? 0.9154 0.9131 0.8901 0.0217  -0.0338 -0.0089 74  PHE C N   
9580  C CA  . PHE C 74  ? 0.9374 0.9456 0.9166 0.0258  -0.0367 -0.0062 74  PHE C CA  
9581  C C   . PHE C 74  ? 0.9011 0.9167 0.8944 0.0222  -0.0468 -0.0062 74  PHE C C   
9582  O O   . PHE C 74  ? 0.9067 0.9335 0.9163 0.0241  -0.0480 -0.0040 74  PHE C O   
9583  C CB  . PHE C 74  ? 0.9262 0.9267 0.8837 0.0308  -0.0369 -0.0066 74  PHE C CB  
9584  C CG  . PHE C 74  ? 0.9236 0.9298 0.8791 0.0328  -0.0385 -0.0036 74  PHE C CG  
9585  C CD1 . PHE C 74  ? 0.9326 0.9489 0.9036 0.0332  -0.0374 -0.0002 74  PHE C CD1 
9586  C CD2 . PHE C 74  ? 0.9827 0.9809 0.9177 0.0336  -0.0401 -0.0045 74  PHE C CD2 
9587  C CE1 . PHE C 74  ? 0.9329 0.9491 0.8978 0.0343  -0.0390 0.0029  74  PHE C CE1 
9588  C CE2 . PHE C 74  ? 0.9886 0.9875 0.9167 0.0334  -0.0408 -0.0014 74  PHE C CE2 
9589  C CZ  . PHE C 74  ? 0.9587 0.9656 0.9013 0.0338  -0.0408 0.0027  74  PHE C CZ  
9599  N N   . ALA C 75  ? 0.9050 0.9137 0.8920 0.0176  -0.0552 -0.0090 75  ALA C N   
9600  C CA  . ALA C 75  ? 0.9126 0.9300 0.9143 0.0146  -0.0679 -0.0095 75  ALA C CA  
9601  C C   . ALA C 75  ? 0.9116 0.9475 0.9468 0.0117  -0.0657 -0.0111 75  ALA C C   
9602  O O   . ALA C 75  ? 0.9132 0.9621 0.9681 0.0152  -0.0726 -0.0100 75  ALA C O   
9603  C CB  . ALA C 75  ? 0.9281 0.9350 0.9170 0.0080  -0.0773 -0.0133 75  ALA C CB  
9609  N N   . SER C 76  ? 0.8923 0.9278 0.9331 0.0055  -0.0557 -0.0141 76  SER C N   
9610  C CA  . SER C 76  ? 0.9107 0.9636 0.9820 0.0011  -0.0499 -0.0169 76  SER C CA  
9611  C C   . SER C 76  ? 0.9042 0.9663 0.9869 0.0091  -0.0441 -0.0139 76  SER C C   
9612  O O   . SER C 76  ? 0.8744 0.9539 0.9858 0.0100  -0.0446 -0.0162 76  SER C O   
9613  C CB  . SER C 76  ? 0.9076 0.9515 0.9732 -0.0082 -0.0379 -0.0197 76  SER C CB  
9614  O OG  . SER C 76  ? 0.9179 0.9520 0.9743 -0.0171 -0.0432 -0.0233 76  SER C OG  
9620  N N   . LEU C 77  ? 0.9006 0.9517 0.9621 0.0149  -0.0386 -0.0096 77  LEU C N   
9621  C CA  . LEU C 77  ? 0.8873 0.9439 0.9554 0.0210  -0.0333 -0.0069 77  LEU C CA  
9622  C C   . LEU C 77  ? 0.8968 0.9586 0.9732 0.0273  -0.0447 -0.0047 77  LEU C C   
9623  O O   . LEU C 77  ? 0.8755 0.9467 0.9720 0.0312  -0.0437 -0.0051 77  LEU C O   
9624  C CB  . LEU C 77  ? 0.8976 0.9430 0.9416 0.0243  -0.0267 -0.0035 77  LEU C CB  
9625  C CG  . LEU C 77  ? 0.8924 0.9409 0.9382 0.0288  -0.0215 -0.0009 77  LEU C CG  
9626  C CD1 . LEU C 77  ? 0.8918 0.9484 0.9576 0.0263  -0.0128 -0.0035 77  LEU C CD1 
9627  C CD2 . LEU C 77  ? 0.8732 0.9147 0.8980 0.0306  -0.0161 0.0011  77  LEU C CD2 
9639  N N   . LEU C 78  ? 0.9178 0.9703 0.9760 0.0287  -0.0557 -0.0025 78  LEU C N   
9640  C CA  . LEU C 78  ? 0.8971 0.9490 0.9572 0.0342  -0.0689 0.0005  78  LEU C CA  
9641  C C   . LEU C 78  ? 0.9127 0.9818 1.0069 0.0354  -0.0775 -0.0031 78  LEU C C   
9642  O O   . LEU C 78  ? 0.9271 1.0005 1.0353 0.0429  -0.0830 -0.0015 78  LEU C O   
9643  C CB  . LEU C 78  ? 0.9465 0.9839 0.9789 0.0328  -0.0795 0.0023  78  LEU C CB  
9644  C CG  . LEU C 78  ? 0.9363 0.9590 0.9370 0.0331  -0.0718 0.0049  78  LEU C CG  
9645  C CD1 . LEU C 78  ? 0.9269 0.9352 0.9007 0.0303  -0.0802 0.0046  78  LEU C CD1 
9646  C CD2 . LEU C 78  ? 0.9203 0.9386 0.9148 0.0375  -0.0691 0.0096  78  LEU C CD2 
9658  N N   . ALA C 79  ? 0.8962 0.9755 1.0052 0.0279  -0.0784 -0.0085 79  ALA C N   
9659  C CA  . ALA C 79  ? 0.9006 1.0022 1.0482 0.0276  -0.0848 -0.0139 79  ALA C CA  
9660  C C   . ALA C 79  ? 0.8790 0.9944 1.0530 0.0299  -0.0703 -0.0170 79  ALA C C   
9661  O O   . ALA C 79  ? 0.8772 1.0101 1.0836 0.0360  -0.0753 -0.0203 79  ALA C O   
9662  C CB  . ALA C 79  ? 0.9418 1.0507 1.0975 0.0158  -0.0866 -0.0200 79  ALA C CB  
9668  N N   . PHE C 80  ? 0.9165 1.0236 1.0766 0.0257  -0.0529 -0.0166 80  PHE C N   
9669  C CA  . PHE C 80  ? 0.9024 1.0184 1.0811 0.0264  -0.0378 -0.0198 80  PHE C CA  
9670  C C   . PHE C 80  ? 0.8792 0.9931 1.0618 0.0384  -0.0407 -0.0166 80  PHE C C   
9671  O O   . PHE C 80  ? 0.8763 1.0028 1.0860 0.0425  -0.0348 -0.0212 80  PHE C O   
9672  C CB  . PHE C 80  ? 0.8778 0.9801 1.0326 0.0197  -0.0218 -0.0185 80  PHE C CB  
9673  C CG  . PHE C 80  ? 0.9023 1.0106 1.0708 0.0168  -0.0051 -0.0227 80  PHE C CG  
9674  C CD1 . PHE C 80  ? 0.9326 1.0580 1.1300 0.0094  0.0026  -0.0307 80  PHE C CD1 
9675  C CD2 . PHE C 80  ? 0.8921 0.9891 1.0438 0.0200  0.0038  -0.0195 80  PHE C CD2 
9676  C CE1 . PHE C 80  ? 0.8635 0.9926 1.0705 0.0055  0.0202  -0.0355 80  PHE C CE1 
9677  C CE2 . PHE C 80  ? 0.8999 0.9995 1.0599 0.0164  0.0194  -0.0238 80  PHE C CE2 
9678  C CZ  . PHE C 80  ? 0.8753 0.9900 1.0619 0.0093  0.0283  -0.0318 80  PHE C CZ  
9688  N N   . ARG C 81  ? 0.8962 0.9928 1.0509 0.0436  -0.0488 -0.0094 81  ARG C N   
9689  C CA  . ARG C 81  ? 0.9030 0.9907 1.0532 0.0530  -0.0509 -0.0055 81  ARG C CA  
9690  C C   . ARG C 81  ? 0.9572 1.0449 1.1167 0.0623  -0.0704 -0.0034 81  ARG C C   
9691  O O   . ARG C 81  ? 0.9807 1.0575 1.1361 0.0710  -0.0739 0.0000  81  ARG C O   
9692  C CB  . ARG C 81  ? 0.9024 0.9700 1.0152 0.0513  -0.0467 0.0007  81  ARG C CB  
9693  C CG  . ARG C 81  ? 0.9130 0.9797 1.0147 0.0438  -0.0313 -0.0007 81  ARG C CG  
9694  C CD  . ARG C 81  ? 0.8904 0.9432 0.9632 0.0433  -0.0268 0.0040  81  ARG C CD  
9695  N NE  . ARG C 81  ? 0.9791 1.0323 1.0504 0.0401  -0.0128 0.0023  81  ARG C NE  
9696  C CZ  . ARG C 81  ? 0.9903 1.0379 1.0414 0.0370  -0.0070 0.0040  81  ARG C CZ  
9697  N NH1 . ARG C 81  ? 0.9809 1.0235 1.0134 0.0369  -0.0116 0.0067  81  ARG C NH1 
9698  N NH2 . ARG C 81  ? 1.0077 1.0553 1.0576 0.0338  0.0036  0.0023  81  ARG C NH2 
9712  N N   . ASP C 82  ? 0.9386 1.0356 1.1079 0.0604  -0.0842 -0.0053 82  ASP C N   
9713  C CA  . ASP C 82  ? 0.9816 1.0787 1.1593 0.0694  -0.1061 -0.0033 82  ASP C CA  
9714  C C   . ASP C 82  ? 0.9944 1.1170 1.2207 0.0771  -0.1085 -0.0106 82  ASP C C   
9715  O O   . ASP C 82  ? 0.9866 1.1341 1.2437 0.0711  -0.1069 -0.0184 82  ASP C O   
9716  C CB  . ASP C 82  ? 1.0018 1.0979 1.1676 0.0631  -0.1209 -0.0029 82  ASP C CB  
9717  C CG  . ASP C 82  ? 1.0307 1.1215 1.1959 0.0718  -0.1464 0.0006  82  ASP C CG  
9718  O OD1 . ASP C 82  ? 1.0464 1.1544 1.2479 0.0814  -0.1562 -0.0028 82  ASP C OD1 
9719  O OD2 . ASP C 82  ? 1.0812 1.1499 1.2089 0.0692  -0.1569 0.0064  82  ASP C OD2 
9724  N N   . LYS C 83  ? 1.0293 1.1455 1.2631 0.0901  -0.1117 -0.0088 83  LYS C N   
9725  C CA  . LYS C 83  ? 1.0388 1.1796 1.3214 0.1003  -0.1135 -0.0168 83  LYS C CA  
9726  C C   . LYS C 83  ? 1.0523 1.2150 1.3649 0.1041  -0.1359 -0.0207 83  LYS C C   
9727  O O   . LYS C 83  ? 1.0373 1.2308 1.3992 0.1092  -0.1358 -0.0304 83  LYS C O   
9728  C CB  . LYS C 83  ? 1.0534 1.1763 1.3325 0.1156  -0.1159 -0.0134 83  LYS C CB  
9729  C CG  . LYS C 83  ? 1.1298 1.2246 1.3781 0.1245  -0.1395 -0.0031 83  LYS C CG  
9730  C CD  . LYS C 83  ? 1.0938 1.1841 1.3631 0.1444  -0.1527 -0.0035 83  LYS C CD  
9731  C CE  . LYS C 83  ? 1.0738 1.1310 1.3133 0.1489  -0.1421 0.0020  83  LYS C CE  
9732  N NZ  . LYS C 83  ? 1.1042 1.1500 1.3589 0.1697  -0.1562 0.0023  83  LYS C NZ  
9746  N N   . ASP C 84  ? 1.1288 1.2772 1.4132 0.1011  -0.1549 -0.0141 84  ASP C N   
9747  C CA  . ASP C 84  ? 1.1382 1.3040 1.4453 0.1041  -0.1799 -0.0169 84  ASP C CA  
9748  C C   . ASP C 84  ? 1.0591 1.2418 1.3713 0.0870  -0.1778 -0.0225 84  ASP C C   
9749  O O   . ASP C 84  ? 1.0234 1.2195 1.3499 0.0860  -0.1990 -0.0250 84  ASP C O   
9750  C CB  . ASP C 84  ? 1.1323 1.2670 1.4009 0.1119  -0.2050 -0.0062 84  ASP C CB  
9751  C CG  . ASP C 84  ? 1.1935 1.3129 1.4644 0.1310  -0.2143 -0.0017 84  ASP C CG  
9752  O OD1 . ASP C 84  ? 1.1913 1.3363 1.5114 0.1438  -0.2195 -0.0090 84  ASP C OD1 
9753  O OD2 . ASP C 84  ? 1.2486 1.3300 1.4724 0.1330  -0.2156 0.0084  84  ASP C OD2 
9758  N N   . PHE C 85  ? 1.0497 1.2300 1.3490 0.0733  -0.1541 -0.0244 85  PHE C N   
9759  C CA  . PHE C 85  ? 1.0444 1.2374 1.3481 0.0567  -0.1502 -0.0302 85  PHE C CA  
9760  C C   . PHE C 85  ? 1.0577 1.2911 1.4192 0.0535  -0.1459 -0.0426 85  PHE C C   
9761  O O   . PHE C 85  ? 1.0547 1.3013 1.4411 0.0558  -0.1271 -0.0478 85  PHE C O   
9762  C CB  . PHE C 85  ? 0.9762 1.1510 1.2470 0.0450  -0.1272 -0.0281 85  PHE C CB  
9763  C CG  . PHE C 85  ? 0.9887 1.1687 1.2573 0.0281  -0.1224 -0.0333 85  PHE C CG  
9764  C CD1 . PHE C 85  ? 1.0059 1.2091 1.3071 0.0179  -0.1077 -0.0427 85  PHE C CD1 
9765  C CD2 . PHE C 85  ? 0.9810 1.1399 1.2123 0.0216  -0.1315 -0.0294 85  PHE C CD2 
9766  C CE1 . PHE C 85  ? 1.0192 1.2225 1.3144 0.0010  -0.1031 -0.0472 85  PHE C CE1 
9767  C CE2 . PHE C 85  ? 0.9636 1.1228 1.1900 0.0062  -0.1272 -0.0344 85  PHE C CE2 
9768  C CZ  . PHE C 85  ? 1.0019 1.1822 1.2595 -0.0044 -0.1135 -0.0429 85  PHE C CZ  
9778  N N   . SER C 86  ? 1.0712 1.3246 1.4539 0.0471  -0.1625 -0.0481 86  SER C N   
9779  C CA  . SER C 86  ? 1.1148 1.4112 1.5566 0.0423  -0.1595 -0.0614 86  SER C CA  
9780  C C   . SER C 86  ? 1.1488 1.4511 1.5881 0.0189  -0.1435 -0.0679 86  SER C C   
9781  O O   . SER C 86  ? 1.1631 1.4682 1.6073 0.0104  -0.1172 -0.0721 86  SER C O   
9782  C CB  . SER C 86  ? 1.0982 1.4179 1.5725 0.0509  -0.1908 -0.0647 86  SER C CB  
9783  O OG  . SER C 86  ? 1.1367 1.5038 1.6756 0.0479  -0.1878 -0.0790 86  SER C OG  
9789  N N   . LYS C 87  ? 1.0457 1.3463 1.4738 0.0078  -0.1594 -0.0687 87  LYS C N   
9790  C CA  . LYS C 87  ? 1.0146 1.3140 1.4339 -0.0150 -0.1465 -0.0742 87  LYS C CA  
9791  C C   . LYS C 87  ? 0.9864 1.2482 1.3489 -0.0226 -0.1538 -0.0667 87  LYS C C   
9792  O O   . LYS C 87  ? 1.0028 1.2499 1.3438 -0.0388 -0.1388 -0.0686 87  LYS C O   
9793  C CB  . LYS C 87  ? 0.9970 1.3382 1.4683 -0.0267 -0.1552 -0.0875 87  LYS C CB  
9794  C CG  . LYS C 87  ? 0.9927 1.3780 1.5289 -0.0154 -0.1550 -0.0966 87  LYS C CG  
9795  C CD  . LYS C 87  ? 0.9688 1.3978 1.5578 -0.0201 -0.1765 -0.1080 87  LYS C CD  
9796  C CE  . LYS C 87  ? 0.9975 1.4125 1.5622 -0.0159 -0.2113 -0.1015 87  LYS C CE  
9797  N NZ  . LYS C 87  ? 1.0293 1.4068 1.5500 0.0046  -0.2237 -0.0867 87  LYS C NZ  
9811  N N   . GLN C 88  ? 0.9686 1.2118 1.3041 -0.0115 -0.1755 -0.0587 88  GLN C N   
9812  C CA  . GLN C 88  ? 0.9547 1.1613 1.2350 -0.0175 -0.1808 -0.0524 88  GLN C CA  
9813  C C   . GLN C 88  ? 0.9408 1.1240 1.1894 -0.0014 -0.1954 -0.0419 88  GLN C C   
9814  O O   . GLN C 88  ? 0.9164 1.1126 1.1862 0.0112  -0.2139 -0.0405 88  GLN C O   
9815  C CB  . GLN C 88  ? 0.9173 1.1296 1.1988 -0.0326 -0.1972 -0.0589 88  GLN C CB  
9816  C CG  . GLN C 88  ? 0.9459 1.1184 1.1689 -0.0393 -0.2010 -0.0541 88  GLN C CG  
9817  C CD  . GLN C 88  ? 0.9995 1.1541 1.1939 -0.0285 -0.2250 -0.0468 88  GLN C CD  
9818  O OE1 . GLN C 88  ? 1.0106 1.1839 1.2308 -0.0184 -0.2454 -0.0462 88  GLN C OE1 
9819  N NE2 . GLN C 88  ? 1.0252 1.1422 1.1651 -0.0303 -0.2225 -0.0415 88  GLN C NE2 
9828  N N   . LYS C 89  ? 0.9529 1.1010 1.1508 -0.0020 -0.1869 -0.0349 89  LYS C N   
9829  C CA  . LYS C 89  ? 0.9611 1.0833 1.1226 0.0096  -0.1968 -0.0253 89  LYS C CA  
9830  C C   . LYS C 89  ? 0.9762 1.0652 1.0860 0.0033  -0.1859 -0.0219 89  LYS C C   
9831  O O   . LYS C 89  ? 0.9689 1.0536 1.0734 -0.0021 -0.1650 -0.0237 89  LYS C O   
9832  C CB  . LYS C 89  ? 0.9443 1.0689 1.1170 0.0241  -0.1883 -0.0203 89  LYS C CB  
9833  C CG  . LYS C 89  ? 0.9656 1.0682 1.1105 0.0362  -0.2042 -0.0112 89  LYS C CG  
9834  C CD  . LYS C 89  ? 1.0211 1.1220 1.1738 0.0488  -0.1936 -0.0067 89  LYS C CD  
9835  C CE  . LYS C 89  ? 1.0035 1.0914 1.1474 0.0623  -0.2151 0.0003  89  LYS C CE  
9836  N NZ  . LYS C 89  ? 0.9887 1.0433 1.0880 0.0658  -0.2072 0.0094  89  LYS C NZ  
9850  N N   . ASN C 90  ? 0.9745 1.0395 1.0460 0.0043  -0.2003 -0.0175 90  ASN C N   
9851  C CA  . ASN C 90  ? 0.9992 1.0335 1.0224 -0.0004 -0.1901 -0.0155 90  ASN C CA  
9852  C C   . ASN C 90  ? 0.9916 1.0103 0.9921 0.0093  -0.1788 -0.0081 90  ASN C C   
9853  O O   . ASN C 90  ? 0.9981 1.0148 0.9985 0.0182  -0.1887 -0.0023 90  ASN C O   
9854  C CB  . ASN C 90  ? 1.0635 1.0781 1.0531 -0.0068 -0.2090 -0.0160 90  ASN C CB  
9855  C CG  . ASN C 90  ? 1.0843 1.1033 1.0795 -0.0209 -0.2123 -0.0246 90  ASN C CG  
9856  O OD1 . ASN C 90  ? 1.0994 1.1437 1.1312 -0.0255 -0.2248 -0.0295 90  ASN C OD1 
9857  N ND2 . ASN C 90  ? 1.1198 1.1143 1.0797 -0.0281 -0.2007 -0.0272 90  ASN C ND2 
9864  N N   . TYR C 91  ? 0.9949 1.0017 0.9758 0.0073  -0.1586 -0.0085 91  TYR C N   
9865  C CA  . TYR C 91  ? 1.0444 1.0405 1.0072 0.0143  -0.1455 -0.0031 91  TYR C CA  
9866  C C   . TYR C 91  ? 1.0463 1.0181 0.9665 0.0107  -0.1379 -0.0037 91  TYR C C   
9867  O O   . TYR C 91  ? 1.0691 1.0355 0.9815 0.0051  -0.1314 -0.0092 91  TYR C O   
9868  C CB  . TYR C 91  ? 0.9780 0.9891 0.9657 0.0172  -0.1269 -0.0038 91  TYR C CB  
9869  C CG  . TYR C 91  ? 0.9602 0.9936 0.9875 0.0223  -0.1307 -0.0034 91  TYR C CG  
9870  C CD1 . TYR C 91  ? 0.9504 1.0050 1.0126 0.0175  -0.1331 -0.0094 91  TYR C CD1 
9871  C CD2 . TYR C 91  ? 0.9514 0.9839 0.9813 0.0313  -0.1309 0.0020  91  TYR C CD2 
9872  C CE1 . TYR C 91  ? 0.9612 1.0384 1.0625 0.0227  -0.1348 -0.0108 91  TYR C CE1 
9873  C CE2 . TYR C 91  ? 0.9396 0.9909 1.0059 0.0375  -0.1336 0.0012  91  TYR C CE2 
9874  C CZ  . TYR C 91  ? 0.9632 1.0383 1.0665 0.0338  -0.1353 -0.0056 91  TYR C CZ  
9875  O OH  . TYR C 91  ? 0.9746 1.0707 1.1170 0.0406  -0.1362 -0.0080 91  TYR C OH  
9885  N N   . ASN C 92  ? 1.0382 0.9942 0.9303 0.0138  -0.1378 0.0012  92  ASN C N   
9886  C CA  . ASN C 92  ? 1.1155 1.0499 0.9674 0.0105  -0.1290 -0.0005 92  ASN C CA  
9887  C C   . ASN C 92  ? 1.1010 1.0394 0.9531 0.0147  -0.1082 0.0001  92  ASN C C   
9888  O O   . ASN C 92  ? 1.1368 1.0781 0.9924 0.0185  -0.1055 0.0053  92  ASN C O   
9889  C CB  . ASN C 92  ? 1.1509 1.0632 0.9673 0.0082  -0.1421 0.0037  92  ASN C CB  
9890  C CG  . ASN C 92  ? 1.2289 1.1277 1.0253 0.0009  -0.1577 0.0000  92  ASN C CG  
9891  O OD1 . ASN C 92  ? 1.2244 1.1324 1.0400 0.0000  -0.1766 0.0001  92  ASN C OD1 
9892  N ND2 . ASN C 92  ? 1.3168 1.1944 1.0754 -0.0046 -0.1496 -0.0043 92  ASN C ND2 
9899  N N   . ILE C 93  ? 1.1051 1.0431 0.9536 0.0143  -0.0946 -0.0055 93  ILE C N   
9900  C CA  . ILE C 93  ? 1.0939 1.0393 0.9467 0.0189  -0.0768 -0.0061 93  ILE C CA  
9901  C C   . ILE C 93  ? 1.0921 1.0249 0.9185 0.0185  -0.0661 -0.0122 93  ILE C C   
9902  O O   . ILE C 93  ? 1.1230 1.0394 0.9269 0.0142  -0.0714 -0.0161 93  ILE C O   
9903  C CB  . ILE C 93  ? 1.0777 1.0400 0.9622 0.0222  -0.0706 -0.0069 93  ILE C CB  
9904  C CG1 . ILE C 93  ? 1.0760 1.0329 0.9619 0.0189  -0.0725 -0.0122 93  ILE C CG1 
9905  C CG2 . ILE C 93  ? 1.0283 1.0048 0.9404 0.0233  -0.0773 -0.0022 93  ILE C CG2 
9906  C CD1 . ILE C 93  ? 1.0382 0.9997 0.9356 0.0224  -0.0606 -0.0143 93  ILE C CD1 
9918  N N   . THR C 94  ? 1.0477 0.9891 0.8782 0.0232  -0.0509 -0.0139 94  THR C N   
9919  C CA  . THR C 94  ? 1.0708 1.0059 0.8844 0.0255  -0.0388 -0.0212 94  THR C CA  
9920  C C   . THR C 94  ? 1.0887 1.0379 0.9241 0.0335  -0.0290 -0.0238 94  THR C C   
9921  O O   . THR C 94  ? 1.0425 1.0064 0.9007 0.0357  -0.0287 -0.0193 94  THR C O   
9922  C CB  . THR C 94  ? 1.1179 1.0496 0.9102 0.0225  -0.0297 -0.0220 94  THR C CB  
9923  O OG1 . THR C 94  ? 1.0427 0.9936 0.8532 0.0257  -0.0195 -0.0204 94  THR C OG1 
9924  C CG2 . THR C 94  ? 1.1682 1.0853 0.9401 0.0149  -0.0416 -0.0159 94  THR C CG2 
9932  N N   . CYS C 95  ? 1.0877 1.0300 0.9137 0.0385  -0.0216 -0.0313 95  CYS C N   
9933  C CA  . CYS C 95  ? 1.0788 1.0300 0.9214 0.0479  -0.0150 -0.0340 95  CYS C CA  
9934  C C   . CYS C 95  ? 1.1028 1.0552 0.9369 0.0552  -0.0029 -0.0427 95  CYS C C   
9935  O O   . CYS C 95  ? 1.0694 1.0065 0.8809 0.0536  0.0000  -0.0489 95  CYS C O   
9936  C CB  . CYS C 95  ? 1.0871 1.0247 0.9315 0.0487  -0.0216 -0.0345 95  CYS C CB  
9937  S SG  . CYS C 95  ? 1.1110 1.0556 0.9743 0.0586  -0.0178 -0.0336 95  CYS C SG  
9943  N N   . SER C 96  ? 1.0923 1.0639 0.9454 0.0633  0.0041  -0.0439 96  SER C N   
9944  C CA  . SER C 96  ? 1.0910 1.0702 0.9444 0.0725  0.0155  -0.0535 96  SER C CA  
9945  C C   . SER C 96  ? 1.0969 1.0544 0.9372 0.0803  0.0150  -0.0605 96  SER C C   
9946  O O   . SER C 96  ? 1.0661 1.0102 0.9080 0.0835  0.0070  -0.0575 96  SER C O   
9947  C CB  . SER C 96  ? 1.0363 1.0403 0.9163 0.0810  0.0186  -0.0533 96  SER C CB  
9948  O OG  . SER C 96  ? 1.0509 1.0471 0.9387 0.0893  0.0111  -0.0508 96  SER C OG  
9954  N N   . GLY C 97  ? 1.1257 1.0772 0.9505 0.0824  0.0246  -0.0702 97  GLY C N   
9955  C CA  . GLY C 97  ? 1.1150 1.0423 0.9235 0.0898  0.0254  -0.0782 97  GLY C CA  
9956  C C   . GLY C 97  ? 1.1912 1.0890 0.9709 0.0784  0.0182  -0.0772 97  GLY C C   
9957  O O   . GLY C 97  ? 1.2321 1.1051 0.9963 0.0826  0.0168  -0.0829 97  GLY C O   
9961  N N   . GLU C 98  ? 1.2063 1.1048 0.9775 0.0644  0.0124  -0.0705 98  GLU C N   
9962  C CA  . GLU C 98  ? 1.2139 1.0877 0.9593 0.0527  0.0025  -0.0692 98  GLU C CA  
9963  C C   . GLU C 98  ? 1.2272 1.1001 0.9519 0.0423  0.0052  -0.0688 98  GLU C C   
9964  O O   . GLU C 98  ? 1.1904 1.0779 0.9247 0.0370  0.0018  -0.0607 98  GLU C O   
9965  C CB  . GLU C 98  ? 1.2098 1.0841 0.9687 0.0464  -0.0127 -0.0595 98  GLU C CB  
9966  C CG  . GLU C 98  ? 1.2529 1.1051 0.9912 0.0347  -0.0254 -0.0591 98  GLU C CG  
9967  C CD  . GLU C 98  ? 1.3524 1.1764 1.0610 0.0351  -0.0215 -0.0694 98  GLU C CD  
9968  O OE1 . GLU C 98  ? 1.3744 1.1914 1.0605 0.0346  -0.0128 -0.0757 98  GLU C OE1 
9969  O OE2 . GLU C 98  ? 1.3236 1.1306 1.0294 0.0349  -0.0261 -0.0717 98  GLU C OE2 
9976  N N   . SER C 99  ? 1.3101 1.1624 1.0032 0.0391  0.0115  -0.0776 99  SER C N   
9977  C CA  . SER C 99  ? 1.3331 1.1797 0.9995 0.0285  0.0164  -0.0781 99  SER C CA  
9978  C C   . SER C 99  ? 1.3272 1.1598 0.9760 0.0155  -0.0020 -0.0687 99  SER C C   
9979  O O   . SER C 99  ? 1.2949 1.1240 0.9248 0.0068  -0.0017 -0.0649 99  SER C O   
9980  C CB  . SER C 99  ? 1.3420 1.1680 0.9763 0.0282  0.0297  -0.0914 99  SER C CB  
9981  O OG  . SER C 99  ? 1.3550 1.1503 0.9620 0.0219  0.0179  -0.0931 99  SER C OG  
9987  N N   . LYS C 100 ? 1.3641 1.1883 1.0184 0.0137  -0.0181 -0.0652 100 LYS C N   
9988  C CA  . LYS C 100 ? 1.3489 1.1622 0.9904 0.0027  -0.0377 -0.0579 100 LYS C CA  
9989  C C   . LYS C 100 ? 1.3348 1.1704 1.0121 0.0043  -0.0492 -0.0473 100 LYS C C   
9990  O O   . LYS C 100 ? 1.3292 1.1813 1.0380 0.0116  -0.0459 -0.0464 100 LYS C O   
9991  C CB  . LYS C 100 ? 1.4826 1.2724 1.1057 -0.0029 -0.0484 -0.0630 100 LYS C CB  
9992  C CG  . LYS C 100 ? 1.5780 1.3381 1.1533 -0.0102 -0.0442 -0.0713 100 LYS C CG  
9993  C CD  . LYS C 100 ? 1.6176 1.3534 1.1718 -0.0194 -0.0598 -0.0746 100 LYS C CD  
9994  C CE  . LYS C 100 ? 1.6685 1.3738 1.1705 -0.0307 -0.0625 -0.0793 100 LYS C CE  
9995  N NZ  . LYS C 100 ? 1.7228 1.4247 1.2022 -0.0297 -0.0434 -0.0825 100 LYS C NZ  
10009 N N   . VAL C 101 ? 1.3060 1.1397 0.9763 -0.0025 -0.0629 -0.0395 101 VAL C N   
10010 C CA  . VAL C 101 ? 1.2465 1.0999 0.9500 -0.0007 -0.0744 -0.0304 101 VAL C CA  
10011 C C   . VAL C 101 ? 1.2218 1.0796 0.9468 -0.0018 -0.0856 -0.0314 101 VAL C C   
10012 O O   . VAL C 101 ? 1.2869 1.1276 0.9936 -0.0081 -0.0934 -0.0364 101 VAL C O   
10013 C CB  . VAL C 101 ? 1.2212 1.0665 0.9083 -0.0062 -0.0886 -0.0226 101 VAL C CB  
10014 C CG1 . VAL C 101 ? 1.2447 1.1072 0.9657 -0.0040 -0.1043 -0.0154 101 VAL C CG1 
10015 C CG2 . VAL C 101 ? 1.1372 0.9815 0.8099 -0.0061 -0.0752 -0.0201 101 VAL C CG2 
10025 N N   . LEU C 102 ? 1.2288 1.1088 0.9915 0.0029  -0.0856 -0.0273 102 LEU C N   
10026 C CA  . LEU C 102 ? 1.1944 1.0805 0.9798 0.0006  -0.0916 -0.0290 102 LEU C CA  
10027 C C   . LEU C 102 ? 1.1844 1.0867 0.9956 -0.0025 -0.1075 -0.0233 102 LEU C C   
10028 O O   . LEU C 102 ? 1.1677 1.0886 1.0047 0.0027  -0.1048 -0.0182 102 LEU C O   
10029 C CB  . LEU C 102 ? 1.1687 1.0652 0.9749 0.0078  -0.0772 -0.0301 102 LEU C CB  
10030 C CG  . LEU C 102 ? 1.2063 1.0870 0.9929 0.0127  -0.0643 -0.0373 102 LEU C CG  
10031 C CD1 . LEU C 102 ? 1.1436 1.0384 0.9450 0.0234  -0.0501 -0.0363 102 LEU C CD1 
10032 C CD2 . LEU C 102 ? 1.1986 1.0642 0.9822 0.0087  -0.0669 -0.0422 102 LEU C CD2 
10044 N N   . ASP C 103 ? 1.2109 1.1064 1.0157 -0.0107 -0.1243 -0.0251 103 ASP C N   
10045 C CA  . ASP C 103 ? 1.1640 1.0783 0.9987 -0.0131 -0.1410 -0.0220 103 ASP C CA  
10046 C C   . ASP C 103 ? 1.1888 1.1190 1.0565 -0.0164 -0.1363 -0.0255 103 ASP C C   
10047 O O   . ASP C 103 ? 1.2672 1.1865 1.1264 -0.0245 -0.1360 -0.0316 103 ASP C O   
10048 C CB  . ASP C 103 ? 1.1993 1.1015 1.0145 -0.0211 -0.1623 -0.0233 103 ASP C CB  
10049 C CG  . ASP C 103 ? 1.2059 1.1297 1.0534 -0.0209 -0.1823 -0.0200 103 ASP C CG  
10050 O OD1 . ASP C 103 ? 1.1986 1.1451 1.0817 -0.0140 -0.1779 -0.0167 103 ASP C OD1 
10051 O OD2 . ASP C 103 ? 1.1884 1.1066 1.0260 -0.0272 -0.2031 -0.0214 103 ASP C OD2 
10056 N N   . VAL C 104 ? 1.1373 1.0903 1.0395 -0.0113 -0.1314 -0.0220 104 VAL C N   
10057 C CA  . VAL C 104 ? 1.1056 1.0725 1.0367 -0.0152 -0.1234 -0.0250 104 VAL C CA  
10058 C C   . VAL C 104 ? 1.0670 1.0589 1.0353 -0.0193 -0.1364 -0.0258 104 VAL C C   
10059 O O   . VAL C 104 ? 1.0582 1.0639 1.0426 -0.0121 -0.1441 -0.0215 104 VAL C O   
10060 C CB  . VAL C 104 ? 1.0912 1.0644 1.0321 -0.0071 -0.1056 -0.0218 104 VAL C CB  
10061 C CG1 . VAL C 104 ? 1.0414 1.0186 0.9987 -0.0129 -0.0957 -0.0251 104 VAL C CG1 
10062 C CG2 . VAL C 104 ? 1.1051 1.0603 1.0149 -0.0005 -0.0953 -0.0209 104 VAL C CG2 
10072 N N   . ASP C 105 ? 1.0681 1.0659 1.0508 -0.0308 -0.1383 -0.0320 105 ASP C N   
10073 C CA  . ASP C 105 ? 1.0537 1.0799 1.0771 -0.0365 -0.1496 -0.0354 105 ASP C CA  
10074 C C   . ASP C 105 ? 1.0042 1.0492 1.0599 -0.0375 -0.1330 -0.0369 105 ASP C C   
10075 O O   . ASP C 105 ? 1.0411 1.0791 1.0943 -0.0476 -0.1212 -0.0410 105 ASP C O   
10076 C CB  . ASP C 105 ? 1.0719 1.0945 1.0915 -0.0515 -0.1615 -0.0426 105 ASP C CB  
10077 C CG  . ASP C 105 ? 1.0700 1.1274 1.1369 -0.0584 -0.1732 -0.0479 105 ASP C CG  
10078 O OD1 . ASP C 105 ? 1.0705 1.1537 1.1728 -0.0497 -0.1719 -0.0460 105 ASP C OD1 
10079 O OD2 . ASP C 105 ? 1.0629 1.1226 1.1329 -0.0728 -0.1834 -0.0548 105 ASP C OD2 
10084 N N   . VAL C 106 ? 1.0322 1.0978 1.1153 -0.0277 -0.1320 -0.0336 106 VAL C N   
10085 C CA  . VAL C 106 ? 1.0053 1.0877 1.1169 -0.0280 -0.1154 -0.0352 106 VAL C CA  
10086 C C   . VAL C 106 ? 0.9885 1.1048 1.1481 -0.0332 -0.1223 -0.0418 106 VAL C C   
10087 O O   . VAL C 106 ? 0.9643 1.0960 1.1421 -0.0267 -0.1407 -0.0417 106 VAL C O   
10088 C CB  . VAL C 106 ? 0.9799 1.0612 1.0890 -0.0139 -0.1070 -0.0284 106 VAL C CB  
10089 C CG1 . VAL C 106 ? 1.0160 1.1131 1.1523 -0.0151 -0.0900 -0.0307 106 VAL C CG1 
10090 C CG2 . VAL C 106 ? 0.9597 1.0130 1.0267 -0.0094 -0.0996 -0.0234 106 VAL C CG2 
10100 N N   . ARG C 107 ? 1.0138 1.1414 1.1937 -0.0448 -0.1076 -0.0480 107 ARG C N   
10101 C CA  . ARG C 107 ? 1.0042 1.1680 1.2342 -0.0516 -0.1098 -0.0565 107 ARG C CA  
10102 C C   . ARG C 107 ? 1.0330 1.2068 1.2819 -0.0556 -0.0860 -0.0596 107 ARG C C   
10103 O O   . ARG C 107 ? 1.0034 1.1525 1.2224 -0.0589 -0.0695 -0.0562 107 ARG C O   
10104 C CB  . ARG C 107 ? 0.9941 1.1631 1.2298 -0.0699 -0.1182 -0.0645 107 ARG C CB  
10105 C CG  . ARG C 107 ? 0.9765 1.1235 1.1779 -0.0701 -0.1379 -0.0616 107 ARG C CG  
10106 C CD  . ARG C 107 ? 0.9586 1.0997 1.1533 -0.0911 -0.1407 -0.0694 107 ARG C CD  
10107 N NE  . ARG C 107 ? 1.0227 1.1299 1.1802 -0.1000 -0.1219 -0.0684 107 ARG C NE  
10108 C CZ  . ARG C 107 ? 1.0375 1.1080 1.1478 -0.0925 -0.1192 -0.0619 107 ARG C CZ  
10109 N NH1 . ARG C 107 ? 1.0740 1.1360 1.1657 -0.0782 -0.1314 -0.0560 107 ARG C NH1 
10110 N NH2 . ARG C 107 ? 1.0280 1.0689 1.1086 -0.0997 -0.1037 -0.0619 107 ARG C NH2 
10124 N N   . ASN C 108 ? 1.1658 1.3755 1.4639 -0.0547 -0.0846 -0.0664 108 ASN C N   
10125 C CA  . ASN C 108 ? 1.1319 1.3531 1.4500 -0.0601 -0.0608 -0.0712 108 ASN C CA  
10126 C C   . ASN C 108 ? 1.1250 1.3375 1.4336 -0.0833 -0.0459 -0.0771 108 ASN C C   
10127 O O   . ASN C 108 ? 1.1623 1.3775 1.4727 -0.0966 -0.0554 -0.0819 108 ASN C O   
10128 C CB  . ASN C 108 ? 1.1676 1.4316 1.5443 -0.0540 -0.0629 -0.0795 108 ASN C CB  
10129 C CG  . ASN C 108 ? 1.2001 1.4780 1.5992 -0.0623 -0.0361 -0.0869 108 ASN C CG  
10130 O OD1 . ASN C 108 ? 1.2345 1.5118 1.6326 -0.0827 -0.0213 -0.0932 108 ASN C OD1 
10131 N ND2 . ASN C 108 ? 1.1865 1.4739 1.6029 -0.0475 -0.0292 -0.0865 108 ASN C ND2 
10138 N N   . ASP C 109 ? 1.0648 1.2640 1.3601 -0.0890 -0.0228 -0.0766 109 ASP C N   
10139 C CA  . ASP C 109 ? 1.0872 1.2679 1.3626 -0.1108 -0.0069 -0.0802 109 ASP C CA  
10140 C C   . ASP C 109 ? 1.0792 1.2764 1.3791 -0.1228 0.0171  -0.0881 109 ASP C C   
10141 O O   . ASP C 109 ? 1.0769 1.2524 1.3531 -0.1410 0.0337  -0.0898 109 ASP C O   
10142 C CB  . ASP C 109 ? 1.0903 1.2234 1.3067 -0.1076 -0.0033 -0.0699 109 ASP C CB  
10143 C CG  . ASP C 109 ? 1.0959 1.2011 1.2839 -0.1283 0.0118  -0.0720 109 ASP C CG  
10144 O OD1 . ASP C 109 ? 1.0793 1.1973 1.2861 -0.1479 0.0151  -0.0810 109 ASP C OD1 
10145 O OD2 . ASP C 109 ? 1.1457 1.2157 1.2922 -0.1251 0.0200  -0.0646 109 ASP C OD2 
10150 N N   . GLY C 110 ? 1.0902 1.3227 1.4348 -0.1133 0.0200  -0.0935 110 GLY C N   
10151 C CA  . GLY C 110 ? 1.0690 1.3213 1.4415 -0.1257 0.0441  -0.1036 110 GLY C CA  
10152 C C   . GLY C 110 ? 1.0660 1.3300 1.4554 -0.1094 0.0535  -0.1035 110 GLY C C   
10153 O O   . GLY C 110 ? 1.1020 1.3942 1.5296 -0.1150 0.0703  -0.1145 110 GLY C O   
10157 N N   . ALA C 111 ? 1.0444 1.2866 1.4056 -0.0901 0.0441  -0.0921 111 ALA C N   
10158 C CA  . ALA C 111 ? 1.0065 1.2536 1.3770 -0.0747 0.0519  -0.0911 111 ALA C CA  
10159 C C   . ALA C 111 ? 0.9943 1.2244 1.3416 -0.0538 0.0326  -0.0792 111 ALA C C   
10160 O O   . ALA C 111 ? 1.0145 1.2316 1.3411 -0.0516 0.0148  -0.0728 111 ALA C O   
10161 C CB  . ALA C 111 ? 0.9977 1.2214 1.3390 -0.0850 0.0776  -0.0908 111 ALA C CB  
10167 N N   . LYS C 112 ? 0.9464 1.1748 1.2951 -0.0396 0.0376  -0.0768 112 LYS C N   
10168 C CA  . LYS C 112 ? 0.9230 1.1374 1.2531 -0.0211 0.0207  -0.0667 112 LYS C CA  
10169 C C   . LYS C 112 ? 0.9450 1.1229 1.2210 -0.0226 0.0204  -0.0559 112 LYS C C   
10170 O O   . LYS C 112 ? 0.9386 1.1043 1.1955 -0.0115 0.0053  -0.0479 112 LYS C O   
10171 C CB  . LYS C 112 ? 0.9503 1.1714 1.2967 -0.0067 0.0267  -0.0679 112 LYS C CB  
10172 C CG  . LYS C 112 ? 0.9643 1.2222 1.3676 -0.0024 0.0306  -0.0803 112 LYS C CG  
10173 C CD  . LYS C 112 ? 0.9731 1.2615 1.4147 -0.0068 0.0169  -0.0874 112 LYS C CD  
10174 C CE  . LYS C 112 ? 0.9987 1.3261 1.4968 -0.0108 0.0314  -0.1032 112 LYS C CE  
10175 N NZ  . LYS C 112 ? 0.9990 1.3569 1.5317 -0.0235 0.0242  -0.1121 112 LYS C NZ  
10189 N N   . ASN C 113 ? 0.9661 1.1260 1.2170 -0.0358 0.0365  -0.0559 113 ASN C N   
10190 C CA  . ASN C 113 ? 0.9578 1.0847 1.1607 -0.0359 0.0356  -0.0467 113 ASN C CA  
10191 C C   . ASN C 113 ? 0.9853 1.0976 1.1679 -0.0464 0.0297  -0.0456 113 ASN C C   
10192 O O   . ASN C 113 ? 0.9555 1.0405 1.1000 -0.0449 0.0276  -0.0387 113 ASN C O   
10193 C CB  . ASN C 113 ? 0.9469 1.0567 1.1278 -0.0416 0.0544  -0.0461 113 ASN C CB  
10194 C CG  . ASN C 113 ? 0.9892 1.0984 1.1732 -0.0607 0.0714  -0.0534 113 ASN C CG  
10195 O OD1 . ASN C 113 ? 1.0015 1.1362 1.2219 -0.0682 0.0749  -0.0624 113 ASN C OD1 
10196 N ND2 . ASN C 113 ? 1.0025 1.0823 1.1480 -0.0693 0.0820  -0.0497 113 ASN C ND2 
10203 N N   . LYS C 114 ? 0.9718 1.1016 1.1797 -0.0566 0.0267  -0.0528 114 LYS C N   
10204 C CA  . LYS C 114 ? 1.0057 1.1199 1.1943 -0.0692 0.0225  -0.0531 114 LYS C CA  
10205 C C   . LYS C 114 ? 1.0252 1.1498 1.2242 -0.0636 0.0010  -0.0529 114 LYS C C   
10206 O O   . LYS C 114 ? 1.0321 1.1868 1.2694 -0.0589 -0.0080 -0.0576 114 LYS C O   
10207 C CB  . LYS C 114 ? 1.0526 1.1750 1.2567 -0.0904 0.0376  -0.0624 114 LYS C CB  
10208 C CG  . LYS C 114 ? 1.0388 1.1394 1.2181 -0.0998 0.0592  -0.0616 114 LYS C CG  
10209 C CD  . LYS C 114 ? 1.0883 1.1947 1.2796 -0.1237 0.0760  -0.0713 114 LYS C CD  
10210 C CE  . LYS C 114 ? 1.1820 1.2463 1.3254 -0.1388 0.0806  -0.0674 114 LYS C CE  
10211 N NZ  . LYS C 114 ? 1.3251 1.3834 1.4657 -0.1631 0.1034  -0.0747 114 LYS C NZ  
10225 N N   . PHE C 115 ? 1.0070 1.1055 1.1709 -0.0638 -0.0077 -0.0481 115 PHE C N   
10226 C CA  . PHE C 115 ? 1.0225 1.1242 1.1864 -0.0588 -0.0278 -0.0472 115 PHE C CA  
10227 C C   . PHE C 115 ? 1.0113 1.0875 1.1452 -0.0701 -0.0310 -0.0480 115 PHE C C   
10228 O O   . PHE C 115 ? 0.9999 1.0484 1.1034 -0.0755 -0.0201 -0.0458 115 PHE C O   
10229 C CB  . PHE C 115 ? 0.9875 1.0807 1.1341 -0.0404 -0.0372 -0.0391 115 PHE C CB  
10230 C CG  . PHE C 115 ? 0.9530 1.0662 1.1249 -0.0286 -0.0363 -0.0379 115 PHE C CG  
10231 C CD1 . PHE C 115 ? 0.9617 1.1027 1.1712 -0.0249 -0.0471 -0.0421 115 PHE C CD1 
10232 C CD2 . PHE C 115 ? 0.9731 1.0760 1.1304 -0.0206 -0.0259 -0.0329 115 PHE C CD2 
10233 C CE1 . PHE C 115 ? 0.9222 1.0774 1.1531 -0.0126 -0.0466 -0.0413 115 PHE C CE1 
10234 C CE2 . PHE C 115 ? 0.9773 1.0946 1.1547 -0.0104 -0.0247 -0.0322 115 PHE C CE2 
10235 C CZ  . PHE C 115 ? 0.9331 1.0749 1.1465 -0.0059 -0.0347 -0.0363 115 PHE C CZ  
10245 N N   . LEU C 116 ? 1.0406 1.1243 1.1817 -0.0734 -0.0471 -0.0511 116 LEU C N   
10246 C CA  . LEU C 116 ? 1.0325 1.0894 1.1415 -0.0815 -0.0536 -0.0518 116 LEU C CA  
10247 C C   . LEU C 116 ? 1.0145 1.0622 1.1039 -0.0676 -0.0694 -0.0469 116 LEU C C   
10248 O O   . LEU C 116 ? 1.0291 1.0978 1.1392 -0.0620 -0.0840 -0.0473 116 LEU C O   
10249 C CB  . LEU C 116 ? 0.9994 1.0704 1.1293 -0.1004 -0.0588 -0.0610 116 LEU C CB  
10250 C CG  . LEU C 116 ? 1.0208 1.0891 1.1562 -0.1201 -0.0409 -0.0668 116 LEU C CG  
10251 C CD1 . LEU C 116 ? 0.9550 1.0458 1.1193 -0.1396 -0.0474 -0.0772 116 LEU C CD1 
10252 C CD2 . LEU C 116 ? 1.0520 1.0735 1.1373 -0.1248 -0.0310 -0.0627 116 LEU C CD2 
10264 N N   . ALA C 117 ? 1.0351 1.0509 1.0840 -0.0619 -0.0665 -0.0426 117 ALA C N   
10265 C CA  . ALA C 117 ? 1.0436 1.0489 1.0704 -0.0492 -0.0768 -0.0384 117 ALA C CA  
10266 C C   . ALA C 117 ? 1.0615 1.0372 1.0534 -0.0548 -0.0813 -0.0411 117 ALA C C   
10267 O O   . ALA C 117 ? 1.0828 1.0332 1.0513 -0.0574 -0.0712 -0.0415 117 ALA C O   
10268 C CB  . ALA C 117 ? 1.0114 1.0099 1.0254 -0.0345 -0.0675 -0.0318 117 ALA C CB  
10274 N N   . LYS C 118 ? 1.0759 1.0520 1.0617 -0.0559 -0.0969 -0.0429 118 LYS C N   
10275 C CA  . LYS C 118 ? 1.1068 1.0536 1.0570 -0.0608 -0.1019 -0.0464 118 LYS C CA  
10276 C C   . LYS C 118 ? 1.0953 1.0287 1.0180 -0.0473 -0.1048 -0.0427 118 LYS C C   
10277 O O   . LYS C 118 ? 1.0874 1.0363 1.0193 -0.0401 -0.1129 -0.0388 118 LYS C O   
10278 C CB  . LYS C 118 ? 1.1294 1.0840 1.0889 -0.0755 -0.1177 -0.0526 118 LYS C CB  
10279 C CG  . LYS C 118 ? 1.1818 1.1099 1.1038 -0.0780 -0.1283 -0.0555 118 LYS C CG  
10280 C CD  . LYS C 118 ? 1.2180 1.1422 1.1404 -0.0979 -0.1382 -0.0637 118 LYS C CD  
10281 C CE  . LYS C 118 ? 1.2374 1.2015 1.2051 -0.1056 -0.1524 -0.0662 118 LYS C CE  
10282 N NZ  . LYS C 118 ? 1.2335 1.2033 1.1960 -0.1036 -0.1756 -0.0660 118 LYS C NZ  
10296 N N   . ILE C 119 ? 1.1310 1.0344 1.0191 -0.0442 -0.0976 -0.0444 119 ILE C N   
10297 C CA  . ILE C 119 ? 1.0993 0.9902 0.9618 -0.0318 -0.0952 -0.0426 119 ILE C CA  
10298 C C   . ILE C 119 ? 1.1881 1.0466 1.0134 -0.0354 -0.0959 -0.0489 119 ILE C C   
10299 O O   . ILE C 119 ? 1.2164 1.0560 1.0321 -0.0434 -0.0931 -0.0534 119 ILE C O   
10300 C CB  . ILE C 119 ? 1.1359 1.0289 1.0009 -0.0185 -0.0804 -0.0384 119 ILE C CB  
10301 C CG1 . ILE C 119 ? 1.1204 1.0145 0.9719 -0.0072 -0.0783 -0.0362 119 ILE C CG1 
10302 C CG2 . ILE C 119 ? 1.1558 1.0232 1.0026 -0.0174 -0.0703 -0.0415 119 ILE C CG2 
10303 C CD1 . ILE C 119 ? 1.1148 1.0103 0.9664 0.0053  -0.0647 -0.0341 119 ILE C CD1 
10315 N N   . LYS C 120 ? 1.2256 1.0749 1.0271 -0.0303 -0.0989 -0.0497 120 LYS C N   
10316 C CA  . LYS C 120 ? 1.2166 1.0336 0.9799 -0.0318 -0.0971 -0.0568 120 LYS C CA  
10317 C C   . LYS C 120 ? 1.2004 1.0030 0.9511 -0.0182 -0.0804 -0.0584 120 LYS C C   
10318 O O   . LYS C 120 ? 1.1713 0.9884 0.9307 -0.0063 -0.0726 -0.0546 120 LYS C O   
10319 C CB  . LYS C 120 ? 1.2675 1.0787 1.0072 -0.0330 -0.1057 -0.0577 120 LYS C CB  
10320 C CG  . LYS C 120 ? 1.2712 1.0475 0.9684 -0.0355 -0.1027 -0.0663 120 LYS C CG  
10321 C CD  . LYS C 120 ? 1.3262 1.0941 0.9964 -0.0411 -0.1136 -0.0672 120 LYS C CD  
10322 C CE  . LYS C 120 ? 1.3857 1.1658 1.0688 -0.0541 -0.1358 -0.0648 120 LYS C CE  
10323 N NZ  . LYS C 120 ? 1.3454 1.1037 0.9904 -0.0636 -0.1494 -0.0686 120 LYS C NZ  
10337 N N   . MET C 121 ? 1.1988 0.9721 0.9289 -0.0199 -0.0758 -0.0645 121 MET C N   
10338 C CA  . MET C 121 ? 1.2198 0.9789 0.9401 -0.0048 -0.0622 -0.0666 121 MET C CA  
10339 C C   . MET C 121 ? 1.2438 0.9791 0.9309 0.0014  -0.0569 -0.0749 121 MET C C   
10340 O O   . MET C 121 ? 1.2963 1.0134 0.9595 -0.0093 -0.0636 -0.0803 121 MET C O   
10341 C CB  . MET C 121 ? 1.2392 0.9764 0.9561 -0.0073 -0.0592 -0.0676 121 MET C CB  
10342 C CG  . MET C 121 ? 1.2566 1.0135 1.0031 -0.0130 -0.0598 -0.0604 121 MET C CG  
10343 S SD  . MET C 121 ? 1.2416 1.0314 1.0175 0.0015  -0.0530 -0.0521 121 MET C SD  
10344 C CE  . MET C 121 ? 1.1791 0.9513 0.9360 0.0226  -0.0432 -0.0557 121 MET C CE  
10354 N N   . PRO C 122 ? 1.2315 0.9677 0.9170 0.0183  -0.0448 -0.0770 122 PRO C N   
10355 C CA  . PRO C 122 ? 1.2927 1.0052 0.9482 0.0254  -0.0366 -0.0871 122 PRO C CA  
10356 C C   . PRO C 122 ? 1.3673 1.0392 0.9936 0.0190  -0.0389 -0.0947 122 PRO C C   
10357 O O   . PRO C 122 ? 1.3676 1.0253 0.9968 0.0160  -0.0417 -0.0928 122 PRO C O   
10358 C CB  . PRO C 122 ? 1.2119 0.9344 0.8809 0.0459  -0.0240 -0.0884 122 PRO C CB  
10359 C CG  . PRO C 122 ? 1.1933 0.9388 0.8943 0.0477  -0.0274 -0.0781 122 PRO C CG  
10360 C CD  . PRO C 122 ? 1.2190 0.9822 0.9316 0.0312  -0.0379 -0.0712 122 PRO C CD  
10368 N N   . LYS C 123 ? 1.3220 0.9723 0.9165 0.0157  -0.0370 -0.1037 123 LYS C N   
10369 C CA  . LYS C 123 ? 1.4264 1.0339 0.9879 0.0101  -0.0377 -0.1127 123 LYS C CA  
10370 C C   . LYS C 123 ? 1.4415 1.0267 0.9952 0.0299  -0.0250 -0.1193 123 LYS C C   
10371 O O   . LYS C 123 ? 1.3631 0.9675 0.9335 0.0480  -0.0149 -0.1195 123 LYS C O   
10372 C CB  . LYS C 123 ? 1.3942 0.9845 0.9211 -0.0001 -0.0396 -0.1207 123 LYS C CB  
10373 C CG  . LYS C 123 ? 1.4406 1.0232 0.9496 0.0146  -0.0232 -0.1302 123 LYS C CG  
10374 C CD  . LYS C 123 ? 1.5037 1.0866 0.9877 0.0041  -0.0241 -0.1335 123 LYS C CD  
10375 C CE  . LYS C 123 ? 1.5104 1.0787 0.9738 -0.0185 -0.0429 -0.1319 123 LYS C CE  
10376 N NZ  . LYS C 123 ? 1.5824 1.1313 1.0038 -0.0276 -0.0423 -0.1392 123 LYS C NZ  
10390 N N   . PHE C 124 ? 1.4691 1.0126 0.9972 0.0262  -0.0262 -0.1250 124 PHE C N   
10391 C CA  . PHE C 124 ? 1.5363 1.0515 1.0530 0.0462  -0.0162 -0.1318 124 PHE C CA  
10392 C C   . PHE C 124 ? 1.5509 1.0508 1.0432 0.0565  -0.0044 -0.1454 124 PHE C C   
10393 O O   . PHE C 124 ? 1.5818 1.0739 1.0506 0.0427  -0.0056 -0.1508 124 PHE C O   
10394 C CB  . PHE C 124 ? 1.5918 1.0618 1.0856 0.0385  -0.0212 -0.1330 124 PHE C CB  
10395 C CG  . PHE C 124 ? 1.5963 1.0330 1.0544 0.0179  -0.0264 -0.1407 124 PHE C CG  
10396 C CD1 . PHE C 124 ? 1.6029 1.0460 1.0646 -0.0077 -0.0392 -0.1355 124 PHE C CD1 
10397 C CD2 . PHE C 124 ? 1.6625 1.0619 1.0841 0.0238  -0.0187 -0.1542 124 PHE C CD2 
10398 C CE1 . PHE C 124 ? 1.6229 1.0372 1.0527 -0.0279 -0.0459 -0.1430 124 PHE C CE1 
10399 C CE2 . PHE C 124 ? 1.7274 1.0941 1.1131 0.0034  -0.0243 -0.1617 124 PHE C CE2 
10400 C CZ  . PHE C 124 ? 1.7269 1.1016 1.1169 -0.0230 -0.0389 -0.1558 124 PHE C CZ  
10410 N N   . LEU C 125 ? 1.6024 1.0985 1.1007 0.0811  0.0069  -0.1513 125 LEU C N   
10411 C CA  . LEU C 125 ? 1.6140 1.0948 1.0920 0.0938  0.0212  -0.1664 125 LEU C CA  
10412 C C   . LEU C 125 ? 1.6755 1.0991 1.1170 0.0989  0.0236  -0.1771 125 LEU C C   
10413 O O   . LEU C 125 ? 1.6842 1.0847 1.0971 0.1009  0.0338  -0.1911 125 LEU C O   
10414 C CB  . LEU C 125 ? 1.5847 1.0990 1.0948 0.1190  0.0330  -0.1690 125 LEU C CB  
10415 C CG  . LEU C 125 ? 1.6146 1.1826 1.1643 0.1166  0.0297  -0.1567 125 LEU C CG  
10416 C CD1 . LEU C 125 ? 1.6244 1.2254 1.2038 0.1396  0.0425  -0.1622 125 LEU C CD1 
10417 C CD2 . LEU C 125 ? 1.5894 1.1748 1.1319 0.0939  0.0262  -0.1526 125 LEU C CD2 
10429 N N   . SER C 126 ? 1.7089 1.1062 1.1477 0.1001  0.0153  -0.1713 126 SER C N   
10430 C CA  . SER C 126 ? 1.7430 1.0796 1.1433 0.1025  0.0160  -0.1801 126 SER C CA  
10431 C C   . SER C 126 ? 1.7138 1.0272 1.1066 0.0853  0.0028  -0.1696 126 SER C C   
10432 O O   . SER C 126 ? 1.7252 1.0670 1.1474 0.0832  -0.0040 -0.1565 126 SER C O   
10433 C CB  . SER C 126 ? 1.7495 1.0689 1.1526 0.1358  0.0255  -0.1882 126 SER C CB  
10434 O OG  . SER C 126 ? 1.7732 1.1321 1.2009 0.1535  0.0381  -0.1954 126 SER C OG  
10440 N N   . LEU C 127 ? 1.7445 1.0054 1.0964 0.0714  0.0002  -0.1762 127 LEU C N   
10441 C CA  . LEU C 127 ? 1.7869 1.0168 1.1252 0.0535  -0.0097 -0.1689 127 LEU C CA  
10442 C C   . LEU C 127 ? 1.8390 0.9983 1.1307 0.0586  -0.0060 -0.1796 127 LEU C C   
10443 O O   . LEU C 127 ? 1.8502 0.9831 1.1107 0.0536  -0.0013 -0.1926 127 LEU C O   
10444 C CB  . LEU C 127 ? 1.8125 1.0590 1.1515 0.0190  -0.0200 -0.1646 127 LEU C CB  
10445 C CG  . LEU C 127 ? 1.8549 1.0737 1.1813 -0.0052 -0.0287 -0.1592 127 LEU C CG  
10446 C CD1 . LEU C 127 ? 1.8201 1.0844 1.1744 -0.0319 -0.0391 -0.1514 127 LEU C CD1 
10447 C CD2 . LEU C 127 ? 1.8772 1.0322 1.1528 -0.0179 -0.0284 -0.1708 127 LEU C CD2 
10459 N N   . GLU C 128 ? 1.8943 1.0194 1.1775 0.0680  -0.0083 -0.1743 128 GLU C N   
10460 C CA  . GLU C 128 ? 1.9466 1.0008 1.1857 0.0791  -0.0046 -0.1840 128 GLU C CA  
10461 C C   . GLU C 128 ? 2.0061 1.0224 1.2317 0.0750  -0.0116 -0.1735 128 GLU C C   
10462 O O   . GLU C 128 ? 1.9971 1.0451 1.2522 0.0754  -0.0166 -0.1600 128 GLU C O   
10463 C CB  . GLU C 128 ? 1.9167 0.9685 1.1612 0.1175  0.0056  -0.1940 128 GLU C CB  
10464 C CG  . GLU C 128 ? 1.9245 1.0380 1.2207 0.1396  0.0062  -0.1859 128 GLU C CG  
10465 C CD  . GLU C 128 ? 1.9206 1.0464 1.2300 0.1735  0.0179  -0.1986 128 GLU C CD  
10466 O OE1 . GLU C 128 ? 1.9220 0.9976 1.1996 0.1879  0.0244  -0.2121 128 GLU C OE1 
10467 O OE2 . GLU C 128 ? 1.8821 1.0680 1.2343 0.1851  0.0213  -0.1958 128 GLU C OE2 
10474 N N   . GLU C 129 ? 2.0915 1.0352 1.2682 0.0702  -0.0113 -0.1801 129 GLU C N   
10475 C CA  . GLU C 129 ? 2.1863 1.0793 1.3386 0.0676  -0.0165 -0.1715 129 GLU C CA  
10476 C C   . GLU C 129 ? 2.3027 1.1511 1.4375 0.1067  -0.0140 -0.1760 129 GLU C C   
10477 O O   . GLU C 129 ? 2.3221 1.1241 1.4241 0.1179  -0.0083 -0.1901 129 GLU C O   
10478 C CB  . GLU C 129 ? 2.1661 1.0050 1.2737 0.0323  -0.0188 -0.1748 129 GLU C CB  
10479 C CG  . GLU C 129 ? 2.3141 1.1082 1.3989 0.0205  -0.0235 -0.1636 129 GLU C CG  
10480 C CD  . GLU C 129 ? 2.2727 1.0730 1.3544 -0.0249 -0.0268 -0.1594 129 GLU C CD  
10481 O OE1 . GLU C 129 ? 2.3038 1.0662 1.3511 -0.0490 -0.0264 -0.1691 129 GLU C OE1 
10482 O OE2 . GLU C 129 ? 2.2727 1.1159 1.3870 -0.0366 -0.0296 -0.1472 129 GLU C OE2 
10489 N N   . ILE C 130 ? 2.5013 1.3648 1.6587 0.1280  -0.0189 -0.1647 130 ILE C N   
10490 C CA  . ILE C 130 ? 2.4954 1.3177 1.6391 0.1660  -0.0206 -0.1667 130 ILE C CA  
10491 C C   . ILE C 130 ? 2.5804 1.3262 1.6758 0.1562  -0.0277 -0.1585 130 ILE C C   
10492 O O   . ILE C 130 ? 2.6198 1.3617 1.7060 0.1231  -0.0309 -0.1484 130 ILE C O   
10493 C CB  . ILE C 130 ? 2.4574 1.3402 1.6524 0.1942  -0.0240 -0.1590 130 ILE C CB  
10494 C CG1 . ILE C 130 ? 2.4648 1.3896 1.6914 0.2226  -0.0149 -0.1730 130 ILE C CG1 
10495 C CG2 . ILE C 130 ? 2.5165 1.3578 1.6970 0.2193  -0.0340 -0.1502 130 ILE C CG2 
10496 C CD1 . ILE C 130 ? 2.4498 1.4059 1.6819 0.2012  -0.0049 -0.1832 130 ILE C CD1 
10508 N N   . ASN C 131 ? 2.6195 1.3011 1.6819 0.1855  -0.0296 -0.1638 131 ASN C N   
10509 C CA  . ASN C 131 ? 2.6679 1.2652 1.6764 0.1802  -0.0367 -0.1561 131 ASN C CA  
10510 C C   . ASN C 131 ? 2.6725 1.2451 1.6809 0.2259  -0.0453 -0.1528 131 ASN C C   
10511 O O   . ASN C 131 ? 2.7168 1.2465 1.7056 0.2558  -0.0437 -0.1650 131 ASN C O   
10512 C CB  . ASN C 131 ? 2.7428 1.2644 1.6937 0.1632  -0.0313 -0.1683 131 ASN C CB  
10513 C CG  . ASN C 131 ? 2.7527 1.2661 1.6836 0.1113  -0.0298 -0.1642 131 ASN C CG  
10514 O OD1 . ASN C 131 ? 2.8381 1.2829 1.7205 0.0917  -0.0325 -0.1591 131 ASN C OD1 
10515 N ND2 . ASN C 131 ? 2.7061 1.2890 1.6739 0.0884  -0.0256 -0.1670 131 ASN C ND2 
10522 N N   . VAL C 132 ? 2.6804 1.2807 1.7112 0.2320  -0.0549 -0.1370 132 VAL C N   
10523 C CA  . VAL C 132 ? 2.6978 1.2785 1.7303 0.2745  -0.0666 -0.1322 132 VAL C CA  
10524 C C   . VAL C 132 ? 2.7583 1.2422 1.7254 0.2704  -0.0763 -0.1223 132 VAL C C   
10525 O O   . VAL C 132 ? 2.7511 1.2105 1.6893 0.2317  -0.0756 -0.1119 132 VAL C O   
10526 C CB  . VAL C 132 ? 2.6650 1.3228 1.7523 0.2846  -0.0734 -0.1207 132 VAL C CB  
10527 C CG1 . VAL C 132 ? 2.5948 1.3462 1.7420 0.2797  -0.0627 -0.1285 132 VAL C CG1 
10528 C CG2 . VAL C 132 ? 2.6374 1.2844 1.7072 0.2539  -0.0795 -0.1019 132 VAL C CG2 
10538 N N   . ASP C 133 ? 2.8340 1.2629 1.7783 0.3109  -0.0854 -0.1256 133 ASP C N   
10539 C CA  . ASP C 133 ? 2.8557 1.1901 1.7359 0.3119  -0.0958 -0.1161 133 ASP C CA  
10540 C C   . ASP C 133 ? 2.9025 1.1866 1.7317 0.2619  -0.0873 -0.1135 133 ASP C C   
10541 O O   . ASP C 133 ? 2.9973 1.2599 1.8084 0.2502  -0.0770 -0.1265 133 ASP C O   
10542 C CB  . ASP C 133 ? 2.8771 1.2153 1.7607 0.3233  -0.1123 -0.0971 133 ASP C CB  
10543 C CG  . ASP C 133 ? 2.8916 1.2739 1.8224 0.3748  -0.1240 -0.0996 133 ASP C CG  
10544 O OD1 . ASP C 133 ? 2.8216 1.2723 1.8073 0.3910  -0.1167 -0.1119 133 ASP C OD1 
10545 O OD2 . ASP C 133 ? 2.9597 1.3161 1.8760 0.3964  -0.1403 -0.0891 133 ASP C OD2 
10550 N N   . GLU C 134 ? 2.8240 1.0918 1.6313 0.2310  -0.0907 -0.0976 134 GLU C N   
10551 C CA  . GLU C 134 ? 2.8328 1.0579 1.5953 0.1810  -0.0822 -0.0949 134 GLU C CA  
10552 C C   . GLU C 134 ? 2.7690 1.0553 1.5638 0.1399  -0.0708 -0.0974 134 GLU C C   
10553 O O   . GLU C 134 ? 2.7524 1.0105 1.5180 0.0997  -0.0623 -0.1014 134 GLU C O   
10554 C CB  . GLU C 134 ? 2.8772 1.0546 1.5967 0.1663  -0.0901 -0.0759 134 GLU C CB  
10555 C CG  . GLU C 134 ? 2.9452 1.0706 1.6129 0.1187  -0.0812 -0.0739 134 GLU C CG  
10556 C CD  . GLU C 134 ? 2.9749 1.0343 1.5871 0.1180  -0.0893 -0.0598 134 GLU C CD  
10557 O OE1 . GLU C 134 ? 2.9698 1.0281 1.5726 0.1047  -0.0932 -0.0450 134 GLU C OE1 
10558 O OE2 . GLU C 134 ? 2.9845 0.9917 1.5603 0.1301  -0.0915 -0.0638 134 GLU C OE2 
10565 N N   . TYR C 135 ? 2.7455 1.1272 1.6065 0.1478  -0.0708 -0.0946 135 TYR C N   
10566 C CA  . TYR C 135 ? 2.6696 1.1253 1.5708 0.1102  -0.0624 -0.0926 135 TYR C CA  
10567 C C   . TYR C 135 ? 2.6242 1.1466 1.5713 0.1131  -0.0547 -0.1072 135 TYR C C   
10568 O O   . TYR C 135 ? 2.6382 1.1675 1.5986 0.1484  -0.0551 -0.1176 135 TYR C O   
10569 C CB  . TYR C 135 ? 2.5879 1.0992 1.5262 0.1138  -0.0679 -0.0777 135 TYR C CB  
10570 C CG  . TYR C 135 ? 2.6493 1.0923 1.5386 0.1139  -0.0765 -0.0628 135 TYR C CG  
10571 C CD1 . TYR C 135 ? 2.7033 1.0916 1.5442 0.0728  -0.0711 -0.0568 135 TYR C CD1 
10572 C CD2 . TYR C 135 ? 2.6728 1.1050 1.5626 0.1541  -0.0904 -0.0550 135 TYR C CD2 
10573 C CE1 . TYR C 135 ? 2.7560 1.0769 1.5459 0.0706  -0.0780 -0.0428 135 TYR C CE1 
10574 C CE2 . TYR C 135 ? 2.6794 1.0448 1.5189 0.1539  -0.1000 -0.0405 135 TYR C CE2 
10575 C CZ  . TYR C 135 ? 2.7472 1.0545 1.5342 0.1117  -0.0931 -0.0342 135 TYR C CZ  
10576 O OH  . TYR C 135 ? 2.8428 1.0790 1.5739 0.1093  -0.1017 -0.0195 135 TYR C OH  
10586 N N   . LYS C 136 ? 2.6057 1.1756 1.5752 0.0748  -0.0476 -0.1085 136 LYS C N   
10587 C CA  . LYS C 136 ? 2.5669 1.2050 1.5799 0.0726  -0.0416 -0.1197 136 LYS C CA  
10588 C C   . LYS C 136 ? 2.4638 1.1927 1.5366 0.0642  -0.0417 -0.1112 136 LYS C C   
10589 O O   . LYS C 136 ? 2.4235 1.1607 1.5001 0.0468  -0.0435 -0.0986 136 LYS C O   
10590 C CB  . LYS C 136 ? 2.5632 1.1787 1.5508 0.0364  -0.0355 -0.1305 136 LYS C CB  
10591 C CG  . LYS C 136 ? 2.5387 1.1593 1.5218 -0.0110 -0.0339 -0.1235 136 LYS C CG  
10592 C CD  . LYS C 136 ? 2.4942 1.1227 1.4729 -0.0459 -0.0299 -0.1354 136 LYS C CD  
10593 C CE  . LYS C 136 ? 2.5459 1.1137 1.4810 -0.0366 -0.0278 -0.1505 136 LYS C CE  
10594 N NZ  . LYS C 136 ? 2.7186 1.1868 1.5868 -0.0444 -0.0276 -0.1504 136 LYS C NZ  
10608 N N   . LEU C 137 ? 2.4251 1.2194 1.5422 0.0763  -0.0387 -0.1186 137 LEU C N   
10609 C CA  . LEU C 137 ? 2.3684 1.2473 1.5428 0.0759  -0.0391 -0.1114 137 LEU C CA  
10610 C C   . LEU C 137 ? 2.2945 1.2282 1.5011 0.0771  -0.0340 -0.1224 137 LEU C C   
10611 O O   . LEU C 137 ? 2.2824 1.2025 1.4813 0.0999  -0.0306 -0.1342 137 LEU C O   
10612 C CB  . LEU C 137 ? 2.3186 1.2132 1.5131 0.1110  -0.0450 -0.1031 137 LEU C CB  
10613 C CG  . LEU C 137 ? 2.4354 1.3072 1.6237 0.1524  -0.0461 -0.1128 137 LEU C CG  
10614 C CD1 . LEU C 137 ? 2.3713 1.3017 1.6074 0.1837  -0.0499 -0.1090 137 LEU C CD1 
10615 C CD2 . LEU C 137 ? 2.5002 1.2808 1.6320 0.1644  -0.0518 -0.1115 137 LEU C CD2 
10627 N N   . GLY C 138 ? 2.1197 1.1129 1.3606 0.0526  -0.0332 -0.1190 138 GLY C N   
10628 C CA  . GLY C 138 ? 2.0608 1.1008 1.3259 0.0484  -0.0298 -0.1280 138 GLY C CA  
10629 C C   . GLY C 138 ? 1.9613 1.0693 1.2751 0.0707  -0.0286 -0.1256 138 GLY C C   
10630 O O   . GLY C 138 ? 1.9803 1.1412 1.3298 0.0599  -0.0306 -0.1166 138 GLY C O   
10634 N N   . LEU C 139 ? 1.9663 1.0734 1.2822 0.1012  -0.0243 -0.1345 139 LEU C N   
10635 C CA  . LEU C 139 ? 1.8566 1.0277 1.2175 0.1209  -0.0213 -0.1344 139 LEU C CA  
10636 C C   . LEU C 139 ? 1.8191 1.0395 1.2010 0.1003  -0.0187 -0.1369 139 LEU C C   
10637 O O   . LEU C 139 ? 1.8286 1.0312 1.1879 0.0876  -0.0158 -0.1470 139 LEU C O   
10638 C CB  . LEU C 139 ? 1.8553 1.0138 1.2133 0.1556  -0.0153 -0.1463 139 LEU C CB  
10639 C CG  . LEU C 139 ? 1.9229 1.1005 1.3078 0.1881  -0.0184 -0.1414 139 LEU C CG  
10640 C CD1 . LEU C 139 ? 1.9930 1.1293 1.3598 0.2212  -0.0154 -0.1535 139 LEU C CD1 
10641 C CD2 . LEU C 139 ? 1.8442 1.0988 1.2800 0.1940  -0.0150 -0.1394 139 LEU C CD2 
10653 N N   . VAL C 140 ? 1.7562 1.0357 1.1790 0.0970  -0.0207 -0.1277 140 VAL C N   
10654 C CA  . VAL C 140 ? 1.7242 1.0539 1.1705 0.0833  -0.0193 -0.1288 140 VAL C CA  
10655 C C   . VAL C 140 ? 1.6895 1.0694 1.1732 0.1062  -0.0147 -0.1275 140 VAL C C   
10656 O O   . VAL C 140 ? 1.6822 1.0954 1.1951 0.1081  -0.0183 -0.1166 140 VAL C O   
10657 C CB  . VAL C 140 ? 1.6330 0.9860 1.0933 0.0537  -0.0264 -0.1191 140 VAL C CB  
10658 C CG1 . VAL C 140 ? 1.5788 0.9889 1.0700 0.0466  -0.0269 -0.1177 140 VAL C CG1 
10659 C CG2 . VAL C 140 ? 1.7101 1.0211 1.1366 0.0273  -0.0302 -0.1234 140 VAL C CG2 
10669 N N   . ARG C 141 ? 1.6797 1.0645 1.1617 0.1225  -0.0060 -0.1391 141 ARG C N   
10670 C CA  . ARG C 141 ? 1.6736 1.1041 1.1903 0.1441  0.0001  -0.1402 141 ARG C CA  
10671 C C   . ARG C 141 ? 1.6419 1.1265 1.1855 0.1291  0.0007  -0.1350 141 ARG C C   
10672 O O   . ARG C 141 ? 1.6195 1.1045 1.1516 0.1055  -0.0026 -0.1342 141 ARG C O   
10673 C CB  . ARG C 141 ? 1.6854 1.1029 1.1918 0.1657  0.0118  -0.1563 141 ARG C CB  
10674 C CG  . ARG C 141 ? 1.7563 1.1190 1.2371 0.1852  0.0112  -0.1624 141 ARG C CG  
10675 C CD  . ARG C 141 ? 1.8174 1.1753 1.2975 0.2116  0.0241  -0.1795 141 ARG C CD  
10676 N NE  . ARG C 141 ? 1.8777 1.2190 1.3658 0.2423  0.0204  -0.1801 141 ARG C NE  
10677 C CZ  . ARG C 141 ? 1.9001 1.1823 1.3568 0.2482  0.0125  -0.1780 141 ARG C CZ  
10678 N NH1 . ARG C 141 ? 1.9119 1.1432 1.3255 0.2266  0.0107  -0.1789 141 ARG C NH1 
10679 N NH2 . ARG C 141 ? 1.9682 1.2411 1.4357 0.2751  0.0050  -0.1746 141 ARG C NH2 
10693 N N   . PHE C 142 ? 1.6860 1.2154 1.2652 0.1431  0.0036  -0.1314 142 PHE C N   
10694 C CA  . PHE C 142 ? 1.6226 1.2016 1.2269 0.1324  0.0053  -0.1269 142 PHE C CA  
10695 C C   . PHE C 142 ? 1.6131 1.2284 1.2447 0.1532  0.0152  -0.1323 142 PHE C C   
10696 O O   . PHE C 142 ? 1.6494 1.2590 1.2891 0.1765  0.0175  -0.1368 142 PHE C O   
10697 C CB  . PHE C 142 ? 1.5487 1.1515 1.1747 0.1189  -0.0045 -0.1119 142 PHE C CB  
10698 C CG  . PHE C 142 ? 1.5219 1.1034 1.1306 0.0944  -0.0132 -0.1069 142 PHE C CG  
10699 C CD1 . PHE C 142 ? 1.5348 1.0785 1.1262 0.0910  -0.0184 -0.1040 142 PHE C CD1 
10700 C CD2 . PHE C 142 ? 1.4889 1.0887 1.0994 0.0742  -0.0167 -0.1051 142 PHE C CD2 
10701 C CE1 . PHE C 142 ? 1.5304 1.0584 1.1094 0.0665  -0.0251 -0.1005 142 PHE C CE1 
10702 C CE2 . PHE C 142 ? 1.4877 1.0732 1.0879 0.0518  -0.0257 -0.1017 142 PHE C CE2 
10703 C CZ  . PHE C 142 ? 1.5135 1.0648 1.0994 0.0472  -0.0289 -0.1000 142 PHE C CZ  
10713 N N   . SER C 143 ? 1.5969 1.2504 1.2437 0.1444  0.0202  -0.1315 143 SER C N   
10714 C CA  . SER C 143 ? 1.5959 1.2902 1.2723 0.1593  0.0301  -0.1357 143 SER C CA  
10715 C C   . SER C 143 ? 1.5967 1.3188 1.3060 0.1670  0.0227  -0.1249 143 SER C C   
10716 O O   . SER C 143 ? 1.5872 1.3375 1.3127 0.1540  0.0188  -0.1149 143 SER C O   
10717 C CB  . SER C 143 ? 1.5504 1.2715 1.2275 0.1442  0.0375  -0.1369 143 SER C CB  
10718 O OG  . SER C 143 ? 1.5098 1.2313 1.1806 0.1220  0.0265  -0.1255 143 SER C OG  
10724 N N   . GLY C 144 ? 1.6310 1.3433 1.3483 0.1884  0.0199  -0.1268 144 GLY C N   
10725 C CA  . GLY C 144 ? 1.6465 1.3799 1.3896 0.1960  0.0113  -0.1167 144 GLY C CA  
10726 C C   . GLY C 144 ? 1.7298 1.4239 1.4580 0.2068  0.0005  -0.1123 144 GLY C C   
10727 O O   . GLY C 144 ? 1.7776 1.4745 1.5192 0.2297  -0.0029 -0.1144 144 GLY C O   
10731 N N   . ILE C 145 ? 1.8051 1.4614 1.5046 0.1901  -0.0055 -0.1065 145 ILE C N   
10732 C CA  . ILE C 145 ? 1.8982 1.5096 1.5757 0.1954  -0.0149 -0.1014 145 ILE C CA  
10733 C C   . ILE C 145 ? 1.9027 1.4634 1.5411 0.1863  -0.0134 -0.1075 145 ILE C C   
10734 O O   . ILE C 145 ? 1.8667 1.4293 1.4955 0.1672  -0.0092 -0.1105 145 ILE C O   
10735 C CB  . ILE C 145 ? 1.9116 1.5278 1.5935 0.1796  -0.0235 -0.0865 145 ILE C CB  
10736 C CG1 . ILE C 145 ? 1.8944 1.4582 1.5468 0.1823  -0.0320 -0.0811 145 ILE C CG1 
10737 C CG2 . ILE C 145 ? 1.8982 1.5264 1.5790 0.1511  -0.0218 -0.0825 145 ILE C CG2 
10738 C CD1 . ILE C 145 ? 1.8370 1.4047 1.4933 0.1709  -0.0389 -0.0675 145 ILE C CD1 
10750 N N   . ASN C 146 ? 1.8152 1.3279 1.4291 0.2001  -0.0178 -0.1094 146 ASN C N   
10751 C CA  . ASN C 146 ? 1.7792 1.2357 1.3516 0.1909  -0.0174 -0.1145 146 ASN C CA  
10752 C C   . ASN C 146 ? 1.7507 1.1688 1.3002 0.1780  -0.0269 -0.1031 146 ASN C C   
10753 O O   . ASN C 146 ? 1.7456 1.1422 1.2894 0.1944  -0.0338 -0.0980 146 ASN C O   
10754 C CB  . ASN C 146 ? 1.8002 1.2243 1.3569 0.2173  -0.0130 -0.1279 146 ASN C CB  
10755 C CG  . ASN C 146 ? 1.8278 1.2978 1.4190 0.2396  -0.0044 -0.1377 146 ASN C CG  
10756 O OD1 . ASN C 146 ? 1.7700 1.2705 1.3713 0.2307  0.0059  -0.1445 146 ASN C OD1 
10757 N ND2 . ASN C 146 ? 1.8726 1.3474 1.4811 0.2682  -0.0090 -0.1386 146 ASN C ND2 
10764 N N   . HIS C 147 ? 1.7069 1.1163 1.2429 0.1481  -0.0274 -0.0994 147 HIS C N   
10765 C CA  . HIS C 147 ? 1.6820 1.0596 1.1981 0.1304  -0.0335 -0.0894 147 HIS C CA  
10766 C C   . HIS C 147 ? 1.7267 1.0352 1.1959 0.1271  -0.0343 -0.0947 147 HIS C C   
10767 O O   . HIS C 147 ? 1.7868 1.0776 1.2386 0.1228  -0.0299 -0.1054 147 HIS C O   
10768 C CB  . HIS C 147 ? 1.6621 1.0702 1.1928 0.0994  -0.0333 -0.0840 147 HIS C CB  
10769 C CG  . HIS C 147 ? 1.6374 1.1059 1.2099 0.1006  -0.0333 -0.0771 147 HIS C CG  
10770 N ND1 . HIS C 147 ? 1.6042 1.0866 1.1891 0.0892  -0.0361 -0.0661 147 HIS C ND1 
10771 C CD2 . HIS C 147 ? 1.6430 1.1586 1.2451 0.1110  -0.0298 -0.0801 147 HIS C CD2 
10772 C CE1 . HIS C 147 ? 1.5375 1.0724 1.1580 0.0933  -0.0351 -0.0628 147 HIS C CE1 
10773 N NE2 . HIS C 147 ? 1.5747 1.1302 1.2060 0.1061  -0.0315 -0.0707 147 HIS C NE2 
10781 N N   . PHE C 148 ? 1.7581 1.0239 1.2032 0.1281  -0.0398 -0.0870 148 PHE C N   
10782 C CA  . PHE C 148 ? 1.8031 0.9950 1.1991 0.1272  -0.0413 -0.0905 148 PHE C CA  
10783 C C   . PHE C 148 ? 1.8393 1.0055 1.2134 0.0931  -0.0422 -0.0827 148 PHE C C   
10784 O O   . PHE C 148 ? 1.8852 1.0395 1.2530 0.0903  -0.0460 -0.0717 148 PHE C O   
10785 C CB  . PHE C 148 ? 1.8071 0.9633 1.1883 0.1597  -0.0478 -0.0884 148 PHE C CB  
10786 C CG  . PHE C 148 ? 1.8119 0.9827 1.2096 0.1937  -0.0455 -0.1000 148 PHE C CG  
10787 C CD1 . PHE C 148 ? 1.7469 0.9862 1.1926 0.2066  -0.0426 -0.1018 148 PHE C CD1 
10788 C CD2 . PHE C 148 ? 1.8911 1.0056 1.2559 0.2122  -0.0452 -0.1097 148 PHE C CD2 
10789 C CE1 . PHE C 148 ? 1.8221 1.0767 1.2847 0.2361  -0.0384 -0.1139 148 PHE C CE1 
10790 C CE2 . PHE C 148 ? 1.8993 1.0283 1.2815 0.2438  -0.0412 -0.1221 148 PHE C CE2 
10791 C CZ  . PHE C 148 ? 1.8771 1.0783 1.3096 0.2551  -0.0373 -0.1245 148 PHE C CZ  
10801 N N   . ILE C 149 ? 1.8906 1.0498 1.2534 0.0660  -0.0386 -0.0888 149 ILE C N   
10802 C CA  . ILE C 149 ? 1.8805 1.0194 1.2264 0.0314  -0.0382 -0.0836 149 ILE C CA  
10803 C C   . ILE C 149 ? 1.9635 1.0211 1.2554 0.0309  -0.0397 -0.0821 149 ILE C C   
10804 O O   . ILE C 149 ? 2.0797 1.0907 1.3417 0.0499  -0.0406 -0.0894 149 ILE C O   
10805 C CB  . ILE C 149 ? 1.8287 0.9841 1.1792 0.0032  -0.0360 -0.0918 149 ILE C CB  
10806 C CG1 . ILE C 149 ? 1.7817 1.0089 1.1785 0.0076  -0.0358 -0.0938 149 ILE C CG1 
10807 C CG2 . ILE C 149 ? 1.8005 0.9493 1.1454 -0.0336 -0.0350 -0.0872 149 ILE C CG2 
10808 C CD1 . ILE C 149 ? 1.7047 0.9877 1.1436 0.0087  -0.0364 -0.0831 149 ILE C CD1 
10820 N N   . PHE C 150 ? 1.9619 0.9998 1.2391 0.0087  -0.0392 -0.0729 150 PHE C N   
10821 C CA  . PHE C 150 ? 2.0461 1.0023 1.2666 0.0015  -0.0399 -0.0701 150 PHE C CA  
10822 C C   . PHE C 150 ? 2.0824 1.0329 1.2941 -0.0419 -0.0341 -0.0672 150 PHE C C   
10823 O O   . PHE C 150 ? 2.0554 1.0378 1.2883 -0.0538 -0.0317 -0.0584 150 PHE C O   
10824 C CB  . PHE C 150 ? 2.0549 0.9824 1.2592 0.0279  -0.0462 -0.0596 150 PHE C CB  
10825 C CG  . PHE C 150 ? 2.2231 1.0604 1.3635 0.0209  -0.0482 -0.0551 150 PHE C CG  
10826 C CD1 . PHE C 150 ? 2.2386 1.0498 1.3543 -0.0169 -0.0422 -0.0496 150 PHE C CD1 
10827 C CD2 . PHE C 150 ? 2.2999 1.0776 1.4046 0.0524  -0.0555 -0.0567 150 PHE C CD2 
10828 C CE1 . PHE C 150 ? 2.2923 1.0163 1.3445 -0.0254 -0.0431 -0.0451 150 PHE C CE1 
10829 C CE2 . PHE C 150 ? 2.3780 1.0670 1.4196 0.0465  -0.0582 -0.0519 150 PHE C CE2 
10830 C CZ  . PHE C 150 ? 2.3805 1.0410 1.3937 0.0067  -0.0519 -0.0456 150 PHE C CZ  
10840 N N   . ASN C 151 ? 2.1220 1.0321 1.3026 -0.0659 -0.0311 -0.0753 151 ASN C N   
10841 C CA  . ASN C 151 ? 2.1442 1.0421 1.3126 -0.1088 -0.0249 -0.0743 151 ASN C CA  
10842 C C   . ASN C 151 ? 2.2643 1.0821 1.3752 -0.1146 -0.0233 -0.0666 151 ASN C C   
10843 O O   . ASN C 151 ? 2.3367 1.0827 1.3980 -0.1039 -0.0261 -0.0698 151 ASN C O   
10844 C CB  . ASN C 151 ? 2.1821 1.0730 1.3426 -0.1340 -0.0236 -0.0871 151 ASN C CB  
10845 C CG  . ASN C 151 ? 2.2216 1.1311 1.3932 -0.1791 -0.0176 -0.0882 151 ASN C CG  
10846 O OD1 . ASN C 151 ? 2.2870 1.1763 1.4441 -0.1968 -0.0114 -0.0807 151 ASN C OD1 
10847 N ND2 . ASN C 151 ? 2.1616 1.1106 1.3593 -0.1982 -0.0194 -0.0980 151 ASN C ND2 
10854 N N   . ILE C 152 ? 2.2269 1.0535 1.3415 -0.1315 -0.0184 -0.0567 152 ILE C N   
10855 C CA  . ILE C 152 ? 2.2945 1.0430 1.3505 -0.1357 -0.0174 -0.0477 152 ILE C CA  
10856 C C   . ILE C 152 ? 2.4145 1.1061 1.4261 -0.1769 -0.0091 -0.0526 152 ILE C C   
10857 O O   . ILE C 152 ? 2.4465 1.0514 1.3945 -0.1777 -0.0100 -0.0493 152 ILE C O   
10858 C CB  . ILE C 152 ? 2.1933 0.9665 1.2628 -0.1382 -0.0145 -0.0353 152 ILE C CB  
10859 C CG1 . ILE C 152 ? 2.1630 1.0144 1.2916 -0.1084 -0.0202 -0.0329 152 ILE C CG1 
10860 C CG2 . ILE C 152 ? 2.2374 0.9280 1.2442 -0.1264 -0.0191 -0.0243 152 ILE C CG2 
10861 C CD1 . ILE C 152 ? 1.9613 0.8460 1.1089 -0.1146 -0.0161 -0.0223 152 ILE C CD1 
10873 N N   . LYS C 153 ? 2.4407 1.1784 1.4844 -0.2119 -0.0016 -0.0607 153 LYS C N   
10874 C CA  . LYS C 153 ? 2.5247 1.2137 1.5307 -0.2529 0.0060  -0.0674 153 LYS C CA  
10875 C C   . LYS C 153 ? 2.6053 1.2368 1.5715 -0.2438 0.0000  -0.0768 153 LYS C C   
10876 O O   . LYS C 153 ? 2.6718 1.2295 1.5826 -0.2678 0.0043  -0.0796 153 LYS C O   
10877 C CB  . LYS C 153 ? 2.5004 1.2618 1.5586 -0.2896 0.0131  -0.0752 153 LYS C CB  
10878 C CG  . LYS C 153 ? 2.5605 1.2862 1.5911 -0.3343 0.0201  -0.0851 153 LYS C CG  
10879 C CD  . LYS C 153 ? 2.5370 1.3392 1.6253 -0.3548 0.0182  -0.0972 153 LYS C CD  
10880 C CE  . LYS C 153 ? 2.5792 1.3438 1.6385 -0.3949 0.0214  -0.1090 153 LYS C CE  
10881 N NZ  . LYS C 153 ? 2.5292 1.3695 1.6459 -0.4294 0.0238  -0.1183 153 LYS C NZ  
10895 N N   . GLU C 154 ? 2.5217 1.1829 1.5128 -0.2105 -0.0087 -0.0822 154 GLU C N   
10896 C CA  . GLU C 154 ? 2.5798 1.1917 1.5367 -0.1997 -0.0131 -0.0929 154 GLU C CA  
10897 C C   . GLU C 154 ? 2.5831 1.1359 1.5026 -0.1560 -0.0198 -0.0886 154 GLU C C   
10898 O O   . GLU C 154 ? 2.6445 1.1806 1.5552 -0.1322 -0.0240 -0.0978 154 GLU C O   
10899 C CB  . GLU C 154 ? 2.6366 1.3166 1.6415 -0.1944 -0.0168 -0.1038 154 GLU C CB  
10900 C CG  . GLU C 154 ? 2.5826 1.3287 1.6316 -0.2327 -0.0137 -0.1082 154 GLU C CG  
10901 C CD  . GLU C 154 ? 2.6865 1.3873 1.7001 -0.2784 -0.0079 -0.1142 154 GLU C CD  
10902 O OE1 . GLU C 154 ? 2.7211 1.3512 1.6822 -0.2821 -0.0087 -0.1215 154 GLU C OE1 
10903 O OE2 . GLU C 154 ? 2.6866 1.4226 1.7253 -0.3112 -0.0016 -0.1124 154 GLU C OE2 
10910 N N   . ASN C 155 ? 2.5889 1.1093 1.4861 -0.1446 -0.0211 -0.0755 155 ASN C N   
10911 C CA  . ASN C 155 ? 2.6247 1.0896 1.4883 -0.1017 -0.0300 -0.0708 155 ASN C CA  
10912 C C   . ASN C 155 ? 2.7185 1.1032 1.5217 -0.1113 -0.0302 -0.0586 155 ASN C C   
10913 O O   . ASN C 155 ? 2.7212 1.1156 1.5239 -0.1438 -0.0228 -0.0512 155 ASN C O   
10914 C CB  . ASN C 155 ? 2.5603 1.0926 1.4768 -0.0614 -0.0371 -0.0661 155 ASN C CB  
10915 C CG  . ASN C 155 ? 2.5449 1.1063 1.4881 -0.0309 -0.0404 -0.0783 155 ASN C CG  
10916 O OD1 . ASN C 155 ? 2.5828 1.1055 1.5061 0.0062  -0.0469 -0.0804 155 ASN C OD1 
10917 N ND2 . ASN C 155 ? 2.4677 1.0970 1.4554 -0.0463 -0.0359 -0.0867 155 ASN C ND2 
10924 N N   . LYS C 156 ? 2.7834 1.0870 1.5342 -0.0826 -0.0384 -0.0569 156 LYS C N   
10925 C CA  . LYS C 156 ? 2.8503 1.0662 1.5347 -0.0880 -0.0410 -0.0446 156 LYS C CA  
10926 C C   . LYS C 156 ? 2.8831 1.1335 1.5877 -0.0775 -0.0453 -0.0295 156 LYS C C   
10927 O O   . LYS C 156 ? 2.8310 1.1685 1.6001 -0.0601 -0.0476 -0.0289 156 LYS C O   
10928 C CB  . LYS C 156 ? 2.9417 1.0911 1.5831 -0.0506 -0.0515 -0.0450 156 LYS C CB  
10929 C CG  . LYS C 156 ? 3.0145 1.1343 1.6334 -0.0622 -0.0461 -0.0583 156 LYS C CG  
10930 C CD  . LYS C 156 ? 3.0843 1.1515 1.6697 -0.0218 -0.0560 -0.0587 156 LYS C CD  
10931 C CE  . LYS C 156 ? 3.1387 1.1745 1.6999 -0.0337 -0.0498 -0.0722 156 LYS C CE  
10932 N NZ  . LYS C 156 ? 3.1662 1.1518 1.6974 0.0066  -0.0585 -0.0738 156 LYS C NZ  
10946 N N   . GLU C 157 ? 2.9720 1.1512 1.6177 -0.0900 -0.0460 -0.0170 157 GLU C N   
10947 C CA  . GLU C 157 ? 2.9233 1.1188 1.5744 -0.0822 -0.0507 -0.0022 157 GLU C CA  
10948 C C   . GLU C 157 ? 2.8447 1.0667 1.5243 -0.0259 -0.0684 0.0009  157 GLU C C   
10949 O O   . GLU C 157 ? 2.8295 1.0040 1.4840 0.0090  -0.0803 -0.0016 157 GLU C O   
10950 C CB  . GLU C 157 ? 3.0546 1.1849 1.6403 -0.0996 -0.0499 0.0101  157 GLU C CB  
10951 C CG  . GLU C 157 ? 3.1464 1.2669 1.7113 -0.1570 -0.0304 0.0075  157 GLU C CG  
10952 C CD  . GLU C 157 ? 3.3231 1.3775 1.8191 -0.1718 -0.0292 0.0179  157 GLU C CD  
10953 O OE1 . GLU C 157 ? 3.3653 1.3750 1.8260 -0.1363 -0.0455 0.0260  157 GLU C OE1 
10954 O OE2 . GLU C 157 ? 3.3931 1.4416 1.8709 -0.2190 -0.0122 0.0173  157 GLU C OE2 
10961 N N   . THR C 158 ? 2.7820 1.0866 1.5182 -0.0173 -0.0698 0.0058  158 THR C N   
10962 C CA  . THR C 158 ? 2.7078 1.0511 1.4808 0.0327  -0.0854 0.0073  158 THR C CA  
10963 C C   . THR C 158 ? 2.6737 1.0686 1.4750 0.0337  -0.0884 0.0190  158 THR C C   
10964 O O   . THR C 158 ? 2.6950 1.1069 1.4964 -0.0040 -0.0761 0.0239  158 THR C O   
10965 C CB  . THR C 158 ? 2.6552 1.0756 1.4942 0.0502  -0.0828 -0.0075 158 THR C CB  
10966 O OG1 . THR C 158 ? 2.5652 1.0418 1.4509 0.0909  -0.0945 -0.0054 158 THR C OG1 
10967 C CG2 . THR C 158 ? 2.6304 1.1245 1.5158 0.0110  -0.0664 -0.0134 158 THR C CG2 
10975 N N   . SER C 159 ? 2.6244 1.0462 1.4519 0.0773  -0.1044 0.0220  159 SER C N   
10976 C CA  . SER C 159 ? 2.5023 0.9825 1.3651 0.0847  -0.1094 0.0309  159 SER C CA  
10977 C C   . SER C 159 ? 2.4104 0.9955 1.3564 0.1004  -0.1068 0.0211  159 SER C C   
10978 O O   . SER C 159 ? 2.4110 1.0117 1.3810 0.1260  -0.1098 0.0100  159 SER C O   
10979 C CB  . SER C 159 ? 2.5067 0.9403 1.3368 0.1218  -0.1320 0.0420  159 SER C CB  
10980 O OG  . SER C 159 ? 2.4811 0.9896 1.3646 0.1426  -0.1402 0.0451  159 SER C OG  
10986 N N   . PHE C 160 ? 2.3373 0.9915 1.3248 0.0847  -0.1002 0.0250  160 PHE C N   
10987 C CA  . PHE C 160 ? 2.2553 1.0060 1.3182 0.0992  -0.0983 0.0173  160 PHE C CA  
10988 C C   . PHE C 160 ? 2.2840 1.0478 1.3670 0.1480  -0.1156 0.0158  160 PHE C C   
10989 O O   . PHE C 160 ? 2.2396 1.0479 1.3650 0.1676  -0.1145 0.0042  160 PHE C O   
10990 C CB  . PHE C 160 ? 2.1567 0.9684 1.2530 0.0782  -0.0909 0.0235  160 PHE C CB  
10991 C CG  . PHE C 160 ? 2.0280 0.8745 1.1453 0.0372  -0.0718 0.0181  160 PHE C CG  
10992 C CD1 . PHE C 160 ? 2.0656 0.8627 1.1464 0.0086  -0.0622 0.0140  160 PHE C CD1 
10993 C CD2 . PHE C 160 ? 1.9394 0.8679 1.1135 0.0273  -0.0642 0.0167  160 PHE C CD2 
10994 C CE1 . PHE C 160 ? 1.9878 0.8215 1.0924 -0.0285 -0.0462 0.0082  160 PHE C CE1 
10995 C CE2 . PHE C 160 ? 1.9070 0.8694 1.1037 -0.0078 -0.0485 0.0114  160 PHE C CE2 
10996 C CZ  . PHE C 160 ? 1.9084 0.8257 1.0723 -0.0356 -0.0399 0.0069  160 PHE C CZ  
11006 N N   . GLU C 161 ? 2.3735 1.0989 1.4261 0.1678  -0.1320 0.0269  161 GLU C N   
11007 C CA  . GLU C 161 ? 2.3468 1.0920 1.4247 0.2144  -0.1501 0.0253  161 GLU C CA  
11008 C C   . GLU C 161 ? 2.3527 1.0571 1.4173 0.2429  -0.1556 0.0150  161 GLU C C   
11009 O O   . GLU C 161 ? 2.3337 1.0841 1.4442 0.2749  -0.1599 0.0049  161 GLU C O   
11010 C CB  . GLU C 161 ? 2.4257 1.1333 1.4690 0.2278  -0.1690 0.0399  161 GLU C CB  
11011 C CG  . GLU C 161 ? 2.4355 1.1729 1.5117 0.2752  -0.1899 0.0384  161 GLU C CG  
11012 C CD  . GLU C 161 ? 2.3930 1.2347 1.5505 0.2843  -0.1830 0.0279  161 GLU C CD  
11013 O OE1 . GLU C 161 ? 2.3027 1.1997 1.4889 0.2599  -0.1728 0.0309  161 GLU C OE1 
11014 O OE2 . GLU C 161 ? 2.3456 1.2126 1.5371 0.3154  -0.1866 0.0161  161 GLU C OE2 
11021 N N   . ASN C 162 ? 2.4256 1.0424 1.4266 0.2312  -0.1543 0.0166  162 ASN C N   
11022 C CA  . ASN C 162 ? 2.4116 0.9842 1.3960 0.2553  -0.1570 0.0055  162 ASN C CA  
11023 C C   . ASN C 162 ? 2.3726 1.0128 1.4129 0.2559  -0.1426 -0.0112 162 ASN C C   
11024 O O   . ASN C 162 ? 2.3526 1.0151 1.4230 0.2918  -0.1474 -0.0220 162 ASN C O   
11025 C CB  . ASN C 162 ? 2.4434 0.9168 1.3518 0.2304  -0.1524 0.0089  162 ASN C CB  
11026 C CG  . ASN C 162 ? 2.5080 0.9166 1.3855 0.2597  -0.1591 -0.0002 162 ASN C CG  
11027 O OD1 . ASN C 162 ? 2.5278 0.9364 1.4193 0.3050  -0.1749 -0.0029 162 ASN C OD1 
11028 N ND2 . ASN C 162 ? 2.5726 0.9259 1.4087 0.2339  -0.1470 -0.0058 162 ASN C ND2 
11035 N N   . ILE C 163 ? 2.3442 1.0184 1.3990 0.2160  -0.1249 -0.0139 163 ILE C N   
11036 C CA  . ILE C 163 ? 2.3087 1.0443 1.4113 0.2129  -0.1121 -0.0286 163 ILE C CA  
11037 C C   . ILE C 163 ? 2.2448 1.0642 1.4131 0.2413  -0.1160 -0.0327 163 ILE C C   
11038 O O   . ILE C 163 ? 2.2141 1.0577 1.4098 0.2662  -0.1142 -0.0457 163 ILE C O   
11039 C CB  . ILE C 163 ? 2.2796 1.0441 1.3908 0.1654  -0.0961 -0.0286 163 ILE C CB  
11040 C CG1 . ILE C 163 ? 2.3053 0.9896 1.3547 0.1357  -0.0904 -0.0280 163 ILE C CG1 
11041 C CG2 . ILE C 163 ? 2.1643 1.0003 1.3282 0.1633  -0.0858 -0.0417 163 ILE C CG2 
11042 C CD1 . ILE C 163 ? 2.3114 1.0179 1.3648 0.0880  -0.0775 -0.0247 163 ILE C CD1 
11054 N N   . ILE C 164 ? 2.2194 1.0842 1.4130 0.2360  -0.1199 -0.0224 164 ILE C N   
11055 C CA  . ILE C 164 ? 2.1562 1.1025 1.4120 0.2583  -0.1229 -0.0257 164 ILE C CA  
11056 C C   . ILE C 164 ? 2.1746 1.1125 1.4401 0.3047  -0.1350 -0.0333 164 ILE C C   
11057 O O   . ILE C 164 ? 2.1192 1.1122 1.4317 0.3230  -0.1301 -0.0455 164 ILE C O   
11058 C CB  . ILE C 164 ? 2.1144 1.0903 1.3816 0.2494  -0.1291 -0.0121 164 ILE C CB  
11059 C CG1 . ILE C 164 ? 2.0579 1.0710 1.3395 0.2076  -0.1136 -0.0093 164 ILE C CG1 
11060 C CG2 . ILE C 164 ? 2.0651 1.1068 1.3855 0.2799  -0.1379 -0.0146 164 ILE C CG2 
11061 C CD1 . ILE C 164 ? 2.0520 1.0582 1.3166 0.1886  -0.1164 0.0050  164 ILE C CD1 
11073 N N   . ASP C 165 ? 2.2262 1.0942 1.4468 0.3244  -0.1510 -0.0264 165 ASP C N   
11074 C CA  . ASP C 165 ? 2.2355 1.0916 1.4652 0.3711  -0.1643 -0.0341 165 ASP C CA  
11075 C C   . ASP C 165 ? 2.2432 1.0857 1.4738 0.3807  -0.1525 -0.0514 165 ASP C C   
11076 O O   . ASP C 165 ? 2.2221 1.1104 1.4975 0.4091  -0.1505 -0.0648 165 ASP C O   
11077 C CB  . ASP C 165 ? 2.2986 1.0713 1.4714 0.3886  -0.1851 -0.0224 165 ASP C CB  
11078 C CG  . ASP C 165 ? 2.3066 1.0789 1.4984 0.4405  -0.2036 -0.0286 165 ASP C CG  
11079 O OD1 . ASP C 165 ? 2.2795 1.1307 1.5333 0.4596  -0.2067 -0.0339 165 ASP C OD1 
11080 O OD2 . ASP C 165 ? 2.3419 1.0354 1.4876 0.4623  -0.2149 -0.0286 165 ASP C OD2 
11085 N N   . LEU C 166 ? 2.2995 1.0787 1.4798 0.3557  -0.1436 -0.0520 166 LEU C N   
11086 C CA  . LEU C 166 ? 2.2818 1.0404 1.4554 0.3620  -0.1323 -0.0686 166 LEU C CA  
11087 C C   . LEU C 166 ? 2.2057 1.0504 1.4392 0.3584  -0.1168 -0.0817 166 LEU C C   
11088 O O   . LEU C 166 ? 2.2073 1.0641 1.4604 0.3837  -0.1116 -0.0974 166 LEU C O   
11089 C CB  . LEU C 166 ? 2.3574 1.0457 1.4717 0.3258  -0.1236 -0.0666 166 LEU C CB  
11090 C CG  . LEU C 166 ? 2.4824 1.0677 1.5247 0.3276  -0.1357 -0.0564 166 LEU C CG  
11091 C CD1 . LEU C 166 ? 2.5732 1.1037 1.5649 0.2833  -0.1236 -0.0555 166 LEU C CD1 
11092 C CD2 . LEU C 166 ? 2.5745 1.1071 1.5983 0.3732  -0.1466 -0.0649 166 LEU C CD2 
11104 N N   . VAL C 167 ? 2.2047 1.1077 1.4659 0.3270  -0.1088 -0.0759 167 VAL C N   
11105 C CA  . VAL C 167 ? 2.1552 1.1356 1.4681 0.3212  -0.0950 -0.0867 167 VAL C CA  
11106 C C   . VAL C 167 ? 2.1600 1.2024 1.5268 0.3560  -0.0997 -0.0920 167 VAL C C   
11107 O O   . VAL C 167 ? 2.1774 1.2560 1.5750 0.3705  -0.0898 -0.1070 167 VAL C O   
11108 C CB  . VAL C 167 ? 2.0384 1.0612 1.3656 0.2802  -0.0872 -0.0784 167 VAL C CB  
11109 C CG1 . VAL C 167 ? 1.9349 1.0373 1.3146 0.2764  -0.0755 -0.0877 167 VAL C CG1 
11110 C CG2 . VAL C 167 ? 2.0523 1.0210 1.3327 0.2448  -0.0810 -0.0766 167 VAL C CG2 
11120 N N   . LYS C 168 ? 2.0919 1.1473 1.4701 0.3686  -0.1145 -0.0804 168 LYS C N   
11121 C CA  . LYS C 168 ? 2.0817 1.1972 1.5127 0.4010  -0.1207 -0.0857 168 LYS C CA  
11122 C C   . LYS C 168 ? 2.1247 1.2206 1.5603 0.4407  -0.1226 -0.1011 168 LYS C C   
11123 O O   . LYS C 168 ? 2.1209 1.2766 1.6075 0.4629  -0.1183 -0.1131 168 LYS C O   
11124 C CB  . LYS C 168 ? 2.0885 1.2056 1.5197 0.4091  -0.1399 -0.0703 168 LYS C CB  
11125 C CG  . LYS C 168 ? 2.0404 1.2039 1.4884 0.3765  -0.1359 -0.0588 168 LYS C CG  
11126 C CD  . LYS C 168 ? 2.0895 1.2186 1.5065 0.3721  -0.1525 -0.0413 168 LYS C CD  
11127 C CE  . LYS C 168 ? 2.0617 1.2302 1.5130 0.4017  -0.1697 -0.0389 168 LYS C CE  
11128 N NZ  . LYS C 168 ? 2.1424 1.2727 1.5840 0.4438  -0.1862 -0.0442 168 LYS C NZ  
11142 N N   . LYS C 169 ? 2.1682 1.1805 1.5512 0.4500  -0.1280 -0.1017 169 LYS C N   
11143 C CA  . LYS C 169 ? 2.2534 1.2423 1.6389 0.4887  -0.1286 -0.1178 169 LYS C CA  
11144 C C   . LYS C 169 ? 2.2740 1.2834 1.6721 0.4808  -0.1057 -0.1361 169 LYS C C   
11145 O O   . LYS C 169 ? 2.2675 1.3026 1.6976 0.5111  -0.0998 -0.1530 169 LYS C O   
11146 C CB  . LYS C 169 ? 2.2903 1.1769 1.6106 0.5006  -0.1419 -0.1123 169 LYS C CB  
11147 C CG  . LYS C 169 ? 2.3896 1.2438 1.7104 0.5479  -0.1477 -0.1272 169 LYS C CG  
11148 C CD  . LYS C 169 ? 2.3641 1.2869 1.7500 0.5878  -0.1572 -0.1344 169 LYS C CD  
11149 C CE  . LYS C 169 ? 2.3595 1.2900 1.7710 0.6233  -0.1469 -0.1584 169 LYS C CE  
11150 N NZ  . LYS C 169 ? 2.3212 1.3512 1.8118 0.6430  -0.1418 -0.1704 169 LYS C NZ  
11164 N N   . TYR C 170 ? 2.2801 1.2789 1.6536 0.4403  -0.0927 -0.1337 170 TYR C N   
11165 C CA  . TYR C 170 ? 2.2720 1.2991 1.6591 0.4279  -0.0720 -0.1494 170 TYR C CA  
11166 C C   . TYR C 170 ? 2.2718 1.3911 1.7251 0.4392  -0.0639 -0.1576 170 TYR C C   
11167 O O   . TYR C 170 ? 2.3133 1.4530 1.7892 0.4608  -0.0527 -0.1756 170 TYR C O   
11168 C CB  . TYR C 170 ? 2.3092 1.3262 1.6692 0.3802  -0.0639 -0.1422 170 TYR C CB  
11169 C CG  . TYR C 170 ? 2.3518 1.3748 1.7067 0.3635  -0.0457 -0.1571 170 TYR C CG  
11170 C CD1 . TYR C 170 ? 2.3736 1.4510 1.7683 0.3787  -0.0328 -0.1725 170 TYR C CD1 
11171 C CD2 . TYR C 170 ? 2.4036 1.3779 1.7126 0.3307  -0.0413 -0.1561 170 TYR C CD2 
11172 C CE1 . TYR C 170 ? 2.3702 1.4492 1.7547 0.3624  -0.0166 -0.1857 170 TYR C CE1 
11173 C CE2 . TYR C 170 ? 2.4334 1.4115 1.7347 0.3148  -0.0268 -0.1695 170 TYR C CE2 
11174 C CZ  . TYR C 170 ? 2.4013 1.4303 1.7385 0.3310  -0.0147 -0.1839 170 TYR C CZ  
11175 O OH  . TYR C 170 ? 2.4007 1.4303 1.7254 0.3146  -0.0005 -0.1970 170 TYR C OH  
11185 N N   . LEU C 171 ? 2.2171 1.3914 1.7008 0.4239  -0.0683 -0.1452 171 LEU C N   
11186 C CA  . LEU C 171 ? 2.1592 1.4201 1.7014 0.4259  -0.0591 -0.1514 171 LEU C CA  
11187 C C   . LEU C 171 ? 2.1649 1.4598 1.7499 0.4679  -0.0638 -0.1620 171 LEU C C   
11188 O O   . LEU C 171 ? 2.1229 1.4903 1.7580 0.4708  -0.0550 -0.1690 171 LEU C O   
11189 C CB  . LEU C 171 ? 2.0925 1.3960 1.6525 0.4004  -0.0646 -0.1348 171 LEU C CB  
11190 C CG  . LEU C 171 ? 2.0299 1.3277 1.5676 0.3574  -0.0572 -0.1266 171 LEU C CG  
11191 C CD1 . LEU C 171 ? 2.0373 1.3547 1.5796 0.3433  -0.0388 -0.1400 171 LEU C CD1 
11192 C CD2 . LEU C 171 ? 2.0493 1.2692 1.5301 0.3430  -0.0649 -0.1173 171 LEU C CD2 
11204 N N   . SER C 172 ? 2.2070 1.4524 1.7744 0.5001  -0.0775 -0.1637 172 SER C N   
11205 C CA  . SER C 172 ? 2.1909 1.4716 1.8035 0.5423  -0.0835 -0.1750 172 SER C CA  
11206 C C   . SER C 172 ? 2.2364 1.5583 1.8825 0.5527  -0.0607 -0.1982 172 SER C C   
11207 O O   . SER C 172 ? 2.1886 1.5843 1.8918 0.5646  -0.0551 -0.2069 172 SER C O   
11208 C CB  . SER C 172 ? 2.1990 1.4090 1.7802 0.5760  -0.1027 -0.1737 172 SER C CB  
11209 O OG  . SER C 172 ? 2.2705 1.4299 1.8243 0.5888  -0.0913 -0.1893 172 SER C OG  
11215 N N   . ASN C 173 ? 2.3381 1.6124 1.9474 0.5465  -0.0464 -0.2090 173 ASN C N   
11216 C CA  . ASN C 173 ? 2.3170 1.6200 1.9487 0.5555  -0.0230 -0.2321 173 ASN C CA  
11217 C C   . ASN C 173 ? 2.3129 1.6671 1.9576 0.5191  -0.0035 -0.2336 173 ASN C C   
11218 O O   . ASN C 173 ? 2.3592 1.7332 2.0144 0.5204  0.0179  -0.2521 173 ASN C O   
11219 C CB  . ASN C 173 ? 2.3970 1.6220 1.9788 0.5644  -0.0160 -0.2439 173 ASN C CB  
11220 C CG  . ASN C 173 ? 2.4722 1.6369 1.9922 0.5259  -0.0160 -0.2322 173 ASN C CG  
11221 O OD1 . ASN C 173 ? 2.4409 1.6223 1.9528 0.4938  -0.0006 -0.2347 173 ASN C OD1 
11222 N ND2 . ASN C 173 ? 2.5312 1.6252 2.0068 0.5283  -0.0338 -0.2195 173 ASN C ND2 
11229 N N   . GLU C 174 ? 2.2321 1.6058 1.8744 0.4874  -0.0101 -0.2152 174 GLU C N   
11230 C CA  . GLU C 174 ? 2.1725 1.5932 1.8267 0.4539  0.0052  -0.2147 174 GLU C CA  
11231 C C   . GLU C 174 ? 2.1079 1.5965 1.8077 0.4485  -0.0018 -0.2037 174 GLU C C   
11232 O O   . GLU C 174 ? 2.0908 1.5696 1.7844 0.4431  -0.0197 -0.1862 174 GLU C O   
11233 C CB  . GLU C 174 ? 2.1626 1.5385 1.7667 0.4166  0.0050  -0.2039 174 GLU C CB  
11234 C CG  . GLU C 174 ? 2.2289 1.5231 1.7790 0.4199  0.0044  -0.2092 174 GLU C CG  
11235 C CD  . GLU C 174 ? 2.2085 1.4727 1.7171 0.3806  0.0097  -0.2047 174 GLU C CD  
11236 O OE1 . GLU C 174 ? 2.1288 1.4261 1.6470 0.3521  0.0072  -0.1921 174 GLU C OE1 
11237 O OE2 . GLU C 174 ? 2.2928 1.5008 1.7600 0.3785  0.0157  -0.2145 174 GLU C OE2 
11244 N N   . GLU C 175 ? 2.0285 1.5833 1.7713 0.4486  0.0133  -0.2144 175 GLU C N   
11245 C CA  . GLU C 175 ? 1.9940 1.6138 1.7788 0.4401  0.0089  -0.2053 175 GLU C CA  
11246 C C   . GLU C 175 ? 1.9990 1.6137 1.7612 0.4025  0.0046  -0.1869 175 GLU C C   
11247 O O   . GLU C 175 ? 2.0095 1.6172 1.7502 0.3768  0.0168  -0.1883 175 GLU C O   
11248 C CB  . GLU C 175 ? 1.9516 1.6370 1.7796 0.4420  0.0294  -0.2214 175 GLU C CB  
11249 C CG  . GLU C 175 ? 1.9373 1.6898 1.8059 0.4284  0.0280  -0.2133 175 GLU C CG  
11250 C CD  . GLU C 175 ? 1.9239 1.6780 1.8020 0.4350  0.0035  -0.1963 175 GLU C CD  
11251 O OE1 . GLU C 175 ? 1.9282 1.6837 1.8266 0.4666  -0.0092 -0.2003 175 GLU C OE1 
11252 O OE2 . GLU C 175 ? 1.9182 1.6714 1.7828 0.4088  -0.0034 -0.1795 175 GLU C OE2 
11259 N N   . TYR C 176 ? 1.9943 1.6121 1.7611 0.3997  -0.0133 -0.1702 176 TYR C N   
11260 C CA  . TYR C 176 ? 1.9770 1.5875 1.7238 0.3667  -0.0184 -0.1529 176 TYR C CA  
11261 C C   . TYR C 176 ? 1.9138 1.5748 1.6958 0.3639  -0.0272 -0.1423 176 TYR C C   
11262 O O   . TYR C 176 ? 1.9060 1.5653 1.6982 0.3838  -0.0427 -0.1373 176 TYR C O   
11263 C CB  . TYR C 176 ? 2.0143 1.5536 1.7125 0.3613  -0.0311 -0.1422 176 TYR C CB  
11264 C CG  . TYR C 176 ? 2.0098 1.5243 1.7048 0.3858  -0.0503 -0.1349 176 TYR C CG  
11265 C CD1 . TYR C 176 ? 1.9878 1.4784 1.6616 0.3719  -0.0644 -0.1171 176 TYR C CD1 
11266 C CD2 . TYR C 176 ? 2.0043 1.5185 1.7166 0.4229  -0.0547 -0.1462 176 TYR C CD2 
11267 C CE1 . TYR C 176 ? 1.9561 1.4194 1.6209 0.3933  -0.0831 -0.1097 176 TYR C CE1 
11268 C CE2 . TYR C 176 ? 1.9968 1.4862 1.7041 0.4465  -0.0751 -0.1390 176 TYR C CE2 
11269 C CZ  . TYR C 176 ? 1.9955 1.4575 1.6765 0.4310  -0.0897 -0.1201 176 TYR C CZ  
11270 O OH  . TYR C 176 ? 1.9904 1.4230 1.6606 0.4537  -0.1111 -0.1122 176 TYR C OH  
11280 N N   . SER C 177 ? 1.9319 1.6355 1.7303 0.3396  -0.0180 -0.1391 177 SER C N   
11281 C CA  . SER C 177 ? 1.8848 1.6292 1.7093 0.3315  -0.0259 -0.1277 177 SER C CA  
11282 C C   . SER C 177 ? 1.9358 1.6450 1.7318 0.3162  -0.0396 -0.1100 177 SER C C   
11283 O O   . SER C 177 ? 1.8999 1.6283 1.7103 0.3163  -0.0503 -0.1003 177 SER C O   
11284 C CB  . SER C 177 ? 1.8016 1.5949 1.6470 0.3095  -0.0118 -0.1293 177 SER C CB  
11285 O OG  . SER C 177 ? 1.7180 1.5317 1.5716 0.2919  -0.0189 -0.1150 177 SER C OG  
11291 N N   . ALA C 178 ? 2.1315 1.7897 1.8871 0.3020  -0.0389 -0.1066 178 ALA C N   
11292 C CA  . ALA C 178 ? 2.1143 1.7372 1.8413 0.2847  -0.0488 -0.0916 178 ALA C CA  
11293 C C   . ALA C 178 ? 2.1495 1.7155 1.8338 0.2728  -0.0457 -0.0932 178 ALA C C   
11294 O O   . ALA C 178 ? 2.1770 1.7354 1.8546 0.2749  -0.0356 -0.1052 178 ALA C O   
11295 C CB  . ALA C 178 ? 2.0445 1.7044 1.7869 0.2586  -0.0464 -0.0818 178 ALA C CB  
11301 N N   . PHE C 179 ? 1.9181 1.4431 1.5718 0.2588  -0.0537 -0.0817 179 PHE C N   
11302 C CA  . PHE C 179 ? 1.8624 1.3331 1.4747 0.2428  -0.0513 -0.0823 179 PHE C CA  
11303 C C   . PHE C 179 ? 1.8005 1.2477 1.3916 0.2193  -0.0570 -0.0683 179 PHE C C   
11304 O O   . PHE C 179 ? 1.7908 1.2491 1.3903 0.2219  -0.0646 -0.0586 179 PHE C O   
11305 C CB  . PHE C 179 ? 1.8326 1.2491 1.4165 0.2664  -0.0547 -0.0902 179 PHE C CB  
11306 C CG  . PHE C 179 ? 1.8285 1.1968 1.3850 0.2773  -0.0689 -0.0805 179 PHE C CG  
11307 C CD1 . PHE C 179 ? 1.8239 1.1369 1.3369 0.2560  -0.0717 -0.0721 179 PHE C CD1 
11308 C CD2 . PHE C 179 ? 1.8575 1.2346 1.4303 0.3081  -0.0799 -0.0800 179 PHE C CD2 
11309 C CE1 . PHE C 179 ? 1.8102 1.0735 1.2918 0.2643  -0.0843 -0.0626 179 PHE C CE1 
11310 C CE2 . PHE C 179 ? 1.8472 1.1754 1.3898 0.3186  -0.0950 -0.0703 179 PHE C CE2 
11311 C CZ  . PHE C 179 ? 1.8323 1.1011 1.3267 0.2962  -0.0968 -0.0611 179 PHE C CZ  
11321 N N   . GLY C 180 ? 1.7865 1.2017 1.3499 0.1952  -0.0527 -0.0684 180 GLY C N   
11322 C CA  . GLY C 180 ? 1.7320 1.1274 1.2771 0.1693  -0.0549 -0.0574 180 GLY C CA  
11323 C C   . GLY C 180 ? 1.7307 1.0600 1.2292 0.1568  -0.0547 -0.0590 180 GLY C C   
11324 O O   . GLY C 180 ? 1.7372 1.0411 1.2193 0.1631  -0.0516 -0.0693 180 GLY C O   
11328 N N   . ILE C 181 ? 1.7271 1.0272 1.2024 0.1373  -0.0570 -0.0491 181 ILE C N   
11329 C CA  . ILE C 181 ? 1.7390 0.9723 1.1665 0.1215  -0.0566 -0.0491 181 ILE C CA  
11330 C C   . ILE C 181 ? 1.7088 0.9493 1.1353 0.0847  -0.0512 -0.0431 181 ILE C C   
11331 O O   . ILE C 181 ? 1.6988 0.9488 1.1297 0.0776  -0.0523 -0.0333 181 ILE C O   
11332 C CB  . ILE C 181 ? 1.7675 0.9391 1.1558 0.1401  -0.0659 -0.0432 181 ILE C CB  
11333 C CG1 . ILE C 181 ? 1.7831 0.9459 1.1742 0.1780  -0.0712 -0.0517 181 ILE C CG1 
11334 C CG2 . ILE C 181 ? 1.8019 0.9024 1.1373 0.1175  -0.0642 -0.0414 181 ILE C CG2 
11335 C CD1 . ILE C 181 ? 1.8960 1.0024 1.2535 0.2023  -0.0837 -0.0460 181 ILE C CD1 
11347 N N   . MET C 182 ? 1.7070 0.9441 1.1285 0.0613  -0.0455 -0.0498 182 MET C N   
11348 C CA  . MET C 182 ? 1.6726 0.9230 1.0999 0.0259  -0.0401 -0.0468 182 MET C CA  
11349 C C   . MET C 182 ? 1.7420 0.9231 1.1193 0.0068  -0.0387 -0.0448 182 MET C C   
11350 O O   . MET C 182 ? 1.8192 0.9627 1.1696 -0.0028 -0.0375 -0.0524 182 MET C O   
11351 C CB  . MET C 182 ? 1.6897 0.9780 1.1415 0.0106  -0.0369 -0.0555 182 MET C CB  
11352 C CG  . MET C 182 ? 1.5667 0.9267 1.0683 0.0186  -0.0368 -0.0556 182 MET C CG  
11353 S SD  . MET C 182 ? 1.5665 0.9700 1.1002 0.0217  -0.0363 -0.0441 182 MET C SD  
11354 C CE  . MET C 182 ? 1.5959 1.0095 1.1385 0.0613  -0.0412 -0.0438 182 MET C CE  
11364 N N   . PHE C 183 ? 1.7704 0.9314 1.1316 -0.0001 -0.0383 -0.0347 183 PHE C N   
11365 C CA  . PHE C 183 ? 1.8008 0.8942 1.1114 -0.0218 -0.0354 -0.0315 183 PHE C CA  
11366 C C   . PHE C 183 ? 1.7924 0.9069 1.1159 -0.0619 -0.0256 -0.0349 183 PHE C C   
11367 O O   . PHE C 183 ? 1.7882 0.9368 1.1341 -0.0784 -0.0197 -0.0299 183 PHE C O   
11368 C CB  . PHE C 183 ? 1.8049 0.8683 1.0905 -0.0151 -0.0384 -0.0194 183 PHE C CB  
11369 C CG  . PHE C 183 ? 1.8277 0.8592 1.0940 0.0236  -0.0506 -0.0164 183 PHE C CG  
11370 C CD1 . PHE C 183 ? 1.9215 0.8777 1.1367 0.0334  -0.0557 -0.0180 183 PHE C CD1 
11371 C CD2 . PHE C 183 ? 1.7996 0.8770 1.1001 0.0506  -0.0575 -0.0128 183 PHE C CD2 
11372 C CE1 . PHE C 183 ? 1.9683 0.8973 1.1696 0.0716  -0.0681 -0.0162 183 PHE C CE1 
11373 C CE2 . PHE C 183 ? 1.8398 0.8932 1.1279 0.0869  -0.0698 -0.0113 183 PHE C CE2 
11374 C CZ  . PHE C 183 ? 1.9447 0.9247 1.1846 0.0985  -0.0755 -0.0130 183 PHE C CZ  
11384 N N   . PHE C 184 ? 1.8626 0.9569 1.1723 -0.0779 -0.0239 -0.0442 184 PHE C N   
11385 C CA  . PHE C 184 ? 1.8570 0.9826 1.1887 -0.1132 -0.0174 -0.0502 184 PHE C CA  
11386 C C   . PHE C 184 ? 1.9105 0.9782 1.1987 -0.1461 -0.0104 -0.0506 184 PHE C C   
11387 O O   . PHE C 184 ? 1.9509 0.9505 1.1895 -0.1444 -0.0124 -0.0530 184 PHE C O   
11388 C CB  . PHE C 184 ? 1.8075 0.9575 1.1573 -0.1106 -0.0216 -0.0613 184 PHE C CB  
11389 C CG  . PHE C 184 ? 1.8238 0.9905 1.1853 -0.1468 -0.0184 -0.0690 184 PHE C CG  
11390 C CD1 . PHE C 184 ? 1.7663 0.9829 1.1658 -0.1697 -0.0132 -0.0672 184 PHE C CD1 
11391 C CD2 . PHE C 184 ? 1.8649 0.9981 1.2002 -0.1578 -0.0210 -0.0790 184 PHE C CD2 
11392 C CE1 . PHE C 184 ? 1.7947 1.0313 1.2101 -0.2022 -0.0117 -0.0753 184 PHE C CE1 
11393 C CE2 . PHE C 184 ? 1.8056 0.9564 1.1532 -0.1919 -0.0200 -0.0866 184 PHE C CE2 
11394 C CZ  . PHE C 184 ? 1.7934 0.9979 1.1831 -0.2137 -0.0159 -0.0849 184 PHE C CZ  
11404 N N   . ASP C 185 ? 1.8900 0.9847 1.1971 -0.1764 -0.0012 -0.0492 185 ASP C N   
11405 C CA  . ASP C 185 ? 1.9377 0.9883 1.2109 -0.2139 0.0084  -0.0508 185 ASP C CA  
11406 C C   . ASP C 185 ? 1.9424 1.0391 1.2524 -0.2449 0.0120  -0.0618 185 ASP C C   
11407 O O   . ASP C 185 ? 1.9160 1.0819 1.2794 -0.2526 0.0151  -0.0628 185 ASP C O   
11408 C CB  . ASP C 185 ? 1.9963 1.0395 1.2602 -0.2254 0.0181  -0.0412 185 ASP C CB  
11409 C CG  . ASP C 185 ? 2.0675 1.0819 1.3081 -0.2703 0.0321  -0.0442 185 ASP C CG  
11410 O OD1 . ASP C 185 ? 2.0619 1.1034 1.3262 -0.2974 0.0360  -0.0548 185 ASP C OD1 
11411 O OD2 . ASP C 185 ? 2.1693 1.1343 1.3673 -0.2797 0.0394  -0.0362 185 ASP C OD2 
11416 N N   . SER C 186 ? 1.9758 1.0325 1.2564 -0.2628 0.0108  -0.0704 186 SER C N   
11417 C CA  . SER C 186 ? 1.9619 1.0617 1.2766 -0.2904 0.0104  -0.0818 186 SER C CA  
11418 C C   . SER C 186 ? 1.9854 1.1085 1.3197 -0.3299 0.0232  -0.0840 186 SER C C   
11419 O O   . SER C 186 ? 1.9550 1.1430 1.3415 -0.3464 0.0224  -0.0914 186 SER C O   
11420 C CB  . SER C 186 ? 2.0594 1.1055 1.3327 -0.3001 0.0055  -0.0910 186 SER C CB  
11421 O OG  . SER C 186 ? 2.1647 1.1683 1.4064 -0.3398 0.0149  -0.0949 186 SER C OG  
11427 N N   . ASP C 187 ? 2.0316 1.1028 1.3247 -0.3456 0.0349  -0.0781 187 ASP C N   
11428 C CA  . ASP C 187 ? 2.0338 1.1223 1.3411 -0.3868 0.0503  -0.0819 187 ASP C CA  
11429 C C   . ASP C 187 ? 2.0408 1.2144 1.4155 -0.3842 0.0549  -0.0810 187 ASP C C   
11430 O O   . ASP C 187 ? 2.0119 1.2383 1.4319 -0.4118 0.0610  -0.0902 187 ASP C O   
11431 C CB  . ASP C 187 ? 2.0421 1.0531 1.2855 -0.4016 0.0628  -0.0741 187 ASP C CB  
11432 C CG  . ASP C 187 ? 2.1430 1.0636 1.3162 -0.4073 0.0592  -0.0755 187 ASP C CG  
11433 O OD1 . ASP C 187 ? 2.1851 1.1042 1.3599 -0.4272 0.0563  -0.0868 187 ASP C OD1 
11434 O OD2 . ASP C 187 ? 2.1847 1.0339 1.2999 -0.3916 0.0585  -0.0653 187 ASP C OD2 
11439 N N   . ASN C 188 ? 2.1166 1.3046 1.4999 -0.3514 0.0517  -0.0708 188 ASN C N   
11440 C CA  . ASN C 188 ? 2.0815 1.3423 1.5224 -0.3466 0.0566  -0.0692 188 ASN C CA  
11441 C C   . ASN C 188 ? 2.0181 1.3370 1.5056 -0.3140 0.0419  -0.0691 188 ASN C C   
11442 O O   . ASN C 188 ? 1.9833 1.3590 1.5161 -0.3045 0.0440  -0.0668 188 ASN C O   
11443 C CB  . ASN C 188 ? 2.0517 1.2858 1.4659 -0.3391 0.0662  -0.0577 188 ASN C CB  
11444 C CG  . ASN C 188 ? 2.0978 1.2723 1.4611 -0.3058 0.0553  -0.0472 188 ASN C CG  
11445 O OD1 . ASN C 188 ? 2.1244 1.3047 1.4939 -0.2777 0.0408  -0.0477 188 ASN C OD1 
11446 N ND2 . ASN C 188 ? 2.1496 1.2664 1.4619 -0.3091 0.0622  -0.0381 188 ASN C ND2 
11453 N N   . LEU C 189 ? 1.8924 1.1958 1.3674 -0.2975 0.0280  -0.0720 189 LEU C N   
11454 C CA  . LEU C 189 ? 1.7746 1.1260 1.2862 -0.2676 0.0150  -0.0719 189 LEU C CA  
11455 C C   . LEU C 189 ? 1.7353 1.1009 1.2551 -0.2374 0.0151  -0.0614 189 LEU C C   
11456 O O   . LEU C 189 ? 1.6285 1.0519 1.1934 -0.2213 0.0103  -0.0605 189 LEU C O   
11457 C CB  . LEU C 189 ? 1.6861 1.1099 1.2581 -0.2817 0.0116  -0.0803 189 LEU C CB  
11458 C CG  . LEU C 189 ? 1.7228 1.1423 1.2921 -0.2997 0.0028  -0.0913 189 LEU C CG  
11459 C CD1 . LEU C 189 ? 1.6731 1.1452 1.2898 -0.3313 0.0056  -0.1004 189 LEU C CD1 
11460 C CD2 . LEU C 189 ? 1.6068 1.0423 1.1837 -0.2734 -0.0128 -0.0926 189 LEU C CD2 
11472 N N   . SER C 190 ? 1.7804 1.0915 1.2549 -0.2301 0.0196  -0.0532 190 SER C N   
11473 C CA  . SER C 190 ? 1.7243 1.0422 1.2006 -0.2024 0.0181  -0.0432 190 SER C CA  
11474 C C   . SER C 190 ? 1.7007 0.9977 1.1595 -0.1668 0.0054  -0.0408 190 SER C C   
11475 O O   . SER C 190 ? 1.7463 1.0096 1.1804 -0.1640 -0.0002 -0.0461 190 SER C O   
11476 C CB  . SER C 190 ? 1.8057 1.0755 1.2409 -0.2132 0.0280  -0.0353 190 SER C CB  
11477 O OG  . SER C 190 ? 1.8452 1.0420 1.2220 -0.1987 0.0217  -0.0303 190 SER C OG  
11483 N N   . MET C 191 ? 1.6617 0.9792 1.1337 -0.1398 0.0016  -0.0337 191 MET C N   
11484 C CA  . MET C 191 ? 1.6267 0.9365 1.0922 -0.1049 -0.0092 -0.0326 191 MET C CA  
11485 C C   . MET C 191 ? 1.6449 0.9624 1.1132 -0.0821 -0.0116 -0.0232 191 MET C C   
11486 O O   . MET C 191 ? 1.5802 0.9487 1.0858 -0.0831 -0.0083 -0.0207 191 MET C O   
11487 C CB  . MET C 191 ? 1.5579 0.9205 1.0643 -0.0966 -0.0144 -0.0397 191 MET C CB  
11488 C CG  . MET C 191 ? 1.6194 0.9638 1.1115 -0.0698 -0.0224 -0.0434 191 MET C CG  
11489 S SD  . MET C 191 ? 1.5146 0.9280 1.0562 -0.0552 -0.0270 -0.0482 191 MET C SD  
11490 C CE  . MET C 191 ? 1.4889 0.9453 1.0619 -0.0383 -0.0260 -0.0388 191 MET C CE  
11500 N N   . LYS C 192 ? 1.6393 0.9058 1.0684 -0.0612 -0.0182 -0.0184 192 LYS C N   
11501 C CA  . LYS C 192 ? 1.6497 0.9211 1.0793 -0.0377 -0.0237 -0.0099 192 LYS C CA  
11502 C C   . LYS C 192 ? 1.6204 0.9172 1.0718 -0.0039 -0.0332 -0.0131 192 LYS C C   
11503 O O   . LYS C 192 ? 1.6350 0.8920 1.0602 0.0146  -0.0398 -0.0159 192 LYS C O   
11504 C CB  . LYS C 192 ? 1.7355 0.9341 1.1075 -0.0356 -0.0268 -0.0020 192 LYS C CB  
11505 C CG  . LYS C 192 ? 1.7379 0.9210 1.0913 -0.0639 -0.0167 0.0044  192 LYS C CG  
11506 C CD  . LYS C 192 ? 1.7602 0.9748 1.1391 -0.0988 -0.0029 -0.0026 192 LYS C CD  
11507 C CE  . LYS C 192 ? 1.8283 1.0108 1.1771 -0.1311 0.0100  0.0012  192 LYS C CE  
11508 N NZ  . LYS C 192 ? 1.8667 1.0953 1.2537 -0.1627 0.0237  -0.0069 192 LYS C NZ  
11522 N N   . PRO C 193 ? 1.5518 0.9129 1.0504 0.0049  -0.0332 -0.0139 193 PRO C N   
11523 C CA  . PRO C 193 ? 1.5716 0.9584 1.0914 0.0339  -0.0398 -0.0183 193 PRO C CA  
11524 C C   . PRO C 193 ? 1.5563 0.9296 1.0662 0.0627  -0.0489 -0.0130 193 PRO C C   
11525 O O   . PRO C 193 ? 1.5590 0.9650 1.0899 0.0689  -0.0506 -0.0075 193 PRO C O   
11526 C CB  . PRO C 193 ? 1.5157 0.9725 1.0858 0.0289  -0.0359 -0.0200 193 PRO C CB  
11527 C CG  . PRO C 193 ? 1.5073 0.9747 1.0845 -0.0020 -0.0277 -0.0180 193 PRO C CG  
11528 C CD  . PRO C 193 ? 1.5680 0.9806 1.1029 -0.0127 -0.0259 -0.0121 193 PRO C CD  
11536 N N   . TYR C 194 ? 1.5771 0.9022 1.0556 0.0809  -0.0555 -0.0151 194 TYR C N   
11537 C CA  . TYR C 194 ? 1.6390 0.9542 1.1128 0.1127  -0.0667 -0.0121 194 TYR C CA  
11538 C C   . TYR C 194 ? 1.6510 1.0125 1.1630 0.1367  -0.0679 -0.0208 194 TYR C C   
11539 O O   . TYR C 194 ? 1.6937 1.0562 1.2090 0.1366  -0.0631 -0.0304 194 TYR C O   
11540 C CB  . TYR C 194 ? 1.7357 0.9747 1.1575 0.1233  -0.0741 -0.0105 194 TYR C CB  
11541 C CG  . TYR C 194 ? 1.7789 1.0079 1.1991 0.1607  -0.0879 -0.0096 194 TYR C CG  
11542 C CD1 . TYR C 194 ? 1.8012 1.0385 1.2365 0.1872  -0.0904 -0.0202 194 TYR C CD1 
11543 C CD2 . TYR C 194 ? 1.8090 1.0208 1.2129 0.1694  -0.0989 0.0010  194 TYR C CD2 
11544 C CE1 . TYR C 194 ? 1.8239 1.0568 1.2635 0.2225  -0.1032 -0.0209 194 TYR C CE1 
11545 C CE2 . TYR C 194 ? 1.8166 1.0219 1.2220 0.2046  -0.1141 0.0014  194 TYR C CE2 
11546 C CZ  . TYR C 194 ? 1.8391 1.0571 1.2652 0.2316  -0.1162 -0.0100 194 TYR C CZ  
11547 O OH  . TYR C 194 ? 1.8577 1.0741 1.2911 0.2678  -0.1314 -0.0111 194 TYR C OH  
11557 N N   . VAL C 195 ? 1.6340 1.0322 1.1728 0.1558  -0.0740 -0.0182 195 VAL C N   
11558 C CA  . VAL C 195 ? 1.6349 1.0810 1.2122 0.1771  -0.0738 -0.0267 195 VAL C CA  
11559 C C   . VAL C 195 ? 1.6879 1.1283 1.2668 0.2091  -0.0865 -0.0258 195 VAL C C   
11560 O O   . VAL C 195 ? 1.7308 1.1427 1.2873 0.2127  -0.0966 -0.0165 195 VAL C O   
11561 C CB  . VAL C 195 ? 1.5878 1.1002 1.2078 0.1651  -0.0670 -0.0261 195 VAL C CB  
11562 C CG1 . VAL C 195 ? 1.5606 1.1149 1.2127 0.1777  -0.0619 -0.0367 195 VAL C CG1 
11563 C CG2 . VAL C 195 ? 1.5647 1.0793 1.1813 0.1325  -0.0584 -0.0231 195 VAL C CG2 
11573 N N   . TYR C 196 ? 1.7039 1.1720 1.3093 0.2323  -0.0861 -0.0362 196 TYR C N   
11574 C CA  . TYR C 196 ? 1.7607 1.2317 1.3764 0.2652  -0.0984 -0.0382 196 TYR C CA  
11575 C C   . TYR C 196 ? 1.7836 1.3191 1.4489 0.2791  -0.0925 -0.0490 196 TYR C C   
11576 O O   . TYR C 196 ? 1.8074 1.3636 1.4855 0.2705  -0.0792 -0.0577 196 TYR C O   
11577 C CB  . TYR C 196 ? 1.7707 1.1796 1.3514 0.2857  -0.1053 -0.0423 196 TYR C CB  
11578 C CG  . TYR C 196 ? 1.8257 1.2330 1.4159 0.3222  -0.1211 -0.0440 196 TYR C CG  
11579 C CD1 . TYR C 196 ? 1.8397 1.2125 1.4039 0.3298  -0.1384 -0.0322 196 TYR C CD1 
11580 C CD2 . TYR C 196 ? 1.8211 1.2614 1.4459 0.3490  -0.1190 -0.0581 196 TYR C CD2 
11581 C CE1 . TYR C 196 ? 1.8384 1.2104 1.4124 0.3646  -0.1559 -0.0337 196 TYR C CE1 
11582 C CE2 . TYR C 196 ? 1.8442 1.2878 1.4834 0.3837  -0.1343 -0.0609 196 TYR C CE2 
11583 C CZ  . TYR C 196 ? 1.8559 1.2655 1.4702 0.3921  -0.1542 -0.0484 196 TYR C CZ  
11584 O OH  . TYR C 196 ? 1.8540 1.2675 1.4836 0.4280  -0.1725 -0.0512 196 TYR C OH  
11594 N N   . VAL C 197 ? 1.7844 1.3512 1.4761 0.2993  -0.1025 -0.0485 197 VAL C N   
11595 C CA  . VAL C 197 ? 1.8082 1.4376 1.5485 0.3128  -0.0971 -0.0592 197 VAL C CA  
11596 C C   . VAL C 197 ? 1.8063 1.4385 1.5612 0.3481  -0.1116 -0.0641 197 VAL C C   
11597 O O   . VAL C 197 ? 1.7945 1.4050 1.5348 0.3572  -0.1289 -0.0547 197 VAL C O   
11598 C CB  . VAL C 197 ? 1.7852 1.4696 1.5553 0.2945  -0.0930 -0.0541 197 VAL C CB  
11599 C CG1 . VAL C 197 ? 1.7774 1.5203 1.5899 0.2976  -0.0804 -0.0662 197 VAL C CG1 
11600 C CG2 . VAL C 197 ? 1.7708 1.4404 1.5196 0.2618  -0.0857 -0.0448 197 VAL C CG2 
11610 N N   . LYS C 198 ? 1.8248 1.4836 1.6083 0.3681  -0.1046 -0.0794 198 LYS C N   
11611 C CA  . LYS C 198 ? 1.8353 1.5033 1.6404 0.4040  -0.1179 -0.0866 198 LYS C CA  
11612 C C   . LYS C 198 ? 1.8106 1.5263 1.6484 0.4084  -0.1303 -0.0815 198 LYS C C   
11613 O O   . LYS C 198 ? 1.8038 1.5060 1.6396 0.4309  -0.1511 -0.0778 198 LYS C O   
11614 C CB  . LYS C 198 ? 1.8317 1.5296 1.6681 0.4213  -0.1037 -0.1061 198 LYS C CB  
11615 C CG  . LYS C 198 ? 1.8299 1.5183 1.6793 0.4618  -0.1159 -0.1162 198 LYS C CG  
11616 C CD  . LYS C 198 ? 1.8026 1.5533 1.7042 0.4803  -0.1268 -0.1201 198 LYS C CD  
11617 C CE  . LYS C 198 ? 1.7822 1.5676 1.7267 0.5115  -0.1206 -0.1412 198 LYS C CE  
11618 N NZ  . LYS C 198 ? 1.7423 1.5807 1.7362 0.5347  -0.1367 -0.1453 198 LYS C NZ  
11632 N N   . GLU C 199 ? 1.7932 1.5627 1.6593 0.3871  -0.1191 -0.0813 199 GLU C N   
11633 C CA  . GLU C 199 ? 1.7732 1.5874 1.6683 0.3876  -0.1300 -0.0768 199 GLU C CA  
11634 C C   . GLU C 199 ? 1.7877 1.5615 1.6462 0.3800  -0.1475 -0.0596 199 GLU C C   
11635 O O   . GLU C 199 ? 1.7849 1.5633 1.6498 0.3966  -0.1674 -0.0559 199 GLU C O   
11636 C CB  . GLU C 199 ? 1.7847 1.6540 1.7085 0.3625  -0.1130 -0.0788 199 GLU C CB  
11637 C CG  . GLU C 199 ? 1.7972 1.7230 1.7677 0.3725  -0.0996 -0.0959 199 GLU C CG  
11638 C CD  . GLU C 199 ? 1.7704 1.7597 1.7833 0.3681  -0.1012 -0.0977 199 GLU C CD  
11639 O OE1 . GLU C 199 ? 1.7862 1.7775 1.7902 0.3505  -0.1079 -0.0854 199 GLU C OE1 
11640 O OE2 . GLU C 199 ? 1.7423 1.7794 1.7972 0.3812  -0.0947 -0.1123 199 GLU C OE2 
11647 N N   . VAL C 200 ? 1.7900 1.5240 1.6093 0.3541  -0.1404 -0.0494 200 VAL C N   
11648 C CA  . VAL C 200 ? 1.7591 1.4525 1.5399 0.3431  -0.1532 -0.0339 200 VAL C CA  
11649 C C   . VAL C 200 ? 1.7903 1.4251 1.5366 0.3671  -0.1726 -0.0300 200 VAL C C   
11650 O O   . VAL C 200 ? 1.7172 1.3283 1.4407 0.3698  -0.1902 -0.0191 200 VAL C O   
11651 C CB  . VAL C 200 ? 1.7240 1.3913 1.4750 0.3097  -0.1386 -0.0264 200 VAL C CB  
11652 C CG1 . VAL C 200 ? 1.7241 1.3405 1.4294 0.2979  -0.1490 -0.0118 200 VAL C CG1 
11653 C CG2 . VAL C 200 ? 1.6745 1.3974 1.4578 0.2875  -0.1236 -0.0281 200 VAL C CG2 
11663 N N   . GLY C 201 ? 1.7637 1.3709 1.5023 0.3849  -0.1701 -0.0387 201 GLY C N   
11664 C CA  . GLY C 201 ? 1.7703 1.3151 1.4723 0.4085  -0.1883 -0.0352 201 GLY C CA  
11665 C C   . GLY C 201 ? 1.7907 1.2625 1.4295 0.3892  -0.1921 -0.0205 201 GLY C C   
11666 O O   . GLY C 201 ? 1.8474 1.2613 1.4483 0.4065  -0.2098 -0.0145 201 GLY C O   
11670 N N   . SER C 202 ? 1.7786 1.2507 1.4046 0.3537  -0.1759 -0.0150 202 SER C N   
11671 C CA  . SER C 202 ? 1.7750 1.1839 1.3445 0.3309  -0.1761 -0.0022 202 SER C CA  
11672 C C   . SER C 202 ? 1.7611 1.1791 1.3304 0.2971  -0.1534 -0.0036 202 SER C C   
11673 O O   . SER C 202 ? 1.7578 1.2334 1.3690 0.2898  -0.1403 -0.0113 202 SER C O   
11674 C CB  . SER C 202 ? 1.8118 1.2166 1.3655 0.3230  -0.1890 0.0109  202 SER C CB  
11675 O OG  . SER C 202 ? 1.7626 1.2392 1.3634 0.3163  -0.1846 0.0085  202 SER C OG  
11681 N N   . GLY C 203 ? 1.7893 1.1488 1.3099 0.2758  -0.1494 0.0039  203 GLY C N   
11682 C CA  . GLY C 203 ? 1.7609 1.1239 1.2789 0.2440  -0.1302 0.0023  203 GLY C CA  
11683 C C   . GLY C 203 ? 1.6976 1.0717 1.2105 0.2138  -0.1236 0.0117  203 GLY C C   
11684 O O   . GLY C 203 ? 1.7555 1.1198 1.2535 0.2143  -0.1334 0.0209  203 GLY C O   
11688 N N   . VAL C 204 ? 1.6452 1.0406 1.1709 0.1874  -0.1069 0.0086  204 VAL C N   
11689 C CA  . VAL C 204 ? 1.6263 1.0331 1.1503 0.1575  -0.0975 0.0153  204 VAL C CA  
11690 C C   . VAL C 204 ? 1.6232 1.0158 1.1374 0.1307  -0.0831 0.0118  204 VAL C C   
11691 O O   . VAL C 204 ? 1.6300 1.0321 1.1577 0.1337  -0.0784 0.0030  204 VAL C O   
11692 C CB  . VAL C 204 ? 1.5880 1.0656 1.1605 0.1557  -0.0936 0.0139  204 VAL C CB  
11693 C CG1 . VAL C 204 ? 1.6115 1.1132 1.2036 0.1846  -0.1078 0.0133  204 VAL C CG1 
11694 C CG2 . VAL C 204 ? 1.5206 1.0418 1.1293 0.1475  -0.0811 0.0049  204 VAL C CG2 
11704 N N   . TYR C 205 ? 1.6046 0.9751 1.0955 0.1036  -0.0758 0.0181  205 TYR C N   
11705 C CA  . TYR C 205 ? 1.5770 0.9389 1.0623 0.0747  -0.0622 0.0147  205 TYR C CA  
11706 C C   . TYR C 205 ? 1.5573 0.9801 1.0852 0.0573  -0.0515 0.0132  205 TYR C C   
11707 O O   . TYR C 205 ? 1.5527 0.9793 1.0768 0.0414  -0.0461 0.0188  205 TYR C O   
11708 C CB  . TYR C 205 ? 1.6537 0.9505 1.0857 0.0549  -0.0595 0.0211  205 TYR C CB  
11709 C CG  . TYR C 205 ? 1.7768 1.0054 1.1613 0.0725  -0.0711 0.0234  205 TYR C CG  
11710 C CD1 . TYR C 205 ? 1.7736 0.9919 1.1514 0.1042  -0.0876 0.0273  205 TYR C CD1 
11711 C CD2 . TYR C 205 ? 1.8352 1.0090 1.1816 0.0575  -0.0665 0.0213  205 TYR C CD2 
11712 C CE1 . TYR C 205 ? 1.8235 0.9782 1.1587 0.1230  -0.0997 0.0292  205 TYR C CE1 
11713 C CE2 . TYR C 205 ? 1.8976 1.0041 1.1977 0.0744  -0.0773 0.0234  205 TYR C CE2 
11714 C CZ  . TYR C 205 ? 1.9435 1.0402 1.2384 0.1083  -0.0942 0.0275  205 TYR C CZ  
11715 O OH  . TYR C 205 ? 2.0723 1.1008 1.3220 0.1279  -0.1065 0.0294  205 TYR C OH  
11725 N N   . GLU C 206 ? 1.5266 0.9948 1.0930 0.0610  -0.0483 0.0055  206 GLU C N   
11726 C CA  . GLU C 206 ? 1.4722 0.9985 1.0805 0.0499  -0.0409 0.0042  206 GLU C CA  
11727 C C   . GLU C 206 ? 1.4310 0.9551 1.0372 0.0187  -0.0293 0.0045  206 GLU C C   
11728 O O   . GLU C 206 ? 1.4473 0.9316 1.0253 0.0032  -0.0257 0.0034  206 GLU C O   
11729 C CB  . GLU C 206 ? 1.4547 1.0213 1.0969 0.0589  -0.0405 -0.0039 206 GLU C CB  
11730 C CG  . GLU C 206 ? 1.4904 1.0575 1.1349 0.0882  -0.0490 -0.0074 206 GLU C CG  
11731 C CD  . GLU C 206 ? 1.4643 1.0769 1.1400 0.1032  -0.0523 -0.0060 206 GLU C CD  
11732 O OE1 . GLU C 206 ? 1.4143 1.0597 1.1108 0.0909  -0.0475 -0.0029 206 GLU C OE1 
11733 O OE2 . GLU C 206 ? 1.4616 1.0777 1.1418 0.1272  -0.0593 -0.0089 206 GLU C OE2 
11740 N N   . ASN C 207 ? 1.4134 0.9814 1.0510 0.0092  -0.0228 0.0052  207 ASN C N   
11741 C CA  . ASN C 207 ? 1.4078 0.9850 1.0544 -0.0188 -0.0110 0.0034  207 ASN C CA  
11742 C C   . ASN C 207 ? 1.4101 1.0093 1.0801 -0.0274 -0.0093 -0.0045 207 ASN C C   
11743 O O   . ASN C 207 ? 1.4199 1.0148 1.0904 -0.0507 -0.0018 -0.0079 207 ASN C O   
11744 C CB  . ASN C 207 ? 1.4240 1.0406 1.0978 -0.0240 -0.0046 0.0056  207 ASN C CB  
11745 C CG  . ASN C 207 ? 1.4074 1.0003 1.0544 -0.0194 -0.0062 0.0132  207 ASN C CG  
11746 O OD1 . ASN C 207 ? 1.4651 1.0207 1.0794 -0.0354 -0.0001 0.0164  207 ASN C OD1 
11747 N ND2 . ASN C 207 ? 1.3931 1.0062 1.0516 0.0014  -0.0146 0.0158  207 ASN C ND2 
11754 N N   . SER C 208 ? 1.3790 1.0018 1.0679 -0.0099 -0.0161 -0.0080 208 SER C N   
11755 C CA  . SER C 208 ? 1.3630 1.0015 1.0676 -0.0164 -0.0169 -0.0152 208 SER C CA  
11756 C C   . SER C 208 ? 1.3497 0.9949 1.0572 0.0064  -0.0242 -0.0183 208 SER C C   
11757 O O   . SER C 208 ? 1.3364 0.9970 1.0527 0.0253  -0.0271 -0.0157 208 SER C O   
11758 C CB  . SER C 208 ? 1.3314 1.0188 1.0764 -0.0292 -0.0127 -0.0173 208 SER C CB  
11759 O OG  . SER C 208 ? 1.4825 1.1650 1.2281 -0.0535 -0.0046 -0.0183 208 SER C OG  
11765 N N   . CYS C 209 ? 1.3518 0.9862 1.0523 0.0031  -0.0263 -0.0248 209 CYS C N   
11766 C CA  . CYS C 209 ? 1.3683 1.0103 1.0714 0.0212  -0.0305 -0.0299 209 CYS C CA  
11767 C C   . CYS C 209 ? 1.2996 0.9547 1.0117 0.0080  -0.0315 -0.0363 209 CYS C C   
11768 O O   . CYS C 209 ? 1.2970 0.9215 0.9875 -0.0042 -0.0322 -0.0406 209 CYS C O   
11769 C CB  . CYS C 209 ? 1.4053 1.0013 1.0746 0.0370  -0.0336 -0.0318 209 CYS C CB  
11770 S SG  . CYS C 209 ? 1.4166 1.0280 1.0946 0.0661  -0.0360 -0.0377 209 CYS C SG  
11776 N N   . ALA C 210 ? 1.3060 1.0042 1.0476 0.0098  -0.0325 -0.0368 210 ALA C N   
11777 C CA  . ALA C 210 ? 1.2957 1.0065 1.0443 -0.0015 -0.0361 -0.0422 210 ALA C CA  
11778 C C   . ALA C 210 ? 1.2935 0.9783 1.0166 0.0066  -0.0382 -0.0494 210 ALA C C   
11779 O O   . ALA C 210 ? 1.2741 0.9430 0.9838 -0.0068 -0.0414 -0.0548 210 ALA C O   
11780 C CB  . ALA C 210 ? 1.1986 0.9554 0.9791 0.0008  -0.0378 -0.0402 210 ALA C CB  
11786 N N   . SER C 211 ? 1.3119 0.9930 1.0288 0.0282  -0.0360 -0.0505 211 SER C N   
11787 C CA  . SER C 211 ? 1.2988 0.9547 0.9918 0.0377  -0.0355 -0.0587 211 SER C CA  
11788 C C   . SER C 211 ? 1.3958 0.9995 1.0548 0.0347  -0.0358 -0.0616 211 SER C C   
11789 O O   . SER C 211 ? 1.4026 0.9789 1.0376 0.0348  -0.0359 -0.0696 211 SER C O   
11790 C CB  . SER C 211 ? 1.3101 0.9790 1.0101 0.0620  -0.0317 -0.0605 211 SER C CB  
11791 O OG  . SER C 211 ? 1.4472 1.0917 1.1361 0.0769  -0.0316 -0.0587 211 SER C OG  
11797 N N   . GLY C 212 ? 1.4044 0.9899 1.0569 0.0318  -0.0356 -0.0554 212 GLY C N   
11798 C CA  . GLY C 212 ? 1.4306 0.9615 1.0468 0.0266  -0.0359 -0.0569 212 GLY C CA  
11799 C C   . GLY C 212 ? 1.4026 0.9216 1.0103 -0.0022 -0.0365 -0.0594 212 GLY C C   
11800 O O   . GLY C 212 ? 1.4273 0.9046 1.0038 -0.0093 -0.0371 -0.0653 212 GLY C O   
11804 N N   . THR C 213 ? 1.3804 0.9364 1.0170 -0.0192 -0.0363 -0.0556 213 THR C N   
11805 C CA  . THR C 213 ? 1.3763 0.9341 1.0153 -0.0463 -0.0382 -0.0596 213 THR C CA  
11806 C C   . THR C 213 ? 1.4080 0.9688 1.0420 -0.0480 -0.0437 -0.0679 213 THR C C   
11807 O O   . THR C 213 ? 1.3792 0.9189 0.9968 -0.0669 -0.0466 -0.0739 213 THR C O   
11808 C CB  . THR C 213 ? 1.3376 0.9427 1.0160 -0.0593 -0.0373 -0.0553 213 THR C CB  
11809 O OG1 . THR C 213 ? 1.3681 0.9751 1.0514 -0.0526 -0.0315 -0.0475 213 THR C OG1 
11810 C CG2 . THR C 213 ? 1.3648 0.9686 1.0469 -0.0887 -0.0377 -0.0594 213 THR C CG2 
11818 N N   . THR C 214 ? 1.3747 0.9604 1.0207 -0.0302 -0.0450 -0.0686 214 THR C N   
11819 C CA  . THR C 214 ? 1.3495 0.9325 0.9836 -0.0307 -0.0492 -0.0765 214 THR C CA  
11820 C C   . THR C 214 ? 1.4386 0.9678 1.0306 -0.0261 -0.0469 -0.0840 214 THR C C   
11821 O O   . THR C 214 ? 1.4557 0.9630 1.0267 -0.0413 -0.0507 -0.0912 214 THR C O   
11822 C CB  . THR C 214 ? 1.3297 0.9462 0.9812 -0.0126 -0.0482 -0.0754 214 THR C CB  
11823 O OG1 . THR C 214 ? 1.2837 0.9446 0.9677 -0.0216 -0.0533 -0.0708 214 THR C OG1 
11824 C CG2 . THR C 214 ? 1.4237 1.0240 1.0511 -0.0075 -0.0483 -0.0844 214 THR C CG2 
11832 N N   . ALA C 215 ? 1.4415 0.9484 1.0208 -0.0044 -0.0414 -0.0831 215 ALA C N   
11833 C CA  . ALA C 215 ? 1.4925 0.9451 1.0319 0.0033  -0.0391 -0.0905 215 ALA C CA  
11834 C C   . ALA C 215 ? 1.5178 0.9290 1.0305 -0.0203 -0.0411 -0.0919 215 ALA C C   
11835 O O   . ALA C 215 ? 1.5294 0.9055 1.0119 -0.0288 -0.0421 -0.1006 215 ALA C O   
11836 C CB  . ALA C 215 ? 1.5472 0.9843 1.0821 0.0307  -0.0353 -0.0877 215 ALA C CB  
11842 N N   . LEU C 216 ? 1.5091 0.9226 1.0309 -0.0325 -0.0406 -0.0839 216 LEU C N   
11843 C CA  . LEU C 216 ? 1.5274 0.9069 1.0274 -0.0595 -0.0408 -0.0853 216 LEU C CA  
11844 C C   . LEU C 216 ? 1.5404 0.9341 1.0451 -0.0832 -0.0462 -0.0929 216 LEU C C   
11845 O O   . LEU C 216 ? 1.5800 0.9323 1.0522 -0.0982 -0.0475 -0.1002 216 LEU C O   
11846 C CB  . LEU C 216 ? 1.5148 0.9093 1.0326 -0.0715 -0.0377 -0.0761 216 LEU C CB  
11847 C CG  . LEU C 216 ? 1.5680 0.9348 1.0697 -0.1017 -0.0345 -0.0760 216 LEU C CG  
11848 C CD1 . LEU C 216 ? 1.5735 0.9654 1.0924 -0.1299 -0.0384 -0.0830 216 LEU C CD1 
11849 C CD2 . LEU C 216 ? 1.5961 0.8880 1.0436 -0.1008 -0.0324 -0.0779 216 LEU C CD2 
11861 N N   . GLY C 217 ? 1.5132 0.9634 1.0567 -0.0867 -0.0507 -0.0913 217 GLY C N   
11862 C CA  . GLY C 217 ? 1.4599 0.9271 1.0109 -0.1089 -0.0590 -0.0976 217 GLY C CA  
11863 C C   . GLY C 217 ? 1.5512 0.9871 1.0678 -0.1066 -0.0624 -0.1074 217 GLY C C   
11864 O O   . GLY C 217 ? 1.5938 1.0073 1.0907 -0.1285 -0.0674 -0.1147 217 GLY C O   
11868 N N   . TYR C 218 ? 1.5480 0.9828 1.0571 -0.0811 -0.0591 -0.1086 218 TYR C N   
11869 C CA  . TYR C 218 ? 1.5398 0.9427 1.0138 -0.0774 -0.0595 -0.1191 218 TYR C CA  
11870 C C   . TYR C 218 ? 1.6187 0.9580 1.0491 -0.0860 -0.0566 -0.1256 218 TYR C C   
11871 O O   . TYR C 218 ? 1.6659 0.9804 1.0704 -0.1044 -0.0615 -0.1344 218 TYR C O   
11872 C CB  . TYR C 218 ? 1.5348 0.9432 1.0080 -0.0472 -0.0521 -0.1202 218 TYR C CB  
11873 C CG  . TYR C 218 ? 1.5260 0.9895 1.0326 -0.0404 -0.0543 -0.1157 218 TYR C CG  
11874 C CD1 . TYR C 218 ? 1.4725 0.9614 0.9878 -0.0577 -0.0644 -0.1166 218 TYR C CD1 
11875 C CD2 . TYR C 218 ? 1.5184 1.0067 1.0466 -0.0170 -0.0473 -0.1105 218 TYR C CD2 
11876 C CE1 . TYR C 218 ? 1.4215 0.9548 0.9629 -0.0512 -0.0669 -0.1118 218 TYR C CE1 
11877 C CE2 . TYR C 218 ? 1.4865 1.0208 1.0418 -0.0123 -0.0485 -0.1065 218 TYR C CE2 
11878 C CZ  . TYR C 218 ? 1.4763 1.0310 1.0365 -0.0292 -0.0580 -0.1067 218 TYR C CZ  
11879 O OH  . TYR C 218 ? 1.4293 1.0243 1.0124 -0.0241 -0.0596 -0.1020 218 TYR C OH  
11889 N N   . TYR C 219 ? 1.6264 0.9356 1.0454 -0.0732 -0.0497 -0.1214 219 TYR C N   
11890 C CA  . TYR C 219 ? 1.6895 0.9314 1.0629 -0.0795 -0.0469 -0.1268 219 TYR C CA  
11891 C C   . TYR C 219 ? 1.7221 0.9524 1.0883 -0.1159 -0.0514 -0.1282 219 TYR C C   
11892 O O   . TYR C 219 ? 1.7622 0.9427 1.0890 -0.1303 -0.0519 -0.1366 219 TYR C O   
11893 C CB  . TYR C 219 ? 1.7286 0.9423 1.0926 -0.0583 -0.0410 -0.1200 219 TYR C CB  
11894 C CG  . TYR C 219 ? 1.8337 0.9847 1.1584 -0.0730 -0.0394 -0.1197 219 TYR C CG  
11895 C CD1 . TYR C 219 ? 1.8094 0.9656 1.1431 -0.0968 -0.0392 -0.1121 219 TYR C CD1 
11896 C CD2 . TYR C 219 ? 1.8867 0.9708 1.1635 -0.0634 -0.0369 -0.1274 219 TYR C CD2 
11897 C CE1 . TYR C 219 ? 1.8676 0.9633 1.1615 -0.1128 -0.0364 -0.1118 219 TYR C CE1 
11898 C CE2 . TYR C 219 ? 1.9626 0.9836 1.1987 -0.0776 -0.0356 -0.1267 219 TYR C CE2 
11899 C CZ  . TYR C 219 ? 1.9977 1.0242 1.2414 -0.1033 -0.0352 -0.1185 219 TYR C CZ  
11900 O OH  . TYR C 219 ? 2.1007 1.0613 1.3002 -0.1200 -0.0326 -0.1176 219 TYR C OH  
11910 N N   . LEU C 220 ? 1.6995 0.9756 1.1042 -0.1319 -0.0539 -0.1210 220 LEU C N   
11911 C CA  . LEU C 220 ? 1.7321 1.0045 1.1367 -0.1676 -0.0571 -0.1237 220 LEU C CA  
11912 C C   . LEU C 220 ? 1.7394 1.0287 1.1463 -0.1860 -0.0678 -0.1330 220 LEU C C   
11913 O O   . LEU C 220 ? 1.7860 1.0535 1.1764 -0.2148 -0.0712 -0.1398 220 LEU C O   
11914 C CB  . LEU C 220 ? 1.6649 0.9844 1.1131 -0.1783 -0.0554 -0.1150 220 LEU C CB  
11915 C CG  . LEU C 220 ? 1.6446 0.9372 1.0819 -0.1774 -0.0455 -0.1069 220 LEU C CG  
11916 C CD1 . LEU C 220 ? 1.5690 0.9113 1.0500 -0.1951 -0.0429 -0.1015 220 LEU C CD1 
11917 C CD2 . LEU C 220 ? 1.6476 0.8683 1.0333 -0.1939 -0.0411 -0.1111 220 LEU C CD2 
11929 N N   . LYS C 221 ? 1.7081 1.0345 1.1333 -0.1713 -0.0736 -0.1335 221 LYS C N   
11930 C CA  . LYS C 221 ? 1.7152 1.0538 1.1372 -0.1874 -0.0857 -0.1418 221 LYS C CA  
11931 C C   . LYS C 221 ? 1.7497 1.0267 1.1163 -0.1909 -0.0848 -0.1532 221 LYS C C   
11932 O O   . LYS C 221 ? 1.8031 1.0721 1.1554 -0.2148 -0.0947 -0.1616 221 LYS C O   
11933 C CB  . LYS C 221 ? 1.6480 1.0350 1.0967 -0.1703 -0.0914 -0.1385 221 LYS C CB  
11934 C CG  . LYS C 221 ? 1.6886 1.0816 1.1253 -0.1829 -0.1051 -0.1464 221 LYS C CG  
11935 C CD  . LYS C 221 ? 1.7040 1.1205 1.1615 -0.2147 -0.1191 -0.1491 221 LYS C CD  
11936 C CE  . LYS C 221 ? 1.7358 1.1421 1.1682 -0.2305 -0.1343 -0.1588 221 LYS C CE  
11937 N NZ  . LYS C 221 ? 1.7019 1.0448 1.0748 -0.2272 -0.1277 -0.1684 221 LYS C NZ  
11951 N N   . LYS C 222 ? 1.8039 1.0370 1.1394 -0.1672 -0.0738 -0.1543 222 LYS C N   
11952 C CA  . LYS C 222 ? 1.8537 1.0231 1.1348 -0.1676 -0.0708 -0.1659 222 LYS C CA  
11953 C C   . LYS C 222 ? 1.9187 1.0325 1.1679 -0.1871 -0.0675 -0.1683 222 LYS C C   
11954 O O   . LYS C 222 ? 2.0399 1.1167 1.2552 -0.2099 -0.0716 -0.1783 222 LYS C O   
11955 C CB  . LYS C 222 ? 1.8551 1.0028 1.1194 -0.1313 -0.0600 -0.1675 222 LYS C CB  
11956 C CG  . LYS C 222 ? 1.8552 1.0579 1.1535 -0.1100 -0.0594 -0.1633 222 LYS C CG  
11957 C CD  . LYS C 222 ? 1.9168 1.1199 1.1956 -0.1132 -0.0630 -0.1732 222 LYS C CD  
11958 C CE  . LYS C 222 ? 1.8858 1.1496 1.2010 -0.1036 -0.0661 -0.1673 222 LYS C CE  
11959 N NZ  . LYS C 222 ? 1.8715 1.1250 1.1618 -0.0898 -0.0600 -0.1764 222 LYS C NZ  
11973 N N   . CYS C 223 ? 1.9650 1.0697 1.2215 -0.1794 -0.0602 -0.1591 223 CYS C N   
11974 C CA  . CYS C 223 ? 2.0853 1.1286 1.3047 -0.1946 -0.0551 -0.1600 223 CYS C CA  
11975 C C   . CYS C 223 ? 2.1157 1.1726 1.3476 -0.2355 -0.0595 -0.1605 223 CYS C C   
11976 O O   . CYS C 223 ? 2.1973 1.1991 1.3914 -0.2570 -0.0563 -0.1647 223 CYS C O   
11977 C CB  . CYS C 223 ? 2.0176 1.0457 1.2379 -0.1704 -0.0469 -0.1491 223 CYS C CB  
11978 S SG  . CYS C 223 ? 2.3506 1.3088 1.5294 -0.1899 -0.0408 -0.1455 223 CYS C SG  
11984 N N   . LYS C 224 ? 1.9965 1.1246 1.2804 -0.2469 -0.0664 -0.1571 224 LYS C N   
11985 C CA  . LYS C 224 ? 1.9666 1.1187 1.2722 -0.2848 -0.0706 -0.1591 224 LYS C CA  
11986 C C   . LYS C 224 ? 1.9053 1.1106 1.2421 -0.3002 -0.0856 -0.1653 224 LYS C C   
11987 O O   . LYS C 224 ? 1.9078 1.1206 1.2513 -0.3342 -0.0916 -0.1719 224 LYS C O   
11988 C CB  . LYS C 224 ? 1.9636 1.1531 1.3090 -0.2863 -0.0636 -0.1481 224 LYS C CB  
11989 C CG  . LYS C 224 ? 2.0148 1.2105 1.3723 -0.3260 -0.0607 -0.1506 224 LYS C CG  
11990 C CD  . LYS C 224 ? 1.9995 1.2561 1.4005 -0.3500 -0.0737 -0.1578 224 LYS C CD  
11991 C CE  . LYS C 224 ? 1.9743 1.2768 1.4210 -0.3763 -0.0692 -0.1567 224 LYS C CE  
11992 N NZ  . LYS C 224 ? 1.8694 1.2382 1.3656 -0.3926 -0.0847 -0.1636 224 LYS C NZ  
12006 N N   . ASN C 225 ? 1.8607 1.1004 1.2142 -0.2774 -0.0923 -0.1639 225 ASN C N   
12007 C CA  . ASN C 225 ? 1.8153 1.1115 1.2034 -0.2883 -0.1083 -0.1666 225 ASN C CA  
12008 C C   . ASN C 225 ? 1.7814 1.1436 1.2313 -0.2949 -0.1102 -0.1589 225 ASN C C   
12009 O O   . ASN C 225 ? 1.7744 1.1779 1.2565 -0.3170 -0.1228 -0.1628 225 ASN C O   
12010 C CB  . ASN C 225 ? 1.8356 1.1114 1.2001 -0.3203 -0.1201 -0.1791 225 ASN C CB  
12011 C CG  . ASN C 225 ? 1.8028 1.1333 1.1988 -0.3290 -0.1402 -0.1818 225 ASN C CG  
12012 O OD1 . ASN C 225 ? 1.7855 1.1357 1.1853 -0.3071 -0.1456 -0.1788 225 ASN C OD1 
12013 N ND2 . ASN C 225 ? 1.7942 1.1493 1.2128 -0.3614 -0.1516 -0.1878 225 ASN C ND2 
12020 N N   . LEU C 226 ? 1.7662 1.1377 1.2327 -0.2752 -0.0979 -0.1487 226 LEU C N   
12021 C CA  . LEU C 226 ? 1.6914 1.1218 1.2135 -0.2771 -0.0966 -0.1412 226 LEU C CA  
12022 C C   . LEU C 226 ? 1.6405 1.1183 1.1934 -0.2508 -0.1029 -0.1349 226 LEU C C   
12023 O O   . LEU C 226 ? 1.6384 1.1042 1.1790 -0.2227 -0.0956 -0.1291 226 LEU C O   
12024 C CB  . LEU C 226 ? 1.7279 1.1362 1.2444 -0.2729 -0.0797 -0.1338 226 LEU C CB  
12025 C CG  . LEU C 226 ? 1.6447 1.1011 1.2098 -0.2817 -0.0738 -0.1280 226 LEU C CG  
12026 C CD1 . LEU C 226 ? 1.5942 1.1005 1.2018 -0.3096 -0.0835 -0.1350 226 LEU C CD1 
12027 C CD2 . LEU C 226 ? 1.7082 1.1210 1.2477 -0.2913 -0.0576 -0.1244 226 LEU C CD2 
12039 N N   . ASP C 227 ? 1.6016 1.1332 1.1949 -0.2602 -0.1170 -0.1362 227 ASP C N   
12040 C CA  . ASP C 227 ? 1.5436 1.1150 1.1606 -0.2377 -0.1248 -0.1305 227 ASP C CA  
12041 C C   . ASP C 227 ? 1.5152 1.1266 1.1742 -0.2226 -0.1164 -0.1204 227 ASP C C   
12042 O O   . ASP C 227 ? 1.4888 1.1150 1.1539 -0.1980 -0.1155 -0.1139 227 ASP C O   
12043 C CB  . ASP C 227 ? 1.5466 1.1541 1.1852 -0.2519 -0.1462 -0.1356 227 ASP C CB  
12044 C CG  . ASP C 227 ? 1.6387 1.2123 1.2318 -0.2526 -0.1567 -0.1425 227 ASP C CG  
12045 O OD1 . ASP C 227 ? 1.6405 1.1594 1.1869 -0.2580 -0.1492 -0.1486 227 ASP C OD1 
12046 O OD2 . ASP C 227 ? 1.7018 1.3008 1.3032 -0.2479 -0.1725 -0.1420 227 ASP C OD2 
12051 N N   . ARG C 228 ? 1.4958 1.1241 1.1823 -0.2380 -0.1092 -0.1196 228 ARG C N   
12052 C CA  . ARG C 228 ? 1.4405 1.1050 1.1649 -0.2256 -0.1005 -0.1110 228 ARG C CA  
12053 C C   . ARG C 228 ? 1.4696 1.1191 1.1942 -0.2415 -0.0849 -0.1105 228 ARG C C   
12054 O O   . ARG C 228 ? 1.5186 1.1474 1.2304 -0.2678 -0.0836 -0.1178 228 ARG C O   
12055 C CB  . ARG C 228 ? 1.3959 1.1241 1.1746 -0.2273 -0.1129 -0.1106 228 ARG C CB  
12056 C CG  . ARG C 228 ? 1.3963 1.1557 1.2133 -0.2545 -0.1133 -0.1169 228 ARG C CG  
12057 C CD  . ARG C 228 ? 1.4047 1.2239 1.2728 -0.2546 -0.1307 -0.1188 228 ARG C CD  
12058 N NE  . ARG C 228 ? 1.3783 1.2329 1.2797 -0.2327 -0.1267 -0.1103 228 ARG C NE  
12059 C CZ  . ARG C 228 ? 1.3530 1.2616 1.3069 -0.2314 -0.1360 -0.1110 228 ARG C CZ  
12060 N NH1 . ARG C 228 ? 1.3935 1.3324 1.3775 -0.2496 -0.1511 -0.1197 228 ARG C NH1 
12061 N NH2 . ARG C 228 ? 1.3245 1.2573 1.3019 -0.2109 -0.1306 -0.1032 228 ARG C NH2 
12075 N N   . ALA C 229 ? 1.4249 1.0838 1.1620 -0.2267 -0.0730 -0.1021 229 ALA C N   
12076 C CA  . ALA C 229 ? 1.4622 1.1052 1.1959 -0.2404 -0.0572 -0.1003 229 ALA C CA  
12077 C C   . ALA C 229 ? 1.4264 1.0902 1.1795 -0.2207 -0.0479 -0.0907 229 ALA C C   
12078 O O   . ALA C 229 ? 1.4020 1.0708 1.1529 -0.1940 -0.0512 -0.0848 229 ALA C O   
12079 C CB  . ALA C 229 ? 1.5079 1.0800 1.1830 -0.2452 -0.0499 -0.1011 229 ALA C CB  
12085 N N   . LYS C 230 ? 1.4457 1.1214 1.2167 -0.2356 -0.0355 -0.0899 230 LYS C N   
12086 C CA  . LYS C 230 ? 1.3917 1.0829 1.1773 -0.2212 -0.0251 -0.0816 230 LYS C CA  
12087 C C   . LYS C 230 ? 1.4103 1.0433 1.1470 -0.2182 -0.0137 -0.0758 230 LYS C C   
12088 O O   . LYS C 230 ? 1.4495 1.0498 1.1631 -0.2415 -0.0048 -0.0786 230 LYS C O   
12089 C CB  . LYS C 230 ? 1.3711 1.1094 1.2044 -0.2389 -0.0172 -0.0851 230 LYS C CB  
12090 C CG  . LYS C 230 ? 1.4353 1.1921 1.2850 -0.2250 -0.0064 -0.0776 230 LYS C CG  
12091 C CD  . LYS C 230 ? 1.4276 1.2299 1.3245 -0.2434 0.0036  -0.0831 230 LYS C CD  
12092 C CE  . LYS C 230 ? 1.4136 1.1875 1.2887 -0.2606 0.0243  -0.0817 230 LYS C CE  
12093 N NZ  . LYS C 230 ? 1.4580 1.2624 1.3678 -0.2912 0.0355  -0.0922 230 LYS C NZ  
12107 N N   . ILE C 231 ? 1.3960 1.0156 1.1165 -0.1901 -0.0146 -0.0678 231 ILE C N   
12108 C CA  . ILE C 231 ? 1.4409 1.0036 1.1135 -0.1813 -0.0086 -0.0618 231 ILE C CA  
12109 C C   . ILE C 231 ? 1.4372 1.0109 1.1189 -0.1756 0.0012  -0.0540 231 ILE C C   
12110 O O   . ILE C 231 ? 1.3798 0.9852 1.0842 -0.1544 -0.0014 -0.0492 231 ILE C O   
12111 C CB  . ILE C 231 ? 1.4221 0.9605 1.0694 -0.1531 -0.0173 -0.0599 231 ILE C CB  
12112 C CG1 . ILE C 231 ? 1.4917 1.0207 1.1292 -0.1595 -0.0264 -0.0687 231 ILE C CG1 
12113 C CG2 . ILE C 231 ? 1.4473 0.9261 1.0468 -0.1426 -0.0131 -0.0544 231 ILE C CG2 
12114 C CD1 . ILE C 231 ? 1.4905 0.9580 1.0810 -0.1758 -0.0241 -0.0732 231 ILE C CD1 
12126 N N   . VAL C 232 ? 1.4259 0.9708 1.0868 -0.1961 0.0131  -0.0529 232 VAL C N   
12127 C CA  . VAL C 232 ? 1.4311 0.9768 1.0907 -0.1930 0.0232  -0.0455 232 VAL C CA  
12128 C C   . VAL C 232 ? 1.4789 0.9816 1.0983 -0.1671 0.0184  -0.0366 232 VAL C C   
12129 O O   . VAL C 232 ? 1.5012 0.9518 1.0785 -0.1623 0.0135  -0.0362 232 VAL C O   
12130 C CB  . VAL C 232 ? 1.4641 0.9896 1.1099 -0.2258 0.0387  -0.0479 232 VAL C CB  
12131 C CG1 . VAL C 232 ? 1.5299 1.0202 1.1415 -0.2219 0.0475  -0.0385 232 VAL C CG1 
12132 C CG2 . VAL C 232 ? 1.4045 0.9919 1.1065 -0.2451 0.0460  -0.0557 232 VAL C CG2 
12142 N N   . GLN C 233 ? 1.4323 0.9560 1.0647 -0.1500 0.0192  -0.0299 233 GLN C N   
12143 C CA  . GLN C 233 ? 1.4521 0.9495 1.0584 -0.1222 0.0121  -0.0221 233 GLN C CA  
12144 C C   . GLN C 233 ? 1.4675 0.9542 1.0601 -0.1238 0.0195  -0.0144 233 GLN C C   
12145 O O   . GLN C 233 ? 1.4497 0.9526 1.0556 -0.1459 0.0318  -0.0158 233 GLN C O   
12146 C CB  . GLN C 233 ? 1.4278 0.9686 1.0672 -0.0960 0.0023  -0.0227 233 GLN C CB  
12147 C CG  . GLN C 233 ? 1.4324 0.9556 1.0585 -0.0823 -0.0074 -0.0272 233 GLN C CG  
12148 C CD  . GLN C 233 ? 1.4090 0.9820 1.0732 -0.0705 -0.0135 -0.0312 233 GLN C CD  
12149 O OE1 . GLN C 233 ? 1.3715 0.9579 1.0426 -0.0464 -0.0184 -0.0291 233 GLN C OE1 
12150 N NE2 . GLN C 233 ? 1.3910 0.9910 1.0792 -0.0881 -0.0136 -0.0374 233 GLN C NE2 
12159 N N   . PRO C 234 ? 1.4744 0.9329 1.0396 -0.1009 0.0120  -0.0069 234 PRO C N   
12160 C CA  . PRO C 234 ? 1.4929 0.9289 1.0331 -0.1046 0.0174  0.0010  234 PRO C CA  
12161 C C   . PRO C 234 ? 1.4883 0.9728 1.0646 -0.1151 0.0280  0.0006  234 PRO C C   
12162 O O   . PRO C 234 ? 1.5084 0.9765 1.0677 -0.1363 0.0406  0.0021  234 PRO C O   
12163 C CB  . PRO C 234 ? 1.5141 0.9320 1.0361 -0.0719 0.0030  0.0077  234 PRO C CB  
12164 C CG  . PRO C 234 ? 1.5179 0.9178 1.0319 -0.0580 -0.0063 0.0033  234 PRO C CG  
12165 C CD  . PRO C 234 ? 1.4985 0.9400 1.0507 -0.0719 -0.0016 -0.0059 234 PRO C CD  
12173 N N   . ASN C 235 ? 1.4544 0.9958 1.0778 -0.1014 0.0243  -0.0019 235 ASN C N   
12174 C CA  . ASN C 235 ? 1.4060 0.9933 1.0653 -0.1086 0.0337  -0.0031 235 ASN C CA  
12175 C C   . ASN C 235 ? 1.3327 0.9771 1.0451 -0.1054 0.0312  -0.0099 235 ASN C C   
12176 O O   . ASN C 235 ? 1.2919 0.9736 1.0329 -0.0897 0.0271  -0.0089 235 ASN C O   
12177 C CB  . ASN C 235 ? 1.4216 1.0105 1.0734 -0.0908 0.0297  0.0043  235 ASN C CB  
12178 C CG  . ASN C 235 ? 1.4246 1.0256 1.0817 -0.1067 0.0440  0.0049  235 ASN C CG  
12179 O OD1 . ASN C 235 ? 1.3680 1.0016 1.0574 -0.1239 0.0560  -0.0018 235 ASN C OD1 
12180 N ND2 . ASN C 235 ? 1.4807 1.0556 1.1061 -0.1005 0.0423  0.0122  235 ASN C ND2 
12187 N N   . GLY C 236 ? 1.3682 1.0172 1.0915 -0.1212 0.0328  -0.0169 236 GLY C N   
12188 C CA  . GLY C 236 ? 1.3086 1.0062 1.0773 -0.1195 0.0279  -0.0232 236 GLY C CA  
12189 C C   . GLY C 236 ? 1.3000 0.9834 1.0618 -0.1302 0.0229  -0.0292 236 GLY C C   
12190 O O   . GLY C 236 ? 1.3516 0.9862 1.0727 -0.1359 0.0227  -0.0284 236 GLY C O   
12194 N N   . TRP C 237 ? 1.2884 1.0134 1.0890 -0.1330 0.0178  -0.0354 237 TRP C N   
12195 C CA  . TRP C 237 ? 1.2626 0.9798 1.0600 -0.1434 0.0108  -0.0420 237 TRP C CA  
12196 C C   . TRP C 237 ? 1.2330 0.9840 1.0565 -0.1283 -0.0024 -0.0441 237 TRP C C   
12197 O O   . TRP C 237 ? 1.1598 0.9537 1.0196 -0.1208 -0.0039 -0.0434 237 TRP C O   
12198 C CB  . TRP C 237 ? 1.2523 0.9827 1.0684 -0.1736 0.0191  -0.0498 237 TRP C CB  
12199 C CG  . TRP C 237 ? 1.2134 1.0042 1.0858 -0.1773 0.0196  -0.0546 237 TRP C CG  
12200 C CD1 . TRP C 237 ? 1.1674 0.9850 1.0661 -0.1837 0.0322  -0.0553 237 TRP C CD1 
12201 C CD2 . TRP C 237 ? 1.1939 1.0233 1.1015 -0.1741 0.0063  -0.0598 237 TRP C CD2 
12202 N NE1 . TRP C 237 ? 1.1528 1.0243 1.1037 -0.1830 0.0275  -0.0609 237 TRP C NE1 
12203 C CE2 . TRP C 237 ? 1.1804 1.0595 1.1369 -0.1770 0.0105  -0.0631 237 TRP C CE2 
12204 C CE3 . TRP C 237 ? 1.2123 1.0369 1.1124 -0.1688 -0.0091 -0.0621 237 TRP C CE3 
12205 C CZ2 . TRP C 237 ? 1.1332 1.0563 1.1316 -0.1734 -0.0022 -0.0679 237 TRP C CZ2 
12206 C CZ3 . TRP C 237 ? 1.1962 1.0634 1.1347 -0.1672 -0.0213 -0.0665 237 TRP C CZ3 
12207 C CH2 . TRP C 237 ? 1.1482 1.0639 1.1356 -0.1688 -0.0188 -0.0689 237 TRP C CH2 
12218 N N   . LEU C 238 ? 1.2918 1.0195 1.0931 -0.1244 -0.0115 -0.0467 238 LEU C N   
12219 C CA  . LEU C 238 ? 1.2419 0.9932 1.0586 -0.1136 -0.0238 -0.0494 238 LEU C CA  
12220 C C   . LEU C 238 ? 1.2924 1.0306 1.0997 -0.1309 -0.0304 -0.0573 238 LEU C C   
12221 O O   . LEU C 238 ? 1.3251 1.0201 1.0983 -0.1416 -0.0269 -0.0594 238 LEU C O   
12222 C CB  . LEU C 238 ? 1.2469 0.9819 1.0419 -0.0881 -0.0281 -0.0454 238 LEU C CB  
12223 C CG  . LEU C 238 ? 1.2738 1.0228 1.0773 -0.0697 -0.0239 -0.0381 238 LEU C CG  
12224 C CD1 . LEU C 238 ? 1.2464 0.9800 1.0298 -0.0465 -0.0281 -0.0366 238 LEU C CD1 
12225 C CD2 . LEU C 238 ? 1.1779 0.9766 1.0234 -0.0686 -0.0247 -0.0370 238 LEU C CD2 
12237 N N   . GLU C 239 ? 1.2790 1.0519 1.1143 -0.1337 -0.0409 -0.0615 239 GLU C N   
12238 C CA  . GLU C 239 ? 1.2856 1.0498 1.1131 -0.1493 -0.0503 -0.0694 239 GLU C CA  
12239 C C   . GLU C 239 ? 1.2955 1.0498 1.1036 -0.1334 -0.0613 -0.0699 239 GLU C C   
12240 O O   . GLU C 239 ? 1.2732 1.0519 1.0959 -0.1159 -0.0656 -0.0658 239 GLU C O   
12241 C CB  . GLU C 239 ? 1.2667 1.0768 1.1392 -0.1662 -0.0567 -0.0750 239 GLU C CB  
12242 C CG  . GLU C 239 ? 1.3365 1.1368 1.2012 -0.1877 -0.0659 -0.0841 239 GLU C CG  
12243 C CD  . GLU C 239 ? 1.3245 1.1755 1.2384 -0.2018 -0.0757 -0.0904 239 GLU C CD  
12244 O OE1 . GLU C 239 ? 1.2816 1.1725 1.2300 -0.1879 -0.0819 -0.0872 239 GLU C OE1 
12245 O OE2 . GLU C 239 ? 1.3365 1.1868 1.2547 -0.2266 -0.0777 -0.0988 239 GLU C OE2 
12252 N N   . TYR C 240 ? 1.3206 1.0363 1.0932 -0.1405 -0.0645 -0.0753 240 TYR C N   
12253 C CA  . TYR C 240 ? 1.3644 1.0675 1.1151 -0.1294 -0.0737 -0.0780 240 TYR C CA  
12254 C C   . TYR C 240 ? 1.3674 1.0833 1.1257 -0.1478 -0.0876 -0.0854 240 TYR C C   
12255 O O   . TYR C 240 ? 1.3691 1.0790 1.1292 -0.1710 -0.0884 -0.0911 240 TYR C O   
12256 C CB  . TYR C 240 ? 1.3858 1.0338 1.0883 -0.1210 -0.0676 -0.0799 240 TYR C CB  
12257 C CG  . TYR C 240 ? 1.4497 1.0559 1.1201 -0.1411 -0.0689 -0.0877 240 TYR C CG  
12258 C CD1 . TYR C 240 ? 1.4741 1.0787 1.1362 -0.1537 -0.0803 -0.0955 240 TYR C CD1 
12259 C CD2 . TYR C 240 ? 1.4498 1.0137 1.0936 -0.1475 -0.0592 -0.0871 240 TYR C CD2 
12260 C CE1 . TYR C 240 ? 1.4914 1.0565 1.1226 -0.1735 -0.0814 -0.1033 240 TYR C CE1 
12261 C CE2 . TYR C 240 ? 1.4870 1.0086 1.0984 -0.1670 -0.0598 -0.0943 240 TYR C CE2 
12262 C CZ  . TYR C 240 ? 1.5213 1.0445 1.1273 -0.1802 -0.0706 -0.1028 240 TYR C CZ  
12263 O OH  . TYR C 240 ? 1.5639 1.0438 1.1361 -0.2011 -0.0713 -0.1107 240 TYR C OH  
12273 N N   . ILE C 241 ? 1.3646 1.0979 1.1265 -0.1384 -0.0991 -0.0855 241 ILE C N   
12274 C CA  . ILE C 241 ? 1.3907 1.1376 1.1587 -0.1533 -0.1160 -0.0916 241 ILE C CA  
12275 C C   . ILE C 241 ? 1.4020 1.1243 1.1326 -0.1435 -0.1225 -0.0940 241 ILE C C   
12276 O O   . ILE C 241 ? 1.3868 1.1214 1.1187 -0.1253 -0.1229 -0.0891 241 ILE C O   
12277 C CB  . ILE C 241 ? 1.3266 1.1278 1.1439 -0.1538 -0.1266 -0.0888 241 ILE C CB  
12278 C CG1 . ILE C 241 ? 1.3261 1.1522 1.1803 -0.1584 -0.1151 -0.0861 241 ILE C CG1 
12279 C CG2 . ILE C 241 ? 1.3784 1.1936 1.2048 -0.1718 -0.1462 -0.0960 241 ILE C CG2 
12280 C CD1 . ILE C 241 ? 1.3085 1.1882 1.2152 -0.1591 -0.1242 -0.0852 241 ILE C CD1 
12292 N N   . ILE C 242 ? 1.4422 1.1283 1.1377 -0.1567 -0.1263 -0.1022 242 ILE C N   
12293 C CA  . ILE C 242 ? 1.5241 1.1839 1.1805 -0.1509 -0.1319 -0.1066 242 ILE C CA  
12294 C C   . ILE C 242 ? 1.5852 1.2660 1.2497 -0.1650 -0.1533 -0.1100 242 ILE C C   
12295 O O   . ILE C 242 ? 1.5783 1.2635 1.2520 -0.1872 -0.1630 -0.1158 242 ILE C O   
12296 C CB  . ILE C 242 ? 1.5340 1.1376 1.1429 -0.1558 -0.1238 -0.1143 242 ILE C CB  
12297 C CG1 . ILE C 242 ? 1.4591 1.0403 1.0531 -0.1324 -0.1061 -0.1107 242 ILE C CG1 
12298 C CG2 . ILE C 242 ? 1.5645 1.1441 1.1360 -0.1620 -0.1343 -0.1224 242 ILE C CG2 
12299 C CD1 . ILE C 242 ? 1.5403 1.0644 1.0850 -0.1293 -0.0983 -0.1185 242 ILE C CD1 
12311 N N   . GLU C 243 ? 1.6261 1.3185 1.2855 -0.1530 -0.1612 -0.1067 243 GLU C N   
12312 C CA  . GLU C 243 ? 1.7249 1.4385 1.3924 -0.1628 -0.1841 -0.1078 243 GLU C CA  
12313 C C   . GLU C 243 ? 1.7751 1.4652 1.3997 -0.1544 -0.1884 -0.1086 243 GLU C C   
12314 O O   . GLU C 243 ? 1.8247 1.5147 1.4428 -0.1356 -0.1774 -0.1032 243 GLU C O   
12315 C CB  . GLU C 243 ? 1.7542 1.5195 1.4744 -0.1565 -0.1920 -0.0998 243 GLU C CB  
12316 C CG  . GLU C 243 ? 1.8238 1.6211 1.5781 -0.1742 -0.2130 -0.1034 243 GLU C CG  
12317 C CD  . GLU C 243 ? 1.8835 1.7304 1.6906 -0.1646 -0.2196 -0.0963 243 GLU C CD  
12318 O OE1 . GLU C 243 ? 1.8388 1.6939 1.6425 -0.1509 -0.2293 -0.0900 243 GLU C OE1 
12319 O OE2 . GLU C 243 ? 1.8297 1.7051 1.6797 -0.1710 -0.2141 -0.0973 243 GLU C OE2 
12326 N N   . ASN C 244 ? 1.8039 1.4737 1.3980 -0.1700 -0.2040 -0.1160 244 ASN C N   
12327 C CA  . ASN C 244 ? 1.8500 1.4933 1.3970 -0.1658 -0.2084 -0.1180 244 ASN C CA  
12328 C C   . ASN C 244 ? 1.8314 1.4413 1.3449 -0.1500 -0.1837 -0.1202 244 ASN C C   
12329 O O   . ASN C 244 ? 1.8106 1.4123 1.3002 -0.1385 -0.1789 -0.1185 244 ASN C O   
12330 C CB  . ASN C 244 ? 1.8716 1.5442 1.4331 -0.1571 -0.2228 -0.1091 244 ASN C CB  
12331 C CG  . ASN C 244 ? 1.8853 1.6034 1.4996 -0.1639 -0.2425 -0.1049 244 ASN C CG  
12332 O OD1 . ASN C 244 ? 1.9172 1.6419 1.5440 -0.1822 -0.2558 -0.1112 244 ASN C OD1 
12333 N ND2 . ASN C 244 ? 1.8354 1.5858 1.4821 -0.1493 -0.2440 -0.0951 244 ASN C ND2 
12340 N N   . ASP C 245 ? 1.7998 1.3898 1.3114 -0.1493 -0.1678 -0.1243 245 ASP C N   
12341 C CA  . ASP C 245 ? 1.8188 1.3802 1.3057 -0.1318 -0.1451 -0.1269 245 ASP C CA  
12342 C C   . ASP C 245 ? 1.7646 1.3561 1.2798 -0.1102 -0.1339 -0.1175 245 ASP C C   
12343 O O   . ASP C 245 ? 1.7650 1.3454 1.2608 -0.0949 -0.1206 -0.1189 245 ASP C O   
12344 C CB  . ASP C 245 ? 1.8829 1.4043 1.3146 -0.1326 -0.1428 -0.1363 245 ASP C CB  
12345 C CG  . ASP C 245 ? 1.9692 1.4459 1.3694 -0.1258 -0.1243 -0.1455 245 ASP C CG  
12346 O OD1 . ASP C 245 ? 2.0034 1.4631 1.4055 -0.1348 -0.1235 -0.1484 245 ASP C OD1 
12347 O OD2 . ASP C 245 ? 1.9964 1.4541 1.3695 -0.1115 -0.1101 -0.1504 245 ASP C OD2 
12352 N N   . GLU C 246 ? 1.7010 1.3317 1.2631 -0.1097 -0.1385 -0.1087 246 GLU C N   
12353 C CA  . GLU C 246 ? 1.6264 1.2860 1.2176 -0.0914 -0.1285 -0.0998 246 GLU C CA  
12354 C C   . GLU C 246 ? 1.5261 1.2037 1.1547 -0.0913 -0.1230 -0.0952 246 GLU C C   
12355 O O   . GLU C 246 ? 1.5044 1.1952 1.1541 -0.1070 -0.1332 -0.0954 246 GLU C O   
12356 C CB  . GLU C 246 ? 1.5645 1.2551 1.1716 -0.0901 -0.1416 -0.0927 246 GLU C CB  
12357 C CG  . GLU C 246 ? 1.6663 1.3362 1.2315 -0.0945 -0.1500 -0.0966 246 GLU C CG  
12358 C CD  . GLU C 246 ? 1.6028 1.2858 1.1655 -0.0822 -0.1466 -0.0901 246 GLU C CD  
12359 O OE1 . GLU C 246 ? 1.5655 1.2501 1.1308 -0.0674 -0.1273 -0.0891 246 GLU C OE1 
12360 O OE2 . GLU C 246 ? 1.6249 1.3159 1.1825 -0.0878 -0.1638 -0.0860 246 GLU C OE2 
12367 N N   . MET C 247 ? 1.4155 1.0938 1.0517 -0.0744 -0.1069 -0.0917 247 MET C N   
12368 C CA  . MET C 247 ? 1.4232 1.1088 1.0843 -0.0736 -0.0995 -0.0877 247 MET C CA  
12369 C C   . MET C 247 ? 1.3365 1.0659 1.0402 -0.0681 -0.1007 -0.0785 247 MET C C   
12370 O O   . MET C 247 ? 1.3146 1.0596 1.0241 -0.0538 -0.0968 -0.0741 247 MET C O   
12371 C CB  . MET C 247 ? 1.3823 1.0402 1.0249 -0.0576 -0.0835 -0.0894 247 MET C CB  
12372 C CG  . MET C 247 ? 1.3224 0.9799 0.9818 -0.0564 -0.0762 -0.0847 247 MET C CG  
12373 S SD  . MET C 247 ? 1.4009 1.0191 1.0392 -0.0767 -0.0771 -0.0902 247 MET C SD  
12374 C CE  . MET C 247 ? 1.3622 1.0216 1.0422 -0.0985 -0.0867 -0.0867 247 MET C CE  
12384 N N   . TYR C 248 ? 1.3106 1.0587 1.0435 -0.0804 -0.1047 -0.0765 248 TYR C N   
12385 C CA  . TYR C 248 ? 1.2514 1.0384 1.0254 -0.0761 -0.1041 -0.0690 248 TYR C CA  
12386 C C   . TYR C 248 ? 1.2943 1.0778 1.0800 -0.0773 -0.0917 -0.0669 248 TYR C C   
12387 O O   . TYR C 248 ? 1.3109 1.0668 1.0794 -0.0883 -0.0881 -0.0713 248 TYR C O   
12388 C CB  . TYR C 248 ? 1.2547 1.0728 1.0581 -0.0891 -0.1199 -0.0693 248 TYR C CB  
12389 C CG  . TYR C 248 ? 1.3056 1.1272 1.0968 -0.0876 -0.1350 -0.0697 248 TYR C CG  
12390 C CD1 . TYR C 248 ? 1.3375 1.1359 1.0990 -0.0995 -0.1458 -0.0767 248 TYR C CD1 
12391 C CD2 . TYR C 248 ? 1.2469 1.0910 1.0518 -0.0753 -0.1387 -0.0629 248 TYR C CD2 
12392 C CE1 . TYR C 248 ? 1.3644 1.1620 1.1092 -0.0991 -0.1604 -0.0766 248 TYR C CE1 
12393 C CE2 . TYR C 248 ? 1.3034 1.1452 1.0910 -0.0748 -0.1529 -0.0624 248 TYR C CE2 
12394 C CZ  . TYR C 248 ? 1.3142 1.1327 1.0712 -0.0867 -0.1640 -0.0691 248 TYR C CZ  
12395 O OH  . TYR C 248 ? 1.4173 1.2298 1.1518 -0.0872 -0.1789 -0.0683 248 TYR C OH  
12405 N N   . ILE C 249 ? 1.2593 1.0674 1.0706 -0.0671 -0.0852 -0.0601 249 ILE C N   
12406 C CA  . ILE C 249 ? 1.2033 1.0103 1.0257 -0.0691 -0.0741 -0.0573 249 ILE C CA  
12407 C C   . ILE C 249 ? 1.1674 1.0152 1.0323 -0.0738 -0.0757 -0.0541 249 ILE C C   
12408 O O   . ILE C 249 ? 1.1339 1.0065 1.0163 -0.0623 -0.0780 -0.0496 249 ILE C O   
12409 C CB  . ILE C 249 ? 1.2342 1.0268 1.0423 -0.0505 -0.0632 -0.0529 249 ILE C CB  
12410 C CG1 . ILE C 249 ? 1.2887 1.0397 1.0571 -0.0447 -0.0609 -0.0576 249 ILE C CG1 
12411 C CG2 . ILE C 249 ? 1.2270 1.0202 1.0460 -0.0530 -0.0536 -0.0487 249 ILE C CG2 
12412 C CD1 . ILE C 249 ? 1.2720 0.9870 1.0186 -0.0588 -0.0587 -0.0616 249 ILE C CD1 
12424 N N   . ASP C 250 ? 1.1535 1.0070 1.0344 -0.0911 -0.0734 -0.0571 250 ASP C N   
12425 C CA  . ASP C 250 ? 1.1422 1.0332 1.0651 -0.0963 -0.0714 -0.0560 250 ASP C CA  
12426 C C   . ASP C 250 ? 1.1715 1.0531 1.0932 -0.0982 -0.0551 -0.0530 250 ASP C C   
12427 O O   . ASP C 250 ? 1.2117 1.0567 1.1021 -0.1024 -0.0480 -0.0533 250 ASP C O   
12428 C CB  . ASP C 250 ? 1.1324 1.0429 1.0796 -0.1164 -0.0801 -0.0633 250 ASP C CB  
12429 C CG  . ASP C 250 ? 1.1157 1.0734 1.1117 -0.1150 -0.0849 -0.0632 250 ASP C CG  
12430 O OD1 . ASP C 250 ? 1.0757 1.0475 1.0838 -0.0999 -0.0799 -0.0573 250 ASP C OD1 
12431 O OD2 . ASP C 250 ? 1.1717 1.1529 1.1950 -0.1289 -0.0941 -0.0698 250 ASP C OD2 
12436 N N   . GLY C 251 ? 1.0924 1.0041 1.0455 -0.0949 -0.0496 -0.0503 251 GLY C N   
12437 C CA  . GLY C 251 ? 1.1270 1.0306 1.0777 -0.0975 -0.0343 -0.0475 251 GLY C CA  
12438 C C   . GLY C 251 ? 1.0692 1.0076 1.0547 -0.0919 -0.0290 -0.0452 251 GLY C C   
12439 O O   . GLY C 251 ? 1.0476 1.0147 1.0579 -0.0830 -0.0379 -0.0448 251 GLY C O   
12443 N N   . PRO C 252 ? 1.0955 1.0283 1.0797 -0.0972 -0.0145 -0.0438 252 PRO C N   
12444 C CA  . PRO C 252 ? 1.0370 1.0001 1.0522 -0.0933 -0.0073 -0.0429 252 PRO C CA  
12445 C C   . PRO C 252 ? 1.0142 0.9712 1.0160 -0.0746 -0.0052 -0.0352 252 PRO C C   
12446 O O   . PRO C 252 ? 1.0230 0.9499 0.9908 -0.0675 -0.0042 -0.0307 252 PRO C O   
12447 C CB  . PRO C 252 ? 0.9715 0.9280 0.9876 -0.1126 0.0090  -0.0466 252 PRO C CB  
12448 C CG  . PRO C 252 ? 1.0201 0.9299 0.9910 -0.1208 0.0108  -0.0452 252 PRO C CG  
12449 C CD  . PRO C 252 ? 1.1327 1.0271 1.0832 -0.1077 -0.0040 -0.0430 252 PRO C CD  
12457 N N   . VAL C 253 ? 0.9963 0.9832 1.0269 -0.0664 -0.0052 -0.0345 253 VAL C N   
12458 C CA  . VAL C 253 ? 1.0033 0.9899 1.0266 -0.0508 -0.0030 -0.0282 253 VAL C CA  
12459 C C   . VAL C 253 ? 0.9882 0.9978 1.0392 -0.0527 0.0070  -0.0299 253 VAL C C   
12460 O O   . VAL C 253 ? 0.9755 1.0139 1.0611 -0.0532 0.0036  -0.0341 253 VAL C O   
12461 C CB  . VAL C 253 ? 0.9878 0.9826 1.0116 -0.0358 -0.0159 -0.0252 253 VAL C CB  
12462 C CG1 . VAL C 253 ? 0.9483 0.9364 0.9567 -0.0221 -0.0129 -0.0194 253 VAL C CG1 
12463 C CG2 . VAL C 253 ? 0.9960 0.9739 0.9998 -0.0370 -0.0260 -0.0267 253 VAL C CG2 
12473 N N   . GLU C 254 ? 0.9654 0.9617 1.0008 -0.0531 0.0187  -0.0271 254 GLU C N   
12474 C CA  . GLU C 254 ? 0.9590 0.9725 1.0147 -0.0544 0.0300  -0.0289 254 GLU C CA  
12475 C C   . GLU C 254 ? 0.9438 0.9561 0.9900 -0.0396 0.0286  -0.0230 254 GLU C C   
12476 O O   . GLU C 254 ? 0.9407 0.9316 0.9570 -0.0333 0.0258  -0.0177 254 GLU C O   
12477 C CB  . GLU C 254 ? 1.0085 1.0060 1.0508 -0.0704 0.0465  -0.0313 254 GLU C CB  
12478 C CG  . GLU C 254 ? 1.0269 1.0415 1.0895 -0.0734 0.0607  -0.0351 254 GLU C CG  
12479 C CD  . GLU C 254 ? 1.0857 1.0852 1.1353 -0.0926 0.0788  -0.0390 254 GLU C CD  
12480 O OE1 . GLU C 254 ? 1.1460 1.1166 1.1653 -0.1026 0.0791  -0.0370 254 GLU C OE1 
12481 O OE2 . GLU C 254 ? 1.0647 1.0786 1.1321 -0.0980 0.0933  -0.0443 254 GLU C OE2 
12488 N N   . ILE C 255 ? 0.9233 0.9589 0.9962 -0.0338 0.0301  -0.0247 255 ILE C N   
12489 C CA  . ILE C 255 ? 0.9339 0.9685 0.9990 -0.0230 0.0311  -0.0202 255 ILE C CA  
12490 C C   . ILE C 255 ? 0.9427 0.9672 0.9969 -0.0305 0.0464  -0.0212 255 ILE C C   
12491 O O   . ILE C 255 ? 0.9209 0.9569 0.9950 -0.0389 0.0580  -0.0273 255 ILE C O   
12492 C CB  . ILE C 255 ? 0.9466 1.0041 1.0399 -0.0137 0.0258  -0.0213 255 ILE C CB  
12493 C CG1 . ILE C 255 ? 0.9444 1.0110 1.0488 -0.0096 0.0105  -0.0214 255 ILE C CG1 
12494 C CG2 . ILE C 255 ? 0.9176 0.9700 0.9972 -0.0036 0.0249  -0.0162 255 ILE C CG2 
12495 C CD1 . ILE C 255 ? 0.9265 0.9765 1.0025 -0.0045 0.0010  -0.0163 255 ILE C CD1 
12507 N N   . ILE C 256 ? 0.9319 0.9353 0.9544 -0.0275 0.0464  -0.0158 256 ILE C N   
12508 C CA  . ILE C 256 ? 0.9526 0.9396 0.9553 -0.0358 0.0588  -0.0158 256 ILE C CA  
12509 C C   . ILE C 256 ? 0.9789 0.9748 0.9876 -0.0309 0.0641  -0.0161 256 ILE C C   
12510 O O   . ILE C 256 ? 0.9810 0.9795 0.9967 -0.0390 0.0780  -0.0209 256 ILE C O   
12511 C CB  . ILE C 256 ? 0.9999 0.9566 0.9631 -0.0347 0.0536  -0.0098 256 ILE C CB  
12512 C CG1 . ILE C 256 ? 0.9969 0.9362 0.9481 -0.0443 0.0536  -0.0108 256 ILE C CG1 
12513 C CG2 . ILE C 256 ? 1.0022 0.9409 0.9400 -0.0393 0.0618  -0.0078 256 ILE C CG2 
12514 C CD1 . ILE C 256 ? 0.9897 0.9005 0.9068 -0.0377 0.0436  -0.0050 256 ILE C CD1 
12526 N N   . ALA C 257 ? 0.9406 0.9402 0.9457 -0.0189 0.0544  -0.0118 257 ALA C N   
12527 C CA  . ALA C 257 ? 0.9265 0.9296 0.9311 -0.0157 0.0587  -0.0117 257 ALA C CA  
12528 C C   . ALA C 257 ? 0.9267 0.9395 0.9355 -0.0038 0.0472  -0.0081 257 ALA C C   
12529 O O   . ALA C 257 ? 0.9247 0.9387 0.9314 0.0018  0.0368  -0.0055 257 ALA C O   
12530 C CB  . ALA C 257 ? 0.9813 0.9625 0.9533 -0.0211 0.0635  -0.0093 257 ALA C CB  
12536 N N   . GLU C 258 ? 0.9530 0.9708 0.9658 -0.0013 0.0504  -0.0087 258 GLU C N   
12537 C CA  . GLU C 258 ? 0.9397 0.9641 0.9530 0.0069  0.0419  -0.0057 258 GLU C CA  
12538 C C   . GLU C 258 ? 0.9329 0.9545 0.9400 0.0054  0.0481  -0.0066 258 GLU C C   
12539 O O   . GLU C 258 ? 0.9218 0.9397 0.9318 0.0001  0.0591  -0.0106 258 GLU C O   
12540 C CB  . GLU C 258 ? 0.8906 0.9276 0.9258 0.0128  0.0358  -0.0061 258 GLU C CB  
12541 C CG  . GLU C 258 ? 0.9276 0.9716 0.9834 0.0142  0.0413  -0.0098 258 GLU C CG  
12542 C CD  . GLU C 258 ? 0.9618 1.0155 1.0369 0.0211  0.0317  -0.0094 258 GLU C CD  
12543 O OE1 . GLU C 258 ? 1.0010 1.0527 1.0669 0.0259  0.0226  -0.0051 258 GLU C OE1 
12544 O OE2 . GLU C 258 ? 0.9187 0.9824 1.0178 0.0213  0.0331  -0.0138 258 GLU C OE2 
12551 N N   . GLY C 259 ? 0.9019 0.9253 0.9002 0.0091  0.0418  -0.0037 259 GLY C N   
12552 C CA  . GLY C 259 ? 0.8867 0.9065 0.8767 0.0063  0.0462  -0.0047 259 GLY C CA  
12553 C C   . GLY C 259 ? 0.9308 0.9537 0.9080 0.0077  0.0385  -0.0020 259 GLY C C   
12554 O O   . GLY C 259 ? 0.9658 0.9973 0.9482 0.0125  0.0317  -0.0001 259 GLY C O   
12558 N N   . LYS C 260 ? 0.9641 0.9807 0.9245 0.0028  0.0397  -0.0024 260 LYS C N   
12559 C CA  . LYS C 260 ? 0.9434 0.9669 0.8952 0.0030  0.0324  -0.0014 260 LYS C CA  
12560 C C   . LYS C 260 ? 0.9494 0.9686 0.8860 0.0040  0.0255  0.0002  260 LYS C C   
12561 O O   . LYS C 260 ? 0.9456 0.9497 0.8695 0.0005  0.0288  0.0005  260 LYS C O   
12562 C CB  . LYS C 260 ? 0.9212 0.9416 0.8662 -0.0040 0.0370  -0.0038 260 LYS C CB  
12563 C CG  . LYS C 260 ? 0.9681 0.9877 0.9245 -0.0038 0.0426  -0.0050 260 LYS C CG  
12564 C CD  . LYS C 260 ? 0.9614 0.9924 0.9243 -0.0010 0.0367  -0.0031 260 LYS C CD  
12565 C CE  . LYS C 260 ? 0.9890 1.0133 0.9586 0.0001  0.0403  -0.0029 260 LYS C CE  
12566 N NZ  . LYS C 260 ? 1.0589 1.0863 1.0413 0.0078  0.0363  -0.0006 260 LYS C NZ  
12580 N N   . ILE C 261 ? 0.9511 0.9828 0.8887 0.0088  0.0161  0.0009  261 ILE C N   
12581 C CA  . ILE C 261 ? 0.9715 1.0004 0.8963 0.0127  0.0064  0.0023  261 ILE C CA  
12582 C C   . ILE C 261 ? 0.9621 1.0075 0.8886 0.0120  -0.0006 0.0002  261 ILE C C   
12583 O O   . ILE C 261 ? 0.9727 1.0357 0.9138 0.0116  0.0008  -0.0020 261 ILE C O   
12584 C CB  . ILE C 261 ? 0.9823 1.0122 0.9117 0.0227  0.0005  0.0038  261 ILE C CB  
12585 C CG1 . ILE C 261 ? 0.9791 1.0083 0.8982 0.0300  -0.0119 0.0047  261 ILE C CG1 
12586 C CG2 . ILE C 261 ? 0.9652 1.0128 0.9136 0.0269  0.0013  0.0022  261 ILE C CG2 
12587 C CD1 . ILE C 261 ? 0.9869 1.0069 0.9032 0.0397  -0.0170 0.0062  261 ILE C CD1 
12599 N N   . TYR C 262 ? 0.9746 1.0137 0.8850 0.0106  -0.0082 0.0007  262 TYR C N   
12600 C CA  . TYR C 262 ? 1.0096 1.0656 0.9219 0.0081  -0.0162 -0.0021 262 TYR C CA  
12601 C C   . TYR C 262 ? 1.0213 1.0882 0.9366 0.0197  -0.0313 -0.0019 262 TYR C C   
12602 O O   . TYR C 262 ? 1.0470 1.0950 0.9434 0.0242  -0.0393 0.0015  262 TYR C O   
12603 C CB  . TYR C 262 ? 0.9671 1.0078 0.8577 -0.0032 -0.0151 -0.0026 262 TYR C CB  
12604 C CG  . TYR C 262 ? 0.9547 0.9794 0.8403 -0.0123 0.0007  -0.0035 262 TYR C CG  
12605 C CD1 . TYR C 262 ? 0.9221 0.9548 0.8175 -0.0190 0.0082  -0.0067 262 TYR C CD1 
12606 C CD2 . TYR C 262 ? 0.9864 0.9875 0.8580 -0.0142 0.0085  -0.0017 262 TYR C CD2 
12607 C CE1 . TYR C 262 ? 0.9259 0.9432 0.8184 -0.0247 0.0218  -0.0080 262 TYR C CE1 
12608 C CE2 . TYR C 262 ? 0.9661 0.9563 0.8382 -0.0210 0.0235  -0.0041 262 TYR C CE2 
12609 C CZ  . TYR C 262 ? 0.9476 0.9458 0.8308 -0.0249 0.0293  -0.0072 262 TYR C CZ  
12610 O OH  . TYR C 262 ? 0.9394 0.9260 0.8246 -0.0290 0.0432  -0.0101 262 TYR C OH  
12620 N N   . ILE C 263 ? 1.0225 1.1184 0.9605 0.0246  -0.0348 -0.0058 263 ILE C N   
12621 C CA  . ILE C 263 ? 1.0826 1.1946 1.0308 0.0379  -0.0485 -0.0076 263 ILE C CA  
12622 C C   . ILE C 263 ? 1.1232 1.2660 1.0868 0.0339  -0.0551 -0.0135 263 ILE C C   
12623 O O   . ILE C 263 ? 1.1408 1.3033 1.1203 0.0256  -0.0461 -0.0177 263 ILE C O   
12624 C CB  . ILE C 263 ? 1.0862 1.2075 1.0512 0.0487  -0.0449 -0.0091 263 ILE C CB  
12625 C CG1 . ILE C 263 ? 1.0599 1.1535 1.0120 0.0488  -0.0369 -0.0043 263 ILE C CG1 
12626 C CG2 . ILE C 263 ? 1.1219 1.2548 1.0955 0.0650  -0.0588 -0.0114 263 ILE C CG2 
12627 C CD1 . ILE C 263 ? 1.0450 1.1438 1.0083 0.0432  -0.0239 -0.0053 263 ILE C CD1 
12639 N N   . GLY C 264 ? 1.1860 1.3321 1.1440 0.0391  -0.0715 -0.0137 264 GLY C N   
12640 C CA  . GLY C 264 ? 1.2643 1.4453 1.2423 0.0368  -0.0804 -0.0205 264 GLY C CA  
12641 C C   . GLY C 264 ? 1.3218 1.5381 1.3340 0.0472  -0.0797 -0.0271 264 GLY C C   
12642 O O   . GLY C 264 ? 1.3228 1.5340 1.3396 0.0611  -0.0789 -0.0261 264 GLY C O   
12646 N N   . LYS C 265 ? 1.4853 1.7374 1.5209 0.0389  -0.0787 -0.0349 265 LYS C N   
12647 C CA  . LYS C 265 ? 1.5306 1.8206 1.6007 0.0459  -0.0752 -0.0434 265 LYS C CA  
12648 C C   . LYS C 265 ? 1.5576 1.8869 1.6526 0.0482  -0.0905 -0.0516 265 LYS C C   
12649 O O   . LYS C 265 ? 1.4852 1.8103 1.5679 0.0417  -0.1030 -0.0501 265 LYS C O   
12650 C CB  . LYS C 265 ? 1.4313 1.7286 1.5078 0.0306  -0.0546 -0.0462 265 LYS C CB  
12651 C CG  . LYS C 265 ? 1.4665 1.8059 1.5766 0.0308  -0.0480 -0.0568 265 LYS C CG  
12652 C CD  . LYS C 265 ? 1.5041 1.8488 1.6273 0.0507  -0.0479 -0.0591 265 LYS C CD  
12653 C CE  . LYS C 265 ? 1.4907 1.8845 1.6529 0.0583  -0.0512 -0.0717 265 LYS C CE  
12654 N NZ  . LYS C 265 ? 1.4737 1.8853 1.6483 0.0683  -0.0733 -0.0741 265 LYS C NZ  
12668 N N   . ARG D 3   ? 1.2070 1.4416 1.2932 -0.0443 0.0999  -0.0182 3   ARG D N   
12669 C CA  . ARG D 3   ? 1.2458 1.4852 1.3385 -0.0478 0.0851  -0.0235 3   ARG D CA  
12670 C C   . ARG D 3   ? 1.2100 1.4276 1.2731 -0.0351 0.0687  -0.0144 3   ARG D C   
12671 O O   . ARG D 3   ? 1.1578 1.3535 1.1958 -0.0260 0.0691  -0.0037 3   ARG D O   
12672 C CB  . ARG D 3   ? 1.3019 1.5259 1.3991 -0.0656 0.0956  -0.0241 3   ARG D CB  
12673 C CG  . ARG D 3   ? 1.3977 1.6352 1.5205 -0.0810 0.1164  -0.0315 3   ARG D CG  
12674 C CD  . ARG D 3   ? 1.4753 1.6897 1.5959 -0.0984 0.1277  -0.0307 3   ARG D CD  
12675 N NE  . ARG D 3   ? 1.4859 1.7287 1.6448 -0.1147 0.1340  -0.0462 3   ARG D NE  
12676 C CZ  . ARG D 3   ? 1.5144 1.7508 1.6851 -0.1325 0.1561  -0.0493 3   ARG D CZ  
12677 N NH1 . ARG D 3   ? 1.5425 1.7420 1.6858 -0.1353 0.1748  -0.0371 3   ARG D NH1 
12678 N NH2 . ARG D 3   ? 1.4762 1.7423 1.6860 -0.1476 0.1596  -0.0655 3   ARG D NH2 
12692 N N   . LYS D 4   ? 1.2443 1.4673 1.3105 -0.0346 0.0546  -0.0193 4   LYS D N   
12693 C CA  . LYS D 4   ? 1.1976 1.4032 1.2397 -0.0238 0.0403  -0.0126 4   LYS D CA  
12694 C C   . LYS D 4   ? 1.1647 1.3462 1.1963 -0.0318 0.0403  -0.0077 4   LYS D C   
12695 O O   . LYS D 4   ? 1.2044 1.3916 1.2504 -0.0427 0.0422  -0.0144 4   LYS D O   
12696 C CB  . LYS D 4   ? 1.1879 1.4147 1.2362 -0.0143 0.0247  -0.0216 4   LYS D CB  
12697 C CG  . LYS D 4   ? 1.2514 1.4596 1.2726 -0.0021 0.0120  -0.0150 4   LYS D CG  
12698 C CD  . LYS D 4   ? 1.2333 1.4163 1.2312 0.0033  0.0153  -0.0022 4   LYS D CD  
12699 C CE  . LYS D 4   ? 1.2051 1.3974 1.2024 0.0118  0.0191  -0.0015 4   LYS D CE  
12700 N NZ  . LYS D 4   ? 1.2079 1.3734 1.1796 0.0184  0.0196  0.0101  4   LYS D NZ  
12714 N N   . VAL D 5   ? 1.1378 1.2928 1.1453 -0.0260 0.0376  0.0029  5   VAL D N   
12715 C CA  . VAL D 5   ? 1.1136 1.2467 1.1111 -0.0310 0.0364  0.0073  5   VAL D CA  
12716 C C   . VAL D 5   ? 1.1032 1.2408 1.0997 -0.0274 0.0242  0.0035  5   VAL D C   
12717 O O   . VAL D 5   ? 1.0370 1.1799 1.0264 -0.0172 0.0153  0.0032  5   VAL D O   
12718 C CB  . VAL D 5   ? 1.0557 1.1614 1.0309 -0.0254 0.0374  0.0183  5   VAL D CB  
12719 C CG1 . VAL D 5   ? 1.0564 1.1554 1.0264 -0.0250 0.0488  0.0222  5   VAL D CG1 
12720 C CG2 . VAL D 5   ? 1.0239 1.1265 0.9866 -0.0139 0.0259  0.0216  5   VAL D CG2 
12730 N N   . GLN D 6   ? 1.0416 1.1743 1.0424 -0.0354 0.0244  0.0005  6   GLN D N   
12731 C CA  . GLN D 6   ? 0.9930 1.1245 0.9893 -0.0326 0.0150  -0.0025 6   GLN D CA  
12732 C C   . GLN D 6   ? 1.0085 1.1156 0.9903 -0.0322 0.0155  0.0054  6   GLN D C   
12733 O O   . GLN D 6   ? 1.0150 1.1091 0.9967 -0.0388 0.0221  0.0081  6   GLN D O   
12734 C CB  . GLN D 6   ? 1.0287 1.1724 1.0402 -0.0410 0.0144  -0.0128 6   GLN D CB  
12735 C CG  . GLN D 6   ? 1.0751 1.2151 1.0787 -0.0372 0.0052  -0.0164 6   GLN D CG  
12736 C CD  . GLN D 6   ? 1.0326 1.1927 1.0502 -0.0390 -0.0013 -0.0295 6   GLN D CD  
12737 O OE1 . GLN D 6   ? 1.0083 1.1737 1.0407 -0.0500 0.0027  -0.0359 6   GLN D OE1 
12738 N NE2 . GLN D 6   ? 1.0751 1.2449 1.0867 -0.0276 -0.0120 -0.0342 6   GLN D NE2 
12747 N N   . VAL D 7   ? 1.0361 1.1364 1.0059 -0.0243 0.0089  0.0086  7   VAL D N   
12748 C CA  . VAL D 7   ? 1.0241 1.1052 0.9842 -0.0232 0.0092  0.0149  7   VAL D CA  
12749 C C   . VAL D 7   ? 0.9415 1.0187 0.8997 -0.0246 0.0070  0.0116  7   VAL D C   
12750 O O   . VAL D 7   ? 1.0524 1.1326 1.0039 -0.0195 0.0022  0.0089  7   VAL D O   
12751 C CB  . VAL D 7   ? 0.9797 1.0542 0.9289 -0.0149 0.0055  0.0204  7   VAL D CB  
12752 C CG1 . VAL D 7   ? 0.9653 1.0232 0.9104 -0.0149 0.0059  0.0253  7   VAL D CG1 
12753 C CG2 . VAL D 7   ? 0.9269 1.0066 0.8754 -0.0115 0.0068  0.0226  7   VAL D CG2 
12763 N N   . LEU D 8   ? 0.9514 1.0191 0.9123 -0.0303 0.0110  0.0118  8   LEU D N   
12764 C CA  . LEU D 8   ? 0.9574 1.0200 0.9160 -0.0318 0.0104  0.0084  8   LEU D CA  
12765 C C   . LEU D 8   ? 0.9506 0.9987 0.9061 -0.0307 0.0129  0.0128  8   LEU D C   
12766 O O   . LEU D 8   ? 1.0193 1.0604 0.9769 -0.0311 0.0149  0.0166  8   LEU D O   
12767 C CB  . LEU D 8   ? 0.9614 1.0270 0.9275 -0.0396 0.0127  0.0024  8   LEU D CB  
12768 C CG  . LEU D 8   ? 0.9694 1.0528 0.9459 -0.0431 0.0113  -0.0041 8   LEU D CG  
12769 C CD1 . LEU D 8   ? 0.9638 1.0495 0.9478 -0.0514 0.0121  -0.0122 8   LEU D CD1 
12770 C CD2 . LEU D 8   ? 1.0117 1.1079 0.9849 -0.0349 0.0037  -0.0073 8   LEU D CD2 
12782 N N   . ASP D 9   ? 0.9855 1.0287 0.9356 -0.0285 0.0129  0.0118  9   ASP D N   
12783 C CA  . ASP D 9   ? 1.0049 1.0379 0.9565 -0.0279 0.0163  0.0140  9   ASP D CA  
12784 C C   . ASP D 9   ? 1.0020 1.0291 0.9564 -0.0317 0.0193  0.0113  9   ASP D C   
12785 O O   . ASP D 9   ? 1.0321 1.0595 0.9829 -0.0340 0.0194  0.0067  9   ASP D O   
12786 C CB  . ASP D 9   ? 0.9943 1.0227 0.9385 -0.0248 0.0181  0.0138  9   ASP D CB  
12787 C CG  . ASP D 9   ? 1.0788 1.1081 1.0171 -0.0209 0.0157  0.0167  9   ASP D CG  
12788 O OD1 . ASP D 9   ? 1.0907 1.1180 1.0345 -0.0203 0.0159  0.0200  9   ASP D OD1 
12789 O OD2 . ASP D 9   ? 1.1141 1.1452 1.0412 -0.0178 0.0128  0.0151  9   ASP D OD2 
12794 N N   . PHE D 10  ? 0.9397 0.9599 0.8988 -0.0312 0.0208  0.0135  10  PHE D N   
12795 C CA  . PHE D 10  ? 0.9446 0.9558 0.9036 -0.0335 0.0235  0.0113  10  PHE D CA  
12796 C C   . PHE D 10  ? 0.9221 0.9272 0.8852 -0.0292 0.0253  0.0112  10  PHE D C   
12797 O O   . PHE D 10  ? 0.8992 0.9077 0.8688 -0.0254 0.0242  0.0130  10  PHE D O   
12798 C CB  . PHE D 10  ? 0.9526 0.9574 0.9100 -0.0357 0.0239  0.0131  10  PHE D CB  
12799 C CG  . PHE D 10  ? 0.9527 0.9487 0.9100 -0.0297 0.0223  0.0165  10  PHE D CG  
12800 C CD1 . PHE D 10  ? 0.9445 0.9285 0.9003 -0.0264 0.0230  0.0153  10  PHE D CD1 
12801 C CD2 . PHE D 10  ? 0.9627 0.9616 0.9202 -0.0259 0.0188  0.0201  10  PHE D CD2 
12802 C CE1 . PHE D 10  ? 0.9802 0.9564 0.9356 -0.0187 0.0192  0.0169  10  PHE D CE1 
12803 C CE2 . PHE D 10  ? 0.9696 0.9596 0.9259 -0.0191 0.0152  0.0220  10  PHE D CE2 
12804 C CZ  . PHE D 10  ? 0.9875 0.9667 0.9432 -0.0151 0.0148  0.0200  10  PHE D CZ  
12814 N N   . ILE D 11  ? 0.9537 0.9506 0.9144 -0.0298 0.0282  0.0083  11  ILE D N   
12815 C CA  . ILE D 11  ? 0.9387 0.9300 0.9045 -0.0248 0.0300  0.0072  11  ILE D CA  
12816 C C   . ILE D 11  ? 0.9245 0.9016 0.8829 -0.0250 0.0305  0.0058  11  ILE D C   
12817 O O   . ILE D 11  ? 0.9661 0.9377 0.9168 -0.0299 0.0327  0.0033  11  ILE D O   
12818 C CB  . ILE D 11  ? 0.9187 0.9119 0.8865 -0.0237 0.0353  0.0044  11  ILE D CB  
12819 C CG1 . ILE D 11  ? 0.9008 0.9023 0.8694 -0.0246 0.0365  0.0059  11  ILE D CG1 
12820 C CG2 . ILE D 11  ? 0.9284 0.9207 0.9071 -0.0178 0.0375  0.0023  11  ILE D CG2 
12821 C CD1 . ILE D 11  ? 0.9370 0.9373 0.8919 -0.0273 0.0366  0.0047  11  ILE D CD1 
12833 N N   . LYS D 12  ? 0.9208 0.8901 0.8796 -0.0193 0.0279  0.0070  12  LYS D N   
12834 C CA  . LYS D 12  ? 0.9549 0.9054 0.9023 -0.0175 0.0288  0.0060  12  LYS D CA  
12835 C C   . LYS D 12  ? 0.9665 0.9143 0.9186 -0.0099 0.0296  0.0022  12  LYS D C   
12836 O O   . LYS D 12  ? 0.9679 0.9246 0.9330 -0.0026 0.0268  0.0010  12  LYS D O   
12837 C CB  . LYS D 12  ? 0.9439 0.8820 0.8828 -0.0133 0.0253  0.0093  12  LYS D CB  
12838 C CG  . LYS D 12  ? 0.9616 0.8744 0.8835 -0.0103 0.0269  0.0087  12  LYS D CG  
12839 C CD  . LYS D 12  ? 1.0306 0.9255 0.9363 -0.0093 0.0267  0.0129  12  LYS D CD  
12840 C CE  . LYS D 12  ? 1.0670 0.9350 0.9522 -0.0141 0.0332  0.0130  12  LYS D CE  
12841 N NZ  . LYS D 12  ? 1.1009 0.9467 0.9665 -0.0135 0.0360  0.0175  12  LYS D NZ  
12855 N N   . ILE D 13  ? 0.9561 0.8923 0.8987 -0.0116 0.0334  -0.0005 13  ILE D N   
12856 C CA  . ILE D 13  ? 0.9859 0.9197 0.9318 -0.0043 0.0357  -0.0046 13  ILE D CA  
12857 C C   . ILE D 13  ? 0.9940 0.9035 0.9225 -0.0011 0.0358  -0.0060 13  ILE D C   
12858 O O   . ILE D 13  ? 1.0048 0.8999 0.9185 -0.0087 0.0372  -0.0048 13  ILE D O   
12859 C CB  . ILE D 13  ? 0.9700 0.9116 0.9183 -0.0083 0.0415  -0.0070 13  ILE D CB  
12860 C CG1 . ILE D 13  ? 0.9543 0.9137 0.9128 -0.0125 0.0419  -0.0049 13  ILE D CG1 
12861 C CG2 . ILE D 13  ? 0.9689 0.9104 0.9234 0.0000  0.0457  -0.0112 13  ILE D CG2 
12862 C CD1 . ILE D 13  ? 0.9650 0.9277 0.9203 -0.0150 0.0479  -0.0067 13  ILE D CD1 
12874 N N   . ASN D 14  ? 0.9919 0.8967 0.9227 0.0104  0.0347  -0.0093 14  ASN D N   
12875 C CA  . ASN D 14  ? 1.0622 0.9409 0.9737 0.0165  0.0343  -0.0109 14  ASN D CA  
12876 C C   . ASN D 14  ? 1.0601 0.9358 0.9702 0.0198  0.0392  -0.0156 14  ASN D C   
12877 O O   . ASN D 14  ? 1.0547 0.9357 0.9746 0.0317  0.0385  -0.0196 14  ASN D O   
12878 C CB  . ASN D 14  ? 1.0304 0.9022 0.9412 0.0306  0.0270  -0.0116 14  ASN D CB  
12879 C CG  . ASN D 14  ? 1.0542 0.8957 0.9414 0.0397  0.0262  -0.0135 14  ASN D CG  
12880 O OD1 . ASN D 14  ? 1.0821 0.9029 0.9497 0.0322  0.0314  -0.0127 14  ASN D OD1 
12881 N ND2 . ASN D 14  ? 1.0569 0.8949 0.9455 0.0564  0.0190  -0.0170 14  ASN D ND2 
12888 N N   . PRO D 15  ? 1.0863 0.9537 0.9848 0.0104  0.0438  -0.0162 15  PRO D N   
12889 C CA  . PRO D 15  ? 1.0691 0.9289 0.9614 0.0146  0.0484  -0.0208 15  PRO D CA  
12890 C C   . PRO D 15  ? 1.0793 0.9089 0.9491 0.0203  0.0478  -0.0227 15  PRO D C   
12891 O O   . PRO D 15  ? 1.0778 0.8874 0.9288 0.0113  0.0490  -0.0228 15  PRO D O   
12892 C CB  . PRO D 15  ? 1.0949 0.9578 0.9825 0.0025  0.0515  -0.0212 15  PRO D CB  
12893 C CG  . PRO D 15  ? 1.0834 0.9430 0.9664 -0.0087 0.0482  -0.0182 15  PRO D CG  
12894 C CD  . PRO D 15  ? 1.0806 0.9472 0.9730 -0.0040 0.0445  -0.0140 15  PRO D CD  
12902 N N   . ALA D 16  ? 1.1200 0.9456 0.9915 0.0354  0.0455  -0.0250 16  ALA D N   
12903 C CA  . ALA D 16  ? 1.1861 0.9803 1.0332 0.0442  0.0443  -0.0271 16  ALA D CA  
12904 C C   . ALA D 16  ? 1.1790 0.9455 1.0026 0.0380  0.0423  -0.0230 16  ALA D C   
12905 O O   . ALA D 16  ? 1.2158 0.9496 1.0128 0.0386  0.0439  -0.0239 16  ALA D O   
12906 C CB  . ALA D 16  ? 1.1142 0.8948 0.9477 0.0428  0.0500  -0.0309 16  ALA D CB  
12912 N N   . GLY D 17  ? 1.1373 0.9146 0.9691 0.0318  0.0399  -0.0186 17  GLY D N   
12913 C CA  . GLY D 17  ? 1.1721 0.9239 0.9824 0.0251  0.0405  -0.0143 17  GLY D CA  
12914 C C   . GLY D 17  ? 1.1797 0.9319 0.9888 0.0049  0.0461  -0.0128 17  GLY D C   
12915 O O   . GLY D 17  ? 1.1870 0.9209 0.9819 -0.0030 0.0490  -0.0096 17  GLY D O   
12919 N N   . ASN D 18  ? 1.1959 0.9676 1.0187 -0.0032 0.0479  -0.0158 18  ASN D N   
12920 C CA  . ASN D 18  ? 1.1832 0.9611 1.0093 -0.0209 0.0507  -0.0165 18  ASN D CA  
12921 C C   . ASN D 18  ? 1.1575 0.9658 1.0052 -0.0253 0.0486  -0.0132 18  ASN D C   
12922 O O   . ASN D 18  ? 1.1147 0.9470 0.9777 -0.0282 0.0475  -0.0147 18  ASN D O   
12923 C CB  . ASN D 18  ? 1.1334 0.9142 0.9595 -0.0248 0.0516  -0.0222 18  ASN D CB  
12924 C CG  . ASN D 18  ? 1.1618 0.9388 0.9851 -0.0420 0.0531  -0.0258 18  ASN D CG  
12925 O OD1 . ASN D 18  ? 1.2282 0.9979 1.0444 -0.0454 0.0529  -0.0315 18  ASN D OD1 
12926 N ND2 . ASN D 18  ? 1.1657 0.9485 0.9955 -0.0525 0.0544  -0.0235 18  ASN D ND2 
12933 N N   . ILE D 19  ? 1.1538 0.9572 0.9987 -0.0248 0.0483  -0.0085 19  ILE D N   
12934 C CA  . ILE D 19  ? 1.0869 0.9152 0.9491 -0.0260 0.0457  -0.0049 19  ILE D CA  
12935 C C   . ILE D 19  ? 1.0677 0.9173 0.9432 -0.0391 0.0468  -0.0068 19  ILE D C   
12936 O O   . ILE D 19  ? 1.0945 0.9366 0.9652 -0.0513 0.0503  -0.0091 19  ILE D O   
12937 C CB  . ILE D 19  ? 1.1218 0.9350 0.9726 -0.0252 0.0467  0.0002  19  ILE D CB  
12938 C CG1 . ILE D 19  ? 1.1439 0.9311 0.9762 -0.0099 0.0439  0.0011  19  ILE D CG1 
12939 C CG2 . ILE D 19  ? 1.0383 0.8763 0.9057 -0.0243 0.0431  0.0038  19  ILE D CG2 
12940 C CD1 . ILE D 19  ? 1.1342 0.9351 0.9789 0.0046  0.0376  -0.0022 19  ILE D CD1 
12952 N N   . THR D 20  ? 1.0486 0.9242 0.9407 -0.0362 0.0436  -0.0068 20  THR D N   
12953 C CA  . THR D 20  ? 1.0291 0.9241 0.9312 -0.0449 0.0428  -0.0092 20  THR D CA  
12954 C C   . THR D 20  ? 0.9930 0.9102 0.9090 -0.0420 0.0399  -0.0054 20  THR D C   
12955 O O   . THR D 20  ? 1.0013 0.9227 0.9226 -0.0329 0.0384  -0.0027 20  THR D O   
12956 C CB  . THR D 20  ? 1.0729 0.9698 0.9733 -0.0434 0.0425  -0.0142 20  THR D CB  
12957 O OG1 . THR D 20  ? 1.0745 0.9906 0.9827 -0.0475 0.0399  -0.0161 20  THR D OG1 
12958 C CG2 . THR D 20  ? 1.0976 0.9953 1.0003 -0.0312 0.0436  -0.0132 20  THR D CG2 
12966 N N   . ILE D 21  ? 0.9776 0.9091 0.9001 -0.0497 0.0388  -0.0060 21  ILE D N   
12967 C CA  . ILE D 21  ? 0.9996 0.9503 0.9324 -0.0473 0.0360  -0.0028 21  ILE D CA  
12968 C C   . ILE D 21  ? 0.9777 0.9428 0.9139 -0.0491 0.0335  -0.0065 21  ILE D C   
12969 O O   . ILE D 21  ? 0.9928 0.9597 0.9278 -0.0558 0.0323  -0.0119 21  ILE D O   
12970 C CB  . ILE D 21  ? 1.0051 0.9587 0.9400 -0.0523 0.0367  0.0002  21  ILE D CB  
12971 C CG1 . ILE D 21  ? 1.0100 0.9502 0.9388 -0.0456 0.0372  0.0055  21  ILE D CG1 
12972 C CG2 . ILE D 21  ? 0.9674 0.9424 0.9118 -0.0523 0.0333  0.0011  21  ILE D CG2 
12973 C CD1 . ILE D 21  ? 1.0570 0.9851 0.9780 -0.0510 0.0418  0.0079  21  ILE D CD1 
12985 N N   . LEU D 22  ? 0.9810 0.9549 0.9205 -0.0427 0.0327  -0.0045 22  LEU D N   
12986 C CA  . LEU D 22  ? 0.9599 0.9422 0.8968 -0.0419 0.0309  -0.0072 22  LEU D CA  
12987 C C   . LEU D 22  ? 0.9569 0.9535 0.8990 -0.0413 0.0277  -0.0044 22  LEU D C   
12988 O O   . LEU D 22  ? 0.9302 0.9298 0.8777 -0.0379 0.0283  0.0006  22  LEU D O   
12989 C CB  . LEU D 22  ? 0.9683 0.9454 0.9012 -0.0355 0.0351  -0.0071 22  LEU D CB  
12990 C CG  . LEU D 22  ? 0.9694 0.9320 0.8956 -0.0341 0.0386  -0.0102 22  LEU D CG  
12991 C CD1 . LEU D 22  ? 0.9714 0.9313 0.8974 -0.0274 0.0450  -0.0098 22  LEU D CD1 
12992 C CD2 . LEU D 22  ? 0.9931 0.9492 0.9082 -0.0383 0.0358  -0.0164 22  LEU D CD2 
13004 N N   . ILE D 23  ? 0.9601 0.9655 0.9008 -0.0440 0.0234  -0.0084 23  ILE D N   
13005 C CA  . ILE D 23  ? 0.9630 0.9813 0.9059 -0.0416 0.0196  -0.0067 23  ILE D CA  
13006 C C   . ILE D 23  ? 0.9436 0.9594 0.8749 -0.0351 0.0187  -0.0074 23  ILE D C   
13007 O O   . ILE D 23  ? 0.9948 1.0032 0.9157 -0.0336 0.0183  -0.0120 23  ILE D O   
13008 C CB  . ILE D 23  ? 0.9813 1.0122 0.9308 -0.0468 0.0152  -0.0119 23  ILE D CB  
13009 C CG1 . ILE D 23  ? 0.9648 0.9937 0.9230 -0.0543 0.0194  -0.0107 23  ILE D CG1 
13010 C CG2 . ILE D 23  ? 0.9899 1.0342 0.9403 -0.0421 0.0108  -0.0108 23  ILE D CG2 
13011 C CD1 . ILE D 23  ? 0.9630 0.9834 0.9207 -0.0515 0.0234  -0.0026 23  ILE D CD1 
13023 N N   . ASP D 24  ? 0.9507 0.9697 0.8808 -0.0309 0.0189  -0.0028 24  ASP D N   
13024 C CA  . ASP D 24  ? 0.9453 0.9571 0.8610 -0.0249 0.0204  -0.0022 24  ASP D CA  
13025 C C   . ASP D 24  ? 0.9500 0.9688 0.8584 -0.0206 0.0139  -0.0030 24  ASP D C   
13026 O O   . ASP D 24  ? 0.9740 1.0048 0.8921 -0.0219 0.0101  -0.0018 24  ASP D O   
13027 C CB  . ASP D 24  ? 0.9269 0.9330 0.8465 -0.0239 0.0277  0.0034  24  ASP D CB  
13028 C CG  . ASP D 24  ? 0.9950 0.9874 0.9019 -0.0209 0.0355  0.0028  24  ASP D CG  
13029 O OD1 . ASP D 24  ? 1.0414 1.0257 0.9325 -0.0183 0.0345  -0.0012 24  ASP D OD1 
13030 O OD2 . ASP D 24  ? 1.0102 0.9993 0.9228 -0.0212 0.0429  0.0059  24  ASP D OD2 
13035 N N   . ASN D 25  ? 0.9618 0.9709 0.8503 -0.0142 0.0127  -0.0054 25  ASN D N   
13036 C CA  . ASN D 25  ? 0.9380 0.9488 0.8137 -0.0070 0.0065  -0.0060 25  ASN D CA  
13037 C C   . ASN D 25  ? 0.9264 0.9562 0.8118 -0.0067 -0.0040 -0.0124 25  ASN D C   
13038 O O   . ASN D 25  ? 0.9271 0.9655 0.8119 -0.0021 -0.0091 -0.0122 25  ASN D O   
13039 C CB  . ASN D 25  ? 0.9299 0.9392 0.8073 -0.0064 0.0103  0.0013  25  ASN D CB  
13040 C CG  . ASN D 25  ? 0.9738 0.9669 0.8455 -0.0076 0.0213  0.0059  25  ASN D CG  
13041 O OD1 . ASN D 25  ? 0.9209 0.9172 0.8087 -0.0125 0.0261  0.0098  25  ASN D OD1 
13042 N ND2 . ASN D 25  ? 1.0346 1.0098 0.8833 -0.0028 0.0255  0.0046  25  ASN D ND2 
13049 N N   . PHE D 26  ? 0.9217 0.9578 0.8166 -0.0118 -0.0067 -0.0189 26  PHE D N   
13050 C CA  . PHE D 26  ? 0.9649 1.0209 0.8741 -0.0140 -0.0151 -0.0271 26  PHE D CA  
13051 C C   . PHE D 26  ? 0.9734 1.0274 0.8711 -0.0089 -0.0242 -0.0376 26  PHE D C   
13052 O O   . PHE D 26  ? 1.0445 1.0801 0.9255 -0.0066 -0.0219 -0.0380 26  PHE D O   
13053 C CB  . PHE D 26  ? 0.9746 1.0389 0.9063 -0.0262 -0.0102 -0.0270 26  PHE D CB  
13054 C CG  . PHE D 26  ? 0.9392 1.0258 0.8906 -0.0307 -0.0142 -0.0329 26  PHE D CG  
13055 C CD1 . PHE D 26  ? 0.9622 1.0600 0.9202 -0.0285 -0.0137 -0.0288 26  PHE D CD1 
13056 C CD2 . PHE D 26  ? 0.9921 1.0882 0.9562 -0.0378 -0.0176 -0.0431 26  PHE D CD2 
13057 C CE1 . PHE D 26  ? 0.9727 1.0918 0.9502 -0.0327 -0.0152 -0.0346 26  PHE D CE1 
13058 C CE2 . PHE D 26  ? 1.0006 1.1190 0.9866 -0.0434 -0.0192 -0.0495 26  PHE D CE2 
13059 C CZ  . PHE D 26  ? 0.9967 1.1272 0.9897 -0.0407 -0.0173 -0.0452 26  PHE D CZ  
13069 N N   . ASP D 27  ? 0.9732 1.0463 0.8799 -0.0061 -0.0348 -0.0468 27  ASP D N   
13070 C CA  . ASP D 27  ? 0.9911 1.0657 0.8905 -0.0007 -0.0466 -0.0595 27  ASP D CA  
13071 C C   . ASP D 27  ? 1.0548 1.1294 0.9676 -0.0125 -0.0445 -0.0648 27  ASP D C   
13072 O O   . ASP D 27  ? 1.0751 1.1681 1.0149 -0.0236 -0.0435 -0.0690 27  ASP D O   
13073 C CB  . ASP D 27  ? 0.9787 1.0788 0.8912 0.0047  -0.0589 -0.0696 27  ASP D CB  
13074 C CG  . ASP D 27  ? 1.0427 1.1495 0.9542 0.0096  -0.0735 -0.0855 27  ASP D CG  
13075 O OD1 . ASP D 27  ? 1.0687 1.1549 0.9608 0.0117  -0.0749 -0.0876 27  ASP D OD1 
13076 O OD2 . ASP D 27  ? 1.0484 1.1819 0.9793 0.0119  -0.0841 -0.0967 27  ASP D OD2 
13081 N N   . ILE D 28  ? 0.9931 1.0449 0.8854 -0.0101 -0.0425 -0.0645 28  ILE D N   
13082 C CA  . ILE D 28  ? 0.9895 1.0358 0.8901 -0.0205 -0.0390 -0.0678 28  ILE D CA  
13083 C C   . ILE D 28  ? 1.0709 1.1316 0.9849 -0.0245 -0.0511 -0.0834 28  ILE D C   
13084 O O   . ILE D 28  ? 1.0714 1.1281 0.9940 -0.0348 -0.0486 -0.0875 28  ILE D O   
13085 C CB  . ILE D 28  ? 1.0701 1.0875 0.9436 -0.0153 -0.0333 -0.0638 28  ILE D CB  
13086 C CG1 . ILE D 28  ? 1.0158 1.0210 0.8632 -0.0033 -0.0447 -0.0732 28  ILE D CG1 
13087 C CG2 . ILE D 28  ? 1.0370 1.0424 0.8995 -0.0112 -0.0218 -0.0505 28  ILE D CG2 
13088 C CD1 . ILE D 28  ? 1.0540 1.0311 0.8771 -0.0003 -0.0390 -0.0721 28  ILE D CD1 
13100 N N   . TYR D 29  ? 1.0547 1.1315 0.9704 -0.0160 -0.0646 -0.0931 29  TYR D N   
13101 C CA  . TYR D 29  ? 1.0320 1.1277 0.9656 -0.0192 -0.0780 -0.1105 29  TYR D CA  
13102 C C   . TYR D 29  ? 1.0522 1.1824 1.0197 -0.0246 -0.0804 -0.1159 29  TYR D C   
13103 O O   . TYR D 29  ? 1.0336 1.1856 1.0142 -0.0200 -0.0948 -0.1309 29  TYR D O   
13104 C CB  . TYR D 29  ? 1.0664 1.1525 0.9735 -0.0024 -0.0945 -0.1210 29  TYR D CB  
13105 C CG  . TYR D 29  ? 1.0537 1.1053 0.9273 0.0025  -0.0918 -0.1180 29  TYR D CG  
13106 C CD1 . TYR D 29  ? 1.0572 1.0996 0.9373 -0.0097 -0.0864 -0.1198 29  TYR D CD1 
13107 C CD2 . TYR D 29  ? 1.0504 1.0762 0.8839 0.0195  -0.0934 -0.1134 29  TYR D CD2 
13108 C CE1 . TYR D 29  ? 1.0892 1.1003 0.9385 -0.0043 -0.0833 -0.1173 29  TYR D CE1 
13109 C CE2 . TYR D 29  ? 1.0516 1.0452 0.8540 0.0242  -0.0887 -0.1107 29  TYR D CE2 
13110 C CZ  . TYR D 29  ? 1.0749 1.0626 0.8863 0.0125  -0.0840 -0.1128 29  TYR D CZ  
13111 O OH  . TYR D 29  ? 1.1206 1.0764 0.9010 0.0180  -0.0788 -0.1104 29  TYR D OH  
13121 N N   . ASP D 30  ? 1.0705 1.2057 1.0522 -0.0335 -0.0664 -0.1044 30  ASP D N   
13122 C CA  . ASP D 30  ? 1.0765 1.2417 1.0887 -0.0391 -0.0652 -0.1079 30  ASP D CA  
13123 C C   . ASP D 30  ? 1.0744 1.2552 1.1183 -0.0570 -0.0621 -0.1186 30  ASP D C   
13124 O O   . ASP D 30  ? 1.0801 1.2435 1.1225 -0.0689 -0.0523 -0.1144 30  ASP D O   
13125 C CB  . ASP D 30  ? 1.0778 1.2380 1.0886 -0.0409 -0.0513 -0.0915 30  ASP D CB  
13126 C CG  . ASP D 30  ? 1.1233 1.3116 1.1589 -0.0427 -0.0499 -0.0940 30  ASP D CG  
13127 O OD1 . ASP D 30  ? 1.1552 1.3612 1.2197 -0.0563 -0.0451 -0.1012 30  ASP D OD1 
13128 O OD2 . ASP D 30  ? 1.1406 1.3319 1.1662 -0.0307 -0.0526 -0.0887 30  ASP D OD2 
13133 N N   . LYS D 31  ? 1.0814 1.2946 1.1541 -0.0589 -0.0702 -0.1331 31  LYS D N   
13134 C CA  . LYS D 31  ? 1.0862 1.3160 1.1925 -0.0775 -0.0663 -0.1452 31  LYS D CA  
13135 C C   . LYS D 31  ? 1.0863 1.3073 1.2021 -0.0940 -0.0449 -0.1334 31  LYS D C   
13136 O O   . LYS D 31  ? 1.0773 1.2911 1.2043 -0.1104 -0.0371 -0.1374 31  LYS D O   
13137 C CB  . LYS D 31  ? 1.0787 1.3496 1.2193 -0.0763 -0.0768 -0.1628 31  LYS D CB  
13138 C CG  . LYS D 31  ? 1.1175 1.4096 1.2981 -0.0969 -0.0730 -0.1785 31  LYS D CG  
13139 C CD  . LYS D 31  ? 1.1132 1.4168 1.3193 -0.1127 -0.0520 -0.1722 31  LYS D CD  
13140 C CE  . LYS D 31  ? 1.1347 1.4638 1.3846 -0.1333 -0.0475 -0.1903 31  LYS D CE  
13141 N NZ  . LYS D 31  ? 1.1747 1.4760 1.4207 -0.1533 -0.0326 -0.1863 31  LYS D NZ  
13155 N N   . ASN D 32  ? 1.0775 1.2958 1.1862 -0.0891 -0.0356 -0.1191 32  ASN D N   
13156 C CA  . ASN D 32  ? 1.0680 1.2759 1.1815 -0.1016 -0.0165 -0.1077 32  ASN D CA  
13157 C C   . ASN D 32  ? 1.0508 1.2220 1.1369 -0.1031 -0.0084 -0.0942 32  ASN D C   
13158 O O   . ASN D 32  ? 1.0425 1.1999 1.1254 -0.1095 0.0058  -0.0834 32  ASN D O   
13159 C CB  . ASN D 32  ? 1.0906 1.3097 1.2059 -0.0943 -0.0114 -0.0989 32  ASN D CB  
13160 C CG  . ASN D 32  ? 1.0973 1.3540 1.2390 -0.0899 -0.0197 -0.1122 32  ASN D CG  
13161 O OD1 . ASN D 32  ? 1.0751 1.3545 1.2489 -0.1026 -0.0157 -0.1246 32  ASN D OD1 
13162 N ND2 . ASN D 32  ? 1.0761 1.3393 1.2047 -0.0718 -0.0308 -0.1103 32  ASN D ND2 
13169 N N   . ILE D 33  ? 1.0800 1.2345 1.1455 -0.0961 -0.0171 -0.0950 33  ILE D N   
13170 C CA  . ILE D 33  ? 1.0745 1.1968 1.1164 -0.0961 -0.0096 -0.0833 33  ILE D CA  
13171 C C   . ILE D 33  ? 1.0568 1.1652 1.1054 -0.1122 0.0039  -0.0817 33  ILE D C   
13172 O O   . ILE D 33  ? 1.0502 1.1395 1.0865 -0.1122 0.0143  -0.0690 33  ILE D O   
13173 C CB  . ILE D 33  ? 1.0583 1.1661 1.0797 -0.0878 -0.0199 -0.0875 33  ILE D CB  
13174 C CG1 . ILE D 33  ? 1.0726 1.1787 1.0744 -0.0704 -0.0267 -0.0816 33  ILE D CG1 
13175 C CG2 . ILE D 33  ? 1.0677 1.1458 1.0730 -0.0923 -0.0116 -0.0809 33  ILE D CG2 
13176 C CD1 . ILE D 33  ? 1.0596 1.1461 1.0443 -0.0657 -0.0171 -0.0658 33  ILE D CD1 
13188 N N   . PRO D 34  ? 1.0501 1.1648 1.1163 -0.1259 0.0042  -0.0943 34  PRO D N   
13189 C CA  . PRO D 34  ? 1.0627 1.1568 1.1293 -0.1413 0.0187  -0.0918 34  PRO D CA  
13190 C C   . PRO D 34  ? 1.0637 1.1579 1.1368 -0.1471 0.0338  -0.0830 34  PRO D C   
13191 O O   . PRO D 34  ? 1.0624 1.1284 1.1189 -0.1504 0.0456  -0.0729 34  PRO D O   
13192 C CB  . PRO D 34  ? 1.0665 1.1728 1.1552 -0.1554 0.0149  -0.1097 34  PRO D CB  
13193 C CG  . PRO D 34  ? 1.0458 1.1707 1.1364 -0.1437 -0.0048 -0.1206 34  PRO D CG  
13194 C CD  . PRO D 34  ? 1.0646 1.2029 1.1493 -0.1275 -0.0093 -0.1123 34  PRO D CD  
13202 N N   . LYS D 35  ? 1.0503 1.1738 1.1450 -0.1470 0.0336  -0.0869 35  LYS D N   
13203 C CA  . LYS D 35  ? 1.0436 1.1659 1.1423 -0.1516 0.0489  -0.0787 35  LYS D CA  
13204 C C   . LYS D 35  ? 1.0342 1.1359 1.1059 -0.1383 0.0509  -0.0616 35  LYS D C   
13205 O O   . LYS D 35  ? 1.0609 1.1384 1.1189 -0.1417 0.0637  -0.0520 35  LYS D O   
13206 C CB  . LYS D 35  ? 1.0091 1.1692 1.1366 -0.1518 0.0472  -0.0870 35  LYS D CB  
13207 C CG  . LYS D 35  ? 1.0572 1.2265 1.2100 -0.1704 0.0638  -0.0938 35  LYS D CG  
13208 C CD  . LYS D 35  ? 1.0834 1.2421 1.2450 -0.1882 0.0680  -0.1044 35  LYS D CD  
13209 C CE  . LYS D 35  ? 1.1044 1.2925 1.3066 -0.2056 0.0760  -0.1204 35  LYS D CE  
13210 N NZ  . LYS D 35  ? 1.2160 1.3838 1.4226 -0.2267 0.0876  -0.1271 35  LYS D NZ  
13224 N N   . LEU D 36  ? 1.0318 1.1412 1.0945 -0.1227 0.0383  -0.0584 36  LEU D N   
13225 C CA  . LEU D 36  ? 1.0463 1.1368 1.0860 -0.1110 0.0391  -0.0441 36  LEU D CA  
13226 C C   . LEU D 36  ? 1.0726 1.1310 1.0931 -0.1130 0.0440  -0.0384 36  LEU D C   
13227 O O   . LEU D 36  ? 1.0547 1.0931 1.0608 -0.1101 0.0512  -0.0281 36  LEU D O   
13228 C CB  . LEU D 36  ? 1.0427 1.1430 1.0750 -0.0963 0.0258  -0.0432 36  LEU D CB  
13229 C CG  . LEU D 36  ? 1.0412 1.1708 1.0874 -0.0904 0.0177  -0.0498 36  LEU D CG  
13230 C CD1 . LEU D 36  ? 1.0315 1.1595 1.0609 -0.0749 0.0078  -0.0451 36  LEU D CD1 
13231 C CD2 . LEU D 36  ? 1.0567 1.1981 1.1150 -0.0934 0.0265  -0.0469 36  LEU D CD2 
13243 N N   . SER D 37  ? 1.0811 1.1332 1.0996 -0.1166 0.0393  -0.0456 37  SER D N   
13244 C CA  . SER D 37  ? 1.0975 1.1191 1.0972 -0.1172 0.0434  -0.0411 37  SER D CA  
13245 C C   . SER D 37  ? 1.0827 1.0831 1.0774 -0.1272 0.0575  -0.0372 37  SER D C   
13246 O O   . SER D 37  ? 1.0647 1.0393 1.0397 -0.1219 0.0621  -0.0282 37  SER D O   
13247 C CB  . SER D 37  ? 1.0985 1.1171 1.0977 -0.1209 0.0368  -0.0512 37  SER D CB  
13248 O OG  . SER D 37  ? 1.1286 1.1585 1.1241 -0.1093 0.0249  -0.0533 37  SER D OG  
13254 N N   . GLU D 38  ? 1.0782 1.0886 1.0902 -0.1413 0.0649  -0.0444 38  GLU D N   
13255 C CA  . GLU D 38  ? 1.1142 1.1003 1.1185 -0.1521 0.0810  -0.0408 38  GLU D CA  
13256 C C   . GLU D 38  ? 1.0818 1.0557 1.0709 -0.1431 0.0874  -0.0280 38  GLU D C   
13257 O O   . GLU D 38  ? 1.1108 1.0514 1.0754 -0.1398 0.0938  -0.0200 38  GLU D O   
13258 C CB  . GLU D 38  ? 1.1337 1.1375 1.1640 -0.1697 0.0895  -0.0518 38  GLU D CB  
13259 C CG  . GLU D 38  ? 1.2076 1.1815 1.2301 -0.1860 0.1048  -0.0539 38  GLU D CG  
13260 C CD  . GLU D 38  ? 1.2218 1.2128 1.2720 -0.2047 0.1176  -0.0635 38  GLU D CD  
13261 O OE1 . GLU D 38  ? 1.2232 1.2546 1.3047 -0.2064 0.1098  -0.0739 38  GLU D OE1 
13262 O OE2 . GLU D 38  ? 1.2888 1.2520 1.3291 -0.2174 0.1359  -0.0612 38  GLU D OE2 
13269 N N   . GLU D 39  ? 1.0704 1.0694 1.0720 -0.1378 0.0850  -0.0265 39  GLU D N   
13270 C CA  . GLU D 39  ? 1.1349 1.1222 1.1219 -0.1292 0.0905  -0.0152 39  GLU D CA  
13271 C C   . GLU D 39  ? 1.1018 1.0694 1.0660 -0.1142 0.0826  -0.0063 39  GLU D C   
13272 O O   . GLU D 39  ? 1.1537 1.0925 1.0960 -0.1096 0.0885  0.0016  39  GLU D O   
13273 C CB  . GLU D 39  ? 1.1113 1.1301 1.1152 -0.1246 0.0871  -0.0160 39  GLU D CB  
13274 C CG  . GLU D 39  ? 1.2381 1.2537 1.2429 -0.1299 0.1022  -0.0129 39  GLU D CG  
13275 C CD  . GLU D 39  ? 1.2997 1.3470 1.3211 -0.1239 0.0984  -0.0142 39  GLU D CD  
13276 O OE1 . GLU D 39  ? 1.2544 1.2959 1.2611 -0.1112 0.0953  -0.0052 39  GLU D OE1 
13277 O OE2 . GLU D 39  ? 1.3103 1.3883 1.3593 -0.1314 0.0978  -0.0251 39  GLU D OE2 
13284 N N   . ILE D 40  ? 1.0836 1.0657 1.0526 -0.1061 0.0695  -0.0082 40  ILE D N   
13285 C CA  . ILE D 40  ? 1.0883 1.0568 1.0416 -0.0928 0.0628  -0.0013 40  ILE D CA  
13286 C C   . ILE D 40  ? 1.1084 1.0439 1.0425 -0.0930 0.0676  0.0010  40  ILE D C   
13287 O O   . ILE D 40  ? 1.0788 0.9962 0.9970 -0.0826 0.0663  0.0077  40  ILE D O   
13288 C CB  . ILE D 40  ? 1.0903 1.0765 1.0510 -0.0865 0.0513  -0.0048 40  ILE D CB  
13289 C CG1 . ILE D 40  ? 1.1205 1.1343 1.0943 -0.0833 0.0458  -0.0060 40  ILE D CG1 
13290 C CG2 . ILE D 40  ? 1.1055 1.0783 1.0539 -0.0748 0.0468  0.0008  40  ILE D CG2 
13291 C CD1 . ILE D 40  ? 1.1321 1.1578 1.1071 -0.0754 0.0358  -0.0081 40  ILE D CD1 
13303 N N   . MET D 41  ? 1.1347 1.0614 1.0695 -0.1040 0.0720  -0.0054 41  MET D N   
13304 C CA  . MET D 41  ? 1.1028 0.9961 1.0167 -0.1031 0.0757  -0.0038 41  MET D CA  
13305 C C   . MET D 41  ? 1.1391 1.0014 1.0328 -0.1049 0.0875  0.0021  41  MET D C   
13306 O O   . MET D 41  ? 1.1417 0.9725 1.0119 -0.0981 0.0887  0.0057  41  MET D O   
13307 C CB  . MET D 41  ? 1.0933 0.9838 1.0119 -0.1146 0.0768  -0.0129 41  MET D CB  
13308 C CG  . MET D 41  ? 1.1215 1.0130 1.0373 -0.1067 0.0671  -0.0156 41  MET D CG  
13309 S SD  . MET D 41  ? 1.1862 1.0736 1.1057 -0.1196 0.0667  -0.0274 41  MET D SD  
13310 C CE  . MET D 41  ? 1.0974 1.0148 1.0447 -0.1351 0.0686  -0.0361 41  MET D CE  
13320 N N   . LYS D 42  ? 1.1493 1.0180 1.0496 -0.1130 0.0966  0.0028  42  LYS D N   
13321 C CA  . LYS D 42  ? 1.1718 1.0066 1.0493 -0.1161 0.1108  0.0081  42  LYS D CA  
13322 C C   . LYS D 42  ? 1.1610 0.9709 1.0114 -0.0979 0.1061  0.0172  42  LYS D C   
13323 O O   . LYS D 42  ? 1.1399 0.9673 0.9965 -0.0849 0.0939  0.0198  42  LYS D O   
13324 C CB  . LYS D 42  ? 1.1542 1.0043 1.0455 -0.1259 0.1218  0.0075  42  LYS D CB  
13325 C CG  . LYS D 42  ? 1.1915 1.0551 1.1053 -0.1466 0.1312  -0.0027 42  LYS D CG  
13326 C CD  . LYS D 42  ? 1.2309 1.1129 1.1622 -0.1560 0.1433  -0.0044 42  LYS D CD  
13327 C CE  . LYS D 42  ? 1.2415 1.1681 1.2130 -0.1670 0.1385  -0.0172 42  LYS D CE  
13328 N NZ  . LYS D 42  ? 1.2992 1.2562 1.2915 -0.1675 0.1425  -0.0183 42  LYS D NZ  
13342 N N   . GLU D 43  ? 1.2127 0.9796 1.0320 -0.0968 0.1158  0.0213  43  GLU D N   
13343 C CA  . GLU D 43  ? 1.2519 0.9907 1.0418 -0.0781 0.1108  0.0288  43  GLU D CA  
13344 C C   . GLU D 43  ? 1.2351 0.9810 1.0230 -0.0708 0.1108  0.0344  43  GLU D C   
13345 O O   . GLU D 43  ? 1.2529 0.9887 1.0257 -0.0533 0.1006  0.0388  43  GLU D O   
13346 C CB  . GLU D 43  ? 1.2881 0.9745 1.0402 -0.0784 0.1221  0.0314  43  GLU D CB  
13347 C CG  . GLU D 43  ? 1.3854 1.0375 1.1026 -0.0568 0.1151  0.0374  43  GLU D CG  
13348 C CD  . GLU D 43  ? 1.4873 1.0874 1.1626 -0.0569 0.1310  0.0431  43  GLU D CD  
13349 O OE1 . GLU D 43  ? 1.5023 1.0906 1.1764 -0.0760 0.1493  0.0418  43  GLU D OE1 
13350 O OE2 . GLU D 43  ? 1.4619 1.0321 1.1050 -0.0380 0.1256  0.0483  43  GLU D OE2 
13357 N N   . THR D 44  ? 1.2190 0.9828 1.0226 -0.0833 0.1212  0.0335  44  THR D N   
13358 C CA  . THR D 44  ? 1.1997 0.9730 1.0031 -0.0770 0.1218  0.0383  44  THR D CA  
13359 C C   . THR D 44  ? 1.1469 0.9664 0.9817 -0.0735 0.1080  0.0356  44  THR D C   
13360 O O   . THR D 44  ? 1.1257 0.9633 0.9702 -0.0739 0.1104  0.0369  44  THR D O   
13361 C CB  . THR D 44  ? 1.1819 0.9484 0.9845 -0.0915 0.1424  0.0385  44  THR D CB  
13362 O OG1 . THR D 44  ? 1.2115 1.0023 1.0439 -0.1108 0.1489  0.0297  44  THR D OG1 
13363 C CG2 . THR D 44  ? 1.2267 0.9381 0.9872 -0.0906 0.1572  0.0440  44  THR D CG2 
13371 N N   . ASN D 45  ? 1.1707 1.0067 1.0190 -0.0694 0.0946  0.0320  45  ASN D N   
13372 C CA  . ASN D 45  ? 1.1109 0.9843 0.9840 -0.0653 0.0816  0.0296  45  ASN D CA  
13373 C C   . ASN D 45  ? 1.0722 0.9401 0.9404 -0.0530 0.0689  0.0299  45  ASN D C   
13374 O O   . ASN D 45  ? 1.1511 0.9890 0.9967 -0.0446 0.0685  0.0327  45  ASN D O   
13375 C CB  . ASN D 45  ? 1.1029 1.0059 1.0029 -0.0792 0.0834  0.0217  45  ASN D CB  
13376 C CG  . ASN D 45  ? 1.1303 1.0681 1.0509 -0.0778 0.0778  0.0203  45  ASN D CG  
13377 O OD1 . ASN D 45  ? 1.1125 1.0635 1.0376 -0.0681 0.0662  0.0215  45  ASN D OD1 
13378 N ND2 . ASN D 45  ? 1.1598 1.1124 1.0936 -0.0876 0.0866  0.0169  45  ASN D ND2 
13385 N N   . LEU D 46  ? 1.1228 1.0184 1.0110 -0.0510 0.0591  0.0267  46  LEU D N   
13386 C CA  . LEU D 46  ? 1.1250 1.0173 1.0135 -0.0440 0.0513  0.0247  46  LEU D CA  
13387 C C   . LEU D 46  ? 1.1418 1.0171 1.0230 -0.0522 0.0581  0.0212  46  LEU D C   
13388 O O   . LEU D 46  ? 1.2572 1.1407 1.1473 -0.0653 0.0645  0.0173  46  LEU D O   
13389 C CB  . LEU D 46  ? 1.1343 1.0566 1.0437 -0.0431 0.0435  0.0217  46  LEU D CB  
13390 C CG  . LEU D 46  ? 1.1418 1.0667 1.0548 -0.0318 0.0347  0.0215  46  LEU D CG  
13391 C CD1 . LEU D 46  ? 1.1058 1.0282 1.0148 -0.0214 0.0288  0.0255  46  LEU D CD1 
13392 C CD2 . LEU D 46  ? 1.0640 1.0127 0.9940 -0.0337 0.0313  0.0181  46  LEU D CD2 
13404 N N   . TYR D 47  ? 1.1270 0.9770 0.9912 -0.0445 0.0567  0.0218  47  TYR D N   
13405 C CA  . TYR D 47  ? 1.1679 0.9951 1.0199 -0.0516 0.0637  0.0189  47  TYR D CA  
13406 C C   . TYR D 47  ? 1.0836 0.9238 0.9478 -0.0522 0.0585  0.0133  47  TYR D C   
13407 O O   . TYR D 47  ? 1.0380 0.8934 0.9122 -0.0425 0.0501  0.0129  47  TYR D O   
13408 C CB  . TYR D 47  ? 1.1441 0.9321 0.9656 -0.0408 0.0651  0.0227  47  TYR D CB  
13409 C CG  . TYR D 47  ? 1.2112 0.9641 1.0101 -0.0459 0.0736  0.0214  47  TYR D CG  
13410 C CD1 . TYR D 47  ? 1.2124 0.9653 1.0172 -0.0639 0.0833  0.0173  47  TYR D CD1 
13411 C CD2 . TYR D 47  ? 1.3106 1.0285 1.0809 -0.0318 0.0712  0.0235  47  TYR D CD2 
13412 C CE1 . TYR D 47  ? 1.2634 0.9802 1.0452 -0.0690 0.0916  0.0159  47  TYR D CE1 
13413 C CE2 . TYR D 47  ? 1.3086 0.9893 1.0534 -0.0349 0.0790  0.0227  47  TYR D CE2 
13414 C CZ  . TYR D 47  ? 1.3040 0.9830 1.0540 -0.0543 0.0899  0.0192  47  TYR D CZ  
13415 O OH  . TYR D 47  ? 1.4324 1.0710 1.1550 -0.0580 0.0981  0.0182  47  TYR D OH  
13424 N N   . ALA D 48  ? 1.0938 0.9279 0.9576 -0.0642 0.0643  0.0085  48  ALA D N   
13425 C CA  . ALA D 48  ? 1.1092 0.9517 0.9804 -0.0641 0.0597  0.0030  48  ALA D CA  
13426 C C   . ALA D 48  ? 1.0947 0.9209 0.9589 -0.0766 0.0660  -0.0026 48  ALA D C   
13427 O O   . ALA D 48  ? 1.1319 0.9515 0.9954 -0.0896 0.0742  -0.0038 48  ALA D O   
13428 C CB  . ALA D 48  ? 1.0443 0.9225 0.9386 -0.0654 0.0537  0.0003  48  ALA D CB  
13434 N N   . GLU D 49  ? 1.0867 0.9071 0.9469 -0.0729 0.0625  -0.0066 49  GLU D N   
13435 C CA  . GLU D 49  ? 1.1234 0.9295 0.9776 -0.0839 0.0661  -0.0132 49  GLU D CA  
13436 C C   . GLU D 49  ? 1.0884 0.9219 0.9623 -0.0925 0.0617  -0.0207 49  GLU D C   
13437 O O   . GLU D 49  ? 1.0924 0.9211 0.9681 -0.1058 0.0644  -0.0277 49  GLU D O   
13438 C CB  . GLU D 49  ? 1.1380 0.9201 0.9739 -0.0736 0.0643  -0.0141 49  GLU D CB  
13439 C CG  . GLU D 49  ? 1.1791 0.9355 0.9948 -0.0603 0.0654  -0.0079 49  GLU D CG  
13440 C CD  . GLU D 49  ? 1.2483 0.9690 1.0387 -0.0551 0.0673  -0.0100 49  GLU D CD  
13441 O OE1 . GLU D 49  ? 1.2505 0.9421 1.0182 -0.0456 0.0690  -0.0059 49  GLU D OE1 
13442 O OE2 . GLU D 49  ? 1.3193 1.0390 1.1101 -0.0592 0.0665  -0.0158 49  GLU D OE2 
13449 N N   . GLN D 50  ? 1.0682 0.9289 0.9559 -0.0850 0.0546  -0.0200 50  GLN D N   
13450 C CA  . GLN D 50  ? 1.0915 0.9757 0.9932 -0.0897 0.0489  -0.0268 50  GLN D CA  
13451 C C   . GLN D 50  ? 1.0729 0.9835 0.9872 -0.0822 0.0442  -0.0230 50  GLN D C   
13452 O O   . GLN D 50  ? 1.0487 0.9591 0.9617 -0.0735 0.0447  -0.0158 50  GLN D O   
13453 C CB  . GLN D 50  ? 1.0500 0.9254 0.9426 -0.0856 0.0453  -0.0321 50  GLN D CB  
13454 C CG  . GLN D 50  ? 1.0881 0.9648 0.9762 -0.0704 0.0435  -0.0274 50  GLN D CG  
13455 C CD  . GLN D 50  ? 1.1074 0.9650 0.9807 -0.0649 0.0439  -0.0308 50  GLN D CD  
13456 O OE1 . GLN D 50  ? 1.1595 1.0054 1.0253 -0.0545 0.0461  -0.0272 50  GLN D OE1 
13457 N NE2 . GLN D 50  ? 1.0356 0.8901 0.9046 -0.0708 0.0410  -0.0387 50  GLN D NE2 
13466 N N   . VAL D 51  ? 1.0880 1.0197 1.0130 -0.0849 0.0386  -0.0285 51  VAL D N   
13467 C CA  . VAL D 51  ? 1.1263 1.0799 1.0599 -0.0779 0.0343  -0.0252 51  VAL D CA  
13468 C C   . VAL D 51  ? 1.1308 1.0950 1.0639 -0.0750 0.0273  -0.0317 51  VAL D C   
13469 O O   . VAL D 51  ? 1.1210 1.0880 1.0566 -0.0818 0.0235  -0.0406 51  VAL D O   
13470 C CB  . VAL D 51  ? 1.1125 1.0816 1.0587 -0.0833 0.0355  -0.0236 51  VAL D CB  
13471 C CG1 . VAL D 51  ? 1.1708 1.1485 1.1279 -0.0959 0.0355  -0.0328 51  VAL D CG1 
13472 C CG2 . VAL D 51  ? 1.0454 1.0347 0.9977 -0.0755 0.0304  -0.0207 51  VAL D CG2 
13482 N N   . GLY D 52  ? 1.0752 1.0433 1.0040 -0.0647 0.0258  -0.0278 52  GLY D N   
13483 C CA  . GLY D 52  ? 1.0106 0.9833 0.9325 -0.0595 0.0204  -0.0325 52  GLY D CA  
13484 C C   . GLY D 52  ? 0.9893 0.9776 0.9144 -0.0537 0.0175  -0.0292 52  GLY D C   
13485 O O   . GLY D 52  ? 1.0292 1.0242 0.9620 -0.0528 0.0201  -0.0225 52  GLY D O   
13489 N N   . PHE D 53  ? 1.0024 0.9934 0.9182 -0.0486 0.0117  -0.0341 53  PHE D N   
13490 C CA  . PHE D 53  ? 0.9910 0.9930 0.9047 -0.0422 0.0080  -0.0322 53  PHE D CA  
13491 C C   . PHE D 53  ? 1.0287 1.0173 0.9216 -0.0327 0.0093  -0.0318 53  PHE D C   
13492 O O   . PHE D 53  ? 1.0275 1.0050 0.9066 -0.0303 0.0064  -0.0380 53  PHE D O   
13493 C CB  . PHE D 53  ? 0.9897 1.0088 0.9113 -0.0444 -0.0016 -0.0404 53  PHE D CB  
13494 C CG  . PHE D 53  ? 1.0234 1.0554 0.9659 -0.0548 0.0001  -0.0411 53  PHE D CG  
13495 C CD1 . PHE D 53  ? 1.0012 1.0283 0.9506 -0.0649 0.0021  -0.0463 53  PHE D CD1 
13496 C CD2 . PHE D 53  ? 1.0056 1.0518 0.9586 -0.0545 0.0010  -0.0365 53  PHE D CD2 
13497 C CE1 . PHE D 53  ? 1.0294 1.0645 0.9954 -0.0752 0.0064  -0.0467 53  PHE D CE1 
13498 C CE2 . PHE D 53  ? 1.0078 1.0630 0.9773 -0.0637 0.0048  -0.0368 53  PHE D CE2 
13499 C CZ  . PHE D 53  ? 1.0346 1.0838 1.0105 -0.0744 0.0083  -0.0418 53  PHE D CZ  
13509 N N   . ILE D 54  ? 1.0032 0.9909 0.8925 -0.0274 0.0140  -0.0247 54  ILE D N   
13510 C CA  . ILE D 54  ? 1.0351 1.0066 0.9056 -0.0201 0.0205  -0.0223 54  ILE D CA  
13511 C C   . ILE D 54  ? 1.0458 1.0141 0.8974 -0.0122 0.0155  -0.0240 54  ILE D C   
13512 O O   . ILE D 54  ? 1.0533 1.0343 0.9103 -0.0113 0.0094  -0.0235 54  ILE D O   
13513 C CB  . ILE D 54  ? 1.0282 0.9989 0.9084 -0.0207 0.0309  -0.0143 54  ILE D CB  
13514 C CG1 . ILE D 54  ? 1.0547 1.0211 0.9447 -0.0239 0.0365  -0.0140 54  ILE D CG1 
13515 C CG2 . ILE D 54  ? 1.1120 1.0698 0.9756 -0.0145 0.0390  -0.0114 54  ILE D CG2 
13516 C CD1 . ILE D 54  ? 1.0457 1.0154 0.9502 -0.0238 0.0440  -0.0084 54  ILE D CD1 
13528 N N   . LYS D 55  ? 1.0496 0.9982 0.8759 -0.0050 0.0184  -0.0260 55  LYS D N   
13529 C CA  . LYS D 55  ? 1.1006 1.0378 0.9008 0.0049  0.0157  -0.0265 55  LYS D CA  
13530 C C   . LYS D 55  ? 1.1067 1.0172 0.8816 0.0104  0.0280  -0.0242 55  LYS D C   
13531 O O   . LYS D 55  ? 1.1176 1.0143 0.8764 0.0140  0.0267  -0.0295 55  LYS D O   
13532 C CB  . LYS D 55  ? 1.0810 1.0227 0.8718 0.0103  -0.0004 -0.0365 55  LYS D CB  
13533 C CG  . LYS D 55  ? 1.0890 1.0174 0.8496 0.0232  -0.0057 -0.0378 55  LYS D CG  
13534 C CD  . LYS D 55  ? 1.1166 1.0545 0.8730 0.0297  -0.0245 -0.0499 55  LYS D CD  
13535 C CE  . LYS D 55  ? 1.0424 0.9572 0.7580 0.0464  -0.0306 -0.0529 55  LYS D CE  
13536 N NZ  . LYS D 55  ? 1.1090 1.0412 0.8280 0.0538  -0.0459 -0.0588 55  LYS D NZ  
13550 N N   . ASP D 56  ? 1.1503 1.0531 0.9223 0.0105  0.0407  -0.0167 56  ASP D N   
13551 C CA  . ASP D 56  ? 1.1857 1.0640 0.9372 0.0140  0.0565  -0.0138 56  ASP D CA  
13552 C C   . ASP D 56  ? 1.1773 1.0575 0.9431 0.0095  0.0629  -0.0153 56  ASP D C   
13553 O O   . ASP D 56  ? 1.1854 1.0837 0.9822 0.0018  0.0652  -0.0128 56  ASP D O   
13554 C CB  . ASP D 56  ? 1.1563 1.0080 0.8649 0.0260  0.0534  -0.0173 56  ASP D CB  
13555 C CG  . ASP D 56  ? 1.2698 1.0912 0.9509 0.0302  0.0728  -0.0129 56  ASP D CG  
13556 O OD1 . ASP D 56  ? 1.3655 1.1585 1.0060 0.0412  0.0726  -0.0156 56  ASP D OD1 
13557 O OD2 . ASP D 56  ? 1.3149 1.1406 1.0152 0.0226  0.0885  -0.0074 56  ASP D OD2 
13562 N N   . SER D 57  ? 1.1752 1.0362 0.9182 0.0151  0.0652  -0.0194 57  SER D N   
13563 C CA  . SER D 57  ? 1.1413 1.0013 0.8944 0.0123  0.0713  -0.0211 57  SER D CA  
13564 C C   . SER D 57  ? 1.0631 0.9300 0.8213 0.0104  0.0564  -0.0282 57  SER D C   
13565 O O   . SER D 57  ? 1.1059 0.9663 0.8649 0.0098  0.0599  -0.0306 57  SER D O   
13566 C CB  . SER D 57  ? 1.1821 1.0139 0.9058 0.0197  0.0857  -0.0212 57  SER D CB  
13567 O OG  . SER D 57  ? 1.1944 1.0143 0.9067 0.0214  0.1003  -0.0156 57  SER D OG  
13573 N N   . HIS D 58  ? 1.0471 0.9264 0.8091 0.0091  0.0408  -0.0321 58  HIS D N   
13574 C CA  . HIS D 58  ? 1.0683 0.9547 0.8371 0.0055  0.0274  -0.0403 58  HIS D CA  
13575 C C   . HIS D 58  ? 1.0530 0.9633 0.8562 -0.0055 0.0243  -0.0385 58  HIS D C   
13576 O O   . HIS D 58  ? 1.0396 0.9646 0.8583 -0.0083 0.0253  -0.0331 58  HIS D O   
13577 C CB  . HIS D 58  ? 1.0225 0.9081 0.7744 0.0117  0.0117  -0.0484 58  HIS D CB  
13578 C CG  . HIS D 58  ? 1.0914 0.9883 0.8560 0.0059  -0.0024 -0.0585 58  HIS D CG  
13579 N ND1 . HIS D 58  ? 1.0964 0.9805 0.8546 0.0042  -0.0030 -0.0641 58  HIS D ND1 
13580 C CD2 . HIS D 58  ? 1.0849 1.0043 0.8692 0.0008  -0.0153 -0.0647 58  HIS D CD2 
13581 C CE1 . HIS D 58  ? 1.0909 0.9885 0.8645 -0.0029 -0.0158 -0.0734 58  HIS D CE1 
13582 N NE2 . HIS D 58  ? 1.1261 1.0464 0.9171 -0.0053 -0.0229 -0.0742 58  HIS D NE2 
13590 N N   . LEU D 59  ? 1.0712 0.9819 0.8831 -0.0115 0.0208  -0.0432 59  LEU D N   
13591 C CA  . LEU D 59  ? 1.0154 0.9419 0.8540 -0.0217 0.0192  -0.0420 59  LEU D CA  
13592 C C   . LEU D 59  ? 1.0188 0.9517 0.8625 -0.0280 0.0072  -0.0517 59  LEU D C   
13593 O O   . LEU D 59  ? 1.0638 0.9835 0.8966 -0.0284 0.0040  -0.0587 59  LEU D O   
13594 C CB  . LEU D 59  ? 0.9950 0.9128 0.8395 -0.0238 0.0288  -0.0383 59  LEU D CB  
13595 C CG  . LEU D 59  ? 1.0140 0.9376 0.8762 -0.0330 0.0271  -0.0385 59  LEU D CG  
13596 C CD1 . LEU D 59  ? 1.0104 0.9531 0.8915 -0.0378 0.0251  -0.0341 59  LEU D CD1 
13597 C CD2 . LEU D 59  ? 1.0015 0.9136 0.8647 -0.0310 0.0359  -0.0349 59  LEU D CD2 
13609 N N   . GLN D 60  ? 1.0549 1.0082 0.9160 -0.0331 0.0009  -0.0529 60  GLN D N   
13610 C CA  . GLN D 60  ? 1.0411 1.0057 0.9135 -0.0404 -0.0096 -0.0634 60  GLN D CA  
13611 C C   . GLN D 60  ? 1.0416 1.0121 0.9352 -0.0531 -0.0042 -0.0612 60  GLN D C   
13612 O O   . GLN D 60  ? 1.0069 0.9918 0.9164 -0.0568 -0.0015 -0.0560 60  GLN D O   
13613 C CB  . GLN D 60  ? 1.0124 0.9965 0.8904 -0.0368 -0.0195 -0.0676 60  GLN D CB  
13614 C CG  . GLN D 60  ? 1.0362 1.0350 0.9278 -0.0429 -0.0317 -0.0815 60  GLN D CG  
13615 C CD  . GLN D 60  ? 1.0055 0.9889 0.8782 -0.0383 -0.0406 -0.0922 60  GLN D CD  
13616 O OE1 . GLN D 60  ? 1.0221 0.9889 0.8672 -0.0254 -0.0425 -0.0913 60  GLN D OE1 
13617 N NE2 . GLN D 60  ? 1.0299 1.0162 0.9155 -0.0489 -0.0454 -0.1026 60  GLN D NE2 
13626 N N   . MET D 61  ? 1.0306 0.9864 0.9210 -0.0590 -0.0023 -0.0652 61  MET D N   
13627 C CA  . MET D 61  ? 1.0542 1.0092 0.9590 -0.0709 0.0034  -0.0637 61  MET D CA  
13628 C C   . MET D 61  ? 1.0887 1.0646 1.0148 -0.0814 -0.0017 -0.0712 61  MET D C   
13629 O O   . MET D 61  ? 1.0635 1.0534 0.9936 -0.0799 -0.0123 -0.0808 61  MET D O   
13630 C CB  . MET D 61  ? 1.0882 1.0196 0.9815 -0.0748 0.0060  -0.0675 61  MET D CB  
13631 C CG  . MET D 61  ? 1.0728 0.9847 0.9489 -0.0649 0.0134  -0.0601 61  MET D CG  
13632 S SD  . MET D 61  ? 1.0011 0.9193 0.8854 -0.0593 0.0224  -0.0466 61  MET D SD  
13633 C CE  . MET D 61  ? 1.0288 0.9368 0.9197 -0.0691 0.0279  -0.0441 61  MET D CE  
13643 N N   . MET D 62  ? 1.0999 1.0771 1.0392 -0.0915 0.0063  -0.0672 62  MET D N   
13644 C CA  . MET D 62  ? 1.0929 1.0921 1.0550 -0.1013 0.0053  -0.0723 62  MET D CA  
13645 C C   . MET D 62  ? 1.0802 1.0875 1.0535 -0.1106 -0.0026 -0.0880 62  MET D C   
13646 O O   . MET D 62  ? 1.0822 1.1151 1.0766 -0.1150 -0.0077 -0.0960 62  MET D O   
13647 C CB  . MET D 62  ? 1.1381 1.1296 1.1064 -0.1104 0.0177  -0.0650 62  MET D CB  
13648 C CG  . MET D 62  ? 1.1711 1.1312 1.1220 -0.1118 0.0255  -0.0602 62  MET D CG  
13649 S SD  . MET D 62  ? 1.1381 1.0819 1.0906 -0.1237 0.0395  -0.0548 62  MET D SD  
13650 C CE  . MET D 62  ? 1.1734 1.1343 1.1503 -0.1426 0.0402  -0.0686 62  MET D CE  
13660 N N   . GLY D 63  ? 1.0894 1.0761 1.0500 -0.1133 -0.0042 -0.0936 63  GLY D N   
13661 C CA  . GLY D 63  ? 1.1050 1.0978 1.0769 -0.1231 -0.0125 -0.1099 63  GLY D CA  
13662 C C   . GLY D 63  ? 1.1124 1.1008 1.0682 -0.1123 -0.0267 -0.1189 63  GLY D C   
13663 O O   . GLY D 63  ? 1.1020 1.0990 1.0677 -0.1176 -0.0377 -0.1345 63  GLY D O   
13667 N N   . GLY D 64  ? 1.0901 1.0639 1.0207 -0.0970 -0.0263 -0.1098 64  GLY D N   
13668 C CA  . GLY D 64  ? 1.1081 1.0704 1.0160 -0.0851 -0.0371 -0.1166 64  GLY D CA  
13669 C C   . GLY D 64  ? 1.0988 1.0300 0.9856 -0.0856 -0.0335 -0.1171 64  GLY D C   
13670 O O   . GLY D 64  ? 1.1809 1.1017 1.0549 -0.0830 -0.0438 -0.1285 64  GLY D O   
13674 N N   . GLU D 65  ? 1.0832 0.9985 0.9649 -0.0878 -0.0197 -0.1055 65  GLU D N   
13675 C CA  . GLU D 65  ? 1.0971 0.9823 0.9597 -0.0882 -0.0148 -0.1054 65  GLU D CA  
13676 C C   . GLU D 65  ? 1.0607 0.9319 0.9058 -0.0753 -0.0050 -0.0923 65  GLU D C   
13677 O O   . GLU D 65  ? 1.0807 0.9648 0.9334 -0.0706 0.0004  -0.0824 65  GLU D O   
13678 C CB  . GLU D 65  ? 1.0613 0.9372 0.9350 -0.1047 -0.0075 -0.1066 65  GLU D CB  
13679 C CG  . GLU D 65  ? 1.1703 1.0522 1.0568 -0.1093 0.0044  -0.0948 65  GLU D CG  
13680 C CD  . GLU D 65  ? 1.1272 1.0412 1.0361 -0.1105 0.0019  -0.0934 65  GLU D CD  
13681 O OE1 . GLU D 65  ? 1.1762 1.1083 1.0908 -0.1067 -0.0093 -0.1016 65  GLU D OE1 
13682 O OE2 . GLU D 65  ? 1.1100 1.0294 1.0284 -0.1135 0.0106  -0.0845 65  GLU D OE2 
13689 N N   . PHE D 66  ? 1.1057 0.9509 0.9284 -0.0695 -0.0027 -0.0932 66  PHE D N   
13690 C CA  . PHE D 66  ? 1.1144 0.9479 0.9226 -0.0567 0.0069  -0.0831 66  PHE D CA  
13691 C C   . PHE D 66  ? 1.0607 0.8867 0.8753 -0.0600 0.0173  -0.0748 66  PHE D C   
13692 O O   . PHE D 66  ? 1.1021 0.9156 0.9175 -0.0699 0.0182  -0.0779 66  PHE D O   
13693 C CB  . PHE D 66  ? 1.1284 0.9369 0.9087 -0.0473 0.0059  -0.0879 66  PHE D CB  
13694 C CG  . PHE D 66  ? 1.1142 0.9107 0.8824 -0.0351 0.0178  -0.0790 66  PHE D CG  
13695 C CD1 . PHE D 66  ? 1.1199 0.9258 0.8864 -0.0251 0.0231  -0.0726 66  PHE D CD1 
13696 C CD2 . PHE D 66  ? 1.0803 0.8558 0.8393 -0.0338 0.0244  -0.0776 66  PHE D CD2 
13697 C CE1 . PHE D 66  ? 1.1202 0.9182 0.8804 -0.0152 0.0353  -0.0659 66  PHE D CE1 
13698 C CE2 . PHE D 66  ? 1.0994 0.8676 0.8513 -0.0218 0.0351  -0.0710 66  PHE D CE2 
13699 C CZ  . PHE D 66  ? 1.1062 0.8873 0.8609 -0.0132 0.0409  -0.0655 66  PHE D CZ  
13709 N N   . SER D 67  ? 1.0290 0.8617 0.8473 -0.0513 0.0248  -0.0648 67  SER D N   
13710 C CA  . SER D 67  ? 1.0776 0.9022 0.8991 -0.0499 0.0329  -0.0575 67  SER D CA  
13711 C C   . SER D 67  ? 1.0523 0.8745 0.8678 -0.0358 0.0399  -0.0522 67  SER D C   
13712 O O   . SER D 67  ? 1.0715 0.9108 0.8957 -0.0308 0.0419  -0.0478 67  SER D O   
13713 C CB  . SER D 67  ? 1.0669 0.9087 0.9082 -0.0564 0.0340  -0.0518 67  SER D CB  
13714 O OG  . SER D 67  ? 1.0671 0.9012 0.9089 -0.0511 0.0404  -0.0446 67  SER D OG  
13720 N N   . GLY D 68  ? 1.0712 0.8719 0.8723 -0.0294 0.0442  -0.0532 68  GLY D N   
13721 C CA  . GLY D 68  ? 1.0834 0.8842 0.8834 -0.0162 0.0523  -0.0492 68  GLY D CA  
13722 C C   . GLY D 68  ? 1.0789 0.8952 0.8987 -0.0133 0.0559  -0.0422 68  GLY D C   
13723 O O   . GLY D 68  ? 1.0594 0.8879 0.8886 -0.0052 0.0617  -0.0391 68  GLY D O   
13727 N N   . ASN D 69  ? 1.0787 0.8934 0.9045 -0.0198 0.0528  -0.0401 69  ASN D N   
13728 C CA  . ASN D 69  ? 1.0914 0.9190 0.9334 -0.0162 0.0541  -0.0340 69  ASN D CA  
13729 C C   . ASN D 69  ? 1.0629 0.9165 0.9221 -0.0195 0.0527  -0.0306 69  ASN D C   
13730 O O   . ASN D 69  ? 1.0344 0.9025 0.9067 -0.0128 0.0558  -0.0274 69  ASN D O   
13731 C CB  . ASN D 69  ? 1.0754 0.8887 0.9129 -0.0215 0.0520  -0.0325 69  ASN D CB  
13732 C CG  . ASN D 69  ? 1.1414 0.9298 0.9639 -0.0122 0.0541  -0.0334 69  ASN D CG  
13733 O OD1 . ASN D 69  ? 1.1327 0.9255 0.9604 0.0008  0.0561  -0.0326 69  ASN D OD1 
13734 N ND2 . ASN D 69  ? 1.1885 0.9505 0.9927 -0.0189 0.0539  -0.0358 69  ASN D ND2 
13741 N N   . ALA D 70  ? 1.0546 0.9146 0.9146 -0.0298 0.0479  -0.0322 70  ALA D N   
13742 C CA  . ALA D 70  ? 1.0095 0.8920 0.8825 -0.0319 0.0459  -0.0294 70  ALA D CA  
13743 C C   . ALA D 70  ? 0.9983 0.8867 0.8692 -0.0243 0.0499  -0.0293 70  ALA D C   
13744 O O   . ALA D 70  ? 1.0287 0.9315 0.9113 -0.0212 0.0527  -0.0250 70  ALA D O   
13745 C CB  . ALA D 70  ? 0.9902 0.8787 0.8637 -0.0424 0.0396  -0.0333 70  ALA D CB  
13751 N N   . SER D 71  ? 1.0596 0.9346 0.9136 -0.0215 0.0510  -0.0341 71  SER D N   
13752 C CA  . SER D 71  ? 1.0426 0.9176 0.8893 -0.0140 0.0572  -0.0339 71  SER D CA  
13753 C C   . SER D 71  ? 1.0288 0.9088 0.8875 -0.0066 0.0670  -0.0301 71  SER D C   
13754 O O   . SER D 71  ? 0.9935 0.8835 0.8589 -0.0040 0.0732  -0.0274 71  SER D O   
13755 C CB  . SER D 71  ? 1.0684 0.9232 0.8910 -0.0107 0.0570  -0.0400 71  SER D CB  
13756 O OG  . SER D 71  ? 1.0658 0.9198 0.8799 -0.0166 0.0467  -0.0452 71  SER D OG  
13762 N N   . ARG D 72  ? 1.0602 0.9329 0.9221 -0.0030 0.0684  -0.0308 72  ARG D N   
13763 C CA  . ARG D 72  ? 1.0476 0.9291 0.9257 0.0048  0.0756  -0.0292 72  ARG D CA  
13764 C C   . ARG D 72  ? 1.0207 0.9226 0.9212 0.0023  0.0729  -0.0249 72  ARG D C   
13765 O O   . ARG D 72  ? 1.0111 0.9266 0.9286 0.0063  0.0791  -0.0242 72  ARG D O   
13766 C CB  . ARG D 72  ? 1.0707 0.9387 0.9451 0.0111  0.0751  -0.0316 72  ARG D CB  
13767 C CG  . ARG D 72  ? 1.0811 0.9290 0.9350 0.0168  0.0801  -0.0362 72  ARG D CG  
13768 C CD  . ARG D 72  ? 1.0897 0.9191 0.9341 0.0216  0.0770  -0.0385 72  ARG D CD  
13769 N NE  . ARG D 72  ? 1.0913 0.9309 0.9540 0.0291  0.0764  -0.0373 72  ARG D NE  
13770 C CZ  . ARG D 72  ? 1.1136 0.9490 0.9775 0.0275  0.0690  -0.0352 72  ARG D CZ  
13771 N NH1 . ARG D 72  ? 1.1354 0.9575 0.9857 0.0171  0.0635  -0.0338 72  ARG D NH1 
13772 N NH2 . ARG D 72  ? 1.1172 0.9616 0.9963 0.0370  0.0672  -0.0351 72  ARG D NH2 
13786 N N   . ALA D 73  ? 1.0302 0.9342 0.9315 -0.0047 0.0644  -0.0227 73  ALA D N   
13787 C CA  . ALA D 73  ? 0.9897 0.9108 0.9088 -0.0066 0.0612  -0.0186 73  ALA D CA  
13788 C C   . ALA D 73  ? 0.9875 0.9211 0.9106 -0.0095 0.0640  -0.0167 73  ALA D C   
13789 O O   . ALA D 73  ? 0.9707 0.9179 0.9101 -0.0079 0.0666  -0.0147 73  ALA D O   
13790 C CB  . ALA D 73  ? 1.0083 0.9259 0.9241 -0.0131 0.0534  -0.0167 73  ALA D CB  
13796 N N   . PHE D 74  ? 1.0050 0.9326 0.9121 -0.0131 0.0630  -0.0181 74  PHE D N   
13797 C CA  . PHE D 74  ? 1.0180 0.9517 0.9220 -0.0137 0.0658  -0.0165 74  PHE D CA  
13798 C C   . PHE D 74  ? 1.0047 0.9378 0.9118 -0.0084 0.0781  -0.0163 74  PHE D C   
13799 O O   . PHE D 74  ? 1.0242 0.9675 0.9426 -0.0092 0.0826  -0.0136 74  PHE D O   
13800 C CB  . PHE D 74  ? 1.0043 0.9284 0.8870 -0.0155 0.0610  -0.0198 74  PHE D CB  
13801 C CG  . PHE D 74  ? 1.0440 0.9697 0.9170 -0.0142 0.0622  -0.0185 74  PHE D CG  
13802 C CD1 . PHE D 74  ? 1.0341 0.9701 0.9185 -0.0142 0.0665  -0.0138 74  PHE D CD1 
13803 C CD2 . PHE D 74  ? 1.0734 0.9879 0.9236 -0.0120 0.0580  -0.0226 74  PHE D CD2 
13804 C CE1 . PHE D 74  ? 1.0338 0.9664 0.9049 -0.0124 0.0683  -0.0123 74  PHE D CE1 
13805 C CE2 . PHE D 74  ? 1.0656 0.9771 0.9016 -0.0086 0.0585  -0.0215 74  PHE D CE2 
13806 C CZ  . PHE D 74  ? 1.0410 0.9605 0.8865 -0.0089 0.0643  -0.0159 74  PHE D CZ  
13816 N N   . ALA D 75  ? 0.9924 0.9131 0.8898 -0.0035 0.0849  -0.0196 75  ALA D N   
13817 C CA  . ALA D 75  ? 1.0483 0.9685 0.9498 0.0011  0.0993  -0.0201 75  ALA D CA  
13818 C C   . ALA D 75  ? 1.0056 0.9450 0.9384 0.0015  0.1024  -0.0195 75  ALA D C   
13819 O O   . ALA D 75  ? 1.0210 0.9686 0.9654 0.0002  0.1118  -0.0186 75  ALA D O   
13820 C CB  . ALA D 75  ? 1.0248 0.9290 0.9120 0.0074  0.1058  -0.0242 75  ALA D CB  
13826 N N   . SER D 76  ? 1.0029 0.9480 0.9486 0.0036  0.0943  -0.0206 76  SER D N   
13827 C CA  . SER D 76  ? 1.0283 0.9915 1.0031 0.0058  0.0937  -0.0215 76  SER D CA  
13828 C C   . SER D 76  ? 0.9917 0.9673 0.9771 -0.0004 0.0909  -0.0179 76  SER D C   
13829 O O   . SER D 76  ? 0.9990 0.9892 1.0074 -0.0005 0.0958  -0.0194 76  SER D O   
13830 C CB  . SER D 76  ? 0.9962 0.9576 0.9747 0.0103  0.0829  -0.0227 76  SER D CB  
13831 O OG  . SER D 76  ? 1.0018 0.9532 0.9748 0.0180  0.0866  -0.0269 76  SER D OG  
13837 N N   . LEU D 77  ? 0.9825 0.9532 0.9527 -0.0056 0.0830  -0.0140 77  LEU D N   
13838 C CA  . LEU D 77  ? 0.9889 0.9692 0.9655 -0.0104 0.0801  -0.0105 77  LEU D CA  
13839 C C   . LEU D 77  ? 1.0070 0.9856 0.9803 -0.0124 0.0923  -0.0099 77  LEU D C   
13840 O O   . LEU D 77  ? 0.9811 0.9698 0.9704 -0.0150 0.0956  -0.0092 77  LEU D O   
13841 C CB  . LEU D 77  ? 0.9809 0.9569 0.9417 -0.0143 0.0699  -0.0075 77  LEU D CB  
13842 C CG  . LEU D 77  ? 0.9277 0.9115 0.8907 -0.0180 0.0663  -0.0038 77  LEU D CG  
13843 C CD1 . LEU D 77  ? 0.9267 0.9232 0.9127 -0.0173 0.0638  -0.0032 77  LEU D CD1 
13844 C CD2 . LEU D 77  ? 0.8827 0.8651 0.8337 -0.0210 0.0565  -0.0022 77  LEU D CD2 
13856 N N   . LEU D 78  ? 1.0149 0.9780 0.9650 -0.0111 0.0992  -0.0104 78  LEU D N   
13857 C CA  . LEU D 78  ? 1.0064 0.9614 0.9472 -0.0120 0.1131  -0.0095 78  LEU D CA  
13858 C C   . LEU D 78  ? 1.0036 0.9694 0.9708 -0.0124 0.1265  -0.0123 78  LEU D C   
13859 O O   . LEU D 78  ? 1.0210 0.9883 0.9944 -0.0166 0.1365  -0.0113 78  LEU D O   
13860 C CB  . LEU D 78  ? 1.0657 0.9991 0.9751 -0.0080 0.1185  -0.0106 78  LEU D CB  
13861 C CG  . LEU D 78  ? 1.0432 0.9666 0.9269 -0.0074 0.1056  -0.0101 78  LEU D CG  
13862 C CD1 . LEU D 78  ? 1.0754 0.9771 0.9296 -0.0020 0.1094  -0.0131 78  LEU D CD1 
13863 C CD2 . LEU D 78  ? 1.0188 0.9412 0.8929 -0.0094 0.1031  -0.0066 78  LEU D CD2 
13875 N N   . ALA D 79  ? 1.0110 0.9841 0.9946 -0.0079 0.1271  -0.0167 79  ALA D N   
13876 C CA  . ALA D 79  ? 1.0136 1.0023 1.0285 -0.0073 0.1380  -0.0214 79  ALA D CA  
13877 C C   . ALA D 79  ? 0.9900 0.9990 1.0342 -0.0109 0.1299  -0.0223 79  ALA D C   
13878 O O   . ALA D 79  ? 1.0010 1.0218 1.0689 -0.0150 0.1400  -0.0253 79  ALA D O   
13879 C CB  . ALA D 79  ? 1.0415 1.0331 1.0652 0.0008  0.1380  -0.0267 79  ALA D CB  
13885 N N   . PHE D 80  ? 0.9993 1.0115 1.0420 -0.0096 0.1123  -0.0201 80  PHE D N   
13886 C CA  . PHE D 80  ? 0.9596 0.9876 1.0250 -0.0115 0.1027  -0.0207 80  PHE D CA  
13887 C C   . PHE D 80  ? 0.9752 1.0026 1.0388 -0.0195 0.1078  -0.0174 80  PHE D C   
13888 O O   . PHE D 80  ? 1.0047 1.0460 1.0934 -0.0226 0.1075  -0.0203 80  PHE D O   
13889 C CB  . PHE D 80  ? 0.9698 0.9946 1.0248 -0.0085 0.0851  -0.0176 80  PHE D CB  
13890 C CG  . PHE D 80  ? 0.9735 1.0116 1.0491 -0.0069 0.0736  -0.0191 80  PHE D CG  
13891 C CD1 . PHE D 80  ? 0.9804 1.0330 1.0839 -0.0008 0.0712  -0.0265 80  PHE D CD1 
13892 C CD2 . PHE D 80  ? 0.9655 1.0016 1.0319 -0.0102 0.0644  -0.0141 80  PHE D CD2 
13893 C CE1 . PHE D 80  ? 0.9644 1.0274 1.0845 0.0022  0.0586  -0.0289 80  PHE D CE1 
13894 C CE2 . PHE D 80  ? 0.9617 1.0071 1.0434 -0.0077 0.0534  -0.0156 80  PHE D CE2 
13895 C CZ  . PHE D 80  ? 0.9507 1.0087 1.0583 -0.0013 0.0500  -0.0231 80  PHE D CZ  
13905 N N   . ARG D 81  ? 0.9825 0.9927 1.0159 -0.0222 0.1118  -0.0122 81  ARG D N   
13906 C CA  . ARG D 81  ? 0.9693 0.9735 0.9935 -0.0282 0.1158  -0.0084 81  ARG D CA  
13907 C C   . ARG D 81  ? 1.0604 1.0550 1.0813 -0.0321 0.1366  -0.0095 81  ARG D C   
13908 O O   . ARG D 81  ? 1.1070 1.0920 1.1171 -0.0371 0.1423  -0.0064 81  ARG D O   
13909 C CB  . ARG D 81  ? 0.9587 0.9489 0.9503 -0.0270 0.1070  -0.0029 81  ARG D CB  
13910 C CG  . ARG D 81  ? 0.9880 0.9861 0.9820 -0.0248 0.0894  -0.0017 81  ARG D CG  
13911 C CD  . ARG D 81  ? 0.9571 0.9479 0.9278 -0.0251 0.0809  0.0026  81  ARG D CD  
13912 N NE  . ARG D 81  ? 0.9626 0.9637 0.9426 -0.0253 0.0679  0.0043  81  ARG D NE  
13913 C CZ  . ARG D 81  ? 0.9854 0.9855 0.9525 -0.0248 0.0584  0.0064  81  ARG D CZ  
13914 N NH1 . ARG D 81  ? 0.9703 0.9619 0.9167 -0.0239 0.0580  0.0061  81  ARG D NH1 
13915 N NH2 . ARG D 81  ? 0.9593 0.9672 0.9348 -0.0248 0.0491  0.0082  81  ARG D NH2 
13929 N N   . ASP D 82  ? 1.0315 1.0261 1.0595 -0.0298 0.1490  -0.0136 82  ASP D N   
13930 C CA  . ASP D 82  ? 1.0793 1.0635 1.1043 -0.0337 0.1720  -0.0149 82  ASP D CA  
13931 C C   . ASP D 82  ? 1.0818 1.0882 1.1506 -0.0398 0.1805  -0.0214 82  ASP D C   
13932 O O   . ASP D 82  ? 1.0601 1.0871 1.1599 -0.0362 0.1783  -0.0282 82  ASP D O   
13933 C CB  . ASP D 82  ? 1.1182 1.0906 1.1277 -0.0275 0.1822  -0.0164 82  ASP D CB  
13934 C CG  . ASP D 82  ? 1.1194 1.0733 1.1146 -0.0306 0.2075  -0.0162 82  ASP D CG  
13935 O OD1 . ASP D 82  ? 1.1673 1.1222 1.1744 -0.0389 0.2195  -0.0164 82  ASP D OD1 
13936 O OD2 . ASP D 82  ? 1.1549 1.0908 1.1252 -0.0247 0.2161  -0.0160 82  ASP D OD2 
13941 N N   . LYS D 83  ? 1.1162 1.1181 1.1876 -0.0487 0.1897  -0.0203 83  LYS D N   
13942 C CA  . LYS D 83  ? 1.1232 1.1465 1.2385 -0.0565 0.1984  -0.0280 83  LYS D CA  
13943 C C   . LYS D 83  ? 1.1438 1.1736 1.2793 -0.0575 0.2203  -0.0348 83  LYS D C   
13944 O O   . LYS D 83  ? 1.1260 1.1827 1.3077 -0.0609 0.2239  -0.0443 83  LYS D O   
13945 C CB  . LYS D 83  ? 1.1291 1.1402 1.2377 -0.0671 0.2065  -0.0252 83  LYS D CB  
13946 C CG  . LYS D 83  ? 1.2012 1.1833 1.2819 -0.0726 0.2332  -0.0218 83  LYS D CG  
13947 C CD  . LYS D 83  ? 1.1853 1.1540 1.2613 -0.0839 0.2422  -0.0199 83  LYS D CD  
13948 C CE  . LYS D 83  ? 1.1737 1.1275 1.2167 -0.0801 0.2230  -0.0120 83  LYS D CE  
13949 N NZ  . LYS D 83  ? 1.1657 1.0808 1.1519 -0.0755 0.2309  -0.0037 83  LYS D NZ  
13963 N N   . ASP D 84  ? 1.2225 1.2286 1.3248 -0.0537 0.2347  -0.0309 84  ASP D N   
13964 C CA  . ASP D 84  ? 1.2250 1.2323 1.3403 -0.0544 0.2591  -0.0364 84  ASP D CA  
13965 C C   . ASP D 84  ? 1.1598 1.1811 1.2869 -0.0431 0.2527  -0.0412 84  ASP D C   
13966 O O   . ASP D 84  ? 1.1850 1.2118 1.3280 -0.0421 0.2718  -0.0471 84  ASP D O   
13967 C CB  . ASP D 84  ? 1.2358 1.2042 1.3032 -0.0556 0.2805  -0.0296 84  ASP D CB  
13968 C CG  . ASP D 84  ? 1.3096 1.2612 1.3675 -0.0673 0.2943  -0.0264 84  ASP D CG  
13969 O OD1 . ASP D 84  ? 1.2758 1.2481 1.3758 -0.0780 0.3029  -0.0330 84  ASP D OD1 
13970 O OD2 . ASP D 84  ? 1.4266 1.3436 1.4345 -0.0655 0.2958  -0.0180 84  ASP D OD2 
13975 N N   . PHE D 85  ? 1.1155 1.1406 1.2338 -0.0346 0.2278  -0.0390 85  PHE D N   
13976 C CA  . PHE D 85  ? 1.1305 1.1672 1.2600 -0.0237 0.2205  -0.0440 85  PHE D CA  
13977 C C   . PHE D 85  ? 1.1449 1.2160 1.3293 -0.0234 0.2234  -0.0555 85  PHE D C   
13978 O O   . PHE D 85  ? 1.1374 1.2288 1.3530 -0.0287 0.2150  -0.0596 85  PHE D O   
13979 C CB  . PHE D 85  ? 1.0988 1.1334 1.2124 -0.0169 0.1936  -0.0400 85  PHE D CB  
13980 C CG  . PHE D 85  ? 1.0924 1.1295 1.2060 -0.0054 0.1864  -0.0435 85  PHE D CG  
13981 C CD1 . PHE D 85  ? 1.1110 1.1736 1.2630 0.0008  0.1811  -0.0525 85  PHE D CD1 
13982 C CD2 . PHE D 85  ? 1.0939 1.1067 1.1682 -0.0001 0.1838  -0.0388 85  PHE D CD2 
13983 C CE1 . PHE D 85  ? 1.1414 1.2027 1.2895 0.0126  0.1744  -0.0557 85  PHE D CE1 
13984 C CE2 . PHE D 85  ? 1.0688 1.0805 1.1406 0.0100  0.1776  -0.0421 85  PHE D CE2 
13985 C CZ  . PHE D 85  ? 1.1063 1.1410 1.2135 0.0167  0.1733  -0.0501 85  PHE D CZ  
13995 N N   . SER D 86  ? 1.1231 1.2010 1.3197 -0.0161 0.2345  -0.0618 86  SER D N   
13996 C CA  . SER D 86  ? 1.1443 1.2571 1.3950 -0.0134 0.2372  -0.0748 86  SER D CA  
13997 C C   . SER D 86  ? 1.1902 1.3115 1.4450 0.0026  0.2208  -0.0793 86  SER D C   
13998 O O   . SER D 86  ? 1.2049 1.3398 1.4734 0.0084  0.1975  -0.0819 86  SER D O   
13999 C CB  . SER D 86  ? 1.1173 1.2341 1.3859 -0.0192 0.2691  -0.0805 86  SER D CB  
14000 O OG  . SER D 86  ? 1.1048 1.2591 1.4297 -0.0157 0.2717  -0.0949 86  SER D OG  
14006 N N   . LYS D 87  ? 1.1136 1.2239 1.3534 0.0105  0.2332  -0.0802 87  LYS D N   
14007 C CA  . LYS D 87  ? 1.0608 1.1728 1.2975 0.0263  0.2198  -0.0839 87  LYS D CA  
14008 C C   . LYS D 87  ? 1.0691 1.1454 1.2516 0.0315  0.2174  -0.0748 87  LYS D C   
14009 O O   . LYS D 87  ? 1.0811 1.1502 1.2490 0.0412  0.1987  -0.0739 87  LYS D O   
14010 C CB  . LYS D 87  ? 1.0622 1.1977 1.3365 0.0342  0.2350  -0.0964 87  LYS D CB  
14011 C CG  . LYS D 87  ? 1.0645 1.2389 1.3989 0.0280  0.2407  -0.1084 87  LYS D CG  
14012 C CD  . LYS D 87  ? 1.0323 1.2234 1.3976 0.0281  0.2691  -0.1183 87  LYS D CD  
14013 C CE  . LYS D 87  ? 1.0405 1.2599 1.4555 0.0131  0.2843  -0.1268 87  LYS D CE  
14014 N NZ  . LYS D 87  ? 1.0442 1.2377 1.4310 -0.0046 0.3001  -0.1158 87  LYS D NZ  
14028 N N   . GLN D 88  ? 1.0907 1.1426 1.2418 0.0257  0.2356  -0.0685 88  GLN D N   
14029 C CA  . GLN D 88  ? 1.0626 1.0801 1.1621 0.0302  0.2329  -0.0612 88  GLN D CA  
14030 C C   . GLN D 88  ? 1.0620 1.0554 1.1283 0.0202  0.2423  -0.0527 88  GLN D C   
14031 O O   . GLN D 88  ? 1.0487 1.0462 1.1274 0.0115  0.2602  -0.0530 88  GLN D O   
14032 C CB  . GLN D 88  ? 1.0688 1.0770 1.1593 0.0409  0.2476  -0.0657 88  GLN D CB  
14033 C CG  . GLN D 88  ? 1.0771 1.0490 1.1144 0.0467  0.2429  -0.0598 88  GLN D CG  
14034 C CD  . GLN D 88  ? 1.1183 1.0608 1.1163 0.0408  0.2578  -0.0531 88  GLN D CD  
14035 O OE1 . GLN D 88  ? 1.1745 1.1198 1.1796 0.0312  0.2701  -0.0509 88  GLN D OE1 
14036 N NE2 . GLN D 88  ? 1.1303 1.0419 1.0841 0.0473  0.2558  -0.0504 88  GLN D NE2 
14045 N N   . LYS D 89  ? 1.0731 1.0400 1.0960 0.0220  0.2303  -0.0459 89  LYS D N   
14046 C CA  . LYS D 89  ? 1.0839 1.0238 1.0681 0.0165  0.2370  -0.0389 89  LYS D CA  
14047 C C   . LYS D 89  ? 1.0983 1.0137 1.0409 0.0218  0.2209  -0.0351 89  LYS D C   
14048 O O   . LYS D 89  ? 1.0837 1.0066 1.0310 0.0231  0.2002  -0.0351 89  LYS D O   
14049 C CB  . LYS D 89  ? 1.0928 1.0410 1.0870 0.0058  0.2326  -0.0349 89  LYS D CB  
14050 C CG  . LYS D 89  ? 1.0873 1.0060 1.0402 0.0019  0.2403  -0.0282 89  LYS D CG  
14051 C CD  . LYS D 89  ? 1.1090 1.0354 1.0745 -0.0085 0.2410  -0.0253 89  LYS D CD  
14052 C CE  . LYS D 89  ? 1.1228 1.0339 1.0804 -0.0142 0.2689  -0.0244 89  LYS D CE  
14053 N NZ  . LYS D 89  ? 1.0940 0.9955 1.0399 -0.0223 0.2684  -0.0192 89  LYS D NZ  
14067 N N   . ASN D 90  ? 1.1310 1.0162 1.0327 0.0248  0.2308  -0.0327 90  ASN D N   
14068 C CA  . ASN D 90  ? 1.1358 0.9973 0.9979 0.0292  0.2155  -0.0308 90  ASN D CA  
14069 C C   . ASN D 90  ? 1.1151 0.9683 0.9575 0.0234  0.2048  -0.0256 90  ASN D C   
14070 O O   . ASN D 90  ? 1.1306 0.9782 0.9676 0.0191  0.2168  -0.0225 90  ASN D O   
14071 C CB  . ASN D 90  ? 1.1471 0.9783 0.9721 0.0378  0.2292  -0.0321 90  ASN D CB  
14072 C CG  . ASN D 90  ? 1.1859 1.0221 1.0236 0.0460  0.2344  -0.0376 90  ASN D CG  
14073 O OD1 . ASN D 90  ? 1.2513 1.0956 1.1077 0.0483  0.2550  -0.0405 90  ASN D OD1 
14074 N ND2 . ASN D 90  ? 1.1923 1.0230 1.0199 0.0504  0.2164  -0.0395 90  ASN D ND2 
14081 N N   . TYR D 91  ? 1.1136 0.9655 0.9455 0.0232  0.1829  -0.0252 91  TYR D N   
14082 C CA  . TYR D 91  ? 1.1404 0.9882 0.9569 0.0189  0.1701  -0.0218 91  TYR D CA  
14083 C C   . TYR D 91  ? 1.1596 0.9859 0.9401 0.0238  0.1570  -0.0238 91  TYR D C   
14084 O O   . TYR D 91  ? 1.1825 1.0096 0.9648 0.0253  0.1465  -0.0273 91  TYR D O   
14085 C CB  . TYR D 91  ? 1.0969 0.9715 0.9451 0.0120  0.1552  -0.0203 91  TYR D CB  
14086 C CG  . TYR D 91  ? 1.0819 0.9773 0.9641 0.0069  0.1651  -0.0191 91  TYR D CG  
14087 C CD1 . TYR D 91  ? 1.0651 0.9788 0.9803 0.0083  0.1705  -0.0229 91  TYR D CD1 
14088 C CD2 . TYR D 91  ? 1.0601 0.9562 0.9413 0.0014  0.1681  -0.0153 91  TYR D CD2 
14089 C CE1 . TYR D 91  ? 1.0585 0.9932 1.0079 0.0035  0.1782  -0.0238 91  TYR D CE1 
14090 C CE2 . TYR D 91  ? 1.0348 0.9492 0.9480 -0.0043 0.1768  -0.0153 91  TYR D CE2 
14091 C CZ  . TYR D 91  ? 1.0585 0.9933 1.0072 -0.0037 0.1814  -0.0201 91  TYR D CZ  
14092 O OH  . TYR D 91  ? 1.0644 1.0194 1.0480 -0.0095 0.1885  -0.0220 91  TYR D OH  
14102 N N   . ASN D 92  ? 1.1354 0.9411 0.8823 0.0265  0.1572  -0.0225 92  ASN D N   
14103 C CA  . ASN D 92  ? 1.1873 0.9736 0.9004 0.0318  0.1425  -0.0262 92  ASN D CA  
14104 C C   . ASN D 92  ? 1.1745 0.9764 0.8965 0.0264  0.1219  -0.0264 92  ASN D C   
14105 O O   . ASN D 92  ? 1.1975 1.0043 0.9203 0.0242  0.1215  -0.0228 92  ASN D O   
14106 C CB  . ASN D 92  ? 1.2467 0.9997 0.9149 0.0406  0.1525  -0.0260 92  ASN D CB  
14107 C CG  . ASN D 92  ? 1.2387 0.9704 0.8888 0.0480  0.1691  -0.0279 92  ASN D CG  
14108 O OD1 . ASN D 92  ? 1.2333 0.9566 0.8731 0.0524  0.1610  -0.0328 92  ASN D OD1 
14109 N ND2 . ASN D 92  ? 1.2798 1.0022 0.9267 0.0490  0.1935  -0.0244 92  ASN D ND2 
14116 N N   . ILE D 93  ? 1.1853 0.9943 0.9144 0.0240  0.1059  -0.0308 93  ILE D N   
14117 C CA  . ILE D 93  ? 1.1827 1.0080 0.9231 0.0181  0.0877  -0.0320 93  ILE D CA  
14118 C C   . ILE D 93  ? 1.1722 0.9856 0.8920 0.0205  0.0725  -0.0400 93  ILE D C   
14119 O O   . ILE D 93  ? 1.1876 0.9797 0.8846 0.0267  0.0752  -0.0440 93  ILE D O   
14120 C CB  . ILE D 93  ? 1.1494 1.0003 0.9280 0.0095  0.0840  -0.0297 93  ILE D CB  
14121 C CG1 . ILE D 93  ? 1.1306 0.9784 0.9134 0.0079  0.0785  -0.0342 93  ILE D CG1 
14122 C CG2 . ILE D 93  ? 1.1374 0.9989 0.9379 0.0085  0.0989  -0.0244 93  ILE D CG2 
14123 C CD1 . ILE D 93  ? 1.1112 0.9783 0.9241 0.0005  0.0733  -0.0321 93  ILE D CD1 
14135 N N   . THR D 94  ? 1.1594 0.9874 0.8888 0.0155  0.0565  -0.0430 94  THR D N   
14136 C CA  . THR D 94  ? 1.1352 0.9591 0.8551 0.0149  0.0402  -0.0523 94  THR D CA  
14137 C C   . THR D 94  ? 1.1502 0.9982 0.9021 0.0031  0.0308  -0.0536 94  THR D C   
14138 O O   . THR D 94  ? 1.0515 0.9182 0.8268 -0.0022 0.0338  -0.0473 94  THR D O   
14139 C CB  . THR D 94  ? 1.1560 0.9711 0.8498 0.0228  0.0292  -0.0575 94  THR D CB  
14140 O OG1 . THR D 94  ? 1.1265 0.9624 0.8365 0.0198  0.0240  -0.0545 94  THR D OG1 
14141 C CG2 . THR D 94  ? 1.2103 0.9965 0.8672 0.0351  0.0410  -0.0549 94  THR D CG2 
14149 N N   . CYS D 95  ? 1.1517 0.9969 0.9033 -0.0013 0.0199  -0.0621 95  CYS D N   
14150 C CA  . CYS D 95  ? 1.0683 0.9320 0.8474 -0.0136 0.0131  -0.0641 95  CYS D CA  
14151 C C   . CYS D 95  ? 1.0932 0.9568 0.8690 -0.0175 -0.0022 -0.0766 95  CYS D C   
14152 O O   . CYS D 95  ? 1.1400 0.9836 0.8939 -0.0128 -0.0062 -0.0837 95  CYS D O   
14153 C CB  . CYS D 95  ? 1.1233 0.9822 0.9136 -0.0186 0.0220  -0.0601 95  CYS D CB  
14154 S SG  . CYS D 95  ? 1.1467 1.0184 0.9624 -0.0338 0.0159  -0.0629 95  CYS D SG  
14160 N N   . SER D 96  ? 1.0941 0.9804 0.8929 -0.0263 -0.0105 -0.0800 96  SER D N   
14161 C CA  . SER D 96  ? 1.1083 1.0005 0.9122 -0.0319 -0.0252 -0.0936 96  SER D CA  
14162 C C   . SER D 96  ? 1.1459 1.0206 0.9456 -0.0388 -0.0249 -0.0995 96  SER D C   
14163 O O   . SER D 96  ? 1.1459 1.0144 0.9532 -0.0453 -0.0145 -0.0931 96  SER D O   
14164 C CB  . SER D 96  ? 1.0635 0.9847 0.8991 -0.0428 -0.0295 -0.0953 96  SER D CB  
14165 O OG  . SER D 96  ? 1.0436 0.9676 0.8966 -0.0526 -0.0180 -0.0868 96  SER D OG  
14171 N N   . GLY D 97  ? 1.1244 0.9893 0.9101 -0.0366 -0.0373 -0.1124 97  GLY D N   
14172 C CA  . GLY D 97  ? 1.1466 0.9916 0.9246 -0.0425 -0.0385 -0.1195 97  GLY D CA  
14173 C C   . GLY D 97  ? 1.1929 1.0068 0.9382 -0.0308 -0.0313 -0.1158 97  GLY D C   
14174 O O   . GLY D 97  ? 1.2023 0.9961 0.9378 -0.0345 -0.0312 -0.1207 97  GLY D O   
14178 N N   . GLU D 98  ? 1.2090 1.0170 0.9365 -0.0172 -0.0241 -0.1075 98  GLU D N   
14179 C CA  . GLU D 98  ? 1.2785 1.0577 0.9744 -0.0050 -0.0151 -0.1041 98  GLU D CA  
14180 C C   . GLU D 98  ? 1.2578 1.0278 0.9259 0.0099  -0.0185 -0.1053 98  GLU D C   
14181 O O   . GLU D 98  ? 1.2035 0.9863 0.8766 0.0134  -0.0143 -0.0981 98  GLU D O   
14182 C CB  . GLU D 98  ? 1.2739 1.0530 0.9783 -0.0043 0.0035  -0.0909 98  GLU D CB  
14183 C CG  . GLU D 98  ? 1.3528 1.1056 1.0290 0.0082  0.0153  -0.0877 98  GLU D CG  
14184 C CD  . GLU D 98  ? 1.4122 1.1397 1.0689 0.0090  0.0108  -0.0962 98  GLU D CD  
14185 O OE1 . GLU D 98  ? 1.3740 1.1049 1.0452 -0.0028 0.0030  -0.1018 98  GLU D OE1 
14186 O OE2 . GLU D 98  ? 1.4406 1.1430 1.0663 0.0212  0.0160  -0.0972 98  GLU D OE2 
14193 N N   . SER D 99  ? 1.3329 1.0774 0.9684 0.0192  -0.0262 -0.1143 99  SER D N   
14194 C CA  . SER D 99  ? 1.3802 1.1102 0.9826 0.0348  -0.0320 -0.1172 99  SER D CA  
14195 C C   . SER D 99  ? 1.3866 1.0945 0.9615 0.0471  -0.0124 -0.1060 99  SER D C   
14196 O O   . SER D 99  ? 1.3813 1.0802 0.9329 0.0583  -0.0118 -0.1040 99  SER D O   
14197 C CB  . SER D 99  ? 1.3551 1.0642 0.9307 0.0412  -0.0496 -0.1326 99  SER D CB  
14198 O OG  . SER D 99  ? 1.3574 1.0380 0.9114 0.0444  -0.0412 -0.1324 99  SER D OG  
14204 N N   . LYS D 100 ? 1.4485 1.1469 1.0252 0.0455  0.0039  -0.0994 100 LYS D N   
14205 C CA  . LYS D 100 ? 1.4112 1.0909 0.9666 0.0559  0.0247  -0.0902 100 LYS D CA  
14206 C C   . LYS D 100 ? 1.3836 1.0872 0.9696 0.0496  0.0395  -0.0782 100 LYS D C   
14207 O O   . LYS D 100 ? 1.4203 1.1496 1.0431 0.0376  0.0376  -0.0757 100 LYS D O   
14208 C CB  . LYS D 100 ? 1.5486 1.2063 1.0905 0.0593  0.0344  -0.0909 100 LYS D CB  
14209 C CG  . LYS D 100 ? 1.6809 1.3009 1.1740 0.0736  0.0305  -0.0984 100 LYS D CG  
14210 C CD  . LYS D 100 ? 1.6708 1.2707 1.1532 0.0754  0.0355  -0.1015 100 LYS D CD  
14211 C CE  . LYS D 100 ? 1.7947 1.3539 1.2247 0.0915  0.0347  -0.1075 100 LYS D CE  
14212 N NZ  . LYS D 100 ? 1.9009 1.4415 1.3075 0.1034  0.0596  -0.0983 100 LYS D NZ  
14226 N N   . VAL D 101 ? 1.3266 1.0191 0.8953 0.0579  0.0549  -0.0711 101 VAL D N   
14227 C CA  . VAL D 101 ? 1.3333 1.0461 0.9297 0.0524  0.0699  -0.0608 101 VAL D CA  
14228 C C   . VAL D 101 ? 1.3181 1.0398 0.9397 0.0475  0.0824  -0.0571 101 VAL D C   
14229 O O   . VAL D 101 ? 1.3696 1.0714 0.9743 0.0539  0.0906  -0.0591 101 VAL D O   
14230 C CB  . VAL D 101 ? 1.3111 1.0052 0.8805 0.0616  0.0857  -0.0550 101 VAL D CB  
14231 C CG1 . VAL D 101 ? 1.2934 1.0063 0.8930 0.0551  0.1042  -0.0456 101 VAL D CG1 
14232 C CG2 . VAL D 101 ? 1.2079 0.8959 0.7549 0.0670  0.0718  -0.0579 101 VAL D CG2 
14242 N N   . LEU D 102 ? 1.2502 1.0006 0.9107 0.0378  0.0832  -0.0523 102 LEU D N   
14243 C CA  . LEU D 102 ? 1.2529 1.0138 0.9389 0.0342  0.0913  -0.0498 102 LEU D CA  
14244 C C   . LEU D 102 ? 1.2484 1.0189 0.9504 0.0358  0.1106  -0.0429 102 LEU D C   
14245 O O   . LEU D 102 ? 1.2377 1.0294 0.9635 0.0299  0.1110  -0.0382 102 LEU D O   
14246 C CB  . LEU D 102 ? 1.2470 1.0300 0.9630 0.0233  0.0786  -0.0502 102 LEU D CB  
14247 C CG  . LEU D 102 ? 1.2878 1.0638 0.9954 0.0187  0.0616  -0.0582 102 LEU D CG  
14248 C CD1 . LEU D 102 ? 1.2013 1.0008 0.9340 0.0075  0.0498  -0.0581 102 LEU D CD1 
14249 C CD2 . LEU D 102 ? 1.2643 1.0265 0.9689 0.0191  0.0631  -0.0613 102 LEU D CD2 
14261 N N   . ASP D 103 ? 1.2558 1.0110 0.9455 0.0437  0.1269  -0.0429 103 ASP D N   
14262 C CA  . ASP D 103 ? 1.2686 1.0359 0.9801 0.0442  0.1465  -0.0385 103 ASP D CA  
14263 C C   . ASP D 103 ? 1.2414 1.0306 0.9890 0.0412  0.1448  -0.0388 103 ASP D C   
14264 O O   . ASP D 103 ? 1.2966 1.0767 1.0389 0.0454  0.1419  -0.0427 103 ASP D O   
14265 C CB  . ASP D 103 ? 1.2596 1.0029 0.9455 0.0539  0.1662  -0.0392 103 ASP D CB  
14266 C CG  . ASP D 103 ? 1.2957 1.0520 1.0046 0.0528  0.1887  -0.0355 103 ASP D CG  
14267 O OD1 . ASP D 103 ? 1.2803 1.0614 1.0273 0.0502  0.1918  -0.0360 103 ASP D OD1 
14268 O OD2 . ASP D 103 ? 1.3028 1.0437 0.9915 0.0546  0.2032  -0.0328 103 ASP D OD2 
14273 N N   . VAL D 104 ? 1.2029 1.0184 0.9844 0.0351  0.1459  -0.0353 104 VAL D N   
14274 C CA  . VAL D 104 ? 1.1685 1.0045 0.9828 0.0334  0.1413  -0.0358 104 VAL D CA  
14275 C C   . VAL D 104 ? 1.1285 0.9815 0.9710 0.0358  0.1579  -0.0356 104 VAL D C   
14276 O O   . VAL D 104 ? 1.1239 0.9850 0.9750 0.0319  0.1675  -0.0328 104 VAL D O   
14277 C CB  . VAL D 104 ? 1.1708 1.0237 1.0019 0.0246  0.1255  -0.0332 104 VAL D CB  
14278 C CG1 . VAL D 104 ? 1.1288 0.9909 0.9793 0.0250  0.1173  -0.0345 104 VAL D CG1 
14279 C CG2 . VAL D 104 ? 1.1839 1.0249 0.9909 0.0206  0.1122  -0.0339 104 VAL D CG2 
14289 N N   . ASP D 105 ? 1.1352 0.9939 0.9930 0.0423  0.1607  -0.0393 105 ASP D N   
14290 C CA  . ASP D 105 ? 1.1280 1.0064 1.0176 0.0458  0.1754  -0.0418 105 ASP D CA  
14291 C C   . ASP D 105 ? 1.1146 1.0195 1.0400 0.0434  0.1639  -0.0423 105 ASP D C   
14292 O O   . ASP D 105 ? 1.1328 1.0394 1.0647 0.0494  0.1544  -0.0452 105 ASP D O   
14293 C CB  . ASP D 105 ? 1.1365 1.0051 1.0201 0.0571  0.1855  -0.0470 105 ASP D CB  
14294 C CG  . ASP D 105 ? 1.1465 1.0381 1.0660 0.0612  0.2024  -0.0513 105 ASP D CG  
14295 O OD1 . ASP D 105 ? 1.1307 1.0486 1.0848 0.0556  0.2015  -0.0515 105 ASP D OD1 
14296 O OD2 . ASP D 105 ? 1.1857 1.0696 1.0998 0.0702  0.2166  -0.0554 105 ASP D OD2 
14301 N N   . VAL D 106 ? 1.1115 1.0340 1.0572 0.0356  0.1647  -0.0397 106 VAL D N   
14302 C CA  . VAL D 106 ? 1.0847 1.0312 1.0627 0.0337  0.1536  -0.0404 106 VAL D CA  
14303 C C   . VAL D 106 ? 1.0826 1.0528 1.0986 0.0378  0.1652  -0.0466 106 VAL D C   
14304 O O   . VAL D 106 ? 1.0642 1.0382 1.0880 0.0351  0.1837  -0.0478 106 VAL D O   
14305 C CB  . VAL D 106 ? 1.0786 1.0310 1.0578 0.0234  0.1467  -0.0349 106 VAL D CB  
14306 C CG1 . VAL D 106 ? 1.1072 1.0853 1.1224 0.0220  0.1391  -0.0365 106 VAL D CG1 
14307 C CG2 . VAL D 106 ? 1.0787 1.0148 1.0295 0.0201  0.1319  -0.0308 106 VAL D CG2 
14317 N N   . ARG D 107 ? 1.1154 1.1012 1.1551 0.0447  0.1543  -0.0513 107 ARG D N   
14318 C CA  . ARG D 107 ? 1.0886 1.1019 1.1702 0.0497  0.1610  -0.0594 107 ARG D CA  
14319 C C   . ARG D 107 ? 1.0904 1.1224 1.1967 0.0505  0.1431  -0.0613 107 ARG D C   
14320 O O   . ARG D 107 ? 1.0625 1.0826 1.1502 0.0508  0.1264  -0.0567 107 ARG D O   
14321 C CB  . ARG D 107 ? 1.0772 1.0891 1.1616 0.0635  0.1663  -0.0665 107 ARG D CB  
14322 C CG  . ARG D 107 ? 1.1027 1.0911 1.1566 0.0650  0.1825  -0.0648 107 ARG D CG  
14323 C CD  . ARG D 107 ? 1.0772 1.0544 1.1200 0.0797  0.1803  -0.0697 107 ARG D CD  
14324 N NE  . ARG D 107 ? 1.1013 1.0581 1.1167 0.0821  0.1604  -0.0661 107 ARG D NE  
14325 C CZ  . ARG D 107 ? 1.1265 1.0544 1.1021 0.0773  0.1565  -0.0602 107 ARG D CZ  
14326 N NH1 . ARG D 107 ? 1.1987 1.1126 1.1530 0.0721  0.1690  -0.0573 107 ARG D NH1 
14327 N NH2 . ARG D 107 ? 1.1374 1.0491 1.0936 0.0780  0.1397  -0.0580 107 ARG D NH2 
14341 N N   . ASN D 108 ? 1.0745 1.1356 1.2230 0.0509  0.1471  -0.0687 108 ASN D N   
14342 C CA  . ASN D 108 ? 1.0787 1.1581 1.2518 0.0536  0.1294  -0.0723 108 ASN D CA  
14343 C C   . ASN D 108 ? 1.0969 1.1756 1.2714 0.0704  0.1155  -0.0783 108 ASN D C   
14344 O O   . ASN D 108 ? 1.0916 1.1715 1.2706 0.0805  0.1231  -0.0844 108 ASN D O   
14345 C CB  . ASN D 108 ? 1.0735 1.1846 1.2933 0.0485  0.1371  -0.0803 108 ASN D CB  
14346 C CG  . ASN D 108 ? 1.1093 1.2348 1.3478 0.0476  0.1182  -0.0820 108 ASN D CG  
14347 O OD1 . ASN D 108 ? 1.0810 1.2296 1.3536 0.0566  0.1089  -0.0926 108 ASN D OD1 
14348 N ND2 . ASN D 108 ? 1.0635 1.1750 1.2790 0.0381  0.1117  -0.0722 108 ASN D ND2 
14355 N N   . ASP D 109 ? 1.0921 1.1663 1.2599 0.0743  0.0954  -0.0764 109 ASP D N   
14356 C CA  . ASP D 109 ? 1.1229 1.1883 1.2824 0.0910  0.0805  -0.0806 109 ASP D CA  
14357 C C   . ASP D 109 ? 1.1150 1.1980 1.2990 0.0977  0.0631  -0.0864 109 ASP D C   
14358 O O   . ASP D 109 ? 1.1327 1.1992 1.2950 0.0996  0.0480  -0.0813 109 ASP D O   
14359 C CB  . ASP D 109 ? 1.1387 1.1678 1.2504 0.0902  0.0740  -0.0711 109 ASP D CB  
14360 C CG  . ASP D 109 ? 1.1394 1.1517 1.2352 0.1074  0.0620  -0.0749 109 ASP D CG  
14361 O OD1 . ASP D 109 ? 1.1367 1.1644 1.2555 0.1219  0.0610  -0.0852 109 ASP D OD1 
14362 O OD2 . ASP D 109 ? 1.1391 1.1221 1.1993 0.1066  0.0541  -0.0680 109 ASP D OD2 
14367 N N   . GLY D 110 ? 1.0963 1.2125 1.3259 0.1011  0.0657  -0.0979 110 GLY D N   
14368 C CA  . GLY D 110 ? 1.1035 1.2386 1.3597 0.1097  0.0476  -0.1064 110 GLY D CA  
14369 C C   . GLY D 110 ? 1.1064 1.2567 1.3817 0.0954  0.0462  -0.1047 110 GLY D C   
14370 O O   . GLY D 110 ? 1.1299 1.3118 1.4499 0.0924  0.0500  -0.1150 110 GLY D O   
14374 N N   . ALA D 111 ? 1.1316 1.2598 1.3745 0.0864  0.0410  -0.0925 111 ALA D N   
14375 C CA  . ALA D 111 ? 1.1140 1.2511 1.3675 0.0741  0.0379  -0.0895 111 ALA D CA  
14376 C C   . ALA D 111 ? 1.1095 1.2347 1.3432 0.0561  0.0543  -0.0782 111 ALA D C   
14377 O O   . ALA D 111 ? 1.1044 1.2143 1.3159 0.0537  0.0665  -0.0730 111 ALA D O   
14378 C CB  . ALA D 111 ? 1.1340 1.2559 1.3664 0.0810  0.0167  -0.0857 111 ALA D CB  
14384 N N   . LYS D 112 ? 1.0546 1.1850 1.2942 0.0447  0.0533  -0.0748 112 LYS D N   
14385 C CA  . LYS D 112 ? 1.0321 1.1514 1.2532 0.0294  0.0677  -0.0651 112 LYS D CA  
14386 C C   . LYS D 112 ? 1.0353 1.1264 1.2115 0.0281  0.0631  -0.0534 112 LYS D C   
14387 O O   . LYS D 112 ? 1.0530 1.1313 1.2080 0.0197  0.0748  -0.0467 112 LYS D O   
14388 C CB  . LYS D 112 ? 1.0598 1.1903 1.2977 0.0183  0.0676  -0.0650 112 LYS D CB  
14389 C CG  . LYS D 112 ? 1.1171 1.2761 1.4009 0.0211  0.0615  -0.0781 112 LYS D CG  
14390 C CD  . LYS D 112 ? 1.1370 1.3173 1.4558 0.0230  0.0756  -0.0894 112 LYS D CD  
14391 C CE  . LYS D 112 ? 1.1711 1.3771 1.5286 0.0361  0.0601  -0.1044 112 LYS D CE  
14392 N NZ  . LYS D 112 ? 1.1687 1.3961 1.5592 0.0415  0.0725  -0.1161 112 LYS D NZ  
14406 N N   . ASN D 113 ? 1.0510 1.1313 1.2119 0.0362  0.0465  -0.0514 113 ASN D N   
14407 C CA  . ASN D 113 ? 1.0385 1.0938 1.1609 0.0336  0.0430  -0.0415 113 ASN D CA  
14408 C C   . ASN D 113 ? 1.0528 1.0908 1.1543 0.0401  0.0456  -0.0411 113 ASN D C   
14409 O O   . ASN D 113 ? 1.0317 1.0497 1.1035 0.0356  0.0456  -0.0341 113 ASN D O   
14410 C CB  . ASN D 113 ? 1.0158 1.0638 1.1283 0.0380  0.0266  -0.0388 113 ASN D CB  
14411 C CG  . ASN D 113 ? 1.0612 1.1075 1.1785 0.0541  0.0141  -0.0457 113 ASN D CG  
14412 O OD1 . ASN D 113 ? 1.0937 1.1599 1.2417 0.0614  0.0115  -0.0557 113 ASN D OD1 
14413 N ND2 . ASN D 113 ? 1.0784 1.1001 1.1653 0.0601  0.0065  -0.0411 113 ASN D ND2 
14420 N N   . LYS D 114 ? 1.0869 1.1323 1.2039 0.0504  0.0475  -0.0493 114 LYS D N   
14421 C CA  . LYS D 114 ? 1.0845 1.1115 1.1807 0.0584  0.0492  -0.0498 114 LYS D CA  
14422 C C   . LYS D 114 ? 1.0752 1.1053 1.1747 0.0549  0.0664  -0.0516 114 LYS D C   
14423 O O   . LYS D 114 ? 1.0943 1.1459 1.2230 0.0531  0.0763  -0.0571 114 LYS D O   
14424 C CB  . LYS D 114 ? 1.0933 1.1222 1.1989 0.0760  0.0378  -0.0580 114 LYS D CB  
14425 C CG  . LYS D 114 ? 1.0730 1.0908 1.1662 0.0821  0.0206  -0.0559 114 LYS D CG  
14426 C CD  . LYS D 114 ? 1.1546 1.1861 1.2708 0.0994  0.0076  -0.0668 114 LYS D CD  
14427 C CE  . LYS D 114 ? 1.2471 1.2849 1.3707 0.1000  -0.0062 -0.0668 114 LYS D CE  
14428 N NZ  . LYS D 114 ? 1.2904 1.3361 1.4294 0.1195  -0.0229 -0.0780 114 LYS D NZ  
14442 N N   . PHE D 115 ? 1.0806 1.0877 1.1495 0.0538  0.0706  -0.0474 115 PHE D N   
14443 C CA  . PHE D 115 ? 1.0952 1.0987 1.1581 0.0506  0.0865  -0.0478 115 PHE D CA  
14444 C C   . PHE D 115 ? 1.1006 1.0820 1.1393 0.0590  0.0867  -0.0492 115 PHE D C   
14445 O O   . PHE D 115 ? 1.1180 1.0845 1.1420 0.0656  0.0752  -0.0488 115 PHE D O   
14446 C CB  . PHE D 115 ? 1.0565 1.0516 1.1010 0.0369  0.0924  -0.0404 115 PHE D CB  
14447 C CG  . PHE D 115 ? 1.0301 1.0431 1.0945 0.0284  0.0954  -0.0390 115 PHE D CG  
14448 C CD1 . PHE D 115 ? 1.0417 1.0696 1.1282 0.0262  0.1101  -0.0430 115 PHE D CD1 
14449 C CD2 . PHE D 115 ? 1.0769 1.0902 1.1370 0.0223  0.0848  -0.0338 115 PHE D CD2 
14450 C CE1 . PHE D 115 ? 1.0383 1.0792 1.1412 0.0174  0.1137  -0.0419 115 PHE D CE1 
14451 C CE2 . PHE D 115 ? 1.0637 1.0910 1.1397 0.0150  0.0873  -0.0326 115 PHE D CE2 
14452 C CZ  . PHE D 115 ? 1.0324 1.0725 1.1292 0.0122  0.1015  -0.0366 115 PHE D CZ  
14462 N N   . LEU D 116 ? 1.1366 1.1130 1.1685 0.0590  0.1006  -0.0507 116 LEU D N   
14463 C CA  . LEU D 116 ? 1.1658 1.1177 1.1699 0.0653  0.1023  -0.0514 116 LEU D CA  
14464 C C   . LEU D 116 ? 1.1863 1.1250 1.1683 0.0567  0.1132  -0.0477 116 LEU D C   
14465 O O   . LEU D 116 ? 1.2013 1.1496 1.1939 0.0553  0.1277  -0.0493 116 LEU D O   
14466 C CB  . LEU D 116 ? 1.1584 1.1172 1.1774 0.0801  0.1078  -0.0598 116 LEU D CB  
14467 C CG  . LEU D 116 ? 1.1719 1.1328 1.1997 0.0941  0.0942  -0.0649 116 LEU D CG  
14468 C CD1 . LEU D 116 ? 1.1588 1.1209 1.1929 0.1101  0.1004  -0.0734 116 LEU D CD1 
14469 C CD2 . LEU D 116 ? 1.2193 1.1512 1.2138 0.0937  0.0806  -0.0596 116 LEU D CD2 
14481 N N   . ALA D 117 ? 1.1555 1.0713 1.1066 0.0511  0.1065  -0.0436 117 ALA D N   
14482 C CA  . ALA D 117 ? 1.1595 1.0625 1.0878 0.0434  0.1124  -0.0407 117 ALA D CA  
14483 C C   . ALA D 117 ? 1.1535 1.0291 1.0510 0.0474  0.1123  -0.0429 117 ALA D C   
14484 O O   . ALA D 117 ? 1.1402 1.0007 1.0237 0.0469  0.1017  -0.0428 117 ALA D O   
14485 C CB  . ALA D 117 ? 1.1045 1.0087 1.0270 0.0317  0.1032  -0.0354 117 ALA D CB  
14491 N N   . LYS D 118 ? 1.1859 1.0526 1.0710 0.0511  0.1247  -0.0449 118 LYS D N   
14492 C CA  . LYS D 118 ? 1.1655 1.0043 1.0185 0.0553  0.1252  -0.0475 118 LYS D CA  
14493 C C   . LYS D 118 ? 1.1681 0.9926 0.9953 0.0475  0.1232  -0.0456 118 LYS D C   
14494 O O   . LYS D 118 ? 1.1771 1.0086 1.0057 0.0445  0.1307  -0.0434 118 LYS D O   
14495 C CB  . LYS D 118 ? 1.1829 1.0188 1.0362 0.0671  0.1404  -0.0517 118 LYS D CB  
14496 C CG  . LYS D 118 ? 1.2531 1.0576 1.0704 0.0729  0.1416  -0.0547 118 LYS D CG  
14497 C CD  . LYS D 118 ? 1.2951 1.0977 1.1151 0.0867  0.1560  -0.0594 118 LYS D CD  
14498 C CE  . LYS D 118 ? 1.3315 1.1402 1.1547 0.0879  0.1758  -0.0592 118 LYS D CE  
14499 N NZ  . LYS D 118 ? 1.3970 1.2036 1.2232 0.1017  0.1906  -0.0645 118 LYS D NZ  
14513 N N   . ILE D 119 ? 1.1994 1.0026 1.0020 0.0446  0.1127  -0.0475 119 ILE D N   
14514 C CA  . ILE D 119 ? 1.2029 0.9937 0.9824 0.0381  0.1069  -0.0480 119 ILE D CA  
14515 C C   . ILE D 119 ? 1.2889 1.0503 1.0372 0.0422  0.1040  -0.0534 119 ILE D C   
14516 O O   . ILE D 119 ? 1.3279 1.0775 1.0723 0.0466  0.1028  -0.0558 119 ILE D O   
14517 C CB  . ILE D 119 ? 1.1957 0.9972 0.9844 0.0261  0.0931  -0.0459 119 ILE D CB  
14518 C CG1 . ILE D 119 ? 1.1960 0.9905 0.9657 0.0210  0.0867  -0.0478 119 ILE D CG1 
14519 C CG2 . ILE D 119 ? 1.1848 0.9764 0.9721 0.0226  0.0838  -0.0477 119 ILE D CG2 
14520 C CD1 . ILE D 119 ? 1.1828 0.9929 0.9656 0.0101  0.0753  -0.0462 119 ILE D CD1 
14532 N N   . LYS D 120 ? 1.3047 1.0519 1.0281 0.0417  0.1023  -0.0557 120 LYS D N   
14533 C CA  . LYS D 120 ? 1.3403 1.0583 1.0317 0.0448  0.0970  -0.0620 120 LYS D CA  
14534 C C   . LYS D 120 ? 1.3254 1.0406 1.0151 0.0330  0.0797  -0.0657 120 LYS D C   
14535 O O   . LYS D 120 ? 1.2850 1.0154 0.9846 0.0248  0.0721  -0.0648 120 LYS D O   
14536 C CB  . LYS D 120 ? 1.3844 1.0860 1.0469 0.0518  0.1026  -0.0639 120 LYS D CB  
14537 C CG  . LYS D 120 ? 1.4710 1.1405 1.0973 0.0563  0.0956  -0.0715 120 LYS D CG  
14538 C CD  . LYS D 120 ? 1.5191 1.1782 1.1210 0.0560  0.0862  -0.0754 120 LYS D CD  
14539 C CE  . LYS D 120 ? 1.4876 1.1677 1.1092 0.0430  0.0705  -0.0762 120 LYS D CE  
14540 N NZ  . LYS D 120 ? 1.5005 1.1672 1.0983 0.0426  0.0545  -0.0848 120 LYS D NZ  
14554 N N   . MET D 121 ? 1.3246 1.0198 1.0022 0.0321  0.0744  -0.0704 121 MET D N   
14555 C CA  . MET D 121 ? 1.3253 1.0176 1.0050 0.0190  0.0607  -0.0745 121 MET D CA  
14556 C C   . MET D 121 ? 1.3332 1.0032 0.9858 0.0175  0.0510  -0.0838 121 MET D C   
14557 O O   . MET D 121 ? 1.3628 1.0111 0.9891 0.0283  0.0551  -0.0869 121 MET D O   
14558 C CB  . MET D 121 ? 1.3242 1.0065 1.0085 0.0168  0.0610  -0.0737 121 MET D CB  
14559 C CG  . MET D 121 ? 1.3164 1.0201 1.0278 0.0171  0.0659  -0.0661 121 MET D CG  
14560 S SD  . MET D 121 ? 1.2631 0.9958 1.0014 0.0030  0.0591  -0.0621 121 MET D SD  
14561 C CE  . MET D 121 ? 1.2247 0.9401 0.9566 -0.0119 0.0499  -0.0671 121 MET D CE  
14571 N N   . PRO D 122 ? 1.2983 0.9731 0.9570 0.0044  0.0380  -0.0893 122 PRO D N   
14572 C CA  . PRO D 122 ? 1.3362 0.9912 0.9722 0.0023  0.0263  -0.1005 122 PRO D CA  
14573 C C   . PRO D 122 ? 1.3980 1.0200 1.0105 0.0060  0.0279  -0.1050 122 PRO D C   
14574 O O   . PRO D 122 ? 1.4519 1.0672 1.0701 0.0042  0.0337  -0.1013 122 PRO D O   
14575 C CB  . PRO D 122 ? 1.3180 0.9893 0.9754 -0.0149 0.0141  -0.1058 122 PRO D CB  
14576 C CG  . PRO D 122 ? 1.2761 0.9675 0.9616 -0.0217 0.0212  -0.0965 122 PRO D CG  
14577 C CD  . PRO D 122 ? 1.2717 0.9721 0.9597 -0.0087 0.0334  -0.0865 122 PRO D CD  
14585 N N   . LYS D 123 ? 1.3756 0.9745 0.9586 0.0125  0.0220  -0.1134 123 LYS D N   
14586 C CA  . LYS D 123 ? 1.4725 1.0368 1.0288 0.0168  0.0221  -0.1189 123 LYS D CA  
14587 C C   . LYS D 123 ? 1.4953 1.0498 1.0556 -0.0001 0.0098  -0.1282 123 LYS D C   
14588 O O   . LYS D 123 ? 1.4658 1.0373 1.0427 -0.0127 -0.0017 -0.1343 123 LYS D O   
14589 C CB  . LYS D 123 ? 1.4596 1.0002 0.9796 0.0312  0.0205  -0.1246 123 LYS D CB  
14590 C CG  . LYS D 123 ? 1.4871 1.0189 0.9937 0.0256  0.0016  -0.1379 123 LYS D CG  
14591 C CD  . LYS D 123 ? 1.5451 1.0621 1.0186 0.0418  -0.0004 -0.1412 123 LYS D CD  
14592 C CE  . LYS D 123 ? 1.5792 1.0757 1.0273 0.0597  0.0179  -0.1339 123 LYS D CE  
14593 N NZ  . LYS D 123 ? 1.6781 1.1436 1.0814 0.0750  0.0144  -0.1406 123 LYS D NZ  
14607 N N   . PHE D 124 ? 1.5468 1.0730 1.0919 -0.0002 0.0131  -0.1298 124 PHE D N   
14608 C CA  . PHE D 124 ? 1.5309 1.0423 1.0774 -0.0174 0.0043  -0.1385 124 PHE D CA  
14609 C C   . PHE D 124 ? 1.5587 1.0544 1.0864 -0.0200 -0.0108 -0.1533 124 PHE D C   
14610 O O   . PHE D 124 ? 1.6227 1.1047 1.1238 -0.0047 -0.0127 -0.1561 124 PHE D O   
14611 C CB  . PHE D 124 ? 1.5688 1.0490 1.0990 -0.0154 0.0124  -0.1359 124 PHE D CB  
14612 C CG  . PHE D 124 ? 1.5863 1.0320 1.0788 0.0007  0.0143  -0.1394 124 PHE D CG  
14613 C CD1 . PHE D 124 ? 1.6428 1.0572 1.1103 -0.0041 0.0039  -0.1520 124 PHE D CD1 
14614 C CD2 . PHE D 124 ? 1.6116 1.0563 1.0947 0.0206  0.0268  -0.1311 124 PHE D CD2 
14615 C CE1 . PHE D 124 ? 1.6422 1.0227 1.0723 0.0118  0.0057  -0.1552 124 PHE D CE1 
14616 C CE2 . PHE D 124 ? 1.6523 1.0654 1.1005 0.0362  0.0300  -0.1345 124 PHE D CE2 
14617 C CZ  . PHE D 124 ? 1.6790 1.0586 1.0988 0.0323  0.0194  -0.1461 124 PHE D CZ  
14627 N N   . LEU D 125 ? 1.5658 1.0629 1.1075 -0.0395 -0.0214 -0.1636 125 LEU D N   
14628 C CA  . LEU D 125 ? 1.6067 1.0898 1.1345 -0.0438 -0.0382 -0.1802 125 LEU D CA  
14629 C C   . LEU D 125 ? 1.5911 1.0327 1.0948 -0.0495 -0.0400 -0.1885 125 LEU D C   
14630 O O   . LEU D 125 ? 1.6350 1.0555 1.1157 -0.0465 -0.0526 -0.2016 125 LEU D O   
14631 C CB  . LEU D 125 ? 1.5791 1.0937 1.1416 -0.0621 -0.0506 -0.1898 125 LEU D CB  
14632 C CG  . LEU D 125 ? 1.5705 1.1263 1.1583 -0.0584 -0.0508 -0.1831 125 LEU D CG  
14633 C CD1 . LEU D 125 ? 1.5818 1.1599 1.1879 -0.0673 -0.0700 -0.1988 125 LEU D CD1 
14634 C CD2 . LEU D 125 ? 1.5548 1.1090 1.1205 -0.0353 -0.0441 -0.1732 125 LEU D CD2 
14646 N N   . SER D 126 ? 1.6319 1.0589 1.1376 -0.0569 -0.0283 -0.1817 126 SER D N   
14647 C CA  . SER D 126 ? 1.6459 1.0285 1.1243 -0.0610 -0.0279 -0.1880 126 SER D CA  
14648 C C   . SER D 126 ? 1.6271 0.9934 1.0973 -0.0549 -0.0113 -0.1744 126 SER D C   
14649 O O   . SER D 126 ? 1.6132 1.0039 1.1077 -0.0573 -0.0024 -0.1634 126 SER D O   
14650 C CB  . SER D 126 ? 1.6355 1.0131 1.1294 -0.0873 -0.0370 -0.2020 126 SER D CB  
14651 O OG  . SER D 126 ? 1.6939 1.0882 1.1973 -0.0918 -0.0549 -0.2169 126 SER D OG  
14657 N N   . LEU D 127 ? 1.6505 0.9740 1.0846 -0.0457 -0.0082 -0.1760 127 LEU D N   
14658 C CA  . LEU D 127 ? 1.6939 0.9955 1.1143 -0.0374 0.0053  -0.1654 127 LEU D CA  
14659 C C   . LEU D 127 ? 1.7532 1.0034 1.1410 -0.0438 0.0036  -0.1738 127 LEU D C   
14660 O O   . LEU D 127 ? 1.7471 0.9701 1.1045 -0.0346 -0.0025 -0.1819 127 LEU D O   
14661 C CB  . LEU D 127 ? 1.7053 1.0107 1.1124 -0.0101 0.0138  -0.1560 127 LEU D CB  
14662 C CG  . LEU D 127 ? 1.7500 1.0408 1.1481 0.0022  0.0264  -0.1456 127 LEU D CG  
14663 C CD1 . LEU D 127 ? 1.7379 1.0619 1.1527 0.0209  0.0353  -0.1350 127 LEU D CD1 
14664 C CD2 . LEU D 127 ? 1.7878 1.0285 1.1431 0.0135  0.0277  -0.1502 127 LEU D CD2 
14676 N N   . GLU D 128 ? 1.7616 0.9957 1.1531 -0.0594 0.0096  -0.1718 128 GLU D N   
14677 C CA  . GLU D 128 ? 1.7999 0.9833 1.1625 -0.0703 0.0092  -0.1799 128 GLU D CA  
14678 C C   . GLU D 128 ? 1.8974 1.0522 1.2428 -0.0652 0.0226  -0.1691 128 GLU D C   
14679 O O   . GLU D 128 ? 1.8693 1.0468 1.2290 -0.0546 0.0305  -0.1566 128 GLU D O   
14680 C CB  . GLU D 128 ? 1.7831 0.9711 1.1677 -0.1012 0.0021  -0.1926 128 GLU D CB  
14681 C CG  . GLU D 128 ? 1.8511 1.0021 1.2115 -0.1104 -0.0084 -0.2092 128 GLU D CG  
14682 C CD  . GLU D 128 ? 1.8437 1.0064 1.2340 -0.1419 -0.0155 -0.2234 128 GLU D CD  
14683 O OE1 . GLU D 128 ? 1.8047 1.0154 1.2367 -0.1514 -0.0176 -0.2228 128 GLU D OE1 
14684 O OE2 . GLU D 128 ? 1.8708 0.9951 1.2440 -0.1572 -0.0187 -0.2358 128 GLU D OE2 
14691 N N   . GLU D 129 ? 1.9599 1.0615 1.2721 -0.0724 0.0244  -0.1748 129 GLU D N   
14692 C CA  . GLU D 129 ? 2.0103 1.0743 1.2981 -0.0680 0.0362  -0.1662 129 GLU D CA  
14693 C C   . GLU D 129 ? 2.0274 1.0514 1.3037 -0.0960 0.0385  -0.1748 129 GLU D C   
14694 O O   . GLU D 129 ? 2.1446 1.1172 1.3828 -0.0964 0.0376  -0.1818 129 GLU D O   
14695 C CB  . GLU D 129 ? 2.0660 1.0963 1.3127 -0.0389 0.0385  -0.1627 129 GLU D CB  
14696 C CG  . GLU D 129 ? 2.1561 1.1474 1.3749 -0.0298 0.0490  -0.1540 129 GLU D CG  
14697 C CD  . GLU D 129 ? 2.2619 1.2261 1.4443 0.0019  0.0505  -0.1512 129 GLU D CD  
14698 O OE1 . GLU D 129 ? 2.2715 1.2143 1.4301 0.0088  0.0450  -0.1596 129 GLU D OE1 
14699 O OE2 . GLU D 129 ? 2.2726 1.2372 1.4505 0.0208  0.0568  -0.1414 129 GLU D OE2 
14706 N N   . ILE D 130 ? 2.0592 1.1069 1.3693 -0.1202 0.0424  -0.1747 130 ILE D N   
14707 C CA  . ILE D 130 ? 2.0868 1.1011 1.3924 -0.1500 0.0472  -0.1833 130 ILE D CA  
14708 C C   . ILE D 130 ? 2.1176 1.0772 1.3845 -0.1466 0.0618  -0.1742 130 ILE D C   
14709 O O   . ILE D 130 ? 2.1005 1.0575 1.3529 -0.1229 0.0672  -0.1610 130 ILE D O   
14710 C CB  . ILE D 130 ? 2.0751 1.1345 1.4313 -0.1765 0.0482  -0.1869 130 ILE D CB  
14711 C CG1 . ILE D 130 ? 1.9970 1.1004 1.3802 -0.1661 0.0540  -0.1721 130 ILE D CG1 
14712 C CG2 . ILE D 130 ? 2.0406 1.1376 1.4265 -0.1851 0.0316  -0.2019 130 ILE D CG2 
14713 C CD1 . ILE D 130 ? 2.0125 1.0846 1.3692 -0.1549 0.0680  -0.1576 130 ILE D CD1 
14725 N N   . ASN D 131 ? 2.1830 1.0964 1.4321 -0.1709 0.0681  -0.1822 131 ASN D N   
14726 C CA  . ASN D 131 ? 2.2104 1.0609 1.4149 -0.1696 0.0826  -0.1748 131 ASN D CA  
14727 C C   . ASN D 131 ? 2.2434 1.0799 1.4618 -0.2055 0.0955  -0.1789 131 ASN D C   
14728 O O   . ASN D 131 ? 2.2958 1.0988 1.5051 -0.2294 0.0969  -0.1919 131 ASN D O   
14729 C CB  . ASN D 131 ? 2.2352 1.0242 1.3863 -0.1583 0.0795  -0.1806 131 ASN D CB  
14730 C CG  . ASN D 131 ? 2.2469 1.0388 1.3755 -0.1191 0.0732  -0.1730 131 ASN D CG  
14731 O OD1 . ASN D 131 ? 2.2501 1.0844 1.4000 -0.1005 0.0731  -0.1622 131 ASN D OD1 
14732 N ND2 . ASN D 131 ? 2.1317 0.8790 1.2183 -0.1066 0.0683  -0.1792 131 ASN D ND2 
14739 N N   . VAL D 132 ? 2.2667 1.1283 1.5075 -0.2093 0.1057  -0.1682 132 VAL D N   
14740 C CA  . VAL D 132 ? 2.3164 1.1663 1.5710 -0.2420 0.1211  -0.1704 132 VAL D CA  
14741 C C   . VAL D 132 ? 2.4069 1.1789 1.6042 -0.2412 0.1381  -0.1630 132 VAL D C   
14742 O O   . VAL D 132 ? 2.4006 1.1533 1.5664 -0.2140 0.1416  -0.1489 132 VAL D O   
14743 C CB  . VAL D 132 ? 2.2748 1.1833 1.5754 -0.2456 0.1252  -0.1622 132 VAL D CB  
14744 C CG1 . VAL D 132 ? 2.2986 1.1941 1.6132 -0.2794 0.1436  -0.1647 132 VAL D CG1 
14745 C CG2 . VAL D 132 ? 2.1805 1.1621 1.5330 -0.2442 0.1079  -0.1694 132 VAL D CG2 
14755 N N   . ASP D 133 ? 2.5760 1.3019 1.7591 -0.2708 0.1486  -0.1732 133 ASP D N   
14756 C CA  . ASP D 133 ? 2.6487 1.2918 1.7716 -0.2724 0.1659  -0.1674 133 ASP D CA  
14757 C C   . ASP D 133 ? 2.6707 1.2727 1.7383 -0.2350 0.1579  -0.1604 133 ASP D C   
14758 O O   . ASP D 133 ? 2.6834 1.2786 1.7401 -0.2269 0.1444  -0.1696 133 ASP D O   
14759 C CB  . ASP D 133 ? 2.6448 1.2808 1.7658 -0.2774 0.1852  -0.1540 133 ASP D CB  
14760 C CG  . ASP D 133 ? 2.6898 1.3517 1.8576 -0.3177 0.1981  -0.1620 133 ASP D CG  
14761 O OD1 . ASP D 133 ? 2.6605 1.3745 1.8799 -0.3352 0.1866  -0.1762 133 ASP D OD1 
14762 O OD2 . ASP D 133 ? 2.7324 1.3621 1.8847 -0.3308 0.2198  -0.1544 133 ASP D OD2 
14767 N N   . GLU D 134 ? 2.5441 1.1194 1.5765 -0.2108 0.1656  -0.1450 134 GLU D N   
14768 C CA  . GLU D 134 ? 2.5292 1.0654 1.5094 -0.1733 0.1589  -0.1386 134 GLU D CA  
14769 C C   . GLU D 134 ? 2.4626 1.0571 1.4659 -0.1388 0.1453  -0.1301 134 GLU D C   
14770 O O   . GLU D 134 ? 2.4480 1.0213 1.4166 -0.1056 0.1385  -0.1258 134 GLU D O   
14771 C CB  . GLU D 134 ? 2.6099 1.0671 1.5273 -0.1668 0.1755  -0.1289 134 GLU D CB  
14772 C CG  . GLU D 134 ? 2.5827 1.0556 1.5108 -0.1652 0.1864  -0.1160 134 GLU D CG  
14773 C CD  . GLU D 134 ? 2.5842 1.0131 1.4996 -0.1999 0.2097  -0.1159 134 GLU D CD  
14774 O OE1 . GLU D 134 ? 2.6185 1.0193 1.5324 -0.2309 0.2170  -0.1277 134 GLU D OE1 
14775 O OE2 . GLU D 134 ? 2.5999 1.0219 1.5072 -0.1963 0.2214  -0.1045 134 GLU D OE2 
14782 N N   . TYR D 135 ? 2.4206 1.0874 1.4821 -0.1461 0.1417  -0.1281 135 TYR D N   
14783 C CA  . TYR D 135 ? 2.3406 1.0642 1.4278 -0.1170 0.1309  -0.1200 135 TYR D CA  
14784 C C   . TYR D 135 ? 2.2833 1.0630 1.4096 -0.1149 0.1154  -0.1288 135 TYR D C   
14785 O O   . TYR D 135 ? 2.2719 1.0703 1.4262 -0.1415 0.1127  -0.1399 135 TYR D O   
14786 C CB  . TYR D 135 ? 2.2829 1.0458 1.4041 -0.1241 0.1377  -0.1110 135 TYR D CB  
14787 C CG  . TYR D 135 ? 2.3602 1.0674 1.4465 -0.1353 0.1559  -0.1041 135 TYR D CG  
14788 C CD1 . TYR D 135 ? 2.4258 1.0664 1.4498 -0.1127 0.1608  -0.0972 135 TYR D CD1 
14789 C CD2 . TYR D 135 ? 2.3895 1.1088 1.5031 -0.1674 0.1688  -0.1049 135 TYR D CD2 
14790 C CE1 . TYR D 135 ? 2.4674 1.0513 1.4534 -0.1214 0.1781  -0.0904 135 TYR D CE1 
14791 C CE2 . TYR D 135 ? 2.4198 1.0846 1.4984 -0.1776 0.1879  -0.0982 135 TYR D CE2 
14792 C CZ  . TYR D 135 ? 2.4590 1.0542 1.4718 -0.1545 0.1926  -0.0906 135 TYR D CZ  
14793 O OH  . TYR D 135 ? 2.5166 1.0519 1.4886 -0.1635 0.2124  -0.0836 135 TYR D OH  
14803 N N   . LYS D 136 ? 2.2385 1.0434 1.3655 -0.0827 0.1055  -0.1245 136 LYS D N   
14804 C CA  . LYS D 136 ? 2.2005 1.0558 1.3591 -0.0760 0.0924  -0.1308 136 LYS D CA  
14805 C C   . LYS D 136 ? 2.1309 1.0555 1.3365 -0.0670 0.0890  -0.1231 136 LYS D C   
14806 O O   . LYS D 136 ? 2.1316 1.0620 1.3321 -0.0445 0.0909  -0.1130 136 LYS D O   
14807 C CB  . LYS D 136 ? 2.2392 1.0684 1.3621 -0.0473 0.0858  -0.1330 136 LYS D CB  
14808 C CG  . LYS D 136 ? 2.2576 1.1218 1.3899 -0.0129 0.0816  -0.1248 136 LYS D CG  
14809 C CD  . LYS D 136 ? 2.3016 1.1356 1.3964 0.0153  0.0773  -0.1279 136 LYS D CD  
14810 C CE  . LYS D 136 ? 2.2973 1.1077 1.3762 0.0035  0.0721  -0.1402 136 LYS D CE  
14811 N NZ  . LYS D 136 ? 2.3311 1.1043 1.3674 0.0312  0.0695  -0.1429 136 LYS D NZ  
14825 N N   . LEU D 137 ? 2.1085 1.0839 1.3592 -0.0845 0.0834  -0.1288 137 LEU D N   
14826 C CA  . LEU D 137 ? 2.0140 1.0539 1.3104 -0.0808 0.0807  -0.1225 137 LEU D CA  
14827 C C   . LEU D 137 ? 2.0433 1.1267 1.3653 -0.0756 0.0690  -0.1291 137 LEU D C   
14828 O O   . LEU D 137 ? 2.0296 1.0935 1.3351 -0.0772 0.0628  -0.1391 137 LEU D O   
14829 C CB  . LEU D 137 ? 1.9523 1.0116 1.2793 -0.1091 0.0872  -0.1221 137 LEU D CB  
14830 C CG  . LEU D 137 ? 1.9955 1.0201 1.3033 -0.1158 0.1010  -0.1137 137 LEU D CG  
14831 C CD1 . LEU D 137 ? 2.1088 1.0580 1.3601 -0.1129 0.1082  -0.1145 137 LEU D CD1 
14832 C CD2 . LEU D 137 ? 1.8743 0.9179 1.2149 -0.1490 0.1082  -0.1174 137 LEU D CD2 
14844 N N   . GLY D 138 ? 2.0198 1.1596 1.3795 -0.0690 0.0661  -0.1236 138 GLY D N   
14845 C CA  . GLY D 138 ? 1.9004 1.0818 1.2836 -0.0638 0.0566  -0.1284 138 GLY D CA  
14846 C C   . GLY D 138 ? 1.8823 1.1042 1.3058 -0.0874 0.0521  -0.1338 138 GLY D C   
14847 O O   . GLY D 138 ? 1.9714 1.1986 1.4117 -0.1064 0.0578  -0.1321 138 GLY D O   
14851 N N   . LEU D 139 ? 1.8165 1.0660 1.2538 -0.0847 0.0421  -0.1407 139 LEU D N   
14852 C CA  . LEU D 139 ? 1.7391 1.0276 1.2130 -0.1039 0.0350  -0.1479 139 LEU D CA  
14853 C C   . LEU D 139 ? 1.6917 1.0169 1.1782 -0.0882 0.0264  -0.1484 139 LEU D C   
14854 O O   . LEU D 139 ? 1.7019 1.0157 1.1718 -0.0826 0.0179  -0.1575 139 LEU D O   
14855 C CB  . LEU D 139 ? 1.7483 1.0131 1.2173 -0.1269 0.0294  -0.1632 139 LEU D CB  
14856 C CG  . LEU D 139 ? 1.7250 1.0257 1.2354 -0.1520 0.0254  -0.1712 139 LEU D CG  
14857 C CD1 . LEU D 139 ? 1.8281 1.0979 1.3360 -0.1795 0.0293  -0.1817 139 LEU D CD1 
14858 C CD2 . LEU D 139 ? 1.7164 1.0498 1.2430 -0.1483 0.0095  -0.1814 139 LEU D CD2 
14870 N N   . VAL D 140 ? 1.6541 1.0198 1.1668 -0.0810 0.0292  -0.1388 140 VAL D N   
14871 C CA  . VAL D 140 ? 1.6042 1.0059 1.1309 -0.0685 0.0233  -0.1381 140 VAL D CA  
14872 C C   . VAL D 140 ? 1.5907 1.0307 1.1531 -0.0859 0.0166  -0.1428 140 VAL D C   
14873 O O   . VAL D 140 ? 1.6318 1.1000 1.2200 -0.0901 0.0215  -0.1348 140 VAL D O   
14874 C CB  . VAL D 140 ? 1.5789 0.9987 1.1104 -0.0477 0.0314  -0.1249 140 VAL D CB  
14875 C CG1 . VAL D 140 ? 1.5334 0.9824 1.0732 -0.0349 0.0277  -0.1246 140 VAL D CG1 
14876 C CG2 . VAL D 140 ? 1.6498 1.0328 1.1498 -0.0310 0.0384  -0.1209 140 VAL D CG2 
14886 N N   . ARG D 141 ? 1.5858 1.0267 1.1494 -0.0954 0.0046  -0.1566 141 ARG D N   
14887 C CA  . ARG D 141 ? 1.6064 1.0848 1.2046 -0.1104 -0.0035 -0.1634 141 ARG D CA  
14888 C C   . ARG D 141 ? 1.5783 1.0941 1.1901 -0.0956 -0.0066 -0.1573 141 ARG D C   
14889 O O   . ARG D 141 ? 1.5839 1.0939 1.1757 -0.0754 -0.0054 -0.1527 141 ARG D O   
14890 C CB  . ARG D 141 ? 1.6325 1.1017 1.2285 -0.1227 -0.0178 -0.1820 141 ARG D CB  
14891 C CG  . ARG D 141 ? 1.6773 1.1160 1.2698 -0.1445 -0.0146 -0.1902 141 ARG D CG  
14892 C CD  . ARG D 141 ? 1.7549 1.2095 1.3726 -0.1656 -0.0276 -0.2091 141 ARG D CD  
14893 N NE  . ARG D 141 ? 1.8343 1.2705 1.4617 -0.1916 -0.0197 -0.2149 141 ARG D NE  
14894 C CZ  . ARG D 141 ? 1.8248 1.2139 1.4246 -0.1991 -0.0168 -0.2208 141 ARG D CZ  
14895 N NH1 . ARG D 141 ? 1.7905 1.1466 1.3513 -0.1821 -0.0222 -0.2220 141 ARG D NH1 
14896 N NH2 . ARG D 141 ? 1.8607 1.2336 1.4707 -0.2244 -0.0072 -0.2256 141 ARG D NH2 
14910 N N   . PHE D 142 ? 1.6238 1.1772 1.2695 -0.1060 -0.0094 -0.1576 142 PHE D N   
14911 C CA  . PHE D 142 ? 1.5797 1.1679 1.2391 -0.0942 -0.0124 -0.1522 142 PHE D CA  
14912 C C   . PHE D 142 ? 1.6001 1.2193 1.2871 -0.1067 -0.0250 -0.1635 142 PHE D C   
14913 O O   . PHE D 142 ? 1.6100 1.2299 1.3134 -0.1264 -0.0285 -0.1738 142 PHE D O   
14914 C CB  . PHE D 142 ? 1.5205 1.1262 1.1941 -0.0891 0.0002  -0.1361 142 PHE D CB  
14915 C CG  . PHE D 142 ? 1.4899 1.0769 1.1412 -0.0706 0.0101  -0.1256 142 PHE D CG  
14916 C CD1 . PHE D 142 ? 1.5039 1.0616 1.1406 -0.0709 0.0187  -0.1214 142 PHE D CD1 
14917 C CD2 . PHE D 142 ? 1.4924 1.0904 1.1372 -0.0525 0.0114  -0.1206 142 PHE D CD2 
14918 C CE1 . PHE D 142 ? 1.5004 1.0438 1.1193 -0.0524 0.0266  -0.1134 142 PHE D CE1 
14919 C CE2 . PHE D 142 ? 1.4848 1.0694 1.1141 -0.0361 0.0214  -0.1125 142 PHE D CE2 
14920 C CZ  . PHE D 142 ? 1.4748 1.0339 1.0926 -0.0354 0.0282  -0.1093 142 PHE D CZ  
14930 N N   . SER D 143 ? 1.6025 1.2471 1.2947 -0.0949 -0.0313 -0.1621 143 SER D N   
14931 C CA  . SER D 143 ? 1.5878 1.2639 1.3046 -0.1021 -0.0449 -0.1730 143 SER D CA  
14932 C C   . SER D 143 ? 1.5789 1.2857 1.3316 -0.1149 -0.0378 -0.1667 143 SER D C   
14933 O O   . SER D 143 ? 1.5785 1.3105 1.3427 -0.1071 -0.0354 -0.1577 143 SER D O   
14934 C CB  . SER D 143 ? 1.5581 1.2441 1.2609 -0.0827 -0.0533 -0.1728 143 SER D CB  
14935 O OG  . SER D 143 ? 1.5318 1.2211 1.2278 -0.0691 -0.0401 -0.1561 143 SER D OG  
14941 N N   . GLY D 144 ? 1.6111 1.3133 1.3799 -0.1351 -0.0334 -0.1716 144 GLY D N   
14942 C CA  . GLY D 144 ? 1.6271 1.3536 1.4270 -0.1483 -0.0247 -0.1662 144 GLY D CA  
14943 C C   . GLY D 144 ? 1.6728 1.3737 1.4692 -0.1616 -0.0095 -0.1604 144 GLY D C   
14944 O O   . GLY D 144 ? 1.7121 1.4219 1.5321 -0.1810 -0.0043 -0.1649 144 GLY D O   
14948 N N   . ILE D 145 ? 1.7523 1.4198 1.5178 -0.1506 -0.0015 -0.1509 145 ILE D N   
14949 C CA  . ILE D 145 ? 1.7922 1.4294 1.5461 -0.1584 0.0128  -0.1439 145 ILE D CA  
14950 C C   . ILE D 145 ? 1.7955 1.3889 1.5137 -0.1526 0.0127  -0.1468 145 ILE D C   
14951 O O   . ILE D 145 ? 1.7989 1.3866 1.4991 -0.1374 0.0048  -0.1494 145 ILE D O   
14952 C CB  . ILE D 145 ? 1.8396 1.4828 1.5930 -0.1470 0.0238  -0.1263 145 ILE D CB  
14953 C CG1 . ILE D 145 ? 1.8170 1.4197 1.5459 -0.1473 0.0363  -0.1189 145 ILE D CG1 
14954 C CG2 . ILE D 145 ? 1.7820 1.4379 1.5268 -0.1242 0.0194  -0.1195 145 ILE D CG2 
14955 C CD1 . ILE D 145 ? 1.7585 1.3666 1.4915 -0.1418 0.0465  -0.1046 145 ILE D CD1 
14967 N N   . ASN D 146 ? 1.7407 1.3003 1.4462 -0.1645 0.0226  -0.1465 146 ASN D N   
14968 C CA  . ASN D 146 ? 1.7187 1.2314 1.3874 -0.1593 0.0244  -0.1483 146 ASN D CA  
14969 C C   . ASN D 146 ? 1.6821 1.1670 1.3298 -0.1514 0.0385  -0.1342 146 ASN D C   
14970 O O   . ASN D 146 ? 1.6663 1.1347 1.3147 -0.1662 0.0489  -0.1321 146 ASN D O   
14971 C CB  . ASN D 146 ? 1.7433 1.2336 1.4109 -0.1815 0.0217  -0.1639 146 ASN D CB  
14972 C CG  . ASN D 146 ? 1.8028 1.3274 1.5002 -0.1923 0.0071  -0.1796 146 ASN D CG  
14973 O OD1 . ASN D 146 ? 1.7483 1.2885 1.4428 -0.1779 -0.0060 -0.1836 146 ASN D OD1 
14974 N ND2 . ASN D 146 ? 1.8823 1.4183 1.6081 -0.2172 0.0096  -0.1891 146 ASN D ND2 
14981 N N   . HIS D 147 ? 1.6446 1.1234 1.2731 -0.1277 0.0390  -0.1253 147 HIS D N   
14982 C CA  . HIS D 147 ? 1.5871 1.0402 1.1947 -0.1159 0.0494  -0.1136 147 HIS D CA  
14983 C C   . HIS D 147 ? 1.6160 1.0158 1.1852 -0.1146 0.0523  -0.1175 147 HIS D C   
14984 O O   . HIS D 147 ? 1.6626 1.0488 1.2155 -0.1088 0.0454  -0.1252 147 HIS D O   
14985 C CB  . HIS D 147 ? 1.5276 1.0005 1.1358 -0.0910 0.0487  -0.1041 147 HIS D CB  
14986 C CG  . HIS D 147 ? 1.5290 1.0496 1.1707 -0.0906 0.0470  -0.0989 147 HIS D CG  
14987 N ND1 . HIS D 147 ? 1.5030 1.0369 1.1538 -0.0820 0.0527  -0.0876 147 HIS D ND1 
14988 C CD2 . HIS D 147 ? 1.5632 1.1193 1.2293 -0.0965 0.0395  -0.1039 147 HIS D CD2 
14989 C CE1 . HIS D 147 ? 1.4590 1.0341 1.1386 -0.0838 0.0495  -0.0856 147 HIS D CE1 
14990 N NE2 . HIS D 147 ? 1.5002 1.0891 1.1889 -0.0922 0.0417  -0.0951 147 HIS D NE2 
14998 N N   . PHE D 148 ? 1.6260 0.9923 1.1773 -0.1188 0.0626  -0.1120 148 PHE D N   
14999 C CA  . PHE D 148 ? 1.6631 0.9737 1.1728 -0.1145 0.0668  -0.1135 148 PHE D CA  
15000 C C   . PHE D 148 ? 1.6802 0.9766 1.1683 -0.0883 0.0707  -0.1022 148 PHE D C   
15001 O O   . PHE D 148 ? 1.6803 0.9965 1.1820 -0.0821 0.0743  -0.0927 148 PHE D O   
15002 C CB  . PHE D 148 ? 1.6683 0.9434 1.1675 -0.1385 0.0764  -0.1167 148 PHE D CB  
15003 C CG  . PHE D 148 ? 1.6785 0.9632 1.1986 -0.1649 0.0723  -0.1309 148 PHE D CG  
15004 C CD1 . PHE D 148 ? 1.6328 0.9684 1.1967 -0.1776 0.0682  -0.1345 148 PHE D CD1 
15005 C CD2 . PHE D 148 ? 1.7179 0.9609 1.2142 -0.1764 0.0717  -0.1418 148 PHE D CD2 
15006 C CE1 . PHE D 148 ? 1.6902 1.0377 1.2764 -0.2007 0.0628  -0.1495 148 PHE D CE1 
15007 C CE2 . PHE D 148 ? 1.7548 1.0087 1.2735 -0.2009 0.0665  -0.1569 148 PHE D CE2 
15008 C CZ  . PHE D 148 ? 1.7147 1.0224 1.2798 -0.2127 0.0616  -0.1613 148 PHE D CZ  
15018 N N   . ILE D 149 ? 1.7392 1.0023 1.1943 -0.0721 0.0691  -0.1040 149 ILE D N   
15019 C CA  . ILE D 149 ? 1.7454 0.9937 1.1794 -0.0453 0.0715  -0.0959 149 ILE D CA  
15020 C C   . ILE D 149 ? 1.8341 1.0196 1.2238 -0.0450 0.0780  -0.0956 149 ILE D C   
15021 O O   . ILE D 149 ? 1.8642 1.0134 1.2312 -0.0568 0.0783  -0.1037 149 ILE D O   
15022 C CB  . ILE D 149 ? 1.7923 1.0527 1.2226 -0.0229 0.0659  -0.0981 149 ILE D CB  
15023 C CG1 . ILE D 149 ? 1.7406 1.0585 1.2103 -0.0224 0.0612  -0.0976 149 ILE D CG1 
15024 C CG2 . ILE D 149 ? 1.7689 1.0130 1.1788 0.0048  0.0684  -0.0919 149 ILE D CG2 
15025 C CD1 . ILE D 149 ? 1.6165 0.9708 1.1125 -0.0128 0.0634  -0.0879 149 ILE D CD1 
15037 N N   . PHE D 150 ? 1.8537 1.0240 1.2289 -0.0309 0.0826  -0.0867 150 PHE D N   
15038 C CA  . PHE D 150 ? 1.8949 1.0016 1.2218 -0.0247 0.0886  -0.0850 150 PHE D CA  
15039 C C   . PHE D 150 ? 1.9283 1.0309 1.2396 0.0090  0.0855  -0.0792 150 PHE D C   
15040 O O   . PHE D 150 ? 1.8921 1.0277 1.2257 0.0195  0.0840  -0.0726 150 PHE D O   
15041 C CB  . PHE D 150 ? 1.9022 0.9843 1.2211 -0.0447 0.0989  -0.0809 150 PHE D CB  
15042 C CG  . PHE D 150 ? 2.0256 1.0398 1.2906 -0.0349 0.1059  -0.0771 150 PHE D CG  
15043 C CD1 . PHE D 150 ? 2.0202 1.0250 1.2672 -0.0072 0.1042  -0.0692 150 PHE D CD1 
15044 C CD2 . PHE D 150 ? 2.0773 1.0352 1.3082 -0.0528 0.1138  -0.0823 150 PHE D CD2 
15045 C CE1 . PHE D 150 ? 2.0353 0.9744 1.2282 0.0044  0.1096  -0.0661 150 PHE D CE1 
15046 C CE2 . PHE D 150 ? 2.1268 1.0168 1.3028 -0.0429 0.1210  -0.0785 150 PHE D CE2 
15047 C CZ  . PHE D 150 ? 2.1029 0.9827 1.2583 -0.0134 0.1186  -0.0701 150 PHE D CZ  
15057 N N   . ASN D 151 ? 1.9943 1.0565 1.2680 0.0263  0.0841  -0.0825 151 ASN D N   
15058 C CA  . ASN D 151 ? 2.0610 1.1137 1.3163 0.0598  0.0809  -0.0791 151 ASN D CA  
15059 C C   . ASN D 151 ? 2.1492 1.1382 1.3553 0.0657  0.0858  -0.0753 151 ASN D C   
15060 O O   . ASN D 151 ? 2.1859 1.1202 1.3540 0.0539  0.0911  -0.0786 151 ASN D O   
15061 C CB  . ASN D 151 ? 2.0861 1.1339 1.3292 0.0784  0.0765  -0.0855 151 ASN D CB  
15062 C CG  . ASN D 151 ? 2.1345 1.1916 1.3745 0.1137  0.0724  -0.0837 151 ASN D CG  
15063 O OD1 . ASN D 151 ? 2.2067 1.2562 1.4394 0.1266  0.0715  -0.0785 151 ASN D OD1 
15064 N ND2 . ASN D 151 ? 2.1465 1.2202 1.3925 0.1302  0.0699  -0.0887 151 ASN D ND2 
15071 N N   . ILE D 152 ? 2.1058 1.0995 1.3105 0.0843  0.0840  -0.0688 152 ILE D N   
15072 C CA  . ILE D 152 ? 2.1215 1.0534 1.2769 0.0905  0.0888  -0.0642 152 ILE D CA  
15073 C C   . ILE D 152 ? 2.1985 1.0808 1.3055 0.1190  0.0852  -0.0673 152 ILE D C   
15074 O O   . ILE D 152 ? 2.2597 1.0741 1.3148 0.1149  0.0915  -0.0678 152 ILE D O   
15075 C CB  . ILE D 152 ? 2.0580 1.0109 1.2270 0.1005  0.0868  -0.0567 152 ILE D CB  
15076 C CG1 . ILE D 152 ? 1.9947 1.0149 1.2229 0.0803  0.0867  -0.0549 152 ILE D CG1 
15077 C CG2 . ILE D 152 ? 2.0443 0.9321 1.1641 0.0951  0.0958  -0.0511 152 ILE D CG2 
15078 C CD1 . ILE D 152 ? 1.8944 0.9317 1.1350 0.0838  0.0863  -0.0474 152 ILE D CD1 
15090 N N   . LYS D 153 ? 2.1769 1.0915 1.2998 0.1484  0.0757  -0.0700 153 LYS D N   
15091 C CA  . LYS D 153 ? 2.2598 1.1328 1.3405 0.1776  0.0717  -0.0742 153 LYS D CA  
15092 C C   . LYS D 153 ? 2.3287 1.1609 1.3801 0.1641  0.0765  -0.0798 153 LYS D C   
15093 O O   . LYS D 153 ? 2.3959 1.1590 1.3905 0.1708  0.0794  -0.0807 153 LYS D O   
15094 C CB  . LYS D 153 ? 2.2225 1.1486 1.3373 0.2069  0.0625  -0.0781 153 LYS D CB  
15095 C CG  . LYS D 153 ? 2.2625 1.1535 1.3390 0.2436  0.0567  -0.0828 153 LYS D CG  
15096 C CD  . LYS D 153 ? 2.3128 1.1699 1.3601 0.2440  0.0598  -0.0890 153 LYS D CD  
15097 C CE  . LYS D 153 ? 2.3129 1.2239 1.4048 0.2330  0.0613  -0.0932 153 LYS D CE  
15098 N NZ  . LYS D 153 ? 2.2123 1.1787 1.3424 0.2599  0.0565  -0.0969 153 LYS D NZ  
15112 N N   . GLU D 154 ? 2.4291 1.3004 1.5158 0.1459  0.0770  -0.0841 154 GLU D N   
15113 C CA  . GLU D 154 ? 2.4249 1.2607 1.4858 0.1344  0.0795  -0.0909 154 GLU D CA  
15114 C C   . GLU D 154 ? 2.4339 1.2123 1.4608 0.1060  0.0880  -0.0905 154 GLU D C   
15115 O O   . GLU D 154 ? 2.5480 1.2657 1.5274 0.1058  0.0907  -0.0947 154 GLU D O   
15116 C CB  . GLU D 154 ? 2.4822 1.3724 1.5879 0.1204  0.0772  -0.0957 154 GLU D CB  
15117 C CG  . GLU D 154 ? 2.4817 1.4215 1.6162 0.1470  0.0720  -0.0973 154 GLU D CG  
15118 C CD  . GLU D 154 ? 2.6346 1.5403 1.7327 0.1724  0.0704  -0.1030 154 GLU D CD  
15119 O OE1 . GLU D 154 ? 2.7159 1.5616 1.7680 0.1660  0.0723  -0.1065 154 GLU D OE1 
15120 O OE2 . GLU D 154 ? 2.7032 1.6423 1.8196 0.1984  0.0679  -0.1045 154 GLU D OE2 
15127 N N   . ASN D 155 ? 2.3251 1.1207 1.3755 0.0815  0.0934  -0.0859 155 ASN D N   
15128 C CA  . ASN D 155 ? 2.3522 1.0980 1.3764 0.0520  0.1041  -0.0858 155 ASN D CA  
15129 C C   . ASN D 155 ? 2.4269 1.1114 1.3995 0.0652  0.1103  -0.0789 155 ASN D C   
15130 O O   . ASN D 155 ? 2.4476 1.1353 1.4104 0.0967  0.1042  -0.0744 155 ASN D O   
15131 C CB  . ASN D 155 ? 2.2900 1.0826 1.3636 0.0198  0.1084  -0.0849 155 ASN D CB  
15132 C CG  . ASN D 155 ? 2.2987 1.0617 1.3657 -0.0164 0.1167  -0.0916 155 ASN D CG  
15133 O OD1 . ASN D 155 ? 2.2762 1.0360 1.3434 -0.0243 0.1124  -0.1009 155 ASN D OD1 
15134 N ND2 . ASN D 155 ? 2.2969 1.0376 1.3582 -0.0386 0.1290  -0.0878 155 ASN D ND2 
15141 N N   . LYS D 156 ? 2.4203 1.0468 1.3588 0.0407  0.1228  -0.0788 156 LYS D N   
15142 C CA  . LYS D 156 ? 2.4597 1.0142 1.3382 0.0511  0.1311  -0.0725 156 LYS D CA  
15143 C C   . LYS D 156 ? 2.4625 1.0274 1.3547 0.0375  0.1401  -0.0641 156 LYS D C   
15144 O O   . LYS D 156 ? 2.4108 1.0397 1.3601 0.0199  0.1396  -0.0635 156 LYS D O   
15145 C CB  . LYS D 156 ? 2.5163 0.9917 1.3420 0.0333  0.1419  -0.0772 156 LYS D CB  
15146 C CG  . LYS D 156 ? 2.5972 1.0549 1.4034 0.0461  0.1335  -0.0859 156 LYS D CG  
15147 C CD  . LYS D 156 ? 2.5977 1.0824 1.4054 0.0897  0.1188  -0.0851 156 LYS D CD  
15148 C CE  . LYS D 156 ? 2.5214 0.9849 1.3062 0.1034  0.1123  -0.0936 156 LYS D CE  
15149 N NZ  . LYS D 156 ? 2.6517 1.0427 1.3901 0.0806  0.1214  -0.0990 156 LYS D NZ  
15163 N N   . GLU D 157 ? 2.5209 1.0183 1.3560 0.0471  0.1486  -0.0576 157 GLU D N   
15164 C CA  . GLU D 157 ? 2.5187 1.0152 1.3559 0.0383  0.1582  -0.0490 157 GLU D CA  
15165 C C   . GLU D 157 ? 2.4947 1.0167 1.3723 -0.0065 0.1717  -0.0508 157 GLU D C   
15166 O O   . GLU D 157 ? 2.4953 0.9903 1.3661 -0.0340 0.1808  -0.0576 157 GLU D O   
15167 C CB  . GLU D 157 ? 2.5991 1.0022 1.3570 0.0504  0.1689  -0.0428 157 GLU D CB  
15168 C CG  . GLU D 157 ? 2.6641 1.0665 1.4093 0.0729  0.1667  -0.0333 157 GLU D CG  
15169 C CD  . GLU D 157 ? 2.6809 1.0681 1.4255 0.0434  0.1862  -0.0267 157 GLU D CD  
15170 O OE1 . GLU D 157 ? 2.6931 1.0261 1.4092 0.0140  0.2058  -0.0275 157 GLU D OE1 
15171 O OE2 . GLU D 157 ? 2.6187 1.0475 1.3914 0.0497  0.1827  -0.0210 157 GLU D OE2 
15178 N N   . THR D 158 ? 2.4545 1.0286 1.3746 -0.0133 0.1725  -0.0456 158 THR D N   
15179 C CA  . THR D 158 ? 2.4343 1.0428 1.3998 -0.0529 0.1838  -0.0479 158 THR D CA  
15180 C C   . THR D 158 ? 2.4979 1.1392 1.4866 -0.0523 0.1872  -0.0392 158 THR D C   
15181 O O   . THR D 158 ? 2.5004 1.1445 1.4754 -0.0214 0.1783  -0.0324 158 THR D O   
15182 C CB  . THR D 158 ? 2.4056 1.0843 1.4321 -0.0656 0.1723  -0.0574 158 THR D CB  
15183 O OG1 . THR D 158 ? 2.3683 1.0895 1.4440 -0.0993 0.1805  -0.0597 158 THR D OG1 
15184 C CG2 . THR D 158 ? 2.3679 1.1077 1.4262 -0.0346 0.1531  -0.0557 158 THR D CG2 
15192 N N   . SER D 159 ? 2.4827 1.1501 1.5081 -0.0867 0.1996  -0.0406 159 SER D N   
15193 C CA  . SER D 159 ? 2.3848 1.0945 1.4430 -0.0908 0.2028  -0.0338 159 SER D CA  
15194 C C   . SER D 159 ? 2.3282 1.1258 1.4619 -0.1057 0.1930  -0.0399 159 SER D C   
15195 O O   . SER D 159 ? 2.3622 1.1754 1.5207 -0.1283 0.1931  -0.0499 159 SER D O   
15196 C CB  . SER D 159 ? 2.4545 1.1194 1.4910 -0.1178 0.2279  -0.0299 159 SER D CB  
15197 O OG  . SER D 159 ? 2.4917 1.2162 1.5833 -0.1376 0.2325  -0.0292 159 SER D OG  
15203 N N   . PHE D 160 ? 2.2468 1.0998 1.4149 -0.0922 0.1838  -0.0346 160 PHE D N   
15204 C CA  . PHE D 160 ? 2.1311 1.0645 1.3669 -0.1048 0.1750  -0.0395 160 PHE D CA  
15205 C C   . PHE D 160 ? 2.1950 1.1386 1.4589 -0.1441 0.1894  -0.0455 160 PHE D C   
15206 O O   . PHE D 160 ? 2.1747 1.1469 1.4705 -0.1615 0.1847  -0.0559 160 PHE D O   
15207 C CB  . PHE D 160 ? 2.0208 1.0026 1.2835 -0.0872 0.1665  -0.0319 160 PHE D CB  
15208 C CG  . PHE D 160 ? 1.8935 0.9010 1.1607 -0.0537 0.1475  -0.0312 160 PHE D CG  
15209 C CD1 . PHE D 160 ? 1.8948 0.8603 1.1212 -0.0321 0.1419  -0.0329 160 PHE D CD1 
15210 C CD2 . PHE D 160 ? 1.8549 0.9280 1.1675 -0.0442 0.1362  -0.0292 160 PHE D CD2 
15211 C CE1 . PHE D 160 ? 1.8385 0.8308 1.0732 -0.0017 0.1258  -0.0333 160 PHE D CE1 
15212 C CE2 . PHE D 160 ? 1.7875 0.8855 1.1077 -0.0153 0.1207  -0.0295 160 PHE D CE2 
15213 C CZ  . PHE D 160 ? 1.7458 0.8050 1.0287 0.0059  0.1158  -0.0318 160 PHE D CZ  
15223 N N   . GLU D 161 ? 2.2928 1.2117 1.5442 -0.1581 0.2073  -0.0397 161 GLU D N   
15224 C CA  . GLU D 161 ? 2.2719 1.2036 1.5542 -0.1959 0.2229  -0.0461 161 GLU D CA  
15225 C C   . GLU D 161 ? 2.2962 1.1940 1.5679 -0.2184 0.2289  -0.0575 161 GLU D C   
15226 O O   . GLU D 161 ? 2.3175 1.2495 1.6328 -0.2463 0.2308  -0.0686 161 GLU D O   
15227 C CB  . GLU D 161 ? 2.3077 1.2036 1.5663 -0.2054 0.2449  -0.0374 161 GLU D CB  
15228 C CG  . GLU D 161 ? 2.3228 1.2383 1.6195 -0.2442 0.2629  -0.0443 161 GLU D CG  
15229 C CD  . GLU D 161 ? 2.2817 1.2856 1.6497 -0.2513 0.2508  -0.0494 161 GLU D CD  
15230 O OE1 . GLU D 161 ? 2.2645 1.2977 1.6743 -0.2809 0.2561  -0.0610 161 GLU D OE1 
15231 O OE2 . GLU D 161 ? 2.1952 1.2387 1.5774 -0.2272 0.2355  -0.0427 161 GLU D OE2 
15238 N N   . ASN D 162 ? 2.3019 1.1311 1.5151 -0.2061 0.2314  -0.0559 162 ASN D N   
15239 C CA  . ASN D 162 ? 2.3277 1.1205 1.5267 -0.2258 0.2358  -0.0671 162 ASN D CA  
15240 C C   . ASN D 162 ? 2.2623 1.1121 1.5070 -0.2281 0.2160  -0.0789 162 ASN D C   
15241 O O   . ASN D 162 ? 2.2515 1.1200 1.5292 -0.2575 0.2185  -0.0913 162 ASN D O   
15242 C CB  . ASN D 162 ? 2.3895 1.1011 1.5148 -0.2051 0.2382  -0.0624 162 ASN D CB  
15243 C CG  . ASN D 162 ? 2.4068 1.0907 1.5181 -0.2137 0.2336  -0.0739 162 ASN D CG  
15244 O OD1 . ASN D 162 ? 2.4415 1.1282 1.5761 -0.2471 0.2415  -0.0852 162 ASN D OD1 
15245 N ND2 . ASN D 162 ? 2.4287 1.0856 1.5021 -0.1832 0.2206  -0.0720 162 ASN D ND2 
15252 N N   . ILE D 163 ? 2.2561 1.1346 1.5038 -0.1969 0.1962  -0.0757 163 ILE D N   
15253 C CA  . ILE D 163 ? 2.2134 1.1439 1.5000 -0.1959 0.1780  -0.0857 163 ILE D CA  
15254 C C   . ILE D 163 ? 2.1500 1.1484 1.5004 -0.2184 0.1762  -0.0918 163 ILE D C   
15255 O O   . ILE D 163 ? 2.1077 1.1308 1.4876 -0.2359 0.1695  -0.1048 163 ILE D O   
15256 C CB  . ILE D 163 ? 2.1365 1.0905 1.4191 -0.1583 0.1606  -0.0797 163 ILE D CB  
15257 C CG1 . ILE D 163 ? 2.1544 1.0458 1.3792 -0.1376 0.1589  -0.0789 163 ILE D CG1 
15258 C CG2 . ILE D 163 ? 2.0264 1.0472 1.3576 -0.1571 0.1441  -0.0871 163 ILE D CG2 
15259 C CD1 . ILE D 163 ? 2.1144 1.0194 1.3293 -0.0995 0.1463  -0.0718 163 ILE D CD1 
15271 N N   . ILE D 164 ? 2.1145 1.1440 1.4861 -0.2162 0.1808  -0.0831 164 ILE D N   
15272 C CA  . ILE D 164 ? 2.0458 1.1413 1.4771 -0.2342 0.1785  -0.0882 164 ILE D CA  
15273 C C   . ILE D 164 ? 2.0634 1.1529 1.5144 -0.2710 0.1892  -0.1016 164 ILE D C   
15274 O O   . ILE D 164 ? 2.0237 1.1587 1.5176 -0.2842 0.1787  -0.1140 164 ILE D O   
15275 C CB  . ILE D 164 ? 2.0529 1.1684 1.4943 -0.2280 0.1858  -0.0762 164 ILE D CB  
15276 C CG1 . ILE D 164 ? 2.0123 1.1407 1.4413 -0.1917 0.1719  -0.0658 164 ILE D CG1 
15277 C CG2 . ILE D 164 ? 1.9915 1.1699 1.4919 -0.2481 0.1858  -0.0820 164 ILE D CG2 
15278 C CD1 . ILE D 164 ? 1.9415 1.1181 1.4007 -0.1836 0.1693  -0.0579 164 ILE D CD1 
15290 N N   . ASP D 165 ? 2.1197 1.1513 1.5386 -0.2878 0.2104  -0.1000 165 ASP D N   
15291 C CA  . ASP D 165 ? 2.1034 1.1266 1.5420 -0.3250 0.2228  -0.1139 165 ASP D CA  
15292 C C   . ASP D 165 ? 2.1407 1.1592 1.5811 -0.3308 0.2089  -0.1287 165 ASP D C   
15293 O O   . ASP D 165 ? 2.1224 1.1788 1.6079 -0.3532 0.2032  -0.1441 165 ASP D O   
15294 C CB  . ASP D 165 ? 2.1502 1.1010 1.5444 -0.3402 0.2499  -0.1087 165 ASP D CB  
15295 C CG  . ASP D 165 ? 2.1684 1.1114 1.5870 -0.3815 0.2660  -0.1237 165 ASP D CG  
15296 O OD1 . ASP D 165 ? 2.1561 1.1574 1.6331 -0.4009 0.2672  -0.1316 165 ASP D OD1 
15297 O OD2 . ASP D 165 ? 2.1596 1.0389 1.5402 -0.3947 0.2773  -0.1284 165 ASP D OD2 
15302 N N   . LEU D 166 ? 2.1645 1.1361 1.5553 -0.3095 0.2024  -0.1249 166 LEU D N   
15303 C CA  . LEU D 166 ? 2.1504 1.1122 1.5365 -0.3121 0.1890  -0.1382 166 LEU D CA  
15304 C C   . LEU D 166 ? 2.0921 1.1270 1.5295 -0.3077 0.1669  -0.1472 166 LEU D C   
15305 O O   . LEU D 166 ? 2.0920 1.1450 1.5578 -0.3283 0.1598  -0.1638 166 LEU D O   
15306 C CB  . LEU D 166 ? 2.2073 1.1155 1.5336 -0.2829 0.1838  -0.1307 166 LEU D CB  
15307 C CG  . LEU D 166 ? 2.3206 1.1467 1.5851 -0.2823 0.2031  -0.1223 166 LEU D CG  
15308 C CD1 . LEU D 166 ? 2.3903 1.1702 1.6009 -0.2522 0.1935  -0.1186 166 LEU D CD1 
15309 C CD2 . LEU D 166 ? 2.3916 1.1772 1.6519 -0.3206 0.2216  -0.1328 166 LEU D CD2 
15321 N N   . VAL D 167 ? 2.0863 1.1620 1.5347 -0.2806 0.1555  -0.1370 167 VAL D N   
15322 C CA  . VAL D 167 ? 2.0427 1.1842 1.5350 -0.2746 0.1360  -0.1440 167 VAL D CA  
15323 C C   . VAL D 167 ? 2.0388 1.2264 1.5854 -0.3033 0.1379  -0.1553 167 VAL D C   
15324 O O   . VAL D 167 ? 2.0612 1.2716 1.6343 -0.3166 0.1262  -0.1715 167 VAL D O   
15325 C CB  . VAL D 167 ? 1.9228 1.0988 1.4193 -0.2438 0.1279  -0.1301 167 VAL D CB  
15326 C CG1 . VAL D 167 ? 1.8155 1.0574 1.3565 -0.2398 0.1106  -0.1367 167 VAL D CG1 
15327 C CG2 . VAL D 167 ? 1.9144 1.0511 1.3632 -0.2146 0.1239  -0.1222 167 VAL D CG2 
15337 N N   . LYS D 168 ? 1.9941 1.1950 1.5573 -0.3127 0.1525  -0.1477 168 LYS D N   
15338 C CA  . LYS D 168 ? 1.9851 1.2331 1.6024 -0.3386 0.1555  -0.1582 168 LYS D CA  
15339 C C   . LYS D 168 ? 2.0065 1.2403 1.6375 -0.3693 0.1579  -0.1779 168 LYS D C   
15340 O O   . LYS D 168 ? 1.9985 1.2812 1.6790 -0.3851 0.1488  -0.1930 168 LYS D O   
15341 C CB  . LYS D 168 ? 1.9944 1.2397 1.6158 -0.3472 0.1767  -0.1473 168 LYS D CB  
15342 C CG  . LYS D 168 ? 1.9394 1.2042 1.5538 -0.3192 0.1735  -0.1297 168 LYS D CG  
15343 C CD  . LYS D 168 ? 1.9811 1.2227 1.5822 -0.3256 0.1962  -0.1180 168 LYS D CD  
15344 C CE  . LYS D 168 ? 2.0003 1.2737 1.6477 -0.3563 0.2090  -0.1272 168 LYS D CE  
15345 N NZ  . LYS D 168 ? 2.0305 1.2622 1.6710 -0.3876 0.2267  -0.1384 168 LYS D NZ  
15359 N N   . LYS D 169 ? 2.0416 1.2086 1.6296 -0.3779 0.1694  -0.1788 169 LYS D N   
15360 C CA  . LYS D 169 ? 2.0907 1.2400 1.6893 -0.4071 0.1709  -0.1985 169 LYS D CA  
15361 C C   . LYS D 169 ? 2.0951 1.2552 1.6941 -0.3968 0.1454  -0.2112 169 LYS D C   
15362 O O   . LYS D 169 ? 2.0933 1.2624 1.7182 -0.4195 0.1388  -0.2313 169 LYS D O   
15363 C CB  . LYS D 169 ? 2.1534 1.2221 1.7018 -0.4204 0.1930  -0.1951 169 LYS D CB  
15364 C CG  . LYS D 169 ? 2.1685 1.2216 1.7298 -0.4521 0.2218  -0.1957 169 LYS D CG  
15365 C CD  . LYS D 169 ? 2.1725 1.2937 1.8069 -0.4777 0.2218  -0.2104 169 LYS D CD  
15366 C CE  . LYS D 169 ? 2.1937 1.3420 1.8644 -0.4942 0.2030  -0.2349 169 LYS D CE  
15367 N NZ  . LYS D 169 ? 2.2062 1.4178 1.9486 -0.5204 0.2038  -0.2515 169 LYS D NZ  
15381 N N   . TYR D 170 ? 2.0753 1.2334 1.6459 -0.3632 0.1313  -0.2008 170 TYR D N   
15382 C CA  . TYR D 170 ? 2.0729 1.2522 1.6491 -0.3506 0.1069  -0.2118 170 TYR D CA  
15383 C C   . TYR D 170 ? 2.0788 1.3306 1.7147 -0.3580 0.0925  -0.2235 170 TYR D C   
15384 O O   . TYR D 170 ? 2.1034 1.3701 1.7618 -0.3717 0.0788  -0.2432 170 TYR D O   
15385 C CB  . TYR D 170 ? 2.0785 1.2495 1.6188 -0.3127 0.0979  -0.1971 170 TYR D CB  
15386 C CG  . TYR D 170 ? 2.1120 1.2879 1.6430 -0.2971 0.0764  -0.2066 170 TYR D CG  
15387 C CD1 . TYR D 170 ? 2.1794 1.3168 1.6622 -0.2710 0.0733  -0.1986 170 TYR D CD1 
15388 C CD2 . TYR D 170 ? 2.1567 1.3748 1.7250 -0.3065 0.0592  -0.2236 170 TYR D CD2 
15389 C CE1 . TYR D 170 ? 2.1626 1.3019 1.6340 -0.2560 0.0555  -0.2069 170 TYR D CE1 
15390 C CE2 . TYR D 170 ? 2.1448 1.3628 1.6994 -0.2908 0.0401  -0.2319 170 TYR D CE2 
15391 C CZ  . TYR D 170 ? 2.1223 1.3003 1.6280 -0.2660 0.0392  -0.2231 170 TYR D CZ  
15392 O OH  . TYR D 170 ? 2.1204 1.2959 1.6097 -0.2498 0.0220  -0.2310 170 TYR D OH  
15402 N N   . LEU D 171 ? 2.0576 1.3539 1.7183 -0.3480 0.0942  -0.2123 171 LEU D N   
15403 C CA  . LEU D 171 ? 2.0357 1.4000 1.7483 -0.3498 0.0795  -0.2217 171 LEU D CA  
15404 C C   . LEU D 171 ? 2.0602 1.4488 1.8202 -0.3838 0.0844  -0.2396 171 LEU D C   
15405 O O   . LEU D 171 ? 2.0657 1.5122 1.8716 -0.3863 0.0725  -0.2489 171 LEU D O   
15406 C CB  . LEU D 171 ? 2.0006 1.4013 1.7248 -0.3313 0.0822  -0.2045 171 LEU D CB  
15407 C CG  . LEU D 171 ? 1.9315 1.3224 1.6211 -0.2975 0.0776  -0.1870 171 LEU D CG  
15408 C CD1 . LEU D 171 ? 1.9461 1.3372 1.6207 -0.2798 0.0577  -0.1939 171 LEU D CD1 
15409 C CD2 . LEU D 171 ? 1.9256 1.2583 1.5683 -0.2911 0.0945  -0.1728 171 LEU D CD2 
15421 N N   . SER D 172 ? 2.0718 1.4179 1.8222 -0.4098 0.1022  -0.2452 172 SER D N   
15422 C CA  . SER D 172 ? 2.0966 1.4658 1.8954 -0.4443 0.1078  -0.2648 172 SER D CA  
15423 C C   . SER D 172 ? 2.1452 1.5532 1.9779 -0.4476 0.0809  -0.2883 172 SER D C   
15424 O O   . SER D 172 ? 2.1240 1.5841 2.0123 -0.4637 0.0757  -0.3036 172 SER D O   
15425 C CB  . SER D 172 ? 2.1023 1.4095 1.8772 -0.4710 0.1301  -0.2685 172 SER D CB  
15426 O OG  . SER D 172 ? 2.1095 1.3737 1.8505 -0.4690 0.1189  -0.2775 172 SER D OG  
15432 N N   . ASN D 173 ? 2.2138 1.5963 2.0125 -0.4311 0.0632  -0.2919 173 ASN D N   
15433 C CA  . ASN D 173 ? 2.1905 1.6023 2.0129 -0.4312 0.0360  -0.3143 173 ASN D CA  
15434 C C   . ASN D 173 ? 2.2149 1.6850 2.0595 -0.4067 0.0162  -0.3119 173 ASN D C   
15435 O O   . ASN D 173 ? 2.1945 1.7105 2.0810 -0.4127 -0.0021 -0.3312 173 ASN D O   
15436 C CB  . ASN D 173 ? 2.2226 1.5825 1.9957 -0.4203 0.0248  -0.3182 173 ASN D CB  
15437 C CG  . ASN D 173 ? 2.2796 1.5709 2.0153 -0.4371 0.0461  -0.3145 173 ASN D CG  
15438 O OD1 . ASN D 173 ? 2.3355 1.6104 2.0864 -0.4670 0.0505  -0.3325 173 ASN D OD1 
15439 N ND2 . ASN D 173 ? 2.2546 1.5045 1.9408 -0.4176 0.0592  -0.2919 173 ASN D ND2 
15446 N N   . GLU D 174 ? 2.3430 1.8107 2.1593 -0.3788 0.0192  -0.2893 174 GLU D N   
15447 C CA  . GLU D 174 ? 2.2846 1.7980 2.1121 -0.3534 0.0018  -0.2851 174 GLU D CA  
15448 C C   . GLU D 174 ? 2.2095 1.7752 2.0820 -0.3592 0.0084  -0.2810 174 GLU D C   
15449 O O   . GLU D 174 ? 2.2218 1.7792 2.0966 -0.3689 0.0307  -0.2684 174 GLU D O   
15450 C CB  . GLU D 174 ? 2.3303 1.8178 2.1096 -0.3221 0.0034  -0.2636 174 GLU D CB  
15451 C CG  . GLU D 174 ? 2.3070 1.8367 2.0943 -0.2963 -0.0093 -0.2557 174 GLU D CG  
15452 C CD  . GLU D 174 ? 2.3195 1.8221 2.0602 -0.2668 -0.0121 -0.2417 174 GLU D CD  
15453 O OE1 . GLU D 174 ? 2.3387 1.8234 2.0586 -0.2565 0.0031  -0.2227 174 GLU D OE1 
15454 O OE2 . GLU D 174 ? 2.2566 1.7559 1.9818 -0.2533 -0.0295 -0.2505 174 GLU D OE2 
15461 N N   . GLU D 175 ? 1.9859 1.6031 1.8914 -0.3519 -0.0113 -0.2921 175 GLU D N   
15462 C CA  . GLU D 175 ? 1.8696 1.5384 1.8134 -0.3508 -0.0083 -0.2873 175 GLU D CA  
15463 C C   . GLU D 175 ? 1.8625 1.5355 1.7796 -0.3200 -0.0096 -0.2654 175 GLU D C   
15464 O O   . GLU D 175 ? 1.8436 1.5175 1.7403 -0.2976 -0.0270 -0.2658 175 GLU D O   
15465 C CB  . GLU D 175 ? 1.7224 1.4438 1.7134 -0.3563 -0.0296 -0.3105 175 GLU D CB  
15466 C CG  . GLU D 175 ? 1.6666 1.4422 1.6889 -0.3453 -0.0331 -0.3051 175 GLU D CG  
15467 C CD  . GLU D 175 ? 1.6290 1.4088 1.6617 -0.3539 -0.0069 -0.2877 175 GLU D CD  
15468 O OE1 . GLU D 175 ? 1.6494 1.3948 1.6731 -0.3730 0.0147  -0.2831 175 GLU D OE1 
15469 O OE2 . GLU D 175 ? 1.5971 1.4122 1.6441 -0.3409 -0.0080 -0.2785 175 GLU D OE2 
15476 N N   . TYR D 176 ? 1.8521 1.5260 1.7687 -0.3189 0.0095  -0.2469 176 TYR D N   
15477 C CA  . TYR D 176 ? 1.8186 1.4915 1.7096 -0.2920 0.0110  -0.2258 176 TYR D CA  
15478 C C   . TYR D 176 ? 1.7520 1.4541 1.6670 -0.2941 0.0240  -0.2140 176 TYR D C   
15479 O O   . TYR D 176 ? 1.7515 1.4556 1.6881 -0.3161 0.0392  -0.2167 176 TYR D O   
15480 C CB  . TYR D 176 ? 1.8970 1.5147 1.7385 -0.2824 0.0218  -0.2117 176 TYR D CB  
15481 C CG  . TYR D 176 ? 1.8798 1.4689 1.7126 -0.2957 0.0458  -0.2006 176 TYR D CG  
15482 C CD1 . TYR D 176 ? 1.8848 1.4706 1.7034 -0.2812 0.0570  -0.1804 176 TYR D CD1 
15483 C CD2 . TYR D 176 ? 1.9033 1.4665 1.7404 -0.3227 0.0573  -0.2108 176 TYR D CD2 
15484 C CE1 . TYR D 176 ? 1.8668 1.4224 1.6722 -0.2911 0.0780  -0.1703 176 TYR D CE1 
15485 C CE2 . TYR D 176 ? 1.9104 1.4418 1.7339 -0.3341 0.0807  -0.2000 176 TYR D CE2 
15486 C CZ  . TYR D 176 ? 1.8618 1.3887 1.6677 -0.3172 0.0905  -0.1796 176 TYR D CZ  
15487 O OH  . TYR D 176 ? 1.8354 1.3268 1.6228 -0.3263 0.1128  -0.1692 176 TYR D OH  
15497 N N   . SER D 177 ? 1.7722 1.4950 1.6818 -0.2712 0.0187  -0.2012 177 SER D N   
15498 C CA  . SER D 177 ? 1.7259 1.4751 1.6540 -0.2696 0.0290  -0.1891 177 SER D CA  
15499 C C   . SER D 177 ? 1.8065 1.5228 1.7038 -0.2612 0.0461  -0.1683 177 SER D C   
15500 O O   . SER D 177 ? 1.7799 1.5035 1.6881 -0.2672 0.0600  -0.1597 177 SER D O   
15501 C CB  . SER D 177 ? 1.5846 1.3748 1.5251 -0.2501 0.0137  -0.1874 177 SER D CB  
15502 O OG  . SER D 177 ? 1.5938 1.3704 1.5041 -0.2272 0.0152  -0.1698 177 SER D OG  
15508 N N   . ALA D 178 ? 1.9797 1.6599 1.8381 -0.2463 0.0448  -0.1610 178 ALA D N   
15509 C CA  . ALA D 178 ? 1.9542 1.6032 1.7824 -0.2353 0.0582  -0.1430 178 ALA D CA  
15510 C C   . ALA D 178 ? 1.9497 1.5575 1.7384 -0.2228 0.0551  -0.1413 178 ALA D C   
15511 O O   . ALA D 178 ? 1.9784 1.5881 1.7622 -0.2169 0.0414  -0.1506 178 ALA D O   
15512 C CB  . ALA D 178 ? 1.8920 1.5692 1.7262 -0.2166 0.0567  -0.1293 178 ALA D CB  
15518 N N   . PHE D 179 ? 1.7867 1.3556 1.5451 -0.2173 0.0676  -0.1295 179 PHE D N   
15519 C CA  . PHE D 179 ? 1.7371 1.2652 1.4563 -0.2032 0.0663  -0.1267 179 PHE D CA  
15520 C C   . PHE D 179 ? 1.6911 1.2000 1.3867 -0.1856 0.0751  -0.1101 179 PHE D C   
15521 O O   . PHE D 179 ? 1.7084 1.2329 1.4165 -0.1857 0.0820  -0.1014 179 PHE D O   
15522 C CB  . PHE D 179 ? 1.7176 1.2033 1.4191 -0.2212 0.0711  -0.1371 179 PHE D CB  
15523 C CG  . PHE D 179 ? 1.6967 1.1405 1.3766 -0.2307 0.0895  -0.1297 179 PHE D CG  
15524 C CD1 . PHE D 179 ? 1.7429 1.1944 1.4447 -0.2529 0.1020  -0.1313 179 PHE D CD1 
15525 C CD2 . PHE D 179 ? 1.6967 1.0915 1.3323 -0.2166 0.0949  -0.1216 179 PHE D CD2 
15526 C CE1 . PHE D 179 ? 1.7708 1.1781 1.4473 -0.2613 0.1207  -0.1241 179 PHE D CE1 
15527 C CE2 . PHE D 179 ? 1.7208 1.0716 1.3305 -0.2235 0.1115  -0.1148 179 PHE D CE2 
15528 C CZ  . PHE D 179 ? 1.7477 1.1030 1.3761 -0.2461 0.1249  -0.1156 179 PHE D CZ  
15538 N N   . GLY D 180 ? 1.6544 1.1298 1.3159 -0.1692 0.0740  -0.1067 180 GLY D N   
15539 C CA  . GLY D 180 ? 1.6286 1.0863 1.2678 -0.1496 0.0797  -0.0932 180 GLY D CA  
15540 C C   . GLY D 180 ? 1.6312 1.0353 1.2279 -0.1411 0.0831  -0.0929 180 GLY D C   
15541 O O   . GLY D 180 ? 1.6187 1.0041 1.2026 -0.1448 0.0784  -0.1023 180 GLY D O   
15545 N N   . ILE D 181 ? 1.6565 1.0341 1.2295 -0.1284 0.0904  -0.0825 181 ILE D N   
15546 C CA  . ILE D 181 ? 1.6278 0.9525 1.1568 -0.1158 0.0935  -0.0808 181 ILE D CA  
15547 C C   . ILE D 181 ? 1.6171 0.9477 1.1376 -0.0871 0.0905  -0.0710 181 ILE D C   
15548 O O   . ILE D 181 ? 1.6097 0.9452 1.1331 -0.0826 0.0946  -0.0626 181 ILE D O   
15549 C CB  . ILE D 181 ? 1.6574 0.9307 1.1582 -0.1311 0.1069  -0.0799 181 ILE D CB  
15550 C CG1 . ILE D 181 ? 1.6754 0.9529 1.1960 -0.1629 0.1113  -0.0906 181 ILE D CG1 
15551 C CG2 . ILE D 181 ? 1.7092 0.9246 1.1611 -0.1174 0.1086  -0.0797 181 ILE D CG2 
15552 C CD1 . ILE D 181 ? 1.7957 1.0131 1.2831 -0.1799 0.1243  -0.0939 181 ILE D CD1 
15564 N N   . MET D 182 ? 1.6157 0.9463 1.1265 -0.0676 0.0835  -0.0729 182 MET D N   
15565 C CA  . MET D 182 ? 1.5920 0.9314 1.0990 -0.0400 0.0803  -0.0660 182 MET D CA  
15566 C C   . MET D 182 ? 1.6352 0.9189 1.0969 -0.0257 0.0838  -0.0641 182 MET D C   
15567 O O   . MET D 182 ? 1.7273 0.9858 1.1657 -0.0161 0.0817  -0.0689 182 MET D O   
15568 C CB  . MET D 182 ? 1.5854 0.9574 1.1089 -0.0263 0.0728  -0.0694 182 MET D CB  
15569 C CG  . MET D 182 ? 1.5051 0.9266 1.0669 -0.0383 0.0687  -0.0719 182 MET D CG  
15570 S SD  . MET D 182 ? 1.4662 0.9306 1.0632 -0.0429 0.0695  -0.0638 182 MET D SD  
15571 C CE  . MET D 182 ? 1.5230 0.9912 1.1342 -0.0744 0.0721  -0.0691 182 MET D CE  
15581 N N   . PHE D 183 ? 1.6644 0.9255 1.1102 -0.0233 0.0891  -0.0572 183 PHE D N   
15582 C CA  . PHE D 183 ? 1.7064 0.9122 1.1053 -0.0063 0.0916  -0.0547 183 PHE D CA  
15583 C C   . PHE D 183 ? 1.6984 0.9215 1.0997 0.0257  0.0829  -0.0532 183 PHE D C   
15584 O O   . PHE D 183 ? 1.7099 0.9567 1.1262 0.0383  0.0795  -0.0479 183 PHE D O   
15585 C CB  . PHE D 183 ? 1.7164 0.8923 1.0958 -0.0129 0.1002  -0.0478 183 PHE D CB  
15586 C CG  . PHE D 183 ? 1.7265 0.8803 1.1018 -0.0448 0.1117  -0.0503 183 PHE D CG  
15587 C CD1 . PHE D 183 ? 1.7887 0.8819 1.1223 -0.0533 0.1196  -0.0536 183 PHE D CD1 
15588 C CD2 . PHE D 183 ? 1.7101 0.9041 1.1243 -0.0665 0.1150  -0.0501 183 PHE D CD2 
15589 C CE1 . PHE D 183 ? 1.8289 0.9033 1.1625 -0.0846 0.1315  -0.0573 183 PHE D CE1 
15590 C CE2 . PHE D 183 ? 1.7446 0.9223 1.1601 -0.0964 0.1262  -0.0540 183 PHE D CE2 
15591 C CZ  . PHE D 183 ? 1.8112 0.9298 1.1879 -0.1063 0.1349  -0.0579 183 PHE D CZ  
15601 N N   . PHE D 184 ? 1.7428 0.9537 1.1298 0.0390  0.0794  -0.0586 184 PHE D N   
15602 C CA  . PHE D 184 ? 1.7774 1.0165 1.1780 0.0660  0.0723  -0.0597 184 PHE D CA  
15603 C C   . PHE D 184 ? 1.8312 1.0253 1.1904 0.0922  0.0703  -0.0602 184 PHE D C   
15604 O O   . PHE D 184 ? 1.8677 1.0138 1.1889 0.0918  0.0730  -0.0638 184 PHE D O   
15605 C CB  . PHE D 184 ? 1.7270 0.9919 1.1458 0.0630  0.0705  -0.0660 184 PHE D CB  
15606 C CG  . PHE D 184 ? 1.7206 0.9897 1.1348 0.0906  0.0672  -0.0694 184 PHE D CG  
15607 C CD1 . PHE D 184 ? 1.7042 1.0157 1.1486 0.1091  0.0638  -0.0678 184 PHE D CD1 
15608 C CD2 . PHE D 184 ? 1.8274 1.0588 1.2086 0.0977  0.0680  -0.0750 184 PHE D CD2 
15609 C CE1 . PHE D 184 ? 1.7280 1.0466 1.1725 0.1338  0.0623  -0.0720 184 PHE D CE1 
15610 C CE2 . PHE D 184 ? 1.7784 1.0149 1.1563 0.1238  0.0662  -0.0785 184 PHE D CE2 
15611 C CZ  . PHE D 184 ? 1.7180 0.9995 1.1292 0.1417  0.0639  -0.0772 184 PHE D CZ  
15621 N N   . ASP D 185 ? 1.8151 1.0251 1.1821 0.1158  0.0645  -0.0577 185 ASP D N   
15622 C CA  . ASP D 185 ? 1.8659 1.0406 1.1983 0.1456  0.0600  -0.0594 185 ASP D CA  
15623 C C   . ASP D 185 ? 1.8756 1.0838 1.2298 0.1673  0.0551  -0.0656 185 ASP D C   
15624 O O   . ASP D 185 ? 1.8692 1.1328 1.2678 0.1731  0.0517  -0.0660 185 ASP D O   
15625 C CB  . ASP D 185 ? 1.9510 1.1217 1.2778 0.1601  0.0550  -0.0546 185 ASP D CB  
15626 C CG  . ASP D 185 ? 2.0677 1.2041 1.3594 0.1944  0.0477  -0.0576 185 ASP D CG  
15627 O OD1 . ASP D 185 ? 2.0799 1.2418 1.3885 0.2158  0.0419  -0.0639 185 ASP D OD1 
15628 O OD2 . ASP D 185 ? 2.1349 1.2177 1.3811 0.2008  0.0481  -0.0541 185 ASP D OD2 
15633 N N   . SER D 186 ? 1.9499 1.1226 1.2719 0.1793  0.0558  -0.0706 186 SER D N   
15634 C CA  . SER D 186 ? 1.9223 1.1237 1.2627 0.1991  0.0538  -0.0769 186 SER D CA  
15635 C C   . SER D 186 ? 1.9704 1.1879 1.3199 0.2318  0.0461  -0.0796 186 SER D C   
15636 O O   . SER D 186 ? 1.9194 1.1814 1.3038 0.2457  0.0452  -0.0845 186 SER D O   
15637 C CB  . SER D 186 ? 1.9550 1.1111 1.2557 0.2025  0.0570  -0.0819 186 SER D CB  
15638 O OG  . SER D 186 ? 2.0152 1.1352 1.2810 0.2325  0.0526  -0.0850 186 SER D OG  
15644 N N   . ASP D 187 ? 2.0008 1.1818 1.3189 0.2450  0.0406  -0.0774 187 ASP D N   
15645 C CA  . ASP D 187 ? 2.0499 1.2443 1.3748 0.2785  0.0304  -0.0818 187 ASP D CA  
15646 C C   . ASP D 187 ? 2.0524 1.3097 1.4323 0.2772  0.0257  -0.0809 187 ASP D C   
15647 O O   . ASP D 187 ? 2.0199 1.3219 1.4367 0.2964  0.0209  -0.0875 187 ASP D O   
15648 C CB  . ASP D 187 ? 2.0977 1.2284 1.3660 0.2946  0.0249  -0.0799 187 ASP D CB  
15649 C CG  . ASP D 187 ? 2.1361 1.1969 1.3458 0.2881  0.0317  -0.0790 187 ASP D CG  
15650 O OD1 . ASP D 187 ? 2.1563 1.1970 1.3448 0.3084  0.0302  -0.0852 187 ASP D OD1 
15651 O OD2 . ASP D 187 ? 2.1593 1.1851 1.3448 0.2624  0.0392  -0.0725 187 ASP D OD2 
15656 N N   . ASN D 188 ? 2.1748 1.4365 1.5618 0.2545  0.0277  -0.0734 188 ASN D N   
15657 C CA  . ASN D 188 ? 2.0772 1.3939 1.5125 0.2511  0.0233  -0.0719 188 ASN D CA  
15658 C C   . ASN D 188 ? 2.0583 1.4259 1.5398 0.2270  0.0309  -0.0706 188 ASN D C   
15659 O O   . ASN D 188 ? 2.0465 1.4603 1.5690 0.2219  0.0285  -0.0692 188 ASN D O   
15660 C CB  . ASN D 188 ? 2.0713 1.3634 1.4867 0.2422  0.0211  -0.0643 188 ASN D CB  
15661 C CG  . ASN D 188 ? 2.2893 1.5090 1.6404 0.2558  0.0191  -0.0628 188 ASN D CG  
15662 O OD1 . ASN D 188 ? 2.3167 1.5162 1.6461 0.2852  0.0115  -0.0688 188 ASN D OD1 
15663 N ND2 . ASN D 188 ? 2.2948 1.4742 1.6146 0.2349  0.0268  -0.0551 188 ASN D ND2 
15670 N N   . LEU D 189 ? 1.8991 1.2571 1.3725 0.2132  0.0393  -0.0714 189 LEU D N   
15671 C CA  . LEU D 189 ? 1.8024 1.1994 1.3103 0.1897  0.0461  -0.0698 189 LEU D CA  
15672 C C   . LEU D 189 ? 1.7220 1.1320 1.2440 0.1670  0.0463  -0.0627 189 LEU D C   
15673 O O   . LEU D 189 ? 1.6150 1.0711 1.1766 0.1554  0.0478  -0.0613 189 LEU D O   
15674 C CB  . LEU D 189 ? 1.7527 1.2044 1.3059 0.2012  0.0469  -0.0748 189 LEU D CB  
15675 C CG  . LEU D 189 ? 1.7123 1.1562 1.2558 0.2210  0.0497  -0.0822 189 LEU D CG  
15676 C CD1 . LEU D 189 ? 1.6725 1.1632 1.2569 0.2423  0.0481  -0.0886 189 LEU D CD1 
15677 C CD2 . LEU D 189 ? 1.6214 1.0631 1.1607 0.2052  0.0589  -0.0826 189 LEU D CD2 
15689 N N   . SER D 190 ? 1.7724 1.1389 1.2595 0.1612  0.0459  -0.0583 190 SER D N   
15690 C CA  . SER D 190 ? 1.7055 1.0771 1.2001 0.1403  0.0478  -0.0517 190 SER D CA  
15691 C C   . SER D 190 ? 1.6659 1.0264 1.1552 0.1111  0.0560  -0.0505 190 SER D C   
15692 O O   . SER D 190 ? 1.6878 1.0174 1.1520 0.1076  0.0594  -0.0541 190 SER D O   
15693 C CB  . SER D 190 ? 1.7869 1.1144 1.2445 0.1491  0.0452  -0.0476 190 SER D CB  
15694 O OG  . SER D 190 ? 1.7661 1.0418 1.1842 0.1317  0.0534  -0.0448 190 SER D OG  
15700 N N   . MET D 191 ? 1.6007 0.9873 1.1145 0.0906  0.0582  -0.0464 191 MET D N   
15701 C CA  . MET D 191 ? 1.5743 0.9565 1.0891 0.0625  0.0645  -0.0466 191 MET D CA  
15702 C C   . MET D 191 ? 1.5685 0.9559 1.0916 0.0461  0.0675  -0.0408 191 MET D C   
15703 O O   . MET D 191 ? 1.5011 0.9288 1.0554 0.0476  0.0641  -0.0377 191 MET D O   
15704 C CB  . MET D 191 ? 1.4986 0.9239 1.0467 0.0550  0.0639  -0.0505 191 MET D CB  
15705 C CG  . MET D 191 ? 1.5703 0.9810 1.1097 0.0337  0.0674  -0.0549 191 MET D CG  
15706 S SD  . MET D 191 ? 1.5083 0.9707 1.0887 0.0152  0.0661  -0.0569 191 MET D SD  
15707 C CE  . MET D 191 ? 1.4248 0.9337 1.0358 0.0357  0.0633  -0.0553 191 MET D CE  
15717 N N   . LYS D 192 ? 1.5601 0.9055 1.0548 0.0304  0.0747  -0.0395 192 LYS D N   
15718 C CA  . LYS D 192 ? 1.5858 0.9344 1.0879 0.0122  0.0804  -0.0345 192 LYS D CA  
15719 C C   . LYS D 192 ? 1.5558 0.9249 1.0811 -0.0154 0.0846  -0.0387 192 LYS D C   
15720 O O   . LYS D 192 ? 1.5343 0.8707 1.0399 -0.0303 0.0904  -0.0431 192 LYS D O   
15721 C CB  . LYS D 192 ? 1.6143 0.9029 1.0708 0.0115  0.0881  -0.0306 192 LYS D CB  
15722 C CG  . LYS D 192 ? 1.6320 0.9121 1.0753 0.0323  0.0841  -0.0244 192 LYS D CG  
15723 C CD  . LYS D 192 ? 1.6454 0.9265 1.0815 0.0639  0.0728  -0.0270 192 LYS D CD  
15724 C CE  . LYS D 192 ? 1.7354 1.0433 1.1876 0.0829  0.0636  -0.0238 192 LYS D CE  
15725 N NZ  . LYS D 192 ? 1.6841 1.0158 1.1506 0.1098  0.0519  -0.0289 192 LYS D NZ  
15739 N N   . PRO D 193 ? 1.5236 0.9452 1.0898 -0.0224 0.0810  -0.0386 193 PRO D N   
15740 C CA  . PRO D 193 ? 1.5426 0.9851 1.1307 -0.0454 0.0823  -0.0443 193 PRO D CA  
15741 C C   . PRO D 193 ? 1.5297 0.9649 1.1213 -0.0688 0.0909  -0.0434 193 PRO D C   
15742 O O   . PRO D 193 ? 1.5300 0.9947 1.1450 -0.0737 0.0917  -0.0393 193 PRO D O   
15743 C CB  . PRO D 193 ? 1.4554 0.9536 1.0816 -0.0400 0.0751  -0.0441 193 PRO D CB  
15744 C CG  . PRO D 193 ? 1.4455 0.9556 1.0765 -0.0218 0.0724  -0.0371 193 PRO D CG  
15745 C CD  . PRO D 193 ? 1.4968 0.9601 1.0902 -0.0077 0.0744  -0.0346 193 PRO D CD  
15753 N N   . TYR D 194 ? 1.5482 0.9435 1.1168 -0.0839 0.0984  -0.0478 194 TYR D N   
15754 C CA  . TYR D 194 ? 1.6018 0.9927 1.1788 -0.1099 0.1085  -0.0496 194 TYR D CA  
15755 C C   . TYR D 194 ? 1.5880 1.0208 1.2027 -0.1274 0.1035  -0.0586 194 TYR D C   
15756 O O   . TYR D 194 ? 1.6278 1.0664 1.2448 -0.1254 0.0955  -0.0660 194 TYR D O   
15757 C CB  . TYR D 194 ? 1.7002 1.0310 1.2391 -0.1211 0.1196  -0.0519 194 TYR D CB  
15758 C CG  . TYR D 194 ? 1.7387 1.0667 1.2910 -0.1517 0.1316  -0.0567 194 TYR D CG  
15759 C CD1 . TYR D 194 ? 1.7692 1.0845 1.3163 -0.1599 0.1448  -0.0500 194 TYR D CD1 
15760 C CD2 . TYR D 194 ? 1.7314 1.0700 1.3025 -0.1721 0.1298  -0.0689 194 TYR D CD2 
15761 C CE1 . TYR D 194 ? 1.7735 1.0883 1.3360 -0.1886 0.1579  -0.0551 194 TYR D CE1 
15762 C CE2 . TYR D 194 ? 1.7381 1.0784 1.3271 -0.2008 0.1407  -0.0753 194 TYR D CE2 
15763 C CZ  . TYR D 194 ? 1.7961 1.1255 1.3821 -0.2095 0.1557  -0.0683 194 TYR D CZ  
15764 O OH  . TYR D 194 ? 1.8073 1.1398 1.4137 -0.2386 0.1688  -0.0753 194 TYR D OH  
15774 N N   . VAL D 195 ? 1.6054 1.0661 1.2482 -0.1434 0.1079  -0.0586 195 VAL D N   
15775 C CA  . VAL D 195 ? 1.5961 1.0990 1.2764 -0.1590 0.1022  -0.0679 195 VAL D CA  
15776 C C   . VAL D 195 ? 1.6651 1.1657 1.3590 -0.1851 0.1141  -0.0721 195 VAL D C   
15777 O O   . VAL D 195 ? 1.6910 1.1673 1.3702 -0.1890 0.1272  -0.0650 195 VAL D O   
15778 C CB  . VAL D 195 ? 1.5293 1.0843 1.2395 -0.1471 0.0924  -0.0642 195 VAL D CB  
15779 C CG1 . VAL D 195 ? 1.5205 1.1153 1.2646 -0.1604 0.0850  -0.0746 195 VAL D CG1 
15780 C CG2 . VAL D 195 ? 1.5018 1.0581 1.1998 -0.1222 0.0838  -0.0601 195 VAL D CG2 
15790 N N   . TYR D 196 ? 1.6527 1.1784 1.3748 -0.2027 0.1097  -0.0847 196 TYR D N   
15791 C CA  . TYR D 196 ? 1.6960 1.2239 1.4376 -0.2297 0.1209  -0.0921 196 TYR D CA  
15792 C C   . TYR D 196 ? 1.7226 1.3032 1.5084 -0.2396 0.1096  -0.1044 196 TYR D C   
15793 O O   . TYR D 196 ? 1.7331 1.3300 1.5237 -0.2309 0.0941  -0.1109 196 TYR D O   
15794 C CB  . TYR D 196 ? 1.6996 1.1769 1.4160 -0.2458 0.1307  -0.0989 196 TYR D CB  
15795 C CG  . TYR D 196 ? 1.7515 1.2257 1.4869 -0.2758 0.1461  -0.1069 196 TYR D CG  
15796 C CD1 . TYR D 196 ? 1.7422 1.2451 1.5139 -0.2961 0.1404  -0.1240 196 TYR D CD1 
15797 C CD2 . TYR D 196 ? 1.7788 1.2197 1.4952 -0.2837 0.1668  -0.0982 196 TYR D CD2 
15798 C CE1 . TYR D 196 ? 1.7559 1.2592 1.5501 -0.3249 0.1556  -0.1330 196 TYR D CE1 
15799 C CE2 . TYR D 196 ? 1.7718 1.2089 1.5064 -0.3125 0.1840  -0.1058 196 TYR D CE2 
15800 C CZ  . TYR D 196 ? 1.7850 1.2553 1.5610 -0.3337 0.1787  -0.1235 196 TYR D CZ  
15801 O OH  . TYR D 196 ? 1.7658 1.2356 1.5648 -0.3634 0.1968  -0.1325 196 TYR D OH  
15811 N N   . VAL D 197 ? 1.7481 1.3541 1.5645 -0.2566 0.1175  -0.1078 197 VAL D N   
15812 C CA  . VAL D 197 ? 1.7519 1.4086 1.6123 -0.2666 0.1071  -0.1211 197 VAL D CA  
15813 C C   . VAL D 197 ? 1.7643 1.4228 1.6493 -0.2956 0.1211  -0.1317 197 VAL D C   
15814 O O   . VAL D 197 ? 1.7416 1.3805 1.6190 -0.3044 0.1404  -0.1240 197 VAL D O   
15815 C CB  . VAL D 197 ? 1.7062 1.4083 1.5880 -0.2520 0.0996  -0.1140 197 VAL D CB  
15816 C CG1 . VAL D 197 ? 1.7028 1.4516 1.6186 -0.2531 0.0823  -0.1277 197 VAL D CG1 
15817 C CG2 . VAL D 197 ? 1.6732 1.3640 1.5270 -0.2256 0.0943  -0.0995 197 VAL D CG2 
15827 N N   . LYS D 198 ? 1.7879 1.4696 1.7023 -0.3103 0.1116  -0.1502 198 LYS D N   
15828 C CA  . LYS D 198 ? 1.7788 1.4678 1.7239 -0.3397 0.1246  -0.1634 198 LYS D CA  
15829 C C   . LYS D 198 ? 1.7544 1.4776 1.7290 -0.3444 0.1355  -0.1589 198 LYS D C   
15830 O O   . LYS D 198 ? 1.7454 1.4513 1.7221 -0.3625 0.1580  -0.1571 198 LYS D O   
15831 C CB  . LYS D 198 ? 1.7888 1.5067 1.7665 -0.3511 0.1076  -0.1859 198 LYS D CB  
15832 C CG  . LYS D 198 ? 1.8108 1.5262 1.8167 -0.3841 0.1208  -0.2028 198 LYS D CG  
15833 C CD  . LYS D 198 ? 1.7932 1.5573 1.8487 -0.3973 0.1288  -0.2090 198 LYS D CD  
15834 C CE  . LYS D 198 ? 1.7987 1.5717 1.8930 -0.4305 0.1381  -0.2306 198 LYS D CE  
15835 N NZ  . LYS D 198 ? 1.7968 1.6071 1.9248 -0.4329 0.1123  -0.2539 198 LYS D NZ  
15849 N N   . GLU D 199 ? 1.7391 1.5085 1.7342 -0.3281 0.1208  -0.1570 199 GLU D N   
15850 C CA  . GLU D 199 ? 1.7194 1.5230 1.7426 -0.3309 0.1296  -0.1535 199 GLU D CA  
15851 C C   . GLU D 199 ? 1.7066 1.4770 1.6982 -0.3246 0.1487  -0.1336 199 GLU D C   
15852 O O   . GLU D 199 ? 1.6991 1.4788 1.7061 -0.3349 0.1651  -0.1311 199 GLU D O   
15853 C CB  . GLU D 199 ? 1.6938 1.5472 1.7380 -0.3119 0.1088  -0.1545 199 GLU D CB  
15854 C CG  . GLU D 199 ? 1.6861 1.5866 1.7762 -0.3220 0.0947  -0.1761 199 GLU D CG  
15855 C CD  . GLU D 199 ? 1.6528 1.6042 1.7743 -0.3135 0.0886  -0.1766 199 GLU D CD  
15856 O OE1 . GLU D 199 ? 1.6605 1.6126 1.7638 -0.2941 0.0875  -0.1603 199 GLU D OE1 
15857 O OE2 . GLU D 199 ? 1.6189 1.6099 1.7839 -0.3259 0.0843  -0.1941 199 GLU D OE2 
15864 N N   . VAL D 200 ? 1.7315 1.4630 1.6787 -0.3067 0.1464  -0.1201 200 VAL D N   
15865 C CA  . VAL D 200 ? 1.7120 1.4067 1.6250 -0.2993 0.1627  -0.1027 200 VAL D CA  
15866 C C   . VAL D 200 ? 1.7150 1.3616 1.6091 -0.3205 0.1859  -0.1039 200 VAL D C   
15867 O O   . VAL D 200 ? 1.6969 1.3235 1.5788 -0.3253 0.2056  -0.0950 200 VAL D O   
15868 C CB  . VAL D 200 ? 1.6840 1.3553 1.5588 -0.2724 0.1515  -0.0899 200 VAL D CB  
15869 C CG1 . VAL D 200 ? 1.7034 1.3298 1.5385 -0.2641 0.1666  -0.0742 200 VAL D CG1 
15870 C CG2 . VAL D 200 ? 1.6539 1.3702 1.5464 -0.2528 0.1331  -0.0870 200 VAL D CG2 
15880 N N   . GLY D 201 ? 1.7199 1.3441 1.6086 -0.3334 0.1847  -0.1150 201 GLY D N   
15881 C CA  . GLY D 201 ? 1.7262 1.2981 1.5918 -0.3536 0.2070  -0.1162 201 GLY D CA  
15882 C C   . GLY D 201 ? 1.7343 1.2438 1.5404 -0.3386 0.2164  -0.0996 201 GLY D C   
15883 O O   . GLY D 201 ? 1.7376 1.1968 1.5168 -0.3531 0.2380  -0.0976 201 GLY D O   
15887 N N   . SER D 202 ? 1.7219 1.2323 1.5062 -0.3096 0.2011  -0.0883 202 SER D N   
15888 C CA  . SER D 202 ? 1.7314 1.1875 1.4614 -0.2911 0.2067  -0.0735 202 SER D CA  
15889 C C   . SER D 202 ? 1.7089 1.1770 1.4282 -0.2627 0.1842  -0.0687 202 SER D C   
15890 O O   . SER D 202 ? 1.6949 1.2145 1.4470 -0.2553 0.1677  -0.0724 202 SER D O   
15891 C CB  . SER D 202 ? 1.7504 1.1960 1.4672 -0.2862 0.2217  -0.0605 202 SER D CB  
15892 O OG  . SER D 202 ? 1.7193 1.2238 1.4766 -0.2826 0.2142  -0.0604 202 SER D OG  
15898 N N   . GLY D 203 ? 1.7459 1.1645 1.4180 -0.2464 0.1846  -0.0606 203 GLY D N   
15899 C CA  . GLY D 203 ? 1.6993 1.1246 1.3596 -0.2197 0.1661  -0.0565 203 GLY D CA  
15900 C C   . GLY D 203 ? 1.6657 1.0943 1.3129 -0.1955 0.1627  -0.0431 203 GLY D C   
15901 O O   . GLY D 203 ? 1.7399 1.1513 1.3739 -0.1967 0.1753  -0.0354 203 GLY D O   
15905 N N   . VAL D 204 ? 1.6243 1.0752 1.2753 -0.1734 0.1456  -0.0410 204 VAL D N   
15906 C CA  . VAL D 204 ? 1.6036 1.0611 1.2457 -0.1493 0.1394  -0.0304 204 VAL D CA  
15907 C C   . VAL D 204 ? 1.6292 1.0801 1.2561 -0.1266 0.1262  -0.0301 204 VAL D C   
15908 O O   . VAL D 204 ? 1.6117 1.0756 1.2494 -0.1285 0.1184  -0.0377 204 VAL D O   
15909 C CB  . VAL D 204 ? 1.5763 1.0911 1.2589 -0.1488 0.1330  -0.0289 204 VAL D CB  
15910 C CG1 . VAL D 204 ? 1.5871 1.1173 1.2935 -0.1735 0.1450  -0.0329 204 VAL D CG1 
15911 C CG2 . VAL D 204 ? 1.4841 1.0414 1.1942 -0.1422 0.1170  -0.0347 204 VAL D CG2 
15921 N N   . TYR D 205 ? 1.5931 1.0236 1.1945 -0.1042 0.1234  -0.0219 205 TYR D N   
15922 C CA  . TYR D 205 ? 1.5803 1.0070 1.1697 -0.0804 0.1116  -0.0219 205 TYR D CA  
15923 C C   . TYR D 205 ? 1.5491 1.0263 1.1698 -0.0662 0.0999  -0.0192 205 TYR D C   
15924 O O   . TYR D 205 ? 1.5102 0.9922 1.1303 -0.0566 0.0991  -0.0126 205 TYR D O   
15925 C CB  . TYR D 205 ? 1.6518 1.0232 1.1934 -0.0634 0.1146  -0.0167 205 TYR D CB  
15926 C CG  . TYR D 205 ? 1.7832 1.0981 1.2883 -0.0764 0.1269  -0.0193 205 TYR D CG  
15927 C CD1 . TYR D 205 ? 1.7818 1.0816 1.2863 -0.1022 0.1424  -0.0198 205 TYR D CD1 
15928 C CD2 . TYR D 205 ? 1.8351 1.1110 1.3065 -0.0631 0.1239  -0.0216 205 TYR D CD2 
15929 C CE1 . TYR D 205 ? 1.8517 1.0981 1.3234 -0.1161 0.1551  -0.0227 205 TYR D CE1 
15930 C CE2 . TYR D 205 ? 1.8749 1.0954 1.3103 -0.0754 0.1354  -0.0240 205 TYR D CE2 
15931 C CZ  . TYR D 205 ? 1.9367 1.1420 1.3724 -0.1027 0.1513  -0.0246 205 TYR D CZ  
15932 O OH  . TYR D 205 ? 1.9765 1.1249 1.3768 -0.1167 0.1643  -0.0275 205 TYR D OH  
15942 N N   . GLU D 206 ? 1.4947 1.0067 1.1407 -0.0648 0.0914  -0.0245 206 GLU D N   
15943 C CA  . GLU D 206 ? 1.4445 1.0046 1.1221 -0.0554 0.0825  -0.0227 206 GLU D CA  
15944 C C   . GLU D 206 ? 1.3987 0.9566 1.0678 -0.0296 0.0752  -0.0195 206 GLU D C   
15945 O O   . GLU D 206 ? 1.4082 0.9340 1.0507 -0.0170 0.0744  -0.0207 206 GLU D O   
15946 C CB  . GLU D 206 ? 1.4424 1.0356 1.1453 -0.0621 0.0772  -0.0295 206 GLU D CB  
15947 C CG  . GLU D 206 ? 1.4310 1.0585 1.1634 -0.0798 0.0779  -0.0316 206 GLU D CG  
15948 C CD  . GLU D 206 ? 1.4847 1.0941 1.2129 -0.1021 0.0860  -0.0368 206 GLU D CD  
15949 O OE1 . GLU D 206 ? 1.5258 1.0924 1.2254 -0.1048 0.0923  -0.0377 206 GLU D OE1 
15950 O OE2 . GLU D 206 ? 1.4719 1.1096 1.2258 -0.1170 0.0863  -0.0406 206 GLU D OE2 
15957 N N   . ASN D 207 ? 1.3487 0.9422 1.0421 -0.0217 0.0694  -0.0162 207 ASN D N   
15958 C CA  . ASN D 207 ? 1.3494 0.9512 1.0451 0.0015  0.0612  -0.0155 207 ASN D CA  
15959 C C   . ASN D 207 ? 1.3788 0.9935 1.0835 0.0087  0.0580  -0.0212 207 ASN D C   
15960 O O   . ASN D 207 ? 1.3924 0.9947 1.0858 0.0270  0.0544  -0.0231 207 ASN D O   
15961 C CB  . ASN D 207 ? 1.3614 1.0003 1.0844 0.0052  0.0562  -0.0120 207 ASN D CB  
15962 C CG  . ASN D 207 ? 1.3136 0.9379 1.0248 0.0014  0.0593  -0.0061 207 ASN D CG  
15963 O OD1 . ASN D 207 ? 1.3936 0.9771 1.0720 0.0078  0.0619  -0.0038 207 ASN D OD1 
15964 N ND2 . ASN D 207 ? 1.2899 0.9444 1.0245 -0.0083 0.0596  -0.0036 207 ASN D ND2 
15971 N N   . SER D 208 ? 1.3467 0.9857 1.0706 -0.0043 0.0591  -0.0244 208 SER D N   
15972 C CA  . SER D 208 ? 1.3101 0.9584 1.0391 0.0014  0.0577  -0.0297 208 SER D CA  
15973 C C   . SER D 208 ? 1.3167 0.9683 1.0485 -0.0167 0.0598  -0.0341 208 SER D C   
15974 O O   . SER D 208 ? 1.2878 0.9510 1.0307 -0.0325 0.0610  -0.0335 208 SER D O   
15975 C CB  . SER D 208 ? 1.3034 0.9906 1.0606 0.0122  0.0542  -0.0293 208 SER D CB  
15976 O OG  . SER D 208 ? 1.4259 1.1146 1.1855 0.0286  0.0503  -0.0271 208 SER D OG  
15982 N N   . CYS D 209 ? 1.2909 0.9325 1.0127 -0.0130 0.0597  -0.0395 209 CYS D N   
15983 C CA  . CYS D 209 ? 1.3321 0.9764 1.0551 -0.0269 0.0593  -0.0455 209 CYS D CA  
15984 C C   . CYS D 209 ? 1.2895 0.9442 1.0141 -0.0159 0.0579  -0.0491 209 CYS D C   
15985 O O   . CYS D 209 ? 1.2757 0.9076 0.9811 -0.0047 0.0593  -0.0515 209 CYS D O   
15986 C CB  . CYS D 209 ? 1.3613 0.9665 1.0590 -0.0381 0.0619  -0.0497 209 CYS D CB  
15987 S SG  . CYS D 209 ? 1.3958 1.0092 1.1034 -0.0617 0.0599  -0.0582 209 CYS D SG  
15993 N N   . ALA D 210 ? 1.2690 0.9556 1.0139 -0.0183 0.0561  -0.0494 210 ALA D N   
15994 C CA  . ALA D 210 ? 1.2873 0.9813 1.0310 -0.0085 0.0570  -0.0525 210 ALA D CA  
15995 C C   . ALA D 210 ? 1.2944 0.9644 1.0161 -0.0131 0.0552  -0.0601 210 ALA D C   
15996 O O   . ALA D 210 ? 1.2779 0.9316 0.9832 -0.0016 0.0577  -0.0628 210 ALA D O   
15997 C CB  . ALA D 210 ? 1.2332 0.9615 0.9987 -0.0104 0.0562  -0.0507 210 ALA D CB  
16003 N N   . SER D 211 ? 1.3064 0.9746 1.0287 -0.0297 0.0507  -0.0645 211 SER D N   
16004 C CA  . SER D 211 ? 1.2861 0.9311 0.9887 -0.0353 0.0472  -0.0733 211 SER D CA  
16005 C C   . SER D 211 ? 1.3435 0.9492 1.0209 -0.0334 0.0502  -0.0748 211 SER D C   
16006 O O   . SER D 211 ? 1.3823 0.9641 1.0377 -0.0295 0.0490  -0.0808 211 SER D O   
16007 C CB  . SER D 211 ? 1.2971 0.9522 1.0110 -0.0541 0.0409  -0.0795 211 SER D CB  
16008 O OG  . SER D 211 ? 1.3812 1.0453 1.1111 -0.0650 0.0434  -0.0751 211 SER D OG  
16014 N N   . GLY D 212 ? 1.3532 0.9484 1.0299 -0.0352 0.0540  -0.0694 212 GLY D N   
16015 C CA  . GLY D 212 ? 1.3665 0.9197 1.0148 -0.0321 0.0572  -0.0703 212 GLY D CA  
16016 C C   . GLY D 212 ? 1.3275 0.8695 0.9612 -0.0094 0.0593  -0.0685 212 GLY D C   
16017 O O   . GLY D 212 ? 1.3902 0.8979 0.9963 -0.0039 0.0601  -0.0725 212 GLY D O   
16021 N N   . THR D 213 ? 1.3122 0.8831 0.9652 0.0039  0.0605  -0.0634 213 THR D N   
16022 C CA  . THR D 213 ? 1.3370 0.9058 0.9838 0.0252  0.0631  -0.0636 213 THR D CA  
16023 C C   . THR D 213 ? 1.4012 0.9669 1.0381 0.0282  0.0638  -0.0695 213 THR D C   
16024 O O   . THR D 213 ? 1.4024 0.9462 1.0189 0.0416  0.0663  -0.0726 213 THR D O   
16025 C CB  . THR D 213 ? 1.3152 0.9206 0.9908 0.0356  0.0645  -0.0586 213 THR D CB  
16026 O OG1 . THR D 213 ? 1.3285 0.9394 1.0140 0.0299  0.0623  -0.0534 213 THR D OG1 
16027 C CG2 . THR D 213 ? 1.3590 0.9613 1.0314 0.0580  0.0674  -0.0597 213 THR D CG2 
16035 N N   . THR D 214 ? 1.3675 0.9534 1.0165 0.0172  0.0613  -0.0714 214 THR D N   
16036 C CA  . THR D 214 ? 1.3527 0.9308 0.9870 0.0199  0.0608  -0.0775 214 THR D CA  
16037 C C   . THR D 214 ? 1.4275 0.9648 1.0308 0.0154  0.0575  -0.0844 214 THR D C   
16038 O O   . THR D 214 ? 1.4685 0.9853 1.0494 0.0267  0.0593  -0.0885 214 THR D O   
16039 C CB  . THR D 214 ? 1.3127 0.9160 0.9621 0.0088  0.0563  -0.0790 214 THR D CB  
16040 O OG1 . THR D 214 ? 1.2866 0.9206 0.9557 0.0175  0.0615  -0.0738 214 THR D OG1 
16041 C CG2 . THR D 214 ? 1.4356 1.0214 1.0630 0.0075  0.0517  -0.0875 214 THR D CG2 
16049 N N   . ALA D 215 ? 1.3912 0.9154 0.9927 -0.0017 0.0535  -0.0862 215 ALA D N   
16050 C CA  . ALA D 215 ? 1.4842 0.9678 1.0571 -0.0085 0.0510  -0.0934 215 ALA D CA  
16051 C C   . ALA D 215 ? 1.5268 0.9771 1.0731 0.0078  0.0559  -0.0918 215 ALA D C   
16052 O O   . ALA D 215 ? 1.5610 0.9809 1.0795 0.0136  0.0551  -0.0978 215 ALA D O   
16053 C CB  . ALA D 215 ? 1.4619 0.9383 1.0412 -0.0309 0.0491  -0.0951 215 ALA D CB  
16059 N N   . LEU D 216 ? 1.4921 0.9468 1.0452 0.0169  0.0601  -0.0845 216 LEU D N   
16060 C CA  . LEU D 216 ? 1.5404 0.9653 1.0689 0.0354  0.0634  -0.0835 216 LEU D CA  
16061 C C   . LEU D 216 ? 1.5492 0.9820 1.0747 0.0558  0.0662  -0.0856 216 LEU D C   
16062 O O   . LEU D 216 ? 1.6022 1.0026 1.0989 0.0682  0.0676  -0.0893 216 LEU D O   
16063 C CB  . LEU D 216 ? 1.4836 0.9155 1.0221 0.0425  0.0650  -0.0762 216 LEU D CB  
16064 C CG  . LEU D 216 ? 1.5245 0.9358 1.0445 0.0666  0.0667  -0.0754 216 LEU D CG  
16065 C CD1 . LEU D 216 ? 1.5444 0.9027 1.0262 0.0653  0.0668  -0.0759 216 LEU D CD1 
16066 C CD2 . LEU D 216 ? 1.4934 0.9380 1.0411 0.0782  0.0663  -0.0698 216 LEU D CD2 
16078 N N   . GLY D 217 ? 1.5302 1.0038 1.0839 0.0597  0.0684  -0.0833 217 GLY D N   
16079 C CA  . GLY D 217 ? 1.5298 1.0111 1.0816 0.0774  0.0741  -0.0853 217 GLY D CA  
16080 C C   . GLY D 217 ? 1.5755 1.0288 1.0976 0.0767  0.0729  -0.0924 217 GLY D C   
16081 O O   . GLY D 217 ? 1.6247 1.0562 1.1246 0.0929  0.0770  -0.0955 217 GLY D O   
16085 N N   . TYR D 218 ? 1.5891 1.0427 1.1101 0.0590  0.0666  -0.0958 218 TYR D N   
16086 C CA  . TYR D 218 ? 1.6217 1.0464 1.1130 0.0575  0.0627  -0.1040 218 TYR D CA  
16087 C C   . TYR D 218 ? 1.7141 1.0923 1.1721 0.0609  0.0616  -0.1079 218 TYR D C   
16088 O O   . TYR D 218 ? 1.7147 1.0672 1.1449 0.0746  0.0638  -0.1122 218 TYR D O   
16089 C CB  . TYR D 218 ? 1.5862 1.0181 1.0844 0.0365  0.0530  -0.1089 218 TYR D CB  
16090 C CG  . TYR D 218 ? 1.5773 1.0475 1.0992 0.0346  0.0524  -0.1068 218 TYR D CG  
16091 C CD1 . TYR D 218 ? 1.5283 1.0106 1.0490 0.0508  0.0602  -0.1044 218 TYR D CD1 
16092 C CD2 . TYR D 218 ? 1.5587 1.0511 1.1029 0.0166  0.0451  -0.1075 218 TYR D CD2 
16093 C CE1 . TYR D 218 ? 1.4801 0.9921 1.0180 0.0490  0.0606  -0.1021 218 TYR D CE1 
16094 C CE2 . TYR D 218 ? 1.5089 1.0331 1.0712 0.0162  0.0440  -0.1057 218 TYR D CE2 
16095 C CZ  . TYR D 218 ? 1.5123 1.0444 1.0697 0.0323  0.0517  -0.1027 218 TYR D CZ  
16096 O OH  . TYR D 218 ? 1.4506 1.0094 1.0218 0.0318  0.0514  -0.1006 218 TYR D OH  
16106 N N   . TYR D 219 ? 1.8673 1.2317 1.3253 0.0486  0.0590  -0.1064 219 TYR D N   
16107 C CA  . TYR D 219 ? 1.8724 1.1876 1.2956 0.0497  0.0586  -0.1098 219 TYR D CA  
16108 C C   . TYR D 219 ? 1.8629 1.1634 1.2694 0.0758  0.0647  -0.1073 219 TYR D C   
16109 O O   . TYR D 219 ? 1.8699 1.1286 1.2408 0.0842  0.0647  -0.1119 219 TYR D O   
16110 C CB  . TYR D 219 ? 1.9229 1.2276 1.3505 0.0318  0.0576  -0.1072 219 TYR D CB  
16111 C CG  . TYR D 219 ? 2.0694 1.3206 1.4613 0.0229  0.0565  -0.1127 219 TYR D CG  
16112 C CD1 . TYR D 219 ? 2.0435 1.2796 1.4281 0.0030  0.0508  -0.1220 219 TYR D CD1 
16113 C CD2 . TYR D 219 ? 2.0239 1.2383 1.3886 0.0345  0.0609  -0.1093 219 TYR D CD2 
16114 C CE1 . TYR D 219 ? 2.0703 1.2561 1.4231 -0.0070 0.0506  -0.1278 219 TYR D CE1 
16115 C CE2 . TYR D 219 ? 2.0776 1.2382 1.4060 0.0259  0.0611  -0.1141 219 TYR D CE2 
16116 C CZ  . TYR D 219 ? 2.1375 1.2842 1.4610 0.0040  0.0567  -0.1233 219 TYR D CZ  
16117 O OH  . TYR D 219 ? 2.1689 1.2608 1.4571 -0.0064 0.0577  -0.1288 219 TYR D OH  
16127 N N   . LEU D 220 ? 1.7613 1.0957 1.1938 0.0892  0.0694  -0.1010 220 LEU D N   
16128 C CA  . LEU D 220 ? 1.7532 1.0803 1.1765 0.1151  0.0744  -0.1001 220 LEU D CA  
16129 C C   . LEU D 220 ? 1.7717 1.1021 1.1875 0.1310  0.0800  -0.1043 220 LEU D C   
16130 O O   . LEU D 220 ? 1.7882 1.0975 1.1833 0.1514  0.0836  -0.1068 220 LEU D O   
16131 C CB  . LEU D 220 ? 1.6483 1.0132 1.1059 0.1233  0.0765  -0.0938 220 LEU D CB  
16132 C CG  . LEU D 220 ? 1.6465 0.9995 1.1025 0.1190  0.0727  -0.0893 220 LEU D CG  
16133 C CD1 . LEU D 220 ? 1.5285 0.9136 1.0118 0.1368  0.0736  -0.0858 220 LEU D CD1 
16134 C CD2 . LEU D 220 ? 1.6324 0.9279 1.0436 0.1228  0.0709  -0.0918 220 LEU D CD2 
16146 N N   . LYS D 221 ? 1.7319 1.0868 1.1619 0.1234  0.0812  -0.1051 221 LYS D N   
16147 C CA  . LYS D 221 ? 1.7665 1.1222 1.1864 0.1378  0.0884  -0.1085 221 LYS D CA  
16148 C C   . LYS D 221 ? 1.8042 1.1125 1.1797 0.1390  0.0847  -0.1158 221 LYS D C   
16149 O O   . LYS D 221 ? 1.8410 1.1385 1.1985 0.1557  0.0914  -0.1190 221 LYS D O   
16150 C CB  . LYS D 221 ? 1.7054 1.0975 1.1500 0.1292  0.0908  -0.1065 221 LYS D CB  
16151 C CG  . LYS D 221 ? 1.7079 1.1050 1.1449 0.1438  0.1014  -0.1084 221 LYS D CG  
16152 C CD  . LYS D 221 ? 1.7557 1.1606 1.1993 0.1668  0.1140  -0.1079 221 LYS D CD  
16153 C CE  . LYS D 221 ? 1.8058 1.1955 1.2249 0.1813  0.1246  -0.1119 221 LYS D CE  
16154 N NZ  . LYS D 221 ? 1.8298 1.1691 1.2014 0.1829  0.1173  -0.1182 221 LYS D NZ  
16168 N N   . LYS D 222 ? 1.8210 1.0998 1.1787 0.1217  0.0749  -0.1190 222 LYS D N   
16169 C CA  . LYS D 222 ? 1.8112 1.0414 1.1262 0.1215  0.0701  -0.1270 222 LYS D CA  
16170 C C   . LYS D 222 ? 1.8850 1.0749 1.1715 0.1329  0.0713  -0.1275 222 LYS D C   
16171 O O   . LYS D 222 ? 2.0265 1.1812 1.2778 0.1471  0.0727  -0.1326 222 LYS D O   
16172 C CB  . LYS D 222 ? 1.8076 1.0262 1.1192 0.0950  0.0589  -0.1325 222 LYS D CB  
16173 C CG  . LYS D 222 ? 1.8494 1.1096 1.1938 0.0798  0.0547  -0.1317 222 LYS D CG  
16174 C CD  . LYS D 222 ? 1.8443 1.1356 1.2013 0.0944  0.0617  -0.1286 222 LYS D CD  
16175 C CE  . LYS D 222 ? 1.8227 1.1408 1.1978 0.0799  0.0547  -0.1306 222 LYS D CE  
16176 N NZ  . LYS D 222 ? 1.7425 1.1050 1.1595 0.0714  0.0569  -0.1226 222 LYS D NZ  
16190 N N   . CYS D 223 ? 1.8640 1.0556 1.1619 0.1279  0.0706  -0.1224 223 CYS D N   
16191 C CA  . CYS D 223 ? 1.9361 1.0844 1.2028 0.1380  0.0707  -0.1226 223 CYS D CA  
16192 C C   . CYS D 223 ? 1.9505 1.1058 1.2164 0.1689  0.0773  -0.1209 223 CYS D C   
16193 O O   . CYS D 223 ? 2.0154 1.1321 1.2454 0.1860  0.0784  -0.1249 223 CYS D O   
16194 C CB  . CYS D 223 ? 1.9513 1.0966 1.2274 0.1226  0.0683  -0.1175 223 CYS D CB  
16195 S SG  . CYS D 223 ? 2.1282 1.2450 1.3930 0.0875  0.0624  -0.1218 223 CYS D SG  
16201 N N   . LYS D 224 ? 1.9049 1.1092 1.2111 0.1765  0.0812  -0.1158 224 LYS D N   
16202 C CA  . LYS D 224 ? 1.9128 1.1335 1.2289 0.2047  0.0872  -0.1156 224 LYS D CA  
16203 C C   . LYS D 224 ? 1.8833 1.1388 1.2201 0.2150  0.0964  -0.1173 224 LYS D C   
16204 O O   . LYS D 224 ? 1.9174 1.1725 1.2492 0.2391  0.1032  -0.1206 224 LYS D O   
16205 C CB  . LYS D 224 ? 1.9494 1.1999 1.2971 0.2070  0.0851  -0.1101 224 LYS D CB  
16206 C CG  . LYS D 224 ? 2.0037 1.2663 1.3605 0.2370  0.0873  -0.1116 224 LYS D CG  
16207 C CD  . LYS D 224 ? 1.9710 1.2739 1.3562 0.2518  0.0973  -0.1147 224 LYS D CD  
16208 C CE  . LYS D 224 ? 1.9637 1.3014 1.3810 0.2749  0.0991  -0.1165 224 LYS D CE  
16209 N NZ  . LYS D 224 ? 1.9482 1.3280 1.3980 0.2833  0.1120  -0.1195 224 LYS D NZ  
16223 N N   . ASN D 225 ? 1.8622 1.1442 1.2190 0.1978  0.0975  -0.1157 225 ASN D N   
16224 C CA  . ASN D 225 ? 1.8509 1.1674 1.2293 0.2053  0.1081  -0.1159 225 ASN D CA  
16225 C C   . ASN D 225 ? 1.8728 1.2406 1.2995 0.2106  0.1134  -0.1115 225 ASN D C   
16226 O O   . ASN D 225 ? 1.8991 1.2943 1.3460 0.2244  0.1252  -0.1126 225 ASN D O   
16227 C CB  . ASN D 225 ? 1.8715 1.1664 1.2232 0.2279  0.1169  -0.1213 225 ASN D CB  
16228 C CG  . ASN D 225 ? 1.8579 1.1799 1.2241 0.2329  0.1301  -0.1215 225 ASN D CG  
16229 O OD1 . ASN D 225 ? 1.9409 1.2574 1.2958 0.2203  0.1289  -0.1218 225 ASN D OD1 
16230 N ND2 . ASN D 225 ? 1.9074 1.2583 1.2986 0.2516  0.1428  -0.1220 225 ASN D ND2 
16237 N N   . LEU D 226 ? 1.8081 1.1880 1.2534 0.1995  0.1054  -0.1072 226 LEU D N   
16238 C CA  . LEU D 226 ? 1.7695 1.1977 1.2610 0.2017  0.1080  -0.1035 226 LEU D CA  
16239 C C   . LEU D 226 ? 1.7058 1.1679 1.2234 0.1852  0.1121  -0.1001 226 LEU D C   
16240 O O   . LEU D 226 ? 1.6792 1.1362 1.1925 0.1646  0.1051  -0.0976 226 LEU D O   
16241 C CB  . LEU D 226 ? 1.7629 1.1871 1.2593 0.1963  0.0977  -0.0999 226 LEU D CB  
16242 C CG  . LEU D 226 ? 1.6958 1.1534 1.2262 0.2107  0.0971  -0.0992 226 LEU D CG  
16243 C CD1 . LEU D 226 ? 1.7274 1.2013 1.2701 0.2363  0.1056  -0.1052 226 LEU D CD1 
16244 C CD2 . LEU D 226 ? 1.7156 1.1450 1.2271 0.2141  0.0865  -0.0976 226 LEU D CD2 
16256 N N   . ASP D 227 ? 1.6645 1.1605 1.2091 0.1945  0.1241  -0.1006 227 ASP D N   
16257 C CA  . ASP D 227 ? 1.6610 1.1838 1.2244 0.1816  0.1303  -0.0976 227 ASP D CA  
16258 C C   . ASP D 227 ? 1.6320 1.1958 1.2375 0.1713  0.1280  -0.0926 227 ASP D C   
16259 O O   . ASP D 227 ? 1.6149 1.1976 1.2333 0.1584  0.1308  -0.0893 227 ASP D O   
16260 C CB  . ASP D 227 ? 1.6376 1.1711 1.2045 0.1955  0.1476  -0.1004 227 ASP D CB  
16261 C CG  . ASP D 227 ? 1.7406 1.2332 1.2618 0.2008  0.1503  -0.1043 227 ASP D CG  
16262 O OD1 . ASP D 227 ? 1.7700 1.2350 1.2670 0.2157  0.1498  -0.1087 227 ASP D OD1 
16263 O OD2 . ASP D 227 ? 1.7343 1.2207 1.2416 0.1912  0.1522  -0.1034 227 ASP D OD2 
16268 N N   . ARG D 228 ? 1.6373 1.2126 1.2613 0.1776  0.1222  -0.0921 228 ARG D N   
16269 C CA  . ARG D 228 ? 1.6209 1.2312 1.2814 0.1681  0.1181  -0.0877 228 ARG D CA  
16270 C C   . ARG D 228 ? 1.6112 1.2174 1.2757 0.1775  0.1082  -0.0882 228 ARG D C   
16271 O O   . ARG D 228 ? 1.6151 1.2063 1.2679 0.1967  0.1083  -0.0931 228 ARG D O   
16272 C CB  . ARG D 228 ? 1.6024 1.2558 1.3023 0.1717  0.1307  -0.0882 228 ARG D CB  
16273 C CG  . ARG D 228 ? 1.6691 1.3405 1.3912 0.1931  0.1368  -0.0942 228 ARG D CG  
16274 C CD  . ARG D 228 ? 1.7547 1.4725 1.5229 0.1938  0.1493  -0.0956 228 ARG D CD  
16275 N NE  . ARG D 228 ? 1.8675 1.5951 1.6476 0.2140  0.1611  -0.1034 228 ARG D NE  
16276 C CZ  . ARG D 228 ? 1.8732 1.6416 1.6983 0.2209  0.1713  -0.1084 228 ARG D CZ  
16277 N NH1 . ARG D 228 ? 1.8157 1.6180 1.6771 0.2084  0.1722  -0.1060 228 ARG D NH1 
16278 N NH2 . ARG D 228 ? 1.8544 1.6301 1.6894 0.2406  0.1808  -0.1168 228 ARG D NH2 
16292 N N   . ALA D 229 ? 1.5264 1.1447 1.2057 0.1655  0.0998  -0.0835 229 ALA D N   
16293 C CA  . ALA D 229 ? 1.5270 1.1388 1.2065 0.1748  0.0899  -0.0834 229 ALA D CA  
16294 C C   . ALA D 229 ? 1.4652 1.0962 1.1648 0.1598  0.0833  -0.0776 229 ALA D C   
16295 O O   . ALA D 229 ? 1.4421 1.0723 1.1384 0.1398  0.0830  -0.0732 229 ALA D O   
16296 C CB  . ALA D 229 ? 1.5509 1.1105 1.1842 0.1779  0.0838  -0.0841 229 ALA D CB  
16302 N N   . LYS D 230 ? 1.4769 1.1255 1.1973 0.1708  0.0772  -0.0784 230 LYS D N   
16303 C CA  . LYS D 230 ? 1.4402 1.1013 1.1743 0.1597  0.0698  -0.0731 230 LYS D CA  
16304 C C   . LYS D 230 ? 1.4474 1.0653 1.1441 0.1558  0.0620  -0.0696 230 LYS D C   
16305 O O   . LYS D 230 ? 1.5004 1.0893 1.1729 0.1723  0.0576  -0.0725 230 LYS D O   
16306 C CB  . LYS D 230 ? 1.4146 1.1095 1.1839 0.1743  0.0652  -0.0765 230 LYS D CB  
16307 C CG  . LYS D 230 ? 1.4532 1.1946 1.2658 0.1728  0.0742  -0.0793 230 LYS D CG  
16308 C CD  . LYS D 230 ? 1.4692 1.2420 1.3171 0.1907  0.0695  -0.0864 230 LYS D CD  
16309 C CE  . LYS D 230 ? 1.4717 1.2510 1.3283 0.1885  0.0565  -0.0835 230 LYS D CE  
16310 N NZ  . LYS D 230 ? 1.5642 1.3071 1.3876 0.2029  0.0440  -0.0840 230 LYS D NZ  
16324 N N   . ILE D 231 ? 1.4060 1.0182 1.0972 0.1342  0.0611  -0.0637 231 ILE D N   
16325 C CA  . ILE D 231 ? 1.4436 1.0140 1.1002 0.1261  0.0572  -0.0604 231 ILE D CA  
16326 C C   . ILE D 231 ? 1.4325 1.0127 1.1002 0.1228  0.0514  -0.0554 231 ILE D C   
16327 O O   . ILE D 231 ? 1.3727 0.9757 1.0599 0.1060  0.0522  -0.0513 231 ILE D O   
16328 C CB  . ILE D 231 ? 1.4372 0.9909 1.0780 0.1037  0.0611  -0.0592 231 ILE D CB  
16329 C CG1 . ILE D 231 ? 1.4784 1.0218 1.1065 0.1088  0.0659  -0.0646 231 ILE D CG1 
16330 C CG2 . ILE D 231 ? 1.4566 0.9667 1.0640 0.0941  0.0593  -0.0566 231 ILE D CG2 
16331 C CD1 . ILE D 231 ? 1.4869 0.9876 1.0790 0.1246  0.0651  -0.0683 231 ILE D CD1 
16343 N N   . VAL D 232 ? 1.4246 0.9852 1.0770 0.1403  0.0451  -0.0561 232 VAL D N   
16344 C CA  . VAL D 232 ? 1.4225 0.9830 1.0763 0.1393  0.0391  -0.0514 232 VAL D CA  
16345 C C   . VAL D 232 ? 1.4469 0.9768 1.0755 0.1175  0.0431  -0.0453 232 VAL D C   
16346 O O   . VAL D 232 ? 1.4896 0.9787 1.0843 0.1122  0.0472  -0.0458 232 VAL D O   
16347 C CB  . VAL D 232 ? 1.4506 0.9897 1.0861 0.1657  0.0303  -0.0545 232 VAL D CB  
16348 C CG1 . VAL D 232 ? 1.5209 1.0310 1.1315 0.1631  0.0262  -0.0485 232 VAL D CG1 
16349 C CG2 . VAL D 232 ? 1.4091 0.9937 1.0851 0.1836  0.0243  -0.0606 232 VAL D CG2 
16359 N N   . GLN D 233 ? 1.3915 0.9408 1.0374 0.1045  0.0426  -0.0403 233 GLN D N   
16360 C CA  . GLN D 233 ? 1.4187 0.9487 1.0501 0.0823  0.0478  -0.0351 233 GLN D CA  
16361 C C   . GLN D 233 ? 1.4380 0.9628 1.0651 0.0850  0.0443  -0.0298 233 GLN D C   
16362 O O   . GLN D 233 ? 1.4133 0.9552 1.0533 0.1028  0.0363  -0.0307 233 GLN D O   
16363 C CB  . GLN D 233 ? 1.3873 0.9514 1.0473 0.0610  0.0520  -0.0350 233 GLN D CB  
16364 C CG  . GLN D 233 ? 1.4116 0.9636 1.0612 0.0531  0.0563  -0.0398 233 GLN D CG  
16365 C CD  . GLN D 233 ? 1.3683 0.9560 1.0454 0.0384  0.0580  -0.0412 233 GLN D CD  
16366 O OE1 . GLN D 233 ? 1.3501 0.9416 1.0318 0.0190  0.0597  -0.0400 233 GLN D OE1 
16367 N NE2 . GLN D 233 ? 1.3347 0.9471 1.0287 0.0483  0.0580  -0.0442 233 GLN D NE2 
16376 N N   . PRO D 234 ? 1.4276 0.9272 1.0359 0.0680  0.0505  -0.0250 234 PRO D N   
16377 C CA  . PRO D 234 ? 1.4545 0.9377 1.0480 0.0728  0.0488  -0.0196 234 PRO D CA  
16378 C C   . PRO D 234 ? 1.4593 0.9845 1.0853 0.0824  0.0402  -0.0186 234 PRO D C   
16379 O O   . PRO D 234 ? 1.4740 0.9915 1.0911 0.1040  0.0313  -0.0195 234 PRO D O   
16380 C CB  . PRO D 234 ? 1.4463 0.9156 1.0323 0.0463  0.0598  -0.0153 234 PRO D CB  
16381 C CG  . PRO D 234 ? 1.4566 0.9071 1.0311 0.0338  0.0662  -0.0197 234 PRO D CG  
16382 C CD  . PRO D 234 ? 1.4561 0.9381 1.0538 0.0443  0.0598  -0.0253 234 PRO D CD  
16390 N N   . ASN D 235 ? 1.4094 0.9777 1.0719 0.0674  0.0417  -0.0177 235 ASN D N   
16391 C CA  . ASN D 235 ? 1.3569 0.9632 1.0496 0.0739  0.0344  -0.0167 235 ASN D CA  
16392 C C   . ASN D 235 ? 1.3185 0.9711 1.0506 0.0741  0.0326  -0.0212 235 ASN D C   
16393 O O   . ASN D 235 ? 1.2702 0.9578 1.0310 0.0648  0.0325  -0.0195 235 ASN D O   
16394 C CB  . ASN D 235 ? 1.3702 0.9829 1.0676 0.0571  0.0386  -0.0106 235 ASN D CB  
16395 C CG  . ASN D 235 ? 1.3697 0.9743 1.0577 0.0700  0.0318  -0.0072 235 ASN D CG  
16396 O OD1 . ASN D 235 ? 1.3163 0.9289 1.0102 0.0906  0.0211  -0.0107 235 ASN D OD1 
16397 N ND2 . ASN D 235 ? 1.3863 0.9753 1.0603 0.0584  0.0380  -0.0012 235 ASN D ND2 
16404 N N   . GLY D 236 ? 1.3619 1.0128 1.0934 0.0851  0.0321  -0.0268 236 GLY D N   
16405 C CA  . GLY D 236 ? 1.2765 0.9663 1.0413 0.0860  0.0332  -0.0311 236 GLY D CA  
16406 C C   . GLY D 236 ? 1.2977 0.9729 1.0503 0.0931  0.0368  -0.0362 236 GLY D C   
16407 O O   . GLY D 236 ? 1.3259 0.9610 1.0443 0.0965  0.0377  -0.0366 236 GLY D O   
16411 N N   . TRP D 237 ? 1.2883 0.9949 1.0677 0.0952  0.0398  -0.0403 237 TRP D N   
16412 C CA  . TRP D 237 ? 1.2781 0.9749 1.0485 0.1024  0.0445  -0.0454 237 TRP D CA  
16413 C C   . TRP D 237 ? 1.2592 0.9821 1.0494 0.0914  0.0522  -0.0463 237 TRP D C   
16414 O O   . TRP D 237 ? 1.1934 0.9500 1.0127 0.0859  0.0533  -0.0450 237 TRP D O   
16415 C CB  . TRP D 237 ? 1.2576 0.9601 1.0360 0.1270  0.0402  -0.0519 237 TRP D CB  
16416 C CG  . TRP D 237 ? 1.2275 0.9767 1.0498 0.1325  0.0400  -0.0556 237 TRP D CG  
16417 C CD1 . TRP D 237 ? 1.2318 1.0017 1.0760 0.1403  0.0316  -0.0568 237 TRP D CD1 
16418 C CD2 . TRP D 237 ? 1.2076 0.9861 1.0560 0.1301  0.0494  -0.0590 237 TRP D CD2 
16419 N NE1 . TRP D 237 ? 1.1786 0.9906 1.0639 0.1415  0.0352  -0.0614 237 TRP D NE1 
16420 C CE2 . TRP D 237 ? 1.1816 0.9984 1.0692 0.1352  0.0474  -0.0623 237 TRP D CE2 
16421 C CE3 . TRP D 237 ? 1.2525 1.0260 1.0928 0.1244  0.0598  -0.0598 237 TRP D CE3 
16422 C CZ2 . TRP D 237 ? 1.1866 1.0362 1.1060 0.1333  0.0574  -0.0661 237 TRP D CZ2 
16423 C CZ3 . TRP D 237 ? 1.2098 1.0140 1.0782 0.1243  0.0693  -0.0630 237 TRP D CZ3 
16424 C CH2 . TRP D 237 ? 1.1654 1.0070 1.0733 0.1280  0.0691  -0.0659 237 TRP D CH2 
16435 N N   . LEU D 238 ? 1.2509 0.9542 1.0214 0.0890  0.0574  -0.0487 238 LEU D N   
16436 C CA  . LEU D 238 ? 1.2817 1.0008 1.0615 0.0815  0.0646  -0.0501 238 LEU D CA  
16437 C C   . LEU D 238 ? 1.2872 0.9923 1.0538 0.0948  0.0697  -0.0558 238 LEU D C   
16438 O O   . LEU D 238 ? 1.3109 0.9832 1.0504 0.1028  0.0672  -0.0578 238 LEU D O   
16439 C CB  . LEU D 238 ? 1.2853 0.9929 1.0512 0.0615  0.0647  -0.0478 238 LEU D CB  
16440 C CG  . LEU D 238 ? 1.2586 0.9841 1.0396 0.0469  0.0615  -0.0427 238 LEU D CG  
16441 C CD1 . LEU D 238 ? 1.2458 0.9611 1.0146 0.0289  0.0613  -0.0431 238 LEU D CD1 
16442 C CD2 . LEU D 238 ? 1.2015 0.9656 1.0143 0.0480  0.0634  -0.0412 238 LEU D CD2 
16454 N N   . GLU D 239 ? 1.2839 1.0113 1.0675 0.0977  0.0777  -0.0582 239 GLU D N   
16455 C CA  . GLU D 239 ? 1.3655 1.0815 1.1374 0.1102  0.0848  -0.0635 239 GLU D CA  
16456 C C   . GLU D 239 ? 1.3198 1.0243 1.0738 0.0995  0.0902  -0.0636 239 GLU D C   
16457 O O   . GLU D 239 ? 1.2951 1.0205 1.0634 0.0908  0.0947  -0.0616 239 GLU D O   
16458 C CB  . GLU D 239 ? 1.3509 1.0989 1.1546 0.1238  0.0923  -0.0675 239 GLU D CB  
16459 C CG  . GLU D 239 ? 1.3609 1.0986 1.1533 0.1366  0.1023  -0.0731 239 GLU D CG  
16460 C CD  . GLU D 239 ? 1.3689 1.1357 1.1937 0.1530  0.1091  -0.0791 239 GLU D CD  
16461 O OE1 . GLU D 239 ? 1.3322 1.1342 1.1924 0.1484  0.1133  -0.0788 239 GLU D OE1 
16462 O OE2 . GLU D 239 ? 1.4295 1.1844 1.2451 0.1705  0.1104  -0.0849 239 GLU D OE2 
16469 N N   . TYR D 240 ? 1.3756 1.0448 1.0963 0.1012  0.0890  -0.0663 240 TYR D N   
16470 C CA  . TYR D 240 ? 1.4544 1.1087 1.1543 0.0951  0.0927  -0.0685 240 TYR D CA  
16471 C C   . TYR D 240 ? 1.4700 1.1269 1.1690 0.1108  0.1041  -0.0725 240 TYR D C   
16472 O O   . TYR D 240 ? 1.4612 1.1163 1.1628 0.1271  0.1068  -0.0755 240 TYR D O   
16473 C CB  . TYR D 240 ? 1.4557 1.0697 1.1207 0.0883  0.0857  -0.0707 240 TYR D CB  
16474 C CG  . TYR D 240 ? 1.5329 1.1138 1.1693 0.1030  0.0877  -0.0755 240 TYR D CG  
16475 C CD1 . TYR D 240 ? 1.5435 1.1151 1.1650 0.1109  0.0944  -0.0795 240 TYR D CD1 
16476 C CD2 . TYR D 240 ? 1.5094 1.0650 1.1300 0.1098  0.0830  -0.0758 240 TYR D CD2 
16477 C CE1 . TYR D 240 ? 1.5657 1.1065 1.1601 0.1252  0.0963  -0.0840 240 TYR D CE1 
16478 C CE2 . TYR D 240 ? 1.5560 1.0789 1.1475 0.1243  0.0846  -0.0804 240 TYR D CE2 
16479 C CZ  . TYR D 240 ? 1.5846 1.1013 1.1639 0.1315  0.0912  -0.0846 240 TYR D CZ  
16480 O OH  . TYR D 240 ? 1.6536 1.1379 1.2032 0.1467  0.0932  -0.0894 240 TYR D OH  
16490 N N   . ILE D 241 ? 1.5913 1.2525 1.2861 0.1067  0.1112  -0.0728 241 ILE D N   
16491 C CA  . ILE D 241 ? 1.5445 1.2064 1.2362 0.1204  0.1249  -0.0761 241 ILE D CA  
16492 C C   . ILE D 241 ? 1.5495 1.1886 1.2097 0.1161  0.1272  -0.0777 241 ILE D C   
16493 O O   . ILE D 241 ? 1.5797 1.2287 1.2426 0.1059  0.1275  -0.0753 241 ILE D O   
16494 C CB  . ILE D 241 ? 1.4982 1.1988 1.2274 0.1231  0.1363  -0.0745 241 ILE D CB  
16495 C CG1 . ILE D 241 ? 1.5396 1.2610 1.2865 0.1066  0.1309  -0.0691 241 ILE D CG1 
16496 C CG2 . ILE D 241 ? 1.5018 1.2221 1.2593 0.1356  0.1365  -0.0769 241 ILE D CG2 
16497 C CD1 . ILE D 241 ? 1.5188 1.2742 1.2994 0.1065  0.1420  -0.0675 241 ILE D CD1 
16509 N N   . ILE D 242 ? 1.6007 1.2068 1.2284 0.1250  0.1276  -0.0824 242 ILE D N   
16510 C CA  . ILE D 242 ? 1.6352 1.2152 1.2288 0.1241  0.1287  -0.0854 242 ILE D CA  
16511 C C   . ILE D 242 ? 1.6812 1.2673 1.2744 0.1373  0.1471  -0.0861 242 ILE D C   
16512 O O   . ILE D 242 ? 1.6782 1.2702 1.2814 0.1517  0.1575  -0.0879 242 ILE D O   
16513 C CB  . ILE D 242 ? 1.6602 1.1991 1.2172 0.1277  0.1208  -0.0907 242 ILE D CB  
16514 C CG1 . ILE D 242 ? 1.5704 1.0999 1.1268 0.1134  0.1055  -0.0904 242 ILE D CG1 
16515 C CG2 . ILE D 242 ? 1.6371 1.1482 1.1577 0.1269  0.1194  -0.0951 242 ILE D CG2 
16516 C CD1 . ILE D 242 ? 1.6143 1.1501 1.1857 0.1192  0.1052  -0.0884 242 ILE D CD1 
16528 N N   . GLU D 243 ? 1.6769 1.2602 1.2573 0.1331  0.1516  -0.0852 243 GLU D N   
16529 C CA  . GLU D 243 ? 1.7601 1.3480 1.3392 0.1437  0.1720  -0.0848 243 GLU D CA  
16530 C C   . GLU D 243 ? 1.8000 1.3620 1.3410 0.1423  0.1721  -0.0858 243 GLU D C   
16531 O O   . GLU D 243 ? 1.7809 1.3480 1.3216 0.1304  0.1624  -0.0838 243 GLU D O   
16532 C CB  . GLU D 243 ? 1.7404 1.3689 1.3628 0.1393  0.1823  -0.0802 243 GLU D CB  
16533 C CG  . GLU D 243 ? 1.7731 1.4090 1.4009 0.1489  0.2068  -0.0802 243 GLU D CG  
16534 C CD  . GLU D 243 ? 1.8034 1.4673 1.4584 0.1392  0.2158  -0.0753 243 GLU D CD  
16535 O OE1 . GLU D 243 ? 1.7548 1.4469 1.4438 0.1298  0.2065  -0.0729 243 GLU D OE1 
16536 O OE2 . GLU D 243 ? 1.8118 1.4666 1.4512 0.1413  0.2325  -0.0740 243 GLU D OE2 
16543 N N   . ASN D 244 ? 1.8442 1.3775 1.3518 0.1560  0.1824  -0.0894 244 ASN D N   
16544 C CA  . ASN D 244 ? 1.9210 1.4237 1.3855 0.1583  0.1821  -0.0914 244 ASN D CA  
16545 C C   . ASN D 244 ? 1.9068 1.3971 1.3562 0.1456  0.1572  -0.0943 244 ASN D C   
16546 O O   . ASN D 244 ? 1.9165 1.4096 1.3602 0.1384  0.1509  -0.0933 244 ASN D O   
16547 C CB  . ASN D 244 ? 1.9268 1.4415 1.3958 0.1584  0.1992  -0.0865 244 ASN D CB  
16548 C CG  . ASN D 244 ? 1.9195 1.4639 1.4260 0.1633  0.2221  -0.0834 244 ASN D CG  
16549 O OD1 . ASN D 244 ? 1.9422 1.4874 1.4562 0.1741  0.2307  -0.0863 244 ASN D OD1 
16550 N ND2 . ASN D 244 ? 1.9044 1.4735 1.4353 0.1556  0.2319  -0.0783 244 ASN D ND2 
16557 N N   . ASP D 245 ? 1.8587 1.3358 1.3031 0.1430  0.1433  -0.0986 245 ASP D N   
16558 C CA  . ASP D 245 ? 1.8697 1.3369 1.3058 0.1292  0.1205  -0.1031 245 ASP D CA  
16559 C C   . ASP D 245 ? 1.8444 1.3426 1.3091 0.1140  0.1125  -0.0992 245 ASP D C   
16560 O O   . ASP D 245 ? 1.8503 1.3430 1.3030 0.1063  0.0988  -0.1030 245 ASP D O   
16561 C CB  . ASP D 245 ? 1.9708 1.3989 1.3593 0.1340  0.1118  -0.1110 245 ASP D CB  
16562 C CG  . ASP D 245 ? 2.0220 1.4434 1.3883 0.1426  0.1212  -0.1097 245 ASP D CG  
16563 O OD1 . ASP D 245 ? 1.9911 1.4356 1.3749 0.1354  0.1208  -0.1055 245 ASP D OD1 
16564 O OD2 . ASP D 245 ? 2.0871 1.4765 1.4148 0.1574  0.1295  -0.1128 245 ASP D OD2 
16569 N N   . GLU D 246 ? 1.7782 1.3103 1.2824 0.1107  0.1206  -0.0923 246 GLU D N   
16570 C CA  . GLU D 246 ? 1.7064 1.2691 1.2407 0.0968  0.1136  -0.0881 246 GLU D CA  
16571 C C   . GLU D 246 ? 1.6322 1.2182 1.2023 0.0911  0.1123  -0.0842 246 GLU D C   
16572 O O   . GLU D 246 ? 1.6171 1.2139 1.2032 0.1003  0.1246  -0.0816 246 GLU D O   
16573 C CB  . GLU D 246 ? 1.6988 1.2787 1.2410 0.0997  0.1268  -0.0828 246 GLU D CB  
16574 C CG  . GLU D 246 ? 1.7769 1.3307 1.2792 0.1068  0.1287  -0.0858 246 GLU D CG  
16575 C CD  . GLU D 246 ? 1.7817 1.3479 1.2866 0.0997  0.1230  -0.0835 246 GLU D CD  
16576 O OE1 . GLU D 246 ? 1.7708 1.3611 1.3000 0.0976  0.1346  -0.0768 246 GLU D OE1 
16577 O OE2 . GLU D 246 ? 1.8239 1.3758 1.3068 0.0968  0.1062  -0.0893 246 GLU D OE2 
16584 N N   . MET D 247 ? 1.5441 1.1370 1.1259 0.0768  0.0975  -0.0846 247 MET D N   
16585 C CA  . MET D 247 ? 1.5136 1.1244 1.1244 0.0712  0.0952  -0.0807 247 MET D CA  
16586 C C   . MET D 247 ? 1.4530 1.1002 1.0977 0.0671  0.0998  -0.0741 247 MET D C   
16587 O O   . MET D 247 ? 1.4517 1.1101 1.0990 0.0606  0.0973  -0.0728 247 MET D O   
16588 C CB  . MET D 247 ? 1.4594 1.0598 1.0669 0.0566  0.0799  -0.0838 247 MET D CB  
16589 C CG  . MET D 247 ? 1.3855 0.9907 1.0104 0.0529  0.0781  -0.0805 247 MET D CG  
16590 S SD  . MET D 247 ? 1.5192 1.0888 1.1197 0.0639  0.0798  -0.0838 247 MET D SD  
16591 C CE  . MET D 247 ? 1.4529 1.0465 1.0780 0.0809  0.0917  -0.0787 247 MET D CE  
16601 N N   . TYR D 248 ? 1.4422 1.1067 1.1118 0.0718  0.1054  -0.0705 248 TYR D N   
16602 C CA  . TYR D 248 ? 1.3954 1.0939 1.0989 0.0678  0.1086  -0.0650 248 TYR D CA  
16603 C C   . TYR D 248 ? 1.3884 1.0961 1.1114 0.0658  0.1021  -0.0629 248 TYR D C   
16604 O O   . TYR D 248 ? 1.4182 1.1120 1.1347 0.0749  0.1024  -0.0652 248 TYR D O   
16605 C CB  . TYR D 248 ? 1.4266 1.1406 1.1438 0.0782  0.1252  -0.0638 248 TYR D CB  
16606 C CG  . TYR D 248 ? 1.4560 1.1565 1.1494 0.0820  0.1348  -0.0650 248 TYR D CG  
16607 C CD1 . TYR D 248 ? 1.4230 1.1304 1.1143 0.0744  0.1342  -0.0623 248 TYR D CD1 
16608 C CD2 . TYR D 248 ? 1.5083 1.1866 1.1783 0.0945  0.1446  -0.0689 248 TYR D CD2 
16609 C CE1 . TYR D 248 ? 1.4857 1.1760 1.1498 0.0795  0.1428  -0.0633 248 TYR D CE1 
16610 C CE2 . TYR D 248 ? 1.5604 1.2224 1.2042 0.0990  0.1540  -0.0697 248 TYR D CE2 
16611 C CZ  . TYR D 248 ? 1.5592 1.2261 1.1990 0.0917  0.1530  -0.0668 248 TYR D CZ  
16612 O OH  . TYR D 248 ? 1.6290 1.2746 1.2370 0.0980  0.1624  -0.0676 248 TYR D OH  
16622 N N   . ILE D 249 ? 1.3600 1.0880 1.1035 0.0551  0.0961  -0.0588 249 ILE D N   
16623 C CA  . ILE D 249 ? 1.2629 0.9988 1.0229 0.0536  0.0901  -0.0562 249 ILE D CA  
16624 C C   . ILE D 249 ? 1.2402 1.0086 1.0329 0.0570  0.0951  -0.0529 249 ILE D C   
16625 O O   . ILE D 249 ? 1.2048 0.9916 1.0099 0.0494  0.0963  -0.0499 249 ILE D O   
16626 C CB  . ILE D 249 ? 1.2869 1.0178 1.0429 0.0381  0.0792  -0.0548 249 ILE D CB  
16627 C CG1 . ILE D 249 ? 1.2979 0.9955 1.0243 0.0340  0.0743  -0.0598 249 ILE D CG1 
16628 C CG2 . ILE D 249 ? 1.2814 1.0210 1.0536 0.0367  0.0748  -0.0508 249 ILE D CG2 
16629 C CD1 . ILE D 249 ? 1.2845 0.9573 0.9973 0.0409  0.0735  -0.0609 249 ILE D CD1 
16641 N N   . ASP D 250 ? 1.2478 1.0224 1.0539 0.0692  0.0978  -0.0544 250 ASP D N   
16642 C CA  . ASP D 250 ? 1.2394 1.0448 1.0795 0.0732  0.1004  -0.0532 250 ASP D CA  
16643 C C   . ASP D 250 ? 1.2342 1.0409 1.0816 0.0728  0.0889  -0.0512 250 ASP D C   
16644 O O   . ASP D 250 ? 1.2802 1.0613 1.1060 0.0743  0.0823  -0.0516 250 ASP D O   
16645 C CB  . ASP D 250 ? 1.2447 1.0592 1.0981 0.0887  0.1106  -0.0584 250 ASP D CB  
16646 C CG  . ASP D 250 ? 1.1722 1.0221 1.0635 0.0892  0.1179  -0.0589 250 ASP D CG  
16647 O OD1 . ASP D 250 ? 1.1836 1.0511 1.0954 0.0851  0.1102  -0.0568 250 ASP D OD1 
16648 O OD2 . ASP D 250 ? 1.2636 1.1225 1.1637 0.0936  0.1323  -0.0617 250 ASP D OD2 
16653 N N   . GLY D 251 ? 1.1819 1.0157 1.0577 0.0709  0.0871  -0.0491 251 GLY D N   
16654 C CA  . GLY D 251 ? 1.1893 1.0243 1.0713 0.0726  0.0765  -0.0474 251 GLY D CA  
16655 C C   . GLY D 251 ? 1.1545 1.0196 1.0665 0.0688  0.0744  -0.0452 251 GLY D C   
16656 O O   . GLY D 251 ? 1.1268 1.0113 1.0545 0.0625  0.0818  -0.0444 251 GLY D O   
16660 N N   . PRO D 252 ? 1.1439 1.0100 1.0612 0.0728  0.0644  -0.0442 252 PRO D N   
16661 C CA  . PRO D 252 ? 1.1168 1.0099 1.0619 0.0702  0.0609  -0.0430 252 PRO D CA  
16662 C C   . PRO D 252 ? 1.0813 0.9741 1.0202 0.0553  0.0574  -0.0361 252 PRO D C   
16663 O O   . PRO D 252 ? 1.0831 0.9541 0.9980 0.0485  0.0543  -0.0325 252 PRO D O   
16664 C CB  . PRO D 252 ? 1.0551 0.9460 1.0048 0.0851  0.0503  -0.0465 252 PRO D CB  
16665 C CG  . PRO D 252 ? 1.1203 0.9775 1.0385 0.0938  0.0483  -0.0478 252 PRO D CG  
16666 C CD  . PRO D 252 ? 1.1594 0.9991 1.0552 0.0820  0.0562  -0.0449 252 PRO D CD  
16674 N N   . VAL D 253 ? 1.0810 0.9990 1.0437 0.0503  0.0584  -0.0349 253 VAL D N   
16675 C CA  . VAL D 253 ? 1.0716 0.9942 1.0328 0.0380  0.0552  -0.0289 253 VAL D CA  
16676 C C   . VAL D 253 ? 1.0414 0.9864 1.0286 0.0407  0.0503  -0.0294 253 VAL D C   
16677 O O   . VAL D 253 ? 1.0066 0.9722 1.0184 0.0431  0.0557  -0.0335 253 VAL D O   
16678 C CB  . VAL D 253 ? 1.0647 0.9913 1.0217 0.0270  0.0631  -0.0268 253 VAL D CB  
16679 C CG1 . VAL D 253 ? 1.0217 0.9466 0.9697 0.0156  0.0581  -0.0215 253 VAL D CG1 
16680 C CG2 . VAL D 253 ? 1.0454 0.9540 0.9824 0.0282  0.0690  -0.0293 253 VAL D CG2 
16690 N N   . GLU D 254 ? 1.0235 0.9634 1.0051 0.0399  0.0409  -0.0259 254 GLU D N   
16691 C CA  . GLU D 254 ? 0.9905 0.9483 0.9927 0.0421  0.0344  -0.0263 254 GLU D CA  
16692 C C   . GLU D 254 ? 0.9817 0.9427 0.9795 0.0299  0.0337  -0.0198 254 GLU D C   
16693 O O   . GLU D 254 ? 0.9823 0.9269 0.9586 0.0241  0.0324  -0.0151 254 GLU D O   
16694 C CB  . GLU D 254 ? 1.0507 0.9976 1.0475 0.0552  0.0227  -0.0284 254 GLU D CB  
16695 C CG  . GLU D 254 ? 1.0783 1.0419 1.0946 0.0587  0.0136  -0.0299 254 GLU D CG  
16696 C CD  . GLU D 254 ? 1.1351 1.0857 1.1431 0.0747  0.0004  -0.0332 254 GLU D CD  
16697 O OE1 . GLU D 254 ? 1.1727 1.0936 1.1492 0.0781  -0.0016 -0.0294 254 GLU D OE1 
16698 O OE2 . GLU D 254 ? 1.1069 1.0754 1.1388 0.0840  -0.0080 -0.0400 254 GLU D OE2 
16705 N N   . ILE D 255 ? 0.9745 0.9564 0.9932 0.0260  0.0351  -0.0201 255 ILE D N   
16706 C CA  . ILE D 255 ? 0.9670 0.9527 0.9823 0.0169  0.0331  -0.0144 255 ILE D CA  
16707 C C   . ILE D 255 ? 0.9674 0.9496 0.9816 0.0227  0.0217  -0.0133 255 ILE D C   
16708 O O   . ILE D 255 ? 0.9722 0.9647 1.0042 0.0310  0.0156  -0.0180 255 ILE D O   
16709 C CB  . ILE D 255 ? 0.9843 0.9886 1.0180 0.0111  0.0394  -0.0151 255 ILE D CB  
16710 C CG1 . ILE D 255 ? 0.9969 1.0005 1.0281 0.0078  0.0518  -0.0167 255 ILE D CG1 
16711 C CG2 . ILE D 255 ? 0.9479 0.9535 0.9739 0.0029  0.0371  -0.0092 255 ILE D CG2 
16712 C CD1 . ILE D 255 ? 0.9602 0.9474 0.9651 0.0029  0.0538  -0.0133 255 ILE D CD1 
16724 N N   . ILE D 256 ? 0.9810 0.9485 0.9743 0.0186  0.0191  -0.0076 256 ILE D N   
16725 C CA  . ILE D 256 ? 0.9693 0.9260 0.9534 0.0251  0.0099  -0.0058 256 ILE D CA  
16726 C C   . ILE D 256 ? 0.9906 0.9598 0.9832 0.0214  0.0061  -0.0030 256 ILE D C   
16727 O O   . ILE D 256 ? 0.9915 0.9675 0.9959 0.0290  -0.0021 -0.0059 256 ILE D O   
16728 C CB  . ILE D 256 ? 1.0056 0.9367 0.9614 0.0222  0.0117  -0.0013 256 ILE D CB  
16729 C CG1 . ILE D 256 ? 1.0090 0.9218 0.9525 0.0289  0.0132  -0.0045 256 ILE D CG1 
16730 C CG2 . ILE D 256 ? 0.9822 0.9003 0.9243 0.0267  0.0052  0.0024  256 ILE D CG2 
16731 C CD1 . ILE D 256 ? 1.0433 0.9556 0.9941 0.0453  0.0052  -0.0103 256 ILE D CD1 
16743 N N   . ALA D 257 ? 0.9574 0.9298 0.9443 0.0105  0.0111  0.0018  257 ALA D N   
16744 C CA  . ALA D 257 ? 0.9423 0.9233 0.9328 0.0077  0.0077  0.0050  257 ALA D CA  
16745 C C   . ALA D 257 ? 0.9311 0.9212 0.9213 -0.0028 0.0144  0.0075  257 ALA D C   
16746 O O   . ALA D 257 ? 0.9386 0.9267 0.9238 -0.0076 0.0206  0.0068  257 ALA D O   
16747 C CB  . ALA D 257 ? 0.9969 0.9622 0.9691 0.0106  0.0028  0.0093  257 ALA D CB  
16753 N N   . GLU D 258 ? 0.9666 0.9648 0.9599 -0.0050 0.0120  0.0100  258 GLU D N   
16754 C CA  . GLU D 258 ? 0.9535 0.9588 0.9438 -0.0124 0.0165  0.0122  258 GLU D CA  
16755 C C   . GLU D 258 ? 0.9375 0.9466 0.9264 -0.0122 0.0119  0.0155  258 GLU D C   
16756 O O   . GLU D 258 ? 0.9725 0.9826 0.9685 -0.0073 0.0061  0.0148  258 GLU D O   
16757 C CB  . GLU D 258 ? 0.9093 0.9222 0.9093 -0.0146 0.0229  0.0092  258 GLU D CB  
16758 C CG  . GLU D 258 ? 0.9449 0.9666 0.9603 -0.0136 0.0221  0.0077  258 GLU D CG  
16759 C CD  . GLU D 258 ? 0.9666 0.9924 0.9891 -0.0171 0.0320  0.0052  258 GLU D CD  
16760 O OE1 . GLU D 258 ? 1.0215 1.0434 1.0304 -0.0210 0.0372  0.0074  258 GLU D OE1 
16761 O OE2 . GLU D 258 ? 0.9443 0.9766 0.9855 -0.0155 0.0347  0.0004  258 GLU D OE2 
16768 N N   . GLY D 259 ? 0.9081 0.9197 0.8879 -0.0167 0.0137  0.0181  259 GLY D N   
16769 C CA  . GLY D 259 ? 0.9282 0.9429 0.9044 -0.0159 0.0099  0.0213  259 GLY D CA  
16770 C C   . GLY D 259 ? 0.9479 0.9658 0.9144 -0.0195 0.0115  0.0230  259 GLY D C   
16771 O O   . GLY D 259 ? 0.9799 1.0022 0.9444 -0.0227 0.0146  0.0211  259 GLY D O   
16775 N N   . LYS D 260 ? 0.9743 0.9900 0.9347 -0.0181 0.0094  0.0258  260 LYS D N   
16776 C CA  . LYS D 260 ? 0.9624 0.9849 0.9178 -0.0209 0.0109  0.0264  260 LYS D CA  
16777 C C   . LYS D 260 ? 0.9540 0.9703 0.9053 -0.0234 0.0145  0.0272  260 LYS D C   
16778 O O   . LYS D 260 ? 0.9800 0.9840 0.9253 -0.0197 0.0138  0.0299  260 LYS D O   
16779 C CB  . LYS D 260 ? 0.9514 0.9779 0.9028 -0.0167 0.0072  0.0290  260 LYS D CB  
16780 C CG  . LYS D 260 ? 1.0001 1.0287 0.9523 -0.0152 0.0054  0.0285  260 LYS D CG  
16781 C CD  . LYS D 260 ? 0.9821 1.0179 0.9294 -0.0163 0.0066  0.0263  260 LYS D CD  
16782 C CE  . LYS D 260 ? 1.0420 1.0737 0.9845 -0.0148 0.0070  0.0263  260 LYS D CE  
16783 N NZ  . LYS D 260 ? 1.1509 1.1770 1.1022 -0.0168 0.0100  0.0256  260 LYS D NZ  
16797 N N   . ILE D 261 ? 0.9241 0.9476 0.8776 -0.0297 0.0184  0.0242  261 ILE D N   
16798 C CA  . ILE D 261 ? 0.9694 0.9876 0.9206 -0.0348 0.0244  0.0241  261 ILE D CA  
16799 C C   . ILE D 261 ? 0.9590 0.9924 0.9145 -0.0368 0.0261  0.0229  261 ILE D C   
16800 O O   . ILE D 261 ? 0.9721 1.0213 0.9334 -0.0363 0.0223  0.0193  261 ILE D O   
16801 C CB  . ILE D 261 ? 0.9701 0.9839 0.9238 -0.0420 0.0284  0.0198  261 ILE D CB  
16802 C CG1 . ILE D 261 ? 0.9814 0.9897 0.9338 -0.0498 0.0367  0.0188  261 ILE D CG1 
16803 C CG2 . ILE D 261 ? 0.9728 1.0009 0.9337 -0.0445 0.0255  0.0142  261 ILE D CG2 
16804 C CD1 . ILE D 261 ? 1.0703 1.0660 1.0206 -0.0566 0.0411  0.0155  261 ILE D CD1 
16816 N N   . TYR D 262 ? 0.9594 0.9870 0.9104 -0.0378 0.0319  0.0255  262 TYR D N   
16817 C CA  . TYR D 262 ? 0.9659 1.0086 0.9224 -0.0389 0.0350  0.0242  262 TYR D CA  
16818 C C   . TYR D 262 ? 1.0096 1.0560 0.9748 -0.0499 0.0450  0.0196  262 TYR D C   
16819 O O   . TYR D 262 ? 1.0419 1.0688 0.9986 -0.0540 0.0533  0.0222  262 TYR D O   
16820 C CB  . TYR D 262 ? 0.9425 0.9756 0.8869 -0.0313 0.0358  0.0305  262 TYR D CB  
16821 C CG  . TYR D 262 ? 0.9263 0.9516 0.8623 -0.0219 0.0262  0.0344  262 TYR D CG  
16822 C CD1 . TYR D 262 ? 0.8926 0.9301 0.8306 -0.0168 0.0194  0.0340  262 TYR D CD1 
16823 C CD2 . TYR D 262 ? 0.9619 0.9670 0.8881 -0.0180 0.0239  0.0376  262 TYR D CD2 
16824 C CE1 . TYR D 262 ? 0.8713 0.9010 0.8033 -0.0102 0.0119  0.0366  262 TYR D CE1 
16825 C CE2 . TYR D 262 ? 0.9404 0.9414 0.8638 -0.0105 0.0149  0.0392  262 TYR D CE2 
16826 C CZ  . TYR D 262 ? 0.9223 0.9356 0.8494 -0.0078 0.0097  0.0388  262 TYR D CZ  
16827 O OH  . TYR D 262 ? 0.9168 0.9253 0.8428 -0.0024 0.0020  0.0396  262 TYR D OH  
16837 N N   . ILE D 263 ? 1.0281 1.0986 1.0098 -0.0542 0.0440  0.0121  263 ILE D N   
16838 C CA  . ILE D 263 ? 1.0906 1.1701 1.0869 -0.0662 0.0529  0.0052  263 ILE D CA  
16839 C C   . ILE D 263 ? 1.1278 1.2324 1.1387 -0.0656 0.0549  0.0007  263 ILE D C   
16840 O O   . ILE D 263 ? 1.1194 1.2433 1.1363 -0.0584 0.0448  -0.0031 263 ILE D O   
16841 C CB  . ILE D 263 ? 1.0976 1.1847 1.1042 -0.0727 0.0482  -0.0032 263 ILE D CB  
16842 C CG1 . ILE D 263 ? 1.0776 1.1392 1.0703 -0.0737 0.0485  0.0007  263 ILE D CG1 
16843 C CG2 . ILE D 263 ? 1.1525 1.2546 1.1794 -0.0856 0.0558  -0.0129 263 ILE D CG2 
16844 C CD1 . ILE D 263 ? 1.0693 1.1314 1.0570 -0.0662 0.0376  0.0007  263 ILE D CD1 
16856 N N   . GLY D 264 ? 1.3247 1.4276 1.3400 -0.0725 0.0685  0.0008  264 GLY D N   
16857 C CA  . GLY D 264 ? 1.3689 1.4990 1.4030 -0.0733 0.0725  -0.0054 264 GLY D CA  
16858 C C   . GLY D 264 ? 1.3462 1.5053 1.4080 -0.0811 0.0684  -0.0192 264 GLY D C   
16859 O O   . GLY D 264 ? 1.3546 1.5087 1.4213 -0.0904 0.0681  -0.0240 264 GLY D O   
16863 N N   . LYS D 265 ? 1.3849 1.5744 1.4644 -0.0761 0.0640  -0.0266 265 LYS D N   
16864 C CA  . LYS D 265 ? 1.4936 1.7141 1.6014 -0.0813 0.0576  -0.0420 265 LYS D CA  
16865 C C   . LYS D 265 ? 1.5215 1.7590 1.6573 -0.0961 0.0735  -0.0506 265 LYS D C   
16866 O O   . LYS D 265 ? 1.4915 1.7279 1.6274 -0.0968 0.0872  -0.0461 265 LYS D O   
16867 C CB  . LYS D 265 ? 1.4666 1.7115 1.5786 -0.0660 0.0423  -0.0473 265 LYS D CB  
16868 C CG  . LYS D 265 ? 1.5045 1.7850 1.6472 -0.0683 0.0339  -0.0653 265 LYS D CG  
16869 C CD  . LYS D 265 ? 1.5052 1.7811 1.6520 -0.0771 0.0276  -0.0725 265 LYS D CD  
16870 C CE  . LYS D 265 ? 1.4778 1.7890 1.6616 -0.0847 0.0236  -0.0921 265 LYS D CE  
16871 N NZ  . LYS D 265 ? 1.4225 1.7450 1.6336 -0.1021 0.0430  -0.0967 265 LYS D NZ  
# 
