data_8VYD
# 
_entry.id   8VYD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8VYD         pdb_00008vyd 10.2210/pdb8vyd/pdb 
WWPDB D_1000281212 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        8VYD 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-08 
_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           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 thomas.santangelo@colostate.edu Thomas Santangelo J     'principal investigator/group leader' 0000-0003-4559-3244 
5 shing.ho@colostate.edu          Pui    Ho         Shing 'principal investigator/group leader' 0000-0002-8082-4311 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ho, P.S.'         1 0000-0002-8082-4311 
'Santangelo, T.J.' 2 0000-0003-4559-3244 
'Fluke, K.'        3 0000-0002-3398-3184 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'A novel synthase generates m4(2)C to stabilize the archaeal ribosome' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fluke, K.'        1  0000-0002-3398-3184 
primary 'Dai, N.'          2  ?                   
primary 'Fuchs, R.T.'      3  0000-0001-8238-6442 
primary 'Ho, P.S.'         4  0000-0002-8082-4311 
primary 'Febvre, H.P.'     5  ?                   
primary 'Talbott, V.'      6  0009-0000-6078-997X 
primary 'Wolf, E.J.'       7  ?                   
primary 'Tsai, Y.-L.'      8  ?                   
primary 'Elkins, L.'       9  0009-0007-7060-4511 
primary 'Schiltz, J.'      10 ?                   
primary 'Czarny, R.'       11 ?                   
primary 'Robb, B.'         12 ?                   
primary 'Correa Jr, I.R.'  13 0000-0002-3169-6878 
primary 'Santangelo, T.J.' 14 0000-0003-4559-3244 
# 
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 'SAM-dependent methyltransferase, UPF0020 family' 32947.027 2   ? ? ? ? 
2 non-polymer syn 'SODIUM ION'                                      22.990    6   ? ? ? ? 
3 water       nat water                                             18.015    182 ? ? ? ? 
# 
_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       
;MEEIYYITFREARMLLASRGNVKLNLDLRKTNRVQEVEIKDEGAVFPDGTLVEREVLEKIARDDGTVYFVSNGGVYKAAI
AGESGFYKLVPTIPPTIEINGIAMHRTKEMNPLQDTRNKVNTVMPREGETVLDTCMGLGYTAIEASKRGAYVITIEKDPN
VIEIARINPWSRELFTGGKIQVIQGDAFEVVKKFKQASFDVIIHDPPRFSLAGHLYSEEFYRELFRILKPGGRLFHYVGN
PGKKYRRKDLQKGVMERLRRVGFVGVRRVEEALGVVARKPEKGVKASQRD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEEIYYITFREARMLLASRGNVKLNLDLRKTNRVQEVEIKDEGAVFPDGTLVEREVLEKIARDDGTVYFVSNGGVYKAAI
AGESGFYKLVPTIPPTIEINGIAMHRTKEMNPLQDTRNKVNTVMPREGETVLDTCMGLGYTAIEASKRGAYVITIEKDPN
VIEIARINPWSRELFTGGKIQVIQGDAFEVVKKFKQASFDVIIHDPPRFSLAGHLYSEEFYRELFRILKPGGRLFHYVGN
PGKKYRRKDLQKGVMERLRRVGFVGVRRVEEALGVVARKPEKGVKASQRD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SODIUM ION' NA  
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   GLU n 
1 3   GLU n 
1 4   ILE n 
1 5   TYR n 
1 6   TYR n 
1 7   ILE n 
1 8   THR n 
1 9   PHE n 
1 10  ARG n 
1 11  GLU n 
1 12  ALA n 
1 13  ARG n 
1 14  MET n 
1 15  LEU n 
1 16  LEU n 
1 17  ALA n 
1 18  SER n 
1 19  ARG n 
1 20  GLY n 
1 21  ASN n 
1 22  VAL n 
1 23  LYS n 
1 24  LEU n 
1 25  ASN n 
1 26  LEU n 
1 27  ASP n 
1 28  LEU n 
1 29  ARG n 
1 30  LYS n 
1 31  THR n 
1 32  ASN n 
1 33  ARG n 
1 34  VAL n 
1 35  GLN n 
1 36  GLU n 
1 37  VAL n 
1 38  GLU n 
1 39  ILE n 
1 40  LYS n 
1 41  ASP n 
1 42  GLU n 
1 43  GLY n 
1 44  ALA n 
1 45  VAL n 
1 46  PHE n 
1 47  PRO n 
1 48  ASP n 
1 49  GLY n 
1 50  THR n 
1 51  LEU n 
1 52  VAL n 
1 53  GLU n 
1 54  ARG n 
1 55  GLU n 
1 56  VAL n 
1 57  LEU n 
1 58  GLU n 
1 59  LYS n 
1 60  ILE n 
1 61  ALA n 
1 62  ARG n 
1 63  ASP n 
1 64  ASP n 
1 65  GLY n 
1 66  THR n 
1 67  VAL n 
1 68  TYR n 
1 69  PHE n 
1 70  VAL n 
1 71  SER n 
1 72  ASN n 
1 73  GLY n 
1 74  GLY n 
1 75  VAL n 
1 76  TYR n 
1 77  LYS n 
1 78  ALA n 
1 79  ALA n 
1 80  ILE n 
1 81  ALA n 
1 82  GLY n 
1 83  GLU n 
1 84  SER n 
1 85  GLY n 
1 86  PHE n 
1 87  TYR n 
1 88  LYS n 
1 89  LEU n 
1 90  VAL n 
1 91  PRO n 
1 92  THR n 
1 93  ILE n 
1 94  PRO n 
1 95  PRO n 
1 96  THR n 
1 97  ILE n 
1 98  GLU n 
1 99  ILE n 
1 100 ASN n 
1 101 GLY n 
1 102 ILE n 
1 103 ALA n 
1 104 MET n 
1 105 HIS n 
1 106 ARG n 
1 107 THR n 
1 108 LYS n 
1 109 GLU n 
1 110 MET n 
1 111 ASN n 
1 112 PRO n 
1 113 LEU n 
1 114 GLN n 
1 115 ASP n 
1 116 THR n 
1 117 ARG n 
1 118 ASN n 
1 119 LYS n 
1 120 VAL n 
1 121 ASN n 
1 122 THR n 
1 123 VAL n 
1 124 MET n 
1 125 PRO n 
1 126 ARG n 
1 127 GLU n 
1 128 GLY n 
1 129 GLU n 
1 130 THR n 
1 131 VAL n 
1 132 LEU n 
1 133 ASP n 
1 134 THR n 
1 135 CYS n 
1 136 MET n 
1 137 GLY n 
1 138 LEU n 
1 139 GLY n 
1 140 TYR n 
1 141 THR n 
1 142 ALA n 
1 143 ILE n 
1 144 GLU n 
1 145 ALA n 
1 146 SER n 
1 147 LYS n 
1 148 ARG n 
1 149 GLY n 
1 150 ALA n 
1 151 TYR n 
1 152 VAL n 
1 153 ILE n 
1 154 THR n 
1 155 ILE n 
1 156 GLU n 
1 157 LYS n 
1 158 ASP n 
1 159 PRO n 
1 160 ASN n 
1 161 VAL n 
1 162 ILE n 
1 163 GLU n 
1 164 ILE n 
1 165 ALA n 
1 166 ARG n 
1 167 ILE n 
1 168 ASN n 
1 169 PRO n 
1 170 TRP n 
1 171 SER n 
1 172 ARG n 
1 173 GLU n 
1 174 LEU n 
1 175 PHE n 
1 176 THR n 
1 177 GLY n 
1 178 GLY n 
1 179 LYS n 
1 180 ILE n 
1 181 GLN n 
1 182 VAL n 
1 183 ILE n 
1 184 GLN n 
1 185 GLY n 
1 186 ASP n 
1 187 ALA n 
1 188 PHE n 
1 189 GLU n 
1 190 VAL n 
1 191 VAL n 
1 192 LYS n 
1 193 LYS n 
1 194 PHE n 
1 195 LYS n 
1 196 GLN n 
1 197 ALA n 
1 198 SER n 
1 199 PHE n 
1 200 ASP n 
1 201 VAL n 
1 202 ILE n 
1 203 ILE n 
1 204 HIS n 
1 205 ASP n 
1 206 PRO n 
1 207 PRO n 
1 208 ARG n 
1 209 PHE n 
1 210 SER n 
1 211 LEU n 
1 212 ALA n 
1 213 GLY n 
1 214 HIS n 
1 215 LEU n 
1 216 TYR n 
1 217 SER n 
1 218 GLU n 
1 219 GLU n 
1 220 PHE n 
1 221 TYR n 
1 222 ARG n 
1 223 GLU n 
1 224 LEU n 
1 225 PHE n 
1 226 ARG n 
1 227 ILE n 
1 228 LEU n 
1 229 LYS n 
1 230 PRO n 
1 231 GLY n 
1 232 GLY n 
1 233 ARG n 
1 234 LEU n 
1 235 PHE n 
1 236 HIS n 
1 237 TYR n 
1 238 VAL n 
1 239 GLY n 
1 240 ASN n 
1 241 PRO n 
1 242 GLY n 
1 243 LYS n 
1 244 LYS n 
1 245 TYR n 
1 246 ARG n 
1 247 ARG n 
1 248 LYS n 
1 249 ASP n 
1 250 LEU n 
1 251 GLN n 
1 252 LYS n 
1 253 GLY n 
1 254 VAL n 
1 255 MET n 
1 256 GLU n 
1 257 ARG n 
1 258 LEU n 
1 259 ARG n 
1 260 ARG n 
1 261 VAL n 
1 262 GLY n 
1 263 PHE n 
1 264 VAL n 
1 265 GLY n 
1 266 VAL n 
1 267 ARG n 
1 268 ARG n 
1 269 VAL n 
1 270 GLU n 
1 271 GLU n 
1 272 ALA n 
1 273 LEU n 
1 274 GLY n 
1 275 VAL n 
1 276 VAL n 
1 277 ALA n 
1 278 ARG n 
1 279 LYS n 
1 280 PRO n 
1 281 GLU n 
1 282 LYS n 
1 283 GLY n 
1 284 VAL n 
1 285 LYS n 
1 286 ALA n 
1 287 SER n 
1 288 GLN n 
1 289 ARG n 
1 290 ASP 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                   290 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TK2045 
_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      'Thermococcus kodakarensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     311400 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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              Rosetta2 
_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 
NA  non-polymer         . 'SODIUM ION'    ? 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_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   GLU 2   2   2   GLU GLU A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   TYR 5   5   5   TYR TYR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 MET 104 104 ?   ?   ?   A . n 
A 1 105 HIS 105 105 ?   ?   ?   A . n 
A 1 106 ARG 106 106 ?   ?   ?   A . n 
A 1 107 THR 107 107 ?   ?   ?   A . n 
A 1 108 LYS 108 108 ?   ?   ?   A . n 
A 1 109 GLU 109 109 ?   ?   ?   A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 MET 124 124 124 MET MET A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 CYS 135 135 135 CYS CYS A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 TRP 170 170 170 TRP TRP A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 GLN 196 196 196 GLN GLN A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 ASN 240 240 ?   ?   ?   A . n 
A 1 241 PRO 241 241 ?   ?   ?   A . n 
A 1 242 GLY 242 242 ?   ?   ?   A . n 
A 1 243 LYS 243 243 ?   ?   ?   A . n 
A 1 244 LYS 244 244 ?   ?   ?   A . n 
A 1 245 TYR 245 245 ?   ?   ?   A . n 
A 1 246 ARG 246 246 ?   ?   ?   A . n 
A 1 247 ARG 247 247 ?   ?   ?   A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 ARG 267 267 267 ARG ARG A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 GLY 283 283 ?   ?   ?   A . n 
A 1 284 VAL 284 284 ?   ?   ?   A . n 
A 1 285 LYS 285 285 ?   ?   ?   A . n 
A 1 286 ALA 286 286 ?   ?   ?   A . n 
A 1 287 SER 287 287 ?   ?   ?   A . n 
A 1 288 GLN 288 288 ?   ?   ?   A . n 
A 1 289 ARG 289 289 ?   ?   ?   A . n 
A 1 290 ASP 290 290 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   2   GLU GLU B . n 
B 1 3   GLU 3   3   3   GLU GLU B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   TYR 5   5   5   TYR TYR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   ILE 7   7   7   ILE ILE B . n 
B 1 8   THR 8   8   8   THR THR B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  MET 14  14  14  MET MET B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  VAL 22  22  22  VAL VAL B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  ASN 25  25  25  ASN ASN B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  LEU 28  28  28  LEU LEU B . n 
B 1 29  ARG 29  29  29  ARG ARG B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  THR 31  31  31  THR THR B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  VAL 37  37  37  VAL VAL B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  LYS 40  40  40  LYS LYS B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  GLY 43  43  43  GLY GLY B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  PHE 46  46  46  PHE PHE B . n 
B 1 47  PRO 47  47  47  PRO PRO B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  ASP 64  64  64  ASP ASP B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  VAL 67  67  67  VAL VAL B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  PHE 69  69  69  PHE PHE B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  SER 71  71  71  SER SER B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  THR 92  92  92  THR THR B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 ASN 100 100 100 ASN ASN B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 ALA 103 103 ?   ?   ?   B . n 
B 1 104 MET 104 104 ?   ?   ?   B . n 
B 1 105 HIS 105 105 ?   ?   ?   B . n 
B 1 106 ARG 106 106 ?   ?   ?   B . n 
B 1 107 THR 107 107 ?   ?   ?   B . n 
B 1 108 LYS 108 108 ?   ?   ?   B . n 
B 1 109 GLU 109 109 ?   ?   ?   B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLN 114 114 114 GLN GLN B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASN 121 121 121 ASN ASN B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 MET 124 124 124 MET MET B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 ARG 126 126 126 ARG ARG B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 THR 130 130 130 THR THR B . n 
B 1 131 VAL 131 131 131 VAL VAL B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 CYS 135 135 135 CYS CYS B . n 
B 1 136 MET 136 136 136 MET MET B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 SER 146 146 146 SER SER B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 TYR 151 151 151 TYR TYR B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 GLU 156 156 156 GLU GLU B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 ASN 160 160 160 ASN ASN B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 ARG 166 166 166 ARG ARG B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 ASN 168 168 168 ASN ASN B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 TRP 170 170 170 TRP TRP B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 GLU 173 173 173 GLU GLU B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 LYS 179 179 179 LYS LYS B . n 
B 1 180 ILE 180 180 180 ILE ILE B . n 
B 1 181 GLN 181 181 181 GLN GLN B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 GLN 184 184 184 GLN GLN B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 PHE 188 188 188 PHE PHE B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 LYS 192 192 192 LYS LYS B . n 
B 1 193 LYS 193 193 193 LYS LYS B . n 
B 1 194 PHE 194 194 194 PHE PHE B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 GLN 196 196 196 GLN GLN B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 HIS 204 204 204 HIS HIS B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ARG 208 208 208 ARG ARG B . n 
B 1 209 PHE 209 209 209 PHE PHE B . n 
B 1 210 SER 210 210 210 SER SER B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 GLY 213 213 213 GLY GLY B . n 
B 1 214 HIS 214 214 214 HIS HIS B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 TYR 216 216 216 TYR TYR B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 GLU 218 218 218 GLU GLU B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 PHE 220 220 220 PHE PHE B . n 
B 1 221 TYR 221 221 221 TYR TYR B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 ILE 227 227 227 ILE ILE B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 LYS 229 229 229 LYS LYS B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 ARG 233 233 233 ARG ARG B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 HIS 236 236 236 HIS HIS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 VAL 238 238 238 VAL VAL B . n 
B 1 239 GLY 239 239 ?   ?   ?   B . n 
B 1 240 ASN 240 240 ?   ?   ?   B . n 
B 1 241 PRO 241 241 ?   ?   ?   B . n 
B 1 242 GLY 242 242 ?   ?   ?   B . n 
B 1 243 LYS 243 243 ?   ?   ?   B . n 
B 1 244 LYS 244 244 ?   ?   ?   B . n 
B 1 245 TYR 245 245 ?   ?   ?   B . n 
B 1 246 ARG 246 246 ?   ?   ?   B . n 
B 1 247 ARG 247 247 ?   ?   ?   B . n 
B 1 248 LYS 248 248 ?   ?   ?   B . n 
B 1 249 ASP 249 249 249 ASP ASP B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 MET 255 255 255 MET MET B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 ARG 257 257 257 ARG ARG B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 PHE 263 263 263 PHE PHE B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 ARG 267 267 267 ARG ARG B . n 
B 1 268 ARG 268 268 268 ARG ARG B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 ARG 278 278 278 ARG ARG B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 PRO 280 280 280 PRO PRO B . n 
B 1 281 GLU 281 281 281 GLU GLU B . n 
B 1 282 LYS 282 282 ?   ?   ?   B . n 
B 1 283 GLY 283 283 ?   ?   ?   B . n 
B 1 284 VAL 284 284 ?   ?   ?   B . n 
B 1 285 LYS 285 285 ?   ?   ?   B . n 
B 1 286 ALA 286 286 ?   ?   ?   B . n 
B 1 287 SER 287 287 ?   ?   ?   B . n 
B 1 288 GLN 288 288 ?   ?   ?   B . n 
B 1 289 ARG 289 289 ?   ?   ?   B . n 
B 1 290 ASP 290 290 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NA  1   301 1   NA  NA  A . 
D 2 NA  1   302 2   NA  NA  A . 
E 2 NA  1   303 3   NA  NA  A . 
F 2 NA  1   304 4   NA  NA  A . 
G 2 NA  1   305 5   NA  NA  A . 
H 2 NA  1   306 8   NA  NA  A . 
I 3 HOH 1   401 85  HOH HOH A . 
I 3 HOH 2   402 167 HOH HOH A . 
I 3 HOH 3   403 137 HOH HOH A . 
I 3 HOH 4   404 3   HOH HOH A . 
I 3 HOH 5   405 73  HOH HOH A . 
I 3 HOH 6   406 186 HOH HOH A . 
I 3 HOH 7   407 90  HOH HOH A . 
I 3 HOH 8   408 123 HOH HOH A . 
I 3 HOH 9   409 152 HOH HOH A . 
I 3 HOH 10  410 33  HOH HOH A . 
I 3 HOH 11  411 7   HOH HOH A . 
I 3 HOH 12  412 30  HOH HOH A . 
I 3 HOH 13  413 8   HOH HOH A . 
I 3 HOH 14  414 67  HOH HOH A . 
I 3 HOH 15  415 165 HOH HOH A . 
I 3 HOH 16  416 34  HOH HOH A . 
I 3 HOH 17  417 124 HOH HOH A . 
I 3 HOH 18  418 162 HOH HOH A . 
I 3 HOH 19  419 4   HOH HOH A . 
I 3 HOH 20  420 17  HOH HOH A . 
I 3 HOH 21  421 84  HOH HOH A . 
I 3 HOH 22  422 25  HOH HOH A . 
I 3 HOH 23  423 32  HOH HOH A . 
I 3 HOH 24  424 147 HOH HOH A . 
I 3 HOH 25  425 99  HOH HOH A . 
I 3 HOH 26  426 68  HOH HOH A . 
I 3 HOH 27  427 114 HOH HOH A . 
I 3 HOH 28  428 5   HOH HOH A . 
I 3 HOH 29  429 160 HOH HOH A . 
I 3 HOH 30  430 97  HOH HOH A . 
I 3 HOH 31  431 72  HOH HOH A . 
I 3 HOH 32  432 6   HOH HOH A . 
I 3 HOH 33  433 94  HOH HOH A . 
I 3 HOH 34  434 150 HOH HOH A . 
I 3 HOH 35  435 48  HOH HOH A . 
I 3 HOH 36  436 31  HOH HOH A . 
I 3 HOH 37  437 155 HOH HOH A . 
I 3 HOH 38  438 115 HOH HOH A . 
I 3 HOH 39  439 1   HOH HOH A . 
I 3 HOH 40  440 27  HOH HOH A . 
I 3 HOH 41  441 63  HOH HOH A . 
I 3 HOH 42  442 133 HOH HOH A . 
I 3 HOH 43  443 176 HOH HOH A . 
I 3 HOH 44  444 135 HOH HOH A . 
I 3 HOH 45  445 55  HOH HOH A . 
I 3 HOH 46  446 145 HOH HOH A . 
I 3 HOH 47  447 83  HOH HOH A . 
I 3 HOH 48  448 54  HOH HOH A . 
I 3 HOH 49  449 125 HOH HOH A . 
I 3 HOH 50  450 13  HOH HOH A . 
I 3 HOH 51  451 46  HOH HOH A . 
I 3 HOH 52  452 82  HOH HOH A . 
I 3 HOH 53  453 2   HOH HOH A . 
I 3 HOH 54  454 86  HOH HOH A . 
I 3 HOH 55  455 101 HOH HOH A . 
I 3 HOH 56  456 49  HOH HOH A . 
I 3 HOH 57  457 18  HOH HOH A . 
I 3 HOH 58  458 110 HOH HOH A . 
I 3 HOH 59  459 93  HOH HOH A . 
I 3 HOH 60  460 9   HOH HOH A . 
I 3 HOH 61  461 166 HOH HOH A . 
I 3 HOH 62  462 51  HOH HOH A . 
I 3 HOH 63  463 53  HOH HOH A . 
I 3 HOH 64  464 172 HOH HOH A . 
I 3 HOH 65  465 69  HOH HOH A . 
I 3 HOH 66  466 92  HOH HOH A . 
I 3 HOH 67  467 29  HOH HOH A . 
I 3 HOH 68  468 16  HOH HOH A . 
I 3 HOH 69  469 78  HOH HOH A . 
I 3 HOH 70  470 127 HOH HOH A . 
I 3 HOH 71  471 142 HOH HOH A . 
I 3 HOH 72  472 178 HOH HOH A . 
I 3 HOH 73  473 58  HOH HOH A . 
I 3 HOH 74  474 26  HOH HOH A . 
I 3 HOH 75  475 59  HOH HOH A . 
I 3 HOH 76  476 159 HOH HOH A . 
I 3 HOH 77  477 10  HOH HOH A . 
I 3 HOH 78  478 128 HOH HOH A . 
I 3 HOH 79  479 151 HOH HOH A . 
I 3 HOH 80  480 11  HOH HOH A . 
I 3 HOH 81  481 47  HOH HOH A . 
I 3 HOH 82  482 154 HOH HOH A . 
I 3 HOH 83  483 143 HOH HOH A . 
I 3 HOH 84  484 118 HOH HOH A . 
I 3 HOH 85  485 71  HOH HOH A . 
I 3 HOH 86  486 148 HOH HOH A . 
I 3 HOH 87  487 170 HOH HOH A . 
I 3 HOH 88  488 35  HOH HOH A . 
I 3 HOH 89  489 52  HOH HOH A . 
I 3 HOH 90  490 168 HOH HOH A . 
I 3 HOH 91  491 77  HOH HOH A . 
I 3 HOH 92  492 180 HOH HOH A . 
I 3 HOH 93  493 153 HOH HOH A . 
I 3 HOH 94  494 12  HOH HOH A . 
I 3 HOH 95  495 80  HOH HOH A . 
I 3 HOH 96  496 161 HOH HOH A . 
I 3 HOH 97  497 50  HOH HOH A . 
I 3 HOH 98  498 107 HOH HOH A . 
I 3 HOH 99  499 76  HOH HOH A . 
I 3 HOH 100 500 60  HOH HOH A . 
I 3 HOH 101 501 129 HOH HOH A . 
I 3 HOH 102 502 116 HOH HOH A . 
I 3 HOH 103 503 98  HOH HOH A . 
I 3 HOH 104 504 81  HOH HOH A . 
I 3 HOH 105 505 79  HOH HOH A . 
I 3 HOH 106 506 132 HOH HOH A . 
I 3 HOH 107 507 126 HOH HOH A . 
I 3 HOH 108 508 130 HOH HOH A . 
I 3 HOH 109 509 174 HOH HOH A . 
I 3 HOH 110 510 181 HOH HOH A . 
I 3 HOH 111 511 102 HOH HOH A . 
I 3 HOH 112 512 173 HOH HOH A . 
I 3 HOH 113 513 177 HOH HOH A . 
J 3 HOH 1   301 36  HOH HOH B . 
J 3 HOH 2   302 23  HOH HOH B . 
J 3 HOH 3   303 100 HOH HOH B . 
J 3 HOH 4   304 119 HOH HOH B . 
J 3 HOH 5   305 108 HOH HOH B . 
J 3 HOH 6   306 120 HOH HOH B . 
J 3 HOH 7   307 42  HOH HOH B . 
J 3 HOH 8   308 105 HOH HOH B . 
J 3 HOH 9   309 21  HOH HOH B . 
J 3 HOH 10  310 40  HOH HOH B . 
J 3 HOH 11  311 74  HOH HOH B . 
J 3 HOH 12  312 136 HOH HOH B . 
J 3 HOH 13  313 41  HOH HOH B . 
J 3 HOH 14  314 19  HOH HOH B . 
J 3 HOH 15  315 38  HOH HOH B . 
J 3 HOH 16  316 66  HOH HOH B . 
J 3 HOH 17  317 43  HOH HOH B . 
J 3 HOH 18  318 157 HOH HOH B . 
J 3 HOH 19  319 88  HOH HOH B . 
J 3 HOH 20  320 57  HOH HOH B . 
J 3 HOH 21  321 96  HOH HOH B . 
J 3 HOH 22  322 163 HOH HOH B . 
J 3 HOH 23  323 139 HOH HOH B . 
J 3 HOH 24  324 146 HOH HOH B . 
J 3 HOH 25  325 61  HOH HOH B . 
J 3 HOH 26  326 109 HOH HOH B . 
J 3 HOH 27  327 158 HOH HOH B . 
J 3 HOH 28  328 56  HOH HOH B . 
J 3 HOH 29  329 106 HOH HOH B . 
J 3 HOH 30  330 22  HOH HOH B . 
J 3 HOH 31  331 39  HOH HOH B . 
J 3 HOH 32  332 28  HOH HOH B . 
J 3 HOH 33  333 113 HOH HOH B . 
J 3 HOH 34  334 95  HOH HOH B . 
J 3 HOH 35  335 91  HOH HOH B . 
J 3 HOH 36  336 175 HOH HOH B . 
J 3 HOH 37  337 20  HOH HOH B . 
J 3 HOH 38  338 64  HOH HOH B . 
J 3 HOH 39  339 75  HOH HOH B . 
J 3 HOH 40  340 112 HOH HOH B . 
J 3 HOH 41  341 45  HOH HOH B . 
J 3 HOH 42  342 15  HOH HOH B . 
J 3 HOH 43  343 141 HOH HOH B . 
J 3 HOH 44  344 103 HOH HOH B . 
J 3 HOH 45  345 89  HOH HOH B . 
J 3 HOH 46  346 122 HOH HOH B . 
J 3 HOH 47  347 44  HOH HOH B . 
J 3 HOH 48  348 182 HOH HOH B . 
J 3 HOH 49  349 156 HOH HOH B . 
J 3 HOH 50  350 117 HOH HOH B . 
J 3 HOH 51  351 134 HOH HOH B . 
J 3 HOH 52  352 65  HOH HOH B . 
J 3 HOH 53  353 104 HOH HOH B . 
J 3 HOH 54  354 62  HOH HOH B . 
J 3 HOH 55  355 144 HOH HOH B . 
J 3 HOH 56  356 149 HOH HOH B . 
J 3 HOH 57  357 169 HOH HOH B . 
J 3 HOH 58  358 131 HOH HOH B . 
J 3 HOH 59  359 121 HOH HOH B . 
J 3 HOH 60  360 37  HOH HOH B . 
J 3 HOH 61  361 70  HOH HOH B . 
J 3 HOH 62  362 140 HOH HOH B . 
J 3 HOH 63  363 138 HOH HOH B . 
J 3 HOH 64  364 164 HOH HOH B . 
J 3 HOH 65  365 87  HOH HOH B . 
J 3 HOH 66  366 24  HOH HOH B . 
J 3 HOH 67  367 179 HOH HOH B . 
J 3 HOH 68  368 184 HOH HOH B . 
J 3 HOH 69  369 183 HOH HOH B . 
# 
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   ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE   ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.642 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VYD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.670 
_cell.length_a_esd                 ? 
_cell.length_b                     97.280 
_cell.length_b_esd                 ? 
_cell.length_c                     89.020 
_cell.length_c_esd                 ? 
_cell.volume                       321608.839 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VYD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8VYD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.32 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 3350, Tris-HCL, NaCl, DTT' 
_exptl_crystal_grow.pdbx_pH_range   '9.2 - 9.3' 
_exptl_crystal_grow.temp            288 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     77 
_diffrn.ambient_temp_details             'Lq N2 stream' 
_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                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-22 
_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   0.97625 
_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                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          32.12 
_reflns.entry_id                                       8VYD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               42.54 
_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                                     44882 
_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                           84.53 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.28 
_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                                0.2001 
_reflns.pdbx_Rpim_I_all                                0.06204 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.942 
_reflns.pdbx_CC_star                                   0.985 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1891 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     2.02 
_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                             56908 
_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                               12.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.518 
_reflns_shell.pdbx_CC_star                                  0.826 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          40.20 
_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               ? 
# 
_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                               46.82 
_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                                 8VYD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             42.54 
_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                     39015 
_refine.ls_number_reflns_R_free                  1598 
_refine.ls_number_reflns_R_work                  37417 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.66 
_refine.ls_percent_reflns_R_free                 4.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2404 
_refine.ls_R_factor_R_free                       0.2871 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2383 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 40.6604 
_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                            0.3837 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        42.54 
_refine_hist.number_atoms_solvent             182 
_refine_hist.number_atoms_total               4411 
_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        4223 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_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' ? 0.0080 ? 4384 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1258 ? 5923 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0586 ? 657  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0111 ? 775  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.7700 ? 608  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 2.00  . . 80  1750 58.60 . . . . 0.3550 . . . . . . . . . . . 0.3074 
'X-RAY DIFFRACTION' 2.02 2.09  . . 124 2790 76.74 . . . . 0.5131 . . . . . . . . . . . 0.5942 
'X-RAY DIFFRACTION' 2.09 2.17  . . 115 2831 71.07 . . . . 0.3396 . . . . . . . . . . . 0.3997 
'X-RAY DIFFRACTION' 2.17 2.27  . . 142 3385 84.34 . . . . 0.4250 . . . . . . . . . . . 0.5295 
'X-RAY DIFFRACTION' 2.27 2.39  . . 143 3379 84.12 . . . . 0.2687 . . . . . . . . . . . 0.2886 
'X-RAY DIFFRACTION' 2.39 2.54  . . 174 4003 99.90 . . . . 0.2677 . . . . . . . . . . . 0.2926 
'X-RAY DIFFRACTION' 2.54 2.73  . . 143 3422 85.19 . . . . 0.3299 . . . . . . . . . . . 0.4407 
'X-RAY DIFFRACTION' 2.73 3.01  . . 170 3995 99.98 . . . . 0.2600 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 3.01 3.44  . . 164 3970 98.01 . . . . 0.2374 . . . . . . . . . . . 0.3169 
'X-RAY DIFFRACTION' 3.44 4.34  . . 161 3808 94.84 . . . . 0.1909 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 4.34 42.54 . . 182 4084 99.77 . . . . 0.1689 . . . . . . . . . . . 0.2052 
# 
_struct.entry_id                     8VYD 
_struct.title                        'A novel synthase generates m4(2)C to stabilize the archaeal ribosome' 
_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        8VYD 
_struct_keywords.text            'N4, N4-dimethylcytidine, synthase, RNA modifications, hyperthermophile, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5JDR0_THEKO 
_struct_ref.pdbx_db_accession          Q5JDR0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEEIYYITFREARMLLASRGNVKLNLDLRKTNRVQEVEIKDEGAVFPDGTLVEREVLEKIARDDGTVYFVSNGGVYKAAI
AGESGFYKLVPTIPPTIEINGIRMHRTKEMNPLQDTRNKVNTVMPREGETVLDTCMGLGYTAIEASKRGAYVITIEKDPN
VIEIARINPWSRELFTGGKIQVIQGDAFEVVKKFKQASFDVIIHDPPRFSLAGHLYSEEFYRELFRILKPGGRLFHYVGN
PGKKYRRKDLQKGVMERLRRVGFVGVRRVEEALGVVARKPEKGVKASQRD
;
_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 8VYD A 1 ? 290 ? Q5JDR0 1 ? 290 ? 1 290 
2 1 8VYD B 1 ? 290 ? Q5JDR0 1 ? 290 ? 1 290 
# 
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 8VYD ALA A 103 ? UNP Q5JDR0 ARG 103 conflict 103 1 
2 8VYD ALA B 103 ? UNP Q5JDR0 ARG 103 conflict 103 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I 
2 1 B,J             
# 
_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 THR A 8   ? SER A 18  ? THR A 8   SER A 18  1 ? 11 
HELX_P HELX_P2  AA2 ARG A 54  ? ASP A 63  ? ARG A 54  ASP A 63  1 ? 10 
HELX_P HELX_P3  AA3 ASN A 111 ? MET A 124 ? ASN A 111 MET A 124 1 ? 14 
HELX_P HELX_P4  AA4 GLY A 139 ? LYS A 147 ? GLY A 139 LYS A 147 1 ? 9  
HELX_P HELX_P5  AA5 ASP A 158 ? ASN A 168 ? ASP A 158 ASN A 168 1 ? 11 
HELX_P HELX_P6  AA6 PRO A 169 ? PHE A 175 ? PRO A 169 PHE A 175 5 ? 7  
HELX_P HELX_P7  AA7 ASP A 186 ? VAL A 191 ? ASP A 186 VAL A 191 1 ? 6  
HELX_P HELX_P8  AA8 LYS A 192 ? PHE A 194 ? LYS A 192 PHE A 194 5 ? 3  
HELX_P HELX_P9  AA9 ARG A 208 ? TYR A 216 ? ARG A 208 TYR A 216 5 ? 9  
HELX_P HELX_P10 AB1 SER A 217 ? ILE A 227 ? SER A 217 ILE A 227 1 ? 11 
HELX_P HELX_P11 AB2 ASP A 249 ? GLY A 262 ? ASP A 249 GLY A 262 1 ? 14 
HELX_P HELX_P12 AB3 THR B 8   ? SER B 18  ? THR B 8   SER B 18  1 ? 11 
HELX_P HELX_P13 AB4 ARG B 54  ? ARG B 62  ? ARG B 54  ARG B 62  1 ? 9  
HELX_P HELX_P14 AB5 ASN B 111 ? THR B 122 ? ASN B 111 THR B 122 1 ? 12 
HELX_P HELX_P15 AB6 GLY B 139 ? ARG B 148 ? GLY B 139 ARG B 148 1 ? 10 
HELX_P HELX_P16 AB7 ASP B 158 ? ASN B 168 ? ASP B 158 ASN B 168 1 ? 11 
HELX_P HELX_P17 AB8 PRO B 169 ? PHE B 175 ? PRO B 169 PHE B 175 5 ? 7  
HELX_P HELX_P18 AB9 ASP B 186 ? PHE B 194 ? ASP B 186 PHE B 194 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 212 ? TYR B 216 ? ALA B 212 TYR B 216 5 ? 5  
HELX_P HELX_P20 AC2 SER B 217 ? ILE B 227 ? SER B 217 ILE B 227 1 ? 11 
HELX_P HELX_P21 AC3 LYS B 252 ? VAL B 261 ? LYS B 252 VAL B 261 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 129 OE2 ? ? ? 1_555 H NA  . NA ? ? A GLU 129 A NA  306 1_555 ? ? ? ? ? ? ? 2.847 ? ? 
metalc2  metalc ? ? A ASP 133 OD1 ? ? ? 1_555 C NA  . NA ? ? A ASP 133 A NA  301 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc3  metalc ? ? A CYS 135 O   A ? ? 1_555 C NA  . NA ? ? A CYS 135 A NA  301 1_555 ? ? ? ? ? ? ? 2.834 ? ? 
metalc4  metalc ? ? A CYS 135 O   B ? ? 1_555 C NA  . NA ? ? A CYS 135 A NA  301 1_555 ? ? ? ? ? ? ? 2.807 ? ? 
metalc5  metalc ? ? A MET 136 O   ? ? ? 1_555 E NA  . NA ? ? A MET 136 A NA  303 1_555 ? ? ? ? ? ? ? 2.979 ? ? 
metalc6  metalc ? ? A TYR 140 O   ? ? ? 1_555 D NA  . NA ? ? A TYR 140 A NA  302 1_555 ? ? ? ? ? ? ? 2.964 ? ? 
metalc7  metalc ? ? A ASP 186 OD1 ? ? ? 1_555 F NA  . NA ? ? A ASP 186 A NA  304 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc8  metalc ? ? C NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  301 A HOH 412 1_555 ? ? ? ? ? ? ? 2.528 ? ? 
metalc9  metalc ? ? C NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  301 A HOH 453 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc10 metalc ? ? D NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  302 A HOH 404 1_555 ? ? ? ? ? ? ? 2.677 ? ? 
metalc11 metalc ? ? D NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  302 A HOH 445 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc12 metalc ? ? E NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  303 A HOH 439 1_555 ? ? ? ? ? ? ? 2.771 ? ? 
metalc13 metalc ? ? E NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  303 A HOH 474 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc14 metalc ? ? G NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  305 A HOH 462 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc15 metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  306 A HOH 438 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 129 ? A GLU 129 ? 1_555 NA ? H NA . ? A NA 306 ? 1_555 O ? I HOH .   ? A HOH 438 ? 1_555 121.9 ? 
2  OD1 ? A ASP 133 ? A ASP 133 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O A A CYS 135 ? A CYS 135 ? 1_555 108.6 ? 
3  OD1 ? A ASP 133 ? A ASP 133 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O B A CYS 135 ? A CYS 135 ? 1_555 108.0 ? 
4  O   A A CYS 135 ? A CYS 135 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O B A CYS 135 ? A CYS 135 ? 1_555 1.0   ? 
5  OD1 ? A ASP 133 ? A ASP 133 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 412 ? 1_555 133.9 ? 
6  O   A A CYS 135 ? A CYS 135 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 412 ? 1_555 109.1 ? 
7  O   B A CYS 135 ? A CYS 135 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 412 ? 1_555 109.2 ? 
8  OD1 ? A ASP 133 ? A ASP 133 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 453 ? 1_555 87.8  ? 
9  O   A A CYS 135 ? A CYS 135 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 453 ? 1_555 87.1  ? 
10 O   B A CYS 135 ? A CYS 135 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 453 ? 1_555 88.0  ? 
11 O   ? I HOH .   ? A HOH 412 ? 1_555 NA ? C NA . ? A NA 301 ? 1_555 O ? I HOH .   ? A HOH 453 ? 1_555 119.6 ? 
12 O   ? A MET 136 ? A MET 136 ? 1_555 NA ? E NA . ? A NA 303 ? 1_555 O ? I HOH .   ? A HOH 439 ? 1_555 58.1  ? 
13 O   ? A MET 136 ? A MET 136 ? 1_555 NA ? E NA . ? A NA 303 ? 1_555 O ? I HOH .   ? A HOH 474 ? 1_555 82.5  ? 
14 O   ? I HOH .   ? A HOH 439 ? 1_555 NA ? E NA . ? A NA 303 ? 1_555 O ? I HOH .   ? A HOH 474 ? 1_555 126.7 ? 
15 O   ? A TYR 140 ? A TYR 140 ? 1_555 NA ? D NA . ? A NA 302 ? 1_555 O ? I HOH .   ? A HOH 404 ? 1_555 113.3 ? 
16 O   ? A TYR 140 ? A TYR 140 ? 1_555 NA ? D NA . ? A NA 302 ? 1_555 O ? I HOH .   ? A HOH 445 ? 1_555 135.6 ? 
17 O   ? I HOH .   ? A HOH 404 ? 1_555 NA ? D NA . ? A NA 302 ? 1_555 O ? I HOH .   ? A HOH 445 ? 1_555 105.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 93 A . ? ILE 93 A PRO 94 A ? PRO 94 A 1 -3.31 
2 ILE 93 B . ? ILE 93 B PRO 94 B ? PRO 94 B 1 3.98  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 3 ? 
AA8 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 5   ? ILE A 7   ? TYR A 5   ILE A 7   
AA1 2 TYR A 68  ? SER A 71  ? TYR A 68  SER A 71  
AA1 3 GLY A 74  ? LYS A 77  ? GLY A 74  LYS A 77  
AA2 1 ASN A 21  ? ASN A 25  ? ASN A 21  ASN A 25  
AA2 2 VAL A 34  ? ILE A 39  ? VAL A 34  ILE A 39  
AA2 3 GLY A 43  ? VAL A 45  ? GLY A 43  VAL A 45  
AA2 4 LEU A 51  ? GLU A 53  ? LEU A 51  GLU A 53  
AA3 1 ALA A 79  ? GLY A 82  ? ALA A 79  GLY A 82  
AA3 2 GLY A 85  ? VAL A 90  ? GLY A 85  VAL A 90  
AA3 3 THR A 96  ? ILE A 99  ? THR A 96  ILE A 99  
AA4 1 ILE A 180 ? GLN A 184 ? ILE A 180 GLN A 184 
AA4 2 TYR A 151 ? GLU A 156 ? TYR A 151 GLU A 156 
AA4 3 THR A 130 ? ASP A 133 ? THR A 130 ASP A 133 
AA4 4 PHE A 199 ? HIS A 204 ? PHE A 199 HIS A 204 
AA4 5 LEU A 228 ? TYR A 237 ? LEU A 228 TYR A 237 
AA4 6 GLY A 274 ? ARG A 278 ? GLY A 274 ARG A 278 
AA4 7 VAL A 264 ? VAL A 269 ? VAL A 264 VAL A 269 
AA5 1 TYR B 5   ? ILE B 7   ? TYR B 5   ILE B 7   
AA5 2 TYR B 68  ? SER B 71  ? TYR B 68  SER B 71  
AA5 3 GLY B 74  ? LYS B 77  ? GLY B 74  LYS B 77  
AA6 1 GLY B 20  ? ASN B 25  ? GLY B 20  ASN B 25  
AA6 2 VAL B 34  ? ILE B 39  ? VAL B 34  ILE B 39  
AA6 3 GLY B 43  ? VAL B 45  ? GLY B 43  VAL B 45  
AA6 4 LEU B 51  ? GLU B 53  ? LEU B 51  GLU B 53  
AA7 1 ALA B 79  ? GLY B 82  ? ALA B 79  GLY B 82  
AA7 2 GLY B 85  ? VAL B 90  ? GLY B 85  VAL B 90  
AA7 3 THR B 96  ? ILE B 99  ? THR B 96  ILE B 99  
AA8 1 ILE B 180 ? GLN B 184 ? ILE B 180 GLN B 184 
AA8 2 TYR B 151 ? GLU B 156 ? TYR B 151 GLU B 156 
AA8 3 THR B 130 ? ASP B 133 ? THR B 130 ASP B 133 
AA8 4 PHE B 199 ? HIS B 204 ? PHE B 199 HIS B 204 
AA8 5 LEU B 228 ? TYR B 237 ? LEU B 228 TYR B 237 
AA8 6 GLY B 274 ? ARG B 278 ? GLY B 274 ARG B 278 
AA8 7 VAL B 264 ? VAL B 269 ? VAL B 264 VAL B 269 
# 
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 7   ? N ILE A 7   O TYR A 68  ? O TYR A 68  
AA1 2 3 N PHE A 69  ? N PHE A 69  O TYR A 76  ? O TYR A 76  
AA2 1 2 N LEU A 24  ? N LEU A 24  O GLN A 35  ? O GLN A 35  
AA2 2 3 N GLU A 38  ? N GLU A 38  O VAL A 45  ? O VAL A 45  
AA2 3 4 N ALA A 44  ? N ALA A 44  O VAL A 52  ? O VAL A 52  
AA3 1 2 N ILE A 80  ? N ILE A 80  O TYR A 87  ? O TYR A 87  
AA3 2 3 N VAL A 90  ? N VAL A 90  O THR A 96  ? O THR A 96  
AA4 1 2 O ILE A 183 ? O ILE A 183 N THR A 154 ? N THR A 154 
AA4 2 3 O ILE A 153 ? O ILE A 153 N ASP A 133 ? N ASP A 133 
AA4 3 4 N LEU A 132 ? N LEU A 132 O ILE A 203 ? O ILE A 203 
AA4 4 5 N HIS A 204 ? N HIS A 204 O PHE A 235 ? O PHE A 235 
AA4 5 6 N HIS A 236 ? N HIS A 236 O VAL A 275 ? O VAL A 275 
AA4 6 7 O ARG A 278 ? O ARG A 278 N VAL A 264 ? N VAL A 264 
AA5 1 2 N TYR B 5   ? N TYR B 5   O VAL B 70  ? O VAL B 70  
AA5 2 3 N PHE B 69  ? N PHE B 69  O TYR B 76  ? O TYR B 76  
AA6 1 2 N GLY B 20  ? N GLY B 20  O ILE B 39  ? O ILE B 39  
AA6 2 3 N GLU B 38  ? N GLU B 38  O VAL B 45  ? O VAL B 45  
AA6 3 4 N ALA B 44  ? N ALA B 44  O VAL B 52  ? O VAL B 52  
AA7 1 2 N ILE B 80  ? N ILE B 80  O TYR B 87  ? O TYR B 87  
AA7 2 3 N VAL B 90  ? N VAL B 90  O THR B 96  ? O THR B 96  
AA8 1 2 O GLN B 181 ? O GLN B 181 N VAL B 152 ? N VAL B 152 
AA8 2 3 O ILE B 153 ? O ILE B 153 N ASP B 133 ? N ASP B 133 
AA8 3 4 N LEU B 132 ? N LEU B 132 O ILE B 203 ? O ILE B 203 
AA8 4 5 N HIS B 204 ? N HIS B 204 O PHE B 235 ? O PHE B 235 
AA8 5 6 N HIS B 236 ? N HIS B 236 O VAL B 275 ? O VAL B 275 
AA8 6 7 O GLY B 274 ? O GLY B 274 N VAL B 269 ? N VAL B 269 
# 
_pdbx_entry_details.entry_id                   8VYD 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 29  ? ? 59.89   18.94   
2  1 ASN A 32  ? ? 68.93   -20.70  
3  1 PRO A 47  ? ? -69.01  2.31    
4  1 ASN A 72  ? ? 53.58   -136.38 
5  1 GLU A 83  ? ? 64.16   -98.49  
6  1 PRO A 91  ? ? -77.01  49.76   
7  1 ASN A 100 ? ? 57.74   -66.45  
8  1 ASN A 100 ? ? 53.36   -66.45  
9  1 ASN A 111 ? A -104.36 -73.67  
10 1 ASN A 111 ? B -104.69 -73.19  
11 1 PRO A 112 ? ? -68.60  -70.09  
12 1 PRO A 112 ? ? -68.34  -70.09  
13 1 LYS A 179 ? ? 121.10  -35.94  
14 1 PRO A 207 ? ? -59.52  172.38  
15 1 ALA A 212 ? ? -147.66 48.03   
16 1 VAL A 238 ? ? -130.97 -46.77  
17 1 LYS A 252 ? ? -29.99  -79.11  
18 1 PRO A 280 ? ? -80.08  -155.68 
19 1 ASN B 32  ? ? 68.05   -11.51  
20 1 SER B 84  ? ? -86.98  30.41   
21 1 PRO B 91  ? ? -74.40  34.84   
22 1 MET B 124 ? ? 23.17   87.06   
23 1 PRO B 207 ? ? -62.50  -179.19 
24 1 ALA B 212 ? ? -172.96 101.10  
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 8.355  12.566  34.461 0.628048201705 0.262998698776 0.297989786176 -0.0286083336973 
0.0732474171834  -0.029292504677   4.35500645691 3.57198284145 6.97539438221 0.908628203124  0.45680612772    0.942075189124 
0.21857334389    -0.0580718576375 -0.0773664613163  -0.267310504507  0.516182055177   -0.165464223111 0.539837336123   
-0.881804992483 0.172767449475  
'X-RAY DIFFRACTION' 2 ? refined 2.116  -6.114  19.871 0.477568618031 0.468309936741 0.380885404335 0.0419358576784  
0.0401591642835  -0.129867582176   7.70155887383 5.92283815691 1.15407061578 -6.01590902524  -2.75457671176   1.69816973478  
-0.369367016254  0.13545741864    0.499231778058    -1.12582604818   0.0214886223323  0.586291149819  1.33537066785    
0.0227616123588 -0.563267318338 
'X-RAY DIFFRACTION' 3 ? refined -1.452 1.287   7.751  0.103652311205 0.312820935754 0.192529091151 0.0304360745404  
0.0269834599417  0.0211695177846   3.01315804577 3.08869128701 3.94874181757 0.802323447036  0.606618212595   1.26277361118  
-0.124429774463  0.112437975868   -0.00219512633524 0.633238751083   0.0591010975605  0.158889495572  -0.0110128140495 
-0.25055449788  0.0288837313073 
'X-RAY DIFFRACTION' 4 ? refined -7.743 -14.511 5.083  0.223085166776 0.319098107324 0.501415941236 -0.0443473079027 
0.0645106748412  -0.194707243908   4.55265518706 5.71130181931 7.20375956484 -1.16132419398  0.76432434285    0.334473594003 
-0.0953054079447 -0.0583814388412 0.260032497688    0.684762831573   -1.41313032102   0.410291180767  0.407263529535   
0.0718763015669 -0.539642879778 
'X-RAY DIFFRACTION' 5 ? refined -0.358 16.441  82.090 0.250803028834 0.233946235647 0.241048313602 0.0495010288256  
0.0448993059729  0.0521699718878   6.49926935507 6.65160360775 8.29453566368 2.40163194658   -0.0204363809892 -1.22727386591 
0.114722567685   -0.144960674782  -0.0122143826553  -0.0492297698928 0.5140832988     -0.268752203826 0.0408275490074  
-0.398424747896 0.451229875238  
'X-RAY DIFFRACTION' 6 ? refined -9.424 6.583   71.564 0.344374791163 0.422238872583 0.262985995823 -0.0310672643978 
0.0825535356885  -0.045608175423   2.53182680982 4.44357902592 7.08809053186 1.21695265004   -1.03804204116   2.62435178403  
-0.115063706153  -0.405702427067  0.431081118256    -0.12192047513   0.00472370986194 0.511983450105  0.209296565746   
0.866491829925  -0.618948641574 
'X-RAY DIFFRACTION' 7 ? refined 1.087  -5.615  51.945 0.450596984997 0.300271414887 0.226977751598 0.0984981486369  
0.00376632319758 -0.00110750254251 2.42273980509 4.3408928315  4.6313348652  -0.755704552519 -0.0615459939211 1.76258873458  
0.0949313014898  0.024203640008   -0.117730909862   -0.0492908890843 -0.373308584833  0.0863544337993 0.142084394993   
0.784144969463  0.408228971614  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 2   A 99  '( CHAIN A AND RESID 2:99 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 100 A 123 '( CHAIN A AND RESID 100:123 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 A 124 A 248 '( CHAIN A AND RESID 124:248 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 A 249 A 282 '( CHAIN A AND RESID 249:282 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 5 5 B 2   B 61  '( CHAIN B AND RESID 2:61 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 6 6 B 62  B 111 '( CHAIN B AND RESID 62:111 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 7 7 B 112 B 281 '( CHAIN B AND RESID 112:281 )' ? ? ? ? ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 508 ? 5.85 . 
2 1 O ? A HOH 509 ? 5.92 . 
3 1 O ? A HOH 510 ? 5.97 . 
4 1 O ? A HOH 511 ? 6.01 . 
5 1 O ? A HOH 512 ? 6.66 . 
6 1 O ? A HOH 513 ? 7.30 . 
7 1 O ? B HOH 369 ? 6.18 . 
# 
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 MET 104 ? A MET 104 
3  1 Y 1 A HIS 105 ? A HIS 105 
4  1 Y 1 A ARG 106 ? A ARG 106 
5  1 Y 1 A THR 107 ? A THR 107 
6  1 Y 1 A LYS 108 ? A LYS 108 
7  1 Y 1 A GLU 109 ? A GLU 109 
8  1 Y 1 A ASN 240 ? A ASN 240 
9  1 Y 1 A PRO 241 ? A PRO 241 
10 1 Y 1 A GLY 242 ? A GLY 242 
11 1 Y 1 A LYS 243 ? A LYS 243 
12 1 Y 1 A LYS 244 ? A LYS 244 
13 1 Y 1 A TYR 245 ? A TYR 245 
14 1 Y 1 A ARG 246 ? A ARG 246 
15 1 Y 1 A ARG 247 ? A ARG 247 
16 1 Y 1 A GLY 283 ? A GLY 283 
17 1 Y 1 A VAL 284 ? A VAL 284 
18 1 Y 1 A LYS 285 ? A LYS 285 
19 1 Y 1 A ALA 286 ? A ALA 286 
20 1 Y 1 A SER 287 ? A SER 287 
21 1 Y 1 A GLN 288 ? A GLN 288 
22 1 Y 1 A ARG 289 ? A ARG 289 
23 1 Y 1 A ASP 290 ? A ASP 290 
24 1 Y 1 B MET 1   ? B MET 1   
25 1 Y 1 B ALA 103 ? B ALA 103 
26 1 Y 1 B MET 104 ? B MET 104 
27 1 Y 1 B HIS 105 ? B HIS 105 
28 1 Y 1 B ARG 106 ? B ARG 106 
29 1 Y 1 B THR 107 ? B THR 107 
30 1 Y 1 B LYS 108 ? B LYS 108 
31 1 Y 1 B GLU 109 ? B GLU 109 
32 1 Y 1 B GLY 239 ? B GLY 239 
33 1 Y 1 B ASN 240 ? B ASN 240 
34 1 Y 1 B PRO 241 ? B PRO 241 
35 1 Y 1 B GLY 242 ? B GLY 242 
36 1 Y 1 B LYS 243 ? B LYS 243 
37 1 Y 1 B LYS 244 ? B LYS 244 
38 1 Y 1 B TYR 245 ? B TYR 245 
39 1 Y 1 B ARG 246 ? B ARG 246 
40 1 Y 1 B ARG 247 ? B ARG 247 
41 1 Y 1 B LYS 248 ? B LYS 248 
42 1 Y 1 B LYS 282 ? B LYS 282 
43 1 Y 1 B GLY 283 ? B GLY 283 
44 1 Y 1 B VAL 284 ? B VAL 284 
45 1 Y 1 B LYS 285 ? B LYS 285 
46 1 Y 1 B ALA 286 ? B ALA 286 
47 1 Y 1 B SER 287 ? B SER 287 
48 1 Y 1 B GLN 288 ? B GLN 288 
49 1 Y 1 B ARG 289 ? B ARG 289 
50 1 Y 1 B ASP 290 ? B ASP 290 
# 
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 
NA  NA   NA N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' 2022065      1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35-GM143963 2 
'National Science Foundation (NSF, United States)'                                         'United States' 2124202      3 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM132057     4 
# 
_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   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VYD 
_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]   0.026546 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004510 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010280 
_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]   0.011394 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
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   . GLU A 1 2   ? 16.46211  22.30489  25.79278  1.000 78.96883 ? 2   GLU A N   1 
ATOM   2    C  CA  . GLU A 1 2   ? 16.84655  21.58735  24.58033  1.000 84.40684 ? 2   GLU A CA  1 
ATOM   3    C  C   . GLU A 1 2   ? 16.38895  20.12813  24.66265  1.000 87.63859 ? 2   GLU A C   1 
ATOM   4    O  O   . GLU A 1 2   ? 15.46456  19.70583  23.96214  1.000 79.61061 ? 2   GLU A O   1 
ATOM   5    C  CB  . GLU A 1 2   ? 18.36314  21.66753  24.37207  1.000 80.29243 ? 2   GLU A CB  1 
ATOM   6    C  CG  . GLU A 1 2   ? 18.92142  20.68905  23.34603  1.000 79.55850 ? 2   GLU A CG  1 
ATOM   7    C  CD  . GLU A 1 2   ? 20.31779  20.21500  23.70578  1.000 77.79046 ? 2   GLU A CD  1 
ATOM   8    O  OE1 . GLU A 1 2   ? 20.56047  19.91942  24.89493  1.000 68.50649 ? 2   GLU A OE1 1 
ATOM   9    O  OE2 . GLU A 1 2   ? 21.17431  20.14206  22.79926  1.000 94.47555 ? 2   GLU A OE2 1 
ATOM   10   N  N   . GLU A 1 3   ? 17.04731  19.36878  25.53409  1.000 83.95176 ? 3   GLU A N   1 
ATOM   11   C  CA  . GLU A 1 3   ? 16.68628  17.98135  25.77063  1.000 70.24379 ? 3   GLU A CA  1 
ATOM   12   C  C   . GLU A 1 3   ? 15.38377  17.90176  26.55555  1.000 66.80803 ? 3   GLU A C   1 
ATOM   13   O  O   . GLU A 1 3   ? 15.06209  18.77656  27.36245  1.000 66.27232 ? 3   GLU A O   1 
ATOM   14   C  CB  . GLU A 1 3   ? 17.79947  17.27574  26.54575  1.000 73.01808 ? 3   GLU A CB  1 
ATOM   15   C  CG  . GLU A 1 3   ? 17.79038  15.76319  26.45615  1.000 72.93214 ? 3   GLU A CG  1 
ATOM   16   C  CD  . GLU A 1 3   ? 19.13297  15.15529  26.83372  1.000 77.96927 ? 3   GLU A CD  1 
ATOM   17   O  OE1 . GLU A 1 3   ? 20.13785  15.90374  26.88601  1.000 76.78282 ? 3   GLU A OE1 1 
ATOM   18   O  OE2 . GLU A 1 3   ? 19.17964  13.92944  27.08223  1.000 71.28270 ? 3   GLU A OE2 1 
ATOM   19   N  N   . ILE A 1 4   ? 14.62780  16.83707  26.32057  1.000 65.13352 ? 4   ILE A N   1 
ATOM   20   C  CA  . ILE A 1 4   ? 13.41757  16.56620  27.08197  1.000 54.29869 ? 4   ILE A CA  1 
ATOM   21   C  C   . ILE A 1 4   ? 13.69613  15.41382  28.02709  1.000 55.57409 ? 4   ILE A C   1 
ATOM   22   O  O   . ILE A 1 4   ? 14.24169  14.37988  27.61970  1.000 56.14955 ? 4   ILE A O   1 
ATOM   23   C  CB  . ILE A 1 4   ? 12.21754  16.23995  26.18252  1.000 50.90633 ? 4   ILE A CB  1 
ATOM   24   C  CG1 . ILE A 1 4   ? 11.98641  17.35171  25.16083  1.000 56.15406 ? 4   ILE A CG1 1 
ATOM   25   C  CG2 . ILE A 1 4   ? 10.98396  16.05550  27.04186  1.000 47.76351 ? 4   ILE A CG2 1 
ATOM   26   C  CD1 . ILE A 1 4   ? 10.55865  17.43175  24.66654  1.000 54.94584 ? 4   ILE A CD1 1 
ATOM   27   N  N   . TYR A 1 5   ? 13.31942  15.59271  29.28426  1.000 53.55690 ? 5   TYR A N   1 
ATOM   28   C  CA  . TYR A 1 5   ? 13.36453  14.52890  30.26780  1.000 49.80348 ? 5   TYR A CA  1 
ATOM   29   C  C   . TYR A 1 5   ? 11.94661  14.04814  30.50631  1.000 46.31098 ? 5   TYR A C   1 
ATOM   30   O  O   . TYR A 1 5   ? 11.08754  14.82019  30.95046  1.000 45.85171 ? 5   TYR A O   1 
ATOM   31   C  CB  . TYR A 1 5   ? 14.01602  15.02025  31.55205  1.000 48.27687 ? 5   TYR A CB  1 
ATOM   32   C  CG  . TYR A 1 5   ? 15.33055  15.65971  31.24122  1.000 57.48851 ? 5   TYR A CG  1 
ATOM   33   C  CD1 . TYR A 1 5   ? 16.33066  14.93274  30.62235  1.000 53.31003 ? 5   TYR A CD1 1 
ATOM   34   C  CD2 . TYR A 1 5   ? 15.56247  16.99844  31.51530  1.000 56.42489 ? 5   TYR A CD2 1 
ATOM   35   C  CE1 . TYR A 1 5   ? 17.53454  15.50773  30.31931  1.000 61.57120 ? 5   TYR A CE1 1 
ATOM   36   C  CE2 . TYR A 1 5   ? 16.76891  17.58252  31.20986  1.000 54.49440 ? 5   TYR A CE2 1 
ATOM   37   C  CZ  . TYR A 1 5   ? 17.74970  16.83085  30.61029  1.000 59.06585 ? 5   TYR A CZ  1 
ATOM   38   O  OH  . TYR A 1 5   ? 18.95904  17.39862  30.29311  1.000 69.10854 ? 5   TYR A OH  1 
ATOM   39   N  N   . TYR A 1 6   ? 11.70586  12.78572  30.18421  1.000 40.41918 ? 6   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 6   ? 10.42252  12.15512  30.42806  1.000 40.51960 ? 6   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 6   ? 10.41768  11.52248  31.81139  1.000 39.15906 ? 6   TYR A C   1 
ATOM   42   O  O   . TYR A 1 6   ? 11.35368  10.80913  32.18309  1.000 37.08558 ? 6   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 6   ? 10.13775  11.12468  29.34231  1.000 28.49240 ? 6   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 6   ? 10.01799  11.79530  28.00992  1.000 34.53587 ? 6   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 6   ? 11.14436  12.05335  27.24279  1.000 42.11914 ? 6   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 6   ? 8.79052   12.21316  27.53424  1.000 35.92004 ? 6   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 6   ? 11.04645  12.68705  26.02558  1.000 47.21959 ? 6   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 6   ? 8.68149   12.85779  26.32566  1.000 37.02686 ? 6   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 6   ? 9.81327   13.09468  25.57179  1.000 40.70837 ? 6   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 6   ? 9.71180   13.72177  24.34952  1.000 40.03161 ? 6   TYR A OH  1 
ATOM   51   N  N   . ILE A 1 7   ? 9.37755   11.81147  32.58031  1.000 35.80446 ? 7   ILE A N   1 
ATOM   52   C  CA  . ILE A 1 7   ? 9.24371   11.26686  33.92220  1.000 42.63548 ? 7   ILE A CA  1 
ATOM   53   C  C   . ILE A 1 7   ? 7.79886   10.83213  34.14485  1.000 36.26179 ? 7   ILE A C   1 
ATOM   54   O  O   . ILE A 1 7   ? 6.85170   11.52484  33.75660  1.000 35.53342 ? 7   ILE A O   1 
ATOM   55   C  CB  . ILE A 1 7   ? 9.70562   12.28863  34.98272  1.000 38.29544 ? 7   ILE A CB  1 
ATOM   56   C  CG1 . ILE A 1 7   ? 9.05566   13.63713  34.74631  1.000 36.31475 ? 7   ILE A CG1 1 
ATOM   57   C  CG2 . ILE A 1 7   ? 11.20861  12.47613  34.92383  1.000 41.34212 ? 7   ILE A CG2 1 
ATOM   58   C  CD1 . ILE A 1 7   ? 8.96946   14.48638  35.99170  1.000 46.32487 ? 7   ILE A CD1 1 
ATOM   59   N  N   . THR A 1 8   ? 7.63757   9.67682   34.76112  1.000 35.07632 ? 8   THR A N   1 
ATOM   60   C  CA  . THR A 1 8   ? 6.34872   9.13561   35.13241  1.000 33.34916 ? 8   THR A CA  1 
ATOM   61   C  C   . THR A 1 8   ? 6.31485   8.92000   36.63990  1.000 39.02202 ? 8   THR A C   1 
ATOM   62   O  O   . THR A 1 8   ? 7.29752   9.16215   37.34833  1.000 35.74662 ? 8   THR A O   1 
ATOM   63   C  CB  . THR A 1 8   ? 6.09162   7.82267   34.40065  1.000 34.84176 ? 8   THR A CB  1 
ATOM   64   O  OG1 . THR A 1 8   ? 6.97579   6.82565   34.92055  1.000 30.36373 ? 8   THR A OG1 1 
ATOM   65   C  CG2 . THR A 1 8   ? 6.35142   7.98420   32.90634  1.000 31.41423 ? 8   THR A CG2 1 
ATOM   66   N  N   . PHE A 1 9   ? 5.17127   8.42692   37.12062  1.000 38.66614 ? 9   PHE A N   1 
ATOM   67   C  CA  . PHE A 1 9   ? 5.03197   8.10355   38.53860  1.000 38.22577 ? 9   PHE A CA  1 
ATOM   68   C  C   . PHE A 1 9   ? 6.20953   7.28264   39.04293  1.000 40.58541 ? 9   PHE A C   1 
ATOM   69   O  O   . PHE A 1 9   ? 6.66953   7.47972   40.17282  1.000 39.12259 ? 9   PHE A O   1 
ATOM   70   C  CB  . PHE A 1 9   ? 3.72308   7.34982   38.76949  1.000 38.66876 ? 9   PHE A CB  1 
ATOM   71   C  CG  . PHE A 1 9   ? 3.71843   5.96348   38.18623  1.000 37.71013 ? 9   PHE A CG  1 
ATOM   72   C  CD1 . PHE A 1 9   ? 3.41546   5.76612   36.85271  1.000 39.15271 ? 9   PHE A CD1 1 
ATOM   73   C  CD2 . PHE A 1 9   ? 4.03138   4.85568   38.97311  1.000 34.05026 ? 9   PHE A CD2 1 
ATOM   74   C  CE1 . PHE A 1 9   ? 3.41571   4.48816   36.30739  1.000 36.22939 ? 9   PHE A CE1 1 
ATOM   75   C  CE2 . PHE A 1 9   ? 4.03271   3.58212   38.43968  1.000 40.91642 ? 9   PHE A CE2 1 
ATOM   76   C  CZ  . PHE A 1 9   ? 3.73071   3.39454   37.09558  1.000 37.99428 ? 9   PHE A CZ  1 
ATOM   77   N  N   . ARG A 1 10  ? 6.73001   6.37382   38.20710  1.000 37.66521 ? 10  ARG A N   1 
ATOM   78   C  CA  . ARG A 1 10  ? 7.82900   5.50862   38.63599  1.000 37.06364 ? 10  ARG A CA  1 
ATOM   79   C  C   . ARG A 1 10  ? 9.02770   6.33746   39.06598  1.000 41.26269 ? 10  ARG A C   1 
ATOM   80   O  O   . ARG A 1 10  ? 9.62794   6.09228   40.11919  1.000 40.36592 ? 10  ARG A O   1 
ATOM   81   C  CB  . ARG A 1 10  ? 8.22815   4.55522   37.50652  1.000 43.54049 ? 10  ARG A CB  1 
ATOM   82   C  CG  . ARG A 1 10  ? 7.26570   3.39824   37.29476  1.000 35.49498 ? 10  ARG A CG  1 
ATOM   83   C  CD  . ARG A 1 10  ? 7.68834   2.53487   36.11479  1.000 45.84503 ? 10  ARG A CD  1 
ATOM   84   N  NE  . ARG A 1 10  ? 6.53684   1.89103   35.49285  1.000 41.65709 ? 10  ARG A NE  1 
ATOM   85   C  CZ  . ARG A 1 10  ? 5.83510   2.41090   34.49358  1.000 43.01981 ? 10  ARG A CZ  1 
ATOM   86   N  NH1 . ARG A 1 10  ? 6.18917   3.55335   33.91319  1.000 42.33378 ? 10  ARG A NH1 1 
ATOM   87   N  NH2 . ARG A 1 10  ? 4.74272   1.77878   34.07287  1.000 44.44259 ? 10  ARG A NH2 1 
ATOM   88   N  N   . GLU A 1 11  ? 9.37871   7.33924   38.26167  1.000 38.05879 ? 11  GLU A N   1 
ATOM   89   C  CA  . GLU A 1 11  ? 10.54261  8.15610   38.56771  1.000 40.73503 ? 11  GLU A CA  1 
ATOM   90   C  C   . GLU A 1 11  ? 10.27692  9.07007   39.75762  1.000 42.90518 ? 11  GLU A C   1 
ATOM   91   O  O   . GLU A 1 11  ? 11.15686  9.27031   40.60337  1.000 42.12932 ? 11  GLU A O   1 
ATOM   92   C  CB  . GLU A 1 11  ? 10.93967  8.96274   37.33212  1.000 40.78470 ? 11  GLU A CB  1 
ATOM   93   C  CG  . GLU A 1 11  ? 11.56330  8.09831   36.23441  1.000 43.67754 ? 11  GLU A CG  1 
ATOM   94   C  CD  . GLU A 1 11  ? 10.53428  7.47955   35.32255  1.000 42.33063 ? 11  GLU A CD  1 
ATOM   95   O  OE1 . GLU A 1 11  ? 9.44242   8.06837   35.15613  1.000 38.77229 ? 11  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A 1 11  ? 10.81952  6.40451   34.75691  1.000 56.39125 ? 11  GLU A OE2 1 
ATOM   97   N  N   . ALA A 1 12  ? 9.06775   9.62994   39.84498  1.000 41.96705 ? 12  ALA A N   1 
ATOM   98   C  CA  . ALA A 1 12  ? 8.77482   10.56094  40.92764  1.000 43.25809 ? 12  ALA A CA  1 
ATOM   99   C  C   . ALA A 1 12  ? 8.82565   9.86982   42.27643  1.000 38.64310 ? 12  ALA A C   1 
ATOM   100  O  O   . ALA A 1 12  ? 9.38268   10.41591  43.23241  1.000 46.23440 ? 12  ALA A O   1 
ATOM   101  C  CB  . ALA A 1 12  ? 7.40847   11.19217  40.72531  1.000 45.57051 ? 12  ALA A CB  1 
ATOM   102  N  N   . ARG A 1 13  ? 8.22535   8.68049   42.37612  1.000 37.95126 ? 13  ARG A N   1 
ATOM   103  C  CA  . ARG A 1 13  ? 8.32271   7.90052   43.60208  1.000 45.71432 ? 13  ARG A CA  1 
ATOM   104  C  C   . ARG A 1 13  ? 9.77689   7.64822   43.95928  1.000 49.03858 ? 13  ARG A C   1 
ATOM   105  O  O   . ARG A 1 13  ? 10.19135  7.84124   45.10898  1.000 44.85904 ? 13  ARG A O   1 
ATOM   106  C  CB  . ARG A 1 13  ? 7.55848   6.58231   43.44860  1.000 40.28327 ? 13  ARG A CB  1 
ATOM   107  C  CG  . ARG A 1 13  ? 6.07290   6.79763   43.24206  1.000 38.77047 ? 13  ARG A CG  1 
ATOM   108  C  CD  . ARG A 1 13  ? 5.35711   5.58007   42.76394  1.000 37.87410 ? 13  ARG A CD  1 
ATOM   109  N  NE  . ARG A 1 13  ? 3.93653   5.86916   42.63700  1.000 38.10416 ? 13  ARG A NE  1 
ATOM   110  C  CZ  . ARG A 1 13  ? 3.01508   4.99551   42.25184  1.000 37.76945 ? 13  ARG A CZ  1 
ATOM   111  N  NH1 . ARG A 1 13  ? 3.32788   3.74492   41.94961  1.000 38.35541 ? 13  ARG A NH1 1 
ATOM   112  N  NH2 . ARG A 1 13  ? 1.74620   5.38590   42.17162  1.000 38.40846 ? 13  ARG A NH2 1 
ATOM   113  N  N   . MET A 1 14  ? 10.56889  7.22883   42.97222  1.000 45.77757 ? 14  MET A N   1 
ATOM   114  C  CA  . MET A 1 14  ? 11.99948  7.04244   43.17925  1.000 47.96757 ? 14  MET A CA  1 
ATOM   115  C  C   . MET A 1 14  ? 12.62633  8.27863   43.80140  1.000 43.37720 ? 14  MET A C   1 
ATOM   116  O  O   . MET A 1 14  ? 13.33433  8.19494   44.80618  1.000 50.83563 ? 14  MET A O   1 
ATOM   117  C  CB  . MET A 1 14  ? 12.67907  6.72008   41.84224  1.000 50.63512 ? 14  MET A CB  1 
ATOM   118  C  CG  . MET A 1 14  ? 14.18277  6.89310   41.89019  1.000 48.02077 ? 14  MET A CG  1 
ATOM   119  S  SD  . MET A 1 14  ? 14.93874  5.30156   42.20653  1.000 59.26046 ? 14  MET A SD  1 
ATOM   120  C  CE  . MET A 1 14  ? 14.34355  4.44948   40.75254  1.000 40.13192 ? 14  MET A CE  1 
ATOM   121  N  N   . LEU A 1 15  ? 12.35994  9.44652   43.22203  1.000 46.62094 ? 15  LEU A N   1 
ATOM   122  C  CA  . LEU A 1 15  ? 13.05663  10.64225  43.67379  1.000 49.35718 ? 15  LEU A CA  1 
ATOM   123  C  C   . LEU A 1 15  ? 12.55007  11.12553  45.02517  1.000 51.68203 ? 15  LEU A C   1 
ATOM   124  O  O   . LEU A 1 15  ? 13.32116  11.71206  45.78608  1.000 59.21902 ? 15  LEU A O   1 
ATOM   125  C  CB  . LEU A 1 15  ? 12.93631  11.74359  42.62746  1.000 50.28823 ? 15  LEU A CB  1 
ATOM   126  C  CG  . LEU A 1 15  ? 13.61014  11.41931  41.29334  1.000 46.28787 ? 15  LEU A CG  1 
ATOM   127  C  CD1 . LEU A 1 15  ? 12.80777  11.97641  40.15658  1.000 45.61312 ? 15  LEU A CD1 1 
ATOM   128  C  CD2 . LEU A 1 15  ? 15.02925  11.94976  41.25691  1.000 44.14319 ? 15  LEU A CD2 1 
ATOM   129  N  N   . LEU A 1 16  ? 11.27327  10.89893  45.34919  1.000 50.10087 ? 16  LEU A N   1 
ATOM   130  C  CA  . LEU A 1 16  ? 10.78074  11.31747  46.66038  1.000 54.13314 ? 16  LEU A CA  1 
ATOM   131  C  C   . LEU A 1 16  ? 11.31160  10.42948  47.77282  1.000 56.42903 ? 16  LEU A C   1 
ATOM   132  O  O   . LEU A 1 16  ? 11.40873  10.86931  48.92426  1.000 63.59899 ? 16  LEU A O   1 
ATOM   133  C  CB  . LEU A 1 16  ? 9.25534   11.31799  46.69956  1.000 48.94085 ? 16  LEU A CB  1 
ATOM   134  C  CG  . LEU A 1 16  ? 8.53168   12.27044  45.76158  1.000 47.51126 ? 16  LEU A CG  1 
ATOM   135  C  CD1 . LEU A 1 16  ? 7.07163   11.91625  45.77425  1.000 46.96589 ? 16  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A 1 16  ? 8.73346   13.70208  46.20658  1.000 50.40222 ? 16  LEU A CD2 1 
ATOM   137  N  N   . ALA A 1 17  ? 11.66107  9.18738   47.45749  1.000 61.16393 ? 17  ALA A N   1 
ATOM   138  C  CA  . ALA A 1 17  ? 12.09041  8.22685   48.46404  1.000 58.00708 ? 17  ALA A CA  1 
ATOM   139  C  C   . ALA A 1 17  ? 13.58801  7.97441   48.45207  1.000 60.18497 ? 17  ALA A C   1 
ATOM   140  O  O   . ALA A 1 17  ? 14.07617  7.20906   49.28763  1.000 62.56799 ? 17  ALA A O   1 
ATOM   141  C  CB  . ALA A 1 17  ? 11.35335  6.90055   48.26615  1.000 54.17524 ? 17  ALA A CB  1 
ATOM   142  N  N   . SER A 1 18  ? 14.32208  8.56700   47.51885  1.000 61.70776 ? 18  SER A N   1 
ATOM   143  C  CA  . SER A 1 18  ? 15.74886  8.33018   47.39086  1.000 66.34101 ? 18  SER A CA  1 
ATOM   144  C  C   . SER A 1 18  ? 16.51611  9.52623   47.95087  1.000 75.15306 ? 18  SER A C   1 
ATOM   145  O  O   . SER A 1 18  ? 15.94970  10.58710  48.23631  1.000 71.27074 ? 18  SER A O   1 
ATOM   146  C  CB  . SER A 1 18  ? 16.11287  8.06467   45.92495  1.000 66.08132 ? 18  SER A CB  1 
ATOM   147  O  OG  . SER A 1 18  ? 17.25052  7.22826   45.81998  1.000 70.05469 ? 18  SER A OG  1 
ATOM   148  N  N   . ARG A 1 19  ? 17.82181  9.34284   48.12265  1.000 76.58298 ? 19  ARG A N   1 
ATOM   149  C  CA  . ARG A 1 19  ? 18.65276  10.34797  48.76121  1.000 76.63452 ? 19  ARG A CA  1 
ATOM   150  C  C   . ARG A 1 19  ? 19.77559  10.80505  47.83659  1.000 80.70751 ? 19  ARG A C   1 
ATOM   151  O  O   . ARG A 1 19  ? 20.13010  10.13254  46.86274  1.000 79.46670 ? 19  ARG A O   1 
ATOM   152  C  CB  . ARG A 1 19  ? 19.23655  9.81578   50.07106  1.000 83.89555 ? 19  ARG A CB  1 
ATOM   153  C  CG  . ARG A 1 19  ? 18.44923  10.22400  51.30222  1.000 84.54982 ? 19  ARG A CG  1 
ATOM   154  C  CD  . ARG A 1 19  ? 19.37567  10.50301  52.45342  1.000 85.02394 ? 19  ARG A CD  1 
ATOM   155  N  NE  . ARG A 1 19  ? 20.37467  11.50860  52.11425  1.000 94.54676 ? 19  ARG A NE  1 
ATOM   156  C  CZ  . ARG A 1 19  ? 20.31781  12.78145  52.48375  1.000 95.13631 ? 19  ARG A CZ  1 
ATOM   157  N  NH1 . ARG A 1 19  ? 19.32154  13.24473  53.22188  1.000 94.89335 ? 19  ARG A NH1 1 
ATOM   158  N  NH2 . ARG A 1 19  ? 21.29280  13.60744  52.11539  1.000 94.03906 ? 19  ARG A NH2 1 
ATOM   159  N  N   . GLY A 1 20  ? 20.32722  11.97343  48.16134  1.000 81.27966 ? 20  GLY A N   1 
ATOM   160  C  CA  . GLY A 1 20  ? 21.43549  12.54871  47.42614  1.000 81.83252 ? 20  GLY A CA  1 
ATOM   161  C  C   . GLY A 1 20  ? 21.25296  12.58880  45.92040  1.000 82.78845 ? 20  GLY A C   1 
ATOM   162  O  O   . GLY A 1 20  ? 20.66154  13.52811  45.37828  1.000 80.93380 ? 20  GLY A O   1 
ATOM   163  N  N   . ASN A 1 21  ? 21.76284  11.56647  45.23432  1.000 80.14991 ? 21  ASN A N   1 
ATOM   164  C  CA  . ASN A 1 21  ? 21.83318  11.55363  43.78109  1.000 72.24386 ? 21  ASN A CA  1 
ATOM   165  C  C   . ASN A 1 21  ? 21.54989  10.14936  43.27935  1.000 71.30688 ? 21  ASN A C   1 
ATOM   166  O  O   . ASN A 1 21  ? 22.05034  9.16993   43.84003  1.000 70.79881 ? 21  ASN A O   1 
ATOM   167  C  CB  . ASN A 1 21  ? 23.20922  12.00330  43.28669  1.000 69.94825 ? 21  ASN A CB  1 
ATOM   168  C  CG  . ASN A 1 21  ? 23.77245  13.14352  44.10170  1.000 75.79170 ? 21  ASN A CG  1 
ATOM   169  O  OD1 . ASN A 1 21  ? 23.67942  14.30243  43.71511  1.000 76.65128 ? 21  ASN A OD1 1 
ATOM   170  N  ND2 . ASN A 1 21  ? 24.35161  12.81832  45.24952  1.000 84.58545 ? 21  ASN A ND2 1 
ATOM   171  N  N   . VAL A 1 22  ? 20.74947  10.05963  42.21713  1.000 56.06374 ? 22  VAL A N   1 
ATOM   172  C  CA  . VAL A 1 22  ? 20.35062  8.78366   41.64122  1.000 65.72590 ? 22  VAL A CA  1 
ATOM   173  C  C   . VAL A 1 22  ? 20.53403  8.83843   40.13042  1.000 61.73451 ? 22  VAL A C   1 
ATOM   174  O  O   . VAL A 1 22  ? 20.53900  9.90637   39.51451  1.000 58.68786 ? 22  VAL A O   1 
ATOM   175  C  CB  . VAL A 1 22  ? 18.89297  8.40795   41.98921  1.000 58.46817 ? 22  VAL A CB  1 
ATOM   176  C  CG1 . VAL A 1 22  ? 18.62861  8.62343   43.44758  1.000 62.11850 ? 22  VAL A CG1 1 
ATOM   177  C  CG2 . VAL A 1 22  ? 17.92392  9.23346   41.17344  1.000 55.89415 ? 22  VAL A CG2 1 
ATOM   178  N  N   . LYS A 1 23  ? 20.69365  7.65714   39.54086  1.000 57.50938 ? 23  LYS A N   1 
ATOM   179  C  CA  . LYS A 1 23  ? 20.82269  7.48818   38.10012  1.000 48.54304 ? 23  LYS A CA  1 
ATOM   180  C  C   . LYS A 1 23  ? 19.49690  6.95072   37.57308  1.000 54.83390 ? 23  LYS A C   1 
ATOM   181  O  O   . LYS A 1 23  ? 19.11140  5.81721   37.88157  1.000 54.88491 ? 23  LYS A O   1 
ATOM   182  C  CB  . LYS A 1 23  ? 21.95720  6.52266   37.76764  1.000 54.60426 ? 23  LYS A CB  1 
ATOM   183  C  CG  . LYS A 1 23  ? 23.29954  6.76906   38.43296  1.000 61.22945 ? 23  LYS A CG  1 
ATOM   184  C  CD  . LYS A 1 23  ? 23.92554  8.07439   37.99074  1.000 65.82205 ? 23  LYS A CD  1 
ATOM   185  C  CE  . LYS A 1 23  ? 25.27200  8.28777   38.67403  1.000 66.07906 ? 23  LYS A CE  1 
ATOM   186  N  NZ  . LYS A 1 23  ? 26.12822  7.06548   38.76966  1.000 68.18900 ? 23  LYS A NZ  1 
ATOM   187  N  N   . LEU A 1 24  ? 18.80152  7.73626   36.76055  1.000 49.30246 ? 24  LEU A N   1 
ATOM   188  C  CA  . LEU A 1 24  ? 17.50215  7.28220   36.30255  1.000 47.75096 ? 24  LEU A CA  1 
ATOM   189  C  C   . LEU A 1 24  ? 17.31807  7.56743   34.81900  1.000 42.32278 ? 24  LEU A C   1 
ATOM   190  O  O   . LEU A 1 24  ? 17.96306  8.43719   34.23401  1.000 45.96266 ? 24  LEU A O   1 
ATOM   191  C  CB  . LEU A 1 24  ? 16.38873  7.89886   37.15021  1.000 48.57924 ? 24  LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 24  ? 16.02875  9.35631   36.93640  1.000 48.63941 ? 24  LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 24  ? 14.54581  9.53018   37.10884  1.000 50.17165 ? 24  LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 24  ? 16.76574  10.20594  37.94629  1.000 54.22565 ? 24  LEU A CD2 1 
ATOM   195  N  N   . ASN A 1 25  ? 16.43633  6.78069   34.22270  1.000 43.45415 ? 25  ASN A N   1 
ATOM   196  C  CA  . ASN A 1 25  ? 16.16357  6.80156   32.79818  1.000 41.12229 ? 25  ASN A CA  1 
ATOM   197  C  C   . ASN A 1 25  ? 15.08223  7.83381   32.51053  1.000 37.93135 ? 25  ASN A C   1 
ATOM   198  O  O   . ASN A 1 25  ? 14.02878  7.83640   33.15384  1.000 40.91332 ? 25  ASN A O   1 
ATOM   199  C  CB  . ASN A 1 25  ? 15.73402  5.39971   32.35448  1.000 46.13604 ? 25  ASN A CB  1 
ATOM   200  C  CG  . ASN A 1 25  ? 15.47783  5.29175   30.86448  1.000 43.67291 ? 25  ASN A CG  1 
ATOM   201  O  OD1 . ASN A 1 25  ? 14.82577  6.13910   30.27188  1.000 43.26473 ? 25  ASN A OD1 1 
ATOM   202  N  ND2 . ASN A 1 25  ? 15.98064  4.22708   30.25837  1.000 50.57323 ? 25  ASN A ND2 1 
ATOM   203  N  N   . LEU A 1 26  ? 15.33557  8.69575   31.52885  1.000 42.77097 ? 26  LEU A N   1 
ATOM   204  C  CA  . LEU A 1 26  ? 14.49268  9.85891   31.28463  1.000 38.13837 ? 26  LEU A CA  1 
ATOM   205  C  C   . LEU A 1 26  ? 13.92368  9.89182   29.86966  1.000 39.31353 ? 26  LEU A C   1 
ATOM   206  O  O   . LEU A 1 26  ? 13.56029  10.96620  29.37107  1.000 33.27165 ? 26  LEU A O   1 
ATOM   207  C  CB  . LEU A 1 26  ? 15.28084  11.13651  31.56575  1.000 40.69836 ? 26  LEU A CB  1 
ATOM   208  C  CG  . LEU A 1 26  ? 15.85593  11.22028  32.97386  1.000 42.95856 ? 26  LEU A CG  1 
ATOM   209  C  CD1 . LEU A 1 26  ? 16.83988  12.37470  33.09990  1.000 43.96141 ? 26  LEU A CD1 1 
ATOM   210  C  CD2 . LEU A 1 26  ? 14.71164  11.36092  33.95826  1.000 41.79038 ? 26  LEU A CD2 1 
ATOM   211  N  N   . ASP A 1 27  ? 13.83745  8.74809   29.20046  1.000 34.51495 ? 27  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 27  ? 13.11093  8.71324   27.93549  1.000 38.90993 ? 27  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 27  ? 12.16244  7.52798   27.88541  1.000 34.19393 ? 27  ASP A C   1 
ATOM   214  O  O   . ASP A 1 27  ? 11.91749  6.97114   26.81267  1.000 32.11587 ? 27  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 27  ? 14.05683  8.71072   26.73150  1.000 43.29198 ? 27  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 27  ? 15.15301  7.65850   26.82752  1.000 45.89755 ? 27  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 27  ? 14.90512  6.52998   27.32852  1.000 38.77654 ? 27  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 27  ? 16.27753  7.98854   26.39622  1.000 52.77736 ? 27  ASP A OD2 1 
ATOM   219  N  N   . LEU A 1 28  ? 11.63234  7.13631   29.04797  1.000 28.64287 ? 28  LEU A N   1 
ATOM   220  C  CA  . LEU A 1 28  ? 10.58264  6.12772   29.15012  1.000 26.15651 ? 28  LEU A CA  1 
ATOM   221  C  C   . LEU A 1 28  ? 11.09208  4.76885   28.67673  1.000 36.68617 ? 28  LEU A C   1 
ATOM   222  O  O   . LEU A 1 28  ? 10.42174  4.07508   27.91190  1.000 38.47967 ? 28  LEU A O   1 
ATOM   223  C  CB  . LEU A 1 28  ? 9.36280   6.53107   28.32869  1.000 31.82853 ? 28  LEU A CB  1 
ATOM   224  C  CG  . LEU A 1 28  ? 8.67834   7.84288   28.68700  1.000 32.67711 ? 28  LEU A CG  1 
ATOM   225  C  CD1 . LEU A 1 28  ? 7.52878   8.12280   27.68553  1.000 33.43328 ? 28  LEU A CD1 1 
ATOM   226  C  CD2 . LEU A 1 28  ? 8.24322   7.92313   30.10474  1.000 24.91479 ? 28  LEU A CD2 1 
ATOM   227  N  N   . ARG A 1 29  ? 12.30735  4.40651   29.09024  1.000 36.89297 ? 29  ARG A N   1 
ATOM   228  C  CA  . ARG A 1 29  ? 12.96484  3.15413   28.71393  1.000 35.33219 ? 29  ARG A CA  1 
ATOM   229  C  C   . ARG A 1 29  ? 13.16052  3.02069   27.20894  1.000 43.66296 ? 29  ARG A C   1 
ATOM   230  O  O   . ARG A 1 29  ? 13.37495  1.91290   26.70971  1.000 46.11528 ? 29  ARG A O   1 
ATOM   231  C  CB  . ARG A 1 29  ? 12.21404  1.91813   29.23811  1.000 36.50241 ? 29  ARG A CB  1 
ATOM   232  C  CG  . ARG A 1 29  ? 11.51712  2.07573   30.59931  1.000 46.69628 ? 29  ARG A CG  1 
ATOM   233  C  CD  . ARG A 1 29  ? 12.51266  2.15037   31.73017  1.000 41.27949 ? 29  ARG A CD  1 
ATOM   234  N  NE  . ARG A 1 29  ? 11.97007  2.87390   32.87692  1.000 50.34614 ? 29  ARG A NE  1 
ATOM   235  C  CZ  . ARG A 1 29  ? 11.48124  2.29973   33.96877  1.000 60.45050 ? 29  ARG A CZ  1 
ATOM   236  N  NH1 . ARG A 1 29  ? 11.48039  0.98279   34.11690  1.000 56.78983 ? 29  ARG A NH1 1 
ATOM   237  N  NH2 . ARG A 1 29  ? 10.98345  3.06621   34.93936  1.000 54.84346 ? 29  ARG A NH2 1 
ATOM   238  N  N   . LYS A 1 30  ? 13.10206  4.11880   26.45633  1.000 42.10009 ? 30  LYS A N   1 
ATOM   239  C  CA  . LYS A 1 30  ? 13.32513  4.00751   25.01895  1.000 39.54268 ? 30  LYS A CA  1 
ATOM   240  C  C   . LYS A 1 30  ? 14.77265  3.64788   24.71351  1.000 53.21532 ? 30  LYS A C   1 
ATOM   241  O  O   . LYS A 1 30  ? 15.03985  2.81469   23.83580  1.000 52.67971 ? 30  LYS A O   1 
ATOM   242  C  CB  . LYS A 1 30  ? 12.94700  5.30905   24.31585  1.000 35.56372 ? 30  LYS A CB  1 
ATOM   243  C  CG  . LYS A 1 30  ? 13.42780  5.38465   22.86634  1.000 35.96762 ? 30  LYS A CG  1 
ATOM   244  C  CD  . LYS A 1 30  ? 12.59216  4.48592   21.96471  1.000 36.20328 ? 30  LYS A CD  1 
ATOM   245  C  CE  . LYS A 1 30  ? 12.90882  4.71533   20.48714  1.000 40.62309 ? 30  LYS A CE  1 
ATOM   246  N  NZ  . LYS A 1 30  ? 12.04332  3.86364   19.63373  1.000 42.83041 ? 30  LYS A NZ  1 
ATOM   247  N  N   . THR A 1 31  ? 15.71892  4.26153   25.43009  1.000 49.06983 ? 31  THR A N   1 
ATOM   248  C  CA  . THR A 1 31  ? 17.13732  4.12967   25.12711  1.000 50.28356 ? 31  THR A CA  1 
ATOM   249  C  C   . THR A 1 31  ? 17.97063  3.58540   26.27352  1.000 56.29440 ? 31  THR A C   1 
ATOM   250  O  O   . THR A 1 31  ? 19.20521  3.65560   26.19374  1.000 64.01933 ? 31  THR A O   1 
ATOM   251  C  CB  . THR A 1 31  ? 17.73583  5.47132   24.69987  1.000 59.51821 ? 31  THR A CB  1 
ATOM   252  O  OG1 . THR A 1 31  ? 18.18450  6.18110   25.86824  1.000 53.40985 ? 31  THR A OG1 1 
ATOM   253  C  CG2 . THR A 1 31  ? 16.73621  6.29684   23.89813  1.000 61.67586 ? 31  THR A CG2 1 
ATOM   254  N  N   . ASN A 1 32  ? 17.35594  3.09999   27.35620  1.000 60.19846 ? 32  ASN A N   1 
ATOM   255  C  CA  . ASN A 1 32  ? 18.10083  2.29106   28.32184  1.000 67.76814 ? 32  ASN A CA  1 
ATOM   256  C  C   . ASN A 1 32  ? 19.13226  3.13971   29.08352  1.000 67.40034 ? 32  ASN A C   1 
ATOM   257  O  O   . ASN A 1 32  ? 19.53078  2.78332   30.19811  1.000 63.49214 ? 32  ASN A O   1 
ATOM   258  C  CB  . ASN A 1 32  ? 18.67704  1.08173   27.53970  1.000 63.96324 ? 32  ASN A CB  1 
ATOM   259  C  CG  . ASN A 1 32  ? 19.78131  0.30678   28.25641  1.000 67.03503 ? 32  ASN A CG  1 
ATOM   260  O  OD1 . ASN A 1 32  ? 20.57777  0.83445   29.01823  1.000 73.57619 ? 32  ASN A OD1 1 
ATOM   261  N  ND2 . ASN A 1 32  ? 19.82574  -0.98741  27.98134  1.000 68.85533 ? 32  ASN A ND2 1 
ATOM   262  N  N   . ARG A 1 33  ? 19.52014  4.29115   28.52944  1.000 58.99898 ? 33  ARG A N   1 
ATOM   263  C  CA  . ARG A 1 33  ? 20.47224  5.17989   29.18621  1.000 52.62538 ? 33  ARG A CA  1 
ATOM   264  C  C   . ARG A 1 33  ? 19.87401  5.80907   30.43997  1.000 56.75614 ? 33  ARG A C   1 
ATOM   265  O  O   . ARG A 1 33  ? 18.70732  6.21701   30.45973  1.000 51.64095 ? 33  ARG A O   1 
ATOM   266  C  CB  . ARG A 1 33  ? 20.90694  6.29434   28.23385  1.000 56.49991 ? 33  ARG A CB  1 
ATOM   267  C  CG  . ARG A 1 33  ? 21.28149  7.60160   28.94738  1.000 55.61361 ? 33  ARG A CG  1 
ATOM   268  C  CD  . ARG A 1 33  ? 21.22683  8.80833   28.02474  1.000 56.57995 ? 33  ARG A CD  1 
ATOM   269  N  NE  . ARG A 1 33  ? 22.09669  9.88979   28.47354  1.000 59.42136 ? 33  ARG A NE  1 
ATOM   270  C  CZ  . ARG A 1 33  ? 21.98953  11.14977  28.07243  1.000 60.87784 ? 33  ARG A CZ  1 
ATOM   271  N  NH1 . ARG A 1 33  ? 21.02091  11.53577  27.25917  1.000 67.88339 ? 33  ARG A NH1 1 
ATOM   272  N  NH2 . ARG A 1 33  ? 22.87349  12.04592  28.50078  1.000 61.81924 ? 33  ARG A NH2 1 
ATOM   273  N  N   . VAL A 1 34  ? 20.69004  5.91017   31.48441  1.000 53.86756 ? 34  VAL A N   1 
ATOM   274  C  CA  . VAL A 1 34  ? 20.30174  6.59693   32.70648  1.000 47.81678 ? 34  VAL A CA  1 
ATOM   275  C  C   . VAL A 1 34  ? 21.11534  7.88012   32.83218  1.000 54.74504 ? 34  VAL A C   1 
ATOM   276  O  O   . VAL A 1 34  ? 22.20921  8.01931   32.27631  1.000 57.07194 ? 34  VAL A O   1 
ATOM   277  C  CB  . VAL A 1 34  ? 20.47830  5.70724   33.95321  1.000 50.35390 ? 34  VAL A CB  1 
ATOM   278  C  CG1 . VAL A 1 34  ? 19.96444  4.29839   33.67800  1.000 48.03271 ? 34  VAL A CG1 1 
ATOM   279  C  CG2 . VAL A 1 34  ? 21.94263  5.67722   34.36991  1.000 50.39957 ? 34  VAL A CG2 1 
ATOM   280  N  N   . GLN A 1 35  ? 20.55301  8.84093   33.56463  1.000 53.52707 ? 35  GLN A N   1 
ATOM   281  C  CA  . GLN A 1 35  ? 21.20453  10.11276  33.83480  1.000 48.71653 ? 35  GLN A CA  1 
ATOM   282  C  C   . GLN A 1 35  ? 21.07236  10.44653  35.31558  1.000 51.09050 ? 35  GLN A C   1 
ATOM   283  O  O   . GLN A 1 35  ? 20.15086  9.98427   35.99372  1.000 54.95744 ? 35  GLN A O   1 
ATOM   284  C  CB  . GLN A 1 35  ? 20.60619  11.23508  32.99155  1.000 50.81490 ? 35  GLN A CB  1 
ATOM   285  C  CG  . GLN A 1 35  ? 20.09565  10.80438  31.64036  1.000 52.66435 ? 35  GLN A CG  1 
ATOM   286  C  CD  . GLN A 1 35  ? 19.77339  11.98757  30.74844  1.000 59.27821 ? 35  GLN A CD  1 
ATOM   287  O  OE1 . GLN A 1 35  ? 20.47047  13.00605  30.78049  1.000 63.36732 ? 35  GLN A OE1 1 
ATOM   288  N  NE2 . GLN A 1 35  ? 18.70511  11.86746  29.95496  1.000 51.88978 ? 35  GLN A NE2 1 
ATOM   289  N  N   . GLU A 1 36  ? 21.99734  11.25044  35.82174  1.000 51.01865 ? 36  GLU A N   1 
ATOM   290  C  CA  . GLU A 1 36  ? 22.00953  11.55991  37.24256  1.000 53.05822 ? 36  GLU A CA  1 
ATOM   291  C  C   . GLU A 1 36  ? 21.15671  12.78599  37.52498  1.000 54.62770 ? 36  GLU A C   1 
ATOM   292  O  O   . GLU A 1 36  ? 21.27842  13.81131  36.84365  1.000 57.63404 ? 36  GLU A O   1 
ATOM   293  C  CB  . GLU A 1 36  ? 23.42812  11.78840  37.75955  1.000 57.22960 ? 36  GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 36  ? 23.46251  11.92373  39.26278  1.000 60.60467 ? 36  GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 36  ? 24.63870  11.21252  39.88949  1.000 71.30607 ? 36  GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 36  ? 25.78649  11.46000  39.46123  1.000 72.57305 ? 36  GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 36  ? 24.41412  10.38997  40.80572  1.000 76.10538 ? 36  GLU A OE2 1 
ATOM   298  N  N   . VAL A 1 37  ? 20.29987  12.67031  38.53512  1.000 58.86186 ? 37  VAL A N   1 
ATOM   299  C  CA  . VAL A 1 37  ? 19.47280  13.76326  39.02832  1.000 56.05550 ? 37  VAL A CA  1 
ATOM   300  C  C   . VAL A 1 37  ? 19.76394  13.88894  40.51610  1.000 62.33492 ? 37  VAL A C   1 
ATOM   301  O  O   . VAL A 1 37  ? 19.49765  12.95585  41.28352  1.000 65.41183 ? 37  VAL A O   1 
ATOM   302  C  CB  . VAL A 1 37  ? 17.97823  13.49900  38.78085  1.000 61.17073 ? 37  VAL A CB  1 
ATOM   303  C  CG1 . VAL A 1 37  ? 17.12162  14.34899  39.69966  1.000 61.86087 ? 37  VAL A CG1 1 
ATOM   304  C  CG2 . VAL A 1 37  ? 17.61701  13.71668  37.31600  1.000 58.95890 ? 37  VAL A CG2 1 
ATOM   305  N  N   . GLU A 1 38  ? 20.33680  15.01426  40.92620  1.000 66.41278 ? 38  GLU A N   1 
ATOM   306  C  CA  . GLU A 1 38  ? 20.62762  15.19142  42.33726  1.000 71.15236 ? 38  GLU A CA  1 
ATOM   307  C  C   . GLU A 1 38  ? 19.37416  15.64757  43.07238  1.000 74.31049 ? 38  GLU A C   1 
ATOM   308  O  O   . GLU A 1 38  ? 18.63426  16.51788  42.60060  1.000 67.35018 ? 38  GLU A O   1 
ATOM   309  C  CB  . GLU A 1 38  ? 21.77910  16.17640  42.54177  1.000 79.70622 ? 38  GLU A CB  1 
ATOM   310  C  CG  . GLU A 1 38  ? 21.54572  17.51902  41.96648  1.000 77.47618 ? 38  GLU A CG  1 
ATOM   311  C  CD  . GLU A 1 38  ? 22.32263  18.65111  42.62747  1.000 91.30705 ? 38  GLU A CD  1 
ATOM   312  O  OE1 . GLU A 1 38  ? 22.99727  19.39482  41.87471  1.000 94.29300 ? 38  GLU A OE1 1 
ATOM   313  O  OE2 . GLU A 1 38  ? 22.24708  18.81977  43.87479  1.000 77.41300 ? 38  GLU A OE2 1 
ATOM   314  N  N   . ILE A 1 39  ? 19.13499  15.03022  44.22482  1.000 75.87092 ? 39  ILE A N   1 
ATOM   315  C  CA  . ILE A 1 39  ? 17.93722  15.26564  45.01982  1.000 74.06889 ? 39  ILE A CA  1 
ATOM   316  C  C   . ILE A 1 39  ? 18.24870  16.30562  46.08179  1.000 68.51749 ? 39  ILE A C   1 
ATOM   317  O  O   . ILE A 1 39  ? 19.26343  16.21324  46.78204  1.000 77.34375 ? 39  ILE A O   1 
ATOM   318  C  CB  . ILE A 1 39  ? 17.44340  13.95852  45.66172  1.000 73.68236 ? 39  ILE A CB  1 
ATOM   319  C  CG1 . ILE A 1 39  ? 16.90016  13.01655  44.59391  1.000 65.54766 ? 39  ILE A CG1 1 
ATOM   320  C  CG2 . ILE A 1 39  ? 16.40804  14.24276  46.73850  1.000 78.27610 ? 39  ILE A CG2 1 
ATOM   321  C  CD1 . ILE A 1 39  ? 16.83395  11.57281  45.03028  1.000 69.63558 ? 39  ILE A CD1 1 
ATOM   322  N  N   . LYS A 1 40  ? 17.37763  17.29407  46.20449  1.000 69.91905 ? 40  LYS A N   1 
ATOM   323  C  CA  . LYS A 1 40  ? 17.48359  18.29796  47.24492  1.000 68.66503 ? 40  LYS A CA  1 
ATOM   324  C  C   . LYS A 1 40  ? 16.20535  18.30842  48.07163  1.000 68.56055 ? 40  LYS A C   1 
ATOM   325  O  O   . LYS A 1 40  ? 15.21267  17.66283  47.73480  1.000 72.10825 ? 40  LYS A O   1 
ATOM   326  C  CB  . LYS A 1 40  ? 17.75171  19.68230  46.64716  1.000 73.60293 ? 40  LYS A CB  1 
ATOM   327  C  CG  . LYS A 1 40  ? 18.92691  19.73777  45.68678  1.000 72.93578 ? 40  LYS A CG  1 
ATOM   328  C  CD  . LYS A 1 40  ? 20.16593  20.22072  46.41461  1.000 76.12530 ? 40  LYS A CD  1 
ATOM   329  C  CE  . LYS A 1 40  ? 19.94753  21.61341  46.97143  1.000 80.23882 ? 40  LYS A CE  1 
ATOM   330  N  NZ  . LYS A 1 40  ? 20.54446  21.77578  48.32936  1.000 84.88287 ? 40  LYS A NZ  1 
ATOM   331  N  N   . ASP A 1 41  ? 16.24263  19.05440  49.17497  1.000 76.78475 ? 41  ASP A N   1 
ATOM   332  C  CA  . ASP A 1 41  ? 15.07437  19.14636  50.04638  1.000 81.37393 ? 41  ASP A CA  1 
ATOM   333  C  C   . ASP A 1 41  ? 13.87460  19.72630  49.30893  1.000 73.03804 ? 41  ASP A C   1 
ATOM   334  O  O   . ASP A 1 41  ? 12.74223  19.25865  49.47802  1.000 69.98729 ? 41  ASP A O   1 
ATOM   335  C  CB  . ASP A 1 41  ? 15.40613  19.99173  51.27745  1.000 79.15902 ? 41  ASP A CB  1 
ATOM   336  C  CG  . ASP A 1 41  ? 16.03020  19.17566  52.38236  1.000 81.28184 ? 41  ASP A CG  1 
ATOM   337  O  OD1 . ASP A 1 41  ? 16.34621  17.99152  52.12467  1.000 82.93453 ? 41  ASP A OD1 1 
ATOM   338  O  OD2 . ASP A 1 41  ? 16.21508  19.71169  53.49790  1.000 85.95448 ? 41  ASP A OD2 1 
ATOM   339  N  N   . GLU A 1 42  ? 14.10062  20.74853  48.49199  1.000 81.67004 ? 42  GLU A N   1 
ATOM   340  C  CA  . GLU A 1 42  ? 13.00598  21.38340  47.77789  1.000 80.17126 ? 42  GLU A CA  1 
ATOM   341  C  C   . GLU A 1 42  ? 12.63350  20.64965  46.50000  1.000 75.86811 ? 42  GLU A C   1 
ATOM   342  O  O   . GLU A 1 42  ? 11.56387  20.91627  45.94870  1.000 77.65958 ? 42  GLU A O   1 
ATOM   343  C  CB  . GLU A 1 42  ? 13.33082  22.85309  47.46868  1.000 81.26062 ? 42  GLU A CB  1 
ATOM   344  C  CG  . GLU A 1 42  ? 14.73468  23.17104  46.93486  1.000 86.25231 ? 42  GLU A CG  1 
ATOM   345  C  CD  . GLU A 1 42  ? 15.85720  22.94955  47.95146  1.000 85.43642 ? 42  GLU A CD  1 
ATOM   346  O  OE1 . GLU A 1 42  ? 15.69617  23.32427  49.13252  1.000 90.48460 ? 42  GLU A OE1 1 
ATOM   347  O  OE2 . GLU A 1 42  ? 16.91837  22.42776  47.55983  1.000 86.09504 ? 42  GLU A OE2 1 
ATOM   348  N  N   . GLY A 1 43  ? 13.46190  19.72479  46.03497  1.000 65.93528 ? 43  GLY A N   1 
ATOM   349  C  CA  . GLY A 1 43  ? 13.08579  18.94888  44.86457  1.000 69.30879 ? 43  GLY A CA  1 
ATOM   350  C  C   . GLY A 1 43  ? 14.26643  18.20971  44.28120  1.000 65.28510 ? 43  GLY A C   1 
ATOM   351  O  O   . GLY A 1 43  ? 15.24000  17.90466  44.97863  1.000 69.26130 ? 43  GLY A O   1 
ATOM   352  N  N   . ALA A 1 44  ? 14.16559  17.92432  42.99288  1.000 54.88982 ? 44  ALA A N   1 
ATOM   353  C  CA  . ALA A 1 44  ? 15.20409  17.22129  42.26587  1.000 62.41773 ? 44  ALA A CA  1 
ATOM   354  C  C   . ALA A 1 44  ? 15.63045  18.10658  41.11108  1.000 65.51546 ? 44  ALA A C   1 
ATOM   355  O  O   . ALA A 1 44  ? 14.77847  18.65601  40.40400  1.000 56.37208 ? 44  ALA A O   1 
ATOM   356  C  CB  . ALA A 1 44  ? 14.69901  15.86996  41.75942  1.000 58.73084 ? 44  ALA A CB  1 
ATOM   357  N  N   . VAL A 1 45  ? 16.93660  18.27037  40.93148  1.000 64.39990 ? 45  VAL A N   1 
ATOM   358  C  CA  . VAL A 1 45  ? 17.44073  19.03727  39.80753  1.000 64.37409 ? 45  VAL A CA  1 
ATOM   359  C  C   . VAL A 1 45  ? 17.98731  18.05031  38.78624  1.000 63.77270 ? 45  VAL A C   1 
ATOM   360  O  O   . VAL A 1 45  ? 18.68094  17.08538  39.13484  1.000 63.37456 ? 45  VAL A O   1 
ATOM   361  C  CB  . VAL A 1 45  ? 18.48201  20.08887  40.23847  1.000 65.58213 ? 45  VAL A CB  1 
ATOM   362  C  CG1 . VAL A 1 45  ? 19.84112  19.53394  40.31185  1.000 72.45201 ? 45  VAL A CG1 1 
ATOM   363  C  CG2 . VAL A 1 45  ? 18.48256  21.25256  39.28529  1.000 65.30706 ? 45  VAL A CG2 1 
ATOM   364  N  N   . PHE A 1 46  ? 17.62774  18.27041  37.53471  1.000 63.83087 ? 46  PHE A N   1 
ATOM   365  C  CA  . PHE A 1 46  ? 17.76609  17.30938  36.45696  1.000 61.56129 ? 46  PHE A CA  1 
ATOM   366  C  C   . PHE A 1 46  ? 19.07549  17.56779  35.71907  1.000 67.77655 ? 46  PHE A C   1 
ATOM   367  O  O   . PHE A 1 46  ? 19.79642  18.49836  36.09589  1.000 73.50856 ? 46  PHE A O   1 
ATOM   368  C  CB  . PHE A 1 46  ? 16.52175  17.41714  35.57308  1.000 66.32592 ? 46  PHE A CB  1 
ATOM   369  C  CG  . PHE A 1 46  ? 15.39661  16.53569  36.03053  1.000 58.67937 ? 46  PHE A CG  1 
ATOM   370  C  CD1 . PHE A 1 46  ? 14.81592  16.72623  37.27213  1.000 61.26953 ? 46  PHE A CD1 1 
ATOM   371  C  CD2 . PHE A 1 46  ? 14.93199  15.51236  35.23478  1.000 57.28954 ? 46  PHE A CD2 1 
ATOM   372  C  CE1 . PHE A 1 46  ? 13.79162  15.91472  37.70613  1.000 54.01267 ? 46  PHE A CE1 1 
ATOM   373  C  CE2 . PHE A 1 46  ? 13.90217  14.69735  35.66534  1.000 56.85398 ? 46  PHE A CE2 1 
ATOM   374  C  CZ  . PHE A 1 46  ? 13.33169  14.89927  36.90083  1.000 50.94622 ? 46  PHE A CZ  1 
ATOM   375  N  N   . PRO A 1 47  ? 19.45329  16.78007  34.70201  1.000 67.51763 ? 47  PRO A N   1 
ATOM   376  C  CA  . PRO A 1 47  ? 20.74896  17.02560  34.04394  1.000 68.81839 ? 47  PRO A CA  1 
ATOM   377  C  C   . PRO A 1 47  ? 20.80818  18.31324  33.23559  1.000 74.79945 ? 47  PRO A C   1 
ATOM   378  O  O   . PRO A 1 47  ? 21.84502  18.58438  32.61874  1.000 77.44816 ? 47  PRO A O   1 
ATOM   379  C  CB  . PRO A 1 47  ? 20.93807  15.79476  33.13885  1.000 70.67127 ? 47  PRO A CB  1 
ATOM   380  C  CG  . PRO A 1 47  ? 19.79708  14.87584  33.41831  1.000 65.49886 ? 47  PRO A CG  1 
ATOM   381  C  CD  . PRO A 1 47  ? 18.73107  15.65484  34.07964  1.000 60.81436 ? 47  PRO A CD  1 
ATOM   382  N  N   . ASP A 1 48  ? 19.74288  19.11243  33.22438  1.000 75.09566 ? 48  ASP A N   1 
ATOM   383  C  CA  . ASP A 1 48  ? 19.75981  20.44357  32.63224  1.000 68.94643 ? 48  ASP A CA  1 
ATOM   384  C  C   . ASP A 1 48  ? 19.86759  21.56382  33.65827  1.000 71.09247 ? 48  ASP A C   1 
ATOM   385  O  O   . ASP A 1 48  ? 20.26738  22.67585  33.29680  1.000 75.04279 ? 48  ASP A O   1 
ATOM   386  C  CB  . ASP A 1 48  ? 18.51509  20.63277  31.74921  1.000 69.82323 ? 48  ASP A CB  1 
ATOM   387  C  CG  . ASP A 1 48  ? 17.32575  21.17999  32.51233  1.000 69.03556 ? 48  ASP A CG  1 
ATOM   388  O  OD1 . ASP A 1 48  ? 17.14836  20.78572  33.68179  1.000 74.76386 ? 48  ASP A OD1 1 
ATOM   389  O  OD2 . ASP A 1 48  ? 16.54744  21.97239  31.94830  1.000 68.42768 ? 48  ASP A OD2 1 
ATOM   390  N  N   . GLY A 1 49  ? 19.55337  21.29740  34.92151  1.000 72.97284 ? 49  GLY A N   1 
ATOM   391  C  CA  . GLY A 1 49  ? 19.56844  22.31339  35.95434  1.000 65.87538 ? 49  GLY A CA  1 
ATOM   392  C  C   . GLY A 1 49  ? 18.19615  22.77449  36.39065  1.000 69.56976 ? 49  GLY A C   1 
ATOM   393  O  O   . GLY A 1 49  ? 18.10243  23.59134  37.31708  1.000 70.56436 ? 49  GLY A O   1 
ATOM   394  N  N   . THR A 1 50  ? 17.12964  22.28957  35.75598  1.000 74.30002 ? 50  THR A N   1 
ATOM   395  C  CA  . THR A 1 50  ? 15.78664  22.58035  36.23610  1.000 72.37645 ? 50  THR A CA  1 
ATOM   396  C  C   . THR A 1 50  ? 15.51885  21.80069  37.51150  1.000 65.54739 ? 50  THR A C   1 
ATOM   397  O  O   . THR A 1 50  ? 15.78236  20.59755  37.58393  1.000 62.64875 ? 50  THR A O   1 
ATOM   398  C  CB  . THR A 1 50  ? 14.73778  22.23036  35.17938  1.000 69.49475 ? 50  THR A CB  1 
ATOM   399  O  OG1 . THR A 1 50  ? 15.14730  22.73359  33.89831  1.000 68.03046 ? 50  THR A OG1 1 
ATOM   400  C  CG2 . THR A 1 50  ? 13.38390  22.81629  35.56310  1.000 70.50239 ? 50  THR A CG2 1 
ATOM   401  N  N   . LEU A 1 51  ? 15.01299  22.48552  38.52543  1.000 69.28399 ? 51  LEU A N   1 
ATOM   402  C  CA  . LEU A 1 51  ? 14.59589  21.82837  39.75079  1.000 62.96178 ? 51  LEU A CA  1 
ATOM   403  C  C   . LEU A 1 51  ? 13.09419  21.62776  39.64278  1.000 70.85952 ? 51  LEU A C   1 
ATOM   404  O  O   . LEU A 1 51  ? 12.32785  22.59654  39.61897  1.000 70.38317 ? 51  LEU A O   1 
ATOM   405  C  CB  . LEU A 1 51  ? 14.97972  22.63142  40.99304  1.000 70.46785 ? 51  LEU A CB  1 
ATOM   406  C  CG  . LEU A 1 51  ? 14.33805  22.31094  42.35369  1.000 67.49105 ? 51  LEU A CG  1 
ATOM   407  C  CD1 . LEU A 1 51  ? 15.26967  22.82525  43.43043  1.000 75.93360 ? 51  LEU A CD1 1 
ATOM   408  C  CD2 . LEU A 1 51  ? 12.96118  22.92266  42.57456  1.000 76.87791 ? 51  LEU A CD2 1 
ATOM   409  N  N   . VAL A 1 52  ? 12.68744  20.37209  39.51818  1.000 67.48663 ? 52  VAL A N   1 
ATOM   410  C  CA  . VAL A 1 52  ? 11.29668  19.99155  39.70958  1.000 63.90441 ? 52  VAL A CA  1 
ATOM   411  C  C   . VAL A 1 52  ? 11.07229  19.87039  41.20760  1.000 65.34280 ? 52  VAL A C   1 
ATOM   412  O  O   . VAL A 1 52  ? 11.69466  19.03126  41.86580  1.000 63.19261 ? 52  VAL A O   1 
ATOM   413  C  CB  . VAL A 1 52  ? 10.98601  18.67773  38.98426  1.000 60.35526 ? 52  VAL A CB  1 
ATOM   414  C  CG1 . VAL A 1 52  ? 9.49711   18.50598  38.82697  1.000 65.60272 ? 52  VAL A CG1 1 
ATOM   415  C  CG2 . VAL A 1 52  ? 11.66508  18.67429  37.62239  1.000 62.98666 ? 52  VAL A CG2 1 
ATOM   416  N  N   . GLU A 1 53  ? 10.22576  20.73560  41.75614  1.000 67.37564 ? 53  GLU A N   1 
ATOM   417  C  CA  . GLU A 1 53  ? 10.08237  20.80066  43.20179  1.000 73.45835 ? 53  GLU A CA  1 
ATOM   418  C  C   . GLU A 1 53  ? 9.22459   19.65646  43.72187  1.000 70.22320 ? 53  GLU A C   1 
ATOM   419  O  O   . GLU A 1 53  ? 8.33171   19.15677  43.03291  1.000 69.85478 ? 53  GLU A O   1 
ATOM   420  C  CB  . GLU A 1 53  ? 9.49294   22.14293  43.63655  1.000 79.01920 ? 53  GLU A CB  1 
ATOM   421  C  CG  . GLU A 1 53  ? 8.22798   22.54586  42.91892  1.000 84.15811 ? 53  GLU A CG  1 
ATOM   422  C  CD  . GLU A 1 53  ? 8.44091   23.75587  42.02853  1.000 91.95479 ? 53  GLU A CD  1 
ATOM   423  O  OE1 . GLU A 1 53  ? 9.61576   24.10411  41.78117  1.000 94.34051 ? 53  GLU A OE1 1 
ATOM   424  O  OE2 . GLU A 1 53  ? 7.44045   24.35693  41.57662  1.000 94.35757 ? 53  GLU A OE2 1 
ATOM   425  N  N   . ARG A 1 54  ? 9.51140   19.25146  44.96014  1.000 70.72048 ? 54  ARG A N   1 
ATOM   426  C  CA  . ARG A 1 54  ? 8.84195   18.13988  45.62692  1.000 66.41397 ? 54  ARG A CA  1 
ATOM   427  C  C   . ARG A 1 54  ? 7.34073   18.15442  45.36690  1.000 62.87678 ? 54  ARG A C   1 
ATOM   428  O  O   . ARG A 1 54  ? 6.74478   17.10831  45.08735  1.000 59.95649 ? 54  ARG A O   1 
ATOM   429  C  CB  . ARG A 1 54  ? 9.12530   18.18875  47.13235  1.000 72.40006 ? 54  ARG A CB  1 
ATOM   430  C  CG  . ARG A 1 54  ? 9.27895   16.81533  47.75885  1.000 70.80124 ? 54  ARG A CG  1 
ATOM   431  C  CD  . ARG A 1 54  ? 10.34519  16.75344  48.86087  1.000 72.46549 ? 54  ARG A CD  1 
ATOM   432  N  NE  . ARG A 1 54  ? 10.67641  15.36625  49.17783  1.000 68.62338 ? 54  ARG A NE  1 
ATOM   433  C  CZ  . ARG A 1 54  ? 9.82007   14.48077  49.67510  1.000 65.85860 ? 54  ARG A CZ  1 
ATOM   434  N  NH1 . ARG A 1 54  ? 8.58431   14.82323  50.00903  1.000 67.66137 ? 54  ARG A NH1 1 
ATOM   435  N  NH2 . ARG A 1 54  ? 10.21365  13.21987  49.84578  1.000 59.11288 ? 54  ARG A NH2 1 
ATOM   436  N  N   . GLU A 1 55  ? 6.74064   19.34778  45.43714  1.000 68.78351 ? 55  GLU A N   1 
ATOM   437  C  CA  . GLU A 1 55  ? 5.32758   19.52805  45.11142  1.000 68.09601 ? 55  GLU A CA  1 
ATOM   438  C  C   . GLU A 1 55  ? 4.96189   18.83685  43.80176  1.000 60.44985 ? 55  GLU A C   1 
ATOM   439  O  O   . GLU A 1 55  ? 3.98716   18.07936  43.73007  1.000 53.60011 ? 55  GLU A O   1 
ATOM   440  C  CB  . GLU A 1 55  ? 5.01492   21.02302  45.01579  1.000 68.33287 ? 55  GLU A CB  1 
ATOM   441  C  CG  . GLU A 1 55  ? 5.74801   21.90296  46.02171  1.000 67.75945 ? 55  GLU A CG  1 
ATOM   442  C  CD  . GLU A 1 55  ? 5.14197   21.85189  47.40771  1.000 83.63907 ? 55  GLU A CD  1 
ATOM   443  O  OE1 . GLU A 1 55  ? 3.89526   21.89016  47.51357  1.000 88.02733 ? 55  GLU A OE1 1 
ATOM   444  O  OE2 . GLU A 1 55  ? 5.90772   21.80097  48.39441  1.000 84.78905 ? 55  GLU A OE2 1 
ATOM   445  N  N   . VAL A 1 56  ? 5.73535   19.09742  42.74810  1.000 62.93074 ? 56  VAL A N   1 
ATOM   446  C  CA  . VAL A 1 56  ? 5.44495   18.50097  41.44714  1.000 60.80217 ? 56  VAL A CA  1 
ATOM   447  C  C   . VAL A 1 56  ? 5.61290   16.99123  41.50000  1.000 53.25724 ? 56  VAL A C   1 
ATOM   448  O  O   . VAL A 1 56  ? 4.71965   16.24300  41.08221  1.000 51.19095 ? 56  VAL A O   1 
ATOM   449  C  CB  . VAL A 1 56  ? 6.32851   19.12228  40.35227  1.000 60.61925 ? 56  VAL A CB  1 
ATOM   450  C  CG1 . VAL A 1 56  ? 5.69099   18.91342  38.98703  1.000 65.75539 ? 56  VAL A CG1 1 
ATOM   451  C  CG2 . VAL A 1 56  ? 6.53079   20.58972  40.61201  1.000 64.96781 ? 56  VAL A CG2 1 
ATOM   452  N  N   . LEU A 1 57  ? 6.76173   16.52137  42.00916  1.000 56.17266 ? 57  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 57  ? 7.02290   15.08233  42.04960  1.000 53.14272 ? 57  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 57  ? 5.96531   14.33740  42.84726  1.000 48.73908 ? 57  LEU A C   1 
ATOM   455  O  O   . LEU A 1 57  ? 5.52073   13.26258  42.43503  1.000 42.09491 ? 57  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 57  ? 8.41050   14.78218  42.61751  1.000 54.59259 ? 57  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 57  ? 9.67882   15.25476  41.91587  1.000 50.32735 ? 57  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 57  ? 9.83124   16.71784  42.03288  1.000 61.36580 ? 57  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 57  ? 10.87770  14.57936  42.54099  1.000 53.46512 ? 57  LEU A CD2 1 
ATOM   460  N  N   . GLU A 1 58  ? 5.55546   14.88204  43.99547  1.000 52.44640 ? 58  GLU A N   1 
ATOM   461  C  CA  . GLU A 1 58  ? 4.46727   14.25909  44.73713  1.000 51.54943 ? 58  GLU A CA  1 
ATOM   462  C  C   . GLU A 1 58  ? 3.22002   14.13722  43.87285  1.000 47.02628 ? 58  GLU A C   1 
ATOM   463  O  O   . GLU A 1 58  ? 2.61585   13.06149  43.78493  1.000 46.32804 ? 58  GLU A O   1 
ATOM   464  C  CB  . GLU A 1 58  ? 4.17696   15.04425  46.01236  1.000 55.78401 ? 58  GLU A CB  1 
ATOM   465  C  CG  . GLU A 1 58  ? 5.32105   15.01303  47.01053  1.000 60.25529 ? 58  GLU A CG  1 
ATOM   466  C  CD  . GLU A 1 58  ? 4.96672   15.69051  48.31528  1.000 66.83095 ? 58  GLU A CD  1 
ATOM   467  O  OE1 . GLU A 1 58  ? 4.29438   15.03084  49.14010  1.000 63.80626 ? 58  GLU A OE1 1 
ATOM   468  O  OE2 . GLU A 1 58  ? 5.36584   16.86055  48.52434  1.000 65.57733 ? 58  GLU A OE2 1 
ATOM   469  N  N   . LYS A 1 59  ? 2.83217   15.22933  43.21024  1.000 47.78998 ? 59  LYS A N   1 
ATOM   470  C  CA  . LYS A 1 59  ? 1.68284   15.19084  42.31095  1.000 49.07436 ? 59  LYS A CA  1 
ATOM   471  C  C   . LYS A 1 59  ? 1.80451   14.06605  41.29181  1.000 46.28348 ? 59  LYS A C   1 
ATOM   472  O  O   . LYS A 1 59  ? 0.88286   13.26050  41.12548  1.000 49.29792 ? 59  LYS A O   1 
ATOM   473  C  CB  . LYS A 1 59  ? 1.52623   16.53957  41.60501  1.000 55.36052 ? 59  LYS A CB  1 
ATOM   474  C  CG  . LYS A 1 59  ? 0.56963   16.53479  40.40939  1.000 52.37870 ? 59  LYS A CG  1 
ATOM   475  C  CD  . LYS A 1 59  ? 1.26588   17.11826  39.16810  1.000 47.05832 ? 59  LYS A CD  1 
ATOM   476  C  CE  . LYS A 1 59  ? 0.38364   17.08028  37.92746  1.000 45.66280 ? 59  LYS A CE  1 
ATOM   477  N  NZ  . LYS A 1 59  ? -0.93378  17.74229  38.12903  1.000 53.85364 ? 59  LYS A NZ  1 
ATOM   478  N  N   A ILE A 1 60  ? 2.93880   13.99322  40.59565  0.855 45.58571 ? 60  ILE A N   1 
ATOM   479  N  N   B ILE A 1 60  ? 2.93895   13.98355  40.59277  0.145 45.72385 ? 60  ILE A N   1 
ATOM   480  C  CA  A ILE A 1 60  ? 3.04493   12.96521  39.57830  0.855 45.16198 ? 60  ILE A CA  1 
ATOM   481  C  CA  B ILE A 1 60  ? 3.05205   12.95123  39.56450  0.145 45.30345 ? 60  ILE A CA  1 
ATOM   482  C  C   A ILE A 1 60  ? 3.29037   11.59807  40.21152  0.855 45.25499 ? 60  ILE A C   1 
ATOM   483  C  C   B ILE A 1 60  ? 3.48820   11.60719  40.12940  0.145 45.23908 ? 60  ILE A C   1 
ATOM   484  O  O   A ILE A 1 60  ? 2.88405   10.57460  39.64839  0.855 43.55386 ? 60  ILE A O   1 
ATOM   485  O  O   B ILE A 1 60  ? 3.43690   10.60502  39.40872  0.145 44.48483 ? 60  ILE A O   1 
ATOM   486  C  CB  A ILE A 1 60  ? 4.11129   13.33571  38.52460  0.855 49.59907 ? 60  ILE A CB  1 
ATOM   487  C  CB  B ILE A 1 60  ? 3.97543   13.42041  38.42108  0.145 49.09319 ? 60  ILE A CB  1 
ATOM   488  C  CG1 A ILE A 1 60  ? 5.49585   13.50891  39.13263  0.855 49.61751 ? 60  ILE A CG1 1 
ATOM   489  C  CG1 B ILE A 1 60  ? 5.42471   13.01409  38.65653  0.145 46.41945 ? 60  ILE A CG1 1 
ATOM   490  C  CG2 A ILE A 1 60  ? 3.75444   14.65852  37.85743  0.855 48.65898 ? 60  ILE A CG2 1 
ATOM   491  C  CG2 B ILE A 1 60  ? 3.88038   14.92650  38.23176  0.145 48.12815 ? 60  ILE A CG2 1 
ATOM   492  C  CD1 A ILE A 1 60  ? 6.40170   14.38984  38.28488  0.855 40.39387 ? 60  ILE A CD1 1 
ATOM   493  C  CD1 B ILE A 1 60  ? 6.00270   12.20383  37.52806  0.145 42.05532 ? 60  ILE A CD1 1 
ATOM   494  N  N   . ALA A 1 61  ? 3.89044   11.54808  41.40505  1.000 46.43348 ? 61  ALA A N   1 
ATOM   495  C  CA  . ALA A 1 61  ? 4.06988   10.25744  42.07899  1.000 43.06738 ? 61  ALA A CA  1 
ATOM   496  C  C   . ALA A 1 61  ? 2.73273   9.59108   42.37048  1.000 47.23284 ? 61  ALA A C   1 
ATOM   497  O  O   . ALA A 1 61  ? 2.64207   8.35634   42.38576  1.000 40.54857 ? 61  ALA A O   1 
ATOM   498  C  CB  . ALA A 1 61  ? 4.84065   10.42426  43.39190  1.000 42.03042 ? 61  ALA A CB  1 
ATOM   499  N  N   . ARG A 1 62  ? 1.68892   10.39370  42.59391  1.000 46.81470 ? 62  ARG A N   1 
ATOM   500  C  CA  . ARG A 1 62  ? 0.34035   9.90983   42.84864  1.000 44.83524 ? 62  ARG A CA  1 
ATOM   501  C  C   . ARG A 1 62  ? -0.50963  9.73914   41.59640  1.000 49.36970 ? 62  ARG A C   1 
ATOM   502  O  O   . ARG A 1 62  ? -1.57171  9.11566   41.68221  1.000 59.10419 ? 62  ARG A O   1 
ATOM   503  C  CB  . ARG A 1 62  ? -0.38374  10.86785  43.78691  1.000 46.17852 ? 62  ARG A CB  1 
ATOM   504  C  CG  . ARG A 1 62  ? 0.20535   10.93224  45.17906  1.000 51.39391 ? 62  ARG A CG  1 
ATOM   505  C  CD  . ARG A 1 62  ? -0.27629  12.16796  45.91662  1.000 51.99125 ? 62  ARG A CD  1 
ATOM   506  N  NE  . ARG A 1 62  ? -0.59686  11.87999  47.30696  1.000 64.60720 ? 62  ARG A NE  1 
ATOM   507  C  CZ  . ARG A 1 62  ? 0.29864   11.59014  48.24283  1.000 61.15525 ? 62  ARG A CZ  1 
ATOM   508  N  NH1 . ARG A 1 62  ? 1.58318   11.43701  47.94745  1.000 54.07927 ? 62  ARG A NH1 1 
ATOM   509  N  NH2 . ARG A 1 62  ? -0.10272  11.46268  49.51009  1.000 60.00626 ? 62  ARG A NH2 1 
ATOM   510  N  N   . ASP A 1 63  ? -0.09778  10.28610  40.45365  1.000 48.76121 ? 63  ASP A N   1 
ATOM   511  C  CA  . ASP A 1 63  ? -0.86730  10.19932  39.21077  1.000 46.08656 ? 63  ASP A CA  1 
ATOM   512  C  C   . ASP A 1 63  ? -0.11460  9.25838   38.27581  1.000 43.09198 ? 63  ASP A C   1 
ATOM   513  O  O   . ASP A 1 63  ? 0.77155   9.67501   37.53278  1.000 45.37012 ? 63  ASP A O   1 
ATOM   514  C  CB  . ASP A 1 63  ? -1.07415  11.58670  38.57221  1.000 51.03272 ? 63  ASP A CB  1 
ATOM   515  C  CG  . ASP A 1 63  ? -1.42966  11.51278  37.06658  1.000 54.29496 ? 63  ASP A CG  1 
ATOM   516  O  OD1 . ASP A 1 63  ? -2.13046  10.55807  36.64180  1.000 44.81000 ? 63  ASP A OD1 1 
ATOM   517  O  OD2 . ASP A 1 63  ? -0.98951  12.40714  36.30364  1.000 45.77592 ? 63  ASP A OD2 1 
ATOM   518  N  N   . ASP A 1 64  ? -0.46845  7.97858   38.32149  1.000 39.08636 ? 64  ASP A N   1 
ATOM   519  C  CA  . ASP A 1 64  ? 0.17240   6.97640   37.49035  1.000 42.19393 ? 64  ASP A CA  1 
ATOM   520  C  C   . ASP A 1 64  ? -0.52601  6.81168   36.15198  1.000 44.92101 ? 64  ASP A C   1 
ATOM   521  O  O   . ASP A 1 64  ? -0.33908  5.78690   35.47954  1.000 47.33560 ? 64  ASP A O   1 
ATOM   522  C  CB  . ASP A 1 64  ? 0.23296   5.63463   38.22763  1.000 38.47260 ? 64  ASP A CB  1 
ATOM   523  C  CG  . ASP A 1 64  ? -1.12575  5.01844   38.44564  1.000 43.97677 ? 64  ASP A CG  1 
ATOM   524  O  OD1 . ASP A 1 64  ? -2.15200  5.68667   38.18708  1.000 52.98581 ? 64  ASP A OD1 1 
ATOM   525  O  OD2 . ASP A 1 64  ? -1.16831  3.85726   38.91167  1.000 46.12985 ? 64  ASP A OD2 1 
ATOM   526  N  N   . GLY A 1 65  ? -1.33456  7.78882   35.75682  1.000 43.68707 ? 65  GLY A N   1 
ATOM   527  C  CA  . GLY A 1 65  ? -2.09310  7.66323   34.53623  1.000 42.91190 ? 65  GLY A CA  1 
ATOM   528  C  C   . GLY A 1 65  ? -1.65614  8.60004   33.43203  1.000 46.18289 ? 65  GLY A C   1 
ATOM   529  O  O   . GLY A 1 65  ? -2.28772  8.62609   32.37270  1.000 53.35668 ? 65  GLY A O   1 
ATOM   530  N  N   . THR A 1 66  ? -0.59807  9.38094   33.64925  1.000 45.44221 ? 66  THR A N   1 
ATOM   531  C  CA  . THR A 1 66  ? -0.13165  10.30565  32.62560  1.000 43.01858 ? 66  THR A CA  1 
ATOM   532  C  C   . THR A 1 66  ? 1.38849   10.36619  32.63675  1.000 38.52766 ? 66  THR A C   1 
ATOM   533  O  O   . THR A 1 66  ? 2.02527   10.16684  33.67210  1.000 38.85563 ? 66  THR A O   1 
ATOM   534  C  CB  . THR A 1 66  ? -0.71551  11.72038  32.82344  1.000 45.91263 ? 66  THR A CB  1 
ATOM   535  O  OG1 . THR A 1 66  ? -2.05435  11.62508  33.32580  1.000 40.92557 ? 66  THR A OG1 1 
ATOM   536  C  CG2 . THR A 1 66  ? -0.74565  12.46462  31.50530  1.000 40.86296 ? 66  THR A CG2 1 
ATOM   537  N  N   A VAL A 1 67  ? 1.97744   10.62305  31.48735  0.050 37.90452 ? 67  VAL A N   1 
ATOM   538  N  N   B VAL A 1 67  ? 1.95232   10.63491  31.44281  0.950 37.78003 ? 67  VAL A N   1 
ATOM   539  C  CA  A VAL A 1 67  ? 3.41862   10.81869  31.42237  0.050 38.36336 ? 67  VAL A CA  1 
ATOM   540  C  CA  B VAL A 1 67  ? 3.37112   10.90610  31.22893  0.950 38.36569 ? 67  VAL A CA  1 
ATOM   541  C  C   A VAL A 1 67  ? 3.69752   12.31148  31.35282  0.050 38.36322 ? 67  VAL A C   1 
ATOM   542  C  C   B VAL A 1 67  ? 3.61311   12.39360  31.42694  0.950 38.43630 ? 67  VAL A C   1 
ATOM   543  O  O   A VAL A 1 67  ? 2.96975   13.07190  30.70216  0.050 38.79608 ? 67  VAL A O   1 
ATOM   544  O  O   B VAL A 1 67  ? 2.80665   13.23355  30.99727  0.950 37.97870 ? 67  VAL A O   1 
ATOM   545  C  CB  A VAL A 1 67  ? 4.04922   10.05854  30.24046  0.050 35.58795 ? 67  VAL A CB  1 
ATOM   546  C  CB  B VAL A 1 67  ? 3.81785   10.46434  29.81528  0.950 32.77044 ? 67  VAL A CB  1 
ATOM   547  C  CG1 A VAL A 1 67  ? 3.44456   10.50289  28.96284  0.050 35.82175 ? 67  VAL A CG1 1 
ATOM   548  C  CG1 B VAL A 1 67  ? 5.22366   10.95860  29.50386  0.950 32.01167 ? 67  VAL A CG1 1 
ATOM   549  C  CG2 A VAL A 1 67  ? 5.55336   10.27233  30.20783  0.050 34.41356 ? 67  VAL A CG2 1 
ATOM   550  C  CG2 B VAL A 1 67  ? 3.78679   8.95856   29.67469  0.950 34.39018 ? 67  VAL A CG2 1 
ATOM   551  N  N   . TYR A 1 68  ? 4.73353   12.73209  32.06146  1.000 37.01620 ? 68  TYR A N   1 
ATOM   552  C  CA  . TYR A 1 68  ? 5.12780   14.12029  32.20257  1.000 40.40565 ? 68  TYR A CA  1 
ATOM   553  C  C   . TYR A 1 68  ? 6.48855   14.31303  31.55123  1.000 36.47500 ? 68  TYR A C   1 
ATOM   554  O  O   . TYR A 1 68  ? 7.23665   13.35588  31.34610  1.000 38.39107 ? 68  TYR A O   1 
ATOM   555  C  CB  . TYR A 1 68  ? 5.16437   14.51786  33.68395  1.000 38.15761 ? 68  TYR A CB  1 
ATOM   556  C  CG  . TYR A 1 68  ? 3.80040   14.48546  34.34213  1.000 41.77772 ? 68  TYR A CG  1 
ATOM   557  C  CD1 . TYR A 1 68  ? 3.23406   13.28290  34.76194  1.000 46.06531 ? 68  TYR A CD1 1 
ATOM   558  C  CD2 . TYR A 1 68  ? 3.08006   15.65435  34.54993  1.000 37.14330 ? 68  TYR A CD2 1 
ATOM   559  C  CE1 . TYR A 1 68  ? 1.97361   13.24518  35.37025  1.000 41.21759 ? 68  TYR A CE1 1 
ATOM   560  C  CE2 . TYR A 1 68  ? 1.82337   15.62528  35.15411  1.000 45.64480 ? 68  TYR A CE2 1 
ATOM   561  C  CZ  . TYR A 1 68  ? 1.28111   14.41509  35.55490  1.000 41.62754 ? 68  TYR A CZ  1 
ATOM   562  O  OH  . TYR A 1 68  ? 0.04153   14.38236  36.14528  1.000 52.01474 ? 68  TYR A OH  1 
ATOM   563  N  N   . PHE A 1 69  ? 6.81473   15.55889  31.21977  1.000 35.71259 ? 69  PHE A N   1 
ATOM   564  C  CA  . PHE A 1 69  ? 8.13774   15.81009  30.67166  1.000 43.31523 ? 69  PHE A CA  1 
ATOM   565  C  C   . PHE A 1 69  ? 8.60005   17.21111  31.03977  1.000 48.07813 ? 69  PHE A C   1 
ATOM   566  O  O   . PHE A 1 69  ? 7.79449   18.11073  31.28194  1.000 46.16935 ? 69  PHE A O   1 
ATOM   567  C  CB  . PHE A 1 69  ? 8.17589   15.59910  29.14809  1.000 44.71296 ? 69  PHE A CB  1 
ATOM   568  C  CG  . PHE A 1 69  ? 7.33770   16.56979  28.35737  1.000 44.00096 ? 69  PHE A CG  1 
ATOM   569  C  CD1 . PHE A 1 69  ? 7.86230   17.79061  27.95301  1.000 46.90815 ? 69  PHE A CD1 1 
ATOM   570  C  CD2 . PHE A 1 69  ? 6.05308   16.23358  27.96729  1.000 39.50719 ? 69  PHE A CD2 1 
ATOM   571  C  CE1 . PHE A 1 69  ? 7.10886   18.68131  27.20236  1.000 47.81381 ? 69  PHE A CE1 1 
ATOM   572  C  CE2 . PHE A 1 69  ? 5.29179   17.11110  27.22112  1.000 42.39495 ? 69  PHE A CE2 1 
ATOM   573  C  CZ  . PHE A 1 69  ? 5.82014   18.34480  26.83550  1.000 48.08803 ? 69  PHE A CZ  1 
ATOM   574  N  N   . VAL A 1 70  ? 9.92125   17.37838  31.06271  1.000 50.32370 ? 70  VAL A N   1 
ATOM   575  C  CA  . VAL A 1 70  ? 10.57963  18.60867  31.48256  1.000 53.91714 ? 70  VAL A CA  1 
ATOM   576  C  C   . VAL A 1 70  ? 11.23339  19.22312  30.25126  1.000 57.05944 ? 70  VAL A C   1 
ATOM   577  O  O   . VAL A 1 70  ? 12.22503  18.69789  29.73117  1.000 58.08237 ? 70  VAL A O   1 
ATOM   578  C  CB  . VAL A 1 70  ? 11.61039  18.34149  32.58753  1.000 60.51456 ? 70  VAL A CB  1 
ATOM   579  C  CG1 . VAL A 1 70  ? 12.03442  19.64250  33.25624  1.000 53.99950 ? 70  VAL A CG1 1 
ATOM   580  C  CG2 . VAL A 1 70  ? 11.05259  17.34864  33.60209  1.000 49.51799 ? 70  VAL A CG2 1 
ATOM   581  N  N   . SER A 1 71  ? 10.68492  20.33844  29.78232  1.000 57.83187 ? 71  SER A N   1 
ATOM   582  C  CA  . SER A 1 71  ? 11.10052  20.92430  28.51778  1.000 62.68221 ? 71  SER A CA  1 
ATOM   583  C  C   . SER A 1 71  ? 11.21196  22.42775  28.68592  1.000 68.76913 ? 71  SER A C   1 
ATOM   584  O  O   . SER A 1 71  ? 10.24833  23.08113  29.09622  1.000 68.01596 ? 71  SER A O   1 
ATOM   585  C  CB  . SER A 1 71  ? 10.10822  20.59074  27.40149  1.000 56.26391 ? 71  SER A CB  1 
ATOM   586  O  OG  . SER A 1 71  ? 10.03369  21.64598  26.46039  1.000 63.05678 ? 71  SER A OG  1 
ATOM   587  N  N   . ASN A 1 72  ? 12.37678  22.96917  28.34232  1.000 69.34881 ? 72  ASN A N   1 
ATOM   588  C  CA  . ASN A 1 72  ? 12.69006  24.35166  28.66395  1.000 71.85296 ? 72  ASN A CA  1 
ATOM   589  C  C   . ASN A 1 72  ? 12.48488  24.55909  30.15675  1.000 71.83568 ? 72  ASN A C   1 
ATOM   590  O  O   . ASN A 1 72  ? 12.86430  23.70278  30.96170  1.000 70.89070 ? 72  ASN A O   1 
ATOM   591  C  CB  . ASN A 1 72  ? 11.84961  25.31978  27.82770  1.000 76.59909 ? 72  ASN A CB  1 
ATOM   592  C  CG  . ASN A 1 72  ? 12.07981  25.14464  26.33309  1.000 81.75162 ? 72  ASN A CG  1 
ATOM   593  O  OD1 . ASN A 1 72  ? 13.01014  24.44957  25.91951  1.000 80.59122 ? 72  ASN A OD1 1 
ATOM   594  N  ND2 . ASN A 1 72  ? 11.24324  25.78584  25.51659  1.000 73.70941 ? 72  ASN A ND2 1 
ATOM   595  N  N   . GLY A 1 73  ? 11.86040  25.66630  30.53837  1.000 71.82180 ? 73  GLY A N   1 
ATOM   596  C  CA  . GLY A 1 73  ? 11.84556  26.03462  31.94152  1.000 78.41215 ? 73  GLY A CA  1 
ATOM   597  C  C   . GLY A 1 73  ? 11.14689  25.03990  32.85059  1.000 78.85637 ? 73  GLY A C   1 
ATOM   598  O  O   . GLY A 1 73  ? 11.53384  24.88194  34.01055  1.000 82.26028 ? 73  GLY A O   1 
ATOM   599  N  N   . GLY A 1 74  ? 10.11418  24.35336  32.35295  1.000 69.04607 ? 74  GLY A N   1 
ATOM   600  C  CA  . GLY A 1 74  ? 9.11552   23.79700  33.23824  1.000 56.73958 ? 74  GLY A CA  1 
ATOM   601  C  C   . GLY A 1 74  ? 8.69424   22.38712  32.88145  1.000 66.01959 ? 74  GLY A C   1 
ATOM   602  O  O   . GLY A 1 74  ? 9.04867   21.83276  31.83756  1.000 68.22399 ? 74  GLY A O   1 
ATOM   603  N  N   . VAL A 1 75  ? 7.93080   21.82610  33.78614  1.000 61.59221 ? 75  VAL A N   1 
ATOM   604  C  CA  . VAL A 1 75  ? 7.37364   20.48886  33.67130  1.000 59.78496 ? 75  VAL A CA  1 
ATOM   605  C  C   . VAL A 1 75  ? 6.04125   20.58689  32.95384  1.000 57.04476 ? 75  VAL A C   1 
ATOM   606  O  O   . VAL A 1 75  ? 5.31366   21.58279  33.06359  1.000 57.96391 ? 75  VAL A O   1 
ATOM   607  C  CB  . VAL A 1 75  ? 7.23034   19.84000  35.06190  1.000 57.28525 ? 75  VAL A CB  1 
ATOM   608  C  CG1 . VAL A 1 75  ? 8.54516   19.92095  35.79002  1.000 58.49123 ? 75  VAL A CG1 1 
ATOM   609  C  CG2 . VAL A 1 75  ? 6.16805   20.55738  35.86237  1.000 64.00004 ? 75  VAL A CG2 1 
ATOM   610  N  N   . TYR A 1 76  ? 5.71841   19.54196  32.20496  1.000 47.84883 ? 76  TYR A N   1 
ATOM   611  C  CA  . TYR A 1 76  ? 4.54149   19.56012  31.36163  1.000 50.40950 ? 76  TYR A CA  1 
ATOM   612  C  C   . TYR A 1 76  ? 3.90935   18.18240  31.35495  1.000 43.63436 ? 76  TYR A C   1 
ATOM   613  O  O   . TYR A 1 76  ? 4.53828   17.17366  31.67712  1.000 42.52381 ? 76  TYR A O   1 
ATOM   614  C  CB  . TYR A 1 76  ? 4.88581   20.01268  29.93795  1.000 50.93528 ? 76  TYR A CB  1 
ATOM   615  C  CG  . TYR A 1 76  ? 5.26042   21.46956  29.87431  1.000 55.80026 ? 76  TYR A CG  1 
ATOM   616  C  CD1 . TYR A 1 76  ? 4.28274   22.45949  29.93477  1.000 58.80303 ? 76  TYR A CD1 1 
ATOM   617  C  CD2 . TYR A 1 76  ? 6.58777   21.86244  29.76057  1.000 56.12708 ? 76  TYR A CD2 1 
ATOM   618  C  CE1 . TYR A 1 76  ? 4.61344   23.80802  29.87751  1.000 56.43585 ? 76  TYR A CE1 1 
ATOM   619  C  CE2 . TYR A 1 76  ? 6.92989   23.20665  29.70784  1.000 62.30423 ? 76  TYR A CE2 1 
ATOM   620  C  CZ  . TYR A 1 76  ? 5.93563   24.17830  29.76595  1.000 59.73973 ? 76  TYR A CZ  1 
ATOM   621  O  OH  . TYR A 1 76  ? 6.26591   25.51731  29.71373  1.000 62.04688 ? 76  TYR A OH  1 
ATOM   622  N  N   . LYS A 1 77  ? 2.64073   18.16139  30.99187  1.000 49.67568 ? 77  LYS A N   1 
ATOM   623  C  CA  . LYS A 1 77  ? 1.83264   16.95676  31.00643  1.000 46.25684 ? 77  LYS A CA  1 
ATOM   624  C  C   . LYS A 1 77  ? 1.60295   16.55499  29.56100  1.000 48.43739 ? 77  LYS A C   1 
ATOM   625  O  O   . LYS A 1 77  ? 1.15742   17.37638  28.75390  1.000 45.72636 ? 77  LYS A O   1 
ATOM   626  C  CB  . LYS A 1 77  ? 0.51763   17.23108  31.73744  1.000 49.32154 ? 77  LYS A CB  1 
ATOM   627  C  CG  . LYS A 1 77  ? -0.50419  16.12333  31.75503  1.000 49.96844 ? 77  LYS A CG  1 
ATOM   628  C  CD  . LYS A 1 77  ? -1.20956  16.14270  33.09356  1.000 46.98559 ? 77  LYS A CD  1 
ATOM   629  C  CE  . LYS A 1 77  ? -2.67234  16.51087  32.93818  1.000 56.77057 ? 77  LYS A CE  1 
ATOM   630  N  NZ  . LYS A 1 77  ? -3.52724  15.76398  33.90204  1.000 60.52909 ? 77  LYS A NZ  1 
ATOM   631  N  N   . ALA A 1 78  ? 1.95715   15.31607  29.22344  1.000 46.41499 ? 78  ALA A N   1 
ATOM   632  C  CA  . ALA A 1 78  ? 1.83342   14.82721  27.85061  1.000 43.56066 ? 78  ALA A CA  1 
ATOM   633  C  C   . ALA A 1 78  ? 0.36101   14.54001  27.59755  1.000 45.59552 ? 78  ALA A C   1 
ATOM   634  O  O   . ALA A 1 78  ? -0.10902  13.39819  27.63380  1.000 46.17283 ? 78  ALA A O   1 
ATOM   635  C  CB  . ALA A 1 78  ? 2.69317   13.58944  27.62131  1.000 39.62207 ? 78  ALA A CB  1 
ATOM   636  N  N   . ALA A 1 79  ? -0.38411  15.60968  27.36456  1.000 45.88017 ? 79  ALA A N   1 
ATOM   637  C  CA  . ALA A 1 79  ? -1.79405  15.48670  27.05017  1.000 50.50439 ? 79  ALA A CA  1 
ATOM   638  C  C   . ALA A 1 79  ? -2.16549  16.62662  26.12326  1.000 55.13207 ? 79  ALA A C   1 
ATOM   639  O  O   . ALA A 1 79  ? -1.39608  17.57226  25.93702  1.000 56.38180 ? 79  ALA A O   1 
ATOM   640  C  CB  . ALA A 1 79  ? -2.65340  15.49035  28.31223  1.000 50.67667 ? 79  ALA A CB  1 
ATOM   641  N  N   . ILE A 1 80  ? -3.34516  16.50844  25.51530  1.000 59.53201 ? 80  ILE A N   1 
ATOM   642  C  CA  . ILE A 1 80  ? -3.89038  17.53570  24.62952  1.000 59.19796 ? 80  ILE A CA  1 
ATOM   643  C  C   . ILE A 1 80  ? -5.40283  17.54547  24.77976  1.000 64.71746 ? 80  ILE A C   1 
ATOM   644  O  O   . ILE A 1 80  ? -6.04863  16.49638  24.69751  1.000 65.60196 ? 80  ILE A O   1 
ATOM   645  C  CB  . ILE A 1 80  ? -3.52914  17.30771  23.14711  1.000 60.45520 ? 80  ILE A CB  1 
ATOM   646  C  CG1 . ILE A 1 80  ? -2.02191  17.18904  22.93560  1.000 55.24932 ? 80  ILE A CG1 1 
ATOM   647  C  CG2 . ILE A 1 80  ? -4.09046  18.42323  22.28239  1.000 58.12582 ? 80  ILE A CG2 1 
ATOM   648  C  CD1 . ILE A 1 80  ? -1.63833  17.15627  21.47136  1.000 48.36177 ? 80  ILE A CD1 1 
ATOM   649  N  N   . ALA A 1 81  ? -5.96964  18.73025  24.99705  1.000 74.54539 ? 81  ALA A N   1 
ATOM   650  C  CA  . ALA A 1 81  ? -7.40878  18.92250  24.90568  1.000 69.73282 ? 81  ALA A CA  1 
ATOM   651  C  C   . ALA A 1 81  ? -7.74641  19.39545  23.49827  1.000 74.57318 ? 81  ALA A C   1 
ATOM   652  O  O   . ALA A 1 81  ? -7.14131  20.34922  22.99699  1.000 75.82375 ? 81  ALA A O   1 
ATOM   653  C  CB  . ALA A 1 81  ? -7.89029  19.93578  25.94226  1.000 74.43774 ? 81  ALA A CB  1 
ATOM   654  N  N   . GLY A 1 82  ? -8.69695  18.72315  22.85494  1.000 79.33546 ? 82  GLY A N   1 
ATOM   655  C  CA  . GLY A 1 82  ? -9.04917  19.11771  21.50508  1.000 86.18682 ? 82  GLY A CA  1 
ATOM   656  C  C   . GLY A 1 82  ? -10.39668 18.64868  20.99630  1.000 84.69090 ? 82  GLY A C   1 
ATOM   657  O  O   . GLY A 1 82  ? -10.78402 17.49199  21.20337  1.000 82.75799 ? 82  GLY A O   1 
ATOM   658  N  N   . GLU A 1 83  ? -11.11578 19.55379  20.32585  1.000 80.98240 ? 83  GLU A N   1 
ATOM   659  C  CA  . GLU A 1 83  ? -12.33330 19.21573  19.59642  1.000 79.30707 ? 83  GLU A CA  1 
ATOM   660  C  C   . GLU A 1 83  ? -13.38758 18.72958  20.59559  1.000 82.01104 ? 83  GLU A C   1 
ATOM   661  O  O   . GLU A 1 83  ? -14.02630 19.55074  21.25747  1.000 83.99659 ? 83  GLU A O   1 
ATOM   662  C  CB  . GLU A 1 83  ? -11.95982 18.23321  18.45828  1.000 78.10582 ? 83  GLU A CB  1 
ATOM   663  C  CG  . GLU A 1 83  ? -12.88680 17.08052  18.04103  1.000 82.72539 ? 83  GLU A CG  1 
ATOM   664  C  CD  . GLU A 1 83  ? -13.90217 17.45743  16.97172  1.000 88.43417 ? 83  GLU A CD  1 
ATOM   665  O  OE1 . GLU A 1 83  ? -13.99912 18.65526  16.60731  1.000 90.02777 ? 83  GLU A OE1 1 
ATOM   666  O  OE2 . GLU A 1 83  ? -14.59039 16.53501  16.47969  1.000 81.80976 ? 83  GLU A OE2 1 
ATOM   667  N  N   . SER A 1 84  ? -13.56092 17.42268  20.75436  1.000 89.10762 ? 84  SER A N   1 
ATOM   668  C  CA  . SER A 1 84  ? -14.43942 16.87171  21.76958  1.000 87.92952 ? 84  SER A CA  1 
ATOM   669  C  C   . SER A 1 84  ? -13.74806 15.82352  22.61820  1.000 93.03563 ? 84  SER A C   1 
ATOM   670  O  O   . SER A 1 84  ? -14.34114 15.35841  23.59977  1.000 92.11341 ? 84  SER A O   1 
ATOM   671  C  CB  . SER A 1 84  ? -15.69807 16.25752  21.13473  1.000 93.56576 ? 84  SER A CB  1 
ATOM   672  O  OG  . SER A 1 84  ? -16.26301 17.12104  20.16106  1.000 94.88720 ? 84  SER A OG  1 
ATOM   673  N  N   . GLY A 1 85  ? -12.51757 15.44714  22.28166  1.000 81.51893 ? 85  GLY A N   1 
ATOM   674  C  CA  . GLY A 1 85  ? -11.78324 14.48122  23.06623  1.000 86.07097 ? 85  GLY A CA  1 
ATOM   675  C  C   . GLY A 1 85  ? -10.66663 15.09557  23.88463  1.000 81.82616 ? 85  GLY A C   1 
ATOM   676  O  O   . GLY A 1 85  ? -10.22792 16.22243  23.61951  1.000 75.71964 ? 85  GLY A O   1 
ATOM   677  N  N   . PHE A 1 86  ? -10.21438 14.35698  24.89767  1.000 76.99775 ? 86  PHE A N   1 
ATOM   678  C  CA  . PHE A 1 86  ? -9.03527  14.70220  25.68408  1.000 72.19946 ? 86  PHE A CA  1 
ATOM   679  C  C   . PHE A 1 86  ? -8.06266  13.53471  25.60927  1.000 70.39664 ? 86  PHE A C   1 
ATOM   680  O  O   . PHE A 1 86  ? -8.32655  12.46041  26.16213  1.000 68.66649 ? 86  PHE A O   1 
ATOM   681  C  CB  . PHE A 1 86  ? -9.39895  15.02152  27.12997  1.000 74.74209 ? 86  PHE A CB  1 
ATOM   682  C  CG  . PHE A 1 86  ? -8.24399  15.53448  27.94024  1.000 77.73524 ? 86  PHE A CG  1 
ATOM   683  C  CD1 . PHE A 1 86  ? -7.87212  16.87116  27.88185  1.000 81.91898 ? 86  PHE A CD1 1 
ATOM   684  C  CD2 . PHE A 1 86  ? -7.53955  14.68382  28.77453  1.000 75.05003 ? 86  PHE A CD2 1 
ATOM   685  C  CE1 . PHE A 1 86  ? -6.80682  17.34574  28.63106  1.000 77.11109 ? 86  PHE A CE1 1 
ATOM   686  C  CE2 . PHE A 1 86  ? -6.47844  15.15115  29.52932  1.000 78.92288 ? 86  PHE A CE2 1 
ATOM   687  C  CZ  . PHE A 1 86  ? -6.11028  16.48459  29.45566  1.000 79.35720 ? 86  PHE A CZ  1 
ATOM   688  N  N   . TYR A 1 87  ? -6.94118  13.75402  24.93539  1.000 64.34126 ? 87  TYR A N   1 
ATOM   689  C  CA  . TYR A 1 87  ? -5.94257  12.72961  24.67542  1.000 57.65147 ? 87  TYR A CA  1 
ATOM   690  C  C   . TYR A 1 87  ? -4.78382  12.85723  25.65602  1.000 55.64686 ? 87  TYR A C   1 
ATOM   691  O  O   . TYR A 1 87  ? -4.43668  13.95526  26.09804  1.000 59.80930 ? 87  TYR A O   1 
ATOM   692  C  CB  . TYR A 1 87  ? -5.42121  12.82889  23.24064  1.000 50.73513 ? 87  TYR A CB  1 
ATOM   693  C  CG  . TYR A 1 87  ? -6.49829  13.01060  22.19818  1.000 53.39598 ? 87  TYR A CG  1 
ATOM   694  C  CD1 . TYR A 1 87  ? -7.23269  14.18798  22.12041  1.000 56.03797 ? 87  TYR A CD1 1 
ATOM   695  C  CD2 . TYR A 1 87  ? -6.77189  12.00460  21.27909  1.000 48.72804 ? 87  TYR A CD2 1 
ATOM   696  C  CE1 . TYR A 1 87  ? -8.21258  14.34600  21.18317  1.000 55.85919 ? 87  TYR A CE1 1 
ATOM   697  C  CE2 . TYR A 1 87  ? -7.75234  12.15587  20.33120  1.000 49.22769 ? 87  TYR A CE2 1 
ATOM   698  C  CZ  . TYR A 1 87  ? -8.47053  13.33485  20.28205  1.000 52.00525 ? 87  TYR A CZ  1 
ATOM   699  O  OH  . TYR A 1 87  ? -9.45398  13.51193  19.33674  1.000 55.68589 ? 87  TYR A OH  1 
ATOM   700  N  N   . LYS A 1 88  ? -4.19289  11.71869  26.00212  1.000 44.16941 ? 88  LYS A N   1 
ATOM   701  C  CA  . LYS A 1 88  ? -3.03595  11.72669  26.87985  1.000 45.42852 ? 88  LYS A CA  1 
ATOM   702  C  C   . LYS A 1 88  ? -2.21141  10.48079  26.62243  1.000 42.05015 ? 88  LYS A C   1 
ATOM   703  O  O   . LYS A 1 88  ? -2.74168  9.42574   26.26047  1.000 40.08968 ? 88  LYS A O   1 
ATOM   704  C  CB  . LYS A 1 88  ? -3.42983  11.80160  28.35824  1.000 43.27146 ? 88  LYS A CB  1 
ATOM   705  C  CG  . LYS A 1 88  ? -4.31679  10.66453  28.84294  1.000 47.49394 ? 88  LYS A CG  1 
ATOM   706  C  CD  . LYS A 1 88  ? -4.67038  10.83027  30.32616  1.000 49.92296 ? 88  LYS A CD  1 
ATOM   707  C  CE  . LYS A 1 88  ? -5.14329  9.51219   30.93738  1.000 56.90973 ? 88  LYS A CE  1 
ATOM   708  N  NZ  . LYS A 1 88  ? -4.44539  9.13263   32.20537  1.000 49.01265 ? 88  LYS A NZ  1 
ATOM   709  N  N   . LEU A 1 89  ? -0.90511  10.62608  26.80365  1.000 34.26350 ? 89  LEU A N   1 
ATOM   710  C  CA  . LEU A 1 89  ? 0.01534   9.50248   26.76413  1.000 30.71007 ? 89  LEU A CA  1 
ATOM   711  C  C   . LEU A 1 89  ? 0.05901   8.87720   28.15415  1.000 39.19760 ? 89  LEU A C   1 
ATOM   712  O  O   . LEU A 1 89  ? 0.17476   9.58841   29.16018  1.000 40.64234 ? 89  LEU A O   1 
ATOM   713  C  CB  . LEU A 1 89  ? 1.39051   9.98593   26.31753  1.000 35.50791 ? 89  LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 89  ? 2.45883   8.99837   25.87414  1.000 38.77883 ? 89  LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 89  ? 1.94469   8.21236   24.67879  1.000 35.23617 ? 89  LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 89  ? 3.72229   9.75529   25.50283  1.000 35.78361 ? 89  LEU A CD2 1 
ATOM   717  N  N   . VAL A 1 90  ? -0.07328  7.56162   28.20880  1.000 35.52294 ? 90  VAL A N   1 
ATOM   718  C  CA  . VAL A 1 90  ? -0.26552  6.81477   29.44924  1.000 31.85460 ? 90  VAL A CA  1 
ATOM   719  C  C   . VAL A 1 90  ? 1.03134   6.07621   29.75218  1.000 34.84147 ? 90  VAL A C   1 
ATOM   720  O  O   . VAL A 1 90  ? 1.58135   5.42501   28.85774  1.000 31.80389 ? 90  VAL A O   1 
ATOM   721  C  CB  . VAL A 1 90  ? -1.44603  5.82819   29.33798  1.000 35.03619 ? 90  VAL A CB  1 
ATOM   722  C  CG1 . VAL A 1 90  ? -1.55995  4.92593   30.58244  1.000 36.91236 ? 90  VAL A CG1 1 
ATOM   723  C  CG2 . VAL A 1 90  ? -2.73196  6.57355   29.09745  1.000 40.39264 ? 90  VAL A CG2 1 
ATOM   724  N  N   . PRO A 1 91  ? 1.54676   6.14806   30.96558  1.000 38.51005 ? 91  PRO A N   1 
ATOM   725  C  CA  . PRO A 1 91  ? 2.88122   5.62187   31.28163  1.000 31.46353 ? 91  PRO A CA  1 
ATOM   726  C  C   . PRO A 1 91  ? 2.94865   4.10272   31.42437  1.000 36.12296 ? 91  PRO A C   1 
ATOM   727  O  O   . PRO A 1 91  ? 3.48615   3.57088   32.40325  1.000 33.48700 ? 91  PRO A O   1 
ATOM   728  C  CB  . PRO A 1 91  ? 3.21369   6.32202   32.60243  1.000 37.92542 ? 91  PRO A CB  1 
ATOM   729  C  CG  . PRO A 1 91  ? 1.89316   6.52748   33.23366  1.000 36.55998 ? 91  PRO A CG  1 
ATOM   730  C  CD  . PRO A 1 91  ? 0.95478   6.85880   32.10688  1.000 31.90718 ? 91  PRO A CD  1 
ATOM   731  N  N   . THR A 1 92  ? 2.40241   3.39710   30.44318  1.000 32.93826 ? 92  THR A N   1 
ATOM   732  C  CA  . THR A 1 92  ? 2.70624   1.98787   30.31780  1.000 31.41091 ? 92  THR A CA  1 
ATOM   733  C  C   . THR A 1 92  ? 4.08339   1.83919   29.67906  1.000 30.87512 ? 92  THR A C   1 
ATOM   734  O  O   . THR A 1 92  ? 4.69646   2.81647   29.24412  1.000 28.92354 ? 92  THR A O   1 
ATOM   735  C  CB  . THR A 1 92  ? 1.62253   1.28677   29.50114  1.000 33.62557 ? 92  THR A CB  1 
ATOM   736  O  OG1 . THR A 1 92  ? 1.34962   2.04701   28.31795  1.000 29.43435 ? 92  THR A OG1 1 
ATOM   737  C  CG2 . THR A 1 92  ? 0.33806   1.20102   30.32435  1.000 33.63298 ? 92  THR A CG2 1 
ATOM   738  N  N   . ILE A 1 93  ? 4.58902   0.61339   29.64586  1.000 31.92267 ? 93  ILE A N   1 
ATOM   739  C  CA  . ILE A 1 93  ? 5.83427   0.31672   28.94749  1.000 38.24983 ? 93  ILE A CA  1 
ATOM   740  C  C   . ILE A 1 93  ? 5.51293   -0.63493  27.79344  1.000 36.25452 ? 93  ILE A C   1 
ATOM   741  O  O   . ILE A 1 93  ? 5.24255   -1.82223  28.02558  1.000 40.37366 ? 93  ILE A O   1 
ATOM   742  C  CB  . ILE A 1 93  ? 6.88902   -0.28062  29.88707  1.000 37.82618 ? 93  ILE A CB  1 
ATOM   743  C  CG1 . ILE A 1 93  ? 7.06222   0.60149   31.11610  1.000 35.62349 ? 93  ILE A CG1 1 
ATOM   744  C  CG2 . ILE A 1 93  ? 8.23617   -0.37892  29.17216  1.000 37.88083 ? 93  ILE A CG2 1 
ATOM   745  C  CD1 . ILE A 1 93  ? 8.17117   0.12746   32.04136  1.000 49.55678 ? 93  ILE A CD1 1 
ATOM   746  N  N   . PRO A 1 94  ? 5.51011   -0.16789  26.53632  1.000 39.04687 ? 94  PRO A N   1 
ATOM   747  C  CA  . PRO A 1 94  ? 5.72465   1.22021   26.12887  1.000 30.42188 ? 94  PRO A CA  1 
ATOM   748  C  C   . PRO A 1 94  ? 4.47440   2.04408   26.34545  1.000 30.16144 ? 94  PRO A C   1 
ATOM   749  O  O   . PRO A 1 94  ? 3.44295   1.46652   26.65404  1.000 27.89305 ? 94  PRO A O   1 
ATOM   750  C  CB  . PRO A 1 94  ? 6.04866   1.08945   24.64159  1.000 36.34033 ? 94  PRO A CB  1 
ATOM   751  C  CG  . PRO A 1 94  ? 5.25209   -0.10117  24.20910  1.000 30.11552 ? 94  PRO A CG  1 
ATOM   752  C  CD  . PRO A 1 94  ? 5.25193   -1.04636  25.38050  1.000 34.34621 ? 94  PRO A CD  1 
ATOM   753  N  N   . PRO A 1 95  ? 4.56690   3.36707   26.20135  1.000 33.97174 ? 95  PRO A N   1 
ATOM   754  C  CA  . PRO A 1 95  ? 3.38547   4.21115   26.39478  1.000 31.39629 ? 95  PRO A CA  1 
ATOM   755  C  C   . PRO A 1 95  ? 2.22699   3.82802   25.48377  1.000 33.64106 ? 95  PRO A C   1 
ATOM   756  O  O   . PRO A 1 95  ? 2.41440   3.40468   24.34039  1.000 30.74379 ? 95  PRO A O   1 
ATOM   757  C  CB  . PRO A 1 95  ? 3.89894   5.60848   26.05726  1.000 25.06880 ? 95  PRO A CB  1 
ATOM   758  C  CG  . PRO A 1 95  ? 5.33857   5.56004   26.38075  1.000 27.00045 ? 95  PRO A CG  1 
ATOM   759  C  CD  . PRO A 1 95  ? 5.80062   4.16974   26.11664  1.000 32.91468 ? 95  PRO A CD  1 
ATOM   760  N  N   A THR A 1 96  ? 1.01449   3.97067   26.00929  0.241 32.35422 ? 96  THR A N   1 
ATOM   761  N  N   B THR A 1 96  ? 1.01739   3.98427   26.01423  0.759 31.88275 ? 96  THR A N   1 
ATOM   762  C  CA  A THR A 1 96  ? -0.19513  3.85630   25.21350  0.241 34.25885 ? 96  THR A CA  1 
ATOM   763  C  CA  B THR A 1 96  ? -0.20617  3.83506   25.25040  0.759 34.27994 ? 96  THR A CA  1 
ATOM   764  C  C   A THR A 1 96  ? -0.93834  5.18278   25.25954  0.241 34.93688 ? 96  THR A C   1 
ATOM   765  C  C   B THR A 1 96  ? -0.93054  5.17584   25.26742  0.759 34.90361 ? 96  THR A C   1 
ATOM   766  O  O   A THR A 1 96  ? -0.70348  6.01989   26.13434  0.241 31.97659 ? 96  THR A O   1 
ATOM   767  O  O   B THR A 1 96  ? -0.66196  6.03179   26.11394  0.759 31.72129 ? 96  THR A O   1 
ATOM   768  C  CB  A THR A 1 96  ? -1.10378  2.71777   25.70149  0.241 35.06974 ? 96  THR A CB  1 
ATOM   769  C  CB  B THR A 1 96  ? -1.09063  2.71286   25.81882  0.759 35.06960 ? 96  THR A CB  1 
ATOM   770  O  OG1 A THR A 1 96  ? -2.27334  2.65300   24.87430  0.241 37.05011 ? 96  THR A OG1 1 
ATOM   771  O  OG1 B THR A 1 96  ? -1.00151  2.70154   27.24048  0.759 34.91174 ? 96  THR A OG1 1 
ATOM   772  C  CG2 A THR A 1 96  ? -1.52515  2.94088   27.14006  0.241 35.05123 ? 96  THR A CG2 1 
ATOM   773  C  CG2 B THR A 1 96  ? -0.61743  1.36097   25.34204  0.759 35.63951 ? 96  THR A CG2 1 
ATOM   774  N  N   . ILE A 1 97  ? -1.82458  5.37537   24.29649  1.000 32.16809 ? 97  ILE A N   1 
ATOM   775  C  CA  . ILE A 1 97  ? -2.58607  6.61124   24.18857  1.000 35.34436 ? 97  ILE A CA  1 
ATOM   776  C  C   . ILE A 1 97  ? -3.95970  6.41057   24.82142  1.000 45.96348 ? 97  ILE A C   1 
ATOM   777  O  O   . ILE A 1 97  ? -4.54407  5.31988   24.78376  1.000 45.93438 ? 97  ILE A O   1 
ATOM   778  C  CB  . ILE A 1 97  ? -2.70662  7.06754   22.72211  1.000 39.65605 ? 97  ILE A CB  1 
ATOM   779  C  CG1 . ILE A 1 97  ? -3.20716  8.51441   22.64106  1.000 42.37005 ? 97  ILE A CG1 1 
ATOM   780  C  CG2 . ILE A 1 97  ? -3.66916  6.17353   21.97191  1.000 43.68210 ? 97  ILE A CG2 1 
ATOM   781  C  CD1 . ILE A 1 97  ? -3.34067  9.01736   21.18818  1.000 39.84278 ? 97  ILE A CD1 1 
ATOM   782  N  N   . GLU A 1 98  ? -4.48765  7.47167   25.41905  1.000 42.05510 ? 98  GLU A N   1 
ATOM   783  C  CA  . GLU A 1 98  ? -5.85324  7.45235   25.91954  1.000 51.97769 ? 98  GLU A CA  1 
ATOM   784  C  C   . GLU A 1 98  ? -6.60842  8.62164   25.31579  1.000 54.89303 ? 98  GLU A C   1 
ATOM   785  O  O   . GLU A 1 98  ? -6.22432  9.77603   25.51355  1.000 53.76787 ? 98  GLU A O   1 
ATOM   786  C  CB  . GLU A 1 98  ? -5.89173  7.51722   27.44671  1.000 54.00370 ? 98  GLU A CB  1 
ATOM   787  C  CG  . GLU A 1 98  ? -7.07303  6.77447   28.04942  1.000 64.25009 ? 98  GLU A CG  1 
ATOM   788  C  CD  . GLU A 1 98  ? -6.70995  6.02825   29.31225  1.000 61.04221 ? 98  GLU A CD  1 
ATOM   789  O  OE1 . GLU A 1 98  ? -6.18963  4.89379   29.20690  1.000 64.58706 ? 98  GLU A OE1 1 
ATOM   790  O  OE2 . GLU A 1 98  ? -6.95393  6.57628   30.40768  1.000 54.69083 ? 98  GLU A OE2 1 
ATOM   791  N  N   A ILE A 1 99  ? -7.70722  8.30947   24.63306  0.560 58.92135 ? 99  ILE A N   1 
ATOM   792  N  N   B ILE A 1 99  ? -7.63693  8.34371   24.53016  0.440 58.95060 ? 99  ILE A N   1 
ATOM   793  C  CA  A ILE A 1 99  ? -8.59939  9.27056   23.99759  0.560 59.29289 ? 99  ILE A CA  1 
ATOM   794  C  CA  B ILE A 1 99  ? -8.50039  9.41192   24.05173  0.440 59.25454 ? 99  ILE A CA  1 
ATOM   795  C  C   A ILE A 1 99  ? -9.85713  9.31481   24.85512  0.560 65.37294 ? 99  ILE A C   1 
ATOM   796  C  C   B ILE A 1 99  ? -9.76589  9.31077   24.89242  0.440 65.33064 ? 99  ILE A C   1 
ATOM   797  O  O   A ILE A 1 99  ? -10.71982 8.43842   24.72704  0.560 69.66731 ? 99  ILE A O   1 
ATOM   798  O  O   B ILE A 1 99  ? -10.47023 8.29406   24.87648  0.440 69.14553 ? 99  ILE A O   1 
ATOM   799  C  CB  A ILE A 1 99  ? -8.92254  8.86038   22.55555  0.560 60.75378 ? 99  ILE A CB  1 
ATOM   800  C  CB  B ILE A 1 99  ? -8.73283  9.34499   22.53036  0.440 60.93329 ? 99  ILE A CB  1 
ATOM   801  C  CG1 A ILE A 1 99  ? -7.63079  8.65699   21.75643  0.560 58.75982 ? 99  ILE A CG1 1 
ATOM   802  C  CG1 B ILE A 1 99  ? -10.02012 8.64434   22.12079  0.440 61.42371 ? 99  ILE A CG1 1 
ATOM   803  C  CG2 A ILE A 1 99  ? -9.83949  9.87493   21.89564  0.560 60.32429 ? 99  ILE A CG2 1 
ATOM   804  C  CG2 B ILE A 1 99  ? -7.55808  8.64225   21.85289  0.440 58.71364 ? 99  ILE A CG2 1 
ATOM   805  C  CD1 A ILE A 1 99  ? -7.82597  7.94785   20.43399  0.560 55.59709 ? 99  ILE A CD1 1 
ATOM   806  C  CD1 B ILE A 1 99  ? -10.44855 8.94633   20.70220  0.440 61.00528 ? 99  ILE A CD1 1 
ATOM   807  N  N   . ASN A 1 100 ? -9.97479  10.32317  25.73098  1.000 69.79095 ? 100 ASN A N   1 
ATOM   808  C  CA  . ASN A 1 100 ? -10.97349 10.29896  26.80541  1.000 71.14172 ? 100 ASN A CA  1 
ATOM   809  C  C   . ASN A 1 100 ? -10.77037 9.05990   27.68051  1.000 72.06737 ? 100 ASN A C   1 
ATOM   810  O  O   . ASN A 1 100 ? -10.39874 9.17548   28.85216  1.000 75.55999 ? 100 ASN A O   1 
ATOM   811  C  CB  . ASN A 1 100 ? -12.39988 10.35894  26.24592  1.000 70.29316 ? 100 ASN A CB  1 
ATOM   812  C  CG  . ASN A 1 100 ? -12.58073 11.48226  25.24163  1.000 73.12115 ? 100 ASN A CG  1 
ATOM   813  O  OD1 . ASN A 1 100 ? -12.85139 12.62578  25.61103  1.000 76.32194 ? 100 ASN A OD1 1 
ATOM   814  N  ND2 . ASN A 1 100 ? -12.41073 11.16427  23.96308  1.000 68.69301 ? 100 ASN A ND2 1 
ATOM   815  N  N   . GLY A 1 101 ? -11.00123 7.87126   27.10926  1.000 75.28374 ? 101 GLY A N   1 
ATOM   816  C  CA  . GLY A 1 101 ? -10.59248 6.60616   27.69274  1.000 70.65348 ? 101 GLY A CA  1 
ATOM   817  C  C   . GLY A 1 101 ? -10.61155 5.45926   26.69505  1.000 74.07387 ? 101 GLY A C   1 
ATOM   818  O  O   . GLY A 1 101 ? -11.68092 4.89886   26.44467  1.000 67.83938 ? 101 GLY A O   1 
ATOM   819  N  N   . ILE A 1 102 ? -9.45358  5.10464   26.11672  1.000 81.11199 ? 102 ILE A N   1 
ATOM   820  C  CA  . ILE A 1 102 ? -9.34333  4.01935   25.13713  1.000 85.14182 ? 102 ILE A CA  1 
ATOM   821  C  C   . ILE A 1 102 ? -8.00699  3.29792   25.30974  1.000 84.82583 ? 102 ILE A C   1 
ATOM   822  O  O   . ILE A 1 102 ? -7.03445  3.86370   25.81607  1.000 82.52779 ? 102 ILE A O   1 
ATOM   823  C  CB  . ILE A 1 102 ? -9.52961  4.51976   23.67008  1.000 91.43668 ? 102 ILE A CB  1 
ATOM   824  C  CG1 . ILE A 1 102 ? -10.98466 4.90835   23.38832  1.000 96.26610 ? 102 ILE A CG1 1 
ATOM   825  C  CG2 . ILE A 1 102 ? -9.02888  3.53210   22.60832  1.000 81.85974 ? 102 ILE A CG2 1 
ATOM   826  C  CD1 . ILE A 1 102 ? -11.18558 5.54195   22.03105  1.000 85.98847 ? 102 ILE A CD1 1 
ATOM   827  N  N   . ALA A 1 103 ? -7.98046  2.02035   24.91558  1.000 84.37908 ? 103 ALA A N   1 
ATOM   828  C  CA  . ALA A 1 103 ? -6.74411  1.24579   24.78265  1.000 87.63840 ? 103 ALA A CA  1 
ATOM   829  C  C   . ALA A 1 103 ? -5.78126  1.88744   23.78680  1.000 68.99550 ? 103 ALA A C   1 
ATOM   830  O  O   . ALA A 1 103 ? -4.98114  1.19503   23.15729  1.000 67.33855 ? 103 ALA A O   1 
ATOM   831  C  CB  . ALA A 1 103 ? -7.05462  -0.18946  24.35120  1.000 85.98472 ? 103 ALA A CB  1 
ATOM   832  N  N   . MET A 1 110 ? 5.74066   -12.16725 28.01800  1.000 82.14255 ? 110 MET A N   1 
ATOM   833  C  CA  . MET A 1 110 ? 5.76392   -10.71981 27.83629  1.000 77.59268 ? 110 MET A CA  1 
ATOM   834  C  C   . MET A 1 110 ? 4.67223   -10.32149 26.84745  1.000 76.10637 ? 110 MET A C   1 
ATOM   835  O  O   . MET A 1 110 ? 4.37191   -11.06625 25.90899  1.000 76.20890 ? 110 MET A O   1 
ATOM   836  C  CB  . MET A 1 110 ? 7.14427   -10.25645 27.36431  1.000 83.32836 ? 110 MET A CB  1 
ATOM   837  C  CG  . MET A 1 110 ? 7.32919   -10.23725 25.86016  1.000 77.35640 ? 110 MET A CG  1 
ATOM   838  S  SD  . MET A 1 110 ? 8.29261   -8.81166  25.33491  1.000 87.92825 ? 110 MET A SD  1 
ATOM   839  C  CE  . MET A 1 110 ? 7.07088   -7.52243  25.53648  1.000 63.90170 ? 110 MET A CE  1 
ATOM   840  N  N   A ASN A 1 111 ? 4.08368   -9.14480  27.05511  0.538 68.41267 ? 111 ASN A N   1 
ATOM   841  N  N   B ASN A 1 111 ? 4.07937   -9.14442  27.05437  0.462 68.40808 ? 111 ASN A N   1 
ATOM   842  C  CA  A ASN A 1 111 ? 2.87967   -8.78938  26.31489  0.538 65.86734 ? 111 ASN A CA  1 
ATOM   843  C  CA  B ASN A 1 111 ? 2.87935   -8.79667  26.30334  0.462 65.84104 ? 111 ASN A CA  1 
ATOM   844  C  C   A ASN A 1 111 ? 3.13506   -7.77988  25.19480  0.538 63.60344 ? 111 ASN A C   1 
ATOM   845  C  C   B ASN A 1 111 ? 3.13876   -7.78036  25.18984  0.462 63.58491 ? 111 ASN A C   1 
ATOM   846  O  O   A ASN A 1 111 ? 3.14408   -8.16670  24.01939  0.538 61.41429 ? 111 ASN A O   1 
ATOM   847  O  O   B ASN A 1 111 ? 3.15271   -8.16189  24.01300  0.462 61.38638 ? 111 ASN A O   1 
ATOM   848  C  CB  A ASN A 1 111 ? 1.81034   -8.26326  27.27848  0.538 61.48778 ? 111 ASN A CB  1 
ATOM   849  C  CB  B ASN A 1 111 ? 1.78418   -8.28254  27.24757  0.462 61.56699 ? 111 ASN A CB  1 
ATOM   850  C  CG  A ASN A 1 111 ? 0.42966   -8.79889  26.96232  0.538 62.82961 ? 111 ASN A CG  1 
ATOM   851  C  CG  B ASN A 1 111 ? 2.27945   -8.06362  28.66639  0.462 63.85876 ? 111 ASN A CG  1 
ATOM   852  O  OD1 A ASN A 1 111 ? 0.10502   -9.06714  25.80189  0.538 56.55404 ? 111 ASN A OD1 1 
ATOM   853  O  OD1 B ASN A 1 111 ? 3.36143   -8.51052  29.04150  0.462 64.84066 ? 111 ASN A OD1 1 
ATOM   854  N  ND2 A ASN A 1 111 ? -0.39320  -8.96349  27.99533  0.538 64.50687 ? 111 ASN A ND2 1 
ATOM   855  N  ND2 B ASN A 1 111 ? 1.47991   -7.36830  29.46427  0.462 67.60776 ? 111 ASN A ND2 1 
ATOM   856  N  N   . PRO A 1 112 ? 3.37493   -6.48781  25.50103  1.000 66.62107 ? 112 PRO A N   1 
ATOM   857  C  CA  . PRO A 1 112 ? 3.11065   -5.43914  24.49453  1.000 51.75238 ? 112 PRO A CA  1 
ATOM   858  C  C   . PRO A 1 112 ? 4.01354   -5.41050  23.27471  1.000 55.93578 ? 112 PRO A C   1 
ATOM   859  O  O   . PRO A 1 112 ? 3.55138   -5.68900  22.16405  1.000 52.47877 ? 112 PRO A O   1 
ATOM   860  C  CB  . PRO A 1 112 ? 3.24521   -4.13720  25.29565  1.000 63.72952 ? 112 PRO A CB  1 
ATOM   861  C  CG  . PRO A 1 112 ? 3.84406   -4.51950  26.64216  1.000 65.04661 ? 112 PRO A CG  1 
ATOM   862  C  CD  . PRO A 1 112 ? 4.18441   -5.96581  26.61907  1.000 65.38071 ? 112 PRO A CD  1 
ATOM   863  N  N   . LEU A 1 113 ? 5.27946   -5.03356  23.43666  1.000 56.16511 ? 113 LEU A N   1 
ATOM   864  C  CA  . LEU A 1 113 ? 6.10307   -4.84423  22.25319  1.000 53.40749 ? 113 LEU A CA  1 
ATOM   865  C  C   . LEU A 1 113 ? 6.38457   -6.15969  21.52539  1.000 51.04126 ? 113 LEU A C   1 
ATOM   866  O  O   . LEU A 1 113 ? 6.63845   -6.14081  20.31612  1.000 44.41129 ? 113 LEU A O   1 
ATOM   867  C  CB  . LEU A 1 113 ? 7.37664   -4.08935  22.64198  1.000 50.72588 ? 113 LEU A CB  1 
ATOM   868  C  CG  . LEU A 1 113 ? 8.24861   -4.61132  23.77953  1.000 55.80197 ? 113 LEU A CG  1 
ATOM   869  C  CD1 . LEU A 1 113 ? 9.44585   -5.36927  23.25342  1.000 59.53598 ? 113 LEU A CD1 1 
ATOM   870  C  CD2 . LEU A 1 113 ? 8.69774   -3.45992  24.67753  1.000 58.57005 ? 113 LEU A CD2 1 
ATOM   871  N  N   . GLN A 1 114 ? 6.29660   -7.30220  22.21185  1.000 50.08396 ? 114 GLN A N   1 
ATOM   872  C  CA  . GLN A 1 114 ? 6.30569   -8.57526  21.49706  1.000 47.75295 ? 114 GLN A CA  1 
ATOM   873  C  C   . GLN A 1 114 ? 5.09097   -8.68877  20.58486  1.000 45.90172 ? 114 GLN A C   1 
ATOM   874  O  O   . GLN A 1 114 ? 5.18796   -9.22010  19.47017  1.000 42.55787 ? 114 GLN A O   1 
ATOM   875  C  CB  . GLN A 1 114 ? 6.32834   -9.74427  22.48622  1.000 53.80410 ? 114 GLN A CB  1 
ATOM   876  C  CG  . GLN A 1 114 ? 6.47352   -11.12757 21.85576  1.000 40.81204 ? 114 GLN A CG  1 
ATOM   877  C  CD  . GLN A 1 114 ? 7.79093   -11.29161 21.12164  1.000 45.10060 ? 114 GLN A CD  1 
ATOM   878  O  OE1 . GLN A 1 114 ? 8.85397   -11.10279 21.70322  1.000 49.64839 ? 114 GLN A OE1 1 
ATOM   879  N  NE2 . GLN A 1 114 ? 7.72903   -11.64425 19.83829  1.000 31.81345 ? 114 GLN A NE2 1 
ATOM   880  N  N   . ASP A 1 115 ? 3.93347   -8.19756  21.04285  1.000 46.36139 ? 115 ASP A N   1 
ATOM   881  C  CA  . ASP A 1 115 ? 2.71455   -8.30954  20.24188  1.000 44.98877 ? 115 ASP A CA  1 
ATOM   882  C  C   . ASP A 1 115 ? 2.85956   -7.58504  18.91033  1.000 35.38366 ? 115 ASP A C   1 
ATOM   883  O  O   . ASP A 1 115 ? 2.40869   -8.08274  17.87559  1.000 31.91725 ? 115 ASP A O   1 
ATOM   884  C  CB  . ASP A 1 115 ? 1.49949   -7.76184  21.00386  1.000 47.11794 ? 115 ASP A CB  1 
ATOM   885  C  CG  . ASP A 1 115 ? 0.98573   -8.71524  22.09853  1.000 57.71007 ? 115 ASP A CG  1 
ATOM   886  O  OD1 . ASP A 1 115 ? 1.34025   -9.91520  22.09072  1.000 54.75100 ? 115 ASP A OD1 1 
ATOM   887  O  OD2 . ASP A 1 115 ? 0.22662   -8.24798  22.98064  1.000 50.88807 ? 115 ASP A OD2 1 
ATOM   888  N  N   . THR A 1 116 ? 3.47516   -6.40404  18.90497  1.000 36.49901 ? 116 THR A N   1 
ATOM   889  C  CA  . THR A 1 116 ? 3.64163   -5.72256  17.62459  1.000 36.00487 ? 116 THR A CA  1 
ATOM   890  C  C   . THR A 1 116 ? 4.67751   -6.41686  16.75452  1.000 31.20582 ? 116 THR A C   1 
ATOM   891  O  O   . THR A 1 116 ? 4.57041   -6.38901  15.52492  1.000 35.77760 ? 116 THR A O   1 
ATOM   892  C  CB  . THR A 1 116 ? 3.99245   -4.24420  17.82561  1.000 40.50901 ? 116 THR A CB  1 
ATOM   893  O  OG1 . THR A 1 116 ? 4.95279   -3.84089  16.84123  1.000 37.75634 ? 116 THR A OG1 1 
ATOM   894  C  CG2 . THR A 1 116 ? 4.51385   -3.99395  19.18631  1.000 39.43554 ? 116 THR A CG2 1 
ATOM   895  N  N   . ARG A 1 117 ? 5.65153   -7.08779  17.35967  1.000 34.61386 ? 117 ARG A N   1 
ATOM   896  C  CA  . ARG A 1 117 ? 6.56673   -7.89451  16.56493  1.000 33.20250 ? 117 ARG A CA  1 
ATOM   897  C  C   . ARG A 1 117 ? 5.86889   -9.13336  16.02137  1.000 34.35791 ? 117 ARG A C   1 
ATOM   898  O  O   . ARG A 1 117 ? 6.14030   -9.55916  14.89494  1.000 32.25660 ? 117 ARG A O   1 
ATOM   899  C  CB  . ARG A 1 117 ? 7.78218   -8.28142  17.39810  1.000 30.51922 ? 117 ARG A CB  1 
ATOM   900  C  CG  . ARG A 1 117 ? 8.63185   -7.09338  17.77335  1.000 39.41061 ? 117 ARG A CG  1 
ATOM   901  C  CD  . ARG A 1 117 ? 10.07931  -7.52079  17.96765  1.000 41.72634 ? 117 ARG A CD  1 
ATOM   902  N  NE  . ARG A 1 117 ? 10.20146  -8.25961  19.21249  1.000 35.91947 ? 117 ARG A NE  1 
ATOM   903  C  CZ  . ARG A 1 117 ? 10.35725  -7.68652  20.39317  1.000 41.46602 ? 117 ARG A CZ  1 
ATOM   904  N  NH1 . ARG A 1 117 ? 10.46620  -6.37481  20.50814  1.000 47.39593 ? 117 ARG A NH1 1 
ATOM   905  N  NH2 . ARG A 1 117 ? 10.41169  -8.44874  21.48226  1.000 46.49037 ? 117 ARG A NH2 1 
ATOM   906  N  N   . ASN A 1 118 ? 4.96418   -9.72929  16.79844  1.000 30.44601 ? 118 ASN A N   1 
ATOM   907  C  CA  . ASN A 1 118 ? 4.20456   -10.85790 16.27422  1.000 34.75665 ? 118 ASN A CA  1 
ATOM   908  C  C   . ASN A 1 118 ? 3.34240   -10.42878 15.09399  1.000 34.50309 ? 118 ASN A C   1 
ATOM   909  O  O   . ASN A 1 118 ? 3.24225   -11.14324 14.09104  1.000 37.88545 ? 118 ASN A O   1 
ATOM   910  C  CB  . ASN A 1 118 ? 3.33883   -11.47015 17.37693  1.000 36.53315 ? 118 ASN A CB  1 
ATOM   911  C  CG  . ASN A 1 118 ? 4.16145   -12.16438 18.44698  1.000 38.56944 ? 118 ASN A CG  1 
ATOM   912  O  OD1 . ASN A 1 118 ? 5.31530   -12.52513 18.21705  1.000 31.75652 ? 118 ASN A OD1 1 
ATOM   913  N  ND2 . ASN A 1 118 ? 3.56277   -12.36857 19.62031  1.000 36.35941 ? 118 ASN A ND2 1 
ATOM   914  N  N   . LYS A 1 119 ? 2.71032   -9.26112  15.19887  1.000 33.93712 ? 119 LYS A N   1 
ATOM   915  C  CA  . LYS A 1 119 ? 1.89017   -8.74852  14.10313  1.000 33.55008 ? 119 LYS A CA  1 
ATOM   916  C  C   . LYS A 1 119 ? 2.71657   -8.57014  12.82640  1.000 29.39693 ? 119 LYS A C   1 
ATOM   917  O  O   . LYS A 1 119 ? 2.36374   -9.08566  11.76300  1.000 31.01749 ? 119 LYS A O   1 
ATOM   918  C  CB  . LYS A 1 119 ? 1.27636   -7.42297  14.51422  1.000 27.10509 ? 119 LYS A CB  1 
ATOM   919  C  CG  . LYS A 1 119 ? -0.09459  -7.50647  15.15824  1.000 31.22358 ? 119 LYS A CG  1 
ATOM   920  C  CD  . LYS A 1 119 ? -0.38165  -6.15156  15.77237  1.000 30.93575 ? 119 LYS A CD  1 
ATOM   921  C  CE  . LYS A 1 119 ? -1.31045  -6.26655  16.96970  1.000 42.33695 ? 119 LYS A CE  1 
ATOM   922  N  NZ  . LYS A 1 119 ? -1.43377  -4.94852  17.65065  1.000 49.70311 ? 119 LYS A NZ  1 
ATOM   923  N  N   . VAL A 1 120 ? 3.81562   -7.82371  12.91698  1.000 33.65825 ? 120 VAL A N   1 
ATOM   924  C  CA  . VAL A 1 120 ? 4.65587   -7.57572  11.75641  1.000 26.29703 ? 120 VAL A CA  1 
ATOM   925  C  C   . VAL A 1 120 ? 5.28816   -8.87543  11.26919  1.000 34.01137 ? 120 VAL A C   1 
ATOM   926  O  O   . VAL A 1 120 ? 5.52328   -9.05316  10.06240  1.000 30.95142 ? 120 VAL A O   1 
ATOM   927  C  CB  . VAL A 1 120 ? 5.70510   -6.50663  12.11091  1.000 25.31685 ? 120 VAL A CB  1 
ATOM   928  C  CG1 . VAL A 1 120 ? 6.71163   -6.33675  10.98598  1.000 27.55223 ? 120 VAL A CG1 1 
ATOM   929  C  CG2 . VAL A 1 120 ? 5.02700   -5.17251  12.41746  1.000 24.78528 ? 120 VAL A CG2 1 
ATOM   930  N  N   . ASN A 1 121 ? 5.53819   -9.82582  12.17369  1.000 26.54904 ? 121 ASN A N   1 
ATOM   931  C  CA  . ASN A 1 121 ? 6.11971   -11.08550 11.73040  1.000 29.85825 ? 121 ASN A CA  1 
ATOM   932  C  C   . ASN A 1 121 ? 5.19530   -11.86814 10.81421  1.000 40.22279 ? 121 ASN A C   1 
ATOM   933  O  O   . ASN A 1 121 ? 5.68863   -12.71125 10.05896  1.000 41.66192 ? 121 ASN A O   1 
ATOM   934  C  CB  . ASN A 1 121 ? 6.50515   -11.96929 12.91306  1.000 30.80145 ? 121 ASN A CB  1 
ATOM   935  C  CG  . ASN A 1 121 ? 7.79974   -11.55092 13.53513  1.000 29.24784 ? 121 ASN A CG  1 
ATOM   936  O  OD1 . ASN A 1 121 ? 8.56056   -10.77851 12.94616  1.000 34.22513 ? 121 ASN A OD1 1 
ATOM   937  N  ND2 . ASN A 1 121 ? 8.05614   -12.02941 14.74439  1.000 33.10993 ? 121 ASN A ND2 1 
ATOM   938  N  N   . THR A 1 122 ? 3.87869   -11.62195 10.86425  1.000 33.64848 ? 122 THR A N   1 
ATOM   939  C  CA  . THR A 1 122 ? 2.96589   -12.38816 10.02427  1.000 30.50309 ? 122 THR A CA  1 
ATOM   940  C  C   . THR A 1 122 ? 3.23754   -12.14417 8.54867   1.000 36.60566 ? 122 THR A C   1 
ATOM   941  O  O   . THR A 1 122 ? 3.09456   -13.05794 7.72356   1.000 36.98392 ? 122 THR A O   1 
ATOM   942  C  CB  . THR A 1 122 ? 1.51332   -12.03767 10.33249  1.000 32.04914 ? 122 THR A CB  1 
ATOM   943  O  OG1 . THR A 1 122 ? 1.26882   -10.65325 10.00301  1.000 27.11561 ? 122 THR A OG1 1 
ATOM   944  C  CG2 . THR A 1 122 ? 1.20239   -12.29786 11.80800  1.000 34.71221 ? 122 THR A CG2 1 
ATOM   945  N  N   . VAL A 1 123 ? 3.59915   -10.91519 8.19203   1.000 28.94500 ? 123 VAL A N   1 
ATOM   946  C  CA  . VAL A 1 123 ? 3.78970   -10.54253 6.79411   1.000 32.87823 ? 123 VAL A CA  1 
ATOM   947  C  C   . VAL A 1 123 ? 5.25759   -10.31695 6.44037   1.000 38.49165 ? 123 VAL A C   1 
ATOM   948  O  O   . VAL A 1 123 ? 5.57475   -10.15047 5.24949   1.000 31.22792 ? 123 VAL A O   1 
ATOM   949  C  CB  . VAL A 1 123 ? 2.95550   -9.30005  6.43127   1.000 36.12256 ? 123 VAL A CB  1 
ATOM   950  C  CG1 . VAL A 1 123 ? 1.47067   -9.64638  6.44529   1.000 35.48728 ? 123 VAL A CG1 1 
ATOM   951  C  CG2 . VAL A 1 123 ? 3.22575   -8.18386  7.40385   1.000 28.77960 ? 123 VAL A CG2 1 
ATOM   952  N  N   . MET A 1 124 ? 6.14806   -10.28715 7.42555   1.000 34.00387 ? 124 MET A N   1 
ATOM   953  C  CA  . MET A 1 124 ? 7.59283   -10.31508 7.21819   1.000 35.31458 ? 124 MET A CA  1 
ATOM   954  C  C   . MET A 1 124 ? 8.03824   -9.28426  6.16948   1.000 31.94383 ? 124 MET A C   1 
ATOM   955  O  O   . MET A 1 124 ? 8.54795   -9.64759  5.10924   1.000 30.00136 ? 124 MET A O   1 
ATOM   956  C  CB  . MET A 1 124 ? 8.01537   -11.71815 6.80787   1.000 40.55609 ? 124 MET A CB  1 
ATOM   957  C  CG  . MET A 1 124 ? 8.39507   -12.69775 7.93766   1.000 38.62008 ? 124 MET A CG  1 
ATOM   958  S  SD  . MET A 1 124 ? 9.15235   -12.29692 9.52352   1.000 39.06523 ? 124 MET A SD  1 
ATOM   959  C  CE  . MET A 1 124 ? 10.19124  -10.88814 9.22999   1.000 43.58722 ? 124 MET A CE  1 
ATOM   960  N  N   . PRO A 1 125 ? 7.81896   -7.99432  6.42050   1.000 31.58303 ? 125 PRO A N   1 
ATOM   961  C  CA  . PRO A 1 125 ? 8.18580   -6.97489  5.42498   1.000 32.53051 ? 125 PRO A CA  1 
ATOM   962  C  C   . PRO A 1 125 ? 9.69256   -6.90524  5.25385   1.000 38.86197 ? 125 PRO A C   1 
ATOM   963  O  O   . PRO A 1 125 ? 10.43732  -6.86980  6.23304   1.000 34.21489 ? 125 PRO A O   1 
ATOM   964  C  CB  . PRO A 1 125 ? 7.63157   -5.67228  6.01900   1.000 33.20207 ? 125 PRO A CB  1 
ATOM   965  C  CG  . PRO A 1 125 ? 6.82550   -6.07080  7.19769   1.000 29.64313 ? 125 PRO A CG  1 
ATOM   966  C  CD  . PRO A 1 125 ? 7.28744   -7.40191  7.64718   1.000 26.78787 ? 125 PRO A CD  1 
ATOM   967  N  N   . ARG A 1 126 ? 10.13506  -6.86788  4.00242   1.000 39.14525 ? 126 ARG A N   1 
ATOM   968  C  CA  . ARG A 1 126 ? 11.54710  -6.96144  3.66353   1.000 40.20946 ? 126 ARG A CA  1 
ATOM   969  C  C   . ARG A 1 126 ? 12.04843  -5.62907  3.11707   1.000 39.71493 ? 126 ARG A C   1 
ATOM   970  O  O   . ARG A 1 126 ? 11.27414  -4.79216  2.64305   1.000 37.23822 ? 126 ARG A O   1 
ATOM   971  C  CB  . ARG A 1 126 ? 11.77825  -8.06705  2.62043   1.000 42.38000 ? 126 ARG A CB  1 
ATOM   972  C  CG  . ARG A 1 126 ? 12.21984  -9.40999  3.19400   1.000 48.06585 ? 126 ARG A CG  1 
ATOM   973  C  CD  . ARG A 1 126 ? 13.10626  -10.26462 2.22717   1.000 56.32525 ? 126 ARG A CD  1 
ATOM   974  N  NE  . ARG A 1 126 ? 14.40641  -9.67739  1.90223   1.000 48.63251 ? 126 ARG A NE  1 
ATOM   975  C  CZ  . ARG A 1 126 ? 14.64182  -8.85509  0.88249   1.000 57.40209 ? 126 ARG A CZ  1 
ATOM   976  N  NH1 . ARG A 1 126 ? 13.68667  -8.52012  0.02367   1.000 55.82607 ? 126 ARG A NH1 1 
ATOM   977  N  NH2 . ARG A 1 126 ? 15.87138  -8.36569  0.71087   1.000 46.69082 ? 126 ARG A NH2 1 
ATOM   978  N  N   . GLU A 1 127 ? 13.36484  -5.45097  3.17551   1.000 39.74975 ? 127 GLU A N   1 
ATOM   979  C  CA  . GLU A 1 127 ? 14.01574  -4.34435  2.48742   1.000 35.68895 ? 127 GLU A CA  1 
ATOM   980  C  C   . GLU A 1 127 ? 13.61399  -4.31723  1.01387   1.000 34.71135 ? 127 GLU A C   1 
ATOM   981  O  O   . GLU A 1 127 ? 13.54652  -5.35640  0.35402   1.000 35.92353 ? 127 GLU A O   1 
ATOM   982  C  CB  . GLU A 1 127 ? 15.53736  -4.47943  2.64340   1.000 41.85738 ? 127 GLU A CB  1 
ATOM   983  C  CG  . GLU A 1 127 ? 16.36856  -3.73467  1.62539   1.000 38.84803 ? 127 GLU A CG  1 
ATOM   984  C  CD  . GLU A 1 127 ? 17.86221  -4.01145  1.76308   1.000 48.18679 ? 127 GLU A CD  1 
ATOM   985  O  OE1 . GLU A 1 127 ? 18.25730  -4.88413  2.57634   1.000 42.24431 ? 127 GLU A OE1 1 
ATOM   986  O  OE2 . GLU A 1 127 ? 18.64092  -3.36999  1.02611   1.000 44.36934 ? 127 GLU A OE2 1 
ATOM   987  N  N   . GLY A 1 128 ? 13.32522  -3.11380  0.50551   1.000 34.50194 ? 128 GLY A N   1 
ATOM   988  C  CA  . GLY A 1 128 ? 12.87467  -2.92720  -0.85955  1.000 35.65553 ? 128 GLY A CA  1 
ATOM   989  C  C   . GLY A 1 128 ? 11.37650  -3.00366  -1.04841  1.000 38.18084 ? 128 GLY A C   1 
ATOM   990  O  O   . GLY A 1 128 ? 10.90063  -2.87330  -2.18315  1.000 42.18020 ? 128 GLY A O   1 
ATOM   991  N  N   . GLU A 1 129 ? 10.61641  -3.22080  0.01623   1.000 38.90509 ? 129 GLU A N   1 
ATOM   992  C  CA  . GLU A 1 129 ? 9.16955   -3.36554  -0.07165  1.000 34.90511 ? 129 GLU A CA  1 
ATOM   993  C  C   . GLU A 1 129 ? 8.48097   -2.13267  0.49767   1.000 27.59100 ? 129 GLU A C   1 
ATOM   994  O  O   . GLU A 1 129 ? 9.05079   -1.39689  1.30498   1.000 32.10861 ? 129 GLU A O   1 
ATOM   995  C  CB  . GLU A 1 129 ? 8.71082   -4.62253  0.67165   1.000 32.77642 ? 129 GLU A CB  1 
ATOM   996  C  CG  . GLU A 1 129 ? 8.92847   -5.90296  -0.12646  1.000 32.50340 ? 129 GLU A CG  1 
ATOM   997  C  CD  . GLU A 1 129 ? 8.64377   -7.15107  0.68564   1.000 31.53791 ? 129 GLU A CD  1 
ATOM   998  O  OE1 . GLU A 1 129 ? 8.47476   -7.01981  1.91218   1.000 37.69717 ? 129 GLU A OE1 1 
ATOM   999  O  OE2 . GLU A 1 129 ? 8.59267   -8.25949  0.10328   1.000 33.23658 ? 129 GLU A OE2 1 
ATOM   1000 N  N   . THR A 1 130 ? 7.23282   -1.92535  0.08785   1.000 31.21947 ? 130 THR A N   1 
ATOM   1001 C  CA  . THR A 1 130 ? 6.42102   -0.81140  0.55393   1.000 27.98610 ? 130 THR A CA  1 
ATOM   1002 C  C   . THR A 1 130 ? 5.22193   -1.37479  1.30216   1.000 33.12559 ? 130 THR A C   1 
ATOM   1003 O  O   . THR A 1 130 ? 4.50126   -2.22459  0.76994   1.000 31.51254 ? 130 THR A O   1 
ATOM   1004 C  CB  . THR A 1 130 ? 5.95549   0.06297   -0.62461  1.000 33.67277 ? 130 THR A CB  1 
ATOM   1005 O  OG1 . THR A 1 130 ? 7.06575   0.34042   -1.49336  1.000 37.27582 ? 130 THR A OG1 1 
ATOM   1006 C  CG2 . THR A 1 130 ? 5.37283   1.37267   -0.12455  1.000 27.78249 ? 130 THR A CG2 1 
ATOM   1007 N  N   . VAL A 1 131 ? 5.00652   -0.91638  2.53327   1.000 25.60858 ? 131 VAL A N   1 
ATOM   1008 C  CA  . VAL A 1 131 ? 3.95110   -1.47789  3.36564   1.000 27.95518 ? 131 VAL A CA  1 
ATOM   1009 C  C   . VAL A 1 131 ? 2.94151   -0.38742  3.68310   1.000 24.16952 ? 131 VAL A C   1 
ATOM   1010 O  O   . VAL A 1 131 ? 3.27460   0.79561   3.81704   1.000 27.22550 ? 131 VAL A O   1 
ATOM   1011 C  CB  . VAL A 1 131 ? 4.48034   -2.14373  4.66684   1.000 33.67033 ? 131 VAL A CB  1 
ATOM   1012 C  CG1 . VAL A 1 131 ? 5.96100   -2.02107  4.77973   1.000 28.31643 ? 131 VAL A CG1 1 
ATOM   1013 C  CG2 . VAL A 1 131 ? 3.78812   -1.60390  5.91597   1.000 23.86183 ? 131 VAL A CG2 1 
ATOM   1014 N  N   . LEU A 1 132 ? 1.69081   -0.79505  3.76773   1.000 23.11831 ? 132 LEU A N   1 
ATOM   1015 C  CA  . LEU A 1 132 ? 0.60881   0.08515   4.16879   1.000 27.41193 ? 132 LEU A CA  1 
ATOM   1016 C  C   . LEU A 1 132 ? 0.15016   -0.35378  5.54404   1.000 25.54766 ? 132 LEU A C   1 
ATOM   1017 O  O   . LEU A 1 132 ? -0.23904  -1.51880  5.73440   1.000 24.03152 ? 132 LEU A O   1 
ATOM   1018 C  CB  . LEU A 1 132 ? -0.55461  0.03765   3.18096   1.000 19.36373 ? 132 LEU A CB  1 
ATOM   1019 C  CG  . LEU A 1 132 ? -1.71595  0.88896   3.68638   1.000 21.22588 ? 132 LEU A CG  1 
ATOM   1020 C  CD1 . LEU A 1 132 ? -1.31120  2.32860   3.85569   1.000 20.55187 ? 132 LEU A CD1 1 
ATOM   1021 C  CD2 . LEU A 1 132 ? -2.90595  0.80362   2.72709   1.000 21.79082 ? 132 LEU A CD2 1 
ATOM   1022 N  N   . ASP A 1 133 ? 0.22302   0.56147   6.50110   1.000 20.85131 ? 133 ASP A N   1 
ATOM   1023 C  CA  . ASP A 1 133 ? -0.29086  0.33862   7.84224   1.000 19.42542 ? 133 ASP A CA  1 
ATOM   1024 C  C   . ASP A 1 133 ? -1.51537  1.24186   7.99219   1.000 19.81021 ? 133 ASP A C   1 
ATOM   1025 O  O   . ASP A 1 133 ? -1.38217  2.46481   8.09490   1.000 20.79823 ? 133 ASP A O   1 
ATOM   1026 C  CB  . ASP A 1 133 ? 0.83812   0.60181   8.83924   1.000 24.51052 ? 133 ASP A CB  1 
ATOM   1027 C  CG  . ASP A 1 133 ? 0.38429   0.61894   10.26275  1.000 27.97918 ? 133 ASP A CG  1 
ATOM   1028 O  OD1 . ASP A 1 133 ? -0.08997  -0.42659  10.72056  1.000 32.82589 ? 133 ASP A OD1 1 
ATOM   1029 O  OD2 . ASP A 1 133 ? 0.58279   1.64576   10.95429  1.000 29.09678 ? 133 ASP A OD2 1 
ATOM   1030 N  N   . THR A 1 134 ? -2.71448  0.63233   7.97660   1.000 19.81757 ? 134 THR A N   1 
ATOM   1031 C  CA  . THR A 1 134 ? -3.97133  1.36795   7.82591   1.000 18.69175 ? 134 THR A CA  1 
ATOM   1032 C  C   . THR A 1 134 ? -4.38131  2.20357   9.03586   1.000 22.66585 ? 134 THR A C   1 
ATOM   1033 O  O   . THR A 1 134 ? -5.11636  3.17329   8.86654   1.000 25.77541 ? 134 THR A O   1 
ATOM   1034 C  CB  . THR A 1 134 ? -5.11950  0.41441   7.52521   1.000 17.10255 ? 134 THR A CB  1 
ATOM   1035 O  OG1 . THR A 1 134 ? -5.23641  -0.53644  8.58030   1.000 22.55144 ? 134 THR A OG1 1 
ATOM   1036 C  CG2 . THR A 1 134 ? -4.88747  -0.32866  6.24715   1.000 20.23596 ? 134 THR A CG2 1 
ATOM   1037 N  N   A CYS A 1 135 ? -3.97682  1.83751   10.25025  0.572 23.87876 ? 135 CYS A N   1 
ATOM   1038 N  N   B CYS A 1 135 ? -3.92747  1.85590   10.24085  0.428 24.76134 ? 135 CYS A N   1 
ATOM   1039 C  CA  A CYS A 1 135 ? -4.33575  2.60973   11.44754  0.572 28.38096 ? 135 CYS A CA  1 
ATOM   1040 C  CA  B CYS A 1 135 ? -4.32214  2.55004   11.47225  0.428 28.00607 ? 135 CYS A CA  1 
ATOM   1041 C  C   A CYS A 1 135 ? -3.09433  2.79251   12.31637  0.572 24.72226 ? 135 CYS A C   1 
ATOM   1042 C  C   B CYS A 1 135 ? -3.07240  2.77910   12.31929  0.428 27.77542 ? 135 CYS A C   1 
ATOM   1043 O  O   A CYS A 1 135 ? -2.68320  1.86186   13.01093  0.572 27.04755 ? 135 CYS A O   1 
ATOM   1044 O  O   B CYS A 1 135 ? -2.62593  1.85963   13.01065  0.428 27.41476 ? 135 CYS A O   1 
ATOM   1045 C  CB  A CYS A 1 135 ? -5.46981  1.94645   12.22572  0.572 28.46294 ? 135 CYS A CB  1 
ATOM   1046 C  CB  B CYS A 1 135 ? -5.37041  1.73899   12.23478  0.428 28.45817 ? 135 CYS A CB  1 
ATOM   1047 S  SG  A CYS A 1 135 ? -6.75269  1.15054   11.22338  0.572 32.07150 ? 135 CYS A SG  1 
ATOM   1048 S  SG  B CYS A 1 135 ? -6.08371  2.53780   13.70709  0.428 36.41053 ? 135 CYS A SG  1 
ATOM   1049 N  N   . MET A 1 136 ? -2.50375  3.99173   12.25512  1.000 24.50187 ? 136 MET A N   1 
ATOM   1050 C  CA  . MET A 1 136 ? -1.30855  4.31799   13.04133  1.000 31.44043 ? 136 MET A CA  1 
ATOM   1051 C  C   . MET A 1 136 ? -1.40172  3.95956   14.51745  1.000 30.63529 ? 136 MET A C   1 
ATOM   1052 O  O   . MET A 1 136 ? -0.54686  3.23650   15.04593  1.000 26.52793 ? 136 MET A O   1 
ATOM   1053 C  CB  . MET A 1 136 ? -0.97004  5.81235   13.01862  1.000 31.25306 ? 136 MET A CB  1 
ATOM   1054 C  CG  . MET A 1 136 ? 0.52698   6.10025   12.85641  1.000 26.46371 ? 136 MET A CG  1 
ATOM   1055 S  SD  . MET A 1 136 ? 0.92867   7.79013   12.44742  1.000 21.54024 ? 136 MET A SD  1 
ATOM   1056 C  CE  . MET A 1 136 ? 0.47424   8.55866   13.98417  1.000 31.49303 ? 136 MET A CE  1 
ATOM   1057 N  N   . GLY A 1 137 ? -2.32740  4.60551   15.22028  1.000 24.03924 ? 137 GLY A N   1 
ATOM   1058 C  CA  . GLY A 1 137 ? -2.22292  4.72158   16.67220  1.000 26.77231 ? 137 GLY A CA  1 
ATOM   1059 C  C   . GLY A 1 137 ? -0.95684  5.49679   16.99150  1.000 29.15082 ? 137 GLY A C   1 
ATOM   1060 O  O   . GLY A 1 137 ? -0.68470  6.55309   16.41613  1.000 28.78863 ? 137 GLY A O   1 
ATOM   1061 N  N   . LEU A 1 138 ? -0.10934  4.94120   17.84618  1.000 30.56231 ? 138 LEU A N   1 
ATOM   1062 C  CA  . LEU A 1 138 ? 1.16258   5.57505   18.15976  1.000 27.98230 ? 138 LEU A CA  1 
ATOM   1063 C  C   . LEU A 1 138 ? 2.25409   5.21323   17.16357  1.000 24.28005 ? 138 LEU A C   1 
ATOM   1064 O  O   . LEU A 1 138 ? 3.38804   5.67662   17.31019  1.000 27.13301 ? 138 LEU A O   1 
ATOM   1065 C  CB  . LEU A 1 138 ? 1.59184   5.20060   19.58960  1.000 26.18685 ? 138 LEU A CB  1 
ATOM   1066 C  CG  . LEU A 1 138 ? 0.74368   5.93968   20.62355  1.000 28.65693 ? 138 LEU A CG  1 
ATOM   1067 C  CD1 . LEU A 1 138 ? 1.09224   5.55853   22.06600  1.000 26.66660 ? 138 LEU A CD1 1 
ATOM   1068 C  CD2 . LEU A 1 138 ? 0.85691   7.44403   20.40896  1.000 32.50075 ? 138 LEU A CD2 1 
ATOM   1069 N  N   . GLY A 1 139 ? 1.95080   4.38989   16.17005  1.000 28.86848 ? 139 GLY A N   1 
ATOM   1070 C  CA  . GLY A 1 139 ? 2.90237   4.09612   15.12522  1.000 25.10587 ? 139 GLY A CA  1 
ATOM   1071 C  C   . GLY A 1 139 ? 3.76417   2.88803   15.36763  1.000 20.45338 ? 139 GLY A C   1 
ATOM   1072 O  O   . GLY A 1 139 ? 4.70615   2.65571   14.59673  1.000 27.44243 ? 139 GLY A O   1 
ATOM   1073 N  N   . TYR A 1 140 ? 3.47993   2.10477   16.40950  1.000 23.13517 ? 140 TYR A N   1 
ATOM   1074 C  CA  . TYR A 1 140 ? 4.42083   1.06449   16.81360  1.000 21.57570 ? 140 TYR A CA  1 
ATOM   1075 C  C   . TYR A 1 140 ? 4.51833   -0.02118  15.76619  1.000 28.68692 ? 140 TYR A C   1 
ATOM   1076 O  O   . TYR A 1 140 ? 5.59431   -0.59092  15.56384  1.000 23.39444 ? 140 TYR A O   1 
ATOM   1077 C  CB  . TYR A 1 140 ? 4.01231   0.44548   18.14793  1.000 30.65277 ? 140 TYR A CB  1 
ATOM   1078 C  CG  . TYR A 1 140 ? 4.12291   1.37757   19.32301  1.000 28.22882 ? 140 TYR A CG  1 
ATOM   1079 C  CD1 . TYR A 1 140 ? 4.91975   2.51789   19.26997  1.000 27.63088 ? 140 TYR A CD1 1 
ATOM   1080 C  CD2 . TYR A 1 140 ? 3.46503   1.09174   20.50406  1.000 32.05343 ? 140 TYR A CD2 1 
ATOM   1081 C  CE1 . TYR A 1 140 ? 5.02628   3.36325   20.36627  1.000 31.83603 ? 140 TYR A CE1 1 
ATOM   1082 C  CE2 . TYR A 1 140 ? 3.56147   1.92878   21.59786  1.000 35.83598 ? 140 TYR A CE2 1 
ATOM   1083 C  CZ  . TYR A 1 140 ? 4.34445   3.04545   21.53108  1.000 29.02305 ? 140 TYR A CZ  1 
ATOM   1084 O  OH  . TYR A 1 140 ? 4.42490   3.84766   22.62601  1.000 28.69202 ? 140 TYR A OH  1 
ATOM   1085 N  N   . THR A 1 141 ? 3.39399   -0.35975  15.12540  1.000 22.84340 ? 141 THR A N   1 
ATOM   1086 C  CA  . THR A 1 141 ? 3.45227   -1.35741  14.06577  1.000 29.21627 ? 141 THR A CA  1 
ATOM   1087 C  C   . THR A 1 141 ? 4.13584   -0.79524  12.83024  1.000 26.21364 ? 141 THR A C   1 
ATOM   1088 O  O   . THR A 1 141 ? 4.91177   -1.49668  12.16799  1.000 30.19397 ? 141 THR A O   1 
ATOM   1089 C  CB  . THR A 1 141 ? 2.04719   -1.85531  13.73026  1.000 24.61955 ? 141 THR A CB  1 
ATOM   1090 O  OG1 . THR A 1 141 ? 1.46085   -2.45228  14.89273  1.000 31.21720 ? 141 THR A OG1 1 
ATOM   1091 C  CG2 . THR A 1 141 ? 2.12172   -2.88154  12.68429  1.000 18.57137 ? 141 THR A CG2 1 
ATOM   1092 N  N   . ALA A 1 142 ? 3.86859   0.47293   12.51058  1.000 23.47264 ? 142 ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 142 ? 4.53236   1.10999   11.38114  1.000 28.17557 ? 142 ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 142 ? 6.03227   1.15275   11.59807  1.000 23.51082 ? 142 ALA A C   1 
ATOM   1095 O  O   . ALA A 1 142 ? 6.81055   0.80808   10.69937  1.000 28.48865 ? 142 ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 142 ? 3.96873   2.51687   11.15865  1.000 21.86511 ? 142 ALA A CB  1 
ATOM   1097 N  N   . ILE A 1 143 ? 6.45971   1.54032   12.80261  1.000 26.99497 ? 143 ILE A N   1 
ATOM   1098 C  CA  . ILE A 1 143 ? 7.88899   1.63463   13.10268  1.000 25.84586 ? 143 ILE A CA  1 
ATOM   1099 C  C   . ILE A 1 143 ? 8.55628   0.25804   13.04514  1.000 25.21235 ? 143 ILE A C   1 
ATOM   1100 O  O   . ILE A 1 143 ? 9.61482   0.09584   12.43197  1.000 31.10586 ? 143 ILE A O   1 
ATOM   1101 C  CB  . ILE A 1 143 ? 8.09264   2.33519   14.46072  1.000 26.02102 ? 143 ILE A CB  1 
ATOM   1102 C  CG1 . ILE A 1 143 ? 7.68062   3.80179   14.34485  1.000 26.79395 ? 143 ILE A CG1 1 
ATOM   1103 C  CG2 . ILE A 1 143 ? 9.50584   2.21243   14.96274  1.000 30.32240 ? 143 ILE A CG2 1 
ATOM   1104 C  CD1 . ILE A 1 143 ? 7.56962   4.51146   15.66752  1.000 24.86401 ? 143 ILE A CD1 1 
ATOM   1105 N  N   . GLU A 1 144 ? 7.95647   -0.74794  13.68644  1.000 27.47019 ? 144 GLU A N   1 
ATOM   1106 C  CA  . GLU A 1 144 ? 8.52660   -2.09443  13.65785  1.000 24.79918 ? 144 GLU A CA  1 
ATOM   1107 C  C   . GLU A 1 144 ? 8.66937   -2.61116  12.23044  1.000 30.48025 ? 144 GLU A C   1 
ATOM   1108 O  O   . GLU A 1 144 ? 9.67270   -3.25148  11.89117  1.000 29.35606 ? 144 GLU A O   1 
ATOM   1109 C  CB  . GLU A 1 144 ? 7.65880   -3.05478  14.47972  1.000 30.83582 ? 144 GLU A CB  1 
ATOM   1110 C  CG  . GLU A 1 144 ? 8.11854   -4.51698  14.46188  1.000 29.74643 ? 144 GLU A CG  1 
ATOM   1111 C  CD  . GLU A 1 144 ? 9.39297   -4.71836  15.24033  1.000 34.50086 ? 144 GLU A CD  1 
ATOM   1112 O  OE1 . GLU A 1 144 ? 9.58968   -3.99613  16.23965  1.000 40.45445 ? 144 GLU A OE1 1 
ATOM   1113 O  OE2 . GLU A 1 144 ? 10.19441  -5.59483  14.85841  1.000 34.72343 ? 144 GLU A OE2 1 
ATOM   1114 N  N   . ALA A 1 145 ? 7.68137   -2.33774  11.37242  1.000 30.26178 ? 145 ALA A N   1 
ATOM   1115 C  CA  . ALA A 1 145 ? 7.76504   -2.77861  9.97918   1.000 30.45245 ? 145 ALA A CA  1 
ATOM   1116 C  C   . ALA A 1 145 ? 8.85087   -2.04186  9.20637   1.000 32.86539 ? 145 ALA A C   1 
ATOM   1117 O  O   . ALA A 1 145 ? 9.38988   -2.57916  8.23425   1.000 35.17762 ? 145 ALA A O   1 
ATOM   1118 C  CB  . ALA A 1 145 ? 6.41343   -2.59352  9.28702   1.000 31.96675 ? 145 ALA A CB  1 
ATOM   1119 N  N   . SER A 1 146 ? 9.16064   -0.80773  9.59689   1.000 27.95783 ? 146 SER A N   1 
ATOM   1120 C  CA  . SER A 1 146 ? 10.20466  -0.04569  8.93321   1.000 26.59733 ? 146 SER A CA  1 
ATOM   1121 C  C   . SER A 1 146 ? 11.58589  -0.44225  9.42912   1.000 37.33583 ? 146 SER A C   1 
ATOM   1122 O  O   . SER A 1 146 ? 12.55808  -0.36514  8.67759   1.000 33.50426 ? 146 SER A O   1 
ATOM   1123 C  CB  . SER A 1 146 ? 9.99105   1.44297   9.17999   1.000 31.74601 ? 146 SER A CB  1 
ATOM   1124 O  OG  . SER A 1 146 ? 10.35494  1.76972   10.51814  1.000 30.40684 ? 146 SER A OG  1 
ATOM   1125 N  N   . LYS A 1 147 ? 11.69936  -0.85208  10.68977  1.000 40.76869 ? 147 LYS A N   1 
ATOM   1126 C  CA  . LYS A 1 147 ? 12.98258  -1.32215  11.18848  1.000 39.63850 ? 147 LYS A CA  1 
ATOM   1127 C  C   . LYS A 1 147 ? 13.44222  -2.58291  10.47435  1.000 33.25722 ? 147 LYS A C   1 
ATOM   1128 O  O   . LYS A 1 147 ? 14.61299  -2.95514  10.59473  1.000 52.66143 ? 147 LYS A O   1 
ATOM   1129 C  CB  . LYS A 1 147 ? 12.89565  -1.54841  12.70122  1.000 41.00614 ? 147 LYS A CB  1 
ATOM   1130 C  CG  . LYS A 1 147 ? 13.02297  -0.25729  13.51812  1.000 35.37354 ? 147 LYS A CG  1 
ATOM   1131 C  CD  . LYS A 1 147 ? 13.41114  -0.54805  14.96002  1.000 46.62590 ? 147 LYS A CD  1 
ATOM   1132 C  CE  . LYS A 1 147 ? 12.98556  0.58777   15.89392  1.000 47.73728 ? 147 LYS A CE  1 
ATOM   1133 N  NZ  . LYS A 1 147 ? 12.04637  0.12202   16.96426  1.000 44.49161 ? 147 LYS A NZ  1 
ATOM   1134 N  N   . ARG A 1 148 ? 12.56787  -3.23801  9.72346   1.000 39.57406 ? 148 ARG A N   1 
ATOM   1135 C  CA  . ARG A 1 148 ? 12.97883  -4.38297  8.91844   1.000 43.37924 ? 148 ARG A CA  1 
ATOM   1136 C  C   . ARG A 1 148 ? 13.57413  -3.97982  7.57436   1.000 44.74126 ? 148 ARG A C   1 
ATOM   1137 O  O   . ARG A 1 148 ? 14.14678  -4.83419  6.88744   1.000 48.21244 ? 148 ARG A O   1 
ATOM   1138 C  CB  . ARG A 1 148 ? 11.78836  -5.31372  8.66574   1.000 46.09320 ? 148 ARG A CB  1 
ATOM   1139 C  CG  . ARG A 1 148 ? 11.57225  -6.33520  9.75922   1.000 46.51736 ? 148 ARG A CG  1 
ATOM   1140 C  CD  . ARG A 1 148 ? 10.36607  -5.93317  10.54994  1.000 41.60904 ? 148 ARG A CD  1 
ATOM   1141 N  NE  . ARG A 1 148 ? 10.32562  -6.50117  11.89063  1.000 39.71498 ? 148 ARG A NE  1 
ATOM   1142 C  CZ  . ARG A 1 148 ? 9.81814   -7.69105  12.17812  1.000 38.62277 ? 148 ARG A CZ  1 
ATOM   1143 N  NH1 . ARG A 1 148 ? 9.42464   -8.52658  11.22563  1.000 41.34380 ? 148 ARG A NH1 1 
ATOM   1144 N  NH2 . ARG A 1 148 ? 9.69020   -8.04880  13.45020  1.000 38.86595 ? 148 ARG A NH2 1 
ATOM   1145 N  N   . GLY A 1 149 ? 13.44300  -2.71683  7.17800   1.000 32.85682 ? 149 GLY A N   1 
ATOM   1146 C  CA  . GLY A 1 149 ? 13.96268  -2.24088  5.91049   1.000 38.08286 ? 149 GLY A CA  1 
ATOM   1147 C  C   . GLY A 1 149 ? 12.91040  -1.74468  4.95021   1.000 33.11248 ? 149 GLY A C   1 
ATOM   1148 O  O   . GLY A 1 149 ? 13.25954  -1.16746  3.91035   1.000 39.09872 ? 149 GLY A O   1 
ATOM   1149 N  N   . ALA A 1 150 ? 11.63235  -1.93553  5.24574   1.000 41.57772 ? 150 ALA A N   1 
ATOM   1150 C  CA  . ALA A 1 150 ? 10.58268  -1.55870  4.31931   1.000 33.82420 ? 150 ALA A CA  1 
ATOM   1151 C  C   . ALA A 1 150 ? 10.21500  -0.08661  4.48364   1.000 31.92054 ? 150 ALA A C   1 
ATOM   1152 O  O   . ALA A 1 150 ? 10.39608  0.50784   5.55075   1.000 27.13898 ? 150 ALA A O   1 
ATOM   1153 C  CB  . ALA A 1 150 ? 9.36514   -2.45352  4.53642   1.000 29.08859 ? 150 ALA A CB  1 
ATOM   1154 N  N   . TYR A 1 151 ? 9.70958   0.50490   3.40195   1.000 30.27211 ? 151 TYR A N   1 
ATOM   1155 C  CA  . TYR A 1 151 ? 9.14939   1.85142   3.44816   1.000 34.20350 ? 151 TYR A CA  1 
ATOM   1156 C  C   . TYR A 1 151 ? 7.67438   1.76957   3.82664   1.000 26.75034 ? 151 TYR A C   1 
ATOM   1157 O  O   . TYR A 1 151 ? 6.90542   1.06178   3.17674   1.000 29.65136 ? 151 TYR A O   1 
ATOM   1158 C  CB  . TYR A 1 151 ? 9.30893   2.55150   2.09809   1.000 27.19583 ? 151 TYR A CB  1 
ATOM   1159 C  CG  . TYR A 1 151 ? 8.87048   4.01220   2.10605   1.000 36.75097 ? 151 TYR A CG  1 
ATOM   1160 C  CD1 . TYR A 1 151 ? 9.68566   5.00543   2.64988   1.000 31.78476 ? 151 TYR A CD1 1 
ATOM   1161 C  CD2 . TYR A 1 151 ? 7.62478   4.39028   1.58735   1.000 30.74265 ? 151 TYR A CD2 1 
ATOM   1162 C  CE1 . TYR A 1 151 ? 9.29938   6.33882   2.64867   1.000 34.09468 ? 151 TYR A CE1 1 
ATOM   1163 C  CE2 . TYR A 1 151 ? 7.22745   5.71622   1.58440   1.000 28.29937 ? 151 TYR A CE2 1 
ATOM   1164 C  CZ  . TYR A 1 151 ? 8.06908   6.69005   2.12176   1.000 37.12627 ? 151 TYR A CZ  1 
ATOM   1165 O  OH  . TYR A 1 151 ? 7.68389   8.01525   2.11750   1.000 33.11780 ? 151 TYR A OH  1 
ATOM   1166 N  N   . VAL A 1 152 ? 7.27813   2.49020   4.87347   1.000 31.54972 ? 152 VAL A N   1 
ATOM   1167 C  CA  . VAL A 1 152 ? 5.95268   2.34551   5.47103   1.000 26.21384 ? 152 VAL A CA  1 
ATOM   1168 C  C   . VAL A 1 152 ? 5.11377   3.60007   5.25672   1.000 23.44561 ? 152 VAL A C   1 
ATOM   1169 O  O   . VAL A 1 152 ? 5.57359   4.72373   5.49883   1.000 28.14818 ? 152 VAL A O   1 
ATOM   1170 C  CB  . VAL A 1 152 ? 6.05428   2.02903   6.96728   1.000 31.77146 ? 152 VAL A CB  1 
ATOM   1171 C  CG1 . VAL A 1 152 ? 4.67942   1.63865   7.48056   1.000 20.79987 ? 152 VAL A CG1 1 
ATOM   1172 C  CG2 . VAL A 1 152 ? 7.06209   0.90885   7.18236   1.000 21.07822 ? 152 VAL A CG2 1 
ATOM   1173 N  N   . ILE A 1 153 ? 3.87856   3.40312   4.81378   1.000 24.67667 ? 153 ILE A N   1 
ATOM   1174 C  CA  . ILE A 1 153 ? 2.86826   4.44535   4.78951   1.000 23.73778 ? 153 ILE A CA  1 
ATOM   1175 C  C   . ILE A 1 153 ? 1.83308   4.07989   5.83301   1.000 23.41319 ? 153 ILE A C   1 
ATOM   1176 O  O   . ILE A 1 153 ? 1.39281   2.92697   5.89811   1.000 25.72475 ? 153 ILE A O   1 
ATOM   1177 C  CB  . ILE A 1 153 ? 2.23378   4.58428   3.40585   1.000 25.32514 ? 153 ILE A CB  1 
ATOM   1178 C  CG1 . ILE A 1 153 ? 3.27325   5.14113   2.42719   1.000 34.44984 ? 153 ILE A CG1 1 
ATOM   1179 C  CG2 . ILE A 1 153 ? 1.02132   5.45746   3.49955   1.000 22.29598 ? 153 ILE A CG2 1 
ATOM   1180 C  CD1 . ILE A 1 153 ? 3.59100   4.23230   1.29380   1.000 35.00917 ? 153 ILE A CD1 1 
ATOM   1181 N  N   . THR A 1 154 ? 1.49264   5.02839   6.69101   1.000 23.87056 ? 154 THR A N   1 
ATOM   1182 C  CA  . THR A 1 154 ? 0.61037   4.71366   7.80201   1.000 22.36348 ? 154 THR A CA  1 
ATOM   1183 C  C   . THR A 1 154 ? -0.40083  5.83553   7.91702   1.000 26.39163 ? 154 THR A C   1 
ATOM   1184 O  O   . THR A 1 154 ? -0.06180  7.01667   7.73701   1.000 25.28919 ? 154 THR A O   1 
ATOM   1185 C  CB  . THR A 1 154 ? 1.40481   4.49341   9.09451   1.000 27.01032 ? 154 THR A CB  1 
ATOM   1186 O  OG1 . THR A 1 154 ? 0.51430   4.15750   10.17061  1.000 28.48810 ? 154 THR A OG1 1 
ATOM   1187 C  CG2 . THR A 1 154 ? 2.22356   5.72291   9.45142   1.000 27.09543 ? 154 THR A CG2 1 
ATOM   1188 N  N   . ILE A 1 155 ? -1.66151  5.44811   8.12379   1.000 23.74655 ? 155 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 155 ? -2.77847  6.37618   8.10183   1.000 26.85809 ? 155 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 155 ? -3.25644  6.59636   9.52644   1.000 29.09098 ? 155 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 155 ? -3.38217  5.64034   10.29713  1.000 30.81393 ? 155 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 155 ? -3.90326  5.84197   7.19268   1.000 31.72259 ? 155 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 155 ? -3.36209  5.64323   5.77241   1.000 29.20864 ? 155 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 155 ? -5.07704  6.82384   7.14867   1.000 30.23712 ? 155 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 155 ? -4.12528  4.65099   4.94808   1.000 29.39638 ? 155 ILE A CD1 1 
ATOM   1196 N  N   . GLU A 1 156 ? -3.50898  7.85779   9.88274   1.000 26.24105 ? 156 GLU A N   1 
ATOM   1197 C  CA  . GLU A 1 156 ? -4.05491  8.21556   11.18709  1.000 34.89830 ? 156 GLU A CA  1 
ATOM   1198 C  C   . GLU A 1 156 ? -5.21325  9.17529   10.97596  1.000 36.46118 ? 156 GLU A C   1 
ATOM   1199 O  O   . GLU A 1 156 ? -5.04349  10.24201  10.37566  1.000 35.74394 ? 156 GLU A O   1 
ATOM   1200 C  CB  . GLU A 1 156 ? -2.99785  8.84826   12.10602  1.000 28.25315 ? 156 GLU A CB  1 
ATOM   1201 C  CG  . GLU A 1 156 ? -3.52412  9.16572   13.50711  1.000 32.70624 ? 156 GLU A CG  1 
ATOM   1202 C  CD  . GLU A 1 156 ? -4.52150  8.13134   14.04390  1.000 35.91969 ? 156 GLU A CD  1 
ATOM   1203 O  OE1 . GLU A 1 156 ? -4.21003  6.92074   14.10322  1.000 34.05444 ? 156 GLU A OE1 1 
ATOM   1204 O  OE2 . GLU A 1 156 ? -5.64253  8.53542   14.40452  1.000 39.51523 ? 156 GLU A OE2 1 
ATOM   1205 N  N   . LYS A 1 157 ? -6.39296  8.79007   11.46178  1.000 37.28616 ? 157 LYS A N   1 
ATOM   1206 C  CA  . LYS A 1 157 ? -7.57966  9.60775   11.25771  1.000 34.95736 ? 157 LYS A CA  1 
ATOM   1207 C  C   . LYS A 1 157 ? -7.55364  10.86125  12.11075  1.000 37.37018 ? 157 LYS A C   1 
ATOM   1208 O  O   . LYS A 1 157 ? -8.07258  11.90444  11.69404  1.000 36.74754 ? 157 LYS A O   1 
ATOM   1209 C  CB  . LYS A 1 157 ? -8.83259  8.78841   11.57502  1.000 39.46368 ? 157 LYS A CB  1 
ATOM   1210 C  CG  . LYS A 1 157 ? -10.11023 9.58198   11.51487  1.000 41.36709 ? 157 LYS A CG  1 
ATOM   1211 C  CD  . LYS A 1 157 ? -11.26244 8.76946   10.91608  1.000 53.13799 ? 157 LYS A CD  1 
ATOM   1212 C  CE  . LYS A 1 157 ? -12.16174 9.66790   10.04928  1.000 44.18239 ? 157 LYS A CE  1 
ATOM   1213 N  NZ  . LYS A 1 157 ? -13.32781 8.92131   9.52080   1.000 42.71893 ? 157 LYS A NZ  1 
ATOM   1214 N  N   . ASP A 1 158 ? -6.97823  10.77914  13.31169  1.000 33.33899 ? 158 ASP A N   1 
ATOM   1215 C  CA  . ASP A 1 158 ? -7.14441  11.84073  14.30225  1.000 42.49627 ? 158 ASP A CA  1 
ATOM   1216 C  C   . ASP A 1 158 ? -5.87786  12.67742  14.38808  1.000 37.99687 ? 158 ASP A C   1 
ATOM   1217 O  O   . ASP A 1 158 ? -4.84099  12.16318  14.83150  1.000 38.04333 ? 158 ASP A O   1 
ATOM   1218 C  CB  . ASP A 1 158 ? -7.48016  11.23962  15.66479  1.000 36.77339 ? 158 ASP A CB  1 
ATOM   1219 C  CG  . ASP A 1 158 ? -7.93079  12.26626  16.66450  1.000 42.88700 ? 158 ASP A CG  1 
ATOM   1220 O  OD1 . ASP A 1 158 ? -7.40888  13.40505  16.64461  1.000 46.05555 ? 158 ASP A OD1 1 
ATOM   1221 O  OD2 . ASP A 1 158 ? -8.81440  11.92610  17.48753  1.000 47.14540 ? 158 ASP A OD2 1 
ATOM   1222 N  N   . PRO A 1 159 ? -5.90576  13.95366  14.00962  1.000 39.55991 ? 159 PRO A N   1 
ATOM   1223 C  CA  . PRO A 1 159 ? -4.68382  14.76839  14.12161  1.000 36.25328 ? 159 PRO A CA  1 
ATOM   1224 C  C   . PRO A 1 159 ? -4.17903  14.92642  15.54724  1.000 40.35994 ? 159 PRO A C   1 
ATOM   1225 O  O   . PRO A 1 159 ? -3.02863  15.33394  15.73802  1.000 42.15372 ? 159 PRO A O   1 
ATOM   1226 C  CB  . PRO A 1 159 ? -5.08567  16.11858  13.51321  1.000 40.51499 ? 159 PRO A CB  1 
ATOM   1227 C  CG  . PRO A 1 159 ? -6.56988  16.08761  13.30264  1.000 38.97856 ? 159 PRO A CG  1 
ATOM   1228 C  CD  . PRO A 1 159 ? -7.05461  14.68035  13.42944  1.000 39.73635 ? 159 PRO A CD  1 
ATOM   1229 N  N   . ASN A 1 160 ? -4.99233  14.63040  16.55929  1.000 43.33168 ? 160 ASN A N   1 
ATOM   1230 C  CA  . ASN A 1 160 ? -4.48678  14.70346  17.92550  1.000 41.50778 ? 160 ASN A CA  1 
ATOM   1231 C  C   . ASN A 1 160 ? -3.71275  13.45296  18.31512  1.000 40.44011 ? 160 ASN A C   1 
ATOM   1232 O  O   . ASN A 1 160 ? -2.85622  13.51937  19.20257  1.000 40.65250 ? 160 ASN A O   1 
ATOM   1233 C  CB  . ASN A 1 160 ? -5.63110  14.94886  18.91140  1.000 40.43115 ? 160 ASN A CB  1 
ATOM   1234 C  CG  . ASN A 1 160 ? -6.27966  16.29650  18.71904  1.000 52.71570 ? 160 ASN A CG  1 
ATOM   1235 O  OD1 . ASN A 1 160 ? -5.71473  17.17879  18.07310  1.000 57.92745 ? 160 ASN A OD1 1 
ATOM   1236 N  ND2 . ASN A 1 160 ? -7.47349  16.46710  19.26691  1.000 49.60132 ? 160 ASN A ND2 1 
ATOM   1237 N  N   . VAL A 1 161 ? -4.00834  12.30899  17.68914  1.000 38.50389 ? 161 VAL A N   1 
ATOM   1238 C  CA  . VAL A 1 161 ? -3.18400  11.12336  17.88995  1.000 32.71816 ? 161 VAL A CA  1 
ATOM   1239 C  C   . VAL A 1 161 ? -1.78456  11.37004  17.34436  1.000 40.15178 ? 161 VAL A C   1 
ATOM   1240 O  O   . VAL A 1 161 ? -0.77892  10.99627  17.95999  1.000 37.15690 ? 161 VAL A O   1 
ATOM   1241 C  CB  . VAL A 1 161 ? -3.84332  9.90149   17.22432  1.000 34.48653 ? 161 VAL A CB  1 
ATOM   1242 C  CG1 . VAL A 1 161 ? -2.94381  8.70602   17.30104  1.000 29.45463 ? 161 VAL A CG1 1 
ATOM   1243 C  CG2 . VAL A 1 161 ? -5.16330  9.58838   17.88225  1.000 36.88918 ? 161 VAL A CG2 1 
ATOM   1244 N  N   . ILE A 1 162 ? -1.70740  12.01930  16.18429  1.000 36.10217 ? 162 ILE A N   1 
ATOM   1245 C  CA  . ILE A 1 162 ? -0.43383  12.36092  15.56345  1.000 33.75826 ? 162 ILE A CA  1 
ATOM   1246 C  C   . ILE A 1 162 ? 0.36013   13.28667  16.46217  1.000 37.65193 ? 162 ILE A C   1 
ATOM   1247 O  O   . ILE A 1 162 ? 1.56534   13.09919  16.65941  1.000 41.51181 ? 162 ILE A O   1 
ATOM   1248 C  CB  . ILE A 1 162 ? -0.69352  12.99844  14.18823  1.000 40.01847 ? 162 ILE A CB  1 
ATOM   1249 C  CG1 . ILE A 1 162 ? -1.32095  11.97607  13.25030  1.000 37.75040 ? 162 ILE A CG1 1 
ATOM   1250 C  CG2 . ILE A 1 162 ? 0.58505   13.57168  13.58557  1.000 43.71901 ? 162 ILE A CG2 1 
ATOM   1251 C  CD1 . ILE A 1 162 ? -1.89413  12.58927  12.01745  1.000 32.56861 ? 162 ILE A CD1 1 
ATOM   1252 N  N   . GLU A 1 163 ? -0.30344  14.29819  17.02922  1.000 40.58590 ? 163 GLU A N   1 
ATOM   1253 C  CA  . GLU A 1 163 ? 0.40352   15.25872  17.87072  1.000 40.14784 ? 163 GLU A CA  1 
ATOM   1254 C  C   . GLU A 1 163 ? 0.90191   14.60784  19.15254  1.000 35.07850 ? 163 GLU A C   1 
ATOM   1255 O  O   . GLU A 1 163 ? 2.00504   14.91207  19.61660  1.000 39.37464 ? 163 GLU A O   1 
ATOM   1256 C  CB  . GLU A 1 163 ? -0.49191  16.46062  18.17448  1.000 37.99679 ? 163 GLU A CB  1 
ATOM   1257 C  CG  . GLU A 1 163 ? -0.31235  17.60763  17.19136  1.000 44.74747 ? 163 GLU A CG  1 
ATOM   1258 C  CD  . GLU A 1 163 ? 1.07337   17.60938  16.55161  1.000 55.40475 ? 163 GLU A CD  1 
ATOM   1259 O  OE1 . GLU A 1 163 ? 2.04533   17.94554  17.26691  1.000 57.19500 ? 163 GLU A OE1 1 
ATOM   1260 O  OE2 . GLU A 1 163 ? 1.19573   17.27142  15.34309  1.000 49.56416 ? 163 GLU A OE2 1 
ATOM   1261 N  N   . ILE A 1 164 ? 0.11875   13.69142  19.72516  1.000 41.44987 ? 164 ILE A N   1 
ATOM   1262 C  CA  . ILE A 1 164 ? 0.56776   12.96264  20.91063  1.000 34.37127 ? 164 ILE A CA  1 
ATOM   1263 C  C   . ILE A 1 164 ? 1.73592   12.05102  20.56117  1.000 35.80603 ? 164 ILE A C   1 
ATOM   1264 O  O   . ILE A 1 164 ? 2.69207   11.90712  21.33711  1.000 36.29322 ? 164 ILE A O   1 
ATOM   1265 C  CB  . ILE A 1 164 ? -0.60052  12.16810  21.53071  1.000 29.43294 ? 164 ILE A CB  1 
ATOM   1266 C  CG1 . ILE A 1 164 ? -1.53668  13.08668  22.32209  1.000 41.37965 ? 164 ILE A CG1 1 
ATOM   1267 C  CG2 . ILE A 1 164 ? -0.07877  11.04466  22.41394  1.000 38.71760 ? 164 ILE A CG2 1 
ATOM   1268 C  CD1 . ILE A 1 164 ? -1.14072  13.25693  23.77070  1.000 41.85412 ? 164 ILE A CD1 1 
ATOM   1269 N  N   . ALA A 1 165 ? 1.68005   11.41009  19.39482  1.000 36.47914 ? 165 ALA A N   1 
ATOM   1270 C  CA  . ALA A 1 165 ? 2.81247   10.60186  18.96105  1.000 31.44904 ? 165 ALA A CA  1 
ATOM   1271 C  C   . ALA A 1 165 ? 4.06917   11.43819  18.89634  1.000 26.18220 ? 165 ALA A C   1 
ATOM   1272 O  O   . ALA A 1 165 ? 5.15611   10.93531  19.17614  1.000 28.53625 ? 165 ALA A O   1 
ATOM   1273 C  CB  . ALA A 1 165 ? 2.53162   9.96955   17.60086  1.000 27.82703 ? 165 ALA A CB  1 
ATOM   1274 N  N   . ARG A 1 166 ? 3.91981   12.73470  18.62179  1.000 32.92714 ? 166 ARG A N   1 
ATOM   1275 C  CA  . ARG A 1 166 ? 5.06055   13.61677  18.40042  1.000 37.56495 ? 166 ARG A CA  1 
ATOM   1276 C  C   . ARG A 1 166 ? 5.87184   13.84744  19.66534  1.000 34.08047 ? 166 ARG A C   1 
ATOM   1277 O  O   . ARG A 1 166 ? 7.07617   14.11014  19.58036  1.000 39.45345 ? 166 ARG A O   1 
ATOM   1278 C  CB  . ARG A 1 166 ? 4.57457   14.94689  17.83698  1.000 38.64150 ? 166 ARG A CB  1 
ATOM   1279 C  CG  . ARG A 1 166 ? 5.32397   15.41820  16.60194  1.000 45.38840 ? 166 ARG A CG  1 
ATOM   1280 C  CD  . ARG A 1 166 ? 4.85583   16.80548  16.17169  1.000 49.91190 ? 166 ARG A CD  1 
ATOM   1281 N  NE  . ARG A 1 166 ? 3.82283   16.71100  15.14710  1.000 49.48290 ? 166 ARG A NE  1 
ATOM   1282 C  CZ  . ARG A 1 166 ? 4.06889   16.55770  13.85236  1.000 53.46318 ? 166 ARG A CZ  1 
ATOM   1283 N  NH1 . ARG A 1 166 ? 5.30669   16.55765  13.37784  1.000 54.03484 ? 166 ARG A NH1 1 
ATOM   1284 N  NH2 . ARG A 1 166 ? 3.04929   16.39083  13.01315  1.000 52.73733 ? 166 ARG A NH2 1 
ATOM   1285 N  N   . ILE A 1 167 ? 5.24730   13.76793  20.84273  1.000 37.14446 ? 167 ILE A N   1 
ATOM   1286 C  CA  . ILE A 1 167 ? 5.97582   13.94878  22.09474  1.000 32.25081 ? 167 ILE A CA  1 
ATOM   1287 C  C   . ILE A 1 167 ? 6.30257   12.63327  22.76607  1.000 36.02285 ? 167 ILE A C   1 
ATOM   1288 O  O   . ILE A 1 167 ? 6.91477   12.63222  23.84067  1.000 37.79915 ? 167 ILE A O   1 
ATOM   1289 C  CB  . ILE A 1 167 ? 5.21020   14.87907  23.05897  1.000 45.54178 ? 167 ILE A CB  1 
ATOM   1290 C  CG1 . ILE A 1 167 ? 3.78790   14.37245  23.29846  1.000 36.21744 ? 167 ILE A CG1 1 
ATOM   1291 C  CG2 . ILE A 1 167 ? 5.19996   16.30694  22.52842  1.000 42.68829 ? 167 ILE A CG2 1 
ATOM   1292 C  CD1 . ILE A 1 167 ? 2.85662   15.44026  23.85820  1.000 40.73079 ? 167 ILE A CD1 1 
ATOM   1293 N  N   . ASN A 1 168 ? 5.94728   11.51188  22.14613  1.000 30.63857 ? 168 ASN A N   1 
ATOM   1294 C  CA  . ASN A 1 168 ? 6.26488   10.19284  22.66423  1.000 29.75937 ? 168 ASN A CA  1 
ATOM   1295 C  C   . ASN A 1 168 ? 7.61120   9.73898   22.11321  1.000 31.40110 ? 168 ASN A C   1 
ATOM   1296 O  O   . ASN A 1 168 ? 7.74223   9.56933   20.88986  1.000 30.96319 ? 168 ASN A O   1 
ATOM   1297 C  CB  . ASN A 1 168 ? 5.16890   9.21219   22.26793  1.000 28.07500 ? 168 ASN A CB  1 
ATOM   1298 C  CG  . ASN A 1 168 ? 5.48493   7.79623   22.64077  1.000 27.09146 ? 168 ASN A CG  1 
ATOM   1299 O  OD1 . ASN A 1 168 ? 6.32086   7.55667   23.49572  1.000 31.95795 ? 168 ASN A OD1 1 
ATOM   1300 N  ND2 . ASN A 1 168 ? 4.82029   6.83515   21.99300  1.000 26.71411 ? 168 ASN A ND2 1 
ATOM   1301 N  N   . PRO A 1 169 ? 8.62514   9.52756   22.95295  1.000 31.00296 ? 169 PRO A N   1 
ATOM   1302 C  CA  . PRO A 1 169 ? 9.92335   9.07553   22.42694  1.000 24.34367 ? 169 PRO A CA  1 
ATOM   1303 C  C   . PRO A 1 169 ? 9.85784   7.74644   21.72109  1.000 34.51040 ? 169 PRO A C   1 
ATOM   1304 O  O   . PRO A 1 169 ? 10.78164  7.42735   20.96532  1.000 32.26662 ? 169 PRO A O   1 
ATOM   1305 C  CB  . PRO A 1 169 ? 10.81370  8.99465   23.67604  1.000 35.09147 ? 169 PRO A CB  1 
ATOM   1306 C  CG  . PRO A 1 169 ? 9.88646   9.03041   24.84556  1.000 35.52348 ? 169 PRO A CG  1 
ATOM   1307 C  CD  . PRO A 1 169 ? 8.63452   9.70883   24.41630  1.000 30.85002 ? 169 PRO A CD  1 
ATOM   1308 N  N   . TRP A 1 170 ? 8.79991   6.96116   21.92728  1.000 31.26620 ? 170 TRP A N   1 
ATOM   1309 C  CA  . TRP A 1 170 ? 8.66790   5.66969   21.26682  1.000 33.00748 ? 170 TRP A CA  1 
ATOM   1310 C  C   . TRP A 1 170 ? 8.06122   5.77392   19.87732  1.000 26.51704 ? 170 TRP A C   1 
ATOM   1311 O  O   . TRP A 1 170 ? 8.07854   4.78740   19.13783  1.000 31.74612 ? 170 TRP A O   1 
ATOM   1312 C  CB  . TRP A 1 170 ? 7.80817   4.72671   22.11074  1.000 31.34583 ? 170 TRP A CB  1 
ATOM   1313 C  CG  . TRP A 1 170 ? 8.48898   4.23910   23.34538  1.000 28.58304 ? 170 TRP A CG  1 
ATOM   1314 C  CD1 . TRP A 1 170 ? 8.69950   4.93668   24.49501  1.000 28.47630 ? 170 TRP A CD1 1 
ATOM   1315 C  CD2 . TRP A 1 170 ? 9.02817   2.94019   23.55825  1.000 29.58795 ? 170 TRP A CD2 1 
ATOM   1316 N  NE1 . TRP A 1 170 ? 9.34096   4.14728   25.41940  1.000 27.98676 ? 170 TRP A NE1 1 
ATOM   1317 C  CE2 . TRP A 1 170 ? 9.54772   2.91267   24.86735  1.000 33.73722 ? 170 TRP A CE2 1 
ATOM   1318 C  CE3 . TRP A 1 170 ? 9.11174   1.78784   22.77247  1.000 35.64455 ? 170 TRP A CE3 1 
ATOM   1319 C  CZ2 . TRP A 1 170 ? 10.15671  1.78616   25.40085  1.000 39.25187 ? 170 TRP A CZ2 1 
ATOM   1320 C  CZ3 . TRP A 1 170 ? 9.71874   0.66261   23.30960  1.000 41.96554 ? 170 TRP A CZ3 1 
ATOM   1321 C  CH2 . TRP A 1 170 ? 10.23298  0.67413   24.60400  1.000 41.01873 ? 170 TRP A CH2 1 
ATOM   1322 N  N   . SER A 1 171 ? 7.49850   6.92034   19.51353  1.000 24.96482 ? 171 SER A N   1 
ATOM   1323 C  CA  . SER A 1 171 ? 6.98412   7.13253   18.17287  1.000 28.36334 ? 171 SER A CA  1 
ATOM   1324 C  C   . SER A 1 171 ? 7.92929   7.96294   17.32190  1.000 33.65176 ? 171 SER A C   1 
ATOM   1325 O  O   . SER A 1 171 ? 7.57570   8.31218   16.19036  1.000 34.23213 ? 171 SER A O   1 
ATOM   1326 C  CB  . SER A 1 171 ? 5.61309   7.80581   18.23645  1.000 31.98772 ? 171 SER A CB  1 
ATOM   1327 O  OG  . SER A 1 171 ? 4.70867   7.02766   19.00099  1.000 25.19812 ? 171 SER A OG  1 
ATOM   1328 N  N   . ARG A 1 172 ? 9.13366   8.25354   17.83353  1.000 29.40068 ? 172 ARG A N   1 
ATOM   1329 C  CA  . ARG A 1 172 ? 10.03323  9.22555   17.20564  1.000 30.12217 ? 172 ARG A CA  1 
ATOM   1330 C  C   . ARG A 1 172 ? 10.27489  8.93173   15.72921  1.000 37.96083 ? 172 ARG A C   1 
ATOM   1331 O  O   . ARG A 1 172 ? 10.32907  9.85619   14.90897  1.000 40.71041 ? 172 ARG A O   1 
ATOM   1332 C  CB  . ARG A 1 172 ? 11.36626  9.25631   17.95294  1.000 30.06974 ? 172 ARG A CB  1 
ATOM   1333 C  CG  . ARG A 1 172 ? 11.57540  10.50833  18.78294  1.000 40.99012 ? 172 ARG A CG  1 
ATOM   1334 C  CD  . ARG A 1 172 ? 12.64626  10.34095  19.86416  1.000 42.61656 ? 172 ARG A CD  1 
ATOM   1335 N  NE  . ARG A 1 172 ? 12.53882  11.37557  20.88713  1.000 42.57704 ? 172 ARG A NE  1 
ATOM   1336 C  CZ  . ARG A 1 172 ? 13.09974  11.31674  22.08763  1.000 41.01593 ? 172 ARG A CZ  1 
ATOM   1337 N  NH1 . ARG A 1 172 ? 13.85177  10.29107  22.45358  1.000 41.55114 ? 172 ARG A NH1 1 
ATOM   1338 N  NH2 . ARG A 1 172 ? 12.90045  12.31362  22.94392  1.000 47.17368 ? 172 ARG A NH2 1 
ATOM   1339 N  N   . GLU A 1 173 ? 10.43355  7.65469   15.36748  1.000 29.74489 ? 173 GLU A N   1 
ATOM   1340 C  CA  . GLU A 1 173 ? 10.77742  7.32144   13.99141  1.000 30.45228 ? 173 GLU A CA  1 
ATOM   1341 C  C   . GLU A 1 173 ? 9.65695   7.63632   13.00645  1.000 34.78673 ? 173 GLU A C   1 
ATOM   1342 O  O   . GLU A 1 173 ? 9.90900   7.65722   11.79943  1.000 33.27918 ? 173 GLU A O   1 
ATOM   1343 C  CB  . GLU A 1 173 ? 11.17350  5.85107   13.88962  1.000 31.70384 ? 173 GLU A CB  1 
ATOM   1344 C  CG  . GLU A 1 173 ? 12.34626  5.47273   14.80243  1.000 32.97216 ? 173 GLU A CG  1 
ATOM   1345 C  CD  . GLU A 1 173 ? 11.89992  4.97424   16.16190  1.000 39.93979 ? 173 GLU A CD  1 
ATOM   1346 O  OE1 . GLU A 1 173 ? 10.93364  5.54767   16.72449  1.000 38.11930 ? 173 GLU A OE1 1 
ATOM   1347 O  OE2 . GLU A 1 173 ? 12.52885  4.02155   16.67638  1.000 49.56940 ? 173 GLU A OE2 1 
ATOM   1348 N  N   . LEU A 1 174 ? 8.44047   7.90427   13.47981  1.000 33.55637 ? 174 LEU A N   1 
ATOM   1349 C  CA  . LEU A 1 174 ? 7.41927   8.42712   12.58378  1.000 38.55616 ? 174 LEU A CA  1 
ATOM   1350 C  C   . LEU A 1 174 ? 7.81459   9.77203   11.99215  1.000 38.80040 ? 174 LEU A C   1 
ATOM   1351 O  O   . LEU A 1 174 ? 7.32689   10.12442  10.91426  1.000 35.46350 ? 174 LEU A O   1 
ATOM   1352 C  CB  . LEU A 1 174 ? 6.08165   8.57602   13.31010  1.000 36.44189 ? 174 LEU A CB  1 
ATOM   1353 C  CG  . LEU A 1 174 ? 5.36073   7.35221   13.88412  1.000 36.89363 ? 174 LEU A CG  1 
ATOM   1354 C  CD1 . LEU A 1 174 ? 4.07234   7.82387   14.57470  1.000 30.04606 ? 174 LEU A CD1 1 
ATOM   1355 C  CD2 . LEU A 1 174 ? 5.05274   6.29435   12.81836  1.000 28.31938 ? 174 LEU A CD2 1 
ATOM   1356 N  N   . PHE A 1 175 ? 8.69392   10.52539  12.65703  1.000 40.92133 ? 175 PHE A N   1 
ATOM   1357 C  CA  . PHE A 1 175 ? 8.99136   11.88932  12.24713  1.000 45.96960 ? 175 PHE A CA  1 
ATOM   1358 C  C   . PHE A 1 175 ? 10.46375  12.17930  11.95586  1.000 48.53050 ? 175 PHE A C   1 
ATOM   1359 O  O   . PHE A 1 175 ? 10.77371  13.29697  11.53460  1.000 44.49110 ? 175 PHE A O   1 
ATOM   1360 C  CB  . PHE A 1 175 ? 8.49912   12.88037  13.31217  1.000 41.84266 ? 175 PHE A CB  1 
ATOM   1361 C  CG  . PHE A 1 175 ? 7.14318   12.54945  13.87656  1.000 40.92440 ? 175 PHE A CG  1 
ATOM   1362 C  CD1 . PHE A 1 175 ? 5.98946   12.99020  13.25289  1.000 43.95426 ? 175 PHE A CD1 1 
ATOM   1363 C  CD2 . PHE A 1 175 ? 7.02765   11.82251  15.04436  1.000 35.74984 ? 175 PHE A CD2 1 
ATOM   1364 C  CE1 . PHE A 1 175 ? 4.74438   12.69810  13.78023  1.000 40.41854 ? 175 PHE A CE1 1 
ATOM   1365 C  CE2 . PHE A 1 175 ? 5.78822   11.51586  15.57532  1.000 40.57600 ? 175 PHE A CE2 1 
ATOM   1366 C  CZ  . PHE A 1 175 ? 4.64237   11.95603  14.94341  1.000 36.37461 ? 175 PHE A CZ  1 
ATOM   1367 N  N   . THR A 1 176 ? 11.38405  11.23606  12.17253  1.000 55.46361 ? 176 THR A N   1 
ATOM   1368 C  CA  . THR A 1 176 ? 12.80821  11.51525  11.95437  1.000 61.04869 ? 176 THR A CA  1 
ATOM   1369 C  C   . THR A 1 176 ? 13.15710  11.22935  10.50031  1.000 56.29120 ? 176 THR A C   1 
ATOM   1370 O  O   . THR A 1 176 ? 13.68573  10.17330  10.14569  1.000 58.56630 ? 176 THR A O   1 
ATOM   1371 C  CB  . THR A 1 176 ? 13.69331  10.70380  12.89306  1.000 66.38794 ? 176 THR A CB  1 
ATOM   1372 O  OG1 . THR A 1 176 ? 13.59650  9.30703   12.56406  1.000 62.05792 ? 176 THR A OG1 1 
ATOM   1373 C  CG2 . THR A 1 176 ? 13.31263  10.95145  14.35133  1.000 54.29560 ? 176 THR A CG2 1 
ATOM   1374 N  N   . GLY A 1 177 ? 12.88896  12.21561  9.65559   1.000 57.18877 ? 177 GLY A N   1 
ATOM   1375 C  CA  . GLY A 1 177 ? 13.17218  12.06885  8.24109   1.000 54.73601 ? 177 GLY A CA  1 
ATOM   1376 C  C   . GLY A 1 177 ? 12.17427  11.13030  7.60434   1.000 58.50915 ? 177 GLY A C   1 
ATOM   1377 O  O   . GLY A 1 177 ? 10.96666  11.27835  7.78221   1.000 50.56572 ? 177 GLY A O   1 
ATOM   1378 N  N   . GLY A 1 178 ? 12.68143  10.14994  6.85596   1.000 65.27344 ? 178 GLY A N   1 
ATOM   1379 C  CA  . GLY A 1 178 ? 11.84490  9.17001   6.19808   1.000 49.73639 ? 178 GLY A CA  1 
ATOM   1380 C  C   . GLY A 1 178 ? 12.30546  7.75801   6.51336   1.000 53.81424 ? 178 GLY A C   1 
ATOM   1381 O  O   . GLY A 1 178 ? 13.29867  7.54413   7.21571   1.000 56.24087 ? 178 GLY A O   1 
ATOM   1382 N  N   . LYS A 1 179 ? 11.60643  6.81352   5.88080   1.000 57.17934 ? 179 LYS A N   1 
ATOM   1383 C  CA  . LYS A 1 179 ? 11.45757  5.39335   6.19680   1.000 48.68659 ? 179 LYS A CA  1 
ATOM   1384 C  C   . LYS A 1 179 ? 9.96546   5.18363   6.39274   1.000 33.86477 ? 179 LYS A C   1 
ATOM   1385 O  O   . LYS A 1 179 ? 9.41813   4.15216   6.00430   1.000 35.14063 ? 179 LYS A O   1 
ATOM   1386 C  CB  . LYS A 1 179 ? 12.23084  4.94518   7.43878   1.000 52.15464 ? 179 LYS A CB  1 
ATOM   1387 C  CG  . LYS A 1 179 ? 13.40275  3.96411   7.19782   1.000 55.13369 ? 179 LYS A CG  1 
ATOM   1388 C  CD  . LYS A 1 179 ? 12.93802  2.63147   6.57033   1.000 50.28597 ? 179 LYS A CD  1 
ATOM   1389 C  CE  . LYS A 1 179 ? 14.09233  1.62886   6.45241   1.000 53.12805 ? 179 LYS A CE  1 
ATOM   1390 N  NZ  . LYS A 1 179 ? 15.08666  1.88788   5.36620   1.000 50.95180 ? 179 LYS A NZ  1 
ATOM   1391 N  N   . ILE A 1 180 ? 9.30231   6.18496   6.96879   1.000 31.40850 ? 180 ILE A N   1 
ATOM   1392 C  CA  . ILE A 1 180 ? 7.87805   6.14357   7.28422   1.000 36.82346 ? 180 ILE A CA  1 
ATOM   1393 C  C   . ILE A 1 180 ? 7.26797   7.47679   6.89533   1.000 35.05067 ? 180 ILE A C   1 
ATOM   1394 O  O   . ILE A 1 180 ? 7.86987   8.53419   7.11535   1.000 35.59329 ? 180 ILE A O   1 
ATOM   1395 C  CB  . ILE A 1 180 ? 7.61559   5.87326   8.77928   1.000 32.90376 ? 180 ILE A CB  1 
ATOM   1396 C  CG1 . ILE A 1 180 ? 8.30944   4.58397   9.22191   1.000 30.33980 ? 180 ILE A CG1 1 
ATOM   1397 C  CG2 . ILE A 1 180 ? 6.12082   5.78479   9.06147   1.000 31.27228 ? 180 ILE A CG2 1 
ATOM   1398 C  CD1 . ILE A 1 180 ? 8.02595   4.23632   10.66552  1.000 29.57645 ? 180 ILE A CD1 1 
ATOM   1399 N  N   . GLN A 1 181 ? 6.06703   7.42606   6.32328   1.000 24.51761 ? 181 GLN A N   1 
ATOM   1400 C  CA  . GLN A 1 181 ? 5.34484   8.62063   5.94356   1.000 26.01408 ? 181 GLN A CA  1 
ATOM   1401 C  C   . GLN A 1 181 ? 3.92523   8.53297   6.48270   1.000 28.52480 ? 181 GLN A C   1 
ATOM   1402 O  O   . GLN A 1 181 ? 3.27854   7.48481   6.41851   1.000 35.22411 ? 181 GLN A O   1 
ATOM   1403 C  CB  . GLN A 1 181 ? 5.39227   8.81283   4.42806   1.000 28.47178 ? 181 GLN A CB  1 
ATOM   1404 C  CG  . GLN A 1 181 ? 4.14896   8.51379   3.72583   1.000 25.56258 ? 181 GLN A CG  1 
ATOM   1405 C  CD  . GLN A 1 181 ? 4.19018   8.97687   2.33356   1.000 29.71021 ? 181 GLN A CD  1 
ATOM   1406 O  OE1 . GLN A 1 181 ? 5.26066   9.18284   1.74725   1.000 35.95518 ? 181 GLN A OE1 1 
ATOM   1407 N  NE2 . GLN A 1 181 ? 3.03085   9.18392   1.77595   1.000 31.56177 ? 181 GLN A NE2 1 
ATOM   1408 N  N   . VAL A 1 182 ? 3.45843   9.63575   7.04350   1.000 30.42207 ? 182 VAL A N   1 
ATOM   1409 C  CA  . VAL A 1 182 ? 2.25196   9.65535   7.84810   1.000 28.73720 ? 182 VAL A CA  1 
ATOM   1410 C  C   . VAL A 1 182 ? 1.19640   10.39790  7.06005   1.000 32.83823 ? 182 VAL A C   1 
ATOM   1411 O  O   . VAL A 1 182 ? 1.39354   11.55929  6.68903   1.000 36.44097 ? 182 VAL A O   1 
ATOM   1412 C  CB  . VAL A 1 182 ? 2.49768   10.31295  9.21491   1.000 33.89148 ? 182 VAL A CB  1 
ATOM   1413 C  CG1 . VAL A 1 182 ? 1.19978   10.43541  9.99562   1.000 37.59975 ? 182 VAL A CG1 1 
ATOM   1414 C  CG2 . VAL A 1 182 ? 3.50802   9.50942   10.00901  1.000 31.69282 ? 182 VAL A CG2 1 
ATOM   1415 N  N   . ILE A 1 183 ? 0.08732   9.72507   6.78576   1.000 34.00774 ? 183 ILE A N   1 
ATOM   1416 C  CA  . ILE A 1 183 ? -1.03776  10.32488  6.09220   1.000 31.50299 ? 183 ILE A CA  1 
ATOM   1417 C  C   . ILE A 1 183 ? -2.12255  10.53776  7.12541   1.000 35.24159 ? 183 ILE A C   1 
ATOM   1418 O  O   . ILE A 1 183 ? -2.52346  9.58999   7.81399   1.000 31.65302 ? 183 ILE A O   1 
ATOM   1419 C  CB  . ILE A 1 183 ? -1.54146  9.45566   4.93161   1.000 33.07446 ? 183 ILE A CB  1 
ATOM   1420 C  CG1 . ILE A 1 183 ? -0.46186  9.32309   3.86401   1.000 33.41080 ? 183 ILE A CG1 1 
ATOM   1421 C  CG2 . ILE A 1 183 ? -2.79987  10.07613  4.30402   1.000 35.18424 ? 183 ILE A CG2 1 
ATOM   1422 C  CD1 . ILE A 1 183 ? -0.88270  8.48152   2.67530   1.000 28.84240 ? 183 ILE A CD1 1 
ATOM   1423 N  N   . GLN A 1 184 ? -2.57529  11.77934  7.26676   1.000 34.89676 ? 184 GLN A N   1 
ATOM   1424 C  CA  . GLN A 1 184 ? -3.73070  12.03968  8.10374   1.000 40.28170 ? 184 GLN A CA  1 
ATOM   1425 C  C   . GLN A 1 184 ? -4.96307  11.97359  7.22560   1.000 38.96421 ? 184 GLN A C   1 
ATOM   1426 O  O   . GLN A 1 184 ? -5.05645  12.70000  6.22809   1.000 38.58830 ? 184 GLN A O   1 
ATOM   1427 C  CB  . GLN A 1 184 ? -3.67218  13.39394  8.80212   1.000 36.13603 ? 184 GLN A CB  1 
ATOM   1428 C  CG  . GLN A 1 184 ? -4.71390  13.43336  9.88245   1.000 35.97561 ? 184 GLN A CG  1 
ATOM   1429 C  CD  . GLN A 1 184 ? -5.36602  14.75679  10.04305  1.000 41.89658 ? 184 GLN A CD  1 
ATOM   1430 O  OE1 . GLN A 1 184 ? -4.73461  15.72246  10.49209  1.000 46.99145 ? 184 GLN A OE1 1 
ATOM   1431 N  NE2 . GLN A 1 184 ? -6.65381  14.82564  9.70819   1.000 48.88977 ? 184 GLN A NE2 1 
ATOM   1432 N  N   . GLY A 1 185 ? -5.90260  11.11347  7.59344   1.000 34.90907 ? 185 GLY A N   1 
ATOM   1433 C  CA  . GLY A 1 185 ? -7.14842  11.06394  6.86534   1.000 35.19958 ? 185 GLY A CA  1 
ATOM   1434 C  C   . GLY A 1 185 ? -7.91840  9.80806   7.19634   1.000 36.11021 ? 185 GLY A C   1 
ATOM   1435 O  O   . GLY A 1 185 ? -7.56230  9.05221   8.10399   1.000 34.62230 ? 185 GLY A O   1 
ATOM   1436 N  N   . ASP A 1 186 ? -8.98776  9.60983   6.43644   1.000 36.08474 ? 186 ASP A N   1 
ATOM   1437 C  CA  . ASP A 1 186 ? -9.90128  8.50443   6.66887   1.000 37.39027 ? 186 ASP A CA  1 
ATOM   1438 C  C   . ASP A 1 186 ? -9.47568  7.32432   5.80730   1.000 33.64159 ? 186 ASP A C   1 
ATOM   1439 O  O   . ASP A 1 186 ? -9.51959  7.39344   4.57178   1.000 32.49938 ? 186 ASP A O   1 
ATOM   1440 C  CB  . ASP A 1 186 ? -11.33589 8.92801   6.36987   1.000 39.97913 ? 186 ASP A CB  1 
ATOM   1441 C  CG  . ASP A 1 186 ? -12.28797 7.75648   6.34733   1.000 49.54375 ? 186 ASP A CG  1 
ATOM   1442 O  OD1 . ASP A 1 186 ? -12.59719 7.23605   7.44151   1.000 49.47252 ? 186 ASP A OD1 1 
ATOM   1443 O  OD2 . ASP A 1 186 ? -12.74469 7.37063   5.24619   1.000 53.46805 ? 186 ASP A OD2 1 
ATOM   1444 N  N   . ALA A 1 187 ? -9.06836  6.24243   6.46722   1.000 32.99785 ? 187 ALA A N   1 
ATOM   1445 C  CA  . ALA A 1 187 ? -8.41672  5.13853   5.77231   1.000 30.95955 ? 187 ALA A CA  1 
ATOM   1446 C  C   . ALA A 1 187 ? -9.29962  4.55868   4.68025   1.000 33.08604 ? 187 ALA A C   1 
ATOM   1447 O  O   . ALA A 1 187 ? -8.80282  4.10708   3.64486   1.000 28.16542 ? 187 ALA A O   1 
ATOM   1448 C  CB  . ALA A 1 187 ? -8.04266  4.05510   6.77913   1.000 32.33230 ? 187 ALA A CB  1 
ATOM   1449 N  N   . PHE A 1 188 ? -10.61014 4.52383   4.91123   1.000 32.25384 ? 188 PHE A N   1 
ATOM   1450 C  CA  . PHE A 1 188 ? -11.51966 3.96383   3.92739   1.000 32.40928 ? 188 PHE A CA  1 
ATOM   1451 C  C   . PHE A 1 188 ? -11.51012 4.80320   2.67004   1.000 38.13313 ? 188 PHE A C   1 
ATOM   1452 O  O   . PHE A 1 188 ? -11.64350 4.26984   1.55976   1.000 30.14190 ? 188 PHE A O   1 
ATOM   1453 C  CB  . PHE A 1 188 ? -12.93055 3.89156   4.52616   1.000 37.38992 ? 188 PHE A CB  1 
ATOM   1454 C  CG  . PHE A 1 188 ? -13.99711 3.40713   3.58150   1.000 35.89249 ? 188 PHE A CG  1 
ATOM   1455 C  CD1 . PHE A 1 188 ? -14.60872 4.26961   2.69094   1.000 47.69591 ? 188 PHE A CD1 1 
ATOM   1456 C  CD2 . PHE A 1 188 ? -14.44353 2.09950   3.64450   1.000 42.65072 ? 188 PHE A CD2 1 
ATOM   1457 C  CE1 . PHE A 1 188 ? -15.62519 3.82985   1.85038   1.000 48.73146 ? 188 PHE A CE1 1 
ATOM   1458 C  CE2 . PHE A 1 188 ? -15.45502 1.65189   2.81379   1.000 41.81461 ? 188 PHE A CE2 1 
ATOM   1459 C  CZ  . PHE A 1 188 ? -16.04530 2.51787   1.91530   1.000 48.68163 ? 188 PHE A CZ  1 
ATOM   1460 N  N   . GLU A 1 189 ? -11.35210 6.11576   2.83154   1.000 37.05624 ? 189 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 189 ? -11.30257 6.99461   1.67932   1.000 35.51849 ? 189 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 189 ? -9.88393  7.11048   1.13639   1.000 31.52083 ? 189 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 189 ? -9.70537  7.12586   -0.07973  1.000 38.22910 ? 189 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 189 ? -11.87664 8.36956   2.03738   1.000 37.87184 ? 189 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 189 ? -13.42144 8.41057   2.22238   1.000 38.48353 ? 189 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 189 ? -14.23213 7.95650   0.98614   1.000 49.04702 ? 189 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 189 ? -14.38870 8.74094   0.01963   1.000 44.59217 ? 189 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 189 ? -14.73838 6.81303   0.97941   1.000 45.15869 ? 189 GLU A OE2 1 
ATOM   1469 N  N   . VAL A 1 190 ? -8.86547  7.13784   2.00330   1.000 31.86801 ? 190 VAL A N   1 
ATOM   1470 C  CA  . VAL A 1 190 ? -7.48763  7.29245   1.52728   1.000 33.61148 ? 190 VAL A CA  1 
ATOM   1471 C  C   . VAL A 1 190 ? -7.12041  6.17938   0.55286   1.000 31.52200 ? 190 VAL A C   1 
ATOM   1472 O  O   . VAL A 1 190 ? -6.59318  6.43920   -0.53119  1.000 38.99165 ? 190 VAL A O   1 
ATOM   1473 C  CB  . VAL A 1 190 ? -6.49257  7.34568   2.69936   1.000 26.83944 ? 190 VAL A CB  1 
ATOM   1474 C  CG1 . VAL A 1 190 ? -5.07658  7.17974   2.17378   1.000 28.99873 ? 190 VAL A CG1 1 
ATOM   1475 C  CG2 . VAL A 1 190 ? -6.59229  8.66883   3.43175   1.000 33.31775 ? 190 VAL A CG2 1 
ATOM   1476 N  N   . VAL A 1 191 ? -7.38440  4.92577   0.92273   1.000 30.66110 ? 191 VAL A N   1 
ATOM   1477 C  CA  . VAL A 1 191 ? -6.96961  3.79892   0.08812   1.000 28.45469 ? 191 VAL A CA  1 
ATOM   1478 C  C   . VAL A 1 191 ? -7.52378  3.90926   -1.31992  1.000 42.91291 ? 191 VAL A C   1 
ATOM   1479 O  O   . VAL A 1 191 ? -6.91989  3.39038   -2.27204  1.000 38.55862 ? 191 VAL A O   1 
ATOM   1480 C  CB  . VAL A 1 191 ? -7.38836  2.46882   0.74262   1.000 35.76939 ? 191 VAL A CB  1 
ATOM   1481 C  CG1 . VAL A 1 191 ? -6.60772  2.25520   2.01689   1.000 28.83969 ? 191 VAL A CG1 1 
ATOM   1482 C  CG2 . VAL A 1 191 ? -8.88499  2.47070   1.01340   1.000 28.10054 ? 191 VAL A CG2 1 
ATOM   1483 N  N   . LYS A 1 192 ? -8.66853  4.59198   -1.48407  1.000 40.94791 ? 192 LYS A N   1 
ATOM   1484 C  CA  . LYS A 1 192 ? -9.24473  4.78632   -2.81058  1.000 34.84980 ? 192 LYS A CA  1 
ATOM   1485 C  C   . LYS A 1 192 ? -8.30545  5.56231   -3.72125  1.000 40.24973 ? 192 LYS A C   1 
ATOM   1486 O  O   . LYS A 1 192 ? -8.23618  5.28563   -4.92109  1.000 37.36011 ? 192 LYS A O   1 
ATOM   1487 C  CB  . LYS A 1 192 ? -10.58266 5.52194   -2.71235  1.000 41.16003 ? 192 LYS A CB  1 
ATOM   1488 C  CG  . LYS A 1 192 ? -11.73368 4.67876   -2.21822  1.000 43.96392 ? 192 LYS A CG  1 
ATOM   1489 C  CD  . LYS A 1 192 ? -13.05383 5.33018   -2.57617  1.000 41.77814 ? 192 LYS A CD  1 
ATOM   1490 C  CE  . LYS A 1 192 ? -14.10454 5.04974   -1.50875  1.000 48.23859 ? 192 LYS A CE  1 
ATOM   1491 N  NZ  . LYS A 1 192 ? -15.05191 6.19820   -1.34605  1.000 49.40563 ? 192 LYS A NZ  1 
ATOM   1492 N  N   A LYS A 1 193 ? -7.57067  6.53462   -3.17282  0.586 39.20042 ? 193 LYS A N   1 
ATOM   1493 N  N   B LYS A 1 193 ? -7.58080  6.54300   -3.17430  0.414 39.20738 ? 193 LYS A N   1 
ATOM   1494 C  CA  A LYS A 1 193 ? -6.65730  7.35518   -3.96275  0.586 40.65456 ? 193 LYS A CA  1 
ATOM   1495 C  CA  B LYS A 1 193 ? -6.66981  7.32144   -4.00798  0.414 40.63050 ? 193 LYS A CA  1 
ATOM   1496 C  C   A LYS A 1 193 ? -5.25092  6.75813   -4.05385  0.586 42.13084 ? 193 LYS A C   1 
ATOM   1497 C  C   B LYS A 1 193 ? -5.42942  6.51934   -4.37943  0.414 41.80863 ? 193 LYS A C   1 
ATOM   1498 O  O   A LYS A 1 193 ? -4.34085  7.41343   -4.57678  0.586 38.85559 ? 193 LYS A O   1 
ATOM   1499 O  O   B LYS A 1 193 ? -4.81172  6.78460   -5.41846  0.414 41.08902 ? 193 LYS A O   1 
ATOM   1500 C  CB  A LYS A 1 193 ? -6.59555  8.78804   -3.40134  0.586 43.95709 ? 193 LYS A CB  1 
ATOM   1501 C  CB  B LYS A 1 193 ? -6.26432  8.61842   -3.29649  0.414 43.14910 ? 193 LYS A CB  1 
ATOM   1502 C  CG  A LYS A 1 193 ? -6.07080  8.91270   -1.96596  0.586 39.57644 ? 193 LYS A CG  1 
ATOM   1503 C  CG  B LYS A 1 193 ? -4.75042  8.78173   -3.08808  0.414 43.43700 ? 193 LYS A CG  1 
ATOM   1504 C  CD  A LYS A 1 193 ? -4.83912  9.81815   -1.84130  0.586 45.79958 ? 193 LYS A CD  1 
ATOM   1505 C  CD  B LYS A 1 193 ? -4.26746  10.19760  -3.38519  0.414 40.93441 ? 193 LYS A CD  1 
ATOM   1506 C  CE  A LYS A 1 193 ? -3.93347  9.35613   -0.69879  0.586 37.05387 ? 193 LYS A CE  1 
ATOM   1507 C  CE  B LYS A 1 193 ? -2.75666  10.23815  -3.59749  0.414 41.02614 ? 193 LYS A CE  1 
ATOM   1508 N  NZ  A LYS A 1 193 ? -3.46298  10.48098  0.16969   0.586 36.28036 ? 193 LYS A NZ  1 
ATOM   1509 N  NZ  B LYS A 1 193 ? -2.03378  9.14602   -2.88277  0.414 36.44450 ? 193 LYS A NZ  1 
ATOM   1510 N  N   . PHE A 1 194 ? -5.05704  5.54009   -3.55307  1.000 39.97607 ? 194 PHE A N   1 
ATOM   1511 C  CA  . PHE A 1 194 ? -3.82154  4.80609   -3.77455  1.000 40.35870 ? 194 PHE A CA  1 
ATOM   1512 C  C   . PHE A 1 194 ? -3.84605  4.12776   -5.13661  1.000 44.10775 ? 194 PHE A C   1 
ATOM   1513 O  O   . PHE A 1 194 ? -4.88937  3.65447   -5.59418  1.000 35.00119 ? 194 PHE A O   1 
ATOM   1514 C  CB  . PHE A 1 194 ? -3.62731  3.76400   -2.68755  1.000 35.60379 ? 194 PHE A CB  1 
ATOM   1515 C  CG  . PHE A 1 194 ? -3.14721  4.33201   -1.38952  1.000 36.81256 ? 194 PHE A CG  1 
ATOM   1516 C  CD1 . PHE A 1 194 ? -2.55323  5.57877   -1.34434  1.000 40.79109 ? 194 PHE A CD1 1 
ATOM   1517 C  CD2 . PHE A 1 194 ? -3.30619  3.62928   -0.21470  1.000 37.74390 ? 194 PHE A CD2 1 
ATOM   1518 C  CE1 . PHE A 1 194 ? -2.11783  6.10066   -0.16148  1.000 32.12961 ? 194 PHE A CE1 1 
ATOM   1519 C  CE2 . PHE A 1 194 ? -2.87903  4.15816   0.97445   1.000 26.65593 ? 194 PHE A CE2 1 
ATOM   1520 C  CZ  . PHE A 1 194 ? -2.29407  5.39241   1.00194   1.000 25.05064 ? 194 PHE A CZ  1 
ATOM   1521 N  N   . LYS A 1 195 ? -2.68888  4.08173   -5.78826  1.000 42.91244 ? 195 LYS A N   1 
ATOM   1522 C  CA  . LYS A 1 195 ? -2.61321  3.40796   -7.07826  1.000 48.96780 ? 195 LYS A CA  1 
ATOM   1523 C  C   . LYS A 1 195 ? -2.67497  1.89222   -6.89513  1.000 40.76328 ? 195 LYS A C   1 
ATOM   1524 O  O   . LYS A 1 195 ? -2.27127  1.34952   -5.85992  1.000 35.50418 ? 195 LYS A O   1 
ATOM   1525 C  CB  . LYS A 1 195 ? -1.33075  3.79904   -7.81948  1.000 40.16755 ? 195 LYS A CB  1 
ATOM   1526 C  CG  . LYS A 1 195 ? -0.94783  5.28997   -7.77056  1.000 42.96154 ? 195 LYS A CG  1 
ATOM   1527 C  CD  . LYS A 1 195 ? -2.12344  6.21511   -8.08389  1.000 50.92893 ? 195 LYS A CD  1 
ATOM   1528 C  CE  . LYS A 1 195 ? -1.75924  7.21678   -9.20574  1.000 46.94650 ? 195 LYS A CE  1 
ATOM   1529 N  NZ  . LYS A 1 195 ? -1.01761  8.42179   -8.70017  1.000 58.94369 ? 195 LYS A NZ  1 
ATOM   1530 N  N   . GLN A 1 196 ? -3.20090  1.21267   -7.91234  1.000 38.77356 ? 196 GLN A N   1 
ATOM   1531 C  CA  . GLN A 1 196 ? -3.22438  -0.24568  -7.92032  1.000 42.96754 ? 196 GLN A CA  1 
ATOM   1532 C  C   . GLN A 1 196 ? -1.81105  -0.81837  -7.85089  1.000 41.30457 ? 196 GLN A C   1 
ATOM   1533 O  O   . GLN A 1 196 ? -0.85068  -0.22664  -8.35434  1.000 44.28355 ? 196 GLN A O   1 
ATOM   1534 C  CB  . GLN A 1 196 ? -3.91704  -0.76592  -9.18171  1.000 42.66669 ? 196 GLN A CB  1 
ATOM   1535 C  CG  . GLN A 1 196 ? -4.05929  -2.29532  -9.19559  1.000 45.64011 ? 196 GLN A CG  1 
ATOM   1536 C  CD  . GLN A 1 196 ? -4.72476  -2.84334  -10.44157 1.000 54.57203 ? 196 GLN A CD  1 
ATOM   1537 O  OE1 . GLN A 1 196 ? -4.10730  -3.58381  -11.20274 1.000 57.52072 ? 196 GLN A OE1 1 
ATOM   1538 N  NE2 . GLN A 1 196 ? -6.00064  -2.51209  -10.63645 1.000 45.78041 ? 196 GLN A NE2 1 
ATOM   1539 N  N   . ALA A 1 197 ? -1.70397  -1.99100  -7.22771  1.000 40.53926 ? 197 ALA A N   1 
ATOM   1540 C  CA  . ALA A 1 197 ? -0.44695  -2.71676  -7.02871  1.000 39.02173 ? 197 ALA A CA  1 
ATOM   1541 C  C   . ALA A 1 197 ? 0.67173   -1.77682  -6.58191  1.000 40.20284 ? 197 ALA A C   1 
ATOM   1542 O  O   . ALA A 1 197 ? 1.72218   -1.65726  -7.21182  1.000 41.93770 ? 197 ALA A O   1 
ATOM   1543 C  CB  . ALA A 1 197 ? -0.05644  -3.48436  -8.28367  1.000 43.13083 ? 197 ALA A CB  1 
ATOM   1544 N  N   . SER A 1 198 ? 0.40825   -1.10266  -5.46142  1.000 37.28863 ? 198 SER A N   1 
ATOM   1545 C  CA  . SER A 1 198 ? 1.29001   -0.15456  -4.79106  1.000 36.62657 ? 198 SER A CA  1 
ATOM   1546 C  C   . SER A 1 198 ? 2.15015   -0.81711  -3.72316  1.000 36.14258 ? 198 SER A C   1 
ATOM   1547 O  O   . SER A 1 198 ? 3.31504   -0.44883  -3.53701  1.000 36.09679 ? 198 SER A O   1 
ATOM   1548 C  CB  . SER A 1 198 ? 0.44879   0.92428   -4.09329  1.000 39.19312 ? 198 SER A CB  1 
ATOM   1549 O  OG  . SER A 1 198 ? 0.20932   2.05570   -4.89660  1.000 48.06263 ? 198 SER A OG  1 
ATOM   1550 N  N   . PHE A 1 199 ? 1.56967   -1.76378  -2.99104  1.000 31.33234 ? 199 PHE A N   1 
ATOM   1551 C  CA  . PHE A 1 199 ? 2.07986   -2.19981  -1.70447  1.000 27.39080 ? 199 PHE A CA  1 
ATOM   1552 C  C   . PHE A 1 199 ? 2.43548   -3.67217  -1.72494  1.000 29.04393 ? 199 PHE A C   1 
ATOM   1553 O  O   . PHE A 1 199 ? 1.64837   -4.50286  -2.18785  1.000 33.52126 ? 199 PHE A O   1 
ATOM   1554 C  CB  . PHE A 1 199 ? 1.05425   -1.96017  -0.60367  1.000 25.63805 ? 199 PHE A CB  1 
ATOM   1555 C  CG  . PHE A 1 199 ? 0.78062   -0.53208  -0.36056  1.000 27.66633 ? 199 PHE A CG  1 
ATOM   1556 C  CD1 . PHE A 1 199 ? 1.71569   0.25094   0.28368   1.000 25.04700 ? 199 PHE A CD1 1 
ATOM   1557 C  CD2 . PHE A 1 199 ? -0.40686  0.04088   -0.77865  1.000 26.97473 ? 199 PHE A CD2 1 
ATOM   1558 C  CE1 . PHE A 1 199 ? 1.46527   1.58216   0.51673   1.000 27.28383 ? 199 PHE A CE1 1 
ATOM   1559 C  CE2 . PHE A 1 199 ? -0.65566  1.36642   -0.54762  1.000 28.77406 ? 199 PHE A CE2 1 
ATOM   1560 C  CZ  . PHE A 1 199 ? 0.28577   2.14185   0.09752   1.000 29.75562 ? 199 PHE A CZ  1 
ATOM   1561 N  N   . ASP A 1 200 ? 3.60218   -3.98667  -1.17341  1.000 25.92529 ? 200 ASP A N   1 
ATOM   1562 C  CA  . ASP A 1 200 ? 3.97869   -5.37702  -0.95678  1.000 28.86228 ? 200 ASP A CA  1 
ATOM   1563 C  C   . ASP A 1 200 ? 3.22749   -6.00044  0.20965   1.000 30.26937 ? 200 ASP A C   1 
ATOM   1564 O  O   . ASP A 1 200 ? 2.91895   -7.19608  0.17920   1.000 30.04204 ? 200 ASP A O   1 
ATOM   1565 C  CB  . ASP A 1 200 ? 5.47543   -5.44841  -0.71869  1.000 27.06301 ? 200 ASP A CB  1 
ATOM   1566 C  CG  . ASP A 1 200 ? 6.25092   -4.99712  -1.92365  1.000 35.98692 ? 200 ASP A CG  1 
ATOM   1567 O  OD1 . ASP A 1 200 ? 6.43156   -5.82920  -2.83757  1.000 41.37271 ? 200 ASP A OD1 1 
ATOM   1568 O  OD2 . ASP A 1 200 ? 6.65958   -3.81699  -1.97074  1.000 35.72803 ? 200 ASP A OD2 1 
ATOM   1569 N  N   . VAL A 1 201 ? 2.96662   -5.24067  1.27130   1.000 34.06675 ? 201 VAL A N   1 
ATOM   1570 C  CA  . VAL A 1 201 ? 2.21613   -5.78966  2.39184   1.000 27.83730 ? 201 VAL A CA  1 
ATOM   1571 C  C   . VAL A 1 201 ? 1.32464   -4.70431  2.97018   1.000 25.59516 ? 201 VAL A C   1 
ATOM   1572 O  O   . VAL A 1 201 ? 1.60685   -3.50754  2.85767   1.000 29.14799 ? 201 VAL A O   1 
ATOM   1573 C  CB  . VAL A 1 201 ? 3.12023   -6.42438  3.48767   1.000 33.04969 ? 201 VAL A CB  1 
ATOM   1574 C  CG1 . VAL A 1 201 ? 4.53236   -6.57515  3.04164   1.000 22.54997 ? 201 VAL A CG1 1 
ATOM   1575 C  CG2 . VAL A 1 201 ? 3.03987   -5.67166  4.78303   1.000 26.45496 ? 201 VAL A CG2 1 
ATOM   1576 N  N   . ILE A 1 202 ? 0.21099   -5.14118  3.55483   1.000 21.81216 ? 202 ILE A N   1 
ATOM   1577 C  CA  . ILE A 1 202 ? -0.71986  -4.27465  4.25227   1.000 20.16672 ? 202 ILE A CA  1 
ATOM   1578 C  C   . ILE A 1 202 ? -0.90689  -4.85589  5.64362   1.000 20.30817 ? 202 ILE A C   1 
ATOM   1579 O  O   . ILE A 1 202 ? -1.07808  -6.07202  5.79083   1.000 25.34748 ? 202 ILE A O   1 
ATOM   1580 C  CB  . ILE A 1 202 ? -2.06978  -4.18890  3.52202   1.000 20.85786 ? 202 ILE A CB  1 
ATOM   1581 C  CG1 . ILE A 1 202 ? -1.92949  -3.47964  2.18281   1.000 20.23051 ? 202 ILE A CG1 1 
ATOM   1582 C  CG2 . ILE A 1 202 ? -3.12869  -3.45638  4.37840   1.000 22.66641 ? 202 ILE A CG2 1 
ATOM   1583 C  CD1 . ILE A 1 202 ? -3.18591  -3.61718  1.35960   1.000 21.28203 ? 202 ILE A CD1 1 
ATOM   1584 N  N   . ILE A 1 203 ? -0.85865  -4.00739  6.66048   1.000 20.65909 ? 203 ILE A N   1 
ATOM   1585 C  CA  . ILE A 1 203 ? -1.15990  -4.42705  8.02455   1.000 18.75308 ? 203 ILE A CA  1 
ATOM   1586 C  C   . ILE A 1 203 ? -2.41116  -3.68086  8.44380   1.000 21.17931 ? 203 ILE A C   1 
ATOM   1587 O  O   . ILE A 1 203 ? -2.39601  -2.45171  8.60435   1.000 21.06051 ? 203 ILE A O   1 
ATOM   1588 C  CB  . ILE A 1 203 ? -0.00544  -4.17303  8.98993   1.000 21.96684 ? 203 ILE A CB  1 
ATOM   1589 C  CG1 . ILE A 1 203 ? 1.19240   -5.04034  8.59437   1.000 20.66101 ? 203 ILE A CG1 1 
ATOM   1590 C  CG2 . ILE A 1 203 ? -0.43119  -4.49406  10.40059  1.000 17.56023 ? 203 ILE A CG2 1 
ATOM   1591 C  CD1 . ILE A 1 203 ? 2.50728   -4.45388  8.96974   1.000 20.76987 ? 203 ILE A CD1 1 
ATOM   1592 N  N   . HIS A 1 204 ? -3.50617  -4.41526  8.59118   1.000 19.88148 ? 204 HIS A N   1 
ATOM   1593 C  CA  . HIS A 1 204 ? -4.80901  -3.82120  8.87029   1.000 18.94454 ? 204 HIS A CA  1 
ATOM   1594 C  C   . HIS A 1 204 ? -5.13565  -4.13378  10.31923  1.000 21.92427 ? 204 HIS A C   1 
ATOM   1595 O  O   . HIS A 1 204 ? -5.38821  -5.29173  10.66011  1.000 26.55630 ? 204 HIS A O   1 
ATOM   1596 C  CB  . HIS A 1 204 ? -5.86067  -4.37741  7.92837   1.000 17.43445 ? 204 HIS A CB  1 
ATOM   1597 C  CG  . HIS A 1 204 ? -7.19874  -3.70922  8.04447   1.000 23.88857 ? 204 HIS A CG  1 
ATOM   1598 N  ND1 . HIS A 1 204 ? -7.34903  -2.34533  8.18583   1.000 17.93122 ? 204 HIS A ND1 1 
ATOM   1599 C  CD2 . HIS A 1 204 ? -8.44549  -4.22470  8.03201   1.000 19.14312 ? 204 HIS A CD2 1 
ATOM   1600 C  CE1 . HIS A 1 204 ? -8.63318  -2.05511  8.24919   1.000 22.47073 ? 204 HIS A CE1 1 
ATOM   1601 N  NE2 . HIS A 1 204 ? -9.31879  -3.18000  8.16720   1.000 21.58277 ? 204 HIS A NE2 1 
ATOM   1602 N  N   . ASP A 1 205 ? -5.12944  -3.10386  11.16431  1.000 24.44609 ? 205 ASP A N   1 
ATOM   1603 C  CA  . ASP A 1 205 ? -5.38295  -3.22210  12.60316  1.000 22.49326 ? 205 ASP A CA  1 
ATOM   1604 C  C   . ASP A 1 205 ? -6.45636  -2.22709  13.01157  1.000 28.11571 ? 205 ASP A C   1 
ATOM   1605 O  O   . ASP A 1 205 ? -6.17365  -1.26861  13.74022  1.000 30.54816 ? 205 ASP A O   1 
ATOM   1606 C  CB  . ASP A 1 205 ? -4.09967  -2.95314  13.39632  1.000 33.24490 ? 205 ASP A CB  1 
ATOM   1607 C  CG  . ASP A 1 205 ? -4.15654  -3.48534  14.81894  1.000 33.79797 ? 205 ASP A CG  1 
ATOM   1608 O  OD1 . ASP A 1 205 ? -5.22452  -3.99877  15.20687  1.000 33.89827 ? 205 ASP A OD1 1 
ATOM   1609 O  OD2 . ASP A 1 205 ? -3.13703  -3.37178  15.54141  1.000 26.64594 ? 205 ASP A OD2 1 
ATOM   1610 N  N   . PRO A 1 206 ? -7.70177  -2.42813  12.57581  1.000 24.55442 ? 206 PRO A N   1 
ATOM   1611 C  CA  . PRO A 1 206 ? -8.73080  -1.39794  12.75396  1.000 30.21056 ? 206 PRO A CA  1 
ATOM   1612 C  C   . PRO A 1 206 ? -9.27281  -1.38711  14.17203  1.000 33.71894 ? 206 PRO A C   1 
ATOM   1613 O  O   . PRO A 1 206 ? -9.00568  -2.30911  14.95804  1.000 28.48044 ? 206 PRO A O   1 
ATOM   1614 C  CB  . PRO A 1 206 ? -9.82303  -1.82744  11.76106  1.000 23.99489 ? 206 PRO A CB  1 
ATOM   1615 C  CG  . PRO A 1 206 ? -9.75135  -3.30415  11.78210  1.000 24.05919 ? 206 PRO A CG  1 
ATOM   1616 C  CD  . PRO A 1 206 ? -8.24747  -3.62677  11.90934  1.000 25.41967 ? 206 PRO A CD  1 
ATOM   1617 N  N   . PRO A 1 207 ? -10.05748 -0.36757  14.52835  1.000 33.81177 ? 207 PRO A N   1 
ATOM   1618 C  CA  . PRO A 1 207 ? -10.86029 -0.43652  15.75568  1.000 32.53490 ? 207 PRO A CA  1 
ATOM   1619 C  C   . PRO A 1 207 ? -11.82674 -1.61144  15.71535  1.000 36.94578 ? 207 PRO A C   1 
ATOM   1620 O  O   . PRO A 1 207 ? -11.99292 -2.29850  14.70333  1.000 29.46729 ? 207 PRO A O   1 
ATOM   1621 C  CB  . PRO A 1 207 ? -11.61342 0.89572   15.77242  1.000 41.44653 ? 207 PRO A CB  1 
ATOM   1622 C  CG  . PRO A 1 207 ? -10.86375 1.80263   14.79142  1.000 34.59060 ? 207 PRO A CG  1 
ATOM   1623 C  CD  . PRO A 1 207 ? -10.25605 0.89203   13.78333  1.000 30.91872 ? 207 PRO A CD  1 
ATOM   1624 N  N   . ARG A 1 208 ? -12.47960 -1.84207  16.85067  1.000 37.53292 ? 208 ARG A N   1 
ATOM   1625 C  CA  . ARG A 1 208 ? -13.40169 -2.96237  16.95970  1.000 37.68258 ? 208 ARG A CA  1 
ATOM   1626 C  C   . ARG A 1 208 ? -14.55058 -2.80597  15.96779  1.000 36.72113 ? 208 ARG A C   1 
ATOM   1627 O  O   . ARG A 1 208 ? -14.95438 -1.69121  15.63224  1.000 34.56074 ? 208 ARG A O   1 
ATOM   1628 C  CB  . ARG A 1 208 ? -13.97370 -3.05494  18.38092  1.000 43.30702 ? 208 ARG A CB  1 
ATOM   1629 C  CG  . ARG A 1 208 ? -12.99836 -3.30101  19.57081  1.000 56.05560 ? 208 ARG A CG  1 
ATOM   1630 C  CD  . ARG A 1 208 ? -12.20752 -4.64011  19.58820  1.000 61.37230 ? 208 ARG A CD  1 
ATOM   1631 N  NE  . ARG A 1 208 ? -11.56231 -5.01850  18.33280  1.000 58.14296 ? 208 ARG A NE  1 
ATOM   1632 C  CZ  . ARG A 1 208 ? -10.26934 -4.84805  18.08389  1.000 51.54225 ? 208 ARG A CZ  1 
ATOM   1633 N  NH1 . ARG A 1 208 ? -9.45582  -4.32114  18.98656  1.000 58.73438 ? 208 ARG A NH1 1 
ATOM   1634 N  NH2 . ARG A 1 208 ? -9.78054  -5.21337  16.90400  1.000 41.99625 ? 208 ARG A NH2 1 
ATOM   1635 N  N   . PHE A 1 209 ? -15.07962 -3.94281  15.50392  1.000 39.33283 ? 209 PHE A N   1 
ATOM   1636 C  CA  . PHE A 1 209 ? -16.23430 -4.00214  14.60208  1.000 36.40562 ? 209 PHE A CA  1 
ATOM   1637 C  C   . PHE A 1 209 ? -17.28356 -2.93220  14.84014  1.000 40.45899 ? 209 PHE A C   1 
ATOM   1638 O  O   . PHE A 1 209 ? -17.61060 -2.16500  13.93097  1.000 40.93124 ? 209 PHE A O   1 
ATOM   1639 C  CB  . PHE A 1 209 ? -16.92658 -5.35335  14.71541  1.000 42.40119 ? 209 PHE A CB  1 
ATOM   1640 C  CG  . PHE A 1 209 ? -17.55695 -5.82569  13.44213  1.000 42.69677 ? 209 PHE A CG  1 
ATOM   1641 C  CD1 . PHE A 1 209 ? -16.86879 -5.82832  12.25628  1.000 44.44098 ? 209 PHE A CD1 1 
ATOM   1642 C  CD2 . PHE A 1 209 ? -18.89201 -6.22801  13.44181  1.000 52.96142 ? 209 PHE A CD2 1 
ATOM   1643 C  CE1 . PHE A 1 209 ? -17.48933 -6.26273  11.08205  1.000 44.81478 ? 209 PHE A CE1 1 
ATOM   1644 C  CE2 . PHE A 1 209 ? -19.51724 -6.66565  12.27775  1.000 52.16456 ? 209 PHE A CE2 1 
ATOM   1645 C  CZ  . PHE A 1 209 ? -18.80494 -6.67625  11.09095  1.000 55.06619 ? 209 PHE A CZ  1 
ATOM   1646 N  N   . SER A 1 210 ? -17.82673 -2.89153  16.05883  1.000 43.60129 ? 210 SER A N   1 
ATOM   1647 C  CA  . SER A 1 210 ? -18.96929 -2.02998  16.34634  1.000 46.30756 ? 210 SER A CA  1 
ATOM   1648 C  C   . SER A 1 210 ? -18.64994 -0.55529  16.16305  1.000 38.52843 ? 210 SER A C   1 
ATOM   1649 O  O   . SER A 1 210 ? -19.56592 0.23881   15.93445  1.000 55.57446 ? 210 SER A O   1 
ATOM   1650 C  CB  . SER A 1 210 ? -19.46756 -2.28098  17.76870  1.000 45.57764 ? 210 SER A CB  1 
ATOM   1651 O  OG  . SER A 1 210 ? -18.40313 -2.16199  18.70058  1.000 45.54664 ? 210 SER A OG  1 
ATOM   1652 N  N   . LEU A 1 211 ? -17.38176 -0.17042  16.24468  1.000 43.51109 ? 211 LEU A N   1 
ATOM   1653 C  CA  . LEU A 1 211 ? -16.99633 1.22244   16.06337  1.000 49.94918 ? 211 LEU A CA  1 
ATOM   1654 C  C   . LEU A 1 211 ? -16.33009 1.50766   14.71842  1.000 45.97012 ? 211 LEU A C   1 
ATOM   1655 O  O   . LEU A 1 211 ? -16.08766 2.68268   14.40944  1.000 46.81627 ? 211 LEU A O   1 
ATOM   1656 C  CB  . LEU A 1 211 ? -16.06830 1.67272   17.20983  1.000 49.36709 ? 211 LEU A CB  1 
ATOM   1657 C  CG  . LEU A 1 211 ? -16.42656 1.15656   18.61807  1.000 53.04934 ? 211 LEU A CG  1 
ATOM   1658 C  CD1 . LEU A 1 211 ? -15.21566 1.10307   19.58042  1.000 45.45010 ? 211 LEU A CD1 1 
ATOM   1659 C  CD2 . LEU A 1 211 ? -17.58536 1.95215   19.22229  1.000 42.37421 ? 211 LEU A CD2 1 
ATOM   1660 N  N   . ALA A 1 212 ? -16.04753 0.48662   13.90712  1.000 46.99982 ? 212 ALA A N   1 
ATOM   1661 C  CA  . ALA A 1 212 ? -15.34864 0.68822   12.63407  1.000 33.74110 ? 212 ALA A CA  1 
ATOM   1662 C  C   . ALA A 1 212 ? -15.81740 -0.33018  11.59473  1.000 35.89275 ? 212 ALA A C   1 
ATOM   1663 O  O   . ALA A 1 212 ? -15.01269 -0.95499  10.90352  1.000 37.20489 ? 212 ALA A O   1 
ATOM   1664 C  CB  . ALA A 1 212 ? -13.83407 0.60736   12.82597  1.000 33.26493 ? 212 ALA A CB  1 
ATOM   1665 N  N   . GLY A 1 213 ? -17.13754 -0.49141  11.45807  1.000 38.37144 ? 213 GLY A N   1 
ATOM   1666 C  CA  . GLY A 1 213 ? -17.66994 -1.54041  10.59722  1.000 34.44353 ? 213 GLY A CA  1 
ATOM   1667 C  C   . GLY A 1 213 ? -17.21334 -1.42925  9.15460   1.000 30.73173 ? 213 GLY A C   1 
ATOM   1668 O  O   . GLY A 1 213 ? -16.97799 -2.44382  8.48931   1.000 31.37074 ? 213 GLY A O   1 
ATOM   1669 N  N   . HIS A 1 214 ? -17.04860 -0.19812  8.65876   1.000 33.66155 ? 214 HIS A N   1 
ATOM   1670 C  CA  . HIS A 1 214 ? -16.68451 -0.00930  7.25622   1.000 38.31212 ? 214 HIS A CA  1 
ATOM   1671 C  C   . HIS A 1 214 ? -15.26579 -0.48295  6.94936   1.000 31.06017 ? 214 HIS A C   1 
ATOM   1672 O  O   . HIS A 1 214 ? -14.95604 -0.73508  5.78297   1.000 29.54642 ? 214 HIS A O   1 
ATOM   1673 C  CB  . HIS A 1 214 ? -16.85307 1.46275   6.85732   1.000 35.12159 ? 214 HIS A CB  1 
ATOM   1674 C  CG  . HIS A 1 214 ? -16.01606 2.40598   7.66534   1.000 33.29026 ? 214 HIS A CG  1 
ATOM   1675 N  ND1 . HIS A 1 214 ? -16.31717 2.73508   8.96857   1.000 39.21114 ? 214 HIS A ND1 1 
ATOM   1676 C  CD2 . HIS A 1 214 ? -14.87623 3.07419   7.36224   1.000 39.02910 ? 214 HIS A CD2 1 
ATOM   1677 C  CE1 . HIS A 1 214 ? -15.40009 3.56672   9.43470   1.000 41.02562 ? 214 HIS A CE1 1 
ATOM   1678 N  NE2 . HIS A 1 214 ? -14.51088 3.78457   8.48265   1.000 37.63097 ? 214 HIS A NE2 1 
ATOM   1679 N  N   . LEU A 1 215 ? -14.40013 -0.60361  7.95623   1.000 31.12558 ? 215 LEU A N   1 
ATOM   1680 C  CA  . LEU A 1 215 ? -13.07271 -1.17635  7.77361   1.000 29.85679 ? 215 LEU A CA  1 
ATOM   1681 C  C   . LEU A 1 215 ? -13.07838 -2.70041  7.78868   1.000 29.37527 ? 215 LEU A C   1 
ATOM   1682 O  O   . LEU A 1 215 ? -12.00388 -3.31210  7.72948   1.000 27.93466 ? 215 LEU A O   1 
ATOM   1683 C  CB  . LEU A 1 215 ? -12.12682 -0.65020  8.84902   1.000 28.11232 ? 215 LEU A CB  1 
ATOM   1684 C  CG  . LEU A 1 215 ? -12.02081 0.87755   8.78539   1.000 33.16392 ? 215 LEU A CG  1 
ATOM   1685 C  CD1 . LEU A 1 215 ? -11.23916 1.43765   9.94724   1.000 39.39624 ? 215 LEU A CD1 1 
ATOM   1686 C  CD2 . LEU A 1 215 ? -11.39203 1.26616   7.48179   1.000 32.08658 ? 215 LEU A CD2 1 
ATOM   1687 N  N   . TYR A 1 216 ? -14.25755 -3.31540  7.89091   1.000 30.43410 ? 216 TYR A N   1 
ATOM   1688 C  CA  . TYR A 1 216 ? -14.43068 -4.75236  7.73838   1.000 28.58578 ? 216 TYR A CA  1 
ATOM   1689 C  C   . TYR A 1 216 ? -15.31220 -5.07516  6.54038   1.000 28.30676 ? 216 TYR A C   1 
ATOM   1690 O  O   . TYR A 1 216 ? -15.70178 -6.23232  6.36114   1.000 29.54019 ? 216 TYR A O   1 
ATOM   1691 C  CB  . TYR A 1 216 ? -15.04559 -5.37023  8.99675   1.000 37.14965 ? 216 TYR A CB  1 
ATOM   1692 C  CG  . TYR A 1 216 ? -14.25471 -5.20859  10.27836  1.000 33.76624 ? 216 TYR A CG  1 
ATOM   1693 C  CD1 . TYR A 1 216 ? -14.14796 -3.97389  10.90207  1.000 27.39909 ? 216 TYR A CD1 1 
ATOM   1694 C  CD2 . TYR A 1 216 ? -13.63467 -6.30090  10.87935  1.000 29.29008 ? 216 TYR A CD2 1 
ATOM   1695 C  CE1 . TYR A 1 216 ? -13.43881 -3.83055  12.08829  1.000 33.40467 ? 216 TYR A CE1 1 
ATOM   1696 C  CE2 . TYR A 1 216 ? -12.93998 -6.16369  12.06308  1.000 33.18999 ? 216 TYR A CE2 1 
ATOM   1697 C  CZ  . TYR A 1 216 ? -12.84184 -4.93033  12.66152  1.000 31.14703 ? 216 TYR A CZ  1 
ATOM   1698 O  OH  . TYR A 1 216 ? -12.12480 -4.78777  13.83024  1.000 30.50894 ? 216 TYR A OH  1 
ATOM   1699 N  N   . SER A 1 217 ? -15.63023 -4.08447  5.71548   1.000 32.02241 ? 217 SER A N   1 
ATOM   1700 C  CA  . SER A 1 217 ? -16.55723 -4.25798  4.60748   1.000 35.73733 ? 217 SER A CA  1 
ATOM   1701 C  C   . SER A 1 217 ? -15.85107 -4.81206  3.37433   1.000 31.03178 ? 217 SER A C   1 
ATOM   1702 O  O   . SER A 1 217 ? -14.65460 -4.61260  3.17881   1.000 30.80373 ? 217 SER A O   1 
ATOM   1703 C  CB  . SER A 1 217 ? -17.21882 -2.92149  4.26700   1.000 34.91510 ? 217 SER A CB  1 
ATOM   1704 O  OG  . SER A 1 217 ? -16.25126 -1.99617  3.78780   1.000 34.84305 ? 217 SER A OG  1 
ATOM   1705 N  N   . GLU A 1 218 ? -16.60799 -5.52535  2.54276   1.000 33.04643 ? 218 GLU A N   1 
ATOM   1706 C  CA  . GLU A 1 218 ? -16.09743 -5.92914  1.23874   1.000 33.42345 ? 218 GLU A CA  1 
ATOM   1707 C  C   . GLU A 1 218 ? -15.59604 -4.73626  0.44663   1.000 33.25828 ? 218 GLU A C   1 
ATOM   1708 O  O   . GLU A 1 218 ? -14.58063 -4.83098  -0.24395  1.000 32.48447 ? 218 GLU A O   1 
ATOM   1709 C  CB  . GLU A 1 218 ? -17.17161 -6.66173  0.43561   1.000 36.76450 ? 218 GLU A CB  1 
ATOM   1710 C  CG  . GLU A 1 218 ? -16.91313 -8.15241  0.29686   1.000 40.18753 ? 218 GLU A CG  1 
ATOM   1711 C  CD  . GLU A 1 218 ? -17.97225 -8.87210  -0.52624  1.000 53.22003 ? 218 GLU A CD  1 
ATOM   1712 O  OE1 . GLU A 1 218 ? -19.09075 -9.09088  -0.00945  1.000 40.97082 ? 218 GLU A OE1 1 
ATOM   1713 O  OE2 . GLU A 1 218 ? -17.66893 -9.22336  -1.69346  1.000 58.63437 ? 218 GLU A OE2 1 
ATOM   1714 N  N   . GLU A 1 219 ? -16.31132 -3.61135  0.50580   1.000 40.26880 ? 219 GLU A N   1 
ATOM   1715 C  CA  . GLU A 1 219 ? -15.85506 -2.42801  -0.21250  1.000 40.91394 ? 219 GLU A CA  1 
ATOM   1716 C  C   . GLU A 1 219 ? -14.43803 -2.07851  0.19413   1.000 32.00366 ? 219 GLU A C   1 
ATOM   1717 O  O   . GLU A 1 219 ? -13.57533 -1.86740  -0.66464  1.000 33.11137 ? 219 GLU A O   1 
ATOM   1718 C  CB  . GLU A 1 219 ? -16.77766 -1.23324  0.01951   1.000 36.20483 ? 219 GLU A CB  1 
ATOM   1719 C  CG  . GLU A 1 219 ? -16.33888 -0.02171  -0.81053  1.000 38.59522 ? 219 GLU A CG  1 
ATOM   1720 C  CD  . GLU A 1 219 ? -17.33087 1.13727   -0.79840  1.000 51.60910 ? 219 GLU A CD  1 
ATOM   1721 O  OE1 . GLU A 1 219 ? -18.28910 1.12252   0.01638   1.000 59.59300 ? 219 GLU A OE1 1 
ATOM   1722 O  OE2 . GLU A 1 219 ? -17.14611 2.07207   -1.61558  1.000 54.68977 ? 219 GLU A OE2 1 
ATOM   1723 N  N   . PHE A 1 220 ? -14.16386 -2.05567  1.50747   1.000 30.19786 ? 220 PHE A N   1 
ATOM   1724 C  CA  . PHE A 1 220 ? -12.80233 -1.75443  1.95169   1.000 27.94024 ? 220 PHE A CA  1 
ATOM   1725 C  C   . PHE A 1 220 ? -11.82537 -2.84380  1.54814   1.000 31.91231 ? 220 PHE A C   1 
ATOM   1726 O  O   . PHE A 1 220 ? -10.69870 -2.54435  1.11024   1.000 30.18558 ? 220 PHE A O   1 
ATOM   1727 C  CB  . PHE A 1 220 ? -12.73756 -1.56143  3.45824   1.000 26.51488 ? 220 PHE A CB  1 
ATOM   1728 C  CG  . PHE A 1 220 ? -11.40881 -1.07608  3.93607   1.000 24.56587 ? 220 PHE A CG  1 
ATOM   1729 C  CD1 . PHE A 1 220 ? -11.00971 0.22611   3.70594   1.000 30.11410 ? 220 PHE A CD1 1 
ATOM   1730 C  CD2 . PHE A 1 220 ? -10.56030 -1.91258  4.61226   1.000 22.94170 ? 220 PHE A CD2 1 
ATOM   1731 C  CE1 . PHE A 1 220 ? -9.77547  0.68744   4.14022   1.000 29.38419 ? 220 PHE A CE1 1 
ATOM   1732 C  CE2 . PHE A 1 220 ? -9.31540  -1.46011  5.06092   1.000 28.42839 ? 220 PHE A CE2 1 
ATOM   1733 C  CZ  . PHE A 1 220 ? -8.92478  -0.15997  4.81824   1.000 23.94968 ? 220 PHE A CZ  1 
ATOM   1734 N  N   . TYR A 1 221 ? -12.21456 -4.11505  1.71755   1.000 27.25385 ? 221 TYR A N   1 
ATOM   1735 C  CA  . TYR A 1 221 ? -11.28346 -5.19841  1.40201   1.000 33.58732 ? 221 TYR A CA  1 
ATOM   1736 C  C   . TYR A 1 221 ? -10.94584 -5.19980  -0.08211  1.000 33.82832 ? 221 TYR A C   1 
ATOM   1737 O  O   . TYR A 1 221 ? -9.80526  -5.47964  -0.45929  1.000 31.62996 ? 221 TYR A O   1 
ATOM   1738 C  CB  . TYR A 1 221 ? -11.86139 -6.55271  1.81026   1.000 27.82587 ? 221 TYR A CB  1 
ATOM   1739 C  CG  . TYR A 1 221 ? -11.97293 -6.76940  3.29285   1.000 26.19844 ? 221 TYR A CG  1 
ATOM   1740 C  CD1 . TYR A 1 221 ? -11.49588 -5.84052  4.20096   1.000 31.29951 ? 221 TYR A CD1 1 
ATOM   1741 C  CD2 . TYR A 1 221 ? -12.57271 -7.90870  3.78269   1.000 29.69141 ? 221 TYR A CD2 1 
ATOM   1742 C  CE1 . TYR A 1 221 ? -11.61834 -6.05561  5.57647   1.000 30.35894 ? 221 TYR A CE1 1 
ATOM   1743 C  CE2 . TYR A 1 221 ? -12.70372 -8.12899  5.12418   1.000 31.33263 ? 221 TYR A CE2 1 
ATOM   1744 C  CZ  . TYR A 1 221 ? -12.23921 -7.20845  6.02322   1.000 31.45494 ? 221 TYR A CZ  1 
ATOM   1745 O  OH  . TYR A 1 221 ? -12.40822 -7.47568  7.37233   1.000 25.91321 ? 221 TYR A OH  1 
ATOM   1746 N  N   . ARG A 1 222 ? -11.93252 -4.90149  -0.94053  1.000 29.88521 ? 222 ARG A N   1 
ATOM   1747 C  CA  . ARG A 1 222 ? -11.64081 -4.74246  -2.36160  1.000 32.20010 ? 222 ARG A CA  1 
ATOM   1748 C  C   . ARG A 1 222 ? -10.58870 -3.66608  -2.58670  1.000 31.56631 ? 222 ARG A C   1 
ATOM   1749 O  O   . ARG A 1 222 ? -9.72668  -3.80294  -3.46534  1.000 31.61129 ? 222 ARG A O   1 
ATOM   1750 C  CB  . ARG A 1 222 ? -12.92411 -4.41843  -3.13838  1.000 37.73465 ? 222 ARG A CB  1 
ATOM   1751 C  CG  . ARG A 1 222 ? -13.64407 -5.66444  -3.61967  1.000 35.60704 ? 222 ARG A CG  1 
ATOM   1752 C  CD  . ARG A 1 222 ? -14.97188 -5.39234  -4.27753  1.000 39.89024 ? 222 ARG A CD  1 
ATOM   1753 N  NE  . ARG A 1 222 ? -15.66855 -4.23416  -3.73762  1.000 46.65425 ? 222 ARG A NE  1 
ATOM   1754 C  CZ  . ARG A 1 222 ? -16.91133 -4.25774  -3.27373  1.000 44.63195 ? 222 ARG A CZ  1 
ATOM   1755 N  NH1 . ARG A 1 222 ? -17.58341 -5.39265  -3.15215  1.000 46.52838 ? 222 ARG A NH1 1 
ATOM   1756 N  NH2 . ARG A 1 222 ? -17.49710 -3.11414  -2.93047  1.000 40.67560 ? 222 ARG A NH2 1 
ATOM   1757 N  N   . GLU A 1 223 ? -10.63027 -2.58879  -1.79933  1.000 31.09254 ? 223 GLU A N   1 
ATOM   1758 C  CA  . GLU A 1 223 ? -9.63074  -1.54271  -1.97374  1.000 32.90737 ? 223 GLU A CA  1 
ATOM   1759 C  C   . GLU A 1 223 ? -8.25775  -2.05552  -1.55736  1.000 28.54451 ? 223 GLU A C   1 
ATOM   1760 O  O   . GLU A 1 223 ? -7.26783  -1.82254  -2.25246  1.000 33.05797 ? 223 GLU A O   1 
ATOM   1761 C  CB  . GLU A 1 223 ? -10.01129 -0.28279  -1.18904  1.000 29.07384 ? 223 GLU A CB  1 
ATOM   1762 C  CG  . GLU A 1 223 ? -11.18083 0.53884   -1.76658  1.000 37.51583 ? 223 GLU A CG  1 
ATOM   1763 C  CD  . GLU A 1 223 ? -11.03580 0.89689   -3.24517  1.000 38.72488 ? 223 GLU A CD  1 
ATOM   1764 O  OE1 . GLU A 1 223 ? -9.95006  1.35607   -3.66552  1.000 40.41755 ? 223 GLU A OE1 1 
ATOM   1765 O  OE2 . GLU A 1 223 ? -12.03147 0.74685   -3.98429  1.000 45.99154 ? 223 GLU A OE2 1 
ATOM   1766 N  N   . LEU A 1 224 ? -8.18011  -2.74654  -0.41081  1.000 28.09021 ? 224 LEU A N   1 
ATOM   1767 C  CA  . LEU A 1 224 ? -6.94833  -3.42404  -0.01903  1.000 28.76443 ? 224 LEU A CA  1 
ATOM   1768 C  C   . LEU A 1 224 ? -6.46906  -4.37388  -1.10935  1.000 30.99390 ? 224 LEU A C   1 
ATOM   1769 O  O   . LEU A 1 224 ? -5.26842  -4.46747  -1.38627  1.000 31.15068 ? 224 LEU A O   1 
ATOM   1770 C  CB  . LEU A 1 224 ? -7.16418  -4.20734  1.27495   1.000 23.62167 ? 224 LEU A CB  1 
ATOM   1771 C  CG  . LEU A 1 224 ? -7.56008  -3.46814  2.54330   1.000 30.67826 ? 224 LEU A CG  1 
ATOM   1772 C  CD1 . LEU A 1 224 ? -7.50426  -4.43840  3.72995   1.000 28.14422 ? 224 LEU A CD1 1 
ATOM   1773 C  CD2 . LEU A 1 224 ? -6.69004  -2.27285  2.78039   1.000 21.19605 ? 224 LEU A CD2 1 
ATOM   1774 N  N   . PHE A 1 225 ? -7.39212  -5.11514  -1.71774  1.000 30.68441 ? 225 PHE A N   1 
ATOM   1775 C  CA  . PHE A 1 225 ? -7.00522  -6.04119  -2.77105  1.000 28.59537 ? 225 PHE A CA  1 
ATOM   1776 C  C   . PHE A 1 225 ? -6.39002  -5.28413  -3.94379  1.000 36.67062 ? 225 PHE A C   1 
ATOM   1777 O  O   . PHE A 1 225 ? -5.24136  -5.53402  -4.33651  1.000 34.07337 ? 225 PHE A O   1 
ATOM   1778 C  CB  . PHE A 1 225 ? -8.22380  -6.84902  -3.21428  1.000 34.58875 ? 225 PHE A CB  1 
ATOM   1779 C  CG  . PHE A 1 225 ? -7.89800  -7.97645  -4.14112  1.000 37.08389 ? 225 PHE A CG  1 
ATOM   1780 C  CD1 . PHE A 1 225 ? -7.28396  -9.12256  -3.67082  1.000 40.65099 ? 225 PHE A CD1 1 
ATOM   1781 C  CD2 . PHE A 1 225 ? -8.19847  -7.89558  -5.47748  1.000 40.31976 ? 225 PHE A CD2 1 
ATOM   1782 C  CE1 . PHE A 1 225 ? -6.97027  -10.16044 -4.52540  1.000 38.06784 ? 225 PHE A CE1 1 
ATOM   1783 C  CE2 . PHE A 1 225 ? -7.87626  -8.93324  -6.33517  1.000 46.74783 ? 225 PHE A CE2 1 
ATOM   1784 C  CZ  . PHE A 1 225 ? -7.26448  -10.06530 -5.84866  1.000 40.84573 ? 225 PHE A CZ  1 
ATOM   1785 N  N   . ARG A 1 226 ? -7.15152  -4.34107  -4.51115  1.000 33.71646 ? 226 ARG A N   1 
ATOM   1786 C  CA  . ARG A 1 226 ? -6.67652  -3.51349  -5.61647  1.000 32.46538 ? 226 ARG A CA  1 
ATOM   1787 C  C   . ARG A 1 226 ? -5.26769  -2.94781  -5.38799  1.000 36.05741 ? 226 ARG A C   1 
ATOM   1788 O  O   . ARG A 1 226 ? -4.41750  -3.00191  -6.27502  1.000 35.96553 ? 226 ARG A O   1 
ATOM   1789 C  CB  . ARG A 1 226 ? -7.67378  -2.37446  -5.84304  1.000 34.46608 ? 226 ARG A CB  1 
ATOM   1790 C  CG  . ARG A 1 226 ? -7.21675  -1.33211  -6.85338  1.000 37.55677 ? 226 ARG A CG  1 
ATOM   1791 C  CD  . ARG A 1 226 ? -8.32458  -0.34279  -7.15375  1.000 37.25601 ? 226 ARG A CD  1 
ATOM   1792 N  NE  . ARG A 1 226 ? -8.32198  0.80433   -6.24666  1.000 41.01012 ? 226 ARG A NE  1 
ATOM   1793 C  CZ  . ARG A 1 226 ? -7.25456  1.51842   -5.89434  1.000 45.17206 ? 226 ARG A CZ  1 
ATOM   1794 N  NH1 . ARG A 1 226 ? -6.08446  1.38167   -6.50475  1.000 40.39710 ? 226 ARG A NH1 1 
ATOM   1795 N  NH2 . ARG A 1 226 ? -7.37414  2.43137   -4.93165  1.000 34.96677 ? 226 ARG A NH2 1 
ATOM   1796 N  N   . ILE A 1 227 ? -4.98094  -2.40530  -4.20185  1.000 29.45557 ? 227 ILE A N   1 
ATOM   1797 C  CA  . ILE A 1 227 ? -3.71200  -1.70520  -4.02370  1.000 32.01102 ? 227 ILE A CA  1 
ATOM   1798 C  C   . ILE A 1 227 ? -2.55063  -2.63078  -3.67157  1.000 31.77013 ? 227 ILE A C   1 
ATOM   1799 O  O   . ILE A 1 227 ? -1.41185  -2.16054  -3.57483  1.000 32.49809 ? 227 ILE A O   1 
ATOM   1800 C  CB  . ILE A 1 227 ? -3.80856  -0.60323  -2.95164  1.000 31.87001 ? 227 ILE A CB  1 
ATOM   1801 C  CG1 . ILE A 1 227 ? -3.95223  -1.22313  -1.56572  1.000 25.29729 ? 227 ILE A CG1 1 
ATOM   1802 C  CG2 . ILE A 1 227 ? -4.97130  0.34182   -3.27662  1.000 33.59840 ? 227 ILE A CG2 1 
ATOM   1803 C  CD1 . ILE A 1 227 ? -4.22172  -0.21504  -0.47752  1.000 25.63270 ? 227 ILE A CD1 1 
ATOM   1804 N  N   . LEU A 1 228 ? -2.79277  -3.91750  -3.45630  1.000 31.94322 ? 228 LEU A N   1 
ATOM   1805 C  CA  . LEU A 1 228 ? -1.69513  -4.82853  -3.17362  1.000 31.63657 ? 228 LEU A CA  1 
ATOM   1806 C  C   . LEU A 1 228 ? -1.09028  -5.26772  -4.48677  1.000 41.69166 ? 228 LEU A C   1 
ATOM   1807 O  O   . LEU A 1 228 ? -1.80165  -5.42359  -5.48028  1.000 31.34437 ? 228 LEU A O   1 
ATOM   1808 C  CB  . LEU A 1 228 ? -2.17268  -6.06969  -2.41829  1.000 31.20608 ? 228 LEU A CB  1 
ATOM   1809 C  CG  . LEU A 1 228 ? -2.03943  -6.11252  -0.89852  1.000 31.02380 ? 228 LEU A CG  1 
ATOM   1810 C  CD1 . LEU A 1 228 ? -2.69449  -7.38423  -0.35858  1.000 31.25816 ? 228 LEU A CD1 1 
ATOM   1811 C  CD2 . LEU A 1 228 ? -0.59802  -5.99977  -0.40407  1.000 29.13075 ? 228 LEU A CD2 1 
ATOM   1812 N  N   . LYS A 1 229 ? 0.23137   -5.46771  -4.47870  1.000 38.43094 ? 229 LYS A N   1 
ATOM   1813 C  CA  . LYS A 1 229 ? 0.90612   -6.09052  -5.59727  1.000 37.49877 ? 229 LYS A CA  1 
ATOM   1814 C  C   . LYS A 1 229 ? 0.51638   -7.56020  -5.67702  1.000 38.13209 ? 229 LYS A C   1 
ATOM   1815 O  O   . LYS A 1 229 ? 0.09981   -8.15282  -4.67988  1.000 36.18639 ? 229 LYS A O   1 
ATOM   1816 C  CB  . LYS A 1 229 ? 2.42220   -5.96776  -5.45383  1.000 32.55176 ? 229 LYS A CB  1 
ATOM   1817 C  CG  . LYS A 1 229 ? 2.93617   -4.56041  -5.56958  1.000 33.21940 ? 229 LYS A CG  1 
ATOM   1818 C  CD  . LYS A 1 229 ? 4.44202   -4.46744  -5.25443  1.000 41.19230 ? 229 LYS A CD  1 
ATOM   1819 C  CE  . LYS A 1 229 ? 4.96436   -3.05385  -5.47979  1.000 38.90222 ? 229 LYS A CE  1 
ATOM   1820 N  NZ  . LYS A 1 229 ? 6.42124   -2.92802  -5.18024  1.000 51.47483 ? 229 LYS A NZ  1 
ATOM   1821 N  N   . PRO A 1 230 ? 0.61622   -8.16703  -6.86344  1.000 43.45996 ? 230 PRO A N   1 
ATOM   1822 C  CA  . PRO A 1 230 ? 0.47406   -9.62457  -6.94860  1.000 43.53632 ? 230 PRO A CA  1 
ATOM   1823 C  C   . PRO A 1 230 ? 1.47345   -10.30320 -6.02670  1.000 41.95897 ? 230 PRO A C   1 
ATOM   1824 O  O   . PRO A 1 230 ? 2.61346   -9.85930  -5.88901  1.000 44.63992 ? 230 PRO A O   1 
ATOM   1825 C  CB  . PRO A 1 230 ? 0.76449   -9.92535  -8.42412  1.000 51.47767 ? 230 PRO A CB  1 
ATOM   1826 C  CG  . PRO A 1 230 ? 0.38545   -8.67300  -9.13598  1.000 44.84163 ? 230 PRO A CG  1 
ATOM   1827 C  CD  . PRO A 1 230 ? 0.78269   -7.55156  -8.19092  1.000 41.44314 ? 230 PRO A CD  1 
ATOM   1828 N  N   . GLY A 1 231 ? 1.02855   -11.37009 -5.36665  1.000 40.99757 ? 231 GLY A N   1 
ATOM   1829 C  CA  . GLY A 1 231 ? 1.83915   -11.94865 -4.31287  1.000 42.22499 ? 231 GLY A CA  1 
ATOM   1830 C  C   . GLY A 1 231 ? 1.93182   -11.11727 -3.05178  1.000 34.99066 ? 231 GLY A C   1 
ATOM   1831 O  O   . GLY A 1 231 ? 2.72771   -11.44465 -2.16676  1.000 38.80866 ? 231 GLY A O   1 
ATOM   1832 N  N   . GLY A 1 232 ? 1.16494   -10.04556 -2.94351  1.000 33.23180 ? 232 GLY A N   1 
ATOM   1833 C  CA  . GLY A 1 232 ? 1.24764   -9.20044  -1.76964  1.000 29.25374 ? 232 GLY A CA  1 
ATOM   1834 C  C   . GLY A 1 232 ? 0.59740   -9.83169  -0.54576  1.000 35.71591 ? 232 GLY A C   1 
ATOM   1835 O  O   . GLY A 1 232 ? -0.26969  -10.69996 -0.64367  1.000 35.14310 ? 232 GLY A O   1 
ATOM   1836 N  N   . ARG A 1 233 ? 1.03432   -9.38555  0.63168   1.000 28.88726 ? 233 ARG A N   1 
ATOM   1837 C  CA  . ARG A 1 233 ? 0.66891   -10.01083 1.89190   1.000 32.47107 ? 233 ARG A CA  1 
ATOM   1838 C  C   . ARG A 1 233 ? -0.17473  -9.06873  2.73787   1.000 30.65188 ? 233 ARG A C   1 
ATOM   1839 O  O   . ARG A 1 233 ? 0.14437   -7.88121  2.88997   1.000 28.09737 ? 233 ARG A O   1 
ATOM   1840 C  CB  . ARG A 1 233 ? 1.90106   -10.40652 2.69538   1.000 31.79927 ? 233 ARG A CB  1 
ATOM   1841 C  CG  . ARG A 1 233 ? 2.70434   -11.56063 2.14691   1.000 31.95256 ? 233 ARG A CG  1 
ATOM   1842 C  CD  . ARG A 1 233 ? 3.93346   -11.06281 1.42350   1.000 33.78316 ? 233 ARG A CD  1 
ATOM   1843 N  NE  . ARG A 1 233 ? 4.87947   -10.43935 2.33741   1.000 36.54419 ? 233 ARG A NE  1 
ATOM   1844 C  CZ  . ARG A 1 233 ? 5.87234   -9.65972  1.94387   1.000 34.12933 ? 233 ARG A CZ  1 
ATOM   1845 N  NH1 . ARG A 1 233 ? 6.03560   -9.34737  0.67134   1.000 35.16756 ? 233 ARG A NH1 1 
ATOM   1846 N  NH2 . ARG A 1 233 ? 6.72589   -9.18753  2.84605   1.000 34.29250 ? 233 ARG A NH2 1 
ATOM   1847 N  N   . LEU A 1 234 ? -1.21565  -9.61658  3.34312   1.000 29.72315 ? 234 LEU A N   1 
ATOM   1848 C  CA  . LEU A 1 234 ? -2.10159  -8.85528  4.20608   1.000 26.74675 ? 234 LEU A CA  1 
ATOM   1849 C  C   . LEU A 1 234 ? -2.12029  -9.50207  5.58308   1.000 29.72223 ? 234 LEU A C   1 
ATOM   1850 O  O   . LEU A 1 234 ? -2.18048  -10.72923 5.70796   1.000 30.76325 ? 234 LEU A O   1 
ATOM   1851 C  CB  . LEU A 1 234 ? -3.51676  -8.80442  3.62060   1.000 21.41342 ? 234 LEU A CB  1 
ATOM   1852 C  CG  . LEU A 1 234 ? -4.63628  -8.26143  4.50093   1.000 20.67382 ? 234 LEU A CG  1 
ATOM   1853 C  CD1 . LEU A 1 234 ? -4.33192  -6.89670  5.07837   1.000 21.79965 ? 234 LEU A CD1 1 
ATOM   1854 C  CD2 . LEU A 1 234 ? -5.94098  -8.20475  3.74151   1.000 26.57190 ? 234 LEU A CD2 1 
ATOM   1855 N  N   . PHE A 1 235 ? -2.03206  -8.69317  6.62188   1.000 24.73490 ? 235 PHE A N   1 
ATOM   1856 C  CA  . PHE A 1 235 ? -2.41626  -9.15733  7.94141   1.000 23.62379 ? 235 PHE A CA  1 
ATOM   1857 C  C   . PHE A 1 235 ? -3.62818  -8.35760  8.35904   1.000 23.83404 ? 235 PHE A C   1 
ATOM   1858 O  O   . PHE A 1 235 ? -3.62542  -7.12715  8.25783   1.000 23.67660 ? 235 PHE A O   1 
ATOM   1859 C  CB  . PHE A 1 235 ? -1.29388  -9.01135  8.95805   1.000 27.53800 ? 235 PHE A CB  1 
ATOM   1860 C  CG  . PHE A 1 235 ? -1.72738  -9.27965  10.37632  1.000 25.64731 ? 235 PHE A CG  1 
ATOM   1861 C  CD1 . PHE A 1 235 ? -1.86290  -10.57703 10.83261  1.000 27.17782 ? 235 PHE A CD1 1 
ATOM   1862 C  CD2 . PHE A 1 235 ? -1.99784  -8.24077  11.24318  1.000 29.41530 ? 235 PHE A CD2 1 
ATOM   1863 C  CE1 . PHE A 1 235 ? -2.24807  -10.83951 12.11355  1.000 25.65132 ? 235 PHE A CE1 1 
ATOM   1864 C  CE2 . PHE A 1 235 ? -2.39222  -8.50185  12.54323  1.000 32.74095 ? 235 PHE A CE2 1 
ATOM   1865 C  CZ  . PHE A 1 235 ? -2.51404  -9.81552  12.97113  1.000 26.88814 ? 235 PHE A CZ  1 
ATOM   1866 N  N   . HIS A 1 236 ? -4.67021  -9.05524  8.78796   1.000 22.00262 ? 236 HIS A N   1 
ATOM   1867 C  CA  . HIS A 1 236 ? -5.86968  -8.41716  9.30623   1.000 23.83687 ? 236 HIS A CA  1 
ATOM   1868 C  C   . HIS A 1 236 ? -6.05527  -8.88922  10.73890  1.000 24.93774 ? 236 HIS A C   1 
ATOM   1869 O  O   . HIS A 1 236 ? -6.24669  -10.08236 10.97630  1.000 28.44631 ? 236 HIS A O   1 
ATOM   1870 C  CB  . HIS A 1 236 ? -7.07969  -8.75875  8.42883   1.000 20.33163 ? 236 HIS A CB  1 
ATOM   1871 C  CG  . HIS A 1 236 ? -8.33603  -8.02072  8.78249   1.000 23.84115 ? 236 HIS A CG  1 
ATOM   1872 N  ND1 . HIS A 1 236 ? -8.54221  -7.43777  10.01483  1.000 28.65291 ? 236 HIS A ND1 1 
ATOM   1873 C  CD2 . HIS A 1 236 ? -9.47944  -7.81942  8.07706   1.000 25.09784 ? 236 HIS A CD2 1 
ATOM   1874 C  CE1 . HIS A 1 236 ? -9.74555  -6.88643  10.04522  1.000 28.15354 ? 236 HIS A CE1 1 
ATOM   1875 N  NE2 . HIS A 1 236 ? -10.33124 -7.09743  8.87877   1.000 26.75165 ? 236 HIS A NE2 1 
ATOM   1876 N  N   . TYR A 1 237 ? -5.97626  -7.96175  11.68476  1.000 28.07643 ? 237 TYR A N   1 
ATOM   1877 C  CA  . TYR A 1 237 ? -6.17815  -8.28017  13.09046  1.000 24.78789 ? 237 TYR A CA  1 
ATOM   1878 C  C   . TYR A 1 237 ? -7.63762  -8.60648  13.34556  1.000 35.07270 ? 237 TYR A C   1 
ATOM   1879 O  O   . TYR A 1 237 ? -8.52936  -8.05744  12.69912  1.000 29.26067 ? 237 TYR A O   1 
ATOM   1880 C  CB  . TYR A 1 237 ? -5.77745  -7.09590  13.96935  1.000 29.92280 ? 237 TYR A CB  1 
ATOM   1881 C  CG  . TYR A 1 237 ? -5.78977  -7.39316  15.46015  1.000 33.68455 ? 237 TYR A CG  1 
ATOM   1882 C  CD1 . TYR A 1 237 ? -4.83189  -8.22246  16.01462  1.000 36.30694 ? 237 TYR A CD1 1 
ATOM   1883 C  CD2 . TYR A 1 237 ? -6.72861  -6.82263  16.31036  1.000 36.71862 ? 237 TYR A CD2 1 
ATOM   1884 C  CE1 . TYR A 1 237 ? -4.80884  -8.50227  17.36014  1.000 39.08504 ? 237 TYR A CE1 1 
ATOM   1885 C  CE2 . TYR A 1 237 ? -6.71246  -7.09935  17.68921  1.000 43.48608 ? 237 TYR A CE2 1 
ATOM   1886 C  CZ  . TYR A 1 237 ? -5.73603  -7.94794  18.19224  1.000 40.38739 ? 237 TYR A CZ  1 
ATOM   1887 O  OH  . TYR A 1 237 ? -5.65808  -8.26823  19.52109  1.000 43.69575 ? 237 TYR A OH  1 
ATOM   1888 N  N   . VAL A 1 238 ? -7.87437  -9.48884  14.31997  1.000 28.82674 ? 238 VAL A N   1 
ATOM   1889 C  CA  . VAL A 1 238 ? -9.21541  -9.92368  14.68308  1.000 38.42612 ? 238 VAL A CA  1 
ATOM   1890 C  C   . VAL A 1 238 ? -9.36947  -9.81671  16.19133  1.000 41.77398 ? 238 VAL A C   1 
ATOM   1891 O  O   . VAL A 1 238 ? -10.37046 -9.29500  16.68972  1.000 48.53221 ? 238 VAL A O   1 
ATOM   1892 C  CB  . VAL A 1 238 ? -9.47984  -11.35956 14.20379  1.000 41.68189 ? 238 VAL A CB  1 
ATOM   1893 C  CG1 . VAL A 1 238 ? -10.77159 -11.90531 14.81394  1.000 41.57851 ? 238 VAL A CG1 1 
ATOM   1894 C  CG2 . VAL A 1 238 ? -9.50948  -11.42019 12.66629  1.000 31.66495 ? 238 VAL A CG2 1 
ATOM   1895 N  N   . GLY A 1 239 ? -8.38135  -10.31018 16.92567  1.000 46.80842 ? 239 GLY A N   1 
ATOM   1896 C  CA  . GLY A 1 239 ? -8.40993  -10.27474 18.37721  1.000 55.66246 ? 239 GLY A CA  1 
ATOM   1897 C  C   . GLY A 1 239 ? -9.17683  -11.42473 19.00540  1.000 58.53848 ? 239 GLY A C   1 
ATOM   1898 O  O   . GLY A 1 239 ? -10.14218 -11.21128 19.74632  1.000 67.92764 ? 239 GLY A O   1 
ATOM   1899 N  N   . LYS A 1 248 ? -13.92335 -16.68086 16.86443  1.000 78.53634 ? 248 LYS A N   1 
ATOM   1900 C  CA  . LYS A 1 248 ? -14.97376 -15.66802 16.87808  1.000 79.82673 ? 248 LYS A CA  1 
ATOM   1901 C  C   . LYS A 1 248 ? -15.92218 -15.85074 15.69687  1.000 82.37423 ? 248 LYS A C   1 
ATOM   1902 O  O   . LYS A 1 248 ? -15.70030 -16.70238 14.82744  1.000 73.12598 ? 248 LYS A O   1 
ATOM   1903 C  CB  . LYS A 1 248 ? -14.38018 -14.25511 16.83362  1.000 73.56783 ? 248 LYS A CB  1 
ATOM   1904 C  CG  . LYS A 1 248 ? -13.18561 -13.99021 17.74915  1.000 75.13325 ? 248 LYS A CG  1 
ATOM   1905 C  CD  . LYS A 1 248 ? -13.56481 -13.81247 19.21773  1.000 75.40128 ? 248 LYS A CD  1 
ATOM   1906 C  CE  . LYS A 1 248 ? -12.30460 -13.65098 20.07202  1.000 77.02672 ? 248 LYS A CE  1 
ATOM   1907 N  NZ  . LYS A 1 248 ? -12.26446 -12.37453 20.84859  1.000 60.86692 ? 248 LYS A NZ  1 
ATOM   1908 N  N   . ASP A 1 249 ? -16.97540 -15.02665 15.67481  1.000 85.40061 ? 249 ASP A N   1 
ATOM   1909 C  CA  . ASP A 1 249 ? -17.92897 -14.99323 14.57160  1.000 78.75783 ? 249 ASP A CA  1 
ATOM   1910 C  C   . ASP A 1 249 ? -17.57760 -13.96493 13.50749  1.000 69.78856 ? 249 ASP A C   1 
ATOM   1911 O  O   . ASP A 1 249 ? -18.08381 -14.05936 12.38317  1.000 64.77561 ? 249 ASP A O   1 
ATOM   1912 C  CB  . ASP A 1 249 ? -19.33561 -14.68274 15.08515  1.000 71.24328 ? 249 ASP A CB  1 
ATOM   1913 C  CG  . ASP A 1 249 ? -19.74742 -15.57357 16.23231  1.000 86.86565 ? 249 ASP A CG  1 
ATOM   1914 O  OD1 . ASP A 1 249 ? -19.00014 -15.63503 17.23266  1.000 87.11127 ? 249 ASP A OD1 1 
ATOM   1915 O  OD2 . ASP A 1 249 ? -20.82416 -16.20115 16.13569  1.000 91.95648 ? 249 ASP A OD2 1 
ATOM   1916 N  N   . LEU A 1 250 ? -16.76516 -12.96065 13.83897  1.000 57.35019 ? 250 LEU A N   1 
ATOM   1917 C  CA  . LEU A 1 250 ? -16.36967 -12.00353 12.81375  1.000 60.46128 ? 250 LEU A CA  1 
ATOM   1918 C  C   . LEU A 1 250 ? -15.16841 -12.50681 12.03054  1.000 48.02574 ? 250 LEU A C   1 
ATOM   1919 O  O   . LEU A 1 250 ? -15.07092 -12.24762 10.82698  1.000 49.16525 ? 250 LEU A O   1 
ATOM   1920 C  CB  . LEU A 1 250 ? -16.08565 -10.62334 13.42659  1.000 56.56173 ? 250 LEU A CB  1 
ATOM   1921 C  CG  . LEU A 1 250 ? -14.71357 -10.18872 13.94994  1.000 40.27559 ? 250 LEU A CG  1 
ATOM   1922 C  CD1 . LEU A 1 250 ? -14.81050 -8.77065  14.49818  1.000 47.94715 ? 250 LEU A CD1 1 
ATOM   1923 C  CD2 . LEU A 1 250 ? -14.20794 -11.12732 15.02246  1.000 44.44309 ? 250 LEU A CD2 1 
ATOM   1924 N  N   . GLN A 1 251 ? -14.26912 -13.23677 12.69791  1.000 51.87342 ? 251 GLN A N   1 
ATOM   1925 C  CA  . GLN A 1 251 ? -13.15403 -13.89565 12.02676  1.000 47.68844 ? 251 GLN A CA  1 
ATOM   1926 C  C   . GLN A 1 251 ? -13.62601 -14.67628 10.82020  1.000 45.20504 ? 251 GLN A C   1 
ATOM   1927 O  O   . GLN A 1 251 ? -12.99696 -14.65991 9.75570   1.000 36.04062 ? 251 GLN A O   1 
ATOM   1928 C  CB  . GLN A 1 251 ? -12.47090 -14.85532 12.98729  1.000 54.96719 ? 251 GLN A CB  1 
ATOM   1929 C  CG  . GLN A 1 251 ? -11.16555 -15.34140 12.45406  1.000 53.61721 ? 251 GLN A CG  1 
ATOM   1930 C  CD  . GLN A 1 251 ? -10.63959 -16.49454 13.24974  1.000 53.27153 ? 251 GLN A CD  1 
ATOM   1931 O  OE1 . GLN A 1 251 ? -9.86462  -16.32172 14.18342  1.000 55.56755 ? 251 GLN A OE1 1 
ATOM   1932 N  NE2 . GLN A 1 251 ? -11.06212 -17.70052 12.87773  1.000 59.91015 ? 251 GLN A NE2 1 
ATOM   1933 N  N   . LYS A 1 252 ? -14.67987 -15.45621 11.02876  1.000 49.15100 ? 252 LYS A N   1 
ATOM   1934 C  CA  . LYS A 1 252 ? -15.57127 -15.96842 10.00748  1.000 47.39773 ? 252 LYS A CA  1 
ATOM   1935 C  C   . LYS A 1 252 ? -15.71951 -15.07724 8.79689   1.000 48.81971 ? 252 LYS A C   1 
ATOM   1936 O  O   . LYS A 1 252 ? -15.16885 -15.36965 7.73197   1.000 46.83730 ? 252 LYS A O   1 
ATOM   1937 C  CB  . LYS A 1 252 ? -16.93207 -16.15929 10.50172  1.000 61.99969 ? 252 LYS A CB  1 
ATOM   1938 C  CG  . LYS A 1 252 ? -17.29329 -17.52218 10.92453  1.000 67.25831 ? 252 LYS A CG  1 
ATOM   1939 C  CD  . LYS A 1 252 ? -16.66982 -18.53396 10.01237  1.000 64.58822 ? 252 LYS A CD  1 
ATOM   1940 C  CE  . LYS A 1 252 ? -17.36340 -18.49505 8.65810   1.000 62.62979 ? 252 LYS A CE  1 
ATOM   1941 N  NZ  . LYS A 1 252 ? -18.77885 -18.97355 8.80131   1.000 67.32434 ? 252 LYS A NZ  1 
ATOM   1942 N  N   . GLY A 1 253 ? -16.54428 -14.03643 8.95212   1.000 50.28001 ? 253 GLY A N   1 
ATOM   1943 C  CA  . GLY A 1 253 ? -16.82050 -13.14967 7.84546   1.000 42.21994 ? 253 GLY A CA  1 
ATOM   1944 C  C   . GLY A 1 253 ? -15.55943 -12.54322 7.27287   1.000 38.03218 ? 253 GLY A C   1 
ATOM   1945 O  O   . GLY A 1 253 ? -15.42900 -12.41464 6.05507   1.000 37.45683 ? 253 GLY A O   1 
ATOM   1946 N  N   . VAL A 1 254 ? -14.60830 -12.17284 8.14018   1.000 36.04225 ? 254 VAL A N   1 
ATOM   1947 C  CA  . VAL A 1 254 ? -13.34759 -11.60935 7.65498   1.000 38.64377 ? 254 VAL A CA  1 
ATOM   1948 C  C   . VAL A 1 254 ? -12.68200 -12.58228 6.70089   1.000 35.13560 ? 254 VAL A C   1 
ATOM   1949 O  O   . VAL A 1 254 ? -12.34709 -12.23463 5.56415   1.000 36.41634 ? 254 VAL A O   1 
ATOM   1950 C  CB  . VAL A 1 254 ? -12.40411 -11.25344 8.81834   1.000 35.71991 ? 254 VAL A CB  1 
ATOM   1951 C  CG1 . VAL A 1 254 ? -10.99689 -11.09642 8.28973   1.000 29.51643 ? 254 VAL A CG1 1 
ATOM   1952 C  CG2 . VAL A 1 254 ? -12.83030 -9.96427  9.48656   1.000 34.70554 ? 254 VAL A CG2 1 
ATOM   1953 N  N   . MET A 1 255 ? -12.49591 -13.82542 7.14197   1.000 34.99245 ? 255 MET A N   1 
ATOM   1954 C  CA  . MET A 1 255 ? -11.94352 -14.82702 6.24065   1.000 43.59572 ? 255 MET A CA  1 
ATOM   1955 C  C   . MET A 1 255 ? -12.81754 -14.98015 4.99502   1.000 41.25335 ? 255 MET A C   1 
ATOM   1956 O  O   . MET A 1 255 ? -12.30812 -14.96666 3.86961   1.000 44.24004 ? 255 MET A O   1 
ATOM   1957 C  CB  . MET A 1 255 ? -11.74216 -16.14275 7.00573   1.000 38.93778 ? 255 MET A CB  1 
ATOM   1958 C  CG  . MET A 1 255 ? -10.38501 -16.16534 7.74621   1.000 43.94788 ? 255 MET A CG  1 
ATOM   1959 S  SD  . MET A 1 255 ? -9.90828  -17.63736 8.68391   1.000 35.54725 ? 255 MET A SD  1 
ATOM   1960 C  CE  . MET A 1 255 ? -11.42315 -18.52252 8.74235   1.000 43.56505 ? 255 MET A CE  1 
ATOM   1961 N  N   . GLU A 1 256 ? -14.13879 -15.03063 5.17229   1.000 38.59203 ? 256 GLU A N   1 
ATOM   1962 C  CA  . GLU A 1 256 ? -15.04390 -15.22034 4.03891   1.000 41.60222 ? 256 GLU A CA  1 
ATOM   1963 C  C   . GLU A 1 256 ? -14.97107 -14.04746 3.06296   1.000 39.95735 ? 256 GLU A C   1 
ATOM   1964 O  O   . GLU A 1 256 ? -14.85429 -14.24032 1.84805   1.000 39.92069 ? 256 GLU A O   1 
ATOM   1965 C  CB  . GLU A 1 256 ? -16.46640 -15.38060 4.55575   1.000 44.45774 ? 256 GLU A CB  1 
ATOM   1966 C  CG  . GLU A 1 256 ? -17.05263 -16.75404 4.49287   1.000 48.62130 ? 256 GLU A CG  1 
ATOM   1967 C  CD  . GLU A 1 256 ? -18.37366 -16.80698 5.25105   1.000 58.94986 ? 256 GLU A CD  1 
ATOM   1968 O  OE1 . GLU A 1 256 ? -19.05942 -15.75492 5.32623   1.000 62.08794 ? 256 GLU A OE1 1 
ATOM   1969 O  OE2 . GLU A 1 256 ? -18.73528 -17.88965 5.76600   1.000 71.77145 ? 256 GLU A OE2 1 
ATOM   1970 N  N   . ARG A 1 257 ? -15.05865 -12.82007 3.58205   1.000 37.57308 ? 257 ARG A N   1 
ATOM   1971 C  CA  . ARG A 1 257 ? -15.05479 -11.63077 2.73524   1.000 36.72284 ? 257 ARG A CA  1 
ATOM   1972 C  C   . ARG A 1 257 ? -13.72377 -11.44443 2.02841   1.000 37.68667 ? 257 ARG A C   1 
ATOM   1973 O  O   . ARG A 1 257 ? -13.67426 -10.89268 0.92190   1.000 40.42668 ? 257 ARG A O   1 
ATOM   1974 C  CB  . ARG A 1 257 ? -15.33880 -10.38397 3.57174   1.000 37.13679 ? 257 ARG A CB  1 
ATOM   1975 C  CG  . ARG A 1 257 ? -16.77215 -10.02956 3.76447   1.000 43.50092 ? 257 ARG A CG  1 
ATOM   1976 C  CD  . ARG A 1 257 ? -16.86912 -8.97108  4.86394   1.000 38.49091 ? 257 ARG A CD  1 
ATOM   1977 N  NE  . ARG A 1 257 ? -17.47003 -9.54329  6.06145   1.000 49.20311 ? 257 ARG A NE  1 
ATOM   1978 C  CZ  . ARG A 1 257 ? -16.92593 -9.51433  7.27037   1.000 40.47612 ? 257 ARG A CZ  1 
ATOM   1979 N  NH1 . ARG A 1 257 ? -15.77890 -8.89402  7.50510   1.000 35.66777 ? 257 ARG A NH1 1 
ATOM   1980 N  NH2 . ARG A 1 257 ? -17.55599 -10.11451 8.27356   1.000 48.45103 ? 257 ARG A NH2 1 
ATOM   1981 N  N   . LEU A 1 258 ? -12.63103 -11.87864 2.64640   1.000 38.26717 ? 258 LEU A N   1 
ATOM   1982 C  CA  . LEU A 1 258 ? -11.34628 -11.71877 1.99024   1.000 30.18000 ? 258 LEU A CA  1 
ATOM   1983 C  C   . LEU A 1 258 ? -11.24250 -12.63275 0.77562   1.000 37.66240 ? 258 LEU A C   1 
ATOM   1984 O  O   . LEU A 1 258 ? -10.73425 -12.22660 -0.27449  1.000 35.34074 ? 258 LEU A O   1 
ATOM   1985 C  CB  . LEU A 1 258 ? -10.21899 -11.98200 2.98518   1.000 32.38878 ? 258 LEU A CB  1 
ATOM   1986 C  CG  . LEU A 1 258 ? -9.87338  -10.88898 3.98958   1.000 26.49147 ? 258 LEU A CG  1 
ATOM   1987 C  CD1 . LEU A 1 258 ? -8.66055  -11.28354 4.80669   1.000 30.43464 ? 258 LEU A CD1 1 
ATOM   1988 C  CD2 . LEU A 1 258 ? -9.61782  -9.56088  3.30965   1.000 29.10049 ? 258 LEU A CD2 1 
ATOM   1989 N  N   . ARG A 1 259 ? -11.72126 -13.87102 0.89010   1.000 35.15925 ? 259 ARG A N   1 
ATOM   1990 C  CA  . ARG A 1 259 ? -11.72947 -14.74769 -0.27560  1.000 42.73335 ? 259 ARG A CA  1 
ATOM   1991 C  C   . ARG A 1 259 ? -12.66058 -14.21213 -1.35455  1.000 38.51061 ? 259 ARG A C   1 
ATOM   1992 O  O   . ARG A 1 259 ? -12.28278 -14.13741 -2.52460  1.000 47.35797 ? 259 ARG A O   1 
ATOM   1993 C  CB  . ARG A 1 259 ? -12.12566 -16.16235 0.13003   1.000 41.03087 ? 259 ARG A CB  1 
ATOM   1994 C  CG  . ARG A 1 259 ? -11.40918 -16.64962 1.36710   1.000 41.77081 ? 259 ARG A CG  1 
ATOM   1995 C  CD  . ARG A 1 259 ? -11.60671 -18.15130 1.56894   1.000 43.79971 ? 259 ARG A CD  1 
ATOM   1996 N  NE  . ARG A 1 259 ? -10.72430 -18.63044 2.62398   1.000 48.31863 ? 259 ARG A NE  1 
ATOM   1997 C  CZ  . ARG A 1 259 ? -11.14057 -19.16597 3.76336   1.000 44.42929 ? 259 ARG A CZ  1 
ATOM   1998 N  NH1 . ARG A 1 259 ? -12.42413 -19.38286 3.99651   1.000 45.88004 ? 259 ARG A NH1 1 
ATOM   1999 N  NH2 . ARG A 1 259 ? -10.24565 -19.47638 4.69722   1.000 44.87764 ? 259 ARG A NH2 1 
ATOM   2000 N  N   . ARG A 1 260 ? -13.89239 -13.85475 -0.98053  1.000 40.88444 ? 260 ARG A N   1 
ATOM   2001 C  CA  . ARG A 1 260 ? -14.83882 -13.27251 -1.93467  1.000 46.95910 ? 260 ARG A CA  1 
ATOM   2002 C  C   . ARG A 1 260 ? -14.18683 -12.17571 -2.77434  1.000 43.28113 ? 260 ARG A C   1 
ATOM   2003 O  O   . ARG A 1 260 ? -14.34339 -12.13263 -3.99904  1.000 47.55884 ? 260 ARG A O   1 
ATOM   2004 C  CB  . ARG A 1 260 ? -16.05220 -12.72574 -1.17776  1.000 46.61320 ? 260 ARG A CB  1 
ATOM   2005 C  CG  . ARG A 1 260 ? -17.29959 -12.56988 -2.00511  1.000 47.81131 ? 260 ARG A CG  1 
ATOM   2006 C  CD  . ARG A 1 260 ? -18.56218 -13.07895 -1.28609  1.000 51.14788 ? 260 ARG A CD  1 
ATOM   2007 N  NE  . ARG A 1 260 ? -18.93546 -12.20294 -0.18154  1.000 56.94317 ? 260 ARG A NE  1 
ATOM   2008 C  CZ  . ARG A 1 260 ? -19.11237 -12.60592 1.07072   1.000 51.02298 ? 260 ARG A CZ  1 
ATOM   2009 N  NH1 . ARG A 1 260 ? -19.02890 -13.88619 1.40368   1.000 55.19506 ? 260 ARG A NH1 1 
ATOM   2010 N  NH2 . ARG A 1 260 ? -19.38734 -11.70504 2.01038   1.000 49.14333 ? 260 ARG A NH2 1 
ATOM   2011 N  N   . VAL A 1 261 ? -13.39878 -11.31982 -2.12860  1.000 42.91030 ? 261 VAL A N   1 
ATOM   2012 C  CA  . VAL A 1 261 ? -12.74487 -10.18692 -2.76621  1.000 36.65566 ? 261 VAL A CA  1 
ATOM   2013 C  C   . VAL A 1 261 ? -11.58128 -10.61371 -3.67626  1.000 47.19396 ? 261 VAL A C   1 
ATOM   2014 O  O   . VAL A 1 261 ? -11.21643 -9.88733  -4.61558  1.000 43.23596 ? 261 VAL A O   1 
ATOM   2015 C  CB  . VAL A 1 261 ? -12.33185 -9.25463  -1.61429  1.000 45.68181 ? 261 VAL A CB  1 
ATOM   2016 C  CG1 . VAL A 1 261 ? -10.90695 -8.73021  -1.76819  1.000 39.70131 ? 261 VAL A CG1 1 
ATOM   2017 C  CG2 . VAL A 1 261 ? -13.38119 -8.16333  -1.41603  1.000 35.55866 ? 261 VAL A CG2 1 
ATOM   2018 N  N   . GLY A 1 262 ? -10.99798 -11.78939 -3.44232  1.000 39.45240 ? 262 GLY A N   1 
ATOM   2019 C  CA  . GLY A 1 262 ? -9.94058  -12.28327 -4.29781  1.000 39.81531 ? 262 GLY A CA  1 
ATOM   2020 C  C   . GLY A 1 262 ? -8.79564  -12.95083 -3.56066  1.000 35.73103 ? 262 GLY A C   1 
ATOM   2021 O  O   . GLY A 1 262 ? -8.05395  -13.73910 -4.15389  1.000 36.12653 ? 262 GLY A O   1 
ATOM   2022 N  N   . PHE A 1 263 ? -8.66305  -12.67891 -2.26504  1.000 32.44947 ? 263 PHE A N   1 
ATOM   2023 C  CA  . PHE A 1 263 ? -7.50923  -13.16074 -1.51942  1.000 35.88112 ? 263 PHE A CA  1 
ATOM   2024 C  C   . PHE A 1 263 ? -7.49666  -14.67838 -1.44081  1.000 38.96788 ? 263 PHE A C   1 
ATOM   2025 O  O   . PHE A 1 263 ? -8.53015  -15.34298 -1.54191  1.000 36.37482 ? 263 PHE A O   1 
ATOM   2026 C  CB  . PHE A 1 263 ? -7.48793  -12.59961 -0.10062  1.000 33.46671 ? 263 PHE A CB  1 
ATOM   2027 C  CG  . PHE A 1 263 ? -7.16194  -11.14619 -0.03254  1.000 36.64477 ? 263 PHE A CG  1 
ATOM   2028 C  CD1 . PHE A 1 263 ? -5.86323  -10.71626 -0.17280  1.000 31.66818 ? 263 PHE A CD1 1 
ATOM   2029 C  CD2 . PHE A 1 263 ? -8.15866  -10.20710 0.16449   1.000 34.46132 ? 263 PHE A CD2 1 
ATOM   2030 C  CE1 . PHE A 1 263 ? -5.56533  -9.36765  -0.09672  1.000 35.32247 ? 263 PHE A CE1 1 
ATOM   2031 C  CE2 . PHE A 1 263 ? -7.86971  -8.86441  0.23597   1.000 27.64711 ? 263 PHE A CE2 1 
ATOM   2032 C  CZ  . PHE A 1 263 ? -6.57241  -8.43995  0.09477   1.000 33.10599 ? 263 PHE A CZ  1 
ATOM   2033 N  N   . VAL A 1 264 ? -6.29269  -15.22107 -1.25522  1.000 34.36523 ? 264 VAL A N   1 
ATOM   2034 C  CA  . VAL A 1 264 ? -6.05938  -16.64684 -1.07573  1.000 39.94079 ? 264 VAL A CA  1 
ATOM   2035 C  C   . VAL A 1 264 ? -5.08298  -16.81779 0.08207   1.000 39.03750 ? 264 VAL A C   1 
ATOM   2036 O  O   . VAL A 1 264 ? -4.55222  -15.84156 0.61907   1.000 37.56538 ? 264 VAL A O   1 
ATOM   2037 C  CB  . VAL A 1 264 ? -5.51617  -17.31526 -2.35664  1.000 42.34291 ? 264 VAL A CB  1 
ATOM   2038 C  CG1 . VAL A 1 264 ? -6.57093  -17.28101 -3.44546  1.000 39.18425 ? 264 VAL A CG1 1 
ATOM   2039 C  CG2 . VAL A 1 264 ? -4.23257  -16.63855 -2.81822  1.000 36.27137 ? 264 VAL A CG2 1 
ATOM   2040 N  N   . GLY A 1 265 ? -4.83319  -18.06834 0.46265   1.000 38.91750 ? 265 GLY A N   1 
ATOM   2041 C  CA  . GLY A 1 265 ? -4.00765  -18.31066 1.63544   1.000 37.20162 ? 265 GLY A CA  1 
ATOM   2042 C  C   . GLY A 1 265 ? -4.58184  -17.68623 2.88818   1.000 39.72334 ? 265 GLY A C   1 
ATOM   2043 O  O   . GLY A 1 265 ? -3.83743  -17.34851 3.81264   1.000 39.01763 ? 265 GLY A O   1 
ATOM   2044 N  N   . VAL A 1 266 ? -5.89648  -17.50568 2.93244   1.000 33.81745 ? 266 VAL A N   1 
ATOM   2045 C  CA  . VAL A 1 266 ? -6.56392  -16.84754 4.05152   1.000 37.41046 ? 266 VAL A CA  1 
ATOM   2046 C  C   . VAL A 1 266 ? -6.64227  -17.82787 5.22314   1.000 32.29630 ? 266 VAL A C   1 
ATOM   2047 O  O   . VAL A 1 266 ? -7.30698  -18.85837 5.12884   1.000 38.62628 ? 266 VAL A O   1 
ATOM   2048 C  CB  . VAL A 1 266 ? -7.95450  -16.35528 3.63422   1.000 40.53365 ? 266 VAL A CB  1 
ATOM   2049 C  CG1 . VAL A 1 266 ? -8.62951  -15.58281 4.75948   1.000 40.16603 ? 266 VAL A CG1 1 
ATOM   2050 C  CG2 . VAL A 1 266 ? -7.84777  -15.49297 2.37366   1.000 36.67896 ? 266 VAL A CG2 1 
ATOM   2051 N  N   . ARG A 1 267 ? -5.97127  -17.50693 6.33432   1.000 38.55376 ? 267 ARG A N   1 
ATOM   2052 C  CA  . ARG A 1 267 ? -6.01161  -18.36490 7.51558   1.000 34.87094 ? 267 ARG A CA  1 
ATOM   2053 C  C   . ARG A 1 267 ? -5.71158  -17.58112 8.79441   1.000 33.90950 ? 267 ARG A C   1 
ATOM   2054 O  O   . ARG A 1 267 ? -5.01192  -16.56782 8.76740   1.000 37.89519 ? 267 ARG A O   1 
ATOM   2055 C  CB  . ARG A 1 267 ? -5.03410  -19.53703 7.38040   1.000 36.83881 ? 267 ARG A CB  1 
ATOM   2056 C  CG  . ARG A 1 267 ? -3.55769  -19.16900 7.49697   1.000 39.55154 ? 267 ARG A CG  1 
ATOM   2057 C  CD  . ARG A 1 267 ? -2.66938  -20.34524 7.15028   1.000 42.43804 ? 267 ARG A CD  1 
ATOM   2058 N  NE  . ARG A 1 267 ? -2.60349  -20.67292 5.72946   1.000 55.54718 ? 267 ARG A NE  1 
ATOM   2059 C  CZ  . ARG A 1 267 ? -1.82075  -20.06283 4.84553   1.000 61.23759 ? 267 ARG A CZ  1 
ATOM   2060 N  NH1 . ARG A 1 267 ? -1.06869  -19.02410 5.18556   1.000 46.18477 ? 267 ARG A NH1 1 
ATOM   2061 N  NH2 . ARG A 1 267 ? -1.77477  -20.52055 3.59323   1.000 57.35629 ? 267 ARG A NH2 1 
ATOM   2062 N  N   . ARG A 1 268 ? -6.26379  -18.06123 9.91603   1.000 39.01675 ? 268 ARG A N   1 
ATOM   2063 C  CA  . ARG A 1 268 ? -5.82722  -17.62218 11.24054  1.000 40.22978 ? 268 ARG A CA  1 
ATOM   2064 C  C   . ARG A 1 268 ? -4.32582  -17.73966 11.42919  1.000 39.77852 ? 268 ARG A C   1 
ATOM   2065 O  O   . ARG A 1 268 ? -3.70601  -18.72013 11.02051  1.000 44.49143 ? 268 ARG A O   1 
ATOM   2066 C  CB  . ARG A 1 268 ? -6.52801  -18.42194 12.35175  1.000 42.05064 ? 268 ARG A CB  1 
ATOM   2067 C  CG  . ARG A 1 268 ? -6.63271  -17.59846 13.65875  1.000 50.81538 ? 268 ARG A CG  1 
ATOM   2068 C  CD  . ARG A 1 268 ? -7.52224  -18.14971 14.79937  1.000 52.52841 ? 268 ARG A CD  1 
ATOM   2069 N  NE  . ARG A 1 268 ? -7.98925  -19.51851 14.60870  1.000 62.36790 ? 268 ARG A NE  1 
ATOM   2070 C  CZ  . ARG A 1 268 ? -9.25977  -19.88732 14.72903  1.000 59.93605 ? 268 ARG A CZ  1 
ATOM   2071 N  NH1 . ARG A 1 268 ? -10.18298 -19.04993 15.17050  1.000 66.23196 ? 268 ARG A NH1 1 
ATOM   2072 N  NH2 . ARG A 1 268 ? -9.61128  -21.12785 14.41541  1.000 54.51947 ? 268 ARG A NH2 1 
ATOM   2073 N  N   . VAL A 1 269 ? -3.76693  -16.72951 12.09189  1.000 41.85025 ? 269 VAL A N   1 
ATOM   2074 C  CA  . VAL A 1 269 ? -2.49450  -16.81097 12.79534  1.000 48.48439 ? 269 VAL A CA  1 
ATOM   2075 C  C   . VAL A 1 269 ? -2.82382  -16.64463 14.27269  1.000 45.27796 ? 269 VAL A C   1 
ATOM   2076 O  O   . VAL A 1 269 ? -3.24962  -15.56846 14.70967  1.000 43.15751 ? 269 VAL A O   1 
ATOM   2077 C  CB  . VAL A 1 269 ? -1.49536  -15.74306 12.33062  1.000 46.98947 ? 269 VAL A CB  1 
ATOM   2078 C  CG1 . VAL A 1 269 ? -0.10109  -16.06480 12.86248  1.000 54.42553 ? 269 VAL A CG1 1 
ATOM   2079 C  CG2 . VAL A 1 269 ? -1.47526  -15.64099 10.82552  1.000 48.74161 ? 269 VAL A CG2 1 
ATOM   2080 N  N   . GLU A 1 270 ? -2.62552  -17.70738 15.04151  1.000 53.55830 ? 270 GLU A N   1 
ATOM   2081 C  CA  . GLU A 1 270 ? -3.09653  -17.73283 16.42125  1.000 59.35380 ? 270 GLU A CA  1 
ATOM   2082 C  C   . GLU A 1 270 ? -2.30937  -16.76213 17.29334  1.000 48.55273 ? 270 GLU A C   1 
ATOM   2083 O  O   . GLU A 1 270 ? -2.89568  -15.98206 18.04857  1.000 52.50680 ? 270 GLU A O   1 
ATOM   2084 C  CB  . GLU A 1 270 ? -3.00409  -19.16350 16.95488  1.000 61.89308 ? 270 GLU A CB  1 
ATOM   2085 C  CG  . GLU A 1 270 ? -4.10501  -19.54908 17.92886  1.000 67.28490 ? 270 GLU A CG  1 
ATOM   2086 C  CD  . GLU A 1 270 ? -3.65251  -19.48864 19.37331  1.000 76.60419 ? 270 GLU A CD  1 
ATOM   2087 O  OE1 . GLU A 1 270 ? -4.39895  -19.97461 20.25186  1.000 80.03456 ? 270 GLU A OE1 1 
ATOM   2088 O  OE2 . GLU A 1 270 ? -2.54351  -18.96746 19.62647  1.000 82.77749 ? 270 GLU A OE2 1 
ATOM   2089 N  N   . GLU A 1 271 ? -0.97813  -16.77868 17.17475  1.000 56.37672 ? 271 GLU A N   1 
ATOM   2090 C  CA  . GLU A 1 271 ? -0.11480  -15.95285 18.01992  1.000 56.95165 ? 271 GLU A CA  1 
ATOM   2091 C  C   . GLU A 1 271 ? -0.43896  -14.46610 17.90731  1.000 58.78424 ? 271 GLU A C   1 
ATOM   2092 O  O   . GLU A 1 271 ? -0.43399  -13.74613 18.91442  1.000 59.65584 ? 271 GLU A O   1 
ATOM   2093 C  CB  . GLU A 1 271 ? 1.35274   -16.20168 17.66662  1.000 61.43730 ? 271 GLU A CB  1 
ATOM   2094 C  CG  . GLU A 1 271 ? 1.67078   -17.62598 17.17564  1.000 79.27807 ? 271 GLU A CG  1 
ATOM   2095 C  CD  . GLU A 1 271 ? 1.38498   -17.85610 15.69092  1.000 79.95506 ? 271 GLU A CD  1 
ATOM   2096 O  OE1 . GLU A 1 271 ? 0.19337   -17.89633 15.31712  1.000 73.11482 ? 271 GLU A OE1 1 
ATOM   2097 O  OE2 . GLU A 1 271 ? 2.34748   -18.00293 14.90132  1.000 83.53941 ? 271 GLU A OE2 1 
ATOM   2098 N  N   . ALA A 1 272 ? -0.71461  -13.98135 16.69925  1.000 49.51366 ? 272 ALA A N   1 
ATOM   2099 C  CA  . ALA A 1 272 ? -0.94241  -12.56422 16.47617  1.000 37.52882 ? 272 ALA A CA  1 
ATOM   2100 C  C   . ALA A 1 272 ? -2.42305  -12.18284 16.46650  1.000 39.23147 ? 272 ALA A C   1 
ATOM   2101 O  O   . ALA A 1 272 ? -2.75244  -11.03081 16.15887  1.000 34.87162 ? 272 ALA A O   1 
ATOM   2102 C  CB  . ALA A 1 272 ? -0.27780  -12.14595 15.17055  1.000 38.31004 ? 272 ALA A CB  1 
ATOM   2103 N  N   . LEU A 1 273 ? -3.31233  -13.11969 16.78981  1.000 38.08925 ? 273 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 273 ? -4.76228  -12.90619 16.85282  1.000 39.35385 ? 273 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 273 ? -5.27041  -12.16233 15.61836  1.000 33.72834 ? 273 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 273 ? -5.79154  -11.05072 15.68469  1.000 35.09866 ? 273 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 273 ? -5.15342  -12.17626 18.13963  1.000 35.38332 ? 273 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 273 ? -4.56338  -12.82953 19.38378  1.000 43.20927 ? 273 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 273 ? -4.88974  -12.02265 20.62828  1.000 46.49702 ? 273 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 273 ? -5.06402  -14.25184 19.50530  1.000 51.50391 ? 273 LEU A CD2 1 
ATOM   2111 N  N   . GLY A 1 274 ? -5.12042  -12.80618 14.47502  1.000 32.26704 ? 274 GLY A N   1 
ATOM   2112 C  CA  . GLY A 1 274 ? -5.54420  -12.16541 13.25601  1.000 29.97931 ? 274 GLY A CA  1 
ATOM   2113 C  C   . GLY A 1 274 ? -5.58977  -13.15981 12.12507  1.000 38.80908 ? 274 GLY A C   1 
ATOM   2114 O  O   . GLY A 1 274 ? -5.51008  -14.36914 12.33046  1.000 34.58909 ? 274 GLY A O   1 
ATOM   2115 N  N   . VAL A 1 275 ? -5.70848  -12.62057 10.92165  1.000 34.14025 ? 275 VAL A N   1 
ATOM   2116 C  CA  . VAL A 1 275 ? -5.86704  -13.40325 9.70964   1.000 32.86927 ? 275 VAL A CA  1 
ATOM   2117 C  C   . VAL A 1 275 ? -4.83691  -12.90667 8.71212   1.000 28.74044 ? 275 VAL A C   1 
ATOM   2118 O  O   . VAL A 1 275 ? -4.59575  -11.70101 8.60874   1.000 27.60239 ? 275 VAL A O   1 
ATOM   2119 C  CB  . VAL A 1 275 ? -7.30079  -13.27206 9.15381   1.000 32.72147 ? 275 VAL A CB  1 
ATOM   2120 C  CG1 . VAL A 1 275 ? -7.39288  -13.83474 7.74785   1.000 32.60939 ? 275 VAL A CG1 1 
ATOM   2121 C  CG2 . VAL A 1 275 ? -8.27889  -14.00242 10.07250  1.000 33.82287 ? 275 VAL A CG2 1 
ATOM   2122 N  N   . VAL A 1 276 ? -4.18259  -13.82672 8.02206   1.000 32.99891 ? 276 VAL A N   1 
ATOM   2123 C  CA  . VAL A 1 276 ? -3.27533  -13.43833 6.95608   1.000 30.61741 ? 276 VAL A CA  1 
ATOM   2124 C  C   . VAL A 1 276 ? -3.96036  -13.78580 5.65498   1.000 31.64334 ? 276 VAL A C   1 
ATOM   2125 O  O   . VAL A 1 276 ? -4.88740  -14.60020 5.60734   1.000 34.17333 ? 276 VAL A O   1 
ATOM   2126 C  CB  . VAL A 1 276 ? -1.88453  -14.10524 7.02834   1.000 30.97847 ? 276 VAL A CB  1 
ATOM   2127 C  CG1 . VAL A 1 276 ? -1.01592  -13.44210 8.06115   1.000 32.37284 ? 276 VAL A CG1 1 
ATOM   2128 C  CG2 . VAL A 1 276 ? -1.99835  -15.62349 7.24552   1.000 38.20493 ? 276 VAL A CG2 1 
ATOM   2129 N  N   . ALA A 1 277 ? -3.50471  -13.14618 4.58590   1.000 31.43022 ? 277 ALA A N   1 
ATOM   2130 C  CA  . ALA A 1 277 ? -4.04797  -13.44226 3.27179   1.000 33.41661 ? 277 ALA A CA  1 
ATOM   2131 C  C   . ALA A 1 277 ? -2.98927  -13.08606 2.25731   1.000 28.26897 ? 277 ALA A C   1 
ATOM   2132 O  O   . ALA A 1 277 ? -2.09124  -12.29816 2.53647   1.000 34.49372 ? 277 ALA A O   1 
ATOM   2133 C  CB  . ALA A 1 277 ? -5.33558  -12.66333 2.99378   1.000 28.82104 ? 277 ALA A CB  1 
ATOM   2134 N  N   A ARG A 1 278 ? -3.11420  -13.63720 1.05965   0.505 31.28630 ? 278 ARG A N   1 
ATOM   2135 N  N   B ARG A 1 278 ? -3.10456  -13.69516 1.08106   0.495 31.34133 ? 278 ARG A N   1 
ATOM   2136 C  CA  A ARG A 1 278 ? -2.13492  -13.33842 0.02792   0.505 38.18832 ? 278 ARG A CA  1 
ATOM   2137 C  CA  B ARG A 1 278 ? -2.20861  -13.45206 -0.03620  0.495 38.27101 ? 278 ARG A CA  1 
ATOM   2138 C  C   A ARG A 1 278 ? -2.85835  -13.08467 -1.28451  0.505 38.37159 ? 278 ARG A C   1 
ATOM   2139 C  C   B ARG A 1 278 ? -3.02114  -12.97327 -1.22975  0.495 38.21365 ? 278 ARG A C   1 
ATOM   2140 O  O   A ARG A 1 278 ? -3.78246  -13.82004 -1.64014  0.505 37.63096 ? 278 ARG A O   1 
ATOM   2141 O  O   B ARG A 1 278 ? -4.13865  -13.44515 -1.45833  0.495 37.38912 ? 278 ARG A O   1 
ATOM   2142 C  CB  A ARG A 1 278 ? -1.10799  -14.47821 -0.07832  0.505 37.87234 ? 278 ARG A CB  1 
ATOM   2143 C  CB  B ARG A 1 278 ? -1.41800  -14.72922 -0.40448  0.495 37.54873 ? 278 ARG A CB  1 
ATOM   2144 C  CG  A ARG A 1 278 ? -1.11444  -15.28572 -1.35725  0.505 37.24190 ? 278 ARG A CG  1 
ATOM   2145 C  CG  B ARG A 1 278 ? 0.01405   -14.46835 -0.84773  0.495 39.17724 ? 278 ARG A CG  1 
ATOM   2146 C  CD  A ARG A 1 278 ? -0.25467  -16.52388 -1.17360  0.505 42.51912 ? 278 ARG A CD  1 
ATOM   2147 C  CD  B ARG A 1 278 ? 0.79844   -15.75096 -1.15725  0.495 37.78539 ? 278 ARG A CD  1 
ATOM   2148 N  NE  A ARG A 1 278 ? -0.99067  -17.77788 -1.31090  0.505 42.11675 ? 278 ARG A NE  1 
ATOM   2149 N  NE  B ARG A 1 278 ? 0.09358   -16.75021 -1.96140  0.495 46.25323 ? 278 ARG A NE  1 
ATOM   2150 C  CZ  A ARG A 1 278 ? -1.02081  -18.72757 -0.38554  0.505 40.30182 ? 278 ARG A CZ  1 
ATOM   2151 C  CZ  B ARG A 1 278 ? -0.28303  -16.60357 -3.22878  0.495 42.32962 ? 278 ARG A CZ  1 
ATOM   2152 N  NH1 A ARG A 1 278 ? -0.46914  -18.54868 0.80441   0.505 38.54814 ? 278 ARG A NH1 1 
ATOM   2153 N  NH1 B ARG A 1 278 ? -0.10030  -15.46794 -3.88304  0.495 45.34675 ? 278 ARG A NH1 1 
ATOM   2154 N  NH2 A ARG A 1 278 ? -1.62956  -19.87816 -0.65516  0.505 39.86545 ? 278 ARG A NH2 1 
ATOM   2155 N  NH2 B ARG A 1 278 ? -0.85138  -17.62740 -3.85875  0.495 40.60255 ? 278 ARG A NH2 1 
ATOM   2156 N  N   . LYS A 1 279 ? -2.46710  -12.01544 -1.97224  1.000 33.46124 ? 279 LYS A N   1 
ATOM   2157 C  CA  . LYS A 1 279 ? -3.08260  -11.70263 -3.25566  1.000 38.93867 ? 279 LYS A CA  1 
ATOM   2158 C  C   . LYS A 1 279 ? -2.43496  -12.56477 -4.33130  1.000 41.71972 ? 279 LYS A C   1 
ATOM   2159 O  O   . LYS A 1 279 ? -1.21205  -12.72905 -4.33172  1.000 42.61512 ? 279 LYS A O   1 
ATOM   2160 C  CB  . LYS A 1 279 ? -2.90540  -10.22198 -3.59363  1.000 38.30538 ? 279 LYS A CB  1 
ATOM   2161 C  CG  . LYS A 1 279 ? -3.03455  -9.88989  -5.06237  1.000 39.75887 ? 279 LYS A CG  1 
ATOM   2162 C  CD  . LYS A 1 279 ? -3.15831  -8.38723  -5.27245  1.000 41.19701 ? 279 LYS A CD  1 
ATOM   2163 C  CE  . LYS A 1 279 ? -3.93151  -8.06202  -6.53798  1.000 36.24491 ? 279 LYS A CE  1 
ATOM   2164 N  NZ  . LYS A 1 279 ? -4.22707  -6.61120  -6.65963  1.000 36.64449 ? 279 LYS A NZ  1 
ATOM   2165 N  N   . PRO A 1 280 ? -3.20562  -13.16527 -5.24085  1.000 43.58072 ? 280 PRO A N   1 
ATOM   2166 C  CA  . PRO A 1 280 ? -2.63234  -14.20963 -6.10532  1.000 51.53533 ? 280 PRO A CA  1 
ATOM   2167 C  C   . PRO A 1 280 ? -1.83161  -13.68446 -7.28581  1.000 59.10017 ? 280 PRO A C   1 
ATOM   2168 O  O   . PRO A 1 280 ? -1.29382  -12.57282 -7.25314  1.000 52.65315 ? 280 PRO A O   1 
ATOM   2169 C  CB  . PRO A 1 280 ? -3.86911  -14.98476 -6.58046  1.000 51.04824 ? 280 PRO A CB  1 
ATOM   2170 C  CG  . PRO A 1 280 ? -4.99531  -14.02274 -6.49132  1.000 41.45842 ? 280 PRO A CG  1 
ATOM   2171 C  CD  . PRO A 1 280 ? -4.67062  -13.09301 -5.34888  1.000 44.92673 ? 280 PRO A CD  1 
ATOM   2172 N  N   . GLU A 1 281 ? -1.73679  -14.51479 -8.32643  1.000 88.24265 ? 281 GLU A N   1 
ATOM   2173 C  CA  . GLU A 1 281 ? -1.12966  -14.14770 -9.60756  1.000 88.95128 ? 281 GLU A CA  1 
ATOM   2174 C  C   . GLU A 1 281 ? 0.27750   -13.58746 -9.40852  1.000 87.00938 ? 281 GLU A C   1 
ATOM   2175 O  O   . GLU A 1 281 ? 0.65116   -12.55607 -9.96767  1.000 95.03703 ? 281 GLU A O   1 
ATOM   2176 C  CB  . GLU A 1 281 ? -2.03426  -13.16936 -10.37389 1.000 80.01710 ? 281 GLU A CB  1 
ATOM   2177 C  CG  . GLU A 1 281 ? -1.57736  -12.78169 -11.78346 1.000 89.56421 ? 281 GLU A CG  1 
ATOM   2178 C  CD  . GLU A 1 281 ? -1.46245  -13.96193 -12.73002 1.000 93.63031 ? 281 GLU A CD  1 
ATOM   2179 O  OE1 . GLU A 1 281 ? -2.20735  -14.95011 -12.56209 1.000 97.04337 ? 281 GLU A OE1 1 
ATOM   2180 O  OE2 . GLU A 1 281 ? -0.61197  -13.89863 -13.64234 1.000 87.75975 ? 281 GLU A OE2 1 
ATOM   2181 N  N   . LYS A 1 282 ? 1.06816   -14.28565 -8.59614  1.000 76.53462 ? 282 LYS A N   1 
ATOM   2182 C  CA  . LYS A 1 282 ? 2.44706   -13.86428 -8.33733  1.000 74.96429 ? 282 LYS A CA  1 
ATOM   2183 C  C   . LYS A 1 282 ? 3.24572   -13.72297 -9.63222  1.000 85.80941 ? 282 LYS A C   1 
ATOM   2184 O  O   . LYS A 1 282 ? 3.33036   -12.63854 -10.21197 1.000 88.20703 ? 282 LYS A O   1 
ATOM   2185 C  CB  . LYS A 1 282 ? 3.16258   -14.84887 -7.41335  1.000 70.59662 ? 282 LYS A CB  1 
ATOM   2186 C  CG  . LYS A 1 282 ? 2.56172   -15.00212 -6.03910  1.000 53.70439 ? 282 LYS A CG  1 
ATOM   2187 C  CD  . LYS A 1 282 ? 3.59569   -15.60271 -5.10986  1.000 55.64147 ? 282 LYS A CD  1 
ATOM   2188 C  CE  . LYS A 1 282 ? 3.10946   -15.61582 -3.68875  1.000 48.07914 ? 282 LYS A CE  1 
ATOM   2189 N  NZ  . LYS A 1 282 ? 4.21904   -15.79241 -2.69985  1.000 52.73059 ? 282 LYS A NZ  1 
ATOM   2190 N  N   . GLU B 1 2   ? 1.56066   25.63262  68.34617  1.000 71.36237 ? 2   GLU B N   1 
ATOM   2191 C  CA  . GLU B 1 2   ? 0.49409   24.80136  67.79974  1.000 69.83479 ? 2   GLU B CA  1 
ATOM   2192 C  C   . GLU B 1 2   ? 0.76205   23.32688  68.07701  1.000 73.14168 ? 2   GLU B C   1 
ATOM   2193 O  O   . GLU B 1 2   ? 0.53746   22.47032  67.21889  1.000 77.42835 ? 2   GLU B O   1 
ATOM   2194 C  CB  . GLU B 1 2   ? 0.32738   25.03953  66.29167  1.000 75.41984 ? 2   GLU B CB  1 
ATOM   2195 C  CG  . GLU B 1 2   ? 1.54554   24.71342  65.42060  1.000 82.34899 ? 2   GLU B CG  1 
ATOM   2196 C  CD  . GLU B 1 2   ? 2.43536   25.92228  65.16400  1.000 88.61594 ? 2   GLU B CD  1 
ATOM   2197 O  OE1 . GLU B 1 2   ? 2.51870   26.80476  66.04869  1.000 89.94716 ? 2   GLU B OE1 1 
ATOM   2198 O  OE2 . GLU B 1 2   ? 3.04186   25.99818  64.06863  1.000 87.87057 ? 2   GLU B OE2 1 
ATOM   2199 N  N   . GLU B 1 3   ? 1.22920   23.02920  69.28638  1.000 55.79571 ? 3   GLU B N   1 
ATOM   2200 C  CA  . GLU B 1 3   ? 1.57694   21.67155  69.67019  1.000 51.68335 ? 3   GLU B CA  1 
ATOM   2201 C  C   . GLU B 1 3   ? 0.49089   21.09074  70.56560  1.000 47.75092 ? 3   GLU B C   1 
ATOM   2202 O  O   . GLU B 1 3   ? -0.04469  21.77331  71.44202  1.000 49.89894 ? 3   GLU B O   1 
ATOM   2203 C  CB  . GLU B 1 3   ? 2.95383   21.63100  70.35115  1.000 55.12678 ? 3   GLU B CB  1 
ATOM   2204 C  CG  . GLU B 1 3   ? 2.97400   21.89856  71.84454  1.000 60.88282 ? 3   GLU B CG  1 
ATOM   2205 C  CD  . GLU B 1 3   ? 4.16189   21.24243  72.54600  1.000 68.71163 ? 3   GLU B CD  1 
ATOM   2206 O  OE1 . GLU B 1 3   ? 4.75721   21.88526  73.44489  1.000 72.33948 ? 3   GLU B OE1 1 
ATOM   2207 O  OE2 . GLU B 1 3   ? 4.49027   20.08125  72.20738  1.000 66.13857 ? 3   GLU B OE2 1 
ATOM   2208 N  N   . ILE B 1 4   ? 0.14746   19.83649  70.31350  1.000 47.56490 ? 4   ILE B N   1 
ATOM   2209 C  CA  . ILE B 1 4   ? -0.93172  19.15110  71.00518  1.000 38.63965 ? 4   ILE B CA  1 
ATOM   2210 C  C   . ILE B 1 4   ? -0.31550  18.26740  72.07477  1.000 38.34232 ? 4   ILE B C   1 
ATOM   2211 O  O   . ILE B 1 4   ? 0.68695   17.59018  71.82230  1.000 41.13352 ? 4   ILE B O   1 
ATOM   2212 C  CB  . ILE B 1 4   ? -1.77280  18.33005  70.01571  1.000 36.97376 ? 4   ILE B CB  1 
ATOM   2213 C  CG1 . ILE B 1 4   ? -2.24536  19.22632  68.88022  1.000 42.21772 ? 4   ILE B CG1 1 
ATOM   2214 C  CG2 . ILE B 1 4   ? -2.96315  17.69671  70.70352  1.000 39.87860 ? 4   ILE B CG2 1 
ATOM   2215 C  CD1 . ILE B 1 4   ? -2.69152  18.47373  67.63460  1.000 42.27493 ? 4   ILE B CD1 1 
ATOM   2216 N  N   . TYR B 1 5   ? -0.89248  18.29006  73.27176  1.000 32.10704 ? 5   TYR B N   1 
ATOM   2217 C  CA  . TYR B 1 5   ? -0.43206  17.46420  74.38063  1.000 37.37225 ? 5   TYR B CA  1 
ATOM   2218 C  C   . TYR B 1 5   ? -1.34024  16.25578  74.52325  1.000 36.72784 ? 5   TYR B C   1 
ATOM   2219 O  O   . TYR B 1 5   ? -2.54689  16.40793  74.73113  1.000 39.60911 ? 5   TYR B O   1 
ATOM   2220 C  CB  . TYR B 1 5   ? -0.40146  18.26047  75.68122  1.000 36.03078 ? 5   TYR B CB  1 
ATOM   2221 C  CG  . TYR B 1 5   ? 0.21590   19.60963  75.46362  1.000 42.49887 ? 5   TYR B CG  1 
ATOM   2222 C  CD1 . TYR B 1 5   ? 1.56846   19.73481  75.21467  1.000 32.66738 ? 5   TYR B CD1 1 
ATOM   2223 C  CD2 . TYR B 1 5   ? -0.56438  20.75272  75.44501  1.000 41.90633 ? 5   TYR B CD2 1 
ATOM   2224 C  CE1 . TYR B 1 5   ? 2.12404   20.96510  74.99100  1.000 47.33509 ? 5   TYR B CE1 1 
ATOM   2225 C  CE2 . TYR B 1 5   ? -0.01297  21.97544  75.21421  1.000 40.85845 ? 5   TYR B CE2 1 
ATOM   2226 C  CZ  . TYR B 1 5   ? 1.32921   22.08146  74.98773  1.000 45.43107 ? 5   TYR B CZ  1 
ATOM   2227 O  OH  . TYR B 1 5   ? 1.87885   23.31840  74.74999  1.000 55.58657 ? 5   TYR B OH  1 
ATOM   2228 N  N   . TYR B 1 6   ? -0.75770  15.06358  74.42337  1.000 30.04498 ? 6   TYR B N   1 
ATOM   2229 C  CA  . TYR B 1 6   ? -1.49036  13.81687  74.57925  1.000 33.48687 ? 6   TYR B CA  1 
ATOM   2230 C  C   . TYR B 1 6   ? -1.34947  13.34104  76.01025  1.000 34.96365 ? 6   TYR B C   1 
ATOM   2231 O  O   . TYR B 1 6   ? -0.23263  13.21030  76.51392  1.000 38.54674 ? 6   TYR B O   1 
ATOM   2232 C  CB  . TYR B 1 6   ? -0.96697  12.75574  73.61959  1.000 32.16642 ? 6   TYR B CB  1 
ATOM   2233 C  CG  . TYR B 1 6   ? -1.32886  13.09884  72.20704  1.000 37.69345 ? 6   TYR B CG  1 
ATOM   2234 C  CD1 . TYR B 1 6   ? -0.53568  13.95793  71.46493  1.000 33.54006 ? 6   TYR B CD1 1 
ATOM   2235 C  CD2 . TYR B 1 6   ? -2.49207  12.61341  71.62988  1.000 32.93703 ? 6   TYR B CD2 1 
ATOM   2236 C  CE1 . TYR B 1 6   ? -0.87259  14.30143  70.19274  1.000 33.48538 ? 6   TYR B CE1 1 
ATOM   2237 C  CE2 . TYR B 1 6   ? -2.83295  12.95714  70.34542  1.000 38.56834 ? 6   TYR B CE2 1 
ATOM   2238 C  CZ  . TYR B 1 6   ? -2.01842  13.79687  69.63835  1.000 32.74795 ? 6   TYR B CZ  1 
ATOM   2239 O  OH  . TYR B 1 6   ? -2.34427  14.15945  68.36180  1.000 37.54500 ? 6   TYR B OH  1 
ATOM   2240 N  N   . ILE B 1 7   ? -2.47439  13.08106  76.65893  1.000 29.13730 ? 7   ILE B N   1 
ATOM   2241 C  CA  . ILE B 1 7   ? -2.47649  12.54541  78.00833  1.000 37.77413 ? 7   ILE B CA  1 
ATOM   2242 C  C   . ILE B 1 7   ? -3.40958  11.34801  78.06805  1.000 33.59301 ? 7   ILE B C   1 
ATOM   2243 O  O   . ILE B 1 7   ? -4.49609  11.35535  77.47847  1.000 37.17079 ? 7   ILE B O   1 
ATOM   2244 C  CB  . ILE B 1 7   ? -2.87010  13.61677  79.04585  1.000 36.32129 ? 7   ILE B CB  1 
ATOM   2245 C  CG1 . ILE B 1 7   ? -4.11808  14.35503  78.62416  1.000 35.19008 ? 7   ILE B CG1 1 
ATOM   2246 C  CG2 . ILE B 1 7   ? -1.75059  14.63401  79.17889  1.000 43.63478 ? 7   ILE B CG2 1 
ATOM   2247 C  CD1 . ILE B 1 7   ? -4.36108  15.62572  79.46978  1.000 38.20136 ? 7   ILE B CD1 1 
ATOM   2248 N  N   . THR B 1 8   ? -2.96454  10.31717  78.76623  1.000 21.58241 ? 8   THR B N   1 
ATOM   2249 C  CA  . THR B 1 8   ? -3.67576  9.07886   79.02326  1.000 32.60177 ? 8   THR B CA  1 
ATOM   2250 C  C   . THR B 1 8   ? -3.85309  8.91614   80.51824  1.000 22.28476 ? 8   THR B C   1 
ATOM   2251 O  O   . THR B 1 8   ? -3.35149  9.70254   81.31537  1.000 26.29973 ? 8   THR B O   1 
ATOM   2252 C  CB  . THR B 1 8   ? -2.88781  7.88923   78.49528  1.000 35.18760 ? 8   THR B CB  1 
ATOM   2253 O  OG1 . THR B 1 8   ? -1.78497  7.65129   79.38989  1.000 34.89193 ? 8   THR B OG1 1 
ATOM   2254 C  CG2 . THR B 1 8   ? -2.34283  8.23231   77.16030  1.000 30.76143 ? 8   THR B CG2 1 
ATOM   2255 N  N   . PHE B 1 9   ? -4.52337  7.84271   80.89855  1.000 29.50424 ? 9   PHE B N   1 
ATOM   2256 C  CA  . PHE B 1 9   ? -4.70427  7.58498   82.31583  1.000 30.51550 ? 9   PHE B CA  1 
ATOM   2257 C  C   . PHE B 1 9   ? -3.37775  7.64448   83.05222  1.000 31.43283 ? 9   PHE B C   1 
ATOM   2258 O  O   . PHE B 1 9   ? -3.32188  8.09208   84.20415  1.000 30.94101 ? 9   PHE B O   1 
ATOM   2259 C  CB  . PHE B 1 9   ? -5.37896  6.22623   82.51311  1.000 28.20554 ? 9   PHE B CB  1 
ATOM   2260 C  CG  . PHE B 1 9   ? -4.52972  5.05096   82.12019  1.000 33.80858 ? 9   PHE B CG  1 
ATOM   2261 C  CD1 . PHE B 1 9   ? -4.38602  4.68913   80.78524  1.000 33.18395 ? 9   PHE B CD1 1 
ATOM   2262 C  CD2 . PHE B 1 9   ? -3.89659  4.28702   83.08610  1.000 31.47073 ? 9   PHE B CD2 1 
ATOM   2263 C  CE1 . PHE B 1 9   ? -3.62127  3.58392   80.43310  1.000 38.42276 ? 9   PHE B CE1 1 
ATOM   2264 C  CE2 . PHE B 1 9   ? -3.12875  3.18649   82.74175  1.000 33.06805 ? 9   PHE B CE2 1 
ATOM   2265 C  CZ  . PHE B 1 9   ? -2.98991  2.83114   81.41724  1.000 37.44567 ? 9   PHE B CZ  1 
ATOM   2266 N  N   . ARG B 1 10  ? -2.29720  7.22379   82.39425  1.000 28.79773 ? 10  ARG B N   1 
ATOM   2267 C  CA  . ARG B 1 10  ? -0.99882  7.19071   83.05622  1.000 30.41448 ? 10  ARG B CA  1 
ATOM   2268 C  C   . ARG B 1 10  ? -0.53541  8.58818   83.44858  1.000 32.91975 ? 10  ARG B C   1 
ATOM   2269 O  O   . ARG B 1 10  ? 0.02131   8.79328   84.53773  1.000 26.19811 ? 10  ARG B O   1 
ATOM   2270 C  CB  . ARG B 1 10  ? 0.01213   6.54393   82.14159  1.000 26.78487 ? 10  ARG B CB  1 
ATOM   2271 C  CG  . ARG B 1 10  ? -0.23292  5.08968   81.94491  1.000 33.23790 ? 10  ARG B CG  1 
ATOM   2272 C  CD  . ARG B 1 10  ? 0.94881   4.47317   81.23874  1.000 44.56885 ? 10  ARG B CD  1 
ATOM   2273 N  NE  . ARG B 1 10  ? 0.58000   4.06708   79.88842  1.000 50.28406 ? 10  ARG B NE  1 
ATOM   2274 C  CZ  . ARG B 1 10  ? 0.45984   4.89688   78.86091  1.000 48.26251 ? 10  ARG B CZ  1 
ATOM   2275 N  NH1 . ARG B 1 10  ? 0.72329   6.19045   78.97971  1.000 40.33559 ? 10  ARG B NH1 1 
ATOM   2276 N  NH2 . ARG B 1 10  ? 0.05075   4.41977   77.68756  1.000 44.34966 ? 10  ARG B NH2 1 
ATOM   2277 N  N   . GLU B 1 11  ? -0.74800  9.56215   82.57156  1.000 30.46206 ? 11  GLU B N   1 
ATOM   2278 C  CA  . GLU B 1 11  ? -0.33157  10.91766  82.89105  1.000 34.75244 ? 11  GLU B CA  1 
ATOM   2279 C  C   . GLU B 1 11  ? -1.27382  11.53771  83.91527  1.000 31.65822 ? 11  GLU B C   1 
ATOM   2280 O  O   . GLU B 1 11  ? -0.83059  12.18400  84.87588  1.000 24.73459 ? 11  GLU B O   1 
ATOM   2281 C  CB  . GLU B 1 11  ? -0.27336  11.75273  81.60683  1.000 34.32754 ? 11  GLU B CB  1 
ATOM   2282 C  CG  . GLU B 1 11  ? 0.88697   11.34005  80.65581  1.000 34.37020 ? 11  GLU B CG  1 
ATOM   2283 C  CD  . GLU B 1 11  ? 0.59392   10.06024  79.87655  1.000 33.24378 ? 11  GLU B CD  1 
ATOM   2284 O  OE1 . GLU B 1 11  ? -0.55997  9.85770   79.45810  1.000 36.55305 ? 11  GLU B OE1 1 
ATOM   2285 O  OE2 . GLU B 1 11  ? 1.51504   9.24390   79.68765  1.000 44.32670 ? 11  GLU B OE2 1 
ATOM   2286 N  N   . ALA B 1 12  ? -2.57852  11.34469  83.71453  1.000 27.62166 ? 12  ALA B N   1 
ATOM   2287 C  CA  . ALA B 1 12  ? -3.56010  11.81518  84.67729  1.000 31.40627 ? 12  ALA B CA  1 
ATOM   2288 C  C   . ALA B 1 12  ? -3.25659  11.26359  86.05875  1.000 27.85291 ? 12  ALA B C   1 
ATOM   2289 O  O   . ALA B 1 12  ? -3.24510  12.00347  87.04643  1.000 29.94762 ? 12  ALA B O   1 
ATOM   2290 C  CB  . ALA B 1 12  ? -4.96803  11.40927  84.23094  1.000 26.51485 ? 12  ALA B CB  1 
ATOM   2291 N  N   . ARG B 1 13  ? -2.96764  9.96425   86.14569  1.000 27.32438 ? 13  ARG B N   1 
ATOM   2292 C  CA  . ARG B 1 13  ? -2.68110  9.40680   87.45881  1.000 28.23470 ? 13  ARG B CA  1 
ATOM   2293 C  C   . ARG B 1 13  ? -1.39901  9.97997   88.03791  1.000 28.73936 ? 13  ARG B C   1 
ATOM   2294 O  O   . ARG B 1 13  ? -1.31252  10.17333  89.25478  1.000 27.53921 ? 13  ARG B O   1 
ATOM   2295 C  CB  . ARG B 1 13  ? -2.61039  7.87738   87.39933  1.000 28.27627 ? 13  ARG B CB  1 
ATOM   2296 C  CG  . ARG B 1 13  ? -3.98166  7.21636   87.32009  1.000 29.44853 ? 13  ARG B CG  1 
ATOM   2297 C  CD  . ARG B 1 13  ? -3.87478  5.74992   86.98745  1.000 27.77713 ? 13  ARG B CD  1 
ATOM   2298 N  NE  . ARG B 1 13  ? -5.13588  5.21784   86.49197  1.000 23.57235 ? 13  ARG B NE  1 
ATOM   2299 C  CZ  . ARG B 1 13  ? -5.40927  3.92397   86.40372  1.000 28.08076 ? 13  ARG B CZ  1 
ATOM   2300 N  NH1 . ARG B 1 13  ? -4.56022  2.99958   86.83665  1.000 30.13799 ? 13  ARG B NH1 1 
ATOM   2301 N  NH2 . ARG B 1 13  ? -6.57950  3.54500   85.90953  1.000 32.80200 ? 13  ARG B NH2 1 
ATOM   2302 N  N   . MET B 1 14  ? -0.39180  10.26816  87.20355  1.000 31.33243 ? 14  MET B N   1 
ATOM   2303 C  CA  . MET B 1 14  ? 0.83867   10.83868  87.75964  1.000 34.01338 ? 14  MET B CA  1 
ATOM   2304 C  C   . MET B 1 14  ? 0.59260   12.24359  88.29856  1.000 30.60588 ? 14  MET B C   1 
ATOM   2305 O  O   . MET B 1 14  ? 1.08174   12.60544  89.37763  1.000 36.60081 ? 14  MET B O   1 
ATOM   2306 C  CB  . MET B 1 14  ? 1.95501   10.86358  86.71690  1.000 31.26371 ? 14  MET B CB  1 
ATOM   2307 C  CG  . MET B 1 14  ? 3.24429   11.45789  87.28249  1.000 42.36153 ? 14  MET B CG  1 
ATOM   2308 S  SD  . MET B 1 14  ? 4.17836   10.22723  88.21500  1.000 42.50292 ? 14  MET B SD  1 
ATOM   2309 C  CE  . MET B 1 14  ? 3.94047   10.75976  89.90226  1.000 37.19957 ? 14  MET B CE  1 
ATOM   2310 N  N   . LEU B 1 15  ? -0.20832  13.02564  87.58699  1.000 27.05525 ? 15  LEU B N   1 
ATOM   2311 C  CA  . LEU B 1 15  ? -0.50644  14.37599  88.03289  1.000 28.66331 ? 15  LEU B CA  1 
ATOM   2312 C  C   . LEU B 1 15  ? -1.24120  14.36279  89.35984  1.000 32.91821 ? 15  LEU B C   1 
ATOM   2313 O  O   . LEU B 1 15  ? -0.94387  15.16186  90.25307  1.000 39.07069 ? 15  LEU B O   1 
ATOM   2314 C  CB  . LEU B 1 15  ? -1.33048  15.09062  86.96871  1.000 27.75112 ? 15  LEU B CB  1 
ATOM   2315 C  CG  . LEU B 1 15  ? -0.62239  15.32293  85.63707  1.000 37.04926 ? 15  LEU B CG  1 
ATOM   2316 C  CD1 . LEU B 1 15  ? -1.65151  15.68183  84.57464  1.000 26.80621 ? 15  LEU B CD1 1 
ATOM   2317 C  CD2 . LEU B 1 15  ? 0.42099   16.41615  85.76737  1.000 29.95811 ? 15  LEU B CD2 1 
ATOM   2318 N  N   . LEU B 1 16  ? -2.19865  13.45151  89.51606  1.000 32.40384 ? 16  LEU B N   1 
ATOM   2319 C  CA  . LEU B 1 16  ? -2.94577  13.39071  90.76255  1.000 32.98452 ? 16  LEU B CA  1 
ATOM   2320 C  C   . LEU B 1 16  ? -2.07704  12.87455  91.89096  1.000 29.61787 ? 16  LEU B C   1 
ATOM   2321 O  O   . LEU B 1 16  ? -2.32025  13.20063  93.05451  1.000 38.74088 ? 16  LEU B O   1 
ATOM   2322 C  CB  . LEU B 1 16  ? -4.18332  12.51504  90.58189  1.000 33.17400 ? 16  LEU B CB  1 
ATOM   2323 C  CG  . LEU B 1 16  ? -5.07682  13.02690  89.45782  1.000 31.89716 ? 16  LEU B CG  1 
ATOM   2324 C  CD1 . LEU B 1 16  ? -6.03185  11.96272  89.02930  1.000 37.07234 ? 16  LEU B CD1 1 
ATOM   2325 C  CD2 . LEU B 1 16  ? -5.82664  14.28745  89.91100  1.000 36.11146 ? 16  LEU B CD2 1 
ATOM   2326 N  N   . ALA B 1 17  ? -1.05313  12.08296  91.57168  1.000 32.61737 ? 17  ALA B N   1 
ATOM   2327 C  CA  . ALA B 1 17  ? -0.16911  11.56887  92.60787  1.000 31.99799 ? 17  ALA B CA  1 
ATOM   2328 C  C   . ALA B 1 17  ? 0.88312   12.57597  93.03971  1.000 37.93449 ? 17  ALA B C   1 
ATOM   2329 O  O   . ALA B 1 17  ? 1.40840   12.45760  94.15501  1.000 50.88343 ? 17  ALA B O   1 
ATOM   2330 C  CB  . ALA B 1 17  ? 0.51781   10.29010  92.13497  1.000 36.78260 ? 17  ALA B CB  1 
ATOM   2331 N  N   . SER B 1 18  ? 1.17990   13.57234  92.20687  1.000 38.32954 ? 18  SER B N   1 
ATOM   2332 C  CA  . SER B 1 18  ? 2.20830   14.56175  92.49891  1.000 39.01702 ? 18  SER B CA  1 
ATOM   2333 C  C   . SER B 1 18  ? 1.59496   15.86021  93.00903  1.000 41.92440 ? 18  SER B C   1 
ATOM   2334 O  O   . SER B 1 18  ? 0.46600   16.22039  92.66901  1.000 49.17633 ? 18  SER B O   1 
ATOM   2335 C  CB  . SER B 1 18  ? 3.04015   14.87657  91.25695  1.000 38.95527 ? 18  SER B CB  1 
ATOM   2336 O  OG  . SER B 1 18  ? 3.23185   13.73961  90.43132  1.000 40.54473 ? 18  SER B OG  1 
ATOM   2337 N  N   . ARG B 1 19  ? 2.36398   16.57226  93.81129  1.000 42.79824 ? 19  ARG B N   1 
ATOM   2338 C  CA  . ARG B 1 19  ? 2.09639   17.96636  94.10237  1.000 54.53905 ? 19  ARG B CA  1 
ATOM   2339 C  C   . ARG B 1 19  ? 3.28336   18.79794  93.64563  1.000 53.67416 ? 19  ARG B C   1 
ATOM   2340 O  O   . ARG B 1 19  ? 4.41335   18.31082  93.57905  1.000 55.65465 ? 19  ARG B O   1 
ATOM   2341 C  CB  . ARG B 1 19  ? 1.82003   18.20543  95.58814  1.000 59.34787 ? 19  ARG B CB  1 
ATOM   2342 C  CG  . ARG B 1 19  ? 1.08378   19.51150  95.79899  1.000 75.44246 ? 19  ARG B CG  1 
ATOM   2343 C  CD  . ARG B 1 19  ? 0.69525   19.80690  97.24139  1.000 79.92344 ? 19  ARG B CD  1 
ATOM   2344 N  NE  . ARG B 1 19  ? -0.74132  20.04393  97.35770  1.000 86.31628 ? 19  ARG B NE  1 
ATOM   2345 C  CZ  . ARG B 1 19  ? -1.41455  21.00025  96.72473  1.000 89.06477 ? 19  ARG B CZ  1 
ATOM   2346 N  NH1 . ARG B 1 19  ? -0.80907  21.87448  95.93224  1.000 79.68713 ? 19  ARG B NH1 1 
ATOM   2347 N  NH2 . ARG B 1 19  ? -2.73333  21.07971  96.88701  1.000 88.71292 ? 19  ARG B NH2 1 
ATOM   2348 N  N   . GLY B 1 20  ? 3.01695   20.04425  93.29919  1.000 61.53184 ? 20  GLY B N   1 
ATOM   2349 C  CA  . GLY B 1 20  ? 4.06626   20.87933  92.74361  1.000 65.29860 ? 20  GLY B CA  1 
ATOM   2350 C  C   . GLY B 1 20  ? 4.17802   20.66966  91.24812  1.000 64.45087 ? 20  GLY B C   1 
ATOM   2351 O  O   . GLY B 1 20  ? 3.18856   20.78017  90.51708  1.000 58.46990 ? 20  GLY B O   1 
ATOM   2352 N  N   . ASN B 1 21  ? 5.38402   20.35696  90.78617  1.000 57.72388 ? 21  ASN B N   1 
ATOM   2353 C  CA  . ASN B 1 21  ? 5.68713   20.29575  89.36699  1.000 52.02208 ? 21  ASN B CA  1 
ATOM   2354 C  C   . ASN B 1 21  ? 6.14864   18.88992  89.01534  1.000 53.89801 ? 21  ASN B C   1 
ATOM   2355 O  O   . ASN B 1 21  ? 6.67857   18.17147  89.86313  1.000 60.35590 ? 21  ASN B O   1 
ATOM   2356 C  CB  . ASN B 1 21  ? 6.74626   21.31675  89.01263  1.000 53.10459 ? 21  ASN B CB  1 
ATOM   2357 C  CG  . ASN B 1 21  ? 6.15431   22.68942  88.77221  1.000 64.12289 ? 21  ASN B CG  1 
ATOM   2358 O  OD1 . ASN B 1 21  ? 5.07909   23.00774  89.28216  1.000 63.58827 ? 21  ASN B OD1 1 
ATOM   2359 N  ND2 . ASN B 1 21  ? 6.87332   23.52763  88.04161  1.000 74.89131 ? 21  ASN B ND2 1 
ATOM   2360 N  N   . VAL B 1 22  ? 5.91929   18.48554  87.76905  1.000 50.66912 ? 22  VAL B N   1 
ATOM   2361 C  CA  . VAL B 1 22  ? 6.17398   17.10562  87.37316  1.000 48.58948 ? 22  VAL B CA  1 
ATOM   2362 C  C   . VAL B 1 22  ? 6.51248   17.06724  85.89210  1.000 50.12537 ? 22  VAL B C   1 
ATOM   2363 O  O   . VAL B 1 22  ? 5.96585   17.83214  85.09365  1.000 47.70788 ? 22  VAL B O   1 
ATOM   2364 C  CB  . VAL B 1 22  ? 4.97608   16.19032  87.70496  1.000 47.20709 ? 22  VAL B CB  1 
ATOM   2365 C  CG1 . VAL B 1 22  ? 3.77263   16.55978  86.86281  1.000 44.14086 ? 22  VAL B CG1 1 
ATOM   2366 C  CG2 . VAL B 1 22  ? 5.35171   14.73156  87.49631  1.000 45.46860 ? 22  VAL B CG2 1 
ATOM   2367 N  N   . LYS B 1 23  ? 7.43869   16.17356  85.54392  1.000 53.93287 ? 23  LYS B N   1 
ATOM   2368 C  CA  . LYS B 1 23  ? 7.90251   15.98026  84.17662  1.000 42.03966 ? 23  LYS B CA  1 
ATOM   2369 C  C   . LYS B 1 23  ? 7.06949   14.88915  83.53173  1.000 43.00971 ? 23  LYS B C   1 
ATOM   2370 O  O   . LYS B 1 23  ? 6.99694   13.77245  84.05405  1.000 49.16118 ? 23  LYS B O   1 
ATOM   2371 C  CB  . LYS B 1 23  ? 9.38261   15.60057  84.15297  1.000 37.20017 ? 23  LYS B CB  1 
ATOM   2372 C  CG  . LYS B 1 23  ? 10.29524  16.70871  84.61783  1.000 45.41162 ? 23  LYS B CG  1 
ATOM   2373 C  CD  . LYS B 1 23  ? 9.66403   18.08572  84.40028  1.000 50.04826 ? 23  LYS B CD  1 
ATOM   2374 C  CE  . LYS B 1 23  ? 10.52642  19.15876  85.03737  1.000 56.50930 ? 23  LYS B CE  1 
ATOM   2375 N  NZ  . LYS B 1 23  ? 11.93571  19.03702  84.55035  1.000 49.74237 ? 23  LYS B NZ  1 
ATOM   2376 N  N   . LEU B 1 24  ? 6.44635   15.21211  82.40365  1.000 41.61904 ? 24  LEU B N   1 
ATOM   2377 C  CA  . LEU B 1 24  ? 5.50419   14.31708  81.75243  1.000 41.41885 ? 24  LEU B CA  1 
ATOM   2378 C  C   . LEU B 1 24  ? 5.84234   14.18819  80.27821  1.000 40.61027 ? 24  LEU B C   1 
ATOM   2379 O  O   . LEU B 1 24  ? 6.22537   15.16582  79.62980  1.000 38.81359 ? 24  LEU B O   1 
ATOM   2380 C  CB  . LEU B 1 24  ? 4.06795   14.82489  81.89506  1.000 37.71019 ? 24  LEU B CB  1 
ATOM   2381 C  CG  . LEU B 1 24  ? 3.41315   14.60210  83.25599  1.000 36.09688 ? 24  LEU B CG  1 
ATOM   2382 C  CD1 . LEU B 1 24  ? 1.93547   14.56619  83.07119  1.000 34.81249 ? 24  LEU B CD1 1 
ATOM   2383 C  CD2 . LEU B 1 24  ? 3.89485   13.30500  83.85252  1.000 45.01146 ? 24  LEU B CD2 1 
ATOM   2384 N  N   . ASN B 1 25  ? 5.69015   12.98306  79.74997  1.000 40.29072 ? 25  ASN B N   1 
ATOM   2385 C  CA  . ASN B 1 25  ? 5.68293   12.82022  78.31051  1.000 38.82449 ? 25  ASN B CA  1 
ATOM   2386 C  C   . ASN B 1 25  ? 4.28970   13.11059  77.78002  1.000 37.24614 ? 25  ASN B C   1 
ATOM   2387 O  O   . ASN B 1 25  ? 3.29390   12.64562  78.34079  1.000 42.14324 ? 25  ASN B O   1 
ATOM   2388 C  CB  . ASN B 1 25  ? 6.10889   11.42148  77.90673  1.000 42.94084 ? 25  ASN B CB  1 
ATOM   2389 C  CG  . ASN B 1 25  ? 5.96122   11.20735  76.42430  1.000 45.27622 ? 25  ASN B CG  1 
ATOM   2390 O  OD1 . ASN B 1 25  ? 4.92317   10.73764  75.95690  1.000 47.66261 ? 25  ASN B OD1 1 
ATOM   2391 N  ND2 . ASN B 1 25  ? 6.95587   11.63381  75.66906  1.000 45.76735 ? 25  ASN B ND2 1 
ATOM   2392 N  N   . LEU B 1 26  ? 4.21651   13.88987  76.70268  1.000 39.48376 ? 26  LEU B N   1 
ATOM   2393 C  CA  . LEU B 1 26  ? 2.93365   14.33408  76.17218  1.000 37.01243 ? 26  LEU B CA  1 
ATOM   2394 C  C   . LEU B 1 26  ? 2.79193   14.02033  74.68711  1.000 37.33465 ? 26  LEU B C   1 
ATOM   2395 O  O   . LEU B 1 26  ? 2.10227   14.74355  73.96800  1.000 36.65842 ? 26  LEU B O   1 
ATOM   2396 C  CB  . LEU B 1 26  ? 2.72698   15.82745  76.43126  1.000 30.43058 ? 26  LEU B CB  1 
ATOM   2397 C  CG  . LEU B 1 26  ? 2.87939   16.26477  77.89703  1.000 36.32974 ? 26  LEU B CG  1 
ATOM   2398 C  CD1 . LEU B 1 26  ? 2.97049   17.78263  78.04638  1.000 36.42204 ? 26  LEU B CD1 1 
ATOM   2399 C  CD2 . LEU B 1 26  ? 1.74816   15.72379  78.76561  1.000 32.87640 ? 26  LEU B CD2 1 
ATOM   2400 N  N   . ASP B 1 27  ? 3.43725   12.94926  74.20349  1.000 40.06679 ? 27  ASP B N   1 
ATOM   2401 C  CA  . ASP B 1 27  ? 3.17007   12.46333  72.85274  1.000 42.32752 ? 27  ASP B CA  1 
ATOM   2402 C  C   . ASP B 1 27  ? 3.01714   10.94622  72.81645  1.000 41.42411 ? 27  ASP B C   1 
ATOM   2403 O  O   . ASP B 1 27  ? 3.30522   10.31600  71.79866  1.000 34.85457 ? 27  ASP B O   1 
ATOM   2404 C  CB  . ASP B 1 27  ? 4.24520   12.90999  71.86316  1.000 43.47555 ? 27  ASP B CB  1 
ATOM   2405 C  CG  . ASP B 1 27  ? 5.65714   12.60197  72.33544  1.000 49.36578 ? 27  ASP B CG  1 
ATOM   2406 O  OD1 . ASP B 1 27  ? 5.86791   11.60784  73.06003  1.000 45.72378 ? 27  ASP B OD1 1 
ATOM   2407 O  OD2 . ASP B 1 27  ? 6.56028   13.37197  71.96422  1.000 53.13106 ? 27  ASP B OD2 1 
ATOM   2408 N  N   . LEU B 1 28  ? 2.54206   10.35016  73.91010  1.000 39.99046 ? 28  LEU B N   1 
ATOM   2409 C  CA  . LEU B 1 28  ? 2.26566   8.91261   73.97231  1.000 41.93679 ? 28  LEU B CA  1 
ATOM   2410 C  C   . LEU B 1 28  ? 3.55346   8.11374   73.81953  1.000 42.96375 ? 28  LEU B C   1 
ATOM   2411 O  O   . LEU B 1 28  ? 3.58898   7.07933   73.15410  1.000 43.75065 ? 28  LEU B O   1 
ATOM   2412 C  CB  . LEU B 1 28  ? 1.23448   8.47890   72.92441  1.000 40.94358 ? 28  LEU B CB  1 
ATOM   2413 C  CG  . LEU B 1 28  ? -0.16786  9.08164   72.98204  1.000 38.63812 ? 28  LEU B CG  1 
ATOM   2414 C  CD1 . LEU B 1 28  ? -0.98700  8.60568   71.82815  1.000 36.42611 ? 28  LEU B CD1 1 
ATOM   2415 C  CD2 . LEU B 1 28  ? -0.86095  8.67291   74.23442  1.000 26.35247 ? 28  LEU B CD2 1 
ATOM   2416 N  N   . ARG B 1 29  ? 4.61758   8.61729   74.43186  1.000 46.58676 ? 29  ARG B N   1 
ATOM   2417 C  CA  . ARG B 1 29  ? 5.94121   8.00537   74.43044  1.000 50.19837 ? 29  ARG B CA  1 
ATOM   2418 C  C   . ARG B 1 29  ? 6.51818   7.91073   73.03394  1.000 55.82261 ? 29  ARG B C   1 
ATOM   2419 O  O   . ARG B 1 29  ? 7.38377   7.06815   72.77617  1.000 66.86188 ? 29  ARG B O   1 
ATOM   2420 C  CB  . ARG B 1 29  ? 5.93204   6.61547   75.08975  1.000 59.01063 ? 29  ARG B CB  1 
ATOM   2421 C  CG  . ARG B 1 29  ? 5.35686   6.56413   76.52530  1.000 63.29336 ? 29  ARG B CG  1 
ATOM   2422 C  CD  . ARG B 1 29  ? 5.53298   7.88959   77.26132  1.000 73.19789 ? 29  ARG B CD  1 
ATOM   2423 N  NE  . ARG B 1 29  ? 5.72657   7.74540   78.69711  1.000 68.83286 ? 29  ARG B NE  1 
ATOM   2424 C  CZ  . ARG B 1 29  ? 6.88940   7.45736   79.26378  1.000 70.42010 ? 29  ARG B CZ  1 
ATOM   2425 N  NH1 . ARG B 1 29  ? 7.97871   7.24579   78.53863  1.000 66.59349 ? 29  ARG B NH1 1 
ATOM   2426 N  NH2 . ARG B 1 29  ? 6.96249   7.38461   80.58981  1.000 75.77886 ? 29  ARG B NH2 1 
ATOM   2427 N  N   . LYS B 1 30  ? 6.05132   8.74913   72.10524  1.000 56.83410 ? 30  LYS B N   1 
ATOM   2428 C  CA  . LYS B 1 30  ? 6.65921   8.72851   70.78187  1.000 54.17887 ? 30  LYS B CA  1 
ATOM   2429 C  C   . LYS B 1 30  ? 8.06670   9.29883   70.81709  1.000 63.18671 ? 30  LYS B C   1 
ATOM   2430 O  O   . LYS B 1 30  ? 8.92053   8.86992   70.03427  1.000 61.54189 ? 30  LYS B O   1 
ATOM   2431 C  CB  . LYS B 1 30  ? 5.81044   9.49032   69.75952  1.000 45.96662 ? 30  LYS B CB  1 
ATOM   2432 C  CG  . LYS B 1 30  ? 6.30939   9.32002   68.30904  1.000 51.49529 ? 30  LYS B CG  1 
ATOM   2433 C  CD  . LYS B 1 30  ? 5.89582   10.48274  67.41975  1.000 51.74188 ? 30  LYS B CD  1 
ATOM   2434 C  CE  . LYS B 1 30  ? 6.27872   10.26386  65.93139  1.000 57.81545 ? 30  LYS B CE  1 
ATOM   2435 N  NZ  . LYS B 1 30  ? 6.69533   8.86290   65.57770  1.000 62.04955 ? 30  LYS B NZ  1 
ATOM   2436 N  N   . THR B 1 31  ? 8.33870   10.23300  71.72993  1.000 62.89525 ? 31  THR B N   1 
ATOM   2437 C  CA  . THR B 1 31  ? 9.58776   10.98011  71.69599  1.000 72.33421 ? 31  THR B CA  1 
ATOM   2438 C  C   . THR B 1 31  ? 10.38471  10.90637  72.99896  1.000 77.19865 ? 31  THR B C   1 
ATOM   2439 O  O   . THR B 1 31  ? 11.59815  11.16310  72.97129  1.000 80.57646 ? 31  THR B O   1 
ATOM   2440 C  CB  . THR B 1 31  ? 9.29520   12.44903  71.33704  1.000 74.77686 ? 31  THR B CB  1 
ATOM   2441 O  OG1 . THR B 1 31  ? 8.81269   12.50481  69.99065  1.000 73.45471 ? 31  THR B OG1 1 
ATOM   2442 C  CG2 . THR B 1 31  ? 10.55374  13.31217  71.36597  1.000 80.59091 ? 31  THR B CG2 1 
ATOM   2443 N  N   . ASN B 1 32  ? 9.76247   10.53654  74.12597  1.000 78.26498 ? 32  ASN B N   1 
ATOM   2444 C  CA  . ASN B 1 32  ? 10.43946  10.38056  75.41777  1.000 83.10845 ? 32  ASN B CA  1 
ATOM   2445 C  C   . ASN B 1 32  ? 10.91460  11.72112  75.96654  1.000 77.04774 ? 32  ASN B C   1 
ATOM   2446 O  O   . ASN B 1 32  ? 11.34739  11.81055  77.11916  1.000 73.56933 ? 32  ASN B O   1 
ATOM   2447 C  CB  . ASN B 1 32  ? 11.61266  9.39801   75.31850  1.000 88.78640 ? 32  ASN B CB  1 
ATOM   2448 C  CG  . ASN B 1 32  ? 11.21489  8.07289   74.68894  1.000 92.45647 ? 32  ASN B CG  1 
ATOM   2449 O  OD1 . ASN B 1 32  ? 10.42769  8.03209   73.73969  1.000 91.17746 ? 32  ASN B OD1 1 
ATOM   2450 N  ND2 . ASN B 1 32  ? 11.75850  6.98051   75.21586  1.000 95.15155 ? 32  ASN B ND2 1 
ATOM   2451 N  N   . ARG B 1 33  ? 10.87081  12.75070  75.12790  1.000 66.72334 ? 33  ARG B N   1 
ATOM   2452 C  CA  . ARG B 1 33  ? 10.84554  14.14394  75.54715  1.000 60.20451 ? 33  ARG B CA  1 
ATOM   2453 C  C   . ARG B 1 33  ? 9.86024   14.35448  76.68766  1.000 47.10018 ? 33  ARG B C   1 
ATOM   2454 O  O   . ARG B 1 33  ? 8.65611   14.13723  76.53260  1.000 47.01413 ? 33  ARG B O   1 
ATOM   2455 C  CB  . ARG B 1 33  ? 10.44437  14.99216  74.34491  1.000 56.44400 ? 33  ARG B CB  1 
ATOM   2456 C  CG  . ARG B 1 33  ? 10.60745  16.48215  74.44169  1.000 54.69106 ? 33  ARG B CG  1 
ATOM   2457 C  CD  . ARG B 1 33  ? 9.40273   17.08108  73.71127  1.000 55.59605 ? 33  ARG B CD  1 
ATOM   2458 N  NE  . ARG B 1 33  ? 9.41422   18.52129  73.47096  1.000 62.87958 ? 33  ARG B NE  1 
ATOM   2459 C  CZ  . ARG B 1 33  ? 9.66597   19.46657  74.36855  1.000 58.73832 ? 33  ARG B CZ  1 
ATOM   2460 N  NH1 . ARG B 1 33  ? 10.00537  19.17559  75.61519  1.000 55.14940 ? 33  ARG B NH1 1 
ATOM   2461 N  NH2 . ARG B 1 33  ? 9.57101   20.74305  74.00363  1.000 55.70446 ? 33  ARG B NH2 1 
ATOM   2462 N  N   . VAL B 1 34  ? 10.36426  14.75777  77.84214  1.000 46.80642 ? 34  VAL B N   1 
ATOM   2463 C  CA  . VAL B 1 34  ? 9.50830   15.08302  78.96690  1.000 45.61076 ? 34  VAL B CA  1 
ATOM   2464 C  C   . VAL B 1 34  ? 9.35766   16.59507  79.03069  1.000 46.28922 ? 34  VAL B C   1 
ATOM   2465 O  O   . VAL B 1 34  ? 10.18911  17.35281  78.52087  1.000 53.40649 ? 34  VAL B O   1 
ATOM   2466 C  CB  . VAL B 1 34  ? 10.02721  14.50529  80.30429  1.000 43.55575 ? 34  VAL B CB  1 
ATOM   2467 C  CG1 . VAL B 1 34  ? 9.65656   13.03547  80.41371  1.000 46.74877 ? 34  VAL B CG1 1 
ATOM   2468 C  CG2 . VAL B 1 34  ? 11.50992  14.67389  80.41895  1.000 44.67351 ? 34  VAL B CG2 1 
ATOM   2469 N  N   . GLN B 1 35  ? 8.24901   17.04198  79.62468  1.000 42.39251 ? 35  GLN B N   1 
ATOM   2470 C  CA  . GLN B 1 35  ? 7.94133   18.46091  79.71353  1.000 42.42626 ? 35  GLN B CA  1 
ATOM   2471 C  C   . GLN B 1 35  ? 7.35395   18.79352  81.07759  1.000 45.92935 ? 35  GLN B C   1 
ATOM   2472 O  O   . GLN B 1 35  ? 6.85353   17.92858  81.80511  1.000 48.42989 ? 35  GLN B O   1 
ATOM   2473 C  CB  . GLN B 1 35  ? 6.95601   18.92515  78.62961  1.000 43.56638 ? 35  GLN B CB  1 
ATOM   2474 C  CG  . GLN B 1 35  ? 7.32464   18.55508  77.22017  1.000 39.99289 ? 35  GLN B CG  1 
ATOM   2475 C  CD  . GLN B 1 35  ? 6.34623   19.11877  76.21949  1.000 47.87930 ? 35  GLN B CD  1 
ATOM   2476 O  OE1 . GLN B 1 35  ? 6.08290   20.32425  76.19840  1.000 51.93334 ? 35  GLN B OE1 1 
ATOM   2477 N  NE2 . GLN B 1 35  ? 5.78366   18.24755  75.39060  1.000 44.14544 ? 35  GLN B NE2 1 
ATOM   2478 N  N   . GLU B 1 36  ? 7.36881   20.09036  81.36467  1.000 44.65013 ? 36  GLU B N   1 
ATOM   2479 C  CA  . GLU B 1 36  ? 7.07853   20.64709  82.67628  1.000 46.58624 ? 36  GLU B CA  1 
ATOM   2480 C  C   . GLU B 1 36  ? 5.58855   20.98735  82.77415  1.000 42.87650 ? 36  GLU B C   1 
ATOM   2481 O  O   . GLU B 1 36  ? 5.08201   21.81854  82.01617  1.000 45.08500 ? 36  GLU B O   1 
ATOM   2482 C  CB  . GLU B 1 36  ? 7.97334   21.87569  82.85708  1.000 54.49216 ? 36  GLU B CB  1 
ATOM   2483 C  CG  . GLU B 1 36  ? 7.45197   23.05401  83.65614  1.000 65.61090 ? 36  GLU B CG  1 
ATOM   2484 C  CD  . GLU B 1 36  ? 7.68243   22.88782  85.14238  1.000 71.75399 ? 36  GLU B CD  1 
ATOM   2485 O  OE1 . GLU B 1 36  ? 8.07695   21.77455  85.56580  1.000 69.46997 ? 36  GLU B OE1 1 
ATOM   2486 O  OE2 . GLU B 1 36  ? 7.52422   23.89223  85.87394  1.000 75.68036 ? 36  GLU B OE2 1 
ATOM   2487 N  N   . VAL B 1 37  ? 4.88836   20.33758  83.69785  1.000 46.97441 ? 37  VAL B N   1 
ATOM   2488 C  CA  . VAL B 1 37  ? 3.45831   20.53819  83.91634  1.000 46.32281 ? 37  VAL B CA  1 
ATOM   2489 C  C   . VAL B 1 37  ? 3.27826   20.87021  85.39190  1.000 48.57374 ? 37  VAL B C   1 
ATOM   2490 O  O   . VAL B 1 37  ? 3.52860   20.01675  86.24907  1.000 47.15202 ? 37  VAL B O   1 
ATOM   2491 C  CB  . VAL B 1 37  ? 2.64423   19.29368  83.54036  1.000 35.70316 ? 37  VAL B CB  1 
ATOM   2492 C  CG1 . VAL B 1 37  ? 1.14119   19.54237  83.66452  1.000 38.06423 ? 37  VAL B CG1 1 
ATOM   2493 C  CG2 . VAL B 1 37  ? 3.01747   18.79930  82.16038  1.000 41.56636 ? 37  VAL B CG2 1 
ATOM   2494 N  N   . GLU B 1 38  ? 2.84873   22.09760  85.69740  1.000 51.39604 ? 38  GLU B N   1 
ATOM   2495 C  CA  . GLU B 1 38  ? 2.62833   22.47123  87.08922  1.000 47.54114 ? 38  GLU B CA  1 
ATOM   2496 C  C   . GLU B 1 38  ? 1.29515   21.92570  87.56663  1.000 46.88016 ? 38  GLU B C   1 
ATOM   2497 O  O   . GLU B 1 38  ? 0.32514   21.87330  86.80736  1.000 44.41473 ? 38  GLU B O   1 
ATOM   2498 C  CB  . GLU B 1 38  ? 2.65083   23.98631  87.30090  1.000 52.10008 ? 38  GLU B CB  1 
ATOM   2499 C  CG  . GLU B 1 38  ? 3.79316   24.73720  86.64810  1.000 62.36409 ? 38  GLU B CG  1 
ATOM   2500 C  CD  . GLU B 1 38  ? 3.53753   25.05507  85.19411  1.000 65.99801 ? 38  GLU B CD  1 
ATOM   2501 O  OE1 . GLU B 1 38  ? 4.01397   24.29788  84.31940  1.000 64.46870 ? 38  GLU B OE1 1 
ATOM   2502 O  OE2 . GLU B 1 38  ? 2.89033   26.09622  84.93199  1.000 69.93475 ? 38  GLU B OE2 1 
ATOM   2503 N  N   . ILE B 1 39  ? 1.25012   21.51058  88.82787  1.000 50.91228 ? 39  ILE B N   1 
ATOM   2504 C  CA  . ILE B 1 39  ? 0.01999   21.03355  89.44453  1.000 56.31699 ? 39  ILE B CA  1 
ATOM   2505 C  C   . ILE B 1 39  ? -0.36109  22.03962  90.51904  1.000 59.37207 ? 39  ILE B C   1 
ATOM   2506 O  O   . ILE B 1 39  ? 0.17607   22.00473  91.63355  1.000 61.26481 ? 39  ILE B O   1 
ATOM   2507 C  CB  . ILE B 1 39  ? 0.15838   19.62389  90.02724  1.000 56.76038 ? 39  ILE B CB  1 
ATOM   2508 C  CG1 . ILE B 1 39  ? 1.21018   18.82433  89.26777  1.000 49.94981 ? 39  ILE B CG1 1 
ATOM   2509 C  CG2 . ILE B 1 39  ? -1.18179  18.88486  89.93667  1.000 45.68160 ? 39  ILE B CG2 1 
ATOM   2510 C  CD1 . ILE B 1 39  ? 1.14297   17.35456  89.56593  1.000 44.44411 ? 39  ILE B CD1 1 
ATOM   2511 N  N   . LYS B 1 40  ? -1.27320  22.95135  90.17610  1.000 58.98072 ? 40  LYS B N   1 
ATOM   2512 C  CA  . LYS B 1 40  ? -1.94631  23.76872  91.16896  1.000 50.53414 ? 40  LYS B CA  1 
ATOM   2513 C  C   . LYS B 1 40  ? -3.10103  22.98243  91.77225  1.000 53.34401 ? 40  LYS B C   1 
ATOM   2514 O  O   . LYS B 1 40  ? -3.35602  21.82502  91.42833  1.000 58.56790 ? 40  LYS B O   1 
ATOM   2515 C  CB  . LYS B 1 40  ? -2.47751  25.06126  90.55698  1.000 58.31779 ? 40  LYS B CB  1 
ATOM   2516 C  CG  . LYS B 1 40  ? -1.53275  25.80621  89.63830  1.000 61.89734 ? 40  LYS B CG  1 
ATOM   2517 C  CD  . LYS B 1 40  ? -2.24511  27.02741  89.06293  1.000 53.42831 ? 40  LYS B CD  1 
ATOM   2518 C  CE  . LYS B 1 40  ? -1.58376  28.31176  89.50770  1.000 53.84039 ? 40  LYS B CE  1 
ATOM   2519 N  NZ  . LYS B 1 40  ? -0.57419  28.76903  88.50928  1.000 58.75956 ? 40  LYS B NZ  1 
ATOM   2520 N  N   . ASP B 1 41  ? -3.83732  23.63588  92.66581  1.000 65.30333 ? 41  ASP B N   1 
ATOM   2521 C  CA  . ASP B 1 41  ? -5.02800  23.00334  93.21484  1.000 65.19435 ? 41  ASP B CA  1 
ATOM   2522 C  C   . ASP B 1 41  ? -6.16294  22.96740  92.19905  1.000 61.12029 ? 41  ASP B C   1 
ATOM   2523 O  O   . ASP B 1 41  ? -6.94657  22.01177  92.18134  1.000 59.23376 ? 41  ASP B O   1 
ATOM   2524 C  CB  . ASP B 1 41  ? -5.46290  23.72613  94.48162  1.000 65.53753 ? 41  ASP B CB  1 
ATOM   2525 C  CG  . ASP B 1 41  ? -5.92947  22.76992  95.54295  1.000 78.77689 ? 41  ASP B CG  1 
ATOM   2526 O  OD1 . ASP B 1 41  ? -5.17366  21.81415  95.83452  1.000 73.44210 ? 41  ASP B OD1 1 
ATOM   2527 O  OD2 . ASP B 1 41  ? -7.04447  22.96270  96.07531  1.000 85.10836 ? 41  ASP B OD2 1 
ATOM   2528 N  N   . GLU B 1 42  ? -6.25661  23.98732  91.34139  1.000 60.97907 ? 42  GLU B N   1 
ATOM   2529 C  CA  . GLU B 1 42  ? -7.27141  24.01085  90.29543  1.000 51.61695 ? 42  GLU B CA  1 
ATOM   2530 C  C   . GLU B 1 42  ? -7.11458  22.85523  89.31267  1.000 49.88457 ? 42  GLU B C   1 
ATOM   2531 O  O   . GLU B 1 42  ? -8.07644  22.49778  88.62063  1.000 43.55717 ? 42  GLU B O   1 
ATOM   2532 C  CB  . GLU B 1 42  ? -7.20782  25.35611  89.56450  1.000 49.64449 ? 42  GLU B CB  1 
ATOM   2533 C  CG  . GLU B 1 42  ? -8.46360  25.70606  88.78137  1.000 59.17858 ? 42  GLU B CG  1 
ATOM   2534 C  CD  . GLU B 1 42  ? -8.57176  27.19366  88.45698  1.000 57.53265 ? 42  GLU B CD  1 
ATOM   2535 O  OE1 . GLU B 1 42  ? -7.57669  27.77284  87.96686  1.000 61.16039 ? 42  GLU B OE1 1 
ATOM   2536 O  OE2 . GLU B 1 42  ? -9.65086  27.78455  88.68709  1.000 60.63733 ? 42  GLU B OE2 1 
ATOM   2537 N  N   . GLY B 1 43  ? -5.94150  22.25406  89.24786  1.000 51.01746 ? 43  GLY B N   1 
ATOM   2538 C  CA  . GLY B 1 43  ? -5.65354  21.24681  88.25796  1.000 39.95644 ? 43  GLY B CA  1 
ATOM   2539 C  C   . GLY B 1 43  ? -4.24032  21.41254  87.75003  1.000 43.71068 ? 43  GLY B C   1 
ATOM   2540 O  O   . GLY B 1 43  ? -3.37217  21.93628  88.44287  1.000 46.59103 ? 43  GLY B O   1 
ATOM   2541 N  N   . ALA B 1 44  ? -4.00936  20.96782  86.52024  1.000 36.19938 ? 44  ALA B N   1 
ATOM   2542 C  CA  . ALA B 1 44  ? -2.68099  20.96859  85.92681  1.000 35.95503 ? 44  ALA B CA  1 
ATOM   2543 C  C   . ALA B 1 44  ? -2.57624  22.05658  84.86110  1.000 43.83318 ? 44  ALA B C   1 
ATOM   2544 O  O   . ALA B 1 44  ? -3.46404  22.19100  84.01145  1.000 44.19922 ? 44  ALA B O   1 
ATOM   2545 C  CB  . ALA B 1 44  ? -2.36581  19.59592  85.33628  1.000 36.97344 ? 44  ALA B CB  1 
ATOM   2546 N  N   . VAL B 1 45  ? -1.49848  22.83755  84.92041  1.000 43.90257 ? 45  VAL B N   1 
ATOM   2547 C  CA  . VAL B 1 45  ? -1.19856  23.87731  83.94168  1.000 40.75718 ? 45  VAL B CA  1 
ATOM   2548 C  C   . VAL B 1 45  ? -0.15652  23.31715  82.98112  1.000 43.30149 ? 45  VAL B C   1 
ATOM   2549 O  O   . VAL B 1 45  ? 0.98648   23.05747  83.37118  1.000 42.96180 ? 45  VAL B O   1 
ATOM   2550 C  CB  . VAL B 1 45  ? -0.69542  25.16186  84.61560  1.000 47.78203 ? 45  VAL B CB  1 
ATOM   2551 C  CG1 . VAL B 1 45  ? -0.57612  26.28768  83.60214  1.000 39.45858 ? 45  VAL B CG1 1 
ATOM   2552 C  CG2 . VAL B 1 45  ? -1.61046  25.56213  85.77558  1.000 40.39070 ? 45  VAL B CG2 1 
ATOM   2553 N  N   . PHE B 1 46  ? -0.53330  23.15373  81.72392  1.000 42.79450 ? 46  PHE B N   1 
ATOM   2554 C  CA  . PHE B 1 46  ? 0.32938   22.54642  80.71799  1.000 43.02293 ? 46  PHE B CA  1 
ATOM   2555 C  C   . PHE B 1 46  ? 1.24481   23.59814  80.10390  1.000 46.87260 ? 46  PHE B C   1 
ATOM   2556 O  O   . PHE B 1 46  ? 1.11370   24.78808  80.40097  1.000 49.98848 ? 46  PHE B O   1 
ATOM   2557 C  CB  . PHE B 1 46  ? -0.53871  21.84834  79.67642  1.000 39.56830 ? 46  PHE B CB  1 
ATOM   2558 C  CG  . PHE B 1 46  ? -0.96210  20.47600  80.09689  1.000 33.42070 ? 46  PHE B CG  1 
ATOM   2559 C  CD1 . PHE B 1 46  ? -1.97427  20.30919  81.03350  1.000 36.02496 ? 46  PHE B CD1 1 
ATOM   2560 C  CD2 . PHE B 1 46  ? -0.31562  19.35580  79.59685  1.000 38.09276 ? 46  PHE B CD2 1 
ATOM   2561 C  CE1 . PHE B 1 46  ? -2.35534  19.04814  81.44187  1.000 33.85274 ? 46  PHE B CE1 1 
ATOM   2562 C  CE2 . PHE B 1 46  ? -0.66992  18.07991  80.00264  1.000 32.33796 ? 46  PHE B CE2 1 
ATOM   2563 C  CZ  . PHE B 1 46  ? -1.70066  17.91820  80.92228  1.000 41.62529 ? 46  PHE B CZ  1 
ATOM   2564 N  N   . PRO B 1 47  ? 2.23453   23.19794  79.28403  1.000 42.53074 ? 47  PRO B N   1 
ATOM   2565 C  CA  . PRO B 1 47  ? 3.08374   24.21231  78.63253  1.000 48.49993 ? 47  PRO B CA  1 
ATOM   2566 C  C   . PRO B 1 47  ? 2.29373   25.12824  77.74367  1.000 54.73323 ? 47  PRO B C   1 
ATOM   2567 O  O   . PRO B 1 47  ? 2.74427   26.24215  77.45032  1.000 54.94477 ? 47  PRO B O   1 
ATOM   2568 C  CB  . PRO B 1 47  ? 4.09157   23.37712  77.82738  1.000 39.27734 ? 47  PRO B CB  1 
ATOM   2569 C  CG  . PRO B 1 47  ? 4.15563   22.09492  78.55945  1.000 36.31416 ? 47  PRO B CG  1 
ATOM   2570 C  CD  . PRO B 1 47  ? 2.72616   21.84313  78.97989  1.000 47.38218 ? 47  PRO B CD  1 
ATOM   2571 N  N   . ASP B 1 48  ? 1.12694   24.67440  77.29056  1.000 52.75030 ? 48  ASP B N   1 
ATOM   2572 C  CA  . ASP B 1 48  ? 0.13153   25.56922  76.72697  1.000 55.90732 ? 48  ASP B CA  1 
ATOM   2573 C  C   . ASP B 1 48  ? -0.19540  26.71648  77.65865  1.000 58.59878 ? 48  ASP B C   1 
ATOM   2574 O  O   . ASP B 1 48  ? -0.64056  27.76984  77.19015  1.000 65.19320 ? 48  ASP B O   1 
ATOM   2575 C  CB  . ASP B 1 48  ? -1.15775  24.80468  76.44161  1.000 41.84328 ? 48  ASP B CB  1 
ATOM   2576 C  CG  . ASP B 1 48  ? -1.81875  25.25152  75.16839  1.000 51.32813 ? 48  ASP B CG  1 
ATOM   2577 O  OD1 . ASP B 1 48  ? -1.33512  26.25021  74.59370  1.000 52.13714 ? 48  ASP B OD1 1 
ATOM   2578 O  OD2 . ASP B 1 48  ? -2.80375  24.60053  74.73816  1.000 53.32828 ? 48  ASP B OD2 1 
ATOM   2579 N  N   . GLY B 1 49  ? 0.04685   26.56330  78.96305  1.000 55.66985 ? 49  GLY B N   1 
ATOM   2580 C  CA  . GLY B 1 49  ? -0.60168  27.39744  79.95630  1.000 44.81519 ? 49  GLY B CA  1 
ATOM   2581 C  C   . GLY B 1 49  ? -2.07089  27.10795  80.08405  1.000 46.55060 ? 49  GLY B C   1 
ATOM   2582 O  O   . GLY B 1 49  ? -2.78531  27.84676  80.76525  1.000 50.85583 ? 49  GLY B O   1 
ATOM   2583 N  N   . THR B 1 50  ? -2.54230  26.05611  79.42229  1.000 51.38853 ? 50  THR B N   1 
ATOM   2584 C  CA  . THR B 1 50  ? -3.90069  25.58493  79.59357  1.000 48.00977 ? 50  THR B CA  1 
ATOM   2585 C  C   . THR B 1 50  ? -4.02884  24.86993  80.92814  1.000 39.09741 ? 50  THR B C   1 
ATOM   2586 O  O   . THR B 1 50  ? -3.24227  23.97391  81.24270  1.000 35.77373 ? 50  THR B O   1 
ATOM   2587 C  CB  . THR B 1 50  ? -4.27662  24.64522  78.45403  1.000 46.04614 ? 50  THR B CB  1 
ATOM   2588 O  OG1 . THR B 1 50  ? -4.19111  25.35785  77.21384  1.000 50.15503 ? 50  THR B OG1 1 
ATOM   2589 C  CG2 . THR B 1 50  ? -5.69558  24.11716  78.64479  1.000 43.36899 ? 50  THR B CG2 1 
ATOM   2590 N  N   . LEU B 1 51  ? -5.00373  25.27502  81.72550  1.000 41.16200 ? 51  LEU B N   1 
ATOM   2591 C  CA  . LEU B 1 51  ? -5.28771  24.55783  82.95028  1.000 39.75788 ? 51  LEU B CA  1 
ATOM   2592 C  C   . LEU B 1 51  ? -6.25351  23.42883  82.63683  1.000 36.86972 ? 51  LEU B C   1 
ATOM   2593 O  O   . LEU B 1 51  ? -7.30951  23.65405  82.04359  1.000 44.33853 ? 51  LEU B O   1 
ATOM   2594 C  CB  . LEU B 1 51  ? -5.86344  25.49071  84.00861  1.000 40.12574 ? 51  LEU B CB  1 
ATOM   2595 C  CG  . LEU B 1 51  ? -5.58717  24.94285  85.41292  1.000 44.14671 ? 51  LEU B CG  1 
ATOM   2596 C  CD1 . LEU B 1 51  ? -5.24957  26.08284  86.36635  1.000 47.18618 ? 51  LEU B CD1 1 
ATOM   2597 C  CD2 . LEU B 1 51  ? -6.77459  24.15445  85.90784  1.000 49.54216 ? 51  LEU B CD2 1 
ATOM   2598 N  N   . VAL B 1 52  ? -5.87776  22.21728  83.00150  1.000 38.29282 ? 52  VAL B N   1 
ATOM   2599 C  CA  . VAL B 1 52  ? -6.76854  21.06956  82.92252  1.000 37.76967 ? 52  VAL B CA  1 
ATOM   2600 C  C   . VAL B 1 52  ? -7.28965  20.82325  84.32721  1.000 41.13660 ? 52  VAL B C   1 
ATOM   2601 O  O   . VAL B 1 52  ? -6.54253  20.39083  85.21020  1.000 35.69674 ? 52  VAL B O   1 
ATOM   2602 C  CB  . VAL B 1 52  ? -6.06383  19.83544  82.35767  1.000 39.66408 ? 52  VAL B CB  1 
ATOM   2603 C  CG1 . VAL B 1 52  ? -7.02063  18.65549  82.35854  1.000 32.61730 ? 52  VAL B CG1 1 
ATOM   2604 C  CG2 . VAL B 1 52  ? -5.55045  20.13162  80.95061  1.000 32.90467 ? 52  VAL B CG2 1 
ATOM   2605 N  N   . GLU B 1 53  ? -8.56672  21.12950  84.53433  1.000 44.40253 ? 53  GLU B N   1 
ATOM   2606 C  CA  . GLU B 1 53  ? -9.16074  21.09641  85.85835  1.000 44.83242 ? 53  GLU B CA  1 
ATOM   2607 C  C   . GLU B 1 53  ? -9.03954  19.69796  86.47320  1.000 43.24358 ? 53  GLU B C   1 
ATOM   2608 O  O   . GLU B 1 53  ? -8.88719  18.68562  85.77590  1.000 31.63099 ? 53  GLU B O   1 
ATOM   2609 C  CB  . GLU B 1 53  ? -10.62366 21.53669  85.77826  1.000 41.73634 ? 53  GLU B CB  1 
ATOM   2610 C  CG  . GLU B 1 53  ? -10.84707 23.06546  85.69149  1.000 49.53538 ? 53  GLU B CG  1 
ATOM   2611 C  CD  . GLU B 1 53  ? -11.12227 23.55982  84.26004  1.000 60.40239 ? 53  GLU B CD  1 
ATOM   2612 O  OE1 . GLU B 1 53  ? -10.81716 22.81585  83.29679  1.000 56.88267 ? 53  GLU B OE1 1 
ATOM   2613 O  OE2 . GLU B 1 53  ? -11.65301 24.68632  84.09805  1.000 56.69178 ? 53  GLU B OE2 1 
ATOM   2614 N  N   . ARG B 1 54  ? -9.09302  19.65827  87.80916  1.000 38.44140 ? 54  ARG B N   1 
ATOM   2615 C  CA  . ARG B 1 54  ? -8.91683  18.40361  88.53404  1.000 36.55544 ? 54  ARG B CA  1 
ATOM   2616 C  C   . ARG B 1 54  ? -9.91950  17.34415  88.08670  1.000 35.87426 ? 54  ARG B C   1 
ATOM   2617 O  O   . ARG B 1 54  ? -9.56102  16.18074  87.86305  1.000 33.46509 ? 54  ARG B O   1 
ATOM   2618 C  CB  . ARG B 1 54  ? -9.05834  18.66331  90.03709  1.000 39.56759 ? 54  ARG B CB  1 
ATOM   2619 C  CG  . ARG B 1 54  ? -8.41297  17.59760  90.88928  1.000 43.61737 ? 54  ARG B CG  1 
ATOM   2620 C  CD  . ARG B 1 54  ? -7.55133  18.22825  91.95491  1.000 47.66127 ? 54  ARG B CD  1 
ATOM   2621 N  NE  . ARG B 1 54  ? -6.41279  17.36845  92.25797  1.000 56.61475 ? 54  ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 1 54  ? -5.14578  17.75276  92.14888  1.000 62.48315 ? 54  ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 1 54  ? -4.82371  18.98763  91.78233  1.000 56.48560 ? 54  ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 1 54  ? -4.17710  16.87346  92.39491  1.000 58.23544 ? 54  ARG B NH2 1 
ATOM   2625 N  N   . GLU B 1 55  ? -11.18380 17.72693  87.95795  1.000 37.63385 ? 55  GLU B N   1 
ATOM   2626 C  CA  . GLU B 1 55  ? -12.23269 16.75551  87.68102  1.000 40.95787 ? 55  GLU B CA  1 
ATOM   2627 C  C   . GLU B 1 55  ? -11.99937 16.05721  86.34957  1.000 37.78978 ? 55  GLU B C   1 
ATOM   2628 O  O   . GLU B 1 55  ? -12.22013 14.84652  86.23364  1.000 30.93476 ? 55  GLU B O   1 
ATOM   2629 C  CB  . GLU B 1 55  ? -13.59804 17.43722  87.71539  1.000 36.69881 ? 55  GLU B CB  1 
ATOM   2630 C  CG  . GLU B 1 55  ? -13.72917 18.56776  88.75521  1.000 60.18504 ? 55  GLU B CG  1 
ATOM   2631 C  CD  . GLU B 1 55  ? -12.93558 19.83685  88.40444  1.000 61.16843 ? 55  GLU B CD  1 
ATOM   2632 O  OE1 . GLU B 1 55  ? -12.27233 20.40865  89.30333  1.000 54.87964 ? 55  GLU B OE1 1 
ATOM   2633 O  OE2 . GLU B 1 55  ? -12.99636 20.25931  87.22694  1.000 66.16506 ? 55  GLU B OE2 1 
ATOM   2634 N  N   . VAL B 1 56  ? -11.51183 16.79845  85.34709  1.000 33.81292 ? 56  VAL B N   1 
ATOM   2635 C  CA  . VAL B 1 56  ? -11.14395 16.20222  84.05959  1.000 37.21921 ? 56  VAL B CA  1 
ATOM   2636 C  C   . VAL B 1 56  ? -9.98267  15.22034  84.22788  1.000 33.50294 ? 56  VAL B C   1 
ATOM   2637 O  O   . VAL B 1 56  ? -9.98538  14.11765  83.66291  1.000 33.66347 ? 56  VAL B O   1 
ATOM   2638 C  CB  . VAL B 1 56  ? -10.80719 17.31030  83.04204  1.000 34.44951 ? 56  VAL B CB  1 
ATOM   2639 C  CG1 . VAL B 1 56  ? -10.49221 16.71432  81.68136  1.000 29.89637 ? 56  VAL B CG1 1 
ATOM   2640 C  CG2 . VAL B 1 56  ? -11.95530 18.26265  82.93406  1.000 39.07324 ? 56  VAL B CG2 1 
ATOM   2641 N  N   . LEU B 1 57  ? -8.96718  15.60708  85.00340  1.000 32.17888 ? 57  LEU B N   1 
ATOM   2642 C  CA  . LEU B 1 57  ? -7.85039  14.70018  85.26585  1.000 32.80923 ? 57  LEU B CA  1 
ATOM   2643 C  C   . LEU B 1 57  ? -8.32446  13.40065  85.90621  1.000 29.88197 ? 57  LEU B C   1 
ATOM   2644 O  O   . LEU B 1 57  ? -7.82989  12.31540  85.58098  1.000 30.88597 ? 57  LEU B O   1 
ATOM   2645 C  CB  . LEU B 1 57  ? -6.82001  15.38551  86.16998  1.000 30.38496 ? 57  LEU B CB  1 
ATOM   2646 C  CG  . LEU B 1 57  ? -5.93272  16.49548  85.60723  1.000 33.45923 ? 57  LEU B CG  1 
ATOM   2647 C  CD1 . LEU B 1 57  ? -4.86292  16.91385  86.62265  1.000 28.33596 ? 57  LEU B CD1 1 
ATOM   2648 C  CD2 . LEU B 1 57  ? -5.29182  16.03949  84.29030  1.000 31.02359 ? 57  LEU B CD2 1 
ATOM   2649 N  N   . GLU B 1 58  ? -9.26718  13.48902  86.83490  1.000 31.07556 ? 58  GLU B N   1 
ATOM   2650 C  CA  . GLU B 1 58  ? -9.76003  12.28361  87.47925  1.000 32.63410 ? 58  GLU B CA  1 
ATOM   2651 C  C   . GLU B 1 58  ? -10.55229 11.43893  86.49563  1.000 30.70225 ? 58  GLU B C   1 
ATOM   2652 O  O   . GLU B 1 58  ? -10.49993 10.20511  86.54503  1.000 27.25601 ? 58  GLU B O   1 
ATOM   2653 C  CB  . GLU B 1 58  ? -10.61258 12.65272  88.70106  1.000 34.83691 ? 58  GLU B CB  1 
ATOM   2654 C  CG  . GLU B 1 58  ? -9.86694  13.50290  89.73727  1.000 34.08433 ? 58  GLU B CG  1 
ATOM   2655 C  CD  . GLU B 1 58  ? -10.75535 13.96281  90.86227  1.000 34.97177 ? 58  GLU B CD  1 
ATOM   2656 O  OE1 . GLU B 1 58  ? -11.97683 14.11756  90.64086  1.000 36.98849 ? 58  GLU B OE1 1 
ATOM   2657 O  OE2 . GLU B 1 58  ? -10.23315 14.17218  91.97572  1.000 43.21941 ? 58  GLU B OE2 1 
ATOM   2658 N  N   . LYS B 1 59  ? -11.29965 12.08698  85.60162  1.000 31.85147 ? 59  LYS B N   1 
ATOM   2659 C  CA  . LYS B 1 59  ? -12.03600 11.35147  84.57665  1.000 35.83725 ? 59  LYS B CA  1 
ATOM   2660 C  C   . LYS B 1 59  ? -11.08755 10.54739  83.69222  1.000 32.24857 ? 59  LYS B C   1 
ATOM   2661 O  O   . LYS B 1 59  ? -11.33228 9.37178   83.40163  1.000 30.61769 ? 59  LYS B O   1 
ATOM   2662 C  CB  . LYS B 1 59  ? -12.87647 12.32081  83.74141  1.000 37.65246 ? 59  LYS B CB  1 
ATOM   2663 C  CG  . LYS B 1 59  ? -13.80326 11.63332  82.74588  1.000 44.44578 ? 59  LYS B CG  1 
ATOM   2664 C  CD  . LYS B 1 59  ? -13.54522 12.10013  81.29128  1.000 40.91063 ? 59  LYS B CD  1 
ATOM   2665 C  CE  . LYS B 1 59  ? -14.05069 13.51422  81.08886  1.000 43.03593 ? 59  LYS B CE  1 
ATOM   2666 N  NZ  . LYS B 1 59  ? -14.00429 14.00846  79.68338  1.000 54.58591 ? 59  LYS B NZ  1 
ATOM   2667 N  N   . ILE B 1 60  ? -9.99641  11.16493  83.25156  1.000 31.97985 ? 60  ILE B N   1 
ATOM   2668 C  CA  . ILE B 1 60  ? -9.02619  10.44200  82.43181  1.000 32.78060 ? 60  ILE B CA  1 
ATOM   2669 C  C   . ILE B 1 60  ? -8.36830  9.32767   83.24062  1.000 30.13680 ? 60  ILE B C   1 
ATOM   2670 O  O   . ILE B 1 60  ? -8.32540  8.16951   82.80993  1.000 30.75165 ? 60  ILE B O   1 
ATOM   2671 C  CB  . ILE B 1 60  ? -7.99144  11.41754  81.85259  1.000 30.31884 ? 60  ILE B CB  1 
ATOM   2672 C  CG1 . ILE B 1 60  ? -8.67844  12.35810  80.86868  1.000 29.50944 ? 60  ILE B CG1 1 
ATOM   2673 C  CG2 . ILE B 1 60  ? -6.86038  10.65386  81.17738  1.000 32.73109 ? 60  ILE B CG2 1 
ATOM   2674 C  CD1 . ILE B 1 60  ? -8.03432  13.72647  80.77634  1.000 32.52316 ? 60  ILE B CD1 1 
ATOM   2675 N  N   . ALA B 1 61  ? -7.87277  9.65365   84.44152  1.000 27.54764 ? 61  ALA B N   1 
ATOM   2676 C  CA  . ALA B 1 61  ? -7.27456  8.63545   85.30915  1.000 25.15776 ? 61  ALA B CA  1 
ATOM   2677 C  C   . ALA B 1 61  ? -8.19154  7.44570   85.51221  1.000 30.77334 ? 61  ALA B C   1 
ATOM   2678 O  O   . ALA B 1 61  ? -7.71823  6.33383   85.78062  1.000 32.45353 ? 61  ALA B O   1 
ATOM   2679 C  CB  . ALA B 1 61  ? -6.92951  9.22810   86.67972  1.000 27.02239 ? 61  ALA B CB  1 
ATOM   2680 N  N   . ARG B 1 62  ? -9.50552  7.67230   85.44018  1.000 40.74956 ? 62  ARG B N   1 
ATOM   2681 C  CA  . ARG B 1 62  ? -10.50584 6.62048   85.57639  1.000 43.27113 ? 62  ARG B CA  1 
ATOM   2682 C  C   . ARG B 1 62  ? -10.56900 5.71565   84.35727  1.000 42.40283 ? 62  ARG B C   1 
ATOM   2683 O  O   . ARG B 1 62  ? -11.10733 4.60996   84.45233  1.000 46.68514 ? 62  ARG B O   1 
ATOM   2684 C  CB  . ARG B 1 62  ? -11.89066 7.24196   85.77003  1.000 44.39820 ? 62  ARG B CB  1 
ATOM   2685 C  CG  . ARG B 1 62  ? -12.43795 7.15510   87.12664  1.000 47.79964 ? 62  ARG B CG  1 
ATOM   2686 C  CD  . ARG B 1 62  ? -13.92212 7.45506   87.16253  1.000 49.69974 ? 62  ARG B CD  1 
ATOM   2687 N  NE  . ARG B 1 62  ? -14.37775 8.64381   86.44554  1.000 47.80407 ? 62  ARG B NE  1 
ATOM   2688 C  CZ  . ARG B 1 62  ? -14.41305 9.87617   86.94316  1.000 47.63062 ? 62  ARG B CZ  1 
ATOM   2689 N  NH1 . ARG B 1 62  ? -13.83222 10.18007  88.08546  1.000 48.51303 ? 62  ARG B NH1 1 
ATOM   2690 N  NH2 . ARG B 1 62  ? -15.03799 10.83512  86.26656  1.000 46.89615 ? 62  ARG B NH2 1 
ATOM   2691 N  N   . ASP B 1 63  ? -10.04198 6.16364   83.22404  1.000 39.35273 ? 63  ASP B N   1 
ATOM   2692 C  CA  . ASP B 1 63  ? -10.34234 5.60384   81.91520  1.000 41.28517 ? 63  ASP B CA  1 
ATOM   2693 C  C   . ASP B 1 63  ? -9.03239  5.12869   81.31066  1.000 38.69133 ? 63  ASP B C   1 
ATOM   2694 O  O   . ASP B 1 63  ? -8.38515  5.88589   80.58701  1.000 41.72534 ? 63  ASP B O   1 
ATOM   2695 C  CB  . ASP B 1 63  ? -11.02976 6.69042   81.04492  1.000 47.92262 ? 63  ASP B CB  1 
ATOM   2696 C  CG  . ASP B 1 63  ? -11.38073 6.21478   79.63376  1.000 49.59306 ? 63  ASP B CG  1 
ATOM   2697 O  OD1 . ASP B 1 63  ? -11.34930 4.99092   79.36301  1.000 50.33533 ? 63  ASP B OD1 1 
ATOM   2698 O  OD2 . ASP B 1 63  ? -11.71297 7.08910   78.79573  1.000 44.12647 ? 63  ASP B OD2 1 
ATOM   2699 N  N   . ASP B 1 64  ? -8.65194  3.87277   81.57873  1.000 39.03087 ? 64  ASP B N   1 
ATOM   2700 C  CA  . ASP B 1 64  ? -7.39677  3.36588   81.03571  1.000 38.39640 ? 64  ASP B CA  1 
ATOM   2701 C  C   . ASP B 1 64  ? -7.53052  2.84062   79.60899  1.000 45.54458 ? 64  ASP B C   1 
ATOM   2702 O  O   . ASP B 1 64  ? -6.64695  2.10901   79.13980  1.000 38.72720 ? 64  ASP B O   1 
ATOM   2703 C  CB  . ASP B 1 64  ? -6.78544  2.30561   81.96427  1.000 41.56032 ? 64  ASP B CB  1 
ATOM   2704 C  CG  . ASP B 1 64  ? -7.38360  0.91894   81.79612  1.000 47.52236 ? 64  ASP B CG  1 
ATOM   2705 O  OD1 . ASP B 1 64  ? -8.36516  0.73622   81.03550  1.000 47.22653 ? 64  ASP B OD1 1 
ATOM   2706 O  OD2 . ASP B 1 64  ? -6.85902  -0.01129  82.46416  1.000 48.21466 ? 64  ASP B OD2 1 
ATOM   2707 N  N   . GLY B 1 65  ? -8.59866  3.20125   78.90374  1.000 41.42657 ? 65  GLY B N   1 
ATOM   2708 C  CA  . GLY B 1 65  ? -8.79632  2.66499   77.57230  1.000 36.06726 ? 65  GLY B CA  1 
ATOM   2709 C  C   . GLY B 1 65  ? -8.94291  3.71630   76.49740  1.000 39.61926 ? 65  GLY B C   1 
ATOM   2710 O  O   . GLY B 1 65  ? -9.27583  3.38284   75.35548  1.000 46.46046 ? 65  GLY B O   1 
ATOM   2711 N  N   . THR B 1 66  ? -8.68095  4.98167   76.82847  1.000 34.31430 ? 66  THR B N   1 
ATOM   2712 C  CA  . THR B 1 66  ? -8.91020  6.06660   75.88919  1.000 33.37552 ? 66  THR B CA  1 
ATOM   2713 C  C   . THR B 1 66  ? -7.74731  7.04847   75.91392  1.000 41.94523 ? 66  THR B C   1 
ATOM   2714 O  O   . THR B 1 66  ? -7.15501  7.30678   76.96633  1.000 36.00361 ? 66  THR B O   1 
ATOM   2715 C  CB  . THR B 1 66  ? -10.20940 6.79799   76.21223  1.000 39.87565 ? 66  THR B CB  1 
ATOM   2716 O  OG1 . THR B 1 66  ? -11.21050 5.84584   76.59609  1.000 47.87007 ? 66  THR B OG1 1 
ATOM   2717 C  CG2 . THR B 1 66  ? -10.69572 7.55220   75.00436  1.000 51.48208 ? 66  THR B CG2 1 
ATOM   2718 N  N   . VAL B 1 67  ? -7.42084  7.57909   74.74638  1.000 35.74902 ? 67  VAL B N   1 
ATOM   2719 C  CA  . VAL B 1 67  ? -6.43869  8.64353   74.60982  1.000 31.58836 ? 67  VAL B CA  1 
ATOM   2720 C  C   . VAL B 1 67  ? -7.16942  9.97628   74.60738  1.000 33.53610 ? 67  VAL B C   1 
ATOM   2721 O  O   . VAL B 1 67  ? -8.24288  10.11876  74.01064  1.000 33.19675 ? 67  VAL B O   1 
ATOM   2722 C  CB  . VAL B 1 67  ? -5.60827  8.46624   73.32577  1.000 38.21106 ? 67  VAL B CB  1 
ATOM   2723 C  CG1 . VAL B 1 67  ? -4.78047  9.72579   73.04544  1.000 32.01453 ? 67  VAL B CG1 1 
ATOM   2724 C  CG2 . VAL B 1 67  ? -4.70864  7.24585   73.43708  1.000 35.95446 ? 67  VAL B CG2 1 
ATOM   2725 N  N   . TYR B 1 68  ? -6.60432  10.94995  75.30393  1.000 33.74056 ? 68  TYR B N   1 
ATOM   2726 C  CA  . TYR B 1 68  ? -7.12043  12.30393  75.31471  1.000 33.40799 ? 68  TYR B CA  1 
ATOM   2727 C  C   . TYR B 1 68  ? -6.02373  13.24066  74.83218  1.000 29.19688 ? 68  TYR B C   1 
ATOM   2728 O  O   . TYR B 1 68  ? -4.84078  12.89469  74.83297  1.000 25.37783 ? 68  TYR B O   1 
ATOM   2729 C  CB  . TYR B 1 68  ? -7.59488  12.70838  76.72167  1.000 39.00644 ? 68  TYR B CB  1 
ATOM   2730 C  CG  . TYR B 1 68  ? -8.77160  11.91088  77.24880  1.000 35.27685 ? 68  TYR B CG  1 
ATOM   2731 C  CD1 . TYR B 1 68  ? -8.59059  10.63411  77.77100  1.000 46.05650 ? 68  TYR B CD1 1 
ATOM   2732 C  CD2 . TYR B 1 68  ? -10.05606 12.44790  77.26454  1.000 38.76590 ? 68  TYR B CD2 1 
ATOM   2733 C  CE1 . TYR B 1 68  ? -9.65820  9.90364   78.28281  1.000 39.38453 ? 68  TYR B CE1 1 
ATOM   2734 C  CE2 . TYR B 1 68  ? -11.13006 11.72404  77.77161  1.000 42.64711 ? 68  TYR B CE2 1 
ATOM   2735 C  CZ  . TYR B 1 68  ? -10.92176 10.44915  78.27169  1.000 43.96667 ? 68  TYR B CZ  1 
ATOM   2736 O  OH  . TYR B 1 68  ? -11.97841 9.71387   78.76145  1.000 48.60520 ? 68  TYR B OH  1 
ATOM   2737 N  N   . PHE B 1 69  ? -6.42315  14.42547  74.38451  1.000 29.36316 ? 69  PHE B N   1 
ATOM   2738 C  CA  . PHE B 1 69  ? -5.43523  15.44438  74.08287  1.000 33.02091 ? 69  PHE B CA  1 
ATOM   2739 C  C   . PHE B 1 69  ? -6.01434  16.81058  74.39215  1.000 38.05477 ? 69  PHE B C   1 
ATOM   2740 O  O   . PHE B 1 69  ? -7.23319  17.01491  74.41354  1.000 36.83212 ? 69  PHE B O   1 
ATOM   2741 C  CB  . PHE B 1 69  ? -4.94193  15.38686  72.62649  1.000 30.78382 ? 69  PHE B CB  1 
ATOM   2742 C  CG  . PHE B 1 69  ? -6.03024  15.50243  71.59114  1.000 36.84081 ? 69  PHE B CG  1 
ATOM   2743 C  CD1 . PHE B 1 69  ? -6.68204  14.37389  71.11674  1.000 32.04049 ? 69  PHE B CD1 1 
ATOM   2744 C  CD2 . PHE B 1 69  ? -6.36742  16.73227  71.06036  1.000 32.91175 ? 69  PHE B CD2 1 
ATOM   2745 C  CE1 . PHE B 1 69  ? -7.66531  14.47836  70.15662  1.000 38.73646 ? 69  PHE B CE1 1 
ATOM   2746 C  CE2 . PHE B 1 69  ? -7.35350  16.84130  70.10558  1.000 34.52196 ? 69  PHE B CE2 1 
ATOM   2747 C  CZ  . PHE B 1 69  ? -8.00486  15.71443  69.64623  1.000 34.03047 ? 69  PHE B CZ  1 
ATOM   2748 N  N   . VAL B 1 70  ? -5.11344  17.74626  74.64929  1.000 36.08909 ? 70  VAL B N   1 
ATOM   2749 C  CA  . VAL B 1 70  ? -5.47744  19.13076  74.87360  1.000 37.62084 ? 70  VAL B CA  1 
ATOM   2750 C  C   . VAL B 1 70  ? -4.84071  19.94972  73.76462  1.000 39.03024 ? 70  VAL B C   1 
ATOM   2751 O  O   . VAL B 1 70  ? -3.62214  19.88920  73.56119  1.000 42.26981 ? 70  VAL B O   1 
ATOM   2752 C  CB  . VAL B 1 70  ? -5.05369  19.61172  76.27057  1.000 33.58055 ? 70  VAL B CB  1 
ATOM   2753 C  CG1 . VAL B 1 70  ? -3.83272  18.86074  76.73815  1.000 35.20040 ? 70  VAL B CG1 1 
ATOM   2754 C  CG2 . VAL B 1 70  ? -4.81018  21.11464  76.27053  1.000 43.93065 ? 70  VAL B CG2 1 
ATOM   2755 N  N   . SER B 1 71  ? -5.67214  20.66760  73.01481  1.000 35.34813 ? 71  SER B N   1 
ATOM   2756 C  CA  . SER B 1 71  ? -5.21406  21.62291  72.01623  1.000 46.63833 ? 71  SER B CA  1 
ATOM   2757 C  C   . SER B 1 71  ? -6.19366  22.78191  72.00367  1.000 49.33080 ? 71  SER B C   1 
ATOM   2758 O  O   . SER B 1 71  ? -7.38474  22.60261  72.28342  1.000 47.48611 ? 71  SER B O   1 
ATOM   2759 C  CB  . SER B 1 71  ? -5.12178  21.02153  70.60543  1.000 49.86490 ? 71  SER B CB  1 
ATOM   2760 O  OG  . SER B 1 71  ? -6.30163  21.29681  69.85559  1.000 43.85461 ? 71  SER B OG  1 
ATOM   2761 N  N   . ASN B 1 72  ? -5.68411  23.97124  71.67073  1.000 51.31880 ? 72  ASN B N   1 
ATOM   2762 C  CA  . ASN B 1 72  ? -6.48129  25.19729  71.71074  1.000 45.23211 ? 72  ASN B CA  1 
ATOM   2763 C  C   . ASN B 1 72  ? -7.18178  25.32490  73.05602  1.000 40.22902 ? 72  ASN B C   1 
ATOM   2764 O  O   . ASN B 1 72  ? -8.30967  25.81427  73.15400  1.000 48.55263 ? 72  ASN B O   1 
ATOM   2765 C  CB  . ASN B 1 72  ? -7.48987  25.25283  70.56272  1.000 48.12853 ? 72  ASN B CB  1 
ATOM   2766 C  CG  . ASN B 1 72  ? -6.86718  24.90139  69.22754  1.000 62.14023 ? 72  ASN B CG  1 
ATOM   2767 O  OD1 . ASN B 1 72  ? -7.14686  23.84127  68.66357  1.000 62.36871 ? 72  ASN B OD1 1 
ATOM   2768 N  ND2 . ASN B 1 72  ? -6.01810  25.79244  68.70924  1.000 64.73135 ? 72  ASN B ND2 1 
ATOM   2769 N  N   . GLY B 1 73  ? -6.49759  24.87022  74.10575  1.000 42.51357 ? 73  GLY B N   1 
ATOM   2770 C  CA  . GLY B 1 73  ? -7.00749  24.96125  75.45397  1.000 46.34138 ? 73  GLY B CA  1 
ATOM   2771 C  C   . GLY B 1 73  ? -8.14724  24.02632  75.79012  1.000 39.40516 ? 73  GLY B C   1 
ATOM   2772 O  O   . GLY B 1 73  ? -8.68458  24.11015  76.89963  1.000 38.23954 ? 73  GLY B O   1 
ATOM   2773 N  N   . GLY B 1 74  ? -8.54052  23.13954  74.88675  1.000 34.81495 ? 74  GLY B N   1 
ATOM   2774 C  CA  . GLY B 1 74  ? -9.66721  22.24636  75.11256  1.000 40.12730 ? 74  GLY B CA  1 
ATOM   2775 C  C   . GLY B 1 74  ? -9.19183  20.80745  75.19209  1.000 40.96827 ? 74  GLY B C   1 
ATOM   2776 O  O   . GLY B 1 74  ? -8.33498  20.38933  74.41456  1.000 47.36265 ? 74  GLY B O   1 
ATOM   2777 N  N   . VAL B 1 75  ? -9.74724  20.06548  76.12683  1.000 35.25160 ? 75  VAL B N   1 
ATOM   2778 C  CA  . VAL B 1 75  ? -9.43579  18.65163  76.28010  1.000 42.19452 ? 75  VAL B CA  1 
ATOM   2779 C  C   . VAL B 1 75  ? -10.41213 17.85384  75.43495  1.000 41.24895 ? 75  VAL B C   1 
ATOM   2780 O  O   . VAL B 1 75  ? -11.61468 18.13036  75.44199  1.000 42.96328 ? 75  VAL B O   1 
ATOM   2781 C  CB  . VAL B 1 75  ? -9.50535  18.23577  77.75790  1.000 45.41104 ? 75  VAL B CB  1 
ATOM   2782 C  CG1 . VAL B 1 75  ? -9.08177  16.78003  77.89831  1.000 49.39389 ? 75  VAL B CG1 1 
ATOM   2783 C  CG2 . VAL B 1 75  ? -8.63030  19.14767  78.59877  1.000 36.85878 ? 75  VAL B CG2 1 
ATOM   2784 N  N   . TYR B 1 76  ? -9.89729  16.87394  74.68829  1.000 38.80399 ? 76  TYR B N   1 
ATOM   2785 C  CA  . TYR B 1 76  ? -10.69581 16.14298  73.71448  1.000 38.51426 ? 76  TYR B CA  1 
ATOM   2786 C  C   . TYR B 1 76  ? -10.35714 14.66437  73.77861  1.000 34.78042 ? 76  TYR B C   1 
ATOM   2787 O  O   . TYR B 1 76  ? -9.25065  14.28153  74.15605  1.000 36.49823 ? 76  TYR B O   1 
ATOM   2788 C  CB  . TYR B 1 76  ? -10.45354 16.63811  72.27977  1.000 40.86910 ? 76  TYR B CB  1 
ATOM   2789 C  CG  . TYR B 1 76  ? -10.73062 18.10658  72.05291  1.000 44.34557 ? 76  TYR B CG  1 
ATOM   2790 C  CD1 . TYR B 1 76  ? -12.03343 18.58779  71.99038  1.000 47.65674 ? 76  TYR B CD1 1 
ATOM   2791 C  CD2 . TYR B 1 76  ? -9.68953  19.01157  71.88985  1.000 45.18573 ? 76  TYR B CD2 1 
ATOM   2792 C  CE1 . TYR B 1 76  ? -12.29229 19.93482  71.76653  1.000 51.07606 ? 76  TYR B CE1 1 
ATOM   2793 C  CE2 . TYR B 1 76  ? -9.93821  20.36328  71.67541  1.000 48.76142 ? 76  TYR B CE2 1 
ATOM   2794 C  CZ  . TYR B 1 76  ? -11.24103 20.81520  71.61759  1.000 47.16923 ? 76  TYR B CZ  1 
ATOM   2795 O  OH  . TYR B 1 76  ? -11.48582 22.14908  71.40025  1.000 56.78957 ? 76  TYR B OH  1 
ATOM   2796 N  N   . LYS B 1 77  ? -11.32175 13.83868  73.40337  1.000 34.18674 ? 77  LYS B N   1 
ATOM   2797 C  CA  . LYS B 1 77  ? -11.09173 12.41486  73.25155  1.000 37.31943 ? 77  LYS B CA  1 
ATOM   2798 C  C   . LYS B 1 77  ? -10.54722 12.15293  71.85452  1.000 36.51546 ? 77  LYS B C   1 
ATOM   2799 O  O   . LYS B 1 77  ? -11.03882 12.70848  70.86870  1.000 32.44566 ? 77  LYS B O   1 
ATOM   2800 C  CB  . LYS B 1 77  ? -12.38007 11.61559  73.46580  1.000 33.99426 ? 77  LYS B CB  1 
ATOM   2801 C  CG  . LYS B 1 77  ? -12.96974 11.70940  74.86636  1.000 46.40862 ? 77  LYS B CG  1 
ATOM   2802 C  CD  . LYS B 1 77  ? -14.17392 10.77385  75.02225  1.000 54.94658 ? 77  LYS B CD  1 
ATOM   2803 C  CE  . LYS B 1 77  ? -13.73510 9.31614   75.14311  1.000 53.44195 ? 77  LYS B CE  1 
ATOM   2804 N  NZ  . LYS B 1 77  ? -14.71232 8.35912   74.54103  1.000 61.69127 ? 77  LYS B NZ  1 
ATOM   2805 N  N   . ALA B 1 78  ? -9.51974  11.31196  71.77531  1.000 34.44651 ? 78  ALA B N   1 
ATOM   2806 C  CA  . ALA B 1 78  ? -9.01460  10.84715  70.48946  1.000 31.73212 ? 78  ALA B CA  1 
ATOM   2807 C  C   . ALA B 1 78  ? -9.95213  9.74049   70.01687  1.000 42.10252 ? 78  ALA B C   1 
ATOM   2808 O  O   . ALA B 1 78  ? -9.64974  8.54527   70.06253  1.000 39.28115 ? 78  ALA B O   1 
ATOM   2809 C  CB  . ALA B 1 78  ? -7.57215  10.37393  70.60656  1.000 32.75609 ? 78  ALA B CB  1 
ATOM   2810 N  N   . ALA B 1 79  ? -11.13697 10.17338  69.58947  1.000 44.98817 ? 79  ALA B N   1 
ATOM   2811 C  CA  . ALA B 1 79  ? -12.20401 9.27104   69.19799  1.000 38.54405 ? 79  ALA B CA  1 
ATOM   2812 C  C   . ALA B 1 79  ? -13.03088 9.92673   68.10437  1.000 41.84747 ? 79  ALA B C   1 
ATOM   2813 O  O   . ALA B 1 79  ? -13.08051 11.15375  68.00077  1.000 41.54697 ? 79  ALA B O   1 
ATOM   2814 C  CB  . ALA B 1 79  ? -13.09515 8.90382   70.38520  1.000 38.41604 ? 79  ALA B CB  1 
ATOM   2815 N  N   . ILE B 1 80  ? -13.66920 9.09297   67.28741  1.000 38.98973 ? 80  ILE B N   1 
ATOM   2816 C  CA  . ILE B 1 80  ? -14.53839 9.53234   66.20224  1.000 47.79951 ? 80  ILE B CA  1 
ATOM   2817 C  C   . ILE B 1 80  ? -15.85458 8.79553   66.35473  1.000 50.43516 ? 80  ILE B C   1 
ATOM   2818 O  O   . ILE B 1 80  ? -15.85954 7.58380   66.59786  1.000 50.71362 ? 80  ILE B O   1 
ATOM   2819 C  CB  . ILE B 1 80  ? -13.93253 9.23501   64.80853  1.000 47.37824 ? 80  ILE B CB  1 
ATOM   2820 C  CG1 . ILE B 1 80  ? -12.63181 10.02065  64.57345  1.000 54.00218 ? 80  ILE B CG1 1 
ATOM   2821 C  CG2 . ILE B 1 80  ? -14.95493 9.52255   63.70826  1.000 55.46782 ? 80  ILE B CG2 1 
ATOM   2822 C  CD1 . ILE B 1 80  ? -12.81149 11.53915  64.45390  1.000 52.27577 ? 80  ILE B CD1 1 
ATOM   2823 N  N   . ALA B 1 81  ? -16.96932 9.51474   66.20861  1.000 58.41842 ? 81  ALA B N   1 
ATOM   2824 C  CA  . ALA B 1 81  ? -18.30485 8.91550   66.23556  1.000 52.39790 ? 81  ALA B CA  1 
ATOM   2825 C  C   . ALA B 1 81  ? -18.96484 9.14127   64.87940  1.000 59.89435 ? 81  ALA B C   1 
ATOM   2826 O  O   . ALA B 1 81  ? -19.54719 10.20196  64.63258  1.000 67.79918 ? 81  ALA B O   1 
ATOM   2827 C  CB  . ALA B 1 81  ? -19.15745 9.49209   67.36522  1.000 55.49979 ? 81  ALA B CB  1 
ATOM   2828 N  N   . GLY B 1 82  ? -18.88566 8.13948   64.00380  1.000 59.71573 ? 82  GLY B N   1 
ATOM   2829 C  CA  . GLY B 1 82  ? -19.50297 8.19555   62.70131  1.000 59.89564 ? 82  GLY B CA  1 
ATOM   2830 C  C   . GLY B 1 82  ? -20.72057 7.29045   62.62422  1.000 59.79982 ? 82  GLY B C   1 
ATOM   2831 O  O   . GLY B 1 82  ? -21.07754 6.59636   63.57199  1.000 63.93182 ? 82  GLY B O   1 
ATOM   2832 N  N   . GLU B 1 83  ? -21.35881 7.31114   61.45295  1.000 58.61310 ? 83  GLU B N   1 
ATOM   2833 C  CA  . GLU B 1 83  ? -22.46072 6.38650   61.20541  1.000 61.47333 ? 83  GLU B CA  1 
ATOM   2834 C  C   . GLU B 1 83  ? -21.99245 4.94089   61.16502  1.000 60.20445 ? 83  GLU B C   1 
ATOM   2835 O  O   . GLU B 1 83  ? -22.82670 4.03209   61.22924  1.000 63.50760 ? 83  GLU B O   1 
ATOM   2836 C  CB  . GLU B 1 83  ? -23.15285 6.72567   59.89602  1.000 65.51204 ? 83  GLU B CB  1 
ATOM   2837 C  CG  . GLU B 1 83  ? -22.18015 7.03534   58.78088  1.000 68.35850 ? 83  GLU B CG  1 
ATOM   2838 C  CD  . GLU B 1 83  ? -22.69859 8.09487   57.84405  1.000 70.74056 ? 83  GLU B CD  1 
ATOM   2839 O  OE1 . GLU B 1 83  ? -23.77020 7.86696   57.23164  1.000 71.82272 ? 83  GLU B OE1 1 
ATOM   2840 O  OE2 . GLU B 1 83  ? -22.02697 9.14638   57.72368  1.000 70.15903 ? 83  GLU B OE2 1 
ATOM   2841 N  N   . SER B 1 84  ? -20.68037 4.71992   61.05191  1.000 61.30401 ? 84  SER B N   1 
ATOM   2842 C  CA  . SER B 1 84  ? -20.05099 3.41435   61.19982  1.000 61.73834 ? 84  SER B CA  1 
ATOM   2843 C  C   . SER B 1 84  ? -19.70913 3.09640   62.64813  1.000 64.89288 ? 84  SER B C   1 
ATOM   2844 O  O   . SER B 1 84  ? -18.71866 2.39797   62.90466  1.000 68.78490 ? 84  SER B O   1 
ATOM   2845 C  CB  . SER B 1 84  ? -18.78147 3.35172   60.35075  1.000 57.04662 ? 84  SER B CB  1 
ATOM   2846 O  OG  . SER B 1 84  ? -18.94312 4.08474   59.15479  1.000 66.46320 ? 84  SER B OG  1 
ATOM   2847 N  N   . GLY B 1 85  ? -20.47849 3.60701   63.60516  1.000 61.55262 ? 85  GLY B N   1 
ATOM   2848 C  CA  . GLY B 1 85  ? -20.14498 3.40658   64.99246  1.000 52.20007 ? 85  GLY B CA  1 
ATOM   2849 C  C   . GLY B 1 85  ? -19.05135 4.35008   65.45997  1.000 64.29791 ? 85  GLY B C   1 
ATOM   2850 O  O   . GLY B 1 85  ? -18.67061 5.32243   64.79297  1.000 59.02495 ? 85  GLY B O   1 
ATOM   2851 N  N   . PHE B 1 86  ? -18.53209 4.04309   66.64154  1.000 58.64033 ? 86  PHE B N   1 
ATOM   2852 C  CA  . PHE B 1 86  ? -17.59857 4.92374   67.32288  1.000 52.76356 ? 86  PHE B CA  1 
ATOM   2853 C  C   . PHE B 1 86  ? -16.19774 4.34520   67.20202  1.000 48.64222 ? 86  PHE B C   1 
ATOM   2854 O  O   . PHE B 1 86  ? -15.99324 3.14366   67.40605  1.000 53.56954 ? 86  PHE B O   1 
ATOM   2855 C  CB  . PHE B 1 86  ? -17.98905 5.11380   68.79217  1.000 53.42742 ? 86  PHE B CB  1 
ATOM   2856 C  CG  . PHE B 1 86  ? -19.47469 4.97615   69.05415  1.000 73.55879 ? 86  PHE B CG  1 
ATOM   2857 C  CD1 . PHE B 1 86  ? -20.40330 5.71468   68.32470  1.000 70.40284 ? 86  PHE B CD1 1 
ATOM   2858 C  CD2 . PHE B 1 86  ? -19.93912 4.12427   70.05015  1.000 79.49318 ? 86  PHE B CD2 1 
ATOM   2859 C  CE1 . PHE B 1 86  ? -21.75592 5.58297   68.55980  1.000 70.36498 ? 86  PHE B CE1 1 
ATOM   2860 C  CE2 . PHE B 1 86  ? -21.29471 3.99423   70.29571  1.000 77.67385 ? 86  PHE B CE2 1 
ATOM   2861 C  CZ  . PHE B 1 86  ? -22.20416 4.72600   69.54983  1.000 80.82846 ? 86  PHE B CZ  1 
ATOM   2862 N  N   . TYR B 1 87  ? -15.24745 5.19785   66.84437  1.000 50.46611 ? 87  TYR B N   1 
ATOM   2863 C  CA  . TYR B 1 87  ? -13.84868 4.82533   66.69991  1.000 46.34592 ? 87  TYR B CA  1 
ATOM   2864 C  C   . TYR B 1 87  ? -13.03560 5.56532   67.74548  1.000 42.87413 ? 87  TYR B C   1 
ATOM   2865 O  O   . TYR B 1 87  ? -13.28334 6.74443   67.99937  1.000 47.99615 ? 87  TYR B O   1 
ATOM   2866 C  CB  . TYR B 1 87  ? -13.34042 5.17425   65.30279  1.000 44.70961 ? 87  TYR B CB  1 
ATOM   2867 C  CG  . TYR B 1 87  ? -14.00364 4.38538   64.19934  1.000 43.12304 ? 87  TYR B CG  1 
ATOM   2868 C  CD1 . TYR B 1 87  ? -15.32302 4.63537   63.83860  1.000 46.25114 ? 87  TYR B CD1 1 
ATOM   2869 C  CD2 . TYR B 1 87  ? -13.30640 3.40448   63.50633  1.000 42.26801 ? 87  TYR B CD2 1 
ATOM   2870 C  CE1 . TYR B 1 87  ? -15.93947 3.91577   62.82830  1.000 51.76430 ? 87  TYR B CE1 1 
ATOM   2871 C  CE2 . TYR B 1 87  ? -13.90952 2.68133   62.49181  1.000 43.55581 ? 87  TYR B CE2 1 
ATOM   2872 C  CZ  . TYR B 1 87  ? -15.22930 2.93948   62.16292  1.000 48.41261 ? 87  TYR B CZ  1 
ATOM   2873 O  OH  . TYR B 1 87  ? -15.83227 2.23410   61.15704  1.000 49.98829 ? 87  TYR B OH  1 
ATOM   2874 N  N   . LYS B 1 88  ? -12.06887 4.88390   68.35912  1.000 38.03354 ? 88  LYS B N   1 
ATOM   2875 C  CA  . LYS B 1 88  ? -11.24868 5.56785   69.34479  1.000 37.63156 ? 88  LYS B CA  1 
ATOM   2876 C  C   . LYS B 1 88  ? -9.85690  4.95691   69.38964  1.000 36.20527 ? 88  LYS B C   1 
ATOM   2877 O  O   . LYS B 1 88  ? -9.67022  3.75450   69.18635  1.000 36.82509 ? 88  LYS B O   1 
ATOM   2878 C  CB  . LYS B 1 88  ? -11.91089 5.54901   70.72618  1.000 42.43904 ? 88  LYS B CB  1 
ATOM   2879 C  CG  . LYS B 1 88  ? -11.63209 4.33116   71.57137  1.000 43.81508 ? 88  LYS B CG  1 
ATOM   2880 C  CD  . LYS B 1 88  ? -12.74309 4.14570   72.58376  1.000 38.91682 ? 88  LYS B CD  1 
ATOM   2881 C  CE  . LYS B 1 88  ? -12.20026 4.13519   73.98486  1.000 35.77804 ? 88  LYS B CE  1 
ATOM   2882 N  NZ  . LYS B 1 88  ? -13.30284 4.06796   74.97271  1.000 48.60581 ? 88  LYS B NZ  1 
ATOM   2883 N  N   . LEU B 1 89  ? -8.88172  5.81935   69.63024  1.000 34.17748 ? 89  LEU B N   1 
ATOM   2884 C  CA  . LEU B 1 89  ? -7.48006  5.43969   69.72708  1.000 31.54171 ? 89  LEU B CA  1 
ATOM   2885 C  C   . LEU B 1 89  ? -7.16256  5.08047   71.17685  1.000 42.71755 ? 89  LEU B C   1 
ATOM   2886 O  O   . LEU B 1 89  ? -7.42331  5.87259   72.09226  1.000 39.64579 ? 89  LEU B O   1 
ATOM   2887 C  CB  . LEU B 1 89  ? -6.60891  6.60530   69.25764  1.000 36.64198 ? 89  LEU B CB  1 
ATOM   2888 C  CG  . LEU B 1 89  ? -5.09464  6.42088   69.27491  1.000 37.84271 ? 89  LEU B CG  1 
ATOM   2889 C  CD1 . LEU B 1 89  ? -4.73457  5.57338   68.08807  1.000 35.31626 ? 89  LEU B CD1 1 
ATOM   2890 C  CD2 . LEU B 1 89  ? -4.34601  7.74804   69.25878  1.000 25.40358 ? 89  LEU B CD2 1 
ATOM   2891 N  N   . VAL B 1 90  ? -6.60593  3.89611   71.39680  1.000 35.97206 ? 90  VAL B N   1 
ATOM   2892 C  CA  . VAL B 1 90  ? -6.48276  3.44797   72.77663  1.000 39.68435 ? 90  VAL B CA  1 
ATOM   2893 C  C   . VAL B 1 90  ? -5.03685  3.58877   73.23271  1.000 38.27970 ? 90  VAL B C   1 
ATOM   2894 O  O   . VAL B 1 90  ? -4.10950  3.37314   72.44469  1.000 41.25494 ? 90  VAL B O   1 
ATOM   2895 C  CB  . VAL B 1 90  ? -7.01903  2.01746   72.95124  1.000 41.94084 ? 90  VAL B CB  1 
ATOM   2896 C  CG1 . VAL B 1 90  ? -8.35110  1.87078   72.23867  1.000 34.64022 ? 90  VAL B CG1 1 
ATOM   2897 C  CG2 . VAL B 1 90  ? -6.03540  1.00927   72.44490  1.000 42.44743 ? 90  VAL B CG2 1 
ATOM   2898 N  N   . PRO B 1 91  ? -4.80575  3.94811   74.49390  1.000 36.75102 ? 91  PRO B N   1 
ATOM   2899 C  CA  . PRO B 1 91  ? -3.45565  4.28892   74.94266  1.000 36.94774 ? 91  PRO B CA  1 
ATOM   2900 C  C   . PRO B 1 91  ? -2.53418  3.09456   75.11616  1.000 45.59551 ? 91  PRO B C   1 
ATOM   2901 O  O   . PRO B 1 91  ? -1.69777  3.08051   76.03068  1.000 43.41009 ? 91  PRO B O   1 
ATOM   2902 C  CB  . PRO B 1 91  ? -3.72102  4.96629   76.29492  1.000 39.24619 ? 91  PRO B CB  1 
ATOM   2903 C  CG  . PRO B 1 91  ? -4.85772  4.21559   76.81857  1.000 34.98227 ? 91  PRO B CG  1 
ATOM   2904 C  CD  . PRO B 1 91  ? -5.75891  3.97288   75.61266  1.000 36.37727 ? 91  PRO B CD  1 
ATOM   2905 N  N   . THR B 1 92  ? -2.66617  2.07387   74.27839  1.000 45.51201 ? 92  THR B N   1 
ATOM   2906 C  CA  . THR B 1 92  ? -1.65593  1.03552   74.31958  1.000 42.14053 ? 92  THR B CA  1 
ATOM   2907 C  C   . THR B 1 92  ? -0.33829  1.59415   73.77578  1.000 45.41533 ? 92  THR B C   1 
ATOM   2908 O  O   . THR B 1 92  ? -0.22371  2.76391   73.39369  1.000 40.92057 ? 92  THR B O   1 
ATOM   2909 C  CB  . THR B 1 92  ? -2.12500  -0.19270  73.54970  1.000 43.21303 ? 92  THR B CB  1 
ATOM   2910 O  OG1 . THR B 1 92  ? -2.47772  0.18903   72.21799  1.000 42.86720 ? 92  THR B OG1 1 
ATOM   2911 C  CG2 . THR B 1 92  ? -3.35357  -0.80142  74.23593  1.000 40.49184 ? 92  THR B CG2 1 
ATOM   2912 N  N   . ILE B 1 93  ? 0.68297   0.75569   73.77633  1.000 45.63165 ? 93  ILE B N   1 
ATOM   2913 C  CA  . ILE B 1 93  ? 2.00160   1.17655   73.32050  1.000 49.69990 ? 93  ILE B CA  1 
ATOM   2914 C  C   . ILE B 1 93  ? 2.48198   0.11072   72.34703  1.000 44.74750 ? 93  ILE B C   1 
ATOM   2915 O  O   . ILE B 1 93  ? 2.94062   -0.95517  72.78049  1.000 48.65393 ? 93  ILE B O   1 
ATOM   2916 C  CB  . ILE B 1 93  ? 2.96311   1.36826   74.50604  1.000 53.91507 ? 93  ILE B CB  1 
ATOM   2917 C  CG1 . ILE B 1 93  ? 2.43488   2.48170   75.43077  1.000 56.93890 ? 93  ILE B CG1 1 
ATOM   2918 C  CG2 . ILE B 1 93  ? 4.37673   1.66647   74.01564  1.000 45.24677 ? 93  ILE B CG2 1 
ATOM   2919 C  CD1 . ILE B 1 93  ? 3.47566   3.12295   76.32785  1.000 63.25345 ? 93  ILE B CD1 1 
ATOM   2920 N  N   . PRO B 1 94  ? 2.37435   0.33060   71.02746  1.000 48.09153 ? 94  PRO B N   1 
ATOM   2921 C  CA  . PRO B 1 94  ? 1.91081   1.52980   70.33693  1.000 37.78383 ? 94  PRO B CA  1 
ATOM   2922 C  C   . PRO B 1 94  ? 0.40402   1.65101   70.39282  1.000 37.65601 ? 94  PRO B C   1 
ATOM   2923 O  O   . PRO B 1 94  ? -0.25648  0.62245   70.52479  1.000 42.08643 ? 94  PRO B O   1 
ATOM   2924 C  CB  . PRO B 1 94  ? 2.38235   1.30827   68.88941  1.000 40.39627 ? 94  PRO B CB  1 
ATOM   2925 C  CG  . PRO B 1 94  ? 2.94559   -0.05569  68.83514  1.000 47.12159 ? 94  PRO B CG  1 
ATOM   2926 C  CD  . PRO B 1 94  ? 2.57331   -0.76976  70.07957  1.000 52.48364 ? 94  PRO B CD  1 
ATOM   2927 N  N   . PRO B 1 95  ? -0.12741  2.87035   70.29819  1.000 38.99166 ? 95  PRO B N   1 
ATOM   2928 C  CA  . PRO B 1 95  ? -1.58535  3.03813   70.29351  1.000 35.82731 ? 95  PRO B CA  1 
ATOM   2929 C  C   . PRO B 1 95  ? -2.21827  2.12715   69.26329  1.000 41.43102 ? 95  PRO B C   1 
ATOM   2930 O  O   . PRO B 1 95  ? -1.67009  1.91237   68.17665  1.000 39.20951 ? 95  PRO B O   1 
ATOM   2931 C  CB  . PRO B 1 95  ? -1.77544  4.51390   69.93327  1.000 31.55134 ? 95  PRO B CB  1 
ATOM   2932 C  CG  . PRO B 1 95  ? -0.48819  5.16101   70.35676  1.000 34.24087 ? 95  PRO B CG  1 
ATOM   2933 C  CD  . PRO B 1 95  ? 0.57733   4.14399   70.09136  1.000 35.40722 ? 95  PRO B CD  1 
ATOM   2934 N  N   . THR B 1 96  ? -3.34857  1.53923   69.63306  1.000 37.98793 ? 96  THR B N   1 
ATOM   2935 C  CA  . THR B 1 96  ? -4.14437  0.77588   68.68743  1.000 39.03849 ? 96  THR B CA  1 
ATOM   2936 C  C   . THR B 1 96  ? -5.51150  1.43916   68.55706  1.000 42.90123 ? 96  THR B C   1 
ATOM   2937 O  O   . THR B 1 96  ? -5.83055  2.40664   69.25517  1.000 40.85794 ? 96  THR B O   1 
ATOM   2938 C  CB  . THR B 1 96  ? -4.25485  -0.70454  69.10341  1.000 41.85810 ? 96  THR B CB  1 
ATOM   2939 O  OG1 . THR B 1 96  ? -5.00818  -0.83000  70.31213  1.000 45.13725 ? 96  THR B OG1 1 
ATOM   2940 C  CG2 . THR B 1 96  ? -2.87589  -1.30803  69.33234  1.000 44.19094 ? 96  THR B CG2 1 
ATOM   2941 N  N   . ILE B 1 97  ? -6.30966  0.92879   67.62895  1.000 39.22017 ? 97  ILE B N   1 
ATOM   2942 C  CA  . ILE B 1 97  ? -7.61977  1.48344   67.32595  1.000 39.14061 ? 97  ILE B CA  1 
ATOM   2943 C  C   . ILE B 1 97  ? -8.68950  0.48984   67.76117  1.000 43.40182 ? 97  ILE B C   1 
ATOM   2944 O  O   . ILE B 1 97  ? -8.54521  -0.72062  67.56003  1.000 45.29771 ? 97  ILE B O   1 
ATOM   2945 C  CB  . ILE B 1 97  ? -7.71306  1.82649   65.82602  1.000 44.07541 ? 97  ILE B CB  1 
ATOM   2946 C  CG1 . ILE B 1 97  ? -9.07191  2.42524   65.47254  1.000 47.06262 ? 97  ILE B CG1 1 
ATOM   2947 C  CG2 . ILE B 1 97  ? -7.39889  0.62066   64.97152  1.000 56.35762 ? 97  ILE B CG2 1 
ATOM   2948 C  CD1 . ILE B 1 97  ? -9.13281  2.91727   64.02783  1.000 43.58379 ? 97  ILE B CD1 1 
ATOM   2949 N  N   . GLU B 1 98  ? -9.75190  0.99628   68.38616  1.000 40.04771 ? 98  GLU B N   1 
ATOM   2950 C  CA  . GLU B 1 98  ? -10.81770 0.15313   68.91051  1.000 48.60680 ? 98  GLU B CA  1 
ATOM   2951 C  C   . GLU B 1 98  ? -12.14206 0.58745   68.30276  1.000 52.52159 ? 98  GLU B C   1 
ATOM   2952 O  O   . GLU B 1 98  ? -12.54290 1.74771   68.44413  1.000 48.10603 ? 98  GLU B O   1 
ATOM   2953 C  CB  . GLU B 1 98  ? -10.85785 0.22144   70.43558  1.000 48.71725 ? 98  GLU B CB  1 
ATOM   2954 C  CG  . GLU B 1 98  ? -12.15910 -0.20754  71.08837  1.000 53.19171 ? 98  GLU B CG  1 
ATOM   2955 C  CD  . GLU B 1 98  ? -12.00747 -0.36737  72.60122  1.000 58.17130 ? 98  GLU B CD  1 
ATOM   2956 O  OE1 . GLU B 1 98  ? -10.90777 -0.77143  73.04862  1.000 63.26060 ? 98  GLU B OE1 1 
ATOM   2957 O  OE2 . GLU B 1 98  ? -12.97841 -0.09199  73.34208  1.000 55.15410 ? 98  GLU B OE2 1 
ATOM   2958 N  N   . ILE B 1 99  ? -12.80968 -0.34332  67.62330  1.000 51.94381 ? 99  ILE B N   1 
ATOM   2959 C  CA  . ILE B 1 99  ? -14.06343 -0.08417  66.92766  1.000 55.21200 ? 99  ILE B CA  1 
ATOM   2960 C  C   . ILE B 1 99  ? -15.18527 -0.73726  67.70791  1.000 63.06916 ? 99  ILE B C   1 
ATOM   2961 O  O   . ILE B 1 99  ? -15.21573 -1.96598  67.85695  1.000 67.35951 ? 99  ILE B O   1 
ATOM   2962 C  CB  . ILE B 1 99  ? -14.03843 -0.59559  65.47872  1.000 55.65163 ? 99  ILE B CB  1 
ATOM   2963 C  CG1 . ILE B 1 99  ? -12.63268 -0.47192  64.88465  1.000 58.49458 ? 99  ILE B CG1 1 
ATOM   2964 C  CG2 . ILE B 1 99  ? -15.09564 0.11075   64.63765  1.000 51.83517 ? 99  ILE B CG2 1 
ATOM   2965 C  CD1 . ILE B 1 99  ? -12.41076 -1.29808  63.62547  1.000 54.14035 ? 99  ILE B CD1 1 
ATOM   2966 N  N   . ASN B 1 100 ? -16.10188 0.09034   68.20589  1.000 63.84519 ? 100 ASN B N   1 
ATOM   2967 C  CA  . ASN B 1 100 ? -17.28841 -0.37686  68.90748  1.000 64.78704 ? 100 ASN B CA  1 
ATOM   2968 C  C   . ASN B 1 100 ? -16.92087 -1.36785  70.00874  1.000 71.78530 ? 100 ASN B C   1 
ATOM   2969 O  O   . ASN B 1 100 ? -17.60926 -2.36925  70.23339  1.000 71.78836 ? 100 ASN B O   1 
ATOM   2970 C  CB  . ASN B 1 100 ? -18.28698 -0.97664  67.92040  1.000 71.24527 ? 100 ASN B CB  1 
ATOM   2971 C  CG  . ASN B 1 100 ? -18.73375 0.02712   66.86547  1.000 68.85551 ? 100 ASN B CG  1 
ATOM   2972 O  OD1 . ASN B 1 100 ? -19.43322 0.99928   67.16536  1.000 65.92465 ? 100 ASN B OD1 1 
ATOM   2973 N  ND2 . ASN B 1 100 ? -18.32356 -0.20220  65.62566  1.000 65.75454 ? 100 ASN B ND2 1 
ATOM   2974 N  N   . GLY B 1 101 ? -15.81302 -1.08359  70.69043  1.000 65.90081 ? 101 GLY B N   1 
ATOM   2975 C  CA  . GLY B 1 101 ? -15.36949 -1.87302  71.82747  1.000 64.30468 ? 101 GLY B CA  1 
ATOM   2976 C  C   . GLY B 1 101 ? -14.81800 -3.24895  71.50945  1.000 66.62936 ? 101 GLY B C   1 
ATOM   2977 O  O   . GLY B 1 101 ? -15.02766 -4.18580  72.28957  1.000 64.74541 ? 101 GLY B O   1 
ATOM   2978 N  N   . ILE B 1 102 ? -14.11481 -3.39794  70.39115  1.000 60.96775 ? 102 ILE B N   1 
ATOM   2979 C  CA  . ILE B 1 102 ? -13.51347 -4.68113  70.04256  1.000 69.23639 ? 102 ILE B CA  1 
ATOM   2980 C  C   . ILE B 1 102 ? -11.99232 -4.57301  69.95278  1.000 65.87444 ? 102 ILE B C   1 
ATOM   2981 O  O   . ILE B 1 102 ? -11.45035 -3.82382  69.14288  1.000 65.39966 ? 102 ILE B O   1 
ATOM   2982 C  CB  . ILE B 1 102 ? -14.10658 -5.24144  68.72562  1.000 72.04156 ? 102 ILE B CB  1 
ATOM   2983 C  CG1 . ILE B 1 102 ? -15.58166 -5.61593  68.91809  1.000 70.91056 ? 102 ILE B CG1 1 
ATOM   2984 C  CG2 . ILE B 1 102 ? -13.29347 -6.42869  68.22456  1.000 73.10139 ? 102 ILE B CG2 1 
ATOM   2985 C  CD1 . ILE B 1 102 ? -16.31409 -5.93186  67.63141  1.000 67.93662 ? 102 ILE B CD1 1 
ATOM   2986 N  N   . MET B 1 110 ? 3.42456   -9.59887  73.91822  1.000 88.52771 ? 110 MET B N   1 
ATOM   2987 C  CA  . MET B 1 110 ? 3.04880   -9.12425  72.58940  1.000 86.65542 ? 110 MET B CA  1 
ATOM   2988 C  C   . MET B 1 110 ? 4.26317   -8.67817  71.76377  1.000 78.54883 ? 110 MET B C   1 
ATOM   2989 O  O   . MET B 1 110 ? 4.67900   -9.37649  70.83354  1.000 76.83365 ? 110 MET B O   1 
ATOM   2990 C  CB  . MET B 1 110 ? 2.03809   -7.97723  72.70499  1.000 87.15262 ? 110 MET B CB  1 
ATOM   2991 C  CG  . MET B 1 110 ? 0.57820   -8.40701  72.92267  1.000 89.71096 ? 110 MET B CG  1 
ATOM   2992 S  SD  . MET B 1 110 ? -0.38154  -8.75923  71.42080  1.000 96.37667 ? 110 MET B SD  1 
ATOM   2993 C  CE  . MET B 1 110 ? 0.13423   -10.42824 71.00691  1.000 83.54823 ? 110 MET B CE  1 
ATOM   2994 N  N   . ASN B 1 111 ? 4.83530   -7.53262  72.12429  1.000 76.01778 ? 111 ASN B N   1 
ATOM   2995 C  CA  . ASN B 1 111 ? 5.85270   -6.85934  71.32272  1.000 81.22563 ? 111 ASN B CA  1 
ATOM   2996 C  C   . ASN B 1 111 ? 5.41735   -6.62373  69.87394  1.000 77.63091 ? 111 ASN B C   1 
ATOM   2997 O  O   . ASN B 1 111 ? 6.06133   -7.11278  68.93879  1.000 80.25822 ? 111 ASN B O   1 
ATOM   2998 C  CB  . ASN B 1 111 ? 7.17954   -7.60527  71.36204  1.000 73.37969 ? 111 ASN B CB  1 
ATOM   2999 C  CG  . ASN B 1 111 ? 8.19016   -6.93176  72.25578  1.000 82.49944 ? 111 ASN B CG  1 
ATOM   3000 O  OD1 . ASN B 1 111 ? 8.95303   -6.07711  71.80029  1.000 81.23094 ? 111 ASN B OD1 1 
ATOM   3001 N  ND2 . ASN B 1 111 ? 8.21778   -7.31614  73.52751  1.000 94.90984 ? 111 ASN B ND2 1 
ATOM   3002 N  N   . PRO B 1 112 ? 4.35328   -5.85002  69.65131  1.000 72.01151 ? 112 PRO B N   1 
ATOM   3003 C  CA  . PRO B 1 112 ? 3.95538   -5.55740  68.26908  1.000 66.12179 ? 112 PRO B CA  1 
ATOM   3004 C  C   . PRO B 1 112 ? 4.97264   -4.70350  67.55106  1.000 66.58292 ? 112 PRO B C   1 
ATOM   3005 O  O   . PRO B 1 112 ? 5.03212   -4.73202  66.31411  1.000 64.73693 ? 112 PRO B O   1 
ATOM   3006 C  CB  . PRO B 1 112 ? 2.62349   -4.81735  68.43738  1.000 65.19108 ? 112 PRO B CB  1 
ATOM   3007 C  CG  . PRO B 1 112 ? 2.75269   -4.13766  69.75111  1.000 61.66639 ? 112 PRO B CG  1 
ATOM   3008 C  CD  . PRO B 1 112 ? 3.67341   -4.96943  70.61845  1.000 65.28119 ? 112 PRO B CD  1 
ATOM   3009 N  N   . LEU B 1 113 ? 5.77443   -3.94978  68.30488  1.000 63.32682 ? 113 LEU B N   1 
ATOM   3010 C  CA  . LEU B 1 113 ? 6.76261   -3.05669  67.71669  1.000 60.12685 ? 113 LEU B CA  1 
ATOM   3011 C  C   . LEU B 1 113 ? 7.77240   -3.84108  66.89391  1.000 57.42920 ? 113 LEU B C   1 
ATOM   3012 O  O   . LEU B 1 113 ? 8.04375   -3.51439  65.73217  1.000 56.50346 ? 113 LEU B O   1 
ATOM   3013 C  CB  . LEU B 1 113 ? 7.45683   -2.28122  68.83277  1.000 55.02462 ? 113 LEU B CB  1 
ATOM   3014 C  CG  . LEU B 1 113 ? 7.88236   -0.86193  68.52026  1.000 49.83730 ? 113 LEU B CG  1 
ATOM   3015 C  CD1 . LEU B 1 113 ? 6.71810   -0.14367  67.84001  1.000 53.16613 ? 113 LEU B CD1 1 
ATOM   3016 C  CD2 . LEU B 1 113 ? 8.31372   -0.16256  69.79742  1.000 45.78762 ? 113 LEU B CD2 1 
ATOM   3017 N  N   . GLN B 1 114 ? 8.33293   -4.89259  67.48611  1.000 60.10595 ? 114 GLN B N   1 
ATOM   3018 C  CA  . GLN B 1 114 ? 9.23358   -5.76493  66.74623  1.000 59.55097 ? 114 GLN B CA  1 
ATOM   3019 C  C   . GLN B 1 114 ? 8.48501   -6.53247  65.66760  1.000 60.74710 ? 114 GLN B C   1 
ATOM   3020 O  O   . GLN B 1 114 ? 9.02862   -6.78560  64.58611  1.000 56.28311 ? 114 GLN B O   1 
ATOM   3021 C  CB  . GLN B 1 114 ? 9.92860   -6.73536  67.70020  1.000 54.62166 ? 114 GLN B CB  1 
ATOM   3022 C  CG  . GLN B 1 114 ? 11.03991  -7.49968  67.03154  1.000 56.33551 ? 114 GLN B CG  1 
ATOM   3023 C  CD  . GLN B 1 114 ? 12.25289  -6.62797  66.80899  1.000 64.36504 ? 114 GLN B CD  1 
ATOM   3024 O  OE1 . GLN B 1 114 ? 12.61360  -5.81508  67.67323  1.000 64.43664 ? 114 GLN B OE1 1 
ATOM   3025 N  NE2 . GLN B 1 114 ? 12.86800  -6.75351  65.63145  1.000 59.69981 ? 114 GLN B NE2 1 
ATOM   3026 N  N   . ASP B 1 115 ? 7.23817   -6.91862  65.94900  1.000 62.55640 ? 115 ASP B N   1 
ATOM   3027 C  CA  . ASP B 1 115 ? 6.46692   -7.68277  64.97638  1.000 62.03193 ? 115 ASP B CA  1 
ATOM   3028 C  C   . ASP B 1 115 ? 6.30955   -6.89880  63.68352  1.000 53.90216 ? 115 ASP B C   1 
ATOM   3029 O  O   . ASP B 1 115 ? 6.43741   -7.45672  62.58724  1.000 50.90491 ? 115 ASP B O   1 
ATOM   3030 C  CB  . ASP B 1 115 ? 5.10259   -8.04144  65.56477  1.000 69.57682 ? 115 ASP B CB  1 
ATOM   3031 C  CG  . ASP B 1 115 ? 5.15323   -9.28952  66.42531  1.000 77.08484 ? 115 ASP B CG  1 
ATOM   3032 O  OD1 . ASP B 1 115 ? 4.08251   -9.85498  66.73592  1.000 80.57377 ? 115 ASP B OD1 1 
ATOM   3033 O  OD2 . ASP B 1 115 ? 6.27034   -9.69884  66.80460  1.000 82.38590 ? 115 ASP B OD2 1 
ATOM   3034 N  N   . THR B 1 116 ? 6.04064   -5.59753  63.79539  1.000 54.80043 ? 116 THR B N   1 
ATOM   3035 C  CA  . THR B 1 116 ? 6.03869   -4.73071  62.62258  1.000 47.97415 ? 116 THR B CA  1 
ATOM   3036 C  C   . THR B 1 116 ? 7.39995   -4.73432  61.94922  1.000 50.94967 ? 116 THR B C   1 
ATOM   3037 O  O   . THR B 1 116 ? 7.50671   -4.88569  60.72448  1.000 55.36880 ? 116 THR B O   1 
ATOM   3038 C  CB  . THR B 1 116 ? 5.66255   -3.30963  63.02691  1.000 47.32263 ? 116 THR B CB  1 
ATOM   3039 O  OG1 . THR B 1 116 ? 4.43060   -3.32770  63.75397  1.000 54.40775 ? 116 THR B OG1 1 
ATOM   3040 C  CG2 . THR B 1 116 ? 5.52390   -2.43273  61.80495  1.000 41.81124 ? 116 THR B CG2 1 
ATOM   3041 N  N   . ARG B 1 117 ? 8.45831   -4.56471  62.74060  1.000 51.54849 ? 117 ARG B N   1 
ATOM   3042 C  CA  . ARG B 1 117 ? 9.80050   -4.60153  62.18244  1.000 51.28747 ? 117 ARG B CA  1 
ATOM   3043 C  C   . ARG B 1 117 ? 10.03588  -5.91061  61.45316  1.000 51.46095 ? 117 ARG B C   1 
ATOM   3044 O  O   . ARG B 1 117 ? 10.42392  -5.91590  60.27928  1.000 47.77757 ? 117 ARG B O   1 
ATOM   3045 C  CB  . ARG B 1 117 ? 10.83096  -4.40905  63.28471  1.000 49.75887 ? 117 ARG B CB  1 
ATOM   3046 C  CG  . ARG B 1 117 ? 11.00839  -2.97635  63.68075  1.000 50.29686 ? 117 ARG B CG  1 
ATOM   3047 C  CD  . ARG B 1 117 ? 12.37693  -2.75368  64.26575  1.000 55.74702 ? 117 ARG B CD  1 
ATOM   3048 N  NE  . ARG B 1 117 ? 12.42097  -3.12979  65.67080  1.000 62.04071 ? 117 ARG B NE  1 
ATOM   3049 C  CZ  . ARG B 1 117 ? 11.83819  -2.45011  66.64861  1.000 58.87763 ? 117 ARG B CZ  1 
ATOM   3050 N  NH1 . ARG B 1 117 ? 11.11291  -1.37191  66.40504  1.000 56.05339 ? 117 ARG B NH1 1 
ATOM   3051 N  NH2 . ARG B 1 117 ? 11.99025  -2.86206  67.90140  1.000 53.50867 ? 117 ARG B NH2 1 
ATOM   3052 N  N   . ASN B 1 118 ? 9.76358   -7.03152  62.12947  1.000 47.28001 ? 118 ASN B N   1 
ATOM   3053 C  CA  . ASN B 1 118 ? 9.97499   -8.34649  61.53040  1.000 53.98946 ? 118 ASN B CA  1 
ATOM   3054 C  C   . ASN B 1 118 ? 9.20387   -8.49279  60.22504  1.000 52.16442 ? 118 ASN B C   1 
ATOM   3055 O  O   . ASN B 1 118 ? 9.72139   -9.05094  59.24988  1.000 55.16836 ? 118 ASN B O   1 
ATOM   3056 C  CB  . ASN B 1 118 ? 9.56716   -9.44022  62.51694  1.000 59.22686 ? 118 ASN B CB  1 
ATOM   3057 C  CG  . ASN B 1 118 ? 10.57596  -9.61912  63.64356  1.000 63.20063 ? 118 ASN B CG  1 
ATOM   3058 O  OD1 . ASN B 1 118 ? 11.69623  -9.10646  63.57986  1.000 58.36133 ? 118 ASN B OD1 1 
ATOM   3059 N  ND2 . ASN B 1 118 ? 10.17821  -10.34856 64.68483  1.000 60.66459 ? 118 ASN B ND2 1 
ATOM   3060 N  N   . LYS B 1 119 ? 7.96997   -7.98208  60.18523  1.000 49.46757 ? 119 LYS B N   1 
ATOM   3061 C  CA  . LYS B 1 119 ? 7.14510   -8.07858  58.98448  1.000 45.92817 ? 119 LYS B CA  1 
ATOM   3062 C  C   . LYS B 1 119 ? 7.82806   -7.41176  57.79724  1.000 44.00936 ? 119 LYS B C   1 
ATOM   3063 O  O   . LYS B 1 119 ? 7.96873   -8.01355  56.72591  1.000 42.49983 ? 119 LYS B O   1 
ATOM   3064 C  CB  . LYS B 1 119 ? 5.78371   -7.42993  59.23718  1.000 46.95475 ? 119 LYS B CB  1 
ATOM   3065 C  CG  . LYS B 1 119 ? 4.75835   -8.31414  59.93675  1.000 53.20980 ? 119 LYS B CG  1 
ATOM   3066 C  CD  . LYS B 1 119 ? 3.37838   -7.65325  59.91947  1.000 57.02128 ? 119 LYS B CD  1 
ATOM   3067 C  CE  . LYS B 1 119 ? 2.42662   -8.28844  60.93100  1.000 59.77757 ? 119 LYS B CE  1 
ATOM   3068 N  NZ  . LYS B 1 119 ? 1.43392   -7.29116  61.45747  1.000 54.32189 ? 119 LYS B NZ  1 
ATOM   3069 N  N   . VAL B 1 120 ? 8.25292   -6.15554  57.97253  1.000 42.27853 ? 120 VAL B N   1 
ATOM   3070 C  CA  . VAL B 1 120 ? 8.97325   -5.43100  56.92855  1.000 47.48995 ? 120 VAL B CA  1 
ATOM   3071 C  C   . VAL B 1 120 ? 10.34946  -6.04657  56.69931  1.000 55.63734 ? 120 VAL B C   1 
ATOM   3072 O  O   . VAL B 1 120 ? 10.88210  -6.02860  55.57767  1.000 48.67605 ? 120 VAL B O   1 
ATOM   3073 C  CB  . VAL B 1 120 ? 9.07109   -3.94591  57.31364  1.000 39.07565 ? 120 VAL B CB  1 
ATOM   3074 C  CG1 . VAL B 1 120 ? 9.80502   -3.15793  56.23799  1.000 38.40423 ? 120 VAL B CG1 1 
ATOM   3075 C  CG2 . VAL B 1 120 ? 7.68384   -3.38869  57.54952  1.000 42.84881 ? 120 VAL B CG2 1 
ATOM   3076 N  N   . ASN B 1 121 ? 10.92581  -6.63313  57.74435  1.000 47.78080 ? 121 ASN B N   1 
ATOM   3077 C  CA  . ASN B 1 121 ? 12.25377  -7.20294  57.67892  1.000 49.71832 ? 121 ASN B CA  1 
ATOM   3078 C  C   . ASN B 1 121 ? 12.30764  -8.38748  56.72647  1.000 49.68826 ? 121 ASN B C   1 
ATOM   3079 O  O   . ASN B 1 121 ? 13.40391  -8.81208  56.35175  1.000 51.75676 ? 121 ASN B O   1 
ATOM   3080 C  CB  . ASN B 1 121 ? 12.67571  -7.63837  59.08819  1.000 46.90857 ? 121 ASN B CB  1 
ATOM   3081 C  CG  . ASN B 1 121 ? 13.83630  -6.82479  59.63537  1.000 53.60495 ? 121 ASN B CG  1 
ATOM   3082 O  OD1 . ASN B 1 121 ? 14.20391  -5.79406  59.07827  1.000 57.45245 ? 121 ASN B OD1 1 
ATOM   3083 N  ND2 . ASN B 1 121 ? 14.41825  -7.28789  60.73834  1.000 58.75294 ? 121 ASN B ND2 1 
ATOM   3084 N  N   . THR B 1 122 ? 11.14958  -8.93234  56.33175  1.000 44.04628 ? 122 THR B N   1 
ATOM   3085 C  CA  . THR B 1 122 ? 11.12509  -10.09988 55.45741  1.000 51.92401 ? 122 THR B CA  1 
ATOM   3086 C  C   . THR B 1 122 ? 11.33770  -9.73975  53.99377  1.000 52.16751 ? 122 THR B C   1 
ATOM   3087 O  O   . THR B 1 122 ? 11.84412  -10.56550 53.22524  1.000 53.12526 ? 122 THR B O   1 
ATOM   3088 C  CB  . THR B 1 122 ? 9.80507   -10.86671 55.60892  1.000 47.69831 ? 122 THR B CB  1 
ATOM   3089 O  OG1 . THR B 1 122 ? 8.69843   -9.99393  55.34831  1.000 52.29975 ? 122 THR B OG1 1 
ATOM   3090 C  CG2 . THR B 1 122 ? 9.67852   -11.47487 56.98185  1.000 51.43925 ? 122 THR B CG2 1 
ATOM   3091 N  N   . VAL B 1 123 ? 10.96414  -8.53099  53.58692  1.000 52.32616 ? 123 VAL B N   1 
ATOM   3092 C  CA  . VAL B 1 123 ? 11.14453  -8.08767  52.21526  1.000 43.80758 ? 123 VAL B CA  1 
ATOM   3093 C  C   . VAL B 1 123 ? 12.18131  -6.98040  52.08260  1.000 52.34616 ? 123 VAL B C   1 
ATOM   3094 O  O   . VAL B 1 123 ? 12.51093  -6.60542  50.94989  1.000 51.60286 ? 123 VAL B O   1 
ATOM   3095 C  CB  . VAL B 1 123 ? 9.80493   -7.64672  51.60678  1.000 46.59358 ? 123 VAL B CB  1 
ATOM   3096 C  CG1 . VAL B 1 123 ? 8.88476   -8.85050  51.45148  1.000 47.81197 ? 123 VAL B CG1 1 
ATOM   3097 C  CG2 . VAL B 1 123 ? 9.16479   -6.64254  52.51395  1.000 41.84609 ? 123 VAL B CG2 1 
ATOM   3098 N  N   . MET B 1 124 ? 12.73699  -6.46844  53.20178  1.000 52.35213 ? 124 MET B N   1 
ATOM   3099 C  CA  . MET B 1 124 ? 13.65500  -5.32638  53.26196  1.000 50.56982 ? 124 MET B CA  1 
ATOM   3100 C  C   . MET B 1 124 ? 13.56776  -4.36481  52.08356  1.000 48.28147 ? 124 MET B C   1 
ATOM   3101 O  O   . MET B 1 124 ? 14.33726  -4.48496  51.12654  1.000 52.71981 ? 124 MET B O   1 
ATOM   3102 C  CB  . MET B 1 124 ? 15.11280  -5.77949  53.41189  1.000 54.09220 ? 124 MET B CB  1 
ATOM   3103 C  CG  . MET B 1 124 ? 15.34374  -7.08589  54.11495  1.000 56.64901 ? 124 MET B CG  1 
ATOM   3104 S  SD  . MET B 1 124 ? 15.41751  -6.66824  55.87805  1.000 51.51036 ? 124 MET B SD  1 
ATOM   3105 C  CE  . MET B 1 124 ? 16.61675  -5.33931  55.86941  1.000 54.45126 ? 124 MET B CE  1 
ATOM   3106 N  N   . PRO B 1 125 ? 12.67912  -3.38029  52.13873  1.000 48.97572 ? 125 PRO B N   1 
ATOM   3107 C  CA  . PRO B 1 125 ? 12.61621  -2.38016  51.06915  1.000 48.81802 ? 125 PRO B CA  1 
ATOM   3108 C  C   . PRO B 1 125 ? 13.79654  -1.42099  51.13965  1.000 50.88505 ? 125 PRO B C   1 
ATOM   3109 O  O   . PRO B 1 125 ? 14.20633  -0.99858  52.21864  1.000 46.67124 ? 125 PRO B O   1 
ATOM   3110 C  CB  . PRO B 1 125 ? 11.28894  -1.65778  51.34273  1.000 46.89471 ? 125 PRO B CB  1 
ATOM   3111 C  CG  . PRO B 1 125 ? 10.60368  -2.45511  52.45157  1.000 45.28614 ? 125 PRO B CG  1 
ATOM   3112 C  CD  . PRO B 1 125 ? 11.70712  -3.10573  53.20358  1.000 46.27946 ? 125 PRO B CD  1 
ATOM   3113 N  N   . ARG B 1 126 ? 14.33277  -1.06263  49.97230  1.000 52.12266 ? 126 ARG B N   1 
ATOM   3114 C  CA  . ARG B 1 126 ? 15.51506  -0.21514  49.86362  1.000 48.50563 ? 126 ARG B CA  1 
ATOM   3115 C  C   . ARG B 1 126 ? 15.12709  1.20516   49.45242  1.000 56.30030 ? 126 ARG B C   1 
ATOM   3116 O  O   . ARG B 1 126 ? 13.95878  1.51281   49.19569  1.000 56.42536 ? 126 ARG B O   1 
ATOM   3117 C  CB  . ARG B 1 126 ? 16.50494  -0.81321  48.86646  1.000 58.96604 ? 126 ARG B CB  1 
ATOM   3118 C  CG  . ARG B 1 126 ? 17.52356  -1.76526  49.46096  1.000 68.15207 ? 126 ARG B CG  1 
ATOM   3119 C  CD  . ARG B 1 126 ? 17.03279  -3.20341  49.49358  1.000 66.20509 ? 126 ARG B CD  1 
ATOM   3120 N  NE  . ARG B 1 126 ? 17.92415  -4.04513  50.28541  1.000 71.88999 ? 126 ARG B NE  1 
ATOM   3121 C  CZ  . ARG B 1 126 ? 17.92106  -4.12774  51.61026  1.000 69.74507 ? 126 ARG B CZ  1 
ATOM   3122 N  NH1 . ARG B 1 126 ? 17.10311  -3.39542  52.34886  1.000 62.87761 ? 126 ARG B NH1 1 
ATOM   3123 N  NH2 . ARG B 1 126 ? 18.77211  -4.95758  52.20967  1.000 73.65486 ? 126 ARG B NH2 1 
ATOM   3124 N  N   . GLU B 1 127 ? 16.13477  2.08036   49.36715  1.000 60.94703 ? 127 GLU B N   1 
ATOM   3125 C  CA  . GLU B 1 127 ? 15.87793  3.49130   49.07668  1.000 64.99449 ? 127 GLU B CA  1 
ATOM   3126 C  C   . GLU B 1 127 ? 15.22258  3.68433   47.71145  1.000 65.60524 ? 127 GLU B C   1 
ATOM   3127 O  O   . GLU B 1 127 ? 14.23277  4.41373   47.58470  1.000 64.30947 ? 127 GLU B O   1 
ATOM   3128 C  CB  . GLU B 1 127 ? 17.17345  4.29755   49.17486  1.000 67.01715 ? 127 GLU B CB  1 
ATOM   3129 C  CG  . GLU B 1 127 ? 17.64418  4.51982   50.60350  1.000 77.06623 ? 127 GLU B CG  1 
ATOM   3130 C  CD  . GLU B 1 127 ? 17.69887  5.99969   50.98080  1.000 88.61023 ? 127 GLU B CD  1 
ATOM   3131 O  OE1 . GLU B 1 127 ? 17.53597  6.32352   52.18116  1.000 87.09204 ? 127 GLU B OE1 1 
ATOM   3132 O  OE2 . GLU B 1 127 ? 17.92325  6.83597   50.07636  1.000 90.30078 ? 127 GLU B OE2 1 
ATOM   3133 N  N   . GLY B 1 128 ? 15.75614  3.05314   46.67529  1.000 57.02474 ? 128 GLY B N   1 
ATOM   3134 C  CA  . GLY B 1 128 ? 15.14104  3.23179   45.37247  1.000 63.34180 ? 128 GLY B CA  1 
ATOM   3135 C  C   . GLY B 1 128 ? 13.97512  2.29907   45.08798  1.000 66.02157 ? 128 GLY B C   1 
ATOM   3136 O  O   . GLY B 1 128 ? 13.95168  1.66611   44.02449  1.000 63.11176 ? 128 GLY B O   1 
ATOM   3137 N  N   . GLU B 1 129 ? 12.99559  2.20649   45.99713  1.000 49.44095 ? 129 GLU B N   1 
ATOM   3138 C  CA  . GLU B 1 129 ? 12.00058  1.14467   45.90076  1.000 45.88286 ? 129 GLU B CA  1 
ATOM   3139 C  C   . GLU B 1 129 ? 10.61297  1.63513   46.28290  1.000 40.50623 ? 129 GLU B C   1 
ATOM   3140 O  O   . GLU B 1 129 ? 10.44700  2.61105   47.01547  1.000 42.74900 ? 129 GLU B O   1 
ATOM   3141 C  CB  . GLU B 1 129 ? 12.36972  -0.05937  46.77393  1.000 46.98658 ? 129 GLU B CB  1 
ATOM   3142 C  CG  . GLU B 1 129 ? 13.56342  -0.82347  46.24585  1.000 53.77187 ? 129 GLU B CG  1 
ATOM   3143 C  CD  . GLU B 1 129 ? 13.67767  -2.21543  46.81119  1.000 50.64521 ? 129 GLU B CD  1 
ATOM   3144 O  OE1 . GLU B 1 129 ? 13.01659  -2.51313  47.82708  1.000 55.35799 ? 129 GLU B OE1 1 
ATOM   3145 O  OE2 . GLU B 1 129 ? 14.42893  -3.01679  46.22366  1.000 54.17255 ? 129 GLU B OE2 1 
ATOM   3146 N  N   . THR B 1 130 ? 9.60614   0.92752   45.77426  1.000 37.22754 ? 130 THR B N   1 
ATOM   3147 C  CA  . THR B 1 130 ? 8.20569   1.22991   46.04322  1.000 41.38053 ? 130 THR B CA  1 
ATOM   3148 C  C   . THR B 1 130 ? 7.54694   0.00416   46.65554  1.000 36.16845 ? 130 THR B C   1 
ATOM   3149 O  O   . THR B 1 130 ? 7.65668   -1.09820  46.10603  1.000 40.95256 ? 130 THR B O   1 
ATOM   3150 C  CB  . THR B 1 130 ? 7.46405   1.62816   44.76385  1.000 35.67063 ? 130 THR B CB  1 
ATOM   3151 O  OG1 . THR B 1 130 ? 8.03303   2.83033   44.24812  1.000 41.65809 ? 130 THR B OG1 1 
ATOM   3152 C  CG2 . THR B 1 130 ? 6.00889   1.88112   45.06346  1.000 37.62327 ? 130 THR B CG2 1 
ATOM   3153 N  N   . VAL B 1 131 ? 6.85814   0.19544   47.77981  1.000 39.28956 ? 131 VAL B N   1 
ATOM   3154 C  CA  . VAL B 1 131 ? 6.13176   -0.87561  48.45043  1.000 33.71250 ? 131 VAL B CA  1 
ATOM   3155 C  C   . VAL B 1 131 ? 4.64153   -0.57833  48.40413  1.000 33.28176 ? 131 VAL B C   1 
ATOM   3156 O  O   . VAL B 1 131 ? 4.22080   0.57327   48.58308  1.000 31.40000 ? 131 VAL B O   1 
ATOM   3157 C  CB  . VAL B 1 131 ? 6.60417   -1.05595  49.90745  1.000 38.80694 ? 131 VAL B CB  1 
ATOM   3158 C  CG1 . VAL B 1 131 ? 6.65209   0.25365   50.58893  1.000 41.31284 ? 131 VAL B CG1 1 
ATOM   3159 C  CG2 . VAL B 1 131 ? 5.62819   -1.93809  50.68898  1.000 32.62204 ? 131 VAL B CG2 1 
ATOM   3160 N  N   . LEU B 1 132 ? 3.84270   -1.61591  48.15821  1.000 28.69088 ? 132 LEU B N   1 
ATOM   3161 C  CA  . LEU B 1 132 ? 2.41021   -1.55245  48.40262  1.000 32.91405 ? 132 LEU B CA  1 
ATOM   3162 C  C   . LEU B 1 132 ? 2.12849   -2.12444  49.78085  1.000 26.85478 ? 132 LEU B C   1 
ATOM   3163 O  O   . LEU B 1 132 ? 2.50014   -3.26629  50.07311  1.000 24.13421 ? 132 LEU B O   1 
ATOM   3164 C  CB  . LEU B 1 132 ? 1.61013   -2.33119  47.36060  1.000 25.15616 ? 132 LEU B CB  1 
ATOM   3165 C  CG  . LEU B 1 132 ? 0.10903   -2.34605  47.66199  1.000 33.84409 ? 132 LEU B CG  1 
ATOM   3166 C  CD1 . LEU B 1 132 ? -0.43553  -0.91057  47.77920  1.000 30.52558 ? 132 LEU B CD1 1 
ATOM   3167 C  CD2 . LEU B 1 132 ? -0.69349  -3.13928  46.61740  1.000 29.88536 ? 132 LEU B CD2 1 
ATOM   3168 N  N   . ASP B 1 133 ? 1.45095   -1.35038  50.60764  1.000 25.09873 ? 133 ASP B N   1 
ATOM   3169 C  CA  . ASP B 1 133 ? 0.95281   -1.83391  51.88749  1.000 28.18646 ? 133 ASP B CA  1 
ATOM   3170 C  C   . ASP B 1 133 ? -0.56330  -1.92969  51.77602  1.000 28.64375 ? 133 ASP B C   1 
ATOM   3171 O  O   . ASP B 1 133 ? -1.25054  -0.90605  51.72961  1.000 28.01220 ? 133 ASP B O   1 
ATOM   3172 C  CB  . ASP B 1 133 ? 1.36565   -0.90341  53.02063  1.000 30.39764 ? 133 ASP B CB  1 
ATOM   3173 C  CG  . ASP B 1 133 ? 0.86894   -1.38275  54.34504  1.000 31.62010 ? 133 ASP B CG  1 
ATOM   3174 O  OD1 . ASP B 1 133 ? 1.08757   -2.56716  54.63318  1.000 34.61315 ? 133 ASP B OD1 1 
ATOM   3175 O  OD2 . ASP B 1 133 ? 0.23650   -0.59881  55.07797  1.000 34.95194 ? 133 ASP B OD2 1 
ATOM   3176 N  N   . THR B 1 134 ? -1.09381  -3.15106  51.72919  1.000 28.93967 ? 134 THR B N   1 
ATOM   3177 C  CA  . THR B 1 134 ? -2.48299  -3.28384  51.29395  1.000 36.20814 ? 134 THR B CA  1 
ATOM   3178 C  C   . THR B 1 134 ? -3.50530  -2.94068  52.36916  1.000 33.74317 ? 134 THR B C   1 
ATOM   3179 O  O   . THR B 1 134 ? -4.64165  -2.59615  52.03457  1.000 34.65140 ? 134 THR B O   1 
ATOM   3180 C  CB  . THR B 1 134 ? -2.74995  -4.69008  50.77731  1.000 35.16999 ? 134 THR B CB  1 
ATOM   3181 O  OG1 . THR B 1 134 ? -2.29214  -5.64215  51.73936  1.000 32.06787 ? 134 THR B OG1 1 
ATOM   3182 C  CG2 . THR B 1 134 ? -2.03194  -4.90893  49.48214  1.000 34.39961 ? 134 THR B CG2 1 
ATOM   3183 N  N   A CYS B 1 135 ? -3.13459  -3.01005  53.64585  0.702 36.24413 ? 135 CYS B N   1 
ATOM   3184 N  N   B CYS B 1 135 ? -3.14306  -3.02727  53.64371  0.298 35.91510 ? 135 CYS B N   1 
ATOM   3185 C  CA  A CYS B 1 135 ? -4.05406  -2.72745  54.75215  0.702 35.50825 ? 135 CYS B CA  1 
ATOM   3186 C  CA  B CYS B 1 135 ? -4.06223  -2.70569  54.73639  0.298 35.31361 ? 135 CYS B CA  1 
ATOM   3187 C  C   A CYS B 1 135 ? -3.35134  -1.78409  55.72133  0.702 35.62273 ? 135 CYS B C   1 
ATOM   3188 C  C   B CYS B 1 135 ? -3.33542  -1.77967  55.70273  0.298 35.43787 ? 135 CYS B C   1 
ATOM   3189 O  O   A CYS B 1 135 ? -2.57277  -2.23897  56.56465  0.702 35.48359 ? 135 CYS B O   1 
ATOM   3190 O  O   B CYS B 1 135 ? -2.53395  -2.23980  56.51989  0.298 34.95665 ? 135 CYS B O   1 
ATOM   3191 C  CB  A CYS B 1 135 ? -4.48434  -4.01754  55.44352  0.702 34.31247 ? 135 CYS B CB  1 
ATOM   3192 C  CB  B CYS B 1 135 ? -4.55970  -3.97049  55.42546  0.298 34.34404 ? 135 CYS B CB  1 
ATOM   3193 S  SG  A CYS B 1 135 ? -5.80597  -3.85823  56.65541  0.702 41.16500 ? 135 CYS B SG  1 
ATOM   3194 S  SG  B CYS B 1 135 ? -4.54486  -5.43657  54.34978  0.298 37.01393 ? 135 CYS B SG  1 
ATOM   3195 N  N   . MET B 1 136 ? -3.60293  -0.47591  55.57701  1.000 29.85949 ? 136 MET B N   1 
ATOM   3196 C  CA  . MET B 1 136 ? -3.04937  0.51140   56.50245  1.000 29.87454 ? 136 MET B CA  1 
ATOM   3197 C  C   . MET B 1 136 ? -3.21536  0.12883   57.96026  1.000 34.92333 ? 136 MET B C   1 
ATOM   3198 O  O   . MET B 1 136 ? -2.23785  -0.00625  58.70088  1.000 31.76861 ? 136 MET B O   1 
ATOM   3199 C  CB  . MET B 1 136 ? -3.75756  1.85097   56.40175  1.000 39.68409 ? 136 MET B CB  1 
ATOM   3200 C  CG  . MET B 1 136 ? -2.88710  2.99648   56.82834  1.000 33.27784 ? 136 MET B CG  1 
ATOM   3201 S  SD  . MET B 1 136 ? -3.11586  4.50385   55.96989  1.000 22.85402 ? 136 MET B SD  1 
ATOM   3202 C  CE  . MET B 1 136 ? -4.38482  5.18073   57.07003  1.000 30.07593 ? 136 MET B CE  1 
ATOM   3203 N  N   . GLY B 1 137 ? -4.46699  0.09349   58.41408  1.000 31.41123 ? 137 GLY B N   1 
ATOM   3204 C  CA  . GLY B 1 137 ? -4.71339  0.25878   59.83834  1.000 33.38849 ? 137 GLY B CA  1 
ATOM   3205 C  C   . GLY B 1 137 ? -4.20537  1.61865   60.27444  1.000 34.91348 ? 137 GLY B C   1 
ATOM   3206 O  O   . GLY B 1 137 ? -4.33191  2.61257   59.55825  1.000 38.42872 ? 137 GLY B O   1 
ATOM   3207 N  N   . LEU B 1 138 ? -3.59298  1.66900   61.45603  1.000 34.29064 ? 138 LEU B N   1 
ATOM   3208 C  CA  . LEU B 1 138 ? -2.94722  2.90435   61.87422  1.000 29.32639 ? 138 LEU B CA  1 
ATOM   3209 C  C   . LEU B 1 138 ? -1.64959  3.16977   61.13119  1.000 33.08375 ? 138 LEU B C   1 
ATOM   3210 O  O   . LEU B 1 138 ? -0.98734  4.17080   61.42894  1.000 33.66696 ? 138 LEU B O   1 
ATOM   3211 C  CB  . LEU B 1 138 ? -2.67367  2.86630   63.37119  1.000 29.75264 ? 138 LEU B CB  1 
ATOM   3212 C  CG  . LEU B 1 138 ? -3.92010  2.99619   64.23526  1.000 33.21248 ? 138 LEU B CG  1 
ATOM   3213 C  CD1 . LEU B 1 138 ? -3.55600  3.05039   65.74580  1.000 37.51784 ? 138 LEU B CD1 1 
ATOM   3214 C  CD2 . LEU B 1 138 ? -4.72708  4.21195   63.79982  1.000 31.50702 ? 138 LEU B CD2 1 
ATOM   3215 N  N   . GLY B 1 139 ? -1.24723  2.29034   60.21989  1.000 28.16919 ? 139 GLY B N   1 
ATOM   3216 C  CA  . GLY B 1 139 ? -0.16314  2.58723   59.31004  1.000 32.83156 ? 139 GLY B CA  1 
ATOM   3217 C  C   . GLY B 1 139 ? 1.21878   2.25699   59.81670  1.000 34.26689 ? 139 GLY B C   1 
ATOM   3218 O  O   . GLY B 1 139 ? 2.19513   2.75562   59.25050  1.000 31.81352 ? 139 GLY B O   1 
ATOM   3219 N  N   . TYR B 1 140 ? 1.33441   1.42809   60.85749  1.000 37.38211 ? 140 TYR B N   1 
ATOM   3220 C  CA  . TYR B 1 140 ? 2.63908   1.12093   61.43839  1.000 34.48496 ? 140 TYR B CA  1 
ATOM   3221 C  C   . TYR B 1 140 ? 3.54494   0.37639   60.47074  1.000 27.73550 ? 140 TYR B C   1 
ATOM   3222 O  O   . TYR B 1 140 ? 4.76506   0.56057   60.50423  1.000 30.71248 ? 140 TYR B O   1 
ATOM   3223 C  CB  . TYR B 1 140 ? 2.46520   0.29836   62.71259  1.000 28.64398 ? 140 TYR B CB  1 
ATOM   3224 C  CG  . TYR B 1 140 ? 1.79990   1.07546   63.81235  1.000 38.11376 ? 140 TYR B CG  1 
ATOM   3225 C  CD1 . TYR B 1 140 ? 1.99116   2.44346   63.92559  1.000 34.46741 ? 140 TYR B CD1 1 
ATOM   3226 C  CD2 . TYR B 1 140 ? 0.96062   0.45247   64.71742  1.000 33.68392 ? 140 TYR B CD2 1 
ATOM   3227 C  CE1 . TYR B 1 140 ? 1.37967   3.16483   64.91238  1.000 37.79297 ? 140 TYR B CE1 1 
ATOM   3228 C  CE2 . TYR B 1 140 ? 0.33527   1.16951   65.71493  1.000 37.41716 ? 140 TYR B CE2 1 
ATOM   3229 C  CZ  . TYR B 1 140 ? 0.55719   2.52992   65.81078  1.000 38.98449 ? 140 TYR B CZ  1 
ATOM   3230 O  OH  . TYR B 1 140 ? -0.05578  3.26270   66.80207  1.000 36.41469 ? 140 TYR B OH  1 
ATOM   3231 N  N   . THR B 1 141 ? 2.98364   -0.48681  59.62991  1.000 33.60152 ? 141 THR B N   1 
ATOM   3232 C  CA  . THR B 1 141 ? 3.81300   -1.20845  58.67276  1.000 35.08354 ? 141 THR B CA  1 
ATOM   3233 C  C   . THR B 1 141 ? 4.29965   -0.27774  57.57015  1.000 33.14195 ? 141 THR B C   1 
ATOM   3234 O  O   . THR B 1 141 ? 5.49192   -0.25243  57.23754  1.000 36.45186 ? 141 THR B O   1 
ATOM   3235 C  CB  . THR B 1 141 ? 3.03295   -2.38453  58.08990  1.000 30.48795 ? 141 THR B CB  1 
ATOM   3236 O  OG1 . THR B 1 141 ? 2.98222   -3.43200  59.05442  1.000 35.03617 ? 141 THR B OG1 1 
ATOM   3237 C  CG2 . THR B 1 141 ? 3.71496   -2.92215  56.86277  1.000 32.07873 ? 141 THR B CG2 1 
ATOM   3238 N  N   . ALA B 1 142 ? 3.38206   0.49524   56.99506  1.000 37.35906 ? 142 ALA B N   1 
ATOM   3239 C  CA  . ALA B 1 142 ? 3.74375   1.48371   55.99004  1.000 33.96134 ? 142 ALA B CA  1 
ATOM   3240 C  C   . ALA B 1 142 ? 4.79709   2.43348   56.50956  1.000 34.03151 ? 142 ALA B C   1 
ATOM   3241 O  O   . ALA B 1 142 ? 5.67322   2.87087   55.75585  1.000 35.55475 ? 142 ALA B O   1 
ATOM   3242 C  CB  . ALA B 1 142 ? 2.50896   2.27091   55.56359  1.000 26.85536 ? 142 ALA B CB  1 
ATOM   3243 N  N   . ILE B 1 143 ? 4.73727   2.75117   57.79443  1.000 30.15850 ? 143 ILE B N   1 
ATOM   3244 C  CA  . ILE B 1 143 ? 5.70751   3.66485   58.37269  1.000 30.33607 ? 143 ILE B CA  1 
ATOM   3245 C  C   . ILE B 1 143 ? 7.07866   3.01528   58.35716  1.000 30.04754 ? 143 ILE B C   1 
ATOM   3246 O  O   . ILE B 1 143 ? 8.03397   3.55106   57.79213  1.000 38.46589 ? 143 ILE B O   1 
ATOM   3247 C  CB  . ILE B 1 143 ? 5.29787   4.03832   59.80872  1.000 29.95642 ? 143 ILE B CB  1 
ATOM   3248 C  CG1 . ILE B 1 143 ? 4.29956   5.15956   59.76391  1.000 37.27941 ? 143 ILE B CG1 1 
ATOM   3249 C  CG2 . ILE B 1 143 ? 6.47876   4.53071   60.58960  1.000 40.63389 ? 143 ILE B CG2 1 
ATOM   3250 C  CD1 . ILE B 1 143 ? 4.85594   6.26537   59.04849  1.000 47.51705 ? 143 ILE B CD1 1 
ATOM   3251 N  N   . GLU B 1 144 ? 7.18139   1.85177   59.00735  1.000 31.39893 ? 144 GLU B N   1 
ATOM   3252 C  CA  . GLU B 1 144 ? 8.41113   1.07634   59.05021  1.000 33.62258 ? 144 GLU B CA  1 
ATOM   3253 C  C   . GLU B 1 144 ? 8.96204   0.83996   57.65785  1.000 40.51011 ? 144 GLU B C   1 
ATOM   3254 O  O   . GLU B 1 144 ? 10.16911  0.98173   57.42613  1.000 44.89997 ? 144 GLU B O   1 
ATOM   3255 C  CB  . GLU B 1 144 ? 8.13849   -0.25369  59.76329  1.000 32.42060 ? 144 GLU B CB  1 
ATOM   3256 C  CG  . GLU B 1 144 ? 9.32018   -1.16848  59.91780  1.000 40.25243 ? 144 GLU B CG  1 
ATOM   3257 C  CD  . GLU B 1 144 ? 10.31593  -0.66515  60.92590  1.000 41.11409 ? 144 GLU B CD  1 
ATOM   3258 O  OE1 . GLU B 1 144 ? 9.92152   0.14714   61.79156  1.000 50.56136 ? 144 GLU B OE1 1 
ATOM   3259 O  OE2 . GLU B 1 144 ? 11.49144  -1.08075  60.85967  1.000 47.98683 ? 144 GLU B OE2 1 
ATOM   3260 N  N   . ALA B 1 145 ? 8.08814   0.48776   56.71355  1.000 34.29884 ? 145 ALA B N   1 
ATOM   3261 C  CA  . ALA B 1 145 ? 8.53829   0.25274   55.35045  1.000 31.14751 ? 145 ALA B CA  1 
ATOM   3262 C  C   . ALA B 1 145 ? 9.22278   1.48240   54.77591  1.000 31.95417 ? 145 ALA B C   1 
ATOM   3263 O  O   . ALA B 1 145 ? 10.24976  1.36308   54.10326  1.000 42.34000 ? 145 ALA B O   1 
ATOM   3264 C  CB  . ALA B 1 145 ? 7.35780   -0.16969  54.48337  1.000 33.99766 ? 145 ALA B CB  1 
ATOM   3265 N  N   . SER B 1 146 ? 8.69776   2.67972   55.05440  1.000 36.93235 ? 146 SER B N   1 
ATOM   3266 C  CA  . SER B 1 146 ? 9.28530   3.87474   54.44564  1.000 40.83521 ? 146 SER B CA  1 
ATOM   3267 C  C   . SER B 1 146 ? 10.56017  4.30474   55.13885  1.000 42.93524 ? 146 SER B C   1 
ATOM   3268 O  O   . SER B 1 146 ? 11.45072  4.86939   54.49123  1.000 49.27875 ? 146 SER B O   1 
ATOM   3269 C  CB  . SER B 1 146 ? 8.31344   5.04561   54.46005  1.000 32.06504 ? 146 SER B CB  1 
ATOM   3270 O  OG  . SER B 1 146 ? 8.38950   5.74339   55.67880  1.000 42.10774 ? 146 SER B OG  1 
ATOM   3271 N  N   . LYS B 1 147 ? 10.65934  4.05299   56.44389  1.000 39.23503 ? 147 LYS B N   1 
ATOM   3272 C  CA  . LYS B 1 147 ? 11.87779  4.37301   57.17110  1.000 44.22919 ? 147 LYS B CA  1 
ATOM   3273 C  C   . LYS B 1 147 ? 13.06681  3.59557   56.63492  1.000 43.86089 ? 147 LYS B C   1 
ATOM   3274 O  O   . LYS B 1 147 ? 14.21443  3.96876   56.89605  1.000 47.70227 ? 147 LYS B O   1 
ATOM   3275 C  CB  . LYS B 1 147 ? 11.67067  4.09087   58.65454  1.000 44.05780 ? 147 LYS B CB  1 
ATOM   3276 C  CG  . LYS B 1 147 ? 10.52863  4.87447   59.22480  1.000 41.40227 ? 147 LYS B CG  1 
ATOM   3277 C  CD  . LYS B 1 147 ? 10.62753  5.02024   60.72860  1.000 44.46944 ? 147 LYS B CD  1 
ATOM   3278 C  CE  . LYS B 1 147 ? 9.73555   6.17127   61.16457  1.000 48.97436 ? 147 LYS B CE  1 
ATOM   3279 N  NZ  . LYS B 1 147 ? 10.20424  7.47219   60.59003  1.000 48.67145 ? 147 LYS B NZ  1 
ATOM   3280 N  N   . ARG B 1 148 ? 12.80991  2.51392   55.90070  1.000 47.85499 ? 148 ARG B N   1 
ATOM   3281 C  CA  . ARG B 1 148 ? 13.83381  1.84901   55.12030  1.000 41.61298 ? 148 ARG B CA  1 
ATOM   3282 C  C   . ARG B 1 148 ? 14.22103  2.64756   53.88725  1.000 45.89905 ? 148 ARG B C   1 
ATOM   3283 O  O   . ARG B 1 148 ? 15.14688  2.24380   53.17371  1.000 49.77556 ? 148 ARG B O   1 
ATOM   3284 C  CB  . ARG B 1 148 ? 13.34235  0.46330   54.70995  1.000 42.55658 ? 148 ARG B CB  1 
ATOM   3285 C  CG  . ARG B 1 148 ? 12.68077  -0.30946  55.83065  1.000 40.79131 ? 148 ARG B CG  1 
ATOM   3286 C  CD  . ARG B 1 148 ? 13.66639  -0.57438  56.93882  1.000 41.77172 ? 148 ARG B CD  1 
ATOM   3287 N  NE  . ARG B 1 148 ? 13.05697  -1.31018  58.03614  1.000 48.50506 ? 148 ARG B NE  1 
ATOM   3288 C  CZ  . ARG B 1 148 ? 13.11246  -2.62595  58.18064  1.000 53.29951 ? 148 ARG B CZ  1 
ATOM   3289 N  NH1 . ARG B 1 148 ? 13.72867  -3.39023  57.29459  1.000 51.95139 ? 148 ARG B NH1 1 
ATOM   3290 N  NH2 . ARG B 1 148 ? 12.54346  -3.18645  59.24788  1.000 45.49574 ? 148 ARG B NH2 1 
ATOM   3291 N  N   . GLY B 1 149 ? 13.54861  3.76379   53.62750  1.000 46.17924 ? 149 GLY B N   1 
ATOM   3292 C  CA  . GLY B 1 149 ? 13.81681  4.56145   52.45626  1.000 47.07481 ? 149 GLY B CA  1 
ATOM   3293 C  C   . GLY B 1 149 ? 12.93881  4.26184   51.26578  1.000 52.30221 ? 149 GLY B C   1 
ATOM   3294 O  O   . GLY B 1 149 ? 13.24423  4.72795   50.16677  1.000 52.42406 ? 149 GLY B O   1 
ATOM   3295 N  N   . ALA B 1 150 ? 11.85207  3.52057   51.44673  1.000 48.75329 ? 150 ALA B N   1 
ATOM   3296 C  CA  . ALA B 1 150 ? 10.97488  3.14301   50.34902  1.000 41.82182 ? 150 ALA B CA  1 
ATOM   3297 C  C   . ALA B 1 150 ? 9.79079   4.09238   50.24865  1.000 37.56693 ? 150 ALA B C   1 
ATOM   3298 O  O   . ALA B 1 150 ? 9.28370   4.58590   51.25841  1.000 40.02745 ? 150 ALA B O   1 
ATOM   3299 C  CB  . ALA B 1 150 ? 10.46243  1.71779   50.52339  1.000 41.96678 ? 150 ALA B CB  1 
ATOM   3300 N  N   . TYR B 1 151 ? 9.38009   4.37056   49.02021  1.000 37.04753 ? 151 TYR B N   1 
ATOM   3301 C  CA  . TYR B 1 151 ? 8.09796   5.00218   48.78604  1.000 30.93281 ? 151 TYR B CA  1 
ATOM   3302 C  C   . TYR B 1 151 ? 7.02001   3.97657   49.05799  1.000 32.36870 ? 151 TYR B C   1 
ATOM   3303 O  O   . TYR B 1 151 ? 7.09980   2.84266   48.57425  1.000 40.50611 ? 151 TYR B O   1 
ATOM   3304 C  CB  . TYR B 1 151 ? 8.00992   5.50778   47.34415  1.000 30.85883 ? 151 TYR B CB  1 
ATOM   3305 C  CG  . TYR B 1 151 ? 6.80705   6.38044   47.07737  1.000 30.29751 ? 151 TYR B CG  1 
ATOM   3306 C  CD1 . TYR B 1 151 ? 5.55654   5.82907   46.85140  1.000 32.99817 ? 151 TYR B CD1 1 
ATOM   3307 C  CD2 . TYR B 1 151 ? 6.92785   7.76380   47.04574  1.000 32.89590 ? 151 TYR B CD2 1 
ATOM   3308 C  CE1 . TYR B 1 151 ? 4.44120   6.64082   46.62609  1.000 32.24396 ? 151 TYR B CE1 1 
ATOM   3309 C  CE2 . TYR B 1 151 ? 5.83301   8.57385   46.82619  1.000 37.36896 ? 151 TYR B CE2 1 
ATOM   3310 C  CZ  . TYR B 1 151 ? 4.59422   8.00846   46.61326  1.000 32.13489 ? 151 TYR B CZ  1 
ATOM   3311 O  OH  . TYR B 1 151 ? 3.51841   8.82991   46.38035  1.000 39.57656 ? 151 TYR B OH  1 
ATOM   3312 N  N   . VAL B 1 152 ? 6.00788   4.36362   49.82583  1.000 33.20597 ? 152 VAL B N   1 
ATOM   3313 C  CA  . VAL B 1 152 ? 4.99684   3.43102   50.30437  1.000 34.97136 ? 152 VAL B CA  1 
ATOM   3314 C  C   . VAL B 1 152 ? 3.63453   3.90734   49.84604  1.000 27.30806 ? 152 VAL B C   1 
ATOM   3315 O  O   . VAL B 1 152 ? 3.27533   5.07311   50.03909  1.000 28.75807 ? 152 VAL B O   1 
ATOM   3316 C  CB  . VAL B 1 152 ? 5.01321   3.28546   51.83773  1.000 38.67439 ? 152 VAL B CB  1 
ATOM   3317 C  CG1 . VAL B 1 152 ? 4.17293   2.08332   52.26578  1.000 27.71372 ? 152 VAL B CG1 1 
ATOM   3318 C  CG2 . VAL B 1 152 ? 6.42831   3.17443   52.34911  1.000 28.43114 ? 152 VAL B CG2 1 
ATOM   3319 N  N   . ILE B 1 153 ? 2.87644   2.99931   49.25810  1.000 24.91877 ? 153 ILE B N   1 
ATOM   3320 C  CA  . ILE B 1 153 ? 1.46884   3.21028   48.97256  1.000 27.96709 ? 153 ILE B CA  1 
ATOM   3321 C  C   . ILE B 1 153 ? 0.72608   2.30734   49.93890  1.000 31.84483 ? 153 ILE B C   1 
ATOM   3322 O  O   . ILE B 1 153 ? 0.98552   1.09494   49.98901  1.000 31.69270 ? 153 ILE B O   1 
ATOM   3323 C  CB  . ILE B 1 153 ? 1.13934   2.90590   47.50251  1.000 28.28460 ? 153 ILE B CB  1 
ATOM   3324 C  CG1 . ILE B 1 153 ? 1.84757   3.91466   46.62723  1.000 25.58275 ? 153 ILE B CG1 1 
ATOM   3325 C  CG2 . ILE B 1 153 ? -0.33973  3.01442   47.23953  1.000 31.27940 ? 153 ILE B CG2 1 
ATOM   3326 C  CD1 . ILE B 1 153 ? 1.45022   3.83814   45.14505  1.000 39.78890 ? 153 ILE B CD1 1 
ATOM   3327 N  N   . THR B 1 154 ? -0.13183  2.89982   50.76710  1.000 26.44217 ? 154 THR B N   1 
ATOM   3328 C  CA  . THR B 1 154 ? -0.87806  2.13398   51.74684  1.000 27.15888 ? 154 THR B CA  1 
ATOM   3329 C  C   . THR B 1 154 ? -2.36783  2.37756   51.53427  1.000 28.74401 ? 154 THR B C   1 
ATOM   3330 O  O   . THR B 1 154 ? -2.77784  3.48827   51.19188  1.000 31.10958 ? 154 THR B O   1 
ATOM   3331 C  CB  . THR B 1 154 ? -0.42238  2.50666   53.16126  1.000 29.00608 ? 154 THR B CB  1 
ATOM   3332 O  OG1 . THR B 1 154 ? -1.21761  1.80840   54.12042  1.000 31.41473 ? 154 THR B OG1 1 
ATOM   3333 C  CG2 . THR B 1 154 ? -0.56060  3.98763   53.37855  1.000 30.52233 ? 154 THR B CG2 1 
ATOM   3334 N  N   . ILE B 1 155 ? -3.17119  1.32511   51.66231  1.000 28.29329 ? 155 ILE B N   1 
ATOM   3335 C  CA  . ILE B 1 155 ? -4.60272  1.37871   51.35761  1.000 35.29745 ? 155 ILE B CA  1 
ATOM   3336 C  C   . ILE B 1 155 ? -5.39280  1.09877   52.62501  1.000 30.60509 ? 155 ILE B C   1 
ATOM   3337 O  O   . ILE B 1 155 ? -5.20517  0.04906   53.25177  1.000 35.52750 ? 155 ILE B O   1 
ATOM   3338 C  CB  . ILE B 1 155 ? -5.01351  0.35454   50.28514  1.000 28.90284 ? 155 ILE B CB  1 
ATOM   3339 C  CG1 . ILE B 1 155 ? -4.30394  0.59308   48.95953  1.000 32.07487 ? 155 ILE B CG1 1 
ATOM   3340 C  CG2 . ILE B 1 155 ? -6.53788  0.35503   50.10329  1.000 30.09169 ? 155 ILE B CG2 1 
ATOM   3341 C  CD1 . ILE B 1 155 ? -4.39750  -0.63440  48.03341  1.000 26.80538 ? 155 ILE B CD1 1 
ATOM   3342 N  N   . GLU B 1 156 ? -6.31710  1.99908   52.95983  1.000 29.71530 ? 156 GLU B N   1 
ATOM   3343 C  CA  . GLU B 1 156 ? -7.24754  1.81320   54.06516  1.000 35.29308 ? 156 GLU B CA  1 
ATOM   3344 C  C   . GLU B 1 156 ? -8.67934  1.88312   53.54592  1.000 36.05694 ? 156 GLU B C   1 
ATOM   3345 O  O   . GLU B 1 156 ? -9.05850  2.85211   52.87842  1.000 37.42963 ? 156 GLU B O   1 
ATOM   3346 C  CB  . GLU B 1 156 ? -7.02862  2.86874   55.15569  1.000 29.88223 ? 156 GLU B CB  1 
ATOM   3347 C  CG  . GLU B 1 156 ? -7.98118  2.75476   56.34197  1.000 30.44917 ? 156 GLU B CG  1 
ATOM   3348 C  CD  . GLU B 1 156 ? -8.07877  1.34688   56.87744  1.000 35.76140 ? 156 GLU B CD  1 
ATOM   3349 O  OE1 . GLU B 1 156 ? -7.01827  0.73362   57.13734  1.000 38.53973 ? 156 GLU B OE1 1 
ATOM   3350 O  OE2 . GLU B 1 156 ? -9.21661  0.83542   57.01331  1.000 39.72757 ? 156 GLU B OE2 1 
ATOM   3351 N  N   . LYS B 1 157 ? -9.47585  0.85832   53.85755  1.000 30.26025 ? 157 LYS B N   1 
ATOM   3352 C  CA  . LYS B 1 157 ? -10.87552 0.86593   53.44494  1.000 37.92204 ? 157 LYS B CA  1 
ATOM   3353 C  C   . LYS B 1 157 ? -11.69945 1.86914   54.23498  1.000 44.80749 ? 157 LYS B C   1 
ATOM   3354 O  O   . LYS B 1 157 ? -12.55952 2.55422   53.66645  1.000 46.89805 ? 157 LYS B O   1 
ATOM   3355 C  CB  . LYS B 1 157 ? -11.48330 -0.52380  53.58226  1.000 42.22067 ? 157 LYS B CB  1 
ATOM   3356 C  CG  . LYS B 1 157 ? -12.92961 -0.58096  53.09637  1.000 49.91840 ? 157 LYS B CG  1 
ATOM   3357 C  CD  . LYS B 1 157 ? -13.18288 0.27026   51.84747  1.000 52.04020 ? 157 LYS B CD  1 
ATOM   3358 C  CE  . LYS B 1 157 ? -14.20314 -0.36965  50.93694  1.000 53.69581 ? 157 LYS B CE  1 
ATOM   3359 N  NZ  . LYS B 1 157 ? -14.90396 -1.47969  51.64052  1.000 55.29006 ? 157 LYS B NZ  1 
ATOM   3360 N  N   . ASP B 1 158 ? -11.46895 1.97036   55.53489  1.000 41.89917 ? 158 ASP B N   1 
ATOM   3361 C  CA  . ASP B 1 158 ? -12.38115 2.72560   56.38691  1.000 42.63647 ? 158 ASP B CA  1 
ATOM   3362 C  C   . ASP B 1 158 ? -11.90415 4.16475   56.51788  1.000 40.53408 ? 158 ASP B C   1 
ATOM   3363 O  O   . ASP B 1 158 ? -10.77373 4.39529   56.97366  1.000 41.59015 ? 158 ASP B O   1 
ATOM   3364 C  CB  . ASP B 1 158 ? -12.49855 2.07724   57.75715  1.000 39.02664 ? 158 ASP B CB  1 
ATOM   3365 C  CG  . ASP B 1 158 ? -13.59365 2.67714   58.58497  1.000 40.04092 ? 158 ASP B CG  1 
ATOM   3366 O  OD1 . ASP B 1 158 ? -13.99607 3.81651   58.28707  1.000 42.11742 ? 158 ASP B OD1 1 
ATOM   3367 O  OD2 . ASP B 1 158 ? -14.07131 2.01119   59.53215  1.000 45.80369 ? 158 ASP B OD2 1 
ATOM   3368 N  N   . PRO B 1 159 ? -12.71951 5.14910   56.13720  1.000 44.92879 ? 159 PRO B N   1 
ATOM   3369 C  CA  . PRO B 1 159 ? -12.32556 6.55153   56.33716  1.000 44.80030 ? 159 PRO B CA  1 
ATOM   3370 C  C   . PRO B 1 159 ? -12.09452 6.91597   57.79148  1.000 40.69338 ? 159 PRO B C   1 
ATOM   3371 O  O   . PRO B 1 159 ? -11.25655 7.78106   58.06702  1.000 43.76439 ? 159 PRO B O   1 
ATOM   3372 C  CB  . PRO B 1 159 ? -13.50491 7.33727   55.75007  1.000 45.16346 ? 159 PRO B CB  1 
ATOM   3373 C  CG  . PRO B 1 159 ? -14.27017 6.37647   54.93852  1.000 36.25655 ? 159 PRO B CG  1 
ATOM   3374 C  CD  . PRO B 1 159 ? -13.99484 5.00789   55.41897  1.000 44.49778 ? 159 PRO B CD  1 
ATOM   3375 N  N   . ASN B 1 160 ? -12.82405 6.30190   58.73097  1.000 43.22158 ? 160 ASN B N   1 
ATOM   3376 C  CA  . ASN B 1 160 ? -12.67252 6.63508   60.14933  1.000 41.77495 ? 160 ASN B CA  1 
ATOM   3377 C  C   . ASN B 1 160 ? -11.37939 6.09160   60.74413  1.000 39.07745 ? 160 ASN B C   1 
ATOM   3378 O  O   . ASN B 1 160 ? -10.93574 6.58788   61.78561  1.000 41.04321 ? 160 ASN B O   1 
ATOM   3379 C  CB  . ASN B 1 160 ? -13.85215 6.09596   60.96203  1.000 43.72456 ? 160 ASN B CB  1 
ATOM   3380 C  CG  . ASN B 1 160 ? -15.18131 6.54954   60.42365  1.000 44.47855 ? 160 ASN B CG  1 
ATOM   3381 O  OD1 . ASN B 1 160 ? -15.43829 7.74533   60.31458  1.000 52.96252 ? 160 ASN B OD1 1 
ATOM   3382 N  ND2 . ASN B 1 160 ? -16.03254 5.59444   60.06159  1.000 46.28708 ? 160 ASN B ND2 1 
ATOM   3383 N  N   . VAL B 1 161 ? -10.79625 5.05935   60.13449  1.000 35.10379 ? 161 VAL B N   1 
ATOM   3384 C  CA  . VAL B 1 161 ? -9.47739  4.59580   60.54918  1.000 41.72393 ? 161 VAL B CA  1 
ATOM   3385 C  C   . VAL B 1 161 ? -8.42111  5.59030   60.09412  1.000 37.00898 ? 161 VAL B C   1 
ATOM   3386 O  O   . VAL B 1 161 ? -7.39610  5.77816   60.75966  1.000 39.14283 ? 161 VAL B O   1 
ATOM   3387 C  CB  . VAL B 1 161 ? -9.22560  3.17498   59.99881  1.000 39.00713 ? 161 VAL B CB  1 
ATOM   3388 C  CG1 . VAL B 1 161 ? -7.77286  2.75156   60.19000  1.000 37.11377 ? 161 VAL B CG1 1 
ATOM   3389 C  CG2 . VAL B 1 161 ? -10.17390 2.16796   60.66519  1.000 37.00914 ? 161 VAL B CG2 1 
ATOM   3390 N  N   . ILE B 1 162 ? -8.67015  6.27483   58.97983  1.000 33.92315 ? 162 ILE B N   1 
ATOM   3391 C  CA  . ILE B 1 162 ? -7.73560  7.29150   58.52111  1.000 36.06966 ? 162 ILE B CA  1 
ATOM   3392 C  C   . ILE B 1 162 ? -7.79912  8.51929   59.41768  1.000 34.35978 ? 162 ILE B C   1 
ATOM   3393 O  O   . ILE B 1 162 ? -6.76975  9.13073   59.72391  1.000 34.42111 ? 162 ILE B O   1 
ATOM   3394 C  CB  . ILE B 1 162 ? -8.00664  7.64149   57.04724  1.000 37.52098 ? 162 ILE B CB  1 
ATOM   3395 C  CG1 . ILE B 1 162 ? -7.83073  6.39364   56.17293  1.000 36.99206 ? 162 ILE B CG1 1 
ATOM   3396 C  CG2 . ILE B 1 162 ? -7.04959  8.74495   56.56520  1.000 36.14852 ? 162 ILE B CG2 1 
ATOM   3397 C  CD1 . ILE B 1 162 ? -7.73209  6.69418   54.68574  1.000 34.68935 ? 162 ILE B CD1 1 
ATOM   3398 N  N   . GLU B 1 163 ? -8.99659  8.89569   59.86534  1.000 32.48151 ? 163 GLU B N   1 
ATOM   3399 C  CA  . GLU B 1 163 ? -9.10201  10.04112  60.76866  1.000 38.83772 ? 163 GLU B CA  1 
ATOM   3400 C  C   . GLU B 1 163 ? -8.48932  9.74245   62.13788  1.000 33.58156 ? 163 GLU B C   1 
ATOM   3401 O  O   . GLU B 1 163 ? -7.86140  10.62012  62.74171  1.000 38.35632 ? 163 GLU B O   1 
ATOM   3402 C  CB  . GLU B 1 163 ? -10.55964 10.47947  60.91574  1.000 39.97746 ? 163 GLU B CB  1 
ATOM   3403 C  CG  . GLU B 1 163 ? -11.10337 11.21268  59.68055  1.000 47.64362 ? 163 GLU B CG  1 
ATOM   3404 C  CD  . GLU B 1 163 ? -10.06844 12.13047  59.02845  1.000 41.31964 ? 163 GLU B CD  1 
ATOM   3405 O  OE1 . GLU B 1 163 ? -9.85536  13.25506  59.52572  1.000 53.66277 ? 163 GLU B OE1 1 
ATOM   3406 O  OE2 . GLU B 1 163 ? -9.48707  11.74229  57.99923  1.000 47.21006 ? 163 GLU B OE2 1 
ATOM   3407 N  N   . ILE B 1 164 ? -8.65687  8.52004   62.65165  1.000 31.71447 ? 164 ILE B N   1 
ATOM   3408 C  CA  . ILE B 1 164 ? -7.99894  8.17363   63.90996  1.000 39.65757 ? 164 ILE B CA  1 
ATOM   3409 C  C   . ILE B 1 164 ? -6.48425  8.25481   63.75673  1.000 33.87788 ? 164 ILE B C   1 
ATOM   3410 O  O   . ILE B 1 164 ? -5.77721  8.70569   64.66559  1.000 39.51971 ? 164 ILE B O   1 
ATOM   3411 C  CB  . ILE B 1 164 ? -8.44653  6.78579   64.40174  1.000 32.16160 ? 164 ILE B CB  1 
ATOM   3412 C  CG1 . ILE B 1 164 ? -9.88716  6.83753   64.88234  1.000 43.95790 ? 164 ILE B CG1 1 
ATOM   3413 C  CG2 . ILE B 1 164 ? -7.54928  6.30439   65.55400  1.000 34.14615 ? 164 ILE B CG2 1 
ATOM   3414 C  CD1 . ILE B 1 164 ? -10.09397 7.71330   66.13732  1.000 33.89865 ? 164 ILE B CD1 1 
ATOM   3415 N  N   . ALA B 1 165 ? -5.96256  7.83357   62.60364  1.000 39.00054 ? 165 ALA B N   1 
ATOM   3416 C  CA  . ALA B 1 165 ? -4.52830  7.94529   62.35591  1.000 36.13074 ? 165 ALA B CA  1 
ATOM   3417 C  C   . ALA B 1 165 ? -4.07920  9.39919   62.29845  1.000 35.61332 ? 165 ALA B C   1 
ATOM   3418 O  O   . ALA B 1 165 ? -2.95406  9.71612   62.70271  1.000 41.83656 ? 165 ALA B O   1 
ATOM   3419 C  CB  . ALA B 1 165 ? -4.15632  7.23000   61.05718  1.000 34.56664 ? 165 ALA B CB  1 
ATOM   3420 N  N   . ARG B 1 166 ? -4.93724  10.29241  61.80580  1.000 35.39070 ? 166 ARG B N   1 
ATOM   3421 C  CA  . ARG B 1 166 ? -4.57144  11.70040  61.73476  1.000 40.60911 ? 166 ARG B CA  1 
ATOM   3422 C  C   . ARG B 1 166 ? -4.25858  12.27179  63.09959  1.000 39.76704 ? 166 ARG B C   1 
ATOM   3423 O  O   . ARG B 1 166 ? -3.40980  13.15853  63.22337  1.000 44.74410 ? 166 ARG B O   1 
ATOM   3424 C  CB  . ARG B 1 166 ? -5.68216  12.51548  61.08320  1.000 39.82157 ? 166 ARG B CB  1 
ATOM   3425 C  CG  . ARG B 1 166 ? -5.39919  12.72893  59.63217  1.000 39.51425 ? 166 ARG B CG  1 
ATOM   3426 C  CD  . ARG B 1 166 ? -6.27308  13.77119  58.98381  1.000 39.60449 ? 166 ARG B CD  1 
ATOM   3427 N  NE  . ARG B 1 166 ? -6.75771  13.21405  57.72741  1.000 48.23666 ? 166 ARG B NE  1 
ATOM   3428 C  CZ  . ARG B 1 166 ? -6.03493  13.15824  56.61770  1.000 51.15081 ? 166 ARG B CZ  1 
ATOM   3429 N  NH1 . ARG B 1 166 ? -4.77788  13.58495  56.58954  1.000 39.11419 ? 166 ARG B NH1 1 
ATOM   3430 N  NH2 . ARG B 1 166 ? -6.57939  12.64842  55.51190  1.000 61.84580 ? 166 ARG B NH2 1 
ATOM   3431 N  N   . ILE B 1 167 ? -4.92654  11.78945  64.13977  1.000 38.70769 ? 167 ILE B N   1 
ATOM   3432 C  CA  . ILE B 1 167 ? -4.68014  12.32564  65.46248  1.000 39.33269 ? 167 ILE B CA  1 
ATOM   3433 C  C   . ILE B 1 167 ? -3.71240  11.45234  66.24772  1.000 38.30429 ? 167 ILE B C   1 
ATOM   3434 O  O   . ILE B 1 167 ? -3.30600  11.81800  67.35276  1.000 41.62710 ? 167 ILE B O   1 
ATOM   3435 C  CB  . ILE B 1 167 ? -6.01618  12.52260  66.20894  1.000 38.57845 ? 167 ILE B CB  1 
ATOM   3436 C  CG1 . ILE B 1 167 ? -5.83978  13.51513  67.35896  1.000 46.81623 ? 167 ILE B CG1 1 
ATOM   3437 C  CG2 . ILE B 1 167 ? -6.55773  11.19706  66.69086  1.000 34.17397 ? 167 ILE B CG2 1 
ATOM   3438 C  CD1 . ILE B 1 167 ? -5.01678  14.76592  66.94841  1.000 44.37813 ? 167 ILE B CD1 1 
ATOM   3439 N  N   . ASN B 1 168 ? -3.29919  10.32489  65.68741  1.000 37.89059 ? 168 ASN B N   1 
ATOM   3440 C  CA  . ASN B 1 168 ? -2.32339  9.46518   66.34167  1.000 32.34702 ? 168 ASN B CA  1 
ATOM   3441 C  C   . ASN B 1 168 ? -0.92324  10.03684  66.14765  1.000 41.27851 ? 168 ASN B C   1 
ATOM   3442 O  O   . ASN B 1 168 ? -0.51075  10.26606  65.00240  1.000 40.07983 ? 168 ASN B O   1 
ATOM   3443 C  CB  . ASN B 1 168 ? -2.40777  8.06572   65.74957  1.000 33.18630 ? 168 ASN B CB  1 
ATOM   3444 C  CG  . ASN B 1 168 ? -1.48730  7.08798   66.43079  1.000 34.48101 ? 168 ASN B CG  1 
ATOM   3445 O  OD1 . ASN B 1 168 ? -1.02301  7.32461   67.54635  1.000 31.01517 ? 168 ASN B OD1 1 
ATOM   3446 N  ND2 . ASN B 1 168 ? -1.20718  5.98056   65.75784  1.000 32.36599 ? 168 ASN B ND2 1 
ATOM   3447 N  N   . PRO B 1 169 ? -0.16754  10.29551  67.21228  1.000 37.26711 ? 169 PRO B N   1 
ATOM   3448 C  CA  . PRO B 1 169 ? 1.21865   10.74983  67.01095  1.000 35.27871 ? 169 PRO B CA  1 
ATOM   3449 C  C   . PRO B 1 169 ? 2.14296   9.66179   66.48357  1.000 42.24254 ? 169 PRO B C   1 
ATOM   3450 O  O   . PRO B 1 169 ? 3.15174   9.98852   65.85008  1.000 37.89812 ? 169 PRO B O   1 
ATOM   3451 C  CB  . PRO B 1 169 ? 1.64450   11.23178  68.39720  1.000 34.35981 ? 169 PRO B CB  1 
ATOM   3452 C  CG  . PRO B 1 169 ? 0.69952   10.57495  69.35913  1.000 38.63045 ? 169 PRO B CG  1 
ATOM   3453 C  CD  . PRO B 1 169 ? -0.53130  10.16034  68.63465  1.000 37.38475 ? 169 PRO B CD  1 
ATOM   3454 N  N   . TRP B 1 170 ? 1.83115   8.38216   66.68882  1.000 41.65493 ? 170 TRP B N   1 
ATOM   3455 C  CA  . TRP B 1 170 ? 2.65267   7.33898   66.09169  1.000 33.63391 ? 170 TRP B CA  1 
ATOM   3456 C  C   . TRP B 1 170 ? 2.35258   7.12095   64.61645  1.000 35.15886 ? 170 TRP B C   1 
ATOM   3457 O  O   . TRP B 1 170 ? 3.02871   6.30094   63.98258  1.000 31.55035 ? 170 TRP B O   1 
ATOM   3458 C  CB  . TRP B 1 170 ? 2.49294   6.02025   66.85598  1.000 35.67446 ? 170 TRP B CB  1 
ATOM   3459 C  CG  . TRP B 1 170 ? 2.99614   6.07818   68.25685  1.000 41.43331 ? 170 TRP B CG  1 
ATOM   3460 C  CD1 . TRP B 1 170 ? 2.39979   6.68506   69.30451  1.000 35.30187 ? 170 TRP B CD1 1 
ATOM   3461 C  CD2 . TRP B 1 170 ? 4.20639   5.50288   68.76199  1.000 46.31230 ? 170 TRP B CD2 1 
ATOM   3462 N  NE1 . TRP B 1 170 ? 3.14746   6.52128   70.43870  1.000 45.21859 ? 170 TRP B NE1 1 
ATOM   3463 C  CE2 . TRP B 1 170 ? 4.26907   5.80387   70.13039  1.000 43.72626 ? 170 TRP B CE2 1 
ATOM   3464 C  CE3 . TRP B 1 170 ? 5.24235   4.76543   68.18800  1.000 48.22305 ? 170 TRP B CE3 1 
ATOM   3465 C  CZ2 . TRP B 1 170 ? 5.32181   5.39056   70.94105  1.000 53.08751 ? 170 TRP B CZ2 1 
ATOM   3466 C  CZ3 . TRP B 1 170 ? 6.29071   4.35991   68.99290  1.000 43.80457 ? 170 TRP B CZ3 1 
ATOM   3467 C  CH2 . TRP B 1 170 ? 6.32041   4.66978   70.35465  1.000 51.84909 ? 170 TRP B CH2 1 
ATOM   3468 N  N   . SER B 1 171 ? 1.38629   7.84125   64.04910  1.000 31.91098 ? 171 SER B N   1 
ATOM   3469 C  CA  . SER B 1 171 ? 1.01169   7.68253   62.65021  1.000 38.04876 ? 171 SER B CA  1 
ATOM   3470 C  C   . SER B 1 171 ? 1.39268   8.88192   61.79706  1.000 35.58478 ? 171 SER B C   1 
ATOM   3471 O  O   . SER B 1 171 ? 1.03919   8.92404   60.61715  1.000 37.33550 ? 171 SER B O   1 
ATOM   3472 C  CB  . SER B 1 171 ? -0.48956  7.43040   62.53144  1.000 35.85592 ? 171 SER B CB  1 
ATOM   3473 O  OG  . SER B 1 171 ? -0.81111  6.13058   62.97740  1.000 30.56507 ? 171 SER B OG  1 
ATOM   3474 N  N   . ARG B 1 172 ? 2.13474   9.83265   62.36122  1.000 32.51880 ? 172 ARG B N   1 
ATOM   3475 C  CA  . ARG B 1 172 ? 2.34179   11.13091  61.73074  1.000 32.80180 ? 172 ARG B CA  1 
ATOM   3476 C  C   . ARG B 1 172 ? 2.92997   11.03187  60.33086  1.000 39.25523 ? 172 ARG B C   1 
ATOM   3477 O  O   . ARG B 1 172 ? 2.54639   11.79381  59.43559  1.000 41.93356 ? 172 ARG B O   1 
ATOM   3478 C  CB  . ARG B 1 172 ? 3.24421   11.97917  62.61748  1.000 29.80013 ? 172 ARG B CB  1 
ATOM   3479 C  CG  . ARG B 1 172 ? 2.45915   12.64900  63.71965  1.000 36.89421 ? 172 ARG B CG  1 
ATOM   3480 C  CD  . ARG B 1 172 ? 3.17061   13.85151  64.28956  1.000 35.88314 ? 172 ARG B CD  1 
ATOM   3481 N  NE  . ARG B 1 172 ? 2.47324   14.33782  65.47395  1.000 44.14883 ? 172 ARG B NE  1 
ATOM   3482 C  CZ  . ARG B 1 172 ? 3.06051   14.57952  66.63933  1.000 45.15371 ? 172 ARG B CZ  1 
ATOM   3483 N  NH1 . ARG B 1 172 ? 4.36349   14.40188  66.80728  1.000 41.14239 ? 172 ARG B NH1 1 
ATOM   3484 N  NH2 . ARG B 1 172 ? 2.31959   14.99632  67.66526  1.000 46.47052 ? 172 ARG B NH2 1 
ATOM   3485 N  N   . GLU B 1 173 ? 3.87653   10.12571  60.11539  1.000 34.65666 ? 173 GLU B N   1 
ATOM   3486 C  CA  . GLU B 1 173 ? 4.50050   10.15528  58.79810  1.000 41.65074 ? 173 GLU B CA  1 
ATOM   3487 C  C   . GLU B 1 173 ? 3.56391   9.70120   57.68217  1.000 38.81244 ? 173 GLU B C   1 
ATOM   3488 O  O   . GLU B 1 173 ? 3.95892   9.75652   56.51661  1.000 36.05371 ? 173 GLU B O   1 
ATOM   3489 C  CB  . GLU B 1 173 ? 5.76372   9.30323   58.78642  1.000 38.60773 ? 173 GLU B CB  1 
ATOM   3490 C  CG  . GLU B 1 173 ? 6.79519   9.64209   59.84515  1.000 40.13034 ? 173 GLU B CG  1 
ATOM   3491 C  CD  . GLU B 1 173 ? 6.59393   8.84180   61.12097  1.000 48.43029 ? 173 GLU B CD  1 
ATOM   3492 O  OE1 . GLU B 1 173 ? 5.42301   8.53538   61.44222  1.000 47.03364 ? 173 GLU B OE1 1 
ATOM   3493 O  OE2 . GLU B 1 173 ? 7.60021   8.52507   61.80175  1.000 47.23699 ? 173 GLU B OE2 1 
ATOM   3494 N  N   . LEU B 1 174 ? 2.34102   9.25743   57.98605  1.000 34.27915 ? 174 LEU B N   1 
ATOM   3495 C  CA  . LEU B 1 174 ? 1.39492   8.97096   56.91075  1.000 36.32919 ? 174 LEU B CA  1 
ATOM   3496 C  C   . LEU B 1 174 ? 0.96750   10.22601  56.16467  1.000 34.24606 ? 174 LEU B C   1 
ATOM   3497 O  O   . LEU B 1 174 ? 0.54800   10.12557  55.00296  1.000 36.34829 ? 174 LEU B O   1 
ATOM   3498 C  CB  . LEU B 1 174 ? 0.13289   8.28202   57.45553  1.000 39.01848 ? 174 LEU B CB  1 
ATOM   3499 C  CG  . LEU B 1 174 ? 0.32222   6.90753   58.08596  1.000 37.61213 ? 174 LEU B CG  1 
ATOM   3500 C  CD1 . LEU B 1 174 ? -0.98223  6.42172   58.66235  1.000 33.46647 ? 174 LEU B CD1 1 
ATOM   3501 C  CD2 . LEU B 1 174 ? 0.83861   5.95674   57.02613  1.000 34.99047 ? 174 LEU B CD2 1 
ATOM   3502 N  N   . PHE B 1 175 ? 1.03766   11.39495  56.81031  1.000 38.96919 ? 175 PHE B N   1 
ATOM   3503 C  CA  . PHE B 1 175 ? 0.36570   12.59762  56.32358  1.000 41.75681 ? 175 PHE B CA  1 
ATOM   3504 C  C   . PHE B 1 175 ? 1.31458   13.75189  56.04175  1.000 38.46018 ? 175 PHE B C   1 
ATOM   3505 O  O   . PHE B 1 175 ? 0.85871   14.85469  55.72988  1.000 44.02786 ? 175 PHE B O   1 
ATOM   3506 C  CB  . PHE B 1 175 ? -0.70551  13.03264  57.32623  1.000 35.37800 ? 175 PHE B CB  1 
ATOM   3507 C  CG  . PHE B 1 175 ? -1.56507  11.90166  57.80654  1.000 39.35011 ? 175 PHE B CG  1 
ATOM   3508 C  CD1 . PHE B 1 175 ? -2.47696  11.30548  56.94742  1.000 38.23243 ? 175 PHE B CD1 1 
ATOM   3509 C  CD2 . PHE B 1 175 ? -1.45468  11.42337  59.10876  1.000 35.23645 ? 175 PHE B CD2 1 
ATOM   3510 C  CE1 . PHE B 1 175 ? -3.27393  10.25720  57.36813  1.000 35.48869 ? 175 PHE B CE1 1 
ATOM   3511 C  CE2 . PHE B 1 175 ? -2.24494  10.36069  59.53851  1.000 34.73382 ? 175 PHE B CE2 1 
ATOM   3512 C  CZ  . PHE B 1 175 ? -3.16051  9.78584   58.66791  1.000 35.69033 ? 175 PHE B CZ  1 
ATOM   3513 N  N   . THR B 1 176 ? 2.61733   13.53324  56.13024  1.000 41.53623 ? 176 THR B N   1 
ATOM   3514 C  CA  . THR B 1 176 ? 3.56872   14.57713  55.80681  1.000 47.60607 ? 176 THR B CA  1 
ATOM   3515 C  C   . THR B 1 176 ? 4.86138   13.89026  55.40720  1.000 50.97741 ? 176 THR B C   1 
ATOM   3516 O  O   . THR B 1 176 ? 5.20935   12.85290  55.97242  1.000 47.53957 ? 176 THR B O   1 
ATOM   3517 C  CB  . THR B 1 176 ? 3.77350   15.52897  56.99607  1.000 51.88086 ? 176 THR B CB  1 
ATOM   3518 O  OG1 . THR B 1 176 ? 4.90448   16.38194  56.76472  1.000 55.06038 ? 176 THR B OG1 1 
ATOM   3519 C  CG2 . THR B 1 176 ? 3.98030   14.74558  58.28116  1.000 48.27856 ? 176 THR B CG2 1 
ATOM   3520 N  N   . GLY B 1 177 ? 5.54495   14.43980  54.40596  1.000 50.12884 ? 177 GLY B N   1 
ATOM   3521 C  CA  . GLY B 1 177 ? 6.82984   13.92943  53.97552  1.000 57.90923 ? 177 GLY B CA  1 
ATOM   3522 C  C   . GLY B 1 177 ? 6.85262   13.34933  52.57604  1.000 64.47723 ? 177 GLY B C   1 
ATOM   3523 O  O   . GLY B 1 177 ? 7.93498   13.25458  51.98296  1.000 70.72519 ? 177 GLY B O   1 
ATOM   3524 N  N   . GLY B 1 178 ? 5.70580   12.93920  52.03641  1.000 54.54341 ? 178 GLY B N   1 
ATOM   3525 C  CA  . GLY B 1 178 ? 5.64005   12.50884  50.65534  1.000 55.13799 ? 178 GLY B CA  1 
ATOM   3526 C  C   . GLY B 1 178 ? 6.18017   11.12633  50.36374  1.000 53.93915 ? 178 GLY B C   1 
ATOM   3527 O  O   . GLY B 1 178 ? 6.14459   10.70412  49.20304  1.000 52.54484 ? 178 GLY B O   1 
ATOM   3528 N  N   . LYS B 1 179 ? 6.69543   10.41438  51.36383  1.000 50.37633 ? 179 LYS B N   1 
ATOM   3529 C  CA  . LYS B 1 179 ? 7.09098   9.02626   51.17461  1.000 43.94639 ? 179 LYS B CA  1 
ATOM   3530 C  C   . LYS B 1 179 ? 5.92092   8.06008   51.23726  1.000 39.39752 ? 179 LYS B C   1 
ATOM   3531 O  O   . LYS B 1 179 ? 6.04113   6.94633   50.72147  1.000 39.95065 ? 179 LYS B O   1 
ATOM   3532 C  CB  . LYS B 1 179 ? 8.12038   8.59631   52.22570  1.000 43.54700 ? 179 LYS B CB  1 
ATOM   3533 C  CG  . LYS B 1 179 ? 9.48533   9.25168   52.15614  1.000 47.79593 ? 179 LYS B CG  1 
ATOM   3534 C  CD  . LYS B 1 179 ? 10.55893  8.21076   52.56327  1.000 50.43211 ? 179 LYS B CD  1 
ATOM   3535 C  CE  . LYS B 1 179 ? 11.89641  8.83333   53.01551  1.000 64.99469 ? 179 LYS B CE  1 
ATOM   3536 N  NZ  . LYS B 1 179 ? 11.95408  10.33592  52.98261  1.000 57.35102 ? 179 LYS B NZ  1 
ATOM   3537 N  N   . ILE B 1 180 ? 4.81157   8.43324   51.87661  1.000 45.41940 ? 180 ILE B N   1 
ATOM   3538 C  CA  . ILE B 1 180 ? 3.68688   7.52413   52.08955  1.000 40.44763 ? 180 ILE B CA  1 
ATOM   3539 C  C   . ILE B 1 180 ? 2.46709   8.05262   51.35639  1.000 37.18045 ? 180 ILE B C   1 
ATOM   3540 O  O   . ILE B 1 180 ? 2.00981   9.17013   51.62078  1.000 34.97754 ? 180 ILE B O   1 
ATOM   3541 C  CB  . ILE B 1 180 ? 3.35306   7.33943   53.57360  1.000 36.95510 ? 180 ILE B CB  1 
ATOM   3542 C  CG1 . ILE B 1 180 ? 4.61987   7.19570   54.38425  1.000 39.38992 ? 180 ILE B CG1 1 
ATOM   3543 C  CG2 . ILE B 1 180 ? 2.47813   6.10346   53.75724  1.000 33.03447 ? 180 ILE B CG2 1 
ATOM   3544 C  CD1 . ILE B 1 180 ? 5.17275   5.86458   54.25310  1.000 40.08307 ? 180 ILE B CD1 1 
ATOM   3545 N  N   . GLN B 1 181 ? 1.90246   7.22582   50.49090  1.000 33.35117 ? 181 GLN B N   1 
ATOM   3546 C  CA  . GLN B 1 181 ? 0.68393   7.56092   49.77646  1.000 31.10281 ? 181 GLN B CA  1 
ATOM   3547 C  C   . GLN B 1 181 ? -0.45973  6.78021   50.39508  1.000 32.07083 ? 181 GLN B C   1 
ATOM   3548 O  O   . GLN B 1 181 ? -0.38889  5.54853   50.51860  1.000 36.97249 ? 181 GLN B O   1 
ATOM   3549 C  CB  . GLN B 1 181 ? 0.83337   7.23746   48.28778  1.000 36.51997 ? 181 GLN B CB  1 
ATOM   3550 C  CG  . GLN B 1 181 ? -0.23852  7.81060   47.41568  1.000 36.51614 ? 181 GLN B CG  1 
ATOM   3551 C  CD  . GLN B 1 181 ? -0.04446  7.43047   45.97592  1.000 40.34924 ? 181 GLN B CD  1 
ATOM   3552 O  OE1 . GLN B 1 181 ? 1.09169   7.29299   45.51248  1.000 42.36307 ? 181 GLN B OE1 1 
ATOM   3553 N  NE2 . GLN B 1 181 ? -1.14820  7.24214   45.25251  1.000 35.68584 ? 181 GLN B NE2 1 
ATOM   3554 N  N   . VAL B 1 182 ? -1.48557  7.49854   50.82631  1.000 32.55271 ? 182 VAL B N   1 
ATOM   3555 C  CA  . VAL B 1 182 ? -2.65239  6.90594   51.46189  1.000 34.12338 ? 182 VAL B CA  1 
ATOM   3556 C  C   . VAL B 1 182 ? -3.76373  6.84116   50.43589  1.000 34.27061 ? 182 VAL B C   1 
ATOM   3557 O  O   . VAL B 1 182 ? -4.22226  7.87679   49.94455  1.000 31.60580 ? 182 VAL B O   1 
ATOM   3558 C  CB  . VAL B 1 182 ? -3.10232  7.70993   52.68789  1.000 27.43265 ? 182 VAL B CB  1 
ATOM   3559 C  CG1 . VAL B 1 182 ? -4.27161  7.01836   53.33166  1.000 31.90593 ? 182 VAL B CG1 1 
ATOM   3560 C  CG2 . VAL B 1 182 ? -1.96683  7.82848   53.66200  1.000 33.19427 ? 182 VAL B CG2 1 
ATOM   3561 N  N   . ILE B 1 183 ? -4.20023  5.63239   50.10882  1.000 34.68983 ? 183 ILE B N   1 
ATOM   3562 C  CA  . ILE B 1 183 ? -5.37224  5.43979   49.27377  1.000 38.84650 ? 183 ILE B CA  1 
ATOM   3563 C  C   . ILE B 1 183 ? -6.48093  4.93302   50.18019  1.000 34.70492 ? 183 ILE B C   1 
ATOM   3564 O  O   . ILE B 1 183 ? -6.25848  4.02897   50.99289  1.000 39.70420 ? 183 ILE B O   1 
ATOM   3565 C  CB  . ILE B 1 183 ? -5.11928  4.46027   48.11361  1.000 30.76139 ? 183 ILE B CB  1 
ATOM   3566 C  CG1 . ILE B 1 183 ? -4.31507  5.10258   46.99507  1.000 37.32239 ? 183 ILE B CG1 1 
ATOM   3567 C  CG2 . ILE B 1 183 ? -6.43881  4.03724   47.49734  1.000 34.20913 ? 183 ILE B CG2 1 
ATOM   3568 C  CD1 . ILE B 1 183 ? -2.90089  5.40136   47.32224  1.000 39.42315 ? 183 ILE B CD1 1 
ATOM   3569 N  N   . GLN B 1 184 ? -7.66024  5.52164   50.05607  1.000 31.29900 ? 184 GLN B N   1 
ATOM   3570 C  CA  . GLN B 1 184 ? -8.86494  4.99355   50.67441  1.000 34.91161 ? 184 GLN B CA  1 
ATOM   3571 C  C   . GLN B 1 184 ? -9.67457  4.21930   49.63910  1.000 35.04262 ? 184 GLN B C   1 
ATOM   3572 O  O   . GLN B 1 184 ? -10.10371 4.79446   48.63375  1.000 42.37226 ? 184 GLN B O   1 
ATOM   3573 C  CB  . GLN B 1 184 ? -9.69498  6.13080   51.26198  1.000 39.20941 ? 184 GLN B CB  1 
ATOM   3574 C  CG  . GLN B 1 184 ? -10.83810 5.64721   52.10609  1.000 41.37139 ? 184 GLN B CG  1 
ATOM   3575 C  CD  . GLN B 1 184 ? -11.99956 6.58683   52.06607  1.000 49.71764 ? 184 GLN B CD  1 
ATOM   3576 O  OE1 . GLN B 1 184 ? -13.15472 6.16125   51.96705  1.000 55.34167 ? 184 GLN B OE1 1 
ATOM   3577 N  NE2 . GLN B 1 184 ? -11.71208 7.88545   52.17682  1.000 48.57283 ? 184 GLN B NE2 1 
ATOM   3578 N  N   . GLY B 1 185 ? -9.88693  2.92961   49.88197  1.000 33.94352 ? 185 GLY B N   1 
ATOM   3579 C  CA  . GLY B 1 185 ? -10.76052 2.15201   49.02349  1.000 40.64973 ? 185 GLY B CA  1 
ATOM   3580 C  C   . GLY B 1 185 ? -10.64524 0.66480   49.30854  1.000 41.82323 ? 185 GLY B C   1 
ATOM   3581 O  O   . GLY B 1 185 ? -9.97981  0.24378   50.26320  1.000 43.33388 ? 185 GLY B O   1 
ATOM   3582 N  N   . ASP B 1 186 ? -11.36329 -0.11837  48.49469  1.000 36.37600 ? 186 ASP B N   1 
ATOM   3583 C  CA  . ASP B 1 186 ? -11.14526 -1.55806  48.42587  1.000 42.01548 ? 186 ASP B CA  1 
ATOM   3584 C  C   . ASP B 1 186 ? -9.75058  -1.86709  47.93988  1.000 41.51745 ? 186 ASP B C   1 
ATOM   3585 O  O   . ASP B 1 186 ? -9.39901  -1.54957  46.79687  1.000 48.17711 ? 186 ASP B O   1 
ATOM   3586 C  CB  . ASP B 1 186 ? -12.15011 -2.23756  47.49255  1.000 46.14865 ? 186 ASP B CB  1 
ATOM   3587 C  CG  . ASP B 1 186 ? -13.19610 -3.03783  48.22930  1.000 51.16292 ? 186 ASP B CG  1 
ATOM   3588 O  OD1 . ASP B 1 186 ? -13.70176 -4.02832  47.64917  1.000 59.25888 ? 186 ASP B OD1 1 
ATOM   3589 O  OD2 . ASP B 1 186 ? -13.47448 -2.72830  49.39708  1.000 58.10147 ? 186 ASP B OD2 1 
ATOM   3590 N  N   . ALA B 1 187 ? -8.96899  -2.50924  48.80482  1.000 39.72179 ? 187 ALA B N   1 
ATOM   3591 C  CA  . ALA B 1 187 ? -7.74951  -3.15723  48.35253  1.000 41.26070 ? 187 ALA B CA  1 
ATOM   3592 C  C   . ALA B 1 187 ? -8.01783  -3.97967  47.09818  1.000 45.18943 ? 187 ALA B C   1 
ATOM   3593 O  O   . ALA B 1 187 ? -7.32742  -3.83092  46.08768  1.000 40.41359 ? 187 ALA B O   1 
ATOM   3594 C  CB  . ALA B 1 187 ? -7.18891  -4.03599  49.46984  1.000 39.40144 ? 187 ALA B CB  1 
ATOM   3595 N  N   . PHE B 1 188 ? -9.05672  -4.82293  47.13706  1.000 44.38506 ? 188 PHE B N   1 
ATOM   3596 C  CA  . PHE B 1 188 ? -9.37298  -5.69367  46.00736  1.000 39.38393 ? 188 PHE B CA  1 
ATOM   3597 C  C   . PHE B 1 188 ? -9.60992  -4.90796  44.72312  1.000 44.23926 ? 188 PHE B C   1 
ATOM   3598 O  O   . PHE B 1 188 ? -9.28414  -5.38935  43.63178  1.000 51.48641 ? 188 PHE B O   1 
ATOM   3599 C  CB  . PHE B 1 188 ? -10.59672 -6.54057  46.35153  1.000 43.47195 ? 188 PHE B CB  1 
ATOM   3600 C  CG  . PHE B 1 188 ? -10.92555 -7.61183  45.34618  1.000 45.87065 ? 188 PHE B CG  1 
ATOM   3601 C  CD1 . PHE B 1 188 ? -11.71519 -7.33340  44.24066  1.000 43.77951 ? 188 PHE B CD1 1 
ATOM   3602 C  CD2 . PHE B 1 188 ? -10.48465 -8.91563  45.53337  1.000 46.40614 ? 188 PHE B CD2 1 
ATOM   3603 C  CE1 . PHE B 1 188 ? -12.03914 -8.33444  43.32921  1.000 45.45714 ? 188 PHE B CE1 1 
ATOM   3604 C  CE2 . PHE B 1 188 ? -10.81024 -9.91478  44.62706  1.000 50.69161 ? 188 PHE B CE2 1 
ATOM   3605 C  CZ  . PHE B 1 188 ? -11.58748 -9.61623  43.52386  1.000 41.65557 ? 188 PHE B CZ  1 
ATOM   3606 N  N   . GLU B 1 189 ? -10.16727 -3.70923  44.81829  1.000 42.80120 ? 189 GLU B N   1 
ATOM   3607 C  CA  . GLU B 1 189 ? -10.46539 -2.97797  43.59719  1.000 43.02020 ? 189 GLU B CA  1 
ATOM   3608 C  C   . GLU B 1 189 ? -9.31706  -2.06781  43.18807  1.000 43.20837 ? 189 GLU B C   1 
ATOM   3609 O  O   . GLU B 1 189 ? -9.02950  -1.94198  41.99557  1.000 44.74160 ? 189 GLU B O   1 
ATOM   3610 C  CB  . GLU B 1 189 ? -11.75589 -2.17185  43.76995  1.000 46.41398 ? 189 GLU B CB  1 
ATOM   3611 C  CG  . GLU B 1 189 ? -13.01065 -3.02184  43.62589  1.000 48.25952 ? 189 GLU B CG  1 
ATOM   3612 C  CD  . GLU B 1 189 ? -13.23993 -3.48044  42.19498  1.000 57.30334 ? 189 GLU B CD  1 
ATOM   3613 O  OE1 . GLU B 1 189 ? -13.17076 -2.61881  41.28941  1.000 61.60937 ? 189 GLU B OE1 1 
ATOM   3614 O  OE2 . GLU B 1 189 ? -13.47501 -4.69617  41.97156  1.000 49.82981 ? 189 GLU B OE2 1 
ATOM   3615 N  N   . VAL B 1 190 ? -8.64013  -1.44338  44.15640  1.000 47.46483 ? 190 VAL B N   1 
ATOM   3616 C  CA  . VAL B 1 190 ? -7.56992  -0.50285  43.82775  1.000 41.00599 ? 190 VAL B CA  1 
ATOM   3617 C  C   . VAL B 1 190 ? -6.43401  -1.21202  43.10029  1.000 39.30958 ? 190 VAL B C   1 
ATOM   3618 O  O   . VAL B 1 190 ? -5.89041  -0.69263  42.11841  1.000 44.06910 ? 190 VAL B O   1 
ATOM   3619 C  CB  . VAL B 1 190 ? -7.08332  0.21693   45.10123  1.000 40.96471 ? 190 VAL B CB  1 
ATOM   3620 C  CG1 . VAL B 1 190 ? -5.82362  1.01023   44.81353  1.000 41.36168 ? 190 VAL B CG1 1 
ATOM   3621 C  CG2 . VAL B 1 190 ? -8.17725  1.14815   45.62814  1.000 37.33899 ? 190 VAL B CG2 1 
ATOM   3622 N  N   . VAL B 1 191 ? -6.07143  -2.42027  43.54323  1.000 42.81097 ? 191 VAL B N   1 
ATOM   3623 C  CA  . VAL B 1 191 ? -4.98268  -3.13373  42.87808  1.000 39.95448 ? 191 VAL B CA  1 
ATOM   3624 C  C   . VAL B 1 191 ? -5.31499  -3.47152  41.43904  1.000 35.43033 ? 191 VAL B C   1 
ATOM   3625 O  O   . VAL B 1 191 ? -4.40193  -3.65741  40.62849  1.000 40.02453 ? 191 VAL B O   1 
ATOM   3626 C  CB  . VAL B 1 191 ? -4.55671  -4.40681  43.65418  1.000 39.01052 ? 191 VAL B CB  1 
ATOM   3627 C  CG1 . VAL B 1 191 ? -4.45476  -4.12974  45.14457  1.000 44.11239 ? 191 VAL B CG1 1 
ATOM   3628 C  CG2 . VAL B 1 191 ? -5.54750  -5.53001  43.41946  1.000 36.47841 ? 191 VAL B CG2 1 
ATOM   3629 N  N   . LYS B 1 192 ? -6.59811  -3.53505  41.08036  1.000 39.47803 ? 192 LYS B N   1 
ATOM   3630 C  CA  . LYS B 1 192 ? -6.93099  -3.73437  39.67659  1.000 44.57511 ? 192 LYS B CA  1 
ATOM   3631 C  C   . LYS B 1 192 ? -6.57174  -2.52954  38.82291  1.000 42.86187 ? 192 LYS B C   1 
ATOM   3632 O  O   . LYS B 1 192 ? -6.38200  -2.67846  37.61036  1.000 47.33135 ? 192 LYS B O   1 
ATOM   3633 C  CB  . LYS B 1 192 ? -8.41522  -4.05699  39.51153  1.000 42.82289 ? 192 LYS B CB  1 
ATOM   3634 C  CG  . LYS B 1 192 ? -8.77834  -5.47480  39.90443  1.000 38.35032 ? 192 LYS B CG  1 
ATOM   3635 C  CD  . LYS B 1 192 ? -10.24673 -5.75313  39.63147  1.000 44.26864 ? 192 LYS B CD  1 
ATOM   3636 C  CE  . LYS B 1 192 ? -10.81486 -6.67483  40.69867  1.000 48.65295 ? 192 LYS B CE  1 
ATOM   3637 N  NZ  . LYS B 1 192 ? -10.38644 -8.09822  40.49972  1.000 42.04236 ? 192 LYS B NZ  1 
ATOM   3638 N  N   . LYS B 1 193 ? -6.47555  -1.34621  39.41666  1.000 43.03329 ? 193 LYS B N   1 
ATOM   3639 C  CA  . LYS B 1 193 ? -6.16541  -0.15284  38.64373  1.000 45.56436 ? 193 LYS B CA  1 
ATOM   3640 C  C   . LYS B 1 193 ? -4.66861  0.13827   38.56028  1.000 44.57140 ? 193 LYS B C   1 
ATOM   3641 O  O   . LYS B 1 193 ? -4.25382  0.90070   37.68187  1.000 55.03359 ? 193 LYS B O   1 
ATOM   3642 C  CB  . LYS B 1 193 ? -6.91565  1.05395   39.22574  1.000 43.43159 ? 193 LYS B CB  1 
ATOM   3643 C  CG  . LYS B 1 193 ? -8.38908  1.10759   38.77836  1.000 52.71106 ? 193 LYS B CG  1 
ATOM   3644 C  CD  . LYS B 1 193 ? -9.14380  2.34995   39.26791  1.000 58.60542 ? 193 LYS B CD  1 
ATOM   3645 C  CE  . LYS B 1 193 ? -8.47835  3.64693   38.82038  1.000 65.69537 ? 193 LYS B CE  1 
ATOM   3646 N  NZ  . LYS B 1 193 ? -8.33634  4.61984   39.94163  1.000 57.07704 ? 193 LYS B NZ  1 
ATOM   3647 N  N   . PHE B 1 194 ? -3.84801  -0.46325  39.41744  1.000 40.18963 ? 194 PHE B N   1 
ATOM   3648 C  CA  . PHE B 1 194 ? -2.41741  -0.20041  39.37374  1.000 37.73541 ? 194 PHE B CA  1 
ATOM   3649 C  C   . PHE B 1 194 ? -1.80751  -0.73096  38.08282  1.000 43.31432 ? 194 PHE B C   1 
ATOM   3650 O  O   . PHE B 1 194 ? -2.32118  -1.66114  37.45233  1.000 42.29386 ? 194 PHE B O   1 
ATOM   3651 C  CB  . PHE B 1 194 ? -1.69130  -0.86024  40.54157  1.000 41.00918 ? 194 PHE B CB  1 
ATOM   3652 C  CG  . PHE B 1 194 ? -1.96095  -0.23234  41.86162  1.000 33.06818 ? 194 PHE B CG  1 
ATOM   3653 C  CD1 . PHE B 1 194 ? -1.93827  1.14383   42.00650  1.000 38.72159 ? 194 PHE B CD1 1 
ATOM   3654 C  CD2 . PHE B 1 194 ? -2.18457  -1.02416  42.97899  1.000 36.03088 ? 194 PHE B CD2 1 
ATOM   3655 C  CE1 . PHE B 1 194 ? -2.17272  1.72583   43.23765  1.000 35.82152 ? 194 PHE B CE1 1 
ATOM   3656 C  CE2 . PHE B 1 194 ? -2.41842  -0.44734  44.21314  1.000 37.14262 ? 194 PHE B CE2 1 
ATOM   3657 C  CZ  . PHE B 1 194 ? -2.41170  0.93105   44.33888  1.000 40.84018 ? 194 PHE B CZ  1 
ATOM   3658 N  N   . LYS B 1 195 ? -0.67706  -0.14846  37.70225  1.000 37.68931 ? 195 LYS B N   1 
ATOM   3659 C  CA  . LYS B 1 195 ? -0.04778  -0.63912  36.49217  1.000 40.01655 ? 195 LYS B CA  1 
ATOM   3660 C  C   . LYS B 1 195 ? 0.70730   -1.92225  36.79160  1.000 44.25047 ? 195 LYS B C   1 
ATOM   3661 O  O   . LYS B 1 195 ? 1.03981   -2.22857  37.94174  1.000 33.28406 ? 195 LYS B O   1 
ATOM   3662 C  CB  . LYS B 1 195 ? 0.90033   0.40122   35.89559  1.000 40.64331 ? 195 LYS B CB  1 
ATOM   3663 C  CG  . LYS B 1 195 ? 0.39035   1.04747   34.61080  1.000 42.83419 ? 195 LYS B CG  1 
ATOM   3664 C  CD  . LYS B 1 195 ? -0.11703  2.44070   34.90461  1.000 41.01293 ? 195 LYS B CD  1 
ATOM   3665 C  CE  . LYS B 1 195 ? -0.88331  3.04400   33.73442  1.000 39.53060 ? 195 LYS B CE  1 
ATOM   3666 N  NZ  . LYS B 1 195 ? -1.87195  3.99830   34.31551  1.000 38.74452 ? 195 LYS B NZ  1 
ATOM   3667 N  N   . GLN B 1 196 ? 0.94262   -2.68347  35.72962  1.000 37.22425 ? 196 GLN B N   1 
ATOM   3668 C  CA  . GLN B 1 196 ? 1.83961   -3.82874  35.76898  1.000 41.09564 ? 196 GLN B CA  1 
ATOM   3669 C  C   . GLN B 1 196 ? 3.23995   -3.39779  36.19358  1.000 40.30140 ? 196 GLN B C   1 
ATOM   3670 O  O   . GLN B 1 196 ? 3.73336   -2.34410  35.78304  1.000 44.05925 ? 196 GLN B O   1 
ATOM   3671 C  CB  . GLN B 1 196 ? 1.88598   -4.48662  34.38088  1.000 43.24045 ? 196 GLN B CB  1 
ATOM   3672 C  CG  . GLN B 1 196 ? 2.98813   -5.49525  34.21942  1.000 46.58612 ? 196 GLN B CG  1 
ATOM   3673 C  CD  . GLN B 1 196 ? 2.75410   -6.42411  33.06670  1.000 51.04703 ? 196 GLN B CD  1 
ATOM   3674 O  OE1 . GLN B 1 196 ? 2.53245   -5.98131  31.94355  1.000 51.11879 ? 196 GLN B OE1 1 
ATOM   3675 N  NE2 . GLN B 1 196 ? 2.81392   -7.72671  33.32886  1.000 48.37807 ? 196 GLN B NE2 1 
ATOM   3676 N  N   . ALA B 1 197 ? 3.87827   -4.21819  37.02525  1.000 45.08255 ? 197 ALA B N   1 
ATOM   3677 C  CA  . ALA B 1 197 ? 5.25613   -3.99941  37.46687  1.000 40.65235 ? 197 ALA B CA  1 
ATOM   3678 C  C   . ALA B 1 197 ? 5.44820   -2.58337  38.01589  1.000 37.32564 ? 197 ALA B C   1 
ATOM   3679 O  O   . ALA B 1 197 ? 6.26910   -1.79712  37.54259  1.000 36.40722 ? 197 ALA B O   1 
ATOM   3680 C  CB  . ALA B 1 197 ? 6.23797   -4.29510  36.32752  1.000 48.83686 ? 197 ALA B CB  1 
ATOM   3681 N  N   . SER B 1 198 ? 4.65583   -2.24844  39.02437  1.000 35.80910 ? 198 SER B N   1 
ATOM   3682 C  CA  . SER B 1 198 ? 4.77219   -0.93485  39.63557  1.000 38.42445 ? 198 SER B CA  1 
ATOM   3683 C  C   . SER B 1 198 ? 5.24648   -0.98780  41.08467  1.000 36.13739 ? 198 SER B C   1 
ATOM   3684 O  O   . SER B 1 198 ? 5.45497   0.07212   41.68341  1.000 35.54259 ? 198 SER B O   1 
ATOM   3685 C  CB  . SER B 1 198 ? 3.43281   -0.19197  39.54580  1.000 33.09218 ? 198 SER B CB  1 
ATOM   3686 O  OG  . SER B 1 198 ? 2.37454   -1.02079  39.99504  1.000 41.93807 ? 198 SER B OG  1 
ATOM   3687 N  N   . PHE B 1 199 ? 5.42117   -2.18108  41.66516  1.000 32.14681 ? 199 PHE B N   1 
ATOM   3688 C  CA  . PHE B 1 199 ? 5.87900   -2.32972  43.04860  1.000 36.98808 ? 199 PHE B CA  1 
ATOM   3689 C  C   . PHE B 1 199 ? 7.04109   -3.30860  43.12304  1.000 37.41508 ? 199 PHE B C   1 
ATOM   3690 O  O   . PHE B 1 199 ? 6.97268   -4.40956  42.56552  1.000 47.72489 ? 199 PHE B O   1 
ATOM   3691 C  CB  . PHE B 1 199 ? 4.75407   -2.81016  43.96382  1.000 30.21793 ? 199 PHE B CB  1 
ATOM   3692 C  CG  . PHE B 1 199 ? 3.60958   -1.84398  44.05716  1.000 37.57778 ? 199 PHE B CG  1 
ATOM   3693 C  CD1 . PHE B 1 199 ? 3.65304   -0.78559  44.94444  1.000 33.88881 ? 199 PHE B CD1 1 
ATOM   3694 C  CD2 . PHE B 1 199 ? 2.50002   -1.98373  43.23841  1.000 33.51604 ? 199 PHE B CD2 1 
ATOM   3695 C  CE1 . PHE B 1 199 ? 2.60558   0.11316   45.02651  1.000 32.00669 ? 199 PHE B CE1 1 
ATOM   3696 C  CE2 . PHE B 1 199 ? 1.45536   -1.08624  43.30499  1.000 34.12820 ? 199 PHE B CE2 1 
ATOM   3697 C  CZ  . PHE B 1 199 ? 1.51025   -0.03591  44.20646  1.000 39.19996 ? 199 PHE B CZ  1 
ATOM   3698 N  N   . ASP B 1 200 ? 8.12042   -2.89173  43.78196  1.000 38.80878 ? 200 ASP B N   1 
ATOM   3699 C  CA  . ASP B 1 200 ? 9.18590   -3.82476  44.11581  1.000 39.41785 ? 200 ASP B CA  1 
ATOM   3700 C  C   . ASP B 1 200 ? 8.77258   -4.76735  45.23501  1.000 38.43078 ? 200 ASP B C   1 
ATOM   3701 O  O   . ASP B 1 200 ? 9.33227   -5.86425  45.34341  1.000 38.35701 ? 200 ASP B O   1 
ATOM   3702 C  CB  . ASP B 1 200 ? 10.44796  -3.08320  44.56744  1.000 39.70599 ? 200 ASP B CB  1 
ATOM   3703 C  CG  . ASP B 1 200 ? 10.86141  -1.97769  43.62901  1.000 41.59460 ? 200 ASP B CG  1 
ATOM   3704 O  OD1 . ASP B 1 200 ? 10.40745  -0.82913  43.81832  1.000 48.10866 ? 200 ASP B OD1 1 
ATOM   3705 O  OD2 . ASP B 1 200 ? 11.67669  -2.24271  42.72746  1.000 46.10655 ? 200 ASP B OD2 1 
ATOM   3706 N  N   . VAL B 1 201 ? 7.82811   -4.35008  46.07795  1.000 37.24190 ? 201 VAL B N   1 
ATOM   3707 C  CA  . VAL B 1 201 ? 7.48441   -5.05587  47.31155  1.000 37.29627 ? 201 VAL B CA  1 
ATOM   3708 C  C   . VAL B 1 201 ? 6.00910   -4.85155  47.60649  1.000 35.18379 ? 201 VAL B C   1 
ATOM   3709 O  O   . VAL B 1 201 ? 5.50054   -3.73094  47.53619  1.000 36.61745 ? 201 VAL B O   1 
ATOM   3710 C  CB  . VAL B 1 201 ? 8.31095   -4.55216  48.50675  1.000 30.76712 ? 201 VAL B CB  1 
ATOM   3711 C  CG1 . VAL B 1 201 ? 7.76276   -5.13051  49.78568  1.000 32.22053 ? 201 VAL B CG1 1 
ATOM   3712 C  CG2 . VAL B 1 201 ? 9.74915   -4.91655  48.35519  1.000 39.98584 ? 201 VAL B CG2 1 
ATOM   3713 N  N   . ILE B 1 202 ? 5.32978   -5.92463  47.98234  1.000 32.45533 ? 202 ILE B N   1 
ATOM   3714 C  CA  . ILE B 1 202 ? 3.97569   -5.83467  48.50444  1.000 27.42420 ? 202 ILE B CA  1 
ATOM   3715 C  C   . ILE B 1 202 ? 3.97418   -6.46592  49.88439  1.000 30.93401 ? 202 ILE B C   1 
ATOM   3716 O  O   . ILE B 1 202 ? 4.55698   -7.53607  50.07703  1.000 35.81137 ? 202 ILE B O   1 
ATOM   3717 C  CB  . ILE B 1 202 ? 2.96206   -6.54351  47.59013  1.000 34.82266 ? 202 ILE B CB  1 
ATOM   3718 C  CG1 . ILE B 1 202 ? 2.87152   -5.84780  46.22896  1.000 30.34089 ? 202 ILE B CG1 1 
ATOM   3719 C  CG2 . ILE B 1 202 ? 1.58638   -6.49027  48.21973  1.000 37.37208 ? 202 ILE B CG2 1 
ATOM   3720 C  CD1 . ILE B 1 202 ? 2.08933   -6.63255  45.22548  1.000 30.91791 ? 202 ILE B CD1 1 
ATOM   3721 N  N   . ILE B 1 203 ? 3.33861   -5.80369  50.84866  1.000 34.21133 ? 203 ILE B N   1 
ATOM   3722 C  CA  . ILE B 1 203 ? 3.15832   -6.34277  52.19892  1.000 30.39404 ? 203 ILE B CA  1 
ATOM   3723 C  C   . ILE B 1 203 ? 1.66331   -6.49183  52.41476  1.000 31.16361 ? 203 ILE B C   1 
ATOM   3724 O  O   . ILE B 1 203 ? 0.93880   -5.49464  52.51407  1.000 28.10062 ? 203 ILE B O   1 
ATOM   3725 C  CB  . ILE B 1 203 ? 3.77912   -5.45767  53.28177  1.000 28.00754 ? 203 ILE B CB  1 
ATOM   3726 C  CG1 . ILE B 1 203 ? 5.29783   -5.44069  53.14801  1.000 31.57752 ? 203 ILE B CG1 1 
ATOM   3727 C  CG2 . ILE B 1 203 ? 3.38742   -5.96391  54.65733  1.000 30.70810 ? 203 ILE B CG2 1 
ATOM   3728 C  CD1 . ILE B 1 203 ? 5.96877   -4.40316  54.02016  1.000 28.29664 ? 203 ILE B CD1 1 
ATOM   3729 N  N   . HIS B 1 204 ? 1.19490   -7.72316  52.45056  1.000 36.15440 ? 204 HIS B N   1 
ATOM   3730 C  CA  . HIS B 1 204 ? -0.23219  -8.01520  52.42723  1.000 37.70954 ? 204 HIS B CA  1 
ATOM   3731 C  C   . HIS B 1 204 ? -0.58842  -8.59323  53.78739  1.000 37.92404 ? 204 HIS B C   1 
ATOM   3732 O  O   . HIS B 1 204 ? -0.26949  -9.74391  54.08832  1.000 39.64563 ? 204 HIS B O   1 
ATOM   3733 C  CB  . HIS B 1 204 ? -0.58501  -8.97591  51.29604  1.000 35.96307 ? 204 HIS B CB  1 
ATOM   3734 C  CG  . HIS B 1 204 ? -2.05310  -9.23294  51.16216  1.000 35.97144 ? 204 HIS B CG  1 
ATOM   3735 N  ND1 . HIS B 1 204 ? -2.99085  -8.22829  51.24934  1.000 36.72337 ? 204 HIS B ND1 1 
ATOM   3736 C  CD2 . HIS B 1 204 ? -2.74594  -10.37796 50.95740  1.000 37.01038 ? 204 HIS B CD2 1 
ATOM   3737 C  CE1 . HIS B 1 204 ? -4.19779  -8.74118  51.09008  1.000 39.40667 ? 204 HIS B CE1 1 
ATOM   3738 N  NE2 . HIS B 1 204 ? -4.07777  -10.04302 50.91181  1.000 36.95146 ? 204 HIS B NE2 1 
ATOM   3739 N  N   . ASP B 1 205 ? -1.24448  -7.78796  54.60896  1.000 42.06805 ? 205 ASP B N   1 
ATOM   3740 C  CA  . ASP B 1 205 ? -1.55724  -8.14920  55.98922  1.000 38.44341 ? 205 ASP B CA  1 
ATOM   3741 C  C   . ASP B 1 205 ? -3.05126  -7.96659  56.22092  1.000 42.71288 ? 205 ASP B C   1 
ATOM   3742 O  O   . ASP B 1 205 ? -3.47611  -7.07602  56.96699  1.000 45.83138 ? 205 ASP B O   1 
ATOM   3743 C  CB  . ASP B 1 205 ? -0.73235  -7.30067  56.95427  1.000 37.57855 ? 205 ASP B CB  1 
ATOM   3744 C  CG  . ASP B 1 205 ? -0.68064  -7.89064  58.33069  1.000 46.58584 ? 205 ASP B CG  1 
ATOM   3745 O  OD1 . ASP B 1 205 ? -1.36652  -8.90905  58.55499  1.000 47.54620 ? 205 ASP B OD1 1 
ATOM   3746 O  OD2 . ASP B 1 205 ? 0.05575   -7.34828  59.17805  1.000 48.67333 ? 205 ASP B OD2 1 
ATOM   3747 N  N   . PRO B 1 206 ? -3.87719  -8.80447  55.60077  1.000 47.11465 ? 206 PRO B N   1 
ATOM   3748 C  CA  . PRO B 1 206 ? -5.33006  -8.61294  55.66552  1.000 49.30978 ? 206 PRO B CA  1 
ATOM   3749 C  C   . PRO B 1 206 ? -5.88831  -9.10769  56.98717  1.000 54.32222 ? 206 PRO B C   1 
ATOM   3750 O  O   . PRO B 1 206 ? -5.16315  -9.71633  57.78892  1.000 54.76152 ? 206 PRO B O   1 
ATOM   3751 C  CB  . PRO B 1 206 ? -5.83349  -9.47875  54.50605  1.000 41.38647 ? 206 PRO B CB  1 
ATOM   3752 C  CG  . PRO B 1 206 ? -4.88248  -10.64488 54.54279  1.000 45.24643 ? 206 PRO B CG  1 
ATOM   3753 C  CD  . PRO B 1 206 ? -3.52595  -10.03889 54.87290  1.000 44.89045 ? 206 PRO B CD  1 
ATOM   3754 N  N   . PRO B 1 207 ? -7.18630  -8.86341  57.25229  1.000 57.77226 ? 207 PRO B N   1 
ATOM   3755 C  CA  . PRO B 1 207 ? -7.88130  -9.58795  58.33283  1.000 60.22425 ? 207 PRO B CA  1 
ATOM   3756 C  C   . PRO B 1 207 ? -7.93918  -11.08882 58.07662  1.000 60.58651 ? 207 PRO B C   1 
ATOM   3757 O  O   . PRO B 1 207 ? -7.42180  -11.55679 57.05621  1.000 63.25596 ? 207 PRO B O   1 
ATOM   3758 C  CB  . PRO B 1 207 ? -9.28510  -8.96513  58.33430  1.000 62.86582 ? 207 PRO B CB  1 
ATOM   3759 C  CG  . PRO B 1 207 ? -9.38042  -8.15649  57.04709  1.000 55.91379 ? 207 PRO B CG  1 
ATOM   3760 C  CD  . PRO B 1 207 ? -7.98767  -7.75120  56.71006  1.000 47.20912 ? 207 PRO B CD  1 
ATOM   3761 N  N   . ARG B 1 208 ? -8.55833  -11.85948 58.97459  1.000 68.83215 ? 208 ARG B N   1 
ATOM   3762 C  CA  . ARG B 1 208 ? -8.57566  -13.30929 58.80393  1.000 67.37251 ? 208 ARG B CA  1 
ATOM   3763 C  C   . ARG B 1 208 ? -9.53668  -13.70179 57.67479  1.000 69.54379 ? 208 ARG B C   1 
ATOM   3764 O  O   . ARG B 1 208 ? -10.27786 -12.87290 57.13850  1.000 69.73798 ? 208 ARG B O   1 
ATOM   3765 C  CB  . ARG B 1 208 ? -8.93719  -14.01286 60.11615  1.000 71.86208 ? 208 ARG B CB  1 
ATOM   3766 C  CG  . ARG B 1 208 ? -8.08399  -15.27940 60.37804  1.000 80.68213 ? 208 ARG B CG  1 
ATOM   3767 C  CD  . ARG B 1 208 ? -8.72004  -16.28188 61.36138  1.000 80.43324 ? 208 ARG B CD  1 
ATOM   3768 N  NE  . ARG B 1 208 ? -7.71503  -17.06522 62.07960  1.000 82.30805 ? 208 ARG B NE  1 
ATOM   3769 C  CZ  . ARG B 1 208 ? -7.97147  -17.86993 63.10408  1.000 93.81039 ? 208 ARG B CZ  1 
ATOM   3770 N  NH1 . ARG B 1 208 ? -9.20047  -18.03046 63.56594  1.000 96.87321 ? 208 ARG B NH1 1 
ATOM   3771 N  NH2 . ARG B 1 208 ? -6.96981  -18.53746 63.67530  1.000 89.64655 ? 208 ARG B NH2 1 
ATOM   3772 N  N   . PHE B 1 209 ? -9.50972  -14.98911 57.30304  1.000 67.69014 ? 209 PHE B N   1 
ATOM   3773 C  CA  . PHE B 1 209 ? -10.19359 -15.42440 56.08368  1.000 67.84056 ? 209 PHE B CA  1 
ATOM   3774 C  C   . PHE B 1 209 ? -11.69963 -15.19839 56.18153  1.000 71.99187 ? 209 PHE B C   1 
ATOM   3775 O  O   . PHE B 1 209 ? -12.30281 -14.59874 55.28490  1.000 72.37189 ? 209 PHE B O   1 
ATOM   3776 C  CB  . PHE B 1 209 ? -9.86530  -16.89645 55.78223  1.000 67.05693 ? 209 PHE B CB  1 
ATOM   3777 C  CG  . PHE B 1 209 ? -10.31604 -17.37270 54.39958  1.000 78.53916 ? 209 PHE B CG  1 
ATOM   3778 C  CD1 . PHE B 1 209 ? -11.61179 -17.15967 53.93158  1.000 81.08393 ? 209 PHE B CD1 1 
ATOM   3779 C  CD2 . PHE B 1 209 ? -9.41064  -17.98855 53.54628  1.000 73.86753 ? 209 PHE B CD2 1 
ATOM   3780 C  CE1 . PHE B 1 209 ? -12.00328 -17.57643 52.66672  1.000 73.93243 ? 209 PHE B CE1 1 
ATOM   3781 C  CE2 . PHE B 1 209 ? -9.79469  -18.40294 52.27677  1.000 71.43807 ? 209 PHE B CE2 1 
ATOM   3782 C  CZ  . PHE B 1 209 ? -11.09299 -18.19258 51.83801  1.000 74.11781 ? 209 PHE B CZ  1 
ATOM   3783 N  N   . SER B 1 210 ? -12.33136 -15.68433 57.25412  1.000 79.88313 ? 210 SER B N   1 
ATOM   3784 C  CA  . SER B 1 210 ? -13.77793 -15.51710 57.38015  1.000 82.89817 ? 210 SER B CA  1 
ATOM   3785 C  C   . SER B 1 210 ? -14.16418 -14.04118 57.37605  1.000 79.00958 ? 210 SER B C   1 
ATOM   3786 O  O   . SER B 1 210 ? -15.14933 -13.65248 56.73569  1.000 82.16287 ? 210 SER B O   1 
ATOM   3787 C  CB  . SER B 1 210 ? -14.29029 -16.19975 58.65170  1.000 78.05891 ? 210 SER B CB  1 
ATOM   3788 O  OG  . SER B 1 210 ? -13.96179 -15.45092 59.81121  1.000 71.37732 ? 210 SER B OG  1 
ATOM   3789 N  N   . LEU B 1 211 ? -13.38600 -13.20124 58.06870  1.000 72.36323 ? 211 LEU B N   1 
ATOM   3790 C  CA  . LEU B 1 211 ? -13.73245 -11.78787 58.17895  1.000 71.33366 ? 211 LEU B CA  1 
ATOM   3791 C  C   . LEU B 1 211 ? -13.81781 -11.12121 56.81108  1.000 76.22021 ? 211 LEU B C   1 
ATOM   3792 O  O   . LEU B 1 211 ? -14.58916 -10.16996 56.63844  1.000 78.87914 ? 211 LEU B O   1 
ATOM   3793 C  CB  . LEU B 1 211 ? -12.72149 -11.07057 59.07931  1.000 70.86764 ? 211 LEU B CB  1 
ATOM   3794 C  CG  . LEU B 1 211 ? -13.03493 -11.07251 60.58531  1.000 74.61135 ? 211 LEU B CG  1 
ATOM   3795 C  CD1 . LEU B 1 211 ? -11.76514 -11.16676 61.43283  1.000 74.72664 ? 211 LEU B CD1 1 
ATOM   3796 C  CD2 . LEU B 1 211 ? -13.84040 -9.84075  60.97506  1.000 61.32631 ? 211 LEU B CD2 1 
ATOM   3797 N  N   . ALA B 1 212 ? -13.05367 -11.61864 55.82984  1.000 72.81838 ? 212 ALA B N   1 
ATOM   3798 C  CA  . ALA B 1 212 ? -13.10756 -11.16066 54.44319  1.000 64.25679 ? 212 ALA B CA  1 
ATOM   3799 C  C   . ALA B 1 212 ? -12.23932 -12.04671 53.55159  1.000 70.22598 ? 212 ALA B C   1 
ATOM   3800 O  O   . ALA B 1 212 ? -11.01472 -11.88144 53.50702  1.000 67.03966 ? 212 ALA B O   1 
ATOM   3801 C  CB  . ALA B 1 212 ? -12.65799 -9.70335  54.32855  1.000 72.96199 ? 212 ALA B CB  1 
ATOM   3802 N  N   . GLY B 1 213 ? -12.86154 -12.97201 52.81887  1.000 66.73801 ? 213 GLY B N   1 
ATOM   3803 C  CA  . GLY B 1 213 ? -12.12454 -13.98163 52.07684  1.000 59.49614 ? 213 GLY B CA  1 
ATOM   3804 C  C   . GLY B 1 213 ? -11.64403 -13.59804 50.69182  1.000 58.83578 ? 213 GLY B C   1 
ATOM   3805 O  O   . GLY B 1 213 ? -10.77620 -14.27392 50.13046  1.000 58.58536 ? 213 GLY B O   1 
ATOM   3806 N  N   . HIS B 1 214 ? -12.20327 -12.52549 50.12412  1.000 53.91129 ? 214 HIS B N   1 
ATOM   3807 C  CA  . HIS B 1 214 ? -11.78152 -12.07122 48.80161  1.000 49.69702 ? 214 HIS B CA  1 
ATOM   3808 C  C   . HIS B 1 214 ? -10.29760 -11.72549 48.76282  1.000 55.22703 ? 214 HIS B C   1 
ATOM   3809 O  O   . HIS B 1 214 ? -9.64364  -11.91963 47.73030  1.000 59.71450 ? 214 HIS B O   1 
ATOM   3810 C  CB  . HIS B 1 214 ? -12.61360 -10.86233 48.38361  1.000 52.30718 ? 214 HIS B CB  1 
ATOM   3811 C  CG  . HIS B 1 214 ? -12.44834 -9.68414  49.29209  1.000 54.75085 ? 214 HIS B CG  1 
ATOM   3812 N  ND1 . HIS B 1 214 ? -13.05998 -9.60441  50.52569  1.000 59.73392 ? 214 HIS B ND1 1 
ATOM   3813 C  CD2 . HIS B 1 214 ? -11.73690 -8.54123  49.15170  1.000 51.79310 ? 214 HIS B CD2 1 
ATOM   3814 C  CE1 . HIS B 1 214 ? -12.73002 -8.46362  51.10687  1.000 59.00447 ? 214 HIS B CE1 1 
ATOM   3815 N  NE2 . HIS B 1 214 ? -11.92742 -7.79973  50.29478  1.000 57.85592 ? 214 HIS B NE2 1 
ATOM   3816 N  N   . LEU B 1 215 ? -9.74625  -11.22313 49.86973  1.000 52.56806 ? 215 LEU B N   1 
ATOM   3817 C  CA  . LEU B 1 215 ? -8.33844  -10.85334 49.95347  1.000 47.55432 ? 215 LEU B CA  1 
ATOM   3818 C  C   . LEU B 1 215 ? -7.41643  -12.05726 50.02418  1.000 52.17332 ? 215 LEU B C   1 
ATOM   3819 O  O   . LEU B 1 215 ? -6.21558  -11.89030 50.26314  1.000 52.97738 ? 215 LEU B O   1 
ATOM   3820 C  CB  . LEU B 1 215 ? -8.09980  -9.96066  51.17263  1.000 46.27072 ? 215 LEU B CB  1 
ATOM   3821 C  CG  . LEU B 1 215 ? -8.65294  -8.53817  51.15768  1.000 47.15607 ? 215 LEU B CG  1 
ATOM   3822 C  CD1 . LEU B 1 215 ? -7.90901  -7.71325  52.17928  1.000 41.26161 ? 215 LEU B CD1 1 
ATOM   3823 C  CD2 . LEU B 1 215 ? -8.52507  -7.90395  49.77286  1.000 46.77837 ? 215 LEU B CD2 1 
ATOM   3824 N  N   . TYR B 1 216 ? -7.95180  -13.25849 49.81819  1.000 55.11558 ? 216 TYR B N   1 
ATOM   3825 C  CA  . TYR B 1 216 ? -7.18578  -14.49482 49.83349  1.000 53.69176 ? 216 TYR B CA  1 
ATOM   3826 C  C   . TYR B 1 216 ? -7.33001  -15.23587 48.51859  1.000 57.15854 ? 216 TYR B C   1 
ATOM   3827 O  O   . TYR B 1 216 ? -6.84683  -16.36620 48.39572  1.000 50.89873 ? 216 TYR B O   1 
ATOM   3828 C  CB  . TYR B 1 216 ? -7.66772  -15.37106 50.98983  1.000 56.76165 ? 216 TYR B CB  1 
ATOM   3829 C  CG  . TYR B 1 216 ? -7.12909  -14.93880 52.32842  1.000 55.81743 ? 216 TYR B CG  1 
ATOM   3830 C  CD1 . TYR B 1 216 ? -7.83394  -14.03493 53.10872  1.000 56.09019 ? 216 TYR B CD1 1 
ATOM   3831 C  CD2 . TYR B 1 216 ? -5.96180  -15.47969 52.84487  1.000 51.82209 ? 216 TYR B CD2 1 
ATOM   3832 C  CE1 . TYR B 1 216 ? -7.36282  -13.62941 54.33909  1.000 57.24034 ? 216 TYR B CE1 1 
ATOM   3833 C  CE2 . TYR B 1 216 ? -5.48553  -15.08440 54.08316  1.000 54.94188 ? 216 TYR B CE2 1 
ATOM   3834 C  CZ  . TYR B 1 216 ? -6.19337  -14.16283 54.82714  1.000 57.79642 ? 216 TYR B CZ  1 
ATOM   3835 O  OH  . TYR B 1 216 ? -5.72996  -13.76463 56.06405  1.000 68.85342 ? 216 TYR B OH  1 
ATOM   3836 N  N   . SER B 1 217 ? -7.98757  -14.62575 47.53958  1.000 57.58306 ? 217 SER B N   1 
ATOM   3837 C  CA  . SER B 1 217 ? -8.53474  -15.34722 46.40192  1.000 68.73125 ? 217 SER B CA  1 
ATOM   3838 C  C   . SER B 1 217 ? -7.49924  -15.53638 45.30033  1.000 63.11884 ? 217 SER B C   1 
ATOM   3839 O  O   . SER B 1 217 ? -6.36940  -15.04200 45.35623  1.000 61.10542 ? 217 SER B O   1 
ATOM   3840 C  CB  . SER B 1 217 ? -9.76349  -14.62245 45.84161  1.000 56.53639 ? 217 SER B CB  1 
ATOM   3841 O  OG  . SER B 1 217 ? -9.48071  -13.25103 45.61130  1.000 55.81864 ? 217 SER B OG  1 
ATOM   3842 N  N   . GLU B 1 218 ? -7.91159  -16.28240 44.28364  1.000 72.93206 ? 218 GLU B N   1 
ATOM   3843 C  CA  . GLU B 1 218 ? -7.07773  -16.43804 43.10673  1.000 71.33407 ? 218 GLU B CA  1 
ATOM   3844 C  C   . GLU B 1 218 ? -6.90972  -15.10914 42.38977  1.000 72.23717 ? 218 GLU B C   1 
ATOM   3845 O  O   . GLU B 1 218 ? -5.78363  -14.66688 42.13256  1.000 70.26067 ? 218 GLU B O   1 
ATOM   3846 C  CB  . GLU B 1 218 ? -7.69001  -17.49292 42.18528  1.000 80.64951 ? 218 GLU B CB  1 
ATOM   3847 C  CG  . GLU B 1 218 ? -6.71000  -18.24535 41.29262  1.000 81.80850 ? 218 GLU B CG  1 
ATOM   3848 C  CD  . GLU B 1 218 ? -5.50207  -18.83828 42.00396  1.000 88.06773 ? 218 GLU B CD  1 
ATOM   3849 O  OE1 . GLU B 1 218 ? -5.37616  -18.74255 43.24502  1.000 82.57603 ? 218 GLU B OE1 1 
ATOM   3850 O  OE2 . GLU B 1 218 ? -4.65392  -19.41218 41.28941  1.000 91.78749 ? 218 GLU B OE2 1 
ATOM   3851 N  N   . GLU B 1 219 ? -8.02553  -14.44900 42.07724  1.000 53.87167 ? 219 GLU B N   1 
ATOM   3852 C  CA  . GLU B 1 219 ? -7.96018  -13.17492 41.37126  1.000 58.68686 ? 219 GLU B CA  1 
ATOM   3853 C  C   . GLU B 1 219 ? -7.08100  -12.17546 42.10275  1.000 50.81473 ? 219 GLU B C   1 
ATOM   3854 O  O   . GLU B 1 219 ? -6.26330  -11.49044 41.48101  1.000 49.12964 ? 219 GLU B O   1 
ATOM   3855 C  CB  . GLU B 1 219 ? -9.36140  -12.59525 41.18355  1.000 57.59698 ? 219 GLU B CB  1 
ATOM   3856 C  CG  . GLU B 1 219 ? -10.28723 -12.86117 42.34763  1.000 63.75859 ? 219 GLU B CG  1 
ATOM   3857 C  CD  . GLU B 1 219 ? -11.73488 -12.60412 41.99758  1.000 60.66650 ? 219 GLU B CD  1 
ATOM   3858 O  OE1 . GLU B 1 219 ? -11.99501 -11.60768 41.28590  1.000 56.93136 ? 219 GLU B OE1 1 
ATOM   3859 O  OE2 . GLU B 1 219 ? -12.60408 -13.39709 42.43083  1.000 65.30393 ? 219 GLU B OE2 1 
ATOM   3860 N  N   . PHE B 1 220 ? -7.21930  -12.07939 43.42606  1.000 51.75233 ? 220 PHE B N   1 
ATOM   3861 C  CA  . PHE B 1 220 ? -6.44760  -11.06453 44.13550  1.000 47.38440 ? 220 PHE B CA  1 
ATOM   3862 C  C   . PHE B 1 220 ? -4.95633  -11.34580 44.05962  1.000 46.36893 ? 220 PHE B C   1 
ATOM   3863 O  O   . PHE B 1 220 ? -4.16001  -10.41726 43.88444  1.000 47.19749 ? 220 PHE B O   1 
ATOM   3864 C  CB  . PHE B 1 220 ? -6.86789  -10.94486 45.59495  1.000 45.47861 ? 220 PHE B CB  1 
ATOM   3865 C  CG  . PHE B 1 220 ? -6.21085  -9.79250  46.29615  1.000 40.94275 ? 220 PHE B CG  1 
ATOM   3866 C  CD1 . PHE B 1 220 ? -6.64099  -8.49218  46.06983  1.000 44.61219 ? 220 PHE B CD1 1 
ATOM   3867 C  CD2 . PHE B 1 220 ? -5.14274  -9.99579  47.15254  1.000 42.53012 ? 220 PHE B CD2 1 
ATOM   3868 C  CE1 . PHE B 1 220 ? -6.03522  -7.40013  46.70998  1.000 38.15728 ? 220 PHE B CE1 1 
ATOM   3869 C  CE2 . PHE B 1 220 ? -4.53576  -8.91979  47.79059  1.000 45.76211 ? 220 PHE B CE2 1 
ATOM   3870 C  CZ  . PHE B 1 220 ? -4.98367  -7.61072  47.56293  1.000 37.40106 ? 220 PHE B CZ  1 
ATOM   3871 N  N   . TYR B 1 221 ? -4.55468  -12.61217 44.20586  1.000 46.78900 ? 221 TYR B N   1 
ATOM   3872 C  CA  . TYR B 1 221 ? -3.14171  -12.93521 44.06299  1.000 43.97275 ? 221 TYR B CA  1 
ATOM   3873 C  C   . TYR B 1 221 ? -2.66267  -12.68268 42.63929  1.000 50.17480 ? 221 TYR B C   1 
ATOM   3874 O  O   . TYR B 1 221 ? -1.51729  -12.26320 42.43865  1.000 52.75509 ? 221 TYR B O   1 
ATOM   3875 C  CB  . TYR B 1 221 ? -2.87727  -14.38485 44.46289  1.000 51.62299 ? 221 TYR B CB  1 
ATOM   3876 C  CG  . TYR B 1 221 ? -3.20052  -14.71622 45.90974  1.000 53.60679 ? 221 TYR B CG  1 
ATOM   3877 C  CD1 . TYR B 1 221 ? -3.38325  -13.71406 46.85358  1.000 52.48116 ? 221 TYR B CD1 1 
ATOM   3878 C  CD2 . TYR B 1 221 ? -3.31399  -16.03428 46.32738  1.000 51.99096 ? 221 TYR B CD2 1 
ATOM   3879 C  CE1 . TYR B 1 221 ? -3.68133  -14.01426 48.16917  1.000 50.50393 ? 221 TYR B CE1 1 
ATOM   3880 C  CE2 . TYR B 1 221 ? -3.60842  -16.34054 47.63396  1.000 54.98482 ? 221 TYR B CE2 1 
ATOM   3881 C  CZ  . TYR B 1 221 ? -3.79032  -15.32701 48.55064  1.000 50.60435 ? 221 TYR B CZ  1 
ATOM   3882 O  OH  . TYR B 1 221 ? -4.08352  -15.63538 49.85663  1.000 53.74672 ? 221 TYR B OH  1 
ATOM   3883 N  N   . ARG B 1 222 ? -3.52286  -12.91962 41.64524  1.000 46.24624 ? 222 ARG B N   1 
ATOM   3884 C  CA  . ARG B 1 222 ? -3.16265  -12.60649 40.26429  1.000 51.14651 ? 222 ARG B CA  1 
ATOM   3885 C  C   . ARG B 1 222 ? -2.83901  -11.12502 40.09653  1.000 49.40216 ? 222 ARG B C   1 
ATOM   3886 O  O   . ARG B 1 222 ? -1.87571  -10.76720 39.40720  1.000 47.49321 ? 222 ARG B O   1 
ATOM   3887 C  CB  . ARG B 1 222 ? -4.29417  -13.00370 39.32031  1.000 46.54182 ? 222 ARG B CB  1 
ATOM   3888 C  CG  . ARG B 1 222 ? -4.34002  -14.46504 38.95179  1.000 50.99222 ? 222 ARG B CG  1 
ATOM   3889 C  CD  . ARG B 1 222 ? -5.29106  -14.65091 37.77422  1.000 55.96058 ? 222 ARG B CD  1 
ATOM   3890 N  NE  . ARG B 1 222 ? -6.68050  -14.65516 38.21860  1.000 54.36216 ? 222 ARG B NE  1 
ATOM   3891 C  CZ  . ARG B 1 222 ? -7.34746  -15.74468 38.57345  1.000 63.11097 ? 222 ARG B CZ  1 
ATOM   3892 N  NH1 . ARG B 1 222 ? -6.80426  -16.94841 38.47925  1.000 60.76494 ? 222 ARG B NH1 1 
ATOM   3893 N  NH2 . ARG B 1 222 ? -8.59340  -15.62437 39.02390  1.000 65.74665 ? 222 ARG B NH2 1 
ATOM   3894 N  N   . GLU B 1 223 ? -3.63875  -10.24713 40.70950  1.000 40.61528 ? 223 GLU B N   1 
ATOM   3895 C  CA  . GLU B 1 223 ? -3.36444  -8.82110  40.60549  1.000 38.83489 ? 223 GLU B CA  1 
ATOM   3896 C  C   . GLU B 1 223 ? -2.09309  -8.46154  41.35782  1.000 43.08662 ? 223 GLU B C   1 
ATOM   3897 O  O   . GLU B 1 223 ? -1.28371  -7.66269  40.87121  1.000 45.62473 ? 223 GLU B O   1 
ATOM   3898 C  CB  . GLU B 1 223 ? -4.53935  -8.00390  41.14411  1.000 40.48032 ? 223 GLU B CB  1 
ATOM   3899 C  CG  . GLU B 1 223 ? -5.83160  -8.06287  40.32341  1.000 46.94669 ? 223 GLU B CG  1 
ATOM   3900 C  CD  . GLU B 1 223 ? -5.64348  -7.74283  38.84312  1.000 44.16479 ? 223 GLU B CD  1 
ATOM   3901 O  OE1 . GLU B 1 223 ? -4.95208  -6.74950  38.50695  1.000 43.48241 ? 223 GLU B OE1 1 
ATOM   3902 O  OE2 . GLU B 1 223 ? -6.21666  -8.48495  38.01658  1.000 47.88002 ? 223 GLU B OE2 1 
ATOM   3903 N  N   . LEU B 1 224 ? -1.91034  -9.02592  42.55627  1.000 39.11900 ? 224 LEU B N   1 
ATOM   3904 C  CA  . LEU B 1 224 ? -0.65976  -8.82314  43.27647  1.000 39.07502 ? 224 LEU B CA  1 
ATOM   3905 C  C   . LEU B 1 224 ? 0.52632   -9.23604  42.42278  1.000 40.48730 ? 224 LEU B C   1 
ATOM   3906 O  O   . LEU B 1 224 ? 1.51530   -8.50237  42.32751  1.000 42.33091 ? 224 LEU B O   1 
ATOM   3907 C  CB  . LEU B 1 224 ? -0.67563  -9.59996  44.59224  1.000 46.61866 ? 224 LEU B CB  1 
ATOM   3908 C  CG  . LEU B 1 224 ? -1.61685  -9.16639  45.73219  1.000 37.14784 ? 224 LEU B CG  1 
ATOM   3909 C  CD1 . LEU B 1 224 ? -1.07769  -9.64918  47.08823  1.000 36.58211 ? 224 LEU B CD1 1 
ATOM   3910 C  CD2 . LEU B 1 224 ? -1.85564  -7.65983  45.74302  1.000 39.45366 ? 224 LEU B CD2 1 
ATOM   3911 N  N   . PHE B 1 225 ? 0.41612   -10.38316 41.74768  1.000 44.47362 ? 225 PHE B N   1 
ATOM   3912 C  CA  . PHE B 1 225 ? 1.46789   -10.84355 40.84423  1.000 43.41721 ? 225 PHE B CA  1 
ATOM   3913 C  C   . PHE B 1 225 ? 1.70775   -9.85817  39.70575  1.000 43.42847 ? 225 PHE B C   1 
ATOM   3914 O  O   . PHE B 1 225 ? 2.85443   -9.62477  39.31060  1.000 45.88518 ? 225 PHE B O   1 
ATOM   3915 C  CB  . PHE B 1 225 ? 1.09893   -12.22100 40.27735  1.000 48.94383 ? 225 PHE B CB  1 
ATOM   3916 C  CG  . PHE B 1 225 ? 2.18709   -12.85467 39.44694  1.000 49.64213 ? 225 PHE B CG  1 
ATOM   3917 C  CD1 . PHE B 1 225 ? 3.29035   -13.42046 40.05067  1.000 52.07861 ? 225 PHE B CD1 1 
ATOM   3918 C  CD2 . PHE B 1 225 ? 2.10421   -12.88193 38.07053  1.000 54.48301 ? 225 PHE B CD2 1 
ATOM   3919 C  CE1 . PHE B 1 225 ? 4.27972   -13.99527 39.30226  1.000 50.17805 ? 225 PHE B CE1 1 
ATOM   3920 C  CE2 . PHE B 1 225 ? 3.10135   -13.45791 37.31803  1.000 54.09221 ? 225 PHE B CE2 1 
ATOM   3921 C  CZ  . PHE B 1 225 ? 4.19000   -14.01289 37.93945  1.000 54.25088 ? 225 PHE B CZ  1 
ATOM   3922 N  N   . ARG B 1 226 ? 0.63915   -9.28780  39.15154  1.000 42.55200 ? 226 ARG B N   1 
ATOM   3923 C  CA  . ARG B 1 226 ? 0.77679   -8.42833  37.97879  1.000 45.82192 ? 226 ARG B CA  1 
ATOM   3924 C  C   . ARG B 1 226 ? 1.47099   -7.11844  38.32602  1.000 41.38308 ? 226 ARG B C   1 
ATOM   3925 O  O   . ARG B 1 226 ? 2.36885   -6.66725  37.60339  1.000 40.42001 ? 226 ARG B O   1 
ATOM   3926 C  CB  . ARG B 1 226 ? -0.59944  -8.15306  37.37183  1.000 36.52957 ? 226 ARG B CB  1 
ATOM   3927 C  CG  . ARG B 1 226 ? -0.56944  -7.31326  36.11525  1.000 37.89147 ? 226 ARG B CG  1 
ATOM   3928 C  CD  . ARG B 1 226 ? -1.98809  -7.01074  35.61395  1.000 38.14860 ? 226 ARG B CD  1 
ATOM   3929 N  NE  . ARG B 1 226 ? -2.79434  -6.33529  36.62348  1.000 47.69610 ? 226 ARG B NE  1 
ATOM   3930 C  CZ  . ARG B 1 226 ? -2.80924  -5.02388  36.81650  1.000 37.90605 ? 226 ARG B CZ  1 
ATOM   3931 N  NH1 . ARG B 1 226 ? -2.12775  -4.20510  36.03588  1.000 41.78116 ? 226 ARG B NH1 1 
ATOM   3932 N  NH2 . ARG B 1 226 ? -3.52082  -4.52481  37.81845  1.000 37.75692 ? 226 ARG B NH2 1 
ATOM   3933 N  N   . ILE B 1 227 ? 1.07068   -6.49421  39.43050  1.000 42.61355 ? 227 ILE B N   1 
ATOM   3934 C  CA  . ILE B 1 227 ? 1.58834   -5.17426  39.77940  1.000 39.97426 ? 227 ILE B CA  1 
ATOM   3935 C  C   . ILE B 1 227 ? 2.96503   -5.22738  40.42048  1.000 36.91028 ? 227 ILE B C   1 
ATOM   3936 O  O   . ILE B 1 227 ? 3.57035   -4.17373  40.64749  1.000 36.93624 ? 227 ILE B O   1 
ATOM   3937 C  CB  . ILE B 1 227 ? 0.57158   -4.46942  40.69276  1.000 39.21915 ? 227 ILE B CB  1 
ATOM   3938 C  CG1 . ILE B 1 227 ? 0.42289   -5.23739  42.00911  1.000 34.48246 ? 227 ILE B CG1 1 
ATOM   3939 C  CG2 . ILE B 1 227 ? -0.77161  -4.34403  39.97755  1.000 36.74628 ? 227 ILE B CG2 1 
ATOM   3940 C  CD1 . ILE B 1 227 ? -0.35099  -4.49888  43.06066  1.000 34.94876 ? 227 ILE B CD1 1 
ATOM   3941 N  N   . LEU B 1 228 ? 3.47120   -6.41709  40.72176  1.000 38.52585 ? 228 LEU B N   1 
ATOM   3942 C  CA  . LEU B 1 228 ? 4.83704   -6.57743  41.18355  1.000 37.65811 ? 228 LEU B CA  1 
ATOM   3943 C  C   . LEU B 1 228 ? 5.80537   -6.50020  40.00586  1.000 42.30307 ? 228 LEU B C   1 
ATOM   3944 O  O   . LEU B 1 228 ? 5.51083   -6.94799  38.89387  1.000 45.47200 ? 228 LEU B O   1 
ATOM   3945 C  CB  . LEU B 1 228 ? 5.00014   -7.92303  41.88991  1.000 41.27246 ? 228 LEU B CB  1 
ATOM   3946 C  CG  . LEU B 1 228 ? 4.94003   -8.02495  43.41401  1.000 33.65826 ? 228 LEU B CG  1 
ATOM   3947 C  CD1 . LEU B 1 228 ? 5.47715   -9.35887  43.83718  1.000 39.27797 ? 228 LEU B CD1 1 
ATOM   3948 C  CD2 . LEU B 1 228 ? 5.74002   -6.92155  44.05062  1.000 37.42948 ? 228 LEU B CD2 1 
ATOM   3949 N  N   . LYS B 1 229 ? 6.97508   -5.93384  40.26193  1.000 42.07205 ? 229 LYS B N   1 
ATOM   3950 C  CA  . LYS B 1 229 ? 8.03575   -5.96747  39.27580  1.000 40.33602 ? 229 LYS B CA  1 
ATOM   3951 C  C   . LYS B 1 229 ? 8.67228   -7.35423  39.24155  1.000 44.49972 ? 229 LYS B C   1 
ATOM   3952 O  O   . LYS B 1 229 ? 8.58508   -8.10687  40.21589  1.000 49.61954 ? 229 LYS B O   1 
ATOM   3953 C  CB  . LYS B 1 229 ? 9.08739   -4.91093  39.59316  1.000 40.48115 ? 229 LYS B CB  1 
ATOM   3954 C  CG  . LYS B 1 229 ? 8.62563   -3.50753  39.28113  1.000 42.61397 ? 229 LYS B CG  1 
ATOM   3955 C  CD  . LYS B 1 229 ? 9.50805   -2.46655  39.91942  1.000 42.88853 ? 229 LYS B CD  1 
ATOM   3956 C  CE  . LYS B 1 229 ? 8.74186   -1.17091  40.08954  1.000 45.78369 ? 229 LYS B CE  1 
ATOM   3957 N  NZ  . LYS B 1 229 ? 9.63146   -0.00543  40.43460  1.000 46.83488 ? 229 LYS B NZ  1 
ATOM   3958 N  N   . PRO B 1 230 ? 9.28076   -7.73211  38.11720  1.000 47.83906 ? 230 PRO B N   1 
ATOM   3959 C  CA  . PRO B 1 230 ? 10.09865  -8.95114  38.09839  1.000 50.14196 ? 230 PRO B CA  1 
ATOM   3960 C  C   . PRO B 1 230 ? 11.12334  -8.92786  39.22487  1.000 50.44205 ? 230 PRO B C   1 
ATOM   3961 O  O   . PRO B 1 230 ? 11.73011  -7.89516  39.51666  1.000 55.37911 ? 230 PRO B O   1 
ATOM   3962 C  CB  . PRO B 1 230 ? 10.76471  -8.90706  36.72164  1.000 47.38929 ? 230 PRO B CB  1 
ATOM   3963 C  CG  . PRO B 1 230 ? 9.81156   -8.16188  35.87311  1.000 46.48142 ? 230 PRO B CG  1 
ATOM   3964 C  CD  . PRO B 1 230 ? 9.13353   -7.14582  36.77352  1.000 50.35876 ? 230 PRO B CD  1 
ATOM   3965 N  N   . GLY B 1 231 ? 11.29759  -10.07213 39.88171  1.000 49.61673 ? 231 GLY B N   1 
ATOM   3966 C  CA  . GLY B 1 231 ? 12.10206  -10.08402 41.08659  1.000 52.51537 ? 231 GLY B CA  1 
ATOM   3967 C  C   . GLY B 1 231 ? 11.49490  -9.32942  42.24803  1.000 56.90888 ? 231 GLY B C   1 
ATOM   3968 O  O   . GLY B 1 231 ? 12.17451  -9.11520  43.25747  1.000 63.63859 ? 231 GLY B O   1 
ATOM   3969 N  N   . GLY B 1 232 ? 10.23901  -8.90493  42.13404  1.000 50.05003 ? 232 GLY B N   1 
ATOM   3970 C  CA  . GLY B 1 232 ? 9.57476   -8.27438  43.25301  1.000 46.49727 ? 232 GLY B CA  1 
ATOM   3971 C  C   . GLY B 1 232 ? 9.31031   -9.25884  44.37195  1.000 51.52833 ? 232 GLY B C   1 
ATOM   3972 O  O   . GLY B 1 232 ? 9.26765   -10.47847 44.17558  1.000 56.40563 ? 232 GLY B O   1 
ATOM   3973 N  N   . ARG B 1 233 ? 9.14230   -8.70947  45.57300  1.000 49.19866 ? 233 ARG B N   1 
ATOM   3974 C  CA  . ARG B 1 233 ? 9.01427   -9.49210  46.79409  1.000 50.22290 ? 233 ARG B CA  1 
ATOM   3975 C  C   . ARG B 1 233 ? 7.65467   -9.25953  47.42726  1.000 38.38237 ? 233 ARG B C   1 
ATOM   3976 O  O   . ARG B 1 233 ? 7.18213   -8.12532  47.50809  1.000 36.09551 ? 233 ARG B O   1 
ATOM   3977 C  CB  . ARG B 1 233 ? 10.09916  -9.12898  47.81234  1.000 50.77084 ? 233 ARG B CB  1 
ATOM   3978 C  CG  . ARG B 1 233 ? 11.51172  -9.35416  47.34374  1.000 50.79236 ? 233 ARG B CG  1 
ATOM   3979 C  CD  . ARG B 1 233 ? 12.11883  -8.04871  46.89499  1.000 54.79226 ? 233 ARG B CD  1 
ATOM   3980 N  NE  . ARG B 1 233 ? 12.44256  -7.14082  47.99212  1.000 45.24133 ? 233 ARG B NE  1 
ATOM   3981 C  CZ  . ARG B 1 233 ? 12.80846  -5.88127  47.79652  1.000 49.94651 ? 233 ARG B CZ  1 
ATOM   3982 N  NH1 . ARG B 1 233 ? 12.88565  -5.36971  46.57886  1.000 49.15033 ? 233 ARG B NH1 1 
ATOM   3983 N  NH2 . ARG B 1 233 ? 13.09321  -5.11186  48.84205  1.000 41.57609 ? 233 ARG B NH2 1 
ATOM   3984 N  N   . LEU B 1 234 ? 7.04793   -10.32951 47.91025  1.000 43.31070 ? 234 LEU B N   1 
ATOM   3985 C  CA  . LEU B 1 234 ? 5.74826   -10.24491 48.55305  1.000 42.92978 ? 234 LEU B CA  1 
ATOM   3986 C  C   . LEU B 1 234 ? 5.81741   -10.89084 49.92525  1.000 44.75140 ? 234 LEU B C   1 
ATOM   3987 O  O   . LEU B 1 234 ? 6.44794   -11.93759 50.09376  1.000 50.19999 ? 234 LEU B O   1 
ATOM   3988 C  CB  . LEU B 1 234 ? 4.67599   -10.92977 47.70817  1.000 44.34648 ? 234 LEU B CB  1 
ATOM   3989 C  CG  . LEU B 1 234 ? 3.41092   -11.28435 48.48198  1.000 45.37829 ? 234 LEU B CG  1 
ATOM   3990 C  CD1 . LEU B 1 234 ? 2.52387   -10.06149 48.61314  1.000 43.25761 ? 234 LEU B CD1 1 
ATOM   3991 C  CD2 . LEU B 1 234 ? 2.68081   -12.44629 47.82322  1.000 48.13792 ? 234 LEU B CD2 1 
ATOM   3992 N  N   . PHE B 1 235 ? 5.19193   -10.25373 50.90940  1.000 42.77573 ? 235 PHE B N   1 
ATOM   3993 C  CA  . PHE B 1 235 ? 4.96535   -10.85949 52.21296  1.000 38.02931 ? 235 PHE B CA  1 
ATOM   3994 C  C   . PHE B 1 235 ? 3.46610   -10.94460 52.44357  1.000 43.07297 ? 235 PHE B C   1 
ATOM   3995 O  O   . PHE B 1 235 ? 2.74628   -9.96434  52.22075  1.000 45.98801 ? 235 PHE B O   1 
ATOM   3996 C  CB  . PHE B 1 235 ? 5.62223   -10.06144 53.34032  1.000 40.23430 ? 235 PHE B CB  1 
ATOM   3997 C  CG  . PHE B 1 235 ? 5.33447   -10.61245 54.70759  1.000 36.05966 ? 235 PHE B CG  1 
ATOM   3998 C  CD1 . PHE B 1 235 ? 6.01529   -11.71912 55.17517  1.000 45.79100 ? 235 PHE B CD1 1 
ATOM   3999 C  CD2 . PHE B 1 235 ? 4.36547   -10.03529 55.51118  1.000 45.25262 ? 235 PHE B CD2 1 
ATOM   4000 C  CE1 . PHE B 1 235 ? 5.74451   -12.23565 56.42842  1.000 49.91134 ? 235 PHE B CE1 1 
ATOM   4001 C  CE2 . PHE B 1 235 ? 4.08497   -10.53661 56.75654  1.000 49.28766 ? 235 PHE B CE2 1 
ATOM   4002 C  CZ  . PHE B 1 235 ? 4.78243   -11.64630 57.22283  1.000 50.11766 ? 235 PHE B CZ  1 
ATOM   4003 N  N   . HIS B 1 236 ? 3.00046   -12.10769 52.89259  1.000 39.42611 ? 236 HIS B N   1 
ATOM   4004 C  CA  . HIS B 1 236 ? 1.58641   -12.34336 53.15680  1.000 43.56134 ? 236 HIS B CA  1 
ATOM   4005 C  C   . HIS B 1 236 ? 1.44554   -12.88128 54.57308  1.000 47.76957 ? 236 HIS B C   1 
ATOM   4006 O  O   . HIS B 1 236 ? 1.97406   -13.95332 54.87334  1.000 52.35455 ? 236 HIS B O   1 
ATOM   4007 C  CB  . HIS B 1 236 ? 1.02060   -13.32996 52.13377  1.000 40.10578 ? 236 HIS B CB  1 
ATOM   4008 C  CG  . HIS B 1 236 ? -0.45608  -13.55712 52.23876  1.000 47.45962 ? 236 HIS B CG  1 
ATOM   4009 N  ND1 . HIS B 1 236 ? -1.12410  -13.63820 53.44279  1.000 50.71415 ? 236 HIS B ND1 1 
ATOM   4010 C  CD2 . HIS B 1 236 ? -1.39081  -13.75310 51.27944  1.000 44.35133 ? 236 HIS B CD2 1 
ATOM   4011 C  CE1 . HIS B 1 236 ? -2.40701  -13.86169 53.22040  1.000 47.77865 ? 236 HIS B CE1 1 
ATOM   4012 N  NE2 . HIS B 1 236 ? -2.59516  -13.93706 51.91518  1.000 52.19582 ? 236 HIS B NE2 1 
ATOM   4013 N  N   . TYR B 1 237 ? 0.72877   -12.15263 55.43516  1.000 48.71760 ? 237 TYR B N   1 
ATOM   4014 C  CA  . TYR B 1 237 ? 0.54375   -12.56886 56.82427  1.000 46.45177 ? 237 TYR B CA  1 
ATOM   4015 C  C   . TYR B 1 237 ? -0.46958  -13.70046 56.93163  1.000 46.76052 ? 237 TYR B C   1 
ATOM   4016 O  O   . TYR B 1 237 ? -1.39326  -13.80587 56.12519  1.000 52.37772 ? 237 TYR B O   1 
ATOM   4017 C  CB  . TYR B 1 237 ? 0.07266   -11.39896 57.69138  1.000 48.92924 ? 237 TYR B CB  1 
ATOM   4018 C  CG  . TYR B 1 237 ? -0.01194  -11.72571 59.17625  1.000 58.02565 ? 237 TYR B CG  1 
ATOM   4019 C  CD1 . TYR B 1 237 ? 1.11451   -11.63874 59.98796  1.000 57.46831 ? 237 TYR B CD1 1 
ATOM   4020 C  CD2 . TYR B 1 237 ? -1.20970  -12.13591 59.76233  1.000 55.84620 ? 237 TYR B CD2 1 
ATOM   4021 C  CE1 . TYR B 1 237 ? 1.05565   -11.93840 61.32775  1.000 55.64184 ? 237 TYR B CE1 1 
ATOM   4022 C  CE2 . TYR B 1 237 ? -1.27657  -12.45043 61.11582  1.000 56.56516 ? 237 TYR B CE2 1 
ATOM   4023 C  CZ  . TYR B 1 237 ? -0.13709  -12.34571 61.89193  1.000 62.13260 ? 237 TYR B CZ  1 
ATOM   4024 O  OH  . TYR B 1 237 ? -0.17074  -12.64467 63.24054  1.000 66.97296 ? 237 TYR B OH  1 
ATOM   4025 N  N   . VAL B 1 238 ? -0.30108  -14.53968 57.95710  1.000 59.85537 ? 238 VAL B N   1 
ATOM   4026 C  CA  . VAL B 1 238 ? -1.25380  -15.61813 58.23836  1.000 60.08909 ? 238 VAL B CA  1 
ATOM   4027 C  C   . VAL B 1 238 ? -2.58191  -15.03743 58.72920  1.000 60.61022 ? 238 VAL B C   1 
ATOM   4028 O  O   . VAL B 1 238 ? -3.04991  -15.37688 59.82374  1.000 66.28814 ? 238 VAL B O   1 
ATOM   4029 C  CB  . VAL B 1 238 ? -0.71274  -16.62142 59.28327  1.000 61.91079 ? 238 VAL B CB  1 
ATOM   4030 C  CG1 . VAL B 1 238 ? 0.22540   -17.63132 58.63356  1.000 69.31070 ? 238 VAL B CG1 1 
ATOM   4031 C  CG2 . VAL B 1 238 ? -0.06935  -15.91184 60.46002  1.000 59.99927 ? 238 VAL B CG2 1 
ATOM   4032 N  N   A ASP B 1 249 ? -4.78729  -21.84869 61.27733  0.625 78.00864 ? 249 ASP B N   1 
ATOM   4033 N  N   B ASP B 1 249 ? -4.40007  -21.76765 61.52194  0.375 76.50033 ? 249 ASP B N   1 
ATOM   4034 C  CA  A ASP B 1 249 ? -4.17410  -23.15925 61.08931  0.625 75.52459 ? 249 ASP B CA  1 
ATOM   4035 C  CA  B ASP B 1 249 ? -3.94687  -23.12578 61.24021  0.375 75.62137 ? 249 ASP B CA  1 
ATOM   4036 C  C   A ASP B 1 249 ? -3.19080  -23.16596 59.92655  0.625 75.89024 ? 249 ASP B C   1 
ATOM   4037 C  C   B ASP B 1 249 ? -3.06940  -23.16532 59.99541  0.375 75.83379 ? 249 ASP B C   1 
ATOM   4038 O  O   A ASP B 1 249 ? -2.73581  -22.11637 59.47127  0.625 69.06513 ? 249 ASP B O   1 
ATOM   4039 O  O   B ASP B 1 249 ? -2.59456  -22.13066 59.52672  0.375 69.28209 ? 249 ASP B O   1 
ATOM   4040 C  CB  A ASP B 1 249 ? -5.24252  -24.23253 60.86010  0.625 78.08561 ? 249 ASP B CB  1 
ATOM   4041 C  CB  B ASP B 1 249 ? -5.13885  -24.07014 61.07079  0.375 77.78559 ? 249 ASP B CB  1 
ATOM   4042 C  CG  A ASP B 1 249 ? -6.32431  -24.21678 61.91600  0.625 80.82871 ? 249 ASP B CG  1 
ATOM   4043 C  CG  B ASP B 1 249 ? -5.02228  -25.31222 61.93134  0.375 83.62171 ? 249 ASP B CG  1 
ATOM   4044 O  OD1 A ASP B 1 249 ? -7.18988  -23.31893 61.88195  0.625 78.53538 ? 249 ASP B OD1 1 
ATOM   4045 O  OD1 B ASP B 1 249 ? -5.19050  -25.20386 63.16295  0.375 85.67248 ? 249 ASP B OD1 1 
ATOM   4046 O  OD2 A ASP B 1 249 ? -6.29971  -25.10517 62.78990  0.625 85.60792 ? 249 ASP B OD2 1 
ATOM   4047 O  OD2 B ASP B 1 249 ? -4.75272  -26.39678 61.37625  0.375 86.42205 ? 249 ASP B OD2 1 
ATOM   4048 N  N   . LEU B 1 250 ? -2.84975  -24.37093 59.46550  1.000 81.77395 ? 250 LEU B N   1 
ATOM   4049 C  CA  . LEU B 1 250 ? -2.05349  -24.54508 58.25209  1.000 73.25284 ? 250 LEU B CA  1 
ATOM   4050 C  C   . LEU B 1 250 ? -2.98237  -24.45762 57.05098  1.000 79.23434 ? 250 LEU B C   1 
ATOM   4051 O  O   . LEU B 1 250 ? -3.38372  -25.45380 56.44403  1.000 74.67139 ? 250 LEU B O   1 
ATOM   4052 C  CB  . LEU B 1 250 ? -1.26943  -25.84645 58.27572  1.000 77.56861 ? 250 LEU B CB  1 
ATOM   4053 C  CG  . LEU B 1 250 ? 0.21878   -25.64780 58.56989  1.000 77.03135 ? 250 LEU B CG  1 
ATOM   4054 C  CD1 . LEU B 1 250 ? 0.82840   -24.75928 57.49620  1.000 72.45721 ? 250 LEU B CD1 1 
ATOM   4055 C  CD2 . LEU B 1 250 ? 0.45156   -25.05036 59.95206  1.000 79.84903 ? 250 LEU B CD2 1 
ATOM   4056 N  N   . GLN B 1 251 ? -3.34652  -23.21793 56.73175  1.000 83.68705 ? 251 GLN B N   1 
ATOM   4057 C  CA  . GLN B 1 251 ? -3.83527  -22.88268 55.40639  1.000 81.01470 ? 251 GLN B CA  1 
ATOM   4058 C  C   . GLN B 1 251 ? -2.66811  -22.92093 54.43540  1.000 81.86692 ? 251 GLN B C   1 
ATOM   4059 O  O   . GLN B 1 251 ? -2.16730  -21.87827 53.99761  1.000 80.20430 ? 251 GLN B O   1 
ATOM   4060 C  CB  . GLN B 1 251 ? -4.50599  -21.51579 55.40070  1.000 74.26124 ? 251 GLN B CB  1 
ATOM   4061 C  CG  . GLN B 1 251 ? -5.55467  -21.38143 56.46979  1.000 75.17000 ? 251 GLN B CG  1 
ATOM   4062 C  CD  . GLN B 1 251 ? -6.10507  -19.99066 56.53041  1.000 79.15587 ? 251 GLN B CD  1 
ATOM   4063 O  OE1 . GLN B 1 251 ? -5.63376  -19.10480 55.82184  1.000 73.23511 ? 251 GLN B OE1 1 
ATOM   4064 N  NE2 . GLN B 1 251 ? -7.11018  -19.78149 57.37366  1.000 91.26934 ? 251 GLN B NE2 1 
ATOM   4065 N  N   . LYS B 1 252 ? -2.20115  -24.14166 54.16567  1.000 74.61922 ? 252 LYS B N   1 
ATOM   4066 C  CA  . LYS B 1 252 ? -1.36124  -24.43911 53.01190  1.000 75.65208 ? 252 LYS B CA  1 
ATOM   4067 C  C   . LYS B 1 252 ? -1.91081  -23.83053 51.72998  1.000 72.23167 ? 252 LYS B C   1 
ATOM   4068 O  O   . LYS B 1 252 ? -1.14728  -23.53826 50.80210  1.000 72.98154 ? 252 LYS B O   1 
ATOM   4069 C  CB  . LYS B 1 252 ? -1.25179  -25.96038 52.88938  1.000 77.13563 ? 252 LYS B CB  1 
ATOM   4070 C  CG  . LYS B 1 252 ? -1.52929  -26.52082 51.51200  1.000 81.36842 ? 252 LYS B CG  1 
ATOM   4071 C  CD  . LYS B 1 252 ? -1.42658  -28.04007 51.52577  1.000 87.41210 ? 252 LYS B CD  1 
ATOM   4072 C  CE  . LYS B 1 252 ? -1.76679  -28.64196 50.17073  1.000 80.88664 ? 252 LYS B CE  1 
ATOM   4073 N  NZ  . LYS B 1 252 ? -1.66418  -30.12905 50.18980  1.000 89.44072 ? 252 LYS B NZ  1 
ATOM   4074 N  N   . GLY B 1 253 ? -3.22897  -23.62407 51.66600  1.000 75.43402 ? 253 GLY B N   1 
ATOM   4075 C  CA  . GLY B 1 253 ? -3.85141  -23.14091 50.44673  1.000 69.29641 ? 253 GLY B CA  1 
ATOM   4076 C  C   . GLY B 1 253 ? -3.30032  -21.81887 49.95900  1.000 65.04716 ? 253 GLY B C   1 
ATOM   4077 O  O   . GLY B 1 253 ? -3.25327  -21.57422 48.75143  1.000 65.51864 ? 253 GLY B O   1 
ATOM   4078 N  N   . VAL B 1 254 ? -2.87423  -20.94928 50.87499  1.000 66.19716 ? 254 VAL B N   1 
ATOM   4079 C  CA  . VAL B 1 254 ? -2.34994  -19.66012 50.44307  1.000 59.66744 ? 254 VAL B CA  1 
ATOM   4080 C  C   . VAL B 1 254 ? -1.06598  -19.85093 49.64323  1.000 63.27014 ? 254 VAL B C   1 
ATOM   4081 O  O   . VAL B 1 254 ? -0.92635  -19.30630 48.54191  1.000 59.94404 ? 254 VAL B O   1 
ATOM   4082 C  CB  . VAL B 1 254 ? -2.15291  -18.71701 51.64160  1.000 61.72999 ? 254 VAL B CB  1 
ATOM   4083 C  CG1 . VAL B 1 254 ? -1.15519  -17.62627 51.30379  1.000 47.22643 ? 254 VAL B CG1 1 
ATOM   4084 C  CG2 . VAL B 1 254 ? -3.48036  -18.08322 52.02546  1.000 61.02339 ? 254 VAL B CG2 1 
ATOM   4085 N  N   . MET B 1 255 ? -0.13386  -20.66955 50.15154  1.000 63.45190 ? 255 MET B N   1 
ATOM   4086 C  CA  . MET B 1 255 ? 1.15383   -20.82120 49.46986  1.000 61.92800 ? 255 MET B CA  1 
ATOM   4087 C  C   . MET B 1 255 ? 1.00533   -21.44158 48.08195  1.000 60.93653 ? 255 MET B C   1 
ATOM   4088 O  O   . MET B 1 255 ? 1.64885   -20.98737 47.12702  1.000 61.08927 ? 255 MET B O   1 
ATOM   4089 C  CB  . MET B 1 255 ? 2.13996   -21.63633 50.30943  1.000 63.96125 ? 255 MET B CB  1 
ATOM   4090 C  CG  . MET B 1 255 ? 1.97950   -21.55744 51.82308  1.000 61.91120 ? 255 MET B CG  1 
ATOM   4091 S  SD  . MET B 1 255 ? 3.31112   -22.48438 52.61267  1.000 61.39383 ? 255 MET B SD  1 
ATOM   4092 C  CE  . MET B 1 255 ? 4.73749   -21.57211 52.05544  1.000 58.50595 ? 255 MET B CE  1 
ATOM   4093 N  N   . GLU B 1 256 ? 0.17484   -22.47850 47.93789  1.000 57.98627 ? 256 GLU B N   1 
ATOM   4094 C  CA  . GLU B 1 256 ? -0.02364  -23.03029 46.59833  1.000 59.68894 ? 256 GLU B CA  1 
ATOM   4095 C  C   . GLU B 1 256 ? -0.72611  -22.03932 45.67808  1.000 59.36261 ? 256 GLU B C   1 
ATOM   4096 O  O   . GLU B 1 256 ? -0.52571  -22.07297 44.45800  1.000 56.83880 ? 256 GLU B O   1 
ATOM   4097 C  CB  . GLU B 1 256 ? -0.81598  -24.33387 46.65723  1.000 68.37733 ? 256 GLU B CB  1 
ATOM   4098 C  CG  . GLU B 1 256 ? -2.09664  -24.26665 47.46705  1.000 66.72669 ? 256 GLU B CG  1 
ATOM   4099 C  CD  . GLU B 1 256 ? -3.01121  -25.44800 47.19485  1.000 74.03444 ? 256 GLU B CD  1 
ATOM   4100 O  OE1 . GLU B 1 256 ? -3.73908  -25.40068 46.17825  1.000 73.46849 ? 256 GLU B OE1 1 
ATOM   4101 O  OE2 . GLU B 1 256 ? -2.98346  -26.42879 47.98071  1.000 78.86806 ? 256 GLU B OE2 1 
ATOM   4102 N  N   . ARG B 1 257 ? -1.54576  -21.15324 46.23853  1.000 57.90928 ? 257 ARG B N   1 
ATOM   4103 C  CA  . ARG B 1 257 ? -2.28640  -20.21541 45.40514  1.000 62.12123 ? 257 ARG B CA  1 
ATOM   4104 C  C   . ARG B 1 257 ? -1.38845  -19.09810 44.89003  1.000 54.63919 ? 257 ARG B C   1 
ATOM   4105 O  O   . ARG B 1 257 ? -1.57712  -18.62321 43.76553  1.000 58.19810 ? 257 ARG B O   1 
ATOM   4106 C  CB  . ARG B 1 257 ? -3.47713  -19.65527 46.17793  1.000 55.91094 ? 257 ARG B CB  1 
ATOM   4107 C  CG  . ARG B 1 257 ? -4.71299  -20.53038 46.08909  1.000 56.81483 ? 257 ARG B CG  1 
ATOM   4108 C  CD  . ARG B 1 257 ? -5.88030  -19.85461 46.74589  1.000 58.39594 ? 257 ARG B CD  1 
ATOM   4109 N  NE  . ARG B 1 257 ? -5.76681  -19.92449 48.19533  1.000 62.92649 ? 257 ARG B NE  1 
ATOM   4110 C  CZ  . ARG B 1 257 ? -6.58786  -19.31213 49.03526  1.000 65.97458 ? 257 ARG B CZ  1 
ATOM   4111 N  NH1 . ARG B 1 257 ? -7.60362  -18.58583 48.59753  1.000 67.10154 ? 257 ARG B NH1 1 
ATOM   4112 N  NH2 . ARG B 1 257 ? -6.38181  -19.42650 50.34593  1.000 62.41513 ? 257 ARG B NH2 1 
ATOM   4113 N  N   . LEU B 1 258 ? -0.41399  -18.65347 45.69263  1.000 55.79278 ? 258 LEU B N   1 
ATOM   4114 C  CA  . LEU B 1 258 ? 0.63454   -17.79559 45.14213  1.000 57.58389 ? 258 LEU B CA  1 
ATOM   4115 C  C   . LEU B 1 258 ? 1.37396   -18.48706 44.00279  1.000 56.07621 ? 258 LEU B C   1 
ATOM   4116 O  O   . LEU B 1 258 ? 1.73264   -17.84716 43.00892  1.000 53.37313 ? 258 LEU B O   1 
ATOM   4117 C  CB  . LEU B 1 258 ? 1.63818   -17.36776 46.21697  1.000 51.66231 ? 258 LEU B CB  1 
ATOM   4118 C  CG  . LEU B 1 258 ? 1.32556   -16.30675 47.27546  1.000 50.00459 ? 258 LEU B CG  1 
ATOM   4119 C  CD1 . LEU B 1 258 ? 0.54093   -15.13746 46.67461  1.000 48.58233 ? 258 LEU B CD1 1 
ATOM   4120 C  CD2 . LEU B 1 258 ? 0.65813   -16.84465 48.48950  1.000 48.69746 ? 258 LEU B CD2 1 
ATOM   4121 N  N   . ARG B 1 259 ? 1.61990   -19.79296 44.13303  1.000 53.24907 ? 259 ARG B N   1 
ATOM   4122 C  CA  . ARG B 1 259 ? 2.36985   -20.50163 43.10229  1.000 56.26071 ? 259 ARG B CA  1 
ATOM   4123 C  C   . ARG B 1 259 ? 1.53854   -20.71842 41.84886  1.000 55.52442 ? 259 ARG B C   1 
ATOM   4124 O  O   . ARG B 1 259 ? 2.08241   -20.70090 40.73913  1.000 59.71520 ? 259 ARG B O   1 
ATOM   4125 C  CB  . ARG B 1 259 ? 2.86788   -21.84503 43.63777  1.000 60.44382 ? 259 ARG B CB  1 
ATOM   4126 C  CG  . ARG B 1 259 ? 4.22860   -21.77762 44.31251  1.000 62.31130 ? 259 ARG B CG  1 
ATOM   4127 C  CD  . ARG B 1 259 ? 4.71512   -23.16028 44.73515  1.000 60.99968 ? 259 ARG B CD  1 
ATOM   4128 N  NE  . ARG B 1 259 ? 5.16956   -23.14980 46.11961  1.000 61.96740 ? 259 ARG B NE  1 
ATOM   4129 C  CZ  . ARG B 1 259 ? 4.63386   -23.88167 47.08693  1.000 63.55910 ? 259 ARG B CZ  1 
ATOM   4130 N  NH1 . ARG B 1 259 ? 3.62231   -24.70245 46.85148  1.000 67.80523 ? 259 ARG B NH1 1 
ATOM   4131 N  NH2 . ARG B 1 259 ? 5.12168   -23.78381 48.32076  1.000 63.39899 ? 259 ARG B NH2 1 
ATOM   4132 N  N   . ARG B 1 260 ? 0.23102   -20.93951 41.99950  1.000 55.11259 ? 260 ARG B N   1 
ATOM   4133 C  CA  . ARG B 1 260 ? -0.61111  -21.13836 40.82644  1.000 55.78396 ? 260 ARG B CA  1 
ATOM   4134 C  C   . ARG B 1 260 ? -0.69281  -19.86954 39.98335  1.000 55.64016 ? 260 ARG B C   1 
ATOM   4135 O  O   . ARG B 1 260 ? -0.65624  -19.93809 38.75114  1.000 60.48643 ? 260 ARG B O   1 
ATOM   4136 C  CB  . ARG B 1 260 ? -2.00334  -21.60153 41.25088  1.000 60.15751 ? 260 ARG B CB  1 
ATOM   4137 C  CG  . ARG B 1 260 ? -2.93803  -21.87518 40.08744  1.000 66.33017 ? 260 ARG B CG  1 
ATOM   4138 C  CD  . ARG B 1 260 ? -4.19969  -22.56356 40.55285  1.000 68.99941 ? 260 ARG B CD  1 
ATOM   4139 N  NE  . ARG B 1 260 ? -4.01130  -23.17700 41.86081  1.000 71.14378 ? 260 ARG B NE  1 
ATOM   4140 C  CZ  . ARG B 1 260 ? -4.81007  -22.98279 42.90051  1.000 71.43383 ? 260 ARG B CZ  1 
ATOM   4141 N  NH1 . ARG B 1 260 ? -5.85528  -22.17217 42.82862  1.000 69.81252 ? 260 ARG B NH1 1 
ATOM   4142 N  NH2 . ARG B 1 260 ? -4.55445  -23.61776 44.04101  1.000 71.87392 ? 260 ARG B NH2 1 
ATOM   4143 N  N   . VAL B 1 261 ? -0.78979  -18.69976 40.62141  1.000 54.82893 ? 261 VAL B N   1 
ATOM   4144 C  CA  . VAL B 1 261 ? -0.82167  -17.45029 39.86815  1.000 50.44352 ? 261 VAL B CA  1 
ATOM   4145 C  C   . VAL B 1 261 ? 0.54836   -17.06146 39.32815  1.000 57.07792 ? 261 VAL B C   1 
ATOM   4146 O  O   . VAL B 1 261 ? 0.64111   -16.11407 38.53941  1.000 55.51340 ? 261 VAL B O   1 
ATOM   4147 C  CB  . VAL B 1 261 ? -1.40486  -16.30109 40.71546  1.000 45.76550 ? 261 VAL B CB  1 
ATOM   4148 C  CG1 . VAL B 1 261 ? -2.74535  -16.69983 41.29006  1.000 57.97661 ? 261 VAL B CG1 1 
ATOM   4149 C  CG2 . VAL B 1 261 ? -0.45940  -15.90763 41.82975  1.000 52.20598 ? 261 VAL B CG2 1 
ATOM   4150 N  N   . GLY B 1 262 ? 1.61255   -17.76223 39.72728  1.000 57.72227 ? 262 GLY B N   1 
ATOM   4151 C  CA  . GLY B 1 262 ? 2.92582   -17.60636 39.11568  1.000 49.43604 ? 262 GLY B CA  1 
ATOM   4152 C  C   . GLY B 1 262 ? 4.07754   -17.30129 40.05780  1.000 53.53819 ? 262 GLY B C   1 
ATOM   4153 O  O   . GLY B 1 262 ? 5.22899   -17.27602 39.59894  1.000 53.75472 ? 262 GLY B O   1 
ATOM   4154 N  N   . PHE B 1 263 ? 3.84535   -17.05890 41.34416  1.000 57.46885 ? 263 PHE B N   1 
ATOM   4155 C  CA  . PHE B 1 263 ? 4.93538   -16.69736 42.24679  1.000 55.92307 ? 263 PHE B CA  1 
ATOM   4156 C  C   . PHE B 1 263 ? 5.92000   -17.85033 42.41682  1.000 57.36149 ? 263 PHE B C   1 
ATOM   4157 O  O   . PHE B 1 263 ? 5.55734   -19.02753 42.35261  1.000 56.55012 ? 263 PHE B O   1 
ATOM   4158 C  CB  . PHE B 1 263 ? 4.38724   -16.28959 43.61989  1.000 50.57539 ? 263 PHE B CB  1 
ATOM   4159 C  CG  . PHE B 1 263 ? 3.78242   -14.91407 43.64745  1.000 52.72067 ? 263 PHE B CG  1 
ATOM   4160 C  CD1 . PHE B 1 263 ? 4.58963   -13.79702 43.72116  1.000 44.08977 ? 263 PHE B CD1 1 
ATOM   4161 C  CD2 . PHE B 1 263 ? 2.40412   -14.74229 43.59035  1.000 47.56961 ? 263 PHE B CD2 1 
ATOM   4162 C  CE1 . PHE B 1 263 ? 4.03014   -12.53609 43.73997  1.000 48.84863 ? 263 PHE B CE1 1 
ATOM   4163 C  CE2 . PHE B 1 263 ? 1.84413   -13.49385 43.61450  1.000 42.35960 ? 263 PHE B CE2 1 
ATOM   4164 C  CZ  . PHE B 1 263 ? 2.65237   -12.38459 43.69181  1.000 43.06892 ? 263 PHE B CZ  1 
ATOM   4165 N  N   . VAL B 1 264 ? 7.18286   -17.50254 42.65537  1.000 58.16757 ? 264 VAL B N   1 
ATOM   4166 C  CA  . VAL B 1 264 ? 8.22302   -18.48877 42.91292  1.000 58.22286 ? 264 VAL B CA  1 
ATOM   4167 C  C   . VAL B 1 264 ? 8.92482   -18.14501 44.22277  1.000 54.87696 ? 264 VAL B C   1 
ATOM   4168 O  O   . VAL B 1 264 ? 8.73754   -17.06693 44.79844  1.000 56.00171 ? 264 VAL B O   1 
ATOM   4169 C  CB  . VAL B 1 264 ? 9.24021   -18.58740 41.76149  1.000 54.97443 ? 264 VAL B CB  1 
ATOM   4170 C  CG1 . VAL B 1 264 ? 8.53593   -18.96183 40.48616  1.000 56.22306 ? 264 VAL B CG1 1 
ATOM   4171 C  CG2 . VAL B 1 264 ? 9.99577   -17.28186 41.59915  1.000 55.14244 ? 264 VAL B CG2 1 
ATOM   4172 N  N   . GLY B 1 265 ? 9.74330   -19.09307 44.68606  1.000 55.63006 ? 265 GLY B N   1 
ATOM   4173 C  CA  . GLY B 1 265 ? 10.38481  -19.00084 45.98129  1.000 56.13093 ? 265 GLY B CA  1 
ATOM   4174 C  C   . GLY B 1 265 ? 9.37227   -18.82567 47.09122  1.000 60.49086 ? 265 GLY B C   1 
ATOM   4175 O  O   . GLY B 1 265 ? 9.54337   -17.97439 47.97353  1.000 60.43286 ? 265 GLY B O   1 
ATOM   4176 N  N   . VAL B 1 266 ? 8.30376   -19.61829 47.05633  1.000 56.73302 ? 266 VAL B N   1 
ATOM   4177 C  CA  . VAL B 1 266 ? 7.16875   -19.42701 47.95330  1.000 53.23204 ? 266 VAL B CA  1 
ATOM   4178 C  C   . VAL B 1 266 ? 7.40761   -20.32744 49.16495  1.000 63.00661 ? 266 VAL B C   1 
ATOM   4179 O  O   . VAL B 1 266 ? 7.15867   -21.53536 49.12069  1.000 60.11641 ? 266 VAL B O   1 
ATOM   4180 C  CB  . VAL B 1 266 ? 5.84360   -19.73750 47.25277  1.000 55.10051 ? 266 VAL B CB  1 
ATOM   4181 C  CG1 . VAL B 1 266 ? 4.71131   -19.92891 48.26411  1.000 63.03102 ? 266 VAL B CG1 1 
ATOM   4182 C  CG2 . VAL B 1 266 ? 5.51315   -18.66891 46.22652  1.000 49.90397 ? 266 VAL B CG2 1 
ATOM   4183 N  N   . ARG B 1 267 ? 7.92615   -19.74436 50.24610  1.000 67.12867 ? 267 ARG B N   1 
ATOM   4184 C  CA  . ARG B 1 267 ? 8.20148   -20.48091 51.47391  1.000 67.47902 ? 267 ARG B CA  1 
ATOM   4185 C  C   . ARG B 1 267 ? 7.78069   -19.62243 52.65282  1.000 65.20420 ? 267 ARG B C   1 
ATOM   4186 O  O   . ARG B 1 267 ? 7.61434   -18.40678 52.52734  1.000 64.67591 ? 267 ARG B O   1 
ATOM   4187 C  CB  . ARG B 1 267 ? 9.68403   -20.87813 51.60341  1.000 75.28576 ? 267 ARG B CB  1 
ATOM   4188 C  CG  . ARG B 1 267 ? 10.67166  -19.91507 50.94919  1.000 77.54395 ? 267 ARG B CG  1 
ATOM   4189 C  CD  . ARG B 1 267 ? 11.30900  -18.96205 51.95820  1.000 84.94884 ? 267 ARG B CD  1 
ATOM   4190 N  NE  . ARG B 1 267 ? 12.11713  -17.94147 51.29766  1.000 86.64930 ? 267 ARG B NE  1 
ATOM   4191 C  CZ  . ARG B 1 267 ? 12.48089  -16.79044 51.84847  1.000 87.04168 ? 267 ARG B CZ  1 
ATOM   4192 N  NH1 . ARG B 1 267 ? 12.17788  -16.49737 53.10240  1.000 86.64807 ? 267 ARG B NH1 1 
ATOM   4193 N  NH2 . ARG B 1 267 ? 13.17851  -15.91728 51.12621  1.000 82.53428 ? 267 ARG B NH2 1 
ATOM   4194 N  N   . ARG B 1 268 ? 7.60844   -20.25441 53.80967  1.000 65.13694 ? 268 ARG B N   1 
ATOM   4195 C  CA  . ARG B 1 268 ? 7.04694   -19.52066 54.93178  1.000 73.86414 ? 268 ARG B CA  1 
ATOM   4196 C  C   . ARG B 1 268 ? 8.12814   -19.13333 55.93351  1.000 68.32823 ? 268 ARG B C   1 
ATOM   4197 O  O   . ARG B 1 268 ? 9.13826   -19.82190 56.08783  1.000 67.27174 ? 268 ARG B O   1 
ATOM   4198 C  CB  . ARG B 1 268 ? 5.91366   -20.30382 55.61407  1.000 69.70761 ? 268 ARG B CB  1 
ATOM   4199 C  CG  . ARG B 1 268 ? 6.20453   -21.08199 56.88292  1.000 69.53273 ? 268 ARG B CG  1 
ATOM   4200 C  CD  . ARG B 1 268 ? 6.63822   -22.51965 56.67268  1.000 75.72625 ? 268 ARG B CD  1 
ATOM   4201 N  NE  . ARG B 1 268 ? 6.52652   -23.23138 57.94206  1.000 76.90421 ? 268 ARG B NE  1 
ATOM   4202 C  CZ  . ARG B 1 268 ? 6.92505   -24.47674 58.16322  1.000 81.48635 ? 268 ARG B CZ  1 
ATOM   4203 N  NH1 . ARG B 1 268 ? 7.44633   -25.22012 57.20082  1.000 86.83559 ? 268 ARG B NH1 1 
ATOM   4204 N  NH2 . ARG B 1 268 ? 6.79801   -24.98962 59.38385  1.000 85.67771 ? 268 ARG B NH2 1 
ATOM   4205 N  N   . VAL B 1 269 ? 7.92022   -17.98646 56.57773  1.000 62.42087 ? 269 VAL B N   1 
ATOM   4206 C  CA  . VAL B 1 269 ? 8.81982   -17.46713 57.60075  1.000 67.63497 ? 269 VAL B CA  1 
ATOM   4207 C  C   . VAL B 1 269 ? 8.09723   -17.52118 58.93445  1.000 72.43757 ? 269 VAL B C   1 
ATOM   4208 O  O   . VAL B 1 269 ? 6.97113   -17.02433 59.06057  1.000 71.92566 ? 269 VAL B O   1 
ATOM   4209 C  CB  . VAL B 1 269 ? 9.28003   -16.03023 57.29541  1.000 76.27684 ? 269 VAL B CB  1 
ATOM   4210 C  CG1 . VAL B 1 269 ? 10.55603  -15.70778 58.08285  1.000 75.22424 ? 269 VAL B CG1 1 
ATOM   4211 C  CG2 . VAL B 1 269 ? 9.49179   -15.83432 55.79389  1.000 67.42617 ? 269 VAL B CG2 1 
ATOM   4212 N  N   . GLU B 1 270 ? 8.75239   -18.10562 59.93233  1.000 77.62119 ? 270 GLU B N   1 
ATOM   4213 C  CA  . GLU B 1 270 ? 8.10245   -18.29477 61.21996  1.000 82.30339 ? 270 GLU B CA  1 
ATOM   4214 C  C   . GLU B 1 270 ? 8.12281   -17.02205 62.05373  1.000 67.66454 ? 270 GLU B C   1 
ATOM   4215 O  O   . GLU B 1 270 ? 7.10087   -16.64890 62.63891  1.000 61.70942 ? 270 GLU B O   1 
ATOM   4216 C  CB  . GLU B 1 270 ? 8.77494   -19.44153 61.97804  1.000 89.09490 ? 270 GLU B CB  1 
ATOM   4217 C  CG  . GLU B 1 270 ? 8.20427   -20.79915 61.62655  1.000 88.28001 ? 270 GLU B CG  1 
ATOM   4218 C  CD  . GLU B 1 270 ? 6.73123   -20.89879 61.97928  1.000 94.10513 ? 270 GLU B CD  1 
ATOM   4219 O  OE1 . GLU B 1 270 ? 6.39492   -20.76987 63.18123  1.000 91.53850 ? 270 GLU B OE1 1 
ATOM   4220 O  OE2 . GLU B 1 270 ? 5.91148   -21.08060 61.04779  1.000 90.27684 ? 270 GLU B OE2 1 
ATOM   4221 N  N   . GLU B 1 271 ? 9.27067   -16.33908 62.09850  1.000 73.15719 ? 271 GLU B N   1 
ATOM   4222 C  CA  . GLU B 1 271 ? 9.46307   -15.24891 63.04915  1.000 77.32720 ? 271 GLU B CA  1 
ATOM   4223 C  C   . GLU B 1 271 ? 8.44007   -14.13701 62.86230  1.000 75.62217 ? 271 GLU B C   1 
ATOM   4224 O  O   . GLU B 1 271 ? 8.14321   -13.40288 63.81238  1.000 78.71097 ? 271 GLU B O   1 
ATOM   4225 C  CB  . GLU B 1 271 ? 10.88341  -14.69727 62.92305  1.000 82.98686 ? 271 GLU B CB  1 
ATOM   4226 C  CG  . GLU B 1 271 ? 11.24117  -13.64434 63.96706  1.000 86.91997 ? 271 GLU B CG  1 
ATOM   4227 C  CD  . GLU B 1 271 ? 12.64433  -13.10916 63.78396  1.000 87.40514 ? 271 GLU B CD  1 
ATOM   4228 O  OE1 . GLU B 1 271 ? 12.97502  -12.70309 62.64566  1.000 88.84184 ? 271 GLU B OE1 1 
ATOM   4229 O  OE2 . GLU B 1 271 ? 13.40995  -13.09673 64.77371  1.000 78.76483 ? 271 GLU B OE2 1 
ATOM   4230 N  N   . ALA B 1 272 ? 7.88664   -13.99913 61.65975  1.000 72.09472 ? 272 ALA B N   1 
ATOM   4231 C  CA  . ALA B 1 272 ? 6.82746   -13.03455 61.39821  1.000 64.36109 ? 272 ALA B CA  1 
ATOM   4232 C  C   . ALA B 1 272 ? 5.48428   -13.69159 61.11750  1.000 59.76250 ? 272 ALA B C   1 
ATOM   4233 O  O   . ALA B 1 272 ? 4.50594   -12.97954 60.86522  1.000 60.83513 ? 272 ALA B O   1 
ATOM   4234 C  CB  . ALA B 1 272 ? 7.21170   -12.13255 60.22106  1.000 57.95043 ? 272 ALA B CB  1 
ATOM   4235 N  N   . LEU B 1 273 ? 5.41413   -15.02361 61.15723  1.000 62.45765 ? 273 LEU B N   1 
ATOM   4236 C  CA  . LEU B 1 273 ? 4.20709   -15.78799 60.82883  1.000 66.85651 ? 273 LEU B CA  1 
ATOM   4237 C  C   . LEU B 1 273 ? 3.61814   -15.33679 59.48990  1.000 61.10048 ? 273 LEU B C   1 
ATOM   4238 O  O   . LEU B 1 273 ? 2.51451   -14.80305 59.40726  1.000 56.51617 ? 273 LEU B O   1 
ATOM   4239 C  CB  . LEU B 1 273 ? 3.16331   -15.70003 61.94958  1.000 66.24591 ? 273 LEU B CB  1 
ATOM   4240 C  CG  . LEU B 1 273 ? 3.56564   -15.93872 63.41344  1.000 64.53808 ? 273 LEU B CG  1 
ATOM   4241 C  CD1 . LEU B 1 273 ? 4.07153   -14.66066 64.09637  1.000 61.14668 ? 273 LEU B CD1 1 
ATOM   4242 C  CD2 . LEU B 1 273 ? 2.40196   -16.54860 64.19090  1.000 60.31864 ? 273 LEU B CD2 1 
ATOM   4243 N  N   . GLY B 1 274 ? 4.38425   -15.55880 58.42889  1.000 60.33936 ? 274 GLY B N   1 
ATOM   4244 C  CA  . GLY B 1 274 ? 3.92140   -15.17654 57.11168  1.000 55.51026 ? 274 GLY B CA  1 
ATOM   4245 C  C   . GLY B 1 274 ? 4.59530   -15.99714 56.03621  1.000 58.35342 ? 274 GLY B C   1 
ATOM   4246 O  O   . GLY B 1 274 ? 5.45694   -16.83743 56.30510  1.000 61.38639 ? 274 GLY B O   1 
ATOM   4247 N  N   . VAL B 1 275 ? 4.17632   -15.73632 54.80009  1.000 59.06751 ? 275 VAL B N   1 
ATOM   4248 C  CA  . VAL B 1 275 ? 4.73304   -16.35578 53.60453  1.000 55.05005 ? 275 VAL B CA  1 
ATOM   4249 C  C   . VAL B 1 275 ? 5.42666   -15.26940 52.80152  1.000 49.06633 ? 275 VAL B C   1 
ATOM   4250 O  O   . VAL B 1 275 ? 4.91217   -14.15312 52.69232  1.000 52.90651 ? 275 VAL B O   1 
ATOM   4251 C  CB  . VAL B 1 275 ? 3.63317   -17.04026 52.76856  1.000 55.03344 ? 275 VAL B CB  1 
ATOM   4252 C  CG1 . VAL B 1 275 ? 4.17926   -17.51001 51.42991  1.000 60.29533 ? 275 VAL B CG1 1 
ATOM   4253 C  CG2 . VAL B 1 275 ? 3.03434   -18.20571 53.53864  1.000 51.72790 ? 275 VAL B CG2 1 
ATOM   4254 N  N   . VAL B 1 276 ? 6.59815   -15.58403 52.26042  1.000 49.08265 ? 276 VAL B N   1 
ATOM   4255 C  CA  . VAL B 1 276 ? 7.34513   -14.66861 51.40862  1.000 52.97777 ? 276 VAL B CA  1 
ATOM   4256 C  C   . VAL B 1 276 ? 7.42058   -15.27858 50.01520  1.000 55.61801 ? 276 VAL B C   1 
ATOM   4257 O  O   . VAL B 1 276 ? 7.54299   -16.49949 49.87489  1.000 60.84971 ? 276 VAL B O   1 
ATOM   4258 C  CB  . VAL B 1 276 ? 8.74923   -14.38521 51.98885  1.000 63.89239 ? 276 VAL B CB  1 
ATOM   4259 C  CG1 . VAL B 1 276 ? 9.75101   -14.02097 50.89169  1.000 68.66126 ? 276 VAL B CG1 1 
ATOM   4260 C  CG2 . VAL B 1 276 ? 8.67689   -13.28304 53.04858  1.000 53.09039 ? 276 VAL B CG2 1 
ATOM   4261 N  N   . ALA B 1 277 ? 7.32726   -14.43655 48.98677  1.000 55.30721 ? 277 ALA B N   1 
ATOM   4262 C  CA  . ALA B 1 277 ? 7.23884   -14.92618 47.61939  1.000 54.89138 ? 277 ALA B CA  1 
ATOM   4263 C  C   . ALA B 1 277 ? 7.97271   -13.97457 46.69184  1.000 56.78808 ? 277 ALA B C   1 
ATOM   4264 O  O   . ALA B 1 277 ? 8.15913   -12.79461 47.00407  1.000 52.34918 ? 277 ALA B O   1 
ATOM   4265 C  CB  . ALA B 1 277 ? 5.78335   -15.07326 47.17301  1.000 47.93201 ? 277 ALA B CB  1 
ATOM   4266 N  N   . ARG B 1 278 ? 8.36818   -14.50044 45.53073  1.000 54.97469 ? 278 ARG B N   1 
ATOM   4267 C  CA  . ARG B 1 278 ? 9.11138   -13.74500 44.53022  1.000 61.22867 ? 278 ARG B CA  1 
ATOM   4268 C  C   . ARG B 1 278 ? 8.35937   -13.73579 43.20076  1.000 62.30452 ? 278 ARG B C   1 
ATOM   4269 O  O   . ARG B 1 278 ? 7.74858   -14.73692 42.81246  1.000 62.19825 ? 278 ARG B O   1 
ATOM   4270 C  CB  . ARG B 1 278 ? 10.51721  -14.34993 44.33201  1.000 65.87502 ? 278 ARG B CB  1 
ATOM   4271 C  CG  . ARG B 1 278 ? 11.68946  -13.43269 44.68258  1.000 66.30583 ? 278 ARG B CG  1 
ATOM   4272 C  CD  . ARG B 1 278 ? 12.03950  -13.59611 46.14838  1.000 72.44546 ? 278 ARG B CD  1 
ATOM   4273 N  NE  . ARG B 1 278 ? 12.98253  -12.60233 46.64736  1.000 71.53690 ? 278 ARG B NE  1 
ATOM   4274 C  CZ  . ARG B 1 278 ? 13.13897  -12.30937 47.93398  1.000 83.13057 ? 278 ARG B CZ  1 
ATOM   4275 N  NH1 . ARG B 1 278 ? 12.36190  -12.84354 48.86513  1.000 74.55510 ? 278 ARG B NH1 1 
ATOM   4276 N  NH2 . ARG B 1 278 ? 14.08852  -11.44887 48.29549  1.000 81.60149 ? 278 ARG B NH2 1 
ATOM   4277 N  N   . LYS B 1 279 ? 8.39958   -12.60309 42.50537  1.000 56.59146 ? 279 LYS B N   1 
ATOM   4278 C  CA  . LYS B 1 279 ? 7.91430   -12.72559 41.13434  1.000 58.30392 ? 279 LYS B CA  1 
ATOM   4279 C  C   . LYS B 1 279 ? 9.06466   -13.13952 40.21600  1.000 56.06409 ? 279 LYS B C   1 
ATOM   4280 O  O   . LYS B 1 279 ? 10.18404  -12.64758 40.37764  1.000 56.38048 ? 279 LYS B O   1 
ATOM   4281 C  CB  . LYS B 1 279 ? 7.31565   -11.40545 40.65319  1.000 51.61610 ? 279 LYS B CB  1 
ATOM   4282 C  CG  . LYS B 1 279 ? 6.76709   -11.44660 39.22484  1.000 53.38011 ? 279 LYS B CG  1 
ATOM   4283 C  CD  . LYS B 1 279 ? 6.28061   -10.07605 38.78973  1.000 48.31110 ? 279 LYS B CD  1 
ATOM   4284 C  CE  . LYS B 1 279 ? 5.44572   -10.17064 37.53172  1.000 40.98078 ? 279 LYS B CE  1 
ATOM   4285 N  NZ  . LYS B 1 279 ? 4.38179   -9.13179  37.51061  1.000 42.62151 ? 279 LYS B NZ  1 
ATOM   4286 N  N   . PRO B 1 280 ? 8.83993   -14.05906 39.24543  1.000 57.64256 ? 280 PRO B N   1 
ATOM   4287 C  CA  . PRO B 1 280 ? 9.96323   -14.59221 38.44894  1.000 55.13539 ? 280 PRO B CA  1 
ATOM   4288 C  C   . PRO B 1 280 ? 10.64992  -13.56789 37.56085  1.000 62.05792 ? 280 PRO B C   1 
ATOM   4289 O  O   . PRO B 1 280 ? 10.22964  -12.40783 37.49252  1.000 62.39553 ? 280 PRO B O   1 
ATOM   4290 C  CB  . PRO B 1 280 ? 9.31215   -15.68955 37.59308  1.000 52.92497 ? 280 PRO B CB  1 
ATOM   4291 C  CG  . PRO B 1 280 ? 7.98685   -15.95301 38.19271  1.000 53.94219 ? 280 PRO B CG  1 
ATOM   4292 C  CD  . PRO B 1 280 ? 7.56858   -14.73919 38.94730  1.000 55.79153 ? 280 PRO B CD  1 
ATOM   4293 N  N   . GLU B 1 281 ? 11.68893  -14.01308 36.85234  1.000 64.70058 ? 281 GLU B N   1 
ATOM   4294 C  CA  . GLU B 1 281 ? 12.48438  -13.16625 35.95790  1.000 66.16176 ? 281 GLU B CA  1 
ATOM   4295 C  C   . GLU B 1 281 ? 13.00489  -11.93244 36.68379  1.000 64.22744 ? 281 GLU B C   1 
ATOM   4296 O  O   . GLU B 1 281 ? 13.31899  -11.99565 37.87218  1.000 66.25552 ? 281 GLU B O   1 
ATOM   4297 C  CB  . GLU B 1 281 ? 11.67876  -12.74405 34.72014  1.000 68.66986 ? 281 GLU B CB  1 
ATOM   4298 C  CG  . GLU B 1 281 ? 11.00158  -13.88723 33.96701  1.000 67.12436 ? 281 GLU B CG  1 
ATOM   4299 C  CD  . GLU B 1 281 ? 11.31590  -13.87623 32.47745  1.000 76.19982 ? 281 GLU B CD  1 
ATOM   4300 O  OE1 . GLU B 1 281 ? 10.57691  -13.21987 31.71238  1.000 72.60491 ? 281 GLU B OE1 1 
ATOM   4301 O  OE2 . GLU B 1 281 ? 12.30365  -14.52968 32.06886  1.000 70.45553 ? 281 GLU B OE2 1 
HETATM 4302 NA NA  . NA  C 2 .   ? -1.46331  -0.64391  12.49906  1.000 32.02733 ? 301 NA  A NA  1 
HETATM 4303 NA NA  . NA  D 2 .   ? 7.81409   -0.03333  17.44758  1.000 35.28338 ? 302 NA  A NA  1 
HETATM 4304 NA NA  . NA  E 2 .   ? 0.46047   0.62334   16.06179  1.000 43.41729 ? 303 NA  A NA  1 
HETATM 4305 NA NA  . NA  F 2 .   ? -12.00393 5.11737   8.13157   1.000 46.61860 ? 304 NA  A NA  1 
HETATM 4306 NA NA  . NA  G 2 .   ? -0.50916  20.68676  32.68784  1.000 60.58742 ? 305 NA  A NA  1 
HETATM 4307 NA NA  . NA  H 2 .   ? 9.48201   -10.79090 1.05462   1.000 49.39673 ? 306 NA  A NA  1 
HETATM 4308 O  O   . HOH I 3 .   ? -16.51284 -10.30342 10.21540  1.000 43.19821 ? 401 HOH A O   1 
HETATM 4309 O  O   . HOH I 3 .   ? 11.99419  5.19064   32.91428  1.000 45.81007 ? 402 HOH A O   1 
HETATM 4310 O  O   . HOH I 3 .   ? -12.62396 2.20651   1.09013   1.000 39.96125 ? 403 HOH A O   1 
HETATM 4311 O  O   . HOH I 3 .   ? 10.11578  -1.21092  16.75283  1.000 33.51981 ? 404 HOH A O   1 
HETATM 4312 O  O   . HOH I 3 .   ? -0.28058  4.15660   41.89141  1.000 35.74940 ? 405 HOH A O   1 
HETATM 4313 O  O   . HOH I 3 .   ? 23.64166  18.34181  34.17962  1.000 62.32243 ? 406 HOH A O   1 
HETATM 4314 O  O   . HOH I 3 .   ? 4.88282   -9.48049  30.62987  1.000 57.46050 ? 407 HOH A O   1 
HETATM 4315 O  O   . HOH I 3 .   ? 2.59145   -15.43236 7.68817   1.000 37.59096 ? 408 HOH A O   1 
HETATM 4316 O  O   . HOH I 3 .   ? -11.05719 8.49676   -1.56098  1.000 41.34665 ? 409 HOH A O   1 
HETATM 4317 O  O   . HOH I 3 .   ? 18.14246  -1.02409  1.45821   1.000 42.12792 ? 410 HOH A O   1 
HETATM 4318 O  O   . HOH I 3 .   ? 18.071    -4.145    -1.217    1.000 32.89995 ? 411 HOH A O   1 
HETATM 4319 O  O   . HOH I 3 .   ? -1.34563  -1.96230  14.65340  1.000 41.70767 ? 412 HOH A O   1 
HETATM 4320 O  O   . HOH I 3 .   ? 0.40862   1.98600   39.00775  1.000 38.60589 ? 413 HOH A O   1 
HETATM 4321 O  O   . HOH I 3 .   ? 7.44547   -3.59654  -7.33188  1.000 49.63029 ? 414 HOH A O   1 
HETATM 4322 O  O   . HOH I 3 .   ? -10.91815 -8.87172  19.50991  1.000 49.23795 ? 415 HOH A O   1 
HETATM 4323 O  O   . HOH I 3 .   ? -8.46086  -14.96270 -6.29074  1.000 33.47634 ? 416 HOH A O   1 
HETATM 4324 O  O   . HOH I 3 .   ? -7.88857  -14.76709 13.99935  1.000 42.32915 ? 417 HOH A O   1 
HETATM 4325 O  O   . HOH I 3 .   ? -15.12008 6.49883   5.60165   1.000 43.08864 ? 418 HOH A O   1 
HETATM 4326 O  O   . HOH I 3 .   ? -1.22921  -16.98165 3.64190   1.000 32.93397 ? 419 HOH A O   1 
HETATM 4327 O  O   . HOH I 3 .   ? 5.01138   -9.96623  -1.60021  1.000 33.01940 ? 420 HOH A O   1 
HETATM 4328 O  O   . HOH I 3 .   ? -8.29096  6.60452   8.89068   1.000 37.78539 ? 421 HOH A O   1 
HETATM 4329 O  O   . HOH I 3 .   ? 5.26670   -8.06627  -3.33978  1.000 33.78509 ? 422 HOH A O   1 
HETATM 4330 O  O   . HOH I 3 .   ? -13.98264 -0.73484  -3.15984  1.000 38.41401 ? 423 HOH A O   1 
HETATM 4331 O  O   . HOH I 3 .   ? 12.33110  -7.70007  -2.02533  1.000 50.56220 ? 424 HOH A O   1 
HETATM 4332 O  O   . HOH I 3 .   ? 0.95724   -11.73198 19.82314  1.000 42.13514 ? 425 HOH A O   1 
HETATM 4333 O  O   . HOH I 3 .   ? 2.91499   9.09759   35.89589  1.000 39.50004 ? 426 HOH A O   1 
HETATM 4334 O  O   . HOH I 3 .   ? -19.67903 -13.38638 4.37640   1.000 45.04122 ? 427 HOH A O   1 
HETATM 4335 O  O   . HOH I 3 .   ? -0.18623  -18.50918 7.61747   1.000 41.53736 ? 428 HOH A O   1 
HETATM 4336 O  O   . HOH I 3 .   ? 3.70319   -13.73046 14.35765  1.000 40.68180 ? 429 HOH A O   1 
HETATM 4337 O  O   . HOH I 3 .   ? -4.05468  -4.63739  17.79839  1.000 40.23199 ? 430 HOH A O   1 
HETATM 4338 O  O   . HOH I 3 .   ? -15.77786 -16.34172 0.52532   1.000 38.36693 ? 431 HOH A O   1 
HETATM 4339 O  O   . HOH I 3 .   ? 3.27039   -13.87860 -1.13238  1.000 40.05473 ? 432 HOH A O   1 
HETATM 4340 O  O   . HOH I 3 .   ? -2.19269  3.29116   22.30402  1.000 33.62682 ? 433 HOH A O   1 
HETATM 4341 O  O   . HOH I 3 .   ? 11.82623  7.96255   31.67637  1.000 39.71827 ? 434 HOH A O   1 
HETATM 4342 O  O   . HOH I 3 .   ? -9.37094  11.42416  4.53130   1.000 39.79916 ? 435 HOH A O   1 
HETATM 4343 O  O   . HOH I 3 .   ? -6.85909  0.72302   15.36405  1.000 38.45223 ? 436 HOH A O   1 
HETATM 4344 O  O   . HOH I 3 .   ? -4.38712  10.27665  34.61897  1.000 47.94839 ? 437 HOH A O   1 
HETATM 4345 O  O   . HOH I 3 .   ? 9.07091   -11.50271 3.24782   1.000 40.89313 ? 438 HOH A O   1 
HETATM 4346 O  O   . HOH I 3 .   ? 1.17682   1.59901   13.56886  1.000 24.76652 ? 439 HOH A O   1 
HETATM 4347 O  O   . HOH I 3 .   ? 7.77422   11.18640  18.65247  1.000 28.95070 ? 440 HOH A O   1 
HETATM 4348 O  O   . HOH I 3 .   ? 5.24915   11.64091  7.03308   1.000 34.87217 ? 441 HOH A O   1 
HETATM 4349 O  O   . HOH I 3 .   ? 9.44948   9.17776   9.19371   1.000 39.53930 ? 442 HOH A O   1 
HETATM 4350 O  O   . HOH I 3 .   ? -2.29618  -7.39592  26.87189  1.000 56.60753 ? 443 HOH A O   1 
HETATM 4351 O  O   . HOH I 3 .   ? -6.52041  4.86485   10.45646  1.000 38.45896 ? 444 HOH A O   1 
HETATM 4352 O  O   . HOH I 3 .   ? 8.54282   2.09767   19.09474  1.000 32.42284 ? 445 HOH A O   1 
HETATM 4353 O  O   . HOH I 3 .   ? -14.58830 -18.90921 2.33665   1.000 41.75641 ? 446 HOH A O   1 
HETATM 4354 O  O   . HOH I 3 .   ? -9.30374  9.16271   17.39806  1.000 42.95627 ? 447 HOH A O   1 
HETATM 4355 O  O   . HOH I 3 .   ? -11.97745 -0.04835  18.95856  1.000 42.68820 ? 448 HOH A O   1 
HETATM 4356 O  O   . HOH I 3 .   ? 0.566     4.219     -3.123    1.000 32.33430 ? 449 HOH A O   1 
HETATM 4357 O  O   . HOH I 3 .   ? -1.82378  13.82550  5.47230   1.000 28.35006 ? 450 HOH A O   1 
HETATM 4358 O  O   . HOH I 3 .   ? -6.36416  5.90727   12.57959  1.000 33.82616 ? 451 HOH A O   1 
HETATM 4359 O  O   . HOH I 3 .   ? -8.21879  -21.11744 6.59403   1.000 40.92441 ? 452 HOH A O   1 
HETATM 4360 O  O   . HOH I 3 .   ? -3.15845  -1.03980  11.02940  1.000 24.06602 ? 453 HOH A O   1 
HETATM 4361 O  O   . HOH I 3 .   ? -19.00095 2.81407   9.96883   1.000 43.27486 ? 454 HOH A O   1 
HETATM 4362 O  O   . HOH I 3 .   ? 1.33571   -2.51506  17.75907  1.000 38.72900 ? 455 HOH A O   1 
HETATM 4363 O  O   . HOH I 3 .   ? -11.28082 -7.15859  -5.57077  1.000 35.33514 ? 456 HOH A O   1 
HETATM 4364 O  O   . HOH I 3 .   ? -10.25696 3.51586   -6.03787  1.000 38.75304 ? 457 HOH A O   1 
HETATM 4365 O  O   . HOH I 3 .   ? 18.22421  21.07421  49.94645  1.000 64.09320 ? 458 HOH A O   1 
HETATM 4366 O  O   . HOH I 3 .   ? -1.29663  -5.80261  22.53456  1.000 46.77893 ? 459 HOH A O   1 
HETATM 4367 O  O   . HOH I 3 .   ? -7.56743  7.55745   16.37666  1.000 36.12736 ? 460 HOH A O   1 
HETATM 4368 O  O   . HOH I 3 .   ? 10.90583  0.83329   37.01115  1.000 54.60842 ? 461 HOH A O   1 
HETATM 4369 O  O   . HOH I 3 .   ? 0.72812   20.41139  30.72409  1.000 50.84759 ? 462 HOH A O   1 
HETATM 4370 O  O   . HOH I 3 .   ? -6.06056  -6.46200  -9.02620  1.000 40.26840 ? 463 HOH A O   1 
HETATM 4371 O  O   . HOH I 3 .   ? 0.13496   19.76483  24.52350  1.000 48.79875 ? 464 HOH A O   1 
HETATM 4372 O  O   . HOH I 3 .   ? -16.58742 -8.02011  -4.27388  1.000 47.55768 ? 465 HOH A O   1 
HETATM 4373 O  O   . HOH I 3 .   ? 1.15266   -4.13352  21.15204  1.000 43.52136 ? 466 HOH A O   1 
HETATM 4374 O  O   . HOH I 3 .   ? -7.87508  -20.60433 9.30155   1.000 35.78557 ? 467 HOH A O   1 
HETATM 4375 O  O   . HOH I 3 .   ? 9.46182   13.43087  17.72199  1.000 41.26284 ? 468 HOH A O   1 
HETATM 4376 O  O   . HOH I 3 .   ? -4.42655  -16.93501 -13.46003 1.000 48.77060 ? 469 HOH A O   1 
HETATM 4377 O  O   . HOH I 3 .   ? -6.73281  1.49139   -9.57203  1.000 48.10700 ? 470 HOH A O   1 
HETATM 4378 O  O   . HOH I 3 .   ? 14.85723  -7.63090  5.58139   1.000 45.67495 ? 471 HOH A O   1 
HETATM 4379 O  O   . HOH I 3 .   ? -10.50491 3.02335   28.74728  1.000 52.26457 ? 472 HOH A O   1 
HETATM 4380 O  O   . HOH I 3 .   ? 16.05362  -0.09327  10.81857  1.000 45.34394 ? 473 HOH A O   1 
HETATM 4381 O  O   . HOH I 3 .   ? 0.52650   1.79791   18.11250  1.000 31.63208 ? 474 HOH A O   1 
HETATM 4382 O  O   . HOH I 3 .   ? 17.23916  0.23007   7.12356   1.000 49.06314 ? 475 HOH A O   1 
HETATM 4383 O  O   . HOH I 3 .   ? 5.93970   -14.35341 15.53173  1.000 43.69190 ? 476 HOH A O   1 
HETATM 4384 O  O   . HOH I 3 .   ? 10.48554  -11.75908 16.93606  1.000 42.57944 ? 477 HOH A O   1 
HETATM 4385 O  O   . HOH I 3 .   ? 11.44025  -12.43820 12.97959  1.000 47.23857 ? 478 HOH A O   1 
HETATM 4386 O  O   . HOH I 3 .   ? 12.27178  4.85238   38.50090  1.000 48.98952 ? 479 HOH A O   1 
HETATM 4387 O  O   . HOH I 3 .   ? 11.99253  0.10238   0.75979   1.000 36.43772 ? 480 HOH A O   1 
HETATM 4388 O  O   . HOH I 3 .   ? -13.94515 10.53069  4.92800   1.000 48.67867 ? 481 HOH A O   1 
HETATM 4389 O  O   . HOH I 3 .   ? -20.21029 -11.58245 5.67787   1.000 47.14655 ? 482 HOH A O   1 
HETATM 4390 O  O   . HOH I 3 .   ? -2.22666  -6.18820  -9.43780  1.000 43.63105 ? 483 HOH A O   1 
HETATM 4391 O  O   . HOH I 3 .   ? 2.59652   25.05588  48.10850  1.000 63.96571 ? 484 HOH A O   1 
HETATM 4392 O  O   . HOH I 3 .   ? -12.17469 -2.18195  -5.91259  1.000 44.51647 ? 485 HOH A O   1 
HETATM 4393 O  O   . HOH I 3 .   ? 18.309    2.707     4.228     1.000 49.35169 ? 486 HOH A O   1 
HETATM 4394 O  O   . HOH I 3 .   ? -10.06475 -14.25893 17.89133  1.000 57.49350 ? 487 HOH A O   1 
HETATM 4395 O  O   . HOH I 3 .   ? -16.90871 -5.55887  18.31707  1.000 42.53518 ? 488 HOH A O   1 
HETATM 4396 O  O   . HOH I 3 .   ? 6.97191   -15.80026 18.86585  1.000 42.90072 ? 489 HOH A O   1 
HETATM 4397 O  O   . HOH I 3 .   ? -4.36099  1.86351   19.48225  1.000 48.59737 ? 490 HOH A O   1 
HETATM 4398 O  O   . HOH I 3 .   ? -1.73256  13.12820  2.40138   1.000 39.65472 ? 491 HOH A O   1 
HETATM 4399 O  O   . HOH I 3 .   ? -15.36684 -10.25632 19.84905  1.000 53.55110 ? 492 HOH A O   1 
HETATM 4400 O  O   . HOH I 3 .   ? -18.57039 5.04943   0.58694   1.000 49.39883 ? 493 HOH A O   1 
HETATM 4401 O  O   . HOH I 3 .   ? -8.14481  3.46566   11.50308  1.000 34.16322 ? 494 HOH A O   1 
HETATM 4402 O  O   . HOH I 3 .   ? 13.64584  4.40221   2.40847   1.000 41.84158 ? 495 HOH A O   1 
HETATM 4403 O  O   . HOH I 3 .   ? -8.43260  -0.85867  -13.59131 1.000 47.03391 ? 496 HOH A O   1 
HETATM 4404 O  O   . HOH I 3 .   ? -5.69159  7.10445   35.79548  1.000 41.85808 ? 497 HOH A O   1 
HETATM 4405 O  O   . HOH I 3 .   ? -4.77526  12.07094  48.41699  1.000 40.83617 ? 498 HOH A O   1 
HETATM 4406 O  O   . HOH I 3 .   ? 13.03801  -9.50999  8.74125   1.000 43.55674 ? 499 HOH A O   1 
HETATM 4407 O  O   . HOH I 3 .   ? 8.99755   24.60531  21.79479  1.000 47.39389 ? 500 HOH A O   1 
HETATM 4408 O  O   . HOH I 3 .   ? -4.78428  4.30299   19.11102  1.000 42.52119 ? 501 HOH A O   1 
HETATM 4409 O  O   . HOH I 3 .   ? -6.28388  -8.85440  -10.22677 1.000 38.43057 ? 502 HOH A O   1 
HETATM 4410 O  O   . HOH I 3 .   ? 16.16139  19.67909  18.71240  1.000 53.67164 ? 503 HOH A O   1 
HETATM 4411 O  O   . HOH I 3 .   ? 7.25155   -19.55714 12.71155  1.000 43.19072 ? 504 HOH A O   1 
HETATM 4412 O  O   . HOH I 3 .   ? 18.53058  -6.10735  30.00327  1.000 42.72797 ? 505 HOH A O   1 
HETATM 4413 O  O   . HOH I 3 .   ? 8.44421   -15.27776 5.83869   1.000 49.30394 ? 506 HOH A O   1 
HETATM 4414 O  O   . HOH I 3 .   ? -10.75688 -7.71543  -9.89388  1.000 49.21853 ? 507 HOH A O   1 
HETATM 4415 O  O   . HOH I 3 .   ? -6.64272  -14.73402 22.83390  1.000 53.37904 ? 508 HOH A O   1 
HETATM 4416 O  O   . HOH I 3 .   ? 1.26894   22.79867  20.56689  1.000 49.87437 ? 509 HOH A O   1 
HETATM 4417 O  O   . HOH I 3 .   ? -7.71315  -6.09726  24.68561  1.000 54.66796 ? 510 HOH A O   1 
HETATM 4418 O  O   . HOH I 3 .   ? -4.13488  -13.87575 23.64943  1.000 51.93183 ? 511 HOH A O   1 
HETATM 4419 O  O   . HOH I 3 .   ? 1.48144   22.87098  23.10776  1.000 50.14650 ? 512 HOH A O   1 
HETATM 4420 O  O   . HOH I 3 .   ? 14.22924  -13.32317 8.53408   1.000 42.25604 ? 513 HOH A O   1 
HETATM 4421 O  O   . HOH J 3 .   ? -10.19834 4.75633   46.41904  1.000 35.89830 ? 301 HOH B O   1 
HETATM 4422 O  O   . HOH J 3 .   ? 0.06033   -3.35152  56.49119  1.000 31.04037 ? 302 HOH B O   1 
HETATM 4423 O  O   . HOH J 3 .   ? 8.53923   1.92859   39.99461  1.000 41.72200 ? 303 HOH B O   1 
HETATM 4424 O  O   . HOH J 3 .   ? -0.09528  1.85585   79.93972  1.000 43.47453 ? 304 HOH B O   1 
HETATM 4425 O  O   . HOH J 3 .   ? -6.881    29.425    86.494    1.000 41.99191 ? 305 HOH B O   1 
HETATM 4426 O  O   . HOH J 3 .   ? -9.35025  -2.21776  51.07885  1.000 40.53827 ? 306 HOH B O   1 
HETATM 4427 O  O   . HOH J 3 .   ? 0.73750   7.07781   85.97923  1.000 35.80479 ? 307 HOH B O   1 
HETATM 4428 O  O   . HOH J 3 .   ? -10.01220 21.36323  81.59654  1.000 43.00277 ? 308 HOH B O   1 
HETATM 4429 O  O   . HOH J 3 .   ? 0.29304   -0.36989  57.46452  1.000 32.01804 ? 309 HOH B O   1 
HETATM 4430 O  O   . HOH J 3 .   ? -0.70454  11.14350  62.77691  1.000 39.26606 ? 310 HOH B O   1 
HETATM 4431 O  O   . HOH J 3 .   ? 5.55432   1.89933   62.36747  1.000 37.38167 ? 311 HOH B O   1 
HETATM 4432 O  O   . HOH J 3 .   ? 6.29759   14.37779  69.76516  1.000 48.53213 ? 312 HOH B O   1 
HETATM 4433 O  O   . HOH J 3 .   ? -6.40846  6.65151   79.22566  1.000 33.87242 ? 313 HOH B O   1 
HETATM 4434 O  O   . HOH J 3 .   ? 1.34439   11.29229  76.38795  1.000 35.08910 ? 314 HOH B O   1 
HETATM 4435 O  O   . HOH J 3 .   ? 3.34311   16.02592  69.71123  1.000 39.55213 ? 315 HOH B O   1 
HETATM 4436 O  O   . HOH J 3 .   ? -8.83923  25.61565  81.57591  1.000 43.38142 ? 316 HOH B O   1 
HETATM 4437 O  O   . HOH J 3 .   ? -13.51517 8.18507   82.68021  1.000 33.21091 ? 317 HOH B O   1 
HETATM 4438 O  O   . HOH J 3 .   ? -7.04099  -2.27324  52.94999  1.000 41.37319 ? 318 HOH B O   1 
HETATM 4439 O  O   . HOH J 3 .   ? -1.42040  -4.30276  33.53828  1.000 39.84025 ? 319 HOH B O   1 
HETATM 4440 O  O   . HOH J 3 .   ? -13.06103 16.24077  78.74407  1.000 37.12594 ? 320 HOH B O   1 
HETATM 4441 O  O   . HOH J 3 .   ? -10.89821 -1.36401  40.25454  1.000 41.50872 ? 321 HOH B O   1 
HETATM 4442 O  O   . HOH J 3 .   ? 16.49209  -2.31120  54.65433  1.000 50.71154 ? 322 HOH B O   1 
HETATM 4443 O  O   . HOH J 3 .   ? -7.64504  -10.65962 39.36841  1.000 47.60628 ? 323 HOH B O   1 
HETATM 4444 O  O   . HOH J 3 .   ? -1.311    29.511    75.271    1.000 50.12821 ? 324 HOH B O   1 
HETATM 4445 O  O   . HOH J 3 .   ? 6.46717   15.58575  75.93945  1.000 40.06156 ? 325 HOH B O   1 
HETATM 4446 O  O   . HOH J 3 .   ? 0.173     31.232    89.306    1.000 40.73674 ? 326 HOH B O   1 
HETATM 4447 O  O   . HOH J 3 .   ? 11.87088  0.95241   63.47171  1.000 50.60500 ? 327 HOH B O   1 
HETATM 4448 O  O   . HOH J 3 .   ? -0.73821  -4.60531  54.44533  1.000 30.53361 ? 328 HOH B O   1 
HETATM 4449 O  O   . HOH J 3 .   ? -2.87547  8.60655   90.86686  1.000 37.48402 ? 329 HOH B O   1 
HETATM 4450 O  O   . HOH J 3 .   ? -7.81390  -1.22717  55.35739  1.000 35.96939 ? 330 HOH B O   1 
HETATM 4451 O  O   . HOH J 3 .   ? -0.29294  14.06064  65.80079  1.000 44.77484 ? 331 HOH B O   1 
HETATM 4452 O  O   . HOH J 3 .   ? -5.461    27.772    76.569    1.000 40.81055 ? 332 HOH B O   1 
HETATM 4453 O  O   . HOH J 3 .   ? -9.20045  23.34497  79.96581  1.000 45.33916 ? 333 HOH B O   1 
HETATM 4454 O  O   . HOH J 3 .   ? 1.43220   14.09181  60.76007  1.000 45.47485 ? 334 HOH B O   1 
HETATM 4455 O  O   . HOH J 3 .   ? 2.23393   -11.06434 64.01256  1.000 58.85651 ? 335 HOH B O   1 
HETATM 4456 O  O   . HOH J 3 .   ? 2.82176   13.69280  51.97256  1.000 49.99489 ? 336 HOH B O   1 
HETATM 4457 O  O   . HOH J 3 .   ? 14.65048  -5.53901  63.48309  1.000 45.47120 ? 337 HOH B O   1 
HETATM 4458 O  O   . HOH J 3 .   ? 4.32395   10.45023  80.98969  1.000 35.84129 ? 338 HOH B O   1 
HETATM 4459 O  O   . HOH J 3 .   ? -7.10946  -1.66336  59.16066  1.000 46.36315 ? 339 HOH B O   1 
HETATM 4460 O  O   . HOH J 3 .   ? -8.05235  8.27479   48.59247  1.000 37.79280 ? 340 HOH B O   1 
HETATM 4461 O  O   . HOH J 3 .   ? -0.86271  -0.55068  61.93418  1.000 33.42549 ? 341 HOH B O   1 
HETATM 4462 O  O   . HOH J 3 .   ? -10.756   27.052    74.800    1.000 44.66072 ? 342 HOH B O   1 
HETATM 4463 O  O   . HOH J 3 .   ? -4.20121  -1.88026  34.84139  1.000 44.59465 ? 343 HOH B O   1 
HETATM 4464 O  O   . HOH J 3 .   ? -14.37883 14.83015  73.78613  1.000 44.04605 ? 344 HOH B O   1 
HETATM 4465 O  O   . HOH J 3 .   ? -0.11169  -1.63811  32.71371  1.000 42.16424 ? 345 HOH B O   1 
HETATM 4466 O  O   . HOH J 3 .   ? 2.40015   -16.59443 35.64172  1.000 53.84961 ? 346 HOH B O   1 
HETATM 4467 O  O   . HOH J 3 .   ? -4.62778  -0.87013  63.54623  1.000 43.75452 ? 347 HOH B O   1 
HETATM 4468 O  O   . HOH J 3 .   ? -8.47420  -5.27534  68.08125  1.000 56.51923 ? 348 HOH B O   1 
HETATM 4469 O  O   . HOH J 3 .   ? -6.40660  -3.46324  66.88639  1.000 45.06663 ? 349 HOH B O   1 
HETATM 4470 O  O   . HOH J 3 .   ? -2.104    -28.836   61.648    1.000 43.36072 ? 350 HOH B O   1 
HETATM 4471 O  O   . HOH J 3 .   ? 0.50499   1.17189   82.22372  1.000 50.57656 ? 351 HOH B O   1 
HETATM 4472 O  O   . HOH J 3 .   ? -7.515    12.001    93.316    1.000 40.99137 ? 352 HOH B O   1 
HETATM 4473 O  O   . HOH J 3 .   ? -17.77788 10.38555  75.26988  1.000 44.98839 ? 353 HOH B O   1 
HETATM 4474 O  O   . HOH J 3 .   ? 4.47717   -20.80789 37.83638  1.000 49.11177 ? 354 HOH B O   1 
HETATM 4475 O  O   . HOH J 3 .   ? 1.819     30.466    90.954    1.000 45.17762 ? 355 HOH B O   1 
HETATM 4476 O  O   . HOH J 3 .   ? -0.54807  -9.22161  32.28752  1.000 46.65591 ? 356 HOH B O   1 
HETATM 4477 O  O   . HOH J 3 .   ? -14.88575 15.58278  83.20127  1.000 50.62948 ? 357 HOH B O   1 
HETATM 4478 O  O   . HOH J 3 .   ? -16.00150 6.65174   71.02518  1.000 46.62020 ? 358 HOH B O   1 
HETATM 4479 O  O   . HOH J 3 .   ? -4.83718  -7.58870  33.24735  1.000 44.37371 ? 359 HOH B O   1 
HETATM 4480 O  O   . HOH J 3 .   ? -7.09615  5.42118   43.85307  1.000 38.57273 ? 360 HOH B O   1 
HETATM 4481 O  O   . HOH J 3 .   ? 10.142    4.722     81.306    1.000 45.63088 ? 361 HOH B O   1 
HETATM 4482 O  O   . HOH J 3 .   ? -12.83961 -16.20793 38.88834  1.000 51.52324 ? 362 HOH B O   1 
HETATM 4483 O  O   . HOH J 3 .   ? -3.64335  -10.56167 35.14113  1.000 49.74570 ? 363 HOH B O   1 
HETATM 4484 O  O   . HOH J 3 .   ? -4.19232  -4.29101  67.35296  1.000 46.05528 ? 364 HOH B O   1 
HETATM 4485 O  O   . HOH J 3 .   ? -7.35922  -1.13494  62.21082  1.000 39.39365 ? 365 HOH B O   1 
HETATM 4486 O  O   . HOH J 3 .   ? -9.05241  -3.94767  57.09728  1.000 53.34798 ? 366 HOH B O   1 
HETATM 4487 O  O   . HOH J 3 .   ? -14.81645 -3.09343  58.11070  1.000 47.13513 ? 367 HOH B O   1 
HETATM 4488 O  O   . HOH J 3 .   ? -16.28709 17.28125  91.23347  1.000 48.88227 ? 368 HOH B O   1 
HETATM 4489 O  O   . HOH J 3 .   ? -6.91283  -8.00634  68.78720  1.000 45.61531 ? 369 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 2   ? 1.32141 0.75586 0.92319 -0.33663 0.13881  0.06664  2   GLU A N   
2    C CA  . GLU A 2   ? 1.35852 0.86650 0.98206 -0.34384 0.14941  0.08083  2   GLU A CA  
3    C C   . GLU A 2   ? 1.37163 0.93621 1.02203 -0.31425 0.14951  0.07511  2   GLU A C   
4    O O   . GLU A 2   ? 1.27426 0.83535 0.91524 -0.27909 0.15177  0.09062  2   GLU A O   
5    C CB  . GLU A 2   ? 1.27426 0.85124 0.92525 -0.39666 0.15598  0.07190  2   GLU A CB  
6    C CG  . GLU A 2   ? 1.21931 0.89813 0.90542 -0.40281 0.16815  0.07555  2   GLU A CG  
7    C CD  . GLU A 2   ? 1.14636 0.92531 0.88402 -0.43979 0.16983  0.05208  2   GLU A CD  
8    O OE1 . GLU A 2   ? 1.01733 0.80948 0.77612 -0.44430 0.15756  0.03041  2   GLU A OE1 
9    O OE2 . GLU A 2   ? 1.32724 1.17658 1.08582 -0.46256 0.18210  0.05420  2   GLU A OE2 
10   N N   . GLU A 3   ? 1.28879 0.91968 0.98132 -0.31823 0.14029  0.04949  3   GLU A N   
11   C CA  . GLU A 3   ? 1.08025 0.77778 0.81092 -0.27530 0.13030  0.03760  3   GLU A CA  
12   C C   . GLU A 3   ? 1.06332 0.70229 0.77279 -0.23352 0.12075  0.03609  3   GLU A C   
13   O O   . GLU A 3   ? 1.09150 0.65688 0.76966 -0.23855 0.11784  0.03189  3   GLU A O   
14   C CB  . GLU A 3   ? 1.07221 0.85123 0.85092 -0.28845 0.11899  0.01252  3   GLU A CB  
15   C CG  . GLU A 3   ? 1.03011 0.88879 0.85219 -0.25189 0.11096  0.00274  3   GLU A CG  
16   C CD  . GLU A 3   ? 1.04593 0.99677 0.91978 -0.26721 0.10192  -0.01793 3   GLU A CD  
17   O OE1 . GLU A 3   ? 1.02169 0.99240 0.90330 -0.31203 0.10605  -0.02322 3   GLU A OE1 
18   O OE2 . GLU A 3   ? 0.93284 0.93579 0.83978 -0.23445 0.08969  -0.02886 3   GLU A OE2 
19   N N   . ILE A 4   ? 1.02489 0.69857 0.75132 -0.19349 0.11700  0.03733  4   ILE A N   
20   C CA  . ILE A 4   ? 0.90291 0.54238 0.61781 -0.15590 0.10939  0.03376  4   ILE A CA  
21   C C   . ILE A 4   ? 0.89075 0.58378 0.63703 -0.14453 0.09590  0.01456  4   ILE A C   
22   O O   . ILE A 4   ? 0.86366 0.62527 0.64450 -0.14058 0.09254  0.01021  4   ILE A O   
23   C CB  . ILE A 4   ? 0.86418 0.49891 0.57112 -0.12170 0.11364  0.05044  4   ILE A CB  
24   C CG1 . ILE A 4   ? 0.95995 0.54182 0.63183 -0.13079 0.12379  0.07401  4   ILE A CG1 
25   C CG2 . ILE A 4   ? 0.83664 0.44314 0.53501 -0.08771 0.10799  0.04481  4   ILE A CG2 
26   C CD1 . ILE A 4   ? 0.96021 0.51342 0.61406 -0.09208 0.12304  0.08966  4   ILE A CD1 
27   N N   . TYR A 5   ? 0.88196 0.54041 0.61254 -0.13805 0.08811  0.00304  5   TYR A N   
28   C CA  . TYR A 5   ? 0.81647 0.51158 0.56426 -0.12432 0.07401  -0.01035 5   TYR A CA  
29   C C   . TYR A 5   ? 0.78289 0.45858 0.51814 -0.08980 0.07569  -0.00611 5   TYR A C   
30   O O   . TYR A 5   ? 0.80491 0.42650 0.51074 -0.08087 0.08186  -0.00651 5   TYR A O   
31   C CB  . TYR A 5   ? 0.80668 0.48572 0.54189 -0.14668 0.06364  -0.02700 5   TYR A CB  
32   C CG  . TYR A 5   ? 0.91267 0.61117 0.66046 -0.18631 0.06384  -0.03115 5   TYR A CG  
33   C CD1 . TYR A 5   ? 0.81917 0.59600 0.61037 -0.19420 0.06028  -0.03206 5   TYR A CD1 
34   C CD2 . TYR A 5   ? 0.92933 0.56848 0.64608 -0.21688 0.06910  -0.03533 5   TYR A CD2 
35   C CE1 . TYR A 5   ? 0.90808 0.71561 0.71573 -0.23350 0.06273  -0.03690 5   TYR A CE1 
36   C CE2 . TYR A 5   ? 0.89402 0.55398 0.62253 -0.26027 0.07041  -0.03882 5   TYR A CE2 
37   C CZ  . TYR A 5   ? 0.90602 0.65608 0.68214 -0.26938 0.06786  -0.03927 5   TYR A CZ  
38   O OH  . TYR A 5   ? 1.01628 0.80030 0.80923 -0.31545 0.07132  -0.04390 5   TYR A OH  
39   N N   . TYR A 6   ? 0.68555 0.40622 0.44398 -0.07107 0.07102  -0.00362 6   TYR A N   
40   C CA  . TYR A 6   ? 0.69129 0.40561 0.44266 -0.04458 0.07196  -0.00059 6   TYR A CA  
41   C C   . TYR A 6   ? 0.67587 0.39211 0.41988 -0.04297 0.06050  -0.01094 6   TYR A C   
42   O O   . TYR A 6   ? 0.63426 0.38105 0.39377 -0.05011 0.04655  -0.01645 6   TYR A O   
43   C CB  . TYR A 6   ? 0.51813 0.27227 0.29218 -0.03037 0.07264  0.00678  6   TYR A CB  
44   C CG  . TYR A 6   ? 0.59666 0.34712 0.36843 -0.03192 0.08371  0.01891  6   TYR A CG  
45   C CD1 . TYR A 6   ? 0.68162 0.45399 0.46472 -0.05179 0.08691  0.02023  6   TYR A CD1 
46   C CD2 . TYR A 6   ? 0.62658 0.35475 0.38346 -0.01429 0.09071  0.02983  6   TYR A CD2 
47   C CE1 . TYR A 6   ? 0.75192 0.51771 0.52450 -0.05672 0.09756  0.03436  6   TYR A CE1 
48   C CE2 . TYR A 6   ? 0.64609 0.36664 0.39412 -0.01485 0.09785  0.04445  6   TYR A CE2 
49   C CZ  . TYR A 6   ? 0.68629 0.42203 0.43841 -0.03762 0.10166  0.04786  6   TYR A CZ  
50   O OH  . TYR A 6   ? 0.68633 0.41267 0.42202 -0.04136 0.10927  0.06538  6   TYR A OH  
51   N N   . ILE A 7   ? 0.65198 0.33743 0.37099 -0.03269 0.06624  -0.01348 7   ILE A N   
52   C CA  . ILE A 7   ? 0.74459 0.42872 0.44665 -0.03344 0.05798  -0.02141 7   ILE A CA  
53   C C   . ILE A 7   ? 0.66760 0.35014 0.36004 -0.01525 0.06774  -0.01799 7   ILE A C   
54   O O   . ILE A 7   ? 0.66476 0.33215 0.35320 -0.00199 0.08190  -0.01651 7   ILE A O   
55   C CB  . ILE A 7   ? 0.71055 0.36073 0.38377 -0.05018 0.05625  -0.03530 7   ILE A CB  
56   C CG1 . ILE A 7   ? 0.70777 0.31001 0.36201 -0.04552 0.07283  -0.03849 7   ILE A CG1 
57   C CG2 . ILE A 7   ? 0.73858 0.40606 0.42618 -0.07363 0.04290  -0.04009 7   ILE A CG2 
58   C CD1 . ILE A 7   ? 0.86136 0.42131 0.47746 -0.05373 0.07536  -0.05672 7   ILE A CD1 
59   N N   . THR A 8   ? 0.64797 0.34762 0.33715 -0.01492 0.05945  -0.01600 8   THR A N   
60   C CA  . THR A 8   ? 0.62783 0.33260 0.30669 -0.00608 0.06868  -0.01326 8   THR A CA  
61   C C   . THR A 8   ? 0.71546 0.40802 0.35918 -0.01624 0.06497  -0.01911 8   THR A C   
62   O O   . THR A 8   ? 0.68307 0.36391 0.31122 -0.02821 0.05237  -0.02516 8   THR A O   
63   C CB  . THR A 8   ? 0.63078 0.36187 0.33117 -0.00191 0.06324  -0.00289 8   THR A CB  
64   O OG1 . THR A 8   ? 0.57525 0.30695 0.27148 -0.00972 0.04458  -0.00031 8   THR A OG1 
65   C CG2 . THR A 8   ? 0.57235 0.31876 0.30249 0.00526  0.06459  0.00121  8   THR A CG2 
66   N N   . PHE A 9   ? 0.71270 0.41342 0.34302 -0.01389 0.07574  -0.01706 9   PHE A N   
67   C CA  . PHE A 9   ? 0.72341 0.41533 0.31366 -0.02623 0.07444  -0.01998 9   PHE A CA  
68   C C   . PHE A 9   ? 0.75944 0.44481 0.33781 -0.03786 0.04863  -0.01243 9   PHE A C   
69   O O   . PHE A 9   ? 0.75719 0.42906 0.30022 -0.04896 0.04027  -0.01775 9   PHE A O   
70   C CB  . PHE A 9   ? 0.72468 0.43613 0.30842 -0.02772 0.08857  -0.01399 9   PHE A CB  
71   C CG  . PHE A 9   ? 0.70377 0.42560 0.30344 -0.03259 0.07719  0.00218  9   PHE A CG  
72   C CD1 . PHE A 9   ? 0.70279 0.44342 0.34142 -0.02223 0.07944  0.00569  9   PHE A CD1 
73   C CD2 . PHE A 9   ? 0.67203 0.37903 0.24270 -0.04751 0.06283  0.01379  9   PHE A CD2 
74   C CE1 . PHE A 9   ? 0.66083 0.40505 0.31066 -0.02756 0.06917  0.01640  9   PHE A CE1 
75   C CE2 . PHE A 9   ? 0.75649 0.46031 0.33784 -0.05100 0.05177  0.02720  9   PHE A CE2 
76   C CZ  . PHE A 9   ? 0.69985 0.42204 0.32173 -0.04140 0.05556  0.02648  9   PHE A CZ  
77   N N   . ARG A 10  ? 0.70933 0.40532 0.31646 -0.03325 0.03452  -0.00152 10  ARG A N   
78   C CA  . ARG A 10  ? 0.70513 0.39705 0.30607 -0.03683 0.00782  0.00588  10  ARG A CA  
79   C C   . ARG A 10  ? 0.75858 0.45177 0.35745 -0.04248 -0.00551 -0.00473 10  ARG A C   
80   O O   . ARG A 10  ? 0.75877 0.44585 0.32910 -0.05038 -0.02409 -0.00337 10  ARG A O   
81   C CB  . ARG A 10  ? 0.77078 0.47457 0.40899 -0.02543 -0.00233 0.01327  10  ARG A CB  
82   C CG  . ARG A 10  ? 0.67364 0.36906 0.30594 -0.02582 0.00201  0.02455  10  ARG A CG  
83   C CD  . ARG A 10  ? 0.79081 0.49335 0.45774 -0.01367 -0.00709 0.02630  10  ARG A CD  
84   N NE  . ARG A 10  ? 0.73667 0.43877 0.40734 -0.01702 0.00547  0.03031  10  ARG A NE  
85   C CZ  . ARG A 10  ? 0.73790 0.46413 0.43253 -0.01380 0.02270  0.02445  10  ARG A CZ  
86   N NH1 . ARG A 10  ? 0.71642 0.46089 0.43118 -0.00598 0.02998  0.01671  10  ARG A NH1 
87   N NH2 . ARG A 10  ? 0.75371 0.48513 0.44977 -0.02046 0.03165  0.02750  10  ARG A NH2 
88   N N   . GLU A 11  ? 0.70631 0.40731 0.33244 -0.04123 0.00297  -0.01459 11  GLU A N   
89   C CA  . GLU A 11  ? 0.73839 0.44319 0.36616 -0.05292 -0.00867 -0.02583 11  GLU A CA  
90   C C   . GLU A 11  ? 0.78954 0.46842 0.37224 -0.06636 -0.00312 -0.03875 11  GLU A C   
91   O O   . GLU A 11  ? 0.78496 0.46602 0.34974 -0.08015 -0.02119 -0.04618 11  GLU A O   
92   C CB  . GLU A 11  ? 0.72366 0.43838 0.38759 -0.05319 0.00134  -0.03040 11  GLU A CB  
93   C CG  . GLU A 11  ? 0.73439 0.48343 0.44172 -0.04296 -0.00694 -0.02302 11  GLU A CG  
94   C CD  . GLU A 11  ? 0.71369 0.46243 0.43225 -0.02769 0.00653  -0.01379 11  GLU A CD  
95   O OE1 . GLU A 11  ? 0.67871 0.40969 0.38477 -0.02510 0.02533  -0.01318 11  GLU A OE1 
96   O OE2 . GLU A 11  ? 0.87804 0.64571 0.61886 -0.01719 -0.00253 -0.00885 11  GLU A OE2 
97   N N   . ALA A 12  ? 0.79077 0.44871 0.35508 -0.06139 0.02120  -0.04377 12  ALA A N   
98   C CA  . ALA A 12  ? 0.83056 0.46186 0.35119 -0.07106 0.03000  -0.06116 12  ALA A CA  
99   C C   . ALA A 12  ? 0.78631 0.41923 0.26272 -0.08154 0.01719  -0.05923 12  ALA A C   
100  O O   . ALA A 12  ? 0.89772 0.51906 0.33992 -0.09693 0.00770  -0.07321 12  ALA A O   
101  C CB  . ALA A 12  ? 0.86682 0.48273 0.38192 -0.05667 0.05916  -0.06792 12  ALA A CB  
102  N N   . ARG A 13  ? 0.77548 0.41949 0.24700 -0.07610 0.01655  -0.04166 13  ARG A N   
103  C CA  . ARG A 13  ? 0.89067 0.53137 0.31489 -0.08764 0.00181  -0.03330 13  ARG A CA  
104  C C   . ARG A 13  ? 0.93036 0.57877 0.35411 -0.09426 -0.03312 -0.03031 13  ARG A C   
105  O O   . ARG A 13  ? 0.89439 0.53702 0.27303 -0.10837 -0.04687 -0.03648 13  ARG A O   
106  C CB  . ARG A 13  ? 0.82100 0.46550 0.24408 -0.08372 0.00449  -0.01108 13  ARG A CB  
107  C CG  . ARG A 13  ? 0.79962 0.45009 0.22340 -0.08060 0.03815  -0.01542 13  ARG A CG  
108  C CD  . ARG A 13  ? 0.78146 0.43985 0.21773 -0.08028 0.04154  0.00425  13  ARG A CD  
109  N NE  . ARG A 13  ? 0.77654 0.45396 0.21729 -0.07925 0.07335  -0.00265 13  ARG A NE  
110  C CZ  . ARG A 13  ? 0.76349 0.45616 0.21542 -0.08405 0.08353  0.00956  13  ARG A CZ  
111  N NH1 . ARG A 13  ? 0.77461 0.45382 0.22890 -0.09053 0.06519  0.02952  13  ARG A NH1 
112  N NH2 . ARG A 13  ? 0.75583 0.48076 0.22276 -0.08137 0.11122  -0.00007 13  ARG A NH2 
113  N N   . MET A 14  ? 0.86571 0.53319 0.34044 -0.08354 -0.04794 -0.02260 14  MET A N   
114  C CA  . MET A 14  ? 0.88178 0.57085 0.36991 -0.08598 -0.08074 -0.02252 14  MET A CA  
115  C C   . MET A 14  ? 0.82904 0.51931 0.29979 -0.10587 -0.08465 -0.04469 14  MET A C   
116  O O   . MET A 14  ? 0.93071 0.62916 0.37165 -0.11689 -0.10994 -0.04690 14  MET A O   
117  C CB  . MET A 14  ? 0.88440 0.60163 0.43787 -0.07138 -0.08617 -0.01905 14  MET A CB  
118  C CG  . MET A 14  ? 0.82948 0.58425 0.41084 -0.07553 -0.11339 -0.02663 14  MET A CG  
119  S SD  . MET A 14  ? 0.96351 0.73590 0.55221 -0.05360 -0.15135 -0.00729 14  MET A SD  
120  C CE  . MET A 14  ? 0.70911 0.47605 0.33967 -0.03064 -0.13329 0.00230  14  MET A CE  
121  N N   . LEU A 15  ? 0.86937 0.54742 0.35459 -0.11157 -0.06111 -0.06120 15  LEU A N   
122  C CA  . LEU A 15  ? 0.91056 0.58258 0.38221 -0.13396 -0.06554 -0.08382 15  LEU A CA  
123  C C   . LEU A 15  ? 0.97229 0.61493 0.37647 -0.14728 -0.06078 -0.09868 15  LEU A C   
124  O O   . LEU A 15  ? 1.07557 0.71928 0.45521 -0.16884 -0.07710 -0.11548 15  LEU A O   
125  C CB  . LEU A 15  ? 0.91824 0.57326 0.41923 -0.13672 -0.04269 -0.09450 15  LEU A CB  
126  C CG  . LEU A 15  ? 0.83533 0.52482 0.39858 -0.12992 -0.04674 -0.08332 15  LEU A CG  
127  C CD1 . LEU A 15  ? 0.82859 0.49451 0.40999 -0.11945 -0.01838 -0.08039 15  LEU A CD1 
128  C CD2 . LEU A 15  ? 0.79059 0.50996 0.37669 -0.15389 -0.06509 -0.09482 15  LEU A CD2 
129  N N   . LEU A 16  ? 0.96962 0.59112 0.34287 -0.13695 -0.03811 -0.09507 16  LEU A N   
130  C CA  . LEU A 16  ? 1.04526 0.65013 0.36142 -0.14753 -0.03007 -0.10953 16  LEU A CA  
131  C C   . LEU A 16  ? 1.07667 0.70365 0.36373 -0.15553 -0.05828 -0.09573 16  LEU A C   
132  O O   . LEU A 16  ? 1.17748 0.80607 0.43292 -0.16739 -0.06097 -0.10793 16  LEU A O   
133  C CB  . LEU A 16  ? 0.98427 0.58029 0.29497 -0.13218 0.00446  -0.10839 16  LEU A CB  
134  C CG  . LEU A 16  ? 0.96442 0.53919 0.30160 -0.11766 0.03323  -0.12147 16  LEU A CG  
135  C CD1 . LEU A 16  ? 0.95265 0.53907 0.29277 -0.10070 0.06025  -0.11538 16  LEU A CD1 
136  C CD2 . LEU A 16  ? 1.01308 0.56175 0.34022 -0.12491 0.04042  -0.14863 16  LEU A CD2 
137  N N   . ALA A 17  ? 1.12892 0.77024 0.42479 -0.14720 -0.08047 -0.07007 17  ALA A N   
138  C CA  . ALA A 17  ? 1.09296 0.74883 0.36222 -0.14905 -0.10828 -0.05105 17  ALA A CA  
139  C C   . ALA A 17  ? 1.10552 0.78944 0.39179 -0.15086 -0.15099 -0.04794 17  ALA A C   
140  O O   . ALA A 17  ? 1.13742 0.83521 0.40467 -0.14832 -0.17860 -0.03164 17  ALA A O   
141  C CB  . ALA A 17  ? 1.04815 0.69540 0.31487 -0.13561 -0.10463 -0.02135 17  ALA A CB  
142  N N   . SER A 18  ? 1.10366 0.80418 0.43677 -0.15283 -0.15545 -0.06164 18  SER A N   
143  C CA  . SER A 18  ? 1.13386 0.88068 0.50611 -0.15197 -0.19245 -0.06016 18  SER A CA  
144  C C   . SER A 18  ? 1.24531 1.00586 0.60431 -0.18194 -0.20226 -0.08892 18  SER A C   
145  O O   . SER A 18  ? 1.21415 0.94397 0.54984 -0.19722 -0.17477 -0.10970 18  SER A O   
146  C CB  . SER A 18  ? 1.09517 0.86823 0.54740 -0.13361 -0.18663 -0.05450 18  SER A CB  
147  O OG  . SER A 18  ? 1.11719 0.93750 0.60707 -0.11852 -0.22300 -0.04354 18  SER A OG  
148  N N   . ARG A 19  ? 1.23693 1.04984 0.62304 -0.18638 -0.23985 -0.09001 19  ARG A N   
149  C CA  . ARG A 19  ? 1.22929 1.06784 0.61464 -0.21431 -0.25082 -0.11521 19  ARG A CA  
150  C C   . ARG A 19  ? 1.24316 1.13123 0.69212 -0.22978 -0.26349 -0.12867 19  ARG A C   
151  O O   . ARG A 19  ? 1.19434 1.11801 0.70702 -0.20635 -0.26591 -0.11404 19  ARG A O   
152  C CB  . ARG A 19  ? 1.31977 1.18952 0.67837 -0.21056 -0.28446 -0.10735 19  ARG A CB  
153  C CG  . ARG A 19  ? 1.36235 1.19411 0.65605 -0.21976 -0.26673 -0.11447 19  ARG A CG  
154  C CD  . ARG A 19  ? 1.36160 1.23081 0.63811 -0.23394 -0.29649 -0.12639 19  ARG A CD  
155  N NE  . ARG A 19  ? 1.45778 1.35983 0.77473 -0.25862 -0.30504 -0.15356 19  ARG A NE  
156  C CZ  . ARG A 19  ? 1.47905 1.35729 0.77840 -0.28585 -0.28735 -0.18287 19  ARG A CZ  
157  N NH1 . ARG A 19  ? 1.51160 1.33839 0.75553 -0.28877 -0.26091 -0.19193 19  ARG A NH1 
158  N NH2 . ARG A 19  ? 1.44169 1.34972 0.78165 -0.31077 -0.29617 -0.20383 19  ARG A NH2 
159  N N   . GLY A 20  ? 1.24580 1.14302 0.69944 -0.26052 -0.25986 -0.15459 20  GLY A N   
160  C CA  . GLY A 20  ? 1.21533 1.16439 0.72955 -0.28377 -0.26783 -0.16915 20  GLY A CA  
161  C C   . GLY A 20  ? 1.21079 1.15765 0.77714 -0.27703 -0.24189 -0.16283 20  GLY A C   
162  O O   . GLY A 20  ? 1.20853 1.10116 0.76542 -0.29175 -0.20788 -0.17270 20  GLY A O   
163  N N   . ASN A 21  ? 1.13771 1.14299 0.76463 -0.24766 -0.25494 -0.14484 21  ASN A N   
164  C CA  . ASN A 21  ? 1.01081 1.03374 0.70039 -0.23830 -0.23071 -0.13937 21  ASN A CA  
165  C C   . ASN A 21  ? 0.98546 1.02198 0.70190 -0.19031 -0.23500 -0.11498 21  ASN A C   
166  O O   . ASN A 21  ? 0.96462 1.03849 0.68693 -0.16752 -0.26888 -0.10492 21  ASN A O   
167  C CB  . ASN A 21  ? 0.93296 1.03830 0.68646 -0.26501 -0.24238 -0.15434 21  ASN A CB  
168  C CG  . ASN A 21  ? 1.01581 1.12264 0.74130 -0.31540 -0.25371 -0.17962 21  ASN A CG  
169  O OD1 . ASN A 21  ? 1.04245 1.11113 0.75882 -0.35169 -0.22902 -0.19391 21  ASN A OD1 
170  N ND2 . ASN A 21  ? 1.12033 1.26628 0.82725 -0.31854 -0.29284 -0.18498 21  ASN A ND2 
171  N N   . VAL A 22  ? 0.79915 0.80175 0.52927 -0.17501 -0.20228 -0.10564 22  VAL A N   
172  C CA  . VAL A 22  ? 0.91431 0.91785 0.66512 -0.13341 -0.20178 -0.08552 22  VAL A CA  
173  C C   . VAL A 22  ? 0.83501 0.86622 0.64440 -0.12774 -0.17848 -0.08649 22  VAL A C   
174  O O   . VAL A 22  ? 0.79620 0.82009 0.61358 -0.15492 -0.15474 -0.09643 22  VAL A O   
175  C CB  . VAL A 22  ? 0.86674 0.79434 0.56044 -0.11877 -0.18526 -0.07104 22  VAL A CB  
176  C CG1 . VAL A 22  ? 0.94534 0.84261 0.57228 -0.13295 -0.19964 -0.07360 22  VAL A CG1 
177  C CG2 . VAL A 22  ? 0.85116 0.73356 0.53900 -0.12763 -0.14512 -0.07458 22  VAL A CG2 
178  N N   . LYS A 23  ? 0.76017 0.81903 0.60589 -0.09215 -0.18599 -0.07590 23  LYS A N   
179  C CA  . LYS A 23  ? 0.62011 0.70739 0.51691 -0.08144 -0.16456 -0.07702 23  LYS A CA  
180  C C   . LYS A 23  ? 0.72910 0.75392 0.60042 -0.06040 -0.14278 -0.06260 23  LYS A C   
181  O O   . LYS A 23  ? 0.74149 0.74489 0.59900 -0.03196 -0.15622 -0.05035 23  LYS A O   
182  C CB  . LYS A 23  ? 0.65044 0.81617 0.60810 -0.05392 -0.18758 -0.08078 23  LYS A CB  
183  C CG  . LYS A 23  ? 0.69810 0.94104 0.68729 -0.06676 -0.21788 -0.09392 23  LYS A CG  
184  C CD  . LYS A 23  ? 0.73402 1.01844 0.74848 -0.11302 -0.20043 -0.11104 23  LYS A CD  
185  C CE  . LYS A 23  ? 0.69625 1.06812 0.74633 -0.12959 -0.23247 -0.12610 23  LYS A CE  
186  N NZ  . LYS A 23  ? 0.68081 1.12774 0.78233 -0.08509 -0.26519 -0.12584 23  LYS A NZ  
187  N N   . LEU A 24  ? 0.67115 0.66643 0.53569 -0.07483 -0.11071 -0.06311 24  LEU A N   
188  C CA  . LEU A 24  ? 0.67610 0.62036 0.51786 -0.05711 -0.09199 -0.05075 24  LEU A CA  
189  C C   . LEU A 24  ? 0.59433 0.54953 0.46421 -0.05737 -0.06563 -0.05125 24  LEU A C   
190  O O   . LEU A 24  ? 0.62380 0.60706 0.51551 -0.07915 -0.05506 -0.05902 24  LEU A O   
191  C CB  . LEU A 24  ? 0.72705 0.60791 0.51083 -0.06904 -0.08186 -0.04722 24  LEU A CB  
192  C CG  . LEU A 24  ? 0.74329 0.59464 0.51015 -0.09400 -0.05881 -0.05487 24  LEU A CG  
193  C CD1 . LEU A 24  ? 0.79477 0.58968 0.52185 -0.08594 -0.03955 -0.04846 24  LEU A CD1 
194  C CD2 . LEU A 24  ? 0.81936 0.67304 0.56793 -0.12168 -0.07232 -0.06875 24  LEU A CD2 
195  N N   . ASN A 25  ? 0.61737 0.55041 0.48329 -0.03542 -0.05608 -0.04221 25  ASN A N   
196  C CA  . ASN A 25  ? 0.57707 0.52112 0.46427 -0.03089 -0.03442 -0.04145 25  ASN A CA  
197  C C   . ASN A 25  ? 0.56230 0.46050 0.41842 -0.04435 -0.01123 -0.03496 25  ASN A C   
198  O O   . ASN A 25  ? 0.62633 0.48042 0.44777 -0.04008 -0.00876 -0.02882 25  ASN A O   
199  C CB  . ASN A 25  ? 0.63905 0.57977 0.53415 -0.00162 -0.03883 -0.03739 25  ASN A CB  
200  C CG  . ASN A 25  ? 0.59614 0.55279 0.51044 0.00387  -0.01872 -0.03926 25  ASN A CG  
201  O OD1 . ASN A 25  ? 0.60118 0.54124 0.50144 -0.00911 0.00112  -0.03416 25  ASN A OD1 
202  N ND2 . ASN A 25  ? 0.66380 0.65047 0.60729 0.02538  -0.02499 -0.04706 25  ASN A ND2 
203  N N   . LEU A 26  ? 0.61564 0.52571 0.48375 -0.05948 0.00592  -0.03576 26  LEU A N   
204  C CA  . LEU A 26  ? 0.58274 0.44551 0.42084 -0.07146 0.02449  -0.02895 26  LEU A CA  
205  C C   . LEU A 26  ? 0.59538 0.45981 0.43854 -0.06390 0.04230  -0.01974 26  LEU A C   
206  O O   . LEU A 26  ? 0.53497 0.36935 0.35985 -0.07527 0.05666  -0.01235 26  LEU A O   
207  C CB  . LEU A 26  ? 0.61949 0.47531 0.45155 -0.10337 0.02674  -0.03510 26  LEU A CB  
208  C CG  . LEU A 26  ? 0.65113 0.50739 0.47371 -0.11490 0.00751  -0.04632 26  LEU A CG  
209  C CD1 . LEU A 26  ? 0.66142 0.52310 0.48581 -0.15239 0.00814  -0.05573 26  LEU A CD1 
210  C CD2 . LEU A 26  ? 0.66998 0.46923 0.44863 -0.10501 0.00808  -0.04485 26  LEU A CD2 
211  N N   . ASP A 27  ? 0.51774 0.41238 0.38129 -0.04474 0.04043  -0.02006 27  ASP A N   
212  C CA  . ASP A 27  ? 0.57459 0.46866 0.43515 -0.03694 0.05520  -0.01202 27  ASP A CA  
213  C C   . ASP A 27  ? 0.51741 0.40614 0.37566 -0.01405 0.05041  -0.01106 27  ASP A C   
214  O O   . ASP A 27  ? 0.48182 0.38979 0.34864 -0.00534 0.05617  -0.01138 27  ASP A O   
215  C CB  . ASP A 27  ? 0.60557 0.54824 0.49109 -0.04575 0.06417  -0.01599 27  ASP A CB  
216  C CG  . ASP A 27  ? 0.60802 0.60453 0.53134 -0.03650 0.05268  -0.03175 27  ASP A CG  
217  O OD1 . ASP A 27  ? 0.51785 0.50956 0.44592 -0.01427 0.03853  -0.03645 27  ASP A OD1 
218  O OD2 . ASP A 27  ? 0.67114 0.71484 0.61931 -0.05194 0.05803  -0.03916 27  ASP A OD2 
219  N N   . LEU A 28  ? 0.46093 0.32326 0.30411 -0.00784 0.04031  -0.01051 28  LEU A N   
220  C CA  . LEU A 28  ? 0.43679 0.28600 0.27104 0.00620  0.03745  -0.00745 28  LEU A CA  
221  C C   . LEU A 28  ? 0.55574 0.42725 0.41093 0.01853  0.02770  -0.01503 28  LEU A C   
222  O O   . LEU A 28  ? 0.57781 0.45070 0.43354 0.02608  0.03156  -0.01556 28  LEU A O   
223  C CB  . LEU A 28  ? 0.51448 0.35631 0.33855 0.00958  0.05169  0.00036  28  LEU A CB  
224  C CG  . LEU A 28  ? 0.54133 0.35550 0.34476 0.00581  0.06166  0.00725  28  LEU A CG  
225  C CD1 . LEU A 28  ? 0.55103 0.36840 0.35087 0.01551  0.07175  0.01588  28  LEU A CD1 
226  C CD2 . LEU A 28  ? 0.45789 0.24675 0.24201 0.00474  0.05838  0.00519  28  LEU A CD2 
227  N N   . ARG A 29  ? 0.54582 0.43653 0.41941 0.02165  0.01424  -0.02289 29  ARG A N   
228  C CA  . ARG A 29  ? 0.51185 0.42222 0.40839 0.03955  0.00316  -0.03308 29  ARG A CA  
229  C C   . ARG A 29  ? 0.59944 0.54363 0.51592 0.04377  0.01700  -0.04251 29  ARG A C   
230  O O   . ARG A 29  ? 0.62363 0.57548 0.55306 0.06101  0.01191  -0.05373 29  ARG A O   
231  C CB  . ARG A 29  ? 0.54641 0.41686 0.42366 0.05104  -0.00872 -0.02881 29  ARG A CB  
232  C CG  . ARG A 29  ? 0.69988 0.53118 0.54318 0.04150  -0.01513 -0.01583 29  ARG A CG  
233  C CD  . ARG A 29  ? 0.63052 0.46463 0.47328 0.04265  -0.03425 -0.01540 29  ARG A CD  
234  N NE  . ARG A 29  ? 0.76483 0.57417 0.57393 0.02688  -0.03301 -0.00685 29  ARG A NE  
235  C CZ  . ARG A 29  ? 0.91564 0.69035 0.69086 0.02501  -0.04351 0.00305  29  ARG A CZ  
236  N NH1 . ARG A 29  ? 0.87926 0.63117 0.64732 0.03702  -0.05863 0.00883  29  ARG A NH1 
237  N NH2 . ARG A 29  ? 0.86043 0.61913 0.60425 0.01000  -0.03810 0.00694  29  ARG A NH2 
238  N N   . LYS A 30  ? 0.57468 0.53537 0.48955 0.02843  0.03438  -0.03853 30  LYS A N   
239  C CA  . LYS A 30  ? 0.52651 0.52227 0.45366 0.02978  0.04810  -0.04639 30  LYS A CA  
240  C C   . LYS A 30  ? 0.66950 0.71890 0.63354 0.03604  0.04657  -0.06377 30  LYS A C   
241  O O   . LYS A 30  ? 0.64911 0.72470 0.62778 0.05051  0.05046  -0.07904 30  LYS A O   
242  C CB  . LYS A 30  ? 0.48205 0.47727 0.39193 0.01078  0.06545  -0.03350 30  LYS A CB  
243  C CG  . LYS A 30  ? 0.47016 0.50839 0.38806 0.00586  0.08084  -0.03960 30  LYS A CG  
244  C CD  . LYS A 30  ? 0.47688 0.51436 0.38432 0.01926  0.08261  -0.04512 30  LYS A CD  
245  C CE  . LYS A 30  ? 0.52090 0.59827 0.42432 0.01137  0.09953  -0.04899 30  LYS A CE  
246  N NZ  . LYS A 30  ? 0.55428 0.63012 0.44296 0.02207  0.09922  -0.05639 30  LYS A NZ  
247  N N   . THR A 31  ? 0.60435 0.67496 0.58512 0.02542  0.04098  -0.06433 31  THR A N   
248  C CA  . THR A 31  ? 0.58331 0.72117 0.60607 0.02748  0.04147  -0.08115 31  THR A CA  
249  C C   . THR A 31  ? 0.64625 0.79873 0.69394 0.04259  0.01689  -0.08871 31  THR A C   
250  O O   . THR A 31  ? 0.70861 0.92694 0.79690 0.04221  0.01515  -0.10244 31  THR A O   
251  C CB  . THR A 31  ? 0.68784 0.85862 0.71495 -0.00606 0.05882  -0.07676 31  THR A CB  
252  O OG1 . THR A 31  ? 0.61230 0.77611 0.64092 -0.02283 0.04662  -0.07229 31  THR A OG1 
253  C CG2 . THR A 31  ? 0.74042 0.87440 0.72859 -0.02312 0.07742  -0.05969 31  THR A CG2 
254  N N   . ASN A 32  ? 0.72158 0.81999 0.74569 0.05379  -0.00239 -0.07925 32  ASN A N   
255  C CA  . ASN A 32  ? 0.80811 0.91588 0.85089 0.07598  -0.02969 -0.08491 32  ASN A CA  
256  C C   . ASN A 32  ? 0.78212 0.93351 0.84528 0.05820  -0.03955 -0.08690 32  ASN A C   
257  O O   . ASN A 32  ? 0.73364 0.88125 0.79752 0.06888  -0.06577 -0.08480 32  ASN A O   
258  C CB  . ASN A 32  ? 0.73811 0.87775 0.81445 0.10976  -0.03263 -0.10411 32  ASN A CB  
259  C CG  . ASN A 32  ? 0.75512 0.92604 0.86587 0.13969  -0.06051 -0.11413 32  ASN A CG  
260  O OD1 . ASN A 32  ? 0.81914 1.02795 0.94848 0.13122  -0.07405 -0.11333 32  ASN A OD1 
261  N ND2 . ASN A 32  ? 0.78141 0.93476 0.90002 0.17662  -0.07078 -0.12467 32  ASN A ND2 
262  N N   . ARG A 33  ? 0.66000 0.84784 0.73385 0.02755  -0.01996 -0.08929 33  ARG A N   
263  C CA  . ARG A 33  ? 0.55988 0.78831 0.65133 0.00219  -0.02749 -0.09295 33  ARG A CA  
264  C C   . ARG A 33  ? 0.64700 0.81495 0.69452 -0.01470 -0.03914 -0.07991 33  ARG A C   
265  O O   . ARG A 33  ? 0.61835 0.72125 0.62252 -0.02260 -0.02711 -0.06720 33  ARG A O   
266  C CB  . ARG A 33  ? 0.59183 0.85940 0.69551 -0.03327 -0.00073 -0.09599 33  ARG A CB  
267  C CG  . ARG A 33  ? 0.58574 0.84941 0.67791 -0.07467 -0.00218 -0.09249 33  ARG A CG  
268  C CD  . ARG A 33  ? 0.60443 0.86279 0.68256 -0.11341 0.02670  -0.08608 33  ARG A CD  
269  N NE  . ARG A 33  ? 0.62909 0.91295 0.71570 -0.15628 0.02578  -0.09077 33  ARG A NE  
270  C CZ  . ARG A 33  ? 0.66742 0.91892 0.72674 -0.19734 0.04533  -0.08166 33  ARG A CZ  
271  N NH1 . ARG A 33  ? 0.78877 0.98100 0.80950 -0.19744 0.06531  -0.06519 33  ARG A NH1 
272  N NH2 . ARG A 33  ? 0.66758 0.94448 0.73679 -0.23990 0.04304  -0.08873 33  ARG A NH2 
273  N N   . VAL A 34  ? 0.59722 0.79265 0.65684 -0.01979 -0.06270 -0.08501 34  VAL A N   
274  C CA  . VAL A 34  ? 0.55068 0.69826 0.56788 -0.03989 -0.07345 -0.07758 34  VAL A CA  
275  C C   . VAL A 34  ? 0.62329 0.80508 0.65169 -0.08159 -0.06876 -0.08650 34  VAL A C   
276  O O   . VAL A 34  ? 0.61104 0.86949 0.68795 -0.09235 -0.06632 -0.09857 34  VAL A O   
277  C CB  . VAL A 34  ? 0.58862 0.72877 0.59583 -0.01673 -0.10763 -0.07447 34  VAL A CB  
278  C CG1 . VAL A 34  ? 0.56833 0.68279 0.57390 0.02350  -0.11394 -0.06756 34  VAL A CG1 
279  C CG2 . VAL A 34  ? 0.54657 0.76857 0.59982 -0.01789 -0.13203 -0.08781 34  VAL A CG2 
280  N N   . GLN A 35  ? 0.64279 0.76634 0.62466 -0.10713 -0.06588 -0.08213 35  GLN A N   
281  C CA  . GLN A 35  ? 0.57859 0.71379 0.55863 -0.15117 -0.06294 -0.09121 35  GLN A CA  
282  C C   . GLN A 35  ? 0.63412 0.73312 0.57396 -0.16213 -0.08375 -0.09459 35  GLN A C   
283  O O   . GLN A 35  ? 0.71404 0.75979 0.61431 -0.14107 -0.08983 -0.08606 35  GLN A O   
284  C CB  . GLN A 35  ? 0.63001 0.71562 0.58511 -0.17690 -0.03154 -0.08467 35  GLN A CB  
285  C CG  . GLN A 35  ? 0.64911 0.73622 0.61567 -0.15744 -0.00984 -0.07485 35  GLN A CG  
286  C CD  . GLN A 35  ? 0.75265 0.80226 0.69739 -0.18632 0.01734  -0.06648 35  GLN A CD  
287  O OE1 . GLN A 35  ? 0.80245 0.85816 0.74706 -0.22673 0.02222  -0.07142 35  GLN A OE1 
288  N NE2 . GLN A 35  ? 0.68005 0.68803 0.60350 -0.16725 0.03360  -0.05277 35  GLN A NE2 
289  N N   . GLU A 36  ? 0.61990 0.75074 0.56783 -0.19847 -0.09401 -0.10820 36  GLU A N   
290  C CA  . GLU A 36  ? 0.66718 0.77270 0.57608 -0.21160 -0.11628 -0.11526 36  GLU A CA  
291  C C   . GLU A 36  ? 0.73642 0.75251 0.58667 -0.23832 -0.09645 -0.11748 36  GLU A C   
292  O O   . GLU A 36  ? 0.78031 0.77830 0.63123 -0.26929 -0.07544 -0.12077 36  GLU A O   
293  C CB  . GLU A 36  ? 0.68085 0.86805 0.62556 -0.23837 -0.14169 -0.13200 36  GLU A CB  
294  C CG  . GLU A 36  ? 0.74447 0.91229 0.64594 -0.24774 -0.16984 -0.13924 36  GLU A CG  
295  C CD  . GLU A 36  ? 0.83546 1.09641 0.77744 -0.23833 -0.20960 -0.14594 36  GLU A CD  
296  O OE1 . GLU A 36  ? 0.80293 1.15110 0.80342 -0.25941 -0.21482 -0.15876 36  GLU A OE1 
297  O OE2 . GLU A 36  ? 0.90886 1.15855 0.82425 -0.20941 -0.23615 -0.13737 36  GLU A OE2 
298  N N   . VAL A 37  ? 0.82668 0.78553 0.62427 -0.22565 -0.10285 -0.11570 37  VAL A N   
299  C CA  . VAL A 37  ? 0.83843 0.71373 0.57769 -0.24411 -0.08689 -0.12272 37  VAL A CA  
300  C C   . VAL A 37  ? 0.93152 0.80395 0.63298 -0.25870 -0.11184 -0.13717 37  VAL A C   
301  O O   . VAL A 37  ? 0.97363 0.85386 0.65786 -0.23414 -0.12962 -0.13001 37  VAL A O   
302  C CB  . VAL A 37  ? 0.93385 0.74716 0.64319 -0.21214 -0.06539 -0.10893 37  VAL A CB  
303  C CG1 . VAL A 37  ? 0.98819 0.72699 0.63525 -0.22053 -0.05603 -0.12004 37  VAL A CG1 
304  C CG2 . VAL A 37  ? 0.90054 0.70472 0.63491 -0.20527 -0.03964 -0.09711 37  VAL A CG2 
305  N N   . GLU A 38  ? 0.99277 0.85295 0.67766 -0.30108 -0.11444 -0.15705 38  GLU A N   
306  C CA  . GLU A 38  ? 1.06707 0.92548 0.71092 -0.31845 -0.13893 -0.17385 38  GLU A CA  
307  C C   . GLU A 38  ? 1.16072 0.92971 0.73302 -0.31082 -0.12254 -0.18000 38  GLU A C   
308  O O   . GLU A 38  ? 1.10229 0.80250 0.65421 -0.31420 -0.09362 -0.18362 38  GLU A O   
309  C CB  . GLU A 38  ? 1.16317 1.04844 0.81686 -0.37098 -0.15055 -0.19658 38  GLU A CB  
310  C CG  . GLU A 38  ? 1.16320 0.97987 0.80067 -0.40101 -0.12122 -0.20499 38  GLU A CG  
311  C CD  . GLU A 38  ? 1.34209 1.15484 0.97232 -0.43751 -0.12594 -0.22271 38  GLU A CD  
312  O OE1 . GLU A 38  ? 1.36687 1.18960 1.02624 -0.46908 -0.11478 -0.22365 38  GLU A OE1 
313  O OE2 . GLU A 38  ? 1.18363 0.98144 0.77626 -0.43641 -0.13935 -0.23530 38  GLU A OE2 
314  N N   . ILE A 39  ? 1.19215 0.96468 0.72592 -0.29837 -0.14130 -0.18046 39  ILE A N   
315  C CA  . ILE A 39  ? 1.21434 0.91829 0.68164 -0.28771 -0.12532 -0.18649 39  ILE A CA  
316  C C   . ILE A 39  ? 1.15852 0.84604 0.59880 -0.31022 -0.12716 -0.20802 39  ILE A C   
317  O O   . ILE A 39  ? 1.25150 0.98885 0.69836 -0.32768 -0.15599 -0.21517 39  ILE A O   
318  C CB  . ILE A 39  ? 1.20997 0.93227 0.65736 -0.25700 -0.13860 -0.16740 39  ILE A CB  
319  C CG1 . ILE A 39  ? 1.08861 0.82259 0.57931 -0.22152 -0.12542 -0.14047 39  ILE A CG1 
320  C CG2 . ILE A 39  ? 1.30385 0.97903 0.69125 -0.24993 -0.12240 -0.17452 39  ILE A CG2 
321  C CD1 . ILE A 39  ? 1.13213 0.89460 0.61911 -0.19591 -0.14671 -0.11811 39  ILE A CD1 
322  N N   . LYS A 40  ? 1.20858 0.82836 0.61967 -0.30741 -0.09799 -0.21906 40  LYS A N   
323  C CA  . LYS A 40  ? 1.21275 0.80582 0.59039 -0.32474 -0.09705 -0.24185 40  LYS A CA  
324  C C   . LYS A 40  ? 1.24055 0.79376 0.57068 -0.29984 -0.07808 -0.24631 40  LYS A C   
325  O O   . LYS A 40  ? 1.28954 0.83335 0.61689 -0.27127 -0.06241 -0.23131 40  LYS A O   
326  C CB  . LYS A 40  ? 1.28676 0.83456 0.67525 -0.34755 -0.08086 -0.25479 40  LYS A CB  
327  C CG  . LYS A 40  ? 1.24748 0.83701 0.68674 -0.37517 -0.09237 -0.24885 40  LYS A CG  
328  C CD  . LYS A 40  ? 1.27337 0.90119 0.71785 -0.41227 -0.11625 -0.26651 40  LYS A CD  
329  C CE  . LYS A 40  ? 1.36156 0.91937 0.76778 -0.42902 -0.10203 -0.28843 40  LYS A CE  
330  N NZ  . LYS A 40  ? 1.42056 1.00356 0.80104 -0.44767 -0.12536 -0.30924 40  LYS A NZ  
331  N N   . ASP A 41  ? 1.36301 0.89758 0.65688 -0.31240 -0.07917 -0.26872 41  ASP A N   
332  C CA  . ASP A 41  ? 1.44565 0.95065 0.69553 -0.29158 -0.06010 -0.27745 41  ASP A CA  
333  C C   . ASP A 41  ? 1.35654 0.80730 0.61127 -0.26633 -0.02508 -0.27790 41  ASP A C   
334  O O   . ASP A 41  ? 1.32287 0.77144 0.56489 -0.23880 -0.00729 -0.27157 41  ASP A O   
335  C CB  . ASP A 41  ? 1.43498 0.92680 0.64590 -0.31183 -0.06713 -0.30609 41  ASP A CB  
336  C CG  . ASP A 41  ? 1.45124 0.99773 0.63938 -0.32179 -0.09719 -0.30325 41  ASP A CG  
337  O OD1 . ASP A 41  ? 1.45003 1.04364 0.65746 -0.31391 -0.11564 -0.27803 41  ASP A OD1 
338  O OD2 . ASP A 41  ? 1.52510 1.06597 0.67481 -0.33606 -0.10389 -0.32580 41  ASP A OD2 
339  N N   . GLU A 42  ? 1.47328 0.88268 0.74713 -0.27524 -0.01553 -0.28413 42  GLU A N   
340  C CA  . GLU A 42  ? 1.47025 0.82672 0.74917 -0.24809 0.01385  -0.28331 42  GLU A CA  
341  C C   . GLU A 42  ? 1.39941 0.76881 0.71442 -0.22829 0.02160  -0.25583 42  GLU A C   
342  O O   . GLU A 42  ? 1.43039 0.76934 0.75098 -0.19871 0.04432  -0.25126 42  GLU A O   
343  C CB  . GLU A 42  ? 1.50489 0.80093 0.78172 -0.26380 0.02037  -0.29912 42  GLU A CB  
344  C CG  . GLU A 42  ? 1.55692 0.86354 0.85673 -0.30395 0.00219  -0.29569 42  GLU A CG  
345  C CD  . GLU A 42  ? 1.53443 0.88815 0.82361 -0.33756 -0.02549 -0.30945 42  GLU A CD  
346  O OE1 . GLU A 42  ? 1.61524 0.95664 0.86612 -0.34056 -0.02779 -0.33226 42  GLU A OE1 
347  O OE2 . GLU A 42  ? 1.51459 0.92129 0.83533 -0.36051 -0.04574 -0.29857 42  GLU A OE2 
348  N N   . GLY A 43  ? 1.24933 0.66633 0.58958 -0.24168 0.00226  -0.23900 43  GLY A N   
349  C CA  . GLY A 43  ? 1.27751 0.70757 0.64834 -0.22241 0.00922  -0.21545 43  GLY A CA  
350  C C   . GLY A 43  ? 1.19966 0.67873 0.60215 -0.24337 -0.01435 -0.20351 43  GLY A C   
351  O O   . GLY A 43  ? 1.23688 0.75722 0.63752 -0.26542 -0.04003 -0.20950 43  GLY A O   
352  N N   . ALA A 44  ? 1.05761 0.53677 0.49119 -0.23466 -0.00631 -0.18733 44  ALA A N   
353  C CA  . ALA A 44  ? 1.12167 0.65454 0.59538 -0.24996 -0.02500 -0.17599 44  ALA A CA  
354  C C   . ALA A 44  ? 1.15967 0.67018 0.65943 -0.26828 -0.01300 -0.17312 44  ALA A C   
355  O O   . ALA A 44  ? 1.06365 0.52105 0.55718 -0.25133 0.01040  -0.16648 44  ALA A O   
356  C CB  . ALA A 44  ? 1.04905 0.62713 0.55532 -0.21409 -0.02496 -0.14960 44  ALA A CB  
357  N N   . VAL A 45  ? 1.12226 0.67490 0.64974 -0.30366 -0.02924 -0.17745 45  VAL A N   
358  C CA  . VAL A 45  ? 1.11831 0.65760 0.67001 -0.32787 -0.01722 -0.17185 45  VAL A CA  
359  C C   . VAL A 45  ? 1.06173 0.68455 0.67679 -0.31645 -0.02151 -0.15027 45  VAL A C   
360  O O   . VAL A 45  ? 1.02037 0.72111 0.66646 -0.31214 -0.04376 -0.14971 45  VAL A O   
361  C CB  . VAL A 45  ? 1.13310 0.67418 0.68455 -0.36973 -0.02490 -0.18675 45  VAL A CB  
362  C CG1 . VAL A 45  ? 1.17522 0.80899 0.76863 -0.39894 -0.04955 -0.19162 45  VAL A CG1 
363  C CG2 . VAL A 45  ? 1.14765 0.63497 0.69875 -0.38482 -0.00363 -0.17823 45  VAL A CG2 
364  N N   . PHE A 46  ? 1.06346 0.66748 0.69434 -0.30776 -0.00076 -0.13286 46  PHE A N   
365  C CA  . PHE A 46  ? 0.99660 0.66488 0.67757 -0.28664 0.00206  -0.11279 46  PHE A CA  
366  C C   . PHE A 46  ? 1.04286 0.76785 0.76449 -0.32439 0.00067  -0.11326 46  PHE A C   
367  O O   . PHE A 46  ? 1.12461 0.83481 0.83357 -0.36873 -0.00311 -0.12796 46  PHE A O   
368  C CB  . PHE A 46  ? 1.07844 0.69534 0.74630 -0.25547 0.02489  -0.09481 46  PHE A CB  
369  C CG  . PHE A 46  ? 0.98636 0.59964 0.64355 -0.21257 0.02416  -0.09008 46  PHE A CG  
370  C CD1 . PHE A 46  ? 1.04577 0.62037 0.66182 -0.20663 0.02056  -0.10430 46  PHE A CD1 
371  C CD2 . PHE A 46  ? 0.94694 0.59703 0.63277 -0.18202 0.02799  -0.07310 46  PHE A CD2 
372  C CE1 . PHE A 46  ? 0.95674 0.53337 0.56213 -0.17308 0.02228  -0.09935 46  PHE A CE1 
373  C CE2 . PHE A 46  ? 0.94594 0.59300 0.62125 -0.14948 0.02781  -0.06874 46  PHE A CE2 
374  C CZ  . PHE A 46  ? 0.89583 0.50815 0.53175 -0.14607 0.02569  -0.08073 46  PHE A CZ  
375  N N   . PRO A 47  ? 1.00047 0.79421 0.77068 -0.31178 0.00419  -0.10041 47  PRO A N   
376  C CA  . PRO A 47  ? 0.98064 0.84161 0.79254 -0.35003 0.00539  -0.10385 47  PRO A CA  
377  C C   . PRO A 47  ? 1.08286 0.88760 0.87157 -0.38954 0.02808  -0.09675 47  PRO A C   
378  O O   . PRO A 47  ? 1.08770 0.94739 0.90758 -0.42761 0.03352  -0.09798 47  PRO A O   
379  C CB  . PRO A 47  ? 0.96026 0.90120 0.82372 -0.31780 0.00700  -0.09366 47  PRO A CB  
380  C CG  . PRO A 47  ? 0.90986 0.82171 0.75708 -0.26686 0.00289  -0.08513 47  PRO A CG  
381  C CD  . PRO A 47  ? 0.90233 0.71739 0.69094 -0.26522 0.00887  -0.08478 47  PRO A CD  
382  N N   . ASP A 48  ? 1.14015 0.83819 0.87495 -0.38165 0.04135  -0.08905 48  ASP A N   
383  C CA  . ASP A 48  ? 1.09934 0.72087 0.79944 -0.41888 0.05905  -0.08144 48  ASP A CA  
384  C C   . ASP A 48  ? 1.16157 0.71757 0.82205 -0.44055 0.05239  -0.09826 48  ASP A C   
385  O O   . ASP A 48  ? 1.22813 0.74950 0.87365 -0.46697 0.06094  -0.09295 48  ASP A O   
386  C CB  . ASP A 48  ? 1.14335 0.69503 0.81459 -0.38335 0.07711  -0.05748 48  ASP A CB  
387  C CG  . ASP A 48  ? 1.18281 0.63633 0.80390 -0.35483 0.07742  -0.06269 48  ASP A CG  
388  O OD1 . ASP A 48  ? 1.25426 0.71578 0.87064 -0.34158 0.06405  -0.08187 48  ASP A OD1 
389  O OD2 . ASP A 48  ? 1.20654 0.59361 0.79978 -0.33470 0.08899  -0.04675 48  ASP A OD2 
390  N N   . GLY A 49  ? 1.19431 0.74001 0.83832 -0.42526 0.03692  -0.11737 49  GLY A N   
391  C CA  . GLY A 49  ? 1.13466 0.62607 0.74223 -0.43567 0.03153  -0.13396 49  GLY A CA  
392  C C   . GLY A 49  ? 1.22703 0.62826 0.78804 -0.39526 0.04063  -0.13428 49  GLY A C   
393  O O   . GLY A 49  ? 1.26539 0.62071 0.79502 -0.39997 0.03742  -0.15098 49  GLY A O   
394  N N   . THR A 50  ? 1.29475 0.67510 0.85321 -0.35523 0.05220  -0.11775 50  THR A N   
395  C CA  . THR A 50  ? 1.30293 0.61958 0.82747 -0.31198 0.06000  -0.12031 50  THR A CA  
396  C C   . THR A 50  ? 1.21002 0.55409 0.72639 -0.29721 0.04804  -0.13952 50  THR A C   
397  O O   . THR A 50  ? 1.14568 0.55079 0.68390 -0.29581 0.03708  -0.13917 50  THR A O   
398  C CB  . THR A 50  ? 1.27011 0.57062 0.79975 -0.27294 0.07397  -0.09679 50  THR A CB  
399  O OG1 . THR A 50  ? 1.25113 0.54352 0.79020 -0.29043 0.08233  -0.07534 50  THR A OG1 
400  C CG2 . THR A 50  ? 1.31309 0.55207 0.81360 -0.23009 0.08313  -0.09961 50  THR A CG2 
401  N N   . LEU A 51  ? 1.28331 0.58294 0.76623 -0.28678 0.04942  -0.15650 51  LEU A N   
402  C CA  . LEU A 51  ? 1.20128 0.52251 0.66847 -0.27012 0.04148  -0.17248 51  LEU A CA  
403  C C   . LEU A 51  ? 1.31401 0.60798 0.77035 -0.22133 0.05811  -0.16559 51  LEU A C   
404  O O   . LEU A 51  ? 1.33279 0.57005 0.77140 -0.20209 0.07150  -0.16841 51  LEU A O   
405  C CB  . LEU A 51  ? 1.31283 0.61350 0.75113 -0.29057 0.03360  -0.19765 51  LEU A CB  
406  C CG  . LEU A 51  ? 1.28335 0.58865 0.69235 -0.27131 0.03078  -0.21548 51  LEU A CG  
407  C CD1 . LEU A 51  ? 1.39391 0.70627 0.78495 -0.30638 0.01444  -0.23838 51  LEU A CD1 
408  C CD2 . LEU A 51  ? 1.42894 0.67826 0.81381 -0.23350 0.05151  -0.22136 51  LEU A CD2 
409  N N   . VAL A 52  ? 1.25237 0.58959 0.72223 -0.20134 0.05638  -0.15648 52  VAL A N   
410  C CA  . VAL A 52  ? 1.21209 0.54297 0.67301 -0.15899 0.07004  -0.15401 52  VAL A CA  
411  C C   . VAL A 52  ? 1.23664 0.57739 0.66870 -0.15828 0.06567  -0.17435 52  VAL A C   
412  O O   . VAL A 52  ? 1.19628 0.58038 0.62437 -0.17458 0.04857  -0.17788 52  VAL A O   
413  C CB  . VAL A 52  ? 1.14548 0.51793 0.62982 -0.14194 0.06995  -0.13638 52  VAL A CB  
414  C CG1 . VAL A 52  ? 1.21453 0.57994 0.69814 -0.09955 0.08776  -0.13021 52  VAL A CG1 
415  C CG2 . VAL A 52  ? 1.15971 0.55110 0.68241 -0.15328 0.06791  -0.11523 52  VAL A CG2 
416  N N   . GLU A 53  ? 1.28235 0.58423 0.69338 -0.13971 0.07949  -0.18791 53  GLU A N   
417  C CA  . GLU A 53  ? 1.36761 0.67564 0.74783 -0.14342 0.07706  -0.21006 53  GLU A CA  
418  C C   . GLU A 53  ? 1.31343 0.66551 0.68923 -0.12177 0.08215  -0.20569 53  GLU A C   
419  O O   . GLU A 53  ? 1.29844 0.66259 0.69313 -0.09435 0.09478  -0.19123 53  GLU A O   
420  C CB  . GLU A 53  ? 1.46376 0.71556 0.82306 -0.13127 0.09047  -0.23033 53  GLU A CB  
421  C CG  . GLU A 53  ? 1.53305 0.75900 0.90558 -0.08989 0.11021  -0.22332 53  GLU A CG  
422  C CD  . GLU A 53  ? 1.65102 0.81503 1.02781 -0.09112 0.11226  -0.21804 53  GLU A CD  
423  O OE1 . GLU A 53  ? 1.68667 0.83606 1.06178 -0.12786 0.10016  -0.21535 53  GLU A OE1 
424  O OE2 . GLU A 53  ? 1.69001 0.82292 1.07223 -0.05610 0.12505  -0.21596 53  GLU A OE2 
425  N N   . ARG A 54  ? 1.32001 0.69785 0.66919 -0.13639 0.07154  -0.21733 54  ARG A N   
426  C CA  . ARG A 54  ? 1.25526 0.67566 0.59251 -0.12438 0.07397  -0.21121 54  ARG A CA  
427  C C   . ARG A 54  ? 1.20723 0.62766 0.55414 -0.08889 0.10044  -0.20974 54  ARG A C   
428  O O   . ARG A 54  ? 1.15429 0.61030 0.51348 -0.07636 0.10528  -0.19273 54  ARG A O   
429  C CB  . ARG A 54  ? 1.34034 0.77231 0.63822 -0.14139 0.06463  -0.22894 54  ARG A CB  
430  C CG  . ARG A 54  ? 1.30844 0.78928 0.59241 -0.14826 0.04967  -0.21321 54  ARG A CG  
431  C CD  . ARG A 54  ? 1.33395 0.83079 0.58863 -0.17621 0.02340  -0.22190 54  ARG A CD  
432  N NE  . ARG A 54  ? 1.27336 0.81270 0.52131 -0.18036 0.00258  -0.19893 54  ARG A NE  
433  C CZ  . ARG A 54  ? 1.23774 0.79649 0.46810 -0.16869 0.01119  -0.18547 54  ARG A CZ  
434  N NH1 . ARG A 54  ? 1.26673 0.81814 0.48596 -0.15354 0.04052  -0.19594 54  ARG A NH1 
435  N NH2 . ARG A 54  ? 1.14428 0.73209 0.36965 -0.17225 -0.01079 -0.16060 54  ARG A NH2 
436  N N   . GLU A 55  ? 1.29585 0.67831 0.63930 -0.07261 0.11619  -0.22806 55  GLU A N   
437  C CA  . GLU A 55  ? 1.28018 0.66695 0.64021 -0.03523 0.13943  -0.22951 55  GLU A CA  
438  C C   . GLU A 55  ? 1.16478 0.57060 0.56145 -0.01884 0.14248  -0.20292 55  GLU A C   
439  O O   . GLU A 55  ? 1.05940 0.50731 0.46985 -0.00041 0.15431  -0.19519 55  GLU A O   
440  C CB  . GLU A 55  ? 1.30248 0.63370 0.66016 -0.01891 0.14897  -0.24907 55  GLU A CB  
441  C CG  . GLU A 55  ? 1.31890 0.61434 0.64131 -0.04243 0.14104  -0.27512 55  GLU A CG  
442  C CD  . GLU A 55  ? 1.52173 0.84145 0.81472 -0.03758 0.15064  -0.30024 55  GLU A CD  
443  O OE1 . GLU A 55  ? 1.56755 0.90680 0.87028 -0.00517 0.17064  -0.30884 55  GLU A OE1 
444  O OE2 . GLU A 55  ? 1.54583 0.86934 0.80643 -0.06613 0.13799  -0.31241 55  GLU A OE2 
445  N N   . VAL A 56  ? 1.19999 0.57838 0.61271 -0.02758 0.13234  -0.18932 56  VAL A N   
446  C CA  . VAL A 56  ? 1.15698 0.55124 0.60199 -0.01234 0.13462  -0.16543 56  VAL A CA  
447  C C   . VAL A 56  ? 1.04326 0.48825 0.49202 -0.02256 0.12694  -0.15134 56  VAL A C   
448  O O   . VAL A 56  ? 0.99977 0.47868 0.46656 -0.00323 0.13685  -0.13983 56  VAL A O   
449  C CB  . VAL A 56  ? 1.16343 0.51914 0.62069 -0.02439 0.12561  -0.15409 56  VAL A CB  
450  C CG1 . VAL A 56  ? 1.21641 0.57812 0.70388 0.00150  0.13283  -0.13271 56  VAL A CG1 
451  C CG2 . VAL A 56  ? 1.24301 0.54163 0.68384 -0.02846 0.12715  -0.16925 56  VAL A CG2 
452  N N   . LEU A 57  ? 1.08312 0.53565 0.51553 -0.05309 0.10731  -0.15180 57  LEU A N   
453  C CA  . LEU A 57  ? 1.02997 0.52507 0.46415 -0.06140 0.09497  -0.13612 57  LEU A CA  
454  C C   . LEU A 57  ? 0.96782 0.49563 0.38842 -0.05138 0.10632  -0.13420 57  LEU A C   
455  O O   . LEU A 57  ? 0.86676 0.42801 0.30465 -0.04471 0.10702  -0.11551 57  LEU A O   
456  C CB  . LEU A 57  ? 1.04893 0.55410 0.47123 -0.09156 0.06769  -0.13705 57  LEU A CB  
457  C CG  . LEU A 57  ? 0.98819 0.48782 0.43620 -0.11041 0.05185  -0.13523 57  LEU A CG  
458  C CD1 . LEU A 57  ? 1.15312 0.59767 0.58083 -0.12095 0.06052  -0.15635 57  LEU A CD1 
459  C CD2 . LEU A 57  ? 1.01673 0.55221 0.46249 -0.13327 0.02268  -0.13304 57  LEU A CD2 
460  N N   . GLU A 58  ? 1.02390 0.54890 0.41992 -0.05253 0.11457  -0.15186 58  GLU A N   
461  C CA  . GLU A 58  ? 1.00324 0.56528 0.39013 -0.04529 0.12884  -0.15081 58  GLU A CA  
462  C C   . GLU A 58  ? 0.92701 0.51117 0.34861 -0.01821 0.14980  -0.14430 58  GLU A C   
463  O O   . GLU A 58  ? 0.90190 0.52551 0.33284 -0.01876 0.15403  -0.12870 58  GLU A O   
464  C CB  . GLU A 58  ? 1.06900 0.62496 0.42558 -0.04761 0.13764  -0.17575 58  GLU A CB  
465  C CG  . GLU A 58  ? 1.14116 0.68738 0.46089 -0.07602 0.11549  -0.18127 58  GLU A CG  
466  C CD  . GLU A 58  ? 1.23641 0.78097 0.52189 -0.07844 0.12514  -0.20671 58  GLU A CD  
467  O OE1 . GLU A 58  ? 1.19271 0.77232 0.45932 -0.08003 0.13356  -0.20376 58  GLU A OE1 
468  O OE2 . GLU A 58  ? 1.23601 0.74395 0.51168 -0.08048 0.12429  -0.22945 58  GLU A OE2 
469  N N   . LYS A 59  ? 0.93830 0.49751 0.37999 0.00488  0.16094  -0.15467 59  LYS A N   
470  C CA  . LYS A 59  ? 0.93410 0.51828 0.41222 0.03407  0.17710  -0.14813 59  LYS A CA  
471  C C   . LYS A 59  ? 0.88354 0.49137 0.38365 0.03049  0.17001  -0.12285 59  LYS A C   
472  O O   . LYS A 59  ? 0.89978 0.55531 0.41800 0.03653  0.17980  -0.11378 59  LYS A O   
473  C CB  . LYS A 59  ? 1.02275 0.56443 0.51627 0.05921  0.18182  -0.15681 59  LYS A CB  
474  C CG  . LYS A 59  ? 0.96447 0.52769 0.49799 0.09116  0.19093  -0.14469 59  LYS A CG  
475  C CD  . LYS A 59  ? 0.90981 0.42481 0.45338 0.09587  0.17974  -0.13064 59  LYS A CD  
476  C CE  . LYS A 59  ? 0.87261 0.40997 0.45240 0.12772  0.18481  -0.11532 59  LYS A CE  
477  N NZ  . LYS A 59  ? 0.96326 0.52165 0.56128 0.16328  0.19837  -0.12829 59  LYS A NZ  
478  N N   A ILE A 60  ? 0.88243 0.46368 0.38594 0.01851  0.15207  -0.11183 60  ILE A N   
479  N N   B ILE A 60  ? 0.88401 0.46559 0.38769 0.01845  0.15200  -0.11167 60  ILE A N   
480  C CA  A ILE A 60  ? 0.85242 0.46894 0.39459 0.01694  0.14064  -0.08637 60  ILE A CA  
481  C CA  B ILE A 60  ? 0.85394 0.47081 0.39658 0.01684  0.14040  -0.08603 60  ILE A CA  
482  C C   A ILE A 60  ? 0.84824 0.49304 0.37820 -0.00421 0.12937  -0.07488 60  ILE A C   
483  C C   B ILE A 60  ? 0.84848 0.49027 0.38013 -0.00567 0.12611  -0.07375 60  ILE A C   
484  O O   A ILE A 60  ? 0.80773 0.48520 0.36192 -0.00363 0.12723  -0.05817 60  ILE A O   
485  O O   B ILE A 60  ? 0.82078 0.48962 0.37982 -0.00649 0.11834  -0.05538 60  ILE A O   
486  C CB  A ILE A 60  ? 0.90873 0.50328 0.47253 0.01262  0.12519  -0.07644 60  ILE A CB  
487  C CB  B ILE A 60  ? 0.90156 0.49584 0.46792 0.01620  0.12735  -0.07643 60  ILE A CB  
488  C CG1 A ILE A 60  ? 0.92408 0.49525 0.46591 -0.01354 0.10778  -0.08292 60  ILE A CG1 
489  C CG1 B ILE A 60  ? 0.87118 0.46128 0.43127 -0.01047 0.10519  -0.07248 60  ILE A CG1 
490  C CG2 A ILE A 60  ? 0.90747 0.46481 0.47654 0.03325  0.13622  -0.08259 60  ILE A CG2 
491  C CG2 B ILE A 60  ? 0.90986 0.45319 0.46560 0.02983  0.13714  -0.08996 60  ILE A CG2 
492  C CD1 A ILE A 60  ? 0.81287 0.35414 0.36777 -0.02016 0.10124  -0.08166 60  ILE A CD1 
493  C CD1 B ILE A 60  ? 0.79410 0.41194 0.39187 -0.01276 0.09192  -0.05302 60  ILE A CD1 
494  N N   . ALA A 61  ? 0.88220 0.51172 0.37033 -0.02324 0.12145  -0.08341 61  ALA A N   
495  C CA  . ALA A 61  ? 0.84000 0.48823 0.30813 -0.04138 0.10909  -0.06908 61  ALA A CA  
496  C C   . ALA A 61  ? 0.88407 0.56359 0.34697 -0.04019 0.12913  -0.06445 61  ALA A C   
497  O O   . ALA A 61  ? 0.79464 0.48945 0.25657 -0.05237 0.12079  -0.04512 61  ALA A O   
498  C CB  . ALA A 61  ? 0.85081 0.47880 0.26735 -0.06092 0.09677  -0.07928 61  ALA A CB  
499  N N   . ARG A 62  ? 0.87141 0.56595 0.34138 -0.02544 0.15303  -0.08126 62  ARG A N   
500  C CA  . ARG A 62  ? 0.82576 0.56909 0.30869 -0.02381 0.17228  -0.07961 62  ARG A CA  
501  C C   . ARG A 62  ? 0.85855 0.63175 0.38553 -0.00622 0.18353  -0.07313 62  ARG A C   
502  O O   . ARG A 62  ? 0.96077 0.78239 0.50254 -0.01090 0.19653  -0.06895 62  ARG A O   
503  C CB  . ARG A 62  ? 0.84164 0.59861 0.31432 -0.01351 0.19145  -0.10419 62  ARG A CB  
504  C CG  . ARG A 62  ? 0.92864 0.66930 0.35480 -0.03320 0.18352  -0.11152 62  ARG A CG  
505  C CD  . ARG A 62  ? 0.93974 0.68016 0.35553 -0.01790 0.20049  -0.14169 62  ARG A CD  
506  N NE  . ARG A 62  ? 1.10352 0.86792 0.48334 -0.03384 0.20702  -0.14761 62  ARG A NE  
507  C CZ  . ARG A 62  ? 1.08134 0.82412 0.41817 -0.05739 0.18967  -0.14314 62  ARG A CZ  
508  N NH1 . ARG A 62  ? 1.00767 0.71160 0.33550 -0.06892 0.16332  -0.13220 62  ARG A NH1 
509  N NH2 . ARG A 62  ? 1.07111 0.83586 0.37299 -0.06853 0.19852  -0.15017 62  ARG A NH2 
510  N N   . ASP A 63  ? 0.84889 0.60162 0.40220 0.01210  0.17663  -0.07124 63  ASP A N   
511  C CA  . ASP A 63  ? 0.78726 0.57418 0.38964 0.03077  0.18079  -0.06313 63  ASP A CA  
512  C C   . ASP A 63  ? 0.74381 0.52759 0.36590 0.01872  0.15832  -0.04197 63  ASP A C   
513  O O   . ASP A 63  ? 0.77775 0.53480 0.41131 0.02487  0.14471  -0.03804 63  ASP A O   
514  C CB  . ASP A 63  ? 0.84994 0.61844 0.47062 0.06363  0.18731  -0.07452 63  ASP A CB  
515  C CG  . ASP A 63  ? 0.86826 0.66004 0.53466 0.08110  0.18072  -0.05981 63  ASP A CG  
516  O OD1 . ASP A 63  ? 0.72293 0.56573 0.41392 0.07507  0.18160  -0.04996 63  ASP A OD1 
517  O OD2 . ASP A 63  ? 0.76961 0.52648 0.44319 0.09771  0.17399  -0.05767 63  ASP A OD2 
518  N N   . ASP A 64  ? 0.68380 0.49359 0.30772 0.00001  0.15572  -0.02953 64  ASP A N   
519  C CA  . ASP A 64  ? 0.71975 0.52383 0.35959 -0.00964 0.13567  -0.01312 64  ASP A CA  
520  C C   . ASP A 64  ? 0.72841 0.56734 0.41104 0.00222  0.13767  -0.00857 64  ASP A C   
521  O O   . ASP A 64  ? 0.75348 0.59668 0.44838 -0.00830 0.12561  0.00192  64  ASP A O   
522  C CB  . ASP A 64  ? 0.68364 0.48213 0.29601 -0.03685 0.12856  -0.00130 64  ASP A CB  
523  C CG  . ASP A 64  ? 0.73904 0.57821 0.35366 -0.05064 0.14651  0.00058  64  ASP A CG  
524  O OD1 . ASP A 64  ? 0.83082 0.71221 0.47019 -0.03637 0.16562  -0.01043 64  ASP A OD1 
525  O OD2 . ASP A 64  ? 0.77767 0.60673 0.36833 -0.07653 0.14113  0.01347  64  ASP A OD2 
526  N N   . GLY A 65  ? 0.69796 0.56053 0.40143 0.02538  0.15124  -0.01712 65  GLY A N   
527  C CA  . GLY A 65  ? 0.66189 0.56490 0.40366 0.03749  0.15113  -0.01234 65  GLY A CA  
528  C C   . GLY A 65  ? 0.70374 0.58943 0.46157 0.06126  0.14342  -0.00942 65  GLY A C   
529  O O   . GLY A 65  ? 0.77414 0.69330 0.55987 0.07437  0.14145  -0.00450 65  GLY A O   
530  N N   . THR A 66  ? 0.71774 0.55283 0.45602 0.06438  0.13845  -0.01156 66  THR A N   
531  C CA  . THR A 66  ? 0.69198 0.50381 0.43873 0.08103  0.13254  -0.00623 66  THR A CA  
532  C C   . THR A 66  ? 0.65406 0.42446 0.38536 0.06477  0.12060  -0.00374 66  THR A C   
533  O O   . THR A 66  ? 0.67186 0.42274 0.38174 0.04911  0.11793  -0.01019 66  THR A O   
534  C CB  . THR A 66  ? 0.73675 0.52919 0.47853 0.10886  0.14416  -0.01464 66  THR A CB  
535  O OG1 . THR A 66  ? 0.65429 0.49220 0.40849 0.12228  0.15849  -0.02394 66  THR A OG1 
536  C CG2 . THR A 66  ? 0.67198 0.45401 0.42662 0.12941  0.13793  -0.00251 66  THR A CG2 
537  N N   A VAL A 67  ? 0.64502 0.40815 0.38704 0.06723  0.11306  0.00560  67  VAL A N   
538  N N   B VAL A 67  ? 0.64298 0.40680 0.38569 0.06789  0.11312  0.00593  67  VAL A N   
539  C CA  A VAL A 67  ? 0.66337 0.39760 0.39666 0.05146  0.10417  0.00638  67  VAL A CA  
540  C CA  B VAL A 67  ? 0.66259 0.39734 0.39780 0.05360  0.10450  0.00785  67  VAL A CA  
541  C C   A VAL A 67  ? 0.68366 0.37261 0.40136 0.05791  0.10922  0.00513  67  VAL A C   
542  C C   B VAL A 67  ? 0.68582 0.37255 0.40203 0.05945  0.11026  0.00428  67  VAL A C   
543  O O   A VAL A 67  ? 0.69136 0.37174 0.41097 0.07831  0.11482  0.01127  67  VAL A O   
544  O O   B VAL A 67  ? 0.68434 0.35888 0.39980 0.08123  0.11726  0.00776  67  VAL A O   
545  C CB  A VAL A 67  ? 0.61403 0.37165 0.36651 0.04441  0.09479  0.01530  67  VAL A CB  
546  C CB  B VAL A 67  ? 0.57853 0.33425 0.33235 0.05116  0.09739  0.01878  67  VAL A CB  
547  C CG1 A VAL A 67  ? 0.60972 0.37926 0.37209 0.05916  0.09782  0.02556  67  VAL A CG1 
548  C CG1 B VAL A 67  ? 0.57756 0.31173 0.32701 0.03643  0.09283  0.02008  67  VAL A CG1 
549  C CG2 A VAL A 67  ? 0.60548 0.34670 0.35537 0.02808  0.08760  0.01374  67  VAL A CG2 
550  C CG2 B VAL A 67  ? 0.58291 0.37287 0.35089 0.04300  0.09015  0.01828  67  VAL A CG2 
551  N N   . TYR A 68  ? 0.68296 0.34032 0.38317 0.04033  0.10565  -0.00288 68  TYR A N   
552  C CA  . TYR A 68  ? 0.75109 0.35440 0.42974 0.03812  0.10978  -0.00744 68  TYR A CA  
553  C C   . TYR A 68  ? 0.70235 0.29846 0.38508 0.01433  0.10212  -0.00109 68  TYR A C   
554  O O   . TYR A 68  ? 0.70747 0.34226 0.40895 0.00111  0.09319  0.00083  68  TYR A O   
555  C CB  . TYR A 68  ? 0.74115 0.31630 0.39236 0.03192  0.11303  -0.02678 68  TYR A CB  
556  C CG  . TYR A 68  ? 0.78538 0.37089 0.43109 0.05497  0.12552  -0.03574 68  TYR A CG  
557  C CD1 . TYR A 68  ? 0.82007 0.45441 0.47580 0.05395  0.12598  -0.03494 68  TYR A CD1 
558  C CD2 . TYR A 68  ? 0.74489 0.29127 0.37511 0.07734  0.13770  -0.04581 68  TYR A CD2 
559  C CE1 . TYR A 68  ? 0.75279 0.40741 0.40588 0.07056  0.14041  -0.04395 68  TYR A CE1 
560  C CE2 . TYR A 68  ? 0.84511 0.41326 0.47593 0.10066  0.15150  -0.05721 68  TYR A CE2 
561  C CZ  . TYR A 68  ? 0.77011 0.39774 0.41381 0.09492  0.15372  -0.05613 68  TYR A CZ  
562  O OH  . TYR A 68  ? 0.89022 0.54927 0.53683 0.11343  0.17001  -0.06794 68  TYR A OH  
563  N N   . PHE A 69  ? 0.71535 0.26129 0.38027 0.00869  0.10623  0.00163  69  PHE A N   
564  C CA  . PHE A 69  ? 0.81133 0.35506 0.47939 -0.02071 0.10173  0.00653  69  PHE A CA  
565  C C   . PHE A 69  ? 0.90522 0.37941 0.54212 -0.03799 0.10539  0.00042  69  PHE A C   
566  O O   . PHE A 69  ? 0.90789 0.32618 0.52015 -0.01950 0.11240  -0.00216 69  PHE A O   
567  C CB  . PHE A 69  ? 0.81558 0.38438 0.49893 -0.01798 0.10341  0.02630  69  PHE A CB  
568  C CG  . PHE A 69  ? 0.82764 0.35255 0.49165 0.00116  0.11003  0.04211  69  PHE A CG  
569  C CD1 . PHE A 69  ? 0.89322 0.35851 0.53057 -0.01543 0.11381  0.05142  69  PHE A CD1 
570  C CD2 . PHE A 69  ? 0.76129 0.30616 0.43365 0.03435  0.11080  0.04926  69  PHE A CD2 
571  C CE1 . PHE A 69  ? 0.92843 0.34511 0.54316 0.00519  0.11689  0.06969  69  PHE A CE1 
572  C CE2 . PHE A 69  ? 0.81523 0.32417 0.47141 0.05664  0.11298  0.06537  69  PHE A CE2 
573  C CZ  . PHE A 69  ? 0.92059 0.36082 0.54571 0.04423  0.11531  0.07691  69  PHE A CZ  
574  N N   . VAL A 70  ? 0.93098 0.41044 0.57065 -0.07384 0.10035  -0.00336 70  VAL A N   
575  C CA  . VAL A 70  ? 1.00690 0.42418 0.61752 -0.10212 0.10187  -0.01213 70  VAL A CA  
576  C C   . VAL A 70  ? 1.05233 0.45474 0.66093 -0.12566 0.10709  0.00655  70  VAL A C   
577  O O   . VAL A 70  ? 1.03709 0.49736 0.67242 -0.14974 0.10448  0.01021  70  VAL A O   
578  C CB  . VAL A 70  ? 1.08062 0.52323 0.69543 -0.13127 0.09059  -0.03293 70  VAL A CB  
579  C CG1 . VAL A 70  ? 1.03481 0.40465 0.61227 -0.15895 0.09185  -0.04820 70  VAL A CG1 
580  C CG2 . VAL A 70  ? 0.92797 0.40548 0.54801 -0.10926 0.08386  -0.04417 70  VAL A CG2 
581  N N   . SER A 71  ? 1.09905 0.42389 0.67440 -0.11805 0.11482  0.01863  71  SER A N   
582  C CA  . SER A 71  ? 1.16514 0.48096 0.73554 -0.13485 0.11877  0.04149  71  SER A CA  
583  C C   . SER A 71  ? 1.27435 0.52186 0.81671 -0.14558 0.11778  0.03985  71  SER A C   
584  O O   . SER A 71  ? 1.28637 0.48618 0.81175 -0.11350 0.11684  0.03538  71  SER A O   
585  C CB  . SER A 71  ? 1.07794 0.40772 0.65212 -0.09901 0.12124  0.06492  71  SER A CB  
586  O OG  . SER A 71  ? 1.18295 0.47497 0.73795 -0.10091 0.12145  0.08479  71  SER A OG  
587  N N   . ASN A 72  ? 1.28344 0.52911 0.82239 -0.19078 0.11884  0.04330  72  ASN A N   
588  C CA  . ASN A 72  ? 1.34653 0.52575 0.85781 -0.21014 0.11742  0.03833  72  ASN A CA  
589  C C   . ASN A 72  ? 1.35818 0.51161 0.85964 -0.20323 0.11270  0.00889  72  ASN A C   
590  O O   . ASN A 72  ? 1.32530 0.52480 0.84342 -0.21278 0.10888  -0.00937 72  ASN A O   
591  C CB  . ASN A 72  ? 1.43529 0.55315 0.92197 -0.18394 0.11830  0.06068  72  ASN A CB  
592  C CG  . ASN A 72  ? 1.48993 0.63541 0.98085 -0.19338 0.12204  0.09070  72  ASN A CG  
593  O OD1 . ASN A 72  ? 1.44744 0.65568 0.95897 -0.22529 0.12656  0.09281  72  ASN A OD1 
594  N ND2 . ASN A 72  ? 1.40887 0.51128 0.88047 -0.16562 0.11986  0.11341  72  ASN A ND2 
595  N N   . GLY A 73  ? 1.39128 0.47265 0.86496 -0.18528 0.11237  0.00381  73  GLY A N   
596  C CA  . GLY A 73  ? 1.48803 0.54352 0.94775 -0.18703 0.10926  -0.02591 73  GLY A CA  
597  C C   . GLY A 73  ? 1.47629 0.57156 0.94833 -0.15689 0.10873  -0.04305 73  GLY A C   
598  O O   . GLY A 73  ? 1.51706 0.62383 0.98462 -0.17210 0.10434  -0.06763 73  GLY A O   
599  N N   . GLY A 74  ? 1.33930 0.45862 0.82552 -0.11560 0.11254  -0.03026 74  GLY A N   
600  C CA  . GLY A 74  ? 1.17645 0.31337 0.66603 -0.07960 0.11500  -0.04631 74  GLY A CA  
601  C C   . GLY A 74  ? 1.26389 0.46476 0.77979 -0.06121 0.11633  -0.03697 74  GLY A C   
602  O O   . GLY A 74  ? 1.27640 0.50673 0.80907 -0.07001 0.11565  -0.01665 74  GLY A O   
603  N N   . VAL A 75  ? 1.20018 0.42229 0.71776 -0.03709 0.11914  -0.05298 75  VAL A N   
604  C CA  . VAL A 75  ? 1.15167 0.42953 0.69035 -0.01756 0.12115  -0.04826 75  VAL A CA  
605  C C   . VAL A 75  ? 1.11274 0.39269 0.66201 0.02712  0.12781  -0.03428 75  VAL A C   
606  O O   . VAL A 75  ? 1.13998 0.38331 0.67908 0.05109  0.13120  -0.03789 75  VAL A O   
607  C CB  . VAL A 75  ? 1.11394 0.41742 0.64521 -0.01830 0.12092  -0.07226 75  VAL A CB  
608  C CG1 . VAL A 75  ? 1.13435 0.43503 0.65302 -0.06124 0.11015  -0.08641 75  VAL A CG1 
609  C CG2 . VAL A 75  ? 1.21091 0.49256 0.72824 0.01038  0.12982  -0.08816 75  VAL A CG2 
610  N N   . TYR A 76  ? 0.97261 0.30029 0.54514 0.03901  0.12788  -0.01882 76  TYR A N   
611  C CA  . TYR A 76  ? 0.99665 0.33632 0.58236 0.07834  0.13108  -0.00303 76  TYR A CA  
612  C C   . TYR A 76  ? 0.86964 0.29787 0.49040 0.08978  0.12985  -0.00174 76  TYR A C   
613  O O   . TYR A 76  ? 0.83578 0.30975 0.47018 0.06616  0.12462  -0.00555 76  TYR A O   
614  C CB  . TYR A 76  ? 1.00952 0.33206 0.59372 0.07260  0.12596  0.02468  76  TYR A CB  
615  C CG  . TYR A 76  ? 1.10058 0.35874 0.66083 0.06194  0.12348  0.02586  76  TYR A CG  
616  C CD1 . TYR A 76  ? 1.15369 0.37505 0.70550 0.09634  0.12364  0.02455  76  TYR A CD1 
617  C CD2 . TYR A 76  ? 1.11657 0.35176 0.66424 0.01733  0.12082  0.02753  76  TYR A CD2 
618  C CE1 . TYR A 76  ? 1.15467 0.30763 0.68201 0.08717  0.12057  0.02594  76  TYR A CE1 
619  C CE2 . TYR A 76  ? 1.22375 0.39593 0.74760 0.00474  0.11892  0.02875  76  TYR A CE2 
620  C CZ  . TYR A 76  ? 1.21068 0.33678 0.72238 0.04012  0.11851  0.02847  76  TYR A CZ  
621  O OH  . TYR A 76  ? 1.27230 0.32714 0.75806 0.02818  0.11595  0.03008  76  TYR A OH  
622  N N   . LYS A 77  ? 0.93407 0.38440 0.56897 0.12680  0.13365  0.00350  77  LYS A N   
623  C CA  . LYS A 77  ? 0.85351 0.38414 0.51990 0.13711  0.13411  0.00318  77  LYS A CA  
624  C C   . LYS A 77  ? 0.86238 0.42880 0.54922 0.14429  0.12605  0.02658  77  LYS A C   
625  O O   . LYS A 77  ? 0.83925 0.37851 0.51964 0.16773  0.12392  0.04066  77  LYS A O   
626  C CB  . LYS A 77  ? 0.88680 0.42960 0.55760 0.17108  0.14555  -0.01245 77  LYS A CB  
627  C CG  . LYS A 77  ? 0.85592 0.48311 0.55954 0.18055  0.14851  -0.01317 77  LYS A CG  
628  C CD  . LYS A 77  ? 0.81521 0.45658 0.51345 0.18965  0.16379  -0.03746 77  LYS A CD  
629  C CE  . LYS A 77  ? 0.91839 0.59764 0.64099 0.23233  0.17305  -0.04259 77  LYS A CE  
630  N NZ  . LYS A 77  ? 0.93935 0.68498 0.67551 0.22963  0.18792  -0.05952 77  LYS A NZ  
631  N N   . ALA A 78  ? 0.81182 0.43321 0.51853 0.12425  0.12030  0.03070  78  ALA A N   
632  C CA  . ALA A 78  ? 0.75821 0.41647 0.48043 0.12638  0.11275  0.04888  78  ALA A CA  
633  C C   . ALA A 78  ? 0.76047 0.46744 0.50451 0.15595  0.11292  0.05025  78  ALA A C   
634  O O   . ALA A 78  ? 0.74073 0.50649 0.50713 0.14996  0.11165  0.04546  78  ALA A O   
635  C CB  . ALA A 78  ? 0.69115 0.38777 0.42654 0.09796  0.10723  0.04768  78  ALA A CB  
636  N N   . ALA A 79  ? 0.77488 0.45590 0.51246 0.18834  0.11383  0.05627  79  ALA A N   
637  C CA  . ALA A 79  ? 0.80698 0.54180 0.57016 0.22091  0.11207  0.05785  79  ALA A CA  
638  C C   . ALA A 79  ? 0.88192 0.58062 0.63222 0.25330  0.10394  0.07718  79  ALA A C   
639  O O   . ALA A 79  ? 0.93445 0.55607 0.65173 0.24905  0.10311  0.08712  79  ALA A O   
640  C CB  . ALA A 79  ? 0.79766 0.55387 0.57395 0.23654  0.12501  0.03548  79  ALA A CB  
641  N N   . ILE A 80  ? 0.91029 0.66599 0.68567 0.28375  0.09635  0.08389  80  ILE A N   
642  C CA  . ILE A 80  ? 0.91833 0.64763 0.68329 0.32263  0.08447  0.10464  80  ILE A CA  
643  C C   . ILE A 80  ? 0.95243 0.75034 0.75621 0.36599  0.08239  0.09627  80  ILE A C   
644  O O   . ILE A 80  ? 0.92116 0.81071 0.76071 0.35727  0.08112  0.08851  80  ILE A O   
645  C CB  . ILE A 80  ? 0.93554 0.67513 0.68636 0.31004  0.06881  0.13178  80  ILE A CB  
646  C CG1 . ILE A 80  ? 0.89620 0.58711 0.61592 0.26487  0.07326  0.13774  80  ILE A CG1 
647  C CG2 . ILE A 80  ? 0.92421 0.62813 0.65617 0.35147  0.05407  0.15735  80  ILE A CG2 
648  C CD1 . ILE A 80  ? 0.81514 0.50942 0.51296 0.25378  0.06144  0.16418  80  ILE A CD1 
649  N N   . ALA A 81  ? 1.09317 0.84806 0.89115 0.41153  0.08190  0.09635  81  ALA A N   
650  C CA  . ALA A 81  ? 0.99453 0.82159 0.83341 0.45106  0.07485  0.09013  81  ALA A CA  
651  C C   . ALA A 81  ? 1.05749 0.88635 0.88960 0.46934  0.04973  0.11913  81  ALA A C   
652  O O   . ALA A 81  ? 1.11525 0.85798 0.90773 0.46581  0.04148  0.13684  81  ALA A O   
653  C CB  . ALA A 81  ? 1.06409 0.85730 0.90690 0.47365  0.08491  0.06746  81  ALA A CB  
654  N N   . GLY A 82  ? 1.07176 1.00125 0.94138 0.48396  0.03718  0.12348  82  GLY A N   
655  C CA  . GLY A 82  ? 1.15898 1.09607 1.01965 0.49898  0.01150  0.15026  82  GLY A CA  
656  C C   . GLY A 82  ? 1.08468 1.13860 0.99459 0.52257  -0.00393 0.14797  82  GLY A C   
657  O O   . GLY A 82  ? 1.01640 1.16492 0.96311 0.50846  0.00116  0.13408  82  GLY A O   
658  N N   . GLU A 83  ? 1.03895 1.08738 0.95063 0.55609  -0.02375 0.16130  83  GLU A N   
659  C CA  . GLU A 83  ? 0.96872 1.12328 0.92131 0.57652  -0.04422 0.16392  83  GLU A CA  
660  C C   . GLU A 83  ? 0.94960 1.20184 0.96461 0.58829  -0.03023 0.13163  83  GLU A C   
661  O O   . GLU A 83  ? 0.97161 1.21344 1.00643 0.62129  -0.02447 0.11779  83  GLU A O   
662  C CB  . GLU A 83  ? 0.94388 1.14243 0.88136 0.54432  -0.05892 0.18139  83  GLU A CB  
663  C CG  . GLU A 83  ? 0.94112 1.27630 0.92577 0.53500  -0.06999 0.17119  83  GLU A CG  
664  C CD  . GLU A 83  ? 0.99153 1.37869 0.98987 0.56087  -0.09942 0.18482  83  GLU A CD  
665  O OE1 . GLU A 83  ? 1.04153 1.36152 1.01760 0.59273  -0.11194 0.20281  83  GLU A OE1 
666  O OE2 . GLU A 83  ? 0.86125 1.35552 0.89163 0.54664  -0.11122 0.17749  83  GLU A OE2 
667  N N   . SER A 84  ? 0.99837 1.34342 1.04390 0.55863  -0.02316 0.11817  84  SER A N   
668  C CA  . SER A 84  ? 0.93518 1.37038 1.03536 0.55632  -0.00535 0.08731  84  SER A CA  
669  C C   . SER A 84  ? 0.99755 1.44060 1.09678 0.51379  0.01926  0.07151  84  SER A C   
670  O O   . SER A 84  ? 0.95310 1.45794 1.08885 0.50273  0.03888  0.04579  84  SER A O   
671  C CB  . SER A 84  ? 0.94586 1.51208 1.09713 0.55796  -0.02249 0.08302  84  SER A CB  
672  O OG  . SER A 84  ? 0.96534 1.52619 1.11376 0.59537  -0.04959 0.10180  84  SER A OG  
673  N N   . GLY A 85  ? 0.88604 1.26769 0.94361 0.48831  0.01941  0.08636  85  GLY A N   
674  C CA  . GLY A 85  ? 0.94970 1.32113 0.99948 0.43939  0.04126  0.07116  85  GLY A CA  
675  C C   . GLY A 85  ? 0.95009 1.20361 0.95532 0.43286  0.05873  0.06885  85  GLY A C   
676  O O   . GLY A 85  ? 0.91224 1.08025 0.88451 0.46284  0.05228  0.08435  85  GLY A O   
677  N N   . PHE A 86  ? 0.89220 1.13943 0.89393 0.39188  0.07971  0.05001  86  PHE A N   
678  C CA  . PHE A 86  ? 0.87947 1.02530 0.83848 0.37377  0.09401  0.04608  86  PHE A CA  
679  C C   . PHE A 86  ? 0.86656 1.00093 0.80726 0.31649  0.09470  0.04733  86  PHE A C   
680  O O   . PHE A 86  ? 0.82138 1.00757 0.78006 0.28555  0.10379  0.03334  86  PHE A O   
681  C CB  . PHE A 86  ? 0.90899 1.05421 0.87666 0.38522  0.11798  0.02043  86  PHE A CB  
682  C CG  . PHE A 86  ? 0.99692 1.03804 0.91863 0.37068  0.12961  0.01500  86  PHE A CG  
683  C CD1 . PHE A 86  ? 1.08955 1.04117 0.98183 0.40307  0.12698  0.02075  86  PHE A CD1 
684  C CD2 . PHE A 86  ? 0.97151 1.00243 0.87762 0.32392  0.14147  0.00429  86  PHE A CD2 
685  C CE1 . PHE A 86  ? 1.07345 0.93271 0.92371 0.38453  0.13669  0.01343  86  PHE A CE1 
686  C CE2 . PHE A 86  ? 1.06290 1.00718 0.92863 0.30966  0.14928  -0.00171 86  PHE A CE2 
687  C CZ  . PHE A 86  ? 1.10500 0.96624 0.94397 0.33792  0.14730  0.00152  86  PHE A CZ  
688  N N   . TYR A 87  ? 0.82499 0.89048 0.72920 0.30295  0.08565  0.06400  87  TYR A N   
689  C CA  . TYR A 87  ? 0.74940 0.80345 0.63765 0.25658  0.08394  0.06553  87  TYR A CA  
690  C C   . TYR A 87  ? 0.75736 0.73931 0.61766 0.23475  0.09669  0.05752  87  TYR A C   
691  O O   . TYR A 87  ? 0.83820 0.75661 0.67768 0.25193  0.10212  0.05804  87  TYR A O   
692  C CB  . TYR A 87  ? 0.67352 0.71245 0.54173 0.25359  0.06713  0.08693  87  TYR A CB  
693  C CG  . TYR A 87  ? 0.68124 0.77998 0.56758 0.28177  0.04993  0.09909  87  TYR A CG  
694  C CD1 . TYR A 87  ? 0.71599 0.80639 0.60681 0.32996  0.04401  0.10874  87  TYR A CD1 
695  C CD2 . TYR A 87  ? 0.59733 0.75946 0.49465 0.26165  0.03760  0.10002  87  TYR A CD2 
696  C CE1 . TYR A 87  ? 0.68777 0.83807 0.59655 0.35881  0.02466  0.12102  87  TYR A CE1 
697  C CE2 . TYR A 87  ? 0.57803 0.80139 0.49101 0.28556  0.01893  0.11049  87  TYR A CE2 
698  C CZ  . TYR A 87  ? 0.61195 0.83222 0.53179 0.33526  0.01141  0.12240  87  TYR A CZ  
699  O OH  . TYR A 87  ? 0.63117 0.91687 0.56777 0.36343  -0.01102 0.13457  87  TYR A OH  
700  N N   . LYS A 88  ? 0.60965 0.60014 0.46844 0.19696  0.09973  0.04947  88  LYS A N   
701  C CA  . LYS A 88  ? 0.65339 0.58513 0.48755 0.17528  0.10735  0.04285  88  LYS A CA  
702  C C   . LYS A 88  ? 0.60906 0.54802 0.44063 0.14036  0.10176  0.04222  88  LYS A C   
703  O O   . LYS A 88  ? 0.56182 0.55070 0.41070 0.12828  0.09744  0.03962  88  LYS A O   
704  C CB  . LYS A 88  ? 0.62627 0.55713 0.46071 0.17637  0.12238  0.02544  88  LYS A CB  
705  C CG  . LYS A 88  ? 0.64985 0.64770 0.50701 0.16125  0.12818  0.01566  88  LYS A CG  
706  C CD  . LYS A 88  ? 0.68347 0.67992 0.53345 0.16074  0.14587  -0.00081 88  LYS A CD  
707  C CE  . LYS A 88  ? 0.75334 0.79763 0.61135 0.12948  0.15215  -0.00682 88  LYS A CE  
708  N NZ  . LYS A 88  ? 0.67695 0.68256 0.50274 0.10421  0.15934  -0.01325 88  LYS A NZ  
709  N N   . LEU A 89  ? 0.53421 0.42285 0.34480 0.12474  0.10136  0.04311  89  LEU A N   
710  C CA  . LEU A 89  ? 0.48934 0.37915 0.29836 0.09716  0.09649  0.03934  89  LEU A CA  
711  C C   . LEU A 89  ? 0.60005 0.48412 0.40516 0.08286  0.10161  0.02770  89  LEU A C   
712  O O   . LEU A 89  ? 0.63272 0.48746 0.42404 0.08697  0.10887  0.02223  89  LEU A O   
713  C CB  . LEU A 89  ? 0.56826 0.41911 0.36177 0.08834  0.09365  0.04497  89  LEU A CB  
714  C CG  . LEU A 89  ? 0.60600 0.46480 0.40261 0.06804  0.08765  0.04158  89  LEU A CG  
715  C CD1 . LEU A 89  ? 0.54378 0.44399 0.35105 0.06854  0.08202  0.04356  89  LEU A CD1 
716  C CD2 . LEU A 89  ? 0.58172 0.41133 0.36656 0.05995  0.08862  0.04655  89  LEU A CD2 
717  N N   . VAL A 90  ? 0.54314 0.45111 0.35546 0.06542  0.09754  0.02401  90  VAL A N   
718  C CA  . VAL A 90  ? 0.50011 0.40590 0.30433 0.04972  0.10148  0.01740  90  VAL A CA  
719  C C   . VAL A 90  ? 0.55324 0.42628 0.34429 0.03343  0.09162  0.01673  90  VAL A C   
720  O O   . VAL A 90  ? 0.51112 0.38736 0.30992 0.02922  0.08256  0.01760  90  VAL A O   
721  C CB  . VAL A 90  ? 0.52022 0.47193 0.33906 0.03892  0.10336  0.01555  90  VAL A CB  
722  C CG1 . VAL A 90  ? 0.55273 0.49469 0.35508 0.01579  0.10729  0.01268  90  VAL A CG1 
723  C CG2 . VAL A 90  ? 0.56621 0.56341 0.40512 0.05840  0.11181  0.01460  90  VAL A CG2 
724  N N   . PRO A 91  ? 0.61568 0.46050 0.38703 0.02613  0.09215  0.01392  91  PRO A N   
725  C CA  . PRO A 91  ? 0.53883 0.35620 0.30044 0.01643  0.07943  0.01375  91  PRO A CA  
726  C C   . PRO A 91  ? 0.60017 0.41420 0.35814 0.00330  0.06937  0.01564  91  PRO A C   
727  O O   . PRO A 91  ? 0.58154 0.37088 0.31993 -0.00539 0.06108  0.01742  91  PRO A O   
728  C CB  . PRO A 91  ? 0.63709 0.42906 0.37483 0.01351  0.08234  0.00991  91  PRO A CB  
729  C CG  . PRO A 91  ? 0.61726 0.42443 0.34742 0.01496  0.09726  0.00730  91  PRO A CG  
730  C CD  . PRO A 91  ? 0.53877 0.37849 0.29506 0.02945  0.10436  0.00893  91  PRO A CD  
731  N N   . THR A 92  ? 0.54797 0.38246 0.32108 0.00161  0.06841  0.01550  92  THR A N   
732  C CA  . THR A 92  ? 0.53520 0.35387 0.30440 -0.00867 0.05669  0.01498  92  THR A CA  
733  C C   . THR A 92  ? 0.52842 0.33678 0.30792 0.00188  0.04544  0.01021  92  THR A C   
734  O O   . THR A 92  ? 0.49648 0.31593 0.28655 0.01152  0.04860  0.00866  92  THR A O   
735  C CB  . THR A 92  ? 0.55156 0.39495 0.33111 -0.01782 0.05962  0.01263  92  THR A CB  
736  O OG1 . THR A 92  ? 0.48012 0.35832 0.27993 -0.00509 0.06420  0.01001  92  THR A OG1 
737  C CG2 . THR A 92  ? 0.54892 0.40865 0.32032 -0.03325 0.07063  0.01637  92  THR A CG2 
738  N N   . ILE A 93  ? 0.55037 0.33642 0.32613 -0.00020 0.03279  0.00744  93  ILE A N   
739  C CA  . ILE A 93  ? 0.62530 0.41137 0.41665 0.01311  0.02343  -0.00125 93  ILE A CA  
740  C C   . ILE A 93  ? 0.59616 0.38647 0.39488 0.01280  0.02220  -0.01118 93  ILE A C   
741  O O   . ILE A 93  ? 0.66337 0.42181 0.44883 0.00577  0.01384  -0.01247 93  ILE A O   
742  C CB  . ILE A 93  ? 0.63288 0.38868 0.41566 0.01908  0.00668  0.00037  93  ILE A CB  
743  C CG1 . ILE A 93  ? 0.61148 0.36256 0.37949 0.01437  0.00682  0.00875  93  ILE A CG1 
744  C CG2 . ILE A 93  ? 0.61937 0.39215 0.42778 0.03649  -0.00062 -0.01149 93  ILE A CG2 
745  C CD1 . ILE A 93  ? 0.79797 0.52758 0.55738 0.02125  -0.01336 0.01137  93  ILE A CD1 
746  N N   . PRO A 94  ? 0.61497 0.43939 0.42924 0.01800  0.02992  -0.01832 94  PRO A N   
747  C CA  . PRO A 94  ? 0.49296 0.34644 0.31650 0.02314  0.04000  -0.01377 94  PRO A CA  
748  C C   . PRO A 94  ? 0.48772 0.35306 0.30522 0.01796  0.04931  -0.00336 94  PRO A C   
749  O O   . PRO A 94  ? 0.46132 0.32566 0.27282 0.00850  0.04940  -0.00208 94  PRO A O   
750  C CB  . PRO A 94  ? 0.55544 0.43598 0.38934 0.02816  0.04322  -0.02424 94  PRO A CB  
751  C CG  . PRO A 94  ? 0.48087 0.35482 0.30856 0.02144  0.03856  -0.03306 94  PRO A CG  
752  C CD  . PRO A 94  ? 0.55220 0.38333 0.36947 0.01676  0.02854  -0.03150 94  PRO A CD  
753  N N   . PRO A 95  ? 0.53194 0.40763 0.35120 0.02394  0.05714  0.00340  95  PRO A N   
754  C CA  . PRO A 95  ? 0.49697 0.38305 0.31289 0.02667  0.06532  0.01162  95  PRO A CA  
755  C C   . PRO A 95  ? 0.51217 0.43102 0.33501 0.02602  0.06569  0.01114  95  PRO A C   
756  O O   . PRO A 95  ? 0.46895 0.40391 0.29526 0.02548  0.06202  0.00633  95  PRO A O   
757  C CB  . PRO A 95  ? 0.41904 0.30054 0.23292 0.03499  0.07107  0.01826  95  PRO A CB  
758  C CG  . PRO A 95  ? 0.44854 0.31414 0.26321 0.02985  0.06703  0.01356  95  PRO A CG  
759  C CD  . PRO A 95  ? 0.51843 0.39076 0.34142 0.02734  0.05841  0.00369  95  PRO A CD  
760  N N   A THR A 96  ? 0.48982 0.42446 0.31503 0.02517  0.07037  0.01419  96  THR A N   
761  N N   B THR A 96  ? 0.48391 0.41841 0.30908 0.02531  0.07044  0.01426  96  THR A N   
762  C CA  A THR A 96  ? 0.49551 0.47373 0.33244 0.02589  0.06996  0.01436  96  THR A CA  
763  C CA  B THR A 96  ? 0.49591 0.47380 0.33277 0.02546  0.07004  0.01424  96  THR A CA  
764  C C   A THR A 96  ? 0.49581 0.49258 0.33904 0.04587  0.07639  0.02297  96  THR A C   
765  C C   B THR A 96  ? 0.49554 0.49197 0.33867 0.04572  0.07640  0.02291  96  THR A C   
766  O O   A THR A 96  ? 0.46921 0.44037 0.30538 0.05479  0.08340  0.02573  96  THR A O   
767  O O   B THR A 96  ? 0.46645 0.43656 0.30226 0.05488  0.08324  0.02586  96  THR A O   
768  C CB  A THR A 96  ? 0.49963 0.49278 0.34008 0.00557  0.06946  0.00826  96  THR A CB  
769  C CB  B THR A 96  ? 0.50069 0.49144 0.34035 0.00505  0.06995  0.00840  96  THR A CB  
770  O OG1 A THR A 96  ? 0.50161 0.54811 0.35802 0.00430  0.06748  0.00670  96  THR A OG1 
771  O OG1 B THR A 96  ? 0.51112 0.47574 0.33963 -0.00124 0.07614  0.01044  96  THR A OG1 
772  C CG2 A THR A 96  ? 0.50381 0.48875 0.33923 0.00149  0.07899  0.01099  96  THR A CG2 
773  C CG2 B THR A 96  ? 0.51627 0.48875 0.34912 -0.01164 0.06062  -0.00084 96  THR A CG2 
774  N N   . ILE A 97  ? 0.44253 0.48223 0.29748 0.05455  0.07239  0.02615  97  ILE A N   
775  C CA  . ILE A 97  ? 0.47415 0.53214 0.33664 0.08045  0.07500  0.03527  97  ILE A CA  
776  C C   . ILE A 97  ? 0.58496 0.69171 0.46973 0.08156  0.08012  0.02946  97  ILE A C   
777  O O   . ILE A 97  ? 0.56907 0.71114 0.46508 0.05954  0.07788  0.02154  97  ILE A O   
778  C CB  . ILE A 97  ? 0.52273 0.60142 0.38260 0.09376  0.06481  0.04556  97  ILE A CB  
779  C CG1 . ILE A 97  ? 0.55869 0.63301 0.41817 0.12630  0.06522  0.05922  97  ILE A CG1 
780  C CG2 . ILE A 97  ? 0.54815 0.68776 0.42381 0.08373  0.05538  0.03940  97  ILE A CG2 
781  C CD1 . ILE A 97  ? 0.52508 0.61473 0.37402 0.14033  0.05258  0.07475  97  ILE A CD1 
782  N N   . GLU A 98  ? 0.53250 0.64174 0.42367 0.10615  0.08821  0.03170  98  GLU A N   
783  C CA  . GLU A 98  ? 0.62886 0.79885 0.54720 0.11305  0.09520  0.02474  98  GLU A CA  
784  C C   . GLU A 98  ? 0.65097 0.84934 0.58538 0.15346  0.09040  0.03224  98  GLU A C   
785  O O   . GLU A 98  ? 0.65766 0.80790 0.57737 0.17970  0.09355  0.03805  98  GLU A O   
786  C CB  . GLU A 98  ? 0.66255 0.81506 0.57429 0.10690  0.11249  0.01537  98  GLU A CB  
787  C CG  . GLU A 98  ? 0.76236 0.98159 0.69726 0.08957  0.12242  0.00532  98  GLU A CG  
788  C CD  . GLU A 98  ? 0.73913 0.92890 0.65130 0.05815  0.13403  -0.00008 98  GLU A CD  
789  O OE1 . GLU A 98  ? 0.79680 0.96304 0.69418 0.02653  0.12653  0.00234  98  GLU A OE1 
790  O OE2 . GLU A 98  ? 0.66137 0.84924 0.56738 0.06643  0.15008  -0.00699 98  GLU A OE2 
791  N N   A ILE A 99  ? 0.66645 0.94184 0.63045 0.15800  0.08171  0.03150  99  ILE A N   
792  N N   B ILE A 99  ? 0.66867 0.94051 0.63067 0.15883  0.08036  0.03280  99  ILE A N   
793  C CA  A ILE A 99  ? 0.64996 0.96786 0.63503 0.19947  0.07244  0.03931  99  ILE A CA  
794  C CA  B ILE A 99  ? 0.65398 0.96176 0.63566 0.20253  0.07330  0.04021  99  ILE A CA  
795  C C   A ILE A 99  ? 0.68977 1.07988 0.71422 0.21106  0.08488  0.02503  99  ILE A C   
796  C C   B ILE A 99  ? 0.69239 1.07593 0.71395 0.20970  0.08548  0.02515  99  ILE A C   
797  O O   A ILE A 99  ? 0.70735 1.17780 0.76189 0.18976  0.08308  0.01640  99  ILE A O   
798  O O   B ILE A 99  ? 0.70910 1.16261 0.75550 0.18145  0.08557  0.01576  99  ILE A O   
799  C CB  A ILE A 99  ? 0.65068 1.01573 0.64196 0.19585  0.05075  0.04780  99  ILE A CB  
800  C CB  B ILE A 99  ? 0.66323 1.00542 0.64654 0.20920  0.05055  0.05309  99  ILE A CB  
801  C CG1 A ILE A 99  ? 0.66028 0.96100 0.61132 0.17828  0.04326  0.05768  99  ILE A CG1 
802  C CG1 B ILE A 99  ? 0.62072 1.06869 0.64441 0.20214  0.04127  0.04473  99  ILE A CG1 
803  C CG2 A ILE A 99  ? 0.62404 1.03307 0.63493 0.24277  0.03679  0.05923  99  ILE A CG2 
804  C CG2 B ILE A 99  ? 0.66185 0.95736 0.61164 0.17679  0.04479  0.05698  99  ILE A CG2 
805  C CD1 A ILE A 99  ? 0.60607 0.95097 0.55539 0.16298  0.02510  0.05970  99  ILE A CD1 
806  C CD1 B ILE A 99  ? 0.60098 1.08999 0.62695 0.22228  0.01618  0.05872  99  ILE A CD1 
807  N N   . ASN A 100 ? 0.86725 0.94239 0.84209 0.21830  0.23821  -0.35481 100 ASN A N   
808  C CA  . ASN A 100 ? 0.89843 0.97520 0.82943 0.23090  0.26611  -0.35834 100 ASN A CA  
809  C C   . ASN A 100 ? 0.93203 1.00502 0.80118 0.23352  0.27783  -0.35562 100 ASN A C   
810  O O   . ASN A 100 ? 0.99811 1.05963 0.81320 0.24550  0.27642  -0.37703 100 ASN A O   
811  C CB  . ASN A 100 ? 0.87012 0.96877 0.83193 0.23315  0.29046  -0.33496 100 ASN A CB  
812  C CG  . ASN A 100 ? 0.88572 0.98950 0.90305 0.23331  0.28050  -0.33079 100 ASN A CG  
813  O OD1 . ASN A 100 ? 0.92758 1.02284 0.94947 0.24337  0.28557  -0.34389 100 ASN A OD1 
814  N ND2 . ASN A 100 ? 0.81241 0.92861 0.86900 0.22526  0.26838  -0.31126 100 ASN A ND2 
815  N N   . GLY A 101 ? 0.96456 1.05165 0.84423 0.22440  0.28880  -0.32992 101 GLY A N   
816  C CA  . GLY A 101 ? 0.92296 1.00597 0.75558 0.22426  0.30047  -0.32214 101 GLY A CA  
817  C C   . GLY A 101 ? 0.94692 1.04969 0.81786 0.21066  0.30133  -0.29778 101 GLY A C   
818  O O   . GLY A 101 ? 0.84881 0.97788 0.75090 0.21196  0.32737  -0.27799 101 GLY A O   
819  N N   . ILE A 102 ? 1.03514 1.13355 0.91319 0.19886  0.26965  -0.30145 102 ILE A N   
820  C CA  . ILE A 102 ? 1.06640 1.18440 0.98420 0.18344  0.26626  -0.28357 102 ILE A CA  
821  C C   . ILE A 102 ? 1.08020 1.18244 0.96036 0.17950  0.24657  -0.28671 102 ILE A C   
822  O O   . ILE A 102 ? 1.06997 1.15108 0.91462 0.18603  0.22030  -0.30592 102 ILE A O   
823  C CB  . ILE A 102 ? 1.11597 1.25105 1.10716 0.17167  0.24426  -0.28002 102 ILE A CB  
824  C CG1 . ILE A 102 ? 1.15547 1.31584 1.18636 0.17552  0.26313  -0.27319 102 ILE A CG1 
825  C CG2 . ILE A 102 ? 0.97834 1.12687 1.00509 0.15635  0.22855  -0.26941 102 ILE A CG2 
826  C CD1 . ILE A 102 ? 1.00336 1.17643 1.08738 0.17336  0.24266  -0.26808 102 ILE A CD1 
827  N N   . ALA A 103 ? 1.06471 1.18177 0.95954 0.16927  0.25815  -0.26920 103 ALA A N   
828  C CA  . ALA A 103 ? 1.11730 1.22422 0.98834 0.16312  0.23715  -0.26819 103 ALA A CA  
829  C C   . ALA A 103 ? 0.87249 0.96974 0.77928 0.15317  0.19250  -0.27985 103 ALA A C   
830  O O   . ALA A 103 ? 0.84794 0.94400 0.76661 0.14266  0.17515  -0.27455 103 ALA A O   
831  C CB  . ALA A 103 ? 1.07794 1.20627 0.98282 0.14815  0.26333  -0.24721 103 ALA A CB  
832  N N   . MET A 110 ? 1.30929 1.19397 0.61778 0.23464  0.15418  0.06347  110 MET A N   
833  C CA  . MET A 110 ? 1.24562 1.14622 0.55633 0.23369  0.10776  0.00393  110 MET A CA  
834  C C   . MET A 110 ? 1.19160 1.09972 0.60037 0.18990  0.12717  -0.00360 110 MET A C   
835  O O   . MET A 110 ? 1.16800 1.07113 0.65645 0.15024  0.14652  0.02098  110 MET A O   
836  C CB  . MET A 110 ? 1.31339 1.21317 0.63954 0.22147  0.03517  -0.03388 110 MET A CB  
837  C CG  . MET A 110 ? 1.20774 1.09876 0.63269 0.16642  0.01542  -0.03745 110 MET A CG  
838  S SD  . MET A 110 ? 1.32469 1.22030 0.79588 0.15642  -0.05588 -0.10133 110 MET A SD  
839  C CE  . MET A 110 ? 1.00697 0.92191 0.49910 0.16248  -0.04050 -0.13538 110 MET A CE  
840  N N   A ASN A 111 ? 1.08791 1.01230 0.49917 0.19850  0.11874  -0.04146 111 ASN A N   
841  N N   B ASN A 111 ? 1.08778 1.01221 0.49921 0.19845  0.11888  -0.04143 111 ASN A N   
842  C CA  A ASN A 111 ? 1.02245 0.95953 0.52068 0.16656  0.14413  -0.04557 111 ASN A CA  
843  C CA  B ASN A 111 ? 1.02185 0.95888 0.52093 0.16612  0.14417  -0.04536 111 ASN A CA  
844  C C   A ASN A 111 ? 0.96632 0.91143 0.53889 0.13567  0.09634  -0.08564 111 ASN A C   
845  C C   B ASN A 111 ? 0.96601 0.91109 0.53883 0.13553  0.09616  -0.08566 111 ASN A C   
846  O O   A ASN A 111 ? 0.91331 0.85842 0.56173 0.10036  0.09061  -0.07594 111 ASN A O   
847  O O   B ASN A 111 ? 0.91290 0.85797 0.56153 0.10025  0.09016  -0.07615 111 ASN A O   
848  C CB  A ASN A 111 ? 0.97676 0.92549 0.43401 0.19848  0.18318  -0.05005 111 ASN A CB  
849  C CB  B ASN A 111 ? 0.97670 0.92550 0.43707 0.19712  0.18425  -0.04925 111 ASN A CB  
850  C CG  A ASN A 111 ? 0.96754 0.92338 0.49631 0.17772  0.24515  -0.02136 111 ASN A CG  
851  C CG  B ASN A 111 ? 1.04516 0.99269 0.38850 0.25445  0.17680  -0.05616 111 ASN A CG  
852  O OD1 A ASN A 111 ? 0.85223 0.81606 0.48051 0.13528  0.24281  -0.02165 111 ASN A OD1 
853  O OD1 B ASN A 111 ? 1.07321 1.01335 0.37709 0.26850  0.14708  -0.04964 111 ASN A OD1 
854  N ND2 A ASN A 111 ? 1.00446 0.95981 0.48670 0.21185  0.30149  0.00117  111 ASN A ND2 
855  N ND2 B ASN A 111 ? 1.09365 1.05450 0.42064 0.27588  0.19227  -0.06839 111 ASN A ND2 
856  N N   . PRO A 112 ? 1.00761 0.95952 0.56417 0.15207  0.06330  -0.13096 112 PRO A N   
857  C CA  . PRO A 112 ? 0.78916 0.74977 0.42743 0.12842  0.04389  -0.15999 112 PRO A CA  
858  C C   . PRO A 112 ? 0.82490 0.77467 0.52573 0.10170  0.00842  -0.16215 112 PRO A C   
859  O O   . PRO A 112 ? 0.75744 0.71356 0.52296 0.07720  0.01843  -0.14652 112 PRO A O   
860  C CB  . PRO A 112 ? 0.94932 0.91614 0.55597 0.15694  0.02226  -0.20773 112 PRO A CB  
861  C CG  . PRO A 112 ? 1.00113 0.96544 0.50490 0.19802  0.01504  -0.21141 112 PRO A CG  
862  C CD  . PRO A 112 ? 1.01944 0.97090 0.49384 0.19341  0.03260  -0.16216 112 PRO A CD  
863  N N   . LEU A 113 ? 0.83660 0.77284 0.52458 0.10994  -0.03313 -0.18477 113 LEU A N   
864  C CA  . LEU A 113 ? 0.78339 0.70649 0.53936 0.08800  -0.06047 -0.18585 113 LEU A CA  
865  C C   . LEU A 113 ? 0.75303 0.66737 0.51893 0.06657  -0.05462 -0.14429 113 LEU A C   
866  O O   . LEU A 113 ? 0.65073 0.55993 0.47677 0.04886  -0.06408 -0.13589 113 LEU A O   
867  C CB  . LEU A 113 ? 0.75243 0.66380 0.51113 0.10151  -0.10305 -0.22479 113 LEU A CB  
868  C CG  . LEU A 113 ? 0.83945 0.75135 0.52942 0.12307  -0.12313 -0.22980 113 LEU A CG  
869  C CD1 . LEU A 113 ? 0.88653 0.78179 0.59377 0.10837  -0.14510 -0.20956 113 LEU A CD1 
870  C CD2 . LEU A 113 ? 0.86169 0.79084 0.57286 0.14106  -0.14250 -0.26701 113 LEU A CD2 
871  N N   . GLN A 114 ? 0.76005 0.67269 0.47022 0.07174  -0.03476 -0.11651 114 GLN A N   
872  C CA  . GLN A 114 ? 0.72404 0.63132 0.45904 0.04909  -0.02015 -0.07845 114 GLN A CA  
873  C C   . GLN A 114 ? 0.67097 0.59867 0.47442 0.03037  0.00637  -0.07217 114 GLN A C   
874  O O   . GLN A 114 ? 0.61012 0.54016 0.46673 0.01106  0.00026  -0.06095 114 GLN A O   
875  C CB  . GLN A 114 ? 0.82492 0.72480 0.49458 0.06255  0.00763  -0.04655 114 GLN A CB  
876  C CG  . GLN A 114 ? 0.65305 0.54380 0.35382 0.03960  0.02412  -0.00861 114 GLN A CG  
877  C CD  . GLN A 114 ? 0.70818 0.58204 0.42340 0.02662  -0.01844 -0.00867 114 GLN A CD  
878  O OE1 . GLN A 114 ? 0.78670 0.64789 0.45182 0.04375  -0.04764 -0.01742 114 GLN A OE1 
879  N NE2 . GLN A 114 ? 0.51556 0.39199 0.30122 0.00019  -0.02317 -0.00189 114 GLN A NE2 
880  N N   . ASP A 115 ? 0.67044 0.61665 0.47443 0.03951  0.03404  -0.08295 115 ASP A N   
881  C CA  . ASP A 115 ? 0.62070 0.59325 0.49542 0.02538  0.05758  -0.08342 115 ASP A CA  
882  C C   . ASP A 115 ? 0.47685 0.45902 0.40854 0.01983  0.02844  -0.10070 115 ASP A C   
883  O O   . ASP A 115 ? 0.40695 0.40887 0.39688 0.00902  0.03046  -0.09764 115 ASP A O   
884  C CB  . ASP A 115 ? 0.64470 0.63473 0.51083 0.03868  0.09095  -0.09437 115 ASP A CB  
885  C CG  . ASP A 115 ? 0.79246 0.77760 0.62266 0.04717  0.13904  -0.06645 115 ASP A CG  
886  O OD1 . ASP A 115 ? 0.75815 0.73107 0.59106 0.03801  0.15319  -0.03718 115 ASP A OD1 
887  O OD2 . ASP A 115 ? 0.71407 0.70568 0.51376 0.06645  0.16715  -0.07125 115 ASP A OD2 
888  N N   . THR A 116 ? 0.49867 0.46873 0.41939 0.03205  0.00337  -0.12035 116 THR A N   
889  C CA  . THR A 116 ? 0.47321 0.44753 0.44728 0.03460  -0.01428 -0.12746 116 THR A CA  
890  C C   . THR A 116 ? 0.41311 0.37115 0.40142 0.02567  -0.03589 -0.10868 116 THR A C   
891  O O   . THR A 116 ? 0.45291 0.42262 0.48385 0.03025  -0.04185 -0.10443 116 THR A O   
892  C CB  . THR A 116 ? 0.53306 0.49523 0.51087 0.05070  -0.02551 -0.15138 116 THR A CB  
893  O OG1 . THR A 116 ? 0.49215 0.43551 0.50691 0.05460  -0.04510 -0.14620 116 THR A OG1 
894  C CG2 . THR A 116 ? 0.54220 0.48892 0.46724 0.05714  -0.03304 -0.16798 116 THR A CG2 
895  N N   . ARG A 117 ? 0.47726 0.41118 0.42673 0.01777  -0.04714 -0.09677 117 ARG A N   
896  C CA  . ARG A 117 ? 0.45981 0.37897 0.42277 0.00734  -0.06434 -0.07644 117 ARG A CA  
897  C C   . ARG A 117 ? 0.45885 0.39911 0.44748 -0.00626 -0.04836 -0.06122 117 ARG A C   
898  O O   . ARG A 117 ? 0.41952 0.36386 0.44223 -0.00867 -0.06078 -0.05366 117 ARG A O   
899  C CB  . ARG A 117 ? 0.45095 0.34163 0.36701 0.00487  -0.08134 -0.06982 117 ARG A CB  
900  C CG  . ARG A 117 ? 0.56951 0.44287 0.48504 0.01793  -0.10446 -0.09503 117 ARG A CG  
901  C CD  . ARG A 117 ? 0.61238 0.46024 0.51279 0.01499  -0.13180 -0.08975 117 ARG A CD  
902  N NE  . ARG A 117 ? 0.56211 0.41112 0.39155 0.02121  -0.13053 -0.08640 117 ARG A NE  
903  C CZ  . ARG A 117 ? 0.64528 0.49845 0.43179 0.04233  -0.14091 -0.11524 117 ARG A CZ  
904  N NH1 . ARG A 117 ? 0.70877 0.56393 0.52813 0.05271  -0.15556 -0.15425 117 ARG A NH1 
905  N NH2 . ARG A 117 ? 0.73331 0.58953 0.44359 0.05812  -0.13479 -0.10537 117 ARG A NH2 
906  N N   . ASN A 118 ? 0.40741 0.36192 0.38748 -0.01247 -0.01852 -0.05836 118 ASN A N   
907  C CA  . ASN A 118 ? 0.43703 0.41491 0.46866 -0.02657 0.00067  -0.05192 118 ASN A CA  
908  C C   . ASN A 118 ? 0.40006 0.41603 0.49487 -0.01873 -0.00619 -0.07514 118 ASN A C   
909  O O   . ASN A 118 ? 0.42004 0.45572 0.56372 -0.02253 -0.01551 -0.07911 118 ASN A O   
910  C CB  . ASN A 118 ? 0.46005 0.44324 0.48480 -0.03129 0.04424  -0.04261 118 ASN A CB  
911  C CG  . ASN A 118 ? 0.51890 0.46875 0.47781 -0.02994 0.05540  -0.01359 118 ASN A CG  
912  O OD1 . ASN A 118 ? 0.44758 0.37513 0.38389 -0.03380 0.03017  -0.00104 118 ASN A OD1 
913  N ND2 . ASN A 118 ? 0.50282 0.45001 0.42866 -0.01938 0.09566  -0.00089 118 ASN A ND2 
914  N N   . LYS A 119 ? 0.38877 0.41851 0.48218 -0.00305 -0.00295 -0.09327 119 LYS A N   
915  C CA  . LYS A 119 ? 0.35382 0.42259 0.49834 0.01381  -0.00992 -0.11488 119 LYS A CA  
916  C C   . LYS A 119 ? 0.30051 0.36470 0.45174 0.03071  -0.03983 -0.10972 119 LYS A C   
917  O O   . LYS A 119 ? 0.29624 0.39313 0.48916 0.04085  -0.05079 -0.12026 119 LYS A O   
918  C CB  . LYS A 119 ? 0.27405 0.34942 0.40640 0.03018  -0.00026 -0.12956 119 LYS A CB  
919  C CG  . LYS A 119 ? 0.30824 0.41314 0.46498 0.02535  0.03052  -0.14413 119 LYS A CG  
920  C CD  . LYS A 119 ? 0.31671 0.41513 0.44357 0.04038  0.03813  -0.15431 119 LYS A CD  
921  C CE  . LYS A 119 ? 0.46225 0.56727 0.57909 0.03353  0.07348  -0.15744 119 LYS A CE  
922  N NZ  . LYS A 119 ? 0.57123 0.66609 0.65117 0.04916  0.07742  -0.16946 119 LYS A NZ  
923  N N   . VAL A 120 ? 0.37931 0.40478 0.49478 0.03808  -0.05212 -0.09603 120 VAL A N   
924  C CA  . VAL A 120 ? 0.28741 0.30127 0.41049 0.05843  -0.07136 -0.08402 120 VAL A CA  
925  C C   . VAL A 120 ? 0.38535 0.39416 0.51277 0.04488  -0.08515 -0.07051 120 VAL A C   
926  O O   . VAL A 120 ? 0.33733 0.35739 0.48129 0.06632  -0.09914 -0.06657 120 VAL A O   
927  C CB  . VAL A 120 ? 0.29598 0.26611 0.39984 0.06501  -0.07469 -0.07467 120 VAL A CB  
928  C CG1 . VAL A 120 ? 0.32808 0.28020 0.43858 0.07972  -0.08222 -0.05203 120 VAL A CG1 
929  C CG2 . VAL A 120 ? 0.28388 0.26174 0.39611 0.08218  -0.05970 -0.09103 120 VAL A CG2 
930  N N   . ASN A 121 ? 0.30139 0.29492 0.41243 0.01442  -0.07912 -0.06232 121 ASN A N   
931  C CA  . ASN A 121 ? 0.34204 0.32967 0.46276 0.00054  -0.08902 -0.04905 121 ASN A CA  
932  C C   . ASN A 121 ? 0.43850 0.47360 0.61618 0.00518  -0.09026 -0.06930 121 ASN A C   
933  O O   . ASN A 121 ? 0.45369 0.48732 0.64196 0.00498  -0.10168 -0.06311 121 ASN A O   
934  C CB  . ASN A 121 ? 0.37176 0.33429 0.46427 -0.02742 -0.07577 -0.03268 121 ASN A CB  
935  C CG  . ASN A 121 ? 0.38375 0.30267 0.42486 -0.02819 -0.08923 -0.01650 121 ASN A CG  
936  O OD1 . ASN A 121 ? 0.45197 0.35440 0.49402 -0.01412 -0.10776 -0.01480 121 ASN A OD1 
937  N ND2 . ASN A 121 ? 0.45216 0.35352 0.45235 -0.03971 -0.07791 -0.00561 121 ASN A ND2 
938  N N   . THR A 122 ? 0.32927 0.40591 0.54331 0.01136  -0.07692 -0.09598 122 THR A N   
939  C CA  . THR A 122 ? 0.25254 0.37710 0.52934 0.01745  -0.07973 -0.12461 122 THR A CA  
940  C C   . THR A 122 ? 0.34727 0.46056 0.58302 0.04896  -0.09374 -0.12258 122 THR A C   
941  O O   . THR A 122 ? 0.34801 0.46506 0.59215 0.05063  -0.09644 -0.13285 122 THR A O   
942  C CB  . THR A 122 ? 0.24216 0.41041 0.56515 0.02044  -0.06235 -0.15545 122 THR A CB  
943  O OG1 . THR A 122 ? 0.18859 0.36260 0.47907 0.05214  -0.06914 -0.15955 122 THR A OG1 
944  C CG2 . THR A 122 ? 0.28303 0.43180 0.60408 -0.01114 -0.02559 -0.14254 122 THR A CG2 
945  N N   . VAL A 123 ? 0.27032 0.36830 0.46116 0.07041  -0.09661 -0.10903 123 VAL A N   
946  C CA  . VAL A 123 ? 0.33602 0.42807 0.48514 0.09125  -0.09708 -0.09960 123 VAL A CA  
947  C C   . VAL A 123 ? 0.43268 0.48674 0.54308 0.08818  -0.09111 -0.06277 123 VAL A C   
948  O O   . VAL A 123 ? 0.34923 0.40103 0.43626 0.10586  -0.09258 -0.06067 123 VAL A O   
949  C CB  . VAL A 123 ? 0.37500 0.48566 0.51183 0.11368  -0.09104 -0.10416 123 VAL A CB  
950  C CG1 . VAL A 123 ? 0.34028 0.49381 0.51427 0.11640  -0.09641 -0.14436 123 VAL A CG1 
951  C CG2 . VAL A 123 ? 0.28867 0.38289 0.42194 0.11365  -0.08095 -0.08973 123 VAL A CG2 
952  N N   . MET A 124 ? 0.30912 0.51550 0.46737 0.09059  -0.00412 -0.14389 124 MET A N   
953  C CA  . MET A 124 ? 0.31479 0.54282 0.48418 0.09607  -0.00927 -0.15435 124 MET A CA  
954  C C   . MET A 124 ? 0.25913 0.52894 0.42565 0.08009  0.00001  -0.15288 124 MET A C   
955  O O   . MET A 124 ? 0.22357 0.52024 0.39610 0.07754  0.00278  -0.16918 124 MET A O   
956  C CB  . MET A 124 ? 0.37861 0.60163 0.56071 0.10871  -0.01577 -0.17676 124 MET A CB  
957  C CG  . MET A 124 ? 0.36658 0.54806 0.55275 0.12909  -0.03087 -0.17945 124 MET A CG  
958  S SD  . MET A 124 ? 0.38118 0.53932 0.56381 0.14114  -0.04493 -0.16529 124 MET A SD  
959  C CE  . MET A 124 ? 0.41828 0.62830 0.60954 0.12975  -0.03891 -0.16281 124 MET A CE  
960  N N   . PRO A 125 ? 0.25681 0.53052 0.41269 0.06896  0.00486  -0.13384 125 PRO A N   
961  C CA  . PRO A 125 ? 0.26023 0.56643 0.40935 0.05317  0.01295  -0.13026 125 PRO A CA  
962  C C   . PRO A 125 ? 0.32717 0.66014 0.48927 0.05459  0.01185  -0.14293 125 PRO A C   
963  O O   . PRO A 125 ? 0.26688 0.59347 0.43966 0.06345  0.00491  -0.14311 125 PRO A O   
964  C CB  . PRO A 125 ? 0.27621 0.57151 0.41381 0.04458  0.01561  -0.10688 125 PRO A CB  
965  C CG  . PRO A 125 ? 0.24255 0.50363 0.38013 0.05484  0.01081  -0.09990 125 PRO A CG  
966  C CD  . PRO A 125 ? 0.20687 0.45461 0.35634 0.07095  0.00252  -0.11587 125 PRO A CD  
967  N N   . ARG A 126 ? 0.32002 0.68592 0.48140 0.04536  0.01845  -0.15440 126 ARG A N   
968  C CA  . ARG A 126 ? 0.31768 0.71568 0.49441 0.04624  0.01925  -0.17137 126 ARG A CA  
969  C C   . ARG A 126 ? 0.30498 0.73102 0.47298 0.02685  0.02835  -0.16233 126 ARG A C   
970  O O   . ARG A 126 ? 0.28086 0.70494 0.42909 0.01274  0.03387  -0.14605 126 ARG A O   
971  C CB  . ARG A 126 ? 0.33545 0.75398 0.52081 0.05059  0.02047  -0.19619 126 ARG A CB  
972  C CG  . ARG A 126 ? 0.40488 0.80974 0.61167 0.07256  0.00973  -0.21450 126 ARG A CG  
973  C CD  . ARG A 126 ? 0.49206 0.93112 0.71692 0.07760  0.01115  -0.24399 126 ARG A CD  
974  N NE  . ARG A 126 ? 0.37702 0.85734 0.61346 0.07141  0.01642  -0.25335 126 ARG A NE  
975  C CZ  . ARG A 126 ? 0.47970 0.99554 0.70577 0.05129  0.02885  -0.25316 126 ARG A CZ  
976  N NH1 . ARG A 126 ? 0.46715 0.98373 0.67026 0.03638  0.03585  -0.24418 126 ARG A NH1 
977  N NH2 . ARG A 126 ? 0.32729 0.88027 0.56648 0.04556  0.03383  -0.26259 126 ARG A NH2 
978  N N   . GLU A 127 ? 0.29100 0.74435 0.47496 0.02617  0.02926  -0.17363 127 GLU A N   
979  C CA  . GLU A 127 ? 0.23051 0.71687 0.40864 0.00565  0.03927  -0.17016 127 GLU A CA  
980  C C   . GLU A 127 ? 0.21663 0.72453 0.37771 -0.00853 0.04815  -0.17382 127 GLU A C   
981  O O   . GLU A 127 ? 0.22685 0.74494 0.39314 -0.00134 0.04782  -0.19247 127 GLU A O   
982  C CB  . GLU A 127 ? 0.28923 0.80860 0.49256 0.00880  0.03922  -0.18904 127 GLU A CB  
983  C CG  . GLU A 127 ? 0.23702 0.80074 0.43829 -0.01263 0.05164  -0.19507 127 GLU A CG  
984  C CD  . GLU A 127 ? 0.33286 0.93410 0.56392 -0.00786 0.05183  -0.21774 127 GLU A CD  
985  O OE1 . GLU A 127 ? 0.25277 0.84573 0.50659 0.01460  0.04056  -0.23012 127 GLU A OE1 
986  O OE2 . GLU A 127 ? 0.27119 0.91165 0.50299 -0.02700 0.06297  -0.22364 127 GLU A OE2 
987  N N   . GLY A 128 ? 0.21871 0.73324 0.35896 -0.02922 0.05505  -0.15576 128 GLY A N   
988  C CA  . GLY A 128 ? 0.23356 0.76789 0.35330 -0.04483 0.06182  -0.15491 128 GLY A CA  
989  C C   . GLY A 128 ? 0.28013 0.78918 0.38138 -0.04283 0.05772  -0.14089 128 GLY A C   
990  O O   . GLY A 128 ? 0.33092 0.85728 0.41445 -0.05522 0.06130  -0.13942 128 GLY A O   
991  N N   . GLU A 129 ? 0.30040 0.77206 0.40576 -0.02836 0.05026  -0.13123 129 GLU A N   
992  C CA  . GLU A 129 ? 0.26140 0.71128 0.35355 -0.02529 0.04650  -0.12015 129 GLU A CA  
993  C C   . GLU A 129 ? 0.17982 0.60891 0.25960 -0.03162 0.04547  -0.09283 129 GLU A C   
994  O O   . GLU A 129 ? 0.23779 0.65909 0.32310 -0.03372 0.04579  -0.08403 129 GLU A O   
995  C CB  . GLU A 129 ? 0.23838 0.66203 0.34495 -0.00545 0.03977  -0.13098 129 GLU A CB  
996  C CG  . GLU A 129 ? 0.22592 0.66771 0.34135 0.00001  0.03973  -0.15710 129 GLU A CG  
997  C CD  . GLU A 129 ? 0.21760 0.63162 0.34908 0.01882  0.03257  -0.16805 129 GLU A CD  
998  O OE1 . GLU A 129 ? 0.30418 0.68804 0.44009 0.02744  0.02797  -0.15605 129 GLU A OE1 
999  O OE2 . GLU A 129 ? 0.23354 0.65612 0.37318 0.02427  0.03140  -0.18892 129 GLU A OE2 
1000 N N   . THR A 130 ? 0.23289 0.65539 0.29792 -0.03429 0.04357  -0.08069 130 THR A N   
1001 C CA  . THR A 130 ? 0.20124 0.60595 0.25615 -0.03835 0.04177  -0.05544 130 THR A CA  
1002 C C   . THR A 130 ? 0.27334 0.65029 0.33499 -0.02326 0.03649  -0.05294 130 THR A C   
1003 O O   . THR A 130 ? 0.25171 0.63315 0.31248 -0.01911 0.03460  -0.06251 130 THR A O   
1004 C CB  . THR A 130 ? 0.27414 0.69973 0.30554 -0.05576 0.04328  -0.04030 130 THR A CB  
1005 O OG1 . THR A 130 ? 0.31307 0.76626 0.33699 -0.07197 0.04941  -0.04663 130 THR A OG1 
1006 C CG2 . THR A 130 ? 0.20880 0.61653 0.23028 -0.06127 0.04151  -0.01236 130 THR A CG2 
1007 N N   . VAL A 131 ? 0.18464 0.53491 0.25346 -0.01663 0.03457  -0.04148 131 VAL A N   
1008 C CA  . VAL A 131 ? 0.22084 0.54405 0.29728 -0.00364 0.03091  -0.04029 131 VAL A CA  
1009 C C   . VAL A 131 ? 0.17756 0.49214 0.24864 -0.00522 0.02990  -0.01882 131 VAL A C   
1010 O O   . VAL A 131 ? 0.21692 0.53502 0.28251 -0.01323 0.03144  -0.00375 131 VAL A O   
1011 C CB  . VAL A 131 ? 0.29619 0.59586 0.38727 0.00829  0.02887  -0.04849 131 VAL A CB  
1012 C CG1 . VAL A 131 ? 0.22177 0.53483 0.31930 0.00588  0.02957  -0.05641 131 VAL A CG1 
1013 C CG2 . VAL A 131 ? 0.17988 0.45350 0.27326 0.01395  0.02758  -0.03479 131 VAL A CG2 
1014 N N   . LEU A 132 ? 0.16625 0.47167 0.24047 0.00168  0.02740  -0.01766 132 LEU A N   
1015 C CA  . LEU A 132 ? 0.22254 0.52082 0.29817 0.00485  0.02556  0.00013  132 LEU A CA  
1016 C C   . LEU A 132 ? 0.20589 0.47231 0.29249 0.01579  0.02637  -0.00303 132 LEU A C   
1017 O O   . LEU A 132 ? 0.18814 0.44435 0.28060 0.01982  0.02661  -0.01576 132 LEU A O   
1018 C CB  . LEU A 132 ? 0.11418 0.43365 0.18790 0.00391  0.02130  0.00370  132 LEU A CB  
1019 C CG  . LEU A 132 ? 0.14278 0.44382 0.21989 0.01153  0.01601  0.02019  132 LEU A CG  
1020 C CD1 . LEU A 132 ? 0.14624 0.42651 0.20812 0.00835  0.01311  0.04006  132 LEU A CD1 
1021 C CD2 . LEU A 132 ? 0.14270 0.46461 0.22064 0.01251  0.00787  0.02243  132 LEU A CD2 
1022 N N   . ASP A 133 ? 0.15248 0.40102 0.23875 0.01875  0.02719  0.00885  133 ASP A N   
1023 C CA  . ASP A 133 ? 0.14357 0.36066 0.23385 0.02756  0.02901  0.00794  133 ASP A CA  
1024 C C   . ASP A 133 ? 0.15296 0.35722 0.24252 0.03171  0.02776  0.02053  133 ASP A C   
1025 O O   . ASP A 133 ? 0.17320 0.36331 0.25372 0.03092  0.02500  0.03335  133 ASP A O   
1026 C CB  . ASP A 133 ? 0.21606 0.41412 0.30111 0.02769  0.02886  0.00744  133 ASP A CB  
1027 C CG  . ASP A 133 ? 0.27328 0.43597 0.35383 0.03452  0.03059  0.00912  133 ASP A CG  
1028 O OD1 . ASP A 133 ? 0.33645 0.49057 0.42021 0.03889  0.03307  0.00129  133 ASP A OD1 
1029 O OD2 . ASP A 133 ? 0.29760 0.43918 0.36876 0.03393  0.02981  0.01734  133 ASP A OD2 
1030 N N   . THR A 134 ? 0.14723 0.35735 0.24839 0.03608  0.02940  0.01552  134 THR A N   
1031 C CA  . THR A 134 ? 0.12993 0.34193 0.23834 0.04189  0.02661  0.02387  134 THR A CA  
1032 C C   . THR A 134 ? 0.19044 0.37231 0.29844 0.04969  0.03044  0.02931  134 THR A C   
1033 O O   . THR A 134 ? 0.22905 0.40878 0.34152 0.05695  0.02593  0.03791  134 THR A O   
1034 C CB  . THR A 134 ? 0.09719 0.32977 0.22286 0.04237  0.02803  0.01359  134 THR A CB  
1035 O OG1 . THR A 134 ? 0.17237 0.38444 0.30004 0.04051  0.03690  0.00301  134 THR A OG1 
1036 C CG2 . THR A 134 ? 0.13071 0.38591 0.25226 0.03416  0.02264  0.00620  134 THR A CG2 
1037 N N   A CYS A 135 ? 0.21575 0.37384 0.31769 0.04950  0.03780  0.02359  135 CYS A N   
1038 N N   B CYS A 135 ? 0.22720 0.38503 0.32858 0.04934  0.03760  0.02380  135 CYS A N   
1039 C CA  A CYS A 135 ? 0.28370 0.41340 0.38125 0.05571  0.04297  0.02603  135 CYS A CA  
1040 C CA  B CYS A 135 ? 0.27900 0.40865 0.37645 0.05547  0.04325  0.02556  135 CYS A CA  
1041 C C   A CYS A 135 ? 0.25253 0.35582 0.33099 0.05200  0.04311  0.02634  135 CYS A C   
1042 C C   B CYS A 135 ? 0.29127 0.39452 0.36955 0.05188  0.04308  0.02626  135 CYS A C   
1043 O O   A CYS A 135 ? 0.28722 0.38139 0.35908 0.04943  0.04646  0.01918  135 CYS A O   
1044 O O   B CYS A 135 ? 0.29209 0.38606 0.36349 0.04925  0.04621  0.01920  135 CYS A O   
1045 C CB  A CYS A 135 ? 0.28123 0.41074 0.38949 0.05809  0.05359  0.01708  135 CYS A CB  
1046 C CB  B CYS A 135 ? 0.28146 0.41115 0.38867 0.05671  0.05390  0.01602  135 CYS A CB  
1047 S SG  A CYS A 135 ? 0.30471 0.47425 0.43961 0.05705  0.05340  0.01063  135 CYS A SG  
1048 S SG  B CYS A 135 ? 0.39226 0.49549 0.49568 0.06374  0.06489  0.01407  135 CYS A SG  
1049 N N   . MET A 136 ? 0.25738 0.34720 0.32638 0.05118  0.03782  0.03497  136 MET A N   
1050 C CA  . MET A 136 ? 0.35775 0.42604 0.41080 0.04604  0.03614  0.03450  136 MET A CA  
1051 C C   . MET A 136 ? 0.35963 0.40266 0.40171 0.04896  0.04223  0.02715  136 MET A C   
1052 O O   . MET A 136 ? 0.31211 0.35039 0.34544 0.04569  0.03999  0.02217  136 MET A O   
1053 C CB  . MET A 136 ? 0.36528 0.41337 0.40882 0.04380  0.03140  0.04396  136 MET A CB  
1054 C CG  . MET A 136 ? 0.30713 0.35673 0.34164 0.03106  0.02595  0.04580  136 MET A CG  
1055 S SD  . MET A 136 ? 0.25615 0.28365 0.27863 0.02210  0.02007  0.05940  136 MET A SD  
1056 C CE  . MET A 136 ? 0.40072 0.38326 0.41261 0.03077  0.02272  0.05422  136 MET A CE  
1057 N N   . GLY A 137 ? 0.28282 0.30773 0.32283 0.05539  0.04869  0.02649  137 GLY A N   
1058 C CA  . GLY A 137 ? 0.33367 0.32907 0.35448 0.05571  0.05416  0.02076  137 GLY A CA  
1059 C C   . GLY A 137 ? 0.37496 0.35237 0.38027 0.04992  0.04541  0.02300  137 GLY A C   
1060 O O   . GLY A 137 ? 0.37066 0.34462 0.37856 0.04803  0.03995  0.02935  137 GLY A O   
1061 N N   . LEU A 138 ? 0.40197 0.36841 0.39085 0.04568  0.04222  0.01846  138 LEU A N   
1062 C CA  . LEU A 138 ? 0.37641 0.33254 0.35425 0.03862  0.03236  0.01837  138 LEU A CA  
1063 C C   . LEU A 138 ? 0.31491 0.30052 0.30710 0.03226  0.02341  0.02037  138 LEU A C   
1064 O O   . LEU A 138 ? 0.35199 0.33811 0.34083 0.02424  0.01531  0.01905  138 LEU A O   
1065 C CB  . LEU A 138 ? 0.36986 0.30256 0.32256 0.03794  0.03025  0.01179  138 LEU A CB  
1066 C CG  . LEU A 138 ? 0.41735 0.32003 0.35145 0.04086  0.04000  0.00743  138 LEU A CG  
1067 C CD1 . LEU A 138 ? 0.41117 0.28933 0.31271 0.03849  0.03849  0.00145  138 LEU A CD1 
1068 C CD2 . LEU A 138 ? 0.46987 0.35888 0.40613 0.03895  0.03788  0.00830  138 LEU A CD2 
1069 N N   . GLY A 139 ? 0.35838 0.37121 0.36728 0.03462  0.02531  0.02133  139 GLY A N   
1070 C CA  . GLY A 139 ? 0.29526 0.34022 0.31843 0.02864  0.01968  0.02078  139 GLY A CA  
1071 C C   . GLY A 139 ? 0.23045 0.28846 0.25822 0.03162  0.01364  0.01146  139 GLY A C   
1072 O O   . GLY A 139 ? 0.30390 0.39254 0.34625 0.02748  0.00941  0.00711  139 GLY A O   
1073 N N   . TYR A 140 ? 0.27623 0.31155 0.29125 0.03881  0.01298  0.00796  140 TYR A N   
1074 C CA  . TYR A 140 ? 0.25524 0.29376 0.27077 0.04393  0.00269  0.00042  140 TYR A CA  
1075 C C   . TYR A 140 ? 0.32930 0.39543 0.36524 0.04829  0.00257  -0.00586 140 TYR A C   
1076 O O   . TYR A 140 ? 0.25154 0.33699 0.30035 0.05233  -0.00665 -0.01462 140 TYR A O   
1077 C CB  . TYR A 140 ? 0.39123 0.39230 0.38113 0.04930  0.00138  0.00114  140 TYR A CB  
1078 C CG  . TYR A 140 ? 0.37768 0.35160 0.34329 0.04553  -0.00032 0.00340  140 TYR A CG  
1079 C CD1 . TYR A 140 ? 0.36591 0.34829 0.33565 0.03856  -0.00563 0.00248  140 TYR A CD1 
1080 C CD2 . TYR A 140 ? 0.44759 0.38663 0.38367 0.04682  0.00378  0.00537  140 TYR A CD2 
1081 C CE1 . TYR A 140 ? 0.43616 0.39128 0.38218 0.03442  -0.00784 0.00202  140 TYR A CE1 
1082 C CE2 . TYR A 140 ? 0.51224 0.42661 0.42275 0.04305  0.00284  0.00493  140 TYR A CE2 
1083 C CZ  . TYR A 140 ? 0.42165 0.34344 0.33766 0.03770  -0.00376 0.00247  140 TYR A CZ  
1084 O OH  . TYR A 140 ? 0.43523 0.33042 0.32452 0.03343  -0.00510 -0.00028 140 TYR A OH  
1085 N N   . THR A 141 ? 0.25264 0.32211 0.29319 0.04837  0.01212  -0.00376 141 THR A N   
1086 C CA  . THR A 141 ? 0.31877 0.41416 0.37716 0.05111  0.01223  -0.01192 141 THR A CA  
1087 C C   . THR A 141 ? 0.26167 0.39749 0.33684 0.04470  0.01254  -0.01440 141 THR A C   
1088 O O   . THR A 141 ? 0.29784 0.46093 0.38846 0.04735  0.00939  -0.02601 141 THR A O   
1089 C CB  . THR A 141 ? 0.26217 0.35233 0.32093 0.05050  0.02139  -0.01025 141 THR A CB  
1090 O OG1 . THR A 141 ? 0.36373 0.41740 0.40498 0.05281  0.02338  -0.00831 141 THR A OG1 
1091 C CG2 . THR A 141 ? 0.17251 0.28616 0.24695 0.05226  0.02072  -0.02074 141 THR A CG2 
1092 N N   . ALA A 142 ? 0.22742 0.36610 0.29833 0.03596  0.01658  -0.00401 142 ALA A N   
1093 C CA  . ALA A 142 ? 0.27295 0.44507 0.35253 0.02566  0.01761  -0.00310 142 ALA A CA  
1094 C C   . ALA A 142 ? 0.20479 0.39511 0.29341 0.02225  0.01180  -0.01163 142 ALA A C   
1095 O O   . ALA A 142 ? 0.24967 0.47888 0.35389 0.01848  0.01306  -0.02140 142 ALA A O   
1096 C CB  . ALA A 142 ? 0.20103 0.36055 0.26919 0.01722  0.02048  0.01234  142 ALA A CB  
1097 N N   . ILE A 143 ? 0.25984 0.42589 0.33996 0.02356  0.00538  -0.01023 143 ILE A N   
1098 C CA  . ILE A 143 ? 0.23461 0.42103 0.32638 0.02021  -0.00256 -0.01934 143 ILE A CA  
1099 C C   . ILE A 143 ? 0.21306 0.42113 0.32376 0.03399  -0.00930 -0.03569 143 ILE A C   
1100 O O   . ILE A 143 ? 0.26583 0.51659 0.39946 0.03139  -0.01051 -0.04800 143 ILE A O   
1101 C CB  . ILE A 143 ? 0.25358 0.40644 0.32866 0.01881  -0.00996 -0.01490 143 ILE A CB  
1102 C CG1 . ILE A 143 ? 0.27380 0.40919 0.33505 0.00447  -0.00390 -0.00219 143 ILE A CG1 
1103 C CG2 . ILE A 143 ? 0.29661 0.47023 0.38527 0.01859  -0.02209 -0.02638 143 ILE A CG2 
1104 C CD1 . ILE A 143 ? 0.26967 0.36498 0.31007 0.00397  -0.00869 0.00092  143 ILE A CD1 
1105 N N   . GLU A 144 ? 0.25462 0.43291 0.35622 0.04853  -0.01353 -0.03679 144 GLU A N   
1106 C CA  . GLU A 144 ? 0.21218 0.40076 0.32931 0.06397  -0.02210 -0.05159 144 GLU A CA  
1107 C C   . GLU A 144 ? 0.26270 0.49317 0.40224 0.06343  -0.01428 -0.06387 144 GLU A C   
1108 O O   . GLU A 144 ? 0.23775 0.48604 0.39160 0.06811  -0.01889 -0.07762 144 GLU A O   
1109 C CB  . GLU A 144 ? 0.31117 0.45235 0.40811 0.07530  -0.02579 -0.04717 144 GLU A CB  
1110 C CG  . GLU A 144 ? 0.29431 0.43305 0.40287 0.09257  -0.03629 -0.06073 144 GLU A CG  
1111 C CD  . GLU A 144 ? 0.35072 0.49286 0.46730 0.10457  -0.05499 -0.06809 144 GLU A CD  
1112 O OE1 . GLU A 144 ? 0.43783 0.56224 0.53701 0.10023  -0.06152 -0.05894 144 GLU A OE1 
1113 O OE2 . GLU A 144 ? 0.33908 0.50130 0.47896 0.11830  -0.06366 -0.08402 144 GLU A OE2 
1114 N N   . ALA A 145 ? 0.26138 0.49472 0.39371 0.05421  -0.00208 -0.05672 145 ALA A N   
1115 C CA  . ALA A 145 ? 0.25643 0.50913 0.39150 0.04751  0.00485  -0.06403 145 ALA A CA  
1116 C C   . ALA A 145 ? 0.27446 0.55948 0.41480 0.03405  0.00857  -0.06708 145 ALA A C   
1117 O O   . ALA A 145 ? 0.29619 0.59995 0.44045 0.03214  0.01146  -0.07887 145 ALA A O   
1118 C CB  . ALA A 145 ? 0.28199 0.52770 0.40490 0.04075  0.01327  -0.05435 145 ALA A CB  
1119 N N   . SER A 146 ? 0.20960 0.50296 0.34971 0.02339  0.00929  -0.05756 146 SER A N   
1120 C CA  . SER A 146 ? 0.18098 0.50416 0.32544 0.00734  0.01382  -0.05979 146 SER A CA  
1121 C C   . SER A 146 ? 0.30528 0.64479 0.46852 0.01335  0.00629  -0.07502 146 SER A C   
1122 O O   . SER A 146 ? 0.24466 0.61292 0.41543 0.00485  0.01100  -0.08448 146 SER A O   
1123 C CB  . SER A 146 ? 0.24829 0.57241 0.38550 -0.00966 0.01711  -0.04318 146 SER A CB  
1124 O OG  . SER A 146 ? 0.23301 0.54594 0.37637 -0.00591 0.00751  -0.04286 146 SER A OG  
1125 N N   . LYS A 147 ? 0.35194 0.67490 0.52218 0.02829  -0.00625 -0.07780 147 LYS A N   
1126 C CA  . LYS A 147 ? 0.32690 0.66401 0.51517 0.03712  -0.01667 -0.09218 147 LYS A CA  
1127 C C   . LYS A 147 ? 0.23993 0.58636 0.43733 0.04876  -0.01620 -0.10867 147 LYS A C   
1128 O O   . LYS A 147 ? 0.47288 0.83964 0.68837 0.05515  -0.02247 -0.12294 147 LYS A O   
1129 C CB  . LYS A 147 ? 0.35318 0.66447 0.54040 0.05242  -0.03388 -0.08999 147 LYS A CB  
1130 C CG  . LYS A 147 ? 0.28162 0.59588 0.46654 0.03997  -0.03921 -0.08153 147 LYS A CG  
1131 C CD  . LYS A 147 ? 0.43154 0.72587 0.61417 0.05505  -0.06096 -0.08429 147 LYS A CD  
1132 C CE  . LYS A 147 ? 0.46976 0.72352 0.62051 0.04143  -0.06197 -0.06836 147 LYS A CE  
1133 N NZ  . LYS A 147 ? 0.46010 0.65432 0.57605 0.05411  -0.06803 -0.05762 147 LYS A NZ  
1134 N N   . ARG A 148 ? 0.32735 0.66193 0.51435 0.05133  -0.00967 -0.10861 148 ARG A N   
1135 C CA  . ARG A 148 ? 0.36865 0.71517 0.56439 0.05987  -0.00894 -0.12650 148 ARG A CA  
1136 C C   . ARG A 148 ? 0.37243 0.75723 0.57031 0.04438  0.00341  -0.13446 148 ARG A C   
1137 O O   . ARG A 148 ? 0.40650 0.81016 0.61519 0.05060  0.00409  -0.15319 148 ARG A O   
1138 C CB  . ARG A 148 ? 0.41591 0.73506 0.60037 0.06763  -0.00834 -0.12541 148 ARG A CB  
1139 C CG  . ARG A 148 ? 0.43185 0.71699 0.61861 0.08785  -0.02222 -0.12771 148 ARG A CG  
1140 C CD  . ARG A 148 ? 0.38581 0.63906 0.55608 0.08688  -0.02233 -0.10970 148 ARG A CD  
1141 N NE  . ARG A 148 ? 0.37458 0.59313 0.54128 0.10383  -0.03738 -0.10722 148 ARG A NE  
1142 C CZ  . ARG A 148 ? 0.37367 0.55899 0.53483 0.11726  -0.04401 -0.11059 148 ARG A CZ  
1143 N NH1 . ARG A 148 ? 0.40614 0.59385 0.57088 0.11696  -0.03777 -0.12051 148 ARG A NH1 
1144 N NH2 . ARG A 148 ? 0.39449 0.53946 0.54278 0.13033  -0.05808 -0.10339 148 ARG A NH2 
1145 N N   . GLY A 149 ? 0.22176 0.61792 0.40872 0.02435  0.01258  -0.12134 149 GLY A N   
1146 C CA  . GLY A 149 ? 0.27762 0.70806 0.46129 0.00714  0.02414  -0.12644 149 GLY A CA  
1147 C C   . GLY A 149 ? 0.22458 0.64948 0.38406 -0.00643 0.03265  -0.11308 149 GLY A C   
1148 O O   . GLY A 149 ? 0.29440 0.74573 0.44544 -0.02383 0.04168  -0.11334 149 GLY A O   
1149 N N   . ALA A 150 ? 0.34627 0.73957 0.49393 0.00024  0.02964  -0.10142 150 ALA A N   
1150 C CA  . ALA A 150 ? 0.25601 0.64631 0.38285 -0.01006 0.03533  -0.08998 150 ALA A CA  
1151 C C   . ALA A 150 ? 0.23816 0.62272 0.35196 -0.02558 0.03830  -0.06784 150 ALA A C   
1152 O O   . ALA A 150 ? 0.17940 0.55203 0.29972 -0.02526 0.03490  -0.06016 150 ALA A O   
1153 C CB  . ALA A 150 ? 0.20644 0.56924 0.32956 0.00346  0.03092  -0.08919 150 ALA A CB  
1154 N N   . TYR A 151 ? 0.22036 0.61476 0.31508 -0.03998 0.04367  -0.05780 151 TYR A N   
1155 C CA  . TYR A 151 ? 0.27871 0.66304 0.35782 -0.05425 0.04527  -0.03410 151 TYR A CA  
1156 C C   . TYR A 151 ? 0.19486 0.55318 0.26836 -0.04325 0.04104  -0.02197 151 TYR A C   
1157 O O   . TYR A 151 ? 0.23275 0.59274 0.30112 -0.03698 0.03999  -0.02633 151 TYR A O   
1158 C CB  . TYR A 151 ? 0.18966 0.59556 0.24809 -0.07573 0.05139  -0.02639 151 TYR A CB  
1159 C CG  . TYR A 151 ? 0.32251 0.71258 0.36127 -0.09307 0.05207  0.00091  151 TYR A CG  
1160 C CD1 . TYR A 151 ? 0.26109 0.64589 0.30070 -0.10819 0.05423  0.00840  151 TYR A CD1 
1161 C CD2 . TYR A 151 ? 0.25724 0.63488 0.27596 -0.09436 0.04931  0.01975  151 TYR A CD2 
1162 C CE1 . TYR A 151 ? 0.30598 0.66587 0.32360 -0.12531 0.05385  0.03448  151 TYR A CE1 
1163 C CE2 . TYR A 151 ? 0.24138 0.59556 0.23830 -0.10863 0.04799  0.04709  151 TYR A CE2 
1164 C CZ  . TYR A 151 ? 0.35833 0.69906 0.35324 -0.12428 0.05020  0.05467  151 TYR A CZ  
1165 O OH  . TYR A 151 ? 0.32847 0.63255 0.29730 -0.13825 0.04685  0.08230  151 TYR A OH  
1166 N N   . VAL A 152 ? 0.26191 0.59923 0.33761 -0.04173 0.03885  -0.00804 152 VAL A N   
1167 C CA  . VAL A 152 ? 0.20192 0.51617 0.27792 -0.02850 0.03557  0.00057  152 VAL A CA  
1168 C C   . VAL A 152 ? 0.17894 0.47557 0.23631 -0.03691 0.03467  0.02531  152 VAL A C   
1169 O O   . VAL A 152 ? 0.24761 0.52767 0.29423 -0.04913 0.03401  0.03787  152 VAL A O   
1170 C CB  . VAL A 152 ? 0.27391 0.56878 0.36448 -0.01516 0.03174  -0.00452 152 VAL A CB  
1171 C CG1 . VAL A 152 ? 0.14666 0.41042 0.23322 -0.00094 0.02892  0.00020  152 VAL A CG1 
1172 C CG2 . VAL A 152 ? 0.13210 0.43307 0.23571 -0.00661 0.02854  -0.02576 152 VAL A CG2 
1173 N N   . ILE A 153 ? 0.19902 0.48846 0.25011 -0.02893 0.03155  0.03127  153 ILE A N   
1174 C CA  . ILE A 153 ? 0.20288 0.46090 0.23815 -0.02750 0.02524  0.05235  153 ILE A CA  
1175 C C   . ILE A 153 ? 0.20368 0.43512 0.25080 -0.00861 0.02235  0.04917  153 ILE A C   
1176 O O   . ILE A 153 ? 0.22434 0.46832 0.28477 0.00047  0.02400  0.03546  153 ILE A O   
1177 C CB  . ILE A 153 ? 0.22213 0.49829 0.24182 -0.03335 0.02202  0.06188  153 ILE A CB  
1178 C CG1 . ILE A 153 ? 0.33698 0.63469 0.33727 -0.05648 0.02687  0.06843  153 ILE A CG1 
1179 C CG2 . ILE A 153 ? 0.19752 0.44133 0.20829 -0.02420 0.01205  0.08056  153 ILE A CG2 
1180 C CD1 . ILE A 153 ? 0.32859 0.67394 0.32766 -0.06389 0.03313  0.05400  153 ILE A CD1 
1181 N N   . THR A 154 ? 0.22368 0.41780 0.26549 -0.00417 0.01932  0.06003  154 THR A N   
1182 C CA  . THR A 154 ? 0.20885 0.38012 0.26074 0.01147  0.01986  0.05491  154 THR A CA  
1183 C C   . THR A 154 ? 0.27096 0.41477 0.31704 0.01868  0.01485  0.06923  154 THR A C   
1184 O O   . THR A 154 ? 0.26865 0.39220 0.30003 0.01181  0.01057  0.08287  154 THR A O   
1185 C CB  . THR A 154 ? 0.27271 0.42684 0.32672 0.01270  0.02269  0.04575  154 THR A CB  
1186 O OG1 . THR A 154 ? 0.29755 0.42924 0.35563 0.02529  0.02511  0.04129  154 THR A OG1 
1187 C CG2 . THR A 154 ? 0.28487 0.41804 0.32659 0.00264  0.02044  0.05442  154 THR A CG2 
1188 N N   . ILE A 155 ? 0.23279 0.37771 0.29176 0.03207  0.01499  0.06552  155 ILE A N   
1189 C CA  . ILE A 155 ? 0.27702 0.40524 0.33822 0.04336  0.00908  0.07570  155 ILE A CA  
1190 C C   . ILE A 155 ? 0.31217 0.41290 0.38026 0.05425  0.01534  0.06872  155 ILE A C   
1191 O O   . ILE A 155 ? 0.32965 0.43538 0.40576 0.05589  0.02391  0.05568  155 ILE A O   
1192 C CB  . ILE A 155 ? 0.32392 0.48271 0.39868 0.04996  0.00408  0.07468  155 ILE A CB  
1193 C CG1 . ILE A 155 ? 0.28761 0.47319 0.34899 0.03733  -0.00161 0.08059  155 ILE A CG1 
1194 C CG2 . ILE A 155 ? 0.30695 0.45269 0.38924 0.06528  -0.00482 0.08417  155 ILE A CG2 
1195 C CD1 . ILE A 155 ? 0.27360 0.49632 0.34700 0.03888  -0.00422 0.07200  155 ILE A CD1 
1196 N N   . GLU A 156 ? 0.28876 0.35754 0.35074 0.06098  0.01123  0.07714  156 GLU A N   
1197 C CA  . GLU A 156 ? 0.40528 0.44836 0.47233 0.07230  0.01794  0.06879  156 GLU A CA  
1198 C C   . GLU A 156 ? 0.42496 0.45730 0.50309 0.08942  0.01114  0.07438  156 GLU A C   
1199 O O   . GLU A 156 ? 0.42695 0.43764 0.49351 0.09020  -0.00033 0.08895  156 GLU A O   
1200 C CB  . GLU A 156 ? 0.33912 0.34751 0.38687 0.06431  0.02008  0.06800  156 GLU A CB  
1201 C CG  . GLU A 156 ? 0.40417 0.38637 0.45215 0.07465  0.02834  0.05673  156 GLU A CG  
1202 C CD  . GLU A 156 ? 0.43222 0.43611 0.49646 0.08254  0.03951  0.04394  156 GLU A CD  
1203 O OE1 . GLU A 156 ? 0.40215 0.42536 0.46640 0.07462  0.04404  0.03879  156 GLU A OE1 
1204 O OE2 . GLU A 156 ? 0.47398 0.47534 0.55207 0.09652  0.04400  0.03831  156 GLU A OE2 
1205 N N   . LYS A 157 ? 0.42271 0.47021 0.52378 0.10292  0.01785  0.06265  157 LYS A N   
1206 C CA  . LYS A 157 ? 0.38739 0.43344 0.50739 0.12298  0.01066  0.06436  157 LYS A CA  
1207 C C   . LYS A 157 ? 0.43572 0.43635 0.54782 0.13342  0.01093  0.06325  157 LYS A C   
1208 O O   . LYS A 157 ? 0.43213 0.41476 0.54935 0.14878  -0.00171 0.07140  157 LYS A O   
1209 C CB  . LYS A 157 ? 0.42154 0.50462 0.57328 0.13220  0.02018  0.04866  157 LYS A CB  
1210 C CG  . LYS A 157 ? 0.43428 0.52358 0.61391 0.15584  0.01396  0.04541  157 LYS A CG  
1211 C CD  . LYS A 157 ? 0.55542 0.69653 0.76706 0.15887  0.01190  0.03680  157 LYS A CD  
1212 C CE  . LYS A 157 ? 0.43466 0.58093 0.66314 0.17648  -0.00960 0.04214  157 LYS A CE  
1213 N NZ  . LYS A 157 ? 0.38972 0.58344 0.64997 0.17490  -0.01313 0.02980  157 LYS A NZ  
1214 N N   . ASP A 158 ? 0.39629 0.37571 0.49473 0.12628  0.02373  0.05263  158 ASP A N   
1215 C CA  . ASP A 158 ? 0.52716 0.46699 0.62052 0.13730  0.02722  0.04489  158 ASP A CA  
1216 C C   . ASP A 158 ? 0.49486 0.39131 0.55753 0.12403  0.02017  0.05455  158 ASP A C   
1217 O O   . ASP A 158 ? 0.50174 0.39709 0.54664 0.10613  0.02543  0.05223  158 ASP A O   
1218 C CB  . ASP A 158 ? 0.45197 0.39749 0.54777 0.13756  0.04683  0.02455  158 ASP A CB  
1219 C CG  . ASP A 158 ? 0.54029 0.45361 0.63560 0.15210  0.05293  0.01145  158 ASP A CG  
1220 O OD1 . ASP A 158 ? 0.59983 0.47057 0.67950 0.15418  0.04293  0.01751  158 ASP A OD1 
1221 O OD2 . ASP A 158 ? 0.58371 0.51400 0.69360 0.16014  0.06895  -0.00631 158 ASP A OD2 
1222 N N   . PRO A 159 ? 0.52929 0.38853 0.58528 0.13161  0.00758  0.06488  159 PRO A N   
1223 C CA  . PRO A 159 ? 0.51158 0.32792 0.53795 0.11455  0.00195  0.07333  159 PRO A CA  
1224 C C   . PRO A 159 ? 0.57654 0.36779 0.58917 0.10907  0.01291  0.05612  159 PRO A C   
1225 O O   . PRO A 159 ? 0.61507 0.38147 0.60511 0.09021  0.00967  0.05984  159 PRO A O   
1226 C CB  . PRO A 159 ? 0.58067 0.35533 0.60339 0.12712  -0.01384 0.08692  159 PRO A CB  
1227 C CG  . PRO A 159 ? 0.54402 0.33903 0.59796 0.15614  -0.01665 0.08156  159 PRO A CG  
1228 C CD  . PRO A 159 ? 0.52644 0.38102 0.60234 0.15585  -0.00373 0.06964  159 PRO A CD  
1229 N N   . ASN A 160 ? 0.60781 0.40649 0.63211 0.12319  0.02595  0.03671  160 ASN A N   
1230 C CA  . ASN A 160 ? 0.59862 0.37502 0.60347 0.11603  0.03616  0.02037  160 ASN A CA  
1231 C C   . ASN A 160 ? 0.57937 0.38367 0.57350 0.09823  0.04283  0.01785  160 ASN A C   
1232 O O   . ASN A 160 ? 0.59605 0.38119 0.56737 0.08606  0.04445  0.01058  160 ASN A O   
1233 C CB  . ASN A 160 ? 0.58288 0.35413 0.59919 0.13643  0.04930  -0.00064 160 ASN A CB  
1234 C CG  . ASN A 160 ? 0.74715 0.48247 0.77333 0.15714  0.04129  -0.00219 160 ASN A CG  
1235 O OD1 . ASN A 160 ? 0.82891 0.52869 0.84338 0.15257  0.02572  0.01281  160 ASN A OD1 
1236 N ND2 . ASN A 160 ? 0.69520 0.44518 0.74424 0.17582  0.04919  -0.02113 160 ASN A ND2 
1237 N N   . VAL A 161 ? 0.53521 0.38268 0.54508 0.09737  0.04520  0.02275  161 VAL A N   
1238 C CA  . VAL A 161 ? 0.45788 0.32715 0.45811 0.08201  0.04781  0.02233  161 VAL A CA  
1239 C C   . VAL A 161 ? 0.55812 0.42173 0.54574 0.06466  0.03608  0.03307  161 VAL A C   
1240 O O   . VAL A 161 ? 0.52579 0.38747 0.49854 0.05243  0.03516  0.02850  161 VAL A O   
1241 C CB  . VAL A 161 ? 0.45903 0.37141 0.47989 0.08493  0.05191  0.02435  161 VAL A CB  
1242 C CG1 . VAL A 161 ? 0.39262 0.32213 0.40438 0.07134  0.05181  0.02451  161 VAL A CG1 
1243 C CG2 . VAL A 161 ? 0.48151 0.40421 0.51590 0.09741  0.06595  0.01160  161 VAL A CG2 
1244 N N   . ILE A 162 ? 0.50547 0.36768 0.49857 0.06282  0.02658  0.04740  162 ILE A N   
1245 C CA  . ILE A 162 ? 0.48039 0.34001 0.46226 0.04327  0.01781  0.05794  162 ILE A CA  
1246 C C   . ILE A 162 ? 0.54924 0.36968 0.51167 0.03316  0.01537  0.05230  162 ILE A C   
1247 O O   . ILE A 162 ? 0.59841 0.42615 0.55271 0.01563  0.01250  0.05031  162 ILE A O   
1248 C CB  . ILE A 162 ? 0.55895 0.41761 0.54396 0.04283  0.00900  0.07605  162 ILE A CB  
1249 C CG1 . ILE A 162 ? 0.50958 0.41281 0.51195 0.04927  0.00992  0.07988  162 ILE A CG1 
1250 C CG2 . ILE A 162 ? 0.61371 0.46421 0.58321 0.01885  0.00238  0.08750  162 ILE A CG2 
1251 C CD1 . ILE A 162 ? 0.44422 0.34539 0.44785 0.05406  -0.00015 0.09674  162 ILE A CD1 
1252 N N   . GLU A 163 ? 0.60182 0.38175 0.55851 0.04460  0.01590  0.04744  163 GLU A N   
1253 C CA  . GLU A 163 ? 0.61703 0.35490 0.55350 0.03425  0.01293  0.04018  163 GLU A CA  
1254 C C   . GLU A 163 ? 0.55441 0.29898 0.47944 0.02947  0.01848  0.02333  163 GLU A C   
1255 O O   . GLU A 163 ? 0.61760 0.35043 0.52803 0.01209  0.01285  0.01920  163 GLU A O   
1256 C CB  . GLU A 163 ? 0.60642 0.29712 0.54017 0.05068  0.01224  0.03605  163 GLU A CB  
1257 C CG  . GLU A 163 ? 0.70532 0.36154 0.63334 0.04471  -0.00001 0.05396  163 GLU A CG  
1258 C CD  . GLU A 163 ? 0.84095 0.50650 0.75769 0.01413  -0.00617 0.06681  163 GLU A CD  
1259 O OE1 . GLU A 163 ? 0.87394 0.52276 0.77645 -0.00403 -0.00706 0.05803  163 GLU A OE1 
1260 O OE2 . GLU A 163 ? 0.75595 0.44881 0.67846 0.00735  -0.00970 0.08401  163 GLU A OE2 
1261 N N   . ILE A 164 ? 0.62687 0.39098 0.55706 0.04302  0.02862  0.01408  164 ILE A N   
1262 C CA  . ILE A 164 ? 0.54130 0.30991 0.45474 0.03805  0.03249  0.00135  164 ILE A CA  
1263 C C   . ILE A 164 ? 0.54825 0.34833 0.46389 0.02384  0.02456  0.00718  164 ILE A C   
1264 O O   . ILE A 164 ? 0.56089 0.35721 0.46087 0.01340  0.01855  0.00012  164 ILE A O   
1265 C CB  . ILE A 164 ? 0.47393 0.25461 0.38978 0.05286  0.04674  -0.00760 164 ILE A CB  
1266 C CG1 . ILE A 164 ? 0.63768 0.38747 0.54710 0.06571  0.05635  -0.02160 164 ILE A CG1 
1267 C CG2 . ILE A 164 ? 0.59379 0.38596 0.49135 0.04565  0.04826  -0.01317 164 ILE A CG2 
1268 C CD1 . ILE A 164 ? 0.66301 0.38742 0.53983 0.05942  0.06010  -0.03774 164 ILE A CD1 
1269 N N   . ALA A 165 ? 0.53885 0.37237 0.47483 0.02431  0.02353  0.01836  165 ALA A N   
1270 C CA  . ALA A 165 ? 0.46225 0.32806 0.40460 0.01263  0.01650  0.02127  165 ALA A CA  
1271 C C   . ALA A 165 ? 0.39999 0.25804 0.33678 -0.00594 0.00706  0.02201  165 ALA A C   
1272 O O   . ALA A 165 ? 0.42299 0.30075 0.36051 -0.01527 0.00020  0.01669  165 ALA A O   
1273 C CB  . ALA A 165 ? 0.39764 0.29843 0.36124 0.01494  0.01775  0.03137  165 ALA A CB  
1274 N N   . ARG A 166 ? 0.49772 0.32459 0.42877 -0.01127 0.00582  0.02737  166 ARG A N   
1275 C CA  . ARG A 166 ? 0.56122 0.37876 0.48732 -0.03359 -0.00196 0.02999  166 ARG A CA  
1276 C C   . ARG A 166 ? 0.52720 0.32950 0.43821 -0.04279 -0.00777 0.01520  166 ARG A C   
1277 O O   . ARG A 166 ? 0.59029 0.40488 0.50388 -0.06332 -0.01527 0.01340  166 ARG A O   
1278 C CB  . ARG A 166 ? 0.59066 0.36781 0.50974 -0.03615 -0.00274 0.04081  166 ARG A CB  
1279 C CG  . ARG A 166 ? 0.67161 0.45907 0.59387 -0.05787 -0.00674 0.05623  166 ARG A CG  
1280 C CD  . ARG A 166 ? 0.75128 0.48566 0.65948 -0.06065 -0.01029 0.06876  166 ARG A CD  
1281 N NE  . ARG A 166 ? 0.74249 0.48085 0.65679 -0.04497 -0.00971 0.08392  166 ARG A NE  
1282 C CZ  . ARG A 166 ? 0.78398 0.54719 0.70019 -0.05651 -0.01098 0.10054  166 ARG A CZ  
1283 N NH1 . ARG A 166 ? 0.78440 0.57039 0.69829 -0.08493 -0.01064 0.10422  166 ARG A NH1 
1284 N NH2 . ARG A 166 ? 0.77127 0.54033 0.69218 -0.03985 -0.01238 0.11239  166 ARG A NH2 
1285 N N   . ILE A 167 ? 0.57939 0.35778 0.47415 -0.02956 -0.00435 0.00351  167 ILE A N   
1286 C CA  . ILE A 167 ? 0.52896 0.29248 0.40394 -0.03799 -0.01126 -0.01121 167 ILE A CA  
1287 C C   . ILE A 167 ? 0.56837 0.36033 0.44001 -0.03178 -0.01476 -0.01730 167 ILE A C   
1288 O O   . ILE A 167 ? 0.60023 0.38326 0.45271 -0.03729 -0.02312 -0.02874 167 ILE A O   
1289 C CB  . ILE A 167 ? 0.72209 0.43478 0.57351 -0.03078 -0.00605 -0.02247 167 ILE A CB  
1290 C CG1 . ILE A 167 ? 0.60497 0.31521 0.45592 -0.00742 0.00776  -0.02414 167 ILE A CG1 
1291 C CG2 . ILE A 167 ? 0.69868 0.37351 0.54977 -0.03985 -0.00801 -0.01799 167 ILE A CG2 
1292 C CD1 . ILE A 167 ? 0.68137 0.34641 0.51981 0.00311  0.01564  -0.03473 167 ILE A CD1 
1293 N N   . ASN A 168 ? 0.48411 0.30786 0.37216 -0.02104 -0.01048 -0.00979 168 ASN A N   
1294 C CA  . ASN A 168 ? 0.46659 0.31250 0.35164 -0.01435 -0.01542 -0.01330 168 ASN A CA  
1295 C C   . ASN A 168 ? 0.46693 0.35279 0.37338 -0.02413 -0.02811 -0.01317 168 ASN A C   
1296 O O   . ASN A 168 ? 0.44330 0.35821 0.37495 -0.02684 -0.02498 -0.00577 168 ASN A O   
1297 C CB  . ASN A 168 ? 0.43916 0.29571 0.33186 0.00112  -0.00409 -0.00710 168 ASN A CB  
1298 C CG  . ASN A 168 ? 0.42186 0.29590 0.31159 0.00752  -0.00984 -0.00829 168 ASN A CG  
1299 O OD1 . ASN A 168 ? 0.48973 0.36034 0.36418 0.00449  -0.02232 -0.01433 168 ASN A OD1 
1300 N ND2 . ASN A 168 ? 0.40677 0.29781 0.31044 0.01662  -0.00256 -0.00259 168 ASN A ND2 
1301 N N   . PRO A 169 ? 0.46256 0.35455 0.36086 -0.02923 -0.04266 -0.02236 169 PRO A N   
1302 C CA  . PRO A 169 ? 0.35380 0.29153 0.27962 -0.03643 -0.05494 -0.02535 169 PRO A CA  
1303 C C   . PRO A 169 ? 0.46449 0.43536 0.41139 -0.02264 -0.05369 -0.02159 169 PRO A C   
1304 O O   . PRO A 169 ? 0.41177 0.42589 0.38832 -0.02738 -0.05898 -0.02470 169 PRO A O   
1305 C CB  . PRO A 169 ? 0.49649 0.43064 0.40618 -0.03913 -0.07324 -0.03690 169 PRO A CB  
1306 C CG  . PRO A 169 ? 0.53116 0.41875 0.39982 -0.03039 -0.06919 -0.03811 169 PRO A CG  
1307 C CD  . PRO A 169 ? 0.48273 0.34298 0.34645 -0.02848 -0.04920 -0.03180 169 PRO A CD  
1308 N N   . TRP A 170 ? 0.43371 0.38693 0.36734 -0.00696 -0.04590 -0.01670 170 TRP A N   
1309 C CA  . TRP A 170 ? 0.44140 0.41978 0.39295 0.00542  -0.04473 -0.01421 170 TRP A CA  
1310 C C   . TRP A 170 ? 0.34602 0.34264 0.31886 0.00385  -0.03078 -0.00710 170 TRP A C   
1311 O O   . TRP A 170 ? 0.39731 0.42025 0.38865 0.01137  -0.02974 -0.00743 170 TRP A O   
1312 C CB  . TRP A 170 ? 0.43855 0.38811 0.36433 0.01914  -0.04258 -0.01180 170 TRP A CB  
1313 C CG  . TRP A 170 ? 0.41589 0.35147 0.31866 0.02335  -0.05982 -0.01667 170 TRP A CG  
1314 C CD1 . TRP A 170 ? 0.43319 0.34268 0.30610 0.01702  -0.06652 -0.02090 170 TRP A CD1 
1315 C CD2 . TRP A 170 ? 0.42514 0.36904 0.33002 0.03577  -0.07442 -0.01778 170 TRP A CD2 
1316 N NE1 . TRP A 170 ? 0.43552 0.33830 0.28956 0.02411  -0.08546 -0.02325 170 TRP A NE1 
1317 C CE2 . TRP A 170 ? 0.49548 0.41720 0.36918 0.03673  -0.09126 -0.02056 170 TRP A CE2 
1318 C CE3 . TRP A 170 ? 0.48691 0.45197 0.41545 0.04701  -0.07599 -0.01738 170 TRP A CE3 
1319 C CZ2 . TRP A 170 ? 0.56901 0.48786 0.43453 0.04973  -0.11147 -0.02065 170 TRP A CZ2 
1320 C CZ3 . TRP A 170 ? 0.57054 0.53086 0.49310 0.06051  -0.09489 -0.01926 170 TRP A CZ3 
1321 C CH2 . TRP A 170 ? 0.57680 0.51359 0.46813 0.06236  -0.11321 -0.01971 170 TRP A CH2 
1322 N N   . SER A 171 ? 0.33314 0.31367 0.30174 -0.00464 -0.02142 -0.00098 171 SER A N   
1323 C CA  . SER A 171 ? 0.36543 0.36200 0.35025 -0.00710 -0.01159 0.00754  171 SER A CA  
1324 C C   . SER A 171 ? 0.42058 0.43907 0.41896 -0.02576 -0.01357 0.00965  171 SER A C   
1325 O O   . SER A 171 ? 0.42244 0.45046 0.42776 -0.03112 -0.00652 0.01885  171 SER A O   
1326 C CB  . SER A 171 ? 0.42687 0.39001 0.39851 -0.00154 -0.00123 0.01469  171 SER A CB  
1327 O OG  . SER A 171 ? 0.34970 0.29770 0.31001 0.01223  0.00379  0.01181  171 SER A OG  
1328 N N   . ARG A 172 ? 0.36236 0.39095 0.36379 -0.03720 -0.02346 0.00134  172 ARG A N   
1329 C CA  . ARG A 172 ? 0.36304 0.40744 0.37403 -0.06058 -0.02389 0.00277  172 ARG A CA  
1330 C C   . ARG A 172 ? 0.44124 0.52809 0.47300 -0.06784 -0.01627 0.00742  172 ARG A C   
1331 O O   . ARG A 172 ? 0.47813 0.56223 0.50645 -0.08599 -0.01039 0.01742  172 ARG A O   
1332 C CB  . ARG A 172 ? 0.35300 0.41688 0.37263 -0.07044 -0.03684 -0.01074 172 ARG A CB  
1333 C CG  . ARG A 172 ? 0.51049 0.53674 0.51021 -0.08573 -0.04173 -0.01247 172 ARG A CG  
1334 C CD  . ARG A 172 ? 0.52578 0.56526 0.52820 -0.08914 -0.05819 -0.02777 172 ARG A CD  
1335 N NE  . ARG A 172 ? 0.55008 0.54290 0.52476 -0.09829 -0.06296 -0.03134 172 ARG A NE  
1336 C CZ  . ARG A 172 ? 0.53602 0.52326 0.49914 -0.09795 -0.07793 -0.04376 172 ARG A CZ  
1337 N NH1 . ARG A 172 ? 0.52550 0.54993 0.50333 -0.08780 -0.09206 -0.05245 172 ARG A NH1 
1338 N NH2 . ARG A 172 ? 0.63857 0.58031 0.57351 -0.10701 -0.08019 -0.04826 172 ARG A NH2 
1339 N N   . GLU A 173 ? 0.31868 0.44239 0.36910 -0.05469 -0.01647 0.00011  173 GLU A N   
1340 C CA  . GLU A 173 ? 0.30606 0.47521 0.37578 -0.06225 -0.00867 0.00018  173 GLU A CA  
1341 C C   . GLU A 173 ? 0.37031 0.52442 0.42700 -0.06258 0.00148  0.01565  173 GLU A C   
1342 O O   . GLU A 173 ? 0.33826 0.52416 0.40204 -0.07432 0.00860  0.01877  173 GLU A O   
1343 C CB  . GLU A 173 ? 0.30151 0.50889 0.39420 -0.04523 -0.01219 -0.01430 173 GLU A CB  
1344 C CG  . GLU A 173 ? 0.30567 0.53253 0.41459 -0.04160 -0.02613 -0.02991 173 GLU A CG  
1345 C CD  . GLU A 173 ? 0.41350 0.60002 0.50401 -0.02261 -0.03756 -0.03066 173 GLU A CD  
1346 O OE1 . GLU A 173 ? 0.41584 0.55451 0.47802 -0.02211 -0.03418 -0.01990 173 GLU A OE1 
1347 O OE2 . GLU A 173 ? 0.52585 0.72830 0.62926 -0.00812 -0.05020 -0.04235 173 GLU A OE2 
1348 N N   . LEU A 174 ? 0.37592 0.48527 0.41380 -0.05043 0.00205  0.02456  174 LEU A N   
1349 C CA  . LEU A 174 ? 0.44793 0.54215 0.47488 -0.05101 0.00813  0.03978  174 LEU A CA  
1350 C C   . LEU A 174 ? 0.45920 0.54083 0.47421 -0.07403 0.00908  0.05240  174 LEU A C   
1351 O O   . LEU A 174 ? 0.41963 0.50143 0.42639 -0.07925 0.01252  0.06601  174 LEU A O   
1352 C CB  . LEU A 174 ? 0.43965 0.49128 0.45369 -0.03321 0.00830  0.04414  174 LEU A CB  
1353 C CG  . LEU A 174 ? 0.44299 0.49667 0.46213 -0.01301 0.00974  0.03578  174 LEU A CG  
1354 C CD1 . LEU A 174 ? 0.37368 0.38767 0.38025 -0.00088 0.01283  0.03990  174 LEU A CD1 
1355 C CD2 . LEU A 174 ? 0.31775 0.40711 0.35114 -0.00767 0.01345  0.03439  174 LEU A CD2 
1356 N N   . PHE A 175 ? 0.49133 0.56047 0.50302 -0.08941 0.00507  0.04871  175 PHE A N   
1357 C CA  . PHE A 175 ? 0.56885 0.61300 0.56479 -0.11324 0.00551  0.06163  175 PHE A CA  
1358 C C   . PHE A 175 ? 0.58613 0.66512 0.59268 -0.14248 0.00706  0.05590  175 PHE A C   
1359 O O   . PHE A 175 ? 0.54695 0.60506 0.53845 -0.16736 0.00864  0.06780  175 PHE A O   
1360 C CB  . PHE A 175 ? 0.54320 0.52611 0.52052 -0.10906 -0.00005 0.06369  175 PHE A CB  
1361 C CG  . PHE A 175 ? 0.54250 0.49784 0.51461 -0.08011 -0.00007 0.06327  175 PHE A CG  
1362 C CD1 . PHE A 175 ? 0.59220 0.52260 0.55526 -0.06976 0.00121  0.07749  175 PHE A CD1 
1363 C CD2 . PHE A 175 ? 0.47583 0.43101 0.45149 -0.06427 -0.00180 0.04866  175 PHE A CD2 
1364 C CE1 . PHE A 175 ? 0.55315 0.46567 0.51690 -0.04434 0.00253  0.07448  175 PHE A CE1 
1365 C CE2 . PHE A 175 ? 0.54585 0.47935 0.51650 -0.04150 0.00113  0.04736  175 PHE A CE2 
1366 C CZ  . PHE A 175 ? 0.49975 0.41495 0.46738 -0.03167 0.00419  0.05899  175 PHE A CZ  
1367 N N   . THR A 176 ? 0.64801 0.77862 0.68074 -0.14086 0.00621  0.03778  176 THR A N   
1368 C CA  . THR A 176 ? 0.69926 0.87134 0.74898 -0.16846 0.00791  0.02879  176 THR A CA  
1369 C C   . THR A 176 ? 0.61991 0.84097 0.67793 -0.18315 0.02024  0.03207  176 THR A C   
1370 O O   . THR A 176 ? 0.62076 0.89896 0.70553 -0.17567 0.02362  0.01641  176 THR A O   
1371 C CB  . THR A 176 ? 0.74593 0.95344 0.82306 -0.15839 -0.00123 0.00610  176 THR A CB  
1372 O OG1 . THR A 176 ? 0.67117 0.91826 0.76848 -0.13535 -0.00004 -0.00408 176 THR A OG1 
1373 C CG2 . THR A 176 ? 0.61437 0.77248 0.67614 -0.14472 -0.01335 0.00307  176 THR A CG2 
1374 N N   . GLY A 177 ? 0.64806 0.84430 0.68055 -0.20496 0.02661  0.05227  177 GLY A N   
1375 C CA  . GLY A 177 ? 0.60371 0.84153 0.63448 -0.22290 0.03920  0.05796  177 GLY A CA  
1376 C C   . GLY A 177 ? 0.64960 0.89603 0.67745 -0.19709 0.04098  0.06042  177 GLY A C   
1377 O O   . GLY A 177 ? 0.57087 0.77004 0.58036 -0.17782 0.03466  0.07320  177 GLY A O   
1378 N N   . GLY A 178 ? 0.71137 1.01200 0.75672 -0.19090 0.04757  0.04418  178 GLY A N   
1379 C CA  . GLY A 178 ? 0.51063 0.82407 0.55505 -0.16948 0.04925  0.04249  178 GLY A CA  
1380 C C   . GLY A 178 ? 0.53889 0.89053 0.61528 -0.14569 0.04757  0.01539  178 GLY A C   
1381 O O   . GLY A 178 ? 0.55569 0.92610 0.65511 -0.14432 0.04420  -0.00101 178 GLY A O   
1382 N N   . LYS A 179 ? 0.57958 0.93882 0.65416 -0.12740 0.04862  0.01116  179 LYS A N   
1383 C CA  . LYS A 179 ? 0.46147 0.83230 0.55610 -0.09936 0.04445  -0.00794 179 LYS A CA  
1384 C C   . LYS A 179 ? 0.28546 0.63054 0.37070 -0.08523 0.04172  0.00443  179 LYS A C   
1385 O O   . LYS A 179 ? 0.30014 0.64776 0.38729 -0.06819 0.04083  -0.00430 179 LYS A O   
1386 C CB  . LYS A 179 ? 0.49459 0.87161 0.61544 -0.08764 0.03669  -0.02367 179 LYS A CB  
1387 C CG  . LYS A 179 ? 0.51541 0.92301 0.65641 -0.07770 0.03616  -0.04769 179 LYS A CG  
1388 C CD  . LYS A 179 ? 0.45381 0.86223 0.59459 -0.05767 0.03647  -0.05860 179 LYS A CD  
1389 C CE  . LYS A 179 ? 0.47395 0.90880 0.63587 -0.04664 0.03472  -0.08235 179 LYS A CE  
1390 N NZ  . LYS A 179 ? 0.43359 0.90572 0.59663 -0.06345 0.04459  -0.09173 179 LYS A NZ  
1391 N N   . ILE A 180 ? 0.27330 0.57788 0.34221 -0.08974 0.03803  0.02396  180 ILE A N   
1392 C CA  . ILE A 180 ? 0.36037 0.62281 0.41595 -0.07139 0.03253  0.03487  180 ILE A CA  
1393 C C   . ILE A 180 ? 0.35900 0.58546 0.38730 -0.08330 0.03096  0.05893  180 ILE A C   
1394 O O   . ILE A 180 ? 0.37502 0.58400 0.39336 -0.10110 0.03049  0.06741  180 ILE A O   
1395 C CB  . ILE A 180 ? 0.31952 0.54915 0.38152 -0.05310 0.02515  0.02890  180 ILE A CB  
1396 C CG1 . ILE A 180 ? 0.26961 0.52776 0.35540 -0.04065 0.02314  0.00733  180 ILE A CG1 
1397 C CG2 . ILE A 180 ? 0.31398 0.50846 0.36576 -0.03601 0.02283  0.03750  180 ILE A CG2 
1398 C CD1 . ILE A 180 ? 0.27187 0.49531 0.35659 -0.02393 0.01512  0.00361  180 ILE A CD1 
1399 N N   . GLN A 181 ? 0.23360 0.44753 0.25043 -0.07321 0.02860  0.06951  181 GLN A N   
1400 C CA  . GLN A 181 ? 0.27338 0.44967 0.26536 -0.07838 0.02337  0.09277  181 GLN A CA  
1401 C C   . GLN A 181 ? 0.31441 0.46023 0.30917 -0.05355 0.01670  0.09598  181 GLN A C   
1402 O O   . GLN A 181 ? 0.38819 0.55352 0.39665 -0.03853 0.01753  0.08560  181 GLN A O   
1403 C CB  . GLN A 181 ? 0.30325 0.50282 0.27573 -0.09505 0.02580  0.10467  181 GLN A CB  
1404 C CG  . GLN A 181 ? 0.26884 0.46838 0.23404 -0.08103 0.01971  0.11197  181 GLN A CG  
1405 C CD  . GLN A 181 ? 0.32717 0.53818 0.26351 -0.09932 0.01908  0.12839  181 GLN A CD  
1406 O OE1 . GLN A 181 ? 0.40238 0.63647 0.32729 -0.12454 0.02802  0.12898  181 GLN A OE1 
1407 N NE2 . GLN A 181 ? 0.35999 0.55634 0.28288 -0.08818 0.00824  0.14232  181 GLN A NE2 
1408 N N   . VAL A 182 ? 0.35806 0.45643 0.34141 -0.05003 0.01080  0.10843  182 VAL A N   
1409 C CA  . VAL A 182 ? 0.34355 0.41392 0.33441 -0.02657 0.00688  0.10685  182 VAL A CA  
1410 C C   . VAL A 182 ? 0.40574 0.45733 0.38463 -0.01960 -0.00199 0.12502  182 VAL A C   
1411 O O   . VAL A 182 ? 0.46865 0.48944 0.42650 -0.03019 -0.00795 0.14237  182 VAL A O   
1412 C CB  . VAL A 182 ? 0.42238 0.45356 0.41178 -0.02407 0.00676  0.10236  182 VAL A CB  
1413 C CG1 . VAL A 182 ? 0.47613 0.48049 0.47199 -0.00082 0.00522  0.09970  182 VAL A CG1 
1414 C CG2 . VAL A 182 ? 0.38398 0.43550 0.38470 -0.02863 0.01182  0.08479  182 VAL A CG2 
1415 N N   . ILE A 183 ? 0.41025 0.47961 0.40228 -0.00247 -0.00424 0.12132  183 ILE A N   
1416 C CA  . ILE A 183 ? 0.38443 0.44163 0.37091 0.00900  -0.01573 0.13626  183 ILE A CA  
1417 C C   . ILE A 183 ? 0.43335 0.46753 0.43814 0.03258  -0.01691 0.12932  183 ILE A C   
1418 O O   . ILE A 183 ? 0.37471 0.42771 0.40025 0.04197  -0.00879 0.11216  183 ILE A O   
1419 C CB  . ILE A 183 ? 0.38873 0.48937 0.37858 0.00983  -0.01878 0.13557  183 ILE A CB  
1420 C CG1 . ILE A 183 ? 0.39201 0.51687 0.36058 -0.01453 -0.01562 0.14108  183 ILE A CG1 
1421 C CG2 . ILE A 183 ? 0.41992 0.50971 0.40721 0.02518  -0.03437 0.15028  183 ILE A CG2 
1422 C CD1 . ILE A 183 ? 0.32046 0.48805 0.28737 -0.01575 -0.01831 0.13836  183 ILE A CD1 
1423 N N   . GLN A 184 ? 0.44596 0.43775 0.44221 0.04145  -0.02619 0.14173  184 GLN A N   
1424 C CA  . GLN A 184 ? 0.51282 0.48838 0.52932 0.06627  -0.02718 0.13344  184 GLN A CA  
1425 C C   . GLN A 184 ? 0.48496 0.48100 0.51451 0.08297  -0.03924 0.13990  184 GLN A C   
1426 O O   . GLN A 184 ? 0.49074 0.47304 0.50241 0.08196  -0.05441 0.15989  184 GLN A O   
1427 C CB  . GLN A 184 ? 0.48303 0.40150 0.48847 0.07190  -0.03147 0.13867  184 GLN A CB  
1428 C CG  . GLN A 184 ? 0.47541 0.38650 0.50500 0.09605  -0.02629 0.12205  184 GLN A CG  
1429 C CD  . GLN A 184 ? 0.56612 0.43090 0.59486 0.11462  -0.03730 0.12837  184 GLN A CD  
1430 O OE1 . GLN A 184 ? 0.65351 0.46949 0.66246 0.10786  -0.03901 0.13222  184 GLN A OE1 
1431 N NE2 . GLN A 184 ? 0.64200 0.52115 0.69443 0.13921  -0.04573 0.12767  184 GLN A NE2 
1432 N N   . GLY A 185 ? 0.41296 0.44136 0.47207 0.09688  -0.03341 0.12363  185 GLY A N   
1433 C CA  . GLY A 185 ? 0.40228 0.45496 0.48019 0.11390  -0.04580 0.12653  185 GLY A CA  
1434 C C   . GLY A 185 ? 0.38820 0.48638 0.49744 0.11883  -0.03523 0.10620  185 GLY A C   
1435 O O   . GLY A 185 ? 0.36621 0.46893 0.48035 0.11142  -0.01839 0.09116  185 GLY A O   
1436 N N   . ASP A 186 ? 0.37066 0.50088 0.49952 0.13057  -0.04685 0.10675  186 ASP A N   
1437 C CA  . ASP A 186 ? 0.36123 0.53608 0.52335 0.13441  -0.03842 0.08754  186 ASP A CA  
1438 C C   . ASP A 186 ? 0.30514 0.51437 0.45871 0.11562  -0.03723 0.08483  186 ASP A C   
1439 O O   . ASP A 186 ? 0.28917 0.51465 0.43101 0.11256  -0.05264 0.09603  186 ASP A O   
1440 C CB  . ASP A 186 ? 0.37697 0.57183 0.57023 0.15665  -0.05208 0.08502  186 ASP A CB  
1441 C CG  . ASP A 186 ? 0.47353 0.71295 0.69595 0.15045  -0.04507 0.06319  186 ASP A CG  
1442 O OD1 . ASP A 186 ? 0.46619 0.70816 0.70538 0.14710  -0.02601 0.04489  186 ASP A OD1 
1443 O OD2 . ASP A 186 ? 0.51252 0.78072 0.73829 0.14684  -0.05867 0.06468  186 ASP A OD2 
1444 N N   . ALA A 187 ? 0.29298 0.51072 0.45007 0.10352  -0.01965 0.06955  187 ALA A N   
1445 C CA  . ALA A 187 ? 0.26314 0.50405 0.40913 0.08597  -0.01690 0.06473  187 ALA A CA  
1446 C C   . ALA A 187 ? 0.27107 0.55477 0.43127 0.08640  -0.02781 0.06093  187 ALA A C   
1447 O O   . ALA A 187 ? 0.20858 0.50984 0.35174 0.07447  -0.03320 0.06285  187 ALA A O   
1448 C CB  . ALA A 187 ? 0.27976 0.51776 0.43096 0.07752  0.00131  0.04827  187 ALA A CB  
1449 N N   . PHE A 188 ? 0.24552 0.54472 0.43526 0.09734  -0.03002 0.05189  188 PHE A N   
1450 C CA  . PHE A 188 ? 0.23339 0.56388 0.43414 0.09378  -0.04060 0.04431  188 PHE A CA  
1451 C C   . PHE A 188 ? 0.30953 0.64665 0.49271 0.09989  -0.06350 0.06330  188 PHE A C   
1452 O O   . PHE A 188 ? 0.20292 0.56533 0.37700 0.09090  -0.07290 0.06153  188 PHE A O   
1453 C CB  . PHE A 188 ? 0.28193 0.62048 0.51824 0.10144  -0.03749 0.03000  188 PHE A CB  
1454 C CG  . PHE A 188 ? 0.24596 0.61809 0.49970 0.09907  -0.04960 0.02276  188 PHE A CG  
1455 C CD1 . PHE A 188 ? 0.39061 0.77334 0.64828 0.11269  -0.07255 0.03341  188 PHE A CD1 
1456 C CD2 . PHE A 188 ? 0.32181 0.71093 0.58779 0.08357  -0.03897 0.00592  188 PHE A CD2 
1457 C CE1 . PHE A 188 ? 0.38708 0.80229 0.66221 0.11082  -0.08496 0.02631  188 PHE A CE1 
1458 C CE2 . PHE A 188 ? 0.29490 0.71587 0.57799 0.08076  -0.04992 -0.00113 188 PHE A CE2 
1459 C CZ  . PHE A 188 ? 0.37481 0.81129 0.66358 0.09443  -0.07293 0.00844  188 PHE A CZ  
1460 N N   . GLU A 189 ? 0.30868 0.61701 0.48228 0.11393  -0.07293 0.08173  189 GLU A N   
1461 C CA  . GLU A 189 ? 0.30067 0.60068 0.44820 0.11751  -0.09567 0.10324  189 GLU A CA  
1462 C C   . GLU A 189 ? 0.26871 0.55560 0.37333 0.09973  -0.09389 0.11970  189 GLU A C   
1463 O O   . GLU A 189 ? 0.35859 0.65791 0.43603 0.09031  -0.10673 0.13046  189 GLU A O   
1464 C CB  . GLU A 189 ? 0.34033 0.60452 0.49411 0.13929  -0.10836 0.11404  189 GLU A CB  
1465 C CG  . GLU A 189 ? 0.32771 0.61033 0.52416 0.15640  -0.11621 0.09771  189 GLU A CG  
1466 C CD  . GLU A 189 ? 0.44789 0.76608 0.64960 0.15380  -0.13461 0.09526  189 GLU A CD  
1467 O OE1 . GLU A 189 ? 0.40303 0.70771 0.58356 0.16090  -0.15926 0.11260  189 GLU A OE1 
1468 O OE2 . GLU A 189 ? 0.37850 0.73412 0.60320 0.14364  -0.12511 0.07598  189 GLU A OE2 
1469 N N   . VAL A 190 ? 0.28601 0.54394 0.38090 0.09042  -0.07563 0.11688  190 VAL A N   
1470 C CA  . VAL A 190 ? 0.32603 0.56869 0.38237 0.06975  -0.07082 0.12731  190 VAL A CA  
1471 C C   . VAL A 190 ? 0.28940 0.57291 0.33538 0.05288  -0.06780 0.11741  190 VAL A C   
1472 O O   . VAL A 190 ? 0.39343 0.68198 0.40610 0.03967  -0.07483 0.13017  190 VAL A O   
1473 C CB  . VAL A 190 ? 0.25029 0.46398 0.30551 0.06318  -0.05239 0.12107  190 VAL A CB  
1474 C CG1 . VAL A 190 ? 0.28677 0.50246 0.31259 0.04005  -0.04489 0.12451  190 VAL A CG1 
1475 C CG2 . VAL A 190 ? 0.34913 0.51546 0.40133 0.07507  -0.05691 0.13373  190 VAL A CG2 
1476 N N   . VAL A 191 ? 0.26077 0.57170 0.33252 0.05187  -0.05669 0.09400  191 VAL A N   
1477 C CA  . VAL A 191 ? 0.22417 0.56950 0.28748 0.03664  -0.05229 0.08023  191 VAL A CA  
1478 C C   . VAL A 191 ? 0.40383 0.77650 0.45017 0.03400  -0.07061 0.08832  191 VAL A C   
1479 O O   . VAL A 191 ? 0.34906 0.74389 0.37211 0.01832  -0.06883 0.08345  191 VAL A O   
1480 C CB  . VAL A 191 ? 0.30045 0.66336 0.39527 0.03773  -0.04053 0.05478  191 VAL A CB  
1481 C CG1 . VAL A 191 ? 0.22002 0.55497 0.32079 0.03710  -0.02348 0.04799  191 VAL A CG1 
1482 C CG2 . VAL A 191 ? 0.18810 0.56485 0.31474 0.05177  -0.04866 0.05091  191 VAL A CG2 
1483 N N   . LYS A 192 ? 0.37524 0.74826 0.43233 0.04999  -0.08924 0.09973  192 LYS A N   
1484 C CA  . LYS A 192 ? 0.30029 0.68640 0.33744 0.04794  -0.10774 0.10700  192 LYS A CA  
1485 C C   . LYS A 192 ? 0.39169 0.75957 0.37805 0.03386  -0.11288 0.12910  192 LYS A C   
1486 O O   . LYS A 192 ? 0.35832 0.74308 0.31811 0.02129  -0.11820 0.12838  192 LYS A O   
1487 C CB  . LYS A 192 ? 0.37675 0.75148 0.43566 0.06928  -0.12569 0.11288  192 LYS A CB  
1488 C CG  . LYS A 192 ? 0.38840 0.78851 0.49352 0.07721  -0.12190 0.08866  192 LYS A CG  
1489 C CD  . LYS A 192 ? 0.35449 0.75570 0.47719 0.09467  -0.14420 0.09272  192 LYS A CD  
1490 C CE  . LYS A 192 ? 0.41604 0.82625 0.59056 0.10653  -0.13608 0.07414  192 LYS A CE  
1491 N NZ  . LYS A 192 ? 0.42898 0.82442 0.62379 0.12968  -0.15441 0.08270  192 LYS A NZ  
1492 N N   A LYS A 193 ? 0.39612 0.72637 0.36695 0.03341  -0.10955 0.14769  193 LYS A N   
1493 N N   B LYS A 193 ? 0.39626 0.72631 0.36713 0.03357  -0.10974 0.14782  193 LYS A N   
1494 C CA  A LYS A 193 ? 0.43936 0.74374 0.36158 0.01584  -0.11092 0.16821  193 LYS A CA  
1495 C CA  B LYS A 193 ? 0.43865 0.74459 0.36054 0.01550  -0.11107 0.16773  193 LYS A CA  
1496 C C   A LYS A 193 ? 0.45789 0.77971 0.36318 -0.00832 -0.08941 0.15907  193 LYS A C   
1497 C C   B LYS A 193 ? 0.45047 0.78323 0.35483 -0.00914 -0.09137 0.15531  193 LYS A C   
1498 O O   A LYS A 193 ? 0.43477 0.73660 0.30496 -0.02665 -0.08460 0.17234  193 LYS A O   
1499 O O   B LYS A 193 ? 0.45437 0.78510 0.32173 -0.02794 -0.08975 0.16279  193 LYS A O   
1500 C CB  A LYS A 193 ? 0.50347 0.75097 0.41573 0.02484  -0.11837 0.19135  193 LYS A CB  
1501 C CB  B LYS A 193 ? 0.49208 0.74394 0.40345 0.01965  -0.11228 0.18883  193 LYS A CB  
1502 C CG  A LYS A 193 ? 0.44674 0.67557 0.38141 0.02948  -0.10364 0.18783  193 LYS A CG  
1503 C CG  B LYS A 193 ? 0.50755 0.74721 0.39565 -0.00399 -0.09349 0.19274  193 LYS A CG  
1504 C CD  A LYS A 193 ? 0.54996 0.73864 0.45158 0.01094  -0.09571 0.20458  193 LYS A CD  
1505 C CD  B LYS A 193 ? 0.50632 0.69122 0.35778 -0.01353 -0.09918 0.21711  193 LYS A CD  
1506 C CE  A LYS A 193 ? 0.43271 0.61959 0.35558 0.00439  -0.07226 0.18505  193 LYS A CE  
1507 C CE  B LYS A 193 ? 0.51520 0.70109 0.34252 -0.04370 -0.07972 0.21643  193 LYS A CE  
1508 N NZ  A LYS A 193 ? 0.44258 0.57660 0.35931 0.00443  -0.07043 0.19685  193 LYS A NZ  
1509 N NZ  B LYS A 193 ? 0.43564 0.66044 0.28864 -0.04954 -0.05971 0.19406  193 LYS A NZ  
1510 N N   . PHE A 194 ? 0.41090 0.76365 0.34436 -0.00867 -0.07452 0.13240  194 PHE A N   
1511 C CA  . PHE A 194 ? 0.41196 0.78581 0.33568 -0.02805 -0.05492 0.11630  194 PHE A CA  
1512 C C   . PHE A 194 ? 0.45370 0.86583 0.35636 -0.04091 -0.05690 0.10656  194 PHE A C   
1513 O O   . PHE A 194 ? 0.32936 0.75815 0.24238 -0.03253 -0.06842 0.09901  194 PHE A O   
1514 C CB  . PHE A 194 ? 0.33664 0.71620 0.29994 -0.02065 -0.03917 0.08959  194 PHE A CB  
1515 C CG  . PHE A 194 ? 0.35971 0.70232 0.33669 -0.01487 -0.03102 0.09449  194 PHE A CG  
1516 C CD1 . PHE A 194 ? 0.42833 0.74008 0.38147 -0.02241 -0.03285 0.11685  194 PHE A CD1 
1517 C CD2 . PHE A 194 ? 0.36260 0.69870 0.37279 -0.00362 -0.02218 0.07713  194 PHE A CD2 
1518 C CE1 . PHE A 194 ? 0.32600 0.60424 0.29054 -0.01825 -0.02633 0.11918  194 PHE A CE1 
1519 C CE2 . PHE A 194 ? 0.23055 0.53330 0.24895 0.00104  -0.01587 0.08107  194 PHE A CE2 
1520 C CZ  . PHE A 194 ? 0.22659 0.50172 0.22349 -0.00576 -0.01823 0.10089  194 PHE A CZ  
1521 N N   . LYS A 195 ? 0.44319 0.86419 0.32309 -0.06160 -0.04283 0.10251  195 LYS A N   
1522 C CA  . LYS A 195 ? 0.51457 0.96646 0.37953 -0.07393 -0.04043 0.08845  195 LYS A CA  
1523 C C   . LYS A 195 ? 0.38914 0.87724 0.28244 -0.06938 -0.03108 0.05448  195 LYS A C   
1524 O O   . LYS A 195 ? 0.31356 0.80385 0.23159 -0.06279 -0.02079 0.03999  195 LYS A O   
1525 C CB  . LYS A 195 ? 0.41149 0.86441 0.25029 -0.09706 -0.02728 0.09114  195 LYS A CB  
1526 C CG  . LYS A 195 ? 0.47013 0.87999 0.28223 -0.10544 -0.03162 0.12170  195 LYS A CG  
1527 C CD  . LYS A 195 ? 0.58895 0.96532 0.38080 -0.09405 -0.05559 0.14840  195 LYS A CD  
1528 C CE  . LYS A 195 ? 0.56241 0.91461 0.30673 -0.11194 -0.06038 0.16998  195 LYS A CE  
1529 N NZ  . LYS A 195 ? 0.73369 1.04174 0.46416 -0.12083 -0.05640 0.19002  195 LYS A NZ  
1530 N N   . GLN A 196 ? 0.35789 0.87009 0.24524 -0.07280 -0.03571 0.04152  196 GLN A N   
1531 C CA  . GLN A 196 ? 0.39357 0.93492 0.30408 -0.07102 -0.02678 0.00757  196 GLN A CA  
1532 C C   . GLN A 196 ? 0.36555 0.92058 0.28325 -0.08017 -0.00653 -0.01283 196 GLN A C   
1533 O O   . GLN A 196 ? 0.40955 0.96380 0.30923 -0.09400 0.00040  -0.00457 196 GLN A O   
1534 C CB  . GLN A 196 ? 0.38715 0.94947 0.28452 -0.07643 -0.03475 -0.00174 196 GLN A CB  
1535 C CG  . GLN A 196 ? 0.40896 0.99457 0.33059 -0.07446 -0.02671 -0.03762 196 GLN A CG  
1536 C CD  . GLN A 196 ? 0.51988 1.12574 0.42787 -0.08098 -0.03422 -0.04853 196 GLN A CD  
1537 O OE1 . GLN A 196 ? 0.55227 1.17892 0.45434 -0.09109 -0.02354 -0.06957 196 GLN A OE1 
1538 N NE2 . GLN A 196 ? 0.41081 1.01138 0.31725 -0.07416 -0.05359 -0.03610 196 GLN A NE2 
1539 N N   . ALA A 197 ? 0.34294 0.90754 0.28983 -0.07182 0.00113  -0.04082 197 ALA A N   
1540 C CA  . ALA A 197 ? 0.31580 0.88667 0.28018 -0.07380 0.01480  -0.06444 197 ALA A CA  
1541 C C   . ALA A 197 ? 0.33818 0.89171 0.29764 -0.07892 0.02067  -0.04911 197 ALA A C   
1542 O O   . ALA A 197 ? 0.35927 0.92325 0.31092 -0.09110 0.02751  -0.05425 197 ALA A O   
1543 C CB  . ALA A 197 ? 0.36048 0.95887 0.31943 -0.08428 0.01926  -0.08598 197 ALA A CB  
1544 N N   . SER A 198 ? 0.30820 0.83554 0.27306 -0.06995 0.01846  -0.03105 198 SER A N   
1545 C CA  . SER A 198 ? 0.30801 0.81223 0.27141 -0.07326 0.02306  -0.01529 198 SER A CA  
1546 C C   . SER A 198 ? 0.29917 0.78451 0.28957 -0.06237 0.02897  -0.03398 198 SER A C   
1547 O O   . SER A 198 ? 0.30021 0.77991 0.29140 -0.06845 0.03448  -0.03454 198 SER A O   
1548 C CB  . SER A 198 ? 0.35174 0.83158 0.30584 -0.06735 0.01599  0.01473  198 SER A CB  
1549 O OG  . SER A 198 ? 0.47824 0.94838 0.39953 -0.07860 0.00689  0.04140  198 SER A OG  
1550 N N   . PHE A 199 ? 0.23673 0.70672 0.24704 -0.04661 0.02678  -0.04776 199 PHE A N   
1551 C CA  . PHE A 199 ? 0.19195 0.62645 0.22233 -0.03368 0.02886  -0.05532 199 PHE A CA  
1552 C C   . PHE A 199 ? 0.20949 0.64096 0.25309 -0.02619 0.02990  -0.08347 199 PHE A C   
1553 O O   . PHE A 199 ? 0.26242 0.70331 0.30792 -0.02457 0.02739  -0.09617 199 PHE A O   
1554 C CB  . PHE A 199 ? 0.17553 0.58125 0.21735 -0.02236 0.02515  -0.04207 199 PHE A CB  
1555 C CG  . PHE A 199 ? 0.20375 0.60879 0.23865 -0.02639 0.02396  -0.01488 199 PHE A CG  
1556 C CD1 . PHE A 199 ? 0.17602 0.56566 0.20999 -0.02979 0.02772  -0.00555 199 PHE A CD1 
1557 C CD2 . PHE A 199 ? 0.19340 0.60904 0.22248 -0.02645 0.01669  0.00176  199 PHE A CD2 
1558 C CE1 . PHE A 199 ? 0.21010 0.59184 0.23472 -0.03471 0.02643  0.02046  199 PHE A CE1 
1559 C CE2 . PHE A 199 ? 0.22888 0.61952 0.24489 -0.02696 0.01001  0.02796  199 PHE A CE2 
1560 C CZ  . PHE A 199 ? 0.24909 0.62006 0.26143 -0.03166 0.01541  0.03733  199 PHE A CZ  
1561 N N   . ASP A 200 ? 0.17026 0.58995 0.22483 -0.02146 0.03296  -0.09310 200 ASP A N   
1562 C CA  . ASP A 200 ? 0.20457 0.61664 0.27543 -0.01118 0.03260  -0.11725 200 ASP A CA  
1563 C C   . ASP A 200 ? 0.23023 0.60602 0.31384 0.00145  0.02921  -0.11572 200 ASP A C   
1564 O O   . ASP A 200 ? 0.22559 0.59654 0.31932 0.00731  0.02774  -0.13351 200 ASP A O   
1565 C CB  . ASP A 200 ? 0.17700 0.59368 0.25759 -0.00907 0.03550  -0.12666 200 ASP A CB  
1566 C CG  . ASP A 200 ? 0.28039 0.73606 0.35088 -0.02365 0.04067  -0.13198 200 ASP A CG  
1567 O OD1 . ASP A 200 ? 0.33969 0.81936 0.41292 -0.02547 0.04207  -0.15302 200 ASP A OD1 
1568 O OD2 . ASP A 200 ? 0.27816 0.74100 0.33834 -0.03470 0.04378  -0.11556 200 ASP A OD2 
1569 N N   . VAL A 201 ? 0.28640 0.63706 0.37092 0.00481  0.02840  -0.09611 201 VAL A N   
1570 C CA  . VAL A 201 ? 0.21448 0.53341 0.30980 0.01425  0.02636  -0.09385 201 VAL A CA  
1571 C C   . VAL A 201 ? 0.19187 0.49787 0.28276 0.01261  0.02595  -0.07112 201 VAL A C   
1572 O O   . VAL A 201 ? 0.23711 0.55074 0.31964 0.00738  0.02657  -0.05653 201 VAL A O   
1573 C CB  . VAL A 201 ? 0.28344 0.58064 0.39166 0.02543  0.02498  -0.10118 201 VAL A CB  
1574 C CG1 . VAL A 201 ? 0.14291 0.45909 0.25480 0.02597  0.02520  -0.11401 201 VAL A CG1 
1575 C CG2 . VAL A 201 ? 0.20775 0.48078 0.31664 0.02912  0.02442  -0.08358 201 VAL A CG2 
1576 N N   . ILE A 202 ? 0.14715 0.43623 0.24538 0.01637  0.02533  -0.06958 202 ILE A N   
1577 C CA  . ILE A 202 ? 0.13048 0.40617 0.22959 0.01726  0.02531  -0.05168 202 ILE A CA  
1578 C C   . ILE A 202 ? 0.13890 0.38524 0.24748 0.02430  0.02786  -0.05305 202 ILE A C   
1579 O O   . ILE A 202 ? 0.20197 0.44270 0.31843 0.02643  0.02888  -0.06740 202 ILE A O   
1580 C CB  . ILE A 202 ? 0.13318 0.42581 0.23351 0.01323  0.02268  -0.04927 202 ILE A CB  
1581 C CG1 . ILE A 202 ? 0.11810 0.44489 0.20568 0.00644  0.01931  -0.04479 202 ILE A CG1 
1582 C CG2 . ILE A 202 ? 0.15846 0.43661 0.26615 0.01700  0.02281  -0.03455 202 ILE A CG2 
1583 C CD1 . ILE A 202 ? 0.12271 0.47316 0.21275 0.00336  0.01396  -0.04618 202 ILE A CD1 
1584 N N   . ILE A 203 ? 0.14925 0.37915 0.25655 0.02770  0.02939  -0.03990 203 ILE A N   
1585 C CA  . ILE A 203 ? 0.13151 0.33733 0.24369 0.03374  0.03321  -0.04016 203 ILE A CA  
1586 C C   . ILE A 203 ? 0.16310 0.36446 0.27716 0.03261  0.03699  -0.02856 203 ILE A C   
1587 O O   . ILE A 203 ? 0.16313 0.36408 0.27300 0.03407  0.03632  -0.01604 203 ILE A O   
1588 C CB  . ILE A 203 ? 0.17797 0.37020 0.28647 0.04055  0.03181  -0.03861 203 ILE A CB  
1589 C CG1 . ILE A 203 ? 0.15785 0.35684 0.27033 0.04422  0.02696  -0.05322 203 ILE A CG1 
1590 C CG2 . ILE A 203 ? 0.13902 0.29034 0.23784 0.04343  0.03356  -0.03402 203 ILE A CG2 
1591 C CD1 . ILE A 203 ? 0.15845 0.36061 0.27010 0.04702  0.02292  -0.05142 203 ILE A CD1 
1592 N N   . HIS A 204 ? 0.14401 0.34458 0.26681 0.02981  0.04128  -0.03439 204 HIS A N   
1593 C CA  . HIS A 204 ? 0.12924 0.33150 0.25906 0.02851  0.04505  -0.02686 204 HIS A CA  
1594 C C   . HIS A 204 ? 0.17936 0.35006 0.30360 0.02805  0.05405  -0.02600 204 HIS A C   
1595 O O   . HIS A 204 ? 0.24363 0.39907 0.36632 0.02183  0.05802  -0.03405 204 HIS A O   
1596 C CB  . HIS A 204 ? 0.09936 0.32240 0.24066 0.02180  0.04257  -0.03376 204 HIS A CB  
1597 C CG  . HIS A 204 ? 0.17409 0.40577 0.32780 0.02235  0.04379  -0.02769 204 HIS A CG  
1598 N ND1 . HIS A 204 ? 0.09868 0.33007 0.25255 0.03032  0.04116  -0.01588 204 HIS A ND1 
1599 C CD2 . HIS A 204 ? 0.10487 0.34828 0.27419 0.01644  0.04698  -0.03388 204 HIS A CD2 
1600 C CE1 . HIS A 204 ? 0.14675 0.38944 0.31760 0.03177  0.04215  -0.01597 204 HIS A CE1 
1601 N NE2 . HIS A 204 ? 0.12949 0.38065 0.30991 0.02270  0.04600  -0.02614 204 HIS A NE2 
1602 N N   . ASP A 205 ? 0.21881 0.37445 0.33558 0.03297  0.05699  -0.01597 205 ASP A N   
1603 C CA  . ASP A 205 ? 0.20927 0.33233 0.31304 0.03150  0.06608  -0.01403 205 ASP A CA  
1604 C C   . ASP A 205 ? 0.27473 0.40547 0.38806 0.03438  0.07371  -0.01017 205 ASP A C   
1605 O O   . ASP A 205 ? 0.31502 0.42851 0.41716 0.04014  0.07507  -0.00419 205 ASP A O   
1606 C CB  . ASP A 205 ? 0.36245 0.45660 0.44410 0.03602  0.06143  -0.00918 205 ASP A CB  
1607 C CG  . ASP A 205 ? 0.38950 0.44554 0.44912 0.03257  0.06792  -0.00827 205 ASP A CG  
1608 O OD1 . ASP A 205 ? 0.39165 0.44362 0.45271 0.02475  0.07886  -0.01082 205 ASP A OD1 
1609 O OD2 . ASP A 205 ? 0.31353 0.34538 0.35351 0.03633  0.06185  -0.00494 205 ASP A OD2 
1610 N N   . PRO A 206 ? 0.21306 0.37083 0.34906 0.03105  0.07838  -0.01556 206 PRO A N   
1611 C CA  . PRO A 206 ? 0.27383 0.44762 0.42642 0.03799  0.08250  -0.01435 206 PRO A CA  
1612 C C   . PRO A 206 ? 0.32816 0.48156 0.47145 0.03445  0.09766  -0.01730 206 PRO A C   
1613 O O   . PRO A 206 ? 0.27603 0.40457 0.40152 0.02397  0.10703  -0.01921 206 PRO A O   
1614 C CB  . PRO A 206 ? 0.17765 0.38112 0.35293 0.03390  0.07780  -0.01754 206 PRO A CB  
1615 C CG  . PRO A 206 ? 0.18119 0.38139 0.35156 0.01978  0.08207  -0.02637 206 PRO A CG  
1616 C CD  . PRO A 206 ? 0.21359 0.38939 0.36285 0.02078  0.07888  -0.02526 206 PRO A CD  
1617 N N   . PRO A 207 ? 0.32370 0.48533 0.47566 0.04253  0.09953  -0.01864 207 PRO A N   
1618 C CA  . PRO A 207 ? 0.31180 0.46571 0.45867 0.03732  0.11514  -0.02462 207 PRO A CA  
1619 C C   . PRO A 207 ? 0.35837 0.52954 0.51586 0.02247  0.12273  -0.03048 207 PRO A C   
1620 O O   . PRO A 207 ? 0.25273 0.44262 0.42428 0.01781  0.11512  -0.03103 207 PRO A O   
1621 C CB  . PRO A 207 ? 0.41357 0.58373 0.57747 0.05249  0.11252  -0.02758 207 PRO A CB  
1622 C CG  . PRO A 207 ? 0.32566 0.49380 0.49482 0.06498  0.09632  -0.01988 207 PRO A CG  
1623 C CD  . PRO A 207 ? 0.27661 0.45339 0.44477 0.05673  0.08767  -0.01586 207 PRO A CD  
1624 N N   . ARG A 208 ? 0.37118 0.53424 0.52066 0.01313  0.13878  -0.03551 208 ARG A N   
1625 C CA  . ARG A 208 ? 0.36641 0.54119 0.52417 -0.00505 0.14865  -0.04139 208 ARG A CA  
1626 C C   . ARG A 208 ? 0.32699 0.54639 0.52186 -0.00023 0.14098  -0.04539 208 ARG A C   
1627 O O   . ARG A 208 ? 0.28705 0.52658 0.49952 0.01756  0.13403  -0.04410 208 ARG A O   
1628 C CB  . ARG A 208 ? 0.44753 0.60896 0.58897 -0.01624 0.16802  -0.04561 208 ARG A CB  
1629 C CG  . ARG A 208 ? 0.64055 0.75226 0.73704 -0.02425 0.17807  -0.04036 208 ARG A CG  
1630 C CD  . ARG A 208 ? 0.72869 0.80445 0.79873 -0.04067 0.18080  -0.03462 208 ARG A CD  
1631 N NE  . ARG A 208 ? 0.67981 0.76332 0.76603 -0.03511 0.16715  -0.03330 208 ARG A NE  
1632 C CZ  . ARG A 208 ? 0.60955 0.66975 0.67906 -0.02312 0.15263  -0.02583 208 ARG A CZ  
1633 N NH1 . ARG A 208 ? 0.72242 0.74961 0.75961 -0.01637 0.15062  -0.01886 208 ARG A NH1 
1634 N NH2 . ARG A 208 ? 0.47986 0.55176 0.56405 -0.01794 0.13644  -0.02621 208 ARG A NH2 
1635 N N   . PHE A 209 ? 0.35219 0.58387 0.55841 -0.01670 0.14254  -0.05064 209 PHE A N   
1636 C CA  . PHE A 209 ? 0.28994 0.56262 0.53069 -0.01642 0.13615  -0.05621 209 PHE A CA  
1637 C C   . PHE A 209 ? 0.32405 0.62460 0.58861 -0.00258 0.13862  -0.05871 209 PHE A C   
1638 O O   . PHE A 209 ? 0.31469 0.63842 0.60209 0.01360  0.12513  -0.05608 209 PHE A O   
1639 C CB  . PHE A 209 ? 0.36238 0.64030 0.60837 -0.04184 0.14625  -0.06575 209 PHE A CB  
1640 C CG  . PHE A 209 ? 0.34627 0.65661 0.61940 -0.04571 0.13425  -0.07216 209 PHE A CG  
1641 C CD1 . PHE A 209 ? 0.36762 0.68010 0.64084 -0.03766 0.11678  -0.06906 209 PHE A CD1 
1642 C CD2 . PHE A 209 ? 0.45736 0.79890 0.75603 -0.05803 0.14072  -0.08261 209 PHE A CD2 
1643 C CE1 . PHE A 209 ? 0.35499 0.69777 0.64999 -0.04228 0.10527  -0.07656 209 PHE A CE1 
1644 C CE2 . PHE A 209 ? 0.42859 0.80149 0.75194 -0.06257 0.12892  -0.09022 209 PHE A CE2 
1645 C CZ  . PHE A 209 ? 0.46662 0.83907 0.78657 -0.05441 0.11067  -0.08713 209 PHE A CZ  
1646 N N   . SER A 210 ? 0.36657 0.66411 0.62597 -0.00941 0.15637  -0.06445 210 SER A N   
1647 C CA  . SER A 210 ? 0.38136 0.71006 0.66806 0.00193  0.16175  -0.07115 210 SER A CA  
1648 C C   . SER A 210 ? 0.28194 0.60897 0.57299 0.02968  0.15192  -0.06563 210 SER A C   
1649 O O   . SER A 210 ? 0.47798 0.83381 0.79978 0.04449  0.14960  -0.07011 210 SER A O   
1650 C CB  . SER A 210 ? 0.37814 0.70082 0.65279 -0.01218 0.18455  -0.07912 210 SER A CB  
1651 O OG  . SER A 210 ? 0.40545 0.68546 0.63965 -0.01383 0.19082  -0.07365 210 SER A OG  
1652 N N   . LEU A 211 ? 0.36565 0.65937 0.62820 0.03680  0.14584  -0.05701 211 LEU A N   
1653 C CA  . LEU A 211 ? 0.44885 0.73617 0.71283 0.06105  0.13640  -0.05230 211 LEU A CA  
1654 C C   . LEU A 211 ? 0.39707 0.68370 0.66588 0.07066  0.11635  -0.04091 211 LEU A C   
1655 O O   . LEU A 211 ? 0.40792 0.68928 0.68161 0.09015  0.10707  -0.03576 211 LEU A O   
1656 C CB  . LEU A 211 ? 0.46523 0.71580 0.69470 0.06221  0.14422  -0.05357 211 LEU A CB  
1657 C CG  . LEU A 211 ? 0.52075 0.76135 0.73354 0.04612  0.16554  -0.06222 211 LEU A CG  
1658 C CD1 . LEU A 211 ? 0.45372 0.64888 0.62430 0.03872  0.17119  -0.05960 211 LEU A CD1 
1659 C CD2 . LEU A 211 ? 0.37069 0.63464 0.60469 0.05693  0.17640  -0.07331 211 LEU A CD2 
1660 N N   . ALA A 212 ? 0.40921 0.69936 0.67721 0.05702  0.10973  -0.03776 212 ALA A N   
1661 C CA  . ALA A 212 ? 0.24103 0.52900 0.51198 0.06252  0.09217  -0.02850 212 ALA A CA  
1662 C C   . ALA A 212 ? 0.25564 0.56682 0.54131 0.04967  0.08413  -0.03260 212 ALA A C   
1663 O O   . ALA A 212 ? 0.27952 0.58228 0.55182 0.04190  0.07644  -0.03055 212 ALA A O   
1664 C CB  . ALA A 212 ? 0.25659 0.51223 0.49509 0.06038  0.09100  -0.02202 212 ALA A CB  
1665 N N   . GLY A 213 ? 0.26697 0.61033 0.58064 0.04777  0.08541  -0.04057 213 GLY A N   
1666 C CA  . GLY A 213 ? 0.20512 0.57223 0.53134 0.03349  0.07910  -0.04770 213 GLY A CA  
1667 C C   . GLY A 213 ? 0.15565 0.53003 0.48198 0.03775  0.05831  -0.04330 213 GLY A C   
1668 O O   . GLY A 213 ? 0.16503 0.54332 0.48359 0.02421  0.05378  -0.04823 213 GLY A O   
1669 N N   . HIS A 214 ? 0.19047 0.56561 0.52291 0.05601  0.04509  -0.03520 214 HIS A N   
1670 C CA  . HIS A 214 ? 0.24728 0.63296 0.57545 0.05962  0.02371  -0.03098 214 HIS A CA  
1671 C C   . HIS A 214 ? 0.17456 0.53659 0.46899 0.05141  0.02254  -0.02718 214 HIS A C   
1672 O O   . HIS A 214 ? 0.15437 0.52920 0.43906 0.04831  0.00881  -0.02657 214 HIS A O   
1673 C CB  . HIS A 214 ? 0.20189 0.59146 0.54111 0.08137  0.00798  -0.02219 214 HIS A CB  
1674 C CG  . HIS A 214 ? 0.19477 0.55076 0.51935 0.09201  0.01353  -0.01518 214 HIS A CG  
1675 N ND1 . HIS A 214 ? 0.27133 0.61420 0.60431 0.09638  0.03130  -0.01881 214 HIS A ND1 
1676 C CD2 . HIS A 214 ? 0.28336 0.61772 0.58185 0.09836  0.00414  -0.00479 214 HIS A CD2 
1677 C CE1 . HIS A 214 ? 0.31043 0.62263 0.62573 0.10498  0.03140  -0.01391 214 HIS A CE1 
1678 N NE2 . HIS A 214 ? 0.27643 0.58337 0.57001 0.10638  0.01478  -0.00441 214 HIS A NE2 
1679 N N   . LEU A 215 ? 0.19217 0.52263 0.46783 0.04828  0.03643  -0.02503 215 LEU A N   
1680 C CA  . LEU A 215 ? 0.19223 0.50272 0.43947 0.04055  0.03659  -0.02323 215 LEU A CA  
1681 C C   . LEU A 215 ? 0.18760 0.49851 0.43002 0.02372  0.04360  -0.03331 215 LEU A C   
1682 O O   . LEU A 215 ? 0.18158 0.47599 0.40382 0.01819  0.04469  -0.03441 215 LEU A O   
1683 C CB  . LEU A 215 ? 0.18664 0.46465 0.41685 0.04534  0.04608  -0.01759 215 LEU A CB  
1684 C CG  . LEU A 215 ? 0.25080 0.52640 0.48287 0.06201  0.03732  -0.00914 215 LEU A CG  
1685 C CD1 . LEU A 215 ? 0.34522 0.59055 0.56111 0.06659  0.04692  -0.00636 215 LEU A CD1 
1686 C CD2 . LEU A 215 ? 0.23769 0.52479 0.45666 0.06533  0.02009  0.00053  215 LEU A CD2 
1687 N N   . TYR A 216 ? 0.18804 0.51832 0.44999 0.01557  0.04810  -0.04212 216 TYR A N   
1688 C CA  . TYR A 216 ? 0.16340 0.49804 0.42469 -0.00224 0.05235  -0.05466 216 TYR A CA  
1689 C C   . TYR A 216 ? 0.14220 0.51227 0.42106 -0.00685 0.04012  -0.06324 216 TYR A C   
1690 O O   . TYR A 216 ? 0.15334 0.53174 0.43731 -0.02302 0.04329  -0.07647 216 TYR A O   
1691 C CB  . TYR A 216 ? 0.27319 0.59892 0.53941 -0.01406 0.07043  -0.06046 216 TYR A CB  
1692 C CG  . TYR A 216 ? 0.24890 0.53996 0.49410 -0.01242 0.08347  -0.05422 216 TYR A CG  
1693 C CD1 . TYR A 216 ? 0.17186 0.45512 0.41406 0.00303  0.08565  -0.04424 216 TYR A CD1 
1694 C CD2 . TYR A 216 ? 0.20642 0.47133 0.43514 -0.02708 0.09385  -0.05993 216 TYR A CD2 
1695 C CE1 . TYR A 216 ? 0.26546 0.51820 0.48557 0.00364  0.09689  -0.04051 216 TYR A CE1 
1696 C CE2 . TYR A 216 ? 0.27370 0.50591 0.48146 -0.02642 0.10540  -0.05469 216 TYR A CE2 
1697 C CZ  . TYR A 216 ? 0.25131 0.47867 0.45346 -0.01121 0.10627  -0.04531 216 TYR A CZ  
1698 O OH  . TYR A 216 ? 0.26243 0.45620 0.44057 -0.01125 0.11694  -0.04150 216 TYR A OH  
1699 N N   . SER A 217 ? 0.17944 0.57006 0.46720 0.00620  0.02553  -0.05688 217 SER A N   
1700 C CA  . SER A 217 ? 0.20858 0.63588 0.51339 0.00380  0.01195  -0.06416 217 SER A CA  
1701 C C   . SER A 217 ? 0.15358 0.58727 0.43821 -0.00220 0.00058  -0.06895 217 SER A C   
1702 O O   . SER A 217 ? 0.16498 0.58056 0.42485 0.00133  -0.00070 -0.06274 217 SER A O   
1703 C CB  . SER A 217 ? 0.18567 0.63238 0.50856 0.02194  -0.00086 -0.05496 217 SER A CB  
1704 O OG  . SER A 217 ? 0.19608 0.62976 0.49804 0.03403  -0.01139 -0.04202 217 SER A OG  
1705 N N   . GLU A 218 ? 0.16601 0.62814 0.46147 -0.01213 -0.00692 -0.08161 218 GLU A N   
1706 C CA  . GLU A 218 ? 0.17273 0.64787 0.44933 -0.01669 -0.01901 -0.08766 218 GLU A CA  
1707 C C   . GLU A 218 ? 0.17383 0.65538 0.43445 -0.00199 -0.03373 -0.07237 218 GLU A C   
1708 O O   . GLU A 218 ? 0.17419 0.65245 0.40762 -0.00386 -0.03702 -0.07166 218 GLU A O   
1709 C CB  . GLU A 218 ? 0.19835 0.70711 0.49142 -0.02787 -0.02725 -0.10294 218 GLU A CB  
1710 C CG  . GLU A 218 ? 0.24603 0.74880 0.53212 -0.04746 -0.01953 -0.12282 218 GLU A CG  
1711 C CD  . GLU A 218 ? 0.39485 0.93059 0.69668 -0.06014 -0.02799 -0.13924 218 GLU A CD  
1712 O OE1 . GLU A 218 ? 0.22599 0.77500 0.55572 -0.06696 -0.02346 -0.14420 218 GLU A OE1 
1713 O OE2 . GLU A 218 ? 0.46421 1.01394 0.74969 -0.06411 -0.03850 -0.14798 218 GLU A OE2 
1714 N N   . GLU A 219 ? 0.25335 0.74584 0.53083 0.01226  -0.04297 -0.06076 219 GLU A N   
1715 C CA  . GLU A 219 ? 0.26625 0.76136 0.52693 0.02584  -0.05858 -0.04425 219 GLU A CA  
1716 C C   . GLU A 219 ? 0.17238 0.63766 0.40595 0.02784  -0.04984 -0.03436 219 GLU A C   
1717 O O   . GLU A 219 ? 0.19461 0.66349 0.39999 0.02641  -0.05698 -0.02794 219 GLU A O   
1718 C CB  . GLU A 219 ? 0.19567 0.69868 0.48127 0.04357  -0.06932 -0.03352 219 GLU A CB  
1719 C CG  . GLU A 219 ? 0.23351 0.73515 0.49778 0.05719  -0.08910 -0.01446 219 GLU A CG  
1720 C CD  . GLU A 219 ? 0.38757 0.89649 0.67686 0.07704  -0.10567 -0.00471 219 GLU A CD  
1721 O OE1 . GLU A 219 ? 0.47378 0.99018 0.80031 0.08173  -0.09814 -0.01296 219 GLU A OE1 
1722 O OE2 . GLU A 219 ? 0.43399 0.93986 0.70412 0.08778  -0.12649 0.01188  219 GLU A OE2 
1723 N N   . PHE A 220 ? 0.15651 0.59385 0.39702 0.02945  -0.03358 -0.03350 220 PHE A N   
1724 C CA  . PHE A 220 ? 0.14507 0.55474 0.36179 0.03093  -0.02569 -0.02512 220 PHE A CA  
1725 C C   . PHE A 220 ? 0.20353 0.60959 0.39940 0.01784  -0.01984 -0.03564 220 PHE A C   
1726 O O   . PHE A 220 ? 0.19048 0.59361 0.36283 0.01788  -0.02132 -0.02934 220 PHE A O   
1727 C CB  . PHE A 220 ? 0.13359 0.51380 0.36006 0.03475  -0.01026 -0.02335 220 PHE A CB  
1728 C CG  . PHE A 220 ? 0.12511 0.47873 0.32955 0.03799  -0.00470 -0.01385 220 PHE A CG  
1729 C CD1 . PHE A 220 ? 0.19887 0.55111 0.39422 0.04965  -0.01372 0.00235  220 PHE A CD1 
1730 C CD2 . PHE A 220 ? 0.11607 0.44636 0.30925 0.02978  0.00803  -0.02019 220 PHE A CD2 
1731 C CE1 . PHE A 220 ? 0.20296 0.53410 0.37941 0.05091  -0.00847 0.01152  220 PHE A CE1 
1732 C CE2 . PHE A 220 ? 0.19900 0.50724 0.37391 0.03276  0.01208  -0.01232 220 PHE A CE2 
1733 C CZ  . PHE A 220 ? 0.14411 0.45461 0.31125 0.04214  0.00466  0.00299  220 PHE A CZ  
1734 N N   . TYR A 221 ? 0.14108 0.54806 0.34639 0.00634  -0.01265 -0.05247 221 TYR A N   
1735 C CA  . TYR A 221 ? 0.22863 0.62982 0.41771 -0.00378 -0.00747 -0.06561 221 TYR A CA  
1736 C C   . TYR A 221 ? 0.22818 0.65774 0.39940 -0.00690 -0.01874 -0.06944 221 TYR A C   
1737 O O   . TYR A 221 ? 0.20752 0.63491 0.35936 -0.00978 -0.01557 -0.07415 221 TYR A O   
1738 C CB  . TYR A 221 ? 0.15170 0.54979 0.35576 -0.01628 0.00051  -0.08371 221 TYR A CB  
1739 C CG  . TYR A 221 ? 0.13708 0.50685 0.35149 -0.01729 0.01454  -0.08129 221 TYR A CG  
1740 C CD1 . TYR A 221 ? 0.21106 0.55815 0.42003 -0.00647 0.01968  -0.06564 221 TYR A CD1 
1741 C CD2 . TYR A 221 ? 0.17777 0.54443 0.40594 -0.03119 0.02320  -0.09553 221 TYR A CD2 
1742 C CE1 . TYR A 221 ? 0.20522 0.52847 0.41981 -0.00843 0.03335  -0.06417 221 TYR A CE1 
1743 C CE2 . TYR A 221 ? 0.20449 0.54752 0.43848 -0.03494 0.03728  -0.09320 221 TYR A CE2 
1744 C CZ  . TYR A 221 ? 0.21560 0.53790 0.44165 -0.02303 0.04241  -0.07751 221 TYR A CZ  
1745 O OH  . TYR A 221 ? 0.15209 0.45234 0.38015 -0.02852 0.05759  -0.07656 221 TYR A OH  
1746 N N   . ARG A 222 ? 0.16649 0.62495 0.34406 -0.00653 -0.03191 -0.06837 222 ARG A N   
1747 C CA  . ARG A 222 ? 0.19412 0.67991 0.34943 -0.00961 -0.04365 -0.06852 222 ARG A CA  
1748 C C   . ARG A 222 ? 0.19543 0.67735 0.32660 -0.00365 -0.04587 -0.04989 222 ARG A C   
1749 O O   . ARG A 222 ? 0.19976 0.69568 0.30565 -0.01063 -0.04614 -0.05310 222 ARG A O   
1750 C CB  . ARG A 222 ? 0.25136 0.76492 0.41746 -0.00762 -0.06039 -0.06621 222 ARG A CB  
1751 C CG  . ARG A 222 ? 0.21491 0.74641 0.39158 -0.02031 -0.06103 -0.08895 222 ARG A CG  
1752 C CD  . ARG A 222 ? 0.25444 0.81430 0.44690 -0.01828 -0.07800 -0.08795 222 ARG A CD  
1753 N NE  . ARG A 222 ? 0.33404 0.89189 0.54672 -0.00295 -0.08561 -0.07023 222 ARG A NE  
1754 C CZ  . ARG A 222 ? 0.29292 0.86212 0.54077 -0.00030 -0.08783 -0.07433 222 ARG A CZ  
1755 N NH1 . ARG A 222 ? 0.30709 0.88755 0.57323 -0.01402 -0.08135 -0.09368 222 ARG A NH1 
1756 N NH2 . ARG A 222 ? 0.23641 0.80667 0.50240 0.01608  -0.09665 -0.05953 222 ARG A NH2 
1757 N N   . GLU A 223 ? 0.19285 0.65723 0.33129 0.00786  -0.04653 -0.03130 223 GLU A N   
1758 C CA  . GLU A 223 ? 0.22494 0.68478 0.34062 0.01133  -0.04905 -0.01231 223 GLU A CA  
1759 C C   . GLU A 223 ? 0.17771 0.62436 0.28249 0.00479  -0.03355 -0.02006 223 GLU A C   
1760 O O   . GLU A 223 ? 0.23814 0.69849 0.31942 -0.00187 -0.03361 -0.01627 223 GLU A O   
1761 C CB  . GLU A 223 ? 0.17865 0.62005 0.30597 0.02606  -0.05392 0.00756  223 GLU A CB  
1762 C CG  . GLU A 223 ? 0.27929 0.73242 0.41372 0.03660  -0.07375 0.01904  223 GLU A CG  
1763 C CD  . GLU A 223 ? 0.29913 0.77050 0.40173 0.03138  -0.09055 0.02957  223 GLU A CD  
1764 O OE1 . GLU A 223 ? 0.33336 0.79912 0.40321 0.02457  -0.08987 0.04254  223 GLU A OE1 
1765 O OE2 . GLU A 223 ? 0.38282 0.87293 0.49171 0.03283  -0.10452 0.02536  223 GLU A OE2 
1766 N N   . LEU A 224 ? 0.17583 0.59495 0.29651 0.00606  -0.02068 -0.03063 224 LEU A N   
1767 C CA  . LEU A 224 ? 0.19276 0.59503 0.30512 0.00194  -0.00853 -0.04104 224 LEU A CA  
1768 C C   . LEU A 224 ? 0.21687 0.64360 0.31717 -0.00766 -0.00810 -0.06025 224 LEU A C   
1769 O O   . LEU A 224 ? 0.22209 0.65290 0.30859 -0.01070 -0.00237 -0.06518 224 LEU A O   
1770 C CB  . LEU A 224 ? 0.13325 0.50213 0.26213 0.00379  0.00116  -0.04945 224 LEU A CB  
1771 C CG  . LEU A 224 ? 0.22742 0.57053 0.36769 0.01188  0.00501  -0.03593 224 LEU A CG  
1772 C CD1 . LEU A 224 ? 0.20191 0.51651 0.35092 0.00985  0.01600  -0.04529 224 LEU A CD1 
1773 C CD2 . LEU A 224 ? 0.11408 0.44880 0.24248 0.01782  0.00473  -0.01946 224 LEU A CD2 
1774 N N   . PHE A 225 ? 0.20479 0.64926 0.31182 -0.01289 -0.01333 -0.07383 225 PHE A N   
1775 C CA  . PHE A 225 ? 0.17381 0.64298 0.26971 -0.02214 -0.01269 -0.09558 225 PHE A CA  
1776 C C   . PHE A 225 ? 0.27448 0.77531 0.34352 -0.02695 -0.01741 -0.08732 225 PHE A C   
1777 O O   . PHE A 225 ? 0.24199 0.75479 0.29785 -0.03174 -0.00952 -0.09788 225 PHE A O   
1778 C CB  . PHE A 225 ? 0.24133 0.72369 0.34919 -0.02822 -0.01878 -0.11015 225 PHE A CB  
1779 C CG  . PHE A 225 ? 0.26904 0.77100 0.36898 -0.03784 -0.01664 -0.13744 225 PHE A CG  
1780 C CD1 . PHE A 225 ? 0.31614 0.80216 0.42625 -0.03953 -0.00704 -0.16010 225 PHE A CD1 
1781 C CD2 . PHE A 225 ? 0.30505 0.83926 0.38766 -0.04451 -0.02468 -0.14106 225 PHE A CD2 
1782 C CE1 . PHE A 225 ? 0.27924 0.78240 0.38476 -0.04692 -0.00499 -0.18861 225 PHE A CE1 
1783 C CE2 . PHE A 225 ? 0.38362 0.93400 0.45858 -0.05308 -0.02082 -0.16782 225 PHE A CE2 
1784 C CZ  . PHE A 225 ? 0.30986 0.84456 0.39753 -0.05371 -0.01057 -0.19260 225 PHE A CZ  
1785 N N   . ARG A 226 ? 0.23546 0.74974 0.29587 -0.02603 -0.03069 -0.06815 226 ARG A N   
1786 C CA  . ARG A 226 ? 0.22309 0.75908 0.25137 -0.03262 -0.03712 -0.05418 226 ARG A CA  
1787 C C   . ARG A 226 ? 0.27441 0.80808 0.28753 -0.03620 -0.02759 -0.04586 226 ARG A C   
1788 O O   . ARG A 226 ? 0.27517 0.82780 0.26355 -0.04749 -0.02150 -0.05127 226 ARG A O   
1789 C CB  . ARG A 226 ? 0.25092 0.78329 0.27534 -0.02573 -0.05488 -0.02829 226 ARG A CB  
1790 C CG  . ARG A 226 ? 0.30127 0.83881 0.28691 -0.03235 -0.06301 -0.00635 226 ARG A CG  
1791 C CD  . ARG A 226 ? 0.30129 0.83011 0.28416 -0.02272 -0.08432 0.01627  226 ARG A CD  
1792 N NE  . ARG A 226 ? 0.35597 0.85644 0.34580 -0.01056 -0.08868 0.03968  226 ARG A NE  
1793 C CZ  . ARG A 226 ? 0.42077 0.90306 0.39251 -0.01457 -0.08120 0.05477  226 ARG A CZ  
1794 N NH1 . ARG A 226 ? 0.36727 0.85785 0.30978 -0.03152 -0.06959 0.05206  226 ARG A NH1 
1795 N NH2 . ARG A 226 ? 0.29681 0.75122 0.28056 -0.00190 -0.08475 0.07223  226 ARG A NH2 
1796 N N   . ILE A 227 ? 0.19346 0.70315 0.22257 -0.02779 -0.02408 -0.03362 227 ILE A N   
1797 C CA  . ILE A 227 ? 0.23517 0.73344 0.24766 -0.03212 -0.01446 -0.02235 227 ILE A CA  
1798 C C   . ILE A 227 ? 0.22794 0.72815 0.25103 -0.03398 0.00237  -0.04611 227 ILE A C   
1799 O O   . ILE A 227 ? 0.24103 0.73935 0.25440 -0.03897 0.01151  -0.04130 227 ILE A O   
1800 C CB  . ILE A 227 ? 0.24295 0.70473 0.26324 -0.02247 -0.01638 0.00173  227 ILE A CB  
1801 C CG1 . ILE A 227 ? 0.15654 0.59483 0.20982 -0.01136 -0.00831 -0.00960 227 ILE A CG1 
1802 C CG2 . ILE A 227 ? 0.26821 0.72632 0.28206 -0.01616 -0.03488 0.02403  227 ILE A CG2 
1803 C CD1 . ILE A 227 ? 0.16939 0.57368 0.23085 -0.00121 -0.01003 0.00995  227 ILE A CD1 
1804 N N   . LEU A 228 ? 0.22585 0.72158 0.26626 -0.02954 0.00564  -0.07119 228 LEU A N   
1805 C CA  . LEU A 228 ? 0.22696 0.70478 0.27031 -0.02744 0.01475  -0.09254 228 LEU A CA  
1806 C C   . LEU A 228 ? 0.34617 0.86286 0.37507 -0.03861 0.01678  -0.11105 228 LEU A C   
1807 O O   . LEU A 228 ? 0.20546 0.75973 0.22576 -0.04666 0.01281  -0.11700 228 LEU A O   
1808 C CB  . LEU A 228 ? 0.22410 0.67310 0.28849 -0.01928 0.01519  -0.11006 228 LEU A CB  
1809 C CG  . LEU A 228 ? 0.23263 0.63415 0.31198 -0.00898 0.01747  -0.10152 228 LEU A CG  
1810 C CD1 . LEU A 228 ? 0.23525 0.61935 0.33307 -0.00604 0.01808  -0.11822 228 LEU A CD1 
1811 C CD2 . LEU A 228 ? 0.21480 0.59964 0.29240 -0.00502 0.02189  -0.10176 228 LEU A CD2 
1812 N N   . LYS A 229 ? 0.30693 0.81576 0.33751 -0.03928 0.02212  -0.12010 229 LYS A N   
1813 C CA  . LYS A 229 ? 0.28588 0.82445 0.31446 -0.04784 0.02510  -0.14104 229 LYS A CA  
1814 C C   . LYS A 229 ? 0.28852 0.82606 0.33426 -0.04212 0.02424  -0.17008 229 LYS A C   
1815 O O   . LYS A 229 ? 0.26986 0.77517 0.32989 -0.03119 0.02291  -0.17471 229 LYS A O   
1816 C CB  . LYS A 229 ? 0.22403 0.75656 0.25622 -0.04805 0.03146  -0.14508 229 LYS A CB  
1817 C CG  . LYS A 229 ? 0.23633 0.77405 0.25181 -0.05865 0.03399  -0.12022 229 LYS A CG  
1818 C CD  . LYS A 229 ? 0.33616 0.86925 0.35971 -0.05869 0.04058  -0.12681 229 LYS A CD  
1819 C CE  . LYS A 229 ? 0.31070 0.85068 0.31673 -0.07379 0.04423  -0.10364 229 LYS A CE  
1820 N NZ  . LYS A 229 ? 0.46608 1.00786 0.48187 -0.07574 0.05105  -0.11178 229 LYS A NZ  
1821 N N   . PRO A 230 ? 0.34540 0.91530 0.39058 -0.05042 0.02641  -0.18882 230 PRO A N   
1822 C CA  . PRO A 230 ? 0.34143 0.90686 0.40589 -0.04481 0.02727  -0.21875 230 PRO A CA  
1823 C C   . PRO A 230 ? 0.32622 0.85882 0.40921 -0.03112 0.02936  -0.23031 230 PRO A C   
1824 O O   . PRO A 230 ? 0.36085 0.89279 0.44248 -0.02954 0.03260  -0.22530 230 PRO A O   
1825 C CB  . PRO A 230 ? 0.43222 1.03555 0.48815 -0.05600 0.03204  -0.23343 230 PRO A CB  
1826 C CG  . PRO A 230 ? 0.34942 0.97624 0.37811 -0.06902 0.03095  -0.20787 230 PRO A CG  
1827 C CD  . PRO A 230 ? 0.31452 0.92119 0.33894 -0.06573 0.02934  -0.18188 230 PRO A CD  
1828 N N   . GLY A 231 ? 0.31724 0.82236 0.41812 -0.02156 0.02756  -0.24491 231 GLY A N   
1829 C CA  . GLY A 231 ? 0.33931 0.80804 0.45700 -0.00651 0.02777  -0.24991 231 GLY A CA  
1830 C C   . GLY A 231 ? 0.25901 0.69705 0.37343 -0.00013 0.02656  -0.22437 231 GLY A C   
1831 O O   . GLY A 231 ? 0.31200 0.72393 0.43862 0.01206  0.02602  -0.22524 231 GLY A O   
1832 N N   . GLY A 232 ? 0.24084 0.68190 0.33992 -0.00703 0.02569  -0.20124 232 GLY A N   
1833 C CA  . GLY A 232 ? 0.20102 0.61219 0.29830 -0.00120 0.02563  -0.17601 232 GLY A CA  
1834 C C   . GLY A 232 ? 0.29030 0.66397 0.40277 0.00782  0.02464  -0.17497 232 GLY A C   
1835 O O   . GLY A 232 ? 0.28042 0.65277 0.40209 0.00638  0.02437  -0.18961 232 GLY A O   
1836 N N   . ARG A 233 ? 0.21240 0.55726 0.32793 0.01555  0.02470  -0.15858 233 ARG A N   
1837 C CA  . ARG A 233 ? 0.26515 0.57459 0.39401 0.02440  0.02440  -0.15800 233 ARG A CA  
1838 C C   . ARG A 233 ? 0.24837 0.54284 0.37343 0.02196  0.02538  -0.13275 233 ARG A C   
1839 O O   . ARG A 233 ? 0.21902 0.51465 0.33390 0.02040  0.02517  -0.11339 233 ARG A O   
1840 C CB  . ARG A 233 ? 0.26092 0.54956 0.39775 0.03736  0.02209  -0.16234 233 ARG A CB  
1841 C CG  . ARG A 233 ? 0.25753 0.55161 0.40492 0.04451  0.01955  -0.18863 233 ARG A CG  
1842 C CD  . ARG A 233 ? 0.27183 0.59556 0.41622 0.04237  0.02003  -0.19166 233 ARG A CD  
1843 N NE  . ARG A 233 ? 0.30985 0.62280 0.45586 0.04882  0.01810  -0.17867 233 ARG A NE  
1844 C CZ  . ARG A 233 ? 0.27239 0.60954 0.41483 0.04379  0.02034  -0.17573 233 ARG A CZ  
1845 N NH1 . ARG A 233 ? 0.27670 0.64854 0.41096 0.03213  0.02498  -0.18233 233 ARG A NH1 
1846 N NH2 . ARG A 233 ? 0.27587 0.60402 0.42307 0.04960  0.01797  -0.16713 233 ARG A NH2 
1847 N N   . LEU A 234 ? 0.23805 0.51770 0.37359 0.02133  0.02731  -0.13486 234 LEU A N   
1848 C CA  . LEU A 234 ? 0.20464 0.47129 0.34033 0.01898  0.02924  -0.11407 234 LEU A CA  
1849 C C   . LEU A 234 ? 0.25345 0.48126 0.39460 0.02489  0.03215  -0.11462 234 LEU A C   
1850 O O   . LEU A 234 ? 0.27443 0.47753 0.41690 0.02479  0.03107  -0.12901 234 LEU A O   
1851 C CB  . LEU A 234 ? 0.12916 0.41494 0.26951 0.00851  0.02875  -0.11354 234 LEU A CB  
1852 C CG  . LEU A 234 ? 0.12154 0.39588 0.26809 0.00592  0.03151  -0.09751 234 LEU A CG  
1853 C CD1 . LEU A 234 ? 0.14313 0.40592 0.27923 0.01204  0.03090  -0.07462 234 LEU A CD1 
1854 C CD2 . LEU A 234 ? 0.18586 0.48464 0.33911 -0.00309 0.02791  -0.09878 234 LEU A CD2 
1855 N N   . PHE A 235 ? 0.19850 0.40789 0.33343 0.02839  0.03346  -0.09620 235 PHE A N   
1856 C CA  . PHE A 235 ? 0.20212 0.36597 0.32951 0.02814  0.03560  -0.08949 235 PHE A CA  
1857 C C   . PHE A 235 ? 0.20307 0.37097 0.33154 0.02040  0.04191  -0.07512 235 PHE A C   
1858 O O   . PHE A 235 ? 0.19441 0.38161 0.32358 0.02300  0.04195  -0.06333 235 PHE A O   
1859 C CB  . PHE A 235 ? 0.26447 0.40044 0.38142 0.03930  0.03144  -0.08303 235 PHE A CB  
1860 C CG  . PHE A 235 ? 0.26154 0.35037 0.36257 0.03723  0.03376  -0.07205 235 PHE A CG  
1861 C CD1 . PHE A 235 ? 0.29727 0.34587 0.38950 0.03552  0.03182  -0.07833 235 PHE A CD1 
1862 C CD2 . PHE A 235 ? 0.31461 0.39670 0.40633 0.03594  0.03814  -0.05586 235 PHE A CD2 
1863 C CE1 . PHE A 235 ? 0.29986 0.30355 0.37123 0.03069  0.03468  -0.06671 235 PHE A CE1 
1864 C CE2 . PHE A 235 ? 0.37691 0.41751 0.44959 0.03221  0.04201  -0.04700 235 PHE A CE2 
1865 C CZ  . PHE A 235 ? 0.31966 0.32140 0.38057 0.02857  0.04050  -0.05148 235 PHE A CZ  
1866 N N   . HIS A 236 ? 0.18514 0.33575 0.31511 0.01044  0.04742  -0.07737 236 HIS A N   
1867 C CA  . HIS A 236 ? 0.20443 0.36131 0.33995 0.00348  0.05542  -0.06736 236 HIS A CA  
1868 C C   . HIS A 236 ? 0.23906 0.35010 0.35836 -0.00139 0.06301  -0.06126 236 HIS A C   
1869 O O   . HIS A 236 ? 0.29495 0.37810 0.40779 -0.01037 0.06475  -0.06830 236 HIS A O   
1870 C CB  . HIS A 236 ? 0.14260 0.33210 0.29782 -0.00793 0.05672  -0.07711 236 HIS A CB  
1871 C CG  . HIS A 236 ? 0.17559 0.38483 0.34544 -0.01235 0.06366  -0.07001 236 HIS A CG  
1872 N ND1 . HIS A 236 ? 0.24576 0.43444 0.40849 -0.01029 0.07268  -0.05887 236 HIS A ND1 
1873 C CD2 . HIS A 236 ? 0.17122 0.41937 0.36301 -0.01789 0.06208  -0.07433 236 HIS A CD2 
1874 C CE1 . HIS A 236 ? 0.22294 0.44027 0.40649 -0.01330 0.07826  -0.05837 236 HIS A CE1 
1875 N NE2 . HIS A 236 ? 0.19138 0.43736 0.38770 -0.01647 0.06850  -0.06432 236 HIS A NE2 
1876 N N   . TYR A 237 ? 0.28586 0.38588 0.39503 0.00346  0.06719  -0.04828 237 TYR A N   
1877 C CA  . TYR A 237 ? 0.26527 0.32351 0.35305 -0.00250 0.07540  -0.04131 237 TYR A CA  
1878 C C   . TYR A 237 ? 0.38976 0.45548 0.48737 -0.01920 0.08935  -0.04417 237 TYR A C   
1879 O O   . TYR A 237 ? 0.29322 0.40154 0.41701 -0.02100 0.09255  -0.04797 237 TYR A O   
1880 C CB  . TYR A 237 ? 0.33743 0.38742 0.41208 0.00624  0.07689  -0.02954 237 TYR A CB  
1881 C CG  . TYR A 237 ? 0.41025 0.41503 0.45458 0.00060  0.08387  -0.02215 237 TYR A CG  
1882 C CD1 . TYR A 237 ? 0.46596 0.42867 0.48487 0.00356  0.07462  -0.01968 237 TYR A CD1 
1883 C CD2 . TYR A 237 ? 0.45015 0.45501 0.48999 -0.00660 0.09885  -0.01817 237 TYR A CD2 
1884 C CE1 . TYR A 237 ? 0.52735 0.44575 0.51195 -0.00211 0.07859  -0.01086 237 TYR A CE1 
1885 C CE2 . TYR A 237 ? 0.56133 0.52431 0.56663 -0.01397 0.10629  -0.01132 237 TYR A CE2 
1886 C CZ  . TYR A 237 ? 0.54704 0.46521 0.52228 -0.01227 0.09508  -0.00633 237 TYR A CZ  
1887 O OH  . TYR A 237 ? 0.61755 0.49044 0.55225 -0.01972 0.09925  0.00255  237 TYR A OH  
1888 N N   . VAL A 238 ? 0.33169 0.35603 0.40756 -0.03199 0.09718  -0.04186 238 VAL A N   
1889 C CA  . VAL A 238 ? 0.44933 0.47848 0.53220 -0.05280 0.11330  -0.04520 238 VAL A CA  
1890 C C   . VAL A 238 ? 0.51407 0.50710 0.56605 -0.06064 0.12631  -0.03456 238 VAL A C   
1891 O O   . VAL A 238 ? 0.58942 0.60383 0.65076 -0.06947 0.14275  -0.03519 238 VAL A O   
1892 C CB  . VAL A 238 ? 0.49593 0.50800 0.57980 -0.06871 0.11174  -0.05497 238 VAL A CB  
1893 C CG1 . VAL A 238 ? 0.49552 0.50390 0.58037 -0.09558 0.13048  -0.05684 238 VAL A CG1 
1894 C CG2 . VAL A 238 ? 0.34440 0.39971 0.45901 -0.06345 0.10087  -0.06862 238 VAL A CG2 
1895 N N   . GLY A 239 ? 0.60788 0.54790 0.62273 -0.05684 0.11858  -0.02582 239 GLY A N   
1896 C CA  . GLY A 239 ? 0.74620 0.64632 0.72240 -0.06489 0.12842  -0.01444 239 GLY A CA  
1897 C C   . GLY A 239 ? 0.80189 0.66656 0.75575 -0.09180 0.14172  -0.01213 239 GLY A C   
1898 O O   . GLY A 239 ? 0.92033 0.79233 0.86828 -0.10929 0.16269  -0.01095 239 GLY A O   
1899 N N   . LYS A 248 ? 1.03102 0.89968 1.05332 -0.23212 0.18610  -0.06085 248 LYS A N   
1900 C CA  . LYS A 248 ? 1.00963 0.95457 1.06885 -0.23148 0.19970  -0.06743 248 LYS A CA  
1901 C C   . LYS A 248 ? 1.00540 1.01078 1.11366 -0.23752 0.19547  -0.08689 248 LYS A C   
1902 O O   . LYS A 248 ? 0.89064 0.88189 1.00593 -0.24535 0.18509  -0.09701 248 LYS A O   
1903 C CB  . LYS A 248 ? 0.91505 0.89322 0.98697 -0.20076 0.19532  -0.06360 248 LYS A CB  
1904 C CG  . LYS A 248 ? 0.96959 0.89180 0.99333 -0.18263 0.18770  -0.04573 248 LYS A CG  
1905 C CD  . LYS A 248 ? 0.99313 0.89055 0.98122 -0.19879 0.20866  -0.03398 248 LYS A CD  
1906 C CE  . LYS A 248 ? 1.05021 0.88906 0.98740 -0.18119 0.19658  -0.01671 248 LYS A CE  
1907 N NZ  . LYS A 248 ? 0.84060 0.70073 0.77133 -0.16840 0.20560  -0.01243 248 LYS A NZ  
1908 N N   . ASP A 249 ? 0.98310 1.03931 1.22243 -0.03597 0.38071  0.06077  249 ASP A N   
1909 C CA  . ASP A 249 ? 0.83267 0.99452 1.16525 -0.04466 0.37093  0.02651  249 ASP A CA  
1910 C C   . ASP A 249 ? 0.71615 0.90375 1.03174 -0.01660 0.33427  -0.00499 249 ASP A C   
1911 O O   . ASP A 249 ? 0.60476 0.86618 0.99023 -0.02569 0.31261  -0.03664 249 ASP A O   
1912 C CB  . ASP A 249 ? 0.70827 0.94279 1.05586 -0.03344 0.39517  0.03495  249 ASP A CB  
1913 C CG  . ASP A 249 ? 0.91415 1.12355 1.26279 -0.05804 0.43158  0.06892  249 ASP A CG  
1914 O OD1 . ASP A 249 ? 0.97502 1.09258 1.24224 -0.05009 0.44509  0.09938  249 ASP A OD1 
1915 O OD2 . ASP A 249 ? 0.92913 1.21035 1.35444 -0.08477 0.44420  0.06615  249 ASP A OD2 
1916 N N   . LEU A 250 ? 0.61579 0.73776 0.82549 0.01750  0.31526  0.00394  250 LEU A N   
1917 C CA  . LEU A 250 ? 0.65999 0.79357 0.84369 0.03975  0.27579  -0.02192 250 LEU A CA  
1918 C C   . LEU A 250 ? 0.51117 0.60929 0.70430 0.01740  0.24071  -0.03704 250 LEU A C   
1919 O O   . LEU A 250 ? 0.50385 0.64186 0.72234 0.01828  0.21364  -0.06560 250 LEU A O   
1920 C CB  . LEU A 250 ? 0.66717 0.74609 0.73583 0.08343  0.26947  -0.00835 250 LEU A CB  
1921 C CG  . LEU A 250 ? 0.52889 0.50356 0.49783 0.08988  0.24533  0.00658  250 LEU A CG  
1922 C CD1 . LEU A 250 ? 0.67457 0.60727 0.53994 0.13310  0.24207  0.01400  250 LEU A CD1 
1923 C CD2 . LEU A 250 ? 0.60616 0.52210 0.56037 0.07005  0.26194  0.03368  250 LEU A CD2 
1924 N N   . GLN A 251 ? 0.59086 0.61732 0.76278 0.00032  0.24169  -0.01798 251 GLN A N   
1925 C CA  . GLN A 251 ? 0.53958 0.53918 0.73319 -0.01934 0.21345  -0.03253 251 GLN A CA  
1926 C C   . GLN A 251 ? 0.45260 0.52015 0.74483 -0.04374 0.20728  -0.06701 251 GLN A C   
1927 O O   . GLN A 251 ? 0.32805 0.40869 0.63264 -0.04599 0.17900  -0.09368 251 GLN A O   
1928 C CB  . GLN A 251 ? 0.66048 0.58701 0.84101 -0.03435 0.22234  -0.00629 251 GLN A CB  
1929 C CG  . GLN A 251 ? 0.65223 0.54520 0.83977 -0.04273 0.19142  -0.01863 251 GLN A CG  
1930 C CD  . GLN A 251 ? 0.66768 0.49595 0.86045 -0.05660 0.19876  0.00359  251 GLN A CD  
1931 O OE1 . GLN A 251 ? 0.74102 0.50467 0.86563 -0.04314 0.19168  0.03036  251 GLN A OE1 
1932 N NE2 . GLN A 251 ? 0.72113 0.56196 0.99322 -0.08370 0.21030  -0.00790 251 GLN A NE2 
1933 N N   . LYS A 252 ? 0.46605 0.57297 0.82849 -0.06552 0.23471  -0.06604 252 LYS A N   
1934 C CA  . LYS A 252 ? 0.38433 0.57421 0.84236 -0.08679 0.23203  -0.09965 252 LYS A CA  
1935 C C   . LYS A 252 ? 0.38289 0.63362 0.83842 -0.06584 0.20293  -0.13145 252 LYS A C   
1936 O O   . LYS A 252 ? 0.35296 0.60640 0.82024 -0.07311 0.17291  -0.15943 252 LYS A O   
1937 C CB  . LYS A 252 ? 0.53033 0.77555 1.04983 -0.09977 0.26081  -0.00456 252 LYS A CB  
1938 C CG  . LYS A 252 ? 0.58129 0.80856 1.16566 -0.13885 0.27078  0.01420  252 LYS A CG  
1939 C CD  . LYS A 252 ? 0.54235 0.73828 1.17342 -0.16176 0.23411  -0.01999 252 LYS A CD  
1940 C CE  . LYS A 252 ? 0.47837 0.74379 1.15748 -0.16447 0.20319  -0.06433 252 LYS A CE  
1941 N NZ  . LYS A 252 ? 0.49966 0.81932 1.23904 -0.18704 0.21332  -0.05058 252 LYS A NZ  
1942 N N   . GLY A 253 ? 0.39587 0.68924 0.82530 -0.03671 0.20901  -0.12451 253 GLY A N   
1943 C CA  . GLY A 253 ? 0.28328 0.62445 0.69643 -0.01256 0.17799  -0.14689 253 GLY A CA  
1944 C C   . GLY A 253 ? 0.26523 0.56271 0.61710 0.00049  0.15298  -0.15585 253 GLY A C   
1945 O O   . GLY A 253 ? 0.24595 0.57350 0.60374 0.00156  0.12466  -0.18179 253 GLY A O   
1946 N N   . VAL A 254 ? 0.29340 0.50746 0.56858 0.00908  0.15612  -0.12781 254 VAL A N   
1947 C CA  . VAL A 254 ? 0.36283 0.53005 0.57541 0.01590  0.12898  -0.12959 254 VAL A CA  
1948 C C   . VAL A 254 ? 0.29646 0.47750 0.56103 -0.00960 0.11378  -0.15625 254 VAL A C   
1949 O O   . VAL A 254 ? 0.30707 0.51353 0.56305 -0.00527 0.09198  -0.17802 254 VAL A O   
1950 C CB  . VAL A 254 ? 0.38044 0.46012 0.51663 0.02220  0.13220  -0.09738 254 VAL A CB  
1951 C CG1 . VAL A 254 ? 0.32391 0.36868 0.42890 0.01530  0.10620  -0.10202 254 VAL A CG1 
1952 C CG2 . VAL A 254 ? 0.40202 0.45655 0.46008 0.05493  0.13717  -0.07846 254 VAL A CG2 
1953 N N   . MET A 255 ? 0.28475 0.44545 0.59935 -0.03455 0.12614  -0.15489 255 MET A N   
1954 C CA  . MET A 255 ? 0.37332 0.54379 0.73933 -0.05487 0.11273  -0.18476 255 MET A CA  
1955 C C   . MET A 255 ? 0.30312 0.54739 0.71693 -0.05965 0.09987  -0.22165 255 MET A C   
1956 O O   . MET A 255 ? 0.34192 0.59697 0.74202 -0.05655 0.07770  -0.24628 255 MET A O   
1957 C CB  . MET A 255 ? 0.31555 0.44043 0.72347 -0.07803 0.12833  -0.17464 255 MET A CB  
1958 C CG  . MET A 255 ? 0.42164 0.47096 0.77722 -0.07036 0.12316  -0.14968 255 MET A CG  
1959 S SD  . MET A 255 ? 0.32952 0.30684 0.71427 -0.08788 0.13524  -0.13182 255 MET A SD  
1960 C CE  . MET A 255 ? 0.39497 0.40374 0.85656 -0.11685 0.16069  -0.13885 255 MET A CE  
1961 N N   . GLU A 256 ? 0.24756 0.52926 0.68951 -0.06198 0.10848  -0.21853 256 GLU A N   
1962 C CA  . GLU A 256 ? 0.25964 0.59431 0.72675 -0.06421 0.08898  -0.24665 256 GLU A CA  
1963 C C   . GLU A 256 ? 0.24382 0.61163 0.66275 -0.03800 0.06581  -0.25881 256 GLU A C   
1964 O O   . GLU A 256 ? 0.23832 0.62454 0.65395 -0.03843 0.04467  -0.28844 256 GLU A O   
1965 C CB  . GLU A 256 ? 0.26705 0.64400 0.77814 -0.07057 0.10431  -0.23586 256 GLU A CB  
1966 C CG  . GLU A 256 ? 0.29790 0.67710 0.87239 -0.10210 0.10913  -0.24734 256 GLU A CG  
1967 C CD  . GLU A 256 ? 0.39922 0.82351 1.01710 -0.11044 0.13092  -0.22750 256 GLU A CD  
1968 O OE1 . GLU A 256 ? 0.42662 0.90126 1.03118 -0.08515 0.13219  -0.21812 256 GLU A OE1 
1969 O OE2 . GLU A 256 ? 0.55097 0.96110 1.21493 -0.14020 0.14754  -0.22004 256 GLU A OE2 
1970 N N   . ARG A 257 ? 0.22771 0.59826 0.60163 -0.01124 0.07166  -0.23605 257 ARG A N   
1971 C CA  . ARG A 257 ? 0.22695 0.62071 0.54764 0.01745  0.05051  -0.24260 257 ARG A CA  
1972 C C   . ARG A 257 ? 0.26227 0.62880 0.54085 0.01659  0.03685  -0.25244 257 ARG A C   
1973 O O   . ARG A 257 ? 0.29777 0.69209 0.54617 0.02994  0.01627  -0.26854 257 ARG A O   
1974 C CB  . ARG A 257 ? 0.25571 0.63348 0.52183 0.05106  0.06199  -0.21426 257 ARG A CB  
1975 C CG  . ARG A 257 ? 0.31219 0.73946 0.60118 0.06928  0.06636  -0.20926 257 ARG A CG  
1976 C CD  . ARG A 257 ? 0.28242 0.67060 0.50946 0.10262  0.08449  -0.17964 257 ARG A CD  
1977 N NE  . ARG A 257 ? 0.40261 0.79605 0.67083 0.09327  0.11813  -0.16277 257 ARG A NE  
1978 C CZ  . ARG A 257 ? 0.32284 0.66009 0.55498 0.09526  0.14398  -0.14183 257 ARG A CZ  
1979 N NH1 . ARG A 257 ? 0.32008 0.57151 0.46362 0.10234  0.13167  -0.12666 257 ARG A NH1 
1980 N NH2 . ARG A 257 ? 0.40619 0.75644 0.67828 0.08481  0.17750  -0.12657 257 ARG A NH2 
1981 N N   . LEU A 258 ? 0.28770 0.60358 0.56269 0.00280  0.04899  -0.24220 258 LEU A N   
1982 C CA  . LEU A 258 ? 0.20762 0.49749 0.44159 0.00002  0.03666  -0.24660 258 LEU A CA  
1983 C C   . LEU A 258 ? 0.27560 0.60395 0.55146 -0.01403 0.02400  -0.28563 258 LEU A C   
1984 O O   . LEU A 258 ? 0.25055 0.59795 0.49429 -0.00770 0.00985  -0.29561 258 LEU A O   
1985 C CB  . LEU A 258 ? 0.26323 0.48659 0.48080 -0.01040 0.04681  -0.22196 258 LEU A CB  
1986 C CG  . LEU A 258 ? 0.23232 0.39812 0.37611 0.00306  0.04959  -0.18388 258 LEU A CG  
1987 C CD1 . LEU A 258 ? 0.30360 0.41422 0.43856 -0.00894 0.05218  -0.16599 258 LEU A CD1 
1988 C CD2 . LEU A 258 ? 0.29122 0.45209 0.36238 0.01855  0.03430  -0.17776 258 LEU A CD2 
1989 N N   . ARG A 259 ? 0.22795 0.55037 0.55758 -0.03084 0.03002  -0.29976 259 ARG A N   
1990 C CA  . ARG A 259 ? 0.31235 0.65096 0.66036 -0.03192 0.02420  -0.33272 259 ARG A CA  
1991 C C   . ARG A 259 ? 0.24400 0.63934 0.57989 -0.01816 0.00825  -0.35237 259 ARG A C   
1992 O O   . ARG A 259 ? 0.35197 0.77502 0.67239 -0.00591 0.00158  -0.36691 259 ARG A O   
1993 C CB  . ARG A 259 ? 0.27838 0.59549 0.68512 -0.04947 0.03467  -0.33889 259 ARG A CB  
1994 C CG  . ARG A 259 ? 0.30144 0.56389 0.72177 -0.05980 0.05025  -0.31407 259 ARG A CG  
1995 C CD  . ARG A 259 ? 0.31720 0.55569 0.79130 -0.07493 0.05844  -0.32143 259 ARG A CD  
1996 N NE  . ARG A 259 ? 0.39075 0.57485 0.87029 -0.07943 0.07009  -0.29717 259 ARG A NE  
1997 C CZ  . ARG A 259 ? 0.34431 0.49455 0.84925 -0.09509 0.08525  -0.27456 259 ARG A CZ  
1998 N NH1 . ARG A 259 ? 0.34556 0.51614 0.88153 -0.11060 0.09331  -0.27328 259 ARG A NH1 
1999 N NH2 . ARG A 259 ? 0.37033 0.46740 0.86741 -0.09505 0.09263  -0.24983 259 ARG A NH2 
2000 N N   . ARG A 260 ? 0.25972 0.68236 0.61135 -0.01704 0.00388  -0.34625 260 ARG A N   
2001 C CA  . ARG A 260 ? 0.32100 0.80122 0.66201 0.00084  -0.01463 -0.36300 260 ARG A CA  
2002 C C   . ARG A 260 ? 0.29036 0.78659 0.56754 0.02635  -0.02644 -0.36266 260 ARG A C   
2003 O O   . ARG A 260 ? 0.33610 0.86670 0.60422 0.03961  -0.03780 -0.37783 260 ARG A O   
2004 C CB  . ARG A 260 ? 0.30026 0.80963 0.66120 0.00786  -0.01357 -0.34419 260 ARG A CB  
2005 C CG  . ARG A 260 ? 0.28860 0.86085 0.66716 0.02028  -0.03161 -0.36410 260 ARG A CG  
2006 C CD  . ARG A 260 ? 0.29825 0.89999 0.74514 0.00628  -0.02116 -0.35635 260 ARG A CD  
2007 N NE  . ARG A 260 ? 0.37355 0.97823 0.81180 0.02372  -0.00633 -0.32159 260 ARG A NE  
2008 C CZ  . ARG A 260 ? 0.29353 0.87927 0.76584 0.00886  0.02165  -0.29619 260 ARG A CZ  
2009 N NH1 . ARG A 260 ? 0.33702 0.90136 0.85879 -0.02620 0.03496  -0.30030 260 ARG A NH1 
2010 N NH2 . ARG A 260 ? 0.27734 0.86199 0.72790 0.03326  0.03810  -0.26581 260 ARG A NH2 
2011 N N   . VAL A 261 ? 0.30685 0.77848 0.54506 0.03245  -0.02306 -0.33762 261 VAL A N   
2012 C CA  . VAL A 261 ? 0.25585 0.71253 0.42437 0.04986  -0.03444 -0.30770 261 VAL A CA  
2013 C C   . VAL A 261 ? 0.39895 0.83818 0.55603 0.03820  -0.03092 -0.30443 261 VAL A C   
2014 O O   . VAL A 261 ? 0.37037 0.80104 0.47137 0.04879  -0.03854 -0.29004 261 VAL A O   
2015 C CB  . VAL A 261 ? 0.41063 0.80306 0.52201 0.05621  -0.02477 -0.27093 261 VAL A CB  
2016 C CG1 . VAL A 261 ? 0.37485 0.70662 0.42700 0.04785  -0.02076 -0.24046 261 VAL A CG1 
2017 C CG2 . VAL A 261 ? 0.29169 0.69412 0.36525 0.08957  -0.03274 -0.26039 261 VAL A CG2 
2018 N N   . GLY A 262 ? 0.28639 0.71894 0.49368 0.01874  -0.01805 -0.31859 262 GLY A N   
2019 C CA  . GLY A 262 ? 0.29404 0.72245 0.49632 0.01269  -0.01508 -0.32193 262 GLY A CA  
2020 C C   . GLY A 262 ? 0.24648 0.64051 0.47063 -0.00286 -0.00111 -0.31536 262 GLY A C   
2021 O O   . GLY A 262 ? 0.24251 0.64407 0.48607 -0.00679 0.00247  -0.32944 262 GLY A O   
2022 N N   . PHE A 263 ? 0.21849 0.57520 0.43925 -0.00921 0.00545  -0.29649 263 PHE A N   
2023 C CA  . PHE A 263 ? 0.27015 0.59025 0.50292 -0.01990 0.01600  -0.28684 263 PHE A CA  
2024 C C   . PHE A 263 ? 0.28859 0.60689 0.58512 -0.02515 0.02442  -0.30877 263 PHE A C   
2025 O O   . PHE A 263 ? 0.24333 0.56850 0.57024 -0.02510 0.02583  -0.32722 263 PHE A O   
2026 C CB  . PHE A 263 ? 0.26297 0.53540 0.47322 -0.02277 0.02100  -0.26338 263 PHE A CB  
2027 C CG  . PHE A 263 ? 0.33681 0.58570 0.46983 -0.01467 0.01643  -0.23665 263 PHE A CG  
2028 C CD1 . PHE A 263 ? 0.28990 0.52269 0.39065 -0.02055 0.01760  -0.22362 263 PHE A CD1 
2029 C CD2 . PHE A 263 ? 0.32384 0.56767 0.41787 -0.00049 0.01155  -0.22608 263 PHE A CD2 
2030 C CE1 . PHE A 263 ? 0.37039 0.57350 0.39821 -0.01831 0.01306  -0.19846 263 PHE A CE1 
2031 C CE2 . PHE A 263 ? 0.27515 0.48314 0.29217 0.00844  0.00644  -0.19895 263 PHE A CE2 
2032 C CZ  . PHE A 263 ? 0.36407 0.54736 0.34645 -0.00332 0.00663  -0.18435 263 PHE A CZ  
2033 N N   . VAL A 264 ? 0.23252 0.53217 0.54104 -0.02845 0.02899  -0.30626 264 VAL A N   
2034 C CA  . VAL A 264 ? 0.29167 0.57449 0.65140 -0.03023 0.03437  -0.32141 264 VAL A CA  
2035 C C   . VAL A 264 ? 0.29065 0.53293 0.65967 -0.03235 0.03980  -0.30334 264 VAL A C   
2036 O O   . VAL A 264 ? 0.28977 0.51701 0.62053 -0.03316 0.03879  -0.28232 264 VAL A O   
2037 C CB  . VAL A 264 ? 0.30391 0.62329 0.68164 -0.02662 0.02903  -0.34902 264 VAL A CB  
2038 C CG1 . VAL A 264 ? 0.25020 0.61085 0.62778 -0.02236 0.02266  -0.37119 264 VAL A CG1 
2039 C CG2 . VAL A 264 ? 0.23168 0.56886 0.57761 -0.02607 0.02640  -0.34344 264 VAL A CG2 
2040 N N   . GLY A 265 ? 0.28355 0.49940 0.69574 -0.03279 0.04236  -0.30996 265 GLY A N   
2041 C CA  . GLY A 265 ? 0.27629 0.44416 0.69304 -0.03217 0.04339  -0.28888 265 GLY A CA  
2042 C C   . GLY A 265 ? 0.33065 0.45727 0.72139 -0.03818 0.04752  -0.25894 265 GLY A C   
2043 O O   . GLY A 265 ? 0.33987 0.43071 0.71192 -0.03670 0.04460  -0.23673 265 GLY A O   
2044 N N   . VAL A 266 ? 0.25383 0.38679 0.64429 -0.04494 0.05314  -0.26022 266 VAL A N   
2045 C CA  . VAL A 266 ? 0.31652 0.41901 0.68590 -0.05240 0.05931  -0.23629 266 VAL A CA  
2046 C C   . VAL A 266 ? 0.26251 0.30935 0.65526 -0.05913 0.06884  -0.21579 266 VAL A C   
2047 O O   . VAL A 266 ? 0.33026 0.37516 0.76220 -0.06685 0.07558  -0.22489 266 VAL A O   
2048 C CB  . VAL A 266 ? 0.34206 0.48322 0.71481 -0.05684 0.06234  -0.24976 266 VAL A CB  
2049 C CG1 . VAL A 266 ? 0.35260 0.47409 0.69943 -0.05770 0.07236  -0.21923 266 VAL A CG1 
2050 C CG2 . VAL A 266 ? 0.28716 0.47836 0.62811 -0.04613 0.05054  -0.26748 266 VAL A CG2 
2051 N N   . ARG A 267 ? 0.36912 0.36520 0.73054 -0.05574 0.06831  -0.18612 267 ARG A N   
2052 C CA  . ARG A 267 ? 0.34043 0.27717 0.70734 -0.05851 0.07696  -0.15907 267 ARG A CA  
2053 C C   . ARG A 267 ? 0.36435 0.25061 0.67345 -0.05165 0.07808  -0.12109 267 ARG A C   
2054 O O   . ARG A 267 ? 0.42707 0.32212 0.69066 -0.04153 0.06404  -0.11344 267 ARG A O   
2055 C CB  . ARG A 267 ? 0.36311 0.28264 0.75396 -0.05021 0.06672  -0.16370 267 ARG A CB  
2056 C CG  . ARG A 267 ? 0.40622 0.31834 0.77822 -0.03466 0.04982  -0.15828 267 ARG A CG  
2057 C CD  . ARG A 267 ? 0.43204 0.33954 0.84087 -0.02362 0.04125  -0.17254 267 ARG A CD  
2058 N NE  . ARG A 267 ? 0.56781 0.53075 1.01198 -0.02277 0.04046  -0.21164 267 ARG A NE  
2059 C CZ  . ARG A 267 ? 0.62220 0.63543 1.06912 -0.01581 0.03430  -0.23272 267 ARG A CZ  
2060 N NH1 . ARG A 267 ? 0.43825 0.45602 0.86054 -0.01204 0.02778  -0.22162 267 ARG A NH1 
2061 N NH2 . ARG A 267 ? 0.54958 0.60732 1.02238 -0.01402 0.03451  -0.26619 267 ARG A NH2 
2062 N N   . ARG A 268 ? 0.44830 0.28540 0.74876 -0.05630 0.09420  -0.09265 268 ARG A N   
2063 C CA  . ARG A 268 ? 0.50452 0.28598 0.73805 -0.04405 0.09191  -0.05231 268 ARG A CA  
2064 C C   . ARG A 268 ? 0.51176 0.26767 0.73197 -0.03049 0.06567  -0.04715 268 ARG A C   
2065 O O   . ARG A 268 ? 0.55643 0.31808 0.81595 -0.02758 0.05593  -0.06070 268 ARG A O   
2066 C CB  . ARG A 268 ? 0.53947 0.25029 0.80797 -0.05367 0.09826  -0.02566 268 ARG A CB  
2067 C CG  . ARG A 268 ? 0.69514 0.36914 0.86648 -0.04572 0.10800  0.02157  268 ARG A CG  
2068 C CD  . ARG A 268 ? 0.73811 0.36594 0.89179 -0.05947 0.13790  0.06508  268 ARG A CD  
2069 N NE  . ARG A 268 ? 0.84019 0.45728 1.07223 -0.08036 0.14564  0.06190  268 ARG A NE  
2070 C CZ  . ARG A 268 ? 0.79149 0.42717 1.05864 -0.10364 0.17817  0.06941  268 ARG A CZ  
2071 N NH1 . ARG A 268 ? 0.87442 0.53541 1.10668 -0.10633 0.21176  0.08641  268 ARG A NH1 
2072 N NH2 . ARG A 268 ? 0.70099 0.33587 1.03462 -0.12229 0.17538  0.05877  268 ARG A NH2 
2073 N N   . VAL A 269 ? 0.56567 0.30448 0.71997 -0.01979 0.05106  -0.02561 269 VAL A N   
2074 C CA  . VAL A 269 ? 0.67005 0.37284 0.79929 -0.00694 0.02583  -0.00790 269 VAL A CA  
2075 C C   . VAL A 269 ? 0.67572 0.31169 0.73295 0.00059  0.03079  0.03093  269 VAL A C   
2076 O O   . VAL A 269 ? 0.67229 0.30099 0.66651 0.00278  0.03371  0.04236  269 VAL A O   
2077 C CB  . VAL A 269 ? 0.64466 0.38451 0.75621 -0.00544 0.00061  -0.01697 269 VAL A CB  
2078 C CG1 . VAL A 269 ? 0.74346 0.46644 0.85802 0.00632  -0.02826 -0.00611 269 VAL A CG1 
2079 C CG2 . VAL A 269 ? 0.62620 0.43611 0.78966 -0.01407 0.00466  -0.05278 269 VAL A CG2 
2080 N N   . GLU A 270 ? 0.79628 0.38957 0.84913 0.00666  0.02834  0.04927  270 GLU A N   
2081 C CA  . GLU A 270 ? 0.90616 0.45408 0.89493 0.01121  0.03285  0.08366  270 GLU A CA  
2082 C C   . GLU A 270 ? 0.79262 0.32926 0.72291 0.02513  0.00868  0.10162  270 GLU A C   
2083 O O   . GLU A 270 ? 0.86576 0.39572 0.73354 0.02787  0.01814  0.11434  270 GLU A O   
2084 C CB  . GLU A 270 ? 0.94709 0.45706 0.94750 0.01224  0.03143  0.09694  270 GLU A CB  
2085 C CG  . GLU A 270 ? 1.03317 0.51787 1.00548 0.00417  0.05870  0.12405  270 GLU A CG  
2086 C CD  . GLU A 270 ? 1.18358 0.63128 1.09575 0.01840  0.04272  0.15757  270 GLU A CD  
2087 O OE1 . GLU A 270 ? 1.24612 0.66575 1.12908 0.01365  0.06503  0.18166  270 GLU A OE1 
2088 O OE2 . GLU A 270 ? 1.26366 0.71702 1.16449 0.03404  0.01344  0.15991  270 GLU A OE2 
2089 N N   . GLU A 271 ? 0.88711 0.42592 0.82902 0.03554  -0.01715 0.09749  271 GLU A N   
2090 C CA  . GLU A 271 ? 0.91747 0.44929 0.79714 0.04480  -0.04632 0.10877  271 GLU A CA  
2091 C C   . GLU A 271 ? 0.95355 0.49846 0.78152 0.03675  -0.04995 0.10037  271 GLU A C   
2092 O O   . GLU A 271 ? 0.99223 0.52111 0.75330 0.04175  -0.05806 0.11033  271 GLU A O   
2093 C CB  . GLU A 271 ? 0.96009 0.50257 0.87169 0.05256  -0.08445 0.09964  271 GLU A CB  
2094 C CG  . GLU A 271 ? 1.16222 0.70497 1.14502 0.06197  -0.08035 0.09211  271 GLU A CG  
2095 C CD  . GLU A 271 ? 1.13014 0.71595 1.19184 0.05010  -0.06834 0.05891  271 GLU A CD  
2096 O OE1 . GLU A 271 ? 1.04212 0.62924 1.10666 0.03605  -0.03579 0.05197  271 GLU A OE1 
2097 O OE2 . GLU A 271 ? 1.13875 0.77120 1.26416 0.05528  -0.08838 0.03698  271 GLU A OE2 
2098 N N   . ALA A 272 ? 0.81888 0.38884 0.67358 0.02517  -0.04476 0.07928  272 ALA A N   
2099 C CA  . ALA A 272 ? 0.68108 0.25842 0.48642 0.01888  -0.04979 0.07153  272 ALA A CA  
2100 C C   . ALA A 272 ? 0.71111 0.28789 0.49161 0.02124  -0.01556 0.07127  272 ALA A C   
2101 O O   . ALA A 272 ? 0.66771 0.24818 0.40907 0.02048  -0.01665 0.06294  272 ALA A O   
2102 C CB  . ALA A 272 ? 0.66161 0.28232 0.51167 0.00427  -0.06554 0.04869  272 ALA A CB  
2103 N N   . LEU A 273 ? 0.69174 0.26151 0.49397 0.02408  0.01364  0.08089  273 LEU A N   
2104 C CA  . LEU A 273 ? 0.71399 0.28306 0.49822 0.02715  0.05010  0.08352  273 LEU A CA  
2105 C C   . LEU A 273 ? 0.62242 0.23123 0.42787 0.02260  0.05742  0.05955  273 LEU A C   
2106 O O   . LEU A 273 ? 0.65938 0.26347 0.41074 0.03311  0.06046  0.05833  273 LEU A O   
2107 C CB  . LEU A 273 ? 0.69850 0.24435 0.40156 0.04186  0.05311  0.09777  273 LEU A CB  
2108 C CG  . LEU A 273 ? 0.81235 0.33356 0.49584 0.04612  0.04102  0.11633  273 LEU A CG  
2109 C CD1 . LEU A 273 ? 0.89004 0.38559 0.49105 0.06101  0.04361  0.12189  273 LEU A CD1 
2110 C CD2 . LEU A 273 ? 0.90452 0.41841 0.63398 0.03945  0.06531  0.13154  273 LEU A CD2 
2111 N N   . GLY A 274 ? 0.55789 0.22017 0.44794 0.00868  0.05699  0.03643  274 GLY A N   
2112 C CA  . GLY A 274 ? 0.50115 0.22061 0.41732 0.00437  0.05842  0.01080  274 GLY A CA  
2113 C C   . GLY A 274 ? 0.56404 0.33802 0.57251 -0.00947 0.06389  -0.01527 274 GLY A C   
2114 O O   . GLY A 274 ? 0.49891 0.26200 0.55332 -0.01577 0.07144  -0.01359 274 GLY A O   
2115 N N   . VAL A 275 ? 0.48122 0.30704 0.50891 -0.01283 0.05864  -0.03963 275 VAL A N   
2116 C CA  . VAL A 275 ? 0.42101 0.30260 0.52527 -0.02349 0.06251  -0.07048 275 VAL A CA  
2117 C C   . VAL A 275 ? 0.35877 0.27026 0.46298 -0.02640 0.04234  -0.08686 275 VAL A C   
2118 O O   . VAL A 275 ? 0.36446 0.27074 0.41356 -0.02323 0.03143  -0.07914 275 VAL A O   
2119 C CB  . VAL A 275 ? 0.39613 0.32317 0.52396 -0.02349 0.07992  -0.08540 275 VAL A CB  
2120 C CG1 . VAL A 275 ? 0.35365 0.33990 0.54547 -0.03332 0.07583  -0.12240 275 VAL A CG1 
2121 C CG2 . VAL A 275 ? 0.40876 0.31901 0.55735 -0.02730 0.10551  -0.07023 275 VAL A CG2 
2122 N N   . VAL A 276 ? 0.38452 0.32245 0.54684 -0.03230 0.03850  -0.10809 276 VAL A N   
2123 C CA  . VAL A 276 ? 0.33820 0.31791 0.50721 -0.03539 0.02646  -0.12583 276 VAL A CA  
2124 C C   . VAL A 276 ? 0.32010 0.35410 0.52811 -0.03799 0.03482  -0.16011 276 VAL A C   
2125 O O   . VAL A 276 ? 0.33721 0.37632 0.58490 -0.04047 0.04574  -0.17364 276 VAL A O   
2126 C CB  . VAL A 276 ? 0.33114 0.31214 0.53376 -0.03446 0.01514  -0.12828 276 VAL A CB  
2127 C CG1 . VAL A 276 ? 0.37628 0.31973 0.53401 -0.03378 -0.00213 -0.09803 276 VAL A CG1 
2128 C CG2 . VAL A 276 ? 0.40886 0.37322 0.66954 -0.02984 0.02230  -0.13933 276 VAL A CG2 
2129 N N   . ALA A 277 ? 0.30849 0.38314 0.50257 -0.03947 0.02896  -0.17378 277 ALA A N   
2130 C CA  . ALA A 277 ? 0.30728 0.43445 0.52794 -0.03945 0.03310  -0.20836 277 ALA A CA  
2131 C C   . ALA A 277 ? 0.23237 0.39789 0.44384 -0.04113 0.02931  -0.22018 277 ALA A C   
2132 O O   . ALA A 277 ? 0.32592 0.48073 0.50396 -0.04598 0.02366  -0.19760 277 ALA A O   
2133 C CB  . ALA A 277 ? 0.25524 0.39544 0.44439 -0.03490 0.03418  -0.20768 277 ALA A CB  
2134 N N   A ARG A 278 ? 0.24612 0.45827 0.48435 -0.03735 0.03325  -0.24972 278 ARG A N   
2135 N N   B ARG A 278 ? 0.24615 0.45769 0.48699 -0.03725 0.03341  -0.25017 278 ARG A N   
2136 C CA  A ARG A 278 ? 0.32277 0.57752 0.55069 -0.03838 0.03499  -0.26150 278 ARG A CA  
2137 C CA  B ARG A 278 ? 0.32155 0.57846 0.55412 -0.03761 0.03512  -0.26356 278 ARG A CA  
2138 C C   A ARG A 278 ? 0.31899 0.61149 0.52746 -0.03497 0.03228  -0.26956 278 ARG A C   
2139 C C   B ARG A 278 ? 0.31983 0.60899 0.52312 -0.03469 0.03163  -0.26692 278 ARG A C   
2140 O O   A ARG A 278 ? 0.29585 0.59942 0.53453 -0.03096 0.02894  -0.28400 278 ARG A O   
2141 O O   B ARG A 278 ? 0.30043 0.59634 0.52384 -0.03045 0.02779  -0.27616 278 ARG A O   
2142 C CB  A ARG A 278 ? 0.29537 0.56446 0.57915 -0.03503 0.03748  -0.28277 278 ARG A CB  
2143 C CB  B ARG A 278 ? 0.28710 0.56295 0.57663 -0.03435 0.03615  -0.28838 278 ARG A CB  
2144 C CG  A ARG A 278 ? 0.26993 0.57327 0.57182 -0.03226 0.03465  -0.30824 278 ARG A CG  
2145 C CG  B ARG A 278 ? 0.30138 0.60464 0.58253 -0.03396 0.04105  -0.29251 278 ARG A CG  
2146 C CD  A ARG A 278 ? 0.32493 0.61720 0.67340 -0.02447 0.03444  -0.32425 278 ARG A CD  
2147 C CD  B ARG A 278 ? 0.26683 0.57621 0.59264 -0.02373 0.04049  -0.31338 278 ARG A CD  
2148 N NE  A ARG A 278 ? 0.30886 0.59106 0.70032 -0.02158 0.03111  -0.34047 278 ARG A NE  
2149 N NE  B ARG A 278 ? 0.36420 0.68112 0.71209 -0.02111 0.03538  -0.33826 278 ARG A NE  
2150 C CZ  A ARG A 278 ? 0.28629 0.52772 0.71728 -0.01731 0.03122  -0.33615 278 ARG A CZ  
2151 C CZ  B ARG A 278 ? 0.30878 0.66320 0.63636 -0.02124 0.03485  -0.35212 278 ARG A CZ  
2152 N NH1 A ARG A 278 ? 0.27463 0.48092 0.70910 -0.01389 0.03154  -0.31480 278 ARG A NH1 
2153 N NH1 B ARG A 278 ? 0.35325 0.73707 0.63265 -0.02509 0.03951  -0.34166 278 ARG A NH1 
2154 N NH2 A ARG A 278 ? 0.27314 0.50454 0.73703 -0.01516 0.03066  -0.35236 278 ARG A NH2 
2155 N NH2 B ARG A 278 ? 0.27518 0.63651 0.63102 -0.01603 0.03045  -0.37589 278 ARG A NH2 
2156 N N   . LYS A 279 ? 0.26914 0.57758 0.42466 -0.03766 0.03298  -0.25908 279 LYS A N   
2157 C CA  . LYS A 279 ? 0.33827 0.67407 0.46715 -0.03107 0.02849  -0.26308 279 LYS A CA  
2158 C C   . LYS A 279 ? 0.35023 0.72756 0.50737 -0.02951 0.03188  -0.28964 279 LYS A C   
2159 O O   . LYS A 279 ? 0.35369 0.74479 0.52070 -0.03494 0.04047  -0.29494 279 LYS A O   
2160 C CB  . LYS A 279 ? 0.35968 0.68275 0.41300 -0.03391 0.02836  -0.23653 279 LYS A CB  
2161 C CG  . LYS A 279 ? 0.38034 0.73033 0.39999 -0.02748 0.02747  -0.23978 279 LYS A CG  
2162 C CD  . LYS A 279 ? 0.43671 0.75272 0.37587 -0.02798 0.02442  -0.20792 279 LYS A CD  
2163 C CE  . LYS A 279 ? 0.38330 0.70786 0.28598 -0.01289 0.01688  -0.20977 279 LYS A CE  
2164 N NZ  . LYS A 279 ? 0.43205 0.70653 0.25374 -0.00908 0.01074  -0.17773 279 LYS A NZ  
2165 N N   . PRO A 280 ? 0.36192 0.76114 0.53281 -0.02108 0.02506  -0.30965 280 PRO A N   
2166 C CA  . PRO A 280 ? 0.44351 0.87136 0.64324 -0.01747 0.02687  -0.33945 280 PRO A CA  
2167 C C   . PRO A 280 ? 0.54423 1.00198 0.69933 -0.01472 0.03488  -0.34027 280 PRO A C   
2168 O O   . PRO A 280 ? 0.47814 0.93405 0.58839 -0.02138 0.04321  -0.31573 280 PRO A O   
2169 C CB  . PRO A 280 ? 0.42478 0.86283 0.65199 -0.01046 0.01659  -0.36182 280 PRO A CB  
2170 C CG  . PRO A 280 ? 0.31585 0.74866 0.51072 -0.00710 0.00969  -0.34362 280 PRO A CG  
2171 C CD  . PRO A 280 ? 0.37930 0.77782 0.54988 -0.01379 0.01481  -0.31125 280 PRO A CD  
2172 N N   . GLU A 281 ? 0.90132 1.38468 1.06682 -0.00553 0.03440  -0.36893 281 GLU A N   
2173 C CA  . GLU A 281 ? 0.91564 1.42890 1.03520 0.00053  0.04424  -0.37309 281 GLU A CA  
2174 C C   . GLU A 281 ? 0.89123 1.41755 0.99718 -0.00814 0.06343  -0.35693 281 GLU A C   
2175 O O   . GLU A 281 ? 1.00669 1.54489 1.05940 -0.01320 0.07501  -0.33645 281 GLU A O   
2176 C CB  . GLU A 281 ? 0.82313 1.33453 0.88262 0.00551  0.03744  -0.35826 281 GLU A CB  
2177 C CG  . GLU A 281 ? 0.95579 1.49028 0.95697 0.01302  0.04765  -0.36091 281 GLU A CG  
2178 C CD  . GLU A 281 ? 0.99299 1.55306 1.01147 0.02617  0.04727  -0.40056 281 GLU A CD  
2179 O OE1 . GLU A 281 ? 1.02228 1.57857 1.08636 0.03077  0.03210  -0.42645 281 GLU A OE1 
2180 O OE2 . GLU A 281 ? 0.92242 1.50520 0.90685 0.03160  0.06410  -0.40591 281 GLU A OE2 
2181 N N   . LYS A 282 ? 0.74318 1.26631 0.89848 -0.01005 0.06738  -0.36517 282 LYS A N   
2182 C CA  . LYS A 282 ? 0.71575 1.26044 0.87211 -0.01727 0.08569  -0.35185 282 LYS A CA  
2183 C C   . LYS A 282 ? 0.84731 1.43783 0.97522 -0.01170 0.10527  -0.35760 282 LYS A C   
2184 O O   . LYS A 282 ? 0.89086 1.49491 0.96569 -0.02156 0.11620  -0.33550 282 LYS A O   
2185 C CB  . LYS A 282 ? 0.64403 1.17741 0.86092 -0.01114 0.08487  -0.36327 282 LYS A CB  
2186 C CG  . LYS A 282 ? 0.43760 0.92236 0.68056 -0.01642 0.07036  -0.35419 282 LYS A CG  
2187 C CD  . LYS A 282 ? 0.44943 0.92529 0.73941 -0.00979 0.07350  -0.35246 282 LYS A CD  
2188 C CE  . LYS A 282 ? 0.36442 0.78978 0.67259 -0.01427 0.06223  -0.33733 282 LYS A CE  
2189 N NZ  . LYS A 282 ? 0.41144 0.83436 0.75772 -0.00870 0.06358  -0.32216 282 LYS A NZ  
2190 N N   . GLU B 2   ? 1.07185 0.83664 0.80296 -0.11320 0.08149  0.33414  2   GLU B N   
2191 C CA  . GLU B 2   ? 1.05674 0.83630 0.76037 -0.08979 0.06460  0.33005  2   GLU B CA  
2192 C C   . GLU B 2   ? 1.07924 0.91422 0.78560 -0.08457 0.07858  0.29791  2   GLU B C   
2193 O O   . GLU B 2   ? 1.13907 0.99764 0.80522 -0.08163 0.08262  0.29163  2   GLU B O   
2194 C CB  . GLU B 2   ? 1.14672 0.92346 0.79543 -0.09913 0.06291  0.35686  2   GLU B CB  
2195 C CG  . GLU B 2   ? 1.23212 1.04703 0.84973 -0.12656 0.09727  0.35695  2   GLU B CG  
2196 C CD  . GLU B 2   ? 1.31796 1.11056 0.93848 -0.15529 0.11102  0.38342  2   GLU B CD  
2197 O OE1 . GLU B 2   ? 1.33477 1.08869 0.99412 -0.15798 0.10356  0.38853  2   GLU B OE1 
2198 O OE2 . GLU B 2   ? 1.31544 1.12655 0.89669 -0.17702 0.12975  0.39861  2   GLU B OE2 
2199 N N   . GLU B 3   ? 0.83758 0.69144 0.59096 -0.08267 0.08558  0.27781  3   GLU B N   
2200 C CA  . GLU B 3   ? 0.76339 0.67120 0.52915 -0.07386 0.10051  0.24949  3   GLU B CA  
2201 C C   . GLU B 3   ? 0.70575 0.61122 0.49735 -0.04411 0.07933  0.23600  3   GLU B C   
2202 O O   . GLU B 3   ? 0.73137 0.60696 0.55761 -0.03248 0.06345  0.24026  3   GLU B O   
2203 C CB  . GLU B 3   ? 0.77872 0.72767 0.58818 -0.08754 0.12654  0.23926  3   GLU B CB  
2204 C CG  . GLU B 3   ? 0.83410 0.77839 0.70079 -0.07919 0.11793  0.23324  3   GLU B CG  
2205 C CD  . GLU B 3   ? 0.89690 0.90454 0.80928 -0.08153 0.13943  0.21415  3   GLU B CD  
2206 O OE1 . GLU B 3   ? 0.92945 0.93731 0.88181 -0.09796 0.13477  0.21113  3   GLU B OE1 
2207 O OE2 . GLU B 3   ? 0.85040 0.90407 0.75849 -0.06598 0.15741  0.19737  3   GLU B OE2 
2208 N N   . ILE B 4   ? 0.70149 0.63297 0.47279 -0.03209 0.08186  0.21729  4   ILE B N   
2209 C CA  . ILE B 4   ? 0.58302 0.51428 0.37083 -0.00730 0.06417  0.20413  4   ILE B CA  
2210 C C   . ILE B 4   ? 0.55998 0.51606 0.38079 0.00692  0.08201  0.17648  4   ILE B C   
2211 O O   . ILE B 4   ? 0.58826 0.57209 0.40253 0.00365  0.10667  0.16240  4   ILE B O   
2212 C CB  . ILE B 4   ? 0.57808 0.51152 0.31523 -0.00961 0.05106  0.20004  4   ILE B CB  
2213 C CG1 . ILE B 4   ? 0.66589 0.57246 0.36573 -0.02160 0.03438  0.22647  4   ILE B CG1 
2214 C CG2 . ILE B 4   ? 0.60655 0.54408 0.36457 0.00951  0.03057  0.18992  4   ILE B CG2 
2215 C CD1 . ILE B 4   ? 0.68606 0.59728 0.32291 -0.02753 0.03102  0.22338  4   ILE B CD1 
2216 N N   . TYR B 5   ? 0.47090 0.41806 0.33096 0.02258  0.06828  0.16390  5   TYR B N   
2217 C CA  . TYR B 5   ? 0.52142 0.48743 0.41112 0.03345  0.07573  0.13626  5   TYR B CA  
2218 C C   . TYR B 5   ? 0.51768 0.48445 0.39336 0.04696  0.06671  0.12023  5   TYR B C   
2219 O O   . TYR B 5   ? 0.55621 0.51279 0.43597 0.05252  0.04844  0.12462  5   TYR B O   
2220 C CB  . TYR B 5   ? 0.49505 0.44878 0.42518 0.03465  0.06863  0.13126  5   TYR B CB  
2221 C CG  . TYR B 5   ? 0.58080 0.51605 0.51791 0.01543  0.07197  0.14954  5   TYR B CG  
2222 C CD1 . TYR B 5   ? 0.44471 0.40692 0.38959 -0.00419 0.08860  0.15340  5   TYR B CD1 
2223 C CD2 . TYR B 5   ? 0.58779 0.47830 0.52616 0.01672  0.05928  0.16519  5   TYR B CD2 
2224 C CE1 . TYR B 5   ? 0.63576 0.57831 0.58444 -0.02966 0.09123  0.17248  5   TYR B CE1 
2225 C CE2 . TYR B 5   ? 0.58490 0.44364 0.52389 -0.00360 0.06151  0.18378  5   TYR B CE2 
2226 C CZ  . TYR B 5   ? 0.63384 0.51732 0.57501 -0.03067 0.07694  0.18774  5   TYR B CZ  
2227 O OH  . TYR B 5   ? 0.77449 0.62325 0.71430 -0.05877 0.07875  0.20865  5   TYR B OH  
2228 N N   . TYR B 6   ? 0.43315 0.41192 0.29650 0.05228  0.08043  0.10230  6   TYR B N   
2229 C CA  . TYR B 6   ? 0.48632 0.45451 0.33151 0.06001  0.07318  0.08601  6   TYR B CA  
2230 C C   . TYR B 6   ? 0.49226 0.46359 0.37261 0.07119  0.07003  0.07379  6   TYR B C   
2231 O O   . TYR B 6   ? 0.52422 0.51138 0.42900 0.07778  0.08101  0.06919  6   TYR B O   
2232 C CB  . TYR B 6   ? 0.48560 0.44793 0.28865 0.06087  0.09126  0.07156  6   TYR B CB  
2233 C CG  . TYR B 6   ? 0.57517 0.53165 0.32536 0.04393  0.09060  0.08270  6   TYR B CG  
2234 C CD1 . TYR B 6   ? 0.52059 0.49191 0.26187 0.03388  0.10655  0.09824  6   TYR B CD1 
2235 C CD2 . TYR B 6   ? 0.53490 0.47434 0.24222 0.03262  0.07094  0.08149  6   TYR B CD2 
2236 C CE1 . TYR B 6   ? 0.53970 0.50534 0.22725 0.01419  0.10243  0.11210  6   TYR B CE1 
2237 C CE2 . TYR B 6   ? 0.62510 0.56244 0.27789 0.01357  0.06450  0.09546  6   TYR B CE2 
2238 C CZ  . TYR B 6   ? 0.54978 0.50000 0.19449 0.00441  0.07933  0.11022  6   TYR B CZ  
2239 O OH  . TYR B 6   ? 0.62274 0.58093 0.22286 -0.01805 0.06830  0.12603  6   TYR B OH  
2240 N N   . ILE B 7   ? 0.42019 0.38305 0.30384 0.07134  0.05440  0.07122  7   ILE B N   
2241 C CA  . ILE B 7   ? 0.52284 0.48603 0.42637 0.07704  0.05093  0.06213  7   ILE B CA  
2242 C C   . ILE B 7   ? 0.48298 0.42978 0.36362 0.07324  0.04290  0.05511  7   ILE B C   
2243 O O   . ILE B 7   ? 0.53292 0.47989 0.39952 0.06322  0.03276  0.05906  7   ILE B O   
2244 C CB  . ILE B 7   ? 0.49220 0.46319 0.42465 0.07539  0.04499  0.06511  7   ILE B CB  
2245 C CG1 . ILE B 7   ? 0.47656 0.44740 0.41310 0.07426  0.03674  0.07401  7   ILE B CG1 
2246 C CG2 . ILE B 7   ? 0.57622 0.55408 0.52762 0.07251  0.05159  0.06884  7   ILE B CG2 
2247 C CD1 . ILE B 7   ? 0.50628 0.47397 0.47123 0.07843  0.03793  0.07355  7   ILE B CD1 
2248 N N   . THR B 8   ? 0.33629 0.26935 0.21439 0.07914  0.04492  0.04776  8   THR B N   
2249 C CA  . THR B 8   ? 0.49264 0.39868 0.34739 0.07191  0.03790  0.04257  8   THR B CA  
2250 C C   . THR B 8   ? 0.35492 0.26611 0.22569 0.06980  0.03171  0.04706  8   THR B C   
2251 O O   . THR B 8   ? 0.39034 0.32383 0.28509 0.07459  0.03259  0.05034  8   THR B O   
2252 C CB  . THR B 8   ? 0.54621 0.41529 0.37547 0.08303  0.04738  0.03209  8   THR B CB  
2253 O OG1 . THR B 8   ? 0.53183 0.40584 0.38806 0.10227  0.05096  0.03610  8   THR B OG1 
2254 C CG2 . THR B 8   ? 0.49415 0.36718 0.30746 0.08744  0.06144  0.02580  8   THR B CG2 
2255 N N   . PHE B 9   ? 0.46165 0.34779 0.31159 0.05813  0.02528  0.04713  9   PHE B N   
2256 C CA  . PHE B 9   ? 0.47222 0.36117 0.32606 0.05153  0.02050  0.05453  9   PHE B CA  
2257 C C   . PHE B 9   ? 0.47852 0.37049 0.34529 0.06876  0.01981  0.05974  9   PHE B C   
2258 O O   . PHE B 9   ? 0.46337 0.37555 0.33670 0.06294  0.01575  0.06481  9   PHE B O   
2259 C CB  . PHE B 9   ? 0.46635 0.31584 0.28949 0.03404  0.01405  0.05791  9   PHE B CB  
2260 C CG  . PHE B 9   ? 0.56406 0.35633 0.36418 0.04806  0.01398  0.05573  9   PHE B CG  
2261 C CD1 . PHE B 9   ? 0.57250 0.33581 0.35254 0.05306  0.02029  0.04092  9   PHE B CD1 
2262 C CD2 . PHE B 9   ? 0.54547 0.30955 0.34072 0.05731  0.00795  0.06866  9   PHE B CD2 
2263 C CE1 . PHE B 9   ? 0.66607 0.36937 0.42445 0.07078  0.02601  0.03361  9   PHE B CE1 
2264 C CE2 . PHE B 9   ? 0.58978 0.29572 0.37093 0.07782  0.00897  0.06767  9   PHE B CE2 
2265 C CZ  . PHE B 9   ? 0.66175 0.33515 0.42587 0.08648  0.02073  0.04739  9   PHE B CZ  
2266 N N   . ARG B 10  ? 0.44836 0.32615 0.31967 0.08920  0.02425  0.05785  10  ARG B N   
2267 C CA  . ARG B 10  ? 0.45551 0.34894 0.35116 0.10705  0.02021  0.06685  10  ARG B CA  
2268 C C   . ARG B 10  ? 0.46174 0.40385 0.38521 0.10171  0.01962  0.06714  10  ARG B C   
2269 O O   . ARG B 10  ? 0.36636 0.32886 0.30019 0.09871  0.00774  0.07576  10  ARG B O   
2270 C CB  . ARG B 10  ? 0.41057 0.29043 0.31670 0.13389  0.03136  0.06245  10  ARG B CB  
2271 C CG  . ARG B 10  ? 0.52352 0.33969 0.39968 0.14225  0.03132  0.06035  10  ARG B CG  
2272 C CD  . ARG B 10  ? 0.66481 0.46947 0.55913 0.17786  0.04675  0.05384  10  ARG B CD  
2273 N NE  . ARG B 10  ? 0.76314 0.52722 0.62020 0.17679  0.06571  0.03039  10  ARG B NE  
2274 C CZ  . ARG B 10  ? 0.73079 0.52298 0.57999 0.16635  0.07941  0.01814  10  ARG B CZ  
2275 N NH1 . ARG B 10  ? 0.59884 0.45378 0.47995 0.15879  0.07853  0.02712  10  ARG B NH1 
2276 N NH2 . ARG B 10  ? 0.71112 0.46137 0.51259 0.15986  0.09263  -0.00275 10  ARG B NH2 
2277 N N   . GLU B 11  ? 0.42356 0.37966 0.35420 0.09735  0.03002  0.05903  11  GLU B N   
2278 C CA  . GLU B 11  ? 0.46035 0.44715 0.41293 0.08910  0.02994  0.05859  11  GLU B CA  
2279 C C   . GLU B 11  ? 0.42546 0.41079 0.36663 0.07311  0.02507  0.05399  11  GLU B C   
2280 O O   . GLU B 11  ? 0.33181 0.33080 0.27720 0.06349  0.01924  0.05198  11  GLU B O   
2281 C CB  . GLU B 11  ? 0.45093 0.44324 0.41013 0.08886  0.04221  0.05628  11  GLU B CB  
2282 C CG  . GLU B 11  ? 0.44271 0.44856 0.41464 0.10268  0.05472  0.05806  11  GLU B CG  
2283 C CD  . GLU B 11  ? 0.44792 0.42274 0.39245 0.11563  0.06232  0.05130  11  GLU B CD  
2284 O OE1 . GLU B 11  ? 0.50927 0.45734 0.42224 0.10595  0.05905  0.04692  11  GLU B OE1 
2285 O OE2 . GLU B 11  ? 0.58380 0.56056 0.53986 0.13546  0.07134  0.04951  11  GLU B OE2 
2286 N N   . ALA B 12  ? 0.38351 0.35589 0.31010 0.06859  0.02853  0.05071  12  ALA B N   
2287 C CA  . ALA B 12  ? 0.43150 0.40967 0.35212 0.05732  0.03085  0.04452  12  ALA B CA  
2288 C C   . ALA B 12  ? 0.39310 0.37174 0.29344 0.04743  0.02355  0.04746  12  ALA B C   
2289 O O   . ALA B 12  ? 0.41946 0.40673 0.31168 0.03720  0.02540  0.03880  12  ALA B O   
2290 C CB  . ALA B 12  ? 0.37040 0.34898 0.28806 0.05327  0.03432  0.04510  12  ALA B CB  
2291 N N   . ARG B 13  ? 0.39623 0.35949 0.28249 0.04965  0.01435  0.06007  13  ARG B N   
2292 C CA  . ARG B 13  ? 0.41643 0.37774 0.27862 0.03924  0.00284  0.07050  13  ARG B CA  
2293 C C   . ARG B 13  ? 0.41229 0.39491 0.28477 0.04034  -0.00961 0.07309  13  ARG B C   
2294 O O   . ARG B 13  ? 0.40263 0.39416 0.24957 0.02319  -0.01826 0.07456  13  ARG B O   
2295 C CB  . ARG B 13  ? 0.43340 0.36178 0.27919 0.04393  -0.00682 0.08805  13  ARG B CB  
2296 C CG  . ARG B 13  ? 0.46231 0.37094 0.28566 0.02655  0.00048  0.08845  13  ARG B CG  
2297 C CD  . ARG B 13  ? 0.46403 0.32216 0.26921 0.03017  -0.00809 0.10212  13  ARG B CD  
2298 N NE  . ARG B 13  ? 0.42159 0.26205 0.21200 0.00966  -0.00169 0.09834  13  ARG B NE  
2299 C CZ  . ARG B 13  ? 0.50595 0.29270 0.26829 -0.00124 -0.00821 0.10889  13  ARG B CZ  
2300 N NH1 . ARG B 13  ? 0.55305 0.29285 0.29921 0.01171  -0.02045 0.12626  13  ARG B NH1 
2301 N NH2 . ARG B 13  ? 0.57185 0.35091 0.32356 -0.02720 -0.00445 0.10407  13  ARG B NH2 
2302 N N   . MET B 14  ? 0.42908 0.42515 0.33626 0.05578  -0.01075 0.07386  14  MET B N   
2303 C CA  . MET B 14  ? 0.44640 0.47462 0.37133 0.05069  -0.02510 0.07820  14  MET B CA  
2304 C C   . MET B 14  ? 0.40542 0.43927 0.31819 0.02764  -0.02052 0.05926  14  MET B C   
2305 O O   . MET B 14  ? 0.48245 0.53038 0.37784 0.00802  -0.03552 0.05831  14  MET B O   
2306 C CB  . MET B 14  ? 0.38820 0.44004 0.35964 0.06946  -0.02223 0.08353  14  MET B CB  
2307 C CG  . MET B 14  ? 0.50342 0.60250 0.50362 0.05896  -0.03934 0.09076  14  MET B CG  
2308 S SD  . MET B 14  ? 0.49246 0.61676 0.50570 0.07276  -0.06960 0.11998  14  MET B SD  
2309 C CE  . MET B 14  ? 0.44128 0.56933 0.40281 0.03372  -0.09437 0.11960  14  MET B CE  
2310 N N   . LEU B 15  ? 0.36430 0.38214 0.28154 0.02944  -0.00117 0.04403  15  LEU B N   
2311 C CA  . LEU B 15  ? 0.39136 0.39944 0.29827 0.01365  0.00680  0.02383  15  LEU B CA  
2312 C C   . LEU B 15  ? 0.46224 0.46233 0.32618 -0.00175 0.00966  0.01152  15  LEU B C   
2313 O O   . LEU B 15  ? 0.54986 0.54535 0.38929 -0.02214 0.00692  -0.00446 15  LEU B O   
2314 C CB  . LEU B 15  ? 0.38014 0.36973 0.30455 0.02587  0.02503  0.01650  15  LEU B CB  
2315 C CG  . LEU B 15  ? 0.48602 0.48098 0.44070 0.03449  0.02569  0.02769  15  LEU B CG  
2316 C CD1 . LEU B 15  ? 0.35952 0.33744 0.32156 0.04743  0.03781  0.02857  15  LEU B CD1 
2317 C CD2 . LEU B 15  ? 0.39143 0.38928 0.35756 0.01670  0.02119  0.02408  15  LEU B CD2 
2318 N N   . LEU B 16  ? 0.46145 0.45920 0.31055 0.00318  0.01642  0.01767  16  LEU B N   
2319 C CA  . LEU B 16  ? 0.48363 0.48041 0.28922 -0.01421 0.02479  0.00748  16  LEU B CA  
2320 C C   . LEU B 16  ? 0.45090 0.45624 0.21820 -0.03413 0.00124  0.01999  16  LEU B C   
2321 O O   . LEU B 16  ? 0.58290 0.58734 0.30174 -0.05679 0.00538  0.00658  16  LEU B O   
2322 C CB  . LEU B 16  ? 0.48561 0.48480 0.29006 -0.00982 0.03791  0.01527  16  LEU B CB  
2323 C CG  . LEU B 16  ? 0.45505 0.45618 0.30072 0.00854  0.05476  0.00716  16  LEU B CG  
2324 C CD1 . LEU B 16  ? 0.51584 0.52511 0.36762 0.00825  0.05746  0.02101  16  LEU B CD1 
2325 C CD2 . LEU B 16  ? 0.50706 0.50938 0.35563 0.01062  0.07890  -0.01971 16  LEU B CD2 
2326 N N   . ALA B 17  ? 0.47879 0.49425 0.26628 -0.02503 -0.02340 0.04587  17  ALA B N   
2327 C CA  . ALA B 17  ? 0.47519 0.50547 0.23513 -0.04015 -0.05278 0.06550  17  ALA B CA  
2328 C C   . ALA B 17  ? 0.54265 0.59470 0.30399 -0.05873 -0.06966 0.05538  17  ALA B C   
2329 O O   . ALA B 17  ? 0.71458 0.78172 0.43703 -0.08248 -0.09444 0.06470  17  ALA B O   
2330 C CB  . ALA B 17  ? 0.52480 0.55819 0.31459 -0.01679 -0.07269 0.09909  17  ALA B CB  
2331 N N   . SER B 18  ? 0.53469 0.58725 0.33441 -0.05382 -0.05894 0.03832  18  SER B N   
2332 C CA  . SER B 18  ? 0.53554 0.60594 0.34099 -0.07766 -0.07514 0.02901  18  SER B CA  
2333 C C   . SER B 18  ? 0.59883 0.63227 0.36184 -0.10128 -0.05599 -0.00974 18  SER B C   
2334 O O   . SER B 18  ? 0.70311 0.70366 0.46170 -0.08710 -0.02494 -0.02878 18  SER B O   
2335 C CB  . SER B 18  ? 0.50526 0.59658 0.37828 -0.06296 -0.07444 0.03719  18  SER B CB  
2336 O OG  . SER B 18  ? 0.50647 0.61428 0.41976 -0.02945 -0.07426 0.06203  18  SER B OG  
2337 N N   . ARG B 19  ? 0.61747 0.65665 0.35201 -0.13694 -0.07548 -0.02172 19  ARG B N   
2338 C CA  . ARG B 19  ? 0.79238 0.78581 0.49405 -0.16018 -0.05867 -0.06189 19  ARG B CA  
2339 C C   . ARG B 19  ? 0.76568 0.77023 0.50346 -0.18203 -0.07693 -0.06063 19  ARG B C   
2340 O O   . ARG B 19  ? 0.75932 0.82217 0.53313 -0.19021 -0.10831 -0.03190 19  ARG B O   
2341 C CB  . ARG B 19  ? 0.88867 0.86377 0.50252 -0.19486 -0.06093 -0.08769 19  ARG B CB  
2342 C CG  . ARG B 19  ? 1.12696 1.03563 0.70388 -0.20317 -0.02676 -0.13719 19  ARG B CG  
2343 C CD  . ARG B 19  ? 1.21878 1.10496 0.71299 -0.23001 -0.01752 -0.16737 19  ARG B CD  
2344 N NE  . ARG B 19  ? 1.31312 1.16720 0.79931 -0.20114 0.03025  -0.19274 19  ARG B NE  
2345 C CZ  . ARG B 19  ? 1.35604 1.16121 0.86680 -0.17771 0.06337  -0.22076 19  ARG B CZ  
2346 N NH1 . ARG B 19  ? 1.24194 1.00890 0.77691 -0.18368 0.05667  -0.22977 19  ARG B NH1 
2347 N NH2 . ARG B 19  ? 1.35141 1.14890 0.87038 -0.14661 0.10240  -0.23547 19  ARG B NH2 
2348 N N   . GLY B 20  ? 0.88472 0.83462 0.61858 -0.19019 -0.05634 -0.08928 20  GLY B N   
2349 C CA  . GLY B 20  ? 0.91929 0.87318 0.68859 -0.21506 -0.06981 -0.08564 20  GLY B CA  
2350 C C   . GLY B 20  ? 0.87804 0.85100 0.71980 -0.18244 -0.05796 -0.05847 20  GLY B C   
2351 O O   . GLY B 20  ? 0.81202 0.74710 0.66247 -0.14976 -0.03020 -0.06225 20  GLY B O   
2352 N N   . ASN B 21  ? 0.75367 0.79156 0.64801 -0.19169 -0.07879 -0.03037 21  ASN B N   
2353 C CA  . ASN B 21  ? 0.65404 0.71284 0.60973 -0.17011 -0.06509 -0.00779 21  ASN B CA  
2354 C C   . ASN B 21  ? 0.63873 0.76980 0.63935 -0.13871 -0.07343 0.02294  21  ASN B C   
2355 O O   . ASN B 21  ? 0.70505 0.88260 0.70559 -0.14378 -0.09955 0.03428  21  ASN B O   
2356 C CB  . ASN B 21  ? 0.65497 0.72485 0.63791 -0.21084 -0.07321 -0.00460 21  ASN B CB  
2357 C CG  . ASN B 21  ? 0.83648 0.81303 0.78686 -0.22728 -0.05447 -0.02847 21  ASN B CG  
2358 O OD1 . ASN B 21  ? 0.86884 0.77693 0.77030 -0.21558 -0.04079 -0.05545 21  ASN B OD1 
2359 N ND2 . ASN B 21  ? 0.96476 0.93760 0.94317 -0.25531 -0.05292 -0.01800 21  ASN B ND2 
2360 N N   . VAL B 22  ? 0.58555 0.72007 0.61958 -0.10541 -0.05171 0.03640  22  VAL B N   
2361 C CA  . VAL B 22  ? 0.53243 0.71397 0.59978 -0.06941 -0.05254 0.05839  22  VAL B CA  
2362 C C   . VAL B 22  ? 0.53159 0.73150 0.64145 -0.05166 -0.02971 0.07054  22  VAL B C   
2363 O O   . VAL B 22  ? 0.51965 0.67678 0.61625 -0.05499 -0.01036 0.06388  22  VAL B O   
2364 C CB  . VAL B 22  ? 0.54055 0.68454 0.56856 -0.04194 -0.04683 0.05366  22  VAL B CB  
2365 C CG1 . VAL B 22  ? 0.52581 0.61560 0.53574 -0.02706 -0.01998 0.04155  22  VAL B CG1 
2366 C CG2 . VAL B 22  ? 0.49754 0.67690 0.55316 -0.00944 -0.05270 0.07572  22  VAL B CG2 
2367 N N   . LYS B 23  ? 0.54152 0.80608 0.70160 -0.03178 -0.03172 0.08952  23  LYS B N   
2368 C CA  . LYS B 23  ? 0.36864 0.66152 0.56715 -0.01377 -0.00567 0.09915  23  LYS B CA  
2369 C C   . LYS B 23  ? 0.40021 0.65736 0.57660 0.02716  0.01154  0.09624  23  LYS B C   
2370 O O   . LYS B 23  ? 0.47748 0.73675 0.65367 0.05188  0.00078  0.10062  23  LYS B O   
2371 C CB  . LYS B 23  ? 0.25117 0.63931 0.52296 -0.01088 -0.01189 0.11782  23  LYS B CB  
2372 C CG  . LYS B 23  ? 0.33048 0.76454 0.63042 -0.06009 -0.02930 0.12261  23  LYS B CG  
2373 C CD  . LYS B 23  ? 0.42893 0.79188 0.68080 -0.09783 -0.02094 0.10753  23  LYS B CD  
2374 C CE  . LYS B 23  ? 0.49550 0.88783 0.76376 -0.15408 -0.04284 0.10839  23  LYS B CE  
2375 N NZ  . LYS B 23  ? 0.34569 0.84725 0.69704 -0.16398 -0.04009 0.13124  23  LYS B NZ  
2376 N N   . LEU B 24  ? 0.40213 0.62310 0.55610 0.03071  0.03529  0.09090  24  LEU B N   
2377 C CA  . LEU B 24  ? 0.42406 0.60384 0.54582 0.05911  0.04838  0.08501  24  LEU B CA  
2378 C C   . LEU B 24  ? 0.40756 0.60013 0.53531 0.06941  0.07665  0.08748  24  LEU B C   
2379 O O   . LEU B 24  ? 0.37779 0.58420 0.51275 0.04774  0.08812  0.09366  24  LEU B O   
2380 C CB  . LEU B 24  ? 0.41366 0.53157 0.48759 0.05071  0.04494  0.07495  24  LEU B CB  
2381 C CG  . LEU B 24  ? 0.40719 0.50463 0.45969 0.04738  0.02616  0.06764  24  LEU B CG  
2382 C CD1 . LEU B 24  ? 0.41803 0.46942 0.43527 0.05320  0.03162  0.05927  24  LEU B CD1 
2383 C CD2 . LEU B 24  ? 0.50915 0.62834 0.57274 0.06530  0.01479  0.07533  24  LEU B CD2 
2384 N N   . ASN B 25  ? 0.41065 0.59218 0.52804 0.09937  0.08895  0.08206  25  ASN B N   
2385 C CA  . ASN B 25  ? 0.40081 0.57624 0.49810 0.10641  0.11751  0.07764  25  ASN B CA  
2386 C C   . ASN B 25  ? 0.42019 0.53629 0.45871 0.09587  0.11383  0.07301  25  ASN B C   
2387 O O   . ASN B 25  ? 0.50275 0.58093 0.51758 0.10076  0.09770  0.06712  25  ASN B O   
2388 C CB  . ASN B 25  ? 0.44964 0.62837 0.55354 0.14223  0.13497  0.06826  25  ASN B CB  
2389 C CG  . ASN B 25  ? 0.49845 0.65982 0.56203 0.14574  0.16602  0.05706  25  ASN B CG  
2390 O OD1 . ASN B 25  ? 0.56707 0.67089 0.57300 0.14598  0.16417  0.04591  25  ASN B OD1 
2391 N ND2 . ASN B 25  ? 0.48067 0.69040 0.56788 0.13847  0.18941  0.05963  25  ASN B ND2 
2392 N N   . LEU B 26  ? 0.45641 0.57000 0.47379 0.07959  0.12753  0.07934  26  LEU B N   
2393 C CA  . LEU B 26  ? 0.45611 0.52363 0.42656 0.06914  0.11841  0.08229  26  LEU B CA  
2394 C C   . LEU B 26  ? 0.47869 0.53697 0.40289 0.06800  0.13705  0.08152  26  LEU B C   
2395 O O   . LEU B 26  ? 0.48815 0.52566 0.37904 0.05226  0.13089  0.09439  26  LEU B O   
2396 C CB  . LEU B 26  ? 0.37322 0.43063 0.35237 0.04640  0.10696  0.09682  26  LEU B CB  
2397 C CG  . LEU B 26  ? 0.43613 0.49635 0.44789 0.04104  0.09025  0.09236  26  LEU B CG  
2398 C CD1 . LEU B 26  ? 0.44102 0.48332 0.45953 0.01595  0.08511  0.10248  26  LEU B CD1 
2399 C CD2 . LEU B 26  ? 0.40591 0.43875 0.40450 0.05391  0.07443  0.08087  26  LEU B CD2 
2400 N N   . ASP B 27  ? 0.51105 0.58196 0.42935 0.08536  0.15986  0.06658  27  ASP B N   
2401 C CA  . ASP B 27  ? 0.56670 0.61765 0.42390 0.08316  0.17810  0.05741  27  ASP B CA  
2402 C C   . ASP B 27  ? 0.57321 0.59321 0.40751 0.10667  0.18570  0.03101  27  ASP B C   
2403 O O   . ASP B 27  ? 0.50429 0.51441 0.30561 0.10655  0.20368  0.01266  27  ASP B O   
2404 C CB  . ASP B 27  ? 0.56790 0.65719 0.42678 0.07068  0.20621  0.06076  27  ASP B CB  
2405 C CG  . ASP B 27  ? 0.60181 0.74483 0.52904 0.08671  0.22417  0.05395  27  ASP B CG  
2406 O OD1 . ASP B 27  ? 0.54667 0.68726 0.50336 0.11511  0.22076  0.04034  27  ASP B OD1 
2407 O OD2 . ASP B 27  ? 0.62606 0.81427 0.57842 0.06845  0.23906  0.06494  27  ASP B OD2 
2408 N N   . LEU B 28  ? 0.55573 0.55371 0.41002 0.11862  0.16356  0.02692  28  LEU B N   
2409 C CA  . LEU B 28  ? 0.60426 0.55621 0.43294 0.13662  0.16560  0.00562  28  LEU B CA  
2410 C C   . LEU B 28  ? 0.60135 0.56878 0.46230 0.16307  0.18975  -0.00802 28  LEU B C   
2411 O O   . LEU B 28  ? 0.63480 0.56423 0.46330 0.17102  0.20201  -0.03062 28  LEU B O   
2412 C CB  . LEU B 28  ? 0.63383 0.53767 0.38417 0.11826  0.16311  -0.00802 28  LEU B CB  
2413 C CG  . LEU B 28  ? 0.61447 0.50953 0.34407 0.09050  0.13003  0.00684  28  LEU B CG  
2414 C CD1 . LEU B 28  ? 0.62334 0.48348 0.27721 0.06969  0.12621  -0.00530 28  LEU B CD1 
2415 C CD2 . LEU B 28  ? 0.45470 0.33537 0.21120 0.09291  0.10620  0.00993  28  LEU B CD2 
2416 N N   . ARG B 29  ? 0.60471 0.63107 0.53431 0.17199  0.19199  0.00578  29  ARG B N   
2417 C CA  . ARG B 29  ? 0.62190 0.68251 0.60290 0.19500  0.20740  -0.00131 29  ARG B CA  
2418 C C   . ARG B 29  ? 0.69564 0.76969 0.65567 0.19157  0.24028  -0.01961 29  ARG B C   
2419 O O   . ARG B 29  ? 0.82339 0.90764 0.80942 0.21534  0.25879  -0.03604 29  ARG B O   
2420 C CB  . ARG B 29  ? 0.74531 0.76247 0.73436 0.22260  0.19682  -0.01014 29  ARG B CB  
2421 C CG  . ARG B 29  ? 0.80026 0.80175 0.80286 0.22326  0.16334  0.00824  29  ARG B CG  
2422 C CD  . ARG B 29  ? 0.89337 0.95369 0.93412 0.20709  0.14971  0.03051  29  ARG B CD  
2423 N NE  . ARG B 29  ? 0.82086 0.89548 0.89899 0.21336  0.12146  0.04750  29  ARG B NE  
2424 C CZ  . ARG B 29  ? 0.80645 0.92642 0.94277 0.22862  0.11453  0.05716  29  ARG B CZ  
2425 N NH1 . ARG B 29  ? 0.73345 0.89108 0.90572 0.24308  0.13661  0.04962  29  ARG B NH1 
2426 N NH2 . ARG B 29  ? 0.86333 0.99453 1.02140 0.22828  0.08400  0.07512  29  ARG B NH2 
2427 N N   . LYS B 30  ? 0.72445 0.79905 0.63594 0.16210  0.24786  -0.01691 30  LYS B N   
2428 C CA  . LYS B 30  ? 0.69194 0.78731 0.57930 0.15373  0.27969  -0.03305 30  LYS B CA  
2429 C C   . LYS B 30  ? 0.75564 0.93191 0.71326 0.15522  0.29968  -0.02436 30  LYS B C   
2430 O O   . LYS B 30  ? 0.72249 0.92781 0.68801 0.16376  0.33113  -0.04391 30  LYS B O   
2431 C CB  . LYS B 30  ? 0.61889 0.69629 0.43134 0.11724  0.27743  -0.02682 30  LYS B CB  
2432 C CG  . LYS B 30  ? 0.69767 0.79219 0.46673 0.10527  0.30911  -0.04623 30  LYS B CG  
2433 C CD  . LYS B 30  ? 0.71360 0.82115 0.43121 0.06439  0.30477  -0.02458 30  LYS B CD  
2434 C CE  . LYS B 30  ? 0.80247 0.93123 0.46303 0.05121  0.33305  -0.04178 30  LYS B CE  
2435 N NZ  . LYS B 30  ? 0.86445 0.97724 0.51592 0.08127  0.35797  -0.08354 30  LYS B NZ  
2436 N N   . THR B 31  ? 0.72116 0.93719 0.73138 0.14575  0.28257  0.00269  31  THR B N   
2437 C CA  . THR B 31  ? 0.79399 1.08887 0.86551 0.13411  0.29847  0.01450  31  THR B CA  
2438 C C   . THR B 31  ? 0.81021 1.15380 0.96918 0.15179  0.28058  0.02726  31  THR B C   
2439 O O   . THR B 31  ? 0.80800 1.22406 1.02948 0.14946  0.29510  0.03142  31  THR B O   
2440 C CB  . THR B 31  ? 0.83104 1.13357 0.87658 0.09038  0.29504  0.03862  31  THR B CB  
2441 O OG1 . THR B 31  ? 0.85057 1.12254 0.81783 0.07129  0.31242  0.02962  31  THR B OG1 
2442 C CG2 . THR B 31  ? 0.85868 1.23727 0.96614 0.06899  0.30912  0.05354  31  THR B CG2 
2443 N N   . ASN B 32  ? 0.83308 1.14322 0.99741 0.16683  0.24891  0.03391  32  ASN B N   
2444 C CA  . ASN B 32  ? 0.85625 1.20880 1.09269 0.18118  0.22529  0.04765  32  ASN B CA  
2445 C C   . ASN B 32  ? 0.74523 1.15835 1.02388 0.14741  0.21266  0.07141  32  ASN B C   
2446 O O   . ASN B 32  ? 0.67195 1.12181 1.00154 0.14821  0.18594  0.08549  32  ASN B O   
2447 C CB  . ASN B 32  ? 0.89627 1.28818 1.18902 0.21415  0.24006  0.03633  32  ASN B CB  
2448 C CG  . ASN B 32  ? 0.97880 1.30526 1.22887 0.24449  0.25597  0.00937  32  ASN B CG  
2449 O OD1 . ASN B 32  ? 1.00347 1.27903 1.18183 0.23305  0.27188  -0.00661 32  ASN B OD1 
2450 N ND2 . ASN B 32  ? 0.99916 1.32472 1.29145 0.28118  0.24939  0.00499  32  ASN B ND2 
2451 N N   . ARG B 33  ? 0.62007 1.04110 0.87402 0.11364  0.23000  0.07661  33  ARG B N   
2452 C CA  . ARG B 33  ? 0.52711 0.96825 0.79214 0.07218  0.21565  0.09869  33  ARG B CA  
2453 C C   . ARG B 33  ? 0.37795 0.78164 0.63001 0.07041  0.18347  0.10690  33  ARG B C   
2454 O O   . ARG B 33  ? 0.41905 0.75483 0.61244 0.07869  0.17980  0.10008  33  ARG B O   
2455 C CB  . ARG B 33  ? 0.50825 0.92035 0.71602 0.04127  0.23596  0.10293  33  ARG B CB  
2456 C CG  . ARG B 33  ? 0.48065 0.90274 0.69461 -0.00696 0.22822  0.12596  33  ARG B CG  
2457 C CD  . ARG B 33  ? 0.54386 0.89025 0.67829 -0.02286 0.22763  0.13389  33  ARG B CD  
2458 N NE  . ARG B 33  ? 0.64753 0.97423 0.76737 -0.06869 0.22257  0.15694  33  ARG B NE  
2459 C CZ  . ARG B 33  ? 0.58244 0.91324 0.73611 -0.09849 0.20258  0.17059  33  ARG B CZ  
2460 N NH1 . ARG B 33  ? 0.50624 0.87512 0.71407 -0.09174 0.18418  0.16528  33  ARG B NH1 
2461 N NH2 . ARG B 33  ? 0.56714 0.85514 0.69424 -0.13842 0.19826  0.18923  33  ARG B NH2 
2462 N N   . VAL B 34  ? 0.34216 0.79003 0.64624 0.05644  0.15798  0.11925  34  VAL B N   
2463 C CA  . VAL B 34  ? 0.35484 0.74864 0.62951 0.04397  0.12106  0.11706  34  VAL B CA  
2464 C C   . VAL B 34  ? 0.37695 0.74807 0.63377 -0.00491 0.11187  0.12366  34  VAL B C   
2465 O O   . VAL B 34  ? 0.44262 0.85850 0.72808 -0.03436 0.12576  0.13609  34  VAL B O   
2466 C CB  . VAL B 34  ? 0.30083 0.73401 0.62008 0.05601  0.09065  0.12164  34  VAL B CB  
2467 C CG1 . VAL B 34  ? 0.35312 0.76036 0.66276 0.10465  0.09161  0.11488  34  VAL B CG1 
2468 C CG2 . VAL B 34  ? 0.25156 0.79101 0.65481 0.04681  0.09185  0.13737  34  VAL B CG2 
2469 N N   . GLN B 35  ? 0.36874 0.66519 0.57679 -0.01347 0.09119  0.11516  35  GLN B N   
2470 C CA  . GLN B 35  ? 0.39184 0.64373 0.57644 -0.05242 0.08331  0.11785  35  GLN B CA  
2471 C C   . GLN B 35  ? 0.45714 0.66666 0.62131 -0.06171 0.05494  0.10393  35  GLN B C   
2472 O O   . GLN B 35  ? 0.49504 0.69710 0.64797 -0.03745 0.04314  0.09421  35  GLN B O   
2473 C CB  . GLN B 35  ? 0.44433 0.63224 0.57875 -0.05038 0.09781  0.12183  35  GLN B CB  
2474 C CG  . GLN B 35  ? 0.39048 0.60777 0.52130 -0.04282 0.12761  0.13251  35  GLN B CG  
2475 C CD  . GLN B 35  ? 0.52973 0.68462 0.60485 -0.04735 0.13318  0.14205  35  GLN B CD  
2476 O OE1 . GLN B 35  ? 0.60063 0.71123 0.66137 -0.07341 0.12456  0.15427  35  GLN B OE1 
2477 N NE2 . GLN B 35  ? 0.49660 0.64290 0.53783 -0.02247 0.14499  0.13739  35  GLN B NE2 
2478 N N   . GLU B 36  ? 0.45723 0.63020 0.60907 -0.09919 0.04713  0.10245  36  GLU B N   
2479 C CA  . GLU B 36  ? 0.50155 0.63673 0.63178 -0.11891 0.02443  0.08482  36  GLU B CA  
2480 C C   . GLU B 36  ? 0.49986 0.54847 0.58078 -0.10094 0.02821  0.07017  36  GLU B C   
2481 O O   . GLU B 36  ? 0.55076 0.54678 0.61548 -0.10410 0.03906  0.07621  36  GLU B O   
2482 C CB  . GLU B 36  ? 0.59686 0.73356 0.74004 -0.17195 0.01673  0.08818  36  GLU B CB  
2483 C CG  . GLU B 36  ? 0.78099 0.83156 0.88036 -0.20090 0.00549  0.06724  36  GLU B CG  
2484 C CD  . GLU B 36  ? 0.85854 0.92307 0.94472 -0.21809 -0.02010 0.04667  36  GLU B CD  
2485 O OE1 . GLU B 36  ? 0.79749 0.93418 0.90788 -0.20048 -0.03204 0.05325  36  GLU B OE1 
2486 O OE2 . GLU B 36  ? 0.94234 0.94245 0.99071 -0.25133 -0.02890 0.02477  36  GLU B OE2 
2487 N N   . VAL B 37  ? 0.56191 0.60046 0.62244 -0.08168 0.01930  0.05436  37  VAL B N   
2488 C CA  . VAL B 37  ? 0.58648 0.56202 0.61156 -0.06217 0.02526  0.03956  37  VAL B CA  
2489 C C   . VAL B 37  ? 0.63208 0.58442 0.62908 -0.07888 0.01382  0.01453  37  VAL B C   
2490 O O   . VAL B 37  ? 0.60308 0.59308 0.59540 -0.07844 0.00090  0.01161  37  VAL B O   
2491 C CB  . VAL B 37  ? 0.44817 0.43844 0.46995 -0.02524 0.03121  0.04419  37  VAL B CB  
2492 C CG1 . VAL B 37  ? 0.50204 0.44378 0.50044 -0.00695 0.03813  0.03283  37  VAL B CG1 
2493 C CG2 . VAL B 37  ? 0.50720 0.52535 0.54679 -0.01306 0.04234  0.06388  37  VAL B CG2 
2494 N N   . GLU B 38  ? 0.69805 0.58352 0.67124 -0.09349 0.01894  -0.00346 38  GLU B N   
2495 C CA  . GLU B 38  ? 0.67243 0.52736 0.60656 -0.11096 0.01351  -0.03428 38  GLU B CA  
2496 C C   . GLU B 38  ? 0.67563 0.51731 0.58830 -0.07843 0.02655  -0.04851 38  GLU B C   
2497 O O   . GLU B 38  ? 0.64479 0.47100 0.57177 -0.04643 0.04131  -0.04096 38  GLU B O   
2498 C CB  . GLU B 38  ? 0.76426 0.53997 0.67534 -0.13779 0.01830  -0.05500 38  GLU B CB  
2499 C CG  . GLU B 38  ? 0.88724 0.66238 0.81994 -0.17488 0.00967  -0.03796 38  GLU B CG  
2500 C CD  . GLU B 38  ? 0.93091 0.68711 0.88960 -0.15601 0.02324  -0.00981 38  GLU B CD  
2501 O OE1 . GLU B 38  ? 0.87855 0.70107 0.86989 -0.14705 0.02352  0.01816  38  GLU B OE1 
2502 O OE2 . GLU B 38  ? 1.01424 0.68546 0.95751 -0.15077 0.03371  -0.01552 38  GLU B OE2 
2503 N N   . ILE B 39  ? 0.73416 0.58820 0.61207 -0.09022 0.01977  -0.06651 39  ILE B N   
2504 C CA  . ILE B 39  ? 0.81328 0.66002 0.66649 -0.06783 0.03546  -0.08140 39  ILE B CA  
2505 C C   . ILE B 39  ? 0.88716 0.67711 0.69160 -0.08499 0.04840  -0.12173 39  ILE B C   
2506 O O   . ILE B 39  ? 0.92433 0.71997 0.68349 -0.11766 0.03556  -0.13791 39  ILE B O   
2507 C CB  . ILE B 39  ? 0.80377 0.70643 0.64644 -0.06706 0.02162  -0.06713 39  ILE B CB  
2508 C CG1 . ILE B 39  ? 0.68689 0.64052 0.57045 -0.06415 0.00197  -0.03422 39  ILE B CG1 
2509 C CG2 . ILE B 39  ? 0.66157 0.56941 0.50472 -0.03724 0.04020  -0.06528 39  ILE B CG2 
2510 C CD1 . ILE B 39  ? 0.60509 0.59739 0.48619 -0.05060 -0.00814 -0.01558 39  ILE B CD1 
2511 N N   . LYS B 40  ? 0.89870 0.63181 0.71049 -0.06240 0.07322  -0.13806 40  LYS B N   
2512 C CA  . LYS B 40  ? 0.82540 0.50126 0.59340 -0.06423 0.09683  -0.18169 40  LYS B CA  
2513 C C   . LYS B 40  ? 0.85275 0.56343 0.61065 -0.04054 0.11821  -0.19061 40  LYS B C   
2514 O O   . LYS B 40  ? 0.89060 0.66188 0.67283 -0.02724 0.11090  -0.16197 40  LYS B O   
2515 C CB  . LYS B 40  ? 0.94317 0.54102 0.73162 -0.04205 0.11646  -0.19353 40  LYS B CB  
2516 C CG  . LYS B 40  ? 0.99334 0.55624 0.80223 -0.06131 0.09848  -0.17306 40  LYS B CG  
2517 C CD  . LYS B 40  ? 0.90892 0.38540 0.73571 -0.03298 0.11798  -0.17958 40  LYS B CD  
2518 C CE  . LYS B 40  ? 0.95397 0.34660 0.74511 -0.06793 0.11435  -0.20485 40  LYS B CE  
2519 N NZ  . LYS B 40  ? 1.01915 0.38643 0.82701 -0.09819 0.09530  -0.17383 40  LYS B NZ  
2520 N N   . ASP B 41  ? 1.03056 0.69921 0.75145 -0.03620 0.14829  -0.23243 41  ASP B N   
2521 C CA  . ASP B 41  ? 1.01454 0.72637 0.73618 -0.01361 0.17296  -0.23814 41  ASP B CA  
2522 C C   . ASP B 41  ? 0.93134 0.66385 0.72711 0.03509  0.18847  -0.21857 41  ASP B C   
2523 O O   . ASP B 41  ? 0.88045 0.67354 0.69662 0.04824  0.19600  -0.20330 41  ASP B O   
2524 C CB  . ASP B 41  ? 1.03921 0.72996 0.72096 -0.01899 0.19006  -0.27280 41  ASP B CB  
2525 C CG  . ASP B 41  ? 1.20034 0.94688 0.84594 -0.03051 0.19742  -0.27298 41  ASP B CG  
2526 O OD1 . ASP B 41  ? 1.13368 0.91171 0.74508 -0.06206 0.17311  -0.25479 41  ASP B OD1 
2527 O OD2 . ASP B 41  ? 1.27355 1.03395 0.92623 -0.00797 0.22583  -0.28795 41  ASP B OD2 
2528 N N   . GLU B 42  ? 0.93141 0.61768 0.76784 0.05813  0.18814  -0.21389 42  GLU B N   
2529 C CA  . GLU B 42  ? 0.78032 0.49267 0.68822 0.10135  0.19162  -0.18767 42  GLU B CA  
2530 C C   . GLU B 42  ? 0.73216 0.49554 0.66768 0.10252  0.17453  -0.14890 42  GLU B C   
2531 O O   . GLU B 42  ? 0.62108 0.42672 0.60717 0.13106  0.17682  -0.12756 42  GLU B O   
2532 C CB  . GLU B 42  ? 0.76816 0.41539 0.70272 0.11871  0.18541  -0.18319 42  GLU B CB  
2533 C CG  . GLU B 42  ? 0.85872 0.53013 0.85967 0.16444  0.18693  -0.16317 42  GLU B CG  
2534 C CD  . GLU B 42  ? 0.85768 0.45624 0.87206 0.18333  0.18432  -0.16768 42  GLU B CD  
2535 O OE1 . GLU B 42  ? 0.92999 0.46747 0.92636 0.16270  0.16908  -0.15824 42  GLU B OE1 
2536 O OE2 . GLU B 42  ? 0.88617 0.48804 0.92973 0.21837  0.19758  -0.17985 42  GLU B OE2 
2537 N N   . GLY B 43  ? 0.75139 0.52727 0.65977 0.06931  0.14764  -0.13388 43  GLY B N   
2538 C CA  . GLY B 43  ? 0.58731 0.41020 0.52066 0.06901  0.12435  -0.09544 43  GLY B CA  
2539 C C   . GLY B 43  ? 0.64277 0.45013 0.56790 0.04506  0.10093  -0.08079 43  GLY B C   
2540 O O   . GLY B 43  ? 0.69911 0.47868 0.59246 0.01766  0.09607  -0.09840 43  GLY B O   
2541 N N   . ALA B 44  ? 0.53081 0.36061 0.48399 0.05249  0.08715  -0.04909 44  ALA B N   
2542 C CA  . ALA B 44  ? 0.52660 0.35938 0.48015 0.03164  0.07006  -0.03208 44  ALA B CA  
2543 C C   . ALA B 44  ? 0.63398 0.42560 0.60589 0.03620  0.07046  -0.01770 44  ALA B C   
2544 O O   . ALA B 44  ? 0.63292 0.42009 0.62636 0.06170  0.07364  -0.00204 44  ALA B O   
2545 C CB  . ALA B 44  ? 0.51897 0.40439 0.48147 0.03457  0.05888  -0.00931 44  ALA B CB  
2546 N N   . VAL B 45  ? 0.64753 0.41055 0.61002 0.00790  0.06464  -0.01989 45  VAL B N   
2547 C CA  . VAL B 45  ? 0.61904 0.33767 0.59187 0.00217  0.06369  -0.00151 45  VAL B CA  
2548 C C   . VAL B 45  ? 0.63121 0.39820 0.61585 -0.01427 0.05461  0.02688  45  VAL B C   
2549 O O   . VAL B 45  ? 0.61577 0.41603 0.60055 -0.04213 0.04735  0.02419  45  VAL B O   
2550 C CB  . VAL B 45  ? 0.73820 0.38686 0.69044 -0.02533 0.06557  -0.02319 45  VAL B CB  
2551 C CG1 . VAL B 45  ? 0.65062 0.23775 0.61087 -0.02959 0.06545  -0.00022 45  VAL B CG1 
2552 C CG2 . VAL B 45  ? 0.66575 0.27136 0.59755 -0.00988 0.08069  -0.06185 45  VAL B CG2 
2553 N N   . PHE B 46  ? 0.61869 0.39368 0.61362 0.00239  0.05543  0.05407  46  PHE B N   
2554 C CA  . PHE B 46  ? 0.60422 0.42606 0.60440 -0.00871 0.05429  0.07737  46  PHE B CA  
2555 C C   . PHE B 46  ? 0.66171 0.45747 0.66177 -0.03959 0.05571  0.09543  46  PHE B C   
2556 O O   . PHE B 46  ? 0.72551 0.45508 0.71874 -0.05091 0.05464  0.09147  46  PHE B O   
2557 C CB  . PHE B 46  ? 0.55534 0.39544 0.55263 0.01724  0.05444  0.09479  46  PHE B CB  
2558 C CG  . PHE B 46  ? 0.46340 0.34596 0.46047 0.03382  0.05332  0.08168  46  PHE B CG  
2559 C CD1 . PHE B 46  ? 0.49804 0.37345 0.49730 0.04944  0.05269  0.06373  46  PHE B CD1 
2560 C CD2 . PHE B 46  ? 0.50905 0.43528 0.50303 0.03278  0.05576  0.08647  46  PHE B CD2 
2561 C CE1 . PHE B 46  ? 0.46050 0.36991 0.45585 0.05817  0.05134  0.05545  46  PHE B CE1 
2562 C CE2 . PHE B 46  ? 0.42931 0.37996 0.41942 0.04611  0.05371  0.07582  46  PHE B CE2 
2563 C CZ  . PHE B 46  ? 0.55033 0.49174 0.53950 0.05594  0.04983  0.06251  46  PHE B CZ  
2564 N N   . PRO B 47  ? 0.58811 0.43266 0.59520 -0.05620 0.06078  0.11408  47  PRO B N   
2565 C CA  . PRO B 47  ? 0.67041 0.49541 0.67696 -0.09166 0.06495  0.13578  47  PRO B CA  
2566 C C   . PRO B 47  ? 0.77895 0.53608 0.76457 -0.08512 0.06379  0.16060  47  PRO B C   
2567 O O   . PRO B 47  ? 0.80016 0.50894 0.77856 -0.11513 0.06403  0.17776  47  PRO B O   
2568 C CB  . PRO B 47  ? 0.52244 0.42746 0.54245 -0.10073 0.07751  0.14992  47  PRO B CB  
2569 C CG  . PRO B 47  ? 0.46125 0.42069 0.49783 -0.07792 0.07492  0.12810  47  PRO B CG  
2570 C CD  . PRO B 47  ? 0.62167 0.53965 0.63899 -0.04587 0.06635  0.11455  47  PRO B CD  
2571 N N   . ASP B 48  ? 0.75810 0.51142 0.73475 -0.04874 0.05988  0.16645  48  ASP B N   
2572 C CA  . ASP B 48  ? 0.82351 0.51116 0.78955 -0.03252 0.05152  0.18899  48  ASP B CA  
2573 C C   . ASP B 48  ? 0.88162 0.48955 0.85532 -0.03049 0.04890  0.17320  48  ASP B C   
2574 O O   . ASP B 48  ? 0.98957 0.53235 0.95512 -0.02565 0.04054  0.19259  48  ASP B O   
2575 C CB  . ASP B 48  ? 0.63681 0.34817 0.60488 0.00697  0.04352  0.19032  48  ASP B CB  
2576 C CG  . ASP B 48  ? 0.76909 0.46381 0.71733 0.01417  0.02882  0.22303  48  ASP B CG  
2577 O OD1 . ASP B 48  ? 0.80021 0.45266 0.72811 -0.00782 0.02617  0.24250  48  ASP B OD1 
2578 O OD2 . ASP B 48  ? 0.78396 0.51124 0.73103 0.03677  0.01709  0.22456  48  ASP B OD2 
2579 N N   . GLY B 49  ? 0.84037 0.45294 0.82189 -0.03569 0.05272  0.13453  49  GLY B N   
2580 C CA  . GLY B 49  ? 0.72682 0.26726 0.70869 -0.02205 0.05483  0.10784  49  GLY B CA  
2581 C C   . GLY B 49  ? 0.74243 0.28545 0.74083 0.02857  0.05618  0.10184  49  GLY B C   
2582 O O   . GLY B 49  ? 0.81276 0.30262 0.81691 0.04929  0.06104  0.08029  49  GLY B O   
2583 N N   . THR B 50  ? 0.77797 0.38961 0.78495 0.04690  0.05100  0.11811  50  THR B N   
2584 C CA  . THR B 50  ? 0.71944 0.35624 0.74847 0.08757  0.05063  0.11242  50  THR B CA  
2585 C C   . THR B 50  ? 0.59536 0.26499 0.62517 0.08957  0.06160  0.07185  50  THR B C   
2586 O O   . THR B 50  ? 0.54279 0.25792 0.55853 0.06757  0.06089  0.06214  50  THR B O   
2587 C CB  . THR B 50  ? 0.67445 0.37224 0.70286 0.09467  0.03827  0.14063  50  THR B CB  
2588 O OG1 . THR B 50  ? 0.73829 0.41563 0.75175 0.08545  0.02299  0.17273  50  THR B OG1 
2589 C CG2 . THR B 50  ? 0.61739 0.35871 0.67173 0.12555  0.03256  0.13188  50  THR B CG2 
2590 N N   . LEU B 51  ? 0.62369 0.27049 0.66978 0.11687  0.07299  0.04957  51  LEU B N   
2591 C CA  . LEU B 51  ? 0.59584 0.27836 0.63642 0.11806  0.08542  0.01480  51  LEU B CA  
2592 C C   . LEU B 51  ? 0.52772 0.28254 0.59063 0.13804  0.08188  0.02655  51  LEU B C   
2593 O O   . LEU B 51  ? 0.60682 0.37580 0.70204 0.16443  0.07642  0.04305  51  LEU B O   
2594 C CB  . LEU B 51  ? 0.61789 0.24756 0.65915 0.13413  0.10549  -0.02013 51  LEU B CB  
2595 C CG  . LEU B 51  ? 0.67368 0.32182 0.68188 0.11442  0.11853  -0.05909 51  LEU B CG  
2596 C CD1 . LEU B 51  ? 0.74980 0.31726 0.72580 0.10145  0.13308  -0.09705 51  LEU B CD1 
2597 C CD2 . LEU B 51  ? 0.71608 0.42272 0.74357 0.13943  0.13300  -0.06887 51  LEU B CD2 
2598 N N   . VAL B 52  ? 0.53505 0.33985 0.58005 0.12006  0.07925  0.01963  52  VAL B N   
2599 C CA  . VAL B 52  ? 0.50400 0.36879 0.56229 0.13029  0.07725  0.02513  52  VAL B CA  
2600 C C   . VAL B 52  ? 0.54355 0.42236 0.59709 0.13187  0.09588  -0.00547 52  VAL B C   
2601 O O   . VAL B 52  ? 0.48593 0.36497 0.50541 0.10899  0.09784  -0.02220 52  VAL B O   
2602 C CB  . VAL B 52  ? 0.52375 0.42235 0.56096 0.11068  0.06379  0.03877  52  VAL B CB  
2603 C CG1 . VAL B 52  ? 0.41599 0.36278 0.46054 0.11506  0.06126  0.04168  52  VAL B CG1 
2604 C CG2 . VAL B 52  ? 0.44329 0.32986 0.47708 0.10699  0.05157  0.06619  52  VAL B CG2 
2605 N N   . GLU B 53  ? 0.56776 0.46275 0.65658 0.15888  0.10977  -0.01084 53  GLU B N   
2606 C CA  . GLU B 53  ? 0.57047 0.47818 0.65478 0.16241  0.13587  -0.04234 53  GLU B CA  
2607 C C   . GLU B 53  ? 0.54489 0.49889 0.59927 0.13587  0.13352  -0.04426 53  GLU B C   
2608 O O   . GLU B 53  ? 0.38877 0.37132 0.44174 0.12456  0.11394  -0.02098 53  GLU B O   
2609 C CB  . GLU B 53  ? 0.50213 0.44398 0.63967 0.19150  0.14366  -0.04192 53  GLU B CB  
2610 C CG  . GLU B 53  ? 0.61243 0.50262 0.76707 0.21377  0.14490  -0.05095 53  GLU B CG  
2611 C CD  . GLU B 53  ? 0.74025 0.62537 0.92940 0.23012  0.11818  -0.01459 53  GLU B CD  
2612 O OE1 . GLU B 53  ? 0.68902 0.59721 0.87505 0.21775  0.09789  0.01508  53  GLU B OE1 
2613 O OE2 . GLU B 53  ? 0.69459 0.55096 0.90848 0.25523  0.11693  -0.01569 53  GLU B OE2 
2614 N N   . ARG B 54  ? 0.49473 0.44798 0.51789 0.12462  0.15430  -0.07290 54  ARG B N   
2615 C CA  . ARG B 54  ? 0.47224 0.45847 0.45823 0.09695  0.15098  -0.07141 54  ARG B CA  
2616 C C   . ARG B 54  ? 0.43422 0.47847 0.45037 0.09860  0.14829  -0.05009 54  ARG B C   
2617 O O   . ARG B 54  ? 0.40633 0.46258 0.40261 0.07881  0.12965  -0.03179 54  ARG B O   
2618 C CB  . ARG B 54  ? 0.52667 0.50600 0.47072 0.08486  0.17738  -0.10478 54  ARG B CB  
2619 C CG  . ARG B 54  ? 0.59311 0.58437 0.47978 0.04984  0.16562  -0.10009 54  ARG B CG  
2620 C CD  . ARG B 54  ? 0.67716 0.62914 0.50461 0.02843  0.16790  -0.12727 54  ARG B CD  
2621 N NE  . ARG B 54  ? 0.80241 0.75812 0.59058 -0.00028 0.13664  -0.10834 54  ARG B NE  
2622 C CZ  . ARG B 54  ? 0.88904 0.81990 0.66513 -0.01336 0.11266  -0.10659 54  ARG B CZ  
2623 N NH1 . ARG B 54  ? 0.82193 0.71283 0.61144 -0.00740 0.11642  -0.12364 54  ARG B NH1 
2624 N NH2 . ARG B 54  ? 0.83674 0.78438 0.59157 -0.03289 0.08354  -0.08449 54  ARG B NH2 
2625 N N   . GLU B 55  ? 0.42750 0.50789 0.49452 0.12173  0.16644  -0.05220 55  GLU B N   
2626 C CA  . GLU B 55  ? 0.43726 0.58309 0.53587 0.11562  0.16481  -0.03389 55  GLU B CA  
2627 C C   . GLU B 55  ? 0.39394 0.54213 0.49978 0.10814  0.13026  -0.00372 55  GLU B C   
2628 O O   . GLU B 55  ? 0.30341 0.47575 0.39622 0.08382  0.11927  0.00970  55  GLU B O   
2629 C CB  . GLU B 55  ? 0.34383 0.53957 0.51098 0.14548  0.18847  -0.03979 55  GLU B CB  
2630 C CG  . GLU B 55  ? 0.65346 0.82278 0.81052 0.15859  0.21257  -0.07700 55  GLU B CG  
2631 C CD  . GLU B 55  ? 0.69472 0.78754 0.84186 0.17750  0.20272  -0.08583 55  GLU B CD  
2632 O OE1 . GLU B 55  ? 0.64829 0.69110 0.74578 0.16977  0.21502  -0.11369 55  GLU B OE1 
2633 O OE2 . GLU B 55  ? 0.74883 0.83145 0.93369 0.19565  0.18095  -0.06275 55  GLU B OE2 
2634 N N   . VAL B 56  ? 0.35040 0.46606 0.46828 0.12536  0.11405  0.00618  56  VAL B N   
2635 C CA  . VAL B 56  ? 0.39786 0.50874 0.50756 0.11605  0.08474  0.03058  56  VAL B CA  
2636 C C   . VAL B 56  ? 0.37922 0.46016 0.43358 0.09103  0.07533  0.02927  56  VAL B C   
2637 O O   . VAL B 56  ? 0.38455 0.47181 0.42269 0.07497  0.06064  0.04128  56  VAL B O   
2638 C CB  . VAL B 56  ? 0.36765 0.44760 0.49367 0.13700  0.07333  0.04288  56  VAL B CB  
2639 C CG1 . VAL B 56  ? 0.31606 0.39510 0.42477 0.12499  0.04701  0.06627  56  VAL B CG1 
2640 C CG2 . VAL B 56  ? 0.39748 0.50303 0.58410 0.16847  0.08077  0.04777  56  VAL B CG2 
2641 N N   . LEU B 57  ? 0.38339 0.43001 0.40925 0.08777  0.08251  0.01454  57  LEU B N   
2642 C CA  . LEU B 57  ? 0.41123 0.43906 0.39632 0.06951  0.07209  0.01670  57  LEU B CA  
2643 C C   . LEU B 57  ? 0.37488 0.42057 0.33993 0.05112  0.07231  0.02049  57  LEU B C   
2644 O O   . LEU B 57  ? 0.39948 0.43127 0.34277 0.04116  0.05866  0.03166  57  LEU B O   
2645 C CB  . LEU B 57  ? 0.39646 0.39852 0.35951 0.06472  0.07654  0.00152  57  LEU B CB  
2646 C CG  . LEU B 57  ? 0.44226 0.41543 0.41361 0.07094  0.07244  0.00041  57  LEU B CG  
2647 C CD1 . LEU B 57  ? 0.39249 0.34734 0.33680 0.05453  0.07129  -0.01426 57  LEU B CD1 
2648 C CD2 . LEU B 57  ? 0.40977 0.38284 0.38615 0.07251  0.05811  0.02058  57  LEU B CD2 
2649 N N   . GLU B 58  ? 0.37921 0.45191 0.34962 0.04616  0.09027  0.01121  58  GLU B N   
2650 C CA  . GLU B 58  ? 0.40103 0.48995 0.34897 0.02226  0.09196  0.01873  58  GLU B CA  
2651 C C   . GLU B 58  ? 0.36373 0.47154 0.33128 0.01369  0.08010  0.03507  58  GLU B C   
2652 O O   . GLU B 58  ? 0.33484 0.42720 0.27357 -0.00832 0.06986  0.04655  58  GLU B O   
2653 C CB  . GLU B 58  ? 0.41808 0.53962 0.36594 0.01604  0.12022  0.00381  58  GLU B CB  
2654 C CG  . GLU B 58  ? 0.42819 0.52450 0.34237 0.01804  0.13199  -0.01808 58  GLU B CG  
2655 C CD  . GLU B 58  ? 0.43156 0.55716 0.34005 0.01438  0.16682  -0.03963 58  GLU B CD  
2656 O OE1 . GLU B 58  ? 0.42510 0.59775 0.38255 0.02539  0.18636  -0.04113 58  GLU B OE1 
2657 O OE2 . GLU B 58  ? 0.56019 0.66667 0.41528 -0.00025 0.17527  -0.05547 58  GLU B OE2 
2658 N N   . LYS B 59  ? 0.35296 0.49033 0.36692 0.02902  0.07878  0.03757  59  LYS B N   
2659 C CA  . LYS B 59  ? 0.39142 0.55009 0.42014 0.01575  0.06158  0.05295  59  LYS B CA  
2660 C C   . LYS B 59  ? 0.37726 0.48368 0.36436 0.00809  0.04084  0.05881  59  LYS B C   
2661 O O   . LYS B 59  ? 0.36871 0.46240 0.33222 -0.01631 0.02984  0.06529  59  LYS B O   
2662 C CB  . LYS B 59  ? 0.38098 0.58251 0.46713 0.03696  0.05774  0.05922  59  LYS B CB  
2663 C CG  . LYS B 59  ? 0.44847 0.68748 0.55278 0.01755  0.03586  0.07627  59  LYS B CG  
2664 C CD  . LYS B 59  ? 0.40833 0.63320 0.51289 0.02994  0.01156  0.08824  59  LYS B CD  
2665 C CE  . LYS B 59  ? 0.40451 0.66241 0.56825 0.06516  0.01448  0.09586  59  LYS B CE  
2666 N NZ  . LYS B 59  ? 0.55204 0.80470 0.71727 0.07403  -0.01230 0.11597  59  LYS B NZ  
2667 N N   . ILE B 60  ? 0.38799 0.46181 0.36530 0.02755  0.03790  0.05516  60  ILE B N   
2668 C CA  . ILE B 60  ? 0.42432 0.45488 0.36631 0.02511  0.02592  0.05741  60  ILE B CA  
2669 C C   . ILE B 60  ? 0.41382 0.41028 0.32096 0.01456  0.02642  0.05656  60  ILE B C   
2670 O O   . ILE B 60  ? 0.44146 0.40624 0.32072 0.00206  0.01806  0.05937  60  ILE B O   
2671 C CB  . ILE B 60  ? 0.39695 0.41225 0.34278 0.04560  0.02707  0.05578  60  ILE B CB  
2672 C CG1 . ILE B 60  ? 0.37048 0.40812 0.34262 0.05429  0.02100  0.06442  60  ILE B CG1 
2673 C CG2 . ILE B 60  ? 0.45019 0.42942 0.36402 0.04649  0.02326  0.05490  60  ILE B CG2 
2674 C CD1 . ILE B 60  ? 0.40687 0.43413 0.39473 0.07250  0.02696  0.06503  60  ILE B CD1 
2675 N N   . ALA B 61  ? 0.38159 0.37919 0.28590 0.01833  0.03456  0.05339  61  ALA B N   
2676 C CA  . ALA B 61  ? 0.37185 0.34051 0.24351 0.00896  0.03015  0.05985  61  ALA B CA  
2677 C C   . ALA B 61  ? 0.45294 0.41154 0.30476 -0.01710 0.02712  0.06908  61  ALA B C   
2678 O O   . ALA B 61  ? 0.49936 0.41390 0.31983 -0.02399 0.01850  0.07901  61  ALA B O   
2679 C CB  . ALA B 61  ? 0.39323 0.37558 0.25792 0.00750  0.03691  0.05642  61  ALA B CB  
2680 N N   . ARG B 62  ? 0.63973 0.61979 0.28878 -0.15376 0.18368  -0.05732 62  ARG B N   
2681 C CA  . ARG B 62  ? 0.69162 0.63452 0.31797 -0.18203 0.20288  -0.06451 62  ARG B CA  
2682 C C   . ARG B 62  ? 0.68802 0.60969 0.31341 -0.17603 0.20248  -0.05668 62  ARG B C   
2683 O O   . ARG B 62  ? 0.77130 0.64389 0.35863 -0.19776 0.21601  -0.05666 62  ARG B O   
2684 C CB  . ARG B 62  ? 0.67070 0.66079 0.35544 -0.20965 0.22169  -0.10081 62  ARG B CB  
2685 C CG  . ARG B 62  ? 0.73111 0.70096 0.38410 -0.23986 0.23786  -0.11235 62  ARG B CG  
2686 C CD  . ARG B 62  ? 0.72244 0.73514 0.43078 -0.26930 0.25807  -0.15094 62  ARG B CD  
2687 N NE  . ARG B 62  ? 0.64376 0.73195 0.44062 -0.25260 0.25191  -0.17374 62  ARG B NE  
2688 C CZ  . ARG B 62  ? 0.61708 0.74259 0.45007 -0.24448 0.24984  -0.18802 62  ARG B CZ  
2689 N NH1 . ARG B 62  ? 0.65029 0.75187 0.44110 -0.24952 0.25092  -0.17967 62  ARG B NH1 
2690 N NH2 . ARG B 62  ? 0.56194 0.74724 0.47266 -0.22930 0.24528  -0.21133 62  ARG B NH2 
2691 N N   . ASP B 63  ? 0.62603 0.57994 0.28925 -0.15005 0.18872  -0.05196 63  ASP B N   
2692 C CA  . ASP B 63  ? 0.64452 0.59742 0.32671 -0.14814 0.19053  -0.05388 63  ASP B CA  
2693 C C   . ASP B 63  ? 0.63652 0.55279 0.28078 -0.11620 0.17334  -0.02446 63  ASP B C   
2694 O O   . ASP B 63  ? 0.64494 0.60150 0.33893 -0.08778 0.15167  -0.02037 63  ASP B O   
2695 C CB  . ASP B 63  ? 0.67351 0.70476 0.44257 -0.14557 0.18934  -0.07984 63  ASP B CB  
2696 C CG  . ASP B 63  ? 0.68321 0.72291 0.47819 -0.14294 0.18678  -0.08397 63  ASP B CG  
2697 O OD1 . ASP B 63  ? 0.72738 0.71264 0.47249 -0.15396 0.19557  -0.07381 63  ASP B OD1 
2698 O OD2 . ASP B 63  ? 0.57187 0.66813 0.43660 -0.12817 0.17283  -0.09707 63  ASP B OD2 
2699 N N   . ASP B 64  ? 0.68807 0.53037 0.26456 -0.11361 0.17356  -0.00411 64  ASP B N   
2700 C CA  . ASP B 64  ? 0.70267 0.50953 0.24669 -0.07690 0.15530  0.02252  64  ASP B CA  
2701 C C   . ASP B 64  ? 0.78761 0.58815 0.35472 -0.07065 0.15603  0.02056  64  ASP B C   
2702 O O   . ASP B 64  ? 0.72511 0.48368 0.26267 -0.04273 0.14510  0.03990  64  ASP B O   
2703 C CB  . ASP B 64  ? 0.79289 0.52545 0.26077 -0.06638 0.14872  0.04546  64  ASP B CB  
2704 C CG  . ASP B 64  ? 0.90841 0.56606 0.33117 -0.08488 0.16535  0.04603  64  ASP B CG  
2705 O OD1 . ASP B 64  ? 0.89225 0.55958 0.34256 -0.11166 0.18324  0.02656  64  ASP B OD1 
2706 O OD2 . ASP B 64  ? 0.96301 0.54968 0.31924 -0.07278 0.15975  0.06463  64  ASP B OD2 
2707 N N   . GLY B 65  ? 0.70240 0.54732 0.32431 -0.09359 0.16663  -0.00394 65  GLY B N   
2708 C CA  . GLY B 65  ? 0.63086 0.46977 0.26976 -0.09198 0.16648  -0.00759 65  GLY B CA  
2709 C C   . GLY B 65  ? 0.62367 0.53686 0.34483 -0.07945 0.14973  -0.02009 65  GLY B C   
2710 O O   . GLY B 65  ? 0.70340 0.62023 0.44165 -0.08264 0.14900  -0.02701 65  GLY B O   
2711 N N   . THR B 66  ? 0.52424 0.49007 0.28948 -0.06574 0.13609  -0.02273 66  THR B N   
2712 C CA  . THR B 66  ? 0.46994 0.49483 0.30335 -0.05469 0.12109  -0.03413 66  THR B CA  
2713 C C   . THR B 66  ? 0.56576 0.61064 0.41733 -0.02625 0.10170  -0.02119 66  THR B C   
2714 O O   . THR B 66  ? 0.49812 0.53937 0.33049 -0.02213 0.10084  -0.01401 66  THR B O   
2715 C CB  . THR B 66  ? 0.52051 0.59560 0.39898 -0.07507 0.12976  -0.06171 66  THR B CB  
2716 O OG1 . THR B 66  ? 0.63565 0.69382 0.48938 -0.10981 0.15424  -0.07678 66  THR B OG1 
2717 C CG2 . THR B 66  ? 0.63267 0.75396 0.56945 -0.06355 0.11365  -0.07361 66  THR B CG2 
2718 N N   . VAL B 67  ? 0.46993 0.53466 0.35371 -0.01012 0.08707  -0.01952 67  VAL B N   
2719 C CA  . VAL B 67  ? 0.40287 0.48973 0.30762 0.00946  0.07228  -0.01251 67  VAL B CA  
2720 C C   . VAL B 67  ? 0.40055 0.52463 0.34903 0.00652  0.06815  -0.02852 67  VAL B C   
2721 O O   . VAL B 67  ? 0.38233 0.52235 0.35665 0.00092  0.06745  -0.04227 67  VAL B O   
2722 C CB  . VAL B 67  ? 0.48931 0.56785 0.39469 0.02571  0.06245  -0.00204 67  VAL B CB  
2723 C CG1 . VAL B 67  ? 0.39436 0.49819 0.32386 0.03730  0.05116  -0.00022 67  VAL B CG1 
2724 C CG2 . VAL B 67  ? 0.48599 0.52891 0.35121 0.03653  0.06585  0.01263  67  VAL B CG2 
2725 N N   . TYR B 68  ? 0.39590 0.53415 0.35194 0.01128  0.06486  -0.02855 68  TYR B N   
2726 C CA  . TYR B 68  ? 0.37201 0.53407 0.36328 0.01300  0.06131  -0.04260 68  TYR B CA  
2727 C C   . TYR B 68  ? 0.31819 0.47885 0.31230 0.02486  0.05059  -0.03412 68  TYR B C   
2728 O O   . TYR B 68  ? 0.27797 0.43333 0.25295 0.02888  0.04807  -0.02150 68  TYR B O   
2729 C CB  . TYR B 68  ? 0.43794 0.61302 0.43111 0.00010  0.07375  -0.05657 68  TYR B CB  
2730 C CG  . TYR B 68  ? 0.39016 0.56932 0.38088 -0.01858 0.08980  -0.07029 68  TYR B CG  
2731 C CD1 . TYR B 68  ? 0.55137 0.70193 0.49664 -0.03157 0.10022  -0.06036 68  TYR B CD1 
2732 C CD2 . TYR B 68  ? 0.41031 0.62068 0.44194 -0.02368 0.09590  -0.09504 68  TYR B CD2 
2733 C CE1 . TYR B 68  ? 0.47142 0.61899 0.40602 -0.05618 0.11986  -0.07460 68  TYR B CE1 
2734 C CE2 . TYR B 68  ? 0.45510 0.67749 0.48781 -0.04672 0.11471  -0.11273 68  TYR B CE2 
2735 C CZ  . TYR B 68  ? 0.50042 0.68860 0.48151 -0.06638 0.12837  -0.10229 68  TYR B CZ  
2736 O OH  . TYR B 68  ? 0.55996 0.75291 0.53391 -0.09614 0.15140  -0.12105 68  TYR B OH  
2737 N N   . PHE B 69  ? 0.31149 0.47585 0.32833 0.03074  0.04477  -0.04257 69  PHE B N   
2738 C CA  . PHE B 69  ? 0.36254 0.51772 0.37439 0.03451  0.03992  -0.03756 69  PHE B CA  
2739 C C   . PHE B 69  ? 0.42196 0.57382 0.45013 0.03694  0.04050  -0.05153 69  PHE B C   
2740 O O   . PHE B 69  ? 0.39634 0.55584 0.44727 0.04353  0.03950  -0.06429 69  PHE B O   
2741 C CB  . PHE B 69  ? 0.34332 0.48073 0.34559 0.04166  0.03105  -0.02594 69  PHE B CB  
2742 C CG  . PHE B 69  ? 0.41996 0.54774 0.43209 0.05111  0.02074  -0.02864 69  PHE B CG  
2743 C CD1 . PHE B 69  ? 0.35633 0.49068 0.37039 0.05075  0.01872  -0.02834 69  PHE B CD1 
2744 C CD2 . PHE B 69  ? 0.37574 0.48454 0.39021 0.06066  0.01182  -0.03165 69  PHE B CD2 
2745 C CE1 . PHE B 69  ? 0.43759 0.57215 0.46208 0.05878  0.00598  -0.03306 69  PHE B CE1 
2746 C CE2 . PHE B 69  ? 0.39581 0.49863 0.41724 0.07413  -0.00308 -0.03356 69  PHE B CE2 
2747 C CZ  . PHE B 69  ? 0.38065 0.50234 0.41002 0.07278  -0.00718 -0.03514 69  PHE B CZ  
2748 N N   . VAL B 70  ? 0.40402 0.54597 0.42123 0.03137  0.04314  -0.05162 70  VAL B N   
2749 C CA  . VAL B 70  ? 0.42751 0.55149 0.45041 0.03370  0.04556  -0.06406 70  VAL B CA  
2750 C C   . VAL B 70  ? 0.46458 0.55118 0.46721 0.03616  0.03987  -0.05524 70  VAL B C   
2751 O O   . VAL B 70  ? 0.51154 0.59831 0.49621 0.02297  0.04342  -0.04780 70  VAL B O   
2752 C CB  . VAL B 70  ? 0.37381 0.50985 0.39225 0.01779  0.05815  -0.07600 70  VAL B CB  
2753 C CG1 . VAL B 70  ? 0.39224 0.55118 0.39403 0.00476  0.05905  -0.06672 70  VAL B CG1 
2754 C CG2 . VAL B 70  ? 0.51885 0.62240 0.52792 0.01456  0.06283  -0.08523 70  VAL B CG2 
2755 N N   . SER B 71  ? 0.42803 0.48336 0.43168 0.05347  0.03070  -0.05674 71  SER B N   
2756 C CA  . SER B 71  ? 0.59955 0.60180 0.57069 0.05535  0.02641  -0.04831 71  SER B CA  
2757 C C   . SER B 71  ? 0.64566 0.61047 0.61821 0.07637  0.02045  -0.05774 71  SER B C   
2758 O O   . SER B 71  ? 0.60238 0.59245 0.60942 0.09597  0.01331  -0.06878 71  SER B O   
2759 C CB  . SER B 71  ? 0.65047 0.63959 0.60457 0.06144  0.01408  -0.03198 71  SER B CB  
2760 O OG  . SER B 71  ? 0.58001 0.54899 0.53727 0.08717  -0.00431 -0.03120 71  SER B OG  
2761 N N   . ASN B 72  ? 0.70427 0.60752 0.63809 0.07210  0.02463  -0.05517 72  ASN B N   
2762 C CA  . ASN B 72  ? 0.64700 0.49904 0.57257 0.09497  0.02034  -0.06384 72  ASN B CA  
2763 C C   . ASN B 72  ? 0.55714 0.44683 0.52455 0.10000  0.03022  -0.08699 72  ASN B C   
2764 O O   . ASN B 72  ? 0.65721 0.54049 0.64708 0.13000  0.02230  -0.09934 72  ASN B O   
2765 C CB  . ASN B 72  ? 0.69289 0.52049 0.61529 0.13096  -0.00586 -0.05469 72  ASN B CB  
2766 C CG  . ASN B 72  ? 0.89447 0.69247 0.77410 0.12294  -0.01517 -0.03230 72  ASN B CG  
2767 O OD1 . ASN B 72  ? 0.87807 0.71656 0.77509 0.12709  -0.02721 -0.02569 72  ASN B OD1 
2768 N ND2 . ASN B 72  ? 0.97222 0.69595 0.79133 0.10771  -0.00675 -0.02245 72  ASN B ND2 
2769 N N   . GLY B 73  ? 0.56881 0.50049 0.54602 0.07114  0.04734  -0.09427 73  GLY B N   
2770 C CA  . GLY B 73  ? 0.59681 0.56123 0.60272 0.06768  0.06063  -0.11633 73  GLY B CA  
2771 C C   . GLY B 73  ? 0.47412 0.49652 0.52658 0.08153  0.05613  -0.12563 73  GLY B C   
2772 O O   . GLY B 73  ? 0.44290 0.49196 0.51807 0.07743  0.06986  -0.14659 73  GLY B O   
2773 N N   . GLY B 74  ? 0.40513 0.44774 0.46994 0.09356  0.04008  -0.11342 74  GLY B N   
2774 C CA  . GLY B 74  ? 0.43988 0.53731 0.54746 0.10175  0.03764  -0.12519 74  GLY B CA  
2775 C C   . GLY B 74  ? 0.44132 0.57195 0.54334 0.08004  0.04089  -0.11300 74  GLY B C   
2776 O O   . GLY B 74  ? 0.53640 0.65077 0.61240 0.07464  0.03352  -0.09252 74  GLY B O   
2777 N N   . VAL B 75  ? 0.34844 0.52020 0.47076 0.06760  0.05369  -0.12660 75  VAL B N   
2778 C CA  . VAL B 75  ? 0.43356 0.62585 0.54379 0.04922  0.05793  -0.11574 75  VAL B CA  
2779 C C   . VAL B 75  ? 0.40635 0.62109 0.53983 0.05774  0.04830  -0.11821 75  VAL B C   
2780 O O   . VAL B 75  ? 0.40595 0.64849 0.57796 0.06896  0.04711  -0.13944 75  VAL B O   
2781 C CB  . VAL B 75  ? 0.46926 0.68200 0.57415 0.02676  0.07850  -0.12779 75  VAL B CB  
2782 C CG1 . VAL B 75  ? 0.52721 0.74380 0.60574 0.01103  0.08143  -0.11250 75  VAL B CG1 
2783 C CG2 . VAL B 75  ? 0.37361 0.56943 0.45742 0.01762  0.08618  -0.12985 75  VAL B CG2 
2784 N N   . TYR B 76  ? 0.38521 0.59163 0.49753 0.05264  0.04152  -0.09940 76  TYR B N   
2785 C CA  . TYR B 76  ? 0.37117 0.59371 0.49849 0.05791  0.03083  -0.10101 76  TYR B CA  
2786 C C   . TYR B 76  ? 0.33250 0.55352 0.43547 0.03804  0.04013  -0.09095 76  TYR B C   
2787 O O   . TYR B 76  ? 0.37235 0.57178 0.44264 0.03025  0.04625  -0.07507 76  TYR B O   
2788 C CB  . TYR B 76  ? 0.41297 0.60974 0.53013 0.07765  0.00849  -0.08711 76  TYR B CB  
2789 C CG  . TYR B 76  ? 0.45989 0.63846 0.58657 0.10130  -0.00327 -0.09248 76  TYR B CG  
2790 C CD1 . TYR B 76  ? 0.47875 0.68568 0.64631 0.12205  -0.01339 -0.11328 76  TYR B CD1 
2791 C CD2 . TYR B 76  ? 0.49731 0.62881 0.59073 0.10326  -0.00366 -0.07854 76  TYR B CD2 
2792 C CE1 . TYR B 76  ? 0.53001 0.70984 0.70081 0.15011  -0.02578 -0.11718 76  TYR B CE1 
2793 C CE2 . TYR B 76  ? 0.55459 0.65298 0.64513 0.12421  -0.01246 -0.08243 76  TYR B CE2 
2794 C CZ  . TYR B 76  ? 0.51555 0.63390 0.64277 0.15044  -0.02447 -0.10036 76  TYR B CZ  
2795 O OH  . TYR B 76  ? 0.65424 0.73009 0.77341 0.17709  -0.03455 -0.10322 76  TYR B OH  
2796 N N   . LYS B 77  ? 0.31215 0.55612 0.43066 0.03075  0.04072  -0.10199 77  LYS B N   
2797 C CA  . LYS B 77  ? 0.36629 0.59629 0.45538 0.01274  0.04945  -0.09290 77  LYS B CA  
2798 C C   . LYS B 77  ? 0.36931 0.57709 0.44102 0.02335  0.03329  -0.07604 77  LYS B C   
2799 O O   . LYS B 77  ? 0.30809 0.52646 0.39824 0.03763  0.01512  -0.07995 77  LYS B O   
2800 C CB  . LYS B 77  ? 0.30699 0.56895 0.41569 -0.00779 0.06177  -0.11602 77  LYS B CB  
2801 C CG  . LYS B 77  ? 0.45336 0.73652 0.57343 -0.02557 0.08403  -0.13582 77  LYS B CG  
2802 C CD  . LYS B 77  ? 0.54695 0.86025 0.68053 -0.05433 0.10155  -0.16062 77  LYS B CD  
2803 C CE  . LYS B 77  ? 0.56364 0.82882 0.63809 -0.07962 0.11741  -0.14582 77  LYS B CE  
2804 N NZ  . LYS B 77  ? 0.65935 0.94301 0.74163 -0.10421 0.12552  -0.16444 77  LYS B NZ  
2805 N N   . ALA B 78  ? 0.36659 0.54220 0.40002 0.01813  0.03942  -0.05787 78  ALA B N   
2806 C CA  . ALA B 78  ? 0.34599 0.50008 0.35961 0.02354  0.03018  -0.04528 78  ALA B CA  
2807 C C   . ALA B 78  ? 0.47591 0.63579 0.48801 0.00782  0.03452  -0.05636 78  ALA B C   
2808 O O   . ALA B 78  ? 0.45976 0.59241 0.44034 -0.00434 0.04750  -0.05081 78  ALA B O   
2809 C CB  . ALA B 78  ? 0.38000 0.50435 0.36024 0.02698  0.03638  -0.02647 78  ALA B CB  
2810 N N   . ALA B 79  ? 0.48865 0.68517 0.53552 0.00861  0.02328  -0.07446 79  ALA B N   
2811 C CA  . ALA B 79  ? 0.39690 0.61515 0.45245 -0.01074 0.02679  -0.09255 79  ALA B CA  
2812 C C   . ALA B 79  ? 0.41660 0.67044 0.50297 0.00330  0.00043  -0.10379 79  ALA B C   
2813 O O   . ALA B 79  ? 0.40227 0.66680 0.50952 0.02803  -0.01708 -0.10217 79  ALA B O   
2814 C CB  . ALA B 79  ? 0.37980 0.62579 0.45404 -0.03332 0.04770  -0.11417 79  ALA B CB  
2815 N N   . ILE B 80  ? 0.37675 0.64426 0.46043 -0.01232 -0.00309 -0.11526 80  ILE B N   
2816 C CA  . ILE B 80  ? 0.46668 0.77360 0.57588 -0.00051 -0.03169 -0.12791 80  ILE B CA  
2817 C C   . ILE B 80  ? 0.46920 0.83446 0.61264 -0.02690 -0.02450 -0.16111 80  ILE B C   
2818 O O   . ILE B 80  ? 0.48699 0.83446 0.60544 -0.06050 0.00065  -0.16677 80  ILE B O   
2819 C CB  . ILE B 80  ? 0.48865 0.75747 0.55404 0.00258  -0.04597 -0.11095 80  ILE B CB  
2820 C CG1 . ILE B 80  ? 0.60090 0.81736 0.63358 0.02424  -0.05068 -0.08210 80  ILE B CG1 
2821 C CG2 . ILE B 80  ? 0.57001 0.88224 0.65527 0.01116  -0.07770 -0.12604 80  ILE B CG2 
2822 C CD1 . ILE B 80  ? 0.57050 0.79432 0.62143 0.05522  -0.07492 -0.07810 80  ILE B CD1 
2823 N N   . ALA B 81  ? 0.52877 0.96276 0.72811 -0.01193 -0.04575 -0.18483 81  ALA B N   
2824 C CA  . ALA B 81  ? 0.41295 0.92154 0.65639 -0.03718 -0.04200 -0.22310 81  ALA B CA  
2825 C C   . ALA B 81  ? 0.48815 1.03927 0.74830 -0.02127 -0.08082 -0.23299 81  ALA B C   
2826 O O   . ALA B 81  ? 0.55895 1.15539 0.86173 0.01542  -0.11198 -0.24140 81  ALA B O   
2827 C CB  . ALA B 81  ? 0.41056 0.98183 0.71635 -0.03440 -0.03150 -0.25104 81  ALA B CB  
2828 N N   . GLY B 82  ? 0.50417 1.03777 0.72699 -0.04747 -0.07990 -0.23260 82  GLY B N   
2829 C CA  . GLY B 82  ? 0.49114 1.06417 0.72044 -0.03920 -0.11609 -0.24321 82  GLY B CA  
2830 C C   . GLY B 82  ? 0.45460 1.09951 0.71801 -0.07725 -0.10716 -0.28338 82  GLY B C   
2831 O O   . GLY B 82  ? 0.49855 1.15557 0.77500 -0.11257 -0.06980 -0.30254 82  GLY B O   
2832 N N   . GLU B 83  ? 0.43139 1.10147 0.69418 -0.06819 -0.13617 -0.28841 83  GLU B N   
2833 C CA  . GLU B 83  ? 0.44556 1.16449 0.72566 -0.10388 -0.12343 -0.31943 83  GLU B CA  
2834 C C   . GLU B 83  ? 0.46172 1.13566 0.69012 -0.15940 -0.08844 -0.32366 83  GLU B C   
2835 O O   . GLU B 83  ? 0.49149 1.19405 0.72745 -0.19769 -0.06507 -0.35023 83  GLU B O   
2836 C CB  . GLU B 83  ? 0.48351 1.23647 0.76918 -0.08209 -0.16517 -0.32180 83  GLU B CB  
2837 C CG  . GLU B 83  ? 0.56008 1.25178 0.78545 -0.06241 -0.19543 -0.28944 83  GLU B CG  
2838 C CD  . GLU B 83  ? 0.58130 1.29146 0.81505 -0.01644 -0.24390 -0.27925 83  GLU B CD  
2839 O OE1 . GLU B 83  ? 0.56819 1.33488 0.82587 -0.02183 -0.26000 -0.30009 83  GLU B OE1 
2840 O OE2 . GLU B 83  ? 0.59665 1.26055 0.80852 0.02368  -0.26464 -0.25022 83  GLU B OE2 
2841 N N   . SER B 84  ? 0.51996 1.11860 0.69071 -0.16383 -0.08286 -0.29892 84  SER B N   
2842 C CA  . SER B 84  ? 0.57061 1.09559 0.67957 -0.20829 -0.04289 -0.29526 84  SER B CA  
2843 C C   . SER B 84  ? 0.62564 1.11099 0.72900 -0.22245 -0.00094 -0.28964 84  SER B C   
2844 O O   . SER B 84  ? 0.72673 1.11911 0.76767 -0.23180 0.02670  -0.26575 84  SER B O   
2845 C CB  . SER B 84  ? 0.56487 0.99893 0.60371 -0.19007 -0.04873 -0.25771 84  SER B CB  
2846 O OG  . SER B 84  ? 0.67394 1.13651 0.71485 -0.16286 -0.09325 -0.25326 84  SER B OG  
2847 N N   . GLY B 85  ? 0.54059 1.09288 0.70525 -0.22168 0.00363  -0.31110 85  GLY B N   
2848 C CA  . GLY B 85  ? 0.43930 0.95191 0.59216 -0.23398 0.04103  -0.30429 85  GLY B CA  
2849 C C   . GLY B 85  ? 0.61272 1.07627 0.75403 -0.18737 0.03223  -0.26563 85  GLY B C   
2850 O O   . GLY B 85  ? 0.54112 1.00898 0.69258 -0.14498 -0.00195 -0.24728 85  GLY B O   
2851 N N   . PHE B 86  ? 0.56745 0.97969 0.68093 -0.19831 0.06451  -0.25372 86  PHE B N   
2852 C CA  . PHE B 86  ? 0.50594 0.88419 0.61464 -0.16156 0.06033  -0.22418 86  PHE B CA  
2853 C C   . PHE B 86  ? 0.50988 0.79117 0.54713 -0.15479 0.07048  -0.18806 86  PHE B C   
2854 O O   . PHE B 86  ? 0.60758 0.83373 0.59409 -0.18434 0.09769  -0.18671 86  PHE B O   
2855 C CB  . PHE B 86  ? 0.50066 0.89836 0.63099 -0.17472 0.08549  -0.23770 86  PHE B CB  
2856 C CG  . PHE B 86  ? 0.70760 1.19291 0.89439 -0.20599 0.09575  -0.28411 86  PHE B CG  
2857 C CD1 . PHE B 86  ? 0.61312 1.19132 0.87055 -0.18698 0.06411  -0.30938 86  PHE B CD1 
2858 C CD2 . PHE B 86  ? 0.79232 1.26797 0.96009 -0.25408 0.13713  -0.30380 86  PHE B CD2 
2859 C CE1 . PHE B 86  ? 0.58135 1.21869 0.87351 -0.20186 0.07325  -0.34511 86  PHE B CE1 
2860 C CE2 . PHE B 86  ? 0.73801 1.27400 0.93924 -0.27422 0.14678  -0.34264 86  PHE B CE2 
2861 C CZ  . PHE B 86  ? 0.72965 1.34731 0.99415 -0.24579 0.11534  -0.36285 86  PHE B CZ  
2862 N N   . TYR B 87  ? 0.54159 0.80170 0.57419 -0.11592 0.04930  -0.16094 87  TYR B N   
2863 C CA  . TYR B 87  ? 0.53295 0.71718 0.51081 -0.10335 0.05599  -0.12973 87  TYR B CA  
2864 C C   . TYR B 87  ? 0.49328 0.66240 0.47335 -0.08085 0.05896  -0.11099 87  TYR B C   
2865 O O   . TYR B 87  ? 0.53105 0.74053 0.55205 -0.06178 0.04368  -0.11422 87  TYR B O   
2866 C CB  . TYR B 87  ? 0.51924 0.69381 0.48570 -0.08338 0.03166  -0.11713 87  TYR B CB  
2867 C CG  . TYR B 87  ? 0.50037 0.68363 0.45448 -0.10669 0.02778  -0.13430 87  TYR B CG  
2868 C CD1 . TYR B 87  ? 0.50149 0.75651 0.49933 -0.11738 0.01096  -0.16237 87  TYR B CD1 
2869 C CD2 . TYR B 87  ? 0.52722 0.65105 0.42772 -0.11704 0.04022  -0.12506 87  TYR B CD2 
2870 C CE1 . TYR B 87  ? 0.57023 0.83993 0.55665 -0.14177 0.00563  -0.18086 87  TYR B CE1 
2871 C CE2 . TYR B 87  ? 0.54694 0.67633 0.43165 -0.14198 0.03801  -0.14291 87  TYR B CE2 
2872 C CZ  . TYR B 87  ? 0.56964 0.77330 0.49652 -0.15616 0.02012  -0.17076 87  TYR B CZ  
2873 O OH  . TYR B 87  ? 0.59072 0.80653 0.50207 -0.18348 0.01600  -0.19093 87  TYR B OH  
2874 N N   . LYS B 88  ? 0.46674 0.57708 0.40129 -0.08161 0.07748  -0.09256 88  LYS B N   
2875 C CA  . LYS B 88  ? 0.46434 0.56595 0.39954 -0.06166 0.07781  -0.07625 88  LYS B CA  
2876 C C   . LYS B 88  ? 0.48156 0.52442 0.36966 -0.04778 0.08418  -0.05171 88  LYS B C   
2877 O O   . LYS B 88  ? 0.51923 0.51480 0.36516 -0.05853 0.09838  -0.04861 88  LYS B O   
2878 C CB  . LYS B 88  ? 0.51771 0.63392 0.46086 -0.08001 0.09552  -0.08920 88  LYS B CB  
2879 C CG  . LYS B 88  ? 0.57414 0.63111 0.45952 -0.09956 0.12127  -0.08198 88  LYS B CG  
2880 C CD  . LYS B 88  ? 0.50335 0.58033 0.39499 -0.13253 0.14284  -0.10487 88  LYS B CD  
2881 C CE  . LYS B 88  ? 0.48688 0.52987 0.34265 -0.13211 0.15572  -0.09172 88  LYS B CE  
2882 N NZ  . LYS B 88  ? 0.64005 0.70524 0.50151 -0.16741 0.17961  -0.11665 88  LYS B NZ  
2883 N N   . LEU B 89  ? 0.45124 0.49909 0.34826 -0.02310 0.07359  -0.03668 89  LEU B N   
2884 C CA  . LEU B 89  ? 0.44027 0.45163 0.30653 -0.00467 0.07597  -0.01685 89  LEU B CA  
2885 C C   . LEU B 89  ? 0.59650 0.58770 0.43887 -0.00473 0.08690  -0.00959 89  LEU B C   
2886 O O   . LEU B 89  ? 0.54172 0.56073 0.40391 -0.00723 0.08530  -0.01385 89  LEU B O   
2887 C CB  . LEU B 89  ? 0.48947 0.52405 0.37870 0.01617  0.06023  -0.00866 89  LEU B CB  
2888 C CG  . LEU B 89  ? 0.51579 0.53389 0.38818 0.03581  0.06108  0.00621  89  LEU B CG  
2889 C CD1 . LEU B 89  ? 0.50036 0.49052 0.35098 0.03819  0.06547  0.00783  89  LEU B CD1 
2890 C CD2 . LEU B 89  ? 0.33985 0.38823 0.23713 0.04676  0.05048  0.00946  89  LEU B CD2 
2891 N N   . VAL B 90  ? 0.54460 0.48279 0.33938 -0.00080 0.09761  0.00122  90  VAL B N   
2892 C CA  . VAL B 90  ? 0.61352 0.52210 0.37221 -0.00318 0.10693  0.00878  90  VAL B CA  
2893 C C   . VAL B 90  ? 0.60042 0.50507 0.34897 0.02924  0.09523  0.02690  90  VAL B C   
2894 O O   . VAL B 90  ? 0.63897 0.53897 0.38956 0.05135  0.08886  0.03382  90  VAL B O   
2895 C CB  . VAL B 90  ? 0.68355 0.52549 0.38452 -0.02338 0.12777  0.00786  90  VAL B CB  
2896 C CG1 . VAL B 90  ? 0.57881 0.43856 0.29880 -0.05683 0.13777  -0.01488 90  VAL B CG1 
2897 C CG2 . VAL B 90  ? 0.72282 0.50752 0.38247 -0.00006 0.12876  0.02266  90  VAL B CG2 
2898 N N   . PRO B 91  ? 0.58193 0.49367 0.32077 0.03181  0.09239  0.03220  91  PRO B N   
2899 C CA  . PRO B 91  ? 0.57821 0.50671 0.31893 0.06118  0.07695  0.04481  91  PRO B CA  
2900 C C   . PRO B 91  ? 0.72116 0.59837 0.41290 0.08813  0.07475  0.06121  91  PRO B C   
2901 O O   . PRO B 91  ? 0.69906 0.57805 0.37227 0.10886  0.06284  0.07211  91  PRO B O   
2902 C CB  . PRO B 91  ? 0.60193 0.54964 0.33960 0.04932  0.07603  0.04248  91  PRO B CB  
2903 C CG  . PRO B 91  ? 0.57588 0.47959 0.27370 0.02199  0.09513  0.03807  91  PRO B CG  
2904 C CD  . PRO B 91  ? 0.58555 0.49018 0.30644 0.00542  0.10481  0.02482  91  PRO B CD  
2905 N N   . THR B 92  ? 0.74402 0.57368 0.41155 0.09026  0.08486  0.06241  92  THR B N   
2906 C CA  . THR B 92  ? 0.73054 0.51291 0.35769 0.12469  0.08100  0.07669  92  THR B CA  
2907 C C   . THR B 92  ? 0.73667 0.57733 0.41158 0.15684  0.06483  0.07604  92  THR B C   
2908 O O   . THR B 92  ? 0.63954 0.54635 0.36891 0.14783  0.05882  0.06621  92  THR B O   
2909 C CB  . THR B 92  ? 0.78188 0.49232 0.36770 0.11722  0.09919  0.07547  92  THR B CB  
2910 O OG1 . THR B 92  ? 0.75167 0.49593 0.38116 0.10230  0.10369  0.06065  92  THR B OG1 
2911 C CG2 . THR B 92  ? 0.78488 0.43648 0.31714 0.08077  0.11833  0.07399  92  THR B CG2 
2912 N N   . ILE B 93  ? 0.75572 0.57016 0.40791 0.19492  0.05867  0.08523  93  ILE B N   
2913 C CA  . ILE B 93  ? 0.77067 0.64728 0.47042 0.22570  0.04568  0.08044  93  ILE B CA  
2914 C C   . ILE B 93  ? 0.72647 0.56203 0.41170 0.25032  0.05502  0.07903  93  ILE B C   
2915 O O   . ILE B 93  ? 0.80939 0.58982 0.44942 0.28395  0.05160  0.09017  93  ILE B O   
2916 C CB  . ILE B 93  ? 0.81338 0.72300 0.51214 0.25526  0.02340  0.08865  93  ILE B CB  
2917 C CG1 . ILE B 93  ? 0.83471 0.78281 0.54590 0.22551  0.01778  0.08674  93  ILE B CG1 
2918 C CG2 . ILE B 93  ? 0.66209 0.64329 0.41379 0.28724  0.01174  0.07884  93  ILE B CG2 
2919 C CD1 . ILE B 93  ? 0.88597 0.89870 0.61867 0.24477  -0.00480 0.08653  93  ILE B CD1 
2920 N N   . PRO B 94  ? 0.75301 0.60586 0.46839 0.23560  0.06724  0.06563  94  PRO B N   
2921 C CA  . PRO B 94  ? 0.58969 0.49609 0.34984 0.20203  0.06967  0.05399  94  PRO B CA  
2922 C C   . PRO B 94  ? 0.60393 0.48106 0.34577 0.16335  0.07758  0.05329  94  PRO B C   
2923 O O   . PRO B 94  ? 0.69796 0.50866 0.39247 0.15647  0.08866  0.05718  94  PRO B O   
2924 C CB  . PRO B 94  ? 0.61609 0.52683 0.39195 0.20618  0.08104  0.04242  94  PRO B CB  
2925 C CG  . PRO B 94  ? 0.73081 0.58747 0.47213 0.23997  0.08734  0.04592  94  PRO B CG  
2926 C CD  . PRO B 94  ? 0.83442 0.63419 0.52553 0.25044  0.08178  0.06197  94  PRO B CD  
2927 N N   . PRO B 95  ? 0.59311 0.51768 0.37071 0.13888  0.07292  0.04656  95  PRO B N   
2928 C CA  . PRO B 95  ? 0.55975 0.47042 0.33110 0.10565  0.07881  0.04129  95  PRO B CA  
2929 C C   . PRO B 95  ? 0.65360 0.52010 0.40049 0.09232  0.09197  0.03517  95  PRO B C   
2930 O O   . PRO B 95  ? 0.62506 0.48919 0.37553 0.10087  0.09515  0.03144  95  PRO B O   
2931 C CB  . PRO B 95  ? 0.47102 0.43907 0.28871 0.09268  0.06984  0.03362  95  PRO B CB  
2932 C CG  . PRO B 95  ? 0.48414 0.49275 0.32411 0.11257  0.06062  0.03687  95  PRO B CG  
2933 C CD  . PRO B 95  ? 0.51000 0.50081 0.33450 0.14027  0.06357  0.04094  95  PRO B CD  
2934 N N   . THR B 96  ? 0.63134 0.46204 0.35000 0.06845  0.10211  0.03185  96  THR B N   
2935 C CA  . THR B 96  ? 0.66295 0.45954 0.36079 0.04635  0.11490  0.02126  96  THR B CA  
2936 C C   . THR B 96  ? 0.68984 0.52472 0.41549 0.01360  0.11241  0.00669  96  THR B C   
2937 O O   . THR B 96  ? 0.63911 0.51735 0.39596 0.01063  0.10346  0.00549  96  THR B O   
2938 C CB  . THR B 96  ? 0.74785 0.46126 0.38131 0.04413  0.13309  0.02570  96  THR B CB  
2939 O OG1 . THR B 96  ? 0.80285 0.49880 0.41337 0.02474  0.13963  0.02723  96  THR B OG1 
2940 C CG2 . THR B 96  ? 0.79704 0.47572 0.40630 0.08652  0.13095  0.04032  96  THR B CG2 
2941 N N   . ILE B 97  ? 0.65057 0.47286 0.36676 -0.00963 0.11963  -0.00678 97  ILE B N   
2942 C CA  . ILE B 97  ? 0.62394 0.49165 0.37157 -0.03710 0.11391  -0.02442 97  ILE B CA  
2943 C C   . ILE B 97  ? 0.69798 0.53514 0.41595 -0.07174 0.13404  -0.03837 97  ILE B C   
2944 O O   . ILE B 97  ? 0.76079 0.53266 0.42766 -0.08050 0.15195  -0.03796 97  ILE B O   
2945 C CB  . ILE B 97  ? 0.67381 0.56407 0.43678 -0.03857 0.10187  -0.03180 97  ILE B CB  
2946 C CG1 . ILE B 97  ? 0.68223 0.62578 0.48015 -0.06006 0.08956  -0.05052 97  ILE B CG1 
2947 C CG2 . ILE B 97  ? 0.86260 0.69768 0.58105 -0.04454 0.11664  -0.03435 97  ILE B CG2 
2948 C CD1 . ILE B 97  ? 0.62830 0.59285 0.43484 -0.05726 0.07143  -0.05432 97  ILE B CD1 
2949 N N   . GLU B 98  ? 0.63066 0.51233 0.37864 -0.09273 0.13385  -0.05272 98  GLU B N   
2950 C CA  . GLU B 98  ? 0.75369 0.61573 0.47741 -0.13253 0.15684  -0.07041 98  GLU B CA  
2951 C C   . GLU B 98  ? 0.76260 0.69680 0.53618 -0.15861 0.14952  -0.09938 98  GLU B C   
2952 O O   . GLU B 98  ? 0.66453 0.66817 0.49511 -0.14779 0.13159  -0.10606 98  GLU B O   
2953 C CB  . GLU B 98  ? 0.76457 0.61326 0.47320 -0.13688 0.16886  -0.06462 98  GLU B CB  
2954 C CG  . GLU B 98  ? 0.82130 0.67676 0.52298 -0.18353 0.19251  -0.08920 98  GLU B CG  
2955 C CD  . GLU B 98  ? 0.91072 0.72727 0.57225 -0.18950 0.20897  -0.07912 98  GLU B CD  
2956 O OE1 . GLU B 98  ? 1.01427 0.76506 0.62428 -0.16316 0.20761  -0.05167 98  GLU B OE1 
2957 O OE2 . GLU B 98  ? 0.85381 0.70741 0.53438 -0.21963 0.22271  -0.09981 98  GLU B OE2 
2958 N N   . ILE B 99  ? 0.76815 0.68589 0.51959 -0.19144 0.16254  -0.11796 99  ILE B N   
2959 C CA  . ILE B 99  ? 0.76958 0.76116 0.56706 -0.21705 0.15318  -0.14890 99  ILE B CA  
2960 C C   . ILE B 99  ? 0.86858 0.86775 0.66000 -0.26544 0.18143  -0.17627 99  ILE B C   
2961 O O   . ILE B 99  ? 0.96807 0.89466 0.69662 -0.29705 0.21083  -0.17971 99  ILE B O   
2962 C CB  . ILE B 99  ? 0.78503 0.76476 0.56472 -0.22413 0.14565  -0.15521 99  ILE B CB  
2963 C CG1 . ILE B 99  ? 0.84581 0.77766 0.59905 -0.18509 0.13517  -0.12571 99  ILE B CG1 
2964 C CG2 . ILE B 99  ? 0.68583 0.75917 0.52450 -0.23142 0.11924  -0.18030 99  ILE B CG2 
2965 C CD1 . ILE B 99  ? 0.81731 0.70901 0.53077 -0.19610 0.13954  -0.13051 99  ILE B CD1 
2966 N N   . ASN B 100 ? 0.82925 0.91299 0.68359 -0.27191 0.17471  -0.19735 100 ASN B N   
2967 C CA  . ASN B 100 ? 0.82860 0.94158 0.69143 -0.32164 0.20242  -0.23100 100 ASN B CA  
2968 C C   . ASN B 100 ? 0.97668 0.99136 0.75948 -0.34661 0.24071  -0.21876 100 ASN B C   
2969 O O   . ASN B 100 ? 0.99966 0.98417 0.74380 -0.39873 0.27350  -0.24067 100 ASN B O   
2970 C CB  . ASN B 100 ? 0.89171 1.04645 0.76884 -0.36075 0.20439  -0.26578 100 ASN B CB  
2971 C CG  . ASN B 100 ? 0.80368 1.05711 0.75541 -0.33357 0.16192  -0.27792 100 ASN B CG  
2972 O OD1 . ASN B 100 ? 0.71252 1.05599 0.73632 -0.32084 0.14582  -0.29558 100 ASN B OD1 
2973 N ND2 . ASN B 100 ? 0.77884 1.01077 0.70877 -0.32276 0.14353  -0.26847 100 ASN B ND2 
2974 N N   . GLY B 101 ? 0.92973 0.89142 0.68278 -0.30976 0.23583  -0.18374 101 GLY B N   
2975 C CA  . GLY B 101 ? 0.96675 0.83360 0.64294 -0.32121 0.26204  -0.16627 101 GLY B CA  
2976 C C   . GLY B 101 ? 1.06105 0.81451 0.65605 -0.32723 0.27445  -0.15100 101 GLY B C   
2977 O O   . GLY B 101 ? 1.08086 0.75881 0.62036 -0.35142 0.29300  -0.15212 101 GLY B O   
2978 N N   . ILE B 102 ? 0.99974 0.73463 0.58213 -0.30426 0.26494  -0.13934 102 ILE B N   
2979 C CA  . ILE B 102 ? 1.16587 0.79095 0.67385 -0.30362 0.27695  -0.12576 102 ILE B CA  
2980 C C   . ILE B 102 ? 1.14799 0.72561 0.62933 -0.24622 0.26241  -0.08979 102 ILE B C   
2981 O O   . ILE B 102 ? 1.10921 0.73847 0.63720 -0.21359 0.23761  -0.08358 102 ILE B O   
2982 C CB  . ILE B 102 ? 1.19823 0.83266 0.70636 -0.33523 0.28406  -0.15096 102 ILE B CB  
2983 C CG1 . ILE B 102 ? 1.16660 0.83686 0.69082 -0.39766 0.30259  -0.18987 102 ILE B CG1 
2984 C CG2 . ILE B 102 ? 1.27415 0.79474 0.70863 -0.32476 0.29511  -0.13548 102 ILE B CG2 
2985 C CD1 . ILE B 102 ? 1.10866 0.82181 0.65082 -0.43282 0.30549  -0.21959 102 ILE B CD1 
2986 N N   . MET B 110 ? 1.65565 0.84055 0.86745 0.39797  0.09640  0.13205  110 MET B N   
2987 C CA  . MET B 110 ? 1.60569 0.82387 0.86295 0.37459  0.11509  0.11797  110 MET B CA  
2988 C C   . MET B 110 ? 1.44630 0.75459 0.78360 0.41301  0.10220  0.10776  110 MET B C   
2989 O O   . MET B 110 ? 1.43152 0.71787 0.76994 0.42797  0.11419  0.09821  110 MET B O   
2990 C CB  . MET B 110 ? 1.58976 0.84861 0.87303 0.32841  0.11971  0.11692  110 MET B CB  
2991 C CG  . MET B 110 ? 1.66929 0.84906 0.89025 0.27178  0.14536  0.11493  110 MET B CG  
2992 S SD  . MET B 110 ? 1.76958 0.91005 0.98225 0.22735  0.17995  0.09647  110 MET B SD  
2993 C CE  . MET B 110 ? 1.66084 0.70562 0.80799 0.25252  0.19450  0.09383  110 MET B CE  
2994 N N   . ASN B 111 ? 1.35774 0.76886 0.76173 0.42510  0.07949  0.10724  111 ASN B N   
2995 C CA  . ASN B 111 ? 1.36120 0.87437 0.85063 0.44679  0.07123  0.09194  111 ASN B CA  
2996 C C   . ASN B 111 ? 1.30513 0.82388 0.82061 0.42106  0.09659  0.07627  111 ASN B C   
2997 O O   . ASN B 111 ? 1.32975 0.85427 0.86543 0.43689  0.10574  0.06266  111 ASN B O   
2998 C CB  . ASN B 111 ? 1.25233 0.78026 0.75550 0.49641  0.05686  0.08749  111 ASN B CB  
2999 C CG  . ASN B 111 ? 1.32068 0.94119 0.87274 0.52327  0.02500  0.08753  111 ASN B CG  
3000 O OD1 . ASN B 111 ? 1.24335 0.96847 0.87458 0.52735  0.01817  0.07143  111 ASN B OD1 
3001 N ND2 . ASN B 111 ? 1.50681 1.08924 1.01010 0.53801  0.00666  0.10341  111 ASN B ND2 
3002 N N   . PRO B 112 ? 1.22392 0.92307 0.58911 0.20226  -0.04583 0.07547  112 PRO B N   
3003 C CA  . PRO B 112 ? 1.12616 0.84894 0.53723 0.18667  -0.03555 0.07203  112 PRO B CA  
3004 C C   . PRO B 112 ? 1.09415 0.88280 0.55290 0.19622  -0.05514 0.05170  112 PRO B C   
3005 O O   . PRO B 112 ? 1.05372 0.86033 0.54565 0.19399  -0.05400 0.04789  112 PRO B O   
3006 C CB  . PRO B 112 ? 1.11294 0.83498 0.52904 0.15479  -0.00678 0.07627  112 PRO B CB  
3007 C CG  . PRO B 112 ? 1.07312 0.80410 0.46582 0.15646  -0.01007 0.07157  112 PRO B CG  
3008 C CD  . PRO B 112 ? 1.14176 0.84604 0.49259 0.18450  -0.03154 0.07531  112 PRO B CD  
3009 N N   . LEU B 113 ? 1.03953 0.86464 0.50196 0.20580  -0.07262 0.03748  113 LEU B N   
3010 C CA  . LEU B 113 ? 0.96016 0.85281 0.47158 0.21071  -0.08982 0.01514  113 LEU B CA  
3011 C C   . LEU B 113 ? 0.91317 0.82230 0.44658 0.23505  -0.10755 0.00900  113 LEU B C   
3012 O O   . LEU B 113 ? 0.87426 0.82229 0.45032 0.23120  -0.10716 -0.00087 113 LEU B O   
3013 C CB  . LEU B 113 ? 0.88738 0.80904 0.39426 0.21704  -0.10705 0.00026  113 LEU B CB  
3014 C CG  . LEU B 113 ? 0.78521 0.77006 0.33832 0.20310  -0.11212 -0.02289 113 LEU B CG  
3015 C CD1 . LEU B 113 ? 0.82464 0.80483 0.39060 0.17404  -0.08476 -0.01837 113 LEU B CD1 
3016 C CD2 . LEU B 113 ? 0.73438 0.73284 0.27250 0.20566  -0.12610 -0.03547 113 LEU B CD2 
3017 N N   . GLN B 114 ? 0.96743 0.84618 0.47014 0.26133  -0.12220 0.01387  114 GLN B N   
3018 C CA  . GLN B 114 ? 0.95157 0.83942 0.47168 0.28728  -0.13719 0.00751  114 GLN B CA  
3019 C C   . GLN B 114 ? 0.98034 0.82989 0.49788 0.27954  -0.11999 0.02123  114 GLN B C   
3020 O O   . GLN B 114 ? 0.90405 0.77976 0.45469 0.29035  -0.12557 0.01204  114 GLN B O   
3021 C CB  . GLN B 114 ? 0.91296 0.76874 0.39367 0.31822  -0.15597 0.00922  114 GLN B CB  
3022 C CG  . GLN B 114 ? 0.91996 0.79643 0.42410 0.34847  -0.17404 -0.00374 114 GLN B CG  
3023 C CD  . GLN B 114 ? 0.97215 0.93739 0.53603 0.35714  -0.19276 -0.03213 114 GLN B CD  
3024 O OE1 . GLN B 114 ? 0.96098 0.95760 0.52973 0.35448  -0.20368 -0.04299 114 GLN B OE1 
3025 N NE2 . GLN B 114 ? 0.88271 0.89098 0.49463 0.36493  -0.19487 -0.04580 114 GLN B NE2 
3026 N N   . ASP B 115 ? 1.03584 0.82510 0.51592 0.26023  -0.09840 0.04161  115 ASP B N   
3027 C CA  . ASP B 115 ? 1.04345 0.79284 0.52064 0.25036  -0.08252 0.05336  115 ASP B CA  
3028 C C   . ASP B 115 ? 0.90928 0.70439 0.43436 0.23603  -0.07578 0.04443  115 ASP B C   
3029 O O   . ASP B 115 ? 0.86711 0.65865 0.40839 0.24261  -0.07634 0.04261  115 ASP B O   
3030 C CB  . ASP B 115 ? 1.17247 0.86086 0.61027 0.22600  -0.05800 0.07329  115 ASP B CB  
3031 C CG  . ASP B 115 ? 1.30722 0.93067 0.69099 0.24067  -0.06079 0.08559  115 ASP B CG  
3032 O OD1 . ASP B 115 ? 1.38018 0.94859 0.73267 0.22107  -0.03929 0.10163  115 ASP B OD1 
3033 O OD2 . ASP B 115 ? 1.37628 1.00483 0.74918 0.27151  -0.08398 0.07803  115 ASP B OD2 
3034 N N   . THR B 116 ? 0.89830 0.73564 0.44823 0.21525  -0.06821 0.03686  116 THR B N   
3035 C CA  . THR B 116 ? 0.77316 0.66201 0.38763 0.19505  -0.05883 0.02293  116 THR B CA  
3036 C C   . THR B 116 ? 0.78128 0.72109 0.43349 0.21520  -0.07606 0.00498  116 THR B C   
3037 O O   . THR B 116 ? 0.82152 0.77554 0.50670 0.21159  -0.06967 -0.00050 116 THR B O   
3038 C CB  . THR B 116 ? 0.74722 0.66891 0.38191 0.17114  -0.04943 0.01570  116 THR B CB  
3039 O OG1 . THR B 116 ? 0.86275 0.74182 0.46267 0.15538  -0.03240 0.03033  116 THR B OG1 
3040 C CG2 . THR B 116 ? 0.64599 0.60607 0.33658 0.14973  -0.03778 0.00524  116 THR B CG2 
3041 N N   . ARG B 117 ? 0.77985 0.75050 0.42826 0.23698  -0.09797 -0.00612 117 ARG B N   
3042 C CA  . ARG B 117 ? 0.74372 0.77105 0.43392 0.25725  -0.11420 -0.02620 117 ARG B CA  
3043 C C   . ARG B 117 ? 0.75891 0.75741 0.43896 0.28161  -0.11848 -0.02175 117 ARG B C   
3044 O O   . ARG B 117 ? 0.68780 0.71778 0.40975 0.27991  -0.11177 -0.03272 117 ARG B O   
3045 C CB  . ARG B 117 ? 0.71585 0.77623 0.39853 0.28135  -0.14171 -0.03936 117 ARG B CB  
3046 C CG  . ARG B 117 ? 0.69495 0.80639 0.40971 0.25769  -0.14019 -0.05473 117 ARG B CG  
3047 C CD  . ARG B 117 ? 0.73618 0.90661 0.47535 0.27943  -0.16804 -0.07848 117 ARG B CD  
3048 N NE  . ARG B 117 ? 0.84402 0.97578 0.53746 0.29368  -0.18033 -0.07192 117 ARG B NE  
3049 C CZ  . ARG B 117 ? 0.81975 0.93235 0.48498 0.27757  -0.17656 -0.06703 117 ARG B CZ  
3050 N NH1 . ARG B 117 ? 0.77663 0.90017 0.45298 0.24665  -0.16011 -0.06798 117 ARG B NH1 
3051 N NH2 . ARG B 117 ? 0.77681 0.85703 0.39925 0.29389  -0.18905 -0.06213 117 ARG B NH2 
3052 N N   . ASN B 118 ? 0.74758 0.67984 0.36901 0.30224  -0.12669 -0.00555 118 ASN B N   
3053 C CA  . ASN B 118 ? 0.84948 0.74341 0.45847 0.32350  -0.12941 -0.00275 118 ASN B CA  
3054 C C   . ASN B 118 ? 0.82667 0.70455 0.45079 0.30512  -0.11040 0.00219  118 ASN B C   
3055 O O   . ASN B 118 ? 0.85469 0.74245 0.49900 0.32059  -0.11280 -0.00762 118 ASN B O   
3056 C CB  . ASN B 118 ? 0.96240 0.77720 0.51075 0.33108  -0.12990 0.01390  118 ASN B CB  
3057 C CG  . ASN B 118 ? 1.01361 0.84004 0.54769 0.35684  -0.15123 0.00500  118 ASN B CG  
3058 O OD1 . ASN B 118 ? 0.91585 0.81083 0.49079 0.37211  -0.16737 -0.01641 118 ASN B OD1 
3059 N ND2 . ASN B 118 ? 1.02289 0.78300 0.49909 0.36093  -0.15088 0.02049  118 ASN B ND2 
3060 N N   . LYS B 119 ? 0.80046 0.65717 0.42191 0.26881  -0.08887 0.01361  119 LYS B N   
3061 C CA  . LYS B 119 ? 0.75359 0.59659 0.39489 0.24595  -0.07015 0.01528  119 LYS B CA  
3062 C C   . LYS B 119 ? 0.68927 0.59659 0.38629 0.24267  -0.06703 -0.00378 119 LYS B C   
3063 O O   . LYS B 119 ? 0.66927 0.57012 0.37541 0.25029  -0.06467 -0.00933 119 LYS B O   
3064 C CB  . LYS B 119 ? 0.77326 0.59903 0.41178 0.20960  -0.05042 0.02642  119 LYS B CB  
3065 C CG  . LYS B 119 ? 0.89415 0.64573 0.48186 0.20294  -0.04239 0.04622  119 LYS B CG  
3066 C CD  . LYS B 119 ? 0.93903 0.68735 0.54017 0.16587  -0.02036 0.05193  119 LYS B CD  
3067 C CE  . LYS B 119 ? 1.01070 0.69710 0.56348 0.15533  -0.00817 0.07045  119 LYS B CE  
3068 N NZ  . LYS B 119 ? 0.93146 0.63572 0.49680 0.12716  0.01004  0.07240  119 LYS B NZ  
3069 N N   . VAL B 120 ? 0.63617 0.60255 0.36767 0.23005  -0.06537 -0.01433 120 VAL B N   
3070 C CA  . VAL B 120 ? 0.66542 0.69200 0.44698 0.22371  -0.05899 -0.03166 120 VAL B CA  
3071 C C   . VAL B 120 ? 0.75148 0.81294 0.54955 0.25698  -0.07355 -0.04754 120 VAL B C   
3072 O O   . VAL B 120 ? 0.64249 0.73577 0.47121 0.25889  -0.06547 -0.06010 120 VAL B O   
3073 C CB  . VAL B 120 ? 0.53430 0.60642 0.34398 0.19992  -0.05324 -0.03849 120 VAL B CB  
3074 C CG1 . VAL B 120 ? 0.49132 0.61924 0.34862 0.18892  -0.04250 -0.05467 120 VAL B CG1 
3075 C CG2 . VAL B 120 ? 0.59910 0.63639 0.39256 0.17212  -0.03961 -0.02437 120 VAL B CG2 
3076 N N   . ASN B 121 ? 0.66192 0.71638 0.43715 0.28586  -0.09514 -0.04762 121 ASN B N   
3077 C CA  . ASN B 121 ? 0.66776 0.76028 0.46103 0.32268  -0.11326 -0.06495 121 ASN B CA  
3078 C C   . ASN B 121 ? 0.68232 0.74170 0.46391 0.34411  -0.11166 -0.06522 121 ASN B C   
3079 O O   . ASN B 121 ? 0.68721 0.78577 0.49354 0.37382  -0.12156 -0.08326 121 ASN B O   
3080 C CB  . ASN B 121 ? 0.64885 0.72659 0.40688 0.35223  -0.14041 -0.06187 121 ASN B CB  
3081 C CG  . ASN B 121 ? 0.69198 0.85168 0.49308 0.36029  -0.15654 -0.08454 121 ASN B CG  
3082 O OD1 . ASN B 121 ? 0.70088 0.92454 0.55751 0.33576  -0.14337 -0.10022 121 ASN B OD1 
3083 N ND2 . ASN B 121 ? 0.76940 0.91655 0.54640 0.38041  -0.17541 -0.08804 121 ASN B ND2 
3084 N N   . THR B 122 ? 0.64555 0.63570 0.39231 0.32992  -0.09970 -0.04800 122 THR B N   
3085 C CA  . THR B 122 ? 0.76440 0.71395 0.49453 0.34906  -0.09938 -0.04922 122 THR B CA  
3086 C C   . THR B 122 ? 0.74095 0.73065 0.51052 0.33769  -0.08218 -0.06407 122 THR B C   
3087 O O   . THR B 122 ? 0.75472 0.73945 0.52435 0.36242  -0.08436 -0.07503 122 THR B O   
3088 C CB  . THR B 122 ? 0.75799 0.61728 0.43705 0.33589  -0.09382 -0.02762 122 THR B CB  
3089 O OG1 . THR B 122 ? 0.81207 0.67220 0.50287 0.29353  -0.07470 -0.01965 122 THR B OG1 
3090 C CG2 . THR B 122 ? 0.84020 0.64644 0.46781 0.35214  -0.10860 -0.01163 122 THR B CG2 
3091 N N   . VAL B 123 ? 0.72180 0.74661 0.51975 0.30246  -0.06479 -0.06464 123 VAL B N   
3092 C CA  . VAL B 123 ? 0.59333 0.65118 0.41997 0.28999  -0.04668 -0.07635 123 VAL B CA  
3093 C C   . VAL B 123 ? 0.65705 0.79785 0.53402 0.28208  -0.03871 -0.09280 123 VAL B C   
3094 O O   . VAL B 123 ? 0.63007 0.80142 0.52919 0.27319  -0.02102 -0.10328 123 VAL B O   
3095 C CB  . VAL B 123 ? 0.64540 0.66674 0.45820 0.25611  -0.03164 -0.06367 123 VAL B CB  
3096 C CG1 . VAL B 123 ? 0.69944 0.64570 0.47150 0.26242  -0.03703 -0.05351 123 VAL B CG1 
3097 C CG2 . VAL B 123 ? 0.58336 0.60808 0.39852 0.22992  -0.02963 -0.05222 123 VAL B CG2 
3098 N N   . MET B 124 ? 0.63934 0.81651 0.53329 0.28473  -0.05086 -0.09659 124 MET B N   
3099 C CA  . MET B 124 ? 0.57387 0.82900 0.51856 0.27097  -0.04436 -0.11318 124 MET B CA  
3100 C C   . MET B 124 ? 0.52905 0.80812 0.49731 0.23914  -0.01623 -0.11695 124 MET B C   
3101 O O   . MET B 124 ? 0.56465 0.88080 0.55766 0.24601  -0.00349 -0.13192 124 MET B O   
3102 C CB  . MET B 124 ? 0.58594 0.90297 0.56635 0.30460  -0.05781 -0.13663 124 MET B CB  
3103 C CG  . MET B 124 ? 0.63955 0.92376 0.58909 0.34874  -0.08520 -0.13487 124 MET B CG  
3104 S SD  . MET B 124 ? 0.57685 0.86594 0.51437 0.35246  -0.11144 -0.13032 124 MET B SD  
3105 C CE  . MET B 124 ? 0.55095 0.95133 0.56662 0.33442  -0.10634 -0.15902 124 MET B CE  
3106 N N   . PRO B 125 ? 0.54774 0.80619 0.50693 0.20564  -0.00541 -0.10423 125 PRO B N   
3107 C CA  . PRO B 125 ? 0.53548 0.80971 0.50968 0.17650  0.02016  -0.10609 125 PRO B CA  
3108 C C   . PRO B 125 ? 0.52084 0.86770 0.54486 0.16306  0.02996  -0.12463 125 PRO B C   
3109 O O   . PRO B 125 ? 0.45098 0.82726 0.49505 0.16129  0.01677  -0.13142 125 PRO B O   
3110 C CB  . PRO B 125 ? 0.53558 0.76263 0.48358 0.15053  0.02299  -0.08742 125 PRO B CB  
3111 C CG  . PRO B 125 ? 0.53878 0.72434 0.45754 0.16579  0.00232  -0.07581 125 PRO B CG  
3112 C CD  . PRO B 125 ? 0.53568 0.75448 0.46825 0.19429  -0.01527 -0.08809 125 PRO B CD  
3113 N N   . ARG B 126 ? 0.52103 0.89582 0.56357 0.15173  0.05433  -0.13370 126 ARG B N   
3114 C CA  . ARG B 126 ? 0.43400 0.88062 0.52837 0.13522  0.06969  -0.15342 126 ARG B CA  
3115 C C   . ARG B 126 ? 0.53806 0.97183 0.62927 0.09299  0.09314  -0.14537 126 ARG B C   
3116 O O   . ARG B 126 ? 0.57400 0.94637 0.62354 0.08093  0.09585  -0.12542 126 ARG B O   
3117 C CB  . ARG B 126 ? 0.54384 1.03424 0.66236 0.15161  0.08518  -0.17104 126 ARG B CB  
3118 C CG  . ARG B 126 ? 0.63394 1.17116 0.78437 0.18759  0.06300  -0.18981 126 ARG B CG  
3119 C CD  . ARG B 126 ? 0.63968 1.12653 0.74928 0.22719  0.04265  -0.18173 126 ARG B CD  
3120 N NE  . ARG B 126 ? 0.69610 1.21061 0.82478 0.26014  0.01481  -0.19452 126 ARG B NE  
3121 C CZ  . ARG B 126 ? 0.66786 1.18620 0.79594 0.27524  -0.01285 -0.19467 126 ARG B CZ  
3122 N NH1 . ARG B 126 ? 0.59492 1.08830 0.70584 0.25471  -0.01663 -0.18099 126 ARG B NH1 
3123 N NH2 . ARG B 126 ? 0.70927 1.24432 0.84496 0.30643  -0.03850 -0.20568 126 ARG B NH2 
3124 N N   . GLU B 127 ? 0.56214 1.05448 0.69910 0.07049  0.11045  -0.16234 127 GLU B N   
3125 C CA  . GLU B 127 ? 0.62004 1.09622 0.75323 0.02916  0.13277  -0.15557 127 GLU B CA  
3126 C C   . GLU B 127 ? 0.65992 1.08416 0.74862 0.01820  0.15746  -0.13897 127 GLU B C   
3127 O O   . GLU B 127 ? 0.67484 1.04215 0.72648 0.00076  0.16059  -0.12082 127 GLU B O   
3128 C CB  . GLU B 127 ? 0.60091 1.15090 0.79454 0.00484  0.14943  -0.17933 127 GLU B CB  
3129 C CG  . GLU B 127 ? 0.70111 1.29382 0.93324 0.00655  0.12307  -0.19517 127 GLU B CG  
3130 C CD  . GLU B 127 ? 0.84207 1.43530 1.08942 -0.03610 0.13439  -0.19876 127 GLU B CD  
3131 O OE1 . GLU B 127 ? 0.82106 1.41490 1.07314 -0.03674 0.11025  -0.20291 127 GLU B OE1 
3132 O OE2 . GLU B 127 ? 0.86394 1.45261 1.11446 -0.06882 0.16788  -0.19761 127 GLU B OE2 
3133 N N   . GLY B 128 ? 0.54497 0.98739 0.63433 0.03035  0.17424  -0.14600 128 GLY B N   
3134 C CA  . GLY B 128 ? 0.65934 1.04848 0.69888 0.02193  0.19528  -0.13044 128 GLY B CA  
3135 C C   . GLY B 128 ? 0.73014 1.05920 0.71918 0.04745  0.17632  -0.11553 128 GLY B C   
3136 O O   . GLY B 128 ? 0.70701 1.02123 0.66972 0.06112  0.18642  -0.11575 128 GLY B O   
3137 N N   . GLU B 129 ? 0.53689 0.83008 0.51155 0.05267  0.15001  -0.10363 129 GLU B N   
3138 C CA  . GLU B 129 ? 0.51958 0.76524 0.45852 0.07683  0.12994  -0.09360 129 GLU B CA  
3139 C C   . GLU B 129 ? 0.47939 0.67061 0.38906 0.06595  0.11753  -0.07537 129 GLU B C   
3140 O O   . GLU B 129 ? 0.50359 0.69642 0.42426 0.04702  0.11681  -0.07165 129 GLU B O   
3141 C CB  . GLU B 129 ? 0.52024 0.78689 0.47815 0.10664  0.10674  -0.10269 129 GLU B CB  
3142 C CG  . GLU B 129 ? 0.58280 0.89611 0.56418 0.12761  0.11497  -0.12174 129 GLU B CG  
3143 C CD  . GLU B 129 ? 0.54472 0.85425 0.52532 0.16422  0.09019  -0.12713 129 GLU B CD  
3144 O OE1 . GLU B 129 ? 0.61859 0.89823 0.58653 0.17030  0.06751  -0.11681 129 GLU B OE1 
3145 O OE2 . GLU B 129 ? 0.57863 0.91171 0.56797 0.18756  0.09486  -0.14167 129 GLU B OE2 
3146 N N   . THR B 130 ? 0.46522 0.60978 0.33948 0.07875  0.10731  -0.06636 130 THR B N   
3147 C CA  . THR B 130 ? 0.54126 0.63892 0.39209 0.07191  0.09468  -0.05189 130 THR B CA  
3148 C C   . THR B 130 ? 0.48378 0.56122 0.32924 0.09084  0.07287  -0.04985 130 THR B C   
3149 O O   . THR B 130 ? 0.55128 0.61954 0.38520 0.10931  0.06866  -0.05490 130 THR B O   
3150 C CB  . THR B 130 ? 0.49509 0.55280 0.30744 0.06612  0.10250  -0.04385 130 THR B CB  
3151 O OG1 . THR B 130 ? 0.56921 0.63498 0.37863 0.04628  0.12498  -0.04262 130 THR B OG1 
3152 C CG2 . THR B 130 ? 0.53843 0.55627 0.33481 0.06257  0.08672  -0.03253 130 THR B CG2 
3153 N N   . VAL B 131 ? 0.52508 0.59185 0.37589 0.08545  0.06088  -0.04279 131 VAL B N   
3154 C CA  . VAL B 131 ? 0.46587 0.50710 0.30796 0.09801  0.04408  -0.03840 131 VAL B CA  
3155 C C   . VAL B 131 ? 0.47740 0.48214 0.30501 0.08683  0.03927  -0.02846 131 VAL B C   
3156 O O   . VAL B 131 ? 0.45225 0.45734 0.28347 0.07142  0.04390  -0.02403 131 VAL B O   
3157 C CB  . VAL B 131 ? 0.51880 0.57927 0.37642 0.10364  0.03494  -0.03948 131 VAL B CB  
3158 C CG1 . VAL B 131 ? 0.53939 0.61859 0.41172 0.08496  0.03984  -0.03854 131 VAL B CG1 
3159 C CG2 . VAL B 131 ? 0.45867 0.48169 0.29913 0.10982  0.02217  -0.03048 131 VAL B CG2 
3160 N N   . LEU B 132 ? 0.43433 0.40812 0.24767 0.09482  0.02967  -0.02682 132 LEU B N   
3161 C CA  . LEU B 132 ? 0.49776 0.44519 0.30763 0.08509  0.02303  -0.02033 132 LEU B CA  
3162 C C   . LEU B 132 ? 0.42175 0.36222 0.23639 0.08543  0.01786  -0.01537 132 LEU B C   
3163 O O   . LEU B 132 ? 0.39416 0.32249 0.20035 0.09819  0.01261  -0.01614 132 LEU B O   
3164 C CB  . LEU B 132 ? 0.41425 0.33275 0.20883 0.08932  0.01559  -0.02362 132 LEU B CB  
3165 C CG  . LEU B 132 ? 0.52846 0.42823 0.32923 0.07835  0.00812  -0.02046 132 LEU B CG  
3166 C CD1 . LEU B 132 ? 0.47950 0.39084 0.28949 0.06715  0.01153  -0.01659 132 LEU B CD1 
3167 C CD2 . LEU B 132 ? 0.49024 0.36500 0.28027 0.08115  -0.00236 -0.02756 132 LEU B CD2 
3168 N N   . ASP B 133 ? 0.39571 0.33897 0.21895 0.07281  0.01991  -0.01018 133 ASP B N   
3169 C CA  . ASP B 133 ? 0.43955 0.37062 0.26079 0.07051  0.01818  -0.00424 133 ASP B CA  
3170 C C   . ASP B 133 ? 0.45025 0.36183 0.27625 0.05861  0.01814  -0.00220 133 ASP B C   
3171 O O   . ASP B 133 ? 0.43498 0.35626 0.27310 0.04905  0.02091  -0.00281 133 ASP B O   
3172 C CB  . ASP B 133 ? 0.45827 0.41097 0.28573 0.06589  0.02186  -0.00272 133 ASP B CB  
3173 C CG  . ASP B 133 ? 0.48258 0.41954 0.29929 0.06455  0.02193  0.00405  133 ASP B CG  
3174 O OD1 . ASP B 133 ? 0.53317 0.44904 0.33292 0.07497  0.01749  0.00774  133 ASP B OD1 
3175 O OD2 . ASP B 133 ? 0.52181 0.46308 0.34312 0.05380  0.02743  0.00583  133 ASP B OD2 
3176 N N   . THR B 134 ? 0.46560 0.34991 0.28407 0.05921  0.01479  -0.00134 134 THR B N   
3177 C CA  . THR B 134 ? 0.55717 0.43042 0.38815 0.04694  0.01326  -0.00452 134 THR B CA  
3178 C C   . THR B 134 ? 0.52015 0.39692 0.36503 0.03237  0.02164  -0.00064 134 THR B C   
3179 O O   . THR B 134 ? 0.52214 0.40623 0.38822 0.02259  0.02089  -0.00617 134 THR B O   
3180 C CB  . THR B 134 ? 0.55771 0.39958 0.37901 0.04858  0.00742  -0.00798 134 THR B CB  
3181 O OG1 . THR B 134 ? 0.53286 0.35042 0.33515 0.05294  0.01087  -0.00026 134 THR B OG1 
3182 C CG2 . THR B 134 ? 0.55228 0.39271 0.36204 0.06248  -0.00050 -0.01562 134 THR B CG2 
3183 N N   A CYS B 135 ? 0.55684 0.43052 0.38975 0.03230  0.02923  0.00732  135 CYS B N   
3184 N N   B CYS B 135 ? 0.55282 0.42612 0.38567 0.03223  0.02923  0.00733  135 CYS B N   
3185 C CA  A CYS B 135 ? 0.54451 0.41996 0.38467 0.01895  0.04094  0.01099  135 CYS B CA  
3186 C CA  B CYS B 135 ? 0.54170 0.41769 0.38237 0.01891  0.04087  0.01082  135 CYS B CA  
3187 C C   A CYS B 135 ? 0.54326 0.43598 0.37426 0.02379  0.04476  0.01423  135 CYS B C   
3188 C C   B CYS B 135 ? 0.54084 0.43375 0.37188 0.02399  0.04456  0.01415  135 CYS B C   
3189 O O   A CYS B 135 ? 0.55366 0.43509 0.35946 0.03162  0.04477  0.02067  135 CYS B O   
3190 O O   B CYS B 135 ? 0.54681 0.42861 0.35277 0.03212  0.04426  0.02046  135 CYS B O   
3191 C CB  A CYS B 135 ? 0.54631 0.38731 0.37010 0.01135  0.04859  0.01811  135 CYS B CB  
3192 C CB  B CYS B 135 ? 0.54551 0.38797 0.37144 0.01043  0.04890  0.01764  135 CYS B CB  
3193 S SG  A CYS B 135 ? 0.62957 0.47123 0.46328 -0.00957 0.06911  0.02140  135 CYS B SG  
3194 S SG  B CYS B 135 ? 0.59343 0.40123 0.41170 0.01264  0.03930  0.01429  135 CYS B SG  
3195 N N   . MET B 136 ? 0.45609 0.37331 0.30512 0.02075  0.04586  0.00866  136 MET B N   
3196 C CA  . MET B 136 ? 0.45359 0.38558 0.29592 0.02250  0.04938  0.00869  136 MET B CA  
3197 C C   . MET B 136 ? 0.52807 0.44874 0.35012 0.01991  0.05858  0.01489  136 MET B C   
3198 O O   . MET B 136 ? 0.49673 0.41506 0.29527 0.02873  0.05471  0.01802  136 MET B O   
3199 C CB  . MET B 136 ? 0.56572 0.51407 0.42802 0.01688  0.05291  0.00212  136 MET B CB  
3200 C CG  . MET B 136 ? 0.48227 0.44337 0.33877 0.01928  0.05216  -0.00116 136 MET B CG  
3201 S SD  . MET B 136 ? 0.34304 0.31086 0.21445 0.01779  0.05014  -0.00793 136 MET B SD  
3202 C CE  . MET B 136 ? 0.43012 0.40156 0.31107 0.01366  0.06021  -0.01266 136 MET B CE  
3203 N N   . GLY B 137 ? 0.48159 0.39882 0.31308 0.00820  0.07122  0.01507  137 GLY B N   
3204 C CA  . GLY B 137 ? 0.51466 0.42735 0.32660 0.00447  0.08422  0.01867  137 GLY B CA  
3205 C C   . GLY B 137 ? 0.52705 0.46053 0.33898 0.00942  0.08132  0.01154  137 GLY B C   
3206 O O   . GLY B 137 ? 0.55767 0.50845 0.39400 0.00923  0.07689  0.00331  137 GLY B O   
3207 N N   . LEU B 138 ? 0.53176 0.45924 0.31189 0.01452  0.08253  0.01430  138 LEU B N   
3208 C CA  . LEU B 138 ? 0.46332 0.40883 0.24212 0.01842  0.07697  0.00505  138 LEU B CA  
3209 C C   . LEU B 138 ? 0.50351 0.46298 0.29054 0.02544  0.06043  0.00069  138 LEU B C   
3210 O O   . LEU B 138 ? 0.50534 0.47993 0.29392 0.02572  0.05532  -0.00844 138 LEU B O   
3211 C CB  . LEU B 138 ? 0.48496 0.42082 0.22468 0.02266  0.08074  0.00683  138 LEU B CB  
3212 C CG  . LEU B 138 ? 0.53418 0.46223 0.26551 0.01402  0.10214  0.00749  138 LEU B CG  
3213 C CD1 . LEU B 138 ? 0.60936 0.52456 0.29159 0.02013  0.10547  0.00864  138 LEU B CD1 
3214 C CD2 . LEU B 138 ? 0.49305 0.44230 0.26177 0.00804  0.10823  -0.00497 138 LEU B CD2 
3215 N N   . GLY B 139 ? 0.44106 0.39608 0.23317 0.03021  0.05331  0.00543  139 GLY B N   
3216 C CA  . GLY B 139 ? 0.48945 0.46208 0.29592 0.03473  0.04264  -0.00016 139 GLY B CA  
3217 C C   . GLY B 139 ? 0.50808 0.49258 0.30133 0.04669  0.03080  -0.00292 139 GLY B C   
3218 O O   . GLY B 139 ? 0.46316 0.47175 0.27386 0.04740  0.02482  -0.01131 139 GLY B O   
3219 N N   . TYR B 140 ? 0.56325 0.53154 0.32556 0.05653  0.02740  0.00338  140 TYR B N   
3220 C CA  . TYR B 140 ? 0.52691 0.50827 0.27509 0.07273  0.01166  -0.00101 140 TYR B CA  
3221 C C   . TYR B 140 ? 0.43325 0.42537 0.19521 0.08517  0.00202  -0.00290 140 TYR B C   
3222 O O   . TYR B 140 ? 0.45638 0.48019 0.23036 0.09500  -0.01026 -0.01380 140 TYR B O   
3223 C CB  . TYR B 140 ? 0.47870 0.42952 0.18012 0.08390  0.00943  0.00893  140 TYR B CB  
3224 C CG  . TYR B 140 ? 0.60656 0.55193 0.28966 0.07468  0.01882  0.00777  140 TYR B CG  
3225 C CD1 . TYR B 140 ? 0.54371 0.51778 0.24812 0.06543  0.01828  -0.00656 140 TYR B CD1 
3226 C CD2 . TYR B 140 ? 0.57617 0.48467 0.21900 0.07408  0.03058  0.02039  140 TYR B CD2 
3227 C CE1 . TYR B 140 ? 0.59395 0.56163 0.28038 0.05892  0.02699  -0.00990 140 TYR B CE1 
3228 C CE2 . TYR B 140 ? 0.63065 0.53571 0.25532 0.06640  0.04205  0.01788  140 TYR B CE2 
3229 C CZ  . TYR B 140 ? 0.63294 0.56855 0.27974 0.06038  0.03906  0.00183  140 TYR B CZ  
3230 O OH  . TYR B 140 ? 0.60847 0.53941 0.23571 0.05480  0.05029  -0.00303 140 TYR B OH  
3231 N N   . THR B 141 ? 0.51545 0.48395 0.27730 0.08538  0.00718  0.00525  141 THR B N   
3232 C CA  . THR B 141 ? 0.52808 0.50459 0.30035 0.09886  -0.00065 0.00180  141 THR B CA  
3233 C C   . THR B 141 ? 0.47967 0.49179 0.28778 0.08972  0.00315  -0.00926 141 THR B C   
3234 O O   . THR B 141 ? 0.50559 0.54945 0.32996 0.09914  -0.00328 -0.01943 141 THR B O   
3235 C CB  . THR B 141 ? 0.48784 0.42409 0.24647 0.10039  0.00347  0.01173  141 THR B CB  
3236 O OG1 . THR B 141 ? 0.57061 0.47000 0.29060 0.11284  -0.00114 0.02203  141 THR B OG1 
3237 C CG2 . THR B 141 ? 0.50047 0.44546 0.27291 0.11147  -0.00148 0.00546  141 THR B CG2 
3238 N N   . ALA B 142 ? 0.53101 0.53770 0.35076 0.07186  0.01432  -0.00773 142 ALA B N   
3239 C CA  . ALA B 142 ? 0.47256 0.50183 0.31598 0.06167  0.02005  -0.01531 142 ALA B CA  
3240 C C   . ALA B 142 ? 0.45693 0.52093 0.31518 0.05736  0.01791  -0.02653 142 ALA B C   
3241 O O   . ALA B 142 ? 0.46095 0.55087 0.33910 0.05331  0.02153  -0.03496 142 ALA B O   
3242 C CB  . ALA B 142 ? 0.38715 0.39952 0.23371 0.04672  0.02897  -0.01141 142 ALA B CB  
3243 N N   . ILE B 143 ? 0.41083 0.47598 0.25907 0.05696  0.01300  -0.02808 143 ILE B N   
3244 C CA  . ILE B 143 ? 0.39706 0.49541 0.26016 0.05152  0.00830  -0.04189 143 ILE B CA  
3245 C C   . ILE B 143 ? 0.37742 0.51033 0.25392 0.06719  -0.00356 -0.05167 143 ILE B C   
3246 O O   . ILE B 143 ? 0.46181 0.63107 0.36864 0.05988  -0.00069 -0.06428 143 ILE B O   
3247 C CB  . ILE B 143 ? 0.40243 0.49103 0.24476 0.05088  0.00356  -0.04264 143 ILE B CB  
3248 C CG1 . ILE B 143 ? 0.50047 0.57197 0.34400 0.03319  0.01599  -0.04162 143 ILE B CG1 
3249 C CG2 . ILE B 143 ? 0.52239 0.64665 0.37487 0.05274  -0.00919 -0.05909 143 ILE B CG2 
3250 C CD1 . ILE B 143 ? 0.61611 0.70472 0.48461 0.01790  0.02137  -0.05139 143 ILE B CD1 
3251 N N   . GLU B 144 ? 0.40629 0.52715 0.25958 0.08939  -0.01638 -0.04638 144 GLU B N   
3252 C CA  . GLU B 144 ? 0.42154 0.57173 0.28423 0.11181  -0.03129 -0.05568 144 GLU B CA  
3253 C C   . GLU B 144 ? 0.49251 0.66349 0.38320 0.11249  -0.02294 -0.06096 144 GLU B C   
3254 O O   . GLU B 144 ? 0.52103 0.74104 0.44392 0.11746  -0.02701 -0.07734 144 GLU B O   
3255 C CB  . GLU B 144 ? 0.43269 0.54522 0.25392 0.13670  -0.04362 -0.04345 144 GLU B CB  
3256 C CG  . GLU B 144 ? 0.52414 0.65814 0.34712 0.16721  -0.06295 -0.05194 144 GLU B CG  
3257 C CD  . GLU B 144 ? 0.51734 0.69422 0.35059 0.17623  -0.08193 -0.06841 144 GLU B CD  
3258 O OE1 . GLU B 144 ? 0.64278 0.81497 0.46335 0.16233  -0.08190 -0.06877 144 GLU B OE1 
3259 O OE2 . GLU B 144 ? 0.58360 0.80092 0.43877 0.19835  -0.09789 -0.08314 144 GLU B OE2 
3260 N N   . ALA B 145 ? 0.42887 0.56572 0.30862 0.10728  -0.01081 -0.04908 145 ALA B N   
3261 C CA  . ALA B 145 ? 0.37832 0.52914 0.27600 0.10869  -0.00169 -0.05382 145 ALA B CA  
3262 C C   . ALA B 145 ? 0.36418 0.55495 0.29498 0.08815  0.01124  -0.06587 145 ALA B C   
3263 O O   . ALA B 145 ? 0.47491 0.70309 0.43073 0.09271  0.01599  -0.07791 145 ALA B O   
3264 C CB  . ALA B 145 ? 0.43651 0.54168 0.31357 0.10398  0.00705  -0.04056 145 ALA B CB  
3265 N N   . SER B 146 ? 0.42978 0.61245 0.36103 0.06510  0.01852  -0.06379 146 SER B N   
3266 C CA  . SER B 146 ? 0.46212 0.67063 0.41880 0.04224  0.03355  -0.07326 146 SER B CA  
3267 C C   . SER B 146 ? 0.45935 0.72215 0.44984 0.03895  0.02715  -0.09282 146 SER B C   
3268 O O   . SER B 146 ? 0.51764 0.81603 0.53869 0.02435  0.04043  -0.10494 146 SER B O   
3269 C CB  . SER B 146 ? 0.36648 0.54188 0.30996 0.02036  0.04275  -0.06542 146 SER B CB  
3270 O OG  . SER B 146 ? 0.48933 0.67350 0.43707 0.01294  0.03486  -0.07258 146 SER B OG  
3271 N N   . LYS B 147 ? 0.41202 0.68204 0.39670 0.05147  0.00741  -0.09700 147 LYS B N   
3272 C CA  . LYS B 147 ? 0.44577 0.77140 0.46334 0.05209  -0.00465 -0.11869 147 LYS B CA  
3273 C C   . LYS B 147 ? 0.41364 0.78935 0.46352 0.06978  -0.00787 -0.13238 147 LYS B C   
3274 O O   . LYS B 147 ? 0.42821 0.86383 0.52043 0.06592  -0.01312 -0.15480 147 LYS B O   
3275 C CB  . LYS B 147 ? 0.45512 0.77094 0.44793 0.06825  -0.02808 -0.11869 147 LYS B CB  
3276 C CG  . LYS B 147 ? 0.44587 0.71775 0.40947 0.05194  -0.02271 -0.10822 147 LYS B CG  
3277 C CD  . LYS B 147 ? 0.48944 0.76492 0.43528 0.06030  -0.04263 -0.11590 147 LYS B CD  
3278 C CE  . LYS B 147 ? 0.56178 0.80698 0.49204 0.03803  -0.03286 -0.11343 147 LYS B CE  
3279 N NZ  . LYS B 147 ? 0.53903 0.80525 0.50501 0.00842  -0.01991 -0.12736 147 LYS B NZ  
3280 N N   . ARG B 148 ? 0.47704 0.83122 0.51001 0.08959  -0.00529 -0.12163 148 ARG B N   
3281 C CA  . ARG B 148 ? 0.37385 0.77087 0.43638 0.10523  -0.00202 -0.13456 148 ARG B CA  
3282 C C   . ARG B 148 ? 0.41140 0.83113 0.50142 0.07814  0.02711  -0.14078 148 ARG B C   
3283 O O   . ARG B 148 ? 0.43618 0.89920 0.55586 0.08696  0.03553  -0.15434 148 ARG B O   
3284 C CB  . ARG B 148 ? 0.41059 0.76692 0.43945 0.13404  -0.00774 -0.12122 148 ARG B CB  
3285 C CG  . ARG B 148 ? 0.41664 0.72907 0.40417 0.15506  -0.03007 -0.10826 148 ARG B CG  
3286 C CD  . ARG B 148 ? 0.41095 0.76387 0.41232 0.17811  -0.05541 -0.12356 148 ARG B CD  
3287 N NE  . ARG B 148 ? 0.52927 0.83281 0.48090 0.19862  -0.07509 -0.10910 148 ARG B NE  
3288 C CZ  . ARG B 148 ? 0.60952 0.88368 0.53194 0.23223  -0.08947 -0.10247 148 ARG B CZ  
3289 N NH1 . ARG B 148 ? 0.58132 0.87176 0.52083 0.25204  -0.08818 -0.11047 148 ARG B NH1 
3290 N NH2 . ARG B 148 ? 0.54456 0.76816 0.41592 0.24658  -0.10423 -0.08761 148 ARG B NH2 
3291 N N   . GLY B 149 ? 0.42897 0.81853 0.50710 0.04687  0.04348  -0.13143 149 GLY B N   
3292 C CA  . GLY B 149 ? 0.43387 0.83001 0.52476 0.02027  0.07268  -0.13315 149 GLY B CA  
3293 C C   . GLY B 149 ? 0.53051 0.87437 0.58236 0.02193  0.08712  -0.11448 149 GLY B C   
3294 O O   . GLY B 149 ? 0.53021 0.87716 0.58451 0.00545  0.11191  -0.11516 149 GLY B O   
3295 N N   . ALA B 150 ? 0.51420 0.80945 0.52876 0.03987  0.07296  -0.09861 150 ALA B N   
3296 C CA  . ALA B 150 ? 0.45390 0.70199 0.43315 0.04359  0.08158  -0.08394 150 ALA B CA  
3297 C C   . ALA B 150 ? 0.42550 0.62441 0.37746 0.02439  0.08634  -0.06899 150 ALA B C   
3298 O O   . ALA B 150 ? 0.46081 0.64869 0.41136 0.01810  0.07641  -0.06604 150 ALA B O   
3299 C CB  . ALA B 150 ? 0.47084 0.69470 0.42901 0.07283  0.06371  -0.07785 150 ALA B CB  
3300 N N   . TYR B 151 ? 0.43651 0.60623 0.36490 0.01712  0.10122  -0.06084 151 TYR B N   
3301 C CA  . TYR B 151 ? 0.38662 0.50467 0.28401 0.00872  0.10037  -0.04630 151 TYR B CA  
3302 C C   . TYR B 151 ? 0.41956 0.51028 0.30002 0.02787  0.08184  -0.03860 151 TYR B C   
3303 O O   . TYR B 151 ? 0.52516 0.61500 0.39888 0.04521  0.07738  -0.04004 151 TYR B O   
3304 C CB  . TYR B 151 ? 0.40326 0.49549 0.27375 -0.00023 0.11878  -0.04005 151 TYR B CB  
3305 C CG  . TYR B 151 ? 0.42366 0.46452 0.26299 -0.00788 0.11685  -0.02680 151 TYR B CG  
3306 C CD1 . TYR B 151 ? 0.47621 0.48412 0.29345 0.00710  0.10120  -0.01874 151 TYR B CD1 
3307 C CD2 . TYR B 151 ? 0.46377 0.48887 0.29725 -0.02970 0.13012  -0.02397 151 TYR B CD2 
3308 C CE1 . TYR B 151 ? 0.48815 0.45507 0.28190 0.00381  0.09670  -0.00929 151 TYR B CE1 
3309 C CE2 . TYR B 151 ? 0.54681 0.52259 0.35045 -0.03198 0.12606  -0.01270 151 TYR B CE2 
3310 C CZ  . TYR B 151 ? 0.49518 0.44519 0.28061 -0.01353 0.10851  -0.00593 151 TYR B CZ  
3311 O OH  . TYR B 151 ? 0.61227 0.51904 0.37242 -0.01245 0.10248  0.00273  151 TYR B OH  
3312 N N   . VAL B 152 ? 0.43993 0.50767 0.31408 0.02392  0.07254  -0.03172 152 VAL B N   
3313 C CA  . VAL B 152 ? 0.47256 0.51923 0.33696 0.03713  0.05782  -0.02580 152 VAL B CA  
3314 C C   . VAL B 152 ? 0.39335 0.40376 0.24048 0.03240  0.05626  -0.01730 152 VAL B C   
3315 O O   . VAL B 152 ? 0.41519 0.41621 0.26127 0.02063  0.06030  -0.01521 152 VAL B O   
3316 C CB  . VAL B 152 ? 0.51202 0.57055 0.38688 0.03944  0.04815  -0.02741 152 VAL B CB  
3317 C CG1 . VAL B 152 ? 0.38505 0.42083 0.24711 0.05247  0.03735  -0.02097 152 VAL B CG1 
3318 C CG2 . VAL B 152 ? 0.36162 0.46173 0.25690 0.04337  0.04695  -0.03871 152 VAL B CG2 
3319 N N   . ILE B 153 ? 0.37390 0.36414 0.20876 0.04269  0.04882  -0.01432 153 ILE B N   
3320 C CA  . ILE B 153 ? 0.42445 0.38770 0.25048 0.04167  0.04212  -0.00954 153 ILE B CA  
3321 C C   . ILE B 153 ? 0.47152 0.43164 0.30680 0.04523  0.03358  -0.00854 153 ILE B C   
3322 O O   . ILE B 153 ? 0.47097 0.42937 0.30384 0.05391  0.02938  -0.00972 153 ILE B O   
3323 C CB  . ILE B 153 ? 0.44206 0.38549 0.24714 0.04848  0.03940  -0.00953 153 ILE B CB  
3324 C CG1 . ILE B 153 ? 0.41451 0.35469 0.20283 0.04263  0.05208  -0.00797 153 ILE B CG1 
3325 C CG2 . ILE B 153 ? 0.48811 0.41043 0.28993 0.05013  0.02771  -0.00806 153 ILE B CG2 
3326 C CD1 . ILE B 153 ? 0.61405 0.52765 0.37010 0.05019  0.04951  -0.00658 153 ILE B CD1 
3327 N N   . THR B 154 ? 0.40113 0.35860 0.24495 0.03852  0.03302  -0.00659 154 THR B N   
3328 C CA  . THR B 154 ? 0.40933 0.36283 0.25975 0.03836  0.03008  -0.00489 154 THR B CA  
3329 C C   . THR B 154 ? 0.42955 0.37324 0.28935 0.03459  0.02683  -0.00581 154 THR B C   
3330 O O   . THR B 154 ? 0.45907 0.40187 0.32108 0.03313  0.02662  -0.00715 154 THR B O   
3331 C CB  . THR B 154 ? 0.42757 0.39394 0.28059 0.03493  0.03450  -0.00425 154 THR B CB  
3332 O OG1 . THR B 154 ? 0.46145 0.41857 0.31360 0.03361  0.03526  -0.00085 154 THR B OG1 
3333 C CG2 . THR B 154 ? 0.44327 0.41489 0.30155 0.02703  0.03908  -0.00668 154 THR B CG2 
3334 N N   . ILE B 155 ? 0.42457 0.35997 0.29048 0.03351  0.02373  -0.00628 155 ILE B N   
3335 C CA  . ILE B 155 ? 0.50786 0.44197 0.39132 0.02961  0.01920  -0.01109 155 ILE B CA  
3336 C C   . ILE B 155 ? 0.44185 0.38087 0.34014 0.02017  0.02821  -0.01033 155 ILE B C   
3337 O O   . ILE B 155 ? 0.51056 0.43862 0.40071 0.01653  0.03314  -0.00588 155 ILE B O   
3338 C CB  . ILE B 155 ? 0.43116 0.35304 0.31397 0.03215  0.00870  -0.01611 155 ILE B CB  
3339 C CG1 . ILE B 155 ? 0.48075 0.39532 0.34263 0.04242  0.00157  -0.01742 155 ILE B CG1 
3340 C CG2 . ILE B 155 ? 0.43490 0.36378 0.34467 0.02663  0.00240  -0.02465 155 ILE B CG2 
3341 C CD1 . ILE B 155 ? 0.42216 0.32106 0.27526 0.04672  -0.00800 -0.02336 155 ILE B CD1 
3342 N N   . GLU B 156 ? 0.41982 0.37208 0.33715 0.01725  0.03108  -0.01487 156 GLU B N   
3343 C CA  . GLU B 156 ? 0.48170 0.44285 0.41642 0.00748  0.04292  -0.01653 156 GLU B CA  
3344 C C   . GLU B 156 ? 0.47463 0.45124 0.44413 0.00472  0.03806  -0.02780 156 GLU B C   
3345 O O   . GLU B 156 ? 0.48573 0.47127 0.46516 0.01433  0.02790  -0.03424 156 GLU B O   
3346 C CB  . GLU B 156 ? 0.41224 0.38172 0.34142 0.00802  0.05300  -0.01536 156 GLU B CB  
3347 C CG  . GLU B 156 ? 0.41171 0.39094 0.35428 -0.00124 0.06897  -0.01769 156 GLU B CG  
3348 C CD  . GLU B 156 ? 0.48694 0.45170 0.42014 -0.01193 0.07847  -0.01088 156 GLU B CD  
3349 O OE1 . GLU B 156 ? 0.53913 0.48415 0.44105 -0.00849 0.07661  -0.00141 156 GLU B OE1 
3350 O OE2 . GLU B 156 ? 0.52650 0.49872 0.48425 -0.02371 0.08769  -0.01572 156 GLU B OE2 
3351 N N   . LYS B 157 ? 0.39434 0.37318 0.38223 -0.00832 0.04497  -0.03090 157 LYS B N   
3352 C CA  . LYS B 157 ? 0.46911 0.47195 0.49980 -0.01317 0.04056  -0.04541 157 LYS B CA  
3353 C C   . LYS B 157 ? 0.53829 0.56908 0.59511 -0.01248 0.05134  -0.05254 157 LYS B C   
3354 O O   . LYS B 157 ? 0.54675 0.60107 0.63410 -0.00352 0.03995  -0.06565 157 LYS B O   
3355 C CB  . LYS B 157 ? 0.52000 0.51758 0.56662 -0.03214 0.04785  -0.04843 157 LYS B CB  
3356 C CG  . LYS B 157 ? 0.58885 0.61913 0.68870 -0.03955 0.04167  -0.06760 157 LYS B CG  
3357 C CD  . LYS B 157 ? 0.60691 0.65251 0.71787 -0.01937 0.01485  -0.07876 157 LYS B CD  
3358 C CE  . LYS B 157 ? 0.60895 0.67291 0.75834 -0.02513 -0.00194 -0.09761 157 LYS B CE  
3359 N NZ  . LYS B 157 ? 0.61642 0.68782 0.79654 -0.05349 0.01709  -0.10289 157 LYS B NZ  
3360 N N   . ASP B 158 ? 0.50688 0.53490 0.55020 -0.01920 0.07194  -0.04542 158 ASP B N   
3361 C CA  . ASP B 158 ? 0.49831 0.55376 0.56791 -0.02053 0.08660  -0.05451 158 ASP B CA  
3362 C C   . ASP B 158 ? 0.47737 0.53155 0.53119 -0.00330 0.08126  -0.05479 158 ASP B C   
3363 O O   . ASP B 158 ? 0.51080 0.54332 0.52612 -0.00100 0.08357  -0.04401 158 ASP B O   
3364 C CB  . ASP B 158 ? 0.45816 0.50820 0.51647 -0.03744 0.11408  -0.04783 158 ASP B CB  
3365 C CG  . ASP B 158 ? 0.44951 0.53222 0.53964 -0.04118 0.13332  -0.05989 158 ASP B CG  
3366 O OD1 . ASP B 158 ? 0.46104 0.56601 0.57323 -0.02548 0.12398  -0.07178 158 ASP B OD1 
3367 O OD2 . ASP B 158 ? 0.52162 0.60577 0.61294 -0.05916 0.15907  -0.05775 158 ASP B OD2 
3368 N N   . PRO B 159 ? 0.51637 0.59185 0.59886 0.00946  0.07307  -0.06806 159 PRO B N   
3369 C CA  . PRO B 159 ? 0.52381 0.59003 0.58836 0.02486  0.06986  -0.06881 159 PRO B CA  
3370 C C   . PRO B 159 ? 0.47749 0.54281 0.52586 0.01975  0.09139  -0.06735 159 PRO B C   
3371 O O   . PRO B 159 ? 0.53288 0.57863 0.55134 0.02636  0.08929  -0.06370 159 PRO B O   
3372 C CB  . PRO B 159 ? 0.50775 0.59780 0.61045 0.04105  0.05783  -0.08533 159 PRO B CB  
3373 C CG  . PRO B 159 ? 0.37664 0.48747 0.51348 0.03570  0.04752  -0.09259 159 PRO B CG  
3374 C CD  . PRO B 159 ? 0.48413 0.59073 0.61586 0.01210  0.06298  -0.08418 159 PRO B CD  
3375 N N   . ASN B 160 ? 0.49732 0.58204 0.56286 0.00711  0.11289  -0.07109 160 ASN B N   
3376 C CA  . ASN B 160 ? 0.48720 0.56930 0.53076 0.00357  0.13448  -0.07045 160 ASN B CA  
3377 C C   . ASN B 160 ? 0.48036 0.53150 0.47291 -0.00350 0.13724  -0.05414 160 ASN B C   
3378 O O   . ASN B 160 ? 0.51802 0.56029 0.48114 -0.00164 0.14683  -0.05366 160 ASN B O   
3379 C CB  . ASN B 160 ? 0.49272 0.60308 0.56554 -0.00930 0.16062  -0.07854 160 ASN B CB  
3380 C CG  . ASN B 160 ? 0.46854 0.62009 0.60135 -0.00154 0.15751  -0.09839 160 ASN B CG  
3381 O OD1 . ASN B 160 ? 0.56968 0.72987 0.71279 0.01806  0.14924  -0.10990 160 ASN B OD1 
3382 N ND2 . ASN B 160 ? 0.46950 0.64597 0.64323 -0.01610 0.16246  -0.10397 160 ASN B ND2 
3383 N N   . VAL B 161 ? 0.43892 0.47442 0.42044 -0.00980 0.12806  -0.04276 161 VAL B N   
3384 C CA  . VAL B 161 ? 0.54677 0.55557 0.48298 -0.01068 0.12510  -0.02922 161 VAL B CA  
3385 C C   . VAL B 161 ? 0.49444 0.49570 0.41603 0.00075  0.10808  -0.02996 161 VAL B C   
3386 O O   . VAL B 161 ? 0.53569 0.52582 0.42574 0.00255  0.10696  -0.02599 161 VAL B O   
3387 C CB  . VAL B 161 ? 0.51936 0.51264 0.45010 -0.01832 0.12063  -0.01893 161 VAL B CB  
3388 C CG1 . VAL B 161 ? 0.51729 0.48663 0.40624 -0.01284 0.11166  -0.00727 161 VAL B CG1 
3389 C CG2 . VAL B 161 ? 0.49212 0.48433 0.42972 -0.03468 0.14222  -0.01674 161 VAL B CG2 
3390 N N   . ILE B 162 ? 0.44642 0.45292 0.38958 0.00820  0.09486  -0.03596 162 ILE B N   
3391 C CA  . ILE B 162 ? 0.48273 0.47717 0.41058 0.01554  0.08295  -0.03624 162 ILE B CA  
3392 C C   . ILE B 162 ? 0.46379 0.45737 0.38436 0.01937  0.08968  -0.04506 162 ILE B C   
3393 O O   . ILE B 162 ? 0.47591 0.45791 0.37402 0.01872  0.08635  -0.04501 162 ILE B O   
3394 C CB  . ILE B 162 ? 0.49745 0.48830 0.43988 0.02318  0.06789  -0.03790 162 ILE B CB  
3395 C CG1 . ILE B 162 ? 0.49076 0.47978 0.43499 0.01967  0.06050  -0.03107 162 ILE B CG1 
3396 C CG2 . ILE B 162 ? 0.49328 0.46495 0.41525 0.02745  0.06013  -0.03667 162 ILE B CG2 
3397 C CD1 . ILE B 162 ? 0.46532 0.44427 0.40844 0.02798  0.04451  -0.03084 162 ILE B CD1 
3398 N N   . GLU B 163 ? 0.42833 0.43601 0.36981 0.02316  0.09947  -0.05505 163 GLU B N   
3399 C CA  . GLU B 163 ? 0.51297 0.51755 0.44514 0.02872  0.10686  -0.06561 163 GLU B CA  
3400 C C   . GLU B 163 ? 0.45816 0.45909 0.35869 0.02149  0.11876  -0.06349 163 GLU B C   
3401 O O   . GLU B 163 ? 0.52993 0.51911 0.40832 0.02366  0.11723  -0.06974 163 GLU B O   
3402 C CB  . GLU B 163 ? 0.50950 0.53472 0.47473 0.03753  0.11544  -0.07919 163 GLU B CB  
3403 C CG  . GLU B 163 ? 0.59966 0.62262 0.58796 0.05233  0.09843  -0.08500 163 GLU B CG  
3404 C CD  . GLU B 163 ? 0.54097 0.52847 0.50052 0.05669  0.08358  -0.08000 163 GLU B CD  
3405 O OE1 . GLU B 163 ? 0.70868 0.67787 0.65239 0.06225  0.08540  -0.08747 163 GLU B OE1 
3406 O OE2 . GLU B 163 ? 0.62179 0.59801 0.57397 0.05367  0.07153  -0.06955 163 GLU B OE2 
3407 N N   . ILE B 164 ? 0.43475 0.44149 0.32876 0.01306  0.12979  -0.05521 164 ILE B N   
3408 C CA  . ILE B 164 ? 0.55222 0.54877 0.40582 0.00938  0.13793  -0.05099 164 ILE B CA  
3409 C C   . ILE B 164 ? 0.49151 0.47520 0.32050 0.01066  0.11994  -0.04627 164 ILE B C   
3410 O O   . ILE B 164 ? 0.57464 0.55222 0.37471 0.01245  0.11806  -0.05118 164 ILE B O   
3411 C CB  . ILE B 164 ? 0.46096 0.45591 0.30513 0.00014  0.15340  -0.04002 164 ILE B CB  
3412 C CG1 . ILE B 164 ? 0.59646 0.60972 0.46402 -0.00431 0.17720  -0.04839 164 ILE B CG1 
3413 C CG2 . ILE B 164 ? 0.51049 0.48563 0.30128 0.00029  0.15570  -0.03187 164 ILE B CG2 
3414 C CD1 . ILE B 164 ? 0.47625 0.49069 0.32105 0.00086  0.19229  -0.05954 164 ILE B CD1 
3415 N N   . ALA B 165 ? 0.55255 0.53503 0.39426 0.00991  0.10641  -0.03900 165 ALA B N   
3416 C CA  . ALA B 165 ? 0.52241 0.50065 0.34975 0.01052  0.09142  -0.03713 165 ALA B CA  
3417 C C   . ALA B 165 ? 0.51624 0.49164 0.34526 0.01051  0.08581  -0.04893 165 ALA B C   
3418 O O   . ALA B 165 ? 0.59978 0.57596 0.41386 0.00829  0.07795  -0.05342 165 ALA B O   
3419 C CB  . ALA B 165 ? 0.49784 0.47627 0.33927 0.01025  0.08166  -0.02855 165 ALA B CB  
3420 N N   . ARG B 166 ? 0.50884 0.47975 0.35609 0.01328  0.08874  -0.05526 166 ARG B N   
3421 C CA  . ARG B 166 ? 0.58051 0.53793 0.42452 0.01297  0.08449  -0.06577 166 ARG B CA  
3422 C C   . ARG B 166 ? 0.57794 0.53317 0.39986 0.01191  0.08824  -0.07752 166 ARG B C   
3423 O O   . ARG B 166 ? 0.64719 0.59256 0.46033 0.00646  0.08166  -0.08639 166 ARG B O   
3424 C CB  . ARG B 166 ? 0.56786 0.51543 0.42975 0.02145  0.08599  -0.07057 166 ARG B CB  
3425 C CG  . ARG B 166 ? 0.56621 0.50032 0.43483 0.02159  0.07587  -0.06353 166 ARG B CG  
3426 C CD  . ARG B 166 ? 0.57151 0.48599 0.44729 0.03329  0.07259  -0.06871 166 ARG B CD  
3427 N NE  . ARG B 166 ? 0.67566 0.59253 0.56459 0.03953  0.06454  -0.06019 166 ARG B NE  
3428 C CZ  . ARG B 166 ? 0.72147 0.62292 0.59910 0.03564  0.05724  -0.05081 166 ARG B CZ  
3429 N NH1 . ARG B 166 ? 0.57991 0.46710 0.43915 0.02323  0.05899  -0.04859 166 ARG B NH1 
3430 N NH2 . ARG B 166 ? 0.85385 0.75647 0.73954 0.04361  0.04863  -0.04512 166 ARG B NH2 
3431 N N   . ILE B 167 ? 0.56573 0.52854 0.37645 0.01568  0.09969  -0.07880 167 ILE B N   
3432 C CA  . ILE B 167 ? 0.58451 0.54285 0.36711 0.01669  0.10321  -0.09100 167 ILE B CA  
3433 C C   . ILE B 167 ? 0.57954 0.54323 0.33261 0.01478  0.09705  -0.08578 167 ILE B C   
3434 O O   . ILE B 167 ? 0.63271 0.59270 0.35623 0.01646  0.09527  -0.09631 167 ILE B O   
3435 C CB  . ILE B 167 ? 0.57429 0.53521 0.35630 0.02379  0.12206  -0.09829 167 ILE B CB  
3436 C CG1 . ILE B 167 ? 0.69169 0.64157 0.44554 0.02716  0.12467  -0.11613 167 ILE B CG1 
3437 C CG2 . ILE B 167 ? 0.51755 0.48933 0.29157 0.02209  0.13605  -0.08635 167 ILE B CG2 
3438 C CD1 . ILE B 167 ? 0.66613 0.59803 0.42201 0.02365  0.10936  -0.12788 167 ILE B CD1 
3439 N N   . ASN B 168 ? 0.57052 0.54079 0.32836 0.01357  0.09142  -0.07112 168 ASN B N   
3440 C CA  . ASN B 168 ? 0.50892 0.48190 0.23821 0.01644  0.08187  -0.06596 168 ASN B CA  
3441 C C   . ASN B 168 ? 0.61687 0.60018 0.35135 0.01326  0.06292  -0.07608 168 ASN B C   
3442 O O   . ASN B 168 ? 0.59002 0.57939 0.35344 0.00732  0.05770  -0.07483 168 ASN B O   
3443 C CB  . ASN B 168 ? 0.51827 0.49072 0.25194 0.01803  0.08252  -0.04813 168 ASN B CB  
3444 C CG  . ASN B 168 ? 0.54711 0.51617 0.24684 0.02584  0.07187  -0.04138 168 ASN B CG  
3445 O OD1 . ASN B 168 ? 0.51509 0.48173 0.18161 0.03126  0.06640  -0.04860 168 ASN B OD1 
3446 N ND2 . ASN B 168 ? 0.51935 0.48604 0.22438 0.02886  0.06687  -0.02859 168 ASN B ND2 
3447 N N   . PRO B 169 ? 0.57377 0.56063 0.28158 0.01610  0.05278  -0.08752 169 PRO B N   
3448 C CA  . PRO B 169 ? 0.53798 0.54307 0.25938 0.01076  0.03409  -0.09982 169 PRO B CA  
3449 C C   . PRO B 169 ? 0.61677 0.64044 0.34782 0.01613  0.02175  -0.09052 169 PRO B C   
3450 O O   . PRO B 169 ? 0.54542 0.59018 0.30436 0.00882  0.01186  -0.09873 169 PRO B O   
3451 C CB  . PRO B 169 ? 0.53734 0.54264 0.22553 0.01457  0.02456  -0.11681 169 PRO B CB  
3452 C CG  . PRO B 169 ? 0.61170 0.59832 0.25777 0.02610  0.03703  -0.10709 169 PRO B CG  
3453 C CD  . PRO B 169 ? 0.59372 0.56963 0.25711 0.02405  0.05794  -0.09091 169 PRO B CD  
3454 N N   . TRP B 170 ? 0.61935 0.63438 0.32897 0.02812  0.02369  -0.07427 170 TRP B N   
3455 C CA  . TRP B 170 ? 0.51024 0.53837 0.22933 0.03608  0.01217  -0.06604 170 TRP B CA  
3456 C C   . TRP B 170 ? 0.51779 0.54655 0.27153 0.02924  0.02065  -0.05663 170 TRP B C   
3457 O O   . TRP B 170 ? 0.46493 0.50468 0.22916 0.03589  0.01278  -0.05148 170 TRP B O   
3458 C CB  . TRP B 170 ? 0.55673 0.56559 0.23314 0.05254  0.00989  -0.05172 170 TRP B CB  
3459 C CG  . TRP B 170 ? 0.64464 0.65150 0.27814 0.06408  -0.00323 -0.05998 170 TRP B CG  
3460 C CD1 . TRP B 170 ? 0.58267 0.57454 0.18411 0.06222  0.00485  -0.06593 170 TRP B CD1 
3461 C CD2 . TRP B 170 ? 0.70779 0.72859 0.32327 0.08205  -0.02855 -0.06484 170 TRP B CD2 
3462 N NE1 . TRP B 170 ? 0.72182 0.71395 0.28233 0.07668  -0.01391 -0.07316 170 TRP B NE1 
3463 C CE2 . TRP B 170 ? 0.69353 0.70437 0.26350 0.08975  -0.03625 -0.07282 170 TRP B CE2 
3464 C CE3 . TRP B 170 ? 0.71852 0.76069 0.35305 0.09431  -0.04615 -0.06466 170 TRP B CE3 
3465 C CZ2 . TRP B 170 ? 0.81455 0.83434 0.36819 0.10589  -0.06182 -0.07781 170 TRP B CZ2 
3466 C CZ3 . TRP B 170 ? 0.66619 0.72176 0.27643 0.11571  -0.07289 -0.07307 170 TRP B CZ3 
3467 C CH2 . TRP B 170 ? 0.78419 0.82706 0.35879 0.11990  -0.08059 -0.07821 170 TRP B CH2 
3468 N N   . SER B 171 ? 0.47519 0.49235 0.24493 0.01871  0.03482  -0.05573 171 SER B N   
3469 C CA  . SER B 171 ? 0.54508 0.55940 0.34120 0.01420  0.04085  -0.04747 171 SER B CA  
3470 C C   . SER B 171 ? 0.50415 0.52348 0.32443 0.00226  0.04148  -0.05639 171 SER B C   
3471 O O   . SER B 171 ? 0.52369 0.53577 0.35912 -0.00074 0.04639  -0.04994 171 SER B O   
3472 C CB  . SER B 171 ? 0.52388 0.51947 0.31901 0.01417  0.05480  -0.03844 171 SER B CB  
3473 O OG  . SER B 171 ? 0.46651 0.45260 0.24222 0.02101  0.05747  -0.02691 171 SER B OG  
3474 N N   . ARG B 172 ? 0.46214 0.49052 0.28290 -0.00510 0.03628  -0.07131 172 ARG B N   
3475 C CA  . ARG B 172 ? 0.46279 0.48409 0.29944 -0.01980 0.04055  -0.07990 172 ARG B CA  
3476 C C   . ARG B 172 ? 0.53561 0.56326 0.39266 -0.02665 0.04313  -0.07438 172 ARG B C   
3477 O O   . ARG B 172 ? 0.57551 0.58132 0.43645 -0.03431 0.05133  -0.07131 172 ARG B O   
3478 C CB  . ARG B 172 ? 0.42114 0.45435 0.25678 -0.02899 0.03275  -0.09919 172 ARG B CB  
3479 C CG  . ARG B 172 ? 0.52509 0.53867 0.33806 -0.02618 0.03519  -0.10745 172 ARG B CG  
3480 C CD  . ARG B 172 ? 0.51189 0.52558 0.32593 -0.03976 0.02949  -0.12900 172 ARG B CD  
3481 N NE  . ARG B 172 ? 0.63151 0.62793 0.41802 -0.03327 0.03064  -0.13868 172 ARG B NE  
3482 C CZ  . ARG B 172 ? 0.64652 0.65319 0.41593 -0.03303 0.01886  -0.15620 172 ARG B CZ  
3483 N NH1 . ARG B 172 ? 0.58099 0.61920 0.36303 -0.03873 0.00268  -0.16745 172 ARG B NH1 
3484 N NH2 . ARG B 172 ? 0.67960 0.66715 0.41892 -0.02551 0.02281  -0.16438 172 ARG B NH2 
3485 N N   . GLU B 173 ? 0.46493 0.52011 0.33175 -0.02232 0.03645  -0.07356 173 GLU B N   
3486 C CA  . GLU B 173 ? 0.54488 0.60771 0.42995 -0.03021 0.04230  -0.07097 173 GLU B CA  
3487 C C   . GLU B 173 ? 0.51901 0.55798 0.39770 -0.02377 0.04924  -0.05523 173 GLU B C   
3488 O O   . GLU B 173 ? 0.48191 0.52047 0.36749 -0.02910 0.05556  -0.05187 173 GLU B O   
3489 C CB  . GLU B 173 ? 0.48760 0.59041 0.38890 -0.02462 0.03405  -0.07681 173 GLU B CB  
3490 C CG  . GLU B 173 ? 0.49242 0.62767 0.40468 -0.02839 0.02227  -0.09550 173 GLU B CG  
3491 C CD  . GLU B 173 ? 0.60470 0.74190 0.49354 -0.00876 0.00726  -0.09484 173 GLU B CD  
3492 O OE1 . GLU B 173 ? 0.60643 0.71163 0.46900 -0.00091 0.01150  -0.08216 173 GLU B OE1 
3493 O OE2 . GLU B 173 ? 0.57611 0.74677 0.47191 -0.00099 -0.00848 -0.10749 173 GLU B OE2 
3494 N N   . LEU B 174 ? 0.47193 0.49259 0.33793 -0.01329 0.04879  -0.04692 174 LEU B N   
3495 C CA  . LEU B 174 ? 0.50516 0.50579 0.36939 -0.00854 0.05269  -0.03601 174 LEU B CA  
3496 C C   . LEU B 174 ? 0.48813 0.46339 0.34968 -0.01597 0.05857  -0.03613 174 LEU B C   
3497 O O   . LEU B 174 ? 0.52114 0.48110 0.37882 -0.01247 0.05971  -0.02852 174 LEU B O   
3498 C CB  . LEU B 174 ? 0.54411 0.53584 0.40258 0.00106  0.05219  -0.03032 174 LEU B CB  
3499 C CG  . LEU B 174 ? 0.52537 0.52697 0.37675 0.00946  0.04801  -0.02576 174 LEU B CG  
3500 C CD1 . LEU B 174 ? 0.47877 0.46824 0.32456 0.01267  0.05311  -0.02082 174 LEU B CD1 
3501 C CD2 . LEU B 174 ? 0.48945 0.49504 0.34499 0.01459  0.04438  -0.02042 174 LEU B CD2 
3502 N N   . PHE B 175 ? 0.55205 0.51769 0.41091 -0.02442 0.06101  -0.04493 175 PHE B N   
3503 C CA  . PHE B 175 ? 0.60199 0.53280 0.45178 -0.02678 0.06518  -0.04460 175 PHE B CA  
3504 C C   . PHE B 175 ? 0.56645 0.48254 0.41232 -0.04477 0.07163  -0.05053 175 PHE B C   
3505 O O   . PHE B 175 ? 0.65419 0.53237 0.48631 -0.04717 0.07517  -0.05041 175 PHE B O   
3506 C CB  . PHE B 175 ? 0.52526 0.44680 0.37215 -0.01877 0.06422  -0.05054 175 PHE B CB  
3507 C CG  . PHE B 175 ? 0.56777 0.50677 0.42058 -0.00666 0.06235  -0.04646 175 PHE B CG  
3508 C CD1 . PHE B 175 ? 0.55268 0.48812 0.41186 0.00267  0.06044  -0.03821 175 PHE B CD1 
3509 C CD2 . PHE B 175 ? 0.51096 0.46754 0.36032 -0.00568 0.06270  -0.05128 175 PHE B CD2 
3510 C CE1 . PHE B 175 ? 0.51021 0.46040 0.37779 0.00914  0.06107  -0.03552 175 PHE B CE1 
3511 C CE2 . PHE B 175 ? 0.50109 0.46719 0.35144 0.00221  0.06490  -0.04571 175 PHE B CE2 
3512 C CZ  . PHE B 175 ? 0.51011 0.47357 0.37240 0.00776  0.06522  -0.03823 175 PHE B CZ  
3513 N N   . THR B 176 ? 0.59188 0.53601 0.45030 -0.05752 0.07351  -0.05657 176 THR B N   
3514 C CA  . THR B 176 ? 0.67150 0.60557 0.53174 -0.07975 0.08280  -0.06353 176 THR B CA  
3515 C C   . THR B 176 ? 0.69348 0.66897 0.57447 -0.08845 0.08633  -0.06665 176 THR B C   
3516 O O   . THR B 176 ? 0.63210 0.64678 0.52740 -0.07779 0.07681  -0.07033 176 THR B O   
3517 C CB  . THR B 176 ? 0.72628 0.65636 0.58859 -0.09060 0.08006  -0.07999 176 THR B CB  
3518 O OG1 . THR B 176 ? 0.76355 0.69299 0.63550 -0.11716 0.08917  -0.09006 176 THR B OG1 
3519 C CG2 . THR B 176 ? 0.66367 0.63407 0.53662 -0.08123 0.06767  -0.08961 176 THR B CG2 
3520 N N   . GLY B 177 ? 0.68661 0.65126 0.56679 -0.10619 0.10102  -0.06478 177 GLY B N   
3521 C CA  . GLY B 177 ? 0.76246 0.77062 0.66720 -0.11655 0.10847  -0.07084 177 GLY B CA  
3522 C C   . GLY B 177 ? 0.85207 0.85321 0.74456 -0.11093 0.11915  -0.05730 177 GLY B C   
3523 O O   . GLY B 177 ? 0.91671 0.94494 0.82558 -0.12444 0.13288  -0.06241 177 GLY B O   
3524 N N   . GLY B 178 ? 0.74572 0.71502 0.61167 -0.09130 0.11329  -0.04244 178 GLY B N   
3525 C CA  . GLY B 178 ? 0.76485 0.71921 0.61093 -0.08548 0.12185  -0.03057 178 GLY B CA  
3526 C C   . GLY B 178 ? 0.73021 0.72681 0.59242 -0.07267 0.11908  -0.03269 178 GLY B C   
3527 O O   . GLY B 178 ? 0.72278 0.70749 0.56620 -0.06649 0.12600  -0.02473 178 GLY B O   
3528 N N   . LYS B 179 ? 0.66013 0.70191 0.55203 -0.06656 0.10841  -0.04366 179 LYS B N   
3529 C CA  . LYS B 179 ? 0.56413 0.63840 0.46722 -0.04885 0.10234  -0.04536 179 LYS B CA  
3530 C C   . LYS B 179 ? 0.51919 0.57266 0.40508 -0.02671 0.08755  -0.03543 179 LYS B C   
3531 O O   . LYS B 179 ? 0.52379 0.58625 0.40791 -0.01211 0.08449  -0.03388 179 LYS B O   
3532 C CB  . LYS B 179 ? 0.53004 0.65718 0.46736 -0.04686 0.09376  -0.06093 179 LYS B CB  
3533 C CG  . LYS B 179 ? 0.56025 0.72694 0.52883 -0.06799 0.10691  -0.07647 179 LYS B CG  
3534 C CD  . LYS B 179 ? 0.56234 0.78948 0.56437 -0.05282 0.09705  -0.09095 179 LYS B CD  
3535 C CE  . LYS B 179 ? 0.71345 0.99586 0.76019 -0.07198 0.10146  -0.11334 179 LYS B CE  
3536 N NZ  . LYS B 179 ? 0.62258 0.88556 0.67094 -0.10626 0.11709  -0.11672 179 LYS B NZ  
3537 N N   . ILE B 180 ? 0.60752 0.63511 0.48310 -0.02447 0.07926  -0.03062 180 ILE B N   
3538 C CA  . ILE B 180 ? 0.55204 0.56596 0.41883 -0.00774 0.06727  -0.02373 180 ILE B CA  
3539 C C   . ILE B 180 ? 0.52983 0.50545 0.37740 -0.00609 0.06708  -0.01541 180 ILE B C   
3540 O O   . ILE B 180 ? 0.51018 0.46633 0.35247 -0.01311 0.06915  -0.01535 180 ILE B O   
3541 C CB  . ILE B 180 ? 0.50244 0.52544 0.37624 -0.00402 0.05817  -0.02704 180 ILE B CB  
3542 C CG1 . ILE B 180 ? 0.51581 0.57505 0.40577 -0.00588 0.05533  -0.03767 180 ILE B CG1 
3543 C CG2 . ILE B 180 ? 0.45780 0.47216 0.32519 0.01052  0.04993  -0.02046 180 ILE B CG2 
3544 C CD1 . ILE B 180 ? 0.51712 0.59508 0.41078 0.00940  0.04909  -0.03773 180 ILE B CD1 
3545 N N   . GLN B 181 ? 0.48851 0.45297 0.32571 0.00539  0.06211  -0.01017 181 GLN B N   
3546 C CA  . GLN B 181 ? 0.47562 0.40914 0.29700 0.01136  0.05655  -0.00467 181 GLN B CA  
3547 C C   . GLN B 181 ? 0.48276 0.41937 0.31642 0.02017  0.04541  -0.00530 181 GLN B C   
3548 O O   . GLN B 181 ? 0.53908 0.48696 0.37875 0.02566  0.04136  -0.00591 181 GLN B O   
3549 C CB  . GLN B 181 ? 0.55674 0.47523 0.35563 0.01702  0.05784  -0.00086 181 GLN B CB  
3550 C CG  . GLN B 181 ? 0.57585 0.45992 0.35167 0.02448  0.05027  0.00403  181 GLN B CG  
3551 C CD  . GLN B 181 ? 0.63981 0.50730 0.38597 0.03154  0.05057  0.00711  181 GLN B CD  
3552 O OE1 . GLN B 181 ? 0.66556 0.54105 0.40300 0.02551  0.06459  0.00715  181 GLN B OE1 
3553 N NE2 . GLN B 181 ? 0.59247 0.43972 0.32371 0.04506  0.03495  0.00773  181 GLN B NE2 
3554 N N   . VAL B 182 ? 0.49102 0.41695 0.32888 0.02094  0.04214  -0.00600 182 VAL B N   
3555 C CA  . VAL B 182 ? 0.50320 0.43586 0.35747 0.02590  0.03590  -0.00825 182 VAL B CA  
3556 C C   . VAL B 182 ? 0.50995 0.42940 0.36278 0.03527  0.02517  -0.00884 182 VAL B C   
3557 O O   . VAL B 182 ? 0.48523 0.38706 0.32858 0.04036  0.02145  -0.00879 182 VAL B O   
3558 C CB  . VAL B 182 ? 0.41373 0.35049 0.27810 0.02233  0.04025  -0.01222 182 VAL B CB  
3559 C CG1 . VAL B 182 ? 0.46079 0.40817 0.34332 0.02507  0.03878  -0.01490 182 VAL B CG1 
3560 C CG2 . VAL B 182 ? 0.48300 0.43263 0.34560 0.01415  0.04712  -0.01391 182 VAL B CG2 
3561 N N   . ILE B 183 ? 0.51072 0.43605 0.37129 0.03854  0.01849  -0.01041 183 ILE B N   
3562 C CA  . ILE B 183 ? 0.56311 0.48320 0.42968 0.04683  0.00500  -0.01511 183 ILE B CA  
3563 C C   . ILE B 183 ? 0.49353 0.43233 0.39277 0.04280  0.00513  -0.02134 183 ILE B C   
3564 O O   . ILE B 183 ? 0.55169 0.49854 0.45835 0.03451  0.01315  -0.01971 183 ILE B O   
3565 C CB  . ILE B 183 ? 0.46860 0.38002 0.32017 0.05159  -0.00320 -0.01571 183 ILE B CB  
3566 C CG1 . ILE B 183 ? 0.57031 0.46124 0.38652 0.05699  -0.00233 -0.01065 183 ILE B CG1 
3567 C CG2 . ILE B 183 ? 0.50687 0.41998 0.37294 0.05803  -0.01985 -0.02463 183 ILE B CG2 
3568 C CD1 . ILE B 183 ? 0.59942 0.49352 0.40495 0.04889  0.01388  -0.00510 183 ILE B CD1 
3569 N N   . GLN B 184 ? 0.44230 0.38720 0.35972 0.04929  -0.00276 -0.02865 184 GLN B N   
3570 C CA  . GLN B 184 ? 0.46775 0.43612 0.42261 0.04464  -0.00202 -0.03778 184 GLN B CA  
3571 C C   . GLN B 184 ? 0.46293 0.43633 0.43220 0.04827  -0.01888 -0.04685 184 GLN B C   
3572 O O   . GLN B 184 ? 0.55964 0.52729 0.52302 0.06267  -0.03616 -0.05179 184 GLN B O   
3573 C CB  . GLN B 184 ? 0.51173 0.49224 0.48581 0.05097  0.00006  -0.04451 184 GLN B CB  
3574 C CG  . GLN B 184 ? 0.51501 0.52606 0.53085 0.04327  0.00805  -0.05465 184 GLN B CG  
3575 C CD  . GLN B 184 ? 0.60487 0.63475 0.64943 0.05671  0.00080  -0.06776 184 GLN B CD  
3576 O OE1 . GLN B 184 ? 0.65230 0.71207 0.73836 0.05609  -0.00397 -0.08135 184 GLN B OE1 
3577 N NE2 . GLN B 184 ? 0.60237 0.61564 0.62753 0.06899  0.00014  -0.06554 184 GLN B NE2 
3578 N N   . GLY B 185 ? 0.44162 0.42182 0.42626 0.03573  -0.01506 -0.04955 185 GLY B N   
3579 C CA  . GLY B 185 ? 0.51725 0.50503 0.52223 0.03541  -0.03106 -0.06205 185 GLY B CA  
3580 C C   . GLY B 185 ? 0.53294 0.51374 0.54242 0.01890  -0.02356 -0.06176 185 GLY B C   
3581 O O   . GLY B 185 ? 0.55969 0.53031 0.55649 0.00967  -0.00594 -0.05098 185 GLY B O   
3582 N N   . ASP B 186 ? 0.45699 0.44124 0.48389 0.01591  -0.03863 -0.07501 186 ASP B N   
3583 C CA  . ASP B 186 ? 0.53684 0.50159 0.55797 0.00277  -0.03601 -0.07571 186 ASP B CA  
3584 C C   . ASP B 186 ? 0.55738 0.49021 0.52988 0.01300  -0.03687 -0.06453 186 ASP B C   
3585 O O   . ASP B 186 ? 0.65248 0.57657 0.60145 0.02799  -0.05194 -0.06713 186 ASP B O   
3586 C CB  . ASP B 186 ? 0.57734 0.55086 0.62524 -0.00167 -0.05576 -0.09562 186 ASP B CB  
3587 C CG  . ASP B 186 ? 0.61950 0.61031 0.71415 -0.02697 -0.04439 -0.10580 186 ASP B CG  
3588 O OD1 . ASP B 186 ? 0.71866 0.70423 0.82868 -0.03831 -0.05509 -0.12005 186 ASP B OD1 
3589 O OD2 . ASP B 186 ? 0.69593 0.70247 0.80919 -0.03736 -0.02295 -0.09994 186 ASP B OD2 
3590 N N   . ALA B 187 ? 0.54584 0.46141 0.50200 0.00609  -0.02052 -0.05286 187 ALA B N   
3591 C CA  . ALA B 187 ? 0.58683 0.47532 0.50557 0.01530  -0.02204 -0.04683 187 ALA B CA  
3592 C C   . ALA B 187 ? 0.64376 0.51676 0.55648 0.01847  -0.03932 -0.05985 187 ALA B C   
3593 O O   . ALA B 187 ? 0.59586 0.45943 0.48024 0.03359  -0.04829 -0.06112 187 ALA B O   
3594 C CB  . ALA B 187 ? 0.57372 0.44281 0.48055 0.00795  -0.00669 -0.03625 187 ALA B CB  
3595 N N   . PHE B 188 ? 0.62536 0.49626 0.56482 0.00287  -0.04328 -0.07125 188 PHE B N   
3596 C CA  . PHE B 188 ? 0.56898 0.42327 0.50416 0.00352  -0.06133 -0.08696 188 PHE B CA  
3597 C C   . PHE B 188 ? 0.62853 0.49619 0.55617 0.02022  -0.08297 -0.09732 188 PHE B C   
3598 O O   . PHE B 188 ? 0.73630 0.58381 0.63614 0.03075  -0.09703 -0.10569 188 PHE B O   
3599 C CB  . PHE B 188 ? 0.60649 0.46358 0.58167 -0.02097 -0.06093 -0.09989 188 PHE B CB  
3600 C CG  . PHE B 188 ? 0.64519 0.48005 0.61763 -0.02504 -0.07874 -0.11823 188 PHE B CG  
3601 C CD1 . PHE B 188 ? 0.60627 0.46174 0.59542 -0.01963 -0.10412 -0.13869 188 PHE B CD1 
3602 C CD2 . PHE B 188 ? 0.67385 0.46410 0.62528 -0.03343 -0.07180 -0.11640 188 PHE B CD2 
3603 C CE1 . PHE B 188 ? 0.63546 0.47025 0.62145 -0.02413 -0.12246 -0.15857 188 PHE B CE1 
3604 C CE2 . PHE B 188 ? 0.73745 0.50299 0.68560 -0.03835 -0.08838 -0.13554 188 PHE B CE2 
3605 C CZ  . PHE B 188 ? 0.60890 0.39853 0.57530 -0.03461 -0.11380 -0.15746 188 PHE B CZ  
3606 N N   . GLU B 189 ? 0.59432 0.49119 0.54074 0.02496  -0.08632 -0.09707 189 GLU B N   
3607 C CA  . GLU B 189 ? 0.60004 0.50206 0.53247 0.04312  -0.10899 -0.10590 189 GLU B CA  
3608 C C   . GLU B 189 ? 0.62321 0.51031 0.50820 0.06086  -0.10328 -0.09066 189 GLU B C   
3609 O O   . GLU B 189 ? 0.66057 0.53091 0.50849 0.07609  -0.11680 -0.09424 189 GLU B O   
3610 C CB  . GLU B 189 ? 0.61643 0.55446 0.59263 0.04296  -0.11971 -0.11633 189 GLU B CB  
3611 C CG  . GLU B 189 ? 0.61704 0.57546 0.64115 0.02823  -0.13374 -0.13937 189 GLU B CG  
3612 C CD  . GLU B 189 ? 0.74215 0.68819 0.74693 0.03966  -0.16368 -0.15706 189 GLU B CD  
3613 O OE1 . GLU B 189 ? 0.80825 0.75049 0.78213 0.06375  -0.18205 -0.15720 189 GLU B OE1 
3614 O OE2 . GLU B 189 ? 0.64766 0.58275 0.66290 0.02489  -0.16882 -0.17072 189 GLU B OE2 
3615 N N   . VAL B 190 ? 0.67591 0.56784 0.55970 0.05776  -0.08242 -0.07461 190 VAL B N   
3616 C CA  . VAL B 190 ? 0.61052 0.49149 0.45603 0.06972  -0.07454 -0.06170 190 VAL B CA  
3617 C C   . VAL B 190 ? 0.60906 0.46815 0.41638 0.07628  -0.07088 -0.06003 190 VAL B C   
3618 O O   . VAL B 190 ? 0.68650 0.53203 0.45589 0.08846  -0.07287 -0.05749 190 VAL B O   
3619 C CB  . VAL B 190 ? 0.60203 0.49515 0.45929 0.06235  -0.05419 -0.04864 190 VAL B CB  
3620 C CG1 . VAL B 190 ? 0.62230 0.50480 0.44446 0.06916  -0.04314 -0.03724 190 VAL B CG1 
3621 C CG2 . VAL B 190 ? 0.53935 0.45215 0.42722 0.06112  -0.05784 -0.05176 190 VAL B CG2 
3622 N N   . VAL B 191 ? 0.65352 0.50593 0.46717 0.06944  -0.06465 -0.06181 191 VAL B N   
3623 C CA  . VAL B 191 ? 0.63481 0.46845 0.41483 0.07908  -0.06114 -0.06269 191 VAL B CA  
3624 C C   . VAL B 191 ? 0.59222 0.40856 0.34541 0.08988  -0.07922 -0.07600 191 VAL B C   
3625 O O   . VAL B 191 ? 0.66730 0.46982 0.38363 0.10180  -0.07510 -0.07671 191 VAL B O   
3626 C CB  . VAL B 191 ? 0.62371 0.44660 0.41191 0.07363  -0.05342 -0.06240 191 VAL B CB  
3627 C CG1 . VAL B 191 ? 0.67582 0.51297 0.48728 0.06314  -0.03908 -0.05038 191 VAL B CG1 
3628 C CG2 . VAL B 191 ? 0.59301 0.39905 0.39395 0.06552  -0.06724 -0.07624 191 VAL B CG2 
3629 N N   . LYS B 192 ? 0.63661 0.45602 0.40736 0.08689  -0.09949 -0.08841 192 LYS B N   
3630 C CA  . LYS B 192 ? 0.71669 0.52001 0.45696 0.09967  -0.12061 -0.10245 192 LYS B CA  
3631 C C   . LYS B 192 ? 0.71137 0.50788 0.40930 0.11559  -0.12157 -0.09440 192 LYS B C   
3632 O O   . LYS B 192 ? 0.78998 0.56533 0.44306 0.12957  -0.13185 -0.10147 192 LYS B O   
3633 C CB  . LYS B 192 ? 0.67928 0.49374 0.45406 0.09297  -0.14526 -0.12079 192 LYS B CB  
3634 C CG  . LYS B 192 ? 0.61586 0.42302 0.41826 0.07647  -0.14682 -0.13332 192 LYS B CG  
3635 C CD  . LYS B 192 ? 0.67217 0.49612 0.51372 0.06716  -0.17129 -0.15524 192 LYS B CD  
3636 C CE  . LYS B 192 ? 0.70938 0.53906 0.60015 0.04000  -0.16057 -0.15960 192 LYS B CE  
3637 N NZ  . LYS B 192 ? 0.64457 0.43579 0.51706 0.03322  -0.15908 -0.16726 192 LYS B NZ  
3638 N N   . LYS B 193 ? 0.70675 0.51549 0.41283 0.11359  -0.11038 -0.07993 193 LYS B N   
3639 C CA  . LYS B 193 ? 0.75871 0.55198 0.42055 0.12651  -0.10943 -0.07041 193 LYS B CA  
3640 C C   . LYS B 193 ? 0.76004 0.54409 0.38938 0.12602  -0.08194 -0.05693 193 LYS B C   
3641 O O   . LYS B 193 ? 0.91579 0.67845 0.49679 0.13515  -0.07737 -0.04989 193 LYS B O   
3642 C CB  . LYS B 193 ? 0.72019 0.52539 0.40462 0.12593  -0.11353 -0.06391 193 LYS B CB  
3643 C CG  . LYS B 193 ? 0.82961 0.64217 0.53100 0.13559  -0.14543 -0.07939 193 LYS B CG  
3644 C CD  . LYS B 193 ? 0.89382 0.71749 0.61543 0.14087  -0.15103 -0.07497 193 LYS B CD  
3645 C CE  . LYS B 193 ? 1.01260 0.80359 0.67993 0.15212  -0.14167 -0.05731 193 LYS B CE  
3646 N NZ  . LYS B 193 ? 0.89247 0.69252 0.58368 0.14369  -0.12383 -0.04579 193 LYS B NZ  
3647 N N   . PHE B 194 ? 0.69158 0.49076 0.34468 0.11611  -0.06368 -0.05402 194 PHE B N   
3648 C CA  . PHE B 194 ? 0.66675 0.46760 0.29942 0.11555  -0.03849 -0.04505 194 PHE B CA  
3649 C C   . PHE B 194 ? 0.75947 0.54118 0.34510 0.12819  -0.03632 -0.05189 194 PHE B C   
3650 O O   . PHE B 194 ? 0.75472 0.52292 0.32934 0.13653  -0.05392 -0.06547 194 PHE B O   
3651 C CB  . PHE B 194 ? 0.68892 0.51207 0.35717 0.10727  -0.02485 -0.04372 194 PHE B CB  
3652 C CG  . PHE B 194 ? 0.56974 0.41167 0.27503 0.09495  -0.02018 -0.03551 194 PHE B CG  
3653 C CD1 . PHE B 194 ? 0.64226 0.48577 0.34321 0.09019  -0.01288 -0.02598 194 PHE B CD1 
3654 C CD2 . PHE B 194 ? 0.59228 0.44533 0.33140 0.08829  -0.02146 -0.03713 194 PHE B CD2 
3655 C CE1 . PHE B 194 ? 0.58968 0.44913 0.32224 0.07998  -0.00850 -0.02062 194 PHE B CE1 
3656 C CE2 . PHE B 194 ? 0.59160 0.46066 0.35900 0.07786  -0.01575 -0.03017 194 PHE B CE2 
3657 C CZ  . PHE B 194 ? 0.63739 0.51157 0.40278 0.07421  -0.00979 -0.02307 194 PHE B CZ  
3658 N N   . LYS B 195 ? 0.69740 0.47874 0.25587 0.12824  -0.01282 -0.04401 195 LYS B N   
3659 C CA  . LYS B 195 ? 0.73966 0.51160 0.26918 0.13642  -0.00620 -0.04881 195 LYS B CA  
3660 C C   . LYS B 195 ? 0.78266 0.56946 0.32920 0.14113  0.00017  -0.05980 195 LYS B C   
3661 O O   . LYS B 195 ? 0.62756 0.43297 0.20411 0.13761  0.00560  -0.06029 195 LYS B O   
3662 C CB  . LYS B 195 ? 0.75467 0.52652 0.26307 0.12964  0.01921  -0.03658 195 LYS B CB  
3663 C CG  . LYS B 195 ? 0.80772 0.54727 0.27251 0.13562  0.01155  -0.03141 195 LYS B CG  
3664 C CD  . LYS B 195 ? 0.79216 0.51640 0.24974 0.12951  0.01034  -0.01763 195 LYS B CD  
3665 C CE  . LYS B 195 ? 0.80047 0.48716 0.21435 0.14096  -0.00494 -0.01355 195 LYS B CE  
3666 N NZ  . LYS B 195 ? 0.79254 0.46709 0.21249 0.14254  -0.02075 -0.00718 195 LYS B NZ  
3667 N N   . GLN B 196 ? 0.70450 0.48010 0.22975 0.15110  -0.00207 -0.06886 196 GLN B N   
3668 C CA  . GLN B 196 ? 0.74680 0.53311 0.28154 0.15916  0.00651  -0.07932 196 GLN B CA  
3669 C C   . GLN B 196 ? 0.71999 0.53958 0.27170 0.15448  0.03545  -0.07385 196 GLN B C   
3670 O O   . GLN B 196 ? 0.76866 0.59614 0.30924 0.14511  0.05354  -0.06457 196 GLN B O   
3671 C CB  . GLN B 196 ? 0.79102 0.55841 0.29351 0.17038  0.00166  -0.08920 196 GLN B CB  
3672 C CG  . GLN B 196 ? 0.82789 0.60696 0.33521 0.18065  0.01468  -0.09963 196 GLN B CG  
3673 C CD  . GLN B 196 ? 0.90215 0.65665 0.38075 0.19290  0.00290  -0.11292 196 GLN B CD  
3674 O OE1 . GLN B 196 ? 0.91928 0.65961 0.36340 0.19419  0.00218  -0.11143 196 GLN B OE1 
3675 N NE2 . GLN B 196 ? 0.86762 0.61331 0.35721 0.20265  -0.00665 -0.12601 196 GLN B NE2 
3676 N N   . ALA B 197 ? 0.76514 0.60343 0.34436 0.16097  0.03899  -0.08068 197 ALA B N   
3677 C CA  . ALA B 197 ? 0.68781 0.56563 0.29116 0.15997  0.06275  -0.08069 197 ALA B CA  
3678 C C   . ALA B 197 ? 0.63516 0.53245 0.25060 0.14178  0.07733  -0.06785 197 ALA B C   
3679 O O   . ALA B 197 ? 0.61857 0.53368 0.23105 0.13170  0.09989  -0.06485 197 ALA B O   
3680 C CB  . ALA B 197 ? 0.79295 0.68082 0.38181 0.16662  0.07964  -0.08910 197 ALA B CB  
3681 N N   . SER B 198 ? 0.61382 0.50508 0.24168 0.13591  0.06521  -0.06102 198 SER B N   
3682 C CA  . SER B 198 ? 0.63708 0.54340 0.27947 0.11805  0.07647  -0.04921 198 SER B CA  
3683 C C   . SER B 198 ? 0.58039 0.52079 0.27187 0.11254  0.07640  -0.04841 198 SER B C   
3684 O O   . SER B 198 ? 0.56185 0.51808 0.27052 0.09664  0.08536  -0.04110 198 SER B O   
3685 C CB  . SER B 198 ? 0.58536 0.46020 0.21179 0.11035  0.06084  -0.03930 198 SER B CB  
3686 O OG  . SER B 198 ? 0.69693 0.55900 0.33752 0.11543  0.03628  -0.04308 198 SER B OG  
3687 N N   . PHE B 199 ? 0.52150 0.46876 0.23117 0.12610  0.06560  -0.05593 199 PHE B N   
3688 C CA  . PHE B 199 ? 0.56108 0.53572 0.30857 0.12532  0.06250  -0.05512 199 PHE B CA  
3689 C C   . PHE B 199 ? 0.55401 0.55345 0.31414 0.14516  0.06593  -0.06764 199 PHE B C   
3690 O O   . PHE B 199 ? 0.69771 0.67583 0.43978 0.16284  0.05897  -0.07565 199 PHE B O   
3691 C CB  . PHE B 199 ? 0.48133 0.43140 0.23542 0.12340  0.04264  -0.04885 199 PHE B CB  
3692 C CG  . PHE B 199 ? 0.58084 0.51510 0.33184 0.10666  0.03824  -0.03911 199 PHE B CG  
3693 C CD1 . PHE B 199 ? 0.52183 0.47371 0.29208 0.09263  0.04352  -0.03197 199 PHE B CD1 
3694 C CD2 . PHE B 199 ? 0.54707 0.44999 0.27640 0.10690  0.02725  -0.03949 199 PHE B CD2 
3695 C CE1 . PHE B 199 ? 0.50405 0.44061 0.27145 0.08085  0.03927  -0.02464 199 PHE B CE1 
3696 C CE2 . PHE B 199 ? 0.55828 0.45065 0.28778 0.09579  0.02124  -0.03271 199 PHE B CE2 
3697 C CZ  . PHE B 199 ? 0.61091 0.51926 0.35925 0.08359  0.02802  -0.02491 199 PHE B CZ  
3698 N N   . ASP B 200 ? 0.54578 0.59102 0.33776 0.14333  0.07565  -0.07152 200 ASP B N   
3699 C CA  . ASP B 200 ? 0.53729 0.61150 0.34891 0.16611  0.07348  -0.08446 200 ASP B CA  
3700 C C   . ASP B 200 ? 0.53149 0.58358 0.34512 0.17951  0.05077  -0.08054 200 ASP B C   
3701 O O   . ASP B 200 ? 0.53061 0.58242 0.34436 0.20493  0.04293  -0.08967 200 ASP B O   
3702 C CB  . ASP B 200 ? 0.50692 0.64330 0.35842 0.16003  0.08735  -0.09258 200 ASP B CB  
3703 C CG  . ASP B 200 ? 0.52486 0.68049 0.37506 0.13930  0.11436  -0.09379 200 ASP B CG  
3704 O OD1 . ASP B 200 ? 0.61098 0.75783 0.45911 0.11432  0.11977  -0.08282 200 ASP B OD1 
3705 O OD2 . ASP B 200 ? 0.57458 0.75279 0.42447 0.14812  0.13182  -0.10602 200 ASP B OD2 
3706 N N   . VAL B 201 ? 0.52354 0.55519 0.33630 0.16378  0.04154  -0.06726 201 VAL B N   
3707 C CA  . VAL B 201 ? 0.53087 0.54287 0.34335 0.17181  0.02472  -0.06108 201 VAL B CA  
3708 C C   . VAL B 201 ? 0.52171 0.49447 0.32065 0.15340  0.01890  -0.04806 201 VAL B C   
3709 O O   . VAL B 201 ? 0.53563 0.51551 0.34017 0.13336  0.02539  -0.04250 201 VAL B O   
3710 C CB  . VAL B 201 ? 0.42559 0.47870 0.26472 0.17265  0.02247  -0.06224 201 VAL B CB  
3711 C CG1 . VAL B 201 ? 0.45805 0.48125 0.28493 0.17786  0.00681  -0.05219 201 VAL B CG1 
3712 C CG2 . VAL B 201 ? 0.52054 0.61817 0.38057 0.19428  0.02444  -0.07815 201 VAL B CG2 
3713 N N   . ILE B 202 ? 0.50647 0.43773 0.28896 0.16007  0.00736  -0.04394 202 ILE B N   
3714 C CA  . ILE B 202 ? 0.45445 0.35564 0.23191 0.14211  0.00323  -0.03330 202 ILE B CA  
3715 C C   . ILE B 202 ? 0.50662 0.39074 0.27799 0.14783  -0.00352 -0.02537 202 ILE B C   
3716 O O   . ILE B 202 ? 0.57916 0.44510 0.33641 0.16863  -0.01060 -0.02780 202 ILE B O   
3717 C CB  . ILE B 202 ? 0.56659 0.42837 0.32814 0.13850  -0.00197 -0.03633 202 ILE B CB  
3718 C CG1 . ILE B 202 ? 0.50699 0.38061 0.26522 0.13423  0.00282  -0.04295 202 ILE B CG1 
3719 C CG2 . ILE B 202 ? 0.60497 0.44446 0.37054 0.11891  -0.00487 -0.02798 202 ILE B CG2 
3720 C CD1 . ILE B 202 ? 0.53210 0.37064 0.27200 0.13584  -0.00584 -0.05053 202 ILE B CD1 
3721 N N   . ILE B 203 ? 0.54525 0.43193 0.32270 0.13155  -0.00118 -0.01602 203 ILE B N   
3722 C CA  . ILE B 203 ? 0.50951 0.37304 0.27229 0.13414  -0.00516 -0.00626 203 ILE B CA  
3723 C C   . ILE B 203 ? 0.53140 0.36259 0.29009 0.11296  -0.00075 0.00134  203 ILE B C   
3724 O O   . ILE B 203 ? 0.48113 0.33004 0.25652 0.09495  0.00553  0.00283  203 ILE B O   
3725 C CB  . ILE B 203 ? 0.46504 0.36256 0.23656 0.13430  -0.00488 -0.00415 203 ILE B CB  
3726 C CG1 . ILE B 203 ? 0.49414 0.42923 0.27643 0.15540  -0.01056 -0.01480 203 ILE B CG1 
3727 C CG2 . ILE B 203 ? 0.51788 0.38421 0.26467 0.13530  -0.00761 0.00755  203 ILE B CG2 
3728 C CD1 . ILE B 203 ? 0.43278 0.41058 0.23179 0.15214  -0.01145 -0.01793 203 ILE B CD1 
3729 N N   . HIS B 204 ? 0.61687 0.40120 0.35563 0.11479  -0.00348 0.00451  204 HIS B N   
3730 C CA  . HIS B 204 ? 0.64479 0.40133 0.38667 0.09221  0.00172  0.00741  204 HIS B CA  
3731 C C   . HIS B 204 ? 0.66664 0.38841 0.38589 0.08669  0.00777  0.02081  204 HIS B C   
3732 O O   . HIS B 204 ? 0.71371 0.39035 0.40230 0.09846  0.00415  0.02591  204 HIS B O   
3733 C CB  . HIS B 204 ? 0.63447 0.36058 0.37139 0.09306  -0.00433 -0.00172 204 HIS B CB  
3734 C CG  . HIS B 204 ? 0.63685 0.34351 0.38639 0.06764  -0.00070 -0.00340 204 HIS B CG  
3735 N ND1 . HIS B 204 ? 0.62639 0.36428 0.40465 0.04872  0.00475  -0.00431 204 HIS B ND1 
3736 C CD2 . HIS B 204 ? 0.66804 0.32928 0.40891 0.05760  -0.00187 -0.00643 204 HIS B CD2 
3737 C CE1 . HIS B 204 ? 0.66196 0.38176 0.45355 0.02873  0.00637  -0.00908 204 HIS B CE1 
3738 N NE2 . HIS B 204 ? 0.65387 0.32656 0.42356 0.03139  0.00302  -0.01046 204 HIS B NE2 
3739 N N   . ASP B 205 ? 0.70995 0.44871 0.43973 0.07003  0.01780  0.02664  205 ASP B N   
3740 C CA  . ASP B 205 ? 0.68266 0.39203 0.38599 0.06413  0.02718  0.04019  205 ASP B CA  
3741 C C   . ASP B 205 ? 0.73128 0.43798 0.45364 0.03450  0.04274  0.04125  205 ASP B C   
3742 O O   . ASP B 205 ? 0.75929 0.49058 0.49151 0.02448  0.05281  0.04367  205 ASP B O   
3743 C CB  . ASP B 205 ? 0.66512 0.40310 0.35960 0.07613  0.02523  0.04403  205 ASP B CB  
3744 C CG  . ASP B 205 ? 0.80697 0.50573 0.45735 0.08055  0.02981  0.05845  205 ASP B CG  
3745 O OD1 . ASP B 205 ? 0.84425 0.49106 0.47123 0.07058  0.03851  0.06735  205 ASP B OD1 
3746 O OD2 . ASP B 205 ? 0.83199 0.54905 0.46832 0.09355  0.02452  0.06046  205 ASP B OD2 
3747 N N   . PRO B 206 ? 0.79354 0.47274 0.52386 0.01998  0.04505  0.03713  206 PRO B N   
3748 C CA  . PRO B 206 ? 0.80790 0.49648 0.56916 -0.00913 0.05873  0.03302  206 PRO B CA  
3749 C C   . PRO B 206 ? 0.89072 0.54542 0.62786 -0.02538 0.07949  0.04671  206 PRO B C   
3750 O O   . PRO B 206 ? 0.92609 0.53984 0.61476 -0.01251 0.08065  0.06078  206 PRO B O   
3751 C CB  . PRO B 206 ? 0.70955 0.37795 0.48499 -0.01740 0.05071  0.02138  206 PRO B CB  
3752 C CG  . PRO B 206 ? 0.79142 0.40598 0.52176 0.00053  0.04381  0.02860  206 PRO B CG  
3753 C CD  . PRO B 206 ? 0.78594 0.42230 0.49739 0.02944  0.03526  0.03418  206 PRO B CD  
3754 N N   . PRO B 207 ? 0.91863 0.58938 0.68707 -0.05283 0.09681  0.04254  207 PRO B N   
3755 C CA  . PRO B 207 ? 0.97071 0.60112 0.71641 -0.07498 0.12182  0.05443  207 PRO B CA  
3756 C C   . PRO B 207 ? 1.00627 0.57023 0.72552 -0.08375 0.12295  0.05897  207 PRO B C   
3757 O O   . PRO B 207 ? 1.04393 0.59600 0.76351 -0.07003 0.10269  0.05120  207 PRO B O   
3758 C CB  . PRO B 207 ? 0.97028 0.64639 0.77194 -0.10228 0.13804  0.04199  207 PRO B CB  
3759 C CG  . PRO B 207 ? 0.84836 0.57712 0.69899 -0.09293 0.11594  0.02304  207 PRO B CG  
3760 C CD  . PRO B 207 ? 0.74669 0.47708 0.56996 -0.06151 0.09549  0.02737  207 PRO B CD  
3761 N N   . ARG B 208 ? 1.13533 0.65157 0.82841 -0.10688 0.14779  0.07112  208 ARG B N   
3762 C CA  . ARG B 208 ? 1.15299 0.59372 0.81313 -0.11605 0.15014  0.07706  208 ARG B CA  
3763 C C   . ARG B 208 ? 1.15752 0.61166 0.87317 -0.14182 0.14706  0.05576  208 ARG B C   
3764 O O   . ARG B 208 ? 1.11667 0.63839 0.89467 -0.15289 0.14467  0.03792  208 ARG B O   
3765 C CB  . ARG B 208 ? 1.24852 0.62553 0.85638 -0.13504 0.18020  0.09840  208 ARG B CB  
3766 C CG  . ARG B 208 ? 1.40631 0.70937 0.94987 -0.11352 0.16875  0.11182  208 ARG B CG  
3767 C CD  . ARG B 208 ? 1.42716 0.68646 0.94247 -0.13445 0.19142  0.12285  208 ARG B CD  
3768 N NE  . ARG B 208 ? 1.49346 0.69618 0.93768 -0.10423 0.18068  0.13900  208 ARG B NE  
3769 C CZ  . ARG B 208 ? 1.66949 0.82472 1.07016 -0.11273 0.19728  0.15255  208 ARG B CZ  
3770 N NH1 . ARG B 208 ? 1.70077 0.85863 1.12134 -0.15139 0.22749  0.15277  208 ARG B NH1 
3771 N NH2 . ARG B 208 ? 1.65499 0.75984 0.99133 -0.08098 0.18315  0.16503  208 ARG B NH2 
3772 N N   . PHE B 209 ? 1.16501 0.55137 0.85554 -0.14944 0.14473  0.05636  209 PHE B N   
3773 C CA  . PHE B 209 ? 1.14825 0.54371 0.88568 -0.16759 0.13364  0.03283  209 PHE B CA  
3774 C C   . PHE B 209 ? 1.16632 0.60274 0.96630 -0.21053 0.15456  0.01908  209 PHE B C   
3775 O O   . PHE B 209 ? 1.12881 0.62964 0.99135 -0.21546 0.14059  -0.00420 209 PHE B O   
3776 C CB  . PHE B 209 ? 1.18331 0.48872 0.87582 -0.16844 0.12883  0.03590  209 PHE B CB  
3777 C CG  . PHE B 209 ? 1.31406 0.62433 1.04574 -0.17908 0.11006  0.00894  209 PHE B CG  
3778 C CD1 . PHE B 209 ? 1.30748 0.66538 1.10796 -0.21454 0.11498  -0.01306 209 PHE B CD1 
3779 C CD2 . PHE B 209 ? 1.27794 0.55024 0.97844 -0.15031 0.08539  0.00312  209 PHE B CD2 
3780 C CE1 . PHE B 209 ? 1.20417 0.56756 1.03737 -0.22202 0.09387  -0.03976 209 PHE B CE1 
3781 C CE2 . PHE B 209 ? 1.23637 0.51149 0.96646 -0.15789 0.06701  -0.02294 209 PHE B CE2 
3782 C CZ  . PHE B 209 ? 1.23379 0.55360 1.02876 -0.19391 0.07001  -0.04433 209 PHE B CZ  
3783 N N   . SER B 210 ? 1.28303 0.68497 1.06720 -0.24060 0.18781  0.03226  210 SER B N   
3784 C CA  . SER B 210 ? 1.28060 0.73612 1.13303 -0.27874 0.20771  0.01664  210 SER B CA  
3785 C C   . SER B 210 ? 1.18465 0.72729 1.09007 -0.27503 0.20869  0.00523  210 SER B C   
3786 O O   . SER B 210 ? 1.17869 0.78460 1.15852 -0.29223 0.20423  -0.02003 210 SER B O   
3787 C CB  . SER B 210 ? 1.23711 0.66544 1.06333 -0.29727 0.23808  0.03382  210 SER B CB  
3788 O OG  . SER B 210 ? 1.15972 0.59952 0.95276 -0.28325 0.25410  0.05184  210 SER B OG  
3789 N N   . LEU B 211 ? 1.10803 0.66321 0.97823 -0.24608 0.20847  0.02169  211 LEU B N   
3790 C CA  . LEU B 211 ? 1.05220 0.69015 0.96800 -0.23703 0.20771  0.01193  211 LEU B CA  
3791 C C   . LEU B 211 ? 1.07687 0.77300 1.04615 -0.22104 0.17421  -0.01173 211 LEU B C   
3792 O O   . LEU B 211 ? 1.06832 0.83358 1.09515 -0.22416 0.17365  -0.02796 211 LEU B O   
3793 C CB  . LEU B 211 ? 1.06610 0.69837 0.92818 -0.20715 0.20862  0.03223  211 LEU B CB  
3794 C CG  . LEU B 211 ? 1.13189 0.74348 0.95953 -0.22274 0.24557  0.04958  211 LEU B CG  
3795 C CD1 . LEU B 211 ? 1.17874 0.73841 0.92213 -0.19398 0.24146  0.07456  211 LEU B CD1 
3796 C CD2 . LEU B 211 ? 0.92123 0.60879 0.80011 -0.22872 0.25985  0.03707  211 LEU B CD2 
3797 N N   . ALA B 212 ? 1.05075 0.71736 0.99865 -0.20241 0.14653  -0.01435 212 ALA B N   
3798 C CA  . ALA B 212 ? 0.91560 0.62415 0.90171 -0.18774 0.11494  -0.03582 212 ALA B CA  
3799 C C   . ALA B 212 ? 1.02088 0.67820 0.96919 -0.17168 0.09270  -0.03617 212 ALA B C   
3800 O O   . ALA B 212 ? 1.00143 0.64066 0.90511 -0.14080 0.08143  -0.02374 212 ALA B O   
3801 C CB  . ALA B 212 ? 1.00541 0.76755 0.99926 -0.15881 0.10223  -0.03543 212 ALA B CB  
3802 N N   . GLY B 213 ? 0.97663 0.61368 0.94543 -0.19209 0.08591  -0.05303 213 GLY B N   
3803 C CA  . GLY B 213 ? 0.91779 0.49602 0.84677 -0.17973 0.06870  -0.05457 213 GLY B CA  
3804 C C   . GLY B 213 ? 0.89969 0.50270 0.83310 -0.15196 0.03599  -0.07054 213 GLY B C   
3805 O O   . GLY B 213 ? 0.92516 0.48320 0.81761 -0.13283 0.02259  -0.06984 213 GLY B O   
3806 N N   . HIS B 214 ? 0.79926 0.47062 0.77850 -0.14796 0.02348  -0.08519 214 HIS B N   
3807 C CA  . HIS B 214 ? 0.74001 0.43215 0.71611 -0.12135 -0.00594 -0.09860 214 HIS B CA  
3808 C C   . HIS B 214 ? 0.83224 0.50925 0.75689 -0.08658 -0.00995 -0.08168 214 HIS B C   
3809 O O   . HIS B 214 ? 0.90128 0.56537 0.80223 -0.06582 -0.02838 -0.08941 214 HIS B O   
3810 C CB  . HIS B 214 ? 0.73281 0.49563 0.75900 -0.11989 -0.01693 -0.11268 214 HIS B CB  
3811 C CG  . HIS B 214 ? 0.75052 0.54848 0.78128 -0.11149 -0.00195 -0.09666 214 HIS B CG  
3812 N ND1 . HIS B 214 ? 0.80278 0.61184 0.85499 -0.13343 0.02456  -0.08885 214 HIS B ND1 
3813 C CD2 . HIS B 214 ? 0.71071 0.53210 0.72509 -0.08478 -0.00851 -0.08799 214 HIS B CD2 
3814 C CE1 . HIS B 214 ? 0.78526 0.62328 0.83336 -0.11847 0.03155  -0.07722 214 HIS B CE1 
3815 N NE2 . HIS B 214 ? 0.77553 0.62061 0.80212 -0.09004 0.01152  -0.07650 214 HIS B NE2 
3816 N N   . LEU B 215 ? 0.80302 0.48358 0.71074 -0.08012 0.00736  -0.06062 215 LEU B N   
3817 C CA  . LEU B 215 ? 0.75498 0.42963 0.62224 -0.04958 0.00437  -0.04664 215 LEU B CA  
3818 C C   . LEU B 215 ? 0.84942 0.46302 0.66991 -0.03751 0.00364  -0.03955 215 LEU B C   
3819 O O   . LEU B 215 ? 0.87143 0.48056 0.66090 -0.01227 0.00257  -0.02850 215 LEU B O   
3820 C CB  . LEU B 215 ? 0.73137 0.42965 0.59706 -0.04776 0.02079  -0.02959 215 LEU B CB  
3821 C CG  . LEU B 215 ? 0.71064 0.46825 0.61283 -0.04896 0.02060  -0.03429 215 LEU B CG  
3822 C CD1 . LEU B 215 ? 0.63758 0.40820 0.52197 -0.03771 0.03171  -0.01823 215 LEU B CD1 
3823 C CD2 . LEU B 215 ? 0.69425 0.47767 0.60544 -0.03291 -0.00106 -0.04774 215 LEU B CD2 
3824 N N   . TYR B 216 ? 0.90354 0.47047 0.72013 -0.05454 0.00345  -0.04736 216 TYR B N   
3825 C CA  . TYR B 216 ? 0.92366 0.42275 0.69363 -0.04244 0.00144  -0.04251 216 TYR B CA  
3826 C C   . TYR B 216 ? 0.97531 0.45180 0.74466 -0.04060 -0.01697 -0.06462 216 TYR B C   
3827 O O   . TYR B 216 ? 0.92896 0.34321 0.66175 -0.03215 -0.02012 -0.06517 216 TYR B O   
3828 C CB  . TYR B 216 ? 0.98634 0.43096 0.73938 -0.06661 0.02204  -0.02859 216 TYR B CB  
3829 C CG  . TYR B 216 ? 0.98285 0.42756 0.71041 -0.05766 0.03764  -0.00435 216 TYR B CG  
3830 C CD1 . TYR B 216 ? 0.96191 0.45079 0.71848 -0.07610 0.05384  0.00152  216 TYR B CD1 
3831 C CD2 . TYR B 216 ? 0.96559 0.36447 0.63894 -0.02996 0.03534  0.01091  216 TYR B CD2 
3832 C CE1 . TYR B 216 ? 0.98602 0.47358 0.71527 -0.06773 0.06713  0.02174  216 TYR B CE1 
3833 C CE2 . TYR B 216 ? 1.01356 0.41297 0.66102 -0.02055 0.04626  0.03123  216 TYR B CE2 
3834 C CZ  . TYR B 216 ? 1.02672 0.46896 0.70032 -0.04049 0.06244  0.03663  216 TYR B CZ  
3835 O OH  . TYR B 216 ? 1.17721 0.61819 0.82071 -0.03075 0.07237  0.05504  216 TYR B OH  
3836 N N   . SER B 217 ? 0.95341 0.47583 0.75866 -0.04624 -0.03060 -0.08360 217 SER B N   
3837 C CA  . SER B 217 ? 1.09864 0.60175 0.91108 -0.05442 -0.04797 -0.10833 217 SER B CA  
3838 C C   . SER B 217 ? 1.04427 0.53384 0.82012 -0.02075 -0.06505 -0.11735 217 SER B C   
3839 O O   . SER B 217 ? 1.02233 0.52532 0.77408 0.00778  -0.06274 -0.10559 217 SER B O   
3840 C CB  . SER B 217 ? 0.90746 0.46714 0.77353 -0.07308 -0.05840 -0.12684 217 SER B CB  
3841 O OG  . SER B 217 ? 0.87644 0.49334 0.75108 -0.05349 -0.06332 -0.12194 217 SER B OG  
3842 N N   . GLU B 218 ? 1.17788 0.64192 0.95128 -0.02563 -0.08162 -0.14079 218 GLU B N   
3843 C CA  . GLU B 218 ? 1.17233 0.62663 0.91141 0.00503  -0.09754 -0.15361 218 GLU B CA  
3844 C C   . GLU B 218 ? 1.16019 0.67700 0.90749 0.02172  -0.10574 -0.15549 218 GLU B C   
3845 O O   . GLU B 218 ? 1.14039 0.66884 0.86035 0.05002  -0.10247 -0.14764 218 GLU B O   
3846 C CB  . GLU B 218 ? 1.30571 0.71850 1.04011 -0.00629 -0.11489 -0.18111 218 GLU B CB  
3847 C CG  . GLU B 218 ? 1.34679 0.72533 1.03622 0.02369  -0.12299 -0.19051 218 GLU B CG  
3848 C CD  . GLU B 218 ? 1.44906 0.79243 1.10469 0.04604  -0.10808 -0.17092 218 GLU B CD  
3849 O OE1 . GLU B 218 ? 1.38472 0.71326 1.03954 0.03971  -0.09335 -0.15037 218 GLU B OE1 
3850 O OE2 . GLU B 218 ? 1.50862 0.84139 1.13750 0.07188  -0.11199 -0.17663 218 GLU B OE2 
3851 N N   . GLU B 219 ? 0.90147 0.45860 0.68680 0.00439  -0.11579 -0.16613 219 GLU B N   
3852 C CA  . GLU B 219 ? 0.94528 0.55231 0.73225 0.02070  -0.12508 -0.16710 219 GLU B CA  
3853 C C   . GLU B 219 ? 0.83835 0.47310 0.61928 0.03425  -0.10691 -0.14214 219 GLU B C   
3854 O O   . GLU B 219 ? 0.82024 0.47070 0.57576 0.05710  -0.10775 -0.13873 219 GLU B O   
3855 C CB  . GLU B 219 ? 0.90250 0.54958 0.73634 0.00124  -0.13852 -0.18038 219 GLU B CB  
3856 C CG  . GLU B 219 ? 0.96261 0.61636 0.84356 -0.03147 -0.12468 -0.17641 219 GLU B CG  
3857 C CD  . GLU B 219 ? 0.89292 0.58546 0.82667 -0.05138 -0.14117 -0.19845 219 GLU B CD  
3858 O OE1 . GLU B 219 ? 0.83060 0.56258 0.76995 -0.03547 -0.15857 -0.20527 219 GLU B OE1 
3859 O OE2 . GLU B 219 ? 0.94303 0.62595 0.91227 -0.08262 -0.13664 -0.20942 219 GLU B OE2 
3860 N N   . PHE B 220 ? 0.84154 0.48128 0.64353 0.01930  -0.08926 -0.12525 220 PHE B N   
3861 C CA  . PHE B 220 ? 0.77758 0.44650 0.57632 0.03075  -0.07468 -0.10465 220 PHE B CA  
3862 C C   . PHE B 220 ? 0.78347 0.43489 0.54345 0.05654  -0.06875 -0.09701 220 PHE B C   
3863 O O   . PHE B 220 ? 0.78692 0.46799 0.53838 0.07224  -0.06419 -0.08992 220 PHE B O   
3864 C CB  . PHE B 220 ? 0.74352 0.41840 0.56606 0.01139  -0.05728 -0.08937 220 PHE B CB  
3865 C CG  . PHE B 220 ? 0.67496 0.38336 0.49732 0.02138  -0.04550 -0.07213 220 PHE B CG  
3866 C CD1 . PHE B 220 ? 0.69975 0.45185 0.54346 0.02112  -0.04851 -0.07299 220 PHE B CD1 
3867 C CD2 . PHE B 220 ? 0.70741 0.40186 0.50668 0.03278  -0.03367 -0.05669 220 PHE B CD2 
3868 C CE1 . PHE B 220 ? 0.60941 0.38818 0.45221 0.02841  -0.03770 -0.05881 220 PHE B CE1 
3869 C CE2 . PHE B 220 ? 0.73666 0.46395 0.53815 0.04025  -0.02476 -0.04410 220 PHE B CE2 
3870 C CZ  . PHE B 220 ? 0.60978 0.37807 0.43322 0.03648  -0.02585 -0.04534 220 PHE B CZ  
3871 N N   . TYR B 221 ? 0.81220 0.41566 0.54991 0.06121  -0.06813 -0.09924 221 TYR B N   
3872 C CA  . TYR B 221 ? 0.79158 0.38270 0.49649 0.08994  -0.06470 -0.09602 221 TYR B CA  
3873 C C   . TYR B 221 ? 0.87232 0.47596 0.55812 0.10906  -0.07348 -0.11089 221 TYR B C   
3874 O O   . TYR B 221 ? 0.90274 0.52734 0.57437 0.13043  -0.06610 -0.10711 221 TYR B O   
3875 C CB  . TYR B 221 ? 0.91679 0.44670 0.59795 0.09449  -0.06466 -0.09673 221 TYR B CB  
3876 C CG  . TYR B 221 ? 0.94798 0.45475 0.63408 0.07830  -0.05305 -0.07896 221 TYR B CG  
3877 C CD1 . TYR B 221 ? 0.91323 0.45966 0.62116 0.06763  -0.04200 -0.06320 221 TYR B CD1 
3878 C CD2 . TYR B 221 ? 0.95768 0.39716 0.62059 0.07417  -0.05222 -0.07788 221 TYR B CD2 
3879 C CE1 . TYR B 221 ? 0.89687 0.41989 0.60216 0.05358  -0.02976 -0.04706 221 TYR B CE1 
3880 C CE2 . TYR B 221 ? 1.00650 0.41803 0.66464 0.05920  -0.03937 -0.05978 221 TYR B CE2 
3881 C CZ  . TYR B 221 ? 0.92966 0.38479 0.60828 0.04922  -0.02781 -0.04446 221 TYR B CZ  
3882 O OH  . TYR B 221 ? 0.98342 0.40830 0.65041 0.03501  -0.01339 -0.02641 221 TYR B OH  
3883 N N   . ARG B 222 ? 0.82653 0.41924 0.51137 0.10115  -0.08864 -0.12889 222 ARG B N   
3884 C CA  . ARG B 222 ? 0.89419 0.49613 0.55302 0.11917  -0.09699 -0.14251 222 ARG B CA  
3885 C C   . ARG B 222 ? 0.85489 0.50492 0.51725 0.12419  -0.08930 -0.13131 222 ARG B C   
3886 O O   . ARG B 222 ? 0.83591 0.49680 0.47181 0.14351  -0.08233 -0.13217 222 ARG B O   
3887 C CB  . ARG B 222 ? 0.84158 0.42666 0.50014 0.10839  -0.11846 -0.16431 222 ARG B CB  
3888 C CG  . ARG B 222 ? 0.92262 0.45335 0.56151 0.11012  -0.12788 -0.18238 222 ARG B CG  
3889 C CD  . ARG B 222 ? 0.98340 0.51752 0.62533 0.10202  -0.14893 -0.20271 222 ARG B CD  
3890 N NE  . ARG B 222 ? 0.94927 0.48537 0.63087 0.07232  -0.16072 -0.21170 222 ARG B NE  
3891 C CZ  . ARG B 222 ? 1.06454 0.56817 0.76523 0.04960  -0.16338 -0.22095 222 ARG B CZ  
3892 N NH1 . ARG B 222 ? 1.05640 0.51727 0.73512 0.05525  -0.15796 -0.22280 222 ARG B NH1 
3893 N NH2 . ARG B 222 ? 1.07874 0.59524 0.82410 0.01974  -0.17036 -0.22883 222 ARG B NH2 
3894 N N   . GLU B 223 ? 0.72394 0.40124 0.41801 0.10640  -0.08879 -0.12153 223 GLU B N   
3895 C CA  . GLU B 223 ? 0.68871 0.40319 0.38365 0.11030  -0.08152 -0.11045 223 GLU B CA  
3896 C C   . GLU B 223 ? 0.73716 0.46887 0.43106 0.11886  -0.06138 -0.09527 223 GLU B C   
3897 O O   . GLU B 223 ? 0.76799 0.51941 0.44613 0.12936  -0.05195 -0.09145 223 GLU B O   
3898 C CB  . GLU B 223 ? 0.69007 0.42761 0.42039 0.09188  -0.08646 -0.10563 223 GLU B CB  
3899 C CG  . GLU B 223 ? 0.76983 0.50529 0.50864 0.08543  -0.10940 -0.12293 223 GLU B CG  
3900 C CD  . GLU B 223 ? 0.75069 0.47913 0.44824 0.10385  -0.12249 -0.13327 223 GLU B CD  
3901 O OE1 . GLU B 223 ? 0.74647 0.48611 0.41955 0.11570  -0.11287 -0.12222 223 GLU B OE1 
3902 O OE2 . GLU B 223 ? 0.80755 0.51674 0.49493 0.10513  -0.14215 -0.15307 223 GLU B OE2 
3903 N N   . LEU B 224 ? 0.68415 0.40837 0.39382 0.11374  -0.05457 -0.08697 224 LEU B N   
3904 C CA  . LEU B 224 ? 0.67816 0.41952 0.38699 0.12514  -0.04018 -0.07621 224 LEU B CA  
3905 C C   . LEU B 224 ? 0.70523 0.44484 0.38827 0.14860  -0.03639 -0.08551 224 LEU B C   
3906 O O   . LEU B 224 ? 0.71780 0.48982 0.40077 0.15710  -0.02403 -0.08197 224 LEU B O   
3907 C CB  . LEU B 224 ? 0.77733 0.49898 0.49499 0.12078  -0.03765 -0.06758 224 LEU B CB  
3908 C CG  . LEU B 224 ? 0.64680 0.37516 0.38948 0.09840  -0.03406 -0.05602 224 LEU B CG  
3909 C CD1 . LEU B 224 ? 0.64541 0.36086 0.38368 0.10199  -0.02667 -0.04342 224 LEU B CD1 
3910 C CD2 . LEU B 224 ? 0.65606 0.42607 0.41692 0.09037  -0.02966 -0.05071 224 LEU B CD2 
3911 N N   . PHE B 225 ? 0.77493 0.47784 0.43703 0.15805  -0.04585 -0.09952 225 PHE B N   
3912 C CA  . PHE B 225 ? 0.77144 0.47119 0.40702 0.18247  -0.04177 -0.11178 225 PHE B CA  
3913 C C   . PHE B 225 ? 0.76857 0.49370 0.38782 0.18547  -0.03506 -0.11548 225 PHE B C   
3914 O O   . PHE B 225 ? 0.79526 0.54331 0.40486 0.20065  -0.02028 -0.11818 225 PHE B O   
3915 C CB  . PHE B 225 ? 0.86610 0.51458 0.47895 0.19005  -0.05531 -0.12832 225 PHE B CB  
3916 C CG  . PHE B 225 ? 0.88117 0.53037 0.47463 0.21412  -0.05056 -0.13855 225 PHE B CG  
3917 C CD1 . PHE B 225 ? 0.90852 0.56294 0.50729 0.23300  -0.04363 -0.13584 225 PHE B CD1 
3918 C CD2 . PHE B 225 ? 0.94801 0.59878 0.52332 0.21655  -0.05362 -0.14865 225 PHE B CD2 
3919 C CE1 . PHE B 225 ? 0.88412 0.54796 0.47446 0.25291  -0.03909 -0.14463 225 PHE B CE1 
3920 C CE2 . PHE B 225 ? 0.94528 0.60177 0.50820 0.23566  -0.04689 -0.15636 225 PHE B CE2 
3921 C CZ  . PHE B 225 ? 0.94138 0.60593 0.51398 0.25351  -0.03920 -0.15508 225 PHE B CZ  
3922 N N   . ARG B 226 ? 0.76059 0.48109 0.37510 0.17187  -0.04539 -0.11631 226 ARG B N   
3923 C CA  . ARG B 226 ? 0.80815 0.53900 0.39388 0.17679  -0.04118 -0.11896 226 ARG B CA  
3924 C C   . ARG B 226 ? 0.73582 0.50437 0.33218 0.17159  -0.02140 -0.10348 226 ARG B C   
3925 O O   . ARG B 226 ? 0.72208 0.50821 0.30548 0.17690  -0.00518 -0.10153 226 ARG B O   
3926 C CB  . ARG B 226 ? 0.69849 0.41334 0.27613 0.16684  -0.06209 -0.12421 226 ARG B CB  
3927 C CG  . ARG B 226 ? 0.72194 0.44433 0.27343 0.17031  -0.06040 -0.12064 226 ARG B CG  
3928 C CD  . ARG B 226 ? 0.73059 0.44087 0.27802 0.16426  -0.08566 -0.12651 226 ARG B CD  
3929 N NE  . ARG B 226 ? 0.83815 0.55988 0.41421 0.15123  -0.09206 -0.12058 226 ARG B NE  
3930 C CZ  . ARG B 226 ? 0.70764 0.44679 0.28583 0.14738  -0.08428 -0.10551 226 ARG B CZ  
3931 N NH1 . ARG B 226 ? 0.76774 0.50714 0.31262 0.15469  -0.07090 -0.09642 226 ARG B NH1 
3932 N NH2 . ARG B 226 ? 0.68562 0.44282 0.30615 0.13336  -0.08723 -0.09748 226 ARG B NH2 
3933 N N   . ILE B 227 ? 0.73462 0.51976 0.36474 0.15591  -0.02112 -0.09001 227 ILE B N   
3934 C CA  . ILE B 227 ? 0.68752 0.50342 0.32790 0.14781  -0.00475 -0.07678 227 ILE B CA  
3935 C C   . ILE B 227 ? 0.63286 0.47878 0.29078 0.15367  0.01323  -0.07485 227 ILE B C   
3936 O O   . ILE B 227 ? 0.62063 0.49439 0.28838 0.14573  0.02877  -0.06707 227 ILE B O   
3937 C CB  . ILE B 227 ? 0.66699 0.48805 0.33511 0.13050  -0.01263 -0.06607 227 ILE B CB  
3938 C CG1 . ILE B 227 ? 0.59653 0.41822 0.29542 0.12567  -0.01615 -0.06349 227 ILE B CG1 
3939 C CG2 . ILE B 227 ? 0.64659 0.44675 0.30285 0.12730  -0.03206 -0.07123 227 ILE B CG2 
3940 C CD1 . ILE B 227 ? 0.58919 0.42258 0.31612 0.10931  -0.01734 -0.05306 227 ILE B CD1 
3941 N N   . LEU B 228 ? 0.65364 0.49386 0.31631 0.16785  0.01023  -0.08300 228 LEU B N   
3942 C CA  . LEU B 228 ? 0.62659 0.49869 0.30555 0.17984  0.02371  -0.08561 228 LEU B CA  
3943 C C   . LEU B 228 ? 0.68662 0.57453 0.34617 0.19185  0.04042  -0.09629 228 LEU B C   
3944 O O   . LEU B 228 ? 0.74285 0.60718 0.37770 0.19568  0.03578  -0.10234 228 LEU B O   
3945 C CB  . LEU B 228 ? 0.67659 0.52988 0.36169 0.19535  0.01222  -0.09054 228 LEU B CB  
3946 C CG  . LEU B 228 ? 0.57058 0.42789 0.28039 0.19074  0.00620  -0.07965 228 LEU B CG  
3947 C CD1 . LEU B 228 ? 0.65075 0.48704 0.35459 0.21389  -0.00181 -0.08594 228 LEU B CD1 
3948 C CD2 . LEU B 228 ? 0.59294 0.50015 0.32907 0.18423  0.01841  -0.07372 228 LEU B CD2 
3949 N N   . LYS B 229 ? 0.66045 0.59418 0.34391 0.19112  0.05879  -0.09613 229 LYS B N   
3950 C CA  . LYS B 229 ? 0.63054 0.58823 0.31382 0.19584  0.07637  -0.10449 229 LYS B CA  
3951 C C   . LYS B 229 ? 0.68148 0.63829 0.37101 0.22060  0.06948  -0.11792 229 LYS B C   
3952 O O   . LYS B 229 ? 0.74577 0.69290 0.44665 0.23353  0.05434  -0.11887 229 LYS B O   
3953 C CB  . LYS B 229 ? 0.60515 0.61503 0.31792 0.18367  0.09932  -0.10300 229 LYS B CB  
3954 C CG  . LYS B 229 ? 0.63918 0.64287 0.33709 0.15874  0.11079  -0.09026 229 LYS B CG  
3955 C CD  . LYS B 229 ? 0.61609 0.66638 0.34710 0.14329  0.13043  -0.08861 229 LYS B CD  
3956 C CE  . LYS B 229 ? 0.66401 0.69522 0.38034 0.12111  0.13308  -0.07314 229 LYS B CE  
3957 N NZ  . LYS B 229 ? 0.65586 0.72608 0.39758 0.10055  0.15710  -0.07202 229 LYS B NZ  
3958 N N   . PRO B 230 ? 0.72636 0.68734 0.40397 0.22823  0.08008  -0.12801 230 PRO B N   
3959 C CA  . PRO B 230 ? 0.74994 0.71736 0.43786 0.25314  0.07633  -0.14181 230 PRO B CA  
3960 C C   . PRO B 230 ? 0.72335 0.73805 0.45518 0.26271  0.07887  -0.14476 230 PRO B C   
3961 O O   . PRO B 230 ? 0.76142 0.82227 0.52046 0.24885  0.09541  -0.14271 230 PRO B O   
3962 C CB  . PRO B 230 ? 0.71588 0.69546 0.38924 0.25380  0.09635  -0.15167 230 PRO B CB  
3963 C CG  . PRO B 230 ? 0.72652 0.67643 0.36313 0.23489  0.09807  -0.14262 230 PRO B CG  
3964 C CD  . PRO B 230 ? 0.77167 0.72304 0.41870 0.21632  0.09359  -0.12714 230 PRO B CD  
3965 N N   . GLY B 231 ? 0.71584 0.71622 0.45315 0.28616  0.06070  -0.14968 231 GLY B N   
3966 C CA  . GLY B 231 ? 0.72749 0.76628 0.50157 0.29781  0.05560  -0.15103 231 GLY B CA  
3967 C C   . GLY B 231 ? 0.78005 0.81958 0.56265 0.28399  0.04887  -0.13789 231 GLY B C   
3968 O O   . GLY B 231 ? 0.84207 0.91999 0.65592 0.29073  0.04521  -0.13917 231 GLY B O   
3969 N N   . GLY B 232 ? 0.71508 0.71529 0.47130 0.26536  0.04619  -0.12667 232 GLY B N   
3970 C CA  . GLY B 232 ? 0.67011 0.66566 0.43091 0.25352  0.03992  -0.11501 232 GLY B CA  
3971 C C   . GLY B 232 ? 0.74612 0.70822 0.50350 0.26786  0.01850  -0.10965 232 GLY B C   
3972 O O   . GLY B 232 ? 0.82803 0.75068 0.56445 0.28876  0.00777  -0.11578 232 GLY B O   
3973 N N   . ARG B 233 ? 0.70689 0.68085 0.48159 0.25523  0.01275  -0.09721 233 ARG B N   
3974 C CA  . ARG B 233 ? 0.73185 0.67691 0.49948 0.26813  -0.00497 -0.08966 233 ARG B CA  
3975 C C   . ARG B 233 ? 0.59965 0.50455 0.35415 0.24214  -0.01010 -0.07186 233 ARG B C   
3976 O O   . ARG B 233 ? 0.55951 0.48466 0.32729 0.21666  -0.00232 -0.06475 233 ARG B O   
3977 C CB  . ARG B 233 ? 0.71185 0.70852 0.50869 0.28030  -0.00881 -0.09271 233 ARG B CB  
3978 C CG  . ARG B 233 ? 0.68674 0.73541 0.50772 0.30727  -0.00419 -0.11322 233 ARG B CG  
3979 C CD  . ARG B 233 ? 0.70279 0.81895 0.56012 0.28665  0.01624  -0.12059 233 ARG B CD  
3980 N NE  . ARG B 233 ? 0.55850 0.71532 0.44515 0.27348  0.01265  -0.11698 233 ARG B NE  
3981 C CZ  . ARG B 233 ? 0.59181 0.79769 0.50823 0.24816  0.02982  -0.12056 233 ARG B CZ  
3982 N NH1 . ARG B 233 ? 0.57769 0.79528 0.49452 0.23342  0.05291  -0.12504 233 ARG B NH1 
3983 N NH2 . ARG B 233 ? 0.46641 0.70529 0.40801 0.23677  0.02406  -0.11957 233 ARG B NH2 
3984 N N   . LEU B 234 ? 0.68979 0.53722 0.41860 0.24876  -0.02196 -0.06530 234 LEU B N   
3985 C CA  . LEU B 234 ? 0.70068 0.51099 0.41946 0.22377  -0.02410 -0.05009 234 LEU B CA  
3986 C C   . LEU B 234 ? 0.73941 0.51963 0.44131 0.23413  -0.03342 -0.03877 234 LEU B C   
3987 O O   . LEU B 234 ? 0.82392 0.57726 0.50619 0.26225  -0.04296 -0.04228 234 LEU B O   
3988 C CB  . LEU B 234 ? 0.74147 0.50198 0.44152 0.21316  -0.02616 -0.05279 234 LEU B CB  
3989 C CG  . LEU B 234 ? 0.77312 0.48800 0.46305 0.19162  -0.02874 -0.03989 234 LEU B CG  
3990 C CD1 . LEU B 234 ? 0.72919 0.47269 0.44172 0.16267  -0.02157 -0.03340 234 LEU B CD1 
3991 C CD2 . LEU B 234 ? 0.83456 0.49112 0.50334 0.18928  -0.03468 -0.04649 234 LEU B CD2 
3992 N N   . PHE B 235 ? 0.71251 0.49485 0.41791 0.21373  -0.03061 -0.02538 235 PHE B N   
3993 C CA  . PHE B 235 ? 0.67498 0.41641 0.35355 0.21790  -0.03649 -0.01144 235 PHE B CA  
3994 C C   . PHE B 235 ? 0.75529 0.45633 0.42495 0.18704  -0.02852 -0.00033 235 PHE B C   
3995 O O   . PHE B 235 ? 0.77474 0.50400 0.46859 0.16231  -0.02003 -0.00028 235 PHE B O   
3996 C CB  . PHE B 235 ? 0.68656 0.46820 0.37396 0.22292  -0.03938 -0.00707 235 PHE B CB  
3997 C CG  . PHE B 235 ? 0.66123 0.39707 0.31180 0.22707  -0.04454 0.00877  235 PHE B CG  
3998 C CD1 . PHE B 235 ? 0.80876 0.50614 0.42495 0.25920  -0.05835 0.01128  235 PHE B CD1 
3999 C CD2 . PHE B 235 ? 0.78193 0.50946 0.42800 0.20039  -0.03474 0.02118  235 PHE B CD2 
4000 C CE1 . PHE B 235 ? 0.89282 0.53905 0.46453 0.26376  -0.06227 0.02818  235 PHE B CE1 
4001 C CE2 . PHE B 235 ? 0.86162 0.54381 0.46727 0.20298  -0.03589 0.03659  235 PHE B CE2 
4002 C CZ  . PHE B 235 ? 0.90033 0.53870 0.46521 0.23444  -0.04972 0.04132  235 PHE B CZ  
4003 N N   . HIS B 236 ? 0.74248 0.37727 0.37826 0.18859  -0.03067 0.00826  236 HIS B N   
4004 C CA  . HIS B 236 ? 0.80984 0.40544 0.43985 0.15732  -0.02066 0.01714  236 HIS B CA  
4005 C C   . HIS B 236 ? 0.89153 0.44010 0.48340 0.15805  -0.01756 0.03523  236 HIS B C   
4006 O O   . HIS B 236 ? 0.97995 0.47643 0.53285 0.18068  -0.02565 0.04007  236 HIS B O   
4007 C CB  . HIS B 236 ? 0.78295 0.33435 0.40654 0.15162  -0.02286 0.00800  236 HIS B CB  
4008 C CG  . HIS B 236 ? 0.88423 0.40538 0.51365 0.11612  -0.01273 0.01182  236 HIS B CG  
4009 N ND1 . HIS B 236 ? 0.93848 0.43393 0.55450 0.09748  -0.00059 0.02776  236 HIS B ND1 
4010 C CD2 . HIS B 236 ? 0.84067 0.35529 0.48919 0.09582  -0.01285 -0.00029 236 HIS B CD2 
4011 C CE1 . HIS B 236 ? 0.90131 0.38021 0.53385 0.06538  0.00861  0.02474  236 HIS B CE1 
4012 N NE2 . HIS B 236 ? 0.94600 0.43721 0.60000 0.06425  -0.00068 0.00701  236 HIS B NE2 
4013 N N   . TYR B 237 ? 0.89674 0.45928 0.49502 0.13511  -0.00554 0.04517  237 TYR B N   
4014 C CA  . TYR B 237 ? 0.89721 0.41476 0.45299 0.13394  0.00074  0.06345  237 TYR B CA  
4015 C C   . TYR B 237 ? 0.93478 0.37789 0.46401 0.11319  0.01247  0.07224  237 TYR B C   
4016 O O   . TYR B 237 ? 0.99624 0.43950 0.55438 0.08818  0.01938  0.06336  237 TYR B O   
4017 C CB  . TYR B 237 ? 0.91052 0.46786 0.48071 0.11554  0.01248  0.06906  237 TYR B CB  
4018 C CG  . TYR B 237 ? 1.05716 0.57122 0.57633 0.11718  0.01955  0.08768  237 TYR B CG  
4019 C CD1 . TYR B 237 ? 1.05914 0.57728 0.54711 0.14801  0.00477  0.09212  237 TYR B CD1 
4020 C CD2 . TYR B 237 ? 1.05056 0.52004 0.55130 0.08812  0.04120  0.09983  237 TYR B CD2 
4021 C CE1 . TYR B 237 ? 1.06758 0.54412 0.50244 0.15182  0.00935  0.10848  237 TYR B CE1 
4022 C CE2 . TYR B 237 ? 1.09349 0.51738 0.53835 0.08963  0.05056  0.11839  237 TYR B CE2 
4023 C CZ  . TYR B 237 ? 1.17015 0.60373 0.58687 0.12136  0.03323  0.12019  237 TYR B CZ  
4024 O OH  . TYR B 237 ? 1.25329 0.66099 0.63039 0.12202  0.03934  0.13012  237 TYR B OH  
4025 N N   . VAL B 238 ? 1.14159 0.51903 0.61361 0.12302  0.01447  0.08947  238 VAL B N   
4026 C CA  . VAL B 238 ? 1.17894 0.48201 0.62216 0.09855  0.03000  0.09954  238 VAL B CA  
4027 C C   . VAL B 238 ? 1.17499 0.48978 0.63814 0.05669  0.05575  0.10541  238 VAL B C   
4028 O O   . VAL B 238 ? 1.26684 0.55124 0.70056 0.04217  0.07239  0.11910  238 VAL B O   
4029 C CB  . VAL B 238 ? 1.23437 0.49219 0.62577 0.11558  0.02668  0.11054  238 VAL B CB  
4030 C CG1 . VAL B 238 ? 1.34115 0.57439 0.71795 0.14659  0.00642  0.10128  238 VAL B CG1 
4031 C CG2 . VAL B 238 ? 1.20655 0.49400 0.57915 0.13318  0.02257  0.11840  238 VAL B CG2 
4032 N N   A ASP B 249 ? 1.57749 0.53574 0.85074 -0.01440 0.11568  0.15224  249 ASP B N   
4033 N N   B ASP B 249 ? 1.56305 0.52175 0.82186 -0.00075 0.11042  0.15519  249 ASP B N   
4034 C CA  A ASP B 249 ? 1.58269 0.47424 0.81266 0.00653  0.10206  0.15402  249 ASP B CA  
4035 C CA  B ASP B 249 ? 1.58703 0.47822 0.80801 0.01470  0.09903  0.15583  249 ASP B CA  
4036 C C   A ASP B 249 ? 1.57490 0.48677 0.82181 0.04074  0.07238  0.13778  249 ASP B C   
4037 C C   B ASP B 249 ? 1.57587 0.48720 0.81826 0.04504  0.07074  0.13859  249 ASP B C   
4038 O O   A ASP B 249 ? 1.45614 0.43156 0.73647 0.05600  0.06025  0.12847  249 ASP B O   
4039 O O   B ASP B 249 ? 1.46064 0.43534 0.73642 0.06088  0.05816  0.12906  249 ASP B O   
4040 C CB  A ASP B 249 ? 1.63219 0.46967 0.86503 -0.03241 0.12094  0.15394  249 ASP B CB  
4041 C CB  B ASP B 249 ? 1.62838 0.47110 0.85602 -0.02842 0.12110  0.15646  249 ASP B CB  
4042 C CG  A ASP B 249 ? 1.67381 0.49852 0.89880 -0.07083 0.15423  0.16731  249 ASP B CG  
4043 C CG  B ASP B 249 ? 1.75388 0.51104 0.91232 -0.02439 0.12848  0.17291  249 ASP B CG  
4044 O OD1 A ASP B 249 ? 1.60888 0.49011 0.88500 -0.10036 0.17065  0.16155  249 ASP B OD1 
4045 O OD1 B ASP B 249 ? 1.79804 0.53878 0.91835 -0.02904 0.14488  0.18937  249 ASP B OD1 
4046 O OD2 A ASP B 249 ? 1.77617 0.53409 0.94246 -0.07038 0.16444  0.18301  249 ASP B OD2 
4047 O OD2 B ASP B 249 ? 1.81353 0.51729 0.95282 -0.01550 0.11773  0.16896  249 ASP B OD2 
4048 N N   . LEU B 250 ? 1.67641 0.53259 0.89804 0.05334  0.06178  0.13417  250 LEU B N   
4049 C CA  . LEU B 250 ? 1.55727 0.42899 0.79702 0.08193  0.03698  0.11592  250 LEU B CA  
4050 C C   . LEU B 250 ? 1.60864 0.49829 0.90361 0.04946  0.04184  0.09849  250 LEU B C   
4051 O O   . LEU B 250 ? 1.56584 0.41062 0.86071 0.03594  0.04205  0.09054  250 LEU B O   
4052 C CB  . LEU B 250 ? 1.65054 0.45718 0.83953 0.11169  0.02297  0.11758  250 LEU B CB  
4053 C CG  . LEU B 250 ? 1.64447 0.47379 0.80858 0.16481  -0.00093 0.11661  250 LEU B CG  
4054 C CD1 . LEU B 250 ? 1.54381 0.44992 0.75932 0.18363  -0.01709 0.09691  250 LEU B CD1 
4055 C CD2 . LEU B 250 ? 1.68595 0.52672 0.82123 0.17249  0.00395  0.13304  250 LEU B CD2 
4056 N N   . GLN B 251 ? 1.62700 0.58317 0.96956 0.03663  0.04506  0.09143  251 GLN B N   
4057 C CA  . GLN B 251 ? 1.56441 0.55384 0.95994 0.02159  0.03920  0.06951  251 GLN B CA  
4058 C C   . GLN B 251 ? 1.56955 0.57690 0.96412 0.06357  0.01351  0.05464  251 GLN B C   
4059 O O   . GLN B 251 ? 1.52065 0.58711 0.93964 0.08096  0.00391  0.04674  251 GLN B O   
4060 C CB  . GLN B 251 ? 1.44269 0.49506 0.88384 -0.00088 0.04925  0.06662  251 GLN B CB  
4061 C CG  . GLN B 251 ? 1.45553 0.50172 0.89886 -0.03859 0.07686  0.08099  251 GLN B CG  
4062 C CD  . GLN B 251 ? 1.47009 0.58113 0.95634 -0.05579 0.08638  0.07797  251 GLN B CD  
4063 O OE1 . GLN B 251 ? 1.37303 0.52808 0.88150 -0.03767 0.07131  0.06729  251 GLN B OE1 
4064 N NE2 . GLN B 251 ? 1.61710 0.73541 1.11531 -0.09046 0.11254  0.08653  251 GLN B NE2 
4065 N N   . LYS B 252 ? 1.50529 0.46069 0.86921 0.08066  0.00402  0.05143  252 LYS B N   
4066 C CA  . LYS B 252 ? 1.51292 0.47943 0.88208 0.11200  -0.01667 0.03216  252 LYS B CA  
4067 C C   . LYS B 252 ? 1.43840 0.44842 0.85765 0.09598  -0.02062 0.00985  252 LYS B C   
4068 O O   . LYS B 252 ? 1.43194 0.47839 0.86264 0.12362  -0.03557 -0.00587 252 LYS B O   
4069 C CB  . LYS B 252 ? 1.56845 0.46062 0.90173 0.11769  -0.02046 0.03101  252 LYS B CB  
4070 C CG  . LYS B 252 ? 1.61781 0.50069 0.97312 0.11162  -0.02907 0.00701  252 LYS B CG  
4071 C CD  . LYS B 252 ? 1.73434 0.53683 1.05009 0.11682  -0.03149 0.00772  252 LYS B CD  
4072 C CE  . LYS B 252 ? 1.64878 0.43890 0.98564 0.10872  -0.03982 -0.01789 252 LYS B CE  
4073 N NZ  . LYS B 252 ? 1.79795 0.50524 1.09516 0.11380  -0.04196 -0.01763 252 LYS B NZ  
4074 N N   . GLY B 253 ? 1.46866 0.47883 0.91865 0.05168  -0.00723 0.00683  253 GLY B N   
4075 C CA  . GLY B 253 ? 1.36357 0.41056 0.85882 0.03528  -0.01377 -0.01706 253 GLY B CA  
4076 C C   . GLY B 253 ? 1.27992 0.39554 0.79604 0.05619  -0.02293 -0.02427 253 GLY B C   
4077 O O   . GLY B 253 ? 1.26982 0.41351 0.80609 0.06303  -0.03550 -0.04577 253 GLY B O   
4078 N N   . VAL B 254 ? 1.28741 0.43068 0.79711 0.06680  -0.01668 -0.00708 254 VAL B N   
4079 C CA  . VAL B 254 ? 1.17641 0.38363 0.70705 0.08535  -0.02386 -0.01369 254 VAL B CA  
4080 C C   . VAL B 254 ? 1.21905 0.44543 0.73950 0.12730  -0.03992 -0.02544 254 VAL B C   
4081 O O   . VAL B 254 ? 1.15679 0.42252 0.69829 0.13495  -0.04784 -0.04344 254 VAL B O   
4082 C CB  . VAL B 254 ? 1.19587 0.42746 0.72213 0.08745  -0.01367 0.00660  254 VAL B CB  
4083 C CG1 . VAL B 254 ? 0.98264 0.28532 0.52643 0.11690  -0.02302 0.00144  254 VAL B CG1 
4084 C CG2 . VAL B 254 ? 1.16915 0.42123 0.72823 0.04420  0.00285  0.01013  254 VAL B CG2 
4085 N N   . MET B 255 ? 1.24134 0.44083 0.72872 0.15443  -0.04443 -0.01690 255 MET B N   
4086 C CA  . MET B 255 ? 1.21475 0.44086 0.69737 0.19456  -0.05770 -0.02900 255 MET B CA  
4087 C C   . MET B 255 ? 1.20349 0.41955 0.69227 0.19473  -0.06515 -0.05112 255 MET B C   
4088 O O   . MET B 255 ? 1.18531 0.44761 0.68819 0.21438  -0.07118 -0.06633 255 MET B O   
4089 C CB  . MET B 255 ? 1.26175 0.46008 0.70841 0.22389  -0.06332 -0.01801 255 MET B CB  
4090 C CG  . MET B 255 ? 1.25074 0.42718 0.67442 0.21658  -0.05565 0.00557  255 MET B CG  
4091 S SD  . MET B 255 ? 1.26732 0.41814 0.64722 0.25921  -0.06852 0.01224  255 MET B SD  
4092 C CE  . MET B 255 ? 1.19044 0.43030 0.60222 0.29794  -0.08134 -0.00392 255 MET B CE  
4093 N N   . GLU B 256 ? 1.18921 0.34668 0.66732 0.17231  -0.06377 -0.05392 256 GLU B N   
4094 C CA  . GLU B 256 ? 1.21133 0.36084 0.69574 0.17135  -0.07214 -0.07696 256 GLU B CA  
4095 C C   . GLU B 256 ? 1.18013 0.37658 0.69879 0.15288  -0.07369 -0.09237 256 GLU B C   
4096 O O   . GLU B 256 ? 1.14031 0.35594 0.66336 0.16353  -0.08230 -0.11205 256 GLU B O   
4097 C CB  . GLU B 256 ? 1.35038 0.42769 0.81996 0.14839  -0.07033 -0.07852 256 GLU B CB  
4098 C CG  . GLU B 256 ? 1.33324 0.38638 0.81569 0.10459  -0.05673 -0.06688 256 GLU B CG  
4099 C CD  . GLU B 256 ? 1.44582 0.43981 0.92735 0.07579  -0.05458 -0.07600 256 GLU B CD  
4100 O OE1 . GLU B 256 ? 1.42429 0.43252 0.93466 0.05673  -0.06075 -0.09857 256 GLU B OE1 
4101 O OE2 . GLU B 256 ? 1.53743 0.47089 0.98831 0.07306  -0.04763 -0.06172 256 GLU B OE2 
4102 N N   . ARG B 257 ? 1.14836 0.36336 0.68857 0.12631  -0.06574 -0.08402 257 ARG B N   
4103 C CA  . ARG B 257 ? 1.17739 0.43453 0.74840 0.10904  -0.06971 -0.09937 257 ARG B CA  
4104 C C   . ARG B 257 ? 1.06023 0.37925 0.63655 0.13650  -0.07270 -0.10305 257 ARG B C   
4105 O O   . ARG B 257 ? 1.09114 0.44159 0.67854 0.13677  -0.08006 -0.12007 257 ARG B O   
4106 C CB  . ARG B 257 ? 1.09080 0.34825 0.68532 0.07127  -0.05999 -0.09099 257 ARG B CB  
4107 C CG  . ARG B 257 ? 1.11065 0.32874 0.71932 0.03366  -0.05831 -0.09999 257 ARG B CG  
4108 C CD  . ARG B 257 ? 1.11479 0.34846 0.75553 -0.00464 -0.04726 -0.09523 257 ARG B CD  
4109 N NE  . ARG B 257 ? 1.18547 0.39581 0.80964 -0.01093 -0.02780 -0.06785 257 ARG B NE  
4110 C CZ  . ARG B 257 ? 1.20853 0.44047 0.85773 -0.04048 -0.01150 -0.05723 257 ARG B CZ  
4111 N NH1 . ARG B 257 ? 1.18465 0.47668 0.88822 -0.06555 -0.01297 -0.07142 257 ARG B NH1 
4112 N NH2 . ARG B 257 ? 1.18194 0.38526 0.80430 -0.04226 0.00636  -0.03186 257 ARG B NH2 
4113 N N   . LEU B 258 ? 1.07068 0.40996 0.63923 0.15897  -0.06678 -0.08767 258 LEU B N   
4114 C CA  . LEU B 258 ? 1.07173 0.46974 0.64646 0.18654  -0.06741 -0.09332 258 LEU B CA  
4115 C C   . LEU B 258 ? 1.05575 0.45628 0.61861 0.20915  -0.07407 -0.10950 258 LEU B C   
4116 O O   . LEU B 258 ? 1.00459 0.44868 0.57467 0.21839  -0.07393 -0.12114 258 LEU B O   
4117 C CB  . LEU B 258 ? 0.98985 0.41094 0.56214 0.20774  -0.06190 -0.07727 258 LEU B CB  
4118 C CG  . LEU B 258 ? 0.95083 0.40602 0.54310 0.19078  -0.05305 -0.05950 258 LEU B CG  
4119 C CD1 . LEU B 258 ? 0.90359 0.41218 0.53015 0.16503  -0.04926 -0.06384 258 LEU B CD1 
4120 C CD2 . LEU B 258 ? 0.95617 0.36066 0.53345 0.17291  -0.04827 -0.04205 258 LEU B CD2 
4121 N N   . ARG B 259 ? 1.04313 0.39533 0.58476 0.21816  -0.07850 -0.10976 259 ARG B N   
4122 C CA  . ARG B 259 ? 1.08568 0.43751 0.61446 0.24174  -0.08418 -0.12550 259 ARG B CA  
4123 C C   . ARG B 259 ? 1.07950 0.42094 0.60924 0.22542  -0.09043 -0.14430 259 ARG B C   
4124 O O   . ARG B 259 ? 1.12632 0.49166 0.65093 0.24212  -0.09239 -0.15864 259 ARG B O   
4125 C CB  . ARG B 259 ? 1.16484 0.46392 0.66783 0.25794  -0.08833 -0.12086 259 ARG B CB  
4126 C CG  . ARG B 259 ? 1.18105 0.50691 0.67959 0.29166  -0.08794 -0.11269 259 ARG B CG  
4127 C CD  . ARG B 259 ? 1.19310 0.46340 0.66120 0.31083  -0.09496 -0.11018 259 ARG B CD  
4128 N NE  . ARG B 259 ? 1.21110 0.47496 0.66842 0.32155  -0.09540 -0.09136 259 ARG B NE  
4129 C CZ  . ARG B 259 ? 1.26118 0.46172 0.69205 0.30939  -0.09528 -0.07587 259 ARG B CZ  
4130 N NH1 . ARG B 259 ? 1.33991 0.47882 0.75756 0.28402  -0.09350 -0.07724 259 ARG B NH1 
4131 N NH2 . ARG B 259 ? 1.26397 0.46379 0.68111 0.32183  -0.09637 -0.05932 259 ARG B NH2 
4132 N N   . ARG B 260 ? 1.08298 0.39102 0.62002 0.19250  -0.09340 -0.14550 260 ARG B N   
4133 C CA  . ARG B 260 ? 1.09185 0.39453 0.63316 0.17653  -0.10272 -0.16594 260 ARG B CA  
4134 C C   . ARG B 260 ? 1.06628 0.42784 0.61995 0.17747  -0.10442 -0.17322 260 ARG B C   
4135 O O   . ARG B 260 ? 1.12705 0.49969 0.67146 0.18473  -0.11131 -0.18945 260 ARG B O   
4136 C CB  . ARG B 260 ? 1.15581 0.41851 0.71139 0.13829  -0.10493 -0.16745 260 ARG B CB  
4137 C CG  . ARG B 260 ? 1.23200 0.49152 0.79673 0.12041  -0.11754 -0.19160 260 ARG B CG  
4138 C CD  . ARG B 260 ? 1.27314 0.49177 0.85675 0.08190  -0.11767 -0.19570 260 ARG B CD  
4139 N NE  . ARG B 260 ? 1.31837 0.49271 0.89206 0.07697  -0.10430 -0.17465 260 ARG B NE  
4140 C CZ  . ARG B 260 ? 1.31873 0.48345 0.91198 0.04674  -0.09369 -0.16166 260 ARG B CZ  
4141 N NH1 . ARG B 260 ? 1.27438 0.47408 0.90410 0.01845  -0.09543 -0.16909 260 ARG B NH1 
4142 N NH2 . ARG B 260 ? 1.34540 0.46559 0.91988 0.04554  -0.08103 -0.14068 260 ARG B NH2 
4143 N N   . VAL B 261 ? 1.03850 0.43567 0.60908 0.17100  -0.09778 -0.16076 261 VAL B N   
4144 C CA  . VAL B 261 ? 0.96295 0.41268 0.54099 0.17282  -0.09815 -0.16530 261 VAL B CA  
4145 C C   . VAL B 261 ? 1.03848 0.52599 0.60423 0.20277  -0.08910 -0.16451 261 VAL B C   
4146 O O   . VAL B 261 ? 1.00594 0.53242 0.57089 0.20515  -0.08665 -0.16760 261 VAL B O   
4147 C CB  . VAL B 261 ? 0.88844 0.36202 0.48842 0.15548  -0.09362 -0.15361 261 VAL B CB  
4148 C CG1 . VAL B 261 ? 1.04820 0.48858 0.66606 0.12310  -0.09957 -0.15514 261 VAL B CG1 
4149 C CG2 . VAL B 261 ? 0.96507 0.45258 0.56594 0.16998  -0.07999 -0.13554 261 VAL B CG2 
4150 N N   . GLY B 262 ? 1.05278 0.53070 0.60971 0.22494  -0.08363 -0.16046 262 GLY B N   
4151 C CA  . GLY B 262 ? 0.93772 0.45222 0.48841 0.25228  -0.07504 -0.16447 262 GLY B CA  
4152 C C   . GLY B 262 ? 0.97543 0.52048 0.53829 0.27090  -0.06482 -0.15293 262 GLY B C   
4153 O O   . GLY B 262 ? 0.96652 0.54516 0.53075 0.29297  -0.05710 -0.15855 262 GLY B O   
4154 N N   . PHE B 263 ? 1.02408 0.56211 0.59736 0.26312  -0.06427 -0.13826 263 PHE B N   
4155 C CA  . PHE B 263 ? 0.98873 0.56129 0.57481 0.28160  -0.05737 -0.12877 263 PHE B CA  
4156 C C   . PHE B 263 ? 1.01615 0.57216 0.59117 0.30911  -0.06241 -0.13230 263 PHE B C   
4157 O O   . PHE B 263 ? 1.03173 0.53145 0.58547 0.30968  -0.07138 -0.13517 263 PHE B O   
4158 C CB  . PHE B 263 ? 0.92279 0.48293 0.51591 0.26777  -0.05735 -0.11187 263 PHE B CB  
4159 C CG  . PHE B 263 ? 0.93346 0.52660 0.54309 0.24812  -0.05017 -0.10814 263 PHE B CG  
4160 C CD1 . PHE B 263 ? 0.79611 0.45290 0.42620 0.25414  -0.03942 -0.10548 263 PHE B CD1 
4161 C CD2 . PHE B 263 ? 0.87429 0.44558 0.48756 0.21755  -0.05409 -0.10543 263 PHE B CD2 
4162 C CE1 . PHE B 263 ? 0.83704 0.53117 0.48781 0.22841  -0.03294 -0.09659 263 PHE B CE1 
4163 C CE2 . PHE B 263 ? 0.78578 0.40051 0.42318 0.19504  -0.04891 -0.09768 263 PHE B CE2 
4164 C CZ  . PHE B 263 ? 0.77050 0.44244 0.42348 0.20098  -0.03845 -0.09234 263 PHE B CZ  
4165 N N   . VAL B 264 ? 1.00392 0.61079 0.59539 0.33154  -0.05687 -0.13319 264 VAL B N   
4166 C CA  . VAL B 264 ? 1.00894 0.60928 0.59398 0.36110  -0.06336 -0.13757 264 VAL B CA  
4167 C C   . VAL B 264 ? 0.95255 0.58041 0.55211 0.37365  -0.06590 -0.12677 264 VAL B C   
4168 O O   . VAL B 264 ? 0.94993 0.61003 0.56785 0.36059  -0.06014 -0.11797 264 VAL B O   
4169 C CB  . VAL B 264 ? 0.95140 0.59227 0.54511 0.38071  -0.05622 -0.15542 264 VAL B CB  
4170 C CG1 . VAL B 264 ? 0.98419 0.59438 0.55765 0.36984  -0.05569 -0.16627 264 VAL B CG1 
4171 C CG2 . VAL B 264 ? 0.91546 0.63623 0.54347 0.37959  -0.04069 -0.15762 264 VAL B CG2 
4172 N N   . GLY B 265 ? 0.97031 0.58398 0.55940 0.40052  -0.07608 -0.12864 265 GLY B N   
4173 C CA  . GLY B 265 ? 0.96974 0.59901 0.56397 0.41548  -0.08384 -0.11934 265 GLY B CA  
4174 C C   . GLY B 265 ? 1.04525 0.63124 0.62189 0.39431  -0.08644 -0.09904 265 GLY B C   
4175 O O   . GLY B 265 ? 1.02801 0.64812 0.62005 0.39185  -0.08566 -0.09041 265 GLY B O   
4176 N N   . VAL B 266 ? 1.03251 0.54457 0.57852 0.37711  -0.08839 -0.09210 266 VAL B N   
4177 C CA  . VAL B 266 ? 1.00663 0.47698 0.53896 0.34977  -0.08587 -0.07363 266 VAL B CA  
4178 C C   . VAL B 266 ? 1.15778 0.57953 0.65666 0.36259  -0.09490 -0.06007 266 VAL B C   
4179 O O   . VAL B 266 ? 1.15299 0.51054 0.62062 0.36442  -0.09948 -0.05898 266 VAL B O   
4180 C CB  . VAL B 266 ? 1.04890 0.47195 0.57272 0.31934  -0.08131 -0.07546 266 VAL B CB  
4181 C CG1 . VAL B 266 ? 1.17350 0.54153 0.67986 0.29141  -0.07794 -0.05677 266 VAL B CG1 
4182 C CG2 . VAL B 266 ? 0.95771 0.42890 0.50951 0.30537  -0.07350 -0.08662 266 VAL B CG2 
4183 N N   . ARG B 267 ? 1.19857 0.65033 0.70169 0.37231  -0.09790 -0.05061 267 ARG B N   
4184 C CA  . ARG B 267 ? 1.22928 0.63849 0.69612 0.38593  -0.10704 -0.03763 267 ARG B CA  
4185 C C   . ARG B 267 ? 1.19774 0.61618 0.66354 0.37004  -0.10251 -0.02050 267 ARG B C   
4186 O O   . ARG B 267 ? 1.16235 0.63362 0.66142 0.35738  -0.09546 -0.02155 267 ARG B O   
4187 C CB  . ARG B 267 ? 1.31687 0.75843 0.78522 0.42744  -0.12168 -0.04961 267 ARG B CB  
4188 C CG  . ARG B 267 ? 1.29686 0.83323 0.81622 0.44166  -0.12088 -0.06771 267 ARG B CG  
4189 C CD  . ARG B 267 ? 1.36466 0.95852 0.90448 0.44940  -0.12588 -0.06493 267 ARG B CD  
4190 N NE  . ARG B 267 ? 1.33741 1.02338 0.93149 0.45453  -0.12081 -0.08202 267 ARG B NE  
4191 C CZ  . ARG B 267 ? 1.31078 1.05961 0.93680 0.45065  -0.11993 -0.08273 267 ARG B CZ  
4192 N NH1 . ARG B 267 ? 1.31724 1.04973 0.92526 0.44516  -0.12593 -0.06799 267 ARG B NH1 
4193 N NH2 . ARG B 267 ? 1.20988 1.03962 0.88643 0.45081  -0.11156 -0.09913 267 ARG B NH2 
4194 N N   . ARG B 268 ? 1.22850 0.59340 0.65301 0.37102  -0.10580 -0.00462 268 ARG B N   
4195 C CA  . ARG B 268 ? 1.34138 0.70636 0.75876 0.35194  -0.09874 0.01270  268 ARG B CA  
4196 C C   . ARG B 268 ? 1.25876 0.66357 0.67383 0.37935  -0.11181 0.01229  268 ARG B C   
4197 O O   . ARG B 268 ? 1.25048 0.65397 0.65157 0.41200  -0.12692 0.00406  268 ARG B O   
4198 C CB  . ARG B 268 ? 1.33116 0.61232 0.70510 0.32569  -0.08803 0.03195  268 ARG B CB  
4199 C CG  . ARG B 268 ? 1.36312 0.59371 0.68509 0.33986  -0.09375 0.04549  268 ARG B CG  
4200 C CD  . ARG B 268 ? 1.47314 0.64532 0.75879 0.36180  -0.10375 0.04186  268 ARG B CD  
4201 N NE  . ARG B 268 ? 1.52860 0.63639 0.75701 0.36504  -0.10370 0.05948  268 ARG B NE  
4202 C CZ  . ARG B 268 ? 1.62266 0.66837 0.80507 0.38675  -0.11308 0.06140  268 ARG B CZ  
4203 N NH1 . ARG B 268 ? 1.69152 0.72915 0.87869 0.40708  -0.12340 0.04646  268 ARG B NH1 
4204 N NH2 . ARG B 268 ? 1.71325 0.70144 0.84067 0.38895  -0.11170 0.07863  268 ARG B NH2 
4205 N N   . VAL B 269 ? 1.16548 0.60918 0.59705 0.36618  -0.10694 0.01916  269 VAL B N   
4206 C CA  . VAL B 269 ? 1.21745 0.70236 0.65001 0.38673  -0.11933 0.01774  269 VAL B CA  
4207 C C   . VAL B 269 ? 1.30887 0.74492 0.69850 0.37057  -0.11302 0.03880  269 VAL B C   
4208 O O   . VAL B 269 ? 1.30706 0.72860 0.69719 0.33708  -0.09578 0.05155  269 VAL B O   
4209 C CB  . VAL B 269 ? 1.27809 0.85398 0.76610 0.38541  -0.11948 0.00611  269 VAL B CB  
4210 C CG1 . VAL B 269 ? 1.24363 0.87221 0.74234 0.41388  -0.13757 -0.00477 269 VAL B CG1 
4211 C CG2 . VAL B 269 ? 1.13909 0.75403 0.66877 0.38650  -0.11479 -0.01054 269 VAL B CG2 
4212 N N   . GLU B 270 ? 1.39486 0.80726 0.74713 0.39491  -0.12646 0.04150  270 GLU B N   
4213 C CA  . GLU B 270 ? 1.48843 0.84706 0.79167 0.38174  -0.11920 0.06147  270 GLU B CA  
4214 C C   . GLU B 270 ? 1.28042 0.69035 0.60017 0.37354  -0.11845 0.06370  270 GLU B C   
4215 O O   . GLU B 270 ? 1.21779 0.60478 0.52210 0.34391  -0.10101 0.07934  270 GLU B O   
4216 C CB  . GLU B 270 ? 1.60996 0.91593 0.85931 0.41287  -0.13455 0.06396  270 GLU B CB  
4217 C CG  . GLU B 270 ? 1.64148 0.86246 0.85030 0.40682  -0.12708 0.07286  270 GLU B CG  
4218 C CD  . GLU B 270 ? 1.74195 0.90692 0.92670 0.36391  -0.10113 0.09354  270 GLU B CD  
4219 O OE1 . GLU B 270 ? 1.73000 0.86941 0.87864 0.35600  -0.09443 0.10825  270 GLU B OE1 
4220 O OE2 . GLU B 270 ? 1.69190 0.84202 0.89619 0.33763  -0.08708 0.09348  270 GLU B OE2 
4221 N N   . GLU B 271 ? 1.31453 0.79676 0.66835 0.39797  -0.13638 0.04657  271 GLU B N   
4222 C CA  . GLU B 271 ? 1.34921 0.87619 0.71268 0.39485  -0.14040 0.04644  271 GLU B CA  
4223 C C   . GLU B 271 ? 1.31127 0.86162 0.70040 0.35744  -0.12059 0.05417  271 GLU B C   
4224 O O   . GLU B 271 ? 1.35015 0.91056 0.72995 0.34520  -0.11680 0.06091  271 GLU B O   
4225 C CB  . GLU B 271 ? 1.37918 0.98766 0.78629 0.42387  -0.16244 0.02257  271 GLU B CB  
4226 C CG  . GLU B 271 ? 1.41031 1.06543 0.82683 0.42371  -0.17115 0.01870  271 GLU B CG  
4227 C CD  . GLU B 271 ? 1.37111 1.11168 0.83820 0.44855  -0.19208 -0.00789 271 GLU B CD  
4228 O OE1 . GLU B 271 ? 1.35295 1.14890 0.87373 0.44564  -0.18868 -0.02221 271 GLU B OE1 
4229 O OE2 . GLU B 271 ? 1.26199 1.01511 0.71561 0.47015  -0.21118 -0.01533 271 GLU B OE2 
4230 N N   . ALA B 272 ? 1.25411 0.81198 0.67317 0.33995  -0.10835 0.05252  272 ALA B N   
4231 C CA  . ALA B 272 ? 1.14425 0.71728 0.58390 0.30511  -0.08949 0.06013  272 ALA B CA  
4232 C C   . ALA B 272 ? 1.11624 0.62205 0.53242 0.27646  -0.06859 0.07540  272 ALA B C   
4233 O O   . ALA B 272 ? 1.12141 0.63581 0.55423 0.24660  -0.05185 0.08123  272 ALA B O   
4234 C CB  . ALA B 272 ? 1.02071 0.66368 0.51747 0.30562  -0.09187 0.04472  272 ALA B CB  
4235 N N   . LEU B 273 ? 1.18438 0.62504 0.56369 0.28390  -0.06919 0.08061  273 LEU B N   
4236 C CA  . LEU B 273 ? 1.26767 0.64415 0.62842 0.25563  -0.05029 0.09187  273 LEU B CA  
4237 C C   . LEU B 273 ? 1.17266 0.57201 0.57687 0.23669  -0.04221 0.08433  273 LEU B C   
4238 O O   . LEU B 273 ? 1.11098 0.50868 0.52769 0.20405  -0.02430 0.09122  273 LEU B O   
4239 C CB  . LEU B 273 ? 1.28199 0.62286 0.61220 0.22683  -0.03006 0.10991  273 LEU B CB  
4240 C CG  . LEU B 273 ? 1.28385 0.60153 0.56677 0.24142  -0.03487 0.11897  273 LEU B CG  
4241 C CD1 . LEU B 273 ? 1.21377 0.59537 0.51416 0.24920  -0.04282 0.11409  273 LEU B CD1 
4242 C CD2 . LEU B 273 ? 1.26600 0.51800 0.50783 0.21209  -0.01046 0.13710  273 LEU B CD2 
4243 N N   . GLY B 274 ? 1.14777 0.56984 0.57501 0.25871  -0.05551 0.06842  274 GLY B N   
4244 C CA  . GLY B 274 ? 1.06786 0.50911 0.53217 0.24530  -0.04993 0.05897  274 GLY B CA  
4245 C C   . GLY B 274 ? 1.10316 0.53973 0.57427 0.26753  -0.06091 0.04276  274 GLY B C   
4246 O O   . GLY B 274 ? 1.15392 0.57537 0.60311 0.29425  -0.07324 0.03911  274 GLY B O   
4247 N N   . VAL B 275 ? 1.09814 0.54768 0.59847 0.25650  -0.05622 0.03178  275 VAL B N   
4248 C CA  . VAL B 275 ? 1.04239 0.49603 0.55323 0.27419  -0.06378 0.01342  275 VAL B CA  
4249 C C   . VAL B 275 ? 0.92667 0.45722 0.48041 0.28693  -0.06551 -0.00216 275 VAL B C   
4250 O O   . VAL B 275 ? 0.94835 0.52713 0.53473 0.25861  -0.05497 -0.00165 275 VAL B O   
4251 C CB  . VAL B 275 ? 1.06081 0.46332 0.56688 0.24889  -0.05628 0.01002  275 VAL B CB  
4252 C CG1 . VAL B 275 ? 1.11934 0.53425 0.63736 0.26581  -0.06346 -0.01091 275 VAL B CG1 
4253 C CG2 . VAL B 275 ? 1.05746 0.38482 0.52314 0.23558  -0.05231 0.02409  275 VAL B CG2 
4254 N N   . VAL B 276 ? 0.91221 0.47578 0.47692 0.31572  -0.07443 -0.01801 276 VAL B N   
4255 C CA  . VAL B 276 ? 0.92259 0.56132 0.52900 0.32611  -0.07175 -0.03519 276 VAL B CA  
4256 C C   . VAL B 276 ? 0.95742 0.58923 0.56658 0.32969  -0.06944 -0.05156 276 VAL B C   
4257 O O   . VAL B 276 ? 1.04714 0.63395 0.63091 0.34029  -0.07670 -0.05336 276 VAL B O   
4258 C CB  . VAL B 276 ? 1.03484 0.73334 0.65943 0.35370  -0.08171 -0.04230 276 VAL B CB  
4259 C CG1 . VAL B 276 ? 1.05936 0.82636 0.72309 0.36717  -0.07747 -0.06456 276 VAL B CG1 
4260 C CG2 . VAL B 276 ? 0.88227 0.61547 0.51945 0.34267  -0.08131 -0.03182 276 VAL B CG2 
4261 N N   . ALA B 277 ? 0.93045 0.60454 0.56643 0.31967  -0.05882 -0.06328 277 ALA B N   
4262 C CA  . ALA B 277 ? 0.92934 0.59410 0.56218 0.31910  -0.05590 -0.07777 277 ALA B CA  
4263 C C   . ALA B 277 ? 0.91874 0.65623 0.58272 0.32209  -0.04449 -0.09219 277 ALA B C   
4264 O O   . ALA B 277 ? 0.83608 0.62637 0.52658 0.31035  -0.03630 -0.08885 277 ALA B O   
4265 C CB  . ALA B 277 ? 0.86358 0.47657 0.48105 0.29064  -0.05332 -0.07481 277 ALA B CB  
4266 N N   . ARG B 278 ? 0.89539 0.63675 0.55664 0.33053  -0.04254 -0.10585 278 ARG B N   
4267 C CA  . ARG B 278 ? 0.94564 0.74981 0.63096 0.33114  -0.02841 -0.11843 278 ARG B CA  
4268 C C   . ARG B 278 ? 0.97195 0.75494 0.64039 0.31558  -0.02258 -0.12467 278 ARG B C   
4269 O O   . ARG B 278 ? 0.99751 0.72544 0.64030 0.31598  -0.03227 -0.12730 278 ARG B O   
4270 C CB  . ARG B 278 ? 0.98850 0.82651 0.68794 0.35934  -0.03005 -0.13080 278 ARG B CB  
4271 C CG  . ARG B 278 ? 0.95286 0.87180 0.69466 0.36493  -0.02127 -0.13642 278 ARG B CG  
4272 C CD  . ARG B 278 ? 1.02793 0.94926 0.77540 0.37912  -0.03705 -0.12904 278 ARG B CD  
4273 N NE  . ARG B 278 ? 0.97609 0.97503 0.76696 0.37929  -0.03169 -0.13471 278 ARG B NE  
4274 C CZ  . ARG B 278 ? 1.11609 1.12746 0.91503 0.38406  -0.04361 -0.12791 278 ARG B CZ  
4275 N NH1 . ARG B 278 ? 1.04024 0.98899 0.80352 0.38692  -0.05822 -0.11211 278 ARG B NH1 
4276 N NH2 . ARG B 278 ? 1.05678 1.14400 0.89970 0.38341  -0.04003 -0.13731 278 ARG B NH2 
4277 N N   . LYS B 279 ? 0.88148 0.70649 0.56224 0.30072  -0.00746 -0.12691 279 LYS B N   
4278 C CA  . LYS B 279 ? 0.91626 0.72286 0.57616 0.29250  -0.00432 -0.13434 279 LYS B CA  
4279 C C   . LYS B 279 ? 0.87734 0.71163 0.54121 0.31067  0.00483  -0.14797 279 LYS B C   
4280 O O   . LYS B 279 ? 0.85336 0.74337 0.54547 0.31782  0.01737  -0.15141 279 LYS B O   
4281 C CB  . LYS B 279 ? 0.82522 0.65107 0.48489 0.26810  0.00639  -0.12889 279 LYS B CB  
4282 C CG  . LYS B 279 ? 0.86301 0.66889 0.49630 0.26066  0.00677  -0.13539 279 LYS B CG  
4283 C CD  . LYS B 279 ? 0.79395 0.61796 0.42369 0.23925  0.01622  -0.12756 279 LYS B CD  
4284 C CE  . LYS B 279 ? 0.72162 0.51541 0.32006 0.23291  0.00881  -0.13238 279 LYS B CE  
4285 N NZ  . LYS B 279 ? 0.74654 0.53455 0.33833 0.21308  0.00403  -0.12290 279 LYS B NZ  
4286 N N   . PRO B 280 ? 0.91790 0.71620 0.55606 0.31791  -0.00068 -0.15789 280 PRO B N   
4287 C CA  . PRO B 280 ? 0.87778 0.69874 0.51837 0.33841  0.00814  -0.17240 280 PRO B CA  
4288 C C   . PRO B 280 ? 0.94385 0.81816 0.59590 0.33025  0.03260  -0.17701 280 PRO B C   
4289 O O   . PRO B 280 ? 0.94217 0.83231 0.59627 0.30799  0.04212  -0.16776 280 PRO B O   
4290 C CB  . PRO B 280 ? 0.88069 0.64422 0.48600 0.34302  -0.00382 -0.18130 280 PRO B CB  
4291 C CG  . PRO B 280 ? 0.91588 0.62662 0.50706 0.32731  -0.02120 -0.17204 280 PRO B CG  
4292 C CD  . PRO B 280 ? 0.92522 0.66053 0.53407 0.30814  -0.01639 -0.15807 280 PRO B CD  
4293 N N   . GLU B 281 ? 0.96793 0.86576 0.62464 0.34738  0.04396  -0.19143 281 GLU B N   
4294 C CA  . GLU B 281 ? 0.96711 0.91329 0.63344 0.33936  0.07183  -0.19778 281 GLU B CA  
4295 C C   . GLU B 281 ? 0.91158 0.91304 0.61573 0.32387  0.08666  -0.19000 281 GLU B C   
4296 O O   . GLU B 281 ? 0.92104 0.94175 0.65461 0.33155  0.07640  -0.18678 281 GLU B O   
4297 C CB  . GLU B 281 ? 1.02163 0.93959 0.64793 0.32226  0.07831  -0.19609 281 GLU B CB  
4298 C CG  . GLU B 281 ? 1.03369 0.89525 0.62147 0.33371  0.06114  -0.20472 281 GLU B CG  
4299 C CD  . GLU B 281 ? 1.15784 1.02045 0.71695 0.33527  0.07775  -0.21637 281 GLU B CD  
4300 O OE1 . GLU B 281 ? 1.12789 0.97373 0.65703 0.31835  0.07970  -0.21070 281 GLU B OE1 
4301 O OE2 . GLU B 281 ? 1.07762 0.95700 0.64237 0.35474  0.08836  -0.23156 281 GLU B OE2 
# 
