data_9CA5
# 
_entry.id   9CA5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9CA5         pdb_00009ca5 10.2210/pdb9ca5/pdb 
WWPDB D_1000285021 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CA5 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-17 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              f.jon.kull@dartmouth.edu 
_pdbx_contact_author.name_first         F 
_pdbx_contact_author.name_last          Kull 
_pdbx_contact_author.name_mi            Jon 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5191-3200 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tolbert, J.D.' 1 ? 
'Midget, C.R.'  2 ? 
'Kull, F.J.'    3 ? 
# 
loop_
_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 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? ?  ? ? primary 'To Be Published'                                ?      0353 ?         ? ? ?  ? ?   ?   
'Structure of Regulatory protein Rns'                                                                        ?    ? ? ?        ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861 877 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix' 2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tolbert, J.F.'     1  ?                   
primary 'Talbot, K.M.'      2  ?                   
primary 'Midgett, C.R.'     3  ?                   
primary 'Munson, G.P.'      4  ?                   
primary 'Kull, F.J.'        5  ?                   
1       'Liebschner, D.'    6  0000-0003-3921-3209 
1       'Afonine, P.V.'     7  0000-0002-5052-991X 
1       'Baker, M.L.'       8  ?                   
1       'Bunkoczi, G.'      9  ?                   
1       'Chen, V.B.'        10 0000-0003-2492-979X 
1       'Croll, T.I.'       11 ?                   
1       'Hintze, B.'        12 0000-0002-4871-2096 
1       'Hung, L.W.'        13 0000-0001-6690-8458 
1       'Jain, S.'          14 ?                   
1       'McCoy, A.J.'       15 ?                   
1       'Moriarty, N.W.'    16 0000-0001-8857-9464 
1       'Oeffner, R.D.'     17 0000-0003-3107-2202 
1       'Poon, B.K.'        18 0000-0001-9633-6067 
1       'Prisant, M.G.'     19 ?                   
1       'Read, R.J.'        20 0000-0001-8273-0047 
1       'Richardson, J.S.'  21 0000-0002-3311-2944 
1       'Richardson, D.C.'  22 ?                   
1       'Sammito, M.D.'     23 0000-0002-8346-9247 
1       'Sobolev, O.V.'     24 0000-0002-0623-3214 
1       'Stockwell, D.H.'   25 ?                   
1       'Terwilliger, T.C.' 26 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  27 ?                   
1       'Videau, L.L.'      28 ?                   
1       'Williams, C.J.'    29 ?                   
1       'Adams, P.D.'       30 0000-0001-9333-8219 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'AraC-family, transcriptional regulator Rns' 
_entity.formula_weight             30802.756 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;MDFKYTEEKETIKINNIMIAKYTVLYTSNCIMDIYSEEEKITCFSNRLVFLERGVNISVRMQKQILSEKPYVAFRLNGDM
LRHLKDALMIIYGMSKIDTNACRSMSRKIMTTEVNKTLLDELKNINSHDNSAFISSLIYLISKLENNEKIIESIYISSVS
FFSDKVRNLIEKDLSRKWTLGIIADAFNASEITIRKRLESENTNFNQILMQLRMSKAALLLLENSYQISQISNMIGISSA
SYFIRIFNKHYGVTPKQFFTYFKGG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDFKYTEEKETIKINNIMIAKYTVLYTSNCIMDIYSEEEKITCFSNRLVFLERGVNISVRMQKQILSEKPYVAFRLNGDM
LRHLKDALMIIYGMSKIDTNACRSMSRKIMTTEVNKTLLDELKNINSHDNSAFISSLIYLISKLENNEKIIESIYISSVS
FFSDKVRNLIEKDLSRKWTLGIIADAFNASEITIRKRLESENTNFNQILMQLRMSKAALLLLENSYQISQISNMIGISSA
SYFIRIFNKHYGVTPKQFFTYFKGG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   PHE n 
1 4   LYS n 
1 5   TYR n 
1 6   THR n 
1 7   GLU n 
1 8   GLU n 
1 9   LYS n 
1 10  GLU n 
1 11  THR n 
1 12  ILE n 
1 13  LYS n 
1 14  ILE n 
1 15  ASN n 
1 16  ASN n 
1 17  ILE n 
1 18  MET n 
1 19  ILE n 
1 20  ALA n 
1 21  LYS n 
1 22  TYR n 
1 23  THR n 
1 24  VAL n 
1 25  LEU n 
1 26  TYR n 
1 27  THR n 
1 28  SER n 
1 29  ASN n 
1 30  CYS n 
1 31  ILE n 
1 32  MET n 
1 33  ASP n 
1 34  ILE n 
1 35  TYR n 
1 36  SER n 
1 37  GLU n 
1 38  GLU n 
1 39  GLU n 
1 40  LYS n 
1 41  ILE n 
1 42  THR n 
1 43  CYS n 
1 44  PHE n 
1 45  SER n 
1 46  ASN n 
1 47  ARG n 
1 48  LEU n 
1 49  VAL n 
1 50  PHE n 
1 51  LEU n 
1 52  GLU n 
1 53  ARG n 
1 54  GLY n 
1 55  VAL n 
1 56  ASN n 
1 57  ILE n 
1 58  SER n 
1 59  VAL n 
1 60  ARG n 
1 61  MET n 
1 62  GLN n 
1 63  LYS n 
1 64  GLN n 
1 65  ILE n 
1 66  LEU n 
1 67  SER n 
1 68  GLU n 
1 69  LYS n 
1 70  PRO n 
1 71  TYR n 
1 72  VAL n 
1 73  ALA n 
1 74  PHE n 
1 75  ARG n 
1 76  LEU n 
1 77  ASN n 
1 78  GLY n 
1 79  ASP n 
1 80  MET n 
1 81  LEU n 
1 82  ARG n 
1 83  HIS n 
1 84  LEU n 
1 85  LYS n 
1 86  ASP n 
1 87  ALA n 
1 88  LEU n 
1 89  MET n 
1 90  ILE n 
1 91  ILE n 
1 92  TYR n 
1 93  GLY n 
1 94  MET n 
1 95  SER n 
1 96  LYS n 
1 97  ILE n 
1 98  ASP n 
1 99  THR n 
1 100 ASN n 
1 101 ALA n 
1 102 CYS n 
1 103 ARG n 
1 104 SER n 
1 105 MET n 
1 106 SER n 
1 107 ARG n 
1 108 LYS n 
1 109 ILE n 
1 110 MET n 
1 111 THR n 
1 112 THR n 
1 113 GLU n 
1 114 VAL n 
1 115 ASN n 
1 116 LYS n 
1 117 THR n 
1 118 LEU n 
1 119 LEU n 
1 120 ASP n 
1 121 GLU n 
1 122 LEU n 
1 123 LYS n 
1 124 ASN n 
1 125 ILE n 
1 126 ASN n 
1 127 SER n 
1 128 HIS n 
1 129 ASP n 
1 130 ASN n 
1 131 SER n 
1 132 ALA n 
1 133 PHE n 
1 134 ILE n 
1 135 SER n 
1 136 SER n 
1 137 LEU n 
1 138 ILE n 
1 139 TYR n 
1 140 LEU n 
1 141 ILE n 
1 142 SER n 
1 143 LYS n 
1 144 LEU n 
1 145 GLU n 
1 146 ASN n 
1 147 ASN n 
1 148 GLU n 
1 149 LYS n 
1 150 ILE n 
1 151 ILE n 
1 152 GLU n 
1 153 SER n 
1 154 ILE n 
1 155 TYR n 
1 156 ILE n 
1 157 SER n 
1 158 SER n 
1 159 VAL n 
1 160 SER n 
1 161 PHE n 
1 162 PHE n 
1 163 SER n 
1 164 ASP n 
1 165 LYS n 
1 166 VAL n 
1 167 ARG n 
1 168 ASN n 
1 169 LEU n 
1 170 ILE n 
1 171 GLU n 
1 172 LYS n 
1 173 ASP n 
1 174 LEU n 
1 175 SER n 
1 176 ARG n 
1 177 LYS n 
1 178 TRP n 
1 179 THR n 
1 180 LEU n 
1 181 GLY n 
1 182 ILE n 
1 183 ILE n 
1 184 ALA n 
1 185 ASP n 
1 186 ALA n 
1 187 PHE n 
1 188 ASN n 
1 189 ALA n 
1 190 SER n 
1 191 GLU n 
1 192 ILE n 
1 193 THR n 
1 194 ILE n 
1 195 ARG n 
1 196 LYS n 
1 197 ARG n 
1 198 LEU n 
1 199 GLU n 
1 200 SER n 
1 201 GLU n 
1 202 ASN n 
1 203 THR n 
1 204 ASN n 
1 205 PHE n 
1 206 ASN n 
1 207 GLN n 
1 208 ILE n 
1 209 LEU n 
1 210 MET n 
1 211 GLN n 
1 212 LEU n 
1 213 ARG n 
1 214 MET n 
1 215 SER n 
1 216 LYS n 
1 217 ALA n 
1 218 ALA n 
1 219 LEU n 
1 220 LEU n 
1 221 LEU n 
1 222 LEU n 
1 223 GLU n 
1 224 ASN n 
1 225 SER n 
1 226 TYR n 
1 227 GLN n 
1 228 ILE n 
1 229 SER n 
1 230 GLN n 
1 231 ILE n 
1 232 SER n 
1 233 ASN n 
1 234 MET n 
1 235 ILE n 
1 236 GLY n 
1 237 ILE n 
1 238 SER n 
1 239 SER n 
1 240 ALA n 
1 241 SER n 
1 242 TYR n 
1 243 PHE n 
1 244 ILE n 
1 245 ARG n 
1 246 ILE n 
1 247 PHE n 
1 248 ASN n 
1 249 LYS n 
1 250 HIS n 
1 251 TYR n 
1 252 GLY n 
1 253 VAL n 
1 254 THR n 
1 255 PRO n 
1 256 LYS n 
1 257 GLN n 
1 258 PHE n 
1 259 PHE n 
1 260 THR n 
1 261 TYR n 
1 262 PHE n 
1 263 LYS n 
1 264 GLY n 
1 265 GLY 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                   265 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   TYR 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  CYS 43  43  43  CYS CYS A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  GLN 64  64  64  GLN GLN A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  HIS 83  83  83  HIS HIS A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  MET 94  94  94  MET MET A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  LYS 96  96  ?   ?   ?   A . n 
A 1 97  ILE 97  97  ?   ?   ?   A . n 
A 1 98  ASP 98  98  ?   ?   ?   A . n 
A 1 99  THR 99  99  ?   ?   ?   A . n 
A 1 100 ASN 100 100 ?   ?   ?   A . n 
A 1 101 ALA 101 101 ?   ?   ?   A . n 
A 1 102 CYS 102 102 ?   ?   ?   A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 ILE 154 154 154 ILE ILE A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ARG 176 176 176 ARG ARG A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 TRP 178 178 178 TRP TRP A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 MET 214 214 214 MET MET A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 TYR 226 226 226 TYR TYR A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 GLN 230 230 230 GLN GLN A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 TYR 242 242 242 TYR TYR A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 LYS 263 263 ?   ?   ?   A . n 
A 1 264 GLY 264 264 ?   ?   ?   A . n 
A 1 265 GLY 265 265 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   ?   ?   ?   B . n 
B 1 3   PHE 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   TYR 5   5   ?   ?   ?   B . n 
B 1 6   THR 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   GLU 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLU 10  10  10  GLU GLU B . n 
B 1 11  THR 11  11  11  THR THR B . n 
B 1 12  ILE 12  12  12  ILE ILE B . n 
B 1 13  LYS 13  13  13  LYS LYS B . n 
B 1 14  ILE 14  14  14  ILE ILE B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  MET 18  18  18  MET MET B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  THR 23  23  23  THR THR B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  TYR 26  26  26  TYR TYR B . n 
B 1 27  THR 27  27  27  THR THR B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  ASN 29  29  29  ASN ASN B . n 
B 1 30  CYS 30  30  30  CYS CYS B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  MET 32  32  32  MET MET B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ILE 34  34  34  ILE ILE B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  LYS 40  40  40  LYS LYS B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  THR 42  42  42  THR THR B . n 
B 1 43  CYS 43  43  43  CYS CYS B . n 
B 1 44  PHE 44  44  44  PHE PHE B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  ASN 46  46  46  ASN ASN B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  LEU 48  48  48  LEU LEU B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  GLU 52  52  52  GLU GLU B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  LYS 63  63  63  LYS LYS B . n 
B 1 64  GLN 64  64  64  GLN GLN B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  ARG 75  75  75  ARG ARG B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  ASP 79  79  79  ASP ASP B . n 
B 1 80  MET 80  80  80  MET MET B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  HIS 83  83  83  HIS HIS B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  LYS 85  85  85  LYS LYS B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  MET 89  89  89  MET MET B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  TYR 92  92  92  TYR TYR B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  MET 94  94  ?   ?   ?   B . n 
B 1 95  SER 95  95  ?   ?   ?   B . n 
B 1 96  LYS 96  96  ?   ?   ?   B . n 
B 1 97  ILE 97  97  ?   ?   ?   B . n 
B 1 98  ASP 98  98  ?   ?   ?   B . n 
B 1 99  THR 99  99  ?   ?   ?   B . n 
B 1 100 ASN 100 100 ?   ?   ?   B . n 
B 1 101 ALA 101 101 ?   ?   ?   B . n 
B 1 102 CYS 102 102 ?   ?   ?   B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 MET 105 105 105 MET MET B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 GLU 113 113 113 GLU GLU B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 THR 117 117 117 THR THR B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 HIS 128 128 128 HIS HIS B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 ASN 130 130 130 ASN ASN B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 TYR 139 139 139 TYR TYR B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 ASN 147 147 147 ASN ASN B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 ILE 154 154 154 ILE ILE B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ILE 156 156 156 ILE ILE B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 SER 163 163 163 SER SER B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 LYS 165 165 165 LYS LYS B . n 
B 1 166 VAL 166 166 166 VAL VAL B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 ASN 168 168 168 ASN ASN B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 ASP 173 173 173 ASP ASP B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 ARG 176 176 176 ARG ARG B . n 
B 1 177 LYS 177 177 177 LYS LYS B . n 
B 1 178 TRP 178 178 178 TRP TRP B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 PHE 187 187 187 PHE PHE B . n 
B 1 188 ASN 188 188 188 ASN ASN B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 ILE 194 194 194 ILE ILE B . n 
B 1 195 ARG 195 195 195 ARG ARG B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 ARG 197 197 197 ARG ARG B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 GLU 201 201 201 GLU GLU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 ASN 204 204 204 ASN ASN B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 GLN 207 207 207 GLN GLN B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 MET 210 210 210 MET MET B . n 
B 1 211 GLN 211 211 211 GLN GLN B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 MET 214 214 214 MET MET B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 LYS 216 216 216 LYS LYS B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 ALA 218 218 218 ALA ALA B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 ASN 224 224 224 ASN ASN B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 TYR 226 226 226 TYR TYR B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 ILE 228 228 228 ILE ILE B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 GLN 230 230 230 GLN GLN B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ILE 235 235 235 ILE ILE B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 SER 241 241 241 SER SER B . n 
B 1 242 TYR 242 242 242 TYR TYR B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 GLY 252 252 252 GLY GLY B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 LYS 256 256 256 LYS LYS B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 PHE 258 258 258 PHE PHE B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 TYR 261 261 261 TYR TYR B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 LYS 263 263 263 LYS LYS B . n 
B 1 264 GLY 264 264 ?   ?   ?   B . n 
B 1 265 GLY 265 265 ?   ?   ?   B . n 
# 
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 ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
# 
_cell.volume             638916.248 
_cell.length_a           47.730 
_cell.length_b           97.930 
_cell.length_c           136.690 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           9CA5 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.entry_id                         9CA5 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_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                   9CA5 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1:1 v/v DMSO, 0.1 M succinnic acid, 14% PEG 3350, 0.03 M glycyl-glycyl-gylcine' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-01-22 
_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   0.979351 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979351 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          87.44 
_reflns.entry_id                                       9CA5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.9 
_reflns.d_resolution_low                               46.1 
_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                                     13705 
_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                           92.34 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.08 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   0.996 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.9 
_reflns_shell.d_res_low                                     3 
_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                             1448 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.0739 
_reflns_shell.pdbx_CC_star                                  0.371 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.ls_percent_reflns_R_free                 10.02 
_refine.pdbx_overall_phase_error                 41.2600 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.2694 
_refine.B_iso_mean                               101.08 
_refine.ls_number_reflns_R_free                  1372 
_refine.ls_percent_reflns_obs                    92.37 
_refine.ls_R_factor_R_work                       0.2641 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.90 
_refine.ls_number_reflns_obs                     13705 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  12336 
_refine.ls_d_res_low                             46.10 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.3149 
_refine.overall_SU_ML                            0.5663 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.entry_id                                 9CA5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4025 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4025 
_refine_hist.d_res_high                       2.90 
_refine_hist.d_res_low                        46.10 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           4083 0.0063  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          5479 0.7493  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     635  0.0478  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      677  0.0078  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 1559 15.4249 ? ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    0.753985605881 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' 2.90 3.00  1372 0.4099 99.31 0.4560 146 . . . . . . . 
'X-RAY DIFFRACTION' 3.00 3.12  1290 0.3723 99.38 0.3819 144 . . . . . . . 
'X-RAY DIFFRACTION' 3.12 3.27  1305 0.3434 99.93 0.3838 146 . . . . . . . 
'X-RAY DIFFRACTION' 3.27 3.41  1136 0.3156 99.37 0.3881 125 . . . . . . . 
'X-RAY DIFFRACTION' 3.47 3.64  1040 0.2912 99.14 0.3789 115 . . . . . . . 
'X-RAY DIFFRACTION' 3.70 3.94  815  0.2917 75.88 0.3599 91  . . . . . . . 
'X-RAY DIFFRACTION' 3.94 4.33  1332 0.2452 99.66 0.3314 149 . . . . . . . 
'X-RAY DIFFRACTION' 4.33 4.96  1331 0.2066 99.20 0.3035 148 . . . . . . . 
'X-RAY DIFFRACTION' 4.96 6.24  1353 0.2752 99.41 0.2989 151 . . . . . . . 
'X-RAY DIFFRACTION' 6.25 46.10 1429 0.2355 99.19 0.2449 161 . . . . . . . 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   -0.999666916069 
_struct_ncs_oper.matrix[1][2]   -0.0257700862902 
_struct_ncs_oper.matrix[1][3]   -0.00139984635365 
_struct_ncs_oper.matrix[2][1]   -0.0257320729036 
_struct_ncs_oper.matrix[2][2]   0.999415308827 
_struct_ncs_oper.matrix[2][3]   -0.0225144599249 
_struct_ncs_oper.matrix[3][1]   0.00197922745089 
_struct_ncs_oper.matrix[3][2]   -0.0224709397717 
_struct_ncs_oper.matrix[3][3]   -0.999745537387 
_struct_ncs_oper.vector[1]      -0.0803531543984 
_struct_ncs_oper.vector[2]      0.189633716683 
_struct_ncs_oper.vector[3]      18.1995524988 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 9 through 93 or resid 103 through 124 or resid 126 through 127 or resid 130 through 171 or resid 173 through 176 or resid 178 through 262))
;
ens_1 d_2 
;(chain "B" and (resid 9 through 124 or resid 126 through 127 or resid 130 through 171 or resid 173 through 176 or resid 178 through 262))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A LYS 9   . A GLY 93  . A LYS 9   A GLY 93  ? ? 
ens_1 d_1 2 A ARG 103 . A ASN 124 . A ARG 103 A ASN 124 ? ? 
ens_1 d_1 3 A ASN 126 . A SER 127 . A ASN 126 A SER 127 ? ? 
ens_1 d_1 4 A ASN 130 . A GLU 171 . A ASN 130 A GLU 171 ? ? 
ens_1 d_1 5 A ASP 173 . A ARG 176 . A ASP 173 A ARG 176 ? ? 
ens_1 d_1 6 A TRP 178 . A PHE 262 . A TRP 178 A PHE 262 ? ? 
ens_1 d_2 1 B LYS 9   . B ASN 124 . B LYS 9   B ASN 124 ? ? 
ens_1 d_2 2 B ASN 126 . B SER 127 . B ASN 126 B SER 127 ? ? 
ens_1 d_2 3 B ASN 130 . B GLU 171 . B ASN 130 B GLU 171 ? ? 
ens_1 d_2 4 B ASP 173 . B ARG 176 . B ASP 173 B ARG 176 ? ? 
ens_1 d_2 5 B TRP 178 . B PHE 262 . B TRP 178 B PHE 262 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9CA5 
_struct.title                        'Rns pocket mutant - H20A' 
_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        9CA5 
_struct_keywords.text            'Mutation, DNA Binding, AraC Family, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A7ZGQ6_ECO24 
_struct_ref.pdbx_db_accession          A7ZGQ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDFKYTEEKETIKINNIMIHKYTVLYTSNCIMDIYSEEEKITCFSNRLVFLERGVNISVRMQKQILSEKPYVAFRLNGDM
LRHLKDALMIIYGMSKIDTNACRSMSRKIMTTEVNKTLLDELKNINSHDNSAFISSLIYLISKLENNEKIIESIYISSVS
FFSDKVRNLIEKDLSRKWTLGIIADAFNASEITIRKRLESENTNFNQILMQLRMSKAALLLLENSYQISQISNMIGISSA
SYFIRIFNKHYGVTPKQFFTYFKGG
;
_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 9CA5 A 1 ? 265 ? A7ZGQ6 1 ? 265 ? 1 265 
2 1 9CA5 B 1 ? 265 ? A7ZGQ6 1 ? 265 ? 1 265 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CA5 ALA A 20 ? UNP A7ZGQ6 HIS 20 'engineered mutation' 20 1 
2 9CA5 ALA B 20 ? UNP A7ZGQ6 HIS 20 'engineered mutation' 20 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1540  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  25330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 77  ? TYR A 92  ? ASN A 77  TYR A 92  1 ? 16 
HELX_P HELX_P2  AA2 SER A 104 ? ARG A 107 ? SER A 104 ARG A 107 5 ? 4  
HELX_P HELX_P3  AA3 ASN A 115 ? ILE A 125 ? ASN A 115 ILE A 125 1 ? 11 
HELX_P HELX_P4  AA4 ASP A 129 ? LYS A 143 ? ASP A 129 LYS A 143 1 ? 15 
HELX_P HELX_P5  AA5 ASN A 146 ? SER A 157 ? ASN A 146 SER A 157 1 ? 12 
HELX_P HELX_P6  AA6 PHE A 161 ? ASP A 173 ? PHE A 161 ASP A 173 1 ? 13 
HELX_P HELX_P7  AA7 THR A 179 ? PHE A 187 ? THR A 179 PHE A 187 1 ? 9  
HELX_P HELX_P8  AA8 SER A 190 ? GLU A 201 ? SER A 190 GLU A 201 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 204 ? GLU A 223 ? ASN A 204 GLU A 223 1 ? 20 
HELX_P HELX_P10 AB1 GLN A 227 ? GLY A 236 ? GLN A 227 GLY A 236 1 ? 10 
HELX_P HELX_P11 AB2 SER A 239 ? GLY A 252 ? SER A 239 GLY A 252 1 ? 14 
HELX_P HELX_P12 AB3 THR A 254 ? PHE A 262 ? THR A 254 PHE A 262 1 ? 9  
HELX_P HELX_P13 AB4 ASN B 77  ? TYR B 92  ? ASN B 77  TYR B 92  1 ? 16 
HELX_P HELX_P14 AB5 SER B 104 ? ARG B 107 ? SER B 104 ARG B 107 5 ? 4  
HELX_P HELX_P15 AB6 ASN B 115 ? ASN B 124 ? ASN B 115 ASN B 124 1 ? 10 
HELX_P HELX_P16 AB7 ASP B 129 ? LYS B 143 ? ASP B 129 LYS B 143 1 ? 15 
HELX_P HELX_P17 AB8 ASN B 146 ? SER B 157 ? ASN B 146 SER B 157 1 ? 12 
HELX_P HELX_P18 AB9 PHE B 161 ? LYS B 172 ? PHE B 161 LYS B 172 1 ? 12 
HELX_P HELX_P19 AC1 THR B 179 ? PHE B 187 ? THR B 179 PHE B 187 1 ? 9  
HELX_P HELX_P20 AC2 SER B 190 ? GLU B 201 ? SER B 190 GLU B 201 1 ? 12 
HELX_P HELX_P21 AC3 ASN B 204 ? GLU B 223 ? ASN B 204 GLU B 223 1 ? 20 
HELX_P HELX_P22 AC4 GLN B 227 ? GLY B 236 ? GLN B 227 GLY B 236 1 ? 10 
HELX_P HELX_P23 AC5 SER B 239 ? GLY B 252 ? SER B 239 GLY B 252 1 ? 14 
HELX_P HELX_P24 AC6 THR B 254 ? LYS B 263 ? THR B 254 LYS B 263 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
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 
AA1 3 4 ? 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 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 THR A 11  ? MET A 18  ? THR A 11  MET A 18  
AA1 2 ASN A 56  ? LYS A 63  ? ASN A 56  LYS A 63  
AA1 3 CYS A 30  ? SER A 36  ? CYS A 30  SER A 36  
AA1 4 GLU A 39  ? CYS A 43  ? GLU A 39  CYS A 43  
AA2 1 VAL A 72  ? LEU A 76  ? VAL A 72  LEU A 76  
AA2 2 TYR A 22  ? TYR A 26  ? TYR A 22  TYR A 26  
AA2 3 ARG A 47  ? LEU A 51  ? ARG A 47  LEU A 51  
AA2 4 ILE A 109 ? GLU A 113 ? ILE A 109 GLU A 113 
AA3 1 THR B 11  ? MET B 18  ? THR B 11  MET B 18  
AA3 2 ASN B 56  ? LYS B 63  ? ASN B 56  LYS B 63  
AA3 3 CYS B 30  ? SER B 36  ? CYS B 30  SER B 36  
AA3 4 GLU B 39  ? CYS B 43  ? GLU B 39  CYS B 43  
AA4 1 VAL B 72  ? LEU B 76  ? VAL B 72  LEU B 76  
AA4 2 TYR B 22  ? TYR B 26  ? TYR B 22  TYR B 26  
AA4 3 ARG B 47  ? LEU B 51  ? ARG B 47  LEU B 51  
AA4 4 ILE B 109 ? GLU B 113 ? ILE B 109 GLU B 113 
# 
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 17 ? N ILE A 17 O ILE A 57  ? O ILE A 57  
AA1 2 3 O SER A 58 ? O SER A 58 N TYR A 35  ? N TYR A 35  
AA1 3 4 N ILE A 34 ? N ILE A 34 O ILE A 41  ? O ILE A 41  
AA2 1 2 O VAL A 72 ? O VAL A 72 N TYR A 26  ? N TYR A 26  
AA2 2 3 N LEU A 25 ? N LEU A 25 O VAL A 49  ? O VAL A 49  
AA2 3 4 N LEU A 48 ? N LEU A 48 O THR A 112 ? O THR A 112 
AA3 1 2 N ILE B 17 ? N ILE B 17 O ILE B 57  ? O ILE B 57  
AA3 2 3 O SER B 58 ? O SER B 58 N TYR B 35  ? N TYR B 35  
AA3 3 4 N ILE B 34 ? N ILE B 34 O ILE B 41  ? O ILE B 41  
AA4 1 2 O PHE B 74 ? O PHE B 74 N VAL B 24  ? N VAL B 24  
AA4 2 3 N LEU B 25 ? N LEU B 25 O VAL B 49  ? O VAL B 49  
AA4 3 4 N LEU B 48 ? N LEU B 48 O THR B 112 ? O THR B 112 
# 
_pdbx_entry_details.entry_id                   9CA5 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ARG 
_pdbx_validate_rmsd_bond.auth_seq_id_1             197 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            ARG 
_pdbx_validate_rmsd_bond.auth_seq_id_2             197 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.674 
_pdbx_validate_rmsd_bond.bond_target_value         1.515 
_pdbx_validate_rmsd_bond.bond_deviation            0.159 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.025 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 28  ? ? 56.46   -110.69 
2 1 ASN A 29  ? ? -97.97  45.76   
3 1 LYS A 143 ? ? -88.48  30.17   
4 1 SER B 28  ? ? 56.90   -110.19 
5 1 ASN B 29  ? ? -100.10 47.98   
6 1 ASN B 124 ? ? -86.36  47.11   
7 1 SER B 127 ? ? -79.28  39.64   
8 1 HIS B 128 ? ? -133.47 -56.24  
9 1 ASP B 173 ? ? -158.23 79.70   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_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[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 11.6004480288  -7.90334351676 -4.1054607499  0.735115767161 0.64811946795  0.795224500386 
-0.0604082437381  -0.0704304443412 0.0908296799434  4.19609618462  2.59186600639 7.45875576285  -1.00363975888  -4.40763529029  
2.61344024099   0.0641085262376 0.0850775282818  -0.402402890632  0.486289494554  -0.0978308990343 0.143988645605   
-0.167138223638 -0.197275788711  0.0667028917576  
2 ? 'X-RAY DIFFRACTION' refined 14.070147032   12.6959742857  -11.9334922667 0.620203206162 0.859386411921 0.732714920358 
-0.161736962002   -0.0322362694904 -0.0852815934195 4.81326563494  7.60516962833 7.06204166335  -1.11917005229  -2.90334638122  
-4.98209525915  0.45191725511   -0.0679234177468 0.624592424286   0.74192167115   -1.09481767546   -0.666006632174  
-0.555378162474 0.382688047334   0.947063781877   
3 ? 'X-RAY DIFFRACTION' refined 11.5594810561  -2.40469121074 -26.547451097  0.599741761886 0.79918228318  0.673728516649 
-0.0223706708942  0.0707787399505  0.0365713756129  6.20516316331  4.03834194249 4.43192991287  -4.61205949168  1.15529709448   
0.772674823446  -0.161562807756 0.312281768674   -0.410021756887  -0.109306425419 -0.0231406117506 0.36286504905    
-0.485844449702 0.528092448127   -0.018802919934  
4 ? 'X-RAY DIFFRACTION' refined -11.6275292266 -2.88663464915 24.4156351709  0.917922076283 0.730283177618 0.761319203629 
-0.00450554901618 -0.0542825973665 -0.0447513399046 2.45106157616  1.30402268455 0.690171959195 -0.188176691358 0.217152106214  
-0.268722030874 0.144503584721  0.393057289425   -0.184598759007  -0.152529771535 -0.238994426959  0.00298081340288 
0.0496443243239 -0.0684720729301 0.0565828031107  
5 ? 'X-RAY DIFFRACTION' refined -13.5138542811 1.55451975462  42.3694349475  0.504061196871 0.812777489584 0.778426304896 
0.000315203101073 -0.0384121765618 -0.0292097101339 0.460069241102 7.82884868122 0.777695449372 0.257328994028  -0.407108218443 
-2.1688569345   0.185395369925  -0.150214023121  0.00189907036491 0.107778922095  -0.0955727371335 0.949025667146   0.14590068036 
-0.242322954009  -0.0507744778883 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 9   A 1   A 143 A 128 . 
;chain 'A' and (resid 9 through 143 )
;
2 2 'X-RAY DIFFRACTION' A 144 A 129 A 204 A 189 . 
;chain 'A' and (resid 144 through 204 )
;
3 3 'X-RAY DIFFRACTION' A 205 A 190 A 262 A 247 . 
;chain 'A' and (resid 205 through 262 )
;
4 4 'X-RAY DIFFRACTION' B 9   B 1   B 190 B 173 . 
;chain 'B' and (resid 9 through 190 )
;
5 5 'X-RAY DIFFRACTION' B 191 B 174 B 263 B 246 . 
;chain 'B' and (resid 191 through 263 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ASP 2   ? A ASP 2   
3  1 Y 1 A PHE 3   ? A PHE 3   
4  1 Y 1 A LYS 4   ? A LYS 4   
5  1 Y 1 A TYR 5   ? A TYR 5   
6  1 Y 1 A THR 6   ? A THR 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A GLU 8   ? A GLU 8   
9  1 Y 1 A LYS 96  ? A LYS 96  
10 1 Y 1 A ILE 97  ? A ILE 97  
11 1 Y 1 A ASP 98  ? A ASP 98  
12 1 Y 1 A THR 99  ? A THR 99  
13 1 Y 1 A ASN 100 ? A ASN 100 
14 1 Y 1 A ALA 101 ? A ALA 101 
15 1 Y 1 A CYS 102 ? A CYS 102 
16 1 Y 1 A LYS 263 ? A LYS 263 
17 1 Y 1 A GLY 264 ? A GLY 264 
18 1 Y 1 A GLY 265 ? A GLY 265 
19 1 Y 1 B MET 1   ? B MET 1   
20 1 Y 1 B ASP 2   ? B ASP 2   
21 1 Y 1 B PHE 3   ? B PHE 3   
22 1 Y 1 B LYS 4   ? B LYS 4   
23 1 Y 1 B TYR 5   ? B TYR 5   
24 1 Y 1 B THR 6   ? B THR 6   
25 1 Y 1 B GLU 7   ? B GLU 7   
26 1 Y 1 B GLU 8   ? B GLU 8   
27 1 Y 1 B MET 94  ? B MET 94  
28 1 Y 1 B SER 95  ? B SER 95  
29 1 Y 1 B LYS 96  ? B LYS 96  
30 1 Y 1 B ILE 97  ? B ILE 97  
31 1 Y 1 B ASP 98  ? B ASP 98  
32 1 Y 1 B THR 99  ? B THR 99  
33 1 Y 1 B ASN 100 ? B ASN 100 
34 1 Y 1 B ALA 101 ? B ALA 101 
35 1 Y 1 B CYS 102 ? B CYS 102 
36 1 Y 1 B GLY 264 ? B GLY 264 
37 1 Y 1 B GLY 265 ? B GLY 265 
# 
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 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI168157 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6xiu 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CA5 
_atom_sites.fract_transf_matrix[1][1]   0.020951 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010211 
_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]   0.007316 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . LYS A 1 9   ? 19.19548  -21.48499 -23.93740 1.000 98.32235  ?  9   LYS A N   1 
ATOM 2    C CA  . LYS A 1 9   ? 19.42125  -22.13633 -22.65578 1.000 107.26046 ?  9   LYS A CA  1 
ATOM 3    C C   . LYS A 1 9   ? 18.44498  -21.61986 -21.61089 1.000 113.15747 ?  9   LYS A C   1 
ATOM 4    O O   . LYS A 1 9   ? 17.51439  -20.87904 -21.92751 1.000 111.96040 ?  9   LYS A O   1 
ATOM 5    C CB  . LYS A 1 9   ? 20.85021  -21.88879 -22.17555 1.000 107.95867 ?  9   LYS A CB  1 
ATOM 6    C CG  . LYS A 1 9   ? 21.92978  -22.49687 -23.03985 1.000 96.38177  ?  9   LYS A CG  1 
ATOM 7    C CD  . LYS A 1 9   ? 23.29327  -22.14487 -22.47738 1.000 93.40039  ?  9   LYS A CD  1 
ATOM 8    C CE  . LYS A 1 9   ? 24.40594  -22.73946 -23.31063 1.000 110.21091 ?  9   LYS A CE  1 
ATOM 9    N NZ  . LYS A 1 9   ? 25.72891  -22.36226 -22.75350 1.000 109.25288 ?  9   LYS A NZ  1 
ATOM 10   N N   . GLU A 1 10  ? 18.67288  -22.01279 -20.35966 1.000 120.49897 ?  10  GLU A N   1 
ATOM 11   C CA  . GLU A 1 10  ? 17.92425  -21.50452 -19.21918 1.000 121.42425 ?  10  GLU A CA  1 
ATOM 12   C C   . GLU A 1 10  ? 18.62628  -20.33531 -18.55393 1.000 119.03569 ?  10  GLU A C   1 
ATOM 13   O O   . GLU A 1 10  ? 18.26168  -19.95558 -17.43765 1.000 119.22892 ?  10  GLU A O   1 
ATOM 14   C CB  . GLU A 1 10  ? 17.70538  -22.60536 -18.18189 1.000 130.37044 ?  10  GLU A CB  1 
ATOM 15   C CG  . GLU A 1 10  ? 18.95997  -23.39055 -17.86351 1.000 135.29189 ?  10  GLU A CG  1 
ATOM 16   C CD  . GLU A 1 10  ? 19.13261  -24.60275 -18.75174 1.000 155.99226 ?  10  GLU A CD  1 
ATOM 17   O OE1 . GLU A 1 10  ? 19.33619  -24.43018 -19.97409 1.000 159.54790 ?  10  GLU A OE1 1 
ATOM 18   O OE2 . GLU A 1 10  ? 19.08035  -25.72949 -18.21946 1.000 162.28706 -1 10  GLU A OE2 1 
ATOM 19   N N   . THR A 1 11  ? 19.62685  -19.76682 -19.20524 1.000 91.83748  ?  11  THR A N   1 
ATOM 20   C CA  . THR A 1 11  ? 20.43321  -18.71281 -18.62082 1.000 94.24633  ?  11  THR A CA  1 
ATOM 21   C C   . THR A 1 11  ? 20.33185  -17.46450 -19.47884 1.000 91.92835  ?  11  THR A C   1 
ATOM 22   O O   . THR A 1 11  ? 20.36663  -17.53506 -20.71203 1.000 98.88251  ?  11  THR A O   1 
ATOM 23   C CB  . THR A 1 11  ? 21.90063  -19.14676 -18.47701 1.000 88.38093  ?  11  THR A CB  1 
ATOM 24   O OG1 . THR A 1 11  ? 22.31945  -19.84176 -19.65816 1.000 112.43122 ?  11  THR A OG1 1 
ATOM 25   C CG2 . THR A 1 11  ? 22.06761  -20.06049 -17.28117 1.000 94.39910  ?  11  THR A CG2 1 
ATOM 26   N N   . ILE A 1 12  ? 20.16444  -16.32407 -18.81452 1.000 86.07014  ?  12  ILE A N   1 
ATOM 27   C CA  . ILE A 1 12  ? 20.10489  -15.03704 -19.48909 1.000 72.50768  ?  12  ILE A CA  1 
ATOM 28   C C   . ILE A 1 12  ? 20.93860  -14.04335 -18.69867 1.000 75.60120  ?  12  ILE A C   1 
ATOM 29   O O   . ILE A 1 12  ? 21.18727  -14.21205 -17.50416 1.000 88.04177  ?  12  ILE A O   1 
ATOM 30   C CB  . ILE A 1 12  ? 18.66569  -14.50757 -19.65577 1.000 78.44826  ?  12  ILE A CB  1 
ATOM 31   C CG1 . ILE A 1 12  ? 18.61095  -13.44776 -20.76175 1.000 62.38719  ?  12  ILE A CG1 1 
ATOM 32   C CG2 . ILE A 1 12  ? 18.15267  -13.94508 -18.34171 1.000 80.66082  ?  12  ILE A CG2 1 
ATOM 33   C CD1 . ILE A 1 12  ? 17.22808  -13.25875 -21.35588 1.000 82.90696  ?  12  ILE A CD1 1 
ATOM 34   N N   . LYS A 1 13  ? 21.39721  -13.01129 -19.39940 1.000 75.69582  ?  13  LYS A N   1 
ATOM 35   C CA  . LYS A 1 13  ? 22.11364  -11.89280 -18.79347 1.000 67.05068  ?  13  LYS A CA  1 
ATOM 36   C C   . LYS A 1 13  ? 21.53268  -10.62995 -19.41170 1.000 63.02149  ?  13  LYS A C   1 
ATOM 37   O O   . LYS A 1 13  ? 21.83585  -10.30335 -20.56168 1.000 77.20088  ?  13  LYS A O   1 
ATOM 38   C CB  . LYS A 1 13  ? 23.61471  -11.97847 -19.02685 1.000 78.13046  ?  13  LYS A CB  1 
ATOM 39   C CG  . LYS A 1 13  ? 24.42927  -11.03120 -18.16201 1.000 78.54817  ?  13  LYS A CG  1 
ATOM 40   C CD  . LYS A 1 13  ? 25.77130  -10.78037 -18.81847 1.000 99.32374  ?  13  LYS A CD  1 
ATOM 41   C CE  . LYS A 1 13  ? 25.66953  -9.66035  -19.85128 1.000 108.12766 ?  13  LYS A CE  1 
ATOM 42   N NZ  . LYS A 1 13  ? 25.99268  -8.31329  -19.29457 1.000 101.12144 ?  13  LYS A NZ  1 
ATOM 43   N N   . ILE A 1 14  ? 20.66414  -9.96104  -18.67511 1.000 71.92395  ?  14  ILE A N   1 
ATOM 44   C CA  . ILE A 1 14  ? 20.04543  -8.73126  -19.15225 1.000 64.02049  ?  14  ILE A CA  1 
ATOM 45   C C   . ILE A 1 14  ? 20.74244  -7.54894  -18.50405 1.000 63.94437  ?  14  ILE A C   1 
ATOM 46   O O   . ILE A 1 14  ? 21.02250  -7.55424  -17.29688 1.000 72.42169  ?  14  ILE A O   1 
ATOM 47   C CB  . ILE A 1 14  ? 18.53380  -8.71543  -18.87240 1.000 70.15189  ?  14  ILE A CB  1 
ATOM 48   C CG1 . ILE A 1 14  ? 17.90059  -10.01985 -19.36083 1.000 58.11580  ?  14  ILE A CG1 1 
ATOM 49   C CG2 . ILE A 1 14  ? 17.89778  -7.53126  -19.56874 1.000 69.92579  ?  14  ILE A CG2 1 
ATOM 50   C CD1 . ILE A 1 14  ? 16.42161  -10.07228 -19.17817 1.000 78.73690  ?  14  ILE A CD1 1 
ATOM 51   N N   . ASN A 1 15  ? 20.98976  -6.51795  -19.29448 1.000 78.95671  ?  15  ASN A N   1 
ATOM 52   C CA  . ASN A 1 15  ? 21.68675  -5.33237  -18.83433 1.000 81.48079  ?  15  ASN A CA  1 
ATOM 53   C C   . ASN A 1 15  ? 20.69894  -4.18664  -18.67531 1.000 81.53837  ?  15  ASN A C   1 
ATOM 54   O O   . ASN A 1 15  ? 19.56900  -4.24150  -19.15908 1.000 85.07822  ?  15  ASN A O   1 
ATOM 55   C CB  . ASN A 1 15  ? 22.79414  -4.94791  -19.82485 1.000 88.08793  ?  15  ASN A CB  1 
ATOM 56   C CG  . ASN A 1 15  ? 23.83156  -6.04749  -20.00588 1.000 79.41527  ?  15  ASN A CG  1 
ATOM 57   O OD1 . ASN A 1 15  ? 24.74011  -6.20676  -19.19300 1.000 78.78286  ?  15  ASN A OD1 1 
ATOM 58   N ND2 . ASN A 1 15  ? 23.69314  -6.81366  -21.07792 1.000 95.40573  ?  15  ASN A ND2 1 
ATOM 59   N N   . ASN A 1 16  ? 21.15373  -3.14410  -17.98712 1.000 63.45596  ?  16  ASN A N   1 
ATOM 60   C CA  . ASN A 1 16  ? 20.42799  -1.88011  -17.83686 1.000 65.02840  ?  16  ASN A CA  1 
ATOM 61   C C   . ASN A 1 16  ? 18.95548  -2.07882  -17.49986 1.000 69.02019  ?  16  ASN A C   1 
ATOM 62   O O   . ASN A 1 16  ? 18.06949  -1.46962  -18.10111 1.000 74.69775  ?  16  ASN A O   1 
ATOM 63   C CB  . ASN A 1 16  ? 20.56941  -1.02420  -19.08813 1.000 66.44839  ?  16  ASN A CB  1 
ATOM 64   C CG  . ASN A 1 16  ? 21.99749  -0.67312  -19.38625 1.000 78.51012  ?  16  ASN A CG  1 
ATOM 65   O OD1 . ASN A 1 16  ? 22.74416  -0.25310  -18.50113 1.000 82.41104  ?  16  ASN A OD1 1 
ATOM 66   N ND2 . ASN A 1 16  ? 22.39864  -0.85924  -20.63471 1.000 74.53914  ?  16  ASN A ND2 1 
ATOM 67   N N   . ILE A 1 17  ? 18.69242  -2.93363  -16.51863 1.000 73.25769  ?  17  ILE A N   1 
ATOM 68   C CA  . ILE A 1 17  ? 17.34277  -3.06705  -15.98456 1.000 61.76014  ?  17  ILE A CA  1 
ATOM 69   C C   . ILE A 1 17  ? 17.11730  -1.98464  -14.93920 1.000 61.54656  ?  17  ILE A C   1 
ATOM 70   O O   . ILE A 1 17  ? 17.84093  -1.90900  -13.94378 1.000 76.46171  ?  17  ILE A O   1 
ATOM 71   C CB  . ILE A 1 17  ? 17.09797  -4.46875  -15.41009 1.000 68.17728  ?  17  ILE A CB  1 
ATOM 72   C CG1 . ILE A 1 17  ? 17.37540  -5.51814  -16.49219 1.000 66.27579  ?  17  ILE A CG1 1 
ATOM 73   C CG2 . ILE A 1 17  ? 15.70955  -4.57806  -14.80813 1.000 71.52854  ?  17  ILE A CG2 1 
ATOM 74   C CD1 . ILE A 1 17  ? 16.79991  -6.88781  -16.18695 1.000 80.00130  ?  17  ILE A CD1 1 
ATOM 75   N N   . MET A 1 18  ? 16.12053  -1.13694  -15.18052 1.000 69.98851  ?  18  MET A N   1 
ATOM 76   C CA  . MET A 1 18  ? 15.77391  -0.03164  -14.29464 1.000 74.62722  ?  18  MET A CA  1 
ATOM 77   C C   . MET A 1 18  ? 14.55908  -0.38523  -13.45179 1.000 77.06666  ?  18  MET A C   1 
ATOM 78   O O   . MET A 1 18  ? 13.50531  -0.74218  -13.99002 1.000 84.37028  ?  18  MET A O   1 
ATOM 79   C CB  . MET A 1 18  ? 15.47178  1.23257   -15.09636 1.000 78.58690  ?  18  MET A CB  1 
ATOM 80   C CG  . MET A 1 18  ? 14.72409  2.28519   -14.29019 1.000 76.82451  ?  18  MET A CG  1 
ATOM 81   S SD  . MET A 1 18  ? 15.76935  3.41340   -13.37119 1.000 114.51048 ?  18  MET A SD  1 
ATOM 82   C CE  . MET A 1 18  ? 14.56232  4.64054   -12.87709 1.000 104.35352 ?  18  MET A CE  1 
ATOM 83   N N   . ILE A 1 19  ? 14.69641  -0.24782  -12.13722 1.000 82.38915  ?  19  ILE A N   1 
ATOM 84   C CA  . ILE A 1 19  ? 13.59100  -0.48022  -11.21655 1.000 69.89491  ?  19  ILE A CA  1 
ATOM 85   C C   . ILE A 1 19  ? 12.83420  0.83559   -11.09145 1.000 74.51679  ?  19  ILE A C   1 
ATOM 86   O O   . ILE A 1 19  ? 13.33664  1.79922   -10.50883 1.000 82.80127  ?  19  ILE A O   1 
ATOM 87   C CB  . ILE A 1 19  ? 14.08302  -0.97710  -9.85376  1.000 68.63847  ?  19  ILE A CB  1 
ATOM 88   C CG1 . ILE A 1 19  ? 14.48204  -2.45383  -9.92959  1.000 77.12087  ?  19  ILE A CG1 1 
ATOM 89   C CG2 . ILE A 1 19  ? 13.00712  -0.79184  -8.80336  1.000 78.86741  ?  19  ILE A CG2 1 
ATOM 90   C CD1 . ILE A 1 19  ? 15.85951  -2.71492  -10.52665 1.000 68.39847  ?  19  ILE A CD1 1 
ATOM 91   N N   . ALA A 1 20  ? 11.61857  0.87600   -11.63221 1.000 65.70435  ?  20  ALA A N   1 
ATOM 92   C CA  . ALA A 1 20  ? 10.83941  2.10350   -11.65175 1.000 68.57928  ?  20  ALA A CA  1 
ATOM 93   C C   . ALA A 1 20  ? 9.77657   2.13558   -10.57281 1.000 73.04722  ?  20  ALA A C   1 
ATOM 94   O O   . ALA A 1 20  ? 9.26593   3.21360   -10.25504 1.000 84.32017  ?  20  ALA A O   1 
ATOM 95   C CB  . ALA A 1 20  ? 10.17256  2.29290   -13.01783 1.000 70.96797  ?  20  ALA A CB  1 
ATOM 96   N N   . LYS A 1 21  ? 9.46153   0.98920   -9.99130  1.000 66.33376  ?  21  LYS A N   1 
ATOM 97   C CA  . LYS A 1 21  ? 8.49358   0.87427   -8.91894  1.000 66.26394  ?  21  LYS A CA  1 
ATOM 98   C C   . LYS A 1 21  ? 9.13167   0.01840   -7.84156  1.000 75.66743  ?  21  LYS A C   1 
ATOM 99   O O   . LYS A 1 21  ? 9.82993   -0.94882  -8.16263  1.000 64.93776  ?  21  LYS A O   1 
ATOM 100  C CB  . LYS A 1 21  ? 7.19967   0.22256   -9.42437  1.000 69.50803  ?  21  LYS A CB  1 
ATOM 101  C CG  . LYS A 1 21  ? 6.56985   0.90536   -10.63411 1.000 70.22867  ?  21  LYS A CG  1 
ATOM 102  C CD  . LYS A 1 21  ? 5.27082   0.21776   -11.05931 1.000 84.21932  ?  21  LYS A CD  1 
ATOM 103  C CE  . LYS A 1 21  ? 4.71982   0.79687   -12.36407 1.000 109.79911 ?  21  LYS A CE  1 
ATOM 104  N NZ  . LYS A 1 21  ? 3.68664   -0.08681  -12.99450 1.000 122.89172 ?  21  LYS A NZ  1 
ATOM 105  N N   . TYR A 1 22  ? 8.92215   0.38508   -6.57307  1.000 76.75586  ?  22  TYR A N   1 
ATOM 106  C CA  . TYR A 1 22  ? 9.45875   -0.42308  -5.48577  1.000 71.67550  ?  22  TYR A CA  1 
ATOM 107  C C   . TYR A 1 22  ? 9.07420   -1.88123  -5.70108  1.000 79.14997  ?  22  TYR A C   1 
ATOM 108  O O   . TYR A 1 22  ? 7.89582   -2.19434  -5.89480  1.000 78.85380  ?  22  TYR A O   1 
ATOM 109  C CB  . TYR A 1 22  ? 8.95047   0.07091   -4.13106  1.000 64.85423  ?  22  TYR A CB  1 
ATOM 110  C CG  . TYR A 1 22  ? 9.78111   -0.52395  -3.02766  1.000 79.76351  ?  22  TYR A CG  1 
ATOM 111  C CD1 . TYR A 1 22  ? 10.96615  0.07919   -2.63389  1.000 79.49075  ?  22  TYR A CD1 1 
ATOM 112  C CD2 . TYR A 1 22  ? 9.42362   -1.72417  -2.42921  1.000 63.99961  ?  22  TYR A CD2 1 
ATOM 113  C CE1 . TYR A 1 22  ? 11.75271  -0.47195  -1.64933  1.000 80.75161  ?  22  TYR A CE1 1 
ATOM 114  C CE2 . TYR A 1 22  ? 10.20735  -2.28643  -1.44417  1.000 63.46322  ?  22  TYR A CE2 1 
ATOM 115  C CZ  . TYR A 1 22  ? 11.37353  -1.65531  -1.05690  1.000 84.75876  ?  22  TYR A CZ  1 
ATOM 116  O OH  . TYR A 1 22  ? 12.17041  -2.20191  -0.07275  1.000 86.46785  ?  22  TYR A OH  1 
ATOM 117  N N   . THR A 1 23  ? 10.07032  -2.77008  -5.73955  1.000 71.09182  ?  23  THR A N   1 
ATOM 118  C CA  . THR A 1 23  ? 9.85759   -4.13672  -6.20277  1.000 74.63614  ?  23  THR A CA  1 
ATOM 119  C C   . THR A 1 23  ? 10.23217  -5.13991  -5.12422  1.000 66.80949  ?  23  THR A C   1 
ATOM 120  O O   . THR A 1 23  ? 11.31649  -5.06118  -4.53795  1.000 81.73937  ?  23  THR A O   1 
ATOM 121  C CB  . THR A 1 23  ? 10.65127  -4.42441  -7.48678  1.000 77.51099  ?  23  THR A CB  1 
ATOM 122  O OG1 . THR A 1 23  ? 10.21485  -3.54346  -8.53201  1.000 72.65609  ?  23  THR A OG1 1 
ATOM 123  C CG2 . THR A 1 23  ? 10.46317  -5.87775  -7.92899  1.000 71.11080  ?  23  THR A CG2 1 
ATOM 124  N N   . VAL A 1 24  ? 9.32436   -6.06713  -4.85780  1.000 65.22707  ?  24  VAL A N   1 
ATOM 125  C CA  . VAL A 1 24  ? 9.57679   -7.21570  -4.00290  1.000 76.18054  ?  24  VAL A CA  1 
ATOM 126  C C   . VAL A 1 24  ? 9.50742   -8.44596  -4.89362  1.000 74.39906  ?  24  VAL A C   1 
ATOM 127  O O   . VAL A 1 24  ? 8.44034   -8.78671  -5.41680  1.000 75.54995  ?  24  VAL A O   1 
ATOM 128  C CB  . VAL A 1 24  ? 8.56945   -7.30067  -2.85038  1.000 70.34847  ?  24  VAL A CB  1 
ATOM 129  C CG1 . VAL A 1 24  ? 9.00923   -8.34187  -1.83663  1.000 59.56192  ?  24  VAL A CG1 1 
ATOM 130  C CG2 . VAL A 1 24  ? 8.41761   -5.94056  -2.20358  1.000 72.26654  ?  24  VAL A CG2 1 
ATOM 131  N N   . LEU A 1 25  ? 10.63943  -9.10688  -5.07863  1.000 64.89254  ?  25  LEU A N   1 
ATOM 132  C CA  . LEU A 1 25  ? 10.74744  -10.23575 -5.98653  1.000 73.03335  ?  25  LEU A CA  1 
ATOM 133  C C   . LEU A 1 25  ? 10.98679  -11.51250 -5.19207  1.000 76.72239  ?  25  LEU A C   1 
ATOM 134  O O   . LEU A 1 25  ? 11.78881  -11.52479 -4.26082  1.000 92.71712  ?  25  LEU A O   1 
ATOM 135  C CB  . LEU A 1 25  ? 11.89108  -9.99997  -6.97224  1.000 75.83218  ?  25  LEU A CB  1 
ATOM 136  C CG  . LEU A 1 25  ? 11.92220  -10.84602 -8.23408  1.000 82.66270  ?  25  LEU A CG  1 
ATOM 137  C CD1 . LEU A 1 25  ? 12.32890  -9.97772  -9.40729  1.000 84.42254  ?  25  LEU A CD1 1 
ATOM 138  C CD2 . LEU A 1 25  ? 12.89107  -11.99156 -8.04080  1.000 86.28114  ?  25  LEU A CD2 1 
ATOM 139  N N   . TYR A 1 26  ? 10.30868  -12.59335 -5.56362  1.000 74.41211  ?  26  TYR A N   1 
ATOM 140  C CA  . TYR A 1 26  ? 10.52386  -13.90391 -4.96186  1.000 76.95384  ?  26  TYR A CA  1 
ATOM 141  C C   . TYR A 1 26  ? 11.21774  -14.76119 -6.00931  1.000 82.90265  ?  26  TYR A C   1 
ATOM 142  O O   . TYR A 1 26  ? 10.59455  -15.14899 -7.00651  1.000 90.61665  ?  26  TYR A O   1 
ATOM 143  C CB  . TYR A 1 26  ? 9.21880   -14.54111 -4.49887  1.000 82.93410  ?  26  TYR A CB  1 
ATOM 144  C CG  . TYR A 1 26  ? 9.45535   -15.79639 -3.68855  1.000 95.68097  ?  26  TYR A CG  1 
ATOM 145  C CD1 . TYR A 1 26  ? 10.04709  -15.71993 -2.43778  1.000 98.51370  ?  26  TYR A CD1 1 
ATOM 146  C CD2 . TYR A 1 26  ? 9.10848   -17.05197 -4.17250  1.000 98.82941  ?  26  TYR A CD2 1 
ATOM 147  C CE1 . TYR A 1 26  ? 10.28337  -16.85297 -1.68258  1.000 117.06613 ?  26  TYR A CE1 1 
ATOM 148  C CE2 . TYR A 1 26  ? 9.33869   -18.19781 -3.42289  1.000 94.42603  ?  26  TYR A CE2 1 
ATOM 149  C CZ  . TYR A 1 26  ? 9.92779   -18.09204 -2.17718  1.000 114.11455 ?  26  TYR A CZ  1 
ATOM 150  O OH  . TYR A 1 26  ? 10.16436  -19.22533 -1.42383  1.000 94.67567  ?  26  TYR A OH  1 
ATOM 151  N N   . THR A 1 27  ? 12.51384  -15.02633 -5.78165  1.000 94.20369  ?  27  THR A N   1 
ATOM 152  C CA  . THR A 1 27  ? 13.35599  -15.72311 -6.75419  1.000 91.22254  ?  27  THR A CA  1 
ATOM 153  C C   . THR A 1 27  ? 12.68520  -16.97159 -7.31332  1.000 108.39757 ?  27  THR A C   1 
ATOM 154  O O   . THR A 1 27  ? 12.78606  -17.24265 -8.51574  1.000 130.19704 ?  27  THR A O   1 
ATOM 155  C CB  . THR A 1 27  ? 14.70723  -16.07722 -6.13739  1.000 87.09152  ?  27  THR A CB  1 
ATOM 156  O OG1 . THR A 1 27  ? 14.53056  -17.06423 -5.11791  1.000 91.21770  ?  27  THR A OG1 1 
ATOM 157  C CG2 . THR A 1 27  ? 15.32834  -14.83751 -5.52246  1.000 91.53212  ?  27  THR A CG2 1 
ATOM 158  N N   . SER A 1 28  ? 12.01771  -17.75440 -6.46079  1.000 105.72453 ?  28  SER A N   1 
ATOM 159  C CA  . SER A 1 28  ? 11.26697  -18.91826 -6.92804  1.000 106.63698 ?  28  SER A CA  1 
ATOM 160  C C   . SER A 1 28  ? 12.13408  -19.89994 -7.71606  1.000 122.46840 ?  28  SER A C   1 
ATOM 161  O O   . SER A 1 28  ? 13.00615  -20.55845 -7.13894  1.000 131.77113 ?  28  SER A O   1 
ATOM 162  C CB  . SER A 1 28  ? 10.08036  -18.45639 -7.77610  1.000 98.86131  ?  28  SER A CB  1 
ATOM 163  O OG  . SER A 1 28  ? 9.37495   -19.55949 -8.30533  1.000 116.18810 ?  28  SER A OG  1 
ATOM 164  N N   . ASN A 1 29  ? 11.90252  -20.00576 -9.02415  1.000 116.13565 ?  29  ASN A N   1 
ATOM 165  C CA  . ASN A 1 29  ? 12.61350  -20.94736 -9.89817  1.000 112.75432 ?  29  ASN A CA  1 
ATOM 166  C C   . ASN A 1 29  ? 13.76724  -20.29313 -10.65071 1.000 110.89636 ?  29  ASN A C   1 
ATOM 167  O O   . ASN A 1 29  ? 13.91371  -20.50469 -11.85300 1.000 114.74127 ?  29  ASN A O   1 
ATOM 168  C CB  . ASN A 1 29  ? 11.63818  -21.58958 -10.87784 1.000 109.24363 ?  29  ASN A CB  1 
ATOM 169  C CG  . ASN A 1 29  ? 11.10081  -22.91578 -10.38086 1.000 132.08778 ?  29  ASN A CG  1 
ATOM 170  O OD1 . ASN A 1 29  ? 11.84826  -23.75191 -9.86885  1.000 141.36979 ?  29  ASN A OD1 1 
ATOM 171  N ND2 . ASN A 1 29  ? 9.79274   -23.10523 -10.50283 1.000 131.16966 ?  29  ASN A ND2 1 
ATOM 172  N N   . CYS A 1 30  ? 14.59910  -19.49735 -9.97557  1.000 100.50664 ?  30  CYS A N   1 
ATOM 173  C CA  . CYS A 1 30  ? 15.75869  -18.90325 -10.62855 1.000 91.80878  ?  30  CYS A CA  1 
ATOM 174  C C   . CYS A 1 30  ? 16.78098  -18.47345 -9.58313  1.000 88.97950  ?  30  CYS A C   1 
ATOM 175  O O   . CYS A 1 30  ? 16.42102  -18.11831 -8.45940  1.000 95.15491  ?  30  CYS A O   1 
ATOM 176  C CB  . CYS A 1 30  ? 15.37497  -17.70920 -11.51054 1.000 85.01197  ?  30  CYS A CB  1 
ATOM 177  S SG  . CYS A 1 30  ? 15.07811  -16.19462 -10.60612 1.000 80.01141  ?  30  CYS A SG  1 
ATOM 178  N N   . ILE A 1 31  ? 18.05549  -18.56739 -9.95590  1.000 92.12713  ?  31  ILE A N   1 
ATOM 179  C CA  . ILE A 1 31  ? 19.17643  -18.01442 -9.19913  1.000 82.24286  ?  31  ILE A CA  1 
ATOM 180  C C   . ILE A 1 31  ? 19.62645  -16.73775 -9.90105  1.000 89.30808  ?  31  ILE A C   1 
ATOM 181  O O   . ILE A 1 31  ? 19.86031  -16.74973 -11.11824 1.000 84.29000  ?  31  ILE A O   1 
ATOM 182  C CB  . ILE A 1 31  ? 20.33739  -19.02143 -9.10559  1.000 86.37167  ?  31  ILE A CB  1 
ATOM 183  C CG1 . ILE A 1 31  ? 19.84150  -20.39932 -8.65489  1.000 91.53665  ?  31  ILE A CG1 1 
ATOM 184  C CG2 . ILE A 1 31  ? 21.42226  -18.50253 -8.17520  1.000 82.58754  ?  31  ILE A CG2 1 
ATOM 185  C CD1 . ILE A 1 31  ? 19.05753  -20.39458 -7.36618  1.000 95.58060  ?  31  ILE A CD1 1 
ATOM 186  N N   . MET A 1 32  ? 19.72518  -15.62848 -9.15893  1.000 101.56213 ?  32  MET A N   1 
ATOM 187  C CA  . MET A 1 32  ? 20.01626  -14.32631 -9.76427  1.000 95.07424  ?  32  MET A CA  1 
ATOM 188  C C   . MET A 1 32  ? 21.30393  -13.73438 -9.21076  1.000 96.55322  ?  32  MET A C   1 
ATOM 189  O O   . MET A 1 32  ? 21.40787  -13.49309 -8.00910  1.000 108.68468 ?  32  MET A O   1 
ATOM 190  C CB  . MET A 1 32  ? 18.87781  -13.33268 -9.53819  1.000 68.21962  ?  32  MET A CB  1 
ATOM 191  C CG  . MET A 1 32  ? 17.70615  -13.54321 -10.44329 1.000 95.45917  ?  32  MET A CG  1 
ATOM 192  S SD  . MET A 1 32  ? 16.33975  -12.48100 -9.98398  1.000 102.21810 ?  32  MET A SD  1 
ATOM 193  C CE  . MET A 1 32  ? 17.24588  -11.10659 -9.30697  1.000 75.52178  ?  32  MET A CE  1 
ATOM 194  N N   . ASP A 1 33  ? 22.27271  -13.46966 -10.07873 1.000 100.73370 ?  33  ASP A N   1 
ATOM 195  C CA  . ASP A 1 33  ? 23.43011  -12.65540 -9.71217  1.000 103.52297 ?  33  ASP A CA  1 
ATOM 196  C C   . ASP A 1 33  ? 23.19572  -11.22732 -10.20385 1.000 104.23616 ?  33  ASP A C   1 
ATOM 197  O O   . ASP A 1 33  ? 23.19281  -10.97215 -11.41220 1.000 110.76568 ?  33  ASP A O   1 
ATOM 198  C CB  . ASP A 1 33  ? 24.71779  -13.25033 -10.27541 1.000 106.61014 ?  33  ASP A CB  1 
ATOM 199  C CG  . ASP A 1 33  ? 25.02959  -14.60631 -9.67730  1.000 108.19769 ?  33  ASP A CG  1 
ATOM 200  O OD1 . ASP A 1 33  ? 24.17748  -15.11728 -8.92019  1.000 108.02000 ?  33  ASP A OD1 1 
ATOM 201  O OD2 . ASP A 1 33  ? 26.11857  -15.15442 -9.94888  1.000 110.84381 -1 33  ASP A OD2 1 
ATOM 202  N N   . ILE A 1 34  ? 22.97317  -10.30635 -9.26738  1.000 74.98596  ?  34  ILE A N   1 
ATOM 203  C CA  . ILE A 1 34  ? 22.66878  -8.91111  -9.55735  1.000 82.79525  ?  34  ILE A CA  1 
ATOM 204  C C   . ILE A 1 34  ? 23.93636  -8.08304  -9.46804  1.000 78.45182  ?  34  ILE A C   1 
ATOM 205  O O   . ILE A 1 34  ? 24.61563  -8.08975  -8.43913  1.000 96.17066  ?  34  ILE A O   1 
ATOM 206  C CB  . ILE A 1 34  ? 21.60584  -8.36338  -8.59131  1.000 82.65108  ?  34  ILE A CB  1 
ATOM 207  C CG1 . ILE A 1 34  ? 20.36119  -9.25756  -8.59074  1.000 64.52042  ?  34  ILE A CG1 1 
ATOM 208  C CG2 . ILE A 1 34  ? 21.30928  -6.89379  -8.88884  1.000 73.75875  ?  34  ILE A CG2 1 
ATOM 209  C CD1 . ILE A 1 34  ? 19.17784  -8.61730  -7.91235  1.000 74.95611  ?  34  ILE A CD1 1 
ATOM 210  N N   . TYR A 1 35  ? 24.23679  -7.34559  -10.53027 1.000 82.70120  ?  35  TYR A N   1 
ATOM 211  C CA  . TYR A 1 35  ? 25.36320  -6.42309  -10.57621 1.000 91.77685  ?  35  TYR A CA  1 
ATOM 212  C C   . TYR A 1 35  ? 24.79572  -5.01335  -10.57920 1.000 96.36161  ?  35  TYR A C   1 
ATOM 213  O O   . TYR A 1 35  ? 24.00594  -4.66590  -11.46217 1.000 92.93754  ?  35  TYR A O   1 
ATOM 214  C CB  . TYR A 1 35  ? 26.22480  -6.64504  -11.82099 1.000 93.27587  ?  35  TYR A CB  1 
ATOM 215  C CG  . TYR A 1 35  ? 26.52623  -8.09053  -12.11996 1.000 90.26219  ?  35  TYR A CG  1 
ATOM 216  C CD1 . TYR A 1 35  ? 25.66110  -8.85460  -12.89224 1.000 95.09659  ?  35  TYR A CD1 1 
ATOM 217  C CD2 . TYR A 1 35  ? 27.67537  -8.69313  -11.63059 1.000 92.69877  ?  35  TYR A CD2 1 
ATOM 218  C CE1 . TYR A 1 35  ? 25.93081  -10.18536 -13.16485 1.000 113.96428 ?  35  TYR A CE1 1 
ATOM 219  C CE2 . TYR A 1 35  ? 27.95921  -10.02058 -11.89738 1.000 95.86286  ?  35  TYR A CE2 1 
ATOM 220  C CZ  . TYR A 1 35  ? 27.08603  -10.76501 -12.66556 1.000 123.64164 ?  35  TYR A CZ  1 
ATOM 221  O OH  . TYR A 1 35  ? 27.37340  -12.08993 -12.93083 1.000 116.12357 ?  35  TYR A OH  1 
ATOM 222  N N   . SER A 1 36  ? 25.17785  -4.21564  -9.58720  1.000 145.22398 ?  36  SER A N   1 
ATOM 223  C CA  . SER A 1 36  ? 24.78530  -2.81263  -9.58505  1.000 153.81496 ?  36  SER A CA  1 
ATOM 224  C C   . SER A 1 36  ? 25.73992  -2.02897  -8.69807  1.000 165.95595 ?  36  SER A C   1 
ATOM 225  O O   . SER A 1 36  ? 26.24294  -2.55243  -7.70225  1.000 172.43874 ?  36  SER A O   1 
ATOM 226  C CB  . SER A 1 36  ? 23.33918  -2.64384  -9.10516  1.000 152.59510 ?  36  SER A CB  1 
ATOM 227  O OG  . SER A 1 36  ? 23.04163  -1.28868  -8.82162  1.000 155.55856 ?  36  SER A OG  1 
ATOM 228  N N   . GLU A 1 37  ? 25.93742  -0.75237  -9.04323  1.000 163.20225 ?  37  GLU A N   1 
ATOM 229  C CA  . GLU A 1 37  ? 26.85761  0.13999   -8.32421  1.000 163.62119 ?  37  GLU A CA  1 
ATOM 230  C C   . GLU A 1 37  ? 28.20508  -0.53961  -8.06970  1.000 151.85573 ?  37  GLU A C   1 
ATOM 231  O O   . GLU A 1 37  ? 28.78436  -0.43467  -6.98613  1.000 152.22978 ?  37  GLU A O   1 
ATOM 232  C CB  . GLU A 1 37  ? 26.24111  0.64837   -7.01330  1.000 168.66164 ?  37  GLU A CB  1 
ATOM 233  C CG  . GLU A 1 37  ? 24.95037  1.46628   -7.17105  1.000 169.65438 ?  37  GLU A CG  1 
ATOM 234  C CD  . GLU A 1 37  ? 24.36621  1.92351   -5.83626  1.000 157.14469 ?  37  GLU A CD  1 
ATOM 235  O OE1 . GLU A 1 37  ? 24.84723  1.45861   -4.78077  1.000 155.15408 ?  37  GLU A OE1 1 
ATOM 236  O OE2 . GLU A 1 37  ? 23.43293  2.75702   -5.84267  1.000 153.18419 -1 37  GLU A OE2 1 
ATOM 237  N N   . GLU A 1 38  ? 28.69883  -1.25207  -9.08940  1.000 157.23949 ?  38  GLU A N   1 
ATOM 238  C CA  . GLU A 1 38  ? 29.98660  -1.95512  -9.04662  1.000 144.94819 ?  38  GLU A CA  1 
ATOM 239  C C   . GLU A 1 38  ? 30.04622  -2.97468  -7.90873  1.000 133.68215 ?  38  GLU A C   1 
ATOM 240  O O   . GLU A 1 38  ? 31.09099  -3.18137  -7.28693  1.000 123.29281 ?  38  GLU A O   1 
ATOM 241  C CB  . GLU A 1 38  ? 31.15372  -0.97467  -8.95498  1.000 131.30738 ?  38  GLU A CB  1 
ATOM 242  C CG  . GLU A 1 38  ? 31.33902  -0.11261  -10.18216 1.000 117.17709 ?  38  GLU A CG  1 
ATOM 243  C CD  . GLU A 1 38  ? 32.55783  0.76775   -10.05192 1.000 143.51602 ?  38  GLU A CD  1 
ATOM 244  O OE1 . GLU A 1 38  ? 33.18743  0.74502   -8.97367  1.000 159.67588 ?  38  GLU A OE1 1 
ATOM 245  O OE2 . GLU A 1 38  ? 32.89145  1.48468   -11.01162 1.000 130.25107 -1 38  GLU A OE2 1 
ATOM 246  N N   . GLU A 1 39  ? 28.91438  -3.61830  -7.63684  1.000 129.10316 ?  39  GLU A N   1 
ATOM 247  C CA  . GLU A 1 39  ? 28.81275  -4.63099  -6.59865  1.000 112.48310 ?  39  GLU A CA  1 
ATOM 248  C C   . GLU A 1 39  ? 28.01348  -5.80879  -7.14096  1.000 102.57411 ?  39  GLU A C   1 
ATOM 249  O O   . GLU A 1 39  ? 27.29574  -5.68988  -8.13882  1.000 128.72853 ?  39  GLU A O   1 
ATOM 250  C CB  . GLU A 1 39  ? 28.16469  -4.08475  -5.31479  1.000 131.56145 ?  39  GLU A CB  1 
ATOM 251  C CG  . GLU A 1 39  ? 28.95664  -2.99585  -4.59521  1.000 129.74900 ?  39  GLU A CG  1 
ATOM 252  C CD  . GLU A 1 39  ? 28.15720  -2.33545  -3.48314  1.000 137.59735 ?  39  GLU A CD  1 
ATOM 253  O OE1 . GLU A 1 39  ? 27.75918  -3.04409  -2.52962  1.000 134.42381 ?  39  GLU A OE1 1 
ATOM 254  O OE2 . GLU A 1 39  ? 27.92171  -1.11124  -3.56466  1.000 137.47443 -1 39  GLU A OE2 1 
ATOM 255  N N   . LYS A 1 40  ? 28.11759  -6.94052  -6.44312  1.000 87.47794  ?  40  LYS A N   1 
ATOM 256  C CA  . LYS A 1 40  ? 27.48270  -8.19473  -6.83687  1.000 79.36859  ?  40  LYS A CA  1 
ATOM 257  C C   . LYS A 1 40  ? 26.73211  -8.78337  -5.65076  1.000 68.93955  ?  40  LYS A C   1 
ATOM 258  O O   . LYS A 1 40  ? 27.31502  -9.00120  -4.58592  1.000 88.10066  ?  40  LYS A O   1 
ATOM 259  C CB  . LYS A 1 40  ? 28.51790  -9.19945  -7.35315  1.000 70.49404  ?  40  LYS A CB  1 
ATOM 260  C CG  . LYS A 1 40  ? 27.93559  -10.53195 -7.79641  1.000 72.14985  ?  40  LYS A CG  1 
ATOM 261  C CD  . LYS A 1 40  ? 29.02833  -11.56325 -8.03541  1.000 76.45886  ?  40  LYS A CD  1 
ATOM 262  C CE  . LYS A 1 40  ? 28.46706  -12.85334 -8.61154  1.000 84.22608  ?  40  LYS A CE  1 
ATOM 263  N NZ  . LYS A 1 40  ? 27.99441  -12.65969 -10.01140 1.000 115.59322 ?  40  LYS A NZ  1 
ATOM 264  N N   . ILE A 1 41  ? 25.44523  -9.04475  -5.84622  1.000 85.23582  ?  41  ILE A N   1 
ATOM 265  C CA  . ILE A 1 41  ? 24.57126  -9.66579  -4.85798  1.000 84.52831  ?  41  ILE A CA  1 
ATOM 266  C C   . ILE A 1 41  ? 23.96264  -10.91471 -5.48474  1.000 87.87572  ?  41  ILE A C   1 
ATOM 267  O O   . ILE A 1 41  ? 23.29292  -10.82650 -6.51741  1.000 92.09724  ?  41  ILE A O   1 
ATOM 268  C CB  . ILE A 1 41  ? 23.47073  -8.69402  -4.40148  1.000 80.17560  ?  41  ILE A CB  1 
ATOM 269  C CG1 . ILE A 1 41  ? 24.09798  -7.44906  -3.76958  1.000 92.27349  ?  41  ILE A CG1 1 
ATOM 270  C CG2 . ILE A 1 41  ? 22.49782  -9.37894  -3.46131  1.000 92.29281  ?  41  ILE A CG2 1 
ATOM 271  C CD1 . ILE A 1 41  ? 23.09653  -6.52251  -3.13164  1.000 110.68796 ?  41  ILE A CD1 1 
ATOM 272  N N   . THR A 1 42  ? 24.19494  -12.07477 -4.87981  1.000 90.93720  ?  42  THR A N   1 
ATOM 273  C CA  . THR A 1 42  ? 23.63503  -13.32520 -5.38453  1.000 95.22166  ?  42  THR A CA  1 
ATOM 274  C C   . THR A 1 42  ? 22.40476  -13.71597 -4.56610  1.000 102.96770 ?  42  THR A C   1 
ATOM 275  O O   . THR A 1 42  ? 22.50359  -13.95296 -3.35791  1.000 111.65260 ?  42  THR A O   1 
ATOM 276  C CB  . THR A 1 42  ? 24.67183  -14.44437 -5.36489  1.000 87.28398  ?  42  THR A CB  1 
ATOM 277  O OG1 . THR A 1 42  ? 25.72501  -14.12772 -6.28396  1.000 103.98901 ?  42  THR A OG1 1 
ATOM 278  C CG2 . THR A 1 42  ? 24.02444  -15.75687 -5.77037  1.000 84.70309  ?  42  THR A CG2 1 
ATOM 279  N N   . CYS A 1 43  ? 21.25000  -13.76082 -5.22374  1.000 98.47520  ?  43  CYS A N   1 
ATOM 280  C CA  . CYS A 1 43  ? 20.00563  -14.23537 -4.63834  1.000 91.27971  ?  43  CYS A CA  1 
ATOM 281  C C   . CYS A 1 43  ? 19.81093  -15.70444 -4.98736  1.000 99.61123  ?  43  CYS A C   1 
ATOM 282  O O   . CYS A 1 43  ? 19.80569  -16.07549 -6.17235  1.000 109.64681 ?  43  CYS A O   1 
ATOM 283  C CB  . CYS A 1 43  ? 18.82237  -13.41912 -5.15509  1.000 84.53242  ?  43  CYS A CB  1 
ATOM 284  S SG  . CYS A 1 43  ? 19.10580  -11.63902 -5.14255  1.000 108.44811 ?  43  CYS A SG  1 
ATOM 285  N N   . PHE A 1 44  ? 19.61382  -16.51984 -3.95701  1.000 92.91522  ?  44  PHE A N   1 
ATOM 286  C CA  . PHE A 1 44  ? 19.45780  -17.95966 -4.06701  1.000 96.84295  ?  44  PHE A CA  1 
ATOM 287  C C   . PHE A 1 44  ? 17.98195  -18.27826 -4.28924  1.000 95.10188  ?  44  PHE A C   1 
ATOM 288  O O   . PHE A 1 44  ? 17.12157  -17.39507 -4.25157  1.000 92.55933  ?  44  PHE A O   1 
ATOM 289  C CB  . PHE A 1 44  ? 20.00546  -18.62370 -2.79446  1.000 95.28071  ?  44  PHE A CB  1 
ATOM 290  C CG  . PHE A 1 44  ? 20.17334  -20.12375 -2.87866  1.000 110.66584 ?  44  PHE A CG  1 
ATOM 291  C CD1 . PHE A 1 44  ? 20.98512  -20.70124 -3.84473  1.000 105.87524 ?  44  PHE A CD1 1 
ATOM 292  C CD2 . PHE A 1 44  ? 19.55723  -20.95422 -1.94253  1.000 114.50960 ?  44  PHE A CD2 1 
ATOM 293  C CE1 . PHE A 1 44  ? 21.14786  -22.08551 -3.89884  1.000 121.97386 ?  44  PHE A CE1 1 
ATOM 294  C CE2 . PHE A 1 44  ? 19.71793  -22.33696 -1.98621  1.000 101.21675 ?  44  PHE A CE2 1 
ATOM 295  C CZ  . PHE A 1 44  ? 20.51312  -22.90225 -2.96489  1.000 117.42281 ?  44  PHE A CZ  1 
ATOM 296  N N   . SER A 1 45  ? 17.68522  -19.54976 -4.53824  1.000 91.99407  ?  45  SER A N   1 
ATOM 297  C CA  . SER A 1 45  ? 16.29468  -19.93617 -4.71407  1.000 98.19522  ?  45  SER A CA  1 
ATOM 298  C C   . SER A 1 45  ? 15.55926  -19.84515 -3.37990  1.000 101.63309 ?  45  SER A C   1 
ATOM 299  O O   . SER A 1 45  ? 16.14395  -20.03332 -2.30967  1.000 109.69355 ?  45  SER A O   1 
ATOM 300  C CB  . SER A 1 45  ? 16.19841  -21.34742 -5.29132  1.000 92.09785  ?  45  SER A CB  1 
ATOM 301  O OG  . SER A 1 45  ? 17.00691  -22.25125 -4.56315  1.000 104.53644 ?  45  SER A OG  1 
ATOM 302  N N   . ASN A 1 46  ? 14.26179  -19.54777 -3.45618  1.000 88.82893  ?  46  ASN A N   1 
ATOM 303  C CA  . ASN A 1 46  ? 13.39441  -19.41699 -2.28066  1.000 98.34468  ?  46  ASN A CA  1 
ATOM 304  C C   . ASN A 1 46  ? 13.87036  -18.31184 -1.33464  1.000 92.15852  ?  46  ASN A C   1 
ATOM 305  O O   . ASN A 1 46  ? 14.01702  -18.51274 -0.12767  1.000 101.83729 ?  46  ASN A O   1 
ATOM 306  C CB  . ASN A 1 46  ? 13.27210  -20.75196 -1.54342  1.000 100.10498 ?  46  ASN A CB  1 
ATOM 307  C CG  . ASN A 1 46  ? 12.91642  -21.89347 -2.47286  1.000 120.96627 ?  46  ASN A CG  1 
ATOM 308  O OD1 . ASN A 1 46  ? 13.79308  -22.61265 -2.96015  1.000 111.95100 ?  46  ASN A OD1 1 
ATOM 309  N ND2 . ASN A 1 46  ? 11.62308  -22.06458 -2.72955  1.000 130.12945 ?  46  ASN A ND2 1 
ATOM 310  N N   . ARG A 1 47  ? 14.07720  -17.12319 -1.89508  1.000 84.18927  ?  47  ARG A N   1 
ATOM 311  C CA  . ARG A 1 47  ? 14.48342  -15.93849 -1.15329  1.000 84.01228  ?  47  ARG A CA  1 
ATOM 312  C C   . ARG A 1 47  ? 13.59049  -14.78298 -1.57801  1.000 86.14450  ?  47  ARG A C   1 
ATOM 313  O O   . ARG A 1 47  ? 12.90203  -14.85637 -2.59562  1.000 94.47515  ?  47  ARG A O   1 
ATOM 314  C CB  . ARG A 1 47  ? 15.95694  -15.57124 -1.40697  1.000 96.89584  ?  47  ARG A CB  1 
ATOM 315  C CG  . ARG A 1 47  ? 16.99757  -16.59602 -0.95565  1.000 91.52905  ?  47  ARG A CG  1 
ATOM 316  C CD  . ARG A 1 47  ? 17.08634  -16.68816 0.56342   1.000 100.95103 ?  47  ARG A CD  1 
ATOM 317  N NE  . ARG A 1 47  ? 18.33654  -17.29480 1.01105   1.000 105.93893 ?  47  ARG A NE  1 
ATOM 318  C CZ  . ARG A 1 47  ? 18.61694  -18.59183 0.96357   1.000 109.70986 ?  47  ARG A CZ  1 
ATOM 319  N NH1 . ARG A 1 47  ? 17.72639  -19.48259 0.55617   1.000 106.00758 ?  47  ARG A NH1 1 
ATOM 320  N NH2 . ARG A 1 47  ? 19.81781  -19.00858 1.35195   1.000 114.07103 ?  47  ARG A NH2 1 
ATOM 321  N N   . LEU A 1 48  ? 13.61366  -13.70353 -0.80130  1.000 91.17303  ?  48  LEU A N   1 
ATOM 322  C CA  . LEU A 1 48  ? 12.89845  -12.47730 -1.13754  1.000 72.67674  ?  48  LEU A CA  1 
ATOM 323  C C   . LEU A 1 48  ? 13.89476  -11.35056 -1.34897  1.000 82.19030  ?  48  LEU A C   1 
ATOM 324  O O   . LEU A 1 48  ? 14.78728  -11.14111 -0.52219  1.000 86.79115  ?  48  LEU A O   1 
ATOM 325  C CB  . LEU A 1 48  ? 11.89485  -12.08385 -0.05406  1.000 88.10013  ?  48  LEU A CB  1 
ATOM 326  C CG  . LEU A 1 48  ? 10.41120  -12.33433 -0.33485  1.000 97.46419  ?  48  LEU A CG  1 
ATOM 327  C CD1 . LEU A 1 48  ? 9.56302   -11.65315 0.72415   1.000 86.03735  ?  48  LEU A CD1 1 
ATOM 328  C CD2 . LEU A 1 48  ? 10.01396  -11.86394 -1.72167  1.000 102.16282 ?  48  LEU A CD2 1 
ATOM 329  N N   . VAL A 1 49  ? 13.74201  -10.64045 -2.46069  1.000 81.27616  ?  49  VAL A N   1 
ATOM 330  C CA  . VAL A 1 49  ? 14.60156  -9.53164  -2.84447  1.000 87.99775  ?  49  VAL A CA  1 
ATOM 331  C C   . VAL A 1 49  ? 13.79334  -8.24570  -2.77006  1.000 78.35892  ?  49  VAL A C   1 
ATOM 332  O O   . VAL A 1 49  ? 12.62986  -8.19941  -3.18526  1.000 66.45717  ?  49  VAL A O   1 
ATOM 333  C CB  . VAL A 1 49  ? 15.18190  -9.73386  -4.25845  1.000 78.94451  ?  49  VAL A CB  1 
ATOM 334  C CG1 . VAL A 1 49  ? 16.30901  -8.75114  -4.51510  1.000 80.54595  ?  49  VAL A CG1 1 
ATOM 335  C CG2 . VAL A 1 49  ? 15.66302  -11.16452 -4.43270  1.000 76.88259  ?  49  VAL A CG2 1 
ATOM 336  N N   . PHE A 1 50  ? 14.41677  -7.20485  -2.23692  1.000 82.97326  ?  50  PHE A N   1 
ATOM 337  C CA  . PHE A 1 50  ? 13.82132  -5.88507  -2.09771  1.000 77.01495  ?  50  PHE A CA  1 
ATOM 338  C C   . PHE A 1 50  ? 14.67373  -4.93613  -2.91572  1.000 80.44198  ?  50  PHE A C   1 
ATOM 339  O O   . PHE A 1 50  ? 15.81852  -4.64632  -2.53973  1.000 91.08362  ?  50  PHE A O   1 
ATOM 340  C CB  . PHE A 1 50  ? 13.75399  -5.47271  -0.63321  1.000 68.01677  ?  50  PHE A CB  1 
ATOM 341  C CG  . PHE A 1 50  ? 12.84535  -6.33696  0.17278   1.000 81.13501  ?  50  PHE A CG  1 
ATOM 342  C CD1 . PHE A 1 50  ? 13.23417  -7.61464  0.54449   1.000 77.21980  ?  50  PHE A CD1 1 
ATOM 343  C CD2 . PHE A 1 50  ? 11.59346  -5.88434  0.55061   1.000 88.96913  ?  50  PHE A CD2 1 
ATOM 344  C CE1 . PHE A 1 50  ? 12.39008  -8.42676  1.27729   1.000 88.25295  ?  50  PHE A CE1 1 
ATOM 345  C CE2 . PHE A 1 50  ? 10.74081  -6.69228  1.29053   1.000 85.48643  ?  50  PHE A CE2 1 
ATOM 346  C CZ  . PHE A 1 50  ? 11.14040  -7.96417  1.65344   1.000 89.01604  ?  50  PHE A CZ  1 
ATOM 347  N N   . LEU A 1 51  ? 14.13095  -4.51158  -4.05656  1.000 81.72995  ?  51  LEU A N   1 
ATOM 348  C CA  . LEU A 1 51  ? 14.78756  -3.58888  -4.96800  1.000 80.84483  ?  51  LEU A CA  1 
ATOM 349  C C   . LEU A 1 51  ? 14.10384  -2.23361  -4.84782  1.000 73.25565  ?  51  LEU A C   1 
ATOM 350  O O   . LEU A 1 51  ? 12.88735  -2.11431  -5.05665  1.000 70.14655  ?  51  LEU A O   1 
ATOM 351  C CB  . LEU A 1 51  ? 14.74141  -4.13004  -6.39941  1.000 62.88590  ?  51  LEU A CB  1 
ATOM 352  C CG  . LEU A 1 51  ? 15.30091  -5.56152  -6.44078  1.000 69.10738  ?  51  LEU A CG  1 
ATOM 353  C CD1 . LEU A 1 51  ? 14.32005  -6.58416  -7.00573  1.000 56.00500  ?  51  LEU A CD1 1 
ATOM 354  C CD2 . LEU A 1 51  ? 16.62081  -5.61605  -7.18432  1.000 74.95912  ?  51  LEU A CD2 1 
ATOM 355  N N   . GLU A 1 52  ? 14.88781  -1.22232  -4.49905  1.000 68.59510  ?  52  GLU A N   1 
ATOM 356  C CA  . GLU A 1 52  ? 14.34795  0.10267   -4.28182  1.000 74.47411  ?  52  GLU A CA  1 
ATOM 357  C C   . GLU A 1 52  ? 14.16864  0.82172   -5.60898  1.000 73.96980  ?  52  GLU A C   1 
ATOM 358  O O   . GLU A 1 52  ? 14.81516  0.51120   -6.60978  1.000 90.86551  ?  52  GLU A O   1 
ATOM 359  C CB  . GLU A 1 52  ? 15.25295  0.90185   -3.33644  1.000 90.41964  ?  52  GLU A CB  1 
ATOM 360  C CG  . GLU A 1 52  ? 16.45859  1.57668   -3.98051  1.000 92.27952  ?  52  GLU A CG  1 
ATOM 361  C CD  . GLU A 1 52  ? 17.22292  2.46442   -2.99908  1.000 103.92100 ?  52  GLU A CD  1 
ATOM 362  O OE1 . GLU A 1 52  ? 16.96008  2.36400   -1.78030  1.000 99.91840  ?  52  GLU A OE1 1 
ATOM 363  O OE2 . GLU A 1 52  ? 18.09109  3.25274   -3.44389  1.000 94.54937  -1 52  GLU A OE2 1 
ATOM 364  N N   . ARG A 1 53  ? 13.27648  1.80013   -5.60492  1.000 79.13765  ?  53  ARG A N   1 
ATOM 365  C CA  . ARG A 1 53  ? 12.93353  2.49841   -6.83315  1.000 74.49567  ?  53  ARG A CA  1 
ATOM 366  C C   . ARG A 1 53  ? 14.12590  3.31843   -7.30839  1.000 81.76179  ?  53  ARG A C   1 
ATOM 367  O O   . ARG A 1 53  ? 14.60289  4.20470   -6.59170  1.000 89.73033  ?  53  ARG A O   1 
ATOM 368  C CB  . ARG A 1 53  ? 11.71992  3.39275   -6.59255  1.000 82.83737  ?  53  ARG A CB  1 
ATOM 369  C CG  . ARG A 1 53  ? 11.12849  4.00389   -7.84175  1.000 80.95099  ?  53  ARG A CG  1 
ATOM 370  C CD  . ARG A 1 53  ? 10.06562  5.02845   -7.49429  1.000 84.86033  ?  53  ARG A CD  1 
ATOM 371  N NE  . ARG A 1 53  ? 10.50876  6.37782   -7.82264  1.000 85.78551  ?  53  ARG A NE  1 
ATOM 372  C CZ  . ARG A 1 53  ? 11.25107  7.13190   -7.02612  1.000 89.93870  ?  53  ARG A CZ  1 
ATOM 373  N NH1 . ARG A 1 53  ? 11.66666  6.69304   -5.85061  1.000 99.84711  ?  53  ARG A NH1 1 
ATOM 374  N NH2 . ARG A 1 53  ? 11.58510  8.35555   -7.41814  1.000 92.50349  ?  53  ARG A NH2 1 
ATOM 375  N N   . GLY A 1 54  ? 14.59919  3.03491   -8.51906  1.000 92.52890  ?  54  GLY A N   1 
ATOM 376  C CA  . GLY A 1 54  ? 15.63106  3.83429   -9.16204  1.000 84.01216  ?  54  GLY A CA  1 
ATOM 377  C C   . GLY A 1 54  ? 16.94053  3.12222   -9.42779  1.000 89.96706  ?  54  GLY A C   1 
ATOM 378  O O   . GLY A 1 54  ? 17.75168  3.63889   -10.21390 1.000 83.32515  ?  54  GLY A O   1 
ATOM 379  N N   . VAL A 1 55  ? 17.19133  1.95982   -8.82429  1.000 85.15244  ?  55  VAL A N   1 
ATOM 380  C CA  . VAL A 1 55  ? 18.46774  1.27909   -9.01484  1.000 83.80721  ?  55  VAL A CA  1 
ATOM 381  C C   . VAL A 1 55  ? 18.52545  0.71322   -10.41952 1.000 86.23081  ?  55  VAL A C   1 
ATOM 382  O O   . VAL A 1 55  ? 17.66485  -0.08802  -10.82463 1.000 93.59691  ?  55  VAL A O   1 
ATOM 383  C CB  . VAL A 1 55  ? 18.67993  0.17829   -7.96772  1.000 79.41433  ?  55  VAL A CB  1 
ATOM 384  C CG1 . VAL A 1 55  ? 19.08122  0.77435   -6.63565  1.000 104.42566 ?  55  VAL A CG1 1 
ATOM 385  C CG2 . VAL A 1 55  ? 17.42875  -0.66207  -7.81864  1.000 82.67039  ?  55  VAL A CG2 1 
ATOM 386  N N   . ASN A 1 56  ? 19.51462  1.12849   -11.19135 1.000 82.99841  ?  56  ASN A N   1 
ATOM 387  C CA  . ASN A 1 56  ? 19.78558  0.51452   -12.47944 1.000 88.61494  ?  56  ASN A CA  1 
ATOM 388  C C   . ASN A 1 56  ? 20.68712  -0.68944  -12.24050 1.000 80.49176  ?  56  ASN A C   1 
ATOM 389  O O   . ASN A 1 56  ? 21.82102  -0.54254  -11.77284 1.000 81.87673  ?  56  ASN A O   1 
ATOM 390  C CB  . ASN A 1 56  ? 20.41930  1.50126   -13.44990 1.000 95.11382  ?  56  ASN A CB  1 
ATOM 391  C CG  . ASN A 1 56  ? 20.48538  0.95081   -14.84771 1.000 81.81308  ?  56  ASN A CG  1 
ATOM 392  O OD1 . ASN A 1 56  ? 19.49369  0.96633   -15.57821 1.000 84.31588  ?  56  ASN A OD1 1 
ATOM 393  N ND2 . ASN A 1 56  ? 21.64707  0.43290   -15.22454 1.000 96.85228  ?  56  ASN A ND2 1 
ATOM 394  N N   . ILE A 1 57  ? 20.16677  -1.88134  -12.50192 1.000 75.10559  ?  57  ILE A N   1 
ATOM 395  C CA  . ILE A 1 57  ? 20.89317  -3.10371  -12.20818 1.000 82.89063  ?  57  ILE A CA  1 
ATOM 396  C C   . ILE A 1 57  ? 21.01933  -3.91915  -13.48453 1.000 72.12746  ?  57  ILE A C   1 
ATOM 397  O O   . ILE A 1 57  ? 20.33852  -3.67068  -14.48028 1.000 87.26761  ?  57  ILE A O   1 
ATOM 398  C CB  . ILE A 1 57  ? 20.20351  -3.92137  -11.10696 1.000 78.11355  ?  57  ILE A CB  1 
ATOM 399  C CG1 . ILE A 1 57  ? 18.87629  -4.46426  -11.61114 1.000 80.18031  ?  57  ILE A CG1 1 
ATOM 400  C CG2 . ILE A 1 57  ? 19.92238  -3.03931  -9.91336  1.000 91.13554  ?  57  ILE A CG2 1 
ATOM 401  C CD1 . ILE A 1 57  ? 18.36847  -5.60841  -10.79189 1.000 74.98450  ?  57  ILE A CD1 1 
ATOM 402  N N   . SER A 1 58  ? 21.92990  -4.88537  -13.44817 1.000 68.77279  ?  58  SER A N   1 
ATOM 403  C CA  . SER A 1 58  ? 22.06504  -5.91926  -14.46346 1.000 71.87299  ?  58  SER A CA  1 
ATOM 404  C C   . SER A 1 58  ? 21.91957  -7.25837  -13.76661 1.000 66.80285  ?  58  SER A C   1 
ATOM 405  O O   . SER A 1 58  ? 22.27173  -7.38514  -12.59630 1.000 85.00970  ?  58  SER A O   1 
ATOM 406  C CB  . SER A 1 58  ? 23.40825  -5.83918  -15.18480 1.000 73.83377  ?  58  SER A CB  1 
ATOM 407  O OG  . SER A 1 58  ? 23.50014  -4.64401  -15.93837 1.000 93.96399  ?  58  SER A OG  1 
ATOM 408  N N   . VAL A 1 59  ? 21.33886  -8.24179  -14.43797 1.000 70.32854  ?  59  VAL A N   1 
ATOM 409  C CA  . VAL A 1 59  ? 21.06373  -9.51229  -13.78119 1.000 67.87369  ?  59  VAL A CA  1 
ATOM 410  C C   . VAL A 1 59  ? 21.55112  -10.65940 -14.65194 1.000 73.63240  ?  59  VAL A C   1 
ATOM 411  O O   . VAL A 1 59  ? 21.39945  -10.63607 -15.88002 1.000 72.15240  ?  59  VAL A O   1 
ATOM 412  C CB  . VAL A 1 59  ? 19.56508  -9.67371  -13.46645 1.000 70.81302  ?  59  VAL A CB  1 
ATOM 413  C CG1 . VAL A 1 59  ? 19.35046  -10.86831 -12.55529 1.000 90.18181  ?  59  VAL A CG1 1 
ATOM 414  C CG2 . VAL A 1 59  ? 19.02533  -8.41879  -12.83650 1.000 78.54367  ?  59  VAL A CG2 1 
ATOM 415  N N   . ARG A 1 60  ? 22.13704  -11.66644 -14.00953 1.000 73.91878  ?  60  ARG A N   1 
ATOM 416  C CA  . ARG A 1 60  ? 22.45649  -12.94095 -14.64296 1.000 83.65417  ?  60  ARG A CA  1 
ATOM 417  C C   . ARG A 1 60  ? 21.60291  -14.00459 -13.95760 1.000 84.70565  ?  60  ARG A C   1 
ATOM 418  O O   . ARG A 1 60  ? 21.84911  -14.36271 -12.80000 1.000 80.03596  ?  60  ARG A O   1 
ATOM 419  C CB  . ARG A 1 60  ? 23.96242  -13.20656 -14.56591 1.000 91.36814  ?  60  ARG A CB  1 
ATOM 420  C CG  . ARG A 1 60  ? 24.49502  -14.43805 -15.30440 1.000 88.64069  ?  60  ARG A CG  1 
ATOM 421  C CD  . ARG A 1 60  ? 26.02932  -14.32680 -15.44670 1.000 117.30417 ?  60  ARG A CD  1 
ATOM 422  N NE  . ARG A 1 60  ? 26.78129  -14.29981 -14.19541 1.000 127.25949 ?  60  ARG A NE  1 
ATOM 423  C CZ  . ARG A 1 60  ? 27.39879  -15.34481 -13.66034 1.000 133.42775 ?  60  ARG A CZ  1 
ATOM 424  N NH1 . ARG A 1 60  ? 27.28727  -16.55654 -14.18192 1.000 137.51329 ?  60  ARG A NH1 1 
ATOM 425  N NH2 . ARG A 1 60  ? 28.11961  -15.17523 -12.55399 1.000 130.20552 ?  60  ARG A NH2 1 
ATOM 426  N N   . MET A 1 61  ? 20.57989  -14.47265 -14.67132 1.000 74.70848  ?  61  MET A N   1 
ATOM 427  C CA  . MET A 1 61  ? 19.58205  -15.39820 -14.15695 1.000 71.82182  ?  61  MET A CA  1 
ATOM 428  C C   . MET A 1 61  ? 19.79205  -16.79570 -14.71483 1.000 71.31320  ?  61  MET A C   1 
ATOM 429  O O   . MET A 1 61  ? 20.07387  -16.96646 -15.90647 1.000 88.85666  ?  61  MET A O   1 
ATOM 430  C CB  . MET A 1 61  ? 18.17424  -14.94675 -14.53235 1.000 82.67154  ?  61  MET A CB  1 
ATOM 431  C CG  . MET A 1 61  ? 17.90461  -13.47889 -14.35308 1.000 91.25771  ?  61  MET A CG  1 
ATOM 432  S SD  . MET A 1 61  ? 16.14998  -13.16601 -14.58640 1.000 86.22304  ?  61  MET A SD  1 
ATOM 433  C CE  . MET A 1 61  ? 15.48388  -14.48996 -13.59704 1.000 80.17222  ?  61  MET A CE  1 
ATOM 434  N N   . GLN A 1 62  ? 19.61601  -17.78605 -13.84649 1.000 71.75913  ?  62  GLN A N   1 
ATOM 435  C CA  . GLN A 1 62  ? 19.67053  -19.20012 -14.20140 1.000 73.31929  ?  62  GLN A CA  1 
ATOM 436  C C   . GLN A 1 62  ? 18.38183  -19.85335 -13.71627 1.000 85.33236  ?  62  GLN A C   1 
ATOM 437  O O   . GLN A 1 62  ? 18.16066  -19.95418 -12.50644 1.000 100.76391 ?  62  GLN A O   1 
ATOM 438  C CB  . GLN A 1 62  ? 20.89077  -19.86421 -13.57268 1.000 84.43984  ?  62  GLN A CB  1 
ATOM 439  C CG  . GLN A 1 62  ? 20.89518  -21.37514 -13.65543 1.000 103.38632 ?  62  GLN A CG  1 
ATOM 440  C CD  . GLN A 1 62  ? 21.84348  -21.99813 -12.64875 1.000 104.71884 ?  62  GLN A CD  1 
ATOM 441  O OE1 . GLN A 1 62  ? 22.99465  -21.57689 -12.52191 1.000 90.33898  ?  62  GLN A OE1 1 
ATOM 442  N NE2 . GLN A 1 62  ? 21.35628  -22.99147 -11.90998 1.000 109.35737 ?  62  GLN A NE2 1 
ATOM 443  N N   . LYS A 1 63  ? 17.53039  -20.29148 -14.64282 1.000 94.86272  ?  63  LYS A N   1 
ATOM 444  C CA  . LYS A 1 63  ? 16.26319  -20.90853 -14.26539 1.000 95.02796  ?  63  LYS A CA  1 
ATOM 445  C C   . LYS A 1 63  ? 16.48095  -22.33280 -13.76237 1.000 106.15174 ?  63  LYS A C   1 
ATOM 446  O O   . LYS A 1 63  ? 17.25736  -23.09922 -14.33845 1.000 110.75285 ?  63  LYS A O   1 
ATOM 447  C CB  . LYS A 1 63  ? 15.28324  -20.91758 -15.44291 1.000 96.24107  ?  63  LYS A CB  1 
ATOM 448  C CG  . LYS A 1 63  ? 14.35717  -19.70425 -15.48365 1.000 98.07738  ?  63  LYS A CG  1 
ATOM 449  C CD  . LYS A 1 63  ? 13.21144  -19.86072 -16.47939 1.000 92.22161  ?  63  LYS A CD  1 
ATOM 450  C CE  . LYS A 1 63  ? 13.67748  -20.22086 -17.87026 1.000 104.43322 ?  63  LYS A CE  1 
ATOM 451  N NZ  . LYS A 1 63  ? 12.49345  -20.47961 -18.73422 1.000 89.77377  ?  63  LYS A NZ  1 
ATOM 452  N N   . GLN A 1 64  ? 15.78295  -22.68816 -12.67938 1.000 108.88937 ?  64  GLN A N   1 
ATOM 453  C CA  . GLN A 1 64  ? 15.82576  -24.06336 -12.18604 1.000 121.60793 ?  64  GLN A CA  1 
ATOM 454  C C   . GLN A 1 64  ? 14.92800  -24.98031 -13.01273 1.000 130.67469 ?  64  GLN A C   1 
ATOM 455  O O   . GLN A 1 64  ? 15.38323  -25.99904 -13.54488 1.000 134.52805 ?  64  GLN A O   1 
ATOM 456  C CB  . GLN A 1 64  ? 15.43036  -24.11997 -10.70362 1.000 121.24250 ?  64  GLN A CB  1 
ATOM 457  C CG  . GLN A 1 64  ? 16.06333  -23.05104 -9.81475  1.000 117.35655 ?  64  GLN A CG  1 
ATOM 458  C CD  . GLN A 1 64  ? 15.77776  -23.27584 -8.33058  1.000 127.64776 ?  64  GLN A CD  1 
ATOM 459  O OE1 . GLN A 1 64  ? 14.73361  -22.87415 -7.81849  1.000 130.69636 ?  64  GLN A OE1 1 
ATOM 460  N NE2 . GLN A 1 64  ? 16.71442  -23.91281 -7.63463  1.000 124.11251 ?  64  GLN A NE2 1 
ATOM 461  N N   . ILE A 1 65  ? 13.64752  -24.63826 -13.12471 1.000 131.12170 ?  65  ILE A N   1 
ATOM 462  C CA  . ILE A 1 65  ? 12.71070  -25.35584 -13.98084 1.000 117.22040 ?  65  ILE A CA  1 
ATOM 463  C C   . ILE A 1 65  ? 12.46627  -24.51570 -15.22403 1.000 123.82238 ?  65  ILE A C   1 
ATOM 464  O O   . ILE A 1 65  ? 12.13205  -23.32732 -15.12589 1.000 119.92511 ?  65  ILE A O   1 
ATOM 465  C CB  . ILE A 1 65  ? 11.39282  -25.65170 -13.24675 1.000 127.52490 ?  65  ILE A CB  1 
ATOM 466  C CG1 . ILE A 1 65  ? 11.65232  -26.54131 -12.03004 1.000 134.61115 ?  65  ILE A CG1 1 
ATOM 467  C CG2 . ILE A 1 65  ? 10.39235  -26.30239 -14.19131 1.000 124.20168 ?  65  ILE A CG2 1 
ATOM 468  C CD1 . ILE A 1 65  ? 12.39101  -27.82000 -12.35980 1.000 125.24720 ?  65  ILE A CD1 1 
ATOM 469  N N   . LEU A 1 66  ? 12.63658  -25.12834 -16.39525 1.000 128.73935 ?  66  LEU A N   1 
ATOM 470  C CA  . LEU A 1 66  ? 12.59076  -24.36431 -17.63603 1.000 130.30182 ?  66  LEU A CA  1 
ATOM 471  C C   . LEU A 1 66  ? 11.15958  -24.07867 -18.07609 1.000 139.82748 ?  66  LEU A C   1 
ATOM 472  O O   . LEU A 1 66  ? 10.88022  -22.99881 -18.60943 1.000 138.37579 ?  66  LEU A O   1 
ATOM 473  C CB  . LEU A 1 66  ? 13.35577  -25.09812 -18.73351 1.000 127.81680 ?  66  LEU A CB  1 
ATOM 474  C CG  . LEU A 1 66  ? 14.87443  -24.98371 -18.61326 1.000 124.04535 ?  66  LEU A CG  1 
ATOM 475  C CD1 . LEU A 1 66  ? 15.43377  -26.12862 -17.78245 1.000 123.76530 ?  66  LEU A CD1 1 
ATOM 476  C CD2 . LEU A 1 66  ? 15.51781  -24.93150 -19.98789 1.000 140.19758 ?  66  LEU A CD2 1 
ATOM 477  N N   . SER A 1 67  ? 10.24960  -25.04064 -17.88933 1.000 153.00329 ?  67  SER A N   1 
ATOM 478  C CA  . SER A 1 67  ? 8.87842   -24.86807 -18.36362 1.000 160.08170 ?  67  SER A CA  1 
ATOM 479  C C   . SER A 1 67  ? 8.18082   -23.69364 -17.68456 1.000 153.58503 ?  67  SER A C   1 
ATOM 480  O O   . SER A 1 67  ? 7.28828   -23.07700 -18.27954 1.000 154.99665 ?  67  SER A O   1 
ATOM 481  C CB  . SER A 1 67  ? 8.07468   -26.15384 -18.14887 1.000 158.03443 ?  67  SER A CB  1 
ATOM 482  O OG  . SER A 1 67  ? 7.67534   -26.30202 -16.79638 1.000 150.64345 ?  67  SER A OG  1 
ATOM 483  N N   . GLU A 1 68  ? 8.55123   -23.37953 -16.44430 1.000 134.88677 ?  68  GLU A N   1 
ATOM 484  C CA  . GLU A 1 68  ? 7.87228   -22.32759 -15.70438 1.000 139.20515 ?  68  GLU A CA  1 
ATOM 485  C C   . GLU A 1 68  ? 8.58134   -20.97897 -15.85492 1.000 124.17056 ?  68  GLU A C   1 
ATOM 486  O O   . GLU A 1 68  ? 9.64197   -20.85065 -16.47226 1.000 118.37973 ?  68  GLU A O   1 
ATOM 487  C CB  . GLU A 1 68  ? 7.74543   -22.69247 -14.22508 1.000 128.70596 ?  68  GLU A CB  1 
ATOM 488  C CG  . GLU A 1 68  ? 6.84749   -23.87604 -13.94056 1.000 127.69217 ?  68  GLU A CG  1 
ATOM 489  C CD  . GLU A 1 68  ? 6.63075   -24.09071 -12.45603 1.000 136.78083 ?  68  GLU A CD  1 
ATOM 490  O OE1 . GLU A 1 68  ? 7.28147   -23.39358 -11.64518 1.000 126.10910 ?  68  GLU A OE1 1 
ATOM 491  O OE2 . GLU A 1 68  ? 5.81133   -24.96394 -12.10172 1.000 152.42120 -1 68  GLU A OE2 1 
ATOM 492  N N   . LYS A 1 69  ? 7.97148   -19.96197 -15.25537 1.000 113.79782 ?  69  LYS A N   1 
ATOM 493  C CA  . LYS A 1 69  ? 8.51395   -18.61989 -15.20947 1.000 90.61241  ?  69  LYS A CA  1 
ATOM 494  C C   . LYS A 1 69  ? 9.72027   -18.57030 -14.27231 1.000 96.12835  ?  69  LYS A C   1 
ATOM 495  O O   . LYS A 1 69  ? 9.92949   -19.47967 -13.46508 1.000 109.18787 ?  69  LYS A O   1 
ATOM 496  C CB  . LYS A 1 69  ? 7.42517   -17.66266 -14.73846 1.000 87.55007  ?  69  LYS A CB  1 
ATOM 497  C CG  . LYS A 1 69  ? 6.97365   -17.96044 -13.31910 1.000 87.87756  ?  69  LYS A CG  1 
ATOM 498  C CD  . LYS A 1 69  ? 5.63066   -17.33715 -12.99707 1.000 84.23127  ?  69  LYS A CD  1 
ATOM 499  C CE  . LYS A 1 69  ? 4.55422   -18.41575 -12.98291 1.000 96.78377  ?  69  LYS A CE  1 
ATOM 500  N NZ  . LYS A 1 69  ? 3.20254   -17.88285 -12.67533 1.000 105.93557 ?  69  LYS A NZ  1 
ATOM 501  N N   . PRO A 1 70  ? 10.55548  -17.53097 -14.38360 1.000 95.27027  ?  70  PRO A N   1 
ATOM 502  C CA  . PRO A 1 70  ? 11.71546  -17.42867 -13.48421 1.000 96.62920  ?  70  PRO A CA  1 
ATOM 503  C C   . PRO A 1 70  ? 11.35885  -17.10059 -12.04196 1.000 97.38211  ?  70  PRO A C   1 
ATOM 504  O O   . PRO A 1 70  ? 11.66080  -17.87630 -11.12960 1.000 99.19996  ?  70  PRO A O   1 
ATOM 505  C CB  . PRO A 1 70  ? 12.53914  -16.29367 -14.10617 1.000 78.79899  ?  70  PRO A CB  1 
ATOM 506  C CG  . PRO A 1 70  ? 12.07246  -16.21007 -15.52180 1.000 95.10372  ?  70  PRO A CG  1 
ATOM 507  C CD  . PRO A 1 70  ? 10.61390  -16.52976 -15.46035 1.000 81.77428  ?  70  PRO A CD  1 
ATOM 508  N N   . TYR A 1 71  ? 10.68302  -15.96922 -11.83542 1.000 93.50846  ?  71  TYR A N   1 
ATOM 509  C CA  . TYR A 1 71  ? 10.48334  -15.39144 -10.51313 1.000 84.59834  ?  71  TYR A CA  1 
ATOM 510  C C   . TYR A 1 71  ? 9.04720   -14.90101 -10.38216 1.000 93.23558  ?  71  TYR A C   1 
ATOM 511  O O   . TYR A 1 71  ? 8.25775   -14.97375 -11.32857 1.000 97.02460  ?  71  TYR A O   1 
ATOM 512  C CB  . TYR A 1 71  ? 11.47158  -14.24474 -10.25653 1.000 74.22852  ?  71  TYR A CB  1 
ATOM 513  C CG  . TYR A 1 71  ? 11.48819  -13.15917 -11.32457 1.000 83.08741  ?  71  TYR A CG  1 
ATOM 514  C CD1 . TYR A 1 71  ? 10.47042  -12.21393 -11.40854 1.000 78.57027  ?  71  TYR A CD1 1 
ATOM 515  C CD2 . TYR A 1 71  ? 12.54880  -13.05174 -12.21957 1.000 86.98159  ?  71  TYR A CD2 1 
ATOM 516  C CE1 . TYR A 1 71  ? 10.48792  -11.21779 -12.37917 1.000 90.42321  ?  71  TYR A CE1 1 
ATOM 517  C CE2 . TYR A 1 71  ? 12.57919  -12.05326 -13.18892 1.000 75.43269  ?  71  TYR A CE2 1 
ATOM 518  C CZ  . TYR A 1 71  ? 11.54717  -11.14015 -13.26531 1.000 86.31968  ?  71  TYR A CZ  1 
ATOM 519  O OH  . TYR A 1 71  ? 11.56937  -10.14986 -14.22901 1.000 81.19991  ?  71  TYR A OH  1 
ATOM 520  N N   . VAL A 1 72  ? 8.70917   -14.40089 -9.19030  1.000 90.57822  ?  72  VAL A N   1 
ATOM 521  C CA  . VAL A 1 72  ? 7.39420   -13.82426 -8.90095  1.000 78.81227  ?  72  VAL A CA  1 
ATOM 522  C C   . VAL A 1 72  ? 7.58959   -12.39402 -8.40557  1.000 76.77137  ?  72  VAL A C   1 
ATOM 523  O O   . VAL A 1 72  ? 8.21210   -12.18123 -7.36398  1.000 90.18419  ?  72  VAL A O   1 
ATOM 524  C CB  . VAL A 1 72  ? 6.63368   -14.65853 -7.85701  1.000 93.23746  ?  72  VAL A CB  1 
ATOM 525  C CG1 . VAL A 1 72  ? 5.21575   -14.14097 -7.68813  1.000 88.29601  ?  72  VAL A CG1 1 
ATOM 526  C CG2 . VAL A 1 72  ? 6.64231   -16.13761 -8.23920  1.000 84.98189  ?  72  VAL A CG2 1 
ATOM 527  N N   . ALA A 1 73  ? 7.04538   -11.41472 -9.12144  1.000 71.25492  ?  73  ALA A N   1 
ATOM 528  C CA  . ALA A 1 73  ? 7.33324   -10.01922 -8.80787  1.000 75.52548  ?  73  ALA A CA  1 
ATOM 529  C C   . ALA A 1 73  ? 6.12164   -9.31898  -8.20561  1.000 84.42644  ?  73  ALA A C   1 
ATOM 530  O O   . ALA A 1 73  ? 4.97524   -9.67284  -8.49534  1.000 85.05538  ?  73  ALA A O   1 
ATOM 531  C CB  . ALA A 1 73  ? 7.79150   -9.25558  -10.05285 1.000 76.57982  ?  73  ALA A CB  1 
ATOM 532  N N   . PHE A 1 74  ? 6.39253   -8.30339  -7.37529  1.000 82.27882  ?  74  PHE A N   1 
ATOM 533  C CA  . PHE A 1 74  ? 5.36255   -7.45301  -6.77085  1.000 83.49981  ?  74  PHE A CA  1 
ATOM 534  C C   . PHE A 1 74  ? 5.85545   -6.01438  -6.84558  1.000 75.29853  ?  74  PHE A C   1 
ATOM 535  O O   . PHE A 1 74  ? 6.79583   -5.64947  -6.13804  1.000 75.06099  ?  74  PHE A O   1 
ATOM 536  C CB  . PHE A 1 74  ? 5.08376   -7.83634  -5.31379  1.000 76.39027  ?  74  PHE A CB  1 
ATOM 537  C CG  . PHE A 1 74  ? 4.72714   -9.27904  -5.11469  1.000 80.09454  ?  74  PHE A CG  1 
ATOM 538  C CD1 . PHE A 1 74  ? 3.41629   -9.69709  -5.21316  1.000 82.01497  ?  74  PHE A CD1 1 
ATOM 539  C CD2 . PHE A 1 74  ? 5.70504   -10.21687 -4.82063  1.000 88.60683  ?  74  PHE A CD2 1 
ATOM 540  C CE1 . PHE A 1 74  ? 3.08715   -11.01677 -5.03608  1.000 89.80240  ?  74  PHE A CE1 1 
ATOM 541  C CE2 . PHE A 1 74  ? 5.37966   -11.54605 -4.63814  1.000 84.57537  ?  74  PHE A CE2 1 
ATOM 542  C CZ  . PHE A 1 74  ? 4.06778   -11.94628 -4.74454  1.000 99.32120  ?  74  PHE A CZ  1 
ATOM 543  N N   . ARG A 1 75  ? 5.23304   -5.19991  -7.69088  1.000 77.64533  ?  75  ARG A N   1 
ATOM 544  C CA  . ARG A 1 75  ? 5.66213   -3.82633  -7.91021  1.000 78.79255  ?  75  ARG A CA  1 
ATOM 545  C C   . ARG A 1 75  ? 4.65503   -2.87253  -7.26988  1.000 84.25837  ?  75  ARG A C   1 
ATOM 546  O O   . ARG A 1 75  ? 3.44299   -3.10627  -7.33118  1.000 88.22023  ?  75  ARG A O   1 
ATOM 547  C CB  . ARG A 1 75  ? 5.80413   -3.55349  -9.41710  1.000 79.36473  ?  75  ARG A CB  1 
ATOM 548  C CG  . ARG A 1 75  ? 6.73459   -4.54416  -10.15784 1.000 75.25532  ?  75  ARG A CG  1 
ATOM 549  C CD  . ARG A 1 75  ? 6.54181   -4.51772  -11.68575 1.000 75.86213  ?  75  ARG A CD  1 
ATOM 550  N NE  . ARG A 1 75  ? 6.90717   -3.21794  -12.24225 1.000 111.69285 ?  75  ARG A NE  1 
ATOM 551  C CZ  . ARG A 1 75  ? 6.37126   -2.66335  -13.32440 1.000 112.36973 ?  75  ARG A CZ  1 
ATOM 552  N NH1 . ARG A 1 75  ? 5.36065   -3.22935  -13.96771 1.000 102.46322 ?  75  ARG A NH1 1 
ATOM 553  N NH2 . ARG A 1 75  ? 6.84290   -1.49343  -13.75468 1.000 89.21652  ?  75  ARG A NH2 1 
ATOM 554  N N   . LEU A 1 76  ? 5.14414   -1.77845  -6.68665  1.000 73.04246  ?  76  LEU A N   1 
ATOM 555  C CA  . LEU A 1 76  ? 4.28802   -0.84651  -5.95877  1.000 78.58335  ?  76  LEU A CA  1 
ATOM 556  C C   . LEU A 1 76  ? 4.19372   0.47174   -6.70812  1.000 77.41566  ?  76  LEU A C   1 
ATOM 557  O O   . LEU A 1 76  ? 5.20930   1.13634   -6.93344  1.000 87.68531  ?  76  LEU A O   1 
ATOM 558  C CB  . LEU A 1 76  ? 4.80542   -0.59675  -4.54262  1.000 65.98892  ?  76  LEU A CB  1 
ATOM 559  C CG  . LEU A 1 76  ? 4.28364   -1.50122  -3.42784  1.000 87.91945  ?  76  LEU A CG  1 
ATOM 560  C CD1 . LEU A 1 76  ? 4.86174   -2.90537  -3.54191  1.000 85.06063  ?  76  LEU A CD1 1 
ATOM 561  C CD2 . LEU A 1 76  ? 4.62719   -0.90393  -2.07712  1.000 103.91252 ?  76  LEU A CD2 1 
ATOM 562  N N   . ASN A 1 77  ? 2.97115   0.86353   -7.05133  1.000 77.28421  ?  77  ASN A N   1 
ATOM 563  C CA  . ASN A 1 77  ? 2.73511   2.15380   -7.67343  1.000 93.27195  ?  77  ASN A CA  1 
ATOM 564  C C   . ASN A 1 77  ? 2.97438   3.27914   -6.66667  1.000 95.31583  ?  77  ASN A C   1 
ATOM 565  O O   . ASN A 1 77  ? 3.22639   3.05260   -5.47956  1.000 90.76830  ?  77  ASN A O   1 
ATOM 566  C CB  . ASN A 1 77  ? 1.31440   2.23508   -8.23493  1.000 92.67433  ?  77  ASN A CB  1 
ATOM 567  C CG  . ASN A 1 77  ? 0.25188   2.09517   -7.16058  1.000 111.46679 ?  77  ASN A CG  1 
ATOM 568  O OD1 . ASN A 1 77  ? -0.10299  3.06574   -6.49106  1.000 117.91732 ?  77  ASN A OD1 1 
ATOM 569  N ND2 . ASN A 1 77  ? -0.27551  0.88672   -7.00298  1.000 123.23971 ?  77  ASN A ND2 1 
ATOM 570  N N   . GLY A 1 78  ? 2.92815   4.51092   -7.17774  1.000 108.11453 ?  78  GLY A N   1 
ATOM 571  C CA  . GLY A 1 78  ? 3.15481   5.67706   -6.33529  1.000 105.19142 ?  78  GLY A CA  1 
ATOM 572  C C   . GLY A 1 78  ? 2.23061   5.74762   -5.13513  1.000 107.45957 ?  78  GLY A C   1 
ATOM 573  O O   . GLY A 1 78  ? 2.67086   6.01047   -4.01432  1.000 108.05206 ?  78  GLY A O   1 
ATOM 574  N N   . ASP A 1 79  ? 0.92765   5.54690   -5.35831  1.000 104.69975 ?  79  ASP A N   1 
ATOM 575  C CA  . ASP A 1 79  ? -0.04056  5.63508   -4.26669  1.000 116.24177 ?  79  ASP A CA  1 
ATOM 576  C C   . ASP A 1 79  ? 0.25509   4.61464   -3.17376  1.000 110.73735 ?  79  ASP A C   1 
ATOM 577  O O   . ASP A 1 79  ? 0.34965   4.96197   -1.98760  1.000 105.70944 ?  79  ASP A O   1 
ATOM 578  C CB  . ASP A 1 79  ? -1.45638  5.42262   -4.80628  1.000 122.02453 ?  79  ASP A CB  1 
ATOM 579  C CG  . ASP A 1 79  ? -2.14958  6.71789   -5.16293  1.000 127.78073 ?  79  ASP A CG  1 
ATOM 580  O OD1 . ASP A 1 79  ? -2.07873  7.67753   -4.36336  1.000 125.07320 ?  79  ASP A OD1 1 
ATOM 581  O OD2 . ASP A 1 79  ? -2.77639  6.76778   -6.24261  1.000 138.17888 -1 79  ASP A OD2 1 
ATOM 582  N N   . MET A 1 80  ? 0.37433   3.34196   -3.55895  1.000 104.74034 ?  80  MET A N   1 
ATOM 583  C CA  . MET A 1 80  ? 0.66723   2.28644   -2.59640  1.000 105.14499 ?  80  MET A CA  1 
ATOM 584  C C   . MET A 1 80  ? 1.98939   2.53100   -1.88203  1.000 104.04997 ?  80  MET A C   1 
ATOM 585  O O   . MET A 1 80  ? 2.09193   2.34238   -0.66487  1.000 106.33059 ?  80  MET A O   1 
ATOM 586  C CB  . MET A 1 80  ? 0.67291   0.92968   -3.29234  1.000 100.12093 ?  80  MET A CB  1 
ATOM 587  C CG  . MET A 1 80  ? 0.92243   -0.21681  -2.34313  1.000 106.69320 ?  80  MET A CG  1 
ATOM 588  S SD  . MET A 1 80  ? 0.35672   -1.76965  -3.03628  1.000 142.53006 ?  80  MET A SD  1 
ATOM 589  C CE  . MET A 1 80  ? -1.36164  -1.36292  -3.35266  1.000 121.14609 ?  80  MET A CE  1 
ATOM 590  N N   . LEU A 1 81  ? 3.02925   2.89964   -2.63315  1.000 114.55015 ?  81  LEU A N   1 
ATOM 591  C CA  . LEU A 1 81  ? 4.32293   3.17633   -2.01641  1.000 111.68063 ?  81  LEU A CA  1 
ATOM 592  C C   . LEU A 1 81  ? 4.21899   4.28810   -0.98055  1.000 114.73872 ?  81  LEU A C   1 
ATOM 593  O O   . LEU A 1 81  ? 4.76462   4.17108   0.12053   1.000 117.70609 ?  81  LEU A O   1 
ATOM 594  C CB  . LEU A 1 81  ? 5.35322   3.53950   -3.08155  1.000 109.06645 ?  81  LEU A CB  1 
ATOM 595  C CG  . LEU A 1 81  ? 6.75220   3.75753   -2.50676  1.000 105.24578 ?  81  LEU A CG  1 
ATOM 596  C CD1 . LEU A 1 81  ? 7.23093   2.52387   -1.74709  1.000 103.77608 ?  81  LEU A CD1 1 
ATOM 597  C CD2 . LEU A 1 81  ? 7.72261   4.14157   -3.60580  1.000 102.56881 ?  81  LEU A CD2 1 
ATOM 598  N N   . ARG A 1 82  ? 3.53156   5.38253   -1.32210  1.000 100.83428 ?  82  ARG A N   1 
ATOM 599  C CA  . ARG A 1 82  ? 3.38299   6.49720   -0.38960  1.000 98.73537  ?  82  ARG A CA  1 
ATOM 600  C C   . ARG A 1 82  ? 2.63277   6.07342   0.86678   1.000 102.25382 ?  82  ARG A C   1 
ATOM 601  O O   . ARG A 1 82  ? 3.02089   6.43448   1.98616   1.000 80.71433  ?  82  ARG A O   1 
ATOM 602  C CB  . ARG A 1 82  ? 2.66899   7.66136   -1.07533  1.000 109.56779 ?  82  ARG A CB  1 
ATOM 603  C CG  . ARG A 1 82  ? 3.59955   8.74299   -1.61528  1.000 114.61739 ?  82  ARG A CG  1 
ATOM 604  C CD  . ARG A 1 82  ? 3.30861   9.00863   -3.08293  1.000 117.87196 ?  82  ARG A CD  1 
ATOM 605  N NE  . ARG A 1 82  ? 1.91119   9.37198   -3.29133  1.000 141.53859 ?  82  ARG A NE  1 
ATOM 606  C CZ  . ARG A 1 82  ? 1.32383   9.45512   -4.47778  1.000 135.66098 ?  82  ARG A CZ  1 
ATOM 607  N NH1 . ARG A 1 82  ? 1.98856   9.21507   -5.59722  1.000 113.65002 ?  82  ARG A NH1 1 
ATOM 608  N NH2 . ARG A 1 82  ? 0.03570   9.78389   -4.54207  1.000 147.01048 ?  82  ARG A NH2 1 
ATOM 609  N N   . HIS A 1 83  ? 1.52704   5.33897   0.69277   1.000 107.12432 ?  83  HIS A N   1 
ATOM 610  C CA  . HIS A 1 83  ? 0.74010   4.87640   1.83622   1.000 107.53323 ?  83  HIS A CA  1 
ATOM 611  C C   . HIS A 1 83  ? 1.54874   3.94808   2.74351   1.000 108.18768 ?  83  HIS A C   1 
ATOM 612  O O   . HIS A 1 83  ? 1.50383   4.07077   3.97496   1.000 115.17955 ?  83  HIS A O   1 
ATOM 613  C CB  . HIS A 1 83  ? -0.54448  4.20411   1.34971   1.000 102.37234 ?  83  HIS A CB  1 
ATOM 614  C CG  . HIS A 1 83  ? -1.53470  5.15939   0.75992   1.000 98.00014  ?  83  HIS A CG  1 
ATOM 615  N ND1 . HIS A 1 83  ? -1.50931  6.51449   1.02453   1.000 91.36226  ?  83  HIS A ND1 1 
ATOM 616  C CD2 . HIS A 1 83  ? -2.59712  4.95816   -0.05384  1.000 101.27943 ?  83  HIS A CD2 1 
ATOM 617  C CE1 . HIS A 1 83  ? -2.50272  7.10472   0.38854   1.000 94.87756  ?  83  HIS A CE1 1 
ATOM 618  N NE2 . HIS A 1 83  ? -3.17934  6.18252   -0.27470  1.000 111.26933 ?  83  HIS A NE2 1 
ATOM 619  N N   . LEU A 1 84  ? 2.25955   2.98277   2.15558   1.000 98.39433  ?  84  LEU A N   1 
ATOM 620  C CA  . LEU A 1 84  ? 3.17621   2.15257   2.93269   1.000 96.83251  ?  84  LEU A CA  1 
ATOM 621  C C   . LEU A 1 84  ? 4.22013   3.00159   3.65253   1.000 101.94543 ?  84  LEU A C   1 
ATOM 622  O O   . LEU A 1 84  ? 4.56724   2.72618   4.80630   1.000 102.10309 ?  84  LEU A O   1 
ATOM 623  C CB  . LEU A 1 84  ? 3.85927   1.13656   2.01910   1.000 99.95214  ?  84  LEU A CB  1 
ATOM 624  C CG  . LEU A 1 84  ? 4.86639   0.17608   2.65419   1.000 80.99119  ?  84  LEU A CG  1 
ATOM 625  C CD1 . LEU A 1 84  ? 4.19834   -0.72121  3.66890   1.000 92.90621  ?  84  LEU A CD1 1 
ATOM 626  C CD2 . LEU A 1 84  ? 5.54138   -0.64516  1.58196   1.000 96.99291  ?  84  LEU A CD2 1 
ATOM 627  N N   . LYS A 1 85  ? 4.76782   4.00713   2.96546   1.000 93.68219  ?  85  LYS A N   1 
ATOM 628  C CA  . LYS A 1 85  ? 5.72079   4.91796   3.58405   1.000 88.22972  ?  85  LYS A CA  1 
ATOM 629  C C   . LYS A 1 85  ? 5.15236   5.53479   4.84982   1.000 107.59154 ?  85  LYS A C   1 
ATOM 630  O O   . LYS A 1 85  ? 5.76270   5.45805   5.91913   1.000 115.24612 ?  85  LYS A O   1 
ATOM 631  C CB  . LYS A 1 85  ? 6.10740   6.00818   2.58738   1.000 79.39345  ?  85  LYS A CB  1 
ATOM 632  C CG  . LYS A 1 85  ? 6.69577   7.27159   3.20899   1.000 92.25076  ?  85  LYS A CG  1 
ATOM 633  C CD  . LYS A 1 85  ? 6.56756   8.45694   2.25618   1.000 102.66424 ?  85  LYS A CD  1 
ATOM 634  C CE  . LYS A 1 85  ? 6.90385   9.79086   2.91319   1.000 99.21051  ?  85  LYS A CE  1 
ATOM 635  N NZ  . LYS A 1 85  ? 6.94116   10.90698  1.90826   1.000 102.10909 ?  85  LYS A NZ  1 
ATOM 636  N N   . ASP A 1 86  ? 3.98200   6.16323   4.73681   1.000 104.06600 ?  86  ASP A N   1 
ATOM 637  C CA  . ASP A 1 86  ? 3.37468   6.82826   5.88778   1.000 98.83777  ?  86  ASP A CA  1 
ATOM 638  C C   . ASP A 1 86  ? 3.05042   5.83491   7.00234   1.000 103.45087 ?  86  ASP A C   1 
ATOM 639  O O   . ASP A 1 86  ? 3.27193   6.12222   8.18882   1.000 97.99211  ?  86  ASP A O   1 
ATOM 640  C CB  . ASP A 1 86  ? 2.12646   7.58903   5.45378   1.000 95.66662  ?  86  ASP A CB  1 
ATOM 641  C CG  . ASP A 1 86  ? 2.40558   8.58284   4.35325   1.000 100.24764 ?  86  ASP A CG  1 
ATOM 642  O OD1 . ASP A 1 86  ? 3.58837   8.93990   4.16568   1.000 116.16629 ?  86  ASP A OD1 1 
ATOM 643  O OD2 . ASP A 1 86  ? 1.44043   9.01641   3.68712   1.000 105.44215 -1 86  ASP A OD2 1 
ATOM 644  N N   . ALA A 1 87  ? 2.49204   4.67387   6.64440   1.000 102.27702 ?  87  ALA A N   1 
ATOM 645  C CA  . ALA A 1 87  ? 2.22400   3.63995   7.63964   1.000 95.95276  ?  87  ALA A CA  1 
ATOM 646  C C   . ALA A 1 87  ? 3.49541   3.26016   8.38774   1.000 94.72355  ?  87  ALA A C   1 
ATOM 647  O O   . ALA A 1 87  ? 3.48943   3.13319   9.61409   1.000 105.15405 ?  87  ALA A O   1 
ATOM 648  C CB  . ALA A 1 87  ? 1.59998   2.41211   6.97463   1.000 81.70011  ?  87  ALA A CB  1 
ATOM 649  N N   . LEU A 1 88  ? 4.59554   3.05717   7.66153   1.000 102.40766 ?  88  LEU A N   1 
ATOM 650  C CA  . LEU A 1 88  ? 5.86318   2.71896   8.29586   1.000 100.53960 ?  88  LEU A CA  1 
ATOM 651  C C   . LEU A 1 88  ? 6.45142   3.87800   9.08027   1.000 86.43224  ?  88  LEU A C   1 
ATOM 652  O O   . LEU A 1 88  ? 7.24251   3.65301   9.99914   1.000 94.27394  ?  88  LEU A O   1 
ATOM 653  C CB  . LEU A 1 88  ? 6.86705   2.25046   7.24560   1.000 104.26781 ?  88  LEU A CB  1 
ATOM 654  C CG  . LEU A 1 88  ? 6.59124   0.84265   6.72904   1.000 98.23971  ?  88  LEU A CG  1 
ATOM 655  C CD1 . LEU A 1 88  ? 7.64295   0.42938   5.70494   1.000 104.13178 ?  88  LEU A CD1 1 
ATOM 656  C CD2 . LEU A 1 88  ? 6.52720   -0.13317  7.89957   1.000 91.25628  ?  88  LEU A CD2 1 
ATOM 657  N N   . MET A 1 89  ? 6.09884   5.10607   8.73304   1.000 89.85415  ?  89  MET A N   1 
ATOM 658  C CA  . MET A 1 89  ? 6.56915   6.24024   9.50940   1.000 110.89857 ?  89  MET A CA  1 
ATOM 659  C C   . MET A 1 89  ? 5.76198   6.41396   10.78635  1.000 114.74451 ?  89  MET A C   1 
ATOM 660  O O   . MET A 1 89  ? 6.22761   7.07289   11.72115  1.000 124.23419 ?  89  MET A O   1 
ATOM 661  C CB  . MET A 1 89  ? 6.52025   7.52258   8.66595   1.000 121.96143 ?  89  MET A CB  1 
ATOM 662  C CG  . MET A 1 89  ? 7.48398   7.56918   7.47297   1.000 114.93821 ?  89  MET A CG  1 
ATOM 663  S SD  . MET A 1 89  ? 9.20477   7.95457   7.89270   1.000 141.00129 ?  89  MET A SD  1 
ATOM 664  C CE  . MET A 1 89  ? 10.05587  6.46197   7.35594   1.000 106.49463 ?  89  MET A CE  1 
ATOM 665  N N   . ILE A 1 90  ? 4.56903   5.83686   10.84636  1.000 104.64012 ?  90  ILE A N   1 
ATOM 666  C CA  . ILE A 1 90  ? 3.81682   5.82517   12.09962  1.000 89.98304  ?  90  ILE A CA  1 
ATOM 667  C C   . ILE A 1 90  ? 4.16064   4.61151   12.95217  1.000 94.19438  ?  90  ILE A C   1 
ATOM 668  O O   . ILE A 1 90  ? 4.31892   4.72173   14.17041  1.000 101.89564 ?  90  ILE A O   1 
ATOM 669  C CB  . ILE A 1 90  ? 2.30786   5.90823   11.80921  1.000 84.13221  ?  90  ILE A CB  1 
ATOM 670  C CG1 . ILE A 1 90  ? 1.98013   7.29916   11.26713  1.000 86.59469  ?  90  ILE A CG1 1 
ATOM 671  C CG2 . ILE A 1 90  ? 1.48813   5.55635   13.04891  1.000 96.88006  ?  90  ILE A CG2 1 
ATOM 672  C CD1 . ILE A 1 90  ? 0.61043   7.42688   10.69862  1.000 82.82245  ?  90  ILE A CD1 1 
ATOM 673  N N   . ILE A 1 91  ? 4.32822   3.45664   12.32213  1.000 95.47540  ?  91  ILE A N   1 
ATOM 674  C CA  . ILE A 1 91  ? 4.47160   2.20492   13.05297  1.000 96.75945  ?  91  ILE A CA  1 
ATOM 675  C C   . ILE A 1 91  ? 5.85533   2.09184   13.68065  1.000 105.72320 ?  91  ILE A C   1 
ATOM 676  O O   . ILE A 1 91  ? 5.98759   1.83662   14.88309  1.000 113.18739 ?  91  ILE A O   1 
ATOM 677  C CB  . ILE A 1 91  ? 4.16795   1.03848   12.09887  1.000 93.82705  ?  91  ILE A CB  1 
ATOM 678  C CG1 . ILE A 1 91  ? 2.66788   1.04104   11.77607  1.000 98.89292  ?  91  ILE A CG1 1 
ATOM 679  C CG2 . ILE A 1 91  ? 4.64343   -0.27476  12.69089  1.000 95.79406  ?  91  ILE A CG2 1 
ATOM 680  C CD1 . ILE A 1 91  ? 2.24635   0.07486   10.71083  1.000 80.84831  ?  91  ILE A CD1 1 
ATOM 681  N N   . TYR A 1 92  ? 6.90298   2.30976   12.88837  1.000 105.89072 ?  92  TYR A N   1 
ATOM 682  C CA  . TYR A 1 92  ? 8.28312   2.16511   13.33498  1.000 111.98269 ?  92  TYR A CA  1 
ATOM 683  C C   . TYR A 1 92  ? 8.95519   3.49465   13.65505  1.000 125.99111 ?  92  TYR A C   1 
ATOM 684  O O   . TYR A 1 92  ? 10.16458  3.51985   13.91021  1.000 124.89777 ?  92  TYR A O   1 
ATOM 685  C CB  . TYR A 1 92  ? 9.09925   1.39411   12.29220  1.000 104.72376 ?  92  TYR A CB  1 
ATOM 686  C CG  . TYR A 1 92  ? 8.86229   -0.09781  12.33366  1.000 111.80664 ?  92  TYR A CG  1 
ATOM 687  C CD1 . TYR A 1 92  ? 9.61733   -0.90451  13.17539  1.000 121.12549 ?  92  TYR A CD1 1 
ATOM 688  C CD2 . TYR A 1 92  ? 7.86414   -0.69603  11.57388  1.000 119.19244 ?  92  TYR A CD2 1 
ATOM 689  C CE1 . TYR A 1 92  ? 9.41166   -2.26530  13.23774  1.000 132.14142 ?  92  TYR A CE1 1 
ATOM 690  C CE2 . TYR A 1 92  ? 7.64378   -2.06547  11.63649  1.000 123.84776 ?  92  TYR A CE2 1 
ATOM 691  C CZ  . TYR A 1 92  ? 8.42401   -2.84006  12.47030  1.000 117.94267 ?  92  TYR A CZ  1 
ATOM 692  O OH  . TYR A 1 92  ? 8.22378   -4.19216  12.54306  1.000 108.07537 ?  92  TYR A OH  1 
ATOM 693  N N   . GLY A 1 93  ? 8.20658   4.58985   13.66266  1.000 126.09497 ?  93  GLY A N   1 
ATOM 694  C CA  . GLY A 1 93  ? 8.77059   5.88726   13.96220  1.000 130.83869 ?  93  GLY A CA  1 
ATOM 695  C C   . GLY A 1 93  ? 9.13108   6.66838   12.70784  1.000 144.57351 ?  93  GLY A C   1 
ATOM 696  O O   . GLY A 1 93  ? 9.37923   6.11233   11.63474  1.000 133.67348 ?  93  GLY A O   1 
ATOM 697  N N   . MET A 1 94  ? 9.16860   7.98969   12.85936  1.000 195.28768 ?  94  MET A N   1 
ATOM 698  C CA  . MET A 1 94  ? 9.42198   8.89010   11.74524  1.000 194.59316 ?  94  MET A CA  1 
ATOM 699  C C   . MET A 1 94  ? 10.91762  8.99136   11.44738  1.000 194.18168 ?  94  MET A C   1 
ATOM 700  O O   . MET A 1 94  ? 11.77055  8.71805   12.29704  1.000 198.51388 ?  94  MET A O   1 
ATOM 701  C CB  . MET A 1 94  ? 8.86507   10.28483  12.04242  1.000 203.28854 ?  94  MET A CB  1 
ATOM 702  C CG  . MET A 1 94  ? 7.38003   10.33697  12.39398  1.000 198.93372 ?  94  MET A CG  1 
ATOM 703  S SD  . MET A 1 94  ? 6.27277   10.16878  10.97853  1.000 214.00794 ?  94  MET A SD  1 
ATOM 704  C CE  . MET A 1 94  ? 7.11344   11.16890  9.74838   1.000 202.00586 ?  94  MET A CE  1 
ATOM 705  N N   . SER A 1 95  ? 11.22542  9.40121   10.21775  1.000 155.50305 ?  95  SER A N   1 
ATOM 706  C CA  . SER A 1 95  ? 12.60296  9.65841   9.80220   1.000 145.56116 ?  95  SER A CA  1 
ATOM 707  C C   . SER A 1 95  ? 12.68058  10.77830  8.76178   1.000 141.19963 ?  95  SER A C   1 
ATOM 708  O O   . SER A 1 95  ? 11.66895  11.37568  8.38988   1.000 124.65749 ?  95  SER A O   1 
ATOM 709  C CB  . SER A 1 95  ? 13.24728  8.38682   9.24500   1.000 138.05359 ?  95  SER A CB  1 
ATOM 710  O OG  . SER A 1 95  ? 13.51213  7.45448   10.27708  1.000 128.92585 ?  95  SER A OG  1 
ATOM 711  N N   . ARG A 1 103 ? 24.06328  5.12155   1.24168   1.000 152.75414 ?  103 ARG A N   1 
ATOM 712  C CA  . ARG A 1 103 ? 24.08299  5.37327   -0.19541  1.000 152.57611 ?  103 ARG A CA  1 
ATOM 713  C C   . ARG A 1 103 ? 24.71856  4.19078   -0.92687  1.000 136.44481 ?  103 ARG A C   1 
ATOM 714  O O   . ARG A 1 103 ? 25.26245  4.35680   -2.01333  1.000 142.23133 ?  103 ARG A O   1 
ATOM 715  C CB  . ARG A 1 103 ? 24.82117  6.67476   -0.53917  1.000 163.75682 ?  103 ARG A CB  1 
ATOM 716  C CG  . ARG A 1 103 ? 24.31657  7.91745   0.20119   1.000 162.44896 ?  103 ARG A CG  1 
ATOM 717  C CD  . ARG A 1 103 ? 22.84044  8.22466   -0.05252  1.000 168.79770 ?  103 ARG A CD  1 
ATOM 718  N NE  . ARG A 1 103 ? 22.40888  9.39681   0.70476   1.000 184.49809 ?  103 ARG A NE  1 
ATOM 719  C CZ  . ARG A 1 103 ? 22.31408  10.62357  0.20712   1.000 171.47518 ?  103 ARG A CZ  1 
ATOM 720  N NH1 . ARG A 1 103 ? 22.61672  10.88258  -1.05324  1.000 158.40973 ?  103 ARG A NH1 1 
ATOM 721  N NH2 . ARG A 1 103 ? 21.92777  11.62004  1.00086   1.000 158.71575 ?  103 ARG A NH2 1 
ATOM 722  N N   . SER A 1 104 ? 24.68706  3.01078   -0.31032  1.000 111.31650 ?  104 SER A N   1 
ATOM 723  C CA  . SER A 1 104 ? 25.36204  1.82613   -0.82492  1.000 126.97962 ?  104 SER A CA  1 
ATOM 724  C C   . SER A 1 104 ? 24.35025  0.78484   -1.29376  1.000 132.59747 ?  104 SER A C   1 
ATOM 725  O O   . SER A 1 104 ? 23.23123  0.70468   -0.77835  1.000 138.23435 ?  104 SER A O   1 
ATOM 726  C CB  . SER A 1 104 ? 26.27371  1.20603   0.24118   1.000 129.44470 ?  104 SER A CB  1 
ATOM 727  O OG  . SER A 1 104 ? 25.52806  0.76185   1.36393   1.000 136.93895 ?  104 SER A OG  1 
ATOM 728  N N   . MET A 1 105 ? 24.75230  0.00298   -2.30627  1.000 144.09745 ?  105 MET A N   1 
ATOM 729  C CA  . MET A 1 105 ? 23.87877  -1.02915  -2.86400  1.000 138.25559 ?  105 MET A CA  1 
ATOM 730  C C   . MET A 1 105 ? 23.37544  -1.98778  -1.79775  1.000 137.73999 ?  105 MET A C   1 
ATOM 731  O O   . MET A 1 105 ? 22.24501  -2.48045  -1.88844  1.000 134.95911 ?  105 MET A O   1 
ATOM 732  C CB  . MET A 1 105 ? 24.61891  -1.83039  -3.93510  1.000 134.44183 ?  105 MET A CB  1 
ATOM 733  C CG  . MET A 1 105 ? 23.73326  -2.78577  -4.73170  1.000 134.53779 ?  105 MET A CG  1 
ATOM 734  S SD  . MET A 1 105 ? 24.69177  -4.09095  -5.53531  1.000 150.30398 ?  105 MET A SD  1 
ATOM 735  C CE  . MET A 1 105 ? 23.43083  -5.04367  -6.37408  1.000 125.66007 ?  105 MET A CE  1 
ATOM 736  N N   . SER A 1 106 ? 24.20254  -2.26844  -0.78861  1.000 133.18827 ?  106 SER A N   1 
ATOM 737  C CA  . SER A 1 106 ? 23.80468  -3.16512  0.29085   1.000 127.46746 ?  106 SER A CA  1 
ATOM 738  C C   . SER A 1 106 ? 22.53284  -2.68812  0.97961   1.000 130.98939 ?  106 SER A C   1 
ATOM 739  O O   . SER A 1 106 ? 21.78366  -3.50505  1.52697   1.000 134.21990 ?  106 SER A O   1 
ATOM 740  C CB  . SER A 1 106 ? 24.94992  -3.30860  1.29222   1.000 149.20729 ?  106 SER A CB  1 
ATOM 741  O OG  . SER A 1 106 ? 26.11153  -3.81033  0.64763   1.000 139.05428 ?  106 SER A OG  1 
ATOM 742  N N   . ARG A 1 107 ? 22.28678  -1.37695  0.99048   1.000 122.17952 ?  107 ARG A N   1 
ATOM 743  C CA  . ARG A 1 107 ? 21.05842  -0.81310  1.53574   1.000 132.32521 ?  107 ARG A CA  1 
ATOM 744  C C   . ARG A 1 107 ? 20.05367  -0.43128  0.45183   1.000 117.62479 ?  107 ARG A C   1 
ATOM 745  O O   . ARG A 1 107 ? 19.03123  0.19081   0.76164   1.000 112.23883 ?  107 ARG A O   1 
ATOM 746  C CB  . ARG A 1 107 ? 21.37080  0.41447   2.39754   1.000 136.86090 ?  107 ARG A CB  1 
ATOM 747  C CG  . ARG A 1 107 ? 22.00990  0.10597   3.73879   1.000 125.89583 ?  107 ARG A CG  1 
ATOM 748  C CD  . ARG A 1 107 ? 22.21471  1.37471   4.56709   1.000 141.93515 ?  107 ARG A CD  1 
ATOM 749  N NE  . ARG A 1 107 ? 23.27888  2.22856   4.04594   1.000 156.63677 ?  107 ARG A NE  1 
ATOM 750  C CZ  . ARG A 1 107 ? 23.61276  3.41007   4.55162   1.000 138.54165 ?  107 ARG A CZ  1 
ATOM 751  N NH1 . ARG A 1 107 ? 23.05846  3.87002   5.66246   1.000 129.10076 ?  107 ARG A NH1 1 
ATOM 752  N NH2 . ARG A 1 107 ? 24.55686  4.12966   3.95120   1.000 130.57184 ?  107 ARG A NH2 1 
ATOM 753  N N   . LYS A 1 108 ? 20.30856  -0.80738  -0.80295  1.000 110.32766 ?  108 LYS A N   1 
ATOM 754  C CA  . LYS A 1 108 ? 19.37293  -0.58166  -1.89641  1.000 96.56611  ?  108 LYS A CA  1 
ATOM 755  C C   . LYS A 1 108 ? 18.79986  -1.86238  -2.48374  1.000 98.83653  ?  108 LYS A C   1 
ATOM 756  O O   . LYS A 1 108 ? 17.65959  -1.85463  -2.95118  1.000 95.55088  ?  108 LYS A O   1 
ATOM 757  C CB  . LYS A 1 108 ? 20.05462  0.22046   -3.00971  1.000 99.35442  ?  108 LYS A CB  1 
ATOM 758  C CG  . LYS A 1 108 ? 20.51963  1.59602   -2.56465  1.000 108.97753 ?  108 LYS A CG  1 
ATOM 759  C CD  . LYS A 1 108 ? 21.03318  2.42436   -3.73104  1.000 111.45355 ?  108 LYS A CD  1 
ATOM 760  C CE  . LYS A 1 108 ? 21.49683  3.79752   -3.26317  1.000 115.60343 ?  108 LYS A CE  1 
ATOM 761  N NZ  . LYS A 1 108 ? 21.99607  4.63376   -4.39001  1.000 104.59674 ?  108 LYS A NZ  1 
ATOM 762  N N   . ILE A 1 109 ? 19.56738  -2.94923  -2.48863  1.000 93.05795  ?  109 ILE A N   1 
ATOM 763  C CA  . ILE A 1 109 ? 19.10717  -4.26976  -2.91100  1.000 87.80687  ?  109 ILE A CA  1 
ATOM 764  C C   . ILE A 1 109 ? 19.34321  -5.21754  -1.74899  1.000 84.31487  ?  109 ILE A C   1 
ATOM 765  O O   . ILE A 1 109 ? 20.49573  -5.52261  -1.42265  1.000 96.90525  ?  109 ILE A O   1 
ATOM 766  C CB  . ILE A 1 109 ? 19.82728  -4.75979  -4.17091  1.000 90.46583  ?  109 ILE A CB  1 
ATOM 767  C CG1 . ILE A 1 109 ? 19.72175  -3.70549  -5.27469  1.000 93.28950  ?  109 ILE A CG1 1 
ATOM 768  C CG2 . ILE A 1 109 ? 19.29275  -6.12161  -4.59246  1.000 91.49284  ?  109 ILE A CG2 1 
ATOM 769  C CD1 . ILE A 1 109 ? 20.03243  -4.22480  -6.64258  1.000 93.02189  ?  109 ILE A CD1 1 
ATOM 770  N N   . MET A 1 110 ? 18.26624  -5.71860  -1.14504  1.000 101.20519 ?  110 MET A N   1 
ATOM 771  C CA  . MET A 1 110 ? 18.39654  -6.51163  0.07566   1.000 85.59216  ?  110 MET A CA  1 
ATOM 772  C C   . MET A 1 110 ? 17.65841  -7.83649  -0.04749  1.000 83.36158  ?  110 MET A C   1 
ATOM 773  O O   . MET A 1 110 ? 16.48036  -7.85669  -0.40572  1.000 93.84796  ?  110 MET A O   1 
ATOM 774  C CB  . MET A 1 110 ? 17.87104  -5.72109  1.27534   1.000 87.01429  ?  110 MET A CB  1 
ATOM 775  C CG  . MET A 1 110 ? 18.76471  -4.55665  1.66140   1.000 96.03641  ?  110 MET A CG  1 
ATOM 776  S SD  . MET A 1 110 ? 17.85371  -3.01685  1.84424   1.000 124.50545 ?  110 MET A SD  1 
ATOM 777  C CE  . MET A 1 110 ? 17.06282  -2.92112  0.24281   1.000 88.99809  ?  110 MET A CE  1 
ATOM 778  N N   . THR A 1 111 ? 18.34525  -8.93996  0.25650   1.000 93.21671  ?  111 THR A N   1 
ATOM 779  C CA  . THR A 1 111 ? 17.76876  -10.27445 0.14105   1.000 100.48826 ?  111 THR A CA  1 
ATOM 780  C C   . THR A 1 111 ? 17.64794  -10.92587 1.51275   1.000 98.31769  ?  111 THR A C   1 
ATOM 781  O O   . THR A 1 111 ? 18.51883  -10.76139 2.37229   1.000 104.25645 ?  111 THR A O   1 
ATOM 782  C CB  . THR A 1 111 ? 18.60250  -11.17445 -0.78136  1.000 97.34912  ?  111 THR A CB  1 
ATOM 783  O OG1 . THR A 1 111 ? 17.96770  -12.45299 -0.89983  1.000 118.26613 ?  111 THR A OG1 1 
ATOM 784  C CG2 . THR A 1 111 ? 19.99954  -11.38189 -0.22362  1.000 90.24014  ?  111 THR A CG2 1 
ATOM 785  N N   . THR A 1 112 ? 16.56906  -11.68189 1.70082   1.000 118.43271 ?  112 THR A N   1 
ATOM 786  C CA  . THR A 1 112 ? 16.26997  -12.31347 2.97748   1.000 128.17011 ?  112 THR A CA  1 
ATOM 787  C C   . THR A 1 112 ? 15.64530  -13.68057 2.73544   1.000 124.24973 ?  112 THR A C   1 
ATOM 788  O O   . THR A 1 112 ? 15.17686  -13.98897 1.63517   1.000 122.39921 ?  112 THR A O   1 
ATOM 789  C CB  . THR A 1 112 ? 15.32477  -11.45357 3.83587   1.000 130.70729 ?  112 THR A CB  1 
ATOM 790  O OG1 . THR A 1 112 ? 14.21212  -11.01522 3.04332   1.000 113.01416 ?  112 THR A OG1 1 
ATOM 791  C CG2 . THR A 1 112 ? 16.05842  -10.24176 4.42373   1.000 127.73480 ?  112 THR A CG2 1 
ATOM 792  N N   . GLU A 1 113 ? 15.64407  -14.50223 3.78455   1.000 117.34665 ?  113 GLU A N   1 
ATOM 793  C CA  . GLU A 1 113 ? 15.03474  -15.82290 3.72600   1.000 111.32280 ?  113 GLU A CA  1 
ATOM 794  C C   . GLU A 1 113 ? 13.58919  -15.75267 4.20343   1.000 117.19375 ?  113 GLU A C   1 
ATOM 795  O O   . GLU A 1 113 ? 13.29086  -15.11171 5.21593   1.000 122.60066 ?  113 GLU A O   1 
ATOM 796  C CB  . GLU A 1 113 ? 15.82476  -16.82541 4.56293   1.000 99.68225  ?  113 GLU A CB  1 
ATOM 797  C CG  . GLU A 1 113 ? 15.40990  -18.25725 4.30151   1.000 112.79632 ?  113 GLU A CG  1 
ATOM 798  C CD  . GLU A 1 113 ? 16.58449  -19.15746 3.97182   1.000 128.55338 ?  113 GLU A CD  1 
ATOM 799  O OE1 . GLU A 1 113 ? 17.62947  -19.05443 4.65454   1.000 117.55632 ?  113 GLU A OE1 1 
ATOM 800  O OE2 . GLU A 1 113 ? 16.46420  -19.96053 3.01956   1.000 128.48591 -1 113 GLU A OE2 1 
ATOM 801  N N   . VAL A 1 114 ? 12.69656  -16.40088 3.46236   1.000 104.23916 ?  114 VAL A N   1 
ATOM 802  C CA  . VAL A 1 114 ? 11.26165  -16.34971 3.71433   1.000 102.96426 ?  114 VAL A CA  1 
ATOM 803  C C   . VAL A 1 114 ? 10.81967  -17.63009 4.39665   1.000 125.30663 ?  114 VAL A C   1 
ATOM 804  O O   . VAL A 1 114 ? 11.19112  -18.72939 3.96858   1.000 144.30683 ?  114 VAL A O   1 
ATOM 805  C CB  . VAL A 1 114 ? 10.47954  -16.13984 2.41389   1.000 121.76651 ?  114 VAL A CB  1 
ATOM 806  C CG1 . VAL A 1 114 ? 8.99706   -16.03121 2.71415   1.000 131.97976 ?  114 VAL A CG1 1 
ATOM 807  C CG2 . VAL A 1 114 ? 10.98253  -14.91278 1.73996   1.000 113.07193 ?  114 VAL A CG2 1 
ATOM 808  N N   . ASN A 1 115 ? 10.00967  -17.49264 5.43852   1.000 125.39629 ?  115 ASN A N   1 
ATOM 809  C CA  . ASN A 1 115 ? 9.50914   -18.63755 6.18042   1.000 132.54923 ?  115 ASN A CA  1 
ATOM 810  C C   . ASN A 1 115 ? 8.19071   -19.12660 5.58260   1.000 134.36432 ?  115 ASN A C   1 
ATOM 811  O O   . ASN A 1 115 ? 7.47583   -18.37906 4.90956   1.000 134.91278 ?  115 ASN A O   1 
ATOM 812  C CB  . ASN A 1 115 ? 9.32955   -18.27171 7.65491   1.000 124.20737 ?  115 ASN A CB  1 
ATOM 813  C CG  . ASN A 1 115 ? 9.11078   -19.48149 8.53309   1.000 140.74538 ?  115 ASN A CG  1 
ATOM 814  O OD1 . ASN A 1 115 ? 9.10948   -20.61802 8.05843   1.000 155.55360 ?  115 ASN A OD1 1 
ATOM 815  N ND2 . ASN A 1 115 ? 8.93511   -19.24567 9.82698   1.000 141.69262 ?  115 ASN A ND2 1 
ATOM 816  N N   . LYS A 1 116 ? 7.90446   -20.41648 5.79876   1.000 133.31264 ?  116 LYS A N   1 
ATOM 817  C CA  . LYS A 1 116 ? 6.66164   -21.02157 5.31799   1.000 137.83244 ?  116 LYS A CA  1 
ATOM 818  C C   . LYS A 1 116 ? 5.43272   -20.24446 5.77822   1.000 151.60728 ?  116 LYS A C   1 
ATOM 819  O O   . LYS A 1 116 ? 4.46295   -20.08236 5.02194   1.000 155.08810 ?  116 LYS A O   1 
ATOM 820  C CB  . LYS A 1 116 ? 6.57841   -22.47514 5.78735   1.000 131.17060 ?  116 LYS A CB  1 
ATOM 821  C CG  . LYS A 1 116 ? 7.66807   -23.35852 5.21571   1.000 135.26358 ?  116 LYS A CG  1 
ATOM 822  C CD  . LYS A 1 116 ? 7.58542   -24.77618 5.74759   1.000 115.60873 ?  116 LYS A CD  1 
ATOM 823  C CE  . LYS A 1 116 ? 8.60088   -25.66033 5.04779   1.000 122.15093 ?  116 LYS A CE  1 
ATOM 824  N NZ  . LYS A 1 116 ? 8.54682   -27.06821 5.50763   1.000 119.95369 ?  116 LYS A NZ  1 
ATOM 825  N N   . THR A 1 117 ? 5.45255   -19.75816 7.02041   1.000 148.43831 ?  117 THR A N   1 
ATOM 826  C CA  . THR A 1 117 ? 4.35119   -18.93370 7.50178   1.000 141.47771 ?  117 THR A CA  1 
ATOM 827  C C   . THR A 1 117 ? 4.21095   -17.69174 6.63519   1.000 137.43661 ?  117 THR A C   1 
ATOM 828  O O   . THR A 1 117 ? 3.10843   -17.34019 6.20061   1.000 144.50521 ?  117 THR A O   1 
ATOM 829  C CB  . THR A 1 117 ? 4.57332   -18.56443 8.96730   1.000 134.96870 ?  117 THR A CB  1 
ATOM 830  O OG1 . THR A 1 117 ? 4.87458   -19.75055 9.71621   1.000 133.16079 ?  117 THR A OG1 1 
ATOM 831  C CG2 . THR A 1 117 ? 3.33149   -17.90737 9.54044   1.000 135.42734 ?  117 THR A CG2 1 
ATOM 832  N N   . LEU A 1 118 ? 5.32805   -17.01243 6.37705   1.000 137.45694 ?  118 LEU A N   1 
ATOM 833  C CA  . LEU A 1 118 ? 5.32873   -15.90855 5.42495   1.000 141.54725 ?  118 LEU A CA  1 
ATOM 834  C C   . LEU A 1 118 ? 4.96221   -16.38269 4.01822   1.000 145.00800 ?  118 LEU A C   1 
ATOM 835  O O   . LEU A 1 118 ? 4.41495   -15.60709 3.22807   1.000 136.83680 ?  118 LEU A O   1 
ATOM 836  C CB  . LEU A 1 118 ? 6.69074   -15.21234 5.44064   1.000 138.42617 ?  118 LEU A CB  1 
ATOM 837  C CG  . LEU A 1 118 ? 7.33574   -15.06153 6.82667   1.000 129.32719 ?  118 LEU A CG  1 
ATOM 838  C CD1 . LEU A 1 118 ? 8.75219   -14.49869 6.72136   1.000 128.60124 ?  118 LEU A CD1 1 
ATOM 839  C CD2 . LEU A 1 118 ? 6.47965   -14.21330 7.76339   1.000 116.48076 ?  118 LEU A CD2 1 
ATOM 840  N N   . LEU A 1 119 ? 5.27019   -17.64219 3.68183   1.000 153.55454 ?  119 LEU A N   1 
ATOM 841  C CA  . LEU A 1 119 ? 4.86491   -18.19475 2.38860   1.000 153.69343 ?  119 LEU A CA  1 
ATOM 842  C C   . LEU A 1 119 ? 3.34810   -18.20410 2.23808   1.000 156.46268 ?  119 LEU A C   1 
ATOM 843  O O   . LEU A 1 119 ? 2.82495   -18.01129 1.13189   1.000 162.71249 ?  119 LEU A O   1 
ATOM 844  C CB  . LEU A 1 119 ? 5.42548   -19.61055 2.21431   1.000 151.65958 ?  119 LEU A CB  1 
ATOM 845  C CG  . LEU A 1 119 ? 4.86800   -20.49609 1.08908   1.000 155.46416 ?  119 LEU A CG  1 
ATOM 846  C CD1 . LEU A 1 119 ? 5.14530   -19.90295 -0.28442  1.000 164.94165 ?  119 LEU A CD1 1 
ATOM 847  C CD2 . LEU A 1 119 ? 5.39963   -21.92462 1.17918   1.000 145.62389 ?  119 LEU A CD2 1 
ATOM 848  N N   . ASP A 1 120 ? 2.62222   -18.47029 3.32712   1.000 152.53090 ?  120 ASP A N   1 
ATOM 849  C CA  . ASP A 1 120 ? 1.16435   -18.40478 3.24457   1.000 152.93163 ?  120 ASP A CA  1 
ATOM 850  C C   . ASP A 1 120 ? 0.69759   -17.02488 2.78385   1.000 151.47150 ?  120 ASP A C   1 
ATOM 851  O O   . ASP A 1 120 ? -0.18267  -16.91445 1.92372   1.000 153.32773 ?  120 ASP A O   1 
ATOM 852  C CB  . ASP A 1 120 ? 0.53026   -18.76793 4.58834   1.000 157.40839 ?  120 ASP A CB  1 
ATOM 853  C CG  . ASP A 1 120 ? -0.95308  -19.11507 4.46401   1.000 162.88850 ?  120 ASP A CG  1 
ATOM 854  O OD1 . ASP A 1 120 ? -1.28178  -20.17416 3.88300   1.000 161.11017 -1 120 ASP A OD1 1 
ATOM 855  O OD2 . ASP A 1 120 ? -1.79326  -18.32825 4.95163   1.000 159.32393 ?  120 ASP A OD2 1 
ATOM 856  N N   . GLU A 1 121 ? 1.27908   -15.95738 3.33305   1.000 146.37526 ?  121 GLU A N   1 
ATOM 857  C CA  . GLU A 1 121 ? 0.94485   -14.62141 2.84549   1.000 145.35903 ?  121 GLU A CA  1 
ATOM 858  C C   . GLU A 1 121 ? 1.44196   -14.41270 1.41652   1.000 140.48243 ?  121 GLU A C   1 
ATOM 859  O O   . GLU A 1 121 ? 0.76783   -13.76447 0.60741   1.000 138.83464 ?  121 GLU A O   1 
ATOM 860  C CB  . GLU A 1 121 ? 1.51643   -13.56103 3.78573   1.000 149.19514 ?  121 GLU A CB  1 
ATOM 861  C CG  . GLU A 1 121 ? 0.56212   -13.12429 4.91036   1.000 145.93708 ?  121 GLU A CG  1 
ATOM 862  C CD  . GLU A 1 121 ? -0.87729  -12.90840 4.45866   1.000 138.64646 ?  121 GLU A CD  1 
ATOM 863  O OE1 . GLU A 1 121 ? -1.13018  -11.95351 3.69435   1.000 140.51153 ?  121 GLU A OE1 1 
ATOM 864  O OE2 . GLU A 1 121 ? -1.75925  -13.68999 4.88120   1.000 127.30649 -1 121 GLU A OE2 1 
ATOM 865  N N   . LEU A 1 122 ? 2.62401   -14.94878 1.09226   1.000 142.70275 ?  122 LEU A N   1 
ATOM 866  C CA  . LEU A 1 122 ? 3.16394   -14.85058 -0.26287  1.000 146.36502 ?  122 LEU A CA  1 
ATOM 867  C C   . LEU A 1 122 ? 2.27356   -15.52201 -1.29671  1.000 148.82323 ?  122 LEU A C   1 
ATOM 868  O O   . LEU A 1 122 ? 2.44703   -15.28299 -2.49540  1.000 145.14791 ?  122 LEU A O   1 
ATOM 869  C CB  . LEU A 1 122 ? 4.56101   -15.46731 -0.33895  1.000 144.56533 ?  122 LEU A CB  1 
ATOM 870  C CG  . LEU A 1 122 ? 5.77504   -14.58347 -0.06124  1.000 143.52676 ?  122 LEU A CG  1 
ATOM 871  C CD1 . LEU A 1 122 ? 7.02625   -15.42732 -0.15590  1.000 134.41791 ?  122 LEU A CD1 1 
ATOM 872  C CD2 . LEU A 1 122 ? 5.84488   -13.41556 -1.04190  1.000 128.50482 ?  122 LEU A CD2 1 
ATOM 873  N N   . LYS A 1 123 ? 1.40371   -16.43370 -0.87494  1.000 154.18197 ?  123 LYS A N   1 
ATOM 874  C CA  . LYS A 1 123 ? 0.36990   -16.93332 -1.77253  1.000 154.50307 ?  123 LYS A CA  1 
ATOM 875  C C   . LYS A 1 123 ? -0.95939  -16.20189 -1.60483  1.000 153.42578 ?  123 LYS A C   1 
ATOM 876  O O   . LYS A 1 123 ? -1.76575  -16.19749 -2.54268  1.000 153.33109 ?  123 LYS A O   1 
ATOM 877  C CB  . LYS A 1 123 ? 0.16856   -18.44724 -1.59746  1.000 158.50037 ?  123 LYS A CB  1 
ATOM 878  C CG  . LYS A 1 123 ? -0.58963  -18.87467 -0.36063  1.000 157.29925 ?  123 LYS A CG  1 
ATOM 879  C CD  . LYS A 1 123 ? -1.66475  -19.88937 -0.70082  1.000 152.88824 ?  123 LYS A CD  1 
ATOM 880  C CE  . LYS A 1 123 ? -2.11754  -20.62622 0.54014   1.000 155.16729 ?  123 LYS A CE  1 
ATOM 881  N NZ  . LYS A 1 123 ? -0.97492  -21.34824 1.16020   1.000 157.51153 ?  123 LYS A NZ  1 
ATOM 882  N N   . ASN A 1 124 ? -1.19860  -15.57449 -0.44747  1.000 143.34659 ?  124 ASN A N   1 
ATOM 883  C CA  . ASN A 1 124 ? -2.39632  -14.77237 -0.21259  1.000 132.76491 ?  124 ASN A CA  1 
ATOM 884  C C   . ASN A 1 124 ? -2.26318  -13.32939 -0.68443  1.000 127.97909 ?  124 ASN A C   1 
ATOM 885  O O   . ASN A 1 124 ? -3.16409  -12.52414 -0.41907  1.000 108.92526 ?  124 ASN A O   1 
ATOM 886  C CB  . ASN A 1 124 ? -2.76741  -14.77030 1.27428   1.000 134.62722 ?  124 ASN A CB  1 
ATOM 887  C CG  . ASN A 1 124 ? -3.17690  -16.14138 1.78198   1.000 153.90843 ?  124 ASN A CG  1 
ATOM 888  O OD1 . ASN A 1 124 ? -3.53292  -17.03153 1.00443   1.000 140.76682 ?  124 ASN A OD1 1 
ATOM 889  N ND2 . ASN A 1 124 ? -3.14742  -16.31134 3.10034   1.000 159.46888 ?  124 ASN A ND2 1 
ATOM 890  N N   . ILE A 1 125 ? -1.16528  -12.97871 -1.35614  1.000 138.54795 ?  125 ILE A N   1 
ATOM 891  C CA  . ILE A 1 125 ? -1.03991  -11.65271 -1.95042  1.000 125.98091 ?  125 ILE A CA  1 
ATOM 892  C C   . ILE A 1 125 ? -1.98355  -11.54596 -3.14085  1.000 125.26095 ?  125 ILE A C   1 
ATOM 893  O O   . ILE A 1 125 ? -2.05667  -12.44906 -3.98393  1.000 133.57540 ?  125 ILE A O   1 
ATOM 894  C CB  . ILE A 1 125 ? 0.41651   -11.37472 -2.35254  1.000 122.56602 ?  125 ILE A CB  1 
ATOM 895  C CG1 . ILE A 1 125 ? 1.12491   -12.66824 -2.75186  1.000 128.69300 ?  125 ILE A CG1 1 
ATOM 896  C CG2 . ILE A 1 125 ? 1.17912   -10.73293 -1.19910  1.000 109.49608 ?  125 ILE A CG2 1 
ATOM 897  C CD1 . ILE A 1 125 ? 0.75800   -13.24553 -4.11674  1.000 118.32071 ?  125 ILE A CD1 1 
ATOM 898  N N   . ASN A 1 126 ? -2.72226  -10.44525 -3.20832  1.000 121.05239 ?  126 ASN A N   1 
ATOM 899  C CA  . ASN A 1 126 ? -3.72177  -10.24282 -4.24441  1.000 118.14533 ?  126 ASN A CA  1 
ATOM 900  C C   . ASN A 1 126 ? -3.69854  -8.78391  -4.66724  1.000 130.44948 ?  126 ASN A C   1 
ATOM 901  O O   . ASN A 1 126 ? -3.60183  -7.88864  -3.82348  1.000 126.56397 ?  126 ASN A O   1 
ATOM 902  C CB  . ASN A 1 126 ? -5.12591  -10.63884 -3.76789  1.000 125.38819 ?  126 ASN A CB  1 
ATOM 903  C CG  . ASN A 1 126 ? -5.34160  -12.14876 -3.75099  1.000 137.54950 ?  126 ASN A CG  1 
ATOM 904  O OD1 . ASN A 1 126 ? -4.59901  -12.90612 -4.37703  1.000 113.58479 ?  126 ASN A OD1 1 
ATOM 905  N ND2 . ASN A 1 126 ? -6.38057  -12.58853 -3.04544  1.000 144.93561 ?  126 ASN A ND2 1 
ATOM 906  N N   . SER A 1 127 ? -3.78472  -8.55044  -5.97909  1.000 142.47030 ?  127 SER A N   1 
ATOM 907  C CA  . SER A 1 127 ? -3.76842  -7.18161  -6.48249  1.000 137.37389 ?  127 SER A CA  1 
ATOM 908  C C   . SER A 1 127 ? -5.06110  -6.45038  -6.14596  1.000 141.47308 ?  127 SER A C   1 
ATOM 909  O O   . SER A 1 127 ? -5.09257  -5.21476  -6.15000  1.000 141.58528 ?  127 SER A O   1 
ATOM 910  C CB  . SER A 1 127 ? -3.53492  -7.18236  -7.99315  1.000 115.37289 ?  127 SER A CB  1 
ATOM 911  O OG  . SER A 1 127 ? -4.59009  -7.84507  -8.66867  1.000 132.75365 ?  127 SER A OG  1 
ATOM 912  N N   . HIS A 1 128 ? -6.12778  -7.18593  -5.85163  1.000 150.99024 ?  128 HIS A N   1 
ATOM 913  C CA  . HIS A 1 128 ? -7.31010  -6.58768  -5.25891  1.000 166.08907 ?  128 HIS A CA  1 
ATOM 914  C C   . HIS A 1 128 ? -7.12273  -6.44595  -3.74739  1.000 173.73018 ?  128 HIS A C   1 
ATOM 915  O O   . HIS A 1 128 ? -6.16587  -6.96450  -3.16343  1.000 174.26216 ?  128 HIS A O   1 
ATOM 916  C CB  . HIS A 1 128 ? -8.55156  -7.41943  -5.58011  1.000 175.75808 ?  128 HIS A CB  1 
ATOM 917  C CG  . HIS A 1 128 ? -8.27692  -8.88436  -5.73805  1.000 167.99896 ?  128 HIS A CG  1 
ATOM 918  N ND1 . HIS A 1 128 ? -7.82163  -9.43263  -6.91782  1.000 162.09702 ?  128 HIS A ND1 1 
ATOM 919  C CD2 . HIS A 1 128 ? -8.40421  -9.91504  -4.86839  1.000 173.39797 ?  128 HIS A CD2 1 
ATOM 920  C CE1 . HIS A 1 128 ? -7.67542  -10.73778 -6.76758  1.000 159.87758 ?  128 HIS A CE1 1 
ATOM 921  N NE2 . HIS A 1 128 ? -8.02201  -11.05563 -5.53351  1.000 169.52716 ?  128 HIS A NE2 1 
ATOM 922  N N   . ASP A 1 129 ? -8.05595  -5.72951  -3.11568  1.000 171.87325 ?  129 ASP A N   1 
ATOM 923  C CA  . ASP A 1 129 ? -7.99170  -5.40903  -1.68621  1.000 168.39974 ?  129 ASP A CA  1 
ATOM 924  C C   . ASP A 1 129 ? -6.64093  -4.78539  -1.32812  1.000 165.25826 ?  129 ASP A C   1 
ATOM 925  O O   . ASP A 1 129 ? -5.89616  -5.28780  -0.48273  1.000 168.47590 ?  129 ASP A O   1 
ATOM 926  C CB  . ASP A 1 129 ? -8.27745  -6.64604  -0.82964  1.000 167.07421 ?  129 ASP A CB  1 
ATOM 927  C CG  . ASP A 1 129 ? -8.77958  -6.29284  0.56037   1.000 175.07778 ?  129 ASP A CG  1 
ATOM 928  O OD1 . ASP A 1 129 ? -8.54227  -5.15283  1.01355   1.000 170.52643 ?  129 ASP A OD1 1 
ATOM 929  O OD2 . ASP A 1 129 ? -9.40775  -7.15965  1.20486   1.000 187.24426 ?  129 ASP A OD2 1 
ATOM 930  N N   . ASN A 1 130 ? -6.33070  -3.66943  -1.99774  1.000 135.88468 ?  130 ASN A N   1 
ATOM 931  C CA  . ASN A 1 130 ? -5.05594  -2.98188  -1.79857  1.000 118.94448 ?  130 ASN A CA  1 
ATOM 932  C C   . ASN A 1 130 ? -4.81849  -2.64560  -0.33511  1.000 118.71011 ?  130 ASN A C   1 
ATOM 933  O O   . ASN A 1 130 ? -3.67334  -2.63831  0.13082   1.000 107.00592 ?  130 ASN A O   1 
ATOM 934  C CB  . ASN A 1 130 ? -5.01725  -1.72321  -2.65300  1.000 114.10709 ?  130 ASN A CB  1 
ATOM 935  C CG  . ASN A 1 130 ? -5.36097  -2.00701  -4.08387  1.000 125.55816 ?  130 ASN A CG  1 
ATOM 936  O OD1 . ASN A 1 130 ? -6.48526  -2.40413  -4.39600  1.000 133.35608 ?  130 ASN A OD1 1 
ATOM 937  N ND2 . ASN A 1 130 ? -4.39279  -1.82337  -4.96912  1.000 129.44571 ?  130 ASN A ND2 1 
ATOM 938  N N   . SER A 1 131 ? -5.88710  -2.30579  0.38779   1.000 124.15054 ?  131 SER A N   1 
ATOM 939  C CA  . SER A 1 131 ? -5.79944  -2.13757  1.83368   1.000 108.01010 ?  131 SER A CA  1 
ATOM 940  C C   . SER A 1 131 ? -5.14905  -3.35768  2.47915   1.000 104.36829 ?  131 SER A C   1 
ATOM 941  O O   . SER A 1 131 ? -4.16733  -3.23813  3.22245   1.000 122.65115 ?  131 SER A O   1 
ATOM 942  C CB  . SER A 1 131 ? -7.20052  -1.90389  2.40386   1.000 106.20245 ?  131 SER A CB  1 
ATOM 943  O OG  . SER A 1 131 ? -7.67052  -0.59359  2.12637   1.000 100.19615 ?  131 SER A OG  1 
ATOM 944  N N   . ALA A 1 132 ? -5.68536  -4.54781  2.19112   1.000 103.82371 ?  132 ALA A N   1 
ATOM 945  C CA  . ALA A 1 132 ? -5.12424  -5.78284  2.73256   1.000 109.27560 ?  132 ALA A CA  1 
ATOM 946  C C   . ALA A 1 132 ? -3.69846  -6.01509  2.24350   1.000 112.28398 ?  132 ALA A C   1 
ATOM 947  O O   . ALA A 1 132 ? -2.87267  -6.57519  2.97284   1.000 108.85795 ?  132 ALA A O   1 
ATOM 948  C CB  . ALA A 1 132 ? -6.01296  -6.97384  2.37975   1.000 118.78176 ?  132 ALA A CB  1 
ATOM 949  N N   . PHE A 1 133 ? -3.39901  -5.63847  0.99581   1.000 110.52115 ?  133 PHE A N   1 
ATOM 950  C CA  . PHE A 1 133 ? -2.04397  -5.82998  0.48155   1.000 106.27261 ?  133 PHE A CA  1 
ATOM 951  C C   . PHE A 1 133 ? -1.02706  -5.01319  1.27639   1.000 96.98260  ?  133 PHE A C   1 
ATOM 952  O O   . PHE A 1 133 ? 0.01613   -5.53382  1.69406   1.000 93.48551  ?  133 PHE A O   1 
ATOM 953  C CB  . PHE A 1 133 ? -1.96975  -5.46623  -0.99913  1.000 99.72035  ?  133 PHE A CB  1 
ATOM 954  C CG  . PHE A 1 133 ? -0.71454  -5.95253  -1.65489  1.000 106.13565 ?  133 PHE A CG  1 
ATOM 955  C CD1 . PHE A 1 133 ? 0.38553   -5.12107  -1.80048  1.000 101.24177 ?  133 PHE A CD1 1 
ATOM 956  C CD2 . PHE A 1 133 ? -0.61345  -7.26932  -2.06927  1.000 102.07949 ?  133 PHE A CD2 1 
ATOM 957  C CE1 . PHE A 1 133 ? 1.55080   -5.59033  -2.38090  1.000 82.91642  ?  133 PHE A CE1 1 
ATOM 958  C CE2 . PHE A 1 133 ? 0.54182   -7.74005  -2.65155  1.000 103.64058 ?  133 PHE A CE2 1 
ATOM 959  C CZ  . PHE A 1 133 ? 1.62733   -6.90375  -2.80614  1.000 86.05091  ?  133 PHE A CZ  1 
ATOM 960  N N   . ILE A 1 134 ? -1.28976  -3.71333  1.44333   1.000 92.65811  ?  134 ILE A N   1 
ATOM 961  C CA  . ILE A 1 134 ? -0.42943  -2.87042  2.27136   1.000 98.98173  ?  134 ILE A CA  1 
ATOM 962  C C   . ILE A 1 134 ? -0.34966  -3.42235  3.69384   1.000 95.00958  ?  134 ILE A C   1 
ATOM 963  O O   . ILE A 1 134 ? 0.71845   -3.41331  4.31926   1.000 94.28359  ?  134 ILE A O   1 
ATOM 964  C CB  . ILE A 1 134 ? -0.92513  -1.41074  2.25191   1.000 96.32940  ?  134 ILE A CB  1 
ATOM 965  C CG1 . ILE A 1 134 ? -1.08924  -0.91595  0.81338   1.000 111.83982 ?  134 ILE A CG1 1 
ATOM 966  C CG2 . ILE A 1 134 ? 0.04686   -0.50342  2.99085   1.000 89.36734  ?  134 ILE A CG2 1 
ATOM 967  C CD1 . ILE A 1 134 ? -1.80848  0.42843   0.70036   1.000 104.36090 ?  134 ILE A CD1 1 
ATOM 968  N N   . SER A 1 135 ? -1.48163  -3.87703  4.24000   1.000 86.39845  ?  135 SER A N   1 
ATOM 969  C CA  . SER A 1 135 ? -1.46601  -4.50539  5.55818   1.000 92.84778  ?  135 SER A CA  1 
ATOM 970  C C   . SER A 1 135 ? -0.48877  -5.67325  5.60478   1.000 102.27901 ?  135 SER A C   1 
ATOM 971  O O   . SER A 1 135 ? 0.27280   -5.82669  6.56653   1.000 107.79237 ?  135 SER A O   1 
ATOM 972  C CB  . SER A 1 135 ? -2.87058  -4.98194  5.94282   1.000 100.86171 ?  135 SER A CB  1 
ATOM 973  O OG  . SER A 1 135 ? -3.85303  -3.98284  5.72811   1.000 98.12432  ?  135 SER A OG  1 
ATOM 974  N N   . SER A 1 136 ? -0.52438  -6.52885  4.58263   1.000 93.15108  ?  136 SER A N   1 
ATOM 975  C CA  . SER A 1 136 ? 0.35251   -7.69528  4.55255   1.000 91.58924  ?  136 SER A CA  1 
ATOM 976  C C   . SER A 1 136 ? 1.81714   -7.29337  4.41378   1.000 85.53191  ?  136 SER A C   1 
ATOM 977  O O   . SER A 1 136 ? 2.70287   -7.94627  4.97599   1.000 93.37466  ?  136 SER A O   1 
ATOM 978  C CB  . SER A 1 136 ? -0.07850  -8.63138  3.43049   1.000 84.27924  ?  136 SER A CB  1 
ATOM 979  O OG  . SER A 1 136 ? -1.48207  -8.80890  3.46771   1.000 98.93623  ?  136 SER A OG  1 
ATOM 980  N N   . LEU A 1 137 ? 2.09858   -6.24103  3.65188   1.000 67.61807  ?  137 LEU A N   1 
ATOM 981  C CA  . LEU A 1 137 ? 3.46589   -5.73407  3.61317   1.000 85.94573  ?  137 LEU A CA  1 
ATOM 982  C C   . LEU A 1 137 ? 3.91394   -5.28549  4.99742   1.000 98.51225  ?  137 LEU A C   1 
ATOM 983  O O   . LEU A 1 137 ? 5.03267   -5.58995  5.43104   1.000 96.53406  ?  137 LEU A O   1 
ATOM 984  C CB  . LEU A 1 137 ? 3.58998   -4.58961  2.60851   1.000 104.67278 ?  137 LEU A CB  1 
ATOM 985  C CG  . LEU A 1 137 ? 3.33147   -4.96385  1.15353   1.000 99.74799  ?  137 LEU A CG  1 
ATOM 986  C CD1 . LEU A 1 137 ? 3.38537   -3.72630  0.27013   1.000 94.10592  ?  137 LEU A CD1 1 
ATOM 987  C CD2 . LEU A 1 137 ? 4.36301   -5.99900  0.72009   1.000 72.03987  ?  137 LEU A CD2 1 
ATOM 988  N N   . ILE A 1 138 ? 3.06371   -4.51590  5.68343   1.000 103.20398 ?  138 ILE A N   1 
ATOM 989  C CA  . ILE A 1 138 ? 3.32748   -4.13325  7.07091   1.000 93.56061  ?  138 ILE A CA  1 
ATOM 990  C C   . ILE A 1 138 ? 3.64717   -5.36341  7.91209   1.000 92.89839  ?  138 ILE A C   1 
ATOM 991  O O   . ILE A 1 138 ? 4.63506   -5.39464  8.65569   1.000 99.84590  ?  138 ILE A O   1 
ATOM 992  C CB  . ILE A 1 138 ? 2.13006   -3.35505  7.64681   1.000 88.55784  ?  138 ILE A CB  1 
ATOM 993  C CG1 . ILE A 1 138 ? 1.90286   -2.05980  6.86527   1.000 94.53122  ?  138 ILE A CG1 1 
ATOM 994  C CG2 . ILE A 1 138 ? 2.33333   -3.07107  9.11302   1.000 89.53844  ?  138 ILE A CG2 1 
ATOM 995  C CD1 . ILE A 1 138 ? 3.01002   -1.04596  7.02397   1.000 103.62037 ?  138 ILE A CD1 1 
ATOM 996  N N   . TYR A 1 139 ? 2.80428   -6.39197  7.80661   1.000 84.29429  ?  139 TYR A N   1 
ATOM 997  C CA  . TYR A 1 139 ? 2.97447   -7.60266  8.60719   1.000 99.76068  ?  139 TYR A CA  1 
ATOM 998  C C   . TYR A 1 139 ? 4.31402   -8.28094  8.32645   1.000 101.38664 ?  139 TYR A C   1 
ATOM 999  O O   . TYR A 1 139 ? 5.04526   -8.65742  9.25425   1.000 96.30052  ?  139 TYR A O   1 
ATOM 1000 C CB  . TYR A 1 139 ? 1.82062   -8.56131  8.33547   1.000 100.60507 ?  139 TYR A CB  1 
ATOM 1001 C CG  . TYR A 1 139 ? 1.90289   -9.83877  9.13113   1.000 115.57096 ?  139 TYR A CG  1 
ATOM 1002 C CD1 . TYR A 1 139 ? 1.79169   -9.82805  10.51676  1.000 108.29781 ?  139 TYR A CD1 1 
ATOM 1003 C CD2 . TYR A 1 139 ? 2.11858   -11.05532 8.49757   1.000 116.95411 ?  139 TYR A CD2 1 
ATOM 1004 C CE1 . TYR A 1 139 ? 1.86834   -10.99802 11.24286  1.000 112.26386 ?  139 TYR A CE1 1 
ATOM 1005 C CE2 . TYR A 1 139 ? 2.20125   -12.22861 9.21337   1.000 121.60579 ?  139 TYR A CE2 1 
ATOM 1006 C CZ  . TYR A 1 139 ? 2.07487   -12.19798 10.58512  1.000 128.66715 ?  139 TYR A CZ  1 
ATOM 1007 O OH  . TYR A 1 139 ? 2.15915   -13.37719 11.28940  1.000 130.09771 ?  139 TYR A OH  1 
ATOM 1008 N N   . LEU A 1 140 ? 4.62632   -8.48719  7.04435   1.000 99.84342  ?  140 LEU A N   1 
ATOM 1009 C CA  . LEU A 1 140 ? 5.89349   -9.10308  6.66229   1.000 90.72253  ?  140 LEU A CA  1 
ATOM 1010 C C   . LEU A 1 140 ? 7.07808   -8.29988  7.18257   1.000 91.31804  ?  140 LEU A C   1 
ATOM 1011 O O   . LEU A 1 140 ? 7.97022   -8.84552  7.84286   1.000 92.02176  ?  140 LEU A O   1 
ATOM 1012 C CB  . LEU A 1 140 ? 5.96629   -9.23869  5.14440   1.000 88.53062  ?  140 LEU A CB  1 
ATOM 1013 C CG  . LEU A 1 140 ? 7.19913   -9.97824  4.63590   1.000 84.98283  ?  140 LEU A CG  1 
ATOM 1014 C CD1 . LEU A 1 140 ? 7.31855   -11.31267 5.34338   1.000 102.25545 ?  140 LEU A CD1 1 
ATOM 1015 C CD2 . LEU A 1 140 ? 7.11873   -10.17483 3.13429   1.000 82.10941  ?  140 LEU A CD2 1 
ATOM 1016 N N   . ILE A 1 141 ? 7.10393   -6.99658  6.88863   1.000 88.40489  ?  141 ILE A N   1 
ATOM 1017 C CA  . ILE A 1 141 ? 8.17739   -6.13335  7.37610   1.000 93.20242  ?  141 ILE A CA  1 
ATOM 1018 C C   . ILE A 1 141 ? 8.31622   -6.24917  8.88971   1.000 97.13460  ?  141 ILE A C   1 
ATOM 1019 O O   . ILE A 1 141 ? 9.42585   -6.21945  9.43454   1.000 105.53785 ?  141 ILE A O   1 
ATOM 1020 C CB  . ILE A 1 141 ? 7.93105   -4.68041  6.92399   1.000 86.46999  ?  141 ILE A CB  1 
ATOM 1021 C CG1 . ILE A 1 141 ? 8.10328   -4.57057  5.40585   1.000 77.59917  ?  141 ILE A CG1 1 
ATOM 1022 C CG2 . ILE A 1 141 ? 8.84817   -3.70933  7.65443   1.000 83.67268  ?  141 ILE A CG2 1 
ATOM 1023 C CD1 . ILE A 1 141 ? 7.38745   -3.39662  4.79222   1.000 94.17615  ?  141 ILE A CD1 1 
ATOM 1024 N N   . SER A 1 142 ? 7.19316   -6.38064  9.59320   1.000 95.78634  ?  142 SER A N   1 
ATOM 1025 C CA  . SER A 1 142 ? 7.25230   -6.57290  11.03565  1.000 94.94313  ?  142 SER A CA  1 
ATOM 1026 C C   . SER A 1 142 ? 7.90760   -7.89638  11.39985  1.000 90.72670  ?  142 SER A C   1 
ATOM 1027 O O   . SER A 1 142 ? 8.62428   -7.98450  12.40236  1.000 108.10745 ?  142 SER A O   1 
ATOM 1028 C CB  . SER A 1 142 ? 5.84995   -6.50010  11.63180  1.000 100.88317 ?  142 SER A CB  1 
ATOM 1029 O OG  . SER A 1 142 ? 5.21697   -7.76676  11.57677  1.000 102.96841 ?  142 SER A OG  1 
ATOM 1030 N N   . LYS A 1 143 ? 7.66596   -8.94336  10.60941  1.000 98.74389  ?  143 LYS A N   1 
ATOM 1031 C CA  . LYS A 1 143 ? 8.15612   -10.27664 10.94648  1.000 102.73923 ?  143 LYS A CA  1 
ATOM 1032 C C   . LYS A 1 143 ? 9.55931   -10.56199 10.41544  1.000 104.08811 ?  143 LYS A C   1 
ATOM 1033 O O   . LYS A 1 143 ? 9.89053   -11.72994 10.16989  1.000 99.31446  ?  143 LYS A O   1 
ATOM 1034 C CB  . LYS A 1 143 ? 7.17488   -11.33661 10.44337  1.000 95.72104  ?  143 LYS A CB  1 
ATOM 1035 C CG  . LYS A 1 143 ? 5.76669   -11.15678 10.96199  1.000 101.32199 ?  143 LYS A CG  1 
ATOM 1036 C CD  . LYS A 1 143 ? 5.59835   -11.85979 12.29734  1.000 115.14439 ?  143 LYS A CD  1 
ATOM 1037 C CE  . LYS A 1 143 ? 5.25246   -10.86973 13.40262  1.000 112.95091 ?  143 LYS A CE  1 
ATOM 1038 N NZ  . LYS A 1 143 ? 4.73007   -11.55936 14.61031  1.000 104.70378 ?  143 LYS A NZ  1 
ATOM 1039 N N   . LEU A 1 144 ? 10.41411  -9.54791  10.28221  1.000 113.16469 ?  144 LEU A N   1 
ATOM 1040 C CA  . LEU A 1 144 ? 11.69569  -9.70409  9.60038   1.000 127.62798 ?  144 LEU A CA  1 
ATOM 1041 C C   . LEU A 1 144 ? 12.83770  -9.24894  10.49810  1.000 130.53333 ?  144 LEU A C   1 
ATOM 1042 O O   . LEU A 1 144 ? 12.75160  -8.19615  11.13890  1.000 126.20511 ?  144 LEU A O   1 
ATOM 1043 C CB  . LEU A 1 144 ? 11.73690  -8.91912  8.27686   1.000 112.70345 ?  144 LEU A CB  1 
ATOM 1044 C CG  . LEU A 1 144 ? 11.00167  -9.49584  7.05882   1.000 106.65070 ?  144 LEU A CG  1 
ATOM 1045 C CD1 . LEU A 1 144 ? 11.39793  -8.76432  5.76713   1.000 89.91889  ?  144 LEU A CD1 1 
ATOM 1046 C CD2 . LEU A 1 144 ? 11.19966  -11.00714 6.93609   1.000 96.68293  ?  144 LEU A CD2 1 
ATOM 1047 N N   . GLU A 1 145 ? 13.90061  -10.05021 10.54470  1.000 142.80959 ?  145 GLU A N   1 
ATOM 1048 C CA  . GLU A 1 145 ? 15.12403  -9.63254  11.21316  1.000 147.49720 ?  145 GLU A CA  1 
ATOM 1049 C C   . GLU A 1 145 ? 15.81214  -8.52938  10.42303  1.000 153.37417 ?  145 GLU A C   1 
ATOM 1050 O O   . GLU A 1 145 ? 15.92874  -8.60049  9.19635   1.000 149.79357 ?  145 GLU A O   1 
ATOM 1051 C CB  . GLU A 1 145 ? 16.08170  -10.81409 11.38612  1.000 144.51343 ?  145 GLU A CB  1 
ATOM 1052 C CG  . GLU A 1 145 ? 15.59114  -11.89808 12.33762  1.000 164.84826 ?  145 GLU A CG  1 
ATOM 1053 C CD  . GLU A 1 145 ? 14.66956  -12.90604 11.67991  1.000 165.14097 ?  145 GLU A CD  1 
ATOM 1054 O OE1 . GLU A 1 145 ? 14.41724  -12.78578 10.45903  1.000 150.60374 ?  145 GLU A OE1 1 
ATOM 1055 O OE2 . GLU A 1 145 ? 14.19056  -13.81333 12.39771  1.000 149.78299 -1 145 GLU A OE2 1 
ATOM 1056 N N   . ASN A 1 146 ? 16.28188  -7.51218  11.14158  1.000 191.77796 ?  146 ASN A N   1 
ATOM 1057 C CA  . ASN A 1 146 ? 16.97600  -6.37452  10.54388  1.000 193.21174 ?  146 ASN A CA  1 
ATOM 1058 C C   . ASN A 1 146 ? 16.16743  -5.74704  9.40815   1.000 189.56221 ?  146 ASN A C   1 
ATOM 1059 O O   . ASN A 1 146 ? 16.65319  -5.55666  8.28911   1.000 187.17043 ?  146 ASN A O   1 
ATOM 1060 C CB  . ASN A 1 146 ? 18.37307  -6.77959  10.08060  1.000 199.72176 ?  146 ASN A CB  1 
ATOM 1061 C CG  . ASN A 1 146 ? 19.36078  -5.64629  10.18845  1.000 201.99019 ?  146 ASN A CG  1 
ATOM 1062 O OD1 . ASN A 1 146 ? 19.28082  -4.68010  9.42786   1.000 201.24709 ?  146 ASN A OD1 1 
ATOM 1063 N ND2 . ASN A 1 146 ? 20.27540  -5.73187  11.16102  1.000 208.38784 ?  146 ASN A ND2 1 
ATOM 1064 N N   . ASN A 1 147 ? 14.90719  -5.42281  9.71598   1.000 130.50270 ?  147 ASN A N   1 
ATOM 1065 C CA  . ASN A 1 147 ? 14.02488  -4.80032  8.73724   1.000 120.96897 ?  147 ASN A CA  1 
ATOM 1066 C C   . ASN A 1 147 ? 14.36140  -3.33321  8.50832   1.000 118.52569 ?  147 ASN A C   1 
ATOM 1067 O O   . ASN A 1 147 ? 13.88744  -2.75750  7.52179   1.000 123.37746 ?  147 ASN A O   1 
ATOM 1068 C CB  . ASN A 1 147 ? 12.55482  -4.93406  9.15780   1.000 96.78421  ?  147 ASN A CB  1 
ATOM 1069 C CG  . ASN A 1 147 ? 12.30130  -4.48925  10.59112  1.000 122.75582 ?  147 ASN A CG  1 
ATOM 1070 O OD1 . ASN A 1 147 ? 12.54119  -3.33743  10.94835  1.000 124.28820 ?  147 ASN A OD1 1 
ATOM 1071 N ND2 . ASN A 1 147 ? 11.80019  -5.40154  11.41559  1.000 134.78968 ?  147 ASN A ND2 1 
ATOM 1072 N N   . GLU A 1 148 ? 15.16477  -2.72295  9.39004   1.000 106.41802 ?  148 GLU A N   1 
ATOM 1073 C CA  . GLU A 1 148 ? 15.52678  -1.31428  9.23651   1.000 101.12521 ?  148 GLU A CA  1 
ATOM 1074 C C   . GLU A 1 148 ? 16.03411  -1.00936  7.83443   1.000 109.81574 ?  148 GLU A C   1 
ATOM 1075 O O   . GLU A 1 148 ? 15.56795  -0.05870  7.19244   1.000 108.85409 ?  148 GLU A O   1 
ATOM 1076 C CB  . GLU A 1 148 ? 16.57471  -0.91375  10.27751  1.000 113.69345 ?  148 GLU A CB  1 
ATOM 1077 C CG  . GLU A 1 148 ? 17.79458  -1.82585  10.36694  1.000 118.68633 ?  148 GLU A CG  1 
ATOM 1078 C CD  . GLU A 1 148 ? 17.60968  -2.93908  11.38248  1.000 157.32084 ?  148 GLU A CD  1 
ATOM 1079 O OE1 . GLU A 1 148 ? 16.45312  -3.35264  11.60670  1.000 152.42791 ?  148 GLU A OE1 1 
ATOM 1080 O OE2 . GLU A 1 148 ? 18.61798  -3.39280  11.96721  1.000 176.98151 -1 148 GLU A OE2 1 
ATOM 1081 N N   . LYS A 1 149 ? 16.94798  -1.84285  7.32180   1.000 117.43555 ?  149 LYS A N   1 
ATOM 1082 C CA  . LYS A 1 149 ? 17.42751  -1.68300  5.95342   1.000 110.99102 ?  149 LYS A CA  1 
ATOM 1083 C C   . LYS A 1 149 ? 16.25022  -1.55692  5.00232   1.000 112.29171 ?  149 LYS A C   1 
ATOM 1084 O O   . LYS A 1 149 ? 16.04554  -0.51364  4.36570   1.000 116.89775 ?  149 LYS A O   1 
ATOM 1085 C CB  . LYS A 1 149 ? 18.28571  -2.88323  5.54239   1.000 114.29417 ?  149 LYS A CB  1 
ATOM 1086 C CG  . LYS A 1 149 ? 19.49473  -3.16866  6.40360   1.000 133.51430 ?  149 LYS A CG  1 
ATOM 1087 C CD  . LYS A 1 149 ? 20.15588  -4.47893  5.97351   1.000 132.89356 ?  149 LYS A CD  1 
ATOM 1088 C CE  . LYS A 1 149 ? 21.40547  -4.24062  5.12169   1.000 133.66712 ?  149 LYS A CE  1 
ATOM 1089 N NZ  . LYS A 1 149 ? 21.13268  -3.57053  3.81492   1.000 106.92386 ?  149 LYS A NZ  1 
ATOM 1090 N N   . ILE A 1 150 ? 15.39926  -2.58455  4.99384   1.000 98.93276  ?  150 ILE A N   1 
ATOM 1091 C CA  . ILE A 1 150 ? 14.25876  -2.60119  4.09109   1.000 90.66791  ?  150 ILE A CA  1 
ATOM 1092 C C   . ILE A 1 150 ? 13.43182  -1.33865  4.27795   1.000 94.71444  ?  150 ILE A C   1 
ATOM 1093 O O   . ILE A 1 150 ? 13.10884  -0.64008  3.30539   1.000 102.41016 ?  150 ILE A O   1 
ATOM 1094 C CB  . ILE A 1 150 ? 13.42483  -3.88004  4.32489   1.000 93.64609  ?  150 ILE A CB  1 
ATOM 1095 C CG1 . ILE A 1 150 ? 14.23318  -5.14310  3.98940   1.000 97.45918  ?  150 ILE A CG1 1 
ATOM 1096 C CG2 . ILE A 1 150 ? 12.12282  -3.84751  3.54321   1.000 89.66127  ?  150 ILE A CG2 1 
ATOM 1097 C CD1 . ILE A 1 150 ? 15.04580  -5.71358  5.14555   1.000 108.96953 ?  150 ILE A CD1 1 
ATOM 1098 N N   . ILE A 1 151 ? 13.19980  -0.95071  5.53457   1.000 106.96768 ?  151 ILE A N   1 
ATOM 1099 C CA  . ILE A 1 151 ? 12.31423  0.17909   5.80158   1.000 112.78111 ?  151 ILE A CA  1 
ATOM 1100 C C   . ILE A 1 151 ? 12.88550  1.44833   5.18577   1.000 93.54245  ?  151 ILE A C   1 
ATOM 1101 O O   . ILE A 1 151 ? 12.17788  2.20322   4.50461   1.000 98.07896  ?  151 ILE A O   1 
ATOM 1102 C CB  . ILE A 1 151 ? 12.06725  0.32826   7.31633   1.000 102.16954 ?  151 ILE A CB  1 
ATOM 1103 C CG1 . ILE A 1 151 ? 11.39970  -0.92814  7.87486   1.000 89.82834  ?  151 ILE A CG1 1 
ATOM 1104 C CG2 . ILE A 1 151 ? 11.19649  1.53332   7.61014   1.000 99.29251  ?  151 ILE A CG2 1 
ATOM 1105 C CD1 . ILE A 1 151 ? 11.31311  -0.94135  9.36939   1.000 106.83040 ?  151 ILE A CD1 1 
ATOM 1106 N N   . GLU A 1 152 ? 14.19231  1.66364   5.35579   1.000 108.24142 ?  152 GLU A N   1 
ATOM 1107 C CA  . GLU A 1 152 ? 14.81305  2.84323   4.76478   1.000 119.05023 ?  152 GLU A CA  1 
ATOM 1108 C C   . GLU A 1 152 ? 14.56791  2.89708   3.26217   1.000 106.85084 ?  152 GLU A C   1 
ATOM 1109 O O   . GLU A 1 152 ? 14.16184  3.94141   2.73122   1.000 102.09679 ?  152 GLU A O   1 
ATOM 1110 C CB  . GLU A 1 152 ? 16.30664  2.86447   5.09147   1.000 120.42910 ?  152 GLU A CB  1 
ATOM 1111 C CG  . GLU A 1 152 ? 16.59603  2.99917   6.57945   1.000 119.25503 ?  152 GLU A CG  1 
ATOM 1112 C CD  . GLU A 1 152 ? 17.99792  2.56098   6.94715   1.000 134.88998 ?  152 GLU A CD  1 
ATOM 1113 O OE1 . GLU A 1 152 ? 18.57982  1.74727   6.19842   1.000 130.99995 ?  152 GLU A OE1 1 
ATOM 1114 O OE2 . GLU A 1 152 ? 18.52554  3.04746   7.97288   1.000 137.11170 -1 152 GLU A OE2 1 
ATOM 1115 N N   . SER A 1 153 ? 14.72743  1.76156   2.57339   1.000 105.87015 ?  153 SER A N   1 
ATOM 1116 C CA  . SER A 1 153 ? 14.48449  1.75110   1.13684   1.000 102.91936 ?  153 SER A CA  1 
ATOM 1117 C C   . SER A 1 153 ? 13.09334  2.27934   0.82502   1.000 98.50289  ?  153 SER A C   1 
ATOM 1118 O O   . SER A 1 153 ? 12.94626  3.24591   0.06447   1.000 99.01316  ?  153 SER A O   1 
ATOM 1119 C CB  . SER A 1 153 ? 14.66553  0.33983   0.57131   1.000 106.52542 ?  153 SER A CB  1 
ATOM 1120 O OG  . SER A 1 153 ? 16.03817  0.00844   0.44726   1.000 105.58924 ?  153 SER A OG  1 
ATOM 1121 N N   . ILE A 1 154 ? 12.07232  1.74516   1.50910   1.000 85.09526  ?  154 ILE A N   1 
ATOM 1122 C CA  . ILE A 1 154 ? 10.70009  2.12806   1.18210   1.000 88.12310  ?  154 ILE A CA  1 
ATOM 1123 C C   . ILE A 1 154 ? 10.52096  3.63139   1.34340   1.000 103.46533 ?  154 ILE A C   1 
ATOM 1124 O O   . ILE A 1 154 ? 9.79170   4.27264   0.57398   1.000 101.68181 ?  154 ILE A O   1 
ATOM 1125 C CB  . ILE A 1 154 ? 9.69229   1.33234   2.03113   1.000 82.44400  ?  154 ILE A CB  1 
ATOM 1126 C CG1 . ILE A 1 154 ? 9.60765   -0.10772  1.54429   1.000 82.44543  ?  154 ILE A CG1 1 
ATOM 1127 C CG2 . ILE A 1 154 ? 8.31112   1.95132   1.96572   1.000 80.09354  ?  154 ILE A CG2 1 
ATOM 1128 C CD1 . ILE A 1 154 ? 9.26667   -1.08358  2.64376   1.000 88.72849  ?  154 ILE A CD1 1 
ATOM 1129 N N   . TYR A 1 155 ? 11.18723  4.22200   2.33958   1.000 113.94974 ?  155 TYR A N   1 
ATOM 1130 C CA  . TYR A 1 155 ? 11.02748  5.65669   2.53222   1.000 114.41341 ?  155 TYR A CA  1 
ATOM 1131 C C   . TYR A 1 155 ? 11.87013  6.44690   1.54021   1.000 116.37096 ?  155 TYR A C   1 
ATOM 1132 O O   . TYR A 1 155 ? 11.38568  7.42472   0.95643   1.000 117.01217 ?  155 TYR A O   1 
ATOM 1133 C CB  . TYR A 1 155 ? 11.38713  6.05803   3.96577   1.000 118.02442 ?  155 TYR A CB  1 
ATOM 1134 C CG  . TYR A 1 155 ? 11.34354  7.55728   4.18891   1.000 120.33872 ?  155 TYR A CG  1 
ATOM 1135 C CD1 . TYR A 1 155 ? 10.13868  8.21837   4.39290   1.000 119.83566 ?  155 TYR A CD1 1 
ATOM 1136 C CD2 . TYR A 1 155 ? 12.50655  8.31570   4.16448   1.000 126.34112 ?  155 TYR A CD2 1 
ATOM 1137 C CE1 . TYR A 1 155 ? 10.09752  9.59053   4.58769   1.000 123.63836 ?  155 TYR A CE1 1 
ATOM 1138 C CE2 . TYR A 1 155 ? 12.47554  9.68748   4.35711   1.000 130.94315 ?  155 TYR A CE2 1 
ATOM 1139 C CZ  . TYR A 1 155 ? 11.26996  10.31943  4.56786   1.000 131.92329 ?  155 TYR A CZ  1 
ATOM 1140 O OH  . TYR A 1 155 ? 11.23912  11.68251  4.76081   1.000 136.54871 ?  155 TYR A OH  1 
ATOM 1141 N N   . ILE A 1 156 ? 13.11501  6.01669   1.30138   1.000 118.13595 ?  156 ILE A N   1 
ATOM 1142 C CA  . ILE A 1 156 ? 13.97440  6.78755   0.40555   1.000 101.19804 ?  156 ILE A CA  1 
ATOM 1143 C C   . ILE A 1 156 ? 13.49517  6.66223   -1.03786  1.000 110.91259 ?  156 ILE A C   1 
ATOM 1144 O O   . ILE A 1 156 ? 13.69106  7.57727   -1.84957  1.000 102.48926 ?  156 ILE A O   1 
ATOM 1145 C CB  . ILE A 1 156 ? 15.44873  6.37439   0.57010   1.000 83.10282  ?  156 ILE A CB  1 
ATOM 1146 C CG1 . ILE A 1 156 ? 16.35300  7.41346   -0.08096  1.000 84.35827  ?  156 ILE A CG1 1 
ATOM 1147 C CG2 . ILE A 1 156 ? 15.71967  5.02021   -0.04798  1.000 108.05061 ?  156 ILE A CG2 1 
ATOM 1148 C CD1 . ILE A 1 156 ? 16.04860  8.82442   0.35713   1.000 104.40291 ?  156 ILE A CD1 1 
ATOM 1149 N N   . SER A 1 157 ? 12.83568  5.55266   -1.37445  1.000 100.57953 ?  157 SER A N   1 
ATOM 1150 C CA  . SER A 1 157 ? 12.23477  5.39242   -2.68701  1.000 88.09568  ?  157 SER A CA  1 
ATOM 1151 C C   . SER A 1 157 ? 10.96066  6.20868   -2.85125  1.000 90.40721  ?  157 SER A C   1 
ATOM 1152 O O   . SER A 1 157 ? 10.34508  6.12717   -3.91808  1.000 109.53793 ?  157 SER A O   1 
ATOM 1153 C CB  . SER A 1 157 ? 11.94896  3.91107   -2.96309  1.000 77.42844  ?  157 SER A CB  1 
ATOM 1154 O OG  . SER A 1 157 ? 10.87771  3.43482   -2.17535  1.000 90.47348  ?  157 SER A OG  1 
ATOM 1155 N N   . SER A 1 158 ? 10.53730  6.97725   -1.84197  1.000 89.61586  ?  158 SER A N   1 
ATOM 1156 C CA  . SER A 1 158 ? 9.33426   7.79971   -1.96295  1.000 99.14526  ?  158 SER A CA  1 
ATOM 1157 C C   . SER A 1 158 ? 9.58649   9.26600   -2.33504  1.000 101.33339 ?  158 SER A C   1 
ATOM 1158 O O   . SER A 1 158 ? 8.62618   9.96322   -2.68952  1.000 108.84212 ?  158 SER A O   1 
ATOM 1159 C CB  . SER A 1 158 ? 8.52015   7.72650   -0.65975  1.000 112.53465 ?  158 SER A CB  1 
ATOM 1160 O OG  . SER A 1 158 ? 9.13770   8.42447   0.41273   1.000 97.13177  ?  158 SER A OG  1 
ATOM 1161 N N   . VAL A 1 159 ? 10.84421  9.74447   -2.28960  1.000 84.34455  ?  159 VAL A N   1 
ATOM 1162 C CA  . VAL A 1 159 ? 11.19216  11.12910  -2.61987  1.000 88.81995  ?  159 VAL A CA  1 
ATOM 1163 C C   . VAL A 1 159 ? 11.23264  11.33097  -4.13902  1.000 108.44518 ?  159 VAL A C   1 
ATOM 1164 O O   . VAL A 1 159 ? 11.44055  10.37665  -4.90749  1.000 105.23668 ?  159 VAL A O   1 
ATOM 1165 C CB  . VAL A 1 159 ? 12.53605  11.51181  -1.97093  1.000 83.23291  ?  159 VAL A CB  1 
ATOM 1166 C CG1 . VAL A 1 159 ? 12.86424  12.95955  -2.25869  1.000 109.91901 ?  159 VAL A CG1 1 
ATOM 1167 C CG2 . VAL A 1 159 ? 12.52332  11.23248  -0.47617  1.000 110.94657 ?  159 VAL A CG2 1 
ATOM 1168 N N   . SER A 1 160 ? 10.93578  12.57872  -4.57554  1.000 107.33518 ?  160 SER A N   1 
ATOM 1169 C CA  . SER A 1 160 ? 10.90359  12.99958  -5.98496  1.000 110.40684 ?  160 SER A CA  1 
ATOM 1170 C C   . SER A 1 160 ? 12.14308  13.81220  -6.38528  1.000 110.01888 ?  160 SER A C   1 
ATOM 1171 O O   . SER A 1 160 ? 12.43127  14.88439  -5.81177  1.000 116.03414 ?  160 SER A O   1 
ATOM 1172 C CB  . SER A 1 160 ? 9.58824   13.73932  -6.27723  1.000 104.13019 ?  160 SER A CB  1 
ATOM 1173 O OG  . SER A 1 160 ? 9.67137   14.63723  -7.37293  1.000 133.63516 ?  160 SER A OG  1 
ATOM 1174 N N   . PHE A 1 161 ? 12.88964  13.25010  -7.35488  1.000 95.31888  ?  161 PHE A N   1 
ATOM 1175 C CA  . PHE A 1 161 ? 14.13246  13.76119  -7.91521  1.000 98.08587  ?  161 PHE A CA  1 
ATOM 1176 C C   . PHE A 1 161 ? 13.87942  14.41342  -9.29009  1.000 117.27097 ?  161 PHE A C   1 
ATOM 1177 O O   . PHE A 1 161 ? 12.76822  14.45938  -9.81464  1.000 117.67512 ?  161 PHE A O   1 
ATOM 1178 C CB  . PHE A 1 161 ? 15.15251  12.60769  -7.94146  1.000 108.14039 ?  161 PHE A CB  1 
ATOM 1179 C CG  . PHE A 1 161 ? 15.22884  11.79251  -6.62347  1.000 81.60558  ?  161 PHE A CG  1 
ATOM 1180 C CD1 . PHE A 1 161 ? 15.91622  12.26565  -5.50972  1.000 88.83491  ?  161 PHE A CD1 1 
ATOM 1181 C CD2 . PHE A 1 161 ? 14.60408  10.54700  -6.50297  1.000 88.65108  ?  161 PHE A CD2 1 
ATOM 1182 C CE1 . PHE A 1 161 ? 16.01636  11.49369  -4.28897  1.000 93.04929  ?  161 PHE A CE1 1 
ATOM 1183 C CE2 . PHE A 1 161 ? 14.68465  9.75329   -5.25987  1.000 96.85880  ?  161 PHE A CE2 1 
ATOM 1184 C CZ  . PHE A 1 161 ? 15.40088  10.24871  -4.15736  1.000 104.55843 ?  161 PHE A CZ  1 
ATOM 1185 N N   . PHE A 1 162 ? 14.95511  14.95292  -9.88877  1.000 120.47923 ?  162 PHE A N   1 
ATOM 1186 C CA  . PHE A 1 162 ? 14.86643  15.50382  -11.22579 1.000 111.02380 ?  162 PHE A CA  1 
ATOM 1187 C C   . PHE A 1 162 ? 14.47833  14.42634  -12.17057 1.000 108.75476 ?  162 PHE A C   1 
ATOM 1188 O O   . PHE A 1 162 ? 13.49531  14.58713  -12.88877 1.000 104.72209 ?  162 PHE A O   1 
ATOM 1189 C CB  . PHE A 1 162 ? 16.18319  16.13108  -11.65183 1.000 135.02727 ?  162 PHE A CB  1 
ATOM 1190 C CG  . PHE A 1 162 ? 16.09639  16.90562  -12.87062 1.000 139.82645 ?  162 PHE A CG  1 
ATOM 1191 C CD1 . PHE A 1 162 ? 14.99712  17.66966  -13.15349 1.000 124.57405 ?  162 PHE A CD1 1 
ATOM 1192 C CD2 . PHE A 1 162 ? 17.16104  16.97309  -13.69400 1.000 138.30609 ?  162 PHE A CD2 1 
ATOM 1193 C CE1 . PHE A 1 162 ? 14.93355  18.41963  -14.31258 1.000 128.24525 ?  162 PHE A CE1 1 
ATOM 1194 C CE2 . PHE A 1 162 ? 17.12661  17.77131  -14.83555 1.000 132.45587 ?  162 PHE A CE2 1 
ATOM 1195 C CZ  . PHE A 1 162 ? 16.01555  18.48354  -15.16297 1.000 138.29817 ?  162 PHE A CZ  1 
ATOM 1196 N N   . SER A 1 163 ? 15.12194  13.25546  -12.05314 1.000 107.90560 ?  163 SER A N   1 
ATOM 1197 C CA  . SER A 1 163 ? 14.80297  12.11189  -12.89042 1.000 119.80777 ?  163 SER A CA  1 
ATOM 1198 C C   . SER A 1 163 ? 13.31806  11.78286  -12.83557 1.000 106.74141 ?  163 SER A C   1 
ATOM 1199 O O   . SER A 1 163 ? 12.72225  11.48968  -13.86870 1.000 104.43628 ?  163 SER A O   1 
ATOM 1200 C CB  . SER A 1 163 ? 15.65342  10.89912  -12.51387 1.000 133.09750 ?  163 SER A CB  1 
ATOM 1201 O OG  . SER A 1 163 ? 15.54867  10.50009  -11.13459 1.000 114.04780 ?  163 SER A OG  1 
ATOM 1202 N N   . ASP A 1 164 ? 12.67658  12.02984  -11.68241 1.000 95.15750  ?  164 ASP A N   1 
ATOM 1203 C CA  . ASP A 1 164 ? 11.24046  11.77071  -11.55851 1.000 88.95565  ?  164 ASP A CA  1 
ATOM 1204 C C   . ASP A 1 164 ? 10.36980  12.83633  -12.23089 1.000 98.90018  ?  164 ASP A C   1 
ATOM 1205 O O   . ASP A 1 164 ? 9.41506   12.50331  -12.94667 1.000 103.82284 ?  164 ASP A O   1 
ATOM 1206 C CB  . ASP A 1 164 ? 10.88610  11.60870  -10.08728 1.000 101.58485 ?  164 ASP A CB  1 
ATOM 1207 C CG  . ASP A 1 164 ? 11.52259  10.38407  -9.49216  1.000 102.71855 ?  164 ASP A CG  1 
ATOM 1208 O OD1 . ASP A 1 164 ? 11.58240  9.35802   -10.20399 1.000 110.53185 ?  164 ASP A OD1 1 
ATOM 1209 O OD2 . ASP A 1 164 ? 11.97762  10.43091  -8.33015  1.000 91.81353  -1 164 ASP A OD2 1 
ATOM 1210 N N   . LYS A 1 165 ? 10.68337  14.12302  -12.03267 1.000 95.73450  ?  165 LYS A N   1 
ATOM 1211 C CA  . LYS A 1 165 ? 9.86474   15.15357  -12.67362 1.000 84.69428  ?  165 LYS A CA  1 
ATOM 1212 C C   . LYS A 1 165 ? 10.04537  15.14684  -14.18816 1.000 92.69042  ?  165 LYS A C   1 
ATOM 1213 O O   . LYS A 1 165 ? 9.06215   15.22874  -14.94040 1.000 85.25851  ?  165 LYS A O   1 
ATOM 1214 C CB  . LYS A 1 165 ? 10.15649  16.54269  -12.09301 1.000 96.93671  ?  165 LYS A CB  1 
ATOM 1215 C CG  . LYS A 1 165 ? 9.74032   16.71992  -10.63264 1.000 113.12954 ?  165 LYS A CG  1 
ATOM 1216 C CD  . LYS A 1 165 ? 9.79322   18.18781  -10.21309 1.000 123.54501 ?  165 LYS A CD  1 
ATOM 1217 C CE  . LYS A 1 165 ? 9.49295   18.39089  -8.73436  1.000 118.20051 ?  165 LYS A CE  1 
ATOM 1218 N NZ  . LYS A 1 165 ? 9.96003   17.25569  -7.90050  1.000 127.40085 ?  165 LYS A NZ  1 
ATOM 1219 N N   . VAL A 1 166 ? 11.29883  15.07480  -14.65016 1.000 96.52141  ?  166 VAL A N   1 
ATOM 1220 C CA  . VAL A 1 166 ? 11.57989  14.91807  -16.07588 1.000 86.36187  ?  166 VAL A CA  1 
ATOM 1221 C C   . VAL A 1 166 ? 10.85931  13.70440  -16.63381 1.000 84.07390  ?  166 VAL A C   1 
ATOM 1222 O O   . VAL A 1 166 ? 10.25486  13.76849  -17.70722 1.000 89.65963  ?  166 VAL A O   1 
ATOM 1223 C CB  . VAL A 1 166 ? 13.09518  14.81004  -16.31733 1.000 91.61924  ?  166 VAL A CB  1 
ATOM 1224 C CG1 . VAL A 1 166 ? 13.38396  14.49067  -17.75735 1.000 77.45396  ?  166 VAL A CG1 1 
ATOM 1225 C CG2 . VAL A 1 166 ? 13.72517  16.08606  -16.01590 1.000 87.52615  ?  166 VAL A CG2 1 
ATOM 1226 N N   . ARG A 1 167 ? 10.94893  12.56609  -15.93684 1.000 83.99649  ?  167 ARG A N   1 
ATOM 1227 C CA  . ARG A 1 167 ? 10.26532  11.36525  -16.39734 1.000 82.66015  ?  167 ARG A CA  1 
ATOM 1228 C C   . ARG A 1 167 ? 8.76201   11.58296  -16.51189 1.000 85.99436  ?  167 ARG A C   1 
ATOM 1229 O O   . ARG A 1 167 ? 8.13996   11.09277  -17.45338 1.000 94.43830  ?  167 ARG A O   1 
ATOM 1230 C CB  . ARG A 1 167 ? 10.59732  10.18310  -15.48875 1.000 80.94941  ?  167 ARG A CB  1 
ATOM 1231 C CG  . ARG A 1 167 ? 11.87824  9.47867   -15.90647 1.000 76.43990  ?  167 ARG A CG  1 
ATOM 1232 C CD  . ARG A 1 167 ? 12.16411  8.23384   -15.09097 1.000 73.32402  ?  167 ARG A CD  1 
ATOM 1233 N NE  . ARG A 1 167 ? 12.37431  8.49070   -13.67025 1.000 97.83733  ?  167 ARG A NE  1 
ATOM 1234 C CZ  . ARG A 1 167 ? 13.52149  8.30648   -13.02964 1.000 98.41887  ?  167 ARG A CZ  1 
ATOM 1235 N NH1 . ARG A 1 167 ? 14.60006  7.86103   -13.65271 1.000 89.44211  ?  167 ARG A NH1 1 
ATOM 1236 N NH2 . ARG A 1 167 ? 13.57521  8.52930   -11.71939 1.000 112.72325 ?  167 ARG A NH2 1 
ATOM 1237 N N   . ASN A 1 168 ? 8.14663   12.26972  -15.54814 1.000 93.21561  ?  168 ASN A N   1 
ATOM 1238 C CA  . ASN A 1 168 ? 6.71207   12.53759  -15.65692 1.000 97.78060  ?  168 ASN A CA  1 
ATOM 1239 C C   . ASN A 1 168 ? 6.39505   13.37794  -16.89185 1.000 102.72189 ?  168 ASN A C   1 
ATOM 1240 O O   . ASN A 1 168 ? 5.49513   13.04557  -17.68539 1.000 104.98199 ?  168 ASN A O   1 
ATOM 1241 C CB  . ASN A 1 168 ? 6.21472   13.24379  -14.39748 1.000 107.03533 ?  168 ASN A CB  1 
ATOM 1242 C CG  . ASN A 1 168 ? 4.82581   13.83793  -14.57215 1.000 121.19210 ?  168 ASN A CG  1 
ATOM 1243 O OD1 . ASN A 1 168 ? 4.68023   15.02244  -14.88389 1.000 126.50668 ?  168 ASN A OD1 1 
ATOM 1244 N ND2 . ASN A 1 168 ? 3.79991   13.01825  -14.37602 1.000 119.25157 ?  168 ASN A ND2 1 
ATOM 1245 N N   . LEU A 1 169 ? 7.12880   14.47841  -17.06550 1.000 101.69299 ?  169 LEU A N   1 
ATOM 1246 C CA  . LEU A 1 169 ? 6.92264   15.33605  -18.22905 1.000 95.28032  ?  169 LEU A CA  1 
ATOM 1247 C C   . LEU A 1 169 ? 7.06565   14.55172  -19.53213 1.000 86.04642  ?  169 LEU A C   1 
ATOM 1248 O O   . LEU A 1 169 ? 6.24240   14.68406  -20.44307 1.000 87.87078  ?  169 LEU A O   1 
ATOM 1249 C CB  . LEU A 1 169 ? 7.89854   16.50992  -18.18461 1.000 98.03356  ?  169 LEU A CB  1 
ATOM 1250 C CG  . LEU A 1 169 ? 7.87461   17.44711  -19.38789 1.000 95.52305  ?  169 LEU A CG  1 
ATOM 1251 C CD1 . LEU A 1 169 ? 6.49711   18.07279  -19.55159 1.000 86.03273  ?  169 LEU A CD1 1 
ATOM 1252 C CD2 . LEU A 1 169 ? 8.94301   18.51247  -19.21638 1.000 93.51582  ?  169 LEU A CD2 1 
ATOM 1253 N N   . ILE A 1 170 ? 8.11366   13.73380  -19.64024 1.000 88.22638  ?  170 ILE A N   1 
ATOM 1254 C CA  . ILE A 1 170 ? 8.33281   12.95629  -20.85587 1.000 82.98720  ?  170 ILE A CA  1 
ATOM 1255 C C   . ILE A 1 170 ? 7.26599   11.87559  -21.01636 1.000 87.41157  ?  170 ILE A C   1 
ATOM 1256 O O   . ILE A 1 170 ? 6.87691   11.53680  -22.14004 1.000 102.30887 ?  170 ILE A O   1 
ATOM 1257 C CB  . ILE A 1 170 ? 9.76049   12.37247  -20.86093 1.000 80.57499  ?  170 ILE A CB  1 
ATOM 1258 C CG1 . ILE A 1 170 ? 10.79768  13.48890  -20.71050 1.000 65.76442  ?  170 ILE A CG1 1 
ATOM 1259 C CG2 . ILE A 1 170 ? 10.03483  11.60899  -22.13678 1.000 91.50043  ?  170 ILE A CG2 1 
ATOM 1260 C CD1 . ILE A 1 170 ? 12.21469  13.02006  -20.87905 1.000 59.04606  ?  170 ILE A CD1 1 
ATOM 1261 N N   . GLU A 1 171 ? 6.79148   11.29839  -19.90867 1.000 70.51923  ?  171 GLU A N   1 
ATOM 1262 C CA  . GLU A 1 171 ? 5.73562   10.29269  -19.98688 1.000 85.83787  ?  171 GLU A CA  1 
ATOM 1263 C C   . GLU A 1 171 ? 4.43615   10.87798  -20.50401 1.000 98.78749  ?  171 GLU A C   1 
ATOM 1264 O O   . GLU A 1 171 ? 3.57072   10.13628  -20.98754 1.000 90.59203  ?  171 GLU A O   1 
ATOM 1265 C CB  . GLU A 1 171 ? 5.50156   9.64257   -18.62690 1.000 100.05673 ?  171 GLU A CB  1 
ATOM 1266 C CG  . GLU A 1 171 ? 6.08668   8.24976   -18.50647 1.000 112.02949 ?  171 GLU A CG  1 
ATOM 1267 C CD  . GLU A 1 171 ? 5.85165   7.64241   -17.13867 1.000 135.19777 ?  171 GLU A CD  1 
ATOM 1268 O OE1 . GLU A 1 171 ? 6.66356   7.89972   -16.22235 1.000 118.79998 ?  171 GLU A OE1 1 
ATOM 1269 O OE2 . GLU A 1 171 ? 4.84399   6.91817   -16.97961 1.000 156.79161 -1 171 GLU A OE2 1 
ATOM 1270 N N   . LYS A 1 172 ? 4.25674   12.19218  -20.35509 1.000 109.95173 ?  172 LYS A N   1 
ATOM 1271 C CA  . LYS A 1 172 ? 3.08687   12.83187  -20.95529 1.000 89.13246  ?  172 LYS A CA  1 
ATOM 1272 C C   . LYS A 1 172 ? 2.98138   12.53152  -22.45241 1.000 84.00407  ?  172 LYS A C   1 
ATOM 1273 O O   . LYS A 1 172 ? 1.89243   12.22341  -22.94945 1.000 87.80017  ?  172 LYS A O   1 
ATOM 1274 C CB  . LYS A 1 172 ? 3.11927   14.33854  -20.70733 1.000 87.22436  ?  172 LYS A CB  1 
ATOM 1275 C CG  . LYS A 1 172 ? 2.82799   14.72145  -19.26829 1.000 93.83823  ?  172 LYS A CG  1 
ATOM 1276 C CD  . LYS A 1 172 ? 2.93280   16.22538  -19.06203 1.000 122.26153 ?  172 LYS A CD  1 
ATOM 1277 C CE  . LYS A 1 172 ? 2.69743   16.60895  -17.60445 1.000 124.33955 ?  172 LYS A CE  1 
ATOM 1278 N NZ  . LYS A 1 172 ? 2.81112   18.08171  -17.38706 1.000 129.18761 ?  172 LYS A NZ  1 
ATOM 1279 N N   . ASP A 1 173 ? 4.10995   12.59381  -23.19099 1.000 77.23184  ?  173 ASP A N   1 
ATOM 1280 C CA  . ASP A 1 173 ? 4.09592   12.35758  -24.64789 1.000 91.69350  ?  173 ASP A CA  1 
ATOM 1281 C C   . ASP A 1 173 ? 5.43371   11.74330  -25.08320 1.000 96.96638  ?  173 ASP A C   1 
ATOM 1282 O O   . ASP A 1 173 ? 6.30374   12.41596  -25.64278 1.000 96.01504  ?  173 ASP A O   1 
ATOM 1283 C CB  . ASP A 1 173 ? 3.81338   13.64122  -25.42889 1.000 85.76462  ?  173 ASP A CB  1 
ATOM 1284 C CG  . ASP A 1 173 ? 3.45755   13.37519  -26.88325 1.000 108.38394 ?  173 ASP A CG  1 
ATOM 1285 O OD1 . ASP A 1 173 ? 3.40316   12.18894  -27.27803 1.000 118.70074 ?  173 ASP A OD1 1 
ATOM 1286 O OD2 . ASP A 1 173 ? 3.23231   14.35219  -27.63285 1.000 117.14488 -1 173 ASP A OD2 1 
ATOM 1287 N N   . LEU A 1 174 ? 5.57794   10.43420  -24.84142 1.000 99.36014  ?  174 LEU A N   1 
ATOM 1288 C CA  . LEU A 1 174 ? 6.80655   9.71675   -25.18252 1.000 91.97532  ?  174 LEU A CA  1 
ATOM 1289 C C   . LEU A 1 174 ? 7.14880   9.78058   -26.66716 1.000 103.11944 ?  174 LEU A C   1 
ATOM 1290 O O   . LEU A 1 174 ? 8.29602   9.50145   -27.03371 1.000 114.72849 ?  174 LEU A O   1 
ATOM 1291 C CB  . LEU A 1 174 ? 6.70344   8.24467   -24.77374 1.000 94.41296  ?  174 LEU A CB  1 
ATOM 1292 C CG  . LEU A 1 174 ? 7.13220   7.79835   -23.37482 1.000 93.17147  ?  174 LEU A CG  1 
ATOM 1293 C CD1 . LEU A 1 174 ? 7.21624   6.27599   -23.31389 1.000 86.21656  ?  174 LEU A CD1 1 
ATOM 1294 C CD2 . LEU A 1 174 ? 8.44052   8.43200   -22.96117 1.000 91.24077  ?  174 LEU A CD2 1 
ATOM 1295 N N   . SER A 1 175 ? 6.19137   10.11929  -27.53418 1.000 111.98993 ?  175 SER A N   1 
ATOM 1296 C CA  . SER A 1 175 ? 6.44464   10.11960  -28.97180 1.000 106.34408 ?  175 SER A CA  1 
ATOM 1297 C C   . SER A 1 175 ? 7.03491   11.42898  -29.47889 1.000 99.61840  ?  175 SER A C   1 
ATOM 1298 O O   . SER A 1 175 ? 7.55574   11.45808  -30.59757 1.000 107.72923 ?  175 SER A O   1 
ATOM 1299 C CB  . SER A 1 175 ? 5.15058   9.82188   -29.74902 1.000 103.71712 ?  175 SER A CB  1 
ATOM 1300 O OG  . SER A 1 175 ? 4.39457   8.77621   -29.15520 1.000 112.46893 ?  175 SER A OG  1 
ATOM 1301 N N   . ARG A 1 176 ? 7.00742   12.48925  -28.67484 1.000 104.76209 ?  176 ARG A N   1 
ATOM 1302 C CA  . ARG A 1 176 ? 7.47618   13.79917  -29.10436 1.000 109.46100 ?  176 ARG A CA  1 
ATOM 1303 C C   . ARG A 1 176 ? 8.99797   13.80838  -29.25814 1.000 100.20350 ?  176 ARG A C   1 
ATOM 1304 O O   . ARG A 1 176 ? 9.71142   12.96250  -28.71514 1.000 109.92818 ?  176 ARG A O   1 
ATOM 1305 C CB  . ARG A 1 176 ? 7.02108   14.86789  -28.10120 1.000 101.95439 ?  176 ARG A CB  1 
ATOM 1306 C CG  . ARG A 1 176 ? 7.24315   16.32248  -28.51949 1.000 96.67099  ?  176 ARG A CG  1 
ATOM 1307 C CD  . ARG A 1 176 ? 7.88712   17.11939  -27.38287 1.000 97.48925  ?  176 ARG A CD  1 
ATOM 1308 N NE  . ARG A 1 176 ? 6.94683   17.38163  -26.29725 1.000 93.07108  ?  176 ARG A NE  1 
ATOM 1309 C CZ  . ARG A 1 176 ? 6.26761   18.51323  -26.15114 1.000 103.04044 ?  176 ARG A CZ  1 
ATOM 1310 N NH1 . ARG A 1 176 ? 6.43943   19.53373  -26.97675 1.000 107.17852 ?  176 ARG A NH1 1 
ATOM 1311 N NH2 . ARG A 1 176 ? 5.38291   18.61929  -25.16063 1.000 85.64208  ?  176 ARG A NH2 1 
ATOM 1312 N N   . LYS A 1 177 ? 9.48931   14.77151  -30.04071 1.000 97.14003  ?  177 LYS A N   1 
ATOM 1313 C CA  . LYS A 1 177 ? 10.92545  14.97076  -30.23224 1.000 91.88126  ?  177 LYS A CA  1 
ATOM 1314 C C   . LYS A 1 177 ? 11.43303  15.88771  -29.12072 1.000 97.18947  ?  177 LYS A C   1 
ATOM 1315 O O   . LYS A 1 177 ? 11.65336  17.08714  -29.30266 1.000 111.55537 ?  177 LYS A O   1 
ATOM 1316 C CB  . LYS A 1 177 ? 11.20689  15.53980  -31.61838 1.000 101.53611 ?  177 LYS A CB  1 
ATOM 1317 C CG  . LYS A 1 177 ? 10.71642  14.65919  -32.76935 1.000 123.79519 ?  177 LYS A CG  1 
ATOM 1318 C CD  . LYS A 1 177 ? 11.67647  13.50412  -33.06386 1.000 111.31825 ?  177 LYS A CD  1 
ATOM 1319 C CE  . LYS A 1 177 ? 10.94525  12.16240  -33.18265 1.000 112.44461 ?  177 LYS A CE  1 
ATOM 1320 N NZ  . LYS A 1 177 ? 10.72211  11.49725  -31.85894 1.000 123.87215 ?  177 LYS A NZ  1 
ATOM 1321 N N   . TRP A 1 178 ? 11.61581  15.29924  -27.94078 1.000 98.74708  ?  178 TRP A N   1 
ATOM 1322 C CA  . TRP A 1 178 ? 12.11599  16.04845  -26.79594 1.000 95.90783  ?  178 TRP A CA  1 
ATOM 1323 C C   . TRP A 1 178 ? 13.56730  16.46779  -26.98866 1.000 98.72113  ?  178 TRP A C   1 
ATOM 1324 O O   . TRP A 1 178 ? 14.39458  15.70737  -27.50205 1.000 92.40650  ?  178 TRP A O   1 
ATOM 1325 C CB  . TRP A 1 178 ? 12.00559  15.21253  -25.52304 1.000 81.22863  ?  178 TRP A CB  1 
ATOM 1326 C CG  . TRP A 1 178 ? 10.63000  14.86453  -25.14921 1.000 79.06691  ?  178 TRP A CG  1 
ATOM 1327 C CD1 . TRP A 1 178 ? 9.94253   13.74545  -25.50211 1.000 89.51834  ?  178 TRP A CD1 1 
ATOM 1328 C CD2 . TRP A 1 178 ? 9.75311   15.63798  -24.32523 1.000 80.91614  ?  178 TRP A CD2 1 
ATOM 1329 N NE1 . TRP A 1 178 ? 8.68101   13.77599  -24.95374 1.000 104.98393 ?  178 TRP A NE1 1 
ATOM 1330 C CE2 . TRP A 1 178 ? 8.54157   14.92865  -24.22592 1.000 85.75734  ?  178 TRP A CE2 1 
ATOM 1331 C CE3 . TRP A 1 178 ? 9.87337   16.86543  -23.66843 1.000 78.74999  ?  178 TRP A CE3 1 
ATOM 1332 C CZ2 . TRP A 1 178 ? 7.45949   15.40254  -23.49590 1.000 88.55607  ?  178 TRP A CZ2 1 
ATOM 1333 C CZ3 . TRP A 1 178 ? 8.79800   17.33416  -22.94200 1.000 87.27107  ?  178 TRP A CZ3 1 
ATOM 1334 C CH2 . TRP A 1 178 ? 7.60692   16.60472  -22.86023 1.000 90.44319  ?  178 TRP A CH2 1 
ATOM 1335 N N   . THR A 1 179 ? 13.88106  17.67122  -26.51780 1.000 100.04882 ?  179 THR A N   1 
ATOM 1336 C CA  . THR A 1 179 ? 15.23949  18.18350  -26.45915 1.000 93.68135  ?  179 THR A CA  1 
ATOM 1337 C C   . THR A 1 179 ? 15.45195  18.78971  -25.08011 1.000 84.40703  ?  179 THR A C   1 
ATOM 1338 O O   . THR A 1 179 ? 14.52905  18.87460  -24.26720 1.000 93.93370  ?  179 THR A O   1 
ATOM 1339 C CB  . THR A 1 179 ? 15.50182  19.23635  -27.54481 1.000 87.01758  ?  179 THR A CB  1 
ATOM 1340 O OG1 . THR A 1 179 ? 14.63903  20.35326  -27.33148 1.000 97.71361  ?  179 THR A OG1 1 
ATOM 1341 C CG2 . THR A 1 179 ? 15.20805  18.67121  -28.92638 1.000 85.17982  ?  179 THR A CG2 1 
ATOM 1342 N N   . LEU A 1 180 ? 16.68463  19.21390  -24.81270 1.000 82.03748  ?  180 LEU A N   1 
ATOM 1343 C CA  . LEU A 1 180 ? 16.96791  19.85247  -23.53194 1.000 99.84318  ?  180 LEU A CA  1 
ATOM 1344 C C   . LEU A 1 180 ? 16.33759  21.23469  -23.44619 1.000 95.95161  ?  180 LEU A C   1 
ATOM 1345 O O   . LEU A 1 180 ? 15.98536  21.68868  -22.35055 1.000 97.56458  ?  180 LEU A O   1 
ATOM 1346 C CB  . LEU A 1 180 ? 18.47288  19.94908  -23.31505 1.000 111.60275 ?  180 LEU A CB  1 
ATOM 1347 C CG  . LEU A 1 180 ? 18.93704  20.21088  -21.88709 1.000 100.58835 ?  180 LEU A CG  1 
ATOM 1348 C CD1 . LEU A 1 180 ? 18.71066  18.97989  -21.03511 1.000 90.81225  ?  180 LEU A CD1 1 
ATOM 1349 C CD2 . LEU A 1 180 ? 20.38959  20.59516  -21.90808 1.000 113.32798 ?  180 LEU A CD2 1 
ATOM 1350 N N   . GLY A 1 181 ? 16.23028  21.92479  -24.58345 1.000 95.85734  ?  181 GLY A N   1 
ATOM 1351 C CA  . GLY A 1 181 ? 15.53140  23.20252  -24.60893 1.000 93.41861  ?  181 GLY A CA  1 
ATOM 1352 C C   . GLY A 1 181 ? 14.08505  23.08643  -24.19281 1.000 106.02849 ?  181 GLY A C   1 
ATOM 1353 O O   . GLY A 1 181 ? 13.56147  23.93843  -23.46207 1.000 120.09081 ?  181 GLY A O   1 
ATOM 1354 N N   . ILE A 1 182 ? 13.38062  22.06580  -24.69957 1.000 104.02116 ?  182 ILE A N   1 
ATOM 1355 C CA  . ILE A 1 182 ? 11.99166  21.82643  -24.31980 1.000 105.84934 ?  182 ILE A CA  1 
ATOM 1356 C C   . ILE A 1 182 ? 11.87403  21.63233  -22.80645 1.000 107.57535 ?  182 ILE A C   1 
ATOM 1357 O O   . ILE A 1 182 ? 11.03240  22.25081  -22.14694 1.000 110.62086 ?  182 ILE A O   1 
ATOM 1358 C CB  . ILE A 1 182 ? 11.41510  20.63356  -25.10293 1.000 92.50138  ?  182 ILE A CB  1 
ATOM 1359 C CG1 . ILE A 1 182 ? 11.54158  20.89284  -26.61132 1.000 100.91706 ?  182 ILE A CG1 1 
ATOM 1360 C CG2 . ILE A 1 182 ? 9.97920   20.36535  -24.70800 1.000 71.10312  ?  182 ILE A CG2 1 
ATOM 1361 C CD1 . ILE A 1 182 ? 10.82668  19.88068  -27.49723 1.000 107.29150 ?  182 ILE A CD1 1 
ATOM 1362 N N   . ILE A 1 183 ? 12.71462  20.75384  -22.24652 1.000 108.51916 ?  183 ILE A N   1 
ATOM 1363 C CA  . ILE A 1 183 ? 12.71329  20.53736  -20.79839 1.000 105.24325 ?  183 ILE A CA  1 
ATOM 1364 C C   . ILE A 1 183 ? 12.91556  21.85825  -20.07256 1.000 112.93693 ?  183 ILE A C   1 
ATOM 1365 O O   . ILE A 1 183 ? 12.20895  22.17216  -19.10721 1.000 121.03652 ?  183 ILE A O   1 
ATOM 1366 C CB  . ILE A 1 183 ? 13.79653  19.51487  -20.40220 1.000 98.61765  ?  183 ILE A CB  1 
ATOM 1367 C CG1 . ILE A 1 183 ? 13.65574  18.22711  -21.21890 1.000 89.05757  ?  183 ILE A CG1 1 
ATOM 1368 C CG2 . ILE A 1 183 ? 13.74539  19.24432  -18.89979 1.000 77.25185  ?  183 ILE A CG2 1 
ATOM 1369 C CD1 . ILE A 1 183 ? 12.39933  17.44129  -20.90553 1.000 84.50002  ?  183 ILE A CD1 1 
ATOM 1370 N N   . ALA A 1 184 ? 13.89464  22.64806  -20.52338 1.000 113.16043 ?  184 ALA A N   1 
ATOM 1371 C CA  . ALA A 1 184 ? 14.16503  23.94467  -19.90810 1.000 116.58783 ?  184 ALA A CA  1 
ATOM 1372 C C   . ALA A 1 184 ? 12.93350  24.84745  -19.92785 1.000 127.30832 ?  184 ALA A C   1 
ATOM 1373 O O   . ALA A 1 184 ? 12.53087  25.38535  -18.88971 1.000 131.20405 ?  184 ALA A O   1 
ATOM 1374 C CB  . ALA A 1 184 ? 15.34305  24.61932  -20.61105 1.000 123.12418 ?  184 ALA A CB  1 
ATOM 1375 N N   . ASP A 1 185 ? 12.34408  25.05364  -21.11062 1.000 146.39641 ?  185 ASP A N   1 
ATOM 1376 C CA  . ASP A 1 185 ? 11.14482  25.88427  -21.21693 1.000 148.95495 ?  185 ASP A CA  1 
ATOM 1377 C C   . ASP A 1 185 ? 10.05142  25.40781  -20.27105 1.000 150.41998 ?  185 ASP A C   1 
ATOM 1378 O O   . ASP A 1 185 ? 9.43257   26.21056  -19.56359 1.000 158.66457 ?  185 ASP A O   1 
ATOM 1379 C CB  . ASP A 1 185 ? 10.61795  25.90143  -22.65533 1.000 146.69712 ?  185 ASP A CB  1 
ATOM 1380 C CG  . ASP A 1 185 ? 11.37292  26.86496  -23.54770 1.000 158.10561 ?  185 ASP A CG  1 
ATOM 1381 O OD1 . ASP A 1 185 ? 12.34728  27.48496  -23.07252 1.000 166.03066 ?  185 ASP A OD1 1 
ATOM 1382 O OD2 . ASP A 1 185 ? 10.97165  27.02236  -24.72083 1.000 160.11617 -1 185 ASP A OD2 1 
ATOM 1383 N N   . ALA A 1 186 ? 9.79816   24.09711  -20.24953 1.000 127.75186 ?  186 ALA A N   1 
ATOM 1384 C CA  . ALA A 1 186 ? 8.74940   23.56098  -19.38801 1.000 121.70891 ?  186 ALA A CA  1 
ATOM 1385 C C   . ALA A 1 186 ? 9.02787   23.86316  -17.91978 1.000 126.94465 ?  186 ALA A C   1 
ATOM 1386 O O   . ALA A 1 186 ? 8.11902   24.24824  -17.17486 1.000 131.46153 ?  186 ALA A O   1 
ATOM 1387 C CB  . ALA A 1 186 ? 8.60276   22.05898  -19.61710 1.000 123.50122 ?  186 ALA A CB  1 
ATOM 1388 N N   . PHE A 1 187 ? 10.27157  23.67646  -17.48102 1.000 126.15397 ?  187 PHE A N   1 
ATOM 1389 C CA  . PHE A 1 187 ? 10.66711  23.99054  -16.11375 1.000 113.65904 ?  187 PHE A CA  1 
ATOM 1390 C C   . PHE A 1 187 ? 10.98016  25.46736  -15.91288 1.000 122.85552 ?  187 PHE A C   1 
ATOM 1391 O O   . PHE A 1 187 ? 11.39792  25.84541  -14.81253 1.000 125.90620 ?  187 PHE A O   1 
ATOM 1392 C CB  . PHE A 1 187 ? 11.87658  23.13767  -15.70759 1.000 107.28993 ?  187 PHE A CB  1 
ATOM 1393 C CG  . PHE A 1 187 ? 11.54330  21.69195  -15.44556 1.000 94.05783  ?  187 PHE A CG  1 
ATOM 1394 C CD1 . PHE A 1 187 ? 11.45637  20.78263  -16.48404 1.000 107.47174 ?  187 PHE A CD1 1 
ATOM 1395 C CD2 . PHE A 1 187 ? 11.34509  21.23994  -14.15379 1.000 94.28056  ?  187 PHE A CD2 1 
ATOM 1396 C CE1 . PHE A 1 187 ? 11.14997  19.45662  -16.24174 1.000 108.70366 ?  187 PHE A CE1 1 
ATOM 1397 C CE2 . PHE A 1 187 ? 11.04225  19.91552  -13.90663 1.000 112.52253 ?  187 PHE A CE2 1 
ATOM 1398 C CZ  . PHE A 1 187 ? 10.94554  19.02310  -14.95211 1.000 104.44502 ?  187 PHE A CZ  1 
ATOM 1399 N N   . ASN A 1 188 ? 10.77766  26.29989  -16.93733 1.000 128.25023 ?  188 ASN A N   1 
ATOM 1400 C CA  . ASN A 1 188 ? 11.01983  27.74389  -16.86680 1.000 127.91336 ?  188 ASN A CA  1 
ATOM 1401 C C   . ASN A 1 188 ? 12.41198  28.04772  -16.31811 1.000 127.50373 ?  188 ASN A C   1 
ATOM 1402 O O   . ASN A 1 188 ? 12.59027  28.89165  -15.43799 1.000 145.52020 ?  188 ASN A O   1 
ATOM 1403 C CB  . ASN A 1 188 ? 9.94104   28.45578  -16.04362 1.000 128.61353 ?  188 ASN A CB  1 
ATOM 1404 C CG  . ASN A 1 188 ? 8.56291   27.84284  -16.22060 1.000 146.01059 ?  188 ASN A CG  1 
ATOM 1405 O OD1 . ASN A 1 188 ? 7.99177   27.87419  -17.31181 1.000 138.59108 ?  188 ASN A OD1 1 
ATOM 1406 N ND2 . ASN A 1 188 ? 8.02208   27.27871  -15.14466 1.000 168.92748 ?  188 ASN A ND2 1 
ATOM 1407 N N   . ALA A 1 189 ? 13.41002  27.34371  -16.84712 1.000 129.74330 ?  189 ALA A N   1 
ATOM 1408 C CA  . ALA A 1 189 ? 14.79720  27.55974  -16.45386 1.000 137.45220 ?  189 ALA A CA  1 
ATOM 1409 C C   . ALA A 1 189 ? 15.68146  27.44682  -17.69371 1.000 142.13011 ?  189 ALA A C   1 
ATOM 1410 O O   . ALA A 1 189 ? 15.19605  27.29876  -18.81935 1.000 146.54132 ?  189 ALA A O   1 
ATOM 1411 C CB  . ALA A 1 189 ? 15.20331  26.57169  -15.35257 1.000 126.56465 ?  189 ALA A CB  1 
ATOM 1412 N N   . SER A 1 190 ? 16.99294  27.51600  -17.48443 1.000 156.20437 ?  190 SER A N   1 
ATOM 1413 C CA  . SER A 1 190 ? 17.96906  27.47888  -18.56300 1.000 153.47710 ?  190 SER A CA  1 
ATOM 1414 C C   . SER A 1 190 ? 18.52170  26.06825  -18.73065 1.000 152.35798 ?  190 SER A C   1 
ATOM 1415 O O   . SER A 1 190 ? 18.54178  25.27832  -17.78416 1.000 151.08821 ?  190 SER A O   1 
ATOM 1416 C CB  . SER A 1 190 ? 19.11350  28.45837  -18.29313 1.000 155.41641 ?  190 SER A CB  1 
ATOM 1417 O OG  . SER A 1 190 ? 20.08068  28.41205  -19.32843 1.000 161.23921 ?  190 SER A OG  1 
ATOM 1418 N N   . GLU A 1 191 ? 18.95959  25.76080  -19.95750 1.000 124.12277 ?  191 GLU A N   1 
ATOM 1419 C CA  . GLU A 1 191 ? 19.54767  24.45697  -20.26540 1.000 109.37589 ?  191 GLU A CA  1 
ATOM 1420 C C   . GLU A 1 191 ? 20.59569  24.05475  -19.23138 1.000 121.25111 ?  191 GLU A C   1 
ATOM 1421 O O   . GLU A 1 191 ? 20.58541  22.92694  -18.73031 1.000 111.69096 ?  191 GLU A O   1 
ATOM 1422 C CB  . GLU A 1 191 ? 20.15829  24.47836  -21.67115 1.000 103.13611 ?  191 GLU A CB  1 
ATOM 1423 C CG  . GLU A 1 191 ? 19.15144  24.30558  -22.81286 1.000 120.62733 ?  191 GLU A CG  1 
ATOM 1424 C CD  . GLU A 1 191 ? 19.74832  23.67501  -24.07280 1.000 121.02593 ?  191 GLU A CD  1 
ATOM 1425 O OE1 . GLU A 1 191 ? 20.97838  23.45545  -24.12621 1.000 104.64788 ?  191 GLU A OE1 1 
ATOM 1426 O OE2 . GLU A 1 191 ? 18.97993  23.41434  -25.02411 1.000 113.47595 -1 191 GLU A OE2 1 
ATOM 1427 N N   . ILE A 1 192 ? 21.53909  24.95629  -18.94286 1.000 132.32554 ?  192 ILE A N   1 
ATOM 1428 C CA  . ILE A 1 192 ? 22.59578  24.68803  -17.96358 1.000 114.39199 ?  192 ILE A CA  1 
ATOM 1429 C C   . ILE A 1 192 ? 22.00932  24.21314  -16.63465 1.000 114.84148 ?  192 ILE A C   1 
ATOM 1430 O O   . ILE A 1 192 ? 22.49462  23.25125  -16.02268 1.000 118.70374 ?  192 ILE A O   1 
ATOM 1431 C CB  . ILE A 1 192 ? 23.48144  25.93518  -17.77862 1.000 108.45993 ?  192 ILE A CB  1 
ATOM 1432 C CG1 . ILE A 1 192 ? 24.41878  25.74518  -16.59158 1.000 117.10210 ?  192 ILE A CG1 1 
ATOM 1433 C CG2 . ILE A 1 192 ? 22.63845  27.18669  -17.59544 1.000 119.38888 ?  192 ILE A CG2 1 
ATOM 1434 C CD1 . ILE A 1 192 ? 25.55791  24.78759  -16.88551 1.000 120.67081 ?  192 ILE A CD1 1 
ATOM 1435 N N   . THR A 1 193 ? 20.98225  24.91235  -16.14666 1.000 127.39217 ?  193 THR A N   1 
ATOM 1436 C CA  . THR A 1 193 ? 20.40306  24.58117  -14.84702 1.000 120.15243 ?  193 THR A CA  1 
ATOM 1437 C C   . THR A 1 193 ? 19.78446  23.18192  -14.85282 1.000 115.50950 ?  193 THR A C   1 
ATOM 1438 O O   . THR A 1 193 ? 19.93347  22.42075  -13.88483 1.000 124.40722 ?  193 THR A O   1 
ATOM 1439 C CB  . THR A 1 193 ? 19.37785  25.64981  -14.45486 1.000 114.45726 ?  193 THR A CB  1 
ATOM 1440 O OG1 . THR A 1 193 ? 18.28616  25.63798  -15.37814 1.000 122.94660 ?  193 THR A OG1 1 
ATOM 1441 C CG2 . THR A 1 193 ? 20.01866  27.03656  -14.50543 1.000 103.82915 ?  193 THR A CG2 1 
ATOM 1442 N N   . ILE A 1 194 ? 19.06031  22.83777  -15.92219 1.000 120.97939 ?  194 ILE A N   1 
ATOM 1443 C CA  . ILE A 1 194 ? 18.51114  21.48896  -16.05740 1.000 111.04173 ?  194 ILE A CA  1 
ATOM 1444 C C   . ILE A 1 194 ? 19.64319  20.46419  -16.08525 1.000 118.50387 ?  194 ILE A C   1 
ATOM 1445 O O   . ILE A 1 194 ? 19.58887  19.42909  -15.40303 1.000 120.50180 ?  194 ILE A O   1 
ATOM 1446 C CB  . ILE A 1 194 ? 17.60690  21.39611  -17.30548 1.000 105.47234 ?  194 ILE A CB  1 
ATOM 1447 C CG1 . ILE A 1 194 ? 16.16179  21.81167  -16.98684 1.000 97.90067  ?  194 ILE A CG1 1 
ATOM 1448 C CG2 . ILE A 1 194 ? 17.60957  19.99946  -17.88054 1.000 108.42021 ?  194 ILE A CG2 1 
ATOM 1449 C CD1 . ILE A 1 194 ? 15.93017  23.29377  -16.85157 1.000 110.32969 ?  194 ILE A CD1 1 
ATOM 1450 N N   . ARG A 1 195 ? 20.69066  20.74634  -16.87118 1.000 124.05929 ?  195 ARG A N   1 
ATOM 1451 C CA  . ARG A 1 195 ? 21.86478  19.87830  -16.91443 1.000 121.42155 ?  195 ARG A CA  1 
ATOM 1452 C C   . ARG A 1 195 ? 22.41712  19.63564  -15.51861 1.000 120.80938 ?  195 ARG A C   1 
ATOM 1453 O O   . ARG A 1 195 ? 22.91229  18.54603  -15.22600 1.000 120.73470 ?  195 ARG A O   1 
ATOM 1454 C CB  . ARG A 1 195 ? 22.94255  20.47495  -17.81930 1.000 120.48909 ?  195 ARG A CB  1 
ATOM 1455 C CG  . ARG A 1 195 ? 22.52062  20.58512  -19.25647 1.000 134.99717 ?  195 ARG A CG  1 
ATOM 1456 C CD  . ARG A 1 195 ? 23.56829  21.28707  -20.08634 1.000 137.93453 ?  195 ARG A CD  1 
ATOM 1457 N NE  . ARG A 1 195 ? 24.78974  20.50083  -20.17898 1.000 146.45374 ?  195 ARG A NE  1 
ATOM 1458 C CZ  . ARG A 1 195 ? 25.88016  20.89952  -20.81610 1.000 161.51248 ?  195 ARG A CZ  1 
ATOM 1459 N NH1 . ARG A 1 195 ? 25.93787  22.08089  -21.41031 1.000 152.52967 ?  195 ARG A NH1 1 
ATOM 1460 N NH2 . ARG A 1 195 ? 26.94279  20.09955  -20.84648 1.000 160.20569 ?  195 ARG A NH2 1 
ATOM 1461 N N   . LYS A 1 196 ? 22.35537  20.64735  -14.64616 1.000 123.60573 ?  196 LYS A N   1 
ATOM 1462 C CA  . LYS A 1 196 ? 22.89780  20.48562  -13.29557 1.000 123.50705 ?  196 LYS A CA  1 
ATOM 1463 C C   . LYS A 1 196 ? 21.96269  19.66931  -12.38619 1.000 130.28896 ?  196 LYS A C   1 
ATOM 1464 O O   . LYS A 1 196 ? 22.43567  18.79724  -11.63955 1.000 137.53469 ?  196 LYS A O   1 
ATOM 1465 C CB  . LYS A 1 196 ? 23.21311  21.86210  -12.69253 1.000 123.08770 ?  196 LYS A CB  1 
ATOM 1466 C CG  . LYS A 1 196 ? 24.42097  22.58940  -13.32089 1.000 127.63103 ?  196 LYS A CG  1 
ATOM 1467 C CD  . LYS A 1 196 ? 25.01042  23.62074  -12.34925 1.000 119.13873 ?  196 LYS A CD  1 
ATOM 1468 C CE  . LYS A 1 196 ? 25.07648  25.01531  -12.96482 1.000 125.75351 ?  196 LYS A CE  1 
ATOM 1469 N NZ  . LYS A 1 196 ? 23.71409  25.57235  -13.23737 1.000 129.20570 ?  196 LYS A NZ  1 
ATOM 1470 N N   . ARG A 1 197 ? 20.63779  19.91495  -12.43968 1.000 135.56864 ?  197 ARG A N   1 
ATOM 1471 C CA  . ARG A 1 197 ? 19.71685  19.07815  -11.66009 1.000 131.94662 ?  197 ARG A CA  1 
ATOM 1472 C C   . ARG A 1 197 ? 19.88656  17.60813  -12.05978 1.000 136.00625 ?  197 ARG A C   1 
ATOM 1473 O O   . ARG A 1 197 ? 19.85316  16.72097  -11.19778 1.000 136.96025 ?  197 ARG A O   1 
ATOM 1474 C CB  . ARG A 1 197 ? 18.24768  19.58465  -11.77404 1.000 145.38524 ?  197 ARG A CB  1 
ATOM 1475 C CG  . ARG A 1 197 ? 17.26175  19.21028  -10.55289 1.000 157.73880 ?  197 ARG A CG  1 
ATOM 1476 C CD  . ARG A 1 197 ? 15.64668  19.64014  -10.64681 1.000 146.29741 ?  197 ARG A CD  1 
ATOM 1477 N NE  . ARG A 1 197 ? 14.80704  18.68578  -9.89086  1.000 155.79788 ?  197 ARG A NE  1 
ATOM 1478 C CZ  . ARG A 1 197 ? 13.48364  18.52703  -10.03774 1.000 156.42488 ?  197 ARG A CZ  1 
ATOM 1479 N NH1 . ARG A 1 197 ? 12.78990  19.15505  -10.96842 1.000 147.28777 ?  197 ARG A NH1 1 
ATOM 1480 N NH2 . ARG A 1 197 ? 12.85417  17.64921  -9.23881  1.000 150.96802 ?  197 ARG A NH2 1 
ATOM 1481 N N   . LEU A 1 198 ? 20.18862  17.34138  -13.34337 1.000 115.90083 ?  198 LEU A N   1 
ATOM 1482 C CA  . LEU A 1 198 ? 20.46346  15.96293  -13.77489 1.000 117.30554 ?  198 LEU A CA  1 
ATOM 1483 C C   . LEU A 1 198 ? 21.83892  15.45663  -13.33681 1.000 123.75260 ?  198 LEU A C   1 
ATOM 1484 O O   . LEU A 1 198 ? 21.95193  14.36108  -12.77206 1.000 135.11149 ?  198 LEU A O   1 
ATOM 1485 C CB  . LEU A 1 198 ? 20.32838  15.82205  -15.29887 1.000 121.50348 ?  198 LEU A CB  1 
ATOM 1486 C CG  . LEU A 1 198 ? 18.94845  15.38354  -15.83035 1.000 87.75886  ?  198 LEU A CG  1 
ATOM 1487 C CD1 . LEU A 1 198 ? 18.85466  15.17997  -17.31960 1.000 92.96957  ?  198 LEU A CD1 1 
ATOM 1488 C CD2 . LEU A 1 198 ? 18.46422  14.12879  -15.12495 1.000 115.07424 ?  198 LEU A CD2 1 
ATOM 1489 N N   . GLU A 1 199 ? 22.89599  16.23497  -13.57814 1.000 129.89924 ?  199 GLU A N   1 
ATOM 1490 C CA  . GLU A 1 199 ? 24.24283  15.75769  -13.28666 1.000 134.44356 ?  199 GLU A CA  1 
ATOM 1491 C C   . GLU A 1 199 ? 24.43416  15.47826  -11.80512 1.000 138.68248 ?  199 GLU A C   1 
ATOM 1492 O O   . GLU A 1 199 ? 25.21192  14.58909  -11.43997 1.000 133.69679 ?  199 GLU A O   1 
ATOM 1493 C CB  . GLU A 1 199 ? 25.27487  16.77223  -13.77383 1.000 135.24759 ?  199 GLU A CB  1 
ATOM 1494 C CG  . GLU A 1 199 ? 25.52909  16.72256  -15.26798 1.000 139.21827 ?  199 GLU A CG  1 
ATOM 1495 C CD  . GLU A 1 199 ? 26.52789  17.76870  -15.70881 1.000 158.68365 ?  199 GLU A CD  1 
ATOM 1496 O OE1 . GLU A 1 199 ? 26.93553  18.58558  -14.85714 1.000 159.94681 ?  199 GLU A OE1 1 
ATOM 1497 O OE2 . GLU A 1 199 ? 26.90285  17.77952  -16.90110 1.000 165.26998 -1 199 GLU A OE2 1 
ATOM 1498 N N   . SER A 1 200 ? 23.74450  16.22488  -10.93678 1.000 146.89889 ?  200 SER A N   1 
ATOM 1499 C CA  . SER A 1 200 ? 23.86609  15.96571  -9.50644  1.000 129.37100 ?  200 SER A CA  1 
ATOM 1500 C C   . SER A 1 200 ? 23.45824  14.53653  -9.17466  1.000 122.97472 ?  200 SER A C   1 
ATOM 1501 O O   . SER A 1 200 ? 24.03322  13.91312  -8.27599  1.000 129.28276 ?  200 SER A O   1 
ATOM 1502 C CB  . SER A 1 200 ? 23.02431  16.96279  -8.70890  1.000 125.82306 ?  200 SER A CB  1 
ATOM 1503 O OG  . SER A 1 200 ? 21.68823  16.51277  -8.57724  1.000 133.73855 ?  200 SER A OG  1 
ATOM 1504 N N   . GLU A 1 201 ? 22.46362  14.00301  -9.88609  1.000 109.36048 ?  201 GLU A N   1 
ATOM 1505 C CA  . GLU A 1 201 ? 22.00406  12.63487  -9.69182  1.000 123.74626 ?  201 GLU A CA  1 
ATOM 1506 C C   . GLU A 1 201 ? 22.56374  11.64761  -10.72122 1.000 132.87720 ?  201 GLU A C   1 
ATOM 1507 O O   . GLU A 1 201 ? 21.96376  10.58727  -10.93435 1.000 124.95164 ?  201 GLU A O   1 
ATOM 1508 C CB  . GLU A 1 201 ? 20.47548  12.61820  -9.69842  1.000 111.42442 ?  201 GLU A CB  1 
ATOM 1509 C CG  . GLU A 1 201 ? 19.88539  13.38219  -8.52515  1.000 106.49508 ?  201 GLU A CG  1 
ATOM 1510 C CD  . GLU A 1 201 ? 18.39376  13.60093  -8.63450  1.000 95.37234  ?  201 GLU A CD  1 
ATOM 1511 O OE1 . GLU A 1 201 ? 17.80981  13.26186  -9.68123  1.000 108.10913 ?  201 GLU A OE1 1 
ATOM 1512 O OE2 . GLU A 1 201 ? 17.80117  14.11483  -7.66319  1.000 114.45939 -1 201 GLU A OE2 1 
ATOM 1513 N N   . ASN A 1 202 ? 23.70778  11.96090  -11.33652 1.000 147.33098 ?  202 ASN A N   1 
ATOM 1514 C CA  . ASN A 1 202 ? 24.41612  11.05933  -12.26152 1.000 146.30824 ?  202 ASN A CA  1 
ATOM 1515 C C   . ASN A 1 202 ? 23.51676  10.53442  -13.38290 1.000 144.32734 ?  202 ASN A C   1 
ATOM 1516 O O   . ASN A 1 202 ? 23.43510  9.32844   -13.63642 1.000 143.31564 ?  202 ASN A O   1 
ATOM 1517 C CB  . ASN A 1 202 ? 25.05694  9.89377   -11.50537 1.000 154.20879 ?  202 ASN A CB  1 
ATOM 1518 C CG  . ASN A 1 202 ? 26.21270  9.26765   -12.26841 1.000 150.62068 ?  202 ASN A CG  1 
ATOM 1519 O OD1 . ASN A 1 202 ? 26.03881  8.26339   -12.95626 1.000 141.26023 ?  202 ASN A OD1 1 
ATOM 1520 N ND2 . ASN A 1 202 ? 27.40028  9.84885   -12.13705 1.000 156.37913 ?  202 ASN A ND2 1 
ATOM 1521 N N   . THR A 1 203 ? 22.86928  11.45828  -14.08993 1.000 131.50931 ?  203 THR A N   1 
ATOM 1522 C CA  . THR A 1 203 ? 22.00462  11.12189  -15.21361 1.000 111.58970 ?  203 THR A CA  1 
ATOM 1523 C C   . THR A 1 203 ? 22.10982  12.22092  -16.25705 1.000 106.02662 ?  203 THR A C   1 
ATOM 1524 O O   . THR A 1 203 ? 22.55466  13.33593  -15.97278 1.000 119.71817 ?  203 THR A O   1 
ATOM 1525 C CB  . THR A 1 203 ? 20.53403  10.93826  -14.79804 1.000 100.77096 ?  203 THR A CB  1 
ATOM 1526 O OG1 . THR A 1 203 ? 20.16503  11.96441  -13.87231 1.000 105.79060 ?  203 THR A OG1 1 
ATOM 1527 C CG2 . THR A 1 203 ? 20.28166  9.56887   -14.17989 1.000 109.21669 ?  203 THR A CG2 1 
ATOM 1528 N N   . ASN A 1 204 ? 21.69549  11.88978  -17.47311 1.000 94.82006  ?  204 ASN A N   1 
ATOM 1529 C CA  . ASN A 1 204 ? 21.57053  12.85734  -18.55149 1.000 88.58680  ?  204 ASN A CA  1 
ATOM 1530 C C   . ASN A 1 204 ? 20.21546  12.66751  -19.21955 1.000 96.36242  ?  204 ASN A C   1 
ATOM 1531 O O   . ASN A 1 204 ? 19.63231  11.57925  -19.17987 1.000 99.06637  ?  204 ASN A O   1 
ATOM 1532 C CB  . ASN A 1 204 ? 22.70863  12.72214  -19.56793 1.000 88.22568  ?  204 ASN A CB  1 
ATOM 1533 C CG  . ASN A 1 204 ? 22.84893  11.31027  -20.10054 1.000 101.63816 ?  204 ASN A CG  1 
ATOM 1534 O OD1 . ASN A 1 204 ? 22.18058  10.93533  -21.06189 1.000 108.99074 ?  204 ASN A OD1 1 
ATOM 1535 N ND2 . ASN A 1 204 ? 23.71780  10.51774  -19.47699 1.000 98.16354  ?  204 ASN A ND2 1 
ATOM 1536 N N   . PHE A 1 205 ? 19.70717  13.75372  -19.80631 1.000 99.63163  ?  205 PHE A N   1 
ATOM 1537 C CA  . PHE A 1 205 ? 18.36884  13.74113  -20.38785 1.000 96.45921  ?  205 PHE A CA  1 
ATOM 1538 C C   . PHE A 1 205 ? 18.19372  12.57516  -21.34883 1.000 96.72807  ?  205 PHE A C   1 
ATOM 1539 O O   . PHE A 1 205 ? 17.15657  11.89474  -21.33920 1.000 95.25861  ?  205 PHE A O   1 
ATOM 1540 C CB  . PHE A 1 205 ? 18.10707  15.08274  -21.07791 1.000 98.94051  ?  205 PHE A CB  1 
ATOM 1541 C CG  . PHE A 1 205 ? 17.01982  15.03336  -22.09604 1.000 99.60753  ?  205 PHE A CG  1 
ATOM 1542 C CD1 . PHE A 1 205 ? 15.68959  15.08287  -21.71113 1.000 97.54844  ?  205 PHE A CD1 1 
ATOM 1543 C CD2 . PHE A 1 205 ? 17.32664  14.91749  -23.43956 1.000 97.35957  ?  205 PHE A CD2 1 
ATOM 1544 C CE1 . PHE A 1 205 ? 14.68941  15.02304  -22.64718 1.000 100.94046 ?  205 PHE A CE1 1 
ATOM 1545 C CE2 . PHE A 1 205 ? 16.33354  14.85347  -24.37972 1.000 108.56423 ?  205 PHE A CE2 1 
ATOM 1546 C CZ  . PHE A 1 205 ? 15.01222  14.90628  -23.98644 1.000 112.92973 ?  205 PHE A CZ  1 
ATOM 1547 N N   . ASN A 1 206 ? 19.22610  12.29919  -22.14888 1.000 85.96317  ?  206 ASN A N   1 
ATOM 1548 C CA  . ASN A 1 206 ? 19.15945  11.19720  -23.09726 1.000 82.57012  ?  206 ASN A CA  1 
ATOM 1549 C C   . ASN A 1 206 ? 19.02050  9.86500   -22.37654 1.000 82.06697  ?  206 ASN A C   1 
ATOM 1550 O O   . ASN A 1 206 ? 18.30034  8.97292   -22.84023 1.000 82.96419  ?  206 ASN A O   1 
ATOM 1551 C CB  . ASN A 1 206 ? 20.39992  11.20177  -23.98942 1.000 85.52735  ?  206 ASN A CB  1 
ATOM 1552 C CG  . ASN A 1 206 ? 20.64089  12.54361  -24.63903 1.000 90.55085  ?  206 ASN A CG  1 
ATOM 1553 O OD1 . ASN A 1 206 ? 21.38142  13.37697  -24.11568 1.000 107.39387 ?  206 ASN A OD1 1 
ATOM 1554 N ND2 . ASN A 1 206 ? 20.00988  12.76671  -25.78172 1.000 97.46864  ?  206 ASN A ND2 1 
ATOM 1555 N N   . GLN A 1 207 ? 19.67990  9.71925   -21.22569 1.000 79.65967  ?  207 GLN A N   1 
ATOM 1556 C CA  . GLN A 1 207 ? 19.55817  8.47919   -20.46856 1.000 79.74849  ?  207 GLN A CA  1 
ATOM 1557 C C   . GLN A 1 207 ? 18.15167  8.30738   -19.91853 1.000 80.27959  ?  207 GLN A C   1 
ATOM 1558 O O   . GLN A 1 207 ? 17.58040  7.21410   -19.99068 1.000 82.83178  ?  207 GLN A O   1 
ATOM 1559 C CB  . GLN A 1 207 ? 20.56914  8.44238   -19.32967 1.000 81.73728  ?  207 GLN A CB  1 
ATOM 1560 C CG  . GLN A 1 207 ? 20.49364  7.15954   -18.52184 1.000 91.01373  ?  207 GLN A CG  1 
ATOM 1561 C CD  . GLN A 1 207 ? 21.14041  7.29543   -17.15755 1.000 111.98556 ?  207 GLN A CD  1 
ATOM 1562 O OE1 . GLN A 1 207 ? 21.85711  8.26226   -16.89257 1.000 123.60259 ?  207 GLN A OE1 1 
ATOM 1563 N NE2 . GLN A 1 207 ? 20.87994  6.33339   -16.27786 1.000 100.11776 ?  207 GLN A NE2 1 
ATOM 1564 N N   . ILE A 1 208 ? 17.58505  9.37040   -19.34139 1.000 81.41737  ?  208 ILE A N   1 
ATOM 1565 C CA  . ILE A 1 208 ? 16.20495  9.30428   -18.86103 1.000 83.21454  ?  208 ILE A CA  1 
ATOM 1566 C C   . ILE A 1 208 ? 15.27728  8.85705   -19.97986 1.000 71.41426  ?  208 ILE A C   1 
ATOM 1567 O O   . ILE A 1 208 ? 14.46960  7.93314   -19.81330 1.000 74.96066  ?  208 ILE A O   1 
ATOM 1568 C CB  . ILE A 1 208 ? 15.76376  10.66105  -18.28585 1.000 79.50289  ?  208 ILE A CB  1 
ATOM 1569 C CG1 . ILE A 1 208 ? 16.34224  10.86978  -16.89644 1.000 78.94551  ?  208 ILE A CG1 1 
ATOM 1570 C CG2 . ILE A 1 208 ? 14.24856  10.77338  -18.23841 1.000 75.05499  ?  208 ILE A CG2 1 
ATOM 1571 C CD1 . ILE A 1 208 ? 15.90932  12.17187  -16.30711 1.000 90.82067  ?  208 ILE A CD1 1 
ATOM 1572 N N   . LEU A 1 209 ? 15.37546  9.51741   -21.13378 1.000 71.56221  ?  209 LEU A N   1 
ATOM 1573 C CA  . LEU A 1 209 ? 14.48381  9.19913   -22.24323 1.000 74.63691  ?  209 LEU A CA  1 
ATOM 1574 C C   . LEU A 1 209 ? 14.66769  7.75691   -22.71418 1.000 66.54612  ?  209 LEU A C   1 
ATOM 1575 O O   . LEU A 1 209 ? 13.68562  7.04479   -22.96887 1.000 74.87481  ?  209 LEU A O   1 
ATOM 1576 C CB  . LEU A 1 209 ? 14.71264  10.19151  -23.37750 1.000 78.41771  ?  209 LEU A CB  1 
ATOM 1577 C CG  . LEU A 1 209 ? 13.76305  10.11839  -24.56081 1.000 79.49713  ?  209 LEU A CG  1 
ATOM 1578 C CD1 . LEU A 1 209 ? 13.55772  11.51975  -25.09072 1.000 79.70027  ?  209 LEU A CD1 1 
ATOM 1579 C CD2 . LEU A 1 209 ? 14.35632  9.21518   -25.62667 1.000 101.71782 ?  209 LEU A CD2 1 
ATOM 1580 N N   . MET A 1 210 ? 15.92259  7.31576   -22.86163 1.000 68.96342  ?  210 MET A N   1 
ATOM 1581 C CA  . MET A 1 210 ? 16.18332  5.94587   -23.29637 1.000 72.81451  ?  210 MET A CA  1 
ATOM 1582 C C   . MET A 1 210 ? 15.63779  4.92490   -22.29879 1.000 62.73136  ?  210 MET A C   1 
ATOM 1583 O O   . MET A 1 210 ? 15.07161  3.89933   -22.69825 1.000 60.68910  ?  210 MET A O   1 
ATOM 1584 C CB  . MET A 1 210 ? 17.68188  5.73694   -23.53121 1.000 66.86371  ?  210 MET A CB  1 
ATOM 1585 C CG  . MET A 1 210 ? 18.04223  4.29058   -23.85944 1.000 80.15475  ?  210 MET A CG  1 
ATOM 1586 S SD  . MET A 1 210 ? 17.86178  3.88910   -25.61292 1.000 83.46190  ?  210 MET A SD  1 
ATOM 1587 C CE  . MET A 1 210 ? 19.00458  5.07221   -26.33814 1.000 99.89011  ?  210 MET A CE  1 
ATOM 1588 N N   . GLN A 1 211 ? 15.81108  5.17147   -20.99781 1.000 63.64954  ?  211 GLN A N   1 
ATOM 1589 C CA  . GLN A 1 211 ? 15.28117  4.23240   -20.01359 1.000 65.93173  ?  211 GLN A CA  1 
ATOM 1590 C C   . GLN A 1 211 ? 13.75851  4.20056   -20.03061 1.000 73.19152  ?  211 GLN A C   1 
ATOM 1591 O O   . GLN A 1 211 ? 13.15683  3.12009   -19.96806 1.000 67.57388  ?  211 GLN A O   1 
ATOM 1592 C CB  . GLN A 1 211 ? 15.79289  4.55642   -18.61351 1.000 63.99648  ?  211 GLN A CB  1 
ATOM 1593 C CG  . GLN A 1 211 ? 17.13144  3.92792   -18.30339 1.000 79.56971  ?  211 GLN A CG  1 
ATOM 1594 C CD  . GLN A 1 211 ? 17.04521  2.41690   -18.10007 1.000 90.22738  ?  211 GLN A CD  1 
ATOM 1595 O OE1 . GLN A 1 211 ? 16.01919  1.78503   -18.38014 1.000 71.10476  ?  211 GLN A OE1 1 
ATOM 1596 N NE2 . GLN A 1 211 ? 18.13535  1.83014   -17.61457 1.000 99.03133  ?  211 GLN A NE2 1 
ATOM 1597 N N   . LEU A 1 212 ? 13.11899  5.37050   -20.09904 1.000 76.04167  ?  212 LEU A N   1 
ATOM 1598 C CA  . LEU A 1 212 ? 11.66671  5.41109   -20.21877 1.000 69.99748  ?  212 LEU A CA  1 
ATOM 1599 C C   . LEU A 1 212 ? 11.19286  4.53736   -21.36881 1.000 70.45130  ?  212 LEU A C   1 
ATOM 1600 O O   . LEU A 1 212 ? 10.33970  3.65456   -21.19419 1.000 80.62116  ?  212 LEU A O   1 
ATOM 1601 C CB  . LEU A 1 212 ? 11.19960  6.84645   -20.43455 1.000 69.94163  ?  212 LEU A CB  1 
ATOM 1602 C CG  . LEU A 1 212 ? 10.62538  7.55162   -19.21419 1.000 87.03236  ?  212 LEU A CG  1 
ATOM 1603 C CD1 . LEU A 1 212 ? 10.20004  8.95724   -19.61314 1.000 81.54286  ?  212 LEU A CD1 1 
ATOM 1604 C CD2 . LEU A 1 212 ? 9.47814   6.75307   -18.60868 1.000 80.30124  ?  212 LEU A CD2 1 
ATOM 1605 N N   . ARG A 1 213 ? 11.75721  4.76199   -22.55714 1.000 77.43911  ?  213 ARG A N   1 
ATOM 1606 C CA  . ARG A 1 213 ? 11.26985  4.06033   -23.73860 1.000 62.61025  ?  213 ARG A CA  1 
ATOM 1607 C C   . ARG A 1 213 ? 11.56331  2.56488   -23.67619 1.000 58.76260  ?  213 ARG A C   1 
ATOM 1608 O O   . ARG A 1 213 ? 10.69274  1.75315   -24.00565 1.000 63.00191  ?  213 ARG A O   1 
ATOM 1609 C CB  . ARG A 1 213 ? 11.86086  4.69375   -24.98766 1.000 59.00156  ?  213 ARG A CB  1 
ATOM 1610 C CG  . ARG A 1 213 ? 11.39486  6.12760   -25.15875 1.000 75.80875  ?  213 ARG A CG  1 
ATOM 1611 C CD  . ARG A 1 213 ? 11.84043  6.73164   -26.47621 1.000 81.72637  ?  213 ARG A CD  1 
ATOM 1612 N NE  . ARG A 1 213 ? 11.20743  8.02776   -26.67123 1.000 77.33927  ?  213 ARG A NE  1 
ATOM 1613 C CZ  . ARG A 1 213 ? 11.61664  8.94225   -27.53528 1.000 72.75706  ?  213 ARG A CZ  1 
ATOM 1614 N NH1 . ARG A 1 213 ? 12.64880  8.72544   -28.33169 1.000 96.35921  ?  213 ARG A NH1 1 
ATOM 1615 N NH2 . ARG A 1 213 ? 10.96584  10.09867  -27.61064 1.000 81.66807  ?  213 ARG A NH2 1 
ATOM 1616 N N   . MET A 1 214 ? 12.75421  2.17124   -23.20818 1.000 67.53025  ?  214 MET A N   1 
ATOM 1617 C CA  . MET A 1 214 ? 13.07869  0.74611   -23.16639 1.000 67.88526  ?  214 MET A CA  1 
ATOM 1618 C C   . MET A 1 214 ? 12.29517  0.01084   -22.08392 1.000 66.68833  ?  214 MET A C   1 
ATOM 1619 O O   . MET A 1 214 ? 11.95328  -1.16466  -22.26812 1.000 62.86841  ?  214 MET A O   1 
ATOM 1620 C CB  . MET A 1 214 ? 14.58316  0.53758   -22.97495 1.000 66.96302  ?  214 MET A CB  1 
ATOM 1621 C CG  . MET A 1 214 ? 15.41379  0.85367   -24.21939 1.000 69.94629  ?  214 MET A CG  1 
ATOM 1622 S SD  . MET A 1 214 ? 14.79146  0.06971   -25.72381 1.000 58.43471  ?  214 MET A SD  1 
ATOM 1623 C CE  . MET A 1 214 ? 14.39142  1.51698   -26.69003 1.000 64.20417  ?  214 MET A CE  1 
ATOM 1624 N N   . SER A 1 215 ? 11.97369  0.68283   -20.97065 1.000 67.78711  ?  215 SER A N   1 
ATOM 1625 C CA  . SER A 1 215 ? 11.16733  0.06067   -19.92232 1.000 64.21892  ?  215 SER A CA  1 
ATOM 1626 C C   . SER A 1 215 ? 9.71746   -0.12322  -20.36957 1.000 76.12999  ?  215 SER A C   1 
ATOM 1627 O O   . SER A 1 215 ? 9.13346   -1.21107  -20.21188 1.000 64.00699  ?  215 SER A O   1 
ATOM 1628 C CB  . SER A 1 215 ? 11.24119  0.90937   -18.65330 1.000 65.68675  ?  215 SER A CB  1 
ATOM 1629 O OG  . SER A 1 215 ? 10.27546  0.50149   -17.70122 1.000 99.23897  ?  215 SER A OG  1 
ATOM 1630 N N   . LYS A 1 216 ? 9.10968   0.94405   -20.90479 1.000 76.04697  ?  216 LYS A N   1 
ATOM 1631 C CA  . LYS A 1 216 ? 7.77848   0.82029   -21.48677 1.000 58.92239  ?  216 LYS A CA  1 
ATOM 1632 C C   . LYS A 1 216 ? 7.74844   -0.27806  -22.54576 1.000 67.26160  ?  216 LYS A C   1 
ATOM 1633 O O   . LYS A 1 216 ? 6.78309   -1.05225  -22.62521 1.000 74.02961  ?  216 LYS A O   1 
ATOM 1634 C CB  . LYS A 1 216 ? 7.33445   2.16447   -22.07193 1.000 59.01086  ?  216 LYS A CB  1 
ATOM 1635 C CG  . LYS A 1 216 ? 5.82560   2.35940   -22.06935 1.000 62.34483  ?  216 LYS A CG  1 
ATOM 1636 C CD  . LYS A 1 216 ? 5.24751   2.07303   -20.67138 1.000 90.28803  ?  216 LYS A CD  1 
ATOM 1637 C CE  . LYS A 1 216 ? 3.78170   1.59530   -20.71464 1.000 94.55509  ?  216 LYS A CE  1 
ATOM 1638 N NZ  . LYS A 1 216 ? 3.26542   1.06566   -19.39597 1.000 73.16052  ?  216 LYS A NZ  1 
ATOM 1639 N N   . ALA A 1 217 ? 8.80478   -0.36447  -23.36645 1.000 60.35970  ?  217 ALA A N   1 
ATOM 1640 C CA  . ALA A 1 217 ? 8.85888   -1.37740  -24.41466 1.000 57.37649  ?  217 ALA A CA  1 
ATOM 1641 C C   . ALA A 1 217 ? 8.93079   -2.78060  -23.83770 1.000 66.15641  ?  217 ALA A C   1 
ATOM 1642 O O   . ALA A 1 217 ? 8.26255   -3.69045  -24.33326 1.000 78.43882  ?  217 ALA A O   1 
ATOM 1643 C CB  . ALA A 1 217 ? 10.04909  -1.12267  -25.33165 1.000 66.21240  ?  217 ALA A CB  1 
ATOM 1644 N N   . ALA A 1 218 ? 9.75349   -2.98572  -22.80769 1.000 69.04923  ?  218 ALA A N   1 
ATOM 1645 C CA  . ALA A 1 218 ? 9.83438   -4.30535  -22.18860 1.000 70.16153  ?  218 ALA A CA  1 
ATOM 1646 C C   . ALA A 1 218 ? 8.47799   -4.73474  -21.63411 1.000 86.94495  ?  218 ALA A C   1 
ATOM 1647 O O   . ALA A 1 218 ? 8.03801   -5.87507  -21.85262 1.000 87.40860  ?  218 ALA A O   1 
ATOM 1648 C CB  . ALA A 1 218 ? 10.90541  -4.30938  -21.09510 1.000 55.27306  ?  218 ALA A CB  1 
ATOM 1649 N N   . LEU A 1 219 ? 7.80067   -3.83125  -20.90627 1.000 93.45676  ?  219 LEU A N   1 
ATOM 1650 C CA  . LEU A 1 219 ? 6.47428   -4.15458  -20.37132 1.000 80.56082  ?  219 LEU A CA  1 
ATOM 1651 C C   . LEU A 1 219 ? 5.48816   -4.51086  -21.48295 1.000 82.71757  ?  219 LEU A C   1 
ATOM 1652 O O   . LEU A 1 219 ? 4.83743   -5.56536  -21.43505 1.000 84.89099  ?  219 LEU A O   1 
ATOM 1653 C CB  . LEU A 1 219 ? 5.93336   -3.00088  -19.52305 1.000 72.72944  ?  219 LEU A CB  1 
ATOM 1654 C CG  . LEU A 1 219 ? 6.70988   -2.59861  -18.26908 1.000 78.13305  ?  219 LEU A CG  1 
ATOM 1655 C CD1 . LEU A 1 219 ? 6.17350   -1.30029  -17.66757 1.000 77.68923  ?  219 LEU A CD1 1 
ATOM 1656 C CD2 . LEU A 1 219 ? 6.63242   -3.72410  -17.25278 1.000 69.79048  ?  219 LEU A CD2 1 
ATOM 1657 N N   . LEU A 1 220 ? 5.35356   -3.63557  -22.48836 1.000 77.14660  ?  220 LEU A N   1 
ATOM 1658 C CA  . LEU A 1 220 ? 4.42517   -3.90349  -23.58803 1.000 87.34253  ?  220 LEU A CA  1 
ATOM 1659 C C   . LEU A 1 220 ? 4.75228   -5.21977  -24.28168 1.000 90.47242  ?  220 LEU A C   1 
ATOM 1660 O O   . LEU A 1 220 ? 3.84866   -5.95439  -24.70073 1.000 95.08452  ?  220 LEU A O   1 
ATOM 1661 C CB  . LEU A 1 220 ? 4.44794   -2.75097  -24.59253 1.000 70.71554  ?  220 LEU A CB  1 
ATOM 1662 C CG  . LEU A 1 220 ? 3.82534   -1.44975  -24.09443 1.000 64.46019  ?  220 LEU A CG  1 
ATOM 1663 C CD1 . LEU A 1 220 ? 4.22231   -0.29139  -24.98251 1.000 68.30277  ?  220 LEU A CD1 1 
ATOM 1664 C CD2 . LEU A 1 220 ? 2.31850   -1.58875  -24.02601 1.000 71.02828  ?  220 LEU A CD2 1 
ATOM 1665 N N   . LEU A 1 221 ? 6.04329   -5.51613  -24.43759 1.000 97.88131  ?  221 LEU A N   1 
ATOM 1666 C CA  . LEU A 1 221 ? 6.46683   -6.77115  -25.04375 1.000 98.21453  ?  221 LEU A CA  1 
ATOM 1667 C C   . LEU A 1 221 ? 5.96613   -7.95993  -24.23816 1.000 92.84972  ?  221 LEU A C   1 
ATOM 1668 O O   . LEU A 1 221 ? 5.40788   -8.90892  -24.79716 1.000 104.14760 ?  221 LEU A O   1 
ATOM 1669 C CB  . LEU A 1 221 ? 7.99025   -6.79885  -25.15837 1.000 83.40839  ?  221 LEU A CB  1 
ATOM 1670 C CG  . LEU A 1 221 ? 8.58218   -8.01413  -25.85202 1.000 85.68519  ?  221 LEU A CG  1 
ATOM 1671 C CD1 . LEU A 1 221 ? 8.20874   -8.00515  -27.31939 1.000 86.54258  ?  221 LEU A CD1 1 
ATOM 1672 C CD2 . LEU A 1 221 ? 10.07756  -8.01584  -25.66357 1.000 87.45248  ?  221 LEU A CD2 1 
ATOM 1673 N N   . LEU A 1 222 ? 6.17394   -7.93528  -22.91875 1.000 92.11846  ?  222 LEU A N   1 
ATOM 1674 C CA  . LEU A 1 222 ? 5.71037   -9.05072  -22.09695 1.000 91.68384  ?  222 LEU A CA  1 
ATOM 1675 C C   . LEU A 1 222 ? 4.19025   -9.13698  -22.02987 1.000 96.00547  ?  222 LEU A C   1 
ATOM 1676 O O   . LEU A 1 222 ? 3.66186   -10.20719 -21.71265 1.000 90.92972  ?  222 LEU A O   1 
ATOM 1677 C CB  . LEU A 1 222 ? 6.28992   -8.96242  -20.68441 1.000 86.22008  ?  222 LEU A CB  1 
ATOM 1678 C CG  . LEU A 1 222 ? 7.75074   -9.39691  -20.52151 1.000 97.98892  ?  222 LEU A CG  1 
ATOM 1679 C CD1 . LEU A 1 222 ? 8.12278   -9.46204  -19.05119 1.000 93.44715  ?  222 LEU A CD1 1 
ATOM 1680 C CD2 . LEU A 1 222 ? 8.01384   -10.74073 -21.19474 1.000 83.34363  ?  222 LEU A CD2 1 
ATOM 1681 N N   . GLU A 1 223 ? 3.47361   -8.04897  -22.33271 1.000 105.50815 ?  223 GLU A N   1 
ATOM 1682 C CA  . GLU A 1 223 ? 2.01331   -8.11342  -22.32959 1.000 99.97719  ?  223 GLU A CA  1 
ATOM 1683 C C   . GLU A 1 223 ? 1.45386   -9.03900  -23.40213 1.000 103.44251 ?  223 GLU A C   1 
ATOM 1684 O O   . GLU A 1 223 ? 0.29237   -9.44655  -23.29645 1.000 119.33374 ?  223 GLU A O   1 
ATOM 1685 C CB  . GLU A 1 223 ? 1.41569   -6.72545  -22.51680 1.000 98.10123  ?  223 GLU A CB  1 
ATOM 1686 C CG  . GLU A 1 223 ? 1.59674   -5.82830  -21.32691 1.000 104.06013 ?  223 GLU A CG  1 
ATOM 1687 C CD  . GLU A 1 223 ? 0.66973   -4.64851  -21.37761 1.000 118.55097 ?  223 GLU A CD  1 
ATOM 1688 O OE1 . GLU A 1 223 ? -0.16273  -4.59561  -22.31019 1.000 121.70488 ?  223 GLU A OE1 1 
ATOM 1689 O OE2 . GLU A 1 223 ? 0.77892   -3.77463  -20.49358 1.000 127.34381 -1 223 GLU A OE2 1 
ATOM 1690 N N   . ASN A 1 224 ? 2.23540   -9.36238  -24.43421 1.000 103.50643 ?  224 ASN A N   1 
ATOM 1691 C CA  . ASN A 1 224 ? 1.82582   -10.26990 -25.50712 1.000 95.23495  ?  224 ASN A CA  1 
ATOM 1692 C C   . ASN A 1 224 ? 0.54917   -9.80446  -26.21068 1.000 106.24982 ?  224 ASN A C   1 
ATOM 1693 O O   . ASN A 1 224 ? -0.15930  -10.61337 -26.81837 1.000 101.24784 ?  224 ASN A O   1 
ATOM 1694 C CB  . ASN A 1 224 ? 1.64368   -11.69752 -24.97549 1.000 91.32169  ?  224 ASN A CB  1 
ATOM 1695 C CG  . ASN A 1 224 ? 1.72280   -12.75044 -26.06868 1.000 104.97301 ?  224 ASN A CG  1 
ATOM 1696 O OD1 . ASN A 1 224 ? 2.22502   -12.49500 -27.16446 1.000 96.14483  ?  224 ASN A OD1 1 
ATOM 1697 N ND2 . ASN A 1 224 ? 1.20581   -13.93992 -25.77782 1.000 107.13337 ?  224 ASN A ND2 1 
ATOM 1698 N N   . SER A 1 225 ? 0.23056   -8.51123  -26.13322 1.000 108.94110 ?  225 SER A N   1 
ATOM 1699 C CA  . SER A 1 225 ? -0.96556  -7.95483  -26.75347 1.000 107.59534 ?  225 SER A CA  1 
ATOM 1700 C C   . SER A 1 225 ? -0.63604  -6.97092  -27.86650 1.000 111.31445 ?  225 SER A C   1 
ATOM 1701 O O   . SER A 1 225 ? -1.54949  -6.34634  -28.41643 1.000 116.19193 ?  225 SER A O   1 
ATOM 1702 C CB  . SER A 1 225 ? -1.84729  -7.25284  -25.70936 1.000 100.08117 ?  225 SER A CB  1 
ATOM 1703 O OG  . SER A 1 225 ? -2.36031  -8.14546  -24.74018 1.000 100.31490 ?  225 SER A OG  1 
ATOM 1704 N N   . TYR A 1 226 ? 0.63698   -6.82548  -28.22612 1.000 99.10399  ?  226 TYR A N   1 
ATOM 1705 C CA  . TYR A 1 226 ? 1.04118   -5.76984  -29.14044 1.000 93.33171  ?  226 TYR A CA  1 
ATOM 1706 C C   . TYR A 1 226 ? 2.15272   -6.25545  -30.04948 1.000 90.87189  ?  226 TYR A C   1 
ATOM 1707 O O   . TYR A 1 226 ? 3.04936   -6.98702  -29.62520 1.000 83.59446  ?  226 TYR A O   1 
ATOM 1708 C CB  . TYR A 1 226 ? 1.48972   -4.51319  -28.37701 1.000 83.28961  ?  226 TYR A CB  1 
ATOM 1709 C CG  . TYR A 1 226 ? 0.35296   -3.89033  -27.61544 1.000 82.82456  ?  226 TYR A CG  1 
ATOM 1710 C CD1 . TYR A 1 226 ? -0.62546  -3.16162  -28.27957 1.000 84.57475  ?  226 TYR A CD1 1 
ATOM 1711 C CD2 . TYR A 1 226 ? 0.22165   -4.07230  -26.24781 1.000 73.42846  ?  226 TYR A CD2 1 
ATOM 1712 C CE1 . TYR A 1 226 ? -1.68442  -2.60820  -27.60291 1.000 69.69189  ?  226 TYR A CE1 1 
ATOM 1713 C CE2 . TYR A 1 226 ? -0.83812  -3.51975  -25.55764 1.000 78.41119  ?  226 TYR A CE2 1 
ATOM 1714 C CZ  . TYR A 1 226 ? -1.79029  -2.78825  -26.24152 1.000 79.81839  ?  226 TYR A CZ  1 
ATOM 1715 O OH  . TYR A 1 226 ? -2.85729  -2.22962  -25.56806 1.000 78.64396  ?  226 TYR A OH  1 
ATOM 1716 N N   . GLN A 1 227 ? 2.10348   -5.79974  -31.29164 1.000 94.75242  ?  227 GLN A N   1 
ATOM 1717 C CA  . GLN A 1 227 ? 3.12390   -6.13954  -32.25584 1.000 75.27752  ?  227 GLN A CA  1 
ATOM 1718 C C   . GLN A 1 227 ? 4.35898   -5.29489  -31.98482 1.000 69.47894  ?  227 GLN A C   1 
ATOM 1719 O O   . GLN A 1 227 ? 4.29808   -4.27659  -31.29334 1.000 79.31175  ?  227 GLN A O   1 
ATOM 1720 C CB  . GLN A 1 227 ? 2.61166   -5.87282  -33.66898 1.000 75.43758  ?  227 GLN A CB  1 
ATOM 1721 C CG  . GLN A 1 227 ? 1.44402   -6.74887  -34.09945 1.000 90.63385  ?  227 GLN A CG  1 
ATOM 1722 C CD  . GLN A 1 227 ? 1.73101   -8.23463  -34.04225 1.000 117.61497 ?  227 GLN A CD  1 
ATOM 1723 O OE1 . GLN A 1 227 ? 2.88331   -8.66341  -34.07021 1.000 132.33461 ?  227 GLN A OE1 1 
ATOM 1724 N NE2 . GLN A 1 227 ? 0.67233   -9.03363  -33.97241 1.000 119.81808 ?  227 GLN A NE2 1 
ATOM 1725 N N   . ILE A 1 228 ? 5.49342   -5.73142  -32.53206 1.000 82.57455  ?  228 ILE A N   1 
ATOM 1726 C CA  . ILE A 1 228 ? 6.73174   -4.97734  -32.34929 1.000 79.74430  ?  228 ILE A CA  1 
ATOM 1727 C C   . ILE A 1 228 ? 6.63434   -3.62629  -33.04661 1.000 70.36570  ?  228 ILE A C   1 
ATOM 1728 O O   . ILE A 1 228 ? 7.18112   -2.62444  -32.57281 1.000 69.51996  ?  228 ILE A O   1 
ATOM 1729 C CB  . ILE A 1 228 ? 7.94118   -5.79335  -32.84540 1.000 79.34582  ?  228 ILE A CB  1 
ATOM 1730 C CG1 . ILE A 1 228 ? 8.18466   -7.00164  -31.94198 1.000 84.07814  ?  228 ILE A CG1 1 
ATOM 1731 C CG2 . ILE A 1 228 ? 9.19260   -4.93842  -32.87274 1.000 84.35999  ?  228 ILE A CG2 1 
ATOM 1732 C CD1 . ILE A 1 228 ? 8.54315   -6.62234  -30.52895 1.000 90.46990  ?  228 ILE A CD1 1 
ATOM 1733 N N   . SER A 1 229 ? 5.94469   -3.57809  -34.18700 1.000 76.85334  ?  229 SER A N   1 
ATOM 1734 C CA  . SER A 1 229 ? 5.66702   -2.29733  -34.82562 1.000 70.06207  ?  229 SER A CA  1 
ATOM 1735 C C   . SER A 1 229 ? 4.79040   -1.43013  -33.93453 1.000 74.90754  ?  229 SER A C   1 
ATOM 1736 O O   . SER A 1 229 ? 5.01632   -0.21547  -33.81421 1.000 75.58559  ?  229 SER A O   1 
ATOM 1737 C CB  . SER A 1 229 ? 5.00511   -2.52536  -36.18065 1.000 74.42509  ?  229 SER A CB  1 
ATOM 1738 O OG  . SER A 1 229 ? 3.89667   -3.39693  -36.05307 1.000 84.85932  ?  229 SER A OG  1 
ATOM 1739 N N   . GLN A 1 230 ? 3.78651   -2.04391  -33.29416 1.000 82.96369  ?  230 GLN A N   1 
ATOM 1740 C CA  . GLN A 1 230 ? 2.92595   -1.30861  -32.37255 1.000 67.44821  ?  230 GLN A CA  1 
ATOM 1741 C C   . GLN A 1 230 ? 3.72193   -0.78969  -31.18811 1.000 66.39214  ?  230 GLN A C   1 
ATOM 1742 O O   . GLN A 1 230 ? 3.62268   0.38804   -30.83498 1.000 62.57748  ?  230 GLN A O   1 
ATOM 1743 C CB  . GLN A 1 230 ? 1.77034   -2.18555  -31.88738 1.000 72.08461  ?  230 GLN A CB  1 
ATOM 1744 C CG  . GLN A 1 230 ? 0.90081   -2.78198  -32.97760 1.000 74.01516  ?  230 GLN A CG  1 
ATOM 1745 C CD  . GLN A 1 230 ? -0.32971  -3.47018  -32.41296 1.000 81.05710  ?  230 GLN A CD  1 
ATOM 1746 O OE1 . GLN A 1 230 ? -0.36117  -4.69091  -32.26151 1.000 80.55660  ?  230 GLN A OE1 1 
ATOM 1747 N NE2 . GLN A 1 230 ? -1.35706  -2.68538  -32.10934 1.000 81.89827  ?  230 GLN A NE2 1 
ATOM 1748 N N   . ILE A 1 231 ? 4.51138   -1.66528  -30.55666 1.000 74.76643  ?  231 ILE A N   1 
ATOM 1749 C CA  . ILE A 1 231 ? 5.37163   -1.26000  -29.44410 1.000 65.07457  ?  231 ILE A CA  1 
ATOM 1750 C C   . ILE A 1 231 ? 6.24997   -0.08286  -29.84811 1.000 69.12068  ?  231 ILE A C   1 
ATOM 1751 O O   . ILE A 1 231 ? 6.30849   0.94650   -29.15645 1.000 71.36511  ?  231 ILE A O   1 
ATOM 1752 C CB  . ILE A 1 231 ? 6.21831   -2.45501  -28.97053 1.000 59.49653  ?  231 ILE A CB  1 
ATOM 1753 C CG1 . ILE A 1 231 ? 5.32611   -3.49360  -28.28614 1.000 71.06655  ?  231 ILE A CG1 1 
ATOM 1754 C CG2 . ILE A 1 231 ? 7.34948   -1.98752  -28.05777 1.000 65.34081  ?  231 ILE A CG2 1 
ATOM 1755 C CD1 . ILE A 1 231 ? 5.82289   -4.89667  -28.40719 1.000 81.34140  ?  231 ILE A CD1 1 
ATOM 1756 N N   . SER A 1 232 ? 6.93702   -0.22305  -30.98741 1.000 65.11750  ?  232 SER A N   1 
ATOM 1757 C CA  . SER A 1 232 ? 7.83084   0.81702   -31.48278 1.000 63.62728  ?  232 SER A CA  1 
ATOM 1758 C C   . SER A 1 232 ? 7.11025   2.14897   -31.61101 1.000 62.39046  ?  232 SER A C   1 
ATOM 1759 O O   . SER A 1 232 ? 7.56877   3.16640   -31.08096 1.000 75.45936  ?  232 SER A O   1 
ATOM 1760 C CB  . SER A 1 232 ? 8.43663   0.39560   -32.82407 1.000 74.56281  ?  232 SER A CB  1 
ATOM 1761 O OG  . SER A 1 232 ? 7.59015   0.74936   -33.90532 1.000 95.24261  ?  232 SER A OG  1 
ATOM 1762 N N   . ASN A 1 233 ? 5.98471   2.16871   -32.33037 1.000 67.97125  ?  233 ASN A N   1 
ATOM 1763 C CA  . ASN A 1 233 ? 5.26507   3.42769   -32.50367 1.000 74.76582  ?  233 ASN A CA  1 
ATOM 1764 C C   . ASN A 1 233 ? 4.74861   3.97374   -31.17538 1.000 81.13661  ?  233 ASN A C   1 
ATOM 1765 O O   . ASN A 1 233 ? 4.57490   5.19179   -31.02321 1.000 76.62625  ?  233 ASN A O   1 
ATOM 1766 C CB  . ASN A 1 233 ? 4.11579   3.25702   -33.48621 1.000 66.70480  ?  233 ASN A CB  1 
ATOM 1767 C CG  . ASN A 1 233 ? 3.72567   4.56097   -34.13044 1.000 81.93147  ?  233 ASN A CG  1 
ATOM 1768 O OD1 . ASN A 1 233 ? 2.86800   5.28091   -33.61981 1.000 90.43012  ?  233 ASN A OD1 1 
ATOM 1769 N ND2 . ASN A 1 233 ? 4.35891   4.88286   -35.25715 1.000 96.38613  ?  233 ASN A ND2 1 
ATOM 1770 N N   . MET A 1 234 ? 4.46860   3.08930   -30.21836 1.000 66.05984  ?  234 MET A N   1 
ATOM 1771 C CA  . MET A 1 234 ? 3.93209   3.52035   -28.93633 1.000 58.63924  ?  234 MET A CA  1 
ATOM 1772 C C   . MET A 1 234 ? 4.98140   4.26494   -28.12326 1.000 70.15263  ?  234 MET A C   1 
ATOM 1773 O O   . MET A 1 234 ? 4.73674   5.37864   -27.64440 1.000 80.28138  ?  234 MET A O   1 
ATOM 1774 C CB  . MET A 1 234 ? 3.40900   2.29685   -28.18571 1.000 59.85945  ?  234 MET A CB  1 
ATOM 1775 C CG  . MET A 1 234 ? 2.11151   1.76750   -28.76233 1.000 59.02530  ?  234 MET A CG  1 
ATOM 1776 S SD  . MET A 1 234 ? 1.63326   0.15110   -28.12014 1.000 80.05801  ?  234 MET A SD  1 
ATOM 1777 C CE  . MET A 1 234 ? 1.04709   0.59992   -26.49201 1.000 75.78059  ?  234 MET A CE  1 
ATOM 1778 N N   . ILE A 1 235 ? 6.16890   3.67579   -27.96967 1.000 83.77703  ?  235 ILE A N   1 
ATOM 1779 C CA  . ILE A 1 235 ? 7.17556   4.32058   -27.13153 1.000 82.19812  ?  235 ILE A CA  1 
ATOM 1780 C C   . ILE A 1 235 ? 7.77088   5.55320   -27.79725 1.000 84.27075  ?  235 ILE A C   1 
ATOM 1781 O O   . ILE A 1 235 ? 8.38849   6.37832   -27.11627 1.000 95.06763  ?  235 ILE A O   1 
ATOM 1782 C CB  . ILE A 1 235 ? 8.29503   3.33445   -26.74397 1.000 78.19566  ?  235 ILE A CB  1 
ATOM 1783 C CG1 . ILE A 1 235 ? 8.88323   2.68583   -27.99167 1.000 81.52710  ?  235 ILE A CG1 1 
ATOM 1784 C CG2 . ILE A 1 235 ? 7.79913   2.28926   -25.76518 1.000 78.94825  ?  235 ILE A CG2 1 
ATOM 1785 C CD1 . ILE A 1 235 ? 9.84669   1.56805   -27.68761 1.000 81.78558  ?  235 ILE A CD1 1 
ATOM 1786 N N   . GLY A 1 236 ? 7.58995   5.71652   -29.09792 1.000 86.15936  ?  236 GLY A N   1 
ATOM 1787 C CA  . GLY A 1 236 ? 8.08950   6.86833   -29.80794 1.000 88.80788  ?  236 GLY A CA  1 
ATOM 1788 C C   . GLY A 1 236 ? 9.19972   6.59690   -30.81106 1.000 84.59183  ?  236 GLY A C   1 
ATOM 1789 O O   . GLY A 1 236 ? 9.93480   7.52980   -31.15244 1.000 99.03915  ?  236 GLY A O   1 
ATOM 1790 N N   . ILE A 1 237 ? 9.36046   5.35863   -31.26661 1.000 79.17812  ?  237 ILE A N   1 
ATOM 1791 C CA  . ILE A 1 237 ? 10.41510  4.98934   -32.20331 1.000 89.02302  ?  237 ILE A CA  1 
ATOM 1792 C C   . ILE A 1 237 ? 9.80598   4.82978   -33.58898 1.000 96.82485  ?  237 ILE A C   1 
ATOM 1793 O O   . ILE A 1 237 ? 8.75462   4.19588   -33.74791 1.000 86.87461  ?  237 ILE A O   1 
ATOM 1794 C CB  . ILE A 1 237 ? 11.13574  3.70762   -31.75080 1.000 86.74838  ?  237 ILE A CB  1 
ATOM 1795 C CG1 . ILE A 1 237 ? 11.93014  3.98782   -30.46912 1.000 84.73992  ?  237 ILE A CG1 1 
ATOM 1796 C CG2 . ILE A 1 237 ? 12.01806  3.14218   -32.86601 1.000 85.83192  ?  237 ILE A CG2 1 
ATOM 1797 C CD1 . ILE A 1 237 ? 12.79149  2.82737   -30.00382 1.000 90.09958  ?  237 ILE A CD1 1 
ATOM 1798 N N   . SER A 1 238 ? 10.48074  5.39452   -34.59181 1.000 119.82722 ?  238 SER A N   1 
ATOM 1799 C CA  . SER A 1 238 ? 9.94095   5.46120   -35.94733 1.000 128.49490 ?  238 SER A CA  1 
ATOM 1800 C C   . SER A 1 238 ? 9.82454   4.07926   -36.58958 1.000 128.61879 ?  238 SER A C   1 
ATOM 1801 O O   . SER A 1 238 ? 8.72293   3.62590   -36.92441 1.000 127.28940 ?  238 SER A O   1 
ATOM 1802 C CB  . SER A 1 238 ? 10.81702  6.39296   -36.78581 1.000 129.12431 ?  238 SER A CB  1 
ATOM 1803 O OG  . SER A 1 238 ? 12.17797  6.27539   -36.39510 1.000 121.88103 ?  238 SER A OG  1 
ATOM 1804 N N   . SER A 1 239 ? 10.95109  3.41081   -36.80780 1.000 110.00051 ?  239 SER A N   1 
ATOM 1805 C CA  . SER A 1 239 ? 10.94421  2.11920   -37.47594 1.000 98.37521  ?  239 SER A CA  1 
ATOM 1806 C C   . SER A 1 239 ? 10.90855  0.97824   -36.46483 1.000 93.59590  ?  239 SER A C   1 
ATOM 1807 O O   . SER A 1 239 ? 11.18042  1.15813   -35.27742 1.000 98.53968  ?  239 SER A O   1 
ATOM 1808 C CB  . SER A 1 239 ? 12.16768  1.97275   -38.37789 1.000 102.85655 ?  239 SER A CB  1 
ATOM 1809 O OG  . SER A 1 239 ? 12.39410  0.60927   -38.69339 1.000 107.28809 ?  239 SER A OG  1 
ATOM 1810 N N   . ALA A 1 240 ? 10.55064  -0.21123  -36.95754 1.000 97.12635  ?  240 ALA A N   1 
ATOM 1811 C CA  . ALA A 1 240 ? 10.58045  -1.40867  -36.12429 1.000 90.17084  ?  240 ALA A CA  1 
ATOM 1812 C C   . ALA A 1 240 ? 11.97627  -2.02596  -36.05138 1.000 95.57221  ?  240 ALA A C   1 
ATOM 1813 O O   . ALA A 1 240 ? 12.41669  -2.43495  -34.97024 1.000 106.78171 ?  240 ALA A O   1 
ATOM 1814 C CB  . ALA A 1 240 ? 9.57643   -2.43288  -36.64760 1.000 96.86398  ?  240 ALA A CB  1 
ATOM 1815 N N   . SER A 1 241 ? 12.67809  -2.12323  -37.18429 1.000 99.35198  ?  241 SER A N   1 
ATOM 1816 C CA  . SER A 1 241 ? 14.04654  -2.63840  -37.16756 1.000 100.32680 ?  241 SER A CA  1 
ATOM 1817 C C   . SER A 1 241 ? 14.93562  -1.80205  -36.25235 1.000 99.35218  ?  241 SER A C   1 
ATOM 1818 O O   . SER A 1 241 ? 15.74437  -2.34050  -35.48272 1.000 100.10508 ?  241 SER A O   1 
ATOM 1819 C CB  . SER A 1 241 ? 14.61397  -2.68415  -38.58923 1.000 119.41626 ?  241 SER A CB  1 
ATOM 1820 O OG  . SER A 1 241 ? 14.76348  -1.38762  -39.13779 1.000 120.00629 ?  241 SER A OG  1 
ATOM 1821 N N   . TYR A 1 242 ? 14.82746  -0.47629  -36.36332 1.000 78.55234  ?  242 TYR A N   1 
ATOM 1822 C CA  . TYR A 1 242 ? 15.52417  0.42672   -35.45551 1.000 80.32336  ?  242 TYR A CA  1 
ATOM 1823 C C   . TYR A 1 242 ? 15.23057  0.09023   -33.99803 1.000 85.92341  ?  242 TYR A C   1 
ATOM 1824 O O   . TYR A 1 242 ? 16.14382  0.02777   -33.16554 1.000 93.36106  ?  242 TYR A O   1 
ATOM 1825 C CB  . TYR A 1 242 ? 15.12658  1.86743   -35.76164 1.000 86.86972  ?  242 TYR A CB  1 
ATOM 1826 C CG  . TYR A 1 242 ? 16.03941  2.88366   -35.13176 1.000 90.31913  ?  242 TYR A CG  1 
ATOM 1827 C CD1 . TYR A 1 242 ? 17.41401  2.77556   -35.25166 1.000 103.71534 ?  242 TYR A CD1 1 
ATOM 1828 C CD2 . TYR A 1 242 ? 15.52643  3.95338   -34.41599 1.000 105.52907 ?  242 TYR A CD2 1 
ATOM 1829 C CE1 . TYR A 1 242 ? 18.25429  3.70516   -34.67567 1.000 115.13116 ?  242 TYR A CE1 1 
ATOM 1830 C CE2 . TYR A 1 242 ? 16.35795  4.89149   -33.83913 1.000 101.48516 ?  242 TYR A CE2 1 
ATOM 1831 C CZ  . TYR A 1 242 ? 17.72036  4.76078   -33.96728 1.000 109.11318 ?  242 TYR A CZ  1 
ATOM 1832 O OH  . TYR A 1 242 ? 18.55144  5.69191   -33.38597 1.000 138.47495 ?  242 TYR A OH  1 
ATOM 1833 N N   . PHE A 1 243 ? 13.95042  -0.08773  -33.66242 1.000 79.92940  ?  243 PHE A N   1 
ATOM 1834 C CA  . PHE A 1 243 ? 13.59614  -0.43611  -32.29283 1.000 68.48755  ?  243 PHE A CA  1 
ATOM 1835 C C   . PHE A 1 243 ? 14.27345  -1.72764  -31.85668 1.000 73.58218  ?  243 PHE A C   1 
ATOM 1836 O O   . PHE A 1 243 ? 14.76923  -1.82411  -30.72883 1.000 86.72964  ?  243 PHE A O   1 
ATOM 1837 C CB  . PHE A 1 243 ? 12.08653  -0.56504  -32.12582 1.000 83.41112  ?  243 PHE A CB  1 
ATOM 1838 C CG  . PHE A 1 243 ? 11.69819  -1.28148  -30.86276 1.000 77.68437  ?  243 PHE A CG  1 
ATOM 1839 C CD1 . PHE A 1 243 ? 11.84829  -0.66632  -29.63496 1.000 62.35585  ?  243 PHE A CD1 1 
ATOM 1840 C CD2 . PHE A 1 243 ? 11.22757  -2.58165  -30.90089 1.000 63.91113  ?  243 PHE A CD2 1 
ATOM 1841 C CE1 . PHE A 1 243 ? 11.51555  -1.32305  -28.48590 1.000 67.67115  ?  243 PHE A CE1 1 
ATOM 1842 C CE2 . PHE A 1 243 ? 10.89720  -3.23814  -29.75109 1.000 56.53266  ?  243 PHE A CE2 1 
ATOM 1843 C CZ  . PHE A 1 243 ? 11.03922  -2.60884  -28.54171 1.000 67.10753  ?  243 PHE A CZ  1 
ATOM 1844 N N   . ILE A 1 244 ? 14.24401  -2.75635  -32.70835 1.000 69.21035  ?  244 ILE A N   1 
ATOM 1845 C CA  . ILE A 1 244 ? 14.84821  -4.03368  -32.32738 1.000 69.45062  ?  244 ILE A CA  1 
ATOM 1846 C C   . ILE A 1 244 ? 16.33845  -3.86015  -32.06431 1.000 77.97647  ?  244 ILE A C   1 
ATOM 1847 O O   . ILE A 1 244 ? 16.87793  -4.38800  -31.07933 1.000 88.57546  ?  244 ILE A O   1 
ATOM 1848 C CB  . ILE A 1 244 ? 14.58582  -5.11418  -33.39426 1.000 77.99145  ?  244 ILE A CB  1 
ATOM 1849 C CG1 . ILE A 1 244 ? 13.08816  -5.30997  -33.64790 1.000 71.09772  ?  244 ILE A CG1 1 
ATOM 1850 C CG2 . ILE A 1 244 ? 15.16923  -6.43391  -32.95308 1.000 65.47037  ?  244 ILE A CG2 1 
ATOM 1851 C CD1 . ILE A 1 244 ? 12.80682  -6.42406  -34.65584 1.000 69.04080  ?  244 ILE A CD1 1 
ATOM 1852 N N   . ARG A 1 245 ? 17.02606  -3.10821  -32.92839 1.000 86.57260  ?  245 ARG A N   1 
ATOM 1853 C CA  . ARG A 1 245 ? 18.45439  -2.88221  -32.71724 1.000 88.82948  ?  245 ARG A CA  1 
ATOM 1854 C C   . ARG A 1 245 ? 18.70975  -2.13775  -31.41056 1.000 94.11737  ?  245 ARG A C   1 
ATOM 1855 O O   . ARG A 1 245 ? 19.64895  -2.47144  -30.67625 1.000 99.73020  ?  245 ARG A O   1 
ATOM 1856 C CB  . ARG A 1 245 ? 19.06214  -2.12329  -33.89709 1.000 85.82644  ?  245 ARG A CB  1 
ATOM 1857 C CG  . ARG A 1 245 ? 18.92616  -2.83751  -35.22224 1.000 98.53046  ?  245 ARG A CG  1 
ATOM 1858 C CD  . ARG A 1 245 ? 19.78083  -2.18752  -36.29313 1.000 117.67489 ?  245 ARG A CD  1 
ATOM 1859 N NE  . ARG A 1 245 ? 19.55285  -0.74971  -36.39284 1.000 114.76085 ?  245 ARG A NE  1 
ATOM 1860 C CZ  . ARG A 1 245 ? 18.91634  -0.15902  -37.39609 1.000 110.33363 ?  245 ARG A CZ  1 
ATOM 1861 N NH1 . ARG A 1 245 ? 18.26614  -0.86077  -38.31228 1.000 101.96394 ?  245 ARG A NH1 1 
ATOM 1862 N NH2 . ARG A 1 245 ? 18.89888  1.16939   -37.46031 1.000 114.58582 ?  245 ARG A NH2 1 
ATOM 1863 N N   . ILE A 1 246 ? 17.88263  -1.13473  -31.09163 1.000 71.40382  ?  246 ILE A N   1 
ATOM 1864 C CA  . ILE A 1 246 ? 18.10968  -0.38175  -29.85733 1.000 74.65009  ?  246 ILE A CA  1 
ATOM 1865 C C   . ILE A 1 246 ? 17.83598  -1.24714  -28.63086 1.000 72.30671  ?  246 ILE A C   1 
ATOM 1866 O O   . ILE A 1 246 ? 18.58895  -1.20659  -27.65062 1.000 63.18670  ?  246 ILE A O   1 
ATOM 1867 C CB  . ILE A 1 246 ? 17.26913  0.90693   -29.83344 1.000 65.49202  ?  246 ILE A CB  1 
ATOM 1868 C CG1 . ILE A 1 246 ? 17.63996  1.81631   -30.99146 1.000 67.97051  ?  246 ILE A CG1 1 
ATOM 1869 C CG2 . ILE A 1 246 ? 17.50868  1.67255   -28.55121 1.000 72.76071  ?  246 ILE A CG2 1 
ATOM 1870 C CD1 . ILE A 1 246 ? 16.83175  3.08260   -30.99660 1.000 87.50934  ?  246 ILE A CD1 1 
ATOM 1871 N N   . PHE A 1 247 ? 16.74875  -2.02412  -28.65470 1.000 66.27223  ?  247 PHE A N   1 
ATOM 1872 C CA  . PHE A 1 247 ? 16.44961  -2.93412  -27.55103 1.000 65.12713  ?  247 PHE A CA  1 
ATOM 1873 C C   . PHE A 1 247 ? 17.61229  -3.88593  -27.31029 1.000 67.75630  ?  247 PHE A C   1 
ATOM 1874 O O   . PHE A 1 247 ? 18.01040  -4.12191  -26.16111 1.000 64.98481  ?  247 PHE A O   1 
ATOM 1875 C CB  . PHE A 1 247 ? 15.16090  -3.69543  -27.85801 1.000 67.63933  ?  247 PHE A CB  1 
ATOM 1876 C CG  . PHE A 1 247 ? 14.62200  -4.52085  -26.71333 1.000 64.70035  ?  247 PHE A CG  1 
ATOM 1877 C CD1 . PHE A 1 247 ? 15.12239  -5.79074  -26.44771 1.000 62.10779  ?  247 PHE A CD1 1 
ATOM 1878 C CD2 . PHE A 1 247 ? 13.57095  -4.05090  -25.94346 1.000 62.44927  ?  247 PHE A CD2 1 
ATOM 1879 C CE1 . PHE A 1 247 ? 14.60381  -6.56134  -25.42041 1.000 55.55196  ?  247 PHE A CE1 1 
ATOM 1880 C CE2 . PHE A 1 247 ? 13.04734  -4.81983  -24.91274 1.000 62.47482  ?  247 PHE A CE2 1 
ATOM 1881 C CZ  . PHE A 1 247 ? 13.56841  -6.07220  -24.64809 1.000 55.05209  ?  247 PHE A CZ  1 
ATOM 1882 N N   . ASN A 1 248 ? 18.18544  -4.42683  -28.38601 1.000 67.21829  ?  248 ASN A N   1 
ATOM 1883 C CA  . ASN A 1 248 ? 19.35034  -5.28649  -28.22553 1.000 70.78121  ?  248 ASN A CA  1 
ATOM 1884 C C   . ASN A 1 248 ? 20.51982  -4.51986  -27.60518 1.000 71.22105  ?  248 ASN A C   1 
ATOM 1885 O O   . ASN A 1 248 ? 21.11334  -4.96905  -26.61873 1.000 68.97018  ?  248 ASN A O   1 
ATOM 1886 C CB  . ASN A 1 248 ? 19.74954  -5.88712  -29.57359 1.000 71.65871  ?  248 ASN A CB  1 
ATOM 1887 C CG  . ASN A 1 248 ? 20.46108  -7.22177  -29.42916 1.000 68.42473  ?  248 ASN A CG  1 
ATOM 1888 O OD1 . ASN A 1 248 ? 20.60416  -7.74707  -28.32469 1.000 71.60384  ?  248 ASN A OD1 1 
ATOM 1889 N ND2 . ASN A 1 248 ? 20.95563  -7.75088  -30.54144 1.000 76.55644  ?  248 ASN A ND2 1 
ATOM 1890 N N   . LYS A 1 249 ? 20.85294  -3.34644  -28.15911 1.000 69.31308  ?  249 LYS A N   1 
ATOM 1891 C CA  . LYS A 1 249 ? 22.00077  -2.58021  -27.66800 1.000 64.14471  ?  249 LYS A CA  1 
ATOM 1892 C C   . LYS A 1 249 ? 21.86572  -2.21495  -26.20268 1.000 63.29812  ?  249 LYS A C   1 
ATOM 1893 O O   . LYS A 1 249 ? 22.86882  -2.13489  -25.48436 1.000 83.35669  ?  249 LYS A O   1 
ATOM 1894 C CB  . LYS A 1 249 ? 22.17840  -1.30802  -28.49008 1.000 76.07447  ?  249 LYS A CB  1 
ATOM 1895 C CG  . LYS A 1 249 ? 23.28650  -0.39645  -28.00280 1.000 71.83952  ?  249 LYS A CG  1 
ATOM 1896 C CD  . LYS A 1 249 ? 23.15879  0.96086   -28.66056 1.000 93.29042  ?  249 LYS A CD  1 
ATOM 1897 C CE  . LYS A 1 249 ? 23.35448  0.82126   -30.17897 1.000 110.94616 ?  249 LYS A CE  1 
ATOM 1898 N NZ  . LYS A 1 249 ? 23.25325  2.10153   -30.94393 1.000 100.79287 ?  249 LYS A NZ  1 
ATOM 1899 N N   . HIS A 1 250 ? 20.63876  -2.00416  -25.74190 1.000 80.46401  ?  250 HIS A N   1 
ATOM 1900 C CA  . HIS A 1 250 ? 20.40425  -1.56886  -24.37182 1.000 64.85290  ?  250 HIS A CA  1 
ATOM 1901 C C   . HIS A 1 250 ? 20.41298  -2.75834  -23.41853 1.000 65.74380  ?  250 HIS A C   1 
ATOM 1902 O O   . HIS A 1 250 ? 21.20546  -2.80298  -22.47091 1.000 72.83685  ?  250 HIS A O   1 
ATOM 1903 C CB  . HIS A 1 250 ? 19.07491  -0.81429  -24.30857 1.000 67.92329  ?  250 HIS A CB  1 
ATOM 1904 C CG  . HIS A 1 250 ? 18.73691  -0.26755  -22.95897 1.000 67.80880  ?  250 HIS A CG  1 
ATOM 1905 N ND1 . HIS A 1 250 ? 18.06540  -1.00235  -22.00481 1.000 65.25073  ?  250 HIS A ND1 1 
ATOM 1906 C CD2 . HIS A 1 250 ? 18.92497  0.96146   -22.42326 1.000 66.52132  ?  250 HIS A CD2 1 
ATOM 1907 C CE1 . HIS A 1 250 ? 17.87600  -0.25676  -20.93178 1.000 66.76344  ?  250 HIS A CE1 1 
ATOM 1908 N NE2 . HIS A 1 250 ? 18.39098  0.93904   -21.15877 1.000 69.30909  ?  250 HIS A NE2 1 
ATOM 1909 N N   . TYR A 1 251 ? 19.54062  -3.74051  -23.66453 1.000 58.54538  ?  251 TYR A N   1 
ATOM 1910 C CA  . TYR A 1 251 ? 19.41934  -4.88506  -22.77211 1.000 58.12315  ?  251 TYR A CA  1 
ATOM 1911 C C   . TYR A 1 251 ? 20.43736  -5.98926  -23.06229 1.000 63.97790  ?  251 TYR A C   1 
ATOM 1912 O O   . TYR A 1 251 ? 20.70325  -6.82401  -22.19043 1.000 59.35717  ?  251 TYR A O   1 
ATOM 1913 C CB  . TYR A 1 251 ? 18.00272  -5.44554  -22.86806 1.000 60.12542  ?  251 TYR A CB  1 
ATOM 1914 C CG  . TYR A 1 251 ? 16.96827  -4.57741  -22.18882 1.000 68.88687  ?  251 TYR A CG  1 
ATOM 1915 C CD1 . TYR A 1 251 ? 16.89934  -4.50691  -20.80876 1.000 60.99013  ?  251 TYR A CD1 1 
ATOM 1916 C CD2 . TYR A 1 251 ? 16.05978  -3.82548  -22.92824 1.000 67.69426  ?  251 TYR A CD2 1 
ATOM 1917 C CE1 . TYR A 1 251 ? 15.95732  -3.72188  -20.17690 1.000 56.60939  ?  251 TYR A CE1 1 
ATOM 1918 C CE2 . TYR A 1 251 ? 15.11319  -3.02972  -22.29864 1.000 66.08050  ?  251 TYR A CE2 1 
ATOM 1919 C CZ  . TYR A 1 251 ? 15.07159  -2.98823  -20.91903 1.000 55.85386  ?  251 TYR A CZ  1 
ATOM 1920 O OH  . TYR A 1 251 ? 14.14548  -2.21117  -20.26719 1.000 62.47537  ?  251 TYR A OH  1 
ATOM 1921 N N   . GLY A 1 252 ? 21.01738  -6.02250  -24.25319 1.000 63.82468  ?  252 GLY A N   1 
ATOM 1922 C CA  . GLY A 1 252 ? 21.91574  -7.09907  -24.59396 1.000 68.72235  ?  252 GLY A CA  1 
ATOM 1923 C C   . GLY A 1 252 ? 21.24274  -8.31288  -25.19543 1.000 70.19138  ?  252 GLY A C   1 
ATOM 1924 O O   . GLY A 1 252 ? 21.93290  -9.28021  -25.53188 1.000 87.20456  ?  252 GLY A O   1 
ATOM 1925 N N   . VAL A 1 253 ? 19.91686  -8.30929  -25.32139 1.000 77.49146  ?  253 VAL A N   1 
ATOM 1926 C CA  . VAL A 1 253 ? 19.18965  -9.42971  -25.89681 1.000 69.51065  ?  253 VAL A CA  1 
ATOM 1927 C C   . VAL A 1 253 ? 18.19278  -8.89368  -26.90992 1.000 65.98694  ?  253 VAL A C   1 
ATOM 1928 O O   . VAL A 1 253 ? 17.78473  -7.73099  -26.87116 1.000 66.01311  ?  253 VAL A O   1 
ATOM 1929 C CB  . VAL A 1 253 ? 18.47087  -10.28576 -24.83063 1.000 63.75172  ?  253 VAL A CB  1 
ATOM 1930 C CG1 . VAL A 1 253 ? 19.49054  -11.04461 -24.00167 1.000 71.69128  ?  253 VAL A CG1 1 
ATOM 1931 C CG2 . VAL A 1 253 ? 17.59976  -9.40890  -23.93030 1.000 71.56880  ?  253 VAL A CG2 1 
ATOM 1932 N N   . THR A 1 254 ? 17.81408  -9.74967  -27.81743 1.000 77.76409  ?  254 THR A N   1 
ATOM 1933 C CA  . THR A 1 254 ? 16.77145  -9.35859  -28.74010 1.000 70.63520  ?  254 THR A CA  1 
ATOM 1934 C C   . THR A 1 254 ? 15.42312  -9.42666  -28.03443 1.000 73.42935  ?  254 THR A C   1 
ATOM 1935 O O   . THR A 1 254 ? 15.26210  -10.17499 -27.06694 1.000 77.75399  ?  254 THR A O   1 
ATOM 1936 C CB  . THR A 1 254 ? 16.77729  -10.25976 -29.97139 1.000 71.89897  ?  254 THR A CB  1 
ATOM 1937 O OG1 . THR A 1 254 ? 15.62774  -9.97835  -30.77559 1.000 97.85401  ?  254 THR A OG1 1 
ATOM 1938 C CG2 . THR A 1 254 ? 16.75925  -11.71503 -29.58243 1.000 69.92131  ?  254 THR A CG2 1 
ATOM 1939 N N   . PRO A 1 255 ? 14.46058  -8.60491  -28.44681 1.000 75.27548  ?  255 PRO A N   1 
ATOM 1940 C CA  . PRO A 1 255 ? 13.10658  -8.75320  -27.89319 1.000 70.50005  ?  255 PRO A CA  1 
ATOM 1941 C C   . PRO A 1 255 ? 12.61666  -10.19772 -27.90144 1.000 75.74509  ?  255 PRO A C   1 
ATOM 1942 O O   . PRO A 1 255 ? 11.86862  -10.59910 -27.00085 1.000 77.28661  ?  255 PRO A O   1 
ATOM 1943 C CB  . PRO A 1 255 ? 12.26662  -7.84327  -28.79863 1.000 60.19609  ?  255 PRO A CB  1 
ATOM 1944 C CG  . PRO A 1 255 ? 13.21565  -6.77515  -29.23556 1.000 57.34846  ?  255 PRO A CG  1 
ATOM 1945 C CD  . PRO A 1 255 ? 14.54625  -7.48825  -29.40801 1.000 65.73234  ?  255 PRO A CD  1 
ATOM 1946 N N   . LYS A 1 256 ? 13.01492  -10.99055 -28.90091 1.000 84.40571  ?  256 LYS A N   1 
ATOM 1947 C CA  . LYS A 1 256 ? 12.66025  -12.40859 -28.92590 1.000 88.08211  ?  256 LYS A CA  1 
ATOM 1948 C C   . LYS A 1 256 ? 13.25836  -13.16425 -27.73727 1.000 98.36741  ?  256 LYS A C   1 
ATOM 1949 O O   . LYS A 1 256 ? 12.54809  -13.89599 -27.04315 1.000 100.65913 ?  256 LYS A O   1 
ATOM 1950 C CB  . LYS A 1 256 ? 13.11304  -13.04216 -30.24473 1.000 91.49536  ?  256 LYS A CB  1 
ATOM 1951 C CG  . LYS A 1 256 ? 12.92966  -14.55695 -30.30582 1.000 91.57392  ?  256 LYS A CG  1 
ATOM 1952 C CD  . LYS A 1 256 ? 14.09276  -15.23069 -31.01829 1.000 113.99781 ?  256 LYS A CD  1 
ATOM 1953 C CE  . LYS A 1 256 ? 14.23412  -16.69058 -30.60330 1.000 112.57616 ?  256 LYS A CE  1 
ATOM 1954 N NZ  . LYS A 1 256 ? 14.44080  -16.84819 -29.13932 1.000 110.66201 ?  256 LYS A NZ  1 
ATOM 1955 N N   . GLN A 1 257 ? 14.57392  -13.03518 -27.51543 1.000 93.13249  ?  257 GLN A N   1 
ATOM 1956 C CA  . GLN A 1 257 ? 15.23131  -13.72258 -26.40012 1.000 83.81617  ?  257 GLN A CA  1 
ATOM 1957 C C   . GLN A 1 257 ? 14.61402  -13.32682 -25.06627 1.000 86.50059  ?  257 GLN A C   1 
ATOM 1958 O O   . GLN A 1 257 ? 14.29457  -14.18167 -24.22830 1.000 87.50674  ?  257 GLN A O   1 
ATOM 1959 C CB  . GLN A 1 257 ? 16.72189  -13.39761 -26.40739 1.000 87.59282  ?  257 GLN A CB  1 
ATOM 1960 C CG  . GLN A 1 257 ? 17.55336  -14.25962 -27.33871 1.000 106.86447 ?  257 GLN A CG  1 
ATOM 1961 C CD  . GLN A 1 257 ? 18.87255  -13.59878 -27.69935 1.000 108.55227 ?  257 GLN A CD  1 
ATOM 1962 O OE1 . GLN A 1 257 ? 19.07566  -12.41538 -27.42710 1.000 103.25060 ?  257 GLN A OE1 1 
ATOM 1963 N NE2 . GLN A 1 257 ? 19.77848  -14.36081 -28.30445 1.000 125.37356 ?  257 GLN A NE2 1 
ATOM 1964 N N   . PHE A 1 258 ? 14.47900  -12.02045 -24.84343 1.000 86.45843  ?  258 PHE A N   1 
ATOM 1965 C CA  . PHE A 1 258 ? 13.81367  -11.50225 -23.65718 1.000 82.31618  ?  258 PHE A CA  1 
ATOM 1966 C C   . PHE A 1 258 ? 12.42920  -12.11985 -23.47300 1.000 85.45870  ?  258 PHE A C   1 
ATOM 1967 O O   . PHE A 1 258 ? 12.12652  -12.69512 -22.42245 1.000 86.47171  ?  258 PHE A O   1 
ATOM 1968 C CB  . PHE A 1 258 ? 13.73331  -9.97853  -23.76129 1.000 69.88622  ?  258 PHE A CB  1 
ATOM 1969 C CG  . PHE A 1 258 ? 13.11191  -9.32605  -22.57199 1.000 73.94785  ?  258 PHE A CG  1 
ATOM 1970 C CD1 . PHE A 1 258 ? 13.86277  -9.06096  -21.44286 1.000 77.97298  ?  258 PHE A CD1 1 
ATOM 1971 C CD2 . PHE A 1 258 ? 11.78321  -8.95286  -22.59252 1.000 71.47369  ?  258 PHE A CD2 1 
ATOM 1972 C CE1 . PHE A 1 258 ? 13.28991  -8.46001  -20.35400 1.000 86.81883  ?  258 PHE A CE1 1 
ATOM 1973 C CE2 . PHE A 1 258 ? 11.20705  -8.34568  -21.50453 1.000 72.23412  ?  258 PHE A CE2 1 
ATOM 1974 C CZ  . PHE A 1 258 ? 11.95681  -8.09843  -20.38714 1.000 76.22216  ?  258 PHE A CZ  1 
ATOM 1975 N N   . PHE A 1 259 ? 11.57864  -12.01743 -24.49857 1.000 82.80546  ?  259 PHE A N   1 
ATOM 1976 C CA  . PHE A 1 259 ? 10.21207  -12.52639 -24.40488 1.000 86.55658  ?  259 PHE A CA  1 
ATOM 1977 C C   . PHE A 1 259 ? 10.18999  -14.02574 -24.11137 1.000 93.10324  ?  259 PHE A C   1 
ATOM 1978 O O   . PHE A 1 259 ? 9.45467   -14.48745 -23.22906 1.000 91.34818  ?  259 PHE A O   1 
ATOM 1979 C CB  . PHE A 1 259 ? 9.45449   -12.21384 -25.69514 1.000 92.63089  ?  259 PHE A CB  1 
ATOM 1980 C CG  . PHE A 1 259 ? 7.98303   -12.49567 -25.61410 1.000 103.21078 ?  259 PHE A CG  1 
ATOM 1981 C CD1 . PHE A 1 259 ? 7.12088   -11.58726 -25.02661 1.000 94.37104  ?  259 PHE A CD1 1 
ATOM 1982 C CD2 . PHE A 1 259 ? 7.46541   -13.68692 -26.09726 1.000 111.72175 ?  259 PHE A CD2 1 
ATOM 1983 C CE1 . PHE A 1 259 ? 5.76862   -11.85409 -24.94362 1.000 100.90771 ?  259 PHE A CE1 1 
ATOM 1984 C CE2 . PHE A 1 259 ? 6.11268   -13.95741 -26.01356 1.000 107.76200 ?  259 PHE A CE2 1 
ATOM 1985 C CZ  . PHE A 1 259 ? 5.26425   -13.03931 -25.43683 1.000 108.17942 ?  259 PHE A CZ  1 
ATOM 1986 N N   . THR A 1 260 ? 10.95980  -14.80756 -24.87653 1.000 90.28438  ?  260 THR A N   1 
ATOM 1987 C CA  . THR A 1 260 ? 10.97507  -16.25986 -24.71504 1.000 91.48738  ?  260 THR A CA  1 
ATOM 1988 C C   . THR A 1 260 ? 11.45873  -16.67087 -23.33438 1.000 92.65077  ?  260 THR A C   1 
ATOM 1989 O O   . THR A 1 260 ? 11.00726  -17.69250 -22.80103 1.000 102.29445 ?  260 THR A O   1 
ATOM 1990 C CB  . THR A 1 260 ? 11.86395  -16.91557 -25.77839 1.000 92.52276  ?  260 THR A CB  1 
ATOM 1991 O OG1 . THR A 1 260 ? 11.61335  -16.32275 -27.05728 1.000 106.51649 ?  260 THR A OG1 1 
ATOM 1992 C CG2 . THR A 1 260 ? 11.60695  -18.41840 -25.85591 1.000 80.58277  ?  260 THR A CG2 1 
ATOM 1993 N N   . TYR A 1 261 ? 12.38734  -15.90857 -22.74684 1.000 92.25562  ?  261 TYR A N   1 
ATOM 1994 C CA  . TYR A 1 261 ? 12.89544  -16.28928 -21.43357 1.000 88.91147  ?  261 TYR A CA  1 
ATOM 1995 C C   . TYR A 1 261 ? 11.79920  -16.28599 -20.37465 1.000 86.36260  ?  261 TYR A C   1 
ATOM 1996 O O   . TYR A 1 261 ? 11.82480  -17.11361 -19.45685 1.000 84.10438  ?  261 TYR A O   1 
ATOM 1997 C CB  . TYR A 1 261 ? 14.04609  -15.37550 -21.01591 1.000 79.43450  ?  261 TYR A CB  1 
ATOM 1998 C CG  . TYR A 1 261 ? 14.81838  -15.94500 -19.85968 1.000 75.87469  ?  261 TYR A CG  1 
ATOM 1999 C CD1 . TYR A 1 261 ? 15.69277  -17.00565 -20.05084 1.000 89.51513  ?  261 TYR A CD1 1 
ATOM 2000 C CD2 . TYR A 1 261 ? 14.66270  -15.44395 -18.57733 1.000 73.18260  ?  261 TYR A CD2 1 
ATOM 2001 C CE1 . TYR A 1 261 ? 16.39818  -17.54984 -19.00214 1.000 83.16516  ?  261 TYR A CE1 1 
ATOM 2002 C CE2 . TYR A 1 261 ? 15.36394  -15.98107 -17.51786 1.000 88.26096  ?  261 TYR A CE2 1 
ATOM 2003 C CZ  . TYR A 1 261 ? 16.23368  -17.03505 -17.73822 1.000 91.44140  ?  261 TYR A CZ  1 
ATOM 2004 O OH  . TYR A 1 261 ? 16.94475  -17.58066 -16.69326 1.000 95.29407  ?  261 TYR A OH  1 
ATOM 2005 N N   . PHE A 1 262 ? 10.82409  -15.39176 -20.48795 1.000 85.77744  ?  262 PHE A N   1 
ATOM 2006 C CA  . PHE A 1 262 ? 9.82125   -15.25655 -19.43785 1.000 88.88381  ?  262 PHE A CA  1 
ATOM 2007 C C   . PHE A 1 262 ? 8.49242   -15.95077 -19.78417 1.000 88.29997  ?  262 PHE A C   1 
ATOM 2008 O O   . PHE A 1 262 ? 7.53230   -15.33103 -20.24774 1.000 77.51638  ?  262 PHE A O   1 
ATOM 2009 C CB  . PHE A 1 262 ? 9.62031   -13.76931 -19.13377 1.000 84.44819  ?  262 PHE A CB  1 
ATOM 2010 C CG  . PHE A 1 262 ? 10.85739  -13.10701 -18.57616 1.000 73.86075  ?  262 PHE A CG  1 
ATOM 2011 C CD1 . PHE A 1 262 ? 11.17099  -13.20632 -17.23293 1.000 81.54233  ?  262 PHE A CD1 1 
ATOM 2012 C CD2 . PHE A 1 262 ? 11.72021  -12.40470 -19.40556 1.000 88.97578  ?  262 PHE A CD2 1 
ATOM 2013 C CE1 . PHE A 1 262 ? 12.31583  -12.61121 -16.72374 1.000 87.04337  ?  262 PHE A CE1 1 
ATOM 2014 C CE2 . PHE A 1 262 ? 12.86622  -11.80262 -18.90120 1.000 84.01472  ?  262 PHE A CE2 1 
ATOM 2015 C CZ  . PHE A 1 262 ? 13.16315  -11.90767 -17.55713 1.000 73.31587  ?  262 PHE A CZ  1 
ATOM 2016 N N   . LYS B 1 9   ? -19.69927 -20.91161 42.59309  1.000 104.15871 ?  9   LYS B N   1 
ATOM 2017 C CA  . LYS B 1 9   ? -19.64339 -21.73205 41.39066  1.000 100.35721 ?  9   LYS B CA  1 
ATOM 2018 C C   . LYS B 1 9   ? -18.60583 -21.19252 40.42096  1.000 96.18058  ?  9   LYS B C   1 
ATOM 2019 O O   . LYS B 1 9   ? -17.78753 -20.35167 40.77619  1.000 94.63288  ?  9   LYS B O   1 
ATOM 2020 C CB  . LYS B 1 9   ? -21.00667 -21.78769 40.70822  1.000 94.38704  ?  9   LYS B CB  1 
ATOM 2021 C CG  . LYS B 1 9   ? -22.07953 -22.47548 41.51223  1.000 89.55784  ?  9   LYS B CG  1 
ATOM 2022 C CD  . LYS B 1 9   ? -23.38179 -22.45949 40.74151  1.000 102.10652 ?  9   LYS B CD  1 
ATOM 2023 C CE  . LYS B 1 9   ? -24.48806 -23.15952 41.50234  1.000 111.72764 ?  9   LYS B CE  1 
ATOM 2024 N NZ  . LYS B 1 9   ? -25.75927 -23.12598 40.73132  1.000 95.98788  ?  9   LYS B NZ  1 
ATOM 2025 N N   . GLU B 1 10  ? -18.64585 -21.68952 39.19063  1.000 122.53691 ?  10  GLU B N   1 
ATOM 2026 C CA  . GLU B 1 10  ? -17.80521 -21.18998 38.11287  1.000 122.18039 ?  10  GLU B CA  1 
ATOM 2027 C C   . GLU B 1 10  ? -18.47846 -20.08436 37.31640  1.000 120.99232 ?  10  GLU B C   1 
ATOM 2028 O O   . GLU B 1 10  ? -18.02189 -19.75571 36.21565  1.000 119.64490 ?  10  GLU B O   1 
ATOM 2029 C CB  . GLU B 1 10  ? -17.41041 -22.33182 37.17861  1.000 124.66083 ?  10  GLU B CB  1 
ATOM 2030 C CG  . GLU B 1 10  ? -18.54898 -23.25763 36.81149  1.000 132.20757 ?  10  GLU B CG  1 
ATOM 2031 C CD  . GLU B 1 10  ? -18.68941 -24.39259 37.80432  1.000 143.26148 ?  10  GLU B CD  1 
ATOM 2032 O OE1 . GLU B 1 10  ? -19.06730 -24.12159 38.96549  1.000 149.76525 ?  10  GLU B OE1 1 
ATOM 2033 O OE2 . GLU B 1 10  ? -18.38463 -25.54463 37.43878  1.000 147.52981 -1 10  GLU B OE2 1 
ATOM 2034 N N   . THR B 1 11  ? -19.55792 -19.51707 37.84001  1.000 92.57083  ?  11  THR B N   1 
ATOM 2035 C CA  . THR B 1 11  ? -20.32167 -18.49348 37.14949  1.000 93.02389  ?  11  THR B CA  1 
ATOM 2036 C C   . THR B 1 11  ? -20.32348 -17.24189 38.01396  1.000 90.80871  ?  11  THR B C   1 
ATOM 2037 O O   . THR B 1 11  ? -20.54714 -17.32059 39.22532  1.000 84.89910  ?  11  THR B O   1 
ATOM 2038 C CB  . THR B 1 11  ? -21.75392 -18.96661 36.85981  1.000 93.78295  ?  11  THR B CB  1 
ATOM 2039 O OG1 . THR B 1 11  ? -22.28919 -19.63261 38.00875  1.000 110.57525 ?  11  THR B OG1 1 
ATOM 2040 C CG2 . THR B 1 11  ? -21.76713 -19.93489 35.69028  1.000 100.30736 ?  11  THR B CG2 1 
ATOM 2041 N N   . ILE B 1 12  ? -20.07581 -16.09153 37.38558  1.000 91.99750  ?  12  ILE B N   1 
ATOM 2042 C CA  . ILE B 1 12  ? -20.04673 -14.80336 38.06972  1.000 73.90430  ?  12  ILE B CA  1 
ATOM 2043 C C   . ILE B 1 12  ? -20.81001 -13.79093 37.22662  1.000 86.41213  ?  12  ILE B C   1 
ATOM 2044 O O   . ILE B 1 12  ? -20.97711 -13.95822 36.01831  1.000 96.78112  ?  12  ILE B O   1 
ATOM 2045 C CB  . ILE B 1 12  ? -18.60175 -14.31403 38.31503  1.000 83.03034  ?  12  ILE B CB  1 
ATOM 2046 C CG1 . ILE B 1 12  ? -18.55172 -13.25887 39.41595  1.000 68.74204  ?  12  ILE B CG1 1 
ATOM 2047 C CG2 . ILE B 1 12  ? -17.99944 -13.76193 37.03656  1.000 78.93826  ?  12  ILE B CG2 1 
ATOM 2048 C CD1 . ILE B 1 12  ? -17.18671 -13.13464 40.04682  1.000 91.32962  ?  12  ILE B CD1 1 
ATOM 2049 N N   . LYS B 1 13  ? -21.30915 -12.74320 37.87943  1.000 79.98959  ?  13  LYS B N   1 
ATOM 2050 C CA  . LYS B 1 13  ? -21.96394 -11.64094 37.17538  1.000 78.99785  ?  13  LYS B CA  1 
ATOM 2051 C C   . LYS B 1 13  ? -21.44051 -10.34739 37.78529  1.000 80.38302  ?  13  LYS B C   1 
ATOM 2052 O O   . LYS B 1 13  ? -21.83412 -9.97264  38.89289  1.000 91.81640  ?  13  LYS B O   1 
ATOM 2053 C CB  . LYS B 1 13  ? -23.48767 -11.71890 37.25304  1.000 90.59495  ?  13  LYS B CB  1 
ATOM 2054 C CG  . LYS B 1 13  ? -24.17965 -10.85960 36.18997  1.000 94.90229  ?  13  LYS B CG  1 
ATOM 2055 C CD  . LYS B 1 13  ? -25.61184 -10.51199 36.54748  1.000 100.22535 ?  13  LYS B CD  1 
ATOM 2056 C CE  . LYS B 1 13  ? -25.67873 -9.25192  37.40068  1.000 113.77023 ?  13  LYS B CE  1 
ATOM 2057 N NZ  . LYS B 1 13  ? -25.83777 -8.00696  36.58155  1.000 91.91108  ?  13  LYS B NZ  1 
ATOM 2058 N N   . ILE B 1 14  ? -20.53875 -9.68575  37.07397  1.000 76.50248  ?  14  ILE B N   1 
ATOM 2059 C CA  . ILE B 1 14  ? -19.92762 -8.44618  37.54059  1.000 71.80819  ?  14  ILE B CA  1 
ATOM 2060 C C   . ILE B 1 14  ? -20.65549 -7.27931  36.89335  1.000 65.65427  ?  14  ILE B C   1 
ATOM 2061 O O   . ILE B 1 14  ? -20.97542 -7.31609  35.69787  1.000 77.26090  ?  14  ILE B O   1 
ATOM 2062 C CB  . ILE B 1 14  ? -18.42545 -8.39416  37.20353  1.000 77.24575  ?  14  ILE B CB  1 
ATOM 2063 C CG1 . ILE B 1 14  ? -17.71757 -9.70229  37.58291  1.000 76.71068  ?  14  ILE B CG1 1 
ATOM 2064 C CG2 . ILE B 1 14  ? -17.77866 -7.21789  37.92126  1.000 79.97081  ?  14  ILE B CG2 1 
ATOM 2065 C CD1 . ILE B 1 14  ? -17.20443 -9.76281  38.98422  1.000 80.89390  ?  14  ILE B CD1 1 
ATOM 2066 N N   . ASN B 1 15  ? -20.89921 -6.23236  37.66752  1.000 69.52150  ?  15  ASN B N   1 
ATOM 2067 C CA  . ASN B 1 15  ? -21.59889 -5.05520  37.18038  1.000 72.54098  ?  15  ASN B CA  1 
ATOM 2068 C C   . ASN B 1 15  ? -20.61002 -3.91057  36.99811  1.000 64.36785  ?  15  ASN B C   1 
ATOM 2069 O O   . ASN B 1 15  ? -19.44697 -4.00554  37.38167  1.000 65.82141  ?  15  ASN B O   1 
ATOM 2070 C CB  . ASN B 1 15  ? -22.73916 -4.65954  38.13278  1.000 89.21160  ?  15  ASN B CB  1 
ATOM 2071 C CG  . ASN B 1 15  ? -23.80394 -5.75805  38.27729  1.000 94.78011  ?  15  ASN B CG  1 
ATOM 2072 O OD1 . ASN B 1 15  ? -24.67770 -5.91891  37.41970  1.000 91.70575  ?  15  ASN B OD1 1 
ATOM 2073 N ND2 . ASN B 1 15  ? -23.73652 -6.50469  39.37259  1.000 95.36395  ?  15  ASN B ND2 1 
ATOM 2074 N N   . ASN B 1 16  ? -21.07944 -2.85853  36.33209  1.000 64.15389  ?  16  ASN B N   1 
ATOM 2075 C CA  . ASN B 1 16  ? -20.35391 -1.59458  36.14379  1.000 63.62058  ?  16  ASN B CA  1 
ATOM 2076 C C   . ASN B 1 16  ? -18.89155 -1.80091  35.78519  1.000 63.04249  ?  16  ASN B C   1 
ATOM 2077 O O   . ASN B 1 16  ? -17.99689 -1.14109  36.31537  1.000 72.57561  ?  16  ASN B O   1 
ATOM 2078 C CB  . ASN B 1 16  ? -20.45847 -0.68918  37.36409  1.000 69.08107  ?  16  ASN B CB  1 
ATOM 2079 C CG  . ASN B 1 16  ? -21.86970 -0.28826  37.66716  1.000 79.76089  ?  16  ASN B CG  1 
ATOM 2080 O OD1 . ASN B 1 16  ? -22.62510 0.07947   36.76277  1.000 72.24125  ?  16  ASN B OD1 1 
ATOM 2081 N ND2 . ASN B 1 16  ? -22.23043 -0.30795  38.94921  1.000 70.71038  ?  16  ASN B ND2 1 
ATOM 2082 N N   . ILE B 1 17  ? -18.64636 -2.69289  34.83761  1.000 66.03213  ?  17  ILE B N   1 
ATOM 2083 C CA  . ILE B 1 17  ? -17.30046 -2.84099  34.30512  1.000 62.47729  ?  17  ILE B CA  1 
ATOM 2084 C C   . ILE B 1 17  ? -17.11192 -1.77326  33.24171  1.000 62.16248  ?  17  ILE B C   1 
ATOM 2085 O O   . ILE B 1 17  ? -17.85976 -1.72486  32.26098  1.000 77.46226  ?  17  ILE B O   1 
ATOM 2086 C CB  . ILE B 1 17  ? -17.07499 -4.24346  33.73356  1.000 62.67457  ?  17  ILE B CB  1 
ATOM 2087 C CG1 . ILE B 1 17  ? -17.43892 -5.29945  34.77554  1.000 63.18614  ?  17  ILE B CG1 1 
ATOM 2088 C CG2 . ILE B 1 17  ? -15.63434 -4.39708  33.31034  1.000 62.32637  ?  17  ILE B CG2 1 
ATOM 2089 C CD1 . ILE B 1 17  ? -17.15723 -6.69523  34.32037  1.000 63.53356  ?  17  ILE B CD1 1 
ATOM 2090 N N   . MET B 1 18  ? -16.14400 -0.89138  33.45521  1.000 65.76251  ?  18  MET B N   1 
ATOM 2091 C CA  . MET B 1 18  ? -15.85302 0.19161   32.52762  1.000 72.81745  ?  18  MET B CA  1 
ATOM 2092 C C   . MET B 1 18  ? -14.59668 -0.14432  31.73082  1.000 72.37873  ?  18  MET B C   1 
ATOM 2093 O O   . MET B 1 18  ? -13.54687 -0.44713  32.30818  1.000 61.26690  ?  18  MET B O   1 
ATOM 2094 C CB  . MET B 1 18  ? -15.68073 1.50946   33.28340  1.000 81.80474  ?  18  MET B CB  1 
ATOM 2095 C CG  . MET B 1 18  ? -15.12083 2.66878   32.46684  1.000 87.90902  ?  18  MET B CG  1 
ATOM 2096 S SD  . MET B 1 18  ? -16.44685 3.57767   31.64423  1.000 112.61565 ?  18  MET B SD  1 
ATOM 2097 C CE  . MET B 1 18  ? -15.59079 5.06285   31.13018  1.000 89.06041  ?  18  MET B CE  1 
ATOM 2098 N N   . ILE B 1 19  ? -14.70291 -0.07478  30.40884  1.000 85.42248  ?  19  ILE B N   1 
ATOM 2099 C CA  . ILE B 1 19  ? -13.57112 -0.31838  29.52236  1.000 77.08064  ?  19  ILE B CA  1 
ATOM 2100 C C   . ILE B 1 19  ? -12.83197 1.00704   29.36339  1.000 78.22897  ?  19  ILE B C   1 
ATOM 2101 O O   . ILE B 1 19  ? -13.36840 1.96584   28.80257  1.000 86.52738  ?  19  ILE B O   1 
ATOM 2102 C CB  . ILE B 1 19  ? -14.02315 -0.89571  28.17257  1.000 75.44308  ?  19  ILE B CB  1 
ATOM 2103 C CG1 . ILE B 1 19  ? -14.36054 -2.38529  28.30444  1.000 74.62011  ?  19  ILE B CG1 1 
ATOM 2104 C CG2 . ILE B 1 19  ? -12.95760 -0.72272  27.10462  1.000 74.37404  ?  19  ILE B CG2 1 
ATOM 2105 C CD1 . ILE B 1 19  ? -15.72956 -2.68838  28.89430  1.000 73.67918  ?  19  ILE B CD1 1 
ATOM 2106 N N   . ALA B 1 20  ? -11.60380 1.06924   29.88551  1.000 73.23552  ?  20  ALA B N   1 
ATOM 2107 C CA  . ALA B 1 20  ? -10.81148 2.29113   29.86773  1.000 67.39797  ?  20  ALA B CA  1 
ATOM 2108 C C   . ALA B 1 20  ? -9.77419  2.30506   28.75680  1.000 75.14631  ?  20  ALA B C   1 
ATOM 2109 O O   . ALA B 1 20  ? -9.26061  3.37781   28.41329  1.000 62.07203  ?  20  ALA B O   1 
ATOM 2110 C CB  . ALA B 1 20  ? -10.10266 2.47864   31.21189  1.000 61.05338  ?  20  ALA B CB  1 
ATOM 2111 N N   . LYS B 1 21  ? -9.47427  1.14477   28.18687  1.000 65.07124  ?  21  LYS B N   1 
ATOM 2112 C CA  . LYS B 1 21  ? -8.55871  1.00816   27.07168  1.000 71.56416  ?  21  LYS B CA  1 
ATOM 2113 C C   . LYS B 1 21  ? -9.19836  0.10103   26.03420  1.000 80.12843  ?  21  LYS B C   1 
ATOM 2114 O O   . LYS B 1 21  ? -9.85099  -0.88350  26.39587  1.000 71.76941  ?  21  LYS B O   1 
ATOM 2115 C CB  . LYS B 1 21  ? -7.20698  0.43538   27.52011  1.000 69.16129  ?  21  LYS B CB  1 
ATOM 2116 C CG  . LYS B 1 21  ? -6.51864  1.23024   28.60869  1.000 73.11309  ?  21  LYS B CG  1 
ATOM 2117 C CD  . LYS B 1 21  ? -5.11740  0.70379   28.84578  1.000 86.63033  ?  21  LYS B CD  1 
ATOM 2118 C CE  . LYS B 1 21  ? -4.42089  1.44828   29.97059  1.000 103.02617 ?  21  LYS B CE  1 
ATOM 2119 N NZ  . LYS B 1 21  ? -3.17358  0.75329   30.40448  1.000 140.92964 ?  21  LYS B NZ  1 
ATOM 2120 N N   . TYR B 1 22  ? -9.03011  0.43786   24.74929  1.000 74.13222  ?  22  TYR B N   1 
ATOM 2121 C CA  . TYR B 1 22  ? -9.56002  -0.42527  23.70220  1.000 67.96823  ?  22  TYR B CA  1 
ATOM 2122 C C   . TYR B 1 22  ? -9.11252  -1.85809  23.96254  1.000 75.41764  ?  22  TYR B C   1 
ATOM 2123 O O   . TYR B 1 22  ? -7.91858  -2.11847  24.14514  1.000 74.24183  ?  22  TYR B O   1 
ATOM 2124 C CB  . TYR B 1 22  ? -9.10501  0.03325   22.31289  1.000 67.05182  ?  22  TYR B CB  1 
ATOM 2125 C CG  . TYR B 1 22  ? -9.95589  -0.61031  21.23609  1.000 85.43338  ?  22  TYR B CG  1 
ATOM 2126 C CD1 . TYR B 1 22  ? -9.69501  -1.90081  20.78821  1.000 83.42647  ?  22  TYR B CD1 1 
ATOM 2127 C CD2 . TYR B 1 22  ? -11.06017 0.04819   20.71490  1.000 79.15868  ?  22  TYR B CD2 1 
ATOM 2128 C CE1 . TYR B 1 22  ? -10.49538 -2.50451  19.83578  1.000 67.24202  ?  22  TYR B CE1 1 
ATOM 2129 C CE2 . TYR B 1 22  ? -11.86170 -0.54545  19.75881  1.000 90.29720  ?  22  TYR B CE2 1 
ATOM 2130 C CZ  . TYR B 1 22  ? -11.57659 -1.82221  19.32340  1.000 85.24935  ?  22  TYR B CZ  1 
ATOM 2131 O OH  . TYR B 1 22  ? -12.38040 -2.41490  18.37427  1.000 82.33765  ?  22  TYR B OH  1 
ATOM 2132 N N   . THR B 1 23  ? -10.07394 -2.78081  24.04887  1.000 74.93321  ?  23  THR B N   1 
ATOM 2133 C CA  . THR B 1 23  ? -9.80323  -4.12692  24.53946  1.000 80.25021  ?  23  THR B CA  1 
ATOM 2134 C C   . THR B 1 23  ? -10.14912 -5.17047  23.49104  1.000 70.30202  ?  23  THR B C   1 
ATOM 2135 O O   . THR B 1 23  ? -11.27422 -5.20444  22.98171  1.000 83.21342  ?  23  THR B O   1 
ATOM 2136 C CB  . THR B 1 23  ? -10.57760 -4.41098  25.83145  1.000 85.97300  ?  23  THR B CB  1 
ATOM 2137 O OG1 . THR B 1 23  ? -10.14277 -3.50580  26.85604  1.000 73.45888  ?  23  THR B OG1 1 
ATOM 2138 C CG2 . THR B 1 23  ? -10.39604 -5.87099  26.28145  1.000 67.08577  ?  23  THR B CG2 1 
ATOM 2139 N N   . VAL B 1 24  ? -9.18663  -6.03797  23.20639  1.000 64.93314  ?  24  VAL B N   1 
ATOM 2140 C CA  . VAL B 1 24  ? -9.36937  -7.21080  22.36565  1.000 76.54965  ?  24  VAL B CA  1 
ATOM 2141 C C   . VAL B 1 24  ? -9.22477  -8.41282  23.28025  1.000 70.79196  ?  24  VAL B C   1 
ATOM 2142 O O   . VAL B 1 24  ? -8.14703  -8.67176  23.82207  1.000 76.86947  ?  24  VAL B O   1 
ATOM 2143 C CB  . VAL B 1 24  ? -8.36157  -7.25533  21.21115  1.000 66.76221  ?  24  VAL B CB  1 
ATOM 2144 C CG1 . VAL B 1 24  ? -8.73537  -8.35210  20.22573  1.000 68.01034  ?  24  VAL B CG1 1 
ATOM 2145 C CG2 . VAL B 1 24  ? -8.30206  -5.90108  20.52748  1.000 66.72156  ?  24  VAL B CG2 1 
ATOM 2146 N N   . LEU B 1 25  ? -10.31670 -9.12848  23.47119  1.000 73.66651  ?  25  LEU B N   1 
ATOM 2147 C CA  . LEU B 1 25  ? -10.41062 -10.21280 24.42996  1.000 73.94618  ?  25  LEU B CA  1 
ATOM 2148 C C   . LEU B 1 25  ? -10.58718 -11.54431 23.70757  1.000 87.21209  ?  25  LEU B C   1 
ATOM 2149 O O   . LEU B 1 25  ? -11.28201 -11.62259 22.69604  1.000 98.30706  ?  25  LEU B O   1 
ATOM 2150 C CB  . LEU B 1 25  ? -11.58435 -9.94207  25.36913  1.000 76.58805  ?  25  LEU B CB  1 
ATOM 2151 C CG  . LEU B 1 25  ? -11.69710 -10.66686 26.69387  1.000 83.90172  ?  25  LEU B CG  1 
ATOM 2152 C CD1 . LEU B 1 25  ? -12.19107 -9.68562  27.73805  1.000 74.22816  ?  25  LEU B CD1 1 
ATOM 2153 C CD2 . LEU B 1 25  ? -12.64993 -11.82785 26.52144  1.000 87.70497  ?  25  LEU B CD2 1 
ATOM 2154 N N   . TYR B 1 26  ? -9.93301  -12.58249 24.20285  1.000 94.25078  ?  26  TYR B N   1 
ATOM 2155 C CA  . TYR B 1 26  ? -10.10171 -13.94528 23.71570  1.000 86.67436  ?  26  TYR B CA  1 
ATOM 2156 C C   . TYR B 1 26  ? -10.85726 -14.71455 24.78543  1.000 84.71649  ?  26  TYR B C   1 
ATOM 2157 O O   . TYR B 1 26  ? -10.27923 -15.06401 25.82116  1.000 85.03336  ?  26  TYR B O   1 
ATOM 2158 C CB  . TYR B 1 26  ? -8.75167  -14.59044 23.41887  1.000 86.73559  ?  26  TYR B CB  1 
ATOM 2159 C CG  . TYR B 1 26  ? -8.84415  -15.99334 22.86715  1.000 94.55401  ?  26  TYR B CG  1 
ATOM 2160 C CD1 . TYR B 1 26  ? -9.36963  -16.24423 21.60989  1.000 90.83886  ?  26  TYR B CD1 1 
ATOM 2161 C CD2 . TYR B 1 26  ? -8.41073  -17.07395 23.62276  1.000 101.90139 ?  26  TYR B CD2 1 
ATOM 2162 C CE1 . TYR B 1 26  ? -9.45493  -17.53587 21.12149  1.000 108.55564 ?  26  TYR B CE1 1 
ATOM 2163 C CE2 . TYR B 1 26  ? -8.48953  -18.36533 23.14315  1.000 104.14127 ?  26  TYR B CE2 1 
ATOM 2164 C CZ  . TYR B 1 26  ? -9.01267  -18.59451 21.89304  1.000 114.56327 ?  26  TYR B CZ  1 
ATOM 2165 O OH  . TYR B 1 26  ? -9.09034  -19.88811 21.41760  1.000 120.29842 ?  26  TYR B OH  1 
ATOM 2166 N N   . THR B 1 27  ? -12.14882 -14.96609 24.52334  1.000 103.97721 ?  27  THR B N   1 
ATOM 2167 C CA  . THR B 1 27  ? -13.02279 -15.63102 25.48864  1.000 102.07753 ?  27  THR B CA  1 
ATOM 2168 C C   . THR B 1 27  ? -12.36978 -16.87231 26.06837  1.000 106.49620 ?  27  THR B C   1 
ATOM 2169 O O   . THR B 1 27  ? -12.52332 -17.15613 27.26085  1.000 128.70947 ?  27  THR B O   1 
ATOM 2170 C CB  . THR B 1 27  ? -14.36471 -15.99205 24.85878  1.000 102.18217 ?  27  THR B CB  1 
ATOM 2171 O OG1 . THR B 1 27  ? -14.16421 -16.98959 23.85544  1.000 113.99905 ?  27  THR B OG1 1 
ATOM 2172 C CG2 . THR B 1 27  ? -14.99359 -14.76811 24.23237  1.000 100.57676 ?  27  THR B CG2 1 
ATOM 2173 N N   . SER B 1 28  ? -11.66678 -17.64191 25.23672  1.000 88.23388  ?  28  SER B N   1 
ATOM 2174 C CA  . SER B 1 28  ? -10.93766 -18.80266 25.73386  1.000 107.41810 ?  28  SER B CA  1 
ATOM 2175 C C   . SER B 1 28  ? -11.84953 -19.77773 26.46219  1.000 114.25730 ?  28  SER B C   1 
ATOM 2176 O O   . SER B 1 28  ? -12.67115 -20.45991 25.84080  1.000 123.37698 ?  28  SER B O   1 
ATOM 2177 C CB  . SER B 1 28  ? -9.81093  -18.35977 26.66873  1.000 92.01809  ?  28  SER B CB  1 
ATOM 2178 O OG  . SER B 1 28  ? -9.16818  -19.48396 27.23250  1.000 112.04402 ?  28  SER B OG  1 
ATOM 2179 N N   . ASN B 1 29  ? -11.68369 -19.86489 27.77670  1.000 110.84627 ?  29  ASN B N   1 
ATOM 2180 C CA  . ASN B 1 29  ? -12.44799 -20.78660 28.61701  1.000 118.33237 ?  29  ASN B CA  1 
ATOM 2181 C C   . ASN B 1 29  ? -13.60596 -20.09793 29.34179  1.000 116.55445 ?  29  ASN B C   1 
ATOM 2182 O O   . ASN B 1 29  ? -13.76855 -20.27580 30.54896  1.000 115.87600 ?  29  ASN B O   1 
ATOM 2183 C CB  . ASN B 1 29  ? -11.51486 -21.47711 29.60180  1.000 114.53382 ?  29  ASN B CB  1 
ATOM 2184 C CG  . ASN B 1 29  ? -10.96562 -22.78109 29.05309  1.000 133.09178 ?  29  ASN B CG  1 
ATOM 2185 O OD1 . ASN B 1 29  ? -11.69357 -23.56801 28.44305  1.000 136.71158 ?  29  ASN B OD1 1 
ATOM 2186 N ND2 . ASN B 1 29  ? -9.67240  -23.00842 29.24933  1.000 141.21237 ?  29  ASN B ND2 1 
ATOM 2187 N N   . CYS B 1 30  ? -14.42277 -19.30250 28.64484  1.000 103.72570 ?  30  CYS B N   1 
ATOM 2188 C CA  . CYS B 1 30  ? -15.57403 -18.68026 29.29386  1.000 102.03558 ?  30  CYS B CA  1 
ATOM 2189 C C   . CYS B 1 30  ? -16.62053 -18.29871 28.25391  1.000 98.14598  ?  30  CYS B C   1 
ATOM 2190 O O   . CYS B 1 30  ? -16.29700 -18.01734 27.09822  1.000 97.12886  ?  30  CYS B O   1 
ATOM 2191 C CB  . CYS B 1 30  ? -15.19507 -17.43683 30.10459  1.000 92.78757  ?  30  CYS B CB  1 
ATOM 2192 S SG  . CYS B 1 30  ? -14.98481 -15.96021 29.11206  1.000 91.33127  ?  30  CYS B SG  1 
ATOM 2193 N N   . ILE B 1 31  ? -17.88363 -18.36213 28.67753  1.000 103.27630 ?  31  ILE B N   1 
ATOM 2194 C CA  . ILE B 1 31  ? -19.03077 -17.84689 27.93077  1.000 83.22122  ?  31  ILE B CA  1 
ATOM 2195 C C   . ILE B 1 31  ? -19.45434 -16.53227 28.57333  1.000 88.47936  ?  31  ILE B C   1 
ATOM 2196 O O   . ILE B 1 31  ? -19.74471 -16.49547 29.77514  1.000 93.44790  ?  31  ILE B O   1 
ATOM 2197 C CB  . ILE B 1 31  ? -20.19821 -18.84622 27.94240  1.000 84.52870  ?  31  ILE B CB  1 
ATOM 2198 C CG1 . ILE B 1 31  ? -19.72619 -20.24330 27.54650  1.000 80.86565  ?  31  ILE B CG1 1 
ATOM 2199 C CG2 . ILE B 1 31  ? -21.30132 -18.37717 27.03176  1.000 89.08549  ?  31  ILE B CG2 1 
ATOM 2200 C CD1 . ILE B 1 31  ? -19.00228 -20.28497 26.22960  1.000 97.50386  ?  31  ILE B CD1 1 
ATOM 2201 N N   . MET B 1 32  ? -19.52260 -15.45433 27.79201  1.000 93.33389  ?  32  MET B N   1 
ATOM 2202 C CA  . MET B 1 32  ? -19.78810 -14.13130 28.35431  1.000 90.81357  ?  32  MET B CA  1 
ATOM 2203 C C   . MET B 1 32  ? -21.07241 -13.55417 27.78175  1.000 108.14082 ?  32  MET B C   1 
ATOM 2204 O O   . MET B 1 32  ? -21.16691 -13.32423 26.57560  1.000 113.26776 ?  32  MET B O   1 
ATOM 2205 C CB  . MET B 1 32  ? -18.63879 -13.16414 28.08763  1.000 69.43842  ?  32  MET B CB  1 
ATOM 2206 C CG  . MET B 1 32  ? -17.46006 -13.33634 28.99686  1.000 95.27880  ?  32  MET B CG  1 
ATOM 2207 S SD  . MET B 1 32  ? -16.09889 -12.30082 28.44798  1.000 95.45596  ?  32  MET B SD  1 
ATOM 2208 C CE  . MET B 1 32  ? -17.01665 -10.97502 27.67301  1.000 77.48242  ?  32  MET B CE  1 
ATOM 2209 N N   . ASP B 1 33  ? -22.04101 -13.28176 28.64746  1.000 111.75210 ?  33  ASP B N   1 
ATOM 2210 C CA  . ASP B 1 33  ? -23.22504 -12.51064 28.28208  1.000 115.58351 ?  33  ASP B CA  1 
ATOM 2211 C C   . ASP B 1 33  ? -22.99831 -11.06390 28.70582  1.000 111.78969 ?  33  ASP B C   1 
ATOM 2212 O O   . ASP B 1 33  ? -22.94857 -10.76506 29.90119  1.000 113.93837 ?  33  ASP B O   1 
ATOM 2213 C CB  . ASP B 1 33  ? -24.47887 -13.08989 28.93300  1.000 117.08552 ?  33  ASP B CB  1 
ATOM 2214 C CG  . ASP B 1 33  ? -24.80521 -14.48046 28.43019  1.000 114.29227 ?  33  ASP B CG  1 
ATOM 2215 O OD1 . ASP B 1 33  ? -24.00147 -15.03224 27.64851  1.000 110.12555 ?  33  ASP B OD1 1 
ATOM 2216 O OD2 . ASP B 1 33  ? -25.86153 -15.02279 28.82176  1.000 115.98572 -1 33  ASP B OD2 1 
ATOM 2217 N N   . ILE B 1 34  ? -22.82715 -10.17802 27.72928  1.000 90.96465  ?  34  ILE B N   1 
ATOM 2218 C CA  . ILE B 1 34  ? -22.56194 -8.76610  27.96164  1.000 86.93446  ?  34  ILE B CA  1 
ATOM 2219 C C   . ILE B 1 34  ? -23.87617 -8.00519  27.84760  1.000 88.91299  ?  34  ILE B C   1 
ATOM 2220 O O   . ILE B 1 34  ? -24.54839 -8.06741  26.81431  1.000 96.41723  ?  34  ILE B O   1 
ATOM 2221 C CB  . ILE B 1 34  ? -21.52833 -8.23733  26.95871  1.000 76.77035  ?  34  ILE B CB  1 
ATOM 2222 C CG1 . ILE B 1 34  ? -20.31258 -9.16682  26.93597  1.000 70.51214  ?  34  ILE B CG1 1 
ATOM 2223 C CG2 . ILE B 1 34  ? -21.13015 -6.81029  27.30126  1.000 78.78074  ?  34  ILE B CG2 1 
ATOM 2224 C CD1 . ILE B 1 34  ? -19.13146 -8.59042  26.21285  1.000 83.03138  ?  34  ILE B CD1 1 
ATOM 2225 N N   . TYR B 1 35  ? -24.23941 -7.27921  28.89914  1.000 91.08394  ?  35  TYR B N   1 
ATOM 2226 C CA  . TYR B 1 35  ? -25.43195 -6.44359  28.92695  1.000 80.63946  ?  35  TYR B CA  1 
ATOM 2227 C C   . TYR B 1 35  ? -24.99492 -4.99221  28.97841  1.000 76.64017  ?  35  TYR B C   1 
ATOM 2228 O O   . TYR B 1 35  ? -24.22419 -4.60601  29.86273  1.000 74.29490  ?  35  TYR B O   1 
ATOM 2229 C CB  . TYR B 1 35  ? -26.32488 -6.76260  30.12777  1.000 88.78616  ?  35  TYR B CB  1 
ATOM 2230 C CG  . TYR B 1 35  ? -26.53702 -8.23466  30.36921  1.000 94.99708  ?  35  TYR B CG  1 
ATOM 2231 C CD1 . TYR B 1 35  ? -27.38582 -8.97496  29.55894  1.000 97.15788  ?  35  TYR B CD1 1 
ATOM 2232 C CD2 . TYR B 1 35  ? -25.89236 -8.88624  31.41144  1.000 101.02251 ?  35  TYR B CD2 1 
ATOM 2233 C CE1 . TYR B 1 35  ? -27.58620 -10.32852 29.77569  1.000 103.79049 ?  35  TYR B CE1 1 
ATOM 2234 C CE2 . TYR B 1 35  ? -26.08340 -10.24296 31.63711  1.000 116.23577 ?  35  TYR B CE2 1 
ATOM 2235 C CZ  . TYR B 1 35  ? -26.93298 -10.95979 30.81507  1.000 117.40035 ?  35  TYR B CZ  1 
ATOM 2236 O OH  . TYR B 1 35  ? -27.13175 -12.30857 31.03185  1.000 113.96573 ?  35  TYR B OH  1 
ATOM 2237 N N   . SER B 1 36  ? -25.44905 -4.20736  28.01143  1.000 111.63644 ?  36  SER B N   1 
ATOM 2238 C CA  . SER B 1 36  ? -25.24508 -2.76996  28.04975  1.000 118.69083 ?  36  SER B CA  1 
ATOM 2239 C C   . SER B 1 36  ? -26.28367 -2.11916  27.15582  1.000 132.98434 ?  36  SER B C   1 
ATOM 2240 O O   . SER B 1 36  ? -26.72603 -2.71482  26.17071  1.000 143.30585 ?  36  SER B O   1 
ATOM 2241 C CB  . SER B 1 36  ? -23.83676 -2.38059  27.59413  1.000 120.23326 ?  36  SER B CB  1 
ATOM 2242 O OG  . SER B 1 36  ? -23.75690 -0.98616  27.35094  1.000 126.35827 ?  36  SER B OG  1 
ATOM 2243 N N   . GLU B 1 37  ? -26.64614 -0.88284  27.49956  1.000 141.13470 ?  37  GLU B N   1 
ATOM 2244 C CA  . GLU B 1 37  ? -27.60984 -0.09814  26.72673  1.000 144.28747 ?  37  GLU B CA  1 
ATOM 2245 C C   . GLU B 1 37  ? -28.86603 -0.90655  26.40060  1.000 147.42379 ?  37  GLU B C   1 
ATOM 2246 O O   . GLU B 1 37  ? -29.35096 -0.90424  25.26698  1.000 152.04197 ?  37  GLU B O   1 
ATOM 2247 C CB  . GLU B 1 37  ? -26.95383 0.43416   25.44972  1.000 152.99930 ?  37  GLU B CB  1 
ATOM 2248 C CG  . GLU B 1 37  ? -25.72757 1.31308   25.70987  1.000 160.94964 ?  37  GLU B CG  1 
ATOM 2249 C CD  . GLU B 1 37  ? -25.03515 1.78529   24.43529  1.000 150.30009 ?  37  GLU B CD  1 
ATOM 2250 O OE1 . GLU B 1 37  ? -25.38458 1.29887   23.33783  1.000 140.33676 ?  37  GLU B OE1 1 
ATOM 2251 O OE2 . GLU B 1 37  ? -24.12637 2.63849   24.53699  1.000 143.74213 -1 37  GLU B OE2 1 
ATOM 2252 N N   . GLU B 1 38  ? -29.37686 -1.63326  27.40225  1.000 148.37588 ?  38  GLU B N   1 
ATOM 2253 C CA  . GLU B 1 38  ? -30.59568 -2.43990  27.26400  1.000 145.03638 ?  38  GLU B CA  1 
ATOM 2254 C C   . GLU B 1 38  ? -30.45282 -3.49225  26.16296  1.000 142.26786 ?  38  GLU B C   1 
ATOM 2255 O O   . GLU B 1 38  ? -31.41289 -3.81371  25.45833  1.000 135.43402 ?  38  GLU B O   1 
ATOM 2256 C CB  . GLU B 1 38  ? -31.81709 -1.55346  26.99717  1.000 147.53811 ?  38  GLU B CB  1 
ATOM 2257 C CG  . GLU B 1 38  ? -32.21187 -0.62560  28.13664  1.000 142.90738 ?  38  GLU B CG  1 
ATOM 2258 C CD  . GLU B 1 38  ? -33.45911 0.17781   27.81099  1.000 131.07529 ?  38  GLU B CD  1 
ATOM 2259 O OE1 . GLU B 1 38  ? -33.95281 0.06448   26.66504  1.000 121.07316 ?  38  GLU B OE1 1 
ATOM 2260 O OE2 . GLU B 1 38  ? -33.93886 0.92195   28.69610  1.000 122.52481 -1 38  GLU B OE2 1 
ATOM 2261 N N   . GLU B 1 39  ? -29.24938 -4.04567  26.01913  1.000 138.71168 ?  39  GLU B N   1 
ATOM 2262 C CA  . GLU B 1 39  ? -28.97354 -5.03225  24.98567  1.000 116.00488 ?  39  GLU B CA  1 
ATOM 2263 C C   . GLU B 1 39  ? -28.16799 -6.17780  25.58122  1.000 93.51959  ?  39  GLU B C   1 
ATOM 2264 O O   . GLU B 1 39  ? -27.59390 -6.06017  26.66486  1.000 110.03105 ?  39  GLU B O   1 
ATOM 2265 C CB  . GLU B 1 39  ? -28.20848 -4.40385  23.81180  1.000 131.25675 ?  39  GLU B CB  1 
ATOM 2266 C CG  . GLU B 1 39  ? -28.97660 -3.31382  23.07891  1.000 129.31617 ?  39  GLU B CG  1 
ATOM 2267 C CD  . GLU B 1 39  ? -28.10545 -2.52555  22.11680  1.000 140.95868 ?  39  GLU B CD  1 
ATOM 2268 O OE1 . GLU B 1 39  ? -27.56701 -3.12230  21.15598  1.000 139.30696 ?  39  GLU B OE1 1 
ATOM 2269 O OE2 . GLU B 1 39  ? -27.94133 -1.30704  22.34051  1.000 135.24597 -1 39  GLU B OE2 1 
ATOM 2270 N N   . LYS B 1 40  ? -28.14438 -7.29990  24.86528  1.000 77.18932  ?  40  LYS B N   1 
ATOM 2271 C CA  . LYS B 1 40  ? -27.42336 -8.49412  25.29132  1.000 87.25451  ?  40  LYS B CA  1 
ATOM 2272 C C   . LYS B 1 40  ? -26.63423 -9.05650  24.11777  1.000 88.20538  ?  40  LYS B C   1 
ATOM 2273 O O   . LYS B 1 40  ? -27.21232 -9.36488  23.07212  1.000 99.29743  ?  40  LYS B O   1 
ATOM 2274 C CB  . LYS B 1 40  ? -28.38089 -9.55337  25.84864  1.000 72.81206  ?  40  LYS B CB  1 
ATOM 2275 C CG  . LYS B 1 40  ? -27.68635 -10.82453 26.31373  1.000 79.53556  ?  40  LYS B CG  1 
ATOM 2276 C CD  . LYS B 1 40  ? -28.67803 -11.93694 26.60890  1.000 89.77404  ?  40  LYS B CD  1 
ATOM 2277 C CE  . LYS B 1 40  ? -27.97294 -13.15971 27.17870  1.000 107.41635 ?  40  LYS B CE  1 
ATOM 2278 N NZ  . LYS B 1 40  ? -28.89761 -14.29779 27.45280  1.000 104.02822 ?  40  LYS B NZ  1 
ATOM 2279 N N   . ILE B 1 41  ? -25.32440 -9.20954  24.29916  1.000 96.89281  ?  41  ILE B N   1 
ATOM 2280 C CA  . ILE B 1 41  ? -24.43350 -9.81743  23.31293  1.000 99.26288  ?  41  ILE B CA  1 
ATOM 2281 C C   . ILE B 1 41  ? -23.73745 -10.99723 23.97954  1.000 96.05411  ?  41  ILE B C   1 
ATOM 2282 O O   . ILE B 1 41  ? -23.04919 -10.82493 24.99009  1.000 95.30531  ?  41  ILE B O   1 
ATOM 2283 C CB  . ILE B 1 41  ? -23.40331 -8.81340  22.76819  1.000 94.24444  ?  41  ILE B CB  1 
ATOM 2284 C CG1 . ILE B 1 41  ? -24.10871 -7.64260  22.07957  1.000 87.40539  ?  41  ILE B CG1 1 
ATOM 2285 C CG2 . ILE B 1 41  ? -22.42417 -9.50873  21.82914  1.000 87.79689  ?  41  ILE B CG2 1 
ATOM 2286 C CD1 . ILE B 1 41  ? -23.17511 -6.70559  21.35914  1.000 98.96081  ?  41  ILE B CD1 1 
ATOM 2287 N N   . THR B 1 42  ? -23.92490 -12.19214 23.43105  1.000 93.07528  ?  42  THR B N   1 
ATOM 2288 C CA  . THR B 1 42  ? -23.32000 -13.40136 23.97719  1.000 96.19711  ?  42  THR B CA  1 
ATOM 2289 C C   . THR B 1 42  ? -22.09305 -13.80235 23.16032  1.000 99.74838  ?  42  THR B C   1 
ATOM 2290 O O   . THR B 1 42  ? -22.20036 -14.09250 21.96519  1.000 106.77343 ?  42  THR B O   1 
ATOM 2291 C CB  . THR B 1 42  ? -24.33640 -14.54088 24.02871  1.000 89.75603  ?  42  THR B CB  1 
ATOM 2292 O OG1 . THR B 1 42  ? -25.37219 -14.20901 24.96514  1.000 90.77008  ?  42  THR B OG1 1 
ATOM 2293 C CG2 . THR B 1 42  ? -23.66164 -15.83744 24.44824  1.000 79.00042  ?  42  THR B CG2 1 
ATOM 2294 N N   . CYS B 1 43  ? -20.93032 -13.79264 23.80469  1.000 96.96854  ?  43  CYS B N   1 
ATOM 2295 C CA  . CYS B 1 43  ? -19.69818 -14.29583 23.22078  1.000 92.44705  ?  43  CYS B CA  1 
ATOM 2296 C C   . CYS B 1 43  ? -19.48933 -15.74172 23.65203  1.000 99.11672  ?  43  CYS B C   1 
ATOM 2297 O O   . CYS B 1 43  ? -19.50886 -16.05263 24.85268  1.000 105.27174 ?  43  CYS B O   1 
ATOM 2298 C CB  . CYS B 1 43  ? -18.50691 -13.43637 23.64136  1.000 86.74442  ?  43  CYS B CB  1 
ATOM 2299 S SG  . CYS B 1 43  ? -18.78534 -11.66518 23.46098  1.000 95.77923  ?  43  CYS B SG  1 
ATOM 2300 N N   . PHE B 1 44  ? -19.28259 -16.60935 22.66576  1.000 99.58287  ?  44  PHE B N   1 
ATOM 2301 C CA  . PHE B 1 44  ? -19.11212 -18.04297 22.82962  1.000 104.28319 ?  44  PHE B CA  1 
ATOM 2302 C C   . PHE B 1 44  ? -17.63237 -18.34408 23.06620  1.000 99.76420  ?  44  PHE B C   1 
ATOM 2303 O O   . PHE B 1 44  ? -16.77634 -17.46150 22.99023  1.000 94.56546  ?  44  PHE B O   1 
ATOM 2304 C CB  . PHE B 1 44  ? -19.64844 -18.75950 21.58023  1.000 116.91446 ?  44  PHE B CB  1 
ATOM 2305 C CG  . PHE B 1 44  ? -19.81440 -20.25866 21.72251  1.000 128.78660 ?  44  PHE B CG  1 
ATOM 2306 C CD1 . PHE B 1 44  ? -20.64662 -20.79824 22.69251  1.000 131.01067 ?  44  PHE B CD1 1 
ATOM 2307 C CD2 . PHE B 1 44  ? -19.16469 -21.12697 20.84572  1.000 128.05350 ?  44  PHE B CD2 1 
ATOM 2308 C CE1 . PHE B 1 44  ? -20.80701 -22.17799 22.80195  1.000 139.71715 ?  44  PHE B CE1 1 
ATOM 2309 C CE2 . PHE B 1 44  ? -19.32007 -22.50345 20.94837  1.000 115.47917 ?  44  PHE B CE2 1 
ATOM 2310 C CZ  . PHE B 1 44  ? -20.14172 -23.02945 21.92722  1.000 129.36341 ?  44  PHE B CZ  1 
ATOM 2311 N N   . SER B 1 45  ? -17.33169 -19.60606 23.35600  1.000 105.12075 ?  45  SER B N   1 
ATOM 2312 C CA  . SER B 1 45  ? -15.95064 -19.99926 23.59562  1.000 102.85404 ?  45  SER B CA  1 
ATOM 2313 C C   . SER B 1 45  ? -15.13078 -19.95624 22.30496  1.000 106.00384 ?  45  SER B C   1 
ATOM 2314 O O   . SER B 1 45  ? -15.65206 -20.14629 21.20214  1.000 118.32249 ?  45  SER B O   1 
ATOM 2315 C CB  . SER B 1 45  ? -15.90814 -21.39145 24.22647  1.000 97.39381  ?  45  SER B CB  1 
ATOM 2316 O OG  . SER B 1 45  ? -16.71874 -22.30262 23.50973  1.000 106.72367 ?  45  SER B OG  1 
ATOM 2317 N N   . ASN B 1 46  ? -13.82880 -19.68328 22.45991  1.000 102.07709 ?  46  ASN B N   1 
ATOM 2318 C CA  . ASN B 1 46  ? -12.87376 -19.61199 21.34654  1.000 103.63595 ?  46  ASN B CA  1 
ATOM 2319 C C   . ASN B 1 46  ? -13.26945 -18.53892 20.32930  1.000 97.03182  ?  46  ASN B C   1 
ATOM 2320 O O   . ASN B 1 46  ? -13.36468 -18.79016 19.12667  1.000 94.51295  ?  46  ASN B O   1 
ATOM 2321 C CB  . ASN B 1 46  ? -12.72197 -20.98049 20.68069  1.000 123.55051 ?  46  ASN B CB  1 
ATOM 2322 C CG  . ASN B 1 46  ? -12.46221 -22.08511 21.68871  1.000 127.11084 ?  46  ASN B CG  1 
ATOM 2323 O OD1 . ASN B 1 46  ? -13.38906 -22.76334 22.13678  1.000 111.48072 ?  46  ASN B OD1 1 
ATOM 2324 N ND2 . ASN B 1 46  ? -11.19762 -22.26576 22.05780  1.000 128.59662 ?  46  ASN B ND2 1 
ATOM 2325 N N   . ARG B 1 47  ? -13.47121 -17.32191 20.82874  1.000 96.86621  ?  47  ARG B N   1 
ATOM 2326 C CA  . ARG B 1 47  ? -13.88347 -16.16975 20.04078  1.000 85.10533  ?  47  ARG B CA  1 
ATOM 2327 C C   . ARG B 1 47  ? -12.99060 -14.98083 20.37537  1.000 92.78834  ?  47  ARG B C   1 
ATOM 2328 O O   . ARG B 1 47  ? -12.19700 -15.01251 21.31837  1.000 94.92107  ?  47  ARG B O   1 
ATOM 2329 C CB  . ARG B 1 47  ? -15.35305 -15.80741 20.30877  1.000 95.07767  ?  47  ARG B CB  1 
ATOM 2330 C CG  . ARG B 1 47  ? -16.37330 -16.88787 19.95077  1.000 100.44928 ?  47  ARG B CG  1 
ATOM 2331 C CD  . ARG B 1 47  ? -16.49834 -17.11269 18.45228  1.000 113.60490 ?  47  ARG B CD  1 
ATOM 2332 N NE  . ARG B 1 47  ? -17.73735 -17.79993 18.09494  1.000 125.34703 ?  47  ARG B NE  1 
ATOM 2333 C CZ  . ARG B 1 47  ? -17.96695 -19.09510 18.27800  1.000 126.21491 ?  47  ARG B CZ  1 
ATOM 2334 N NH1 . ARG B 1 47  ? -17.03795 -19.90334 18.76295  1.000 129.15340 ?  47  ARG B NH1 1 
ATOM 2335 N NH2 . ARG B 1 47  ? -19.15113 -19.59756 17.94228  1.000 125.25694 ?  47  ARG B NH2 1 
ATOM 2336 N N   . LEU B 1 48  ? -13.09305 -13.93842 19.55705  1.000 93.56498  ?  48  LEU B N   1 
ATOM 2337 C CA  . LEU B 1 48  ? -12.41549 -12.67028 19.78572  1.000 89.16929  ?  48  LEU B CA  1 
ATOM 2338 C C   . LEU B 1 48  ? -13.46281 -11.57592 19.94435  1.000 91.91633  ?  48  LEU B C   1 
ATOM 2339 O O   . LEU B 1 48  ? -14.34743 -11.43676 19.09787  1.000 93.31532  ?  48  LEU B O   1 
ATOM 2340 C CB  . LEU B 1 48  ? -11.47672 -12.34601 18.62239  1.000 91.79587  ?  48  LEU B CB  1 
ATOM 2341 C CG  . LEU B 1 48  ? -9.97809  -12.59357 18.78905  1.000 93.23260  ?  48  LEU B CG  1 
ATOM 2342 C CD1 . LEU B 1 48  ? -9.23823  -11.96091 17.62574  1.000 80.57650  ?  48  LEU B CD1 1 
ATOM 2343 C CD2 . LEU B 1 48  ? -9.45989  -12.06206 20.11893  1.000 91.33253  ?  48  LEU B CD2 1 
ATOM 2344 N N   . VAL B 1 49  ? -13.36503 -10.80330 21.01940  1.000 86.12168  ?  49  VAL B N   1 
ATOM 2345 C CA  . VAL B 1 49  ? -14.28765 -9.71363  21.30996  1.000 81.24078  ?  49  VAL B CA  1 
ATOM 2346 C C   . VAL B 1 49  ? -13.53232 -8.39711  21.22085  1.000 80.71815  ?  49  VAL B C   1 
ATOM 2347 O O   . VAL B 1 49  ? -12.41043 -8.27761  21.71873  1.000 73.73989  ?  49  VAL B O   1 
ATOM 2348 C CB  . VAL B 1 49  ? -14.93666 -9.88332  22.69761  1.000 90.38006  ?  49  VAL B CB  1 
ATOM 2349 C CG1 . VAL B 1 49  ? -16.11793 -8.94058  22.85589  1.000 88.04582  ?  49  VAL B CG1 1 
ATOM 2350 C CG2 . VAL B 1 49  ? -15.36561 -11.32924 22.90611  1.000 89.29003  ?  49  VAL B CG2 1 
ATOM 2351 N N   . PHE B 1 50  ? -14.15809 -7.40476  20.60356  1.000 87.61467  ?  50  PHE B N   1 
ATOM 2352 C CA  . PHE B 1 50  ? -13.59321 -6.07066  20.44985  1.000 81.52495  ?  50  PHE B CA  1 
ATOM 2353 C C   . PHE B 1 50  ? -14.51640 -5.12016  21.18817  1.000 77.04640  ?  50  PHE B C   1 
ATOM 2354 O O   . PHE B 1 50  ? -15.65093 -4.88730  20.74881  1.000 85.62904  ?  50  PHE B O   1 
ATOM 2355 C CB  . PHE B 1 50  ? -13.46050 -5.68004  18.98005  1.000 74.81641  ?  50  PHE B CB  1 
ATOM 2356 C CG  . PHE B 1 50  ? -12.51492 -6.54598  18.21923  1.000 87.75312  ?  50  PHE B CG  1 
ATOM 2357 C CD1 . PHE B 1 50  ? -12.90462 -7.80582  17.78712  1.000 84.70049  ?  50  PHE B CD1 1 
ATOM 2358 C CD2 . PHE B 1 50  ? -11.21427 -6.12488  17.97782  1.000 92.81989  ?  50  PHE B CD2 1 
ATOM 2359 C CE1 . PHE B 1 50  ? -12.02310 -8.61853  17.09480  1.000 94.17898  ?  50  PHE B CE1 1 
ATOM 2360 C CE2 . PHE B 1 50  ? -10.32222 -6.93236  17.29079  1.000 81.43867  ?  50  PHE B CE2 1 
ATOM 2361 C CZ  . PHE B 1 50  ? -10.72744 -8.18105  16.84742  1.000 97.49208  ?  50  PHE B CZ  1 
ATOM 2362 N N   . LEU B 1 51  ? -14.04982 -4.63482  22.33680  1.000 84.45853  ?  51  LEU B N   1 
ATOM 2363 C CA  . LEU B 1 51  ? -14.78152 -3.69427  23.17336  1.000 92.92223  ?  51  LEU B CA  1 
ATOM 2364 C C   . LEU B 1 51  ? -14.11907 -2.32931  23.04652  1.000 76.19965  ?  51  LEU B C   1 
ATOM 2365 O O   . LEU B 1 51  ? -12.90320 -2.19553  23.24956  1.000 83.21951  ?  51  LEU B O   1 
ATOM 2366 C CB  . LEU B 1 51  ? -14.82299 -4.17303  24.62760  1.000 76.75629  ?  51  LEU B CB  1 
ATOM 2367 C CG  . LEU B 1 51  ? -15.15711 -5.67159  24.73105  1.000 79.88206  ?  51  LEU B CG  1 
ATOM 2368 C CD1 . LEU B 1 51  ? -13.96305 -6.45407  25.23656  1.000 88.53893  ?  51  LEU B CD1 1 
ATOM 2369 C CD2 . LEU B 1 51  ? -16.38183 -5.97064  25.58149  1.000 72.18313  ?  51  LEU B CD2 1 
ATOM 2370 N N   . GLU B 1 52  ? -14.90966 -1.33152  22.67162  1.000 80.08241  ?  52  GLU B N   1 
ATOM 2371 C CA  . GLU B 1 52  ? -14.36248 -0.00703  22.45715  1.000 85.40498  ?  52  GLU B CA  1 
ATOM 2372 C C   . GLU B 1 52  ? -14.19807 0.71704   23.78554  1.000 86.45914  ?  52  GLU B C   1 
ATOM 2373 O O   . GLU B 1 52  ? -14.81623 0.37274   24.79274  1.000 106.00814 ?  52  GLU B O   1 
ATOM 2374 C CB  . GLU B 1 52  ? -15.25157 0.80612   21.51698  1.000 94.22241  ?  52  GLU B CB  1 
ATOM 2375 C CG  . GLU B 1 52  ? -16.41119 1.51972   22.18515  1.000 94.74019  ?  52  GLU B CG  1 
ATOM 2376 C CD  . GLU B 1 52  ? -17.16436 2.42384   21.21622  1.000 105.63236 ?  52  GLU B CD  1 
ATOM 2377 O OE1 . GLU B 1 52  ? -16.95228 2.29086   19.98962  1.000 106.85495 ?  52  GLU B OE1 1 
ATOM 2378 O OE2 . GLU B 1 52  ? -17.95506 3.27600   21.68023  1.000 106.20386 -1 52  GLU B OE2 1 
ATOM 2379 N N   . ARG B 1 53  ? -13.33302 1.72085   23.78087  1.000 85.92681  ?  53  ARG B N   1 
ATOM 2380 C CA  . ARG B 1 53  ? -13.01062 2.44296   25.00352  1.000 88.05903  ?  53  ARG B CA  1 
ATOM 2381 C C   . ARG B 1 53  ? -14.21970 3.24374   25.47638  1.000 91.43697  ?  53  ARG B C   1 
ATOM 2382 O O   . ARG B 1 53  ? -14.78031 4.04384   24.71943  1.000 96.50903  ?  53  ARG B O   1 
ATOM 2383 C CB  . ARG B 1 53  ? -11.81275 3.36102   24.76948  1.000 86.22216  ?  53  ARG B CB  1 
ATOM 2384 C CG  . ARG B 1 53  ? -11.25557 3.99383   26.03160  1.000 77.97903  ?  53  ARG B CG  1 
ATOM 2385 C CD  . ARG B 1 53  ? -10.18274 5.02407   25.70995  1.000 63.72916  ?  53  ARG B CD  1 
ATOM 2386 N NE  . ARG B 1 53  ? -10.68276 6.03652   24.78898  1.000 81.43331  ?  53  ARG B NE  1 
ATOM 2387 C CZ  . ARG B 1 53  ? -11.38255 7.10624   25.14552  1.000 81.64188  ?  53  ARG B CZ  1 
ATOM 2388 N NH1 . ARG B 1 53  ? -11.67253 7.35530   26.41156  1.000 76.44400  ?  53  ARG B NH1 1 
ATOM 2389 N NH2 . ARG B 1 53  ? -11.80763 7.94492   24.20494  1.000 87.67183  ?  53  ARG B NH2 1 
ATOM 2390 N N   . GLY B 1 54  ? -14.64747 2.99958   26.71115  1.000 93.22203  ?  54  GLY B N   1 
ATOM 2391 C CA  . GLY B 1 54  ? -15.67235 3.80392   27.35237  1.000 80.63301  ?  54  GLY B CA  1 
ATOM 2392 C C   . GLY B 1 54  ? -16.96611 3.08541   27.65690  1.000 86.50101  ?  54  GLY B C   1 
ATOM 2393 O O   . GLY B 1 54  ? -17.75786 3.59940   28.46111  1.000 96.07153  ?  54  GLY B O   1 
ATOM 2394 N N   . VAL B 1 55  ? -17.21202 1.90769   27.08315  1.000 91.25264  ?  55  VAL B N   1 
ATOM 2395 C CA  . VAL B 1 55  ? -18.49126 1.23141   27.27020  1.000 84.31514  ?  55  VAL B CA  1 
ATOM 2396 C C   . VAL B 1 55  ? -18.57875 0.72585   28.70225  1.000 92.55145  ?  55  VAL B C   1 
ATOM 2397 O O   . VAL B 1 55  ? -17.72946 -0.05146  29.15746  1.000 96.00755  ?  55  VAL B O   1 
ATOM 2398 C CB  . VAL B 1 55  ? -18.66575 0.08054   26.26941  1.000 84.22081  ?  55  VAL B CB  1 
ATOM 2399 C CG1 . VAL B 1 55  ? -19.01034 0.61343   24.89069  1.000 99.50304  ?  55  VAL B CG1 1 
ATOM 2400 C CG2 . VAL B 1 55  ? -17.41690 -0.78229  26.20914  1.000 84.96027  ?  55  VAL B CG2 1 
ATOM 2401 N N   . ASN B 1 56  ? -19.58969 1.18550   29.42936  1.000 83.69082  ?  56  ASN B N   1 
ATOM 2402 C CA  . ASN B 1 56  ? -19.89389 0.64490   30.74689  1.000 81.39946  ?  56  ASN B CA  1 
ATOM 2403 C C   . ASN B 1 56  ? -20.80636 -0.56442  30.56449  1.000 79.17952  ?  56  ASN B C   1 
ATOM 2404 O O   . ASN B 1 56  ? -21.96638 -0.42821  30.16058  1.000 74.34400  ?  56  ASN B O   1 
ATOM 2405 C CB  . ASN B 1 56  ? -20.53932 1.70407   31.62725  1.000 84.15305  ?  56  ASN B CB  1 
ATOM 2406 C CG  . ASN B 1 56  ? -20.65821 1.25766   33.04607  1.000 76.90317  ?  56  ASN B CG  1 
ATOM 2407 O OD1 . ASN B 1 56  ? -19.69781 1.32631   33.81001  1.000 92.24680  ?  56  ASN B OD1 1 
ATOM 2408 N ND2 . ASN B 1 56  ? -21.83114 0.75947   33.40868  1.000 85.28046  ?  56  ASN B ND2 1 
ATOM 2409 N N   . ILE B 1 57  ? -20.28438 -1.74816  30.85077  1.000 72.65478  ?  57  ILE B N   1 
ATOM 2410 C CA  . ILE B 1 57  ? -21.00951 -2.97897  30.58823  1.000 77.78932  ?  57  ILE B CA  1 
ATOM 2411 C C   . ILE B 1 57  ? -21.13923 -3.77418  31.87655  1.000 67.32994  ?  57  ILE B C   1 
ATOM 2412 O O   . ILE B 1 57  ? -20.44433 -3.53049  32.86282  1.000 76.01386  ?  57  ILE B O   1 
ATOM 2413 C CB  . ILE B 1 57  ? -20.32337 -3.81592  29.49368  1.000 65.67767  ?  57  ILE B CB  1 
ATOM 2414 C CG1 . ILE B 1 57  ? -18.94594 -4.27142  29.97216  1.000 75.90428  ?  57  ILE B CG1 1 
ATOM 2415 C CG2 . ILE B 1 57  ? -20.22528 -3.02656  28.19784  1.000 79.03063  ?  57  ILE B CG2 1 
ATOM 2416 C CD1 . ILE B 1 57  ? -18.37933 -5.42535  29.19538  1.000 75.31935  ?  57  ILE B CD1 1 
ATOM 2417 N N   . SER B 1 58  ? -22.05536 -4.73018  31.85432  1.000 64.52792  ?  58  SER B N   1 
ATOM 2418 C CA  . SER B 1 58  ? -22.18523 -5.73335  32.89471  1.000 64.92085  ?  58  SER B CA  1 
ATOM 2419 C C   . SER B 1 58  ? -22.00754 -7.06962  32.21064  1.000 70.31723  ?  58  SER B C   1 
ATOM 2420 O O   . SER B 1 58  ? -22.34117 -7.20267  31.03430  1.000 80.21671  ?  58  SER B O   1 
ATOM 2421 C CB  . SER B 1 58  ? -23.53899 -5.65988  33.59294  1.000 71.55467  ?  58  SER B CB  1 
ATOM 2422 O OG  . SER B 1 58  ? -23.66661 -4.44335  34.30646  1.000 89.82473  ?  58  SER B OG  1 
ATOM 2423 N N   . VAL B 1 59  ? -21.39864 -8.03260  32.89358  1.000 67.11623  ?  59  VAL B N   1 
ATOM 2424 C CA  . VAL B 1 59  ? -21.07550 -9.30332  32.25578  1.000 78.73511  ?  59  VAL B CA  1 
ATOM 2425 C C   . VAL B 1 59  ? -21.50595 -10.46257 33.14211  1.000 82.17830  ?  59  VAL B C   1 
ATOM 2426 O O   . VAL B 1 59  ? -21.42075 -10.38604 34.37254  1.000 90.58706  ?  59  VAL B O   1 
ATOM 2427 C CB  . VAL B 1 59  ? -19.57504 -9.40861  31.91506  1.000 77.16649  ?  59  VAL B CB  1 
ATOM 2428 C CG1 . VAL B 1 59  ? -19.31503 -10.62269 31.02669  1.000 85.64840  ?  59  VAL B CG1 1 
ATOM 2429 C CG2 . VAL B 1 59  ? -19.09748 -8.14582  31.23917  1.000 73.18368  ?  59  VAL B CG2 1 
ATOM 2430 N N   . ARG B 1 60  ? -22.00235 -11.52271 32.50723  1.000 83.29704  ?  60  ARG B N   1 
ATOM 2431 C CA  . ARG B 1 60  ? -22.21688 -12.82257 33.13499  1.000 89.77661  ?  60  ARG B CA  1 
ATOM 2432 C C   . ARG B 1 60  ? -21.25139 -13.81073 32.49956  1.000 89.10512  ?  60  ARG B C   1 
ATOM 2433 O O   . ARG B 1 60  ? -21.41252 -14.17488 31.33012  1.000 101.14082 ?  60  ARG B O   1 
ATOM 2434 C CB  . ARG B 1 60  ? -23.63441 -13.35228 32.95903  1.000 105.02446 ?  60  ARG B CB  1 
ATOM 2435 C CG  . ARG B 1 60  ? -23.80246 -14.66709 33.72097  1.000 101.65401 ?  60  ARG B CG  1 
ATOM 2436 C CD  . ARG B 1 60  ? -25.16604 -15.29758 33.55225  1.000 121.10383 ?  60  ARG B CD  1 
ATOM 2437 N NE  . ARG B 1 60  ? -25.37493 -15.64575 32.14937  1.000 137.63974 ?  60  ARG B NE  1 
ATOM 2438 C CZ  . ARG B 1 60  ? -25.09547 -16.82737 31.61066  1.000 129.36155 ?  60  ARG B CZ  1 
ATOM 2439 N NH1 . ARG B 1 60  ? -24.45436 -17.76621 32.29100  1.000 97.11025  ?  60  ARG B NH1 1 
ATOM 2440 N NH2 . ARG B 1 60  ? -25.41897 -17.05316 30.33930  1.000 126.07612 ?  60  ARG B NH2 1 
ATOM 2441 N N   . MET B 1 61  ? -20.25595 -14.23829 33.25911  1.000 81.84858  ?  61  MET B N   1 
ATOM 2442 C CA  . MET B 1 61  ? -19.24257 -15.15092 32.76141  1.000 76.67983  ?  61  MET B CA  1 
ATOM 2443 C C   . MET B 1 61  ? -19.48641 -16.54444 33.31475  1.000 76.19011  ?  61  MET B C   1 
ATOM 2444 O O   . MET B 1 61  ? -19.84903 -16.71566 34.48404  1.000 87.63689  ?  61  MET B O   1 
ATOM 2445 C CB  . MET B 1 61  ? -17.84437 -14.68033 33.13924  1.000 80.48006  ?  61  MET B CB  1 
ATOM 2446 C CG  . MET B 1 61  ? -17.64413 -13.20049 32.94620  1.000 91.89280  ?  61  MET B CG  1 
ATOM 2447 S SD  . MET B 1 61  ? -15.90459 -12.81740 33.07377  1.000 92.83465  ?  61  MET B SD  1 
ATOM 2448 C CE  . MET B 1 61  ? -15.27467 -14.09227 32.00278  1.000 86.04829  ?  61  MET B CE  1 
ATOM 2449 N N   . GLN B 1 62  ? -19.29065 -17.53252 32.45587  1.000 79.02469  ?  62  GLN B N   1 
ATOM 2450 C CA  . GLN B 1 62  ? -19.42661 -18.93801 32.80710  1.000 85.22086  ?  62  GLN B CA  1 
ATOM 2451 C C   . GLN B 1 62  ? -18.13199 -19.63961 32.41644  1.000 104.39420 ?  62  GLN B C   1 
ATOM 2452 O O   . GLN B 1 62  ? -17.81787 -19.75079 31.22716  1.000 95.55565  ?  62  GLN B O   1 
ATOM 2453 C CB  . GLN B 1 62  ? -20.63309 -19.53849 32.09075  1.000 96.76183  ?  62  GLN B CB  1 
ATOM 2454 C CG  . GLN B 1 62  ? -20.76957 -21.03684 32.15902  1.000 103.32866 ?  62  GLN B CG  1 
ATOM 2455 C CD  . GLN B 1 62  ? -21.67462 -21.54584 31.05693  1.000 114.11790 ?  62  GLN B CD  1 
ATOM 2456 O OE1 . GLN B 1 62  ? -22.75614 -20.99773 30.82564  1.000 112.75932 ?  62  GLN B OE1 1 
ATOM 2457 N NE2 . GLN B 1 62  ? -21.23720 -22.59304 30.36422  1.000 106.59495 ?  62  GLN B NE2 1 
ATOM 2458 N N   . LYS B 1 63  ? -17.37089 -20.08330 33.41215  1.000 110.17629 ?  63  LYS B N   1 
ATOM 2459 C CA  . LYS B 1 63  ? -16.11073 -20.76827 33.16439  1.000 93.17510  ?  63  LYS B CA  1 
ATOM 2460 C C   . LYS B 1 63  ? -16.35107 -22.20357 32.71943  1.000 99.84817  ?  63  LYS B C   1 
ATOM 2461 O O   . LYS B 1 63  ? -17.20133 -22.90584 33.27529  1.000 100.14679 ?  63  LYS B O   1 
ATOM 2462 C CB  . LYS B 1 63  ? -15.25878 -20.77853 34.43142  1.000 110.58208 ?  63  LYS B CB  1 
ATOM 2463 C CG  . LYS B 1 63  ? -14.24861 -19.66278 34.57635  1.000 99.01418  ?  63  LYS B CG  1 
ATOM 2464 C CD  . LYS B 1 63  ? -13.37567 -19.95640 35.78848  1.000 98.92211  ?  63  LYS B CD  1 
ATOM 2465 C CE  . LYS B 1 63  ? -12.32732 -18.89822 35.99725  1.000 93.61932  ?  63  LYS B CE  1 
ATOM 2466 N NZ  . LYS B 1 63  ? -11.50062 -19.20872 37.19092  1.000 102.46884 ?  63  LYS B NZ  1 
ATOM 2467 N N   . GLN B 1 64  ? -15.60278 -22.63693 31.70284  1.000 105.95514 ?  64  GLN B N   1 
ATOM 2468 C CA  . GLN B 1 64  ? -15.60041 -24.05171 31.33656  1.000 106.97601 ?  64  GLN B CA  1 
ATOM 2469 C C   . GLN B 1 64  ? -14.66982 -24.84313 32.25181  1.000 104.92374 ?  64  GLN B C   1 
ATOM 2470 O O   . GLN B 1 64  ? -15.08733 -25.81333 32.89185  1.000 104.20042 ?  64  GLN B O   1 
ATOM 2471 C CB  . GLN B 1 64  ? -15.21210 -24.22782 29.86322  1.000 105.56985 ?  64  GLN B CB  1 
ATOM 2472 C CG  . GLN B 1 64  ? -15.92078 -23.26704 28.90729  1.000 105.57747 ?  64  GLN B CG  1 
ATOM 2473 C CD  . GLN B 1 64  ? -15.63780 -23.56812 27.44351  1.000 113.57497 ?  64  GLN B CD  1 
ATOM 2474 O OE1 . GLN B 1 64  ? -14.63968 -23.11282 26.88327  1.000 103.35840 ?  64  GLN B OE1 1 
ATOM 2475 N NE2 . GLN B 1 64  ? -16.51455 -24.34890 26.82008  1.000 108.25417 ?  64  GLN B NE2 1 
ATOM 2476 N N   . ILE B 1 65  ? -13.40219 -24.44145 32.32265  1.000 109.35490 ?  65  ILE B N   1 
ATOM 2477 C CA  . ILE B 1 65  ? -12.43487 -25.00213 33.25983  1.000 97.87765  ?  65  ILE B CA  1 
ATOM 2478 C C   . ILE B 1 65  ? -12.20609 -23.98511 34.36918  1.000 115.64987 ?  65  ILE B C   1 
ATOM 2479 O O   . ILE B 1 65  ? -11.91711 -22.81338 34.09449  1.000 119.11453 ?  65  ILE B O   1 
ATOM 2480 C CB  . ILE B 1 65  ? -11.12021 -25.38113 32.55870  1.000 109.10371 ?  65  ILE B CB  1 
ATOM 2481 C CG1 . ILE B 1 65  ? -11.37453 -26.48616 31.52613  1.000 111.87364 ?  65  ILE B CG1 1 
ATOM 2482 C CG2 . ILE B 1 65  ? -10.07964 -25.81134 33.57870  1.000 113.40896 ?  65  ILE B CG2 1 
ATOM 2483 C CD1 . ILE B 1 65  ? -11.09010 -26.10007 30.08784  1.000 104.92039 ?  65  ILE B CD1 1 
ATOM 2484 N N   . LEU B 1 66  ? -12.33848 -24.43571 35.62189  1.000 133.18601 ?  66  LEU B N   1 
ATOM 2485 C CA  . LEU B 1 66  ? -12.34757 -23.52972 36.76929  1.000 132.78308 ?  66  LEU B CA  1 
ATOM 2486 C C   . LEU B 1 66  ? -10.95074 -23.09360 37.19868  1.000 133.41519 ?  66  LEU B C   1 
ATOM 2487 O O   . LEU B 1 66  ? -10.75216 -21.92975 37.56617  1.000 133.35909 ?  66  LEU B O   1 
ATOM 2488 C CB  . LEU B 1 66  ? -13.05378 -24.19514 37.94909  1.000 137.50450 ?  66  LEU B CB  1 
ATOM 2489 C CG  . LEU B 1 66  ? -14.57860 -24.24856 37.91896  1.000 148.78316 ?  66  LEU B CG  1 
ATOM 2490 C CD1 . LEU B 1 66  ? -15.07265 -25.51648 37.23070  1.000 153.43776 ?  66  LEU B CD1 1 
ATOM 2491 C CD2 . LEU B 1 66  ? -15.13426 -24.13960 39.33572  1.000 146.90938 ?  66  LEU B CD2 1 
ATOM 2492 N N   . SER B 1 67  ? -9.98073  -24.01251 37.18102  1.000 120.66175 ?  67  SER B N   1 
ATOM 2493 C CA  . SER B 1 67  ? -8.65232  -23.71009 37.71153  1.000 130.03993 ?  67  SER B CA  1 
ATOM 2494 C C   . SER B 1 67  ? -7.96358  -22.58107 36.95216  1.000 129.21468 ?  67  SER B C   1 
ATOM 2495 O O   . SER B 1 67  ? -7.15356  -21.84843 37.53451  1.000 119.94312 ?  67  SER B O   1 
ATOM 2496 C CB  . SER B 1 67  ? -7.77735  -24.96688 37.69137  1.000 133.02307 ?  67  SER B CB  1 
ATOM 2497 O OG  . SER B 1 67  ? -7.28978  -25.24074 36.38743  1.000 127.29857 ?  67  SER B OG  1 
ATOM 2498 N N   . GLU B 1 68  ? -8.26723  -22.41745 35.66725  1.000 135.88865 ?  68  GLU B N   1 
ATOM 2499 C CA  . GLU B 1 68  ? -7.56647  -21.44288 34.84811  1.000 133.71295 ?  68  GLU B CA  1 
ATOM 2500 C C   . GLU B 1 68  ? -8.28666  -20.09745 34.86303  1.000 119.92292 ?  68  GLU B C   1 
ATOM 2501 O O   . GLU B 1 68  ? -9.36349  -19.93644 35.44318  1.000 112.16981 ?  68  GLU B O   1 
ATOM 2502 C CB  . GLU B 1 68  ? -7.42976  -21.94182 33.40998  1.000 142.82603 ?  68  GLU B CB  1 
ATOM 2503 C CG  . GLU B 1 68  ? -6.55068  -23.16220 33.23081  1.000 157.89155 ?  68  GLU B CG  1 
ATOM 2504 C CD  . GLU B 1 68  ? -6.34944  -23.50880 31.76778  1.000 175.17930 ?  68  GLU B CD  1 
ATOM 2505 O OE1 . GLU B 1 68  ? -7.00613  -22.87625 30.90976  1.000 162.03331 ?  68  GLU B OE1 1 
ATOM 2506 O OE2 . GLU B 1 68  ? -5.53626  -24.41227 31.47719  1.000 193.35416 -1 68  GLU B OE2 1 
ATOM 2507 N N   . LYS B 1 69  ? -7.68074  -19.11695 34.19804  1.000 104.22260 ?  69  LYS B N   1 
ATOM 2508 C CA  . LYS B 1 69  ? -8.30761  -17.82274 34.06107  1.000 98.64669  ?  69  LYS B CA  1 
ATOM 2509 C C   . LYS B 1 69  ? -9.49311  -17.92381 33.10350  1.000 97.96079  ?  69  LYS B C   1 
ATOM 2510 O O   . LYS B 1 69  ? -9.59251  -18.86570 32.31078  1.000 87.32160  ?  69  LYS B O   1 
ATOM 2511 C CB  . LYS B 1 69  ? -7.30695  -16.78325 33.55234  1.000 95.92102  ?  69  LYS B CB  1 
ATOM 2512 C CG  . LYS B 1 69  ? -6.76972  -17.03767 32.14246  1.000 101.98795 ?  69  LYS B CG  1 
ATOM 2513 C CD  . LYS B 1 69  ? -5.55901  -16.14706 31.82164  1.000 103.24774 ?  69  LYS B CD  1 
ATOM 2514 C CE  . LYS B 1 69  ? -4.22896  -16.89058 31.83837  1.000 108.71143 ?  69  LYS B CE  1 
ATOM 2515 N NZ  . LYS B 1 69  ? -3.08294  -15.97521 31.52065  1.000 96.11513  ?  69  LYS B NZ  1 
ATOM 2516 N N   . PRO B 1 70  ? -10.41052 -16.96693 33.16546  1.000 95.78716  ?  70  PRO B N   1 
ATOM 2517 C CA  . PRO B 1 70  ? -11.55712 -16.98508 32.24728  1.000 92.22286  ?  70  PRO B CA  1 
ATOM 2518 C C   . PRO B 1 70  ? -11.16221 -16.70316 30.80953  1.000 87.28347  ?  70  PRO B C   1 
ATOM 2519 O O   . PRO B 1 70  ? -11.44197 -17.50803 29.91914  1.000 91.34525  ?  70  PRO B O   1 
ATOM 2520 C CB  . PRO B 1 70  ? -12.45995 -15.87621 32.79586  1.000 92.70847  ?  70  PRO B CB  1 
ATOM 2521 C CG  . PRO B 1 70  ? -12.03031 -15.70523 34.22582  1.000 99.68648  ?  70  PRO B CG  1 
ATOM 2522 C CD  . PRO B 1 70  ? -10.55761 -15.93705 34.20685  1.000 86.70076  ?  70  PRO B CD  1 
ATOM 2523 N N   . TYR B 1 71  ? -10.50095 -15.57073 30.57441  1.000 82.43987  ?  71  TYR B N   1 
ATOM 2524 C CA  . TYR B 1 71  ? -10.25074 -15.08451 29.22868  1.000 80.47212  ?  71  TYR B CA  1 
ATOM 2525 C C   . TYR B 1 71  ? -8.81747  -14.57365 29.13496  1.000 90.52947  ?  71  TYR B C   1 
ATOM 2526 O O   . TYR B 1 71  ? -8.08301  -14.54130 30.12605  1.000 92.35909  ?  71  TYR B O   1 
ATOM 2527 C CB  . TYR B 1 71  ? -11.25415 -13.98871 28.85715  1.000 82.07153  ?  71  TYR B CB  1 
ATOM 2528 C CG  . TYR B 1 71  ? -11.29986 -12.81150 29.80790  1.000 65.93896  ?  71  TYR B CG  1 
ATOM 2529 C CD1 . TYR B 1 71  ? -10.34049 -11.80791 29.75318  1.000 67.04748  ?  71  TYR B CD1 1 
ATOM 2530 C CD2 . TYR B 1 71  ? -12.29576 -12.70852 30.76359  1.000 73.78989  ?  71  TYR B CD2 1 
ATOM 2531 C CE1 . TYR B 1 71  ? -10.37876 -10.72911 30.61888  1.000 80.25655  ?  71  TYR B CE1 1 
ATOM 2532 C CE2 . TYR B 1 71  ? -12.34593 -11.63193 31.63537  1.000 73.42994  ?  71  TYR B CE2 1 
ATOM 2533 C CZ  . TYR B 1 71  ? -11.38490 -10.64517 31.56140  1.000 78.48117  ?  71  TYR B CZ  1 
ATOM 2534 O OH  . TYR B 1 71  ? -11.43169 -9.57538  32.42951  1.000 66.58042  ?  71  TYR B OH  1 
ATOM 2535 N N   . VAL B 1 72  ? -8.42120  -14.16264 27.92904  1.000 77.76930  ?  72  VAL B N   1 
ATOM 2536 C CA  . VAL B 1 72  ? -7.09962  -13.59689 27.67107  1.000 72.60255  ?  72  VAL B CA  1 
ATOM 2537 C C   . VAL B 1 72  ? -7.28953  -12.20738 27.06970  1.000 78.39197  ?  72  VAL B C   1 
ATOM 2538 O O   . VAL B 1 72  ? -7.84531  -12.07774 25.97793  1.000 84.79490  ?  72  VAL B O   1 
ATOM 2539 C CB  . VAL B 1 72  ? -6.28453  -14.49806 26.72985  1.000 93.80530  ?  72  VAL B CB  1 
ATOM 2540 C CG1 . VAL B 1 72  ? -4.84649  -13.99811 26.60827  1.000 106.33957 ?  72  VAL B CG1 1 
ATOM 2541 C CG2 . VAL B 1 72  ? -6.33925  -15.95301 27.20233  1.000 85.71826  ?  72  VAL B CG2 1 
ATOM 2542 N N   . ALA B 1 73  ? -6.79474  -11.17370 27.74382  1.000 73.89032  ?  73  ALA B N   1 
ATOM 2543 C CA  . ALA B 1 73  ? -7.11112  -9.80617  27.34882  1.000 76.17032  ?  73  ALA B CA  1 
ATOM 2544 C C   . ALA B 1 73  ? -5.91952  -9.10887  26.69972  1.000 88.85570  ?  73  ALA B C   1 
ATOM 2545 O O   . ALA B 1 73  ? -4.76242  -9.47302  26.92693  1.000 88.41840  ?  73  ALA B O   1 
ATOM 2546 C CB  . ALA B 1 73  ? -7.59405  -8.98865  28.54786  1.000 74.14779  ?  73  ALA B CB  1 
ATOM 2547 N N   . PHE B 1 74  ? -6.22480  -8.11991  25.85292  1.000 89.95763  ?  74  PHE B N   1 
ATOM 2548 C CA  . PHE B 1 74  ? -5.22549  -7.28343  25.18733  1.000 88.22879  ?  74  PHE B CA  1 
ATOM 2549 C C   . PHE B 1 74  ? -5.73580  -5.84706  25.21408  1.000 84.97557  ?  74  PHE B C   1 
ATOM 2550 O O   . PHE B 1 74  ? -6.69186  -5.52021  24.50879  1.000 83.98966  ?  74  PHE B O   1 
ATOM 2551 C CB  . PHE B 1 74  ? -4.98209  -7.74798  23.74508  1.000 82.38108  ?  74  PHE B CB  1 
ATOM 2552 C CG  . PHE B 1 74  ? -4.60134  -9.20819  23.62208  1.000 95.18032  ?  74  PHE B CG  1 
ATOM 2553 C CD1 . PHE B 1 74  ? -3.27398  -9.60379  23.70674  1.000 98.57509  ?  74  PHE B CD1 1 
ATOM 2554 C CD2 . PHE B 1 74  ? -5.57113  -10.18333 23.41652  1.000 97.52019  ?  74  PHE B CD2 1 
ATOM 2555 C CE1 . PHE B 1 74  ? -2.92250  -10.93844 23.59611  1.000 95.74188  ?  74  PHE B CE1 1 
ATOM 2556 C CE2 . PHE B 1 74  ? -5.22810  -11.52351 23.30717  1.000 87.70014  ?  74  PHE B CE2 1 
ATOM 2557 C CZ  . PHE B 1 74  ? -3.90205  -11.89959 23.39692  1.000 99.45296  ?  74  PHE B CZ  1 
ATOM 2558 N N   . ARG B 1 75  ? -5.10033  -4.98863  26.00567  1.000 81.42257  ?  75  ARG B N   1 
ATOM 2559 C CA  . ARG B 1 75  ? -5.53282  -3.60832  26.18872  1.000 80.38673  ?  75  ARG B CA  1 
ATOM 2560 C C   . ARG B 1 75  ? -4.58986  -2.66007  25.45051  1.000 76.98035  ?  75  ARG B C   1 
ATOM 2561 O O   . ARG B 1 75  ? -3.38490  -2.91298  25.36680  1.000 88.67961  ?  75  ARG B O   1 
ATOM 2562 C CB  . ARG B 1 75  ? -5.58756  -3.26074  27.68601  1.000 83.29633  ?  75  ARG B CB  1 
ATOM 2563 C CG  . ARG B 1 75  ? -6.52023  -4.15755  28.52941  1.000 79.83346  ?  75  ARG B CG  1 
ATOM 2564 C CD  . ARG B 1 75  ? -6.19105  -4.10507  30.03424  1.000 74.14103  ?  75  ARG B CD  1 
ATOM 2565 N NE  . ARG B 1 75  ? -6.34651  -2.77612  30.62311  1.000 122.72425 ?  75  ARG B NE  1 
ATOM 2566 C CZ  . ARG B 1 75  ? -5.63930  -2.31571  31.65188  1.000 120.67076 ?  75  ARG B CZ  1 
ATOM 2567 N NH1 . ARG B 1 75  ? -4.65098  -3.01854  32.18546  1.000 98.66490  ?  75  ARG B NH1 1 
ATOM 2568 N NH2 . ARG B 1 75  ? -5.91372  -1.10790  32.14252  1.000 102.22002 ?  75  ARG B NH2 1 
ATOM 2569 N N   . LEU B 1 76  ? -5.13637  -1.58141  24.89191  1.000 71.18570  ?  76  LEU B N   1 
ATOM 2570 C CA  . LEU B 1 76  ? -4.35636  -0.63411  24.09918  1.000 70.53321  ?  76  LEU B CA  1 
ATOM 2571 C C   . LEU B 1 76  ? -4.29224  0.70806   24.81566  1.000 80.67086  ?  76  LEU B C   1 
ATOM 2572 O O   . LEU B 1 76  ? -5.33144  1.32815   25.06658  1.000 82.05877  ?  76  LEU B O   1 
ATOM 2573 C CB  . LEU B 1 76  ? -4.96275  -0.45544  22.70894  1.000 81.71397  ?  76  LEU B CB  1 
ATOM 2574 C CG  . LEU B 1 76  ? -4.49787  -1.37539  21.58374  1.000 82.80077  ?  76  LEU B CG  1 
ATOM 2575 C CD1 . LEU B 1 76  ? -5.02778  -2.78290  21.78945  1.000 82.21489  ?  76  LEU B CD1 1 
ATOM 2576 C CD2 . LEU B 1 76  ? -4.99121  -0.82701  20.26194  1.000 98.42621  ?  76  LEU B CD2 1 
ATOM 2577 N N   . ASN B 1 77  ? -3.07585  1.17390   25.10140  1.000 88.42359  ?  77  ASN B N   1 
ATOM 2578 C CA  . ASN B 1 77  ? -2.90010  2.48313   25.71330  1.000 80.71900  ?  77  ASN B CA  1 
ATOM 2579 C C   . ASN B 1 77  ? -3.25547  3.57996   24.71290  1.000 84.82659  ?  77  ASN B C   1 
ATOM 2580 O O   . ASN B 1 77  ? -3.48916  3.32656   23.52847  1.000 96.76468  ?  77  ASN B O   1 
ATOM 2581 C CB  . ASN B 1 77  ? -1.46531  2.66440   26.21803  1.000 86.87892  ?  77  ASN B CB  1 
ATOM 2582 C CG  . ASN B 1 77  ? -0.43783  2.61197   25.10174  1.000 100.86545 ?  77  ASN B CG  1 
ATOM 2583 O OD1 . ASN B 1 77  ? -0.16997  3.61734   24.44033  1.000 94.16521  ?  77  ASN B OD1 1 
ATOM 2584 N ND2 . ASN B 1 77  ? 0.14881   1.43712   24.88997  1.000 108.28815 ?  77  ASN B ND2 1 
ATOM 2585 N N   . GLY B 1 78  ? -3.31531  4.81490   25.21557  1.000 94.18862  ?  78  GLY B N   1 
ATOM 2586 C CA  . GLY B 1 78  ? -3.67274  5.94107   24.36134  1.000 104.82711 ?  78  GLY B CA  1 
ATOM 2587 C C   . GLY B 1 78  ? -2.76792  6.09134   23.15479  1.000 114.22159 ?  78  GLY B C   1 
ATOM 2588 O O   . GLY B 1 78  ? -3.23808  6.23889   22.02309  1.000 99.50973  ?  78  GLY B O   1 
ATOM 2589 N N   . ASP B 1 79  ? -1.44961  6.07984   23.37480  1.000 117.14891 ?  79  ASP B N   1 
ATOM 2590 C CA  . ASP B 1 79  ? -0.50096  6.24753   22.27724  1.000 118.36573 ?  79  ASP B CA  1 
ATOM 2591 C C   . ASP B 1 79  ? -0.61913  5.12140   21.25327  1.000 110.71166 ?  79  ASP B C   1 
ATOM 2592 O O   . ASP B 1 79  ? -0.63821  5.36804   20.04189  1.000 111.81998 ?  79  ASP B O   1 
ATOM 2593 C CB  . ASP B 1 79  ? 0.92191   6.35067   22.82039  1.000 121.52028 ?  79  ASP B CB  1 
ATOM 2594 C CG  . ASP B 1 79  ? 1.33593   7.78430   23.06300  1.000 130.41784 ?  79  ASP B CG  1 
ATOM 2595 O OD1 . ASP B 1 79  ? 1.06283   8.63410   22.18907  1.000 133.47661 -1 79  ASP B OD1 1 
ATOM 2596 O OD2 . ASP B 1 79  ? 1.93092   8.06412   24.12153  1.000 138.75029 ?  79  ASP B OD2 1 
ATOM 2597 N N   . MET B 1 80  ? -0.62205  3.87222   21.72255  1.000 99.64812  ?  80  MET B N   1 
ATOM 2598 C CA  . MET B 1 80  ? -0.78189  2.73990   20.81703  1.000 82.87550  ?  80  MET B CA  1 
ATOM 2599 C C   . MET B 1 80  ? -2.08525  2.83831   20.03425  1.000 97.70325  ?  80  MET B C   1 
ATOM 2600 O O   . MET B 1 80  ? -2.11845  2.58390   18.82286  1.000 104.84704 ?  80  MET B O   1 
ATOM 2601 C CB  . MET B 1 80  ? -0.73422  1.43396   21.59868  1.000 79.50470  ?  80  MET B CB  1 
ATOM 2602 C CG  . MET B 1 80  ? -0.84479  0.22150   20.71164  1.000 92.62945  ?  80  MET B CG  1 
ATOM 2603 S SD  . MET B 1 80  ? -0.24585  -1.25756  21.53194  1.000 141.34207 ?  80  MET B SD  1 
ATOM 2604 C CE  . MET B 1 80  ? 1.41200   -0.73092  21.95770  1.000 127.32535 ?  80  MET B CE  1 
ATOM 2605 N N   . LEU B 1 81  ? -3.18347  3.15946   20.72304  1.000 100.51459 ?  81  LEU B N   1 
ATOM 2606 C CA  . LEU B 1 81  ? -4.46294  3.31970   20.03896  1.000 98.65442  ?  81  LEU B CA  1 
ATOM 2607 C C   . LEU B 1 81  ? -4.38684  4.39846   18.96763  1.000 101.01872 ?  81  LEU B C   1 
ATOM 2608 O O   . LEU B 1 81  ? -4.89987  4.21431   17.86135  1.000 104.29693 ?  81  LEU B O   1 
ATOM 2609 C CB  . LEU B 1 81  ? -5.56941  3.64862   21.03872  1.000 84.58015  ?  81  LEU B CB  1 
ATOM 2610 C CG  . LEU B 1 81  ? -6.96283  3.74095   20.41277  1.000 76.85253  ?  81  LEU B CG  1 
ATOM 2611 C CD1 . LEU B 1 81  ? -7.32328  2.44653   19.71258  1.000 88.07834  ?  81  LEU B CD1 1 
ATOM 2612 C CD2 . LEU B 1 81  ? -7.98696  4.08689   21.45467  1.000 82.63833  ?  81  LEU B CD2 1 
ATOM 2613 N N   . ARG B 1 82  ? -3.77441  5.54137   19.28897  1.000 109.52599 ?  82  ARG B N   1 
ATOM 2614 C CA  . ARG B 1 82  ? -3.64873  6.63111   18.32394  1.000 109.20169 ?  82  ARG B CA  1 
ATOM 2615 C C   . ARG B 1 82  ? -2.84712  6.19585   17.10136  1.000 115.89715 ?  82  ARG B C   1 
ATOM 2616 O O   . ARG B 1 82  ? -3.21737  6.50233   15.96133  1.000 114.71244 ?  82  ARG B O   1 
ATOM 2617 C CB  . ARG B 1 82  ? -3.00527  7.84827   18.99365  1.000 117.84581 ?  82  ARG B CB  1 
ATOM 2618 C CG  . ARG B 1 82  ? -3.99588  8.91218   19.47113  1.000 124.53283 ?  82  ARG B CG  1 
ATOM 2619 C CD  . ARG B 1 82  ? -3.78691  9.26248   20.94676  1.000 134.80586 ?  82  ARG B CD  1 
ATOM 2620 N NE  . ARG B 1 82  ? -2.43204  9.71944   21.24056  1.000 141.09235 ?  82  ARG B NE  1 
ATOM 2621 C CZ  . ARG B 1 82  ? -1.94422  9.88260   22.46409  1.000 135.72670 ?  82  ARG B CZ  1 
ATOM 2622 N NH1 . ARG B 1 82  ? -2.67710  9.64147   23.53946  1.000 125.77426 ?  82  ARG B NH1 1 
ATOM 2623 N NH2 . ARG B 1 82  ? -0.68853  10.29515  22.61248  1.000 143.11743 ?  82  ARG B NH2 1 
ATOM 2624 N N   . HIS B 1 83  ? -1.72237  5.50715   17.32398  1.000 113.20055 ?  83  HIS B N   1 
ATOM 2625 C CA  . HIS B 1 83  ? -0.91009  5.02391   16.20678  1.000 112.66487 ?  83  HIS B CA  1 
ATOM 2626 C C   . HIS B 1 83  ? -1.69829  4.05363   15.32705  1.000 112.70674 ?  83  HIS B C   1 
ATOM 2627 O O   . HIS B 1 83  ? -1.65769  4.14415   14.09159  1.000 118.25046 ?  83  HIS B O   1 
ATOM 2628 C CB  . HIS B 1 83  ? 0.37492   4.36574   16.72430  1.000 98.40814  ?  83  HIS B CB  1 
ATOM 2629 C CG  . HIS B 1 83  ? 1.36004   5.32667   17.31804  1.000 91.02105  ?  83  HIS B CG  1 
ATOM 2630 N ND1 . HIS B 1 83  ? 1.35646   6.67717   17.02923  1.000 84.97707  ?  83  HIS B ND1 1 
ATOM 2631 C CD2 . HIS B 1 83  ? 2.39085   5.13126   18.17376  1.000 78.24834  ?  83  HIS B CD2 1 
ATOM 2632 C CE1 . HIS B 1 83  ? 2.33568   7.26952   17.68527  1.000 75.91238  ?  83  HIS B CE1 1 
ATOM 2633 N NE2 . HIS B 1 83  ? 2.97855   6.35386   18.38990  1.000 94.11355  ?  83  HIS B NE2 1 
ATOM 2634 N N   . LEU B 1 84  ? -2.39550  3.09359   15.94833  1.000 107.09594 ?  84  LEU B N   1 
ATOM 2635 C CA  . LEU B 1 84  ? -3.26423  2.19478   15.18966  1.000 104.07740 ?  84  LEU B CA  1 
ATOM 2636 C C   . LEU B 1 84  ? -4.31313  2.97550   14.40581  1.000 94.24024  ?  84  LEU B C   1 
ATOM 2637 O O   . LEU B 1 84  ? -4.59779  2.65854   13.24502  1.000 102.57680 ?  84  LEU B O   1 
ATOM 2638 C CB  . LEU B 1 84  ? -3.93472  1.18888   16.12771  1.000 89.43242  ?  84  LEU B CB  1 
ATOM 2639 C CG  . LEU B 1 84  ? -4.85239  0.14673   15.47898  1.000 71.85190  ?  84  LEU B CG  1 
ATOM 2640 C CD1 . LEU B 1 84  ? -4.07363  -0.76331  14.54340  1.000 84.00679  ?  84  LEU B CD1 1 
ATOM 2641 C CD2 . LEU B 1 84  ? -5.57105  -0.67001  16.52707  1.000 90.07798  ?  84  LEU B CD2 1 
ATOM 2642 N N   . LYS B 1 85  ? -4.91731  3.98084   15.03991  1.000 88.99398  ?  85  LYS B N   1 
ATOM 2643 C CA  . LYS B 1 85  ? -5.86900  4.85009   14.36242  1.000 97.82966  ?  85  LYS B CA  1 
ATOM 2644 C C   . LYS B 1 85  ? -5.26217  5.44409   13.10217  1.000 108.64657 ?  85  LYS B C   1 
ATOM 2645 O O   . LYS B 1 85  ? -5.86097  5.38698   12.02638  1.000 116.42064 ?  85  LYS B O   1 
ATOM 2646 C CB  . LYS B 1 85  ? -6.32609  5.96517   15.30367  1.000 84.63230  ?  85  LYS B CB  1 
ATOM 2647 C CG  . LYS B 1 85  ? -6.90596  7.16630   14.56714  1.000 98.78236  ?  85  LYS B CG  1 
ATOM 2648 C CD  . LYS B 1 85  ? -6.83294  8.44044   15.39797  1.000 105.17747 ?  85  LYS B CD  1 
ATOM 2649 C CE  . LYS B 1 85  ? -7.12545  9.67408   14.54834  1.000 104.54151 ?  85  LYS B CE  1 
ATOM 2650 N NZ  . LYS B 1 85  ? -7.22403  10.92402  15.35788  1.000 112.13364 ?  85  LYS B NZ  1 
ATOM 2651 N N   . ASP B 1 86  ? -4.08265  6.05364   13.23328  1.000 112.25410 ?  86  ASP B N   1 
ATOM 2652 C CA  . ASP B 1 86  ? -3.43891  6.71159   12.09752  1.000 110.98307 ?  86  ASP B CA  1 
ATOM 2653 C C   . ASP B 1 86  ? -3.13640  5.72233   10.97468  1.000 107.25865 ?  86  ASP B C   1 
ATOM 2654 O O   . ASP B 1 86  ? -3.37430  6.00888   9.79047   1.000 100.56503 ?  86  ASP B O   1 
ATOM 2655 C CB  . ASP B 1 86  ? -2.16186  7.40759   12.56231  1.000 106.95421 ?  86  ASP B CB  1 
ATOM 2656 C CG  . ASP B 1 86  ? -2.40947  8.41837   13.65861  1.000 109.39111 ?  86  ASP B CG  1 
ATOM 2657 O OD1 . ASP B 1 86  ? -3.56850  8.85572   13.81412  1.000 117.11541 ?  86  ASP B OD1 1 
ATOM 2658 O OD2 . ASP B 1 86  ? -1.43885  8.78867   14.35211  1.000 108.53744 -1 86  ASP B OD2 1 
ATOM 2659 N N   . ALA B 1 87  ? -2.58937  4.55690   11.32971  1.000 108.60182 ?  87  ALA B N   1 
ATOM 2660 C CA  . ALA B 1 87  ? -2.34354  3.51934   10.33372  1.000 100.93859 ?  87  ALA B CA  1 
ATOM 2661 C C   . ALA B 1 87  ? -3.62983  3.16090   9.59942   1.000 95.23744  ?  87  ALA B C   1 
ATOM 2662 O O   . ALA B 1 87  ? -3.65588  3.07060   8.36596   1.000 105.25041 ?  87  ALA B O   1 
ATOM 2663 C CB  . ALA B 1 87  ? -1.73513  2.28523   11.00139  1.000 95.88493  ?  87  ALA B CB  1 
ATOM 2664 N N   . LEU B 1 88  ? -4.71639  2.97776   10.34625  1.000 83.80712  ?  88  LEU B N   1 
ATOM 2665 C CA  . LEU B 1 88  ? -5.99792  2.64170   9.74559   1.000 89.62176  ?  88  LEU B CA  1 
ATOM 2666 C C   . LEU B 1 88  ? -6.57065  3.78812   8.92394   1.000 97.62053  ?  88  LEU B C   1 
ATOM 2667 O O   . LEU B 1 88  ? -7.37252  3.54520   8.01577   1.000 109.87479 ?  88  LEU B O   1 
ATOM 2668 C CB  . LEU B 1 88  ? -6.98121  2.24465   10.84881  1.000 102.97631 ?  88  LEU B CB  1 
ATOM 2669 C CG  . LEU B 1 88  ? -6.72734  0.87449   11.48164  1.000 99.51556  ?  88  LEU B CG  1 
ATOM 2670 C CD1 . LEU B 1 88  ? -7.74523  0.56200   12.58962  1.000 79.91159  ?  88  LEU B CD1 1 
ATOM 2671 C CD2 . LEU B 1 88  ? -6.71687  -0.20146  10.40111  1.000 90.61427  ?  88  LEU B CD2 1 
ATOM 2672 N N   . MET B 1 89  ? -6.18565  5.02656   9.22390   1.000 85.15478  ?  89  MET B N   1 
ATOM 2673 C CA  . MET B 1 89  ? -6.64107  6.15967   8.42938   1.000 100.70274 ?  89  MET B CA  1 
ATOM 2674 C C   . MET B 1 89  ? -5.83480  6.31842   7.15208   1.000 105.07813 ?  89  MET B C   1 
ATOM 2675 O O   . MET B 1 89  ? -6.29956  6.97481   6.21295   1.000 104.24591 ?  89  MET B O   1 
ATOM 2676 C CB  . MET B 1 89  ? -6.56597  7.45799   9.23758   1.000 113.18881 ?  89  MET B CB  1 
ATOM 2677 C CG  . MET B 1 89  ? -7.47649  7.50545   10.45520  1.000 114.68552 ?  89  MET B CG  1 
ATOM 2678 S SD  . MET B 1 89  ? -9.21279  7.78068   10.07437  1.000 125.72497 ?  89  MET B SD  1 
ATOM 2679 C CE  . MET B 1 89  ? -9.93904  6.27363   10.73697  1.000 109.31869 ?  89  MET B CE  1 
ATOM 2680 N N   . ILE B 1 90  ? -4.64472  5.72972   7.10009   1.000 107.05328 ?  90  ILE B N   1 
ATOM 2681 C CA  . ILE B 1 90  ? -3.88396  5.70466   5.85265   1.000 95.27624  ?  90  ILE B CA  1 
ATOM 2682 C C   . ILE B 1 90  ? -4.30993  4.53164   4.98547   1.000 100.64862 ?  90  ILE B C   1 
ATOM 2683 O O   . ILE B 1 90  ? -4.43396  4.66404   3.76425   1.000 102.59531 ?  90  ILE B O   1 
ATOM 2684 C CB  . ILE B 1 90  ? -2.37245  5.65073   6.14203   1.000 94.16829  ?  90  ILE B CB  1 
ATOM 2685 C CG1 . ILE B 1 90  ? -1.90446  6.94666   6.79374   1.000 104.96659 ?  90  ILE B CG1 1 
ATOM 2686 C CG2 . ILE B 1 90  ? -1.58206  5.37091   4.85857   1.000 85.86613  ?  90  ILE B CG2 1 
ATOM 2687 C CD1 . ILE B 1 90  ? -0.52020  6.83730   7.36740   1.000 97.99344  ?  90  ILE B CD1 1 
ATOM 2688 N N   . ILE B 1 91  ? -4.55997  3.37990   5.60449   1.000 88.85122  ?  91  ILE B N   1 
ATOM 2689 C CA  . ILE B 1 91  ? -4.82330  2.17288   4.83169   1.000 99.64852  ?  91  ILE B CA  1 
ATOM 2690 C C   . ILE B 1 91  ? -6.22535  2.19512   4.23681   1.000 103.41286 ?  91  ILE B C   1 
ATOM 2691 O O   . ILE B 1 91  ? -6.40526  1.97659   3.03298   1.000 102.02510 ?  91  ILE B O   1 
ATOM 2692 C CB  . ILE B 1 91  ? -4.59371  0.92219   5.69909   1.000 87.78621  ?  91  ILE B CB  1 
ATOM 2693 C CG1 . ILE B 1 91  ? -3.09331  0.72002   5.94649   1.000 97.60073  ?  91  ILE B CG1 1 
ATOM 2694 C CG2 . ILE B 1 91  ? -5.22483  -0.29852  5.05208   1.000 99.13689  ?  91  ILE B CG2 1 
ATOM 2695 C CD1 . ILE B 1 91  ? -2.76359  -0.40754  6.89116   1.000 82.16116  ?  91  ILE B CD1 1 
ATOM 2696 N N   . TYR B 1 92  ? -7.23666  2.47698   5.05454   1.000 97.86406  ?  92  TYR B N   1 
ATOM 2697 C CA  . TYR B 1 92  ? -8.62066  2.39443   4.61020   1.000 110.75433 ?  92  TYR B CA  1 
ATOM 2698 C C   . TYR B 1 92  ? -9.22462  3.75928   4.29325   1.000 114.74238 ?  92  TYR B C   1 
ATOM 2699 O O   . TYR B 1 92  ? -10.41299 3.83855   3.95733   1.000 93.42017  ?  92  TYR B O   1 
ATOM 2700 C CB  . TYR B 1 92  ? -9.45717  1.69370   5.68205   1.000 104.53679 ?  92  TYR B CB  1 
ATOM 2701 C CG  . TYR B 1 92  ? -9.12972  0.22566   5.83703   1.000 97.20441  ?  92  TYR B CG  1 
ATOM 2702 C CD1 . TYR B 1 92  ? -9.72571  -0.73884  5.04235   1.000 100.25506 ?  92  TYR B CD1 1 
ATOM 2703 C CD2 . TYR B 1 92  ? -8.21303  -0.18973  6.78825   1.000 104.61993 ?  92  TYR B CD2 1 
ATOM 2704 C CE1 . TYR B 1 92  ? -9.41332  -2.07737  5.19869   1.000 107.75240 ?  92  TYR B CE1 1 
ATOM 2705 C CE2 . TYR B 1 92  ? -7.89701  -1.51809  6.94772   1.000 98.47703  ?  92  TYR B CE2 1 
ATOM 2706 C CZ  . TYR B 1 92  ? -8.49648  -2.45738  6.15550   1.000 87.81956  ?  92  TYR B CZ  1 
ATOM 2707 O OH  . TYR B 1 92  ? -8.17279  -3.78156  6.33020   1.000 98.79038  ?  92  TYR B OH  1 
ATOM 2708 N N   . GLY B 1 93  ? -8.42431  4.82149   4.33923   1.000 118.38254 ?  93  GLY B N   1 
ATOM 2709 C CA  . GLY B 1 93  ? -8.90875  6.17023   4.09510   1.000 113.29088 ?  93  GLY B CA  1 
ATOM 2710 C C   . GLY B 1 93  ? -9.22977  6.96477   5.35306   1.000 106.83435 ?  93  GLY B C   1 
ATOM 2711 O O   . GLY B 1 93  ? -9.82245  6.45238   6.30627   1.000 83.97694  ?  93  GLY B O   1 
ATOM 2712 N N   . ARG B 1 103 ? -23.80670 4.40574   17.34816  1.000 113.54059 ?  103 ARG B N   1 
ATOM 2713 C CA  . ARG B 1 103 ? -24.70400 4.81704   18.42032  1.000 129.14262 ?  103 ARG B CA  1 
ATOM 2714 C C   . ARG B 1 103 ? -25.31582 3.62016   19.13379  1.000 126.45428 ?  103 ARG B C   1 
ATOM 2715 O O   . ARG B 1 103 ? -26.01083 3.77323   20.13666  1.000 133.89314 ?  103 ARG B O   1 
ATOM 2716 C CB  . ARG B 1 103 ? -25.82527 5.70570   17.85616  1.000 123.56859 ?  103 ARG B CB  1 
ATOM 2717 C CG  . ARG B 1 103 ? -25.34373 6.95231   17.12408  1.000 107.46504 ?  103 ARG B CG  1 
ATOM 2718 C CD  . ARG B 1 103 ? -24.58947 7.85344   18.09384  1.000 111.29860 ?  103 ARG B CD  1 
ATOM 2719 N NE  . ARG B 1 103 ? -24.04159 9.05367   17.47243  1.000 109.97163 ?  103 ARG B NE  1 
ATOM 2720 C CZ  . ARG B 1 103 ? -24.63600 10.23973  17.47267  1.000 101.54614 ?  103 ARG B CZ  1 
ATOM 2721 N NH1 . ARG B 1 103 ? -25.82902 10.41400  18.01425  1.000 110.82650 ?  103 ARG B NH1 1 
ATOM 2722 N NH2 . ARG B 1 103 ? -24.01478 11.27899  16.92057  1.000 88.22716  ?  103 ARG B NH2 1 
ATOM 2723 N N   . SER B 1 104 ? -25.02433 2.42495   18.63639  1.000 141.92280 ?  104 SER B N   1 
ATOM 2724 C CA  . SER B 1 104 ? -25.61403 1.20223   19.15452  1.000 142.56725 ?  104 SER B CA  1 
ATOM 2725 C C   . SER B 1 104 ? -24.52683 0.29041   19.70273  1.000 145.34627 ?  104 SER B C   1 
ATOM 2726 O O   . SER B 1 104 ? -23.39427 0.28242   19.20966  1.000 146.97310 ?  104 SER B O   1 
ATOM 2727 C CB  . SER B 1 104 ? -26.41811 0.47469   18.07291  1.000 143.63459 ?  104 SER B CB  1 
ATOM 2728 O OG  . SER B 1 104 ? -25.58211 0.08379   16.99991  1.000 140.24457 ?  104 SER B OG  1 
ATOM 2729 N N   . MET B 1 105 ? -24.88147 -0.46715  20.74437  1.000 144.17859 ?  105 MET B N   1 
ATOM 2730 C CA  . MET B 1 105 ? -23.93963 -1.40962  21.34057  1.000 129.95552 ?  105 MET B CA  1 
ATOM 2731 C C   . MET B 1 105 ? -23.40650 -2.39997  20.31274  1.000 129.04980 ?  105 MET B C   1 
ATOM 2732 O O   . MET B 1 105 ? -22.26304 -2.85317  20.42724  1.000 127.94638 ?  105 MET B O   1 
ATOM 2733 C CB  . MET B 1 105 ? -24.60297 -2.14786  22.50067  1.000 129.29528 ?  105 MET B CB  1 
ATOM 2734 C CG  . MET B 1 105 ? -23.65777 -3.00352  23.31713  1.000 129.05599 ?  105 MET B CG  1 
ATOM 2735 S SD  . MET B 1 105 ? -24.54534 -4.22015  24.30658  1.000 146.66939 ?  105 MET B SD  1 
ATOM 2736 C CE  . MET B 1 105 ? -23.19298 -5.09586  25.07407  1.000 127.84617 ?  105 MET B CE  1 
ATOM 2737 N N   . SER B 1 106 ? -24.22201 -2.74858  19.31098  1.000 127.51033 ?  106 SER B N   1 
ATOM 2738 C CA  . SER B 1 106 ? -23.81389 -3.70006  18.27849  1.000 110.13733 ?  106 SER B CA  1 
ATOM 2739 C C   . SER B 1 106 ? -22.54107 -3.27453  17.55918  1.000 110.35846 ?  106 SER B C   1 
ATOM 2740 O O   . SER B 1 106 ? -21.79448 -4.13090  17.07071  1.000 118.74383 ?  106 SER B O   1 
ATOM 2741 C CB  . SER B 1 106 ? -24.93422 -3.87305  17.25991  1.000 119.59491 ?  106 SER B CB  1 
ATOM 2742 O OG  . SER B 1 106 ? -25.04006 -2.70918  16.46045  1.000 135.17770 ?  106 SER B OG  1 
ATOM 2743 N N   . ARG B 1 107 ? -22.29528 -1.97100  17.43868  1.000 112.70829 ?  107 ARG B N   1 
ATOM 2744 C CA  . ARG B 1 107 ? -21.07013 -1.47483  16.82643  1.000 117.00045 ?  107 ARG B CA  1 
ATOM 2745 C C   . ARG B 1 107 ? -20.04765 -1.00428  17.85245  1.000 106.60167 ?  107 ARG B C   1 
ATOM 2746 O O   . ARG B 1 107 ? -19.06851 -0.34873  17.48447  1.000 109.23242 ?  107 ARG B O   1 
ATOM 2747 C CB  . ARG B 1 107 ? -21.38485 -0.36716  15.81982  1.000 129.21676 ?  107 ARG B CB  1 
ATOM 2748 C CG  . ARG B 1 107 ? -22.00971 -0.91793  14.54371  1.000 126.91692 ?  107 ARG B CG  1 
ATOM 2749 C CD  . ARG B 1 107 ? -22.24936 0.14191   13.48412  1.000 122.48059 ?  107 ARG B CD  1 
ATOM 2750 N NE  . ARG B 1 107 ? -23.34108 1.03955   13.83593  1.000 144.41337 ?  107 ARG B NE  1 
ATOM 2751 C CZ  . ARG B 1 107 ? -23.72025 2.07897   13.10468  1.000 149.66205 ?  107 ARG B CZ  1 
ATOM 2752 N NH1 . ARG B 1 107 ? -23.19183 2.31726   11.91449  1.000 134.38752 ?  107 ARG B NH1 1 
ATOM 2753 N NH2 . ARG B 1 107 ? -24.67754 2.88047   13.56419  1.000 152.71703 ?  107 ARG B NH2 1 
ATOM 2754 N N   . LYS B 1 108 ? -20.26078 -1.31295  19.12923  1.000 103.21773 ?  108 LYS B N   1 
ATOM 2755 C CA  . LYS B 1 108 ? -19.28053 -1.04996  20.17078  1.000 95.96152  ?  108 LYS B CA  1 
ATOM 2756 C C   . LYS B 1 108 ? -18.70257 -2.31500  20.78720  1.000 90.53834  ?  108 LYS B C   1 
ATOM 2757 O O   . LYS B 1 108 ? -17.55633 -2.29797  21.23841  1.000 93.23351  ?  108 LYS B O   1 
ATOM 2758 C CB  . LYS B 1 108 ? -19.89062 -0.17575  21.27183  1.000 89.01184  ?  108 LYS B CB  1 
ATOM 2759 C CG  . LYS B 1 108 ? -20.32781 1.19918   20.78673  1.000 91.73146  ?  108 LYS B CG  1 
ATOM 2760 C CD  . LYS B 1 108 ? -20.68722 2.09504   21.96105  1.000 111.99653 ?  108 LYS B CD  1 
ATOM 2761 C CE  . LYS B 1 108 ? -21.10114 3.49234   21.51873  1.000 107.26450 ?  108 LYS B CE  1 
ATOM 2762 N NZ  . LYS B 1 108 ? -21.38639 4.35768   22.70335  1.000 114.67826 ?  108 LYS B NZ  1 
ATOM 2763 N N   . ILE B 1 109 ? -19.47168 -3.39985  20.82450  1.000 87.28690  ?  109 ILE B N   1 
ATOM 2764 C CA  . ILE B 1 109 ? -19.02252 -4.70633  21.29742  1.000 83.80893  ?  109 ILE B CA  1 
ATOM 2765 C C   . ILE B 1 109 ? -19.20505 -5.67188  20.13548  1.000 94.22247  ?  109 ILE B C   1 
ATOM 2766 O O   . ILE B 1 109 ? -20.34263 -5.96876  19.75064  1.000 105.32464 ?  109 ILE B O   1 
ATOM 2767 C CB  . ILE B 1 109 ? -19.81984 -5.18192  22.52158  1.000 89.96951  ?  109 ILE B CB  1 
ATOM 2768 C CG1 . ILE B 1 109 ? -19.86210 -4.10336  23.60490  1.000 92.64913  ?  109 ILE B CG1 1 
ATOM 2769 C CG2 . ILE B 1 109 ? -19.24888 -6.48359  23.06730  1.000 88.76094  ?  109 ILE B CG2 1 
ATOM 2770 C CD1 . ILE B 1 109 ? -18.51294 -3.65775  24.07341  1.000 94.89411  ?  109 ILE B CD1 1 
ATOM 2771 N N   . MET B 1 110 ? -18.10517 -6.16797  19.56860  1.000 90.73380  ?  110 MET B N   1 
ATOM 2772 C CA  . MET B 1 110 ? -18.21008 -7.01722  18.38369  1.000 98.98133  ?  110 MET B CA  1 
ATOM 2773 C C   . MET B 1 110 ? -17.40516 -8.29800  18.54735  1.000 99.30190  ?  110 MET B C   1 
ATOM 2774 O O   . MET B 1 110 ? -16.21304 -8.24773  18.85511  1.000 105.29186 ?  110 MET B O   1 
ATOM 2775 C CB  . MET B 1 110 ? -17.74943 -6.26513  17.13664  1.000 109.24453 ?  110 MET B CB  1 
ATOM 2776 C CG  . MET B 1 110 ? -18.75419 -5.24375  16.64049  1.000 111.74488 ?  110 MET B CG  1 
ATOM 2777 S SD  . MET B 1 110 ? -17.94975 -3.68897  16.25549  1.000 123.02281 ?  110 MET B SD  1 
ATOM 2778 C CE  . MET B 1 110 ? -17.10829 -3.39767  17.81441  1.000 107.53300 ?  110 MET B CE  1 
ATOM 2779 N N   . THR B 1 111 ? -18.03991 -9.44174  18.30428  1.000 87.93387  ?  111 THR B N   1 
ATOM 2780 C CA  . THR B 1 111 ? -17.38312 -10.72924 18.47837  1.000 95.41347  ?  111 THR B CA  1 
ATOM 2781 C C   . THR B 1 111 ? -17.23211 -11.45178 17.14098  1.000 99.32146  ?  111 THR B C   1 
ATOM 2782 O O   . THR B 1 111 ? -18.07897 -11.33891 16.24924  1.000 93.44369  ?  111 THR B O   1 
ATOM 2783 C CB  . THR B 1 111 ? -18.14177 -11.60786 19.48116  1.000 76.60984  ?  111 THR B CB  1 
ATOM 2784 O OG1 . THR B 1 111 ? -17.42884 -12.83576 19.66789  1.000 111.64144 ?  111 THR B OG1 1 
ATOM 2785 C CG2 . THR B 1 111 ? -19.54209 -11.92000 18.98504  1.000 85.94384  ?  111 THR B CG2 1 
ATOM 2786 N N   . THR B 1 112 ? -16.12870 -12.18995 17.01355  1.000 96.35547  ?  112 THR B N   1 
ATOM 2787 C CA  . THR B 1 112 ? -15.75305 -12.87621 15.78420  1.000 107.65054 ?  112 THR B CA  1 
ATOM 2788 C C   . THR B 1 112 ? -15.11219 -14.22002 16.11580  1.000 100.95526 ?  112 THR B C   1 
ATOM 2789 O O   . THR B 1 112 ? -14.70082 -14.46924 17.24864  1.000 106.37359 ?  112 THR B O   1 
ATOM 2790 C CB  . THR B 1 112 ? -14.78707 -12.02062 14.94726  1.000 105.23311 ?  112 THR B CB  1 
ATOM 2791 O OG1 . THR B 1 112 ? -13.75013 -11.50763 15.79146  1.000 92.51796  ?  112 THR B OG1 1 
ATOM 2792 C CG2 . THR B 1 112 ? -15.51736 -10.85464 14.28233  1.000 114.86246 ?  112 THR B CG2 1 
ATOM 2793 N N   . GLU B 1 113 ? -15.03383 -15.09001 15.10914  1.000 115.42108 ?  113 GLU B N   1 
ATOM 2794 C CA  . GLU B 1 113 ? -14.40259 -16.39767 15.25309  1.000 112.39525 ?  113 GLU B CA  1 
ATOM 2795 C C   . GLU B 1 113 ? -12.93055 -16.31827 14.86734  1.000 106.41176 ?  113 GLU B C   1 
ATOM 2796 O O   . GLU B 1 113 ? -12.57293 -15.71519 13.85216  1.000 115.05005 ?  113 GLU B O   1 
ATOM 2797 C CB  . GLU B 1 113 ? -15.11704 -17.44393 14.39604  1.000 112.04596 ?  113 GLU B CB  1 
ATOM 2798 C CG  . GLU B 1 113 ? -16.62358 -17.49388 14.61853  1.000 133.88657 ?  113 GLU B CG  1 
ATOM 2799 C CD  . GLU B 1 113 ? -17.11985 -18.86507 15.05558  1.000 142.65750 ?  113 GLU B CD  1 
ATOM 2800 O OE1 . GLU B 1 113 ? -16.28359 -19.71940 15.42288  1.000 133.59561 ?  113 GLU B OE1 1 
ATOM 2801 O OE2 . GLU B 1 113 ? -18.35173 -19.08639 15.03201  1.000 144.08461 -1 113 GLU B OE2 1 
ATOM 2802 N N   . VAL B 1 114 ? -12.07961 -16.95185 15.66789  1.000 94.49799  ?  114 VAL B N   1 
ATOM 2803 C CA  . VAL B 1 114 ? -10.63459 -16.83960 15.51514  1.000 104.39423 ?  114 VAL B CA  1 
ATOM 2804 C C   . VAL B 1 114 ? -10.10806 -18.04637 14.75188  1.000 111.18334 ?  114 VAL B C   1 
ATOM 2805 O O   . VAL B 1 114 ? -10.39668 -19.19757 15.10463  1.000 117.86323 ?  114 VAL B O   1 
ATOM 2806 C CB  . VAL B 1 114 ? -9.94791  -16.71059 16.88620  1.000 116.43345 ?  114 VAL B CB  1 
ATOM 2807 C CG1 . VAL B 1 114 ? -10.47427 -17.77035 17.84958  1.000 116.94785 ?  114 VAL B CG1 1 
ATOM 2808 C CG2 . VAL B 1 114 ? -8.44026  -16.81193 16.74371  1.000 118.41560 ?  114 VAL B CG2 1 
ATOM 2809 N N   . ASN B 1 115 ? -9.31296  -17.77903 13.72110  1.000 122.76263 ?  115 ASN B N   1 
ATOM 2810 C CA  . ASN B 1 115 ? -8.71796  -18.80960 12.88600  1.000 127.92822 ?  115 ASN B CA  1 
ATOM 2811 C C   . ASN B 1 115 ? -7.35614  -19.20167 13.43470  1.000 133.60762 ?  115 ASN B C   1 
ATOM 2812 O O   . ASN B 1 115 ? -6.71446  -18.43414 14.15506  1.000 139.80336 ?  115 ASN B O   1 
ATOM 2813 C CB  . ASN B 1 115 ? -8.58300  -18.33105 11.43841  1.000 125.57378 ?  115 ASN B CB  1 
ATOM 2814 C CG  . ASN B 1 115 ? -8.22215  -19.45534 10.48218  1.000 140.77058 ?  115 ASN B CG  1 
ATOM 2815 O OD1 . ASN B 1 115 ? -8.08330  -20.60993 10.88766  1.000 143.81284 ?  115 ASN B OD1 1 
ATOM 2816 N ND2 . ASN B 1 115 ? -8.07019  -19.12210 9.20456   1.000 136.81439 ?  115 ASN B ND2 1 
ATOM 2817 N N   . LYS B 1 116 ? -6.93496  -20.42654 13.10724  1.000 162.43847 ?  116 LYS B N   1 
ATOM 2818 C CA  . LYS B 1 116 ? -5.62996  -20.91003 13.54670  1.000 163.70484 ?  116 LYS B CA  1 
ATOM 2819 C C   . LYS B 1 116 ? -4.50864  -19.94430 13.17139  1.000 169.89223 ?  116 LYS B C   1 
ATOM 2820 O O   . LYS B 1 116 ? -3.57550  -19.73964 13.95219  1.000 166.85506 ?  116 LYS B O   1 
ATOM 2821 C CB  . LYS B 1 116 ? -5.35859  -22.30060 12.96514  1.000 162.71572 ?  116 LYS B CB  1 
ATOM 2822 C CG  . LYS B 1 116 ? -5.36793  -22.38064 11.44279  1.000 165.74498 ?  116 LYS B CG  1 
ATOM 2823 C CD  . LYS B 1 116 ? -4.75927  -23.69621 10.97098  1.000 168.07458 ?  116 LYS B CD  1 
ATOM 2824 C CE  . LYS B 1 116 ? -4.85091  -23.86533 9.45928   1.000 167.87733 ?  116 LYS B CE  1 
ATOM 2825 N NZ  . LYS B 1 116 ? -4.11196  -22.82058 8.70228   1.000 166.45636 ?  116 LYS B NZ  1 
ATOM 2826 N N   . THR B 1 117 ? -4.56923  -19.35835 11.97149  1.000 165.51487 ?  117 THR B N   1 
ATOM 2827 C CA  . THR B 1 117 ? -3.57452  -18.36413 11.56967  1.000 153.91986 ?  117 THR B CA  1 
ATOM 2828 C C   . THR B 1 117 ? -3.66616  -17.10468 12.42982  1.000 148.42810 ?  117 THR B C   1 
ATOM 2829 O O   . THR B 1 117 ? -2.66680  -16.64382 13.01157  1.000 147.62307 ?  117 THR B O   1 
ATOM 2830 C CB  . THR B 1 117 ? -3.77072  -18.01416 10.09179  1.000 135.32830 ?  117 THR B CB  1 
ATOM 2831 O OG1 . THR B 1 117 ? -3.88567  -19.21753 9.31961   1.000 113.57777 ?  117 THR B OG1 1 
ATOM 2832 C CG2 . THR B 1 117 ? -2.59666  -17.19982 9.57865   1.000 128.08543 ?  117 THR B CG2 1 
ATOM 2833 N N   . LEU B 1 118 ? -4.87207  -16.54326 12.53204  1.000 144.06784 ?  118 LEU B N   1 
ATOM 2834 C CA  . LEU B 1 118 ? -5.06857  -15.37078 13.37087  1.000 138.84253 ?  118 LEU B CA  1 
ATOM 2835 C C   . LEU B 1 118 ? -4.75989  -15.68401 14.82765  1.000 138.09135 ?  118 LEU B C   1 
ATOM 2836 O O   . LEU B 1 118 ? -4.21873  -14.84092 15.54811  1.000 146.03679 ?  118 LEU B O   1 
ATOM 2837 C CB  . LEU B 1 118 ? -6.50345  -14.86258 13.21318  1.000 135.69034 ?  118 LEU B CB  1 
ATOM 2838 C CG  . LEU B 1 118 ? -7.10407  -14.92683 11.79965  1.000 127.43571 ?  118 LEU B CG  1 
ATOM 2839 C CD1 . LEU B 1 118 ? -8.58047  -14.55431 11.81440  1.000 119.78561 ?  118 LEU B CD1 1 
ATOM 2840 C CD2 . LEU B 1 118 ? -6.34332  -14.04777 10.81751  1.000 121.23150 ?  118 LEU B CD2 1 
ATOM 2841 N N   . LEU B 1 119 ? -5.06594  -16.90377 15.27505  1.000 168.02277 ?  119 LEU B N   1 
ATOM 2842 C CA  . LEU B 1 119 ? -4.70769  -17.29016 16.63659  1.000 176.09259 ?  119 LEU B CA  1 
ATOM 2843 C C   . LEU B 1 119 ? -3.19563  -17.38251 16.81192  1.000 172.42466 ?  119 LEU B C   1 
ATOM 2844 O O   . LEU B 1 119 ? -2.66354  -17.00420 17.86282  1.000 169.94338 ?  119 LEU B O   1 
ATOM 2845 C CB  . LEU B 1 119 ? -5.38239  -18.60951 17.00688  1.000 179.11865 ?  119 LEU B CB  1 
ATOM 2846 C CG  . LEU B 1 119 ? -4.90863  -19.27564 18.29464  1.000 178.48756 ?  119 LEU B CG  1 
ATOM 2847 C CD1 . LEU B 1 119 ? -5.17775  -18.36598 19.48474  1.000 171.51263 ?  119 LEU B CD1 1 
ATOM 2848 C CD2 . LEU B 1 119 ? -5.64062  -20.58072 18.46764  1.000 170.27228 ?  119 LEU B CD2 1 
ATOM 2849 N N   . ASP B 1 120 ? -2.49080  -17.90133 15.80198  1.000 148.94644 ?  120 ASP B N   1 
ATOM 2850 C CA  . ASP B 1 120 ? -1.03493  -17.96421 15.86471  1.000 147.10437 ?  120 ASP B CA  1 
ATOM 2851 C C   . ASP B 1 120 ? -0.45005  -16.57610 16.05695  1.000 142.84562 ?  120 ASP B C   1 
ATOM 2852 O O   . ASP B 1 120 ? 0.48227   -16.38840 16.84798  1.000 140.02352 ?  120 ASP B O   1 
ATOM 2853 C CB  . ASP B 1 120 ? -0.47365  -18.62382 14.60547  1.000 144.91595 ?  120 ASP B CB  1 
ATOM 2854 C CG  . ASP B 1 120 ? 0.95879   -19.09919 14.78644  1.000 139.82636 ?  120 ASP B CG  1 
ATOM 2855 O OD1 . ASP B 1 120 ? 1.17396   -20.06658 15.54802  1.000 139.56584 -1 120 ASP B OD1 1 
ATOM 2856 O OD2 . ASP B 1 120 ? 1.86998   -18.51051 14.16752  1.000 137.62639 ?  120 ASP B OD2 1 
ATOM 2857 N N   . GLU B 1 121 ? -0.98591  -15.58882 15.33639  1.000 143.19937 ?  121 GLU B N   1 
ATOM 2858 C CA  . GLU B 1 121 ? -0.57816  -14.20879 15.60232  1.000 144.46168 ?  121 GLU B CA  1 
ATOM 2859 C C   . GLU B 1 121 ? -0.99158  -13.76924 17.00338  1.000 138.99074 ?  121 GLU B C   1 
ATOM 2860 O O   . GLU B 1 121 ? -0.24721  -13.04987 17.68108  1.000 138.62697 ?  121 GLU B O   1 
ATOM 2861 C CB  . GLU B 1 121 ? -1.15087  -13.26000 14.54898  1.000 153.54384 ?  121 GLU B CB  1 
ATOM 2862 C CG  . GLU B 1 121 ? -0.17635  -12.90721 13.43165  1.000 146.23322 ?  121 GLU B CG  1 
ATOM 2863 C CD  . GLU B 1 121 ? 1.21145   -12.56399 13.95683  1.000 127.51812 ?  121 GLU B CD  1 
ATOM 2864 O OE1 . GLU B 1 121 ? 1.35220   -11.52298 14.63254  1.000 128.06099 ?  121 GLU B OE1 1 
ATOM 2865 O OE2 . GLU B 1 121 ? 2.16305   -13.32399 13.68087  1.000 129.23033 -1 121 GLU B OE2 1 
ATOM 2866 N N   . LEU B 1 122 ? -2.17308  -14.19705 17.45610  1.000 139.00134 ?  122 LEU B N   1 
ATOM 2867 C CA  . LEU B 1 122 ? -2.63639  -13.86567 18.79922  1.000 141.44197 ?  122 LEU B CA  1 
ATOM 2868 C C   . LEU B 1 122 ? -1.71637  -14.41657 19.88120  1.000 129.36981 ?  122 LEU B C   1 
ATOM 2869 O O   . LEU B 1 122 ? -1.70422  -13.88843 20.99790  1.000 118.79180 ?  122 LEU B O   1 
ATOM 2870 C CB  . LEU B 1 122 ? -4.05685  -14.40092 19.00446  1.000 149.66175 ?  122 LEU B CB  1 
ATOM 2871 C CG  . LEU B 1 122 ? -5.24329  -13.52567 18.58871  1.000 137.92926 ?  122 LEU B CG  1 
ATOM 2872 C CD1 . LEU B 1 122 ? -6.54850  -14.27313 18.82338  1.000 128.44617 ?  122 LEU B CD1 1 
ATOM 2873 C CD2 . LEU B 1 122 ? -5.24319  -12.19146 19.33238  1.000 110.66897 ?  122 LEU B CD2 1 
ATOM 2874 N N   . LYS B 1 123 ? -0.92458  -15.44039 19.56857  1.000 128.09628 ?  123 LYS B N   1 
ATOM 2875 C CA  . LYS B 1 123 ? 0.08713   -15.92117 20.49875  1.000 133.07567 ?  123 LYS B CA  1 
ATOM 2876 C C   . LYS B 1 123 ? 1.43336   -15.24964 20.29254  1.000 133.35288 ?  123 LYS B C   1 
ATOM 2877 O O   . LYS B 1 123 ? 2.23287   -15.19207 21.23503  1.000 126.67140 ?  123 LYS B O   1 
ATOM 2878 C CB  . LYS B 1 123 ? 0.28071   -17.43392 20.35266  1.000 132.40808 ?  123 LYS B CB  1 
ATOM 2879 C CG  . LYS B 1 123 ? -0.97920  -18.26871 20.47437  1.000 130.19531 ?  123 LYS B CG  1 
ATOM 2880 C CD  . LYS B 1 123 ? -1.06378  -19.27701 19.33590  1.000 131.74031 ?  123 LYS B CD  1 
ATOM 2881 C CE  . LYS B 1 123 ? 0.31468   -19.75631 18.90729  1.000 122.74249 ?  123 LYS B CE  1 
ATOM 2882 N NZ  . LYS B 1 123 ? 0.24648   -20.65818 17.72777  1.000 132.23346 ?  123 LYS B NZ  1 
ATOM 2883 N N   . ASN B 1 124 ? 1.69240   -14.73623 19.09228  1.000 134.39870 ?  124 ASN B N   1 
ATOM 2884 C CA  . ASN B 1 124 ? 2.91259   -13.98861 18.79041  1.000 124.60552 ?  124 ASN B CA  1 
ATOM 2885 C C   . ASN B 1 124 ? 2.75824   -12.51099 19.13702  1.000 115.74508 ?  124 ASN B C   1 
ATOM 2886 O O   . ASN B 1 124 ? 3.09849   -11.62289 18.35808  1.000 108.46003 ?  124 ASN B O   1 
ATOM 2887 C CB  . ASN B 1 124 ? 3.29085   -14.17801 17.32658  1.000 123.09103 ?  124 ASN B CB  1 
ATOM 2888 C CG  . ASN B 1 124 ? 3.67283   -15.61496 17.00335  1.000 137.51349 ?  124 ASN B CG  1 
ATOM 2889 O OD1 . ASN B 1 124 ? 4.01412   -16.39630 17.89462  1.000 124.87101 ?  124 ASN B OD1 1 
ATOM 2890 N ND2 . ASN B 1 124 ? 3.61978   -15.96839 15.72289  1.000 139.97651 ?  124 ASN B ND2 1 
ATOM 2891 N N   . ILE B 1 125 ? 2.23545   -12.25200 20.33094  1.000 116.97930 ?  125 ILE B N   1 
ATOM 2892 C CA  . ILE B 1 125 ? 2.05505   -10.90665 20.85612  1.000 106.19479 ?  125 ILE B CA  1 
ATOM 2893 C C   . ILE B 1 125 ? 3.10894   -10.65537 21.92347  1.000 115.51114 ?  125 ILE B C   1 
ATOM 2894 O O   . ILE B 1 125 ? 3.55778   -11.58070 22.61458  1.000 112.21768 ?  125 ILE B O   1 
ATOM 2895 C CB  . ILE B 1 125 ? 0.62727   -10.73339 21.41298  1.000 104.43898 ?  125 ILE B CB  1 
ATOM 2896 C CG1 . ILE B 1 125 ? 0.28180   -11.87976 22.37589  1.000 108.03877 ?  125 ILE B CG1 1 
ATOM 2897 C CG2 . ILE B 1 125 ? -0.37343  -10.68868 20.27162  1.000 92.76455  ?  125 ILE B CG2 1 
ATOM 2898 C CD1 . ILE B 1 125 ? 0.61921   -11.62598 23.84371  1.000 97.06553  ?  125 ILE B CD1 1 
ATOM 2899 N N   . ASN B 1 126 ? 3.51321   -9.39401  22.06723  1.000 107.04403 ?  126 ASN B N   1 
ATOM 2900 C CA  . ASN B 1 126 ? 4.48951   -9.03985  23.08950  1.000 116.46041 ?  126 ASN B CA  1 
ATOM 2901 C C   . ASN B 1 126 ? 4.33709   -7.57780  23.47676  1.000 121.26353 ?  126 ASN B C   1 
ATOM 2902 O O   . ASN B 1 126 ? 4.21619   -6.71011  22.60677  1.000 124.07053 ?  126 ASN B O   1 
ATOM 2903 C CB  . ASN B 1 126 ? 5.91726   -9.31313  22.60365  1.000 125.94100 ?  126 ASN B CB  1 
ATOM 2904 C CG  . ASN B 1 126 ? 6.94037   -8.40535  23.25789  1.000 131.29391 ?  126 ASN B CG  1 
ATOM 2905 O OD1 . ASN B 1 126 ? 7.59130   -7.60608  22.58621  1.000 141.62965 ?  126 ASN B OD1 1 
ATOM 2906 N ND2 . ASN B 1 126 ? 7.08178   -8.51750  24.57468  1.000 134.12841 ?  126 ASN B ND2 1 
ATOM 2907 N N   . SER B 1 127 ? 4.32295   -7.32392  24.78732  1.000 123.52180 ?  127 SER B N   1 
ATOM 2908 C CA  . SER B 1 127 ? 4.22027   -5.98424  25.36954  1.000 126.63546 ?  127 SER B CA  1 
ATOM 2909 C C   . SER B 1 127 ? 5.53322   -5.20320  25.37377  1.000 121.00655 ?  127 SER B C   1 
ATOM 2910 O O   . SER B 1 127 ? 5.83214   -4.51636  26.35390  1.000 108.20360 ?  127 SER B O   1 
ATOM 2911 C CB  . SER B 1 127 ? 3.65772   -6.09612  26.78497  1.000 120.65835 ?  127 SER B CB  1 
ATOM 2912 O OG  . SER B 1 127 ? 2.31678   -6.55234  26.76394  1.000 122.63019 ?  127 SER B OG  1 
ATOM 2913 N N   . HIS B 1 128 ? 6.33850   -5.28907  24.31562  1.000 139.09512 ?  128 HIS B N   1 
ATOM 2914 C CA  . HIS B 1 128 ? 7.54619   -4.47169  24.21995  1.000 153.09101 ?  128 HIS B CA  1 
ATOM 2915 C C   . HIS B 1 128 ? 7.65443   -3.82929  22.84143  1.000 157.23835 ?  128 HIS B C   1 
ATOM 2916 O O   . HIS B 1 128 ? 7.75400   -2.60234  22.72448  1.000 155.99392 ?  128 HIS B O   1 
ATOM 2917 C CB  . HIS B 1 128 ? 8.79758   -5.30626  24.52164  1.000 157.31881 ?  128 HIS B CB  1 
ATOM 2918 C CG  . HIS B 1 128 ? 10.08614  -4.63026  24.15252  1.000 161.54487 ?  128 HIS B CG  1 
ATOM 2919 N ND1 . HIS B 1 128 ? 10.35826  -3.31529  24.46517  1.000 161.70646 ?  128 HIS B ND1 1 
ATOM 2920 C CD2 . HIS B 1 128 ? 11.17930  -5.09505  23.50095  1.000 160.18180 ?  128 HIS B CD2 1 
ATOM 2921 C CE1 . HIS B 1 128 ? 11.56150  -2.99801  24.01921  1.000 158.93468 ?  128 HIS B CE1 1 
ATOM 2922 N NE2 . HIS B 1 128 ? 12.08066  -4.06001  23.43071  1.000 160.68752 ?  128 HIS B NE2 1 
ATOM 2923 N N   . ASP B 1 129 ? 7.63608   -4.65306  21.79214  1.000 157.91691 ?  129 ASP B N   1 
ATOM 2924 C CA  . ASP B 1 129 ? 7.71054   -4.16739  20.41547  1.000 141.96852 ?  129 ASP B CA  1 
ATOM 2925 C C   . ASP B 1 129 ? 6.32384   -3.67560  20.01254  1.000 131.02556 ?  129 ASP B C   1 
ATOM 2926 O O   . ASP B 1 129 ? 5.51537   -4.39560  19.42135  1.000 132.70011 ?  129 ASP B O   1 
ATOM 2927 C CB  . ASP B 1 129 ? 8.22276   -5.26119  19.48522  1.000 135.05095 ?  129 ASP B CB  1 
ATOM 2928 C CG  . ASP B 1 129 ? 8.70126   -4.71749  18.15433  1.000 141.64702 ?  129 ASP B CG  1 
ATOM 2929 O OD1 . ASP B 1 129 ? 7.98410   -3.89151  17.55324  1.000 137.84549 ?  129 ASP B OD1 1 
ATOM 2930 O OD2 . ASP B 1 129 ? 9.80246   -5.11031  17.71367  1.000 155.67783 -1 129 ASP B OD2 1 
ATOM 2931 N N   . ASN B 1 130 ? 6.04642   -2.41560  20.36128  1.000 124.28274 ?  130 ASN B N   1 
ATOM 2932 C CA  . ASN B 1 130 ? 4.78059   -1.79696  19.97758  1.000 119.23401 ?  130 ASN B CA  1 
ATOM 2933 C C   . ASN B 1 130 ? 4.60039   -1.81723  18.46780  1.000 119.11611 ?  130 ASN B C   1 
ATOM 2934 O O   . ASN B 1 130 ? 3.48229   -1.98562  17.96699  1.000 112.53518 ?  130 ASN B O   1 
ATOM 2935 C CB  . ASN B 1 130 ? 4.72393   -0.36080  20.49245  1.000 106.07275 ?  130 ASN B CB  1 
ATOM 2936 C CG  . ASN B 1 130 ? 5.06160   -0.26113  21.95703  1.000 110.84765 ?  130 ASN B CG  1 
ATOM 2937 O OD1 . ASN B 1 130 ? 4.73243   -1.14940  22.74228  1.000 103.14059 ?  130 ASN B OD1 1 
ATOM 2938 N ND2 . ASN B 1 130 ? 5.73774   0.81642   22.33489  1.000 108.73377 ?  130 ASN B ND2 1 
ATOM 2939 N N   . SER B 1 131 ? 5.69284   -1.60855  17.73195  1.000 125.86294 ?  131 SER B N   1 
ATOM 2940 C CA  . SER B 1 131 ? 5.67797   -1.72881  16.27987  1.000 105.17108 ?  131 SER B CA  1 
ATOM 2941 C C   . SER B 1 131 ? 5.10595   -3.07221  15.83474  1.000 100.29799 ?  131 SER B C   1 
ATOM 2942 O O   . SER B 1 131 ? 4.18936   -3.12772  15.00586  1.000 111.28191 ?  131 SER B O   1 
ATOM 2943 C CB  . SER B 1 131 ? 7.09653   -1.53044  15.74613  1.000 109.22427 ?  131 SER B CB  1 
ATOM 2944 O OG  . SER B 1 131 ? 7.47100   -0.16481  15.80405  1.000 105.40790 ?  131 SER B OG  1 
ATOM 2945 N N   . ALA B 1 132 ? 5.64187   -4.17195  16.37277  1.000 107.01728 ?  132 ALA B N   1 
ATOM 2946 C CA  . ALA B 1 132 ? 5.16625   -5.49200  15.96940  1.000 94.99744  ?  132 ALA B CA  1 
ATOM 2947 C C   . ALA B 1 132 ? 3.69964   -5.70341  16.32518  1.000 114.27526 ?  132 ALA B C   1 
ATOM 2948 O O   . ALA B 1 132 ? 2.94128   -6.27187  15.53049  1.000 118.09360 ?  132 ALA B O   1 
ATOM 2949 C CB  . ALA B 1 132 ? 6.02431   -6.57761  16.60853  1.000 74.53203  ?  132 ALA B CB  1 
ATOM 2950 N N   . PHE B 1 133 ? 3.27622   -5.25292  17.51080  1.000 103.56804 ?  133 PHE B N   1 
ATOM 2951 C CA  . PHE B 1 133 ? 1.88033   -5.42790  17.91169  1.000 96.69949  ?  133 PHE B CA  1 
ATOM 2952 C C   . PHE B 1 133 ? 0.92281   -4.63556  17.02457  1.000 100.59483 ?  133 PHE B C   1 
ATOM 2953 O O   . PHE B 1 133 ? -0.10586  -5.16587  16.58654  1.000 107.23537 ?  133 PHE B O   1 
ATOM 2954 C CB  . PHE B 1 133 ? 1.68282   -5.07077  19.38448  1.000 111.22496 ?  133 PHE B CB  1 
ATOM 2955 C CG  . PHE B 1 133 ? 0.32592   -5.46255  19.91095  1.000 116.28606 ?  133 PHE B CG  1 
ATOM 2956 C CD1 . PHE B 1 133 ? 0.04183   -6.78307  20.24419  1.000 112.37470 ?  133 PHE B CD1 1 
ATOM 2957 C CD2 . PHE B 1 133 ? -0.67084  -4.51069  20.06255  1.000 108.91957 ?  133 PHE B CD2 1 
ATOM 2958 C CE1 . PHE B 1 133 ? -1.21436  -7.14221  20.71832  1.000 104.57349 ?  133 PHE B CE1 1 
ATOM 2959 C CE2 . PHE B 1 133 ? -1.92344  -4.86566  20.53767  1.000 109.88794 ?  133 PHE B CE2 1 
ATOM 2960 C CZ  . PHE B 1 133 ? -2.19443  -6.18060  20.86540  1.000 99.86321  ?  133 PHE B CZ  1 
ATOM 2961 N N   . ILE B 1 134 ? 1.19503   -3.34322  16.81335  1.000 97.41293  ?  134 ILE B N   1 
ATOM 2962 C CA  . ILE B 1 134 ? 0.33684   -2.56123  15.92310  1.000 101.88263 ?  134 ILE B CA  1 
ATOM 2963 C C   . ILE B 1 134 ? 0.29775   -3.18784  14.52803  1.000 88.93165  ?  134 ILE B C   1 
ATOM 2964 O O   . ILE B 1 134 ? -0.76749  -3.26612  13.90360  1.000 92.63270  ?  134 ILE B O   1 
ATOM 2965 C CB  . ILE B 1 134 ? 0.76179   -1.07586  15.90053  1.000 96.29809  ?  134 ILE B CB  1 
ATOM 2966 C CG1 . ILE B 1 134 ? -0.20909  -0.25018  15.05718  1.000 95.54530  ?  134 ILE B CG1 1 
ATOM 2967 C CG2 . ILE B 1 134 ? 2.16099   -0.88762  15.37068  1.000 103.89411 ?  134 ILE B CG2 1 
ATOM 2968 C CD1 . ILE B 1 134 ? 0.22786   1.18573   14.85807  1.000 102.91889 ?  134 ILE B CD1 1 
ATOM 2969 N N   . SER B 1 135 ? 1.44637   -3.64692  14.01603  1.000 89.18926  ?  135 SER B N   1 
ATOM 2970 C CA  . SER B 1 135 ? 1.44688   -4.36076  12.74132  1.000 89.81268  ?  135 SER B CA  1 
ATOM 2971 C C   . SER B 1 135 ? 0.52358   -5.57357  12.77856  1.000 100.28995 ?  135 SER B C   1 
ATOM 2972 O O   . SER B 1 135 ? -0.22375  -5.82377  11.82680  1.000 100.77813 ?  135 SER B O   1 
ATOM 2973 C CB  . SER B 1 135 ? 2.86503   -4.79005  12.35905  1.000 93.93660  ?  135 SER B CB  1 
ATOM 2974 O OG  . SER B 1 135 ? 3.79183   -3.72815  12.47863  1.000 109.57516 ?  135 SER B OG  1 
ATOM 2975 N N   . SER B 1 136 ? 0.59045   -6.36419  13.85516  1.000 91.76361  ?  136 SER B N   1 
ATOM 2976 C CA  . SER B 1 136 ? -0.23476  -7.56844  13.93455  1.000 90.64871  ?  136 SER B CA  1 
ATOM 2977 C C   . SER B 1 136 ? -1.71764  -7.22527  13.99327  1.000 85.02404  ?  136 SER B C   1 
ATOM 2978 O O   . SER B 1 136 ? -2.55333  -7.93298  13.41774  1.000 84.92062  ?  136 SER B O   1 
ATOM 2979 C CB  . SER B 1 136 ? 0.17060   -8.40696  15.14528  1.000 92.97343  ?  136 SER B CB  1 
ATOM 2980 O OG  . SER B 1 136 ? 1.57616   -8.54482  15.21564  1.000 100.26014 ?  136 SER B OG  1 
ATOM 2981 N N   . LEU B 1 137 ? -2.06554  -6.14831  14.69135  1.000 78.70004  ?  137 LEU B N   1 
ATOM 2982 C CA  . LEU B 1 137 ? -3.44906  -5.69076  14.67169  1.000 86.66710  ?  137 LEU B CA  1 
ATOM 2983 C C   . LEU B 1 137 ? -3.87061  -5.33349  13.25648  1.000 87.66125  ?  137 LEU B C   1 
ATOM 2984 O O   . LEU B 1 137 ? -4.96037  -5.70460  12.81326  1.000 84.72532  ?  137 LEU B O   1 
ATOM 2985 C CB  . LEU B 1 137 ? -3.64212  -4.49340  15.60376  1.000 95.66628  ?  137 LEU B CB  1 
ATOM 2986 C CG  . LEU B 1 137 ? -3.38636  -4.69761  17.09803  1.000 100.37933 ?  137 LEU B CG  1 
ATOM 2987 C CD1 . LEU B 1 137 ? -3.55850  -3.38266  17.84359  1.000 92.18509  ?  137 LEU B CD1 1 
ATOM 2988 C CD2 . LEU B 1 137 ? -4.30191  -5.77009  17.66863  1.000 79.88825  ?  137 LEU B CD2 1 
ATOM 2989 N N   . ILE B 1 138 ? -3.02900  -4.57147  12.54990  1.000 94.06539  ?  138 ILE B N   1 
ATOM 2990 C CA  . ILE B 1 138 ? -3.27909  -4.25337  11.14230  1.000 94.60432  ?  138 ILE B CA  1 
ATOM 2991 C C   . ILE B 1 138 ? -3.54172  -5.52436  10.34011  1.000 90.91980  ?  138 ILE B C   1 
ATOM 2992 O O   . ILE B 1 138 ? -4.50862  -5.61643  9.56953   1.000 90.72045  ?  138 ILE B O   1 
ATOM 2993 C CB  . ILE B 1 138 ? -2.09707  -3.45913  10.55476  1.000 86.17535  ?  138 ILE B CB  1 
ATOM 2994 C CG1 . ILE B 1 138 ? -1.89541  -2.13649  11.30182  1.000 85.09175  ?  138 ILE B CG1 1 
ATOM 2995 C CG2 . ILE B 1 138 ? -2.31224  -3.21487  9.07944   1.000 95.68345  ?  138 ILE B CG2 1 
ATOM 2996 C CD1 . ILE B 1 138 ? -3.01950  -1.14556  11.13316  1.000 107.78068 ?  138 ILE B CD1 1 
ATOM 2997 N N   . TYR B 1 139 ? -2.66313  -6.51480  10.49743  1.000 84.27559  ?  139 TYR B N   1 
ATOM 2998 C CA  . TYR B 1 139 ? -2.78250  -7.75673  9.73888   1.000 102.25152 ?  139 TYR B CA  1 
ATOM 2999 C C   . TYR B 1 139 ? -4.10093  -8.46244  10.03235  1.000 96.08172  ?  139 TYR B C   1 
ATOM 3000 O O   . TYR B 1 139 ? -4.83596  -8.84444  9.11321   1.000 87.55793  ?  139 TYR B O   1 
ATOM 3001 C CB  . TYR B 1 139 ? -1.59572  -8.66929  10.04847  1.000 104.11996 ?  139 TYR B CB  1 
ATOM 3002 C CG  . TYR B 1 139 ? -1.64798  -9.99457  9.32574   1.000 106.27147 ?  139 TYR B CG  1 
ATOM 3003 C CD1 . TYR B 1 139 ? -1.59320  -10.05664 7.93842   1.000 103.47573 ?  139 TYR B CD1 1 
ATOM 3004 C CD2 . TYR B 1 139 ? -1.75081  -11.18636 10.03447  1.000 108.32480 ?  139 TYR B CD2 1 
ATOM 3005 C CE1 . TYR B 1 139 ? -1.64455  -11.27176 7.27796   1.000 113.08259 ?  139 TYR B CE1 1 
ATOM 3006 C CE2 . TYR B 1 139 ? -1.79997  -12.40368 9.38721   1.000 108.72324 ?  139 TYR B CE2 1 
ATOM 3007 C CZ  . TYR B 1 139 ? -1.74600  -12.44257 8.01051   1.000 120.84975 ?  139 TYR B CZ  1 
ATOM 3008 O OH  . TYR B 1 139 ? -1.79566  -13.65888 7.37033   1.000 118.39351 ?  139 TYR B OH  1 
ATOM 3009 N N   . LEU B 1 140 ? -4.40708  -8.65297  11.31638  1.000 103.00284 ?  140 LEU B N   1 
ATOM 3010 C CA  . LEU B 1 140 ? -5.65162  -9.30613  11.70777  1.000 103.36368 ?  140 LEU B CA  1 
ATOM 3011 C C   . LEU B 1 140 ? -6.86590  -8.55277  11.17074  1.000 103.23530 ?  140 LEU B C   1 
ATOM 3012 O O   . LEU B 1 140 ? -7.74939  -9.14692  10.54165  1.000 106.22884 ?  140 LEU B O   1 
ATOM 3013 C CB  . LEU B 1 140 ? -5.70581  -9.43053  13.23053  1.000 95.74997  ?  140 LEU B CB  1 
ATOM 3014 C CG  . LEU B 1 140 ? -6.87573  -10.21373 13.81634  1.000 98.02504  ?  140 LEU B CG  1 
ATOM 3015 C CD1 . LEU B 1 140 ? -6.38815  -11.07389 14.96405  1.000 104.46311 ?  140 LEU B CD1 1 
ATOM 3016 C CD2 . LEU B 1 140 ? -7.96011  -9.26765  14.28536  1.000 99.68810  ?  140 LEU B CD2 1 
ATOM 3017 N N   . ILE B 1 141 ? -6.92881  -7.24020  11.42125  1.000 101.74214 ?  141 ILE B N   1 
ATOM 3018 C CA  . ILE B 1 141 ? -8.03709  -6.41487  10.94248  1.000 98.37593  ?  141 ILE B CA  1 
ATOM 3019 C C   . ILE B 1 141 ? -8.22152  -6.56453  9.43513   1.000 103.86137 ?  141 ILE B C   1 
ATOM 3020 O O   . ILE B 1 141 ? -9.35077  -6.56826  8.93205   1.000 111.54604 ?  141 ILE B O   1 
ATOM 3021 C CB  . ILE B 1 141 ? -7.81518  -4.94373  11.34973  1.000 75.90176  ?  141 ILE B CB  1 
ATOM 3022 C CG1 . ILE B 1 141 ? -7.90252  -4.79114  12.87123  1.000 82.22045  ?  141 ILE B CG1 1 
ATOM 3023 C CG2 . ILE B 1 141 ? -8.83263  -4.03337  10.67589  1.000 76.39958  ?  141 ILE B CG2 1 
ATOM 3024 C CD1 . ILE B 1 141 ? -7.18206  -3.56512  13.42086  1.000 83.36926  ?  141 ILE B CD1 1 
ATOM 3025 N N   . SER B 1 142 ? -7.11996  -6.68350  8.68726   1.000 106.47936 ?  142 SER B N   1 
ATOM 3026 C CA  . SER B 1 142 ? -7.24274  -6.89247  7.24652   1.000 109.59060 ?  142 SER B CA  1 
ATOM 3027 C C   . SER B 1 142 ? -7.92944  -8.21430  6.92521   1.000 117.18934 ?  142 SER B C   1 
ATOM 3028 O O   . SER B 1 142 ? -8.62737  -8.31729  5.90745   1.000 120.03930 ?  142 SER B O   1 
ATOM 3029 C CB  . SER B 1 142 ? -5.87039  -6.83835  6.57690   1.000 112.51556 ?  142 SER B CB  1 
ATOM 3030 O OG  . SER B 1 142 ? -5.23824  -8.10463  6.60196   1.000 115.35029 ?  142 SER B OG  1 
ATOM 3031 N N   . LYS B 1 143 ? -7.71811  -9.23999  7.75921   1.000 110.90409 ?  143 LYS B N   1 
ATOM 3032 C CA  . LYS B 1 143 ? -8.22395  -10.59220 7.53598   1.000 110.35391 ?  143 LYS B CA  1 
ATOM 3033 C C   . LYS B 1 143 ? -9.62480  -10.82736 8.10479   1.000 112.48082 ?  143 LYS B C   1 
ATOM 3034 O O   . LYS B 1 143 ? -9.95059  -11.97152 8.44712   1.000 114.83145 ?  143 LYS B O   1 
ATOM 3035 C CB  . LYS B 1 143 ? -7.25346  -11.60689 8.14412   1.000 95.73563  ?  143 LYS B CB  1 
ATOM 3036 C CG  . LYS B 1 143 ? -5.82907  -11.51438 7.63908   1.000 103.17513 ?  143 LYS B CG  1 
ATOM 3037 C CD  . LYS B 1 143 ? -5.63606  -12.39467 6.40969   1.000 111.05654 ?  143 LYS B CD  1 
ATOM 3038 C CE  . LYS B 1 143 ? -5.23050  -11.60067 5.17885   1.000 106.52145 ?  143 LYS B CE  1 
ATOM 3039 N NZ  . LYS B 1 143 ? -4.69963  -12.50591 4.12480   1.000 109.35575 ?  143 LYS B NZ  1 
ATOM 3040 N N   . LEU B 1 144 ? -10.47934 -9.80492  8.18376   1.000 121.52072 ?  144 LEU B N   1 
ATOM 3041 C CA  . LEU B 1 144 ? -11.73321 -9.91396  8.92598   1.000 114.29059 ?  144 LEU B CA  1 
ATOM 3042 C C   . LEU B 1 144 ? -12.92849 -9.50128  8.07755   1.000 125.57352 ?  144 LEU B C   1 
ATOM 3043 O O   . LEU B 1 144 ? -12.89890 -8.45570  7.41971   1.000 131.60542 ?  144 LEU B O   1 
ATOM 3044 C CB  . LEU B 1 144 ? -11.68364 -9.05259  10.19327  1.000 106.52406 ?  144 LEU B CB  1 
ATOM 3045 C CG  . LEU B 1 144 ? -10.84914 -9.60711  11.35021  1.000 92.57095  ?  144 LEU B CG  1 
ATOM 3046 C CD1 . LEU B 1 144 ? -11.11644 -8.81564  12.61615  1.000 103.70937 ?  144 LEU B CD1 1 
ATOM 3047 C CD2 . LEU B 1 144 ? -11.11450 -11.08969 11.56833  1.000 101.88333 ?  144 LEU B CD2 1 
ATOM 3048 N N   . GLU B 1 145 ? -13.98644 -10.31155 8.11707   1.000 138.32025 ?  145 GLU B N   1 
ATOM 3049 C CA  . GLU B 1 145 ? -15.25033 -9.92072  7.50763   1.000 135.61688 ?  145 GLU B CA  1 
ATOM 3050 C C   . GLU B 1 145 ? -15.89642 -8.80419  8.31225   1.000 133.94218 ?  145 GLU B C   1 
ATOM 3051 O O   . GLU B 1 145 ? -15.91424 -8.83639  9.54602   1.000 136.79289 ?  145 GLU B O   1 
ATOM 3052 C CB  . GLU B 1 145 ? -16.20929 -11.10771 7.41075   1.000 125.80092 ?  145 GLU B CB  1 
ATOM 3053 C CG  . GLU B 1 145 ? -15.75845 -12.20173 6.46816   1.000 121.86734 ?  145 GLU B CG  1 
ATOM 3054 C CD  . GLU B 1 145 ? -14.80673 -13.17141 7.12207   1.000 131.18670 ?  145 GLU B CD  1 
ATOM 3055 O OE1 . GLU B 1 145 ? -14.51181 -12.99864 8.32500   1.000 143.78029 ?  145 GLU B OE1 1 
ATOM 3056 O OE2 . GLU B 1 145 ? -14.34909 -14.10302 6.42995   1.000 131.18069 -1 145 GLU B OE2 1 
ATOM 3057 N N   . ASN B 1 146 ? -16.42541 -7.81365  7.59615   1.000 141.31154 ?  146 ASN B N   1 
ATOM 3058 C CA  . ASN B 1 146 ? -17.06848 -6.64476  8.18890   1.000 151.80816 ?  146 ASN B CA  1 
ATOM 3059 C C   . ASN B 1 146 ? -16.15386 -5.99875  9.22889   1.000 149.72972 ?  146 ASN B C   1 
ATOM 3060 O O   . ASN B 1 146 ? -16.54564 -5.74274  10.36882  1.000 152.85712 ?  146 ASN B O   1 
ATOM 3061 C CB  . ASN B 1 146 ? -18.41571 -7.01757  8.80675   1.000 159.56185 ?  146 ASN B CB  1 
ATOM 3062 C CG  . ASN B 1 146 ? -19.46185 -5.93732  8.62753   1.000 150.19257 ?  146 ASN B CG  1 
ATOM 3063 O OD1 . ASN B 1 146 ? -19.36530 -4.84516  9.19339   1.000 149.51554 ?  146 ASN B OD1 1 
ATOM 3064 N ND2 . ASN B 1 146 ? -20.49420 -6.25498  7.84811   1.000 150.41005 ?  146 ASN B ND2 1 
ATOM 3065 N N   . ASN B 1 147 ? -14.90641 -5.74943  8.83085   1.000 135.09289 ?  147 ASN B N   1 
ATOM 3066 C CA  . ASN B 1 147 ? -13.95478 -5.14165  9.75414   1.000 135.00435 ?  147 ASN B CA  1 
ATOM 3067 C C   . ASN B 1 147 ? -14.21226 -3.65394  9.95746   1.000 131.48650 ?  147 ASN B C   1 
ATOM 3068 O O   . ASN B 1 147 ? -13.65473 -3.06328  10.89166  1.000 129.70183 ?  147 ASN B O   1 
ATOM 3069 C CB  . ASN B 1 147 ? -12.53319 -5.38358  9.25605   1.000 132.11819 ?  147 ASN B CB  1 
ATOM 3070 C CG  . ASN B 1 147 ? -12.37130 -5.05311  7.79054   1.000 131.32405 ?  147 ASN B CG  1 
ATOM 3071 O OD1 . ASN B 1 147 ? -12.56384 -3.91445  7.37179   1.000 134.43118 ?  147 ASN B OD1 1 
ATOM 3072 N ND2 . ASN B 1 147 ? -12.05744 -6.06259  6.99350   1.000 131.86311 ?  147 ASN B ND2 1 
ATOM 3073 N N   . GLU B 1 148 ? -15.01044 -3.03808  9.08096   1.000 103.48661 ?  148 GLU B N   1 
ATOM 3074 C CA  . GLU B 1 148 ? -15.36361 -1.62820  9.22018   1.000 109.32433 ?  148 GLU B CA  1 
ATOM 3075 C C   . GLU B 1 148 ? -15.90720 -1.31184  10.60965  1.000 116.70065 ?  148 GLU B C   1 
ATOM 3076 O O   . GLU B 1 148 ? -15.60352 -0.25718  11.17261  1.000 109.24595 ?  148 GLU B O   1 
ATOM 3077 C CB  . GLU B 1 148 ? -16.36756 -1.23819  8.13654   1.000 123.27981 ?  148 GLU B CB  1 
ATOM 3078 C CG  . GLU B 1 148 ? -17.57582 -2.15578  8.04275   1.000 123.32598 ?  148 GLU B CG  1 
ATOM 3079 C CD  . GLU B 1 148 ? -17.35718 -3.32833  7.10264   1.000 147.34497 ?  148 GLU B CD  1 
ATOM 3080 O OE1 . GLU B 1 148 ? -16.19730 -3.77240  6.95257   1.000 152.00732 ?  148 GLU B OE1 1 
ATOM 3081 O OE2 . GLU B 1 148 ? -18.34954 -3.80401  6.51001   1.000 159.55504 -1 148 GLU B OE2 1 
ATOM 3082 N N   . LYS B 1 149 ? -16.77033 -2.17928  11.14385  1.000 121.36432 ?  149 LYS B N   1 
ATOM 3083 C CA  . LYS B 1 149 ? -17.27004 -2.02466  12.50739  1.000 104.46063 ?  149 LYS B CA  1 
ATOM 3084 C C   . LYS B 1 149 ? -16.11895 -1.84213  13.49439  1.000 104.92395 ?  149 LYS B C   1 
ATOM 3085 O O   . LYS B 1 149 ? -16.07538 -0.86922  14.25990  1.000 112.82762 ?  149 LYS B O   1 
ATOM 3086 C CB  . LYS B 1 149 ? -18.12072 -3.24271  12.87417  1.000 119.82982 ?  149 LYS B CB  1 
ATOM 3087 C CG  . LYS B 1 149 ? -19.30293 -3.47624  11.94098  1.000 122.90503 ?  149 LYS B CG  1 
ATOM 3088 C CD  . LYS B 1 149 ? -20.01281 -4.80841  12.21501  1.000 124.11283 ?  149 LYS B CD  1 
ATOM 3089 C CE  . LYS B 1 149 ? -21.31220 -4.64084  12.99517  1.000 96.88973  ?  149 LYS B CE  1 
ATOM 3090 N NZ  . LYS B 1 149 ? -21.09045 -4.10904  14.36553  1.000 107.66765 ?  149 LYS B NZ  1 
ATOM 3091 N N   . ILE B 1 150 ? -15.18696 -2.79738  13.50176  1.000 96.01084  ?  150 ILE B N   1 
ATOM 3092 C CA  . ILE B 1 150 ? -14.04355 -2.73687  14.40873  1.000 93.25497  ?  150 ILE B CA  1 
ATOM 3093 C C   . ILE B 1 150 ? -13.25835 -1.44470  14.19753  1.000 94.69142  ?  150 ILE B C   1 
ATOM 3094 O O   . ILE B 1 150 ? -12.84020 -0.78651  15.16152  1.000 107.22906 ?  150 ILE B O   1 
ATOM 3095 C CB  . ILE B 1 150 ? -13.15434 -3.98691  14.22682  1.000 85.80689  ?  150 ILE B CB  1 
ATOM 3096 C CG1 . ILE B 1 150 ? -13.90801 -5.26609  14.60114  1.000 89.86206  ?  150 ILE B CG1 1 
ATOM 3097 C CG2 . ILE B 1 150 ? -11.90241 -3.89570  15.06376  1.000 96.28006  ?  150 ILE B CG2 1 
ATOM 3098 C CD1 . ILE B 1 150 ? -14.68062 -5.90442  13.46824  1.000 114.70775 ?  150 ILE B CD1 1 
ATOM 3099 N N   . ILE B 1 151 ? -13.04738 -1.06210  12.93623  1.000 89.47094  ?  151 ILE B N   1 
ATOM 3100 C CA  . ILE B 1 151 ? -12.23793 0.11858   12.62962  1.000 102.15646 ?  151 ILE B CA  1 
ATOM 3101 C C   . ILE B 1 151 ? -12.90776 1.38443   13.16323  1.000 99.61613  ?  151 ILE B C   1 
ATOM 3102 O O   . ILE B 1 151 ? -12.24987 2.27604   13.72111  1.000 95.47675  ?  151 ILE B O   1 
ATOM 3103 C CB  . ILE B 1 151 ? -11.97719 0.18859   11.11348  1.000 90.10810  ?  151 ILE B CB  1 
ATOM 3104 C CG1 . ILE B 1 151 ? -11.25717 -1.07709  10.65906  1.000 75.59214  ?  151 ILE B CG1 1 
ATOM 3105 C CG2 . ILE B 1 151 ? -11.12015 1.38148   10.77152  1.000 81.68841  ?  151 ILE B CG2 1 
ATOM 3106 C CD1 . ILE B 1 151 ? -11.14248 -1.21175  9.17940   1.000 95.85762  ?  151 ILE B CD1 1 
ATOM 3107 N N   . GLU B 1 152 ? -14.21938 1.50175   12.95564  1.000 102.17109 ?  152 GLU B N   1 
ATOM 3108 C CA  . GLU B 1 152 ? -14.98121 2.60589   13.52696  1.000 102.34925 ?  152 GLU B CA  1 
ATOM 3109 C C   . GLU B 1 152 ? -14.84100 2.63696   15.03936  1.000 104.45024 ?  152 GLU B C   1 
ATOM 3110 O O   . GLU B 1 152 ? -14.69648 3.71134   15.63170  1.000 102.08834 ?  152 GLU B O   1 
ATOM 3111 C CB  . GLU B 1 152 ? -16.45090 2.47393   13.14293  1.000 103.11753 ?  152 GLU B CB  1 
ATOM 3112 C CG  . GLU B 1 152 ? -16.71486 2.55818   11.66933  1.000 102.20499 ?  152 GLU B CG  1 
ATOM 3113 C CD  . GLU B 1 152 ? -18.02880 1.92241   11.31326  1.000 119.70382 ?  152 GLU B CD  1 
ATOM 3114 O OE1 . GLU B 1 152 ? -18.48624 1.05845   12.09439  1.000 123.30550 ?  152 GLU B OE1 1 
ATOM 3115 O OE2 . GLU B 1 152 ? -18.59943 2.27890   10.26099  1.000 149.56583 -1 152 GLU B OE2 1 
ATOM 3116 N N   . SER B 1 153 ? -14.94600 1.47134   15.68714  1.000 105.04603 ?  153 SER B N   1 
ATOM 3117 C CA  . SER B 1 153 ? -14.75554 1.42687   17.13335  1.000 102.34980 ?  153 SER B CA  1 
ATOM 3118 C C   . SER B 1 153 ? -13.40403 2.01002   17.51666  1.000 104.75104 ?  153 SER B C   1 
ATOM 3119 O O   . SER B 1 153 ? -13.31003 2.80828   18.45324  1.000 106.54953 ?  153 SER B O   1 
ATOM 3120 C CB  . SER B 1 153 ? -14.89841 0.00150   17.66432  1.000 99.52459  ?  153 SER B CB  1 
ATOM 3121 O OG  . SER B 1 153 ? -16.25971 -0.35849  17.75859  1.000 98.91996  ?  153 SER B OG  1 
ATOM 3122 N N   . ILE B 1 154 ? -12.33939 1.59529   16.82090  1.000 84.24859  ?  154 ILE B N   1 
ATOM 3123 C CA  . ILE B 1 154 ? -11.00058 2.08244   17.15855  1.000 90.07572  ?  154 ILE B CA  1 
ATOM 3124 C C   . ILE B 1 154 ? -10.90930 3.59689   16.97463  1.000 96.18396  ?  154 ILE B C   1 
ATOM 3125 O O   . ILE B 1 154 ? -10.31495 4.30968   17.80177  1.000 96.30655  ?  154 ILE B O   1 
ATOM 3126 C CB  . ILE B 1 154 ? -9.93391  1.34385   16.33004  1.000 83.73004  ?  154 ILE B CB  1 
ATOM 3127 C CG1 . ILE B 1 154 ? -9.73953  -0.07911  16.84654  1.000 74.69448  ?  154 ILE B CG1 1 
ATOM 3128 C CG2 . ILE B 1 154 ? -8.61233  2.09416   16.34341  1.000 68.88112  ?  154 ILE B CG2 1 
ATOM 3129 C CD1 . ILE B 1 154 ? -9.32830  -1.04904  15.76099  1.000 87.23880  ?  154 ILE B CD1 1 
ATOM 3130 N N   . TYR B 1 155 ? -11.54264 4.12375   15.92355  1.000 102.10078 ?  155 TYR B N   1 
ATOM 3131 C CA  . TYR B 1 155 ? -11.40097 5.55694   15.67934  1.000 105.52803 ?  155 TYR B CA  1 
ATOM 3132 C C   . TYR B 1 155 ? -12.24830 6.38007   16.64183  1.000 102.24279 ?  155 TYR B C   1 
ATOM 3133 O O   . TYR B 1 155 ? -11.82459 7.45874   17.07039  1.000 105.23298 ?  155 TYR B O   1 
ATOM 3134 C CB  . TYR B 1 155 ? -11.74951 5.92392   14.23490  1.000 119.61551 ?  155 TYR B CB  1 
ATOM 3135 C CG  . TYR B 1 155 ? -11.67533 7.42633   14.01270  1.000 130.69361 ?  155 TYR B CG  1 
ATOM 3136 C CD1 . TYR B 1 155 ? -10.45240 8.06085   13.82177  1.000 123.77051 ?  155 TYR B CD1 1 
ATOM 3137 C CD2 . TYR B 1 155 ? -12.82208 8.21632   14.04253  1.000 134.88111 ?  155 TYR B CD2 1 
ATOM 3138 C CE1 . TYR B 1 155 ? -10.37817 9.43302   13.63932  1.000 125.16345 ?  155 TYR B CE1 1 
ATOM 3139 C CE2 . TYR B 1 155 ? -12.75458 9.58979   13.86254  1.000 128.29035 ?  155 TYR B CE2 1 
ATOM 3140 C CZ  . TYR B 1 155 ? -11.53022 10.19137  13.66114  1.000 130.16160 ?  155 TYR B CZ  1 
ATOM 3141 O OH  . TYR B 1 155 ? -11.45842 11.55453  13.47962  1.000 136.54988 ?  155 TYR B OH  1 
ATOM 3142 N N   . ILE B 1 156 ? -13.46527 5.92855   16.94944  1.000 98.39215  ?  156 ILE B N   1 
ATOM 3143 C CA  . ILE B 1 156 ? -14.28164 6.66572   17.90812  1.000 96.03746  ?  156 ILE B CA  1 
ATOM 3144 C C   . ILE B 1 156 ? -13.72045 6.51340   19.32135  1.000 101.98279 ?  156 ILE B C   1 
ATOM 3145 O O   . ILE B 1 156 ? -13.83034 7.43591   20.13864  1.000 106.80563 ?  156 ILE B O   1 
ATOM 3146 C CB  . ILE B 1 156 ? -15.75657 6.22460   17.82389  1.000 92.95325  ?  156 ILE B CB  1 
ATOM 3147 C CG1 . ILE B 1 156 ? -16.64760 7.20897   18.57610  1.000 95.98837  ?  156 ILE B CG1 1 
ATOM 3148 C CG2 . ILE B 1 156 ? -15.95209 4.82606   18.38963  1.000 104.72834 ?  156 ILE B CG2 1 
ATOM 3149 C CD1 . ILE B 1 156 ? -16.41168 8.64941   18.20477  1.000 117.53294 ?  156 ILE B CD1 1 
ATOM 3150 N N   . SER B 1 157 ? -13.08171 5.37874   19.62952  1.000 87.60204  ?  157 SER B N   1 
ATOM 3151 C CA  . SER B 1 157 ? -12.39800 5.21027   20.90003  1.000 82.27555  ?  157 SER B CA  1 
ATOM 3152 C C   . SER B 1 157 ? -11.06128 5.92973   20.93276  1.000 84.84864  ?  157 SER B C   1 
ATOM 3153 O O   . SER B 1 157 ? -10.41434 5.95260   21.98349  1.000 85.71591  ?  157 SER B O   1 
ATOM 3154 C CB  . SER B 1 157 ? -12.19776 3.72249   21.20177  1.000 83.96983  ?  157 SER B CB  1 
ATOM 3155 O OG  . SER B 1 157 ? -11.22844 3.15078   20.34695  1.000 94.00306  ?  157 SER B OG  1 
ATOM 3156 N N   . SER B 1 158 ? -10.64633 6.53503   19.82246  1.000 89.28074  ?  158 SER B N   1 
ATOM 3157 C CA  . SER B 1 158 ? -9.44554  7.35791   19.82284  1.000 98.27223  ?  158 SER B CA  1 
ATOM 3158 C C   . SER B 1 158 ? -9.75810  8.83025   20.08274  1.000 92.86257  ?  158 SER B C   1 
ATOM 3159 O O   . SER B 1 158 ? -8.83435  9.61088   20.34475  1.000 85.85757  ?  158 SER B O   1 
ATOM 3160 C CB  . SER B 1 158 ? -8.68231  7.19434   18.49516  1.000 91.67255  ?  158 SER B CB  1 
ATOM 3161 O OG  . SER B 1 158 ? -9.34574  7.82125   17.40743  1.000 90.29940  ?  158 SER B OG  1 
ATOM 3162 N N   . VAL B 1 159 ? -11.03940 9.20594   20.08444  1.000 74.41700  ?  159 VAL B N   1 
ATOM 3163 C CA  . VAL B 1 159 ? -11.45599 10.58996  20.28571  1.000 91.29622  ?  159 VAL B CA  1 
ATOM 3164 C C   . VAL B 1 159 ? -11.32259 10.95894  21.75781  1.000 102.84856 ?  159 VAL B C   1 
ATOM 3165 O O   . VAL B 1 159 ? -11.50905 10.11920  22.64535  1.000 103.96107 ?  159 VAL B O   1 
ATOM 3166 C CB  . VAL B 1 159 ? -12.90671 10.77318  19.80346  1.000 91.87543  ?  159 VAL B CB  1 
ATOM 3167 C CG1 . VAL B 1 159 ? -13.36721 12.21222  19.98668  1.000 90.61397  ?  159 VAL B CG1 1 
ATOM 3168 C CG2 . VAL B 1 159 ? -13.04374 10.33136  18.35088  1.000 105.38257 ?  159 VAL B CG2 1 
ATOM 3169 N N   . SER B 1 160 ? -10.97679 12.21655  22.02496  1.000 98.39830  ?  160 SER B N   1 
ATOM 3170 C CA  . SER B 1 160 ? -10.84251 12.72394  23.38492  1.000 90.32006  ?  160 SER B CA  1 
ATOM 3171 C C   . SER B 1 160 ? -12.09062 13.52362  23.75300  1.000 102.73141 ?  160 SER B C   1 
ATOM 3172 O O   . SER B 1 160 ? -12.34850 14.57956  23.16405  1.000 92.67169  ?  160 SER B O   1 
ATOM 3173 C CB  . SER B 1 160 ? -9.58644  13.58538  23.51418  1.000 93.47116  ?  160 SER B CB  1 
ATOM 3174 O OG  . SER B 1 160 ? -9.68927  14.48790  24.60145  1.000 113.28139 ?  160 SER B OG  1 
ATOM 3175 N N   . PHE B 1 161 ? -12.84145 13.04305  24.74870  1.000 109.04945 ?  161 PHE B N   1 
ATOM 3176 C CA  . PHE B 1 161 ? -14.05424 13.70901  25.20025  1.000 106.52862 ?  161 PHE B CA  1 
ATOM 3177 C C   . PHE B 1 161 ? -13.76861 14.55291  26.43761  1.000 108.13020 ?  161 PHE B C   1 
ATOM 3178 O O   . PHE B 1 161 ? -12.65768 14.57048  26.97731  1.000 108.91940 ?  161 PHE B O   1 
ATOM 3179 C CB  . PHE B 1 161 ? -15.16788 12.70219  25.50485  1.000 105.30993 ?  161 PHE B CB  1 
ATOM 3180 C CG  . PHE B 1 161 ? -15.42362 11.72193  24.40608  1.000 105.29553 ?  161 PHE B CG  1 
ATOM 3181 C CD1 . PHE B 1 161 ? -16.17652 12.08797  23.30021  1.000 108.97808 ?  161 PHE B CD1 1 
ATOM 3182 C CD2 . PHE B 1 161 ? -14.93142 10.42882  24.48099  1.000 105.03613 ?  161 PHE B CD2 1 
ATOM 3183 C CE1 . PHE B 1 161 ? -16.42766 11.18541  22.27729  1.000 107.22830 ?  161 PHE B CE1 1 
ATOM 3184 C CE2 . PHE B 1 161 ? -15.17672 9.51741   23.46209  1.000 112.25022 ?  161 PHE B CE2 1 
ATOM 3185 C CZ  . PHE B 1 161 ? -15.92793 9.89858   22.35776  1.000 115.24148 ?  161 PHE B CZ  1 
ATOM 3186 N N   . PHE B 1 162 ? -14.79960 15.27805  26.87896  1.000 110.61789 ?  162 PHE B N   1 
ATOM 3187 C CA  . PHE B 1 162 ? -14.69869 16.05858  28.10728  1.000 104.39980 ?  162 PHE B CA  1 
ATOM 3188 C C   . PHE B 1 162 ? -14.50003 15.15311  29.31895  1.000 97.21523  ?  162 PHE B C   1 
ATOM 3189 O O   . PHE B 1 162 ? -13.65075 15.41759  30.18694  1.000 94.13742  ?  162 PHE B O   1 
ATOM 3190 C CB  . PHE B 1 162 ? -15.95489 16.90223  28.28563  1.000 92.98675  ?  162 PHE B CB  1 
ATOM 3191 C CG  . PHE B 1 162 ? -15.82326 17.93826  29.34112  1.000 90.62686  ?  162 PHE B CG  1 
ATOM 3192 C CD1 . PHE B 1 162 ? -14.79995 18.86153  29.28831  1.000 93.81882  ?  162 PHE B CD1 1 
ATOM 3193 C CD2 . PHE B 1 162 ? -16.66565 17.93646  30.43551  1.000 99.21891  ?  162 PHE B CD2 1 
ATOM 3194 C CE1 . PHE B 1 162 ? -14.66429 19.81113  30.27138  1.000 96.36466  ?  162 PHE B CE1 1 
ATOM 3195 C CE2 . PHE B 1 162 ? -16.52750 18.87740  31.42952  1.000 104.41955 ?  162 PHE B CE2 1 
ATOM 3196 C CZ  . PHE B 1 162 ? -15.52388 19.81602  31.34888  1.000 102.21389 ?  162 PHE B CZ  1 
ATOM 3197 N N   . SER B 1 163 ? -15.31009 14.09158  29.40518  1.000 85.99282  ?  163 SER B N   1 
ATOM 3198 C CA  . SER B 1 163 ? -15.20848 13.14183  30.50557  1.000 91.10465  ?  163 SER B CA  1 
ATOM 3199 C C   . SER B 1 163 ? -13.79755 12.58189  30.63708  1.000 90.74968  ?  163 SER B C   1 
ATOM 3200 O O   . SER B 1 163 ? -13.33070 12.32801  31.75109  1.000 84.95462  ?  163 SER B O   1 
ATOM 3201 C CB  . SER B 1 163 ? -16.24334 12.03435  30.31514  1.000 74.50773  ?  163 SER B CB  1 
ATOM 3202 O OG  . SER B 1 163 ? -16.13365 11.46676  29.02960  1.000 99.99423  ?  163 SER B OG  1 
ATOM 3203 N N   . ASP B 1 164 ? -13.08668 12.42995  29.51980  1.000 92.24205  ?  164 ASP B N   1 
ATOM 3204 C CA  . ASP B 1 164 ? -11.70499 11.95866  29.56963  1.000 89.57528  ?  164 ASP B CA  1 
ATOM 3205 C C   . ASP B 1 164 ? -10.78373 13.00792  30.18226  1.000 85.44577  ?  164 ASP B C   1 
ATOM 3206 O O   . ASP B 1 164 ? -9.83632  12.66962  30.90166  1.000 82.01182  ?  164 ASP B O   1 
ATOM 3207 C CB  . ASP B 1 164 ? -11.22753 11.57640  28.16888  1.000 94.73222  ?  164 ASP B CB  1 
ATOM 3208 C CG  . ASP B 1 164 ? -11.96973 10.38916  27.60922  1.000 98.18661  ?  164 ASP B CG  1 
ATOM 3209 O OD1 . ASP B 1 164 ? -12.28107 9.46977   28.39480  1.000 104.77646 -1 164 ASP B OD1 1 
ATOM 3210 O OD2 . ASP B 1 164 ? -12.25719 10.38256  26.39555  1.000 95.70917  ?  164 ASP B OD2 1 
ATOM 3211 N N   . LYS B 1 165 ? -11.01334 14.28356  29.87673  1.000 91.69907  ?  165 LYS B N   1 
ATOM 3212 C CA  . LYS B 1 165 ? -10.18367 15.32799  30.46641  1.000 91.05424  ?  165 LYS B CA  1 
ATOM 3213 C C   . LYS B 1 165 ? -10.38464 15.38790  31.97369  1.000 79.50710  ?  165 LYS B C   1 
ATOM 3214 O O   . LYS B 1 165 ? -9.41340  15.47129  32.74054  1.000 89.73339  ?  165 LYS B O   1 
ATOM 3215 C CB  . LYS B 1 165 ? -10.50374 16.67931  29.82289  1.000 103.16239 ?  165 LYS B CB  1 
ATOM 3216 C CG  . LYS B 1 165 ? -10.15217 16.77693  28.34067  1.000 91.12043  ?  165 LYS B CG  1 
ATOM 3217 C CD  . LYS B 1 165 ? -10.27009 18.21132  27.85299  1.000 106.09249 ?  165 LYS B CD  1 
ATOM 3218 C CE  . LYS B 1 165 ? -10.00924 18.33267  26.36081  1.000 111.52041 ?  165 LYS B CE  1 
ATOM 3219 N NZ  . LYS B 1 165 ? -10.45233 17.12661  25.61819  1.000 110.53483 ?  165 LYS B NZ  1 
ATOM 3220 N N   . VAL B 1 166 ? -11.64560 15.35892  32.41358  1.000 83.00049  ?  166 VAL B N   1 
ATOM 3221 C CA  . VAL B 1 166 ? -11.92849 15.26292  33.84524  1.000 89.96293  ?  166 VAL B CA  1 
ATOM 3222 C C   . VAL B 1 166 ? -11.25834 14.02829  34.44153  1.000 85.64299  ?  166 VAL B C   1 
ATOM 3223 O O   . VAL B 1 166 ? -10.68477 14.08078  35.53692  1.000 85.14906  ?  166 VAL B O   1 
ATOM 3224 C CB  . VAL B 1 166 ? -13.44941 15.27649  34.09904  1.000 94.26132  ?  166 VAL B CB  1 
ATOM 3225 C CG1 . VAL B 1 166 ? -13.74110 15.03602  35.56738  1.000 85.52859  ?  166 VAL B CG1 1 
ATOM 3226 C CG2 . VAL B 1 166 ? -14.04909 16.61128  33.66096  1.000 81.54812  ?  166 VAL B CG2 1 
ATOM 3227 N N   . ARG B 1 167 ? -11.34979 12.89272  33.74143  1.000 88.40528  ?  167 ARG B N   1 
ATOM 3228 C CA  . ARG B 1 167 ? -10.74740 11.64770  34.20899  1.000 83.95050  ?  167 ARG B CA  1 
ATOM 3229 C C   . ARG B 1 167 ? -9.24418  11.78591  34.42031  1.000 95.22929  ?  167 ARG B C   1 
ATOM 3230 O O   . ARG B 1 167 ? -8.70858  11.33522  35.43446  1.000 95.30697  ?  167 ARG B O   1 
ATOM 3231 C CB  . ARG B 1 167 ? -11.04375 10.53701  33.20826  1.000 65.93121  ?  167 ARG B CB  1 
ATOM 3232 C CG  . ARG B 1 167 ? -11.65908 9.30910   33.81724  1.000 81.25934  ?  167 ARG B CG  1 
ATOM 3233 C CD  . ARG B 1 167 ? -12.18810 8.41300   32.72332  1.000 86.05703  ?  167 ARG B CD  1 
ATOM 3234 N NE  . ARG B 1 167 ? -13.52699 8.80122   32.29777  1.000 87.86089  ?  167 ARG B NE  1 
ATOM 3235 C CZ  . ARG B 1 167 ? -14.09075 8.41925   31.15828  1.000 109.11591 ?  167 ARG B CZ  1 
ATOM 3236 N NH1 . ARG B 1 167 ? -13.43847 7.67243   30.28136  1.000 108.45077 ?  167 ARG B NH1 1 
ATOM 3237 N NH2 . ARG B 1 167 ? -15.34804 8.77773   30.90087  1.000 92.75294  ?  167 ARG B NH2 1 
ATOM 3238 N N   . ASN B 1 168 ? -8.54123  12.38279  33.45894  1.000 114.63444 ?  168 ASN B N   1 
ATOM 3239 C CA  . ASN B 1 168 ? -7.09835  12.57487  33.60104  1.000 117.60267 ?  168 ASN B CA  1 
ATOM 3240 C C   . ASN B 1 168 ? -6.77758  13.50051  34.77276  1.000 117.10171 ?  168 ASN B C   1 
ATOM 3241 O O   . ASN B 1 168 ? -5.86305  13.23005  35.57163  1.000 118.38349 ?  168 ASN B O   1 
ATOM 3242 C CB  . ASN B 1 168 ? -6.50955  13.11633  32.29759  1.000 125.36160 ?  168 ASN B CB  1 
ATOM 3243 C CG  . ASN B 1 168 ? -5.06572  13.56951  32.45044  1.000 128.27419 ?  168 ASN B CG  1 
ATOM 3244 O OD1 . ASN B 1 168 ? -4.13981  12.76115  32.36084  1.000 127.58986 ?  168 ASN B OD1 1 
ATOM 3245 N ND2 . ASN B 1 168 ? -4.86695  14.86521  32.67401  1.000 131.47146 ?  168 ASN B ND2 1 
ATOM 3246 N N   . LEU B 1 169 ? -7.49520  14.62639  34.86447  1.000 102.18839 ?  169 LEU B N   1 
ATOM 3247 C CA  . LEU B 1 169 ? -7.28359  15.55281  35.97520  1.000 103.16859 ?  169 LEU B CA  1 
ATOM 3248 C C   . LEU B 1 169 ? -7.43086  14.85129  37.32371  1.000 94.80777  ?  169 LEU B C   1 
ATOM 3249 O O   . LEU B 1 169 ? -6.59678  15.01592  38.22112  1.000 86.19049  ?  169 LEU B O   1 
ATOM 3250 C CB  . LEU B 1 169 ? -8.25669  16.72460  35.87038  1.000 88.86330  ?  169 LEU B CB  1 
ATOM 3251 C CG  . LEU B 1 169 ? -8.17017  17.67761  37.05622  1.000 81.07495  ?  169 LEU B CG  1 
ATOM 3252 C CD1 . LEU B 1 169 ? -6.76603  18.24862  37.15277  1.000 72.02456  ?  169 LEU B CD1 1 
ATOM 3253 C CD2 . LEU B 1 169 ? -9.20006  18.78046  36.90714  1.000 86.57562  ?  169 LEU B CD2 1 
ATOM 3254 N N   . ILE B 1 170 ? -8.49465  14.06311  37.48228  1.000 93.39099  ?  170 ILE B N   1 
ATOM 3255 C CA  . ILE B 1 170 ? -8.69184  13.32854  38.72623  1.000 88.73879  ?  170 ILE B CA  1 
ATOM 3256 C C   . ILE B 1 170 ? -7.62205  12.25215  38.88263  1.000 86.67224  ?  170 ILE B C   1 
ATOM 3257 O O   . ILE B 1 170 ? -7.20826  11.93291  40.00358  1.000 93.21466  ?  170 ILE B O   1 
ATOM 3258 C CB  . ILE B 1 170 ? -10.12118 12.75299  38.76508  1.000 86.44788  ?  170 ILE B CB  1 
ATOM 3259 C CG1 . ILE B 1 170 ? -11.14119 13.88141  38.56296  1.000 79.10954  ?  170 ILE B CG1 1 
ATOM 3260 C CG2 . ILE B 1 170 ? -10.38081 12.02582  40.07532  1.000 84.99708  ?  170 ILE B CG2 1 
ATOM 3261 C CD1 . ILE B 1 170 ? -12.58068 13.46243  38.73022  1.000 80.16228  ?  170 ILE B CD1 1 
ATOM 3262 N N   . GLU B 1 171 ? -7.15212  11.68697  37.76715  1.000 90.42616  ?  171 GLU B N   1 
ATOM 3263 C CA  . GLU B 1 171 ? -6.11358  10.66276  37.79480  1.000 93.17857  ?  171 GLU B CA  1 
ATOM 3264 C C   . GLU B 1 171 ? -4.82552  11.18474  38.39917  1.000 95.47240  ?  171 GLU B C   1 
ATOM 3265 O O   . GLU B 1 171 ? -4.06432  10.41354  38.99353  1.000 99.39327  ?  171 GLU B O   1 
ATOM 3266 C CB  . GLU B 1 171 ? -5.83790  10.17553  36.37366  1.000 103.04858 ?  171 GLU B CB  1 
ATOM 3267 C CG  . GLU B 1 171 ? -6.45896  8.85494   35.99361  1.000 105.32994 ?  171 GLU B CG  1 
ATOM 3268 C CD  . GLU B 1 171 ? -6.16402  8.49247   34.55052  1.000 121.87142 ?  171 GLU B CD  1 
ATOM 3269 O OE1 . GLU B 1 171 ? -5.21713  9.07460   33.97309  1.000 126.92861 ?  171 GLU B OE1 1 
ATOM 3270 O OE2 . GLU B 1 171 ? -6.88396  7.63848   33.99069  1.000 125.72644 -1 171 GLU B OE2 1 
ATOM 3271 N N   . LYS B 1 172 ? -4.54920  12.48000  38.21792  1.000 105.54248 ?  172 LYS B N   1 
ATOM 3272 C CA  . LYS B 1 172 ? -3.30650  13.05394  38.74327  1.000 91.92371  ?  172 LYS B CA  1 
ATOM 3273 C C   . LYS B 1 172 ? -3.14701  12.84277  40.24879  1.000 88.84864  ?  172 LYS B C   1 
ATOM 3274 O O   . LYS B 1 172 ? -2.01745  12.76844  40.74471  1.000 110.32390 ?  172 LYS B O   1 
ATOM 3275 C CB  . LYS B 1 172 ? -3.22483  14.54906  38.42609  1.000 90.59001  ?  172 LYS B CB  1 
ATOM 3276 C CG  . LYS B 1 172 ? -3.01129  14.86467  36.95333  1.000 108.14099 ?  172 LYS B CG  1 
ATOM 3277 C CD  . LYS B 1 172 ? -1.69571  14.30172  36.43773  1.000 103.06417 ?  172 LYS B CD  1 
ATOM 3278 C CE  . LYS B 1 172 ? -1.82691  13.82229  34.99704  1.000 101.39509 ?  172 LYS B CE  1 
ATOM 3279 N NZ  . LYS B 1 172 ? -2.70635  12.61834  34.88176  1.000 105.07364 ?  172 LYS B NZ  1 
ATOM 3280 N N   . ASP B 1 173 ? -4.25830  12.74698  40.99755  1.000 88.07543  ?  173 ASP B N   1 
ATOM 3281 C CA  . ASP B 1 173 ? -4.18166  12.51953  42.44815  1.000 94.66792  ?  173 ASP B CA  1 
ATOM 3282 C C   . ASP B 1 173 ? -5.50942  11.92428  42.93624  1.000 93.78456  ?  173 ASP B C   1 
ATOM 3283 O O   . ASP B 1 173 ? -6.35724  12.61406  43.50678  1.000 90.16520  ?  173 ASP B O   1 
ATOM 3284 C CB  . ASP B 1 173 ? -3.84700  13.79619  43.21812  1.000 82.95785  ?  173 ASP B CB  1 
ATOM 3285 C CG  . ASP B 1 173 ? -3.45491  13.51687  44.66180  1.000 104.37607 ?  173 ASP B CG  1 
ATOM 3286 O OD1 . ASP B 1 173 ? -3.43151  12.32567  45.05175  1.000 104.32461 ?  173 ASP B OD1 1 
ATOM 3287 O OD2 . ASP B 1 173 ? -3.16962  14.48321  45.40532  1.000 124.64913 -1 173 ASP B OD2 1 
ATOM 3288 N N   . LEU B 1 174 ? -5.66668  10.61280  42.72479  1.000 89.06359  ?  174 LEU B N   1 
ATOM 3289 C CA  . LEU B 1 174 ? -6.89390  9.92619   43.12545  1.000 82.08947  ?  174 LEU B CA  1 
ATOM 3290 C C   . LEU B 1 174 ? -7.19555  10.06565  44.61657  1.000 97.09312  ?  174 LEU B C   1 
ATOM 3291 O O   . LEU B 1 174 ? -8.33472  9.81299   45.02734  1.000 101.28494 ?  174 LEU B O   1 
ATOM 3292 C CB  . LEU B 1 174 ? -6.81731  8.43943   42.76771  1.000 68.82768  ?  174 LEU B CB  1 
ATOM 3293 C CG  . LEU B 1 174 ? -7.29592  7.98509   41.38305  1.000 89.22587  ?  174 LEU B CG  1 
ATOM 3294 C CD1 . LEU B 1 174 ? -7.42499  6.46553   41.32525  1.000 73.92586  ?  174 LEU B CD1 1 
ATOM 3295 C CD2 . LEU B 1 174 ? -8.59415  8.65936   40.95970  1.000 89.55034  ?  174 LEU B CD2 1 
ATOM 3296 N N   . SER B 1 175 ? -6.21666  10.44885  45.44228  1.000 95.74744  ?  175 SER B N   1 
ATOM 3297 C CA  . SER B 1 175 ? -6.44984  10.53354  46.88001  1.000 91.93463  ?  175 SER B CA  1 
ATOM 3298 C C   . SER B 1 175 ? -7.02241  11.87205  47.32242  1.000 83.02812  ?  175 SER B C   1 
ATOM 3299 O O   . SER B 1 175 ? -7.51081  11.96812  48.45254  1.000 83.81168  ?  175 SER B O   1 
ATOM 3300 C CB  . SER B 1 175 ? -5.15635  10.26152  47.65419  1.000 79.91969  ?  175 SER B CB  1 
ATOM 3301 O OG  . SER B 1 175 ? -4.45183  9.16567   47.09425  1.000 90.72029  ?  175 SER B OG  1 
ATOM 3302 N N   . ARG B 1 176 ? -6.99605  12.89229  46.46830  1.000 83.22470  ?  176 ARG B N   1 
ATOM 3303 C CA  . ARG B 1 176 ? -7.50821  14.19581  46.86219  1.000 88.72271  ?  176 ARG B CA  1 
ATOM 3304 C C   . ARG B 1 176 ? -9.03001  14.17616  46.94868  1.000 94.81955  ?  176 ARG B C   1 
ATOM 3305 O O   . ARG B 1 176 ? -9.70959  13.46342  46.20446  1.000 93.76402  ?  176 ARG B O   1 
ATOM 3306 C CB  . ARG B 1 176 ? -7.07121  15.28022  45.87871  1.000 80.23511  ?  176 ARG B CB  1 
ATOM 3307 C CG  . ARG B 1 176 ? -7.40412  16.68078  46.37345  1.000 81.76273  ?  176 ARG B CG  1 
ATOM 3308 C CD  . ARG B 1 176 ? -8.10654  17.49631  45.30817  1.000 89.57365  ?  176 ARG B CD  1 
ATOM 3309 N NE  . ARG B 1 176 ? -7.19434  17.92296  44.25538  1.000 103.07306 ?  176 ARG B NE  1 
ATOM 3310 C CZ  . ARG B 1 176 ? -6.61655  19.11612  44.21557  1.000 96.21651  ?  176 ARG B CZ  1 
ATOM 3311 N NH1 . ARG B 1 176 ? -6.86595  20.03435  45.13584  1.000 81.99783  ?  176 ARG B NH1 1 
ATOM 3312 N NH2 . ARG B 1 176 ? -5.77846  19.39920  43.22196  1.000 90.30479  ?  176 ARG B NH2 1 
ATOM 3313 N N   . LYS B 1 177 ? -9.56331  14.98074  47.87034  1.000 87.66376  ?  177 LYS B N   1 
ATOM 3314 C CA  . LYS B 1 177 ? -11.00706 15.15755  48.01934  1.000 89.70304  ?  177 LYS B CA  1 
ATOM 3315 C C   . LYS B 1 177 ? -11.49696 16.09488  46.91386  1.000 90.98569  ?  177 LYS B C   1 
ATOM 3316 O O   . LYS B 1 177 ? -11.77291 17.27994  47.12459  1.000 87.85371  ?  177 LYS B O   1 
ATOM 3317 C CB  . LYS B 1 177 ? -11.33808 15.68476  49.41320  1.000 99.35435  ?  177 LYS B CB  1 
ATOM 3318 C CG  . LYS B 1 177 ? -10.79219 14.81605  50.55244  1.000 102.99182 ?  177 LYS B CG  1 
ATOM 3319 C CD  . LYS B 1 177 ? -11.25202 13.36448  50.40521  1.000 106.47239 ?  177 LYS B CD  1 
ATOM 3320 C CE  . LYS B 1 177 ? -10.46156 12.41912  51.30057  1.000 85.95590  ?  177 LYS B CE  1 
ATOM 3321 N NZ  . LYS B 1 177 ? -10.81204 10.98807  51.05271  1.000 75.46580  ?  177 LYS B NZ  1 
ATOM 3322 N N   . TRP B 1 178 ? -11.59623 15.54598  45.70194  1.000 88.22477  ?  178 TRP B N   1 
ATOM 3323 C CA  . TRP B 1 178 ? -12.08756 16.32955  44.57750  1.000 87.05605  ?  178 TRP B CA  1 
ATOM 3324 C C   . TRP B 1 178 ? -13.53519 16.73879  44.79763  1.000 86.06491  ?  178 TRP B C   1 
ATOM 3325 O O   . TRP B 1 178 ? -14.32903 16.00143  45.38511  1.000 86.37192  ?  178 TRP B O   1 
ATOM 3326 C CB  . TRP B 1 178 ? -12.00947 15.55393  43.26570  1.000 80.96858  ?  178 TRP B CB  1 
ATOM 3327 C CG  . TRP B 1 178 ? -10.65879 15.13520  42.82860  1.000 86.37174  ?  178 TRP B CG  1 
ATOM 3328 C CD1 . TRP B 1 178 ? -10.07068 13.92841  43.03634  1.000 86.17482  ?  178 TRP B CD1 1 
ATOM 3329 C CD2 . TRP B 1 178 ? -9.70556  15.93268  42.11640  1.000 84.56297  ?  178 TRP B CD2 1 
ATOM 3330 N NE1 . TRP B 1 178 ? -8.81768  13.91034  42.47214  1.000 82.59845  ?  178 TRP B NE1 1 
ATOM 3331 C CE2 . TRP B 1 178 ? -8.56645  15.13255  41.90963  1.000 69.44742  ?  178 TRP B CE2 1 
ATOM 3332 C CE3 . TRP B 1 178 ? -9.70968  17.24358  41.62706  1.000 85.21041  ?  178 TRP B CE3 1 
ATOM 3333 C CZ2 . TRP B 1 178 ? -7.43941  15.59734  41.24301  1.000 85.44570  ?  178 TRP B CZ2 1 
ATOM 3334 C CZ3 . TRP B 1 178 ? -8.59033  17.70417  40.95888  1.000 88.41538  ?  178 TRP B CZ3 1 
ATOM 3335 C CH2 . TRP B 1 178 ? -7.46928  16.88271  40.77345  1.000 94.55234  ?  178 TRP B CH2 1 
ATOM 3336 N N   . THR B 1 179 ? -13.87664 17.92788  44.30861  1.000 86.19473  ?  179 THR B N   1 
ATOM 3337 C CA  . THR B 1 179 ? -15.25295 18.39284  44.26602  1.000 81.05069  ?  179 THR B CA  1 
ATOM 3338 C C   . THR B 1 179 ? -15.52957 18.96360  42.88226  1.000 89.17595  ?  179 THR B C   1 
ATOM 3339 O O   . THR B 1 179 ? -14.63205 19.09348  42.04459  1.000 100.20887 ?  179 THR B O   1 
ATOM 3340 C CB  . THR B 1 179 ? -15.53042 19.45978  45.32929  1.000 79.40084  ?  179 THR B CB  1 
ATOM 3341 O OG1 . THR B 1 179 ? -14.71425 20.60078  45.06316  1.000 95.07196  ?  179 THR B OG1 1 
ATOM 3342 C CG2 . THR B 1 179 ? -15.18903 18.93394  46.71785  1.000 77.08240  ?  179 THR B CG2 1 
ATOM 3343 N N   . LEU B 1 180 ? -16.79384 19.31582  42.65073  1.000 95.35079  ?  180 LEU B N   1 
ATOM 3344 C CA  . LEU B 1 180 ? -17.17719 19.92535  41.38090  1.000 100.32669 ?  180 LEU B CA  1 
ATOM 3345 C C   . LEU B 1 180 ? -16.63908 21.34076  41.22921  1.000 99.51136  ?  180 LEU B C   1 
ATOM 3346 O O   . LEU B 1 180 ? -16.39065 21.78614  40.10358  1.000 87.77895  ?  180 LEU B O   1 
ATOM 3347 C CB  . LEU B 1 180 ? -18.68981 19.94660  41.24716  1.000 105.36968 ?  180 LEU B CB  1 
ATOM 3348 C CG  . LEU B 1 180 ? -19.20898 20.27332  39.85546  1.000 95.16007  ?  180 LEU B CG  1 
ATOM 3349 C CD1 . LEU B 1 180 ? -18.98180 19.15320  38.85732  1.000 85.49559  ?  180 LEU B CD1 1 
ATOM 3350 C CD2 . LEU B 1 180 ? -20.64790 20.60771  40.02241  1.000 97.67607  ?  180 LEU B CD2 1 
ATOM 3351 N N   . GLY B 1 181 ? -16.50712 22.07844  42.33209  1.000 99.33520  ?  181 GLY B N   1 
ATOM 3352 C CA  . GLY B 1 181 ? -15.88953 23.39186  42.25128  1.000 95.12687  ?  181 GLY B CA  1 
ATOM 3353 C C   . GLY B 1 181 ? -14.47073 23.32595  41.72271  1.000 98.27242  ?  181 GLY B C   1 
ATOM 3354 O O   . GLY B 1 181 ? -14.06433 24.13988  40.88861  1.000 91.00319  ?  181 GLY B O   1 
ATOM 3355 N N   . ILE B 1 182 ? -13.68866 22.36694  42.22742  1.000 102.36909 ?  182 ILE B N   1 
ATOM 3356 C CA  . ILE B 1 182 ? -12.31358 22.17334  41.76933  1.000 96.16893  ?  182 ILE B CA  1 
ATOM 3357 C C   . ILE B 1 182 ? -12.27627 21.89917  40.26739  1.000 91.68751  ?  182 ILE B C   1 
ATOM 3358 O O   . ILE B 1 182 ? -11.52820 22.54301  39.52003  1.000 91.74357  ?  182 ILE B O   1 
ATOM 3359 C CB  . ILE B 1 182 ? -11.64288 21.04914  42.58217  1.000 78.83646  ?  182 ILE B CB  1 
ATOM 3360 C CG1 . ILE B 1 182 ? -11.69551 21.39027  44.07679  1.000 84.13056  ?  182 ILE B CG1 1 
ATOM 3361 C CG2 . ILE B 1 182 ? -10.22122 20.81812  42.12793  1.000 77.94055  ?  182 ILE B CG2 1 
ATOM 3362 C CD1 . ILE B 1 182 ? -10.89180 20.45909  44.96289  1.000 98.21423  ?  182 ILE B CD1 1 
ATOM 3363 N N   . ILE B 1 183 ? -13.07320 20.92930  39.80770  1.000 98.52093  ?  183 ILE B N   1 
ATOM 3364 C CA  . ILE B 1 183 ? -13.12758 20.61012  38.37940  1.000 101.88214 ?  183 ILE B CA  1 
ATOM 3365 C C   . ILE B 1 183 ? -13.52552 21.83683  37.56469  1.000 107.78489 ?  183 ILE B C   1 
ATOM 3366 O O   . ILE B 1 183 ? -12.92200 22.13307  36.52639  1.000 114.49060 ?  183 ILE B O   1 
ATOM 3367 C CB  . ILE B 1 183 ? -14.08631 19.43330  38.12043  1.000 102.23518 ?  183 ILE B CB  1 
ATOM 3368 C CG1 . ILE B 1 183 ? -13.73137 18.23905  39.00948  1.000 101.31639 ?  183 ILE B CG1 1 
ATOM 3369 C CG2 . ILE B 1 183 ? -14.05916 19.05008  36.65147  1.000 100.83709 ?  183 ILE B CG2 1 
ATOM 3370 C CD1 . ILE B 1 183 ? -12.40877 17.58708  38.66842  1.000 105.79154 ?  183 ILE B CD1 1 
ATOM 3371 N N   . ALA B 1 184 ? -14.57277 22.54636  38.00440  1.000 108.50106 ?  184 ALA B N   1 
ATOM 3372 C CA  . ALA B 1 184 ? -15.03153 23.74164  37.29775  1.000 107.06793 ?  184 ALA B CA  1 
ATOM 3373 C C   . ALA B 1 184 ? -13.91716 24.77320  37.16777  1.000 103.21581 ?  184 ALA B C   1 
ATOM 3374 O O   . ALA B 1 184 ? -13.61014 25.23449  36.06291  1.000 105.05426 ?  184 ALA B O   1 
ATOM 3375 C CB  . ALA B 1 184 ? -16.24266 24.34363  38.01227  1.000 110.29573 ?  184 ALA B CB  1 
ATOM 3376 N N   . ASP B 1 185 ? -13.30854 25.15512  38.29568  1.000 106.51447 ?  185 ASP B N   1 
ATOM 3377 C CA  . ASP B 1 185 ? -12.19585 26.10068  38.27563  1.000 100.39967 ?  185 ASP B CA  1 
ATOM 3378 C C   . ASP B 1 185 ? -11.09277 25.65516  37.32466  1.000 104.75752 ?  185 ASP B C   1 
ATOM 3379 O O   . ASP B 1 185 ? -10.55774 26.46860  36.56117  1.000 108.98509 ?  185 ASP B O   1 
ATOM 3380 C CB  . ASP B 1 185 ? -11.64339 26.29158  39.68895  1.000 112.92103 ?  185 ASP B CB  1 
ATOM 3381 C CG  . ASP B 1 185 ? -12.47501 27.26389  40.51696  1.000 140.40832 ?  185 ASP B CG  1 
ATOM 3382 O OD1 . ASP B 1 185 ? -13.50291 27.76158  40.00222  1.000 135.96180 ?  185 ASP B OD1 1 
ATOM 3383 O OD2 . ASP B 1 185 ? -12.09293 27.54020  41.67745  1.000 139.78423 -1 185 ASP B OD2 1 
ATOM 3384 N N   . ALA B 1 186 ? -10.73703 24.36608  37.35792  1.000 107.78363 ?  186 ALA B N   1 
ATOM 3385 C CA  . ALA B 1 186 ? -9.67440  23.86715  36.48828  1.000 101.80132 ?  186 ALA B CA  1 
ATOM 3386 C C   . ALA B 1 186 ? -9.99481  24.09990  35.01542  1.000 99.27797  ?  186 ALA B C   1 
ATOM 3387 O O   . ALA B 1 186 ? -9.12843  24.53286  34.24895  1.000 104.94545 ?  186 ALA B O   1 
ATOM 3388 C CB  . ALA B 1 186 ? -9.43307  22.38197  36.74999  1.000 100.19992 ?  186 ALA B CB  1 
ATOM 3389 N N   . PHE B 1 187 ? -11.22599 23.81945  34.59709  1.000 99.80406  ?  187 PHE B N   1 
ATOM 3390 C CA  . PHE B 1 187 ? -11.61044 24.04342  33.20824  1.000 104.42319 ?  187 PHE B CA  1 
ATOM 3391 C C   . PHE B 1 187 ? -12.00288 25.49111  32.91647  1.000 117.76991 ?  187 PHE B C   1 
ATOM 3392 O O   . PHE B 1 187 ? -12.43583 25.78093  31.79447  1.000 113.09795 ?  187 PHE B O   1 
ATOM 3393 C CB  . PHE B 1 187 ? -12.75014 23.09578  32.82371  1.000 98.47108  ?  187 PHE B CB  1 
ATOM 3394 C CG  . PHE B 1 187 ? -12.32503 21.65866  32.71125  1.000 94.07544  ?  187 PHE B CG  1 
ATOM 3395 C CD1 . PHE B 1 187 ? -12.29535 20.84244  33.83047  1.000 99.87602  ?  187 PHE B CD1 1 
ATOM 3396 C CD2 . PHE B 1 187 ? -11.92475 21.13002  31.49585  1.000 97.50586  ?  187 PHE B CD2 1 
ATOM 3397 C CE1 . PHE B 1 187 ? -11.89737 19.51724  33.73703  1.000 94.52963  ?  187 PHE B CE1 1 
ATOM 3398 C CE2 . PHE B 1 187 ? -11.52201 19.80462  31.39589  1.000 94.88325  ?  187 PHE B CE2 1 
ATOM 3399 C CZ  . PHE B 1 187 ? -11.50971 18.99868  32.51896  1.000 85.44018  ?  187 PHE B CZ  1 
ATOM 3400 N N   . ASN B 1 188 ? -11.85450 26.39619  33.88695  1.000 136.54814 ?  188 ASN B N   1 
ATOM 3401 C CA  . ASN B 1 188 ? -12.16447 27.82098  33.72396  1.000 135.07116 ?  188 ASN B CA  1 
ATOM 3402 C C   . ASN B 1 188 ? -13.56943 28.03443  33.16523  1.000 135.25780 ?  188 ASN B C   1 
ATOM 3403 O O   . ASN B 1 188 ? -13.79098 28.81848  32.23894  1.000 132.53405 ?  188 ASN B O   1 
ATOM 3404 C CB  . ASN B 1 188 ? -11.11773 28.51810  32.85435  1.000 137.79750 ?  188 ASN B CB  1 
ATOM 3405 C CG  . ASN B 1 188 ? -9.72542  27.96312  33.06496  1.000 154.07196 ?  188 ASN B CG  1 
ATOM 3406 O OD1 . ASN B 1 188 ? -9.15986  28.07101  34.15620  1.000 152.65817 ?  188 ASN B OD1 1 
ATOM 3407 N ND2 . ASN B 1 188 ? -9.16413  27.35925  32.02062  1.000 156.14619 ?  188 ASN B ND2 1 
ATOM 3408 N N   . ALA B 1 189 ? -14.52585 27.31773  33.74640  1.000 114.96025 ?  189 ALA B N   1 
ATOM 3409 C CA  . ALA B 1 189 ? -15.93177 27.44702  33.39747  1.000 129.91970 ?  189 ALA B CA  1 
ATOM 3410 C C   . ALA B 1 189 ? -16.74540 27.33415  34.68372  1.000 127.42635 ?  189 ALA B C   1 
ATOM 3411 O O   . ALA B 1 189 ? -16.19626 27.27251  35.78846  1.000 126.73537 ?  189 ALA B O   1 
ATOM 3412 C CB  . ALA B 1 189 ? -16.32865 26.40417  32.34437  1.000 126.97247 ?  189 ALA B CB  1 
ATOM 3413 N N   . SER B 1 190 ? -18.06460 27.30921  34.54590  1.000 134.73116 ?  190 SER B N   1 
ATOM 3414 C CA  . SER B 1 190 ? -18.95796 27.27451  35.69322  1.000 135.74768 ?  190 SER B CA  1 
ATOM 3415 C C   . SER B 1 190 ? -19.40692 25.84815  35.98934  1.000 135.21551 ?  190 SER B C   1 
ATOM 3416 O O   . SER B 1 190 ? -19.43526 24.99006  35.10321  1.000 135.17258 ?  190 SER B O   1 
ATOM 3417 C CB  . SER B 1 190 ? -20.17465 28.17428  35.46097  1.000 138.53016 ?  190 SER B CB  1 
ATOM 3418 O OG  . SER B 1 190 ? -20.57072 28.15569  34.10009  1.000 143.45513 ?  190 SER B OG  1 
ATOM 3419 N N   . GLU B 1 191 ? -19.74074 25.60827  37.26286  1.000 119.62405 ?  191 GLU B N   1 
ATOM 3420 C CA  . GLU B 1 191 ? -20.22550 24.30165  37.70567  1.000 123.77012 ?  191 GLU B CA  1 
ATOM 3421 C C   . GLU B 1 191 ? -21.30798 23.75566  36.77782  1.000 119.04995 ?  191 GLU B C   1 
ATOM 3422 O O   . GLU B 1 191 ? -21.24269 22.60064  36.34853  1.000 117.89698 ?  191 GLU B O   1 
ATOM 3423 C CB  . GLU B 1 191 ? -20.74845 24.40445  39.14274  1.000 121.69340 ?  191 GLU B CB  1 
ATOM 3424 C CG  . GLU B 1 191 ? -19.67621 24.36254  40.22655  1.000 116.62838 ?  191 GLU B CG  1 
ATOM 3425 C CD  . GLU B 1 191 ? -20.19667 23.80870  41.54834  1.000 124.35000 ?  191 GLU B CD  1 
ATOM 3426 O OE1 . GLU B 1 191 ? -21.41864 23.57136  41.65308  1.000 125.17475 ?  191 GLU B OE1 1 
ATOM 3427 O OE2 . GLU B 1 191 ? -19.38923 23.61348  42.48539  1.000 122.68781 -1 191 GLU B OE2 1 
ATOM 3428 N N   . ILE B 1 192 ? -22.33075 24.56808  36.49182  1.000 118.50931 ?  192 ILE B N   1 
ATOM 3429 C CA  . ILE B 1 192 ? -23.41916 24.15682  35.60242  1.000 115.64418 ?  192 ILE B CA  1 
ATOM 3430 C C   . ILE B 1 192 ? -22.86738 23.59666  34.29731  1.000 112.14480 ?  192 ILE B C   1 
ATOM 3431 O O   . ILE B 1 192 ? -23.28031 22.52703  33.82840  1.000 104.22540 ?  192 ILE B O   1 
ATOM 3432 C CB  . ILE B 1 192 ? -24.36620 25.34547  35.34095  1.000 124.69184 ?  192 ILE B CB  1 
ATOM 3433 C CG1 . ILE B 1 192 ? -25.35100 25.03716  34.20853  1.000 110.31540 ?  192 ILE B CG1 1 
ATOM 3434 C CG2 . ILE B 1 192 ? -23.57692 26.62689  35.03243  1.000 118.14777 ?  192 ILE B CG2 1 
ATOM 3435 C CD1 . ILE B 1 192 ? -26.45127 24.09147  34.59432  1.000 93.76650  ?  192 ILE B CD1 1 
ATOM 3436 N N   . THR B 1 193 ? -21.93518 24.32928  33.68520  1.000 114.23405 ?  193 THR B N   1 
ATOM 3437 C CA  . THR B 1 193 ? -21.38981 23.92936  32.39409  1.000 111.51127 ?  193 THR B CA  1 
ATOM 3438 C C   . THR B 1 193 ? -20.62928 22.60924  32.48434  1.000 115.02780 ?  193 THR B C   1 
ATOM 3439 O O   . THR B 1 193 ? -20.77797 21.74759  31.61210  1.000 110.25076 ?  193 THR B O   1 
ATOM 3440 C CB  . THR B 1 193 ? -20.50693 25.05050  31.83754  1.000 117.22231 ?  193 THR B CB  1 
ATOM 3441 O OG1 . THR B 1 193 ? -19.41459 25.30366  32.73237  1.000 110.92571 ?  193 THR B OG1 1 
ATOM 3442 C CG2 . THR B 1 193 ? -21.31965 26.32799  31.64727  1.000 120.89933 ?  193 THR B CG2 1 
ATOM 3443 N N   . ILE B 1 194 ? -19.80007 22.43482  33.51890  1.000 115.24850 ?  194 ILE B N   1 
ATOM 3444 C CA  . ILE B 1 194 ? -19.07652 21.17359  33.68815  1.000 102.10868 ?  194 ILE B CA  1 
ATOM 3445 C C   . ILE B 1 194 ? -20.05391 20.01786  33.88741  1.000 110.15658 ?  194 ILE B C   1 
ATOM 3446 O O   . ILE B 1 194 ? -19.91701 18.95373  33.27040  1.000 111.41273 ?  194 ILE B O   1 
ATOM 3447 C CB  . ILE B 1 194 ? -18.07173 21.27222  34.85380  1.000 103.55772 ?  194 ILE B CB  1 
ATOM 3448 C CG1 . ILE B 1 194 ? -16.74665 21.87571  34.38468  1.000 104.60068 ?  194 ILE B CG1 1 
ATOM 3449 C CG2 . ILE B 1 194 ? -17.79747 19.90035  35.45215  1.000 101.05006 ?  194 ILE B CG2 1 
ATOM 3450 C CD1 . ILE B 1 194 ? -16.77822 23.36765  34.18612  1.000 113.67473 ?  194 ILE B CD1 1 
ATOM 3451 N N   . ARG B 1 195 ? -21.04484 20.20665  34.76889  1.000 110.91286 ?  195 ARG B N   1 
ATOM 3452 C CA  . ARG B 1 195 ? -22.04850 19.17218  35.02054  1.000 107.04552 ?  195 ARG B CA  1 
ATOM 3453 C C   . ARG B 1 195 ? -22.77667 18.76590  33.75499  1.000 106.39628 ?  195 ARG B C   1 
ATOM 3454 O O   . ARG B 1 195 ? -23.02672 17.57947  33.52955  1.000 112.89610 ?  195 ARG B O   1 
ATOM 3455 C CB  . ARG B 1 195 ? -23.08231 19.66159  36.02673  1.000 110.78472 ?  195 ARG B CB  1 
ATOM 3456 C CG  . ARG B 1 195 ? -22.51965 19.99780  37.34976  1.000 123.53766 ?  195 ARG B CG  1 
ATOM 3457 C CD  . ARG B 1 195 ? -23.56649 20.58114  38.28624  1.000 135.09859 ?  195 ARG B CD  1 
ATOM 3458 N NE  . ARG B 1 195 ? -24.57079 19.60715  38.69172  1.000 139.90874 ?  195 ARG B NE  1 
ATOM 3459 C CZ  . ARG B 1 195 ? -25.58506 19.88358  39.49847  1.000 138.93312 ?  195 ARG B CZ  1 
ATOM 3460 N NH1 . ARG B 1 195 ? -25.76760 21.10119  39.98418  1.000 137.62281 ?  195 ARG B NH1 1 
ATOM 3461 N NH2 . ARG B 1 195 ? -26.43232 18.91383  39.83223  1.000 140.80067 ?  195 ARG B NH2 1 
ATOM 3462 N N   . LYS B 1 196 ? -23.14418 19.73577  32.92529  1.000 103.30598 ?  196 LYS B N   1 
ATOM 3463 C CA  . LYS B 1 196 ? -23.92437 19.39480  31.74575  1.000 102.31713 ?  196 LYS B CA  1 
ATOM 3464 C C   . LYS B 1 196 ? -23.05484 18.82348  30.63533  1.000 108.07423 ?  196 LYS B C   1 
ATOM 3465 O O   . LYS B 1 196 ? -23.46948 17.88061  29.95258  1.000 122.18929 ?  196 LYS B O   1 
ATOM 3466 C CB  . LYS B 1 196 ? -24.71035 20.61430  31.27546  1.000 123.12918 ?  196 LYS B CB  1 
ATOM 3467 C CG  . LYS B 1 196 ? -25.81007 20.96409  32.26162  1.000 123.27943 ?  196 LYS B CG  1 
ATOM 3468 C CD  . LYS B 1 196 ? -26.94634 21.71698  31.62674  1.000 113.42107 ?  196 LYS B CD  1 
ATOM 3469 C CE  . LYS B 1 196 ? -28.25886 21.26429  32.24151  1.000 124.41007 ?  196 LYS B CE  1 
ATOM 3470 N NZ  . LYS B 1 196 ? -28.38810 21.63068  33.67555  1.000 124.26852 ?  196 LYS B NZ  1 
ATOM 3471 N N   . ARG B 1 197 ? -21.86175 19.38912  30.42055  1.000 100.79336 ?  197 ARG B N   1 
ATOM 3472 C CA  . ARG B 1 197 ? -20.93258 18.80650  29.46146  1.000 95.63229  ?  197 ARG B CA  1 
ATOM 3473 C C   . ARG B 1 197 ? -20.60135 17.37100  29.84141  1.000 106.88814 ?  197 ARG B C   1 
ATOM 3474 O O   . ARG B 1 197 ? -20.41794 16.52475  28.96190  1.000 112.97508 ?  197 ARG B O   1 
ATOM 3475 C CB  . ARG B 1 197 ? -19.65974 19.65198  29.37003  1.000 106.24111 ?  197 ARG B CB  1 
ATOM 3476 C CG  . ARG B 1 197 ? -19.19157 19.91411  27.92815  1.000 123.83118 ?  197 ARG B CG  1 
ATOM 3477 C CD  . ARG B 1 197 ? -17.83108 20.61626  27.85860  1.000 112.47924 ?  197 ARG B CD  1 
ATOM 3478 N NE  . ARG B 1 197 ? -17.46616 20.99968  26.49582  1.000 128.55425 ?  197 ARG B NE  1 
ATOM 3479 C CZ  . ARG B 1 197 ? -16.87933 20.20761  25.60638  1.000 127.81882 ?  197 ARG B CZ  1 
ATOM 3480 N NH1 . ARG B 1 197 ? -16.65006 18.92981  25.86017  1.000 129.07297 ?  197 ARG B NH1 1 
ATOM 3481 N NH2 . ARG B 1 197 ? -16.52519 20.70848  24.42512  1.000 125.62513 ?  197 ARG B NH2 1 
ATOM 3482 N N   . LEU B 1 198 ? -20.54621 17.07493  31.14498  1.000 111.75871 ?  198 LEU B N   1 
ATOM 3483 C CA  . LEU B 1 198 ? -20.35196 15.70280  31.59650  1.000 107.04258 ?  198 LEU B CA  1 
ATOM 3484 C C   . LEU B 1 198 ? -21.61374 14.87878  31.35215  1.000 115.96894 ?  198 LEU B C   1 
ATOM 3485 O O   . LEU B 1 198 ? -21.53823 13.72950  30.90428  1.000 125.85281 ?  198 LEU B O   1 
ATOM 3486 C CB  . LEU B 1 198 ? -19.97407 15.70510  33.07737  1.000 102.01006 ?  198 LEU B CB  1 
ATOM 3487 C CG  . LEU B 1 198 ? -18.49594 15.94788  33.41685  1.000 100.91496 ?  198 LEU B CG  1 
ATOM 3488 C CD1 . LEU B 1 198 ? -18.25805 15.85793  34.91627  1.000 93.58643  ?  198 LEU B CD1 1 
ATOM 3489 C CD2 . LEU B 1 198 ? -17.56086 15.02122  32.66120  1.000 95.62273  ?  198 LEU B CD2 1 
ATOM 3490 N N   . GLU B 1 199 ? -22.78115 15.45535  31.65402  1.000 106.74755 ?  199 GLU B N   1 
ATOM 3491 C CA  . GLU B 1 199 ? -24.06150 14.77868  31.46333  1.000 121.38765 ?  199 GLU B CA  1 
ATOM 3492 C C   . GLU B 1 199 ? -24.32576 14.45605  29.99624  1.000 123.50036 ?  199 GLU B C   1 
ATOM 3493 O O   . GLU B 1 199 ? -25.08003 13.52347  29.69411  1.000 111.47459 ?  199 GLU B O   1 
ATOM 3494 C CB  . GLU B 1 199 ? -25.19612 15.64417  32.01393  1.000 125.13248 ?  199 GLU B CB  1 
ATOM 3495 C CG  . GLU B 1 199 ? -25.37279 15.58785  33.52216  1.000 131.92071 ?  199 GLU B CG  1 
ATOM 3496 C CD  . GLU B 1 199 ? -26.46909 16.52238  34.00560  1.000 140.88751 ?  199 GLU B CD  1 
ATOM 3497 O OE1 . GLU B 1 199 ? -27.00804 17.28313  33.17339  1.000 124.79468 ?  199 GLU B OE1 1 
ATOM 3498 O OE2 . GLU B 1 199 ? -26.78574 16.50449  35.21501  1.000 151.64129 -1 199 GLU B OE2 1 
ATOM 3499 N N   . SER B 1 200 ? -23.77729 15.25638  29.07641  1.000 124.54524 ?  200 SER B N   1 
ATOM 3500 C CA  . SER B 1 200 ? -23.96865 14.99589  27.65176  1.000 115.81440 ?  200 SER B CA  1 
ATOM 3501 C C   . SER B 1 200 ? -23.47058 13.60427  27.27031  1.000 127.17587 ?  200 SER B C   1 
ATOM 3502 O O   . SER B 1 200 ? -24.05443 12.94888  26.39950  1.000 139.98466 ?  200 SER B O   1 
ATOM 3503 C CB  . SER B 1 200 ? -23.27507 16.07422  26.82120  1.000 110.49826 ?  200 SER B CB  1 
ATOM 3504 O OG  . SER B 1 200 ? -21.91097 15.75986  26.61742  1.000 126.78824 ?  200 SER B OG  1 
ATOM 3505 N N   . GLU B 1 201 ? -22.39109 13.13292  27.90563  1.000 117.66356 ?  201 GLU B N   1 
ATOM 3506 C CA  . GLU B 1 201 ? -21.92852 11.75992  27.72083  1.000 120.96819 ?  201 GLU B CA  1 
ATOM 3507 C C   . GLU B 1 201 ? -22.46720 10.82495  28.79522  1.000 118.46186 ?  201 GLU B C   1 
ATOM 3508 O O   . GLU B 1 201 ? -21.83494 9.80307   29.09888  1.000 122.93382 ?  201 GLU B O   1 
ATOM 3509 C CB  . GLU B 1 201 ? -20.39796 11.68304  27.68226  1.000 120.37903 ?  201 GLU B CB  1 
ATOM 3510 C CG  . GLU B 1 201 ? -19.73406 12.31005  26.46788  1.000 117.50243 ?  201 GLU B CG  1 
ATOM 3511 C CD  . GLU B 1 201 ? -19.32070 13.74182  26.70159  1.000 126.03658 ?  201 GLU B CD  1 
ATOM 3512 O OE1 . GLU B 1 201 ? -19.47434 14.21677  27.84178  1.000 133.43785 ?  201 GLU B OE1 1 
ATOM 3513 O OE2 . GLU B 1 201 ? -18.84032 14.39269  25.74976  1.000 143.88588 -1 201 GLU B OE2 1 
ATOM 3514 N N   . ASN B 1 202 ? -23.61909 11.15836  29.37580  1.000 118.33617 ?  202 ASN B N   1 
ATOM 3515 C CA  . ASN B 1 202 ? -24.31709 10.32227  30.35111  1.000 120.04453 ?  202 ASN B CA  1 
ATOM 3516 C C   . ASN B 1 202 ? -23.39388 9.94867   31.51340  1.000 127.47948 ?  202 ASN B C   1 
ATOM 3517 O O   . ASN B 1 202 ? -23.21912 8.77897   31.86314  1.000 127.45817 ?  202 ASN B O   1 
ATOM 3518 C CB  . ASN B 1 202 ? -24.89175 9.07701   29.66799  1.000 124.63146 ?  202 ASN B CB  1 
ATOM 3519 C CG  . ASN B 1 202 ? -26.09276 8.50260   30.39799  1.000 121.48866 ?  202 ASN B CG  1 
ATOM 3520 O OD1 . ASN B 1 202 ? -25.97033 7.55918   31.18077  1.000 113.42805 ?  202 ASN B OD1 1 
ATOM 3521 N ND2 . ASN B 1 202 ? -27.26866 9.06085   30.12677  1.000 119.40904 ?  202 ASN B ND2 1 
ATOM 3522 N N   . THR B 1 203 ? -22.81690 10.98218  32.12794  1.000 132.45019 ?  203 THR B N   1 
ATOM 3523 C CA  . THR B 1 203 ? -21.92019 10.81329  33.26206  1.000 130.23341 ?  203 THR B CA  1 
ATOM 3524 C C   . THR B 1 203 ? -22.12152 11.95853  34.24012  1.000 124.11669 ?  203 THR B C   1 
ATOM 3525 O O   . THR B 1 203 ? -22.65789 13.01744  33.90399  1.000 121.88823 ?  203 THR B O   1 
ATOM 3526 C CB  . THR B 1 203 ? -20.43461 10.78078  32.85678  1.000 129.89278 ?  203 THR B CB  1 
ATOM 3527 O OG1 . THR B 1 203 ? -20.16239 11.83587  31.92585  1.000 139.90928 ?  203 THR B OG1 1 
ATOM 3528 C CG2 . THR B 1 203 ? -20.06636 9.44787   32.23256  1.000 128.97734 ?  203 THR B CG2 1 
ATOM 3529 N N   . ASN B 1 204 ? -21.68027 11.72225  35.46239  1.000 105.10952 ?  204 ASN B N   1 
ATOM 3530 C CA  . ASN B 1 204 ? -21.61531 12.74177  36.48876  1.000 100.94518 ?  204 ASN B CA  1 
ATOM 3531 C C   . ASN B 1 204 ? -20.24747 12.63010  37.14355  1.000 106.84502 ?  204 ASN B C   1 
ATOM 3532 O O   . ASN B 1 204 ? -19.63874 11.55729  37.14026  1.000 107.21109 ?  204 ASN B O   1 
ATOM 3533 C CB  . ASN B 1 204 ? -22.72446 12.56450  37.51382  1.000 70.09337  ?  204 ASN B CB  1 
ATOM 3534 C CG  . ASN B 1 204 ? -22.75046 11.16980  38.09289  1.000 96.23955  ?  204 ASN B CG  1 
ATOM 3535 O OD1 . ASN B 1 204 ? -22.03002 10.88745  39.04739  1.000 106.10464 ?  204 ASN B OD1 1 
ATOM 3536 N ND2 . ASN B 1 204 ? -23.58985 10.29159  37.53495  1.000 95.51181  ?  204 ASN B ND2 1 
ATOM 3537 N N   . PHE B 1 205 ? -19.75906 13.75088  37.68218  1.000 98.39414  ?  205 PHE B N   1 
ATOM 3538 C CA  . PHE B 1 205 ? -18.42792 13.79213  38.28903  1.000 98.11340  ?  205 PHE B CA  1 
ATOM 3539 C C   . PHE B 1 205 ? -18.22668 12.67216  39.31277  1.000 90.58422  ?  205 PHE B C   1 
ATOM 3540 O O   . PHE B 1 205 ? -17.14436 12.06927  39.38779  1.000 91.07617  ?  205 PHE B O   1 
ATOM 3541 C CB  . PHE B 1 205 ? -18.21749 15.17501  38.91131  1.000 110.00970 ?  205 PHE B CB  1 
ATOM 3542 C CG  . PHE B 1 205 ? -17.16402 15.22361  39.97053  1.000 101.84151 ?  205 PHE B CG  1 
ATOM 3543 C CD1 . PHE B 1 205 ? -15.82026 15.29644  39.63691  1.000 99.46023  ?  205 PHE B CD1 1 
ATOM 3544 C CD2 . PHE B 1 205 ? -17.52437 15.21544  41.30711  1.000 101.13572 ?  205 PHE B CD2 1 
ATOM 3545 C CE1 . PHE B 1 205 ? -14.85305 15.35066  40.62365  1.000 106.93893 ?  205 PHE B CE1 1 
ATOM 3546 C CE2 . PHE B 1 205 ? -16.56945 15.26413  42.29434  1.000 112.95088 ?  205 PHE B CE2 1 
ATOM 3547 C CZ  . PHE B 1 205 ? -15.22884 15.33170  41.95549  1.000 114.77621 ?  205 PHE B CZ  1 
ATOM 3548 N N   . ASN B 1 206 ? -19.26317 12.37530  40.10394  1.000 91.95714  ?  206 ASN B N   1 
ATOM 3549 C CA  . ASN B 1 206 ? -19.17405 11.29285  41.08065  1.000 90.52104  ?  206 ASN B CA  1 
ATOM 3550 C C   . ASN B 1 206 ? -19.00538 9.93702   40.40290  1.000 88.08072  ?  206 ASN B C   1 
ATOM 3551 O O   . ASN B 1 206 ? -18.27180 9.07795   40.90465  1.000 80.23303  ?  206 ASN B O   1 
ATOM 3552 C CB  . ASN B 1 206 ? -20.40665 11.29824  41.97959  1.000 86.38716  ?  206 ASN B CB  1 
ATOM 3553 C CG  . ASN B 1 206 ? -20.65287 12.64989  42.61017  1.000 95.97953  ?  206 ASN B CG  1 
ATOM 3554 O OD1 . ASN B 1 206 ? -21.40187 13.47077  42.07936  1.000 116.33661 ?  206 ASN B OD1 1 
ATOM 3555 N ND2 . ASN B 1 206 ? -20.01191 12.89547  43.74482  1.000 81.09969  ?  206 ASN B ND2 1 
ATOM 3556 N N   . GLN B 1 207 ? -19.66195 9.72249   39.25844  1.000 79.17194  ?  207 GLN B N   1 
ATOM 3557 C CA  . GLN B 1 207 ? -19.45880 8.46361   38.54757  1.000 82.08334  ?  207 GLN B CA  1 
ATOM 3558 C C   . GLN B 1 207 ? -18.03754 8.36689   38.00970  1.000 81.94862  ?  207 GLN B C   1 
ATOM 3559 O O   . GLN B 1 207 ? -17.41512 7.30583   38.08518  1.000 76.31890  ?  207 GLN B O   1 
ATOM 3560 C CB  . GLN B 1 207 ? -20.46463 8.29378   37.40249  1.000 93.43270  ?  207 GLN B CB  1 
ATOM 3561 C CG  . GLN B 1 207 ? -20.29676 6.94712   36.65466  1.000 102.29585 ?  207 GLN B CG  1 
ATOM 3562 C CD  . GLN B 1 207 ? -20.96152 6.88704   35.27212  1.000 119.85012 ?  207 GLN B CD  1 
ATOM 3563 O OE1 . GLN B 1 207 ? -21.77632 7.74075   34.91029  1.000 116.71922 ?  207 GLN B OE1 1 
ATOM 3564 N NE2 . GLN B 1 207 ? -20.60756 5.86205   34.49623  1.000 106.00061 ?  207 GLN B NE2 1 
ATOM 3565 N N   . ILE B 1 208 ? -17.52040 9.45074   37.42972  1.000 77.66338  ?  208 ILE B N   1 
ATOM 3566 C CA  . ILE B 1 208 ? -16.14246 9.44516   36.94422  1.000 70.49316  ?  208 ILE B CA  1 
ATOM 3567 C C   . ILE B 1 208 ? -15.18731 9.05062   38.06475  1.000 70.79003  ?  208 ILE B C   1 
ATOM 3568 O O   . ILE B 1 208 ? -14.34145 8.16146   37.90221  1.000 78.09916  ?  208 ILE B O   1 
ATOM 3569 C CB  . ILE B 1 208 ? -15.78345 10.81422  36.33495  1.000 77.52792  ?  208 ILE B CB  1 
ATOM 3570 C CG1 . ILE B 1 208 ? -16.42414 10.94991  34.95487  1.000 77.06135  ?  208 ILE B CG1 1 
ATOM 3571 C CG2 . ILE B 1 208 ? -14.26785 11.00324  36.21742  1.000 72.17325  ?  208 ILE B CG2 1 
ATOM 3572 C CD1 . ILE B 1 208 ? -16.11986 12.25357  34.26876  1.000 79.02713  ?  208 ILE B CD1 1 
ATOM 3573 N N   . LEU B 1 209 ? -15.30487 9.71501   39.21658  1.000 71.09116  ?  209 LEU B N   1 
ATOM 3574 C CA  . LEU B 1 209 ? -14.40580 9.43831   40.33804  1.000 77.36855  ?  209 LEU B CA  1 
ATOM 3575 C C   . LEU B 1 209 ? -14.56480 8.00431   40.85641  1.000 64.78152  ?  209 LEU B C   1 
ATOM 3576 O O   . LEU B 1 209 ? -13.57374 7.31542   41.14126  1.000 73.42960  ?  209 LEU B O   1 
ATOM 3577 C CB  . LEU B 1 209 ? -14.65034 10.46689  41.43555  1.000 71.82778  ?  209 LEU B CB  1 
ATOM 3578 C CG  . LEU B 1 209 ? -13.73037 10.47521  42.63766  1.000 74.98424  ?  209 LEU B CG  1 
ATOM 3579 C CD1 . LEU B 1 209 ? -13.57188 11.90551  43.08998  1.000 79.63914  ?  209 LEU B CD1 1 
ATOM 3580 C CD2 . LEU B 1 209 ? -14.36223 9.63337   43.72339  1.000 101.46043 ?  209 LEU B CD2 1 
ATOM 3581 N N   . MET B 1 210 ? -15.80858 7.54876   41.01775  1.000 61.94930  ?  210 MET B N   1 
ATOM 3582 C CA  . MET B 1 210 ? -16.05238 6.18054   41.46187  1.000 75.62591  ?  210 MET B CA  1 
ATOM 3583 C C   . MET B 1 210 ? -15.47090 5.16484   40.47732  1.000 64.97641  ?  210 MET B C   1 
ATOM 3584 O O   . MET B 1 210 ? -14.88605 4.15480   40.88348  1.000 56.18832  ?  210 MET B O   1 
ATOM 3585 C CB  . MET B 1 210 ? -17.56011 5.95614   41.63548  1.000 70.86713  ?  210 MET B CB  1 
ATOM 3586 C CG  . MET B 1 210 ? -17.93927 4.52285   41.97069  1.000 74.34360  ?  210 MET B CG  1 
ATOM 3587 S SD  . MET B 1 210 ? -17.91102 4.19799   43.73776  1.000 89.81443  ?  210 MET B SD  1 
ATOM 3588 C CE  . MET B 1 210 ? -19.14962 5.38035   44.28685  1.000 110.81385 ?  210 MET B CE  1 
ATOM 3589 N N   . GLN B 1 211 ? -15.63642 5.40717   39.17717  1.000 58.83271  ?  211 GLN B N   1 
ATOM 3590 C CA  . GLN B 1 211 ? -15.12554 4.48257   38.17367  1.000 60.68376  ?  211 GLN B CA  1 
ATOM 3591 C C   . GLN B 1 211 ? -13.60222 4.44570   38.18834  1.000 70.57421  ?  211 GLN B C   1 
ATOM 3592 O O   . GLN B 1 211 ? -12.99722 3.36990   38.12320  1.000 60.36515  ?  211 GLN B O   1 
ATOM 3593 C CB  . GLN B 1 211 ? -15.63866 4.88222   36.79491  1.000 57.77346  ?  211 GLN B CB  1 
ATOM 3594 C CG  . GLN B 1 211 ? -17.03385 4.40079   36.44143  1.000 83.97701  ?  211 GLN B CG  1 
ATOM 3595 C CD  . GLN B 1 211 ? -17.10457 2.91398   36.15678  1.000 87.31505  ?  211 GLN B CD  1 
ATOM 3596 O OE1 . GLN B 1 211 ? -16.16679 2.16631   36.43883  1.000 63.63426  ?  211 GLN B OE1 1 
ATOM 3597 N NE2 . GLN B 1 211 ? -18.21186 2.48285   35.55425  1.000 83.88806  ?  211 GLN B NE2 1 
ATOM 3598 N N   . LEU B 1 212 ? -12.96716 5.61872   38.26207  1.000 70.83894  ?  212 LEU B N   1 
ATOM 3599 C CA  . LEU B 1 212 ? -11.51423 5.68796   38.38126  1.000 61.00018  ?  212 LEU B CA  1 
ATOM 3600 C C   . LEU B 1 212 ? -11.01820 4.83781   39.54102  1.000 74.43741  ?  212 LEU B C   1 
ATOM 3601 O O   . LEU B 1 212 ? -10.14692 3.96902   39.37574  1.000 77.69737  ?  212 LEU B O   1 
ATOM 3602 C CB  . LEU B 1 212 ? -11.09134 7.13853   38.58285  1.000 62.82131  ?  212 LEU B CB  1 
ATOM 3603 C CG  . LEU B 1 212 ? -10.55363 7.82534   37.34098  1.000 84.30484  ?  212 LEU B CG  1 
ATOM 3604 C CD1 . LEU B 1 212 ? -10.17982 9.26189   37.66495  1.000 84.47059  ?  212 LEU B CD1 1 
ATOM 3605 C CD2 . LEU B 1 212 ? -9.37373  7.03616   36.82138  1.000 78.97506  ?  212 LEU B CD2 1 
ATOM 3606 N N   . ARG B 1 213 ? -11.57955 5.07576   40.73037  1.000 77.93781  ?  213 ARG B N   1 
ATOM 3607 C CA  . ARG B 1 213 ? -11.09117 4.40063   41.92546  1.000 57.76452  ?  213 ARG B CA  1 
ATOM 3608 C C   . ARG B 1 213 ? -11.38550 2.90945   41.89068  1.000 60.24669  ?  213 ARG B C   1 
ATOM 3609 O O   . ARG B 1 213 ? -10.52437 2.10123   42.24921  1.000 71.66300  ?  213 ARG B O   1 
ATOM 3610 C CB  . ARG B 1 213 ? -11.70066 5.04870   43.15699  1.000 66.93703  ?  213 ARG B CB  1 
ATOM 3611 C CG  . ARG B 1 213 ? -11.24865 6.47956   43.30915  1.000 78.63754  ?  213 ARG B CG  1 
ATOM 3612 C CD  . ARG B 1 213 ? -11.74514 7.08353   44.58947  1.000 90.50158  ?  213 ARG B CD  1 
ATOM 3613 N NE  . ARG B 1 213 ? -11.13342 8.38429   44.80872  1.000 80.60502  ?  213 ARG B NE  1 
ATOM 3614 C CZ  . ARG B 1 213 ? -11.61539 9.29944   45.63370  1.000 81.92911  ?  213 ARG B CZ  1 
ATOM 3615 N NH1 . ARG B 1 213 ? -12.71169 9.07755   46.34476  1.000 68.03880  ?  213 ARG B NH1 1 
ATOM 3616 N NH2 . ARG B 1 213 ? -10.97310 10.45731  45.76106  1.000 78.00193  ?  213 ARG B NH2 1 
ATOM 3617 N N   . MET B 1 214 ? -12.57633 2.51734   41.42743  1.000 55.87694  ?  214 MET B N   1 
ATOM 3618 C CA  . MET B 1 214 ? -12.92124 1.10168   41.40979  1.000 54.42906  ?  214 MET B CA  1 
ATOM 3619 C C   . MET B 1 214 ? -12.15287 0.34430   40.33688  1.000 65.62435  ?  214 MET B C   1 
ATOM 3620 O O   . MET B 1 214 ? -11.81954 -0.82928  40.53675  1.000 65.59876  ?  214 MET B O   1 
ATOM 3621 C CB  . MET B 1 214 ? -14.42945 0.92043   41.22882  1.000 64.33859  ?  214 MET B CB  1 
ATOM 3622 C CG  . MET B 1 214 ? -15.24121 1.26075   42.47484  1.000 62.59982  ?  214 MET B CG  1 
ATOM 3623 S SD  . MET B 1 214 ? -14.57587 0.48581   43.97172  1.000 66.61936  ?  214 MET B SD  1 
ATOM 3624 C CE  . MET B 1 214 ? -14.18417 1.93893   44.94102  1.000 56.93369  ?  214 MET B CE  1 
ATOM 3625 N N   . SER B 1 215 ? -11.83077 0.99845   39.21427  1.000 71.29718  ?  215 SER B N   1 
ATOM 3626 C CA  . SER B 1 215 ? -11.03443 0.35800   38.17241  1.000 65.47962  ?  215 SER B CA  1 
ATOM 3627 C C   . SER B 1 215 ? -9.58592  0.17630   38.61730  1.000 62.34538  ?  215 SER B C   1 
ATOM 3628 O O   . SER B 1 215 ? -9.01514  -0.91928  38.48800  1.000 61.76639  ?  215 SER B O   1 
ATOM 3629 C CB  . SER B 1 215 ? -11.11242 1.18566   36.89047  1.000 61.42081  ?  215 SER B CB  1 
ATOM 3630 O OG  . SER B 1 215 ? -10.16316 0.74185   35.94071  1.000 96.76727  ?  215 SER B OG  1 
ATOM 3631 N N   . LYS B 1 216 ? -8.96747  1.24664   39.13091  1.000 60.80668  ?  216 LYS B N   1 
ATOM 3632 C CA  . LYS B 1 216 ? -7.63557  1.10621   39.70663  1.000 64.28750  ?  216 LYS B CA  1 
ATOM 3633 C C   . LYS B 1 216 ? -7.61640  0.02084   40.77716  1.000 66.98626  ?  216 LYS B C   1 
ATOM 3634 O O   . LYS B 1 216 ? -6.67333  -0.77721  40.84277  1.000 75.55900  ?  216 LYS B O   1 
ATOM 3635 C CB  . LYS B 1 216 ? -7.14860  2.44820   40.26068  1.000 54.50491  ?  216 LYS B CB  1 
ATOM 3636 C CG  . LYS B 1 216 ? -5.62168  2.58544   40.26475  1.000 73.47326  ?  216 LYS B CG  1 
ATOM 3637 C CD  . LYS B 1 216 ? -5.00235  2.21945   38.89799  1.000 97.86718  ?  216 LYS B CD  1 
ATOM 3638 C CE  . LYS B 1 216 ? -3.54949  1.70421   39.03455  1.000 88.49613  ?  216 LYS B CE  1 
ATOM 3639 N NZ  . LYS B 1 216 ? -2.97044  1.08207   37.78460  1.000 60.34061  ?  216 LYS B NZ  1 
ATOM 3640 N N   . ALA B 1 217 ? -8.66251  -0.04123  41.60941  1.000 82.04566  ?  217 ALA B N   1 
ATOM 3641 C CA  . ALA B 1 217 ? -8.72569  -1.05519  42.65708  1.000 82.08471  ?  217 ALA B CA  1 
ATOM 3642 C C   . ALA B 1 217 ? -8.81053  -2.46103  42.07833  1.000 83.25085  ?  217 ALA B C   1 
ATOM 3643 O O   . ALA B 1 217 ? -8.17293  -3.38453  42.59162  1.000 89.43606  ?  217 ALA B O   1 
ATOM 3644 C CB  . ALA B 1 217 ? -9.91626  -0.79303  43.57469  1.000 81.66389  ?  217 ALA B CB  1 
ATOM 3645 N N   . ALA B 1 218 ? -9.62315  -2.65578  41.03888  1.000 66.79221  ?  218 ALA B N   1 
ATOM 3646 C CA  . ALA B 1 218 ? -9.72365  -3.97542  40.42247  1.000 67.38477  ?  218 ALA B CA  1 
ATOM 3647 C C   . ALA B 1 218 ? -8.37457  -4.43508  39.87626  1.000 86.61475  ?  218 ALA B C   1 
ATOM 3648 O O   . ALA B 1 218 ? -7.95849  -5.58538  40.09373  1.000 90.22309  ?  218 ALA B O   1 
ATOM 3649 C CB  . ALA B 1 218 ? -10.77961 -3.95371  39.32063  1.000 63.71445  ?  218 ALA B CB  1 
ATOM 3650 N N   . LEU B 1 219 ? -7.68141  -3.54792  39.14877  1.000 90.48766  ?  219 LEU B N   1 
ATOM 3651 C CA  . LEU B 1 219 ? -6.35336  -3.88956  38.63233  1.000 76.99312  ?  219 LEU B CA  1 
ATOM 3652 C C   . LEU B 1 219 ? -5.39426  -4.24311  39.76950  1.000 70.56949  ?  219 LEU B C   1 
ATOM 3653 O O   . LEU B 1 219 ? -4.74952  -5.30040  39.74689  1.000 66.20504  ?  219 LEU B O   1 
ATOM 3654 C CB  . LEU B 1 219 ? -5.79251  -2.74071  37.78775  1.000 68.61579  ?  219 LEU B CB  1 
ATOM 3655 C CG  . LEU B 1 219 ? -6.56583  -2.27305  36.54572  1.000 63.21543  ?  219 LEU B CG  1 
ATOM 3656 C CD1 . LEU B 1 219 ? -5.97782  -0.97354  35.98959  1.000 66.99915  ?  219 LEU B CD1 1 
ATOM 3657 C CD2 . LEU B 1 219 ? -6.61399  -3.34866  35.46313  1.000 59.20493  ?  219 LEU B CD2 1 
ATOM 3658 N N   . LEU B 1 220 ? -5.29130  -3.36353  40.77662  1.000 73.74327  ?  220 LEU B N   1 
ATOM 3659 C CA  . LEU B 1 220 ? -4.38925  -3.60182  41.90510  1.000 79.50760  ?  220 LEU B CA  1 
ATOM 3660 C C   . LEU B 1 220 ? -4.70595  -4.91394  42.60544  1.000 76.38625  ?  220 LEU B C   1 
ATOM 3661 O O   . LEU B 1 220 ? -3.79781  -5.64745  43.01343  1.000 83.81064  ?  220 LEU B O   1 
ATOM 3662 C CB  . LEU B 1 220 ? -4.47868  -2.44310  42.89972  1.000 68.68622  ?  220 LEU B CB  1 
ATOM 3663 C CG  . LEU B 1 220 ? -3.88977  -1.11572  42.42870  1.000 63.98642  ?  220 LEU B CG  1 
ATOM 3664 C CD1 . LEU B 1 220 ? -4.36809  0.02989   43.30376  1.000 56.21606  ?  220 LEU B CD1 1 
ATOM 3665 C CD2 . LEU B 1 220 ? -2.37431  -1.20056  42.42169  1.000 68.59059  ?  220 LEU B CD2 1 
ATOM 3666 N N   . LEU B 1 221 ? -5.99190  -5.21629  42.76420  1.000 82.69764  ?  221 LEU B N   1 
ATOM 3667 C CA  . LEU B 1 221 ? -6.40725  -6.46707  43.38184  1.000 88.99333  ?  221 LEU B CA  1 
ATOM 3668 C C   . LEU B 1 221 ? -5.90410  -7.65983  42.57953  1.000 85.23513  ?  221 LEU B C   1 
ATOM 3669 O O   . LEU B 1 221 ? -5.32839  -8.60000  43.13734  1.000 94.82535  ?  221 LEU B O   1 
ATOM 3670 C CB  . LEU B 1 221 ? -7.93044  -6.48865  43.50235  1.000 82.74996  ?  221 LEU B CB  1 
ATOM 3671 C CG  . LEU B 1 221 ? -8.58801  -7.66477  44.20965  1.000 82.68116  ?  221 LEU B CG  1 
ATOM 3672 C CD1 . LEU B 1 221 ? -8.26310  -7.64912  45.69317  1.000 67.48188  ?  221 LEU B CD1 1 
ATOM 3673 C CD2 . LEU B 1 221 ? -10.07866 -7.61466  43.96916  1.000 89.33308  ?  221 LEU B CD2 1 
ATOM 3674 N N   . LEU B 1 222 ? -6.11735  -7.64105  41.26060  1.000 89.00143  ?  222 LEU B N   1 
ATOM 3675 C CA  . LEU B 1 222 ? -5.65823  -8.75560  40.43544  1.000 85.77895  ?  222 LEU B CA  1 
ATOM 3676 C C   . LEU B 1 222 ? -4.14149  -8.85521  40.36637  1.000 90.78787  ?  222 LEU B C   1 
ATOM 3677 O O   . LEU B 1 222 ? -3.62476  -9.92618  40.03384  1.000 95.95514  ?  222 LEU B O   1 
ATOM 3678 C CB  . LEU B 1 222 ? -6.22573  -8.64559  39.02334  1.000 85.49283  ?  222 LEU B CB  1 
ATOM 3679 C CG  . LEU B 1 222 ? -7.68202  -9.07848  38.89604  1.000 93.04660  ?  222 LEU B CG  1 
ATOM 3680 C CD1 . LEU B 1 222 ? -8.08287  -9.12531  37.43793  1.000 105.02899 ?  222 LEU B CD1 1 
ATOM 3681 C CD2 . LEU B 1 222 ? -7.86195  -10.44132 39.54478  1.000 92.69185  ?  222 LEU B CD2 1 
ATOM 3682 N N   . GLU B 1 223 ? -3.41530  -7.77818  40.67935  1.000 99.01574  ?  223 GLU B N   1 
ATOM 3683 C CA  . GLU B 1 223 ? -1.95821  -7.86074  40.66142  1.000 85.39120  ?  223 GLU B CA  1 
ATOM 3684 C C   . GLU B 1 223 ? -1.40945  -8.82268  41.70101  1.000 84.82760  ?  223 GLU B C   1 
ATOM 3685 O O   . GLU B 1 223 ? -0.25546  -9.24518  41.57796  1.000 88.62315  ?  223 GLU B O   1 
ATOM 3686 C CB  . GLU B 1 223 ? -1.33374  -6.49210  40.88444  1.000 83.10932  ?  223 GLU B CB  1 
ATOM 3687 C CG  . GLU B 1 223 ? -1.50612  -5.56615  39.72085  1.000 87.29727  ?  223 GLU B CG  1 
ATOM 3688 C CD  . GLU B 1 223 ? -0.54503  -4.41438  39.78100  1.000 94.79380  ?  223 GLU B CD  1 
ATOM 3689 O OE1 . GLU B 1 223 ? 0.31043   -4.40634  40.69536  1.000 90.53022  ?  223 GLU B OE1 1 
ATOM 3690 O OE2 . GLU B 1 223 ? -0.65421  -3.51594  38.92211  1.000 106.33689 -1 223 GLU B OE2 1 
ATOM 3691 N N   . ASN B 1 224 ? -2.19891  -9.17786  42.71475  1.000 83.30590  ?  224 ASN B N   1 
ATOM 3692 C CA  . ASN B 1 224 ? -1.78331  -10.10945 43.76327  1.000 90.87152  ?  224 ASN B CA  1 
ATOM 3693 C C   . ASN B 1 224 ? -0.53972  -9.63920  44.52276  1.000 87.91203  ?  224 ASN B C   1 
ATOM 3694 O O   . ASN B 1 224 ? 0.15401   -10.44573 45.14430  1.000 74.98606  ?  224 ASN B O   1 
ATOM 3695 C CB  . ASN B 1 224 ? -1.55177  -11.50803 43.17755  1.000 83.83999  ?  224 ASN B CB  1 
ATOM 3696 C CG  . ASN B 1 224 ? -1.53529  -12.58432 44.22980  1.000 84.42769  ?  224 ASN B CG  1 
ATOM 3697 O OD1 . ASN B 1 224 ? -1.97488  -12.37043 45.35800  1.000 88.74218  ?  224 ASN B OD1 1 
ATOM 3698 N ND2 . ASN B 1 224 ? -1.00964  -13.75093 43.87184  1.000 97.10179  ?  224 ASN B ND2 1 
ATOM 3699 N N   . SER B 1 225 ? -0.24413  -8.33981  44.50280  1.000 92.69669  ?  225 SER B N   1 
ATOM 3700 C CA  . SER B 1 225 ? 0.91851   -7.79785  45.19697  1.000 84.60216  ?  225 SER B CA  1 
ATOM 3701 C C   . SER B 1 225 ? 0.53884   -6.83668  46.31798  1.000 90.00597  ?  225 SER B C   1 
ATOM 3702 O O   . SER B 1 225 ? 1.42733   -6.18290  46.88010  1.000 90.12291  ?  225 SER B O   1 
ATOM 3703 C CB  . SER B 1 225 ? 1.86155   -7.08553  44.21486  1.000 83.14437  ?  225 SER B CB  1 
ATOM 3704 O OG  . SER B 1 225 ? 2.42030   -7.97295  43.26036  1.000 90.08012  ?  225 SER B OG  1 
ATOM 3705 N N   . TYR B 1 226 ? -0.74653  -6.70566  46.64585  1.000 83.46547  ?  226 TYR B N   1 
ATOM 3706 C CA  . TYR B 1 226 ? -1.15837  -5.66778  47.57974  1.000 85.73573  ?  226 TYR B CA  1 
ATOM 3707 C C   . TYR B 1 226 ? -2.32834  -6.12963  48.43713  1.000 82.84831  ?  226 TYR B C   1 
ATOM 3708 O O   . TYR B 1 226 ? -3.19444  -6.87260  47.97238  1.000 78.45314  ?  226 TYR B O   1 
ATOM 3709 C CB  . TYR B 1 226 ? -1.53214  -4.38246  46.83370  1.000 74.26038  ?  226 TYR B CB  1 
ATOM 3710 C CG  . TYR B 1 226 ? -0.37367  -3.76341  46.09666  1.000 80.12552  ?  226 TYR B CG  1 
ATOM 3711 C CD1 . TYR B 1 226 ? 0.63970   -3.09526  46.79021  1.000 85.34431  ?  226 TYR B CD1 1 
ATOM 3712 C CD2 . TYR B 1 226 ? -0.28911  -3.83482  44.71110  1.000 63.42017  ?  226 TYR B CD2 1 
ATOM 3713 C CE1 . TYR B 1 226 ? 1.71038   -2.52390  46.12525  1.000 59.38116  ?  226 TYR B CE1 1 
ATOM 3714 C CE2 . TYR B 1 226 ? 0.77671   -3.26440  44.03221  1.000 65.95466  ?  226 TYR B CE2 1 
ATOM 3715 C CZ  . TYR B 1 226 ? 1.77245   -2.61044  44.74309  1.000 74.85901  ?  226 TYR B CZ  1 
ATOM 3716 O OH  . TYR B 1 226 ? 2.83060   -2.04148  44.06965  1.000 69.55816  ?  226 TYR B OH  1 
ATOM 3717 N N   . GLN B 1 227 ? -2.33588  -5.68906  49.69397  1.000 87.76013  ?  227 GLN B N   1 
ATOM 3718 C CA  . GLN B 1 227 ? -3.44115  -5.93512  50.60882  1.000 92.48822  ?  227 GLN B CA  1 
ATOM 3719 C C   . GLN B 1 227 ? -4.58069  -4.95323  50.36056  1.000 87.44039  ?  227 GLN B C   1 
ATOM 3720 O O   . GLN B 1 227 ? -4.43228  -3.93724  49.67339  1.000 86.78002  ?  227 GLN B O   1 
ATOM 3721 C CB  . GLN B 1 227 ? -2.99379  -5.86035  52.06986  1.000 95.61733  ?  227 GLN B CB  1 
ATOM 3722 C CG  . GLN B 1 227 ? -2.21152  -7.06849  52.58599  1.000 111.75354 ?  227 GLN B CG  1 
ATOM 3723 C CD  . GLN B 1 227 ? -1.25410  -7.65831  51.57675  1.000 122.86314 ?  227 GLN B CD  1 
ATOM 3724 O OE1 . GLN B 1 227 ? -0.35988  -6.97305  51.08613  1.000 125.42917 ?  227 GLN B OE1 1 
ATOM 3725 N NE2 . GLN B 1 227 ? -1.43947  -8.93717  51.25496  1.000 118.34411 ?  227 GLN B NE2 1 
ATOM 3726 N N   . ILE B 1 228 ? -5.74336  -5.29320  50.92778  1.000 83.26924  ?  228 ILE B N   1 
ATOM 3727 C CA  . ILE B 1 228 ? -6.94302  -4.47378  50.77609  1.000 80.03321  ?  228 ILE B CA  1 
ATOM 3728 C C   . ILE B 1 228 ? -6.76576  -3.11573  51.44408  1.000 79.08843  ?  228 ILE B C   1 
ATOM 3729 O O   . ILE B 1 228 ? -7.29634  -2.10526  50.96607  1.000 73.74327  ?  228 ILE B O   1 
ATOM 3730 C CB  . ILE B 1 228 ? -8.16705  -5.23459  51.32719  1.000 87.99015  ?  228 ILE B CB  1 
ATOM 3731 C CG1 . ILE B 1 228 ? -8.49479  -6.44933  50.44826  1.000 77.93153  ?  228 ILE B CG1 1 
ATOM 3732 C CG2 . ILE B 1 228 ? -9.37898  -4.31786  51.42780  1.000 100.66304 ?  228 ILE B CG2 1 
ATOM 3733 C CD1 . ILE B 1 228 ? -8.89902  -6.09818  49.03368  1.000 74.80918  ?  228 ILE B CD1 1 
ATOM 3734 N N   . SER B 1 229 ? -6.02773  -3.06428  52.55522  1.000 81.60328  ?  229 SER B N   1 
ATOM 3735 C CA  . SER B 1 229 ? -5.68091  -1.77942  53.15677  1.000 80.25497  ?  229 SER B CA  1 
ATOM 3736 C C   . SER B 1 229 ? -4.82085  -0.93915  52.21730  1.000 83.47701  ?  229 SER B C   1 
ATOM 3737 O O   . SER B 1 229 ? -5.03081  0.27637   52.08272  1.000 81.47519  ?  229 SER B O   1 
ATOM 3738 C CB  . SER B 1 229 ? -4.94675  -2.02154  54.46449  1.000 80.14755  ?  229 SER B CB  1 
ATOM 3739 O OG  . SER B 1 229 ? -3.89164  -2.93312  54.22987  1.000 90.68530  ?  229 SER B OG  1 
ATOM 3740 N N   . GLN B 1 230 ? -3.84458  -1.57349  51.55802  1.000 82.77360  ?  230 GLN B N   1 
ATOM 3741 C CA  . GLN B 1 230 ? -3.00734  -0.86301  50.59798  1.000 60.37140  ?  230 GLN B CA  1 
ATOM 3742 C C   . GLN B 1 230 ? -3.82830  -0.37223  49.41985  1.000 69.62126  ?  230 GLN B C   1 
ATOM 3743 O O   . GLN B 1 230 ? -3.70540  0.78335   49.00475  1.000 70.67452  ?  230 GLN B O   1 
ATOM 3744 C CB  . GLN B 1 230 ? -1.88000  -1.76409  50.10037  1.000 77.44867  ?  230 GLN B CB  1 
ATOM 3745 C CG  . GLN B 1 230 ? -0.99725  -2.35499  51.17502  1.000 89.11775  ?  230 GLN B CG  1 
ATOM 3746 C CD  . GLN B 1 230 ? 0.19003   -3.08911  50.58391  1.000 83.51742  ?  230 GLN B CD  1 
ATOM 3747 O OE1 . GLN B 1 230 ? 0.17951   -4.31271  50.47429  1.000 89.19361  ?  230 GLN B OE1 1 
ATOM 3748 N NE2 . GLN B 1 230 ? 1.21921   -2.34216  50.19329  1.000 75.45333  ?  230 GLN B NE2 1 
ATOM 3749 N N   . ILE B 1 231 ? -4.62974  -1.26246  48.82788  1.000 74.45857  ?  231 ILE B N   1 
ATOM 3750 C CA  . ILE B 1 231 ? -5.50015  -0.87385  47.72015  1.000 62.83461  ?  231 ILE B CA  1 
ATOM 3751 C C   . ILE B 1 231 ? -6.35592  0.32047   48.11742  1.000 78.23149  ?  231 ILE B C   1 
ATOM 3752 O O   . ILE B 1 231 ? -6.41341  1.33537   47.40571  1.000 80.14137  ?  231 ILE B O   1 
ATOM 3753 C CB  . ILE B 1 231 ? -6.36053  -2.06928  47.27830  1.000 60.14333  ?  231 ILE B CB  1 
ATOM 3754 C CG1 . ILE B 1 231 ? -5.47964  -3.12286  46.61157  1.000 66.25926  ?  231 ILE B CG1 1 
ATOM 3755 C CG2 . ILE B 1 231 ? -7.48250  -1.61673  46.35333  1.000 68.58343  ?  231 ILE B CG2 1 
ATOM 3756 C CD1 . ILE B 1 231 ? -5.98711  -4.52059  46.75967  1.000 74.95142  ?  231 ILE B CD1 1 
ATOM 3757 N N   . SER B 1 232 ? -7.01578  0.21728   49.27823  1.000 68.64331  ?  232 SER B N   1 
ATOM 3758 C CA  . SER B 1 232 ? -7.87371  1.28780   49.77043  1.000 62.27874  ?  232 SER B CA  1 
ATOM 3759 C C   . SER B 1 232 ? -7.12134  2.60384   49.82969  1.000 67.89772  ?  232 SER B C   1 
ATOM 3760 O O   . SER B 1 232 ? -7.56443  3.61638   49.27516  1.000 63.84884  ?  232 SER B O   1 
ATOM 3761 C CB  . SER B 1 232 ? -8.41487  0.93751   51.15776  1.000 77.93334  ?  232 SER B CB  1 
ATOM 3762 O OG  . SER B 1 232 ? -7.51214  1.34533   52.18164  1.000 90.90819  ?  232 SER B OG  1 
ATOM 3763 N N   . ASN B 1 233 ? -5.97868  2.61096   50.51575  1.000 74.14504  ?  233 ASN B N   1 
ATOM 3764 C CA  . ASN B 1 233 ? -5.24037  3.85561   50.64889  1.000 72.52942  ?  233 ASN B CA  1 
ATOM 3765 C C   . ASN B 1 233 ? -4.75991  4.37198   49.29895  1.000 76.49622  ?  233 ASN B C   1 
ATOM 3766 O O   . ASN B 1 233 ? -4.65112  5.59009   49.10345  1.000 75.04988  ?  233 ASN B O   1 
ATOM 3767 C CB  . ASN B 1 233 ? -4.06855  3.67065   51.59946  1.000 60.94941  ?  233 ASN B CB  1 
ATOM 3768 C CG  . ASN B 1 233 ? -3.64612  4.96452   52.22082  1.000 77.33329  ?  233 ASN B CG  1 
ATOM 3769 O OD1 . ASN B 1 233 ? -2.79294  5.67151   51.68349  1.000 76.11405  ?  233 ASN B OD1 1 
ATOM 3770 N ND2 . ASN B 1 233 ? -4.25104  5.30068   53.35821  1.000 91.14584  ?  233 ASN B ND2 1 
ATOM 3771 N N   . MET B 1 234 ? -4.47880  3.47086   48.35326  1.000 68.05733  ?  234 MET B N   1 
ATOM 3772 C CA  . MET B 1 234 ? -3.96383  3.91171   47.06334  1.000 66.50871  ?  234 MET B CA  1 
ATOM 3773 C C   . MET B 1 234 ? -5.03990  4.62926   46.26527  1.000 67.94849  ?  234 MET B C   1 
ATOM 3774 O O   . MET B 1 234 ? -4.81860  5.73474   45.75772  1.000 74.15640  ?  234 MET B O   1 
ATOM 3775 C CB  . MET B 1 234 ? -3.38473  2.73560   46.27377  1.000 62.08139  ?  234 MET B CB  1 
ATOM 3776 C CG  . MET B 1 234 ? -2.03141  2.25078   46.78533  1.000 54.33535  ?  234 MET B CG  1 
ATOM 3777 S SD  . MET B 1 234 ? -1.36590  0.81836   45.89811  1.000 82.09706  ?  234 MET B SD  1 
ATOM 3778 C CE  . MET B 1 234 ? -2.22819  -0.57678  46.59053  1.000 61.88564  ?  234 MET B CE  1 
ATOM 3779 N N   . ILE B 1 235 ? -6.22383  4.02672   46.15416  1.000 78.71659  ?  235 ILE B N   1 
ATOM 3780 C CA  . ILE B 1 235 ? -7.26697  4.65612   45.35285  1.000 74.70402  ?  235 ILE B CA  1 
ATOM 3781 C C   . ILE B 1 235 ? -7.83954  5.89646   46.02383  1.000 81.43504  ?  235 ILE B C   1 
ATOM 3782 O O   . ILE B 1 235 ? -8.56078  6.66261   45.37296  1.000 83.26353  ?  235 ILE B O   1 
ATOM 3783 C CB  . ILE B 1 235 ? -8.36378  3.63376   44.98843  1.000 61.44194  ?  235 ILE B CB  1 
ATOM 3784 C CG1 . ILE B 1 235 ? -8.91293  2.95458   46.22677  1.000 61.40052  ?  235 ILE B CG1 1 
ATOM 3785 C CG2 . ILE B 1 235 ? -7.81892  2.58252   44.03384  1.000 70.69982  ?  235 ILE B CG2 1 
ATOM 3786 C CD1 . ILE B 1 235 ? -9.82322  1.82702   45.89572  1.000 61.17203  ?  235 ILE B CD1 1 
ATOM 3787 N N   . GLY B 1 236 ? -7.55929  6.10593   47.30554  1.000 79.83660  ?  236 GLY B N   1 
ATOM 3788 C CA  . GLY B 1 236 ? -7.96961  7.29888   48.01072  1.000 81.40853  ?  236 GLY B CA  1 
ATOM 3789 C C   . GLY B 1 236 ? -9.04278  7.10396   49.06255  1.000 84.37223  ?  236 GLY B C   1 
ATOM 3790 O O   . GLY B 1 236 ? -9.68069  8.08762   49.45843  1.000 99.47639  ?  236 GLY B O   1 
ATOM 3791 N N   . ILE B 1 237 ? -9.25419  5.88978   49.52504  1.000 76.39433  ?  237 ILE B N   1 
ATOM 3792 C CA  . ILE B 1 237 ? -10.31252 5.56600   50.46679  1.000 59.49981  ?  237 ILE B CA  1 
ATOM 3793 C C   . ILE B 1 237 ? -9.70765  5.39747   51.85128  1.000 76.92406  ?  237 ILE B C   1 
ATOM 3794 O O   . ILE B 1 237 ? -8.63230  4.80401   52.01131  1.000 73.60829  ?  237 ILE B O   1 
ATOM 3795 C CB  . ILE B 1 237 ? -11.06477 4.30664   49.99946  1.000 69.93862  ?  237 ILE B CB  1 
ATOM 3796 C CG1 . ILE B 1 237 ? -11.82990 4.62934   48.70744  1.000 63.84397  ?  237 ILE B CG1 1 
ATOM 3797 C CG2 . ILE B 1 237 ? -11.96140 3.75078   51.10141  1.000 82.23037  ?  237 ILE B CG2 1 
ATOM 3798 C CD1 . ILE B 1 237 ? -12.71677 3.50548   48.19849  1.000 77.46467  ?  237 ILE B CD1 1 
ATOM 3799 N N   . SER B 1 238 ? -10.38988 5.94631   52.85276  1.000 95.22617  ?  238 SER B N   1 
ATOM 3800 C CA  . SER B 1 238 ? -9.88404  6.00491   54.21783  1.000 108.69691 ?  238 SER B CA  1 
ATOM 3801 C C   . SER B 1 238 ? -9.73512  4.62870   54.86449  1.000 103.95560 ?  238 SER B C   1 
ATOM 3802 O O   . SER B 1 238 ? -8.61704  4.19586   55.16340  1.000 101.67829 ?  238 SER B O   1 
ATOM 3803 C CB  . SER B 1 238 ? -10.81917 6.88597   55.04826  1.000 117.74526 ?  238 SER B CB  1 
ATOM 3804 O OG  . SER B 1 238 ? -12.16941 6.71337   54.63070  1.000 99.12838  ?  238 SER B OG  1 
ATOM 3805 N N   . SER B 1 239 ? -10.84723 3.94488   55.10460  1.000 96.54365  ?  239 SER B N   1 
ATOM 3806 C CA  . SER B 1 239 ? -10.82286 2.64510   55.75721  1.000 95.70151  ?  239 SER B CA  1 
ATOM 3807 C C   . SER B 1 239 ? -10.85381 1.52827   54.72033  1.000 89.83459  ?  239 SER B C   1 
ATOM 3808 O O   . SER B 1 239 ? -11.17952 1.74488   53.55230  1.000 98.85441  ?  239 SER B O   1 
ATOM 3809 C CB  . SER B 1 239 ? -12.00020 2.50376   56.72568  1.000 103.80867 ?  239 SER B CB  1 
ATOM 3810 O OG  . SER B 1 239 ? -12.23675 1.14401   57.05356  1.000 103.44876 ?  239 SER B OG  1 
ATOM 3811 N N   . ALA B 1 240 ? -10.50344 0.31757   55.16356  1.000 89.49323  ?  240 ALA B N   1 
ATOM 3812 C CA  . ALA B 1 240 ? -10.62205 -0.84848  54.29149  1.000 89.74559  ?  240 ALA B CA  1 
ATOM 3813 C C   . ALA B 1 240 ? -12.05395 -1.37397  54.25047  1.000 93.40374  ?  240 ALA B C   1 
ATOM 3814 O O   . ALA B 1 240 ? -12.51256 -1.84887  53.20352  1.000 93.81640  ?  240 ALA B O   1 
ATOM 3815 C CB  . ALA B 1 240 ? -9.66264  -1.95288  54.72694  1.000 84.74923  ?  240 ALA B CB  1 
ATOM 3816 N N   . SER B 1 241 ? -12.75064 -1.35644  55.39016  1.000 101.15063 ?  241 SER B N   1 
ATOM 3817 C CA  . SER B 1 241 ? -14.14876 -1.77597  55.40677  1.000 95.68487  ?  241 SER B CA  1 
ATOM 3818 C C   . SER B 1 241 ? -14.97478 -0.96566  54.41618  1.000 92.90849  ?  241 SER B C   1 
ATOM 3819 O O   . SER B 1 241 ? -15.77213 -1.52417  53.65218  1.000 97.63490  ?  241 SER B O   1 
ATOM 3820 C CB  . SER B 1 241 ? -14.72656 -1.63706  56.81647  1.000 105.87502 ?  241 SER B CB  1 
ATOM 3821 O OG  . SER B 1 241 ? -14.79576 -0.27769  57.21191  1.000 116.51093 ?  241 SER B OG  1 
ATOM 3822 N N   . TYR B 1 242 ? -14.81346 0.35926   54.43352  1.000 68.77757  ?  242 TYR B N   1 
ATOM 3823 C CA  . TYR B 1 242 ? -15.47887 1.20185   53.44782  1.000 74.81081  ?  242 TYR B CA  1 
ATOM 3824 C C   . TYR B 1 242 ? -15.16134 0.75026   52.02216  1.000 81.72825  ?  242 TYR B C   1 
ATOM 3825 O O   . TYR B 1 242 ? -16.06308 0.63217   51.18411  1.000 83.46154  ?  242 TYR B O   1 
ATOM 3826 C CB  . TYR B 1 242 ? -15.09392 2.66551   53.65942  1.000 81.96489  ?  242 TYR B CB  1 
ATOM 3827 C CG  . TYR B 1 242 ? -16.00944 3.64648   52.94856  1.000 92.89405  ?  242 TYR B CG  1 
ATOM 3828 C CD1 . TYR B 1 242 ? -17.39542 3.56679   53.07452  1.000 89.52603  ?  242 TYR B CD1 1 
ATOM 3829 C CD2 . TYR B 1 242 ? -15.48541 4.64016   52.13105  1.000 91.99226  ?  242 TYR B CD2 1 
ATOM 3830 C CE1 . TYR B 1 242 ? -18.22828 4.46656   52.41010  1.000 94.75813  ?  242 TYR B CE1 1 
ATOM 3831 C CE2 . TYR B 1 242 ? -16.30446 5.53511   51.46498  1.000 87.17923  ?  242 TYR B CE2 1 
ATOM 3832 C CZ  . TYR B 1 242 ? -17.67086 5.44918   51.60300  1.000 94.02950  ?  242 TYR B CZ  1 
ATOM 3833 O OH  . TYR B 1 242 ? -18.46481 6.35618   50.92704  1.000 93.06835  ?  242 TYR B OH  1 
ATOM 3834 N N   . PHE B 1 243 ? -13.87822 0.51684   51.72037  1.000 72.71662  ?  243 PHE B N   1 
ATOM 3835 C CA  . PHE B 1 243 ? -13.49987 0.08509   50.37509  1.000 74.88787  ?  243 PHE B CA  1 
ATOM 3836 C C   . PHE B 1 243 ? -14.21057 -1.19986  49.96444  1.000 76.78017  ?  243 PHE B C   1 
ATOM 3837 O O   . PHE B 1 243 ? -14.67789 -1.31828  48.82655  1.000 71.48277  ?  243 PHE B O   1 
ATOM 3838 C CB  . PHE B 1 243 ? -11.99343 -0.12315  50.26469  1.000 85.18579  ?  243 PHE B CB  1 
ATOM 3839 C CG  . PHE B 1 243 ? -11.60033 -0.94666  49.06267  1.000 79.70237  ?  243 PHE B CG  1 
ATOM 3840 C CD1 . PHE B 1 243 ? -11.66054 -0.41291  47.79018  1.000 57.76241  ?  243 PHE B CD1 1 
ATOM 3841 C CD2 . PHE B 1 243 ? -11.23096 -2.27726  49.20912  1.000 67.23068  ?  243 PHE B CD2 1 
ATOM 3842 C CE1 . PHE B 1 243 ? -11.31826 -1.17831  46.69636  1.000 72.39448  ?  243 PHE B CE1 1 
ATOM 3843 C CE2 . PHE B 1 243 ? -10.89315 -3.04353  48.12261  1.000 61.03816  ?  243 PHE B CE2 1 
ATOM 3844 C CZ  . PHE B 1 243 ? -10.93461 -2.49454  46.86209  1.000 75.25918  ?  243 PHE B CZ  1 
ATOM 3845 N N   . ILE B 1 244 ? -14.22279 -2.20550  50.84742  1.000 70.92353  ?  244 ILE B N   1 
ATOM 3846 C CA  . ILE B 1 244 ? -14.86376 -3.47698  50.51155  1.000 62.47619  ?  244 ILE B CA  1 
ATOM 3847 C C   . ILE B 1 244 ? -16.36086 -3.29564  50.30187  1.000 71.12934  ?  244 ILE B C   1 
ATOM 3848 O O   . ILE B 1 244 ? -16.94349 -3.87634  49.37469  1.000 82.04567  ?  244 ILE B O   1 
ATOM 3849 C CB  . ILE B 1 244 ? -14.56875 -4.55120  51.57263  1.000 63.32011  ?  244 ILE B CB  1 
ATOM 3850 C CG1 . ILE B 1 244 ? -13.06062 -4.73729  51.74476  1.000 69.92539  ?  244 ILE B CG1 1 
ATOM 3851 C CG2 . ILE B 1 244 ? -15.19433 -5.86826  51.16712  1.000 63.51785  ?  244 ILE B CG2 1 
ATOM 3852 C CD1 . ILE B 1 244 ? -12.69836 -5.85709  52.68494  1.000 62.76156  ?  244 ILE B CD1 1 
ATOM 3853 N N   . ARG B 1 245 ? -17.02017 -2.51416  51.16694  1.000 76.54654  ?  245 ARG B N   1 
ATOM 3854 C CA  . ARG B 1 245 ? -18.45842 -2.30648  50.98533  1.000 77.17313  ?  245 ARG B CA  1 
ATOM 3855 C C   . ARG B 1 245 ? -18.75027 -1.59582  49.66603  1.000 76.72182  ?  245 ARG B C   1 
ATOM 3856 O O   . ARG B 1 245 ? -19.69929 -1.95435  48.95901  1.000 80.81843  ?  245 ARG B O   1 
ATOM 3857 C CB  . ARG B 1 245 ? -19.06654 -1.52226  52.15133  1.000 87.97825  ?  245 ARG B CB  1 
ATOM 3858 C CG  . ARG B 1 245 ? -18.91362 -2.14868  53.52253  1.000 90.33957  ?  245 ARG B CG  1 
ATOM 3859 C CD  . ARG B 1 245 ? -19.82750 -1.47141  54.54231  1.000 94.85248  ?  245 ARG B CD  1 
ATOM 3860 N NE  . ARG B 1 245 ? -19.72565 -0.01482  54.53294  1.000 88.10684  ?  245 ARG B NE  1 
ATOM 3861 C CZ  . ARG B 1 245 ? -19.14248 0.70867   55.47920  1.000 93.14340  ?  245 ARG B CZ  1 
ATOM 3862 N NH1 . ARG B 1 245 ? -18.41829 0.14578   56.43070  1.000 103.33492 ?  245 ARG B NH1 1 
ATOM 3863 N NH2 . ARG B 1 245 ? -19.26292 2.03320   55.45160  1.000 94.87815  ?  245 ARG B NH2 1 
ATOM 3864 N N   . ILE B 1 246 ? -17.94530 -0.58843  49.31254  1.000 66.55860  ?  246 ILE B N   1 
ATOM 3865 C CA  . ILE B 1 246 ? -18.17241 0.12100   48.05554  1.000 71.44629  ?  246 ILE B CA  1 
ATOM 3866 C C   . ILE B 1 246 ? -17.85534 -0.77661  46.85878  1.000 76.76168  ?  246 ILE B C   1 
ATOM 3867 O O   . ILE B 1 246 ? -18.57548 -0.76212  45.85678  1.000 66.92182  ?  246 ILE B O   1 
ATOM 3868 C CB  . ILE B 1 246 ? -17.36866 1.43342   48.01490  1.000 73.63571  ?  246 ILE B CB  1 
ATOM 3869 C CG1 . ILE B 1 246 ? -17.78119 2.34626   49.16459  1.000 65.66461  ?  246 ILE B CG1 1 
ATOM 3870 C CG2 . ILE B 1 246 ? -17.61334 2.16355   46.70356  1.000 79.63243  ?  246 ILE B CG2 1 
ATOM 3871 C CD1 . ILE B 1 246 ? -19.24073 2.72194   49.14588  1.000 83.10219  ?  246 ILE B CD1 1 
ATOM 3872 N N   . PHE B 1 247 ? -16.76470 -1.54941  46.92627  1.000 71.75300  ?  247 PHE B N   1 
ATOM 3873 C CA  . PHE B 1 247 ? -16.44411 -2.48999  45.85484  1.000 67.52447  ?  247 PHE B CA  1 
ATOM 3874 C C   . PHE B 1 247 ? -17.59912 -3.46102  45.62089  1.000 66.44076  ?  247 PHE B C   1 
ATOM 3875 O O   . PHE B 1 247 ? -18.02053 -3.68673  44.47895  1.000 65.93633  ?  247 PHE B O   1 
ATOM 3876 C CB  . PHE B 1 247 ? -15.15421 -3.24363  46.20893  1.000 59.16493  ?  247 PHE B CB  1 
ATOM 3877 C CG  . PHE B 1 247 ? -14.59883 -4.11248  45.09242  1.000 68.39901  ?  247 PHE B CG  1 
ATOM 3878 C CD1 . PHE B 1 247 ? -15.12597 -5.37897  44.83903  1.000 65.43670  ?  247 PHE B CD1 1 
ATOM 3879 C CD2 . PHE B 1 247 ? -13.50788 -3.69715  44.34560  1.000 71.05251  ?  247 PHE B CD2 1 
ATOM 3880 C CE1 . PHE B 1 247 ? -14.61017 -6.19226  43.83248  1.000 58.09783  ?  247 PHE B CE1 1 
ATOM 3881 C CE2 . PHE B 1 247 ? -12.98282 -4.51420  43.33843  1.000 69.39038  ?  247 PHE B CE2 1 
ATOM 3882 C CZ  . PHE B 1 247 ? -13.54075 -5.76139  43.08528  1.000 56.69437  ?  247 PHE B CZ  1 
ATOM 3883 N N   . ASN B 1 248 ? -18.14735 -4.01993  46.69915  1.000 63.93893  ?  248 ASN B N   1 
ATOM 3884 C CA  . ASN B 1 248 ? -19.27697 -4.92611  46.56201  1.000 65.92393  ?  248 ASN B CA  1 
ATOM 3885 C C   . ASN B 1 248 ? -20.48160 -4.20726  45.95487  1.000 71.22771  ?  248 ASN B C   1 
ATOM 3886 O O   . ASN B 1 248 ? -21.11251 -4.70872  45.01587  1.000 68.85248  ?  248 ASN B O   1 
ATOM 3887 C CB  . ASN B 1 248 ? -19.62589 -5.52659  47.92436  1.000 70.58133  ?  248 ASN B CB  1 
ATOM 3888 C CG  . ASN B 1 248 ? -20.27999 -6.89557  47.81553  1.000 70.60169  ?  248 ASN B CG  1 
ATOM 3889 O OD1 . ASN B 1 248 ? -20.39935 -7.45279  46.72722  1.000 76.78782  ?  248 ASN B OD1 1 
ATOM 3890 N ND2 . ASN B 1 248 ? -20.78042 -7.40535  48.93848  1.000 72.79329  ?  248 ASN B ND2 1 
ATOM 3891 N N   . LYS B 1 249 ? -20.82752 -3.03342  46.49598  1.000 72.63896  ?  249 LYS B N   1 
ATOM 3892 C CA  . LYS B 1 249 ? -21.98438 -2.28314  46.01108  1.000 70.94376  ?  249 LYS B CA  1 
ATOM 3893 C C   . LYS B 1 249 ? -21.84426 -1.90880  44.54068  1.000 69.95767  ?  249 LYS B C   1 
ATOM 3894 O O   . LYS B 1 249 ? -22.83626 -1.89652  43.80698  1.000 80.31266  ?  249 LYS B O   1 
ATOM 3895 C CB  . LYS B 1 249 ? -22.16251 -1.03173  46.87268  1.000 71.84432  ?  249 LYS B CB  1 
ATOM 3896 C CG  . LYS B 1 249 ? -23.29239 -0.09954  46.49914  1.000 74.23586  ?  249 LYS B CG  1 
ATOM 3897 C CD  . LYS B 1 249 ? -23.09276 1.25043   47.19359  1.000 100.36615 ?  249 LYS B CD  1 
ATOM 3898 C CE  . LYS B 1 249 ? -23.15412 1.11033   48.72217  1.000 121.33393 ?  249 LYS B CE  1 
ATOM 3899 N NZ  . LYS B 1 249 ? -22.94950 2.39706   49.46755  1.000 98.74431  ?  249 LYS B NZ  1 
ATOM 3900 N N   . HIS B 1 250 ? -20.61711 -1.66081  44.08141  1.000 78.26066  ?  250 HIS B N   1 
ATOM 3901 C CA  . HIS B 1 250 ? -20.37497 -1.20875  42.71462  1.000 75.31374  ?  250 HIS B CA  1 
ATOM 3902 C C   . HIS B 1 250 ? -20.34871 -2.37514  41.73421  1.000 74.96092  ?  250 HIS B C   1 
ATOM 3903 O O   . HIS B 1 250 ? -21.15836 -2.43267  40.80193  1.000 71.40748  ?  250 HIS B O   1 
ATOM 3904 C CB  . HIS B 1 250 ? -19.05337 -0.43357  42.65941  1.000 80.09081  ?  250 HIS B CB  1 
ATOM 3905 C CG  . HIS B 1 250 ? -18.70543 0.08632   41.30002  1.000 81.02256  ?  250 HIS B CG  1 
ATOM 3906 N ND1 . HIS B 1 250 ? -17.99812 -0.65851  40.37735  1.000 74.62561  ?  250 HIS B ND1 1 
ATOM 3907 C CD2 . HIS B 1 250 ? -18.94796 1.28131   40.71073  1.000 71.80196  ?  250 HIS B CD2 1 
ATOM 3908 C CE1 . HIS B 1 250 ? -17.83066 0.05171   39.27833  1.000 67.92539  ?  250 HIS B CE1 1 
ATOM 3909 N NE2 . HIS B 1 250 ? -18.40117 1.23226   39.45248  1.000 69.51519  ?  250 HIS B NE2 1 
ATOM 3910 N N   . TYR B 1 251 ? -19.43374 -3.32821  41.94273  1.000 64.80586  ?  251 TYR B N   1 
ATOM 3911 C CA  . TYR B 1 251 ? -19.30190 -4.44000  41.01339  1.000 64.93304  ?  251 TYR B CA  1 
ATOM 3912 C C   . TYR B 1 251 ? -20.29578 -5.56288  41.28041  1.000 74.87348  ?  251 TYR B C   1 
ATOM 3913 O O   . TYR B 1 251 ? -20.57620 -6.34963  40.36877  1.000 76.44224  ?  251 TYR B O   1 
ATOM 3914 C CB  . TYR B 1 251 ? -17.88848 -5.01090  41.06630  1.000 62.57029  ?  251 TYR B CB  1 
ATOM 3915 C CG  . TYR B 1 251 ? -16.85420 -4.16426  40.37968  1.000 62.33665  ?  251 TYR B CG  1 
ATOM 3916 C CD1 . TYR B 1 251 ? -16.81111 -4.08694  38.99894  1.000 67.63154  ?  251 TYR B CD1 1 
ATOM 3917 C CD2 . TYR B 1 251 ? -15.91022 -3.44957  41.10588  1.000 63.32050  ?  251 TYR B CD2 1 
ATOM 3918 C CE1 . TYR B 1 251 ? -15.86219 -3.31680  38.34736  1.000 59.79349  ?  251 TYR B CE1 1 
ATOM 3919 C CE2 . TYR B 1 251 ? -14.95360 -2.67363  40.46296  1.000 64.16516  ?  251 TYR B CE2 1 
ATOM 3920 C CZ  . TYR B 1 251 ? -14.93820 -2.61509  39.07989  1.000 58.15009  ?  251 TYR B CZ  1 
ATOM 3921 O OH  . TYR B 1 251 ? -14.00088 -1.85493  38.41723  1.000 70.66112  ?  251 TYR B OH  1 
ATOM 3922 N N   . GLY B 1 252 ? -20.85936 -5.64559  42.48443  1.000 70.77048  ?  252 GLY B N   1 
ATOM 3923 C CA  . GLY B 1 252 ? -21.73973 -6.74419  42.81268  1.000 70.28338  ?  252 GLY B CA  1 
ATOM 3924 C C   . GLY B 1 252 ? -21.06773 -7.96139  43.41800  1.000 71.70481  ?  252 GLY B C   1 
ATOM 3925 O O   . GLY B 1 252 ? -21.75561 -8.95414  43.67739  1.000 80.64516  ?  252 GLY B O   1 
ATOM 3926 N N   . VAL B 1 253 ? -19.74426 -7.94294  43.61050  1.000 73.94229  ?  253 VAL B N   1 
ATOM 3927 C CA  . VAL B 1 253 ? -19.01500 -9.06363  44.19610  1.000 65.45148  ?  253 VAL B CA  1 
ATOM 3928 C C   . VAL B 1 253 ? -18.06973 -8.54739  45.26922  1.000 66.16386  ?  253 VAL B C   1 
ATOM 3929 O O   . VAL B 1 253 ? -17.76900 -7.35370  45.34936  1.000 71.51943  ?  253 VAL B O   1 
ATOM 3930 C CB  . VAL B 1 253 ? -18.21457 -9.88465  43.16448  1.000 70.94358  ?  253 VAL B CB  1 
ATOM 3931 C CG1 . VAL B 1 253 ? -19.14625 -10.65540 42.25871  1.000 73.51905  ?  253 VAL B CG1 1 
ATOM 3932 C CG2 . VAL B 1 253 ? -17.28683 -8.97514  42.36934  1.000 73.90082  ?  253 VAL B CG2 1 
ATOM 3933 N N   . THR B 1 254 ? -17.64298 -9.46549  46.13717  1.000 69.79287  ?  254 THR B N   1 
ATOM 3934 C CA  . THR B 1 254 ? -16.60859 -9.11440  47.09623  1.000 78.99237  ?  254 THR B CA  1 
ATOM 3935 C C   . THR B 1 254 ? -15.24864 -9.10057  46.40055  1.000 80.65205  ?  254 THR B C   1 
ATOM 3936 O O   . THR B 1 254 ? -15.02372 -9.85872  45.45207  1.000 71.82206  ?  254 THR B O   1 
ATOM 3937 C CB  . THR B 1 254 ? -16.58561 -10.10930 48.25761  1.000 74.66719  ?  254 THR B CB  1 
ATOM 3938 O OG1 . THR B 1 254 ? -16.19794 -11.40386 47.78308  1.000 88.50525  ?  254 THR B OG1 1 
ATOM 3939 C CG2 . THR B 1 254 ? -17.95608 -10.22997 48.87823  1.000 80.65953  ?  254 THR B CG2 1 
ATOM 3940 N N   . PRO B 1 255 ? -14.32811 -8.23727  46.83825  1.000 74.94067  ?  255 PRO B N   1 
ATOM 3941 C CA  . PRO B 1 255 ? -12.96400 -8.30725  46.28994  1.000 67.79909  ?  255 PRO B CA  1 
ATOM 3942 C C   . PRO B 1 255 ? -12.41790 -9.72752  46.30904  1.000 75.31202  ?  255 PRO B C   1 
ATOM 3943 O O   . PRO B 1 255 ? -11.68872 -10.13427 45.39652  1.000 74.74114  ?  255 PRO B O   1 
ATOM 3944 C CB  . PRO B 1 255 ? -12.17844 -7.35481  47.20272  1.000 67.38986  ?  255 PRO B CB  1 
ATOM 3945 C CG  . PRO B 1 255 ? -13.20081 -6.34861  47.65699  1.000 59.74931  ?  255 PRO B CG  1 
ATOM 3946 C CD  . PRO B 1 255 ? -14.48020 -7.14724  47.82041  1.000 65.32932  ?  255 PRO B CD  1 
ATOM 3947 N N   . LYS B 1 256 ? -12.78001 -10.50184 47.33430  1.000 81.70290  ?  256 LYS B N   1 
ATOM 3948 C CA  . LYS B 1 256 ? -12.40275 -11.90990 47.39136  1.000 89.47238  ?  256 LYS B CA  1 
ATOM 3949 C C   . LYS B 1 256 ? -12.98983 -12.69131 46.21988  1.000 91.84078  ?  256 LYS B C   1 
ATOM 3950 O O   . LYS B 1 256 ? -12.28150 -13.45912 45.56177  1.000 95.67264  ?  256 LYS B O   1 
ATOM 3951 C CB  . LYS B 1 256 ? -12.86082 -12.51787 48.71834  1.000 96.28068  ?  256 LYS B CB  1 
ATOM 3952 C CG  . LYS B 1 256 ? -12.70793 -14.03099 48.79110  1.000 106.43885 ?  256 LYS B CG  1 
ATOM 3953 C CD  . LYS B 1 256 ? -13.89541 -14.66856 49.50322  1.000 99.78459  ?  256 LYS B CD  1 
ATOM 3954 C CE  . LYS B 1 256 ? -14.09045 -16.12235 49.07749  1.000 118.07977 ?  256 LYS B CE  1 
ATOM 3955 N NZ  . LYS B 1 256 ? -14.31707 -16.28504 47.60708  1.000 104.07527 ?  256 LYS B NZ  1 
ATOM 3956 N N   . GLN B 1 257 ? -14.30143 -12.55292 45.98685  1.000 91.98378  ?  257 GLN B N   1 
ATOM 3957 C CA  . GLN B 1 257 ? -14.96404 -13.26407 44.89249  1.000 88.09582  ?  257 GLN B CA  1 
ATOM 3958 C C   . GLN B 1 257 ? -14.35356 -12.90031 43.54707  1.000 93.88566  ?  257 GLN B C   1 
ATOM 3959 O O   . GLN B 1 257 ? -14.04113 -13.77712 42.72928  1.000 94.16305  ?  257 GLN B O   1 
ATOM 3960 C CB  . GLN B 1 257 ? -16.45277 -12.93357 44.88978  1.000 91.83947  ?  257 GLN B CB  1 
ATOM 3961 C CG  . GLN B 1 257 ? -17.28488 -13.73211 45.86435  1.000 102.53242 ?  257 GLN B CG  1 
ATOM 3962 C CD  . GLN B 1 257 ? -18.61212 -13.06575 46.13363  1.000 100.64087 ?  257 GLN B CD  1 
ATOM 3963 O OE1 . GLN B 1 257 ? -18.83109 -11.91981 45.73743  1.000 99.13021  ?  257 GLN B OE1 1 
ATOM 3964 N NE2 . GLN B 1 257 ? -19.51010 -13.77748 46.80468  1.000 128.75634 ?  257 GLN B NE2 1 
ATOM 3965 N N   . PHE B 1 258 ? -14.22817 -11.59506 43.29008  1.000 99.46154  ?  258 PHE B N   1 
ATOM 3966 C CA  . PHE B 1 258 ? -13.58664 -11.09373 42.08001  1.000 85.26644  ?  258 PHE B CA  1 
ATOM 3967 C C   . PHE B 1 258 ? -12.20339 -11.70944 41.89289  1.000 85.69536  ?  258 PHE B C   1 
ATOM 3968 O O   . PHE B 1 258 ? -11.89902 -12.27474 40.83726  1.000 99.12447  ?  258 PHE B O   1 
ATOM 3969 C CB  . PHE B 1 258 ? -13.50101 -9.56668  42.15012  1.000 75.56541  ?  258 PHE B CB  1 
ATOM 3970 C CG  . PHE B 1 258 ? -12.95791 -8.92913  40.90939  1.000 82.20579  ?  258 PHE B CG  1 
ATOM 3971 C CD1 . PHE B 1 258 ? -13.79538 -8.63337  39.84795  1.000 92.61932  ?  258 PHE B CD1 1 
ATOM 3972 C CD2 . PHE B 1 258 ? -11.61073 -8.63513  40.79563  1.000 84.03576  ?  258 PHE B CD2 1 
ATOM 3973 C CE1 . PHE B 1 258 ? -13.29860 -8.04511  38.70479  1.000 94.06656  ?  258 PHE B CE1 1 
ATOM 3974 C CE2 . PHE B 1 258 ? -11.10893 -8.05103  39.65051  1.000 72.58405  ?  258 PHE B CE2 1 
ATOM 3975 C CZ  . PHE B 1 258 ? -11.95057 -7.75431  38.60927  1.000 71.70154  ?  258 PHE B CZ  1 
ATOM 3976 N N   . PHE B 1 259 ? -11.34606 -11.59890 42.91061  1.000 86.28441  ?  259 PHE B N   1 
ATOM 3977 C CA  . PHE B 1 259 ? -9.99177  -12.13309 42.80305  1.000 88.61487  ?  259 PHE B CA  1 
ATOM 3978 C C   . PHE B 1 259 ? -9.99323  -13.63788 42.53724  1.000 92.42865  ?  259 PHE B C   1 
ATOM 3979 O O   . PHE B 1 259 ? -9.32904  -14.11248 41.60795  1.000 96.70341  ?  259 PHE B O   1 
ATOM 3980 C CB  . PHE B 1 259 ? -9.19366  -11.80770 44.06637  1.000 82.62840  ?  259 PHE B CB  1 
ATOM 3981 C CG  . PHE B 1 259 ? -7.74782  -12.17851 43.96287  1.000 89.29578  ?  259 PHE B CG  1 
ATOM 3982 C CD1 . PHE B 1 259 ? -6.85724  -11.36892 43.27914  1.000 91.53722  ?  259 PHE B CD1 1 
ATOM 3983 C CD2 . PHE B 1 259 ? -7.28077  -13.35631 44.52655  1.000 92.32171  ?  259 PHE B CD2 1 
ATOM 3984 C CE1 . PHE B 1 259 ? -5.52218  -11.72391 43.17003  1.000 99.12281  ?  259 PHE B CE1 1 
ATOM 3985 C CE2 . PHE B 1 259 ? -5.94709  -13.71548 44.42143  1.000 77.34831  ?  259 PHE B CE2 1 
ATOM 3986 C CZ  . PHE B 1 259 ? -5.06811  -12.89896 43.74520  1.000 84.16650  ?  259 PHE B CZ  1 
ATOM 3987 N N   . THR B 1 260 ? -10.72429 -14.40999 43.34957  1.000 102.88775 ?  260 THR B N   1 
ATOM 3988 C CA  . THR B 1 260 ? -10.70348 -15.86389 43.20078  1.000 102.29329 ?  260 THR B CA  1 
ATOM 3989 C C   . THR B 1 260 ? -11.23062 -16.29098 41.83901  1.000 106.86695 ?  260 THR B C   1 
ATOM 3990 O O   . THR B 1 260 ? -10.74325 -17.26955 41.25908  1.000 108.53606 ?  260 THR B O   1 
ATOM 3991 C CB  . THR B 1 260 ? -11.51042 -16.53581 44.31003  1.000 106.85573 ?  260 THR B CB  1 
ATOM 3992 O OG1 . THR B 1 260 ? -11.22114 -15.90304 45.56090  1.000 112.99272 ?  260 THR B OG1 1 
ATOM 3993 C CG2 . THR B 1 260 ? -11.13563 -18.00780 44.40783  1.000 104.14438 ?  260 THR B CG2 1 
ATOM 3994 N N   . TYR B 1 261 ? -12.22408 -15.57309 41.30622  1.000 89.68876  ?  261 TYR B N   1 
ATOM 3995 C CA  . TYR B 1 261 ? -12.72989 -15.94439 39.99255  1.000 88.10386  ?  261 TYR B CA  1 
ATOM 3996 C C   . TYR B 1 261 ? -11.65369 -15.80264 38.92145  1.000 86.94438  ?  261 TYR B C   1 
ATOM 3997 O O   . TYR B 1 261 ? -11.58518 -16.62387 38.00124  1.000 94.04267  ?  261 TYR B O   1 
ATOM 3998 C CB  . TYR B 1 261 ? -13.95531 -15.10546 39.62661  1.000 93.02330  ?  261 TYR B CB  1 
ATOM 3999 C CG  . TYR B 1 261 ? -14.71586 -15.68394 38.45811  1.000 77.76022  ?  261 TYR B CG  1 
ATOM 4000 C CD1 . TYR B 1 261 ? -15.53480 -16.78984 38.62487  1.000 85.49048  ?  261 TYR B CD1 1 
ATOM 4001 C CD2 . TYR B 1 261 ? -14.57459 -15.15930 37.18321  1.000 65.56217  ?  261 TYR B CD2 1 
ATOM 4002 C CE1 . TYR B 1 261 ? -16.21704 -17.33744 37.56308  1.000 89.13286  ?  261 TYR B CE1 1 
ATOM 4003 C CE2 . TYR B 1 261 ? -15.24995 -15.70296 36.11224  1.000 80.48402  ?  261 TYR B CE2 1 
ATOM 4004 C CZ  . TYR B 1 261 ? -16.07383 -16.79032 36.30897  1.000 86.22301  ?  261 TYR B CZ  1 
ATOM 4005 O OH  . TYR B 1 261 ? -16.75900 -17.33819 35.24967  1.000 88.49368  ?  261 TYR B OH  1 
ATOM 4006 N N   . PHE B 1 262 ? -10.78099 -14.80415 39.04062  1.000 84.53892  ?  262 PHE B N   1 
ATOM 4007 C CA  . PHE B 1 262 ? -9.78369  -14.52727 38.01413  1.000 96.23028  ?  262 PHE B CA  1 
ATOM 4008 C C   . PHE B 1 262 ? -8.39885  -15.07584 38.34486  1.000 99.11304  ?  262 PHE B C   1 
ATOM 4009 O O   . PHE B 1 262 ? -7.44169  -14.76568 37.62840  1.000 97.09051  ?  262 PHE B O   1 
ATOM 4010 C CB  . PHE B 1 262 ? -9.68889  -13.02311 37.74710  1.000 92.93076  ?  262 PHE B CB  1 
ATOM 4011 C CG  . PHE B 1 262 ? -10.90433 -12.44054 37.08139  1.000 91.87798  ?  262 PHE B CG  1 
ATOM 4012 C CD1 . PHE B 1 262 ? -11.05426 -12.51529 35.70767  1.000 89.95104  ?  262 PHE B CD1 1 
ATOM 4013 C CD2 . PHE B 1 262 ? -11.88412 -11.80065 37.82109  1.000 95.61751  ?  262 PHE B CD2 1 
ATOM 4014 C CE1 . PHE B 1 262 ? -12.16098 -11.97470 35.08609  1.000 89.49310  ?  262 PHE B CE1 1 
ATOM 4015 C CE2 . PHE B 1 262 ? -12.99624 -11.25723 37.20148  1.000 97.17925  ?  262 PHE B CE2 1 
ATOM 4016 C CZ  . PHE B 1 262 ? -13.13316 -11.34528 35.83104  1.000 88.47349  ?  262 PHE B CZ  1 
ATOM 4017 N N   . LYS B 1 263 ? -8.26995  -15.88156 39.39650  1.000 101.93449 ?  263 LYS B N   1 
ATOM 4018 C CA  . LYS B 1 263 ? -7.00943  -16.55737 39.71214  1.000 100.45637 ?  263 LYS B CA  1 
ATOM 4019 C C   . LYS B 1 263 ? -5.82592  -15.59242 39.79045  1.000 98.70803  ?  263 LYS B C   1 
ATOM 4020 O O   . LYS B 1 263 ? -6.00114  -14.37883 39.91520  1.000 84.28792  ?  263 LYS B O   1 
ATOM 4021 C CB  . LYS B 1 263 ? -6.71761  -17.65456 38.67722  1.000 99.47109  ?  263 LYS B CB  1 
ATOM 4022 C CG  . LYS B 1 263 ? -7.70129  -18.81878 38.71005  1.000 105.40093 ?  263 LYS B CG  1 
ATOM 4023 C CD  . LYS B 1 263 ? -7.69939  -19.48453 40.07320  1.000 105.54279 ?  263 LYS B CD  1 
ATOM 4024 C CE  . LYS B 1 263 ? -8.94762  -20.31777 40.28981  1.000 112.74003 ?  263 LYS B CE  1 
ATOM 4025 N NZ  . LYS B 1 263 ? -9.06538  -20.73365 41.71925  1.000 123.05031 ?  263 LYS B NZ  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   . LYS A 9   ? 0.97524 1.23926 1.52130 -0.20021 0.01019  -0.25684 9   LYS A N   
2    C CA  . LYS A 9   ? 1.11311 1.30294 1.65935 -0.19167 0.02622  -0.23500 9   LYS A CA  
3    C C   . LYS A 9   ? 1.19555 1.37986 1.72406 -0.18890 0.01927  -0.21829 9   LYS A C   
4    O O   . LYS A 9   ? 1.16386 1.40461 1.68552 -0.19490 0.00519  -0.22821 9   LYS A O   
5    C CB  . LYS A 9   ? 1.13683 1.29124 1.67386 -0.16310 0.01256  -0.20196 9   LYS A CB  
6    C CG  . LYS A 9   ? 0.98396 1.13711 1.54099 -0.16187 0.02245  -0.21605 9   LYS A CG  
7    C CD  . LYS A 9   ? 0.95377 1.09026 1.50475 -0.13240 0.00597  -0.18652 9   LYS A CD  
8    C CE  . LYS A 9   ? 1.15780 1.29820 1.73151 -0.12849 0.01610  -0.20116 9   LYS A CE  
9    N NZ  . LYS A 9   ? 1.14536 1.28764 1.71811 -0.10000 -0.00123 -0.17790 9   LYS A NZ  
10   N N   . GLU A 10  ? 1.31418 1.43188 1.83234 -0.17562 0.02971  -0.19188 10  GLU A N   
11   C CA  . GLU A 10  ? 1.33772 1.44078 1.83507 -0.16980 0.02322  -0.17088 10  GLU A CA  
12   C C   . GLU A 10  ? 1.31691 1.41865 1.78726 -0.14258 -0.00976 -0.13356 10  GLU A C   
13   O O   . GLU A 10  ? 1.33406 1.41242 1.78368 -0.13335 -0.01476 -0.11117 10  GLU A O   
14   C CB  . GLU A 10  ? 1.47780 1.50444 1.97124 -0.17082 0.05792  -0.16326 10  GLU A CB  
15   C CG  . GLU A 10  ? 1.56213 1.52717 2.05118 -0.14617 0.07042  -0.14338 10  GLU A CG  
16   C CD  . GLU A 10  ? 1.82312 1.76711 2.33677 -0.16333 0.10659  -0.17472 10  GLU A CD  
17   O OE1 . GLU A 10  ? 1.84252 1.84153 2.37804 -0.17741 0.09695  -0.20108 10  GLU A OE1 
18   O OE2 . GLU A 10  ? 1.93099 1.79756 2.43762 -0.16171 0.14810  -0.17243 10  GLU A OE2 
19   N N   . THR A 11  ? 0.96454 1.09043 1.43444 -0.13294 -0.02871 -0.12977 11  THR A N   
20   C CA  . THR A 11  ? 1.00278 1.12781 1.45035 -0.11375 -0.05348 -0.10216 11  THR A CA  
21   C C   . THR A 11  ? 0.96333 1.13320 1.39633 -0.11763 -0.07092 -0.10674 11  THR A C   
22   O O   . THR A 11  ? 1.03716 1.23955 1.48037 -0.12670 -0.06830 -0.12773 11  THR A O   
23   C CB  . THR A 11  ? 0.93063 1.03947 1.38797 -0.09707 -0.05493 -0.09340 11  THR A CB  
24   O OG1 . THR A 11  ? 1.22213 1.34456 1.70518 -0.10613 -0.04248 -0.11753 11  THR A OG1 
25   C CG2 . THR A 11  ? 1.02560 1.08290 1.47823 -0.07822 -0.04178 -0.07467 11  THR A CG2 
26   N N   . ILE A 12  ? 0.89989 1.06662 1.30377 -0.10940 -0.08516 -0.08669 12  ILE A N   
27   C CA  . ILE A 12  ? 0.72889 0.91954 1.10653 -0.10760 -0.09528 -0.08468 12  ILE A CA  
28   C C   . ILE A 12  ? 0.78328 0.95213 1.13709 -0.10095 -0.10445 -0.06464 12  ILE A C   
29   O O   . ILE A 12  ? 0.94824 1.09504 1.30190 -0.09568 -0.10795 -0.05137 12  ILE A O   
30   C CB  . ILE A 12  ? 0.80223 1.01623 1.16222 -0.10521 -0.09622 -0.08674 12  ILE A CB  
31   C CG1 . ILE A 12  ? 0.59999 0.84014 0.93030 -0.09669 -0.10044 -0.08757 12  ILE A CG1 
32   C CG2 . ILE A 12  ? 0.84609 1.03327 1.18538 -0.09792 -0.10018 -0.06553 12  ILE A CG2 
33   C CD1 . ILE A 12  ? 0.84686 1.13503 1.16820 -0.08838 -0.10147 -0.09851 12  ILE A CD1 
34   N N   . LYS A 13  ? 0.78987 0.96537 1.12085 -0.10231 -0.10512 -0.06494 13  LYS A N   
35   C CA  . LYS A 13  ? 0.69570 0.85155 1.00037 -0.10365 -0.10671 -0.05348 13  LYS A CA  
36   C C   . LYS A 13  ? 0.66305 0.80879 0.92268 -0.09941 -0.09895 -0.04695 13  LYS A C   
37   O O   . LYS A 13  ? 0.84464 0.99724 1.09140 -0.10053 -0.09084 -0.05422 13  LYS A O   
38   C CB  . LYS A 13  ? 0.82664 0.99274 1.14922 -0.11236 -0.10579 -0.06452 13  LYS A CB  
39   C CG  . LYS A 13  ? 0.84036 0.99765 1.14646 -0.11989 -0.10617 -0.06129 13  LYS A CG  
40   C CD  . LYS A 13  ? 1.09324 1.26966 1.41095 -0.13407 -0.09888 -0.07973 13  LYS A CD  
41   C CE  . LYS A 13  ? 1.22563 1.37910 1.50363 -0.14454 -0.07943 -0.08209 13  LYS A CE  
42   N NZ  . LYS A 13  ? 1.15859 1.28370 1.39987 -0.15933 -0.06475 -0.08152 13  LYS A NZ  
43   N N   . ILE A 14  ? 0.79118 0.91825 1.02335 -0.09086 -0.09913 -0.03205 14  ILE A N   
44   C CA  . ILE A 14  ? 0.71367 0.82318 0.89564 -0.07815 -0.08849 -0.02115 14  ILE A CA  
45   C C   . ILE A 14  ? 0.73919 0.80366 0.88674 -0.08708 -0.07578 -0.01290 14  ILE A C   
46   O O   . ILE A 14  ? 0.84672 0.90127 1.00371 -0.09644 -0.08104 -0.01087 14  ILE A O   
47   C CB  . ILE A 14  ? 0.78988 0.91284 0.96273 -0.05984 -0.09325 -0.01291 14  ILE A CB  
48   C CG1 . ILE A 14  ? 0.60633 0.77961 0.82220 -0.06137 -0.10195 -0.03057 14  ILE A CG1 
49   C CG2 . ILE A 14  ? 0.80893 0.92080 0.92713 -0.03581 -0.08185 -0.00035 14  ILE A CG2 
50   C CD1 . ILE A 14  ? 0.85790 1.06103 1.07271 -0.04787 -0.10501 -0.03122 14  ILE A CD1 
51   N N   . ASN A 15  ? 0.95379 0.98921 1.05699 -0.08440 -0.05559 -0.00938 15  ASN A N   
52   C CA  . ASN A 15  ? 1.01477 1.00000 1.08113 -0.09937 -0.03330 -0.00762 15  ASN A CA  
53   C C   . ASN A 15  ? 1.05143 0.98893 1.05772 -0.07773 -0.01561 0.01335  15  ASN A C   
54   O O   . ASN A 15  ? 1.09672 1.04839 1.08747 -0.04700 -0.02116 0.02624  15  ASN A O   
55   C CB  . ASN A 15  ? 1.10743 1.07875 1.16076 -0.11578 -0.01218 -0.02047 15  ASN A CB  
56   C CG  . ASN A 15  ? 0.96077 0.98226 1.07439 -0.13424 -0.02795 -0.04240 15  ASN A CG  
57   O OD1 . ASN A 15  ? 0.93764 0.97505 1.08069 -0.15476 -0.03301 -0.05650 15  ASN A OD1 
58   N ND2 . ASN A 15  ? 1.14738 1.19900 1.27860 -0.12439 -0.03536 -0.04671 15  ASN A ND2 
59   N N   . ASN A 16  ? 0.85094 0.73602 0.82407 -0.09392 0.00763  0.01363  16  ASN A N   
60   C CA  . ASN A 16  ? 0.91459 0.73511 0.82109 -0.07522 0.03536  0.03295  16  ASN A CA  
61   C C   . ASN A 16  ? 0.95939 0.79965 0.86342 -0.04012 0.01786  0.05155  16  ASN A C   
62   O O   . ASN A 16  ? 1.05375 0.87408 0.91034 -0.00343 0.03063  0.07052  16  ASN A O   
63   C CB  . ASN A 16  ? 0.96978 0.73971 0.81524 -0.06069 0.06970  0.04236  16  ASN A CB  
64   C CG  . ASN A 16  ? 1.13268 0.87508 0.97527 -0.10020 0.09601  0.02092  16  ASN A CG  
65   O OD1 . ASN A 16  ? 1.18626 0.90932 1.03566 -0.13607 0.10964  0.00316  16  ASN A OD1 
66   N ND2 . ASN A 16  ? 1.08312 0.83137 0.91765 -0.09599 0.10381  0.01844  16  ASN A ND2 
67   N N   . ILE A 17  ? 0.98289 0.86447 0.93610 -0.04913 -0.00960 0.04572  17  ILE A N   
68   C CA  . ILE A 17  ? 0.83157 0.72983 0.78520 -0.02406 -0.02152 0.05852  17  ILE A CA  
69   C C   . ILE A 17  ? 0.86153 0.70241 0.77456 -0.02530 -0.00152 0.06836  17  ILE A C   
70   O O   . ILE A 17  ? 1.05146 0.87812 0.97562 -0.05526 -0.00041 0.05789  17  ILE A O   
71   C CB  . ILE A 17  ? 0.87240 0.82858 0.88945 -0.03384 -0.05187 0.04837  17  ILE A CB  
72   C CG1 . ILE A 17  ? 0.81942 0.82449 0.87427 -0.03570 -0.06519 0.03523  17  ILE A CG1 
73   C CG2 . ILE A 17  ? 0.90864 0.88186 0.92725 -0.01395 -0.05911 0.05718  17  ILE A CG2 
74   C CD1 . ILE A 17  ? 0.95921 1.01363 1.06684 -0.03884 -0.08545 0.02570  17  ILE A CD1 
75   N N   . MET A 18  ? 0.99444 0.80632 0.85848 0.00978  0.01522  0.08723  18  MET A N   
76   C CA  . MET A 18  ? 1.08938 0.83856 0.90756 0.01425  0.04016  0.09808  18  MET A CA  
77   C C   . MET A 18  ? 1.10236 0.88555 0.94027 0.03176  0.02187  0.10458  18  MET A C   
78   O O   . MET A 18  ? 1.17596 1.00742 1.02231 0.06556  0.00858  0.11145  18  MET A O   
79   C CB  . MET A 18  ? 1.18784 0.86941 0.92869 0.04834  0.07845  0.11803  18  MET A CB  
80   C CG  . MET A 18  ? 1.20194 0.82348 0.89356 0.06775  0.10442  0.13347  18  MET A CG  
81   S SD  . MET A 18  ? 1.72534 1.24819 1.37734 0.02167  0.14897  0.12079  18  MET A SD  
82   C CE  . MET A 18  ? 1.64449 1.09393 1.22655 0.06509  0.18403  0.14637  18  MET A CE  
83   N N   . ILE A 19  ? 1.17469 0.93737 1.01836 0.00825  0.02316  0.09964  19  ILE A N   
84   C CA  . ILE A 19  ? 1.00492 0.78919 0.86158 0.02093  0.01180  0.10529  19  ILE A CA  
85   C C   . ILE A 19  ? 1.10336 0.82966 0.89828 0.05136  0.04277  0.12256  19  ILE A C   
86   O O   . ILE A 19  ? 1.24490 0.90127 0.99990 0.03486  0.07147  0.12205  19  ILE A O   
87   C CB  . ILE A 19  ? 0.97754 0.76713 0.86327 -0.01443 -0.00074 0.09370  19  ILE A CB  
88   C CG1 . ILE A 19  ? 1.04496 0.89485 0.99043 -0.02965 -0.03131 0.08264  19  ILE A CG1 
89   C CG2 . ILE A 19  ? 1.11115 0.89611 0.98935 -0.00313 0.00089  0.10134  19  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.92787 0.78306 0.88790 -0.05146 -0.03445 0.07005  19  ILE A CD1 
91   N N   . ALA A 20  ? 0.98364 0.74240 0.77043 0.09661  0.03908  0.13534  20  ALA A N   
92   C CA  . ALA A 20  ? 1.05812 0.76530 0.78229 0.13827  0.06931  0.15547  20  ALA A CA  
93   C C   . ALA A 20  ? 1.10594 0.82924 0.84029 0.14871  0.06539  0.15744  20  ALA A C   
94   O O   . ALA A 20  ? 1.28501 0.95165 0.96712 0.17581  0.09466  0.17229  20  ALA A O   
95   C CB  . ALA A 20  ? 1.08693 0.82475 0.78477 0.19356  0.07043  0.17029  20  ALA A CB  
96   N N   . LYS A 21  ? 0.97744 0.76881 0.77413 0.12719  0.03474  0.14273  21  LYS A N   
97   C CA  . LYS A 21  ? 0.96524 0.77551 0.77697 0.13016  0.03134  0.14129  21  LYS A CA  
98   C C   . LYS A 21  ? 1.07007 0.88410 0.92085 0.08041  0.01579  0.12710  21  LYS A C   
99   O O   . LYS A 21  ? 0.91120 0.75638 0.79977 0.05678  -0.00382 0.11650  21  LYS A O   
100  C CB  . LYS A 21  ? 0.96318 0.86701 0.81080 0.16200  0.01278  0.13612  21  LYS A CB  
101  C CG  . LYS A 21  ? 0.97720 0.90232 0.78884 0.22012  0.02108  0.14932  21  LYS A CG  
102  C CD  . LYS A 21  ? 1.10130 1.14229 0.95637 0.24811  0.00026  0.13537  21  LYS A CD  
103  C CE  . LYS A 21  ? 1.42374 1.50518 1.24295 0.31153  0.00290  0.14710  21  LYS A CE  
104  N NZ  . LYS A 21  ? 1.52551 1.74505 1.39877 0.32871  -0.02297 0.12234  21  LYS A NZ  
105  N N   . TYR A 22  ? 1.09953 0.88020 0.93664 0.06794  0.02609  0.12787  22  TYR A N   
106  C CA  . TYR A 22  ? 1.02337 0.81073 0.88924 0.02869  0.01144  0.11748  22  TYR A CA  
107  C C   . TYR A 22  ? 1.07628 0.93224 0.99883 0.02366  -0.01347 0.10916  22  TYR A C   
108  O O   . TYR A 22  ? 1.05088 0.95200 0.99320 0.04314  -0.01564 0.10674  22  TYR A O   
109  C CB  . TYR A 22  ? 0.95439 0.71096 0.79882 0.02319  0.02479  0.11943  22  TYR A CB  
110  C CG  . TYR A 22  ? 1.14054 0.89329 0.99682 -0.01412 0.01318  0.11100  22  TYR A CG  
111  C CD1 . TYR A 22  ? 1.15831 0.87315 0.98882 -0.03958 0.02155  0.10331  22  TYR A CD1 
112  C CD2 . TYR A 22  ? 0.91650 0.70710 0.80810 -0.02291 -0.00419 0.10894  22  TYR A CD2 
113  C CE1 . TYR A 22  ? 1.16699 0.89419 1.00702 -0.06714 0.00756  0.09448  22  TYR A CE1 
114  C CE2 . TYR A 22  ? 0.91022 0.69700 0.80409 -0.04760 -0.01445 0.10565  22  TYR A CE2 
115  C CZ  . TYR A 22  ? 1.19668 0.95843 1.06533 -0.06691 -0.01152 0.09872  22  TYR A CZ  
116  O OH  . TYR A 22  ? 1.21441 0.98741 1.08356 -0.08529 -0.02472 0.09421  22  TYR A OH  
117  N N   . THR A 23  ? 0.96200 0.82829 0.91087 -0.00174 -0.02911 0.10210  23  THR A N   
118  C CA  . THR A 23  ? 0.97303 0.89195 0.97085 -0.00665 -0.04556 0.09307  23  THR A CA  
119  C C   . THR A 23  ? 0.86985 0.78314 0.88546 -0.03022 -0.05291 0.09140  23  THR A C   
120  O O   . THR A 23  ? 1.07221 0.95950 1.07402 -0.04493 -0.05712 0.09391  23  THR A O   
121  C CB  . THR A 23  ? 0.99878 0.93549 1.01080 -0.00676 -0.05434 0.08784  23  THR A CB  
122  O OG1 . THR A 23  ? 0.94348 0.88537 0.93175 0.02167  -0.04571 0.09241  23  THR A OG1 
123  C CG2 . THR A 23  ? 0.88480 0.87018 0.94691 -0.01575 -0.06670 0.07501  23  THR A CG2 
124  N N   . VAL A 24  ? 0.83174 0.77150 0.87509 -0.03243 -0.05176 0.08578  24  VAL A N   
125  C CA  . VAL A 24  ? 0.96965 0.89832 1.02654 -0.04952 -0.05296 0.08651  24  VAL A CA  
126  C C   . VAL A 24  ? 0.92233 0.88333 1.02117 -0.05559 -0.05507 0.07362  24  VAL A C   
127  O O   . VAL A 24  ? 0.91488 0.91568 1.03999 -0.05460 -0.04773 0.05861  24  VAL A O   
128  C CB  . VAL A 24  ? 0.90266 0.81980 0.95046 -0.05245 -0.03943 0.08892  24  VAL A CB  
129  C CG1 . VAL A 24  ? 0.77716 0.66527 0.82065 -0.06512 -0.03686 0.09636  24  VAL A CG1 
130  C CG2 . VAL A 24  ? 0.94877 0.84003 0.95701 -0.04427 -0.03376 0.09720  24  VAL A CG2 
131  N N   . LEU A 25  ? 0.80314 0.75284 0.90964 -0.06216 -0.06359 0.07593  25  LEU A N   
132  C CA  . LEU A 25  ? 0.88645 0.85877 1.02972 -0.06869 -0.06288 0.06285  25  LEU A CA  
133  C C   . LEU A 25  ? 0.94262 0.88245 1.09003 -0.07738 -0.05234 0.06794  25  LEU A C   
134  O O   . LEU A 25  ? 1.16484 1.07189 1.28609 -0.07221 -0.05742 0.08497  25  LEU A O   
135  C CB  . LEU A 25  ? 0.91730 0.89927 1.06470 -0.06521 -0.07698 0.06157  25  LEU A CB  
136  C CG  . LEU A 25  ? 0.98066 0.99563 1.16452 -0.06982 -0.07689 0.04427  25  LEU A CG  
137  C CD1 . LEU A 25  ? 0.99710 1.03524 1.17533 -0.06050 -0.08678 0.04092  25  LEU A CD1 
138  C CD2 . LEU A 25  ? 1.02997 1.02178 1.22654 -0.07605 -0.07611 0.04683  25  LEU A CD2 
139  N N   . TYR A 26  ? 0.90040 0.84955 1.07737 -0.08946 -0.03484 0.05188  26  TYR A N   
140  C CA  . TYR A 26  ? 0.94784 0.85218 1.12387 -0.09613 -0.01544 0.05699  26  TYR A CA  
141  C C   . TYR A 26  ? 1.01157 0.92319 1.21517 -0.09933 -0.01494 0.04584  26  TYR A C   
142  O O   . TYR A 26  ? 1.08539 1.03388 1.32375 -0.11411 -0.00547 0.01904  26  TYR A O   
143  C CB  . TYR A 26  ? 1.02350 0.91901 1.20861 -0.11383 0.01548  0.04338  26  TYR A CB  
144  C CG  . TYR A 26  ? 1.21372 1.04058 1.38114 -0.11722 0.04348  0.05520  26  TYR A CG  
145  C CD1 . TYR A 26  ? 1.28202 1.05837 1.40268 -0.09880 0.04053  0.08660  26  TYR A CD1 
146  C CD2 . TYR A 26  ? 1.25085 1.06109 1.44313 -0.13694 0.07591  0.03466  26  TYR A CD2 
147  C CE1 . TYR A 26  ? 1.54898 1.25668 1.64232 -0.09264 0.06816  0.10302  26  TYR A CE1 
148  C CE2 . TYR A 26  ? 1.23035 0.96111 1.39630 -0.13574 0.10921  0.04926  26  TYR A CE2 
149  C CZ  . TYR A 26  ? 1.51479 1.19267 1.62837 -0.10983 0.10471  0.08639  26  TYR A CZ  
150  O OH  . TYR A 26  ? 1.30882 0.90255 1.38587 -0.09983 0.13987  0.10607  26  TYR A OH  
151  N N   . THR A 27  ? 1.16870 1.05329 1.35732 -0.08447 -0.02567 0.06386  27  THR A N   
152  C CA  . THR A 27  ? 1.12076 1.01211 1.33317 -0.08314 -0.02762 0.05557  27  THR A CA  
153  C C   . THR A 27  ? 1.33253 1.21278 1.57330 -0.10206 0.00392  0.03348  27  THR A C   
154  O O   . THR A 27  ? 1.58699 1.50034 1.85956 -0.11192 0.00330  0.01141  27  THR A O   
155  C CB  . THR A 27  ? 1.08575 0.94721 1.27611 -0.06024 -0.03685 0.07867  27  THR A CB  
156  O OG1 . THR A 27  ? 1.16588 0.96848 1.33149 -0.05115 -0.01189 0.09510  27  THR A OG1 
157  C CG2 . THR A 27  ? 1.14409 1.02491 1.30881 -0.04920 -0.06416 0.09184  27  THR A CG2 
158  N N   . SER A 28  ? 1.31932 1.15082 1.54690 -0.10979 0.03559  0.03664  28  SER A N   
159  C CA  . SER A 28  ? 1.32724 1.14360 1.58088 -0.13629 0.07504  0.00884  28  SER A CA  
160  C C   . SER A 28  ? 1.52964 1.32479 1.79881 -0.13422 0.08602  0.00248  28  SER A C   
161  O O   . SER A 28  ? 1.67759 1.41003 1.91909 -0.11121 0.09580  0.02851  28  SER A O   
162  C CB  . SER A 28  ? 1.19024 1.08395 1.48209 -0.16183 0.07370  -0.02871 28  SER A CB  
163  O OG  . SER A 28  ? 1.39907 1.29339 1.72215 -0.19401 0.11245  -0.06529 28  SER A OG  
164  N N   . ASN A 29  ? 1.41744 1.26711 1.72808 -0.15446 0.08494  -0.03179 29  ASN A N   
165  C CA  . ASN A 29  ? 1.37323 1.20758 1.70334 -0.15774 0.09895  -0.04476 29  ASN A CA  
166  C C   . ASN A 29  ? 1.33404 1.20881 1.67070 -0.13697 0.05930  -0.03557 29  ASN A C   
167  O O   . ASN A 29  ? 1.35979 1.27292 1.72694 -0.14941 0.05808  -0.06142 29  ASN A O   
168  C CB  . ASN A 29  ? 1.30251 1.17389 1.67436 -0.19796 0.12792  -0.09467 29  ASN A CB  
169  C CG  . ASN A 29  ? 1.61869 1.41405 1.98599 -0.22190 0.18737  -0.10833 29  ASN A CG  
170  O OD1 . ASN A 29  ? 1.77547 1.48146 2.11447 -0.20411 0.21189  -0.08370 29  ASN A OD1 
171  N ND2 . ASN A 29  ? 1.58720 1.41719 1.97945 -0.26069 0.21407  -0.14817 29  ASN A ND2 
172  N N   . CYS A 30  ? 1.21340 1.08342 1.52198 -0.10835 0.02911  -0.00282 30  CYS A N   
173  C CA  . CYS A 30  ? 1.08947 0.99468 1.40417 -0.09297 -0.00243 0.00246  30  CYS A CA  
174  C C   . CYS A 30  ? 1.07081 0.95683 1.35317 -0.06317 -0.02265 0.03538  30  CYS A C   
175  O O   . CYS A 30  ? 1.16551 1.03119 1.41876 -0.05608 -0.02383 0.05333  30  CYS A O   
176  C CB  . CYS A 30  ? 0.97658 0.94975 1.30374 -0.10314 -0.02677 -0.01299 30  CYS A CB  
177  S SG  . CYS A 30  ? 0.92069 0.90482 1.21455 -0.09266 -0.04996 0.00795  30  CYS A SG  
178  N N   . ILE A 31  ? 1.10431 1.00271 1.39339 -0.04639 -0.03695 0.03978  31  ILE A N   
179  C CA  . ILE A 31  ? 0.98212 0.89272 1.25002 -0.02082 -0.06189 0.06056  31  ILE A CA  
180  C C   . ILE A 31  ? 1.04922 1.01614 1.32794 -0.03226 -0.08839 0.04813  31  ILE A C   
181  O O   . ILE A 31  ? 0.96857 0.96064 1.27343 -0.04349 -0.08918 0.02961  31  ILE A O   
182  C CB  . ILE A 31  ? 1.03980 0.93323 1.30870 0.00889  -0.05692 0.07121  31  ILE A CB  
183  C CG1 . ILE A 31  ? 1.13487 0.95425 1.38885 0.01951  -0.01854 0.08224  31  ILE A CG1 
184  C CG2 . ILE A 31  ? 0.98973 0.91148 1.23674 0.03780  -0.08331 0.08912  31  ILE A CG2 
185  C CD1 . ILE A 31  ? 1.21361 0.98976 1.42826 0.02489  -0.00646 0.10267  31  ILE A CD1 
186  N N   . MET A 32  ? 1.20738 1.18907 1.46244 -0.03111 -0.10554 0.05689  32  MET A N   
187  C CA  . MET A 32  ? 1.11272 1.13093 1.36874 -0.04519 -0.12064 0.04517  32  MET A CA  
188  C C   . MET A 32  ? 1.12536 1.17117 1.37205 -0.03724 -0.13809 0.04670  32  MET A C   
189  O O   . MET A 32  ? 1.28812 1.33099 1.51041 -0.02779 -0.14458 0.05848  32  MET A O   
190  C CB  . MET A 32  ? 0.78161 0.79310 1.01732 -0.05726 -0.11841 0.04659  32  MET A CB  
191  C CG  . MET A 32  ? 1.12020 1.13553 1.37129 -0.06800 -0.10625 0.03466  32  MET A CG  
192  S SD  . MET A 32  ? 1.21496 1.22762 1.44124 -0.07183 -0.10322 0.03900  32  MET A SD  
193  C CE  . MET A 32  ? 0.89005 0.89660 1.08283 -0.06959 -0.11565 0.04909  32  MET A CE  
194  N N   . ASP A 33  ? 1.16087 1.23957 1.42698 -0.04333 -0.14450 0.03119  33  ASP A N   
195  C CA  . ASP A 33  ? 1.18480 1.30222 1.44638 -0.04667 -0.15766 0.02185  33  ASP A CA  
196  C C   . ASP A 33  ? 1.19981 1.31493 1.44576 -0.07301 -0.15215 0.01011  33  ASP A C   
197  O O   . ASP A 33  ? 1.27936 1.39444 1.53478 -0.08453 -0.14447 -0.00041 33  ASP A O   
198  C CB  . ASP A 33  ? 1.20058 1.35730 1.49282 -0.03737 -0.16374 0.00944  33  ASP A CB  
199  C CG  . ASP A 33  ? 1.22026 1.37240 1.51836 -0.00261 -0.16564 0.02500  33  ASP A CG  
200  O OD1 . ASP A 33  ? 1.23928 1.34897 1.51601 0.01006  -0.15827 0.04519  33  ASP A OD1 
201  O OD2 . ASP A 33  ? 1.23438 1.42203 1.55515 0.01399  -0.17137 0.01768  33  ASP A OD2 
202  N N   . ILE A 34  ? 0.84162 0.94916 1.05834 -0.08042 -0.15265 0.01294  34  ILE A N   
203  C CA  . ILE A 34  ? 0.95531 1.04398 1.14654 -0.10174 -0.14016 0.00533  34  ILE A CA  
204  C C   . ILE A 34  ? 0.89028 1.00996 1.08057 -0.12198 -0.13849 -0.01795 34  ILE A C   
205  O O   . ILE A 34  ? 1.10290 1.25760 1.29354 -0.12150 -0.14948 -0.02539 34  ILE A O   
206  C CB  . ILE A 34  ? 0.97534 1.03116 1.13386 -0.10039 -0.13544 0.01918  34  ILE A CB  
207  C CG1 . ILE A 34  ? 0.75094 0.78517 0.91538 -0.08428 -0.13459 0.03651  34  ILE A CG1 
208  C CG2 . ILE A 34  ? 0.88337 0.90967 1.00946 -0.11750 -0.11700 0.01320  34  ILE A CG2 
209  C CD1 . ILE A 34  ? 0.90286 0.90702 1.03810 -0.08410 -0.12637 0.04733  34  ILE A CD1 
210  N N   . TYR A 35  ? 0.94884 1.05826 1.13518 -0.14041 -0.12231 -0.03163 35  TYR A N   
211  C CA  . TYR A 35  ? 1.05805 1.18815 1.24091 -0.16869 -0.11032 -0.05949 35  TYR A CA  
212  C C   . TYR A 35  ? 1.15105 1.22337 1.28688 -0.18737 -0.08242 -0.05983 35  TYR A C   
213  O O   . TYR A 35  ? 1.13107 1.15579 1.24434 -0.18004 -0.06711 -0.04564 35  TYR A O   
214  C CB  . TYR A 35  ? 1.06120 1.21301 1.26984 -0.17733 -0.10445 -0.07598 35  TYR A CB  
215  C CG  . TYR A 35  ? 0.99636 1.18616 1.24703 -0.15320 -0.12554 -0.07041 35  TYR A CG  
216  C CD1 . TYR A 35  ? 1.06433 1.22772 1.32119 -0.13545 -0.12680 -0.05236 35  TYR A CD1 
217  C CD2 . TYR A 35  ? 0.99466 1.24966 1.27780 -0.14687 -0.14177 -0.08557 35  TYR A CD2 
218  C CE1 . TYR A 35  ? 1.28344 1.47093 1.57576 -0.11618 -0.13890 -0.04960 35  TYR A CE1 
219  C CE2 . TYR A 35  ? 1.01551 1.29511 1.33173 -0.11977 -0.15594 -0.07814 35  TYR A CE2 
220  C CZ  . TYR A 35  ? 1.37974 1.61862 1.69946 -0.10657 -0.15201 -0.06018 35  TYR A CZ  
221  O OH  . TYR A 35  ? 1.26966 1.52302 1.61949 -0.08247 -0.15913 -0.05522 35  TYR A OH  
222  N N   . SER A 36  ? 1.77387 1.85178 1.89221 -0.20851 -0.07442 -0.07641 36  SER A N   
223  C CA  . SER A 36  ? 1.92002 1.93417 1.99008 -0.22924 -0.03961 -0.08059 36  SER A CA  
224  C C   . SER A 36  ? 2.06628 2.10806 2.13123 -0.26619 -0.02689 -0.11658 36  SER A C   
225  O O   . SER A 36  ? 2.11793 2.22696 2.20699 -0.26468 -0.05262 -0.12805 36  SER A O   
226  C CB  . SER A 36  ? 1.93162 1.89581 1.97049 -0.20646 -0.03917 -0.05056 36  SER A CB  
227  O OG  . SER A 36  ? 2.00549 1.90948 1.99555 -0.22390 -0.00475 -0.05565 36  SER A OG  
228  N N   . GLU A 37  ? 2.06170 2.04917 2.09008 -0.29809 0.01623  -0.13483 37  GLU A N   
229  C CA  . GLU A 37  ? 2.06213 2.07102 2.08371 -0.34436 0.03949  -0.17886 37  GLU A CA  
230  C C   . GLU A 37  ? 1.85672 1.97917 1.93394 -0.35850 0.01362  -0.21418 37  GLU A C   
231  O O   . GLU A 37  ? 1.83497 2.02457 1.92449 -0.37626 0.00317  -0.24362 37  GLU A O   
232  C CB  . GLU A 37  ? 2.14144 2.13280 2.13414 -0.34784 0.04162  -0.17722 37  GLU A CB  
233  C CG  . GLU A 37  ? 2.20952 2.09150 2.14508 -0.33377 0.07207  -0.14673 37  GLU A CG  
234  C CD  . GLU A 37  ? 2.06423 1.93242 1.97414 -0.33778 0.07425  -0.14710 37  GLU A CD  
235  O OE1 . GLU A 37  ? 2.00437 1.95070 1.94008 -0.34517 0.04581  -0.16499 37  GLU A OE1 
236  O OE2 . GLU A 37  ? 2.05953 1.84020 1.92057 -0.33048 0.10532  -0.12924 37  GLU A OE2 
237  N N   . GLU A 38  ? 1.90458 2.05469 2.01511 -0.34743 0.00280  -0.21205 38  GLU A N   
238  C CA  . GLU A 38  ? 1.69414 1.95324 1.85999 -0.35348 -0.02046 -0.24344 38  GLU A CA  
239  C C   . GLU A 38  ? 1.51558 1.85537 1.70836 -0.31932 -0.06782 -0.23374 38  GLU A C   
240  O O   . GLU A 38  ? 1.33950 1.78116 1.56390 -0.32722 -0.08459 -0.26758 38  GLU A O   
241  C CB  . GLU A 38  ? 1.50671 1.80434 1.67803 -0.41089 0.01255  -0.30238 38  GLU A CB  
242  C CG  . GLU A 38  ? 1.36184 1.58256 1.50779 -0.44402 0.06399  -0.31441 38  GLU A CG  
243  C CD  . GLU A 38  ? 1.67739 1.94171 1.83386 -0.50694 0.10113  -0.37958 38  GLU A CD  
244  O OE1 . GLU A 38  ? 1.84016 2.20234 2.02446 -0.52391 0.08360  -0.41665 38  GLU A OE1 
245  O OE2 . GLU A 38  ? 1.53645 1.74073 1.67177 -0.54024 0.14986  -0.39627 38  GLU A OE2 
246  N N   . GLU A 39  ? 1.47708 1.77348 1.65477 -0.27929 -0.08737 -0.18808 39  GLU A N   
247  C CA  . GLU A 39  ? 1.24482 1.59354 1.43549 -0.24159 -0.12545 -0.17023 39  GLU A CA  
248  C C   . GLU A 39  ? 1.12897 1.43996 1.32842 -0.19891 -0.14171 -0.12695 39  GLU A C   
249  O O   . GLU A 39  ? 1.48561 1.73038 1.67510 -0.19954 -0.12566 -0.11017 39  GLU A O   
250  C CB  . GLU A 39  ? 1.50478 1.83540 1.65855 -0.24517 -0.12487 -0.16529 39  GLU A CB  
251  C CG  . GLU A 39  ? 1.46883 1.84663 1.61442 -0.28975 -0.10878 -0.21398 39  GLU A CG  
252  C CD  . GLU A 39  ? 1.59513 1.93499 1.69796 -0.29708 -0.10062 -0.20810 39  GLU A CD  
253  O OE1 . GLU A 39  ? 1.54923 1.91257 1.64569 -0.26292 -0.12927 -0.18465 39  GLU A OE1 
254  O OE2 . GLU A 39  ? 1.62378 1.90410 1.69552 -0.33585 -0.06189 -0.22611 39  GLU A OE2 
255  N N   . LYS A 40  ? 0.91880 1.27223 1.13273 -0.16085 -0.17090 -0.11009 40  LYS A N   
256  C CA  . LYS A 40  ? 0.82348 1.14464 1.04753 -0.12283 -0.18181 -0.07467 40  LYS A CA  
257  C C   . LYS A 40  ? 0.70523 1.00900 0.90516 -0.09267 -0.19472 -0.04558 40  LYS A C   
258  O O   . LYS A 40  ? 0.93088 1.29068 1.12587 -0.07612 -0.21191 -0.04989 40  LYS A O   
259  C CB  . LYS A 40  ? 0.67787 1.05748 0.94310 -0.10139 -0.19597 -0.08205 40  LYS A CB  
260  C CG  . LYS A 40  ? 0.70865 1.04890 0.98382 -0.06598 -0.20001 -0.05024 40  LYS A CG  
261  C CD  . LYS A 40  ? 0.73200 1.13091 1.04218 -0.03693 -0.21328 -0.05580 40  LYS A CD  
262  C CE  . LYS A 40  ? 0.84455 1.19219 1.16347 -0.00847 -0.20791 -0.02910 40  LYS A CE  
263  N NZ  . LYS A 40  ? 1.25120 1.55787 1.58294 -0.03488 -0.19078 -0.03564 40  LYS A NZ  
264  N N   . ILE A 41  ? 0.94105 1.17256 1.12496 -0.08483 -0.18533 -0.01785 41  ILE A N   
265  C CA  . ILE A 41  ? 0.95039 1.15075 1.11055 -0.05962 -0.19007 0.01075  41  ILE A CA  
266  C C   . ILE A 41  ? 1.00077 1.16210 1.17602 -0.03693 -0.18568 0.03328  41  ILE A C   
267  O O   . ILE A 41  ? 1.06217 1.18936 1.24775 -0.05025 -0.17291 0.03306  41  ILE A O   
268  C CB  . ILE A 41  ? 0.92281 1.07430 1.04920 -0.07868 -0.17627 0.01603  41  ILE A CB  
269  C CG1 . ILE A 41  ? 1.07104 1.25460 1.18033 -0.10598 -0.17398 -0.01088 41  ILE A CG1 
270  C CG2 . ILE A 41  ? 1.09564 1.21177 1.19930 -0.05557 -0.17721 0.04430  41  ILE A CG2 
271  C CD1 . ILE A 41  ? 1.33292 1.46790 1.40482 -0.12061 -0.15887 -0.00555 41  ILE A CD1 
272  N N   . THR A 42  ? 1.03855 1.20472 1.21192 -0.00187 -0.19323 0.05123  42  THR A N   
273  C CA  . THR A 42  ? 1.10461 1.22466 1.28872 0.01662  -0.18111 0.06958  42  THR A CA  
274  C C   . THR A 42  ? 1.23256 1.29372 1.38602 0.02456  -0.16789 0.09326  42  THR A C   
275  O O   . THR A 42  ? 1.35323 1.41344 1.47563 0.04744  -0.17272 0.10934  42  THR A O   
276  C CB  . THR A 42  ? 0.99055 1.13750 1.18834 0.05308  -0.18815 0.07556  42  THR A CB  
277  O OG1 . THR A 42  ? 1.17204 1.37409 1.40498 0.04162  -0.19691 0.05001  42  THR A OG1 
278  C CG2 . THR A 42  ? 0.97769 1.06136 1.17928 0.06953  -0.16676 0.09373  42  THR A CG2 
279  N N   . CYS A 43  ? 1.18719 1.20589 1.34853 0.00585  -0.15066 0.09312  43  CYS A N   
280  C CA  . CYS A 43  ? 1.12043 1.08603 1.26176 0.00769  -0.13250 0.10926  43  CYS A CA  
281  C C   . CYS A 43  ? 1.23520 1.16155 1.38802 0.02204  -0.11214 0.11765  43  CYS A C   
282  O O   . CYS A 43  ? 1.35009 1.28017 1.53582 0.01084  -0.10509 0.10305  43  CYS A O   
283  C CB  . CYS A 43  ? 1.03682 0.99199 1.18304 -0.02046 -0.12394 0.09873  43  CYS A CB  
284  S SG  . CYS A 43  ? 1.33388 1.31975 1.46691 -0.03960 -0.13734 0.08546  43  CYS A SG  
285  N N   . PHE A 44  ? 1.17520 1.05871 1.29645 0.04568  -0.09847 0.14033  44  PHE A N   
286  C CA  . PHE A 44  ? 1.24430 1.07180 1.36349 0.06223  -0.06960 0.15155  44  PHE A CA  
287  C C   . PHE A 44  ? 1.23573 1.01685 1.36085 0.03272  -0.03840 0.14318  44  PHE A C   
288  O O   . PHE A 44  ? 1.19691 0.99480 1.32513 0.00779  -0.04324 0.13295  44  PHE A O   
289  C CB  . PHE A 44  ? 1.24994 1.04890 1.32140 0.10735  -0.06599 0.18275  44  PHE A CB  
290  C CG  . PHE A 44  ? 1.47053 1.20411 1.53016 0.13603  -0.03320 0.19908  44  PHE A CG  
291  C CD1 . PHE A 44  ? 1.39492 1.14203 1.48582 0.14675  -0.03283 0.18986  44  PHE A CD1 
292  C CD2 . PHE A 44  ? 1.56259 1.21422 1.57403 0.15430  0.00161  0.22475  44  PHE A CD2 
293  C CE1 . PHE A 44  ? 1.62755 1.30420 1.70270 0.17549  0.00313  0.20552  44  PHE A CE1 
294  C CE2 . PHE A 44  ? 1.42643 1.00154 1.41780 0.18257  0.04055  0.24161  44  PHE A CE2 
295  C CZ  . PHE A 44  ? 1.61728 1.20371 1.64055 0.19392  0.04167  0.23204  44  PHE A CZ  
296  N N   . SER A 45  ? 1.21443 0.93910 1.34182 0.03517  -0.00310 0.14450  45  SER A N   
297  C CA  . SER A 45  ? 1.30210 0.99038 1.43849 0.00253  0.03127  0.12928  45  SER A CA  
298  C C   . SER A 45  ? 1.37402 1.02073 1.46685 0.00637  0.04568  0.14848  45  SER A C   
299  O O   . SER A 45  ? 1.50090 1.11897 1.54798 0.04144  0.04298  0.17877  45  SER A O   
300  C CB  . SER A 45  ? 1.23971 0.87194 1.38765 -0.00163 0.07333  0.12055  45  SER A CB  
301  O OG  . SER A 45  ? 1.43114 1.00234 1.53843 0.04124  0.08951  0.15197  45  SER A OG  
302  N N   . ASN A 46  ? 1.20596 0.85645 1.31268 -0.02803 0.06077  0.12931  46  ASN A N   
303  C CA  . ASN A 46  ? 1.35035 0.96486 1.42144 -0.03168 0.07820  0.14169  46  ASN A CA  
304  C C   . ASN A 46  ? 1.27331 0.91642 1.31187 -0.01094 0.04225  0.16261  46  ASN A C   
305  O O   . ASN A 46  ? 1.42594 1.02874 1.41468 0.01217  0.04946  0.18934  46  ASN A O   
306  C CB  . ASN A 46  ? 1.41785 0.93676 1.44891 -0.01835 0.12624  0.16096  46  ASN A CB  
307  C CG  . ASN A 46  ? 1.68406 1.16701 1.74510 -0.04201 0.16850  0.13642  46  ASN A CG  
308  O OD1 . ASN A 46  ? 1.57653 1.03730 1.63979 -0.02239 0.17403  0.14231  46  ASN A OD1 
309  N ND2 . ASN A 46  ? 1.79193 1.27431 1.87809 -0.08563 0.20026  0.10484  46  ASN A ND2 
310  N N   . ARG A 47  ? 1.14140 0.85249 1.20492 -0.02053 0.00707  0.14850  47  ARG A N   
311  C CA  . ARG A 47  ? 1.13686 0.87954 1.17569 -0.01091 -0.02296 0.15846  47  ARG A CA  
312  C C   . ARG A 47  ? 1.14490 0.92433 1.20386 -0.03664 -0.03063 0.13885  47  ARG A C   
313  O O   . ARG A 47  ? 1.23201 1.03019 1.32742 -0.05549 -0.02201 0.11772  47  ARG A O   
314  C CB  . ARG A 47  ? 1.28456 1.07020 1.32684 0.00812  -0.05530 0.16099  47  ARG A CB  
315  C CG  . ARG A 47  ? 1.23081 0.99595 1.25093 0.04494  -0.05388 0.18204  47  ARG A CG  
316  C CD  . ARG A 47  ? 1.37738 1.11790 1.34039 0.07177  -0.05235 0.20851  47  ARG A CD  
317  N NE  . ARG A 47  ? 1.44529 1.19619 1.38371 0.11684  -0.06419 0.22798  47  ARG A NE  
318  C CZ  . ARG A 47  ? 1.51474 1.21478 1.43895 0.14731  -0.04074 0.24655  47  ARG A CZ  
319  N NH1 . ARG A 47  ? 1.49004 1.11743 1.42033 0.13170  0.00066  0.24607  47  ARG A NH1 
320  N NH2 . ARG A 47  ? 1.56941 1.29347 1.47130 0.19548  -0.05629 0.26406  47  ARG A NH2 
321  N N   . LEU A 48  ? 1.21297 1.00551 1.24568 -0.03469 -0.04581 0.14496  48  LEU A N   
322  C CA  . LEU A 48  ? 0.96601 0.78689 1.00848 -0.05086 -0.05194 0.13067  48  LEU A CA  
323  C C   . LEU A 48  ? 1.07776 0.93063 1.11446 -0.04868 -0.07723 0.12698  48  LEU A C   
324  O O   . LEU A 48  ? 1.14372 0.99992 1.15403 -0.03894 -0.08980 0.13561  48  LEU A O   
325  C CB  . LEU A 48  ? 1.17770 0.97701 1.19269 -0.05561 -0.03824 0.13662  48  LEU A CB  
326  C CG  . LEU A 48  ? 1.28909 1.08784 1.32626 -0.07162 -0.01401 0.12253  48  LEU A CG  
327  C CD1 . LEU A 48  ? 1.15773 0.94394 1.16737 -0.07477 -0.00472 0.12710  48  LEU A CD1 
328  C CD2 . LEU A 48  ? 1.31916 1.16632 1.39624 -0.07903 -0.02114 0.10083  48  LEU A CD2 
329  N N   . VAL A 49  ? 1.05019 0.92862 1.10932 -0.05773 -0.08194 0.11213  49  VAL A N   
330  C CA  . VAL A 49  ? 1.13059 1.02938 1.18354 -0.06097 -0.09629 0.10502  49  VAL A CA  
331  C C   . VAL A 49  ? 1.01701 0.90895 1.05132 -0.06656 -0.08848 0.10160  49  VAL A C   
332  O O   . VAL A 49  ? 0.86213 0.75615 0.90679 -0.06496 -0.07780 0.09884  49  VAL A O   
333  C CB  . VAL A 49  ? 0.99754 0.92013 1.08186 -0.06264 -0.10256 0.09366  49  VAL A CB  
334  C CG1 . VAL A 49  ? 1.01582 0.95371 1.09084 -0.06879 -0.11267 0.08536  49  VAL A CG1 
335  C CG2 . VAL A 49  ? 0.96435 0.88644 1.07040 -0.05492 -0.10301 0.09671  49  VAL A CG2 
336  N N   . PHE A 50  ? 1.08629 0.97338 1.09294 -0.07247 -0.09160 0.09922  50  PHE A N   
337  C CA  . PHE A 50  ? 1.02579 0.89403 1.00639 -0.07645 -0.07889 0.09654  50  PHE A CA  
338  C C   . PHE A 50  ? 1.07126 0.93965 1.04552 -0.08463 -0.07684 0.08525  50  PHE A C   
339  O O   . PHE A 50  ? 1.20600 1.08310 1.17166 -0.09798 -0.08216 0.07520  50  PHE A O   
340  C CB  . PHE A 50  ? 0.92871 0.77997 0.87564 -0.08172 -0.07508 0.09998  50  PHE A CB  
341  C CG  . PHE A 50  ? 1.09822 0.94004 1.04450 -0.07433 -0.07082 0.11202  50  PHE A CG  
342  C CD1 . PHE A 50  ? 1.04436 0.89067 0.99897 -0.06754 -0.07838 0.12087  50  PHE A CD1 
343  C CD2 . PHE A 50  ? 1.20701 1.03164 1.14177 -0.07258 -0.05499 0.11453  50  PHE A CD2 
344  C CE1 . PHE A 50  ? 1.19343 1.01857 1.14121 -0.06276 -0.06634 0.13203  50  PHE A CE1 
345  C CE2 . PHE A 50  ? 1.16622 0.98099 1.10089 -0.07018 -0.04613 0.12243  50  PHE A CE2 
346  C CZ  . PHE A 50  ? 1.21074 1.02141 1.15005 -0.06712 -0.04986 0.13118  50  PHE A CZ  
347  N N   . LEU A 51  ? 1.08776 0.95158 1.06602 -0.07587 -0.06786 0.08515  51  LEU A N   
348  C CA  . LEU A 51  ? 1.08548 0.93641 1.04985 -0.08062 -0.05811 0.07754  51  LEU A CA  
349  C C   . LEU A 51  ? 1.01805 0.82532 0.94000 -0.07400 -0.03332 0.08168  51  LEU A C   
350  O O   . LEU A 51  ? 0.98071 0.78606 0.89848 -0.05177 -0.02710 0.09179  51  LEU A O   
351  C CB  . LEU A 51  ? 0.84119 0.71581 0.83238 -0.06953 -0.06397 0.07703  51  LEU A CB  
352  C CG  . LEU A 51  ? 0.89456 0.80440 0.92680 -0.07410 -0.08371 0.07350  51  LEU A CG  
353  C CD1 . LEU A 51  ? 0.71027 0.64438 0.77328 -0.06232 -0.08751 0.07526  51  LEU A CD1 
354  C CD2 . LEU A 51  ? 0.95988 0.88366 1.00457 -0.08452 -0.08904 0.06237  51  LEU A CD2 
355  N N   . GLU A 52  ? 0.98026 0.75505 0.87099 -0.09324 -0.01654 0.07120  52  GLU A N   
356  C CA  . GLU A 52  ? 1.08908 0.80796 0.93264 -0.08882 0.01444  0.07420  52  GLU A CA  
357  C C   . GLU A 52  ? 1.10147 0.78774 0.92131 -0.06929 0.03573  0.08173  52  GLU A C   
358  O O   . GLU A 52  ? 1.30508 1.00731 1.14008 -0.07139 0.02985  0.07797  52  GLU A O   
359  C CB  . GLU A 52  ? 1.30817 1.00208 1.12527 -0.12267 0.03058  0.05438  52  GLU A CB  
360  C CG  . GLU A 52  ? 1.34235 1.01705 1.14680 -0.14804 0.05017  0.03461  52  GLU A CG  
361  C CD  . GLU A 52  ? 1.50520 1.16010 1.28322 -0.18676 0.07244  0.00691  52  GLU A CD  
362  O OE1 . GLU A 52  ? 1.45063 1.12031 1.22550 -0.19277 0.06358  0.00363  52  GLU A OE1 
363  O OE2 . GLU A 52  ? 1.40209 1.02855 1.16180 -0.21368 0.10116  -0.01456 52  GLU A OE2 
364  N N   . ARG A 53  ? 1.19687 0.83526 0.97474 -0.04638 0.06252  0.09385  53  ARG A N   
365  C CA  . ARG A 53  ? 1.16061 0.76506 0.90483 -0.01480 0.08477  0.10752  53  ARG A CA  
366  C C   . ARG A 53  ? 1.28252 0.83098 0.99308 -0.03952 0.11505  0.09608  53  ARG A C   
367  O O   . ARG A 53  ? 1.41277 0.90647 1.09010 -0.06668 0.14514  0.08302  53  ARG A O   
368  C CB  . ARG A 53  ? 1.29413 0.85762 0.99569 0.02148  0.10952  0.12459  53  ARG A CB  
369  C CG  . ARG A 53  ? 1.29074 0.83113 0.95389 0.07070  0.12860  0.14488  53  ARG A CG  
370  C CD  . ARG A 53  ? 1.37349 0.86440 0.98642 0.10976  0.15896  0.16191  53  ARG A CD  
371  N NE  . ARG A 53  ? 1.44588 0.82966 0.98393 0.11661  0.21152  0.17002  53  ARG A NE  
372  C CZ  . ARG A 53  ? 1.53319 0.84278 1.04128 0.07495  0.24512  0.15461  53  ARG A CZ  
373  N NH1 . ARG A 53  ? 1.63663 0.97538 1.18173 0.02743  0.22707  0.13169  53  ARG A NH1 
374  N NH2 . ARG A 53  ? 1.62513 0.82857 1.06101 0.08126  0.30116  0.16084  53  ARG A NH2 
375  N N   . GLY A 54  ? 1.41164 0.97390 1.13013 -0.03331 0.11079  0.09751  54  GLY A N   
376  C CA  . GLY A 54  ? 1.33495 0.83971 1.01742 -0.05367 0.14576  0.08764  54  GLY A CA  
377  C C   . GLY A 54  ? 1.38043 0.93117 1.10675 -0.09193 0.12719  0.06403  54  GLY A C   
378  O O   . GLY A 54  ? 1.31664 0.83013 1.01921 -0.10650 0.15475  0.05535  54  GLY A O   
379  N N   . VAL A 55  ? 1.27412 0.90112 1.06017 -0.10642 0.08506  0.05380  55  VAL A N   
380  C CA  . VAL A 55  ? 1.22721 0.90231 1.05477 -0.13717 0.06763  0.03147  55  VAL A CA  
381  C C   . VAL A 55  ? 1.24535 0.94204 1.08899 -0.11824 0.05784  0.03980  55  VAL A C   
382  O O   . VAL A 55  ? 1.31881 1.05228 1.18517 -0.08802 0.03332  0.05583  55  VAL A O   
383  C CB  . VAL A 55  ? 1.13201 0.87579 1.00959 -0.14761 0.02843  0.02350  55  VAL A CB  
384  C CG1 . VAL A 55  ? 1.45700 1.19173 1.31897 -0.17633 0.03876  0.00526  55  VAL A CG1 
385  C CG2 . VAL A 55  ? 1.15862 0.92716 1.05532 -0.11479 0.00392  0.04616  55  VAL A CG2 
386  N N   . ASN A 56  ? 1.21527 0.89142 1.04687 -0.13814 0.07965  0.02576  56  ASN A N   
387  C CA  . ASN A 56  ? 1.27082 0.97456 1.12158 -0.12667 0.06918  0.02852  56  ASN A CA  
388  C C   . ASN A 56  ? 1.12033 0.90069 1.03730 -0.14784 0.03419  0.00914  56  ASN A C   
389  O O   . ASN A 56  ? 1.12826 0.92353 1.05916 -0.18278 0.03922  -0.01670 56  ASN A O   
390  C CB  . ASN A 56  ? 1.39004 1.03103 1.19282 -0.13670 0.11293  0.02367  56  ASN A CB  
391  C CG  . ASN A 56  ? 1.21083 0.87513 1.02256 -0.11722 0.10418  0.03122  56  ASN A CG  
392  O OD1 . ASN A 56  ? 1.25308 0.91074 1.03980 -0.07476 0.10242  0.05570  56  ASN A OD1 
393  N ND2 . ASN A 56  ? 1.37648 1.07773 1.22574 -0.14656 0.09729  0.00801  56  ASN A ND2 
394  N N   . ILE A 57  ? 1.02169 0.85317 0.97882 -0.12596 0.00096  0.01941  57  ILE A N   
395  C CA  . ILE A 57  ? 1.08023 0.97468 1.09455 -0.13708 -0.02934 0.00648  57  ILE A CA  
396  C C   . ILE A 57  ? 0.92525 0.84898 0.96628 -0.12618 -0.03947 0.00626  57  ILE A C   
397  O O   . ILE A 57  ? 1.13012 1.03719 1.14846 -0.10634 -0.02992 0.01772  57  ILE A O   
398  C CB  . ILE A 57  ? 1.00358 0.92371 1.04067 -0.12537 -0.05429 0.01646  57  ILE A CB  
399  C CG1 . ILE A 57  ? 1.02614 0.95187 1.06848 -0.09702 -0.06241 0.03388  57  ILE A CG1 
400  C CG2 . ILE A 57  ? 1.18993 1.07840 1.19440 -0.13373 -0.04229 0.01777  57  ILE A CG2 
401  C CD1 . ILE A 57  ? 0.94001 0.89438 1.01468 -0.09040 -0.08360 0.03895  57  ILE A CD1 
402  N N   . SER A 58  ? 0.85163 0.82258 0.93885 -0.13686 -0.05812 -0.00784 58  SER A N   
403  C CA  . SER A 58  ? 0.86823 0.87269 0.98993 -0.12790 -0.07055 -0.01059 58  SER A CA  
404  C C   . SER A 58  ? 0.77828 0.81812 0.94181 -0.11857 -0.09548 -0.00764 58  SER A C   
405  O O   . SER A 58  ? 1.00390 1.05278 1.17330 -0.12250 -0.10442 -0.00829 58  SER A O   
406  C CB  . SER A 58  ? 0.88338 0.90338 1.01859 -0.14772 -0.06199 -0.03130 58  SER A CB  
407  O OG  . SER A 58  ? 1.16876 1.14331 1.25813 -0.15608 -0.03133 -0.03257 58  SER A OG  
408  N N   . VAL A 59  ? 0.80937 0.86612 0.99668 -0.10545 -0.10332 -0.00466 59  VAL A N   
409  C CA  . VAL A 59  ? 0.76266 0.83511 0.98113 -0.09679 -0.11703 -0.00054 59  VAL A CA  
410  C C   . VAL A 59  ? 0.81467 0.91212 1.07090 -0.09537 -0.12052 -0.01156 59  VAL A C   
411  O O   . VAL A 59  ? 0.79199 0.89865 1.05083 -0.09695 -0.11467 -0.01977 59  VAL A O   
412  C CB  . VAL A 59  ? 0.80655 0.86775 1.01627 -0.08606 -0.11571 0.01079  59  VAL A CB  
413  C CG1 . VAL A 59  ? 1.04464 1.10553 1.27633 -0.08108 -0.12146 0.01591  59  VAL A CG1 
414  C CG2 . VAL A 59  ? 0.92705 0.96106 1.09619 -0.08481 -0.10855 0.02111  59  VAL A CG2 
415  N N   . ARG A 60  ? 0.80674 0.91379 1.08805 -0.08915 -0.12830 -0.01101 60  ARG A N   
416  C CA  . ARG A 60  ? 0.91439 1.03390 1.23019 -0.08378 -0.12710 -0.01901 60  ARG A CA  
417  C C   . ARG A 60  ? 0.93294 1.03042 1.25507 -0.07357 -0.12250 -0.00887 60  ARG A C   
418  O O   . ARG A 60  ? 0.88041 0.96486 1.19573 -0.06079 -0.12619 0.00443  60  ARG A O   
419  C CB  . ARG A 60  ? 0.99691 1.14223 1.33243 -0.08019 -0.13375 -0.02714 60  ARG A CB  
420  C CG  . ARG A 60  ? 0.94711 1.10359 1.31724 -0.07230 -0.12959 -0.03655 60  ARG A CG  
421  C CD  . ARG A 60  ? 1.29069 1.48671 1.67963 -0.07074 -0.13626 -0.04962 60  ARG A CD  
422  N NE  . ARG A 60  ? 1.40995 1.62883 1.79650 -0.05504 -0.14919 -0.04343 60  ARG A NE  
423  C CZ  . ARG A 60  ? 1.47854 1.71047 1.88064 -0.02572 -0.15428 -0.03664 60  ARG A CZ  
424  N NH1 . ARG A 60  ? 1.53187 1.74127 1.95174 -0.01094 -0.14287 -0.03355 60  ARG A NH1 
425  N NH2 . ARG A 60  ? 1.42776 1.69573 1.82373 -0.00859 -0.16895 -0.03319 60  ARG A NH2 
426  N N   . MET A 61  ? 0.80363 0.89931 1.13564 -0.07992 -0.11201 -0.01722 61  MET A N   
427  C CA  . MET A 61  ? 0.77266 0.84590 1.11035 -0.07930 -0.09930 -0.01473 61  MET A CA  
428  C C   . MET A 61  ? 0.75928 0.82400 1.12629 -0.08088 -0.08338 -0.02772 61  MET A C   
429  O O   . MET A 61  ? 0.96682 1.05605 1.35327 -0.08912 -0.08141 -0.04624 61  MET A O   
430  C CB  . MET A 61  ? 0.90707 0.99532 1.23875 -0.08910 -0.09475 -0.02292 61  MET A CB  
431  C CG  . MET A 61  ? 1.02404 1.11902 1.32431 -0.08521 -0.10535 -0.01267 61  MET A CG  
432  S SD  . MET A 61  ? 0.95402 1.07300 1.24907 -0.08621 -0.09927 -0.02041 61  MET A SD  
433  C CE  . MET A 61  ? 0.87923 0.97350 1.19344 -0.09521 -0.08286 -0.02300 61  MET A CE  
434  N N   . GLN A 62  ? 0.77916 0.80296 1.14440 -0.07271 -0.06790 -0.01782 62  GLN A N   
435  C CA  . GLN A 62  ? 0.80167 0.79700 1.18714 -0.07401 -0.04206 -0.02864 62  GLN A CA  
436  C C   . GLN A 62  ? 0.96667 0.92739 1.34818 -0.08790 -0.01491 -0.03352 62  GLN A C   
437  O O   . GLN A 62  ? 1.18376 1.10496 1.53985 -0.07590 -0.00901 -0.01168 62  GLN A O   
438  C CB  . GLN A 62  ? 0.95409 0.92069 1.33355 -0.04411 -0.04097 -0.00946 62  GLN A CB  
439  C CG  . GLN A 62  ? 1.20924 1.12229 1.59668 -0.03793 -0.00572 -0.01287 62  GLN A CG  
440  C CD  . GLN A 62  ? 1.24642 1.12093 1.61149 0.00433  -0.00224 0.01657  62  GLN A CD  
441  O OE1 . GLN A 62  ? 1.05117 0.96386 1.41744 0.02784  -0.02801 0.02562  62  GLN A OE1 
442  N NE2 . GLN A 62  ? 1.33732 1.13864 1.67912 0.01559  0.03174  0.03064  62  GLN A NE2 
443  N N   . LYS A 63  ? 1.07276 1.05288 1.47871 -0.11473 0.00318  -0.06507 63  LYS A N   
444  C CA  . LYS A 63  ? 1.08131 1.03944 1.48987 -0.13586 0.03338  -0.07943 63  LYS A CA  
445  C C   . LYS A 63  ? 1.25058 1.12870 1.65400 -0.13313 0.07432  -0.07532 63  LYS A C   
446  O O   . LYS A 63  ? 1.31145 1.16961 1.72705 -0.12785 0.08755  -0.08174 63  LYS A O   
447  C CB  . LYS A 63  ? 1.06537 1.08668 1.50467 -0.16707 0.04002  -0.12194 63  LYS A CB  
448  C CG  . LYS A 63  ? 1.06991 1.15339 1.50319 -0.16868 0.01611  -0.12469 63  LYS A CG  
449  C CD  . LYS A 63  ? 0.96166 1.11804 1.42430 -0.19525 0.02560  -0.16936 63  LYS A CD  
450  C CE  . LYS A 63  ? 1.09550 1.29145 1.58104 -0.20432 0.02489  -0.19643 63  LYS A CE  
451  N NZ  . LYS A 63  ? 0.87321 1.15008 1.38771 -0.23144 0.03604  -0.24526 63  LYS A NZ  
452  N N   . GLN A 64  ? 1.31006 1.13608 1.69116 -0.13506 0.09850  -0.06370 64  GLN A N   
453  C CA  . GLN A 64  ? 1.50645 1.24117 1.87293 -0.13294 0.14813  -0.05922 64  GLN A CA  
454  C C   . GLN A 64  ? 1.61198 1.34329 2.00977 -0.17820 0.19309  -0.10733 64  GLN A C   
455  O O   . GLN A 64  ? 1.67194 1.36087 2.07864 -0.18207 0.22527  -0.12055 64  GLN A O   
456  C CB  . GLN A 64  ? 1.53691 1.20935 1.86040 -0.11812 0.16276  -0.02813 64  GLN A CB  
457  C CG  . GLN A 64  ? 1.49044 1.18408 1.78449 -0.08228 0.11724  0.01064  64  GLN A CG  
458  C CD  . GLN A 64  ? 1.65965 1.28531 1.90507 -0.06348 0.13559  0.04262  64  GLN A CD  
459  O OE1 . GLN A 64  ? 1.69900 1.32891 1.93796 -0.08371 0.14148  0.03738  64  GLN A OE1 
460  N NE2 . GLN A 64  ? 1.64696 1.21321 1.85554 -0.02087 0.14473  0.07642  64  GLN A NE2 
461  N N   . ILE A 65  ? 1.59538 1.37552 2.01112 -0.21315 0.19783  -0.13729 65  ILE A N   
462  C CA  . ILE A 65  ? 1.39779 1.20531 1.85074 -0.26212 0.23557  -0.19381 65  ILE A CA  
463  C C   . ILE A 65  ? 1.42896 1.35800 1.91772 -0.27389 0.19568  -0.22437 65  ILE A C   
464  O O   . ILE A 65  ? 1.35948 1.35298 1.84415 -0.26104 0.15473  -0.21294 65  ILE A O   
465  C CB  . ILE A 65  ? 1.53523 1.32417 1.98597 -0.29422 0.27372  -0.21314 65  ILE A CB  
466  C CG1 . ILE A 65  ? 1.68501 1.33994 2.08966 -0.27957 0.32013  -0.17975 65  ILE A CG1 
467  C CG2 . ILE A 65  ? 1.46020 1.30208 1.95682 -0.35058 0.31058  -0.28203 65  ILE A CG2 
468  C CD1 . ILE A 65  ? 1.59865 1.16472 1.99545 -0.27728 0.36650  -0.18240 65  ILE A CD1 
469  N N   . LEU A 66  ? 1.47207 1.42854 1.99090 -0.29564 0.21024  -0.26227 66  LEU A N   
470  C CA  . LEU A 66  ? 1.44682 1.51359 1.99047 -0.29843 0.17175  -0.28585 66  LEU A CA  
471  C C   . LEU A 66  ? 1.52494 1.69169 2.09618 -0.33037 0.17264  -0.33278 66  LEU A C   
472  O O   . LEU A 66  ? 1.47544 1.73364 2.04857 -0.31532 0.13065  -0.33316 66  LEU A O   
473  C CB  . LEU A 66  ? 1.40968 1.47400 1.97278 -0.30754 0.18510  -0.30899 66  LEU A CB  
474  C CG  . LEU A 66  ? 1.38672 1.39754 1.92890 -0.26688 0.16519  -0.26457 66  LEU A CG  
475  C CD1 . LEU A 66  ? 1.42910 1.32102 1.95239 -0.25618 0.20854  -0.24397 66  LEU A CD1 
476  C CD2 . LEU A 66  ? 1.56624 1.63125 2.12939 -0.26954 0.15002  -0.28633 66  LEU A CD2 
477  N N   . SER A 67  ? 1.68967 1.84270 2.28106 -0.37336 0.22313  -0.37469 67  SER A N   
478  C CA  . SER A 67  ? 1.72996 1.99668 2.35573 -0.40722 0.22643  -0.42969 67  SER A CA  
479  C C   . SER A 67  ? 1.63593 1.95170 2.24791 -0.38365 0.19163  -0.40591 67  SER A C   
480  O O   . SER A 67  ? 1.60588 2.04367 2.23961 -0.38736 0.16971  -0.43740 67  SER A O   
481  C CB  . SER A 67  ? 1.70744 1.94017 2.35698 -0.46388 0.29551  -0.48203 67  SER A CB  
482  O OG  . SER A 67  ? 1.64920 1.79982 2.27474 -0.46512 0.32251  -0.45755 67  SER A OG  
483  N N   . GLU A 68  ? 1.44124 1.66804 2.01580 -0.35703 0.18729  -0.35216 68  GLU A N   
484  C CA  . GLU A 68  ? 1.48938 1.75065 2.04912 -0.33767 0.16128  -0.33095 68  GLU A CA  
485  C C   . GLU A 68  ? 1.30074 1.58473 1.83245 -0.28893 0.10474  -0.28551 68  GLU A C   
486  O O   . GLU A 68  ? 1.23442 1.50565 1.75782 -0.27087 0.08543  -0.26891 68  GLU A O   
487  C CB  . GLU A 68  ? 1.40024 1.55782 1.93218 -0.33959 0.19151  -0.30266 68  GLU A CB  
488  C CG  . GLU A 68  ? 1.38971 1.51936 1.94265 -0.39036 0.25477  -0.34788 68  GLU A CG  
489  C CD  . GLU A 68  ? 1.55008 1.57980 2.06717 -0.38796 0.28394  -0.31641 68  GLU A CD  
490  O OE1 . GLU A 68  ? 1.44457 1.42645 1.92056 -0.34535 0.25307  -0.25896 68  GLU A OE1 
491  O OE2 . GLU A 68  ? 1.75447 1.75395 2.28289 -0.43083 0.34073  -0.35177 68  GLU A OE2 
492  N N   . LYS A 69  ? 1.16472 1.47846 1.68062 -0.26956 0.08297  -0.26718 69  LYS A N   
493  C CA  . LYS A 69  ? 0.87976 1.20046 1.36264 -0.22686 0.03926  -0.22473 69  LYS A CA  
494  C C   . LYS A 69  ? 0.99674 1.21172 1.44398 -0.20727 0.03481  -0.17494 69  LYS A C   
495  O O   . LYS A 69  ? 1.18967 1.32758 1.63139 -0.21913 0.06395  -0.16740 69  LYS A O   
496  C CB  . LYS A 69  ? 0.82575 1.19941 1.30134 -0.21378 0.02665  -0.22273 69  LYS A CB  
497  C CG  . LYS A 69  ? 0.85476 1.16438 1.31981 -0.22574 0.05121  -0.21043 69  LYS A CG  
498  C CD  . LYS A 69  ? 0.78219 1.16217 1.25604 -0.22450 0.04966  -0.22677 69  LYS A CD  
499  C CE  . LYS A 69  ? 0.91480 1.33150 1.43104 -0.27066 0.09092  -0.28070 69  LYS A CE  
500  N NZ  . LYS A 69  ? 0.99783 1.49709 1.53015 -0.27154 0.09148  -0.30345 69  LYS A NZ  
501  N N   . PRO A 70  ? 0.99610 1.20736 1.41637 -0.17633 0.00123  -0.14220 70  PRO A N   
502  C CA  . PRO A 70  ? 1.05012 1.18117 1.44018 -0.15846 -0.00554 -0.10132 70  PRO A CA  
503  C C   . PRO A 70  ? 1.08355 1.17026 1.44627 -0.15121 -0.00169 -0.07604 70  PRO A C   
504  O O   . PRO A 70  ? 1.13302 1.15243 1.48370 -0.15301 0.01809  -0.06178 70  PRO A O   
505  C CB  . PRO A 70  ? 0.82241 0.97668 1.19492 -0.13543 -0.03797 -0.08422 70  PRO A CB  
506  C CG  . PRO A 70  ? 0.99657 1.22642 1.39053 -0.14098 -0.04275 -0.11508 70  PRO A CG  
507  C CD  . PRO A 70  ? 0.80426 1.08304 1.21975 -0.15765 -0.02727 -0.14482 70  PRO A CD  
508  N N   . TYR A 71  ? 1.02727 1.14943 1.37619 -0.14027 -0.01777 -0.07001 71  TYR A N   
509  C CA  . TYR A 71  ? 0.93778 1.02108 1.25549 -0.13000 -0.01940 -0.04360 71  TYR A CA  
510  C C   . TYR A 71  ? 1.02844 1.16081 1.35328 -0.13408 -0.01436 -0.05973 71  TYR A C   
511  O O   . TYR A 71  ? 1.04264 1.24742 1.39643 -0.14168 -0.01270 -0.09136 71  TYR A O   
512  C CB  . TYR A 71  ? 0.82379 0.88875 1.10781 -0.10651 -0.04607 -0.01329 71  TYR A CB  
513  C CG  . TYR A 71  ? 0.92110 1.03485 1.20099 -0.09348 -0.06509 -0.01748 71  TYR A CG  
514  C CD1 . TYR A 71  ? 0.85523 1.00586 1.12422 -0.08177 -0.06879 -0.01978 71  TYR A CD1 
515  C CD2 . TYR A 71  ? 0.96846 1.08664 1.24980 -0.08896 -0.07660 -0.01683 71  TYR A CD2 
516  C CE1 . TYR A 71  ? 0.99900 1.18370 1.25297 -0.06213 -0.08150 -0.01856 71  TYR A CE1 
517  C CE2 . TYR A 71  ? 0.81568 0.96683 1.08359 -0.07511 -0.08838 -0.01765 71  TYR A CE2 
518  C CZ  . TYR A 71  ? 0.94941 1.13007 1.20028 -0.05967 -0.08996 -0.01671 71  TYR A CZ  
519  O OH  . TYR A 71  ? 0.88474 1.08865 1.11184 -0.03855 -0.09717 -0.01294 71  TYR A OH  
520  N N   . VAL A 72  ? 1.01436 1.11439 1.31281 -0.12741 -0.01218 -0.03977 72  VAL A N   
521  C CA  . VAL A 72  ? 0.84981 0.99312 1.15158 -0.12659 -0.00763 -0.05128 72  VAL A CA  
522  C C   . VAL A 72  ? 0.84173 0.97114 1.10409 -0.09948 -0.02768 -0.02219 72  VAL A C   
523  O O   . VAL A 72  ? 1.04257 1.11039 1.27362 -0.09566 -0.02900 0.00402  72  VAL A O   
524  C CB  . VAL A 72  ? 1.04153 1.15260 1.34846 -0.14970 0.02423  -0.05973 72  VAL A CB  
525  C CG1 . VAL A 72  ? 0.95407 1.12638 1.27440 -0.15149 0.03050  -0.07974 72  VAL A CG1 
526  C CG2 . VAL A 72  ? 0.93177 1.02879 1.26836 -0.17953 0.05384  -0.08597 72  VAL A CG2 
527  N N   . ALA A 73  ? 0.75387 0.93959 1.01391 -0.07914 -0.04037 -0.02756 73  ALA A N   
528  C CA  . ALA A 73  ? 0.83070 0.99095 1.04797 -0.05309 -0.05284 -0.00061 73  ALA A CA  
529  C C   . ALA A 73  ? 0.93927 1.12147 1.14708 -0.04010 -0.04563 -0.00125 73  ALA A C   
530  O O   . ALA A 73  ? 0.91458 1.16358 1.15355 -0.04279 -0.03797 -0.02734 73  ALA A O   
531  C CB  . ALA A 73  ? 0.83982 1.02529 1.04458 -0.03080 -0.06755 0.00264  73  ALA A CB  
532  N N   . PHE A 74  ? 0.94320 1.07391 1.10911 -0.02702 -0.04663 0.02405  74  PHE A N   
533  C CA  . PHE A 74  ? 0.96098 1.10162 1.11001 -0.00973 -0.03867 0.02770  74  PHE A CA  
534  C C   . PHE A 74  ? 0.88686 0.98764 0.98651 0.01703  -0.04225 0.05130  74  PHE A C   
535  O O   . PHE A 74  ? 0.91556 0.95090 0.98551 0.00691  -0.04167 0.06790  74  PHE A O   
536  C CB  . PHE A 74  ? 0.88622 0.98602 1.03024 -0.02994 -0.02466 0.03195  74  PHE A CB  
537  C CG  . PHE A 74  ? 0.91621 1.02907 1.09795 -0.05976 -0.01119 0.01172  74  PHE A CG  
538  C CD1 . PHE A 74  ? 0.90824 1.08314 1.12481 -0.06801 0.00354  -0.01675 74  PHE A CD1 
539  C CD2 . PHE A 74  ? 1.04124 1.10361 1.22180 -0.07885 -0.00921 0.01945  74  PHE A CD2 
540  C CE1 . PHE A 74  ? 0.99548 1.17280 1.24380 -0.10120 0.02481  -0.03929 74  PHE A CE1 
541  C CE2 . PHE A 74  ? 0.98298 1.04060 1.18990 -0.10466 0.01174  0.00267  74  PHE A CE2 
542  C CZ  . PHE A 74  ? 1.14112 1.25135 1.38128 -0.11925 0.03135  -0.02779 74  PHE A CZ  
543  N N   . ARG A 75  ? 0.90735 1.04760 0.99522 0.05184  -0.04292 0.05129  75  ARG A N   
544  C CA  . ARG A 75  ? 0.95616 1.04756 0.99004 0.07995  -0.03748 0.07388  75  ARG A CA  
545  C C   . ARG A 75  ? 1.03638 1.12164 1.04341 0.10744  -0.02309 0.08227  75  ARG A C   
546  O O   . ARG A 75  ? 1.05435 1.20989 1.08773 0.12284  -0.02306 0.06787  75  ARG A O   
547  C CB  . ARG A 75  ? 0.95428 1.08077 0.98045 0.10793  -0.04419 0.07390  75  ARG A CB  
548  C CG  . ARG A 75  ? 0.88742 1.02781 0.94413 0.08154  -0.05746 0.06222  75  ARG A CG  
549  C CD  . ARG A 75  ? 0.87395 1.07551 0.93296 0.10890  -0.06542 0.05471  75  ARG A CD  
550  N NE  . ARG A 75  ? 1.36379 1.51842 1.36161 0.14421  -0.05509 0.07891  75  ARG A NE  
551  C CZ  . ARG A 75  ? 1.36706 1.56318 1.33930 0.19042  -0.05468 0.08389  75  ARG A CZ  
552  N NH1 . ARG A 75  ? 1.19419 1.49780 1.20115 0.20864  -0.06816 0.06245  75  ARG A NH1 
553  N NH2 . ARG A 75  ? 1.11795 1.24714 1.02473 0.22016  -0.03735 0.10960  75  ARG A NH2 
554  N N   . LEU A 76  ? 0.93805 0.94356 0.89367 0.11319  -0.00831 0.10199  76  LEU A N   
555  C CA  . LEU A 76  ? 1.02513 1.00988 0.95080 0.13710  0.00980  0.11079  76  LEU A CA  
556  C C   . LEU A 76  ? 1.03937 0.99207 0.91000 0.18502  0.02657  0.12956  76  LEU A C   
557  O O   . LEU A 76  ? 1.20762 1.08718 1.03684 0.17978  0.03877  0.14192  76  LEU A O   
558  C CB  . LEU A 76  ? 0.89686 0.80934 0.80108 0.10532  0.02080  0.11608  76  LEU A CB  
559  C CG  . LEU A 76  ? 1.15605 1.09090 1.09359 0.07786  0.01710  0.10454  76  LEU A CG  
560  C CD1 . LEU A 76  ? 1.09744 1.05731 1.07716 0.04468  -0.00031 0.09337  76  LEU A CD1 
561  C CD2 . LEU A 76  ? 1.39396 1.25950 1.29475 0.06013  0.03131  0.11246  76  LEU A CD2 
562  N N   . ASN A 77  ? 1.02103 1.02701 0.88840 0.23273  0.03085  0.13088  77  ASN A N   
563  C CA  . ASN A 77  ? 1.25649 1.22581 1.06160 0.29000  0.05200  0.15369  77  ASN A CA  
564  C C   . ASN A 77  ? 1.33737 1.19749 1.08670 0.28771  0.08469  0.16977  77  ASN A C   
565  O O   . ASN A 77  ? 1.28598 1.11460 1.04820 0.24403  0.08664  0.16130  77  ASN A O   
566  C CB  . ASN A 77  ? 1.21125 1.28088 1.02908 0.34836  0.04612  0.14958  77  ASN A CB  
567  C CG  . ASN A 77  ? 1.42660 1.53486 1.27377 0.34504  0.04937  0.13643  77  ASN A CG  
568  O OD1 . ASN A 77  ? 1.54132 1.59242 1.34658 0.36902  0.07403  0.15172  77  ASN A OD1 
569  N ND2 . ASN A 77  ? 1.52087 1.72302 1.43866 0.31403  0.02900  0.10618  77  ASN A ND2 
570  N N   . GLY A 78  ? 1.54296 1.34069 1.22421 0.33623  0.11387  0.19305  78  GLY A N   
571  C CA  . GLY A 78  ? 1.56380 1.24802 1.18497 0.33506  0.15355  0.20610  78  GLY A CA  
572  C C   . GLY A 78  ? 1.58282 1.28136 1.21879 0.33433  0.15880  0.19921  78  GLY A C   
573  O O   . GLY A 78  ? 1.61647 1.24912 1.23989 0.29323  0.17424  0.19359  78  GLY A O   
574  N N   . ASP A 79  ? 1.50853 1.29915 1.17043 0.38049  0.14735  0.19700  79  ASP A N   
575  C CA  . ASP A 79  ? 1.64302 1.45345 1.32019 0.38313  0.15496  0.18901  79  ASP A CA  
576  C C   . ASP A 79  ? 1.55053 1.37707 1.27991 0.31203  0.13695  0.16645  79  ASP A C   
577  O O   . ASP A 79  ? 1.51282 1.27913 1.22453 0.28541  0.15468  0.16500  79  ASP A O   
578  C CB  . ASP A 79  ? 1.66475 1.59771 1.37391 0.44085  0.14124  0.18275  79  ASP A CB  
579  C CG  . ASP A 79  ? 1.76931 1.67160 1.41417 0.52249  0.17160  0.20828  79  ASP A CG  
580  O OD1 . ASP A 79  ? 1.78697 1.58510 1.38014 0.52635  0.20800  0.22200  79  ASP A OD1 
581  O OD2 . ASP A 79  ? 1.87400 1.85843 1.51774 0.58527  0.16040  0.21393  79  ASP A OD2 
582  N N   . MET A 80  ? 1.42784 1.33411 1.21771 0.28330  0.10444  0.14878  80  MET A N   
583  C CA  . MET A 80  ? 1.41557 1.33128 1.24818 0.22234  0.09060  0.13126  80  MET A CA  
584  C C   . MET A 80  ? 1.44510 1.26355 1.24477 0.17847  0.09839  0.13786  80  MET A C   
585  O O   . MET A 80  ? 1.48298 1.27404 1.28305 0.14448  0.10279  0.13214  80  MET A O   
586  C CB  . MET A 80  ? 1.30248 1.30492 1.19673 0.20238  0.06178  0.11264  80  MET A CB  
587  C CG  . MET A 80  ? 1.37289 1.37680 1.30417 0.14649  0.05340  0.09797  80  MET A CG  
588  S SD  . MET A 80  ? 1.76512 1.87892 1.77145 0.12916  0.03403  0.06888  80  MET A SD  
589  C CE  . MET A 80  ? 1.45310 1.66866 1.48124 0.17621  0.04109  0.05283  80  MET A CE  
590  N N   . LEU A 81  ? 1.60202 1.37591 1.37446 0.17727  0.09982  0.14689  81  LEU A N   
591  C CA  . LEU A 81  ? 1.60070 1.29709 1.34557 0.13442  0.10802  0.14640  81  LEU A CA  
592  C C   . LEU A 81  ? 1.68152 1.30149 1.37654 0.13220  0.14102  0.14974  81  LEU A C   
593  O O   . LEU A 81  ? 1.72942 1.32209 1.42078 0.09065  0.14186  0.13997  81  LEU A O   
594  C CB  . LEU A 81  ? 1.58686 1.24887 1.30829 0.13624  0.11160  0.15256  81  LEU A CB  
595  C CG  . LEU A 81  ? 1.56526 1.16631 1.26729 0.08740  0.11890  0.14398  81  LEU A CG  
596  C CD1 . LEU A 81  ? 1.51620 1.16197 1.26485 0.04557  0.08844  0.13054  81  LEU A CD1 
597  C CD2 . LEU A 81  ? 1.54949 1.11800 1.22966 0.08754  0.12742  0.14696  81  LEU A CD2 
598  N N   . ARG A 82  ? 1.53133 1.11611 1.18380 0.17942  0.17017  0.16328  82  ARG A N   
599  C CA  . ARG A 82  ? 1.54888 1.05255 1.15007 0.17958  0.20826  0.16551  82  ARG A CA  
600  C C   . ARG A 82  ? 1.57417 1.11009 1.20092 0.16335  0.20205  0.15498  82  ARG A C   
601  O O   . ARG A 82  ? 1.32656 0.81052 0.92969 0.12873  0.21794  0.14610  82  ARG A O   
602  C CB  . ARG A 82  ? 1.71764 1.17862 1.26681 0.24446  0.24279  0.18585  82  ARG A CB  
603  C CG  . ARG A 82  ? 1.84011 1.19281 1.32203 0.24619  0.28164  0.19563  82  ARG A CG  
604  C CD  . ARG A 82  ? 1.88557 1.24826 1.34476 0.30809  0.28527  0.21812  82  ARG A CD  
605  N NE  . ARG A 82  ? 2.17659 1.57606 1.62517 0.38039  0.29238  0.23439  82  ARG A NE  
606  C CZ  . ARG A 82  ? 2.09059 1.53590 1.52801 0.44746  0.28656  0.25292  82  ARG A CZ  
607  N NH1 . ARG A 82  ? 1.81133 1.26344 1.24342 0.45102  0.27542  0.25933  82  ARG A NH1 
608  N NH2 . ARG A 82  ? 2.22065 1.71325 1.65182 0.51465  0.29157  0.26396  82  ARG A NH2 
609  N N   . HIS A 83  ? 1.59093 1.21510 1.26421 0.18734  0.18213  0.15294  83  HIS A N   
610  C CA  . HIS A 83  ? 1.57684 1.23335 1.27558 0.17130  0.17998  0.14172  83  HIS A CA  
611  C C   . HIS A 83  ? 1.57938 1.23359 1.29767 0.11158  0.16166  0.13026  83  HIS A C   
612  O O   . HIS A 83  ? 1.68328 1.30753 1.38549 0.08723  0.17301  0.12461  83  HIS A O   
613  C CB  . HIS A 83  ? 1.45942 1.22048 1.20978 0.20306  0.16465  0.13507  83  HIS A CB  
614  C CG  . HIS A 83  ? 1.40661 1.18228 1.13467 0.27001  0.18374  0.14556  83  HIS A CG  
615  N ND1 . HIS A 83  ? 1.37450 1.05956 1.03729 0.29763  0.22049  0.16114  83  HIS A ND1 
616  C CD2 . HIS A 83  ? 1.40482 1.27842 1.16492 0.31798  0.17329  0.14146  83  HIS A CD2 
617  C CE1 . HIS A 83  ? 1.41108 1.13122 1.06261 0.36578  0.23186  0.17130  83  HIS A CE1 
618  N NE2 . HIS A 83  ? 1.55778 1.40054 1.26941 0.38036  0.20097  0.15867  83  HIS A NE2 
619  N N   . LEU A 84  ? 1.43304 1.12160 1.18390 0.09158  0.13385  0.12735  84  LEU A N   
620  C CA  . LEU A 84  ? 1.41256 1.09370 1.17293 0.04429  0.11759  0.12075  84  LEU A CA  
621  C C   . LEU A 84  ? 1.51752 1.12692 1.22902 0.01883  0.13242  0.11863  84  LEU A C   
622  O O   . LEU A 84  ? 1.52625 1.12493 1.22828 -0.01143 0.13001  0.11213  84  LEU A O   
623  C CB  . LEU A 84  ? 1.42649 1.14756 1.22367 0.03437  0.08997  0.11947  84  LEU A CB  
624  C CG  . LEU A 84  ? 1.18366 0.90285 0.99079 -0.00403 0.07157  0.11590  84  LEU A CG  
625  C CD1 . LEU A 84  ? 1.32286 1.06107 1.14608 -0.01757 0.07104  0.11308  84  LEU A CD1 
626  C CD2 . LEU A 84  ? 1.36466 1.11632 1.20431 -0.00687 0.04945  0.11523  84  LEU A CD2 
627  N N   . LYS A 85  ? 1.43968 1.00177 1.11804 0.02920  0.14972  0.12171  85  LYS A N   
628  C CA  . LYS A 85  ? 1.40838 0.90322 1.04073 0.00015  0.17185  0.11187  85  LYS A CA  
629  C C   . LYS A 85  ? 1.67523 1.13553 1.27723 -0.00679 0.19620  0.10595  85  LYS A C   
630  O O   . LYS A 85  ? 1.77904 1.23139 1.36840 -0.04419 0.19425  0.09195  85  LYS A O   
631  C CB  . LYS A 85  ? 1.32833 0.76476 0.92350 0.01764  0.19996  0.11669  85  LYS A CB  
632  C CG  . LYS A 85  ? 1.53891 0.88926 1.07693 -0.00665 0.24195  0.10334  85  LYS A CG  
633  C CD  . LYS A 85  ? 1.71232 0.98658 1.20188 0.02685  0.28423  0.11539  85  LYS A CD  
634  C CE  . LYS A 85  ? 1.72276 0.89695 1.14984 0.00527  0.33871  0.10097  85  LYS A CE  
635  N NZ  . LYS A 85  ? 1.80847 0.89181 1.17940 0.03695  0.38703  0.11467  85  LYS A NZ  
636  N N   . ASP A 86  ? 1.64024 1.08494 1.22885 0.03202  0.21942  0.11562  86  ASP A N   
637  C CA  . ASP A 86  ? 1.59658 1.00409 1.15472 0.02882  0.24711  0.10979  86  ASP A CA  
638  C C   . ASP A 86  ? 1.62990 1.08559 1.21517 0.00455  0.22556  0.10310  86  ASP A C   
639  O O   . ASP A 86  ? 1.57945 1.00688 1.13693 -0.02399 0.23784  0.09139  86  ASP A O   
640  C CB  . ASP A 86  ? 1.56604 0.95912 1.10974 0.08403  0.27385  0.12322  86  ASP A CB  
641  C CG  . ASP A 86  ? 1.65678 0.99092 1.16125 0.11641  0.30063  0.13536  86  ASP A CG  
642  O OD1 . ASP A 86  ? 1.88371 1.16723 1.36285 0.08531  0.31049  0.12781  86  ASP A OD1 
643  O OD2 . ASP A 86  ? 1.72334 1.06327 1.21971 0.17455  0.31407  0.15166  86  ASP A OD2 
644  N N   . ALA A 87  ? 1.57486 1.10071 1.21050 0.01522  0.19772  0.10897  87  ALA A N   
645  C CA  . ALA A 87  ? 1.47637 1.03690 1.13250 -0.00812 0.18303  0.10463  87  ALA A CA  
646  C C   . ALA A 87  ? 1.47122 1.01827 1.10957 -0.04821 0.16828  0.09841  87  ALA A C   
647  O O   . ALA A 87  ? 1.61345 1.15127 1.23065 -0.06848 0.17258  0.09325  87  ALA A O   
648  C CB  . ALA A 87  ? 1.25375 0.88434 0.96614 0.00321  0.16105  0.10768  87  ALA A CB  
649  N N   . LEU A 88  ? 1.56403 1.11685 1.21014 -0.05750 0.15023  0.09803  88  LEU A N   
650  C CA  . LEU A 88  ? 1.54414 1.09960 1.17630 -0.09017 0.13394  0.08952  88  LEU A CA  
651  C C   . LEU A 88  ? 1.39617 0.90778 0.98008 -0.11373 0.15683  0.07164  88  LEU A C   
652  O O   . LEU A 88  ? 1.49651 1.02219 1.06328 -0.14031 0.14604  0.05999  88  LEU A O   
653  C CB  . LEU A 88  ? 1.57530 1.15413 1.23227 -0.09265 0.11100  0.09056  88  LEU A CB  
654  C CG  . LEU A 88  ? 1.46796 1.09406 1.17065 -0.08131 0.08565  0.10273  88  LEU A CG  
655  C CD1 . LEU A 88  ? 1.52821 1.17494 1.25338 -0.08422 0.06487  0.10220  88  LEU A CD1 
656  C CD2 . LEU A 88  ? 1.37638 1.01626 1.07468 -0.09289 0.07617  0.10686  88  LEU A CD2 
657  N N   . MET A 89  ? 1.46505 0.92503 1.02397 -0.10332 0.19039  0.06779  89  MET A N   
658  C CA  . MET A 89  ? 1.76426 1.17410 1.27528 -0.13024 0.22113  0.04610  89  MET A CA  
659  C C   . MET A 89  ? 1.82418 1.22293 1.31266 -0.13393 0.23628  0.04242  89  MET A C   
660  O O   . MET A 89  ? 1.96496 1.33938 1.41599 -0.16443 0.25464  0.01997  89  MET A O   
661  C CB  . MET A 89  ? 1.93684 1.27726 1.41988 -0.11682 0.26106  0.04446  89  MET A CB  
662  C CG  . MET A 89  ? 1.84570 1.18318 1.33825 -0.12063 0.25539  0.04328  89  MET A CG  
663  S SD  . MET A 89  ? 2.18269 1.51815 1.65656 -0.18074 0.26038  0.00517  89  MET A SD  
664  C CE  . MET A 89  ? 1.69678 1.12337 1.22616 -0.18342 0.20215  0.01196  89  MET A CE  
665  N N   . ILE A 90  ? 1.68132 1.10180 1.19273 -0.10652 0.23087  0.06000  90  ILE A N   
666  C CA  . ILE A 90  ? 1.50303 0.91961 0.99631 -0.11228 0.24319  0.05659  90  ILE A CA  
667  C C   . ILE A 90  ? 1.53877 1.00099 1.03920 -0.13097 0.21331  0.05901  90  ILE A C   
668  O O   . ILE A 90  ? 1.64954 1.10610 1.11593 -0.15210 0.21934  0.04819  90  ILE A O   
669  C CB  . ILE A 90  ? 1.42201 0.84042 0.93421 -0.07454 0.25927  0.06961  90  ILE A CB  
670  C CG1 . ILE A 90  ? 1.48196 0.84154 0.96670 -0.05042 0.29710  0.06846  90  ILE A CG1 
671  C CG2 . ILE A 90  ? 1.58259 1.01091 1.08750 -0.08194 0.26690  0.06732  90  ILE A CG2 
672  C CD1 . ILE A 90  ? 1.42151 0.79750 0.92787 -0.00184 0.30866  0.08204  90  ILE A CD1 
673  N N   . ILE A 91  ? 1.52810 1.03242 1.06711 -0.12197 0.18337  0.07318  91  ILE A N   
674  C CA  . ILE A 91  ? 1.53290 1.06868 1.07484 -0.12982 0.16193  0.08197  91  ILE A CA  
675  C C   . ILE A 91  ? 1.65097 1.20175 1.16428 -0.15236 0.14308  0.07223  91  ILE A C   
676  O O   . ILE A 91  ? 1.75489 1.31151 1.23420 -0.16289 0.14155  0.07027  91  ILE A O   
677  C CB  . ILE A 91  ? 1.46839 1.03668 1.05993 -0.11288 0.14335  0.09772  91  ILE A CB  
678  C CG1 . ILE A 91  ? 1.52154 1.09513 1.14081 -0.09346 0.16242  0.10069  91  ILE A CG1 
679  C CG2 . ILE A 91  ? 1.48833 1.07558 1.07583 -0.11955 0.12384  0.10882  91  ILE A CG2 
680  C CD1 . ILE A 91  ? 1.26230 0.87518 0.93439 -0.07990 0.14976  0.10708  91  ILE A CD1 
681  N N   . TYR A 92  ? 1.64511 1.20819 1.17007 -0.15886 0.12938  0.06397  92  TYR A N   
682  C CA  . TYR A 92  ? 1.71683 1.31364 1.22435 -0.17830 0.10841  0.04997  92  TYR A CA  
683  C C   . TYR A 92  ? 1.90967 1.49119 1.38623 -0.20790 0.12833  0.01694  92  TYR A C   
684  O O   . TYR A 92  ? 1.88529 1.50724 1.35303 -0.22822 0.11274  -0.00374 92  TYR A O   
685  C CB  . TYR A 92  ? 1.60117 1.23193 1.14592 -0.16975 0.08026  0.05797  92  TYR A CB  
686  C CG  . TYR A 92  ? 1.67757 1.33012 1.24045 -0.14894 0.05936  0.08406  92  TYR A CG  
687  C CD1 . TYR A 92  ? 1.79220 1.47749 1.33253 -0.14620 0.03834  0.08942  92  TYR A CD1 
688  C CD2 . TYR A 92  ? 1.76338 1.40380 1.36159 -0.13103 0.06452  0.10158  92  TYR A CD2 
689  C CE1 . TYR A 92  ? 1.92820 1.61689 1.47568 -0.12514 0.02765  0.11536  92  TYR A CE1 
690  C CE2 . TYR A 92  ? 1.81446 1.46498 1.42621 -0.11799 0.05426  0.12110  92  TYR A CE2 
691  C CZ  . TYR A 92  ? 1.74399 1.40991 1.32738 -0.11462 0.03840  0.12985  92  TYR A CZ  
692  O OH  . TYR A 92  ? 1.61948 1.27952 1.20737 -0.09933 0.03605  0.15147  92  TYR A OH  
693  N N   . GLY A 93  ? 1.93506 1.46150 1.39447 -0.21090 0.16520  0.00884  93  GLY A N   
694  C CA  . GLY A 93  ? 2.01622 1.51294 1.44212 -0.24251 0.19477  -0.02513 93  GLY A CA  
695  C C   . GLY A 93  ? 2.19974 1.65756 1.63584 -0.24437 0.21483  -0.03213 93  GLY A C   
696  O O   . GLY A 93  ? 2.04411 1.52004 1.51483 -0.22771 0.19453  -0.01634 93  GLY A O   
697  N N   . MET A 94  ? 2.87407 2.27144 2.27453 -0.26559 0.25978  -0.05684 94  MET A N   
698  C CA  . MET A 94  ? 2.88706 2.22485 2.28174 -0.26598 0.29221  -0.06226 94  MET A CA  
699  C C   . MET A 94  ? 2.86927 2.23881 2.26995 -0.30529 0.28551  -0.09392 94  MET A C   
700  O O   . MET A 94  ? 2.90342 2.33655 2.30265 -0.33803 0.26579  -0.12205 94  MET A O   
701  C CB  . MET A 94  ? 3.04398 2.28946 2.39060 -0.27219 0.35265  -0.07610 94  MET A CB  
702  C CG  . MET A 94  ? 3.00102 2.21735 2.34021 -0.23330 0.36492  -0.05011 94  MET A CG  
703  S SD  . MET A 94  ? 3.19039 2.38566 2.55528 -0.16694 0.36425  -0.00582 94  MET A SD  
704  C CE  . MET A 94  ? 3.07087 2.19403 2.41041 -0.17194 0.40114  -0.01371 94  MET A CE  
705  N N   . SER A 95  ? 2.39100 1.72038 1.79703 -0.29981 0.30327  -0.09031 95  SER A N   
706  C CA  . SER A 95  ? 2.25699 1.60563 1.66804 -0.33987 0.30775  -0.12401 95  SER A CA  
707  C C   . SER A 95  ? 2.24369 1.49429 1.62696 -0.34251 0.36283  -0.12811 95  SER A C   
708  O O   . SER A 95  ? 2.07061 1.23913 1.42668 -0.30757 0.39638  -0.10258 95  SER A O   
709  C CB  . SER A 95  ? 2.11590 1.55189 1.57761 -0.32782 0.25159  -0.11032 95  SER A CB  
710  O OG  . SER A 95  ? 1.96679 1.48919 1.44262 -0.33190 0.20845  -0.11403 95  SER A OG  
711  N N   . ARG A 103 ? 2.03293 1.94874 1.82229 -0.46756 0.12724  -0.27465 103 ARG A N   
712  C CA  . ARG A 103 ? 2.05469 1.90101 1.84149 -0.46487 0.15469  -0.26116 103 ARG A CA  
713  C C   . ARG A 103 ? 1.80609 1.73158 1.64661 -0.44182 0.11065  -0.25066 103 ARG A C   
714  O O   . ARG A 103 ? 1.88207 1.79004 1.73204 -0.45487 0.13013  -0.25991 103 ARG A O   
715  C CB  . ARG A 103 ? 2.22190 2.01755 1.98256 -0.52514 0.21971  -0.31091 103 ARG A CB  
716  C CG  . ARG A 103 ? 2.25249 1.96303 1.95680 -0.55451 0.27301  -0.32891 103 ARG A CG  
717  C CD  . ARG A 103 ? 2.38834 1.97950 2.04570 -0.50747 0.29051  -0.27240 103 ARG A CD  
718  N NE  . ARG A 103 ? 2.63201 2.14254 2.23554 -0.53408 0.34332  -0.29121 103 ARG A NE  
719  C CZ  . ARG A 103 ? 2.52692 1.91333 2.07503 -0.55585 0.41727  -0.30091 103 ARG A CZ  
720  N NH1 . ARG A 103 ? 2.38571 1.71242 1.92072 -0.55406 0.44821  -0.29259 103 ARG A NH1 
721  N NH2 . ARG A 103 ? 2.40492 1.72044 1.90512 -0.57975 0.46527  -0.31977 103 ARG A NH2 
722  N N   . SER A 104 ? 1.44984 1.45818 1.32151 -0.40792 0.05559  -0.23250 104 SER A N   
723  C CA  . SER A 104 ? 1.60488 1.69344 1.52633 -0.38416 0.01446  -0.22522 104 SER A CA  
724  C C   . SER A 104 ? 1.68451 1.73980 1.61379 -0.32916 -0.01321 -0.16757 104 SER A C   
725  O O   . SER A 104 ? 1.77891 1.78917 1.68419 -0.30584 -0.01634 -0.13687 104 SER A O   
726  C CB  . SER A 104 ? 1.58438 1.80070 1.53323 -0.38444 -0.02385 -0.25240 104 SER A CB  
727  O OG  . SER A 104 ? 1.68389 1.90611 1.61305 -0.35471 -0.04804 -0.22624 104 SER A OG  
728  N N   . MET A 105 ? 1.81049 1.88967 1.77489 -0.31216 -0.02966 -0.15733 105 MET A N   
729  C CA  . MET A 105 ? 1.74079 1.79481 1.71749 -0.26669 -0.05188 -0.11096 105 MET A CA  
730  C C   . MET A 105 ? 1.72344 1.80764 1.70240 -0.23424 -0.08462 -0.08680 105 MET A C   
731  O O   . MET A 105 ? 1.70550 1.74488 1.67745 -0.20606 -0.08920 -0.05140 105 MET A O   
732  C CB  . MET A 105 ? 1.66553 1.75895 1.68370 -0.25720 -0.06688 -0.11214 105 MET A CB  
733  C CG  . MET A 105 ? 1.67311 1.73484 1.70387 -0.21911 -0.08069 -0.07225 105 MET A CG  
734  S SD  . MET A 105 ? 1.83314 1.96070 1.91702 -0.20178 -0.10742 -0.07425 105 MET A SD  
735  C CE  . MET A 105 ? 1.53464 1.61427 1.62561 -0.16661 -0.11394 -0.03404 105 MET A CE  
736  N N   . SER A 106 ? 1.63684 1.80010 1.62360 -0.23694 -0.10562 -0.10702 106 SER A N   
737  C CA  . SER A 106 ? 1.55899 1.74671 1.53748 -0.20285 -0.13300 -0.08248 106 SER A CA  
738  C C   . SER A 106 ? 1.63936 1.75913 1.57852 -0.20170 -0.11776 -0.06320 106 SER A C   
739  O O   . SER A 106 ? 1.68798 1.79348 1.61828 -0.17055 -0.13160 -0.03159 106 SER A O   
740  C CB  . SER A 106 ? 1.79823 2.08899 1.78198 -0.20518 -0.15503 -0.11174 106 SER A CB  
741  O OG  . SER A 106 ? 1.63242 1.99441 1.65660 -0.20133 -0.17010 -0.12973 106 SER A OG  
742  N N   . ARG A 107 ? 1.55164 1.62591 1.46471 -0.23534 -0.08531 -0.08287 107 ARG A N   
743  C CA  . ARG A 107 ? 1.71538 1.72091 1.59146 -0.23339 -0.06624 -0.06599 107 ARG A CA  
744  C C   . ARG A 107 ? 1.55883 1.48246 1.42792 -0.22443 -0.04234 -0.04365 107 ARG A C   
745  O O   . ARG A 107 ? 1.52017 1.38572 1.35867 -0.22149 -0.02173 -0.03203 107 ARG A O   
746  C CB  . ARG A 107 ? 1.78374 1.78833 1.62802 -0.27241 -0.04171 -0.10239 107 ARG A CB  
747  C CG  . ARG A 107 ? 1.61863 1.70658 1.45826 -0.27533 -0.06599 -0.12176 107 ARG A CG  
748  C CD  . ARG A 107 ? 1.83340 1.91866 1.64083 -0.31945 -0.03710 -0.16302 107 ARG A CD  
749  N NE  . ARG A 107 ? 2.00857 2.11570 1.82722 -0.36626 -0.01207 -0.21218 107 ARG A NE  
750  C CZ  . ARG A 107 ? 1.78968 1.89015 1.58413 -0.41554 0.02336  -0.25831 107 ARG A CZ  
751  N NH1 . ARG A 107 ? 1.68741 1.77163 1.44621 -0.42354 0.03309  -0.26363 107 ARG A NH1 
752  N NH2 . ARG A 107 ? 1.68112 1.79282 1.48719 -0.46099 0.05270  -0.30376 107 ARG A NH2 
753  N N   . LYS A 108 ? 1.45763 1.38116 1.35315 -0.21634 -0.04535 -0.03753 108 LYS A N   
754  C CA  . LYS A 108 ? 1.30585 1.16826 1.19495 -0.19997 -0.02819 -0.01536 108 LYS A CA  
755  C C   . LYS A 108 ? 1.31845 1.19737 1.23951 -0.16706 -0.05285 0.01197  108 LYS A C   
756  O O   . LYS A 108 ? 1.29060 1.13440 1.20550 -0.14719 -0.04510 0.03233  108 LYS A O   
757  C CB  . LYS A 108 ? 1.35128 1.18889 1.23485 -0.22045 -0.00187 -0.03332 108 LYS A CB  
758  C CG  . LYS A 108 ? 1.49717 1.29969 1.34380 -0.25856 0.03606  -0.06376 108 LYS A CG  
759  C CD  . LYS A 108 ? 1.54933 1.30519 1.38021 -0.27710 0.07272  -0.07720 108 LYS A CD  
760  C CE  . LYS A 108 ? 1.63070 1.34037 1.42134 -0.32085 0.12031  -0.11175 108 LYS A CE  
761  N NZ  . LYS A 108 ? 1.51964 1.16842 1.28614 -0.34042 0.16549  -0.12424 108 LYS A NZ  
762  N N   . ILE A 109 ? 1.21568 1.14974 1.17035 -0.16054 -0.07960 0.01013  109 ILE A N   
763  C CA  . ILE A 109 ? 1.13552 1.08153 1.11921 -0.13340 -0.09818 0.03208  109 ILE A CA  
764  C C   . ILE A 109 ? 1.07953 1.05815 1.06590 -0.11993 -0.11890 0.03983  109 ILE A C   
765  O O   . ILE A 109 ? 1.21871 1.24773 1.21551 -0.12124 -0.13425 0.02675  109 ILE A O   
766  C CB  . ILE A 109 ? 1.15065 1.11952 1.16712 -0.13231 -0.10441 0.02575  109 ILE A CB  
767  C CG1 . ILE A 109 ? 1.20310 1.13618 1.20529 -0.14435 -0.08027 0.01839  109 ILE A CG1 
768  C CG2 . ILE A 109 ? 1.15213 1.12739 1.19680 -0.10822 -0.11760 0.04446  109 ILE A CG2 
769  C CD1 . ILE A 109 ? 1.18644 1.13215 1.21581 -0.13817 -0.08382 0.01806  109 ILE A CD1 
770  N N   . MET A 110 ? 1.30560 1.25859 1.28114 -0.10408 -0.11796 0.06094  110 MET A N   
771  C CA  . MET A 110 ? 1.10656 1.07590 1.06965 -0.08860 -0.13095 0.07227  110 MET A CA  
772  C C   . MET A 110 ? 1.08115 1.02897 1.05724 -0.06600 -0.13078 0.09572  110 MET A C   
773  O O   . MET A 110 ? 1.22355 1.13843 1.20381 -0.06713 -0.11665 0.10308  110 MET A O   
774  C CB  . MET A 110 ? 1.14334 1.09508 1.06773 -0.09754 -0.12191 0.07126  110 MET A CB  
775  C CG  . MET A 110 ? 1.25418 1.23240 1.16237 -0.12341 -0.11936 0.04240  110 MET A CG  
776  S SD  . MET A 110 ? 1.64503 1.56588 1.51973 -0.14666 -0.08784 0.03354  110 MET A SD  
777  C CE  . MET A 110 ? 1.20271 1.08122 1.09760 -0.13771 -0.07360 0.04606  110 MET A CE  
778  N N   . THR A 111 ? 1.19768 1.16531 1.17881 -0.04479 -0.14323 0.10537  111 THR A N   
779  C CA  . THR A 111 ? 1.29741 1.23387 1.28681 -0.02545 -0.13507 0.12550  111 THR A CA  
780  C C   . THR A 111 ? 1.28854 1.20744 1.23964 -0.00331 -0.13316 0.14643  111 THR A C   
781  O O   . THR A 111 ? 1.35990 1.31430 1.28707 0.00955  -0.14888 0.14637  111 THR A O   
782  C CB  . THR A 111 ? 1.24067 1.19592 1.26223 -0.01294 -0.14216 0.12390  111 THR A CB  
783  O OG1 . THR A 111 ? 1.51786 1.43132 1.54439 0.00108  -0.12575 0.14023  111 THR A OG1 
784  C CG2 . THR A 111 ? 1.13697 1.14121 1.15053 0.00722  -0.16243 0.12257  111 THR A CG2 
785  N N   . THR A 112 ? 1.56275 1.43044 1.50672 0.00106  -0.11186 0.16218  112 THR A N   
786  C CA  . THR A 112 ? 1.71186 1.54612 1.61190 0.02116  -0.10145 0.18485  112 THR A CA  
787  C C   . THR A 112 ? 1.67961 1.45761 1.58370 0.03106  -0.07419 0.19999  112 THR A C   
788  O O   . THR A 112 ? 1.64556 1.41548 1.58958 0.01476  -0.06272 0.18774  112 THR A O   
789  C CB  . THR A 112 ? 1.75851 1.57642 1.63134 0.00478  -0.09230 0.18359  112 THR A CB  
790  O OG1 . THR A 112 ? 1.52924 1.33302 1.43176 -0.02012 -0.07769 0.17062  112 THR A OG1 
791  C CG2 . THR A 112 ? 1.71159 1.57606 1.56569 -0.00260 -0.11295 0.16954  112 THR A CG2 
792  N N   . GLU A 113 ? 1.62087 1.35858 1.47919 0.05774  -0.06047 0.22533  113 GLU A N   
793  C CA  . GLU A 113 ? 1.57071 1.23781 1.42124 0.06540  -0.02381 0.24014  113 GLU A CA  
794  C C   . GLU A 113 ? 1.66369 1.28634 1.50280 0.04058  0.00660  0.23822  113 GLU A C   
795  O O   . GLU A 113 ? 1.74342 1.36715 1.54769 0.04050  0.00299  0.24463  113 GLU A O   
796  C CB  . GLU A 113 ? 1.45141 1.08608 1.24998 0.11365  -0.01762 0.27222  113 GLU A CB  
797  C CG  . GLU A 113 ? 1.64813 1.19898 1.43863 0.12266  0.02674  0.28612  113 GLU A CG  
798  C CD  . GLU A 113 ? 1.85080 1.39796 1.63568 0.16496  0.02300  0.30171  113 GLU A CD  
799  O OE1 . GLU A 113 ? 1.71008 1.29576 1.46077 0.20826  -0.00390 0.31968  113 GLU A OE1 
800  O OE2 . GLU A 113 ? 1.85124 1.36351 1.66713 0.15544  0.04721  0.29325  113 GLU A OE2 
801  N N   . VAL A 114 ? 1.49967 1.09031 1.37063 0.01737  0.03742  0.22509  114 VAL A N   
802  C CA  . VAL A 114 ? 1.49109 1.05551 1.36557 -0.01184 0.06797  0.21373  114 VAL A CA  
803  C C   . VAL A 114 ? 1.81594 1.29375 1.65138 -0.00506 0.11600  0.23136  114 VAL A C   
804  O O   . VAL A 114 ? 2.07037 1.50621 1.90642 0.00528  0.13782  0.23718  114 VAL A O   
805  C CB  . VAL A 114 ? 1.69482 1.29794 1.63381 -0.04563 0.07172  0.17929  114 VAL A CB  
806  C CG1 . VAL A 114 ? 1.82450 1.41894 1.77118 -0.07365 0.10100  0.16315  114 VAL A CG1 
807  C CG2 . VAL A 114 ? 1.55280 1.22537 1.51805 -0.04652 0.03058  0.16741  114 VAL A CG2 
808  N N   . ASN A 115 ? 1.84035 1.28475 1.63939 -0.01178 0.13754  0.23910  115 ASN A N   
809  C CA  . ASN A 115 ? 1.97745 1.32862 1.73021 -0.00788 0.19079  0.25641  115 ASN A CA  
810  C C   . ASN A 115 ? 1.99205 1.32505 1.78813 -0.05505 0.23581  0.22282  115 ASN A C   
811  O O   . ASN A 115 ? 1.95740 1.35894 1.80973 -0.08606 0.22165  0.18964  115 ASN A O   
812  C CB  . ASN A 115 ? 1.90308 1.22685 1.58939 0.00852  0.19435  0.28112  115 ASN A CB  
813  C CG  . ASN A 115 ? 2.17117 1.38688 1.78963 0.02603  0.24884  0.30971  115 ASN A CG  
814  O OD1 . ASN A 115 ? 2.37922 1.53244 1.99867 0.02551  0.28801  0.31115  115 ASN A OD1 
815  N ND2 . ASN A 115 ? 2.21426 1.40129 1.76813 0.04220  0.25562  0.33282  115 ASN A ND2 
816  N N   . LYS A 116 ? 2.01858 1.26010 1.78659 -0.05854 0.29303  0.22996  116 LYS A N   
817  C CA  . LYS A 116 ? 2.06957 1.29119 1.87625 -0.10893 0.34538  0.19203  116 LYS A CA  
818  C C   . LYS A 116 ? 2.22575 1.48633 2.04831 -0.14068 0.35072  0.16982  116 LYS A C   
819  O O   . LYS A 116 ? 2.22920 1.54788 2.11556 -0.18197 0.36040  0.12520  116 LYS A O   
820  C CB  . LYS A 116 ? 2.04496 1.14001 1.79891 -0.10624 0.41598  0.20826  116 LYS A CB  
821  C CG  . LYS A 116 ? 2.11502 1.16645 1.85793 -0.07578 0.42025  0.22575  116 LYS A CG  
822  C CD  . LYS A 116 ? 1.93513 0.84401 1.61347 -0.06716 0.49769  0.24656  116 LYS A CD  
823  C CE  . LYS A 116 ? 2.03327 0.90044 1.70747 -0.03770 0.50573  0.25933  116 LYS A CE  
824  N NZ  . LYS A 116 ? 2.07088 0.80537 1.68144 -0.02418 0.58109  0.27595  116 LYS A NZ  
825  N N   . THR A 117 ? 2.21306 1.44904 1.97789 -0.11985 0.34446  0.19881  117 THR A N   
826  C CA  . THR A 117 ? 2.10756 1.38234 1.88561 -0.14562 0.34701  0.17951  117 THR A CA  
827  C C   . THR A 117 ? 1.99660 1.38560 1.83977 -0.15401 0.29512  0.15282  117 THR A C   
828  O O   . THR A 117 ? 2.05061 1.49515 1.94478 -0.18596 0.30474  0.11577  117 THR A O   
829  C CB  . THR A 117 ? 2.06532 1.29707 1.76580 -0.11754 0.34379  0.21701  117 THR A CB  
830  O OG1 . THR A 117 ? 2.10387 1.22354 1.73209 -0.09744 0.39045  0.24959  117 THR A OG1 
831  C CG2 . THR A 117 ? 2.06041 1.31516 1.77005 -0.14686 0.35979  0.19632  117 THR A CG2 
832  N N   . LEU A 118 ? 1.98565 1.41190 1.82519 -0.12346 0.24231  0.17064  118 LEU A N   
833  C CA  . LEU A 118 ? 1.98842 1.50742 1.88231 -0.12807 0.19903  0.14855  118 LEU A CA  
834  C C   . LEU A 118 ? 1.99628 1.55697 1.95640 -0.15136 0.20681  0.11393  118 LEU A C   
835  O O   . LEU A 118 ? 1.85087 1.48933 1.85898 -0.16213 0.18753  0.08729  118 LEU A O   
836  C CB  . LEU A 118 ? 1.94888 1.48892 1.82177 -0.09554 0.14998  0.17189  118 LEU A CB  
837  C CG  . LEU A 118 ? 1.87093 1.37055 1.67236 -0.06838 0.14328  0.20600  118 LEU A CG  
838  C CD1 . LEU A 118 ? 1.85351 1.38906 1.64369 -0.04093 0.09699  0.21956  118 LEU A CD1 
839  C CD2 . LEU A 118 ? 1.71387 1.21774 1.49412 -0.07892 0.14958  0.20311  118 LEU A CD2 
840  N N   . LEU A 119 ? 2.12147 1.63163 2.08127 -0.15643 0.23623  0.11386  119 LEU A N   
841  C CA  . LEU A 119 ? 2.08967 1.63875 2.11123 -0.18424 0.24995  0.07530  119 LEU A CA  
842  C C   . LEU A 119 ? 2.09653 1.68864 2.15970 -0.22451 0.28153  0.03232  119 LEU A C   
843  O O   . LEU A 119 ? 2.12735 1.80383 2.25116 -0.24308 0.27212  -0.00623 119 LEU A O   
844  C CB  . LEU A 119 ? 2.09569 1.56562 2.10106 -0.18434 0.28665  0.08274  119 LEU A CB  
845  C CG  . LEU A 119 ? 2.11973 1.60677 2.18042 -0.22320 0.32110  0.03755  119 LEU A CG  
846  C CD1 . LEU A 119 ? 2.18716 1.77383 2.30604 -0.22330 0.27608  0.01400  119 LEU A CD1 
847  C CD2 . LEU A 119 ? 2.04138 1.42185 2.06981 -0.22114 0.36974  0.05027  119 LEU A CD2 
848  N N   . ASP A 120 ? 2.07463 1.61507 2.10578 -0.23795 0.32099  0.03596  120 ASP A N   
849  C CA  . ASP A 120 ? 2.04744 1.64140 2.12186 -0.27682 0.35052  -0.00884 120 ASP A CA  
850  C C   . ASP A 120 ? 1.97837 1.68475 2.09212 -0.26635 0.30398  -0.02424 120 ASP A C   
851  O O   . ASP A 120 ? 1.95102 1.74894 2.12579 -0.28785 0.30620  -0.06919 120 ASP A O   
852  C CB  . ASP A 120 ? 2.14538 1.66296 2.17246 -0.29006 0.39871  0.00145  120 ASP A CB  
853  C CG  . ASP A 120 ? 2.18445 1.74489 2.25968 -0.34059 0.44684  -0.05319 120 ASP A CG  
854  O OD1 . ASP A 120 ? 2.15633 1.70402 2.26111 -0.37762 0.49170  -0.08846 120 ASP A OD1 
855  O OD2 . ASP A 120 ? 2.11955 1.72964 2.20439 -0.34480 0.44220  -0.06430 120 ASP A OD2 
856  N N   . GLU A 121 ? 1.92717 1.63003 2.00440 -0.23170 0.26380  0.01104  121 GLU A N   
857  C CA  . GLU A 121 ? 1.87498 1.66772 1.98028 -0.21624 0.22425  0.00104  121 GLU A CA  
858  C C   . GLU A 121 ? 1.77877 1.63481 1.92411 -0.20611 0.19102  -0.01122 121 GLU A C   
859  O O   . GLU A 121 ? 1.71402 1.66016 1.90091 -0.20333 0.17567  -0.03740 121 GLU A O   
860  C CB  . GLU A 121 ? 1.95142 1.71347 2.00385 -0.18677 0.19686  0.03854  121 GLU A CB  
861  C CG  . GLU A 121 ? 1.92042 1.67253 1.95199 -0.19378 0.21859  0.03727  121 GLU A CG  
862  C CD  . GLU A 121 ? 1.78204 1.61684 1.86906 -0.21244 0.23517  -0.00544 121 GLU A CD  
863  O OE1 . GLU A 121 ? 1.76975 1.68224 1.88681 -0.19445 0.20620  -0.01715 121 GLU A OE1 
864  O OE2 . GLU A 121 ? 1.63857 1.46182 1.73667 -0.24348 0.27967  -0.02803 121 GLU A OE2 
865  N N   . LEU A 122 ? 1.82650 1.63866 1.95689 -0.19658 0.18011  0.00828  122 LEU A N   
866  C CA  . LEU A 122 ? 1.84373 1.70844 2.00903 -0.18920 0.15236  -0.00319 122 LEU A CA  
867  C C   . LEU A 122 ? 1.83294 1.76381 2.05786 -0.21853 0.17348  -0.05147 122 LEU A C   
868  O O   . LEU A 122 ? 1.75357 1.74996 2.01143 -0.21213 0.14955  -0.06754 122 LEU A O   
869  C CB  . LEU A 122 ? 1.84973 1.65318 1.98991 -0.17606 0.14362  0.02347  122 LEU A CB  
870  C CG  . LEU A 122 ? 1.85355 1.64241 1.95740 -0.14374 0.10339  0.05841  122 LEU A CG  
871  C CD1 . LEU A 122 ? 1.75987 1.50021 1.84718 -0.13204 0.10108  0.07753  122 LEU A CD1 
872  C CD2 . LEU A 122 ? 1.63155 1.49182 1.75923 -0.13183 0.06833  0.04895  122 LEU A CD2 
873  N N   . LYS A 123 ? 1.90301 1.81524 2.13996 -0.25283 0.22109  -0.07682 123 LYS A N   
874  C CA  . LYS A 123 ? 1.85822 1.85478 2.15741 -0.28666 0.24330  -0.13361 123 LYS A CA  
875  C C   . LYS A 123 ? 1.80540 1.89106 2.13302 -0.29145 0.24463  -0.16217 123 LYS A C   
876  O O   . LYS A 123 ? 1.74866 1.94501 2.13222 -0.30476 0.24362  -0.20932 123 LYS A O   
877  C CB  . LYS A 123 ? 1.92894 1.86048 2.23288 -0.32972 0.30325  -0.15677 123 LYS A CB  
878  C CG  . LYS A 123 ? 1.94283 1.81209 2.22174 -0.35397 0.35331  -0.15854 123 LYS A CG  
879  C CD  . LYS A 123 ? 1.86112 1.76030 2.18764 -0.41148 0.41196  -0.22111 123 LYS A CD  
880  C CE  . LYS A 123 ? 1.93837 1.73250 2.22478 -0.43866 0.47559  -0.21605 123 LYS A CE  
881  N NZ  . LYS A 123 ? 2.04163 1.68626 2.25683 -0.41823 0.49363  -0.16319 123 LYS A NZ  
882  N N   . ASN A 124 ? 1.70282 1.75039 1.99331 -0.27841 0.24604  -0.13631 124 ASN A N   
883  C CA  . ASN A 124 ? 1.53441 1.66267 1.84738 -0.27552 0.24559  -0.15838 124 ASN A CA  
884  C C   . ASN A 124 ? 1.45428 1.64478 1.76356 -0.22849 0.19549  -0.14082 124 ASN A C   
885  O O   . ASN A 124 ? 1.19068 1.43894 1.50904 -0.21498 0.19286  -0.15077 124 ASN A O   
886  C CB  . ASN A 124 ? 1.59618 1.65055 1.86849 -0.28460 0.27557  -0.14053 124 ASN A CB  
887  C CG  . ASN A 124 ? 1.86045 1.85390 2.13347 -0.33244 0.33697  -0.16268 124 ASN A CG  
888  O OD1 . ASN A 124 ? 1.66653 1.69695 1.98502 -0.36695 0.36317  -0.20612 124 ASN A OD1 
889  N ND2 . ASN A 124 ? 1.98107 1.87806 2.19996 -0.33582 0.36445  -0.13462 124 ASN A ND2 
890  N N   . ILE A 125 ? 1.59884 1.77350 1.89184 -0.20252 0.16028  -0.11487 125 ILE A N   
891  C CA  . ILE A 125 ? 1.42473 1.65101 1.71096 -0.15963 0.12086  -0.10080 125 ILE A CA  
892  C C   . ILE A 125 ? 1.35372 1.71106 1.69457 -0.15390 0.11398  -0.14383 125 ILE A C   
893  O O   . ILE A 125 ? 1.43059 1.83323 1.81144 -0.17819 0.12202  -0.17705 125 ILE A O   
894  C CB  . ILE A 125 ? 1.41056 1.58185 1.66454 -0.13940 0.09148  -0.06562 125 ILE A CB  
895  C CG1 . ILE A 125 ? 1.49537 1.63161 1.76277 -0.16556 0.10274  -0.07259 125 ILE A CG1 
896  C CG2 . ILE A 125 ? 1.29444 1.37601 1.48990 -0.12545 0.08448  -0.02317 125 ILE A CG2 
897  C CD1 . ILE A 125 ? 1.31765 1.53939 1.63861 -0.17873 0.10305  -0.11355 125 ILE A CD1 
898  N N   . ASN A 126 ? 1.27875 1.70099 1.61969 -0.11956 0.10054  -0.14488 126 ASN A N   
899  C CA  . ASN A 126 ? 1.17950 1.74166 1.56783 -0.10355 0.09213  -0.18490 126 ASN A CA  
900  C C   . ASN A 126 ? 1.33696 1.92572 1.69381 -0.04156 0.06237  -0.15723 126 ASN A C   
901  O O   . ASN A 126 ? 1.32318 1.84879 1.63689 -0.01969 0.06252  -0.12445 126 ASN A O   
902  C CB  . ASN A 126 ? 1.23066 1.87016 1.66336 -0.12917 0.12214  -0.23052 126 ASN A CB  
903  C CG  . ASN A 126 ? 1.37077 2.01088 1.84461 -0.19275 0.15866  -0.27320 126 ASN A CG  
904  O OD1 . ASN A 126 ? 1.07453 1.68708 1.55410 -0.21204 0.15796  -0.27651 126 ASN A OD1 
905  N ND2 . ASN A 126 ? 1.44530 2.11450 1.94710 -0.22665 0.19547  -0.30830 126 ASN A ND2 
906  N N   . SER A 127 ? 1.45380 2.13180 1.82762 -0.01269 0.04046  -0.17078 127 SER A N   
907  C CA  . SER A 127 ? 1.39619 2.09184 1.73155 0.05194  0.01797  -0.14220 127 SER A CA  
908  C C   . SER A 127 ? 1.41898 2.19349 1.76286 0.08629  0.02425  -0.15470 127 SER A C   
909  O O   . SER A 127 ? 1.44210 2.19679 1.74070 0.14112  0.01625  -0.12285 127 SER A O   
910  C CB  . SER A 127 ? 1.08924 1.86004 1.43436 0.07724  -0.00495 -0.15228 127 SER A CB  
911  O OG  . SER A 127 ? 1.23928 2.15817 1.64658 0.06760  -0.00345 -0.20797 127 SER A OG  
912  N N   . HIS A 128 ? 1.49188 2.35314 1.89192 0.05487  0.04254  -0.20207 128 HIS A N   
913  C CA  . HIS A 128 ? 1.65872 2.58266 2.06924 0.07888  0.05363  -0.21475 128 HIS A CA  
914  C C   . HIS A 128 ? 1.80741 2.60826 2.18528 0.05421  0.07641  -0.18854 128 HIS A C   
915  O O   . HIS A 128 ? 1.86148 2.54462 2.21507 0.01565  0.08407  -0.16685 128 HIS A O   
916  C CB  . HIS A 128 ? 1.70312 2.78337 2.19151 0.05165  0.06646  -0.28346 128 HIS A CB  
917  C CG  . HIS A 128 ? 1.59264 2.66733 2.12323 -0.02099 0.08436  -0.32043 128 HIS A CG  
918  N ND1 . HIS A 128 ? 1.49597 2.61687 2.04610 -0.02843 0.06888  -0.33816 128 HIS A ND1 
919  C CD2 . HIS A 128 ? 1.67158 2.69306 2.22370 -0.08799 0.12132  -0.34270 128 HIS A CD2 
920  C CE1 . HIS A 128 ? 1.46543 2.56003 2.04916 -0.09766 0.09644  -0.37082 128 HIS A CE1 
921  N NE2 . HIS A 128 ? 1.60915 2.63982 2.19229 -0.13364 0.12994  -0.37284 128 HIS A NE2 
922  N N   . ASP A 129 ? 1.77330 2.60803 2.14907 0.08063  0.08707  -0.19115 129 ASP A N   
923  C CA  . ASP A 129 ? 1.77673 2.50504 2.11665 0.06548  0.10828  -0.16665 129 ASP A CA  
924  C C   . ASP A 129 ? 1.80998 2.39047 2.07861 0.07531  0.09815  -0.11103 129 ASP A C   
925  O O   . ASP A 129 ? 1.89261 2.36989 2.13881 0.03420  0.10846  -0.09502 129 ASP A O   
926  C CB  . ASP A 129 ? 1.75570 2.46404 2.12832 -0.00466 0.13956  -0.19630 129 ASP A CB  
927  C CG  . ASP A 129 ? 1.88161 2.53756 2.23299 -0.01316 0.16525  -0.18792 129 ASP A CG  
928  O OD1 . ASP A 129 ? 1.86074 2.45730 2.16118 0.02625  0.15801  -0.15047 129 ASP A OD1 
929  O OD2 . ASP A 129 ? 2.02062 2.69004 2.40377 -0.06157 0.19679  -0.22032 129 ASP A OD2 
930  N N   . ASN A 130 ? 1.45265 2.02709 1.68325 0.13230  0.08004  -0.08314 130 ASN A N   
931  C CA  . ASN A 130 ? 1.30267 1.74846 1.46822 0.14065  0.07347  -0.03747 130 ASN A CA  
932  C C   . ASN A 130 ? 1.34708 1.68925 1.47411 0.11952  0.09239  -0.01770 130 ASN A C   
933  O O   . ASN A 130 ? 1.24535 1.48593 1.33446 0.09704  0.09011  0.00685  130 ASN A O   
934  C CB  . ASN A 130 ? 1.25199 1.70556 1.37800 0.20796  0.06337  -0.01399 130 ASN A CB  
935  C CG  . ASN A 130 ? 1.34746 1.91631 1.50687 0.23608  0.04402  -0.03401 130 ASN A CG  
936  O OD1 . ASN A 130 ? 1.38607 2.08340 1.59745 0.24443  0.04302  -0.07100 130 ASN A OD1 
937  N ND2 . ASN A 130 ? 1.41870 1.94986 1.54979 0.24883  0.02928  -0.01351 130 ASN A ND2 
938  N N   . SER A 131 ? 1.40281 1.77652 1.53782 0.12943  0.11074  -0.02961 131 SER A N   
939  C CA  . SER A 131 ? 1.23770 1.52504 1.34115 0.10390  0.13112  -0.01735 131 SER A CA  
940  C C   . SER A 131 ? 1.20729 1.44095 1.31728 0.04375  0.13574  -0.02029 131 SER A C   
941  O O   . SER A 131 ? 1.48740 1.62145 1.55134 0.02660  0.13572  0.00548  131 SER A O   
942  C CB  . SER A 131 ? 1.18469 1.53793 1.31259 0.11607  0.15189  -0.04017 131 SER A CB  
943  O OG  . SER A 131 ? 1.11171 1.48188 1.21341 0.17852  0.15315  -0.02682 131 SER A OG  
944  N N   . ALA A 132 ? 1.15964 1.46057 1.32462 0.01266  0.14230  -0.05338 132 ALA A N   
945  C CA  . ALA A 132 ? 1.24720 1.49078 1.41400 -0.03929 0.15349  -0.05503 132 ALA A CA  
946  C C   . ALA A 132 ? 1.31379 1.49615 1.45633 -0.04269 0.13119  -0.03008 132 ALA A C   
947  O O   . ALA A 132 ? 1.30750 1.40753 1.42108 -0.06881 0.13598  -0.01236 132 ALA A O   
948  C CB  . ALA A 132 ? 1.31893 1.64478 1.54946 -0.07313 0.17232  -0.10046 132 ALA A CB  
949  N N   . PHE A 133 ? 1.27310 1.49961 1.42659 -0.01456 0.10762  -0.02929 133 PHE A N   
950  C CA  . PHE A 133 ? 1.24345 1.41742 1.37700 -0.01832 0.08776  -0.00845 133 PHE A CA  
951  C C   . PHE A 133 ? 1.17915 1.25465 1.25109 -0.01204 0.08286  0.02688  133 PHE A C   
952  O O   . PHE A 133 ? 1.16233 1.17567 1.21402 -0.03413 0.07825  0.04148  133 PHE A O   
953  C CB  . PHE A 133 ? 1.13311 1.37187 1.28394 0.01316  0.06646  -0.01388 133 PHE A CB  
954  C CG  . PHE A 133 ? 1.22797 1.43096 1.37373 0.00128  0.04963  -0.00270 133 PHE A CG  
955  C CD1 . PHE A 133 ? 1.20218 1.34178 1.30276 0.01870  0.03602  0.02687  133 PHE A CD1 
956  C CD2 . PHE A 133 ? 1.15489 1.38302 1.34065 -0.03102 0.05230  -0.02438 133 PHE A CD2 
957  C CE1 . PHE A 133 ? 0.97933 1.09222 1.07890 0.00657  0.02157  0.03431  133 PHE A CE1 
958  C CE2 . PHE A 133 ? 1.18691 1.38215 1.36881 -0.04007 0.03839  -0.01443 133 PHE A CE2 
959  C CZ  . PHE A 133 ? 0.99577 1.13752 1.13625 -0.02044 0.02125  0.01504  133 PHE A CZ  
960  N N   . ILE A 134 ? 1.13849 1.20278 1.17932 0.01991  0.08508  0.03881  134 ILE A N   
961  C CA  . ILE A 134 ? 1.26733 1.24286 1.25066 0.01982  0.08693  0.06398  134 ILE A CA  
962  C C   . ILE A 134 ? 1.23868 1.16621 1.20504 -0.01302 0.10020  0.06685  134 ILE A C   
963  O O   . ILE A 134 ? 1.26212 1.12781 1.19242 -0.02808 0.09447  0.08269  134 ILE A O   
964  C CB  . ILE A 134 ? 1.24701 1.21393 1.19914 0.05883  0.09741  0.07223  134 ILE A CB  
965  C CG1 . ILE A 134 ? 1.42417 1.43956 1.38567 0.09978  0.08708  0.07262  134 ILE A CG1 
966  C CG2 . ILE A 134 ? 1.20921 1.08399 1.10235 0.05259  0.10352  0.09160  134 ILE A CG2 
967  C CD1 . ILE A 134 ? 1.34037 1.35404 1.27083 0.14965  0.10277  0.08155  134 ILE A CD1 
968  N N   . SER A 135 ? 1.11125 1.07078 1.10072 -0.02303 0.11947  0.05029  135 SER A N   
969  C CA  . SER A 135 ? 1.21597 1.12693 1.18489 -0.05309 0.13637  0.05407  135 SER A CA  
970  C C   . SER A 135 ? 1.34825 1.22392 1.31396 -0.07736 0.12904  0.06264  135 SER A C   
971  O O   . SER A 135 ? 1.45297 1.26708 1.37558 -0.08811 0.12936  0.08092  135 SER A O   
972  C CB  . SER A 135 ? 1.29095 1.24817 1.29317 -0.06479 0.16282  0.02950  135 SER A CB  
973  O OG  . SER A 135 ? 1.23514 1.24381 1.24932 -0.03515 0.16812  0.01864  135 SER A OG  
974  N N   . SER A 136 ? 1.20390 1.12185 1.21356 -0.08382 0.12383  0.04833  136 SER A N   
975  C CA  . SER A 136 ? 1.19681 1.07872 1.20444 -0.10306 0.12144  0.05601  136 SER A CA  
976  C C   . SER A 136 ? 1.14377 0.98722 1.11883 -0.09143 0.09430  0.07976  136 SER A C   
977  O O   . SER A 136 ? 1.26777 1.06374 1.21630 -0.09973 0.09211  0.09578  136 SER A O   
978  C CB  . SER A 136 ? 1.06644 1.00520 1.13059 -0.11480 0.12589  0.02978  136 SER A CB  
979  O OG  . SER A 136 ? 1.22102 1.21642 1.32169 -0.12582 0.15001  -0.00047 136 SER A OG  
980  N N   . LEU A 137 ? 0.90975 0.77464 0.88479 -0.07060 0.07598  0.08135  137 LEU A N   
981  C CA  . LEU A 137 ? 1.16435 0.99360 1.10760 -0.06518 0.05588  0.09839  137 LEU A CA  
982  C C   . LEU A 137 ? 1.35749 1.13581 1.24972 -0.07135 0.06021  0.11191  137 LEU A C   
983  O O   . LEU A 137 ? 1.34936 1.10112 1.21738 -0.07740 0.04830  0.12317  137 LEU A O   
984  C CB  . LEU A 137 ? 1.39480 1.24361 1.33868 -0.04320 0.04546  0.09707  137 LEU A CB  
985  C CG  . LEU A 137 ? 1.29924 1.20422 1.28651 -0.03272 0.03638  0.08488  137 LEU A CG  
986  C CD1 . LEU A 137 ? 1.22967 1.14323 1.20270 -0.00377 0.03141  0.08887  137 LEU A CD1 
987  C CD2 . LEU A 137 ? 0.94547 0.84396 0.94776 -0.04809 0.02279  0.08667  137 LEU A CD2 
988  N N   . ILE A 138 ? 1.42488 1.19641 1.29999 -0.06756 0.07665  0.10898  138 ILE A N   
989  C CA  . ILE A 138 ? 1.33347 1.06160 1.15980 -0.07601 0.08424  0.11773  138 ILE A CA  
990  C C   . ILE A 138 ? 1.33784 1.04269 1.14919 -0.08945 0.08733  0.12771  138 ILE A C   
991  O O   . ILE A 138 ? 1.44723 1.12684 1.21962 -0.09178 0.07702  0.13928  138 ILE A O   
992  C CB  . ILE A 138 ? 1.27308 1.00087 1.09084 -0.07062 0.10691  0.11051  138 ILE A CB  
993  C CG1 . ILE A 138 ? 1.34481 1.08298 1.16397 -0.04823 0.10768  0.10609  138 ILE A CG1 
994  C CG2 . ILE A 138 ? 1.31655 1.00176 1.08375 -0.08221 0.11689  0.11713  138 ILE A CG2 
995  C CD1 . ILE A 138 ? 1.48784 1.18416 1.26510 -0.05006 0.10248  0.11148  138 ILE A CD1 
996  N N   . TYR A 139 ? 1.21633 0.93075 1.05572 -0.09721 0.10467  0.12181  139 TYR A N   
997  C CA  . TYR A 139 ? 1.43222 1.10877 1.24947 -0.10727 0.11836  0.13364  139 TYR A CA  
998  C C   . TYR A 139 ? 1.46084 1.12338 1.26801 -0.10040 0.09779  0.14859  139 TYR A C   
999  O O   . TYR A 139 ? 1.42328 1.05173 1.18398 -0.09450 0.09530  0.16729  139 TYR A O   
1000 C CB  . TYR A 139 ? 1.42644 1.11471 1.28139 -0.12248 0.14776  0.11765  139 TYR A CB  
1001 C CG  . TYR A 139 ? 1.64442 1.27680 1.46995 -0.13307 0.17326  0.13058  139 TYR A CG  
1002 C CD1 . TYR A 139 ? 1.58676 1.17163 1.35643 -0.13367 0.19039  0.14603  139 TYR A CD1 
1003 C CD2 . TYR A 139 ? 1.65866 1.27917 1.50589 -0.14036 0.18367  0.12850  139 TYR A CD2 
1004 C CE1 . TYR A 139 ? 1.66988 1.19367 1.40196 -0.13761 0.21839  0.16222  139 TYR A CE1 
1005 C CE2 . TYR A 139 ? 1.75154 1.30589 1.56304 -0.14598 0.21445  0.14336  139 TYR A CE2 
1006 C CZ  . TYR A 139 ? 1.87771 1.38187 1.62919 -0.14259 0.23216  0.16202  139 TYR A CZ  
1007 O OH  . TYR A 139 ? 1.93615 1.36485 1.64212 -0.14276 0.26738  0.18094  139 TYR A OH  
1008 N N   . LEU A 140 ? 1.41689 1.11027 1.26643 -0.09800 0.08356  0.14016  140 LEU A N   
1009 C CA  . LEU A 140 ? 1.30482 0.99117 1.15105 -0.09001 0.06428  0.15175  140 LEU A CA  
1010 C C   . LEU A 140 ? 1.32523 1.01073 1.13370 -0.08023 0.03942  0.16177  140 LEU A C   
1011 O O   . LEU A 140 ? 1.35089 1.01938 1.12613 -0.07037 0.03151  0.17758  140 LEU A O   
1012 C CB  . LEU A 140 ? 1.24658 0.97196 1.14521 -0.09056 0.05323  0.13722  140 LEU A CB  
1013 C CG  . LEU A 140 ? 1.20200 0.92246 1.10450 -0.08308 0.03676  0.14630  140 LEU A CG  
1014 C CD1 . LEU A 140 ? 1.44443 1.11730 1.32352 -0.08119 0.05687  0.16165  140 LEU A CD1 
1015 C CD2 . LEU A 140 ? 1.13552 0.89446 1.08981 -0.08647 0.03027  0.12929  140 LEU A CD2 
1016 N N   . ILE A 141 ? 1.28072 0.98639 1.09188 -0.08177 0.02968  0.15082  141 ILE A N   
1017 C CA  . ILE A 141 ? 1.35178 1.05978 1.12971 -0.08128 0.01261  0.15108  141 ILE A CA  
1018 C C   . ILE A 141 ? 1.42565 1.11287 1.15216 -0.08073 0.01745  0.16129  141 ILE A C   
1019 O O   . ILE A 141 ? 1.53759 1.23682 1.23555 -0.07622 0.00011  0.16444  141 ILE A O   
1020 C CB  . ILE A 141 ? 1.26358 0.97743 1.04446 -0.08567 0.01576  0.13675  141 ILE A CB  
1021 C CG1 . ILE A 141 ? 1.13068 0.86654 0.95120 -0.08052 0.00713  0.13011  141 ILE A CG1 
1022 C CG2 . ILE A 141 ? 1.24269 0.95208 0.98441 -0.09466 0.00961  0.12965  141 ILE A CG2 
1023 C CD1 . ILE A 141 ? 1.33991 1.07423 1.16412 -0.07409 0.01957  0.12191  141 ILE A CD1 
1024 N N   . SER A 142 ? 1.42103 1.08394 1.13447 -0.08448 0.04127  0.16452  142 SER A N   
1025 C CA  . SER A 142 ? 1.43625 1.07570 1.09545 -0.08216 0.04882  0.17626  142 SER A CA  
1026 C C   . SER A 142 ? 1.39558 1.01961 1.03202 -0.06560 0.04504  0.19780  142 SER A C   
1027 O O   . SER A 142 ? 1.63244 1.25639 1.21876 -0.05321 0.03567  0.20917  142 SER A O   
1028 C CB  . SER A 142 ? 1.52197 1.13635 1.17479 -0.09093 0.07959  0.17419  142 SER A CB  
1029 O OG  . SER A 142 ? 1.55250 1.14320 1.21663 -0.09104 0.10094  0.18311  142 SER A OG  
1030 N N   . LYS A 143 ? 1.49044 1.10182 1.15955 -0.06274 0.05449  0.20304  143 LYS A N   
1031 C CA  . LYS A 143 ? 1.56079 1.13993 1.20290 -0.04369 0.06129  0.22620  143 LYS A CA  
1032 C C   . LYS A 143 ? 1.56605 1.17440 1.21442 -0.02428 0.03099  0.23198  143 LYS A C   
1033 O O   . LYS A 143 ? 1.51478 1.09760 1.16112 -0.00760 0.03877  0.24765  143 LYS A O   
1034 C CB  . LYS A 143 ? 1.47495 1.01702 1.14499 -0.05444 0.09590  0.22529  143 LYS A CB  
1035 C CG  . LYS A 143 ? 1.55300 1.07477 1.22200 -0.07505 0.12893  0.21538  143 LYS A CG  
1036 C CD  . LYS A 143 ? 1.77082 1.23116 1.37298 -0.06582 0.15713  0.23886  143 LYS A CD  
1037 C CE  . LYS A 143 ? 1.75430 1.21935 1.31797 -0.06941 0.15631  0.23781  143 LYS A CE  
1038 N NZ  . LYS A 143 ? 1.69087 1.09306 1.19434 -0.06633 0.19336  0.25654  143 LYS A NZ  
1039 N N   . LEU A 144 ? 1.59917 1.59894 1.10163 -0.02384 0.50182  0.28862  144 LEU A N   
1040 C CA  . LEU A 144 ? 1.75374 1.80084 1.29470 -0.02256 0.46881  0.32070  144 LEU A CA  
1041 C C   . LEU A 144 ? 1.79475 1.89974 1.26518 -0.01810 0.41286  0.36839  144 LEU A C   
1042 O O   . LEU A 144 ? 1.76754 1.87263 1.15505 -0.03756 0.36532  0.34338  144 LEU A O   
1043 C CB  . LEU A 144 ? 1.54653 1.59989 1.13581 -0.05166 0.42994  0.26951  144 LEU A CB  
1044 C CG  . LEU A 144 ? 1.45672 1.46857 1.12695 -0.05880 0.47161  0.23282  144 LEU A CG  
1045 C CD1 . LEU A 144 ? 1.22617 1.25673 0.93360 -0.07915 0.42751  0.19935  144 LEU A CD1 
1046 C CD2 . LEU A 144 ? 1.32531 1.30976 1.03845 -0.03220 0.53620  0.27664  144 LEU A CD2 
1047 N N   . GLU A 145 ? 1.92448 2.07602 1.42561 0.00696  0.41936  0.43910  145 GLU A N   
1048 C CA  . GLU A 145 ? 1.97348 2.20112 1.42962 0.00567  0.35582  0.49279  145 GLU A CA  
1049 C C   . GLU A 145 ? 2.02657 2.29602 1.50493 -0.02988 0.28219  0.46878  145 GLU A C   
1050 O O   . GLU A 145 ? 1.95515 2.22227 1.51405 -0.03219 0.29269  0.45263  145 GLU A O   
1051 C CB  . GLU A 145 ? 1.90404 2.18146 1.40535 0.04708  0.38786  0.58520  145 GLU A CB  
1052 C CG  . GLU A 145 ? 2.18194 2.42711 1.65444 0.08578  0.45762  0.62464  145 GLU A CG  
1053 C CD  . GLU A 145 ? 2.19083 2.35532 1.72846 0.10229  0.54716  0.60152  145 GLU A CD  
1054 O OE1 . GLU A 145 ? 1.99659 2.13024 1.59543 0.08342  0.55213  0.55332  145 GLU A OE1 
1055 O OE2 . GLU A 145 ? 2.00925 2.13503 1.54680 0.12688  0.59230  0.61238  145 GLU A OE2 
1056 N N   . ASN A 146 ? 2.52793 2.83036 1.92839 -0.05850 0.20799  0.46746  146 ASN A N   
1057 C CA  . ASN A 146 ? 2.52813 2.86975 1.94328 -0.09788 0.13299  0.44848  146 ASN A CA  
1058 C C   . ASN A 146 ? 2.48709 2.77397 1.94144 -0.11635 0.14403  0.37027  146 ASN A C   
1059 O O   . ASN A 146 ? 2.42149 2.73587 1.95427 -0.12277 0.13112  0.36946  146 ASN A O   
1060 C CB  . ASN A 146 ? 2.55056 2.98747 2.05049 -0.08674 0.11042  0.52687  146 ASN A CB  
1061 C CG  . ASN A 146 ? 2.56215 3.06603 2.04652 -0.13086 0.01527  0.53911  146 ASN A CG  
1062 O OD1 . ASN A 146 ? 2.55226 3.03966 2.05456 -0.16316 -0.01698 0.48804  146 ASN A OD1 
1063 N ND2 . ASN A 146 ? 2.62965 3.20958 2.07856 -0.13553 -0.03265 0.60771  146 ASN A ND2 
1064 N N   . ASN A 147 ? 1.78272 1.99434 1.18144 -0.12144 0.17077  0.30901  147 ASN A N   
1065 C CA  . ASN A 147 ? 1.66602 1.83164 1.09860 -0.13722 0.18139  0.23864  147 ASN A CA  
1066 C C   . ASN A 147 ? 1.64491 1.81496 1.04357 -0.17608 0.11204  0.20237  147 ASN A C   
1067 O O   . ASN A 147 ? 1.69910 1.84841 1.14027 -0.18770 0.11315  0.15499  147 ASN A O   
1068 C CB  . ASN A 147 ? 1.39520 1.48979 0.79237 -0.12712 0.23614  0.19569  147 ASN A CB  
1069 C CG  . ASN A 147 ? 1.77643 1.83957 1.04817 -0.12749 0.22546  0.19490  147 ASN A CG  
1070 O OD1 . ASN A 147 ? 1.82682 1.87647 1.01909 -0.15421 0.17130  0.16962  147 ASN A OD1 
1071 N ND2 . ASN A 147 ? 1.94428 1.98634 1.19077 -0.09754 0.28023  0.22191  147 ASN A ND2 
1072 N N   . GLU A 148 ? 1.50907 1.70379 0.83053 -0.19832 0.05101  0.22460  148 GLU A N   
1073 C CA  . GLU A 148 ? 1.45712 1.64526 0.73992 -0.24157 -0.01623 0.19036  148 GLU A CA  
1074 C C   . GLU A 148 ? 1.51717 1.74609 0.90924 -0.25107 -0.03237 0.18869  148 GLU A C   
1075 O O   . GLU A 148 ? 1.51656 1.70791 0.91149 -0.26930 -0.04177 0.13498  148 GLU A O   
1076 C CB  . GLU A 148 ? 1.63094 1.85626 0.83263 -0.27028 -0.08776 0.22860  148 GLU A CB  
1077 C CG  . GLU A 148 ? 1.63750 1.96641 0.90563 -0.25661 -0.10470 0.31718  148 GLU A CG  
1078 C CD  . GLU A 148 ? 2.14038 2.47261 1.36448 -0.21950 -0.06370 0.36075  148 GLU A CD  
1079 O OE1 . GLU A 148 ? 2.11247 2.37356 1.30554 -0.19295 0.00144  0.32663  148 GLU A OE1 
1080 O OE2 . GLU A 148 ? 2.36294 2.77373 1.58782 -0.21630 -0.09607 0.43402  148 GLU A OE2 
1081 N N   . LYS A 149 ? 1.55926 1.86124 1.04152 -0.23243 -0.02736 0.25047  149 LYS A N   
1082 C CA  . LYS A 149 ? 1.43244 1.76866 1.01605 -0.23186 -0.03102 0.25503  149 LYS A CA  
1083 C C   . LYS A 149 ? 1.46138 1.73480 1.07039 -0.22279 0.01376  0.18914  149 LYS A C   
1084 O O   . LYS A 149 ? 1.52389 1.77962 1.13807 -0.24440 -0.01051 0.14632  149 LYS A O   
1085 C CB  . LYS A 149 ? 1.42465 1.82408 1.09393 -0.19593 -0.00156 0.32966  149 LYS A CB  
1086 C CG  . LYS A 149 ? 1.64127 2.12390 1.30777 -0.19729 -0.04081 0.41154  149 LYS A CG  
1087 C CD  . LYS A 149 ? 1.58890 2.11970 1.34075 -0.14864 0.00995  0.48687  149 LYS A CD  
1088 C CE  . LYS A 149 ? 1.53946 2.15305 1.38623 -0.14810 -0.01813 0.54375  149 LYS A CE  
1089 N NZ  . LYS A 149 ? 1.19810 1.77791 1.08661 -0.15723 -0.01450 0.49151  149 LYS A NZ  
1090 N N   . ILE A 150 ? 1.30055 1.53819 0.92025 -0.19353 0.07811  0.18083  150 ILE A N   
1091 C CA  . ILE A 150 ? 1.20138 1.39031 0.85328 -0.18803 0.11794  0.12487  150 ILE A CA  
1092 C C   . ILE A 150 ? 1.28456 1.43181 0.88235 -0.21220 0.09652  0.06509  150 ILE A C   
1093 O O   . ILE A 150 ? 1.37358 1.51276 1.00478 -0.22117 0.08859  0.02828  150 ILE A O   
1094 C CB  . ILE A 150 ? 1.24740 1.40126 0.90947 -0.16230 0.18534  0.12745  150 ILE A CB  
1095 C CG1 . ILE A 150 ? 1.26937 1.44855 0.98509 -0.13405 0.21671  0.18543  150 ILE A CG1 
1096 C CG2 . ILE A 150 ? 1.20182 1.31111 0.89379 -0.16563 0.21849  0.06950  150 ILE A CG2 
1097 C CD1 . ILE A 150 ? 1.41318 1.62919 1.09797 -0.11842 0.21355  0.25260  150 ILE A CD1 
1098 N N   . ILE A 151 ? 1.47971 1.59901 0.98557 -0.22134 0.08464  0.05942  151 ILE A N   
1099 C CA  . ILE A 151 ? 1.59372 1.65566 1.03579 -0.23634 0.07910  0.00431  151 ILE A CA  
1100 C C   . ILE A 151 ? 1.34658 1.41542 0.79219 -0.26495 0.02589  -0.01492 151 ILE A C   
1101 O O   . ILE A 151 ? 1.40833 1.44848 0.86974 -0.26791 0.03427  -0.05806 151 ILE A O   
1102 C CB  . ILE A 151 ? 1.51357 1.53173 0.83668 -0.23727 0.07933  0.00518  151 ILE A CB  
1103 C CG1 . ILE A 151 ? 1.35824 1.36775 0.68707 -0.20514 0.14100  0.02631  151 ILE A CG1 
1104 C CG2 . ILE A 151 ? 1.52734 1.47244 0.77289 -0.24753 0.08101  -0.04908 151 ILE A CG2 
1105 C CD1 . ILE A 151 ? 1.62508 1.59884 0.83515 -0.19911 0.14382  0.03930  151 ILE A CD1 
1106 N N   . GLU A 152 ? 1.51832 1.63291 0.96145 -0.28567 -0.02819 0.02319  152 GLU A N   
1107 C CA  . GLU A 152 ? 1.64762 1.77141 1.10434 -0.31642 -0.07880 0.01121  152 GLU A CA  
1108 C C   . GLU A 152 ? 1.45442 1.59564 1.00978 -0.30191 -0.05709 -0.00379 152 GLU A C   
1109 O O   . GLU A 152 ? 1.40588 1.51530 0.95803 -0.31349 -0.06505 -0.04348 152 GLU A O   
1110 C CB  . GLU A 152 ? 1.63938 1.83021 1.10617 -0.34098 -0.13861 0.06808  152 GLU A CB  
1111 C CG  . GLU A 152 ? 1.66844 1.84136 1.02135 -0.36389 -0.17462 0.07962  152 GLU A CG  
1112 C CD  . GLU A 152 ? 1.82556 2.09052 1.20913 -0.37795 -0.22409 0.15394  152 GLU A CD  
1113 O OE1 . GLU A 152 ? 1.71509 2.05365 1.20866 -0.35203 -0.20570 0.20454  152 GLU A OE1 
1114 O OE2 . GLU A 152 ? 1.88394 2.14663 1.17905 -0.41503 -0.28157 0.16380  152 GLU A OE2 
1115 N N   . SER A 153 ? 1.40236 1.58407 1.03615 -0.27367 -0.02429 0.02581  153 SER A N   
1116 C CA  . SER A 153 ? 1.33634 1.52690 1.04723 -0.25920 -0.00400 0.00995  153 SER A CA  
1117 C C   . SER A 153 ? 1.30263 1.44208 0.99795 -0.25706 0.02153  -0.05008 153 SER A C   
1118 O O   . SER A 153 ? 1.30533 1.43890 1.01781 -0.26465 0.00711  -0.07560 153 SER A O   
1119 C CB  . SER A 153 ? 1.35431 1.56827 1.12490 -0.22807 0.03750  0.04216  153 SER A CB  
1120 O OG  . SER A 153 ? 1.30995 1.58167 1.12028 -0.22238 0.01802  0.10445  153 SER A OG  
1121 N N   . ILE A 154 ? 1.15560 1.26037 0.81727 -0.24663 0.05914  -0.06773 154 ILE A N   
1122 C CA  . ILE A 154 ? 1.20405 1.27493 0.86930 -0.24086 0.08854  -0.11391 154 ILE A CA  
1123 C C   . ILE A 154 ? 1.42590 1.46340 1.04191 -0.25637 0.06365  -0.14373 154 ILE A C   
1124 O O   . ILE A 154 ? 1.39634 1.42624 1.04087 -0.25146 0.07380  -0.17278 154 ILE A O   
1125 C CB  . ILE A 154 ? 1.14918 1.19275 0.79056 -0.22780 0.13444  -0.11822 154 ILE A CB  
1126 C CG1 . ILE A 154 ? 1.12141 1.18520 0.82595 -0.21389 0.16800  -0.09916 154 ILE A CG1 
1127 C CG2 . ILE A 154 ? 1.13028 1.14423 0.76867 -0.22306 0.16113  -0.15686 154 ILE A CG2 
1128 C CD1 . ILE A 154 ? 1.21662 1.26209 0.89257 -0.20269 0.20462  -0.07868 154 ILE A CD1 
1129 N N   . TYR A 155 ? 1.59290 1.60652 1.13015 -0.27619 0.03042  -0.13589 155 TYR A N   
1130 C CA  . TYR A 155 ? 1.63647 1.59771 1.11301 -0.29362 0.01048  -0.16750 155 TYR A CA  
1131 C C   . TYR A 155 ? 1.63544 1.62453 1.16160 -0.31064 -0.02849 -0.16273 155 TYR A C   
1132 O O   . TYR A 155 ? 1.65068 1.61239 1.18286 -0.30967 -0.02331 -0.19112 155 TYR A O   
1133 C CB  . TYR A 155 ? 1.74005 1.64861 1.09574 -0.31466 -0.01344 -0.16765 155 TYR A CB  
1134 C CG  . TYR A 155 ? 1.82009 1.65499 1.09724 -0.33776 -0.03503 -0.20229 155 TYR A CG  
1135 C CD1 . TYR A 155 ? 1.85538 1.61652 1.08131 -0.31940 0.00846  -0.24023 155 TYR A CD1 
1136 C CD2 . TYR A 155 ? 1.90109 1.73866 1.16063 -0.37772 -0.09559 -0.19338 155 TYR A CD2 
1137 C CE1 . TYR A 155 ? 1.95761 1.63594 1.10415 -0.33699 -0.00314 -0.27155 155 TYR A CE1 
1138 C CE2 . TYR A 155 ? 2.01200 1.76805 1.19519 -0.40304 -0.11331 -0.22733 155 TYR A CE2 
1139 C CZ  . TYR A 155 ? 2.07368 1.74375 1.19505 -0.38086 -0.06456 -0.26801 155 TYR A CZ  
1140 O OH  . TYR A 155 ? 2.19227 1.76628 1.22969 -0.40267 -0.07444 -0.30138 155 TYR A OH  
1141 N N   . ILE A 156 ? 1.62376 1.67127 1.19360 -0.32179 -0.06225 -0.12094 156 ILE A N   
1142 C CA  . ILE A 156 ? 1.38226 1.45904 1.00377 -0.33749 -0.09712 -0.10888 156 ILE A CA  
1143 C C   . ILE A 156 ? 1.46901 1.57104 1.17412 -0.30934 -0.06747 -0.11838 156 ILE A C   
1144 O O   . ILE A 156 ? 1.35189 1.45537 1.08687 -0.31415 -0.08080 -0.12515 156 ILE A O   
1145 C CB  . ILE A 156 ? 1.12057 1.26211 0.77485 -0.35463 -0.13877 -0.05167 156 ILE A CB  
1146 C CG1 . ILE A 156 ? 1.11573 1.27857 0.81092 -0.38040 -0.18032 -0.03784 156 ILE A CG1 
1147 C CG2 . ILE A 156 ? 1.39101 1.59196 1.12247 -0.32099 -0.10916 -0.01331 156 ILE A CG2 
1148 C CD1 . ILE A 156 ? 1.42043 1.50708 1.03933 -0.41369 -0.20305 -0.08048 156 ILE A CD1 
1149 N N   . SER A 157 ? 1.32197 1.43929 1.06030 -0.28158 -0.02752 -0.11981 157 SER A N   
1150 C CA  . SER A 157 ? 1.13791 1.27137 0.93796 -0.25899 -0.00244 -0.13503 157 SER A CA  
1151 C C   . SER A 157 ? 1.18398 1.28271 0.96838 -0.25375 0.01620  -0.17806 157 SER A C   
1152 O O   . SER A 157 ? 1.40389 1.52146 1.23659 -0.23699 0.03287  -0.19105 157 SER A O   
1153 C CB  . SER A 157 ? 0.98612 1.13699 0.81882 -0.23874 0.03116  -0.12461 157 SER A CB  
1154 O OG  . SER A 157 ? 1.17117 1.29331 0.97310 -0.23630 0.06051  -0.14506 157 SER A OG  
1155 N N   . SER A 158 ? 1.21428 1.26170 0.92902 -0.26532 0.01580  -0.19782 158 SER A N   
1156 C CA  . SER A 158 ? 1.35081 1.36386 1.05240 -0.25344 0.04156  -0.23060 158 SER A CA  
1157 C C   . SER A 158 ? 1.39332 1.37667 1.08022 -0.26173 0.02367  -0.24198 158 SER A C   
1158 O O   . SER A 158 ? 1.49284 1.45748 1.18519 -0.24442 0.04914  -0.26191 158 SER A O   
1159 C CB  . SER A 158 ? 1.56229 1.52286 1.19066 -0.25059 0.06918  -0.24478 158 SER A CB  
1160 O OG  . SER A 158 ? 1.41872 1.32016 0.95168 -0.27299 0.04558  -0.24803 158 SER A OG  
1161 N N   . VAL A 159 ? 1.18206 1.16439 0.85826 -0.28748 -0.01769 -0.22504 159 VAL A N   
1162 C CA  . VAL A 159 ? 1.25419 1.20183 0.91873 -0.30134 -0.03561 -0.23312 159 VAL A CA  
1163 C C   . VAL A 159 ? 1.45610 1.45528 1.20905 -0.28018 -0.03091 -0.22276 159 VAL A C   
1164 O O   . VAL A 159 ? 1.37376 1.43558 1.18917 -0.26427 -0.02827 -0.20359 159 VAL A O   
1165 C CB  . VAL A 159 ? 1.20041 1.13408 0.82799 -0.34435 -0.08632 -0.21454 159 VAL A CB  
1166 C CG1 . VAL A 159 ? 1.55933 1.44468 1.17241 -0.36494 -0.10326 -0.22491 159 VAL A CG1 
1167 C CG2 . VAL A 159 ? 1.60033 1.48611 1.12903 -0.36466 -0.09528 -0.22310 159 VAL A CG2 
1168 N N   . SER A 160 ? 1.45529 1.41866 1.20430 -0.27577 -0.02361 -0.23670 160 SER A N   
1169 C CA  . SER A 160 ? 1.45693 1.46046 1.27756 -0.25253 -0.01683 -0.22668 160 SER A CA  
1170 C C   . SER A 160 ? 1.44488 1.44757 1.28777 -0.27442 -0.04847 -0.20343 160 SER A C   
1171 O O   . SER A 160 ? 1.55952 1.49555 1.35369 -0.30186 -0.06111 -0.21329 160 SER A O   
1172 C CB  . SER A 160 ? 1.38821 1.36513 1.20313 -0.22374 0.02135  -0.24950 160 SER A CB  
1173 O OG  . SER A 160 ? 1.74346 1.73242 1.60165 -0.20710 0.02499  -0.23993 160 SER A OG  
1174 N N   . PHE A 161 ? 1.21178 1.28398 1.12592 -0.26308 -0.05910 -0.17084 161 PHE A N   
1175 C CA  . PHE A 161 ? 1.22312 1.31923 1.18447 -0.27674 -0.08444 -0.13487 161 PHE A CA  
1176 C C   . PHE A 161 ? 1.44328 1.55755 1.45493 -0.24288 -0.06349 -0.12806 161 PHE A C   
1177 O O   . PHE A 161 ? 1.44877 1.56345 1.45890 -0.21074 -0.03453 -0.14989 161 PHE A O   
1178 C CB  . PHE A 161 ? 1.31629 1.47539 1.31716 -0.28001 -0.10210 -0.09496 161 PHE A CB  
1179 C CG  . PHE A 161 ? 0.99999 1.14983 0.95082 -0.30351 -0.11626 -0.09905 161 PHE A CG  
1180 C CD1 . PHE A 161 ? 1.11501 1.23726 1.02305 -0.34995 -0.15454 -0.09292 161 PHE A CD1 
1181 C CD2 . PHE A 161 ? 1.08636 1.25272 1.02927 -0.28072 -0.09202 -0.10817 161 PHE A CD2 
1182 C CE1 . PHE A 161 ? 1.18723 1.30542 1.04281 -0.36843 -0.16879 -0.09194 161 PHE A CE1 
1183 C CE2 . PHE A 161 ? 1.20820 1.36680 1.10519 -0.29798 -0.10036 -0.10634 161 PHE A CE2 
1184 C CZ  . PHE A 161 ? 1.32804 1.46506 1.17965 -0.33947 -0.13895 -0.09685 161 PHE A CZ  
1185 N N   . PHE A 162 ? 1.46019 1.59570 1.52177 -0.25029 -0.07928 -0.09137 162 PHE A N   
1186 C CA  . PHE A 162 ? 1.31695 1.47463 1.42683 -0.21457 -0.05854 -0.07630 162 PHE A CA  
1187 C C   . PHE A 162 ? 1.26277 1.47439 1.39503 -0.17184 -0.03859 -0.07211 162 PHE A C   
1188 O O   . PHE A 162 ? 1.21118 1.42720 1.34058 -0.13959 -0.01584 -0.09062 162 PHE A O   
1189 C CB  . PHE A 162 ? 1.59574 1.77220 1.76247 -0.23011 -0.07661 -0.02960 162 PHE A CB  
1190 C CG  . PHE A 162 ? 1.64010 1.82537 1.84729 -0.19588 -0.05314 -0.01348 162 PHE A CG  
1191 C CD1 . PHE A 162 ? 1.46826 1.61589 1.64909 -0.17334 -0.02707 -0.04326 162 PHE A CD1 
1192 C CD2 . PHE A 162 ? 1.58322 1.81398 1.85780 -0.18520 -0.05476 0.03829  162 PHE A CD2 
1193 C CE1 . PHE A 162 ? 1.49803 1.65777 1.71693 -0.13765 -0.00397 -0.02252 162 PHE A CE1 
1194 C CE2 . PHE A 162 ? 1.49518 1.73161 1.80593 -0.15093 -0.03019 0.05811  162 PHE A CE2 
1195 C CZ  . PHE A 162 ? 1.59050 1.79228 1.87192 -0.12667 -0.00572 0.02740  162 PHE A CZ  
1196 N N   . SER A 163 ? 1.23624 1.48311 1.38057 -0.17345 -0.04663 -0.05144 163 SER A N   
1197 C CA  . SER A 163 ? 1.37427 1.65379 1.52409 -0.13730 -0.02627 -0.05132 163 SER A CA  
1198 C C   . SER A 163 ? 1.22573 1.49122 1.33873 -0.12695 -0.01113 -0.09836 163 SER A C   
1199 O O   . SER A 163 ? 1.18865 1.47386 1.30559 -0.09662 0.00371  -0.10663 163 SER A O   
1200 C CB  . SER A 163 ? 1.53240 1.83459 1.69011 -0.14271 -0.03106 -0.02370 163 SER A CB  
1201 O OG  . SER A 163 ? 1.30837 1.59228 1.43265 -0.17601 -0.04630 -0.03819 163 SER A OG  
1202 N N   . ASP A 164 ? 1.10258 1.33321 1.17977 -0.15185 -0.01504 -0.12700 164 ASP A N   
1203 C CA  . ASP A 164 ? 1.03324 1.25818 1.08849 -0.14192 0.00249  -0.16339 164 ASP A CA  
1204 C C   . ASP A 164 ? 1.15550 1.38094 1.22131 -0.11926 0.01694  -0.17351 164 ASP A C   
1205 O O   . ASP A 164 ? 1.20298 1.46096 1.28086 -0.09689 0.02814  -0.18499 164 ASP A O   
1206 C CB  . ASP A 164 ? 1.22071 1.40706 1.23199 -0.16904 0.00125  -0.18342 164 ASP A CB  
1207 C CG  . ASP A 164 ? 1.23453 1.43059 1.23772 -0.18371 -0.00780 -0.17138 164 ASP A CG  
1208 O OD1 . ASP A 164 ? 1.31608 1.54277 1.34086 -0.16723 0.00019  -0.16365 164 ASP A OD1 
1209 O OD2 . ASP A 164 ? 1.11658 1.28572 1.08620 -0.21071 -0.02188 -0.16835 164 ASP A OD2 
1210 N N   . LYS A 165 ? 1.12849 1.31841 1.19057 -0.12575 0.01642  -0.16683 165 LYS A N   
1211 C CA  . LYS A 165 ? 0.98524 1.17363 1.05913 -0.09810 0.03707  -0.17009 165 LYS A CA  
1212 C C   . LYS A 165 ? 1.05517 1.29654 1.17010 -0.06416 0.03906  -0.14736 165 LYS A C   
1213 O O   . LYS A 165 ? 0.94533 1.22147 1.07264 -0.03469 0.05176  -0.15208 165 LYS A O   
1214 C CB  . LYS A 165 ? 1.17039 1.29054 1.22223 -0.11320 0.04217  -0.16955 165 LYS A CB  
1215 C CG  . LYS A 165 ? 1.41965 1.47058 1.40818 -0.13979 0.04732  -0.19745 165 LYS A CG  
1216 C CD  . LYS A 165 ? 1.59227 1.55764 1.54423 -0.14906 0.06099  -0.20307 165 LYS A CD  
1217 C CE  . LYS A 165 ? 1.58226 1.46002 1.44880 -0.17609 0.06682  -0.23260 165 LYS A CE  
1218 N NZ  . LYS A 165 ? 1.70162 1.59526 1.54377 -0.20647 0.03787  -0.23841 165 LYS A NZ  
1219 N N   . VAL A 166 ? 1.09343 1.34439 1.22955 -0.06644 0.02707  -0.11814 166 VAL A N   
1220 C CA  . VAL A 166 ? 0.94136 1.23597 1.10403 -0.03037 0.03276  -0.09400 166 VAL A CA  
1221 C C   . VAL A 166 ? 0.90620 1.23581 1.05242 -0.01468 0.03308  -0.11231 166 VAL A C   
1222 O O   . VAL A 166 ? 0.96583 1.32735 1.11348 0.01616  0.03901  -0.11205 166 VAL A O   
1223 C CB  . VAL A 166 ? 0.99706 1.29716 1.18689 -0.03537 0.02464  -0.05417 166 VAL A CB  
1224 C CG1 . VAL A 166 ? 0.80124 1.13751 1.00415 0.00754  0.03739  -0.02897 166 VAL A CG1 
1225 C CG2 . VAL A 166 ? 0.94714 1.21790 1.16055 -0.05253 0.02178  -0.03423 166 VAL A CG2 
1226 N N   . ARG A 167 ? 0.91401 1.23602 1.04145 -0.03737 0.02542  -0.12675 167 ARG A N   
1227 C CA  . ARG A 167 ? 0.89703 1.23861 1.00507 -0.03059 0.02587  -0.14745 167 ARG A CA  
1228 C C   . ARG A 167 ? 0.93092 1.29613 1.04034 -0.02621 0.02752  -0.17326 167 ARG A C   
1229 O O   . ARG A 167 ? 1.02986 1.42603 1.13234 -0.01210 0.02305  -0.18224 167 ARG A O   
1230 C CB  . ARG A 167 ? 0.88776 1.20925 0.97870 -0.05642 0.02313  -0.15560 167 ARG A CB  
1231 C CG  . ARG A 167 ? 0.83241 1.14940 0.92256 -0.04606 0.02697  -0.12529 167 ARG A CG  
1232 C CD  . ARG A 167 ? 0.80439 1.10329 0.87830 -0.06471 0.02998  -0.12810 167 ARG A CD  
1233 N NE  . ARG A 167 ? 1.11723 1.40476 1.19539 -0.09557 0.01943  -0.12645 167 ARG A NE  
1234 C CZ  . ARG A 167 ? 1.12093 1.40831 1.21023 -0.10745 0.01259  -0.09370 167 ARG A CZ  
1235 N NH1 . ARG A 167 ? 0.99617 1.29757 1.10465 -0.08762 0.02084  -0.05392 167 ARG A NH1 
1236 N NH2 . ARG A 167 ? 1.31031 1.58428 1.38838 -0.13836 -0.00165 -0.09779 167 ARG A NH2 
1237 N N   . ASN A 168 ? 1.02530 1.37584 1.14063 -0.03873 0.03411  -0.18357 168 ASN A N   
1238 C CA  . ASN A 168 ? 1.06752 1.45038 1.19732 -0.02872 0.04143  -0.19674 168 ASN A CA  
1239 C C   . ASN A 168 ? 1.11015 1.53263 1.26018 0.00684  0.04386  -0.17880 168 ASN A C   
1240 O O   . ASN A 168 ? 1.11729 1.59360 1.27794 0.01898  0.03558  -0.18269 168 ASN A O   
1241 C CB  . ASN A 168 ? 1.19837 1.54524 1.32324 -0.03959 0.05871  -0.20448 168 ASN A CB  
1242 C CG  . ASN A 168 ? 1.35670 1.73974 1.50830 -0.01780 0.07603  -0.20311 168 ASN A CG  
1243 O OD1 . ASN A 168 ? 1.42186 1.80039 1.58443 0.00738  0.09199  -0.18691 168 ASN A OD1 
1244 N ND2 . ASN A 168 ? 1.31369 1.73526 1.48207 -0.02662 0.07534  -0.21492 168 ASN A ND2 
1245 N N   . LEU A 169 ? 1.10331 1.50114 1.25942 0.02181  0.05354  -0.15664 169 LEU A N   
1246 C CA  . LEU A 169 ? 1.00441 1.43629 1.17952 0.06038  0.06092  -0.13331 169 LEU A CA  
1247 C C   . LEU A 169 ? 0.87752 1.35191 1.03994 0.07824  0.04488  -0.12860 169 LEU A C   
1248 O O   . LEU A 169 ? 0.88119 1.40837 1.04913 0.10262  0.03998  -0.12343 169 LEU A O   
1249 C CB  . LEU A 169 ? 1.05091 1.43880 1.23512 0.06786  0.07497  -0.10841 169 LEU A CB  
1250 C CG  . LEU A 169 ? 1.00288 1.41852 1.20805 0.11132  0.08852  -0.07709 169 LEU A CG  
1251 C CD1 . LEU A 169 ? 0.86524 1.31646 1.08715 0.13746  0.10413  -0.07485 169 LEU A CD1 
1252 C CD2 . LEU A 169 ? 0.99051 1.35308 1.20958 0.10875  0.10254  -0.05264 169 LEU A CD2 
1253 N N   . ILE A 170 ? 0.92079 1.37057 1.06084 0.06807  0.03773  -0.12776 170 ILE A N   
1254 C CA  . ILE A 170 ? 0.85884 1.32681 0.96749 0.08772  0.02943  -0.12510 170 ILE A CA  
1255 C C   . ILE A 170 ? 0.91475 1.40732 0.99918 0.07063  0.01060  -0.15833 170 ILE A C   
1256 O O   . ILE A 170 ? 1.10453 1.62400 1.15873 0.08695  -0.00217 -0.16203 170 ILE A O   
1257 C CB  . ILE A 170 ? 0.84636 1.27552 0.93961 0.08643  0.03628  -0.10868 170 ILE A CB  
1258 C CG1 . ILE A 170 ? 0.65105 1.06574 0.78197 0.09604  0.04985  -0.07083 170 ILE A CG1 
1259 C CG2 . ILE A 170 ? 1.00057 1.43009 1.04595 0.11384  0.03747  -0.10462 170 ILE A CG2 
1260 C CD1 . ILE A 170 ? 0.57163 0.96749 0.70437 0.10152  0.05823  -0.04007 170 ILE A CD1 
1261 N N   . GLU A 171 ? 0.70153 1.18273 0.79515 0.03529  0.00739  -0.18217 171 GLU A N   
1262 C CA  . GLU A 171 ? 0.89086 1.39660 0.97400 0.01255  -0.01008 -0.21097 171 GLU A CA  
1263 C C   . GLU A 171 ? 1.02131 1.59752 1.13465 0.02343  -0.02206 -0.20751 171 GLU A C   
1264 O O   . GLU A 171 ? 0.90790 1.52060 1.01358 0.00692  -0.04562 -0.22484 171 GLU A O   
1265 C CB  . GLU A 171 ? 1.07537 1.55596 1.17037 -0.02372 -0.00460 -0.22980 171 GLU A CB  
1266 C CG  . GLU A 171 ? 1.25512 1.69045 1.31104 -0.04433 -0.00555 -0.24589 171 GLU A CG  
1267 C CD  . GLU A 171 ? 1.55173 1.96471 1.62046 -0.07610 0.00302  -0.25918 171 GLU A CD  
1268 O OE1 . GLU A 171 ? 1.35426 1.73502 1.42457 -0.07868 0.01534  -0.24663 171 GLU A OE1 
1269 O OE2 . GLU A 171 ? 1.81642 2.24659 1.89436 -0.09993 -0.00402 -0.27982 171 GLU A OE2 
1270 N N   . LYS A 172 ? 1.14390 1.73950 1.29427 0.04846  -0.00578 -0.18312 172 LYS A N   
1271 C CA  . LYS A 172 ? 0.84352 1.51484 1.02826 0.06903  -0.01245 -0.16779 172 LYS A CA  
1272 C C   . LYS A 172 ? 0.77580 1.48894 0.92704 0.08606  -0.03938 -0.16403 172 LYS A C   
1273 O O   . LYS A 172 ? 0.79680 1.57846 0.96075 0.07764  -0.06601 -0.16737 172 LYS A O   
1274 C CB  . LYS A 172 ? 0.80934 1.47722 1.02757 0.10216  0.01809  -0.13743 172 LYS A CB  
1275 C CG  . LYS A 172 ? 0.89798 1.52854 1.13890 0.08704  0.04407  -0.14307 172 LYS A CG  
1276 C CD  . LYS A 172 ? 1.26155 1.86487 1.51895 0.11873  0.07840  -0.11670 172 LYS A CD  
1277 C CE  . LYS A 172 ? 1.30801 1.85222 1.56411 0.10390  0.10714  -0.12683 172 LYS A CE  
1278 N NZ  . LYS A 172 ? 1.38513 1.88057 1.64284 0.13203  0.14444  -0.10555 172 LYS A NZ  
1279 N N   . ASP A 173 ? 0.71845 1.39187 0.82414 0.10923  -0.03375 -0.15478 173 ASP A N   
1280 C CA  . ASP A 173 ? 0.91018 1.60936 0.96440 0.13202  -0.05444 -0.15033 173 ASP A CA  
1281 C C   . ASP A 173 ? 1.02306 1.64901 1.01221 0.14114  -0.04343 -0.15390 173 ASP A C   
1282 O O   . ASP A 173 ? 1.01929 1.62912 0.99972 0.17992  -0.02258 -0.12336 173 ASP A O   
1283 C CB  . ASP A 173 ? 0.80837 1.56278 0.88751 0.17985  -0.04652 -0.11062 173 ASP A CB  
1284 C CG  . ASP A 173 ? 1.09870 1.89735 1.12205 0.20007  -0.07605 -0.10688 173 ASP A CG  
1285 O OD1 . ASP A 173 ? 1.25799 2.03540 1.21670 0.17263  -0.10388 -0.14023 173 ASP A OD1 
1286 O OD2 . ASP A 173 ? 1.18840 2.03711 1.22546 0.24348  -0.07057 -0.07055 173 ASP A OD2 
1287 N N   . LEU A 174 ? 1.08276 1.66375 1.02873 0.10745  -0.05321 -0.18716 174 LEU A N   
1288 C CA  . LEU A 174 ? 1.03449 1.54165 0.91850 0.11857  -0.03564 -0.18737 174 LEU A CA  
1289 C C   . LEU A 174 ? 1.20209 1.70212 1.01386 0.16042  -0.03563 -0.17402 174 LEU A C   
1290 O O   . LEU A 174 ? 1.38216 1.82506 1.15195 0.18628  -0.00870 -0.15817 174 LEU A O   
1291 C CB  . LEU A 174 ? 1.09609 1.55298 0.93819 0.07759  -0.04361 -0.22615 174 LEU A CB  
1292 C CG  . LEU A 174 ? 1.07931 1.50088 0.95990 0.04859  -0.02643 -0.23139 174 LEU A CG  
1293 C CD1 . LEU A 174 ? 1.03212 1.39041 0.85331 0.02130  -0.02574 -0.26282 174 LEU A CD1 
1294 C CD2 . LEU A 174 ? 1.05270 1.45152 0.96251 0.07303  0.00286  -0.19399 174 LEU A CD2 
1295 N N   . SER A 175 ? 1.30070 1.85930 1.09511 0.17020  -0.06368 -0.17571 175 SER A N   
1296 C CA  . SER A 175 ? 1.26131 1.80993 0.96936 0.21005  -0.06676 -0.16555 175 SER A CA  
1297 C C   . SER A 175 ? 1.15704 1.73167 0.89633 0.26735  -0.03861 -0.11333 175 SER A C   
1298 O O   . SER A 175 ? 1.29140 1.84335 0.95847 0.30998  -0.02724 -0.09598 175 SER A O   
1299 C CB  . SER A 175 ? 1.22392 1.82792 0.88893 0.19147  -0.11726 -0.18937 175 SER A CB  
1300 O OG  . SER A 175 ? 1.33731 1.93435 1.00164 0.13008  -0.14671 -0.23360 175 SER A OG  
1301 N N   . ARG A 176 ? 1.17739 1.78760 1.01550 0.26995  -0.02277 -0.08771 176 ARG A N   
1302 C CA  . ARG A 176 ? 1.21714 1.84877 1.09310 0.31943  0.00534  -0.03780 176 ARG A CA  
1303 C C   . ARG A 176 ? 1.12481 1.69362 0.98884 0.34583  0.04377  -0.00924 176 ARG A C   
1304 O O   . ARG A 176 ? 1.27041 1.78519 1.12117 0.32322  0.05228  -0.02337 176 ARG A O   
1305 C CB  . ARG A 176 ? 1.07762 1.74352 1.05267 0.30869  0.01509  -0.02382 176 ARG A CB  
1306 C CG  . ARG A 176 ? 0.98828 1.67705 1.00773 0.35636  0.04426  0.02639  176 ARG A CG  
1307 C CD  . ARG A 176 ? 0.98858 1.63644 1.07913 0.34139  0.07348  0.04021  176 ARG A CD  
1308 N NE  . ARG A 176 ? 0.91238 1.57523 1.04867 0.31016  0.06733  0.02003  176 ARG A NE  
1309 C CZ  . ARG A 176 ? 1.01395 1.70414 1.19698 0.33020  0.08469  0.04215  176 ARG A CZ  
1310 N NH1 . ARG A 176 ? 1.05658 1.76267 1.25305 0.37882  0.10832  0.08537  176 ARG A NH1 
1311 N NH2 . ARG A 176 ? 0.77992 1.47855 0.99554 0.30523  0.08389  0.02416  176 ARG A NH2 
1312 N N   . LYS A 177 ? 1.07855 1.66013 0.95220 0.39721  0.06953  0.03780  177 LYS A N   
1313 C CA  . LYS A 177 ? 1.02336 1.56045 0.90727 0.42656  0.10992  0.07887  177 LYS A CA  
1314 C C   . LYS A 177 ? 1.05608 1.59102 1.04566 0.40503  0.12654  0.10129  177 LYS A C   
1315 O O   . LYS A 177 ? 1.21516 1.76584 1.25760 0.43068  0.14823  0.14133  177 LYS A O   
1316 C CB  . LYS A 177 ? 1.15531 1.70454 0.99805 0.49202  0.13220  0.12160  177 LYS A CB  
1317 C CG  . LYS A 177 ? 1.48215 2.02312 1.19838 0.51243  0.11231  0.09686  177 LYS A CG  
1318 C CD  . LYS A 177 ? 1.37780 1.83897 1.01282 0.52122  0.13384  0.08971  177 LYS A CD  
1319 C CE  . LYS A 177 ? 1.43775 1.86489 0.96975 0.48530  0.09703  0.02630  177 LYS A CE  
1320 N NZ  . LYS A 177 ? 1.56932 1.98468 1.15258 0.42097  0.07922  -0.01249 177 LYS A NZ  
1321 N N   . TRP A 178 ? 1.07628 1.58525 1.09041 0.35512  0.11582  0.07419  178 TRP A N   
1322 C CA  . TRP A 178 ? 1.01708 1.51362 1.11335 0.32542  0.12424  0.08824  178 TRP A CA  
1323 C C   . TRP A 178 ? 1.04595 1.52242 1.18259 0.34445  0.15399  0.14185  178 TRP A C   
1324 O O   . TRP A 178 ? 0.98188 1.44125 1.08789 0.36495  0.16872  0.16046  178 TRP A O   
1325 C CB  . TRP A 178 ? 0.83712 1.31157 0.93762 0.27013  0.10422  0.04890  178 TRP A CB  
1326 C CG  . TRP A 178 ? 0.80878 1.30511 0.89029 0.24583  0.07863  0.00296  178 TRP A CG  
1327 C CD1 . TRP A 178 ? 0.95847 1.46139 0.98143 0.23724  0.05809  -0.03233 178 TRP A CD1 
1328 C CD2 . TRP A 178 ? 0.81286 1.32504 0.93654 0.22571  0.07333  -0.00988 178 TRP A CD2 
1329 N NE1 . TRP A 178 ? 1.13808 1.67325 1.17757 0.21104  0.03740  -0.06215 178 TRP A NE1 
1330 C CE2 . TRP A 178 ? 0.87238 1.41367 0.97234 0.20798  0.04986  -0.04723 178 TRP A CE2 
1331 C CE3 . TRP A 178 ? 0.77313 1.27051 0.94851 0.22101  0.08913  0.00757  178 TRP A CE3 
1332 C CZ2 . TRP A 178 ? 0.88848 1.45366 1.02259 0.19214  0.04597  -0.06097 178 TRP A CZ2 
1333 C CZ3 . TRP A 178 ? 0.87217 1.37810 1.06563 0.20656  0.08762  -0.01179 178 TRP A CZ3 
1334 C CH2 . TRP A 178 ? 0.90516 1.44931 1.08196 0.19542  0.06824  -0.04254 178 TRP A CH2 
1335 N N   . THR A 179 ? 1.03974 1.51412 1.24754 0.33510  0.16482  0.16841  179 THR A N   
1336 C CA  . THR A 179 ? 0.94316 1.40395 1.21236 0.33681  0.18660  0.22109  179 THR A CA  
1337 C C   . THR A 179 ? 0.81423 1.25130 1.14155 0.27830  0.17183  0.21182  179 THR A C   
1338 O O   . THR A 179 ? 0.94347 1.36943 1.25616 0.24725  0.15315  0.16724  179 THR A O   
1339 C CB  . THR A 179 ? 0.84631 1.32061 1.13935 0.38930  0.21910  0.27272  179 THR A CB  
1340 O OG1 . THR A 179 ? 0.97387 1.44977 1.28903 0.38631  0.21960  0.26325  179 THR A OG1 
1341 C CG2 . THR A 179 ? 0.84261 1.33533 1.05850 0.44902  0.23131  0.27881  179 THR A CG2 
1342 N N   . LEU A 180 ? 0.76578 1.19402 1.15724 0.26230  0.18023  0.25655  180 LEU A N   
1343 C CA  . LEU A 180 ? 0.98641 1.38441 1.42276 0.20115  0.16119  0.24812  180 LEU A CA  
1344 C C   . LEU A 180 ? 0.94224 1.31074 1.39274 0.20014  0.17285  0.24258  180 LEU A C   
1345 O O   . LEU A 180 ? 0.97816 1.30436 1.42449 0.15392  0.15762  0.21019  180 LEU A O   
1346 C CB  . LEU A 180 ? 1.10890 1.51435 1.61715 0.17892  0.16117  0.30302  180 LEU A CB  
1347 C CG  . LEU A 180 ? 0.96747 1.34672 1.50771 0.10437  0.12756  0.29171  180 LEU A CG  
1348 C CD1 . LEU A 180 ? 0.85715 1.24045 1.35285 0.07721  0.10054  0.25238  180 LEU A CD1 
1349 C CD2 . LEU A 180 ? 1.09226 1.49212 1.72157 0.08540  0.12786  0.35922  180 LEU A CD2 
1350 N N   . GLY A 181 ? 0.93211 1.31559 1.39444 0.25357  0.20425  0.27713  181 GLY A N   
1351 C CA  . GLY A 181 ? 0.90745 1.26263 1.37940 0.26374  0.22380  0.27600  181 GLY A CA  
1352 C C   . GLY A 181 ? 1.08531 1.43792 1.50537 0.26350  0.21454  0.22318  181 GLY A C   
1353 O O   . GLY A 181 ? 1.27860 1.58367 1.70063 0.24267  0.22195  0.20512  181 GLY A O   
1354 N N   . ILE A 182 ? 1.05989 1.46075 1.43169 0.28888  0.20169  0.20068  182 ILE A N   
1355 C CA  . ILE A 182 ? 1.09095 1.50506 1.42578 0.28588  0.18967  0.15626  182 ILE A CA  
1356 C C   . ILE A 182 ? 1.13033 1.49794 1.45910 0.22560  0.17102  0.11505  182 ILE A C   
1357 O O   . ILE A 182 ? 1.18018 1.51966 1.50325 0.21683  0.18016  0.09478  182 ILE A O   
1358 C CB  . ILE A 182 ? 0.91946 1.39039 1.20478 0.31035  0.17111  0.13903  182 ILE A CB  
1359 C CG1 . ILE A 182 ? 1.01712 1.52576 1.29151 0.37238  0.18971  0.18010  182 ILE A CG1 
1360 C CG2 . ILE A 182 ? 0.64718 1.14407 0.91035 0.30201  0.15563  0.09979  182 ILE A CG2 
1361 C CD1 . ILE A 182 ? 1.10356 1.66057 1.31246 0.39686  0.16892  0.16081  182 ILE A CD1 
1362 N N   . ILE A 183 ? 1.14641 1.50469 1.47213 0.18803  0.14828  0.10600  183 ILE A N   
1363 C CA  . ILE A 183 ? 1.12357 1.43830 1.43689 0.13126  0.12860  0.07093  183 ILE A CA  
1364 C C   . ILE A 183 ? 1.23824 1.48477 1.56808 0.10501  0.14073  0.07508  183 ILE A C   
1365 O O   . ILE A 183 ? 1.36649 1.56634 1.66601 0.08201  0.14209  0.04121  183 ILE A O   
1366 C CB  . ILE A 183 ? 1.03593 1.35703 1.35406 0.10001  0.10529  0.07630  183 ILE A CB  
1367 C CG1 . ILE A 183 ? 0.90808 1.27688 1.19882 0.12991  0.10176  0.07309  183 ILE A CG1 
1368 C CG2 . ILE A 183 ? 0.78587 1.06683 1.08252 0.04376  0.08258  0.04120  183 ILE A CG2 
1369 C CD1 . ILE A 183 ? 0.86132 1.24212 1.10718 0.12437  0.08961  0.02479  183 ILE A CD1 
1370 N N   . ALA A 184 ? 1.23089 1.46328 1.60540 0.10761  0.15261  0.11766  184 ALA A N   
1371 C CA  . ALA A 184 ? 1.29590 1.45057 1.68334 0.07736  0.16436  0.12205  184 ALA A CA  
1372 C C   . ALA A 184 ? 1.45240 1.57062 1.81411 0.10756  0.19852  0.10650  184 ALA A C   
1373 O O   . ALA A 184 ? 1.53974 1.58044 1.86497 0.07655  0.20360  0.07546  184 ALA A O   
1374 C CB  . ALA A 184 ? 1.35629 1.51361 1.80825 0.08183  0.17597  0.17829  184 ALA A CB  
1375 N N   . ASP A 185 ? 1.67155 1.84252 2.04832 0.17105  0.22500  0.13203  185 ASP A N   
1376 C CA  . ASP A 185 ? 1.71435 1.86779 2.07747 0.20859  0.26080  0.12892  185 ASP A CA  
1377 C C   . ASP A 185 ? 1.75094 1.89513 2.06920 0.19387  0.25330  0.08232  185 ASP A C   
1378 O O   . ASP A 185 ? 1.88644 1.96061 2.18148 0.19110  0.28129  0.06842  185 ASP A O   
1379 C CB  . ASP A 185 ? 1.65140 1.88868 2.03374 0.27927  0.27901  0.16462  185 ASP A CB  
1380 C CG  . ASP A 185 ? 1.78551 2.01118 2.21060 0.30950  0.30955  0.21817  185 ASP A CG  
1381 O OD1 . ASP A 185 ? 1.90121 2.05706 2.35013 0.27057  0.31406  0.22839  185 ASP A OD1 
1382 O OD2 . ASP A 185 ? 1.78724 2.07434 2.22211 0.37094  0.32833  0.25208  185 ASP A OD2 
1383 N N   . ALA A 186 ? 1.44737 1.65555 1.75107 0.18631  0.22064  0.05997  186 ALA A N   
1384 C CA  . ALA A 186 ? 1.38177 1.59032 1.65230 0.17325  0.21496  0.02105  186 ALA A CA  
1385 C C   . ALA A 186 ? 1.49421 1.60263 1.72648 0.12082  0.21403  -0.01008 186 ALA A C   
1386 O O   . ALA A 186 ? 1.57650 1.64023 1.77820 0.12376  0.23799  -0.02964 186 ALA A O   
1387 C CB  . ALA A 186 ? 1.38200 1.66558 1.64490 0.16627  0.17909  0.00336  186 ALA A CB  
1388 N N   . PHE A 187 ? 1.49638 1.57012 1.72677 0.07361  0.18672  -0.01211 187 PHE A N   
1389 C CA  . PHE A 187 ? 1.38544 1.36265 1.57044 0.01747  0.17707  -0.04037 187 PHE A CA  
1390 C C   . PHE A 187 ? 1.53872 1.41486 1.71437 0.00692  0.20445  -0.03104 187 PHE A C   
1391 O O   . PHE A 187 ? 1.62538 1.40654 1.75194 -0.04572 0.19333  -0.05573 187 PHE A O   
1392 C CB  . PHE A 187 ? 1.29680 1.29099 1.48874 -0.03191 0.13068  -0.04053 187 PHE A CB  
1393 C CG  . PHE A 187 ? 1.11391 1.16831 1.29155 -0.03494 0.10761  -0.06120 187 PHE A CG  
1394 C CD1 . PHE A 187 ? 1.24342 1.38712 1.45290 -0.00054 0.10245  -0.04557 187 PHE A CD1 
1395 C CD2 . PHE A 187 ? 1.14835 1.16075 1.27313 -0.07309 0.09273  -0.09624 187 PHE A CD2 
1396 C CE1 . PHE A 187 ? 1.25065 1.43602 1.44358 -0.00682 0.08429  -0.06608 187 PHE A CE1 
1397 C CE2 . PHE A 187 ? 1.36551 1.42880 1.48103 -0.07546 0.07613  -0.11207 187 PHE A CE2 
1398 C CZ  . PHE A 187 ? 1.22298 1.37057 1.37489 -0.04401 0.07229  -0.09755 187 PHE A CZ  
1399 N N   . ASN A 188 ? 1.58974 1.47860 1.80458 0.05449  0.23991  0.00354  188 ASN A N   
1400 C CA  . ASN A 188 ? 1.62113 1.40805 1.83094 0.05036  0.27482  0.01658  188 ASN A CA  
1401 C C   . ASN A 188 ? 1.63677 1.35908 1.84871 -0.02002 0.24220  0.01693  188 ASN A C   
1402 O O   . ASN A 188 ? 1.92297 1.52230 2.08384 -0.06289 0.24937  -0.00519 188 ASN A O   
1403 C CB  . ASN A 188 ? 1.68446 1.37430 1.82797 0.06126  0.31766  -0.01178 188 ASN A CB  
1404 C CG  . ASN A 188 ? 1.87904 1.64680 2.02189 0.11352  0.33537  -0.01657 188 ASN A CG  
1405 O OD1 . ASN A 188 ? 1.73929 1.59445 1.93209 0.17191  0.35426  0.01722  188 ASN A OD1 
1406 N ND2 . ASN A 188 ? 2.19694 1.93711 2.28442 0.09136  0.32770  -0.05544 188 ASN A ND2 
1407 N N   . ALA A 189 ? 1.61828 1.42332 1.88805 -0.03276 0.20606  0.04453  189 ALA A N   
1408 C CA  . ALA A 189 ? 1.71754 1.49124 2.01378 -0.09790 0.17086  0.05930  189 ALA A CA  
1409 C C   . ALA A 189 ? 1.71676 1.57779 2.10575 -0.07096 0.17152  0.11956  189 ALA A C   
1410 O O   . ALA A 189 ? 1.74129 1.66959 2.15702 -0.00281 0.20043  0.14408  189 ALA A O   
1411 C CB  . ALA A 189 ? 1.58923 1.37077 1.84888 -0.15510 0.11815  0.02883  189 ALA A CB  
1412 N N   . SER A 190 ? 1.87855 1.74075 2.31576 -0.12450 0.13918  0.14711  190 SER A N   
1413 C CA  . SER A 190 ? 1.78760 1.72521 2.31862 -0.10240 0.14416  0.21231  190 SER A CA  
1414 C C   . SER A 190 ? 1.73045 1.77080 2.28765 -0.09671 0.11345  0.22898  190 SER A C   
1415 O O   . SER A 190 ? 1.72625 1.76939 2.24502 -0.13573 0.07626  0.19664  190 SER A O   
1416 C CB  . SER A 190 ? 1.81170 1.69567 2.39774 -0.16411 0.13141  0.24453  190 SER A CB  
1417 O OG  . SER A 190 ? 1.82562 1.78840 2.51233 -0.13966 0.14118  0.31583  190 SER A OG  
1418 N N   . GLU A 191 ? 1.32707 1.44535 1.94368 -0.04299 0.13482  0.28186  191 GLU A N   
1419 C CA  . GLU A 191 ? 1.10381 1.30883 1.74314 -0.02745 0.11818  0.30552  191 GLU A CA  
1420 C C   . GLU A 191 ? 1.24111 1.45508 1.91080 -0.09956 0.07044  0.31557  191 GLU A C   
1421 O O   . GLU A 191 ? 1.11851 1.36588 1.75936 -0.10868 0.04601  0.29681  191 GLU A O   
1422 C CB  . GLU A 191 ? 0.98357 1.24860 1.68653 0.03288  0.15322  0.37279  191 GLU A CB  
1423 C CG  . GLU A 191 ? 1.21250 1.50097 1.86982 0.11421  0.19053  0.36471  191 GLU A CG  
1424 C CD  . GLU A 191 ? 1.18670 1.54183 1.86990 0.17621  0.21587  0.41896  191 GLU A CD  
1425 O OE1 . GLU A 191 ? 0.94647 1.33260 1.69707 0.16322  0.21361  0.47215  191 GLU A OE1 
1426 O OE2 . GLU A 191 ? 1.10065 1.47678 1.73414 0.23932  0.23910  0.41130  191 GLU A OE2 
1427 N N   . ILE A 192 ? 1.36849 1.55777 2.10151 -0.15159 0.05621  0.35064  192 ILE A N   
1428 C CA  . ILE A 192 ? 1.12286 1.32995 1.89356 -0.22726 0.00326  0.36825  192 ILE A CA  
1429 C C   . ILE A 192 ? 1.17461 1.33694 1.85191 -0.27334 -0.03531 0.30000  192 ILE A C   
1430 O O   . ILE A 192 ? 1.20576 1.41791 1.88653 -0.29864 -0.07087 0.30638  192 ILE A O   
1431 C CB  . ILE A 192 ? 1.03758 1.20534 1.87806 -0.28806 -0.01054 0.40462  192 ILE A CB  
1432 C CG1 . ILE A 192 ? 1.13581 1.31470 1.99883 -0.37965 -0.07754 0.41254  192 ILE A CG1 
1433 C CG2 . ILE A 192 ? 1.23637 1.28448 2.01538 -0.29871 0.01196  0.35757  192 ILE A CG2 
1434 C CD1 . ILE A 192 ? 1.10610 1.41047 2.06836 -0.37133 -0.09303 0.48740  192 ILE A CD1 
1435 N N   . THR A 193 ? 1.39407 1.45923 1.98703 -0.28248 -0.02464 0.23902  193 THR A N   
1436 C CA  . THR A 193 ? 1.35295 1.36252 1.84977 -0.32425 -0.05474 0.17582  193 THR A CA  
1437 C C   . THR A 193 ? 1.28580 1.35658 1.74645 -0.28196 -0.05186 0.15455  193 THR A C   
1438 O O   . THR A 193 ? 1.40734 1.48686 1.83271 -0.31806 -0.08781 0.13576  193 THR A O   
1439 C CB  . THR A 193 ? 1.34893 1.23689 1.76304 -0.32818 -0.02864 0.12222  193 THR A CB  
1440 O OG1 . THR A 193 ? 1.45528 1.35838 1.85775 -0.24792 0.02424  0.11383  193 THR A OG1 
1441 C CG2 . THR A 193 ? 1.22765 1.04178 1.67560 -0.37117 -0.02673 0.14372  193 THR A CG2 
1442 N N   . ILE A 194 ? 1.34108 1.45051 1.80507 -0.20763 -0.01023 0.15665  194 ILE A N   
1443 C CA  . ILE A 194 ? 1.20696 1.37134 1.64078 -0.17053 -0.00721 0.13875  194 ILE A CA  
1444 C C   . ILE A 194 ? 1.25871 1.49873 1.74517 -0.17918 -0.02977 0.18382  194 ILE A C   
1445 O O   . ILE A 194 ? 1.28831 1.54711 1.74310 -0.19265 -0.04979 0.16607  194 ILE A O   
1446 C CB  . ILE A 194 ? 1.12918 1.32112 1.55717 -0.09530 0.03560  0.13700  194 ILE A CB  
1447 C CG1 . ILE A 194 ? 1.07317 1.21253 1.43408 -0.08201 0.05378  0.08336  194 ILE A CG1 
1448 C CG2 . ILE A 194 ? 1.14383 1.40535 1.57030 -0.05748 0.03823  0.14525  194 ILE A CG2 
1449 C CD1 . ILE A 194 ? 1.25835 1.31992 1.61376 -0.09196 0.07390  0.07954  194 ILE A CD1 
1450 N N   . ARG A 195 ? 1.28586 1.57055 1.85727 -0.16796 -0.02169 0.24860  195 ARG A N   
1451 C CA  . ARG A 195 ? 1.20630 1.56610 1.84107 -0.17221 -0.03641 0.30529  195 ARG A CA  
1452 C C   . ARG A 195 ? 1.20065 1.55908 1.83048 -0.24502 -0.08929 0.29992  195 ARG A C   
1453 O O   . ARG A 195 ? 1.17664 1.59031 1.82042 -0.24400 -0.10218 0.32292  195 ARG A O   
1454 C CB  . ARG A 195 ? 1.14656 1.54823 1.88325 -0.15772 -0.01928 0.38211  195 ARG A CB  
1455 C CG  . ARG A 195 ? 1.32693 1.73836 2.06399 -0.07878 0.03409  0.39671  195 ARG A CG  
1456 C CD  . ARG A 195 ? 1.31909 1.76480 2.15700 -0.06451 0.05562  0.47532  195 ARG A CD  
1457 N NE  . ARG A 195 ? 1.37624 1.89862 2.28971 -0.06093 0.05239  0.54535  195 ARG A NE  
1458 C CZ  . ARG A 195 ? 1.51589 2.08657 2.53429 -0.04908 0.07110  0.62860  195 ARG A CZ  
1459 N NH1 . ARG A 195 ? 1.39608 1.94297 2.45638 -0.04326 0.09270  0.65083  195 ARG A NH1 
1460 N NH2 . ARG A 195 ? 1.45113 2.09677 2.53919 -0.04080 0.07214  0.69658  195 ARG A NH2 
1461 N N   . LYS A 196 ? 1.26739 1.55804 1.87103 -0.30795 -0.11914 0.27135  196 LYS A N   
1462 C CA  . LYS A 196 ? 1.27417 1.55877 1.85976 -0.38223 -0.17590 0.26517  196 LYS A CA  
1463 C C   . LYS A 196 ? 1.40521 1.65777 1.88741 -0.38271 -0.18358 0.20247  196 LYS A C   
1464 O O   . LYS A 196 ? 1.48358 1.77862 1.96349 -0.40660 -0.21516 0.21560  196 LYS A O   
1465 C CB  . LYS A 196 ? 1.29598 1.50490 1.87588 -0.45450 -0.20679 0.25474  196 LYS A CB  
1466 C CG  . LYS A 196 ? 1.29846 1.55130 1.99963 -0.47640 -0.21402 0.32909  196 LYS A CG  
1467 C CD  . LYS A 196 ? 1.21422 1.40386 1.90864 -0.57566 -0.26923 0.32226  196 LYS A CD  
1468 C CE  . LYS A 196 ? 1.30821 1.43155 2.03830 -0.58572 -0.24476 0.33159  196 LYS A CE  
1469 N NZ  . LYS A 196 ? 1.41811 1.43784 2.05328 -0.53865 -0.19185 0.26638  196 LYS A NZ  
1470 N N   . ARG A 197 ? 1.52121 1.70576 1.92401 -0.35358 -0.15238 0.14089  197 ARG A N   
1471 C CA  . ARG A 197 ? 1.51113 1.67392 1.82832 -0.34787 -0.15265 0.08886  197 ARG A CA  
1472 C C   . ARG A 197 ? 1.52517 1.77123 1.87121 -0.30731 -0.14257 0.11391  197 ARG A C   
1473 O O   . ARG A 197 ? 1.54599 1.80225 1.85562 -0.32350 -0.16095 0.10170  197 ARG A O   
1474 C CB  . ARG A 197 ? 1.72890 1.81987 1.97520 -0.31643 -0.11477 0.03071  197 ARG A CB  
1475 C CG  . ARG A 197 ? 1.93904 1.97159 2.08273 -0.33217 -0.11862 -0.02887 197 ARG A CG  
1476 C CD  . ARG A 197 ? 1.83492 1.80694 1.91677 -0.29210 -0.07247 -0.07943 197 ARG A CD  
1477 N NE  . ARG A 197 ? 1.97490 1.94571 1.99900 -0.28521 -0.06811 -0.11383 197 ARG A NE  
1478 C CZ  . ARG A 197 ? 1.99452 1.95724 1.99168 -0.24568 -0.03205 -0.14293 197 ARG A CZ  
1479 N NH1 . ARG A 197 ? 1.86945 1.83549 1.89132 -0.20405 0.00178  -0.14121 197 ARG A NH1 
1480 N NH2 . ARG A 197 ? 1.94102 1.90246 1.89262 -0.24718 -0.03044 -0.16829 197 ARG A NH2 
1481 N N   . LEU A 198 ? 1.23118 1.53225 1.64027 -0.25559 -0.11239 0.15437  198 LEU A N   
1482 C CA  . LEU A 198 ? 1.22141 1.58551 1.65016 -0.21641 -0.09744 0.18121  198 LEU A CA  
1483 C C   . LEU A 198 ? 1.26093 1.68763 1.75348 -0.24309 -0.12495 0.24439  198 LEU A C   
1484 O O   . LEU A 198 ? 1.40234 1.85388 1.87740 -0.24335 -0.13178 0.24790  198 LEU A O   
1485 C CB  . LEU A 198 ? 1.25705 1.64669 1.71284 -0.14939 -0.05324 0.20225  198 LEU A CB  
1486 C CG  . LEU A 198 ? 0.86018 1.22501 1.24925 -0.10669 -0.02497 0.14832  198 LEU A CG  
1487 C CD1 . LEU A 198 ? 0.91496 1.30295 1.31451 -0.04404 0.01182  0.16823  198 LEU A CD1 
1488 C CD2 . LEU A 198 ? 1.22363 1.58635 1.56231 -0.11249 -0.03051 0.11630  198 LEU A CD2 
1489 N N   . GLU A 199 ? 1.30156 1.75905 1.87497 -0.26562 -0.13992 0.30020  199 GLU A N   
1490 C CA  . GLU A 199 ? 1.30575 1.84242 1.96008 -0.28608 -0.16411 0.37464  199 GLU A CA  
1491 C C   . GLU A 199 ? 1.37134 1.90769 1.99027 -0.34861 -0.21733 0.36088  199 GLU A C   
1492 O O   . GLU A 199 ? 1.27156 1.87730 1.93101 -0.35017 -0.23046 0.41151  199 GLU A O   
1493 C CB  . GLU A 199 ? 1.27062 1.84151 2.02666 -0.30706 -0.17381 0.43794  199 GLU A CB  
1494 C CG  . GLU A 199 ? 1.29039 1.89434 2.10493 -0.23529 -0.11787 0.48501  199 GLU A CG  
1495 C CD  . GLU A 199 ? 1.48986 2.12726 2.41213 -0.25723 -0.12424 0.55144  199 GLU A CD  
1496 O OE1 . GLU A 199 ? 1.50211 2.12767 2.44748 -0.33463 -0.17578 0.55205  199 GLU A OE1 
1497 O OE2 . GLU A 199 ? 1.54315 2.21365 2.52270 -0.19882 -0.07746 0.60303  199 GLU A OE2 
1498 N N   . SER A 200 ? 1.52871 1.98535 2.06744 -0.39684 -0.24519 0.29648  200 SER A N   
1499 C CA  . SER A 200 ? 1.32839 1.77434 1.81278 -0.45405 -0.29513 0.27905  200 SER A CA  
1500 C C   . SER A 200 ? 1.25262 1.72287 1.69699 -0.41788 -0.27697 0.26939  200 SER A C   
1501 O O   . SER A 200 ? 1.31818 1.83073 1.76325 -0.44594 -0.31085 0.29654  200 SER A O   
1502 C CB  . SER A 200 ? 1.35525 1.68925 1.73620 -0.49871 -0.31335 0.20395  200 SER A CB  
1503 O OG  . SER A 200 ? 1.50399 1.78225 1.79522 -0.46052 -0.27746 0.13952  200 SER A OG  
1504 N N   . GLU A 201 ? 1.10045 1.54484 1.50991 -0.35772 -0.22494 0.23285  201 GLU A N   
1505 C CA  . GLU A 201 ? 1.29072 1.74733 1.66374 -0.32286 -0.20124 0.22108  201 GLU A CA  
1506 C C   . GLU A 201 ? 1.36461 1.88271 1.80141 -0.26464 -0.16175 0.27606  201 GLU A C   
1507 O O   . GLU A 201 ? 1.28084 1.78682 1.67993 -0.22510 -0.12739 0.25542  201 GLU A O   
1508 C CB  . GLU A 201 ? 1.18770 1.57122 1.47471 -0.30244 -0.17325 0.14279  201 GLU A CB  
1509 C CG  . GLU A 201 ? 1.17511 1.48829 1.38293 -0.35147 -0.20180 0.09073  201 GLU A CG  
1510 C CD  . GLU A 201 ? 1.07855 1.32570 1.21947 -0.32774 -0.16886 0.02448  201 GLU A CD  
1511 O OE1 . GLU A 201 ? 1.22862 1.48992 1.38912 -0.27930 -0.13160 0.01753  201 GLU A OE1 
1512 O OE2 . GLU A 201 ? 1.36735 1.54830 1.43328 -0.35737 -0.18015 -0.01823 201 GLU A OE2 
1513 N N   . ASN A 202 ? 1.49670 2.07469 2.02652 -0.25934 -0.16347 0.34729  202 ASN A N   
1514 C CA  . ASN A 202 ? 1.44505 2.07866 2.03534 -0.20110 -0.12119 0.41181  202 ASN A CA  
1515 C C   . ASN A 202 ? 1.45211 2.03989 1.99178 -0.13709 -0.06473 0.37315  202 ASN A C   
1516 O O   . ASN A 202 ? 1.44785 2.03367 1.96382 -0.09609 -0.02960 0.37932  202 ASN A O   
1517 C CB  . ASN A 202 ? 1.52263 2.20741 2.12919 -0.20086 -0.12696 0.45717  202 ASN A CB  
1518 C CG  . ASN A 202 ? 1.42315 2.18001 2.11974 -0.15275 -0.09155 0.55099  202 ASN A CG  
1519 O OD1 . ASN A 202 ? 1.31867 2.05732 1.99125 -0.09148 -0.03585 0.55596  202 ASN A OD1 
1520 N ND2 . ASN A 202 ? 1.43569 2.27115 2.23486 -0.18117 -0.12214 0.62791  202 ASN A ND2 
1521 N N   . THR A 203 ? 1.30857 1.85767 1.83052 -0.12910 -0.05605 0.33625  203 THR A N   
1522 C CA  . THR A 203 ? 1.08488 1.59699 1.55803 -0.07412 -0.01193 0.30088  203 THR A CA  
1523 C C   . THR A 203 ? 1.00280 1.51525 1.51048 -0.05425 0.00132  0.31656  203 THR A C   
1524 O O   . THR A 203 ? 1.15670 1.67918 1.71286 -0.09103 -0.02488 0.33524  203 THR A O   
1525 C CB  . THR A 203 ? 0.99608 1.45131 1.38145 -0.08444 -0.01563 0.21646  203 THR A CB  
1526 O OG1 . THR A 203 ? 1.07217 1.50293 1.44446 -0.13604 -0.05205 0.18384  203 THR A OG1 
1527 C CG2 . THR A 203 ? 1.11949 1.56679 1.46346 -0.08195 -0.00808 0.20149  203 THR A CG2 
1528 N N   . ASN A 204 ? 0.87656 1.37288 1.35329 0.00312  0.04234  0.30886  204 ASN A N   
1529 C CA  . ASN A 204 ? 0.79441 1.28551 1.28598 0.03174  0.06058  0.31694  204 ASN A CA  
1530 C C   . ASN A 204 ? 0.93469 1.38420 1.34245 0.06182  0.07690  0.25299  204 ASN A C   
1531 O O   . ASN A 204 ? 0.99598 1.42495 1.34314 0.07270  0.08484  0.21805  204 ASN A O   
1532 C CB  . ASN A 204 ? 0.75795 1.28655 1.30768 0.08010  0.09707  0.39574  204 ASN A CB  
1533 C CG  . ASN A 204 ? 0.94591 1.46514 1.45073 0.13061  0.13604  0.40721  204 ASN A CG  
1534 O OD1 . ASN A 204 ? 1.07619 1.55685 1.50811 0.17510  0.16517  0.37643  204 ASN A OD1 
1535 N ND2 . ASN A 204 ? 0.87858 1.42937 1.42182 0.12346  0.13687  0.45270  204 ASN A ND2 
1536 N N   . PHE A 205 ? 1.29959 1.10717 1.37879 -0.28674 -0.25013 -0.04991 205 PHE A N   
1537 C CA  . PHE A 205 ? 1.29709 1.05759 1.31034 -0.26430 -0.23198 -0.02578 205 PHE A CA  
1538 C C   . PHE A 205 ? 1.28611 1.10366 1.28546 -0.26481 -0.18158 0.00845  205 PHE A C   
1539 O O   . PHE A 205 ? 1.28205 1.10394 1.23340 -0.22592 -0.16559 0.01115  205 PHE A O   
1540 C CB  . PHE A 205 ? 1.35898 1.02838 1.37192 -0.29632 -0.24688 -0.00613 205 PHE A CB  
1541 C CG  . PHE A 205 ? 1.39748 1.03254 1.35461 -0.28631 -0.21956 0.02890  205 PHE A CG  
1542 C CD1 . PHE A 205 ? 1.40563 1.00172 1.29904 -0.23707 -0.23042 0.01495  205 PHE A CD1 
1543 C CD2 . PHE A 205 ? 1.36070 1.00957 1.32895 -0.32156 -0.18299 0.07453  205 PHE A CD2 
1544 C CE1 . PHE A 205 ? 1.47260 1.04318 1.31950 -0.22559 -0.20844 0.04208  205 PHE A CE1 
1545 C CE2 . PHE A 205 ? 1.52970 1.15120 1.44405 -0.30571 -0.16140 0.10184  205 PHE A CE2 
1546 C CZ  . PHE A 205 ? 1.61766 1.19953 1.47362 -0.25881 -0.17559 0.08378  205 PHE A CZ  
1547 N N   . ASN A 206 ? 1.11757 0.98475 1.16390 -0.30659 -0.15750 0.03221  206 ASN A N   
1548 C CA  . ASN A 206 ? 1.05958 0.98369 1.09401 -0.30400 -0.11404 0.06021  206 ASN A CA  
1549 C C   . ASN A 206 ? 1.03728 1.02220 1.05869 -0.26246 -0.10434 0.03902  206 ASN A C   
1550 O O   . ASN A 206 ? 1.05288 1.05528 1.04410 -0.23895 -0.07915 0.05103  206 ASN A O   
1551 C CB  . ASN A 206 ? 1.06234 1.03622 1.15108 -0.35219 -0.09195 0.08748  206 ASN A CB  
1552 C CG  . ASN A 206 ? 1.13869 1.05181 1.25001 -0.39658 -0.09823 0.11474  206 ASN A CG  
1553 O OD1 . ASN A 206 ? 1.34027 1.23505 1.50515 -0.42707 -0.12492 0.10137  206 ASN A OD1 
1554 N ND2 . ASN A 206 ? 1.25044 1.12990 1.32303 -0.39866 -0.07505 0.15266  206 ASN A ND2 
1555 N N   . GLN A 207 ? 0.98889 1.00394 1.03387 -0.25036 -0.12566 0.00665  207 GLN A N   
1556 C CA  . GLN A 207 ? 0.97819 1.04519 1.00669 -0.20671 -0.11520 -0.00938 207 GLN A CA  
1557 C C   . GLN A 207 ? 1.01616 1.04391 0.99019 -0.15931 -0.11668 -0.01469 207 GLN A C   
1558 O O   . GLN A 207 ? 1.04534 1.10050 1.00139 -0.13254 -0.09044 -0.00507 207 GLN A O   
1559 C CB  . GLN A 207 ? 0.98001 1.08665 1.03899 -0.19720 -0.14027 -0.04403 207 GLN A CB  
1560 C CG  . GLN A 207 ? 1.08788 1.24539 1.12483 -0.14787 -0.12727 -0.05600 207 GLN A CG  
1561 C CD  . GLN A 207 ? 1.34362 1.52329 1.38803 -0.11870 -0.15997 -0.09606 207 GLN A CD  
1562 O OE1 . GLN A 207 ? 1.48187 1.65141 1.56305 -0.14237 -0.19408 -0.11949 207 GLN A OE1 
1563 N NE2 . GLN A 207 ? 1.19457 1.40356 1.20589 -0.06481 -0.15073 -0.10438 207 GLN A NE2 
1564 N N   . ILE A 208 ? 1.05877 1.02402 1.01069 -0.14734 -0.14797 -0.03079 208 ILE A N   
1565 C CA  . ILE A 208 ? 1.10934 1.04165 1.01078 -0.10147 -0.14826 -0.03397 208 ILE A CA  
1566 C C   . ILE A 208 ? 0.96824 0.89224 0.85294 -0.10598 -0.11732 -0.00419 208 ILE A C   
1567 O O   . ILE A 208 ? 1.01095 0.95706 0.88015 -0.07385 -0.09594 0.00114  208 ILE A O   
1568 C CB  . ILE A 208 ? 1.09343 0.95506 0.97226 -0.09059 -0.18937 -0.05551 208 ILE A CB  
1569 C CG1 . ILE A 208 ? 1.08021 0.95660 0.96277 -0.06087 -0.22304 -0.09471 208 ILE A CG1 
1570 C CG2 . ILE A 208 ? 1.06666 0.89001 0.89508 -0.05361 -0.18520 -0.04998 208 ILE A CG2 
1571 C CD1 . ILE A 208 ? 1.26149 1.06818 1.12110 -0.04413 -0.26852 -0.12179 208 ILE A CD1 
1572 N N   . LEU A 209 ? 0.97884 0.87103 0.86917 -0.14420 -0.11511 0.01570  209 LEU A N   
1573 C CA  . LEU A 209 ? 1.02778 0.91048 0.89760 -0.14297 -0.09156 0.03907  209 LEU A CA  
1574 C C   . LEU A 209 ? 0.89659 0.84713 0.78473 -0.13861 -0.05871 0.04914  209 LEU A C   
1575 O O   . LEU A 209 ? 1.00390 0.96149 0.87952 -0.11429 -0.04317 0.05279  209 LEU A O   
1576 C CB  . LEU A 209 ? 1.09074 0.92983 0.95895 -0.18065 -0.09414 0.06147  209 LEU A CB  
1577 C CG  . LEU A 209 ? 1.12125 0.94092 0.95836 -0.17361 -0.07715 0.08243  209 LEU A CG  
1578 C CD1 . LEU A 209 ? 1.15745 0.89979 0.97101 -0.19090 -0.09410 0.09656  209 LEU A CD1 
1579 C CD2 . LEU A 209 ? 1.37626 1.25573 1.23283 -0.18927 -0.04635 0.10239  209 LEU A CD2 
1580 N N   . MET A 210 ? 0.89872 0.90027 0.82131 -0.16183 -0.04969 0.05188  210 MET A N   
1581 C CA  . MET A 210 ? 0.92126 0.98518 0.86018 -0.15488 -0.02236 0.05824  210 MET A CA  
1582 C C   . MET A 210 ? 0.78791 0.87243 0.72317 -0.11420 -0.01577 0.04512  210 MET A C   
1583 O O   . MET A 210 ? 0.75404 0.85873 0.69314 -0.09831 0.00426  0.05125  210 MET A O   
1584 C CB  . MET A 210 ? 0.81543 0.93397 0.79112 -0.18356 -0.01646 0.06110  210 MET A CB  
1585 C CG  . MET A 210 ? 0.95725 1.14080 0.94746 -0.17057 0.00743  0.06270  210 MET A CG  
1586 S SD  . MET A 210 ? 0.99509 1.19669 0.97940 -0.18043 0.03057  0.08564  210 MET A SD  
1587 C CE  . MET A 210 ? 1.19527 1.40269 1.19741 -0.22808 0.03043  0.10722  210 MET A CE  
1588 N N   . GLN A 211 ? 0.80264 0.88307 0.73268 -0.09471 -0.03246 0.02746  211 GLN A N   
1589 C CA  . GLN A 211 ? 0.82762 0.92751 0.74998 -0.05170 -0.02138 0.02230  211 GLN A CA  
1590 C C   . GLN A 211 ? 0.93685 1.00447 0.83963 -0.02758 -0.01371 0.02966  211 GLN A C   
1591 O O   . GLN A 211 ? 0.85468 0.94377 0.76905 -0.00677 0.00944  0.03859  211 GLN A O   
1592 C CB  . GLN A 211 ? 0.80438 0.91027 0.71692 -0.02727 -0.04199 0.00122  211 GLN A CB  
1593 C CG  . GLN A 211 ? 0.97509 1.13631 0.91189 -0.03104 -0.04031 -0.00781 211 GLN A CG  
1594 C CD  . GLN A 211 ? 1.09505 1.29689 1.03629 -0.00314 -0.01058 0.00334  211 GLN A CD  
1595 O OE1 . GLN A 211 ? 0.85771 1.04809 0.79585 0.01003  0.01103  0.02007  211 GLN A OE1 
1596 N NE2 . GLN A 211 ? 1.18692 1.43577 1.14005 0.00607  -0.01086 -0.00698 211 GLN A NE2 
1597 N N   . LEU A 212 ? 0.99837 1.01464 0.87623 -0.02962 -0.03363 0.02555  212 LEU A N   
1598 C CA  . LEU A 212 ? 0.93567 0.92649 0.79742 -0.00732 -0.02780 0.03069  212 LEU A CA  
1599 C C   . LEU A 212 ? 0.92774 0.93708 0.81201 -0.01742 -0.00481 0.04392  212 LEU A C   
1600 O O   . LEU A 212 ? 1.04482 1.07231 0.94611 0.00518  0.01354  0.04839  212 LEU A O   
1601 C CB  . LEU A 212 ? 0.96571 0.89578 0.79597 -0.01344 -0.05475 0.02443  212 LEU A CB  
1602 C CG  . LEU A 212 ? 1.20141 1.10486 1.00056 0.02369  -0.07596 0.00806  212 LEU A CG  
1603 C CD1 . LEU A 212 ? 1.16437 1.00061 0.93327 0.01510  -0.10472 0.00164  212 LEU A CD1 
1604 C CD2 . LEU A 212 ? 1.10782 1.03742 0.90585 0.06602  -0.05407 0.01381  212 LEU A CD2 
1605 N N   . ARG A 213 ? 1.01556 1.02296 0.90380 -0.04976 -0.00577 0.05023  213 ARG A N   
1606 C CA  . ARG A 213 ? 0.81796 0.84053 0.72042 -0.05291 0.00928  0.05700  213 ARG A CA  
1607 C C   . ARG A 213 ? 0.73985 0.81355 0.67931 -0.04469 0.03019  0.05724  213 ARG A C   
1608 O O   . ARG A 213 ? 0.78286 0.86626 0.74466 -0.03006 0.04103  0.05595  213 ARG A O   
1609 C CB  . ARG A 213 ? 0.77998 0.79213 0.66968 -0.08205 0.00497  0.06666  213 ARG A CB  
1610 C CG  . ARG A 213 ? 1.02553 0.97616 0.87870 -0.08754 -0.01462 0.06984  213 ARG A CG  
1611 C CD  . ARG A 213 ? 1.11022 1.04710 0.94791 -0.11201 -0.01316 0.08752  213 ARG A CD  
1612 N NE  . ARG A 213 ? 1.08977 0.95928 0.88950 -0.11130 -0.03113 0.09233  213 ARG A NE  
1613 C CZ  . ARG A 213 ? 1.04941 0.88606 0.82896 -0.13329 -0.03329 0.11305  213 ARG A CZ  
1614 N NH1 . ARG A 213 ? 1.33161 1.20349 1.12611 -0.15785 -0.01616 0.13267  213 ARG A NH1 
1615 N NH2 . ARG A 213 ? 1.19758 0.96503 0.94041 -0.12807 -0.05152 0.11650  213 ARG A NH2 
1616 N N   . MET A 214 ? 0.83661 0.94222 0.78701 -0.05201 0.03409  0.05684  214 MET A N   
1617 C CA  . MET A 214 ? 0.81630 0.96501 0.79802 -0.04157 0.05240  0.05724  214 MET A CA  
1618 C C   . MET A 214 ? 0.79638 0.94556 0.79192 -0.00993 0.06503  0.05985  214 MET A C   
1619 O O   . MET A 214 ? 0.73097 0.89786 0.75989 0.00053  0.08118  0.06312  214 MET A O   
1620 C CB  . MET A 214 ? 0.79014 0.97653 0.77762 -0.05434 0.05238  0.05508  214 MET A CB  
1621 C CG  . MET A 214 ? 0.82133 1.02662 0.80969 -0.08402 0.05071  0.05895  214 MET A CG  
1622 S SD  . MET A 214 ? 0.66870 0.88529 0.66627 -0.07909 0.06080  0.06044  214 MET A SD  
1623 C CE  . MET A 214 ? 0.76640 0.94264 0.73042 -0.09813 0.05006  0.07084  214 MET A CE  
1624 N N   . SER A 215 ? 0.82459 0.95416 0.79685 0.00770  0.05814  0.05943  215 SER A N   
1625 C CA  . SER A 215 ? 0.77483 0.90878 0.75642 0.04234  0.07497  0.06840  215 SER A CA  
1626 C C   . SER A 215 ? 0.92259 1.04300 0.92700 0.04872  0.08398  0.07360  215 SER A C   
1627 O O   . SER A 215 ? 0.74996 0.88644 0.79558 0.06185  0.10616  0.08451  215 SER A O   
1628 C CB  . SER A 215 ? 0.81019 0.93216 0.75345 0.06644  0.06236  0.06366  215 SER A CB  
1629 O OG  . SER A 215 ? 1.23306 1.35944 1.17813 0.10446  0.08079  0.07672  215 SER A OG  
1630 N N   . LYS A 216 ? 0.93913 1.02924 0.92107 0.04037  0.06618  0.06572  216 LYS A N   
1631 C CA  . LYS A 216 ? 0.71694 0.79945 0.72240 0.04587  0.07020  0.06503  216 LYS A CA  
1632 C C   . LYS A 216 ? 0.79973 0.90331 0.85260 0.03286  0.07930  0.06204  216 LYS A C   
1633 O O   . LYS A 216 ? 0.86544 0.98027 0.96707 0.04293  0.09176  0.06333  216 LYS A O   
1634 C CB  . LYS A 216 ? 0.74401 0.78844 0.70969 0.03910  0.04609  0.05509  216 LYS A CB  
1635 C CG  . LYS A 216 ? 0.78549 0.82180 0.76153 0.05968  0.04661  0.05218  216 LYS A CG  
1636 C CD  . LYS A 216 ? 1.13012 1.18363 1.11678 0.09127  0.06384  0.06318  216 LYS A CD  
1637 C CE  . LYS A 216 ? 1.16196 1.23430 1.19640 0.10814  0.07878  0.06635  216 LYS A CE  
1638 N NZ  . LYS A 216 ? 0.87404 0.97486 0.93086 0.13874  0.10636  0.08668  216 LYS A NZ  
1639 N N   . ALA A 217 ? 0.71258 0.82463 0.75619 0.01189  0.07221  0.05674  217 ALA A N   
1640 C CA  . ALA A 217 ? 0.65501 0.78864 0.73640 0.00576  0.07591  0.04889  217 ALA A CA  
1641 C C   . ALA A 217 ? 0.74192 0.89859 0.87313 0.01688  0.09557  0.05503  217 ALA A C   
1642 O O   . ALA A 217 ? 0.87762 1.04188 1.06082 0.02123  0.09968  0.04802  217 ALA A O   
1643 C CB  . ALA A 217 ? 0.77194 0.91705 0.82678 -0.01364 0.06688  0.04520  217 ALA A CB  
1644 N N   . ALA A 218 ? 0.77964 0.94606 0.89786 0.02321  0.10602  0.06681  218 ALA A N   
1645 C CA  . ALA A 218 ? 0.77477 0.95683 0.93422 0.03789  0.12697  0.07782  218 ALA A CA  
1646 C C   . ALA A 218 ? 0.97505 1.14908 1.17938 0.05374  0.14459  0.09106  218 ALA A C   
1647 O O   . ALA A 218 ? 0.95856 1.13767 1.22490 0.05566  0.15663  0.09389  218 ALA A O   
1648 C CB  . ALA A 218 ? 0.59299 0.78697 0.72016 0.04949  0.13357  0.08781  218 ALA A CB  
1649 N N   . LEU A 219 ? 1.06991 1.23276 1.24826 0.06593  0.14589  0.09909  219 LEU A N   
1650 C CA  . LEU A 219 ? 0.89107 1.05566 1.11421 0.08218  0.16560  0.11438  219 LEU A CA  
1651 C C   . LEU A 219 ? 0.89834 1.06303 1.18152 0.06854  0.15826  0.09850  219 LEU A C   
1652 O O   . LEU A 219 ? 0.89761 1.07186 1.25600 0.07037  0.17590  0.10721  219 LEU A O   
1653 C CB  . LEU A 219 ? 0.81002 0.96676 0.98660 0.10182  0.16330  0.12035  219 LEU A CB  
1654 C CG  . LEU A 219 ? 0.89666 1.05578 1.01626 0.12554  0.16698  0.13140  219 LEU A CG  
1655 C CD1 . LEU A 219 ? 0.91223 1.05858 0.98103 0.14558  0.15329  0.12633  219 LEU A CD1 
1656 C CD2 . LEU A 219 ? 0.77418 0.95322 0.92432 0.15153  0.20270  0.16211  219 LEU A CD2 
1657 N N   . LEU A 220 ? 0.84142 0.99478 1.09503 0.05655  0.13136  0.07486  220 LEU A N   
1658 C CA  . LEU A 220 ? 0.95283 1.10944 1.25635 0.05043  0.11890  0.05353  220 LEU A CA  
1659 C C   . LEU A 220 ? 0.96870 1.13745 1.33140 0.04224  0.11881  0.04231  220 LEU A C   
1660 O O   . LEU A 220 ? 0.99888 1.17574 1.43816 0.04237  0.11795  0.03050  220 LEU A O   
1661 C CB  . LEU A 220 ? 0.76662 0.90709 1.01315 0.04438  0.09028  0.03265  220 LEU A CB  
1662 C CG  . LEU A 220 ? 0.70982 0.83107 0.90830 0.05512  0.08378  0.03682  220 LEU A CG  
1663 C CD1 . LEU A 220 ? 0.78987 0.88503 0.92029 0.04698  0.05818  0.02443  220 LEU A CD1 
1664 C CD2 . LEU A 220 ? 0.77096 0.90431 1.02348 0.06891  0.08795  0.03163  220 LEU A CD2 
1665 N N   . LEU A 221 ? 1.07196 1.24359 1.40349 0.03621  0.11659  0.04234  221 LEU A N   
1666 C CA  . LEU A 221 ? 1.05670 1.23872 1.43628 0.03373  0.11414  0.02995  221 LEU A CA  
1667 C C   . LEU A 221 ? 0.96310 1.14443 1.42033 0.03983  0.13867  0.04850  221 LEU A C   
1668 O O   . LEU A 221 ? 1.08010 1.26226 1.61478 0.03772  0.13320  0.03315  221 LEU A O   
1669 C CB  . LEU A 221 ? 0.88365 1.07500 1.21049 0.02997  0.11089  0.03064  221 LEU A CB  
1670 C CG  . LEU A 221 ? 0.89643 1.10062 1.25860 0.03253  0.10429  0.01425  221 LEU A CG  
1671 C CD1 . LEU A 221 ? 0.90109 1.11264 1.27450 0.03343  0.07747  -0.01948 221 LEU A CD1 
1672 C CD2 . LEU A 221 ? 0.93028 1.15086 1.24166 0.03187  0.10692  0.02056  221 LEU A CD2 
1673 N N   . LEU A 222 ? 0.96058 1.13969 1.39982 0.04966  0.16539  0.08190  222 LEU A N   
1674 C CA  . LEU A 222 ? 0.93232 1.10915 1.44209 0.05805  0.19515  0.10909  222 LEU A CA  
1675 C C   . LEU A 222 ? 0.96031 1.14079 1.54667 0.05624  0.20543  0.11441  222 LEU A C   
1676 O O   . LEU A 222 ? 0.86791 1.04639 1.54061 0.05558  0.22653  0.13195  222 LEU A O   
1677 C CB  . LEU A 222 ? 0.87865 1.05639 1.34093 0.07776  0.22251  0.14538  222 LEU A CB  
1678 C CG  . LEU A 222 ? 1.04190 1.22088 1.46036 0.08376  0.22042  0.14561  222 LEU A CG  
1679 C CD1 . LEU A 222 ? 0.99550 1.17719 1.37787 0.11145  0.24855  0.18123  222 LEU A CD1 
1680 C CD2 . LEU A 222 ? 0.83831 1.01026 1.31811 0.07764  0.21683  0.13503  222 LEU A CD2 
1681 N N   . GLU A 223 ? 1.08700 1.27302 1.64881 0.05535  0.19103  0.10016  223 GLU A N   
1682 C CA  . GLU A 223 ? 0.98712 1.18530 1.62625 0.05485  0.19850  0.10082  223 GLU A CA  
1683 C C   . GLU A 223 ? 0.99740 1.19831 1.73464 0.04063  0.18022  0.06992  223 GLU A C   
1684 O O   . GLU A 223 ? 1.16272 1.37727 1.99414 0.03698  0.19088  0.07336  223 GLU A O   
1685 C CB  . GLU A 223 ? 0.98021 1.18239 1.56480 0.06111  0.18158  0.08663  223 GLU A CB  
1686 C CG  . GLU A 223 ? 1.08103 1.28225 1.59052 0.07999  0.19852  0.11463  223 GLU A CG  
1687 C CD  . GLU A 223 ? 1.27281 1.47804 1.75354 0.09037  0.18584  0.10354  223 GLU A CD  
1688 O OE1 . GLU A 223 ? 1.29593 1.50789 1.82041 0.08305  0.16699  0.07646  223 GLU A OE1 
1689 O OE2 . GLU A 223 ? 1.40796 1.60960 1.82093 0.10957  0.19158  0.11853  223 GLU A OE2 
1690 N N   . ASN A 224 ? 1.00653 1.19902 1.72722 0.03481  0.15155  0.03779  224 ASN A N   
1691 C CA  . ASN A 224 ? 0.87233 1.06674 1.67943 0.02808  0.12653  0.00017  224 ASN A CA  
1692 C C   . ASN A 224 ? 0.99124 1.20207 1.84369 0.02843  0.10460  -0.03123 224 ASN A C   
1693 O O   . ASN A 224 ? 0.89148 1.10932 1.84615 0.02377  0.08821  -0.05975 224 ASN A O   
1694 C CB  . ASN A 224 ? 0.79068 0.97567 1.70346 0.02142  0.14897  0.02000  224 ASN A CB  
1695 C CG  . ASN A 224 ? 0.94231 1.11975 1.92643 0.01763  0.11661  -0.02305 224 ASN A CG  
1696 O OD1 . ASN A 224 ? 0.84540 1.02757 1.78010 0.02522  0.08055  -0.06392 224 ASN A OD1 
1697 N ND2 . ASN A 224 ? 0.93390 1.09956 2.03711 0.00820  0.12917  -0.01357 224 ASN A ND2 
1698 N N   . SER A 225 ? 1.04728 1.26367 1.82832 0.03583  0.10118  -0.02933 225 SER A N   
1699 C CA  . SER A 225 ? 1.01473 1.24783 1.82558 0.04171  0.07986  -0.05883 225 SER A CA  
1700 C C   . SER A 225 ? 1.09504 1.32176 1.81265 0.05311  0.04427  -0.09139 225 SER A C   
1701 O O   . SER A 225 ? 1.15234 1.38977 1.87265 0.06411  0.02396  -0.11645 225 SER A O   
1702 C CB  . SER A 225 ? 0.91480 1.16077 1.72707 0.04719  0.10637  -0.02845 225 SER A CB  
1703 O OG  . SER A 225 ? 0.88118 1.14065 1.78968 0.04008  0.14310  0.00519  225 SER A OG  
1704 N N   . TYR A 226 ? 0.97207 1.18416 1.60927 0.05264  0.03753  -0.09003 226 TYR A N   
1705 C CA  . TYR A 226 ? 0.93390 1.13831 1.47396 0.06272  0.01316  -0.10688 226 TYR A CA  
1706 C C   . TYR A 226 ? 0.91192 1.11878 1.42202 0.06525  -0.00224 -0.12345 226 TYR A C   
1707 O O   . TYR A 226 ? 0.81731 1.02327 1.33563 0.05638  0.01250  -0.10808 226 TYR A O   
1708 C CB  . TYR A 226 ? 0.84505 1.02954 1.29004 0.05976  0.02807  -0.07411 226 TYR A CB  
1709 C CG  . TYR A 226 ? 0.83386 1.01912 1.29398 0.06627  0.03780  -0.06333 226 TYR A CG  
1710 C CD1 . TYR A 226 ? 0.85831 1.04566 1.30949 0.08094  0.01530  -0.08798 226 TYR A CD1 
1711 C CD2 . TYR A 226 ? 0.70601 0.89462 1.18932 0.06349  0.06948  -0.02939 226 TYR A CD2 
1712 C CE1 . TYR A 226 ? 0.66261 0.85658 1.12878 0.09055  0.02318  -0.08051 226 TYR A CE1 
1713 C CE2 . TYR A 226 ? 0.76178 0.95917 1.25831 0.07486  0.07960  -0.01938 226 TYR A CE2 
1714 C CZ  . TYR A 226 ? 0.78066 0.98164 1.27044 0.08732  0.05591  -0.04594 226 TYR A CZ  
1715 O OH  . TYR A 226 ? 0.75692 0.97191 1.25928 0.10212  0.06494  -0.03806 226 TYR A OH  
1716 N N   . GLN A 227 ? 0.97322 1.18556 1.44137 0.08215  -0.03110 -0.15340 227 GLN A N   
1717 C CA  . GLN A 227 ? 0.73606 0.95868 1.16546 0.09188  -0.04558 -0.16885 227 GLN A CA  
1718 C C   . GLN A 227 ? 0.69831 0.91063 1.03093 0.08038  -0.02821 -0.13380 227 GLN A C   
1719 O O   . GLN A 227 ? 0.84449 1.03669 1.13230 0.06952  -0.01473 -0.10677 227 GLN A O   
1720 C CB  . GLN A 227 ? 0.74013 0.97600 1.15015 0.12131  -0.08045 -0.20989 227 GLN A CB  
1721 C CG  . GLN A 227 ? 0.89252 1.14466 1.40649 0.13553  -0.10646 -0.25580 227 GLN A CG  
1722 C CD  . GLN A 227 ? 1.20214 1.46270 1.80399 0.13087  -0.11068 -0.27314 227 GLN A CD  
1723 O OE1 . GLN A 227 ? 1.39902 1.66029 1.96880 0.12884  -0.10303 -0.26215 227 GLN A OE1 
1724 N NE2 . GLN A 227 ? 1.18896 1.45609 1.90749 0.12948  -0.12402 -0.30129 227 GLN A NE2 
1725 N N   . ILE A 228 ? 0.86785 1.09648 1.17313 0.08390  -0.03036 -0.13659 228 ILE A N   
1726 C CA  . ILE A 228 ? 0.85882 1.08606 1.08503 0.07063  -0.01446 -0.10516 228 ILE A CA  
1727 C C   . ILE A 228 ? 0.76975 0.98498 0.91885 0.07650  -0.02203 -0.09803 228 ILE A C   
1728 O O   . ILE A 228 ? 0.78295 0.97993 0.87855 0.05861  -0.00851 -0.06737 228 ILE A O   
1729 C CB  . ILE A 228 ? 0.84594 1.10313 1.06571 0.07637  -0.01470 -0.11121 228 ILE A CB  
1730 C CG1 . ILE A 228 ? 0.88382 1.14215 1.16862 0.06854  -0.00306 -0.10900 228 ILE A CG1 
1731 C CG2 . ILE A 228 ? 0.93160 1.19750 1.07620 0.06305  -0.00026 -0.08162 228 ILE A CG2 
1732 C CD1 . ILE A 228 ? 0.97395 1.21571 1.24779 0.04629  0.02367  -0.07213 228 ILE A CD1 
1733 N N   . SER A 229 ? 0.85125 1.07447 0.99436 0.10395  -0.04552 -0.12717 229 SER A N   
1734 C CA  . SER A 229 ? 0.79572 1.00071 0.86562 0.11490  -0.05245 -0.11870 229 SER A CA  
1735 C C   . SER A 229 ? 0.86959 1.03807 0.93848 0.10301  -0.04809 -0.10529 229 SER A C   
1736 O O   . SER A 229 ? 0.91009 1.04850 0.91332 0.09450  -0.04216 -0.07908 229 SER A O   
1737 C CB  . SER A 229 ? 0.84602 1.07028 0.91152 0.15562  -0.08113 -0.15754 229 SER A CB  
1738 O OG  . SER A 229 ? 0.94598 1.17909 1.09920 0.16593  -0.09946 -0.19596 229 SER A OG  
1739 N N   . GLN A 230 ? 0.94541 1.11663 1.09020 0.10314  -0.05076 -0.12222 230 GLN A N   
1740 C CA  . GLN A 230 ? 0.75630 0.90228 0.90415 0.09670  -0.04475 -0.10992 230 GLN A CA  
1741 C C   . GLN A 230 ? 0.76040 0.88535 0.87684 0.07126  -0.02143 -0.07211 230 GLN A C   
1742 O O   . GLN A 230 ? 0.74082 0.83403 0.80282 0.06838  -0.02139 -0.05548 230 GLN A O   
1743 C CB  . GLN A 230 ? 0.77600 0.93989 1.02300 0.10057  -0.04622 -0.13050 230 GLN A CB  
1744 C CG  . GLN A 230 ? 0.77543 0.96372 1.07309 0.12560  -0.07482 -0.17636 230 GLN A CG  
1745 C CD  . GLN A 230 ? 0.82260 1.02837 1.22883 0.12394  -0.07460 -0.19294 230 GLN A CD  
1746 O OE1 . GLN A 230 ? 0.78081 1.00431 1.27567 0.11569  -0.07190 -0.20427 230 GLN A OE1 
1747 N NE2 . GLN A 230 ? 0.83575 1.03697 1.23904 0.13233  -0.07713 -0.19349 230 GLN A NE2 
1748 N N   . ILE A 231 ? 0.84977 0.99081 1.00021 0.05612  -0.00454 -0.06128 231 ILE A N   
1749 C CA  . ILE A 231 ? 0.74108 0.86885 0.86262 0.03695  0.01419  -0.03078 231 ILE A CA  
1750 C C   . ILE A 231 ? 0.82556 0.93317 0.86754 0.02665  0.01012  -0.01476 231 ILE A C   
1751 O O   . ILE A 231 ? 0.87689 0.95398 0.88068 0.01843  0.01132  0.00171  231 ILE A O   
1752 C CB  . ILE A 231 ? 0.64854 0.80087 0.81119 0.02851  0.02952  -0.02545 231 ILE A CB  
1753 C CG1 . ILE A 231 ? 0.76458 0.92601 1.00962 0.03462  0.03964  -0.02998 231 ILE A CG1 
1754 C CG2 . ILE A 231 ? 0.73813 0.88402 0.86050 0.01269  0.04325  0.00023  231 ILE A CG2 
1755 C CD1 . ILE A 231 ? 0.86969 1.05182 1.16910 0.03445  0.04466  -0.03759 231 ILE A CD1 
1756 N N   . SER A 232 ? 0.77666 0.90177 0.79574 0.02872  0.00497  -0.01918 232 SER A N   
1757 C CA  . SER A 232 ? 0.78432 0.89576 0.73747 0.01680  0.00616  0.00199  232 SER A CA  
1758 C C   . SER A 232 ? 0.80023 0.86525 0.70508 0.02171  -0.00468 0.00916  232 SER A C   
1759 O O   . SER A 232 ? 0.98844 1.02050 0.85817 0.00343  -0.00214 0.03077  232 SER A O   
1760 C CB  . SER A 232 ? 0.91691 1.06228 0.85386 0.02872  0.00391  -0.00410 232 SER A CB  
1761 O OG  . SER A 232 ? 1.19072 1.32773 1.10034 0.05611  -0.01223 -0.01857 232 SER A OG  
1762 N N   . ASN A 233 ? 0.87268 0.93342 0.77650 0.04846  -0.01998 -0.01170 233 ASN A N   
1763 C CA  . ASN A 233 ? 0.99109 1.00602 0.84365 0.05886  -0.03213 -0.00635 233 ASN A CA  
1764 C C   . ASN A 233 ? 1.07956 1.06383 0.93943 0.05118  -0.03192 -0.00118 233 ASN A C   
1765 O O   . ASN A 233 ? 1.05515 0.99188 0.86442 0.05119  -0.04029 0.01080  233 ASN A O   
1766 C CB  . ASN A 233 ? 0.88552 0.90935 0.73961 0.09467  -0.05113 -0.03541 233 ASN A CB  
1767 C CG  . ASN A 233 ? 1.11818 1.09743 0.89741 0.11138  -0.06307 -0.02541 233 ASN A CG  
1768 O OD1 . ASN A 233 ? 1.24126 1.18665 1.00803 0.11920  -0.07280 -0.02858 233 ASN A OD1 
1769 N ND2 . ASN A 233 ? 1.31906 1.29823 1.04495 0.12032  -0.06118 -0.01096 233 ASN A ND2 
1770 N N   . MET A 234 ? 0.85986 0.86964 0.78047 0.04881  -0.02268 -0.00947 234 MET A N   
1771 C CA  . MET A 234 ? 0.77042 0.76112 0.69648 0.05026  -0.02023 -0.00434 234 MET A CA  
1772 C C   . MET A 234 ? 0.93759 0.90159 0.82630 0.02959  -0.01603 0.01746  234 MET A C   
1773 O O   . MET A 234 ? 1.09341 1.01542 0.94150 0.03323  -0.02725 0.02237  234 MET A O   
1774 C CB  . MET A 234 ? 0.74724 0.77690 0.75025 0.05539  -0.00596 -0.01242 234 MET A CB  
1775 C CG  . MET A 234 ? 0.71284 0.76422 0.76564 0.07572  -0.01465 -0.03763 234 MET A CG  
1776 S SD  . MET A 234 ? 0.92744 1.02465 1.08975 0.07443  0.00461  -0.04321 234 MET A SD  
1777 C CE  . MET A 234 ? 0.87399 0.96580 1.03953 0.08178  0.02279  -0.02141 234 MET A CE  
1778 N N   . ILE A 235 ? 1.09706 1.08527 1.00081 0.00971  -0.00327 0.02718  235 ILE A N   
1779 C CA  . ILE A 235 ? 1.09102 1.06118 0.97095 -0.00909 -0.00242 0.04207  235 ILE A CA  
1780 C C   . ILE A 235 ? 1.14754 1.07793 0.97643 -0.02610 -0.01369 0.05542  235 ILE A C   
1781 O O   . ILE A 235 ? 1.29990 1.20199 1.11025 -0.04109 -0.02086 0.06361  235 ILE A O   
1782 C CB  . ILE A 235 ? 1.01533 1.02762 0.92813 -0.02296 0.01342  0.04673  235 ILE A CB  
1783 C CG1 . ILE A 235 ? 1.04403 1.08792 0.96571 -0.03044 0.01901  0.04626  235 ILE A CG1 
1784 C CG2 . ILE A 235 ? 1.00089 1.03941 0.95938 -0.00657 0.02674  0.04176  235 ILE A CG2 
1785 C CD1 . ILE A 235 ? 1.02084 1.10942 0.97722 -0.03734 0.03309  0.04658  235 ILE A CD1 
1786 N N   . GLY A 236 ? 1.18005 1.10631 0.98730 -0.02197 -0.01618 0.05806  236 GLY A N   
1787 C CA  . GLY A 236 ? 1.24298 1.12928 1.00203 -0.03589 -0.02181 0.07829  236 GLY A CA  
1788 C C   . GLY A 236 ? 1.17967 1.09814 0.93629 -0.05255 -0.00710 0.09619  236 GLY A C   
1789 O O   . GLY A 236 ? 1.38066 1.27181 1.11057 -0.07404 -0.00499 0.12153  236 GLY A O   
1790 N N   . ILE A 237 ? 1.08182 1.05781 0.86878 -0.04279 0.00326  0.08466  237 ILE A N   
1791 C CA  . ILE A 237 ? 1.19354 1.21139 0.97754 -0.05131 0.01765  0.09891  237 ILE A CA  
1792 C C   . ILE A 237 ? 1.29884 1.32670 1.05337 -0.01943 0.01409  0.09300  237 ILE A C   
1793 O O   . ILE A 237 ? 1.16464 1.20089 0.93531 0.00904  0.00217  0.06394  237 ILE A O   
1794 C CB  . ILE A 237 ? 1.12895 1.20494 0.96215 -0.05682 0.02829  0.08718  237 ILE A CB  
1795 C CG1 . ILE A 237 ? 1.09903 1.16907 0.95163 -0.08466 0.03120  0.09492  237 ILE A CG1 
1796 C CG2 . ILE A 237 ? 1.10099 1.23022 0.93001 -0.05301 0.04069  0.09441  237 ILE A CG2 
1797 C CD1 . ILE A 237 ? 1.13496 1.26033 1.02809 -0.08868 0.04215  0.08690  237 ILE A CD1 
1798 N N   . SER A 238 ? 1.60250 1.63331 1.31708 -0.02231 0.02472  0.12076  238 SER A N   
1799 C CA  . SER A 238 ? 1.72553 1.76115 1.39554 0.01503  0.02101  0.11959  238 SER A CA  
1800 C C   . SER A 238 ? 1.69745 1.79705 1.39243 0.04637  0.01729  0.08769  238 SER A C   
1801 O O   . SER A 238 ? 1.67802 1.77908 1.37931 0.08031  -0.00191 0.05391  238 SER A O   
1802 C CB  . SER A 238 ? 1.75245 1.77924 1.37444 0.00428  0.03977  0.16571  238 SER A CB  
1803 O OG  . SER A 238 ? 1.63893 1.69920 1.29279 -0.03393 0.05946  0.18758  238 SER A OG  
1804 N N   . SER A 239 ? 1.43783 1.59198 1.14971 0.03755  0.03291  0.09532  239 SER A N   
1805 C CA  . SER A 239 ? 1.26439 1.47691 0.99651 0.07048  0.02638  0.06372  239 SER A CA  
1806 C C   . SER A 239 ? 1.17461 1.40465 0.97695 0.05887  0.02093  0.03515  239 SER A C   
1807 O O   . SER A 239 ? 1.23496 1.44523 1.06387 0.02564  0.02808  0.04577  239 SER A O   
1808 C CB  . SER A 239 ? 1.31139 1.57932 1.01738 0.07666  0.04605  0.08682  239 SER A CB  
1809 O OG  . SER A 239 ? 1.33793 1.66365 1.07488 0.10202  0.03853  0.05327  239 SER A OG  
1810 N N   . ALA A 240 ? 1.19755 1.46322 1.02958 0.09049  0.00662  -0.00224 240 ALA A N   
1811 C CA  . ALA A 240 ? 1.08132 1.36308 0.98168 0.08263  0.00353  -0.02580 240 ALA A CA  
1812 C C   . ALA A 240 ? 1.13133 1.46012 1.03986 0.07213  0.01901  -0.01548 240 ALA A C   
1813 O O   . ALA A 240 ? 1.26105 1.58950 1.20667 0.04839  0.02777  -0.01128 240 ALA A O   
1814 C CB  . ALA A 240 ? 1.14857 1.44217 1.08965 0.11836  -0.02183 -0.07264 240 ALA A CB  
1815 N N   . SER A 241 ? 1.17625 1.55012 1.04855 0.09453  0.02274  -0.01176 241 SER A N   
1816 C CA  . SER A 241 ? 1.16909 1.59607 1.04680 0.08693  0.03853  -0.00092 241 SER A CA  
1817 C C   . SER A 241 ? 1.16022 1.57781 1.03689 0.03981  0.06099  0.03777  241 SER A C   
1818 O O   . SER A 241 ? 1.15122 1.59241 1.05991 0.02277  0.06865  0.03775  241 SER A O   
1819 C CB  . SER A 241 ? 1.40846 1.88994 1.23888 0.12261  0.04232  0.00277  241 SER A CB  
1820 O OG  . SER A 241 ? 1.43830 1.90822 1.21318 0.11497  0.05902  0.04325  241 SER A OG  
1821 N N   . TYR A 242 ? 0.92040 1.30358 0.76065 0.02108  0.06942  0.06924  242 TYR A N   
1822 C CA  . TYR A 242 ? 0.94719 1.31058 0.79415 -0.02447 0.08352  0.10018  242 TYR A CA  
1823 C C   . TYR A 242 ? 1.01350 1.34802 0.90318 -0.04185 0.07525  0.08378  242 TYR A C   
1824 O O   . TYR A 242 ? 1.09370 1.44636 1.00723 -0.06598 0.08339  0.09113  242 TYR A O   
1825 C CB  . TYR A 242 ? 1.06134 1.37255 0.86675 -0.03714 0.08631  0.12981  242 TYR A CB  
1826 C CG  . TYR A 242 ? 1.10714 1.40398 0.92060 -0.08332 0.09982  0.16367  242 TYR A CG  
1827 C CD1 . TYR A 242 ? 1.25092 1.60679 1.08299 -0.10316 0.11924  0.18318  242 TYR A CD1 
1828 C CD2 . TYR A 242 ? 1.32531 1.55176 1.13255 -0.10564 0.09048  0.17290  242 TYR A CD2 
1829 C CE1 . TYR A 242 ? 1.39210 1.73757 1.24479 -0.14778 0.12835  0.21016  242 TYR A CE1 
1830 C CE2 . TYR A 242 ? 1.27468 1.48439 1.09690 -0.14745 0.09695  0.19818  242 TYR A CE2 
1831 C CZ  . TYR A 242 ? 1.34235 1.61182 1.19163 -0.17030 0.11549  0.21620  242 TYR A CZ  
1832 O OH  . TYR A 242 ? 1.70961 1.96504 1.58677 -0.21427 0.11874  0.23738  242 TYR A OH  
1833 N N   . PHE A 243 ? 0.94822 1.24095 0.84778 -0.02735 0.05978  0.06262  243 PHE A N   
1834 C CA  . PHE A 243 ? 0.79853 1.06791 0.73577 -0.03744 0.05624  0.05183  243 PHE A CA  
1835 C C   . PHE A 243 ? 0.83584 1.14782 0.81212 -0.03199 0.06129  0.03806  243 PHE A C   
1836 O O   . PHE A 243 ? 0.99633 1.30801 0.99099 -0.04701 0.06715  0.04313  243 PHE A O   
1837 C CB  . PHE A 243 ? 0.99597 1.22703 0.94625 -0.01917 0.04241  0.03239  243 PHE A CB  
1838 C CG  . PHE A 243 ? 0.91093 1.13320 0.90752 -0.02022 0.04406  0.02237  243 PHE A CG  
1839 C CD1 . PHE A 243 ? 0.72619 0.92378 0.71927 -0.03769 0.04896  0.03655  243 PHE A CD1 
1840 C CD2 . PHE A 243 ? 0.71491 0.95404 0.75939 -0.00128 0.04079  -0.00024 243 PHE A CD2 
1841 C CE1 . PHE A 243 ? 0.78303 0.97691 0.81125 -0.03203 0.05430  0.03226  243 PHE A CE1 
1842 C CE2 . PHE A 243 ? 0.61014 0.84040 0.69745 -0.00170 0.04779  -0.00124 243 PHE A CE2 
1843 C CZ  . PHE A 243 ? 0.75488 0.96472 0.83018 -0.01506 0.05655  0.01705  243 PHE A CZ  
1844 N N   . ILE A 244 ? 0.76526 1.11108 0.75334 -0.00531 0.05604  0.01742  244 ILE A N   
1845 C CA  . ILE A 244 ? 0.74501 1.12454 0.76925 0.00380  0.05825  0.00274  244 ILE A CA  
1846 C C   . ILE A 244 ? 0.84236 1.26407 0.85632 -0.01404 0.07252  0.02053  244 ILE A C   
1847 O O   . ILE A 244 ? 0.96567 1.39652 1.00327 -0.01955 0.07737  0.01913  244 ILE A O   
1848 C CB  . ILE A 244 ? 0.83980 1.24620 0.87732 0.03898  0.04448  -0.02721 244 ILE A CB  
1849 C CG1 . ILE A 244 ? 0.75692 1.12651 0.81795 0.05582  0.02664  -0.05039 244 ILE A CG1 
1850 C CG2 . ILE A 244 ? 0.66042 1.09130 0.73585 0.04960  0.04450  -0.04262 244 ILE A CG2 
1851 C CD1 . ILE A 244 ? 0.71503 1.10922 0.79899 0.09273  0.00589  -0.08836 244 ILE A CD1 
1852 N N   . ARG A 245 ? 0.95272 1.40328 0.93336 -0.02189 0.08057  0.03904  245 ARG A N   
1853 C CA  . ARG A 245 ? 0.96483 1.46351 0.94678 -0.04239 0.09508  0.05668  245 ARG A CA  
1854 C C   . ARG A 245 ? 1.03712 1.50669 1.03222 -0.07520 0.09703  0.06911  245 ARG A C   
1855 O O   . ARG A 245 ? 1.09037 1.59255 1.10637 -0.08341 0.10104  0.06682  245 ARG A O   
1856 C CB  . ARG A 245 ? 0.92556 1.45998 0.87547 -0.04701 0.10805  0.08160  245 ARG A CB  
1857 C CG  . ARG A 245 ? 1.08068 1.65414 1.00889 -0.00550 0.10503  0.06764  245 ARG A CG  
1858 C CD  . ARG A 245 ? 1.31641 1.94205 1.21265 -0.00621 0.12537  0.09912  245 ARG A CD  
1859 N NE  . ARG A 245 ? 1.30130 1.88404 1.17506 -0.03513 0.13552  0.13511  245 ARG A NE  
1860 C CZ  . ARG A 245 ? 1.26701 1.82950 1.09567 -0.01598 0.13706  0.14912  245 ARG A CZ  
1861 N NH1 . ARG A 245 ? 1.16510 1.74119 0.96787 0.03362  0.12391  0.12337  245 ARG A NH1 
1862 N NH2 . ARG A 245 ? 1.34019 1.86373 1.14982 -0.04459 0.14907  0.18738  245 ARG A NH2 
1863 N N   . ILE A 246 ? 0.77403 1.18362 0.75537 -0.08930 0.09116  0.07860  246 ILE A N   
1864 C CA  . ILE A 246 ? 0.82152 1.20259 0.81225 -0.11451 0.08784  0.08535  246 ILE A CA  
1865 C C   . ILE A 246 ? 0.78709 1.15967 0.80056 -0.09893 0.08328  0.06695  246 ILE A C   
1866 O O   . ILE A 246 ? 0.66250 1.04943 0.68888 -0.10764 0.08284  0.06543  246 ILE A O   
1867 C CB  . ILE A 246 ? 0.73528 1.05151 0.70160 -0.12785 0.07981  0.09773  246 ILE A CB  
1868 C CG1 . ILE A 246 ? 0.77331 1.09383 0.71543 -0.14344 0.08809  0.12358  246 ILE A CG1 
1869 C CG2 . ILE A 246 ? 0.83417 1.12086 0.80954 -0.14803 0.07080  0.09843  246 ILE A CG2 
1870 C CD1 . ILE A 246 ? 1.05346 1.30351 0.96799 -0.15376 0.07887  0.13651  246 ILE A CD1 
1871 N N   . PHE A 247 ? 0.71561 1.06559 0.73684 -0.07426 0.08003  0.05363  247 PHE A N   
1872 C CA  . PHE A 247 ? 0.69550 1.03745 0.74158 -0.05744 0.08153  0.04359  247 PHE A CA  
1873 C C   . PHE A 247 ? 0.70687 1.09908 0.76848 -0.04965 0.08766  0.03757  247 PHE A C   
1874 O O   . PHE A 247 ? 0.66851 1.06349 0.73713 -0.04479 0.09013  0.03744  247 PHE A O   
1875 C CB  . PHE A 247 ? 0.72875 1.04627 0.79496 -0.03601 0.07890  0.03197  247 PHE A CB  
1876 C CG  . PHE A 247 ? 0.68720 0.98731 0.78381 -0.02044 0.08539  0.03052  247 PHE A CG  
1877 C CD1 . PHE A 247 ? 0.63795 0.96105 0.76082 -0.00487 0.09183  0.02466  247 PHE A CD1 
1878 C CD2 . PHE A 247 ? 0.67113 0.93201 0.76964 -0.01788 0.08656  0.03727  247 PHE A CD2 
1879 C CE1 . PHE A 247 ? 0.55204 0.85551 0.70316 0.01088  0.10215  0.03043  247 PHE A CE1 
1880 C CE2 . PHE A 247 ? 0.66556 0.91511 0.79309 -0.00099 0.09822  0.04276  247 PHE A CE2 
1881 C CZ  . PHE A 247 ? 0.55617 0.82509 0.71046 0.01245  0.10743  0.04173  247 PHE A CZ  
1882 N N   . ASN A 248 ? 0.68545 1.12066 0.74789 -0.04308 0.08917  0.03147  248 ASN A N   
1883 C CA  . ASN A 248 ? 0.70919 1.19708 0.78309 -0.03304 0.09351  0.02416  248 ASN A CA  
1884 C C   . ASN A 248 ? 0.70569 1.22449 0.77590 -0.05570 0.09644  0.03350  248 ASN A C   
1885 O O   . ASN A 248 ? 0.66871 1.20317 0.74867 -0.04693 0.09655  0.02725  248 ASN A O   
1886 C CB  . ASN A 248 ? 0.70631 1.23986 0.77653 -0.01779 0.09299  0.01472  248 ASN A CB  
1887 C CG  . ASN A 248 ? 0.64725 1.21861 0.73397 0.00799  0.09242  -0.00196 248 ASN A CG  
1888 O OD1 . ASN A 248 ? 0.68697 1.24611 0.78754 0.01511  0.09408  -0.00408 248 ASN A OD1 
1889 N ND2 . ASN A 248 ? 0.73645 1.35566 0.81669 0.02649  0.09000  -0.01316 248 ASN A ND2 
1890 N N   . LYS A 249 ? 0.68261 1.20913 0.74184 -0.08392 0.09791  0.04838  249 LYS A N   
1891 C CA  . LYS A 249 ? 0.60254 1.16166 0.67301 -0.11044 0.09834  0.05523  249 LYS A CA  
1892 C C   . LYS A 249 ? 0.60181 1.12653 0.67670 -0.11229 0.08746  0.04803  249 LYS A C   
1893 O O   . LYS A 249 ? 0.83844 1.39924 0.92949 -0.11779 0.08296  0.04021  249 LYS A O   
1894 C CB  . LYS A 249 ? 0.75643 1.31340 0.82065 -0.14324 0.10279  0.07773  249 LYS A CB  
1895 C CG  . LYS A 249 ? 0.68494 1.26906 0.77558 -0.17770 0.10102  0.08506  249 LYS A CG  
1896 C CD  . LYS A 249 ? 0.96801 1.52236 1.05424 -0.21155 0.10453  0.11182  249 LYS A CD  
1897 C CE  . LYS A 249 ? 1.18289 1.77789 1.25468 -0.20794 0.12523  0.13392  249 LYS A CE  
1898 N NZ  . LYS A 249 ? 1.06693 1.63348 1.12926 -0.23674 0.13434  0.16812  249 LYS A NZ  
1899 N N   . HIS A 250 ? 0.84529 1.30610 0.90588 -0.10327 0.08213  0.04845  250 HIS A N   
1900 C CA  . HIS A 250 ? 0.65986 1.08786 0.71640 -0.09798 0.07165  0.04250  250 HIS A CA  
1901 C C   . HIS A 250 ? 0.66647 1.10504 0.72645 -0.06251 0.07632  0.03277  250 HIS A C   
1902 O O   . HIS A 250 ? 0.74735 1.21041 0.80971 -0.05343 0.07035  0.02314  250 HIS A O   
1903 C CB  . HIS A 250 ? 0.72737 1.08849 0.76491 -0.09923 0.06591  0.04907  250 HIS A CB  
1904 C CG  . HIS A 250 ? 0.74078 1.06822 0.76742 -0.08812 0.05383  0.04253  250 HIS A CG  
1905 N ND1 . HIS A 250 ? 0.71469 1.02840 0.73613 -0.05362 0.05963  0.04001  250 HIS A ND1 
1906 C CD2 . HIS A 250 ? 0.73499 1.03822 0.75429 -0.10343 0.03558  0.03819  250 HIS A CD2 
1907 C CE1 . HIS A 250 ? 0.74769 1.03651 0.75250 -0.04358 0.04640  0.03413  250 HIS A CE1 
1908 N NE2 . HIS A 250 ? 0.78315 1.06328 0.78700 -0.07314 0.02857  0.02942  250 HIS A NE2 
1909 N N   . TYR A 251 ? 0.58053 1.00039 0.64353 -0.04064 0.08630  0.03508  251 TYR A N   
1910 C CA  . TYR A 251 ? 0.57352 0.99238 0.64252 -0.00700 0.09457  0.03319  251 TYR A CA  
1911 C C   . TYR A 251 ? 0.62722 1.09584 0.70781 0.00672  0.09893  0.02457  251 TYR A C   
1912 O O   . TYR A 251 ? 0.56695 1.04096 0.64739 0.03518  0.10418  0.02336  251 TYR A O   
1913 C CB  . TYR A 251 ? 0.60988 0.98414 0.69047 0.00702  0.10344  0.04088  251 TYR A CB  
1914 C CG  . TYR A 251 ? 0.73997 1.06970 0.80772 0.00709  0.10171  0.04930  251 TYR A CG  
1915 C CD1 . TYR A 251 ? 0.64791 0.96780 0.70163 0.02998  0.10507  0.05464  251 TYR A CD1 
1916 C CD2 . TYR A 251 ? 0.73571 1.03593 0.80043 -0.00963 0.09584  0.05087  251 TYR A CD2 
1917 C CE1 . TYR A 251 ? 0.60931 0.89391 0.64767 0.03635  0.10283  0.06084  251 TYR A CE1 
1918 C CE2 . TYR A 251 ? 0.73266 0.99466 0.78344 -0.00550 0.09274  0.05651  251 TYR A CE2 
1919 C CZ  . TYR A 251 ? 0.60935 0.86519 0.64765 0.01759  0.09635  0.06122  251 TYR A CZ  
1920 O OH  . TYR A 251 ? 0.70982 0.93330 0.73066 0.02808  0.09274  0.06544  251 TYR A OH  
1921 N N   . GLY A 252 ? 0.61070 1.11698 0.69736 -0.00791 0.09752  0.01969  252 GLY A N   
1922 C CA  . GLY A 252 ? 0.65357 1.20870 0.74886 0.01033  0.10008  0.00909  252 GLY A CA  
1923 C C   . GLY A 252 ? 0.67400 1.21026 0.78269 0.03332  0.10289  0.00367  252 GLY A C   
1924 O O   . GLY A 252 ? 0.87582 1.44732 0.99024 0.05325  0.10198  -0.00803 252 GLY A O   
1925 N N   . VAL A 253 ? 0.78116 1.26371 0.89945 0.03274  0.10385  0.00896  253 VAL A N   
1926 C CA  . VAL A 253 ? 0.67845 1.13968 0.82295 0.05177  0.10224  -0.00028 253 VAL A CA  
1927 C C   . VAL A 253 ? 0.63968 1.07946 0.78806 0.03887  0.09506  -0.00390 253 VAL A C   
1928 O O   . VAL A 253 ? 0.65136 1.07450 0.78234 0.01820  0.09506  0.00659  253 VAL A O   
1929 C CB  . VAL A 253 ? 0.61245 1.02865 0.78117 0.07152  0.11220  0.00947  253 VAL A CB  
1930 C CG1 . VAL A 253 ? 0.70857 1.14655 0.86883 0.09479  0.11791  0.01076  253 VAL A CG1 
1931 C CG2 . VAL A 253 ? 0.72617 1.10499 0.88812 0.06130  0.12029  0.02800  253 VAL A CG2 
1932 N N   . THR A 254 ? 0.78172 1.22105 0.95192 0.05492  0.08592  -0.02171 254 THR A N   
1933 C CA  . THR A 254 ? 0.69634 1.11511 0.87237 0.05059  0.07595  -0.03003 254 THR A CA  
1934 C C   . THR A 254 ? 0.73859 1.10288 0.94851 0.04805  0.07983  -0.02305 254 THR A C   
1935 O O   . THR A 254 ? 0.79080 1.13439 1.02911 0.05678  0.09019  -0.01435 254 THR A O   
1936 C CB  . THR A 254 ? 0.70065 1.14017 0.89101 0.07458  0.05935  -0.05839 254 THR A CB  
1937 O OG1 . THR A 254 ? 1.03342 1.45014 1.23444 0.07666  0.04627  -0.07131 254 THR A OG1 
1938 C CG2 . THR A 254 ? 0.66611 1.09076 0.89982 0.09655  0.05556  -0.07167 254 THR A CG2 
1939 N N   . PRO A 255 ? 0.77059 1.11338 0.97616 0.03779  0.07423  -0.02312 255 PRO A N   
1940 C CA  . PRO A 255 ? 0.71044 1.01110 0.95714 0.03809  0.07764  -0.01929 255 PRO A CA  
1941 C C   . PRO A 255 ? 0.75924 1.04662 1.07211 0.05430  0.07494  -0.03285 255 PRO A C   
1942 O O   . PRO A 255 ? 0.77413 1.03291 1.12949 0.05442  0.08875  -0.01795 255 PRO A O   
1943 C CB  . PRO A 255 ? 0.58791 0.87954 0.81973 0.03257  0.06418  -0.02899 255 PRO A CB  
1944 C CG  . PRO A 255 ? 0.56503 0.87951 0.73444 0.02038  0.06387  -0.01962 255 PRO A CG  
1945 C CD  . PRO A 255 ? 0.65929 1.01569 0.82255 0.02735  0.06649  -0.02370 255 PRO A CD  
1946 N N   . LYS A 256 ? 0.85816 1.16563 1.18324 0.06969  0.05748  -0.06006 256 LYS A N   
1947 C CA  . LYS A 256 ? 0.88817 1.17772 1.28083 0.08533  0.05025  -0.07644 256 LYS A CA  
1948 C C   . LYS A 256 ? 1.01882 1.29647 1.42222 0.09022  0.07097  -0.05289 256 LYS A C   
1949 O O   . LYS A 256 ? 1.04013 1.28242 1.50204 0.09154  0.08243  -0.04033 256 LYS A O   
1950 C CB  . LYS A 256 ? 0.92248 1.23923 1.31469 0.10757  0.02271  -0.11488 256 LYS A CB  
1951 C CG  . LYS A 256 ? 0.90754 1.20257 1.36927 0.12612  0.00931  -0.13699 256 LYS A CG  
1952 C CD  . LYS A 256 ? 1.18918 1.51925 1.62297 0.15303  -0.00736 -0.16156 256 LYS A CD  
1953 C CE  . LYS A 256 ? 1.16254 1.46220 1.65264 0.16936  -0.01234 -0.17002 256 LYS A CE  
1954 N NZ  . LYS A 256 ? 1.14577 1.41852 1.64036 0.15710  0.02053  -0.12712 256 LYS A NZ  
1955 N N   . GLN A 257 ? 0.95961 1.26898 1.31002 0.09522  0.07646  -0.04613 257 GLN A N   
1956 C CA  . GLN A 257 ? 0.84411 1.14625 1.19427 0.10684  0.09393  -0.02615 257 GLN A CA  
1957 C C   . GLN A 257 ? 0.88653 1.15921 1.24089 0.09947  0.11932  0.00901  257 GLN A C   
1958 O O   . GLN A 257 ? 0.89734 1.13957 1.28795 0.11151  0.13603  0.02852  257 GLN A O   
1959 C CB  . GLN A 257 ? 0.89524 1.24690 1.18599 0.11178  0.09334  -0.02796 257 GLN A CB  
1960 C CG  . GLN A 257 ? 1.12899 1.51251 1.41886 0.13315  0.07532  -0.05649 257 GLN A CG  
1961 C CD  . GLN A 257 ? 1.14714 1.59530 1.38205 0.13095  0.07397  -0.06009 257 GLN A CD  
1962 O OE1 . GLN A 257 ? 1.08496 1.54925 1.28884 0.10825  0.08283  -0.04415 257 GLN A OE1 
1963 N NE2 . GLN A 257 ? 1.34993 1.83640 1.57729 0.15489  0.06240  -0.08125 257 GLN A NE2 
1964 N N   . PHE A 258 ? 0.89630 1.17795 1.21078 0.08300  0.12301  0.01904  258 PHE A N   
1965 C CA  . PHE A 258 ? 0.85251 1.11098 1.16415 0.08105  0.14334  0.04798  258 PHE A CA  
1966 C C   . PHE A 258 ? 0.88123 1.10358 1.26223 0.08203  0.15409  0.05833  258 PHE A C   
1967 O O   . PHE A 258 ? 0.89288 1.09514 1.29751 0.09503  0.17829  0.08688  258 PHE A O   
1968 C CB  . PHE A 258 ? 0.70743 0.97551 0.97241 0.06287  0.13648  0.04759  258 PHE A CB  
1969 C CG  . PHE A 258 ? 0.76950 1.01849 1.02169 0.06634  0.15242  0.07192  258 PHE A CG  
1970 C CD1 . PHE A 258 ? 0.83065 1.08954 1.04242 0.07990  0.16180  0.08624  258 PHE A CD1 
1971 C CD2 . PHE A 258 ? 0.73690 0.96319 1.01559 0.06069  0.15569  0.07718  258 PHE A CD2 
1972 C CE1 . PHE A 258 ? 0.95321 1.19803 1.14748 0.09109  0.17403  0.10561  258 PHE A CE1 
1973 C CE2 . PHE A 258 ? 0.75565 0.97007 1.01884 0.06950  0.17030  0.09884  258 PHE A CE2 
1974 C CZ  . PHE A 258 ? 0.81816 1.04110 1.03683 0.08622  0.17929  0.11309  258 PHE A CZ  
1975 N N   . PHE A 259 ? 0.83736 1.05438 1.25449 0.07024  0.13694  0.03602  259 PHE A N   
1976 C CA  . PHE A 259 ? 0.86763 1.05770 1.36342 0.06725  0.14412  0.04127  259 PHE A CA  
1977 C C   . PHE A 259 ? 0.93565 1.10282 1.49903 0.07834  0.15392  0.04906  259 PHE A C   
1978 O O   . PHE A 259 ? 0.90402 1.04826 1.51853 0.08024  0.18033  0.08034  259 PHE A O   
1979 C CB  . PHE A 259 ? 0.93448 1.12932 1.45575 0.05773  0.11639  0.00612  259 PHE A CB  
1980 C CG  . PHE A 259 ? 1.04672 1.22304 1.65177 0.05162  0.12085  0.00746  259 PHE A CG  
1981 C CD1 . PHE A 259 ? 0.93753 1.11257 1.53558 0.04530  0.13528  0.02689  259 PHE A CD1 
1982 C CD2 . PHE A 259 ? 1.12869 1.29064 1.82559 0.05313  0.10948  -0.01205 259 PHE A CD2 
1983 C CE1 . PHE A 259 ? 0.99491 1.16232 1.67680 0.03992  0.14117  0.02860  259 PHE A CE1 
1984 C CE2 . PHE A 259 ? 1.05189 1.20226 1.84032 0.04418  0.11367  -0.01143 259 PHE A CE2 
1985 C CZ  . PHE A 259 ? 1.05735 1.21423 1.83875 0.03726  0.13122  0.01010  259 PHE A CZ  
1986 N N   . THR A 260 ? 0.89695 1.06944 1.46401 0.08742  0.13314  0.02187  260 THR A N   
1987 C CA  . THR A 260 ? 0.90023 1.04321 1.53267 0.09931  0.13634  0.02431  260 THR A CA  
1988 C C   . THR A 260 ? 0.92649 1.05397 1.53985 0.11409  0.17066  0.06905  260 THR A C   
1989 O O   . THR A 260 ? 1.03888 1.12951 1.71834 0.11995  0.18859  0.09212  260 THR A O   
1990 C CB  . THR A 260 ? 0.91221 1.06873 1.53451 0.11357  0.10417  -0.01672 260 THR A CB  
1991 O OG1 . THR A 260 ? 1.08430 1.26640 1.69645 0.10809  0.07348  -0.05638 260 THR A OG1 
1992 C CG2 . THR A 260 ? 0.74617 0.86205 1.45356 0.12430  0.09712  -0.02497 260 THR A CG2 
1993 N N   . TYR A 261 ? 0.94144 1.09612 1.46773 0.12232  0.17947  0.08167  261 TYR A N   
1994 C CA  . TYR A 261 ? 0.91146 1.05594 1.41084 0.14503  0.20877  0.12000  261 TYR A CA  
1995 C C   . TYR A 261 ? 0.87532 0.99456 1.41150 0.14667  0.24419  0.16466  261 TYR A C   
1996 O O   . TYR A 261 ? 0.84952 0.94384 1.40222 0.16772  0.27224  0.20121  261 TYR A O   
1997 C CB  . TYR A 261 ? 0.80949 0.99351 1.21515 0.15398  0.20602  0.11797  261 TYR A CB  
1998 C CG  . TYR A 261 ? 0.77688 0.95702 1.14899 0.18662  0.22668  0.14497  261 TYR A CG  
1999 C CD1 . TYR A 261 ? 0.95045 1.12723 1.32349 0.20656  0.21905  0.13479  261 TYR A CD1 
2000 C CD2 . TYR A 261 ? 0.75482 0.93519 1.09059 0.20387  0.25220  0.17898  261 TYR A CD2 
2001 C CE1 . TYR A 261 ? 0.88326 1.05532 1.22132 0.24172  0.23699  0.15898  261 TYR A CE1 
2002 C CE2 . TYR A 261 ? 0.95867 1.13714 1.25771 0.24154  0.27022  0.20287  261 TYR A CE2 
2003 C CZ  . TYR A 261 ? 1.00028 1.17368 1.30040 0.25981  0.26290  0.19338  261 TYR A CZ  
2004 O OH  . TYR A 261 ? 1.06379 1.23462 1.32233 0.30227  0.27971  0.21644  261 TYR A OH  
2005 N N   . PHE A 262 ? 0.86122 0.98777 1.41016 0.12815  0.24517  0.16473  262 PHE A N   
2006 C CA  . PHE A 262 ? 0.89550 1.01063 1.47105 0.13379  0.28086  0.20832  262 PHE A CA  
2007 C C   . PHE A 262 ? 0.85779 0.94914 1.54807 0.11588  0.28906  0.21474  262 PHE A C   
2008 O O   . PHE A 262 ? 0.70695 0.80878 1.42954 0.09699  0.28018  0.20066  262 PHE A O   
2009 C CB  . PHE A 262 ? 0.85201 0.99336 1.36328 0.13116  0.27850  0.20697  262 PHE A CB  
2010 C CG  . PHE A 262 ? 0.74329 0.90656 1.15652 0.14927  0.27280  0.20438  262 PHE A CG  
2011 C CD1 . PHE A 262 ? 0.85350 1.01810 1.22664 0.18295  0.30004  0.23965  262 PHE A CD1 
2012 C CD2 . PHE A 262 ? 0.94331 1.12897 1.30839 0.13466  0.24011  0.16657  262 PHE A CD2 
2013 C CE1 . PHE A 262 ? 0.94285 1.13113 1.23328 0.20149  0.28937  0.23022  262 PHE A CE1 
2014 C CE2 . PHE A 262 ? 0.89753 1.10706 1.18758 0.14742  0.23318  0.16187  262 PHE A CE2 
2015 C CZ  . PHE A 262 ? 0.77335 0.98435 1.02797 0.18079  0.25513  0.19020  262 PHE A CZ  
2016 N N   . LYS B 9   ? 1.33690 1.11860 1.50206 -0.17602 -0.04690 0.11118  9   LYS B N   
2017 C CA  . LYS B 9   ? 1.28408 1.05032 1.47872 -0.17286 -0.05466 0.09590  9   LYS B CA  
2018 C C   . LYS B 9   ? 1.24131 0.99628 1.41683 -0.16197 -0.05947 0.07821  9   LYS B C   
2019 O O   . LYS B 9   ? 1.23126 0.98820 1.37616 -0.15815 -0.05765 0.08164  9   LYS B O   
2020 C CB  . LYS B 9   ? 1.20075 0.97275 1.41278 -0.17419 -0.05469 0.08110  9   LYS B CB  
2021 C CG  . LYS B 9   ? 1.12695 0.90969 1.36615 -0.18522 -0.05028 0.09789  9   LYS B CG  
2022 C CD  . LYS B 9   ? 1.27795 1.06675 1.53488 -0.18587 -0.05144 0.08127  9   LYS B CD  
2023 C CE  . LYS B 9   ? 1.38549 1.18616 1.67349 -0.19725 -0.04671 0.09838  9   LYS B CE  
2024 N NZ  . LYS B 9   ? 1.17745 0.98497 1.48469 -0.19799 -0.04871 0.08175  9   LYS B NZ  
2025 N N   . GLU B 10  ? 1.57246 1.31646 1.76693 -0.15707 -0.06568 0.05914  10  GLU B N   
2026 C CA  . GLU B 10  ? 1.57633 1.31212 1.75386 -0.14609 -0.06943 0.04050  10  GLU B CA  
2027 C C   . GLU B 10  ? 1.56595 1.31043 1.72078 -0.14001 -0.06824 0.02131  10  GLU B C   
2028 O O   . GLU B 10  ? 1.55392 1.29325 1.69880 -0.13087 -0.07169 0.00375  10  GLU B O   
2029 C CB  . GLU B 10  ? 1.60263 1.32281 1.81111 -0.14286 -0.07666 0.02902  10  GLU B CB  
2030 C CG  . GLU B 10  ? 1.68679 1.40553 1.93096 -0.14833 -0.08028 0.02186  10  GLU B CG  
2031 C CD  . GLU B 10  ? 1.81674 1.53183 2.09471 -0.15890 -0.08012 0.04428  10  GLU B CD  
2032 O OE1 . GLU B 10  ? 1.89779 1.62468 2.16793 -0.16637 -0.07392 0.06502  10  GLU B OE1 
2033 O OE2 . GLU B 10  ? 1.86417 1.56495 2.17635 -0.15939 -0.08599 0.04167  10  GLU B OE2 
2034 N N   . THR B 11  ? 1.20378 0.96225 1.35124 -0.14456 -0.06322 0.02492  11  THR B N   
2035 C CA  . THR B 11  ? 1.21227 0.97997 1.34225 -0.13924 -0.06224 0.00850  11  THR B CA  
2036 C C   . THR B 11  ? 1.19124 0.97012 1.28896 -0.13909 -0.05494 0.01694  11  THR B C   
2037 O O   . THR B 11  ? 1.11409 0.90044 1.21125 -0.14643 -0.04945 0.03423  11  THR B O   
2038 C CB  . THR B 11  ? 1.21086 0.98581 1.36665 -0.14407 -0.06354 0.00188  11  THR B CB  
2039 O OG1 . THR B 11  ? 1.41501 1.19565 1.59069 -0.15488 -0.05912 0.02149  11  THR B OG1 
2040 C CG2 . THR B 11  ? 1.28833 1.05224 1.47065 -0.14154 -0.07252 -0.01448 11  THR B CG2 
2041 N N   . ILE B 12  ? 1.21454 0.99498 1.28597 -0.13059 -0.05495 0.00465  12  ILE B N   
2042 C CA  . ILE B 12  ? 0.99243 0.78165 1.03395 -0.12919 -0.04900 0.00900  12  ILE B CA  
2043 C C   . ILE B 12  ? 1.15218 0.94854 1.18254 -0.12250 -0.04890 -0.00716 12  ILE B C   
2044 O O   . ILE B 12  ? 1.28197 1.07510 1.32017 -0.11716 -0.05436 -0.02161 12  ILE B O   
2045 C CB  . ILE B 12  ? 1.11781 0.89944 1.13753 -0.12549 -0.04965 0.01445  12  ILE B CB  
2046 C CG1 . ILE B 12  ? 0.94256 0.73285 0.93648 -0.12729 -0.04381 0.02292  12  ILE B CG1 
2047 C CG2 . ILE B 12  ? 1.07163 0.84684 1.08083 -0.11543 -0.05377 -0.00078 12  ILE B CG2 
2048 C CD1 . ILE B 12  ? 1.23539 1.01955 1.21517 -0.12765 -0.04512 0.03383  12  ILE B CD1 
2049 N N   . LYS B 13  ? 1.07325 0.88022 1.08577 -0.12257 -0.04281 -0.00480 13  LYS B N   
2050 C CA  . LYS B 13  ? 1.06221 0.87595 1.06340 -0.11561 -0.04246 -0.01817 13  LYS B CA  
2051 C C   . LYS B 13  ? 1.08876 0.90408 1.06134 -0.11242 -0.03807 -0.01525 13  LYS B C   
2052 O O   . LYS B 13  ? 1.23323 1.05708 1.19830 -0.11660 -0.03155 -0.00775 13  LYS B O   
2053 C CB  . LYS B 13  ? 1.19923 1.02631 1.21665 -0.11887 -0.03965 -0.02119 13  LYS B CB  
2054 C CG  . LYS B 13  ? 1.25321 1.08602 1.26662 -0.11092 -0.04235 -0.03649 13  LYS B CG  
2055 C CD  . LYS B 13  ? 1.31211 1.16073 1.33526 -0.11315 -0.03742 -0.03751 13  LYS B CD  
2056 C CE  . LYS B 13  ? 1.48878 1.34424 1.48973 -0.11087 -0.02936 -0.03412 13  LYS B CE  
2057 N NZ  . LYS B 13  ? 1.21579 1.07283 1.20358 -0.10115 -0.03140 -0.04563 13  LYS B NZ  
2058 N N   . ILE B 14  ? 1.04723 0.85481 1.00471 -0.10509 -0.04156 -0.02124 14  ILE B N   
2059 C CA  . ILE B 14  ? 0.99613 0.80303 0.92922 -0.10193 -0.03891 -0.01950 14  ILE B CA  
2060 C C   . ILE B 14  ? 0.91859 0.73151 0.84446 -0.09491 -0.03814 -0.03056 14  ILE B C   
2061 O O   . ILE B 14  ? 1.06317 0.87632 0.99607 -0.08950 -0.04238 -0.03995 14  ILE B O   
2062 C CB  . ILE B 14  ? 1.07205 0.86726 0.99568 -0.09861 -0.04302 -0.01707 14  ILE B CB  
2063 C CG1 . ILE B 14  ? 1.06324 0.85170 0.99971 -0.10422 -0.04523 -0.00715 14  ILE B CG1 
2064 C CG2 . ILE B 14  ? 1.11414 0.90862 1.01576 -0.09762 -0.04080 -0.01346 14  ILE B CG2 
2065 C CD1 . ILE B 14  ? 1.11870 0.90806 1.04684 -0.11094 -0.04262 0.00709  14  ILE B CD1 
2066 N N   . ASN B 15  ? 0.97052 0.78857 0.88241 -0.09457 -0.03313 -0.02974 15  ASN B N   
2067 C CA  . ASN B 15  ? 1.00861 0.83209 0.91553 -0.08779 -0.03199 -0.03901 15  ASN B CA  
2068 C C   . ASN B 15  ? 0.91370 0.72924 0.80274 -0.08219 -0.03362 -0.04021 15  ASN B C   
2069 O O   . ASN B 15  ? 0.93782 0.74519 0.81790 -0.08427 -0.03509 -0.03394 15  ASN B O   
2070 C CB  . ASN B 15  ? 1.21520 1.05107 1.12337 -0.09055 -0.02458 -0.03909 15  ASN B CB  
2071 C CG  . ASN B 15  ? 1.27539 1.12092 1.20490 -0.09642 -0.02256 -0.03682 15  ASN B CG  
2072 O OD1 . ASN B 15  ? 1.22958 1.08056 1.17426 -0.09382 -0.02517 -0.04389 15  ASN B OD1 
2073 N ND2 . ASN B 15  ? 1.28109 1.12960 1.21271 -0.10457 -0.01831 -0.02618 15  ASN B ND2 
2074 N N   . ASN B 16  ? 0.91089 0.72909 0.79758 -0.07498 -0.03406 -0.04768 16  ASN B N   
2075 C CA  . ASN B 16  ? 0.91071 0.72248 0.78411 -0.06939 -0.03518 -0.04885 16  ASN B CA  
2076 C C   . ASN B 16  ? 0.90912 0.71019 0.77602 -0.06896 -0.03941 -0.04364 16  ASN B C   
2077 O O   . ASN B 16  ? 1.03561 0.83030 0.89163 -0.06955 -0.03947 -0.04009 16  ASN B O   
2078 C CB  . ASN B 16  ? 0.98293 0.79592 0.84592 -0.07127 -0.03014 -0.04895 16  ASN B CB  
2079 C CG  . ASN B 16  ? 1.11218 0.93657 0.98180 -0.06992 -0.02492 -0.05495 16  ASN B CG  
2080 O OD1 . ASN B 16  ? 1.01238 0.84131 0.89115 -0.06400 -0.02640 -0.06045 16  ASN B OD1 
2081 N ND2 . ASN B 16  ? 0.99715 0.82759 0.86193 -0.07494 -0.01864 -0.05370 16  ASN B ND2 
2082 N N   . ILE B 17  ? 0.94488 0.74450 0.81954 -0.06748 -0.04321 -0.04407 17  ILE B N   
2083 C CA  . ILE B 17  ? 0.90411 0.69537 0.77437 -0.06528 -0.04655 -0.04010 17  ILE B CA  
2084 C C   . ILE B 17  ? 0.90181 0.69319 0.76689 -0.05664 -0.04837 -0.04310 17  ILE B C   
2085 O O   . ILE B 17  ? 1.09191 0.88967 0.96163 -0.05137 -0.05005 -0.04908 17  ILE B O   
2086 C CB  . ILE B 17  ? 0.90347 0.69324 0.78464 -0.06647 -0.04932 -0.04048 17  ILE B CB  
2087 C CG1 . ILE B 17  ? 0.90671 0.69723 0.79684 -0.07529 -0.04751 -0.03594 17  ILE B CG1 
2088 C CG2 . ILE B 17  ? 0.90289 0.68498 0.78024 -0.06403 -0.05152 -0.03599 17  ILE B CG2 
2089 C CD1 . ILE B 17  ? 0.90763 0.69453 0.81183 -0.07696 -0.05058 -0.03595 17  ILE B CD1 
2090 N N   . MET B 18  ? 0.95237 0.73754 0.80876 -0.05543 -0.04844 -0.03828 18  MET B N   
2091 C CA  . MET B 18  ? 1.04295 0.82784 0.89594 -0.04782 -0.04980 -0.03817 18  MET B CA  
2092 C C   . MET B 18  ? 1.03897 0.82032 0.89077 -0.04488 -0.05177 -0.03320 18  MET B C   
2093 O O   . MET B 18  ? 0.90082 0.67587 0.75117 -0.04901 -0.05195 -0.02727 18  MET B O   
2094 C CB  . MET B 18  ? 1.16007 0.94052 1.00762 -0.04834 -0.04855 -0.03649 18  MET B CB  
2095 C CG  . MET B 18  ? 1.23857 1.01644 1.08513 -0.04173 -0.05016 -0.03310 18  MET B CG  
2096 S SD  . MET B 18  ? 1.54719 1.33290 1.39879 -0.03385 -0.05015 -0.03822 18  MET B SD  
2097 C CE  . MET B 18  ? 1.25071 1.03049 1.10269 -0.02846 -0.05164 -0.03078 18  MET B CE  
2098 N N   . ILE B 19  ? 1.20216 0.98898 1.05452 -0.03742 -0.05316 -0.03538 19  ILE B N   
2099 C CA  . ILE B 19  ? 1.09727 0.88353 0.94792 -0.03308 -0.05379 -0.03124 19  ILE B CA  
2100 C C   . ILE B 19  ? 1.11393 0.89768 0.96074 -0.02986 -0.05319 -0.02334 19  ILE B C   
2101 O O   . ILE B 19  ? 1.21793 1.00597 1.06375 -0.02467 -0.05351 -0.02323 19  ILE B O   
2102 C CB  . ILE B 19  ? 1.07331 0.86857 0.92461 -0.02630 -0.05545 -0.03785 19  ILE B CB  
2103 C CG1 . ILE B 19  ? 1.06053 0.85553 0.91917 -0.03015 -0.05671 -0.04502 19  ILE B CG1 
2104 C CG2 . ILE B 19  ? 1.06034 0.85848 0.90705 -0.01937 -0.05478 -0.03317 19  ILE B CG2 
2105 C CD1 . ILE B 19  ? 1.04550 0.84323 0.91074 -0.03492 -0.05749 -0.05112 19  ILE B CD1 
2106 N N   . ALA B 20  ? 1.05297 0.82981 0.89983 -0.03325 -0.05282 -0.01601 20  ALA B N   
2107 C CA  . ALA B 20  ? 0.98029 0.75358 0.82694 -0.03178 -0.05281 -0.00791 20  ALA B CA  
2108 C C   . ALA B 20  ? 1.07675 0.85411 0.92436 -0.02586 -0.05165 -0.00073 20  ALA B C   
2109 O O   . ALA B 20  ? 0.91062 0.68777 0.76007 -0.02305 -0.05131 0.00708  20  ALA B O   
2110 C CB  . ALA B 20  ? 0.90281 0.66700 0.74994 -0.03977 -0.05397 -0.00426 20  ALA B CB  
2111 N N   . LYS B 21  ? 0.94774 0.72925 0.79542 -0.02373 -0.05072 -0.00328 21  LYS B N   
2112 C CA  . LYS B 21  ? 1.02784 0.81580 0.87547 -0.01706 -0.04839 0.00176  21  LYS B CA  
2113 C C   . LYS B 21  ? 1.13453 0.93164 0.97835 -0.01104 -0.04815 -0.00777 21  LYS B C   
2114 O O   . LYS B 21  ? 1.02865 0.82369 0.87458 -0.01438 -0.04988 -0.01696 21  LYS B O   
2115 C CB  . LYS B 21  ? 0.99700 0.78014 0.85067 -0.02046 -0.04743 0.00785  21  LYS B CB  
2116 C CG  . LYS B 21  ? 1.04854 0.82303 0.90640 -0.02725 -0.04921 0.01615  21  LYS B CG  
2117 C CD  . LYS B 21  ? 1.21789 0.99036 1.08331 -0.02932 -0.04872 0.02353  21  LYS B CD  
2118 C CE  . LYS B 21  ? 1.42670 1.19122 1.29660 -0.03674 -0.05211 0.03087  21  LYS B CE  
2119 N NZ  . LYS B 21  ? 1.90451 1.66720 1.78298 -0.04003 -0.05304 0.03743  21  LYS B NZ  
2120 N N   . TYR B 22  ? 1.05671 0.86466 0.89532 -0.00232 -0.04629 -0.00551 22  TYR B N   
2121 C CA  . TYR B 22  ? 0.97704 0.79500 0.81044 0.00397  -0.04680 -0.01605 22  TYR B CA  
2122 C C   . TYR B 22  ? 1.07098 0.88432 0.91023 0.00147  -0.04652 -0.02341 22  TYR B C   
2123 O O   . TYR B 22  ? 1.05558 0.86563 0.89964 0.00091  -0.04361 -0.01724 22  TYR B O   
2124 C CB  . TYR B 22  ? 0.96348 0.79532 0.78886 0.01398  -0.04384 -0.01092 22  TYR B CB  
2125 C CG  . TYR B 22  ? 1.19503 1.03895 1.01210 0.02068  -0.04614 -0.02346 22  TYR B CG  
2126 C CD1 . TYR B 22  ? 1.16880 1.01540 0.98562 0.02332  -0.04570 -0.03492 22  TYR B CD1 
2127 C CD2 . TYR B 22  ? 1.11477 0.96703 0.92586 0.02415  -0.04965 -0.02487 22  TYR B CD2 
2128 C CE1 . TYR B 22  ? 0.96263 0.81994 0.77232 0.02901  -0.04906 -0.04856 22  TYR B CE1 
2129 C CE2 . TYR B 22  ? 1.25435 1.11851 1.05802 0.02981  -0.05323 -0.03701 22  TYR B CE2 
2130 C CZ  . TYR B 22  ? 1.19001 1.05660 0.99248 0.03203  -0.05315 -0.04949 22  TYR B CZ  
2131 O OH  . TYR B 22  ? 1.15157 1.02996 0.94693 0.03745  -0.05782 -0.06347 22  TYR B OH  
2132 N N   . THR B 23  ? 1.06429 0.87683 0.90601 -0.00056 -0.04986 -0.03589 23  THR B N   
2133 C CA  . THR B 23  ? 1.13078 0.93597 0.98240 -0.00479 -0.05050 -0.04202 23  THR B CA  
2134 C C   . THR B 23  ? 1.00245 0.81458 0.85412 0.00125  -0.05204 -0.05634 23  THR B C   
2135 O O   . THR B 23  ? 1.16498 0.98365 1.01310 0.00318  -0.05572 -0.06571 23  THR B O   
2136 C CB  . THR B 23  ? 1.20386 0.99979 1.06293 -0.01471 -0.05323 -0.04303 23  THR B CB  
2137 O OG1 . THR B 23  ? 1.04787 0.83735 0.90588 -0.02016 -0.05205 -0.03145 23  THR B OG1 
2138 C CG2 . THR B 23  ? 0.96278 0.75164 0.83453 -0.01908 -0.05439 -0.04814 23  THR B CG2 
2139 N N   . VAL B 24  ? 0.93312 0.74378 0.79027 0.00413  -0.04967 -0.05876 24  VAL B N   
2140 C CA  . VAL B 24  ? 1.07788 0.89234 0.93832 0.00926  -0.05126 -0.07446 24  VAL B CA  
2141 C C   . VAL B 24  ? 1.00329 0.80444 0.88204 0.00208  -0.05298 -0.07727 24  VAL B C   
2142 O O   . VAL B 24  ? 1.07982 0.87417 0.96670 0.00022  -0.05004 -0.06888 24  VAL B O   
2143 C CB  . VAL B 24  ? 0.95294 0.77774 0.80598 0.01992  -0.04631 -0.07596 24  VAL B CB  
2144 C CG1 . VAL B 24  ? 0.96671 0.79733 0.82005 0.02635  -0.04875 -0.09567 24  VAL B CG1 
2145 C CG2 . VAL B 24  ? 0.95368 0.79101 0.79043 0.02561  -0.04358 -0.06637 24  VAL B CG2 
2146 N N   . LEU B 25  ? 1.03800 0.83603 0.92496 -0.00225 -0.05804 -0.08772 25  LEU B N   
2147 C CA  . LEU B 25  ? 1.03924 0.82491 0.94547 -0.01044 -0.06026 -0.08827 25  LEU B CA  
2148 C C   . LEU B 25  ? 1.20347 0.98802 1.12217 -0.00682 -0.06339 -0.10541 25  LEU B C   
2149 O O   . LEU B 25  ? 1.34313 1.13660 1.25549 -0.00129 -0.06650 -0.11958 25  LEU B O   
2150 C CB  . LEU B 25  ? 1.07264 0.85561 0.98175 -0.01961 -0.06318 -0.08483 25  LEU B CB  
2151 C CG  . LEU B 25  ? 1.16347 0.93539 1.08902 -0.03009 -0.06411 -0.07791 25  LEU B CG  
2152 C CD1 . LEU B 25  ? 1.04343 0.81562 0.96128 -0.03687 -0.06288 -0.06672 25  LEU B CD1 
2153 C CD2 . LEU B 25  ? 1.20664 0.97660 1.14914 -0.03291 -0.06880 -0.09038 25  LEU B CD2 
2154 N N   . TYR B 26  ? 1.29005 1.06391 1.22714 -0.00958 -0.06309 -0.10446 26  TYR B N   
2155 C CA  . TYR B 26  ? 1.18975 0.95900 1.14448 -0.00754 -0.06664 -0.12063 26  TYR B CA  
2156 C C   . TYR B 26  ? 1.16153 0.91989 1.13743 -0.01884 -0.07091 -0.11752 26  TYR B C   
2157 O O   . TYR B 26  ? 1.16456 0.91325 1.15307 -0.02502 -0.06949 -0.10418 26  TYR B O   
2158 C CB  . TYR B 26  ? 1.18890 0.95423 1.15242 -0.00119 -0.06273 -0.12161 26  TYR B CB  
2159 C CG  . TYR B 26  ? 1.28322 1.04281 1.26659 0.00211  -0.06622 -0.14014 26  TYR B CG  
2160 C CD1 . TYR B 26  ? 1.23564 1.00403 1.21180 0.01006  -0.06904 -0.16148 26  TYR B CD1 
2161 C CD2 . TYR B 26  ? 1.37201 1.11733 1.38244 -0.00278 -0.06735 -0.13633 26  TYR B CD2 
2162 C CE1 . TYR B 26  ? 1.45557 1.21772 1.45133 0.01301  -0.07297 -0.18055 26  TYR B CE1 
2163 C CE2 . TYR B 26  ? 1.39547 1.13376 1.42767 0.00017  -0.07092 -0.15366 26  TYR B CE2 
2164 C CZ  . TYR B 26  ? 1.52720 1.27345 1.55223 0.00803  -0.07377 -0.17678 26  TYR B CZ  
2165 O OH  . TYR B 26  ? 1.59480 1.33319 1.64280 0.01102  -0.07801 -0.19622 26  TYR B OH  
2166 N N   . THR B 27  ? 1.40302 1.16439 1.38325 -0.02152 -0.07628 -0.12889 27  THR B N   
2167 C CA  . THR B 27  ? 1.37459 1.12829 1.37560 -0.03258 -0.07989 -0.12521 27  THR B CA  
2168 C C   . THR B 27  ? 1.42642 1.16634 1.45361 -0.03638 -0.08036 -0.12163 27  THR B C   
2169 O O   . THR B 27  ? 1.70567 1.43873 1.74597 -0.04608 -0.08015 -0.10732 27  THR B O   
2170 C CB  . THR B 27  ? 1.37182 1.13094 1.37969 -0.03332 -0.08647 -0.14177 27  THR B CB  
2171 O OG1 . THR B 27  ? 1.51852 1.27537 1.53756 -0.02690 -0.09048 -0.16116 27  THR B OG1 
2172 C CG2 . THR B 27  ? 1.35488 1.12851 1.33806 -0.02871 -0.08661 -0.14453 27  THR B CG2 
2173 N N   . SER B 28  ? 1.19340 0.92984 1.22925 -0.02855 -0.08097 -0.13447 28  SER B N   
2174 C CA  . SER B 28  ? 1.43190 1.15473 1.49477 -0.03081 -0.08129 -0.13075 28  SER B CA  
2175 C C   . SER B 28  ? 1.51208 1.22573 1.60345 -0.04138 -0.08653 -0.12924 28  SER B C   
2176 O O   . SER B 28  ? 1.62322 1.33597 1.72858 -0.04122 -0.09223 -0.14670 28  SER B O   
2177 C CB  . SER B 28  ? 1.23946 0.95905 1.29776 -0.03294 -0.07600 -0.10886 28  SER B CB  
2178 O OG  . SER B 28  ? 1.48797 1.19491 1.57428 -0.03569 -0.07703 -0.10292 28  SER B OG  
2179 N N   . ASN B 29  ? 1.46774 1.17531 1.56861 -0.05065 -0.08488 -0.10804 29  ASN B N   
2180 C CA  . ASN B 29  ? 1.55568 1.25543 1.68498 -0.06150 -0.08859 -0.10141 29  ASN B CA  
2181 C C   . ASN B 29  ? 1.53364 1.24174 1.65315 -0.07034 -0.08797 -0.09203 29  ASN B C   
2182 O O   . ASN B 29  ? 1.52273 1.22831 1.65172 -0.07985 -0.08656 -0.07352 29  ASN B O   
2183 C CB  . ASN B 29  ? 1.50472 1.19350 1.65354 -0.06578 -0.08734 -0.08311 29  ASN B CB  
2184 C CG  . ASN B 29  ? 1.73372 1.41018 1.91298 -0.06110 -0.09068 -0.09456 29  ASN B CG  
2185 O OD1 . ASN B 29  ? 1.77436 1.44664 1.97341 -0.06108 -0.09583 -0.11174 29  ASN B OD1 
2186 N ND2 . ASN B 29  ? 1.83671 1.50746 2.02126 -0.05681 -0.08813 -0.08605 29  ASN B ND2 
2187 N N   . CYS B 30  ? 1.37371 1.09297 1.47442 -0.06710 -0.08874 -0.10382 30  CYS B N   
2188 C CA  . CYS B 30  ? 1.35155 1.07932 1.44602 -0.07471 -0.08786 -0.09633 30  CYS B CA  
2189 C C   . CYS B 30  ? 1.30138 1.03941 1.38831 -0.07062 -0.09184 -0.11478 30  CYS B C   
2190 O O   . CYS B 30  ? 1.29187 1.03392 1.36466 -0.06069 -0.09341 -0.12960 30  CYS B O   
2191 C CB  . CYS B 30  ? 1.24134 0.97496 1.30920 -0.07594 -0.08163 -0.07956 30  CYS B CB  
2192 S SG  . CYS B 30  ? 1.23092 0.97550 1.26374 -0.06521 -0.07950 -0.08827 30  CYS B SG  
2193 N N   . ILE B 31  ? 1.36081 1.10407 1.45914 -0.07844 -0.09362 -0.11322 31  ILE B N   
2194 C CA  . ILE B 31  ? 1.10500 0.86045 1.19658 -0.07625 -0.09739 -0.12658 31  ILE B CA  
2195 C C   . ILE B 31  ? 1.17547 0.94135 1.24498 -0.07798 -0.09169 -0.11422 31  ILE B C   
2196 O O   . ILE B 31  ? 1.23639 1.00222 1.31198 -0.08652 -0.08732 -0.09844 31  ILE B O   
2197 C CB  . ILE B 31  ? 1.11089 0.86592 1.23490 -0.08390 -0.10366 -0.13394 31  ILE B CB  
2198 C CG1 . ILE B 31  ? 1.05987 0.80135 1.21131 -0.08373 -0.10908 -0.14418 31  ILE B CG1 
2199 C CG2 . ILE B 31  ? 1.16609 0.93437 1.28438 -0.08063 -0.10918 -0.14961 31  ILE B CG2 
2200 C CD1 . ILE B 31  ? 1.27530 1.01579 1.41362 -0.07161 -0.11241 -0.16392 31  ILE B CD1 
2201 N N   . MET B 32  ? 1.24204 1.01750 1.28672 -0.06980 -0.09164 -0.12117 32  MET B N   
2202 C CA  . MET B 32  ? 1.21426 0.99791 1.23833 -0.07008 -0.08619 -0.11027 32  MET B CA  
2203 C C   . MET B 32  ? 1.42995 1.22701 1.45190 -0.06827 -0.08965 -0.11946 32  MET B C   
2204 O O   . MET B 32  ? 1.49585 1.29906 1.50875 -0.06017 -0.09456 -0.13287 32  MET B O   
2205 C CB  . MET B 32  ? 0.95269 0.73560 0.95005 -0.06221 -0.08222 -0.10579 32  MET B CB  
2206 C CG  . MET B 32  ? 1.28378 1.05641 1.27997 -0.06530 -0.07755 -0.09153 32  MET B CG  
2207 S SD  . MET B 32  ? 1.29481 1.06754 1.26455 -0.05557 -0.07416 -0.08857 32  MET B SD  
2208 C CE  . MET B 32  ? 1.06876 0.85533 1.01989 -0.04951 -0.07493 -0.09517 32  MET B CE  
2209 N N   . ASP B 33  ? 1.47116 1.27423 1.50068 -0.07531 -0.08684 -0.11163 33  ASP B N   
2210 C CA  . ASP B 33  ? 1.51602 1.33302 1.54261 -0.07333 -0.08867 -0.11707 33  ASP B CA  
2211 C C   . ASP B 33  ? 1.47471 1.29581 1.47697 -0.06967 -0.08211 -0.10748 33  ASP B C   
2212 O O   . ASP B 33  ? 1.50309 1.32250 1.50354 -0.07525 -0.07527 -0.09480 33  ASP B O   
2213 C CB  . ASP B 33  ? 1.52443 1.34709 1.57720 -0.08276 -0.08908 -0.11506 33  ASP B CB  
2214 C CG  . ASP B 33  ? 1.48115 1.29971 1.56172 -0.08659 -0.09699 -0.12595 33  ASP B CG  
2215 O OD1 . ASP B 33  ? 1.43180 1.24210 1.51037 -0.08170 -0.10158 -0.13559 33  ASP B OD1 
2216 O OD2 . ASP B 33  ? 1.49242 1.31624 1.59826 -0.09444 -0.09845 -0.12513 33  ASP B OD2 
2217 N N   . ILE B 34  ? 1.21527 1.04184 1.19913 -0.06020 -0.08436 -0.11345 34  ILE B N   
2218 C CA  . ILE B 34  ? 1.17028 0.99962 1.13321 -0.05574 -0.07929 -0.10547 34  ILE B CA  
2219 C C   . ILE B 34  ? 1.18989 1.03242 1.15598 -0.05443 -0.08034 -0.10815 34  ILE B C   
2220 O O   . ILE B 34  ? 1.28054 1.13227 1.25060 -0.04998 -0.08731 -0.11862 34  ILE B O   
2221 C CB  . ILE B 34  ? 1.04864 0.87645 0.99184 -0.04611 -0.08063 -0.10776 34  ILE B CB  
2222 C CG1 . ILE B 34  ? 0.97268 0.78903 0.91743 -0.04676 -0.08023 -0.10741 34  ILE B CG1 
2223 C CG2 . ILE B 34  ? 1.07998 0.90817 1.00516 -0.04261 -0.07538 -0.09780 34  ILE B CG2 
2224 C CD1 . ILE B 34  ? 1.13806 0.95297 1.06379 -0.03824 -0.07886 -0.10590 34  ILE B CD1 
2225 N N   . TYR B 35  ? 1.21734 1.06170 1.18173 -0.05786 -0.07368 -0.09922 35  TYR B N   
2226 C CA  . TYR B 35  ? 1.07966 0.93635 1.04792 -0.05603 -0.07310 -0.10057 35  TYR B CA  
2227 C C   . TYR B 35  ? 1.03573 0.89163 0.98462 -0.04951 -0.06929 -0.09514 35  TYR B C   
2228 O O   . TYR B 35  ? 1.01225 0.85972 0.95090 -0.05179 -0.06321 -0.08697 35  TYR B O   
2229 C CB  . TYR B 35  ? 1.17587 1.03707 1.16053 -0.06480 -0.06753 -0.09569 35  TYR B CB  
2230 C CG  . TYR B 35  ? 1.24830 1.10710 1.25406 -0.07324 -0.06967 -0.09671 35  TYR B CG  
2231 C CD1 . TYR B 35  ? 1.26684 1.13264 1.29208 -0.07395 -0.07760 -0.10697 35  TYR B CD1 
2232 C CD2 . TYR B 35  ? 1.32697 1.17668 1.33474 -0.08066 -0.06447 -0.08702 35  TYR B CD2 
2233 C CE1 . TYR B 35  ? 1.34431 1.20670 1.39256 -0.08206 -0.08010 -0.10803 35  TYR B CE1 
2234 C CE2 . TYR B 35  ? 1.51313 1.35995 1.54335 -0.08849 -0.06658 -0.08630 35  TYR B CE2 
2235 C CZ  . TYR B 35  ? 1.51891 1.37140 1.57037 -0.08928 -0.07430 -0.09706 35  TYR B CZ  
2236 O OH  . TYR B 35  ? 1.46813 1.31662 1.54542 -0.09741 -0.07695 -0.09655 35  TYR B OH  
2237 N N   . SER B 36  ? 1.47745 1.34203 1.42220 -0.04147 -0.07364 -0.09943 36  SER B N   
2238 C CA  . SER B 36  ? 1.57108 1.43576 1.50287 -0.03532 -0.07048 -0.09391 36  SER B CA  
2239 C C   . SER B 36  ? 1.74584 1.62419 1.68277 -0.02841 -0.07577 -0.09839 36  SER B C   
2240 O O   . SER B 36  ? 1.87200 1.75846 1.81450 -0.02622 -0.08352 -0.10601 36  SER B O   
2241 C CB  . SER B 36  ? 1.59977 1.45519 1.51335 -0.03059 -0.07037 -0.08928 36  SER B CB  
2242 O OG  . SER B 36  ? 1.67977 1.53675 1.58451 -0.02377 -0.06929 -0.08446 36  SER B OG  
2243 N N   . GLU B 37  ? 1.84872 1.72958 1.78418 -0.02469 -0.07211 -0.09397 37  GLU B N   
2244 C CA  . GLU B 37  ? 1.88231 1.77607 1.82389 -0.01736 -0.07684 -0.09593 37  GLU B CA  
2245 C C   . GLU B 37  ? 1.91125 1.81849 1.87170 -0.01990 -0.08244 -0.10401 37  GLU B C   
2246 O O   . GLU B 37  ? 1.96533 1.88352 1.92805 -0.01442 -0.09118 -0.10857 37  GLU B O   
2247 C CB  . GLU B 37  ? 1.99699 1.89203 1.92425 -0.00845 -0.08260 -0.09364 37  GLU B CB  
2248 C CG  . GLU B 37  ? 2.10687 1.98955 2.01893 -0.00597 -0.07747 -0.08449 37  GLU B CG  
2249 C CD  . GLU B 37  ? 1.97545 1.86101 1.87426 0.00253  -0.08211 -0.08016 37  GLU B CD  
2250 O OE1 . GLU B 37  ? 1.84590 1.74273 1.74352 0.00645  -0.08939 -0.08538 37  GLU B OE1 
2251 O OE2 . GLU B 37  ? 1.89817 1.77549 1.78789 0.00514  -0.07853 -0.07140 37  GLU B OE2 
2252 N N   . GLU B 38  ? 1.91860 1.82590 1.89312 -0.02860 -0.07772 -0.10528 38  GLU B N   
2253 C CA  . GLU B 38  ? 1.86458 1.78451 1.86163 -0.03272 -0.08217 -0.11187 38  GLU B CA  
2254 C C   . GLU B 38  ? 1.82837 1.75003 1.82712 -0.03284 -0.09267 -0.12041 38  GLU B C   
2255 O O   . GLU B 38  ? 1.73268 1.66735 1.74584 -0.03190 -0.10102 -0.12775 38  GLU B O   
2256 C CB  . GLU B 38  ? 1.88700 1.82224 1.89654 -0.02715 -0.08414 -0.11280 38  GLU B CB  
2257 C CG  . GLU B 38  ? 1.82682 1.76265 1.84036 -0.02714 -0.07350 -0.10735 38  GLU B CG  
2258 C CD  . GLU B 38  ? 1.66628 1.61798 1.69600 -0.02100 -0.07585 -0.10879 38  GLU B CD  
2259 O OE1 . GLU B 38  ? 1.53407 1.49630 1.56987 -0.01669 -0.08664 -0.11284 38  GLU B OE1 
2260 O OE2 . GLU B 38  ? 1.55489 1.50921 1.59129 -0.02013 -0.06713 -0.10626 38  GLU B OE2 
2261 N N   . GLU B 39  ? 1.79218 1.70113 1.77710 -0.03385 -0.09255 -0.12033 39  GLU B N   
2262 C CA  . GLU B 39  ? 1.50459 1.41381 1.48926 -0.03299 -0.10166 -0.13002 39  GLU B CA  
2263 C C   . GLU B 39  ? 1.22346 1.11876 1.21110 -0.04061 -0.09842 -0.12988 39  GLU B C   
2264 O O   . GLU B 39  ? 1.43725 1.32256 1.42087 -0.04508 -0.08958 -0.12060 39  GLU B O   
2265 C CB  . GLU B 39  ? 1.70489 1.61529 1.66698 -0.02267 -0.10602 -0.13070 39  GLU B CB  
2266 C CG  . GLU B 39  ? 1.67620 1.60122 1.63601 -0.01442 -0.11077 -0.12959 39  GLU B CG  
2267 C CD  . GLU B 39  ? 1.83121 1.75691 1.76766 -0.00457 -0.11247 -0.12531 39  GLU B CD  
2268 O OE1 . GLU B 39  ? 1.81322 1.74075 1.73906 -0.00116 -0.11809 -0.13215 39  GLU B OE1 
2269 O OE2 . GLU B 39  ? 1.76156 1.68607 1.69110 -0.00019 -0.10776 -0.11497 39  GLU B OE2 
2270 N N   . LYS B 40  ? 1.01402 0.90908 1.00974 -0.04194 -0.10627 -0.14065 40  LYS B N   
2271 C CA  . LYS B 40  ? 1.14358 1.02537 1.14633 -0.04852 -0.10474 -0.14159 40  LYS B CA  
2272 C C   . LYS B 40  ? 1.16010 1.03862 1.15269 -0.04259 -0.11161 -0.15245 40  LYS B C   
2273 O O   . LYS B 40  ? 1.29590 1.18424 1.29271 -0.03902 -0.12135 -0.16537 40  LYS B O   
2274 C CB  . LYS B 40  ? 0.94984 0.83378 0.98290 -0.05861 -0.10663 -0.14451 40  LYS B CB  
2275 C CG  . LYS B 40  ? 1.03592 0.90570 1.08037 -0.06571 -0.10549 -0.14402 40  LYS B CG  
2276 C CD  . LYS B 40  ? 1.15343 1.02622 1.23136 -0.07519 -0.10952 -0.14804 40  LYS B CD  
2277 C CE  . LYS B 40  ? 1.37728 1.23497 1.46908 -0.08248 -0.10778 -0.14470 40  LYS B CE  
2278 N NZ  . LYS B 40  ? 1.32167 1.18120 1.44972 -0.09234 -0.11198 -0.14743 40  LYS B NZ  
2279 N N   . ILE B 41  ? 1.27863 1.14446 1.25839 -0.04144 -0.10668 -0.14778 41  ILE B N   
2280 C CA  . ILE B 41  ? 1.31293 1.17483 1.28378 -0.03574 -0.11097 -0.15761 41  ILE B CA  
2281 C C   . ILE B 41  ? 1.27274 1.11945 1.25743 -0.04261 -0.10832 -0.15672 41  ILE B C   
2282 O O   . ILE B 41  ? 1.26750 1.10449 1.24917 -0.04654 -0.10031 -0.14338 41  ILE B O   
2283 C CB  . ILE B 41  ? 1.25841 1.12103 1.20143 -0.02622 -0.10719 -0.15169 41  ILE B CB  
2284 C CG1 . ILE B 41  ? 1.17057 1.04836 1.10207 -0.01919 -0.11036 -0.15084 41  ILE B CG1 
2285 C CG2 . ILE B 41  ? 1.18061 1.04015 1.11512 -0.02026 -0.10977 -0.16147 41  ILE B CG2 
2286 C CD1 . ILE B 41  ? 1.32429 1.20494 1.23083 -0.00947 -0.10778 -0.14492 41  ILE B CD1 
2287 N N   . THR B 42  ? 1.23023 1.07495 1.23125 -0.04408 -0.11562 -0.17092 42  THR B N   
2288 C CA  . THR B 42  ? 1.26882 1.09872 1.28751 -0.05022 -0.11429 -0.17076 42  THR B CA  
2289 C C   . THR B 42  ? 1.31986 1.14340 1.32673 -0.04231 -0.11497 -0.17905 42  THR B C   
2290 O O   . THR B 42  ? 1.40805 1.23811 1.41075 -0.03553 -0.12221 -0.19606 42  THR B O   
2291 C CB  . THR B 42  ? 1.17657 1.00643 1.22733 -0.05809 -0.12163 -0.18055 42  THR B CB  
2292 O OG1 . THR B 42  ? 1.18312 1.01898 1.24675 -0.06612 -0.11859 -0.16982 42  THR B OG1 
2293 C CG2 . THR B 42  ? 1.03889 0.85261 1.11015 -0.06339 -0.12129 -0.18103 42  THR B CG2 
2294 N N   . CYS B 43  ? 1.29033 1.10264 1.29139 -0.04284 -0.10741 -0.16719 43  CYS B N   
2295 C CA  . CYS B 43  ? 1.23742 1.04265 1.23250 -0.03630 -0.10655 -0.17315 43  CYS B CA  
2296 C C   . CYS B 43  ? 1.31700 1.10834 1.34065 -0.04263 -0.10862 -0.17709 43  CYS B C   
2297 O O   . CYS B 43  ? 1.39269 1.17548 1.43167 -0.05190 -0.10500 -0.16309 43  CYS B O   
2298 C CB  . CYS B 43  ? 1.17307 0.97481 1.14801 -0.03301 -0.09773 -0.15739 43  CYS B CB  
2299 S SG  . CYS B 43  ? 1.29224 1.10712 1.23981 -0.02797 -0.09449 -0.14801 43  CYS B SG  
2300 N N   . PHE B 44  ? 1.32111 1.11077 1.35181 -0.03724 -0.11448 -0.19604 44  PHE B N   
2301 C CA  . PHE B 44  ? 1.37515 1.15131 1.43582 -0.04157 -0.11809 -0.20394 44  PHE B CA  
2302 C C   . PHE B 44  ? 1.32240 1.08715 1.38104 -0.03784 -0.11165 -0.19704 44  PHE B C   
2303 O O   . PHE B 44  ? 1.26352 1.03215 1.29739 -0.03173 -0.10509 -0.18810 44  PHE B O   
2304 C CB  . PHE B 44  ? 1.53092 1.31174 1.59956 -0.03664 -0.12834 -0.23068 44  PHE B CB  
2305 C CG  . PHE B 44  ? 1.67342 1.44046 1.77943 -0.04253 -0.13443 -0.24155 44  PHE B CG  
2306 C CD1 . PHE B 44  ? 1.69355 1.45448 1.82978 -0.05522 -0.13641 -0.23226 44  PHE B CD1 
2307 C CD2 . PHE B 44  ? 1.66410 1.42507 1.77627 -0.03501 -0.13814 -0.26167 44  PHE B CD2 
2308 C CE1 . PHE B 44  ? 1.79565 1.54340 1.96956 -0.06095 -0.14242 -0.24120 44  PHE B CE1 
2309 C CE2 . PHE B 44  ? 1.49710 1.24403 1.64655 -0.04013 -0.14437 -0.27276 44  PHE B CE2 
2310 C CZ  . PHE B 44  ? 1.66469 1.40449 1.84604 -0.05342 -0.14683 -0.26187 44  PHE B CZ  
2311 N N   . SER B 45  ? 1.38529 1.13597 1.47285 -0.04165 -0.11383 -0.20067 45  SER B N   
2312 C CA  . SER B 45  ? 1.35924 1.09899 1.44975 -0.03809 -0.10841 -0.19421 45  SER B CA  
2313 C C   . SER B 45  ? 1.40317 1.14804 1.47645 -0.02435 -0.10779 -0.21141 45  SER B C   
2314 O O   . SER B 45  ? 1.55802 1.31066 1.62704 -0.01851 -0.11394 -0.23316 45  SER B O   
2315 C CB  . SER B 45  ? 1.28259 1.00589 1.41204 -0.04555 -0.11150 -0.19314 45  SER B CB  
2316 O OG  . SER B 45  ? 1.39411 1.11559 1.54531 -0.04601 -0.12070 -0.21524 45  SER B OG  
2317 N N   . ASN B 46  ? 1.35783 1.09986 1.42077 -0.01913 -0.10019 -0.20102 46  ASN B N   
2318 C CA  . ASN B 46  ? 1.38093 1.12895 1.42782 -0.00579 -0.09703 -0.21367 46  ASN B CA  
2319 C C   . ASN B 46  ? 1.30196 1.06897 1.31584 0.00195  -0.09717 -0.22107 46  ASN B C   
2320 O O   . ASN B 46  ? 1.26999 1.04560 1.27548 0.01099  -0.10053 -0.24226 46  ASN B O   
2321 C CB  . ASN B 46  ? 1.62802 1.36770 1.69864 -0.00131 -0.10196 -0.23657 46  ASN B CB  
2322 C CG  . ASN B 46  ? 1.66719 1.38755 1.77489 -0.00959 -0.10300 -0.22820 46  ASN B CG  
2323 O OD1 . ASN B 46  ? 1.46342 1.17614 1.59620 -0.01893 -0.10963 -0.23018 46  ASN B OD1 
2324 N ND2 . ASN B 46  ? 1.68663 1.39986 1.79960 -0.00633 -0.09655 -0.21738 46  ASN B ND2 
2325 N N   . ARG B 47  ? 1.30383 1.07774 1.29891 -0.00132 -0.09353 -0.20307 47  ARG B N   
2326 C CA  . ARG B 47  ? 1.15880 0.95011 1.12470 0.00478  -0.09349 -0.20466 47  ARG B CA  
2327 C C   . ARG B 47  ? 1.26158 1.05678 1.20718 0.00715  -0.08469 -0.18423 47  ARG B C   
2328 O O   . ARG B 47  ? 1.28927 1.07411 1.24319 0.00268  -0.07969 -0.16889 47  ARG B O   
2329 C CB  . ARG B 47  ? 1.28273 1.07908 1.25071 -0.00258 -0.09980 -0.20448 47  ARG B CB  
2330 C CG  . ARG B 47  ? 1.34420 1.13858 1.33384 -0.00589 -0.10978 -0.22446 47  ARG B CG  
2331 C CD  . ARG B 47  ? 1.51095 1.31750 1.48802 0.00489  -0.11544 -0.24839 47  ARG B CD  
2332 N NE  . ARG B 47  ? 1.65334 1.46204 1.64724 0.00089  -0.12681 -0.26650 47  ARG B NE  
2333 C CZ  . ARG B 47  ? 1.65818 1.45408 1.68333 -0.00434 -0.13257 -0.27904 47  ARG B CZ  
2334 N NH1 . ARG B 47  ? 1.69475 1.47466 1.73784 -0.00536 -0.12819 -0.27628 47  ARG B NH1 
2335 N NH2 . ARG B 47  ? 1.63967 1.43908 1.68044 -0.00853 -0.14355 -0.29465 47  ARG B NH2 
2336 N N   . LEU B 48  ? 1.27482 1.08561 1.19462 0.01445  -0.08340 -0.18400 48  LEU B N   
2337 C CA  . LEU B 48  ? 1.22360 1.03936 1.12506 0.01641  -0.07617 -0.16484 48  LEU B CA  
2338 C C   . LEU B 48  ? 1.25957 1.08318 1.14965 0.01314  -0.07877 -0.15760 48  LEU B C   
2339 O O   . LEU B 48  ? 1.27612 1.11153 1.15791 0.01707  -0.08435 -0.16900 48  LEU B O   
2340 C CB  . LEU B 48  ? 1.25896 1.08727 1.14160 0.02902  -0.07104 -0.16839 48  LEU B CB  
2341 C CG  . LEU B 48  ? 1.27740 1.10035 1.16467 0.03254  -0.06302 -0.16095 48  LEU B CG  
2342 C CD1 . LEU B 48  ? 1.11875 0.95874 0.98405 0.04477  -0.05696 -0.16101 48  LEU B CD1 
2343 C CD2 . LEU B 48  ? 1.25462 1.06650 1.14910 0.02378  -0.05925 -0.13876 48  LEU B CD2 
2344 N N   . VAL B 49  ? 1.18814 1.00575 1.07834 0.00632  -0.07515 -0.13937 49  VAL B N   
2345 C CA  . VAL B 49  ? 1.12714 0.95060 1.00903 0.00328  -0.07655 -0.13160 49  VAL B CA  
2346 C C   . VAL B 49  ? 1.12465 0.95309 0.98919 0.00769  -0.07062 -0.11644 49  VAL B C   
2347 O O   . VAL B 49  ? 1.03826 0.85970 0.90382 0.00674  -0.06515 -0.10563 49  VAL B O   
2348 C CB  . VAL B 49  ? 1.24115 1.05405 1.13883 -0.00860 -0.07737 -0.12442 49  VAL B CB  
2349 C CG1 . VAL B 49  ? 1.21079 1.03140 1.10314 -0.01072 -0.07958 -0.12145 49  VAL B CG1 
2350 C CG2 . VAL B 49  ? 1.22248 1.02773 1.14241 -0.01385 -0.08195 -0.13590 49  VAL B CG2 
2351 N N   . PHE B 50  ? 1.21249 1.05311 1.06335 0.01220  -0.07227 -0.11489 50  PHE B N   
2352 C CA  . PHE B 50  ? 1.13827 0.98418 0.97513 0.01631  -0.06750 -0.09996 50  PHE B CA  
2353 C C   . PHE B 50  ? 1.08151 0.92594 0.91996 0.01088  -0.06907 -0.09209 50  PHE B C   
2354 O O   . PHE B 50  ? 1.18781 1.04122 1.02449 0.01252  -0.07414 -0.09817 50  PHE B O   
2355 C CB  . PHE B 50  ? 1.05329 0.91641 0.87298 0.02776  -0.06765 -0.10339 50  PHE B CB  
2356 C CG  . PHE B 50  ? 1.21703 1.08352 1.03367 0.03439  -0.06480 -0.11195 50  PHE B CG  
2357 C CD1 . PHE B 50  ? 1.17619 1.04288 0.99916 0.03554  -0.06967 -0.13157 50  PHE B CD1 
2358 C CD2 . PHE B 50  ? 1.28256 1.15162 1.09255 0.03933  -0.05707 -0.10079 50  PHE B CD2 
2359 C CE1 . PHE B 50  ? 1.29590 1.16533 1.11714 0.04244  -0.06663 -0.14130 50  PHE B CE1 
2360 C CE2 . PHE B 50  ? 1.13758 1.01079 0.94593 0.04617  -0.05332 -0.10906 50  PHE B CE2 
2361 C CZ  . PHE B 50  ? 1.33920 1.21241 1.15265 0.04810  -0.05796 -0.12999 50  PHE B CZ  
2362 N N   . LEU B 51  ? 1.17755 1.01097 1.02051 0.00441  -0.06512 -0.07978 51  LEU B N   
2363 C CA  . LEU B 51  ? 1.28505 1.11579 1.12978 -0.00059 -0.06531 -0.07264 51  LEU B CA  
2364 C C   . LEU B 51  ? 1.07577 0.90811 0.91136 0.00324  -0.06172 -0.05905 51  LEU B C   
2365 O O   . LEU B 51  ? 1.16682 0.99387 1.00128 0.00311  -0.05764 -0.05060 51  LEU B O   
2366 C CB  . LEU B 51  ? 1.08070 0.89864 0.93706 -0.01105 -0.06406 -0.07014 51  LEU B CB  
2367 C CG  . LEU B 51  ? 1.11720 0.93184 0.98611 -0.01503 -0.06692 -0.08099 51  LEU B CG  
2368 C CD1 . LEU B 51  ? 1.22826 1.03257 1.10324 -0.01804 -0.06417 -0.07688 51  LEU B CD1 
2369 C CD2 . LEU B 51  ? 1.01635 0.82949 0.89679 -0.02290 -0.06899 -0.08400 51  LEU B CD2 
2370 N N   . GLU B 52  ? 1.12379 0.96384 0.95514 0.00678  -0.06361 -0.05656 52  GLU B N   
2371 C CA  . GLU B 52  ? 1.19256 1.03428 1.01816 0.01074  -0.06086 -0.04323 52  GLU B CA  
2372 C C   . GLU B 52  ? 1.20799 1.03699 1.04007 0.00348  -0.05863 -0.03549 52  GLU B C   
2373 O O   . GLU B 52  ? 1.45559 1.27797 1.29426 -0.00352 -0.05935 -0.04044 52  GLU B O   
2374 C CB  . GLU B 52  ? 1.30157 1.15652 1.12193 0.01790  -0.06422 -0.04227 52  GLU B CB  
2375 C CG  . GLU B 52  ? 1.30630 1.15912 1.13428 0.01474  -0.06652 -0.04235 52  GLU B CG  
2376 C CD  . GLU B 52  ? 1.44093 1.30712 1.26550 0.02265  -0.07007 -0.03862 52  GLU B CD  
2377 O OE1 . GLU B 52  ? 1.45551 1.33453 1.26996 0.03017  -0.07173 -0.03823 52  GLU B OE1 
2378 O OE2 . GLU B 52  ? 1.44619 1.31084 1.27824 0.02178  -0.07112 -0.03582 52  GLU B OE2 
2379 N N   . ARG B 53  ? 1.20267 1.02904 1.03312 0.00516  -0.05586 -0.02328 53  ARG B N   
2380 C CA  . ARG B 53  ? 1.23189 1.04600 1.06795 -0.00143 -0.05441 -0.01697 53  ARG B CA  
2381 C C   . ARG B 53  ? 1.27359 1.08707 1.11352 -0.00246 -0.05624 -0.01956 53  ARG B C   
2382 O O   . ARG B 53  ? 1.33541 1.15657 1.17493 0.00383  -0.05774 -0.01673 53  ARG B O   
2383 C CB  . ARG B 53  ? 1.20921 1.02136 1.04548 0.00083  -0.05189 -0.00355 53  ARG B CB  
2384 C CG  . ARG B 53  ? 1.10717 0.90608 0.94960 -0.00648 -0.05142 0.00167  53  ARG B CG  
2385 C CD  . ARG B 53  ? 0.92583 0.72352 0.77207 -0.00425 -0.04987 0.01527  53  ARG B CD  
2386 N NE  . ARG B 53  ? 1.14736 0.95270 0.99404 0.00290  -0.05025 0.02129  53  ARG B NE  
2387 C CZ  . ARG B 53  ? 1.14947 0.95043 1.00212 0.00275  -0.05216 0.02229  53  ARG B CZ  
2388 N NH1 . ARG B 53  ? 1.08600 0.87546 0.94306 -0.00398 -0.05340 0.01639  53  ARG B NH1 
2389 N NH2 . ARG B 53  ? 1.22258 1.03163 1.07692 0.00995  -0.05280 0.02940  53  ARG B NH2 
2390 N N   . GLY B 54  ? 1.29742 1.10310 1.14149 -0.00995 -0.05592 -0.02467 54  GLY B N   
2391 C CA  . GLY B 54  ? 1.13687 0.94124 0.98558 -0.01122 -0.05621 -0.02737 54  GLY B CA  
2392 C C   . GLY B 54  ? 1.20819 1.01773 1.06072 -0.01369 -0.05710 -0.03765 54  GLY B C   
2393 O O   . GLY B 54  ? 1.32836 1.13641 1.18552 -0.01608 -0.05591 -0.04063 54  GLY B O   
2394 N N   . VAL B 55  ? 1.26638 1.08209 1.11871 -0.01337 -0.05897 -0.04368 55  VAL B N   
2395 C CA  . VAL B 55  ? 1.17416 0.99595 1.03348 -0.01585 -0.06051 -0.05292 55  VAL B CA  
2396 C C   . VAL B 55  ? 1.27955 1.09403 1.14295 -0.02511 -0.05727 -0.05418 55  VAL B C   
2397 O O   . VAL B 55  ? 1.32609 1.13376 1.18800 -0.02996 -0.05620 -0.05202 55  VAL B O   
2398 C CB  . VAL B 55  ? 1.17030 0.99965 1.03006 -0.01345 -0.06434 -0.06007 55  VAL B CB  
2399 C CG1 . VAL B 55  ? 1.36144 1.20268 1.21654 -0.00406 -0.06825 -0.06047 55  VAL B CG1 
2400 C CG2 . VAL B 55  ? 1.18310 1.00588 1.03913 -0.01517 -0.06315 -0.05852 55  VAL B CG2 
2401 N N   . ASN B 56  ? 1.16473 0.98164 1.03350 -0.02722 -0.05542 -0.05692 56  ASN B N   
2402 C CA  . ASN B 56  ? 1.13549 0.94959 1.00773 -0.03563 -0.05180 -0.05827 56  ASN B CA  
2403 C C   . ASN B 56  ? 1.10138 0.92299 0.98409 -0.03863 -0.05338 -0.06437 56  ASN B C   
2404 O O   . ASN B 56  ? 1.03417 0.86555 0.92502 -0.03595 -0.05490 -0.06963 56  ASN B O   
2405 C CB  . ASN B 56  ? 1.16989 0.98448 1.04307 -0.03598 -0.04804 -0.05913 56  ASN B CB  
2406 C CG  . ASN B 56  ? 1.07888 0.89156 0.95152 -0.04426 -0.04342 -0.05911 56  ASN B CG  
2407 O OD1 . ASN B 56  ? 1.27872 1.08315 1.14309 -0.04831 -0.04214 -0.05468 56  ASN B OD1 
2408 N ND2 . ASN B 56  ? 1.17890 1.00058 1.06079 -0.04704 -0.04106 -0.06331 56  ASN B ND2 
2409 N N   . ILE B 57  ? 1.01952 0.83664 0.90440 -0.04423 -0.05357 -0.06339 57  ILE B N   
2410 C CA  . ILE B 57  ? 1.07852 0.90089 0.97622 -0.04736 -0.05605 -0.06910 57  ILE B CA  
2411 C C   . ILE B 57  ? 0.94465 0.76434 0.84924 -0.05696 -0.05216 -0.06519 57  ILE B C   
2412 O O   . ILE B 57  ? 1.05941 0.87274 0.95603 -0.06082 -0.04847 -0.05820 57  ILE B O   
2413 C CB  . ILE B 57  ? 0.92585 0.74609 0.82352 -0.04406 -0.06089 -0.07260 57  ILE B CB  
2414 C CG1 . ILE B 57  ? 1.06073 0.86982 0.95346 -0.04723 -0.05905 -0.06581 57  ILE B CG1 
2415 C CG2 . ILE B 57  ? 1.09599 0.92182 0.98499 -0.03424 -0.06425 -0.07518 57  ILE B CG2 
2416 C CD1 . ILE B 57  ? 1.05247 0.85890 0.95042 -0.04584 -0.06254 -0.07029 57  ILE B CD1 
2417 N N   . SER B 58  ? 0.90196 0.72758 0.82222 -0.06096 -0.05346 -0.06927 58  SER B N   
2418 C CA  . SER B 58  ? 0.90402 0.72814 0.83454 -0.07027 -0.05049 -0.06415 58  SER B CA  
2419 C C   . SER B 58  ? 0.96899 0.78971 0.91304 -0.07185 -0.05586 -0.06807 58  SER B C   
2420 O O   . SER B 58  ? 1.09171 0.91621 1.03996 -0.06654 -0.06144 -0.07755 58  SER B O   
2421 C CB  . SER B 58  ? 0.98065 0.81590 0.92220 -0.07442 -0.04627 -0.06447 58  SER B CB  
2422 O OG  . SER B 58  ? 1.21526 1.05308 1.14459 -0.07260 -0.04069 -0.06221 58  SER B OG  
2423 N N   . VAL B 59  ? 0.92883 0.74217 0.87911 -0.07842 -0.05481 -0.06115 59  VAL B N   
2424 C CA  . VAL B 59  ? 1.07310 0.88072 1.03776 -0.07932 -0.06001 -0.06538 59  VAL B CA  
2425 C C   . VAL B 59  ? 1.11009 0.91695 1.09537 -0.08921 -0.05863 -0.05886 59  VAL B C   
2426 O O   . VAL B 59  ? 1.21744 1.02472 1.19973 -0.09531 -0.05310 -0.04707 59  VAL B O   
2427 C CB  . VAL B 59  ? 1.06020 0.85717 1.01460 -0.07541 -0.06132 -0.06305 59  VAL B CB  
2428 C CG1 . VAL B 59  ? 1.16432 0.95636 1.13357 -0.07388 -0.06686 -0.07140 59  VAL B CG1 
2429 C CG2 . VAL B 59  ? 1.01596 0.81457 0.95012 -0.06673 -0.06115 -0.06544 59  VAL B CG2 
2430 N N   . ARG B 60  ? 1.11719 0.92382 1.12390 -0.09081 -0.06393 -0.06659 60  ARG B N   
2431 C CA  . ARG B 60  ? 1.19227 0.99530 1.22354 -0.09985 -0.06419 -0.06034 60  ARG B CA  
2432 C C   . ARG B 60  ? 1.18494 0.97546 1.22519 -0.09784 -0.06955 -0.06473 60  ARG B C   
2433 O O   . ARG B 60  ? 1.33525 1.12516 1.38249 -0.09286 -0.07595 -0.07957 60  ARG B O   
2434 C CB  . ARG B 60  ? 1.37425 1.18644 1.42976 -0.10435 -0.06660 -0.06616 60  ARG B CB  
2435 C CG  . ARG B 60  ? 1.32376 1.13185 1.40678 -0.11458 -0.06613 -0.05649 60  ARG B CG  
2436 C CD  . ARG B 60  ? 1.55754 1.37429 1.66956 -0.12014 -0.06899 -0.06138 60  ARG B CD  
2437 N NE  . ARG B 60  ? 1.76462 1.57943 1.88563 -0.11470 -0.07885 -0.08054 60  ARG B NE  
2438 C CZ  . ARG B 60  ? 1.65603 1.46062 1.79849 -0.11620 -0.08591 -0.08788 60  ARG B CZ  
2439 N NH1 . ARG B 60  ? 1.24636 1.03973 1.40366 -0.12217 -0.08443 -0.07674 60  ARG B NH1 
2440 N NH2 . ARG B 60  ? 1.61206 1.41770 1.76057 -0.11096 -0.09506 -0.10729 60  ARG B NH2 
2441 N N   . MET B 61  ? 1.09608 0.87756 1.13623 -0.10124 -0.06718 -0.05245 61  MET B N   
2442 C CA  . MET B 61  ? 1.03142 0.80073 1.08133 -0.09883 -0.07131 -0.05533 61  MET B CA  
2443 C C   . MET B 61  ? 1.01675 0.78010 1.09802 -0.10754 -0.07304 -0.04860 61  MET B C   
2444 O O   . MET B 61  ? 1.15837 0.92506 1.24637 -0.11607 -0.06881 -0.03328 61  MET B O   
2445 C CB  . MET B 61  ? 1.08794 0.85097 1.11897 -0.09579 -0.06844 -0.04580 61  MET B CB  
2446 C CG  . MET B 61  ? 1.24010 1.00922 1.24218 -0.08964 -0.06554 -0.04734 61  MET B CG  
2447 S SD  . MET B 61  ? 1.26009 1.02105 1.24615 -0.08532 -0.06425 -0.03925 61  MET B SD  
2448 C CE  . MET B 61  ? 1.17069 0.92274 1.17602 -0.08049 -0.06916 -0.04955 61  MET B CE  
2449 N N   . GLN B 62  ? 1.04889 0.80395 1.14974 -0.10510 -0.07920 -0.06024 62  GLN B N   
2450 C CA  . GLN B 62  ? 1.11868 0.86535 1.25398 -0.11245 -0.08219 -0.05564 62  GLN B CA  
2451 C C   . GLN B 62  ? 1.36392 1.09671 1.50588 -0.10756 -0.08494 -0.05803 62  GLN B C   
2452 O O   . GLN B 62  ? 1.25374 0.98334 1.39360 -0.09905 -0.08915 -0.07630 62  GLN B O   
2453 C CB  . GLN B 62  ? 1.25574 1.00573 1.41504 -0.11453 -0.08823 -0.07073 62  GLN B CB  
2454 C CG  . GLN B 62  ? 1.32915 1.06853 1.52834 -0.12090 -0.09326 -0.07072 62  GLN B CG  
2455 C CD  . GLN B 62  ? 1.45877 1.19960 1.67759 -0.11958 -0.10174 -0.09282 62  GLN B CD  
2456 O OE1 . GLN B 62  ? 1.43859 1.19222 1.65352 -0.12055 -0.10259 -0.09888 62  GLN B OE1 
2457 N NE2 . GLN B 62  ? 1.36042 1.08854 1.60116 -0.11706 -0.10852 -0.10582 62  GLN B NE2 
2458 N N   . LYS B 63  ? 1.43703 1.16299 1.58617 -0.11238 -0.08237 -0.03946 63  LYS B N   
2459 C CA  . LYS B 63  ? 1.22282 0.93600 1.38140 -0.10792 -0.08454 -0.03933 63  LYS B CA  
2460 C C   . LYS B 63  ? 1.29803 1.00027 1.49548 -0.10989 -0.09066 -0.04813 63  LYS B C   
2461 O O   . LYS B 63  ? 1.29328 0.99515 1.51669 -0.11921 -0.09200 -0.04080 63  LYS B O   
2462 C CB  . LYS B 63  ? 1.44524 1.15586 1.60052 -0.11286 -0.08082 -0.01510 63  LYS B CB  
2463 C CG  . LYS B 63  ? 1.30855 1.02257 1.43097 -0.10726 -0.07724 -0.01009 63  LYS B CG  
2464 C CD  . LYS B 63  ? 1.30742 1.01788 1.43329 -0.11262 -0.07594 0.01292  63  LYS B CD  
2465 C CE  . LYS B 63  ? 1.24897 0.96252 1.34561 -0.10804 -0.07355 0.01835  63  LYS B CE  
2466 N NZ  . LYS B 63  ? 1.36054 1.07200 1.46081 -0.11355 -0.07367 0.04064  63  LYS B NZ  
2467 N N   . GLN B 64  ? 1.37649 1.07021 1.57912 -0.10094 -0.09420 -0.06429 64  GLN B N   
2468 C CA  . GLN B 64  ? 1.38084 1.06141 1.62235 -0.10194 -0.10017 -0.07297 64  GLN B CA  
2469 C C   . GLN B 64  ? 1.35163 1.02079 1.61420 -0.10578 -0.09916 -0.05283 64  GLN B C   
2470 O O   . GLN B 64  ? 1.33355 0.99609 1.62951 -0.11465 -0.10154 -0.04186 64  GLN B O   
2471 C CB  . GLN B 64  ? 1.36510 1.04224 1.60383 -0.09005 -0.10414 -0.10043 64  GLN B CB  
2472 C CG  . GLN B 64  ? 1.36995 1.06068 1.58084 -0.08436 -0.10500 -0.11833 64  GLN B CG  
2473 C CD  . GLN B 64  ? 1.47228 1.16148 1.68158 -0.07302 -0.10952 -0.14596 64  GLN B CD  
2474 O OE1 . GLN B 64  ? 1.34942 1.04039 1.53733 -0.06296 -0.10606 -0.15062 64  GLN B OE1 
2475 N NE2 . GLN B 64  ? 1.39792 1.08478 1.63047 -0.07465 -0.11733 -0.16459 64  GLN B NE2 
2476 N N   . ILE B 65  ? 1.41413 1.08158 1.65927 -0.09931 -0.09593 -0.04663 65  ILE B N   
2477 C CA  . ILE B 65  ? 1.26641 0.92573 1.52677 -0.10246 -0.09504 -0.02499 65  ILE B CA  
2478 C C   . ILE B 65  ? 1.49771 1.16757 1.72889 -0.10715 -0.08984 -0.00283 65  ILE B C   
2479 O O   . ILE B 65  ? 1.55015 1.22863 1.74703 -0.10173 -0.08651 -0.00740 65  ILE B O   
2480 C CB  . ILE B 65  ? 1.40961 1.05969 1.67614 -0.09171 -0.09582 -0.03408 65  ILE B CB  
2481 C CG1 . ILE B 65  ? 1.43794 1.07693 1.73582 -0.08718 -0.10129 -0.05747 65  ILE B CG1 
2482 C CG2 . ILE B 65  ? 1.46177 1.10564 1.74161 -0.09468 -0.09515 -0.00961 65  ILE B CG2 
2483 C CD1 . ILE B 65  ? 1.35490 0.99729 1.63430 -0.07424 -0.10111 -0.08526 65  ILE B CD1 
2484 N N   . LEU B 66  ? 1.71518 1.38476 1.96052 -0.11722 -0.08937 0.02120  66  LEU B N   
2485 C CA  . LEU B 66  ? 1.71523 1.39659 1.93334 -0.12300 -0.08483 0.04119  66  LEU B CA  
2486 C C   . LEU B 66  ? 1.72889 1.40979 1.93049 -0.11918 -0.08397 0.05325  66  LEU B C   
2487 O O   . LEU B 66  ? 1.73604 1.42672 1.90428 -0.11862 -0.08073 0.05735  66  LEU B O   
2488 C CB  . LEU B 66  ? 1.76744 1.45138 2.00572 -0.13518 -0.08430 0.06297  66  LEU B CB  
2489 C CG  . LEU B 66  ? 1.90516 1.59628 2.15165 -0.14159 -0.08306 0.05757  66  LEU B CG  
2490 C CD1 . LEU B 66  ? 1.95381 1.63313 2.24299 -0.14286 -0.08864 0.04643  66  LEU B CD1 
2491 C CD2 . LEU B 66  ? 1.87883 1.58171 2.12135 -0.15241 -0.07841 0.08280  66  LEU B CD2 
2492 N N   . SER B 67  ? 1.56276 1.23245 1.78938 -0.11667 -0.08724 0.05910  67  SER B N   
2493 C CA  . SER B 67  ? 1.68492 1.35501 1.90100 -0.11420 -0.08730 0.07363  67  SER B CA  
2494 C C   . SER B 67  ? 1.68306 1.35781 1.86870 -0.10469 -0.08491 0.05990  67  SER B C   
2495 O O   . SER B 67  ? 1.57045 1.25083 1.73601 -0.10466 -0.08414 0.07187  67  SER B O   
2496 C CB  . SER B 67  ? 1.71469 1.37155 1.96803 -0.11201 -0.09141 0.08048  67  SER B CB  
2497 O OG  . SER B 67  ? 1.64161 1.29027 1.90488 -0.10094 -0.09203 0.05768  67  SER B OG  
2498 N N   . GLU B 68  ? 1.76918 1.44258 1.95140 -0.09682 -0.08408 0.03557  68  GLU B N   
2499 C CA  . GLU B 68  ? 1.74846 1.42656 1.90547 -0.08718 -0.08147 0.02368  68  GLU B CA  
2500 C C   . GLU B 68  ? 1.58137 1.27123 1.70393 -0.08851 -0.07831 0.01965  68  GLU B C   
2501 O O   . GLU B 68  ? 1.48300 1.17774 1.60120 -0.09612 -0.07777 0.02381  68  GLU B O   
2502 C CB  . GLU B 68  ? 1.86171 1.53419 2.03084 -0.07682 -0.08192 -0.00011 68  GLU B CB  
2503 C CG  . GLU B 68  ? 2.04531 1.70587 2.24797 -0.07273 -0.08431 0.00029  68  GLU B CG  
2504 C CD  . GLU B 68  ? 2.26317 1.92048 2.47237 -0.06101 -0.08379 -0.02576 68  GLU B CD  
2505 O OE1 . GLU B 68  ? 2.10116 1.76581 2.28955 -0.05706 -0.08244 -0.04322 68  GLU B OE1 
2506 O OE2 . GLU B 68  ? 2.48776 2.13597 2.72285 -0.05537 -0.08478 -0.02882 68  GLU B OE2 
2507 N N   . LYS B 69  ? 1.38848 1.08337 1.48813 -0.08067 -0.07585 0.01177  69  LYS B N   
2508 C CA  . LYS B 69  ? 1.32451 1.02934 1.39427 -0.08043 -0.07314 0.00654  69  LYS B CA  
2509 C C   . LYS B 69  ? 1.31466 1.02165 1.38575 -0.07786 -0.07348 -0.01277 69  LYS B C   
2510 O O   . LYS B 69  ? 1.17518 0.87620 1.26644 -0.07393 -0.07578 -0.02563 69  LYS B O   
2511 C CB  . LYS B 69  ? 1.29549 1.00478 1.34429 -0.07275 -0.07070 0.00459  69  LYS B CB  
2512 C CG  . LYS B 69  ? 1.37109 1.07910 1.42488 -0.06136 -0.06956 -0.01179 69  LYS B CG  
2513 C CD  . LYS B 69  ? 1.39050 1.10327 1.42918 -0.05478 -0.06658 -0.00810 69  LYS B CD  
2514 C CE  . LYS B 69  ? 1.45495 1.16232 1.51326 -0.05094 -0.06677 -0.00175 69  LYS B CE  
2515 N NZ  . LYS B 69  ? 1.29764 1.01141 1.34288 -0.04501 -0.06355 0.00262  69  LYS B NZ  
2516 N N   . PRO B 70  ? 1.29094 1.00668 1.34186 -0.07987 -0.07176 -0.01571 70  PRO B N   
2517 C CA  . PRO B 70  ? 1.24422 0.96388 1.29595 -0.07734 -0.07295 -0.03348 70  PRO B CA  
2518 C C   . PRO B 70  ? 1.18401 0.90590 1.22646 -0.06580 -0.07299 -0.05085 70  PRO B C   
2519 O O   . PRO B 70  ? 1.23152 0.95058 1.28860 -0.06175 -0.07598 -0.06640 70  PRO B O   
2520 C CB  . PRO B 70  ? 1.25394 0.98338 1.28518 -0.08172 -0.07044 -0.02926 70  PRO B CB  
2521 C CG  . PRO B 70  ? 1.34382 1.07279 1.37103 -0.08940 -0.06855 -0.00895 70  PRO B CG  
2522 C CD  . PRO B 70  ? 1.18061 0.90306 1.21056 -0.08559 -0.06928 -0.00253 70  PRO B CD  
2523 N N   . TYR B 71  ? 1.12869 0.85624 1.14740 -0.06047 -0.06979 -0.04828 71  TYR B N   
2524 C CA  . TYR B 71  ? 1.10624 0.83971 1.11163 -0.04967 -0.06875 -0.06241 71  TYR B CA  
2525 C C   . TYR B 71  ? 1.23661 0.97038 1.23272 -0.04418 -0.06521 -0.05447 71  TYR B C   
2526 O O   . TYR B 71  ? 1.26013 0.98957 1.25952 -0.04909 -0.06455 -0.03885 71  TYR B O   
2527 C CB  . TYR B 71  ? 1.12977 0.87357 1.11501 -0.04857 -0.06839 -0.06797 71  TYR B CB  
2528 C CG  . TYR B 71  ? 0.92991 0.67702 0.89845 -0.05351 -0.06568 -0.05391 71  TYR B CG  
2529 C CD1 . TYR B 71  ? 0.94860 0.69807 0.90082 -0.04944 -0.06269 -0.04673 71  TYR B CD1 
2530 C CD2 . TYR B 71  ? 1.02832 0.77662 0.99873 -0.06216 -0.06596 -0.04830 71  TYR B CD2 
2531 C CE1 . TYR B 71  ? 1.11983 0.87132 1.05824 -0.05390 -0.06104 -0.03594 71  TYR B CE1 
2532 C CE2 . TYR B 71  ? 1.02791 0.77949 0.98260 -0.06599 -0.06335 -0.03777 71  TYR B CE2 
2533 C CZ  . TYR B 71  ? 1.09689 0.84928 1.03575 -0.06188 -0.06138 -0.03237 71  TYR B CZ  
2534 O OH  . TYR B 71  ? 0.95015 0.70478 0.87483 -0.06569 -0.05959 -0.02383 71  TYR B OH  
2535 N N   . VAL B 72  ? 1.07662 0.81702 1.06124 -0.03395 -0.06306 -0.06474 72  VAL B N   
2536 C CA  . VAL B 72  ? 1.01298 0.75628 0.98931 -0.02788 -0.05888 -0.05772 72  VAL B CA  
2537 C C   . VAL B 72  ? 1.09087 0.84511 1.04255 -0.02332 -0.05632 -0.05822 72  VAL B C   
2538 O O   . VAL B 72  ? 1.17229 0.93423 1.11530 -0.01665 -0.05642 -0.07150 72  VAL B O   
2539 C CB  . VAL B 72  ? 1.27772 1.02005 1.26640 -0.01868 -0.05729 -0.06827 72  VAL B CB  
2540 C CG1 . VAL B 72  ? 1.43663 1.18253 1.42127 -0.01330 -0.05232 -0.05833 72  VAL B CG1 
2541 C CG2 . VAL B 72  ? 1.16988 0.90027 1.18676 -0.02283 -0.06087 -0.07057 72  VAL B CG2 
2542 N N   . ALA B 73  ? 1.03699 0.79223 0.97828 -0.02658 -0.05455 -0.04382 73  ALA B N   
2543 C CA  . ALA B 73  ? 1.06971 0.83346 0.99096 -0.02386 -0.05285 -0.04249 73  ALA B CA  
2544 C C   . ALA B 73  ? 1.23068 1.00058 1.14485 -0.01653 -0.04842 -0.03667 73  ALA B C   
2545 O O   . ALA B 73  ? 1.22284 0.98972 1.14693 -0.01587 -0.04669 -0.02966 73  ALA B O   
2546 C CB  . ALA B 73  ? 1.04722 0.80815 0.96190 -0.03284 -0.05428 -0.03225 73  ALA B CB  
2547 N N   . PHE B 74  ? 1.24659 1.02621 1.14518 -0.01077 -0.04654 -0.03889 74  PHE B N   
2548 C CA  . PHE B 74  ? 1.22446 1.01208 1.11575 -0.00405 -0.04178 -0.03142 74  PHE B CA  
2549 C C   . PHE B 74  ? 1.18640 0.97829 1.06400 -0.00512 -0.04203 -0.02501 74  PHE B C   
2550 O O   . PHE B 74  ? 1.17488 0.97374 1.04261 -0.00132 -0.04300 -0.03250 74  PHE B O   
2551 C CB  . PHE B 74  ? 1.14802 0.94623 1.03586 0.00733  -0.03821 -0.04228 74  PHE B CB  
2552 C CG  . PHE B 74  ? 1.30664 1.10003 1.20974 0.00950  -0.03822 -0.05210 74  PHE B CG  
2553 C CD1 . PHE B 74  ? 1.34614 1.13821 1.26105 0.01208  -0.03426 -0.04571 74  PHE B CD1 
2554 C CD2 . PHE B 74  ? 1.33564 1.12575 1.24394 0.00903  -0.04250 -0.06779 74  PHE B CD2 
2555 C CE1 . PHE B 74  ? 1.30644 1.09332 1.23799 0.01469  -0.03427 -0.05491 74  PHE B CE1 
2556 C CE2 . PHE B 74  ? 1.20756 0.99169 1.13296 0.01104  -0.04298 -0.07737 74  PHE B CE2 
2557 C CZ  . PHE B 74  ? 1.35318 1.13538 1.29019 0.01419  -0.03871 -0.07102 74  PHE B CZ  
2558 N N   . ARG B 75  ? 1.14249 0.93035 1.02084 -0.01005 -0.04176 -0.01158 75  ARG B N   
2559 C CA  . ARG B 75  ? 1.13200 0.92123 1.00109 -0.01182 -0.04249 -0.00543 75  ARG B CA  
2560 C C   . ARG B 75  ? 1.08712 0.88414 0.95365 -0.00592 -0.03834 0.00467  75  ARG B C   
2561 O O   . ARG B 75  ? 1.23230 1.03049 1.10663 -0.00431 -0.03541 0.01122  75  ARG B O   
2562 C CB  . ARG B 75  ? 1.17130 0.95008 1.04350 -0.02222 -0.04596 0.00099  75  ARG B CB  
2563 C CG  . ARG B 75  ? 1.12846 0.90101 1.00384 -0.02886 -0.04920 -0.00608 75  ARG B CG  
2564 C CD  . ARG B 75  ? 1.05803 0.82212 0.93687 -0.03861 -0.05188 0.00198  75  ARG B CD  
2565 N NE  . ARG B 75  ? 1.67639 1.43908 1.54750 -0.04190 -0.05291 0.00667  75  ARG B NE  
2566 C CZ  . ARG B 75  ? 1.65178 1.40942 1.52373 -0.04806 -0.05522 0.01493  75  ARG B CZ  
2567 N NH1 . ARG B 75  ? 1.37140 1.12594 1.25148 -0.05148 -0.05682 0.02156  75  ARG B NH1 
2568 N NH2 . ARG B 75  ? 1.42086 1.17674 1.28629 -0.05057 -0.05648 0.01615  75  ARG B NH2 
2569 N N   . LEU B 76  ? 1.01467 0.81785 0.87221 -0.00249 -0.03791 0.00689  76  LEU B N   
2570 C CA  . LEU B 76  ? 1.00396 0.81600 0.85998 0.00331  -0.03370 0.01808  76  LEU B CA  
2571 C C   . LEU B 76  ? 1.13351 0.93924 0.99237 -0.00221 -0.03586 0.02880  76  LEU B C   
2572 O O   . LEU B 76  ? 1.15363 0.95654 1.00769 -0.00408 -0.03894 0.02562  76  LEU B O   
2573 C CB  . LEU B 76  ? 1.14471 0.97098 0.98907 0.01302  -0.03147 0.01368  76  LEU B CB  
2574 C CG  . LEU B 76  ? 1.15578 0.99387 0.99640 0.02200  -0.02690 0.00722  76  LEU B CG  
2575 C CD1 . LEU B 76  ? 1.14938 0.98210 0.99231 0.02057  -0.02992 -0.00928 76  LEU B CD1 
2576 C CD2 . LEU B 76  ? 1.35286 1.20725 1.17964 0.03131  -0.02499 0.00710  76  LEU B CD2 
2577 N N   . ASN B 77  ? 1.22913 1.03317 1.09739 -0.00440 -0.03436 0.04096  77  ASN B N   
2578 C CA  . ASN B 77  ? 1.13192 0.92973 1.00531 -0.00943 -0.03694 0.05055  77  ASN B CA  
2579 C C   . ASN B 77  ? 1.18229 0.98868 1.05206 -0.00297 -0.03463 0.05704  77  ASN B C   
2580 O O   . ASN B 77  ? 1.33186 1.15093 1.19382 0.00555  -0.03075 0.05568  77  ASN B O   
2581 C CB  . ASN B 77  ? 1.20642 1.00129 1.09330 -0.01364 -0.03680 0.06195  77  ASN B CB  
2582 C CG  . ASN B 77  ? 1.37745 1.18534 1.26964 -0.00612 -0.02996 0.07137  77  ASN B CG  
2583 O OD1 . ASN B 77  ? 1.28937 1.10405 1.18442 -0.00265 -0.02712 0.08217  77  ASN B OD1 
2584 N ND2 . ASN B 77  ? 1.46921 1.28117 1.36407 -0.00332 -0.02687 0.06785  77  ASN B ND2 
2585 N N   . GLY B 78  ? 1.30112 1.10064 1.17697 -0.00701 -0.03755 0.06395  78  GLY B N   
2586 C CA  . GLY B 78  ? 1.43368 1.23984 1.30944 -0.00146 -0.03611 0.07214  78  GLY B CA  
2587 C C   . GLY B 78  ? 1.54697 1.36774 1.42519 0.00587  -0.02968 0.08512  78  GLY B C   
2588 O O   . GLY B 78  ? 1.35923 1.19296 1.22873 0.01411  -0.02666 0.08725  78  GLY B O   
2589 N N   . ASP B 79  ? 1.58008 1.40057 1.47047 0.00312  -0.02746 0.09474  79  ASP B N   
2590 C CA  . ASP B 79  ? 1.58886 1.42484 1.48365 0.00991  -0.02007 0.10859  79  ASP B CA  
2591 C C   . ASP B 79  ? 1.49177 1.34249 1.37228 0.01898  -0.01433 0.10072  79  ASP B C   
2592 O O   . ASP B 79  ? 1.50273 1.36987 1.37605 0.02773  -0.00882 0.10735  79  ASP B O   
2593 C CB  . ASP B 79  ? 1.62374 1.45663 1.53684 0.00452  -0.01923 0.11923  79  ASP B CB  
2594 C CG  . ASP B 79  ? 1.73248 1.56042 1.66239 0.00004  -0.02159 0.13424  79  ASP B CG  
2595 O OD1 . ASP B 79  ? 1.76836 1.60467 1.69847 0.00532  -0.01861 0.14460  79  ASP B OD1 
2596 O OD2 . ASP B 79  ? 1.83742 1.65334 1.78112 -0.00880 -0.02696 0.13584  79  ASP B OD2 
2597 N N   . MET B 80  ? 1.35439 1.20007 1.23171 0.01713  -0.01552 0.08712  80  MET B N   
2598 C CA  . MET B 80  ? 1.14198 0.99946 1.00745 0.02547  -0.01111 0.07640  80  MET B CA  
2599 C C   . MET B 80  ? 1.33294 1.19780 1.18154 0.03131  -0.01270 0.06814  80  MET B C   
2600 O O   . MET B 80  ? 1.42152 1.30329 1.25890 0.04089  -0.00784 0.06684  80  MET B O   
2601 C CB  . MET B 80  ? 1.10174 0.94905 0.97003 0.02122  -0.01386 0.06289  80  MET B CB  
2602 C CG  . MET B 80  ? 1.26750 1.12495 1.12705 0.02959  -0.00991 0.05002  80  MET B CG  
2603 S SD  . MET B 80  ? 1.88394 1.73082 1.75560 0.02556  -0.01110 0.04060  80  MET B SD  
2604 C CE  . MET B 80  ? 1.69990 1.54746 1.59042 0.02253  -0.00739 0.05958  80  MET B CE  
2605 N N   . LEU B 81  ? 1.37306 1.22657 1.21946 0.02588  -0.01965 0.06165  81  LEU B N   
2606 C CA  . LEU B 81  ? 1.35153 1.21225 1.18463 0.03093  -0.02219 0.05465  81  LEU B CA  
2607 C C   . LEU B 81  ? 1.37784 1.25321 1.20720 0.03815  -0.01882 0.06949  81  LEU B C   
2608 O O   . LEU B 81  ? 1.41880 1.30980 1.23421 0.04663  -0.01758 0.06615  81  LEU B O   
2609 C CB  . LEU B 81  ? 1.17732 1.02392 1.01243 0.02370  -0.02930 0.04774  81  LEU B CB  
2610 C CG  . LEU B 81  ? 1.08063 0.93468 0.90473 0.02844  -0.03279 0.03967  81  LEU B CG  
2611 C CD1 . LEU B 81  ? 1.22333 1.08656 1.03668 0.03352  -0.03270 0.02466  81  LEU B CD1 
2612 C CD2 . LEU B 81  ? 1.15676 0.99780 0.98532 0.02148  -0.03849 0.03354  81  LEU B CD2 
2613 N N   . ARG B 82  ? 1.48274 1.35360 1.32515 0.03471  -0.01793 0.08625  82  ARG B N   
2614 C CA  . ARG B 82  ? 1.47413 1.35828 1.31676 0.04086  -0.01463 0.10367  82  ARG B CA  
2615 C C   . ARG B 82  ? 1.55457 1.46003 1.38897 0.05008  -0.00603 0.10996  82  ARG B C   
2616 O O   . ARG B 82  ? 1.53767 1.46089 1.35999 0.05865  -0.00364 0.11573  82  ARG B O   
2617 C CB  . ARG B 82  ? 1.58049 1.45376 1.44336 0.03429  -0.01553 0.11995  82  ARG B CB  
2618 C CG  . ARG B 82  ? 1.66696 1.52910 1.53562 0.03100  -0.02217 0.12112  82  ARG B CG  
2619 C CD  . ARG B 82  ? 1.79937 1.63976 1.68288 0.02013  -0.02733 0.11741  82  ARG B CD  
2620 N NE  . ARG B 82  ? 1.87429 1.71148 1.77510 0.01573  -0.02507 0.13117  82  ARG B NE  
2621 C CZ  . ARG B 82  ? 1.80754 1.62862 1.72084 0.00633  -0.02943 0.12846  82  ARG B CZ  
2622 N NH1 . ARG B 82  ? 1.68757 1.49456 1.59672 0.00047  -0.03538 0.11309  82  ARG B NH1 
2623 N NH2 . ARG B 82  ? 1.89564 1.71610 1.82607 0.00271  -0.02785 0.14175  82  ARG B NH2 
2624 N N   . HIS B 83  ? 1.51826 1.42346 1.35939 0.04879  -0.00111 0.10964  83  HIS B N   
2625 C CA  . HIS B 83  ? 1.50683 1.43301 1.34091 0.05812  0.00832  0.11399  83  HIS B CA  
2626 C C   . HIS B 83  ? 1.51065 1.44934 1.32235 0.06669  0.00837  0.09627  83  HIS B C   
2627 O O   . HIS B 83  ? 1.57816 1.53881 1.37601 0.07663  0.01390  0.10112  83  HIS B O   
2628 C CB  . HIS B 83  ? 1.32297 1.24503 1.17105 0.05500  0.01286  0.11457  83  HIS B CB  
2629 C CG  . HIS B 83  ? 1.22404 1.13980 1.09455 0.04822  0.01386  0.13399  83  HIS B CG  
2630 N ND1 . HIS B 83  ? 1.14382 1.06327 1.02165 0.04781  0.01418  0.15289  83  HIS B ND1 
2631 C CD2 . HIS B 83  ? 1.05922 0.96556 0.94830 0.04146  0.01388  0.13764  83  HIS B CD2 
2632 C CE1 . HIS B 83  ? 1.02399 0.93584 0.92449 0.04073  0.01422  0.16627  83  HIS B CE1 
2633 N NE2 . HIS B 83  ? 1.25484 1.15924 1.16181 0.03675  0.01381  0.15725  83  HIS B NE2 
2634 N N   . LEU B 84  ? 1.44499 1.37082 1.25335 0.06287  0.00214  0.07564  84  LEU B N   
2635 C CA  . LEU B 84  ? 1.40970 1.34524 1.19953 0.06973  0.00009  0.05702  84  LEU B CA  
2636 C C   . LEU B 84  ? 1.28572 1.23313 1.06185 0.07468  -0.00355 0.06101  84  LEU B C   
2637 O O   . LEU B 84  ? 1.39074 1.35775 1.14897 0.08427  -0.00179 0.05559  84  LEU B O   
2638 C CB  . LEU B 84  ? 1.22899 1.14652 1.02251 0.06283  -0.00708 0.03707  84  LEU B CB  
2639 C CG  . LEU B 84  ? 1.00882 0.93335 0.78788 0.06823  -0.01075 0.01553  84  LEU B CG  
2640 C CD1 . LEU B 84  ? 1.16031 1.09958 0.93199 0.07759  -0.00362 0.00763  84  LEU B CD1 
2641 C CD2 . LEU B 84  ? 1.24326 1.14882 1.03047 0.05969  -0.01808 -0.00002 84  LEU B CD2 
2642 N N   . LYS B 85  ? 1.22026 1.15633 1.00478 0.06851  -0.00912 0.06962  85  LYS B N   
2643 C CA  . LYS B 85  ? 1.33159 1.27810 1.10739 0.07304  -0.01287 0.07650  85  LYS B CA  
2644 C C   . LYS B 85  ? 1.46355 1.43373 1.23079 0.08254  -0.00558 0.09432  85  LYS B C   
2645 O O   . LYS B 85  ? 1.56166 1.55106 1.31073 0.09114  -0.00653 0.09216  85  LYS B O   
2646 C CB  . LYS B 85  ? 1.16488 1.09445 0.95631 0.06517  -0.01813 0.08587  85  LYS B CB  
2647 C CG  . LYS B 85  ? 1.34104 1.28191 1.13033 0.07036  -0.01987 0.10152  85  LYS B CG  
2648 C CD  . LYS B 85  ? 1.42039 1.34535 1.23052 0.06357  -0.02200 0.11602  85  LYS B CD  
2649 C CE  . LYS B 85  ? 1.40754 1.34503 1.21954 0.06958  -0.02216 0.13631  85  LYS B CE  
2650 N NZ  . LYS B 85  ? 1.50194 1.42216 1.33647 0.06335  -0.02556 0.14773  85  LYS B NZ  
2651 N N   . ASP B 86  ? 1.50473 1.47482 1.28560 0.08084  0.00146  0.11307  86  ASP B N   
2652 C CA  . ASP B 86  ? 1.48256 1.47585 1.25845 0.08912  0.00957  0.13381  86  ASP B CA  
2653 C C   . ASP B 86  ? 1.43480 1.45138 1.18915 0.09978  0.01622  0.12410  86  ASP B C   
2654 O O   . ASP B 86  ? 1.34782 1.38835 1.08484 0.10927  0.01885  0.13168  86  ASP B O   
2655 C CB  . ASP B 86  ? 1.42588 1.41344 1.22445 0.08402  0.01586  0.15409  86  ASP B CB  
2656 C CG  . ASP B 86  ? 1.45719 1.42188 1.27730 0.07379  0.00894  0.16213  86  ASP B CG  
2657 O OD1 . ASP B 86  ? 1.55821 1.51629 1.37535 0.07278  0.00108  0.15797  86  ASP B OD1 
2658 O OD2 . ASP B 86  ? 1.44303 1.39712 1.28378 0.06705  0.01122  0.17219  86  ASP B OD2 
2659 N N   . ALA B 87  ? 1.45346 1.46394 1.20898 0.09872  0.01899  0.10740  87  ALA B N   
2660 C CA  . ALA B 87  ? 1.35617 1.38652 1.09251 0.10905  0.02481  0.09370  87  ALA B CA  
2661 C C   . ALA B 87  ? 1.28814 1.32907 1.00137 0.11501  0.01734  0.07768  87  ALA B C   
2662 O O   . ALA B 87  ? 1.41335 1.48022 1.10546 0.12588  0.02137  0.07787  87  ALA B O   
2663 C CB  . ALA B 87  ? 1.29353 1.31058 1.03908 0.10586  0.02660  0.07589  87  ALA B CB  
2664 N N   . LEU B 88  ? 1.14824 1.17072 0.86533 0.10799  0.00626  0.06414  88  LEU B N   
2665 C CA  . LEU B 88  ? 1.22497 1.25627 0.92398 0.11236  -0.00235 0.04862  88  LEU B CA  
2666 C C   . LEU B 88  ? 1.32387 1.37293 1.01233 0.11778  -0.00446 0.06658  88  LEU B C   
2667 O O   . LEU B 88  ? 1.47995 1.54656 1.14823 0.12504  -0.00941 0.05735  88  LEU B O   
2668 C CB  . LEU B 88  ? 1.39843 1.40554 1.10866 0.10255  -0.01280 0.03272  88  LEU B CB  
2669 C CG  . LEU B 88  ? 1.35715 1.34978 1.07421 0.09849  -0.01311 0.01104  88  LEU B CG  
2670 C CD1 . LEU B 88  ? 1.11228 1.08291 0.84108 0.08840  -0.02286 -0.00140 88  LEU B CD1 
2671 C CD2 . LEU B 88  ? 1.24461 1.25500 0.94333 0.10839  -0.01166 -0.00801 88  LEU B CD2 
2672 N N   . MET B 89  ? 1.16253 1.20747 0.86549 0.11434  -0.00162 0.09203  89  MET B N   
2673 C CA  . MET B 89  ? 1.35604 1.41792 1.05229 0.11975  -0.00309 0.11239  89  MET B CA  
2674 C C   . MET B 89  ? 1.40681 1.49884 1.08684 0.13061  0.00714  0.12715  89  MET B C   
2675 O O   . MET B 89  ? 1.39370 1.50676 1.06041 0.13774  0.00564  0.14065  89  MET B O   
2676 C CB  . MET B 89  ? 1.51156 1.55644 1.23266 0.11193  -0.00442 0.13397  89  MET B CB  
2677 C CG  . MET B 89  ? 1.53457 1.55266 1.27030 0.10220  -0.01423 0.12163  89  MET B CG  
2678 S SD  . MET B 89  ? 1.67550 1.69978 1.40169 0.10541  -0.02640 0.11467  89  MET B SD  
2679 C CE  . MET B 89  ? 1.47377 1.48472 1.19512 0.10054  -0.03296 0.07998  89  MET B CE  
2680 N N   . ILE B 90  ? 1.43014 1.52595 1.11144 0.13231  0.01767  0.12551  90  ILE B N   
2681 C CA  . ILE B 90  ? 1.27643 1.40364 0.93999 0.14370  0.02878  0.13607  90  ILE B CA  
2682 C C   . ILE B 90  ? 1.34815 1.49302 0.98303 0.15308  0.02732  0.10987  90  ILE B C   
2683 O O   . ILE B 90  ? 1.37094 1.54567 0.98155 0.16385  0.03012  0.11515  90  ILE B O   
2684 C CB  . ILE B 90  ? 1.25741 1.38315 0.93741 0.14208  0.04169  0.14722  90  ILE B CB  
2685 C CG1 . ILE B 90  ? 1.38914 1.50234 1.09677 0.13388  0.04304  0.17579  90  ILE B CG1 
2686 C CG2 . ILE B 90  ? 1.14757 1.30738 0.80757 0.15485  0.05465  0.15294  90  ILE B CG2 
2687 C CD1 . ILE B 90  ? 1.29608 1.40168 1.02554 0.12934  0.05251  0.18355  90  ILE B CD1 
2688 N N   . ILE B 91  ? 1.20373 1.33077 0.84144 0.14907  0.02237  0.08142  91  ILE B N   
2689 C CA  . ILE B 91  ? 1.34339 1.48489 0.95791 0.15762  0.02133  0.05415  91  ILE B CA  
2690 C C   . ILE B 91  ? 1.39409 1.54595 0.98918 0.16102  0.00871  0.04356  91  ILE B C   
2691 O O   . ILE B 91  ? 1.37614 1.55629 0.94407 0.17208  0.00943  0.03807  91  ILE B O   
2692 C CB  . ILE B 91  ? 1.19642 1.31455 0.82451 0.15193  0.02002  0.02861  91  ILE B CB  
2693 C CG1 . ILE B 91  ? 1.31652 1.43332 0.95855 0.15240  0.03367  0.03693  91  ILE B CG1 
2694 C CG2 . ILE B 91  ? 1.34377 1.47072 0.95226 0.15858  0.01434  -0.00314 91  ILE B CG2 
2695 C CD1 . ILE B 91  ? 1.12310 1.21590 0.78274 0.14626  0.03256  0.01661  91  ILE B CD1 
2696 N N   . TYR B 92  ? 1.32632 1.45727 0.93480 0.15192  -0.00303 0.04077  92  TYR B N   
2697 C CA  . TYR B 92  ? 1.49167 1.63038 1.08611 0.15408  -0.01619 0.02847  92  TYR B CA  
2698 C C   . TYR B 92  ? 1.53911 1.68789 1.13268 0.15517  -0.02049 0.05414  92  TYR B C   
2699 O O   . TYR B 92  ? 1.26970 1.42543 0.85441 0.15672  -0.03215 0.04735  92  TYR B O   
2700 C CB  . TYR B 92  ? 1.41671 1.52774 1.02747 0.14392  -0.02661 0.00639  92  TYR B CB  
2701 C CG  . TYR B 92  ? 1.32653 1.42978 0.93701 0.14386  -0.02541 -0.02186 92  TYR B CG  
2702 C CD1 . TYR B 92  ? 1.36680 1.48361 0.95883 0.15030  -0.03197 -0.04762 92  TYR B CD1 
2703 C CD2 . TYR B 92  ? 1.42085 1.50296 1.05127 0.13732  -0.01836 -0.02266 92  TYR B CD2 
2704 C CE1 . TYR B 92  ? 1.46360 1.57151 1.05899 0.15025  -0.03108 -0.07366 92  TYR B CE1 
2705 C CE2 . TYR B 92  ? 1.34471 1.41887 0.97810 0.13745  -0.01735 -0.04687 92  TYR B CE2 
2706 C CZ  . TYR B 92  ? 1.21121 1.29752 0.82802 0.14393  -0.02348 -0.07239 92  TYR B CZ  
2707 O OH  . TYR B 92  ? 1.35125 1.42789 0.97445 0.14405  -0.02272 -0.09678 92  TYR B OH  
2708 N N   . GLY B 93  ? 1.58106 1.73202 1.18492 0.15480  -0.01161 0.08379  93  GLY B N   
2709 C CA  . GLY B 93  ? 1.51274 1.67094 1.12086 0.15553  -0.01514 0.11055  93  GLY B CA  
2710 C C   . GLY B 93  ? 1.43074 1.55905 1.06943 0.14412  -0.01972 0.12024  93  GLY B C   
2711 O O   . GLY B 93  ? 1.14510 1.25032 0.79532 0.13617  -0.02674 0.10101  93  GLY B O   
2712 N N   . ARG B 103 ? 1.50918 1.45713 1.34772 0.05204  -0.10819 -0.04857 103 ARG B N   
2713 C CA  . ARG B 103 ? 1.70276 1.64328 1.56079 0.04727  -0.10686 -0.05001 103 ARG B CA  
2714 C C   . ARG B 103 ? 1.66672 1.60372 1.53424 0.03890  -0.10758 -0.06584 103 ARG B C   
2715 O O   . ARG B 103 ? 1.75764 1.68893 1.64076 0.03390  -0.10489 -0.06822 103 ARG B O   
2716 C CB  . ARG B 103 ? 1.62423 1.57929 1.49153 0.05413  -0.11358 -0.04440 103 ARG B CB  
2717 C CG  . ARG B 103 ? 1.42067 1.38038 1.28214 0.06266  -0.11356 -0.02628 103 ARG B CG  
2718 C CD  . ARG B 103 ? 1.47337 1.41371 1.34176 0.05977  -0.10464 -0.01634 103 ARG B CD  
2719 N NE  . ARG B 103 ? 1.45646 1.39891 1.32305 0.06687  -0.10405 0.00230  103 ARG B NE  
2720 C CZ  . ARG B 103 ? 1.34428 1.28794 1.22607 0.07162  -0.10589 0.01264  103 ARG B CZ  
2721 N NH1 . ARG B 103 ? 1.45574 1.40028 1.35489 0.07092  -0.10828 0.00558  103 ARG B NH1 
2722 N NH2 . ARG B 103 ? 1.17547 1.11971 1.05705 0.07735  -0.10499 0.03108  103 ARG B NH2 
2723 N N   . SER B 104 ? 1.86434 1.80471 1.72337 0.03742  -0.11065 -0.07644 104 SER B N   
2724 C CA  . SER B 104 ? 1.86952 1.80764 1.73974 0.02964  -0.11264 -0.09099 104 SER B CA  
2725 C C   . SER B 104 ? 1.91136 1.83466 1.77648 0.02358  -0.10670 -0.09462 104 SER B C   
2726 O O   . SER B 104 ? 1.93785 1.85860 1.78787 0.02722  -0.10411 -0.09060 104 SER B O   
2727 C CB  . SER B 104 ? 1.87727 1.83282 1.74737 0.03282  -0.12377 -0.10306 104 SER B CB  
2728 O OG  . SER B 104 ? 1.83895 1.80029 1.68942 0.03853  -0.12626 -0.10577 104 SER B OG  
2729 N N   . MET B 105 ? 1.89482 1.80931 1.77400 0.01442  -0.10423 -0.10102 105 MET B N   
2730 C CA  . MET B 105 ? 1.71982 1.62044 1.59746 0.00814  -0.09936 -0.10376 105 MET B CA  
2731 C C   . MET B 105 ? 1.70995 1.61469 1.57866 0.01141  -0.10406 -0.11349 105 MET B C   
2732 O O   . MET B 105 ? 1.70153 1.59661 1.56324 0.01052  -0.09959 -0.11237 105 MET B O   
2733 C CB  . MET B 105 ? 1.70749 1.60173 1.60341 -0.00195 -0.09732 -0.10860 105 MET B CB  
2734 C CG  . MET B 105 ? 1.70927 1.58848 1.60578 -0.00902 -0.09184 -0.10803 105 MET B CG  
2735 S SD  . MET B 105 ? 1.92560 1.80194 1.84523 -0.02029 -0.09194 -0.11483 105 MET B SD  
2736 C CE  . MET B 105 ? 1.69372 1.55286 1.61098 -0.02639 -0.08627 -0.11094 105 MET B CE  
2737 N N   . SER B 106 ? 1.68524 1.60486 1.55471 0.01546  -0.11331 -0.12385 106 SER B N   
2738 C CA  . SER B 106 ? 1.46635 1.39149 1.32688 0.01932  -0.11860 -0.13624 106 SER B CA  
2739 C C   . SER B 106 ? 1.47602 1.40246 1.31464 0.02732  -0.11426 -0.12927 106 SER B C   
2740 O O   . SER B 106 ? 1.58502 1.51007 1.41664 0.02928  -0.11414 -0.13793 106 SER B O   
2741 C CB  . SER B 106 ? 1.57939 1.52309 1.44159 0.02353  -0.13031 -0.14739 106 SER B CB  
2742 O OG  . SER B 106 ? 1.77689 1.73445 1.62479 0.03263  -0.13236 -0.13772 106 SER B OG  
2743 N N   . ARG B 107 ? 1.50771 1.43769 1.33700 0.03237  -0.11070 -0.11387 107 ARG B N   
2744 C CA  . ARG B 107 ? 1.56750 1.49932 1.37866 0.03933  -0.10548 -0.10417 107 ARG B CA  
2745 C C   . ARG B 107 ? 1.44066 1.35544 1.25428 0.03484  -0.09558 -0.09118 107 ARG B C   
2746 O O   . ARG B 107 ? 1.47736 1.39323 1.27975 0.03981  -0.09060 -0.07952 107 ARG B O   
2747 C CB  . ARG B 107 ? 1.72037 1.66953 1.51975 0.04869  -0.10899 -0.09442 107 ARG B CB  
2748 C CG  . ARG B 107 ? 1.68787 1.65686 1.47753 0.05514  -0.11890 -0.10737 107 ARG B CG  
2749 C CD  . ARG B 107 ? 1.62976 1.61814 1.40580 0.06500  -0.12268 -0.09585 107 ARG B CD  
2750 N NE  . ARG B 107 ? 1.90210 1.89321 1.69173 0.06404  -0.12669 -0.08798 107 ARG B NE  
2751 C CZ  . ARG B 107 ? 1.96548 1.97168 1.74932 0.07170  -0.13056 -0.07542 107 ARG B CZ  
2752 N NH1 . ARG B 107 ? 1.77358 1.79611 1.53643 0.08084  -0.13174 -0.06939 107 ARG B NH1 
2753 N NH2 . ARG B 107 ? 1.99876 2.00488 1.79891 0.07055  -0.13326 -0.06854 107 ARG B NH2 
2754 N N   . LYS B 108 ? 1.39769 1.29804 1.22607 0.02545  -0.09287 -0.09244 108 LYS B N   
2755 C CA  . LYS B 108 ? 1.31041 1.19476 1.14093 0.02028  -0.08480 -0.08255 108 LYS B CA  
2756 C C   . LYS B 108 ? 1.24350 1.11622 1.08032 0.01370  -0.08258 -0.08979 108 LYS B C   
2757 O O   . LYS B 108 ? 1.28173 1.14462 1.11610 0.01197  -0.07683 -0.08249 108 LYS B O   
2758 C CB  . LYS B 108 ? 1.22130 1.09873 1.06202 0.01520  -0.08256 -0.07540 108 LYS B CB  
2759 C CG  . LYS B 108 ? 1.25385 1.13981 1.09172 0.02179  -0.08395 -0.06595 108 LYS B CG  
2760 C CD  . LYS B 108 ? 1.51025 1.38671 1.35840 0.01723  -0.08026 -0.05963 108 LYS B CD  
2761 C CE  . LYS B 108 ? 1.44780 1.33082 1.29695 0.02402  -0.08167 -0.04989 108 LYS B CE  
2762 N NZ  . LYS B 108 ? 1.54163 1.41408 1.40154 0.02000  -0.07764 -0.04595 108 LYS B NZ  
2763 N N   . ILE B 109 ? 1.19855 1.07228 1.04568 0.00983  -0.08744 -0.10319 109 ILE B N   
2764 C CA  . ILE B 109 ? 1.15490 1.01818 1.01128 0.00400  -0.08653 -0.11051 109 ILE B CA  
2765 C C   . ILE B 109 ? 1.28439 1.15657 1.13907 0.00900  -0.09292 -0.12642 109 ILE B C   
2766 O O   . ILE B 109 ? 1.41989 1.30075 1.28122 0.00871  -0.10022 -0.13672 109 ILE B O   
2767 C CB  . ILE B 109 ? 1.22953 1.08489 1.10401 -0.00640 -0.08649 -0.11168 109 ILE B CB  
2768 C CG1 . ILE B 109 ? 1.26542 1.11529 1.13954 -0.01022 -0.08093 -0.09854 109 ILE B CG1 
2769 C CG2 . ILE B 109 ? 1.21443 1.05806 1.10002 -0.01256 -0.08524 -0.11577 109 ILE B CG2 
2770 C CD1 . ILE B 109 ? 1.30002 1.13991 1.16562 -0.01039 -0.07473 -0.08732 109 ILE B CD1 
2771 N N   . MET B 110 ? 1.24331 1.11418 1.08998 0.01376  -0.09048 -0.12941 110 MET B N   
2772 C CA  . MET B 110 ? 1.34599 1.22648 1.18837 0.02000  -0.09628 -0.14637 110 MET B CA  
2773 C C   . MET B 110 ? 1.35061 1.21988 1.20253 0.01803  -0.09448 -0.15526 110 MET B C   
2774 O O   . MET B 110 ? 1.43001 1.29165 1.27895 0.01882  -0.08721 -0.14651 110 MET B O   
2775 C CB  . MET B 110 ? 1.47832 1.37465 1.29782 0.03154  -0.09547 -0.14349 110 MET B CB  
2776 C CG  . MET B 110 ? 1.50766 1.41856 1.31958 0.03515  -0.10052 -0.13904 110 MET B CG  
2777 S SD  . MET B 110 ? 1.65414 1.57237 1.44780 0.04264  -0.09356 -0.11758 110 MET B SD  
2778 C CE  . MET B 110 ? 1.46129 1.35743 1.26705 0.03349  -0.08447 -0.10337 110 MET B CE  
2779 N N   . THR B 111 ? 1.20244 1.07100 1.06765 0.01576  -0.10154 -0.17274 111 THR B N   
2780 C CA  . THR B 111 ? 1.29656 1.15314 1.17558 0.01369  -0.10077 -0.18221 111 THR B CA  
2781 C C   . THR B 111 ? 1.34533 1.21140 1.21704 0.02282  -0.10561 -0.20268 111 THR B C   
2782 O O   . THR B 111 ? 1.26875 1.14921 1.13247 0.02708  -0.11333 -0.21414 111 THR B O   
2783 C CB  . THR B 111 ? 1.05337 0.89775 0.95970 0.00212  -0.10441 -0.18514 111 THR B CB  
2784 O OG1 . THR B 111 ? 1.49609 1.32770 1.41807 0.00038  -0.10358 -0.19234 111 THR B OG1 
2785 C CG2 . THR B 111 ? 1.16556 1.01938 1.08053 0.00058  -0.11466 -0.19952 111 THR B CG2 
2786 N N   . THR B 112 ? 1.30929 1.16796 1.18381 0.02619  -0.10111 -0.20752 112 THR B N   
2787 C CA  . THR B 112 ? 1.45227 1.31945 1.31850 0.03615  -0.10350 -0.22740 112 THR B CA  
2788 C C   . THR B 112 ? 1.36542 1.21655 1.25387 0.03398  -0.10249 -0.23781 112 THR B C   
2789 O O   . THR B 112 ? 1.43359 1.26862 1.33951 0.02611  -0.09824 -0.22530 112 THR B O   
2790 C CB  . THR B 112 ? 1.42614 1.30749 1.26474 0.04756  -0.09588 -0.21987 112 THR B CB  
2791 O OG1 . THR B 112 ? 1.26776 1.13938 1.10811 0.04491  -0.08585 -0.19901 112 THR B OG1 
2792 C CG2 . THR B 112 ? 1.54902 1.44922 1.36601 0.05191  -0.09914 -0.21396 112 THR B CG2 
2793 N N   . GLU B 113 ? 1.54714 1.40324 1.43509 0.04139  -0.10684 -0.26119 113 GLU B N   
2794 C CA  . GLU B 113 ? 1.50628 1.34773 1.41649 0.04131  -0.10628 -0.27389 113 GLU B CA  
2795 C C   . GLU B 113 ? 1.43365 1.27766 1.33186 0.05124  -0.09563 -0.27041 113 GLU B C   
2796 O O   . GLU B 113 ? 1.54601 1.40816 1.41721 0.06204  -0.09216 -0.27317 113 GLU B O   
2797 C CB  . GLU B 113 ? 1.49783 1.34201 1.41739 0.04400  -0.11723 -0.30376 113 GLU B CB  
2798 C CG  . GLU B 113 ? 1.77002 1.61529 1.70177 0.03490  -0.12858 -0.30839 113 GLU B CG  
2799 C CD  . GLU B 113 ? 1.87428 1.70266 1.84339 0.02655  -0.13640 -0.32283 113 GLU B CD  
2800 O OE1 . GLU B 113 ? 1.75844 1.57118 1.74641 0.02628  -0.13231 -0.32476 113 GLU B OE1 
2801 O OE2 . GLU B 113 ? 1.88725 1.71826 1.86905 0.02015  -0.14687 -0.33146 113 GLU B OE2 
2802 N N   . VAL B 114 ? 1.28131 1.10835 1.20083 0.04771  -0.09045 -0.26371 114 VAL B N   
2803 C CA  . VAL B 114 ? 1.40837 1.23670 1.32144 0.05565  -0.07963 -0.25642 114 VAL B CA  
2804 C C   . VAL B 114 ? 1.49148 1.31783 1.41515 0.06447  -0.07985 -0.28092 114 VAL B C   
2805 O O   . VAL B 114 ? 1.57179 1.38245 1.52403 0.05956  -0.08584 -0.29342 114 VAL B O   
2806 C CB  . VAL B 114 ? 1.56060 1.37307 1.49027 0.04688  -0.07395 -0.23236 114 VAL B CB  
2807 C CG1 . VAL B 114 ? 1.56269 1.35541 1.52539 0.03582  -0.08039 -0.23486 114 VAL B CG1 
2808 C CG2 . VAL B 114 ? 1.58555 1.39825 1.51546 0.05474  -0.06396 -0.22692 114 VAL B CG2 
2809 N N   . ASN B 115 ? 1.63998 1.48246 1.54198 0.07765  -0.07282 -0.28724 115 ASN B N   
2810 C CA  . ASN B 115 ? 1.70295 1.54688 1.61086 0.08841  -0.07121 -0.31172 115 ASN B CA  
2811 C C   . ASN B 115 ? 1.77246 1.60541 1.69861 0.09045  -0.06126 -0.30138 115 ASN B C   
2812 O O   . ASN B 115 ? 1.85214 1.68356 1.77619 0.08662  -0.05416 -0.27517 115 ASN B O   
2813 C CB  . ASN B 115 ? 1.67588 1.54621 1.54915 0.10257  -0.06806 -0.32452 115 ASN B CB  
2814 C CG  . ASN B 115 ? 1.86591 1.73944 1.74329 0.11405  -0.06833 -0.35592 115 ASN B CG  
2815 O OD1 . ASN B 115 ? 1.90034 1.75473 1.80916 0.11141  -0.07136 -0.36868 115 ASN B OD1 
2816 N ND2 . ASN B 115 ? 1.81803 1.71628 1.66401 0.12716  -0.06515 -0.36850 115 ASN B ND2 
2817 N N   . LYS B 116 ? 2.13355 1.95843 2.07994 0.09639  -0.06159 -0.32289 116 LYS B N   
2818 C CA  . LYS B 116 ? 2.14598 1.96113 2.11293 0.09969  -0.05259 -0.31524 116 LYS B CA  
2819 C C   . LYS B 116 ? 2.22610 2.05914 2.16990 0.10856  -0.03931 -0.29906 116 LYS B C   
2820 O O   . LYS B 116 ? 2.18570 2.01191 2.14213 0.10573  -0.03242 -0.27771 116 LYS B O   
2821 C CB  . LYS B 116 ? 2.12869 1.93650 2.11727 0.10805  -0.05433 -0.34503 116 LYS B CB  
2822 C CG  . LYS B 116 ? 2.16862 1.99765 2.13129 0.12313  -0.05270 -0.37287 116 LYS B CG  
2823 C CD  . LYS B 116 ? 2.19290 2.01411 2.17906 0.13304  -0.05116 -0.40004 116 LYS B CD  
2824 C CE  . LYS B 116 ? 2.19206 2.03477 2.15174 0.14817  -0.05053 -0.43152 116 LYS B CE  
2825 N NZ  . LYS B 116 ? 2.17732 2.04805 2.09922 0.15940  -0.03756 -0.42077 116 LYS B NZ  
2826 N N   . THR B 117 ? 2.17362 2.03065 2.08454 0.11929  -0.03581 -0.30838 117 THR B N   
2827 C CA  . THR B 117 ? 2.02770 1.90391 1.91664 0.12724  -0.02297 -0.29090 117 THR B CA  
2828 C C   . THR B 117 ? 1.96104 1.83611 1.84244 0.11674  -0.02209 -0.25863 117 THR B C   
2829 O O   . THR B 117 ? 1.94910 1.82232 1.83759 0.11526  -0.01386 -0.23658 117 THR B O   
2830 C CB  . THR B 117 ? 1.79467 1.69827 1.64892 0.14039  -0.02044 -0.30709 117 THR B CB  
2831 O OG1 . THR B 117 ? 1.51708 1.42064 1.37771 0.14925  -0.02371 -0.34119 117 THR B OG1 
2832 C CG2 . THR B 117 ? 1.70201 1.62650 1.53815 0.15033  -0.00543 -0.29093 117 THR B CG2 
2833 N N   . LEU B 118 ? 1.90971 1.78581 1.77839 0.10937  -0.03104 -0.25634 118 LEU B N   
2834 C CA  . LEU B 118 ? 1.84623 1.71993 1.70922 0.09944  -0.03103 -0.22850 118 LEU B CA  
2835 C C   . LEU B 118 ? 1.83484 1.68534 1.72666 0.08758  -0.03219 -0.21325 118 LEU B C   
2836 O O   . LEU B 118 ? 1.93620 1.78490 1.82764 0.08250  -0.02764 -0.18895 118 LEU B O   
2837 C CB  . LEU B 118 ? 1.80973 1.68800 1.65788 0.09427  -0.04103 -0.23196 118 LEU B CB  
2838 C CG  . LEU B 118 ? 1.70641 1.60514 1.53043 0.10476  -0.04458 -0.25374 118 LEU B CG  
2839 C CD1 . LEU B 118 ? 1.61146 1.51194 1.42790 0.09798  -0.05628 -0.25682 118 LEU B CD1 
2840 C CD2 . LEU B 118 ? 1.62895 1.55246 1.42483 0.11667  -0.03423 -0.24519 118 LEU B CD2 
2841 N N   . LEU B 119 ? 2.21107 2.04410 2.12893 0.08312  -0.03851 -0.22695 119 LEU B N   
2842 C CA  . LEU B 119 ? 2.31085 2.12340 2.25646 0.07259  -0.03944 -0.21159 119 LEU B CA  
2843 C C   . LEU B 119 ? 2.26092 2.07326 2.21717 0.07792  -0.02963 -0.20050 119 LEU B C   
2844 O O   . LEU B 119 ? 2.22892 2.03303 2.19512 0.07024  -0.02788 -0.17804 119 LEU B O   
2845 C CB  . LEU B 119 ? 2.34584 2.14069 2.31917 0.06699  -0.04838 -0.22776 119 LEU B CB  
2846 C CG  . LEU B 119 ? 2.33397 2.10839 2.33936 0.05800  -0.04919 -0.21393 119 LEU B CG  
2847 C CD1 . LEU B 119 ? 2.24859 2.01868 2.24943 0.04562  -0.05030 -0.18765 119 LEU B CD1 
2848 C CD2 . LEU B 119 ? 2.22583 1.98471 2.25903 0.05352  -0.05802 -0.23106 119 LEU B CD2 
2849 N N   . ASP B 120 ? 1.96071 1.78285 1.91573 0.09121  -0.02335 -0.21662 120 ASP B N   
2850 C CA  . ASP B 120 ? 1.93284 1.75777 1.89869 0.09760  -0.01306 -0.20653 120 ASP B CA  
2851 C C   . ASP B 120 ? 1.88071 1.71772 1.82905 0.09616  -0.00623 -0.18051 120 ASP B C   
2852 O O   . ASP B 120 ? 1.84184 1.67331 1.80510 0.09242  -0.00235 -0.16112 120 ASP B O   
2853 C CB  . ASP B 120 ? 1.90189 1.73960 1.86466 0.11360  -0.00623 -0.22982 120 ASP B CB  
2854 C CG  . ASP B 120 ? 1.83050 1.66644 1.81582 0.11994  0.00308  -0.22388 120 ASP B CG  
2855 O OD1 . ASP B 120 ? 1.82289 1.63929 1.84069 0.11552  -0.00082 -0.22504 120 ASP B OD1 
2856 O OD2 . ASP B 120 ? 1.80071 1.65554 1.77293 0.12938  0.01436  -0.21705 120 ASP B OD2 
2857 N N   . GLU B 121 ? 1.88966 1.74340 1.80786 0.09899  -0.00535 -0.17944 121 GLU B N   
2858 C CA  . GLU B 121 ? 1.90726 1.76999 1.81164 0.09585  -0.00049 -0.15371 121 GLU B CA  
2859 C C   . GLU B 121 ? 1.84038 1.68600 1.75463 0.08059  -0.00752 -0.13549 121 GLU B C   
2860 O O   . GLU B 121 ? 1.83473 1.67912 1.75334 0.07600  -0.00405 -0.11369 121 GLU B O   
2861 C CB  . GLU B 121 ? 2.02611 1.90968 1.89818 0.10188  0.00101  -0.15542 121 GLU B CB  
2862 C CG  . GLU B 121 ? 1.93045 1.83753 1.78822 0.11558  0.01329  -0.15406 121 GLU B CG  
2863 C CD  . GLU B 121 ? 1.68820 1.59530 1.56161 0.11514  0.02242  -0.13271 121 GLU B CD  
2864 O OE1 . GLU B 121 ? 1.69607 1.60073 1.56894 0.10694  0.02206  -0.10940 121 GLU B OE1 
2865 O OE2 . GLU B 121 ? 1.70427 1.61429 1.59160 0.12322  0.02972  -0.13979 121 GLU B OE2 
2866 N N   . LEU B 122 ? 1.84327 1.67650 1.76165 0.07260  -0.01743 -0.14449 122 LEU B N   
2867 C CA  . LEU B 122 ? 1.87626 1.69452 1.80337 0.05853  -0.02359 -0.12889 122 LEU B CA  
2868 C C   . LEU B 122 ? 1.71946 1.52350 1.67250 0.05299  -0.02278 -0.11675 122 LEU B C   
2869 O O   . LEU B 122 ? 1.58696 1.38290 1.54368 0.04271  -0.02540 -0.09877 122 LEU B O   
2870 C CB  . LEU B 122 ? 1.98233 1.79170 1.91243 0.05199  -0.03339 -0.14236 122 LEU B CB  
2871 C CG  . LEU B 122 ? 1.83813 1.65712 1.74543 0.05069  -0.03758 -0.14466 122 LEU B CG  
2872 C CD1 . LEU B 122 ? 1.71782 1.52769 1.63487 0.04421  -0.04720 -0.15895 122 LEU B CD1 
2873 C CD2 . LEU B 122 ? 1.49600 1.31560 1.39332 0.04369  -0.03636 -0.12185 122 LEU B CD2 
2874 N N   . LYS B 123 ? 1.69811 1.49989 1.66907 0.06007  -0.01931 -0.12616 123 LYS B N   
2875 C CA  . LYS B 123 ? 1.75633 1.54719 1.75274 0.05640  -0.01812 -0.11296 123 LYS B CA  
2876 C C   . LYS B 123 ? 1.75652 1.55930 1.75098 0.06234  -0.00894 -0.09852 123 LYS B C   
2877 O O   . LYS B 123 ? 1.66876 1.46488 1.67930 0.05672  -0.00908 -0.08099 123 LYS B O   
2878 C CB  . LYS B 123 ? 1.74249 1.52311 1.76530 0.06086  -0.01948 -0.12954 123 LYS B CB  
2879 C CG  . LYS B 123 ? 1.71583 1.48432 1.74668 0.05549  -0.02861 -0.14541 123 LYS B CG  
2880 C CD  . LYS B 123 ? 1.73252 1.50334 1.76968 0.06684  -0.02779 -0.17348 123 LYS B CD  
2881 C CE  . LYS B 123 ? 1.61245 1.38752 1.66368 0.07818  -0.01903 -0.17598 123 LYS B CE  
2882 N NZ  . LYS B 123 ? 1.73025 1.50950 1.78452 0.09060  -0.01742 -0.20571 123 LYS B NZ  
2883 N N   . ASN B 124 ? 1.76984 1.59126 1.74544 0.07329  -0.00126 -0.10462 124 ASN B N   
2884 C CA  . ASN B 124 ? 1.64188 1.47766 1.61490 0.07905  0.00841  -0.08972 124 ASN B CA  
2885 C C   . ASN B 124 ? 1.53363 1.37475 1.48940 0.07207  0.00780  -0.06985 124 ASN B C   
2886 O O   . ASN B 124 ? 1.44091 1.29930 1.38077 0.07831  0.01486  -0.06365 124 ASN B O   
2887 C CB  . ASN B 124 ? 1.62003 1.47512 1.58174 0.09462  0.01798  -0.10485 124 ASN B CB  
2888 C CG  . ASN B 124 ? 1.79747 1.64735 1.78007 0.10277  0.01982  -0.12456 124 ASN B CG  
2889 O OD1 . ASN B 124 ? 1.63366 1.46697 1.64390 0.09759  0.01592  -0.12128 124 ASN B OD1 
2890 N ND2 . ASN B 124 ? 1.82807 1.69253 1.79787 0.11589  0.02557  -0.14523 124 ASN B ND2 
2891 N N   . ILE B 125 ? 1.55281 1.37912 1.51275 0.05907  -0.00064 -0.05964 125 ILE B N   
2892 C CA  . ILE B 125 ? 1.41995 1.24763 1.36733 0.05126  -0.00261 -0.04206 125 ILE B CA  
2893 C C   . ILE B 125 ? 1.53413 1.35556 1.49920 0.04437  -0.00311 -0.02245 125 ILE B C   
2894 O O   . ILE B 125 ? 1.48884 1.29974 1.47518 0.04153  -0.00577 -0.02179 125 ILE B O   
2895 C CB  . ILE B 125 ? 1.40447 1.22194 1.34179 0.04214  -0.01160 -0.04648 125 ILE B CB  
2896 C CG1 . ILE B 125 ? 1.44954 1.24946 1.40599 0.03468  -0.01852 -0.05148 125 ILE B CG1 
2897 C CG2 . ILE B 125 ? 1.25983 1.08727 1.17753 0.04906  -0.01152 -0.06303 125 ILE B CG2 
2898 C CD1 . ILE B 125 ? 1.31068 1.09912 1.27825 0.02291  -0.02313 -0.03340 125 ILE B CD1 
2899 N N   . ASN B 126 ? 1.42713 1.25516 1.38489 0.04151  -0.00127 -0.00596 126 ASN B N   
2900 C CA  . ASN B 126 ? 1.54272 1.36579 1.51646 0.03422  -0.00318 0.01241  126 ASN B CA  
2901 C C   . ASN B 126 ? 1.60692 1.43140 1.56914 0.02732  -0.00555 0.02644  126 ASN B C   
2902 O O   . ASN B 126 ? 1.64308 1.47964 1.59139 0.03249  -0.00056 0.02843  126 ASN B O   
2903 C CB  . ASN B 126 ? 1.65357 1.48755 1.64406 0.04241  0.00518  0.01831  126 ASN B CB  
2904 C CG  . ASN B 126 ? 1.71694 1.55343 1.71820 0.03654  0.00482  0.03964  126 ASN B CG  
2905 O OD1 . ASN B 126 ? 1.84363 1.69461 1.84304 0.04146  0.01209  0.04864  126 ASN B OD1 
2906 N ND2 . ASN B 126 ? 1.75337 1.57660 1.76630 0.02576  -0.00399 0.04821  126 ASN B ND2 
2907 N N   . SER B 127 ? 1.63754 1.44985 1.60588 0.01582  -0.01344 0.03588  127 SER B N   
2908 C CA  . SER B 127 ? 1.68002 1.49071 1.64084 0.00808  -0.01720 0.04796  127 SER B CA  
2909 C C   . SER B 127 ? 1.60206 1.42064 1.57499 0.00810  -0.01408 0.06452  127 SER B C   
2910 O O   . SER B 127 ? 1.44032 1.25274 1.41818 -0.00108 -0.02023 0.07543  127 SER B O   
2911 C CB  . SER B 127 ? 1.60915 1.40490 1.57042 -0.00379 -0.02688 0.04931  127 SER B CB  
2912 O OG  . SER B 127 ? 1.63995 1.42997 1.58947 -0.00471 -0.02946 0.03591  127 SER B OG  
2913 N N   . HIS B 128 ? 1.82447 1.65741 1.80310 0.01810  -0.00471 0.06651  128 HIS B N   
2914 C CA  . HIS B 128 ? 1.99415 1.83680 1.98581 0.01824  -0.00084 0.08341  128 HIS B CA  
2915 C C   . HIS B 128 ? 2.04385 1.90433 2.02616 0.02816  0.00955  0.08580  128 HIS B C   
2916 O O   . HIS B 128 ? 2.02736 1.89246 2.00723 0.02560  0.01007  0.09791  128 HIS B O   
2917 C CB  . HIS B 128 ? 2.03875 1.88344 2.05521 0.01979  0.00080  0.08882  128 HIS B CB  
2918 C CG  . HIS B 128 ? 2.08223 1.94107 2.11466 0.02245  0.00713  0.10490  128 HIS B CG  
2919 N ND1 . HIS B 128 ? 2.08320 1.94329 2.11762 0.01559  0.00420  0.11933  128 HIS B ND1 
2920 C CD2 . HIS B 128 ? 2.05469 1.92744 2.10404 0.03122  0.01643  0.10883  128 HIS B CD2 
2921 C CE1 . HIS B 128 ? 2.03726 1.91164 2.08990 0.01941  0.01119  0.13252  128 HIS B CE1 
2922 N NE2 . HIS B 128 ? 2.05363 1.93668 2.11509 0.02912  0.01915  0.12666  128 HIS B NE2 
2923 N N   . ASP B 129 ? 2.05057 1.92155 2.02800 0.03963  0.01771  0.07436  129 ASP B N   
2924 C CA  . ASP B 129 ? 1.84596 1.73673 1.81147 0.05029  0.02823  0.07571  129 ASP B CA  
2925 C C   . ASP B 129 ? 1.71626 1.60560 1.65651 0.05037  0.02491  0.06751  129 ASP B C   
2926 O O   . ASP B 129 ? 1.74173 1.63255 1.66771 0.05635  0.02532  0.05021  129 ASP B O   
2927 C CB  . ASP B 129 ? 1.75304 1.65641 1.72187 0.06295  0.03792  0.06462  129 ASP B CB  
2928 C CG  . ASP B 129 ? 1.83104 1.75905 1.79185 0.07408  0.05064  0.07094  129 ASP B CG  
2929 O OD1 . ASP B 129 ? 1.78719 1.72233 1.72797 0.07553  0.05130  0.07314  129 ASP B OD1 
2930 O OD2 . ASP B 129 ? 1.99948 1.94080 1.97477 0.08160  0.06025  0.07468  129 ASP B OD2 
2931 N N   . ASN B 130 ? 1.63312 1.51925 1.56981 0.04344  0.02085  0.07994  130 ASN B N   
2932 C CA  . ASN B 130 ? 1.57629 1.46224 1.49182 0.04373  0.01778  0.07493  130 ASN B CA  
2933 C C   . ASN B 130 ? 1.57333 1.48000 1.47254 0.05650  0.02675  0.07086  130 ASN B C   
2934 O O   . ASN B 130 ? 1.49577 1.40392 1.37613 0.05994  0.02426  0.05811  130 ASN B O   
2935 C CB  . ASN B 130 ? 1.41018 1.29113 1.32896 0.03573  0.01350  0.09080  130 ASN B CB  
2936 C CG  . ASN B 130 ? 1.47137 1.33474 1.40559 0.02361  0.00494  0.09535  130 ASN B CG  
2937 O OD1 . ASN B 130 ? 1.37756 1.22859 1.31272 0.01918  -0.00079 0.08453  130 ASN B OD1 
2938 N ND2 . ASN B 130 ? 1.44048 1.30330 1.38761 0.01807  0.00369  0.11178  130 ASN B ND2 
2939 N N   . SER B 131 ? 1.65055 1.57489 1.55677 0.06358  0.03715  0.08233  131 SER B N   
2940 C CA  . SER B 131 ? 1.38623 1.33352 1.27628 0.07681  0.04711  0.07865  131 SER B CA  
2941 C C   . SER B 131 ? 1.32841 1.27582 1.20663 0.08394  0.04685  0.05348  131 SER B C   
2942 O O   . SER B 131 ? 1.47200 1.42799 1.32822 0.09010  0.04642  0.04240  131 SER B O   
2943 C CB  . SER B 131 ? 1.42672 1.39245 1.33085 0.08285  0.05925  0.09406  131 SER B CB  
2944 O OG  . SER B 131 ? 1.37424 1.34461 1.28618 0.07817  0.06042  0.11756  131 SER B OG  
2945 N N   . ALA B 132 ? 1.41130 1.34932 1.30555 0.08318  0.04644  0.04422  132 ALA B N   
2946 C CA  . ALA B 132 ? 1.26174 1.19832 1.14941 0.08982  0.04593  0.01980  132 ALA B CA  
2947 C C   . ALA B 132 ? 1.51500 1.43704 1.38989 0.08405  0.03460  0.00554  132 ALA B C   
2948 O O   . ALA B 132 ? 1.56657 1.49484 1.42561 0.09102  0.03406  -0.01273 132 ALA B O   
2949 C CB  . ALA B 132 ? 0.99768 0.92446 0.90974 0.08901  0.04660  0.01510  132 ALA B CB  
2950 N N   . PHE B 133 ? 1.38319 1.28692 1.26500 0.07145  0.02543  0.01306  133 PHE B N   
2951 C CA  . PHE B 133 ? 1.30378 1.19476 1.17561 0.06562  0.01545  0.00084  133 PHE B CA  
2952 C C   . PHE B 133 ? 1.35673 1.25983 1.20558 0.06994  0.01492  -0.00041 133 PHE B C   
2953 O O   . PHE B 133 ? 1.44470 1.34856 1.28119 0.07275  0.01061  -0.01757 133 PHE B O   
2954 C CB  . PHE B 133 ? 1.49054 1.36170 1.37380 0.05186  0.00702  0.00974  133 PHE B CB  
2955 C CG  . PHE B 133 ? 1.56103 1.41914 1.43816 0.04574  -0.00214 -0.00328 133 PHE B CG  
2956 C CD1 . PHE B 133 ? 1.51197 1.36001 1.39775 0.04449  -0.00571 -0.01821 133 PHE B CD1 
2957 C CD2 . PHE B 133 ? 1.47232 1.32869 1.33743 0.04138  -0.00694 -0.00004 133 PHE B CD2 
2958 C CE1 . PHE B 133 ? 1.41784 1.25526 1.30021 0.03847  -0.01365 -0.02884 133 PHE B CE1 
2959 C CE2 . PHE B 133 ? 1.48928 1.33553 1.35042 0.03598  -0.01456 -0.01148 133 PHE B CE2 
2960 C CZ  . PHE B 133 ? 1.36246 1.19972 1.23217 0.03426  -0.01777 -0.02547 133 PHE B CZ  
2961 N N   . ILE B 134 ? 1.31483 1.22663 1.15979 0.06970  0.01805  0.01832  134 ILE B N   
2962 C CA  . ILE B 134 ? 1.37390 1.29870 1.19847 0.07454  0.01760  0.01962  134 ILE B CA  
2963 C C   . ILE B 134 ? 1.20859 1.15409 1.01632 0.08786  0.02364  0.00667  134 ILE B C   
2964 O O   . ILE B 134 ? 1.25927 1.21110 1.04926 0.09162  0.01920  -0.00507 134 ILE B O   
2965 C CB  . ILE B 134 ? 1.30028 1.23106 1.12755 0.07244  0.02057  0.04396  134 ILE B CB  
2966 C CG1 . ILE B 134 ? 1.29305 1.23599 1.10124 0.07698  0.01887  0.04685  134 ILE B CG1 
2967 C CG2 . ILE B 134 ? 1.38861 1.33460 1.22429 0.07828  0.03176  0.05811  134 ILE B CG2 
2968 C CD1 . ILE B 134 ? 1.38245 1.33312 1.19489 0.07639  0.02253  0.07165  134 ILE B CD1 
2969 N N   . SER B 135 ? 1.20611 1.16351 1.01917 0.09546  0.03365  0.00785  135 SER B N   
2970 C CA  . SER B 135 ? 1.21290 1.18995 1.00962 0.10870  0.03971  -0.00776 135 SER B CA  
2971 C C   . SER B 135 ? 1.35036 1.31715 1.14305 0.10897  0.03169  -0.03527 135 SER B C   
2972 O O   . SER B 135 ? 1.35903 1.33858 1.13149 0.11645  0.02994  -0.05003 135 SER B O   
2973 C CB  . SER B 135 ? 1.25753 1.24673 1.06491 0.11643  0.05212  -0.00405 135 SER B CB  
2974 O OG  . SER B 135 ? 1.44982 1.44642 1.26711 0.11437  0.05896  0.02242  135 SER B OG  
2975 N N   . SER B 136 ? 1.24302 1.18768 1.05590 0.10093  0.02648  -0.04213 136 SER B N   
2976 C CA  . SER B 136 ? 1.23213 1.16598 1.04613 0.10046  0.01895  -0.06702 136 SER B CA  
2977 C C   . SER B 136 ? 1.16667 1.09624 0.96761 0.09537  0.00848  -0.07306 136 SER B C   
2978 O O   . SER B 136 ? 1.16745 1.10005 0.95910 0.09934  0.00342  -0.09399 136 SER B O   
2979 C CB  . SER B 136 ? 1.26023 1.17164 1.10070 0.09213  0.01565  -0.06867 136 SER B CB  
2980 O OG  . SER B 136 ? 1.34624 1.26153 1.20165 0.09570  0.02472  -0.05893 136 SER B OG  
2981 N N   . LEU B 137 ? 1.08864 1.01128 0.89033 0.08666  0.00479  -0.05573 137 LEU B N   
2982 C CA  . LEU B 137 ? 1.19390 1.11531 0.98374 0.08304  -0.00402 -0.05965 137 LEU B CA  
2983 C C   . LEU B 137 ? 1.20662 1.15178 0.97233 0.09400  -0.00237 -0.06410 137 LEU B C   
2984 O O   . LEU B 137 ? 1.17183 1.12038 0.92697 0.09572  -0.00973 -0.08024 137 LEU B O   
2985 C CB  . LEU B 137 ? 1.30937 1.22083 1.10467 0.07332  -0.00687 -0.03985 137 LEU B CB  
2986 C CG  . LEU B 137 ? 1.36973 1.25880 1.18543 0.06147  -0.01010 -0.03465 137 LEU B CG  
2987 C CD1 . LEU B 137 ? 1.26742 1.15002 1.08517 0.05376  -0.01239 -0.01669 137 LEU B CD1 
2988 C CD2 . LEU B 137 ? 1.11257 0.98787 0.93495 0.05594  -0.01795 -0.05233 137 LEU B CD2 
2989 N N   . ILE B 138 ? 1.28463 1.24751 1.04192 0.10114  0.00690  -0.04848 138 ILE B N   
2990 C CA  . ILE B 138 ? 1.29094 1.27993 1.02366 0.11271  0.00985  -0.05054 138 ILE B CA  
2991 C C   . ILE B 138 ? 1.24496 1.24209 0.96748 0.12117  0.00858  -0.07839 138 ILE B C   
2992 O O   . ILE B 138 ? 1.24469 1.25340 0.94887 0.12582  0.00227  -0.09121 138 ILE B O   
2993 C CB  . ILE B 138 ? 1.17922 1.18652 0.90854 0.11934  0.02231  -0.02914 138 ILE B CB  
2994 C CG1 . ILE B 138 ? 1.16438 1.16326 0.90547 0.11072  0.02222  -0.00231 138 ILE B CG1 
2995 C CG2 . ILE B 138 ? 1.29884 1.33561 1.00109 0.13198  0.02613  -0.03086 138 ILE B CG2 
2996 C CD1 . ILE B 138 ? 1.45443 1.45625 1.18449 0.10873  0.01478  0.00538  138 ILE B CD1 
2997 N N   . TYR B 139 ? 1.15835 1.14991 0.89384 0.12358  0.01415  -0.08843 139 TYR B N   
2998 C CA  . TYR B 139 ? 1.38601 1.38421 1.11487 0.13233  0.01368  -0.11634 139 TYR B CA  
2999 C C   . TYR B 139 ? 1.31166 1.29598 1.04302 0.12647  -0.00008 -0.13735 139 TYR B C   
3000 O O   . TYR B 139 ? 1.20519 1.20235 0.91926 0.13315  -0.00518 -0.15641 139 TYR B O   
3001 C CB  . TYR B 139 ? 1.40554 1.39624 1.15430 0.13476  0.02165  -0.12169 139 TYR B CB  
3002 C CG  . TYR B 139 ? 1.43223 1.42736 1.17825 0.14404  0.02143  -0.15204 139 TYR B CG  
3003 C CD1 . TYR B 139 ? 1.39634 1.41839 1.11687 0.15794  0.02671  -0.16387 139 TYR B CD1 
3004 C CD2 . TYR B 139 ? 1.45790 1.43055 1.22740 0.13900  0.01575  -0.16895 139 TYR B CD2 
3005 C CE1 . TYR B 139 ? 1.51758 1.54334 1.23571 0.16678  0.02601  -0.19425 139 TYR B CE1 
3006 C CE2 . TYR B 139 ? 1.46195 1.43681 1.23223 0.14739  0.01492  -0.19786 139 TYR B CE2 
3007 C CZ  . TYR B 139 ? 1.61542 1.61649 1.35983 0.16136  0.01993  -0.21166 139 TYR B CZ  
3008 O OH  . TYR B 139 ? 1.58339 1.58625 1.32878 0.17001  0.01864  -0.24292 139 TYR B OH  
3009 N N   . LEU B 140 ? 1.40039 1.35955 1.15370 0.11386  -0.00633 -0.13395 140 LEU B N   
3010 C CA  . LEU B 140 ? 1.40733 1.35294 1.16708 0.10699  -0.01873 -0.15112 140 LEU B CA  
3011 C C   . LEU B 140 ? 1.40817 1.36590 1.14840 0.10736  -0.02641 -0.15093 140 LEU B C   
3012 O O   . LEU B 140 ? 1.44675 1.41056 1.17890 0.11052  -0.03436 -0.17197 140 LEU B O   
3013 C CB  . LEU B 140 ? 1.31120 1.23084 1.09603 0.09325  -0.02236 -0.14176 140 LEU B CB  
3014 C CG  . LEU B 140 ? 1.34104 1.24500 1.13846 0.08482  -0.03373 -0.15706 140 LEU B CG  
3015 C CD1 . LEU B 140 ? 1.42082 1.30260 1.24570 0.07682  -0.03366 -0.15640 140 LEU B CD1 
3016 C CD2 . LEU B 140 ? 1.36445 1.26650 1.15674 0.07697  -0.04034 -0.14640 140 LEU B CD2 
3017 N N   . ILE B 141 ? 1.39003 1.35119 1.12452 0.10406  -0.02482 -0.12742 141 ILE B N   
3018 C CA  . ILE B 141 ? 1.34885 1.32177 1.06722 0.10474  -0.03180 -0.12397 141 ILE B CA  
3019 C C   . ILE B 141 ? 1.41801 1.41737 1.11088 0.11764  -0.03196 -0.13651 141 ILE B C   
3020 O O   . ILE B 141 ? 1.51616 1.52404 1.19803 0.11886  -0.04172 -0.14731 141 ILE B O   
3021 C CB  . ILE B 141 ? 1.06416 1.03755 0.78221 0.10108  -0.02800 -0.09531 141 ILE B CB  
3022 C CG1 . ILE B 141 ? 1.14516 1.09306 0.88578 0.08782  -0.03047 -0.08661 141 ILE B CG1 
3023 C CG2 . ILE B 141 ? 1.07091 1.05979 0.77214 0.10419  -0.03403 -0.08975 141 ILE B CG2 
3024 C CD1 . ILE B 141 ? 1.15905 1.10346 0.90515 0.08418  -0.02441 -0.06030 141 ILE B CD1 
3025 N N   . SER B 142 ? 1.44951 1.46385 1.13238 0.12767  -0.02123 -0.13523 142 SER B N   
3026 C CA  . SER B 142 ? 1.48874 1.53019 1.14501 0.14073  -0.02066 -0.14865 142 SER B CA  
3027 C C   . SER B 142 ? 1.58594 1.62418 1.24255 0.14254  -0.02991 -0.18218 142 SER B C   
3028 O O   . SER B 142 ? 1.62279 1.68024 1.25792 0.14974  -0.03632 -0.19638 142 SER B O   
3029 C CB  . SER B 142 ? 1.52307 1.58152 1.17049 0.15125  -0.00575 -0.14136 142 SER B CB  
3030 O OG  . SER B 142 ? 1.55780 1.60899 1.21600 0.15469  -0.00194 -0.16249 142 SER B OG  
3031 N N   . LYS B 143 ? 1.50582 1.52063 1.18740 0.13623  -0.03112 -0.19492 143 LYS B N   
3032 C CA  . LYS B 143 ? 1.49870 1.50711 1.18714 0.13737  -0.03924 -0.22679 143 LYS B CA  
3033 C C   . LYS B 143 ? 1.52629 1.52071 1.22675 0.12675  -0.05405 -0.23568 143 LYS B C   
3034 O O   . LYS B 143 ? 1.55489 1.53370 1.27449 0.12258  -0.06047 -0.25632 143 LYS B O   
3035 C CB  . LYS B 143 ? 1.31146 1.30160 1.02446 0.13618  -0.03287 -0.23436 143 LYS B CB  
3036 C CG  . LYS B 143 ? 1.40356 1.40690 1.10972 0.14669  -0.01773 -0.22729 143 LYS B CG  
3037 C CD  . LYS B 143 ? 1.50258 1.52339 1.19368 0.16056  -0.01585 -0.25559 143 LYS B CD  
3038 C CE  . LYS B 143 ? 1.44519 1.49944 1.10270 0.17347  -0.00705 -0.24772 143 LYS B CE  
3039 N NZ  . LYS B 143 ? 1.47962 1.55026 1.12514 0.18784  -0.00131 -0.27394 143 LYS B NZ  
3040 N N   . LEU B 144 ? 1.64176 1.64203 1.33345 0.12259  -0.05966 -0.22102 144 LEU B N   
3041 C CA  . LEU B 144 ? 1.54971 1.53561 1.25720 0.11135  -0.07172 -0.22480 144 LEU B CA  
3042 C C   . LEU B 144 ? 1.69234 1.69744 1.38144 0.11472  -0.08261 -0.23154 144 LEU B C   
3043 O O   . LEU B 144 ? 1.76948 1.79432 1.43660 0.12106  -0.08005 -0.21642 144 LEU B O   
3044 C CB  . LEU B 144 ? 1.45184 1.42129 1.17430 0.10053  -0.06844 -0.19870 144 LEU B CB  
3045 C CG  . LEU B 144 ? 1.27479 1.22059 1.02189 0.09311  -0.06231 -0.19369 144 LEU B CG  
3046 C CD1 . LEU B 144 ? 1.41653 1.34712 1.17683 0.08157  -0.06240 -0.17253 144 LEU B CD1 
3047 C CD2 . LEU B 144 ? 1.39088 1.32286 1.15736 0.08998  -0.06828 -0.21800 144 LEU B CD2 
3048 N N   . GLU B 145 ? 1.85192 1.85140 1.55222 0.11007  -0.09518 -0.25287 145 GLU B N   
3049 C CA  . GLU B 145 ? 1.81628 1.83174 1.50481 0.11100  -0.10745 -0.25812 145 GLU B CA  
3050 C C   . GLU B 145 ? 1.79434 1.80423 1.49062 0.10274  -0.10880 -0.23400 145 GLU B C   
3051 O O   . GLU B 145 ? 1.83000 1.81790 1.54960 0.09214  -0.10648 -0.22494 145 GLU B O   
3052 C CB  . GLU B 145 ? 1.68892 1.69880 1.39214 0.10704  -0.12106 -0.28724 145 GLU B CB  
3053 C CG  . GLU B 145 ? 1.63945 1.65694 1.33401 0.11627  -0.12227 -0.31565 145 GLU B CG  
3054 C CD  . GLU B 145 ? 1.75749 1.75282 1.47418 0.11373  -0.11433 -0.32249 145 GLU B CD  
3055 O OE1 . GLU B 145 ? 1.91685 1.89162 1.65453 0.10428  -0.10854 -0.30428 145 GLU B OE1 
3056 O OE2 . GLU B 145 ? 1.75735 1.75642 1.47050 0.12158  -0.11408 -0.34629 145 GLU B OE2 
3057 N N   . ASN B 146 ? 1.88729 1.91813 1.56378 0.10815  -0.11258 -0.22372 146 ASN B N   
3058 C CA  . ASN B 146 ? 2.01899 2.04767 1.70136 0.10250  -0.11407 -0.20130 146 ASN B CA  
3059 C C   . ASN B 146 ? 1.99482 2.00614 1.68809 0.09726  -0.10165 -0.17800 146 ASN B C   
3060 O O   . ASN B 146 ? 2.03365 2.02736 1.74687 0.08720  -0.10203 -0.16923 146 ASN B O   
3061 C CB  . ASN B 146 ? 2.11323 2.13237 1.81703 0.09281  -0.12598 -0.21148 146 ASN B CB  
3062 C CG  . ASN B 146 ? 1.99158 2.02373 1.69132 0.09306  -0.13309 -0.19859 146 ASN B CG  
3063 O OD1 . ASN B 146 ? 1.98344 2.01099 1.68648 0.09076  -0.12737 -0.17538 146 ASN B OD1 
3064 N ND2 . ASN B 146 ? 1.99068 2.03898 1.68523 0.09580  -0.14644 -0.21452 146 ASN B ND2 
3065 N N   . ASN B 147 ? 1.81176 1.82919 1.49197 0.10426  -0.09049 -0.16843 147 ASN B N   
3066 C CA  . ASN B 147 ? 1.81210 1.81447 1.50298 0.09953  -0.07942 -0.14685 147 ASN B CA  
3067 C C   . ASN B 147 ? 1.76703 1.77319 1.45567 0.09835  -0.07827 -0.12139 147 ASN B C   
3068 O O   . ASN B 147 ? 1.74527 1.73646 1.44635 0.09237  -0.07160 -0.10433 147 ASN B O   
3069 C CB  . ASN B 147 ? 1.77676 1.78539 1.45774 0.10727  -0.06788 -0.14483 147 ASN B CB  
3070 C CG  . ASN B 147 ? 1.76639 1.80453 1.41879 0.12041  -0.06644 -0.14496 147 ASN B CG  
3071 O OD1 . ASN B 147 ? 1.80501 1.85741 1.44536 0.12384  -0.06605 -0.12602 147 ASN B OD1 
3072 N ND2 . ASN B 147 ? 1.77349 1.82157 1.41514 0.12810  -0.06603 -0.16681 147 ASN B ND2 
3073 N N   . GLU B 148 ? 1.41071 1.43696 1.08435 0.10430  -0.08500 -0.11862 148 GLU B N   
3074 C CA  . GLU B 148 ? 1.48322 1.51317 1.15744 0.10378  -0.08510 -0.09497 148 GLU B CA  
3075 C C   . GLU B 148 ? 1.57620 1.58310 1.27479 0.09214  -0.08686 -0.08944 148 GLU B C   
3076 O O   . GLU B 148 ? 1.48187 1.48136 1.18761 0.08947  -0.08178 -0.06894 148 GLU B O   
3077 C CB  . GLU B 148 ? 1.65728 1.71144 1.31534 0.11106  -0.09496 -0.09655 148 GLU B CB  
3078 C CG  . GLU B 148 ? 1.65591 1.71129 1.31863 0.10832  -0.10801 -0.12115 148 GLU B CG  
3079 C CD  . GLU B 148 ? 1.96119 2.02905 1.60820 0.11492  -0.11088 -0.14545 148 GLU B CD  
3080 O OE1 . GLU B 148 ? 2.02298 2.08904 1.66356 0.11848  -0.10110 -0.14784 148 GLU B OE1 
3081 O OE2 . GLU B 148 ? 2.11344 2.19334 1.75558 0.11674  -0.12322 -0.16292 148 GLU B OE2 
3082 N N   . LYS B 149 ? 1.63420 1.63102 1.34607 0.08537  -0.09436 -0.10757 149 LYS B N   
3083 C CA  . LYS B 149 ? 1.41949 1.39569 1.15385 0.07431  -0.09492 -0.10395 149 LYS B CA  
3084 C C   . LYS B 149 ? 1.42854 1.38621 1.17189 0.06900  -0.08441 -0.09187 149 LYS B C   
3085 O O   . LYS B 149 ? 1.52893 1.47740 1.28061 0.06477  -0.08119 -0.07579 149 LYS B O   
3086 C CB  . LYS B 149 ? 1.61208 1.58104 1.35987 0.06798  -0.10268 -0.12593 149 LYS B CB  
3087 C CG  . LYS B 149 ? 1.64698 1.63422 1.38863 0.07225  -0.11473 -0.13952 149 LYS B CG  
3088 C CD  . LYS B 149 ? 1.65947 1.63962 1.41663 0.06592  -0.12246 -0.16260 149 LYS B CD  
3089 C CE  . LYS B 149 ? 1.30955 1.28464 1.08718 0.05762  -0.12887 -0.16245 149 LYS B CE  
3090 N NZ  . LYS B 149 ? 1.44741 1.40386 1.23961 0.04949  -0.12059 -0.14712 149 LYS B NZ  
3091 N N   . ILE B 150 ? 1.31764 1.26960 1.06073 0.06922  -0.07960 -0.10050 150 ILE B N   
3092 C CA  . ILE B 150 ? 1.28506 1.22073 1.03748 0.06430  -0.07059 -0.08984 150 ILE B CA  
3093 C C   . ILE B 150 ? 1.30376 1.24512 1.04897 0.06834  -0.06362 -0.06717 150 ILE B C   
3094 O O   . ILE B 150 ? 1.46348 1.39108 1.21966 0.06213  -0.05959 -0.05340 150 ILE B O   
3095 C CB  . ILE B 150 ? 1.19161 1.12387 0.94479 0.06612  -0.06688 -0.10297 150 ILE B CB  
3096 C CG1 . ILE B 150 ? 1.24175 1.16462 1.00798 0.06046  -0.07399 -0.12390 150 ILE B CG1 
3097 C CG2 . ILE B 150 ? 1.32574 1.24401 1.08845 0.06201  -0.05803 -0.09057 150 ILE B CG2 
3098 C CD1 . ILE B 150 ? 1.55456 1.49299 1.31083 0.06690  -0.08214 -0.14370 150 ILE B CD1 
3099 N N   . ILE B 151 ? 1.23665 1.19899 0.96385 0.07866  -0.06235 -0.06279 151 ILE B N   
3100 C CA  . ILE B 151 ? 1.39666 1.36621 1.11861 0.08286  -0.05517 -0.03972 151 ILE B CA  
3101 C C   . ILE B 151 ? 1.36336 1.32737 1.09424 0.07885  -0.05827 -0.02433 151 ILE B C   
3102 O O   . ILE B 151 ? 1.31087 1.26605 1.05076 0.07574  -0.05297 -0.00675 151 ILE B O   
3103 C CB  . ILE B 151 ? 1.24267 1.23883 0.94220 0.09518  -0.05326 -0.03833 151 ILE B CB  
3104 C CG1 . ILE B 151 ? 1.05982 1.06014 0.75220 0.09953  -0.04925 -0.05557 151 ILE B CG1 
3105 C CG2 . ILE B 151 ? 1.13422 1.13904 0.83052 0.09929  -0.04521 -0.01244 151 ILE B CG2 
3106 C CD1 . ILE B 151 ? 1.31547 1.34322 0.98346 0.11195  -0.04818 -0.05998 151 ILE B CD1 
3107 N N   . GLU B 152 ? 1.39412 1.36406 1.12386 0.07936  -0.06721 -0.03101 152 GLU B N   
3108 C CA  . GLU B 152 ? 1.39465 1.35838 1.13578 0.07576  -0.07055 -0.01941 152 GLU B CA  
3109 C C   . GLU B 152 ? 1.42318 1.36249 1.18296 0.06495  -0.06807 -0.01916 152 GLU B C   
3110 O O   . GLU B 152 ? 1.39294 1.32353 1.16242 0.06215  -0.06576 -0.00449 152 GLU B O   
3111 C CB  . GLU B 152 ? 1.40150 1.37527 1.14123 0.07745  -0.08095 -0.03018 152 GLU B CB  
3112 C CG  . GLU B 152 ? 1.38778 1.38752 1.10803 0.08815  -0.08521 -0.02969 152 GLU B CG  
3113 C CD  . GLU B 152 ? 1.60677 1.61573 1.32570 0.08867  -0.09652 -0.04768 152 GLU B CD  
3114 O OE1 . GLU B 152 ? 1.65269 1.64817 1.38420 0.08099  -0.09934 -0.06380 152 GLU B OE1 
3115 O OE2 . GLU B 152 ? 1.98206 2.01240 1.68836 0.09651  -0.10290 -0.04497 152 GLU B OE2 
3116 N N   . SER B 153 ? 1.43240 1.36087 1.19801 0.05877  -0.06916 -0.03561 153 SER B N   
3117 C CA  . SER B 153 ? 1.40018 1.30744 1.18121 0.04862  -0.06660 -0.03477 153 SER B CA  
3118 C C   . SER B 153 ? 1.43245 1.33163 1.21598 0.04730  -0.05890 -0.01952 153 SER B C   
3119 O O   . SER B 153 ? 1.45593 1.34267 1.24979 0.04174  -0.05750 -0.01031 153 SER B O   
3120 C CB  . SER B 153 ? 1.36534 1.26390 1.15225 0.04280  -0.06825 -0.05218 153 SER B CB  
3121 O OG  . SER B 153 ? 1.35506 1.25610 1.14735 0.04042  -0.07550 -0.06404 153 SER B OG  
3122 N N   . ILE B 154 ? 1.17313 1.07962 0.94832 0.05235  -0.05392 -0.01768 154 ILE B N   
3123 C CA  . ILE B 154 ? 1.24741 1.14762 1.02744 0.05090  -0.04667 -0.00297 154 ILE B CA  
3124 C C   . ILE B 154 ? 1.32287 1.22645 1.10523 0.05311  -0.04537 0.01661  154 ILE B C   
3125 O O   . ILE B 154 ? 1.32473 1.21565 1.11883 0.04758  -0.04287 0.02775  154 ILE B O   
3126 C CB  . ILE B 154 ? 1.16643 1.07706 0.93787 0.05724  -0.04087 -0.00489 154 ILE B CB  
3127 C CG1 . ILE B 154 ? 1.05355 0.95430 0.83020 0.05308  -0.04126 -0.02156 154 ILE B CG1 
3128 C CG2 . ILE B 154 ? 0.97679 0.88761 0.75277 0.05800  -0.03323 0.01411  154 ILE B CG2 
3129 C CD1 . ILE B 154 ? 1.21150 1.12602 0.97716 0.06159  -0.03876 -0.03292 154 ILE B CD1 
3130 N N   . TYR B 155 ? 1.39546 1.31577 1.16814 0.06092  -0.04798 0.02101  155 TYR B N   
3131 C CA  . TYR B 155 ? 1.43614 1.35997 1.21347 0.06351  -0.04662 0.04166  155 TYR B CA  
3132 C C   . TYR B 155 ? 1.39451 1.30398 1.18627 0.05758  -0.05125 0.04332  155 TYR B C   
3133 O O   . TYR B 155 ? 1.43119 1.33223 1.23496 0.05523  -0.04929 0.05793  155 TYR B O   
3134 C CB  . TYR B 155 ? 1.61143 1.55925 1.37417 0.07419  -0.04784 0.04901  155 TYR B CB  
3135 C CG  . TYR B 155 ? 1.74804 1.69868 1.51904 0.07658  -0.04699 0.07224  155 TYR B CG  
3136 C CD1 . TYR B 155 ? 1.65810 1.61051 1.43411 0.07758  -0.03954 0.09133  155 TYR B CD1 
3137 C CD2 . TYR B 155 ? 1.79895 1.74970 1.57622 0.07748  -0.05370 0.07556  155 TYR B CD2 
3138 C CE1 . TYR B 155 ? 1.67156 1.62527 1.45881 0.07917  -0.03910 0.11336  155 TYR B CE1 
3139 C CE2 . TYR B 155 ? 1.71149 1.66321 1.49975 0.07972  -0.05326 0.09708  155 TYR B CE2 
3140 C CZ  . TYR B 155 ? 1.73312 1.68582 1.52661 0.08034  -0.04611 0.11604  155 TYR B CZ  
3141 O OH  . TYR B 155 ? 1.80927 1.76212 1.61689 0.08214  -0.04600 0.13825  155 TYR B OH  
3142 N N   . ILE B 156 ? 1.34627 1.25380 1.13838 0.05553  -0.05736 0.02853  156 ILE B N   
3143 C CA  . ILE B 156 ? 1.31596 1.21084 1.12218 0.05040  -0.06061 0.02869  156 ILE B CA  
3144 C C   . ILE B 156 ? 1.39466 1.26893 1.21129 0.04060  -0.05764 0.02534  156 ILE B C   
3145 O O   . ILE B 156 ? 1.45568 1.31810 1.28435 0.03669  -0.05776 0.03078  156 ILE B O   
3146 C CB  . ILE B 156 ? 1.27517 1.17608 1.08054 0.05113  -0.06745 0.01467  156 ILE B CB  
3147 C CG1 . ILE B 156 ? 1.31148 1.20392 1.13172 0.04861  -0.07000 0.01752  156 ILE B CG1 
3148 C CG2 . ILE B 156 ? 1.42671 1.32165 1.23084 0.04518  -0.06827 -0.00389 156 ILE B CG2 
3149 C CD1 . ILE B 156 ? 1.58154 1.47559 1.40858 0.05335  -0.06925 0.03655  156 ILE B CD1 
3150 N N   . SER B 157 ? 1.21529 1.08528 1.02791 0.03680  -0.05522 0.01658  157 SER B N   
3151 C CA  . SER B 157 ? 1.15078 1.00349 0.97183 0.02795  -0.05272 0.01572  157 SER B CA  
3152 C C   . SER B 157 ? 1.18307 1.03185 1.00894 0.02761  -0.04827 0.03120  157 SER B C   
3153 O O   . SER B 157 ? 1.19606 1.03112 1.02964 0.02029  -0.04711 0.03216  157 SER B O   
3154 C CB  . SER B 157 ? 1.17429 1.02418 0.99200 0.02424  -0.05229 0.00245  157 SER B CB  
3155 O OG  . SER B 157 ? 1.30089 1.15931 1.11148 0.02924  -0.04872 0.00449  157 SER B OG  
3156 N N   . SER B 158 ? 1.23618 1.09768 1.05840 0.03512  -0.04604 0.04405  158 SER B N   
3157 C CA  . SER B 158 ? 1.34819 1.20699 1.17872 0.03459  -0.04186 0.06100  158 SER B CA  
3158 C C   . SER B 158 ? 1.27754 1.12994 1.12087 0.03389  -0.04405 0.07265  158 SER B C   
3159 O O   . SER B 158 ? 1.18702 1.03297 1.04221 0.03127  -0.04191 0.08571  158 SER B O   
3160 C CB  . SER B 158 ? 1.26152 1.13881 1.08281 0.04297  -0.03676 0.07071  158 SER B CB  
3161 O OG  . SER B 158 ? 1.24119 1.13404 1.05574 0.05120  -0.03816 0.07840  158 SER B OG  
3162 N N   . VAL B 159 ? 1.04354 0.89661 0.88736 0.03577  -0.04863 0.06742  159 VAL B N   
3163 C CA  . VAL B 159 ? 1.25464 1.10161 1.11258 0.03626  -0.05101 0.07714  159 VAL B CA  
3164 C C   . VAL B 159 ? 1.40365 1.22991 1.27421 0.02724  -0.05212 0.07125  159 VAL B C   
3165 O O   . VAL B 159 ? 1.42170 1.24051 1.28783 0.02134  -0.05262 0.05676  159 VAL B O   
3166 C CB  . VAL B 159 ? 1.25991 1.11581 1.11513 0.04182  -0.05565 0.07233  159 VAL B CB  
3167 C CG1 . VAL B 159 ? 1.24035 1.08971 1.11285 0.04327  -0.05812 0.08243  159 VAL B CG1 
3168 C CG2 . VAL B 159 ? 1.42870 1.30680 1.26856 0.05070  -0.05567 0.07643  159 VAL B CG2 
3169 N N   . SER B 160 ? 1.34488 1.16218 1.23163 0.02611  -0.05270 0.08268  160 SER B N   
3170 C CA  . SER B 160 ? 1.24490 1.04309 1.14376 0.01822  -0.05450 0.07651  160 SER B CA  
3171 C C   . SER B 160 ? 1.40088 1.19368 1.30877 0.02002  -0.05792 0.07061  160 SER B C   
3172 O O   . SER B 160 ? 1.26879 1.06363 1.18868 0.02534  -0.05928 0.08232  160 SER B O   
3173 C CB  . SER B 160 ? 1.28238 1.07277 1.19633 0.01513  -0.05364 0.09098  160 SER B CB  
3174 O OG  . SER B 160 ? 1.53402 1.30706 1.46309 0.00980  -0.05700 0.08642  160 SER B OG  
3175 N N   . PHE B 161 ? 1.48443 1.27069 1.38826 0.01571  -0.05894 0.05344  161 PHE B N   
3176 C CA  . PHE B 161 ? 1.45096 1.23296 1.36368 0.01749  -0.06113 0.04571  161 PHE B CA  
3177 C C   . PHE B 161 ? 1.47299 1.23696 1.39850 0.01172  -0.06202 0.04076  161 PHE B C   
3178 O O   . PHE B 161 ? 1.48553 1.24057 1.41234 0.00565  -0.06186 0.04292  161 PHE B O   
3179 C CB  . PHE B 161 ? 1.43701 1.22539 1.33889 0.01688  -0.06104 0.03001  161 PHE B CB  
3180 C CG  . PHE B 161 ? 1.43565 1.24066 1.32444 0.02137  -0.06122 0.03095  161 PHE B CG  
3181 C CD1 . PHE B 161 ? 1.47737 1.29562 1.36769 0.02979  -0.06369 0.03727  161 PHE B CD1 
3182 C CD2 . PHE B 161 ? 1.43586 1.24355 1.31148 0.01743  -0.05954 0.02492  161 PHE B CD2 
3183 C CE1 . PHE B 161 ? 1.45423 1.28878 1.33118 0.03410  -0.06481 0.03625  161 PHE B CE1 
3184 C CE2 . PHE B 161 ? 1.52608 1.34853 1.39039 0.02187  -0.06019 0.02337  161 PHE B CE2 
3185 C CZ  . PHE B 161 ? 1.55948 1.39569 1.42349 0.03016  -0.06300 0.02831  161 PHE B CZ  
3186 N N   . PHE B 162 ? 1.50258 1.26190 1.43850 0.01403  -0.06331 0.03339  162 PHE B N   
3187 C CA  . PHE B 162 ? 1.42566 1.16853 1.37252 0.00933  -0.06421 0.02459  162 PHE B CA  
3188 C C   . PHE B 162 ? 1.34088 1.07930 1.27356 0.00102  -0.06269 0.01009  162 PHE B C   
3189 O O   . PHE B 162 ? 1.30511 1.03188 1.23979 -0.00537 -0.06394 0.00732  162 PHE B O   
3190 C CB  . PHE B 162 ? 1.27721 1.01823 1.23763 0.01479  -0.06496 0.01793  162 PHE B CB  
3191 C CG  . PHE B 162 ? 1.24807 0.97214 1.22320 0.01202  -0.06622 0.00982  162 PHE B CG  
3192 C CD1 . PHE B 162 ? 1.28735 0.99974 1.27759 0.01026  -0.06906 0.01970  162 PHE B CD1 
3193 C CD2 . PHE B 162 ? 1.35866 1.07894 1.33226 0.01063  -0.06444 -0.00855 162 PHE B CD2 
3194 C CE1 . PHE B 162 ? 1.32025 1.01623 1.32494 0.00750  -0.07124 0.01013  162 PHE B CE1 
3195 C CE2 . PHE B 162 ? 1.42559 1.13070 1.41117 0.00846  -0.06567 -0.01846 162 PHE B CE2 
3196 C CZ  . PHE B 162 ? 1.39672 1.08896 1.39798 0.00682  -0.06962 -0.00993 162 PHE B CZ  
3197 N N   . SER B 163 ? 1.19990 0.94810 1.11934 0.00088  -0.06051 0.00114  163 SER B N   
3198 C CA  . SER B 163 ? 1.26972 1.01583 1.17601 -0.00678 -0.05874 -0.01039 163 SER B CA  
3199 C C   . SER B 163 ? 1.26887 1.01122 1.16798 -0.01280 -0.05947 -0.00414 163 SER B C   
3200 O O   . SER B 163 ? 1.19963 0.93497 1.09329 -0.01996 -0.05978 -0.01075 163 SER B O   
3201 C CB  . SER B 163 ? 1.05849 0.81723 0.95524 -0.00563 -0.05656 -0.01722 163 SER B CB  
3202 O OG  . SER B 163 ? 1.37903 1.14859 1.27170 -0.00124 -0.05738 -0.00852 163 SER B OG  
3203 N N   . ASP B 164 ? 1.28576 1.03371 1.18531 -0.00966 -0.05974 0.00903  164 ASP B N   
3204 C CA  . ASP B 164 ? 1.25402 0.99949 1.14994 -0.01447 -0.05997 0.01606  164 ASP B CA  
3205 C C   . ASP B 164 ? 1.20194 0.93442 1.11019 -0.01863 -0.06286 0.02001  164 ASP B C   
3206 O O   . ASP B 164 ? 1.16118 0.88820 1.06669 -0.02550 -0.06429 0.01939  164 ASP B O   
3207 C CB  . ASP B 164 ? 1.31630 1.07315 1.20995 -0.00894 -0.05842 0.02867  164 ASP B CB  
3208 C CG  . ASP B 164 ? 1.36019 1.12930 1.24116 -0.00588 -0.05672 0.02274  164 ASP B CG  
3209 O OD1 . ASP B 164 ? 1.44668 1.21442 1.31992 -0.01087 -0.05625 0.01197  164 ASP B OD1 
3210 O OD2 . ASP B 164 ? 1.32556 1.10610 1.20485 0.00138  -0.05625 0.02893  164 ASP B OD2 
3211 N N   . LYS B 165 ? 1.27760 1.00512 1.20142 -0.01459 -0.06445 0.02473  165 LYS B N   
3212 C CA  . LYS B 165 ? 1.26894 0.98289 1.20782 -0.01884 -0.06811 0.02722  165 LYS B CA  
3213 C C   . LYS B 165 ? 1.12754 0.83136 1.06201 -0.02531 -0.07023 0.01016  165 LYS B C   
3214 O O   . LYS B 165 ? 1.25923 0.95515 1.19507 -0.03234 -0.07363 0.00882  165 LYS B O   
3215 C CB  . LYS B 165 ? 1.41677 1.12683 1.37610 -0.01279 -0.06953 0.03565  165 LYS B CB  
3216 C CG  . LYS B 165 ? 1.25890 0.98001 1.22325 -0.00658 -0.06766 0.05552  165 LYS B CG  
3217 C CD  . LYS B 165 ? 1.44246 1.15772 1.43084 -0.00205 -0.06987 0.06659  165 LYS B CD  
3218 C CE  . LYS B 165 ? 1.50548 1.23445 1.49734 0.00471  -0.06756 0.08799  165 LYS B CE  
3219 N NZ  . LYS B 165 ? 1.49475 1.24135 1.46372 0.00900  -0.06398 0.08688  165 LYS B NZ  
3220 N N   . VAL B 166 ? 1.17301 0.87837 1.10227 -0.02285 -0.06829 -0.00289 166 VAL B N   
3221 C CA  . VAL B 166 ? 1.26591 0.96546 1.18681 -0.02839 -0.06878 -0.01959 166 VAL B CA  
3222 C C   . VAL B 166 ? 1.21569 0.91905 1.11930 -0.03571 -0.06864 -0.02067 166 VAL B C   
3223 O O   . VAL B 166 ? 1.21312 0.90986 1.11229 -0.04250 -0.07172 -0.02739 166 VAL B O   
3224 C CB  . VAL B 166 ? 1.31965 1.02418 1.23767 -0.02378 -0.06496 -0.03178 166 VAL B CB  
3225 C CG1 . VAL B 166 ? 1.21381 0.91591 1.11998 -0.02932 -0.06393 -0.04819 166 VAL B CG1 
3226 C CG2 . VAL B 166 ? 1.15371 0.85264 1.09210 -0.01660 -0.06595 -0.03125 166 VAL B CG2 
3227 N N   . ARG B 167 ? 1.25016 0.96453 1.14430 -0.03424 -0.06558 -0.01456 167 ARG B N   
3228 C CA  . ARG B 167 ? 1.19701 0.91505 1.07768 -0.04041 -0.06535 -0.01423 167 ARG B CA  
3229 C C   . ARG B 167 ? 1.34041 1.05222 1.22565 -0.04573 -0.06960 -0.00618 167 ARG B C   
3230 O O   . ARG B 167 ? 1.34481 1.05410 1.22232 -0.05277 -0.07206 -0.01010 167 ARG B O   
3231 C CB  . ARG B 167 ? 0.96697 0.69657 0.84154 -0.03664 -0.06192 -0.00881 167 ARG B CB  
3232 C CG  . ARG B 167 ? 1.16337 0.89889 1.02523 -0.04013 -0.05949 -0.01660 167 ARG B CG  
3233 C CD  . ARG B 167 ? 1.22137 0.96748 1.08093 -0.03521 -0.05694 -0.01395 167 ARG B CD  
3234 N NE  . ARG B 167 ? 1.24126 0.99288 1.10417 -0.02939 -0.05528 -0.01933 167 ARG B NE  
3235 C CZ  . ARG B 167 ? 1.50705 1.26828 1.37058 -0.02340 -0.05457 -0.01712 167 ARG B CZ  
3236 N NH1 . ARG B 167 ? 1.49806 1.26433 1.35824 -0.02176 -0.05472 -0.01059 167 ARG B NH1 
3237 N NH2 . ARG B 167 ? 1.29653 1.06335 1.16431 -0.01868 -0.05387 -0.02233 167 ARG B NH2 
3238 N N   . ASN B 168 ? 1.58212 1.29290 1.48057 -0.04248 -0.07055 0.00630  168 ASN B N   
3239 C CA  . ASN B 168 ? 1.61858 1.32457 1.52522 -0.04748 -0.07446 0.01516  168 ASN B CA  
3240 C C   . ASN B 168 ? 1.61421 1.30796 1.52716 -0.05349 -0.08048 0.00685  168 ASN B C   
3241 O O   . ASN B 168 ? 1.63223 1.32300 1.54281 -0.06069 -0.08493 0.00624  168 ASN B O   
3242 C CB  . ASN B 168 ? 1.71094 1.42001 1.63222 -0.04232 -0.07318 0.03129  168 ASN B CB  
3243 C CG  . ASN B 168 ? 1.74487 1.44866 1.68030 -0.04750 -0.07731 0.04114  168 ASN B CG  
3244 O OD1 . ASN B 168 ? 1.73533 1.44435 1.66815 -0.05016 -0.07682 0.04788  168 ASN B OD1 
3245 N ND2 . ASN B 168 ? 1.78300 1.47643 1.73589 -0.04890 -0.08161 0.04201  168 ASN B ND2 
3246 N N   . LEU B 169 ? 1.42454 1.11124 1.34691 -0.05032 -0.08130 0.00019  169 LEU B N   
3247 C CA  . LEU B 169 ? 1.43890 1.11342 1.36762 -0.05527 -0.08723 -0.01091 169 LEU B CA  
3248 C C   . LEU B 169 ? 1.33923 1.01504 1.24799 -0.06146 -0.08850 -0.02474 169 LEU B C   
3249 O O   . LEU B 169 ? 1.23212 0.90245 1.14028 -0.06850 -0.09487 -0.02866 169 LEU B O   
3250 C CB  . LEU B 169 ? 1.25588 0.92349 1.19703 -0.04950 -0.08666 -0.01833 169 LEU B CB  
3251 C CG  . LEU B 169 ? 1.15954 0.81424 1.10671 -0.05371 -0.09252 -0.03374 169 LEU B CG  
3252 C CD1 . LEU B 169 ? 1.04243 0.68834 1.00584 -0.05985 -0.10022 -0.02624 169 LEU B CD1 
3253 C CD2 . LEU B 169 ? 1.22668 0.87464 1.18816 -0.04681 -0.09118 -0.04159 169 LEU B CD2 
3254 N N   . ILE B 170 ? 1.32381 1.00800 1.21662 -0.05907 -0.08277 -0.03153 170 ILE B N   
3255 C CA  . ILE B 170 ? 1.27012 0.95795 1.14360 -0.06473 -0.08285 -0.04213 170 ILE B CA  
3256 C C   . ILE B 170 ? 1.24495 0.93730 1.11090 -0.07078 -0.08535 -0.03249 170 ILE B C   
3257 O O   . ILE B 170 ? 1.33146 1.02396 1.18631 -0.07750 -0.08927 -0.03764 170 ILE B O   
3258 C CB  . ILE B 170 ? 1.24187 0.93865 1.10411 -0.06063 -0.07543 -0.04952 170 ILE B CB  
3259 C CG1 . ILE B 170 ? 1.14667 0.83927 1.01986 -0.05385 -0.07321 -0.05826 170 ILE B CG1 
3260 C CG2 . ILE B 170 ? 1.22818 0.93036 1.07096 -0.06642 -0.07451 -0.05886 170 ILE B CG2 
3261 C CD1 . ILE B 170 ? 1.15967 0.86153 1.02460 -0.04999 -0.06621 -0.06693 170 ILE B CD1 
3262 N N   . GLU B 171 ? 1.28894 0.98584 1.16100 -0.06809 -0.08323 -0.01846 171 GLU B N   
3263 C CA  . GLU B 171 ? 1.32352 1.02475 1.19209 -0.07258 -0.08504 -0.00875 171 GLU B CA  
3264 C C   . GLU B 171 ? 1.35209 1.04680 1.22862 -0.07908 -0.09316 -0.00582 171 GLU B C   
3265 O O   . GLU B 171 ? 1.40275 1.10044 1.27330 -0.08480 -0.09663 -0.00227 171 GLU B O   
3266 C CB  . GLU B 171 ? 1.44405 1.15122 1.32011 -0.06696 -0.08078 0.00424  171 GLU B CB  
3267 C CG  . GLU B 171 ? 1.47347 1.18991 1.33868 -0.06447 -0.07532 0.00445  171 GLU B CG  
3268 C CD  . GLU B 171 ? 1.67865 1.40132 1.55059 -0.05810 -0.07154 0.01504  171 GLU B CD  
3269 O OE1 . GLU B 171 ? 1.73913 1.46031 1.62326 -0.05697 -0.07291 0.02498  171 GLU B OE1 
3270 O OE2 . GLU B 171 ? 1.72724 1.45708 1.59271 -0.05420 -0.06720 0.01321  171 GLU B OE2 
3271 N N   . LYS B 172 ? 1.47725 1.16324 1.36964 -0.07831 -0.09680 -0.00633 172 LYS B N   
3272 C CA  . LYS B 172 ? 1.30313 0.98263 1.20693 -0.08492 -0.10559 -0.00372 172 LYS B CA  
3273 C C   . LYS B 172 ? 1.26944 0.94802 1.15838 -0.09253 -0.11205 -0.01541 172 LYS B C   
3274 O O   . LYS B 172 ? 1.54024 1.21811 1.43346 -0.09905 -0.11970 -0.01116 172 LYS B O   
3275 C CB  . LYS B 172 ? 1.28276 0.95157 1.20768 -0.08319 -0.10883 -0.00476 172 LYS B CB  
3276 C CG  . LYS B 172 ? 1.49841 1.16923 1.44122 -0.07701 -0.10423 0.01140  172 LYS B CG  
3277 C CD  . LYS B 172 ? 1.42920 1.10617 1.38059 -0.07954 -0.10501 0.02794  172 LYS B CD  
3278 C CE  . LYS B 172 ? 1.40409 1.09110 1.35736 -0.07167 -0.09626 0.04175  172 LYS B CE  
3279 N NZ  . LYS B 172 ? 1.45508 1.15066 1.38658 -0.06801 -0.09007 0.03641  172 LYS B NZ  
3280 N N   . ASP B 173 ? 1.26495 0.94507 1.13644 -0.09174 -0.10915 -0.02968 173 ASP B N   
3281 C CA  . ASP B 173 ? 1.35369 1.03568 1.20758 -0.09843 -0.11442 -0.04062 173 ASP B CA  
3282 C C   . ASP B 173 ? 1.34681 1.03641 1.18017 -0.09599 -0.10677 -0.05011 173 ASP B C   
3283 O O   . ASP B 173 ? 1.30369 0.99095 1.13122 -0.09414 -0.10524 -0.06527 173 ASP B O   
3284 C CB  . ASP B 173 ? 1.20655 0.87839 1.06708 -0.10193 -0.12316 -0.05349 173 ASP B CB  
3285 C CG  . ASP B 173 ? 1.48267 1.15837 1.32477 -0.10960 -0.13069 -0.06254 173 ASP B CG  
3286 O OD1 . ASP B 173 ? 1.48406 1.17043 1.30937 -0.11223 -0.12880 -0.05654 173 ASP B OD1 
3287 O OD2 . ASP B 173 ? 1.74095 1.40934 1.58580 -0.11296 -0.13891 -0.07555 173 ASP B OD2 
3288 N N   . LEU B 174 ? 1.28690 0.98607 1.11104 -0.09604 -0.10184 -0.04102 174 LEU B N   
3289 C CA  . LEU B 174 ? 1.20118 0.90889 1.00896 -0.09440 -0.09427 -0.04724 174 LEU B CA  
3290 C C   . LEU B 174 ? 1.39627 1.10764 1.18518 -0.09910 -0.09649 -0.06010 174 LEU B C   
3291 O O   . LEU B 174 ? 1.45099 1.16942 1.22796 -0.09712 -0.08942 -0.06773 174 LEU B O   
3292 C CB  . LEU B 174 ? 1.03173 0.74800 0.83541 -0.09526 -0.09056 -0.03468 174 LEU B CB  
3293 C CG  . LEU B 174 ? 1.28609 1.00424 1.09985 -0.08854 -0.08382 -0.02758 174 LEU B CG  
3294 C CD1 . LEU B 174 ? 1.09148 0.81798 0.89939 -0.09010 -0.08035 -0.01976 174 LEU B CD1 
3295 C CD2 . LEU B 174 ? 1.28957 1.00741 1.10552 -0.08196 -0.07784 -0.03701 174 LEU B CD2 
3296 N N   . SER B 175 ? 1.38132 1.08960 1.16705 -0.10521 -0.10608 -0.06274 175 SER B N   
3297 C CA  . SER B 175 ? 1.33815 1.05214 1.10280 -0.10960 -0.10870 -0.07514 175 SER B CA  
3298 C C   . SER B 175 ? 1.22759 0.93489 0.99221 -0.10668 -0.10920 -0.09513 175 SER B C   
3299 O O   . SER B 175 ? 1.24180 0.95575 0.98691 -0.10829 -0.10848 -0.10828 175 SER B O   
3300 C CB  . SER B 175 ? 1.18723 0.90303 0.94632 -0.11776 -0.12002 -0.06971 175 SER B CB  
3301 O OG  . SER B 175 ? 1.32057 1.03997 1.08642 -0.11962 -0.12048 -0.05071 175 SER B OG  
3302 N N   . ARG B 176 ? 1.22692 0.92201 1.01322 -0.10207 -0.11000 -0.09757 176 ARG B N   
3303 C CA  . ARG B 176 ? 1.29791 0.98482 1.08833 -0.09888 -0.11101 -0.11682 176 ARG B CA  
3304 C C   . ARG B 176 ? 1.37574 1.06921 1.15776 -0.09226 -0.09948 -0.12692 176 ARG B C   
3305 O O   . ARG B 176 ? 1.35970 1.05948 1.14343 -0.08838 -0.09104 -0.11723 176 ARG B O   
3306 C CB  . ARG B 176 ? 1.18570 0.85761 1.00526 -0.09571 -0.11498 -0.11401 176 ARG B CB  
3307 C CG  . ARG B 176 ? 1.20597 0.86690 1.03374 -0.09334 -0.11838 -0.13438 176 ARG B CG  
3308 C CD  . ARG B 176 ? 1.30002 0.95220 1.15117 -0.08486 -0.11302 -0.13353 176 ARG B CD  
3309 N NE  . ARG B 176 ? 1.46547 1.10812 1.34272 -0.08531 -0.11808 -0.11786 176 ARG B NE  
3310 C CZ  . ARG B 176 ? 1.37587 1.00417 1.27576 -0.08641 -0.12614 -0.12246 176 ARG B CZ  
3311 N NH1 . ARG B 176 ? 1.19834 0.81859 1.09862 -0.08667 -0.13062 -0.14422 176 ARG B NH1 
3312 N NH2 . ARG B 176 ? 1.29504 0.91733 1.21881 -0.08709 -0.12952 -0.10504 176 ARG B NH2 
3313 N N   . LYS B 177 ? 1.28815 0.98060 1.06207 -0.09082 -0.09936 -0.14748 177 LYS B N   
3314 C CA  . LYS B 177 ? 1.31355 1.01215 1.08260 -0.08383 -0.08834 -0.15937 177 LYS B CA  
3315 C C   . LYS B 177 ? 1.32462 1.01148 1.12095 -0.07579 -0.08588 -0.16014 177 LYS B C   
3316 O O   . LYS B 177 ? 1.28453 0.96167 1.09184 -0.07179 -0.08749 -0.17602 177 LYS B O   
3317 C CB  . LYS B 177 ? 1.44058 1.14344 1.19099 -0.08457 -0.08874 -0.18180 177 LYS B CB  
3318 C CG  . LYS B 177 ? 1.49176 1.20767 1.21380 -0.09270 -0.09238 -0.17992 177 LYS B CG  
3319 C CD  . LYS B 177 ? 1.53461 1.26611 1.24475 -0.09414 -0.08380 -0.16284 177 LYS B CD  
3320 C CE  . LYS B 177 ? 1.27847 1.02091 0.96655 -0.10282 -0.08942 -0.15409 177 LYS B CE  
3321 N NZ  . LYS B 177 ? 1.14337 0.89838 0.82561 -0.10455 -0.08209 -0.13539 177 LYS B NZ  
3322 N N   . TRP B 178 ? 1.28536 0.97343 1.09335 -0.07317 -0.08228 -0.14249 178 TRP B N   
3323 C CA  . TRP B 178 ? 1.26517 0.94489 1.09767 -0.06534 -0.07991 -0.13995 178 TRP B CA  
3324 C C   . TRP B 178 ? 1.25092 0.93532 1.08383 -0.05780 -0.07107 -0.15416 178 TRP B C   
3325 O O   . TRP B 178 ? 1.25606 0.95437 1.07131 -0.05786 -0.06352 -0.15859 178 TRP B O   
3326 C CB  . TRP B 178 ? 1.18407 0.86777 1.02460 -0.06354 -0.07721 -0.11931 178 TRP B CB  
3327 C CG  . TRP B 178 ? 1.25245 0.93282 1.09647 -0.06912 -0.08403 -0.10371 178 TRP B CG  
3328 C CD1 . TRP B 178 ? 1.25196 0.94052 1.08176 -0.07499 -0.08480 -0.09385 178 TRP B CD1 
3329 C CD2 . TRP B 178 ? 1.22637 0.89489 1.09175 -0.06922 -0.09082 -0.09540 178 TRP B CD2 
3330 N NE1 . TRP B 178 ? 1.20483 0.88788 1.04566 -0.07818 -0.09127 -0.08058 178 TRP B NE1 
3331 C CE2 . TRP B 178 ? 1.03499 0.70633 0.89736 -0.07500 -0.09483 -0.08097 178 TRP B CE2 
3332 C CE3 . TRP B 178 ? 1.23087 0.88702 1.11973 -0.06491 -0.09365 -0.09776 178 TRP B CE3 
3333 C CZ2 . TRP B 178 ? 1.23390 0.89755 1.11509 -0.07666 -0.10088 -0.06907 178 TRP B CZ2 
3334 C CZ3 . TRP B 178 ? 1.26785 0.91575 1.17579 -0.06704 -0.10001 -0.08484 178 TRP B CZ3 
3335 C CH2 . TRP B 178 ? 1.34552 0.99788 1.24915 -0.07289 -0.10324 -0.07072 178 TRP B CH2 
3336 N N   . THR B 179 ? 1.24877 0.92193 1.10431 -0.05115 -0.07185 -0.16023 179 THR B N   
3337 C CA  . THR B 179 ? 1.17997 0.85682 1.04278 -0.04244 -0.06359 -0.17120 179 THR B CA  
3338 C C   . THR B 179 ? 1.27609 0.94605 1.16613 -0.03531 -0.06375 -0.15960 179 THR B C   
3339 O O   . THR B 179 ? 1.41436 1.07646 1.31666 -0.03717 -0.06990 -0.14456 179 THR B O   
3340 C CB  . THR B 179 ? 1.16106 0.83121 1.02460 -0.04016 -0.06434 -0.19557 179 THR B CB  
3341 O OG1 . THR B 179 ? 1.35852 1.00962 1.24416 -0.04034 -0.07396 -0.19752 179 THR B OG1 
3342 C CG2 . THR B 179 ? 1.13872 0.81735 0.97272 -0.04725 -0.06503 -0.20683 179 THR B CG2 
3343 N N   . LEU B 180 ? 1.34951 1.02394 1.24945 -0.02683 -0.05671 -0.16605 180 LEU B N   
3344 C CA  . LEU B 180 ? 1.40550 1.07495 1.33151 -0.01918 -0.05711 -0.15531 180 LEU B CA  
3345 C C   . LEU B 180 ? 1.39316 1.04343 1.34439 -0.01686 -0.06437 -0.15883 180 LEU B C   
3346 O O   . LEU B 180 ? 1.23966 0.88375 1.21179 -0.01362 -0.06776 -0.14330 180 LEU B O   
3347 C CB  . LEU B 180 ? 1.46390 1.14406 1.39561 -0.01070 -0.04838 -0.16170 180 LEU B CB  
3348 C CG  . LEU B 180 ? 1.32688 1.00742 1.28135 -0.00292 -0.04855 -0.14744 180 LEU B CG  
3349 C CD1 . LEU B 180 ? 1.20392 0.89486 1.14966 -0.00542 -0.04879 -0.12769 180 LEU B CD1 
3350 C CD2 . LEU B 180 ? 1.35294 1.04130 1.31701 0.00559  -0.04124 -0.15885 180 LEU B CD2 
3351 N N   . GLY B 181 ? 1.39406 1.03540 1.34482 -0.01806 -0.06672 -0.17922 181 GLY B N   
3352 C CA  . GLY B 181 ? 1.33874 0.96019 1.31545 -0.01717 -0.07494 -0.18333 181 GLY B CA  
3353 C C   . GLY B 181 ? 1.37939 0.99280 1.36172 -0.02461 -0.08388 -0.16589 181 GLY B C   
3354 O O   . GLY B 181 ? 1.28203 0.88367 1.29201 -0.02244 -0.08882 -0.15443 181 GLY B O   
3355 N N   . ILE B 182 ? 1.43718 1.05757 1.39480 -0.03344 -0.08593 -0.16295 182 ILE B N   
3356 C CA  . ILE B 182 ? 1.35884 0.97424 1.32090 -0.04069 -0.09366 -0.14603 182 ILE B CA  
3357 C C   . ILE B 182 ? 1.29645 0.91599 1.27127 -0.03693 -0.09131 -0.12121 182 ILE B C   
3358 O O   . ILE B 182 ? 1.29270 0.90276 1.29037 -0.03730 -0.09663 -0.10776 182 ILE B O   
3359 C CB  . ILE B 182 ? 1.14600 0.77106 1.07836 -0.04973 -0.09517 -0.14678 182 ILE B CB  
3360 C CG1 . ILE B 182 ? 1.21863 0.84134 1.13660 -0.05296 -0.09793 -0.17167 182 ILE B CG1 
3361 C CG2 . ILE B 182 ? 1.13387 0.75510 1.07242 -0.05680 -0.10279 -0.12943 182 ILE B CG2 
3362 C CD1 . ILE B 182 ? 1.40320 1.03426 1.29424 -0.06241 -0.10184 -0.17195 182 ILE B CD1 
3363 N N   . ILE B 183 ? 1.38276 1.01752 1.34307 -0.03343 -0.08342 -0.11472 183 ILE B N   
3364 C CA  . ILE B 183 ? 1.42034 1.06135 1.38937 -0.02918 -0.08116 -0.09322 183 ILE B CA  
3365 C C   . ILE B 183 ? 1.48803 1.12011 1.48719 -0.02129 -0.08238 -0.08793 183 ILE B C   
3366 O O   . ILE B 183 ? 1.56851 1.19810 1.58352 -0.02024 -0.08516 -0.06897 183 ILE B O   
3367 C CB  . ILE B 183 ? 1.42532 1.08371 1.37544 -0.02640 -0.07324 -0.09138 183 ILE B CB  
3368 C CG1 . ILE B 183 ? 1.42007 1.08665 1.34285 -0.03430 -0.07204 -0.09606 183 ILE B CG1 
3369 C CG2 . ILE B 183 ? 1.40304 1.06887 1.35944 -0.02231 -0.07200 -0.07074 183 ILE B CG2 
3370 C CD1 . ILE B 183 ? 1.47839 1.14511 1.39609 -0.04089 -0.07647 -0.08117 183 ILE B CD1 
3371 N N   . ALA B 184 ? 1.49532 1.12377 1.50345 -0.01515 -0.07978 -0.10363 184 ALA B N   
3372 C CA  . ALA B 184 ? 1.46975 1.08922 1.50912 -0.00701 -0.08116 -0.09904 184 ALA B CA  
3373 C C   . ALA B 184 ? 1.41858 1.02047 1.48267 -0.01043 -0.08961 -0.09268 184 ALA B C   
3374 O O   . ALA B 184 ? 1.43572 1.03516 1.52070 -0.00752 -0.09176 -0.07244 184 ALA B O   
3375 C CB  . ALA B 184 ? 1.50924 1.12653 1.55497 -0.00032 -0.07715 -0.12041 184 ALA B CB  
3376 N N   . ASP B 185 ? 1.46468 1.05507 1.52731 -0.01674 -0.09476 -0.10960 185 ASP B N   
3377 C CA  . ASP B 185 ? 1.38459 0.95798 1.47216 -0.02143 -0.10391 -0.10513 185 ASP B CA  
3378 C C   . ASP B 185 ? 1.43748 1.01542 1.52741 -0.02619 -0.10627 -0.07871 185 ASP B C   
3379 O O   . ASP B 185 ? 1.48424 1.05347 1.60323 -0.02542 -0.11035 -0.06279 185 ASP B O   
3380 C CB  . ASP B 185 ? 1.54930 1.11362 1.62756 -0.02891 -0.10979 -0.12822 185 ASP B CB  
3381 C CG  . ASP B 185 ? 1.89726 1.45066 1.98695 -0.02352 -0.10983 -0.15428 185 ASP B CG  
3382 O OD1 . ASP B 185 ? 1.83563 1.38852 1.94177 -0.01383 -0.10491 -0.15371 185 ASP B OD1 
3383 O OD2 . ASP B 185 ? 1.89419 1.44006 1.97691 -0.02863 -0.11506 -0.17572 185 ASP B OD2 
3384 N N   . ALA B 186 ? 1.48073 1.07280 1.54176 -0.03090 -0.10336 -0.07325 186 ALA B N   
3385 C CA  . ALA B 186 ? 1.40265 1.00059 1.46475 -0.03484 -0.10461 -0.04969 186 ALA B CA  
3386 C C   . ALA B 186 ? 1.36349 0.96730 1.44132 -0.02711 -0.10088 -0.02740 186 ALA B C   
3387 O O   . ALA B 186 ? 1.42969 1.03068 1.52708 -0.02843 -0.10374 -0.00810 186 ALA B O   
3388 C CB  . ALA B 186 ? 1.38845 1.00112 1.41756 -0.03950 -0.10113 -0.04909 186 ALA B CB  
3389 N N   . PHE B 187 ? 1.36957 0.98303 1.43950 -0.01905 -0.09464 -0.02893 187 PHE B N   
3390 C CA  . PHE B 187 ? 1.42125 1.04217 1.50419 -0.01117 -0.09192 -0.00835 187 PHE B CA  
3391 C C   . PHE B 187 ? 1.58305 1.19101 1.70066 -0.00522 -0.09503 -0.00550 187 PHE B C   
3392 O O   . PHE B 187 ? 1.51759 1.13214 1.64748 0.00214  -0.09325 0.01191  187 PHE B O   
3393 C CB  . PHE B 187 ? 1.34738 0.98538 1.40869 -0.00530 -0.08520 -0.01035 187 PHE B CB  
3394 C CG  . PHE B 187 ? 1.29663 0.94845 1.32936 -0.00982 -0.08211 -0.00649 187 PHE B CG  
3395 C CD1 . PHE B 187 ? 1.37715 1.03012 1.38756 -0.01604 -0.08112 -0.02297 187 PHE B CD1 
3396 C CD2 . PHE B 187 ? 1.33733 1.00128 1.36617 -0.00766 -0.08022 0.01378  187 PHE B CD2 
3397 C CE1 . PHE B 187 ? 1.31325 0.97781 1.30063 -0.02008 -0.07864 -0.01877 187 PHE B CE1 
3398 C CE2 . PHE B 187 ? 1.30824 0.98381 1.31308 -0.01131 -0.07746 0.01587  187 PHE B CE2 
3399 C CZ  . PHE B 187 ? 1.19525 0.87031 1.18078 -0.01761 -0.07688 -0.00012 187 PHE B CZ  
3400 N N   . ASN B 188 ? 1.82135 1.41143 1.95542 -0.00804 -0.10005 -0.02206 188 ASN B N   
3401 C CA  . ASN B 188 ? 1.79542 1.37008 1.96659 -0.00283 -0.10385 -0.02142 188 ASN B CA  
3402 C C   . ASN B 188 ? 1.79343 1.37504 1.97072 0.00850  -0.09910 -0.02043 188 ASN B C   
3403 O O   . ASN B 188 ? 1.75068 1.33014 1.95487 0.01487  -0.10033 -0.00302 188 ASN B O   
3404 C CB  . ASN B 188 ? 1.82257 1.39091 2.02219 -0.00512 -0.10852 0.00381  188 ASN B CB  
3405 C CG  . ASN B 188 ? 2.03175 1.60136 2.22093 -0.01563 -0.11143 0.00983  188 ASN B CG  
3406 O OD1 . ASN B 188 ? 2.01808 1.57680 2.20544 -0.02321 -0.11667 -0.00760 188 ASN B OD1 
3407 N ND2 . ASN B 188 ? 2.05554 1.63959 2.23771 -0.01580 -0.10817 0.03419  188 ASN B ND2 
3408 N N   . ALA B 189 ? 1.54128 1.13239 1.69430 0.01088  -0.09374 -0.03833 189 ALA B N   
3409 C CA  . ALA B 189 ? 1.72645 1.32540 1.88451 0.02116  -0.08923 -0.04110 189 ALA B CA  
3410 C C   . ALA B 189 ? 1.69942 1.29666 1.84554 0.02184  -0.08566 -0.07090 189 ALA B C   
3411 O O   . ALA B 189 ? 1.69701 1.28614 1.83222 0.01478  -0.08744 -0.08833 189 ALA B O   
3412 C CB  . ALA B 189 ? 1.68837 1.30931 1.82669 0.02432  -0.08480 -0.02419 189 ALA B CB  
3413 N N   . SER B 190 ? 1.78819 1.39463 1.93636 0.03052  -0.08057 -0.07655 190 SER B N   
3414 C CA  . SER B 190 ? 1.80358 1.41077 1.94345 0.03274  -0.07562 -0.10362 190 SER B CA  
3415 C C   . SER B 190 ? 1.80216 1.42914 1.90628 0.02967  -0.06893 -0.10860 190 SER B C   
3416 O O   . SER B 190 ? 1.80100 1.44221 1.89274 0.02935  -0.06770 -0.09160 190 SER B O   
3417 C CB  . SER B 190 ? 1.82998 1.43533 1.99821 0.04451  -0.07360 -0.10815 190 SER B CB  
3418 O OG  . SER B 190 ? 1.88506 1.50051 2.06507 0.05074  -0.07434 -0.08396 190 SER B OG  
3419 N N   . GLU B 191 ? 1.10034 1.56044 1.88438 0.13890  0.08951  -0.02883 191 GLU B N   
3420 C CA  . GLU B 191 ? 1.14662 1.60826 1.94783 0.12924  0.08830  -0.02335 191 GLU B CA  
3421 C C   . GLU B 191 ? 1.05324 1.53496 1.93516 0.12693  0.05206  -0.00560 191 GLU B C   
3422 O O   . GLU B 191 ? 1.04422 1.52340 1.91193 0.11983  0.01898  -0.00392 191 GLU B O   
3423 C CB  . GLU B 191 ? 1.11896 1.56901 1.93582 0.12642  0.14402  -0.02249 191 GLU B CB  
3424 C CG  . GLU B 191 ? 1.09803 1.51516 1.81816 0.12187  0.16929  -0.03915 191 GLU B CG  
3425 C CD  . GLU B 191 ? 1.20401 1.59862 1.92210 0.11526  0.21261  -0.03726 191 GLU B CD  
3426 O OE1 . GLU B 191 ? 1.18228 1.58999 1.98381 0.11622  0.23070  -0.02218 191 GLU B OE1 
3427 O OE2 . GLU B 191 ? 1.22227 1.58252 1.85679 0.10892  0.22832  -0.04917 191 GLU B OE2 
3428 N N   . ILE B 192 ? 1.01148 1.51026 1.98107 0.13192  0.05691  0.00931  192 ILE B N   
3429 C CA  . ILE B 192 ? 0.94127 1.45615 1.99652 0.12779  0.01610  0.02998  192 ILE B CA  
3430 C C   . ILE B 192 ? 0.91923 1.42056 1.92120 0.12522  -0.04618 0.02655  192 ILE B C   
3431 O O   . ILE B 192 ? 0.81487 1.31238 1.83284 0.11594  -0.08387 0.03517  192 ILE B O   
3432 C CB  . ILE B 192 ? 1.04066 1.55220 2.14486 0.12969  0.02454  0.04483  192 ILE B CB  
3433 C CG1 . ILE B 192 ? 0.84028 1.35080 2.00040 0.12148  -0.02986 0.06563  192 ILE B CG1 
3434 C CG2 . ILE B 192 ? 0.97462 1.48192 2.03254 0.14101  0.03228  0.03268  192 ILE B CG2 
3435 C CD1 . ILE B 192 ? 0.60808 1.11967 1.83495 0.10965  -0.02990 0.08342  192 ILE B CD1 
3436 N N   . THR B 193 ? 0.97306 1.46025 1.90706 0.13351  -0.05589 0.01461  193 THR B N   
3437 C CA  . THR B 193 ? 0.96743 1.42908 1.84040 0.13353  -0.10770 0.01194  193 THR B CA  
3438 C C   . THR B 193 ? 1.04325 1.48483 1.84245 0.12689  -0.11773 0.00191  193 THR B C   
3439 O O   . THR B 193 ? 0.99643 1.41606 1.77653 0.12096  -0.16184 0.00710  193 THR B O   
3440 C CB  . THR B 193 ? 1.06221 1.51121 1.88050 0.14579  -0.10486 0.00198  193 THR B CB  
3441 O OG1 . THR B 193 ? 1.00223 1.45022 1.76222 0.14972  -0.06388 -0.01483 193 THR B OG1 
3442 C CG2 . THR B 193 ? 1.07724 1.54499 1.97139 0.15224  -0.09888 0.01344  193 THR B CG2 
3443 N N   . ILE B 194 ? 1.06064 1.50399 1.81429 0.12713  -0.07927 -0.01164 194 ILE B N   
3444 C CA  . ILE B 194 ? 0.92044 1.34728 1.61194 0.12086  -0.08618 -0.01928 194 ILE B CA  
3445 C C   . ILE B 194 ? 1.00329 1.43737 1.74479 0.10908  -0.10043 -0.00846 194 ILE B C   
3446 O O   . ILE B 194 ? 1.03706 1.45087 1.74524 0.10326  -0.13371 -0.00751 194 ILE B O   
3447 C CB  . ILE B 194 ? 0.95512 1.38201 1.59760 0.12157  -0.04533 -0.03279 194 ILE B CB  
3448 C CG1 . ILE B 194 ? 0.99677 1.40684 1.57074 0.13082  -0.04664 -0.04273 194 ILE B CG1 
3449 C CG2 . ILE B 194 ? 0.93501 1.35539 1.54904 0.11195  -0.04376 -0.03553 194 ILE B CG2 
3450 C CD1 . ILE B 194 ? 1.10310 1.52038 1.69564 0.14049  -0.03469 -0.04347 194 ILE B CD1 
3451 N N   . ARG B 195 ? 0.97777 1.43679 1.79962 0.10581  -0.07221 0.00063  195 ARG B N   
3452 C CA  . ARG B 195 ? 0.90440 1.37328 1.78957 0.09514  -0.08135 0.01382  195 ARG B CA  
3453 C C   . ARG B 195 ? 0.88634 1.34758 1.80865 0.08938  -0.14085 0.02851  195 ARG B C   
3454 O O   . ARG B 195 ? 0.97249 1.42343 1.89361 0.07921  -0.16905 0.03325  195 ARG B O   
3455 C CB  . ARG B 195 ? 0.91270 1.40570 1.89092 0.09567  -0.03711 0.02540  195 ARG B CB  
3456 C CG  . ARG B 195 ? 1.09045 1.57745 2.02597 0.09899  0.02083  0.01240  195 ARG B CG  
3457 C CD  . ARG B 195 ? 1.20506 1.70325 2.22482 0.10173  0.07154  0.02462  195 ARG B CD  
3458 N NE  . ARG B 195 ? 1.23785 1.74579 2.33226 0.09414  0.07830  0.04049  195 ARG B NE  
3459 C CZ  . ARG B 195 ? 1.19950 1.70962 2.36970 0.09577  0.12490  0.05505  195 ARG B CZ  
3460 N NH1 . ARG B 195 ? 1.18901 1.68409 2.35594 0.10330  0.16704  0.05494  195 ARG B NH1 
3461 N NH2 . ARG B 195 ? 1.20643 1.71577 2.42759 0.08748  0.12835  0.06959  195 ARG B NH2 
3462 N N   . LYS B 196 ? 0.83665 1.29832 1.79019 0.09469  -0.16308 0.03665  196 LYS B N   
3463 C CA  . LYS B 196 ? 0.81719 1.26389 1.80650 0.08694  -0.22554 0.05319  196 LYS B CA  
3464 C C   . LYS B 196 ? 0.94395 1.34131 1.82107 0.08600  -0.26891 0.04270  196 LYS B C   
3465 O O   . LYS B 196 ? 1.13361 1.50407 2.00496 0.07479  -0.31719 0.05114  196 LYS B O   
3466 C CB  . LYS B 196 ? 1.05067 1.51109 2.11659 0.09164  -0.23574 0.06856  196 LYS B CB  
3467 C CG  . LYS B 196 ? 1.01586 1.49887 2.16933 0.08754  -0.18964 0.08278  196 LYS B CG  
3468 C CD  . LYS B 196 ? 0.87340 1.34718 2.08890 0.08255  -0.20979 0.10416  196 LYS B CD  
3469 C CE  . LYS B 196 ? 0.97986 1.45973 2.28743 0.07154  -0.19405 0.12568  196 LYS B CE  
3470 N NZ  . LYS B 196 ? 0.96126 1.46094 2.29943 0.07870  -0.11893 0.12303  196 LYS B NZ  
3471 N N   . ARG B 197 ? 0.88750 1.26696 1.67522 0.09769  -0.25174 0.02578  197 ARG B N   
3472 C CA  . ARG B 197 ? 0.87658 1.20332 1.55370 0.09930  -0.27975 0.01619  197 ARG B CA  
3473 C C   . ARG B 197 ? 1.03595 1.35079 1.67452 0.09076  -0.27882 0.01085  197 ARG B C   
3474 O O   . ARG B 197 ? 1.15024 1.41660 1.72570 0.08593  -0.31600 0.01099  197 ARG B O   
3475 C CB  . ARG B 197 ? 1.03881 1.35514 1.64273 0.11445  -0.25011 0.00114  197 ARG B CB  
3476 C CG  . ARG B 197 ? 1.30691 1.56610 1.83201 0.12138  -0.28439 0.00037  197 ARG B CG  
3477 C CD  . ARG B 197 ? 1.19011 1.43764 1.64595 0.13700  -0.25073 -0.01294 197 ARG B CD  
3478 N NE  . ARG B 197 ? 1.43662 1.62623 1.82162 0.14562  -0.27664 -0.01203 197 ARG B NE  
3479 C CZ  . ARG B 197 ? 1.48038 1.60439 1.77176 0.14719  -0.29457 -0.01438 197 ARG B CZ  
3480 N NH1 . ARG B 197 ? 1.51072 1.62089 1.77257 0.13968  -0.29503 -0.01701 197 ARG B NH1 
3481 N NH2 . ARG B 197 ? 1.49538 1.56055 1.71725 0.15700  -0.31017 -0.01359 197 ARG B NH2 
3482 N N   . LEU B 198 ? 1.07433 1.42656 1.74543 0.08853  -0.23647 0.00658  198 LEU B N   
3483 C CA  . LEU B 198 ? 1.02510 1.37057 1.67146 0.07962  -0.23491 0.00339  198 LEU B CA  
3484 C C   . LEU B 198 ? 1.11560 1.46150 1.82919 0.06537  -0.27266 0.01971  198 LEU B C   
3485 O O   . LEU B 198 ? 1.26542 1.57937 1.93705 0.05697  -0.30216 0.01988  198 LEU B O   
3486 C CB  . LEU B 198 ? 0.94611 1.32504 1.60476 0.08081  -0.18043 -0.00461 198 LEU B CB  
3487 C CG  . LEU B 198 ? 0.96277 1.33190 1.53964 0.08962  -0.15159 -0.02030 198 LEU B CG  
3488 C CD1 . LEU B 198 ? 0.85904 1.25150 1.44531 0.08686  -0.10671 -0.02594 198 LEU B CD1 
3489 C CD2 . LEU B 198 ? 0.93725 1.26626 1.42972 0.09035  -0.17237 -0.02562 198 LEU B CD2 
3490 N N   . GLU B 199 ? 0.95097 1.33128 1.77367 0.06244  -0.27111 0.03515  199 GLU B N   
3491 C CA  . GLU B 199 ? 1.10526 1.49144 2.01548 0.04847  -0.30749 0.05545  199 GLU B CA  
3492 C C   . GLU B 199 ? 1.16006 1.49633 2.03607 0.04048  -0.37979 0.06368  199 GLU B C   
3493 O O   . GLU B 199 ? 1.00057 1.32324 1.91171 0.02580  -0.42140 0.07697  199 GLU B O   
3494 C CB  . GLU B 199 ? 1.09366 1.52500 2.13580 0.04969  -0.28686 0.07353  199 GLU B CB  
3495 C CG  . GLU B 199 ? 1.15041 1.61885 2.24313 0.05222  -0.22081 0.07228  199 GLU B CG  
3496 C CD  . GLU B 199 ? 1.22116 1.71388 2.41804 0.05470  -0.18935 0.08995  199 GLU B CD  
3497 O OE1 . GLU B 199 ? 1.01456 1.49458 2.23249 0.05402  -0.21678 0.10127  199 GLU B OE1 
3498 O OE2 . GLU B 199 ? 1.33840 1.84850 2.57478 0.05659  -0.13285 0.09191  199 GLU B OE2 
3499 N N   . SER B 200 ? 1.20625 1.51022 2.01568 0.04923  -0.39692 0.05753  200 SER B N   
3500 C CA  . SER B 200 ? 1.13491 1.37515 1.89037 0.04190  -0.46517 0.06442  200 SER B CA  
3501 C C   . SER B 200 ? 1.32802 1.51500 1.98909 0.03376  -0.48742 0.05636  200 SER B C   
3502 O O   . SER B 200 ? 1.51180 1.64933 2.15766 0.01979  -0.54863 0.06738  200 SER B O   
3503 C CB  . SER B 200 ? 1.10278 1.31091 1.78474 0.05547  -0.46770 0.05632  200 SER B CB  
3504 O OG  . SER B 200 ? 1.36395 1.53312 1.92031 0.06543  -0.44444 0.03633  200 SER B OG  
3505 N N   . GLU B 201 ? 1.22761 1.41941 1.82366 0.04150  -0.44047 0.03837  201 GLU B N   
3506 C CA  . GLU B 201 ? 1.30953 1.45825 1.82846 0.03451  -0.45222 0.03172  201 GLU B CA  
3507 C C   . GLU B 201 ? 1.23847 1.43148 1.83106 0.02382  -0.43608 0.03645  201 GLU B C   
3508 O O   . GLU B 201 ? 1.31867 1.49713 1.85513 0.02216  -0.42109 0.02702  201 GLU B O   
3509 C CB  . GLU B 201 ? 1.34888 1.47002 1.75496 0.04890  -0.41408 0.01276  201 GLU B CB  
3510 C CG  . GLU B 201 ? 1.36568 1.42293 1.67595 0.05983  -0.42918 0.00808  201 GLU B CG  
3511 C CD  . GLU B 201 ? 1.45430 1.54765 1.78687 0.07500  -0.39523 0.00372  201 GLU B CD  
3512 O OE1 . GLU B 201 ? 1.49803 1.66137 1.91063 0.07687  -0.35819 0.00288  201 GLU B OE1 
3513 O OE2 . GLU B 201 ? 1.71856 1.76466 1.98379 0.08507  -0.40423 0.00121  201 GLU B OE2 
3514 N N   . ASN B 202 ? 1.17731 1.42199 1.89694 0.01740  -0.43585 0.05231  202 ASN B N   
3515 C CA  . ASN B 202 ? 1.15811 1.44171 1.96132 0.00723  -0.42082 0.06092  202 ASN B CA  
3516 C C   . ASN B 202 ? 1.25721 1.56507 2.02135 0.01474  -0.35872 0.04411  202 ASN B C   
3517 O O   . ASN B 202 ? 1.26758 1.56738 2.00787 0.00768  -0.35580 0.04078  202 ASN B O   
3518 C CB  . ASN B 202 ? 1.23256 1.47425 2.02862 -0.01056 -0.47982 0.07121  202 ASN B CB  
3519 C CG  . ASN B 202 ? 1.13506 1.41944 2.06152 -0.02333 -0.48158 0.09055  202 ASN B CG  
3520 O OD1 . ASN B 202 ? 1.02750 1.32615 1.95609 -0.02698 -0.45521 0.08630  202 ASN B OD1 
3521 N ND2 . ASN B 202 ? 1.07865 1.36741 2.09094 -0.02973 -0.49881 0.11155  202 ASN B ND2 
3522 N N   . THR B 203 ? 1.31277 1.64825 2.07148 0.02830  -0.31108 0.03453  203 THR B N   
3523 C CA  . THR B 203 ? 1.29107 1.64522 2.01199 0.03454  -0.25611 0.02013  203 THR B CA  
3524 C C   . THR B 203 ? 1.18084 1.57599 1.95903 0.04256  -0.20781 0.02031  203 THR B C   
3525 O O   . THR B 203 ? 1.13178 1.53892 1.96049 0.04713  -0.21303 0.02801  203 THR B O   
3526 C CB  . THR B 203 ? 1.33721 1.65772 1.94040 0.04378  -0.24978 0.00325  203 THR B CB  
3527 O OG1 . THR B 203 ? 1.47991 1.78147 2.05454 0.05317  -0.26524 0.00169  203 THR B OG1 
3528 C CG2 . THR B 203 ? 1.36294 1.63923 1.89838 0.03696  -0.27885 0.00097  203 THR B CG2 
3529 N N   . ASN B 204 ? 0.93964 1.34999 1.70406 0.04377  -0.16096 0.01216  204 ASN B N   
3530 C CA  . ASN B 204 ? 0.87242 1.30495 1.65809 0.05128  -0.11021 0.00840  204 ASN B CA  
3531 C C   . ASN B 204 ? 0.98205 1.40198 1.67559 0.05509  -0.08308 -0.00867 204 ASN B C   
3532 O O   . ASN B 204 ? 1.00904 1.41362 1.65087 0.05036  -0.09305 -0.01365 204 ASN B O   
3533 C CB  . ASN B 204 ? 0.44403 0.89972 1.31948 0.04649  -0.07744 0.02078  204 ASN B CB  
3534 C CG  . ASN B 204 ? 0.78020 1.23107 1.64540 0.03704  -0.07297 0.02103  204 ASN B CG  
3535 O OD1 . ASN B 204 ? 0.92653 1.36965 1.73530 0.03751  -0.03917 0.00991  204 ASN B OD1 
3536 N ND2 . ASN B 204 ? 0.75210 1.20478 1.67213 0.02740  -0.10942 0.03476  204 ASN B ND2 
3537 N N   . PHE B 205 ? 0.87961 1.30380 1.55512 0.06305  -0.05124 -0.01614 205 PHE B N   
3538 C CA  . PHE B 205 ? 0.90768 1.31806 1.50212 0.06545  -0.03140 -0.02967 205 PHE B CA  
3539 C C   . PHE B 205 ? 0.82215 1.22630 1.39334 0.05670  -0.01385 -0.03167 205 PHE B C   
3540 O O   . PHE B 205 ? 0.85460 1.24424 1.36164 0.05524  -0.01980 -0.03836 205 PHE B O   
3541 C CB  . PHE B 205 ? 1.05812 1.47159 1.65016 0.07224  0.00143  -0.03484 205 PHE B CB  
3542 C CG  . PHE B 205 ? 0.98214 1.37927 1.50810 0.07025  0.02706  -0.04506 205 PHE B CG  
3543 C CD1 . PHE B 205 ? 0.97693 1.36204 1.44007 0.07338  0.01306  -0.05218 205 PHE B CD1 
3544 C CD2 . PHE B 205 ? 0.97589 1.36383 1.50297 0.06496  0.06520  -0.04560 205 PHE B CD2 
3545 C CE1 . PHE B 205 ? 1.09493 1.46355 1.50472 0.06939  0.02981  -0.05842 205 PHE B CE1 
3546 C CE2 . PHE B 205 ? 1.15655 1.51992 1.61515 0.06078  0.08230  -0.05393 205 PHE B CE2 
3547 C CZ  . PHE B 205 ? 1.20062 1.55645 1.60391 0.06207  0.06114  -0.05976 205 PHE B CZ  
3548 N N   . ASN B 206 ? 0.81803 1.23132 1.44461 0.05132  0.00949  -0.02407 206 ASN B N   
3549 C CA  . ASN B 206 ? 0.80995 1.21402 1.41541 0.04307  0.02746  -0.02493 206 ASN B CA  
3550 C C   . ASN B 206 ? 0.78454 1.18576 1.37636 0.03694  -0.00831 -0.02288 206 ASN B C   
3551 O O   . ASN B 206 ? 0.70669 1.09523 1.24657 0.03228  -0.00440 -0.02788 206 ASN B O   
3552 C CB  . ASN B 206 ? 0.73280 1.14297 1.40654 0.04048  0.06434  -0.01497 206 ASN B CB  
3553 C CG  . ASN B 206 ? 0.85214 1.25693 1.53772 0.04745  0.10421  -0.01604 206 ASN B CG  
3554 O OD1 . ASN B 206 ? 1.08218 1.50392 1.83417 0.05323  0.10284  -0.00781 206 ASN B OD1 
3555 N ND2 . ASN B 206 ? 0.69594 1.07188 1.31359 0.04627  0.13824  -0.02549 206 ASN B ND2 
3556 N N   . GLN B 207 ? 0.65559 1.06305 1.28953 0.03611  -0.04530 -0.01488 207 GLN B N   
3557 C CA  . GLN B 207 ? 0.70599 1.09932 1.31348 0.02999  -0.08054 -0.01387 207 GLN B CA  
3558 C C   . GLN B 207 ? 0.74143 1.11198 1.26026 0.03545  -0.09264 -0.02433 207 GLN B C   
3559 O O   . GLN B 207 ? 0.68968 1.04561 1.16447 0.03160  -0.09728 -0.02694 207 GLN B O   
3560 C CB  . GLN B 207 ? 0.83193 1.22451 1.49358 0.02598  -0.12361 -0.00229 207 GLN B CB  
3561 C CG  . GLN B 207 ? 0.96560 1.33172 1.58946 0.01819  -0.16149 -0.00155 207 GLN B CG  
3562 C CD  . GLN B 207 ? 1.18934 1.53415 1.83027 0.01394  -0.21560 0.00732  207 GLN B CD  
3563 O OE1 . GLN B 207 ? 1.12460 1.48214 1.82806 0.01477  -0.22878 0.01673  207 GLN B OE1 
3564 N NE2 . GLN B 207 ? 1.04677 1.35281 1.62796 0.00877  -0.24815 0.00521  207 GLN B NE2 
3565 N N   . ILE B 208 ? 0.69589 1.06210 1.19286 0.04508  -0.09639 -0.02860 208 ILE B N   
3566 C CA  . ILE B 208 ? 0.63725 0.98127 1.05989 0.05209  -0.10137 -0.03573 208 ILE B CA  
3567 C C   . ILE B 208 ? 0.65284 0.99769 1.03917 0.04963  -0.07501 -0.04039 208 ILE B C   
3568 O O   . ILE B 208 ? 0.76579 1.09348 1.10814 0.04901  -0.08122 -0.04091 208 ILE B O   
3569 C CB  . ILE B 208 ? 0.72962 1.07216 1.14392 0.06330  -0.10214 -0.03860 208 ILE B CB  
3570 C CG1 . ILE B 208 ? 0.72622 1.05151 1.15025 0.06555  -0.13853 -0.03345 208 ILE B CG1 
3571 C CG2 . ILE B 208 ? 0.68818 1.01427 1.03980 0.07139  -0.09335 -0.04408 208 ILE B CG2 
3572 C CD1 . ILE B 208 ? 0.75619 1.07639 1.17008 0.07692  -0.14082 -0.03551 208 ILE B CD1 
3573 N N   . LEU B 209 ? 0.64696 1.00578 1.04840 0.04787  -0.04564 -0.04270 209 LEU B N   
3574 C CA  . LEU B 209 ? 0.74263 1.09385 1.10317 0.04348  -0.02573 -0.04612 209 LEU B CA  
3575 C C   . LEU B 209 ? 0.58646 0.93323 0.94171 0.03392  -0.02544 -0.04311 209 LEU B C   
3576 O O   . LEU B 209 ? 0.71394 1.04881 1.02724 0.03134  -0.02736 -0.04324 209 LEU B O   
3577 C CB  . LEU B 209 ? 0.66953 1.02266 1.03694 0.04236  0.00443  -0.04930 209 LEU B CB  
3578 C CG  . LEU B 209 ? 0.73298 1.06717 1.04891 0.03637  0.02076  -0.05270 209 LEU B CG  
3579 C CD1 . LEU B 209 ? 0.79791 1.12449 1.10353 0.03962  0.03772  -0.05735 209 LEU B CD1 
3580 C CD2 . LEU B 209 ? 1.07114 1.39604 1.38785 0.02657  0.04064  -0.05082 209 LEU B CD2 
3581 N N   . MET B 210 ? 0.53102 0.88778 0.93500 0.02852  -0.02218 -0.03855 210 MET B N   
3582 C CA  . MET B 210 ? 0.70528 1.05841 1.10974 0.01958  -0.02186 -0.03508 210 MET B CA  
3583 C C   . MET B 210 ? 0.58460 0.92519 0.95902 0.01967  -0.05181 -0.03415 210 MET B C   
3584 O O   . MET B 210 ? 0.48699 0.81786 0.83005 0.01491  -0.04992 -0.03373 210 MET B O   
3585 C CB  . MET B 210 ? 0.61615 0.98351 1.09297 0.01484  -0.01498 -0.02742 210 MET B CB  
3586 C CG  . MET B 210 ? 0.65766 1.02253 1.14453 0.00564  -0.01696 -0.02255 210 MET B CG  
3587 S SD  . MET B 210 ? 0.86405 1.21790 1.33059 -0.00028 0.02840  -0.02339 210 MET B SD  
3588 C CE  . MET B 210 ? 1.10515 1.46729 1.63798 0.00379  0.06473  -0.01809 210 MET B CE  
3589 N N   . GLN B 211 ? 0.50737 0.84154 0.88647 0.02505  -0.07867 -0.03317 211 GLN B N   
3590 C CA  . GLN B 211 ? 0.55289 0.86092 0.89190 0.02596  -0.10372 -0.03236 211 GLN B CA  
3591 C C   . GLN B 211 ? 0.70240 0.99524 0.98387 0.03277  -0.09424 -0.03490 211 GLN B C   
3592 O O   . GLN B 211 ? 0.58930 0.86505 0.83925 0.03090  -0.09658 -0.03281 211 GLN B O   
3593 C CB  . GLN B 211 ? 0.51984 0.81136 0.86394 0.03003  -0.13442 -0.03057 211 GLN B CB  
3594 C CG  . GLN B 211 ? 0.83338 1.12719 1.23017 0.02038  -0.15977 -0.02340 211 GLN B CG  
3595 C CD  . GLN B 211 ? 0.89131 1.16080 1.26546 0.01183  -0.17844 -0.02087 211 GLN B CD  
3596 O OE1 . GLN B 211 ? 0.61179 0.86860 0.93742 0.01291  -0.16540 -0.02429 211 GLN B OE1 
3597 N NE2 . GLN B 211 ? 0.83865 1.09881 1.24991 0.00272  -0.21186 -0.01337 211 GLN B NE2 
3598 N N   . LEU B 212 ? 0.70660 1.00509 0.97986 0.04074  -0.08332 -0.03759 212 LEU B N   
3599 C CA  . LEU B 212 ? 0.59830 0.88624 0.83319 0.04655  -0.07399 -0.03641 212 LEU B CA  
3600 C C   . LEU B 212 ? 0.77056 1.06218 0.99555 0.03767  -0.06216 -0.03363 212 LEU B C   
3601 O O   . LEU B 212 ? 0.82530 1.10163 1.02522 0.03871  -0.06391 -0.02840 212 LEU B O   
3602 C CB  . LEU B 212 ? 0.61620 0.91474 0.85598 0.05302  -0.06372 -0.03904 212 LEU B CB  
3603 C CG  . LEU B 212 ? 0.89931 1.18145 1.12243 0.06640  -0.07151 -0.03845 212 LEU B CG  
3604 C CD1 . LEU B 212 ? 0.89352 1.18922 1.12676 0.07151  -0.06063 -0.04092 212 LEU B CD1 
3605 C CD2 . LEU B 212 ? 0.85247 1.10820 1.04003 0.07241  -0.07064 -0.03201 212 LEU B CD2 
3606 N N   . ARG B 213 ? 0.80406 1.11067 1.04655 0.02916  -0.04814 -0.03601 213 ARG B N   
3607 C CA  . ARG B 213 ? 0.55617 0.85866 0.77996 0.01992  -0.03774 -0.03330 213 ARG B CA  
3608 C C   . ARG B 213 ? 0.58944 0.88708 0.81258 0.01387  -0.04314 -0.02989 213 ARG B C   
3609 O O   . ARG B 213 ? 0.74505 1.03309 0.94473 0.01069  -0.04359 -0.02466 213 ARG B O   
3610 C CB  . ARG B 213 ? 0.66928 0.97483 0.89919 0.01301  -0.01786 -0.03710 213 ARG B CB  
3611 C CG  . ARG B 213 ? 0.82094 1.12487 1.04206 0.01761  -0.01253 -0.04040 213 ARG B CG  
3612 C CD  . ARG B 213 ? 0.97844 1.27083 1.18938 0.01050  0.01052  -0.04416 213 ARG B CD  
3613 N NE  . ARG B 213 ? 0.86249 1.14583 1.05430 0.01308  0.01282  -0.04711 213 ARG B NE  
3614 C CZ  . ARG B 213 ? 0.88811 1.15590 1.06893 0.01035  0.03421  -0.05193 213 ARG B CZ  
3615 N NH1 . ARG B 213 ? 0.71231 0.97099 0.90187 0.00620  0.05983  -0.05325 213 ARG B NH1 
3616 N NH2 . ARG B 213 ? 0.84891 1.10567 1.00913 0.01211  0.03245  -0.05450 213 ARG B NH2 
3617 N N   . MET B 214 ? 0.52234 0.82561 0.77511 0.01181  -0.04960 -0.03108 214 MET B N   
3618 C CA  . MET B 214 ? 0.50558 0.80281 0.75967 0.00493  -0.05600 -0.02777 214 MET B CA  
3619 C C   . MET B 214 ? 0.66547 0.94038 0.88758 0.01022  -0.07239 -0.02497 214 MET B C   
3620 O O   . MET B 214 ? 0.67390 0.93868 0.87988 0.00574  -0.07228 -0.02119 214 MET B O   
3621 C CB  . MET B 214 ? 0.61101 0.91903 0.91453 -0.00012 -0.06140 -0.02714 214 MET B CB  
3622 C CG  . MET B 214 ? 0.57305 0.89569 0.90977 -0.00584 -0.03472 -0.02672 214 MET B CG  
3623 S SD  . MET B 214 ? 0.64133 0.95203 0.93787 -0.01390 -0.01169 -0.02586 214 MET B SD  
3624 C CE  . MET B 214 ? 0.52889 0.83254 0.80179 -0.01182 0.01167  -0.03031 214 MET B CE  
3625 N N   . SER B 215 ? 0.74632 1.00791 0.95474 0.02045  -0.08305 -0.02615 215 SER B N   
3626 C CA  . SER B 215 ? 0.69731 0.92511 0.86550 0.02772  -0.09099 -0.02277 215 SER B CA  
3627 C C   . SER B 215 ? 0.66550 0.88953 0.81380 0.03216  -0.07521 -0.01609 215 SER B C   
3628 O O   . SER B 215 ? 0.67135 0.87617 0.79932 0.03214  -0.07254 -0.01011 215 SER B O   
3629 C CB  . SER B 215 ? 0.65805 0.86447 0.81119 0.03804  -0.10331 -0.02521 215 SER B CB  
3630 O OG  . SER B 215 ? 1.13583 1.30003 1.24086 0.04792  -0.10144 -0.02120 215 SER B OG  
3631 N N   . LYS B 216 ? 0.63753 0.87779 0.79506 0.03558  -0.06596 -0.01530 216 LYS B N   
3632 C CA  . LYS B 216 ? 0.68382 0.92335 0.83547 0.03671  -0.05654 -0.00559 216 LYS B CA  
3633 C C   . LYS B 216 ? 0.71605 0.96114 0.86798 0.02450  -0.05439 -0.00152 216 LYS B C   
3634 O O   . LYS B 216 ? 0.83071 1.06470 0.97549 0.02541  -0.05137 0.00922  216 LYS B O   
3635 C CB  . LYS B 216 ? 0.55082 0.80571 0.71441 0.03805  -0.05282 -0.00557 216 LYS B CB  
3636 C CG  . LYS B 216 ? 0.79288 1.04028 0.95850 0.04406  -0.04897 0.00809  216 LYS B CG  
3637 C CD  . LYS B 216 ? 1.11426 1.33495 1.26930 0.05935  -0.04213 0.01518  216 LYS B CD  
3638 C CE  . LYS B 216 ? 0.99432 1.20554 1.16259 0.06347  -0.03345 0.03439  216 LYS B CE  
3639 N NZ  . LYS B 216 ? 0.65510 0.82969 0.80788 0.07885  -0.01769 0.04321  216 LYS B NZ  
3640 N N   . ALA B 217 ? 0.89846 1.15805 1.06085 0.01372  -0.05347 -0.00846 217 ALA B N   
3641 C CA  . ALA B 217 ? 0.90019 1.16050 1.05816 0.00220  -0.04943 -0.00499 217 ALA B CA  
3642 C C   . ALA B 217 ? 0.92147 1.16887 1.07281 0.00196  -0.05354 -0.00151 217 ALA B C   
3643 O O   . ALA B 217 ? 1.00486 1.24619 1.14711 -0.00247 -0.05097 0.00663  217 ALA B O   
3644 C CB  . ALA B 217 ? 0.88699 1.15841 1.05746 -0.00699 -0.04079 -0.01240 217 ALA B CB  
3645 N N   . ALA B 218 ? 0.71486 0.95398 0.86895 0.00541  -0.06219 -0.00690 218 ALA B N   
3646 C CA  . ALA B 218 ? 0.73473 0.95193 0.87365 0.00433  -0.06827 -0.00426 218 ALA B CA  
3647 C C   . ALA B 218 ? 0.99555 1.18749 1.10793 0.01371  -0.06163 0.00526  218 ALA B C   
3648 O O   . ALA B 218 ? 1.04798 1.22898 1.15111 0.01075  -0.05690 0.01218  218 ALA B O   
3649 C CB  . ALA B 218 ? 0.69288 0.89536 0.83262 0.00520  -0.08560 -0.01059 218 ALA B CB  
3650 N N   . LEU B 219 ? 1.05116 1.23202 1.15493 0.02599  -0.05826 0.00725  219 LEU B N   
3651 C CA  . LEU B 219 ? 0.89393 1.04907 0.98239 0.03715  -0.04509 0.01967  219 LEU B CA  
3652 C C   . LEU B 219 ? 0.79892 0.97291 0.90949 0.03192  -0.03780 0.03252  219 LEU B C   
3653 O O   . LEU B 219 ? 0.75037 0.90833 0.85680 0.03315  -0.02952 0.04361  219 LEU B O   
3654 C CB  . LEU B 219 ? 0.79377 0.93637 0.87695 0.05142  -0.03935 0.02095  219 LEU B CB  
3655 C CG  . LEU B 219 ? 0.74461 0.85878 0.79851 0.05799  -0.04870 0.01061  219 LEU B CG  
3656 C CD1 . LEU B 219 ? 0.79352 0.90351 0.84863 0.07119  -0.04110 0.01224  219 LEU B CD1 
3657 C CD2 . LEU B 219 ? 0.72930 0.78641 0.73380 0.06257  -0.04771 0.01173  219 LEU B CD2 
3658 N N   . LEU B 220 ? 0.82258 1.02533 0.95401 0.02533  -0.04232 0.03212  220 LEU B N   
3659 C CA  . LEU B 220 ? 0.88690 1.10021 1.03382 0.01765  -0.04336 0.04541  220 LEU B CA  
3660 C C   . LEU B 220 ? 0.84991 1.06240 0.99001 0.00654  -0.04439 0.04732  220 LEU B C   
3661 O O   . LEU B 220 ? 0.94255 1.15018 1.09169 0.00442  -0.04324 0.06281  220 LEU B O   
3662 C CB  . LEU B 220 ? 0.74159 0.97322 0.89495 0.00945  -0.05157 0.04125  220 LEU B CB  
3663 C CG  . LEU B 220 ? 0.67694 0.91134 0.84292 0.01897  -0.05187 0.04320  220 LEU B CG  
3664 C CD1 . LEU B 220 ? 0.57614 0.82242 0.73739 0.01034  -0.05845 0.03353  220 LEU B CD1 
3665 C CD2 . LEU B 220 ? 0.72885 0.95731 0.91997 0.02368  -0.05192 0.06498  220 LEU B CD2 
3666 N N   . LEU B 221 ? 0.93136 1.14901 1.06176 -0.00068 -0.04650 0.03359  221 LEU B N   
3667 C CA  . LEU B 221 ? 1.01332 1.22951 1.13851 -0.01080 -0.04570 0.03464  221 LEU B CA  
3668 C C   . LEU B 221 ? 0.97569 1.16988 1.09297 -0.00452 -0.04062 0.04306  221 LEU B C   
3669 O O   . LEU B 221 ? 1.09746 1.28835 1.21712 -0.00909 -0.03777 0.05437  221 LEU B O   
3670 C CB  . LEU B 221 ? 0.93046 1.15545 1.05821 -0.01755 -0.04689 0.02034  221 LEU B CB  
3671 C CG  . LEU B 221 ? 0.92940 1.15490 1.05720 -0.02855 -0.04389 0.02014  221 LEU B CG  
3672 C CD1 . LEU B 221 ? 0.73853 0.96730 0.85817 -0.03869 -0.03903 0.02520  221 LEU B CD1 
3673 C CD2 . LEU B 221 ? 1.00519 1.23840 1.15066 -0.03211 -0.04544 0.00931  221 LEU B CD2 
3674 N N   . LEU B 222 ? 1.03557 1.20790 1.13818 0.00587  -0.03908 0.03818  222 LEU B N   
3675 C CA  . LEU B 222 ? 1.01295 1.15077 1.09548 0.01266  -0.03026 0.04550  222 LEU B CA  
3676 C C   . LEU B 222 ? 1.07575 1.20313 1.17064 0.02259  -0.01492 0.06483  222 LEU B C   
3677 O O   . LEU B 222 ? 1.15268 1.25435 1.23883 0.02680  -0.00231 0.07508  222 LEU B O   
3678 C CB  . LEU B 222 ? 1.03239 1.13421 1.08174 0.02076  -0.03369 0.03599  222 LEU B CB  
3679 C CG  . LEU B 222 ? 1.13106 1.23152 1.17276 0.00978  -0.05180 0.02276  222 LEU B CG  
3680 C CD1 . LEU B 222 ? 1.31389 1.36412 1.31261 0.01616  -0.06115 0.01670  222 LEU B CD1 
3681 C CD2 . LEU B 222 ? 1.12481 1.22728 1.16977 -0.00039 -0.05008 0.02641  222 LEU B CD2 
3682 N N   . GLU B 223 ? 1.16564 1.31094 1.28557 0.02627  -0.01523 0.07184  223 GLU B N   
3683 C CA  . GLU B 223 ? 0.98597 1.12440 1.13410 0.03489  -0.00246 0.09460  223 GLU B CA  
3684 C C   . GLU B 223 ? 0.96758 1.11709 1.13839 0.02473  -0.00592 0.11000  223 GLU B C   
3685 O O   . GLU B 223 ? 1.00939 1.14849 1.20939 0.03203  0.00642  0.13233  223 GLU B O   
3686 C CB  . GLU B 223 ? 0.94130 1.09839 1.11809 0.03809  -0.00772 0.10023  223 GLU B CB  
3687 C CG  . GLU B 223 ? 1.00528 1.14583 1.16579 0.05214  0.00103  0.09148  223 GLU B CG  
3688 C CD  . GLU B 223 ? 1.08408 1.23649 1.28116 0.05886  0.00247  0.10375  223 GLU B CD  
3689 O OE1 . GLU B 223 ? 1.01061 1.18119 1.24793 0.05187  -0.00596 0.12113  223 GLU B OE1 
3690 O OE2 . GLU B 223 ? 1.23771 1.37904 1.42356 0.07016  0.00930  0.09691  223 GLU B OE2 
3691 N N   . ASN B 224 ? 0.94568 1.11319 1.10637 0.00868  -0.02062 0.10052  224 ASN B N   
3692 C CA  . ASN B 224 ? 1.03512 1.20882 1.20876 -0.00250 -0.02642 0.11394  224 ASN B CA  
3693 C C   . ASN B 224 ? 0.98165 1.16537 1.19323 -0.00598 -0.03795 0.13616  224 ASN B C   
3694 O O   . ASN B 224 ? 0.81154 0.99390 1.04369 -0.01192 -0.04264 0.15493  224 ASN B O   
3695 C CB  . ASN B 224 ? 0.95523 1.10579 1.12452 0.00346  -0.00976 0.12236  224 ASN B CB  
3696 C CG  . ASN B 224 ? 0.95903 1.11632 1.13253 -0.00971 -0.01657 0.13023  224 ASN B CG  
3697 O OD1 . ASN B 224 ? 1.01047 1.18419 1.17714 -0.02411 -0.03280 0.12479  224 ASN B OD1 
3698 N ND2 . ASN B 224 ? 1.12331 1.26206 1.30405 -0.00434 -0.00168 0.14385  224 ASN B ND2 
3699 N N   . SER B 225 ? 1.03527 1.22773 1.25905 -0.00354 -0.04585 0.13579  225 SER B N   
3700 C CA  . SER B 225 ? 0.91763 1.11656 1.18031 -0.00869 -0.06302 0.15792  225 SER B CA  
3701 C C   . SER B 225 ? 0.99143 1.19704 1.23134 -0.02459 -0.08804 0.14815  225 SER B C   
3702 O O   . SER B 225 ? 0.98465 1.19013 1.24948 -0.03089 -0.10863 0.16442  225 SER B O   
3703 C CB  . SER B 225 ? 0.88637 1.08254 1.19020 0.00831  -0.05016 0.17204  225 SER B CB  
3704 O OG  . SER B 225 ? 0.97349 1.15182 1.29733 0.02380  -0.02236 0.18621  225 SER B OG  
3705 N N   . TYR B 226 ? 0.92342 1.13003 1.11786 -0.03122 -0.08611 0.12359  226 TYR B N   
3706 C CA  . TYR B 226 ? 0.96256 1.16626 1.12874 -0.04317 -0.10109 0.11304  226 TYR B CA  
3707 C C   . TYR B 226 ? 0.94372 1.13913 1.06501 -0.05504 -0.09726 0.09703  226 TYR B C   
3708 O O   . TYR B 226 ? 0.88773 1.08920 1.00393 -0.05073 -0.08083 0.08602  226 TYR B O   
3709 C CB  . TYR B 226 ? 0.81366 1.02662 0.98128 -0.03294 -0.09380 0.09899  226 TYR B CB  
3710 C CG  . TYR B 226 ? 0.87213 1.08949 1.08279 -0.02143 -0.09562 0.11528  226 TYR B CG  
3711 C CD1 . TYR B 226 ? 0.93277 1.14578 1.16415 -0.02972 -0.11881 0.13255  226 TYR B CD1 
3712 C CD2 . TYR B 226 ? 0.65383 0.87331 0.88254 -0.00273 -0.07454 0.11475  226 TYR B CD2 
3713 C CE1 . TYR B 226 ? 0.58514 0.80360 0.86747 -0.01886 -0.11891 0.15034  226 TYR B CE1 
3714 C CE2 . TYR B 226 ? 0.67255 0.89146 0.94196 0.00956  -0.06982 0.13125  226 TYR B CE2 
3715 C CZ  . TYR B 226 ? 0.77306 0.99544 1.07580 0.00188  -0.09095 0.14967  226 TYR B CZ  
3716 O OH  . TYR B 226 ? 0.68844 0.91181 1.04264 0.01449  -0.08459 0.16862  226 TYR B OH  
3717 N N   . GLN B 227 ? 1.02410 1.19938 1.11100 -0.07031 -0.11232 0.09710  227 GLN B N   
3718 C CA  . GLN B 227 ? 1.10567 1.26374 1.14472 -0.08074 -0.10282 0.08270  227 GLN B CA  
3719 C C   . GLN B 227 ? 1.04400 1.20780 1.07054 -0.07559 -0.08477 0.06130  227 GLN B C   
3720 O O   . GLN B 227 ? 1.02511 1.20196 1.07018 -0.06682 -0.08554 0.05735  227 GLN B O   
3721 C CB  . GLN B 227 ? 1.17392 1.29259 1.16651 -0.09922 -0.12380 0.09184  227 GLN B CB  
3722 C CG  . GLN B 227 ? 1.38039 1.48812 1.37762 -0.10793 -0.14054 0.11207  227 GLN B CG  
3723 C CD  . GLN B 227 ? 1.48910 1.62613 1.55301 -0.09653 -0.14392 0.12991  227 GLN B CD  
3724 O OE1 . GLN B 227 ? 1.50564 1.65244 1.60766 -0.09092 -0.15588 0.14181  227 GLN B OE1 
3725 N NE2 . GLN B 227 ? 1.42353 1.57087 1.50213 -0.09238 -0.13017 0.13272  227 GLN B NE2 
3726 N N   . ILE B 228 ? 1.00345 1.15696 1.00344 -0.08063 -0.06638 0.04916  228 ILE B N   
3727 C CA  . ILE B 228 ? 0.96144 1.11997 0.95949 -0.07604 -0.04551 0.03185  228 ILE B CA  
3728 C C   . ILE B 228 ? 0.96937 1.10263 0.93300 -0.08094 -0.04906 0.02814  228 ILE B C   
3729 O O   . ILE B 228 ? 0.89327 1.03841 0.87023 -0.07330 -0.03853 0.01769  228 ILE B O   
3730 C CB  . ILE B 228 ? 1.06872 1.21887 1.05564 -0.08050 -0.02200 0.02450  228 ILE B CB  
3731 C CG1 . ILE B 228 ? 0.91914 1.09639 0.94551 -0.07474 -0.01977 0.02588  228 ILE B CG1 
3732 C CG2 . ILE B 228 ? 1.22912 1.37764 1.21798 -0.07724 0.00247  0.01100  228 ILE B CG2 
3733 C CD1 . ILE B 228 ? 0.85542 1.06250 0.92449 -0.06209 -0.02021 0.01910  228 ILE B CD1 
3734 N N   . SER B 229 ? 1.03040 1.12378 0.94637 -0.09459 -0.06601 0.03720  229 SER B N   
3735 C CA  . SER B 229 ? 1.03741 1.09805 0.91386 -0.10104 -0.07618 0.03540  229 SER B CA  
3736 C C   . SER B 229 ? 1.05386 1.14336 0.97452 -0.09237 -0.09462 0.04064  229 SER B C   
3737 O O   . SER B 229 ? 1.03145 1.11801 0.94622 -0.08885 -0.08973 0.03176  229 SER B O   
3738 C CB  . SER B 229 ? 1.07566 1.08045 0.88914 -0.11961 -0.10004 0.04710  229 SER B CB  
3739 O OG  . SER B 229 ? 1.19174 1.21382 1.04006 -0.12192 -0.12693 0.06606  229 SER B OG  
3740 N N   . GLN B 230 ? 1.02112 1.13605 0.98785 -0.08794 -0.11237 0.05617  230 GLN B N   
3741 C CA  . GLN B 230 ? 0.71308 0.85331 0.72744 -0.07745 -0.12372 0.06355  230 GLN B CA  
3742 C C   . GLN B 230 ? 0.81016 0.98223 0.85290 -0.06065 -0.10023 0.04813  230 GLN B C   
3743 O O   . GLN B 230 ? 0.81804 0.99642 0.87086 -0.05453 -0.10120 0.04389  230 GLN B O   
3744 C CB  . GLN B 230 ? 0.90815 1.06451 0.97004 -0.07378 -0.13781 0.08526  230 GLN B CB  
3745 C CG  . GLN B 230 ? 1.07034 1.19858 1.11715 -0.09056 -0.16620 0.10504  230 GLN B CG  
3746 C CD  . GLN B 230 ? 0.97165 1.11921 1.08242 -0.08457 -0.17717 0.13020  230 GLN B CD  
3747 O OE1 . GLN B 230 ? 1.03739 1.19158 1.15998 -0.08292 -0.16916 0.13649  230 GLN B OE1 
3748 N NE2 . GLN B 230 ? 0.85183 1.00697 1.00808 -0.08059 -0.19272 0.14606  230 GLN B NE2 
3749 N N   . ILE B 231 ? 0.86055 1.05080 0.91773 -0.05364 -0.08242 0.04115  231 ILE B N   
3750 C CA  . ILE B 231 ? 0.69761 0.91145 0.77837 -0.04014 -0.06621 0.02781  231 ILE B CA  
3751 C C   . ILE B 231 ? 0.90053 1.10812 0.96379 -0.04166 -0.05525 0.01372  231 ILE B C   
3752 O O   . ILE B 231 ? 0.91472 1.13505 0.99523 -0.03234 -0.05374 0.00837  231 ILE B O   
3753 C CB  . ILE B 231 ? 0.65664 0.88080 0.74773 -0.03761 -0.05435 0.02311  231 ILE B CB  
3754 C CG1 . ILE B 231 ? 0.72694 0.95454 0.83607 -0.03238 -0.06102 0.03648  231 ILE B CG1 
3755 C CG2 . ILE B 231 ? 0.75144 0.99215 0.86227 -0.02830 -0.04341 0.00964  231 ILE B CG2 
3756 C CD1 . ILE B 231 ? 0.83907 1.06453 0.94421 -0.03694 -0.05514 0.03675  231 ILE B CD1 
3757 N N   . SER B 232 ? 0.79957 0.98252 0.82604 -0.05287 -0.04445 0.00851  232 SER B N   
3758 C CA  . SER B 232 ? 0.73060 0.89874 0.73697 -0.05401 -0.02642 -0.00344 232 SER B CA  
3759 C C   . SER B 232 ? 0.80987 0.96689 0.80304 -0.05398 -0.03924 -0.00276 232 SER B C   
3760 O O   . SER B 232 ? 0.74789 0.91872 0.75936 -0.04523 -0.02976 -0.01116 232 SER B O   
3761 C CB  . SER B 232 ? 0.96001 1.08645 0.91465 -0.06665 -0.01057 -0.00553 232 SER B CB  
3762 O OG  . SER B 232 ? 1.15873 1.23988 1.05548 -0.07931 -0.02795 0.00047  232 SER B OG  
3763 N N   . ASN B 233 ? 0.90757 1.03807 0.87153 -0.06469 -0.06341 0.00864  233 ASN B N   
3764 C CA  . ASN B 233 ? 0.89602 1.01164 0.84812 -0.06699 -0.07957 0.01088  233 ASN B CA  
3765 C C   . ASN B 233 ? 0.91295 1.06997 0.92359 -0.05156 -0.08501 0.01364  233 ASN B C   
3766 O O   . ASN B 233 ? 0.89436 1.05049 0.90670 -0.04790 -0.08597 0.00921  233 ASN B O   
3767 C CB  . ASN B 233 ? 0.77333 0.85126 0.69121 -0.08338 -0.11216 0.02644  233 ASN B CB  
3768 C CG  . ASN B 233 ? 1.00698 1.04638 0.88496 -0.09241 -0.12740 0.02558  233 ASN B CG  
3769 O OD1 . ASN B 233 ? 0.97440 1.02978 0.88780 -0.08863 -0.14672 0.03368  233 ASN B OD1 
3770 N ND2 . ASN B 233 ? 1.22655 1.20908 1.02750 -0.10418 -0.11653 0.01613  233 ASN B ND2 
3771 N N   . MET B 234 ? 0.78170 0.96897 0.83520 -0.04197 -0.08611 0.02089  234 MET B N   
3772 C CA  . MET B 234 ? 0.73801 0.95224 0.83678 -0.02646 -0.08753 0.02484  234 MET B CA  
3773 C C   . MET B 234 ? 0.74704 0.97857 0.85612 -0.01487 -0.06889 0.00857  234 MET B C   
3774 O O   . MET B 234 ? 0.81919 1.05726 0.94115 -0.00721 -0.06956 0.00636  234 MET B O   
3775 C CB  . MET B 234 ? 0.66669 0.89500 0.79713 -0.01877 -0.08881 0.03734  234 MET B CB  
3776 C CG  . MET B 234 ? 0.56781 0.78535 0.71133 -0.02646 -0.10943 0.05963  234 MET B CG  
3777 S SD  . MET B 234 ? 0.90302 1.13140 1.08490 -0.01602 -0.10281 0.07615  234 MET B SD  
3778 C CE  . MET B 234 ? 0.65994 0.88140 0.81004 -0.02672 -0.09782 0.06950  234 MET B CE  
3779 N N   . ILE B 235 ? 0.88132 1.12004 0.98951 -0.01401 -0.05378 -0.00136 235 ILE B N   
3780 C CA  . ILE B 235 ? 0.81837 1.07384 0.94621 -0.00404 -0.04118 -0.01327 235 ILE B CA  
3781 C C   . ILE B 235 ? 0.91174 1.15735 1.02507 -0.00734 -0.02985 -0.02253 235 ILE B C   
3782 O O   . ILE B 235 ? 0.92266 1.18274 1.05823 0.00137  -0.02120 -0.03012 235 ILE B O   
3783 C CB  . ILE B 235 ? 0.64221 0.90785 0.78445 -0.00328 -0.03301 -0.01774 235 ILE B CB  
3784 C CG1 . ILE B 235 ? 0.65352 0.90458 0.77484 -0.01605 -0.02236 -0.01873 235 ILE B CG1 
3785 C CG2 . ILE B 235 ? 0.75484 1.02439 0.90704 0.00292  -0.04283 -0.01018 235 ILE B CG2 
3786 C CD1 . ILE B 235 ? 0.64042 0.90178 0.78206 -0.01636 -0.01725 -0.01991 235 ILE B CD1 
3787 N N   . GLY B 236 ? 0.91522 1.13046 0.98775 -0.02001 -0.02966 -0.02149 236 GLY B N   
3788 C CA  . GLY B 236 ? 0.95174 1.14414 0.99726 -0.02366 -0.01681 -0.02963 236 GLY B CA  
3789 C C   . GLY B 236 ? 1.00896 1.17326 1.02355 -0.03142 0.00967  -0.03626 236 GLY B C   
3790 O O   . GLY B 236 ? 1.21104 1.35721 1.21140 -0.03062 0.03075  -0.04395 236 GLY B O   
3791 N N   . ILE B 237 ? 0.91388 1.07072 0.91804 -0.03797 0.01279  -0.03265 237 ILE B N   
3792 C CA  . ILE B 237 ? 0.71719 0.84620 0.69732 -0.04361 0.04319  -0.03702 237 ILE B CA  
3793 C C   . ILE B 237 ? 0.98433 1.05340 0.88503 -0.05911 0.03890  -0.03374 237 ILE B C   
3794 O O   . ILE B 237 ? 0.95014 1.01314 0.83350 -0.06682 0.00876  -0.02448 237 ILE B O   
3795 C CB  . ILE B 237 ? 0.82451 0.98367 0.84917 -0.04033 0.05015  -0.03478 237 ILE B CB  
3796 C CG1 . ILE B 237 ? 0.70900 0.91368 0.80309 -0.02732 0.05200  -0.03798 237 ILE B CG1 
3797 C CG2 . ILE B 237 ? 0.99980 1.12580 0.99878 -0.04738 0.08137  -0.03556 237 ILE B CG2 
3798 C CD1 . ILE B 237 ? 0.85757 1.08722 0.99851 -0.02550 0.05527  -0.03544 237 ILE B CD1 
3799 N N   . SER B 238 ? 1.24974 1.26826 1.10016 -0.06378 0.06928  -0.03990 238 SER B N   
3800 C CA  . SER B 238 ? 1.47748 1.42002 1.23249 -0.07951 0.06574  -0.03822 238 SER B CA  
3801 C C   . SER B 238 ? 1.43367 1.35623 1.15994 -0.08928 0.06012  -0.03099 238 SER B C   
3802 O O   . SER B 238 ? 1.41967 1.32686 1.11678 -0.10026 0.02254  -0.02165 238 SER B O   
3803 C CB  . SER B 238 ? 1.62803 1.51319 1.33256 -0.07941 0.10999  -0.04712 238 SER B CB  
3804 O OG  . SER B 238 ? 1.35954 1.27849 1.12839 -0.06673 0.15129  -0.05024 238 SER B OG  
3805 N N   . SER B 239 ? 1.33590 1.25758 1.07475 -0.08567 0.09689  -0.03333 239 SER B N   
3806 C CA  . SER B 239 ? 1.34189 1.24199 1.05234 -0.09423 0.09695  -0.02704 239 SER B CA  
3807 C C   . SER B 239 ? 1.21597 1.18819 1.00914 -0.08720 0.08270  -0.02198 239 SER B C   
3808 O O   . SER B 239 ? 1.28582 1.31656 1.15364 -0.07519 0.08096  -0.02455 239 SER B O   
3809 C CB  . SER B 239 ? 1.47547 1.32257 1.14621 -0.09476 0.14950  -0.03089 239 SER B CB  
3810 O OG  . SER B 239 ? 1.47055 1.31709 1.14295 -0.09860 0.15561  -0.02503 239 SER B OG  
3811 N N   . ALA B 240 ? 1.22230 1.18302 0.99501 -0.09542 0.07146  -0.01440 240 ALA B N   
3812 C CA  . ALA B 240 ? 1.18386 1.20151 1.02454 -0.08967 0.06292  -0.00991 240 ALA B CA  
3813 C C   . ALA B 240 ? 1.21250 1.24345 1.09296 -0.08381 0.10136  -0.01361 240 ALA B C   
3814 O O   . ALA B 240 ? 1.17557 1.25997 1.12905 -0.07565 0.09773  -0.01344 240 ALA B O   
3815 C CB  . ALA B 240 ? 1.13501 1.13848 0.94659 -0.10015 0.03574  0.00124  240 ALA B CB  
3816 N N   . SER B 241 ? 1.34489 1.32173 1.17665 -0.08853 0.13769  -0.01518 241 SER B N   
3817 C CA  . SER B 241 ? 1.25572 1.24341 1.13646 -0.08229 0.17904  -0.01553 241 SER B CA  
3818 C C   . SER B 241 ? 1.17755 1.21263 1.13991 -0.06999 0.18971  -0.01932 241 SER B C   
3819 O O   . SER B 241 ? 1.19491 1.27655 1.23822 -0.06427 0.19255  -0.01636 241 SER B O   
3820 C CB  . SER B 241 ? 1.43461 1.34474 1.24342 -0.08710 0.22471  -0.01586 241 SER B CB  
3821 O OG  . SER B 241 ? 1.59768 1.46620 1.36300 -0.08537 0.24315  -0.02191 241 SER B OG  
3822 N N   . TYR B 242 ? 0.88391 0.90394 0.82539 -0.06684 0.19353  -0.02489 242 TYR B N   
3823 C CA  . TYR B 242 ? 0.91994 0.98506 0.93747 -0.05542 0.19825  -0.02754 242 TYR B CA  
3824 C C   . TYR B 242 ? 0.96402 1.09453 1.04675 -0.05077 0.15723  -0.02612 242 TYR B C   
3825 O O   . TYR B 242 ? 0.94634 1.11708 1.10773 -0.04410 0.15946  -0.02396 242 TYR B O   
3826 C CB  . TYR B 242 ? 1.03371 1.07136 1.00923 -0.05372 0.20174  -0.03394 242 TYR B CB  
3827 C CG  . TYR B 242 ? 1.13761 1.20719 1.18474 -0.04191 0.22025  -0.03570 242 TYR B CG  
3828 C CD1 . TYR B 242 ? 1.07309 1.14735 1.18115 -0.03591 0.26232  -0.03058 242 TYR B CD1 
3829 C CD2 . TYR B 242 ? 1.11280 1.20856 1.17393 -0.03657 0.19526  -0.04023 242 TYR B CD2 
3830 C CE1 . TYR B 242 ? 1.10414 1.20903 1.28721 -0.02561 0.27605  -0.02907 242 TYR B CE1 
3831 C CE2 . TYR B 242 ? 1.02044 1.14476 1.14721 -0.02613 0.20929  -0.04077 242 TYR B CE2 
3832 C CZ  . TYR B 242 ? 1.08478 1.21426 1.27365 -0.02103 0.24799  -0.03477 242 TYR B CZ  
3833 O OH  . TYR B 242 ? 1.03844 1.19733 1.30041 -0.01116 0.25854  -0.03252 242 TYR B OH  
3834 N N   . PHE B 243 ? 0.85890 0.99475 0.90925 -0.05435 0.11942  -0.02570 243 PHE B N   
3835 C CA  . PHE B 243 ? 0.85418 1.03835 0.95287 -0.04876 0.08620  -0.02396 243 PHE B CA  
3836 C C   . PHE B 243 ? 0.85515 1.06214 1.00001 -0.04924 0.08612  -0.01971 243 PHE B C   
3837 O O   . PHE B 243 ? 0.75810 0.99902 0.95890 -0.04326 0.07222  -0.01952 243 PHE B O   
3838 C CB  . PHE B 243 ? 0.99903 1.17848 1.05916 -0.05220 0.05381  -0.02028 243 PHE B CB  
3839 C CG  . PHE B 243 ? 0.90582 1.11965 1.00287 -0.04698 0.02892  -0.01632 243 PHE B CG  
3840 C CD1 . PHE B 243 ? 0.60610 0.84767 0.74093 -0.03662 0.01653  -0.01904 243 PHE B CD1 
3841 C CD2 . PHE B 243 ? 0.75150 0.96277 0.84018 -0.05228 0.02049  -0.00974 243 PHE B CD2 
3842 C CE1 . PHE B 243 ? 0.77958 1.03755 0.93353 -0.03173 -0.00269 -0.01564 243 PHE B CE1 
3843 C CE2 . PHE B 243 ? 0.65736 0.89003 0.77178 -0.04709 0.00242  -0.00616 243 PHE B CE2 
3844 C CZ  . PHE B 243 ? 0.82144 1.07367 0.96439 -0.03678 -0.00843 -0.00934 243 PHE B CZ  
3845 N N   . ILE B 244 ? 0.79797 0.98215 0.91465 -0.05731 0.09711  -0.01571 244 ILE B N   
3846 C CA  . ILE B 244 ? 0.67028 0.87389 0.82964 -0.05879 0.09647  -0.01118 244 ILE B CA  
3847 C C   . ILE B 244 ? 0.75098 0.97116 0.98045 -0.05486 0.11967  -0.00978 244 ILE B C   
3848 O O   . ILE B 244 ? 0.85928 1.10968 1.14840 -0.05341 0.10365  -0.00664 244 ILE B O   
3849 C CB  . ILE B 244 ? 0.70635 0.87968 0.81984 -0.06811 0.10580  -0.00656 244 ILE B CB  
3850 C CG1 . ILE B 244 ? 0.81357 0.97266 0.87062 -0.07282 0.07784  -0.00389 244 ILE B CG1 
3851 C CG2 . ILE B 244 ? 0.68631 0.88097 0.84611 -0.06966 0.10355  -0.00190 244 ILE B CG2 
3852 C CD1 . ILE B 244 ? 0.74637 0.87713 0.76115 -0.08253 0.08007  0.00252  244 ILE B CD1 
3853 N N   . ARG B 245 ? 0.82940 1.02499 1.05403 -0.05359 0.15774  -0.01023 245 ARG B N   
3854 C CA  . ARG B 245 ? 0.80431 1.01697 1.11094 -0.04893 0.18328  -0.00476 245 ARG B CA  
3855 C C   . ARG B 245 ? 0.76413 1.01744 1.13351 -0.04211 0.15681  -0.00542 245 ARG B C   
3856 O O   . ARG B 245 ? 0.77955 1.06160 1.22958 -0.04134 0.14809  0.00178  245 ARG B O   
3857 C CB  . ARG B 245 ? 0.96151 1.13260 1.24866 -0.04674 0.23634  -0.00381 245 ARG B CB  
3858 C CG  . ARG B 245 ? 1.03373 1.14986 1.24890 -0.05337 0.26757  -0.00256 245 ARG B CG  
3859 C CD  . ARG B 245 ? 1.10879 1.17780 1.31737 -0.04905 0.32947  0.00079  245 ARG B CD  
3860 N NE  . ARG B 245 ? 1.03483 1.08906 1.22376 -0.04341 0.33976  -0.00509 245 ARG B NE  
3861 C CZ  . ARG B 245 ? 1.15434 1.14368 1.24100 -0.04636 0.35731  -0.01188 245 ARG B CZ  
3862 N NH1 . ARG B 245 ? 1.33484 1.26918 1.32224 -0.05620 0.35554  -0.01407 245 ARG B NH1 
3863 N NH2 . ARG B 245 ? 1.18273 1.15859 1.26362 -0.04030 0.37309  -0.01607 245 ARG B NH2 
3864 N N   . ILE B 246 ? 0.64746 0.90042 0.98105 -0.03794 0.14114  -0.01280 246 ILE B N   
3865 C CA  . ILE B 246 ? 0.68168 0.96720 1.06575 -0.03110 0.11602  -0.01353 246 ILE B CA  
3866 C C   . ILE B 246 ? 0.73719 1.04434 1.13506 -0.03242 0.07256  -0.01255 246 ILE B C   
3867 O O   . ILE B 246 ? 0.58555 0.91424 1.04293 -0.03054 0.05213  -0.00854 246 ILE B O   
3868 C CB  . ILE B 246 ? 0.72694 1.00349 1.06740 -0.02584 0.11331  -0.02132 246 ILE B CB  
3869 C CG1 . ILE B 246 ? 0.64297 0.88810 0.96389 -0.02485 0.15785  -0.02252 246 ILE B CG1 
3870 C CG2 . ILE B 246 ? 0.77659 1.08334 1.16574 -0.01827 0.08829  -0.02171 246 ILE B CG2 
3871 C CD1 . ILE B 246 ? 0.83210 1.08953 1.23587 -0.01992 0.18797  -0.01472 246 ILE B CD1 
3872 N N   . PHE B 247 ? 0.69658 0.99236 1.03734 -0.03591 0.05702  -0.01500 247 PHE B N   
3873 C CA  . PHE B 247 ? 0.63881 0.94386 0.98296 -0.03661 0.02285  -0.01364 247 PHE B CA  
3874 C C   . PHE B 247 ? 0.60243 0.91750 1.00452 -0.04213 0.01902  -0.00685 247 PHE B C   
3875 O O   . PHE B 247 ? 0.58223 0.90607 1.01698 -0.04196 -0.01056 -0.00470 247 PHE B O   
3876 C CB  . PHE B 247 ? 0.55921 0.84793 0.84086 -0.03956 0.01645  -0.01403 247 PHE B CB  
3877 C CG  . PHE B 247 ? 0.67928 0.96803 0.95155 -0.03794 -0.01273 -0.01261 247 PHE B CG  
3878 C CD1 . PHE B 247 ? 0.63595 0.92382 0.92653 -0.04360 -0.02105 -0.00886 247 PHE B CD1 
3879 C CD2 . PHE B 247 ? 0.72501 1.00827 0.96639 -0.03059 -0.02832 -0.01405 247 PHE B CD2 
3880 C CE1 . PHE B 247 ? 0.55337 0.82991 0.82418 -0.04213 -0.04456 -0.00785 247 PHE B CE1 
3881 C CE2 . PHE B 247 ? 0.71322 0.98511 0.93819 -0.02767 -0.04750 -0.01183 247 PHE B CE2 
3882 C CZ  . PHE B 247 ? 0.55100 0.81683 0.78631 -0.03363 -0.05550 -0.00935 247 PHE B CZ  
3883 N N   . ASN B 248 ? 0.56892 0.87741 0.98306 -0.04763 0.04798  -0.00241 248 ASN B N   
3884 C CA  . ASN B 248 ? 0.56881 0.88785 1.04815 -0.05322 0.04677  0.00629  248 ASN B CA  
3885 C C   . ASN B 248 ? 0.60065 0.94015 1.16553 -0.05083 0.04196  0.01311  248 ASN B C   
3886 O O   . ASN B 248 ? 0.55001 0.90060 1.16547 -0.05498 0.00971  0.01935  248 ASN B O   
3887 C CB  . ASN B 248 ? 0.63423 0.93807 1.10947 -0.05780 0.08659  0.01072  248 ASN B CB  
3888 C CG  . ASN B 248 ? 0.61825 0.92825 1.13605 -0.06518 0.07928  0.01880  248 ASN B CG  
3889 O OD1 . ASN B 248 ? 0.68486 1.00621 1.22652 -0.06817 0.04102  0.02035  248 ASN B OD1 
3890 N ND2 . ASN B 248 ? 0.64734 0.94418 1.17430 -0.06827 0.11719  0.02465  248 ASN B ND2 
3891 N N   . LYS B 249 ? 0.61250 0.95282 1.19463 -0.04495 0.07259  0.01341  249 LYS B N   
3892 C CA  . LYS B 249 ? 0.55396 0.91473 1.22686 -0.04197 0.07222  0.02279  249 LYS B CA  
3893 C C   . LYS B 249 ? 0.53402 0.90724 1.21681 -0.04051 0.02156  0.02087  249 LYS B C   
3894 O O   . LYS B 249 ? 0.63346 1.02194 1.39612 -0.04338 -0.00185 0.03193  249 LYS B O   
3895 C CB  . LYS B 249 ? 0.56873 0.92045 1.24057 -0.03444 0.11804  0.02178  249 LYS B CB  
3896 C CG  . LYS B 249 ? 0.56032 0.93217 1.32814 -0.02947 0.12586  0.03297  249 LYS B CG  
3897 C CD  . LYS B 249 ? 0.90713 1.26243 1.64390 -0.02082 0.16623  0.02731  249 LYS B CD  
3898 C CE  . LYS B 249 ? 1.19895 1.51628 1.89491 -0.02063 0.22584  0.02724  249 LYS B CE  
3899 N NZ  . LYS B 249 ? 0.93839 1.22504 1.58841 -0.01352 0.26649  0.02112  249 LYS B NZ  
3900 N N   . HIS B 250 ? 0.66958 1.03172 1.27225 -0.03669 0.00262  0.00877  250 HIS B N   
3901 C CA  . HIS B 250 ? 0.63434 0.99728 1.22997 -0.03335 -0.03907 0.00603  250 HIS B CA  
3902 C C   . HIS B 250 ? 0.63799 0.98785 1.22233 -0.04017 -0.08094 0.00795  250 HIS B C   
3903 O O   . HIS B 250 ? 0.57709 0.92712 1.20895 -0.04443 -0.11540 0.01542  250 HIS B O   
3904 C CB  . HIS B 250 ? 0.72418 1.07657 1.24234 -0.02510 -0.03574 -0.00570 250 HIS B CB  
3905 C CG  . HIS B 250 ? 0.74381 1.08999 1.24468 -0.01963 -0.07130 -0.00877 250 HIS B CG  
3906 N ND1 . HIS B 250 ? 0.68743 1.01094 1.13706 -0.01981 -0.10051 -0.01165 250 HIS B ND1 
3907 C CD2 . HIS B 250 ? 0.61755 0.97082 1.13978 -0.01312 -0.07941 -0.00902 250 HIS B CD2 
3908 C CE1 . HIS B 250 ? 0.61091 0.92351 1.04643 -0.01355 -0.12417 -0.01370 250 HIS B CE1 
3909 N NE2 . HIS B 250 ? 0.60919 0.94212 1.08995 -0.00976 -0.11403 -0.01219 250 HIS B NE2 
3910 N N   . TYR B 251 ? 0.53616 0.86957 1.05660 -0.04211 -0.07980 0.00249  251 TYR B N   
3911 C CA  . TYR B 251 ? 0.55313 0.86477 1.04926 -0.04768 -0.11533 0.00328  251 TYR B CA  
3912 C C   . TYR B 251 ? 0.65942 0.97546 1.20997 -0.05908 -0.12050 0.01270  251 TYR B C   
3913 O O   . TYR B 251 ? 0.68660 0.98248 1.23538 -0.06612 -0.15782 0.01579  251 TYR B O   
3914 C CB  . TYR B 251 ? 0.55816 0.84913 0.97009 -0.04397 -0.10986 -0.00406 251 TYR B CB  
3915 C CG  . TYR B 251 ? 0.57734 0.85486 0.93631 -0.03326 -0.11608 -0.01056 251 TYR B CG  
3916 C CD1 . TYR B 251 ? 0.66159 0.91164 0.99647 -0.03041 -0.14849 -0.01156 251 TYR B CD1 
3917 C CD2 . TYR B 251 ? 0.59670 0.88257 0.92662 -0.02651 -0.09041 -0.01463 251 TYR B CD2 
3918 C CE1 . TYR B 251 ? 0.58383 0.81747 0.87058 -0.01919 -0.14962 -0.01632 251 TYR B CE1 
3919 C CE2 . TYR B 251 ? 0.62432 0.89898 0.91468 -0.01642 -0.09531 -0.01851 251 TYR B CE2 
3920 C CZ  . TYR B 251 ? 0.56299 0.81275 0.83370 -0.01187 -0.12211 -0.01926 251 TYR B CZ  
3921 O OH  . TYR B 251 ? 0.73946 0.97399 0.97136 -0.00052 -0.12253 -0.02198 251 TYR B OH  
3922 N N   . GLY B 252 ? 0.58557 0.92127 1.18212 -0.06127 -0.08384 0.01806  252 GLY B N   
3923 C CA  . GLY B 252 ? 0.55992 0.89984 1.21070 -0.07123 -0.08361 0.02818  252 GLY B CA  
3924 C C   . GLY B 252 ? 0.59992 0.92644 1.19810 -0.07495 -0.07070 0.02451  252 GLY B C   
3925 O O   . GLY B 252 ? 0.69855 1.02698 1.33862 -0.08336 -0.07062 0.03269  252 GLY B O   
3926 N N   . VAL B 253 ? 0.66100 0.97391 1.17456 -0.06937 -0.06215 0.01438  253 VAL B N   
3927 C CA  . VAL B 253 ? 0.57405 0.87403 1.03878 -0.07261 -0.05098 0.01270  253 VAL B CA  
3928 C C   . VAL B 253 ? 0.60107 0.89846 1.01439 -0.06743 -0.01888 0.00780  253 VAL B C   
3929 O O   . VAL B 253 ? 0.67152 0.97276 1.07313 -0.06082 -0.01088 0.00361  253 VAL B O   
3930 C CB  . VAL B 253 ? 0.67001 0.94532 1.08021 -0.07312 -0.08245 0.00919  253 VAL B CB  
3931 C CG1 . VAL B 253 ? 0.69394 0.95849 1.14095 -0.08200 -0.11663 0.01453  253 VAL B CG1 
3932 C CG2 . VAL B 253 ? 0.72725 0.99136 1.08928 -0.06324 -0.09439 0.00250  253 VAL B CG2 
3933 N N   . THR B 254 ? 0.66046 0.94797 1.04337 -0.07175 -0.00233 0.00936  254 THR B N   
3934 C CA  . THR B 254 ? 0.80052 1.07624 1.12459 -0.06952 0.01769  0.00645  254 THR B CA  
3935 C C   . THR B 254 ? 0.84132 1.10878 1.11431 -0.06464 -0.00438 0.00358  254 THR B C   
3936 O O   . THR B 254 ? 0.73315 0.99476 1.00101 -0.06431 -0.02622 0.00439  254 THR B O   
3937 C CB  . THR B 254 ? 0.75632 1.01879 1.06191 -0.07645 0.03982  0.01086  254 THR B CB  
3938 O OG1 . THR B 254 ? 0.93659 1.19527 1.23094 -0.08011 0.02106  0.01345  254 THR B OG1 
3939 C CG2 . THR B 254 ? 0.81198 1.07876 1.17396 -0.07986 0.06672  0.01605  254 THR B CG2 
3940 N N   . PRO B 255 ? 0.78342 1.04531 1.01868 -0.06071 0.00198  0.00153  255 PRO B N   
3941 C CA  . PRO B 255 ? 0.70838 0.96218 0.90550 -0.05577 -0.01441 0.00303  255 PRO B CA  
3942 C C   . PRO B 255 ? 0.81312 1.05604 0.99236 -0.05956 -0.01924 0.00924  255 PRO B C   
3943 O O   . PRO B 255 ? 0.81348 1.04769 0.97866 -0.05424 -0.03276 0.01176  255 PRO B O   
3944 C CB  . PRO B 255 ? 0.71601 0.96289 0.88161 -0.05560 -0.00473 0.00332  255 PRO B CB  
3945 C CG  . PRO B 255 ? 0.61067 0.86242 0.79712 -0.05576 0.01277  -0.00228 255 PRO B CG  
3946 C CD  . PRO B 255 ? 0.66608 0.92368 0.89245 -0.06064 0.02457  -0.00086 255 PRO B CD  
3947 N N   . LYS B 256 ? 0.89581 1.13463 1.07390 -0.06797 -0.00498 0.01244  256 LYS B N   
3948 C CA  . LYS B 256 ? 1.00125 1.23090 1.16740 -0.07216 -0.00824 0.01862  256 LYS B CA  
3949 C C   . LYS B 256 ? 1.02402 1.25315 1.21236 -0.07141 -0.02306 0.01702  256 LYS B C   
3950 O O   . LYS B 256 ? 1.08412 1.29907 1.25193 -0.06877 -0.03293 0.02049  256 LYS B O   
3951 C CB  . LYS B 256 ? 1.09135 1.31407 1.25281 -0.08131 0.01166  0.02181  256 LYS B CB  
3952 C CG  . LYS B 256 ? 1.22385 1.43947 1.38087 -0.08630 0.00981  0.02794  256 LYS B CG  
3953 C CD  . LYS B 256 ? 1.13128 1.34687 1.31322 -0.09356 0.02851  0.02838  256 LYS B CD  
3954 C CE  . LYS B 256 ? 1.35895 1.57323 1.55431 -0.09749 0.02082  0.03212  256 LYS B CE  
3955 N NZ  . LYS B 256 ? 1.17353 1.39155 1.38930 -0.09404 -0.00313 0.02872  256 LYS B NZ  
3956 N N   . GLN B 257 ? 1.00832 1.24756 1.23909 -0.07454 -0.02464 0.01354  257 GLN B N   
3957 C CA  . GLN B 257 ? 0.95474 1.18667 1.20582 -0.07696 -0.04624 0.01309  257 GLN B CA  
3958 C C   . GLN B 257 ? 1.04385 1.25760 1.26578 -0.06895 -0.06784 0.00983  257 GLN B C   
3959 O O   . GLN B 257 ? 1.06526 1.25222 1.26028 -0.06875 -0.08128 0.01086  257 GLN B O   
3960 C CB  . GLN B 257 ? 0.97576 1.22375 1.28997 -0.08197 -0.04803 0.01336  257 GLN B CB  
3961 C CG  . GLN B 257 ? 1.09630 1.35216 1.44731 -0.09036 -0.02872 0.01907  257 GLN B CG  
3962 C CD  . GLN B 257 ? 1.04235 1.31698 1.46456 -0.09223 -0.01799 0.02262  257 GLN B CD  
3963 O OE1 . GLN B 257 ? 1.01428 1.29808 1.45414 -0.08713 -0.02302 0.02022  257 GLN B OE1 
3964 N NE2 . GLN B 257 ? 1.38119 1.66104 1.84993 -0.09887 -0.00081 0.03004  257 GLN B NE2 
3965 N N   . PHE B 258 ? 1.11104 1.33329 1.33476 -0.06199 -0.06913 0.00598  258 PHE B N   
3966 C CA  . PHE B 258 ? 0.94873 1.15030 1.14070 -0.05264 -0.08436 0.00333  258 PHE B CA  
3967 C C   . PHE B 258 ? 0.97724 1.15633 1.12246 -0.04638 -0.07720 0.00807  258 PHE B C   
3968 O O   . PHE B 258 ? 1.16986 1.31365 1.28277 -0.04243 -0.08722 0.00859  258 PHE B O   
3969 C CB  . PHE B 258 ? 0.81667 1.03569 1.01878 -0.04588 -0.07986 -0.00037 258 PHE B CB  
3970 C CG  . PHE B 258 ? 0.91770 1.11498 1.09076 -0.03560 -0.09338 -0.00290 258 PHE B CG  
3971 C CD1 . PHE B 258 ? 1.05168 1.23455 1.23289 -0.03596 -0.11729 -0.00629 258 PHE B CD1 
3972 C CD2 . PHE B 258 ? 0.95554 1.14270 1.09474 -0.02583 -0.08292 0.00006  258 PHE B CD2 
3973 C CE1 . PHE B 258 ? 1.09189 1.24582 1.23639 -0.02617 -0.12820 -0.00860 258 PHE B CE1 
3974 C CE2 . PHE B 258 ? 0.82798 0.99019 0.93969 -0.01488 -0.08977 -0.00118 258 PHE B CE2 
3975 C CZ  . PHE B 258 ? 0.82425 0.96737 0.93271 -0.01475 -0.11123 -0.00647 258 PHE B CZ  
3976 N N   . PHE B 259 ? 0.98159 1.17494 1.12189 -0.04561 -0.05977 0.01320  259 PHE B N   
3977 C CA  . PHE B 259 ? 1.02630 1.20251 1.13815 -0.03960 -0.05263 0.02214  259 PHE B CA  
3978 C C   . PHE B 259 ? 1.08690 1.24042 1.18454 -0.04320 -0.05288 0.02619  259 PHE B C   
3979 O O   . PHE B 259 ? 1.16161 1.28215 1.23053 -0.03544 -0.05186 0.03009  259 PHE B O   
3980 C CB  . PHE B 259 ? 0.94337 1.13745 1.05868 -0.04210 -0.04160 0.02944  259 PHE B CB  
3981 C CG  . PHE B 259 ? 1.03632 1.21737 1.13914 -0.03569 -0.03675 0.04289  259 PHE B CG  
3982 C CD1 . PHE B 259 ? 1.06788 1.24193 1.16819 -0.02408 -0.03576 0.04738  259 PHE B CD1 
3983 C CD2 . PHE B 259 ? 1.07756 1.25273 1.17751 -0.04070 -0.03164 0.05319  259 PHE B CD2 
3984 C CE1 . PHE B 259 ? 1.16716 1.32939 1.26967 -0.01724 -0.02808 0.06372  259 PHE B CE1 
3985 C CE2 . PHE B 259 ? 0.89137 1.05548 0.99203 -0.03439 -0.02624 0.06928  259 PHE B CE2 
3986 C CZ  . PHE B 259 ? 0.97810 1.13612 1.08373 -0.02249 -0.02365 0.07545  259 PHE B CZ  
3987 N N   . THR B 260 ? 1.20939 1.37532 1.32456 -0.05430 -0.05083 0.02596  260 THR B N   
3988 C CA  . THR B 260 ? 1.21271 1.35834 1.31563 -0.05848 -0.05034 0.03021  260 THR B CA  
3989 C C   . THR B 260 ? 1.28896 1.39905 1.37245 -0.05749 -0.06717 0.02490  260 THR B C   
3990 O O   . THR B 260 ? 1.33270 1.40719 1.38398 -0.05510 -0.06506 0.02883  260 THR B O   
3991 C CB  . THR B 260 ? 1.25561 1.42045 1.38397 -0.07053 -0.04443 0.03073  260 THR B CB  
3992 O OG1 . THR B 260 ? 1.32382 1.51058 1.45881 -0.07257 -0.03130 0.03350  260 THR B OG1 
3993 C CG2 . THR B 260 ? 1.23208 1.37932 1.34561 -0.07392 -0.03958 0.03772  260 THR B CG2 
3994 N N   . TYR B 261 ? 1.06508 1.17804 1.16464 -0.05983 -0.08505 0.01704  261 TYR B N   
3995 C CA  . TYR B 261 ? 1.06866 1.13761 1.14128 -0.06116 -0.10857 0.01296  261 TYR B CA  
3996 C C   . TYR B 261 ? 1.08967 1.11124 1.10257 -0.04792 -0.10372 0.01400  261 TYR B C   
3997 O O   . TYR B 261 ? 1.21400 1.18010 1.17909 -0.04771 -0.11125 0.01380  261 TYR B O   
3998 C CB  . TYR B 261 ? 1.11537 1.19623 1.22286 -0.06662 -0.13278 0.00742  261 TYR B CB  
3999 C CG  . TYR B 261 ? 0.94524 0.97822 1.03107 -0.07405 -0.16651 0.00530  261 TYR B CG  
4000 C CD1 . TYR B 261 ? 1.03753 1.06526 1.14546 -0.08745 -0.18017 0.00787  261 TYR B CD1 
4001 C CD2 . TYR B 261 ? 0.82289 0.80831 0.85987 -0.06833 -0.18600 0.00150  261 TYR B CD2 
4002 C CE1 . TYR B 261 ? 1.10849 1.08531 1.19284 -0.09665 -0.21703 0.00700  261 TYR B CE1 
4003 C CE2 . TYR B 261 ? 1.04183 0.97036 1.04584 -0.07714 -0.22199 0.00006  261 TYR B CE2 
4004 C CZ  . TYR B 261 ? 1.10775 1.03204 1.13629 -0.09211 -0.23968 0.00297  261 TYR B CZ  
4005 O OH  . TYR B 261 ? 1.16909 1.03064 1.16262 -0.10338 -0.28178 0.00255  261 TYR B OH  
4006 N N   . PHE B 262 ? 1.05431 1.09096 1.06682 -0.03661 -0.08858 0.01620  262 PHE B N   
4007 C CA  . PHE B 262 ? 1.23355 1.22523 1.19754 -0.02207 -0.07888 0.01901  262 PHE B CA  
4008 C C   . PHE B 262 ? 1.27470 1.26027 1.23087 -0.01308 -0.04974 0.03188  262 PHE B C   
4009 O O   . PHE B 262 ? 1.26909 1.22211 1.19779 0.00114  -0.03353 0.03789  262 PHE B O   
4010 C CB  . PHE B 262 ? 1.18367 1.19069 1.15659 -0.01407 -0.08156 0.01530  262 PHE B CB  
4011 C CG  . PHE B 262 ? 1.17268 1.17144 1.14682 -0.01990 -0.11101 0.00549  262 PHE B CG  
4012 C CD1 . PHE B 262 ? 1.18932 1.12272 1.10569 -0.01634 -0.12713 0.00201  262 PHE B CD1 
4013 C CD2 . PHE B 262 ? 1.18385 1.23386 1.21532 -0.02882 -0.12203 0.00148  262 PHE B CD2 
4014 C CE1 . PHE B 262 ? 1.18581 1.10874 1.10578 -0.02328 -0.16057 -0.00447 262 PHE B CE1 
4015 C CE2 . PHE B 262 ? 1.20089 1.24540 1.24607 -0.03418 -0.15022 -0.00389 262 PHE B CE2 
4016 C CZ  . PHE B 262 ? 1.12916 1.11186 1.12057 -0.03221 -0.17296 -0.00645 262 PHE B CZ  
4017 N N   . LYS B 263 ? 1.29226 1.30571 1.27507 -0.02066 -0.04192 0.03815  263 LYS B N   
4018 C CA  . LYS B 263 ? 1.27605 1.28215 1.25869 -0.01389 -0.01816 0.05348  263 LYS B CA  
4019 C C   . LYS B 263 ? 1.24402 1.26262 1.24382 -0.00166 -0.00365 0.06425  263 LYS B C   
4020 O O   . LYS B 263 ? 1.04781 1.09166 1.06309 -0.00069 -0.01213 0.05861  263 LYS B O   
4021 C CB  . LYS B 263 ? 1.30194 1.24286 1.23464 -0.00787 -0.00721 0.05675  263 LYS B CB  
4022 C CG  . LYS B 263 ? 1.38652 1.31272 1.30552 -0.02129 -0.02154 0.04980  263 LYS B CG  
4023 C CD  . LYS B 263 ? 1.35820 1.33134 1.32061 -0.03120 -0.01710 0.05630  263 LYS B CD  
4024 C CE  . LYS B 263 ? 1.44726 1.42232 1.41402 -0.04641 -0.03499 0.04770  263 LYS B CE  
4025 N NZ  . LYS B 263 ? 1.54786 1.57066 1.55683 -0.05586 -0.02947 0.05280  263 LYS B NZ  
# 
