data_9O8N
# 
_entry.id   9O8N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9O8N         pdb_00009o8n 10.2210/pdb9o8n/pdb 
WWPDB D_1000295104 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        9O8N 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-16 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (dapD) from Bordetella pertussis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ung, A.R.'      1 0000-0002-9906-0710 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Cooper, A.'     3 0000-0002-1893-4149 
primary 'Battaile, K.P.' 4 0000-0003-0833-3259 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase' 29966.992 1   2.3.1.117 ? ? ? 
2 non-polymer syn 'CALCIUM ION'                                                        40.078    3   ?         ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                       35.453    3   ?         ? ? ? 
4 non-polymer syn GLYCEROL                                                             92.094    1   ?         ? ? ? 
5 water       nat water                                                                18.015    232 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Tetrahydrodipicolinate N-succinyltransferase,THDP succinyltransferase,THP succinyltransferase,Tetrahydropicolinate succinylase' 
# 
_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       
;MAHHHHHHTLDLQTTIEQAWENRANLSPVDASAEVRDAVEHTIDGLDLGRLRVAEKIDDQWIVHQWIKKAVLLSFRLHDN
AVMGQGPLQFYDKVPTKFAGYGEAAFKAGGYRVVPPAVARRGAFIARNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQI
GKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEENSVLAMGVFLSQSTKIYDRATGKVSYGRVPSGSV
VVPGSLPSEDGSHSLACAVIVKRVDAQTRAKTSINDLL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHTLDLQTTIEQAWENRANLSPVDASAEVRDAVEHTIDGLDLGRLRVAEKIDDQWIVHQWIKKAVLLSFRLHDN
AVMGQGPLQFYDKVPTKFAGYGEAAFKAGGYRVVPPAVARRGAFIARNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQI
GKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEENSVLAMGVFLSQSTKIYDRATGKVSYGRVPSGSV
VVPGSLPSEDGSHSLACAVIVKRVDAQTRAKTSINDLL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'  CA  
3 'CHLORIDE ION' CL  
4 GLYCEROL       GOL 
5 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   THR n 
1 10  LEU n 
1 11  ASP n 
1 12  LEU n 
1 13  GLN n 
1 14  THR n 
1 15  THR n 
1 16  ILE n 
1 17  GLU n 
1 18  GLN n 
1 19  ALA n 
1 20  TRP n 
1 21  GLU n 
1 22  ASN n 
1 23  ARG n 
1 24  ALA n 
1 25  ASN n 
1 26  LEU n 
1 27  SER n 
1 28  PRO n 
1 29  VAL n 
1 30  ASP n 
1 31  ALA n 
1 32  SER n 
1 33  ALA n 
1 34  GLU n 
1 35  VAL n 
1 36  ARG n 
1 37  ASP n 
1 38  ALA n 
1 39  VAL n 
1 40  GLU n 
1 41  HIS n 
1 42  THR n 
1 43  ILE n 
1 44  ASP n 
1 45  GLY n 
1 46  LEU n 
1 47  ASP n 
1 48  LEU n 
1 49  GLY n 
1 50  ARG n 
1 51  LEU n 
1 52  ARG n 
1 53  VAL n 
1 54  ALA n 
1 55  GLU n 
1 56  LYS n 
1 57  ILE n 
1 58  ASP n 
1 59  ASP n 
1 60  GLN n 
1 61  TRP n 
1 62  ILE n 
1 63  VAL n 
1 64  HIS n 
1 65  GLN n 
1 66  TRP n 
1 67  ILE n 
1 68  LYS n 
1 69  LYS n 
1 70  ALA n 
1 71  VAL n 
1 72  LEU n 
1 73  LEU n 
1 74  SER n 
1 75  PHE n 
1 76  ARG n 
1 77  LEU n 
1 78  HIS n 
1 79  ASP n 
1 80  ASN n 
1 81  ALA n 
1 82  VAL n 
1 83  MET n 
1 84  GLY n 
1 85  GLN n 
1 86  GLY n 
1 87  PRO n 
1 88  LEU n 
1 89  GLN n 
1 90  PHE n 
1 91  TYR n 
1 92  ASP n 
1 93  LYS n 
1 94  VAL n 
1 95  PRO n 
1 96  THR n 
1 97  LYS n 
1 98  PHE n 
1 99  ALA n 
1 100 GLY n 
1 101 TYR n 
1 102 GLY n 
1 103 GLU n 
1 104 ALA n 
1 105 ALA n 
1 106 PHE n 
1 107 LYS n 
1 108 ALA n 
1 109 GLY n 
1 110 GLY n 
1 111 TYR n 
1 112 ARG n 
1 113 VAL n 
1 114 VAL n 
1 115 PRO n 
1 116 PRO n 
1 117 ALA n 
1 118 VAL n 
1 119 ALA n 
1 120 ARG n 
1 121 ARG n 
1 122 GLY n 
1 123 ALA n 
1 124 PHE n 
1 125 ILE n 
1 126 ALA n 
1 127 ARG n 
1 128 ASN n 
1 129 VAL n 
1 130 VAL n 
1 131 LEU n 
1 132 MET n 
1 133 PRO n 
1 134 SER n 
1 135 TYR n 
1 136 VAL n 
1 137 ASN n 
1 138 ILE n 
1 139 GLY n 
1 140 ALA n 
1 141 TYR n 
1 142 VAL n 
1 143 ASP n 
1 144 GLU n 
1 145 GLY n 
1 146 THR n 
1 147 MET n 
1 148 VAL n 
1 149 ASP n 
1 150 THR n 
1 151 TRP n 
1 152 ALA n 
1 153 THR n 
1 154 VAL n 
1 155 GLY n 
1 156 SER n 
1 157 CYS n 
1 158 ALA n 
1 159 GLN n 
1 160 ILE n 
1 161 GLY n 
1 162 LYS n 
1 163 ASN n 
1 164 VAL n 
1 165 HIS n 
1 166 LEU n 
1 167 SER n 
1 168 GLY n 
1 169 GLY n 
1 170 VAL n 
1 171 GLY n 
1 172 ILE n 
1 173 GLY n 
1 174 GLY n 
1 175 VAL n 
1 176 LEU n 
1 177 GLU n 
1 178 PRO n 
1 179 LEU n 
1 180 GLN n 
1 181 ALA n 
1 182 ASN n 
1 183 PRO n 
1 184 THR n 
1 185 ILE n 
1 186 ILE n 
1 187 GLU n 
1 188 ASP n 
1 189 ASN n 
1 190 CYS n 
1 191 PHE n 
1 192 ILE n 
1 193 GLY n 
1 194 ALA n 
1 195 ARG n 
1 196 SER n 
1 197 GLU n 
1 198 VAL n 
1 199 VAL n 
1 200 GLU n 
1 201 GLY n 
1 202 VAL n 
1 203 VAL n 
1 204 VAL n 
1 205 GLU n 
1 206 GLU n 
1 207 ASN n 
1 208 SER n 
1 209 VAL n 
1 210 LEU n 
1 211 ALA n 
1 212 MET n 
1 213 GLY n 
1 214 VAL n 
1 215 PHE n 
1 216 LEU n 
1 217 SER n 
1 218 GLN n 
1 219 SER n 
1 220 THR n 
1 221 LYS n 
1 222 ILE n 
1 223 TYR n 
1 224 ASP n 
1 225 ARG n 
1 226 ALA n 
1 227 THR n 
1 228 GLY n 
1 229 LYS n 
1 230 VAL n 
1 231 SER n 
1 232 TYR n 
1 233 GLY n 
1 234 ARG n 
1 235 VAL n 
1 236 PRO n 
1 237 SER n 
1 238 GLY n 
1 239 SER n 
1 240 VAL n 
1 241 VAL n 
1 242 VAL n 
1 243 PRO n 
1 244 GLY n 
1 245 SER n 
1 246 LEU n 
1 247 PRO n 
1 248 SER n 
1 249 GLU n 
1 250 ASP n 
1 251 GLY n 
1 252 SER n 
1 253 HIS n 
1 254 SER n 
1 255 LEU n 
1 256 ALA n 
1 257 CYS n 
1 258 ALA n 
1 259 VAL n 
1 260 ILE n 
1 261 VAL n 
1 262 LYS n 
1 263 ARG n 
1 264 VAL n 
1 265 ASP n 
1 266 ALA n 
1 267 GLN n 
1 268 THR n 
1 269 ARG n 
1 270 ALA n 
1 271 LYS n 
1 272 THR n 
1 273 SER n 
1 274 ILE n 
1 275 ASN n 
1 276 ASP n 
1 277 LEU n 
1 278 LEU 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                   278 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'dapD, BP1764' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Bordetella pertussis Tohama I' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     257313 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       BopeA.00002.a.B2 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'   ?                               'Ca 2'           40.078  
CL  non-polymer         . 'CHLORIDE ION'  ?                               'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
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   -6  ?   ?   ?   A . n 
A 1 2   ALA 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   HIS 8   1   1   HIS HIS A . n 
A 1 9   THR 9   2   2   THR THR A . n 
A 1 10  LEU 10  3   3   LEU LEU A . n 
A 1 11  ASP 11  4   4   ASP ASP A . n 
A 1 12  LEU 12  5   5   LEU LEU A . n 
A 1 13  GLN 13  6   6   GLN GLN A . n 
A 1 14  THR 14  7   7   THR THR A . n 
A 1 15  THR 15  8   8   THR THR A . n 
A 1 16  ILE 16  9   9   ILE ILE A . n 
A 1 17  GLU 17  10  10  GLU GLU A . n 
A 1 18  GLN 18  11  11  GLN GLN A . n 
A 1 19  ALA 19  12  12  ALA ALA A . n 
A 1 20  TRP 20  13  13  TRP TRP A . n 
A 1 21  GLU 21  14  14  GLU GLU A . n 
A 1 22  ASN 22  15  15  ASN ASN A . n 
A 1 23  ARG 23  16  16  ARG ARG A . n 
A 1 24  ALA 24  17  17  ALA ALA A . n 
A 1 25  ASN 25  18  18  ASN ASN A . n 
A 1 26  LEU 26  19  19  LEU LEU A . n 
A 1 27  SER 27  20  20  SER SER A . n 
A 1 28  PRO 28  21  21  PRO PRO A . n 
A 1 29  VAL 29  22  22  VAL VAL A . n 
A 1 30  ASP 30  23  23  ASP ASP A . n 
A 1 31  ALA 31  24  24  ALA ALA A . n 
A 1 32  SER 32  25  25  SER SER A . n 
A 1 33  ALA 33  26  26  ALA ALA A . n 
A 1 34  GLU 34  27  27  GLU GLU A . n 
A 1 35  VAL 35  28  28  VAL VAL A . n 
A 1 36  ARG 36  29  29  ARG ARG A . n 
A 1 37  ASP 37  30  30  ASP ASP A . n 
A 1 38  ALA 38  31  31  ALA ALA A . n 
A 1 39  VAL 39  32  32  VAL VAL A . n 
A 1 40  GLU 40  33  33  GLU GLU A . n 
A 1 41  HIS 41  34  34  HIS HIS A . n 
A 1 42  THR 42  35  35  THR THR A . n 
A 1 43  ILE 43  36  36  ILE ILE A . n 
A 1 44  ASP 44  37  37  ASP ASP A . n 
A 1 45  GLY 45  38  38  GLY GLY A . n 
A 1 46  LEU 46  39  39  LEU LEU A . n 
A 1 47  ASP 47  40  40  ASP ASP A . n 
A 1 48  LEU 48  41  41  LEU LEU A . n 
A 1 49  GLY 49  42  42  GLY GLY A . n 
A 1 50  ARG 50  43  43  ARG ARG A . n 
A 1 51  LEU 51  44  44  LEU LEU A . n 
A 1 52  ARG 52  45  45  ARG ARG A . n 
A 1 53  VAL 53  46  46  VAL VAL A . n 
A 1 54  ALA 54  47  47  ALA ALA A . n 
A 1 55  GLU 55  48  48  GLU GLU A . n 
A 1 56  LYS 56  49  49  LYS LYS A . n 
A 1 57  ILE 57  50  50  ILE ILE A . n 
A 1 58  ASP 58  51  51  ASP ASP A . n 
A 1 59  ASP 59  52  52  ASP ASP A . n 
A 1 60  GLN 60  53  53  GLN GLN A . n 
A 1 61  TRP 61  54  54  TRP TRP A . n 
A 1 62  ILE 62  55  55  ILE ILE A . n 
A 1 63  VAL 63  56  56  VAL VAL A . n 
A 1 64  HIS 64  57  57  HIS HIS A . n 
A 1 65  GLN 65  58  58  GLN GLN A . n 
A 1 66  TRP 66  59  59  TRP TRP A . n 
A 1 67  ILE 67  60  60  ILE ILE A . n 
A 1 68  LYS 68  61  61  LYS LYS A . n 
A 1 69  LYS 69  62  62  LYS LYS A . n 
A 1 70  ALA 70  63  63  ALA ALA A . n 
A 1 71  VAL 71  64  64  VAL VAL A . n 
A 1 72  LEU 72  65  65  LEU LEU A . n 
A 1 73  LEU 73  66  66  LEU LEU A . n 
A 1 74  SER 74  67  67  SER SER A . n 
A 1 75  PHE 75  68  68  PHE PHE A . n 
A 1 76  ARG 76  69  69  ARG ARG A . n 
A 1 77  LEU 77  70  70  LEU LEU A . n 
A 1 78  HIS 78  71  71  HIS HIS A . n 
A 1 79  ASP 79  72  72  ASP ASP A . n 
A 1 80  ASN 80  73  73  ASN ASN A . n 
A 1 81  ALA 81  74  74  ALA ALA A . n 
A 1 82  VAL 82  75  75  VAL VAL A . n 
A 1 83  MET 83  76  76  MET MET A . n 
A 1 84  GLY 84  77  77  GLY GLY A . n 
A 1 85  GLN 85  78  78  GLN GLN A . n 
A 1 86  GLY 86  79  79  GLY GLY A . n 
A 1 87  PRO 87  80  80  PRO PRO A . n 
A 1 88  LEU 88  81  81  LEU LEU A . n 
A 1 89  GLN 89  82  82  GLN GLN A . n 
A 1 90  PHE 90  83  83  PHE PHE A . n 
A 1 91  TYR 91  84  84  TYR TYR A . n 
A 1 92  ASP 92  85  85  ASP ASP A . n 
A 1 93  LYS 93  86  86  LYS LYS A . n 
A 1 94  VAL 94  87  87  VAL VAL A . n 
A 1 95  PRO 95  88  88  PRO PRO A . n 
A 1 96  THR 96  89  89  THR THR A . n 
A 1 97  LYS 97  90  90  LYS LYS A . n 
A 1 98  PHE 98  91  91  PHE PHE A . n 
A 1 99  ALA 99  92  92  ALA ALA A . n 
A 1 100 GLY 100 93  93  GLY GLY A . n 
A 1 101 TYR 101 94  94  TYR TYR A . n 
A 1 102 GLY 102 95  95  GLY GLY A . n 
A 1 103 GLU 103 96  96  GLU GLU A . n 
A 1 104 ALA 104 97  97  ALA ALA A . n 
A 1 105 ALA 105 98  98  ALA ALA A . n 
A 1 106 PHE 106 99  99  PHE PHE A . n 
A 1 107 LYS 107 100 100 LYS LYS A . n 
A 1 108 ALA 108 101 101 ALA ALA A . n 
A 1 109 GLY 109 102 102 GLY GLY A . n 
A 1 110 GLY 110 103 103 GLY GLY A . n 
A 1 111 TYR 111 104 104 TYR TYR A . n 
A 1 112 ARG 112 105 105 ARG ARG A . n 
A 1 113 VAL 113 106 106 VAL VAL A . n 
A 1 114 VAL 114 107 107 VAL VAL A . n 
A 1 115 PRO 115 108 108 PRO PRO A . n 
A 1 116 PRO 116 109 109 PRO PRO A . n 
A 1 117 ALA 117 110 110 ALA ALA A . n 
A 1 118 VAL 118 111 111 VAL VAL A . n 
A 1 119 ALA 119 112 112 ALA ALA A . n 
A 1 120 ARG 120 113 113 ARG ARG A . n 
A 1 121 ARG 121 114 114 ARG ARG A . n 
A 1 122 GLY 122 115 115 GLY GLY A . n 
A 1 123 ALA 123 116 116 ALA ALA A . n 
A 1 124 PHE 124 117 117 PHE PHE A . n 
A 1 125 ILE 125 118 118 ILE ILE A . n 
A 1 126 ALA 126 119 119 ALA ALA A . n 
A 1 127 ARG 127 120 120 ARG ARG A . n 
A 1 128 ASN 128 121 121 ASN ASN A . n 
A 1 129 VAL 129 122 122 VAL VAL A . n 
A 1 130 VAL 130 123 123 VAL VAL A . n 
A 1 131 LEU 131 124 124 LEU LEU A . n 
A 1 132 MET 132 125 125 MET MET A . n 
A 1 133 PRO 133 126 126 PRO PRO A . n 
A 1 134 SER 134 127 127 SER SER A . n 
A 1 135 TYR 135 128 128 TYR TYR A . n 
A 1 136 VAL 136 129 129 VAL VAL A . n 
A 1 137 ASN 137 130 130 ASN ASN A . n 
A 1 138 ILE 138 131 131 ILE ILE A . n 
A 1 139 GLY 139 132 132 GLY GLY A . n 
A 1 140 ALA 140 133 133 ALA ALA A . n 
A 1 141 TYR 141 134 134 TYR TYR A . n 
A 1 142 VAL 142 135 135 VAL VAL A . n 
A 1 143 ASP 143 136 136 ASP ASP A . n 
A 1 144 GLU 144 137 137 GLU GLU A . n 
A 1 145 GLY 145 138 138 GLY GLY A . n 
A 1 146 THR 146 139 139 THR THR A . n 
A 1 147 MET 147 140 140 MET MET A . n 
A 1 148 VAL 148 141 141 VAL VAL A . n 
A 1 149 ASP 149 142 142 ASP ASP A . n 
A 1 150 THR 150 143 143 THR THR A . n 
A 1 151 TRP 151 144 144 TRP TRP A . n 
A 1 152 ALA 152 145 145 ALA ALA A . n 
A 1 153 THR 153 146 146 THR THR A . n 
A 1 154 VAL 154 147 147 VAL VAL A . n 
A 1 155 GLY 155 148 148 GLY GLY A . n 
A 1 156 SER 156 149 149 SER SER A . n 
A 1 157 CYS 157 150 150 CYS CYS A . n 
A 1 158 ALA 158 151 151 ALA ALA A . n 
A 1 159 GLN 159 152 152 GLN GLN A . n 
A 1 160 ILE 160 153 153 ILE ILE A . n 
A 1 161 GLY 161 154 154 GLY GLY A . n 
A 1 162 LYS 162 155 155 LYS LYS A . n 
A 1 163 ASN 163 156 156 ASN ASN A . n 
A 1 164 VAL 164 157 157 VAL VAL A . n 
A 1 165 HIS 165 158 158 HIS HIS A . n 
A 1 166 LEU 166 159 159 LEU LEU A . n 
A 1 167 SER 167 160 160 SER SER A . n 
A 1 168 GLY 168 161 161 GLY GLY A . n 
A 1 169 GLY 169 162 162 GLY GLY A . n 
A 1 170 VAL 170 163 163 VAL VAL A . n 
A 1 171 GLY 171 164 164 GLY GLY A . n 
A 1 172 ILE 172 165 165 ILE ILE A . n 
A 1 173 GLY 173 166 166 GLY GLY A . n 
A 1 174 GLY 174 167 167 GLY GLY A . n 
A 1 175 VAL 175 168 168 VAL VAL A . n 
A 1 176 LEU 176 169 169 LEU LEU A . n 
A 1 177 GLU 177 170 170 GLU GLU A . n 
A 1 178 PRO 178 171 171 PRO PRO A . n 
A 1 179 LEU 179 172 172 LEU LEU A . n 
A 1 180 GLN 180 173 173 GLN GLN A . n 
A 1 181 ALA 181 174 174 ALA ALA A . n 
A 1 182 ASN 182 175 175 ASN ASN A . n 
A 1 183 PRO 183 176 176 PRO PRO A . n 
A 1 184 THR 184 177 177 THR THR A . n 
A 1 185 ILE 185 178 178 ILE ILE A . n 
A 1 186 ILE 186 179 179 ILE ILE A . n 
A 1 187 GLU 187 180 180 GLU GLU A . n 
A 1 188 ASP 188 181 181 ASP ASP A . n 
A 1 189 ASN 189 182 182 ASN ASN A . n 
A 1 190 CYS 190 183 183 CYS CYS A . n 
A 1 191 PHE 191 184 184 PHE PHE A . n 
A 1 192 ILE 192 185 185 ILE ILE A . n 
A 1 193 GLY 193 186 186 GLY GLY A . n 
A 1 194 ALA 194 187 187 ALA ALA A . n 
A 1 195 ARG 195 188 188 ARG ARG A . n 
A 1 196 SER 196 189 189 SER SER A . n 
A 1 197 GLU 197 190 190 GLU GLU A . n 
A 1 198 VAL 198 191 191 VAL VAL A . n 
A 1 199 VAL 199 192 192 VAL VAL A . n 
A 1 200 GLU 200 193 193 GLU GLU A . n 
A 1 201 GLY 201 194 194 GLY GLY A . n 
A 1 202 VAL 202 195 195 VAL VAL A . n 
A 1 203 VAL 203 196 196 VAL VAL A . n 
A 1 204 VAL 204 197 197 VAL VAL A . n 
A 1 205 GLU 205 198 198 GLU GLU A . n 
A 1 206 GLU 206 199 199 GLU GLU A . n 
A 1 207 ASN 207 200 200 ASN ASN A . n 
A 1 208 SER 208 201 201 SER SER A . n 
A 1 209 VAL 209 202 202 VAL VAL A . n 
A 1 210 LEU 210 203 203 LEU LEU A . n 
A 1 211 ALA 211 204 204 ALA ALA A . n 
A 1 212 MET 212 205 205 MET MET A . n 
A 1 213 GLY 213 206 206 GLY GLY A . n 
A 1 214 VAL 214 207 207 VAL VAL A . n 
A 1 215 PHE 215 208 208 PHE PHE A . n 
A 1 216 LEU 216 209 209 LEU LEU A . n 
A 1 217 SER 217 210 210 SER SER A . n 
A 1 218 GLN 218 211 211 GLN GLN A . n 
A 1 219 SER 219 212 212 SER SER A . n 
A 1 220 THR 220 213 213 THR THR A . n 
A 1 221 LYS 221 214 214 LYS LYS A . n 
A 1 222 ILE 222 215 215 ILE ILE A . n 
A 1 223 TYR 223 216 216 TYR TYR A . n 
A 1 224 ASP 224 217 217 ASP ASP A . n 
A 1 225 ARG 225 218 218 ARG ARG A . n 
A 1 226 ALA 226 219 219 ALA ALA A . n 
A 1 227 THR 227 220 220 THR THR A . n 
A 1 228 GLY 228 221 221 GLY GLY A . n 
A 1 229 LYS 229 222 222 LYS LYS A . n 
A 1 230 VAL 230 223 223 VAL VAL A . n 
A 1 231 SER 231 224 224 SER SER A . n 
A 1 232 TYR 232 225 225 TYR TYR A . n 
A 1 233 GLY 233 226 226 GLY GLY A . n 
A 1 234 ARG 234 227 227 ARG ARG A . n 
A 1 235 VAL 235 228 228 VAL VAL A . n 
A 1 236 PRO 236 229 229 PRO PRO A . n 
A 1 237 SER 237 230 230 SER SER A . n 
A 1 238 GLY 238 231 231 GLY GLY A . n 
A 1 239 SER 239 232 232 SER SER A . n 
A 1 240 VAL 240 233 233 VAL VAL A . n 
A 1 241 VAL 241 234 234 VAL VAL A . n 
A 1 242 VAL 242 235 235 VAL VAL A . n 
A 1 243 PRO 243 236 236 PRO PRO A . n 
A 1 244 GLY 244 237 237 GLY GLY A . n 
A 1 245 SER 245 238 238 SER SER A . n 
A 1 246 LEU 246 239 239 LEU LEU A . n 
A 1 247 PRO 247 240 240 PRO PRO A . n 
A 1 248 SER 248 241 241 SER SER A . n 
A 1 249 GLU 249 242 242 GLU GLU A . n 
A 1 250 ASP 250 243 243 ASP ASP A . n 
A 1 251 GLY 251 244 244 GLY GLY A . n 
A 1 252 SER 252 245 245 SER SER A . n 
A 1 253 HIS 253 246 246 HIS HIS A . n 
A 1 254 SER 254 247 247 SER SER A . n 
A 1 255 LEU 255 248 248 LEU LEU A . n 
A 1 256 ALA 256 249 249 ALA ALA A . n 
A 1 257 CYS 257 250 250 CYS CYS A . n 
A 1 258 ALA 258 251 251 ALA ALA A . n 
A 1 259 VAL 259 252 252 VAL VAL A . n 
A 1 260 ILE 260 253 253 ILE ILE A . n 
A 1 261 VAL 261 254 254 VAL VAL A . n 
A 1 262 LYS 262 255 255 LYS LYS A . n 
A 1 263 ARG 263 256 256 ARG ARG A . n 
A 1 264 VAL 264 257 257 VAL VAL A . n 
A 1 265 ASP 265 258 258 ASP ASP A . n 
A 1 266 ALA 266 259 259 ALA ALA A . n 
A 1 267 GLN 267 260 260 GLN GLN A . n 
A 1 268 THR 268 261 261 THR THR A . n 
A 1 269 ARG 269 262 262 ARG ARG A . n 
A 1 270 ALA 270 263 263 ALA ALA A . n 
A 1 271 LYS 271 264 264 LYS LYS A . n 
A 1 272 THR 272 265 265 THR THR A . n 
A 1 273 SER 273 266 266 SER SER A . n 
A 1 274 ILE 274 267 267 ILE ILE A . n 
A 1 275 ASN 275 268 268 ASN ASN A . n 
A 1 276 ASP 276 269 269 ASP ASP A . n 
A 1 277 LEU 277 270 270 LEU LEU A . n 
A 1 278 LEU 278 271 271 LEU LEU A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CA  1   301 1   CA  CA  A . 
C 2 CA  1   302 2   CA  CA  A . 
D 2 CA  1   303 3   CA  CA  A . 
E 3 CL  1   304 1   CL  CL  A . 
F 3 CL  1   305 2   CL  CL  A . 
G 3 CL  1   306 3   CL  CL  A . 
H 4 GOL 1   307 1   GOL GOL A . 
I 5 HOH 1   401 184 HOH HOH A . 
I 5 HOH 2   402 123 HOH HOH A . 
I 5 HOH 3   403 60  HOH HOH A . 
I 5 HOH 4   404 197 HOH HOH A . 
I 5 HOH 5   405 107 HOH HOH A . 
I 5 HOH 6   406 98  HOH HOH A . 
I 5 HOH 7   407 113 HOH HOH A . 
I 5 HOH 8   408 108 HOH HOH A . 
I 5 HOH 9   409 165 HOH HOH A . 
I 5 HOH 10  410 116 HOH HOH A . 
I 5 HOH 11  411 19  HOH HOH A . 
I 5 HOH 12  412 122 HOH HOH A . 
I 5 HOH 13  413 144 HOH HOH A . 
I 5 HOH 14  414 41  HOH HOH A . 
I 5 HOH 15  415 75  HOH HOH A . 
I 5 HOH 16  416 48  HOH HOH A . 
I 5 HOH 17  417 3   HOH HOH A . 
I 5 HOH 18  418 34  HOH HOH A . 
I 5 HOH 19  419 138 HOH HOH A . 
I 5 HOH 20  420 61  HOH HOH A . 
I 5 HOH 21  421 118 HOH HOH A . 
I 5 HOH 22  422 45  HOH HOH A . 
I 5 HOH 23  423 172 HOH HOH A . 
I 5 HOH 24  424 24  HOH HOH A . 
I 5 HOH 25  425 117 HOH HOH A . 
I 5 HOH 26  426 11  HOH HOH A . 
I 5 HOH 27  427 64  HOH HOH A . 
I 5 HOH 28  428 150 HOH HOH A . 
I 5 HOH 29  429 56  HOH HOH A . 
I 5 HOH 30  430 223 HOH HOH A . 
I 5 HOH 31  431 208 HOH HOH A . 
I 5 HOH 32  432 128 HOH HOH A . 
I 5 HOH 33  433 42  HOH HOH A . 
I 5 HOH 34  434 86  HOH HOH A . 
I 5 HOH 35  435 53  HOH HOH A . 
I 5 HOH 36  436 73  HOH HOH A . 
I 5 HOH 37  437 49  HOH HOH A . 
I 5 HOH 38  438 178 HOH HOH A . 
I 5 HOH 39  439 69  HOH HOH A . 
I 5 HOH 40  440 94  HOH HOH A . 
I 5 HOH 41  441 171 HOH HOH A . 
I 5 HOH 42  442 96  HOH HOH A . 
I 5 HOH 43  443 214 HOH HOH A . 
I 5 HOH 44  444 196 HOH HOH A . 
I 5 HOH 45  445 139 HOH HOH A . 
I 5 HOH 46  446 90  HOH HOH A . 
I 5 HOH 47  447 133 HOH HOH A . 
I 5 HOH 48  448 157 HOH HOH A . 
I 5 HOH 49  449 191 HOH HOH A . 
I 5 HOH 50  450 207 HOH HOH A . 
I 5 HOH 51  451 59  HOH HOH A . 
I 5 HOH 52  452 5   HOH HOH A . 
I 5 HOH 53  453 66  HOH HOH A . 
I 5 HOH 54  454 85  HOH HOH A . 
I 5 HOH 55  455 20  HOH HOH A . 
I 5 HOH 56  456 58  HOH HOH A . 
I 5 HOH 57  457 230 HOH HOH A . 
I 5 HOH 58  458 72  HOH HOH A . 
I 5 HOH 59  459 7   HOH HOH A . 
I 5 HOH 60  460 231 HOH HOH A . 
I 5 HOH 61  461 70  HOH HOH A . 
I 5 HOH 62  462 14  HOH HOH A . 
I 5 HOH 63  463 153 HOH HOH A . 
I 5 HOH 64  464 52  HOH HOH A . 
I 5 HOH 65  465 32  HOH HOH A . 
I 5 HOH 66  466 74  HOH HOH A . 
I 5 HOH 67  467 109 HOH HOH A . 
I 5 HOH 68  468 99  HOH HOH A . 
I 5 HOH 69  469 44  HOH HOH A . 
I 5 HOH 70  470 8   HOH HOH A . 
I 5 HOH 71  471 76  HOH HOH A . 
I 5 HOH 72  472 71  HOH HOH A . 
I 5 HOH 73  473 186 HOH HOH A . 
I 5 HOH 74  474 51  HOH HOH A . 
I 5 HOH 75  475 218 HOH HOH A . 
I 5 HOH 76  476 211 HOH HOH A . 
I 5 HOH 77  477 78  HOH HOH A . 
I 5 HOH 78  478 62  HOH HOH A . 
I 5 HOH 79  479 6   HOH HOH A . 
I 5 HOH 80  480 25  HOH HOH A . 
I 5 HOH 81  481 103 HOH HOH A . 
I 5 HOH 82  482 54  HOH HOH A . 
I 5 HOH 83  483 12  HOH HOH A . 
I 5 HOH 84  484 92  HOH HOH A . 
I 5 HOH 85  485 112 HOH HOH A . 
I 5 HOH 86  486 119 HOH HOH A . 
I 5 HOH 87  487 204 HOH HOH A . 
I 5 HOH 88  488 17  HOH HOH A . 
I 5 HOH 89  489 82  HOH HOH A . 
I 5 HOH 90  490 97  HOH HOH A . 
I 5 HOH 91  491 148 HOH HOH A . 
I 5 HOH 92  492 101 HOH HOH A . 
I 5 HOH 93  493 37  HOH HOH A . 
I 5 HOH 94  494 57  HOH HOH A . 
I 5 HOH 95  495 27  HOH HOH A . 
I 5 HOH 96  496 100 HOH HOH A . 
I 5 HOH 97  497 155 HOH HOH A . 
I 5 HOH 98  498 224 HOH HOH A . 
I 5 HOH 99  499 63  HOH HOH A . 
I 5 HOH 100 500 219 HOH HOH A . 
I 5 HOH 101 501 2   HOH HOH A . 
I 5 HOH 102 502 21  HOH HOH A . 
I 5 HOH 103 503 68  HOH HOH A . 
I 5 HOH 104 504 143 HOH HOH A . 
I 5 HOH 105 505 193 HOH HOH A . 
I 5 HOH 106 506 13  HOH HOH A . 
I 5 HOH 107 507 215 HOH HOH A . 
I 5 HOH 108 508 15  HOH HOH A . 
I 5 HOH 109 509 187 HOH HOH A . 
I 5 HOH 110 510 170 HOH HOH A . 
I 5 HOH 111 511 104 HOH HOH A . 
I 5 HOH 112 512 80  HOH HOH A . 
I 5 HOH 113 513 225 HOH HOH A . 
I 5 HOH 114 514 81  HOH HOH A . 
I 5 HOH 115 515 147 HOH HOH A . 
I 5 HOH 116 516 149 HOH HOH A . 
I 5 HOH 117 517 177 HOH HOH A . 
I 5 HOH 118 518 124 HOH HOH A . 
I 5 HOH 119 519 198 HOH HOH A . 
I 5 HOH 120 520 130 HOH HOH A . 
I 5 HOH 121 521 226 HOH HOH A . 
I 5 HOH 122 522 121 HOH HOH A . 
I 5 HOH 123 523 102 HOH HOH A . 
I 5 HOH 124 524 93  HOH HOH A . 
I 5 HOH 125 525 111 HOH HOH A . 
I 5 HOH 126 526 188 HOH HOH A . 
I 5 HOH 127 527 141 HOH HOH A . 
I 5 HOH 128 528 79  HOH HOH A . 
I 5 HOH 129 529 10  HOH HOH A . 
I 5 HOH 130 530 91  HOH HOH A . 
I 5 HOH 131 531 142 HOH HOH A . 
I 5 HOH 132 532 183 HOH HOH A . 
I 5 HOH 133 533 46  HOH HOH A . 
I 5 HOH 134 534 179 HOH HOH A . 
I 5 HOH 135 535 217 HOH HOH A . 
I 5 HOH 136 536 158 HOH HOH A . 
I 5 HOH 137 537 222 HOH HOH A . 
I 5 HOH 138 538 18  HOH HOH A . 
I 5 HOH 139 539 175 HOH HOH A . 
I 5 HOH 140 540 38  HOH HOH A . 
I 5 HOH 141 541 50  HOH HOH A . 
I 5 HOH 142 542 114 HOH HOH A . 
I 5 HOH 143 543 213 HOH HOH A . 
I 5 HOH 144 544 28  HOH HOH A . 
I 5 HOH 145 545 115 HOH HOH A . 
I 5 HOH 146 546 4   HOH HOH A . 
I 5 HOH 147 547 127 HOH HOH A . 
I 5 HOH 148 548 55  HOH HOH A . 
I 5 HOH 149 549 30  HOH HOH A . 
I 5 HOH 150 550 31  HOH HOH A . 
I 5 HOH 151 551 35  HOH HOH A . 
I 5 HOH 152 552 106 HOH HOH A . 
I 5 HOH 153 553 40  HOH HOH A . 
I 5 HOH 154 554 221 HOH HOH A . 
I 5 HOH 155 555 83  HOH HOH A . 
I 5 HOH 156 556 229 HOH HOH A . 
I 5 HOH 157 557 87  HOH HOH A . 
I 5 HOH 158 558 95  HOH HOH A . 
I 5 HOH 159 559 164 HOH HOH A . 
I 5 HOH 160 560 189 HOH HOH A . 
I 5 HOH 161 561 228 HOH HOH A . 
I 5 HOH 162 562 23  HOH HOH A . 
I 5 HOH 163 563 201 HOH HOH A . 
I 5 HOH 164 564 166 HOH HOH A . 
I 5 HOH 165 565 156 HOH HOH A . 
I 5 HOH 166 566 160 HOH HOH A . 
I 5 HOH 167 567 180 HOH HOH A . 
I 5 HOH 168 568 33  HOH HOH A . 
I 5 HOH 169 569 125 HOH HOH A . 
I 5 HOH 170 570 9   HOH HOH A . 
I 5 HOH 171 571 29  HOH HOH A . 
I 5 HOH 172 572 185 HOH HOH A . 
I 5 HOH 173 573 210 HOH HOH A . 
I 5 HOH 174 574 16  HOH HOH A . 
I 5 HOH 175 575 22  HOH HOH A . 
I 5 HOH 176 576 89  HOH HOH A . 
I 5 HOH 177 577 192 HOH HOH A . 
I 5 HOH 178 578 43  HOH HOH A . 
I 5 HOH 179 579 47  HOH HOH A . 
I 5 HOH 180 580 1   HOH HOH A . 
I 5 HOH 181 581 206 HOH HOH A . 
I 5 HOH 182 582 202 HOH HOH A . 
I 5 HOH 183 583 182 HOH HOH A . 
I 5 HOH 184 584 161 HOH HOH A . 
I 5 HOH 185 585 129 HOH HOH A . 
I 5 HOH 186 586 136 HOH HOH A . 
I 5 HOH 187 587 137 HOH HOH A . 
I 5 HOH 188 588 209 HOH HOH A . 
I 5 HOH 189 589 159 HOH HOH A . 
I 5 HOH 190 590 199 HOH HOH A . 
I 5 HOH 191 591 212 HOH HOH A . 
I 5 HOH 192 592 120 HOH HOH A . 
I 5 HOH 193 593 163 HOH HOH A . 
I 5 HOH 194 594 162 HOH HOH A . 
I 5 HOH 195 595 110 HOH HOH A . 
I 5 HOH 196 596 205 HOH HOH A . 
I 5 HOH 197 597 84  HOH HOH A . 
I 5 HOH 198 598 200 HOH HOH A . 
I 5 HOH 199 599 176 HOH HOH A . 
I 5 HOH 200 600 227 HOH HOH A . 
I 5 HOH 201 601 140 HOH HOH A . 
I 5 HOH 202 602 26  HOH HOH A . 
I 5 HOH 203 603 152 HOH HOH A . 
I 5 HOH 204 604 36  HOH HOH A . 
I 5 HOH 205 605 181 HOH HOH A . 
I 5 HOH 206 606 203 HOH HOH A . 
I 5 HOH 207 607 220 HOH HOH A . 
I 5 HOH 208 608 167 HOH HOH A . 
I 5 HOH 209 609 132 HOH HOH A . 
I 5 HOH 210 610 77  HOH HOH A . 
I 5 HOH 211 611 195 HOH HOH A . 
I 5 HOH 212 612 174 HOH HOH A . 
I 5 HOH 213 613 169 HOH HOH A . 
I 5 HOH 214 614 216 HOH HOH A . 
I 5 HOH 215 615 151 HOH HOH A . 
I 5 HOH 216 616 190 HOH HOH A . 
I 5 HOH 217 617 135 HOH HOH A . 
I 5 HOH 218 618 131 HOH HOH A . 
I 5 HOH 219 619 168 HOH HOH A . 
I 5 HOH 220 620 173 HOH HOH A . 
I 5 HOH 221 621 232 HOH HOH A . 
I 5 HOH 222 622 154 HOH HOH A . 
I 5 HOH 223 623 105 HOH HOH A . 
I 5 HOH 224 624 145 HOH HOH A . 
I 5 HOH 225 625 88  HOH HOH A . 
I 5 HOH 226 626 146 HOH HOH A . 
I 5 HOH 227 627 194 HOH HOH A . 
I 5 HOH 228 628 126 HOH HOH A . 
I 5 HOH 229 629 67  HOH HOH A . 
I 5 HOH 230 630 65  HOH HOH A . 
I 5 HOH 231 631 39  HOH HOH A . 
I 5 HOH 232 632 134 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A HIS 1   ? CG  ? A HIS 8   CG  
2  1 Y 1 A HIS 1   ? ND1 ? A HIS 8   ND1 
3  1 Y 1 A HIS 1   ? CD2 ? A HIS 8   CD2 
4  1 Y 1 A HIS 1   ? CE1 ? A HIS 8   CE1 
5  1 Y 1 A HIS 1   ? NE2 ? A HIS 8   NE2 
6  1 Y 1 A LEU 3   ? CG  ? A LEU 10  CG  
7  1 Y 1 A LEU 3   ? CD1 ? A LEU 10  CD1 
8  1 Y 1 A LEU 3   ? CD2 ? A LEU 10  CD2 
9  1 Y 1 A ASP 51  ? CG  ? A ASP 58  CG  
10 1 Y 1 A ASP 51  ? OD1 ? A ASP 58  OD1 
11 1 Y 1 A ASP 51  ? OD2 ? A ASP 58  OD2 
12 1 Y 1 A GLN 260 ? CG  ? A GLN 267 CG  
13 1 Y 1 A GLN 260 ? CD  ? A GLN 267 CD  
14 1 Y 1 A GLN 260 ? OE1 ? A GLN 267 OE1 
15 1 Y 1 A GLN 260 ? NE2 ? A GLN 267 NE2 
16 1 Y 1 A LYS 264 ? CG  ? A LYS 271 CG  
17 1 Y 1 A LYS 264 ? CD  ? A LYS 271 CD  
18 1 Y 1 A LYS 264 ? CE  ? A LYS 271 CE  
19 1 Y 1 A LYS 264 ? NZ  ? A LYS 271 NZ  
20 1 Y 1 A ASP 269 ? CG  ? A ASP 276 CG  
21 1 Y 1 A ASP 269 ? OD1 ? A ASP 276 OD1 
22 1 Y 1 A ASP 269 ? OD2 ? A ASP 276 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? dev_5660 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9O8N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     97.696 
_cell.length_a_esd                 ? 
_cell.length_b                     97.696 
_cell.length_b_esd                 ? 
_cell.length_c                     78.288 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9O8N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9O8N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          65.82 
_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              4.0 
_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    
;Berkeley A1: 2200 mM Sodium chloride, 100 mM Tris HCl/ Sodium hydroxide pH 8.0, 50 mM Calcium chloride. BopeA.00002.a.B2.PW39337 at 16.9 mg/mL. plate 19707 A1 drop 1, Puck: PSL1213, Cryo: 80% crystallant + 20% glycerol.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2025-03-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9786 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9O8N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               48.85 
_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                                     57075 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.201 
_reflns.pdbx_Rpim_I_all                                0.044 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1173267 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.196 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.59 
_reflns_shell.d_res_low                                     1.62 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           60173 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2815 
_reflns_shell.percent_possible_obs                          100.0 
_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                               21.4 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               2.939 
_reflns_shell.pdbx_Rpim_I_all                               0.630 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.308 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.870 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9O8N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.59 
_refine.ls_d_res_low                             48.85 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     57023 
_refine.ls_number_reflns_R_free                  2873 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1587 
_refine.ls_R_factor_R_free                       0.1795 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1577 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.57 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        48.85 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               2267 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2023 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2093 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.917  ? 2853 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 17.619 ? 756  ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.065  ? 331  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 373  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.59 1.62  . . 126 2547 100.00 . . . . 0.3085 . . . . . . . . . . . . . . . 0.3422 
'X-RAY DIFFRACTION' 1.62 1.64  . . 130 2569 100.00 . . . . 0.2952 . . . . . . . . . . . . . . . 0.3182 
'X-RAY DIFFRACTION' 1.64 1.67  . . 160 2544 100.00 . . . . 0.2790 . . . . . . . . . . . . . . . 0.2729 
'X-RAY DIFFRACTION' 1.67 1.71  . . 147 2567 100.00 . . . . 0.2611 . . . . . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 1.71 1.74  . . 150 2581 100.00 . . . . 0.2430 . . . . . . . . . . . . . . . 0.2806 
'X-RAY DIFFRACTION' 1.74 1.78  . . 128 2582 100.00 . . . . 0.2251 . . . . . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 1.78 1.82  . . 150 2551 100.00 . . . . 0.2044 . . . . . . . . . . . . . . . 0.2136 
'X-RAY DIFFRACTION' 1.82 1.87  . . 134 2568 100.00 . . . . 0.1703 . . . . . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 1.87 1.92  . . 137 2587 100.00 . . . . 0.1688 . . . . . . . . . . . . . . . 0.1645 
'X-RAY DIFFRACTION' 1.92 1.97  . . 122 2553 100.00 . . . . 0.1607 . . . . . . . . . . . . . . . 0.1948 
'X-RAY DIFFRACTION' 1.97 2.04  . . 136 2591 100.00 . . . . 0.1537 . . . . . . . . . . . . . . . 0.1746 
'X-RAY DIFFRACTION' 2.04 2.11  . . 126 2564 100.00 . . . . 0.1402 . . . . . . . . . . . . . . . 0.1505 
'X-RAY DIFFRACTION' 2.11 2.19  . . 129 2622 100.00 . . . . 0.1324 . . . . . . . . . . . . . . . 0.1549 
'X-RAY DIFFRACTION' 2.19 2.29  . . 156 2532 100.00 . . . . 0.1306 . . . . . . . . . . . . . . . 0.1509 
'X-RAY DIFFRACTION' 2.29 2.41  . . 135 2577 100.00 . . . . 0.1243 . . . . . . . . . . . . . . . 0.1471 
'X-RAY DIFFRACTION' 2.41 2.57  . . 138 2598 100.00 . . . . 0.1380 . . . . . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 2.57 2.76  . . 133 2570 100.00 . . . . 0.1464 . . . . . . . . . . . . . . . 0.1760 
'X-RAY DIFFRACTION' 2.76 3.04  . . 140 2597 100.00 . . . . 0.1499 . . . . . . . . . . . . . . . 0.1533 
'X-RAY DIFFRACTION' 3.04 3.48  . . 152 2577 100.00 . . . . 0.1462 . . . . . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 3.48 4.39  . . 127 2613 100.00 . . . . 0.1296 . . . . . . . . . . . . . . . 0.1372 
'X-RAY DIFFRACTION' 4.39 48.85 . . 117 2660 99.00  . . . . 0.1627 . . . . . . . . . . . . . . . 0.1903 
# 
_struct.entry_id                     9O8N 
_struct.title                        
'Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (DapD) from Bordetella pertussis' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9O8N 
_struct_keywords.text            
'SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, dapD, Bordetella pertussis, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DAPD_BORPE 
_struct_ref.pdbx_db_accession          P0A4U8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TLDLQTTIEQAWENRANLSPVDASAEVRDAVEHTIDGLDLGRLRVAEKIDDQWIVHQWIKKAVLLSFRLHDNAVMGQGPL
QFYDKVPTKFAGYGEAAFKAGGYRVVPPAVARRGAFIARNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG
GVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEENSVLAMGVFLSQSTKIYDRATGKVSYGRVPSGSVVVPGSLPS
EDGSHSLACAVIVKRVDAQTRAKTSINDLL
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9O8N 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 278 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0A4U8 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  271 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       271 
# 
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 9O8N MET A 1 ? UNP P0A4U8 ? ? 'initiating methionine' -6 1 
1 9O8N ALA A 2 ? UNP P0A4U8 ? ? 'expression tag'        -5 2 
1 9O8N HIS A 3 ? UNP P0A4U8 ? ? 'expression tag'        -4 3 
1 9O8N HIS A 4 ? UNP P0A4U8 ? ? 'expression tag'        -3 4 
1 9O8N HIS A 5 ? UNP P0A4U8 ? ? 'expression tag'        -2 5 
1 9O8N HIS A 6 ? UNP P0A4U8 ? ? 'expression tag'        -1 6 
1 9O8N HIS A 7 ? UNP P0A4U8 ? ? 'expression tag'        0  7 
1 9O8N HIS A 8 ? UNP P0A4U8 ? ? 'expression tag'        1  8 
# 
_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   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 12750 ? 
1 MORE         -268  ? 
1 'SSA (A^2)'  29780 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  1.0000000000 
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_545 -y,x-y-1,z  -0.5000000000 -0.8660254038 0.0000000000 48.8480000000 0.8660254038  
-0.5000000000 0.0000000000 -84.6072178481 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038  0.0000000000 97.6960000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 11  ? ASN A 22  ? ASP A 4   ASN A 15  1 ? 12 
HELX_P HELX_P2 AA2 ARG A 23  ? LEU A 26  ? ARG A 16  LEU A 19  5 ? 4  
HELX_P HELX_P3 AA3 SER A 32  ? LEU A 48  ? SER A 25  LEU A 41  1 ? 17 
HELX_P HELX_P4 AA4 HIS A 64  ? LEU A 77  ? HIS A 57  LEU A 70  1 ? 14 
HELX_P HELX_P5 AA5 GLY A 102 ? GLY A 110 ? GLY A 95  GLY A 103 1 ? 9  
HELX_P HELX_P6 AA6 ASP A 265 ? THR A 272 ? ASP A 258 THR A 265 1 ? 8  
HELX_P HELX_P7 AA7 ILE A 274 ? LEU A 278 ? ILE A 267 LEU A 271 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 32 OG ? ? ? 1_555 C CA  . CA ? ? A SER 25  A CA  302 1_555 ? ? ? ? ? ? ? 3.045 ? ? 
metalc2 metalc ? ? C CA  .  CA ? ? ? 1_555 I HOH . O  ? ? A CA  302 A HOH 567 1_555 ? ? ? ? ? ? ? 3.106 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OG 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   SER 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    32 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    SER 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     25 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   CA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   CA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    CA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     302 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   I 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     567 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 111.2 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 115 A . ? PRO 108 A PRO 116 A ? PRO 109 A 1 5.33  
2 GLU 177 A . ? GLU 170 A PRO 178 A ? PRO 171 A 1 -3.66 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 2  ? 
AA3 ? 10 ? 
AA4 ? 6  ? 
AA5 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
AA3 5 6  ? parallel      
AA3 6 7  ? parallel      
AA3 7 8  ? anti-parallel 
AA3 8 9  ? parallel      
AA3 9 10 ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ALA A 54  ? ILE A 57  ? ALA A 47  ILE A 50  
AA1 2  GLN A 60  ? VAL A 63  ? GLN A 53  VAL A 56  
AA2 1  ALA A 81  ? GLN A 85  ? ALA A 74  GLN A 78  
AA2 2  LEU A 88  ? ASP A 92  ? LEU A 81  ASP A 85  
AA3 1  ARG A 112 ? VAL A 113 ? ARG A 105 VAL A 106 
AA3 2  VAL A 130 ? LEU A 131 ? VAL A 123 LEU A 124 
AA3 3  MET A 147 ? VAL A 148 ? MET A 140 VAL A 141 
AA3 4  HIS A 165 ? LEU A 166 ? HIS A 158 LEU A 159 
AA3 5  PHE A 191 ? ILE A 192 ? PHE A 184 ILE A 185 
AA3 6  VAL A 209 ? LEU A 210 ? VAL A 202 LEU A 203 
AA3 7  SER A 239 ? PRO A 247 ? SER A 232 PRO A 240 
AA3 8  SER A 254 ? ARG A 263 ? SER A 247 ARG A 256 
AA3 9  ILE A 222 ? ASP A 224 ? ILE A 215 ASP A 217 
AA3 10 LYS A 229 ? SER A 231 ? LYS A 222 SER A 224 
AA4 1  VAL A 118 ? ALA A 119 ? VAL A 111 ALA A 112 
AA4 2  SER A 134 ? VAL A 136 ? SER A 127 VAL A 129 
AA4 3  ALA A 152 ? VAL A 154 ? ALA A 145 VAL A 147 
AA4 4  GLY A 171 ? ILE A 172 ? GLY A 164 ILE A 165 
AA4 5  GLU A 197 ? VAL A 198 ? GLU A 190 VAL A 191 
AA4 6  PHE A 215 ? LEU A 216 ? PHE A 208 LEU A 209 
AA5 1  PHE A 124 ? ILE A 125 ? PHE A 117 ILE A 118 
AA5 2  TYR A 141 ? VAL A 142 ? TYR A 134 VAL A 135 
AA5 3  GLN A 159 ? ILE A 160 ? GLN A 152 ILE A 153 
AA5 4  ILE A 185 ? ILE A 186 ? ILE A 178 ILE A 179 
AA5 5  VAL A 203 ? VAL A 204 ? VAL A 196 VAL A 197 
AA5 6  ARG A 234 ? VAL A 235 ? ARG A 227 VAL A 228 
# 
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 57  ? N ILE A 50  O GLN A 60  ? O GLN A 53  
AA2 1 2  N MET A 83  ? N MET A 76  O PHE A 90  ? O PHE A 83  
AA3 1 2  N ARG A 112 ? N ARG A 105 O LEU A 131 ? O LEU A 124 
AA3 2 3  N VAL A 130 ? N VAL A 123 O VAL A 148 ? O VAL A 141 
AA3 3 4  N MET A 147 ? N MET A 140 O LEU A 166 ? O LEU A 159 
AA3 4 5  N HIS A 165 ? N HIS A 158 O ILE A 192 ? O ILE A 185 
AA3 5 6  N PHE A 191 ? N PHE A 184 O LEU A 210 ? O LEU A 203 
AA3 6 7  N VAL A 209 ? N VAL A 202 O SER A 239 ? O SER A 232 
AA3 7 8  N VAL A 240 ? N VAL A 233 O LYS A 262 ? O LYS A 255 
AA3 8 9  O ALA A 258 ? O ALA A 251 N TYR A 223 ? N TYR A 216 
AA3 9 10 N ASP A 224 ? N ASP A 217 O LYS A 229 ? O LYS A 222 
AA4 1 2  N VAL A 118 ? N VAL A 111 O SER A 134 ? O SER A 127 
AA4 2 3  N TYR A 135 ? N TYR A 128 O VAL A 154 ? O VAL A 147 
AA4 3 4  N THR A 153 ? N THR A 146 O ILE A 172 ? O ILE A 165 
AA4 4 5  N GLY A 171 ? N GLY A 164 O VAL A 198 ? O VAL A 191 
AA4 5 6  N GLU A 197 ? N GLU A 190 O LEU A 216 ? O LEU A 209 
AA5 1 2  N PHE A 124 ? N PHE A 117 O VAL A 142 ? O VAL A 135 
AA5 2 3  N TYR A 141 ? N TYR A 134 O ILE A 160 ? O ILE A 153 
AA5 3 4  N GLN A 159 ? N GLN A 152 O ILE A 186 ? O ILE A 179 
AA5 4 5  N ILE A 185 ? N ILE A 178 O VAL A 204 ? O VAL A 197 
AA5 5 6  N VAL A 203 ? N VAL A 196 O VAL A 235 ? O VAL A 228 
# 
_pdbx_entry_details.entry_id                   9O8N 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 109 ? ? -102.30 43.72 
2 1 CYS A 150 ? ? 74.53   -1.23 
3 1 ARG A 188 ? ? 69.17   -0.34 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 424 ? I HOH . 
2 1 A HOH 622 ? I HOH . 
3 1 A HOH 623 ? I HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 52.0047 5.9942   11.8259  0.2393 ? -0.0043 ? 0.0282  ? 0.1084 ? -0.0561 ? 0.1345 ? 6.3877 ? 0.8957 
? 2.5635  ? 8.0153 ? -1.2951 ? 6.7796 ? -0.0130 ? -0.1124 ? 0.2111  ? 0.2499  ? -0.0710 ? 0.0194 ? -0.2924 ? -0.1551 ? 0.0494  ? 
2 'X-RAY DIFFRACTION' ? refined 44.0208 -1.2620  15.4605  0.2979 ? 0.0111  ? 0.0487  ? 0.1810 ? -0.0239 ? 0.1927 ? 9.0440 ? 7.0593 
? 8.1175  ? 5.5646 ? 6.5281  ? 7.9194 ? 0.3039  ? -0.3599 ? -0.0148 ? 0.4666  ? -0.3523 ? 0.2132 ? 0.0729  ? -0.3347 ? 0.0260  ? 
3 'X-RAY DIFFRACTION' ? refined 41.6116 -1.7385  2.3366   0.2832 ? 0.0335  ? -0.0073 ? 0.1263 ? -0.0168 ? 0.2042 ? 6.8278 ? 0.9982 
? 2.4500  ? 3.5131 ? 1.7469  ? 3.6002 ? -0.2346 ? 0.1971  ? 0.3807  ? -0.3587 ? -0.0104 ? 0.4101 ? -0.4902 ? -0.1303 ? 0.2373  ? 
4 'X-RAY DIFFRACTION' ? refined 51.4122 -17.1767 17.6140  0.2451 ? -0.0060 ? 0.0095  ? 0.1846 ? -0.0396 ? 0.1301 ? 8.0260 ? 
-1.3290 ? 0.1345  ? 1.3890 ? 0.4556  ? 3.3878 ? -0.1218 ? -0.3524 ? -0.3048 ? 0.2833  ? 0.0384  ? 0.0613 ? 0.1470  ? -0.1414 ? 
0.0745  ? 
5 'X-RAY DIFFRACTION' ? refined 35.4264 -22.0926 14.5412  0.1949 ? -0.0093 ? 0.0527  ? 0.2090 ? -0.0118 ? 0.1454 ? 3.3578 ? 
-1.2080 ? -0.0857 ? 4.1851 ? 0.6665  ? 4.1932 ? 0.0727  ? -0.1960 ? -0.0190 ? 0.2739  ? -0.1091 ? 0.3217 ? -0.0938 ? -0.4985 ? 
0.0239  ? 
6 'X-RAY DIFFRACTION' ? refined 38.7141 -17.6794 8.5452   0.1848 ? 0.0184  ? 0.0288  ? 0.1542 ? -0.0076 ? 0.0957 ? 4.7572 ? 0.1929 
? -0.3944 ? 3.7156 ? -0.2195 ? 1.9664 ? -0.0714 ? -0.1589 ? 0.1670  ? 0.3104  ? 0.0704  ? 0.1384 ? -0.1629 ? -0.1723 ? 0.0128  ? 
7 'X-RAY DIFFRACTION' ? refined 39.7854 -15.0456 -1.1788  0.1456 ? 0.0177  ? 0.0121  ? 0.1282 ? -0.0076 ? 0.1114 ? 1.7092 ? 
-0.1564 ? 0.1465  ? 3.0564 ? 0.2118  ? 2.3460 ? -0.0278 ? -0.0749 ? 0.0772  ? -0.0411 ? 0.0393  ? 0.0767 ? -0.1925 ? -0.0541 ? 
-0.0040 ? 
8 'X-RAY DIFFRACTION' ? refined 40.0914 -17.2568 -15.6975 0.1608 ? 0.0122  ? -0.0183 ? 0.1216 ? 0.0071  ? 0.1444 ? 1.6993 ? 0.7435 
? -0.2357 ? 1.9205 ? 0.2167  ? 4.6408 ? -0.0612 ? -0.0057 ? 0.0285  ? -0.1094 ? -0.0248 ? 0.1178 ? -0.1207 ? -0.0283 ? 0.0833  ? 
9 'X-RAY DIFFRACTION' ? refined 37.2806 -23.1860 -20.9648 0.1631 ? -0.0060 ? -0.0295 ? 0.1873 ? -0.0251 ? 0.2198 ? 5.4584 ? 
-1.2911 ? -0.6306 ? 2.8853 ? 1.0255  ? 2.2918 ? -0.0415 ? 0.0053  ? -0.2013 ? -0.0195 ? -0.1970 ? 0.5754 ? 0.0057  ? -0.4226 ? 
0.1736  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 25 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 26 through 41 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 42 through 69 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 70 through 95 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 96 through 112 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 113 through 129 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 130 through 182 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 183 through 231 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 232 through 271 )
;
# 
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 -6 ? A MET 1 
2 1 Y 1 A ALA -5 ? A ALA 2 
3 1 Y 1 A HIS -4 ? A HIS 3 
4 1 Y 1 A HIS -3 ? A HIS 4 
5 1 Y 1 A HIS -2 ? A HIS 5 
6 1 Y 1 A HIS -1 ? A HIS 6 
7 1 Y 1 A HIS 0  ? A HIS 7 
# 
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  
CA  CA   CA N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
GLN N    N  N N 90  
GLN CA   C  N S 91  
GLN C    C  N N 92  
GLN O    O  N N 93  
GLN CB   C  N N 94  
GLN CG   C  N N 95  
GLN CD   C  N N 96  
GLN OE1  O  N N 97  
GLN NE2  N  N N 98  
GLN OXT  O  N N 99  
GLN H    H  N N 100 
GLN H2   H  N N 101 
GLN HA   H  N N 102 
GLN HB2  H  N N 103 
GLN HB3  H  N N 104 
GLN HG2  H  N N 105 
GLN HG3  H  N N 106 
GLN HE21 H  N N 107 
GLN HE22 H  N N 108 
GLN HXT  H  N N 109 
GLU N    N  N N 110 
GLU CA   C  N S 111 
GLU C    C  N N 112 
GLU O    O  N N 113 
GLU CB   C  N N 114 
GLU CG   C  N N 115 
GLU CD   C  N N 116 
GLU OE1  O  N N 117 
GLU OE2  O  N N 118 
GLU OXT  O  N N 119 
GLU H    H  N N 120 
GLU H2   H  N N 121 
GLU HA   H  N N 122 
GLU HB2  H  N N 123 
GLU HB3  H  N N 124 
GLU HG2  H  N N 125 
GLU HG3  H  N N 126 
GLU HE2  H  N N 127 
GLU HXT  H  N N 128 
GLY N    N  N N 129 
GLY CA   C  N N 130 
GLY C    C  N N 131 
GLY O    O  N N 132 
GLY OXT  O  N N 133 
GLY H    H  N N 134 
GLY H2   H  N N 135 
GLY HA2  H  N N 136 
GLY HA3  H  N N 137 
GLY HXT  H  N N 138 
GOL C1   C  N N 139 
GOL O1   O  N N 140 
GOL C2   C  N N 141 
GOL O2   O  N N 142 
GOL C3   C  N N 143 
GOL O3   O  N N 144 
GOL H11  H  N N 145 
GOL H12  H  N N 146 
GOL HO1  H  N N 147 
GOL H2   H  N N 148 
GOL HO2  H  N N 149 
GOL H31  H  N N 150 
GOL H32  H  N N 151 
GOL HO3  H  N N 152 
HIS N    N  N N 153 
HIS CA   C  N S 154 
HIS C    C  N N 155 
HIS O    O  N N 156 
HIS CB   C  N N 157 
HIS CG   C  Y N 158 
HIS ND1  N  Y N 159 
HIS CD2  C  Y N 160 
HIS CE1  C  Y N 161 
HIS NE2  N  Y N 162 
HIS OXT  O  N N 163 
HIS H    H  N N 164 
HIS H2   H  N N 165 
HIS HA   H  N N 166 
HIS HB2  H  N N 167 
HIS HB3  H  N N 168 
HIS HD1  H  N N 169 
HIS HD2  H  N N 170 
HIS HE1  H  N N 171 
HIS HE2  H  N N 172 
HIS HXT  H  N N 173 
HOH O    O  N N 174 
HOH H1   H  N N 175 
HOH H2   H  N N 176 
ILE N    N  N N 177 
ILE CA   C  N S 178 
ILE C    C  N N 179 
ILE O    O  N N 180 
ILE CB   C  N S 181 
ILE CG1  C  N N 182 
ILE CG2  C  N N 183 
ILE CD1  C  N N 184 
ILE OXT  O  N N 185 
ILE H    H  N N 186 
ILE H2   H  N N 187 
ILE HA   H  N N 188 
ILE HB   H  N N 189 
ILE HG12 H  N N 190 
ILE HG13 H  N N 191 
ILE HG21 H  N N 192 
ILE HG22 H  N N 193 
ILE HG23 H  N N 194 
ILE HD11 H  N N 195 
ILE HD12 H  N N 196 
ILE HD13 H  N N 197 
ILE HXT  H  N N 198 
LEU N    N  N N 199 
LEU CA   C  N S 200 
LEU C    C  N N 201 
LEU O    O  N N 202 
LEU CB   C  N N 203 
LEU CG   C  N N 204 
LEU CD1  C  N N 205 
LEU CD2  C  N N 206 
LEU OXT  O  N N 207 
LEU H    H  N N 208 
LEU H2   H  N N 209 
LEU HA   H  N N 210 
LEU HB2  H  N N 211 
LEU HB3  H  N N 212 
LEU HG   H  N N 213 
LEU HD11 H  N N 214 
LEU HD12 H  N N 215 
LEU HD13 H  N N 216 
LEU HD21 H  N N 217 
LEU HD22 H  N N 218 
LEU HD23 H  N N 219 
LEU HXT  H  N N 220 
LYS N    N  N N 221 
LYS CA   C  N S 222 
LYS C    C  N N 223 
LYS O    O  N N 224 
LYS CB   C  N N 225 
LYS CG   C  N N 226 
LYS CD   C  N N 227 
LYS CE   C  N N 228 
LYS NZ   N  N N 229 
LYS OXT  O  N N 230 
LYS H    H  N N 231 
LYS H2   H  N N 232 
LYS HA   H  N N 233 
LYS HB2  H  N N 234 
LYS HB3  H  N N 235 
LYS HG2  H  N N 236 
LYS HG3  H  N N 237 
LYS HD2  H  N N 238 
LYS HD3  H  N N 239 
LYS HE2  H  N N 240 
LYS HE3  H  N N 241 
LYS HZ1  H  N N 242 
LYS HZ2  H  N N 243 
LYS HZ3  H  N N 244 
LYS HXT  H  N N 245 
MET N    N  N N 246 
MET CA   C  N S 247 
MET C    C  N N 248 
MET O    O  N N 249 
MET CB   C  N N 250 
MET CG   C  N N 251 
MET SD   S  N N 252 
MET CE   C  N N 253 
MET OXT  O  N N 254 
MET H    H  N N 255 
MET H2   H  N N 256 
MET HA   H  N N 257 
MET HB2  H  N N 258 
MET HB3  H  N N 259 
MET HG2  H  N N 260 
MET HG3  H  N N 261 
MET HE1  H  N N 262 
MET HE2  H  N N 263 
MET HE3  H  N N 264 
MET HXT  H  N N 265 
PHE N    N  N N 266 
PHE CA   C  N S 267 
PHE C    C  N N 268 
PHE O    O  N N 269 
PHE CB   C  N N 270 
PHE CG   C  Y N 271 
PHE CD1  C  Y N 272 
PHE CD2  C  Y N 273 
PHE CE1  C  Y N 274 
PHE CE2  C  Y N 275 
PHE CZ   C  Y N 276 
PHE OXT  O  N N 277 
PHE H    H  N N 278 
PHE H2   H  N N 279 
PHE HA   H  N N 280 
PHE HB2  H  N N 281 
PHE HB3  H  N N 282 
PHE HD1  H  N N 283 
PHE HD2  H  N N 284 
PHE HE1  H  N N 285 
PHE HE2  H  N N 286 
PHE HZ   H  N N 287 
PHE HXT  H  N N 288 
PRO N    N  N N 289 
PRO CA   C  N S 290 
PRO C    C  N N 291 
PRO O    O  N N 292 
PRO CB   C  N N 293 
PRO CG   C  N N 294 
PRO CD   C  N N 295 
PRO OXT  O  N N 296 
PRO H    H  N N 297 
PRO HA   H  N N 298 
PRO HB2  H  N N 299 
PRO HB3  H  N N 300 
PRO HG2  H  N N 301 
PRO HG3  H  N N 302 
PRO HD2  H  N N 303 
PRO HD3  H  N N 304 
PRO HXT  H  N N 305 
SER N    N  N N 306 
SER CA   C  N S 307 
SER C    C  N N 308 
SER O    O  N N 309 
SER CB   C  N N 310 
SER OG   O  N N 311 
SER OXT  O  N N 312 
SER H    H  N N 313 
SER H2   H  N N 314 
SER HA   H  N N 315 
SER HB2  H  N N 316 
SER HB3  H  N N 317 
SER HG   H  N N 318 
SER HXT  H  N N 319 
THR N    N  N N 320 
THR CA   C  N S 321 
THR C    C  N N 322 
THR O    O  N N 323 
THR CB   C  N R 324 
THR OG1  O  N N 325 
THR CG2  C  N N 326 
THR OXT  O  N N 327 
THR H    H  N N 328 
THR H2   H  N N 329 
THR HA   H  N N 330 
THR HB   H  N N 331 
THR HG1  H  N N 332 
THR HG21 H  N N 333 
THR HG22 H  N N 334 
THR HG23 H  N N 335 
THR HXT  H  N N 336 
TRP N    N  N N 337 
TRP CA   C  N S 338 
TRP C    C  N N 339 
TRP O    O  N N 340 
TRP CB   C  N N 341 
TRP CG   C  Y N 342 
TRP CD1  C  Y N 343 
TRP CD2  C  Y N 344 
TRP NE1  N  Y N 345 
TRP CE2  C  Y N 346 
TRP CE3  C  Y N 347 
TRP CZ2  C  Y N 348 
TRP CZ3  C  Y N 349 
TRP CH2  C  Y N 350 
TRP OXT  O  N N 351 
TRP H    H  N N 352 
TRP H2   H  N N 353 
TRP HA   H  N N 354 
TRP HB2  H  N N 355 
TRP HB3  H  N N 356 
TRP HD1  H  N N 357 
TRP HE1  H  N N 358 
TRP HE3  H  N N 359 
TRP HZ2  H  N N 360 
TRP HZ3  H  N N 361 
TRP HH2  H  N N 362 
TRP HXT  H  N N 363 
TYR N    N  N N 364 
TYR CA   C  N S 365 
TYR C    C  N N 366 
TYR O    O  N N 367 
TYR CB   C  N N 368 
TYR CG   C  Y N 369 
TYR CD1  C  Y N 370 
TYR CD2  C  Y N 371 
TYR CE1  C  Y N 372 
TYR CE2  C  Y N 373 
TYR CZ   C  Y N 374 
TYR OH   O  N N 375 
TYR OXT  O  N N 376 
TYR H    H  N N 377 
TYR H2   H  N N 378 
TYR HA   H  N N 379 
TYR HB2  H  N N 380 
TYR HB3  H  N N 381 
TYR HD1  H  N N 382 
TYR HD2  H  N N 383 
TYR HE1  H  N N 384 
TYR HE2  H  N N 385 
TYR HH   H  N N 386 
TYR HXT  H  N N 387 
VAL N    N  N N 388 
VAL CA   C  N S 389 
VAL C    C  N N 390 
VAL O    O  N N 391 
VAL CB   C  N N 392 
VAL CG1  C  N N 393 
VAL CG2  C  N N 394 
VAL OXT  O  N N 395 
VAL H    H  N N 396 
VAL H2   H  N N 397 
VAL HA   H  N N 398 
VAL HB   H  N N 399 
VAL HG11 H  N N 400 
VAL HG12 H  N N 401 
VAL HG13 H  N N 402 
VAL HG21 H  N N 403 
VAL HG22 H  N N 404 
VAL HG23 H  N N 405 
VAL HXT  H  N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-P0A4U8-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9O8N 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.010236 
_atom_sites.fract_transf_matrix[1][2]   0.005910 
_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]   0.011819 
_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]   0.012773 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 8   ? 40.644 6.379   20.350  1.00 66.28 ? 1   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 8   ? 39.741 6.905   19.280  1.00 69.44 ? 1   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 8   ? 40.409 8.071   18.547  1.00 70.32 ? 1   HIS A C   1 
ATOM   4    O  O   . HIS A 1 8   ? 40.208 9.234   18.898  1.00 72.91 ? 1   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 8   ? 38.397 7.345   19.874  1.00 58.85 ? 1   HIS A CB  1 
ATOM   6    N  N   . THR A 1 9   ? 41.202 7.746   17.525  1.00 72.09 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 9   ? 41.895 8.765   16.745  1.00 74.88 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 9   ? 40.918 9.803   16.203  1.00 85.78 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 9   ? 39.766 9.494   15.879  1.00 93.58 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 9   ? 42.642 8.120   15.573  1.00 72.93 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 9   ? 41.980 6.906   15.196  1.00 73.38 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 9   ? 44.077 7.827   15.940  1.00 53.28 ? 2   THR A CG2 1 
ATOM   13   N  N   . LEU A 1 10  ? 41.398 11.048  16.092  1.00 87.27 ? 3   LEU A N   1 
ATOM   14   C  CA  . LEU A 1 10  ? 40.592 12.107  15.488  1.00 85.65 ? 3   LEU A CA  1 
ATOM   15   C  C   . LEU A 1 10  ? 40.331 11.811  14.014  1.00 83.33 ? 3   LEU A C   1 
ATOM   16   O  O   . LEU A 1 10  ? 39.195 11.931  13.537  1.00 87.33 ? 3   LEU A O   1 
ATOM   17   C  CB  . LEU A 1 10  ? 41.276 13.464  15.660  1.00 64.71 ? 3   LEU A CB  1 
ATOM   18   N  N   . ASP A 1 11  ? 41.377 11.437  13.268  1.00 51.39 ? 4   ASP A N   1 
ATOM   19   C  CA  . ASP A 1 11  ? 41.181 10.776  11.984  1.00 49.13 ? 4   ASP A CA  1 
ATOM   20   C  C   . ASP A 1 11  ? 42.141 9.606   11.851  1.00 39.39 ? 4   ASP A C   1 
ATOM   21   O  O   . ASP A 1 11  ? 43.361 9.785   11.693  1.00 32.24 ? 4   ASP A O   1 
ATOM   22   C  CB  . ASP A 1 11  ? 41.356 11.677  10.776  1.00 52.25 ? 4   ASP A CB  1 
ATOM   23   C  CG  . ASP A 1 11  ? 40.980 10.947  9.494   1.00 53.54 ? 4   ASP A CG  1 
ATOM   24   O  OD1 . ASP A 1 11  ? 40.029 10.126  9.538   1.00 69.16 ? 4   ASP A OD1 1 
ATOM   25   O  OD2 . ASP A 1 11  ? 41.639 11.150  8.462   1.00 46.96 ? 4   ASP A OD2 1 
ATOM   26   N  N   . LEU A 1 12  ? 41.561 8.416   11.834  1.00 38.83 ? 5   LEU A N   1 
ATOM   27   C  CA  . LEU A 1 12  ? 42.338 7.189   11.788  1.00 32.59 ? 5   LEU A CA  1 
ATOM   28   C  C   . LEU A 1 12  ? 43.183 7.095   10.523  1.00 29.38 ? 5   LEU A C   1 
ATOM   29   O  O   . LEU A 1 12  ? 44.358 6.714   10.574  1.00 25.47 ? 5   LEU A O   1 
ATOM   30   C  CB  . LEU A 1 12  ? 41.364 6.026   11.881  1.00 36.93 ? 5   LEU A CB  1 
ATOM   31   C  CG  . LEU A 1 12  ? 41.955 4.635   11.749  1.00 26.10 ? 5   LEU A CG  1 
ATOM   32   C  CD1 . LEU A 1 12  ? 42.942 4.417   12.859  1.00 36.30 ? 5   LEU A CD1 1 
ATOM   33   C  CD2 . LEU A 1 12  ? 40.806 3.648   11.789  1.00 33.44 ? 5   LEU A CD2 1 
ATOM   34   N  N   . GLN A 1 13  ? 42.590 7.393   9.368   1.00 25.60 ? 6   GLN A N   1 
ATOM   35   C  CA  . GLN A 1 13  ? 43.349 7.304   8.125   1.00 25.55 ? 6   GLN A CA  1 
ATOM   36   C  C   . GLN A 1 13  ? 44.570 8.210   8.179   1.00 25.72 ? 6   GLN A C   1 
ATOM   37   O  O   . GLN A 1 13  ? 45.677 7.809   7.810   1.00 22.72 ? 6   GLN A O   1 
ATOM   38   C  CB  . GLN A 1 13  ? 42.453 7.665   6.939   1.00 27.67 ? 6   GLN A CB  1 
ATOM   39   C  CG  . GLN A 1 13  ? 43.174 7.689   5.605   1.00 28.31 ? 6   GLN A CG  1 
ATOM   40   C  CD  . GLN A 1 13  ? 42.220 7.740   4.422   1.00 30.86 ? 6   GLN A CD  1 
ATOM   41   O  OE1 . GLN A 1 13  ? 40.998 7.670   4.586   1.00 34.64 ? 6   GLN A OE1 1 
ATOM   42   N  NE2 . GLN A 1 13  ? 42.778 7.847   3.218   1.00 35.92 ? 6   GLN A NE2 1 
ATOM   43   N  N   . THR A 1 14  ? 44.388 9.444   8.644   1.00 24.85 ? 7   THR A N   1 
ATOM   44   C  CA  . THR A 1 14  ? 45.513 10.371  8.680   1.00 25.29 ? 7   THR A CA  1 
ATOM   45   C  C   . THR A 1 14  ? 46.602 9.890   9.622   1.00 24.49 ? 7   THR A C   1 
ATOM   46   O  O   . THR A 1 14  ? 47.797 9.973   9.298   1.00 23.84 ? 7   THR A O   1 
ATOM   47   C  CB  . THR A 1 14  ? 45.019 11.757  9.073   1.00 27.26 ? 7   THR A CB  1 
ATOM   48   O  OG1 . THR A 1 14  ? 44.178 12.238  8.019   1.00 34.06 ? 7   THR A OG1 1 
ATOM   49   C  CG2 . THR A 1 14  ? 46.186 12.683  9.272   1.00 35.21 ? 7   THR A CG2 1 
ATOM   50   N  N   . THR A 1 15  ? 46.219 9.366   10.786  1.00 23.20 ? 8   THR A N   1 
ATOM   51   C  CA  . THR A 1 15  ? 47.216 8.824   11.701  1.00 24.11 ? 8   THR A CA  1 
ATOM   52   C  C   . THR A 1 15  ? 47.986 7.682   11.055  1.00 23.69 ? 8   THR A C   1 
ATOM   53   O  O   . THR A 1 15  ? 49.216 7.608   11.166  1.00 19.63 ? 8   THR A O   1 
ATOM   54   C  CB  . THR A 1 15  ? 46.553 8.353   12.993  1.00 25.34 ? 8   THR A CB  1 
ATOM   55   O  OG1 . THR A 1 15  ? 45.850 9.436   13.601  1.00 28.23 ? 8   THR A OG1 1 
ATOM   56   C  CG2 . THR A 1 15  ? 47.598 7.852   13.953  1.00 26.13 ? 8   THR A CG2 1 
ATOM   57   N  N   . ILE A 1 16  ? 47.283 6.788   10.347  1.00 19.51 ? 9   ILE A N   1 
ATOM   58   C  CA  . ILE A 1 16  ? 47.968 5.683   9.691   1.00 17.72 ? 9   ILE A CA  1 
ATOM   59   C  C   . ILE A 1 16  ? 48.903 6.210   8.620   1.00 19.66 ? 9   ILE A C   1 
ATOM   60   O  O   . ILE A 1 16  ? 50.035 5.744   8.476   1.00 18.52 ? 9   ILE A O   1 
ATOM   61   C  CB  . ILE A 1 16  ? 46.951 4.683   9.104   1.00 18.99 ? 9   ILE A CB  1 
ATOM   62   C  CG1 . ILE A 1 16  ? 46.202 4.000   10.240  1.00 19.79 ? 9   ILE A CG1 1 
ATOM   63   C  CG2 . ILE A 1 16  ? 47.671 3.702   8.197   1.00 18.49 ? 9   ILE A CG2 1 
ATOM   64   C  CD1 . ILE A 1 16  ? 47.078 3.118   11.121  1.00 20.22 ? 9   ILE A CD1 1 
ATOM   65   N  N   . GLU A 1 17  ? 48.454 7.219   7.879   1.00 21.99 ? 10  GLU A N   1 
ATOM   66   C  CA  . GLU A 1 17  ? 49.257 7.707   6.761   1.00 21.65 ? 10  GLU A CA  1 
ATOM   67   C  C   . GLU A 1 17  ? 50.505 8.419   7.256   1.00 19.36 ? 10  GLU A C   1 
ATOM   68   O  O   . GLU A 1 17  ? 51.578 8.305   6.644   1.00 22.78 ? 10  GLU A O   1 
ATOM   69   C  CB  . GLU A 1 17  ? 48.389 8.597   5.883   1.00 25.27 ? 10  GLU A CB  1 
ATOM   70   C  CG  . GLU A 1 17  ? 47.405 7.786   5.025   1.00 28.84 ? 10  GLU A CG  1 
ATOM   71   C  CD  . GLU A 1 17  ? 46.393 8.646   4.293   1.00 34.22 ? 10  GLU A CD  1 
ATOM   72   O  OE1 . GLU A 1 17  ? 46.248 9.834   4.658   1.00 33.43 ? 10  GLU A OE1 1 
ATOM   73   O  OE2 . GLU A 1 17  ? 45.744 8.132   3.351   1.00 35.18 ? 10  GLU A OE2 1 
ATOM   74   N  N   . GLN A 1 18  ? 50.396 9.158   8.361   1.00 18.64 ? 11  GLN A N   1 
ATOM   75   C  CA  . GLN A 1 18  ? 51.576 9.818   8.917   1.00 22.24 ? 11  GLN A CA  1 
ATOM   76   C  C   . GLN A 1 18  ? 52.517 8.819   9.595   1.00 19.74 ? 11  GLN A C   1 
ATOM   77   O  O   . GLN A 1 18  ? 53.738 8.998   9.556   1.00 21.00 ? 11  GLN A O   1 
ATOM   78   C  CB  . GLN A 1 18  ? 51.127 10.924  9.870   1.00 24.39 ? 11  GLN A CB  1 
ATOM   79   C  CG  . GLN A 1 18  ? 50.452 12.065  9.108   1.00 21.54 ? 11  GLN A CG  1 
ATOM   80   C  CD  . GLN A 1 18  ? 50.014 13.233  9.972   1.00 28.45 ? 11  GLN A CD  1 
ATOM   81   O  OE1 . GLN A 1 18  ? 49.802 13.085  11.167  1.00 31.96 ? 11  GLN A OE1 1 
ATOM   82   N  NE2 . GLN A 1 18  ? 49.872 14.406  9.355   1.00 31.33 ? 11  GLN A NE2 1 
ATOM   83   N  N   . ALA A 1 19  ? 51.983 7.752   10.188  1.00 19.67 ? 12  ALA A N   1 
ATOM   84   C  CA  . ALA A 1 19  ? 52.845 6.704   10.719  1.00 19.39 ? 12  ALA A CA  1 
ATOM   85   C  C   . ALA A 1 19  ? 53.601 6.010   9.595   1.00 16.58 ? 12  ALA A C   1 
ATOM   86   O  O   . ALA A 1 19  ? 54.793 5.710   9.727   1.00 18.24 ? 12  ALA A O   1 
ATOM   87   C  CB  . ALA A 1 19  ? 52.012 5.693   11.506  1.00 18.77 ? 12  ALA A CB  1 
ATOM   88   N  N   . TRP A 1 20  ? 52.915 5.732   8.486   1.00 17.91 ? 13  TRP A N   1 
ATOM   89   C  CA  . TRP A 1 20  ? 53.589 5.189   7.312   1.00 17.19 ? 13  TRP A CA  1 
ATOM   90   C  C   . TRP A 1 20  ? 54.754 6.070   6.883   1.00 19.55 ? 13  TRP A C   1 
ATOM   91   O  O   . TRP A 1 20  ? 55.850 5.579   6.588   1.00 19.80 ? 13  TRP A O   1 
ATOM   92   C  CB  . TRP A 1 20  ? 52.576 5.047   6.178   1.00 21.23 ? 13  TRP A CB  1 
ATOM   93   C  CG  . TRP A 1 20  ? 53.135 4.387   4.988   1.00 19.89 ? 13  TRP A CG  1 
ATOM   94   C  CD1 . TRP A 1 20  ? 53.405 4.953   3.785   1.00 23.11 ? 13  TRP A CD1 1 
ATOM   95   C  CD2 . TRP A 1 20  ? 53.489 3.014   4.884   1.00 22.12 ? 13  TRP A CD2 1 
ATOM   96   N  NE1 . TRP A 1 20  ? 53.917 3.999   2.920   1.00 25.25 ? 13  TRP A NE1 1 
ATOM   97   C  CE2 . TRP A 1 20  ? 53.984 2.806   3.588   1.00 25.05 ? 13  TRP A CE2 1 
ATOM   98   C  CE3 . TRP A 1 20  ? 53.452 1.940   5.773   1.00 20.88 ? 13  TRP A CE3 1 
ATOM   99   C  CZ2 . TRP A 1 20  ? 54.429 1.559   3.153   1.00 30.79 ? 13  TRP A CZ2 1 
ATOM   100  C  CZ3 . TRP A 1 20  ? 53.904 0.707   5.341   1.00 27.02 ? 13  TRP A CZ3 1 
ATOM   101  C  CH2 . TRP A 1 20  ? 54.378 0.530   4.051   1.00 28.65 ? 13  TRP A CH2 1 
ATOM   102  N  N   . GLU A 1 21  ? 54.546 7.380   6.854   1.00 21.08 ? 14  GLU A N   1 
ATOM   103  C  CA  . GLU A 1 21  ? 55.613 8.270   6.424   1.00 21.60 ? 14  GLU A CA  1 
ATOM   104  C  C   . GLU A 1 21  ? 56.782 8.215   7.391   1.00 20.37 ? 14  GLU A C   1 
ATOM   105  O  O   . GLU A 1 21  ? 57.933 8.429   6.994   1.00 22.81 ? 14  GLU A O   1 
ATOM   106  C  CB  . GLU A 1 21  ? 55.067 9.695   6.285   1.00 19.78 ? 14  GLU A CB  1 
ATOM   107  C  CG  . GLU A 1 21  ? 54.106 9.864   5.104   1.00 24.00 ? 14  GLU A CG  1 
ATOM   108  C  CD  . GLU A 1 21  ? 53.206 11.109  5.207   1.00 50.14 ? 14  GLU A CD  1 
ATOM   109  O  OE1 . GLU A 1 21  ? 52.393 11.344  4.270   1.00 52.04 ? 14  GLU A OE1 1 
ATOM   110  O  OE2 . GLU A 1 21  ? 53.302 11.847  6.202   1.00 47.54 ? 14  GLU A OE2 1 
ATOM   111  N  N   . ASN A 1 22  ? 56.494 7.920   8.656   1.00 18.66 ? 15  ASN A N   1 
ATOM   112  C  CA  . ASN A 1 22  ? 57.476 7.852   9.723   1.00 21.17 ? 15  ASN A CA  1 
ATOM   113  C  C   . ASN A 1 22  ? 57.956 6.427   9.969   1.00 21.14 ? 15  ASN A C   1 
ATOM   114  O  O   . ASN A 1 22  ? 58.598 6.177   10.994  1.00 24.23 ? 15  ASN A O   1 
ATOM   115  C  CB  . ASN A 1 22  ? 56.855 8.416   11.003  1.00 22.00 ? 15  ASN A CB  1 
ATOM   116  C  CG  . ASN A 1 22  ? 57.841 8.588   12.112  1.00 22.22 ? 15  ASN A CG  1 
ATOM   117  O  OD1 . ASN A 1 22  ? 58.922 9.127   11.911  1.00 25.41 ? 15  ASN A OD1 1 
ATOM   118  N  ND2 . ASN A 1 22  ? 57.466 8.150   13.318  1.00 26.46 ? 15  ASN A ND2 1 
ATOM   119  N  N   . ARG A 1 23  ? 57.682 5.499   9.049   1.00 19.97 ? 16  ARG A N   1 
ATOM   120  C  CA  . ARG A 1 23  ? 57.829 4.085   9.390   1.00 22.21 ? 16  ARG A CA  1 
ATOM   121  C  C   . ARG A 1 23  ? 59.280 3.692   9.652   1.00 24.98 ? 16  ARG A C   1 
ATOM   122  O  O   . ARG A 1 23  ? 59.529 2.741   10.403  1.00 26.84 ? 16  ARG A O   1 
ATOM   123  C  CB  . ARG A 1 23  ? 57.243 3.200   8.294   1.00 20.34 ? 16  ARG A CB  1 
ATOM   124  C  CG  . ARG A 1 23  ? 57.949 3.244   6.955   1.00 23.30 ? 16  ARG A CG  1 
ATOM   125  C  CD  . ARG A 1 23  ? 57.111 2.517   5.876   1.00 29.50 ? 16  ARG A CD  1 
ATOM   126  N  NE  . ARG A 1 23  ? 57.655 2.560   4.521   1.00 26.41 ? 16  ARG A NE  1 
ATOM   127  C  CZ  . ARG A 1 23  ? 57.515 3.577   3.675   1.00 26.23 ? 16  ARG A CZ  1 
ATOM   128  N  NH1 . ARG A 1 23  ? 56.938 4.718   4.044   1.00 26.28 ? 16  ARG A NH1 1 
ATOM   129  N  NH2 . ARG A 1 23  ? 57.991 3.460   2.434   1.00 30.92 ? 16  ARG A NH2 1 
ATOM   130  N  N   . ALA A 1 24  ? 60.244 4.378   9.040   1.00 25.71 ? 17  ALA A N   1 
ATOM   131  C  CA  . ALA A 1 24  ? 61.641 4.022   9.285   1.00 30.54 ? 17  ALA A CA  1 
ATOM   132  C  C   . ALA A 1 24  ? 62.028 4.211   10.744  1.00 35.49 ? 17  ALA A C   1 
ATOM   133  O  O   . ALA A 1 24  ? 63.023 3.636   11.194  1.00 36.67 ? 17  ALA A O   1 
ATOM   134  C  CB  . ALA A 1 24  ? 62.567 4.846   8.396   1.00 32.69 ? 17  ALA A CB  1 
ATOM   135  N  N   . ASN A 1 25  ? 61.269 5.014   11.486  1.00 32.74 ? 18  ASN A N   1 
ATOM   136  C  CA  . ASN A 1 25  ? 61.550 5.321   12.878  1.00 26.41 ? 18  ASN A CA  1 
ATOM   137  C  C   . ASN A 1 25  ? 60.659 4.554   13.838  1.00 27.89 ? 18  ASN A C   1 
ATOM   138  O  O   . ASN A 1 25  ? 60.677 4.835   15.040  1.00 36.42 ? 18  ASN A O   1 
ATOM   139  C  CB  . ASN A 1 25  ? 61.383 6.825   13.113  1.00 35.35 ? 18  ASN A CB  1 
ATOM   140  C  CG  . ASN A 1 25  ? 62.280 7.650   12.228  1.00 38.92 ? 18  ASN A CG  1 
ATOM   141  O  OD1 . ASN A 1 25  ? 63.492 7.458   12.212  1.00 37.21 ? 18  ASN A OD1 1 
ATOM   142  N  ND2 . ASN A 1 25  ? 61.682 8.554   11.454  1.00 37.70 ? 18  ASN A ND2 1 
ATOM   143  N  N   . LEU A 1 26  ? 59.852 3.627   13.333  1.00 28.03 ? 19  LEU A N   1 
ATOM   144  C  CA  . LEU A 1 26  ? 58.965 2.819   14.149  1.00 24.28 ? 19  LEU A CA  1 
ATOM   145  C  C   . LEU A 1 26  ? 59.537 1.415   14.294  1.00 31.00 ? 19  LEU A C   1 
ATOM   146  O  O   . LEU A 1 26  ? 60.033 0.836   13.329  1.00 30.70 ? 19  LEU A O   1 
ATOM   147  C  CB  . LEU A 1 26  ? 57.567 2.745   13.522  1.00 23.90 ? 19  LEU A CB  1 
ATOM   148  C  CG  . LEU A 1 26  ? 56.841 4.093   13.513  1.00 25.94 ? 19  LEU A CG  1 
ATOM   149  C  CD1 . LEU A 1 26  ? 55.539 4.020   12.704  1.00 27.56 ? 19  LEU A CD1 1 
ATOM   150  C  CD2 . LEU A 1 26  ? 56.568 4.547   14.927  1.00 30.75 ? 19  LEU A CD2 1 
ATOM   151  N  N   . SER A 1 27  ? 59.459 0.891   15.505  1.00 28.78 ? 20  SER A N   1 
ATOM   152  C  CA  . SER A 1 27  ? 59.896 -0.469  15.822  1.00 27.91 ? 20  SER A CA  1 
ATOM   153  C  C   . SER A 1 27  ? 59.002 -0.973  16.925  1.00 31.79 ? 20  SER A C   1 
ATOM   154  O  O   . SER A 1 27  ? 58.222 -0.209  17.515  1.00 29.66 ? 20  SER A O   1 
ATOM   155  C  CB  . SER A 1 27  ? 61.351 -0.505  16.282  1.00 32.88 ? 20  SER A CB  1 
ATOM   156  O  OG  . SER A 1 27  ? 61.463 0.079   17.575  1.00 37.82 ? 20  SER A OG  1 
ATOM   157  N  N   . PRO A 1 28  ? 59.123 -2.258  17.282  1.00 29.25 ? 21  PRO A N   1 
ATOM   158  C  CA  . PRO A 1 28  ? 58.356 -2.790  18.417  1.00 36.02 ? 21  PRO A CA  1 
ATOM   159  C  C   . PRO A 1 28  ? 58.736 -2.202  19.767  1.00 39.48 ? 21  PRO A C   1 
ATOM   160  O  O   . PRO A 1 28  ? 58.022 -2.455  20.744  1.00 49.28 ? 21  PRO A O   1 
ATOM   161  C  CB  . PRO A 1 28  ? 58.668 -4.293  18.388  1.00 34.42 ? 21  PRO A CB  1 
ATOM   162  C  CG  . PRO A 1 28  ? 59.119 -4.574  16.977  1.00 34.90 ? 21  PRO A CG  1 
ATOM   163  C  CD  . PRO A 1 28  ? 59.852 -3.315  16.557  1.00 26.40 ? 21  PRO A CD  1 
ATOM   164  N  N   . VAL A 1 29  ? 59.851 -1.491  19.886  1.00 31.28 ? 22  VAL A N   1 
ATOM   165  C  CA  . VAL A 1 29  ? 60.206 -0.850  21.142  1.00 37.51 ? 22  VAL A CA  1 
ATOM   166  C  C   . VAL A 1 29  ? 59.758 0.608   21.183  1.00 36.75 ? 22  VAL A C   1 
ATOM   167  O  O   . VAL A 1 29  ? 59.305 1.090   22.221  1.00 43.81 ? 22  VAL A O   1 
ATOM   168  C  CB  . VAL A 1 29  ? 61.725 -0.960  21.398  1.00 39.28 ? 22  VAL A CB  1 
ATOM   169  C  CG1 . VAL A 1 29  ? 62.027 -0.675  22.872  1.00 52.60 ? 22  VAL A CG1 1 
ATOM   170  C  CG2 . VAL A 1 29  ? 62.250 -2.321  20.990  1.00 51.19 ? 22  VAL A CG2 1 
ATOM   171  N  N   . ASP A 1 30  ? 59.873 1.339   20.081  1.00 34.90 ? 23  ASP A N   1 
ATOM   172  C  CA  . ASP A 1 30  ? 59.764 2.794   20.155  1.00 43.71 ? 23  ASP A CA  1 
ATOM   173  C  C   . ASP A 1 30  ? 58.389 3.362   19.801  1.00 53.18 ? 23  ASP A C   1 
ATOM   174  O  O   . ASP A 1 30  ? 58.193 4.579   19.917  1.00 58.79 ? 23  ASP A O   1 
ATOM   175  C  CB  . ASP A 1 30  ? 60.820 3.434   19.245  1.00 48.78 ? 23  ASP A CB  1 
ATOM   176  C  CG  . ASP A 1 30  ? 60.491 3.288   17.770  1.00 58.64 ? 23  ASP A CG  1 
ATOM   177  O  OD1 . ASP A 1 30  ? 59.318 2.958   17.411  1.00 45.02 ? 23  ASP A OD1 1 
ATOM   178  O  OD2 . ASP A 1 30  ? 61.430 3.511   16.972  1.00 51.45 ? 23  ASP A OD2 1 
ATOM   179  N  N   . ALA A 1 31  ? 57.434 2.536   19.393  1.00 34.76 ? 24  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 31  ? 56.196 3.041   18.816  1.00 31.46 ? 24  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 31  ? 55.249 3.613   19.864  1.00 26.52 ? 24  ALA A C   1 
ATOM   182  O  O   . ALA A 1 31  ? 55.074 3.050   20.940  1.00 28.20 ? 24  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 31  ? 55.482 1.930   18.041  1.00 32.57 ? 24  ALA A CB  1 
ATOM   184  N  N   . SER A 1 32  ? 54.614 4.726   19.514  1.00 22.14 ? 25  SER A N   1 
ATOM   185  C  CA  . SER A 1 32  ? 53.749 5.425   20.442  1.00 23.28 ? 25  SER A CA  1 
ATOM   186  C  C   . SER A 1 32  ? 52.447 4.668   20.659  1.00 23.77 ? 25  SER A C   1 
ATOM   187  O  O   . SER A 1 32  ? 51.993 3.905   19.808  1.00 21.86 ? 25  SER A O   1 
ATOM   188  C  CB  . SER A 1 32  ? 53.411 6.803   19.895  1.00 23.00 ? 25  SER A CB  1 
ATOM   189  O  OG  . SER A 1 32  ? 52.658 6.638   18.716  1.00 20.92 ? 25  SER A OG  1 
ATOM   190  N  N   . ALA A 1 33  ? 51.809 4.957   21.794  1.00 18.65 ? 26  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 33  ? 50.469 4.429   22.045  1.00 21.08 ? 26  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 33  ? 49.489 4.889   20.972  1.00 20.65 ? 26  ALA A C   1 
ATOM   193  O  O   . ALA A 1 33  ? 48.597 4.140   20.563  1.00 19.37 ? 26  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 33  ? 49.988 4.860   23.423  1.00 23.41 ? 26  ALA A CB  1 
ATOM   195  N  N   . GLU A 1 34  ? 49.637 6.127   20.504  1.00 19.61 ? 27  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 34  ? 48.710 6.639   19.498  1.00 20.52 ? 27  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 34  ? 48.751 5.792   18.235  1.00 21.99 ? 27  GLU A C   1 
ATOM   198  O  O   . GLU A 1 34  ? 47.708 5.446   17.666  1.00 19.71 ? 27  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 34  ? 49.050 8.091   19.176  1.00 22.07 ? 27  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 34  ? 48.102 8.725   18.214  1.00 29.73 ? 27  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 34  ? 46.840 9.211   18.866  1.00 37.39 ? 27  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 34  ? 46.733 9.176   20.107  1.00 32.66 ? 27  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 34  ? 45.947 9.627   18.114  1.00 48.52 ? 27  GLU A OE2 1 
ATOM   204  N  N   . VAL A 1 35  ? 49.955 5.462   17.772  1.00 18.55 ? 28  VAL A N   1 
ATOM   205  C  CA  . VAL A 1 35  ? 50.080 4.726   16.511  1.00 18.38 ? 28  VAL A CA  1 
ATOM   206  C  C   . VAL A 1 35  ? 49.721 3.266   16.719  1.00 18.93 ? 28  VAL A C   1 
ATOM   207  O  O   . VAL A 1 35  ? 49.044 2.650   15.885  1.00 19.57 ? 28  VAL A O   1 
ATOM   208  C  CB  . VAL A 1 35  ? 51.502 4.893   15.951  1.00 19.01 ? 28  VAL A CB  1 
ATOM   209  C  CG1 . VAL A 1 35  ? 51.742 3.934   14.807  1.00 21.04 ? 28  VAL A CG1 1 
ATOM   210  C  CG2 . VAL A 1 35  ? 51.700 6.326   15.480  1.00 22.59 ? 28  VAL A CG2 1 
ATOM   211  N  N   . ARG A 1 36  ? 50.157 2.699   17.837  1.00 18.47 ? 29  ARG A N   1 
ATOM   212  C  CA  . ARG A 1 36  ? 49.811 1.312   18.131  1.00 18.35 ? 29  ARG A CA  1 
ATOM   213  C  C   . ARG A 1 36  ? 48.303 1.130   18.208  1.00 19.80 ? 29  ARG A C   1 
ATOM   214  O  O   . ARG A 1 36  ? 47.765 0.132   17.719  1.00 20.75 ? 29  ARG A O   1 
ATOM   215  C  CB  . ARG A 1 36  ? 50.436 0.885   19.444  1.00 23.35 ? 29  ARG A CB  1 
ATOM   216  C  CG  . ARG A 1 36  ? 51.932 0.712   19.424  1.00 24.57 ? 29  ARG A CG  1 
ATOM   217  C  CD  . ARG A 1 36  ? 52.415 0.194   20.797  1.00 36.62 ? 29  ARG A CD  1 
ATOM   218  N  NE  . ARG A 1 36  ? 53.868 0.101   20.868  1.00 47.12 ? 29  ARG A NE  1 
ATOM   219  C  CZ  . ARG A 1 36  ? 54.579 -0.941  20.454  1.00 58.94 ? 29  ARG A CZ  1 
ATOM   220  N  NH1 . ARG A 1 36  ? 54.001 -2.028  19.970  1.00 45.47 ? 29  ARG A NH1 1 
ATOM   221  N  NH2 . ARG A 1 36  ? 55.909 -0.885  20.522  1.00 61.93 ? 29  ARG A NH2 1 
ATOM   222  N  N   . ASP A 1 37  ? 47.607 2.077   18.844  1.00 19.92 ? 30  ASP A N   1 
ATOM   223  C  CA  . ASP A 1 37  ? 46.157 1.973   18.962  1.00 21.70 ? 30  ASP A CA  1 
ATOM   224  C  C   . ASP A 1 37  ? 45.476 2.130   17.607  1.00 22.11 ? 30  ASP A C   1 
ATOM   225  O  O   . ASP A 1 37  ? 44.468 1.469   17.336  1.00 20.62 ? 30  ASP A O   1 
ATOM   226  C  CB  . ASP A 1 37  ? 45.640 3.023   19.936  1.00 22.46 ? 30  ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 37  ? 45.991 2.711   21.387  1.00 32.12 ? 30  ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 37  ? 46.516 1.608   21.669  1.00 35.40 ? 30  ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 37  ? 45.738 3.576   22.243  1.00 33.66 ? 30  ASP A OD2 1 
ATOM   230  N  N   . ALA A 1 38  ? 45.972 3.043   16.768  1.00 18.60 ? 31  ALA A N   1 
ATOM   231  C  CA  . ALA A 1 38  ? 45.383 3.243   15.449  1.00 18.89 ? 31  ALA A CA  1 
ATOM   232  C  C   . ALA A 1 38  ? 45.551 1.992   14.599  1.00 18.25 ? 31  ALA A C   1 
ATOM   233  O  O   . ALA A 1 38  ? 44.616 1.555   13.913  1.00 20.65 ? 31  ALA A O   1 
ATOM   234  C  CB  . ALA A 1 38  ? 46.029 4.449   14.762  1.00 21.30 ? 31  ALA A CB  1 
ATOM   235  N  N   . VAL A 1 39  ? 46.735 1.389   14.641  1.00 18.79 ? 32  VAL A N   1 
ATOM   236  C  CA  . VAL A 1 39  ? 46.953 0.153   13.892  1.00 18.26 ? 32  VAL A CA  1 
ATOM   237  C  C   . VAL A 1 39  ? 46.081 -0.963  14.444  1.00 18.41 ? 32  VAL A C   1 
ATOM   238  O  O   . VAL A 1 39  ? 45.401 -1.667  13.686  1.00 20.10 ? 32  VAL A O   1 
ATOM   239  C  CB  . VAL A 1 39  ? 48.439 -0.223  13.929  1.00 17.26 ? 32  VAL A CB  1 
ATOM   240  C  CG1 . VAL A 1 39  ? 48.655 -1.589  13.339  1.00 18.00 ? 32  VAL A CG1 1 
ATOM   241  C  CG2 . VAL A 1 39  ? 49.233 0.815   13.168  1.00 18.11 ? 32  VAL A CG2 1 
ATOM   242  N  N   . GLU A 1 40  ? 46.068 -1.127  15.776  1.00 19.01 ? 33  GLU A N   1 
ATOM   243  C  CA  . GLU A 1 40  ? 45.270 -2.190  16.378  1.00 19.61 ? 33  GLU A CA  1 
ATOM   244  C  C   . GLU A 1 40  ? 43.797 -2.019  16.044  1.00 21.36 ? 33  GLU A C   1 
ATOM   245  O  O   . GLU A 1 40  ? 43.106 -2.997  15.757  1.00 21.08 ? 33  GLU A O   1 
ATOM   246  C  CB  . GLU A 1 40  ? 45.465 -2.233  17.898  1.00 25.50 ? 33  GLU A CB  1 
ATOM   247  C  CG  . GLU A 1 40  ? 44.596 -3.304  18.558  1.00 33.68 ? 33  GLU A CG  1 
ATOM   248  C  CD  . GLU A 1 40  ? 44.846 -3.476  20.041  1.00 52.31 ? 33  GLU A CD  1 
ATOM   249  O  OE1 . GLU A 1 40  ? 45.559 -2.636  20.627  1.00 54.29 ? 33  GLU A OE1 1 
ATOM   250  O  OE2 . GLU A 1 40  ? 44.323 -4.463  20.616  1.00 50.96 ? 33  GLU A OE2 1 
ATOM   251  N  N   . HIS A 1 41  ? 43.296 -0.783  16.082  1.00 21.35 ? 34  HIS A N   1 
ATOM   252  C  CA  . HIS A 1 41  ? 41.894 -0.538  15.760  1.00 20.88 ? 34  HIS A CA  1 
ATOM   253  C  C   . HIS A 1 41  ? 41.583 -0.894  14.312  1.00 19.04 ? 34  HIS A C   1 
ATOM   254  O  O   . HIS A 1 41  ? 40.478 -1.359  13.995  1.00 20.99 ? 34  HIS A O   1 
ATOM   255  C  CB  . HIS A 1 41  ? 41.568 0.933   16.029  1.00 24.63 ? 34  HIS A CB  1 
ATOM   256  C  CG  . HIS A 1 41  ? 40.118 1.261   15.914  1.00 35.94 ? 34  HIS A CG  1 
ATOM   257  N  ND1 . HIS A 1 41  ? 39.204 0.942   16.894  1.00 48.22 ? 34  HIS A ND1 1 
ATOM   258  C  CD2 . HIS A 1 41  ? 39.420 1.885   14.935  1.00 46.41 ? 34  HIS A CD2 1 
ATOM   259  C  CE1 . HIS A 1 41  ? 38.002 1.346   16.520  1.00 49.12 ? 34  HIS A CE1 1 
ATOM   260  N  NE2 . HIS A 1 41  ? 38.104 1.914   15.331  1.00 40.18 ? 34  HIS A NE2 1 
ATOM   261  N  N   . THR A 1 42  ? 42.531 -0.652  13.413  1.00 18.26 ? 35  THR A N   1 
ATOM   262  C  CA  . THR A 1 42  ? 42.313 -0.988  12.010  1.00 18.40 ? 35  THR A CA  1 
ATOM   263  C  C   . THR A 1 42  ? 42.288 -2.497  11.816  1.00 21.24 ? 35  THR A C   1 
ATOM   264  O  O   . THR A 1 42  ? 41.423 -3.023  11.107  1.00 19.23 ? 35  THR A O   1 
ATOM   265  C  CB  . THR A 1 42  ? 43.396 -0.365  11.145  1.00 19.42 ? 35  THR A CB  1 
ATOM   266  O  OG1 . THR A 1 42  ? 43.431 1.053   11.341  1.00 21.68 ? 35  THR A OG1 1 
ATOM   267  C  CG2 . THR A 1 42  ? 43.123 -0.623  9.676   1.00 19.38 ? 35  THR A CG2 1 
ATOM   268  N  N   . ILE A 1 43  ? 43.225 -3.208  12.445  1.00 18.49 ? 36  ILE A N   1 
ATOM   269  C  CA  . ILE A 1 43  ? 43.237 -4.667  12.339  1.00 17.12 ? 36  ILE A CA  1 
ATOM   270  C  C   . ILE A 1 43  ? 41.975 -5.251  12.967  1.00 18.79 ? 36  ILE A C   1 
ATOM   271  O  O   . ILE A 1 43  ? 41.389 -6.209  12.443  1.00 19.34 ? 36  ILE A O   1 
ATOM   272  C  CB  . ILE A 1 43  ? 44.504 -5.237  12.988  1.00 21.05 ? 36  ILE A CB  1 
ATOM   273  C  CG1 . ILE A 1 43  ? 45.766 -4.639  12.361  1.00 22.93 ? 36  ILE A CG1 1 
ATOM   274  C  CG2 . ILE A 1 43  ? 44.521 -6.761  12.874  1.00 23.28 ? 36  ILE A CG2 1 
ATOM   275  C  CD1 . ILE A 1 43  ? 45.863 -4.766  10.887  1.00 25.07 ? 36  ILE A CD1 1 
ATOM   276  N  N   . ASP A 1 44  ? 41.543 -4.696  14.109  1.00 18.77 ? 37  ASP A N   1 
ATOM   277  C  CA  . ASP A 1 44  ? 40.301 -5.158  14.727  1.00 20.63 ? 37  ASP A CA  1 
ATOM   278  C  C   . ASP A 1 44  ? 39.147 -5.017  13.740  1.00 22.17 ? 37  ASP A C   1 
ATOM   279  O  O   . ASP A 1 44  ? 38.289 -5.902  13.635  1.00 21.16 ? 37  ASP A O   1 
ATOM   280  C  CB  . ASP A 1 44  ? 39.968 -4.347  15.990  1.00 23.40 ? 37  ASP A CB  1 
ATOM   281  C  CG  . ASP A 1 44  ? 40.887 -4.636  17.163  1.00 34.32 ? 37  ASP A CG  1 
ATOM   282  O  OD1 . ASP A 1 44  ? 41.570 -5.664  17.164  1.00 39.39 ? 37  ASP A OD1 1 
ATOM   283  O  OD2 . ASP A 1 44  ? 40.898 -3.822  18.123  1.00 41.85 ? 37  ASP A OD2 1 
ATOM   284  N  N   . GLY A 1 45  ? 39.104 -3.880  13.038  1.00 21.64 ? 38  GLY A N   1 
ATOM   285  C  CA  . GLY A 1 45  ? 38.033 -3.641  12.082  1.00 24.31 ? 38  GLY A CA  1 
ATOM   286  C  C   . GLY A 1 45  ? 38.077 -4.620  10.926  1.00 21.69 ? 38  GLY A C   1 
ATOM   287  O  O   . GLY A 1 45  ? 37.043 -5.135  10.495  1.00 23.27 ? 38  GLY A O   1 
ATOM   288  N  N   . LEU A 1 46  ? 39.279 -4.913  10.427  1.00 17.37 ? 39  LEU A N   1 
ATOM   289  C  CA  . LEU A 1 46  ? 39.425 -5.957  9.420   1.00 18.18 ? 39  LEU A CA  1 
ATOM   290  C  C   . LEU A 1 46  ? 38.940 -7.299  9.938   1.00 21.16 ? 39  LEU A C   1 
ATOM   291  O  O   . LEU A 1 46  ? 38.264 -8.038  9.222   1.00 21.02 ? 39  LEU A O   1 
ATOM   292  C  CB  . LEU A 1 46  ? 40.875 -6.060  9.000   1.00 18.49 ? 39  LEU A CB  1 
ATOM   293  C  CG  . LEU A 1 46  ? 41.398 -4.935  8.108   1.00 18.98 ? 39  LEU A CG  1 
ATOM   294  C  CD1 . LEU A 1 46  ? 42.893 -5.113  7.947   1.00 19.23 ? 39  LEU A CD1 1 
ATOM   295  C  CD2 . LEU A 1 46  ? 40.709 -4.963  6.755   1.00 21.68 ? 39  LEU A CD2 1 
ATOM   296  N  N   . ASP A 1 47  ? 39.310 -7.640  11.171  1.00 18.52 ? 40  ASP A N   1 
ATOM   297  C  CA  . ASP A 1 47  ? 38.985 -8.945  11.724  1.00 20.56 ? 40  ASP A CA  1 
ATOM   298  C  C   . ASP A 1 47  ? 37.485 -9.138  11.821  1.00 21.52 ? 40  ASP A C   1 
ATOM   299  O  O   . ASP A 1 47  ? 36.982 -10.255 11.687  1.00 22.92 ? 40  ASP A O   1 
ATOM   300  C  CB  . ASP A 1 47  ? 39.639 -9.067  13.101  1.00 22.59 ? 40  ASP A CB  1 
ATOM   301  C  CG  . ASP A 1 47  ? 39.652 -10.472 13.621  1.00 31.82 ? 40  ASP A CG  1 
ATOM   302  O  OD1 . ASP A 1 47  ? 40.495 -11.256 13.151  1.00 28.12 ? 40  ASP A OD1 1 
ATOM   303  O  OD2 . ASP A 1 47  ? 38.832 -10.792 14.517  1.00 36.84 ? 40  ASP A OD2 1 
ATOM   304  N  N   . LEU A 1 48  ? 36.764 -8.060  12.124  1.00 21.51 ? 41  LEU A N   1 
ATOM   305  C  CA  . LEU A 1 48  ? 35.326 -8.053  12.293  1.00 23.29 ? 41  LEU A CA  1 
ATOM   306  C  C   . LEU A 1 48  ? 34.576 -7.816  10.999  1.00 21.83 ? 41  LEU A C   1 
ATOM   307  O  O   . LEU A 1 48  ? 33.341 -7.882  11.004  1.00 27.33 ? 41  LEU A O   1 
ATOM   308  C  CB  . LEU A 1 48  ? 34.945 -6.944  13.274  1.00 25.26 ? 41  LEU A CB  1 
ATOM   309  C  CG  . LEU A 1 48  ? 35.530 -7.090  14.666  1.00 33.20 ? 41  LEU A CG  1 
ATOM   310  C  CD1 . LEU A 1 48  ? 35.357 -5.764  15.417  1.00 45.33 ? 41  LEU A CD1 1 
ATOM   311  C  CD2 . LEU A 1 48  ? 34.850 -8.233  15.369  1.00 43.79 ? 41  LEU A CD2 1 
ATOM   312  N  N   . GLY A 1 49  ? 35.280 -7.508  9.923   1.00 23.17 ? 42  GLY A N   1 
ATOM   313  C  CA  . GLY A 1 49  ? 34.653 -7.169  8.668   1.00 23.41 ? 42  GLY A CA  1 
ATOM   314  C  C   . GLY A 1 49  ? 34.034 -5.792  8.618   1.00 27.31 ? 42  GLY A C   1 
ATOM   315  O  O   . GLY A 1 49  ? 33.280 -5.510  7.678   1.00 28.54 ? 42  GLY A O   1 
ATOM   316  N  N   . ARG A 1 50  ? 34.296 -4.940  9.615   1.00 24.46 ? 43  ARG A N   1 
ATOM   317  C  CA  A ARG A 1 50  ? 33.769 -3.578  9.536   0.50 25.96 ? 43  ARG A CA  1 
ATOM   318  C  CA  B ARG A 1 50  ? 33.818 -3.556  9.591   0.50 25.91 ? 43  ARG A CA  1 
ATOM   319  C  C   . ARG A 1 50  ? 34.579 -2.732  8.564   1.00 26.41 ? 43  ARG A C   1 
ATOM   320  O  O   . ARG A 1 50  ? 34.029 -1.799  7.961   1.00 27.98 ? 43  ARG A O   1 
ATOM   321  C  CB  A ARG A 1 50  ? 33.718 -2.925  10.915  0.50 28.25 ? 43  ARG A CB  1 
ATOM   322  C  CB  B ARG A 1 50  ? 33.981 -2.914  10.967  0.50 27.19 ? 43  ARG A CB  1 
ATOM   323  C  CG  A ARG A 1 50  ? 35.028 -2.790  11.649  0.50 34.52 ? 43  ARG A CG  1 
ATOM   324  C  CG  B ARG A 1 50  ? 33.118 -3.504  12.078  0.50 30.82 ? 43  ARG A CG  1 
ATOM   325  C  CD  A ARG A 1 50  ? 34.987 -1.674  12.727  0.50 41.73 ? 43  ARG A CD  1 
ATOM   326  C  CD  B ARG A 1 50  ? 33.021 -2.562  13.294  0.50 36.04 ? 43  ARG A CD  1 
ATOM   327  N  NE  A ARG A 1 50  ? 36.079 -0.722  12.536  0.50 37.82 ? 43  ARG A NE  1 
ATOM   328  N  NE  B ARG A 1 50  ? 34.177 -2.651  14.183  0.50 44.80 ? 43  ARG A NE  1 
ATOM   329  C  CZ  A ARG A 1 50  ? 37.196 -0.673  13.257  0.50 39.43 ? 43  ARG A CZ  1 
ATOM   330  C  CZ  B ARG A 1 50  ? 35.215 -1.823  14.175  0.50 40.26 ? 43  ARG A CZ  1 
ATOM   331  N  NH1 A ARG A 1 50  ? 37.347 -1.388  14.362  0.50 37.79 ? 43  ARG A NH1 1 
ATOM   332  N  NH1 B ARG A 1 50  ? 35.284 -0.802  13.331  0.50 37.02 ? 43  ARG A NH1 1 
ATOM   333  N  NH2 A ARG A 1 50  ? 38.188 0.111   12.856  0.50 38.33 ? 43  ARG A NH2 1 
ATOM   334  N  NH2 B ARG A 1 50  ? 36.209 -2.024  15.038  0.50 37.91 ? 43  ARG A NH2 1 
ATOM   335  N  N   . LEU A 1 51  ? 35.849 -3.051  8.390   1.00 21.42 ? 44  LEU A N   1 
ATOM   336  C  CA  . LEU A 1 51  ? 36.724 -2.527  7.361   1.00 20.50 ? 44  LEU A CA  1 
ATOM   337  C  C   . LEU A 1 51  ? 37.076 -3.653  6.404   1.00 24.73 ? 44  LEU A C   1 
ATOM   338  O  O   . LEU A 1 51  ? 37.091 -4.829  6.787   1.00 21.12 ? 44  LEU A O   1 
ATOM   339  C  CB  . LEU A 1 51  ? 38.025 -1.974  7.955   1.00 21.30 ? 44  LEU A CB  1 
ATOM   340  C  CG  . LEU A 1 51  ? 37.914 -0.793  8.908   1.00 22.77 ? 44  LEU A CG  1 
ATOM   341  C  CD1 . LEU A 1 51  ? 39.281 -0.466  9.464   1.00 24.30 ? 44  LEU A CD1 1 
ATOM   342  C  CD2 . LEU A 1 51  ? 37.333 0.398   8.191   1.00 31.75 ? 44  LEU A CD2 1 
ATOM   343  N  N   . ARG A 1 52  ? 37.395 -3.290  5.165   1.00 21.44 ? 45  ARG A N   1 
ATOM   344  C  CA  . ARG A 1 52  ? 37.877 -4.274  4.197   1.00 19.16 ? 45  ARG A CA  1 
ATOM   345  C  C   . ARG A 1 52  ? 38.856 -3.585  3.252   1.00 17.84 ? 45  ARG A C   1 
ATOM   346  O  O   . ARG A 1 52  ? 38.730 -2.390  2.968   1.00 20.85 ? 45  ARG A O   1 
ATOM   347  C  CB  . ARG A 1 52  ? 36.712 -4.951  3.471   1.00 25.19 ? 45  ARG A CB  1 
ATOM   348  C  CG  . ARG A 1 52  ? 35.757 -4.074  2.739   1.00 29.69 ? 45  ARG A CG  1 
ATOM   349  C  CD  . ARG A 1 52  ? 34.525 -4.919  2.352   1.00 26.13 ? 45  ARG A CD  1 
ATOM   350  N  NE  . ARG A 1 52  ? 34.882 -5.996  1.436   1.00 21.84 ? 45  ARG A NE  1 
ATOM   351  C  CZ  . ARG A 1 52  ? 34.025 -6.870  0.938   1.00 22.06 ? 45  ARG A CZ  1 
ATOM   352  N  NH1 . ARG A 1 52  ? 32.745 -6.841  1.265   1.00 25.45 ? 45  ARG A NH1 1 
ATOM   353  N  NH2 . ARG A 1 52  ? 34.461 -7.788  0.085   1.00 22.49 ? 45  ARG A NH2 1 
ATOM   354  N  N   . VAL A 1 53  ? 39.872 -4.337  2.824   1.00 17.72 ? 46  VAL A N   1 
ATOM   355  C  CA  . VAL A 1 53  ? 40.958 -3.751  2.041   1.00 18.27 ? 46  VAL A CA  1 
ATOM   356  C  C   . VAL A 1 53  ? 40.441 -3.243  0.706   1.00 21.63 ? 46  VAL A C   1 
ATOM   357  O  O   . VAL A 1 53  ? 40.938 -2.248  0.173   1.00 19.44 ? 46  VAL A O   1 
ATOM   358  C  CB  . VAL A 1 53  ? 42.084 -4.780  1.828   1.00 17.99 ? 46  VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 53  ? 43.142 -4.247  0.871   1.00 20.39 ? 46  VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 53  ? 42.700 -5.190  3.171   1.00 22.34 ? 46  VAL A CG2 1 
ATOM   361  N  N   . ALA A 1 54  ? 39.511 -3.974  0.097   1.00 19.26 ? 47  ALA A N   1 
ATOM   362  C  CA  . ALA A 1 54  ? 38.901 -3.562  -1.159  1.00 21.22 ? 47  ALA A CA  1 
ATOM   363  C  C   . ALA A 1 54  ? 37.404 -3.792  -1.060  1.00 23.78 ? 47  ALA A C   1 
ATOM   364  O  O   . ALA A 1 54  ? 36.952 -4.703  -0.368  1.00 24.56 ? 47  ALA A O   1 
ATOM   365  C  CB  . ALA A 1 54  ? 39.465 -4.333  -2.355  1.00 21.53 ? 47  ALA A CB  1 
ATOM   366  N  N   . GLU A 1 55  ? 36.640 -2.957  -1.759  1.00 24.46 ? 48  GLU A N   1 
ATOM   367  C  CA  . GLU A 1 55  ? 35.194 -3.119  -1.818  1.00 23.81 ? 48  GLU A CA  1 
ATOM   368  C  C   . GLU A 1 55  ? 34.704 -2.659  -3.179  1.00 25.37 ? 48  GLU A C   1 
ATOM   369  O  O   . GLU A 1 55  ? 35.369 -1.903  -3.888  1.00 26.16 ? 48  GLU A O   1 
ATOM   370  C  CB  . GLU A 1 55  ? 34.483 -2.347  -0.703  1.00 34.40 ? 48  GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 55  ? 34.796 -0.892  -0.688  1.00 36.32 ? 48  GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 55  ? 34.113 -0.179  0.474   1.00 48.96 ? 48  GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 55  ? 32.869 -0.114  0.494   1.00 47.77 ? 48  GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 55  ? 34.819 0.290   1.379   1.00 41.63 ? 48  GLU A OE2 1 
ATOM   375  N  N   . LYS A 1 56  ? 33.525 -3.125  -3.539  1.00 29.34 ? 49  LYS A N   1 
ATOM   376  C  CA  . LYS A 1 56  ? 32.949 -2.833  -4.837  1.00 29.07 ? 49  LYS A CA  1 
ATOM   377  C  C   . LYS A 1 56  ? 32.024 -1.631  -4.687  1.00 37.25 ? 49  LYS A C   1 
ATOM   378  O  O   . LYS A 1 56  ? 31.084 -1.665  -3.891  1.00 41.47 ? 49  LYS A O   1 
ATOM   379  C  CB  . LYS A 1 56  ? 32.212 -4.055  -5.372  1.00 29.62 ? 49  LYS A CB  1 
ATOM   380  C  CG  . LYS A 1 56  ? 32.030 -4.055  -6.874  1.00 36.62 ? 49  LYS A CG  1 
ATOM   381  C  CD  . LYS A 1 56  ? 31.446 -5.383  -7.346  1.00 34.71 ? 49  LYS A CD  1 
ATOM   382  C  CE  . LYS A 1 56  ? 31.371 -5.430  -8.854  1.00 40.33 ? 49  LYS A CE  1 
ATOM   383  N  NZ  . LYS A 1 56  ? 30.803 -6.705  -9.353  1.00 37.43 ? 49  LYS A NZ  1 
ATOM   384  N  N   . ILE A 1 57  ? 32.328 -0.566  -5.421  1.00 35.58 ? 50  ILE A N   1 
ATOM   385  C  CA  . ILE A 1 57  ? 31.555 0.675   -5.407  1.00 45.11 ? 50  ILE A CA  1 
ATOM   386  C  C   . ILE A 1 57  ? 31.282 1.092   -6.844  1.00 45.15 ? 50  ILE A C   1 
ATOM   387  O  O   . ILE A 1 57  ? 32.204 1.147   -7.665  1.00 49.59 ? 50  ILE A O   1 
ATOM   388  C  CB  . ILE A 1 57  ? 32.303 1.794   -4.654  1.00 43.98 ? 50  ILE A CB  1 
ATOM   389  C  CG1 . ILE A 1 57  ? 32.445 1.414   -3.183  1.00 45.48 ? 50  ILE A CG1 1 
ATOM   390  C  CG2 . ILE A 1 57  ? 31.590 3.123   -4.824  1.00 50.56 ? 50  ILE A CG2 1 
ATOM   391  C  CD1 . ILE A 1 57  ? 33.517 2.185   -2.465  1.00 51.52 ? 50  ILE A CD1 1 
ATOM   392  N  N   . ASP A 1 58  ? 30.025 1.408   -7.145  1.00 57.18 ? 51  ASP A N   1 
ATOM   393  C  CA  . ASP A 1 58  ? 29.633 1.778   -8.504  1.00 56.05 ? 51  ASP A CA  1 
ATOM   394  C  C   . ASP A 1 58  ? 30.074 0.710   -9.501  1.00 60.49 ? 51  ASP A C   1 
ATOM   395  O  O   . ASP A 1 58  ? 30.461 1.004   -10.632 1.00 59.85 ? 51  ASP A O   1 
ATOM   396  C  CB  . ASP A 1 58  ? 30.205 3.142   -8.884  1.00 55.16 ? 51  ASP A CB  1 
ATOM   397  N  N   . ASP A 1 59  ? 30.034 -0.549  -9.062  1.00 54.21 ? 52  ASP A N   1 
ATOM   398  C  CA  . ASP A 1 59  ? 30.350 -1.713  -9.882  1.00 47.51 ? 52  ASP A CA  1 
ATOM   399  C  C   . ASP A 1 59  ? 31.823 -1.789  -10.278 1.00 48.16 ? 52  ASP A C   1 
ATOM   400  O  O   . ASP A 1 59  ? 32.168 -2.454  -11.258 1.00 49.69 ? 52  ASP A O   1 
ATOM   401  C  CB  . ASP A 1 59  ? 29.474 -1.750  -11.140 1.00 59.13 ? 52  ASP A CB  1 
ATOM   402  C  CG  . ASP A 1 59  ? 28.935 -3.132  -11.439 1.00 73.96 ? 52  ASP A CG  1 
ATOM   403  O  OD1 . ASP A 1 59  ? 27.704 -3.325  -11.356 1.00 81.99 ? 52  ASP A OD1 1 
ATOM   404  O  OD2 . ASP A 1 59  ? 29.750 -4.032  -11.746 1.00 79.93 ? 52  ASP A OD2 1 
ATOM   405  N  N   . GLN A 1 60  ? 32.705 -1.127  -9.538  1.00 43.95 ? 53  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 60  ? 34.142 -1.267  -9.721  1.00 43.43 ? 53  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 60  ? 34.769 -1.533  -8.361  1.00 35.57 ? 53  GLN A C   1 
ATOM   408  O  O   . GLN A 1 60  ? 34.404 -0.899  -7.367  1.00 37.47 ? 53  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 60  ? 34.778 -0.017  -10.347 1.00 47.30 ? 53  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 60  ? 34.231 0.350   -11.741 1.00 52.38 ? 53  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 60  ? 34.623 -0.643  -12.836 1.00 65.46 ? 53  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 60  ? 33.790 -1.049  -13.652 1.00 68.65 ? 53  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 60  ? 35.898 -1.020  -12.868 1.00 71.31 ? 53  GLN A NE2 1 
ATOM   414  N  N   . TRP A 1 61  ? 35.714 -2.466  -8.322  1.00 32.63 ? 54  TRP A N   1 
ATOM   415  C  CA  . TRP A 1 61  ? 36.459 -2.705  -7.095  1.00 33.02 ? 54  TRP A CA  1 
ATOM   416  C  C   . TRP A 1 61  ? 37.471 -1.591  -6.867  1.00 31.84 ? 54  TRP A C   1 
ATOM   417  O  O   . TRP A 1 61  ? 38.217 -1.219  -7.780  1.00 35.81 ? 54  TRP A O   1 
ATOM   418  C  CB  . TRP A 1 61  ? 37.156 -4.062  -7.174  1.00 30.55 ? 54  TRP A CB  1 
ATOM   419  C  CG  . TRP A 1 61  ? 36.203 -5.206  -7.002  1.00 27.54 ? 54  TRP A CG  1 
ATOM   420  C  CD1 . TRP A 1 61  ? 35.543 -5.892  -7.978  1.00 29.41 ? 54  TRP A CD1 1 
ATOM   421  C  CD2 . TRP A 1 61  ? 35.808 -5.784  -5.761  1.00 25.52 ? 54  TRP A CD2 1 
ATOM   422  N  NE1 . TRP A 1 61  ? 34.749 -6.866  -7.413  1.00 28.61 ? 54  TRP A NE1 1 
ATOM   423  C  CE2 . TRP A 1 61  ? 34.908 -6.819  -6.049  1.00 26.30 ? 54  TRP A CE2 1 
ATOM   424  C  CE3 . TRP A 1 61  ? 36.131 -5.521  -4.432  1.00 26.48 ? 54  TRP A CE3 1 
ATOM   425  C  CZ2 . TRP A 1 61  ? 34.332 -7.597  -5.053  1.00 25.26 ? 54  TRP A CZ2 1 
ATOM   426  C  CZ3 . TRP A 1 61  ? 35.563 -6.296  -3.445  1.00 25.75 ? 54  TRP A CZ3 1 
ATOM   427  C  CH2 . TRP A 1 61  ? 34.668 -7.322  -3.763  1.00 23.45 ? 54  TRP A CH2 1 
ATOM   428  N  N   . ILE A 1 62  ? 37.473 -1.061  -5.635  1.00 28.00 ? 55  ILE A N   1 
ATOM   429  C  CA  . ILE A 1 62  ? 38.320 0.027   -5.154  1.00 31.72 ? 55  ILE A CA  1 
ATOM   430  C  C   . ILE A 1 62  ? 39.195 -0.528  -4.038  1.00 27.28 ? 55  ILE A C   1 
ATOM   431  O  O   . ILE A 1 62  ? 38.760 -1.393  -3.275  1.00 28.19 ? 55  ILE A O   1 
ATOM   432  C  CB  . ILE A 1 62  ? 37.442 1.198   -4.640  1.00 30.06 ? 55  ILE A CB  1 
ATOM   433  C  CG1 . ILE A 1 62  ? 36.650 1.851   -5.785  1.00 47.26 ? 55  ILE A CG1 1 
ATOM   434  C  CG2 . ILE A 1 62  ? 38.250 2.203   -3.850  1.00 48.72 ? 55  ILE A CG2 1 
ATOM   435  C  CD1 . ILE A 1 62  ? 37.275 1.765   -7.167  1.00 50.72 ? 55  ILE A CD1 1 
ATOM   436  N  N   . VAL A 1 63  ? 40.426 -0.028  -3.928  1.00 25.63 ? 56  VAL A N   1 
ATOM   437  C  CA  . VAL A 1 63  ? 41.343 -0.446  -2.868  1.00 22.51 ? 56  VAL A CA  1 
ATOM   438  C  C   . VAL A 1 63  ? 41.540 0.708   -1.893  1.00 22.57 ? 56  VAL A C   1 
ATOM   439  O  O   . VAL A 1 63  ? 41.568 1.875   -2.298  1.00 26.06 ? 56  VAL A O   1 
ATOM   440  C  CB  . VAL A 1 63  ? 42.693 -0.911  -3.447  1.00 30.26 ? 56  VAL A CB  1 
ATOM   441  C  CG1 . VAL A 1 63  ? 43.434 0.239   -4.037  1.00 36.32 ? 56  VAL A CG1 1 
ATOM   442  C  CG2 . VAL A 1 63  ? 43.543 -1.578  -2.376  1.00 32.71 ? 56  VAL A CG2 1 
ATOM   443  N  N   . HIS A 1 64  ? 41.657 0.376   -0.609  1.00 21.93 ? 57  HIS A N   1 
ATOM   444  C  CA  . HIS A 1 64  ? 41.951 1.348   0.441   1.00 26.29 ? 57  HIS A CA  1 
ATOM   445  C  C   . HIS A 1 64  ? 43.415 1.209   0.815   1.00 23.11 ? 57  HIS A C   1 
ATOM   446  O  O   . HIS A 1 64  ? 43.775 0.385   1.655   1.00 22.05 ? 57  HIS A O   1 
ATOM   447  C  CB  . HIS A 1 64  ? 41.051 1.124   1.647   1.00 23.80 ? 57  HIS A CB  1 
ATOM   448  C  CG  . HIS A 1 64  ? 39.603 1.289   1.333   1.00 25.11 ? 57  HIS A CG  1 
ATOM   449  N  ND1 . HIS A 1 64  ? 39.067 2.494   0.930   1.00 32.90 ? 57  HIS A ND1 1 
ATOM   450  C  CD2 . HIS A 1 64  ? 38.580 0.404   1.343   1.00 26.52 ? 57  HIS A CD2 1 
ATOM   451  C  CE1 . HIS A 1 64  ? 37.771 2.344   0.714   1.00 33.08 ? 57  HIS A CE1 1 
ATOM   452  N  NE2 . HIS A 1 64  ? 37.449 1.086   0.959   1.00 29.75 ? 57  HIS A NE2 1 
ATOM   453  N  N   . GLN A 1 65  ? 44.261 2.050   0.210   1.00 25.56 ? 58  GLN A N   1 
ATOM   454  C  CA  . GLN A 1 65  ? 45.688 1.913   0.457   1.00 24.60 ? 58  GLN A CA  1 
ATOM   455  C  C   . GLN A 1 65  ? 46.030 2.127   1.924   1.00 24.09 ? 58  GLN A C   1 
ATOM   456  O  O   . GLN A 1 65  ? 46.948 1.485   2.437   1.00 21.95 ? 58  GLN A O   1 
ATOM   457  C  CB  . GLN A 1 65  ? 46.478 2.888   -0.410  1.00 26.29 ? 58  GLN A CB  1 
ATOM   458  C  CG  . GLN A 1 65  ? 46.196 2.733   -1.884  1.00 28.97 ? 58  GLN A CG  1 
ATOM   459  C  CD  . GLN A 1 65  ? 47.200 3.454   -2.724  1.00 35.28 ? 58  GLN A CD  1 
ATOM   460  O  OE1 . GLN A 1 65  ? 48.321 3.717   -2.280  1.00 38.89 ? 58  GLN A OE1 1 
ATOM   461  N  NE2 . GLN A 1 65  ? 46.815 3.785   -3.946  1.00 37.30 ? 58  GLN A NE2 1 
ATOM   462  N  N   . TRP A 1 66  ? 45.313 3.016   2.621   1.00 22.66 ? 59  TRP A N   1 
ATOM   463  C  CA  . TRP A 1 66  ? 45.657 3.248   4.022   1.00 22.12 ? 59  TRP A CA  1 
ATOM   464  C  C   . TRP A 1 66  ? 45.473 1.997   4.862   1.00 22.01 ? 59  TRP A C   1 
ATOM   465  O  O   . TRP A 1 66  ? 46.208 1.787   5.834   1.00 20.47 ? 59  TRP A O   1 
ATOM   466  C  CB  . TRP A 1 66  ? 44.838 4.410   4.591   1.00 22.14 ? 59  TRP A CB  1 
ATOM   467  C  CG  . TRP A 1 66  ? 43.388 4.138   4.876   1.00 27.15 ? 59  TRP A CG  1 
ATOM   468  C  CD1 . TRP A 1 66  ? 42.325 4.337   4.027   1.00 28.40 ? 59  TRP A CD1 1 
ATOM   469  C  CD2 . TRP A 1 66  ? 42.829 3.677   6.114   1.00 26.61 ? 59  TRP A CD2 1 
ATOM   470  N  NE1 . TRP A 1 66  ? 41.148 4.005   4.658   1.00 28.80 ? 59  TRP A NE1 1 
ATOM   471  C  CE2 . TRP A 1 66  ? 41.429 3.613   5.945   1.00 26.34 ? 59  TRP A CE2 1 
ATOM   472  C  CE3 . TRP A 1 66  ? 43.378 3.318   7.355   1.00 24.54 ? 59  TRP A CE3 1 
ATOM   473  C  CZ2 . TRP A 1 66  ? 40.574 3.192   6.964   1.00 24.56 ? 59  TRP A CZ2 1 
ATOM   474  C  CZ3 . TRP A 1 66  ? 42.525 2.910   8.364   1.00 26.90 ? 59  TRP A CZ3 1 
ATOM   475  C  CH2 . TRP A 1 66  ? 41.138 2.856   8.162   1.00 26.48 ? 59  TRP A CH2 1 
ATOM   476  N  N   . ILE A 1 67  ? 44.530 1.127   4.490   1.00 18.10 ? 60  ILE A N   1 
ATOM   477  C  CA  . ILE A 1 67  ? 44.347 -0.105  5.245   1.00 17.87 ? 60  ILE A CA  1 
ATOM   478  C  C   . ILE A 1 67  ? 45.509 -1.054  5.018   1.00 20.21 ? 60  ILE A C   1 
ATOM   479  O  O   . ILE A 1 67  ? 45.970 -1.718  5.945   1.00 18.54 ? 60  ILE A O   1 
ATOM   480  C  CB  . ILE A 1 67  ? 42.986 -0.733  4.893   1.00 19.01 ? 60  ILE A CB  1 
ATOM   481  C  CG1 . ILE A 1 67  ? 41.882 0.233   5.323   1.00 21.12 ? 60  ILE A CG1 1 
ATOM   482  C  CG2 . ILE A 1 67  ? 42.824 -2.083  5.571   1.00 21.09 ? 60  ILE A CG2 1 
ATOM   483  C  CD1 . ILE A 1 67  ? 40.455 -0.214  4.926   1.00 25.00 ? 60  ILE A CD1 1 
ATOM   484  N  N   . LYS A 1 68  ? 46.000 -1.145  3.787   1.00 17.86 ? 61  LYS A N   1 
ATOM   485  C  CA  . LYS A 1 68  ? 47.207 -1.918  3.553   1.00 19.65 ? 61  LYS A CA  1 
ATOM   486  C  C   . LYS A 1 68  ? 48.382 -1.375  4.354   1.00 19.79 ? 61  LYS A C   1 
ATOM   487  O  O   . LYS A 1 68  ? 49.202 -2.147  4.857   1.00 18.79 ? 61  LYS A O   1 
ATOM   488  C  CB  . LYS A 1 68  ? 47.548 -1.899  2.076   1.00 20.09 ? 61  LYS A CB  1 
ATOM   489  C  CG  . LYS A 1 68  ? 46.563 -2.629  1.210   1.00 23.51 ? 61  LYS A CG  1 
ATOM   490  C  CD  . LYS A 1 68  ? 47.090 -2.525  -0.198  1.00 29.51 ? 61  LYS A CD  1 
ATOM   491  C  CE  . LYS A 1 68  ? 46.687 -3.616  -1.067  1.00 30.41 ? 61  LYS A CE  1 
ATOM   492  N  NZ  . LYS A 1 68  ? 47.381 -3.405  -2.361  1.00 24.04 ? 61  LYS A NZ  1 
ATOM   493  N  N   . LYS A 1 69  ? 48.506 -0.051  4.434   1.00 19.15 ? 62  LYS A N   1 
ATOM   494  C  CA  . LYS A 1 69  ? 49.570 0.534   5.241   1.00 17.86 ? 62  LYS A CA  1 
ATOM   495  C  C   . LYS A 1 69  ? 49.457 0.088   6.691   1.00 20.52 ? 62  LYS A C   1 
ATOM   496  O  O   . LYS A 1 69  ? 50.460 -0.238  7.327   1.00 18.74 ? 62  LYS A O   1 
ATOM   497  C  CB  . LYS A 1 69  ? 49.527 2.060   5.126   1.00 19.47 ? 62  LYS A CB  1 
ATOM   498  C  CG  . LYS A 1 69  ? 49.942 2.577   3.747   1.00 20.20 ? 62  LYS A CG  1 
ATOM   499  C  CD  . LYS A 1 69  ? 49.747 4.088   3.612   1.00 21.50 ? 62  LYS A CD  1 
ATOM   500  C  CE  . LYS A 1 69  ? 50.234 4.581   2.234   1.00 23.74 ? 62  LYS A CE  1 
ATOM   501  N  NZ  . LYS A 1 69  ? 49.980 6.016   2.017   1.00 28.86 ? 62  LYS A NZ  1 
ATOM   502  N  N   . ALA A 1 70  ? 48.239 0.039   7.224   1.00 17.41 ? 63  ALA A N   1 
ATOM   503  C  CA  . ALA A 1 70  ? 48.062 -0.407  8.606   1.00 18.17 ? 63  ALA A CA  1 
ATOM   504  C  C   . ALA A 1 70  ? 48.515 -1.846  8.771   1.00 17.13 ? 63  ALA A C   1 
ATOM   505  O  O   . ALA A 1 70  ? 49.128 -2.197  9.785   1.00 18.33 ? 63  ALA A O   1 
ATOM   506  C  CB  . ALA A 1 70  ? 46.598 -0.279  9.031   1.00 18.23 ? 63  ALA A CB  1 
ATOM   507  N  N   . VAL A 1 71  ? 48.146 -2.711  7.822   1.00 16.07 ? 64  VAL A N   1 
ATOM   508  C  CA  . VAL A 1 71  ? 48.553 -4.115  7.909   1.00 17.36 ? 64  VAL A CA  1 
ATOM   509  C  C   . VAL A 1 71  ? 50.066 -4.214  7.934   1.00 17.76 ? 64  VAL A C   1 
ATOM   510  O  O   . VAL A 1 71  ? 50.650 -4.899  8.782   1.00 18.40 ? 64  VAL A O   1 
ATOM   511  C  CB  . VAL A 1 71  ? 47.950 -4.923  6.750   1.00 16.57 ? 64  VAL A CB  1 
ATOM   512  C  CG1 . VAL A 1 71  ? 48.544 -6.334  6.698   1.00 19.07 ? 64  VAL A CG1 1 
ATOM   513  C  CG2 . VAL A 1 71  ? 46.425 -4.991  6.918   1.00 20.08 ? 64  VAL A CG2 1 
ATOM   514  N  N   . LEU A 1 72  ? 50.727 -3.482  7.033   1.00 18.36 ? 65  LEU A N   1 
ATOM   515  C  CA  . LEU A 1 72  ? 52.184 -3.510  6.980   1.00 17.59 ? 65  LEU A CA  1 
ATOM   516  C  C   . LEU A 1 72  ? 52.795 -2.944  8.257   1.00 20.97 ? 65  LEU A C   1 
ATOM   517  O  O   . LEU A 1 72  ? 53.796 -3.471  8.755   1.00 19.90 ? 65  LEU A O   1 
ATOM   518  C  CB  . LEU A 1 72  ? 52.663 -2.737  5.746   1.00 17.97 ? 65  LEU A CB  1 
ATOM   519  C  CG  . LEU A 1 72  ? 52.377 -3.478  4.451   1.00 18.94 ? 65  LEU A CG  1 
ATOM   520  C  CD1 . LEU A 1 72  ? 52.480 -2.570  3.249   1.00 25.52 ? 65  LEU A CD1 1 
ATOM   521  C  CD2 . LEU A 1 72  ? 53.322 -4.674  4.296   1.00 24.69 ? 65  LEU A CD2 1 
ATOM   522  N  N   . LEU A 1 73  ? 52.210 -1.875  8.813   1.00 18.37 ? 66  LEU A N   1 
ATOM   523  C  CA  . LEU A 1 73  ? 52.712 -1.358  10.081  1.00 16.88 ? 66  LEU A CA  1 
ATOM   524  C  C   . LEU A 1 73  ? 52.534 -2.351  11.213  1.00 16.63 ? 66  LEU A C   1 
ATOM   525  O  O   . LEU A 1 73  ? 53.361 -2.398  12.117  1.00 20.87 ? 66  LEU A O   1 
ATOM   526  C  CB  . LEU A 1 73  ? 52.014 -0.063  10.453  1.00 17.35 ? 66  LEU A CB  1 
ATOM   527  C  CG  . LEU A 1 73  ? 52.381 1.120   9.578   1.00 20.21 ? 66  LEU A CG  1 
ATOM   528  C  CD1 . LEU A 1 73  ? 51.407 2.266   9.791   1.00 21.41 ? 66  LEU A CD1 1 
ATOM   529  C  CD2 . LEU A 1 73  ? 53.840 1.524   9.878   1.00 24.02 ? 66  LEU A CD2 1 
ATOM   530  N  N   . SER A 1 74  ? 51.468 -3.160  11.178  1.00 17.96 ? 67  SER A N   1 
ATOM   531  C  CA  . SER A 1 74  ? 51.270 -4.120  12.259  1.00 19.05 ? 67  SER A CA  1 
ATOM   532  C  C   . SER A 1 74  ? 52.411 -5.129  12.318  1.00 18.77 ? 67  SER A C   1 
ATOM   533  O  O   . SER A 1 74  ? 52.764 -5.604  13.406  1.00 21.42 ? 67  SER A O   1 
ATOM   534  C  CB  . SER A 1 74  ? 49.912 -4.812  12.112  1.00 20.34 ? 67  SER A CB  1 
ATOM   535  O  OG  . SER A 1 74  ? 49.912 -5.848  11.134  1.00 20.98 ? 67  SER A OG  1 
ATOM   536  N  N   . PHE A 1 75  ? 53.009 -5.458  11.166  1.00 18.72 ? 68  PHE A N   1 
ATOM   537  C  CA  . PHE A 1 75  ? 54.207 -6.301  11.159  1.00 17.79 ? 68  PHE A CA  1 
ATOM   538  C  C   . PHE A 1 75  ? 55.389 -5.574  11.792  1.00 20.30 ? 68  PHE A C   1 
ATOM   539  O  O   . PHE A 1 75  ? 56.119 -6.132  12.615  1.00 25.01 ? 68  PHE A O   1 
ATOM   540  C  CB  . PHE A 1 75  ? 54.578 -6.703  9.730   1.00 20.50 ? 68  PHE A CB  1 
ATOM   541  C  CG  . PHE A 1 75  ? 53.478 -7.399  8.956   1.00 21.99 ? 68  PHE A CG  1 
ATOM   542  C  CD1 . PHE A 1 75  ? 52.429 -8.000  9.596   1.00 22.82 ? 68  PHE A CD1 1 
ATOM   543  C  CD2 . PHE A 1 75  ? 53.508 -7.426  7.571   1.00 29.26 ? 68  PHE A CD2 1 
ATOM   544  C  CE1 . PHE A 1 75  ? 51.437 -8.632  8.883   1.00 26.43 ? 68  PHE A CE1 1 
ATOM   545  C  CE2 . PHE A 1 75  ? 52.514 -8.056  6.852   1.00 31.41 ? 68  PHE A CE2 1 
ATOM   546  C  CZ  . PHE A 1 75  ? 51.479 -8.662  7.519   1.00 29.81 ? 68  PHE A CZ  1 
ATOM   547  N  N   . ARG A 1 76  ? 55.585 -4.314  11.416  1.00 19.85 ? 69  ARG A N   1 
ATOM   548  C  CA  . ARG A 1 76  ? 56.728 -3.553  11.895  1.00 21.35 ? 69  ARG A CA  1 
ATOM   549  C  C   . ARG A 1 76  ? 56.685 -3.308  13.393  1.00 23.70 ? 69  ARG A C   1 
ATOM   550  O  O   . ARG A 1 76  ? 57.739 -3.206  14.030  1.00 24.15 ? 69  ARG A O   1 
ATOM   551  C  CB  . ARG A 1 76  ? 56.777 -2.219  11.147  1.00 25.66 ? 69  ARG A CB  1 
ATOM   552  C  CG  . ARG A 1 76  ? 58.016 -1.394  11.437  1.00 34.77 ? 69  ARG A CG  1 
ATOM   553  C  CD  . ARG A 1 76  ? 58.089 -0.153  10.551  1.00 38.30 ? 69  ARG A CD  1 
ATOM   554  N  NE  . ARG A 1 76  ? 58.163 -0.467  9.128   1.00 34.21 ? 69  ARG A NE  1 
ATOM   555  C  CZ  . ARG A 1 76  ? 59.251 -0.344  8.377   1.00 36.71 ? 69  ARG A CZ  1 
ATOM   556  N  NH1 . ARG A 1 76  ? 60.411 0.008   8.892   1.00 39.07 ? 69  ARG A NH1 1 
ATOM   557  N  NH2 . ARG A 1 76  ? 59.169 -0.582  7.071   1.00 45.70 ? 69  ARG A NH2 1 
ATOM   558  N  N   . LEU A 1 77  ? 55.491 -3.203  13.966  1.00 27.17 ? 70  LEU A N   1 
ATOM   559  C  CA  . LEU A 1 77  ? 55.300 -2.829  15.357  1.00 29.86 ? 70  LEU A CA  1 
ATOM   560  C  C   . LEU A 1 77  ? 55.341 -4.004  16.326  1.00 27.87 ? 70  LEU A C   1 
ATOM   561  O  O   . LEU A 1 77  ? 55.268 -3.777  17.541  1.00 29.05 ? 70  LEU A O   1 
ATOM   562  C  CB  . LEU A 1 77  ? 53.943 -2.134  15.526  1.00 29.14 ? 70  LEU A CB  1 
ATOM   563  C  CG  . LEU A 1 77  ? 53.769 -0.793  14.825  1.00 32.40 ? 70  LEU A CG  1 
ATOM   564  C  CD1 . LEU A 1 77  ? 52.421 -0.202  15.185  1.00 38.82 ? 70  LEU A CD1 1 
ATOM   565  C  CD2 . LEU A 1 77  ? 54.866 0.168   15.165  1.00 37.78 ? 70  LEU A CD2 1 
ATOM   566  N  N   . HIS A 1 78  ? 55.406 -5.233  15.842  1.00 24.48 ? 71  HIS A N   1 
ATOM   567  C  CA  . HIS A 1 78  ? 55.430 -6.381  16.733  1.00 23.79 ? 71  HIS A CA  1 
ATOM   568  C  C   . HIS A 1 78  ? 56.669 -7.225  16.538  1.00 29.32 ? 71  HIS A C   1 
ATOM   569  O  O   . HIS A 1 78  ? 57.129 -7.438  15.413  1.00 24.61 ? 71  HIS A O   1 
ATOM   570  C  CB  . HIS A 1 78  ? 54.200 -7.256  16.561  1.00 28.34 ? 71  HIS A CB  1 
ATOM   571  C  CG  . HIS A 1 78  ? 52.946 -6.565  16.976  1.00 40.51 ? 71  HIS A CG  1 
ATOM   572  N  ND1 . HIS A 1 78  ? 52.027 -6.091  16.068  1.00 37.52 ? 71  HIS A ND1 1 
ATOM   573  C  CD2 . HIS A 1 78  ? 52.499 -6.187  18.199  1.00 45.82 ? 71  HIS A CD2 1 
ATOM   574  C  CE1 . HIS A 1 78  ? 51.044 -5.488  16.715  1.00 49.09 ? 71  HIS A CE1 1 
ATOM   575  N  NE2 . HIS A 1 78  ? 51.309 -5.528  18.008  1.00 44.27 ? 71  HIS A NE2 1 
ATOM   576  N  N   . ASP A 1 79  ? 57.185 -7.696  17.666  1.00 24.62 ? 72  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 79  ? 58.255 -8.662  17.692  1.00 22.77 ? 72  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 79  ? 57.688 -10.046 17.445  1.00 22.76 ? 72  ASP A C   1 
ATOM   579  O  O   . ASP A 1 79  ? 56.502 -10.307 17.673  1.00 21.66 ? 72  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 79  ? 58.954 -8.657  19.053  1.00 25.76 ? 72  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 79  ? 60.015 -7.582  19.179  1.00 44.59 ? 72  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 79  ? 60.801 -7.372  18.223  1.00 42.77 ? 72  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 79  ? 60.079 -6.971  20.262  1.00 44.67 ? 72  ASP A OD2 1 
ATOM   584  N  N   . ASN A 1 80  ? 58.546 -10.932 16.965  1.00 21.67 ? 73  ASN A N   1 
ATOM   585  C  CA  . ASN A 1 80  ? 58.209 -12.349 16.966  1.00 19.48 ? 73  ASN A CA  1 
ATOM   586  C  C   . ASN A 1 80  ? 58.094 -12.881 18.388  1.00 22.77 ? 73  ASN A C   1 
ATOM   587  O  O   . ASN A 1 80  ? 58.780 -12.429 19.309  1.00 24.58 ? 73  ASN A O   1 
ATOM   588  C  CB  . ASN A 1 80  ? 59.256 -13.142 16.199  1.00 18.71 ? 73  ASN A CB  1 
ATOM   589  C  CG  . ASN A 1 80  ? 59.276 -12.783 14.740  1.00 18.56 ? 73  ASN A CG  1 
ATOM   590  O  OD1 . ASN A 1 80  ? 58.258 -12.861 14.061  1.00 20.59 ? 73  ASN A OD1 1 
ATOM   591  N  ND2 . ASN A 1 80  ? 60.440 -12.368 14.247  1.00 25.89 ? 73  ASN A ND2 1 
ATOM   592  N  N   . ALA A 1 81  ? 57.212 -13.863 18.561  1.00 20.42 ? 74  ALA A N   1 
ATOM   593  C  CA  . ALA A 1 81  ? 56.959 -14.450 19.869  1.00 24.92 ? 74  ALA A CA  1 
ATOM   594  C  C   . ALA A 1 81  ? 56.793 -15.952 19.703  1.00 19.12 ? 74  ALA A C   1 
ATOM   595  O  O   . ALA A 1 81  ? 56.278 -16.415 18.686  1.00 20.00 ? 74  ALA A O   1 
ATOM   596  C  CB  . ALA A 1 81  ? 55.700 -13.865 20.520  1.00 32.62 ? 74  ALA A CB  1 
ATOM   597  N  N   . VAL A 1 82  ? 57.245 -16.699 20.708  1.00 21.27 ? 75  VAL A N   1 
ATOM   598  C  CA  . VAL A 1 82  ? 57.039 -18.144 20.711  1.00 20.00 ? 75  VAL A CA  1 
ATOM   599  C  C   . VAL A 1 82  ? 55.552 -18.430 20.861  1.00 28.22 ? 75  VAL A C   1 
ATOM   600  O  O   . VAL A 1 82  ? 54.852 -17.812 21.677  1.00 26.69 ? 75  VAL A O   1 
ATOM   601  C  CB  . VAL A 1 82  ? 57.850 -18.812 21.829  1.00 28.14 ? 75  VAL A CB  1 
ATOM   602  C  CG1 . VAL A 1 82  ? 57.684 -20.329 21.787  1.00 30.97 ? 75  VAL A CG1 1 
ATOM   603  C  CG2 . VAL A 1 82  ? 59.310 -18.458 21.698  1.00 29.97 ? 75  VAL A CG2 1 
ATOM   604  N  N   . MET A 1 83  ? 55.059 -19.372 20.070  1.00 22.05 ? 76  MET A N   1 
ATOM   605  C  CA  . MET A 1 83  ? 53.653 -19.757 20.080  1.00 22.76 ? 76  MET A CA  1 
ATOM   606  C  C   . MET A 1 83  ? 53.599 -21.280 20.112  1.00 28.10 ? 76  MET A C   1 
ATOM   607  O  O   . MET A 1 83  ? 54.483 -21.951 19.578  1.00 22.97 ? 76  MET A O   1 
ATOM   608  C  CB  . MET A 1 83  ? 52.913 -19.209 18.842  1.00 31.45 ? 76  MET A CB  1 
ATOM   609  C  CG  . MET A 1 83  ? 53.310 -17.778 18.438  1.00 31.97 ? 76  MET A CG  1 
ATOM   610  S  SD  . MET A 1 83  ? 52.597 -17.223 16.858  1.00 42.22 ? 76  MET A SD  1 
ATOM   611  C  CE  . MET A 1 83  ? 50.877 -17.285 17.263  1.00 37.21 ? 76  MET A CE  1 
ATOM   612  N  N   . GLY A 1 84  ? 52.584 -21.820 20.772  1.00 33.07 ? 77  GLY A N   1 
ATOM   613  C  CA  . GLY A 1 84  ? 52.357 -23.252 20.732  1.00 28.64 ? 77  GLY A CA  1 
ATOM   614  C  C   . GLY A 1 84  ? 53.163 -23.990 21.778  1.00 40.68 ? 77  GLY A C   1 
ATOM   615  O  O   . GLY A 1 84  ? 53.646 -23.414 22.752  1.00 42.72 ? 77  GLY A O   1 
ATOM   616  N  N   . GLN A 1 85  ? 53.339 -25.291 21.544  1.00 45.88 ? 78  GLN A N   1 
ATOM   617  C  CA  . GLN A 1 85  ? 54.008 -26.164 22.500  1.00 45.71 ? 78  GLN A CA  1 
ATOM   618  C  C   . GLN A 1 85  ? 54.201 -27.541 21.872  1.00 43.78 ? 78  GLN A C   1 
ATOM   619  O  O   . GLN A 1 85  ? 53.707 -27.825 20.778  1.00 43.08 ? 78  GLN A O   1 
ATOM   620  C  CB  . GLN A 1 85  ? 53.192 -26.283 23.786  1.00 59.25 ? 78  GLN A CB  1 
ATOM   621  C  CG  . GLN A 1 85  ? 51.783 -26.745 23.505  1.00 57.09 ? 78  GLN A CG  1 
ATOM   622  C  CD  . GLN A 1 85  ? 51.016 -27.031 24.764  1.00 81.71 ? 78  GLN A CD  1 
ATOM   623  O  OE1 . GLN A 1 85  ? 50.658 -26.118 25.506  1.00 95.16 ? 78  GLN A OE1 1 
ATOM   624  N  NE2 . GLN A 1 85  ? 50.764 -28.306 25.023  1.00 90.89 ? 78  GLN A NE2 1 
ATOM   625  N  N   . GLY A 1 86  ? 54.883 -28.409 22.598  1.00 46.23 ? 79  GLY A N   1 
ATOM   626  C  CA  . GLY A 1 86  ? 55.124 -29.752 22.134  1.00 48.97 ? 79  GLY A CA  1 
ATOM   627  C  C   . GLY A 1 86  ? 55.766 -29.757 20.768  1.00 40.02 ? 79  GLY A C   1 
ATOM   628  O  O   . GLY A 1 86  ? 56.584 -28.897 20.423  1.00 41.52 ? 79  GLY A O   1 
ATOM   629  N  N   . PRO A 1 87  ? 55.406 -30.745 19.936  1.00 53.58 ? 80  PRO A N   1 
ATOM   630  C  CA  . PRO A 1 87  ? 56.004 -30.845 18.606  1.00 53.76 ? 80  PRO A CA  1 
ATOM   631  C  C   . PRO A 1 87  ? 55.488 -29.818 17.615  1.00 57.00 ? 80  PRO A C   1 
ATOM   632  O  O   . PRO A 1 87  ? 55.719 -29.972 16.412  1.00 54.85 ? 80  PRO A O   1 
ATOM   633  C  CB  . PRO A 1 87  ? 55.623 -32.274 18.181  1.00 58.76 ? 80  PRO A CB  1 
ATOM   634  C  CG  . PRO A 1 87  ? 54.334 -32.513 18.872  1.00 55.46 ? 80  PRO A CG  1 
ATOM   635  C  CD  . PRO A 1 87  ? 54.470 -31.849 20.219  1.00 43.41 ? 80  PRO A CD  1 
ATOM   636  N  N   . LEU A 1 88  ? 54.788 -28.802 18.091  1.00 39.33 ? 81  LEU A N   1 
ATOM   637  C  CA  . LEU A 1 88  ? 54.247 -27.801 17.237  1.00 32.23 ? 81  LEU A CA  1 
ATOM   638  C  C   . LEU A 1 88  ? 54.547 -26.442 17.888  1.00 31.50 ? 81  LEU A C   1 
ATOM   639  O  O   . LEU A 1 88  ? 53.635 -25.755 18.345  1.00 38.30 ? 81  LEU A O   1 
ATOM   640  C  CB  . LEU A 1 88  ? 52.750 -27.977 17.022  1.00 40.01 ? 81  LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 88  ? 52.273 -29.292 16.410  1.00 46.52 ? 81  LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 88  ? 50.755 -29.324 16.436  1.00 47.81 ? 81  LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 88  ? 52.780 -29.438 15.015  1.00 42.56 ? 81  LEU A CD2 1 
ATOM   644  N  N   . GLN A 1 89  ? 55.834 -26.096 17.967  1.00 32.96 ? 82  GLN A N   1 
ATOM   645  C  CA  . GLN A 1 89  ? 56.249 -24.773 18.386  1.00 23.87 ? 82  GLN A CA  1 
ATOM   646  C  C   . GLN A 1 89  ? 56.463 -23.891 17.155  1.00 21.21 ? 82  GLN A C   1 
ATOM   647  O  O   . GLN A 1 89  ? 57.054 -24.336 16.151  1.00 20.95 ? 82  GLN A O   1 
ATOM   648  C  CB  . GLN A 1 89  ? 57.551 -24.790 19.187  1.00 32.37 ? 82  GLN A CB  1 
ATOM   649  C  CG  . GLN A 1 89  ? 57.486 -25.456 20.524  1.00 46.09 ? 82  GLN A CG  1 
ATOM   650  C  CD  . GLN A 1 89  ? 57.407 -24.462 21.648  1.00 43.35 ? 82  GLN A CD  1 
ATOM   651  O  OE1 . GLN A 1 89  ? 58.425 -24.032 22.183  1.00 58.54 ? 82  GLN A OE1 1 
ATOM   652  N  NE2 . GLN A 1 89  ? 56.199 -24.077 22.011  1.00 50.42 ? 82  GLN A NE2 1 
ATOM   653  N  N   . PHE A 1 90  ? 56.039 -22.637 17.273  1.00 19.35 ? 83  PHE A N   1 
ATOM   654  C  CA  . PHE A 1 90  ? 56.149 -21.641 16.217  1.00 19.72 ? 83  PHE A CA  1 
ATOM   655  C  C   . PHE A 1 90  ? 56.744 -20.359 16.776  1.00 20.56 ? 83  PHE A C   1 
ATOM   656  O  O   . PHE A 1 90  ? 56.892 -20.191 17.986  1.00 17.71 ? 83  PHE A O   1 
ATOM   657  C  CB  . PHE A 1 90  ? 54.774 -21.378 15.597  1.00 17.46 ? 83  PHE A CB  1 
ATOM   658  C  CG  . PHE A 1 90  ? 53.956 -22.634 15.415  1.00 19.22 ? 83  PHE A CG  1 
ATOM   659  C  CD1 . PHE A 1 90  ? 54.181 -23.486 14.348  1.00 19.17 ? 83  PHE A CD1 1 
ATOM   660  C  CD2 . PHE A 1 90  ? 52.974 -22.966 16.333  1.00 22.48 ? 83  PHE A CD2 1 
ATOM   661  C  CE1 . PHE A 1 90  ? 53.446 -24.631 14.175  1.00 21.08 ? 83  PHE A CE1 1 
ATOM   662  C  CE2 . PHE A 1 90  ? 52.229 -24.120 16.180  1.00 27.64 ? 83  PHE A CE2 1 
ATOM   663  C  CZ  . PHE A 1 90  ? 52.468 -24.963 15.096  1.00 31.12 ? 83  PHE A CZ  1 
ATOM   664  N  N   . TYR A 1 91  ? 57.036 -19.418 15.873  1.00 16.56 ? 84  TYR A N   1 
ATOM   665  C  CA  . TYR A 1 91  ? 57.743 -18.193 16.259  1.00 15.56 ? 84  TYR A CA  1 
ATOM   666  C  C   . TYR A 1 91  ? 57.368 -17.148 15.213  1.00 15.79 ? 84  TYR A C   1 
ATOM   667  O  O   . TYR A 1 91  ? 57.887 -17.182 14.099  1.00 16.70 ? 84  TYR A O   1 
ATOM   668  C  CB  . TYR A 1 91  ? 59.232 -18.425 16.303  1.00 18.02 ? 84  TYR A CB  1 
ATOM   669  C  CG  . TYR A 1 91  ? 60.041 -17.260 16.809  1.00 16.40 ? 84  TYR A CG  1 
ATOM   670  C  CD1 . TYR A 1 91  ? 59.910 -16.841 18.112  1.00 18.24 ? 84  TYR A CD1 1 
ATOM   671  C  CD2 . TYR A 1 91  ? 60.967 -16.634 15.994  1.00 17.43 ? 84  TYR A CD2 1 
ATOM   672  C  CE1 . TYR A 1 91  ? 60.677 -15.781 18.614  1.00 20.22 ? 84  TYR A CE1 1 
ATOM   673  C  CE2 . TYR A 1 91  ? 61.765 -15.579 16.499  1.00 19.85 ? 84  TYR A CE2 1 
ATOM   674  C  CZ  . TYR A 1 91  ? 61.597 -15.166 17.784  1.00 23.60 ? 84  TYR A CZ  1 
ATOM   675  O  OH  . TYR A 1 91  ? 62.360 -14.119 18.284  1.00 26.82 ? 84  TYR A OH  1 
ATOM   676  N  N   . ASP A 1 92  ? 56.433 -16.276 15.562  1.00 15.80 ? 85  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? 55.921 -15.349 14.565  1.00 17.51 ? 85  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? 55.374 -14.120 15.272  1.00 18.90 ? 85  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? 55.211 -14.098 16.492  1.00 19.74 ? 85  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 54.849 -16.006 13.696  1.00 18.56 ? 85  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 54.487 -15.182 12.471  1.00 19.14 ? 85  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 55.361 -14.443 11.942  1.00 20.58 ? 85  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 53.322 -15.303 12.011  1.00 20.13 ? 85  ASP A OD2 1 
ATOM   684  N  N   . LYS A 1 93  ? 55.102 -13.089 14.475  1.00 18.04 ? 86  LYS A N   1 
ATOM   685  C  CA  . LYS A 1 93  ? 54.713 -11.789 14.992  1.00 17.73 ? 86  LYS A CA  1 
ATOM   686  C  C   . LYS A 1 93  ? 53.264 -11.434 14.701  1.00 19.67 ? 86  LYS A C   1 
ATOM   687  O  O   . LYS A 1 93  ? 52.820 -10.352 15.105  1.00 20.49 ? 86  LYS A O   1 
ATOM   688  C  CB  . LYS A 1 93  ? 55.626 -10.697 14.417  1.00 20.50 ? 86  LYS A CB  1 
ATOM   689  C  CG  . LYS A 1 93  ? 55.650 -10.621 12.899  1.00 20.15 ? 86  LYS A CG  1 
ATOM   690  C  CD  . LYS A 1 93  ? 56.435 -9.426  12.362  1.00 23.72 ? 86  LYS A CD  1 
ATOM   691  C  CE  . LYS A 1 93  ? 57.873 -9.411  12.833  1.00 27.73 ? 86  LYS A CE  1 
ATOM   692  N  NZ  . LYS A 1 93  ? 58.488 -8.073  12.563  1.00 35.31 ? 86  LYS A NZ  1 
ATOM   693  N  N   . VAL A 1 94  ? 52.520 -12.306 14.039  1.00 17.75 ? 87  VAL A N   1 
ATOM   694  C  CA  . VAL A 1 94  ? 51.112 -12.083 13.730  1.00 17.70 ? 87  VAL A CA  1 
ATOM   695  C  C   . VAL A 1 94  ? 50.294 -13.064 14.556  1.00 17.87 ? 87  VAL A C   1 
ATOM   696  O  O   . VAL A 1 94  ? 50.448 -14.288 14.393  1.00 19.30 ? 87  VAL A O   1 
ATOM   697  C  CB  . VAL A 1 94  ? 50.814 -12.261 12.234  1.00 18.63 ? 87  VAL A CB  1 
ATOM   698  C  CG1 . VAL A 1 94  ? 49.365 -11.862 11.970  1.00 21.95 ? 87  VAL A CG1 1 
ATOM   699  C  CG2 . VAL A 1 94  ? 51.755 -11.472 11.389  1.00 20.14 ? 87  VAL A CG2 1 
ATOM   700  N  N   . PRO A 1 95  ? 49.403 -12.591 15.415  1.00 17.89 ? 88  PRO A N   1 
ATOM   701  C  CA  . PRO A 1 95  ? 48.565 -13.510 16.185  1.00 17.69 ? 88  PRO A CA  1 
ATOM   702  C  C   . PRO A 1 95  ? 47.620 -14.267 15.274  1.00 18.94 ? 88  PRO A C   1 
ATOM   703  O  O   . PRO A 1 95  ? 47.217 -13.784 14.207  1.00 19.65 ? 88  PRO A O   1 
ATOM   704  C  CB  . PRO A 1 95  ? 47.794 -12.586 17.134  1.00 23.18 ? 88  PRO A CB  1 
ATOM   705  C  CG  . PRO A 1 95  ? 48.562 -11.302 17.145  1.00 31.56 ? 88  PRO A CG  1 
ATOM   706  C  CD  . PRO A 1 95  ? 49.169 -11.182 15.795  1.00 24.24 ? 88  PRO A CD  1 
ATOM   707  N  N   . THR A 1 96  ? 47.297 -15.488 15.684  1.00 18.74 ? 89  THR A N   1 
ATOM   708  C  CA  . THR A 1 96  ? 46.256 -16.221 14.971  1.00 18.60 ? 89  THR A CA  1 
ATOM   709  C  C   . THR A 1 96  ? 44.877 -15.717 15.401  1.00 18.23 ? 89  THR A C   1 
ATOM   710  O  O   . THR A 1 96  ? 44.695 -15.103 16.460  1.00 19.69 ? 89  THR A O   1 
ATOM   711  C  CB  . THR A 1 96  ? 46.380 -17.722 15.203  1.00 21.49 ? 89  THR A CB  1 
ATOM   712  O  OG1 . THR A 1 96  ? 46.172 -18.003 16.586  1.00 23.16 ? 89  THR A OG1 1 
ATOM   713  C  CG2 . THR A 1 96  ? 47.784 -18.201 14.771  1.00 21.76 ? 89  THR A CG2 1 
ATOM   714  N  N   . LYS A 1 97  ? 43.888 -15.995 14.551  1.00 19.55 ? 90  LYS A N   1 
ATOM   715  C  CA  . LYS A 1 97  ? 42.602 -15.325 14.696  1.00 19.30 ? 90  LYS A CA  1 
ATOM   716  C  C   . LYS A 1 97  ? 41.858 -15.788 15.935  1.00 22.72 ? 90  LYS A C   1 
ATOM   717  O  O   . LYS A 1 97  ? 41.161 -14.993 16.581  1.00 20.69 ? 90  LYS A O   1 
ATOM   718  C  CB  . LYS A 1 97  ? 41.748 -15.577 13.461  1.00 18.19 ? 90  LYS A CB  1 
ATOM   719  C  CG  . LYS A 1 97  ? 40.403 -14.835 13.434  1.00 19.63 ? 90  LYS A CG  1 
ATOM   720  C  CD  . LYS A 1 97  ? 39.720 -15.012 12.073  1.00 21.58 ? 90  LYS A CD  1 
ATOM   721  C  CE  . LYS A 1 97  ? 38.262 -14.556 12.118  1.00 25.18 ? 90  LYS A CE  1 
ATOM   722  N  NZ  . LYS A 1 97  ? 38.086 -13.086 12.363  1.00 23.71 ? 90  LYS A NZ  1 
ATOM   723  N  N   . PHE A 1 98  ? 41.960 -17.075 16.252  1.00 21.72 ? 91  PHE A N   1 
ATOM   724  C  CA  . PHE A 1 98  ? 41.088 -17.714 17.233  1.00 25.33 ? 91  PHE A CA  1 
ATOM   725  C  C   . PHE A 1 98  ? 41.760 -17.898 18.584  1.00 31.29 ? 91  PHE A C   1 
ATOM   726  O  O   . PHE A 1 98  ? 41.189 -18.544 19.467  1.00 29.60 ? 91  PHE A O   1 
ATOM   727  C  CB  . PHE A 1 98  ? 40.611 -19.069 16.706  1.00 26.85 ? 91  PHE A CB  1 
ATOM   728  C  CG  . PHE A 1 98  ? 40.178 -19.038 15.279  1.00 22.16 ? 91  PHE A CG  1 
ATOM   729  C  CD1 . PHE A 1 98  ? 39.089 -18.250 14.892  1.00 22.57 ? 91  PHE A CD1 1 
ATOM   730  C  CD2 . PHE A 1 98  ? 40.841 -19.787 14.325  1.00 22.84 ? 91  PHE A CD2 1 
ATOM   731  C  CE1 . PHE A 1 98  ? 38.708 -18.228 13.565  1.00 22.83 ? 91  PHE A CE1 1 
ATOM   732  C  CE2 . PHE A 1 98  ? 40.468 -19.756 13.011  1.00 26.63 ? 91  PHE A CE2 1 
ATOM   733  C  CZ  . PHE A 1 98  ? 39.393 -18.980 12.626  1.00 24.56 ? 91  PHE A CZ  1 
ATOM   734  N  N   . ALA A 1 99  ? 42.945 -17.329 18.775  1.00 33.05 ? 92  ALA A N   1 
ATOM   735  C  CA  . ALA A 1 99  ? 43.623 -17.440 20.062  1.00 37.25 ? 92  ALA A CA  1 
ATOM   736  C  C   . ALA A 1 99  ? 42.739 -16.905 21.182  1.00 35.32 ? 92  ALA A C   1 
ATOM   737  O  O   . ALA A 1 99  ? 42.270 -15.765 21.142  1.00 34.84 ? 92  ALA A O   1 
ATOM   738  C  CB  . ALA A 1 99  ? 44.949 -16.676 20.019  1.00 35.24 ? 92  ALA A CB  1 
ATOM   739  N  N   . GLY A 1 100 ? 42.517 -17.736 22.202  1.00 42.48 ? 93  GLY A N   1 
ATOM   740  C  CA  . GLY A 1 100 ? 41.724 -17.323 23.346  1.00 40.87 ? 93  GLY A CA  1 
ATOM   741  C  C   . GLY A 1 100 ? 40.226 -17.409 23.155  1.00 40.08 ? 93  GLY A C   1 
ATOM   742  O  O   . GLY A 1 100 ? 39.478 -17.144 24.106  1.00 40.20 ? 93  GLY A O   1 
ATOM   743  N  N   . TYR A 1 101 ? 39.763 -17.755 21.959  1.00 31.92 ? 94  TYR A N   1 
ATOM   744  C  CA  . TYR A 1 101 ? 38.345 -17.995 21.755  1.00 32.01 ? 94  TYR A CA  1 
ATOM   745  C  C   . TYR A 1 101 ? 37.862 -19.164 22.599  1.00 35.61 ? 94  TYR A C   1 
ATOM   746  O  O   . TYR A 1 101 ? 38.555 -20.176 22.740  1.00 38.88 ? 94  TYR A O   1 
ATOM   747  C  CB  . TYR A 1 101 ? 38.066 -18.328 20.299  1.00 27.18 ? 94  TYR A CB  1 
ATOM   748  C  CG  . TYR A 1 101 ? 37.890 -17.162 19.372  1.00 28.02 ? 94  TYR A CG  1 
ATOM   749  C  CD1 . TYR A 1 101 ? 38.503 -15.932 19.610  1.00 31.75 ? 94  TYR A CD1 1 
ATOM   750  C  CD2 . TYR A 1 101 ? 37.097 -17.292 18.248  1.00 28.99 ? 94  TYR A CD2 1 
ATOM   751  C  CE1 . TYR A 1 101 ? 38.323 -14.873 18.717  1.00 30.25 ? 94  TYR A CE1 1 
ATOM   752  C  CE2 . TYR A 1 101 ? 36.918 -16.261 17.369  1.00 33.19 ? 94  TYR A CE2 1 
ATOM   753  C  CZ  . TYR A 1 101 ? 37.523 -15.052 17.607  1.00 29.66 ? 94  TYR A CZ  1 
ATOM   754  O  OH  . TYR A 1 101 ? 37.287 -14.052 16.692  1.00 37.58 ? 94  TYR A OH  1 
ATOM   755  N  N   . GLY A 1 102 ? 36.646 -19.039 23.114  1.00 33.26 ? 95  GLY A N   1 
ATOM   756  C  CA  . GLY A 1 102 ? 35.936 -20.172 23.654  1.00 36.46 ? 95  GLY A CA  1 
ATOM   757  C  C   . GLY A 1 102 ? 34.665 -20.434 22.877  1.00 37.56 ? 95  GLY A C   1 
ATOM   758  O  O   . GLY A 1 102 ? 34.481 -19.913 21.772  1.00 35.64 ? 95  GLY A O   1 
ATOM   759  N  N   . GLU A 1 103 ? 33.779 -21.248 23.455  1.00 29.63 ? 96  GLU A N   1 
ATOM   760  C  CA  . GLU A 1 103 ? 32.544 -21.602 22.774  1.00 28.44 ? 96  GLU A CA  1 
ATOM   761  C  C   . GLU A 1 103 ? 31.751 -20.363 22.390  1.00 28.14 ? 96  GLU A C   1 
ATOM   762  O  O   . GLU A 1 103 ? 31.226 -20.274 21.277  1.00 30.73 ? 96  GLU A O   1 
ATOM   763  C  CB  . GLU A 1 103 ? 31.684 -22.508 23.670  1.00 38.10 ? 96  GLU A CB  1 
ATOM   764  C  CG  . GLU A 1 103 ? 30.684 -23.348 22.879  1.00 48.98 ? 96  GLU A CG  1 
ATOM   765  C  CD  . GLU A 1 103 ? 29.561 -23.896 23.737  1.00 62.19 ? 96  GLU A CD  1 
ATOM   766  O  OE1 . GLU A 1 103 ? 29.666 -23.814 24.979  1.00 67.22 ? 96  GLU A OE1 1 
ATOM   767  O  OE2 . GLU A 1 103 ? 28.570 -24.397 23.164  1.00 65.98 ? 96  GLU A OE2 1 
ATOM   768  N  N   . ALA A 1 104 ? 31.646 -19.395 23.303  1.00 27.64 ? 97  ALA A N   1 
ATOM   769  C  CA  . ALA A 1 104 ? 30.810 -18.225 23.047  1.00 30.84 ? 97  ALA A CA  1 
ATOM   770  C  C   . ALA A 1 104 ? 31.278 -17.484 21.803  1.00 30.99 ? 97  ALA A C   1 
ATOM   771  O  O   . ALA A 1 104 ? 30.474 -17.134 20.933  1.00 30.14 ? 97  ALA A O   1 
ATOM   772  C  CB  . ALA A 1 104 ? 30.820 -17.296 24.260  1.00 36.16 ? 97  ALA A CB  1 
ATOM   773  N  N   . ALA A 1 105 ? 32.588 -17.261 21.691  1.00 28.16 ? 98  ALA A N   1 
ATOM   774  C  CA  . ALA A 1 105 ? 33.130 -16.522 20.559  1.00 27.41 ? 98  ALA A CA  1 
ATOM   775  C  C   . ALA A 1 105 ? 32.950 -17.287 19.251  1.00 26.80 ? 98  ALA A C   1 
ATOM   776  O  O   . ALA A 1 105 ? 32.615 -16.698 18.213  1.00 26.27 ? 98  ALA A O   1 
ATOM   777  C  CB  . ALA A 1 105 ? 34.606 -16.215 20.812  1.00 28.40 ? 98  ALA A CB  1 
ATOM   778  N  N   . PHE A 1 106 ? 33.186 -18.593 19.268  1.00 22.94 ? 99  PHE A N   1 
ATOM   779  C  CA  . PHE A 1 106 ? 33.010 -19.360 18.041  1.00 25.33 ? 99  PHE A CA  1 
ATOM   780  C  C   . PHE A 1 106 ? 31.541 -19.408 17.631  1.00 24.38 ? 99  PHE A C   1 
ATOM   781  O  O   . PHE A 1 106 ? 31.210 -19.289 16.439  1.00 24.08 ? 99  PHE A O   1 
ATOM   782  C  CB  . PHE A 1 106 ? 33.567 -20.771 18.234  1.00 21.65 ? 99  PHE A CB  1 
ATOM   783  C  CG  . PHE A 1 106 ? 35.035 -20.911 17.918  1.00 21.86 ? 99  PHE A CG  1 
ATOM   784  C  CD1 . PHE A 1 106 ? 35.523 -20.647 16.643  1.00 19.52 ? 99  PHE A CD1 1 
ATOM   785  C  CD2 . PHE A 1 106 ? 35.909 -21.354 18.886  1.00 21.03 ? 99  PHE A CD2 1 
ATOM   786  C  CE1 . PHE A 1 106 ? 36.861 -20.813 16.358  1.00 19.71 ? 99  PHE A CE1 1 
ATOM   787  C  CE2 . PHE A 1 106 ? 37.245 -21.512 18.594  1.00 20.45 ? 99  PHE A CE2 1 
ATOM   788  C  CZ  . PHE A 1 106 ? 37.702 -21.250 17.332  1.00 16.39 ? 99  PHE A CZ  1 
ATOM   789  N  N   . LYS A 1 107 ? 30.645 -19.604 18.596  1.00 27.49 ? 100 LYS A N   1 
ATOM   790  C  CA  . LYS A 1 107 ? 29.224 -19.623 18.271  1.00 31.34 ? 100 LYS A CA  1 
ATOM   791  C  C   . LYS A 1 107 ? 28.798 -18.294 17.670  1.00 35.60 ? 100 LYS A C   1 
ATOM   792  O  O   . LYS A 1 107 ? 28.061 -18.259 16.678  1.00 40.83 ? 100 LYS A O   1 
ATOM   793  C  CB  . LYS A 1 107 ? 28.412 -19.961 19.517  1.00 33.08 ? 100 LYS A CB  1 
ATOM   794  C  CG  . LYS A 1 107 ? 27.320 -20.994 19.294  1.00 44.78 ? 100 LYS A CG  1 
ATOM   795  C  CD  . LYS A 1 107 ? 26.930 -21.662 20.611  1.00 51.59 ? 100 LYS A CD  1 
ATOM   796  C  CE  . LYS A 1 107 ? 25.852 -22.727 20.425  1.00 74.39 ? 100 LYS A CE  1 
ATOM   797  N  NZ  . LYS A 1 107 ? 24.473 -22.219 20.713  1.00 82.23 ? 100 LYS A NZ  1 
ATOM   798  N  N   . ALA A 1 108 ? 29.305 -17.189 18.220  1.00 31.15 ? 101 ALA A N   1 
ATOM   799  C  CA  . ALA A 1 108 ? 28.966 -15.874 17.688  1.00 35.74 ? 101 ALA A CA  1 
ATOM   800  C  C   . ALA A 1 108 ? 29.441 -15.704 16.251  1.00 35.12 ? 101 ALA A C   1 
ATOM   801  O  O   . ALA A 1 108 ? 28.779 -15.026 15.458  1.00 35.59 ? 101 ALA A O   1 
ATOM   802  C  CB  . ALA A 1 108 ? 29.578 -14.782 18.564  1.00 37.38 ? 101 ALA A CB  1 
ATOM   803  N  N   . GLY A 1 109 ? 30.582 -16.301 15.903  1.00 26.34 ? 102 GLY A N   1 
ATOM   804  C  CA  . GLY A 1 109 ? 31.116 -16.136 14.558  1.00 27.80 ? 102 GLY A CA  1 
ATOM   805  C  C   . GLY A 1 109 ? 30.314 -16.876 13.505  1.00 29.18 ? 102 GLY A C   1 
ATOM   806  O  O   . GLY A 1 109 ? 30.186 -16.408 12.368  1.00 24.18 ? 102 GLY A O   1 
ATOM   807  N  N   . GLY A 1 110 ? 29.777 -18.044 13.859  1.00 25.44 ? 103 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 110 ? 28.889 -18.769 12.979  1.00 24.28 ? 103 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 110 ? 29.559 -19.625 11.937  1.00 20.82 ? 103 GLY A C   1 
ATOM   810  O  O   . GLY A 1 110 ? 28.873 -20.120 11.041  1.00 22.25 ? 103 GLY A O   1 
ATOM   811  N  N   . TYR A 1 111 ? 30.871 -19.816 12.017  1.00 18.92 ? 104 TYR A N   1 
ATOM   812  C  CA  . TYR A 1 111 ? 31.631 -20.590 11.043  1.00 17.72 ? 104 TYR A CA  1 
ATOM   813  C  C   . TYR A 1 111 ? 32.256 -21.793 11.740  1.00 20.86 ? 104 TYR A C   1 
ATOM   814  O  O   . TYR A 1 111 ? 32.180 -21.938 12.968  1.00 20.71 ? 104 TYR A O   1 
ATOM   815  C  CB  . TYR A 1 111 ? 32.703 -19.715 10.357  1.00 19.99 ? 104 TYR A CB  1 
ATOM   816  C  CG  . TYR A 1 111 ? 33.525 -18.903 11.312  1.00 19.14 ? 104 TYR A CG  1 
ATOM   817  C  CD1 . TYR A 1 111 ? 34.551 -19.481 12.034  1.00 22.85 ? 104 TYR A CD1 1 
ATOM   818  C  CD2 . TYR A 1 111 ? 33.257 -17.554 11.519  1.00 19.10 ? 104 TYR A CD2 1 
ATOM   819  C  CE1 . TYR A 1 111 ? 35.295 -18.748 12.934  1.00 25.48 ? 104 TYR A CE1 1 
ATOM   820  C  CE2 . TYR A 1 111 ? 33.996 -16.809 12.416  1.00 21.22 ? 104 TYR A CE2 1 
ATOM   821  C  CZ  . TYR A 1 111 ? 35.018 -17.413 13.120  1.00 24.38 ? 104 TYR A CZ  1 
ATOM   822  O  OH  . TYR A 1 111 ? 35.761 -16.689 14.026  1.00 27.64 ? 104 TYR A OH  1 
ATOM   823  N  N   . ARG A 1 112 ? 32.824 -22.694 10.929  1.00 16.60 ? 105 ARG A N   1 
ATOM   824  C  CA  . ARG A 1 112 ? 33.494 -23.893 11.417  1.00 16.64 ? 105 ARG A CA  1 
ATOM   825  C  C   . ARG A 1 112 ? 34.960 -23.843 11.031  1.00 17.26 ? 105 ARG A C   1 
ATOM   826  O  O   . ARG A 1 112 ? 35.300 -23.407 9.925   1.00 17.15 ? 105 ARG A O   1 
ATOM   827  C  CB  . ARG A 1 112 ? 32.863 -25.159 10.841  1.00 17.67 ? 105 ARG A CB  1 
ATOM   828  C  CG  . ARG A 1 112 ? 31.526 -25.513 11.471  1.00 24.21 ? 105 ARG A CG  1 
ATOM   829  C  CD  . ARG A 1 112 ? 30.800 -26.587 10.677  1.00 22.36 ? 105 ARG A CD  1 
ATOM   830  N  NE  . ARG A 1 112 ? 31.579 -27.809 10.561  1.00 23.41 ? 105 ARG A NE  1 
ATOM   831  C  CZ  . ARG A 1 112 ? 31.457 -28.681 9.569   1.00 27.87 ? 105 ARG A CZ  1 
ATOM   832  N  NH1 . ARG A 1 112 ? 30.588 -28.495 8.587   1.00 30.59 ? 105 ARG A NH1 1 
ATOM   833  N  NH2 . ARG A 1 112 ? 32.223 -29.770 9.564   1.00 28.81 ? 105 ARG A NH2 1 
ATOM   834  N  N   . VAL A 1 113 ? 35.809 -24.316 11.934  1.00 15.96 ? 106 VAL A N   1 
ATOM   835  C  CA  . VAL A 1 113 ? 37.259 -24.352 11.734  1.00 13.42 ? 106 VAL A CA  1 
ATOM   836  C  C   . VAL A 1 113 ? 37.697 -25.793 11.970  1.00 14.02 ? 106 VAL A C   1 
ATOM   837  O  O   . VAL A 1 113 ? 37.753 -26.250 13.119  1.00 14.85 ? 106 VAL A O   1 
ATOM   838  C  CB  . VAL A 1 113 ? 37.994 -23.393 12.671  1.00 16.16 ? 106 VAL A CB  1 
ATOM   839  C  CG1 . VAL A 1 113 ? 39.498 -23.377 12.398  1.00 15.46 ? 106 VAL A CG1 1 
ATOM   840  C  CG2 . VAL A 1 113 ? 37.418 -21.991 12.552  1.00 16.40 ? 106 VAL A CG2 1 
ATOM   841  N  N   . VAL A 1 114 ? 37.950 -26.535 10.889  1.00 14.53 ? 107 VAL A N   1 
ATOM   842  C  CA  . VAL A 1 114 ? 38.274 -27.961 10.949  1.00 14.18 ? 107 VAL A CA  1 
ATOM   843  C  C   . VAL A 1 114 ? 39.770 -28.090 11.204  1.00 16.01 ? 107 VAL A C   1 
ATOM   844  O  O   . VAL A 1 114 ? 40.565 -27.508 10.449  1.00 15.62 ? 107 VAL A O   1 
ATOM   845  C  CB  . VAL A 1 114 ? 37.865 -28.675 9.645   1.00 13.85 ? 107 VAL A CB  1 
ATOM   846  C  CG1 . VAL A 1 114 ? 38.227 -30.159 9.639   1.00 15.63 ? 107 VAL A CG1 1 
ATOM   847  C  CG2 . VAL A 1 114 ? 36.384 -28.447 9.397   1.00 16.01 ? 107 VAL A CG2 1 
ATOM   848  N  N   . PRO A 1 115 ? 40.225 -28.865 12.191  1.00 14.77 ? 108 PRO A N   1 
ATOM   849  C  CA  . PRO A 1 115 ? 41.657 -28.936 12.443  1.00 17.25 ? 108 PRO A CA  1 
ATOM   850  C  C   . PRO A 1 115 ? 42.366 -29.624 11.297  1.00 16.88 ? 108 PRO A C   1 
ATOM   851  O  O   . PRO A 1 115 ? 41.883 -30.650 10.786  1.00 15.93 ? 108 PRO A O   1 
ATOM   852  C  CB  . PRO A 1 115 ? 41.768 -29.751 13.742  1.00 20.87 ? 108 PRO A CB  1 
ATOM   853  C  CG  . PRO A 1 115 ? 40.474 -30.381 13.944  1.00 23.62 ? 108 PRO A CG  1 
ATOM   854  C  CD  . PRO A 1 115 ? 39.428 -29.593 13.200  1.00 19.79 ? 108 PRO A CD  1 
ATOM   855  N  N   . PRO A 1 116 ? 43.555 -29.155 10.905  1.00 16.18 ? 109 PRO A N   1 
ATOM   856  C  CA  . PRO A 1 116 ? 44.360 -28.088 11.511  1.00 16.21 ? 109 PRO A CA  1 
ATOM   857  C  C   . PRO A 1 116 ? 44.312 -26.737 10.796  1.00 16.79 ? 109 PRO A C   1 
ATOM   858  O  O   . PRO A 1 116 ? 45.346 -26.088 10.654  1.00 17.81 ? 109 PRO A O   1 
ATOM   859  C  CB  . PRO A 1 116 ? 45.783 -28.679 11.447  1.00 18.61 ? 109 PRO A CB  1 
ATOM   860  C  CG  . PRO A 1 116 ? 45.768 -29.407 10.113  1.00 19.10 ? 109 PRO A CG  1 
ATOM   861  C  CD  . PRO A 1 116 ? 44.367 -30.013 10.025  1.00 18.90 ? 109 PRO A CD  1 
ATOM   862  N  N   . ALA A 1 117 ? 43.131 -26.285 10.379  1.00 15.38 ? 110 ALA A N   1 
ATOM   863  C  CA  . ALA A 1 117 ? 43.004 -24.970 9.757   1.00 14.82 ? 110 ALA A CA  1 
ATOM   864  C  C   . ALA A 1 117 ? 43.460 -23.855 10.689  1.00 15.89 ? 110 ALA A C   1 
ATOM   865  O  O   . ALA A 1 117 ? 43.232 -23.885 11.910  1.00 16.98 ? 110 ALA A O   1 
ATOM   866  C  CB  . ALA A 1 117 ? 41.542 -24.725 9.348   1.00 15.82 ? 110 ALA A CB  1 
ATOM   867  N  N   . VAL A 1 118 ? 44.094 -22.849 10.096  1.00 15.51 ? 111 VAL A N   1 
ATOM   868  C  CA  . VAL A 1 118 ? 44.528 -21.662 10.812  1.00 14.49 ? 111 VAL A CA  1 
ATOM   869  C  C   . VAL A 1 118 ? 44.176 -20.440 9.988   1.00 14.30 ? 111 VAL A C   1 
ATOM   870  O  O   . VAL A 1 118 ? 44.283 -20.449 8.759   1.00 15.28 ? 111 VAL A O   1 
ATOM   871  C  CB  . VAL A 1 118 ? 46.043 -21.686 11.096  1.00 16.28 ? 111 VAL A CB  1 
ATOM   872  C  CG1 . VAL A 1 118 ? 46.498 -20.381 11.715  1.00 21.12 ? 111 VAL A CG1 1 
ATOM   873  C  CG2 . VAL A 1 118 ? 46.382 -22.878 11.996  1.00 20.10 ? 111 VAL A CG2 1 
ATOM   874  N  N   . ALA A 1 119 ? 43.778 -19.364 10.682  1.00 14.51 ? 112 ALA A N   1 
ATOM   875  C  CA  . ALA A 1 119 ? 43.616 -18.054 10.081  1.00 15.78 ? 112 ALA A CA  1 
ATOM   876  C  C   . ALA A 1 119 ? 44.358 -17.051 10.941  1.00 16.86 ? 112 ALA A C   1 
ATOM   877  O  O   . ALA A 1 119 ? 44.458 -17.227 12.156  1.00 16.43 ? 112 ALA A O   1 
ATOM   878  C  CB  . ALA A 1 119 ? 42.160 -17.613 10.004  1.00 16.37 ? 112 ALA A CB  1 
ATOM   879  N  N   . ARG A 1 120 ? 44.829 -15.984 10.324  1.00 13.57 ? 113 ARG A N   1 
ATOM   880  C  CA  . ARG A 1 120 ? 45.466 -14.916 11.076  1.00 15.31 ? 113 ARG A CA  1 
ATOM   881  C  C   . ARG A 1 120 ? 44.449 -13.874 11.531  1.00 17.29 ? 113 ARG A C   1 
ATOM   882  O  O   . ARG A 1 120 ? 43.455 -13.607 10.864  1.00 15.88 ? 113 ARG A O   1 
ATOM   883  C  CB  . ARG A 1 120 ? 46.557 -14.227 10.243  1.00 18.23 ? 113 ARG A CB  1 
ATOM   884  C  CG  . ARG A 1 120 ? 47.920 -14.893 10.380  1.00 18.03 ? 113 ARG A CG  1 
ATOM   885  C  CD  . ARG A 1 120 ? 48.894 -14.378 9.332   1.00 15.36 ? 113 ARG A CD  1 
ATOM   886  N  NE  . ARG A 1 120 ? 50.289 -14.618 9.695   1.00 16.25 ? 113 ARG A NE  1 
ATOM   887  C  CZ  . ARG A 1 120 ? 51.306 -14.262 8.922   1.00 18.99 ? 113 ARG A CZ  1 
ATOM   888  N  NH1 . ARG A 1 120 ? 51.100 -13.720 7.734   1.00 19.10 ? 113 ARG A NH1 1 
ATOM   889  N  NH2 . ARG A 1 120 ? 52.550 -14.441 9.355   1.00 18.09 ? 113 ARG A NH2 1 
ATOM   890  N  N   . ARG A 1 121 ? 44.734 -13.278 12.676  1.00 17.03 ? 114 ARG A N   1 
ATOM   891  C  CA  A ARG A 1 121 ? 43.975 -12.118 13.129  0.50 19.08 ? 114 ARG A CA  1 
ATOM   892  C  CA  B ARG A 1 121 ? 43.959 -12.125 13.123  0.50 19.08 ? 114 ARG A CA  1 
ATOM   893  C  C   . ARG A 1 121 ? 44.013 -11.051 12.050  1.00 22.53 ? 114 ARG A C   1 
ATOM   894  O  O   . ARG A 1 121 ? 45.060 -10.799 11.452  1.00 24.36 ? 114 ARG A O   1 
ATOM   895  C  CB  A ARG A 1 121 ? 44.574 -11.603 14.430  0.50 21.25 ? 114 ARG A CB  1 
ATOM   896  C  CB  B ARG A 1 121 ? 44.503 -11.587 14.444  0.50 21.26 ? 114 ARG A CB  1 
ATOM   897  C  CG  A ARG A 1 121 ? 44.220 -10.178 14.788  0.50 26.01 ? 114 ARG A CG  1 
ATOM   898  C  CG  B ARG A 1 121 ? 43.942 -10.215 14.859  0.50 26.18 ? 114 ARG A CG  1 
ATOM   899  C  CD  A ARG A 1 121 ? 44.923 -9.775  16.068  0.50 30.88 ? 114 ARG A CD  1 
ATOM   900  C  CD  B ARG A 1 121 ? 44.378 -9.841  16.272  0.50 30.61 ? 114 ARG A CD  1 
ATOM   901  N  NE  A ARG A 1 121 ? 45.012 -8.328  16.181  0.50 37.43 ? 114 ARG A NE  1 
ATOM   902  N  NE  B ARG A 1 121 ? 44.275 -8.409  16.540  0.50 36.87 ? 114 ARG A NE  1 
ATOM   903  C  CZ  A ARG A 1 121 ? 43.978 -7.536  16.426  0.50 32.54 ? 114 ARG A CZ  1 
ATOM   904  C  CZ  B ARG A 1 121 ? 45.240 -7.522  16.312  0.50 37.44 ? 114 ARG A CZ  1 
ATOM   905  N  NH1 A ARG A 1 121 ? 42.751 -8.016  16.541  0.50 29.87 ? 114 ARG A NH1 1 
ATOM   906  N  NH1 B ARG A 1 121 ? 46.380 -7.867  15.728  0.50 30.94 ? 114 ARG A NH1 1 
ATOM   907  N  NH2 A ARG A 1 121 ? 44.178 -6.226  16.555  0.50 34.34 ? 114 ARG A NH2 1 
ATOM   908  N  NH2 B ARG A 1 121 ? 45.056 -6.255  16.677  0.50 38.12 ? 114 ARG A NH2 1 
ATOM   909  N  N   . GLY A 1 122 ? 42.867 -10.414 11.805  1.00 18.38 ? 115 GLY A N   1 
ATOM   910  C  CA  . GLY A 1 122 ? 42.791 -9.437  10.747  1.00 18.49 ? 115 GLY A CA  1 
ATOM   911  C  C   . GLY A 1 122 ? 42.215 -9.979  9.467   1.00 17.74 ? 115 GLY A C   1 
ATOM   912  O  O   . GLY A 1 122 ? 42.156 -9.244  8.470   1.00 18.86 ? 115 GLY A O   1 
ATOM   913  N  N   . ALA A 1 123 ? 41.835 -11.248 9.449   1.00 16.60 ? 116 ALA A N   1 
ATOM   914  C  CA  . ALA A 1 123 ? 41.044 -11.826 8.373   1.00 18.47 ? 116 ALA A CA  1 
ATOM   915  C  C   . ALA A 1 123 ? 39.598 -11.904 8.837   1.00 17.53 ? 116 ALA A C   1 
ATOM   916  O  O   . ALA A 1 123 ? 39.337 -12.289 9.976   1.00 20.35 ? 116 ALA A O   1 
ATOM   917  C  CB  . ALA A 1 123 ? 41.523 -13.227 8.025   1.00 16.59 ? 116 ALA A CB  1 
ATOM   918  N  N   . PHE A 1 124 ? 38.666 -11.538 7.958   1.00 16.99 ? 117 PHE A N   1 
ATOM   919  C  CA  . PHE A 1 124 ? 37.247 -11.674 8.260   1.00 16.90 ? 117 PHE A CA  1 
ATOM   920  C  C   . PHE A 1 124 ? 36.711 -12.997 7.723   1.00 16.06 ? 117 PHE A C   1 
ATOM   921  O  O   . PHE A 1 124 ? 36.901 -13.318 6.545   1.00 17.94 ? 117 PHE A O   1 
ATOM   922  C  CB  . PHE A 1 124 ? 36.435 -10.532 7.665   1.00 16.96 ? 117 PHE A CB  1 
ATOM   923  C  CG  . PHE A 1 124 ? 34.957 -10.708 7.839   1.00 17.86 ? 117 PHE A CG  1 
ATOM   924  C  CD1 . PHE A 1 124 ? 34.401 -10.655 9.093   1.00 19.62 ? 117 PHE A CD1 1 
ATOM   925  C  CD2 . PHE A 1 124 ? 34.136 -10.929 6.752   1.00 22.34 ? 117 PHE A CD2 1 
ATOM   926  C  CE1 . PHE A 1 124 ? 33.039 -10.831 9.266   1.00 22.72 ? 117 PHE A CE1 1 
ATOM   927  C  CE2 . PHE A 1 124 ? 32.778 -11.086 6.918   1.00 21.57 ? 117 PHE A CE2 1 
ATOM   928  C  CZ  . PHE A 1 124 ? 32.240 -11.043 8.166   1.00 22.29 ? 117 PHE A CZ  1 
ATOM   929  N  N   . ILE A 1 125 ? 36.021 -13.742 8.583   1.00 17.25 ? 118 ILE A N   1 
ATOM   930  C  CA  . ILE A 1 125 ? 35.357 -14.993 8.210   1.00 15.74 ? 118 ILE A CA  1 
ATOM   931  C  C   . ILE A 1 125 ? 33.870 -14.830 8.554   1.00 15.55 ? 118 ILE A C   1 
ATOM   932  O  O   . ILE A 1 125 ? 33.507 -14.634 9.729   1.00 17.89 ? 118 ILE A O   1 
ATOM   933  C  CB  . ILE A 1 125 ? 35.955 -16.203 8.941   1.00 17.98 ? 118 ILE A CB  1 
ATOM   934  C  CG1 . ILE A 1 125 ? 37.478 -16.305 8.804   1.00 18.35 ? 118 ILE A CG1 1 
ATOM   935  C  CG2 . ILE A 1 125 ? 35.298 -17.481 8.435   1.00 18.63 ? 118 ILE A CG2 1 
ATOM   936  C  CD1 . ILE A 1 125 ? 37.972 -16.542 7.448   1.00 23.96 ? 118 ILE A CD1 1 
ATOM   937  N  N   . ALA A 1 126 ? 33.021 -14.875 7.532   1.00 17.42 ? 119 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 126 ? 31.593 -14.678 7.719   1.00 16.96 ? 119 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 126 ? 30.899 -15.926 8.277   1.00 17.09 ? 119 ALA A C   1 
ATOM   940  O  O   . ALA A 1 126 ? 31.474 -17.013 8.372   1.00 18.19 ? 119 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 126 ? 30.931 -14.311 6.392   1.00 19.32 ? 119 ALA A CB  1 
ATOM   942  N  N   . ARG A 1 127 ? 29.616 -15.741 8.623   1.00 19.84 ? 120 ARG A N   1 
ATOM   943  C  CA  . ARG A 1 127 ? 28.780 -16.851 9.055   1.00 20.41 ? 120 ARG A CA  1 
ATOM   944  C  C   . ARG A 1 127 ? 28.670 -17.900 7.957   1.00 21.77 ? 120 ARG A C   1 
ATOM   945  O  O   . ARG A 1 127 ? 28.696 -17.586 6.767   1.00 19.22 ? 120 ARG A O   1 
ATOM   946  C  CB  . ARG A 1 127 ? 27.371 -16.371 9.413   1.00 21.44 ? 120 ARG A CB  1 
ATOM   947  C  CG  . ARG A 1 127 ? 27.321 -15.321 10.494  1.00 32.25 ? 120 ARG A CG  1 
ATOM   948  C  CD  . ARG A 1 127 ? 25.878 -15.137 11.024  1.00 31.84 ? 120 ARG A CD  1 
ATOM   949  N  NE  . ARG A 1 127 ? 25.416 -16.369 11.651  1.00 33.45 ? 120 ARG A NE  1 
ATOM   950  C  CZ  . ARG A 1 127 ? 25.681 -16.720 12.903  1.00 39.13 ? 120 ARG A CZ  1 
ATOM   951  N  NH1 . ARG A 1 127 ? 26.394 -15.942 13.706  1.00 42.17 ? 120 ARG A NH1 1 
ATOM   952  N  NH2 . ARG A 1 127 ? 25.208 -17.872 13.367  1.00 40.57 ? 120 ARG A NH2 1 
ATOM   953  N  N   . ASN A 1 128 ? 28.522 -19.161 8.382   1.00 20.11 ? 121 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 128 ? 28.262 -20.327 7.540   1.00 19.67 ? 121 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 128 ? 29.422 -20.643 6.615   1.00 21.15 ? 121 ASN A C   1 
ATOM   956  O  O   . ASN A 1 128 ? 29.263 -21.441 5.690   1.00 24.25 ? 121 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 128 ? 26.963 -20.151 6.753   1.00 22.11 ? 121 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 128 ? 25.777 -19.959 7.668   1.00 26.75 ? 121 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 128 ? 25.657 -20.631 8.695   1.00 27.51 ? 121 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 128 ? 24.914 -19.019 7.325   1.00 35.09 ? 121 ASN A ND2 1 
ATOM   961  N  N   . VAL A 1 129 ? 30.579 -20.087 6.863   1.00 18.56 ? 122 VAL A N   1 
ATOM   962  C  CA  . VAL A 1 129 ? 31.805 -20.526 6.217   1.00 16.40 ? 122 VAL A CA  1 
ATOM   963  C  C   . VAL A 1 129 ? 32.275 -21.816 6.870   1.00 16.69 ? 122 VAL A C   1 
ATOM   964  O  O   . VAL A 1 129 ? 32.140 -22.031 8.081   1.00 17.98 ? 122 VAL A O   1 
ATOM   965  C  CB  . VAL A 1 129 ? 32.872 -19.415 6.315   1.00 16.68 ? 122 VAL A CB  1 
ATOM   966  C  CG1 . VAL A 1 129 ? 34.226 -19.928 5.867   1.00 17.98 ? 122 VAL A CG1 1 
ATOM   967  C  CG2 . VAL A 1 129 ? 32.467 -18.220 5.462   1.00 18.16 ? 122 VAL A CG2 1 
ATOM   968  N  N   . VAL A 1 130 ? 32.865 -22.687 6.052   1.00 17.27 ? 123 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 130 ? 33.549 -23.865 6.549   1.00 16.30 ? 123 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 130 ? 34.996 -23.756 6.113   1.00 14.15 ? 123 VAL A C   1 
ATOM   971  O  O   . VAL A 1 130 ? 35.292 -23.703 4.907   1.00 16.00 ? 123 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 130 ? 32.919 -25.168 6.041   1.00 18.51 ? 123 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 130 ? 33.703 -26.360 6.578   1.00 19.97 ? 123 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 130 ? 31.476 -25.250 6.443   1.00 18.44 ? 123 VAL A CG2 1 
ATOM   975  N  N   . LEU A 1 131 ? 35.891 -23.733 7.082   1.00 15.76 ? 124 LEU A N   1 
ATOM   976  C  CA  . LEU A 1 131 ? 37.324 -23.806 6.810   1.00 15.49 ? 124 LEU A CA  1 
ATOM   977  C  C   . LEU A 1 131 ? 37.757 -25.249 7.059   1.00 15.27 ? 124 LEU A C   1 
ATOM   978  O  O   . LEU A 1 131 ? 37.899 -25.667 8.207   1.00 14.02 ? 124 LEU A O   1 
ATOM   979  C  CB  . LEU A 1 131 ? 38.087 -22.839 7.706   1.00 14.74 ? 124 LEU A CB  1 
ATOM   980  C  CG  . LEU A 1 131 ? 37.747 -21.345 7.606   1.00 15.75 ? 124 LEU A CG  1 
ATOM   981  C  CD1 . LEU A 1 131 ? 38.603 -20.607 8.607   1.00 19.87 ? 124 LEU A CD1 1 
ATOM   982  C  CD2 . LEU A 1 131 ? 37.934 -20.826 6.211   1.00 16.43 ? 124 LEU A CD2 1 
ATOM   983  N  N   . MET A 1 132 ? 37.888 -26.029 5.990   1.00 14.34 ? 125 MET A N   1 
ATOM   984  C  CA  . MET A 1 132 ? 38.605 -27.304 6.070   1.00 14.83 ? 125 MET A CA  1 
ATOM   985  C  C   . MET A 1 132 ? 40.050 -26.947 6.359   1.00 13.80 ? 125 MET A C   1 
ATOM   986  O  O   . MET A 1 132 ? 40.398 -25.767 6.378   1.00 15.77 ? 125 MET A O   1 
ATOM   987  C  CB  . MET A 1 132 ? 38.465 -28.083 4.765   1.00 16.16 ? 125 MET A CB  1 
ATOM   988  C  CG  . MET A 1 132 ? 37.029 -28.477 4.494   1.00 17.31 ? 125 MET A CG  1 
ATOM   989  S  SD  . MET A 1 132 ? 36.443 -29.693 5.716   1.00 21.44 ? 125 MET A SD  1 
ATOM   990  C  CE  . MET A 1 132 ? 37.483 -31.114 5.188   1.00 23.13 ? 125 MET A CE  1 
ATOM   991  N  N   . PRO A 1 133 ? 40.922 -27.925 6.617   1.00 14.52 ? 126 PRO A N   1 
ATOM   992  C  CA  . PRO A 1 133 ? 42.343 -27.570 6.812   1.00 15.49 ? 126 PRO A CA  1 
ATOM   993  C  C   . PRO A 1 133 ? 42.825 -26.657 5.697   1.00 12.55 ? 126 PRO A C   1 
ATOM   994  O  O   . PRO A 1 133 ? 42.727 -27.040 4.539   1.00 15.18 ? 126 PRO A O   1 
ATOM   995  C  CB  . PRO A 1 133 ? 43.042 -28.922 6.778   1.00 16.36 ? 126 PRO A CB  1 
ATOM   996  C  CG  . PRO A 1 133 ? 41.992 -29.870 7.305   1.00 17.60 ? 126 PRO A CG  1 
ATOM   997  C  CD  . PRO A 1 133 ? 40.704 -29.385 6.714   1.00 15.76 ? 126 PRO A CD  1 
ATOM   998  N  N   . SER A 1 134 ? 43.259 -25.442 6.019   1.00 13.85 ? 127 SER A N   1 
ATOM   999  C  CA  . SER A 1 134 ? 43.429 -24.385 5.027   1.00 13.03 ? 127 SER A CA  1 
ATOM   1000 C  C   . SER A 1 134 ? 44.099 -23.235 5.754   1.00 12.81 ? 127 SER A C   1 
ATOM   1001 O  O   . SER A 1 134 ? 44.279 -23.278 6.979   1.00 14.31 ? 127 SER A O   1 
ATOM   1002 C  CB  . SER A 1 134 ? 42.078 -23.960 4.446   1.00 13.60 ? 127 SER A CB  1 
ATOM   1003 O  OG  . SER A 1 134 ? 41.269 -23.405 5.454   1.00 14.62 ? 127 SER A OG  1 
ATOM   1004 N  N   . TYR A 1 135 ? 44.468 -22.202 4.994   1.00 12.90 ? 128 TYR A N   1 
ATOM   1005 C  CA  . TYR A 1 135 ? 45.058 -21.022 5.599   1.00 12.20 ? 128 TYR A CA  1 
ATOM   1006 C  C   . TYR A 1 135 ? 44.377 -19.784 5.067   1.00 11.21 ? 128 TYR A C   1 
ATOM   1007 O  O   . TYR A 1 135 ? 44.143 -19.696 3.860   1.00 13.74 ? 128 TYR A O   1 
ATOM   1008 C  CB  . TYR A 1 135 ? 46.543 -20.938 5.284   1.00 12.40 ? 128 TYR A CB  1 
ATOM   1009 C  CG  . TYR A 1 135 ? 47.264 -19.934 6.135   1.00 12.34 ? 128 TYR A CG  1 
ATOM   1010 C  CD1 . TYR A 1 135 ? 47.409 -20.131 7.506   1.00 13.72 ? 128 TYR A CD1 1 
ATOM   1011 C  CD2 . TYR A 1 135 ? 47.828 -18.810 5.574   1.00 13.59 ? 128 TYR A CD2 1 
ATOM   1012 C  CE1 . TYR A 1 135 ? 48.100 -19.229 8.280   1.00 15.53 ? 128 TYR A CE1 1 
ATOM   1013 C  CE2 . TYR A 1 135 ? 48.525 -17.899 6.349   1.00 16.95 ? 128 TYR A CE2 1 
ATOM   1014 C  CZ  . TYR A 1 135 ? 48.646 -18.114 7.689   1.00 15.25 ? 128 TYR A CZ  1 
ATOM   1015 O  OH  . TYR A 1 135 ? 49.355 -17.247 8.475   1.00 16.91 ? 128 TYR A OH  1 
ATOM   1016 N  N   . VAL A 1 136 ? 44.049 -18.851 5.963   1.00 13.33 ? 129 VAL A N   1 
ATOM   1017 C  CA  . VAL A 1 136 ? 43.508 -17.545 5.600   1.00 11.98 ? 129 VAL A CA  1 
ATOM   1018 C  C   . VAL A 1 136 ? 44.408 -16.476 6.202   1.00 13.48 ? 129 VAL A C   1 
ATOM   1019 O  O   . VAL A 1 136 ? 44.557 -16.393 7.427   1.00 14.76 ? 129 VAL A O   1 
ATOM   1020 C  CB  . VAL A 1 136 ? 42.063 -17.370 6.079   1.00 14.13 ? 129 VAL A CB  1 
ATOM   1021 C  CG1 . VAL A 1 136 ? 41.548 -16.018 5.636   1.00 17.17 ? 129 VAL A CG1 1 
ATOM   1022 C  CG2 . VAL A 1 136 ? 41.212 -18.535 5.522   1.00 17.49 ? 129 VAL A CG2 1 
ATOM   1023 N  N   . ASN A 1 137 ? 45.023 -15.677 5.337   1.00 14.25 ? 130 ASN A N   1 
ATOM   1024 C  CA  . ASN A 1 137 ? 46.027 -14.702 5.750   1.00 13.24 ? 130 ASN A CA  1 
ATOM   1025 C  C   . ASN A 1 137 ? 45.366 -13.362 6.105   1.00 14.48 ? 130 ASN A C   1 
ATOM   1026 O  O   . ASN A 1 137 ? 44.193 -13.111 5.821   1.00 16.34 ? 130 ASN A O   1 
ATOM   1027 C  CB  . ASN A 1 137 ? 47.058 -14.548 4.628   1.00 15.30 ? 130 ASN A CB  1 
ATOM   1028 C  CG  . ASN A 1 137 ? 48.420 -14.139 5.114   1.00 15.51 ? 130 ASN A CG  1 
ATOM   1029 O  OD1 . ASN A 1 137 ? 48.589 -13.637 6.212   1.00 15.61 ? 130 ASN A OD1 1 
ATOM   1030 N  ND2 . ASN A 1 137 ? 49.438 -14.384 4.278   1.00 17.79 ? 130 ASN A ND2 1 
ATOM   1031 N  N   . ILE A 1 138 ? 46.152 -12.499 6.750   1.00 14.71 ? 131 ILE A N   1 
ATOM   1032 C  CA  . ILE A 1 138 ? 45.658 -11.217 7.237   1.00 15.22 ? 131 ILE A CA  1 
ATOM   1033 C  C   . ILE A 1 138 ? 45.114 -10.369 6.099   1.00 17.31 ? 131 ILE A C   1 
ATOM   1034 O  O   . ILE A 1 138 ? 45.649 -10.350 4.984   1.00 16.89 ? 131 ILE A O   1 
ATOM   1035 C  CB  . ILE A 1 138 ? 46.799 -10.512 7.990   1.00 16.50 ? 131 ILE A CB  1 
ATOM   1036 C  CG1 . ILE A 1 138 ? 46.343 -9.188  8.616   1.00 18.30 ? 131 ILE A CG1 1 
ATOM   1037 C  CG2 . ILE A 1 138 ? 47.972 -10.260 7.049   1.00 18.52 ? 131 ILE A CG2 1 
ATOM   1038 C  CD1 . ILE A 1 138 ? 47.300 -8.727  9.696   1.00 19.57 ? 131 ILE A CD1 1 
ATOM   1039 N  N   . GLY A 1 139 ? 44.027 -9.657  6.376   1.00 17.31 ? 132 GLY A N   1 
ATOM   1040 C  CA  . GLY A 1 139 ? 43.425 -8.803  5.380   1.00 16.26 ? 132 GLY A CA  1 
ATOM   1041 C  C   . GLY A 1 139 ? 42.424 -9.460  4.468   1.00 18.59 ? 132 GLY A C   1 
ATOM   1042 O  O   . GLY A 1 139 ? 41.718 -8.746  3.738   1.00 18.74 ? 132 GLY A O   1 
ATOM   1043 N  N   . ALA A 1 140 ? 42.352 -10.788 4.458   1.00 15.83 ? 133 ALA A N   1 
ATOM   1044 C  CA  . ALA A 1 140 ? 41.404 -11.480 3.601   1.00 15.72 ? 133 ALA A CA  1 
ATOM   1045 C  C   . ALA A 1 140 ? 39.994 -11.273 4.124   1.00 15.16 ? 133 ALA A C   1 
ATOM   1046 O  O   . ALA A 1 140 ? 39.776 -11.029 5.313   1.00 16.27 ? 133 ALA A O   1 
ATOM   1047 C  CB  . ALA A 1 140 ? 41.742 -12.970 3.535   1.00 17.10 ? 133 ALA A CB  1 
ATOM   1048 N  N   . TYR A 1 141 ? 39.032 -11.360 3.215   1.00 14.16 ? 134 TYR A N   1 
ATOM   1049 C  CA  . TYR A 1 141 ? 37.614 -11.256 3.537   1.00 14.79 ? 134 TYR A CA  1 
ATOM   1050 C  C   . TYR A 1 141 ? 36.920 -12.459 2.910   1.00 16.45 ? 134 TYR A C   1 
ATOM   1051 O  O   . TYR A 1 141 ? 36.974 -12.624 1.694   1.00 16.66 ? 134 TYR A O   1 
ATOM   1052 C  CB  . TYR A 1 141 ? 37.060 -9.944  2.988   1.00 17.39 ? 134 TYR A CB  1 
ATOM   1053 C  CG  . TYR A 1 141 ? 35.663 -9.592  3.393   1.00 19.58 ? 134 TYR A CG  1 
ATOM   1054 C  CD1 . TYR A 1 141 ? 34.569 -10.208 2.795   1.00 20.04 ? 134 TYR A CD1 1 
ATOM   1055 C  CD2 . TYR A 1 141 ? 35.433 -8.621  4.336   1.00 16.84 ? 134 TYR A CD2 1 
ATOM   1056 C  CE1 . TYR A 1 141 ? 33.289 -9.870  3.158   1.00 23.52 ? 134 TYR A CE1 1 
ATOM   1057 C  CE2 . TYR A 1 141 ? 34.141 -8.256  4.702   1.00 22.07 ? 134 TYR A CE2 1 
ATOM   1058 C  CZ  . TYR A 1 141 ? 33.077 -8.897  4.112   1.00 23.77 ? 134 TYR A CZ  1 
ATOM   1059 O  OH  . TYR A 1 141 ? 31.790 -8.554  4.467   1.00 26.43 ? 134 TYR A OH  1 
ATOM   1060 N  N   . VAL A 1 142 ? 36.321 -13.324 3.737   1.00 16.50 ? 135 VAL A N   1 
ATOM   1061 C  CA  . VAL A 1 142 ? 35.677 -14.540 3.254   1.00 15.80 ? 135 VAL A CA  1 
ATOM   1062 C  C   . VAL A 1 142 ? 34.201 -14.453 3.618   1.00 15.26 ? 135 VAL A C   1 
ATOM   1063 O  O   . VAL A 1 142 ? 33.843 -14.576 4.793   1.00 18.56 ? 135 VAL A O   1 
ATOM   1064 C  CB  . VAL A 1 142 ? 36.324 -15.806 3.839   1.00 15.51 ? 135 VAL A CB  1 
ATOM   1065 C  CG1 . VAL A 1 142 ? 35.684 -17.048 3.222   1.00 19.44 ? 135 VAL A CG1 1 
ATOM   1066 C  CG2 . VAL A 1 142 ? 37.821 -15.809 3.606   1.00 19.03 ? 135 VAL A CG2 1 
ATOM   1067 N  N   . ASP A 1 143 ? 33.345 -14.214 2.617   1.00 18.84 ? 136 ASP A N   1 
ATOM   1068 C  CA  . ASP A 1 143 ? 31.951 -13.877 2.859   1.00 18.82 ? 136 ASP A CA  1 
ATOM   1069 C  C   . ASP A 1 143 ? 31.100 -15.137 3.045   1.00 20.13 ? 136 ASP A C   1 
ATOM   1070 O  O   . ASP A 1 143 ? 31.571 -16.276 2.931   1.00 18.55 ? 136 ASP A O   1 
ATOM   1071 C  CB  . ASP A 1 143 ? 31.418 -13.014 1.714   1.00 18.19 ? 136 ASP A CB  1 
ATOM   1072 C  CG  . ASP A 1 143 ? 30.363 -12.004 2.145   1.00 20.42 ? 136 ASP A CG  1 
ATOM   1073 O  OD1 . ASP A 1 143 ? 29.760 -12.110 3.251   1.00 23.60 ? 136 ASP A OD1 1 
ATOM   1074 O  OD2 . ASP A 1 143 ? 30.115 -11.089 1.332   1.00 23.12 ? 136 ASP A OD2 1 
ATOM   1075 N  N   . GLU A 1 144 ? 29.821 -14.888 3.324   1.00 18.20 ? 137 GLU A N   1 
ATOM   1076 C  CA  . GLU A 1 144 ? 28.911 -15.873 3.890   1.00 20.99 ? 137 GLU A CA  1 
ATOM   1077 C  C   . GLU A 1 144 ? 28.754 -17.103 3.004   1.00 21.83 ? 137 GLU A C   1 
ATOM   1078 O  O   . GLU A 1 144 ? 28.629 -17.002 1.785   1.00 20.69 ? 137 GLU A O   1 
ATOM   1079 C  CB  . GLU A 1 144 ? 27.544 -15.204 4.109   1.00 22.04 ? 137 GLU A CB  1 
ATOM   1080 C  CG  . GLU A 1 144 ? 26.555 -16.016 4.907   1.00 33.64 ? 137 GLU A CG  1 
ATOM   1081 C  CD  . GLU A 1 144 ? 25.661 -16.918 4.046   1.00 49.60 ? 137 GLU A CD  1 
ATOM   1082 O  OE1 . GLU A 1 144 ? 25.165 -17.949 4.565   1.00 48.81 ? 137 GLU A OE1 1 
ATOM   1083 O  OE2 . GLU A 1 144 ? 25.448 -16.601 2.851   1.00 52.82 ? 137 GLU A OE2 1 
ATOM   1084 N  N   . GLY A 1 145 ? 28.724 -18.270 3.641   1.00 19.32 ? 138 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 145 ? 28.398 -19.510 2.968   1.00 21.38 ? 138 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 145 ? 29.516 -20.131 2.175   1.00 19.35 ? 138 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 145 ? 29.291 -21.144 1.502   1.00 21.16 ? 138 GLY A O   1 
ATOM   1088 N  N   . THR A 1 146 ? 30.700 -19.562 2.218   1.00 17.19 ? 139 THR A N   1 
ATOM   1089 C  CA  . THR A 1 146 ? 31.798 -20.036 1.398   1.00 16.22 ? 139 THR A CA  1 
ATOM   1090 C  C   . THR A 1 146 ? 32.478 -21.241 2.014   1.00 19.69 ? 139 THR A C   1 
ATOM   1091 O  O   . THR A 1 146 ? 32.597 -21.355 3.231   1.00 16.80 ? 139 THR A O   1 
ATOM   1092 C  CB  . THR A 1 146 ? 32.781 -18.898 1.168   1.00 17.02 ? 139 THR A CB  1 
ATOM   1093 O  OG1 . THR A 1 146 ? 32.149 -18.027 0.217   1.00 18.90 ? 139 THR A OG1 1 
ATOM   1094 C  CG2 . THR A 1 146 ? 34.099 -19.396 0.637   1.00 19.07 ? 139 THR A CG2 1 
ATOM   1095 N  N   . MET A 1 147 ? 32.895 -22.164 1.145   1.00 16.76 ? 140 MET A N   1 
ATOM   1096 C  CA  . MET A 1 147 ? 33.603 -23.376 1.530   1.00 16.42 ? 140 MET A CA  1 
ATOM   1097 C  C   . MET A 1 147 ? 35.057 -23.226 1.115   1.00 18.99 ? 140 MET A C   1 
ATOM   1098 O  O   . MET A 1 147 ? 35.339 -22.952 -0.053  1.00 17.78 ? 140 MET A O   1 
ATOM   1099 C  CB  . MET A 1 147 ? 32.968 -24.594 0.856   1.00 19.15 ? 140 MET A CB  1 
ATOM   1100 C  CG  . MET A 1 147 ? 31.467 -24.757 1.110   1.00 37.64 ? 140 MET A CG  1 
ATOM   1101 S  SD  . MET A 1 147 ? 30.987 -25.101 2.828   1.00 52.44 ? 140 MET A SD  1 
ATOM   1102 C  CE  . MET A 1 147 ? 29.989 -23.658 3.252   1.00 36.94 ? 140 MET A CE  1 
ATOM   1103 N  N   . VAL A 1 148 ? 35.968 -23.381 2.065   1.00 15.73 ? 141 VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 148 ? 37.399 -23.353 1.805   1.00 15.39 ? 141 VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 148 ? 37.892 -24.770 2.052   1.00 16.19 ? 141 VAL A C   1 
ATOM   1106 O  O   . VAL A 1 148 ? 37.955 -25.213 3.198   1.00 16.18 ? 141 VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 148 ? 38.118 -22.343 2.698   1.00 15.69 ? 141 VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 148 ? 39.602 -22.296 2.399   1.00 16.96 ? 141 VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 148 ? 37.540 -20.928 2.526   1.00 19.03 ? 141 VAL A CG2 1 
ATOM   1110 N  N   . ASP A 1 149 ? 38.233 -25.489 0.987   1.00 14.63 ? 142 ASP A N   1 
ATOM   1111 C  CA  . ASP A 1 149 ? 38.507 -26.913 1.100   1.00 16.06 ? 142 ASP A CA  1 
ATOM   1112 C  C   . ASP A 1 149 ? 39.966 -27.193 1.456   1.00 15.22 ? 142 ASP A C   1 
ATOM   1113 O  O   . ASP A 1 149 ? 40.768 -26.292 1.695   1.00 14.54 ? 142 ASP A O   1 
ATOM   1114 C  CB  . ASP A 1 149 ? 38.114 -27.610 -0.196  1.00 16.81 ? 142 ASP A CB  1 
ATOM   1115 C  CG  . ASP A 1 149 ? 36.626 -27.900 -0.287  1.00 31.51 ? 142 ASP A CG  1 
ATOM   1116 O  OD1 . ASP A 1 149 ? 35.864 -27.510 0.633   1.00 28.77 ? 142 ASP A OD1 1 
ATOM   1117 O  OD2 . ASP A 1 149 ? 36.219 -28.539 -1.289  1.00 28.05 ? 142 ASP A OD2 1 
ATOM   1118 N  N   . THR A 1 150 ? 40.298 -28.483 1.545   1.00 15.90 ? 143 THR A N   1 
ATOM   1119 C  CA  . THR A 1 150 ? 41.533 -28.902 2.200   1.00 15.69 ? 143 THR A CA  1 
ATOM   1120 C  C   . THR A 1 150 ? 42.775 -28.452 1.440   1.00 16.16 ? 143 THR A C   1 
ATOM   1121 O  O   . THR A 1 150 ? 42.905 -28.658 0.225   1.00 15.36 ? 143 THR A O   1 
ATOM   1122 C  CB  . THR A 1 150 ? 41.511 -30.411 2.379   1.00 15.33 ? 143 THR A CB  1 
ATOM   1123 O  OG1 . THR A 1 150 ? 40.335 -30.755 3.143   1.00 16.62 ? 143 THR A OG1 1 
ATOM   1124 C  CG2 . THR A 1 150 ? 42.732 -30.904 3.100   1.00 16.07 ? 143 THR A CG2 1 
ATOM   1125 N  N   . TRP A 1 151 ? 43.685 -27.836 2.200   1.00 13.70 ? 144 TRP A N   1 
ATOM   1126 C  CA  . TRP A 1 151 ? 44.943 -27.245 1.751   1.00 12.84 ? 144 TRP A CA  1 
ATOM   1127 C  C   . TRP A 1 151 ? 44.737 -26.140 0.715   1.00 13.85 ? 144 TRP A C   1 
ATOM   1128 O  O   . TRP A 1 151 ? 45.657 -25.812 -0.052  1.00 15.01 ? 144 TRP A O   1 
ATOM   1129 C  CB  . TRP A 1 151 ? 45.944 -28.284 1.238   1.00 13.63 ? 144 TRP A CB  1 
ATOM   1130 C  CG  . TRP A 1 151 ? 46.127 -29.472 2.130   1.00 14.72 ? 144 TRP A CG  1 
ATOM   1131 C  CD1 . TRP A 1 151 ? 46.101 -30.786 1.742   1.00 15.54 ? 144 TRP A CD1 1 
ATOM   1132 C  CD2 . TRP A 1 151 ? 46.370 -29.481 3.540   1.00 15.34 ? 144 TRP A CD2 1 
ATOM   1133 N  NE1 . TRP A 1 151 ? 46.312 -31.592 2.817   1.00 16.63 ? 144 TRP A NE1 1 
ATOM   1134 C  CE2 . TRP A 1 151 ? 46.468 -30.826 3.938   1.00 16.55 ? 144 TRP A CE2 1 
ATOM   1135 C  CE3 . TRP A 1 151 ? 46.506 -28.493 4.505   1.00 15.19 ? 144 TRP A CE3 1 
ATOM   1136 C  CZ2 . TRP A 1 151 ? 46.675 -31.198 5.248   1.00 17.60 ? 144 TRP A CZ2 1 
ATOM   1137 C  CZ3 . TRP A 1 151 ? 46.727 -28.872 5.811   1.00 16.24 ? 144 TRP A CZ3 1 
ATOM   1138 C  CH2 . TRP A 1 151 ? 46.807 -30.210 6.172   1.00 17.43 ? 144 TRP A CH2 1 
ATOM   1139 N  N   . ALA A 1 152 ? 43.589 -25.493 0.769   1.00 14.12 ? 145 ALA A N   1 
ATOM   1140 C  CA  . ALA A 1 152 ? 43.420 -24.226 0.085   1.00 15.19 ? 145 ALA A CA  1 
ATOM   1141 C  C   . ALA A 1 152 ? 44.048 -23.092 0.884   1.00 14.19 ? 145 ALA A C   1 
ATOM   1142 O  O   . ALA A 1 152 ? 44.360 -23.215 2.083   1.00 12.49 ? 145 ALA A O   1 
ATOM   1143 C  CB  . ALA A 1 152 ? 41.941 -23.919 -0.145  1.00 14.96 ? 145 ALA A CB  1 
ATOM   1144 N  N   . THR A 1 153 ? 44.258 -21.982 0.189   1.00 13.21 ? 146 THR A N   1 
ATOM   1145 C  CA  . THR A 1 153 ? 44.873 -20.795 0.765   1.00 13.17 ? 146 THR A CA  1 
ATOM   1146 C  C   . THR A 1 153 ? 44.122 -19.565 0.283   1.00 12.94 ? 146 THR A C   1 
ATOM   1147 O  O   . THR A 1 153 ? 43.904 -19.408 -0.924  1.00 14.35 ? 146 THR A O   1 
ATOM   1148 C  CB  . THR A 1 153 ? 46.333 -20.657 0.338   1.00 17.87 ? 146 THR A CB  1 
ATOM   1149 O  OG1 . THR A 1 153 ? 47.068 -21.825 0.691   1.00 22.49 ? 146 THR A OG1 1 
ATOM   1150 C  CG2 . THR A 1 153 ? 46.983 -19.446 1.014   1.00 18.80 ? 146 THR A CG2 1 
ATOM   1151 N  N   . VAL A 1 154 ? 43.755 -18.693 1.208   1.00 12.84 ? 147 VAL A N   1 
ATOM   1152 C  CA  . VAL A 1 154 ? 43.213 -17.371 0.880   1.00 12.78 ? 147 VAL A CA  1 
ATOM   1153 C  C   . VAL A 1 154 ? 44.266 -16.367 1.308   1.00 13.60 ? 147 VAL A C   1 
ATOM   1154 O  O   . VAL A 1 154 ? 44.455 -16.132 2.503   1.00 14.18 ? 147 VAL A O   1 
ATOM   1155 C  CB  . VAL A 1 154 ? 41.874 -17.109 1.562   1.00 15.02 ? 147 VAL A CB  1 
ATOM   1156 C  CG1 . VAL A 1 154 ? 41.337 -15.717 1.190   1.00 14.84 ? 147 VAL A CG1 1 
ATOM   1157 C  CG2 . VAL A 1 154 ? 40.857 -18.209 1.186   1.00 16.00 ? 147 VAL A CG2 1 
ATOM   1158 N  N   . GLY A 1 155 ? 44.955 -15.798 0.332   1.00 12.73 ? 148 GLY A N   1 
ATOM   1159 C  CA  . GLY A 1 155 ? 46.078 -14.928 0.604   1.00 14.58 ? 148 GLY A CA  1 
ATOM   1160 C  C   . GLY A 1 155 ? 45.708 -13.561 1.099   1.00 14.51 ? 148 GLY A C   1 
ATOM   1161 O  O   . GLY A 1 155 ? 44.546 -13.130 1.143   1.00 15.39 ? 148 GLY A O   1 
ATOM   1162 N  N   . SER A 1 156 ? 46.750 -12.814 1.466   1.00 14.91 ? 149 SER A N   1 
ATOM   1163 C  CA  A SER A 1 156 ? 46.535 -11.523 2.098   0.50 14.93 ? 149 SER A CA  1 
ATOM   1164 C  CA  B SER A 1 156 ? 46.545 -11.520 2.093   0.50 14.93 ? 149 SER A CA  1 
ATOM   1165 C  C   . SER A 1 156 ? 45.705 -10.605 1.212   1.00 16.12 ? 149 SER A C   1 
ATOM   1166 O  O   . SER A 1 156 ? 45.961 -10.458 0.007   1.00 16.64 ? 149 SER A O   1 
ATOM   1167 C  CB  A SER A 1 156 ? 47.866 -10.863 2.436   0.50 22.22 ? 149 SER A CB  1 
ATOM   1168 C  CB  B SER A 1 156 ? 47.892 -10.879 2.406   0.50 22.24 ? 149 SER A CB  1 
ATOM   1169 O  OG  A SER A 1 156 ? 48.676 -10.810 1.282   0.50 27.96 ? 149 SER A OG  1 
ATOM   1170 O  OG  B SER A 1 156 ? 47.719 -9.632  3.032   0.50 21.17 ? 149 SER A OG  1 
ATOM   1171 N  N   . CYS A 1 157 ? 44.696 -10.009 1.820   1.00 15.55 ? 150 CYS A N   1 
ATOM   1172 C  CA  . CYS A 1 157 ? 43.840 -8.982  1.249   1.00 17.56 ? 150 CYS A CA  1 
ATOM   1173 C  C   . CYS A 1 157 ? 42.843 -9.530  0.238   1.00 17.70 ? 150 CYS A C   1 
ATOM   1174 O  O   . CYS A 1 157 ? 42.035 -8.752  -0.260  1.00 15.84 ? 150 CYS A O   1 
ATOM   1175 C  CB  . CYS A 1 157 ? 44.661 -7.869  0.590   1.00 16.28 ? 150 CYS A CB  1 
ATOM   1176 S  SG  . CYS A 1 157 ? 45.770 -6.995  1.758   1.00 20.92 ? 150 CYS A SG  1 
ATOM   1177 N  N   . ALA A 1 158 ? 42.846 -10.835 -0.052  1.00 15.92 ? 151 ALA A N   1 
ATOM   1178 C  CA  . ALA A 1 158 ? 41.946 -11.378 -1.064  1.00 14.84 ? 151 ALA A CA  1 
ATOM   1179 C  C   . ALA A 1 158 ? 40.505 -11.231 -0.619  1.00 15.34 ? 151 ALA A C   1 
ATOM   1180 O  O   . ALA A 1 158 ? 40.198 -11.332 0.572   1.00 16.21 ? 151 ALA A O   1 
ATOM   1181 C  CB  . ALA A 1 158 ? 42.241 -12.861 -1.311  1.00 15.47 ? 151 ALA A CB  1 
ATOM   1182 N  N   . GLN A 1 159 ? 39.623 -10.968 -1.584  1.00 15.90 ? 152 GLN A N   1 
ATOM   1183 C  CA  . GLN A 1 159 ? 38.195 -10.774 -1.337  1.00 15.18 ? 152 GLN A CA  1 
ATOM   1184 C  C   . GLN A 1 159 ? 37.453 -11.956 -1.947  1.00 16.14 ? 152 GLN A C   1 
ATOM   1185 O  O   . GLN A 1 159 ? 37.427 -12.109 -3.171  1.00 16.64 ? 152 GLN A O   1 
ATOM   1186 C  CB  . GLN A 1 159 ? 37.702 -9.454  -1.924  1.00 15.44 ? 152 GLN A CB  1 
ATOM   1187 C  CG  . GLN A 1 159 ? 38.518 -8.224  -1.459  1.00 16.45 ? 152 GLN A CG  1 
ATOM   1188 C  CD  . GLN A 1 159 ? 38.339 -7.911  0.018   1.00 18.37 ? 152 GLN A CD  1 
ATOM   1189 O  OE1 . GLN A 1 159 ? 37.223 -7.732  0.489   1.00 18.70 ? 152 GLN A OE1 1 
ATOM   1190 N  NE2 . GLN A 1 159 ? 39.450 -7.791  0.755   1.00 18.61 ? 152 GLN A NE2 1 
ATOM   1191 N  N   . ILE A 1 160 ? 36.845 -12.776 -1.093  1.00 14.59 ? 153 ILE A N   1 
ATOM   1192 C  CA  . ILE A 1 160 ? 36.107 -13.957 -1.519  1.00 15.29 ? 153 ILE A CA  1 
ATOM   1193 C  C   . ILE A 1 160 ? 34.633 -13.683 -1.272  1.00 16.92 ? 153 ILE A C   1 
ATOM   1194 O  O   . ILE A 1 160 ? 34.249 -13.300 -0.163  1.00 17.77 ? 153 ILE A O   1 
ATOM   1195 C  CB  . ILE A 1 160 ? 36.545 -15.224 -0.769  1.00 15.36 ? 153 ILE A CB  1 
ATOM   1196 C  CG1 . ILE A 1 160 ? 38.072 -15.386 -0.727  1.00 17.54 ? 153 ILE A CG1 1 
ATOM   1197 C  CG2 . ILE A 1 160 ? 35.890 -16.418 -1.429  1.00 15.47 ? 153 ILE A CG2 1 
ATOM   1198 C  CD1 . ILE A 1 160 ? 38.733 -15.427 -2.092  1.00 17.22 ? 153 ILE A CD1 1 
ATOM   1199 N  N   . GLY A 1 161 ? 33.817 -13.868 -2.299  1.00 17.72 ? 154 GLY A N   1 
ATOM   1200 C  CA  . GLY A 1 161 ? 32.403 -13.562 -2.218  1.00 15.57 ? 154 GLY A CA  1 
ATOM   1201 C  C   . GLY A 1 161 ? 31.617 -14.605 -1.452  1.00 16.63 ? 154 GLY A C   1 
ATOM   1202 O  O   . GLY A 1 161 ? 32.161 -15.530 -0.849  1.00 18.51 ? 154 GLY A O   1 
ATOM   1203 N  N   . LYS A 1 162 ? 30.291 -14.418 -1.476  1.00 16.75 ? 155 LYS A N   1 
ATOM   1204 C  CA  . LYS A 1 162 ? 29.345 -15.311 -0.834  1.00 17.51 ? 155 LYS A CA  1 
ATOM   1205 C  C   . LYS A 1 162 ? 29.164 -16.574 -1.663  1.00 22.43 ? 155 LYS A C   1 
ATOM   1206 O  O   . LYS A 1 162 ? 29.175 -16.525 -2.898  1.00 18.82 ? 155 LYS A O   1 
ATOM   1207 C  CB  . LYS A 1 162 ? 27.985 -14.637 -0.668  1.00 19.74 ? 155 LYS A CB  1 
ATOM   1208 C  CG  . LYS A 1 162 ? 27.982 -13.425 0.229   1.00 20.23 ? 155 LYS A CG  1 
ATOM   1209 C  CD  . LYS A 1 162 ? 26.570 -12.838 0.298   1.00 26.13 ? 155 LYS A CD  1 
ATOM   1210 C  CE  . LYS A 1 162 ? 26.564 -11.602 1.186   1.00 34.34 ? 155 LYS A CE  1 
ATOM   1211 N  NZ  . LYS A 1 162 ? 27.381 -10.494 0.594   1.00 33.99 ? 155 LYS A NZ  1 
ATOM   1212 N  N   . ASN A 1 163 ? 28.978 -17.698 -0.974  1.00 19.16 ? 156 ASN A N   1 
ATOM   1213 C  CA  . ASN A 1 163 ? 28.641 -18.978 -1.606  1.00 21.60 ? 156 ASN A CA  1 
ATOM   1214 C  C   . ASN A 1 163 ? 29.668 -19.395 -2.651  1.00 20.62 ? 156 ASN A C   1 
ATOM   1215 O  O   . ASN A 1 163 ? 29.323 -19.984 -3.676  1.00 20.69 ? 156 ASN A O   1 
ATOM   1216 C  CB  . ASN A 1 163 ? 27.244 -18.915 -2.203  1.00 22.40 ? 156 ASN A CB  1 
ATOM   1217 C  CG  . ASN A 1 163 ? 26.209 -18.611 -1.141  1.00 26.87 ? 156 ASN A CG  1 
ATOM   1218 O  OD1 . ASN A 1 163 ? 26.160 -19.290 -0.110  1.00 31.39 ? 156 ASN A OD1 1 
ATOM   1219 N  ND2 . ASN A 1 163 ? 25.437 -17.562 -1.344  1.00 30.60 ? 156 ASN A ND2 1 
ATOM   1220 N  N   . VAL A 1 164 ? 30.925 -19.086 -2.384  1.00 18.55 ? 157 VAL A N   1 
ATOM   1221 C  CA  . VAL A 1 164 ? 32.053 -19.498 -3.213  1.00 14.68 ? 157 VAL A CA  1 
ATOM   1222 C  C   . VAL A 1 164 ? 32.500 -20.872 -2.738  1.00 17.60 ? 157 VAL A C   1 
ATOM   1223 O  O   . VAL A 1 164 ? 32.394 -21.217 -1.557  1.00 18.32 ? 157 VAL A O   1 
ATOM   1224 C  CB  . VAL A 1 164 ? 33.183 -18.462 -3.144  1.00 15.06 ? 157 VAL A CB  1 
ATOM   1225 C  CG1 . VAL A 1 164 ? 34.467 -19.014 -3.744  1.00 16.50 ? 157 VAL A CG1 1 
ATOM   1226 C  CG2 . VAL A 1 164 ? 32.737 -17.161 -3.826  1.00 16.56 ? 157 VAL A CG2 1 
ATOM   1227 N  N   . HIS A 1 165 ? 32.968 -21.682 -3.678  1.00 16.82 ? 158 HIS A N   1 
ATOM   1228 C  CA  . HIS A 1 165 ? 33.565 -22.975 -3.376  1.00 15.56 ? 158 HIS A CA  1 
ATOM   1229 C  C   . HIS A 1 165 ? 35.014 -22.940 -3.834  1.00 14.58 ? 158 HIS A C   1 
ATOM   1230 O  O   . HIS A 1 165 ? 35.283 -22.927 -5.032  1.00 16.32 ? 158 HIS A O   1 
ATOM   1231 C  CB  . HIS A 1 165 ? 32.795 -24.081 -4.062  1.00 18.41 ? 158 HIS A CB  1 
ATOM   1232 C  CG  . HIS A 1 165 ? 33.183 -25.453 -3.615  1.00 24.90 ? 158 HIS A CG  1 
ATOM   1233 N  ND1 . HIS A 1 165 ? 32.351 -26.537 -3.771  1.00 38.00 ? 158 HIS A ND1 1 
ATOM   1234 C  CD2 . HIS A 1 165 ? 34.299 -25.921 -3.012  1.00 34.05 ? 158 HIS A CD2 1 
ATOM   1235 C  CE1 . HIS A 1 165 ? 32.936 -27.616 -3.283  1.00 36.81 ? 158 HIS A CE1 1 
ATOM   1236 N  NE2 . HIS A 1 165 ? 34.121 -27.273 -2.819  1.00 27.47 ? 158 HIS A NE2 1 
ATOM   1237 N  N   . LEU A 1 166 ? 35.933 -22.901 -2.891  1.00 13.92 ? 159 LEU A N   1 
ATOM   1238 C  CA  . LEU A 1 166 ? 37.356 -23.015 -3.170  1.00 14.38 ? 159 LEU A CA  1 
ATOM   1239 C  C   . LEU A 1 166 ? 37.718 -24.476 -2.937  1.00 14.90 ? 159 LEU A C   1 
ATOM   1240 O  O   . LEU A 1 166 ? 37.711 -24.951 -1.797  1.00 16.14 ? 159 LEU A O   1 
ATOM   1241 C  CB  . LEU A 1 166 ? 38.193 -22.096 -2.287  1.00 13.84 ? 159 LEU A CB  1 
ATOM   1242 C  CG  . LEU A 1 166 ? 37.881 -20.607 -2.350  1.00 14.48 ? 159 LEU A CG  1 
ATOM   1243 C  CD1 . LEU A 1 166 ? 38.811 -19.812 -1.443  1.00 17.11 ? 159 LEU A CD1 1 
ATOM   1244 C  CD2 . LEU A 1 166 ? 37.965 -20.104 -3.769  1.00 16.34 ? 159 LEU A CD2 1 
ATOM   1245 N  N   . SER A 1 167 ? 37.993 -25.198 -4.015  1.00 15.87 ? 160 SER A N   1 
ATOM   1246 C  CA  . SER A 1 167 ? 38.204 -26.626 -3.908  1.00 13.35 ? 160 SER A CA  1 
ATOM   1247 C  C   . SER A 1 167 ? 39.577 -26.939 -3.323  1.00 15.10 ? 160 SER A C   1 
ATOM   1248 O  O   . SER A 1 167 ? 40.377 -26.056 -3.030  1.00 15.64 ? 160 SER A O   1 
ATOM   1249 C  CB  . SER A 1 167 ? 38.053 -27.278 -5.274  1.00 17.38 ? 160 SER A CB  1 
ATOM   1250 O  OG  . SER A 1 167 ? 36.732 -27.120 -5.778  1.00 21.92 ? 160 SER A OG  1 
ATOM   1251 N  N   . GLY A 1 168 ? 39.856 -28.233 -3.201  1.00 15.63 ? 161 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 168 ? 41.095 -28.648 -2.562  1.00 17.38 ? 161 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 168 ? 42.311 -28.080 -3.266  1.00 15.48 ? 161 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 168 ? 42.406 -28.081 -4.493  1.00 15.75 ? 161 GLY A O   1 
ATOM   1255 N  N   . GLY A 1 169 ? 43.249 -27.581 -2.469  1.00 13.45 ? 162 GLY A N   1 
ATOM   1256 C  CA  . GLY A 1 169 ? 44.522 -27.151 -3.008  1.00 17.54 ? 162 GLY A CA  1 
ATOM   1257 C  C   . GLY A 1 169 ? 44.452 -25.881 -3.823  1.00 19.34 ? 162 GLY A C   1 
ATOM   1258 O  O   . GLY A 1 169 ? 45.427 -25.549 -4.509  1.00 21.05 ? 162 GLY A O   1 
ATOM   1259 N  N   . VAL A 1 170 ? 43.349 -25.167 -3.763  1.00 15.44 ? 163 VAL A N   1 
ATOM   1260 C  CA  . VAL A 1 170 ? 43.215 -23.915 -4.501  1.00 11.21 ? 163 VAL A CA  1 
ATOM   1261 C  C   . VAL A 1 170 ? 43.969 -22.817 -3.763  1.00 15.60 ? 163 VAL A C   1 
ATOM   1262 O  O   . VAL A 1 170 ? 43.854 -22.687 -2.545  1.00 18.20 ? 163 VAL A O   1 
ATOM   1263 C  CB  . VAL A 1 170 ? 41.734 -23.555 -4.656  1.00 12.41 ? 163 VAL A CB  1 
ATOM   1264 C  CG1 . VAL A 1 170 ? 41.593 -22.068 -5.052  1.00 17.59 ? 163 VAL A CG1 1 
ATOM   1265 C  CG2 . VAL A 1 170 ? 41.116 -24.432 -5.693  1.00 15.10 ? 163 VAL A CG2 1 
ATOM   1266 N  N   . GLY A 1 171 ? 44.725 -22.018 -4.498  1.00 14.48 ? 164 GLY A N   1 
ATOM   1267 C  CA  . GLY A 1 171 ? 45.352 -20.863 -3.907  1.00 14.91 ? 164 GLY A CA  1 
ATOM   1268 C  C   . GLY A 1 171 ? 44.866 -19.567 -4.521  1.00 14.23 ? 164 GLY A C   1 
ATOM   1269 O  O   . GLY A 1 171 ? 44.876 -19.400 -5.756  1.00 13.94 ? 164 GLY A O   1 
ATOM   1270 N  N   . ILE A 1 172 ? 44.497 -18.638 -3.658  1.00 13.68 ? 165 ILE A N   1 
ATOM   1271 C  CA  . ILE A 1 172 ? 44.094 -17.284 -4.038  1.00 12.13 ? 165 ILE A CA  1 
ATOM   1272 C  C   . ILE A 1 172 ? 45.222 -16.365 -3.566  1.00 15.62 ? 165 ILE A C   1 
ATOM   1273 O  O   . ILE A 1 172 ? 45.477 -16.237 -2.359  1.00 16.99 ? 165 ILE A O   1 
ATOM   1274 C  CB  . ILE A 1 172 ? 42.742 -16.901 -3.420  1.00 14.30 ? 165 ILE A CB  1 
ATOM   1275 C  CG1 . ILE A 1 172 ? 41.677 -17.954 -3.718  1.00 12.91 ? 165 ILE A CG1 1 
ATOM   1276 C  CG2 . ILE A 1 172 ? 42.305 -15.521 -3.962  1.00 17.10 ? 165 ILE A CG2 1 
ATOM   1277 C  CD1 . ILE A 1 172 ? 41.447 -18.244 -5.161  1.00 13.33 ? 165 ILE A CD1 1 
ATOM   1278 N  N   . GLY A 1 173 ? 45.926 -15.763 -4.512  1.00 13.84 ? 166 GLY A N   1 
ATOM   1279 C  CA  . GLY A 1 173 ? 47.180 -15.104 -4.191  1.00 16.30 ? 166 GLY A CA  1 
ATOM   1280 C  C   . GLY A 1 173 ? 46.990 -13.792 -3.460  1.00 15.80 ? 166 GLY A C   1 
ATOM   1281 O  O   . GLY A 1 173 ? 46.059 -13.028 -3.727  1.00 17.21 ? 166 GLY A O   1 
ATOM   1282 N  N   . GLY A 1 174 ? 47.921 -13.523 -2.518  1.00 16.83 ? 167 GLY A N   1 
ATOM   1283 C  CA  . GLY A 1 174 ? 47.891 -12.281 -1.789  1.00 15.98 ? 167 GLY A CA  1 
ATOM   1284 C  C   . GLY A 1 174 ? 48.478 -11.128 -2.577  1.00 17.29 ? 167 GLY A C   1 
ATOM   1285 O  O   . GLY A 1 174 ? 49.314 -11.282 -3.468  1.00 17.90 ? 167 GLY A O   1 
ATOM   1286 N  N   . VAL A 1 175 ? 48.025 -9.937  -2.203  1.00 17.02 ? 168 VAL A N   1 
ATOM   1287 C  CA  . VAL A 1 175 ? 48.482 -8.695  -2.817  1.00 18.76 ? 168 VAL A CA  1 
ATOM   1288 C  C   . VAL A 1 175 ? 48.511 -7.665  -1.699  1.00 26.31 ? 168 VAL A C   1 
ATOM   1289 O  O   . VAL A 1 175 ? 47.493 -7.044  -1.384  1.00 31.66 ? 168 VAL A O   1 
ATOM   1290 C  CB  . VAL A 1 175 ? 47.574 -8.203  -3.959  1.00 20.78 ? 168 VAL A CB  1 
ATOM   1291 C  CG1 . VAL A 1 175 ? 48.147 -6.918  -4.584  1.00 23.45 ? 168 VAL A CG1 1 
ATOM   1292 C  CG2 . VAL A 1 175 ? 47.349 -9.287  -4.996  1.00 21.54 ? 168 VAL A CG2 1 
ATOM   1293 N  N   . LEU A 1 176 ? 49.646 -7.501  -1.054  1.00 25.22 ? 169 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 176 ? 49.801 -6.412  -0.088  1.00 25.72 ? 169 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 176 ? 50.534 -5.257  -0.759  1.00 32.08 ? 169 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 176 ? 49.961 -4.180  -0.943  1.00 34.97 ? 169 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 176 ? 50.491 -6.960  1.169   1.00 31.43 ? 169 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 176 ? 50.296 -6.293  2.531   1.00 38.46 ? 169 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 176 ? 48.882 -5.820  2.831   1.00 26.30 ? 169 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 176 ? 50.745 -7.294  3.599   1.00 36.35 ? 169 LEU A CD2 1 
ATOM   1301 N  N   . GLU A 1 177 ? 51.754 -5.494  -1.233  1.00 32.72 ? 170 GLU A N   1 
ATOM   1302 C  CA  . GLU A 1 177 ? 52.414 -4.531  -2.104  1.00 36.53 ? 170 GLU A CA  1 
ATOM   1303 C  C   . GLU A 1 177 ? 52.286 -4.975  -3.561  1.00 36.65 ? 170 GLU A C   1 
ATOM   1304 O  O   . GLU A 1 177 ? 52.148 -6.168  -3.844  1.00 37.10 ? 170 GLU A O   1 
ATOM   1305 C  CB  . GLU A 1 177 ? 53.898 -4.384  -1.738  1.00 46.44 ? 170 GLU A CB  1 
ATOM   1306 C  CG  . GLU A 1 177 ? 54.167 -3.737  -0.360  1.00 46.08 ? 170 GLU A CG  1 
ATOM   1307 C  CD  . GLU A 1 177 ? 54.541 -2.258  -0.437  1.00 55.20 ? 170 GLU A CD  1 
ATOM   1308 O  OE1 . GLU A 1 177 ? 54.235 -1.611  -1.463  1.00 59.53 ? 170 GLU A OE1 1 
ATOM   1309 O  OE2 . GLU A 1 177 ? 55.146 -1.731  0.530   1.00 54.54 ? 170 GLU A OE2 1 
ATOM   1310 N  N   . PRO A 1 178 ? 52.270 -4.055  -4.521  1.00 35.80 ? 171 PRO A N   1 
ATOM   1311 C  CA  . PRO A 1 178 ? 52.288 -2.595  -4.393  1.00 37.01 ? 171 PRO A CA  1 
ATOM   1312 C  C   . PRO A 1 178 ? 51.030 -2.081  -3.713  1.00 28.05 ? 171 PRO A C   1 
ATOM   1313 O  O   . PRO A 1 178 ? 49.962 -2.668  -3.849  1.00 30.05 ? 171 PRO A O   1 
ATOM   1314 C  CB  . PRO A 1 178 ? 52.373 -2.107  -5.852  1.00 45.24 ? 171 PRO A CB  1 
ATOM   1315 C  CG  . PRO A 1 178 ? 52.780 -3.298  -6.655  1.00 38.64 ? 171 PRO A CG  1 
ATOM   1316 C  CD  . PRO A 1 178 ? 52.222 -4.474  -5.932  1.00 36.91 ? 171 PRO A CD  1 
ATOM   1317 N  N   . LEU A 1 179 ? 51.136 -0.961  -2.995  1.00 32.06 ? 172 LEU A N   1 
ATOM   1318 C  CA  . LEU A 1 179 ? 49.992 -0.465  -2.238  1.00 32.43 ? 172 LEU A CA  1 
ATOM   1319 C  C   . LEU A 1 179 ? 48.795 -0.206  -3.143  1.00 25.14 ? 172 LEU A C   1 
ATOM   1320 O  O   . LEU A 1 179 ? 47.645 -0.454  -2.759  1.00 27.44 ? 172 LEU A O   1 
ATOM   1321 C  CB  . LEU A 1 179 ? 50.392 0.814   -1.504  1.00 26.83 ? 172 LEU A CB  1 
ATOM   1322 C  CG  . LEU A 1 179 ? 51.455 0.593   -0.431  1.00 28.72 ? 172 LEU A CG  1 
ATOM   1323 C  CD1 . LEU A 1 179 ? 51.897 1.909   0.162   1.00 35.01 ? 172 LEU A CD1 1 
ATOM   1324 C  CD2 . LEU A 1 179 ? 50.890 -0.301  0.656   1.00 30.44 ? 172 LEU A CD2 1 
ATOM   1325 N  N   . GLN A 1 180 ? 49.053 0.304   -4.350  1.00 27.46 ? 173 GLN A N   1 
ATOM   1326 C  CA  . GLN A 1 180 ? 47.987 0.719   -5.247  1.00 27.12 ? 173 GLN A CA  1 
ATOM   1327 C  C   . GLN A 1 180 ? 47.264 -0.454  -5.895  1.00 28.97 ? 173 GLN A C   1 
ATOM   1328 O  O   . GLN A 1 180 ? 46.157 -0.259  -6.407  1.00 31.61 ? 173 GLN A O   1 
ATOM   1329 C  CB  . GLN A 1 180 ? 48.572 1.644   -6.323  1.00 36.62 ? 173 GLN A CB  1 
ATOM   1330 C  CG  . GLN A 1 180 ? 49.716 1.025   -7.141  1.00 44.14 ? 173 GLN A CG  1 
ATOM   1331 C  CD  . GLN A 1 180 ? 51.134 1.394   -6.651  1.00 59.73 ? 173 GLN A CD  1 
ATOM   1332 O  OE1 . GLN A 1 180 ? 51.440 1.364   -5.450  1.00 44.41 ? 173 GLN A OE1 1 
ATOM   1333 N  NE2 . GLN A 1 180 ? 52.007 1.735   -7.600  1.00 68.82 ? 173 GLN A NE2 1 
ATOM   1334 N  N   . ALA A 1 181 ? 47.820 -1.659  -5.823  1.00 26.88 ? 174 ALA A N   1 
ATOM   1335 C  CA  . ALA A 1 181 ? 47.286 -2.794  -6.562  1.00 24.72 ? 174 ALA A CA  1 
ATOM   1336 C  C   . ALA A 1 181 ? 46.040 -3.371  -5.898  1.00 34.73 ? 174 ALA A C   1 
ATOM   1337 O  O   . ALA A 1 181 ? 46.021 -3.598  -4.683  1.00 25.24 ? 174 ALA A O   1 
ATOM   1338 C  CB  . ALA A 1 181 ? 48.366 -3.870  -6.676  1.00 29.72 ? 174 ALA A CB  1 
ATOM   1339 N  N   . ASN A 1 182 ? 45.002 -3.635  -6.694  1.00 28.15 ? 175 ASN A N   1 
ATOM   1340 C  CA  . ASN A 1 182 ? 43.827 -4.293  -6.140  1.00 23.89 ? 175 ASN A CA  1 
ATOM   1341 C  C   . ASN A 1 182 ? 44.158 -5.745  -5.786  1.00 19.64 ? 175 ASN A C   1 
ATOM   1342 O  O   . ASN A 1 182 ? 44.982 -6.399  -6.440  1.00 20.57 ? 175 ASN A O   1 
ATOM   1343 C  CB  . ASN A 1 182 ? 42.636 -4.259  -7.104  1.00 27.79 ? 175 ASN A CB  1 
ATOM   1344 C  CG  . ASN A 1 182 ? 41.929 -2.886  -7.144  1.00 45.50 ? 175 ASN A CG  1 
ATOM   1345 O  OD1 . ASN A 1 182 ? 42.189 -2.003  -6.319  1.00 43.54 ? 175 ASN A OD1 1 
ATOM   1346 N  ND2 . ASN A 1 182 ? 41.022 -2.715  -8.105  1.00 44.02 ? 175 ASN A ND2 1 
ATOM   1347 N  N   . PRO A 1 183 ? 43.543 -6.270  -4.741  1.00 18.20 ? 176 PRO A N   1 
ATOM   1348 C  CA  . PRO A 1 183 ? 43.768 -7.674  -4.376  1.00 15.14 ? 176 PRO A CA  1 
ATOM   1349 C  C   . PRO A 1 183 ? 43.049 -8.611  -5.334  1.00 15.49 ? 176 PRO A C   1 
ATOM   1350 O  O   . PRO A 1 183 ? 42.252 -8.205  -6.177  1.00 17.23 ? 176 PRO A O   1 
ATOM   1351 C  CB  . PRO A 1 183 ? 43.189 -7.765  -2.969  1.00 18.45 ? 176 PRO A CB  1 
ATOM   1352 C  CG  . PRO A 1 183 ? 42.139 -6.753  -2.945  1.00 18.66 ? 176 PRO A CG  1 
ATOM   1353 C  CD  . PRO A 1 183 ? 42.602 -5.606  -3.825  1.00 20.51 ? 176 PRO A CD  1 
ATOM   1354 N  N   . THR A 1 184 ? 43.361 -9.891  -5.196  1.00 15.21 ? 177 THR A N   1 
ATOM   1355 C  CA  . THR A 1 184 ? 42.692 -10.923 -5.964  1.00 13.53 ? 177 THR A CA  1 
ATOM   1356 C  C   . THR A 1 184 ? 41.248 -11.022 -5.498  1.00 15.52 ? 177 THR A C   1 
ATOM   1357 O  O   . THR A 1 184 ? 40.972 -10.959 -4.296  1.00 14.52 ? 177 THR A O   1 
ATOM   1358 C  CB  . THR A 1 184 ? 43.420 -12.251 -5.777  1.00 15.51 ? 177 THR A CB  1 
ATOM   1359 O  OG1 . THR A 1 184 ? 44.812 -12.066 -6.078  1.00 15.65 ? 177 THR A OG1 1 
ATOM   1360 C  CG2 . THR A 1 184 ? 42.851 -13.290 -6.692  1.00 15.23 ? 177 THR A CG2 1 
ATOM   1361 N  N   . ILE A 1 185 ? 40.327 -11.129 -6.460  1.00 15.54 ? 178 ILE A N   1 
ATOM   1362 C  CA  . ILE A 1 185 ? 38.893 -11.057 -6.185  1.00 16.73 ? 178 ILE A CA  1 
ATOM   1363 C  C   . ILE A 1 185 ? 38.227 -12.291 -6.780  1.00 14.80 ? 178 ILE A C   1 
ATOM   1364 O  O   . ILE A 1 185 ? 38.363 -12.536 -7.981  1.00 15.25 ? 178 ILE A O   1 
ATOM   1365 C  CB  . ILE A 1 185 ? 38.242 -9.803  -6.806  1.00 17.54 ? 178 ILE A CB  1 
ATOM   1366 C  CG1 . ILE A 1 185 ? 38.872 -8.496  -6.340  1.00 22.56 ? 178 ILE A CG1 1 
ATOM   1367 C  CG2 . ILE A 1 185 ? 36.755 -9.813  -6.542  1.00 19.66 ? 178 ILE A CG2 1 
ATOM   1368 C  CD1 . ILE A 1 185 ? 38.785 -8.275  -4.907  1.00 23.55 ? 178 ILE A CD1 1 
ATOM   1369 N  N   . ILE A 1 186 ? 37.479 -13.022 -5.958  1.00 15.87 ? 179 ILE A N   1 
ATOM   1370 C  CA  . ILE A 1 186 ? 36.607 -14.117 -6.390  1.00 13.06 ? 179 ILE A CA  1 
ATOM   1371 C  C   . ILE A 1 186 ? 35.195 -13.662 -6.029  1.00 14.42 ? 179 ILE A C   1 
ATOM   1372 O  O   . ILE A 1 186 ? 34.870 -13.534 -4.843  1.00 16.82 ? 179 ILE A O   1 
ATOM   1373 C  CB  . ILE A 1 186 ? 36.944 -15.448 -5.711  1.00 15.06 ? 179 ILE A CB  1 
ATOM   1374 C  CG1 . ILE A 1 186 ? 38.435 -15.790 -5.859  1.00 16.55 ? 179 ILE A CG1 1 
ATOM   1375 C  CG2 . ILE A 1 186 ? 36.079 -16.558 -6.296  1.00 14.44 ? 179 ILE A CG2 1 
ATOM   1376 C  CD1 . ILE A 1 186 ? 38.908 -16.018 -7.300  1.00 17.49 ? 179 ILE A CD1 1 
ATOM   1377 N  N   . GLU A 1 187 ? 34.369 -13.400 -7.031  1.00 14.43 ? 180 GLU A N   1 
ATOM   1378 C  CA  . GLU A 1 187 ? 33.055 -12.826 -6.762  1.00 16.25 ? 180 GLU A CA  1 
ATOM   1379 C  C   . GLU A 1 187 ? 32.055 -13.904 -6.359  1.00 18.15 ? 180 GLU A C   1 
ATOM   1380 O  O   . GLU A 1 187 ? 32.365 -15.084 -6.301  1.00 17.50 ? 180 GLU A O   1 
ATOM   1381 C  CB  . GLU A 1 187 ? 32.590 -12.029 -7.967  1.00 17.76 ? 180 GLU A CB  1 
ATOM   1382 C  CG  . GLU A 1 187 ? 33.323 -10.696 -8.097  1.00 18.34 ? 180 GLU A CG  1 
ATOM   1383 C  CD  . GLU A 1 187 ? 32.731 -9.779  -9.141  1.00 22.99 ? 180 GLU A CD  1 
ATOM   1384 O  OE1 . GLU A 1 187 ? 31.869 -10.231 -9.948  1.00 21.54 ? 180 GLU A OE1 1 
ATOM   1385 O  OE2 . GLU A 1 187 ? 33.107 -8.574  -9.154  1.00 26.41 ? 180 GLU A OE2 1 
ATOM   1386 N  N   . ASP A 1 188 ? 30.826 -13.480 -6.051  1.00 18.39 ? 181 ASP A N   1 
ATOM   1387 C  CA  . ASP A 1 188 ? 29.842 -14.402 -5.505  1.00 20.38 ? 181 ASP A CA  1 
ATOM   1388 C  C   . ASP A 1 188 ? 29.610 -15.611 -6.411  1.00 18.75 ? 181 ASP A C   1 
ATOM   1389 O  O   . ASP A 1 188 ? 29.595 -15.507 -7.647  1.00 18.73 ? 181 ASP A O   1 
ATOM   1390 C  CB  . ASP A 1 188 ? 28.487 -13.698 -5.309  1.00 19.65 ? 181 ASP A CB  1 
ATOM   1391 C  CG  . ASP A 1 188 ? 28.500 -12.640 -4.211  1.00 24.08 ? 181 ASP A CG  1 
ATOM   1392 O  OD1 . ASP A 1 188 ? 29.499 -12.504 -3.489  1.00 20.83 ? 181 ASP A OD1 1 
ATOM   1393 O  OD2 . ASP A 1 188 ? 27.481 -11.939 -4.068  1.00 26.45 ? 181 ASP A OD2 1 
ATOM   1394 N  N   . ASN A 1 189 ? 29.382 -16.752 -5.761  1.00 18.56 ? 182 ASN A N   1 
ATOM   1395 C  CA  A ASN A 1 189 ? 28.886 -17.994 -6.350  0.50 19.81 ? 182 ASN A CA  1 
ATOM   1396 C  CA  B ASN A 1 189 ? 28.858 -17.952 -6.402  0.50 19.72 ? 182 ASN A CA  1 
ATOM   1397 C  C   . ASN A 1 189 ? 29.850 -18.621 -7.343  1.00 23.19 ? 182 ASN A C   1 
ATOM   1398 O  O   . ASN A 1 189 ? 29.435 -19.426 -8.187  1.00 27.12 ? 182 ASN A O   1 
ATOM   1399 C  CB  A ASN A 1 189 ? 27.524 -17.800 -7.016  0.50 20.87 ? 182 ASN A CB  1 
ATOM   1400 C  CB  B ASN A 1 189 ? 27.569 -17.666 -7.188  0.50 21.36 ? 182 ASN A CB  1 
ATOM   1401 C  CG  A ASN A 1 189 ? 26.761 -19.098 -7.155  0.50 22.50 ? 182 ASN A CG  1 
ATOM   1402 C  CG  B ASN A 1 189 ? 26.447 -17.155 -6.317  0.50 24.09 ? 182 ASN A CG  1 
ATOM   1403 O  OD1 A ASN A 1 189 ? 26.861 -19.981 -6.301  0.50 28.14 ? 182 ASN A OD1 1 
ATOM   1404 O  OD1 B ASN A 1 189 ? 25.860 -16.106 -6.589  0.50 34.62 ? 182 ASN A OD1 1 
ATOM   1405 N  ND2 A ASN A 1 189 ? 26.003 -19.227 -8.228  0.50 29.67 ? 182 ASN A ND2 1 
ATOM   1406 N  ND2 B ASN A 1 189 ? 26.118 -17.907 -5.281  0.50 23.15 ? 182 ASN A ND2 1 
ATOM   1407 N  N   . CYS A 1 190 ? 31.131 -18.286 -7.262  1.00 17.47 ? 183 CYS A N   1 
ATOM   1408 C  CA  . CYS A 1 190 ? 32.099 -18.931 -8.132  1.00 16.18 ? 183 CYS A CA  1 
ATOM   1409 C  C   . CYS A 1 190 ? 32.453 -20.323 -7.622  1.00 18.13 ? 183 CYS A C   1 
ATOM   1410 O  O   . CYS A 1 190 ? 32.422 -20.592 -6.421  1.00 19.60 ? 183 CYS A O   1 
ATOM   1411 C  CB  . CYS A 1 190 ? 33.381 -18.114 -8.234  1.00 16.97 ? 183 CYS A CB  1 
ATOM   1412 S  SG  . CYS A 1 190 ? 33.124 -16.615 -9.193  1.00 20.19 ? 183 CYS A SG  1 
ATOM   1413 N  N   . PHE A 1 191 ? 32.790 -21.202 -8.554  1.00 18.01 ? 184 PHE A N   1 
ATOM   1414 C  CA  . PHE A 1 191 ? 33.369 -22.499 -8.234  1.00 16.86 ? 184 PHE A CA  1 
ATOM   1415 C  C   . PHE A 1 191 ? 34.793 -22.500 -8.758  1.00 16.33 ? 184 PHE A C   1 
ATOM   1416 O  O   . PHE A 1 191 ? 35.010 -22.226 -9.934  1.00 16.22 ? 184 PHE A O   1 
ATOM   1417 C  CB  . PHE A 1 191 ? 32.575 -23.635 -8.868  1.00 18.80 ? 184 PHE A CB  1 
ATOM   1418 C  CG  . PHE A 1 191 ? 33.215 -24.995 -8.677  1.00 21.80 ? 184 PHE A CG  1 
ATOM   1419 C  CD1 . PHE A 1 191 ? 34.155 -25.466 -9.588  1.00 21.40 ? 184 PHE A CD1 1 
ATOM   1420 C  CD2 . PHE A 1 191 ? 32.893 -25.780 -7.596  1.00 26.52 ? 184 PHE A CD2 1 
ATOM   1421 C  CE1 . PHE A 1 191 ? 34.744 -26.704 -9.418  1.00 22.85 ? 184 PHE A CE1 1 
ATOM   1422 C  CE2 . PHE A 1 191 ? 33.485 -27.019 -7.425  1.00 27.00 ? 184 PHE A CE2 1 
ATOM   1423 C  CZ  . PHE A 1 191 ? 34.413 -27.467 -8.340  1.00 21.97 ? 184 PHE A CZ  1 
ATOM   1424 N  N   . ILE A 1 192 ? 35.768 -22.780 -7.890  1.00 14.39 ? 185 ILE A N   1 
ATOM   1425 C  CA  . ILE A 1 192 ? 37.177 -22.810 -8.298  1.00 16.68 ? 185 ILE A CA  1 
ATOM   1426 C  C   . ILE A 1 192 ? 37.656 -24.247 -8.100  1.00 14.96 ? 185 ILE A C   1 
ATOM   1427 O  O   . ILE A 1 192 ? 37.737 -24.730 -6.959  1.00 16.12 ? 185 ILE A O   1 
ATOM   1428 C  CB  . ILE A 1 192 ? 38.031 -21.821 -7.506  1.00 15.25 ? 185 ILE A CB  1 
ATOM   1429 C  CG1 . ILE A 1 192 ? 37.429 -20.394 -7.472  1.00 17.13 ? 185 ILE A CG1 1 
ATOM   1430 C  CG2 . ILE A 1 192 ? 39.461 -21.767 -8.060  1.00 17.03 ? 185 ILE A CG2 1 
ATOM   1431 C  CD1 . ILE A 1 192 ? 37.273 -19.730 -8.816  1.00 20.37 ? 185 ILE A CD1 1 
ATOM   1432 N  N   . GLY A 1 193 ? 37.946 -24.934 -9.209  1.00 16.20 ? 186 GLY A N   1 
ATOM   1433 C  CA  . GLY A 1 193 ? 38.268 -26.342 -9.150  1.00 17.68 ? 186 GLY A CA  1 
ATOM   1434 C  C   . GLY A 1 193 ? 39.627 -26.624 -8.539  1.00 15.46 ? 186 GLY A C   1 
ATOM   1435 O  O   . GLY A 1 193 ? 40.498 -25.757 -8.476  1.00 17.12 ? 186 GLY A O   1 
ATOM   1436 N  N   . ALA A 1 194 ? 39.800 -27.885 -8.131  1.00 16.74 ? 187 ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 194 ? 40.953 -28.293 -7.343  1.00 17.53 ? 187 ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 194 ? 42.254 -27.928 -8.037  1.00 17.98 ? 187 ALA A C   1 
ATOM   1439 O  O   . ALA A 1 194 ? 42.389 -28.044 -9.262  1.00 18.18 ? 187 ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 194 ? 40.923 -29.797 -7.078  1.00 20.71 ? 187 ALA A CB  1 
ATOM   1441 N  N   . ARG A 1 195 ? 43.221 -27.517 -7.228  1.00 17.33 ? 188 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 195 ? 44.583 -27.160 -7.630  1.00 17.39 ? 188 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 195 ? 44.662 -25.879 -8.447  1.00 21.36 ? 188 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 195 ? 45.763 -25.490 -8.837  1.00 26.41 ? 188 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 195 ? 45.287 -28.267 -8.442  1.00 25.47 ? 188 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 195 ? 45.202 -29.649 -7.867  1.00 34.94 ? 188 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 195 ? 45.888 -29.783 -6.510  1.00 44.57 ? 188 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 195 ? 44.954 -30.372 -5.558  1.00 48.69 ? 188 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 195 ? 45.218 -30.621 -4.283  1.00 44.83 ? 188 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 195 ? 46.410 -30.372 -3.763  1.00 51.76 ? 188 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 195 ? 44.253 -31.101 -3.505  1.00 35.06 ? 188 ARG A NH2 1 
ATOM   1452 N  N   . SER A 1 196 ? 43.549 -25.208 -8.733  1.00 17.34 ? 189 SER A N   1 
ATOM   1453 C  CA  . SER A 1 196 ? 43.627 -23.952 -9.456  1.00 16.67 ? 189 SER A CA  1 
ATOM   1454 C  C   . SER A 1 196 ? 44.305 -22.870 -8.613  1.00 15.05 ? 189 SER A C   1 
ATOM   1455 O  O   . SER A 1 196 ? 44.417 -22.971 -7.392  1.00 16.95 ? 189 SER A O   1 
ATOM   1456 C  CB  . SER A 1 196 ? 42.241 -23.489 -9.874  1.00 17.70 ? 189 SER A CB  1 
ATOM   1457 O  OG  . SER A 1 196 ? 41.754 -24.352 -10.889 1.00 20.67 ? 189 SER A OG  1 
ATOM   1458 N  N   . GLU A 1 197 ? 44.802 -21.842 -9.299  1.00 14.26 ? 190 GLU A N   1 
ATOM   1459 C  CA  . GLU A 1 197 ? 45.476 -20.738 -8.634  1.00 17.47 ? 190 GLU A CA  1 
ATOM   1460 C  C   . GLU A 1 197 ? 45.030 -19.467 -9.331  1.00 16.77 ? 190 GLU A C   1 
ATOM   1461 O  O   . GLU A 1 197 ? 44.981 -19.426 -10.563 1.00 18.23 ? 190 GLU A O   1 
ATOM   1462 C  CB  . GLU A 1 197 ? 46.994 -20.897 -8.688  1.00 23.08 ? 190 GLU A CB  1 
ATOM   1463 C  CG  . GLU A 1 197 ? 47.770 -19.856 -7.850  1.00 37.87 ? 190 GLU A CG  1 
ATOM   1464 C  CD  . GLU A 1 197 ? 48.000 -20.243 -6.406  1.00 24.57 ? 190 GLU A CD  1 
ATOM   1465 O  OE1 . GLU A 1 197 ? 47.905 -21.440 -6.064  1.00 32.91 ? 190 GLU A OE1 1 
ATOM   1466 O  OE2 . GLU A 1 197 ? 48.308 -19.331 -5.573  1.00 42.96 ? 190 GLU A OE2 1 
ATOM   1467 N  N   . VAL A 1 198 ? 44.633 -18.464 -8.554  1.00 14.97 ? 191 VAL A N   1 
ATOM   1468 C  CA  . VAL A 1 198 ? 44.233 -17.157 -9.068  1.00 13.73 ? 191 VAL A CA  1 
ATOM   1469 C  C   . VAL A 1 198 ? 45.012 -16.148 -8.244  1.00 13.01 ? 191 VAL A C   1 
ATOM   1470 O  O   . VAL A 1 198 ? 44.888 -16.132 -7.013  1.00 13.44 ? 191 VAL A O   1 
ATOM   1471 C  CB  . VAL A 1 198 ? 42.721 -16.911 -8.948  1.00 15.69 ? 191 VAL A CB  1 
ATOM   1472 C  CG1 . VAL A 1 198 ? 42.343 -15.574 -9.558  1.00 14.83 ? 191 VAL A CG1 1 
ATOM   1473 C  CG2 . VAL A 1 198 ? 41.936 -18.062 -9.572  1.00 17.04 ? 191 VAL A CG2 1 
ATOM   1474 N  N   . VAL A 1 199 ? 45.887 -15.376 -8.898  1.00 14.32 ? 192 VAL A N   1 
ATOM   1475 C  CA  . VAL A 1 199 ? 46.855 -14.547 -8.195  1.00 14.30 ? 192 VAL A CA  1 
ATOM   1476 C  C   . VAL A 1 199 ? 46.887 -13.144 -8.790  1.00 14.77 ? 192 VAL A C   1 
ATOM   1477 O  O   . VAL A 1 199 ? 46.284 -12.864 -9.828  1.00 15.13 ? 192 VAL A O   1 
ATOM   1478 C  CB  . VAL A 1 199 ? 48.284 -15.157 -8.233  1.00 15.05 ? 192 VAL A CB  1 
ATOM   1479 C  CG1 . VAL A 1 199 ? 48.269 -16.556 -7.655  1.00 17.06 ? 192 VAL A CG1 1 
ATOM   1480 C  CG2 . VAL A 1 199 ? 48.824 -15.139 -9.655  1.00 17.42 ? 192 VAL A CG2 1 
ATOM   1481 N  N   . GLU A 1 200 ? 47.605 -12.261 -8.088  1.00 16.03 ? 193 GLU A N   1 
ATOM   1482 C  CA  . GLU A 1 200 ? 48.051 -10.981 -8.653  1.00 17.88 ? 193 GLU A CA  1 
ATOM   1483 C  C   . GLU A 1 200 ? 46.873 -10.093 -9.046  1.00 20.19 ? 193 GLU A C   1 
ATOM   1484 O  O   . GLU A 1 200 ? 46.955 -9.334  -10.020 1.00 19.71 ? 193 GLU A O   1 
ATOM   1485 C  CB  . GLU A 1 200 ? 48.969 -11.210 -9.871  1.00 21.87 ? 193 GLU A CB  1 
ATOM   1486 C  CG  . GLU A 1 200 ? 50.008 -10.128 -10.149 1.00 38.24 ? 193 GLU A CG  1 
ATOM   1487 C  CD  . GLU A 1 200 ? 50.626 -10.214 -11.576 1.00 46.69 ? 193 GLU A CD  1 
ATOM   1488 O  OE1 . GLU A 1 200 ? 51.133 -9.130  -12.075 1.00 33.54 ? 193 GLU A OE1 1 
ATOM   1489 O  OE2 . GLU A 1 200 ? 50.627 -11.323 -12.184 1.00 25.03 ? 193 GLU A OE2 1 
ATOM   1490 N  N   . GLY A 1 201 ? 45.776 -10.159 -8.286  1.00 16.93 ? 194 GLY A N   1 
ATOM   1491 C  CA  . GLY A 1 201 ? 44.676 -9.239  -8.509  1.00 17.92 ? 194 GLY A CA  1 
ATOM   1492 C  C   . GLY A 1 201 ? 43.792 -9.573  -9.686  1.00 16.12 ? 194 GLY A C   1 
ATOM   1493 O  O   . GLY A 1 201 ? 43.023 -8.715  -10.127 1.00 17.84 ? 194 GLY A O   1 
ATOM   1494 N  N   . VAL A 1 202 ? 43.908 -10.775 -10.235 1.00 14.52 ? 195 VAL A N   1 
ATOM   1495 C  CA  . VAL A 1 202 ? 42.934 -11.247 -11.207 1.00 14.67 ? 195 VAL A CA  1 
ATOM   1496 C  C   . VAL A 1 202 ? 41.568 -11.193 -10.553 1.00 16.71 ? 195 VAL A C   1 
ATOM   1497 O  O   . VAL A 1 202 ? 41.438 -11.414 -9.341  1.00 14.95 ? 195 VAL A O   1 
ATOM   1498 C  CB  . VAL A 1 202 ? 43.294 -12.667 -11.671 1.00 16.00 ? 195 VAL A CB  1 
ATOM   1499 C  CG1 . VAL A 1 202 ? 42.150 -13.304 -12.458 1.00 16.39 ? 195 VAL A CG1 1 
ATOM   1500 C  CG2 . VAL A 1 202 ? 44.573 -12.584 -12.506 1.00 16.22 ? 195 VAL A CG2 1 
ATOM   1501 N  N   . VAL A 1 203 ? 40.558 -10.804 -11.336 1.00 15.73 ? 196 VAL A N   1 
ATOM   1502 C  CA  . VAL A 1 203 ? 39.167 -10.771 -10.889 1.00 15.19 ? 196 VAL A CA  1 
ATOM   1503 C  C   . VAL A 1 203 ? 38.418 -11.908 -11.582 1.00 15.50 ? 196 VAL A C   1 
ATOM   1504 O  O   . VAL A 1 203 ? 38.375 -11.988 -12.819 1.00 16.97 ? 196 VAL A O   1 
ATOM   1505 C  CB  . VAL A 1 203 ? 38.503 -9.426  -11.196 1.00 16.75 ? 196 VAL A CB  1 
ATOM   1506 C  CG1 . VAL A 1 203 ? 37.031 -9.452  -10.770 1.00 18.96 ? 196 VAL A CG1 1 
ATOM   1507 C  CG2 . VAL A 1 203 ? 39.221 -8.299  -10.511 1.00 18.88 ? 196 VAL A CG2 1 
ATOM   1508 N  N   . VAL A 1 204 ? 37.799 -12.767 -10.790 1.00 14.73 ? 197 VAL A N   1 
ATOM   1509 C  CA  . VAL A 1 204 ? 36.895 -13.781 -11.309 1.00 14.16 ? 197 VAL A CA  1 
ATOM   1510 C  C   . VAL A 1 204 ? 35.480 -13.312 -11.004 1.00 16.06 ? 197 VAL A C   1 
ATOM   1511 O  O   . VAL A 1 204 ? 35.073 -13.232 -9.837  1.00 15.71 ? 197 VAL A O   1 
ATOM   1512 C  CB  . VAL A 1 204 ? 37.187 -15.154 -10.698 1.00 13.06 ? 197 VAL A CB  1 
ATOM   1513 C  CG1 . VAL A 1 204 ? 36.228 -16.183 -11.278 1.00 16.06 ? 197 VAL A CG1 1 
ATOM   1514 C  CG2 . VAL A 1 204 ? 38.645 -15.579 -10.969 1.00 15.03 ? 197 VAL A CG2 1 
ATOM   1515 N  N   . GLU A 1 205 ? 34.724 -12.937 -12.046 1.00 16.01 ? 198 GLU A N   1 
ATOM   1516 C  CA  . GLU A 1 205 ? 33.419 -12.352 -11.822 1.00 16.74 ? 198 GLU A CA  1 
ATOM   1517 C  C   . GLU A 1 205 ? 32.393 -13.420 -11.466 1.00 18.11 ? 198 GLU A C   1 
ATOM   1518 O  O   . GLU A 1 205 ? 32.613 -14.614 -11.672 1.00 17.52 ? 198 GLU A O   1 
ATOM   1519 C  CB  . GLU A 1 205 ? 32.956 -11.588 -13.063 1.00 19.56 ? 198 GLU A CB  1 
ATOM   1520 C  CG  . GLU A 1 205 ? 33.834 -10.392 -13.377 1.00 19.08 ? 198 GLU A CG  1 
ATOM   1521 C  CD  . GLU A 1 205 ? 33.293 -9.573  -14.523 1.00 30.21 ? 198 GLU A CD  1 
ATOM   1522 O  OE1 . GLU A 1 205 ? 32.325 -10.014 -15.182 1.00 27.14 ? 198 GLU A OE1 1 
ATOM   1523 O  OE2 . GLU A 1 205 ? 33.817 -8.468  -14.747 1.00 30.60 ? 198 GLU A OE2 1 
ATOM   1524 N  N   . GLU A 1 206 ? 31.256 -12.954 -10.950 1.00 18.48 ? 199 GLU A N   1 
ATOM   1525 C  CA  . GLU A 1 206 ? 30.278 -13.810 -10.302 1.00 19.16 ? 199 GLU A CA  1 
ATOM   1526 C  C   . GLU A 1 206 ? 29.793 -14.922 -11.224 1.00 20.20 ? 199 GLU A C   1 
ATOM   1527 O  O   . GLU A 1 206 ? 29.710 -14.770 -12.448 1.00 19.96 ? 199 GLU A O   1 
ATOM   1528 C  CB  . GLU A 1 206 ? 29.081 -12.985 -9.814  1.00 21.96 ? 199 GLU A CB  1 
ATOM   1529 C  CG  . GLU A 1 206 ? 28.411 -12.155 -10.857 1.00 26.91 ? 199 GLU A CG  1 
ATOM   1530 C  CD  . GLU A 1 206 ? 27.163 -11.450 -10.320 1.00 40.76 ? 199 GLU A CD  1 
ATOM   1531 O  OE1 . GLU A 1 206 ? 26.215 -11.250 -11.105 1.00 54.78 ? 199 GLU A OE1 1 
ATOM   1532 O  OE2 . GLU A 1 206 ? 27.120 -11.110 -9.114  1.00 46.01 ? 199 GLU A OE2 1 
ATOM   1533 N  N   . ASN A 1 207 ? 29.486 -16.060 -10.609 1.00 19.39 ? 200 ASN A N   1 
ATOM   1534 C  CA  . ASN A 1 207 ? 28.905 -17.233 -11.249 1.00 19.29 ? 200 ASN A CA  1 
ATOM   1535 C  C   . ASN A 1 207 ? 29.871 -17.996 -12.145 1.00 20.78 ? 200 ASN A C   1 
ATOM   1536 O  O   . ASN A 1 207 ? 29.439 -18.904 -12.866 1.00 21.99 ? 200 ASN A O   1 
ATOM   1537 C  CB  . ASN A 1 207 ? 27.655 -16.856 -12.051 1.00 21.02 ? 200 ASN A CB  1 
ATOM   1538 C  CG  . ASN A 1 207 ? 26.571 -16.309 -11.178 1.00 27.82 ? 200 ASN A CG  1 
ATOM   1539 O  OD1 . ASN A 1 207 ? 26.353 -16.797 -10.072 1.00 29.63 ? 200 ASN A OD1 1 
ATOM   1540 N  ND2 . ASN A 1 207 ? 25.879 -15.282 -11.657 1.00 33.32 ? 200 ASN A ND2 1 
ATOM   1541 N  N   . SER A 1 208 ? 31.163 -17.699 -12.102 1.00 17.70 ? 201 SER A N   1 
ATOM   1542 C  CA  . SER A 1 208 ? 32.085 -18.394 -12.970 1.00 17.54 ? 201 SER A CA  1 
ATOM   1543 C  C   . SER A 1 208 ? 32.473 -19.745 -12.386 1.00 15.94 ? 201 SER A C   1 
ATOM   1544 O  O   . SER A 1 208 ? 32.354 -19.995 -11.184 1.00 16.62 ? 201 SER A O   1 
ATOM   1545 C  CB  . SER A 1 208 ? 33.340 -17.566 -13.202 1.00 16.83 ? 201 SER A CB  1 
ATOM   1546 O  OG  . SER A 1 208 ? 33.023 -16.349 -13.863 1.00 19.29 ? 201 SER A OG  1 
ATOM   1547 N  N   . VAL A 1 209 ? 33.000 -20.595 -13.259 1.00 16.95 ? 202 VAL A N   1 
ATOM   1548 C  CA  . VAL A 1 209 ? 33.391 -21.957 -12.916 1.00 15.22 ? 202 VAL A CA  1 
ATOM   1549 C  C   . VAL A 1 209 ? 34.764 -22.187 -13.516 1.00 17.48 ? 202 VAL A C   1 
ATOM   1550 O  O   . VAL A 1 209 ? 34.914 -22.137 -14.739 1.00 18.78 ? 202 VAL A O   1 
ATOM   1551 C  CB  . VAL A 1 209 ? 32.387 -22.989 -13.457 1.00 20.83 ? 202 VAL A CB  1 
ATOM   1552 C  CG1 . VAL A 1 209 ? 32.900 -24.416 -13.225 1.00 22.96 ? 202 VAL A CG1 1 
ATOM   1553 C  CG2 . VAL A 1 209 ? 31.007 -22.790 -12.828 1.00 24.23 ? 202 VAL A CG2 1 
ATOM   1554 N  N   . LEU A 1 210 ? 35.767 -22.388 -12.662 1.00 15.53 ? 203 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 210 ? 37.102 -22.791 -13.098 1.00 13.65 ? 203 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 210 ? 37.248 -24.294 -12.874 1.00 17.07 ? 203 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 210 ? 37.014 -24.784 -11.763 1.00 16.93 ? 203 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 210 ? 38.186 -22.034 -12.338 1.00 14.01 ? 203 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 210 ? 38.609 -20.707 -12.927 1.00 18.37 ? 203 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 210 ? 37.433 -19.780 -13.055 1.00 19.23 ? 203 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 210 ? 39.699 -20.059 -12.101 1.00 19.28 ? 203 LEU A CD2 1 
ATOM   1562 N  N   . ALA A 1 211 ? 37.645 -25.013 -13.920 1.00 14.87 ? 204 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 211 ? 37.973 -26.426 -13.805 1.00 14.75 ? 204 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 211 ? 39.254 -26.611 -12.989 1.00 17.38 ? 204 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 211 ? 39.929 -25.646 -12.615 1.00 19.27 ? 204 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 211 ? 38.171 -27.052 -15.189 1.00 20.34 ? 204 ALA A CB  1 
ATOM   1567 N  N   . MET A 1 212 ? 39.584 -27.878 -12.723 1.00 21.00 ? 205 MET A N   1 
ATOM   1568 C  CA  . MET A 1 212 ? 40.845 -28.182 -12.065 1.00 19.60 ? 205 MET A CA  1 
ATOM   1569 C  C   . MET A 1 212 ? 42.014 -27.683 -12.895 1.00 19.90 ? 205 MET A C   1 
ATOM   1570 O  O   . MET A 1 212 ? 42.012 -27.778 -14.124 1.00 19.05 ? 205 MET A O   1 
ATOM   1571 C  CB  . MET A 1 212 ? 40.998 -29.682 -11.857 1.00 18.70 ? 205 MET A CB  1 
ATOM   1572 C  CG  . MET A 1 212 ? 39.940 -30.251 -10.950 1.00 22.59 ? 205 MET A CG  1 
ATOM   1573 S  SD  . MET A 1 212 ? 40.356 -31.904 -10.439 1.00 28.07 ? 205 MET A SD  1 
ATOM   1574 C  CE  . MET A 1 212 ? 39.992 -32.731 -12.032 1.00 22.97 ? 205 MET A CE  1 
ATOM   1575 N  N   . GLY A 1 213 ? 43.045 -27.201 -12.210 1.00 19.58 ? 206 GLY A N   1 
ATOM   1576 C  CA  . GLY A 1 213 ? 44.293 -26.920 -12.880 1.00 20.98 ? 206 GLY A CA  1 
ATOM   1577 C  C   . GLY A 1 213 ? 44.337 -25.665 -13.701 1.00 18.89 ? 206 GLY A C   1 
ATOM   1578 O  O   . GLY A 1 213 ? 45.159 -25.573 -14.628 1.00 21.61 ? 206 GLY A O   1 
ATOM   1579 N  N   . VAL A 1 214 ? 43.440 -24.719 -13.451 1.00 17.62 ? 207 VAL A N   1 
ATOM   1580 C  CA  . VAL A 1 214 ? 43.470 -23.411 -14.109 1.00 14.45 ? 207 VAL A CA  1 
ATOM   1581 C  C   . VAL A 1 214 ? 44.365 -22.498 -13.286 1.00 19.52 ? 207 VAL A C   1 
ATOM   1582 O  O   . VAL A 1 214 ? 44.117 -22.296 -12.097 1.00 18.88 ? 207 VAL A O   1 
ATOM   1583 C  CB  . VAL A 1 214 ? 42.064 -22.814 -14.227 1.00 13.85 ? 207 VAL A CB  1 
ATOM   1584 C  CG1 . VAL A 1 214 ? 42.142 -21.372 -14.709 1.00 18.94 ? 207 VAL A CG1 1 
ATOM   1585 C  CG2 . VAL A 1 214 ? 41.227 -23.666 -15.155 1.00 16.81 ? 207 VAL A CG2 1 
ATOM   1586 N  N   . PHE A 1 215 ? 45.376 -21.914 -13.918 1.00 16.52 ? 208 PHE A N   1 
ATOM   1587 C  CA  . PHE A 1 215 ? 46.304 -21.011 -13.245 1.00 15.97 ? 208 PHE A CA  1 
ATOM   1588 C  C   . PHE A 1 215 ? 46.169 -19.648 -13.907 1.00 19.40 ? 208 PHE A C   1 
ATOM   1589 O  O   . PHE A 1 215 ? 46.413 -19.526 -15.113 1.00 23.29 ? 208 PHE A O   1 
ATOM   1590 C  CB  . PHE A 1 215 ? 47.742 -21.516 -13.343 1.00 19.97 ? 208 PHE A CB  1 
ATOM   1591 C  CG  . PHE A 1 215 ? 47.911 -22.943 -12.910 1.00 21.70 ? 208 PHE A CG  1 
ATOM   1592 C  CD1 . PHE A 1 215 ? 47.382 -23.397 -11.724 1.00 24.36 ? 208 PHE A CD1 1 
ATOM   1593 C  CD2 . PHE A 1 215 ? 48.545 -23.847 -13.725 1.00 27.90 ? 208 PHE A CD2 1 
ATOM   1594 C  CE1 . PHE A 1 215 ? 47.510 -24.731 -11.337 1.00 27.04 ? 208 PHE A CE1 1 
ATOM   1595 C  CE2 . PHE A 1 215 ? 48.672 -25.163 -13.342 1.00 25.23 ? 208 PHE A CE2 1 
ATOM   1596 C  CZ  . PHE A 1 215 ? 48.178 -25.602 -12.152 1.00 23.30 ? 208 PHE A CZ  1 
ATOM   1597 N  N   . LEU A 1 216 ? 45.776 -18.630 -13.136 1.00 15.22 ? 209 LEU A N   1 
ATOM   1598 C  CA  . LEU A 1 216 ? 45.554 -17.296 -13.681 1.00 14.40 ? 209 LEU A CA  1 
ATOM   1599 C  C   . LEU A 1 216 ? 46.373 -16.266 -12.929 1.00 16.96 ? 209 LEU A C   1 
ATOM   1600 O  O   . LEU A 1 216 ? 46.212 -16.110 -11.718 1.00 14.78 ? 209 LEU A O   1 
ATOM   1601 C  CB  . LEU A 1 216 ? 44.080 -16.872 -13.594 1.00 14.44 ? 209 LEU A CB  1 
ATOM   1602 C  CG  . LEU A 1 216 ? 43.058 -17.708 -14.332 1.00 16.78 ? 209 LEU A CG  1 
ATOM   1603 C  CD1 . LEU A 1 216 ? 41.660 -17.213 -14.020 1.00 19.03 ? 209 LEU A CD1 1 
ATOM   1604 C  CD2 . LEU A 1 216 ? 43.327 -17.670 -15.793 1.00 21.38 ? 209 LEU A CD2 1 
ATOM   1605 N  N   . SER A 1 217 ? 47.206 -15.543 -13.663 1.00 15.79 ? 210 SER A N   1 
ATOM   1606 C  CA  . SER A 1 217 ? 47.909 -14.368 -13.198 1.00 14.60 ? 210 SER A CA  1 
ATOM   1607 C  C   . SER A 1 217 ? 47.562 -13.262 -14.186 1.00 14.76 ? 210 SER A C   1 
ATOM   1608 O  O   . SER A 1 217 ? 46.769 -13.467 -15.115 1.00 15.89 ? 210 SER A O   1 
ATOM   1609 C  CB  . SER A 1 217 ? 49.424 -14.597 -13.144 1.00 20.52 ? 210 SER A CB  1 
ATOM   1610 O  OG  . SER A 1 217 ? 49.993 -14.514 -14.434 1.00 22.08 ? 210 SER A OG  1 
ATOM   1611 N  N   . GLN A 1 218 ? 48.164 -12.086 -13.987 1.00 16.71 ? 211 GLN A N   1 
ATOM   1612 C  CA  . GLN A 1 218 ? 47.896 -11.007 -14.924 1.00 16.98 ? 211 GLN A CA  1 
ATOM   1613 C  C   . GLN A 1 218 ? 48.446 -11.307 -16.306 1.00 17.75 ? 211 GLN A C   1 
ATOM   1614 O  O   . GLN A 1 218 ? 47.994 -10.691 -17.270 1.00 19.97 ? 211 GLN A O   1 
ATOM   1615 C  CB  . GLN A 1 218 ? 48.471 -9.682  -14.422 1.00 20.46 ? 211 GLN A CB  1 
ATOM   1616 C  CG  . GLN A 1 218 ? 47.767 -9.152  -13.174 1.00 19.48 ? 211 GLN A CG  1 
ATOM   1617 C  CD  . GLN A 1 218 ? 46.342 -8.668  -13.447 1.00 22.43 ? 211 GLN A CD  1 
ATOM   1618 O  OE1 . GLN A 1 218 ? 45.988 -8.347  -14.574 1.00 22.12 ? 211 GLN A OE1 1 
ATOM   1619 N  NE2 . GLN A 1 218 ? 45.531 -8.597  -12.403 1.00 21.42 ? 211 GLN A NE2 1 
ATOM   1620 N  N   . SER A 1 219 ? 49.417 -12.216 -16.430 1.00 16.25 ? 212 SER A N   1 
ATOM   1621 C  CA  . SER A 1 219 ? 50.007 -12.494 -17.736 1.00 16.69 ? 212 SER A CA  1 
ATOM   1622 C  C   . SER A 1 219 ? 49.464 -13.748 -18.401 1.00 18.59 ? 212 SER A C   1 
ATOM   1623 O  O   . SER A 1 219 ? 49.921 -14.087 -19.510 1.00 20.41 ? 212 SER A O   1 
ATOM   1624 C  CB  . SER A 1 219 ? 51.533 -12.591 -17.620 1.00 25.70 ? 212 SER A CB  1 
ATOM   1625 O  OG  . SER A 1 219 ? 51.924 -13.559 -16.679 1.00 34.94 ? 212 SER A OG  1 
ATOM   1626 N  N   . THR A 1 220 ? 48.462 -14.399 -17.812 1.00 16.74 ? 213 THR A N   1 
ATOM   1627 C  CA  . THR A 1 220 ? 47.894 -15.598 -18.395 1.00 16.22 ? 213 THR A CA  1 
ATOM   1628 C  C   . THR A 1 220 ? 46.935 -15.229 -19.513 1.00 17.11 ? 213 THR A C   1 
ATOM   1629 O  O   . THR A 1 220 ? 45.985 -14.484 -19.289 1.00 17.79 ? 213 THR A O   1 
ATOM   1630 C  CB  . THR A 1 220 ? 47.144 -16.412 -17.340 1.00 16.73 ? 213 THR A CB  1 
ATOM   1631 O  OG1 . THR A 1 220 ? 48.029 -16.731 -16.276 1.00 20.44 ? 213 THR A OG1 1 
ATOM   1632 C  CG2 . THR A 1 220 ? 46.629 -17.710 -17.965 1.00 21.99 ? 213 THR A CG2 1 
ATOM   1633 N  N   . LYS A 1 221 ? 47.158 -15.779 -20.703 1.00 15.15 ? 214 LYS A N   1 
ATOM   1634 C  CA  . LYS A 1 221 ? 46.220 -15.530 -21.787 1.00 14.20 ? 214 LYS A CA  1 
ATOM   1635 C  C   . LYS A 1 221 ? 44.898 -16.224 -21.474 1.00 17.75 ? 214 LYS A C   1 
ATOM   1636 O  O   . LYS A 1 221 ? 44.875 -17.380 -21.040 1.00 17.36 ? 214 LYS A O   1 
ATOM   1637 C  CB  . LYS A 1 221 ? 46.770 -16.009 -23.128 1.00 15.01 ? 214 LYS A CB  1 
ATOM   1638 C  CG  . LYS A 1 221 ? 47.950 -15.219 -23.630 1.00 17.84 ? 214 LYS A CG  1 
ATOM   1639 C  CD  . LYS A 1 221 ? 48.312 -15.580 -25.034 1.00 20.65 ? 214 LYS A CD  1 
ATOM   1640 C  CE  . LYS A 1 221 ? 49.496 -14.730 -25.452 1.00 23.46 ? 214 LYS A CE  1 
ATOM   1641 N  NZ  . LYS A 1 221 ? 49.847 -14.901 -26.863 1.00 37.89 ? 214 LYS A NZ  1 
ATOM   1642 N  N   . ILE A 1 222 ? 43.790 -15.499 -21.656 1.00 15.56 ? 215 ILE A N   1 
ATOM   1643 C  CA  . ILE A 1 222 ? 42.445 -16.062 -21.522 1.00 13.53 ? 215 ILE A CA  1 
ATOM   1644 C  C   . ILE A 1 222 ? 41.855 -16.081 -22.926 1.00 18.35 ? 215 ILE A C   1 
ATOM   1645 O  O   . ILE A 1 222 ? 41.551 -15.034 -23.504 1.00 17.44 ? 215 ILE A O   1 
ATOM   1646 C  CB  . ILE A 1 222 ? 41.589 -15.255 -20.541 1.00 18.78 ? 215 ILE A CB  1 
ATOM   1647 C  CG1 . ILE A 1 222 ? 42.263 -15.214 -19.178 1.00 17.57 ? 215 ILE A CG1 1 
ATOM   1648 C  CG2 . ILE A 1 222 ? 40.195 -15.861 -20.432 1.00 19.73 ? 215 ILE A CG2 1 
ATOM   1649 C  CD1 . ILE A 1 222 ? 41.623 -14.259 -18.227 1.00 16.98 ? 215 ILE A CD1 1 
ATOM   1650 N  N   . TYR A 1 223 ? 41.740 -17.269 -23.507 1.00 14.90 ? 216 TYR A N   1 
ATOM   1651 C  CA  . TYR A 1 223 ? 41.279 -17.437 -24.880 1.00 16.80 ? 216 TYR A CA  1 
ATOM   1652 C  C   . TYR A 1 223 ? 39.794 -17.757 -24.865 1.00 17.88 ? 216 TYR A C   1 
ATOM   1653 O  O   . TYR A 1 223 ? 39.382 -18.752 -24.256 1.00 17.10 ? 216 TYR A O   1 
ATOM   1654 C  CB  . TYR A 1 223 ? 42.059 -18.560 -25.563 1.00 15.62 ? 216 TYR A CB  1 
ATOM   1655 C  CG  . TYR A 1 223 ? 41.642 -18.819 -26.982 1.00 16.02 ? 216 TYR A CG  1 
ATOM   1656 C  CD1 . TYR A 1 223 ? 41.963 -17.930 -27.996 1.00 16.61 ? 216 TYR A CD1 1 
ATOM   1657 C  CD2 . TYR A 1 223 ? 40.915 -19.945 -27.317 1.00 17.80 ? 216 TYR A CD2 1 
ATOM   1658 C  CE1 . TYR A 1 223 ? 41.585 -18.159 -29.275 1.00 17.74 ? 216 TYR A CE1 1 
ATOM   1659 C  CE2 . TYR A 1 223 ? 40.536 -20.184 -28.607 1.00 19.49 ? 216 TYR A CE2 1 
ATOM   1660 C  CZ  . TYR A 1 223 ? 40.864 -19.280 -29.584 1.00 19.75 ? 216 TYR A CZ  1 
ATOM   1661 O  OH  . TYR A 1 223 ? 40.492 -19.504 -30.890 1.00 24.29 ? 216 TYR A OH  1 
ATOM   1662 N  N   . ASP A 1 224 ? 38.987 -16.911 -25.518 1.00 17.33 ? 217 ASP A N   1 
ATOM   1663 C  CA  . ASP A 1 224 ? 37.557 -17.174 -25.620 1.00 19.24 ? 217 ASP A CA  1 
ATOM   1664 C  C   . ASP A 1 224 ? 37.315 -18.022 -26.859 1.00 17.27 ? 217 ASP A C   1 
ATOM   1665 O  O   . ASP A 1 224 ? 37.528 -17.561 -27.986 1.00 18.69 ? 217 ASP A O   1 
ATOM   1666 C  CB  . ASP A 1 224 ? 36.759 -15.876 -25.675 1.00 17.85 ? 217 ASP A CB  1 
ATOM   1667 C  CG  . ASP A 1 224 ? 35.260 -16.144 -25.569 1.00 24.56 ? 217 ASP A CG  1 
ATOM   1668 O  OD1 . ASP A 1 224 ? 34.700 -16.717 -26.507 1.00 29.75 ? 217 ASP A OD1 1 
ATOM   1669 O  OD2 . ASP A 1 224 ? 34.679 -15.873 -24.511 1.00 38.58 ? 217 ASP A OD2 1 
ATOM   1670 N  N   . ARG A 1 225 ? 36.907 -19.280 -26.652 1.00 18.46 ? 218 ARG A N   1 
ATOM   1671 C  CA  . ARG A 1 225 ? 36.793 -20.197 -27.774 1.00 18.31 ? 218 ARG A CA  1 
ATOM   1672 C  C   . ARG A 1 225 ? 35.756 -19.715 -28.787 1.00 22.14 ? 218 ARG A C   1 
ATOM   1673 O  O   . ARG A 1 225 ? 35.952 -19.847 -29.999 1.00 23.52 ? 218 ARG A O   1 
ATOM   1674 C  CB  . ARG A 1 225 ? 36.434 -21.586 -27.263 1.00 22.65 ? 218 ARG A CB  1 
ATOM   1675 C  CG  . ARG A 1 225 ? 36.286 -22.593 -28.395 1.00 26.63 ? 218 ARG A CG  1 
ATOM   1676 C  CD  . ARG A 1 225 ? 36.100 -24.009 -27.870 1.00 28.93 ? 218 ARG A CD  1 
ATOM   1677 N  NE  . ARG A 1 225 ? 34.853 -24.187 -27.131 1.00 28.52 ? 218 ARG A NE  1 
ATOM   1678 C  CZ  . ARG A 1 225 ? 34.381 -25.364 -26.737 1.00 31.92 ? 218 ARG A CZ  1 
ATOM   1679 N  NH1 . ARG A 1 225 ? 35.044 -26.490 -26.964 1.00 30.01 ? 218 ARG A NH1 1 
ATOM   1680 N  NH2 . ARG A 1 225 ? 33.213 -25.417 -26.103 1.00 29.13 ? 218 ARG A NH2 1 
ATOM   1681 N  N   . ALA A 1 226 ? 34.648 -19.160 -28.306 1.00 20.55 ? 219 ALA A N   1 
ATOM   1682 C  CA  . ALA A 1 226 ? 33.561 -18.790 -29.214 1.00 25.43 ? 219 ALA A CA  1 
ATOM   1683 C  C   . ALA A 1 226 ? 33.949 -17.633 -30.122 1.00 26.35 ? 219 ALA A C   1 
ATOM   1684 O  O   . ALA A 1 226 ? 33.539 -17.592 -31.290 1.00 27.14 ? 219 ALA A O   1 
ATOM   1685 C  CB  . ALA A 1 226 ? 32.310 -18.433 -28.406 1.00 28.85 ? 219 ALA A CB  1 
ATOM   1686 N  N   . THR A 1 227 ? 34.711 -16.669 -29.604 1.00 25.26 ? 220 THR A N   1 
ATOM   1687 C  CA  . THR A 1 227 ? 35.059 -15.481 -30.369 1.00 24.70 ? 220 THR A CA  1 
ATOM   1688 C  C   . THR A 1 227 ? 36.456 -15.523 -30.959 1.00 23.77 ? 220 THR A C   1 
ATOM   1689 O  O   . THR A 1 227 ? 36.755 -14.733 -31.863 1.00 24.24 ? 220 THR A O   1 
ATOM   1690 C  CB  . THR A 1 227 ? 34.947 -14.237 -29.493 1.00 25.81 ? 220 THR A CB  1 
ATOM   1691 O  OG1 . THR A 1 227 ? 35.901 -14.325 -28.434 1.00 24.50 ? 220 THR A OG1 1 
ATOM   1692 C  CG2 . THR A 1 227 ? 33.539 -14.120 -28.919 1.00 33.27 ? 220 THR A CG2 1 
ATOM   1693 N  N   . GLY A 1 228 ? 37.317 -16.397 -30.442 1.00 21.19 ? 221 GLY A N   1 
ATOM   1694 C  CA  . GLY A 1 228 ? 38.686 -16.454 -30.901 1.00 21.64 ? 221 GLY A CA  1 
ATOM   1695 C  C   . GLY A 1 228 ? 39.575 -15.350 -30.387 1.00 25.18 ? 221 GLY A C   1 
ATOM   1696 O  O   . GLY A 1 228 ? 40.667 -15.152 -30.930 1.00 24.06 ? 221 GLY A O   1 
ATOM   1697 N  N   . LYS A 1 229 ? 39.152 -14.632 -29.347 1.00 19.23 ? 222 LYS A N   1 
ATOM   1698 C  CA  . LYS A 1 229 ? 39.885 -13.478 -28.839 1.00 18.96 ? 222 LYS A CA  1 
ATOM   1699 C  C   . LYS A 1 229 ? 40.629 -13.792 -27.544 1.00 18.36 ? 222 LYS A C   1 
ATOM   1700 O  O   . LYS A 1 229 ? 40.171 -14.585 -26.722 1.00 18.31 ? 222 LYS A O   1 
ATOM   1701 C  CB  . LYS A 1 229 ? 38.951 -12.292 -28.568 1.00 22.44 ? 222 LYS A CB  1 
ATOM   1702 C  CG  . LYS A 1 229 ? 38.037 -11.903 -29.718 1.00 24.77 ? 222 LYS A CG  1 
ATOM   1703 C  CD  . LYS A 1 229 ? 38.782 -11.584 -30.981 1.00 22.81 ? 222 LYS A CD  1 
ATOM   1704 C  CE  . LYS A 1 229 ? 37.836 -11.118 -32.115 1.00 29.30 ? 222 LYS A CE  1 
ATOM   1705 N  NZ  . LYS A 1 229 ? 38.613 -10.915 -33.360 1.00 38.02 ? 222 LYS A NZ  1 
ATOM   1706 N  N   . VAL A 1 230 ? 41.757 -13.103 -27.354 1.00 18.61 ? 223 VAL A N   1 
ATOM   1707 C  CA  . VAL A 1 230 ? 42.619 -13.251 -26.179 1.00 16.71 ? 223 VAL A CA  1 
ATOM   1708 C  C   . VAL A 1 230 ? 42.455 -12.016 -25.310 1.00 18.68 ? 223 VAL A C   1 
ATOM   1709 O  O   . VAL A 1 230 ? 42.527 -10.881 -25.806 1.00 19.95 ? 223 VAL A O   1 
ATOM   1710 C  CB  . VAL A 1 230 ? 44.094 -13.420 -26.588 1.00 19.67 ? 223 VAL A CB  1 
ATOM   1711 C  CG1 . VAL A 1 230 ? 45.001 -13.266 -25.387 1.00 20.74 ? 223 VAL A CG1 1 
ATOM   1712 C  CG2 . VAL A 1 230 ? 44.318 -14.761 -27.277 1.00 23.31 ? 223 VAL A CG2 1 
ATOM   1713 N  N   . SER A 1 231 ? 42.283 -12.237 -24.010 1.00 17.31 ? 224 SER A N   1 
ATOM   1714 C  CA  . SER A 1 231 ? 42.243 -11.170 -23.025 1.00 18.71 ? 224 SER A CA  1 
ATOM   1715 C  C   . SER A 1 231 ? 43.029 -11.617 -21.798 1.00 18.52 ? 224 SER A C   1 
ATOM   1716 O  O   . SER A 1 231 ? 43.517 -12.749 -21.729 1.00 16.78 ? 224 SER A O   1 
ATOM   1717 C  CB  . SER A 1 231 ? 40.813 -10.804 -22.623 1.00 20.99 ? 224 SER A CB  1 
ATOM   1718 O  OG  . SER A 1 231 ? 40.144 -11.899 -22.037 1.00 23.31 ? 224 SER A OG  1 
ATOM   1719 N  N   . TYR A 1 232 ? 43.138 -10.719 -20.821 1.00 18.99 ? 225 TYR A N   1 
ATOM   1720 C  CA  . TYR A 1 232 ? 43.904 -10.970 -19.619 1.00 17.51 ? 225 TYR A CA  1 
ATOM   1721 C  C   . TYR A 1 232 ? 43.197 -10.392 -18.402 1.00 16.47 ? 225 TYR A C   1 
ATOM   1722 O  O   . TYR A 1 232 ? 42.515 -9.366  -18.482 1.00 18.70 ? 225 TYR A O   1 
ATOM   1723 C  CB  . TYR A 1 232 ? 45.301 -10.325 -19.670 1.00 18.54 ? 225 TYR A CB  1 
ATOM   1724 C  CG  . TYR A 1 232 ? 46.192 -10.755 -20.817 1.00 18.71 ? 225 TYR A CG  1 
ATOM   1725 C  CD1 . TYR A 1 232 ? 46.096 -10.169 -22.065 1.00 22.17 ? 225 TYR A CD1 1 
ATOM   1726 C  CD2 . TYR A 1 232 ? 47.178 -11.721 -20.619 1.00 20.18 ? 225 TYR A CD2 1 
ATOM   1727 C  CE1 . TYR A 1 232 ? 46.946 -10.554 -23.106 1.00 24.92 ? 225 TYR A CE1 1 
ATOM   1728 C  CE2 . TYR A 1 232 ? 48.018 -12.113 -21.649 1.00 19.56 ? 225 TYR A CE2 1 
ATOM   1729 C  CZ  . TYR A 1 232 ? 47.903 -11.541 -22.875 1.00 21.56 ? 225 TYR A CZ  1 
ATOM   1730 O  OH  . TYR A 1 232 ? 48.786 -11.927 -23.885 1.00 27.45 ? 225 TYR A OH  1 
ATOM   1731 N  N   . GLY A 1 233 ? 43.452 -11.011 -17.254 1.00 16.57 ? 226 GLY A N   1 
ATOM   1732 C  CA  . GLY A 1 233 ? 43.256 -10.356 -15.971 1.00 17.94 ? 226 GLY A CA  1 
ATOM   1733 C  C   . GLY A 1 233 ? 41.875 -10.461 -15.371 1.00 17.08 ? 226 GLY A C   1 
ATOM   1734 O  O   . GLY A 1 233 ? 41.692 -10.057 -14.210 1.00 16.83 ? 226 GLY A O   1 
ATOM   1735 N  N   . ARG A 1 234 ? 40.909 -11.004 -16.104 1.00 18.23 ? 227 ARG A N   1 
ATOM   1736 C  CA  . ARG A 1 234 ? 39.519 -10.981 -15.666 1.00 16.80 ? 227 ARG A CA  1 
ATOM   1737 C  C   . ARG A 1 234 ? 38.773 -12.113 -16.338 1.00 17.28 ? 227 ARG A C   1 
ATOM   1738 O  O   . ARG A 1 234 ? 38.883 -12.308 -17.553 1.00 17.46 ? 227 ARG A O   1 
ATOM   1739 C  CB  . ARG A 1 234 ? 38.876 -9.636  -16.000 1.00 19.77 ? 227 ARG A CB  1 
ATOM   1740 C  CG  . ARG A 1 234 ? 37.399 -9.524  -15.680 1.00 21.90 ? 227 ARG A CG  1 
ATOM   1741 C  CD  . ARG A 1 234 ? 36.872 -8.145  -16.075 1.00 24.53 ? 227 ARG A CD  1 
ATOM   1742 N  NE  . ARG A 1 234 ? 37.532 -7.094  -15.314 1.00 28.72 ? 227 ARG A NE  1 
ATOM   1743 C  CZ  . ARG A 1 234 ? 37.129 -6.661  -14.126 1.00 32.26 ? 227 ARG A CZ  1 
ATOM   1744 N  NH1 . ARG A 1 234 ? 36.005 -7.096  -13.572 1.00 30.15 ? 227 ARG A NH1 1 
ATOM   1745 N  NH2 . ARG A 1 234 ? 37.874 -5.774  -13.473 1.00 30.02 ? 227 ARG A NH2 1 
ATOM   1746 N  N   . VAL A 1 235 ? 38.019 -12.864 -15.533 1.00 14.35 ? 228 VAL A N   1 
ATOM   1747 C  CA  . VAL A 1 235 ? 37.107 -13.884 -16.041 1.00 16.09 ? 228 VAL A CA  1 
ATOM   1748 C  C   . VAL A 1 235 ? 35.703 -13.277 -16.053 1.00 14.44 ? 228 VAL A C   1 
ATOM   1749 O  O   . VAL A 1 235 ? 35.164 -12.972 -14.987 1.00 17.03 ? 228 VAL A O   1 
ATOM   1750 C  CB  . VAL A 1 235 ? 37.154 -15.145 -15.175 1.00 16.80 ? 228 VAL A CB  1 
ATOM   1751 C  CG1 . VAL A 1 235 ? 36.132 -16.161 -15.650 1.00 15.39 ? 228 VAL A CG1 1 
ATOM   1752 C  CG2 . VAL A 1 235 ? 38.546 -15.711 -15.184 1.00 19.37 ? 228 VAL A CG2 1 
ATOM   1753 N  N   . PRO A 1 236 ? 35.081 -13.103 -17.221 1.00 15.18 ? 229 PRO A N   1 
ATOM   1754 C  CA  . PRO A 1 236 ? 33.745 -12.488 -17.244 1.00 18.26 ? 229 PRO A CA  1 
ATOM   1755 C  C   . PRO A 1 236 ? 32.715 -13.367 -16.550 1.00 18.66 ? 229 PRO A C   1 
ATOM   1756 O  O   . PRO A 1 236 ? 32.836 -14.595 -16.514 1.00 19.94 ? 229 PRO A O   1 
ATOM   1757 C  CB  . PRO A 1 236 ? 33.442 -12.348 -18.743 1.00 25.64 ? 229 PRO A CB  1 
ATOM   1758 C  CG  . PRO A 1 236 ? 34.778 -12.438 -19.429 1.00 27.18 ? 229 PRO A CG  1 
ATOM   1759 C  CD  . PRO A 1 236 ? 35.605 -13.374 -18.568 1.00 20.24 ? 229 PRO A CD  1 
ATOM   1760 N  N   . SER A 1 237 ? 31.687 -12.717 -16.013 1.00 18.25 ? 230 SER A N   1 
ATOM   1761 C  CA  . SER A 1 237 ? 30.694 -13.412 -15.208 1.00 20.43 ? 230 SER A CA  1 
ATOM   1762 C  C   . SER A 1 237 ? 30.136 -14.617 -15.954 1.00 20.14 ? 230 SER A C   1 
ATOM   1763 O  O   . SER A 1 237 ? 29.820 -14.543 -17.143 1.00 21.62 ? 230 SER A O   1 
ATOM   1764 C  CB  . SER A 1 237 ? 29.551 -12.470 -14.820 1.00 22.67 ? 230 SER A CB  1 
ATOM   1765 O  OG  . SER A 1 237 ? 28.943 -11.905 -15.974 1.00 25.66 ? 230 SER A OG  1 
ATOM   1766 N  N   . GLY A 1 238 ? 29.997 -15.719 -15.235 1.00 20.61 ? 231 GLY A N   1 
ATOM   1767 C  CA  . GLY A 1 238 ? 29.375 -16.911 -15.779 1.00 25.47 ? 231 GLY A CA  1 
ATOM   1768 C  C   . GLY A 1 238 ? 30.264 -17.740 -16.675 1.00 18.79 ? 231 GLY A C   1 
ATOM   1769 O  O   . GLY A 1 238 ? 29.774 -18.684 -17.305 1.00 21.87 ? 231 GLY A O   1 
ATOM   1770 N  N   . SER A 1 239 ? 31.531 -17.393 -16.806 1.00 22.37 ? 232 SER A N   1 
ATOM   1771 C  CA  . SER A 1 239 ? 32.394 -18.139 -17.705 1.00 20.79 ? 232 SER A CA  1 
ATOM   1772 C  C   . SER A 1 239 ? 32.741 -19.500 -17.131 1.00 24.13 ? 232 SER A C   1 
ATOM   1773 O  O   . SER A 1 239 ? 32.990 -19.628 -15.932 1.00 20.56 ? 232 SER A O   1 
ATOM   1774 C  CB  . SER A 1 239 ? 33.706 -17.402 -17.953 1.00 21.15 ? 232 SER A CB  1 
ATOM   1775 O  OG  . SER A 1 239 ? 33.490 -16.181 -18.635 1.00 25.05 ? 232 SER A OG  1 
ATOM   1776 N  N   . VAL A 1 240 ? 32.844 -20.490 -18.009 1.00 19.83 ? 233 VAL A N   1 
ATOM   1777 C  CA  . VAL A 1 240 ? 33.370 -21.807 -17.675 1.00 19.41 ? 233 VAL A CA  1 
ATOM   1778 C  C   . VAL A 1 240 ? 34.759 -21.895 -18.292 1.00 17.73 ? 233 VAL A C   1 
ATOM   1779 O  O   . VAL A 1 240 ? 34.908 -21.796 -19.517 1.00 18.00 ? 233 VAL A O   1 
ATOM   1780 C  CB  . VAL A 1 240 ? 32.455 -22.921 -18.196 1.00 20.63 ? 233 VAL A CB  1 
ATOM   1781 C  CG1 . VAL A 1 240 ? 33.027 -24.274 -17.806 1.00 22.43 ? 233 VAL A CG1 1 
ATOM   1782 C  CG2 . VAL A 1 240 ? 31.048 -22.751 -17.628 1.00 22.64 ? 233 VAL A CG2 1 
ATOM   1783 N  N   . VAL A 1 241 ? 35.780 -22.063 -17.452 1.00 16.93 ? 234 VAL A N   1 
ATOM   1784 C  CA  . VAL A 1 241 ? 37.179 -21.918 -17.855 1.00 15.46 ? 234 VAL A CA  1 
ATOM   1785 C  C   . VAL A 1 241 ? 37.904 -23.236 -17.616 1.00 15.16 ? 234 VAL A C   1 
ATOM   1786 O  O   . VAL A 1 241 ? 37.819 -23.793 -16.525 1.00 15.94 ? 234 VAL A O   1 
ATOM   1787 C  CB  . VAL A 1 241 ? 37.867 -20.801 -17.054 1.00 15.21 ? 234 VAL A CB  1 
ATOM   1788 C  CG1 . VAL A 1 241 ? 39.278 -20.582 -17.551 1.00 16.00 ? 234 VAL A CG1 1 
ATOM   1789 C  CG2 . VAL A 1 241 ? 37.061 -19.503 -17.120 1.00 16.86 ? 234 VAL A CG2 1 
ATOM   1790 N  N   . VAL A 1 242 ? 38.651 -23.702 -18.618 1.00 14.46 ? 235 VAL A N   1 
ATOM   1791 C  CA  . VAL A 1 242 ? 39.400 -24.951 -18.511 1.00 14.17 ? 235 VAL A CA  1 
ATOM   1792 C  C   . VAL A 1 242 ? 40.811 -24.701 -19.015 1.00 14.11 ? 235 VAL A C   1 
ATOM   1793 O  O   . VAL A 1 242 ? 41.060 -23.725 -19.743 1.00 15.31 ? 235 VAL A O   1 
ATOM   1794 C  CB  . VAL A 1 242 ? 38.740 -26.087 -19.326 1.00 14.99 ? 235 VAL A CB  1 
ATOM   1795 C  CG1 . VAL A 1 242 ? 37.249 -26.218 -18.960 1.00 16.51 ? 235 VAL A CG1 1 
ATOM   1796 C  CG2 . VAL A 1 242 ? 38.966 -25.821 -20.806 1.00 16.50 ? 235 VAL A CG2 1 
ATOM   1797 N  N   . PRO A 1 243 ? 41.755 -25.554 -18.650 1.00 12.81 ? 236 PRO A N   1 
ATOM   1798 C  CA  . PRO A 1 243 ? 43.111 -25.390 -19.178 1.00 13.67 ? 236 PRO A CA  1 
ATOM   1799 C  C   . PRO A 1 243 ? 43.210 -25.800 -20.631 1.00 13.60 ? 236 PRO A C   1 
ATOM   1800 O  O   . PRO A 1 243 ? 42.624 -26.796 -21.061 1.00 14.43 ? 236 PRO A O   1 
ATOM   1801 C  CB  . PRO A 1 243 ? 43.970 -26.320 -18.305 1.00 14.44 ? 236 PRO A CB  1 
ATOM   1802 C  CG  . PRO A 1 243 ? 43.121 -26.779 -17.219 1.00 20.79 ? 236 PRO A CG  1 
ATOM   1803 C  CD  . PRO A 1 243 ? 41.677 -26.568 -17.583 1.00 16.11 ? 236 PRO A CD  1 
ATOM   1804 N  N   . GLY A 1 244 ? 43.982 -25.021 -21.380 1.00 13.97 ? 237 GLY A N   1 
ATOM   1805 C  CA  . GLY A 1 244 ? 44.238 -25.342 -22.767 1.00 14.44 ? 237 GLY A CA  1 
ATOM   1806 C  C   . GLY A 1 244 ? 45.544 -24.722 -23.200 1.00 13.94 ? 237 GLY A C   1 
ATOM   1807 O  O   . GLY A 1 244 ? 46.439 -24.514 -22.376 1.00 14.25 ? 237 GLY A O   1 
ATOM   1808 N  N   . SER A 1 245 ? 45.687 -24.501 -24.495 1.00 16.21 ? 238 SER A N   1 
ATOM   1809 C  CA  . SER A 1 245 ? 46.912 -23.944 -25.028 1.00 16.15 ? 238 SER A CA  1 
ATOM   1810 C  C   . SER A 1 245 ? 46.649 -23.318 -26.389 1.00 15.78 ? 238 SER A C   1 
ATOM   1811 O  O   . SER A 1 245 ? 45.627 -23.559 -27.042 1.00 15.43 ? 238 SER A O   1 
ATOM   1812 C  CB  . SER A 1 245 ? 48.008 -25.016 -25.150 1.00 16.57 ? 238 SER A CB  1 
ATOM   1813 O  OG  . SER A 1 245 ? 47.637 -25.985 -26.108 1.00 19.97 ? 238 SER A OG  1 
ATOM   1814 N  N   . LEU A 1 246 ? 47.589 -22.474 -26.790 1.00 16.83 ? 239 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 246 ? 47.597 -21.824 -28.073 1.00 14.20 ? 239 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 246 ? 48.890 -22.158 -28.800 1.00 18.21 ? 239 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 246 ? 49.962 -22.153 -28.182 1.00 17.66 ? 239 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 246 ? 47.477 -20.302 -27.920 1.00 18.62 ? 239 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 246 ? 46.118 -19.847 -27.386 1.00 18.53 ? 239 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 246 ? 46.216 -18.388 -26.984 1.00 22.15 ? 239 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 246 ? 45.057 -20.015 -28.416 1.00 20.76 ? 239 LEU A CD2 1 
ATOM   1822 N  N   . PRO A 1 247 ? 48.813 -22.474 -30.091 1.00 19.31 ? 240 PRO A N   1 
ATOM   1823 C  CA  . PRO A 1 247 ? 50.014 -22.867 -30.842 1.00 19.88 ? 240 PRO A CA  1 
ATOM   1824 C  C   . PRO A 1 247 ? 50.835 -21.668 -31.273 1.00 21.98 ? 240 PRO A C   1 
ATOM   1825 O  O   . PRO A 1 247 ? 50.313 -20.584 -31.559 1.00 23.31 ? 240 PRO A O   1 
ATOM   1826 C  CB  . PRO A 1 247 ? 49.435 -23.578 -32.075 1.00 22.40 ? 240 PRO A CB  1 
ATOM   1827 C  CG  . PRO A 1 247 ? 48.145 -22.858 -32.319 1.00 22.57 ? 240 PRO A CG  1 
ATOM   1828 C  CD  . PRO A 1 247 ? 47.602 -22.518 -30.934 1.00 18.61 ? 240 PRO A CD  1 
ATOM   1829 N  N   . SER A 1 248 ? 52.144 -21.889 -31.356 1.00 21.07 ? 241 SER A N   1 
ATOM   1830 C  CA  . SER A 1 248 ? 53.007 -20.902 -31.984 1.00 24.33 ? 241 SER A CA  1 
ATOM   1831 C  C   . SER A 1 248 ? 52.701 -20.787 -33.482 1.00 26.61 ? 241 SER A C   1 
ATOM   1832 O  O   . SER A 1 248 ? 52.145 -21.697 -34.113 1.00 23.97 ? 241 SER A O   1 
ATOM   1833 C  CB  . SER A 1 248 ? 54.475 -21.279 -31.788 1.00 27.88 ? 241 SER A CB  1 
ATOM   1834 O  OG  . SER A 1 248 ? 54.802 -22.427 -32.542 1.00 25.55 ? 241 SER A OG  1 
ATOM   1835 N  N   . GLU A 1 249 ? 53.116 -19.657 -34.059 1.00 27.63 ? 242 GLU A N   1 
ATOM   1836 C  CA  . GLU A 1 249 ? 52.832 -19.394 -35.466 1.00 30.87 ? 242 GLU A CA  1 
ATOM   1837 C  C   . GLU A 1 249 ? 53.403 -20.481 -36.369 1.00 33.27 ? 242 GLU A C   1 
ATOM   1838 O  O   . GLU A 1 249 ? 52.794 -20.828 -37.385 1.00 34.54 ? 242 GLU A O   1 
ATOM   1839 C  CB  . GLU A 1 249 ? 53.386 -18.019 -35.863 1.00 36.45 ? 242 GLU A CB  1 
ATOM   1840 C  CG  . GLU A 1 249 ? 53.065 -17.580 -37.286 1.00 51.83 ? 242 GLU A CG  1 
ATOM   1841 C  CD  . GLU A 1 249 ? 51.584 -17.301 -37.500 1.00 80.15 ? 242 GLU A CD  1 
ATOM   1842 O  OE1 . GLU A 1 249 ? 50.789 -18.267 -37.561 1.00 76.87 ? 242 GLU A OE1 1 
ATOM   1843 O  OE2 . GLU A 1 249 ? 51.213 -16.111 -37.600 1.00 86.31 ? 242 GLU A OE2 1 
ATOM   1844 N  N   . ASP A 1 250 ? 54.573 -21.027 -36.032 1.00 28.83 ? 243 ASP A N   1 
ATOM   1845 C  CA  . ASP A 1 250 ? 55.194 -22.030 -36.893 1.00 29.04 ? 243 ASP A CA  1 
ATOM   1846 C  C   . ASP A 1 250 ? 54.785 -23.457 -36.540 1.00 30.33 ? 243 ASP A C   1 
ATOM   1847 O  O   . ASP A 1 250 ? 55.223 -24.396 -37.210 1.00 35.12 ? 243 ASP A O   1 
ATOM   1848 C  CB  . ASP A 1 250 ? 56.728 -21.887 -36.876 1.00 35.14 ? 243 ASP A CB  1 
ATOM   1849 C  CG  . ASP A 1 250 ? 57.370 -22.247 -35.533 1.00 37.69 ? 243 ASP A CG  1 
ATOM   1850 O  OD1 . ASP A 1 250 ? 56.679 -22.705 -34.600 1.00 30.87 ? 243 ASP A OD1 1 
ATOM   1851 O  OD2 . ASP A 1 250 ? 58.605 -22.062 -35.415 1.00 39.04 ? 243 ASP A OD2 1 
ATOM   1852 N  N   . GLY A 1 251 ? 53.943 -23.644 -35.530 1.00 28.99 ? 244 GLY A N   1 
ATOM   1853 C  CA  . GLY A 1 251 ? 53.454 -24.966 -35.210 1.00 26.11 ? 244 GLY A CA  1 
ATOM   1854 C  C   . GLY A 1 251 ? 54.413 -25.853 -34.445 1.00 28.08 ? 244 GLY A C   1 
ATOM   1855 O  O   . GLY A 1 251 ? 54.114 -27.034 -34.248 1.00 30.08 ? 244 GLY A O   1 
ATOM   1856 N  N   . SER A 1 252 ? 55.552 -25.334 -33.997 1.00 24.68 ? 245 SER A N   1 
ATOM   1857 C  CA  . SER A 1 252 ? 56.535 -26.187 -33.334 1.00 21.73 ? 245 SER A CA  1 
ATOM   1858 C  C   . SER A 1 252 ? 56.146 -26.561 -31.910 1.00 19.96 ? 245 SER A C   1 
ATOM   1859 O  O   . SER A 1 252 ? 56.638 -27.570 -31.393 1.00 20.34 ? 245 SER A O   1 
ATOM   1860 C  CB  . SER A 1 252 ? 57.895 -25.486 -33.309 1.00 25.07 ? 245 SER A CB  1 
ATOM   1861 O  OG  . SER A 1 252 ? 57.782 -24.217 -32.688 1.00 26.62 ? 245 SER A OG  1 
ATOM   1862 N  N   . HIS A 1 253 ? 55.298 -25.772 -31.263 1.00 19.92 ? 246 HIS A N   1 
ATOM   1863 C  CA  . HIS A 1 253 ? 55.004 -25.956 -29.848 1.00 16.77 ? 246 HIS A CA  1 
ATOM   1864 C  C   . HIS A 1 253 ? 53.773 -25.126 -29.522 1.00 20.55 ? 246 HIS A C   1 
ATOM   1865 O  O   . HIS A 1 253 ? 53.310 -24.329 -30.342 1.00 20.07 ? 246 HIS A O   1 
ATOM   1866 C  CB  . HIS A 1 253 ? 56.187 -25.544 -28.974 1.00 16.50 ? 246 HIS A CB  1 
ATOM   1867 C  CG  . HIS A 1 253 ? 56.432 -24.070 -28.965 1.00 19.38 ? 246 HIS A CG  1 
ATOM   1868 N  ND1 . HIS A 1 253 ? 57.049 -23.411 -30.004 1.00 20.63 ? 246 HIS A ND1 1 
ATOM   1869 C  CD2 . HIS A 1 253 ? 56.103 -23.119 -28.058 1.00 25.33 ? 246 HIS A CD2 1 
ATOM   1870 C  CE1 . HIS A 1 253 ? 57.110 -22.118 -29.730 1.00 25.07 ? 246 HIS A CE1 1 
ATOM   1871 N  NE2 . HIS A 1 253 ? 56.523 -21.912 -28.566 1.00 21.38 ? 246 HIS A NE2 1 
ATOM   1872 N  N   . SER A 1 254 ? 53.266 -25.316 -28.303 1.00 17.02 ? 247 SER A N   1 
ATOM   1873 C  CA  . SER A 1 254 ? 52.181 -24.505 -27.773 1.00 17.96 ? 247 SER A CA  1 
ATOM   1874 C  C   . SER A 1 254 ? 52.545 -24.020 -26.379 1.00 16.56 ? 247 SER A C   1 
ATOM   1875 O  O   . SER A 1 254 ? 53.386 -24.607 -25.684 1.00 15.75 ? 247 SER A O   1 
ATOM   1876 C  CB  . SER A 1 254 ? 50.868 -25.301 -27.716 1.00 17.84 ? 247 SER A CB  1 
ATOM   1877 O  OG  . SER A 1 254 ? 50.501 -25.814 -28.988 1.00 18.49 ? 247 SER A OG  1 
ATOM   1878 N  N   . LEU A 1 255 ? 51.895 -22.932 -25.961 1.00 16.24 ? 248 LEU A N   1 
ATOM   1879 C  CA  . LEU A 1 255 ? 52.020 -22.423 -24.600 1.00 15.67 ? 248 LEU A CA  1 
ATOM   1880 C  C   . LEU A 1 255 ? 50.668 -22.526 -23.887 1.00 14.78 ? 248 LEU A C   1 
ATOM   1881 O  O   . LEU A 1 255 ? 49.628 -22.180 -24.466 1.00 15.63 ? 248 LEU A O   1 
ATOM   1882 C  CB  . LEU A 1 255 ? 52.488 -20.978 -24.594 1.00 16.18 ? 248 LEU A CB  1 
ATOM   1883 C  CG  . LEU A 1 255 ? 53.865 -20.743 -25.188 1.00 17.75 ? 248 LEU A CG  1 
ATOM   1884 C  CD1 . LEU A 1 255 ? 54.247 -19.281 -25.026 1.00 21.42 ? 248 LEU A CD1 1 
ATOM   1885 C  CD2 . LEU A 1 255 ? 54.932 -21.633 -24.545 1.00 19.23 ? 248 LEU A CD2 1 
ATOM   1886 N  N   . ALA A 1 256 ? 50.683 -23.013 -22.649 1.00 14.20 ? 249 ALA A N   1 
ATOM   1887 C  CA  . ALA A 1 256 ? 49.445 -23.208 -21.905 1.00 14.09 ? 249 ALA A CA  1 
ATOM   1888 C  C   . ALA A 1 256 ? 48.760 -21.873 -21.630 1.00 13.90 ? 249 ALA A C   1 
ATOM   1889 O  O   . ALA A 1 256 ? 49.406 -20.834 -21.448 1.00 16.46 ? 249 ALA A O   1 
ATOM   1890 C  CB  . ALA A 1 256 ? 49.708 -23.919 -20.585 1.00 16.77 ? 249 ALA A CB  1 
ATOM   1891 N  N   . CYS A 1 257 ? 47.430 -21.921 -21.598 1.00 14.32 ? 250 CYS A N   1 
ATOM   1892 C  CA  . CYS A 1 257 ? 46.607 -20.747 -21.334 1.00 14.55 ? 250 CYS A CA  1 
ATOM   1893 C  C   . CYS A 1 257 ? 45.299 -21.233 -20.719 1.00 16.83 ? 250 CYS A C   1 
ATOM   1894 O  O   . CYS A 1 257 ? 45.091 -22.431 -20.520 1.00 15.79 ? 250 CYS A O   1 
ATOM   1895 C  CB  . CYS A 1 257 ? 46.344 -19.936 -22.608 1.00 16.59 ? 250 CYS A CB  1 
ATOM   1896 S  SG  . CYS A 1 257 ? 45.336 -20.759 -23.791 1.00 20.56 ? 250 CYS A SG  1 
ATOM   1897 N  N   . ALA A 1 258 ? 44.430 -20.293 -20.375 1.00 15.04 ? 251 ALA A N   1 
ATOM   1898 C  CA  . ALA A 1 258 ? 43.075 -20.615 -19.950 1.00 14.38 ? 251 ALA A CA  1 
ATOM   1899 C  C   . ALA A 1 258 ? 42.151 -20.465 -21.149 1.00 15.95 ? 251 ALA A C   1 
ATOM   1900 O  O   . ALA A 1 258 ? 42.369 -19.608 -21.996 1.00 15.79 ? 251 ALA A O   1 
ATOM   1901 C  CB  . ALA A 1 258 ? 42.630 -19.704 -18.812 1.00 17.34 ? 251 ALA A CB  1 
ATOM   1902 N  N   . VAL A 1 259 ? 41.115 -21.304 -21.226 1.00 14.16 ? 252 VAL A N   1 
ATOM   1903 C  CA  . VAL A 1 259 ? 40.168 -21.244 -22.337 1.00 13.75 ? 252 VAL A CA  1 
ATOM   1904 C  C   . VAL A 1 259 ? 38.765 -21.137 -21.767 1.00 14.53 ? 252 VAL A C   1 
ATOM   1905 O  O   . VAL A 1 259 ? 38.352 -21.983 -20.963 1.00 15.32 ? 252 VAL A O   1 
ATOM   1906 C  CB  . VAL A 1 259 ? 40.267 -22.495 -23.236 1.00 14.23 ? 252 VAL A CB  1 
ATOM   1907 C  CG1 . VAL A 1 259 ? 39.224 -22.427 -24.339 1.00 17.57 ? 252 VAL A CG1 1 
ATOM   1908 C  CG2 . VAL A 1 259 ? 41.677 -22.627 -23.830 1.00 15.34 ? 252 VAL A CG2 1 
ATOM   1909 N  N   . ILE A 1 260 ? 38.022 -20.123 -22.202 1.00 15.57 ? 253 ILE A N   1 
ATOM   1910 C  CA  . ILE A 1 260 ? 36.606 -20.027 -21.868 1.00 16.30 ? 253 ILE A CA  1 
ATOM   1911 C  C   . ILE A 1 260 ? 35.846 -20.862 -22.874 1.00 18.41 ? 253 ILE A C   1 
ATOM   1912 O  O   . ILE A 1 260 ? 35.842 -20.563 -24.078 1.00 17.79 ? 253 ILE A O   1 
ATOM   1913 C  CB  . ILE A 1 260 ? 36.116 -18.574 -21.884 1.00 16.62 ? 253 ILE A CB  1 
ATOM   1914 C  CG1 . ILE A 1 260 ? 36.883 -17.762 -20.841 1.00 17.89 ? 253 ILE A CG1 1 
ATOM   1915 C  CG2 . ILE A 1 260 ? 34.627 -18.551 -21.630 1.00 19.02 ? 253 ILE A CG2 1 
ATOM   1916 C  CD1 . ILE A 1 260 ? 36.623 -16.273 -20.951 1.00 23.09 ? 253 ILE A CD1 1 
ATOM   1917 N  N   . VAL A 1 261 ? 35.192 -21.921 -22.396 1.00 17.40 ? 254 VAL A N   1 
ATOM   1918 C  CA  . VAL A 1 261 ? 34.519 -22.840 -23.310 1.00 18.41 ? 254 VAL A CA  1 
ATOM   1919 C  C   . VAL A 1 261 ? 33.014 -22.642 -23.360 1.00 21.01 ? 254 VAL A C   1 
ATOM   1920 O  O   . VAL A 1 261 ? 32.357 -23.151 -24.286 1.00 23.60 ? 254 VAL A O   1 
ATOM   1921 C  CB  . VAL A 1 261 ? 34.851 -24.313 -22.957 1.00 18.65 ? 254 VAL A CB  1 
ATOM   1922 C  CG1 . VAL A 1 261 ? 36.297 -24.614 -23.225 1.00 18.72 ? 254 VAL A CG1 1 
ATOM   1923 C  CG2 . VAL A 1 261 ? 34.500 -24.603 -21.501 1.00 21.86 ? 254 VAL A CG2 1 
ATOM   1924 N  N   . LYS A 1 262 ? 32.444 -21.918 -22.408 1.00 20.41 ? 255 LYS A N   1 
ATOM   1925 C  CA  . LYS A 1 262 ? 31.066 -21.483 -22.515 1.00 24.23 ? 255 LYS A CA  1 
ATOM   1926 C  C   . LYS A 1 262 ? 30.808 -20.456 -21.425 1.00 26.32 ? 255 LYS A C   1 
ATOM   1927 O  O   . LYS A 1 262 ? 31.662 -20.173 -20.581 1.00 21.45 ? 255 LYS A O   1 
ATOM   1928 C  CB  . LYS A 1 262 ? 30.098 -22.655 -22.436 1.00 38.69 ? 255 LYS A CB  1 
ATOM   1929 C  CG  . LYS A 1 262 ? 30.010 -23.354 -21.112 1.00 36.25 ? 255 LYS A CG  1 
ATOM   1930 C  CD  . LYS A 1 262 ? 28.844 -24.355 -21.191 1.00 42.91 ? 255 LYS A CD  1 
ATOM   1931 C  CE  . LYS A 1 262 ? 28.557 -25.051 -19.876 1.00 61.89 ? 255 LYS A CE  1 
ATOM   1932 N  NZ  . LYS A 1 262 ? 27.459 -26.063 -20.020 1.00 71.32 ? 255 LYS A NZ  1 
ATOM   1933 N  N   . ARG A 1 263 ? 29.631 -19.864 -21.494 1.00 26.62 ? 256 ARG A N   1 
ATOM   1934 C  CA  . ARG A 1 263 ? 29.223 -18.840 -20.543 1.00 32.82 ? 256 ARG A CA  1 
ATOM   1935 C  C   . ARG A 1 263 ? 27.773 -19.098 -20.186 1.00 35.81 ? 256 ARG A C   1 
ATOM   1936 O  O   . ARG A 1 263 ? 26.948 -19.318 -21.079 1.00 37.43 ? 256 ARG A O   1 
ATOM   1937 C  CB  . ARG A 1 263 ? 29.415 -17.451 -21.146 1.00 32.53 ? 256 ARG A CB  1 
ATOM   1938 C  CG  . ARG A 1 263 ? 29.305 -16.353 -20.146 1.00 39.27 ? 256 ARG A CG  1 
ATOM   1939 C  CD  . ARG A 1 263 ? 29.675 -15.034 -20.751 1.00 48.83 ? 256 ARG A CD  1 
ATOM   1940 N  NE  . ARG A 1 263 ? 29.602 -13.981 -19.752 1.00 49.31 ? 256 ARG A NE  1 
ATOM   1941 C  CZ  . ARG A 1 263 ? 29.972 -12.729 -19.957 1.00 40.61 ? 256 ARG A CZ  1 
ATOM   1942 N  NH1 . ARG A 1 263 ? 30.440 -12.332 -21.131 1.00 53.27 ? 256 ARG A NH1 1 
ATOM   1943 N  NH2 . ARG A 1 263 ? 29.878 -11.857 -18.961 1.00 35.13 ? 256 ARG A NH2 1 
ATOM   1944 N  N   . VAL A 1 264 ? 27.470 -19.104 -18.883 1.00 33.90 ? 257 VAL A N   1 
ATOM   1945 C  CA  . VAL A 1 264 ? 26.139 -19.446 -18.393 1.00 34.53 ? 257 VAL A CA  1 
ATOM   1946 C  C   . VAL A 1 264 ? 25.625 -18.320 -17.503 1.00 45.50 ? 257 VAL A C   1 
ATOM   1947 O  O   . VAL A 1 264 ? 26.391 -17.503 -16.987 1.00 38.40 ? 257 VAL A O   1 
ATOM   1948 C  CB  . VAL A 1 264 ? 26.141 -20.788 -17.628 1.00 38.05 ? 257 VAL A CB  1 
ATOM   1949 C  CG1 . VAL A 1 264 ? 26.725 -21.894 -18.498 1.00 42.48 ? 257 VAL A CG1 1 
ATOM   1950 C  CG2 . VAL A 1 264 ? 26.947 -20.692 -16.333 1.00 37.95 ? 257 VAL A CG2 1 
ATOM   1951 N  N   . ASP A 1 265 ? 24.303 -18.280 -17.336 1.00 47.28 ? 258 ASP A N   1 
ATOM   1952 C  CA  . ASP A 1 265 ? 23.653 -17.279 -16.501 1.00 52.94 ? 258 ASP A CA  1 
ATOM   1953 C  C   . ASP A 1 265 ? 23.352 -17.865 -15.117 1.00 51.19 ? 258 ASP A C   1 
ATOM   1954 O  O   . ASP A 1 265 ? 23.572 -19.050 -14.846 1.00 44.78 ? 258 ASP A O   1 
ATOM   1955 C  CB  . ASP A 1 265 ? 22.383 -16.744 -17.180 1.00 56.34 ? 258 ASP A CB  1 
ATOM   1956 C  CG  . ASP A 1 265 ? 21.316 -17.808 -17.382 1.00 55.43 ? 258 ASP A CG  1 
ATOM   1957 O  OD1 . ASP A 1 265 ? 21.501 -18.953 -16.933 1.00 57.34 ? 258 ASP A OD1 1 
ATOM   1958 O  OD2 . ASP A 1 265 ? 20.282 -17.491 -18.003 1.00 61.33 ? 258 ASP A OD2 1 
ATOM   1959 N  N   . ALA A 1 266 ? 22.836 -17.015 -14.221 1.00 54.23 ? 259 ALA A N   1 
ATOM   1960 C  CA  . ALA A 1 266 ? 22.618 -17.458 -12.848 1.00 50.21 ? 259 ALA A CA  1 
ATOM   1961 C  C   . ALA A 1 266 ? 21.566 -18.558 -12.768 1.00 51.54 ? 259 ALA A C   1 
ATOM   1962 O  O   . ALA A 1 266 ? 21.672 -19.454 -11.921 1.00 54.44 ? 259 ALA A O   1 
ATOM   1963 C  CB  . ALA A 1 266 ? 22.215 -16.271 -11.970 1.00 52.13 ? 259 ALA A CB  1 
ATOM   1964 N  N   . GLN A 1 267 ? 20.547 -18.512 -13.628 1.00 51.61 ? 260 GLN A N   1 
ATOM   1965 C  CA  . GLN A 1 267 ? 19.539 -19.569 -13.619 1.00 52.38 ? 260 GLN A CA  1 
ATOM   1966 C  C   . GLN A 1 267 ? 20.170 -20.925 -13.921 1.00 55.05 ? 260 GLN A C   1 
ATOM   1967 O  O   . GLN A 1 267 ? 19.876 -21.923 -13.252 1.00 53.46 ? 260 GLN A O   1 
ATOM   1968 C  CB  . GLN A 1 267 ? 18.431 -19.242 -14.624 1.00 58.01 ? 260 GLN A CB  1 
ATOM   1969 N  N   . THR A 1 268 ? 21.065 -20.973 -14.908 1.00 51.53 ? 261 THR A N   1 
ATOM   1970 C  CA  . THR A 1 268 ? 21.725 -22.230 -15.252 1.00 59.41 ? 261 THR A CA  1 
ATOM   1971 C  C   . THR A 1 268 ? 22.551 -22.764 -14.084 1.00 56.54 ? 261 THR A C   1 
ATOM   1972 O  O   . THR A 1 268 ? 22.549 -23.972 -13.821 1.00 56.92 ? 261 THR A O   1 
ATOM   1973 C  CB  . THR A 1 268 ? 22.591 -22.017 -16.495 1.00 56.96 ? 261 THR A CB  1 
ATOM   1974 O  OG1 . THR A 1 268 ? 21.770 -21.489 -17.549 1.00 57.90 ? 261 THR A OG1 1 
ATOM   1975 C  CG2 . THR A 1 268 ? 23.248 -23.320 -16.954 1.00 49.91 ? 261 THR A CG2 1 
ATOM   1976 N  N   . ARG A 1 269 ? 23.247 -21.882 -13.356 1.00 52.39 ? 262 ARG A N   1 
ATOM   1977 C  CA  . ARG A 1 269 ? 24.063 -22.342 -12.233 1.00 51.57 ? 262 ARG A CA  1 
ATOM   1978 C  C   . ARG A 1 269 ? 23.216 -22.957 -11.121 1.00 61.35 ? 262 ARG A C   1 
ATOM   1979 O  O   . ARG A 1 269 ? 23.680 -23.863 -10.416 1.00 55.37 ? 262 ARG A O   1 
ATOM   1980 C  CB  . ARG A 1 269 ? 24.898 -21.187 -11.669 1.00 51.55 ? 262 ARG A CB  1 
ATOM   1981 C  CG  . ARG A 1 269 ? 26.161 -20.849 -12.459 1.00 39.37 ? 262 ARG A CG  1 
ATOM   1982 C  CD  . ARG A 1 269 ? 27.230 -21.966 -12.403 1.00 42.61 ? 262 ARG A CD  1 
ATOM   1983 N  NE  . ARG A 1 269 ? 27.448 -22.466 -11.048 1.00 44.69 ? 262 ARG A NE  1 
ATOM   1984 C  CZ  . ARG A 1 269 ? 28.308 -21.949 -10.178 1.00 38.35 ? 262 ARG A CZ  1 
ATOM   1985 N  NH1 . ARG A 1 269 ? 29.089 -20.932 -10.497 1.00 31.97 ? 262 ARG A NH1 1 
ATOM   1986 N  NH2 . ARG A 1 269 ? 28.374 -22.455 -8.950  1.00 45.09 ? 262 ARG A NH2 1 
ATOM   1987 N  N   . ALA A 1 270 ? 21.982 -22.480 -10.937 1.00 50.93 ? 263 ALA A N   1 
ATOM   1988 C  CA  . ALA A 1 270 ? 21.130 -23.044 -9.898  1.00 52.30 ? 263 ALA A CA  1 
ATOM   1989 C  C   . ALA A 1 270 ? 20.536 -24.390 -10.304 1.00 61.25 ? 263 ALA A C   1 
ATOM   1990 O  O   . ALA A 1 270 ? 20.271 -25.230 -9.435  1.00 64.24 ? 263 ALA A O   1 
ATOM   1991 C  CB  . ALA A 1 270 ? 20.000 -22.067 -9.549  1.00 53.07 ? 263 ALA A CB  1 
ATOM   1992 N  N   . LYS A 1 271 ? 20.318 -24.618 -11.599 1.00 59.55 ? 264 LYS A N   1 
ATOM   1993 C  CA  . LYS A 1 271 ? 19.678 -25.836 -12.075 1.00 60.93 ? 264 LYS A CA  1 
ATOM   1994 C  C   . LYS A 1 271 ? 20.659 -26.841 -12.678 1.00 62.56 ? 264 LYS A C   1 
ATOM   1995 O  O   . LYS A 1 271 ? 20.221 -27.868 -13.208 1.00 67.49 ? 264 LYS A O   1 
ATOM   1996 C  CB  . LYS A 1 271 ? 18.597 -25.493 -13.105 1.00 62.63 ? 264 LYS A CB  1 
ATOM   1997 N  N   . THR A 1 272 ? 21.968 -26.583 -12.613 1.00 62.28 ? 265 THR A N   1 
ATOM   1998 C  CA  . THR A 1 272 ? 22.959 -27.533 -13.109 1.00 56.58 ? 265 THR A CA  1 
ATOM   1999 C  C   . THR A 1 272 ? 24.095 -27.681 -12.104 1.00 59.58 ? 265 THR A C   1 
ATOM   2000 O  O   . THR A 1 272 ? 24.677 -26.685 -11.660 1.00 56.45 ? 265 THR A O   1 
ATOM   2001 C  CB  . THR A 1 272 ? 23.531 -27.114 -14.476 1.00 65.65 ? 265 THR A CB  1 
ATOM   2002 O  OG1 . THR A 1 272 ? 24.297 -25.907 -14.345 1.00 72.88 ? 265 THR A OG1 1 
ATOM   2003 C  CG2 . THR A 1 272 ? 22.412 -26.895 -15.484 1.00 67.22 ? 265 THR A CG2 1 
ATOM   2004 N  N   . SER A 1 273 ? 24.406 -28.925 -11.750 1.00 61.45 ? 266 SER A N   1 
ATOM   2005 C  CA  . SER A 1 273 ? 25.509 -29.200 -10.850 1.00 60.31 ? 266 SER A CA  1 
ATOM   2006 C  C   . SER A 1 273 ? 26.834 -28.828 -11.508 1.00 46.88 ? 266 SER A C   1 
ATOM   2007 O  O   . SER A 1 273 ? 26.966 -28.782 -12.737 1.00 48.55 ? 266 SER A O   1 
ATOM   2008 C  CB  . SER A 1 273 ? 25.538 -30.677 -10.463 1.00 58.50 ? 266 SER A CB  1 
ATOM   2009 O  OG  . SER A 1 273 ? 25.879 -31.468 -11.591 1.00 58.37 ? 266 SER A OG  1 
ATOM   2010 N  N   . ILE A 1 274 ? 27.835 -28.561 -10.671 1.00 56.20 ? 267 ILE A N   1 
ATOM   2011 C  CA  . ILE A 1 274 ? 29.167 -28.292 -11.204 1.00 50.82 ? 267 ILE A CA  1 
ATOM   2012 C  C   . ILE A 1 274 ? 29.643 -29.479 -12.030 1.00 51.75 ? 267 ILE A C   1 
ATOM   2013 O  O   . ILE A 1 274 ? 30.150 -29.324 -13.146 1.00 44.71 ? 267 ILE A O   1 
ATOM   2014 C  CB  . ILE A 1 274 ? 30.151 -27.966 -10.067 1.00 47.32 ? 267 ILE A CB  1 
ATOM   2015 C  CG1 . ILE A 1 274 ? 29.788 -26.620 -9.433  1.00 49.32 ? 267 ILE A CG1 1 
ATOM   2016 C  CG2 . ILE A 1 274 ? 31.566 -27.977 -10.597 1.00 42.13 ? 267 ILE A CG2 1 
ATOM   2017 C  CD1 . ILE A 1 274 ? 29.811 -25.462 -10.421 1.00 43.15 ? 267 ILE A CD1 1 
ATOM   2018 N  N   . ASN A 1 275 ? 29.473 -30.687 -11.490 1.00 58.99 ? 268 ASN A N   1 
ATOM   2019 C  CA  . ASN A 1 275 ? 29.806 -31.888 -12.245 1.00 61.39 ? 268 ASN A CA  1 
ATOM   2020 C  C   . ASN A 1 275 ? 29.120 -31.894 -13.602 1.00 63.71 ? 268 ASN A C   1 
ATOM   2021 O  O   . ASN A 1 275 ? 29.734 -32.250 -14.611 1.00 58.35 ? 268 ASN A O   1 
ATOM   2022 C  CB  . ASN A 1 275 ? 29.419 -33.125 -11.434 1.00 70.18 ? 268 ASN A CB  1 
ATOM   2023 C  CG  . ASN A 1 275 ? 30.262 -33.280 -10.187 1.00 64.04 ? 268 ASN A CG  1 
ATOM   2024 O  OD1 . ASN A 1 275 ? 31.332 -32.676 -10.074 1.00 74.04 ? 268 ASN A OD1 1 
ATOM   2025 N  ND2 . ASN A 1 275 ? 29.792 -34.091 -9.248  1.00 65.65 ? 268 ASN A ND2 1 
ATOM   2026 N  N   . ASP A 1 276 ? 27.848 -31.484 -13.647 1.00 57.16 ? 269 ASP A N   1 
ATOM   2027 C  CA  . ASP A 1 276 ? 27.081 -31.518 -14.885 1.00 62.28 ? 269 ASP A CA  1 
ATOM   2028 C  C   . ASP A 1 276 ? 27.394 -30.356 -15.816 1.00 58.69 ? 269 ASP A C   1 
ATOM   2029 O  O   . ASP A 1 276 ? 27.094 -30.444 -17.010 1.00 65.16 ? 269 ASP A O   1 
ATOM   2030 C  CB  . ASP A 1 276 ? 25.579 -31.527 -14.573 1.00 55.38 ? 269 ASP A CB  1 
ATOM   2031 N  N   . LEU A 1 277 ? 27.981 -29.268 -15.309 1.00 54.05 ? 270 LEU A N   1 
ATOM   2032 C  CA  . LEU A 1 277 ? 28.297 -28.142 -16.184 1.00 63.65 ? 270 LEU A CA  1 
ATOM   2033 C  C   . LEU A 1 277 ? 29.366 -28.496 -17.210 1.00 68.48 ? 270 LEU A C   1 
ATOM   2034 O  O   . LEU A 1 277 ? 29.600 -27.709 -18.133 1.00 67.63 ? 270 LEU A O   1 
ATOM   2035 C  CB  . LEU A 1 277 ? 28.733 -26.934 -15.353 1.00 60.79 ? 270 LEU A CB  1 
ATOM   2036 C  CG  . LEU A 1 277 ? 28.476 -25.562 -15.978 1.00 61.56 ? 270 LEU A CG  1 
ATOM   2037 C  CD1 . LEU A 1 277 ? 27.004 -25.328 -16.265 1.00 59.77 ? 270 LEU A CD1 1 
ATOM   2038 C  CD2 . LEU A 1 277 ? 28.997 -24.457 -15.070 1.00 61.45 ? 270 LEU A CD2 1 
ATOM   2039 N  N   . LEU A 1 278 ? 30.021 -29.646 -17.067 1.00 77.16 ? 271 LEU A N   1 
ATOM   2040 C  CA  . LEU A 1 278 ? 30.851 -30.218 -18.127 1.00 70.97 ? 271 LEU A CA  1 
ATOM   2041 C  C   . LEU A 1 278 ? 30.582 -31.730 -18.199 1.00 68.27 ? 271 LEU A C   1 
ATOM   2042 O  O   . LEU A 1 278 ? 30.009 -32.306 -17.273 1.00 54.24 ? 271 LEU A O   1 
ATOM   2043 C  CB  . LEU A 1 278 ? 32.331 -29.935 -17.881 1.00 57.43 ? 271 LEU A CB  1 
ATOM   2044 C  CG  . LEU A 1 278 ? 32.646 -28.474 -17.547 1.00 66.76 ? 271 LEU A CG  1 
ATOM   2045 C  CD1 . LEU A 1 278 ? 32.558 -28.208 -16.043 1.00 70.48 ? 271 LEU A CD1 1 
ATOM   2046 C  CD2 . LEU A 1 278 ? 34.016 -28.079 -18.081 1.00 45.27 ? 271 LEU A CD2 1 
ATOM   2047 O  OXT . LEU A 1 278 ? 30.913 -32.422 -19.167 1.00 64.86 ? 271 LEU A OXT 1 
HETATM 2048 CA CA  . CA  B 2 .   ? 48.377 -16.175 18.588  1.00 53.52 ? 301 CA  A CA  1 
HETATM 2049 CA CA  . CA  C 2 .   ? 54.823 7.623   16.814  1.00 26.28 ? 302 CA  A CA  1 
HETATM 2050 CA CA  . CA  D 2 .   ? 34.515 -17.073 24.266  1.00 46.17 ? 303 CA  A CA  1 
HETATM 2051 CL CL  . CL  E 3 .   ? 47.867 -4.689  15.917  1.00 49.57 ? 304 CL  A CL  1 
HETATM 2052 CL CL  . CL  F 3 .   ? 36.514 -4.298  -11.056 1.00 54.46 ? 305 CL  A CL  1 
HETATM 2053 CL CL  . CL  G 3 .   ? 55.250 -19.158 -28.500 1.00 42.06 ? 306 CL  A CL  1 
HETATM 2054 C  C1  . GOL H 4 .   ? 52.302 -8.734  -14.880 1.00 42.72 ? 307 GOL A C1  1 
HETATM 2055 O  O1  . GOL H 4 .   ? 52.757 -9.696  -15.806 1.00 46.30 ? 307 GOL A O1  1 
HETATM 2056 C  C2  . GOL H 4 .   ? 52.527 -7.350  -15.448 1.00 60.13 ? 307 GOL A C2  1 
HETATM 2057 O  O2  . GOL H 4 .   ? 53.092 -7.426  -16.732 1.00 61.87 ? 307 GOL A O2  1 
HETATM 2058 C  C3  . GOL H 4 .   ? 51.168 -6.669  -15.503 1.00 48.50 ? 307 GOL A C3  1 
HETATM 2059 O  O3  . GOL H 4 .   ? 50.393 -7.450  -16.397 1.00 36.87 ? 307 GOL A O3  1 
HETATM 2060 O  O   . HOH I 5 .   ? 44.431 11.354  17.645  1.00 33.80 ? 401 HOH A O   1 
HETATM 2061 O  O   . HOH I 5 .   ? 49.423 11.320  12.853  1.00 23.90 ? 402 HOH A O   1 
HETATM 2062 O  O   . HOH I 5 .   ? 54.896 13.160  7.579   1.00 32.91 ? 403 HOH A O   1 
HETATM 2063 O  O   . HOH I 5 .   ? 27.812 -21.710 -4.698  1.00 40.47 ? 404 HOH A O   1 
HETATM 2064 O  O   . HOH I 5 .   ? 47.292 -0.926  21.262  1.00 43.66 ? 405 HOH A O   1 
HETATM 2065 O  O   . HOH I 5 .   ? 52.557 -16.605 21.865  1.00 37.13 ? 406 HOH A O   1 
HETATM 2066 O  O   . HOH I 5 .   ? 38.692 -11.135 -19.868 1.00 37.47 ? 407 HOH A O   1 
HETATM 2067 O  O   . HOH I 5 .   ? 53.838 0.327   -3.160  1.00 40.01 ? 408 HOH A O   1 
HETATM 2068 O  O   . HOH I 5 .   ? 26.950 -22.234 1.111   1.00 48.24 ? 409 HOH A O   1 
HETATM 2069 O  O   . HOH I 5 .   ? 25.536 -15.702 -4.003  1.00 31.53 ? 410 HOH A O   1 
HETATM 2070 O  O   . HOH I 5 .   ? 27.994 -16.561 21.530  1.00 36.66 ? 411 HOH A O   1 
HETATM 2071 O  O   . HOH I 5 .   ? 51.311 -11.407 -23.442 1.00 46.31 ? 412 HOH A O   1 
HETATM 2072 O  O   . HOH I 5 .   ? 27.595 -23.368 5.094   1.00 42.99 ? 413 HOH A O   1 
HETATM 2073 O  O   . HOH I 5 .   ? 56.809 -26.076 14.198  1.00 19.60 ? 414 HOH A O   1 
HETATM 2074 O  O   . HOH I 5 .   ? 57.941 -29.589 -32.464 1.00 32.13 ? 415 HOH A O   1 
HETATM 2075 O  O   . HOH I 5 .   ? 52.209 -11.794 -14.311 1.00 25.97 ? 416 HOH A O   1 
HETATM 2076 O  O   . HOH I 5 .   ? 50.809 -16.037 12.319  1.00 16.86 ? 417 HOH A O   1 
HETATM 2077 O  O   . HOH I 5 .   ? 39.621 -7.143  3.744   1.00 16.14 ? 418 HOH A O   1 
HETATM 2078 O  O   . HOH I 5 .   ? 58.003 6.046   22.105  1.00 36.96 ? 419 HOH A O   1 
HETATM 2079 O  O   . HOH I 5 .   ? 32.202 -16.527 -23.862 1.00 36.35 ? 420 HOH A O   1 
HETATM 2080 O  O   . HOH I 5 .   ? 31.248 -7.067  6.598   1.00 33.65 ? 421 HOH A O   1 
HETATM 2081 O  O   . HOH I 5 .   ? 46.514 -27.346 -16.067 1.00 23.25 ? 422 HOH A O   1 
HETATM 2082 O  O   . HOH I 5 .   ? 47.296 -18.157 -2.124  1.00 42.31 ? 423 HOH A O   1 
HETATM 2083 O  O   . HOH I 5 .   ? 48.848 -28.202 -25.288 0.33 20.22 ? 424 HOH A O   1 
HETATM 2084 O  O   . HOH I 5 .   ? 43.869 -19.335 16.566  1.00 35.10 ? 425 HOH A O   1 
HETATM 2085 O  O   . HOH I 5 .   ? 44.890 -13.405 -17.113 1.00 16.79 ? 426 HOH A O   1 
HETATM 2086 O  O   . HOH I 5 .   ? 50.998 -10.803 -0.030  1.00 32.37 ? 427 HOH A O   1 
HETATM 2087 O  O   . HOH I 5 .   ? 43.819 -8.548  -25.668 1.00 31.52 ? 428 HOH A O   1 
HETATM 2088 O  O   . HOH I 5 .   ? 41.264 -29.682 -15.844 1.00 27.07 ? 429 HOH A O   1 
HETATM 2089 O  O   . HOH I 5 .   ? 51.721 -10.364 -4.192  1.00 41.25 ? 430 HOH A O   1 
HETATM 2090 O  O   . HOH I 5 .   ? 24.586 -19.139 2.051   1.00 46.70 ? 431 HOH A O   1 
HETATM 2091 O  O   . HOH I 5 .   ? 51.507 -13.622 -21.617 1.00 39.17 ? 432 HOH A O   1 
HETATM 2092 O  O   . HOH I 5 .   ? 31.381 -14.203 11.411  1.00 21.00 ? 433 HOH A O   1 
HETATM 2093 O  O   . HOH I 5 .   ? 44.181 -13.022 18.076  1.00 29.11 ? 434 HOH A O   1 
HETATM 2094 O  O   . HOH I 5 .   ? 38.145 -20.926 -31.114 1.00 25.64 ? 435 HOH A O   1 
HETATM 2095 O  O   . HOH I 5 .   ? 45.222 6.387   18.059  1.00 27.65 ? 436 HOH A O   1 
HETATM 2096 O  O   . HOH I 5 .   ? 46.673 -8.253  -17.171 1.00 19.43 ? 437 HOH A O   1 
HETATM 2097 O  O   . HOH I 5 .   ? 29.070 -10.957 5.588   1.00 48.41 ? 438 HOH A O   1 
HETATM 2098 O  O   . HOH I 5 .   ? 43.067 -31.063 -0.989  1.00 25.34 ? 439 HOH A O   1 
HETATM 2099 O  O   . HOH I 5 .   ? 60.102 6.851   7.303   1.00 31.58 ? 440 HOH A O   1 
HETATM 2100 O  O   . HOH I 5 .   ? 40.073 -8.719  6.679   1.00 36.62 ? 441 HOH A O   1 
HETATM 2101 O  O   . HOH I 5 .   ? 31.882 -9.289  12.790  1.00 35.14 ? 442 HOH A O   1 
HETATM 2102 O  O   . HOH I 5 .   ? 39.627 7.528   8.888   1.00 44.21 ? 443 HOH A O   1 
HETATM 2103 O  O   . HOH I 5 .   ? 41.049 -12.336 16.061  1.00 35.38 ? 444 HOH A O   1 
HETATM 2104 O  O   . HOH I 5 .   ? 56.442 -1.231  7.179   1.00 37.64 ? 445 HOH A O   1 
HETATM 2105 O  O   . HOH I 5 .   ? 49.345 -8.124  12.495  1.00 26.17 ? 446 HOH A O   1 
HETATM 2106 O  O   . HOH I 5 .   ? 35.620 -12.259 -26.698 1.00 26.97 ? 447 HOH A O   1 
HETATM 2107 O  O   . HOH I 5 .   ? 40.189 -8.396  -19.488 1.00 37.22 ? 448 HOH A O   1 
HETATM 2108 O  O   . HOH I 5 .   ? 46.399 -23.758 -16.221 1.00 33.26 ? 449 HOH A O   1 
HETATM 2109 O  O   . HOH I 5 .   ? 34.223 2.264   3.148   1.00 44.00 ? 450 HOH A O   1 
HETATM 2110 O  O   . HOH I 5 .   ? 39.102 -13.382 -24.069 1.00 24.26 ? 451 HOH A O   1 
HETATM 2111 O  O   . HOH I 5 .   ? 44.809 -10.803 -2.772  1.00 16.17 ? 452 HOH A O   1 
HETATM 2112 O  O   . HOH I 5 .   ? 51.888 -8.378  13.474  1.00 29.00 ? 453 HOH A O   1 
HETATM 2113 O  O   . HOH I 5 .   ? 41.481 -18.292 -33.123 1.00 37.52 ? 454 HOH A O   1 
HETATM 2114 O  O   . HOH I 5 .   ? 33.945 -7.031  -11.240 1.00 32.91 ? 455 HOH A O   1 
HETATM 2115 O  O   . HOH I 5 .   ? 34.580 -26.518 2.826   1.00 27.26 ? 456 HOH A O   1 
HETATM 2116 O  O   . HOH I 5 .   ? 31.446 -0.929  8.103   1.00 48.21 ? 457 HOH A O   1 
HETATM 2117 O  O   . HOH I 5 .   ? 29.971 -8.516  2.431   1.00 37.77 ? 458 HOH A O   1 
HETATM 2118 O  O   . HOH I 5 .   ? 49.167 -12.823 -5.731  1.00 18.83 ? 459 HOH A O   1 
HETATM 2119 O  O   . HOH I 5 .   ? 58.843 -23.001 24.690  1.00 49.03 ? 460 HOH A O   1 
HETATM 2120 O  O   . HOH I 5 .   ? 56.035 -4.152  7.319   1.00 27.35 ? 461 HOH A O   1 
HETATM 2121 O  O   . HOH I 5 .   ? 55.064 11.404  9.598   1.00 19.37 ? 462 HOH A O   1 
HETATM 2122 O  O   . HOH I 5 .   ? 46.860 -26.773 -20.867 1.00 20.06 ? 463 HOH A O   1 
HETATM 2123 O  O   . HOH I 5 .   ? 49.455 -18.202 11.052  1.00 17.17 ? 464 HOH A O   1 
HETATM 2124 O  O   . HOH I 5 .   ? 47.881 -26.709 -1.407  1.00 29.54 ? 465 HOH A O   1 
HETATM 2125 O  O   . HOH I 5 .   ? 46.666 -23.747 -1.573  1.00 25.66 ? 466 HOH A O   1 
HETATM 2126 O  O   . HOH I 5 .   ? 62.969 -12.180 16.420  1.00 30.76 ? 467 HOH A O   1 
HETATM 2127 O  O   . HOH I 5 .   ? 44.383 1.848   -6.555  1.00 43.22 ? 468 HOH A O   1 
HETATM 2128 O  O   . HOH I 5 .   ? 38.028 -7.352  6.164   1.00 21.90 ? 469 HOH A O   1 
HETATM 2129 O  O   . HOH I 5 .   ? 44.283 -6.303  -15.331 1.00 20.04 ? 470 HOH A O   1 
HETATM 2130 O  O   . HOH I 5 .   ? 34.901 -14.193 14.866  1.00 28.78 ? 471 HOH A O   1 
HETATM 2131 O  O   . HOH I 5 .   ? 48.151 -18.855 -31.427 1.00 32.36 ? 472 HOH A O   1 
HETATM 2132 O  O   . HOH I 5 .   ? 41.887 -6.733  -8.556  1.00 26.88 ? 473 HOH A O   1 
HETATM 2133 O  O   . HOH I 5 .   ? 41.806 -13.959 19.081  1.00 31.30 ? 474 HOH A O   1 
HETATM 2134 O  O   . HOH I 5 .   ? 60.107 -20.697 -37.314 1.00 48.49 ? 475 HOH A O   1 
HETATM 2135 O  O   . HOH I 5 .   ? 58.224 -11.351 21.813  1.00 42.10 ? 476 HOH A O   1 
HETATM 2136 O  O   . HOH I 5 .   ? 51.635 -19.931 -28.089 1.00 27.97 ? 477 HOH A O   1 
HETATM 2137 O  O   . HOH I 5 .   ? 46.384 -6.208  -8.847  1.00 37.33 ? 478 HOH A O   1 
HETATM 2138 O  O   . HOH I 5 .   ? 42.568 -7.833  -12.757 1.00 21.67 ? 479 HOH A O   1 
HETATM 2139 O  O   . HOH I 5 .   ? 35.456 -29.591 -5.474  1.00 38.40 ? 480 HOH A O   1 
HETATM 2140 O  O   . HOH I 5 .   ? 31.797 -9.622  -0.355  1.00 34.37 ? 481 HOH A O   1 
HETATM 2141 O  O   . HOH I 5 .   ? 33.608 -19.782 -25.589 1.00 24.12 ? 482 HOH A O   1 
HETATM 2142 O  O   . HOH I 5 .   ? 29.722 -23.168 8.972   1.00 25.64 ? 483 HOH A O   1 
HETATM 2143 O  O   . HOH I 5 .   ? 25.565 -33.855 -13.053 1.00 49.09 ? 484 HOH A O   1 
HETATM 2144 O  O   . HOH I 5 .   ? 50.194 -22.973 -35.709 1.00 40.28 ? 485 HOH A O   1 
HETATM 2145 O  O   . HOH I 5 .   ? 49.463 -2.082  17.266  1.00 35.32 ? 486 HOH A O   1 
HETATM 2146 O  O   . HOH I 5 .   ? 29.714 -22.552 -0.918  1.00 34.91 ? 487 HOH A O   1 
HETATM 2147 O  O   . HOH I 5 .   ? 47.093 6.071   1.950   1.00 26.46 ? 488 HOH A O   1 
HETATM 2148 O  O   . HOH I 5 .   ? 50.780 9.118   12.986  1.00 28.20 ? 489 HOH A O   1 
HETATM 2149 O  O   . HOH I 5 .   ? 30.649 -8.603  -11.925 1.00 39.59 ? 490 HOH A O   1 
HETATM 2150 O  O   . HOH I 5 .   ? 59.870 11.097  13.722  1.00 27.03 ? 491 HOH A O   1 
HETATM 2151 O  O   . HOH I 5 .   ? 33.446 -14.157 17.245  1.00 34.20 ? 492 HOH A O   1 
HETATM 2152 O  O   . HOH I 5 .   ? 50.264 -15.072 -2.076  1.00 31.23 ? 493 HOH A O   1 
HETATM 2153 O  O   . HOH I 5 .   ? 51.282 7.760   3.849   1.00 27.06 ? 494 HOH A O   1 
HETATM 2154 O  O   . HOH I 5 .   ? 47.671 -25.475 -28.937 1.00 15.07 ? 495 HOH A O   1 
HETATM 2155 O  O   . HOH I 5 .   ? 32.732 -3.872  5.408   1.00 38.98 ? 496 HOH A O   1 
HETATM 2156 O  O   . HOH I 5 .   ? 34.017 -10.591 -1.030  1.00 26.13 ? 497 HOH A O   1 
HETATM 2157 O  O   . HOH I 5 .   ? 59.862 -4.975  13.296  1.00 41.59 ? 498 HOH A O   1 
HETATM 2158 O  O   . HOH I 5 .   ? 41.882 -7.371  -16.534 1.00 27.32 ? 499 HOH A O   1 
HETATM 2159 O  O   . HOH I 5 .   ? 25.794 -23.484 8.834   1.00 49.71 ? 500 HOH A O   1 
HETATM 2160 O  O   . HOH I 5 .   ? 40.848 -28.983 -20.502 1.00 18.61 ? 501 HOH A O   1 
HETATM 2161 O  O   . HOH I 5 .   ? 51.911 6.533   -0.047  1.00 39.56 ? 502 HOH A O   1 
HETATM 2162 O  O   . HOH I 5 .   ? 35.351 -13.035 11.476  1.00 22.30 ? 503 HOH A O   1 
HETATM 2163 O  O   . HOH I 5 .   ? 24.916 -13.172 -3.612  1.00 47.81 ? 504 HOH A O   1 
HETATM 2164 O  O   . HOH I 5 .   ? 47.376 -20.967 -17.418 1.00 39.75 ? 505 HOH A O   1 
HETATM 2165 O  O   . HOH I 5 .   ? 49.213 -17.954 -21.124 1.00 23.50 ? 506 HOH A O   1 
HETATM 2166 O  O   . HOH I 5 .   ? 38.721 -1.899  18.110  1.00 42.38 ? 507 HOH A O   1 
HETATM 2167 O  O   . HOH I 5 .   ? 32.775 -22.161 -27.296 1.00 25.84 ? 508 HOH A O   1 
HETATM 2168 O  O   . HOH I 5 .   ? 58.279 -7.859  9.667   1.00 36.55 ? 509 HOH A O   1 
HETATM 2169 O  O   . HOH I 5 .   ? 38.628 -14.118 -34.008 1.00 50.52 ? 510 HOH A O   1 
HETATM 2170 O  O   . HOH I 5 .   ? 40.199 -5.049  -9.654  1.00 35.78 ? 511 HOH A O   1 
HETATM 2171 O  O   . HOH I 5 .   ? 41.779 -21.327 7.443   1.00 21.95 ? 512 HOH A O   1 
HETATM 2172 O  O   . HOH I 5 .   ? 26.206 -25.145 -9.666  1.00 45.48 ? 513 HOH A O   1 
HETATM 2173 O  O   . HOH I 5 .   ? 38.235 -30.669 -3.399  1.00 37.11 ? 514 HOH A O   1 
HETATM 2174 O  O   . HOH I 5 .   ? 34.268 -13.506 -22.828 1.00 47.64 ? 515 HOH A O   1 
HETATM 2175 O  O   . HOH I 5 .   ? 48.917 -19.618 -2.716  1.00 35.76 ? 516 HOH A O   1 
HETATM 2176 O  O   . HOH I 5 .   ? 41.871 8.282   0.460   1.00 51.58 ? 517 HOH A O   1 
HETATM 2177 O  O   . HOH I 5 .   ? 42.856 0.290   19.492  1.00 39.95 ? 518 HOH A O   1 
HETATM 2178 O  O   . HOH I 5 .   ? 38.744 8.635   12.645  1.00 41.75 ? 519 HOH A O   1 
HETATM 2179 O  O   . HOH I 5 .   ? 54.706 4.336   0.102   1.00 36.20 ? 520 HOH A O   1 
HETATM 2180 O  O   . HOH I 5 .   ? 31.437 -19.454 -32.186 1.00 54.10 ? 521 HOH A O   1 
HETATM 2181 O  O   . HOH I 5 .   ? 52.161 -8.792  -1.901  1.00 43.85 ? 522 HOH A O   1 
HETATM 2182 O  O   . HOH I 5 .   ? 61.315 -9.953  16.672  1.00 33.92 ? 523 HOH A O   1 
HETATM 2183 O  O   . HOH I 5 .   ? 48.541 16.937  10.094  1.00 32.47 ? 524 HOH A O   1 
HETATM 2184 O  O   . HOH I 5 .   ? 43.221 4.334   -1.349  1.00 39.69 ? 525 HOH A O   1 
HETATM 2185 O  O   . HOH I 5 .   ? 32.760 -15.289 -21.357 1.00 32.13 ? 526 HOH A O   1 
HETATM 2186 O  O   . HOH I 5 .   ? 54.129 -17.550 -32.250 1.00 43.74 ? 527 HOH A O   1 
HETATM 2187 O  O   . HOH I 5 .   ? 28.441 -26.475 8.361   1.00 33.04 ? 528 HOH A O   1 
HETATM 2188 O  O   . HOH I 5 .   ? 38.044 -30.741 1.267   1.00 25.46 ? 529 HOH A O   1 
HETATM 2189 O  O   . HOH I 5 .   ? 47.124 -9.387  13.297  1.00 30.92 ? 530 HOH A O   1 
HETATM 2190 O  O   . HOH I 5 .   ? 30.770 -7.646  9.502   1.00 42.49 ? 531 HOH A O   1 
HETATM 2191 O  O   . HOH I 5 .   ? 29.277 -22.346 13.561  1.00 39.17 ? 532 HOH A O   1 
HETATM 2192 O  O   . HOH I 5 .   ? 49.326 -19.203 -24.531 1.00 22.61 ? 533 HOH A O   1 
HETATM 2193 O  O   . HOH I 5 .   ? 39.107 6.097   15.475  1.00 49.62 ? 534 HOH A O   1 
HETATM 2194 O  O   . HOH I 5 .   ? 28.124 -9.655  -2.188  1.00 54.51 ? 535 HOH A O   1 
HETATM 2195 O  O   . HOH I 5 .   ? 50.965 -20.228 22.732  1.00 37.00 ? 536 HOH A O   1 
HETATM 2196 O  O   . HOH I 5 .   ? 51.562 -7.698  -6.366  1.00 42.15 ? 537 HOH A O   1 
HETATM 2197 O  O   . HOH I 5 .   ? 32.088 -4.985  -1.660  1.00 34.48 ? 538 HOH A O   1 
HETATM 2198 O  O   . HOH I 5 .   ? 57.403 5.766   0.592   1.00 55.53 ? 539 HOH A O   1 
HETATM 2199 O  O   . HOH I 5 .   ? 33.929 -31.634 -11.191 1.00 54.51 ? 540 HOH A O   1 
HETATM 2200 O  O   . HOH I 5 .   ? 36.530 -0.479  4.510   1.00 28.71 ? 541 HOH A O   1 
HETATM 2201 O  O   . HOH I 5 .   ? 31.256 -5.047  3.175   1.00 37.20 ? 542 HOH A O   1 
HETATM 2202 O  O   . HOH I 5 .   ? 51.538 -12.421 -26.581 1.00 39.12 ? 543 HOH A O   1 
HETATM 2203 O  O   . HOH I 5 .   ? 52.167 -13.176 4.717   1.00 27.01 ? 544 HOH A O   1 
HETATM 2204 O  O   . HOH I 5 .   ? 52.258 -10.175 18.067  1.00 41.15 ? 545 HOH A O   1 
HETATM 2205 O  O   . HOH I 5 .   ? 49.498 -13.998 1.057   1.00 17.67 ? 546 HOH A O   1 
HETATM 2206 O  O   . HOH I 5 .   ? 34.663 -22.871 25.845  1.00 37.94 ? 547 HOH A O   1 
HETATM 2207 O  O   . HOH I 5 .   ? 29.879 -22.207 -6.062  1.00 36.57 ? 548 HOH A O   1 
HETATM 2208 O  O   . HOH I 5 .   ? 55.881 -6.991  20.317  1.00 34.33 ? 549 HOH A O   1 
HETATM 2209 O  O   . HOH I 5 .   ? 37.447 -29.807 -8.237  1.00 20.74 ? 550 HOH A O   1 
HETATM 2210 O  O   . HOH I 5 .   ? 38.272 4.394   3.746   1.00 34.64 ? 551 HOH A O   1 
HETATM 2211 O  O   . HOH I 5 .   ? 32.659 -19.364 26.177  1.00 37.76 ? 552 HOH A O   1 
HETATM 2212 O  O   . HOH I 5 .   ? 34.259 -10.822 -3.592  1.00 20.62 ? 553 HOH A O   1 
HETATM 2213 O  O   . HOH I 5 .   ? 36.103 -10.202 -34.946 1.00 47.93 ? 554 HOH A O   1 
HETATM 2214 O  O   . HOH I 5 .   ? 40.851 4.941   0.514   1.00 30.37 ? 555 HOH A O   1 
HETATM 2215 O  O   . HOH I 5 .   ? 58.513 -0.015  3.068   1.00 47.85 ? 556 HOH A O   1 
HETATM 2216 O  O   . HOH I 5 .   ? 27.808 -13.304 12.978  1.00 37.38 ? 557 HOH A O   1 
HETATM 2217 O  O   . HOH I 5 .   ? 28.357 -23.150 11.272  1.00 32.00 ? 558 HOH A O   1 
HETATM 2218 O  O   . HOH I 5 .   ? 56.491 -19.356 -34.289 1.00 31.90 ? 559 HOH A O   1 
HETATM 2219 O  O   . HOH I 5 .   ? 29.925 -10.542 -6.330  1.00 33.71 ? 560 HOH A O   1 
HETATM 2220 O  O   . HOH I 5 .   ? 46.909 2.530   24.902  1.00 50.01 ? 561 HOH A O   1 
HETATM 2221 O  O   . HOH I 5 .   ? 40.897 -12.897 -33.988 1.00 41.18 ? 562 HOH A O   1 
HETATM 2222 O  O   . HOH I 5 .   ? 28.265 -20.040 -24.259 1.00 37.85 ? 563 HOH A O   1 
HETATM 2223 O  O   . HOH I 5 .   ? 22.834 -19.860 -19.949 1.00 42.27 ? 564 HOH A O   1 
HETATM 2224 O  O   . HOH I 5 .   ? 31.565 -10.380 -4.405  1.00 35.91 ? 565 HOH A O   1 
HETATM 2225 O  O   . HOH I 5 .   ? 59.162 7.714   15.881  1.00 40.19 ? 566 HOH A O   1 
HETATM 2226 O  O   . HOH I 5 .   ? 57.648 6.784   17.794  1.00 43.48 ? 567 HOH A O   1 
HETATM 2227 O  O   . HOH I 5 .   ? 58.553 -15.033 22.985  1.00 27.05 ? 568 HOH A O   1 
HETATM 2228 O  O   . HOH I 5 .   ? 56.259 7.401   2.561   1.00 33.50 ? 569 HOH A O   1 
HETATM 2229 O  O   . HOH I 5 .   ? 33.214 -31.118 6.887   1.00 21.58 ? 570 HOH A O   1 
HETATM 2230 O  O   . HOH I 5 .   ? 43.856 5.308   0.985   1.00 30.65 ? 571 HOH A O   1 
HETATM 2231 O  O   . HOH I 5 .   ? 37.369 -30.032 -13.450 1.00 29.89 ? 572 HOH A O   1 
HETATM 2232 O  O   . HOH I 5 .   ? 23.169 -17.612 9.574   1.00 43.39 ? 573 HOH A O   1 
HETATM 2233 O  O   . HOH I 5 .   ? 50.386 -18.028 -26.728 1.00 26.36 ? 574 HOH A O   1 
HETATM 2234 O  O   . HOH I 5 .   ? 41.682 1.321   -6.528  1.00 38.52 ? 575 HOH A O   1 
HETATM 2235 O  O   . HOH I 5 .   ? 52.427 -13.218 17.785  1.00 34.88 ? 576 HOH A O   1 
HETATM 2236 O  O   . HOH I 5 .   ? 45.122 -22.298 -17.328 1.00 39.75 ? 577 HOH A O   1 
HETATM 2237 O  O   . HOH I 5 .   ? 28.257 -12.850 8.160   1.00 22.80 ? 578 HOH A O   1 
HETATM 2238 O  O   . HOH I 5 .   ? 61.428 -10.596 11.711  1.00 28.48 ? 579 HOH A O   1 
HETATM 2239 O  O   . HOH I 5 .   ? 38.953 -33.565 2.234   1.00 13.47 ? 580 HOH A O   1 
HETATM 2240 O  O   . HOH I 5 .   ? 52.413 -16.034 -25.198 1.00 39.80 ? 581 HOH A O   1 
HETATM 2241 O  O   . HOH I 5 .   ? 42.762 4.604   17.397  1.00 40.17 ? 582 HOH A O   1 
HETATM 2242 O  O   . HOH I 5 .   ? 41.198 -5.703  -13.575 1.00 46.13 ? 583 HOH A O   1 
HETATM 2243 O  O   . HOH I 5 .   ? 58.957 -20.642 -32.402 1.00 45.03 ? 584 HOH A O   1 
HETATM 2244 O  O   . HOH I 5 .   ? 36.941 -12.996 -22.188 1.00 35.82 ? 585 HOH A O   1 
HETATM 2245 O  O   . HOH I 5 .   ? 33.797 -1.286  4.561   1.00 38.06 ? 586 HOH A O   1 
HETATM 2246 O  O   . HOH I 5 .   ? 48.613 -16.677 -0.959  1.00 38.67 ? 587 HOH A O   1 
HETATM 2247 O  O   . HOH I 5 .   ? 63.267 10.511  9.044   1.00 41.40 ? 588 HOH A O   1 
HETATM 2248 O  O   . HOH I 5 .   ? 28.002 -24.349 7.289   1.00 37.36 ? 589 HOH A O   1 
HETATM 2249 O  O   . HOH I 5 .   ? 49.548 -5.930  -12.684 1.00 40.25 ? 590 HOH A O   1 
HETATM 2250 O  O   . HOH I 5 .   ? 34.996 -12.715 19.164  1.00 46.18 ? 591 HOH A O   1 
HETATM 2251 O  O   . HOH I 5 .   ? 56.731 -2.266  4.979   1.00 36.06 ? 592 HOH A O   1 
HETATM 2252 O  O   . HOH I 5 .   ? 58.080 -28.102 14.378  1.00 40.70 ? 593 HOH A O   1 
HETATM 2253 O  O   . HOH I 5 .   ? 31.569 -18.768 -24.378 1.00 36.60 ? 594 HOH A O   1 
HETATM 2254 O  O   . HOH I 5 .   ? 58.116 -5.202  8.949   1.00 40.10 ? 595 HOH A O   1 
HETATM 2255 O  O   . HOH I 5 .   ? 45.856 -4.309  -10.227 1.00 53.90 ? 596 HOH A O   1 
HETATM 2256 O  O   . HOH I 5 .   ? 29.739 -24.869 -5.934  1.00 40.66 ? 597 HOH A O   1 
HETATM 2257 O  O   . HOH I 5 .   ? 53.259 15.503  7.285   1.00 51.80 ? 598 HOH A O   1 
HETATM 2258 O  O   . HOH I 5 .   ? 33.389 -28.658 3.382   1.00 44.18 ? 599 HOH A O   1 
HETATM 2259 O  O   . HOH I 5 .   ? 56.610 -29.833 -35.223 1.00 43.79 ? 600 HOH A O   1 
HETATM 2260 O  O   . HOH I 5 .   ? 60.709 5.540   4.533   1.00 42.41 ? 601 HOH A O   1 
HETATM 2261 O  O   . HOH I 5 .   ? 25.653 -16.767 19.557  1.00 45.80 ? 602 HOH A O   1 
HETATM 2262 O  O   . HOH I 5 .   ? 30.067 -4.843  9.827   1.00 47.82 ? 603 HOH A O   1 
HETATM 2263 O  O   . HOH I 5 .   ? 37.070 2.285   4.681   1.00 33.45 ? 604 HOH A O   1 
HETATM 2264 O  O   . HOH I 5 .   ? 51.421 -10.977 4.229   1.00 48.41 ? 605 HOH A O   1 
HETATM 2265 O  O   . HOH I 5 .   ? 33.257 -12.461 13.015  1.00 42.03 ? 606 HOH A O   1 
HETATM 2266 O  O   . HOH I 5 .   ? 35.397 -31.293 1.859   1.00 42.81 ? 607 HOH A O   1 
HETATM 2267 O  O   . HOH I 5 .   ? 50.969 -17.453 -23.031 1.00 37.52 ? 608 HOH A O   1 
HETATM 2268 O  O   . HOH I 5 .   ? 30.776 -7.981  -2.098  1.00 46.78 ? 609 HOH A O   1 
HETATM 2269 O  O   . HOH I 5 .   ? 29.430 -12.423 11.027  1.00 28.91 ? 610 HOH A O   1 
HETATM 2270 O  O   . HOH I 5 .   ? 37.014 -9.597  -23.367 1.00 40.72 ? 611 HOH A O   1 
HETATM 2271 O  O   . HOH I 5 .   ? 32.457 -22.236 -30.022 1.00 42.96 ? 612 HOH A O   1 
HETATM 2272 O  O   . HOH I 5 .   ? 39.655 -31.815 -1.081  1.00 42.43 ? 613 HOH A O   1 
HETATM 2273 O  O   . HOH I 5 .   ? 45.300 -11.133 19.528  1.00 40.85 ? 614 HOH A O   1 
HETATM 2274 O  O   . HOH I 5 .   ? 45.721 6.680   -0.846  1.00 42.40 ? 615 HOH A O   1 
HETATM 2275 O  O   . HOH I 5 .   ? 57.371 -18.775 -31.239 1.00 39.92 ? 616 HOH A O   1 
HETATM 2276 O  O   . HOH I 5 .   ? 29.630 -9.859  11.423  1.00 41.58 ? 617 HOH A O   1 
HETATM 2277 O  O   . HOH I 5 .   ? 35.404 -8.290  -32.261 1.00 42.35 ? 618 HOH A O   1 
HETATM 2278 O  O   . HOH I 5 .   ? 49.570 -22.187 -17.321 1.00 37.77 ? 619 HOH A O   1 
HETATM 2279 O  O   . HOH I 5 .   ? 52.977 -18.294 -21.439 1.00 34.59 ? 620 HOH A O   1 
HETATM 2280 O  O   . HOH I 5 .   ? 60.255 -4.384  10.626  1.00 47.44 ? 621 HOH A O   1 
HETATM 2281 O  O   . HOH I 5 .   ? 48.848 -28.202 -22.433 0.33 20.39 ? 622 HOH A O   1 
HETATM 2282 O  O   . HOH I 5 .   ? 48.848 -28.202 -14.874 0.33 18.15 ? 623 HOH A O   1 
HETATM 2283 O  O   . HOH I 5 .   ? 25.608 -12.036 5.084   1.00 46.12 ? 624 HOH A O   1 
HETATM 2284 O  O   . HOH I 5 .   ? 52.249 -19.454 -18.055 1.00 33.19 ? 625 HOH A O   1 
HETATM 2285 O  O   . HOH I 5 .   ? 49.740 -25.656 -35.126 1.00 43.33 ? 626 HOH A O   1 
HETATM 2286 O  O   . HOH I 5 .   ? 51.257 -15.688 -5.658  1.00 48.65 ? 627 HOH A O   1 
HETATM 2287 O  O   . HOH I 5 .   ? 50.988 -14.251 19.564  1.00 49.71 ? 628 HOH A O   1 
HETATM 2288 O  O   . HOH I 5 .   ? 49.106 -24.592 -17.150 1.00 33.23 ? 629 HOH A O   1 
HETATM 2289 O  O   . HOH I 5 .   ? 47.621 -27.105 -18.454 1.00 29.89 ? 630 HOH A O   1 
HETATM 2290 O  O   . HOH I 5 .   ? 36.215 -30.704 -10.667 1.00 50.76 ? 631 HOH A O   1 
HETATM 2291 O  O   . HOH I 5 .   ? 25.446 -13.251 7.687   1.00 41.26 ? 632 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 8   ? 0.7736 1.0097 0.7350 0.0824  0.2724  -0.0770 1   HIS A N   
2    C CA  . HIS A 8   ? 0.7724 1.0435 0.8225 0.1034  0.2718  -0.0791 1   HIS A CA  
3    C C   . HIS A 8   ? 0.8053 1.0208 0.8458 0.1290  0.2401  -0.1063 1   HIS A C   
4    O O   . HIS A 8   ? 0.8477 1.0460 0.8763 0.1623  0.2402  -0.1293 1   HIS A O   
5    C CB  . HIS A 8   ? 0.6107 0.9145 0.7109 0.1206  0.3179  -0.0811 1   HIS A CB  
6    N N   . THR A 9   ? 0.8374 1.0190 0.8826 0.1114  0.2133  -0.1021 2   THR A N   
7    C CA  . THR A 9   ? 0.8967 1.0157 0.9327 0.1291  0.1838  -0.1178 2   THR A CA  
8    C C   . THR A 9   ? 1.0110 1.1414 1.1067 0.1649  0.1851  -0.1211 2   THR A C   
9    O O   . THR A 9   ? 1.0601 1.2638 1.2318 0.1717  0.1962  -0.1095 2   THR A O   
10   C CB  . THR A 9   ? 0.8771 0.9704 0.9236 0.1028  0.1589  -0.1054 2   THR A CB  
11   O OG1 . THR A 9   ? 0.8499 0.9983 0.9400 0.0774  0.1578  -0.0801 2   THR A OG1 
12   C CG2 . THR A 9   ? 0.6727 0.7058 0.6458 0.0810  0.1452  -0.1060 2   THR A CG2 
13   N N   . LEU A 10  ? 1.0616 1.1164 1.1378 0.1777  0.1741  -0.1363 3   LEU A N   
14   C CA  . LEU A 10  ? 1.0212 1.0779 1.1551 0.2119  0.1674  -0.1396 3   LEU A CA  
15   C C   . LEU A 10  ? 0.9628 1.0496 1.1539 0.2139  0.1329  -0.1205 3   LEU A C   
16   O O   . LEU A 10  ? 0.9699 1.1130 1.2354 0.2337  0.1295  -0.1104 3   LEU A O   
17   C CB  . LEU A 10  ? 0.7959 0.7681 0.8945 0.2198  0.1548  -0.1599 3   LEU A CB  
18   N N   . ASP A 11  ? 0.5809 0.6302 0.7416 0.1899  0.1043  -0.1155 4   ASP A N   
19   C CA  . ASP A 11  ? 0.5312 0.6061 0.7296 0.1718  0.0743  -0.0914 4   ASP A CA  
20   C C   . ASP A 11  ? 0.4300 0.4898 0.5767 0.1295  0.0696  -0.0796 4   ASP A C   
21   O O   . ASP A 11  ? 0.3778 0.3789 0.4682 0.1170  0.0582  -0.0812 4   ASP A O   
22   C CB  . ASP A 11  ? 0.5846 0.6126 0.7881 0.1821  0.0344  -0.0800 4   ASP A CB  
23   C CG  . ASP A 11  ? 0.5832 0.6393 0.8116 0.1598  0.0036  -0.0522 4   ASP A CG  
24   O OD1 . ASP A 11  ? 0.7403 0.8660 1.0216 0.1528  0.0094  -0.0443 4   ASP A OD1 
25   O OD2 . ASP A 11  ? 0.5279 0.5373 0.7192 0.1459  -0.0260 -0.0379 4   ASP A OD2 
26   N N   . LEU A 12  ? 0.3955 0.5096 0.5702 0.1078  0.0753  -0.0659 5   LEU A N   
27   C CA  . LEU A 12  ? 0.3355 0.4344 0.4685 0.0720  0.0709  -0.0564 5   LEU A CA  
28   C C   . LEU A 12  ? 0.3208 0.3733 0.4224 0.0589  0.0388  -0.0482 5   LEU A C   
29   O O   . LEU A 12  ? 0.3007 0.3145 0.3525 0.0444  0.0381  -0.0504 5   LEU A O   
30   C CB  . LEU A 12  ? 0.3546 0.5154 0.5330 0.0510  0.0761  -0.0409 5   LEU A CB  
31   C CG  . LEU A 12  ? 0.2351 0.3763 0.3804 0.0149  0.0656  -0.0298 5   LEU A CG  
32   C CD1 . LEU A 12  ? 0.3940 0.5032 0.4819 0.0092  0.0856  -0.0371 5   LEU A CD1 
33   C CD2 . LEU A 12  ? 0.2896 0.4904 0.4905 -0.0078 0.0653  -0.0117 5   LEU A CD2 
34   N N   . GLN A 13  ? 0.2607 0.3208 0.3910 0.0637  0.0123  -0.0375 6   GLN A N   
35   C CA  . GLN A 13  ? 0.2879 0.3064 0.3767 0.0504  -0.0139 -0.0295 6   GLN A CA  
36   C C   . GLN A 13  ? 0.3229 0.2886 0.3659 0.0567  -0.0101 -0.0350 6   GLN A C   
37   O O   . GLN A 13  ? 0.3086 0.2466 0.3079 0.0405  -0.0107 -0.0340 6   GLN A O   
38   C CB  . GLN A 13  ? 0.3003 0.3319 0.4191 0.0555  -0.0467 -0.0150 6   GLN A CB  
39   C CG  . GLN A 13  ? 0.3417 0.3297 0.4044 0.0421  -0.0716 -0.0058 6   GLN A CG  
40   C CD  . GLN A 13  ? 0.3636 0.3647 0.4441 0.0395  -0.1107 0.0107  6   GLN A CD  
41   O OE1 . GLN A 13  ? 0.3728 0.4226 0.5209 0.0466  -0.1219 0.0163  6   GLN A OE1 
42   N NE2 . GLN A 13  ? 0.4610 0.4230 0.4807 0.0278  -0.1318 0.0200  6   GLN A NE2 
43   N N   . THR A 14  ? 0.3120 0.2634 0.3688 0.0805  -0.0066 -0.0414 7   THR A N   
44   C CA  . THR A 14  ? 0.3491 0.2453 0.3665 0.0810  -0.0093 -0.0438 7   THR A CA  
45   C C   . THR A 14  ? 0.3546 0.2384 0.3374 0.0668  0.0095  -0.0552 7   THR A C   
46   O O   . THR A 14  ? 0.3663 0.2217 0.3179 0.0513  0.0045  -0.0495 7   THR A O   
47   C CB  . THR A 14  ? 0.3750 0.2472 0.4137 0.1108  -0.0134 -0.0522 7   THR A CB  
48   O OG1 . THR A 14  ? 0.4487 0.3257 0.5196 0.1230  -0.0399 -0.0351 7   THR A OG1 
49   C CG2 . THR A 14  ? 0.5100 0.3192 0.5086 0.1055  -0.0191 -0.0552 7   THR A CG2 
50   N N   . THR A 15  ? 0.3274 0.2369 0.3171 0.0703  0.0305  -0.0681 8   THR A N   
51   C CA  . THR A 15  ? 0.3550 0.2519 0.3091 0.0554  0.0418  -0.0748 8   THR A CA  
52   C C   . THR A 15  ? 0.3524 0.2531 0.2945 0.0331  0.0351  -0.0629 8   THR A C   
53   O O   . THR A 15  ? 0.3158 0.1951 0.2349 0.0226  0.0324  -0.0622 8   THR A O   
54   C CB  . THR A 15  ? 0.3604 0.2864 0.3158 0.0596  0.0654  -0.0851 8   THR A CB  
55   O OG1 . THR A 15  ? 0.3950 0.3182 0.3592 0.0866  0.0773  -0.1025 8   THR A OG1 
56   C CG2 . THR A 15  ? 0.3917 0.2977 0.3033 0.0435  0.0695  -0.0884 8   THR A CG2 
57   N N   . ILE A 16  ? 0.2843 0.2117 0.2453 0.0269  0.0306  -0.0549 9   ILE A N   
58   C CA  . ILE A 16  ? 0.2689 0.1905 0.2138 0.0109  0.0242  -0.0500 9   ILE A CA  
59   C C   . ILE A 16  ? 0.3081 0.2068 0.2320 0.0094  0.0160  -0.0457 9   ILE A C   
60   O O   . ILE A 16  ? 0.3022 0.1919 0.2097 0.0024  0.0200  -0.0465 9   ILE A O   
61   C CB  . ILE A 16  ? 0.2712 0.2154 0.2349 0.0023  0.0150  -0.0451 9   ILE A CB  
62   C CG1 . ILE A 16  ? 0.2649 0.2367 0.2503 -0.0042 0.0271  -0.0433 9   ILE A CG1 
63   C CG2 . ILE A 16  ? 0.2805 0.2042 0.2179 -0.0086 0.0056  -0.0466 9   ILE A CG2 
64   C CD1 . ILE A 16  ? 0.2845 0.2388 0.2450 -0.0154 0.0343  -0.0435 9   ILE A CD1 
65   N N   . GLU A 17  ? 0.3387 0.2307 0.2660 0.0165  0.0053  -0.0387 10  GLU A N   
66   C CA  . GLU A 17  ? 0.3496 0.2223 0.2508 0.0099  -0.0012 -0.0282 10  GLU A CA  
67   C C   . GLU A 17  ? 0.3291 0.1837 0.2228 0.0050  0.0062  -0.0266 10  GLU A C   
68   O O   . GLU A 17  ? 0.3774 0.2322 0.2558 -0.0062 0.0119  -0.0194 10  GLU A O   
69   C CB  . GLU A 17  ? 0.3970 0.2618 0.3013 0.0164  -0.0207 -0.0153 10  GLU A CB  
70   C CG  . GLU A 17  ? 0.4359 0.3192 0.3409 0.0134  -0.0360 -0.0128 10  GLU A CG  
71   C CD  . GLU A 17  ? 0.5003 0.3810 0.4188 0.0221  -0.0627 0.0025  10  GLU A CD  
72   O OE1 . GLU A 17  ? 0.4889 0.3542 0.4271 0.0366  -0.0667 0.0079  10  GLU A OE1 
73   O OE2 . GLU A 17  ? 0.5129 0.4021 0.4216 0.0150  -0.0838 0.0088  10  GLU A OE2 
74   N N   . GLN A 18  ? 0.3209 0.1618 0.2257 0.0124  0.0063  -0.0339 11  GLN A N   
75   C CA  . GLN A 18  ? 0.3760 0.1952 0.2737 0.0030  0.0058  -0.0332 11  GLN A CA  
76   C C   . GLN A 18  ? 0.3385 0.1750 0.2364 -0.0059 0.0147  -0.0388 11  GLN A C   
77   O O   . GLN A 18  ? 0.3534 0.1899 0.2548 -0.0187 0.0134  -0.0314 11  GLN A O   
78   C CB  . GLN A 18  ? 0.4137 0.2011 0.3121 0.0152  -0.0011 -0.0447 11  GLN A CB  
79   C CG  . GLN A 18  ? 0.3846 0.1449 0.2889 0.0257  -0.0161 -0.0353 11  GLN A CG  
80   C CD  . GLN A 18  ? 0.4847 0.2049 0.3914 0.0438  -0.0236 -0.0510 11  GLN A CD  
81   O OE1 . GLN A 18  ? 0.5227 0.2601 0.4317 0.0508  -0.0103 -0.0705 11  GLN A OE1 
82   N NE2 . GLN A 18  ? 0.5310 0.2164 0.4432 0.0473  -0.0423 -0.0384 11  GLN A NE2 
83   N N   . ALA A 19  ? 0.3313 0.1849 0.2311 -0.0007 0.0215  -0.0479 12  ALA A N   
84   C CA  . ALA A 19  ? 0.3237 0.1882 0.2249 -0.0074 0.0244  -0.0491 12  ALA A CA  
85   C C   . ALA A 19  ? 0.2810 0.1604 0.1885 -0.0102 0.0291  -0.0434 12  ALA A C   
86   O O   . ALA A 19  ? 0.2943 0.1837 0.2149 -0.0140 0.0305  -0.0405 12  ALA A O   
87   C CB  . ALA A 19  ? 0.3138 0.1872 0.2123 -0.0048 0.0285  -0.0545 12  ALA A CB  
88   N N   . TRP A 20  ? 0.2996 0.1826 0.1982 -0.0070 0.0312  -0.0432 13  TRP A N   
89   C CA  . TRP A 20  ? 0.2903 0.1827 0.1801 -0.0073 0.0396  -0.0426 13  TRP A CA  
90   C C   . TRP A 20  ? 0.3152 0.2174 0.2103 -0.0152 0.0474  -0.0304 13  TRP A C   
91   O O   . TRP A 20  ? 0.3068 0.2308 0.2145 -0.0143 0.0606  -0.0307 13  TRP A O   
92   C CB  . TRP A 20  ? 0.3514 0.2381 0.2170 -0.0062 0.0343  -0.0434 13  TRP A CB  
93   C CG  . TRP A 20  ? 0.3421 0.2318 0.1817 -0.0049 0.0442  -0.0490 13  TRP A CG  
94   C CD1 . TRP A 20  ? 0.3928 0.2843 0.2011 -0.0098 0.0506  -0.0403 13  TRP A CD1 
95   C CD2 . TRP A 20  ? 0.3726 0.2595 0.2085 0.0033  0.0500  -0.0663 13  TRP A CD2 
96   N NE1 . TRP A 20  ? 0.4283 0.3228 0.2084 -0.0036 0.0651  -0.0549 13  TRP A NE1 
97   C CE2 . TRP A 20  ? 0.4189 0.3101 0.2227 0.0068  0.0625  -0.0720 13  TRP A CE2 
98   C CE3 . TRP A 20  ? 0.3503 0.2325 0.2106 0.0082  0.0428  -0.0741 13  TRP A CE3 
99   C CZ2 . TRP A 20  ? 0.4896 0.3845 0.2956 0.0195  0.0656  -0.0892 13  TRP A CZ2 
100  C CZ3 . TRP A 20  ? 0.4288 0.3078 0.2899 0.0185  0.0434  -0.0876 13  TRP A CZ3 
101  C CH2 . TRP A 20  ? 0.4557 0.3410 0.2921 0.0258  0.0547  -0.0977 13  TRP A CH2 
102  N N   . GLU A 21  ? 0.3406 0.2280 0.2322 -0.0229 0.0392  -0.0183 14  GLU A N   
103  C CA  . GLU A 21  ? 0.3426 0.2368 0.2411 -0.0379 0.0437  -0.0007 14  GLU A CA  
104  C C   . GLU A 21  ? 0.3102 0.2201 0.2436 -0.0448 0.0431  -0.0005 14  GLU A C   
105  O O   . GLU A 21  ? 0.3243 0.2624 0.2801 -0.0572 0.0530  0.0132  14  GLU A O   
106  C CB  . GLU A 21  ? 0.3349 0.1948 0.2221 -0.0454 0.0274  0.0132  14  GLU A CB  
107  C CG  . GLU A 21  ? 0.4023 0.2511 0.2584 -0.0416 0.0227  0.0217  14  GLU A CG  
108  C CD  . GLU A 21  ? 0.7474 0.5560 0.6018 -0.0379 -0.0006 0.0306  14  GLU A CD  
109  O OE1 . GLU A 21  ? 0.7818 0.5798 0.6157 -0.0345 -0.0121 0.0419  14  GLU A OE1 
110  O OE2 . GLU A 21  ? 0.7171 0.5008 0.5884 -0.0365 -0.0102 0.0253  14  GLU A OE2 
111  N N   . ASN A 22  ? 0.2913 0.1877 0.2299 -0.0386 0.0311  -0.0133 15  ASN A N   
112  C CA  . ASN A 22  ? 0.3122 0.2163 0.2761 -0.0458 0.0208  -0.0129 15  ASN A CA  
113  C C   . ASN A 22  ? 0.2965 0.2268 0.2799 -0.0342 0.0265  -0.0194 15  ASN A C   
114  O O   . ASN A 22  ? 0.3286 0.2622 0.3299 -0.0373 0.0117  -0.0186 15  ASN A O   
115  C CB  . ASN A 22  ? 0.3425 0.2085 0.2849 -0.0461 0.0027  -0.0234 15  ASN A CB  
116  C CG  . ASN A 22  ? 0.3423 0.2051 0.2969 -0.0587 -0.0166 -0.0221 15  ASN A CG  
117  O OD1 . ASN A 22  ? 0.3681 0.2448 0.3525 -0.0760 -0.0248 -0.0084 15  ASN A OD1 
118  N ND2 . ASN A 22  ? 0.4097 0.2558 0.3400 -0.0535 -0.0261 -0.0341 15  ASN A ND2 
119  N N   . ARG A 23  ? 0.2796 0.2222 0.2569 -0.0208 0.0431  -0.0259 16  ARG A N   
120  C CA  . ARG A 23  ? 0.3029 0.2498 0.2911 -0.0062 0.0427  -0.0358 16  ARG A CA  
121  C C   . ARG A 23  ? 0.3102 0.2906 0.3482 -0.0020 0.0421  -0.0301 16  ARG A C   
122  O O   . ARG A 23  ? 0.3302 0.3058 0.3837 0.0077  0.0292  -0.0328 16  ARG A O   
123  C CB  . ARG A 23  ? 0.2883 0.2300 0.2544 0.0068  0.0564  -0.0482 16  ARG A CB  
124  C CG  . ARG A 23  ? 0.3165 0.2851 0.2837 0.0120  0.0802  -0.0494 16  ARG A CG  
125  C CD  . ARG A 23  ? 0.4168 0.3648 0.3394 0.0214  0.0872  -0.0656 16  ARG A CD  
126  N NE  . ARG A 23  ? 0.3777 0.3461 0.2795 0.0263  0.1130  -0.0697 16  ARG A NE  
127  C CZ  . ARG A 23  ? 0.3829 0.3583 0.2552 0.0117  0.1212  -0.0554 16  ARG A CZ  
128  N NH1 . ARG A 23  ? 0.3889 0.3507 0.2591 -0.0057 0.1039  -0.0366 16  ARG A NH1 
129  N NH2 . ARG A 23  ? 0.4467 0.4404 0.2878 0.0158  0.1479  -0.0596 16  ARG A NH2 
130  N N   . ALA A 24  ? 0.2969 0.3145 0.3655 -0.0100 0.0545  -0.0190 17  ALA A N   
131  C CA  . ALA A 24  ? 0.3210 0.3851 0.4543 -0.0052 0.0543  -0.0114 17  ALA A CA  
132  C C   . ALA A 24  ? 0.3804 0.4344 0.5335 -0.0168 0.0187  -0.0025 17  ALA A C   
133  O O   . ALA A 24  ? 0.3668 0.4521 0.5745 -0.0088 0.0072  0.0035  17  ALA A O   
134  C CB  . ALA A 24  ? 0.3194 0.4349 0.4876 -0.0187 0.0762  0.0044  17  ALA A CB  
135  N N   . ASN A 25  ? 0.3750 0.3855 0.4835 -0.0337 -0.0001 -0.0026 18  ASN A N   
136  C CA  . ASN A 25  ? 0.3025 0.2933 0.4077 -0.0475 -0.0345 0.0023  18  ASN A CA  
137  C C   . ASN A 25  ? 0.3504 0.3012 0.4081 -0.0389 -0.0464 -0.0070 18  ASN A C   
138  O O   . ASN A 25  ? 0.4758 0.4012 0.5070 -0.0509 -0.0727 -0.0055 18  ASN A O   
139  C CB  . ASN A 25  ? 0.4330 0.3964 0.5137 -0.0717 -0.0465 0.0049  18  ASN A CB  
140  C CG  . ASN A 25  ? 0.4505 0.4505 0.5777 -0.0890 -0.0380 0.0218  18  ASN A CG  
141  O OD1 . ASN A 25  ? 0.3904 0.4412 0.5822 -0.0955 -0.0432 0.0360  18  ASN A OD1 
142  N ND2 . ASN A 25  ? 0.4515 0.4301 0.5508 -0.0969 -0.0248 0.0236  18  ASN A ND2 
143  N N   . LEU A 26  ? 0.3607 0.3031 0.4012 -0.0220 -0.0284 -0.0158 19  LEU A N   
144  C CA  . LEU A 26  ? 0.3372 0.2470 0.3382 -0.0188 -0.0366 -0.0189 19  LEU A CA  
145  C C   . LEU A 26  ? 0.4112 0.3252 0.4416 -0.0043 -0.0473 -0.0133 19  LEU A C   
146  O O   . LEU A 26  ? 0.3874 0.3228 0.4561 0.0133  -0.0336 -0.0183 19  LEU A O   
147  C CB  . LEU A 26  ? 0.3488 0.2431 0.3161 -0.0147 -0.0156 -0.0295 19  LEU A CB  
148  C CG  . LEU A 26  ? 0.3874 0.2708 0.3272 -0.0234 -0.0091 -0.0349 19  LEU A CG  
149  C CD1 . LEU A 26  ? 0.4145 0.2943 0.3385 -0.0170 0.0081  -0.0422 19  LEU A CD1 
150  C CD2 . LEU A 26  ? 0.4684 0.3281 0.3718 -0.0327 -0.0230 -0.0366 19  LEU A CD2 
151  N N   . SER A 27  ? 0.3988 0.2882 0.4063 -0.0105 -0.0718 -0.0032 20  SER A N   
152  C CA  . SER A 27  ? 0.3840 0.2627 0.4135 0.0022  -0.0905 0.0068  20  SER A CA  
153  C C   . SER A 27  ? 0.4664 0.3045 0.4370 -0.0123 -0.1043 0.0179  20  SER A C   
154  O O   . SER A 27  ? 0.4600 0.2884 0.3785 -0.0293 -0.0973 0.0154  20  SER A O   
155  C CB  . SER A 27  ? 0.4202 0.3248 0.5043 0.0069  -0.1186 0.0203  20  SER A CB  
156  O OG  . SER A 27  ? 0.5007 0.3894 0.5470 -0.0159 -0.1484 0.0326  20  SER A OG  
157  N N   . PRO A 28  ? 0.4407 0.2534 0.4173 -0.0058 -0.1241 0.0316  21  PRO A N   
158  C CA  . PRO A 28  ? 0.5585 0.3339 0.4761 -0.0255 -0.1386 0.0505  21  PRO A CA  
159  C C   . PRO A 28  ? 0.6186 0.3882 0.4932 -0.0441 -0.1635 0.0650  21  PRO A C   
160  O O   . PRO A 28  ? 0.7730 0.5165 0.5831 -0.0636 -0.1680 0.0798  21  PRO A O   
161  C CB  . PRO A 28  ? 0.5402 0.2835 0.4841 -0.0130 -0.1620 0.0652  21  PRO A CB  
162  C CG  . PRO A 28  ? 0.5204 0.2806 0.5252 0.0166  -0.1451 0.0421  21  PRO A CG  
163  C CD  . PRO A 28  ? 0.3851 0.1979 0.4200 0.0214  -0.1302 0.0291  21  PRO A CD  
164  N N   . VAL A 29  ? 0.4969 0.2893 0.4024 -0.0413 -0.1820 0.0632  22  VAL A N   
165  C CA  . VAL A 29  ? 0.5966 0.3766 0.4520 -0.0618 -0.2112 0.0728  22  VAL A CA  
166  C C   . VAL A 29  ? 0.5988 0.3833 0.4144 -0.0736 -0.1904 0.0500  22  VAL A C   
167  O O   . VAL A 29  ? 0.7233 0.4816 0.4599 -0.0907 -0.1956 0.0480  22  VAL A O   
168  C CB  . VAL A 29  ? 0.5928 0.3914 0.5082 -0.0565 -0.2556 0.0880  22  VAL A CB  
169  C CG1 . VAL A 29  ? 0.7916 0.5638 0.6433 -0.0807 -0.2922 0.1018  22  VAL A CG1 
170  C CG2 . VAL A 29  ? 0.7211 0.5215 0.7026 -0.0319 -0.2697 0.1030  22  VAL A CG2 
171  N N   . ASP A 30  ? 0.5500 0.3626 0.4135 -0.0640 -0.1670 0.0323  23  ASP A N   
172  C CA  . ASP A 30  ? 0.6716 0.4803 0.5090 -0.0750 -0.1607 0.0144  23  ASP A CA  
173  C C   . ASP A 30  ? 0.8080 0.6065 0.6059 -0.0712 -0.1213 -0.0053 23  ASP A C   
174  O O   . ASP A 30  ? 0.8925 0.6771 0.6642 -0.0764 -0.1171 -0.0221 23  ASP A O   
175  C CB  . ASP A 30  ? 0.6984 0.5428 0.6120 -0.0728 -0.1645 0.0133  23  ASP A CB  
176  C CG  . ASP A 30  ? 0.7989 0.6712 0.7580 -0.0556 -0.1264 0.0058  23  ASP A CG  
177  O OD1 . ASP A 30  ? 0.6407 0.5000 0.5697 -0.0475 -0.0995 -0.0030 23  ASP A OD1 
178  O OD2 . ASP A 30  ? 0.6729 0.5836 0.6982 -0.0524 -0.1244 0.0102  23  ASP A OD2 
179  N N   . ALA A 31  ? 0.5736 0.3765 0.3705 -0.0625 -0.0964 -0.0034 24  ALA A N   
180  C CA  . ALA A 31  ? 0.5342 0.3418 0.3195 -0.0562 -0.0618 -0.0193 24  ALA A CA  
181  C C   . ALA A 31  ? 0.5006 0.2902 0.2168 -0.0624 -0.0495 -0.0298 24  ALA A C   
182  O O   . ALA A 31  ? 0.5426 0.3192 0.2097 -0.0732 -0.0559 -0.0191 24  ALA A O   
183  C CB  . ALA A 31  ? 0.5355 0.3554 0.3465 -0.0490 -0.0450 -0.0128 24  ALA A CB  
184  N N   . SER A 32  ? 0.4469 0.2357 0.1584 -0.0537 -0.0300 -0.0503 25  SER A N   
185  C CA  . SER A 32  ? 0.4717 0.2622 0.1507 -0.0475 -0.0122 -0.0618 25  SER A CA  
186  C C   . SER A 32  ? 0.4744 0.2874 0.1413 -0.0465 0.0164  -0.0566 25  SER A C   
187  O O   . SER A 32  ? 0.4372 0.2640 0.1294 -0.0479 0.0265  -0.0483 25  SER A O   
188  C CB  . SER A 32  ? 0.4581 0.2518 0.1641 -0.0320 -0.0031 -0.0798 25  SER A CB  
189  O OG  . SER A 32  ? 0.4105 0.2269 0.1575 -0.0220 0.0143  -0.0785 25  SER A OG  
190  N N   . ALA A 33  ? 0.3911 0.1837 0.1338 -0.0229 0.0384  -0.0102 26  ALA A N   
191  C CA  . ALA A 33  ? 0.4152 0.2202 0.1656 -0.0276 0.0476  -0.0167 26  ALA A CA  
192  C C   . ALA A 33  ? 0.3975 0.2107 0.1766 -0.0119 0.0473  -0.0278 26  ALA A C   
193  O O   . ALA A 33  ? 0.3722 0.1984 0.1654 -0.0110 0.0512  -0.0308 26  ALA A O   
194  C CB  . ALA A 33  ? 0.4443 0.2652 0.1799 -0.0462 0.0613  -0.0312 26  ALA A CB  
195  N N   . GLU A 34  ? 0.3879 0.1849 0.1725 -0.0027 0.0343  -0.0316 27  GLU A N   
196  C CA  . GLU A 34  ? 0.3949 0.1813 0.2036 0.0090  0.0166  -0.0390 27  GLU A CA  
197  C C   . GLU A 34  ? 0.4134 0.2039 0.2183 0.0040  0.0151  -0.0221 27  GLU A C   
198  O O   . GLU A 34  ? 0.3747 0.1716 0.2024 0.0123  0.0128  -0.0288 27  GLU A O   
199  C CB  . GLU A 34  ? 0.4308 0.1756 0.2320 0.0095  -0.0164 -0.0361 27  GLU A CB  
200  C CG  . GLU A 34  ? 0.5313 0.2433 0.3548 0.0188  -0.0552 -0.0413 27  GLU A CG  
201  C CD  . GLU A 34  ? 0.6031 0.3285 0.4889 0.0479  -0.0669 -0.0895 27  GLU A CD  
202  O OE1 . GLU A 34  ? 0.5224 0.2915 0.4269 0.0525  -0.0397 -0.1205 27  GLU A OE1 
203  O OE2 . GLU A 34  ? 0.7420 0.4405 0.6610 0.0626  -0.1065 -0.1023 27  GLU A OE2 
204  N N   . VAL A 35  ? 0.3747 0.1726 0.1577 -0.0106 0.0167  -0.0087 28  VAL A N   
205  C CA  . VAL A 35  ? 0.3639 0.1843 0.1502 -0.0200 0.0162  -0.0058 28  VAL A CA  
206  C C   . VAL A 35  ? 0.3553 0.1965 0.1675 -0.0070 0.0279  -0.0132 28  VAL A C   
207  O O   . VAL A 35  ? 0.3541 0.2072 0.1824 -0.0040 0.0280  -0.0148 28  VAL A O   
208  C CB  . VAL A 35  ? 0.3700 0.2173 0.1350 -0.0459 0.0152  -0.0080 28  VAL A CB  
209  C CG1 . VAL A 35  ? 0.3727 0.2719 0.1548 -0.0574 0.0209  -0.0236 28  VAL A CG1 
210  C CG2 . VAL A 35  ? 0.4400 0.2558 0.1623 -0.0750 -0.0063 0.0089  28  VAL A CG2 
211  N N   . ARG A 36  ? 0.3512 0.1882 0.1622 -0.0037 0.0303  -0.0146 29  ARG A N   
212  C CA  . ARG A 36  ? 0.3461 0.1815 0.1698 -0.0007 0.0248  -0.0144 29  ARG A CA  
213  C C   . ARG A 36  ? 0.3638 0.1992 0.1892 -0.0023 0.0352  -0.0122 29  ARG A C   
214  O O   . ARG A 36  ? 0.3700 0.2098 0.2088 -0.0009 0.0309  -0.0114 29  ARG A O   
215  C CB  . ARG A 36  ? 0.4233 0.2348 0.2291 -0.0092 0.0119  -0.0079 29  ARG A CB  
216  C CG  . ARG A 36  ? 0.4327 0.2479 0.2528 -0.0025 -0.0070 -0.0199 29  ARG A CG  
217  C CD  . ARG A 36  ? 0.6065 0.3798 0.4051 -0.0133 -0.0334 -0.0079 29  ARG A CD  
218  N NE  . ARG A 36  ? 0.7298 0.5076 0.5530 -0.0015 -0.0576 -0.0276 29  ARG A NE  
219  C CZ  . ARG A 36  ? 0.8608 0.6436 0.7349 0.0162  -0.0967 -0.0551 29  ARG A CZ  
220  N NH1 . ARG A 36  ? 0.6855 0.4575 0.5848 0.0233  -0.1196 -0.0588 29  ARG A NH1 
221  N NH2 . ARG A 36  ? 0.8800 0.6841 0.7891 0.0289  -0.1169 -0.0876 29  ARG A NH2 
222  N N   . ASP A 37  ? 0.3664 0.2047 0.1858 -0.0051 0.0470  -0.0199 30  ASP A N   
223  C CA  . ASP A 37  ? 0.3767 0.2369 0.2110 -0.0076 0.0583  -0.0355 30  ASP A CA  
224  C C   . ASP A 37  ? 0.3714 0.2339 0.2347 0.0105  0.0517  -0.0398 30  ASP A C   
225  O O   . ASP A 37  ? 0.3415 0.2219 0.2201 0.0099  0.0578  -0.0471 30  ASP A O   
226  C CB  . ASP A 37  ? 0.3765 0.2586 0.2182 -0.0111 0.0687  -0.0637 30  ASP A CB  
227  C CG  . ASP A 37  ? 0.5079 0.4004 0.3120 -0.0441 0.0798  -0.0617 30  ASP A CG  
228  O OD1 . ASP A 37  ? 0.5692 0.4376 0.3382 -0.0654 0.0702  -0.0333 30  ASP A OD1 
229  O OD2 . ASP A 37  ? 0.5152 0.4376 0.3263 -0.0508 0.0910  -0.0912 30  ASP A OD2 
230  N N   . ALA A 38  ? 0.3334 0.1759 0.1973 0.0188  0.0356  -0.0338 31  ALA A N   
231  C CA  . ALA A 38  ? 0.3354 0.1695 0.2129 0.0243  0.0196  -0.0311 31  ALA A CA  
232  C C   . ALA A 38  ? 0.3209 0.1739 0.1987 0.0187  0.0275  -0.0213 31  ALA A C   
233  O O   . ALA A 38  ? 0.3427 0.2033 0.2387 0.0242  0.0266  -0.0244 31  ALA A O   
234  C CB  . ALA A 38  ? 0.3851 0.1845 0.2399 0.0136  -0.0088 -0.0176 31  ALA A CB  
235  N N   . VAL A 39  ? 0.3271 0.1923 0.1946 0.0108  0.0314  -0.0174 32  VAL A N   
236  C CA  . VAL A 39  ? 0.3058 0.1965 0.1916 0.0111  0.0317  -0.0233 32  VAL A CA  
237  C C   . VAL A 39  ? 0.3058 0.1897 0.2041 0.0184  0.0334  -0.0222 32  VAL A C   
238  O O   . VAL A 39  ? 0.3176 0.2127 0.2334 0.0223  0.0333  -0.0246 32  VAL A O   
239  C CB  . VAL A 39  ? 0.2832 0.1972 0.1756 0.0068  0.0262  -0.0376 32  VAL A CB  
240  C CG1 . VAL A 39  ? 0.2693 0.2131 0.2016 0.0155  0.0165  -0.0595 32  VAL A CG1 
241  C CG2 . VAL A 39  ? 0.2935 0.2304 0.1642 -0.0169 0.0279  -0.0409 32  VAL A CG2 
242  N N   . GLU A 40  ? 0.3254 0.1910 0.2060 0.0113  0.0334  -0.0167 33  GLU A N   
243  C CA  . GLU A 40  ? 0.3390 0.1953 0.2108 -0.0021 0.0296  -0.0103 33  GLU A CA  
244  C C   . GLU A 40  ? 0.3497 0.2294 0.2324 -0.0028 0.0476  -0.0193 33  GLU A C   
245  O O   . GLU A 40  ? 0.3440 0.2264 0.2307 -0.0095 0.0446  -0.0162 33  GLU A O   
246  C CB  . GLU A 40  ? 0.4330 0.2700 0.2658 -0.0289 0.0256  -0.0006 33  GLU A CB  
247  C CG  . GLU A 40  ? 0.5504 0.3771 0.3520 -0.0655 0.0172  0.0114  33  GLU A CG  
248  C CD  . GLU A 40  ? 0.8131 0.6170 0.5575 -0.1115 0.0052  0.0272  33  GLU A CD  
249  O OE1 . GLU A 40  ? 0.8406 0.6449 0.5773 -0.1082 0.0117  0.0235  33  GLU A OE1 
250  O OE2 . GLU A 40  ? 0.8182 0.6008 0.5174 -0.1588 -0.0142 0.0459  33  GLU A OE2 
251  N N   . HIS A 41  ? 0.3407 0.2358 0.2347 0.0057  0.0592  -0.0355 34  HIS A N   
252  C CA  . HIS A 41  ? 0.3162 0.2387 0.2386 0.0119  0.0676  -0.0580 34  HIS A CA  
253  C C   . HIS A 41  ? 0.2881 0.2049 0.2306 0.0271  0.0582  -0.0504 34  HIS A C   
254  O O   . HIS A 41  ? 0.2995 0.2367 0.2611 0.0280  0.0639  -0.0618 34  HIS A O   
255  C CB  . HIS A 41  ? 0.3526 0.2830 0.3003 0.0269  0.0630  -0.0864 34  HIS A CB  
256  C CG  . HIS A 41  ? 0.4670 0.4354 0.4631 0.0383  0.0636  -0.1285 34  HIS A CG  
257  N ND1 . HIS A 41  ? 0.5973 0.6301 0.6048 0.0167  0.0885  -0.1670 34  HIS A ND1 
258  C CD2 . HIS A 41  ? 0.5897 0.5455 0.6282 0.0646  0.0374  -0.1441 34  HIS A CD2 
259  C CE1 . HIS A 41  ? 0.5782 0.6454 0.6427 0.0335  0.0767  -0.2009 34  HIS A CE1 
260  N NE2 . HIS A 41  ? 0.4759 0.4906 0.5603 0.0657  0.0437  -0.1879 34  HIS A NE2 
261  N N   . THR A 42  ? 0.2863 0.1849 0.2225 0.0323  0.0454  -0.0354 35  THR A N   
262  C CA  . THR A 42  ? 0.2828 0.1861 0.2302 0.0349  0.0379  -0.0301 35  THR A CA  
263  C C   . THR A 42  ? 0.3108 0.2290 0.2672 0.0333  0.0432  -0.0287 35  THR A C   
264  O O   . THR A 42  ? 0.2764 0.2051 0.2491 0.0370  0.0446  -0.0311 35  THR A O   
265  C CB  . THR A 42  ? 0.3038 0.2026 0.2317 0.0220  0.0258  -0.0207 35  THR A CB  
266  O OG1 . THR A 42  ? 0.3480 0.2152 0.2606 0.0191  0.0079  -0.0162 35  THR A OG1 
267  C CG2 . THR A 42  ? 0.2980 0.2108 0.2275 0.0105  0.0185  -0.0174 35  THR A CG2 
268  N N   . ILE A 43  ? 0.2803 0.1925 0.2298 0.0292  0.0376  -0.0265 36  ILE A N   
269  C CA  . ILE A 43  ? 0.2591 0.1684 0.2229 0.0297  0.0237  -0.0275 36  ILE A CA  
270  C C   . ILE A 43  ? 0.2888 0.1876 0.2378 0.0154  0.0280  -0.0184 36  ILE A C   
271  O O   . ILE A 43  ? 0.2911 0.1911 0.2527 0.0151  0.0209  -0.0176 36  ILE A O   
272  C CB  . ILE A 43  ? 0.3143 0.2049 0.2806 0.0302  -0.0018 -0.0311 36  ILE A CB  
273  C CG1 . ILE A 43  ? 0.3206 0.2448 0.3059 0.0377  -0.0003 -0.0524 36  ILE A CG1 
274  C CG2 . ILE A 43  ? 0.3414 0.2120 0.3313 0.0340  -0.0369 -0.0358 36  ILE A CG2 
275  C CD1 . ILE A 43  ? 0.3207 0.2966 0.3352 0.0388  0.0066  -0.0752 36  ILE A CD1 
276  N N   . ASP A 44  ? 0.2977 0.1963 0.2192 -0.0030 0.0406  -0.0168 37  ASP A N   
277  C CA  . ASP A 44  ? 0.3220 0.2366 0.2253 -0.0316 0.0518  -0.0193 37  ASP A CA  
278  C C   . ASP A 44  ? 0.3188 0.2664 0.2573 -0.0152 0.0665  -0.0366 37  ASP A C   
279  O O   . ASP A 44  ? 0.3038 0.2618 0.2383 -0.0320 0.0681  -0.0357 37  ASP A O   
280  C CB  . ASP A 44  ? 0.3557 0.2974 0.2361 -0.0573 0.0714  -0.0346 37  ASP A CB  
281  C CG  . ASP A 44  ? 0.5218 0.4295 0.3526 -0.0887 0.0551  -0.0132 37  ASP A CG  
282  O OD1 . ASP A 44  ? 0.6096 0.4655 0.4216 -0.0964 0.0199  0.0135  37  ASP A OD1 
283  O OD2 . ASP A 44  ? 0.6143 0.5467 0.4290 -0.1063 0.0718  -0.0277 37  ASP A OD2 
284  N N   . GLY A 45  ? 0.2987 0.2560 0.2675 0.0129  0.0702  -0.0506 38  GLY A N   
285  C CA  . GLY A 45  ? 0.3145 0.2910 0.3181 0.0294  0.0717  -0.0664 38  GLY A CA  
286  C C   . GLY A 45  ? 0.2821 0.2502 0.2918 0.0347  0.0642  -0.0504 38  GLY A C   
287  O O   . GLY A 45  ? 0.2908 0.2767 0.3167 0.0347  0.0691  -0.0581 38  GLY A O   
288  N N   . LEU A 46  ? 0.2350 0.1870 0.2380 0.0380  0.0529  -0.0366 39  LEU A N   
289  C CA  . LEU A 46  ? 0.2374 0.1967 0.2567 0.0418  0.0451  -0.0352 39  LEU A CA  
290  C C   . LEU A 46  ? 0.2801 0.2283 0.2956 0.0312  0.0377  -0.0299 39  LEU A C   
291  O O   . LEU A 46  ? 0.2699 0.2272 0.3017 0.0337  0.0363  -0.0319 39  LEU A O   
292  C CB  . LEU A 46  ? 0.2365 0.2036 0.2624 0.0439  0.0342  -0.0415 39  LEU A CB  
293  C CG  . LEU A 46  ? 0.2396 0.2248 0.2568 0.0361  0.0376  -0.0439 39  LEU A CG  
294  C CD1 . LEU A 46  ? 0.2300 0.2448 0.2557 0.0297  0.0326  -0.0628 39  LEU A CD1 
295  C CD2 . LEU A 46  ? 0.2652 0.2693 0.2892 0.0294  0.0377  -0.0443 39  LEU A CD2 
296  N N   . ASP A 47  ? 0.2651 0.1868 0.2518 0.0127  0.0265  -0.0197 40  ASP A N   
297  C CA  . ASP A 47  ? 0.3084 0.1995 0.2733 -0.0124 0.0024  -0.0052 40  ASP A CA  
298  C C   . ASP A 47  ? 0.3167 0.2336 0.2673 -0.0361 0.0236  -0.0066 40  ASP A C   
299  O O   . ASP A 47  ? 0.3435 0.2433 0.2842 -0.0538 0.0058  0.0040  40  ASP A O   
300  C CB  . ASP A 47  ? 0.3624 0.2131 0.2826 -0.0415 -0.0197 0.0117  40  ASP A CB  
301  C CG  . ASP A 47  ? 0.5100 0.3003 0.3986 -0.0737 -0.0705 0.0351  40  ASP A CG  
302  O OD1 . ASP A 47  ? 0.4632 0.2170 0.3881 -0.0486 -0.1168 0.0299  40  ASP A OD1 
303  O OD2 . ASP A 47  ? 0.5968 0.3783 0.4246 -0.1297 -0.0702 0.0539  40  ASP A OD2 
304  N N   . LEU A 48  ? 0.3009 0.2619 0.2546 -0.0384 0.0567  -0.0260 41  LEU A N   
305  C CA  . LEU A 48  ? 0.3063 0.3166 0.2621 -0.0595 0.0805  -0.0473 41  LEU A CA  
306  C C   . LEU A 48  ? 0.2629 0.2970 0.2697 -0.0242 0.0882  -0.0642 41  LEU A C   
307  O O   . LEU A 48  ? 0.3123 0.3924 0.3337 -0.0358 0.1046  -0.0891 41  LEU A O   
308  C CB  . LEU A 48  ? 0.3144 0.3744 0.2710 -0.0731 0.1050  -0.0801 41  LEU A CB  
309  C CG  . LEU A 48  ? 0.4386 0.4867 0.3360 -0.1206 0.1019  -0.0661 41  LEU A CG  
310  C CD1 . LEU A 48  ? 0.5667 0.6709 0.4847 -0.1186 0.1263  -0.1088 41  LEU A CD1 
311  C CD2 . LEU A 48  ? 0.5899 0.6469 0.4271 -0.1913 0.0989  -0.0534 41  LEU A CD2 
312  N N   . GLY A 49  ? 0.2341 0.3383 0.3081 -0.0115 0.0884  -0.0329 42  GLY A N   
313  C CA  . GLY A 49  ? 0.2322 0.3260 0.3312 0.0027  0.0747  -0.0480 42  GLY A CA  
314  C C   . GLY A 49  ? 0.2710 0.3822 0.3843 0.0237  0.0714  -0.0754 42  GLY A C   
315  O O   . GLY A 49  ? 0.2785 0.3885 0.4173 0.0353  0.0580  -0.0875 42  GLY A O   
316  N N   . ARG A 50  ? 0.2336 0.3615 0.3344 0.0298  0.0805  -0.0875 43  ARG A N   
317  C CA  A ARG A 50  ? 0.2426 0.3798 0.3640 0.0531  0.0721  -0.1175 43  ARG A CA  
318  C CA  B ARG A 50  ? 0.2425 0.3796 0.3622 0.0530  0.0726  -0.1175 43  ARG A CA  
319  C C   . ARG A 50  ? 0.2734 0.3517 0.3784 0.0684  0.0495  -0.1144 43  ARG A C   
320  O O   . ARG A 50  ? 0.2891 0.3578 0.4164 0.0872  0.0318  -0.1306 43  ARG A O   
321  C CB  A ARG A 50  ? 0.2585 0.4376 0.3773 0.0556  0.0879  -0.1386 43  ARG A CB  
322  C CB  B ARG A 50  ? 0.2503 0.4220 0.3609 0.0548  0.0877  -0.1354 43  ARG A CB  
323  C CG  A ARG A 50  ? 0.3590 0.5176 0.4350 0.0500  0.0924  -0.1278 43  ARG A CG  
324  C CG  B ARG A 50  ? 0.2683 0.5119 0.3909 0.0381  0.1130  -0.1420 43  ARG A CG  
325  C CD  A ARG A 50  ? 0.4423 0.6260 0.5173 0.0603  0.0951  -0.1547 43  ARG A CD  
326  C CD  B ARG A 50  ? 0.3288 0.5986 0.4418 0.0435  0.1165  -0.1621 43  ARG A CD  
327  N NE  A ARG A 50  ? 0.4153 0.5490 0.4728 0.0719  0.0787  -0.1567 43  ARG A NE  
328  N NE  B ARG A 50  ? 0.4581 0.7182 0.5261 0.0339  0.1232  -0.1486 43  ARG A NE  
329  C CZ  A ARG A 50  ? 0.4498 0.5739 0.4743 0.0654  0.0825  -0.1500 43  ARG A CZ  
330  C CZ  B ARG A 50  ? 0.4202 0.6402 0.4694 0.0466  0.1104  -0.1536 43  ARG A CZ  
331  N NH1 A ARG A 50  ? 0.4247 0.5856 0.4254 0.0491  0.0995  -0.1412 43  ARG A NH1 
332  N NH1 B ARG A 50  ? 0.3859 0.5665 0.4540 0.0672  0.0898  -0.1675 43  ARG A NH1 
333  N NH2 A ARG A 50  ? 0.4552 0.5313 0.4700 0.0733  0.0668  -0.1495 43  ARG A NH2 
334  N NH2 B ARG A 50  ? 0.4040 0.6218 0.4147 0.0362  0.1160  -0.1413 43  ARG A NH2 
335  N N   . LEU A 51  ? 0.2345 0.2756 0.3038 0.0596  0.0486  -0.0933 44  LEU A N   
336  C CA  . LEU A 51  ? 0.2462 0.2369 0.2958 0.0653  0.0313  -0.0837 44  LEU A CA  
337  C C   . LEU A 51  ? 0.3090 0.2830 0.3476 0.0537  0.0287  -0.0645 44  LEU A C   
338  O O   . LEU A 51  ? 0.2577 0.2468 0.2980 0.0403  0.0398  -0.0551 44  LEU A O   
339  C CB  . LEU A 51  ? 0.2726 0.2423 0.2943 0.0634  0.0340  -0.0805 44  LEU A CB  
340  C CG  . LEU A 51  ? 0.2844 0.2657 0.3151 0.0754  0.0340  -0.1038 44  LEU A CG  
341  C CD1 . LEU A 51  ? 0.3193 0.2814 0.3226 0.0700  0.0362  -0.0991 44  LEU A CD1 
342  C CD2 . LEU A 51  ? 0.3978 0.3572 0.4515 0.0935  0.0123  -0.1176 44  LEU A CD2 
343  N N   . ARG A 52  ? 0.2815 0.2244 0.3085 0.0579  0.0126  -0.0588 45  ARG A N   
344  C CA  . ARG A 52  ? 0.2609 0.1920 0.2751 0.0483  0.0101  -0.0471 45  ARG A CA  
345  C C   . ARG A 52  ? 0.2644 0.1642 0.2491 0.0480  -0.0002 -0.0390 45  ARG A C   
346  O O   . ARG A 52  ? 0.3100 0.1923 0.2900 0.0557  -0.0129 -0.0388 45  ARG A O   
347  C CB  . ARG A 52  ? 0.3237 0.2712 0.3624 0.0492  0.0025  -0.0523 45  ARG A CB  
348  C CG  . ARG A 52  ? 0.3768 0.3231 0.4282 0.0629  -0.0161 -0.0604 45  ARG A CG  
349  C CD  . ARG A 52  ? 0.3114 0.2853 0.3962 0.0621  -0.0204 -0.0692 45  ARG A CD  
350  N NE  . ARG A 52  ? 0.2627 0.2299 0.3372 0.0523  -0.0238 -0.0643 45  ARG A NE  
351  C CZ  . ARG A 52  ? 0.2505 0.2360 0.3516 0.0490  -0.0300 -0.0722 45  ARG A CZ  
352  N NH1 . ARG A 52  ? 0.2703 0.2855 0.4112 0.0527  -0.0316 -0.0833 45  ARG A NH1 
353  N NH2 . ARG A 52  ? 0.2616 0.2396 0.3534 0.0419  -0.0349 -0.0728 45  ARG A NH2 
354  N N   . VAL A 53  ? 0.2704 0.1648 0.2379 0.0380  0.0049  -0.0325 46  VAL A N   
355  C CA  . VAL A 53  ? 0.2934 0.1688 0.2320 0.0324  0.0010  -0.0251 46  VAL A CA  
356  C C   . VAL A 53  ? 0.3433 0.2097 0.2688 0.0338  -0.0158 -0.0202 46  VAL A C   
357  O O   . VAL A 53  ? 0.3299 0.1765 0.2321 0.0294  -0.0240 -0.0090 46  VAL A O   
358  C CB  . VAL A 53  ? 0.2899 0.1724 0.2210 0.0231  0.0105  -0.0262 46  VAL A CB  
359  C CG1 . VAL A 53  ? 0.3319 0.2078 0.2349 0.0141  0.0096  -0.0213 46  VAL A CG1 
360  C CG2 . VAL A 53  ? 0.3406 0.2270 0.2811 0.0218  0.0217  -0.0265 46  VAL A CG2 
361  N N   . ALA A 54  ? 0.3041 0.1852 0.2425 0.0372  -0.0225 -0.0267 47  ALA A N   
362  C CA  . ALA A 54  ? 0.3351 0.2114 0.2600 0.0395  -0.0421 -0.0225 47  ALA A CA  
363  C C   . ALA A 54  ? 0.3511 0.2418 0.3106 0.0514  -0.0525 -0.0331 47  ALA A C   
364  O O   . ALA A 54  ? 0.3443 0.2554 0.3337 0.0514  -0.0413 -0.0438 47  ALA A O   
365  C CB  . ALA A 54  ? 0.3430 0.2316 0.2435 0.0293  -0.0417 -0.0246 47  ALA A CB  
366  N N   . GLU A 55  ? 0.3638 0.2446 0.3210 0.0601  -0.0757 -0.0287 48  GLU A N   
367  C CA  . GLU A 55  ? 0.3370 0.2363 0.3314 0.0725  -0.0891 -0.0416 48  GLU A CA  
368  C C   . GLU A 55  ? 0.3663 0.2562 0.3416 0.0768  -0.1188 -0.0337 48  GLU A C   
369  O O   . GLU A 55  ? 0.3987 0.2629 0.3325 0.0707  -0.1303 -0.0141 48  GLU A O   
370  C CB  . GLU A 55  ? 0.4574 0.3605 0.4890 0.0866  -0.0892 -0.0515 48  GLU A CB  
371  C CG  . GLU A 55  ? 0.4975 0.3660 0.5164 0.0945  -0.1052 -0.0415 48  GLU A CG  
372  C CD  . GLU A 55  ? 0.6399 0.5185 0.7019 0.1110  -0.1045 -0.0608 48  GLU A CD  
373  O OE1 . GLU A 55  ? 0.6034 0.5052 0.7065 0.1257  -0.1165 -0.0780 48  GLU A OE1 
374  O OE2 . GLU A 55  ? 0.5518 0.4210 0.6091 0.1093  -0.0916 -0.0625 48  GLU A OE2 
375  N N   . LYS A 56  ? 0.3989 0.3116 0.4042 0.0851  -0.1322 -0.0475 49  LYS A N   
376  C CA  . LYS A 56  ? 0.4023 0.3116 0.3907 0.0899  -0.1637 -0.0417 49  LYS A CA  
377  C C   . LYS A 56  ? 0.5018 0.3963 0.5171 0.1097  -0.1913 -0.0401 49  LYS A C   
378  O O   . LYS A 56  ? 0.5293 0.4463 0.5999 0.1230  -0.1891 -0.0607 49  LYS A O   
379  C CB  . LYS A 56  ? 0.3905 0.3344 0.4004 0.0884  -0.1664 -0.0613 49  LYS A CB  
380  C CG  . LYS A 56  ? 0.4907 0.4365 0.4643 0.0869  -0.1940 -0.0560 49  LYS A CG  
381  C CD  . LYS A 56  ? 0.4466 0.4278 0.4442 0.0839  -0.1946 -0.0811 49  LYS A CD  
382  C CE  . LYS A 56  ? 0.5297 0.5189 0.4839 0.0812  -0.2207 -0.0794 49  LYS A CE  
383  N NZ  . LYS A 56  ? 0.4726 0.4962 0.4532 0.0791  -0.2245 -0.1088 49  LYS A NZ  
384  N N   . ILE A 57  ? 0.5052 0.3633 0.4836 0.1104  -0.2174 -0.0157 50  ILE A N   
385  C CA  . ILE A 57  ? 0.6259 0.4587 0.6294 0.1306  -0.2522 -0.0112 50  ILE A CA  
386  C C   . ILE A 57  ? 0.6445 0.4612 0.6100 0.1263  -0.2856 0.0109  50  ILE A C   
387  O O   . ILE A 57  ? 0.7268 0.5276 0.6297 0.1067  -0.2862 0.0375  50  ILE A O   
388  C CB  . ILE A 57  ? 0.6257 0.4203 0.6250 0.1294  -0.2466 0.0003  50  ILE A CB  
389  C CG1 . ILE A 57  ? 0.6244 0.4421 0.6616 0.1339  -0.2128 -0.0248 50  ILE A CG1 
390  C CG2 . ILE A 57  ? 0.7092 0.4817 0.7300 0.1374  -0.2717 0.0025  50  ILE A CG2 
391  C CD1 . ILE A 57  ? 0.7165 0.5031 0.7380 0.1268  -0.2003 -0.0151 50  ILE A CD1 
392  N N   . ASP A 58  ? 0.7815 0.6077 0.7836 0.1405  -0.3075 -0.0011 51  ASP A N   
393  C CA  . ASP A 58  ? 0.7815 0.5969 0.7513 0.1363  -0.3369 0.0186  51  ASP A CA  
394  C C   . ASP A 58  ? 0.8463 0.6868 0.7652 0.1207  -0.3333 0.0247  51  ASP A C   
395  O O   . ASP A 58  ? 0.8601 0.6912 0.7228 0.1057  -0.3451 0.0513  51  ASP A O   
396  C CB  . ASP A 58  ? 0.7977 0.5641 0.7339 0.1263  -0.3512 0.0523  51  ASP A CB  
397  N N   . ASP A 59  ? 0.7470 0.6250 0.6878 0.1224  -0.3152 -0.0026 52  ASP A N   
398  C CA  . ASP A 59  ? 0.6632 0.5727 0.5690 0.1090  -0.3101 -0.0109 52  ASP A CA  
399  C C   . ASP A 59  ? 0.6981 0.5975 0.5341 0.0850  -0.2901 0.0089  52  ASP A C   
400  O O   . ASP A 59  ? 0.7236 0.6478 0.5167 0.0714  -0.2890 0.0054  52  ASP A O   
401  C CB  . ASP A 59  ? 0.8086 0.7344 0.7038 0.1103  -0.3358 -0.0102 52  ASP A CB  
402  C CG  . ASP A 59  ? 0.9728 0.9451 0.8922 0.1103  -0.3317 -0.0441 52  ASP A CG  
403  O OD1 . ASP A 59  ? 1.0498 1.0409 1.0244 0.1241  -0.3439 -0.0639 52  ASP A OD1 
404  O OD2 . ASP A 59  ? 1.0530 1.0438 0.9401 0.0954  -0.3145 -0.0537 52  ASP A OD2 
405  N N   . GLN A 60  ? 0.6576 0.5272 0.4851 0.0786  -0.2717 0.0256  53  GLN A N   
406  C CA  . GLN A 60  ? 0.6688 0.5370 0.4444 0.0546  -0.2445 0.0386  53  GLN A CA  
407  C C   . GLN A 60  ? 0.5584 0.4240 0.3689 0.0547  -0.2082 0.0254  53  GLN A C   
408  O O   . GLN A 60  ? 0.5763 0.4213 0.4263 0.0682  -0.2100 0.0245  53  GLN A O   
409  C CB  . GLN A 60  ? 0.7480 0.5806 0.4687 0.0397  -0.2607 0.0804  53  GLN A CB  
410  C CG  . GLN A 60  ? 0.8184 0.6616 0.5103 0.0345  -0.2840 0.0973  53  GLN A CG  
411  C CD  . GLN A 60  ? 0.9831 0.8756 0.6283 0.0187  -0.2734 0.0866  53  GLN A CD  
412  O OE1 . GLN A 60  ? 1.0148 0.9342 0.6595 0.0251  -0.2916 0.0760  53  GLN A OE1 
413  N NE2 . GLN A 60  ? 1.0633 0.9725 0.6736 -0.0016 -0.2429 0.0856  53  GLN A NE2 
414  N N   . TRP A 61  ? 0.5181 0.4071 0.3147 0.0406  -0.1774 0.0130  54  TRP A N   
415  C CA  . TRP A 61  ? 0.5162 0.4012 0.3374 0.0386  -0.1463 0.0050  54  TRP A CA  
416  C C   . TRP A 61  ? 0.5218 0.3752 0.3129 0.0274  -0.1419 0.0313  54  TRP A C   
417  O O   . TRP A 61  ? 0.5899 0.4413 0.3294 0.0093  -0.1448 0.0511  54  TRP A O   
418  C CB  . TRP A 61  ? 0.4740 0.3910 0.2956 0.0293  -0.1210 -0.0173 54  TRP A CB  
419  C CG  . TRP A 61  ? 0.4128 0.3532 0.2805 0.0393  -0.1222 -0.0443 54  TRP A CG  
420  C CD1 . TRP A 61  ? 0.4284 0.3931 0.2959 0.0409  -0.1378 -0.0604 54  TRP A CD1 
421  C CD2 . TRP A 61  ? 0.3686 0.3116 0.2893 0.0460  -0.1078 -0.0570 54  TRP A CD2 
422  N NE1 . TRP A 61  ? 0.3949 0.3741 0.3180 0.0478  -0.1344 -0.0826 54  TRP A NE1 
423  C CE2 . TRP A 61  ? 0.3595 0.3261 0.3137 0.0495  -0.1151 -0.0784 54  TRP A CE2 
424  C CE3 . TRP A 61  ? 0.3784 0.3084 0.3194 0.0475  -0.0900 -0.0517 54  TRP A CE3 
425  C CZ2 . TRP A 61  ? 0.3255 0.3016 0.3327 0.0511  -0.1041 -0.0903 54  TRP A CZ2 
426  C CZ3 . TRP A 61  ? 0.3493 0.2922 0.3370 0.0501  -0.0786 -0.0640 54  TRP A CZ3 
427  C CH2 . TRP A 61  ? 0.3018 0.2669 0.3223 0.0505  -0.0853 -0.0811 54  TRP A CH2 
428  N N   . ILE A 62  ? 0.4688 0.3017 0.2935 0.0365  -0.1347 0.0302  55  ILE A N   
429  C CA  . ILE A 62  ? 0.5312 0.3311 0.3429 0.0289  -0.1321 0.0493  55  ILE A CA  
430  C C   . ILE A 62  ? 0.4652 0.2773 0.2942 0.0253  -0.0997 0.0344  55  ILE A C   
431  O O   . ILE A 62  ? 0.4580 0.2912 0.3219 0.0353  -0.0865 0.0128  55  ILE A O   
432  C CB  . ILE A 62  ? 0.5111 0.2771 0.3539 0.0474  -0.1582 0.0542  55  ILE A CB  
433  C CG1 . ILE A 62  ? 0.7414 0.4881 0.5663 0.0515  -0.1976 0.0739  55  ILE A CG1 
434  C CG2 . ILE A 62  ? 0.7576 0.4907 0.6028 0.0428  -0.1539 0.0641  55  ILE A CG2 
435  C CD1 . ILE A 62  ? 0.8054 0.5561 0.5655 0.0277  -0.2033 0.0996  55  ILE A CD1 
436  N N   . VAL A 63  ? 0.4564 0.2558 0.2616 0.0093  -0.0883 0.0478  56  VAL A N   
437  C CA  . VAL A 63  ? 0.4084 0.2177 0.2290 0.0062  -0.0620 0.0352  56  VAL A CA  
438  C C   . VAL A 63  ? 0.4147 0.1925 0.2503 0.0103  -0.0665 0.0409  56  VAL A C   
439  O O   . VAL A 63  ? 0.4746 0.2192 0.2965 0.0052  -0.0861 0.0610  56  VAL A O   
440  C CB  . VAL A 63  ? 0.5098 0.3397 0.3002 -0.0145 -0.0437 0.0374  56  VAL A CB  
441  C CG1 . VAL A 63  ? 0.6049 0.4143 0.3608 -0.0344 -0.0505 0.0641  56  VAL A CG1 
442  C CG2 . VAL A 63  ? 0.5285 0.3727 0.3415 -0.0136 -0.0206 0.0208  56  VAL A CG2 
443  N N   . HIS A 64  ? 0.3939 0.1815 0.2578 0.0189  -0.0508 0.0233  57  HIS A N   
444  C CA  . HIS A 64  ? 0.4511 0.2173 0.3306 0.0232  -0.0522 0.0207  57  HIS A CA  
445  C C   . HIS A 64  ? 0.4133 0.1849 0.2798 0.0075  -0.0337 0.0223  57  HIS A C   
446  O O   . HIS A 64  ? 0.3884 0.1828 0.2664 0.0101  -0.0162 0.0082  57  HIS A O   
447  C CB  . HIS A 64  ? 0.4020 0.1840 0.3183 0.0425  -0.0477 -0.0020 57  HIS A CB  
448  C CG  . HIS A 64  ? 0.4106 0.1946 0.3490 0.0588  -0.0656 -0.0084 57  HIS A CG  
449  N ND1 . HIS A 64  ? 0.5172 0.2693 0.4635 0.0681  -0.0935 -0.0022 57  HIS A ND1 
450  C CD2 . HIS A 64  ? 0.4117 0.2256 0.3705 0.0673  -0.0621 -0.0207 57  HIS A CD2 
451  C CE1 . HIS A 64  ? 0.5064 0.2722 0.4783 0.0841  -0.1066 -0.0129 57  HIS A CE1 
452  N NE2 . HIS A 64  ? 0.4484 0.2538 0.4283 0.0826  -0.0864 -0.0246 57  HIS A NE2 
453  N N   . GLN A 65  ? 0.4588 0.2095 0.3029 -0.0103 -0.0394 0.0410  58  GLN A N   
454  C CA  . GLN A 65  ? 0.4454 0.2082 0.2813 -0.0270 -0.0217 0.0407  58  GLN A CA  
455  C C   . GLN A 65  ? 0.4311 0.1918 0.2922 -0.0181 -0.0155 0.0241  58  GLN A C   
456  O O   . GLN A 65  ? 0.3954 0.1790 0.2595 -0.0228 0.0008  0.0146  58  GLN A O   
457  C CB  . GLN A 65  ? 0.4819 0.2248 0.2923 -0.0519 -0.0288 0.0657  58  GLN A CB  
458  C CG  . GLN A 65  ? 0.5250 0.2749 0.3010 -0.0644 -0.0353 0.0846  58  GLN A CG  
459  C CD  . GLN A 65  ? 0.6169 0.3620 0.3616 -0.0966 -0.0344 0.1107  58  GLN A CD  
460  O OE1 . GLN A 65  ? 0.6584 0.4092 0.4102 -0.1115 -0.0213 0.1089  58  GLN A OE1 
461  N NE2 . GLN A 65  ? 0.6524 0.3963 0.3686 -0.1073 -0.0479 0.1328  58  GLN A NE2 
462  N N   . TRP A 66  ? 0.4144 0.1511 0.2954 -0.0040 -0.0301 0.0176  59  TRP A N   
463  C CA  . TRP A 66  ? 0.3994 0.1407 0.3002 0.0037  -0.0242 -0.0018 59  TRP A CA  
464  C C   . TRP A 66  ? 0.3834 0.1623 0.2907 0.0133  -0.0066 -0.0173 59  TRP A C   
465  O O   . TRP A 66  ? 0.3582 0.1508 0.2687 0.0122  0.0029  -0.0273 59  TRP A O   
466  C CB  . TRP A 66  ? 0.4004 0.1154 0.3256 0.0196  -0.0436 -0.0135 59  TRP A CB  
467  C CG  . TRP A 66  ? 0.4512 0.1836 0.3968 0.0413  -0.0471 -0.0288 59  TRP A CG  
468  C CD1 . TRP A 66  ? 0.4671 0.1925 0.4196 0.0491  -0.0628 -0.0213 59  TRP A CD1 
469  C CD2 . TRP A 66  ? 0.4264 0.1944 0.3902 0.0555  -0.0342 -0.0541 59  TRP A CD2 
470  N NE1 . TRP A 66  ? 0.4533 0.2090 0.4321 0.0674  -0.0593 -0.0427 59  TRP A NE1 
471  C CE2 . TRP A 66  ? 0.4109 0.1943 0.3955 0.0699  -0.0404 -0.0619 59  TRP A CE2 
472  C CE3 . TRP A 66  ? 0.3928 0.1845 0.3552 0.0556  -0.0187 -0.0698 59  TRP A CE3 
473  C CZ2 . TRP A 66  ? 0.3682 0.1927 0.3724 0.0813  -0.0282 -0.0844 59  TRP A CZ2 
474  C CZ3 . TRP A 66  ? 0.4049 0.2357 0.3814 0.0670  -0.0080 -0.0895 59  TRP A CZ3 
475  C CH2 . TRP A 66  ? 0.3870 0.2349 0.3844 0.0784  -0.0113 -0.0964 59  TRP A CH2 
476  N N   . ILE A 67  ? 0.3279 0.1230 0.2368 0.0208  -0.0041 -0.0174 60  ILE A N   
477  C CA  . ILE A 67  ? 0.3122 0.1384 0.2282 0.0255  0.0103  -0.0264 60  ILE A CA  
478  C C   . ILE A 67  ? 0.3413 0.1799 0.2468 0.0140  0.0210  -0.0216 60  ILE A C   
479  O O   . ILE A 67  ? 0.3135 0.1674 0.2236 0.0147  0.0289  -0.0266 60  ILE A O   
480  C CB  . ILE A 67  ? 0.3185 0.1577 0.2460 0.0343  0.0082  -0.0284 60  ILE A CB  
481  C CG1 . ILE A 67  ? 0.3400 0.1749 0.2874 0.0489  -0.0024 -0.0403 60  ILE A CG1 
482  C CG2 . ILE A 67  ? 0.3332 0.2000 0.2683 0.0335  0.0215  -0.0316 60  ILE A CG2 
483  C CD1 . ILE A 67  ? 0.3776 0.2288 0.3436 0.0582  -0.0070 -0.0450 60  ILE A CD1 
484  N N   . LYS A 68  ? 0.3170 0.1525 0.2092 0.0035  0.0202  -0.0129 61  LYS A N   
485  C CA  . LYS A 68  ? 0.3348 0.1878 0.2240 -0.0059 0.0300  -0.0154 61  LYS A CA  
486  C C   . LYS A 68  ? 0.3359 0.1880 0.2280 -0.0118 0.0333  -0.0187 61  LYS A C   
487  O O   . LYS A 68  ? 0.3143 0.1839 0.2156 -0.0116 0.0391  -0.0261 61  LYS A O   
488  C CB  . LYS A 68  ? 0.3444 0.2029 0.2161 -0.0184 0.0305  -0.0091 61  LYS A CB  
489  C CG  . LYS A 68  ? 0.3861 0.2523 0.2550 -0.0131 0.0264  -0.0104 61  LYS A CG  
490  C CD  . LYS A 68  ? 0.4660 0.3449 0.3104 -0.0282 0.0282  -0.0058 61  LYS A CD  
491  C CE  . LYS A 68  ? 0.4699 0.3715 0.3140 -0.0250 0.0286  -0.0173 61  LYS A CE  
492  N NZ  . LYS A 68  ? 0.3917 0.3152 0.2067 -0.0428 0.0333  -0.0150 61  LYS A NZ  
493  N N   . LYS A 69  ? 0.3364 0.1668 0.2242 -0.0172 0.0264  -0.0137 62  LYS A N   
494  C CA  . LYS A 69  ? 0.3183 0.1475 0.2129 -0.0232 0.0273  -0.0197 62  LYS A CA  
495  C C   . LYS A 69  ? 0.3445 0.1857 0.2494 -0.0098 0.0287  -0.0327 62  LYS A C   
496  O O   . LYS A 69  ? 0.3152 0.1712 0.2256 -0.0123 0.0317  -0.0392 62  LYS A O   
497  C CB  . LYS A 69  ? 0.3496 0.1465 0.2436 -0.0304 0.0153  -0.0132 62  LYS A CB  
498  C CG  . LYS A 69  ? 0.3678 0.1538 0.2458 -0.0517 0.0133  0.0067  62  LYS A CG  
499  C CD  . LYS A 69  ? 0.3980 0.1410 0.2778 -0.0593 -0.0050 0.0189  62  LYS A CD  
500  C CE  . LYS A 69  ? 0.4371 0.1707 0.2942 -0.0870 -0.0070 0.0463  62  LYS A CE  
501  N NZ  . LYS A 69  ? 0.5172 0.2018 0.3775 -0.0956 -0.0301 0.0645  62  LYS A NZ  
502  N N   . ALA A 70  ? 0.3048 0.1447 0.2120 0.0035  0.0262  -0.0364 63  ALA A N   
503  C CA  . ALA A 70  ? 0.3074 0.1656 0.2173 0.0123  0.0293  -0.0459 63  ALA A CA  
504  C C   . ALA A 70  ? 0.2881 0.1650 0.1978 0.0107  0.0347  -0.0401 63  ALA A C   
505  O O   . ALA A 70  ? 0.2997 0.1891 0.2079 0.0114  0.0340  -0.0428 63  ALA A O   
506  C CB  . ALA A 70  ? 0.3047 0.1687 0.2193 0.0238  0.0292  -0.0520 63  ALA A CB  
507  N N   . VAL A 71  ? 0.2734 0.1514 0.1859 0.0098  0.0370  -0.0329 64  VAL A N   
508  C CA  . VAL A 71  ? 0.2832 0.1730 0.2035 0.0099  0.0375  -0.0297 64  VAL A CA  
509  C C   . VAL A 71  ? 0.2839 0.1805 0.2104 0.0057  0.0359  -0.0352 64  VAL A C   
510  O O   . VAL A 71  ? 0.2872 0.1916 0.2201 0.0087  0.0307  -0.0349 64  VAL A O   
511  C CB  . VAL A 71  ? 0.2709 0.1605 0.1981 0.0099  0.0381  -0.0275 64  VAL A CB  
512  C CG1 . VAL A 71  ? 0.2945 0.1916 0.2384 0.0111  0.0346  -0.0291 64  VAL A CG1 
513  C CG2 . VAL A 71  ? 0.3152 0.2042 0.2435 0.0143  0.0385  -0.0232 64  VAL A CG2 
514  N N   . LEU A 72  ? 0.2923 0.1878 0.2176 -0.0027 0.0390  -0.0394 65  LEU A N   
515  C CA  . LEU A 72  ? 0.2737 0.1842 0.2106 -0.0088 0.0396  -0.0480 65  LEU A CA  
516  C C   . LEU A 72  ? 0.3160 0.2268 0.2541 -0.0077 0.0339  -0.0520 65  LEU A C   
517  O O   . LEU A 72  ? 0.2925 0.2187 0.2449 -0.0056 0.0289  -0.0589 65  LEU A O   
518  C CB  . LEU A 72  ? 0.2790 0.1929 0.2107 -0.0239 0.0467  -0.0483 65  LEU A CB  
519  C CG  . LEU A 72  ? 0.2879 0.2142 0.2176 -0.0258 0.0521  -0.0499 65  LEU A CG  
520  C CD1 . LEU A 72  ? 0.3772 0.3043 0.2882 -0.0434 0.0581  -0.0422 65  LEU A CD1 
521  C CD2 . LEU A 72  ? 0.3424 0.2981 0.2975 -0.0213 0.0536  -0.0674 65  LEU A CD2 
522  N N   . LEU A 73  ? 0.2920 0.1879 0.2182 -0.0074 0.0321  -0.0512 66  LEU A N   
523  C CA  . LEU A 73  ? 0.2717 0.1719 0.1978 -0.0052 0.0255  -0.0598 66  LEU A CA  
524  C C   . LEU A 73  ? 0.2661 0.1796 0.1863 0.0043  0.0205  -0.0568 66  LEU A C   
525  O O   . LEU A 73  ? 0.3154 0.2407 0.2369 0.0055  0.0124  -0.0625 66  LEU A O   
526  C CB  . LEU A 73  ? 0.2855 0.1690 0.2048 -0.0040 0.0229  -0.0657 66  LEU A CB  
527  C CG  . LEU A 73  ? 0.3263 0.1892 0.2523 -0.0166 0.0212  -0.0651 66  LEU A CG  
528  C CD1 . LEU A 73  ? 0.3498 0.1884 0.2755 -0.0108 0.0137  -0.0705 66  LEU A CD1 
529  C CD2 . LEU A 73  ? 0.3669 0.2394 0.3064 -0.0278 0.0180  -0.0741 66  LEU A CD2 
530  N N   . SER A 74  ? 0.2855 0.1979 0.1991 0.0091  0.0236  -0.0460 67  SER A N   
531  C CA  . SER A 74  ? 0.2985 0.2218 0.2035 0.0129  0.0179  -0.0363 67  SER A CA  
532  C C   . SER A 74  ? 0.2886 0.2159 0.2087 0.0144  0.0064  -0.0328 67  SER A C   
533  O O   . SER A 74  ? 0.3223 0.2573 0.2344 0.0164  -0.0051 -0.0257 67  SER A O   
534  C CB  . SER A 74  ? 0.3168 0.2385 0.2174 0.0134  0.0238  -0.0238 67  SER A CB  
535  O OG  . SER A 74  ? 0.3220 0.2351 0.2399 0.0133  0.0222  -0.0171 67  SER A OG  
536  N N   . PHE A 75  ? 0.2809 0.2065 0.2236 0.0139  0.0078  -0.0393 68  PHE A N   
537  C CA  . PHE A 75  ? 0.2579 0.1926 0.2256 0.0183  -0.0044 -0.0447 68  PHE A CA  
538  C C   . PHE A 75  ? 0.2835 0.2322 0.2558 0.0169  -0.0108 -0.0568 68  PHE A C   
539  O O   . PHE A 75  ? 0.3378 0.2938 0.3185 0.0230  -0.0277 -0.0558 68  PHE A O   
540  C CB  . PHE A 75  ? 0.2817 0.2229 0.2744 0.0178  0.0020  -0.0572 68  PHE A CB  
541  C CG  . PHE A 75  ? 0.3046 0.2344 0.2965 0.0192  0.0067  -0.0506 68  PHE A CG  
542  C CD1 . PHE A 75  ? 0.3236 0.2386 0.3048 0.0212  0.0017  -0.0327 68  PHE A CD1 
543  C CD2 . PHE A 75  ? 0.3905 0.3292 0.3920 0.0161  0.0164  -0.0630 68  PHE A CD2 
544  C CE1 . PHE A 75  ? 0.3706 0.2769 0.3566 0.0212  0.0047  -0.0287 68  PHE A CE1 
545  C CE2 . PHE A 75  ? 0.4204 0.3508 0.4222 0.0178  0.0184  -0.0602 68  PHE A CE2 
546  C CZ  . PHE A 75  ? 0.4076 0.3204 0.4046 0.0208  0.0118  -0.0436 68  PHE A CZ  
547  N N   . ARG A 76  ? 0.2783 0.2290 0.2471 0.0081  -0.0002 -0.0672 69  ARG A N   
548  C CA  . ARG A 76  ? 0.2891 0.2536 0.2686 0.0037  -0.0060 -0.0812 69  ARG A CA  
549  C C   . ARG A 76  ? 0.3245 0.2910 0.2849 0.0087  -0.0187 -0.0802 69  ARG A C   
550  O O   . ARG A 76  ? 0.3210 0.3031 0.2935 0.0099  -0.0316 -0.0907 69  ARG A O   
551  C CB  . ARG A 76  ? 0.3457 0.3042 0.3250 -0.0105 0.0064  -0.0877 69  ARG A CB  
552  C CG  . ARG A 76  ? 0.4500 0.4231 0.4482 -0.0201 0.0018  -0.1030 69  ARG A CG  
553  C CD  . ARG A 76  ? 0.4973 0.4597 0.4980 -0.0392 0.0125  -0.1033 69  ARG A CD  
554  N NE  . ARG A 76  ? 0.4409 0.4120 0.4470 -0.0495 0.0266  -0.0976 69  ARG A NE  
555  C CZ  . ARG A 76  ? 0.4557 0.4547 0.4843 -0.0657 0.0349  -0.1058 69  ARG A CZ  
556  N NH1 . ARG A 76  ? 0.4697 0.4903 0.5245 -0.0727 0.0295  -0.1204 69  ARG A NH1 
557  N NH2 . ARG A 76  ? 0.5667 0.5779 0.5919 -0.0763 0.0494  -0.1010 69  ARG A NH2 
558  N N   . LEU A 77  ? 0.3587 0.1705 0.5033 -0.0288 -0.0378 -0.0111 70  LEU A N   
559  C CA  . LEU A 77  ? 0.3966 0.1902 0.5478 -0.0249 -0.0474 -0.0539 70  LEU A CA  
560  C C   . LEU A 77  ? 0.3778 0.1983 0.4827 -0.0211 -0.0494 -0.0809 70  LEU A C   
561  O O   . LEU A 77  ? 0.3932 0.2121 0.4984 -0.0166 -0.0573 -0.1168 70  LEU A O   
562  C CB  . LEU A 77  ? 0.3914 0.1641 0.5514 -0.0077 -0.0482 -0.0617 70  LEU A CB  
563  C CG  . LEU A 77  ? 0.4264 0.1662 0.6384 -0.0067 -0.0477 -0.0378 70  LEU A CG  
564  C CD1 . LEU A 77  ? 0.5110 0.2404 0.7237 0.0139  -0.0487 -0.0519 70  LEU A CD1 
565  C CD2 . LEU A 77  ? 0.4850 0.2151 0.7355 -0.0217 -0.0514 -0.0449 70  LEU A CD2 
566  N N   . HIS A 78  ? 0.3384 0.1854 0.4062 -0.0210 -0.0426 -0.0650 71  HIS A N   
567  C CA  . HIS A 78  ? 0.3354 0.2039 0.3646 -0.0168 -0.0434 -0.0833 71  HIS A CA  
568  C C   . HIS A 78  ? 0.4019 0.2900 0.4219 -0.0257 -0.0434 -0.0756 71  HIS A C   
569  O O   . HIS A 78  ? 0.3375 0.2342 0.3633 -0.0315 -0.0382 -0.0515 71  HIS A O   
570  C CB  . HIS A 78  ? 0.4001 0.2802 0.3963 -0.0062 -0.0357 -0.0773 71  HIS A CB  
571  C CG  . HIS A 78  ? 0.5562 0.4262 0.5569 0.0053  -0.0360 -0.0898 71  HIS A CG  
572  N ND1 . HIS A 78  ? 0.5170 0.3803 0.5284 0.0117  -0.0316 -0.0730 71  HIS A ND1 
573  C CD2 . HIS A 78  ? 0.6237 0.4946 0.6225 0.0137  -0.0408 -0.1189 71  HIS A CD2 
574  C CE1 . HIS A 78  ? 0.6639 0.5209 0.6805 0.0238  -0.0336 -0.0912 71  HIS A CE1 
575  N NE2 . HIS A 78  ? 0.6036 0.4658 0.6127 0.0251  -0.0389 -0.1205 71  HIS A NE2 
576  N N   . ASP A 79  ? 0.3429 0.2444 0.3483 -0.0240 -0.0494 -0.0968 72  ASP A N   
577  C CA  . ASP A 79  ? 0.3166 0.2398 0.3088 -0.0272 -0.0501 -0.0921 72  ASP A CA  
578  C C   . ASP A 79  ? 0.3246 0.2573 0.2829 -0.0191 -0.0422 -0.0797 72  ASP A C   
579  O O   . ASP A 79  ? 0.3178 0.2457 0.2595 -0.0118 -0.0376 -0.0808 72  ASP A O   
580  C CB  . ASP A 79  ? 0.3500 0.2899 0.3388 -0.0250 -0.0604 -0.1181 72  ASP A CB  
581  C CG  . ASP A 79  ? 0.5750 0.5144 0.6046 -0.0375 -0.0698 -0.1326 72  ASP A CG  
582  O OD1 . ASP A 79  ? 0.5442 0.4828 0.5982 -0.0498 -0.0674 -0.1147 72  ASP A OD1 
583  O OD2 . ASP A 79  ? 0.5713 0.5178 0.6080 -0.0345 -0.0768 -0.1576 72  ASP A OD2 
584  N N   . ASN A 80  ? 0.3077 0.2548 0.2608 -0.0207 -0.0407 -0.0693 73  ASN A N   
585  C CA  . ASN A 80  ? 0.2863 0.2394 0.2145 -0.0129 -0.0354 -0.0630 73  ASN A CA  
586  C C   . ASN A 80  ? 0.3327 0.2918 0.2409 -0.0046 -0.0384 -0.0719 73  ASN A C   
587  O O   . ASN A 80  ? 0.3508 0.3221 0.2612 -0.0035 -0.0467 -0.0848 73  ASN A O   
588  C CB  . ASN A 80  ? 0.2703 0.2384 0.2024 -0.0135 -0.0345 -0.0546 73  ASN A CB  
589  C CG  . ASN A 80  ? 0.2611 0.2363 0.2079 -0.0190 -0.0295 -0.0429 73  ASN A CG  
590  O OD1 . ASN A 80  ? 0.2895 0.2611 0.2316 -0.0171 -0.0238 -0.0376 73  ASN A OD1 
591  N ND2 . ASN A 80  ? 0.3419 0.3345 0.3074 -0.0254 -0.0315 -0.0377 73  ASN A ND2 
592  N N   . ALA A 81  ? 0.3098 0.2655 0.2005 0.0012  -0.0314 -0.0642 74  ALA A N   
593  C CA  . ALA A 81  ? 0.3697 0.3363 0.2408 0.0097  -0.0313 -0.0638 74  ALA A CA  
594  C C   . ALA A 81  ? 0.3002 0.2613 0.1648 0.0133  -0.0242 -0.0463 74  ALA A C   
595  O O   . ALA A 81  ? 0.3128 0.2607 0.1862 0.0088  -0.0182 -0.0420 74  ALA A O   
596  C CB  . ALA A 81  ? 0.4694 0.4381 0.3321 0.0122  -0.0281 -0.0717 74  ALA A CB  
597  N N   . VAL A 82  ? 0.3273 0.3010 0.1799 0.0224  -0.0256 -0.0370 75  VAL A N   
598  C CA  . VAL A 82  ? 0.3147 0.2777 0.1677 0.0265  -0.0185 -0.0171 75  VAL A CA  
599  C C   . VAL A 82  ? 0.4220 0.3776 0.2726 0.0220  -0.0078 -0.0094 75  VAL A C   
600  O O   . VAL A 82  ? 0.4015 0.3739 0.2385 0.0234  -0.0061 -0.0125 75  VAL A O   
601  C CB  . VAL A 82  ? 0.4153 0.3966 0.2572 0.0398  -0.0222 -0.0024 75  VAL A CB  
602  C CG1 . VAL A 82  ? 0.4544 0.4166 0.3057 0.0446  -0.0147 0.0222  75  VAL A CG1 
603  C CG2 . VAL A 82  ? 0.4320 0.4280 0.2787 0.0440  -0.0336 -0.0131 75  VAL A CG2 
604  N N   . MET A 83  ? 0.3454 0.2802 0.2123 0.0166  -0.0010 -0.0028 76  MET A N   
605  C CA  . MET A 83  ? 0.3542 0.2837 0.2267 0.0092  0.0095  0.0035  76  MET A CA  
606  C C   . MET A 83  ? 0.4220 0.3325 0.3132 0.0086  0.0159  0.0225  76  MET A C   
607  O O   . MET A 83  ? 0.3573 0.2528 0.2627 0.0128  0.0118  0.0212  76  MET A O   
608  C CB  . MET A 83  ? 0.4620 0.3869 0.3458 0.0002  0.0103  -0.0145 76  MET A CB  
609  C CG  . MET A 83  ? 0.4681 0.4016 0.3449 0.0014  0.0025  -0.0300 76  MET A CG  
610  S SD  . MET A 83  ? 0.5931 0.5274 0.4836 -0.0050 0.0033  -0.0423 76  MET A SD  
611  C CE  . MET A 83  ? 0.5275 0.4687 0.4178 -0.0086 0.0121  -0.0414 76  MET A CE  
612  N N   . GLY A 84  ? 0.4829 0.3953 0.3781 0.0040  0.0264  0.0406  77  GLY A N   
613  C CA  . GLY A 84  ? 0.4253 0.3135 0.3494 -0.0003 0.0340  0.0599  77  GLY A CA  
614  C C   . GLY A 84  ? 0.5794 0.4671 0.4990 0.0125  0.0345  0.0913  77  GLY A C   
615  O O   . GLY A 84  ? 0.6055 0.5229 0.4950 0.0241  0.0309  0.1003  77  GLY A O   
616  N N   . GLN A 85  ? 0.6448 0.5003 0.5981 0.0121  0.0381  0.1065  78  GLN A N   
617  C CA  . GLN A 85  ? 0.6431 0.4941 0.5995 0.0259  0.0399  0.1440  78  GLN A CA  
618  C C   . GLN A 85  ? 0.6181 0.4215 0.6238 0.0245  0.0418  0.1498  78  GLN A C   
619  O O   . GLN A 85  ? 0.6069 0.3867 0.6434 0.0114  0.0422  0.1222  78  GLN A O   
620  C CB  . GLN A 85  ? 0.8101 0.6872 0.7541 0.0247  0.0524  0.1825  78  GLN A CB  
621  C CG  . GLN A 85  ? 0.7772 0.6399 0.7520 0.0036  0.0659  0.1877  78  GLN A CG  
622  C CD  . GLN A 85  ? 1.0813 0.9734 1.0499 0.0021  0.0807  0.2323  78  GLN A CD  
623  O OE1 . GLN A 85  ? 1.2479 1.1892 1.1784 0.0066  0.0824  0.2319  78  GLN A OE1 
624  N NE2 . GLN A 85  ? 1.1930 1.0581 1.2021 -0.0037 0.0913  0.2702  78  GLN A NE2 
625  N N   . GLY A 86  ? 0.6495 0.4417 0.6654 0.0396  0.0426  0.1853  79  GLY A N   
626  C CA  . GLY A 86  ? 0.6831 0.4258 0.7518 0.0416  0.0440  0.1931  79  GLY A CA  
627  C C   . GLY A 86  ? 0.5699 0.2951 0.6557 0.0438  0.0326  0.1446  79  GLY A C   
628  O O   . GLY A 86  ? 0.5903 0.3424 0.6449 0.0526  0.0220  0.1199  79  GLY A O   
629  N N   . PRO A 87  ? 0.7374 0.4210 0.8775 0.0354  0.0346  0.1282  80  PRO A N   
630  C CA  . PRO A 87  ? 0.7360 0.4119 0.8946 0.0401  0.0240  0.0792  80  PRO A CA  
631  C C   . PRO A 87  ? 0.7740 0.4808 0.9110 0.0265  0.0209  0.0370  80  PRO A C   
632  O O   . PRO A 87  ? 0.7401 0.4475 0.8964 0.0275  0.0143  -0.0042 80  PRO A O   
633  C CB  . PRO A 87  ? 0.7931 0.4355 1.0041 0.0330  0.0254  0.0699  80  PRO A CB  
634  C CG  . PRO A 87  ? 0.7492 0.3879 0.9699 0.0127  0.0377  0.0981  80  PRO A CG  
635  C CD  . PRO A 87  ? 0.6034 0.2631 0.7829 0.0204  0.0438  0.1464  80  PRO A CD  
636  N N   . LEU A 88  ? 0.5531 0.2885 0.6526 0.0159  0.0255  0.0468  81  LEU A N   
637  C CA  . LEU A 88  ? 0.4602 0.2236 0.5410 0.0052  0.0231  0.0143  81  LEU A CA  
638  C C   . LEU A 88  ? 0.4570 0.2550 0.4848 0.0100  0.0206  0.0246  81  LEU A C   
639  O O   . LEU A 88  ? 0.5439 0.3585 0.5528 0.0005  0.0262  0.0320  81  LEU A O   
640  C CB  . LEU A 88  ? 0.5523 0.3124 0.6553 -0.0156 0.0319  0.0086  81  LEU A CB  
641  C CG  . LEU A 88  ? 0.6255 0.3520 0.7900 -0.0252 0.0344  -0.0066 81  LEU A CG  
642  C CD1 . LEU A 88  ? 0.6336 0.3660 0.8171 -0.0479 0.0439  -0.0067 81  LEU A CD1 
643  C CD2 . LEU A 88  ? 0.5677 0.3008 0.7486 -0.0191 0.0240  -0.0544 81  LEU A CD2 
644  N N   . GLN A 89  ? 0.4778 0.2878 0.4868 0.0252  0.0118  0.0233  82  GLN A N   
645  C CA  . GLN A 89  ? 0.3654 0.2077 0.3340 0.0283  0.0069  0.0231  82  GLN A CA  
646  C C   . GLN A 89  ? 0.3274 0.1876 0.2909 0.0240  0.0012  -0.0083 82  GLN A C   
647  O O   . GLN A 89  ? 0.3183 0.1775 0.3003 0.0286  -0.0028 -0.0273 82  GLN A O   
648  C CB  . GLN A 89  ? 0.4741 0.3280 0.4280 0.0455  0.0000  0.0386  82  GLN A CB  
649  C CG  . GLN A 89  ? 0.6501 0.5005 0.6004 0.0541  0.0047  0.0761  82  GLN A CG  
650  C CD  . GLN A 89  ? 0.6159 0.5033 0.5281 0.0565  0.0037  0.0867  82  GLN A CD  
651  O OE1 . GLN A 89  ? 0.8057 0.7196 0.6991 0.0691  -0.0052 0.0872  82  GLN A OE1 
652  N NE2 . GLN A 89  ? 0.7062 0.6007 0.6091 0.0452  0.0121  0.0911  82  GLN A NE2 
653  N N   . PHE A 90  ? 0.3051 0.1851 0.2448 0.0175  0.0010  -0.0121 83  PHE A N   
654  C CA  . PHE A 90  ? 0.3053 0.2039 0.2400 0.0132  -0.0029 -0.0324 83  PHE A CA  
655  C C   . PHE A 90  ? 0.3175 0.2337 0.2299 0.0148  -0.0083 -0.0296 83  PHE A C   
656  O O   . PHE A 90  ? 0.2852 0.2045 0.1832 0.0190  -0.0095 -0.0177 83  PHE A O   
657  C CB  . PHE A 90  ? 0.2741 0.1752 0.2139 0.0023  0.0025  -0.0420 83  PHE A CB  
658  C CG  . PHE A 90  ? 0.2936 0.1767 0.2598 -0.0031 0.0085  -0.0443 83  PHE A CG  
659  C CD1 . PHE A 90  ? 0.2851 0.1655 0.2778 -0.0016 0.0063  -0.0645 83  PHE A CD1 
660  C CD2 . PHE A 90  ? 0.3377 0.2101 0.3063 -0.0098 0.0163  -0.0276 83  PHE A CD2 
661  C CE1 . PHE A 90  ? 0.3046 0.1660 0.3304 -0.0082 0.0107  -0.0715 83  PHE A CE1 
662  C CE2 . PHE A 90  ? 0.3981 0.2524 0.3995 -0.0181 0.0225  -0.0281 83  PHE A CE2 
663  C CZ  . PHE A 90  ? 0.4348 0.2801 0.4675 -0.0180 0.0190  -0.0516 83  PHE A CZ  
664  N N   . TYR A 91  ? 0.2617 0.1932 0.1743 0.0111  -0.0115 -0.0411 84  TYR A N   
665  C CA  . TYR A 91  ? 0.2477 0.1925 0.1509 0.0102  -0.0175 -0.0413 84  TYR A CA  
666  C C   . TYR A 91  ? 0.2458 0.1996 0.1543 0.0028  -0.0165 -0.0468 84  TYR A C   
667  O O   . TYR A 91  ? 0.2490 0.2182 0.1674 0.0027  -0.0166 -0.0498 84  TYR A O   
668  C CB  . TYR A 91  ? 0.2730 0.2305 0.1810 0.0168  -0.0238 -0.0415 84  TYR A CB  
669  C CG  . TYR A 91  ? 0.2481 0.2214 0.1538 0.0138  -0.0309 -0.0443 84  TYR A CG  
670  C CD1 . TYR A 91  ? 0.2750 0.2500 0.1679 0.0158  -0.0347 -0.0444 84  TYR A CD1 
671  C CD2 . TYR A 91  ? 0.2505 0.2419 0.1699 0.0089  -0.0338 -0.0481 84  TYR A CD2 
672  C CE1 . TYR A 91  ? 0.2932 0.2847 0.1902 0.0124  -0.0430 -0.0541 84  TYR A CE1 
673  C CE2 . TYR A 91  ? 0.2743 0.2791 0.2007 0.0032  -0.0408 -0.0524 84  TYR A CE2 
674  C CZ  . TYR A 91  ? 0.3257 0.3285 0.2424 0.0047  -0.0461 -0.0582 84  TYR A CZ  
675  O OH  . TYR A 91  ? 0.3573 0.3749 0.2868 -0.0017 -0.0545 -0.0695 84  TYR A OH  
676  N N   . ASP A 92  ? 0.2498 0.1982 0.1525 -0.0011 -0.0151 -0.0467 85  ASP A N   
677  C CA  . ASP A 92  ? 0.2667 0.2219 0.1766 -0.0053 -0.0135 -0.0468 85  ASP A CA  
678  C C   . ASP A 92  ? 0.2879 0.2343 0.1961 -0.0067 -0.0154 -0.0482 85  ASP A C   
679  O O   . ASP A 92  ? 0.3035 0.2444 0.2020 -0.0041 -0.0171 -0.0529 85  ASP A O   
680  C CB  . ASP A 92  ? 0.2774 0.2381 0.1898 -0.0052 -0.0078 -0.0498 85  ASP A CB  
681  C CG  . ASP A 92  ? 0.2763 0.2559 0.1951 -0.0058 -0.0068 -0.0464 85  ASP A CG  
682  O OD1 . ASP A 92  ? 0.2883 0.2796 0.2139 -0.0068 -0.0089 -0.0382 85  ASP A OD1 
683  O OD2 . ASP A 92  ? 0.2860 0.2737 0.2051 -0.0050 -0.0035 -0.0498 85  ASP A OD2 
684  N N   . LYS A 93  ? 0.2724 0.2212 0.1919 -0.0089 -0.0152 -0.0438 86  LYS A N   
685  C CA  . LYS A 93  ? 0.2700 0.2064 0.1973 -0.0089 -0.0183 -0.0468 86  LYS A CA  
686  C C   . LYS A 93  ? 0.2952 0.2305 0.2218 -0.0042 -0.0142 -0.0459 86  LYS A C   
687  O O   . LYS A 93  ? 0.3062 0.2299 0.2424 -0.0011 -0.0167 -0.0504 86  LYS A O   
688  C CB  . LYS A 93  ? 0.2977 0.2329 0.2484 -0.0149 -0.0218 -0.0384 86  LYS A CB  
689  C CG  . LYS A 93  ? 0.2844 0.2374 0.2437 -0.0158 -0.0169 -0.0194 86  LYS A CG  
690  C CD  . LYS A 93  ? 0.3204 0.2728 0.3079 -0.0230 -0.0181 -0.0030 86  LYS A CD  
691  C CE  . LYS A 93  ? 0.3664 0.3216 0.3656 -0.0319 -0.0228 -0.0082 86  LYS A CE  
692  N NZ  . LYS A 93  ? 0.4527 0.3997 0.4892 -0.0425 -0.0242 0.0057  86  LYS A NZ  
693  N N   . VAL A 94  ? 0.2688 0.2173 0.1881 -0.0028 -0.0087 -0.0435 87  VAL A N   
694  C CA  . VAL A 94  ? 0.2657 0.2216 0.1852 0.0020  -0.0052 -0.0440 87  VAL A CA  
695  C C   . VAL A 94  ? 0.2710 0.2287 0.1792 0.0013  -0.0007 -0.0530 87  VAL A C   
696  O O   . VAL A 94  ? 0.2885 0.2502 0.1944 -0.0032 0.0022  -0.0540 87  VAL A O   
697  C CB  . VAL A 94  ? 0.2673 0.2483 0.1920 0.0037  -0.0030 -0.0357 87  VAL A CB  
698  C CG1 . VAL A 94  ? 0.3045 0.2980 0.2314 0.0106  -0.0009 -0.0363 87  VAL A CG1 
699  C CG2 . VAL A 94  ? 0.2807 0.2680 0.2165 0.0035  -0.0051 -0.0198 87  VAL A CG2 
700  N N   . PRO A 95  ? 0.2727 0.2294 0.1776 0.0057  0.0007  -0.0592 88  PRO A N   
701  C CA  . PRO A 95  ? 0.2699 0.2357 0.1666 0.0037  0.0073  -0.0624 88  PRO A CA  
702  C C   . PRO A 95  ? 0.2775 0.2595 0.1826 -0.0005 0.0125  -0.0623 88  PRO A C   
703  O O   . PRO A 95  ? 0.2796 0.2744 0.1927 0.0030  0.0106  -0.0624 88  PRO A O   
704  C CB  . PRO A 95  ? 0.3388 0.3100 0.2321 0.0121  0.0074  -0.0710 88  PRO A CB  
705  C CG  . PRO A 95  ? 0.4477 0.4026 0.3488 0.0173  -0.0011 -0.0761 88  PRO A CG  
706  C CD  . PRO A 95  ? 0.3535 0.3018 0.2658 0.0133  -0.0035 -0.0642 88  PRO A CD  
707  N N   . THR A 96  ? 0.2737 0.2580 0.1804 -0.0081 0.0186  -0.0614 89  THR A N   
708  C CA  . THR A 96  ? 0.2609 0.2632 0.1827 -0.0145 0.0233  -0.0668 89  THR A CA  
709  C C   . THR A 96  ? 0.2486 0.2722 0.1718 -0.0116 0.0280  -0.0698 89  THR A C   
710  O O   . THR A 96  ? 0.2707 0.2947 0.1827 -0.0054 0.0296  -0.0679 89  THR A O   
711  C CB  . THR A 96  ? 0.2967 0.2894 0.2306 -0.0257 0.0285  -0.0646 89  THR A CB  
712  O OG1 . THR A 96  ? 0.3217 0.3098 0.2484 -0.0276 0.0352  -0.0520 89  THR A OG1 
713  C CG2 . THR A 96  ? 0.3062 0.2803 0.2402 -0.0248 0.0230  -0.0642 89  THR A CG2 
714  N N   . LYS A 97  ? 0.2520 0.3003 0.1906 -0.0149 0.0296  -0.0778 90  LYS A N   
715  C CA  . LYS A 97  ? 0.2387 0.3143 0.1805 -0.0085 0.0322  -0.0821 90  LYS A CA  
716  C C   . LYS A 97  ? 0.2782 0.3639 0.2213 -0.0148 0.0422  -0.0786 90  LYS A C   
717  O O   . LYS A 97  ? 0.2487 0.3517 0.1858 -0.0048 0.0444  -0.0808 90  LYS A O   
718  C CB  . LYS A 97  ? 0.2076 0.3165 0.1670 -0.0102 0.0306  -0.0927 90  LYS A CB  
719  C CG  . LYS A 97  ? 0.2123 0.3563 0.1773 -0.0004 0.0318  -0.0975 90  LYS A CG  
720  C CD  . LYS A 97  ? 0.2182 0.4028 0.1988 0.0009  0.0274  -0.1085 90  LYS A CD  
721  C CE  . LYS A 97  ? 0.2461 0.4732 0.2373 0.0086  0.0294  -0.1147 90  LYS A CE  
722  N NZ  . LYS A 97  ? 0.2325 0.4561 0.2124 0.0315  0.0260  -0.1058 90  LYS A NZ  
723  N N   . PHE A 98  ? 0.2643 0.3425 0.2186 -0.0302 0.0489  -0.0722 91  PHE A N   
724  C CA  . PHE A 98  ? 0.3007 0.3972 0.2645 -0.0400 0.0611  -0.0631 91  PHE A CA  
725  C C   . PHE A 98  ? 0.3866 0.4704 0.3318 -0.0379 0.0660  -0.0447 91  PHE A C   
726  O O   . PHE A 98  ? 0.3571 0.4582 0.3092 -0.0461 0.0778  -0.0294 91  PHE A O   
727  C CB  . PHE A 98  ? 0.3075 0.4065 0.3061 -0.0602 0.0666  -0.0648 91  PHE A CB  
728  C CG  . PHE A 98  ? 0.2363 0.3528 0.2528 -0.0615 0.0591  -0.0873 91  PHE A CG  
729  C CD1 . PHE A 98  ? 0.2274 0.3842 0.2459 -0.0537 0.0578  -0.0984 91  PHE A CD1 
730  C CD2 . PHE A 98  ? 0.2454 0.3454 0.2770 -0.0676 0.0530  -0.0988 91  PHE A CD2 
731  C CE1 . PHE A 98  ? 0.2174 0.3999 0.2503 -0.0523 0.0501  -0.1177 91  PHE A CE1 
732  C CE2 . PHE A 98  ? 0.2795 0.4074 0.3249 -0.0663 0.0454  -0.1217 91  PHE A CE2 
733  C CZ  . PHE A 98  ? 0.2390 0.4101 0.2842 -0.0588 0.0439  -0.1299 91  PHE A CZ  
734  N N   . ALA A 99  ? 0.4239 0.4846 0.3472 -0.0270 0.0576  -0.0446 92  ALA A N   
735  C CA  . ALA A 99  ? 0.4845 0.5430 0.3880 -0.0221 0.0602  -0.0301 92  ALA A CA  
736  C C   . ALA A 99  ? 0.4506 0.5490 0.3423 -0.0142 0.0676  -0.0295 92  ALA A C   
737  O O   . ALA A 99  ? 0.4415 0.5552 0.3272 -0.0020 0.0632  -0.0479 92  ALA A O   
738  C CB  . ALA A 99  ? 0.4725 0.5084 0.3581 -0.0110 0.0479  -0.0375 92  ALA A CB  
739  N N   . GLY A 100 ? 0.5354 0.6535 0.4254 -0.0197 0.0794  -0.0067 93  GLY A N   
740  C CA  . GLY A 100 ? 0.5028 0.6707 0.3794 -0.0111 0.0881  -0.0042 93  GLY A CA  
741  C C   . GLY A 100 ? 0.4743 0.6770 0.3714 -0.0186 0.0987  -0.0065 93  GLY A C   
742  O O   . GLY A 100 ? 0.4622 0.7150 0.3505 -0.0116 0.1080  -0.0036 93  GLY A O   
743  N N   . TYR A 101 ? 0.3674 0.5532 0.2921 -0.0316 0.0972  -0.0140 94  TYR A N   
744  C CA  . TYR A 101 ? 0.3476 0.5710 0.2977 -0.0417 0.1072  -0.0159 94  TYR A CA  
745  C C   . TYR A 101 ? 0.3796 0.6262 0.3470 -0.0592 0.1251  0.0157  94  TYR A C   
746  O O   . TYR A 101 ? 0.4283 0.6438 0.4051 -0.0710 0.1284  0.0389  94  TYR A O   
747  C CB  . TYR A 101 ? 0.2829 0.4879 0.2620 -0.0536 0.1010  -0.0307 94  TYR A CB  
748  C CG  . TYR A 101 ? 0.2950 0.5024 0.2673 -0.0375 0.0882  -0.0568 94  TYR A CG  
749  C CD1 . TYR A 101 ? 0.3554 0.5510 0.3001 -0.0157 0.0786  -0.0662 94  TYR A CD1 
750  C CD2 . TYR A 101 ? 0.2933 0.5173 0.2911 -0.0440 0.0855  -0.0713 94  TYR A CD2 
751  C CE1 . TYR A 101 ? 0.3367 0.5309 0.2818 -0.0011 0.0678  -0.0836 94  TYR A CE1 
752  C CE2 . TYR A 101 ? 0.3458 0.5767 0.3384 -0.0274 0.0743  -0.0885 94  TYR A CE2 
753  C CZ  . TYR A 101 ? 0.3155 0.5288 0.2827 -0.0059 0.0662  -0.0916 94  TYR A CZ  
754  O OH  . TYR A 101 ? 0.4136 0.6323 0.3820 0.0105  0.0563  -0.1025 94  TYR A OH  
755  N N   . GLY A 102 ? 0.3283 0.6308 0.3045 -0.0609 0.1373  0.0183  95  GLY A N   
756  C CA  . GLY A 102 ? 0.3500 0.6794 0.3559 -0.0829 0.1562  0.0495  95  GLY A CA  
757  C C   . GLY A 102 ? 0.3413 0.6964 0.3894 -0.1003 0.1610  0.0362  95  GLY A C   
758  O O   . GLY A 102 ? 0.3185 0.6632 0.3726 -0.0956 0.1480  0.0045  95  GLY A O   
759  N N   . GLU A 103 ? 0.4450 0.4474 0.2332 0.0006  0.1246  -0.0184 96  GLU A N   
760  C CA  . GLU A 103 ? 0.4054 0.4404 0.2349 -0.0042 0.1394  -0.0147 96  GLU A CA  
761  C C   . GLU A 103 ? 0.3886 0.4421 0.2385 0.0116  0.1448  -0.0301 96  GLU A C   
762  O O   . GLU A 103 ? 0.4017 0.4749 0.2909 0.0124  0.1418  -0.0319 96  GLU A O   
763  C CB  . GLU A 103 ? 0.5216 0.5752 0.3509 -0.0113 0.1566  -0.0019 96  GLU A CB  
764  C CG  . GLU A 103 ? 0.6341 0.7163 0.5106 -0.0248 0.1670  0.0055  96  GLU A CG  
765  C CD  . GLU A 103 ? 0.7899 0.8977 0.6752 -0.0296 0.1881  0.0152  96  GLU A CD  
766  O OE1 . GLU A 103 ? 0.8685 0.9692 0.7165 -0.0241 0.1949  0.0190  96  GLU A OE1 
767  O OE2 . GLU A 103 ? 0.8129 0.9504 0.7436 -0.0399 0.1973  0.0179  96  GLU A OE2 
768  N N   . ALA A 104 ? 0.3916 0.4403 0.2183 0.0256  0.1470  -0.0416 97  ALA A N   
769  C CA  . ALA A 104 ? 0.4209 0.4842 0.2666 0.0421  0.1524  -0.0567 97  ALA A CA  
770  C C   . ALA A 104 ? 0.4244 0.4696 0.2834 0.0511  0.1385  -0.0618 97  ALA A C   
771  O O   . ALA A 104 ? 0.3948 0.4623 0.2881 0.0608  0.1397  -0.0643 97  ALA A O   
772  C CB  . ALA A 104 ? 0.5036 0.5526 0.3175 0.0527  0.1549  -0.0706 97  ALA A CB  
773  N N   . ALA A 105 ? 0.4078 0.4165 0.2458 0.0460  0.1205  -0.0623 98  ALA A N   
774  C CA  . ALA A 105 ? 0.3991 0.3894 0.2528 0.0498  0.1045  -0.0646 98  ALA A CA  
775  C C   . ALA A 105 ? 0.3733 0.3833 0.2618 0.0420  0.0987  -0.0528 98  ALA A C   
776  O O   . ALA A 105 ? 0.3592 0.3717 0.2673 0.0523  0.0937  -0.0538 98  ALA A O   
777  C CB  . ALA A 105 ? 0.4319 0.3855 0.2619 0.0419  0.0885  -0.0677 98  ALA A CB  
778  N N   . PHE A 106 ? 0.3196 0.3397 0.2121 0.0255  0.0983  -0.0417 99  PHE A N   
779  C CA  . PHE A 106 ? 0.3347 0.3706 0.2570 0.0183  0.0917  -0.0338 99  PHE A CA  
780  C C   . PHE A 106 ? 0.2988 0.3737 0.2538 0.0248  0.1006  -0.0367 99  PHE A C   
781  O O   . PHE A 106 ? 0.2834 0.3700 0.2616 0.0306  0.0913  -0.0373 99  PHE A O   
782  C CB  . PHE A 106 ? 0.2909 0.3233 0.2085 0.0002  0.0897  -0.0229 99  PHE A CB  
783  C CG  . PHE A 106 ? 0.3071 0.3120 0.2116 -0.0047 0.0744  -0.0193 99  PHE A CG  
784  C CD1 . PHE A 106 ? 0.2745 0.2739 0.1933 -0.0021 0.0637  -0.0190 99  PHE A CD1 
785  C CD2 . PHE A 106 ? 0.3110 0.2987 0.1893 -0.0106 0.0715  -0.0158 99  PHE A CD2 
786  C CE1 . PHE A 106 ? 0.2853 0.2661 0.1976 -0.0069 0.0531  -0.0157 99  PHE A CE1 
787  C CE2 . PHE A 106 ? 0.3109 0.2814 0.1849 -0.0139 0.0571  -0.0136 99  PHE A CE2 
788  C CZ  . PHE A 106 ? 0.2533 0.2225 0.1471 -0.0129 0.0495  -0.0138 99  PHE A CZ  
789  N N   . LYS A 107 ? 0.3295 0.4279 0.2871 0.0244  0.1186  -0.0386 100 LYS A N   
790  C CA  . LYS A 107 ? 0.3498 0.4940 0.3468 0.0303  0.1280  -0.0431 100 LYS A CA  
791  C C   . LYS A 107 ? 0.3997 0.5471 0.4059 0.0559  0.1217  -0.0534 100 LYS A C   
792  O O   . LYS A 107 ? 0.4453 0.6210 0.4851 0.0637  0.1140  -0.0558 100 LYS A O   
793  C CB  . LYS A 107 ? 0.3638 0.5327 0.3604 0.0258  0.1532  -0.0429 100 LYS A CB  
794  C CG  . LYS A 107 ? 0.4817 0.6961 0.5236 0.0103  0.1638  -0.0385 100 LYS A CG  
795  C CD  . LYS A 107 ? 0.5730 0.7861 0.6010 -0.0003 0.1845  -0.0267 100 LYS A CD  
796  C CE  . LYS A 107 ? 0.8335 1.0843 0.9088 -0.0186 0.1937  -0.0197 100 LYS A CE  
797  N NZ  . LYS A 107 ? 0.9070 1.1999 1.0173 -0.0065 0.2087  -0.0250 100 LYS A NZ  
798  N N   . ALA A 108 ? 0.3649 0.4793 0.3393 0.0700  0.1223  -0.0599 101 ALA A N   
799  C CA  . ALA A 108 ? 0.4248 0.5307 0.4024 0.0957  0.1167  -0.0684 101 ALA A CA  
800  C C   . ALA A 108 ? 0.4203 0.5097 0.4044 0.0982  0.0973  -0.0620 101 ALA A C   
801  O O   . ALA A 108 ? 0.4180 0.5169 0.4172 0.1191  0.0912  -0.0647 101 ALA A O   
802  C CB  . ALA A 108 ? 0.4728 0.5359 0.4116 0.1062  0.1197  -0.0776 101 ALA A CB  
803  N N   . GLY A 109 ? 0.3216 0.3868 0.2922 0.0797  0.0878  -0.0531 102 GLY A N   
804  C CA  . GLY A 109 ? 0.3457 0.3937 0.3168 0.0823  0.0729  -0.0463 102 GLY A CA  
805  C C   . GLY A 109 ? 0.3410 0.4263 0.3415 0.0834  0.0651  -0.0440 102 GLY A C   
806  O O   . GLY A 109 ? 0.2788 0.3595 0.2803 0.0981  0.0540  -0.0416 102 GLY A O   
807  N N   . GLY A 110 ? 0.2748 0.3946 0.2973 0.0676  0.0703  -0.0447 103 GLY A N   
808  C CA  . GLY A 110 ? 0.2356 0.3951 0.2918 0.0662  0.0620  -0.0468 103 GLY A CA  
809  C C   . GLY A 110 ? 0.1971 0.3450 0.2491 0.0543  0.0478  -0.0417 103 GLY A C   
810  O O   . GLY A 110 ? 0.1978 0.3742 0.2734 0.0556  0.0364  -0.0461 103 GLY A O   
811  N N   . TYR A 111 ? 0.1953 0.3046 0.2192 0.0441  0.0472  -0.0343 104 TYR A N   
812  C CA  . TYR A 111 ? 0.1870 0.2827 0.2035 0.0357  0.0361  -0.0300 104 TYR A CA  
813  C C   . TYR A 111 ? 0.2307 0.3175 0.2442 0.0133  0.0411  -0.0262 104 TYR A C   
814  O O   . TYR A 111 ? 0.2295 0.3168 0.2407 0.0050  0.0530  -0.0249 104 TYR A O   
815  C CB  . TYR A 111 ? 0.2371 0.2966 0.2257 0.0464  0.0317  -0.0236 104 TYR A CB  
816  C CG  . TYR A 111 ? 0.2421 0.2727 0.2123 0.0449  0.0407  -0.0209 104 TYR A CG  
817  C CD1 . TYR A 111 ? 0.2972 0.3129 0.2581 0.0287  0.0438  -0.0180 104 TYR A CD1 
818  C CD2 . TYR A 111 ? 0.2487 0.2660 0.2109 0.0610  0.0442  -0.0229 104 TYR A CD2 
819  C CE1 . TYR A 111 ? 0.3433 0.3360 0.2889 0.0268  0.0483  -0.0187 104 TYR A CE1 
820  C CE2 . TYR A 111 ? 0.2906 0.2795 0.2363 0.0580  0.0504  -0.0241 104 TYR A CE2 
821  C CZ  . TYR A 111 ? 0.3365 0.3152 0.2747 0.0401  0.0515  -0.0227 104 TYR A CZ  
822  O OH  . TYR A 111 ? 0.3912 0.3448 0.3142 0.0366  0.0540  -0.0268 104 TYR A OH  
823  N N   . ARG A 112 ? 0.1809 0.2584 0.1915 0.0058  0.0320  -0.0246 105 ARG A N   
824  C CA  . ARG A 112 ? 0.1879 0.2508 0.1934 -0.0117 0.0343  -0.0204 105 ARG A CA  
825  C C   . ARG A 112 ? 0.2132 0.2465 0.1963 -0.0090 0.0300  -0.0151 105 ARG A C   
826  O O   . ARG A 112 ? 0.2158 0.2439 0.1921 0.0017  0.0236  -0.0156 105 ARG A O   
827  C CB  . ARG A 112 ? 0.1896 0.2665 0.2153 -0.0234 0.0278  -0.0257 105 ARG A CB  
828  C CG  . ARG A 112 ? 0.2519 0.3604 0.3076 -0.0343 0.0358  -0.0296 105 ARG A CG  
829  C CD  . ARG A 112 ? 0.2138 0.3394 0.2964 -0.0465 0.0258  -0.0387 105 ARG A CD  
830  N NE  . ARG A 112 ? 0.2419 0.3357 0.3120 -0.0599 0.0225  -0.0358 105 ARG A NE  
831  C CZ  . ARG A 112 ? 0.2964 0.3874 0.3750 -0.0655 0.0088  -0.0456 105 ARG A CZ  
832  N NH1 . ARG A 112 ? 0.3139 0.4349 0.4134 -0.0599 -0.0051 -0.0593 105 ARG A NH1 
833  N NH2 . ARG A 112 ? 0.3246 0.3810 0.3890 -0.0751 0.0073  -0.0430 105 ARG A NH2 
834  N N   . VAL A 113 ? 0.2061 0.2224 0.1780 -0.0178 0.0339  -0.0097 106 VAL A N   
835  C CA  . VAL A 113 ? 0.1854 0.1807 0.1436 -0.0161 0.0303  -0.0055 106 VAL A CA  
836  C C   . VAL A 113 ? 0.1972 0.1819 0.1537 -0.0253 0.0277  -0.0026 106 VAL A C   
837  O O   . VAL A 113 ? 0.2123 0.1900 0.1619 -0.0325 0.0315  0.0022  106 VAL A O   
838  C CB  . VAL A 113 ? 0.2275 0.2123 0.1742 -0.0144 0.0337  -0.0034 106 VAL A CB  
839  C CG1 . VAL A 113 ? 0.2244 0.1962 0.1668 -0.0138 0.0295  -0.0006 106 VAL A CG1 
840  C CG2 . VAL A 113 ? 0.2294 0.2177 0.1762 -0.0050 0.0372  -0.0069 106 VAL A CG2 
841  N N   . VAL A 114 ? 0.2042 0.1845 0.1632 -0.0236 0.0213  -0.0056 107 VAL A N   
842  C CA  . VAL A 114 ? 0.2056 0.1703 0.1630 -0.0302 0.0180  -0.0047 107 VAL A CA  
843  C C   . VAL A 114 ? 0.2372 0.1871 0.1841 -0.0241 0.0162  0.0003  107 VAL A C   
844  O O   . VAL A 114 ? 0.2311 0.1846 0.1777 -0.0150 0.0155  -0.0012 107 VAL A O   
845  C CB  . VAL A 114 ? 0.1993 0.1645 0.1625 -0.0290 0.0106  -0.0141 107 VAL A CB  
846  C CG1 . VAL A 114 ? 0.2309 0.1722 0.1909 -0.0346 0.0067  -0.0151 107 VAL A CG1 
847  C CG2 . VAL A 114 ? 0.2135 0.2016 0.1934 -0.0342 0.0093  -0.0210 107 VAL A CG2 
848  N N   . PRO A 115 ? 0.2293 0.1638 0.1683 -0.0278 0.0154  0.0068  108 PRO A N   
849  C CA  . PRO A 115 ? 0.2647 0.1922 0.1986 -0.0193 0.0107  0.0101  108 PRO A CA  
850  C C   . PRO A 115 ? 0.2604 0.1824 0.1987 -0.0105 0.0071  0.0054  108 PRO A C   
851  O O   . PRO A 115 ? 0.2536 0.1615 0.1901 -0.0124 0.0051  0.0016  108 PRO A O   
852  C CB  . PRO A 115 ? 0.3214 0.2309 0.2408 -0.0227 0.0089  0.0189  108 PRO A CB  
853  C CG  . PRO A 115 ? 0.3593 0.2609 0.2773 -0.0350 0.0153  0.0211  108 PRO A CG  
854  C CD  . PRO A 115 ? 0.2978 0.2224 0.2316 -0.0392 0.0198  0.0128  108 PRO A CD  
855  N N   . PRO A 116 ? 0.2461 0.1779 0.1907 -0.0010 0.0068  0.0045  109 PRO A N   
856  C CA  . PRO A 116 ? 0.2393 0.1855 0.1910 -0.0006 0.0071  0.0070  109 PRO A CA  
857  C C   . PRO A 116 ? 0.2397 0.1996 0.1985 -0.0017 0.0145  0.0049  109 PRO A C   
858  O O   . PRO A 116 ? 0.2449 0.2158 0.2161 0.0000  0.0167  0.0051  109 PRO A O   
859  C CB  . PRO A 116 ? 0.2653 0.2150 0.2266 0.0099  0.0023  0.0070  109 PRO A CB  
860  C CG  . PRO A 116 ? 0.2736 0.2178 0.2344 0.0179  0.0063  0.0020  109 PRO A CG  
861  C CD  . PRO A 116 ? 0.2818 0.2077 0.2286 0.0103  0.0052  0.0004  109 PRO A CD  
862  N N   . ALA A 117 ? 0.2240 0.1835 0.1768 -0.0045 0.0182  0.0035  110 ALA A N   
863  C CA  . ALA A 117 ? 0.2146 0.1800 0.1686 -0.0030 0.0247  0.0039  110 ALA A CA  
864  C C   . ALA A 117 ? 0.2261 0.1925 0.1851 -0.0085 0.0257  0.0051  110 ALA A C   
865  O O   . ALA A 117 ? 0.2421 0.2062 0.1968 -0.0132 0.0212  0.0040  110 ALA A O   
866  C CB  . ALA A 117 ? 0.2292 0.1956 0.1763 -0.0020 0.0250  0.0015  110 ALA A CB  
867  N N   . VAL A 118 ? 0.2187 0.1862 0.1844 -0.0082 0.0324  0.0070  111 VAL A N   
868  C CA  . VAL A 118 ? 0.2047 0.1687 0.1770 -0.0153 0.0332  0.0058  111 VAL A CA  
869  C C   . VAL A 118 ? 0.2078 0.1605 0.1751 -0.0135 0.0429  0.0097  111 VAL A C   
870  O O   . VAL A 118 ? 0.2217 0.1738 0.1851 -0.0076 0.0507  0.0154  111 VAL A O   
871  C CB  . VAL A 118 ? 0.2164 0.1920 0.2101 -0.0207 0.0309  0.0045  111 VAL A CB  
872  C CG1 . VAL A 118 ? 0.2760 0.2467 0.2798 -0.0310 0.0306  0.0006  111 VAL A CG1 
873  C CG2 . VAL A 118 ? 0.2622 0.2454 0.2562 -0.0183 0.0186  0.0019  111 VAL A CG2 
874  N N   . ALA A 119 ? 0.2159 0.1560 0.1793 -0.0169 0.0426  0.0067  112 ALA A N   
875  C CA  . ALA A 119 ? 0.2401 0.1612 0.1984 -0.0153 0.0514  0.0111  112 ALA A CA  
876  C C   . ALA A 119 ? 0.2541 0.1632 0.2234 -0.0274 0.0505  0.0055  112 ALA A C   
877  O O   . ALA A 119 ? 0.2464 0.1605 0.2174 -0.0323 0.0405  -0.0042 112 ALA A O   
878  C CB  . ALA A 119 ? 0.2564 0.1683 0.1975 -0.0036 0.0509  0.0105  112 ALA A CB  
879  N N   . ARG A 120 ? 0.2255 0.1629 0.1274 0.0030  -0.0147 -0.0273 113 ARG A N   
880  C CA  . ARG A 120 ? 0.2517 0.1793 0.1506 0.0002  -0.0244 -0.0391 113 ARG A CA  
881  C C   . ARG A 120 ? 0.2854 0.1993 0.1721 0.0048  -0.0183 -0.0497 113 ARG A C   
882  O O   . ARG A 120 ? 0.2660 0.1780 0.1593 0.0091  -0.0076 -0.0452 113 ARG A O   
883  C CB  . ARG A 120 ? 0.2795 0.2061 0.2071 -0.0073 -0.0291 -0.0384 113 ARG A CB  
884  C CG  . ARG A 120 ? 0.2680 0.2070 0.2100 -0.0122 -0.0398 -0.0356 113 ARG A CG  
885  C CD  . ARG A 120 ? 0.2220 0.1645 0.1972 -0.0197 -0.0385 -0.0317 113 ARG A CD  
886  N NE  . ARG A 120 ? 0.2223 0.1763 0.2187 -0.0251 -0.0511 -0.0330 113 ARG A NE  
887  C CZ  . ARG A 120 ? 0.2434 0.2046 0.2738 -0.0325 -0.0496 -0.0295 113 ARG A CZ  
888  N NH1 . ARG A 120 ? 0.2424 0.1998 0.2837 -0.0353 -0.0355 -0.0227 113 ARG A NH1 
889  N NH2 . ARG A 120 ? 0.2194 0.1938 0.2743 -0.0372 -0.0626 -0.0314 113 ARG A NH2 
890  N N   . ARG A 121 ? 0.2905 0.1959 0.1608 0.0040  -0.0259 -0.0648 114 ARG A N   
891  C CA  A ARG A 121 ? 0.3241 0.2131 0.1877 0.0081  -0.0197 -0.0799 114 ARG A CA  
892  C CA  B ARG A 121 ? 0.3242 0.2132 0.1877 0.0082  -0.0195 -0.0798 114 ARG A CA  
893  C C   . ARG A 121 ? 0.3609 0.2379 0.2571 0.0061  -0.0166 -0.0775 114 ARG A C   
894  O O   . ARG A 121 ? 0.3769 0.2538 0.2950 -0.0021 -0.0242 -0.0733 114 ARG A O   
895  C CB  A ARG A 121 ? 0.3615 0.2429 0.2032 0.0046  -0.0313 -0.1004 114 ARG A CB  
896  C CB  B ARG A 121 ? 0.3619 0.2429 0.2029 0.0051  -0.0305 -0.1007 114 ARG A CB  
897  C CG  A ARG A 121 ? 0.4281 0.2875 0.2727 0.0058  -0.0276 -0.1220 114 ARG A CG  
898  C CG  B ARG A 121 ? 0.4317 0.2910 0.2722 0.0080  -0.0242 -0.1222 114 ARG A CG  
899  C CD  A ARG A 121 ? 0.4982 0.3548 0.3203 -0.0005 -0.0407 -0.1440 114 ARG A CD  
900  C CD  B ARG A 121 ? 0.4976 0.3550 0.3105 0.0036  -0.0331 -0.1445 114 ARG A CD  
901  N NE  A ARG A 121 ? 0.5816 0.4176 0.4229 -0.0050 -0.0388 -0.1627 114 ARG A NE  
902  N NE  B ARG A 121 ? 0.5791 0.4163 0.4057 0.0008  -0.0287 -0.1650 114 ARG A NE  
903  C CZ  A ARG A 121 ? 0.5251 0.3460 0.3653 0.0018  -0.0222 -0.1737 114 ARG A CZ  
904  C CZ  B ARG A 121 ? 0.5821 0.4063 0.4340 -0.0093 -0.0399 -0.1733 114 ARG A CZ  
905  N NH1 A ARG A 121 ? 0.4934 0.3220 0.3195 0.0132  -0.0058 -0.1685 114 ARG A NH1 
906  N NH1 B ARG A 121 ? 0.4903 0.3228 0.3626 -0.0176 -0.0557 -0.1635 114 ARG A NH1 
907  N NH2 A ARG A 121 ? 0.5505 0.3473 0.4070 -0.0027 -0.0216 -0.1887 114 ARG A NH2 
908  N NH2 B ARG A 121 ? 0.5960 0.3973 0.4550 -0.0114 -0.0341 -0.1905 114 ARG A NH2 
909  N N   . GLY A 122 ? 0.3094 0.1774 0.2115 0.0140  -0.0046 -0.0782 115 GLY A N   
910  C CA  . GLY A 122 ? 0.3042 0.1610 0.2373 0.0138  -0.0016 -0.0705 115 GLY A CA  
911  C C   . GLY A 122 ? 0.2860 0.1576 0.2303 0.0166  0.0044  -0.0484 115 GLY A C   
912  O O   . GLY A 122 ? 0.2947 0.1603 0.2616 0.0165  0.0062  -0.0367 115 GLY A O   
913  N N   . ALA A 123 ? 0.2705 0.1609 0.1995 0.0181  0.0067  -0.0418 116 ALA A N   
914  C CA  . ALA A 123 ? 0.2866 0.1924 0.2227 0.0209  0.0120  -0.0260 116 ALA A CA  
915  C C   . ALA A 123 ? 0.2744 0.1845 0.2070 0.0307  0.0209  -0.0285 116 ALA A C   
916  O O   . ALA A 123 ? 0.3163 0.2263 0.2308 0.0332  0.0248  -0.0389 116 ALA A O   
917  C CB  . ALA A 123 ? 0.2599 0.1827 0.1877 0.0154  0.0098  -0.0195 116 ALA A CB  
918  N N   . PHE A 124 ? 0.2597 0.1755 0.2102 0.0361  0.0242  -0.0176 117 PHE A N   
919  C CA  . PHE A 124 ? 0.2534 0.1790 0.2096 0.0454  0.0328  -0.0179 117 PHE A CA  
920  C C   . PHE A 124 ? 0.2355 0.1850 0.1896 0.0421  0.0329  -0.0087 117 PHE A C   
921  O O   . PHE A 124 ? 0.2542 0.2141 0.2135 0.0370  0.0265  0.0024  117 PHE A O   
922  C CB  . PHE A 124 ? 0.2465 0.1677 0.2301 0.0545  0.0346  -0.0105 117 PHE A CB  
923  C CG  . PHE A 124 ? 0.2479 0.1848 0.2461 0.0643  0.0429  -0.0089 117 PHE A CG  
924  C CD1 . PHE A 124 ? 0.2734 0.2064 0.2658 0.0709  0.0555  -0.0243 117 PHE A CD1 
925  C CD2 . PHE A 124 ? 0.2911 0.2490 0.3085 0.0665  0.0383  0.0076  117 PHE A CD2 
926  C CE1 . PHE A 124 ? 0.3006 0.2510 0.3116 0.0798  0.0658  -0.0224 117 PHE A CE1 
927  C CE2 . PHE A 124 ? 0.2685 0.2444 0.3065 0.0750  0.0450  0.0092  117 PHE A CE2 
928  C CZ  . PHE A 124 ? 0.2792 0.2514 0.3165 0.0817  0.0598  -0.0053 117 PHE A CZ  
929  N N   . ILE A 125 ? 0.2503 0.2083 0.1969 0.0443  0.0412  -0.0138 118 ILE A N   
930  C CA  . ILE A 125 ? 0.2228 0.2017 0.1738 0.0406  0.0429  -0.0068 118 ILE A CA  
931  C C   . ILE A 125 ? 0.2100 0.2014 0.1796 0.0490  0.0534  -0.0065 118 ILE A C   
932  O O   . ILE A 125 ? 0.2438 0.2301 0.2058 0.0547  0.0654  -0.0150 118 ILE A O   
933  C CB  . ILE A 125 ? 0.2580 0.2364 0.1888 0.0341  0.0446  -0.0094 118 ILE A CB  
934  C CG1 . ILE A 125 ? 0.2707 0.2380 0.1884 0.0277  0.0351  -0.0109 118 ILE A CG1 
935  C CG2 . ILE A 125 ? 0.2565 0.2530 0.1984 0.0288  0.0464  -0.0028 118 ILE A CG2 
936  C CD1 . ILE A 125 ? 0.3366 0.3101 0.2638 0.0217  0.0279  -0.0046 118 ILE A CD1 
937  N N   . ALA A 126 ? 0.2193 0.2292 0.2135 0.0500  0.0490  0.0030  119 ALA A N   
938  C CA  . ALA A 126 ? 0.1988 0.2252 0.2205 0.0583  0.0573  0.0050  119 ALA A CA  
939  C C   . ALA A 126 ? 0.1937 0.2369 0.2188 0.0533  0.0672  0.0043  119 ALA A C   
940  O O   . ALA A 126 ? 0.2138 0.2553 0.2219 0.0434  0.0657  0.0042  119 ALA A O   
941  C CB  . ALA A 126 ? 0.2135 0.2578 0.2627 0.0605  0.0452  0.0175  119 ALA A CB  
942  N N   . ARG A 127 ? 0.2137 0.2734 0.2668 0.0609  0.0783  0.0052  120 ARG A N   
943  C CA  . ARG A 127 ? 0.2100 0.2892 0.2763 0.0556  0.0892  0.0073  120 ARG A CA  
944  C C   . ARG A 127 ? 0.2173 0.3133 0.2965 0.0431  0.0753  0.0135  120 ARG A C   
945  O O   . ARG A 127 ? 0.1792 0.2831 0.2679 0.0420  0.0586  0.0176  120 ARG A O   
946  C CB  . ARG A 127 ? 0.2037 0.3030 0.3079 0.0661  0.1031  0.0082  120 ARG A CB  
947  C CG  . ARG A 127 ? 0.3489 0.4327 0.4439 0.0795  0.1201  -0.0021 120 ARG A CG  
948  C CD  . ARG A 127 ? 0.3227 0.4300 0.4571 0.0892  0.1405  -0.0024 120 ARG A CD  
949  N NE  . ARG A 127 ? 0.3395 0.4608 0.4708 0.0783  0.1519  0.0009  120 ARG A NE  
950  C CZ  . ARG A 127 ? 0.4281 0.5367 0.5220 0.0740  0.1638  -0.0049 120 ARG A CZ  
951  N NH1 . ARG A 127 ? 0.4869 0.5719 0.5435 0.0793  0.1665  -0.0173 120 ARG A NH1 
952  N NH2 . ARG A 127 ? 0.4414 0.5627 0.5374 0.0636  0.1719  0.0023  120 ARG A NH2 
953  N N   . ASN A 128 ? 0.1945 0.2957 0.2737 0.0333  0.0829  0.0142  121 ASN A N   
954  C CA  . ASN A 128 ? 0.1781 0.2944 0.2748 0.0200  0.0736  0.0161  121 ASN A CA  
955  C C   . ASN A 128 ? 0.2089 0.3124 0.2821 0.0125  0.0575  0.0127  121 ASN A C   
956  O O   . ASN A 128 ? 0.2403 0.3557 0.3255 0.0020  0.0473  0.0103  121 ASN A O   
957  C CB  . ASN A 128 ? 0.1838 0.3319 0.3244 0.0204  0.0665  0.0193  121 ASN A CB  
958  C CG  . ASN A 128 ? 0.2266 0.3912 0.3984 0.0274  0.0856  0.0224  121 ASN A CG  
959  O OD1 . ASN A 128 ? 0.2390 0.3994 0.4067 0.0241  0.1043  0.0233  121 ASN A OD1 
960  N ND2 . ASN A 128 ? 0.3154 0.4991 0.5189 0.0381  0.0823  0.0255  121 ASN A ND2 
961  N N   . VAL A 129 ? 0.1942 0.2749 0.2360 0.0168  0.0560  0.0108  122 VAL A N   
962  C CA  . VAL A 129 ? 0.1782 0.2460 0.1988 0.0097  0.0461  0.0076  122 VAL A CA  
963  C C   . VAL A 129 ? 0.1876 0.2452 0.2013 0.0024  0.0533  0.0067  122 VAL A C   
964  O O   . VAL A 129 ? 0.2080 0.2591 0.2161 0.0052  0.0658  0.0105  122 VAL A O   
965  C CB  . VAL A 129 ? 0.1959 0.2449 0.1928 0.0166  0.0424  0.0070  122 VAL A CB  
966  C CG1 . VAL A 129 ? 0.2227 0.2594 0.2010 0.0098  0.0362  0.0040  122 VAL A CG1 
967  C CG2 . VAL A 129 ? 0.2086 0.2655 0.2160 0.0228  0.0340  0.0114  122 VAL A CG2 
968  N N   . VAL A 130 ? 0.1957 0.2512 0.2091 -0.0066 0.0461  0.0022  123 VAL A N   
969  C CA  . VAL A 130 ? 0.1895 0.2308 0.1989 -0.0120 0.0513  0.0023  123 VAL A CA  
970  C C   . VAL A 130 ? 0.1734 0.2008 0.1634 -0.0116 0.0443  -0.0018 123 VAL A C   
971  O O   . VAL A 130 ? 0.1951 0.2281 0.1848 -0.0156 0.0363  -0.0089 123 VAL A O   
972  C CB  . VAL A 130 ? 0.2059 0.2554 0.2418 -0.0234 0.0521  -0.0018 123 VAL A CB  
973  C CG1 . VAL A 130 ? 0.2309 0.2613 0.2667 -0.0273 0.0582  0.0006  123 VAL A CG1 
974  C CG2 . VAL A 130 ? 0.1905 0.2576 0.2525 -0.0250 0.0594  0.0030  123 VAL A CG2 
975  N N   . LEU A 131 ? 0.2043 0.2161 0.1783 -0.0071 0.0473  0.0028  124 LEU A N   
976  C CA  . LEU A 131 ? 0.2080 0.2086 0.1718 -0.0071 0.0417  0.0000  124 LEU A CA  
977  C C   . LEU A 131 ? 0.2043 0.1961 0.1797 -0.0112 0.0454  0.0019  124 LEU A C   
978  O O   . LEU A 131 ? 0.1928 0.1761 0.1638 -0.0084 0.0496  0.0119  124 LEU A O   
979  C CB  . LEU A 131 ? 0.2085 0.1994 0.1520 0.0000  0.0393  0.0033  124 LEU A CB  
980  C CG  . LEU A 131 ? 0.2231 0.2166 0.1589 0.0051  0.0370  0.0012  124 LEU A CG  
981  C CD1 . LEU A 131 ? 0.2854 0.2667 0.2030 0.0099  0.0343  0.0007  124 LEU A CD1 
982  C CD2 . LEU A 131 ? 0.2277 0.2276 0.1688 0.0026  0.0308  -0.0019 124 LEU A CD2 
983  N N   . MET A 132 ? 0.1869 0.1806 0.1773 -0.0179 0.0444  -0.0076 125 MET A N   
984  C CA  . MET A 132 ? 0.1924 0.1735 0.1977 -0.0202 0.0477  -0.0082 125 MET A CA  
985  C C   . MET A 132 ? 0.1852 0.1586 0.1804 -0.0138 0.0436  -0.0051 125 MET A C   
986  O O   . MET A 132 ? 0.2147 0.1921 0.1925 -0.0101 0.0386  -0.0047 125 MET A O   
987  C CB  . MET A 132 ? 0.2024 0.1872 0.2243 -0.0287 0.0482  -0.0247 125 MET A CB  
988  C CG  . MET A 132 ? 0.2085 0.2037 0.2456 -0.0369 0.0494  -0.0288 125 MET A CG  
989  S SD  . MET A 132 ? 0.2565 0.2390 0.3190 -0.0396 0.0597  -0.0151 125 MET A SD  
990  C CE  . MET A 132 ? 0.2770 0.2392 0.3627 -0.0431 0.0629  -0.0261 125 MET A CE  
991  N N   . PRO A 133 ? 0.1932 0.1553 0.2034 -0.0122 0.0452  -0.0021 126 PRO A N   
992  C CA  . PRO A 133 ? 0.2073 0.1667 0.2146 -0.0063 0.0397  0.0005  126 PRO A CA  
993  C C   . PRO A 133 ? 0.1693 0.1382 0.1692 -0.0080 0.0379  -0.0115 126 PRO A C   
994  O O   . PRO A 133 ? 0.1988 0.1718 0.2063 -0.0130 0.0427  -0.0245 126 PRO A O   
995  C CB  . PRO A 133 ? 0.2124 0.1610 0.2481 -0.0050 0.0436  0.0014  126 PRO A CB  
996  C CG  . PRO A 133 ? 0.2274 0.1679 0.2736 -0.0084 0.0495  0.0092  126 PRO A CG  
997  C CD  . PRO A 133 ? 0.2037 0.1550 0.2402 -0.0156 0.0518  -0.0004 126 PRO A CD  
998  N N   . SER A 134 ? 0.1899 0.1623 0.1740 -0.0050 0.0316  -0.0077 127 SER A N   
999  C CA  . SER A 134 ? 0.1796 0.1606 0.1548 -0.0074 0.0309  -0.0143 127 SER A CA  
1000 C C   . SER A 134 ? 0.1806 0.1596 0.1466 -0.0039 0.0235  -0.0084 127 SER A C   
1001 O O   . SER A 134 ? 0.2029 0.1762 0.1645 -0.0001 0.0182  -0.0016 127 SER A O   
1002 C CB  . SER A 134 ? 0.1880 0.1763 0.1525 -0.0107 0.0319  -0.0171 127 SER A CB  
1003 O OG  . SER A 134 ? 0.2049 0.1908 0.1599 -0.0071 0.0296  -0.0097 127 SER A OG  
1004 N N   . TYR A 135 ? 0.1813 0.1651 0.1437 -0.0061 0.0230  -0.0108 128 TYR A N   
1005 C CA  . TYR A 135 ? 0.1752 0.1553 0.1332 -0.0047 0.0160  -0.0075 128 TYR A CA  
1006 C C   . TYR A 135 ? 0.1660 0.1464 0.1137 -0.0058 0.0164  -0.0067 128 TYR A C   
1007 O O   . TYR A 135 ? 0.1958 0.1835 0.1429 -0.0089 0.0212  -0.0068 128 TYR A O   
1008 C CB  . TYR A 135 ? 0.1704 0.1546 0.1462 -0.0067 0.0151  -0.0083 128 TYR A CB  
1009 C CG  . TYR A 135 ? 0.1703 0.1507 0.1477 -0.0067 0.0050  -0.0065 128 TYR A CG  
1010 C CD1 . TYR A 135 ? 0.1913 0.1673 0.1627 -0.0033 -0.0052 -0.0049 128 TYR A CD1 
1011 C CD2 . TYR A 135 ? 0.1833 0.1648 0.1681 -0.0112 0.0054  -0.0065 128 TYR A CD2 
1012 C CE1 . TYR A 135 ? 0.2149 0.1887 0.1864 -0.0048 -0.0166 -0.0070 128 TYR A CE1 
1013 C CE2 . TYR A 135 ? 0.2253 0.2024 0.2163 -0.0132 -0.0048 -0.0077 128 TYR A CE2 
1014 C CZ  . TYR A 135 ? 0.2073 0.1811 0.1909 -0.0102 -0.0166 -0.0098 128 TYR A CZ  
1015 O OH  . TYR A 135 ? 0.2279 0.1987 0.2160 -0.0135 -0.0290 -0.0144 128 TYR A OH  
1016 N N   . VAL A 136 ? 0.1984 0.1707 0.1375 -0.0028 0.0115  -0.0058 129 VAL A N   
1017 C CA  . VAL A 136 ? 0.1836 0.1521 0.1194 -0.0020 0.0115  -0.0040 129 VAL A CA  
1018 C C   . VAL A 136 ? 0.2046 0.1627 0.1448 -0.0032 0.0054  -0.0063 129 VAL A C   
1019 O O   . VAL A 136 ? 0.2255 0.1768 0.1584 -0.0011 -0.0002 -0.0119 129 VAL A O   
1020 C CB  . VAL A 136 ? 0.2141 0.1813 0.1414 0.0034  0.0136  -0.0041 129 VAL A CB  
1021 C CG1 . VAL A 136 ? 0.2529 0.2157 0.1838 0.0059  0.0134  -0.0006 129 VAL A CG1 
1022 C CG2 . VAL A 136 ? 0.2522 0.2314 0.1809 0.0022  0.0180  -0.0029 129 VAL A CG2 
1023 N N   . ASN A 137 ? 0.1970 0.1987 0.1458 0.0135  -0.0071 -0.0216 130 ASN A N   
1024 C CA  . ASN A 137 ? 0.1841 0.1852 0.1339 0.0088  -0.0145 -0.0287 130 ASN A CA  
1025 C C   . ASN A 137 ? 0.2091 0.1958 0.1452 0.0081  -0.0126 -0.0345 130 ASN A C   
1026 O O   . ASN A 137 ? 0.2368 0.2166 0.1674 0.0117  -0.0050 -0.0329 130 ASN A O   
1027 C CB  . ASN A 137 ? 0.2002 0.2097 0.1715 0.0024  -0.0143 -0.0293 130 ASN A CB  
1028 C CG  . ASN A 137 ? 0.1964 0.2144 0.1784 -0.0030 -0.0240 -0.0350 130 ASN A CG  
1029 O OD1 . ASN A 137 ? 0.2029 0.2165 0.1736 -0.0035 -0.0325 -0.0402 130 ASN A OD1 
1030 N ND2 . ASN A 137 ? 0.2130 0.2449 0.2182 -0.0073 -0.0227 -0.0345 130 ASN A ND2 
1031 N N   . ILE A 138 ? 0.2148 0.1971 0.1469 0.0036  -0.0207 -0.0421 131 ILE A N   
1032 C CA  . ILE A 138 ? 0.2323 0.1971 0.1488 0.0034  -0.0203 -0.0495 131 ILE A CA  
1033 C C   . ILE A 138 ? 0.2601 0.2146 0.1829 0.0015  -0.0128 -0.0486 131 ILE A C   
1034 O O   . ILE A 138 ? 0.2480 0.2067 0.1868 -0.0046 -0.0111 -0.0451 131 ILE A O   
1035 C CB  . ILE A 138 ? 0.2505 0.2122 0.1644 -0.0036 -0.0327 -0.0586 131 ILE A CB  
1036 C CG1 . ILE A 138 ? 0.2875 0.2266 0.1814 -0.0035 -0.0334 -0.0683 131 ILE A CG1 
1037 C CG2 . ILE A 138 ? 0.2641 0.2353 0.2043 -0.0143 -0.0355 -0.0585 131 ILE A CG2 
1038 C CD1 . ILE A 138 ? 0.3082 0.2431 0.1922 -0.0088 -0.0479 -0.0784 131 ILE A CD1 
1039 N N   . GLY A 139 ? 0.2695 0.2096 0.1785 0.0076  -0.0079 -0.0515 132 GLY A N   
1040 C CA  . GLY A 139 ? 0.2592 0.1867 0.1718 0.0082  -0.0028 -0.0502 132 GLY A CA  
1041 C C   . GLY A 139 ? 0.2835 0.2188 0.2041 0.0141  0.0041  -0.0418 132 GLY A C   
1042 O O   . GLY A 139 ? 0.2890 0.2131 0.2098 0.0174  0.0069  -0.0405 132 GLY A O   
1043 N N   . ALA A 140 ? 0.2406 0.1931 0.1677 0.0154  0.0055  -0.0362 133 ALA A N   
1044 C CA  . ALA A 140 ? 0.2339 0.1938 0.1694 0.0194  0.0104  -0.0293 133 ALA A CA  
1045 C C   . ALA A 140 ? 0.2285 0.1876 0.1600 0.0285  0.0157  -0.0303 133 ALA A C   
1046 O O   . ALA A 140 ? 0.2472 0.2037 0.1673 0.0323  0.0177  -0.0352 133 ALA A O   
1047 C CB  . ALA A 140 ? 0.2440 0.2190 0.1867 0.0178  0.0102  -0.0240 133 ALA A CB  
1048 N N   . TYR A 141 ? 0.2116 0.1738 0.1527 0.0323  0.0179  -0.0261 134 TYR A N   
1049 C CA  . TYR A 141 ? 0.2163 0.1839 0.1619 0.0412  0.0232  -0.0265 134 TYR A CA  
1050 C C   . TYR A 141 ? 0.2269 0.2107 0.1873 0.0404  0.0244  -0.0198 134 TYR A C   
1051 O O   . TYR A 141 ? 0.2278 0.2108 0.1944 0.0378  0.0197  -0.0162 134 TYR A O   
1052 C CB  . TYR A 141 ? 0.2538 0.2075 0.1996 0.0475  0.0217  -0.0291 134 TYR A CB  
1053 C CG  . TYR A 141 ? 0.2771 0.2366 0.2303 0.0590  0.0272  -0.0315 134 TYR A CG  
1054 C CD1 . TYR A 141 ? 0.2709 0.2475 0.2431 0.0627  0.0280  -0.0266 134 TYR A CD1 
1055 C CD2 . TYR A 141 ? 0.2496 0.1979 0.1925 0.0663  0.0315  -0.0394 134 TYR A CD2 
1056 C CE1 . TYR A 141 ? 0.3075 0.2939 0.2924 0.0736  0.0335  -0.0291 134 TYR A CE1 
1057 C CE2 . TYR A 141 ? 0.3104 0.2656 0.2625 0.0786  0.0384  -0.0424 134 TYR A CE2 
1058 C CZ  . TYR A 141 ? 0.3170 0.2935 0.2925 0.0822  0.0397  -0.0368 134 TYR A CZ  
1059 O OH  . TYR A 141 ? 0.3417 0.3299 0.3324 0.0946  0.0471  -0.0400 134 TYR A OH  
1060 N N   . VAL A 142 ? 0.2221 0.2188 0.1860 0.0414  0.0306  -0.0181 135 VAL A N   
1061 C CA  . VAL A 142 ? 0.2036 0.2143 0.1823 0.0385  0.0316  -0.0121 135 VAL A CA  
1062 C C   . VAL A 142 ? 0.1876 0.2116 0.1806 0.0445  0.0389  -0.0123 135 VAL A C   
1063 O O   . VAL A 142 ? 0.2294 0.2583 0.2176 0.0466  0.0484  -0.0132 135 VAL A O   
1064 C CB  . VAL A 142 ? 0.2010 0.2145 0.1738 0.0325  0.0330  -0.0082 135 VAL A CB  
1065 C CG1 . VAL A 142 ? 0.2425 0.2659 0.2302 0.0282  0.0332  -0.0026 135 VAL A CG1 
1066 C CG2 . VAL A 142 ? 0.2521 0.2562 0.2149 0.0284  0.0263  -0.0092 135 VAL A CG2 
1067 N N   . ASP A 143 ? 0.2251 0.2555 0.2353 0.0476  0.0345  -0.0115 136 ASP A N   
1068 C CA  . ASP A 143 ? 0.2134 0.2590 0.2428 0.0553  0.0401  -0.0130 136 ASP A CA  
1069 C C   . ASP A 143 ? 0.2164 0.2830 0.2656 0.0496  0.0457  -0.0084 136 ASP A C   
1070 O O   . ASP A 143 ? 0.1978 0.2634 0.2436 0.0401  0.0443  -0.0039 136 ASP A O   
1071 C CB  . ASP A 143 ? 0.2027 0.2457 0.2426 0.0624  0.0303  -0.0139 136 ASP A CB  
1072 C CG  . ASP A 143 ? 0.2244 0.2742 0.2772 0.0755  0.0353  -0.0185 136 ASP A CG  
1073 O OD1 . ASP A 143 ? 0.2580 0.3210 0.3178 0.0790  0.0484  -0.0210 136 ASP A OD1 
1074 O OD2 . ASP A 143 ? 0.2607 0.3017 0.3160 0.0834  0.0263  -0.0194 136 ASP A OD2 
1075 N N   . GLU A 144 ? 0.1781 0.2634 0.2499 0.0558  0.0525  -0.0098 137 GLU A N   
1076 C CA  . GLU A 144 ? 0.1995 0.3065 0.2914 0.0504  0.0633  -0.0062 137 GLU A CA  
1077 C C   . GLU A 144 ? 0.2028 0.3168 0.3098 0.0390  0.0550  -0.0010 137 GLU A C   
1078 O O   . GLU A 144 ? 0.1854 0.2991 0.3016 0.0392  0.0409  -0.0016 137 GLU A O   
1079 C CB  . GLU A 144 ? 0.1959 0.3253 0.3163 0.0606  0.0708  -0.0098 137 GLU A CB  
1080 C CG  . GLU A 144 ? 0.3270 0.4814 0.4697 0.0555  0.0870  -0.0066 137 GLU A CG  
1081 C CD  . GLU A 144 ? 0.5092 0.6865 0.6889 0.0467  0.0802  -0.0028 137 GLU A CD  
1082 O OE1 . GLU A 144 ? 0.4898 0.6814 0.6833 0.0359  0.0914  0.0022  137 GLU A OE1 
1083 O OE2 . GLU A 144 ? 0.5447 0.7240 0.7381 0.0499  0.0630  -0.0046 137 GLU A OE2 
1084 N N   . GLY A 145 ? 0.1697 0.2877 0.2768 0.0289  0.0637  0.0042  138 GLY A N   
1085 C CA  . GLY A 145 ? 0.1882 0.3123 0.3118 0.0172  0.0579  0.0085  138 GLY A CA  
1086 C C   . GLY A 145 ? 0.1761 0.2790 0.2802 0.0116  0.0457  0.0097  138 GLY A C   
1087 O O   . GLY A 145 ? 0.1950 0.2988 0.3100 0.0024  0.0393  0.0116  138 GLY A O   
1088 N N   . THR A 146 ? 0.1638 0.2482 0.2412 0.0165  0.0426  0.0077  139 THR A N   
1089 C CA  . THR A 146 ? 0.1627 0.2296 0.2242 0.0128  0.0324  0.0078  139 THR A CA  
1090 C C   . THR A 146 ? 0.2139 0.2709 0.2634 0.0059  0.0367  0.0126  139 THR A C   
1091 O O   . THR A 146 ? 0.1808 0.2370 0.2206 0.0063  0.0466  0.0157  139 THR A O   
1092 C CB  . THR A 146 ? 0.1834 0.2371 0.2260 0.0198  0.0281  0.0040  139 THR A CB  
1093 O OG1 . THR A 146 ? 0.2026 0.2602 0.2553 0.0251  0.0205  0.0011  139 THR A OG1 
1094 C CG2 . THR A 146 ? 0.2203 0.2583 0.2462 0.0163  0.0224  0.0043  139 THR A CG2 
1095 N N   . MET A 147 ? 0.1804 0.2280 0.2285 0.0003  0.0289  0.0132  140 MET A N   
1096 C CA  . MET A 147 ? 0.1841 0.2187 0.2212 -0.0048 0.0305  0.0175  140 MET A CA  
1097 C C   . MET A 147 ? 0.2275 0.2478 0.2464 -0.0004 0.0246  0.0147  140 MET A C   
1098 O O   . MET A 147 ? 0.2134 0.2303 0.2319 0.0007  0.0172  0.0103  140 MET A O   
1099 C CB  . MET A 147 ? 0.2145 0.2475 0.2654 -0.0141 0.0266  0.0188  140 MET A CB  
1100 C CG  . MET A 147 ? 0.4340 0.4856 0.5106 -0.0206 0.0317  0.0210  140 MET A CG  
1101 S SD  . MET A 147 ? 0.6195 0.6769 0.6959 -0.0241 0.0499  0.0295  140 MET A SD  
1102 C CE  . MET A 147 ? 0.4091 0.4925 0.5020 -0.0162 0.0578  0.0259  140 MET A CE  
1103 N N   . VAL A 148 ? 0.1934 0.2065 0.1976 0.0022  0.0278  0.0174  141 VAL A N   
1104 C CA  . VAL A 148 ? 0.1963 0.1998 0.1885 0.0061  0.0227  0.0151  141 VAL A CA  
1105 C C   . VAL A 148 ? 0.2119 0.2037 0.1995 0.0042  0.0220  0.0197  141 VAL A C   
1106 O O   . VAL A 148 ? 0.2159 0.2037 0.1951 0.0045  0.0257  0.0256  141 VAL A O   
1107 C CB  . VAL A 148 ? 0.2033 0.2085 0.1843 0.0113  0.0239  0.0136  141 VAL A CB  
1108 C CG1 . VAL A 148 ? 0.2230 0.2231 0.1984 0.0141  0.0184  0.0108  141 VAL A CG1 
1109 C CG2 . VAL A 148 ? 0.2420 0.2545 0.2265 0.0137  0.0252  0.0091  141 VAL A CG2 
1110 N N   . ASP A 149 ? 0.1938 0.1776 0.1843 0.0030  0.0172  0.0170  142 ASP A N   
1111 C CA  . ASP A 149 ? 0.2177 0.1869 0.2054 0.0015  0.0163  0.0207  142 ASP A CA  
1112 C C   . ASP A 149 ? 0.2124 0.1746 0.1911 0.0092  0.0135  0.0211  142 ASP A C   
1113 O O   . ASP A 149 ? 0.2020 0.1724 0.1780 0.0142  0.0124  0.0185  142 ASP A O   
1114 C CB  . ASP A 149 ? 0.2278 0.1893 0.2216 -0.0030 0.0122  0.0162  142 ASP A CB  
1115 C CG  . ASP A 149 ? 0.4084 0.3744 0.4146 -0.0125 0.0131  0.0181  142 ASP A CG  
1116 O OD1 . ASP A 149 ? 0.3679 0.3454 0.3799 -0.0150 0.0191  0.0230  142 ASP A OD1 
1117 O OD2 . ASP A 149 ? 0.3654 0.3241 0.3762 -0.0175 0.0077  0.0139  142 ASP A OD2 
1118 N N   . THR A 150 ? 0.2275 0.1738 0.2029 0.0102  0.0118  0.0245  143 THR A N   
1119 C CA  . THR A 150 ? 0.2294 0.1692 0.1978 0.0188  0.0084  0.0272  143 THR A CA  
1120 C C   . THR A 150 ? 0.2307 0.1783 0.2050 0.0260  0.0053  0.0193  143 THR A C   
1121 O O   . THR A 150 ? 0.2200 0.1647 0.1990 0.0259  0.0059  0.0127  143 THR A O   
1122 C CB  . THR A 150 ? 0.2337 0.1514 0.1975 0.0191  0.0071  0.0329  143 THR A CB  
1123 O OG1 . THR A 150 ? 0.2535 0.1654 0.2127 0.0103  0.0122  0.0414  143 THR A OG1 
1124 C CG2 . THR A 150 ? 0.2479 0.1579 0.2048 0.0299  0.0017  0.0368  143 THR A CG2 
1125 N N   . TRP A 151 ? 0.1966 0.1541 0.1698 0.0316  0.0023  0.0198  144 TRP A N   
1126 C CA  . TRP A 151 ? 0.1785 0.1484 0.1611 0.0370  0.0001  0.0132  144 TRP A CA  
1127 C C   . TRP A 151 ? 0.1862 0.1662 0.1738 0.0319  0.0045  0.0064  144 TRP A C   
1128 O O   . TRP A 151 ? 0.1957 0.1832 0.1916 0.0342  0.0060  0.0007  144 TRP A O   
1129 C CB  . TRP A 151 ? 0.1880 0.1517 0.1781 0.0454  -0.0019 0.0108  144 TRP A CB  
1130 C CG  . TRP A 151 ? 0.2090 0.1575 0.1927 0.0518  -0.0073 0.0183  144 TRP A CG  
1131 C CD1 . TRP A 151 ? 0.2266 0.1553 0.2088 0.0556  -0.0075 0.0195  144 TRP A CD1 
1132 C CD2 . TRP A 151 ? 0.2203 0.1679 0.1947 0.0554  -0.0139 0.0260  144 TRP A CD2 
1133 N NE1 . TRP A 151 ? 0.2477 0.1628 0.2213 0.0615  -0.0135 0.0285  144 TRP A NE1 
1134 C CE2 . TRP A 151 ? 0.2450 0.1715 0.2122 0.0616  -0.0177 0.0330  144 TRP A CE2 
1135 C CE3 . TRP A 151 ? 0.2163 0.1761 0.1848 0.0543  -0.0175 0.0274  144 TRP A CE3 
1136 C CZ2 . TRP A 151 ? 0.2661 0.1835 0.2189 0.0666  -0.0249 0.0426  144 TRP A CZ2 
1137 C CZ3 . TRP A 151 ? 0.2372 0.1890 0.1909 0.0593  -0.0250 0.0355  144 TRP A CZ3 
1138 C CH2 . TRP A 151 ? 0.2622 0.1930 0.2073 0.0654  -0.0286 0.0437  144 TRP A CH2 
1139 N N   . ALA A 152 ? 0.1909 0.1719 0.1738 0.0255  0.0070  0.0076  145 ALA A N   
1140 C CA  . ALA A 152 ? 0.2011 0.1903 0.1858 0.0220  0.0093  0.0029  145 ALA A CA  
1141 C C   . ALA A 152 ? 0.1851 0.1841 0.1699 0.0227  0.0077  0.0018  145 ALA A C   
1142 O O   . ALA A 152 ? 0.1645 0.1647 0.1453 0.0254  0.0040  0.0047  145 ALA A O   
1143 C CB  . ALA A 152 ? 0.1996 0.1872 0.1819 0.0167  0.0111  0.0042  145 ALA A CB  
1144 N N   . THR A 153 ? 0.1704 0.1741 0.1575 0.0200  0.0097  -0.0024 146 THR A N   
1145 C CA  . THR A 153 ? 0.1672 0.1777 0.1553 0.0187  0.0079  -0.0049 146 THR A CA  
1146 C C   . THR A 153 ? 0.1670 0.1743 0.1504 0.0148  0.0106  -0.0065 146 THR A C   
1147 O O   . THR A 153 ? 0.1863 0.1898 0.1692 0.0129  0.0137  -0.0073 146 THR A O   
1148 C CB  . THR A 153 ? 0.2198 0.2391 0.2199 0.0188  0.0078  -0.0086 146 THR A CB  
1149 O OG1 . THR A 153 ? 0.2748 0.2976 0.2820 0.0248  0.0044  -0.0074 146 THR A OG1 
1150 C CG2 . THR A 153 ? 0.2284 0.2544 0.2316 0.0154  0.0043  -0.0117 146 THR A CG2 
1151 N N   . VAL A 154 ? 0.1678 0.1746 0.1454 0.0146  0.0092  -0.0072 147 VAL A N   
1152 C CA  . VAL A 154 ? 0.1701 0.1717 0.1436 0.0125  0.0108  -0.0094 147 VAL A CA  
1153 C C   . VAL A 154 ? 0.1801 0.1824 0.1544 0.0094  0.0083  -0.0136 147 VAL A C   
1154 O O   . VAL A 154 ? 0.1887 0.1919 0.1582 0.0105  0.0044  -0.0157 147 VAL A O   
1155 C CB  . VAL A 154 ? 0.2012 0.2006 0.1688 0.0155  0.0123  -0.0083 147 VAL A CB  
1156 C CG1 . VAL A 154 ? 0.2023 0.1947 0.1667 0.0158  0.0131  -0.0109 147 VAL A CG1 
1157 C CG2 . VAL A 154 ? 0.2115 0.2131 0.1833 0.0164  0.0142  -0.0041 147 VAL A CG2 
1158 N N   . GLY A 155 ? 0.1678 0.1687 0.1471 0.0047  0.0105  -0.0149 148 GLY A N   
1159 C CA  . GLY A 155 ? 0.1885 0.1917 0.1736 -0.0009 0.0085  -0.0189 148 GLY A CA  
1160 C C   . GLY A 155 ? 0.1947 0.1860 0.1706 -0.0032 0.0067  -0.0222 148 GLY A C   
1161 O O   . GLY A 155 ? 0.2127 0.1938 0.1782 0.0009  0.0079  -0.0214 148 GLY A O   
1162 N N   . SER A 156 ? 0.1974 0.1899 0.1793 -0.0098 0.0033  -0.0267 149 SER A N   
1163 C CA  A SER A 156 ? 0.2056 0.1839 0.1777 -0.0124 0.0001  -0.0316 149 SER A CA  
1164 C CA  B SER A 156 ? 0.2056 0.1839 0.1778 -0.0124 0.0001  -0.0316 149 SER A CA  
1165 C C   . SER A 156 ? 0.2298 0.1899 0.1928 -0.0123 0.0054  -0.0292 149 SER A C   
1166 O O   . SER A 156 ? 0.2365 0.1932 0.2026 -0.0168 0.0106  -0.0251 149 SER A O   
1167 C CB  A SER A 156 ? 0.2930 0.2751 0.2760 -0.0222 -0.0050 -0.0371 149 SER A CB  
1168 C CB  B SER A 156 ? 0.2930 0.2755 0.2766 -0.0224 -0.0049 -0.0370 149 SER A CB  
1169 O OG  A SER A 156 ? 0.3589 0.3468 0.3568 -0.0300 0.0013  -0.0343 149 SER A OG  
1170 O OG  B SER A 156 ? 0.2890 0.2541 0.2613 -0.0256 -0.0089 -0.0430 149 SER A OG  
1171 N N   . CYS A 157 ? 0.2310 0.1787 0.1812 -0.0062 0.0042  -0.0316 150 CYS A N   
1172 C CA  . CYS A 157 ? 0.2660 0.1942 0.2070 -0.0034 0.0066  -0.0305 150 CYS A CA  
1173 C C   . CYS A 157 ? 0.2671 0.1974 0.2082 0.0030  0.0099  -0.0236 150 CYS A C   
1174 O O   . CYS A 157 ? 0.2508 0.1662 0.1850 0.0075  0.0100  -0.0219 150 CYS A O   
1175 C CB  . CYS A 157 ? 0.2553 0.1674 0.1959 -0.0136 0.0072  -0.0307 150 CYS A CB  
1176 S SG  . CYS A 157 ? 0.3155 0.2219 0.2576 -0.0232 0.0007  -0.0407 150 CYS A SG  
1177 N N   . ALA A 158 ? 0.2365 0.1834 0.1848 0.0040  0.0112  -0.0200 151 ALA A N   
1178 C CA  . ALA A 158 ? 0.2225 0.1707 0.1705 0.0084  0.0124  -0.0147 151 ALA A CA  
1179 C C   . ALA A 158 ? 0.2291 0.1771 0.1764 0.0177  0.0113  -0.0151 151 ALA A C   
1180 O O   . ALA A 158 ? 0.2381 0.1919 0.1860 0.0212  0.0121  -0.0186 151 ALA A O   
1181 C CB  . ALA A 158 ? 0.2229 0.1866 0.1784 0.0075  0.0135  -0.0125 151 ALA A CB  
1182 N N   . GLN A 159 ? 0.2389 0.1806 0.1846 0.0220  0.0095  -0.0115 152 GLN A N   
1183 C CA  . GLN A 159 ? 0.2270 0.1720 0.1778 0.0317  0.0080  -0.0117 152 GLN A CA  
1184 C C   . GLN A 159 ? 0.2312 0.1907 0.1914 0.0327  0.0060  -0.0081 152 GLN A C   
1185 O O   . GLN A 159 ? 0.2406 0.1949 0.1965 0.0312  0.0019  -0.0045 152 GLN A O   
1186 C CB  . GLN A 159 ? 0.2391 0.1649 0.1828 0.0374  0.0046  -0.0108 152 GLN A CB  
1187 C CG  . GLN A 159 ? 0.2622 0.1679 0.1949 0.0342  0.0059  -0.0146 152 GLN A CG  
1188 C CD  . GLN A 159 ? 0.2854 0.1935 0.2191 0.0384  0.0089  -0.0223 152 GLN A CD  
1189 O OE1 . GLN A 159 ? 0.2866 0.1989 0.2252 0.0489  0.0102  -0.0246 152 GLN A OE1 
1190 N NE2 . GLN A 159 ? 0.2912 0.1963 0.2195 0.0304  0.0098  -0.0268 152 GLN A NE2 
1191 N N   . ILE A 160 ? 0.2024 0.1782 0.1736 0.0346  0.0090  -0.0091 153 ILE A N   
1192 C CA  . ILE A 160 ? 0.2029 0.1925 0.1856 0.0336  0.0072  -0.0063 153 ILE A CA  
1193 C C   . ILE A 160 ? 0.2149 0.2153 0.2126 0.0412  0.0069  -0.0067 153 ILE A C   
1194 O O   . ILE A 160 ? 0.2228 0.2283 0.2242 0.0458  0.0133  -0.0094 153 ILE A O   
1195 C CB  . ILE A 160 ? 0.1997 0.1988 0.1852 0.0284  0.0116  -0.0056 153 ILE A CB  
1196 C CG1 . ILE A 160 ? 0.2332 0.2252 0.2082 0.0232  0.0123  -0.0063 153 ILE A CG1 
1197 C CG2 . ILE A 160 ? 0.1948 0.2024 0.1905 0.0254  0.0087  -0.0030 153 ILE A CG2 
1198 C CD1 . ILE A 160 ? 0.2338 0.2175 0.2030 0.0196  0.0093  -0.0053 153 ILE A CD1 
1199 N N   . GLY A 161 ? 0.2208 0.2254 0.2272 0.0430  -0.0007 -0.0046 154 GLY A N   
1200 C CA  . GLY A 161 ? 0.1823 0.2007 0.2085 0.0510  -0.0029 -0.0052 154 GLY A CA  
1201 C C   . GLY A 161 ? 0.1811 0.2224 0.2284 0.0479  0.0034  -0.0051 154 GLY A C   
1202 O O   . GLY A 161 ? 0.2057 0.2488 0.2487 0.0404  0.0097  -0.0041 154 GLY A O   
1203 N N   . LYS A 162 ? 0.1686 0.2276 0.2401 0.0543  0.0016  -0.0058 155 LYS A N   
1204 C CA  . LYS A 162 ? 0.1615 0.2451 0.2585 0.0507  0.0086  -0.0052 155 LYS A CA  
1205 C C   . LYS A 162 ? 0.2190 0.3085 0.3248 0.0401  0.0003  -0.0027 155 LYS A C   
1206 O O   . LYS A 162 ? 0.1773 0.2593 0.2786 0.0401  -0.0136 -0.0027 155 LYS A O   
1207 C CB  . LYS A 162 ? 0.1734 0.2775 0.2989 0.0614  0.0094  -0.0074 155 LYS A CB  
1208 C CG  . LYS A 162 ? 0.1839 0.2822 0.3027 0.0733  0.0190  -0.0114 155 LYS A CG  
1209 C CD  . LYS A 162 ? 0.2399 0.3613 0.3917 0.0857  0.0198  -0.0141 155 LYS A CD  
1210 C CE  . LYS A 162 ? 0.3500 0.4621 0.4928 0.0993  0.0300  -0.0197 155 LYS A CE  
1211 N NZ  . LYS A 162 ? 0.3656 0.4451 0.4809 0.1052  0.0198  -0.0206 155 LYS A NZ  
1212 N N   . ASN A 163 ? 0.1707 0.2709 0.2864 0.0311  0.0090  -0.0007 156 ASN A N   
1213 C CA  . ASN A 163 ? 0.1957 0.3015 0.3235 0.0200  0.0022  0.0008  156 ASN A CA  
1214 C C   . ASN A 163 ? 0.1991 0.2824 0.3021 0.0157  -0.0081 0.0003  156 ASN A C   
1215 O O   . ASN A 163 ? 0.1983 0.2813 0.3064 0.0109  -0.0201 -0.0010 156 ASN A O   
1216 C CB  . ASN A 163 ? 0.1870 0.3158 0.3482 0.0213  -0.0069 -0.0007 156 ASN A CB  
1217 C CG  . ASN A 163 ? 0.2252 0.3802 0.4155 0.0253  0.0064  -0.0006 156 ASN A CG  
1218 O OD1 . ASN A 163 ? 0.2791 0.4403 0.4733 0.0183  0.0216  0.0022  156 ASN A OD1 
1219 N ND2 . ASN A 163 ? 0.2621 0.4305 0.4702 0.0377  0.0021  -0.0034 156 ASN A ND2 
1220 N N   . VAL A 164 ? 0.1876 0.2528 0.2644 0.0176  -0.0034 0.0006  157 VAL A N   
1221 C CA  . VAL A 164 ? 0.1527 0.1983 0.2067 0.0141  -0.0087 0.0000  157 VAL A CA  
1222 C C   . VAL A 164 ? 0.1914 0.2334 0.2438 0.0058  -0.0034 0.0017  157 VAL A C   
1223 O O   . VAL A 164 ? 0.1966 0.2450 0.2546 0.0039  0.0065  0.0047  157 VAL A O   
1224 C CB  . VAL A 164 ? 0.1696 0.2007 0.2019 0.0195  -0.0058 -0.0006 157 VAL A CB  
1225 C CG1 . VAL A 164 ? 0.1996 0.2149 0.2124 0.0154  -0.0066 -0.0011 157 VAL A CG1 
1226 C CG2 . VAL A 164 ? 0.1902 0.2182 0.2207 0.0274  -0.0128 -0.0014 157 VAL A CG2 
1227 N N   . HIS A 165 ? 0.1889 0.2187 0.2315 0.0012  -0.0100 0.0000  158 HIS A N   
1228 C CA  . HIS A 165 ? 0.1777 0.1982 0.2153 -0.0048 -0.0063 0.0012  158 HIS A CA  
1229 C C   . HIS A 165 ? 0.1780 0.1824 0.1935 -0.0017 -0.0058 -0.0008 158 HIS A C   
1230 O O   . HIS A 165 ? 0.2070 0.2018 0.2114 -0.0013 -0.0122 -0.0045 158 HIS A O   
1231 C CB  . HIS A 165 ? 0.2106 0.2302 0.2587 -0.0130 -0.0138 -0.0006 158 HIS A CB  
1232 C CG  . HIS A 165 ? 0.2974 0.3056 0.3431 -0.0195 -0.0096 0.0014  158 HIS A CG  
1233 N ND1 . HIS A 165 ? 0.4587 0.4666 0.5186 -0.0294 -0.0132 0.0013  158 HIS A ND1 
1234 C CD2 . HIS A 165 ? 0.4219 0.4178 0.4538 -0.0172 -0.0030 0.0038  158 HIS A CD2 
1235 C CE1 . HIS A 165 ? 0.4514 0.4437 0.5036 -0.0328 -0.0083 0.0041  158 HIS A CE1 
1236 N NE2 . HIS A 165 ? 0.3409 0.3265 0.3764 -0.0246 -0.0025 0.0057  158 HIS A NE2 
1237 N N   . LEU A 166 ? 0.1726 0.1748 0.1817 0.0007  0.0017  0.0014  159 LEU A N   
1238 C CA  . LEU A 166 ? 0.1867 0.1782 0.1816 0.0034  0.0031  -0.0004 159 LEU A CA  
1239 C C   . LEU A 166 ? 0.1962 0.1790 0.1908 0.0009  0.0040  0.0007  159 LEU A C   
1240 O O   . LEU A 166 ? 0.2104 0.1945 0.2082 0.0003  0.0080  0.0054  159 LEU A O   
1241 C CB  . LEU A 166 ? 0.1800 0.1752 0.1706 0.0076  0.0079  0.0007  159 LEU A CB  
1242 C CG  . LEU A 166 ? 0.1871 0.1865 0.1767 0.0104  0.0076  -0.0004 159 LEU A CG  
1243 C CD1 . LEU A 166 ? 0.2220 0.2220 0.2063 0.0129  0.0113  -0.0007 159 LEU A CD1 
1244 C CD2 . LEU A 166 ? 0.2156 0.2077 0.1974 0.0106  0.0032  -0.0028 159 LEU A CD2 
1245 N N   . SER A 167 ? 0.2144 0.1857 0.2028 -0.0002 0.0003  -0.0036 160 SER A N   
1246 C CA  . SER A 167 ? 0.1868 0.1458 0.1748 -0.0022 0.0002  -0.0034 160 SER A CA  
1247 C C   . SER A 167 ? 0.2120 0.1665 0.1950 0.0043  0.0046  -0.0022 160 SER A C   
1248 O O   . SER A 167 ? 0.2166 0.1795 0.1981 0.0088  0.0074  -0.0021 160 SER A O   
1249 C CB  . SER A 167 ? 0.2447 0.1904 0.2252 -0.0045 -0.0055 -0.0102 160 SER A CB  
1250 O OG  . SER A 167 ? 0.2983 0.2489 0.2857 -0.0108 -0.0127 -0.0115 160 SER A OG  
1251 N N   . GLY A 168 ? 0.2239 0.1643 0.2056 0.0047  0.0042  -0.0016 161 GLY A N   
1252 C CA  . GLY A 168 ? 0.2480 0.1847 0.2277 0.0124  0.0064  0.0002  161 GLY A CA  
1253 C C   . GLY A 168 ? 0.2226 0.1650 0.2005 0.0191  0.0087  -0.0058 161 GLY A C   
1254 O O   . GLY A 168 ? 0.2298 0.1669 0.2018 0.0190  0.0095  -0.0125 161 GLY A O   
1255 N N   . GLY A 169 ? 0.1919 0.1451 0.1741 0.0243  0.0100  -0.0035 162 GLY A N   
1256 C CA  . GLY A 169 ? 0.2397 0.2009 0.2257 0.0298  0.0132  -0.0087 162 GLY A CA  
1257 C C   . GLY A 169 ? 0.2608 0.2303 0.2438 0.0256  0.0166  -0.0120 162 GLY A C   
1258 O O   . GLY A 169 ? 0.2801 0.2547 0.2651 0.0281  0.0217  -0.0164 162 GLY A O   
1259 N N   . VAL A 170 ? 0.2123 0.1830 0.1913 0.0198  0.0145  -0.0097 163 VAL A N   
1260 C CA  . VAL A 170 ? 0.1591 0.1339 0.1330 0.0167  0.0163  -0.0115 163 VAL A CA  
1261 C C   . VAL A 170 ? 0.2086 0.1953 0.1887 0.0170  0.0181  -0.0102 163 VAL A C   
1262 O O   . VAL A 170 ? 0.2384 0.2303 0.2229 0.0176  0.0154  -0.0070 163 VAL A O   
1263 C CB  . VAL A 170 ? 0.1762 0.1487 0.1466 0.0123  0.0118  -0.0096 163 VAL A CB  
1264 C CG1 . VAL A 170 ? 0.2423 0.2181 0.2079 0.0110  0.0124  -0.0094 163 VAL A CG1 
1265 C CG2 . VAL A 170 ? 0.2165 0.1773 0.1799 0.0105  0.0085  -0.0129 163 VAL A CG2 
1266 N N   . GLY A 171 ? 0.1941 0.1834 0.1728 0.0157  0.0229  -0.0128 164 GLY A N   
1267 C CA  . GLY A 171 ? 0.1945 0.1929 0.1792 0.0135  0.0238  -0.0123 164 GLY A CA  
1268 C C   . GLY A 171 ? 0.1910 0.1836 0.1661 0.0090  0.0252  -0.0115 164 GLY A C   
1269 O O   . GLY A 171 ? 0.1934 0.1782 0.1580 0.0073  0.0293  -0.0122 164 GLY A O   
1270 N N   . ILE A 172 ? 0.1831 0.1773 0.1592 0.0076  0.0219  -0.0100 165 ILE A N   
1271 C CA  . ILE A 172 ? 0.1690 0.1552 0.1368 0.0045  0.0223  -0.0090 165 ILE A CA  
1272 C C   . ILE A 172 ? 0.2093 0.2000 0.1841 0.0001  0.0245  -0.0108 165 ILE A C   
1273 O O   . ILE A 172 ? 0.2220 0.2195 0.2039 0.0006  0.0206  -0.0123 165 ILE A O   
1274 C CB  . ILE A 172 ? 0.1983 0.1816 0.1633 0.0073  0.0172  -0.0075 165 ILE A CB  
1275 C CG1 . ILE A 172 ? 0.1807 0.1642 0.1457 0.0099  0.0142  -0.0062 165 ILE A CG1 
1276 C CG2 . ILE A 172 ? 0.2407 0.2125 0.1965 0.0063  0.0166  -0.0063 165 ILE A CG2 
1277 C CD1 . ILE A 172 ? 0.1919 0.1671 0.1474 0.0091  0.0136  -0.0063 165 ILE A CD1 
1278 N N   . GLY A 173 ? 0.1891 0.1756 0.1612 -0.0051 0.0308  -0.0105 166 GLY A N   
1279 C CA  . GLY A 173 ? 0.2135 0.2077 0.1979 -0.0114 0.0340  -0.0126 166 GLY A CA  
1280 C C   . GLY A 173 ? 0.2106 0.1970 0.1926 -0.0154 0.0298  -0.0133 166 GLY A C   
1281 O O   . GLY A 173 ? 0.2387 0.2089 0.2063 -0.0145 0.0283  -0.0109 166 GLY A O   
1282 N N   . GLY A 174 ? 0.2152 0.2124 0.2116 -0.0193 0.0266  -0.0172 167 GLY A N   
1283 C CA  . GLY A 174 ? 0.2086 0.1965 0.2020 -0.0240 0.0220  -0.0197 167 GLY A CA  
1284 C C   . GLY A 174 ? 0.2291 0.2059 0.2220 -0.0347 0.0284  -0.0185 167 GLY A C   
1285 O O   . GLY A 174 ? 0.2318 0.2154 0.2330 -0.0406 0.0371  -0.0167 167 GLY A O   
1286 N N   . VAL A 175 ? 0.2354 0.1936 0.2177 -0.0372 0.0248  -0.0196 168 VAL A N   
1287 C CA  . VAL A 175 ? 0.2644 0.2054 0.2431 -0.0482 0.0298  -0.0178 168 VAL A CA  
1288 C C   . VAL A 175 ? 0.3641 0.2938 0.3418 -0.0517 0.0216  -0.0242 168 VAL A C   
1289 O O   . VAL A 175 ? 0.4438 0.3539 0.4051 -0.0451 0.0177  -0.0248 168 VAL A O   
1290 C CB  . VAL A 175 ? 0.3055 0.2223 0.2618 -0.0452 0.0344  -0.0103 168 VAL A CB  
1291 C CG1 . VAL A 175 ? 0.3484 0.2439 0.2987 -0.0578 0.0404  -0.0068 168 VAL A CG1 
1292 C CG2 . VAL A 175 ? 0.3140 0.2391 0.2655 -0.0400 0.0400  -0.0057 168 VAL A CG2 
1293 N N   . LEU A 176 ? 0.3399 0.2826 0.3359 -0.0612 0.0182  -0.0299 169 LEU A N   
1294 C CA  . LEU A 176 ? 0.3519 0.2802 0.3451 -0.0671 0.0099  -0.0373 169 LEU A CA  
1295 C C   . LEU A 176 ? 0.4363 0.3487 0.4339 -0.0834 0.0156  -0.0357 169 LEU A C   
1296 O O   . LEU A 176 ? 0.4893 0.3704 0.4689 -0.0847 0.0161  -0.0344 169 LEU A O   
1297 C CB  . LEU A 176 ? 0.4120 0.3627 0.4196 -0.0670 -0.0011 -0.0455 169 LEU A CB  
1298 C CG  . LEU A 176 ? 0.5090 0.4473 0.5050 -0.0661 -0.0133 -0.0552 169 LEU A CG  
1299 C CD1 . LEU A 176 ? 0.3727 0.2856 0.3411 -0.0547 -0.0128 -0.0558 169 LEU A CD1 
1300 C CD2 . LEU A 176 ? 0.4715 0.4343 0.4754 -0.0608 -0.0236 -0.0597 169 LEU A CD2 
1301 N N   . GLU A 177 ? 0.4295 0.3623 0.4513 -0.0953 0.0218  -0.0345 170 GLU A N   
1302 C CA  . GLU A 177 ? 0.4811 0.3999 0.5071 -0.1119 0.0318  -0.0301 170 GLU A CA  
1303 C C   . GLU A 177 ? 0.4855 0.4036 0.5034 -0.1103 0.0474  -0.0192 170 GLU A C   
1304 O O   . GLU A 177 ? 0.4832 0.4220 0.5043 -0.0999 0.0502  -0.0177 170 GLU A O   
1305 C CB  . GLU A 177 ? 0.5869 0.5299 0.6479 -0.1286 0.0307  -0.0360 170 GLU A CB  
1306 C CG  . GLU A 177 ? 0.5817 0.5208 0.6485 -0.1340 0.0136  -0.0478 170 GLU A CG  
1307 C CD  . GLU A 177 ? 0.7070 0.6177 0.7727 -0.1526 0.0142  -0.0495 170 GLU A CD  
1308 O OE1 . GLU A 177 ? 0.7759 0.6600 0.8260 -0.1577 0.0267  -0.0403 170 GLU A OE1 
1309 O OE2 . GLU A 177 ? 0.6937 0.6062 0.7723 -0.1627 0.0013  -0.0602 170 GLU A OE2 
1310 N N   . PRO A 178 ? 0.4886 0.3798 0.4917 -0.1197 0.0575  -0.0114 171 PRO A N   
1311 C CA  . PRO A 178 ? 0.5186 0.3761 0.5118 -0.1315 0.0556  -0.0111 171 PRO A CA  
1312 C C   . PRO A 178 ? 0.4224 0.2524 0.3912 -0.1180 0.0430  -0.0143 171 PRO A C   
1313 O O   . PRO A 178 ? 0.4532 0.2824 0.4060 -0.1009 0.0404  -0.0118 171 PRO A O   
1314 C CB  . PRO A 178 ? 0.6359 0.4711 0.6118 -0.1397 0.0718  0.0019  171 PRO A CB  
1315 C CG  . PRO A 178 ? 0.5395 0.4043 0.5242 -0.1364 0.0837  0.0057  171 PRO A CG  
1316 C CD  . PRO A 178 ? 0.5076 0.3966 0.4981 -0.1186 0.0725  -0.0012 171 PRO A CD  
1317 N N   . LEU A 179 ? 0.4817 0.2884 0.4482 -0.1258 0.0356  -0.0206 172 LEU A N   
1318 C CA  . LEU A 179 ? 0.5016 0.2837 0.4468 -0.1118 0.0247  -0.0259 172 LEU A CA  
1319 C C   . LEU A 179 ? 0.4276 0.1824 0.3450 -0.0987 0.0283  -0.0156 172 LEU A C   
1320 O O   . LEU A 179 ? 0.4615 0.2140 0.3672 -0.0805 0.0220  -0.0178 172 LEU A O   
1321 C CB  . LEU A 179 ? 0.4400 0.1950 0.3844 -0.1240 0.0178  -0.0343 172 LEU A CB  
1322 C CG  . LEU A 179 ? 0.4464 0.2281 0.4169 -0.1352 0.0091  -0.0466 172 LEU A CG  
1323 C CD1 . LEU A 179 ? 0.5365 0.2882 0.5054 -0.1499 0.0019  -0.0552 172 LEU A CD1 
1324 C CD2 . LEU A 179 ? 0.4618 0.2649 0.4298 -0.1179 -0.0011 -0.0549 172 LEU A CD2 
1325 N N   . GLN A 180 ? 0.4674 0.2018 0.3743 -0.1079 0.0384  -0.0041 173 GLN A N   
1326 C CA  . GLN A 180 ? 0.4832 0.1863 0.3609 -0.0964 0.0394  0.0064  173 GLN A CA  
1327 C C   . GLN A 180 ? 0.5015 0.2258 0.3734 -0.0815 0.0406  0.0118  173 GLN A C   
1328 O O   . GLN A 180 ? 0.5486 0.2532 0.3993 -0.0675 0.0364  0.0178  173 GLN A O   
1329 C CB  . GLN A 180 ? 0.6161 0.2929 0.4826 -0.1106 0.0490  0.0178  173 GLN A CB  
1330 C CG  . GLN A 180 ? 0.6979 0.4007 0.5785 -0.1251 0.0635  0.0236  173 GLN A CG  
1331 C CD  . GLN A 180 ? 0.8788 0.5997 0.7910 -0.1453 0.0671  0.0176  173 GLN A CD  
1332 O OE1 . GLN A 180 ? 0.6742 0.4071 0.6059 -0.1491 0.0581  0.0051  173 GLN A OE1 
1333 N NE2 . GLN A 180 ? 0.9914 0.7152 0.9082 -0.1577 0.0796  0.0265  173 GLN A NE2 
1334 N N   . ALA A 181 ? 0.4556 0.2189 0.3469 -0.0831 0.0444  0.0088  174 ALA A N   
1335 C CA  . ALA A 181 ? 0.4245 0.2050 0.3097 -0.0721 0.0467  0.0137  174 ALA A CA  
1336 C C   . ALA A 181 ? 0.5483 0.3386 0.4328 -0.0533 0.0356  0.0087  174 ALA A C   
1337 O O   . ALA A 181 ? 0.4182 0.2238 0.3172 -0.0502 0.0296  -0.0008 174 ALA A O   
1338 C CB  . ALA A 181 ? 0.4684 0.2848 0.3759 -0.0799 0.0551  0.0113  174 ALA A CB  
1339 N N   . ASN A 182 ? 0.4734 0.2555 0.3408 -0.0413 0.0330  0.0153  175 ASN A N   
1340 C CA  . ASN A 182 ? 0.4131 0.2097 0.2849 -0.0251 0.0241  0.0110  175 ASN A CA  
1341 C C   . ASN A 182 ? 0.3413 0.1739 0.2310 -0.0249 0.0259  0.0064  175 ASN A C   
1342 O O   . ASN A 182 ? 0.3481 0.1926 0.2410 -0.0324 0.0334  0.0088  175 ASN A O   
1343 C CB  . ASN A 182 ? 0.4734 0.2557 0.3268 -0.0129 0.0186  0.0186  175 ASN A CB  
1344 C CG  . ASN A 182 ? 0.7143 0.4618 0.5525 -0.0060 0.0126  0.0218  175 ASN A CG  
1345 O OD1 . ASN A 182 ? 0.6929 0.4267 0.5346 -0.0090 0.0123  0.0166  175 ASN A OD1 
1346 N ND2 . ASN A 182 ? 0.7066 0.4385 0.5273 0.0041  0.0064  0.0299  175 ASN A ND2 
1347 N N   . PRO A 183 ? 0.3138 0.1629 0.2147 -0.0161 0.0201  -0.0002 176 PRO A N   
1348 C CA  . PRO A 183 ? 0.2603 0.1393 0.1757 -0.0148 0.0210  -0.0033 176 PRO A CA  
1349 C C   . PRO A 183 ? 0.2646 0.1497 0.1743 -0.0083 0.0204  0.0015  176 PRO A C   
1350 O O   . PRO A 183 ? 0.2968 0.1659 0.1919 -0.0032 0.0173  0.0067  176 PRO A O   
1351 C CB  . PRO A 183 ? 0.2966 0.1846 0.2197 -0.0075 0.0155  -0.0103 176 PRO A CB  
1352 C CG  . PRO A 183 ? 0.3097 0.1771 0.2223 0.0008  0.0118  -0.0099 176 PRO A CG  
1353 C CD  . PRO A 183 ? 0.3468 0.1865 0.2462 -0.0062 0.0137  -0.0049 176 PRO A CD  
1354 N N   . THR A 184 ? 0.2501 0.1572 0.1707 -0.0084 0.0221  -0.0007 177 THR A N   
1355 C CA  . THR A 184 ? 0.2282 0.1414 0.1446 -0.0030 0.0205  0.0018  177 THR A CA  
1356 C C   . THR A 184 ? 0.2514 0.1674 0.1708 0.0070  0.0125  0.0011  177 THR A C   
1357 O O   . THR A 184 ? 0.2327 0.1568 0.1623 0.0101  0.0112  -0.0029 177 THR A O   
1358 C CB  . THR A 184 ? 0.2424 0.1758 0.1711 -0.0052 0.0242  -0.0012 177 THR A CB  
1359 O OG1 . THR A 184 ? 0.2423 0.1778 0.1747 -0.0139 0.0324  -0.0016 177 THR A OG1 
1360 C CG2 . THR A 184 ? 0.2407 0.1757 0.1625 -0.0013 0.0228  0.0003  177 THR A CG2 
1361 N N   . ILE A 185 ? 0.2571 0.1664 0.1671 0.0121  0.0074  0.0049  178 ILE A N   
1362 C CA  . ILE A 185 ? 0.2687 0.1819 0.1852 0.0217  -0.0006 0.0047  178 ILE A CA  
1363 C C   . ILE A 185 ? 0.2390 0.1641 0.1591 0.0234  -0.0054 0.0050  178 ILE A C   
1364 O O   . ILE A 185 ? 0.2529 0.1687 0.1577 0.0215  -0.0075 0.0076  178 ILE A O   
1365 C CB  . ILE A 185 ? 0.2903 0.1823 0.1940 0.0278  -0.0065 0.0089  178 ILE A CB  
1366 C CG1 . ILE A 185 ? 0.3621 0.2358 0.2594 0.0252  -0.0025 0.0086  178 ILE A CG1 
1367 C CG2 . ILE A 185 ? 0.3096 0.2112 0.2262 0.0390  -0.0148 0.0080  178 ILE A CG2 
1368 C CD1 . ILE A 185 ? 0.3670 0.2496 0.2781 0.0277  -0.0003 0.0020  178 ILE A CD1 
1369 N N   . ILE A 186 ? 0.2405 0.1838 0.1788 0.0264  -0.0069 0.0022  179 ILE A N   
1370 C CA  . ILE A 186 ? 0.1984 0.1531 0.1447 0.0274  -0.0129 0.0019  179 ILE A CA  
1371 C C   . ILE A 186 ? 0.2076 0.1712 0.1691 0.0355  -0.0190 0.0020  179 ILE A C   
1372 O O   . ILE A 186 ? 0.2295 0.2042 0.2053 0.0382  -0.0139 -0.0002 179 ILE A O   
1373 C CB  . ILE A 186 ? 0.2154 0.1841 0.1728 0.0226  -0.0079 -0.0005 179 ILE A CB  
1374 C CG1 . ILE A 186 ? 0.2394 0.2024 0.1869 0.0169  -0.0010 -0.0013 179 ILE A CG1 
1375 C CG2 . ILE A 186 ? 0.2029 0.1787 0.1670 0.0215  -0.0148 -0.0010 179 ILE A CG2 
1376 C CD1 . ILE A 186 ? 0.2613 0.2121 0.1912 0.0143  -0.0018 -0.0007 179 ILE A CD1 
1377 N N   . GLU A 187 ? 0.2103 0.1693 0.1685 0.0402  -0.0299 0.0041  180 GLU A N   
1378 C CA  . GLU A 187 ? 0.2241 0.1930 0.2002 0.0499  -0.0365 0.0040  180 GLU A CA  
1379 C C   . GLU A 187 ? 0.2304 0.2254 0.2338 0.0486  -0.0384 0.0016  180 GLU A C   
1380 O O   . GLU A 187 ? 0.2194 0.2207 0.2248 0.0401  -0.0355 0.0004  180 GLU A O   
1381 C CB  . GLU A 187 ? 0.2532 0.2063 0.2153 0.0567  -0.0494 0.0080  180 GLU A CB  
1382 C CG  . GLU A 187 ? 0.2768 0.2032 0.2166 0.0593  -0.0459 0.0113  180 GLU A CG  
1383 C CD  . GLU A 187 ? 0.3470 0.2546 0.2721 0.0683  -0.0591 0.0168  180 GLU A CD  
1384 O OE1 . GLU A 187 ? 0.3252 0.2399 0.2535 0.0720  -0.0729 0.0178  180 GLU A OE1 
1385 O OE2 . GLU A 187 ? 0.4033 0.2872 0.3130 0.0719  -0.0571 0.0201  180 GLU A OE2 
1386 N N   . ASP A 188 ? 0.2207 0.2310 0.2471 0.0572  -0.0426 0.0009  181 ASP A N   
1387 C CA  . ASP A 188 ? 0.2264 0.2644 0.2837 0.0547  -0.0414 -0.0011 181 ASP A CA  
1388 C C   . ASP A 188 ? 0.2034 0.2460 0.2631 0.0460  -0.0514 -0.0013 181 ASP A C   
1389 O O   . ASP A 188 ? 0.2124 0.2425 0.2566 0.0469  -0.0650 -0.0005 181 ASP A O   
1390 C CB  . ASP A 188 ? 0.2017 0.2579 0.2869 0.0665  -0.0462 -0.0020 181 ASP A CB  
1391 C CG  . ASP A 188 ? 0.2576 0.3122 0.3450 0.0760  -0.0343 -0.0039 181 ASP A CG  
1392 O OD1 . ASP A 188 ? 0.2270 0.2685 0.2959 0.0721  -0.0230 -0.0048 181 ASP A OD1 
1393 O OD2 . ASP A 188 ? 0.2765 0.3433 0.3852 0.0882  -0.0371 -0.0054 181 ASP A OD2 
1394 N N   . ASN A 189 ? 0.1898 0.2483 0.2671 0.0374  -0.0448 -0.0025 182 ASN A N   
1395 C CA  A ASN A 189 ? 0.1991 0.2659 0.2877 0.0281  -0.0534 -0.0040 182 ASN A CA  
1396 C CA  B ASN A 189 ? 0.1981 0.2647 0.2866 0.0285  -0.0541 -0.0040 182 ASN A CA  
1397 C C   . ASN A 189 ? 0.2598 0.3034 0.3181 0.0218  -0.0587 -0.0050 182 ASN A C   
1398 O O   . ASN A 189 ? 0.3091 0.3525 0.3688 0.0161  -0.0704 -0.0076 182 ASN A O   
1399 C CB  A ASN A 189 ? 0.1984 0.2827 0.3119 0.0323  -0.0693 -0.0053 182 ASN A CB  
1400 C CB  B ASN A 189 ? 0.2068 0.2882 0.3164 0.0335  -0.0713 -0.0052 182 ASN A CB  
1401 C CG  A ASN A 189 ? 0.2052 0.3064 0.3433 0.0207  -0.0751 -0.0076 182 ASN A CG  
1402 C CG  B ASN A 189 ? 0.2196 0.3292 0.3666 0.0405  -0.0665 -0.0052 182 ASN A CG  
1403 O OD1 A ASN A 189 ? 0.2708 0.3788 0.4195 0.0115  -0.0625 -0.0071 182 ASN A OD1 
1404 O OD1 B ASN A 189 ? 0.3489 0.4628 0.5038 0.0531  -0.0744 -0.0050 182 ASN A OD1 
1405 N ND2 A ASN A 189 ? 0.2918 0.3980 0.4378 0.0205  -0.0950 -0.0101 182 ASN A ND2 
1406 N ND2 B ASN A 189 ? 0.1937 0.3220 0.3637 0.0331  -0.0530 -0.0053 182 ASN A ND2 
1407 N N   . CYS A 190 ? 0.1685 0.2717 0.2236 0.0024  0.0275  -0.0330 183 CYS A N   
1408 C CA  . CYS A 190 ? 0.1639 0.2423 0.2084 -0.0019 0.0199  -0.0243 183 CYS A CA  
1409 C C   . CYS A 190 ? 0.1976 0.2641 0.2271 -0.0182 0.0243  -0.0181 183 CYS A C   
1410 O O   . CYS A 190 ? 0.2193 0.2864 0.2391 -0.0255 0.0318  -0.0179 183 CYS A O   
1411 C CB  . CYS A 190 ? 0.1868 0.2388 0.2190 0.0071  0.0147  -0.0210 183 CYS A CB  
1412 S SG  . CYS A 190 ? 0.2252 0.2756 0.2662 0.0248  0.0073  -0.0250 183 CYS A SG  
1413 N N   . PHE A 191 ? 0.2026 0.2547 0.2269 -0.0235 0.0198  -0.0130 184 PHE A N   
1414 C CA  . PHE A 191 ? 0.2025 0.2310 0.2072 -0.0344 0.0225  -0.0057 184 PHE A CA  
1415 C C   . PHE A 191 ? 0.2072 0.2108 0.2023 -0.0248 0.0164  0.0005  184 PHE A C   
1416 O O   . PHE A 191 ? 0.2047 0.2060 0.2056 -0.0189 0.0107  -0.0005 184 PHE A O   
1417 C CB  . PHE A 191 ? 0.2275 0.2562 0.2305 -0.0493 0.0241  -0.0065 184 PHE A CB  
1418 C CG  . PHE A 191 ? 0.2858 0.2791 0.2634 -0.0583 0.0267  0.0013  184 PHE A CG  
1419 C CD1 . PHE A 191 ? 0.2931 0.2592 0.2607 -0.0516 0.0220  0.0053  184 PHE A CD1 
1420 C CD2 . PHE A 191 ? 0.3536 0.3387 0.3152 -0.0721 0.0343  0.0047  184 PHE A CD2 
1421 C CE1 . PHE A 191 ? 0.3316 0.2618 0.2747 -0.0555 0.0247  0.0121  184 PHE A CE1 
1422 C CE2 . PHE A 191 ? 0.3821 0.3277 0.3162 -0.0779 0.0360  0.0131  184 PHE A CE2 
1423 C CZ  . PHE A 191 ? 0.3305 0.2482 0.2561 -0.0678 0.0310  0.0166  184 PHE A CZ  
1424 N N   . ILE A 192 ? 0.1925 0.1810 0.1730 -0.0231 0.0175  0.0071  185 ILE A N   
1425 C CA  . ILE A 192 ? 0.2288 0.2019 0.2031 -0.0134 0.0122  0.0130  185 ILE A CA  
1426 C C   . ILE A 192 ? 0.2210 0.1700 0.1774 -0.0158 0.0141  0.0210  185 ILE A C   
1427 O O   . ILE A 192 ? 0.2427 0.1846 0.1854 -0.0198 0.0168  0.0264  185 ILE A O   
1428 C CB  . ILE A 192 ? 0.2088 0.1885 0.1823 -0.0074 0.0099  0.0140  185 ILE A CB  
1429 C CG1 . ILE A 192 ? 0.2238 0.2186 0.2085 -0.0052 0.0098  0.0055  185 ILE A CG1 
1430 C CG2 . ILE A 192 ? 0.2338 0.2076 0.2058 0.0011  0.0045  0.0190  185 ILE A CG2 
1431 C CD1 . ILE A 192 ? 0.2608 0.2569 0.2564 0.0007  0.0052  0.0018  185 ILE A CD1 
1432 N N   . GLY A 193 ? 0.2430 0.1762 0.1962 -0.0131 0.0129  0.0216  186 GLY A N   
1433 C CA  . GLY A 193 ? 0.2787 0.1815 0.2117 -0.0139 0.0156  0.0279  186 GLY A CA  
1434 C C   . GLY A 193 ? 0.2568 0.1499 0.1806 0.0000  0.0130  0.0372  186 GLY A C   
1435 O O   . GLY A 193 ? 0.2677 0.1799 0.2029 0.0094  0.0085  0.0378  186 GLY A O   
1436 N N   . ALA A 194 ? 0.2909 0.1529 0.1922 0.0007  0.0154  0.0447  187 ALA A N   
1437 C CA  . ALA A 194 ? 0.3076 0.1607 0.1977 0.0150  0.0119  0.0557  187 ALA A CA  
1438 C C   . ALA A 194 ? 0.3036 0.1713 0.2080 0.0336  0.0075  0.0559  187 ALA A C   
1439 O O   . ALA A 194 ? 0.3058 0.1688 0.2160 0.0378  0.0094  0.0501  187 ALA A O   
1440 C CB  . ALA A 194 ? 0.3729 0.1809 0.2330 0.0159  0.0152  0.0639  187 ALA A CB  
1441 N N   . ARG A 195 ? 0.2875 0.1750 0.1961 0.0431  0.0017  0.0626  188 ARG A N   
1442 C CA  . ARG A 195 ? 0.2756 0.1863 0.1989 0.0593  -0.0029 0.0642  188 ARG A CA  
1443 C C   . ARG A 195 ? 0.3092 0.2484 0.2540 0.0534  -0.0033 0.0545  188 ARG A C   
1444 O O   . ARG A 195 ? 0.3613 0.3234 0.3186 0.0626  -0.0060 0.0547  188 ARG A O   
1445 C CB  . ARG A 195 ? 0.3871 0.2765 0.3043 0.0776  -0.0004 0.0668  188 ARG A CB  
1446 C CG  . ARG A 195 ? 0.5297 0.3779 0.4199 0.0856  0.0009  0.0764  188 ARG A CG  
1447 C CD  . ARG A 195 ? 0.6512 0.5085 0.5338 0.0950  -0.0069 0.0896  188 ARG A CD  
1448 N NE  . ARG A 195 ? 0.7232 0.5482 0.5787 0.0816  -0.0053 0.0958  188 ARG A NE  
1449 C CZ  . ARG A 195 ? 0.6807 0.5028 0.5199 0.0843  -0.0112 0.1081  188 ARG A CZ  
1450 N NH1 . ARG A 195 ? 0.7548 0.6076 0.6043 0.1003  -0.0206 0.1153  188 ARG A NH1 
1451 N NH2 . ARG A 195 ? 0.5756 0.3681 0.3885 0.0676  -0.0076 0.1123  188 ARG A NH2 
1452 N N   . SER A 196 ? 0.2569 0.1963 0.2057 0.0389  -0.0008 0.0464  189 SER A N   
1453 C CA  . SER A 196 ? 0.2364 0.1964 0.2005 0.0345  -0.0022 0.0390  189 SER A CA  
1454 C C   . SER A 196 ? 0.2056 0.1907 0.1754 0.0320  -0.0070 0.0401  189 SER A C   
1455 O O   . SER A 196 ? 0.2311 0.2197 0.1934 0.0307  -0.0093 0.0451  189 SER A O   
1456 C CB  . SER A 196 ? 0.2504 0.2052 0.2169 0.0230  0.0002  0.0312  189 SER A CB  
1457 O OG  . SER A 196 ? 0.2958 0.2321 0.2577 0.0227  0.0034  0.0287  189 SER A OG  
1458 N N   . GLU A 197 ? 0.1872 0.1877 0.1668 0.0295  -0.0085 0.0356  190 GLU A N   
1459 C CA  . GLU A 197 ? 0.2201 0.2415 0.2020 0.0231  -0.0127 0.0351  190 GLU A CA  
1460 C C   . GLU A 197 ? 0.2116 0.2300 0.1956 0.0141  -0.0120 0.0273  190 GLU A C   
1461 O O   . GLU A 197 ? 0.2306 0.2439 0.2184 0.0156  -0.0104 0.0248  190 GLU A O   
1462 C CB  . GLU A 197 ? 0.2805 0.3270 0.2696 0.0298  -0.0161 0.0401  190 GLU A CB  
1463 C CG  . GLU A 197 ? 0.4594 0.5308 0.4486 0.0195  -0.0215 0.0400  190 GLU A CG  
1464 C CD  . GLU A 197 ? 0.2907 0.3706 0.2721 0.0207  -0.0266 0.0466  190 GLU A CD  
1465 O OE1 . GLU A 197 ? 0.4010 0.4713 0.3780 0.0329  -0.0269 0.0540  190 GLU A OE1 
1466 O OE2 . GLU A 197 ? 0.5209 0.6147 0.4967 0.0082  -0.0307 0.0446  190 GLU A OE2 
1467 N N   . VAL A 198 ? 0.1910 0.2083 0.1694 0.0056  -0.0130 0.0233  191 VAL A N   
1468 C CA  . VAL A 198 ? 0.1792 0.1875 0.1551 -0.0010 -0.0129 0.0165  191 VAL A CA  
1469 C C   . VAL A 198 ? 0.1701 0.1865 0.1376 -0.0113 -0.0156 0.0148  191 VAL A C   
1470 O O   . VAL A 198 ? 0.1770 0.1962 0.1375 -0.0144 -0.0159 0.0144  191 VAL A O   
1471 C CB  . VAL A 198 ? 0.2094 0.2027 0.1841 0.0006  -0.0101 0.0111  191 VAL A CB  
1472 C CG1 . VAL A 198 ? 0.2042 0.1845 0.1747 -0.0015 -0.0110 0.0054  191 VAL A CG1 
1473 C CG2 . VAL A 198 ? 0.2255 0.2149 0.2070 0.0066  -0.0079 0.0127  191 VAL A CG2 
1474 N N   . VAL A 199 ? 0.1857 0.2069 0.1516 -0.0189 -0.0173 0.0140  192 VAL A N   
1475 C CA  . VAL A 199 ? 0.1842 0.2176 0.1416 -0.0327 -0.0203 0.0128  192 VAL A CA  
1476 C C   . VAL A 199 ? 0.2013 0.2146 0.1453 -0.0449 -0.0196 0.0072  192 VAL A C   
1477 O O   . VAL A 199 ? 0.2130 0.2061 0.1556 -0.0406 -0.0179 0.0061  192 VAL A O   
1478 C CB  . VAL A 199 ? 0.1779 0.2475 0.1466 -0.0333 -0.0235 0.0191  192 VAL A CB  
1479 C CG1 . VAL A 199 ? 0.1963 0.2781 0.1738 -0.0183 -0.0247 0.0260  192 VAL A CG1 
1480 C CG2 . VAL A 199 ? 0.2031 0.2790 0.1797 -0.0331 -0.0211 0.0197  192 VAL A CG2 
1481 N N   . GLU A 200 ? 0.2205 0.2374 0.1511 -0.0614 -0.0217 0.0042  193 GLU A N   
1482 C CA  . GLU A 200 ? 0.2555 0.2548 0.1691 -0.0783 -0.0214 0.0004  193 GLU A CA  
1483 C C   . GLU A 200 ? 0.3055 0.2585 0.2030 -0.0734 -0.0188 -0.0048 193 GLU A C   
1484 O O   . GLU A 200 ? 0.3109 0.2416 0.1963 -0.0795 -0.0184 -0.0047 193 GLU A O   
1485 C CB  . GLU A 200 ? 0.2958 0.3154 0.2196 -0.0825 -0.0210 0.0052  193 GLU A CB  
1486 C CG  . GLU A 200 ? 0.5077 0.5293 0.4161 -0.1077 -0.0212 0.0032  193 GLU A CG  
1487 C CD  . GLU A 200 ? 0.6089 0.6420 0.5231 -0.1118 -0.0182 0.0069  193 GLU A CD  
1488 O OE1 . GLU A 200 ? 0.4542 0.4723 0.3479 -0.1340 -0.0167 0.0052  193 GLU A OE1 
1489 O OE2 . GLU A 200 ? 0.3205 0.3745 0.2558 -0.0950 -0.0165 0.0109  193 GLU A OE2 
1490 N N   . GLY A 201 ? 0.2694 0.2083 0.1655 -0.0620 -0.0169 -0.0090 194 GLY A N   
1491 C CA  . GLY A 201 ? 0.2999 0.1991 0.1818 -0.0545 -0.0145 -0.0148 194 GLY A CA  
1492 C C   . GLY A 201 ? 0.2756 0.1674 0.1695 -0.0382 -0.0150 -0.0113 194 GLY A C   
1493 O O   . GLY A 201 ? 0.3120 0.1719 0.1939 -0.0309 -0.0151 -0.0142 194 GLY A O   
1494 N N   . VAL A 202 ? 0.2394 0.1580 0.1543 -0.0320 -0.0160 -0.0052 195 VAL A N   
1495 C CA  . VAL A 202 ? 0.2387 0.1539 0.1649 -0.0177 -0.0167 -0.0031 195 VAL A CA  
1496 C C   . VAL A 202 ? 0.2650 0.1741 0.1957 -0.0050 -0.0146 -0.0085 195 VAL A C   
1497 O O   . VAL A 202 ? 0.2394 0.1576 0.1712 -0.0060 -0.0113 -0.0120 195 VAL A O   
1498 C CB  . VAL A 202 ? 0.2403 0.1828 0.1849 -0.0146 -0.0166 0.0024  195 VAL A CB  
1499 C CG1 . VAL A 202 ? 0.2421 0.1832 0.1973 -0.0024 -0.0172 0.0031  195 VAL A CG1 
1500 C CG2 . VAL A 202 ? 0.2416 0.1921 0.1827 -0.0249 -0.0172 0.0064  195 VAL A CG2 
1501 N N   . VAL A 203 ? 0.2571 0.1520 0.1888 0.0068  -0.0166 -0.0092 196 VAL A N   
1502 C CA  . VAL A 203 ? 0.2462 0.1436 0.1873 0.0212  -0.0145 -0.0145 196 VAL A CA  
1503 C C   . VAL A 203 ? 0.2353 0.1562 0.1975 0.0278  -0.0163 -0.0112 196 VAL A C   
1504 O O   . VAL A 203 ? 0.2547 0.1723 0.2176 0.0298  -0.0215 -0.0067 196 VAL A O   
1505 C CB  . VAL A 203 ? 0.2808 0.1475 0.2080 0.0323  -0.0164 -0.0182 196 VAL A CB  
1506 C CG1 . VAL A 203 ? 0.2996 0.1788 0.2421 0.0502  -0.0137 -0.0243 196 VAL A CG1 
1507 C CG2 . VAL A 203 ? 0.3269 0.1630 0.2276 0.0231  -0.0139 -0.0227 196 VAL A CG2 
1508 N N   . VAL A 204 ? 0.2137 0.1562 0.1896 0.0292  -0.0118 -0.0138 197 VAL A N   
1509 C CA  . VAL A 204 ? 0.1938 0.1569 0.1871 0.0328  -0.0125 -0.0126 197 VAL A CA  
1510 C C   . VAL A 204 ? 0.2108 0.1844 0.2149 0.0449  -0.0108 -0.0192 197 VAL A C   
1511 O O   . VAL A 204 ? 0.2031 0.1848 0.2092 0.0457  -0.0038 -0.0250 197 VAL A O   
1512 C CB  . VAL A 204 ? 0.1732 0.1514 0.1716 0.0238  -0.0082 -0.0101 197 VAL A CB  
1513 C CG1 . VAL A 204 ? 0.2014 0.1956 0.2131 0.0237  -0.0085 -0.0097 197 VAL A CG1 
1514 C CG2 . VAL A 204 ? 0.2030 0.1748 0.1931 0.0165  -0.0098 -0.0039 197 VAL A CG2 
1515 N N   . GLU A 205 ? 0.2075 0.1828 0.2182 0.0553  -0.0173 -0.0184 198 GLU A N   
1516 C CA  . GLU A 205 ? 0.2080 0.1971 0.2311 0.0710  -0.0167 -0.0245 198 GLU A CA  
1517 C C   . GLU A 205 ? 0.2046 0.2332 0.2503 0.0674  -0.0123 -0.0279 198 GLU A C   
1518 O O   . GLU A 205 ? 0.1929 0.2314 0.2415 0.0534  -0.0119 -0.0243 198 GLU A O   
1519 C CB  . GLU A 205 ? 0.2470 0.2270 0.2690 0.0850  -0.0270 -0.0211 198 GLU A CB  
1520 C CG  . GLU A 205 ? 0.2646 0.2004 0.2598 0.0877  -0.0304 -0.0179 198 GLU A CG  
1521 C CD  . GLU A 205 ? 0.4122 0.3340 0.4018 0.1035  -0.0411 -0.0132 198 GLU A CD  
1522 O OE1 . GLU A 205 ? 0.3573 0.3084 0.3656 0.1114  -0.0474 -0.0117 198 GLU A OE1 
1523 O OE2 . GLU A 205 ? 0.4393 0.3198 0.4035 0.1072  -0.0436 -0.0107 198 GLU A OE2 
1524 N N   . GLU A 206 ? 0.1974 0.2473 0.2575 0.0804  -0.0085 -0.0353 199 GLU A N   
1525 C CA  . GLU A 206 ? 0.1861 0.2760 0.2660 0.0744  -0.0010 -0.0405 199 GLU A CA  
1526 C C   . GLU A 206 ? 0.1865 0.3013 0.2798 0.0636  -0.0066 -0.0364 199 GLU A C   
1527 O O   . GLU A 206 ? 0.1835 0.2964 0.2784 0.0687  -0.0175 -0.0320 199 GLU A O   
1528 C CB  . GLU A 206 ? 0.2077 0.3224 0.3043 0.0939  0.0036  -0.0499 199 GLU A CB  
1529 C CG  . GLU A 206 ? 0.2653 0.3853 0.3721 0.1159  -0.0071 -0.0488 199 GLU A CG  
1530 C CD  . GLU A 206 ? 0.4232 0.5748 0.5507 0.1385  -0.0016 -0.0588 199 GLU A CD  
1531 O OE1 . GLU A 206 ? 0.5837 0.7657 0.7320 0.1542  -0.0102 -0.0581 199 GLU A OE1 
1532 O OE2 . GLU A 206 ? 0.4921 0.6409 0.6151 0.1411  0.0113  -0.0676 199 GLU A OE2 
1533 N N   . ASN A 207 ? 0.1676 0.3027 0.2664 0.0465  0.0011  -0.0380 200 ASN A N   
1534 C CA  . ASN A 207 ? 0.1554 0.3136 0.2638 0.0313  -0.0014 -0.0364 200 ASN A CA  
1535 C C   . ASN A 207 ? 0.1899 0.3188 0.2810 0.0199  -0.0074 -0.0287 200 ASN A C   
1536 O O   . ASN A 207 ? 0.2002 0.3410 0.2945 0.0074  -0.0106 -0.0280 200 ASN A O   
1537 C CB  . ASN A 207 ? 0.1563 0.3537 0.2888 0.0419  -0.0090 -0.0397 200 ASN A CB  
1538 C CG  . ASN A 207 ? 0.2224 0.4583 0.3764 0.0532  -0.0013 -0.0486 200 ASN A CG  
1539 O OD1 . ASN A 207 ? 0.2406 0.4894 0.3957 0.0415  0.0113  -0.0532 200 ASN A OD1 
1540 N ND2 . ASN A 207 ? 0.2804 0.5350 0.4505 0.0773  -0.0083 -0.0511 200 ASN A ND2 
1541 N N   . SER A 208 ? 0.1691 0.2618 0.2415 0.0226  -0.0081 -0.0239 201 SER A N   
1542 C CA  . SER A 208 ? 0.1796 0.2489 0.2377 0.0145  -0.0123 -0.0179 201 SER A CA  
1543 C C   . SER A 208 ? 0.1659 0.2260 0.2139 -0.0012 -0.0050 -0.0157 201 SER A C   
1544 O O   . SER A 208 ? 0.1735 0.2377 0.2202 -0.0059 0.0028  -0.0169 201 SER A O   
1545 C CB  . SER A 208 ? 0.1851 0.2253 0.2289 0.0225  -0.0154 -0.0138 201 SER A CB  
1546 O OG  . SER A 208 ? 0.2158 0.2548 0.2623 0.0361  -0.0227 -0.0142 201 SER A OG  
1547 N N   . VAL A 209 ? 0.1879 0.2310 0.2250 -0.0083 -0.0076 -0.0123 202 VAL A N   
1548 C CA  . VAL A 209 ? 0.1765 0.2023 0.1994 -0.0208 -0.0017 -0.0095 202 VAL A CA  
1549 C C   . VAL A 209 ? 0.2193 0.2173 0.2278 -0.0158 -0.0034 -0.0047 202 VAL A C   
1550 O O   . VAL A 209 ? 0.2381 0.2314 0.2442 -0.0146 -0.0084 -0.0052 202 VAL A O   
1551 C CB  . VAL A 209 ? 0.2446 0.2792 0.2676 -0.0367 -0.0012 -0.0127 202 VAL A CB  
1552 C CG1 . VAL A 209 ? 0.2894 0.2928 0.2902 -0.0486 0.0050  -0.0093 202 VAL A CG1 
1553 C CG2 . VAL A 209 ? 0.2693 0.3410 0.3103 -0.0430 0.0017  -0.0181 202 VAL A CG2 
1554 N N   . LEU A 210 ? 0.2024 0.1860 0.2018 -0.0125 0.0004  0.0000  203 LEU A N   
1555 C CA  . LEU A 210 ? 0.1889 0.1524 0.1771 -0.0069 0.0002  0.0045  203 LEU A CA  
1556 C C   . LEU A 210 ? 0.2447 0.1864 0.2175 -0.0126 0.0053  0.0074  203 LEU A C   
1557 O O   . LEU A 210 ? 0.2461 0.1842 0.2130 -0.0174 0.0093  0.0102  203 LEU A O   
1558 C CB  . LEU A 210 ? 0.1928 0.1583 0.1814 0.0013  -0.0004 0.0082  203 LEU A CB  
1559 C CG  . LEU A 210 ? 0.2440 0.2159 0.2380 0.0069  -0.0051 0.0067  203 LEU A CG  
1560 C CD1 . LEU A 210 ? 0.2480 0.2314 0.2512 0.0072  -0.0079 0.0018  203 LEU A CD1 
1561 C CD2 . LEU A 210 ? 0.2555 0.2297 0.2472 0.0101  -0.0053 0.0096  203 LEU A CD2 
1562 N N   . ALA A 211 ? 0.2260 0.1499 0.1889 -0.0121 0.0056  0.0066  204 ALA A N   
1563 C CA  . ALA A 211 ? 0.2412 0.1348 0.1844 -0.0139 0.0109  0.0093  204 ALA A CA  
1564 C C   . ALA A 211 ? 0.2789 0.1640 0.2173 0.0000  0.0121  0.0170  204 ALA A C   
1565 O O   . ALA A 211 ? 0.2921 0.1973 0.2426 0.0081  0.0089  0.0192  204 ALA A O   
1566 C CB  . ALA A 211 ? 0.3221 0.1969 0.2540 -0.0146 0.0119  0.0048  204 ALA A CB  
1567 N N   . MET A 212 ? 0.3418 0.1958 0.2604 0.0025  0.0163  0.0213  205 MET A N   
1568 C CA  . MET A 212 ? 0.3279 0.1750 0.2417 0.0192  0.0161  0.0295  205 MET A CA  
1569 C C   . MET A 212 ? 0.3229 0.1850 0.2483 0.0338  0.0147  0.0280  205 MET A C   
1570 O O   . MET A 212 ? 0.3144 0.1708 0.2385 0.0334  0.0168  0.0215  205 MET A O   
1571 C CB  . MET A 212 ? 0.3399 0.1438 0.2268 0.0229  0.0208  0.0344  205 MET A CB  
1572 C CG  . MET A 212 ? 0.4004 0.1868 0.2712 0.0057  0.0233  0.0373  205 MET A CG  
1573 S SD  . MET A 212 ? 0.5017 0.2301 0.3347 0.0126  0.0276  0.0469  205 MET A SD  
1574 C CE  . MET A 212 ? 0.4538 0.1478 0.2711 0.0060  0.0335  0.0358  205 MET A CE  
1575 N N   . GLY A 213 ? 0.3088 0.1913 0.2438 0.0453  0.0114  0.0339  206 GLY A N   
1576 C CA  . GLY A 213 ? 0.3176 0.2168 0.2627 0.0587  0.0113  0.0333  206 GLY A CA  
1577 C C   . GLY A 213 ? 0.2779 0.2023 0.2376 0.0517  0.0095  0.0271  206 GLY A C   
1578 O O   . GLY A 213 ? 0.3079 0.2412 0.2719 0.0585  0.0120  0.0243  206 GLY A O   
1579 N N   . VAL A 214 ? 0.2568 0.1905 0.2222 0.0388  0.0061  0.0246  207 VAL A N   
1580 C CA  . VAL A 214 ? 0.2074 0.1591 0.1824 0.0330  0.0032  0.0205  207 VAL A CA  
1581 C C   . VAL A 214 ? 0.2612 0.2361 0.2446 0.0341  -0.0001 0.0239  207 VAL A C   
1582 O O   . VAL A 214 ? 0.2520 0.2304 0.2350 0.0316  -0.0023 0.0266  207 VAL A O   
1583 C CB  . VAL A 214 ? 0.2003 0.1496 0.1766 0.0221  0.0007  0.0161  207 VAL A CB  
1584 C CG1 . VAL A 214 ? 0.2585 0.2203 0.2408 0.0187  -0.0032 0.0139  207 VAL A CG1 
1585 C CG2 . VAL A 214 ? 0.2460 0.1783 0.2143 0.0175  0.0028  0.0120  207 VAL A CG2 
1586 N N   . PHE A 215 ? 0.2158 0.2071 0.2047 0.0352  0.0000  0.0232  208 PHE A N   
1587 C CA  . PHE A 215 ? 0.1986 0.2142 0.1940 0.0321  -0.0033 0.0256  208 PHE A CA  
1588 C C   . PHE A 215 ? 0.2421 0.2591 0.2360 0.0202  -0.0047 0.0215  208 PHE A C   
1589 O O   . PHE A 215 ? 0.2923 0.3083 0.2844 0.0187  -0.0022 0.0192  208 PHE A O   
1590 C CB  . PHE A 215 ? 0.2390 0.2777 0.2421 0.0422  -0.0015 0.0289  208 PHE A CB  
1591 C CG  . PHE A 215 ? 0.2648 0.2943 0.2656 0.0584  0.0000  0.0337  208 PHE A CG  
1592 C CD1 . PHE A 215 ? 0.3049 0.3221 0.2987 0.0597  -0.0031 0.0387  208 PHE A CD1 
1593 C CD2 . PHE A 215 ? 0.3433 0.3715 0.3451 0.0723  0.0056  0.0329  208 PHE A CD2 
1594 C CE1 . PHE A 215 ? 0.3471 0.3475 0.3328 0.0743  -0.0019 0.0446  208 PHE A CE1 
1595 C CE2 . PHE A 215 ? 0.3176 0.3286 0.3126 0.0891  0.0072  0.0375  208 PHE A CE2 
1596 C CZ  . PHE A 215 ? 0.3012 0.2969 0.2872 0.0899  0.0030  0.0441  208 PHE A CZ  
1597 N N   . LEU A 216 ? 0.1906 0.2062 0.1816 0.0120  -0.0083 0.0205  209 LEU A N   
1598 C CA  . LEU A 216 ? 0.1852 0.1924 0.1694 0.0021  -0.0101 0.0172  209 LEU A CA  
1599 C C   . LEU A 216 ? 0.2151 0.2335 0.1956 -0.0083 -0.0122 0.0172  209 LEU A C   
1600 O O   . LEU A 216 ? 0.1875 0.2076 0.1664 -0.0098 -0.0140 0.0170  209 LEU A O   
1601 C CB  . LEU A 216 ? 0.1938 0.1809 0.1739 0.0027  -0.0119 0.0140  209 LEU A CB  
1602 C CG  . LEU A 216 ? 0.2257 0.2036 0.2083 0.0084  -0.0112 0.0129  209 LEU A CG  
1603 C CD1 . LEU A 216 ? 0.2567 0.2263 0.2400 0.0095  -0.0135 0.0097  209 LEU A CD1 
1604 C CD2 . LEU A 216 ? 0.2869 0.2605 0.2648 0.0070  -0.0111 0.0127  209 LEU A CD2 
1605 N N   . SER A 217 ? 0.1998 0.2242 0.1759 -0.0181 -0.0116 0.0169  210 SER A N   
1606 C CA  . SER A 217 ? 0.1862 0.2152 0.1534 -0.0338 -0.0134 0.0157  210 SER A CA  
1607 C C   . SER A 217 ? 0.2030 0.2044 0.1532 -0.0430 -0.0133 0.0140  210 SER A C   
1608 O O   . SER A 217 ? 0.2238 0.2080 0.1719 -0.0353 -0.0131 0.0143  210 SER A O   
1609 C CB  . SER A 217 ? 0.2449 0.3127 0.2219 -0.0400 -0.0123 0.0179  210 SER A CB  
1610 O OG  . SER A 217 ? 0.2625 0.3372 0.2393 -0.0446 -0.0080 0.0179  210 SER A OG  
1611 N N   . GLN A 218 ? 0.2348 0.2301 0.1699 -0.0605 -0.0140 0.0126  211 GLN A N   
1612 C CA  . GLN A 218 ? 0.2565 0.2188 0.1698 -0.0697 -0.0143 0.0125  211 GLN A CA  
1613 C C   . GLN A 218 ? 0.2627 0.2353 0.1765 -0.0732 -0.0109 0.0155  211 GLN A C   
1614 O O   . GLN A 218 ? 0.3067 0.2499 0.2024 -0.0762 -0.0118 0.0172  211 GLN A O   
1615 C CB  . GLN A 218 ? 0.3133 0.2599 0.2042 -0.0909 -0.0149 0.0101  211 GLN A CB  
1616 C CG  . GLN A 218 ? 0.3111 0.2359 0.1932 -0.0879 -0.0171 0.0053  211 GLN A CG  
1617 C CD  . GLN A 218 ? 0.3662 0.2489 0.2371 -0.0727 -0.0188 0.0039  211 GLN A CD  
1618 O OE1 . GLN A 218 ? 0.3728 0.2340 0.2339 -0.0699 -0.0201 0.0073  211 GLN A OE1 
1619 N NE2 . GLN A 218 ? 0.3560 0.2297 0.2282 -0.0627 -0.0189 -0.0009 211 GLN A NE2 
1620 N N   . SER A 219 ? 0.2240 0.2370 0.1563 -0.0721 -0.0069 0.0162  212 SER A N   
1621 C CA  . SER A 219 ? 0.2256 0.2509 0.1575 -0.0759 -0.0014 0.0174  212 SER A CA  
1622 C C   . SER A 219 ? 0.2452 0.2726 0.1887 -0.0566 0.0008  0.0172  212 SER A C   
1623 O O   . SER A 219 ? 0.2656 0.3026 0.2075 -0.0583 0.0065  0.0168  212 SER A O   
1624 C CB  . SER A 219 ? 0.3202 0.3921 0.2641 -0.0879 0.0035  0.0169  212 SER A CB  
1625 O OG  . SER A 219 ? 0.4178 0.5239 0.3860 -0.0740 0.0026  0.0170  212 SER A OG  
1626 N N   . THR A 220 ? 0.2229 0.2389 0.1744 -0.0409 -0.0028 0.0168  213 THR A N   
1627 C CA  . THR A 220 ? 0.2148 0.2282 0.1732 -0.0261 -0.0008 0.0159  213 THR A CA  
1628 C C   . THR A 220 ? 0.2409 0.2258 0.1832 -0.0277 -0.0035 0.0160  213 THR A C   
1629 O O   . THR A 220 ? 0.2599 0.2219 0.1939 -0.0278 -0.0098 0.0169  213 THR A O   
1630 C CB  . THR A 220 ? 0.2183 0.2293 0.1880 -0.0129 -0.0035 0.0158  213 THR A CB  
1631 O OG1 . THR A 220 ? 0.2528 0.2893 0.2344 -0.0108 -0.0028 0.0173  213 THR A OG1 
1632 C CG2 . THR A 220 ? 0.2858 0.2908 0.2587 -0.0012 -0.0006 0.0144  213 THR A CG2 
1633 N N   . LYS A 221 ? 0.2169 0.2042 0.1545 -0.0273 0.0010  0.0149  214 LYS A N   
1634 C CA  . LYS A 221 ? 0.2186 0.1813 0.1397 -0.0287 -0.0032 0.0155  214 LYS A CA  
1635 C C   . LYS A 221 ? 0.2644 0.2171 0.1930 -0.0170 -0.0083 0.0141  214 LYS A C   
1636 O O   . LYS A 221 ? 0.2522 0.2142 0.1932 -0.0087 -0.0047 0.0114  214 LYS A O   
1637 C CB  . LYS A 221 ? 0.2303 0.1983 0.1416 -0.0328 0.0036  0.0136  214 LYS A CB  
1638 C CG  . LYS A 221 ? 0.2660 0.2448 0.1668 -0.0482 0.0093  0.0150  214 LYS A CG  
1639 C CD  . LYS A 221 ? 0.3058 0.2866 0.1924 -0.0533 0.0164  0.0127  214 LYS A CD  
1640 C CE  . LYS A 221 ? 0.3402 0.3351 0.2162 -0.0719 0.0232  0.0143  214 LYS A CE  
1641 N NZ  . LYS A 221 ? 0.5289 0.5246 0.3862 -0.0803 0.0310  0.0123  214 LYS A NZ  
1642 N N   . ILE A 222 ? 0.2457 0.1797 0.1659 -0.0164 -0.0168 0.0161  215 ILE A N   
1643 C CA  . ILE A 222 ? 0.2185 0.1493 0.1464 -0.0079 -0.0221 0.0143  215 ILE A CA  
1644 C C   . ILE A 222 ? 0.2877 0.2088 0.2007 -0.0105 -0.0270 0.0151  215 ILE A C   
1645 O O   . ILE A 222 ? 0.2859 0.1926 0.1840 -0.0126 -0.0339 0.0196  215 ILE A O   
1646 C CB  . ILE A 222 ? 0.2848 0.2099 0.2188 -0.0023 -0.0280 0.0152  215 ILE A CB  
1647 C CG1 . ILE A 222 ? 0.2632 0.1973 0.2071 -0.0025 -0.0231 0.0141  215 ILE A CG1 
1648 C CG2 . ILE A 222 ? 0.2914 0.2221 0.2363 0.0049  -0.0325 0.0128  215 ILE A CG2 
1649 C CD1 . ILE A 222 ? 0.2585 0.1837 0.2031 0.0012  -0.0268 0.0136  215 ILE A CD1 
1650 N N   . TYR A 223 ? 0.2424 0.1682 0.1554 -0.0108 -0.0236 0.0110  216 TYR A N   
1651 C CA  . TYR A 223 ? 0.2745 0.1930 0.1706 -0.0158 -0.0277 0.0105  216 TYR A CA  
1652 C C   . TYR A 223 ? 0.2850 0.2066 0.1878 -0.0126 -0.0369 0.0093  216 TYR A C   
1653 O O   . TYR A 223 ? 0.2686 0.1973 0.1840 -0.0110 -0.0338 0.0047  216 TYR A O   
1654 C CB  . TYR A 223 ? 0.2615 0.1817 0.1503 -0.0194 -0.0172 0.0048  216 TYR A CB  
1655 C CG  . TYR A 223 ? 0.2765 0.1883 0.1439 -0.0268 -0.0203 0.0028  216 TYR A CG  
1656 C CD1 . TYR A 223 ? 0.2936 0.1980 0.1396 -0.0344 -0.0230 0.0072  216 TYR A CD1 
1657 C CD2 . TYR A 223 ? 0.3008 0.2099 0.1655 -0.0285 -0.0206 -0.0035 216 TYR A CD2 
1658 C CE1 . TYR A 223 ? 0.3178 0.2147 0.1414 -0.0420 -0.0264 0.0058  216 TYR A CE1 
1659 C CE2 . TYR A 223 ? 0.3320 0.2340 0.1745 -0.0373 -0.0240 -0.0061 216 TYR A CE2 
1660 C CZ  . TYR A 223 ? 0.3437 0.2408 0.1660 -0.0434 -0.0273 -0.0012 216 TYR A CZ  
1661 O OH  . TYR A 223 ? 0.4120 0.3021 0.2087 -0.0532 -0.0314 -0.0034 216 TYR A OH  
1662 N N   . ASP A 224 ? 0.2826 0.1998 0.1761 -0.0118 -0.0486 0.0139  217 ASP A N   
1663 C CA  . ASP A 224 ? 0.2999 0.2290 0.2020 -0.0090 -0.0586 0.0128  217 ASP A CA  
1664 C C   . ASP A 224 ? 0.2802 0.2095 0.1664 -0.0192 -0.0606 0.0093  217 ASP A C   
1665 O O   . ASP A 224 ? 0.3090 0.2283 0.1729 -0.0238 -0.0652 0.0130  217 ASP A O   
1666 C CB  . ASP A 224 ? 0.2830 0.2105 0.1846 0.0008  -0.0714 0.0197  217 ASP A CB  
1667 C CG  . ASP A 224 ? 0.3544 0.3057 0.2732 0.0062  -0.0813 0.0178  217 ASP A CG  
1668 O OD1 . ASP A 224 ? 0.4192 0.3802 0.3310 -0.0011 -0.0878 0.0165  217 ASP A OD1 
1669 O OD2 . ASP A 224 ? 0.5209 0.4846 0.4604 0.0157  -0.0813 0.0166  217 ASP A OD2 
1670 N N   . ARG A 225 ? 0.2904 0.2273 0.1839 -0.0246 -0.0563 0.0019  218 ARG A N   
1671 C CA  . ARG A 225 ? 0.2965 0.2283 0.1708 -0.0366 -0.0558 -0.0038 218 ARG A CA  
1672 C C   . ARG A 225 ? 0.3451 0.2869 0.2093 -0.0406 -0.0719 -0.0004 218 ARG A C   
1673 O O   . ARG A 225 ? 0.3740 0.3068 0.2129 -0.0496 -0.0740 -0.0012 218 ARG A O   
1674 C CB  . ARG A 225 ? 0.3491 0.2815 0.2298 -0.0430 -0.0489 -0.0122 218 ARG A CB  
1675 C CG  . ARG A 225 ? 0.4114 0.3327 0.2678 -0.0573 -0.0475 -0.0200 218 ARG A CG  
1676 C CD  . ARG A 225 ? 0.4444 0.3547 0.3002 -0.0648 -0.0383 -0.0285 218 ARG A CD  
1677 N NE  . ARG A 225 ? 0.4263 0.3568 0.3007 -0.0701 -0.0452 -0.0286 218 ARG A NE  
1678 C CZ  . ARG A 225 ? 0.4732 0.3954 0.3441 -0.0821 -0.0399 -0.0352 218 ARG A CZ  
1679 N NH1 . ARG A 225 ? 0.4679 0.3563 0.3159 -0.0872 -0.0279 -0.0422 218 ARG A NH1 
1680 N NH2 . ARG A 225 ? 0.4236 0.3708 0.3126 -0.0892 -0.0460 -0.0352 218 ARG A NH2 
1681 N N   . ALA A 226 ? 0.3115 0.2742 0.1951 -0.0331 -0.0835 0.0034  219 ALA A N   
1682 C CA  . ALA A 226 ? 0.3695 0.3491 0.2476 -0.0345 -0.1007 0.0070  219 ALA A CA  
1683 C C   . ALA A 226 ? 0.3943 0.3575 0.2493 -0.0291 -0.1091 0.0170  219 ALA A C   
1684 O O   . ALA A 226 ? 0.4103 0.3760 0.2450 -0.0358 -0.1204 0.0196  219 ALA A O   
1685 C CB  . ALA A 226 ? 0.3921 0.4035 0.3006 -0.0241 -0.1100 0.0085  219 ALA A CB  
1686 N N   . THR A 227 ? 0.3868 0.3317 0.2415 -0.0188 -0.1045 0.0230  220 THR A N   
1687 C CA  . THR A 227 ? 0.3953 0.3187 0.2246 -0.0150 -0.1121 0.0336  220 THR A CA  
1688 C C   . THR A 227 ? 0.4004 0.2995 0.2033 -0.0272 -0.0997 0.0333  220 THR A C   
1689 O O   . THR A 227 ? 0.4224 0.3025 0.1963 -0.0305 -0.1053 0.0416  220 THR A O   
1690 C CB  . THR A 227 ? 0.4088 0.3230 0.2488 0.0023  -0.1155 0.0407  220 THR A CB  
1691 O OG1 . THR A 227 ? 0.3913 0.2973 0.2425 0.0013  -0.0999 0.0361  220 THR A OG1 
1692 C CG2 . THR A 227 ? 0.4844 0.4274 0.3523 0.0174  -0.1267 0.0404  220 THR A CG2 
1693 N N   . GLY A 228 ? 0.3643 0.2645 0.1764 -0.0331 -0.0830 0.0244  221 GLY A N   
1694 C CA  . GLY A 228 ? 0.3811 0.2667 0.1742 -0.0425 -0.0696 0.0229  221 GLY A CA  
1695 C C   . GLY A 228 ? 0.4311 0.3035 0.2221 -0.0400 -0.0649 0.0295  221 GLY A C   
1696 O O   . GLY A 228 ? 0.4263 0.2896 0.1984 -0.0501 -0.0556 0.0301  221 GLY A O   
1697 N N   . LYS A 229 ? 0.3500 0.2220 0.1587 -0.0284 -0.0702 0.0333  222 LYS A N   
1698 C CA  . LYS A 229 ? 0.3546 0.2091 0.1568 -0.0281 -0.0673 0.0392  222 LYS A CA  
1699 C C   . LYS A 229 ? 0.3352 0.2010 0.1613 -0.0266 -0.0551 0.0333  222 LYS A C   
1700 O O   . LYS A 229 ? 0.3205 0.2034 0.1716 -0.0194 -0.0533 0.0275  222 LYS A O   
1701 C CB  . LYS A 229 ? 0.4048 0.2437 0.2040 -0.0150 -0.0813 0.0475  222 LYS A CB  
1702 C CG  . LYS A 229 ? 0.4442 0.2747 0.2224 -0.0114 -0.0973 0.0554  222 LYS A CG  
1703 C CD  . LYS A 229 ? 0.4390 0.2485 0.1789 -0.0268 -0.0963 0.0614  222 LYS A CD  
1704 C CE  . LYS A 229 ? 0.5285 0.3328 0.2520 -0.0218 -0.1115 0.0691  222 LYS A CE  
1705 N NZ  . LYS A 229 ? 0.6541 0.4438 0.3469 -0.0388 -0.1059 0.0717  222 LYS A NZ  
1706 N N   . VAL A 230 ? 0.3449 0.2010 0.1610 -0.0350 -0.0477 0.0357  223 VAL A N   
1707 C CA  . VAL A 230 ? 0.3101 0.1791 0.1455 -0.0357 -0.0375 0.0314  223 VAL A CA  
1708 C C   . VAL A 230 ? 0.3420 0.1928 0.1748 -0.0326 -0.0423 0.0356  223 VAL A C   
1709 O O   . VAL A 230 ? 0.3763 0.1993 0.1826 -0.0383 -0.0470 0.0425  223 VAL A O   
1710 C CB  . VAL A 230 ? 0.3469 0.2260 0.1745 -0.0497 -0.0248 0.0294  223 VAL A CB  
1711 C CG1 . VAL A 230 ? 0.3499 0.2435 0.1945 -0.0516 -0.0176 0.0272  223 VAL A CG1 
1712 C CG2 . VAL A 230 ? 0.3858 0.2821 0.2178 -0.0492 -0.0172 0.0227  223 VAL A CG2 
1713 N N   . SER A 231 ? 0.3130 0.1755 0.1691 -0.0246 -0.0403 0.0313  224 SER A N   
1714 C CA  . SER A 231 ? 0.3371 0.1832 0.1907 -0.0225 -0.0422 0.0325  224 SER A CA  
1715 C C   . SER A 231 ? 0.3212 0.1885 0.1941 -0.0256 -0.0336 0.0272  224 SER A C   
1716 O O   . SER A 231 ? 0.2852 0.1783 0.1740 -0.0261 -0.0273 0.0238  224 SER A O   
1717 C CB  . SER A 231 ? 0.3667 0.2039 0.2271 -0.0051 -0.0516 0.0329  224 SER A CB  
1718 O OG  . SER A 231 ? 0.3775 0.2425 0.2657 0.0037  -0.0504 0.0273  224 SER A OG  
1719 N N   . TYR A 232 ? 0.3328 0.1869 0.2017 -0.0269 -0.0339 0.0266  225 TYR A N   
1720 C CA  . TYR A 232 ? 0.3031 0.1763 0.1859 -0.0318 -0.0276 0.0225  225 TYR A CA  
1721 C C   . TYR A 232 ? 0.2931 0.1540 0.1786 -0.0236 -0.0301 0.0193  225 TYR A C   
1722 O O   . TYR A 232 ? 0.3371 0.1670 0.2063 -0.0184 -0.0350 0.0204  225 TYR A O   
1723 C CB  . TYR A 232 ? 0.3209 0.1942 0.1893 -0.0518 -0.0226 0.0236  225 TYR A CB  
1724 C CG  . TYR A 232 ? 0.3191 0.2082 0.1834 -0.0623 -0.0175 0.0256  225 TYR A CG  
1725 C CD1 . TYR A 232 ? 0.3794 0.2447 0.2184 -0.0696 -0.0196 0.0304  225 TYR A CD1 
1726 C CD2 . TYR A 232 ? 0.3181 0.2463 0.2024 -0.0644 -0.0101 0.0227  225 TYR A CD2 
1727 C CE1 . TYR A 232 ? 0.4107 0.2922 0.2441 -0.0808 -0.0129 0.0312  225 TYR A CE1 
1728 C CE2 . TYR A 232 ? 0.3053 0.2510 0.1869 -0.0723 -0.0033 0.0229  225 TYR A CE2 
1729 C CZ  . TYR A 232 ? 0.3465 0.2699 0.2029 -0.0815 -0.0040 0.0265  225 TYR A CZ  
1730 O OH  . TYR A 232 ? 0.4158 0.3590 0.2682 -0.0909 0.0046  0.0256  225 TYR A OH  
1731 N N   . GLY A 233 ? 0.2810 0.1646 0.1842 -0.0226 -0.0261 0.0153  226 GLY A N   
1732 C CA  . GLY A 233 ? 0.3023 0.1764 0.2028 -0.0220 -0.0256 0.0112  226 GLY A CA  
1733 C C   . GLY A 233 ? 0.2889 0.1603 0.1998 -0.0052 -0.0274 0.0076  226 GLY A C   
1734 O O   . GLY A 233 ? 0.2876 0.1545 0.1972 -0.0040 -0.0252 0.0027  226 GLY A O   
1735 N N   . ARG A 234 ? 0.2980 0.1754 0.2193 0.0062  -0.0309 0.0091  227 ARG A N   
1736 C CA  . ARG A 234 ? 0.2753 0.1552 0.2078 0.0216  -0.0328 0.0055  227 ARG A CA  
1737 C C   . ARG A 234 ? 0.2680 0.1707 0.2178 0.0269  -0.0351 0.0066  227 ARG A C   
1738 O O   . ARG A 234 ? 0.2730 0.1731 0.2171 0.0245  -0.0391 0.0108  227 ARG A O   
1739 C CB  . ARG A 234 ? 0.3290 0.1775 0.2446 0.0316  -0.0380 0.0060  227 ARG A CB  
1740 C CG  . ARG A 234 ? 0.3484 0.2052 0.2785 0.0512  -0.0403 0.0020  227 ARG A CG  
1741 C CD  . ARG A 234 ? 0.4000 0.2212 0.3106 0.0651  -0.0461 0.0036  227 ARG A CD  
1742 N NE  . ARG A 234 ? 0.4729 0.2587 0.3594 0.0593  -0.0413 0.0001  227 ARG A NE  
1743 C CZ  . ARG A 234 ? 0.5193 0.2998 0.4065 0.0670  -0.0355 -0.0085 227 ARG A CZ  
1744 N NH1 . ARG A 234 ? 0.4746 0.2842 0.3868 0.0828  -0.0332 -0.0142 227 ARG A NH1 
1745 N NH2 . ARG A 234 ? 0.5110 0.2575 0.3721 0.0567  -0.0310 -0.0123 227 ARG A NH2 
1746 N N   . VAL A 235 ? 0.2177 0.1416 0.1858 0.0317  -0.0320 0.0025  228 VAL A N   
1747 C CA  . VAL A 235 ? 0.2278 0.1725 0.2109 0.0343  -0.0341 0.0021  228 VAL A CA  
1748 C C   . VAL A 235 ? 0.2015 0.1534 0.1938 0.0481  -0.0389 -0.0006 228 VAL A C   
1749 O O   . VAL A 235 ? 0.2293 0.1881 0.2296 0.0545  -0.0346 -0.0057 228 VAL A O   
1750 C CB  . VAL A 235 ? 0.2269 0.1897 0.2217 0.0283  -0.0272 -0.0001 228 VAL A CB  
1751 C CG1 . VAL A 235 ? 0.1991 0.1799 0.2058 0.0273  -0.0286 -0.0015 228 VAL A CG1 
1752 C CG2 . VAL A 235 ? 0.2635 0.2215 0.2509 0.0198  -0.0235 0.0031  228 VAL A CG2 
1753 N N   . PRO A 236 ? 0.2107 0.1641 0.2022 0.0537  -0.0477 0.0026  229 PRO A N   
1754 C CA  . PRO A 236 ? 0.2416 0.2075 0.2447 0.0704  -0.0536 0.0006  229 PRO A CA  
1755 C C   . PRO A 236 ? 0.2254 0.2297 0.2541 0.0702  -0.0493 -0.0056 229 PRO A C   
1756 O O   . PRO A 236 ? 0.2350 0.2535 0.2693 0.0560  -0.0454 -0.0065 229 PRO A O   
1757 C CB  . PRO A 236 ? 0.3386 0.3019 0.3339 0.0732  -0.0655 0.0070  229 PRO A CB  
1758 C CG  . PRO A 236 ? 0.3742 0.3117 0.3468 0.0591  -0.0642 0.0119  229 PRO A CG  
1759 C CD  . PRO A 236 ? 0.2820 0.2264 0.2606 0.0462  -0.0528 0.0080  229 PRO A CD  
1760 N N   . SER A 237 ? 0.2105 0.2302 0.2528 0.0862  -0.0496 -0.0101 230 SER A N   
1761 C CA  . SER A 237 ? 0.2167 0.2762 0.2834 0.0848  -0.0433 -0.0170 230 SER A CA  
1762 C C   . SER A 237 ? 0.1991 0.2882 0.2778 0.0717  -0.0475 -0.0161 230 SER A C   
1763 O O   . SER A 237 ? 0.2166 0.3106 0.2943 0.0745  -0.0587 -0.0119 230 SER A O   
1764 C CB  . SER A 237 ? 0.2335 0.3120 0.3159 0.1076  -0.0442 -0.0222 230 SER A CB  
1765 O OG  . SER A 237 ? 0.2687 0.3524 0.3538 0.1228  -0.0579 -0.0174 230 SER A OG  
1766 N N   . GLY A 238 ? 0.1968 0.3032 0.2833 0.0561  -0.0385 -0.0199 231 GLY A N   
1767 C CA  . GLY A 238 ? 0.2469 0.3789 0.3420 0.0402  -0.0405 -0.0208 231 GLY A CA  
1768 C C   . GLY A 238 ? 0.1773 0.2836 0.2529 0.0258  -0.0430 -0.0162 231 GLY A C   
1769 O O   . GLY A 238 ? 0.2110 0.3318 0.2882 0.0118  -0.0457 -0.0175 231 GLY A O   
1770 N N   . SER A 239 ? 0.1827 0.3140 0.3532 0.0428  -0.0105 -0.0882 232 SER A N   
1771 C CA  . SER A 239 ? 0.1767 0.2870 0.3264 0.0351  -0.0184 -0.0741 232 SER A CA  
1772 C C   . SER A 239 ? 0.2218 0.3342 0.3611 0.0196  -0.0035 -0.0656 232 SER A C   
1773 O O   . SER A 239 ? 0.1788 0.2963 0.3062 0.0166  0.0118  -0.0638 232 SER A O   
1774 C CB  . SER A 239 ? 0.2011 0.2801 0.3223 0.0394  -0.0262 -0.0659 232 SER A CB  
1775 O OG  . SER A 239 ? 0.2503 0.3199 0.3815 0.0537  -0.0392 -0.0681 232 SER A OG  
1776 N N   . VAL A 240 ? 0.1683 0.2754 0.3099 0.0116  -0.0085 -0.0601 233 VAL A N   
1777 C CA  . VAL A 240 ? 0.1686 0.2681 0.3010 -0.0020 0.0036  -0.0493 233 VAL A CA  
1778 C C   . VAL A 240 ? 0.1671 0.2385 0.2680 -0.0017 -0.0060 -0.0392 233 VAL A C   
1779 O O   . VAL A 240 ? 0.1734 0.2378 0.2729 0.0017  -0.0210 -0.0410 233 VAL A O   
1780 C CB  . VAL A 240 ? 0.1674 0.2818 0.3344 -0.0125 0.0064  -0.0550 233 VAL A CB  
1781 C CG1 . VAL A 240 ? 0.1967 0.2973 0.3582 -0.0259 0.0209  -0.0419 233 VAL A CG1 
1782 C CG2 . VAL A 240 ? 0.1697 0.3163 0.3743 -0.0130 0.0166  -0.0665 233 VAL A CG2 
1783 N N   . VAL A 241 ? 0.1697 0.2288 0.2448 -0.0038 0.0025  -0.0289 234 VAL A N   
1784 C CA  . VAL A 241 ? 0.1679 0.2042 0.2155 -0.0021 -0.0055 -0.0212 234 VAL A CA  
1785 C C   . VAL A 241 ? 0.1708 0.1972 0.2079 -0.0103 0.0028  -0.0092 234 VAL A C   
1786 O O   . VAL A 241 ? 0.1794 0.2124 0.2139 -0.0132 0.0171  -0.0019 234 VAL A O   
1787 C CB  . VAL A 241 ? 0.1715 0.2045 0.2021 0.0050  -0.0059 -0.0234 234 VAL A CB  
1788 C CG1 . VAL A 241 ? 0.1950 0.2073 0.2056 0.0055  -0.0139 -0.0173 234 VAL A CG1 
1789 C CG2 . VAL A 241 ? 0.1843 0.2250 0.2312 0.0141  -0.0115 -0.0359 234 VAL A CG2 
1790 N N   . VAL A 242 ? 0.1694 0.1804 0.1995 -0.0122 -0.0055 -0.0061 235 VAL A N   
1791 C CA  . VAL A 242 ? 0.1719 0.1707 0.1958 -0.0181 0.0010  0.0040  235 VAL A CA  
1792 C C   . VAL A 242 ? 0.1837 0.1674 0.1849 -0.0142 -0.0075 0.0078  235 VAL A C   
1793 O O   . VAL A 242 ? 0.2018 0.1831 0.1967 -0.0094 -0.0177 0.0031  235 VAL A O   
1794 C CB  . VAL A 242 ? 0.1737 0.1723 0.2234 -0.0260 0.0017  -0.0014 235 VAL A CB  
1795 C CG1 . VAL A 242 ? 0.1760 0.1941 0.2571 -0.0312 0.0096  -0.0084 235 VAL A CG1 
1796 C CG2 . VAL A 242 ? 0.1948 0.1907 0.2412 -0.0225 -0.0146 -0.0114 235 VAL A CG2 
1797 N N   . PRO A 243 ? 0.1740 0.1477 0.1652 -0.0155 -0.0024 0.0177  236 PRO A N   
1798 C CA  . PRO A 243 ? 0.1938 0.1568 0.1689 -0.0123 -0.0095 0.0196  236 PRO A CA  
1799 C C   . PRO A 243 ? 0.1933 0.1498 0.1737 -0.0140 -0.0163 0.0136  236 PRO A C   
1800 O O   . PRO A 243 ? 0.1986 0.1542 0.1953 -0.0186 -0.0142 0.0093  236 PRO A O   
1801 C CB  . PRO A 243 ? 0.2081 0.1659 0.1746 -0.0111 -0.0023 0.0317  236 PRO A CB  
1802 C CG  . PRO A 243 ? 0.2843 0.2494 0.2561 -0.0125 0.0096  0.0393  236 PRO A CG  
1803 C CD  . PRO A 243 ? 0.2153 0.1887 0.2082 -0.0180 0.0114  0.0299  236 PRO A CD  
1804 N N   . GLY A 244 ? 0.2032 0.1566 0.1710 -0.0101 -0.0235 0.0124  237 GLY A N   
1805 C CA  . GLY A 244 ? 0.2107 0.1617 0.1760 -0.0093 -0.0290 0.0075  237 GLY A CA  
1806 C C   . GLY A 244 ? 0.2113 0.1572 0.1611 -0.0061 -0.0303 0.0124  237 GLY A C   
1807 O O   . GLY A 244 ? 0.2173 0.1606 0.1635 -0.0062 -0.0269 0.0176  237 GLY A O   
1808 N N   . SER A 245 ? 0.2422 0.1898 0.1837 -0.0029 -0.0346 0.0103  238 SER A N   
1809 C CA  . SER A 245 ? 0.2467 0.1909 0.1761 -0.0009 -0.0324 0.0165  238 SER A CA  
1810 C C   . SER A 245 ? 0.2448 0.1935 0.1614 0.0051  -0.0362 0.0187  238 SER A C   
1811 O O   . SER A 245 ? 0.2378 0.1953 0.1532 0.0090  -0.0432 0.0120  238 SER A O   
1812 C CB  . SER A 245 ? 0.2525 0.1953 0.1817 -0.0020 -0.0280 0.0143  238 SER A CB  
1813 O OG  . SER A 245 ? 0.2942 0.2412 0.2233 -0.0005 -0.0304 0.0044  238 SER A OG  
1814 N N   . LEU A 246 ? 0.2624 0.2066 0.1705 0.0063  -0.0312 0.0288  239 LEU A N   
1815 C CA  . LEU A 246 ? 0.2337 0.1809 0.1250 0.0133  -0.0311 0.0375  239 LEU A CA  
1816 C C   . LEU A 246 ? 0.2867 0.2375 0.1678 0.0129  -0.0223 0.0405  239 LEU A C   
1817 O O   . LEU A 246 ? 0.2774 0.2238 0.1697 0.0066  -0.0151 0.0417  239 LEU A O   
1818 C CB  . LEU A 246 ? 0.2922 0.2281 0.1872 0.0153  -0.0290 0.0514  239 LEU A CB  
1819 C CG  . LEU A 246 ? 0.2879 0.2231 0.1929 0.0189  -0.0377 0.0478  239 LEU A CG  
1820 C CD1 . LEU A 246 ? 0.3351 0.2549 0.2517 0.0196  -0.0340 0.0582  239 LEU A CD1 
1821 C CD2 . LEU A 246 ? 0.3160 0.2642 0.2085 0.0294  -0.0474 0.0466  239 LEU A CD2 
1822 N N   . PRO A 247 ? 0.3034 0.2664 0.1640 0.0205  -0.0230 0.0397  240 PRO A N   
1823 C CA  . PRO A 247 ? 0.3115 0.2824 0.1616 0.0212  -0.0129 0.0403  240 PRO A CA  
1824 C C   . PRO A 247 ? 0.3417 0.3077 0.1856 0.0213  0.0000  0.0615  240 PRO A C   
1825 O O   . PRO A 247 ? 0.3634 0.3223 0.2000 0.0258  -0.0001 0.0776  240 PRO A O   
1826 C CB  . PRO A 247 ? 0.3443 0.3344 0.1726 0.0313  -0.0196 0.0289  240 PRO A CB  
1827 C CG  . PRO A 247 ? 0.3487 0.3408 0.1683 0.0387  -0.0305 0.0348  240 PRO A CG  
1828 C CD  . PRO A 247 ? 0.2951 0.2706 0.1412 0.0304  -0.0341 0.0354  240 PRO A CD  
1829 N N   . SER A 248 ? 0.3268 0.2969 0.1768 0.0165  0.0122  0.0620  241 SER A N   
1830 C CA  . SER A 248 ? 0.3697 0.3389 0.2157 0.0156  0.0284  0.0818  241 SER A CA  
1831 C C   . SER A 248 ? 0.4063 0.3892 0.2156 0.0284  0.0324  0.0928  241 SER A C   
1832 O O   . SER A 248 ? 0.3741 0.3738 0.1627 0.0373  0.0230  0.0780  241 SER A O   
1833 C CB  . SER A 248 ? 0.4061 0.3830 0.2704 0.0081  0.0409  0.0766  241 SER A CB  
1834 O OG  . SER A 248 ? 0.3752 0.3710 0.2245 0.0145  0.0424  0.0634  241 SER A OG  
1835 N N   . GLU A 249 ? 0.4211 0.3982 0.2304 0.0270  0.0449  0.1140  242 GLU A N   
1836 C CA  . GLU A 249 ? 0.4669 0.4562 0.2500 0.0366  0.0461  0.1219  242 GLU A CA  
1837 C C   . GLU A 249 ? 0.4954 0.5109 0.2578 0.0422  0.0511  0.1084  242 GLU A C   
1838 O O   . GLU A 249 ? 0.5143 0.5463 0.2517 0.0532  0.0434  0.1020  242 GLU A O   
1839 C CB  . GLU A 249 ? 0.5393 0.5152 0.3306 0.0326  0.0615  0.1471  242 GLU A CB  
1840 C CG  . GLU A 249 ? 0.7406 0.7262 0.5026 0.0443  0.0639  0.1610  242 GLU A CG  
1841 C CD  . GLU A 249 ? 1.1042 1.0879 0.8531 0.0557  0.0451  0.1614  242 GLU A CD  
1842 O OE1 . GLU A 249 ? 1.0612 1.0612 0.7984 0.0624  0.0290  0.1412  242 GLU A OE1 
1843 O OE2 . GLU A 249 ? 1.1863 1.1529 0.9402 0.0582  0.0466  0.1810  242 GLU A OE2 
1844 N N   . ASP A 250 ? 0.4330 0.4549 0.2076 0.0358  0.0641  0.1022  243 ASP A N   
1845 C CA  . ASP A 250 ? 0.4323 0.4800 0.1910 0.0418  0.0705  0.0870  243 ASP A CA  
1846 C C   . ASP A 250 ? 0.4457 0.5036 0.2029 0.0467  0.0563  0.0570  243 ASP A C   
1847 O O   . ASP A 250 ? 0.5023 0.5808 0.2511 0.0523  0.0594  0.0382  243 ASP A O   
1848 C CB  . ASP A 250 ? 0.5015 0.5560 0.2777 0.0338  0.0938  0.0939  243 ASP A CB  
1849 C CG  . ASP A 250 ? 0.5242 0.5716 0.3364 0.0239  0.0951  0.0847  243 ASP A CG  
1850 O OD1 . ASP A 250 ? 0.4378 0.4718 0.2631 0.0217  0.0758  0.0701  243 ASP A OD1 
1851 O OD2 . ASP A 250 ? 0.5305 0.5851 0.3676 0.0158  0.1120  0.0879  243 ASP A OD2 
1852 N N   . GLY A 251 ? 0.4295 0.4715 0.2007 0.0434  0.0404  0.0495  244 GLY A N   
1853 C CA  . GLY A 251 ? 0.3883 0.4333 0.1704 0.0441  0.0257  0.0199  244 GLY A CA  
1854 C C   . GLY A 251 ? 0.4043 0.4448 0.2177 0.0369  0.0299  0.0057  244 GLY A C   
1855 O O   . GLY A 251 ? 0.4258 0.4662 0.2509 0.0382  0.0206  -0.0173 244 GLY A O   
1856 N N   . SER A 252 ? 0.3567 0.3935 0.1874 0.0297  0.0432  0.0182  245 SER A N   
1857 C CA  . SER A 252 ? 0.3094 0.3470 0.1693 0.0263  0.0459  0.0048  245 SER A CA  
1858 C C   . SER A 252 ? 0.2851 0.3031 0.1700 0.0206  0.0327  0.0004  245 SER A C   
1859 O O   . SER A 252 ? 0.2836 0.3008 0.1885 0.0220  0.0304  -0.0124 245 SER A O   
1860 C CB  . SER A 252 ? 0.3438 0.3898 0.2190 0.0206  0.0634  0.0173  245 SER A CB  
1861 O OG  . SER A 252 ? 0.3651 0.3966 0.2497 0.0116  0.0648  0.0367  245 SER A OG  
1862 N N   . HIS A 253 ? 0.2899 0.2932 0.1739 0.0158  0.0251  0.0117  246 HIS A N   
1863 C CA  . HIS A 253 ? 0.2480 0.2365 0.1525 0.0108  0.0157  0.0105  246 HIS A CA  
1864 C C   . HIS A 253 ? 0.3024 0.2795 0.1988 0.0084  0.0079  0.0191  246 HIS A C   
1865 O O   . HIS A 253 ? 0.3017 0.2810 0.1800 0.0109  0.0097  0.0283  246 HIS A O   
1866 C CB  . HIS A 253 ? 0.2363 0.2268 0.1638 0.0056  0.0208  0.0153  246 HIS A CB  
1867 C CG  . HIS A 253 ? 0.2723 0.2611 0.2029 -0.0012 0.0277  0.0295  246 HIS A CG  
1868 N ND1 . HIS A 253 ? 0.2872 0.2848 0.2118 -0.0022 0.0424  0.0391  246 HIS A ND1 
1869 C CD2 . HIS A 253 ? 0.3476 0.3259 0.2889 -0.0071 0.0232  0.0355  246 HIS A CD2 
1870 C CE1 . HIS A 253 ? 0.3428 0.3318 0.2780 -0.0095 0.0472  0.0520  246 HIS A CE1 
1871 N NE2 . HIS A 253 ? 0.2964 0.2737 0.2422 -0.0123 0.0348  0.0479  246 HIS A NE2 
1872 N N   . SER A 254 ? 0.2568 0.2234 0.1667 0.0051  -0.0002 0.0173  247 SER A N   
1873 C CA  . SER A 254 ? 0.2723 0.2299 0.1804 0.0027  -0.0066 0.0235  247 SER A CA  
1874 C C   . SER A 254 ? 0.2507 0.2032 0.1754 -0.0023 -0.0076 0.0265  247 SER A C   
1875 O O   . SER A 254 ? 0.2353 0.1915 0.1717 -0.0024 -0.0071 0.0228  247 SER A O   
1876 C CB  . SER A 254 ? 0.2721 0.2273 0.1786 0.0046  -0.0155 0.0145  247 SER A CB  
1877 O OG  . SER A 254 ? 0.2815 0.2463 0.1748 0.0100  -0.0174 0.0057  247 SER A OG  
1878 N N   . LEU A 255 ? 0.2484 0.1944 0.1744 -0.0045 -0.0101 0.0319  248 LEU A N   
1879 C CA  . LEU A 255 ? 0.2370 0.1815 0.1770 -0.0079 -0.0130 0.0299  248 LEU A CA  
1880 C C   . LEU A 255 ? 0.2278 0.1686 0.1654 -0.0066 -0.0196 0.0274  248 LEU A C   
1881 O O   . LEU A 255 ? 0.2418 0.1789 0.1731 -0.0046 -0.0220 0.0294  248 LEU A O   
1882 C CB  . LEU A 255 ? 0.2409 0.1816 0.1924 -0.0124 -0.0085 0.0343  248 LEU A CB  
1883 C CG  . LEU A 255 ? 0.2555 0.2020 0.2168 -0.0161 0.0012  0.0374  248 LEU A CG  
1884 C CD1 . LEU A 255 ? 0.2974 0.2370 0.2793 -0.0228 0.0068  0.0408  248 LEU A CD1 
1885 C CD2 . LEU A 255 ? 0.2660 0.2265 0.2382 -0.0159 -0.0003 0.0282  248 LEU A CD2 
1886 N N   . ALA A 256 ? 0.2176 0.1621 0.1599 -0.0064 -0.0221 0.0237  249 ALA A N   
1887 C CA  . ALA A 256 ? 0.2168 0.1607 0.1578 -0.0055 -0.0248 0.0224  249 ALA A CA  
1888 C C   . ALA A 256 ? 0.2135 0.1560 0.1587 -0.0060 -0.0266 0.0204  249 ALA A C   
1889 O O   . ALA A 256 ? 0.2436 0.1852 0.1965 -0.0076 -0.0262 0.0184  249 ALA A O   
1890 C CB  . ALA A 256 ? 0.2486 0.1987 0.1898 -0.0033 -0.0247 0.0228  249 ALA A CB  
1891 N N   . CYS A 257 ? 0.2188 0.1614 0.1639 -0.0046 -0.0284 0.0192  250 CYS A N   
1892 C CA  . CYS A 257 ? 0.2197 0.1615 0.1716 -0.0028 -0.0304 0.0161  250 CYS A CA  
1893 C C   . CYS A 257 ? 0.2448 0.1946 0.2000 -0.0019 -0.0302 0.0123  250 CYS A C   
1894 O O   . CYS A 257 ? 0.2309 0.1842 0.1847 -0.0039 -0.0273 0.0138  250 CYS A O   
1895 C CB  . CYS A 257 ? 0.2486 0.1820 0.1998 0.0002  -0.0324 0.0218  250 CYS A CB  
1896 S SG  . CYS A 257 ? 0.2996 0.2386 0.2429 0.0040  -0.0371 0.0228  250 CYS A SG  
1897 N N   . ALA A 258 ? 0.2184 0.1709 0.1822 0.0011  -0.0316 0.0072  251 ALA A N   
1898 C CA  . ALA A 258 ? 0.2037 0.1670 0.1755 0.0021  -0.0302 0.0028  251 ALA A CA  
1899 C C   . ALA A 258 ? 0.2213 0.1849 0.1996 0.0056  -0.0365 0.0028  251 ALA A C   
1900 O O   . ALA A 258 ? 0.2231 0.1782 0.1987 0.0104  -0.0414 0.0069  251 ALA A O   
1901 C CB  . ALA A 258 ? 0.2361 0.2075 0.2152 0.0053  -0.0280 -0.0060 251 ALA A CB  
1902 N N   . VAL A 259 ? 0.1916 0.1667 0.1799 0.0037  -0.0361 -0.0014 252 VAL A N   
1903 C CA  . VAL A 259 ? 0.1810 0.1638 0.1776 0.0084  -0.0448 -0.0054 252 VAL A CA  
1904 C C   . VAL A 259 ? 0.1776 0.1776 0.1968 0.0095  -0.0437 -0.0145 252 VAL A C   
1905 O O   . VAL A 259 ? 0.1810 0.1895 0.2114 0.0020  -0.0344 -0.0174 252 VAL A O   
1906 C CB  . VAL A 259 ? 0.1867 0.1723 0.1816 0.0043  -0.0474 -0.0082 252 VAL A CB  
1907 C CG1 . VAL A 259 ? 0.2209 0.2220 0.2246 0.0108  -0.0591 -0.0167 252 VAL A CG1 
1908 C CG2 . VAL A 259 ? 0.2123 0.1843 0.1860 0.0042  -0.0470 -0.0005 252 VAL A CG2 
1909 N N   . ILE A 260 ? 0.1861 0.1917 0.2138 0.0194  -0.0519 -0.0174 253 ILE A N   
1910 C CA  . ILE A 260 ? 0.1795 0.2063 0.2334 0.0222  -0.0524 -0.0283 253 ILE A CA  
1911 C C   . ILE A 260 ? 0.1963 0.2400 0.2631 0.0216  -0.0612 -0.0362 253 ILE A C   
1912 O O   . ILE A 260 ? 0.1910 0.2363 0.2485 0.0310  -0.0747 -0.0348 253 ILE A O   
1913 C CB  . ILE A 260 ? 0.1810 0.2074 0.2431 0.0356  -0.0586 -0.0295 253 ILE A CB  
1914 C CG1 . ILE A 260 ? 0.2045 0.2157 0.2594 0.0350  -0.0502 -0.0279 253 ILE A CG1 
1915 C CG2 . ILE A 260 ? 0.1923 0.2452 0.2851 0.0396  -0.0598 -0.0425 253 ILE A CG2 
1916 C CD1 . ILE A 260 ? 0.2697 0.2720 0.3354 0.0480  -0.0557 -0.0288 253 ILE A CD1 
1917 N N   . VAL A 261 ? 0.1712 0.2293 0.2606 0.0109  -0.0532 -0.0449 254 VAL A N   
1918 C CA  . VAL A 261 ? 0.1717 0.2471 0.2807 0.0076  -0.0614 -0.0576 254 VAL A CA  
1919 C C   . VAL A 261 ? 0.1821 0.2883 0.3278 0.0114  -0.0668 -0.0729 254 VAL A C   
1920 O O   . VAL A 261 ? 0.2017 0.3287 0.3662 0.0123  -0.0791 -0.0879 254 VAL A O   
1921 C CB  . VAL A 261 ? 0.1739 0.2424 0.2923 -0.0084 -0.0489 -0.0586 254 VAL A CB  
1922 C CG1 . VAL A 261 ? 0.1939 0.2374 0.2801 -0.0094 -0.0480 -0.0474 254 VAL A CG1 
1923 C CG2 . VAL A 261 ? 0.2089 0.2789 0.3429 -0.0176 -0.0289 -0.0532 254 VAL A CG2 
1924 N N   . LYS A 262 ? 0.1679 0.2814 0.3264 0.0144  -0.0589 -0.0726 255 LYS A N   
1925 C CA  . LYS A 262 ? 0.1942 0.3386 0.3878 0.0220  -0.0657 -0.0870 255 LYS A CA  
1926 C C   . LYS A 262 ? 0.2196 0.3642 0.4165 0.0283  -0.0559 -0.0844 255 LYS A C   
1927 O O   . LYS A 262 ? 0.1727 0.2963 0.3458 0.0256  -0.0444 -0.0738 255 LYS A O   
1928 C CB  . LYS A 262 ? 0.3543 0.5249 0.5909 0.0081  -0.0595 -0.1030 255 LYS A CB  
1929 C CG  . LYS A 262 ? 0.3191 0.4878 0.5703 -0.0081 -0.0332 -0.0981 255 LYS A CG  
1930 C CD  . LYS A 262 ? 0.3755 0.5735 0.6813 -0.0212 -0.0274 -0.1154 255 LYS A CD  
1931 C CE  . LYS A 262 ? 0.6085 0.8083 0.9346 -0.0371 0.0024  -0.1075 255 LYS A CE  
1932 N NZ  . LYS A 262 ? 0.6990 0.9250 1.0858 -0.0525 0.0103  -0.1240 255 LYS A NZ  
1933 N N   . ARG A 263 ? 0.2040 0.3753 0.4320 0.0386  -0.0624 -0.0968 256 ARG A N   
1934 C CA  . ARG A 263 ? 0.2777 0.4539 0.5156 0.0472  -0.0543 -0.0997 256 ARG A CA  
1935 C C   . ARG A 263 ? 0.2857 0.5025 0.5725 0.0455  -0.0486 -0.1174 256 ARG A C   
1936 O O   . ARG A 263 ? 0.2887 0.5304 0.6031 0.0502  -0.0636 -0.1290 256 ARG A O   
1937 C CB  . ARG A 263 ? 0.2830 0.4445 0.5084 0.0681  -0.0707 -0.0944 256 ARG A CB  
1938 C CG  . ARG A 263 ? 0.3677 0.5247 0.5996 0.0766  -0.0619 -0.0983 256 ARG A CG  
1939 C CD  . ARG A 263 ? 0.5004 0.6331 0.7216 0.0952  -0.0757 -0.0898 256 ARG A CD  
1940 N NE  . ARG A 263 ? 0.5048 0.6313 0.7374 0.1027  -0.0670 -0.0980 256 ARG A NE  
1941 C CZ  . ARG A 263 ? 0.4041 0.5042 0.6349 0.1171  -0.0736 -0.0927 256 ARG A CZ  
1942 N NH1 . ARG A 263 ? 0.5773 0.6542 0.7924 0.1263  -0.0874 -0.0744 256 ARG A NH1 
1943 N NH2 . ARG A 263 ? 0.3306 0.4276 0.5767 0.1225  -0.0647 -0.1061 256 ARG A NH2 
1944 N N   . VAL A 264 ? 0.2542 0.4814 0.5522 0.0391  -0.0266 -0.1204 257 VAL A N   
1945 C CA  . VAL A 264 ? 0.2326 0.5002 0.5793 0.0344  -0.0147 -0.1358 257 VAL A CA  
1946 C C   . VAL A 264 ? 0.3632 0.6448 0.7208 0.0478  -0.0069 -0.1447 257 VAL A C   
1947 O O   . VAL A 264 ? 0.2916 0.5497 0.6179 0.0556  -0.0050 -0.1390 257 VAL A O   
1948 C CB  . VAL A 264 ? 0.2726 0.5453 0.6278 0.0114  0.0107  -0.1301 257 VAL A CB  
1949 C CG1 . VAL A 264 ? 0.3374 0.5922 0.6844 -0.0011 0.0030  -0.1237 257 VAL A CG1 
1950 C CG2 . VAL A 264 ? 0.2894 0.5447 0.6077 0.0080  0.0319  -0.1159 257 VAL A CG2 
1951 N N   . ASP A 265 ? 0.3633 0.6754 0.7577 0.0488  -0.0025 -0.1580 258 ASP A N   
1952 C CA  . ASP A 265 ? 0.4285 0.7519 0.8312 0.0602  0.0057  -0.1672 258 ASP A CA  
1953 C C   . ASP A 265 ? 0.3977 0.7408 0.8063 0.0465  0.0375  -0.1674 258 ASP A C   
1954 O O   . ASP A 265 ? 0.3156 0.6614 0.7243 0.0282  0.0537  -0.1577 258 ASP A O   
1955 C CB  . ASP A 265 ? 0.4564 0.7966 0.8875 0.0717  -0.0100 -0.1788 258 ASP A CB  
1956 C CG  . ASP A 265 ? 0.4242 0.7924 0.8895 0.0572  -0.0043 -0.1862 258 ASP A CG  
1957 O OD1 . ASP A 265 ? 0.4458 0.8176 0.9152 0.0373  0.0143  -0.1807 258 ASP A OD1 
1958 O OD2 . ASP A 265 ? 0.4851 0.8704 0.9746 0.0661  -0.0181 -0.1972 258 ASP A OD2 
1959 N N   . ALA A 266 ? 0.4312 0.7865 0.8426 0.0562  0.0474  -0.1768 259 ALA A N   
1960 C CA  . ALA A 266 ? 0.3755 0.7496 0.7825 0.0466  0.0781  -0.1745 259 ALA A CA  
1961 C C   . ALA A 266 ? 0.3727 0.7719 0.8136 0.0303  0.0936  -0.1718 259 ALA A C   
1962 O O   . ALA A 266 ? 0.4097 0.8157 0.8431 0.0162  0.1198  -0.1586 259 ALA A O   
1963 C CB  . ALA A 266 ? 0.3977 0.7815 0.8015 0.0618  0.0832  -0.1883 259 ALA A CB  
1964 N N   . GLN A 267 ? 0.3571 0.7694 0.8345 0.0324  0.0782  -0.1832 260 GLN A N   
1965 C CA  . GLN A 267 ? 0.3469 0.7820 0.8613 0.0159  0.0914  -0.1836 260 GLN A CA  
1966 C C   . GLN A 267 ? 0.3878 0.8065 0.8974 -0.0040 0.0978  -0.1686 260 GLN A C   
1967 O O   . GLN A 267 ? 0.3610 0.7876 0.8825 -0.0209 0.1232  -0.1577 260 GLN A O   
1968 C CB  . GLN A 267 ? 0.4004 0.8520 0.9519 0.0237  0.0690  -0.2015 260 GLN A CB  
1969 N N   . THR A 268 ? 0.3576 0.7514 0.8489 -0.0017 0.0758  -0.1662 261 THR A N   
1970 C CA  . THR A 268 ? 0.4651 0.8402 0.9518 -0.0196 0.0800  -0.1537 261 THR A CA  
1971 C C   . THR A 268 ? 0.4420 0.8054 0.9009 -0.0296 0.1086  -0.1323 261 THR A C   
1972 O O   . THR A 268 ? 0.4464 0.8027 0.9136 -0.0475 0.1265  -0.1185 261 THR A O   
1973 C CB  . THR A 268 ? 0.4481 0.8008 0.9153 -0.0118 0.0505  -0.1557 261 THR A CB  
1974 O OG1 . THR A 268 ? 0.4496 0.8149 0.9355 0.0006  0.0246  -0.1726 261 THR A OG1 
1975 C CG2 . THR A 268 ? 0.3665 0.6990 0.8309 -0.0294 0.0527  -0.1463 261 THR A CG2 
1976 N N   . ARG A 269 ? 0.4023 0.7622 0.8263 -0.0170 0.1132  -0.1289 262 ARG A N   
1977 C CA  . ARG A 269 ? 0.4063 0.7576 0.7955 -0.0232 0.1389  -0.1086 262 ARG A CA  
1978 C C   . ARG A 269 ? 0.5196 0.8917 0.9199 -0.0321 0.1698  -0.0973 262 ARG A C   
1979 O O   . ARG A 269 ? 0.4538 0.8163 0.8338 -0.0424 0.1918  -0.0733 262 ARG A O   
1980 C CB  . ARG A 269 ? 0.4210 0.7681 0.7696 -0.0058 0.1351  -0.1134 262 ARG A CB  
1981 C CG  . ARG A 269 ? 0.2918 0.6000 0.6040 0.0003  0.1089  -0.1090 262 ARG A CG  
1982 C CD  . ARG A 269 ? 0.3543 0.6316 0.6330 -0.0127 0.1150  -0.0840 262 ARG A CD  
1983 N NE  . ARG A 269 ? 0.3862 0.6717 0.6402 -0.0168 0.1440  -0.0672 262 ARG A NE  
1984 C CZ  . ARG A 269 ? 0.3240 0.6036 0.5294 -0.0063 0.1463  -0.0624 262 ARG A CZ  
1985 N NH1 . ARG A 269 ? 0.2575 0.5191 0.4383 0.0061  0.1231  -0.0733 262 ARG A NH1 
1986 N NH2 . ARG A 269 ? 0.4122 0.7064 0.5947 -0.0079 0.1732  -0.0465 262 ARG A NH2 
1987 N N   . ALA A 270 ? 0.3677 0.7683 0.7989 -0.0272 0.1720  -0.1120 263 ALA A N   
1988 C CA  . ALA A 270 ? 0.3726 0.7971 0.8173 -0.0351 0.2022  -0.1008 263 ALA A CA  
1989 C C   . ALA A 270 ? 0.4740 0.8963 0.9570 -0.0564 0.2104  -0.0920 263 ALA A C   
1990 O O   . ALA A 270 ? 0.5092 0.9386 0.9930 -0.0673 0.2382  -0.0715 263 ALA A O   
1991 C CB  . ALA A 270 ? 0.3639 0.8209 0.8315 -0.0225 0.2029  -0.1210 263 ALA A CB  
1992 N N   . LYS A 271 ? 0.4457 0.8582 0.9588 -0.0614 0.1860  -0.1075 264 LYS A N   
1993 C CA  . LYS A 271 ? 0.4504 0.8603 1.0044 -0.0804 0.1904  -0.1069 264 LYS A CA  
1994 C C   . LYS A 271 ? 0.4879 0.8598 1.0291 -0.0919 0.1844  -0.0948 264 LYS A C   
1995 O O   . LYS A 271 ? 0.5417 0.9059 1.1169 -0.1066 0.1845  -0.0984 264 LYS A O   
1996 C CB  . LYS A 271 ? 0.4502 0.8802 1.0493 -0.0769 0.1673  -0.1367 264 LYS A CB  
1997 N N   . THR A 272 ? 0.5079 0.8557 1.0030 -0.0852 0.1793  -0.0824 265 THR A N   
1998 C CA  . THR A 272 ? 0.4525 0.7634 0.9336 -0.0949 0.1751  -0.0696 265 THR A CA  
1999 C C   . THR A 272 ? 0.5137 0.8056 0.9444 -0.0928 0.1934  -0.0405 265 THR A C   
2000 O O   . THR A 272 ? 0.4837 0.7821 0.8791 -0.0785 0.1916  -0.0404 265 THR A O   
2001 C CB  . THR A 272 ? 0.5729 0.8712 1.0502 -0.0876 0.1413  -0.0881 265 THR A CB  
2002 O OG1 . THR A 272 ? 0.6759 0.9757 1.1174 -0.0709 0.1312  -0.0894 265 THR A OG1 
2003 C CG2 . THR A 272 ? 0.5718 0.8918 1.0902 -0.0851 0.1202  -0.1166 265 THR A CG2 
2004 N N   . SER A 273 ? 0.5469 0.8146 0.9735 -0.1055 0.2098  -0.0171 266 SER A N   
2005 C CA  . SER A 273 ? 0.5565 0.8035 0.9315 -0.1018 0.2242  0.0126  266 SER A CA  
2006 C C   . SER A 273 ? 0.4054 0.6271 0.7488 -0.0940 0.2041  0.0110  266 SER A C   
2007 O O   . SER A 273 ? 0.4229 0.6350 0.7868 -0.0960 0.1811  -0.0079 266 SER A O   
2008 C CB  . SER A 273 ? 0.5400 0.7617 0.9209 -0.1153 0.2421  0.0374  266 SER A CB  
2009 O OG  . SER A 273 ? 0.5412 0.7319 0.9446 -0.1235 0.2263  0.0295  266 SER A OG  
2010 N N   . ILE A 274 ? 0.5439 0.7571 0.8345 -0.0839 0.2121  0.0306  267 ILE A N   
2011 C CA  . ILE A 274 ? 0.4946 0.6823 0.7542 -0.0770 0.1961  0.0324  267 ILE A CA  
2012 C C   . ILE A 274 ? 0.5137 0.6653 0.7871 -0.0881 0.1877  0.0397  267 ILE A C   
2013 O O   . ILE A 274 ? 0.4274 0.5652 0.7064 -0.0879 0.1653  0.0251  267 ILE A O   
2014 C CB  . ILE A 274 ? 0.4724 0.6565 0.6690 -0.0629 0.2046  0.0533  267 ILE A CB  
2015 C CG1 . ILE A 274 ? 0.4930 0.7100 0.6708 -0.0484 0.2023  0.0355  267 ILE A CG1 
2016 C CG2 . ILE A 274 ? 0.4309 0.5809 0.5891 -0.0558 0.1806  0.0579  267 ILE A CG2 
2017 C CD1 . ILE A 274 ? 0.4129 0.6293 0.5971 -0.0403 0.1699  0.0052  267 ILE A CD1 
2018 N N   . ASN A 275 ? 0.6096 0.7453 0.8866 -0.0962 0.2036  0.0606  268 ASN A N   
2019 C CA  . ASN A 275 ? 0.6448 0.7465 0.9413 -0.1054 0.1970  0.0632  268 ASN A CA  
2020 C C   . ASN A 275 ? 0.6555 0.7640 1.0011 -0.1137 0.1786  0.0307  268 ASN A C   
2021 O O   . ASN A 275 ? 0.5933 0.6809 0.9429 -0.1148 0.1611  0.0207  268 ASN A O   
2022 C CB  . ASN A 275 ? 0.7572 0.8461 1.0631 -0.1128 0.2194  0.0861  268 ASN A CB  
2023 C CG  . ASN A 275 ? 0.7009 0.7798 0.9523 -0.1019 0.2323  0.1185  268 ASN A CG  
2024 O OD1 . ASN A 275 ? 0.8442 0.9179 1.0511 -0.0891 0.2214  0.1234  268 ASN A OD1 
2025 N ND2 . ASN A 275 ? 0.7209 0.7981 0.9754 -0.1060 0.2546  0.1400  268 ASN A ND2 
2026 N N   . ASP A 276 ? 0.5501 0.6910 0.9309 -0.1174 0.1805  0.0125  269 ASP A N   
2027 C CA  . ASP A 276 ? 0.5963 0.7486 1.0214 -0.1224 0.1609  -0.0196 269 ASP A CA  
2028 C C   . ASP A 276 ? 0.5496 0.7157 0.9648 -0.1114 0.1332  -0.0420 269 ASP A C   
2029 O O   . ASP A 276 ? 0.6227 0.7929 1.0602 -0.1116 0.1111  -0.0665 269 ASP A O   
2030 C CB  . ASP A 276 ? 0.4847 0.6678 0.9518 -0.1288 0.1722  -0.0306 269 ASP A CB  
2031 N N   . LEU A 277 ? 0.4993 0.6738 0.8805 -0.1001 0.1333  -0.0351 270 LEU A N   
2032 C CA  . LEU A 277 ? 0.6219 0.8058 0.9909 -0.0874 0.1053  -0.0545 270 LEU A CA  
2033 C C   . LEU A 277 ? 0.7013 0.8543 1.0463 -0.0854 0.0839  -0.0553 270 LEU A C   
2034 O O   . LEU A 277 ? 0.6957 0.8505 1.0233 -0.0733 0.0573  -0.0692 270 LEU A O   
2035 C CB  . LEU A 277 ? 0.6010 0.7877 0.9210 -0.0706 0.1054  -0.0458 270 LEU A CB  
2036 C CG  . LEU A 277 ? 0.6078 0.8093 0.9218 -0.0542 0.0800  -0.0659 270 LEU A CG  
2037 C CD1 . LEU A 277 ? 0.5534 0.7941 0.9233 -0.0554 0.0788  -0.0883 270 LEU A CD1 
2038 C CD2 . LEU A 277 ? 0.6215 0.8212 0.8923 -0.0397 0.0825  -0.0592 270 LEU A CD2 
2039 N N   . LEU A 278 ? 0.8211 0.9460 1.1648 -0.0957 0.0962  -0.0396 271 LEU A N   
2040 C CA  . LEU A 278 ? 0.7534 0.8537 1.0893 -0.0965 0.0787  -0.0458 271 LEU A CA  
2041 C C   . LEU A 278 ? 0.7151 0.7973 1.0816 -0.1092 0.0909  -0.0437 271 LEU A C   
2042 O O   . LEU A 278 ? 0.5331 0.6144 0.9133 -0.1157 0.1135  -0.0290 271 LEU A O   
2043 C CB  . LEU A 278 ? 0.6120 0.6833 0.8867 -0.0850 0.0735  -0.0259 271 LEU A CB  
2044 C CG  . LEU A 278 ? 0.7414 0.8219 0.9732 -0.0687 0.0631  -0.0239 271 LEU A CG  
2045 C CD1 . LEU A 278 ? 0.7917 0.8796 1.0068 -0.0664 0.0852  -0.0054 271 LEU A CD1 
2046 C CD2 . LEU A 278 ? 0.4919 0.5496 0.6785 -0.0584 0.0456  -0.0194 271 LEU A CD2 
2047 O OXT . LEU A 278 ? 0.6746 0.7422 1.0478 -0.1104 0.0777  -0.0566 271 LEU A OXT 
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