data_9MZX
# 
_entry.id   9MZX 
# 
_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   9MZX         pdb_00009mzx 10.2210/pdb9mzx/pdb 
WWPDB D_1000291536 ?            ?                   
# 
_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       2025-05-28 
_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                        9MZX 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rachel.kubiak@merck.com 
_pdbx_contact_author.name_first         Rachel 
_pdbx_contact_author.name_last          Palte 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6146-0551 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lesburg, C.A.' 1 ? 
'Palte, R.L.'   2 ? 
'Maskos, K.'    3 ? 
'Thomsen, M.'   4 ? 
'Lammens, A.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                811 
_citation.page_last                 818 
_citation.title                     'The Discovery of Bridged Benzoazepine Amides as Selective Allosteric Modulators of RIPK1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.5c00063 
_citation.pdbx_database_id_PubMed   40365380 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, J.L.'        1  0009-0008-1574-1000 
primary 'Methot, J.L.'      2  0000-0003-3374-181X 
primary 'Mitcheltree, M.J.' 3  0000-0003-3774-628X 
primary 'Musacchio, A.'     4  ?                   
primary 'Corcoran, E.B.'    5  ?                   
primary 'Feng, G.'          6  ?                   
primary 'Lammens, A.'       7  ?                   
primary 'Maskos, K.'        8  ?                   
primary 'Palte, R.L.'       9  ?                   
primary 'Rickard, M.M.'     10 ?                   
primary 'Otte, K.M.'        11 ?                   
primary 'Mansueto, M.S.'    12 ?                   
primary 'Venkat, S.'        13 ?                   
primary 'Sondey, C.'        14 ?                   
primary 'Thomsen, M.'       15 ?                   
primary 'Lesburg, C.A.'     16 0000-0001-7245-7331 
primary 'Fradera, X.'       17 ?                   
primary 'Fell, M.J.'        18 ?                   
primary 'DiMauro, E.F.'     19 0009-0009-5054-1140 
primary 'Siliphaivanh, P.'  20 ?                   
# 
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 'Receptor-interacting serine/threonine-protein kinase 1'                                 32866.012 2  2.7.11.1 ? 
? ? 
2 non-polymer syn '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-2,2-dimethylpropan-1-one' 245.317   2  ?        ? 
? ? 
3 non-polymer syn 'IODIDE ION'                                                                             126.904   7  ?        ? 
? ? 
4 water       nat water                                                                                    18.015    26 ?        ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell death protein RIP,Receptor-interacting protein 1,RIP-1' 
# 
_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       
;SLNVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE
GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMW
SKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGN
RPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SLNVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE
GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMW
SKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGN
RPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-2,2-dimethylpropan-1-one' A1BU4 
3 'IODIDE ION'                                                                             IOD   
4 water                                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LEU n 
1 3   ASN n 
1 4   VAL n 
1 5   ILE n 
1 6   LYS n 
1 7   MET n 
1 8   LYS n 
1 9   SER n 
1 10  SER n 
1 11  ASP n 
1 12  PHE n 
1 13  LEU n 
1 14  GLU n 
1 15  SER n 
1 16  ALA n 
1 17  GLU n 
1 18  LEU n 
1 19  ASP n 
1 20  SER n 
1 21  GLY n 
1 22  GLY n 
1 23  PHE n 
1 24  GLY n 
1 25  LYS n 
1 26  VAL n 
1 27  SER n 
1 28  LEU n 
1 29  ALA n 
1 30  PHE n 
1 31  HIS n 
1 32  ARG n 
1 33  THR n 
1 34  GLN n 
1 35  GLY n 
1 36  LEU n 
1 37  MET n 
1 38  ILE n 
1 39  MET n 
1 40  LYS n 
1 41  THR n 
1 42  VAL n 
1 43  TYR n 
1 44  LYS n 
1 45  GLY n 
1 46  PRO n 
1 47  ASN n 
1 48  CYS n 
1 49  ILE n 
1 50  GLU n 
1 51  HIS n 
1 52  ASN n 
1 53  GLU n 
1 54  ALA n 
1 55  LEU n 
1 56  LEU n 
1 57  GLU n 
1 58  GLU n 
1 59  ALA n 
1 60  LYS n 
1 61  MET n 
1 62  MET n 
1 63  ASN n 
1 64  ARG n 
1 65  LEU n 
1 66  ARG n 
1 67  HIS n 
1 68  SER n 
1 69  ARG n 
1 70  VAL n 
1 71  VAL n 
1 72  LYS n 
1 73  LEU n 
1 74  LEU n 
1 75  GLY n 
1 76  VAL n 
1 77  ILE n 
1 78  ILE n 
1 79  GLU n 
1 80  GLU n 
1 81  GLY n 
1 82  LYS n 
1 83  TYR n 
1 84  SER n 
1 85  LEU n 
1 86  VAL n 
1 87  MET n 
1 88  GLU n 
1 89  TYR n 
1 90  MET n 
1 91  GLU n 
1 92  LYS n 
1 93  GLY n 
1 94  ASN n 
1 95  LEU n 
1 96  MET n 
1 97  HIS n 
1 98  VAL n 
1 99  LEU n 
1 100 LYS n 
1 101 ALA n 
1 102 GLU n 
1 103 MET n 
1 104 SER n 
1 105 THR n 
1 106 PRO n 
1 107 LEU n 
1 108 SER n 
1 109 VAL n 
1 110 LYS n 
1 111 GLY n 
1 112 ARG n 
1 113 ILE n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ILE n 
1 118 ILE n 
1 119 GLU n 
1 120 GLY n 
1 121 MET n 
1 122 ALA n 
1 123 TYR n 
1 124 LEU n 
1 125 HIS n 
1 126 GLY n 
1 127 LYS n 
1 128 GLY n 
1 129 VAL n 
1 130 ILE n 
1 131 HIS n 
1 132 LYS n 
1 133 ASP n 
1 134 LEU n 
1 135 LYS n 
1 136 PRO n 
1 137 GLU n 
1 138 ASN n 
1 139 ILE n 
1 140 LEU n 
1 141 VAL n 
1 142 ASP n 
1 143 ASN n 
1 144 ASP n 
1 145 PHE n 
1 146 HIS n 
1 147 ILE n 
1 148 LYS n 
1 149 ILE n 
1 150 ALA n 
1 151 ASP n 
1 152 LEU n 
1 153 GLY n 
1 154 LEU n 
1 155 ALA n 
1 156 SER n 
1 157 PHE n 
1 158 LYS n 
1 159 MET n 
1 160 TRP n 
1 161 SER n 
1 162 LYS n 
1 163 LEU n 
1 164 ASN n 
1 165 ASN n 
1 166 GLU n 
1 167 GLU n 
1 168 HIS n 
1 169 ASN n 
1 170 GLU n 
1 171 LEU n 
1 172 ARG n 
1 173 GLU n 
1 174 VAL n 
1 175 ASP n 
1 176 GLY n 
1 177 THR n 
1 178 ALA n 
1 179 LYS n 
1 180 LYS n 
1 181 ASN n 
1 182 GLY n 
1 183 GLY n 
1 184 THR n 
1 185 LEU n 
1 186 TYR n 
1 187 TYR n 
1 188 MET n 
1 189 ALA n 
1 190 PRO n 
1 191 GLU n 
1 192 HIS n 
1 193 LEU n 
1 194 ASN n 
1 195 ASP n 
1 196 VAL n 
1 197 ASN n 
1 198 ALA n 
1 199 LYS n 
1 200 PRO n 
1 201 THR n 
1 202 GLU n 
1 203 LYS n 
1 204 SER n 
1 205 ASP n 
1 206 VAL n 
1 207 TYR n 
1 208 SER n 
1 209 PHE n 
1 210 ALA n 
1 211 VAL n 
1 212 VAL n 
1 213 LEU n 
1 214 TRP n 
1 215 ALA n 
1 216 ILE n 
1 217 PHE n 
1 218 ALA n 
1 219 ASN n 
1 220 LYS n 
1 221 GLU n 
1 222 PRO n 
1 223 TYR n 
1 224 GLU n 
1 225 ASN n 
1 226 ALA n 
1 227 ILE n 
1 228 ALA n 
1 229 GLU n 
1 230 GLN n 
1 231 GLN n 
1 232 LEU n 
1 233 ILE n 
1 234 MET n 
1 235 ALA n 
1 236 ILE n 
1 237 LYS n 
1 238 SER n 
1 239 GLY n 
1 240 ASN n 
1 241 ARG n 
1 242 PRO n 
1 243 ASP n 
1 244 VAL n 
1 245 ASP n 
1 246 ASP n 
1 247 ILE n 
1 248 THR n 
1 249 GLU n 
1 250 TYR n 
1 251 CYS n 
1 252 PRO n 
1 253 ARG n 
1 254 GLU n 
1 255 ILE n 
1 256 ILE n 
1 257 SER n 
1 258 LEU n 
1 259 MET n 
1 260 LYS n 
1 261 LEU n 
1 262 CYS n 
1 263 TRP n 
1 264 GLU n 
1 265 ALA n 
1 266 ASN n 
1 267 PRO n 
1 268 GLU n 
1 269 ALA n 
1 270 ARG n 
1 271 PRO n 
1 272 THR n 
1 273 PHE n 
1 274 PRO n 
1 275 GLY n 
1 276 ILE n 
1 277 GLU n 
1 278 GLU n 
1 279 LYS n 
1 280 PHE n 
1 281 ARG n 
1 282 PRO n 
1 283 PHE n 
1 284 TYR n 
1 285 LEU n 
1 286 SER n 
1 287 GLN n 
1 288 LEU n 
1 289 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   289 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RIPK1, RIP, RIP1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BU4 non-polymer         . '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-2,2-dimethylpropan-1-one' ? 
'C15 H19 N O2'   245.317 
ALA   'L-peptide linking' y ALANINE                                                                                  ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                 ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                               ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                          ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                 ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                          ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                  ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                    ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                               ? 
'C6 H13 N O2'    131.173 
IOD   non-polymer         . 'IODIDE ION'                                                                             ? 'I -1' 
126.904 
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   SER 1   6   6   SER SER A . n 
A 1 2   LEU 2   7   7   LEU LEU A . n 
A 1 3   ASN 3   8   8   ASN ASN A . n 
A 1 4   VAL 4   9   9   VAL VAL A . n 
A 1 5   ILE 5   10  10  ILE ILE A . n 
A 1 6   LYS 6   11  11  LYS LYS A . n 
A 1 7   MET 7   12  12  MET MET A . n 
A 1 8   LYS 8   13  13  LYS LYS A . n 
A 1 9   SER 9   14  14  SER SER A . n 
A 1 10  SER 10  15  15  SER SER A . n 
A 1 11  ASP 11  16  16  ASP ASP A . n 
A 1 12  PHE 12  17  17  PHE PHE A . n 
A 1 13  LEU 13  18  18  LEU LEU A . n 
A 1 14  GLU 14  19  19  GLU GLU A . n 
A 1 15  SER 15  20  20  SER SER A . n 
A 1 16  ALA 16  21  21  ALA ALA A . n 
A 1 17  GLU 17  22  22  GLU GLU A . n 
A 1 18  LEU 18  23  ?   ?   ?   A . n 
A 1 19  ASP 19  24  ?   ?   ?   A . n 
A 1 20  SER 20  25  ?   ?   ?   A . n 
A 1 21  GLY 21  26  ?   ?   ?   A . n 
A 1 22  GLY 22  27  ?   ?   ?   A . n 
A 1 23  PHE 23  28  ?   ?   ?   A . n 
A 1 24  GLY 24  29  ?   ?   ?   A . n 
A 1 25  LYS 25  30  30  LYS LYS A . n 
A 1 26  VAL 26  31  31  VAL VAL A . n 
A 1 27  SER 27  32  32  SER SER A . n 
A 1 28  LEU 28  33  33  LEU LEU A . n 
A 1 29  ALA 29  34  34  ALA ALA A . n 
A 1 30  PHE 30  35  35  PHE PHE A . n 
A 1 31  HIS 31  36  36  HIS HIS A . n 
A 1 32  ARG 32  37  37  ARG ARG A . n 
A 1 33  THR 33  38  38  THR THR A . n 
A 1 34  GLN 34  39  39  GLN GLN A . n 
A 1 35  GLY 35  40  40  GLY GLY A . n 
A 1 36  LEU 36  41  41  LEU LEU A . n 
A 1 37  MET 37  42  42  MET MET A . n 
A 1 38  ILE 38  43  43  ILE ILE A . n 
A 1 39  MET 39  44  44  MET MET A . n 
A 1 40  LYS 40  45  45  LYS LYS A . n 
A 1 41  THR 41  46  46  THR THR A . n 
A 1 42  VAL 42  47  47  VAL VAL A . n 
A 1 43  TYR 43  48  48  TYR TYR A . n 
A 1 44  LYS 44  49  49  LYS LYS A . n 
A 1 45  GLY 45  50  50  GLY GLY A . n 
A 1 46  PRO 46  51  51  PRO PRO A . n 
A 1 47  ASN 47  52  52  ASN ASN A . n 
A 1 48  CYS 48  53  53  CYS CYS A . n 
A 1 49  ILE 49  54  54  ILE ILE A . n 
A 1 50  GLU 50  55  55  GLU GLU A . n 
A 1 51  HIS 51  56  56  HIS HIS A . n 
A 1 52  ASN 52  57  57  ASN ASN A . n 
A 1 53  GLU 53  58  58  GLU GLU A . n 
A 1 54  ALA 54  59  59  ALA ALA A . n 
A 1 55  LEU 55  60  60  LEU LEU A . n 
A 1 56  LEU 56  61  61  LEU LEU A . n 
A 1 57  GLU 57  62  62  GLU GLU A . n 
A 1 58  GLU 58  63  63  GLU GLU A . n 
A 1 59  ALA 59  64  64  ALA ALA A . n 
A 1 60  LYS 60  65  65  LYS LYS A . n 
A 1 61  MET 61  66  66  MET MET A . n 
A 1 62  MET 62  67  67  MET MET A . n 
A 1 63  ASN 63  68  68  ASN ASN A . n 
A 1 64  ARG 64  69  69  ARG ARG A . n 
A 1 65  LEU 65  70  70  LEU LEU A . n 
A 1 66  ARG 66  71  71  ARG ARG A . n 
A 1 67  HIS 67  72  72  HIS HIS A . n 
A 1 68  SER 68  73  73  SER SER A . n 
A 1 69  ARG 69  74  74  ARG ARG A . n 
A 1 70  VAL 70  75  75  VAL VAL A . n 
A 1 71  VAL 71  76  76  VAL VAL A . n 
A 1 72  LYS 72  77  77  LYS LYS A . n 
A 1 73  LEU 73  78  78  LEU LEU A . n 
A 1 74  LEU 74  79  79  LEU LEU A . n 
A 1 75  GLY 75  80  80  GLY GLY A . n 
A 1 76  VAL 76  81  81  VAL VAL A . n 
A 1 77  ILE 77  82  82  ILE ILE A . n 
A 1 78  ILE 78  83  83  ILE ILE A . n 
A 1 79  GLU 79  84  84  GLU GLU A . n 
A 1 80  GLU 80  85  85  GLU GLU A . n 
A 1 81  GLY 81  86  86  GLY GLY A . n 
A 1 82  LYS 82  87  87  LYS LYS A . n 
A 1 83  TYR 83  88  88  TYR TYR A . n 
A 1 84  SER 84  89  89  SER SER A . n 
A 1 85  LEU 85  90  90  LEU LEU A . n 
A 1 86  VAL 86  91  91  VAL VAL A . n 
A 1 87  MET 87  92  92  MET MET A . n 
A 1 88  GLU 88  93  93  GLU GLU A . n 
A 1 89  TYR 89  94  94  TYR TYR A . n 
A 1 90  MET 90  95  95  MET MET A . n 
A 1 91  GLU 91  96  96  GLU GLU A . n 
A 1 92  LYS 92  97  97  LYS LYS A . n 
A 1 93  GLY 93  98  98  GLY GLY A . n 
A 1 94  ASN 94  99  99  ASN ASN A . n 
A 1 95  LEU 95  100 100 LEU LEU A . n 
A 1 96  MET 96  101 101 MET MET A . n 
A 1 97  HIS 97  102 102 HIS HIS A . n 
A 1 98  VAL 98  103 103 VAL VAL A . n 
A 1 99  LEU 99  104 104 LEU LEU A . n 
A 1 100 LYS 100 105 105 LYS LYS A . n 
A 1 101 ALA 101 106 106 ALA ALA A . n 
A 1 102 GLU 102 107 107 GLU GLU A . n 
A 1 103 MET 103 108 108 MET MET A . n 
A 1 104 SER 104 109 109 SER SER A . n 
A 1 105 THR 105 110 110 THR THR A . n 
A 1 106 PRO 106 111 111 PRO PRO A . n 
A 1 107 LEU 107 112 112 LEU LEU A . n 
A 1 108 SER 108 113 113 SER SER A . n 
A 1 109 VAL 109 114 114 VAL VAL A . n 
A 1 110 LYS 110 115 115 LYS LYS A . n 
A 1 111 GLY 111 116 116 GLY GLY A . n 
A 1 112 ARG 112 117 117 ARG ARG A . n 
A 1 113 ILE 113 118 118 ILE ILE A . n 
A 1 114 ILE 114 119 119 ILE ILE A . n 
A 1 115 LEU 115 120 120 LEU LEU A . n 
A 1 116 GLU 116 121 121 GLU GLU A . n 
A 1 117 ILE 117 122 122 ILE ILE A . n 
A 1 118 ILE 118 123 123 ILE ILE A . n 
A 1 119 GLU 119 124 124 GLU GLU A . n 
A 1 120 GLY 120 125 125 GLY GLY A . n 
A 1 121 MET 121 126 126 MET MET A . n 
A 1 122 ALA 122 127 127 ALA ALA A . n 
A 1 123 TYR 123 128 128 TYR TYR A . n 
A 1 124 LEU 124 129 129 LEU LEU A . n 
A 1 125 HIS 125 130 130 HIS HIS A . n 
A 1 126 GLY 126 131 131 GLY GLY A . n 
A 1 127 LYS 127 132 132 LYS LYS A . n 
A 1 128 GLY 128 133 133 GLY GLY A . n 
A 1 129 VAL 129 134 134 VAL VAL A . n 
A 1 130 ILE 130 135 135 ILE ILE A . n 
A 1 131 HIS 131 136 136 HIS HIS A . n 
A 1 132 LYS 132 137 137 LYS LYS A . n 
A 1 133 ASP 133 138 138 ASP ASP A . n 
A 1 134 LEU 134 139 139 LEU LEU A . n 
A 1 135 LYS 135 140 140 LYS LYS A . n 
A 1 136 PRO 136 141 141 PRO PRO A . n 
A 1 137 GLU 137 142 142 GLU GLU A . n 
A 1 138 ASN 138 143 143 ASN ASN A . n 
A 1 139 ILE 139 144 144 ILE ILE A . n 
A 1 140 LEU 140 145 145 LEU LEU A . n 
A 1 141 VAL 141 146 146 VAL VAL A . n 
A 1 142 ASP 142 147 147 ASP ASP A . n 
A 1 143 ASN 143 148 148 ASN ASN A . n 
A 1 144 ASP 144 149 149 ASP ASP A . n 
A 1 145 PHE 145 150 150 PHE PHE A . n 
A 1 146 HIS 146 151 151 HIS HIS A . n 
A 1 147 ILE 147 152 152 ILE ILE A . n 
A 1 148 LYS 148 153 153 LYS LYS A . n 
A 1 149 ILE 149 154 154 ILE ILE A . n 
A 1 150 ALA 150 155 155 ALA ALA A . n 
A 1 151 ASP 151 156 156 ASP ASP A . n 
A 1 152 LEU 152 157 157 LEU LEU A . n 
A 1 153 GLY 153 158 158 GLY GLY A . n 
A 1 154 LEU 154 159 159 LEU LEU A . n 
A 1 155 ALA 155 160 160 ALA ALA A . n 
A 1 156 SER 156 161 161 SER SER A . n 
A 1 157 PHE 157 162 162 PHE PHE A . n 
A 1 158 LYS 158 163 163 LYS LYS A . n 
A 1 159 MET 159 164 164 MET MET A . n 
A 1 160 TRP 160 165 165 TRP TRP A . n 
A 1 161 SER 161 166 166 SER SER A . n 
A 1 162 LYS 162 167 167 LYS LYS A . n 
A 1 163 LEU 163 168 168 LEU LEU A . n 
A 1 164 ASN 164 169 169 ASN ASN A . n 
A 1 165 ASN 165 170 170 ASN ASN A . n 
A 1 166 GLU 166 171 ?   ?   ?   A . n 
A 1 167 GLU 167 172 ?   ?   ?   A . n 
A 1 168 HIS 168 173 ?   ?   ?   A . n 
A 1 169 ASN 169 174 ?   ?   ?   A . n 
A 1 170 GLU 170 175 ?   ?   ?   A . n 
A 1 171 LEU 171 176 ?   ?   ?   A . n 
A 1 172 ARG 172 177 ?   ?   ?   A . n 
A 1 173 GLU 173 178 ?   ?   ?   A . n 
A 1 174 VAL 174 179 ?   ?   ?   A . n 
A 1 175 ASP 175 180 ?   ?   ?   A . n 
A 1 176 GLY 176 181 ?   ?   ?   A . n 
A 1 177 THR 177 182 ?   ?   ?   A . n 
A 1 178 ALA 178 183 ?   ?   ?   A . n 
A 1 179 LYS 179 184 ?   ?   ?   A . n 
A 1 180 LYS 180 185 ?   ?   ?   A . n 
A 1 181 ASN 181 186 ?   ?   ?   A . n 
A 1 182 GLY 182 187 ?   ?   ?   A . n 
A 1 183 GLY 183 188 188 GLY GLY A . n 
A 1 184 THR 184 189 189 THR THR A . n 
A 1 185 LEU 185 190 190 LEU LEU A . n 
A 1 186 TYR 186 191 191 TYR TYR A . n 
A 1 187 TYR 187 192 192 TYR TYR A . n 
A 1 188 MET 188 193 193 MET MET A . n 
A 1 189 ALA 189 194 194 ALA ALA A . n 
A 1 190 PRO 190 195 195 PRO PRO A . n 
A 1 191 GLU 191 196 196 GLU GLU A . n 
A 1 192 HIS 192 197 197 HIS HIS A . n 
A 1 193 LEU 193 198 198 LEU LEU A . n 
A 1 194 ASN 194 199 199 ASN ASN A . n 
A 1 195 ASP 195 200 200 ASP ASP A . n 
A 1 196 VAL 196 201 201 VAL VAL A . n 
A 1 197 ASN 197 202 202 ASN ASN A . n 
A 1 198 ALA 198 203 203 ALA ALA A . n 
A 1 199 LYS 199 204 204 LYS LYS A . n 
A 1 200 PRO 200 205 205 PRO PRO A . n 
A 1 201 THR 201 206 206 THR THR A . n 
A 1 202 GLU 202 207 207 GLU GLU A . n 
A 1 203 LYS 203 208 208 LYS LYS A . n 
A 1 204 SER 204 209 209 SER SER A . n 
A 1 205 ASP 205 210 210 ASP ASP A . n 
A 1 206 VAL 206 211 211 VAL VAL A . n 
A 1 207 TYR 207 212 212 TYR TYR A . n 
A 1 208 SER 208 213 213 SER SER A . n 
A 1 209 PHE 209 214 214 PHE PHE A . n 
A 1 210 ALA 210 215 215 ALA ALA A . n 
A 1 211 VAL 211 216 216 VAL VAL A . n 
A 1 212 VAL 212 217 217 VAL VAL A . n 
A 1 213 LEU 213 218 218 LEU LEU A . n 
A 1 214 TRP 214 219 219 TRP TRP A . n 
A 1 215 ALA 215 220 220 ALA ALA A . n 
A 1 216 ILE 216 221 221 ILE ILE A . n 
A 1 217 PHE 217 222 222 PHE PHE A . n 
A 1 218 ALA 218 223 223 ALA ALA A . n 
A 1 219 ASN 219 224 224 ASN ASN A . n 
A 1 220 LYS 220 225 225 LYS LYS A . n 
A 1 221 GLU 221 226 226 GLU GLU A . n 
A 1 222 PRO 222 227 227 PRO PRO A . n 
A 1 223 TYR 223 228 228 TYR TYR A . n 
A 1 224 GLU 224 229 229 GLU GLU A . n 
A 1 225 ASN 225 230 230 ASN ASN A . n 
A 1 226 ALA 226 231 231 ALA ALA A . n 
A 1 227 ILE 227 232 232 ILE ILE A . n 
A 1 228 ALA 228 233 233 ALA ALA A . n 
A 1 229 GLU 229 234 234 GLU GLU A . n 
A 1 230 GLN 230 235 235 GLN GLN A . n 
A 1 231 GLN 231 236 236 GLN GLN A . n 
A 1 232 LEU 232 237 237 LEU LEU A . n 
A 1 233 ILE 233 238 238 ILE ILE A . n 
A 1 234 MET 234 239 239 MET MET A . n 
A 1 235 ALA 235 240 240 ALA ALA A . n 
A 1 236 ILE 236 241 241 ILE ILE A . n 
A 1 237 LYS 237 242 242 LYS LYS A . n 
A 1 238 SER 238 243 243 SER SER A . n 
A 1 239 GLY 239 244 244 GLY GLY A . n 
A 1 240 ASN 240 245 245 ASN ASN A . n 
A 1 241 ARG 241 246 246 ARG ARG A . n 
A 1 242 PRO 242 247 247 PRO PRO A . n 
A 1 243 ASP 243 248 248 ASP ASP A . n 
A 1 244 VAL 244 249 249 VAL VAL A . n 
A 1 245 ASP 245 250 250 ASP ASP A . n 
A 1 246 ASP 246 251 251 ASP ASP A . n 
A 1 247 ILE 247 252 252 ILE ILE A . n 
A 1 248 THR 248 253 253 THR THR A . n 
A 1 249 GLU 249 254 254 GLU GLU A . n 
A 1 250 TYR 250 255 255 TYR TYR A . n 
A 1 251 CYS 251 256 256 CYS CYS A . n 
A 1 252 PRO 252 257 257 PRO PRO A . n 
A 1 253 ARG 253 258 258 ARG ARG A . n 
A 1 254 GLU 254 259 259 GLU GLU A . n 
A 1 255 ILE 255 260 260 ILE ILE A . n 
A 1 256 ILE 256 261 261 ILE ILE A . n 
A 1 257 SER 257 262 262 SER SER A . n 
A 1 258 LEU 258 263 263 LEU LEU A . n 
A 1 259 MET 259 264 264 MET MET A . n 
A 1 260 LYS 260 265 265 LYS LYS A . n 
A 1 261 LEU 261 266 266 LEU LEU A . n 
A 1 262 CYS 262 267 267 CYS CYS A . n 
A 1 263 TRP 263 268 268 TRP TRP A . n 
A 1 264 GLU 264 269 269 GLU GLU A . n 
A 1 265 ALA 265 270 270 ALA ALA A . n 
A 1 266 ASN 266 271 271 ASN ASN A . n 
A 1 267 PRO 267 272 272 PRO PRO A . n 
A 1 268 GLU 268 273 273 GLU GLU A . n 
A 1 269 ALA 269 274 274 ALA ALA A . n 
A 1 270 ARG 270 275 275 ARG ARG A . n 
A 1 271 PRO 271 276 276 PRO PRO A . n 
A 1 272 THR 272 277 277 THR THR A . n 
A 1 273 PHE 273 278 278 PHE PHE A . n 
A 1 274 PRO 274 279 279 PRO PRO A . n 
A 1 275 GLY 275 280 280 GLY GLY A . n 
A 1 276 ILE 276 281 281 ILE ILE A . n 
A 1 277 GLU 277 282 282 GLU GLU A . n 
A 1 278 GLU 278 283 283 GLU GLU A . n 
A 1 279 LYS 279 284 284 LYS LYS A . n 
A 1 280 PHE 280 285 285 PHE PHE A . n 
A 1 281 ARG 281 286 286 ARG ARG A . n 
A 1 282 PRO 282 287 287 PRO PRO A . n 
A 1 283 PHE 283 288 288 PHE PHE A . n 
A 1 284 TYR 284 289 289 TYR TYR A . n 
A 1 285 LEU 285 290 290 LEU LEU A . n 
A 1 286 SER 286 291 291 SER SER A . n 
A 1 287 GLN 287 292 292 GLN GLN A . n 
A 1 288 LEU 288 293 293 LEU LEU A . n 
A 1 289 GLU 289 294 294 GLU GLU A . n 
B 1 1   SER 1   6   6   SER SER B . n 
B 1 2   LEU 2   7   7   LEU LEU B . n 
B 1 3   ASN 3   8   8   ASN ASN B . n 
B 1 4   VAL 4   9   9   VAL VAL B . n 
B 1 5   ILE 5   10  10  ILE ILE B . n 
B 1 6   LYS 6   11  11  LYS LYS B . n 
B 1 7   MET 7   12  12  MET MET B . n 
B 1 8   LYS 8   13  13  LYS LYS B . n 
B 1 9   SER 9   14  14  SER SER B . n 
B 1 10  SER 10  15  15  SER SER B . n 
B 1 11  ASP 11  16  16  ASP ASP B . n 
B 1 12  PHE 12  17  17  PHE PHE B . n 
B 1 13  LEU 13  18  18  LEU LEU B . n 
B 1 14  GLU 14  19  19  GLU GLU B . n 
B 1 15  SER 15  20  ?   ?   ?   B . n 
B 1 16  ALA 16  21  ?   ?   ?   B . n 
B 1 17  GLU 17  22  ?   ?   ?   B . n 
B 1 18  LEU 18  23  ?   ?   ?   B . n 
B 1 19  ASP 19  24  ?   ?   ?   B . n 
B 1 20  SER 20  25  ?   ?   ?   B . n 
B 1 21  GLY 21  26  ?   ?   ?   B . n 
B 1 22  GLY 22  27  ?   ?   ?   B . n 
B 1 23  PHE 23  28  ?   ?   ?   B . n 
B 1 24  GLY 24  29  ?   ?   ?   B . n 
B 1 25  LYS 25  30  30  LYS LYS B . n 
B 1 26  VAL 26  31  31  VAL VAL B . n 
B 1 27  SER 27  32  32  SER SER B . n 
B 1 28  LEU 28  33  33  LEU LEU B . n 
B 1 29  ALA 29  34  34  ALA ALA B . n 
B 1 30  PHE 30  35  35  PHE PHE B . n 
B 1 31  HIS 31  36  36  HIS HIS B . n 
B 1 32  ARG 32  37  37  ARG ARG B . n 
B 1 33  THR 33  38  38  THR THR B . n 
B 1 34  GLN 34  39  39  GLN GLN B . n 
B 1 35  GLY 35  40  40  GLY GLY B . n 
B 1 36  LEU 36  41  41  LEU LEU B . n 
B 1 37  MET 37  42  42  MET MET B . n 
B 1 38  ILE 38  43  43  ILE ILE B . n 
B 1 39  MET 39  44  44  MET MET B . n 
B 1 40  LYS 40  45  45  LYS LYS B . n 
B 1 41  THR 41  46  46  THR THR B . n 
B 1 42  VAL 42  47  47  VAL VAL B . n 
B 1 43  TYR 43  48  48  TYR TYR B . n 
B 1 44  LYS 44  49  49  LYS LYS B . n 
B 1 45  GLY 45  50  50  GLY GLY B . n 
B 1 46  PRO 46  51  51  PRO PRO B . n 
B 1 47  ASN 47  52  52  ASN ASN B . n 
B 1 48  CYS 48  53  53  CYS CYS B . n 
B 1 49  ILE 49  54  54  ILE ILE B . n 
B 1 50  GLU 50  55  55  GLU GLU B . n 
B 1 51  HIS 51  56  56  HIS HIS B . n 
B 1 52  ASN 52  57  57  ASN ASN B . n 
B 1 53  GLU 53  58  58  GLU GLU B . n 
B 1 54  ALA 54  59  59  ALA ALA B . n 
B 1 55  LEU 55  60  60  LEU LEU B . n 
B 1 56  LEU 56  61  61  LEU LEU B . n 
B 1 57  GLU 57  62  62  GLU GLU B . n 
B 1 58  GLU 58  63  63  GLU GLU B . n 
B 1 59  ALA 59  64  64  ALA ALA B . n 
B 1 60  LYS 60  65  65  LYS LYS B . n 
B 1 61  MET 61  66  66  MET MET B . n 
B 1 62  MET 62  67  67  MET MET B . n 
B 1 63  ASN 63  68  68  ASN ASN B . n 
B 1 64  ARG 64  69  69  ARG ARG B . n 
B 1 65  LEU 65  70  70  LEU LEU B . n 
B 1 66  ARG 66  71  71  ARG ARG B . n 
B 1 67  HIS 67  72  72  HIS HIS B . n 
B 1 68  SER 68  73  73  SER SER B . n 
B 1 69  ARG 69  74  74  ARG ARG B . n 
B 1 70  VAL 70  75  75  VAL VAL B . n 
B 1 71  VAL 71  76  76  VAL VAL B . n 
B 1 72  LYS 72  77  77  LYS LYS B . n 
B 1 73  LEU 73  78  78  LEU LEU B . n 
B 1 74  LEU 74  79  79  LEU LEU B . n 
B 1 75  GLY 75  80  80  GLY GLY B . n 
B 1 76  VAL 76  81  81  VAL VAL B . n 
B 1 77  ILE 77  82  82  ILE ILE B . n 
B 1 78  ILE 78  83  83  ILE ILE B . n 
B 1 79  GLU 79  84  84  GLU GLU B . n 
B 1 80  GLU 80  85  85  GLU GLU B . n 
B 1 81  GLY 81  86  86  GLY GLY B . n 
B 1 82  LYS 82  87  87  LYS LYS B . n 
B 1 83  TYR 83  88  88  TYR TYR B . n 
B 1 84  SER 84  89  89  SER SER B . n 
B 1 85  LEU 85  90  90  LEU LEU B . n 
B 1 86  VAL 86  91  91  VAL VAL B . n 
B 1 87  MET 87  92  92  MET MET B . n 
B 1 88  GLU 88  93  93  GLU GLU B . n 
B 1 89  TYR 89  94  94  TYR TYR B . n 
B 1 90  MET 90  95  95  MET MET B . n 
B 1 91  GLU 91  96  96  GLU GLU B . n 
B 1 92  LYS 92  97  97  LYS LYS B . n 
B 1 93  GLY 93  98  98  GLY GLY B . n 
B 1 94  ASN 94  99  99  ASN ASN B . n 
B 1 95  LEU 95  100 100 LEU LEU B . n 
B 1 96  MET 96  101 101 MET MET B . n 
B 1 97  HIS 97  102 102 HIS HIS B . n 
B 1 98  VAL 98  103 103 VAL VAL B . n 
B 1 99  LEU 99  104 104 LEU LEU B . n 
B 1 100 LYS 100 105 105 LYS LYS B . n 
B 1 101 ALA 101 106 106 ALA ALA B . n 
B 1 102 GLU 102 107 107 GLU GLU B . n 
B 1 103 MET 103 108 108 MET MET B . n 
B 1 104 SER 104 109 109 SER SER B . n 
B 1 105 THR 105 110 110 THR THR B . n 
B 1 106 PRO 106 111 111 PRO PRO B . n 
B 1 107 LEU 107 112 112 LEU LEU B . n 
B 1 108 SER 108 113 113 SER SER B . n 
B 1 109 VAL 109 114 114 VAL VAL B . n 
B 1 110 LYS 110 115 115 LYS LYS B . n 
B 1 111 GLY 111 116 116 GLY GLY B . n 
B 1 112 ARG 112 117 117 ARG ARG B . n 
B 1 113 ILE 113 118 118 ILE ILE B . n 
B 1 114 ILE 114 119 119 ILE ILE B . n 
B 1 115 LEU 115 120 120 LEU LEU B . n 
B 1 116 GLU 116 121 121 GLU GLU B . n 
B 1 117 ILE 117 122 122 ILE ILE B . n 
B 1 118 ILE 118 123 123 ILE ILE B . n 
B 1 119 GLU 119 124 124 GLU GLU B . n 
B 1 120 GLY 120 125 125 GLY GLY B . n 
B 1 121 MET 121 126 126 MET MET B . n 
B 1 122 ALA 122 127 127 ALA ALA B . n 
B 1 123 TYR 123 128 128 TYR TYR B . n 
B 1 124 LEU 124 129 129 LEU LEU B . n 
B 1 125 HIS 125 130 130 HIS HIS B . n 
B 1 126 GLY 126 131 131 GLY GLY B . n 
B 1 127 LYS 127 132 132 LYS LYS B . n 
B 1 128 GLY 128 133 133 GLY GLY B . n 
B 1 129 VAL 129 134 134 VAL VAL B . n 
B 1 130 ILE 130 135 135 ILE ILE B . n 
B 1 131 HIS 131 136 136 HIS HIS B . n 
B 1 132 LYS 132 137 137 LYS LYS B . n 
B 1 133 ASP 133 138 138 ASP ASP B . n 
B 1 134 LEU 134 139 139 LEU LEU B . n 
B 1 135 LYS 135 140 140 LYS LYS B . n 
B 1 136 PRO 136 141 141 PRO PRO B . n 
B 1 137 GLU 137 142 142 GLU GLU B . n 
B 1 138 ASN 138 143 143 ASN ASN B . n 
B 1 139 ILE 139 144 144 ILE ILE B . n 
B 1 140 LEU 140 145 145 LEU LEU B . n 
B 1 141 VAL 141 146 146 VAL VAL B . n 
B 1 142 ASP 142 147 147 ASP ASP B . n 
B 1 143 ASN 143 148 148 ASN ASN B . n 
B 1 144 ASP 144 149 149 ASP ASP B . n 
B 1 145 PHE 145 150 150 PHE PHE B . n 
B 1 146 HIS 146 151 151 HIS HIS B . n 
B 1 147 ILE 147 152 152 ILE ILE B . n 
B 1 148 LYS 148 153 153 LYS LYS B . n 
B 1 149 ILE 149 154 154 ILE ILE B . n 
B 1 150 ALA 150 155 155 ALA ALA B . n 
B 1 151 ASP 151 156 156 ASP ASP B . n 
B 1 152 LEU 152 157 157 LEU LEU B . n 
B 1 153 GLY 153 158 158 GLY GLY B . n 
B 1 154 LEU 154 159 159 LEU LEU B . n 
B 1 155 ALA 155 160 160 ALA ALA B . n 
B 1 156 SER 156 161 161 SER SER B . n 
B 1 157 PHE 157 162 162 PHE PHE B . n 
B 1 158 LYS 158 163 163 LYS LYS B . n 
B 1 159 MET 159 164 164 MET MET B . n 
B 1 160 TRP 160 165 165 TRP TRP B . n 
B 1 161 SER 161 166 166 SER SER B . n 
B 1 162 LYS 162 167 167 LYS LYS B . n 
B 1 163 LEU 163 168 168 LEU LEU B . n 
B 1 164 ASN 164 169 169 ASN ASN B . n 
B 1 165 ASN 165 170 170 ASN ASN B . n 
B 1 166 GLU 166 171 171 GLU GLU B . n 
B 1 167 GLU 167 172 172 GLU GLU B . n 
B 1 168 HIS 168 173 173 HIS HIS B . n 
B 1 169 ASN 169 174 174 ASN ASN B . n 
B 1 170 GLU 170 175 175 GLU GLU B . n 
B 1 171 LEU 171 176 176 LEU LEU B . n 
B 1 172 ARG 172 177 ?   ?   ?   B . n 
B 1 173 GLU 173 178 ?   ?   ?   B . n 
B 1 174 VAL 174 179 ?   ?   ?   B . n 
B 1 175 ASP 175 180 ?   ?   ?   B . n 
B 1 176 GLY 176 181 ?   ?   ?   B . n 
B 1 177 THR 177 182 ?   ?   ?   B . n 
B 1 178 ALA 178 183 ?   ?   ?   B . n 
B 1 179 LYS 179 184 ?   ?   ?   B . n 
B 1 180 LYS 180 185 ?   ?   ?   B . n 
B 1 181 ASN 181 186 ?   ?   ?   B . n 
B 1 182 GLY 182 187 ?   ?   ?   B . n 
B 1 183 GLY 183 188 188 GLY GLY B . n 
B 1 184 THR 184 189 189 THR THR B . n 
B 1 185 LEU 185 190 190 LEU LEU B . n 
B 1 186 TYR 186 191 191 TYR TYR B . n 
B 1 187 TYR 187 192 192 TYR TYR B . n 
B 1 188 MET 188 193 193 MET MET B . n 
B 1 189 ALA 189 194 194 ALA ALA B . n 
B 1 190 PRO 190 195 195 PRO PRO B . n 
B 1 191 GLU 191 196 196 GLU GLU B . n 
B 1 192 HIS 192 197 197 HIS HIS B . n 
B 1 193 LEU 193 198 198 LEU LEU B . n 
B 1 194 ASN 194 199 199 ASN ASN B . n 
B 1 195 ASP 195 200 200 ASP ASP B . n 
B 1 196 VAL 196 201 201 VAL VAL B . n 
B 1 197 ASN 197 202 202 ASN ASN B . n 
B 1 198 ALA 198 203 203 ALA ALA B . n 
B 1 199 LYS 199 204 204 LYS LYS B . n 
B 1 200 PRO 200 205 205 PRO PRO B . n 
B 1 201 THR 201 206 206 THR THR B . n 
B 1 202 GLU 202 207 207 GLU GLU B . n 
B 1 203 LYS 203 208 208 LYS LYS B . n 
B 1 204 SER 204 209 209 SER SER B . n 
B 1 205 ASP 205 210 210 ASP ASP B . n 
B 1 206 VAL 206 211 211 VAL VAL B . n 
B 1 207 TYR 207 212 212 TYR TYR B . n 
B 1 208 SER 208 213 213 SER SER B . n 
B 1 209 PHE 209 214 214 PHE PHE B . n 
B 1 210 ALA 210 215 215 ALA ALA B . n 
B 1 211 VAL 211 216 216 VAL VAL B . n 
B 1 212 VAL 212 217 217 VAL VAL B . n 
B 1 213 LEU 213 218 218 LEU LEU B . n 
B 1 214 TRP 214 219 219 TRP TRP B . n 
B 1 215 ALA 215 220 220 ALA ALA B . n 
B 1 216 ILE 216 221 221 ILE ILE B . n 
B 1 217 PHE 217 222 222 PHE PHE B . n 
B 1 218 ALA 218 223 223 ALA ALA B . n 
B 1 219 ASN 219 224 224 ASN ASN B . n 
B 1 220 LYS 220 225 225 LYS LYS B . n 
B 1 221 GLU 221 226 226 GLU GLU B . n 
B 1 222 PRO 222 227 227 PRO PRO B . n 
B 1 223 TYR 223 228 228 TYR TYR B . n 
B 1 224 GLU 224 229 229 GLU GLU B . n 
B 1 225 ASN 225 230 230 ASN ASN B . n 
B 1 226 ALA 226 231 231 ALA ALA B . n 
B 1 227 ILE 227 232 232 ILE ILE B . n 
B 1 228 ALA 228 233 233 ALA ALA B . n 
B 1 229 GLU 229 234 234 GLU GLU B . n 
B 1 230 GLN 230 235 235 GLN GLN B . n 
B 1 231 GLN 231 236 236 GLN GLN B . n 
B 1 232 LEU 232 237 237 LEU LEU B . n 
B 1 233 ILE 233 238 238 ILE ILE B . n 
B 1 234 MET 234 239 239 MET MET B . n 
B 1 235 ALA 235 240 240 ALA ALA B . n 
B 1 236 ILE 236 241 241 ILE ILE B . n 
B 1 237 LYS 237 242 242 LYS LYS B . n 
B 1 238 SER 238 243 243 SER SER B . n 
B 1 239 GLY 239 244 244 GLY GLY B . n 
B 1 240 ASN 240 245 245 ASN ASN B . n 
B 1 241 ARG 241 246 246 ARG ARG B . n 
B 1 242 PRO 242 247 247 PRO PRO B . n 
B 1 243 ASP 243 248 248 ASP ASP B . n 
B 1 244 VAL 244 249 249 VAL VAL B . n 
B 1 245 ASP 245 250 250 ASP ASP B . n 
B 1 246 ASP 246 251 251 ASP ASP B . n 
B 1 247 ILE 247 252 252 ILE ILE B . n 
B 1 248 THR 248 253 253 THR THR B . n 
B 1 249 GLU 249 254 254 GLU GLU B . n 
B 1 250 TYR 250 255 255 TYR TYR B . n 
B 1 251 CYS 251 256 256 CYS CYS B . n 
B 1 252 PRO 252 257 257 PRO PRO B . n 
B 1 253 ARG 253 258 258 ARG ARG B . n 
B 1 254 GLU 254 259 259 GLU GLU B . n 
B 1 255 ILE 255 260 260 ILE ILE B . n 
B 1 256 ILE 256 261 261 ILE ILE B . n 
B 1 257 SER 257 262 262 SER SER B . n 
B 1 258 LEU 258 263 263 LEU LEU B . n 
B 1 259 MET 259 264 264 MET MET B . n 
B 1 260 LYS 260 265 265 LYS LYS B . n 
B 1 261 LEU 261 266 266 LEU LEU B . n 
B 1 262 CYS 262 267 267 CYS CYS B . n 
B 1 263 TRP 263 268 268 TRP TRP B . n 
B 1 264 GLU 264 269 269 GLU GLU B . n 
B 1 265 ALA 265 270 270 ALA ALA B . n 
B 1 266 ASN 266 271 271 ASN ASN B . n 
B 1 267 PRO 267 272 272 PRO PRO B . n 
B 1 268 GLU 268 273 273 GLU GLU B . n 
B 1 269 ALA 269 274 274 ALA ALA B . n 
B 1 270 ARG 270 275 275 ARG ARG B . n 
B 1 271 PRO 271 276 276 PRO PRO B . n 
B 1 272 THR 272 277 277 THR THR B . n 
B 1 273 PHE 273 278 278 PHE PHE B . n 
B 1 274 PRO 274 279 279 PRO PRO B . n 
B 1 275 GLY 275 280 280 GLY GLY B . n 
B 1 276 ILE 276 281 281 ILE ILE B . n 
B 1 277 GLU 277 282 282 GLU GLU B . n 
B 1 278 GLU 278 283 283 GLU GLU B . n 
B 1 279 LYS 279 284 284 LYS LYS B . n 
B 1 280 PHE 280 285 285 PHE PHE B . n 
B 1 281 ARG 281 286 286 ARG ARG B . n 
B 1 282 PRO 282 287 287 PRO PRO B . n 
B 1 283 PHE 283 288 288 PHE PHE B . n 
B 1 284 TYR 284 289 289 TYR TYR B . n 
B 1 285 LEU 285 290 290 LEU LEU B . n 
B 1 286 SER 286 291 291 SER SER B . n 
B 1 287 GLN 287 292 292 GLN GLN B . n 
B 1 288 LEU 288 293 293 LEU LEU B . n 
B 1 289 GLU 289 294 294 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BU4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BU4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BU4 1  301 1  A1BU4 INX A . 
D 3 IOD   1  302 3  IOD   IOD A . 
E 3 IOD   1  303 4  IOD   IOD A . 
F 2 A1BU4 1  301 2  A1BU4 INX B . 
G 3 IOD   1  302 1  IOD   IOD B . 
H 3 IOD   1  303 2  IOD   IOD B . 
I 3 IOD   1  304 5  IOD   IOD B . 
J 3 IOD   1  305 6  IOD   IOD B . 
K 3 IOD   1  306 7  IOD   IOD B . 
L 4 HOH   1  401 62 HOH   HOH A . 
L 4 HOH   2  402 59 HOH   HOH A . 
L 4 HOH   3  403 57 HOH   HOH A . 
L 4 HOH   4  404 40 HOH   HOH A . 
L 4 HOH   5  405 1  HOH   HOH A . 
L 4 HOH   6  406 19 HOH   HOH A . 
L 4 HOH   7  407 48 HOH   HOH A . 
L 4 HOH   8  408 54 HOH   HOH A . 
L 4 HOH   9  409 52 HOH   HOH A . 
L 4 HOH   10 410 60 HOH   HOH A . 
L 4 HOH   11 411 39 HOH   HOH A . 
L 4 HOH   12 412 43 HOH   HOH A . 
L 4 HOH   13 413 45 HOH   HOH A . 
L 4 HOH   14 414 58 HOH   HOH A . 
L 4 HOH   15 415 56 HOH   HOH A . 
L 4 HOH   16 416 46 HOH   HOH A . 
L 4 HOH   17 417 42 HOH   HOH A . 
L 4 HOH   18 418 47 HOH   HOH A . 
L 4 HOH   19 419 41 HOH   HOH A . 
M 4 HOH   1  401 51 HOH   HOH B . 
M 4 HOH   2  402 4  HOH   HOH B . 
M 4 HOH   3  403 44 HOH   HOH B . 
M 4 HOH   4  404 50 HOH   HOH B . 
M 4 HOH   5  405 8  HOH   HOH B . 
M 4 HOH   6  406 61 HOH   HOH B . 
M 4 HOH   7  407 49 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 0 A LYS 11  ? CD  ? A LYS 6   CD  
2   1 Y 0 A LYS 11  ? CE  ? A LYS 6   CE  
3   1 Y 0 A LYS 11  ? NZ  ? A LYS 6   NZ  
4   1 Y 0 A GLU 19  ? CG  ? A GLU 14  CG  
5   1 Y 0 A GLU 19  ? CD  ? A GLU 14  CD  
6   1 Y 0 A GLU 19  ? OE1 ? A GLU 14  OE1 
7   1 Y 0 A GLU 19  ? OE2 ? A GLU 14  OE2 
8   1 Y 0 A LYS 30  ? CG  ? A LYS 25  CG  
9   1 Y 0 A LYS 30  ? CD  ? A LYS 25  CD  
10  1 Y 0 A LYS 30  ? CE  ? A LYS 25  CE  
11  1 Y 0 A LYS 30  ? NZ  ? A LYS 25  NZ  
12  1 Y 0 A ILE 43  ? CD1 ? A ILE 38  CD1 
13  1 Y 0 A ASN 52  ? CG  ? A ASN 47  CG  
14  1 Y 0 A ASN 52  ? OD1 ? A ASN 47  OD1 
15  1 Y 0 A ASN 52  ? ND2 ? A ASN 47  ND2 
16  1 Y 0 A ILE 54  ? CD1 ? A ILE 49  CD1 
17  1 Y 0 A GLU 55  ? CG  ? A GLU 50  CG  
18  1 Y 0 A GLU 55  ? CD  ? A GLU 50  CD  
19  1 Y 0 A GLU 55  ? OE1 ? A GLU 50  OE1 
20  1 Y 0 A GLU 55  ? OE2 ? A GLU 50  OE2 
21  1 Y 0 A HIS 56  ? CG  ? A HIS 51  CG  
22  1 Y 0 A HIS 56  ? ND1 ? A HIS 51  ND1 
23  1 Y 0 A HIS 56  ? CD2 ? A HIS 51  CD2 
24  1 Y 0 A HIS 56  ? CE1 ? A HIS 51  CE1 
25  1 Y 0 A HIS 56  ? NE2 ? A HIS 51  NE2 
26  1 Y 0 A GLU 58  ? CG  ? A GLU 53  CG  
27  1 Y 0 A GLU 58  ? CD  ? A GLU 53  CD  
28  1 Y 0 A GLU 58  ? OE1 ? A GLU 53  OE1 
29  1 Y 0 A GLU 58  ? OE2 ? A GLU 53  OE2 
30  1 Y 0 A LYS 65  ? CD  ? A LYS 60  CD  
31  1 Y 0 A LYS 65  ? CE  ? A LYS 60  CE  
32  1 Y 0 A LYS 65  ? NZ  ? A LYS 60  NZ  
33  1 Y 0 A LYS 77  ? CD  ? A LYS 72  CD  
34  1 Y 0 A LYS 77  ? CE  ? A LYS 72  CE  
35  1 Y 0 A LYS 77  ? NZ  ? A LYS 72  NZ  
36  1 Y 0 A GLU 85  ? CG  ? A GLU 80  CG  
37  1 Y 0 A GLU 85  ? CD  ? A GLU 80  CD  
38  1 Y 0 A GLU 85  ? OE1 ? A GLU 80  OE1 
39  1 Y 0 A GLU 85  ? OE2 ? A GLU 80  OE2 
40  1 Y 0 A LYS 105 ? NZ  ? A LYS 100 NZ  
41  1 Y 0 A GLU 107 ? CG  ? A GLU 102 CG  
42  1 Y 0 A GLU 107 ? CD  ? A GLU 102 CD  
43  1 Y 0 A GLU 107 ? OE1 ? A GLU 102 OE1 
44  1 Y 0 A GLU 107 ? OE2 ? A GLU 102 OE2 
45  1 Y 0 A MET 108 ? SD  ? A MET 103 SD  
46  1 Y 0 A MET 108 ? CE  ? A MET 103 CE  
47  1 Y 0 A SER 109 ? OG  ? A SER 104 OG  
48  1 Y 0 A LYS 132 ? NZ  ? A LYS 127 NZ  
49  1 Y 0 A GLU 142 ? CD  ? A GLU 137 CD  
50  1 Y 0 A GLU 142 ? OE1 ? A GLU 137 OE1 
51  1 Y 0 A GLU 142 ? OE2 ? A GLU 137 OE2 
52  1 Y 0 A LYS 163 ? CG  ? A LYS 158 CG  
53  1 Y 0 A LYS 163 ? CD  ? A LYS 158 CD  
54  1 Y 0 A LYS 163 ? CE  ? A LYS 158 CE  
55  1 Y 0 A LYS 163 ? NZ  ? A LYS 158 NZ  
56  1 Y 0 A MET 164 ? CG  ? A MET 159 CG  
57  1 Y 0 A MET 164 ? SD  ? A MET 159 SD  
58  1 Y 0 A MET 164 ? CE  ? A MET 159 CE  
59  1 Y 0 A LYS 167 ? CG  ? A LYS 162 CG  
60  1 Y 0 A LYS 167 ? CD  ? A LYS 162 CD  
61  1 Y 0 A LYS 167 ? CE  ? A LYS 162 CE  
62  1 Y 0 A LYS 167 ? NZ  ? A LYS 162 NZ  
63  1 Y 0 A ASN 170 ? CG  ? A ASN 165 CG  
64  1 Y 0 A ASN 170 ? OD1 ? A ASN 165 OD1 
65  1 Y 0 A ASN 170 ? ND2 ? A ASN 165 ND2 
66  1 Y 0 A LYS 204 ? CG  ? A LYS 199 CG  
67  1 Y 0 A LYS 204 ? CD  ? A LYS 199 CD  
68  1 Y 0 A LYS 204 ? CE  ? A LYS 199 CE  
69  1 Y 0 A LYS 204 ? NZ  ? A LYS 199 NZ  
70  1 Y 0 A LYS 208 ? NZ  ? A LYS 203 NZ  
71  1 Y 0 A LYS 225 ? CE  ? A LYS 220 CE  
72  1 Y 0 A LYS 225 ? NZ  ? A LYS 220 NZ  
73  1 Y 0 A GLU 229 ? CG  ? A GLU 224 CG  
74  1 Y 0 A GLU 229 ? CD  ? A GLU 224 CD  
75  1 Y 0 A GLU 229 ? OE1 ? A GLU 224 OE1 
76  1 Y 0 A GLU 229 ? OE2 ? A GLU 224 OE2 
77  1 Y 0 A ASN 230 ? CG  ? A ASN 225 CG  
78  1 Y 0 A ASN 230 ? OD1 ? A ASN 225 OD1 
79  1 Y 0 A ASN 230 ? ND2 ? A ASN 225 ND2 
80  1 Y 0 A ILE 232 ? CG1 ? A ILE 227 CG1 
81  1 Y 0 A ILE 232 ? CG2 ? A ILE 227 CG2 
82  1 Y 0 A ILE 232 ? CD1 ? A ILE 227 CD1 
83  1 Y 0 A GLU 234 ? CG  ? A GLU 229 CG  
84  1 Y 0 A GLU 234 ? CD  ? A GLU 229 CD  
85  1 Y 0 A GLU 234 ? OE1 ? A GLU 229 OE1 
86  1 Y 0 A GLU 234 ? OE2 ? A GLU 229 OE2 
87  1 Y 0 A GLN 236 ? CG  ? A GLN 231 CG  
88  1 Y 0 A GLN 236 ? CD  ? A GLN 231 CD  
89  1 Y 0 A GLN 236 ? OE1 ? A GLN 231 OE1 
90  1 Y 0 A GLN 236 ? NE2 ? A GLN 231 NE2 
91  1 Y 0 A ILE 238 ? CD1 ? A ILE 233 CD1 
92  1 Y 0 A ASP 250 ? CG  ? A ASP 245 CG  
93  1 Y 0 A ASP 250 ? OD1 ? A ASP 245 OD1 
94  1 Y 0 A ASP 250 ? OD2 ? A ASP 245 OD2 
95  1 Y 0 A ARG 258 ? CG  ? A ARG 253 CG  
96  1 Y 0 A ARG 258 ? CD  ? A ARG 253 CD  
97  1 Y 0 A ARG 258 ? NE  ? A ARG 253 NE  
98  1 Y 0 A ARG 258 ? CZ  ? A ARG 253 CZ  
99  1 Y 0 A ARG 258 ? NH1 ? A ARG 253 NH1 
100 1 Y 0 A ARG 258 ? NH2 ? A ARG 253 NH2 
101 1 Y 0 A ILE 260 ? CD1 ? A ILE 255 CD1 
102 1 Y 0 A LYS 265 ? CE  ? A LYS 260 CE  
103 1 Y 0 A LYS 265 ? NZ  ? A LYS 260 NZ  
104 1 Y 0 A GLU 273 ? CG  ? A GLU 268 CG  
105 1 Y 0 A GLU 273 ? CD  ? A GLU 268 CD  
106 1 Y 0 A GLU 273 ? OE1 ? A GLU 268 OE1 
107 1 Y 0 A GLU 273 ? OE2 ? A GLU 268 OE2 
108 1 Y 0 A GLU 283 ? CG  ? A GLU 278 CG  
109 1 Y 0 A GLU 283 ? CD  ? A GLU 278 CD  
110 1 Y 0 A GLU 283 ? OE1 ? A GLU 278 OE1 
111 1 Y 0 A GLU 283 ? OE2 ? A GLU 278 OE2 
112 1 Y 0 A LYS 284 ? CD  ? A LYS 279 CD  
113 1 Y 0 A LYS 284 ? CE  ? A LYS 279 CE  
114 1 Y 0 A LYS 284 ? NZ  ? A LYS 279 NZ  
115 1 Y 0 B SER 6   ? N   ? B SER 1   N   
116 1 Y 0 B SER 6   ? CB  ? B SER 1   CB  
117 1 Y 0 B SER 6   ? OG  ? B SER 1   OG  
118 1 Y 0 B LEU 7   ? CG  ? B LEU 2   CG  
119 1 Y 0 B LEU 7   ? CD1 ? B LEU 2   CD1 
120 1 Y 0 B LEU 7   ? CD2 ? B LEU 2   CD2 
121 1 Y 0 B ASN 8   ? CG  ? B ASN 3   CG  
122 1 Y 0 B ASN 8   ? OD1 ? B ASN 3   OD1 
123 1 Y 0 B ASN 8   ? ND2 ? B ASN 3   ND2 
124 1 Y 0 B ILE 10  ? CD1 ? B ILE 5   CD1 
125 1 Y 0 B LYS 13  ? CG  ? B LYS 8   CG  
126 1 Y 0 B LYS 13  ? CD  ? B LYS 8   CD  
127 1 Y 0 B LYS 13  ? CE  ? B LYS 8   CE  
128 1 Y 0 B LYS 13  ? NZ  ? B LYS 8   NZ  
129 1 Y 0 B LYS 30  ? CG  ? B LYS 25  CG  
130 1 Y 0 B LYS 30  ? CD  ? B LYS 25  CD  
131 1 Y 0 B LYS 30  ? CE  ? B LYS 25  CE  
132 1 Y 0 B LYS 30  ? NZ  ? B LYS 25  NZ  
133 1 Y 0 B GLN 39  ? CD  ? B GLN 34  CD  
134 1 Y 0 B GLN 39  ? OE1 ? B GLN 34  OE1 
135 1 Y 0 B GLN 39  ? NE2 ? B GLN 34  NE2 
136 1 Y 0 B LYS 49  ? CD  ? B LYS 44  CD  
137 1 Y 0 B LYS 49  ? CE  ? B LYS 44  CE  
138 1 Y 0 B LYS 49  ? NZ  ? B LYS 44  NZ  
139 1 Y 0 B ILE 54  ? CG1 ? B ILE 49  CG1 
140 1 Y 0 B ILE 54  ? CG2 ? B ILE 49  CG2 
141 1 Y 0 B ILE 54  ? CD1 ? B ILE 49  CD1 
142 1 Y 0 B LYS 65  ? CE  ? B LYS 60  CE  
143 1 Y 0 B LYS 65  ? NZ  ? B LYS 60  NZ  
144 1 Y 0 B MET 66  ? SD  ? B MET 61  SD  
145 1 Y 0 B MET 66  ? CE  ? B MET 61  CE  
146 1 Y 0 B ARG 69  ? CD  ? B ARG 64  CD  
147 1 Y 0 B ARG 69  ? NE  ? B ARG 64  NE  
148 1 Y 0 B ARG 69  ? CZ  ? B ARG 64  CZ  
149 1 Y 0 B ARG 69  ? NH1 ? B ARG 64  NH1 
150 1 Y 0 B ARG 69  ? NH2 ? B ARG 64  NH2 
151 1 Y 0 B LYS 77  ? CD  ? B LYS 72  CD  
152 1 Y 0 B LYS 77  ? CE  ? B LYS 72  CE  
153 1 Y 0 B LYS 77  ? NZ  ? B LYS 72  NZ  
154 1 Y 0 B ILE 83  ? CD1 ? B ILE 78  CD1 
155 1 Y 0 B GLU 85  ? CG  ? B GLU 80  CG  
156 1 Y 0 B GLU 85  ? CD  ? B GLU 80  CD  
157 1 Y 0 B GLU 85  ? OE1 ? B GLU 80  OE1 
158 1 Y 0 B GLU 85  ? OE2 ? B GLU 80  OE2 
159 1 Y 0 B LYS 87  ? NZ  ? B LYS 82  NZ  
160 1 Y 0 B LYS 97  ? CE  ? B LYS 92  CE  
161 1 Y 0 B LYS 97  ? NZ  ? B LYS 92  NZ  
162 1 Y 0 B LYS 105 ? CD  ? B LYS 100 CD  
163 1 Y 0 B LYS 105 ? CE  ? B LYS 100 CE  
164 1 Y 0 B LYS 105 ? NZ  ? B LYS 100 NZ  
165 1 Y 0 B GLU 107 ? CG  ? B GLU 102 CG  
166 1 Y 0 B GLU 107 ? CD  ? B GLU 102 CD  
167 1 Y 0 B GLU 107 ? OE1 ? B GLU 102 OE1 
168 1 Y 0 B GLU 107 ? OE2 ? B GLU 102 OE2 
169 1 Y 0 B MET 108 ? SD  ? B MET 103 SD  
170 1 Y 0 B MET 108 ? CE  ? B MET 103 CE  
171 1 Y 0 B SER 109 ? OG  ? B SER 104 OG  
172 1 Y 0 B LYS 132 ? NZ  ? B LYS 127 NZ  
173 1 Y 0 B ILE 135 ? CD1 ? B ILE 130 CD1 
174 1 Y 0 B LYS 137 ? NZ  ? B LYS 132 NZ  
175 1 Y 0 B LYS 163 ? CG  ? B LYS 158 CG  
176 1 Y 0 B LYS 163 ? CD  ? B LYS 158 CD  
177 1 Y 0 B LYS 163 ? CE  ? B LYS 158 CE  
178 1 Y 0 B LYS 163 ? NZ  ? B LYS 158 NZ  
179 1 Y 0 B LYS 167 ? CG  ? B LYS 162 CG  
180 1 Y 0 B LYS 167 ? CD  ? B LYS 162 CD  
181 1 Y 0 B LYS 167 ? CE  ? B LYS 162 CE  
182 1 Y 0 B LYS 167 ? NZ  ? B LYS 162 NZ  
183 1 Y 0 B GLU 172 ? CD  ? B GLU 167 CD  
184 1 Y 0 B GLU 172 ? OE1 ? B GLU 167 OE1 
185 1 Y 0 B GLU 172 ? OE2 ? B GLU 167 OE2 
186 1 Y 0 B GLU 175 ? CD  ? B GLU 170 CD  
187 1 Y 0 B GLU 175 ? OE1 ? B GLU 170 OE1 
188 1 Y 0 B GLU 175 ? OE2 ? B GLU 170 OE2 
189 1 Y 0 B LEU 190 ? CG  ? B LEU 185 CG  
190 1 Y 0 B LEU 190 ? CD1 ? B LEU 185 CD1 
191 1 Y 0 B LEU 190 ? CD2 ? B LEU 185 CD2 
192 1 Y 0 B ASP 200 ? CG  ? B ASP 195 CG  
193 1 Y 0 B ASP 200 ? OD1 ? B ASP 195 OD1 
194 1 Y 0 B ASP 200 ? OD2 ? B ASP 195 OD2 
195 1 Y 0 B ASN 202 ? CG  ? B ASN 197 CG  
196 1 Y 0 B ASN 202 ? OD1 ? B ASN 197 OD1 
197 1 Y 0 B ASN 202 ? ND2 ? B ASN 197 ND2 
198 1 Y 0 B LYS 204 ? CG  ? B LYS 199 CG  
199 1 Y 0 B LYS 204 ? CD  ? B LYS 199 CD  
200 1 Y 0 B LYS 204 ? CE  ? B LYS 199 CE  
201 1 Y 0 B LYS 204 ? NZ  ? B LYS 199 NZ  
202 1 Y 0 B GLU 207 ? CD  ? B GLU 202 CD  
203 1 Y 0 B GLU 207 ? OE1 ? B GLU 202 OE1 
204 1 Y 0 B GLU 207 ? OE2 ? B GLU 202 OE2 
205 1 Y 0 B LYS 225 ? CE  ? B LYS 220 CE  
206 1 Y 0 B LYS 225 ? NZ  ? B LYS 220 NZ  
207 1 Y 0 B ILE 232 ? CD1 ? B ILE 227 CD1 
208 1 Y 0 B ILE 238 ? CD1 ? B ILE 233 CD1 
209 1 Y 0 B ILE 241 ? CD1 ? B ILE 236 CD1 
210 1 Y 0 B THR 253 ? OG1 ? B THR 248 OG1 
211 1 Y 0 B THR 253 ? CG2 ? B THR 248 CG2 
212 1 Y 0 B GLU 254 ? CG  ? B GLU 249 CG  
213 1 Y 0 B GLU 254 ? CD  ? B GLU 249 CD  
214 1 Y 0 B GLU 254 ? OE1 ? B GLU 249 OE1 
215 1 Y 0 B GLU 254 ? OE2 ? B GLU 249 OE2 
216 1 Y 0 B TYR 255 ? CG  ? B TYR 250 CG  
217 1 Y 0 B TYR 255 ? CD1 ? B TYR 250 CD1 
218 1 Y 0 B TYR 255 ? CD2 ? B TYR 250 CD2 
219 1 Y 0 B TYR 255 ? CE1 ? B TYR 250 CE1 
220 1 Y 0 B TYR 255 ? CE2 ? B TYR 250 CE2 
221 1 Y 0 B TYR 255 ? CZ  ? B TYR 250 CZ  
222 1 Y 0 B TYR 255 ? OH  ? B TYR 250 OH  
223 1 Y 0 B ARG 258 ? CD  ? B ARG 253 CD  
224 1 Y 0 B ARG 258 ? NE  ? B ARG 253 NE  
225 1 Y 0 B ARG 258 ? CZ  ? B ARG 253 CZ  
226 1 Y 0 B ARG 258 ? NH1 ? B ARG 253 NH1 
227 1 Y 0 B ARG 258 ? NH2 ? B ARG 253 NH2 
228 1 Y 0 B ILE 260 ? CD1 ? B ILE 255 CD1 
229 1 Y 0 B ILE 261 ? CD1 ? B ILE 256 CD1 
230 1 Y 0 B LYS 265 ? CE  ? B LYS 260 CE  
231 1 Y 0 B LYS 265 ? NZ  ? B LYS 260 NZ  
232 1 Y 0 B GLU 273 ? CD  ? B GLU 268 CD  
233 1 Y 0 B GLU 273 ? OE1 ? B GLU 268 OE1 
234 1 Y 0 B GLU 273 ? OE2 ? B GLU 268 OE2 
235 1 Y 0 B GLU 283 ? CG  ? B GLU 278 CG  
236 1 Y 0 B GLU 283 ? CD  ? B GLU 278 CD  
237 1 Y 0 B GLU 283 ? OE1 ? B GLU 278 OE1 
238 1 Y 0 B GLU 283 ? OE2 ? B GLU 278 OE2 
239 1 Y 0 B LYS 284 ? CG  ? B LYS 279 CG  
240 1 Y 0 B LYS 284 ? CD  ? B LYS 279 CD  
241 1 Y 0 B LYS 284 ? CE  ? B LYS 279 CE  
242 1 Y 0 B LYS 284 ? NZ  ? B LYS 279 NZ  
243 1 Y 0 B GLU 294 ? CD  ? B GLU 289 CD  
244 1 Y 0 B GLU 294 ? OE1 ? B GLU 289 OE1 
245 1 Y 0 B GLU 294 ? OE2 ? B GLU 289 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? '(VERSION Jan 26' 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '(Version 1.1.7)' 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                 4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0155          5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MZX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.407 
_cell.length_a_esd                 ? 
_cell.length_b                     101.124 
_cell.length_b_esd                 ? 
_cell.length_c                     130.664 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MZX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9MZX 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.44 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% (w/v) PEG3350; 6 mM Gly3; 0.01 m NaAcetate pH 4.75; 0.12 M Na3Citrate; 0.28 M NH4I' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-06-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9998 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MZX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.53 
_reflns.d_resolution_low                               79.97 
_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                                     18320 
_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                                8.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.53 
_reflns_shell.d_res_low                                     79.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             890 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.408 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -1.14 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            2.32 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.19 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               76.691 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.936 
_refine.correlation_coeff_Fo_to_Fc_free          0.921 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9MZX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.53 
_refine.ls_d_res_low                             79.97 
_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                     18178 
_refine.ls_number_reflns_R_free                  832 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    83.02 
_refine.ls_percent_reflns_R_free                 4.4 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21707 
_refine.ls_R_factor_R_free                       0.26284 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21493 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.904 
_refine.pdbx_overall_ESU_R_Free                  0.342 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             27.875 
_refine.overall_SU_ML                            0.279 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.53 
_refine_hist.d_res_low                        79.97 
_refine_hist.number_atoms_solvent             26 
_refine_hist.number_atoms_total               4346 
_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        4277 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.019  4164 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  3989 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.534  1.978  5660 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.245  3.000  9094 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.081  5.000  529  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.530 24.403 159  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.578 15.058 687  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.060 15.000 15   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  651  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.021  4656 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  903  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.364  6.189  2130 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.365  6.188  2129 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.749  10.440 2654 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.747  10.441 2655 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.262  6.270  2034 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.261  6.270  2035 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.482  10.471 3007 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.008  55.042 4377 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.007  55.044 4378 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 1 'interatomic distance' ? A 5852 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 2 'interatomic distance' ? B 5852 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.535 
_refine_ls_shell.d_res_low                        2.600 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             5 
_refine_ls_shell.number_reflns_R_work             85 
_refine_ls_shell.percent_reflns_obs               5.52 
_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                  0.299 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_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                  0.261 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     9MZX 
_struct.title                        'Crystal structure of human RIPK1 with Compound 1' 
_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        9MZX 
_struct_keywords.text            'Kinase, serine/threonine-protein kinase, Inhibitor, TRANSFERASE, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSFERASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RIPK1_HUMAN 
_struct_ref.pdbx_db_accession          Q13546 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE
GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMW
SKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGN
RPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_struct_ref.pdbx_align_begin           6 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9MZX A 1 ? 289 ? Q13546 6 ? 294 ? 6 294 
2 1 9MZX B 1 ? 289 ? Q13546 6 ? 294 ? 6 294 
# 
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 9MZX ALA A 29  ? UNP Q13546 CYS 34  conflict 34  1 
1 9MZX ALA A 122 ? UNP Q13546 CYS 127 conflict 127 2 
1 9MZX ALA A 228 ? UNP Q13546 CYS 233 conflict 233 3 
1 9MZX ALA A 235 ? UNP Q13546 CYS 240 conflict 240 4 
2 9MZX ALA B 29  ? UNP Q13546 CYS 34  conflict 34  5 
2 9MZX ALA B 122 ? UNP Q13546 CYS 127 conflict 127 6 
2 9MZX ALA B 228 ? UNP Q13546 CYS 233 conflict 233 7 
2 9MZX ALA B 235 ? UNP Q13546 CYS 240 conflict 240 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 8   ? SER A 10  ? LYS A 13  SER A 15  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 51  ? LEU A 65  ? HIS A 56  LEU A 70  1 ? 15 
HELX_P HELX_P3  AA3 LEU A 95  ? LYS A 100 ? LEU A 100 LYS A 105 1 ? 6  
HELX_P HELX_P4  AA4 PRO A 106 ? LYS A 127 ? PRO A 111 LYS A 132 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 135 ? GLU A 137 ? LYS A 140 GLU A 142 5 ? 3  
HELX_P HELX_P6  AA6 PHE A 157 ? ASN A 165 ? PHE A 162 ASN A 170 1 ? 9  
HELX_P HELX_P7  AA7 THR A 201 ? ASN A 219 ? THR A 206 ASN A 224 1 ? 19 
HELX_P HELX_P8  AA8 PRO A 222 ? ALA A 226 ? PRO A 227 ALA A 231 5 ? 5  
HELX_P HELX_P9  AA9 GLU A 229 ? GLY A 239 ? GLU A 234 GLY A 244 1 ? 11 
HELX_P HELX_P10 AB1 ASP A 243 ? ILE A 247 ? ASP A 248 ILE A 252 5 ? 5  
HELX_P HELX_P11 AB2 PRO A 252 ? TRP A 263 ? PRO A 257 TRP A 268 1 ? 12 
HELX_P HELX_P12 AB3 ASN A 266 ? ARG A 270 ? ASN A 271 ARG A 275 5 ? 5  
HELX_P HELX_P13 AB4 THR A 272 ? GLN A 287 ? THR A 277 GLN A 292 1 ? 16 
HELX_P HELX_P14 AB5 LYS B 8   ? PHE B 12  ? LYS B 13  PHE B 17  5 ? 5  
HELX_P HELX_P15 AB6 CYS B 48  ? GLU B 50  ? CYS B 53  GLU B 55  5 ? 3  
HELX_P HELX_P16 AB7 HIS B 51  ? LEU B 65  ? HIS B 56  LEU B 70  1 ? 15 
HELX_P HELX_P17 AB8 LEU B 95  ? ALA B 101 ? LEU B 100 ALA B 106 1 ? 7  
HELX_P HELX_P18 AB9 PRO B 106 ? LYS B 127 ? PRO B 111 LYS B 132 1 ? 22 
HELX_P HELX_P19 AC1 LYS B 135 ? GLU B 137 ? LYS B 140 GLU B 142 5 ? 3  
HELX_P HELX_P20 AC2 PHE B 157 ? ASN B 165 ? PHE B 162 ASN B 170 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 189 ? LEU B 193 ? ALA B 194 LEU B 198 5 ? 5  
HELX_P HELX_P22 AC4 THR B 201 ? ASN B 219 ? THR B 206 ASN B 224 1 ? 19 
HELX_P HELX_P23 AC5 ALA B 228 ? GLY B 239 ? ALA B 233 GLY B 244 1 ? 12 
HELX_P HELX_P24 AC6 ASP B 243 ? ILE B 247 ? ASP B 248 ILE B 252 5 ? 5  
HELX_P HELX_P25 AC7 PRO B 252 ? TRP B 263 ? PRO B 257 TRP B 268 1 ? 12 
HELX_P HELX_P26 AC8 ASN B 266 ? ARG B 270 ? ASN B 271 ARG B 275 5 ? 5  
HELX_P HELX_P27 AC9 THR B 272 ? GLN B 287 ? THR B 277 GLN B 292 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 12  ? ALA A 16  ? PHE A 17  ALA A 21  
AA1 2 VAL A 26  ? HIS A 31  ? VAL A 31  HIS A 36  
AA1 3 GLY A 35  ? LYS A 44  ? GLY A 40  LYS A 49  
AA1 4 LYS A 82  ? MET A 87  ? LYS A 87  MET A 92  
AA1 5 LEU A 73  ? ILE A 78  ? LEU A 78  ILE A 83  
AA2 1 GLY A 93  ? ASN A 94  ? GLY A 98  ASN A 99  
AA2 2 ILE A 139 ? VAL A 141 ? ILE A 144 VAL A 146 
AA2 3 ILE A 147 ? ILE A 149 ? ILE A 152 ILE A 154 
AA3 1 LYS B 6   ? MET B 7   ? LYS B 11  MET B 12  
AA3 2 LEU B 73  ? ILE B 78  ? LEU B 78  ILE B 83  
AA3 3 LYS B 82  ? MET B 87  ? LYS B 87  MET B 92  
AA3 4 GLY B 35  ? LYS B 44  ? GLY B 40  LYS B 49  
AA3 5 VAL B 26  ? HIS B 31  ? VAL B 31  HIS B 36  
AA4 1 GLY B 93  ? ASN B 94  ? GLY B 98  ASN B 99  
AA4 2 ILE B 139 ? VAL B 141 ? ILE B 144 VAL B 146 
AA4 3 ILE B 147 ? ILE B 149 ? ILE B 152 ILE B 154 
# 
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 ALA A 16  ? N ALA A 21  O LEU A 28  ? O LEU A 33  
AA1 2 3 N SER A 27  ? N SER A 32  O MET A 39  ? O MET A 44  
AA1 3 4 N LYS A 40  ? N LYS A 45  O LEU A 85  ? O LEU A 90  
AA1 4 5 O SER A 84  ? O SER A 89  N ILE A 77  ? N ILE A 82  
AA2 1 2 N GLY A 93  ? N GLY A 98  O VAL A 141 ? O VAL A 146 
AA2 2 3 N LEU A 140 ? N LEU A 145 O LYS A 148 ? O LYS A 153 
AA3 1 2 N MET B 7   ? N MET B 12  O VAL B 76  ? O VAL B 81  
AA3 2 3 N ILE B 77  ? N ILE B 82  O SER B 84  ? O SER B 89  
AA3 3 4 O MET B 87  ? O MET B 92  N ILE B 38  ? N ILE B 43  
AA3 4 5 O MET B 39  ? O MET B 44  N SER B 27  ? N SER B 32  
AA4 1 2 N GLY B 93  ? N GLY B 98  O VAL B 141 ? O VAL B 146 
AA4 2 3 N LEU B 140 ? N LEU B 145 O LYS B 148 ? O LYS B 153 
# 
_pdbx_entry_details.entry_id                   9MZX 
_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     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             283 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             283 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.361 
_pdbx_validate_rmsd_bond.bond_target_value         1.517 
_pdbx_validate_rmsd_bond.bond_deviation            -0.156 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              283 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              283 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              283 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                128.44 
_pdbx_validate_rmsd_angle.angle_target_value         113.40 
_pdbx_validate_rmsd_angle.angle_deviation            15.04 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 7   ? ? 70.93   -25.75 
2 1 GLU A 55  ? ? 109.73  -4.18  
3 1 GLU A 85  ? ? -64.83  94.53  
4 1 LYS A 137 ? ? 75.88   -9.50  
5 1 ASP A 138 ? ? -158.10 46.88  
6 1 THR B 38  ? ? -95.27  -61.66 
7 1 GLU B 85  ? ? -62.86  94.74  
8 1 LYS B 137 ? ? 75.80   -10.44 
9 1 ASP B 138 ? ? -158.29 47.87  
# 
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 -5.3660  13.9790  12.7760 0.1523 ? -0.0043 ? 0.0257  ? 0.2305 ? 0.0193  ? 0.2242 ? 6.2291  ? 
-1.2541 ? 3.3191  ? 10.5745 ? -1.9151 ? 3.1692 ? -0.1892 ? 0.9064  ? 0.4845  ? -0.7270 ? 0.1098  ? 0.0816  ? -0.1374 ? 0.2759  ? 
0.0794  ? 
2 'X-RAY DIFFRACTION' ? refined -4.8530  7.3070   3.2850  0.2404 ? 0.0053  ? 0.0291  ? 0.4192 ? 0.0550  ? 0.2518 ? 0.4405  ? 
-0.0518 ? -0.5577 ? 0.1334  ? -0.7251 ? 5.6934 ? 0.0432  ? 0.3608  ? 0.1158  ? -0.0383 ? -0.1425 ? -0.0649 ? 0.0441  ? 0.2189  ? 
0.0992  ? 
3 'X-RAY DIFFRACTION' ? refined 4.8070   -11.0380 14.4370 0.1320 ? 0.0721  ? -0.0807 ? 0.0690 ? 0.0105  ? 0.2019 ? 3.5125  ? 
-0.5415 ? 0.5392  ? 4.1995  ? 0.7074  ? 5.4449 ? 0.2175  ? 0.2069  ? -0.1122 ? -0.0763 ? -0.0468 ? -0.1943 ? 0.6443  ? 0.5404  ? 
-0.1706 ? 
4 'X-RAY DIFFRACTION' ? refined -19.7380 -23.0810 37.0630 0.2562 ? 0.0034  ? -0.1046 ? 0.0718 ? -0.0193 ? 0.2420 ? 7.9719  ? 
4.4681  ? -1.2285 ? 7.3868  ? -0.8029 ? 1.6205 ? -0.0346 ? 0.3188  ? -0.7665 ? -0.1789 ? 0.2715  ? 0.0843  ? 0.3964  ? -0.1862 ? 
-0.2370 ? 
5 'X-RAY DIFFRACTION' ? refined -28.8380 -17.1610 42.9200 0.2828 ? 0.0784  ? -0.0420 ? 0.2668 ? 0.1110  ? 0.4869 ? 10.6810 ? 
6.8509  ? -2.1876 ? 6.1569  ? 1.6260  ? 5.6833 ? 0.3904  ? 0.5757  ? 0.0950  ? 0.4239  ? -0.1770 ? -0.0439 ? 0.1370  ? -1.0986 ? 
-0.2133 ? 
6 'X-RAY DIFFRACTION' ? refined -12.3090 2.0430   44.9790 0.2116 ? -0.0094 ? -0.0126 ? 0.0317 ? 0.0272  ? 0.1416 ? 2.5100  ? 
-1.6116 ? -1.9116 ? 5.5584  ? 0.5334  ? 5.9571 ? 0.0607  ? -0.1787 ? 0.2656  ? 0.1759  ? 0.1455  ? -0.0504 ? -0.6268 ? 0.1072  ? 
-0.2061 ? 
# 
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 ? ? A 6   ? ? ? A 95  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 155 ? ? ? A 170 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 96  ? ? ? A 154 ? ? ? 
4 'X-RAY DIFFRACTION' 3 ? ? A 188 ? ? ? A 294 ? ? ? 
5 'X-RAY DIFFRACTION' 4 ? ? B 6   ? ? ? B 95  ? ? ? 
6 'X-RAY DIFFRACTION' 5 ? ? B 155 ? ? ? B 170 ? ? ? 
7 'X-RAY DIFFRACTION' 6 ? ? B 96  ? ? ? B 154 ? ? ? 
8 'X-RAY DIFFRACTION' 6 ? ? B 188 ? ? ? B 294 ? ? ? 
# 
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 LEU 23  ? A LEU 18  
2  1 Y 1 A ASP 24  ? A ASP 19  
3  1 Y 1 A SER 25  ? A SER 20  
4  1 Y 1 A GLY 26  ? A GLY 21  
5  1 Y 1 A GLY 27  ? A GLY 22  
6  1 Y 1 A PHE 28  ? A PHE 23  
7  1 Y 1 A GLY 29  ? A GLY 24  
8  1 Y 1 A GLU 171 ? A GLU 166 
9  1 Y 1 A GLU 172 ? A GLU 167 
10 1 Y 1 A HIS 173 ? A HIS 168 
11 1 Y 1 A ASN 174 ? A ASN 169 
12 1 Y 1 A GLU 175 ? A GLU 170 
13 1 Y 1 A LEU 176 ? A LEU 171 
14 1 Y 1 A ARG 177 ? A ARG 172 
15 1 Y 1 A GLU 178 ? A GLU 173 
16 1 Y 1 A VAL 179 ? A VAL 174 
17 1 Y 1 A ASP 180 ? A ASP 175 
18 1 Y 1 A GLY 181 ? A GLY 176 
19 1 Y 1 A THR 182 ? A THR 177 
20 1 Y 1 A ALA 183 ? A ALA 178 
21 1 Y 1 A LYS 184 ? A LYS 179 
22 1 Y 1 A LYS 185 ? A LYS 180 
23 1 Y 1 A ASN 186 ? A ASN 181 
24 1 Y 1 A GLY 187 ? A GLY 182 
25 1 Y 1 B SER 20  ? B SER 15  
26 1 Y 1 B ALA 21  ? B ALA 16  
27 1 Y 1 B GLU 22  ? B GLU 17  
28 1 Y 1 B LEU 23  ? B LEU 18  
29 1 Y 1 B ASP 24  ? B ASP 19  
30 1 Y 1 B SER 25  ? B SER 20  
31 1 Y 1 B GLY 26  ? B GLY 21  
32 1 Y 1 B GLY 27  ? B GLY 22  
33 1 Y 1 B PHE 28  ? B PHE 23  
34 1 Y 1 B GLY 29  ? B GLY 24  
35 1 Y 1 B ARG 177 ? B ARG 172 
36 1 Y 1 B GLU 178 ? B GLU 173 
37 1 Y 1 B VAL 179 ? B VAL 174 
38 1 Y 1 B ASP 180 ? B ASP 175 
39 1 Y 1 B GLY 181 ? B GLY 176 
40 1 Y 1 B THR 182 ? B THR 177 
41 1 Y 1 B ALA 183 ? B ALA 178 
42 1 Y 1 B LYS 184 ? B LYS 179 
43 1 Y 1 B LYS 185 ? B LYS 180 
44 1 Y 1 B ASN 186 ? B ASN 181 
45 1 Y 1 B GLY 187 ? B GLY 182 
# 
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 
A1BU4 C1   C Y N 1   
A1BU4 C2   C Y N 2   
A1BU4 C3   C Y N 3   
A1BU4 C4   C Y N 4   
A1BU4 C5   C Y N 5   
A1BU4 C6   C Y N 6   
A1BU4 C7   C N S 7   
A1BU4 C12  C N N 8   
A1BU4 O14  O N N 9   
A1BU4 C15  C N N 10  
A1BU4 C16  C N N 11  
A1BU4 C17  C N N 12  
A1BU4 C18  C N N 13  
A1BU4 N8   N N N 14  
A1BU4 C9   C N N 15  
A1BU4 C10  C N S 16  
A1BU4 O11  O N N 17  
A1BU4 C13  C N N 18  
A1BU4 H1   H N N 19  
A1BU4 H2   H N N 20  
A1BU4 H3   H N N 21  
A1BU4 H4   H N N 22  
A1BU4 H5   H N N 23  
A1BU4 H6   H N N 24  
A1BU4 H7   H N N 25  
A1BU4 H8   H N N 26  
A1BU4 H9   H N N 27  
A1BU4 H10  H N N 28  
A1BU4 H11  H N N 29  
A1BU4 H12  H N N 30  
A1BU4 H13  H N N 31  
A1BU4 H14  H N N 32  
A1BU4 H15  H N N 33  
A1BU4 H16  H N N 34  
A1BU4 H17  H N N 35  
A1BU4 H18  H N N 36  
A1BU4 H19  H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
IOD   I    I N N 220 
LEU   N    N N N 221 
LEU   CA   C N S 222 
LEU   C    C N N 223 
LEU   O    O N N 224 
LEU   CB   C N N 225 
LEU   CG   C N N 226 
LEU   CD1  C N N 227 
LEU   CD2  C N N 228 
LEU   OXT  O N N 229 
LEU   H    H N N 230 
LEU   H2   H N N 231 
LEU   HA   H N N 232 
LEU   HB2  H N N 233 
LEU   HB3  H N N 234 
LEU   HG   H N N 235 
LEU   HD11 H N N 236 
LEU   HD12 H N N 237 
LEU   HD13 H N N 238 
LEU   HD21 H N N 239 
LEU   HD22 H N N 240 
LEU   HD23 H N N 241 
LEU   HXT  H N N 242 
LYS   N    N N N 243 
LYS   CA   C N S 244 
LYS   C    C N N 245 
LYS   O    O N N 246 
LYS   CB   C N N 247 
LYS   CG   C N N 248 
LYS   CD   C N N 249 
LYS   CE   C N N 250 
LYS   NZ   N N N 251 
LYS   OXT  O N N 252 
LYS   H    H N N 253 
LYS   H2   H N N 254 
LYS   HA   H N N 255 
LYS   HB2  H N N 256 
LYS   HB3  H N N 257 
LYS   HG2  H N N 258 
LYS   HG3  H N N 259 
LYS   HD2  H N N 260 
LYS   HD3  H N N 261 
LYS   HE2  H N N 262 
LYS   HE3  H N N 263 
LYS   HZ1  H N N 264 
LYS   HZ2  H N N 265 
LYS   HZ3  H N N 266 
LYS   HXT  H N N 267 
MET   N    N N N 268 
MET   CA   C N S 269 
MET   C    C N N 270 
MET   O    O N N 271 
MET   CB   C N N 272 
MET   CG   C N N 273 
MET   SD   S N N 274 
MET   CE   C N N 275 
MET   OXT  O N N 276 
MET   H    H N N 277 
MET   H2   H N N 278 
MET   HA   H N N 279 
MET   HB2  H N N 280 
MET   HB3  H N N 281 
MET   HG2  H N N 282 
MET   HG3  H N N 283 
MET   HE1  H N N 284 
MET   HE2  H N N 285 
MET   HE3  H N N 286 
MET   HXT  H N N 287 
PHE   N    N N N 288 
PHE   CA   C N S 289 
PHE   C    C N N 290 
PHE   O    O N N 291 
PHE   CB   C N N 292 
PHE   CG   C Y N 293 
PHE   CD1  C Y N 294 
PHE   CD2  C Y N 295 
PHE   CE1  C Y N 296 
PHE   CE2  C Y N 297 
PHE   CZ   C Y N 298 
PHE   OXT  O N N 299 
PHE   H    H N N 300 
PHE   H2   H N N 301 
PHE   HA   H N N 302 
PHE   HB2  H N N 303 
PHE   HB3  H N N 304 
PHE   HD1  H N N 305 
PHE   HD2  H N N 306 
PHE   HE1  H N N 307 
PHE   HE2  H N N 308 
PHE   HZ   H N N 309 
PHE   HXT  H N N 310 
PRO   N    N N N 311 
PRO   CA   C N S 312 
PRO   C    C N N 313 
PRO   O    O N N 314 
PRO   CB   C N N 315 
PRO   CG   C N N 316 
PRO   CD   C N N 317 
PRO   OXT  O N N 318 
PRO   H    H N N 319 
PRO   HA   H N N 320 
PRO   HB2  H N N 321 
PRO   HB3  H N N 322 
PRO   HG2  H N N 323 
PRO   HG3  H N N 324 
PRO   HD2  H N N 325 
PRO   HD3  H N N 326 
PRO   HXT  H N N 327 
SER   N    N N N 328 
SER   CA   C N S 329 
SER   C    C N N 330 
SER   O    O N N 331 
SER   CB   C N N 332 
SER   OG   O N N 333 
SER   OXT  O N N 334 
SER   H    H N N 335 
SER   H2   H N N 336 
SER   HA   H N N 337 
SER   HB2  H N N 338 
SER   HB3  H N N 339 
SER   HG   H N N 340 
SER   HXT  H N N 341 
THR   N    N N N 342 
THR   CA   C N S 343 
THR   C    C N N 344 
THR   O    O N N 345 
THR   CB   C N R 346 
THR   OG1  O N N 347 
THR   CG2  C N N 348 
THR   OXT  O N N 349 
THR   H    H N N 350 
THR   H2   H N N 351 
THR   HA   H N N 352 
THR   HB   H N N 353 
THR   HG1  H N N 354 
THR   HG21 H N N 355 
THR   HG22 H N N 356 
THR   HG23 H N N 357 
THR   HXT  H N N 358 
TRP   N    N N N 359 
TRP   CA   C N S 360 
TRP   C    C N N 361 
TRP   O    O N N 362 
TRP   CB   C N N 363 
TRP   CG   C Y N 364 
TRP   CD1  C Y N 365 
TRP   CD2  C Y N 366 
TRP   NE1  N Y N 367 
TRP   CE2  C Y N 368 
TRP   CE3  C Y N 369 
TRP   CZ2  C Y N 370 
TRP   CZ3  C Y N 371 
TRP   CH2  C Y N 372 
TRP   OXT  O N N 373 
TRP   H    H N N 374 
TRP   H2   H N N 375 
TRP   HA   H N N 376 
TRP   HB2  H N N 377 
TRP   HB3  H N N 378 
TRP   HD1  H N N 379 
TRP   HE1  H N N 380 
TRP   HE3  H N N 381 
TRP   HZ2  H N N 382 
TRP   HZ3  H N N 383 
TRP   HH2  H N N 384 
TRP   HXT  H N N 385 
TYR   N    N N N 386 
TYR   CA   C N S 387 
TYR   C    C N N 388 
TYR   O    O N N 389 
TYR   CB   C N N 390 
TYR   CG   C Y N 391 
TYR   CD1  C Y N 392 
TYR   CD2  C Y N 393 
TYR   CE1  C Y N 394 
TYR   CE2  C Y N 395 
TYR   CZ   C Y N 396 
TYR   OH   O N N 397 
TYR   OXT  O N N 398 
TYR   H    H N N 399 
TYR   H2   H N N 400 
TYR   HA   H N N 401 
TYR   HB2  H N N 402 
TYR   HB3  H N N 403 
TYR   HD1  H N N 404 
TYR   HD2  H N N 405 
TYR   HE1  H N N 406 
TYR   HE2  H N N 407 
TYR   HH   H N N 408 
TYR   HXT  H N N 409 
VAL   N    N N N 410 
VAL   CA   C N S 411 
VAL   C    C N N 412 
VAL   O    O N N 413 
VAL   CB   C N N 414 
VAL   CG1  C N N 415 
VAL   CG2  C N N 416 
VAL   OXT  O N N 417 
VAL   H    H N N 418 
VAL   H2   H N N 419 
VAL   HA   H N N 420 
VAL   HB   H N N 421 
VAL   HG11 H N N 422 
VAL   HG12 H N N 423 
VAL   HG13 H N N 424 
VAL   HG21 H N N 425 
VAL   HG22 H N N 426 
VAL   HG23 H N N 427 
VAL   HXT  H N N 428 
# 
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 
A1BU4 C16 C15  sing N N 1   
A1BU4 C18 C15  sing N N 2   
A1BU4 C15 C17  sing N N 3   
A1BU4 C15 C13  sing N N 4   
A1BU4 C3  C2   doub Y N 5   
A1BU4 C3  C4   sing Y N 6   
A1BU4 C2  C1   sing Y N 7   
A1BU4 C13 O14  doub N N 8   
A1BU4 C13 N8   sing N N 9   
A1BU4 C4  O11  sing N N 10  
A1BU4 C4  C5   doub Y N 11  
A1BU4 C1  C6   doub Y N 12  
A1BU4 O11 C10  sing N N 13  
A1BU4 C9  N8   sing N N 14  
A1BU4 C9  C10  sing N N 15  
A1BU4 N8  C7   sing N N 16  
A1BU4 C5  C6   sing Y N 17  
A1BU4 C5  C7   sing N N 18  
A1BU4 C10 C12  sing N N 19  
A1BU4 C7  C12  sing N N 20  
A1BU4 C1  H1   sing N N 21  
A1BU4 C2  H2   sing N N 22  
A1BU4 C3  H3   sing N N 23  
A1BU4 C6  H4   sing N N 24  
A1BU4 C7  H5   sing N N 25  
A1BU4 C12 H6   sing N N 26  
A1BU4 C12 H7   sing N N 27  
A1BU4 C16 H8   sing N N 28  
A1BU4 C16 H9   sing N N 29  
A1BU4 C16 H10  sing N N 30  
A1BU4 C17 H11  sing N N 31  
A1BU4 C17 H12  sing N N 32  
A1BU4 C17 H13  sing N N 33  
A1BU4 C18 H14  sing N N 34  
A1BU4 C18 H15  sing N N 35  
A1BU4 C18 H16  sing N N 36  
A1BU4 C9  H17  sing N N 37  
A1BU4 C9  H18  sing N N 38  
A1BU4 C10 H19  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4ith 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MZX 
_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]   0.019839 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009889 
_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]   0.007653 
_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 
I 
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   . SER   A 1 1   ? -13.746 14.173  23.712  1.00 115.07 ?  6   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -14.043 12.816  24.289  1.00 114.91 ?  6   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -15.271 12.158  23.639  1.00 117.29 ?  6   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -16.305 12.797  23.478  1.00 137.95 ?  6   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -14.241 12.892  25.807  1.00 121.40 ?  6   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -13.066 13.354  26.451  1.00 121.22 ?  6   SER   A OG  1 
ATOM   7    N N   . LEU   A 1 2   ? -15.120 10.893  23.251  1.00 118.25 ?  7   LEU   A N   1 
ATOM   8    C CA  . LEU   A 1 2   ? -16.103 10.059  22.511  1.00 118.57 ?  7   LEU   A CA  1 
ATOM   9    C C   . LEU   A 1 2   ? -16.399 10.358  21.033  1.00 112.30 ?  7   LEU   A C   1 
ATOM   10   O O   . LEU   A 1 2   ? -16.825 9.446   20.327  1.00 105.47 ?  7   LEU   A O   1 
ATOM   11   C CB  . LEU   A 1 2   ? -17.424 9.871   23.279  1.00 123.34 ?  7   LEU   A CB  1 
ATOM   12   C CG  . LEU   A 1 2   ? -17.311 9.227   24.669  1.00 123.39 ?  7   LEU   A CG  1 
ATOM   13   C CD1 . LEU   A 1 2   ? -18.619 9.387   25.434  1.00 133.06 ?  7   LEU   A CD1 1 
ATOM   14   C CD2 . LEU   A 1 2   ? -16.921 7.752   24.592  1.00 114.89 ?  7   LEU   A CD2 1 
ATOM   15   N N   . ASN   A 1 3   ? -16.206 11.601  20.586  1.00 104.19 ?  8   ASN   A N   1 
ATOM   16   C CA  . ASN   A 1 3   ? -16.400 12.025  19.186  1.00 100.56 ?  8   ASN   A CA  1 
ATOM   17   C C   . ASN   A 1 3   ? -15.059 12.471  18.623  1.00 86.71  ?  8   ASN   A C   1 
ATOM   18   O O   . ASN   A 1 3   ? -14.126 12.817  19.387  1.00 80.53  ?  8   ASN   A O   1 
ATOM   19   C CB  . ASN   A 1 3   ? -17.376 13.213  19.081  1.00 101.59 ?  8   ASN   A CB  1 
ATOM   20   C CG  . ASN   A 1 3   ? -18.657 12.998  19.862  1.00 101.83 ?  8   ASN   A CG  1 
ATOM   21   O OD1 . ASN   A 1 3   ? -19.209 11.897  19.870  1.00 99.81  ?  8   ASN   A OD1 1 
ATOM   22   N ND2 . ASN   A 1 3   ? -19.139 14.049  20.526  1.00 101.42 ?  8   ASN   A ND2 1 
ATOM   23   N N   . VAL   A 1 4   ? -14.969 12.472  17.290  1.00 76.21  ?  9   VAL   A N   1 
ATOM   24   C CA  . VAL   A 1 4   ? -13.734 12.863  16.604  1.00 75.24  ?  9   VAL   A CA  1 
ATOM   25   C C   . VAL   A 1 4   ? -13.539 14.377  16.764  1.00 75.84  ?  9   VAL   A C   1 
ATOM   26   O O   . VAL   A 1 4   ? -14.443 15.145  16.448  1.00 79.34  ?  9   VAL   A O   1 
ATOM   27   C CB  . VAL   A 1 4   ? -13.688 12.385  15.117  1.00 72.73  ?  9   VAL   A CB  1 
ATOM   28   C CG1 . VAL   A 1 4   ? -14.653 13.120  14.184  1.00 80.03  ?  9   VAL   A CG1 1 
ATOM   29   C CG2 . VAL   A 1 4   ? -12.264 12.453  14.575  1.00 70.90  ?  9   VAL   A CG2 1 
ATOM   30   N N   . ILE   A 1 5   ? -12.399 14.769  17.339  1.00 70.89  ?  10  ILE   A N   1 
ATOM   31   C CA  . ILE   A 1 5   ? -12.054 16.174  17.536  1.00 69.20  ?  10  ILE   A CA  1 
ATOM   32   C C   . ILE   A 1 5   ? -11.593 16.730  16.185  1.00 65.38  ?  10  ILE   A C   1 
ATOM   33   O O   . ILE   A 1 5   ? -10.533 16.357  15.675  1.00 61.80  ?  10  ILE   A O   1 
ATOM   34   C CB  . ILE   A 1 5   ? -11.019 16.352  18.686  1.00 72.16  ?  10  ILE   A CB  1 
ATOM   35   C CG1 . ILE   A 1 5   ? -11.716 15.992  20.017  1.00 82.69  ?  10  ILE   A CG1 1 
ATOM   36   C CG2 . ILE   A 1 5   ? -10.454 17.778  18.754  1.00 74.71  ?  10  ILE   A CG2 1 
ATOM   37   C CD1 . ILE   A 1 5   ? -10.865 16.050  21.271  1.00 93.32  ?  10  ILE   A CD1 1 
ATOM   38   N N   . LYS   A 1 6   ? -12.424 17.598  15.604  1.00 67.45  ?  11  LYS   A N   1 
ATOM   39   C CA  . LYS   A 1 6   ? -12.032 18.409  14.450  1.00 66.55  ?  11  LYS   A CA  1 
ATOM   40   C C   . LYS   A 1 6   ? -11.067 19.480  14.978  1.00 69.69  ?  11  LYS   A C   1 
ATOM   41   O O   . LYS   A 1 6   ? -11.439 20.289  15.823  1.00 84.68  ?  11  LYS   A O   1 
ATOM   42   C CB  . LYS   A 1 6   ? -13.243 19.074  13.771  1.00 68.85  ?  11  LYS   A CB  1 
ATOM   43   C CG  . LYS   A 1 6   ? -14.309 18.129  13.220  1.00 73.65  ?  11  LYS   A CG  1 
ATOM   44   C CD  . LYS   A 1 6   ? -15.585 18.816  12.833  0.00 74.04  ?  11  LYS   A CD  1 
ATOM   45   C CE  . LYS   A 1 6   ? -16.687 17.828  12.480  0.00 75.64  ?  11  LYS   A CE  1 
ATOM   46   N NZ  . LYS   A 1 6   ? -17.964 18.504  12.123  0.00 79.58  ?  11  LYS   A NZ  1 
ATOM   47   N N   . MET   A 1 7   ? -9.816  19.408  14.538  1.00 68.51  ?  12  MET   A N   1 
ATOM   48   C CA  . MET   A 1 7   ? -8.767  20.346  14.902  1.00 63.53  ?  12  MET   A CA  1 
ATOM   49   C C   . MET   A 1 7   ? -8.464  21.268  13.729  1.00 64.55  ?  12  MET   A C   1 
ATOM   50   O O   . MET   A 1 7   ? -8.789  20.980  12.566  1.00 64.78  ?  12  MET   A O   1 
ATOM   51   C CB  . MET   A 1 7   ? -7.490  19.596  15.274  1.00 64.30  ?  12  MET   A CB  1 
ATOM   52   C CG  . MET   A 1 7   ? -7.617  18.672  16.465  1.00 64.87  ?  12  MET   A CG  1 
ATOM   53   S SD  . MET   A 1 7   ? -6.060  17.814  16.760  1.00 64.34  ?  12  MET   A SD  1 
ATOM   54   C CE  . MET   A 1 7   ? -6.135  17.531  18.526  1.00 60.47  ?  12  MET   A CE  1 
ATOM   55   N N   . LYS   A 1 8   ? -7.809  22.375  14.069  1.00 63.42  ?  13  LYS   A N   1 
ATOM   56   C CA  . LYS   A 1 8   ? -7.398  23.405  13.136  1.00 62.22  ?  13  LYS   A CA  1 
ATOM   57   C C   . LYS   A 1 8   ? -5.883  23.466  13.124  1.00 60.41  ?  13  LYS   A C   1 
ATOM   58   O O   . LYS   A 1 8   ? -5.249  23.232  14.152  1.00 60.06  ?  13  LYS   A O   1 
ATOM   59   C CB  . LYS   A 1 8   ? -7.962  24.746  13.598  1.00 68.26  ?  13  LYS   A CB  1 
ATOM   60   C CG  . LYS   A 1 8   ? -9.484  24.792  13.627  1.00 72.89  ?  13  LYS   A CG  1 
ATOM   61   C CD  . LYS   A 1 8   ? -10.021 26.216  13.665  1.00 79.81  ?  13  LYS   A CD  1 
ATOM   62   C CE  . LYS   A 1 8   ? -10.061 26.833  12.271  1.00 93.75  ?  13  LYS   A CE  1 
ATOM   63   N NZ  . LYS   A 1 8   ? -10.262 28.312  12.248  1.00 105.13 ?  13  LYS   A NZ  1 
ATOM   64   N N   . SER   A 1 9   ? -5.301  23.792  11.973  1.00 64.28  ?  14  SER   A N   1 
ATOM   65   C CA  . SER   A 1 9   ? -3.850  24.075  11.862  1.00 69.28  ?  14  SER   A CA  1 
ATOM   66   C C   . SER   A 1 9   ? -3.365  25.157  12.849  1.00 70.79  ?  14  SER   A C   1 
ATOM   67   O O   . SER   A 1 9   ? -2.276  25.038  13.391  1.00 70.62  ?  14  SER   A O   1 
ATOM   68   C CB  . SER   A 1 9   ? -3.476  24.505  10.428  1.00 74.15  ?  14  SER   A CB  1 
ATOM   69   O OG  . SER   A 1 9   ? -3.906  23.567  9.451   1.00 71.35  ?  14  SER   A OG  1 
ATOM   70   N N   . SER   A 1 10  ? -4.205  26.178  13.074  1.00 78.36  ?  15  SER   A N   1 
ATOM   71   C CA  . SER   A 1 10  ? -3.971  27.248  14.071  1.00 79.55  ?  15  SER   A CA  1 
ATOM   72   C C   . SER   A 1 10  ? -3.882  26.802  15.541  1.00 78.32  ?  15  SER   A C   1 
ATOM   73   O O   . SER   A 1 10  ? -3.373  27.558  16.374  1.00 88.37  ?  15  SER   A O   1 
ATOM   74   C CB  . SER   A 1 10  ? -5.049  28.338  13.962  1.00 81.23  ?  15  SER   A CB  1 
ATOM   75   O OG  . SER   A 1 10  ? -6.284  27.909  14.515  1.00 84.45  ?  15  SER   A OG  1 
ATOM   76   N N   . ASP   A 1 11  ? -4.390  25.608  15.872  1.00 73.79  ?  16  ASP   A N   1 
ATOM   77   C CA  . ASP   A 1 11  ? -4.148  24.983  17.194  1.00 73.00  ?  16  ASP   A CA  1 
ATOM   78   C C   . ASP   A 1 11  ? -2.695  24.574  17.467  1.00 78.19  ?  16  ASP   A C   1 
ATOM   79   O O   . ASP   A 1 11  ? -2.355  24.325  18.622  1.00 85.94  ?  16  ASP   A O   1 
ATOM   80   C CB  . ASP   A 1 11  ? -5.032  23.738  17.415  1.00 67.90  ?  16  ASP   A CB  1 
ATOM   81   C CG  . ASP   A 1 11  ? -6.516  24.033  17.356  1.00 64.85  ?  16  ASP   A CG  1 
ATOM   82   O OD1 . ASP   A 1 11  ? -6.926  25.183  17.606  1.00 70.34  ?  16  ASP   A OD1 1 
ATOM   83   O OD2 . ASP   A 1 11  ? -7.290  23.100  17.061  1.00 58.52  ?  16  ASP   A OD2 1 
ATOM   84   N N   . PHE   A 1 12  ? -1.858  24.494  16.424  1.00 75.42  ?  17  PHE   A N   1 
ATOM   85   C CA  . PHE   A 1 12  ? -0.461  24.084  16.535  1.00 73.39  ?  17  PHE   A CA  1 
ATOM   86   C C   . PHE   A 1 12  ? 0.514   25.256  16.413  1.00 80.56  ?  17  PHE   A C   1 
ATOM   87   O O   . PHE   A 1 12  ? 0.393   26.086  15.503  1.00 77.22  ?  17  PHE   A O   1 
ATOM   88   C CB  . PHE   A 1 12  ? -0.154  22.968  15.537  1.00 66.22  ?  17  PHE   A CB  1 
ATOM   89   C CG  . PHE   A 1 12  ? -1.068  21.793  15.696  1.00 60.47  ?  17  PHE   A CG  1 
ATOM   90   C CD1 . PHE   A 1 12  ? -0.821  20.821  16.664  1.00 60.00  ?  17  PHE   A CD1 1 
ATOM   91   C CD2 . PHE   A 1 12  ? -2.243  21.716  14.957  1.00 61.31  ?  17  PHE   A CD2 1 
ATOM   92   C CE1 . PHE   A 1 12  ? -1.695  19.760  16.848  1.00 55.37  ?  17  PHE   A CE1 1 
ATOM   93   C CE2 . PHE   A 1 12  ? -3.125  20.658  15.133  1.00 56.79  ?  17  PHE   A CE2 1 
ATOM   94   C CZ  . PHE   A 1 12  ? -2.850  19.680  16.080  1.00 55.20  ?  17  PHE   A CZ  1 
ATOM   95   N N   . LEU   A 1 13  ? 1.475   25.297  17.342  1.00 87.49  ?  18  LEU   A N   1 
ATOM   96   C CA  . LEU   A 1 13  ? 2.406   26.430  17.498  1.00 97.08  ?  18  LEU   A CA  1 
ATOM   97   C C   . LEU   A 1 13  ? 3.521   26.378  16.469  1.00 111.03 ?  18  LEU   A C   1 
ATOM   98   O O   . LEU   A 1 13  ? 3.861   27.391  15.854  1.00 143.78 ?  18  LEU   A O   1 
ATOM   99   C CB  . LEU   A 1 13  ? 3.005   26.462  18.914  1.00 97.20  ?  18  LEU   A CB  1 
ATOM   100  C CG  . LEU   A 1 13  ? 2.135   27.083  20.019  1.00 103.16 ?  18  LEU   A CG  1 
ATOM   101  C CD1 . LEU   A 1 13  ? 0.744   26.477  20.116  1.00 103.58 ?  18  LEU   A CD1 1 
ATOM   102  C CD2 . LEU   A 1 13  ? 2.823   27.000  21.380  1.00 107.86 ?  18  LEU   A CD2 1 
ATOM   103  N N   . GLU   A 1 14  ? 4.099   25.193  16.331  1.00 112.59 ?  19  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 14  ? 4.930   24.848  15.182  1.00 121.23 ?  19  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 14  ? 4.818   23.350  14.865  1.00 120.50 ?  19  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 14  ? 4.318   22.548  15.676  1.00 97.35  ?  19  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 14  ? 6.381   25.261  15.425  1.00 121.48 ?  19  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 14  ? 6.829   26.646  15.298  0.00 124.96 ?  19  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 14  ? 6.606   27.207  13.900  0.00 127.34 ?  19  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 14  ? 6.801   26.470  12.907  0.00 127.06 ?  19  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 14  ? 6.242   28.398  13.795  0.00 129.70 ?  19  GLU   A OE2 1 
ATOM   112  N N   . SER   A 1 15  ? 5.261   23.016  13.654  1.00 129.34 ?  20  SER   A N   1 
ATOM   113  C CA  . SER   A 1 15  ? 5.229   21.667  13.106  1.00 112.03 ?  20  SER   A CA  1 
ATOM   114  C C   . SER   A 1 15  ? 6.594   21.389  12.481  1.00 111.94 ?  20  SER   A C   1 
ATOM   115  O O   . SER   A 1 15  ? 6.819   21.683  11.298  1.00 119.09 ?  20  SER   A O   1 
ATOM   116  C CB  . SER   A 1 15  ? 4.098   21.528  12.076  1.00 106.68 ?  20  SER   A CB  1 
ATOM   117  O OG  . SER   A 1 15  ? 2.827   21.674  12.686  1.00 100.21 ?  20  SER   A OG  1 
ATOM   118  N N   . ALA   A 1 16  ? 7.508   20.870  13.303  1.00 101.77 ?  21  ALA   A N   1 
ATOM   119  C CA  . ALA   A 1 16  ? 8.841   20.455  12.847  1.00 107.90 ?  21  ALA   A CA  1 
ATOM   120  C C   . ALA   A 1 16  ? 8.773   19.024  12.298  1.00 107.87 ?  21  ALA   A C   1 
ATOM   121  O O   . ALA   A 1 16  ? 8.201   18.144  12.946  1.00 97.83  ?  21  ALA   A O   1 
ATOM   122  C CB  . ALA   A 1 16  ? 9.846   20.547  13.985  1.00 107.15 ?  21  ALA   A CB  1 
ATOM   123  N N   . GLU   A 1 17  ? 9.355   18.799  11.113  1.00 120.08 ?  22  GLU   A N   1 
ATOM   124  C CA  . GLU   A 1 17  ? 9.345   17.465  10.457  1.00 121.01 ?  22  GLU   A CA  1 
ATOM   125  C C   . GLU   A 1 17  ? 10.225  16.440  11.170  1.00 112.91 ?  22  GLU   A C   1 
ATOM   126  O O   . GLU   A 1 17  ? 10.194  15.260  10.826  1.00 104.29 ?  22  GLU   A O   1 
ATOM   127  C CB  . GLU   A 1 17  ? 9.764   17.545  8.975   1.00 127.31 ?  22  GLU   A CB  1 
ATOM   128  C CG  . GLU   A 1 17  ? 8.652   17.971  8.023   1.00 129.19 ?  22  GLU   A CG  1 
ATOM   129  C CD  . GLU   A 1 17  ? 8.995   17.710  6.564   1.00 136.39 ?  22  GLU   A CD  1 
ATOM   130  O OE1 . GLU   A 1 17  ? 10.150  17.963  6.155   1.00 134.74 ?  22  GLU   A OE1 1 
ATOM   131  O OE2 . GLU   A 1 17  ? 8.105   17.248  5.820   1.00 142.13 ?  22  GLU   A OE2 1 
ATOM   132  N N   . LYS   A 1 25  ? 3.339   12.928  4.496   1.00 110.86 ?  30  LYS   A N   1 
ATOM   133  C CA  . LYS   A 1 25  ? 4.118   13.872  5.302   1.00 111.61 ?  30  LYS   A CA  1 
ATOM   134  C C   . LYS   A 1 25  ? 3.832   13.753  6.822   1.00 105.25 ?  30  LYS   A C   1 
ATOM   135  O O   . LYS   A 1 25  ? 2.854   14.337  7.326   1.00 99.56  ?  30  LYS   A O   1 
ATOM   136  C CB  . LYS   A 1 25  ? 3.865   15.305  4.811   1.00 108.96 ?  30  LYS   A CB  1 
ATOM   137  C CG  . LYS   A 1 25  ? 4.314   15.611  3.385   0.00 120.00 ?  30  LYS   A CG  1 
ATOM   138  C CD  . LYS   A 1 25  ? 3.832   16.969  2.893   0.00 121.87 ?  30  LYS   A CD  1 
ATOM   139  C CE  . LYS   A 1 25  ? 4.433   17.310  1.537   0.00 130.28 ?  30  LYS   A CE  1 
ATOM   140  N NZ  . LYS   A 1 25  ? 4.076   18.683  1.084   0.00 132.84 ?  30  LYS   A NZ  1 
ATOM   141  N N   . VAL   A 1 26  ? 4.678   12.980  7.516   1.00 100.64 ?  31  VAL   A N   1 
ATOM   142  C CA  . VAL   A 1 26  ? 4.636   12.825  8.987   1.00 94.20  ?  31  VAL   A CA  1 
ATOM   143  C C   . VAL   A 1 26  ? 5.522   13.900  9.613   1.00 92.44  ?  31  VAL   A C   1 
ATOM   144  O O   . VAL   A 1 26  ? 6.696   13.999  9.259   1.00 109.36 ?  31  VAL   A O   1 
ATOM   145  C CB  . VAL   A 1 26  ? 5.139   11.437  9.454   1.00 87.45  ?  31  VAL   A CB  1 
ATOM   146  C CG1 . VAL   A 1 26  ? 5.026   11.290  10.972  1.00 77.43  ?  31  VAL   A CG1 1 
ATOM   147  C CG2 . VAL   A 1 26  ? 4.346   10.322  8.779   1.00 94.74  ?  31  VAL   A CG2 1 
ATOM   148  N N   . SER   A 1 27  ? 4.973   14.660  10.564  1.00 84.88  ?  32  SER   A N   1 
ATOM   149  C CA  . SER   A 1 27  ? 5.723   15.687  11.292  1.00 87.01  ?  32  SER   A CA  1 
ATOM   150  C C   . SER   A 1 27  ? 5.306   15.787  12.758  1.00 80.27  ?  32  SER   A C   1 
ATOM   151  O O   . SER   A 1 27  ? 4.172   15.478  13.122  1.00 86.47  ?  32  SER   A O   1 
ATOM   152  C CB  . SER   A 1 27  ? 5.577   17.049  10.603  1.00 93.40  ?  32  SER   A CB  1 
ATOM   153  O OG  . SER   A 1 27  ? 4.246   17.531  10.636  1.00 91.08  ?  32  SER   A OG  1 
ATOM   154  N N   . LEU   A 1 28  ? 6.251   16.218  13.582  1.00 79.79  ?  33  LEU   A N   1 
ATOM   155  C CA  . LEU   A 1 28  ? 6.033   16.434  15.008  1.00 75.64  ?  33  LEU   A CA  1 
ATOM   156  C C   . LEU   A 1 28  ? 5.393   17.808  15.188  1.00 74.43  ?  33  LEU   A C   1 
ATOM   157  O O   . LEU   A 1 28  ? 5.778   18.754  14.513  1.00 89.25  ?  33  LEU   A O   1 
ATOM   158  C CB  . LEU   A 1 28  ? 7.374   16.368  15.738  1.00 78.69  ?  33  LEU   A CB  1 
ATOM   159  C CG  . LEU   A 1 28  ? 7.364   16.299  17.259  1.00 79.99  ?  33  LEU   A CG  1 
ATOM   160  C CD1 . LEU   A 1 28  ? 6.802   14.977  17.744  1.00 83.69  ?  33  LEU   A CD1 1 
ATOM   161  C CD2 . LEU   A 1 28  ? 8.774   16.470  17.801  1.00 84.00  ?  33  LEU   A CD2 1 
ATOM   162  N N   . ALA   A 1 29  ? 4.442   17.915  16.110  1.00 66.73  ?  34  ALA   A N   1 
ATOM   163  C CA  . ALA   A 1 29  ? 3.573   19.090  16.239  1.00 68.20  ?  34  ALA   A CA  1 
ATOM   164  C C   . ALA   A 1 29  ? 3.150   19.314  17.685  1.00 71.26  ?  34  ALA   A C   1 
ATOM   165  O O   . ALA   A 1 29  ? 2.782   18.350  18.361  1.00 71.49  ?  34  ALA   A O   1 
ATOM   166  C CB  . ALA   A 1 29  ? 2.342   18.899  15.382  1.00 65.17  ?  34  ALA   A CB  1 
ATOM   167  N N   . PHE   A 1 30  ? 3.182   20.575  18.140  1.00 76.73  ?  35  PHE   A N   1 
ATOM   168  C CA  . PHE   A 1 30  ? 2.775   20.943  19.503  1.00 75.31  ?  35  PHE   A CA  1 
ATOM   169  C C   . PHE   A 1 30  ? 1.409   21.642  19.535  1.00 67.75  ?  35  PHE   A C   1 
ATOM   170  O O   . PHE   A 1 30  ? 1.277   22.759  19.044  1.00 63.88  ?  35  PHE   A O   1 
ATOM   171  C CB  . PHE   A 1 30  ? 3.826   21.833  20.160  1.00 82.03  ?  35  PHE   A CB  1 
ATOM   172  C CG  . PHE   A 1 30  ? 3.532   22.120  21.603  1.00 94.13  ?  35  PHE   A CG  1 
ATOM   173  C CD1 . PHE   A 1 30  ? 3.833   21.183  22.581  1.00 95.68  ?  35  PHE   A CD1 1 
ATOM   174  C CD2 . PHE   A 1 30  ? 2.915   23.316  21.991  1.00 104.30 ?  35  PHE   A CD2 1 
ATOM   175  C CE1 . PHE   A 1 30  ? 3.550   21.452  23.921  1.00 102.05 ?  35  PHE   A CE1 1 
ATOM   176  C CE2 . PHE   A 1 30  ? 2.615   23.578  23.329  1.00 104.77 ?  35  PHE   A CE2 1 
ATOM   177  C CZ  . PHE   A 1 30  ? 2.942   22.645  24.300  1.00 98.64  ?  35  PHE   A CZ  1 
ATOM   178  N N   . HIS   A 1 31  ? 0.423   20.987  20.152  1.00 65.76  ?  36  HIS   A N   1 
ATOM   179  C CA  . HIS   A 1 31  ? -0.907  21.560  20.380  1.00 70.23  ?  36  HIS   A CA  1 
ATOM   180  C C   . HIS   A 1 31  ? -0.864  22.574  21.532  1.00 82.71  ?  36  HIS   A C   1 
ATOM   181  O O   . HIS   A 1 31  ? -0.223  22.311  22.557  1.00 84.90  ?  36  HIS   A O   1 
ATOM   182  C CB  . HIS   A 1 31  ? -1.897  20.449  20.710  1.00 66.94  ?  36  HIS   A CB  1 
ATOM   183  C CG  . HIS   A 1 31  ? -3.328  20.835  20.502  1.00 68.91  ?  36  HIS   A CG  1 
ATOM   184  N ND1 . HIS   A 1 31  ? -4.065  21.508  21.448  1.00 70.53  ?  36  HIS   A ND1 1 
ATOM   185  C CD2 . HIS   A 1 31  ? -4.160  20.638  19.453  1.00 75.05  ?  36  HIS   A CD2 1 
ATOM   186  C CE1 . HIS   A 1 31  ? -5.291  21.702  21.001  1.00 75.99  ?  36  HIS   A CE1 1 
ATOM   187  N NE2 . HIS   A 1 31  ? -5.375  21.188  19.787  1.00 78.01  ?  36  HIS   A NE2 1 
ATOM   188  N N   . ARG   A 1 32  ? -1.565  23.703  21.369  1.00 85.77  ?  37  ARG   A N   1 
ATOM   189  C CA  . ARG   A 1 32  ? -1.479  24.866  22.293  1.00 89.12  ?  37  ARG   A CA  1 
ATOM   190  C C   . ARG   A 1 32  ? -1.900  24.544  23.732  1.00 90.03  ?  37  ARG   A C   1 
ATOM   191  O O   . ARG   A 1 32  ? -1.227  24.955  24.671  1.00 97.70  ?  37  ARG   A O   1 
ATOM   192  C CB  . ARG   A 1 32  ? -2.278  26.075  21.764  1.00 94.08  ?  37  ARG   A CB  1 
ATOM   193  C CG  . ARG   A 1 32  ? -1.990  27.386  22.521  1.00 110.54 ?  37  ARG   A CG  1 
ATOM   194  C CD  . ARG   A 1 32  ? -2.537  28.682  21.897  1.00 101.86 ?  37  ARG   A CD  1 
ATOM   195  N NE  . ARG   A 1 32  ? -1.871  29.100  20.653  1.00 94.04  ?  37  ARG   A NE  1 
ATOM   196  C CZ  . ARG   A 1 32  ? -2.216  28.738  19.406  1.00 88.06  ?  37  ARG   A CZ  1 
ATOM   197  N NH1 . ARG   A 1 32  ? -3.248  27.910  19.146  1.00 78.57  ?  37  ARG   A NH1 1 
ATOM   198  N NH2 . ARG   A 1 32  ? -1.505  29.210  18.379  1.00 83.74  ?  37  ARG   A NH2 1 
ATOM   199  N N   . THR   A 1 33  ? -3.015  23.830  23.878  1.00 92.86  ?  38  THR   A N   1 
ATOM   200  C CA  . THR   A 1 33  ? -3.508  23.299  25.171  1.00 93.10  ?  38  THR   A CA  1 
ATOM   201  C C   . THR   A 1 33  ? -3.223  21.818  25.521  1.00 86.64  ?  38  THR   A C   1 
ATOM   202  O O   . THR   A 1 33  ? -3.372  21.457  26.690  1.00 94.31  ?  38  THR   A O   1 
ATOM   203  C CB  . THR   A 1 33  ? -5.041  23.531  25.328  1.00 91.72  ?  38  THR   A CB  1 
ATOM   204  O OG1 . THR   A 1 33  ? -5.776  22.684  24.433  1.00 90.10  ?  38  THR   A OG1 1 
ATOM   205  C CG2 . THR   A 1 33  ? -5.416  25.002  25.083  1.00 94.15  ?  38  THR   A CG2 1 
ATOM   206  N N   . GLN   A 1 34  ? -2.792  20.992  24.560  1.00 81.29  ?  39  GLN   A N   1 
ATOM   207  C CA  . GLN   A 1 34  ? -2.741  19.502  24.687  1.00 80.03  ?  39  GLN   A CA  1 
ATOM   208  C C   . GLN   A 1 34  ? -1.348  18.835  24.477  1.00 71.08  ?  39  GLN   A C   1 
ATOM   209  O O   . GLN   A 1 34  ? -1.248  17.596  24.446  1.00 73.84  ?  39  GLN   A O   1 
ATOM   210  C CB  . GLN   A 1 34  ? -3.784  18.862  23.749  1.00 83.60  ?  39  GLN   A CB  1 
ATOM   211  C CG  . GLN   A 1 34  ? -5.231  19.102  24.126  1.00 92.81  ?  39  GLN   A CG  1 
ATOM   212  C CD  . GLN   A 1 34  ? -6.189  18.404  23.163  1.00 104.94 ?  39  GLN   A CD  1 
ATOM   213  O OE1 . GLN   A 1 34  ? -6.068  17.201  22.919  1.00 104.34 ?  39  GLN   A OE1 1 
ATOM   214  N NE2 . GLN   A 1 34  ? -7.145  19.153  22.607  1.00 117.76 ?  39  GLN   A NE2 1 
ATOM   215  N N   . GLY   A 1 35  ? -0.281  19.624  24.357  1.00 69.26  ?  40  GLY   A N   1 
ATOM   216  C CA  . GLY   A 1 35  ? 1.072   19.094  24.286  1.00 72.38  ?  40  GLY   A CA  1 
ATOM   217  C C   . GLY   A 1 35  ? 1.500   18.507  22.948  1.00 71.99  ?  40  GLY   A C   1 
ATOM   218  O O   . GLY   A 1 35  ? 0.930   18.813  21.883  1.00 65.17  ?  40  GLY   A O   1 
ATOM   219  N N   . LEU   A 1 36  ? 2.508   17.640  23.030  1.00 76.78  ?  41  LEU   A N   1 
ATOM   220  C CA  . LEU   A 1 36  ? 3.214   17.138  21.868  1.00 73.45  ?  41  LEU   A CA  1 
ATOM   221  C C   . LEU   A 1 36  ? 2.437   16.014  21.206  1.00 64.29  ?  41  LEU   A C   1 
ATOM   222  O O   . LEU   A 1 36  ? 1.973   15.102  21.879  1.00 68.12  ?  41  LEU   A O   1 
ATOM   223  C CB  . LEU   A 1 36  ? 4.607   16.648  22.270  1.00 80.35  ?  41  LEU   A CB  1 
ATOM   224  C CG  . LEU   A 1 36  ? 5.613   16.395  21.145  1.00 97.81  ?  41  LEU   A CG  1 
ATOM   225  C CD1 . LEU   A 1 36  ? 6.001   17.687  20.438  1.00 103.57 ?  41  LEU   A CD1 1 
ATOM   226  C CD2 . LEU   A 1 36  ? 6.853   15.708  21.696  1.00 106.12 ?  41  LEU   A CD2 1 
ATOM   227  N N   . MET   A 1 37  ? 2.326   16.099  19.880  1.00 59.89  ?  42  MET   A N   1 
ATOM   228  C CA  . MET   A 1 37  ? 1.580   15.166  19.042  1.00 57.19  ?  42  MET   A CA  1 
ATOM   229  C C   . MET   A 1 37  ? 2.323   14.899  17.735  1.00 55.63  ?  42  MET   A C   1 
ATOM   230  O O   . MET   A 1 37  ? 3.344   15.518  17.461  1.00 59.78  ?  42  MET   A O   1 
ATOM   231  C CB  . MET   A 1 37  ? 0.210   15.754  18.717  1.00 63.54  ?  42  MET   A CB  1 
ATOM   232  C CG  . MET   A 1 37  ? -0.597  16.110  19.931  1.00 64.43  ?  42  MET   A CG  1 
ATOM   233  S SD  . MET   A 1 37  ? -2.226  16.622  19.427  1.00 61.03  ?  42  MET   A SD  1 
ATOM   234  C CE  . MET   A 1 37  ? -2.910  16.963  21.051  1.00 65.20  ?  42  MET   A CE  1 
ATOM   235  N N   . ILE   A 1 38  ? 1.808   13.954  16.951  1.00 51.33  ?  43  ILE   A N   1 
ATOM   236  C CA  . ILE   A 1 38  ? 2.320   13.641  15.618  1.00 56.08  ?  43  ILE   A CA  1 
ATOM   237  C C   . ILE   A 1 38  ? 1.215   13.936  14.612  1.00 55.74  ?  43  ILE   A C   1 
ATOM   238  O O   . ILE   A 1 38  ? 0.085   13.483  14.794  1.00 54.99  ?  43  ILE   A O   1 
ATOM   239  C CB  . ILE   A 1 38  ? 2.785   12.158  15.532  1.00 51.84  ?  43  ILE   A CB  1 
ATOM   240  C CG1 . ILE   A 1 38  ? 4.182   12.029  16.148  1.00 50.02  ?  43  ILE   A CG1 1 
ATOM   241  C CG2 . ILE   A 1 38  ? 2.863   11.643  14.095  1.00 53.38  ?  43  ILE   A CG2 1 
ATOM   242  C CD1 . ILE   A 1 38  ? 5.378   12.539  15.422  0.00 49.21  ?  43  ILE   A CD1 1 
ATOM   243  N N   . MET   A 1 39  ? 1.566   14.664  13.547  1.00 57.05  ?  44  MET   A N   1 
ATOM   244  C CA  . MET   A 1 39  ? 0.643   15.025  12.477  1.00 59.33  ?  44  MET   A CA  1 
ATOM   245  C C   . MET   A 1 39  ? 1.033   14.283  11.211  1.00 59.11  ?  44  MET   A C   1 
ATOM   246  O O   . MET   A 1 39  ? 2.087   14.561  10.629  1.00 63.29  ?  44  MET   A O   1 
ATOM   247  C CB  . MET   A 1 39  ? 0.678   16.537  12.222  1.00 64.24  ?  44  MET   A CB  1 
ATOM   248  C CG  . MET   A 1 39  ? -0.363  17.014  11.211  1.00 69.72  ?  44  MET   A CG  1 
ATOM   249  S SD  . MET   A 1 39  ? -0.482  18.800  11.082  1.00 86.35  ?  44  MET   A SD  1 
ATOM   250  C CE  . MET   A 1 39  ? -1.111  19.240  12.699  1.00 81.06  ?  44  MET   A CE  1 
ATOM   251  N N   . LYS   A 1 40  ? 0.193   13.333  10.812  1.00 56.74  ?  45  LYS   A N   1 
ATOM   252  C CA  . LYS   A 1 40  ? 0.307   12.695  9.507   1.00 68.21  ?  45  LYS   A CA  1 
ATOM   253  C C   . LYS   A 1 40  ? -0.608  13.470  8.564   1.00 67.33  ?  45  LYS   A C   1 
ATOM   254  O O   . LYS   A 1 40  ? -1.827  13.310  8.632   1.00 64.43  ?  45  LYS   A O   1 
ATOM   255  C CB  . LYS   A 1 40  ? -0.064  11.196  9.567   1.00 69.97  ?  45  LYS   A CB  1 
ATOM   256  C CG  . LYS   A 1 40  ? -0.136  10.544  8.193   1.00 78.07  ?  45  LYS   A CG  1 
ATOM   257  C CD  . LYS   A 1 40  ? 0.126   9.045   8.199   1.00 78.73  ?  45  LYS   A CD  1 
ATOM   258  C CE  . LYS   A 1 40  ? 0.101   8.482   6.780   1.00 85.77  ?  45  LYS   A CE  1 
ATOM   259  N NZ  . LYS   A 1 40  ? 1.217   7.529   6.545   1.00 94.43  ?  45  LYS   A NZ  1 
ATOM   260  N N   . THR   A 1 41  ? -0.013  14.322  7.722   1.00 68.50  ?  46  THR   A N   1 
ATOM   261  C CA  . THR   A 1 41  ? -0.742  15.066  6.704   1.00 75.54  ?  46  THR   A CA  1 
ATOM   262  C C   . THR   A 1 41  ? -0.804  14.200  5.449   1.00 79.03  ?  46  THR   A C   1 
ATOM   263  O O   . THR   A 1 41  ? 0.215   13.967  4.785   1.00 77.41  ?  46  THR   A O   1 
ATOM   264  C CB  . THR   A 1 41  ? -0.111  16.449  6.412   1.00 78.56  ?  46  THR   A CB  1 
ATOM   265  O OG1 . THR   A 1 41  ? -0.062  17.209  7.625   1.00 75.90  ?  46  THR   A OG1 1 
ATOM   266  C CG2 . THR   A 1 41  ? -0.940  17.231  5.403   1.00 78.78  ?  46  THR   A CG2 1 
ATOM   267  N N   . VAL   A 1 42  ? -2.021  13.760  5.132   1.00 76.44  ?  47  VAL   A N   1 
ATOM   268  C CA  . VAL   A 1 42  ? -2.276  12.779  4.089   1.00 77.80  ?  47  VAL   A CA  1 
ATOM   269  C C   . VAL   A 1 42  ? -2.298  13.466  2.729   1.00 84.94  ?  47  VAL   A C   1 
ATOM   270  O O   . VAL   A 1 42  ? -1.631  12.992  1.807   1.00 90.71  ?  47  VAL   A O   1 
ATOM   271  C CB  . VAL   A 1 42  ? -3.589  12.005  4.364   1.00 77.98  ?  47  VAL   A CB  1 
ATOM   272  C CG1 . VAL   A 1 42  ? -3.848  10.949  3.297   1.00 84.49  ?  47  VAL   A CG1 1 
ATOM   273  C CG2 . VAL   A 1 42  ? -3.511  11.331  5.732   1.00 76.93  ?  47  VAL   A CG2 1 
ATOM   274  N N   . TYR   A 1 43  ? -3.065  14.558  2.611   1.00 87.89  ?  48  TYR   A N   1 
ATOM   275  C CA  . TYR   A 1 43  ? -3.190  15.336  1.354   1.00 93.30  ?  48  TYR   A CA  1 
ATOM   276  C C   . TYR   A 1 43  ? -3.045  16.831  1.609   1.00 93.17  ?  48  TYR   A C   1 
ATOM   277  O O   . TYR   A 1 43  ? -3.626  17.348  2.555   1.00 87.72  ?  48  TYR   A O   1 
ATOM   278  C CB  . TYR   A 1 43  ? -4.532  15.041  0.658   1.00 99.01  ?  48  TYR   A CB  1 
ATOM   279  C CG  . TYR   A 1 43  ? -4.811  15.821  -0.632  1.00 108.84 ?  48  TYR   A CG  1 
ATOM   280  C CD1 . TYR   A 1 43  ? -3.936  15.756  -1.731  1.00 118.55 ?  48  TYR   A CD1 1 
ATOM   281  C CD2 . TYR   A 1 43  ? -5.960  16.615  -0.763  1.00 110.72 ?  48  TYR   A CD2 1 
ATOM   282  C CE1 . TYR   A 1 43  ? -4.195  16.468  -2.906  1.00 124.95 ?  48  TYR   A CE1 1 
ATOM   283  C CE2 . TYR   A 1 43  ? -6.231  17.321  -1.931  1.00 118.15 ?  48  TYR   A CE2 1 
ATOM   284  C CZ  . TYR   A 1 43  ? -5.349  17.249  -2.998  1.00 123.94 ?  48  TYR   A CZ  1 
ATOM   285  O OH  . TYR   A 1 43  ? -5.618  17.950  -4.144  1.00 132.25 ?  48  TYR   A OH  1 
ATOM   286  N N   . LYS   A 1 44  ? -2.265  17.500  0.751   1.00 104.94 ?  49  LYS   A N   1 
ATOM   287  C CA  . LYS   A 1 44  ? -2.057  18.960  0.759   1.00 109.04 ?  49  LYS   A CA  1 
ATOM   288  C C   . LYS   A 1 44  ? -2.049  19.437  -0.695  1.00 119.38 ?  49  LYS   A C   1 
ATOM   289  O O   . LYS   A 1 44  ? -1.310  18.881  -1.518  1.00 125.87 ?  49  LYS   A O   1 
ATOM   290  C CB  . LYS   A 1 44  ? -0.723  19.305  1.443   1.00 108.01 ?  49  LYS   A CB  1 
ATOM   291  C CG  . LYS   A 1 44  ? -0.606  20.746  1.937   1.00 104.01 ?  49  LYS   A CG  1 
ATOM   292  C CD  . LYS   A 1 44  ? 0.641   20.985  2.805   1.00 99.70  ?  49  LYS   A CD  1 
ATOM   293  C CE  . LYS   A 1 44  ? 0.521   20.370  4.199   1.00 84.82  ?  49  LYS   A CE  1 
ATOM   294  N NZ  . LYS   A 1 44  ? 1.663   20.619  5.114   1.00 79.17  ?  49  LYS   A NZ  1 
ATOM   295  N N   . GLY   A 1 45  ? -2.881  20.433  -1.011  1.00 126.81 ?  50  GLY   A N   1 
ATOM   296  C CA  . GLY   A 1 45  ? -2.961  21.006  -2.367  1.00 135.96 ?  50  GLY   A CA  1 
ATOM   297  C C   . GLY   A 1 45  ? -4.324  21.623  -2.660  1.00 140.82 ?  50  GLY   A C   1 
ATOM   298  O O   . GLY   A 1 45  ? -4.915  22.220  -1.750  1.00 132.33 ?  50  GLY   A O   1 
ATOM   299  N N   . PRO   A 1 46  ? -4.826  21.505  -3.921  1.00 154.48 ?  51  PRO   A N   1 
ATOM   300  C CA  . PRO   A 1 46  ? -6.159  22.050  -4.243  1.00 155.94 ?  51  PRO   A CA  1 
ATOM   301  C C   . PRO   A 1 46  ? -7.286  21.274  -3.558  1.00 152.55 ?  51  PRO   A C   1 
ATOM   302  O O   . PRO   A 1 46  ? -7.238  20.042  -3.528  1.00 150.96 ?  51  PRO   A O   1 
ATOM   303  C CB  . PRO   A 1 46  ? -6.244  21.896  -5.764  1.00 161.71 ?  51  PRO   A CB  1 
ATOM   304  C CG  . PRO   A 1 46  ? -5.341  20.765  -6.086  1.00 163.00 ?  51  PRO   A CG  1 
ATOM   305  C CD  . PRO   A 1 46  ? -4.212  20.867  -5.107  1.00 161.65 ?  51  PRO   A CD  1 
ATOM   306  N N   . ASN   A 1 47  ? -8.273  21.991  -3.014  1.00 150.71 ?  52  ASN   A N   1 
ATOM   307  C CA  . ASN   A 1 47  ? -9.358  21.369  -2.242  1.00 148.56 ?  52  ASN   A CA  1 
ATOM   308  C C   . ASN   A 1 47  ? -10.379 20.679  -3.163  1.00 151.34 ?  52  ASN   A C   1 
ATOM   309  O O   . ASN   A 1 47  ? -10.656 21.165  -4.272  1.00 151.48 ?  52  ASN   A O   1 
ATOM   310  C CB  . ASN   A 1 47  ? -10.054 22.397  -1.337  1.00 146.15 ?  52  ASN   A CB  1 
ATOM   311  C CG  . ASN   A 1 47  ? -10.742 23.573  -2.012  0.00 157.49 ?  52  ASN   A CG  1 
ATOM   312  O OD1 . ASN   A 1 47  ? -10.464 23.909  -3.162  0.00 163.85 ?  52  ASN   A OD1 1 
ATOM   313  N ND2 . ASN   A 1 47  ? -11.612 24.258  -1.264  0.00 155.16 ?  52  ASN   A ND2 1 
ATOM   314  N N   . CYS   A 1 48  ? -10.884 19.525  -2.705  1.00 149.89 ?  53  CYS   A N   1 
ATOM   315  C CA  . CYS   A 1 48  ? -11.857 18.696  -3.440  1.00 152.71 ?  53  CYS   A CA  1 
ATOM   316  C C   . CYS   A 1 48  ? -12.868 18.051  -2.471  1.00 144.95 ?  53  CYS   A C   1 
ATOM   317  O O   . CYS   A 1 48  ? -12.572 17.050  -1.817  1.00 125.87 ?  53  CYS   A O   1 
ATOM   318  C CB  . CYS   A 1 48  ? -11.144 17.618  -4.278  1.00 153.22 ?  53  CYS   A CB  1 
ATOM   319  S SG  . CYS   A 1 48  ? -10.418 18.242  -5.811  1.00 152.89 ?  53  CYS   A SG  1 
ATOM   320  N N   . ILE   A 1 49  ? -14.063 18.647  -2.402  1.00 155.12 ?  54  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 49  ? -15.197 18.166  -1.583  1.00 152.31 ?  54  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 49  ? -15.961 17.068  -2.361  1.00 151.25 ?  54  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 49  ? -15.938 17.053  -3.586  1.00 152.54 ?  54  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 49  ? -16.098 19.370  -1.157  1.00 153.82 ?  54  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 49  ? -15.296 20.343  -0.281  1.00 140.26 ?  54  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 49  ? -17.327 18.953  -0.349  1.00 152.60 ?  54  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 49  ? -15.988 21.587  0.102   0.00 150.06 ?  54  ILE   A CD1 1 
ATOM   328  N N   . GLU   A 1 50  ? -16.642 16.190  -1.616  1.00 140.85 ?  55  GLU   A N   1 
ATOM   329  C CA  . GLU   A 1 50  ? -17.336 14.952  -2.059  1.00 138.67 ?  55  GLU   A CA  1 
ATOM   330  C C   . GLU   A 1 50  ? -16.591 13.690  -1.561  1.00 132.56 ?  55  GLU   A C   1 
ATOM   331  O O   . GLU   A 1 50  ? -17.053 12.564  -1.777  1.00 142.37 ?  55  GLU   A O   1 
ATOM   332  C CB  . GLU   A 1 50  ? -17.687 14.874  -3.563  1.00 140.68 ?  55  GLU   A CB  1 
ATOM   333  C CG  . GLU   A 1 50  ? -16.832 14.236  -4.605  0.00 151.22 ?  55  GLU   A CG  1 
ATOM   334  C CD  . GLU   A 1 50  ? -17.404 14.333  -6.012  0.00 159.82 ?  55  GLU   A CD  1 
ATOM   335  O OE1 . GLU   A 1 50  ? -18.598 14.010  -6.203  0.00 162.76 ?  55  GLU   A OE1 1 
ATOM   336  O OE2 . GLU   A 1 50  ? -16.656 14.726  -6.932  0.00 164.10 ?  55  GLU   A OE2 1 
ATOM   337  N N   . HIS   A 1 51  ? -15.440 13.889  -0.914  1.00 118.22 ?  56  HIS   A N   1 
ATOM   338  C CA  . HIS   A 1 51  ? -14.877 12.929  0.013   1.00 115.60 ?  56  HIS   A CA  1 
ATOM   339  C C   . HIS   A 1 51  ? -14.990 13.339  1.492   1.00 110.38 ?  56  HIS   A C   1 
ATOM   340  O O   . HIS   A 1 51  ? -14.859 12.463  2.317   1.00 108.13 ?  56  HIS   A O   1 
ATOM   341  C CB  . HIS   A 1 51  ? -13.413 12.675  -0.337  1.00 119.26 ?  56  HIS   A CB  1 
ATOM   342  C CG  . HIS   A 1 51  ? -13.232 11.942  -1.626  0.00 124.50 ?  56  HIS   A CG  1 
ATOM   343  N ND1 . HIS   A 1 51  ? -13.003 10.590  -1.770  0.00 125.66 ?  56  HIS   A ND1 1 
ATOM   344  C CD2 . HIS   A 1 51  ? -13.304 12.447  -2.878  0.00 130.88 ?  56  HIS   A CD2 1 
ATOM   345  C CE1 . HIS   A 1 51  ? -12.921 10.296  -3.055  0.00 132.46 ?  56  HIS   A CE1 1 
ATOM   346  N NE2 . HIS   A 1 51  ? -13.099 11.405  -3.749  0.00 135.74 ?  56  HIS   A NE2 1 
ATOM   347  N N   . ASN   A 1 52  ? -15.215 14.621  1.821   1.00 101.36 ?  57  ASN   A N   1 
ATOM   348  C CA  . ASN   A 1 52  ? -15.169 15.111  3.225   1.00 91.59  ?  57  ASN   A CA  1 
ATOM   349  C C   . ASN   A 1 52  ? -16.162 14.441  4.174   1.00 87.79  ?  57  ASN   A C   1 
ATOM   350  O O   . ASN   A 1 52  ? -15.838 14.211  5.338   1.00 93.74  ?  57  ASN   A O   1 
ATOM   351  C CB  . ASN   A 1 52  ? -15.389 16.630  3.303   1.00 91.93  ?  57  ASN   A CB  1 
ATOM   352  C CG  . ASN   A 1 52  ? -14.202 17.425  2.801   1.00 89.80  ?  57  ASN   A CG  1 
ATOM   353  O OD1 . ASN   A 1 52  ? -13.388 16.939  2.017   1.00 91.61  ?  57  ASN   A OD1 1 
ATOM   354  N ND2 . ASN   A 1 52  ? -14.101 18.668  3.249   1.00 87.34  ?  57  ASN   A ND2 1 
ATOM   355  N N   . GLU   A 1 53  ? -17.358 14.147  3.676   1.00 91.08  ?  58  GLU   A N   1 
ATOM   356  C CA  . GLU   A 1 53  ? -18.377 13.435  4.456   1.00 87.63  ?  58  GLU   A CA  1 
ATOM   357  C C   . GLU   A 1 53  ? -17.909 12.015  4.773   1.00 83.78  ?  58  GLU   A C   1 
ATOM   358  O O   . GLU   A 1 53  ? -17.980 11.577  5.923   1.00 85.35  ?  58  GLU   A O   1 
ATOM   359  C CB  . GLU   A 1 53  ? -19.717 13.410  3.711   1.00 92.74  ?  58  GLU   A CB  1 
ATOM   360  C CG  . GLU   A 1 53  ? -20.358 14.748  3.287   0.00 95.61  ?  58  GLU   A CG  1 
ATOM   361  C CD  . GLU   A 1 53  ? -20.852 15.620  4.444   0.00 93.46  ?  58  GLU   A CD  1 
ATOM   362  O OE1 . GLU   A 1 53  ? -20.919 16.854  4.249   0.00 94.51  ?  58  GLU   A OE1 1 
ATOM   363  O OE2 . GLU   A 1 53  ? -21.173 15.098  5.539   0.00 91.25  ?  58  GLU   A OE2 1 
ATOM   364  N N   . ALA   A 1 54  ? -17.403 11.327  3.751   1.00 84.59  ?  59  ALA   A N   1 
ATOM   365  C CA  . ALA   A 1 54  ? -16.824 9.984   3.891   1.00 85.40  ?  59  ALA   A CA  1 
ATOM   366  C C   . ALA   A 1 54  ? -15.525 9.950   4.717   1.00 79.82  ?  59  ALA   A C   1 
ATOM   367  O O   . ALA   A 1 54  ? -15.308 9.006   5.479   1.00 76.97  ?  59  ALA   A O   1 
ATOM   368  C CB  . ALA   A 1 54  ? -16.580 9.370   2.518   1.00 90.10  ?  59  ALA   A CB  1 
ATOM   369  N N   . LEU   A 1 55  ? -14.667 10.953  4.524   1.00 74.25  ?  60  LEU   A N   1 
ATOM   370  C CA  . LEU   A 1 55  ? -13.412 11.104  5.276   1.00 68.84  ?  60  LEU   A CA  1 
ATOM   371  C C   . LEU   A 1 55  ? -13.654 11.324  6.761   1.00 66.57  ?  60  LEU   A C   1 
ATOM   372  O O   . LEU   A 1 55  ? -12.980 10.708  7.594   1.00 67.70  ?  60  LEU   A O   1 
ATOM   373  C CB  . LEU   A 1 55  ? -12.558 12.256  4.726   1.00 67.97  ?  60  LEU   A CB  1 
ATOM   374  C CG  . LEU   A 1 55  ? -11.847 12.001  3.402   1.00 71.97  ?  60  LEU   A CG  1 
ATOM   375  C CD1 . LEU   A 1 55  ? -11.427 13.319  2.784   1.00 75.97  ?  60  LEU   A CD1 1 
ATOM   376  C CD2 . LEU   A 1 55  ? -10.621 11.123  3.586   1.00 74.08  ?  60  LEU   A CD2 1 
ATOM   377  N N   . LEU   A 1 56  ? -14.604 12.202  7.084   1.00 70.90  ?  61  LEU   A N   1 
ATOM   378  C CA  . LEU   A 1 56  ? -14.986 12.453  8.472   1.00 71.47  ?  61  LEU   A CA  1 
ATOM   379  C C   . LEU   A 1 56  ? -15.575 11.208  9.109   1.00 68.91  ?  61  LEU   A C   1 
ATOM   380  O O   . LEU   A 1 56  ? -15.233 10.900  10.244  1.00 66.07  ?  61  LEU   A O   1 
ATOM   381  C CB  . LEU   A 1 56  ? -15.986 13.607  8.590   1.00 78.18  ?  61  LEU   A CB  1 
ATOM   382  C CG  . LEU   A 1 56  ? -16.331 14.098  10.009  1.00 82.87  ?  61  LEU   A CG  1 
ATOM   383  C CD1 . LEU   A 1 56  ? -15.147 14.796  10.662  1.00 79.53  ?  61  LEU   A CD1 1 
ATOM   384  C CD2 . LEU   A 1 56  ? -17.529 15.032  9.979   1.00 90.60  ?  61  LEU   A CD2 1 
ATOM   385  N N   . GLU   A 1 57  ? -16.449 10.513  8.376   1.00 75.23  ?  62  GLU   A N   1 
ATOM   386  C CA  . GLU   A 1 57  ? -17.043 9.254   8.850   1.00 79.88  ?  62  GLU   A CA  1 
ATOM   387  C C   . GLU   A 1 57  ? -15.969 8.177   9.127   1.00 78.54  ?  62  GLU   A C   1 
ATOM   388  O O   . GLU   A 1 57  ? -16.072 7.461   10.116  1.00 79.55  ?  62  GLU   A O   1 
ATOM   389  C CB  . GLU   A 1 57  ? -18.103 8.756   7.847   1.00 90.96  ?  62  GLU   A CB  1 
ATOM   390  C CG  . GLU   A 1 57  ? -18.798 7.436   8.172   1.00 109.83 ?  62  GLU   A CG  1 
ATOM   391  C CD  . GLU   A 1 57  ? -19.404 7.390   9.564   1.00 122.86 ?  62  GLU   A CD  1 
ATOM   392  O OE1 . GLU   A 1 57  ? -20.025 8.398   9.985   1.00 113.00 ?  62  GLU   A OE1 1 
ATOM   393  O OE2 . GLU   A 1 57  ? -19.257 6.337   10.236  1.00 126.62 ?  62  GLU   A OE2 1 
ATOM   394  N N   . GLU   A 1 58  ? -14.951 8.084   8.271   1.00 75.85  ?  63  GLU   A N   1 
ATOM   395  C CA  . GLU   A 1 58  ? -13.809 7.181   8.510   1.00 71.48  ?  63  GLU   A CA  1 
ATOM   396  C C   . GLU   A 1 58  ? -12.982 7.586   9.717   1.00 69.80  ?  63  GLU   A C   1 
ATOM   397  O O   . GLU   A 1 58  ? -12.509 6.719   10.450  1.00 77.53  ?  63  GLU   A O   1 
ATOM   398  C CB  . GLU   A 1 58  ? -12.902 7.049   7.280   1.00 71.02  ?  63  GLU   A CB  1 
ATOM   399  C CG  . GLU   A 1 58  ? -13.289 5.879   6.385   1.00 74.38  ?  63  GLU   A CG  1 
ATOM   400  C CD  . GLU   A 1 58  ? -12.540 5.846   5.079   1.00 76.02  ?  63  GLU   A CD  1 
ATOM   401  O OE1 . GLU   A 1 58  ? -11.344 6.192   5.046   1.00 75.98  ?  63  GLU   A OE1 1 
ATOM   402  O OE2 . GLU   A 1 58  ? -13.140 5.448   4.058   1.00 78.57  ?  63  GLU   A OE2 1 
ATOM   403  N N   . ALA   A 1 59  ? -12.794 8.891   9.917   1.00 67.41  ?  64  ALA   A N   1 
ATOM   404  C CA  . ALA   A 1 59  ? -12.145 9.403   11.127  1.00 62.13  ?  64  ALA   A CA  1 
ATOM   405  C C   . ALA   A 1 59  ? -12.973 9.119   12.395  1.00 59.83  ?  64  ALA   A C   1 
ATOM   406  O O   . ALA   A 1 59  ? -12.387 8.908   13.447  1.00 50.32  ?  64  ALA   A O   1 
ATOM   407  C CB  . ALA   A 1 59  ? -11.864 10.886  10.990  1.00 65.24  ?  64  ALA   A CB  1 
ATOM   408  N N   . LYS   A 1 60  ? -14.312 9.126   12.281  1.00 62.75  ?  65  LYS   A N   1 
ATOM   409  C CA  . LYS   A 1 60  ? -15.207 8.659   13.353  1.00 64.25  ?  65  LYS   A CA  1 
ATOM   410  C C   . LYS   A 1 60  ? -14.993 7.175   13.692  1.00 63.57  ?  65  LYS   A C   1 
ATOM   411  O O   . LYS   A 1 60  ? -15.011 6.820   14.883  1.00 68.91  ?  65  LYS   A O   1 
ATOM   412  C CB  . LYS   A 1 60  ? -16.698 8.945   13.047  1.00 71.67  ?  65  LYS   A CB  1 
ATOM   413  C CG  . LYS   A 1 60  ? -17.108 10.414  13.107  1.00 72.10  ?  65  LYS   A CG  1 
ATOM   414  C CD  . LYS   A 1 60  ? -18.566 10.658  12.914  0.00 74.74  ?  65  LYS   A CD  1 
ATOM   415  C CE  . LYS   A 1 60  ? -18.887 12.144  12.965  0.00 75.39  ?  65  LYS   A CE  1 
ATOM   416  N NZ  . LYS   A 1 60  ? -20.350 12.413  13.027  0.00 79.64  ?  65  LYS   A NZ  1 
ATOM   417  N N   A MET   A 1 61  ? -14.798 6.327   12.671  0.50 65.40  ?  66  MET   A N   1 
ATOM   418  N N   B MET   A 1 61  ? -14.795 6.330   12.676  0.50 62.64  ?  66  MET   A N   1 
ATOM   419  C CA  A MET   A 1 61  ? -14.483 4.898   12.877  0.50 67.46  ?  66  MET   A CA  1 
ATOM   420  C CA  B MET   A 1 61  ? -14.486 4.910   12.892  0.50 62.83  ?  66  MET   A CA  1 
ATOM   421  C C   A MET   A 1 61  ? -13.125 4.705   13.572  0.50 64.76  ?  66  MET   A C   1 
ATOM   422  C C   B MET   A 1 61  ? -13.123 4.703   13.571  0.50 62.05  ?  66  MET   A C   1 
ATOM   423  O O   A MET   A 1 61  ? -13.007 3.878   14.485  0.50 64.66  ?  66  MET   A O   1 
ATOM   424  O O   B MET   A 1 61  ? -13.003 3.874   14.483  0.50 62.02  ?  66  MET   A O   1 
ATOM   425  C CB  A MET   A 1 61  ? -14.482 4.107   11.555  0.50 73.41  ?  66  MET   A CB  1 
ATOM   426  C CB  B MET   A 1 61  ? -14.558 4.134   11.580  0.50 64.98  ?  66  MET   A CB  1 
ATOM   427  C CG  A MET   A 1 61  ? -15.824 3.893   10.875  0.50 82.11  ?  66  MET   A CG  1 
ATOM   428  C CG  B MET   A 1 61  ? -15.958 4.084   10.972  0.50 69.85  ?  66  MET   A CG  1 
ATOM   429  S SD  A MET   A 1 61  ? -15.567 3.116   9.258   0.50 88.77  ?  66  MET   A SD  1 
ATOM   430  S SD  B MET   A 1 61  ? -17.259 3.427   12.042  0.50 69.50  ?  66  MET   A SD  1 
ATOM   431  C CE  A MET   A 1 61  ? -16.553 4.176   8.199   0.50 89.59  ?  66  MET   A CE  1 
ATOM   432  C CE  B MET   A 1 61  ? -17.277 1.703   11.539  0.50 72.97  ?  66  MET   A CE  1 
ATOM   433  N N   . MET   A 1 62  ? -12.113 5.460   13.132  1.00 59.55  ?  67  MET   A N   1 
ATOM   434  C CA  . MET   A 1 62  ? -10.785 5.502   13.807  1.00 57.97  ?  67  MET   A CA  1 
ATOM   435  C C   . MET   A 1 62  ? -10.870 5.890   15.296  1.00 62.52  ?  67  MET   A C   1 
ATOM   436  O O   . MET   A 1 62  ? -10.160 5.350   16.151  1.00 69.11  ?  67  MET   A O   1 
ATOM   437  C CB  . MET   A 1 62  ? -9.855  6.529   13.146  1.00 57.24  ?  67  MET   A CB  1 
ATOM   438  C CG  . MET   A 1 62  ? -9.370  6.210   11.753  1.00 61.59  ?  67  MET   A CG  1 
ATOM   439  S SD  . MET   A 1 62  ? -8.449  7.572   11.026  1.00 62.12  ?  67  MET   A SD  1 
ATOM   440  C CE  . MET   A 1 62  ? -8.539  7.181   9.282   1.00 64.23  ?  67  MET   A CE  1 
ATOM   441  N N   . ASN   A 1 63  ? -11.729 6.864   15.577  1.00 60.53  ?  68  ASN   A N   1 
ATOM   442  C CA  . ASN   A 1 63  ? -11.954 7.376   16.915  1.00 60.20  ?  68  ASN   A CA  1 
ATOM   443  C C   . ASN   A 1 63  ? -12.577 6.360   17.896  1.00 63.28  ?  68  ASN   A C   1 
ATOM   444  O O   . ASN   A 1 63  ? -12.356 6.473   19.111  1.00 64.60  ?  68  ASN   A O   1 
ATOM   445  C CB  . ASN   A 1 63  ? -12.841 8.631   16.824  1.00 64.49  ?  68  ASN   A CB  1 
ATOM   446  C CG  . ASN   A 1 63  ? -12.763 9.498   18.053  1.00 63.96  ?  68  ASN   A CG  1 
ATOM   447  O OD1 . ASN   A 1 63  ? -13.742 9.629   18.789  1.00 62.05  ?  68  ASN   A OD1 1 
ATOM   448  N ND2 . ASN   A 1 63  ? -11.589 10.044  18.322  1.00 62.26  ?  68  ASN   A ND2 1 
ATOM   449  N N   . ARG   A 1 64  ? -13.359 5.392   17.388  1.00 67.84  ?  69  ARG   A N   1 
ATOM   450  C CA  . ARG   A 1 64  ? -13.928 4.291   18.221  1.00 65.68  ?  69  ARG   A CA  1 
ATOM   451  C C   . ARG   A 1 64  ? -12.886 3.373   18.901  1.00 63.21  ?  69  ARG   A C   1 
ATOM   452  O O   . ARG   A 1 64  ? -13.166 2.800   19.957  1.00 64.49  ?  69  ARG   A O   1 
ATOM   453  C CB  . ARG   A 1 64  ? -14.855 3.375   17.396  1.00 77.83  ?  69  ARG   A CB  1 
ATOM   454  C CG  . ARG   A 1 64  ? -16.124 3.992   16.804  1.00 95.74  ?  69  ARG   A CG  1 
ATOM   455  C CD  . ARG   A 1 64  ? -16.984 2.949   16.069  1.00 112.55 ?  69  ARG   A CD  1 
ATOM   456  N NE  . ARG   A 1 64  ? -16.224 2.181   15.057  1.00 121.27 ?  69  ARG   A NE  1 
ATOM   457  C CZ  . ARG   A 1 64  ? -15.742 0.928   15.169  1.00 113.21 ?  69  ARG   A CZ  1 
ATOM   458  N NH1 . ARG   A 1 64  ? -15.938 0.165   16.256  1.00 111.32 ?  69  ARG   A NH1 1 
ATOM   459  N NH2 . ARG   A 1 64  ? -15.051 0.412   14.144  1.00 113.33 ?  69  ARG   A NH2 1 
ATOM   460  N N   . LEU   A 1 65  ? -11.709 3.234   18.283  1.00 59.58  ?  70  LEU   A N   1 
ATOM   461  C CA  . LEU   A 1 65  ? -10.685 2.275   18.696  1.00 54.87  ?  70  LEU   A CA  1 
ATOM   462  C C   . LEU   A 1 65  ? -9.758  2.854   19.757  1.00 53.53  ?  70  LEU   A C   1 
ATOM   463  O O   . LEU   A 1 65  ? -8.707  3.424   19.439  1.00 58.05  ?  70  LEU   A O   1 
ATOM   464  C CB  . LEU   A 1 65  ? -9.899  1.784   17.474  1.00 51.12  ?  70  LEU   A CB  1 
ATOM   465  C CG  . LEU   A 1 65  ? -10.762 1.134   16.382  1.00 54.18  ?  70  LEU   A CG  1 
ATOM   466  C CD1 . LEU   A 1 65  ? -9.963  0.953   15.102  1.00 53.82  ?  70  LEU   A CD1 1 
ATOM   467  C CD2 . LEU   A 1 65  ? -11.370 -0.183  16.840  1.00 58.99  ?  70  LEU   A CD2 1 
ATOM   468  N N   . ARG   A 1 66  ? -10.158 2.683   21.022  1.00 55.76  ?  71  ARG   A N   1 
ATOM   469  C CA  . ARG   A 1 66  ? -9.412  3.171   22.200  1.00 57.32  ?  71  ARG   A CA  1 
ATOM   470  C C   . ARG   A 1 66  ? -8.872  1.974   22.987  1.00 54.19  ?  71  ARG   A C   1 
ATOM   471  O O   . ARG   A 1 66  ? -9.644  1.162   23.492  1.00 58.58  ?  71  ARG   A O   1 
ATOM   472  C CB  . ARG   A 1 66  ? -10.296 4.005   23.143  1.00 67.31  ?  71  ARG   A CB  1 
ATOM   473  C CG  . ARG   A 1 66  ? -11.178 5.056   22.504  1.00 74.06  ?  71  ARG   A CG  1 
ATOM   474  C CD  . ARG   A 1 66  ? -10.388 6.253   22.024  1.00 78.15  ?  71  ARG   A CD  1 
ATOM   475  N NE  . ARG   A 1 66  ? -11.317 7.213   21.441  1.00 87.46  ?  71  ARG   A NE  1 
ATOM   476  C CZ  . ARG   A 1 66  ? -12.156 8.015   22.111  1.00 90.85  ?  71  ARG   A CZ  1 
ATOM   477  N NH1 . ARG   A 1 66  ? -12.212 8.051   23.449  1.00 93.12  ?  71  ARG   A NH1 1 
ATOM   478  N NH2 . ARG   A 1 66  ? -12.954 8.814   21.419  1.00 94.92  ?  71  ARG   A NH2 1 
ATOM   479  N N   . HIS   A 1 67  ? -7.553  1.882   23.098  1.00 49.71  ?  72  HIS   A N   1 
ATOM   480  C CA  . HIS   A 1 67  ? -6.893  0.787   23.800  1.00 46.50  ?  72  HIS   A CA  1 
ATOM   481  C C   . HIS   A 1 67  ? -5.433  1.168   24.027  1.00 46.04  ?  72  HIS   A C   1 
ATOM   482  O O   . HIS   A 1 67  ? -4.819  1.737   23.147  1.00 45.72  ?  72  HIS   A O   1 
ATOM   483  C CB  . HIS   A 1 67  ? -6.994  -0.511  22.999  1.00 46.46  ?  72  HIS   A CB  1 
ATOM   484  C CG  . HIS   A 1 67  ? -6.517  -1.701  23.750  1.00 53.19  ?  72  HIS   A CG  1 
ATOM   485  N ND1 . HIS   A 1 67  ? -5.324  -2.327  23.466  1.00 56.10  ?  72  HIS   A ND1 1 
ATOM   486  C CD2 . HIS   A 1 67  ? -7.051  -2.362  24.799  1.00 56.32  ?  72  HIS   A CD2 1 
ATOM   487  C CE1 . HIS   A 1 67  ? -5.146  -3.331  24.302  1.00 59.56  ?  72  HIS   A CE1 1 
ATOM   488  N NE2 . HIS   A 1 67  ? -6.183  -3.377  25.118  1.00 62.65  ?  72  HIS   A NE2 1 
ATOM   489  N N   . SER   A 1 68  ? -4.891  0.854   25.203  1.00 52.02  ?  73  SER   A N   1 
ATOM   490  C CA  . SER   A 1 68  ? -3.507  1.200   25.591  1.00 50.00  ?  73  SER   A CA  1 
ATOM   491  C C   . SER   A 1 68  ? -2.390  0.727   24.637  1.00 47.96  ?  73  SER   A C   1 
ATOM   492  O O   . SER   A 1 68  ? -1.291  1.293   24.632  1.00 54.88  ?  73  SER   A O   1 
ATOM   493  C CB  . SER   A 1 68  ? -3.226  0.680   27.014  1.00 54.21  ?  73  SER   A CB  1 
ATOM   494  O OG  . SER   A 1 68  ? -3.530  -0.700  27.116  1.00 63.24  ?  73  SER   A OG  1 
ATOM   495  N N   . ARG   A 1 69  ? -2.649  -0.356  23.915  1.00 49.06  ?  74  ARG   A N   1 
ATOM   496  C CA  . ARG   A 1 69  ? -1.758  -0.895  22.868  1.00 51.31  ?  74  ARG   A CA  1 
ATOM   497  C C   . ARG   A 1 69  ? -2.210  -0.623  21.434  1.00 51.68  ?  74  ARG   A C   1 
ATOM   498  O O   . ARG   A 1 69  ? -1.792  -1.342  20.510  1.00 57.08  ?  74  ARG   A O   1 
ATOM   499  C CB  . ARG   A 1 69  ? -1.561  -2.410  23.080  1.00 51.55  ?  74  ARG   A CB  1 
ATOM   500  C CG  . ARG   A 1 69  ? -1.357  -2.866  24.514  1.00 52.18  ?  74  ARG   A CG  1 
ATOM   501  C CD  . ARG   A 1 69  ? -0.252  -2.109  25.234  1.00 56.68  ?  74  ARG   A CD  1 
ATOM   502  N NE  . ARG   A 1 69  ? -0.307  -2.382  26.662  1.00 66.80  ?  74  ARG   A NE  1 
ATOM   503  C CZ  . ARG   A 1 69  ? 0.273   -1.668  27.631  1.00 67.66  ?  74  ARG   A CZ  1 
ATOM   504  N NH1 . ARG   A 1 69  ? 0.985   -0.562  27.386  1.00 63.05  ?  74  ARG   A NH1 1 
ATOM   505  N NH2 . ARG   A 1 69  ? 0.103   -2.072  28.888  1.00 76.76  ?  74  ARG   A NH2 1 
ATOM   506  N N   . VAL   A 1 70  ? -3.029  0.411   21.235  1.00 47.15  ?  75  VAL   A N   1 
ATOM   507  C CA  . VAL   A 1 70  ? -3.469  0.850   19.908  1.00 46.99  ?  75  VAL   A CA  1 
ATOM   508  C C   . VAL   A 1 70  ? -3.227  2.355   19.843  1.00 49.27  ?  75  VAL   A C   1 
ATOM   509  O O   . VAL   A 1 70  ? -3.545  3.073   20.791  1.00 51.48  ?  75  VAL   A O   1 
ATOM   510  C CB  . VAL   A 1 70  ? -4.945  0.507   19.656  1.00 46.35  ?  75  VAL   A CB  1 
ATOM   511  C CG1 . VAL   A 1 70  ? -5.405  1.031   18.300  1.00 50.82  ?  75  VAL   A CG1 1 
ATOM   512  C CG2 . VAL   A 1 70  ? -5.160  -1.007  19.722  1.00 49.60  ?  75  VAL   A CG2 1 
ATOM   513  N N   . VAL   A 1 71  ? -2.670  2.823   18.725  1.00 54.62  ?  76  VAL   A N   1 
ATOM   514  C CA  . VAL   A 1 71  ? -2.371  4.259   18.539  1.00 53.30  ?  76  VAL   A CA  1 
ATOM   515  C C   . VAL   A 1 71  ? -3.702  5.016   18.494  1.00 47.34  ?  76  VAL   A C   1 
ATOM   516  O O   . VAL   A 1 71  ? -4.559  4.668   17.707  1.00 45.35  ?  76  VAL   A O   1 
ATOM   517  C CB  . VAL   A 1 71  ? -1.550  4.524   17.255  1.00 54.79  ?  76  VAL   A CB  1 
ATOM   518  C CG1 . VAL   A 1 71  ? -1.394  6.020   16.987  1.00 58.64  ?  76  VAL   A CG1 1 
ATOM   519  C CG2 . VAL   A 1 71  ? -0.175  3.886   17.373  1.00 54.92  ?  76  VAL   A CG2 1 
ATOM   520  N N   . LYS   A 1 72  ? -3.866  6.009   19.367  1.00 46.05  ?  77  LYS   A N   1 
ATOM   521  C CA  . LYS   A 1 72  ? -5.105  6.781   19.482  1.00 46.61  ?  77  LYS   A CA  1 
ATOM   522  C C   . LYS   A 1 72  ? -5.060  7.926   18.467  1.00 48.83  ?  77  LYS   A C   1 
ATOM   523  O O   . LYS   A 1 72  ? -4.001  8.557   18.279  1.00 44.65  ?  77  LYS   A O   1 
ATOM   524  C CB  . LYS   A 1 72  ? -5.285  7.313   20.910  1.00 47.36  ?  77  LYS   A CB  1 
ATOM   525  C CG  . LYS   A 1 72  ? -6.704  7.714   21.274  1.00 55.96  ?  77  LYS   A CG  1 
ATOM   526  C CD  . LYS   A 1 72  ? -6.890  8.367   22.558  0.00 49.79  ?  77  LYS   A CD  1 
ATOM   527  C CE  . LYS   A 1 72  ? -8.155  9.216   22.602  0.00 51.06  ?  77  LYS   A CE  1 
ATOM   528  N NZ  . LYS   A 1 72  ? -8.494  9.681   23.974  0.00 53.34  ?  77  LYS   A NZ  1 
ATOM   529  N N   . LEU   A 1 73  ? -6.182  8.142   17.777  1.00 46.77  ?  78  LEU   A N   1 
ATOM   530  C CA  . LEU   A 1 73  ? -6.368  9.331   16.943  1.00 48.43  ?  78  LEU   A CA  1 
ATOM   531  C C   . LEU   A 1 73  ? -6.815  10.432  17.890  1.00 46.70  ?  78  LEU   A C   1 
ATOM   532  O O   . LEU   A 1 73  ? -7.915  10.363  18.438  1.00 48.26  ?  78  LEU   A O   1 
ATOM   533  C CB  . LEU   A 1 73  ? -7.422  9.093   15.861  1.00 50.56  ?  78  LEU   A CB  1 
ATOM   534  C CG  . LEU   A 1 73  ? -7.705  10.228  14.871  1.00 50.14  ?  78  LEU   A CG  1 
ATOM   535  C CD1 . LEU   A 1 73  ? -6.565  10.412  13.887  1.00 51.19  ?  78  LEU   A CD1 1 
ATOM   536  C CD2 . LEU   A 1 73  ? -8.972  9.928   14.100  1.00 56.66  ?  78  LEU   A CD2 1 
ATOM   537  N N   . LEU   A 1 74  ? -5.955  11.420  18.101  1.00 46.36  ?  79  LEU   A N   1 
ATOM   538  C CA  . LEU   A 1 74  ? -6.269  12.564  18.970  1.00 50.06  ?  79  LEU   A CA  1 
ATOM   539  C C   . LEU   A 1 74  ? -7.193  13.591  18.299  1.00 51.08  ?  79  LEU   A C   1 
ATOM   540  O O   . LEU   A 1 74  ? -7.938  14.311  18.973  1.00 52.78  ?  79  LEU   A O   1 
ATOM   541  C CB  . LEU   A 1 74  ? -4.980  13.239  19.431  1.00 50.42  ?  79  LEU   A CB  1 
ATOM   542  C CG  . LEU   A 1 74  ? -3.994  12.349  20.188  1.00 51.72  ?  79  LEU   A CG  1 
ATOM   543  C CD1 . LEU   A 1 74  ? -2.763  13.161  20.547  1.00 58.02  ?  79  LEU   A CD1 1 
ATOM   544  C CD2 . LEU   A 1 74  ? -4.608  11.752  21.441  1.00 47.67  ?  79  LEU   A CD2 1 
ATOM   545  N N   . GLY   A 1 75  ? -7.104  13.688  16.982  1.00 52.21  ?  80  GLY   A N   1 
ATOM   546  C CA  . GLY   A 1 75  ? -8.025  14.499  16.209  1.00 55.37  ?  80  GLY   A CA  1 
ATOM   547  C C   . GLY   A 1 75  ? -7.754  14.400  14.729  1.00 53.07  ?  80  GLY   A C   1 
ATOM   548  O O   . GLY   A 1 75  ? -6.863  13.672  14.304  1.00 47.27  ?  80  GLY   A O   1 
ATOM   549  N N   . VAL   A 1 76  ? -8.517  15.166  13.963  1.00 57.06  ?  81  VAL   A N   1 
ATOM   550  C CA  . VAL   A 1 76  ? -8.409  15.213  12.504  1.00 60.87  ?  81  VAL   A CA  1 
ATOM   551  C C   . VAL   A 1 76  ? -8.456  16.675  12.024  1.00 58.50  ?  81  VAL   A C   1 
ATOM   552  O O   . VAL   A 1 76  ? -9.185  17.476  12.597  1.00 65.41  ?  81  VAL   A O   1 
ATOM   553  C CB  . VAL   A 1 76  ? -9.515  14.322  11.884  1.00 61.59  ?  81  VAL   A CB  1 
ATOM   554  C CG1 . VAL   A 1 76  ? -10.920 14.885  12.105  1.00 67.33  ?  81  VAL   A CG1 1 
ATOM   555  C CG2 . VAL   A 1 76  ? -9.266  14.086  10.415  1.00 66.43  ?  81  VAL   A CG2 1 
ATOM   556  N N   . ILE   A 1 77  ? -7.667  17.008  11.001  1.00 57.47  ?  82  ILE   A N   1 
ATOM   557  C CA  . ILE   A 1 77  ? -7.733  18.300  10.321  1.00 56.85  ?  82  ILE   A CA  1 
ATOM   558  C C   . ILE   A 1 77  ? -8.368  18.031  8.970   1.00 59.23  ?  82  ILE   A C   1 
ATOM   559  O O   . ILE   A 1 77  ? -7.829  17.273  8.184   1.00 61.82  ?  82  ILE   A O   1 
ATOM   560  C CB  . ILE   A 1 77  ? -6.342  18.958  10.173  1.00 58.80  ?  82  ILE   A CB  1 
ATOM   561  C CG1 . ILE   A 1 77  ? -5.751  19.229  11.568  1.00 54.90  ?  82  ILE   A CG1 1 
ATOM   562  C CG2 . ILE   A 1 77  ? -6.412  20.282  9.388   1.00 63.75  ?  82  ILE   A CG2 1 
ATOM   563  C CD1 . ILE   A 1 77  ? -4.290  19.635  11.577  1.00 58.18  ?  82  ILE   A CD1 1 
ATOM   564  N N   . ILE   A 1 78  ? -9.520  18.646  8.730   1.00 65.07  ?  83  ILE   A N   1 
ATOM   565  C CA  . ILE   A 1 78  ? -10.167 18.664  7.422   1.00 69.34  ?  83  ILE   A CA  1 
ATOM   566  C C   . ILE   A 1 78  ? -10.340 20.151  7.125   1.00 73.51  ?  83  ILE   A C   1 
ATOM   567  O O   . ILE   A 1 78  ? -11.238 20.786  7.677   1.00 76.61  ?  83  ILE   A O   1 
ATOM   568  C CB  . ILE   A 1 78  ? -11.503 17.876  7.424   1.00 67.84  ?  83  ILE   A CB  1 
ATOM   569  C CG1 . ILE   A 1 78  ? -11.242 16.376  7.707   1.00 65.91  ?  83  ILE   A CG1 1 
ATOM   570  C CG2 . ILE   A 1 78  ? -12.225 18.027  6.082   1.00 72.46  ?  83  ILE   A CG2 1 
ATOM   571  C CD1 . ILE   A 1 78  ? -12.473 15.535  8.007   1.00 65.27  ?  83  ILE   A CD1 1 
ATOM   572  N N   . GLU   A 1 79  ? -9.461  20.688  6.279   1.00 76.56  ?  84  GLU   A N   1 
ATOM   573  C CA  . GLU   A 1 79  ? -9.488  22.087  5.852   1.00 83.97  ?  84  GLU   A CA  1 
ATOM   574  C C   . GLU   A 1 79  ? -9.518  22.208  4.327   1.00 94.28  ?  84  GLU   A C   1 
ATOM   575  O O   . GLU   A 1 79  ? -9.461  21.204  3.609   1.00 101.53 ?  84  GLU   A O   1 
ATOM   576  C CB  . GLU   A 1 79  ? -8.273  22.798  6.431   1.00 84.05  ?  84  GLU   A CB  1 
ATOM   577  C CG  . GLU   A 1 79  ? -8.360  22.990  7.939   1.00 83.24  ?  84  GLU   A CG  1 
ATOM   578  C CD  . GLU   A 1 79  ? -7.215  23.809  8.526   1.00 84.41  ?  84  GLU   A CD  1 
ATOM   579  O OE1 . GLU   A 1 79  ? -6.134  23.898  7.901   1.00 88.51  ?  84  GLU   A OE1 1 
ATOM   580  O OE2 . GLU   A 1 79  ? -7.402  24.371  9.630   1.00 80.75  ?  84  GLU   A OE2 1 
ATOM   581  N N   . GLU   A 1 80  ? -9.651  23.447  3.849   1.00 105.25 ?  85  GLU   A N   1 
ATOM   582  C CA  . GLU   A 1 80  ? -9.619  23.747  2.416   1.00 113.70 ?  85  GLU   A CA  1 
ATOM   583  C C   . GLU   A 1 80  ? -8.225  23.412  1.878   1.00 109.06 ?  85  GLU   A C   1 
ATOM   584  O O   . GLU   A 1 80  ? -7.292  24.216  2.000   1.00 104.19 ?  85  GLU   A O   1 
ATOM   585  C CB  . GLU   A 1 80  ? -10.002 25.212  2.138   1.00 119.23 ?  85  GLU   A CB  1 
ATOM   586  C CG  . GLU   A 1 80  ? -11.517 25.457  2.416   0.00 117.18 ?  85  GLU   A CG  1 
ATOM   587  C CD  . GLU   A 1 80  ? -11.981 26.825  1.949   0.00 121.64 ?  85  GLU   A CD  1 
ATOM   588  O OE1 . GLU   A 1 80  ? -11.283 27.826  2.220   0.00 122.37 ?  85  GLU   A OE1 1 
ATOM   589  O OE2 . GLU   A 1 80  ? -13.056 26.901  1.317   0.00 124.63 ?  85  GLU   A OE2 1 
ATOM   590  N N   . GLY   A 1 81  ? -8.095  22.193  1.347   1.00 102.53 ?  86  GLY   A N   1 
ATOM   591  C CA  . GLY   A 1 81  ? -6.866  21.739  0.696   1.00 104.83 ?  86  GLY   A CA  1 
ATOM   592  C C   . GLY   A 1 81  ? -5.953  20.834  1.509   1.00 100.74 ?  86  GLY   A C   1 
ATOM   593  O O   . GLY   A 1 81  ? -5.191  20.062  0.911   1.00 105.69 ?  86  GLY   A O   1 
ATOM   594  N N   . LYS   A 1 82  ? -6.002  20.936  2.846   1.00 92.67  ?  87  LYS   A N   1 
ATOM   595  C CA  . LYS   A 1 82  ? -5.145  20.166  3.764   1.00 86.18  ?  87  LYS   A CA  1 
ATOM   596  C C   . LYS   A 1 82  ? -5.982  19.117  4.502   1.00 80.81  ?  87  LYS   A C   1 
ATOM   597  O O   . LYS   A 1 82  ? -7.059  19.439  5.005   1.00 83.85  ?  87  LYS   A O   1 
ATOM   598  C CB  . LYS   A 1 82  ? -4.474  21.106  4.780   1.00 86.63  ?  87  LYS   A CB  1 
ATOM   599  C CG  . LYS   A 1 82  ? -3.412  20.454  5.669   1.00 88.48  ?  87  LYS   A CG  1 
ATOM   600  C CD  . LYS   A 1 82  ? -2.879  21.398  6.738   1.00 89.43  ?  87  LYS   A CD  1 
ATOM   601  C CE  . LYS   A 1 82  ? -2.101  20.636  7.802   1.00 92.29  ?  87  LYS   A CE  1 
ATOM   602  N NZ  . LYS   A 1 82  ? -1.527  21.501  8.872   1.00 98.31  ?  87  LYS   A NZ  1 
ATOM   603  N N   . TYR   A 1 83  ? -5.475  17.881  4.578   1.00 75.60  ?  88  TYR   A N   1 
ATOM   604  C CA  . TYR   A 1 83  ? -6.117  16.767  5.304   1.00 66.23  ?  88  TYR   A CA  1 
ATOM   605  C C   . TYR   A 1 83  ? -5.051  16.041  6.120   1.00 60.02  ?  88  TYR   A C   1 
ATOM   606  O O   . TYR   A 1 83  ? -4.023  15.613  5.561   1.00 59.35  ?  88  TYR   A O   1 
ATOM   607  C CB  . TYR   A 1 83  ? -6.767  15.787  4.335   1.00 69.79  ?  88  TYR   A CB  1 
ATOM   608  C CG  . TYR   A 1 83  ? -7.904  16.358  3.529   1.00 72.99  ?  88  TYR   A CG  1 
ATOM   609  C CD1 . TYR   A 1 83  ? -7.653  17.109  2.383   1.00 77.40  ?  88  TYR   A CD1 1 
ATOM   610  C CD2 . TYR   A 1 83  ? -9.240  16.135  3.893   1.00 72.73  ?  88  TYR   A CD2 1 
ATOM   611  C CE1 . TYR   A 1 83  ? -8.687  17.638  1.616   1.00 81.21  ?  88  TYR   A CE1 1 
ATOM   612  C CE2 . TYR   A 1 83  ? -10.288 16.657  3.131   1.00 76.01  ?  88  TYR   A CE2 1 
ATOM   613  C CZ  . TYR   A 1 83  ? -10.005 17.412  1.988   1.00 81.31  ?  88  TYR   A CZ  1 
ATOM   614  O OH  . TYR   A 1 83  ? -11.006 17.952  1.205   1.00 86.92  ?  88  TYR   A OH  1 
ATOM   615  N N   . SER   A 1 84  ? -5.296  15.914  7.426   1.00 55.53  ?  89  SER   A N   1 
ATOM   616  C CA  . SER   A 1 84  ? -4.327  15.351  8.365   1.00 54.90  ?  89  SER   A CA  1 
ATOM   617  C C   . SER   A 1 84  ? -4.984  14.524  9.446   1.00 52.03  ?  89  SER   A C   1 
ATOM   618  O O   . SER   A 1 84  ? -6.102  14.820  9.870   1.00 49.95  ?  89  SER   A O   1 
ATOM   619  C CB  . SER   A 1 84  ? -3.480  16.433  9.057   1.00 55.71  ?  89  SER   A CB  1 
ATOM   620  O OG  . SER   A 1 84  ? -2.804  17.277  8.138   1.00 60.55  ?  89  SER   A OG  1 
ATOM   621  N N   . LEU   A 1 85  ? -4.267  13.483  9.874   1.00 52.83  ?  90  LEU   A N   1 
ATOM   622  C CA  . LEU   A 1 85  ? -4.616  12.696  11.055  1.00 48.90  ?  90  LEU   A CA  1 
ATOM   623  C C   . LEU   A 1 85  ? -3.601  13.069  12.109  1.00 46.51  ?  90  LEU   A C   1 
ATOM   624  O O   . LEU   A 1 85  ? -2.400  13.188  11.822  1.00 46.76  ?  90  LEU   A O   1 
ATOM   625  C CB  . LEU   A 1 85  ? -4.559  11.200  10.764  1.00 48.42  ?  90  LEU   A CB  1 
ATOM   626  C CG  . LEU   A 1 85  ? -5.505  10.721  9.652   1.00 51.52  ?  90  LEU   A CG  1 
ATOM   627  C CD1 . LEU   A 1 85  ? -5.159  9.317   9.189   1.00 54.13  ?  90  LEU   A CD1 1 
ATOM   628  C CD2 . LEU   A 1 85  ? -6.942  10.779  10.133  1.00 51.40  ?  90  LEU   A CD2 1 
ATOM   629  N N   . VAL   A 1 86  ? -4.095  13.269  13.324  1.00 47.88  ?  91  VAL   A N   1 
ATOM   630  C CA  . VAL   A 1 86  ? -3.281  13.697  14.449  1.00 49.79  ?  91  VAL   A CA  1 
ATOM   631  C C   . VAL   A 1 86  ? -3.349  12.595  15.482  1.00 50.89  ?  91  VAL   A C   1 
ATOM   632  O O   . VAL   A 1 86  ? -4.432  12.261  15.972  1.00 48.91  ?  91  VAL   A O   1 
ATOM   633  C CB  . VAL   A 1 86  ? -3.756  15.025  15.053  1.00 49.06  ?  91  VAL   A CB  1 
ATOM   634  C CG1 . VAL   A 1 86  ? -2.863  15.419  16.228  1.00 47.58  ?  91  VAL   A CG1 1 
ATOM   635  C CG2 . VAL   A 1 86  ? -3.707  16.117  13.990  1.00 53.48  ?  91  VAL   A CG2 1 
ATOM   636  N N   . MET   A 1 87  ? -2.178  12.046  15.803  1.00 55.62  ?  92  MET   A N   1 
ATOM   637  C CA  . MET   A 1 87  ? -2.055  10.906  16.692  1.00 53.73  ?  92  MET   A CA  1 
ATOM   638  C C   . MET   A 1 87  ? -0.952  11.133  17.691  1.00 57.79  ?  92  MET   A C   1 
ATOM   639  O O   . MET   A 1 87  ? -0.175  12.093  17.580  1.00 70.67  ?  92  MET   A O   1 
ATOM   640  C CB  . MET   A 1 87  ? -1.824  9.645   15.877  1.00 54.61  ?  92  MET   A CB  1 
ATOM   641  C CG  . MET   A 1 87  ? -0.474  9.561   15.210  1.00 56.78  ?  92  MET   A CG  1 
ATOM   642  S SD  . MET   A 1 87  ? -0.543  8.640   13.693  1.00 65.15  ?  92  MET   A SD  1 
ATOM   643  C CE  . MET   A 1 87  ? 1.175   8.139   13.693  1.00 78.09  ?  92  MET   A CE  1 
ATOM   644  N N   . GLU   A 1 88  ? -0.905  10.245  18.673  1.00 61.70  ?  93  GLU   A N   1 
ATOM   645  C CA  . GLU   A 1 88  ? 0.005   10.409  19.807  1.00 65.55  ?  93  GLU   A CA  1 
ATOM   646  C C   . GLU   A 1 88  ? 1.451   10.048  19.455  1.00 55.89  ?  93  GLU   A C   1 
ATOM   647  O O   . GLU   A 1 88  ? 1.707   9.229   18.590  1.00 54.46  ?  93  GLU   A O   1 
ATOM   648  C CB  . GLU   A 1 88  ? -0.514  9.687   21.061  1.00 69.81  ?  93  GLU   A CB  1 
ATOM   649  C CG  . GLU   A 1 88  ? -0.600  8.167   21.003  1.00 79.47  ?  93  GLU   A CG  1 
ATOM   650  C CD  . GLU   A 1 88  ? -1.634  7.594   21.959  1.00 82.82  ?  93  GLU   A CD  1 
ATOM   651  O OE1 . GLU   A 1 88  ? -1.747  8.076   23.105  1.00 97.60  ?  93  GLU   A OE1 1 
ATOM   652  O OE2 . GLU   A 1 88  ? -2.327  6.631   21.563  1.00 87.26  ?  93  GLU   A OE2 1 
ATOM   653  N N   . TYR   A 1 89  ? 2.371   10.716  20.137  1.00 60.51  ?  94  TYR   A N   1 
ATOM   654  C CA  . TYR   A 1 89  ? 3.809   10.625  19.884  1.00 58.55  ?  94  TYR   A CA  1 
ATOM   655  C C   . TYR   A 1 89  ? 4.362   9.374   20.534  1.00 54.59  ?  94  TYR   A C   1 
ATOM   656  O O   . TYR   A 1 89  ? 4.086   9.118   21.709  1.00 54.06  ?  94  TYR   A O   1 
ATOM   657  C CB  . TYR   A 1 89  ? 4.521   11.862  20.463  1.00 56.45  ?  94  TYR   A CB  1 
ATOM   658  C CG  . TYR   A 1 89  ? 6.022   11.910  20.288  1.00 52.96  ?  94  TYR   A CG  1 
ATOM   659  C CD1 . TYR   A 1 89  ? 6.605   11.904  19.012  1.00 52.30  ?  94  TYR   A CD1 1 
ATOM   660  C CD2 . TYR   A 1 89  ? 6.869   12.024  21.396  1.00 54.70  ?  94  TYR   A CD2 1 
ATOM   661  C CE1 . TYR   A 1 89  ? 7.985   11.968  18.844  1.00 56.34  ?  94  TYR   A CE1 1 
ATOM   662  C CE2 . TYR   A 1 89  ? 8.258   12.097  21.236  1.00 59.69  ?  94  TYR   A CE2 1 
ATOM   663  C CZ  . TYR   A 1 89  ? 8.811   12.085  19.959  1.00 60.20  ?  94  TYR   A CZ  1 
ATOM   664  O OH  . TYR   A 1 89  ? 10.176  12.163  19.807  1.00 64.02  ?  94  TYR   A OH  1 
ATOM   665  N N   . MET   A 1 90  ? 5.167   8.632   19.775  1.00 56.32  ?  95  MET   A N   1 
ATOM   666  C CA  . MET   A 1 90  ? 5.896   7.455   20.257  1.00 55.93  ?  95  MET   A CA  1 
ATOM   667  C C   . MET   A 1 90  ? 7.370   7.713   19.975  1.00 59.59  ?  95  MET   A C   1 
ATOM   668  O O   . MET   A 1 90  ? 7.812   7.644   18.821  1.00 57.70  ?  95  MET   A O   1 
ATOM   669  C CB  . MET   A 1 90  ? 5.398   6.190   19.555  1.00 57.64  ?  95  MET   A CB  1 
ATOM   670  C CG  . MET   A 1 90  ? 3.897   5.957   19.672  1.00 62.34  ?  95  MET   A CG  1 
ATOM   671  S SD  . MET   A 1 90  ? 3.301   5.756   21.368  1.00 65.90  ?  95  MET   A SD  1 
ATOM   672  C CE  . MET   A 1 90  ? 3.771   4.051   21.643  1.00 70.12  ?  95  MET   A CE  1 
ATOM   673  N N   . GLU   A 1 91  ? 8.117   8.019   21.040  1.00 64.56  ?  96  GLU   A N   1 
ATOM   674  C CA  . GLU   A 1 91  ? 9.473   8.589   20.936  1.00 66.42  ?  96  GLU   A CA  1 
ATOM   675  C C   . GLU   A 1 91  ? 10.499  7.711   20.218  1.00 68.69  ?  96  GLU   A C   1 
ATOM   676  O O   . GLU   A 1 91  ? 11.256  8.226   19.401  1.00 70.55  ?  96  GLU   A O   1 
ATOM   677  C CB  . GLU   A 1 91  ? 9.981   8.979   22.326  1.00 66.92  ?  96  GLU   A CB  1 
ATOM   678  C CG  . GLU   A 1 91  ? 11.388  9.552   22.361  1.00 78.72  ?  96  GLU   A CG  1 
ATOM   679  C CD  . GLU   A 1 91  ? 11.691  10.369  23.596  1.00 91.30  ?  96  GLU   A CD  1 
ATOM   680  O OE1 . GLU   A 1 91  ? 11.012  10.205  24.637  1.00 99.05  ?  96  GLU   A OE1 1 
ATOM   681  O OE2 . GLU   A 1 91  ? 12.635  11.187  23.525  1.00 95.22  ?  96  GLU   A OE2 1 
ATOM   682  N N   . LYS   A 1 92  ? 10.510  6.411   20.525  1.00 69.20  ?  97  LYS   A N   1 
ATOM   683  C CA  . LYS   A 1 92  ? 11.494  5.454   19.965  1.00 68.99  ?  97  LYS   A CA  1 
ATOM   684  C C   . LYS   A 1 92  ? 11.190  4.925   18.554  1.00 69.30  ?  97  LYS   A C   1 
ATOM   685  O O   . LYS   A 1 92  ? 11.989  4.158   17.996  1.00 77.16  ?  97  LYS   A O   1 
ATOM   686  C CB  . LYS   A 1 92  ? 11.698  4.282   20.933  1.00 70.12  ?  97  LYS   A CB  1 
ATOM   687  C CG  . LYS   A 1 92  ? 12.327  4.717   22.237  1.00 72.26  ?  97  LYS   A CG  1 
ATOM   688  C CD  . LYS   A 1 92  ? 12.844  3.544   23.048  1.00 74.16  ?  97  LYS   A CD  1 
ATOM   689  C CE  . LYS   A 1 92  ? 13.713  4.027   24.192  1.00 81.16  ?  97  LYS   A CE  1 
ATOM   690  N NZ  . LYS   A 1 92  ? 15.068  4.438   23.743  1.00 85.46  ?  97  LYS   A NZ  1 
ATOM   691  N N   . GLY   A 1 93  ? 10.058  5.327   17.976  1.00 62.53  ?  98  GLY   A N   1 
ATOM   692  C CA  . GLY   A 1 93  ? 9.770   5.064   16.571  1.00 56.47  ?  98  GLY   A CA  1 
ATOM   693  C C   . GLY   A 1 93  ? 9.200   3.691   16.430  1.00 54.65  ?  98  GLY   A C   1 
ATOM   694  O O   . GLY   A 1 93  ? 8.636   3.160   17.401  1.00 57.16  ?  98  GLY   A O   1 
ATOM   695  N N   . ASN   A 1 94  ? 9.341   3.101   15.238  1.00 56.31  ?  99  ASN   A N   1 
ATOM   696  C CA  . ASN   A 1 94  ? 8.778   1.766   14.996  1.00 55.39  ?  99  ASN   A CA  1 
ATOM   697  C C   . ASN   A 1 94  ? 9.627   0.663   15.629  1.00 57.78  ?  99  ASN   A C   1 
ATOM   698  O O   . ASN   A 1 94  ? 10.773  0.913   16.045  1.00 57.84  ?  99  ASN   A O   1 
ATOM   699  C CB  . ASN   A 1 94  ? 8.455   1.530   13.513  1.00 58.14  ?  99  ASN   A CB  1 
ATOM   700  C CG  . ASN   A 1 94  ? 9.664   1.262   12.636  1.00 59.16  ?  99  ASN   A CG  1 
ATOM   701  O OD1 . ASN   A 1 94  ? 10.532  0.461   12.953  1.00 65.34  ?  99  ASN   A OD1 1 
ATOM   702  N ND2 . ASN   A 1 94  ? 9.668   1.871   11.461  1.00 64.89  ?  99  ASN   A ND2 1 
ATOM   703  N N   . LEU   A 1 95  ? 9.053   -0.543  15.682  1.00 53.28  ?  100 LEU   A N   1 
ATOM   704  C CA  . LEU   A 1 95  ? 9.674   -1.698  16.337  1.00 52.90  ?  100 LEU   A CA  1 
ATOM   705  C C   . LEU   A 1 95  ? 11.012  -2.089  15.708  1.00 59.92  ?  100 LEU   A C   1 
ATOM   706  O O   . LEU   A 1 95  ? 11.954  -2.383  16.437  1.00 65.34  ?  100 LEU   A O   1 
ATOM   707  C CB  . LEU   A 1 95  ? 8.727   -2.911  16.344  1.00 53.86  ?  100 LEU   A CB  1 
ATOM   708  C CG  . LEU   A 1 95  ? 9.231   -4.230  16.959  1.00 49.63  ?  100 LEU   A CG  1 
ATOM   709  C CD1 . LEU   A 1 95  ? 9.685   -4.035  18.397  1.00 50.04  ?  100 LEU   A CD1 1 
ATOM   710  C CD2 . LEU   A 1 95  ? 8.132   -5.268  16.893  1.00 50.65  ?  100 LEU   A CD2 1 
ATOM   711  N N   . MET   A 1 96  ? 11.097  -2.059  14.374  1.00 62.27  ?  101 MET   A N   1 
ATOM   712  C CA  . MET   A 1 96  ? 12.336  -2.406  13.666  1.00 63.00  ?  101 MET   A CA  1 
ATOM   713  C C   . MET   A 1 96  ? 13.490  -1.438  13.944  1.00 65.11  ?  101 MET   A C   1 
ATOM   714  O O   . MET   A 1 96  ? 14.629  -1.874  14.076  1.00 75.30  ?  101 MET   A O   1 
ATOM   715  C CB  . MET   A 1 96  ? 12.086  -2.517  12.160  1.00 66.98  ?  101 MET   A CB  1 
ATOM   716  C CG  . MET   A 1 96  ? 13.210  -3.162  11.365  1.00 78.39  ?  101 MET   A CG  1 
ATOM   717  S SD  . MET   A 1 96  ? 13.736  -4.797  11.926  1.00 85.14  ?  101 MET   A SD  1 
ATOM   718  C CE  . MET   A 1 96  ? 12.244  -5.757  11.695  1.00 81.00  ?  101 MET   A CE  1 
ATOM   719  N N   . HIS   A 1 97  ? 13.194  -0.144  14.037  1.00 62.58  ?  102 HIS   A N   1 
ATOM   720  C CA  . HIS   A 1 97  ? 14.171  0.870   14.483  1.00 66.96  ?  102 HIS   A CA  1 
ATOM   721  C C   . HIS   A 1 97  ? 14.746  0.543   15.864  1.00 69.18  ?  102 HIS   A C   1 
ATOM   722  O O   . HIS   A 1 97  ? 15.949  0.670   16.078  1.00 75.20  ?  102 HIS   A O   1 
ATOM   723  C CB  . HIS   A 1 97  ? 13.538  2.280   14.487  1.00 69.47  ?  102 HIS   A CB  1 
ATOM   724  C CG  . HIS   A 1 97  ? 14.503  3.389   14.798  1.00 74.41  ?  102 HIS   A CG  1 
ATOM   725  N ND1 . HIS   A 1 97  ? 14.555  4.005   16.033  1.00 79.86  ?  102 HIS   A ND1 1 
ATOM   726  C CD2 . HIS   A 1 97  ? 15.461  3.981   14.043  1.00 75.22  ?  102 HIS   A CD2 1 
ATOM   727  C CE1 . HIS   A 1 97  ? 15.500  4.928   16.026  1.00 80.20  ?  102 HIS   A CE1 1 
ATOM   728  N NE2 . HIS   A 1 97  ? 16.064  4.934   14.830  1.00 80.99  ?  102 HIS   A NE2 1 
ATOM   729  N N   . VAL   A 1 98  ? 13.880  0.104   16.774  1.00 69.59  ?  103 VAL   A N   1 
ATOM   730  C CA  . VAL   A 1 98  ? 14.278  -0.291  18.135  1.00 74.04  ?  103 VAL   A CA  1 
ATOM   731  C C   . VAL   A 1 98  ? 15.119  -1.584  18.134  1.00 76.61  ?  103 VAL   A C   1 
ATOM   732  O O   . VAL   A 1 98  ? 16.130  -1.661  18.842  1.00 75.17  ?  103 VAL   A O   1 
ATOM   733  C CB  . VAL   A 1 98  ? 13.038  -0.403  19.063  1.00 76.11  ?  103 VAL   A CB  1 
ATOM   734  C CG1 . VAL   A 1 98  ? 13.385  -0.974  20.438  1.00 72.56  ?  103 VAL   A CG1 1 
ATOM   735  C CG2 . VAL   A 1 98  ? 12.402  0.979   19.228  1.00 80.30  ?  103 VAL   A CG2 1 
ATOM   736  N N   . LEU   A 1 99  ? 14.706  -2.576  17.340  1.00 73.80  ?  104 LEU   A N   1 
ATOM   737  C CA  . LEU   A 1 99  ? 15.445  -3.843  17.196  1.00 75.92  ?  104 LEU   A CA  1 
ATOM   738  C C   . LEU   A 1 99  ? 16.820  -3.687  16.524  1.00 82.00  ?  104 LEU   A C   1 
ATOM   739  O O   . LEU   A 1 99  ? 17.779  -4.313  16.960  1.00 89.74  ?  104 LEU   A O   1 
ATOM   740  C CB  . LEU   A 1 99  ? 14.626  -4.860  16.409  1.00 70.05  ?  104 LEU   A CB  1 
ATOM   741  C CG  . LEU   A 1 99  ? 13.318  -5.326  17.039  1.00 65.62  ?  104 LEU   A CG  1 
ATOM   742  C CD1 . LEU   A 1 99  ? 12.523  -6.105  16.002  1.00 64.51  ?  104 LEU   A CD1 1 
ATOM   743  C CD2 . LEU   A 1 99  ? 13.539  -6.166  18.285  1.00 68.52  ?  104 LEU   A CD2 1 
ATOM   744  N N   . LYS   A 1 100 ? 16.899  -2.858  15.481  1.00 79.53  ?  105 LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 100 ? 18.173  -2.548  14.800  1.00 81.61  ?  105 LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 100 ? 19.089  -1.551  15.541  1.00 84.12  ?  105 LYS   A C   1 
ATOM   747  O O   . LYS   A 1 100 ? 20.218  -1.341  15.092  1.00 96.13  ?  105 LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 100 ? 17.934  -2.102  13.336  1.00 84.31  ?  105 LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 100 ? 17.671  -3.261  12.373  1.00 88.45  ?  105 LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 100 ? 17.489  -2.799  10.927  1.00 90.23  ?  105 LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 100 ? 17.328  -3.972  9.965   1.00 88.89  ?  105 LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 100 ? 16.997  -3.575  8.600   0.00 88.38  ?  105 LYS   A NZ  1 
ATOM   753  N N   . ALA   A 1 101 ? 18.637  -0.945  16.650  1.00 85.25  ?  106 ALA   A N   1 
ATOM   754  C CA  . ALA   A 1 101 ? 19.466  -0.020  17.455  1.00 94.09  ?  106 ALA   A CA  1 
ATOM   755  C C   . ALA   A 1 101 ? 20.666  -0.708  18.118  1.00 104.54 ?  106 ALA   A C   1 
ATOM   756  O O   . ALA   A 1 101 ? 20.619  -1.918  18.388  1.00 102.07 ?  106 ALA   A O   1 
ATOM   757  C CB  . ALA   A 1 101 ? 18.618  0.671   18.513  1.00 92.05  ?  106 ALA   A CB  1 
ATOM   758  N N   . GLU   A 1 102 ? 21.718  0.080   18.375  1.00 114.55 ?  107 GLU   A N   1 
ATOM   759  C CA  . GLU   A 1 102 ? 23.011  -0.414  18.906  1.00 125.33 ?  107 GLU   A CA  1 
ATOM   760  C C   . GLU   A 1 102 ? 22.901  -1.092  20.283  1.00 133.09 ?  107 GLU   A C   1 
ATOM   761  O O   . GLU   A 1 102 ? 23.578  -2.092  20.520  1.00 136.36 ?  107 GLU   A O   1 
ATOM   762  C CB  . GLU   A 1 102 ? 24.062  0.711   18.956  1.00 121.45 ?  107 GLU   A CB  1 
ATOM   763  C CG  . GLU   A 1 102 ? 24.489  1.358   17.666  0.00 126.56 ?  107 GLU   A CG  1 
ATOM   764  C CD  . GLU   A 1 102 ? 25.585  2.401   17.816  0.00 131.95 ?  107 GLU   A CD  1 
ATOM   765  O OE1 . GLU   A 1 102 ? 25.462  3.291   18.687  0.00 132.37 ?  107 GLU   A OE1 1 
ATOM   766  O OE2 . GLU   A 1 102 ? 26.570  2.338   17.053  0.00 135.83 ?  107 GLU   A OE2 1 
ATOM   767  N N   . MET   A 1 103 ? 22.043  -0.556  21.158  1.00 136.75 ?  108 MET   A N   1 
ATOM   768  C CA  . MET   A 1 103 ? 21.677  -1.225  22.418  1.00 133.59 ?  108 MET   A CA  1 
ATOM   769  C C   . MET   A 1 103 ? 20.676  -2.350  22.120  1.00 129.30 ?  108 MET   A C   1 
ATOM   770  O O   . MET   A 1 103 ? 19.581  -2.087  21.601  1.00 111.42 ?  108 MET   A O   1 
ATOM   771  C CB  . MET   A 1 103 ? 21.086  -0.234  23.422  1.00 131.16 ?  108 MET   A CB  1 
ATOM   772  C CG  . MET   A 1 103 ? 21.081  -0.742  24.855  1.00 130.14 ?  108 MET   A CG  1 
ATOM   773  S SD  . MET   A 1 103 ? 22.643  -0.766  25.688  0.00 148.01 ?  108 MET   A SD  1 
ATOM   774  C CE  . MET   A 1 103 ? 22.203  -1.595  27.215  0.00 147.29 ?  108 MET   A CE  1 
ATOM   775  N N   . SER   A 1 104 ? 21.055  -3.589  22.450  1.00 138.60 ?  109 SER   A N   1 
ATOM   776  C CA  . SER   A 1 104 ? 20.198  -4.775  22.260  1.00 130.13 ?  109 SER   A CA  1 
ATOM   777  C C   . SER   A 1 104 ? 19.115  -4.838  23.348  1.00 120.17 ?  109 SER   A C   1 
ATOM   778  O O   . SER   A 1 104 ? 19.431  -4.708  24.535  1.00 128.45 ?  109 SER   A O   1 
ATOM   779  C CB  . SER   A 1 104 ? 21.040  -6.059  22.291  1.00 125.41 ?  109 SER   A CB  1 
ATOM   780  O OG  . SER   A 1 104 ? 21.796  -6.158  23.468  0.00 129.57 ?  109 SER   A OG  1 
ATOM   781  N N   . THR   A 1 105 ? 17.860  -5.061  22.940  1.00 97.00  ?  110 THR   A N   1 
ATOM   782  C CA  . THR   A 1 105 ? 16.709  -5.093  23.854  1.00 87.80  ?  110 THR   A CA  1 
ATOM   783  C C   . THR   A 1 105 ? 16.656  -6.468  24.554  1.00 76.77  ?  110 THR   A C   1 
ATOM   784  O O   . THR   A 1 105 ? 16.643  -7.482  23.863  1.00 72.04  ?  110 THR   A O   1 
ATOM   785  C CB  . THR   A 1 105 ? 15.389  -4.843  23.079  1.00 80.40  ?  110 THR   A CB  1 
ATOM   786  O OG1 . THR   A 1 105 ? 15.541  -3.691  22.245  1.00 81.34  ?  110 THR   A OG1 1 
ATOM   787  C CG2 . THR   A 1 105 ? 14.219  -4.597  24.002  1.00 75.28  ?  110 THR   A CG2 1 
ATOM   788  N N   . PRO   A 1 106 ? 16.590  -6.510  25.910  1.00 75.75  ?  111 PRO   A N   1 
ATOM   789  C CA  . PRO   A 1 106 ? 16.571  -7.819  26.605  1.00 73.73  ?  111 PRO   A CA  1 
ATOM   790  C C   . PRO   A 1 106 ? 15.291  -8.644  26.394  1.00 66.95  ?  111 PRO   A C   1 
ATOM   791  O O   . PRO   A 1 106 ? 14.244  -8.102  26.014  1.00 72.47  ?  111 PRO   A O   1 
ATOM   792  C CB  . PRO   A 1 106 ? 16.738  -7.439  28.083  1.00 71.47  ?  111 PRO   A CB  1 
ATOM   793  C CG  . PRO   A 1 106 ? 16.196  -6.070  28.185  1.00 70.92  ?  111 PRO   A CG  1 
ATOM   794  C CD  . PRO   A 1 106 ? 16.485  -5.394  26.873  1.00 73.59  ?  111 PRO   A CD  1 
ATOM   795  N N   . LEU   A 1 107 ? 15.407  -9.944  26.648  1.00 66.36  ?  112 LEU   A N   1 
ATOM   796  C CA  . LEU   A 1 107 ? 14.314  -10.914 26.495  1.00 65.14  ?  112 LEU   A CA  1 
ATOM   797  C C   . LEU   A 1 107 ? 13.040  -10.554 27.259  1.00 63.99  ?  112 LEU   A C   1 
ATOM   798  O O   . LEU   A 1 107 ? 11.945  -10.755 26.739  1.00 63.80  ?  112 LEU   A O   1 
ATOM   799  C CB  . LEU   A 1 107 ? 14.787  -12.317 26.922  1.00 65.77  ?  112 LEU   A CB  1 
ATOM   800  C CG  . LEU   A 1 107 ? 13.804  -13.498 26.903  1.00 66.07  ?  112 LEU   A CG  1 
ATOM   801  C CD1 . LEU   A 1 107 ? 13.099  -13.648 25.565  1.00 63.57  ?  112 LEU   A CD1 1 
ATOM   802  C CD2 . LEU   A 1 107 ? 14.550  -14.783 27.241  1.00 71.68  ?  112 LEU   A CD2 1 
ATOM   803  N N   . SER   A 1 108 ? 13.199  -10.023 28.476  1.00 70.45  ?  113 SER   A N   1 
ATOM   804  C CA  . SER   A 1 108 ? 12.061  -9.614  29.317  1.00 69.37  ?  113 SER   A CA  1 
ATOM   805  C C   . SER   A 1 108 ? 11.226  -8.509  28.680  1.00 65.86  ?  113 SER   A C   1 
ATOM   806  O O   . SER   A 1 108 ? 9.993   -8.580  28.717  1.00 70.29  ?  113 SER   A O   1 
ATOM   807  C CB  . SER   A 1 108 ? 12.524  -9.196  30.712  1.00 72.55  ?  113 SER   A CB  1 
ATOM   808  O OG  . SER   A 1 108 ? 13.460  -8.139  30.636  1.00 82.33  ?  113 SER   A OG  1 
ATOM   809  N N   . VAL   A 1 109 ? 11.899  -7.526  28.077  1.00 62.65  ?  114 VAL   A N   1 
ATOM   810  C CA  . VAL   A 1 109 ? 11.216  -6.465  27.322  1.00 64.09  ?  114 VAL   A CA  1 
ATOM   811  C C   . VAL   A 1 109 ? 10.574  -7.029  26.040  1.00 63.65  ?  114 VAL   A C   1 
ATOM   812  O O   . VAL   A 1 109 ? 9.421   -6.704  25.755  1.00 70.18  ?  114 VAL   A O   1 
ATOM   813  C CB  . VAL   A 1 109 ? 12.141  -5.271  27.002  1.00 68.52  ?  114 VAL   A CB  1 
ATOM   814  C CG1 . VAL   A 1 109 ? 11.423  -4.227  26.140  1.00 66.58  ?  114 VAL   A CG1 1 
ATOM   815  C CG2 . VAL   A 1 109 ? 12.641  -4.610  28.287  1.00 69.97  ?  114 VAL   A CG2 1 
ATOM   816  N N   . LYS   A 1 110 ? 11.304  -7.862  25.298  1.00 61.67  ?  115 LYS   A N   1 
ATOM   817  C CA  . LYS   A 1 110 ? 10.748  -8.528  24.095  1.00 60.57  ?  115 LYS   A CA  1 
ATOM   818  C C   . LYS   A 1 110 ? 9.505   -9.383  24.374  1.00 58.41  ?  115 LYS   A C   1 
ATOM   819  O O   . LYS   A 1 110 ? 8.577   -9.412  23.561  1.00 58.61  ?  115 LYS   A O   1 
ATOM   820  C CB  . LYS   A 1 110 ? 11.809  -9.380  23.391  1.00 61.40  ?  115 LYS   A CB  1 
ATOM   821  C CG  . LYS   A 1 110 ? 12.841  -8.541  22.674  1.00 62.84  ?  115 LYS   A CG  1 
ATOM   822  C CD  . LYS   A 1 110 ? 13.898  -9.388  21.990  1.00 64.32  ?  115 LYS   A CD  1 
ATOM   823  C CE  . LYS   A 1 110 ? 14.788  -8.506  21.145  1.00 67.24  ?  115 LYS   A CE  1 
ATOM   824  N NZ  . LYS   A 1 110 ? 15.846  -9.268  20.449  1.00 73.43  ?  115 LYS   A NZ  1 
ATOM   825  N N   . GLY   A 1 111 ? 9.511   -10.094 25.501  1.00 57.96  ?  116 GLY   A N   1 
ATOM   826  C CA  . GLY   A 1 111 ? 8.337   -10.834 25.998  1.00 54.40  ?  116 GLY   A CA  1 
ATOM   827  C C   . GLY   A 1 111 ? 7.135   -9.937  26.238  1.00 53.91  ?  116 GLY   A C   1 
ATOM   828  O O   . GLY   A 1 111 ? 6.012   -10.244 25.821  1.00 49.91  ?  116 GLY   A O   1 
ATOM   829  N N   . ARG   A 1 112 ? 7.379   -8.809  26.895  1.00 59.01  ?  117 ARG   A N   1 
ATOM   830  C CA  . ARG   A 1 112 ? 6.329   -7.813  27.154  1.00 57.19  ?  117 ARG   A CA  1 
ATOM   831  C C   . ARG   A 1 112 ? 5.794   -7.193  25.866  1.00 53.22  ?  117 ARG   A C   1 
ATOM   832  O O   . ARG   A 1 112 ? 4.576   -7.017  25.737  1.00 52.02  ?  117 ARG   A O   1 
ATOM   833  C CB  . ARG   A 1 112 ? 6.840   -6.726  28.089  1.00 59.24  ?  117 ARG   A CB  1 
ATOM   834  C CG  . ARG   A 1 112 ? 5.740   -5.933  28.772  1.00 59.71  ?  117 ARG   A CG  1 
ATOM   835  C CD  . ARG   A 1 112 ? 6.322   -4.813  29.611  1.00 64.60  ?  117 ARG   A CD  1 
ATOM   836  N NE  . ARG   A 1 112 ? 7.116   -3.882  28.813  1.00 63.35  ?  117 ARG   A NE  1 
ATOM   837  C CZ  . ARG   A 1 112 ? 7.894   -2.915  29.293  1.00 65.25  ?  117 ARG   A CZ  1 
ATOM   838  N NH1 . ARG   A 1 112 ? 8.011   -2.689  30.605  1.00 75.93  ?  117 ARG   A NH1 1 
ATOM   839  N NH2 . ARG   A 1 112 ? 8.567   -2.148  28.438  1.00 68.73  ?  117 ARG   A NH2 1 
ATOM   840  N N   . ILE   A 1 113 ? 6.701   -6.887  24.928  1.00 47.98  ?  118 ILE   A N   1 
ATOM   841  C CA  . ILE   A 1 113 ? 6.335   -6.392  23.592  1.00 44.47  ?  118 ILE   A CA  1 
ATOM   842  C C   . ILE   A 1 113 ? 5.362   -7.345  22.896  1.00 45.15  ?  118 ILE   A C   1 
ATOM   843  O O   . ILE   A 1 113 ? 4.324   -6.917  22.416  1.00 49.93  ?  118 ILE   A O   1 
ATOM   844  C CB  . ILE   A 1 113 ? 7.587   -6.122  22.713  1.00 46.81  ?  118 ILE   A CB  1 
ATOM   845  C CG1 . ILE   A 1 113 ? 8.308   -4.861  23.234  1.00 48.09  ?  118 ILE   A CG1 1 
ATOM   846  C CG2 . ILE   A 1 113 ? 7.224   -5.956  21.225  1.00 47.95  ?  118 ILE   A CG2 1 
ATOM   847  C CD1 . ILE   A 1 113 ? 9.669   -4.548  22.638  1.00 52.93  ?  118 ILE   A CD1 1 
ATOM   848  N N   . ILE   A 1 114 ? 5.717   -8.622  22.862  1.00 47.35  ?  119 ILE   A N   1 
ATOM   849  C CA  . ILE   A 1 114 ? 4.894   -9.681  22.246  1.00 45.97  ?  119 ILE   A CA  1 
ATOM   850  C C   . ILE   A 1 114 ? 3.519   -9.748  22.900  1.00 46.01  ?  119 ILE   A C   1 
ATOM   851  O O   . ILE   A 1 114 ? 2.505   -9.802  22.205  1.00 51.71  ?  119 ILE   A O   1 
ATOM   852  C CB  . ILE   A 1 114 ? 5.605   -11.059 22.314  1.00 49.33  ?  119 ILE   A CB  1 
ATOM   853  C CG1 . ILE   A 1 114 ? 6.811   -11.054 21.362  1.00 50.31  ?  119 ILE   A CG1 1 
ATOM   854  C CG2 . ILE   A 1 114 ? 4.673   -12.216 21.931  1.00 54.43  ?  119 ILE   A CG2 1 
ATOM   855  C CD1 . ILE   A 1 114 ? 7.877   -12.078 21.687  1.00 53.87  ?  119 ILE   A CD1 1 
ATOM   856  N N   . LEU   A 1 115 ? 3.501   -9.749  24.227  1.00 45.13  ?  120 LEU   A N   1 
ATOM   857  C CA  . LEU   A 1 115 ? 2.251   -9.743  24.984  1.00 46.02  ?  120 LEU   A CA  1 
ATOM   858  C C   . LEU   A 1 115 ? 1.420   -8.507  24.671  1.00 48.76  ?  120 LEU   A C   1 
ATOM   859  O O   . LEU   A 1 115 ? 0.221   -8.618  24.450  1.00 48.53  ?  120 LEU   A O   1 
ATOM   860  C CB  . LEU   A 1 115 ? 2.523   -9.834  26.487  1.00 47.02  ?  120 LEU   A CB  1 
ATOM   861  C CG  . LEU   A 1 115 ? 1.347   -9.900  27.462  1.00 46.94  ?  120 LEU   A CG  1 
ATOM   862  C CD1 . LEU   A 1 115 ? 0.341   -10.987 27.119  1.00 50.17  ?  120 LEU   A CD1 1 
ATOM   863  C CD2 . LEU   A 1 115 ? 1.880   -10.134 28.856  1.00 49.50  ?  120 LEU   A CD2 1 
ATOM   864  N N   . GLU   A 1 116 ? 2.064   -7.345  24.627  1.00 52.20  ?  121 GLU   A N   1 
ATOM   865  C CA  . GLU   A 1 116 ? 1.368   -6.101  24.273  1.00 51.77  ?  121 GLU   A CA  1 
ATOM   866  C C   . GLU   A 1 116 ? 0.830   -6.090  22.843  1.00 52.31  ?  121 GLU   A C   1 
ATOM   867  O O   . GLU   A 1 116 ? -0.275  -5.587  22.621  1.00 61.65  ?  121 GLU   A O   1 
ATOM   868  C CB  . GLU   A 1 116 ? 2.253   -4.895  24.524  1.00 54.74  ?  121 GLU   A CB  1 
ATOM   869  C CG  . GLU   A 1 116 ? 2.360   -4.557  26.002  1.00 57.64  ?  121 GLU   A CG  1 
ATOM   870  C CD  . GLU   A 1 116 ? 3.267   -3.382  26.304  1.00 63.49  ?  121 GLU   A CD  1 
ATOM   871  O OE1 . GLU   A 1 116 ? 3.991   -2.896  25.404  1.00 61.76  ?  121 GLU   A OE1 1 
ATOM   872  O OE2 . GLU   A 1 116 ? 3.260   -2.953  27.477  1.00 69.03  ?  121 GLU   A OE2 1 
ATOM   873  N N   . ILE   A 1 117 ? 1.590   -6.647  21.889  1.00 49.30  ?  122 ILE   A N   1 
ATOM   874  C CA  . ILE   A 1 117 ? 1.108   -6.845  20.504  1.00 42.33  ?  122 ILE   A CA  1 
ATOM   875  C C   . ILE   A 1 117 ? -0.142  -7.734  20.484  1.00 44.23  ?  122 ILE   A C   1 
ATOM   876  O O   . ILE   A 1 117 ? -1.097  -7.415  19.791  1.00 49.27  ?  122 ILE   A O   1 
ATOM   877  C CB  . ILE   A 1 117 ? 2.205   -7.420  19.564  1.00 42.19  ?  122 ILE   A CB  1 
ATOM   878  C CG1 . ILE   A 1 117 ? 3.299   -6.365  19.311  1.00 44.64  ?  122 ILE   A CG1 1 
ATOM   879  C CG2 . ILE   A 1 117 ? 1.637   -7.843  18.200  1.00 44.80  ?  122 ILE   A CG2 1 
ATOM   880  C CD1 . ILE   A 1 117 ? 4.608   -6.886  18.723  1.00 44.54  ?  122 ILE   A CD1 1 
ATOM   881  N N   . ILE   A 1 118 ? -0.122  -8.829  21.244  1.00 44.83  ?  123 ILE   A N   1 
ATOM   882  C CA  . ILE   A 1 118 ? -1.263  -9.756  21.353  1.00 45.79  ?  123 ILE   A CA  1 
ATOM   883  C C   . ILE   A 1 118 ? -2.494  -9.037  21.918  1.00 46.28  ?  123 ILE   A C   1 
ATOM   884  O O   . ILE   A 1 118 ? -3.571  -9.142  21.346  1.00 50.47  ?  123 ILE   A O   1 
ATOM   885  C CB  . ILE   A 1 118 ? -0.901  -11.005 22.214  1.00 48.71  ?  123 ILE   A CB  1 
ATOM   886  C CG1 . ILE   A 1 118 ? 0.112   -11.896 21.474  1.00 50.14  ?  123 ILE   A CG1 1 
ATOM   887  C CG2 . ILE   A 1 118 ? -2.133  -11.834 22.598  1.00 50.55  ?  123 ILE   A CG2 1 
ATOM   888  C CD1 . ILE   A 1 118 ? 0.980   -12.717 22.402  1.00 51.62  ?  123 ILE   A CD1 1 
ATOM   889  N N   . GLU   A 1 119 ? -2.315  -8.347  23.046  1.00 48.82  ?  124 GLU   A N   1 
ATOM   890  C CA  . GLU   A 1 119 ? -3.370  -7.539  23.700  1.00 55.14  ?  124 GLU   A CA  1 
ATOM   891  C C   . GLU   A 1 119 ? -4.035  -6.578  22.709  1.00 56.49  ?  124 GLU   A C   1 
ATOM   892  O O   . GLU   A 1 119 ? -5.274  -6.562  22.571  1.00 53.22  ?  124 GLU   A O   1 
ATOM   893  C CB  . GLU   A 1 119 ? -2.805  -6.725  24.885  1.00 57.63  ?  124 GLU   A CB  1 
ATOM   894  C CG  . GLU   A 1 119 ? -2.541  -7.514  26.171  1.00 59.27  ?  124 GLU   A CG  1 
ATOM   895  C CD  . GLU   A 1 119 ? -1.844  -6.713  27.284  1.00 66.83  ?  124 GLU   A CD  1 
ATOM   896  O OE1 . GLU   A 1 119 ? -1.492  -5.520  27.113  1.00 65.61  ?  124 GLU   A OE1 1 
ATOM   897  O OE2 . GLU   A 1 119 ? -1.644  -7.299  28.370  1.00 76.53  ?  124 GLU   A OE2 1 
ATOM   898  N N   . GLY   A 1 120 ? -3.188  -5.819  22.006  1.00 53.74  ?  125 GLY   A N   1 
ATOM   899  C CA  . GLY   A 1 120 ? -3.630  -4.851  21.011  1.00 53.21  ?  125 GLY   A CA  1 
ATOM   900  C C   . GLY   A 1 120 ? -4.387  -5.460  19.846  1.00 52.27  ?  125 GLY   A C   1 
ATOM   901  O O   . GLY   A 1 120 ? -5.471  -4.985  19.485  1.00 59.39  ?  125 GLY   A O   1 
ATOM   902  N N   . MET   A 1 121 ? -3.823  -6.520  19.278  1.00 48.39  ?  126 MET   A N   1 
ATOM   903  C CA  . MET   A 1 121 ? -4.493  -7.280  18.211  1.00 50.48  ?  126 MET   A CA  1 
ATOM   904  C C   . MET   A 1 121 ? -5.774  -7.975  18.643  1.00 47.19  ?  126 MET   A C   1 
ATOM   905  O O   . MET   A 1 121 ? -6.733  -8.065  17.857  1.00 53.61  ?  126 MET   A O   1 
ATOM   906  C CB  . MET   A 1 121 ? -3.541  -8.305  17.585  1.00 56.06  ?  126 MET   A CB  1 
ATOM   907  C CG  . MET   A 1 121 ? -2.431  -7.702  16.729  1.00 55.35  ?  126 MET   A CG  1 
ATOM   908  S SD  . MET   A 1 121 ? -2.982  -6.619  15.414  1.00 54.49  ?  126 MET   A SD  1 
ATOM   909  C CE  . MET   A 1 121 ? -4.233  -7.623  14.597  1.00 58.85  ?  126 MET   A CE  1 
ATOM   910  N N   . ALA   A 1 122 ? -5.790  -8.474  19.872  1.00 48.76  ?  127 ALA   A N   1 
ATOM   911  C CA  . ALA   A 1 122 ? -7.001  -9.064  20.450  1.00 52.85  ?  127 ALA   A CA  1 
ATOM   912  C C   . ALA   A 1 122 ? -8.127  -8.032  20.591  1.00 51.38  ?  127 ALA   A C   1 
ATOM   913  O O   . ALA   A 1 122 ? -9.284  -8.347  20.315  1.00 51.13  ?  127 ALA   A O   1 
ATOM   914  C CB  . ALA   A 1 122 ? -6.698  -9.709  21.788  1.00 55.86  ?  127 ALA   A CB  1 
ATOM   915  N N   . TYR   A 1 123 ? -7.776  -6.805  20.988  1.00 51.34  ?  128 TYR   A N   1 
ATOM   916  C CA  . TYR   A 1 123 ? -8.745  -5.702  21.053  1.00 50.86  ?  128 TYR   A CA  1 
ATOM   917  C C   . TYR   A 1 123 ? -9.368  -5.400  19.685  1.00 54.41  ?  128 TYR   A C   1 
ATOM   918  O O   . TYR   A 1 123 ? -10.600 -5.316  19.576  1.00 57.93  ?  128 TYR   A O   1 
ATOM   919  C CB  . TYR   A 1 123 ? -8.118  -4.439  21.660  1.00 48.07  ?  128 TYR   A CB  1 
ATOM   920  C CG  . TYR   A 1 123 ? -8.993  -3.207  21.544  1.00 51.76  ?  128 TYR   A CG  1 
ATOM   921  C CD1 . TYR   A 1 123 ? -10.032 -2.982  22.450  1.00 50.80  ?  128 TYR   A CD1 1 
ATOM   922  C CD2 . TYR   A 1 123 ? -8.808  -2.275  20.497  1.00 49.89  ?  128 TYR   A CD2 1 
ATOM   923  C CE1 . TYR   A 1 123 ? -10.853 -1.858  22.345  1.00 53.69  ?  128 TYR   A CE1 1 
ATOM   924  C CE2 . TYR   A 1 123 ? -9.625  -1.147  20.386  1.00 51.77  ?  128 TYR   A CE2 1 
ATOM   925  C CZ  . TYR   A 1 123 ? -10.647 -0.948  21.313  1.00 53.01  ?  128 TYR   A CZ  1 
ATOM   926  O OH  . TYR   A 1 123 ? -11.463 0.142   21.238  1.00 54.96  ?  128 TYR   A OH  1 
ATOM   927  N N   . LEU   A 1 124 ? -8.514  -5.243  18.668  1.00 53.41  ?  129 LEU   A N   1 
ATOM   928  C CA  . LEU   A 1 124 ? -8.952  -4.886  17.304  1.00 50.47  ?  129 LEU   A CA  1 
ATOM   929  C C   . LEU   A 1 124 ? -9.856  -5.932  16.670  1.00 51.57  ?  129 LEU   A C   1 
ATOM   930  O O   . LEU   A 1 124 ? -10.917 -5.591  16.112  1.00 60.99  ?  129 LEU   A O   1 
ATOM   931  C CB  . LEU   A 1 124 ? -7.756  -4.603  16.392  1.00 48.46  ?  129 LEU   A CB  1 
ATOM   932  C CG  . LEU   A 1 124 ? -6.876  -3.378  16.702  1.00 46.97  ?  129 LEU   A CG  1 
ATOM   933  C CD1 . LEU   A 1 124 ? -5.658  -3.396  15.798  1.00 45.11  ?  129 LEU   A CD1 1 
ATOM   934  C CD2 . LEU   A 1 124 ? -7.611  -2.050  16.552  1.00 45.63  ?  129 LEU   A CD2 1 
ATOM   935  N N   . HIS   A 1 125 ? -9.469  -7.199  16.795  1.00 56.35  ?  130 HIS   A N   1 
ATOM   936  C CA  . HIS   A 1 125 ? -10.326 -8.327  16.347  1.00 56.37  ?  130 HIS   A CA  1 
ATOM   937  C C   . HIS   A 1 125 ? -11.672 -8.369  17.059  1.00 53.63  ?  130 HIS   A C   1 
ATOM   938  O O   . HIS   A 1 125 ? -12.697 -8.545  16.410  1.00 58.97  ?  130 HIS   A O   1 
ATOM   939  C CB  . HIS   A 1 125 ? -9.589  -9.658  16.489  1.00 56.04  ?  130 HIS   A CB  1 
ATOM   940  C CG  . HIS   A 1 125 ? -8.475  -9.831  15.503  1.00 58.93  ?  130 HIS   A CG  1 
ATOM   941  N ND1 . HIS   A 1 125 ? -7.793  -11.017 15.354  1.00 63.73  ?  130 HIS   A ND1 1 
ATOM   942  C CD2 . HIS   A 1 125 ? -7.941  -8.976  14.599  1.00 59.94  ?  130 HIS   A CD2 1 
ATOM   943  C CE1 . HIS   A 1 125 ? -6.871  -10.875 14.420  1.00 60.52  ?  130 HIS   A CE1 1 
ATOM   944  N NE2 . HIS   A 1 125 ? -6.942  -9.647  13.947  1.00 58.65  ?  130 HIS   A NE2 1 
ATOM   945  N N   . GLY   A 1 126 ? -11.654 -8.150  18.373  1.00 52.03  ?  131 GLY   A N   1 
ATOM   946  C CA  . GLY   A 1 126 ? -12.866 -7.935  19.178  1.00 54.90  ?  131 GLY   A CA  1 
ATOM   947  C C   . GLY   A 1 126 ? -13.794 -6.810  18.738  1.00 59.90  ?  131 GLY   A C   1 
ATOM   948  O O   . GLY   A 1 126 ? -15.021 -6.901  18.917  1.00 63.00  ?  131 GLY   A O   1 
ATOM   949  N N   . LYS   A 1 127 ? -13.206 -5.760  18.154  1.00 58.97  ?  132 LYS   A N   1 
ATOM   950  C CA  . LYS   A 1 127 ? -13.937 -4.642  17.533  1.00 60.20  ?  132 LYS   A CA  1 
ATOM   951  C C   . LYS   A 1 127 ? -14.262 -4.825  16.023  1.00 65.92  ?  132 LYS   A C   1 
ATOM   952  O O   . LYS   A 1 127 ? -14.689 -3.872  15.359  1.00 74.32  ?  132 LYS   A O   1 
ATOM   953  C CB  . LYS   A 1 127 ? -13.148 -3.336  17.780  1.00 58.38  ?  132 LYS   A CB  1 
ATOM   954  C CG  . LYS   A 1 127 ? -13.141 -2.885  19.241  1.00 60.19  ?  132 LYS   A CG  1 
ATOM   955  C CD  . LYS   A 1 127 ? -14.450 -2.204  19.651  1.00 65.78  ?  132 LYS   A CD  1 
ATOM   956  C CE  . LYS   A 1 127 ? -14.487 -1.883  21.135  1.00 68.60  ?  132 LYS   A CE  1 
ATOM   957  N NZ  . LYS   A 1 127 ? -15.786 -1.322  21.567  0.00 66.69  ?  132 LYS   A NZ  1 
ATOM   958  N N   . GLY   A 1 128 ? -14.106 -6.041  15.492  1.00 66.71  ?  133 GLY   A N   1 
ATOM   959  C CA  . GLY   A 1 128 ? -14.395 -6.337  14.083  1.00 66.06  ?  133 GLY   A CA  1 
ATOM   960  C C   . GLY   A 1 128 ? -13.405 -5.788  13.063  1.00 63.64  ?  133 GLY   A C   1 
ATOM   961  O O   . GLY   A 1 128 ? -13.743 -5.696  11.870  1.00 62.74  ?  133 GLY   A O   1 
ATOM   962  N N   . VAL   A 1 129 ? -12.189 -5.460  13.515  1.00 57.45  ?  134 VAL   A N   1 
ATOM   963  C CA  . VAL   A 1 129 ? -11.186 -4.781  12.705  1.00 54.82  ?  134 VAL   A CA  1 
ATOM   964  C C   . VAL   A 1 129 ? -10.100 -5.794  12.405  1.00 56.31  ?  134 VAL   A C   1 
ATOM   965  O O   . VAL   A 1 129 ? -9.385  -6.237  13.302  1.00 53.69  ?  134 VAL   A O   1 
ATOM   966  C CB  . VAL   A 1 129 ? -10.578 -3.562  13.439  1.00 54.03  ?  134 VAL   A CB  1 
ATOM   967  C CG1 . VAL   A 1 129 ? -9.477  -2.904  12.606  1.00 53.41  ?  134 VAL   A CG1 1 
ATOM   968  C CG2 . VAL   A 1 129 ? -11.666 -2.542  13.767  1.00 56.37  ?  134 VAL   A CG2 1 
ATOM   969  N N   . ILE   A 1 130 ? -9.987  -6.151  11.134  1.00 58.70  ?  135 ILE   A N   1 
ATOM   970  C CA  . ILE   A 1 130 ? -8.838  -6.888  10.626  1.00 51.62  ?  135 ILE   A CA  1 
ATOM   971  C C   . ILE   A 1 130 ? -7.831  -5.835  10.183  1.00 47.64  ?  135 ILE   A C   1 
ATOM   972  O O   . ILE   A 1 130 ? -8.176  -4.917  9.438   1.00 53.60  ?  135 ILE   A O   1 
ATOM   973  C CB  . ILE   A 1 130 ? -9.243  -7.855  9.504   1.00 51.43  ?  135 ILE   A CB  1 
ATOM   974  C CG1 . ILE   A 1 130 ? -10.216 -8.907  10.072  1.00 53.37  ?  135 ILE   A CG1 1 
ATOM   975  C CG2 . ILE   A 1 130 ? -8.019  -8.569  8.940   1.00 52.55  ?  135 ILE   A CG2 1 
ATOM   976  C CD1 . ILE   A 1 130 ? -11.048 -9.611  9.038   1.00 61.79  ?  135 ILE   A CD1 1 
ATOM   977  N N   . HIS   A 1 131 ? -6.596  -5.972  10.652  1.00 46.90  ?  136 HIS   A N   1 
ATOM   978  C CA  . HIS   A 1 131 ? -5.513  -5.052  10.308  1.00 49.04  ?  136 HIS   A CA  1 
ATOM   979  C C   . HIS   A 1 131 ? -5.146  -5.111  8.836   1.00 52.03  ?  136 HIS   A C   1 
ATOM   980  O O   . HIS   A 1 131 ? -5.041  -4.073  8.192   1.00 61.03  ?  136 HIS   A O   1 
ATOM   981  C CB  . HIS   A 1 131 ? -4.265  -5.308  11.160  1.00 44.85  ?  136 HIS   A CB  1 
ATOM   982  C CG  . HIS   A 1 131 ? -3.352  -4.127  11.267  1.00 47.47  ?  136 HIS   A CG  1 
ATOM   983  N ND1 . HIS   A 1 131 ? -2.756  -3.516  10.179  1.00 52.73  ?  136 HIS   A ND1 1 
ATOM   984  C CD2 . HIS   A 1 131 ? -2.926  -3.445  12.351  1.00 48.22  ?  136 HIS   A CD2 1 
ATOM   985  C CE1 . HIS   A 1 131 ? -2.012  -2.510  10.590  1.00 50.05  ?  136 HIS   A CE1 1 
ATOM   986  N NE2 . HIS   A 1 131 ? -2.099  -2.444  11.903  1.00 51.05  ?  136 HIS   A NE2 1 
ATOM   987  N N   . LYS   A 1 132 ? -4.914  -6.325  8.337   1.00 59.32  ?  137 LYS   A N   1 
ATOM   988  C CA  . LYS   A 1 132 ? -4.521  -6.612  6.933   1.00 63.58  ?  137 LYS   A CA  1 
ATOM   989  C C   . LYS   A 1 132 ? -3.046  -6.299  6.574   1.00 58.37  ?  137 LYS   A C   1 
ATOM   990  O O   . LYS   A 1 132 ? -2.584  -6.736  5.521   1.00 60.54  ?  137 LYS   A O   1 
ATOM   991  C CB  . LYS   A 1 132 ? -5.469  -5.957  5.896   1.00 63.57  ?  137 LYS   A CB  1 
ATOM   992  C CG  . LYS   A 1 132 ? -6.969  -6.112  6.159   1.00 65.20  ?  137 LYS   A CG  1 
ATOM   993  C CD  . LYS   A 1 132 ? -7.799  -5.117  5.351   1.00 76.40  ?  137 LYS   A CD  1 
ATOM   994  C CE  . LYS   A 1 132 ? -9.233  -5.020  5.859   1.00 84.43  ?  137 LYS   A CE  1 
ATOM   995  N NZ  . LYS   A 1 132 ? -9.351  -4.167  7.077   1.00 87.48  ?  137 LYS   A NZ  1 
ATOM   996  N N   . ASP   A 1 133 ? -2.311  -5.629  7.469   1.00 53.24  ?  138 ASP   A N   1 
ATOM   997  C CA  . ASP   A 1 133 ? -0.979  -5.055  7.188   1.00 56.38  ?  138 ASP   A CA  1 
ATOM   998  C C   . ASP   A 1 133 ? -0.160  -4.834  8.481   1.00 54.94  ?  138 ASP   A C   1 
ATOM   999  O O   . ASP   A 1 133 ? 0.464   -3.796  8.693   1.00 57.17  ?  138 ASP   A O   1 
ATOM   1000 C CB  . ASP   A 1 133 ? -1.101  -3.760  6.366   1.00 63.06  ?  138 ASP   A CB  1 
ATOM   1001 C CG  . ASP   A 1 133 ? 0.221   -3.332  5.693   1.00 75.42  ?  138 ASP   A CG  1 
ATOM   1002 O OD1 . ASP   A 1 133 ? 1.101   -4.178  5.392   1.00 77.99  ?  138 ASP   A OD1 1 
ATOM   1003 O OD2 . ASP   A 1 133 ? 0.366   -2.114  5.444   1.00 91.24  ?  138 ASP   A OD2 1 
ATOM   1004 N N   . LEU   A 1 134 ? -0.154  -5.864  9.325   1.00 55.74  ?  139 LEU   A N   1 
ATOM   1005 C CA  . LEU   A 1 134 ? 0.602   -5.882  10.563  1.00 57.27  ?  139 LEU   A CA  1 
ATOM   1006 C C   . LEU   A 1 134 ? 2.060   -6.177  10.201  1.00 57.86  ?  139 LEU   A C   1 
ATOM   1007 O O   . LEU   A 1 134 ? 2.345   -7.137  9.498   1.00 52.91  ?  139 LEU   A O   1 
ATOM   1008 C CB  . LEU   A 1 134 ? 0.054   -6.952  11.525  1.00 60.33  ?  139 LEU   A CB  1 
ATOM   1009 C CG  . LEU   A 1 134 ? 0.815   -7.287  12.817  1.00 60.88  ?  139 LEU   A CG  1 
ATOM   1010 C CD1 . LEU   A 1 134 ? 0.910   -6.064  13.720  1.00 58.22  ?  139 LEU   A CD1 1 
ATOM   1011 C CD2 . LEU   A 1 134 ? 0.148   -8.453  13.541  1.00 55.90  ?  139 LEU   A CD2 1 
ATOM   1012 N N   . LYS   A 1 135 ? 2.961   -5.341  10.699  1.00 57.77  ?  140 LYS   A N   1 
ATOM   1013 C CA  . LYS   A 1 135 ? 4.401   -5.448  10.456  1.00 58.17  ?  140 LYS   A CA  1 
ATOM   1014 C C   . LYS   A 1 135 ? 5.131   -4.527  11.456  1.00 59.48  ?  140 LYS   A C   1 
ATOM   1015 O O   . LYS   A 1 135 ? 4.472   -3.708  12.106  1.00 64.38  ?  140 LYS   A O   1 
ATOM   1016 C CB  . LYS   A 1 135 ? 4.730   -5.055  9.012   1.00 64.73  ?  140 LYS   A CB  1 
ATOM   1017 C CG  . LYS   A 1 135 ? 4.112   -3.731  8.570   1.00 73.90  ?  140 LYS   A CG  1 
ATOM   1018 C CD  . LYS   A 1 135 ? 4.355   -3.439  7.106   1.00 77.73  ?  140 LYS   A CD  1 
ATOM   1019 C CE  . LYS   A 1 135 ? 3.629   -2.182  6.662   1.00 77.86  ?  140 LYS   A CE  1 
ATOM   1020 N NZ  . LYS   A 1 135 ? 3.662   -2.054  5.182   1.00 84.54  ?  140 LYS   A NZ  1 
ATOM   1021 N N   . PRO   A 1 136 ? 6.466   -4.660  11.599  1.00 60.97  ?  141 PRO   A N   1 
ATOM   1022 C CA  . PRO   A 1 136 ? 7.181   -3.799  12.570  1.00 61.41  ?  141 PRO   A CA  1 
ATOM   1023 C C   . PRO   A 1 136 ? 7.050   -2.286  12.348  1.00 60.89  ?  141 PRO   A C   1 
ATOM   1024 O O   . PRO   A 1 136 ? 6.990   -1.543  13.324  1.00 67.42  ?  141 PRO   A O   1 
ATOM   1025 C CB  . PRO   A 1 136 ? 8.638   -4.254  12.436  1.00 61.41  ?  141 PRO   A CB  1 
ATOM   1026 C CG  . PRO   A 1 136 ? 8.535   -5.668  11.989  1.00 59.87  ?  141 PRO   A CG  1 
ATOM   1027 C CD  . PRO   A 1 136 ? 7.348   -5.718  11.075  1.00 57.20  ?  141 PRO   A CD  1 
ATOM   1028 N N   . GLU   A 1 137 ? 7.001   -1.845  11.088  1.00 62.66  ?  142 GLU   A N   1 
ATOM   1029 C CA  . GLU   A 1 137 ? 6.708   -0.426  10.733  1.00 62.13  ?  142 GLU   A CA  1 
ATOM   1030 C C   . GLU   A 1 137 ? 5.384   0.129   11.327  1.00 59.44  ?  142 GLU   A C   1 
ATOM   1031 O O   . GLU   A 1 137 ? 5.287   1.321   11.623  1.00 60.34  ?  142 GLU   A O   1 
ATOM   1032 C CB  . GLU   A 1 137 ? 6.696   -0.218  9.202   1.00 66.15  ?  142 GLU   A CB  1 
ATOM   1033 C CG  . GLU   A 1 137 ? 8.070   -0.113  8.519   1.00 72.25  ?  142 GLU   A CG  1 
ATOM   1034 C CD  . GLU   A 1 137 ? 8.014   -0.008  7.024   0.00 69.74  ?  142 GLU   A CD  1 
ATOM   1035 O OE1 . GLU   A 1 137 ? 7.290   -0.787  6.353   0.00 69.26  ?  142 GLU   A OE1 1 
ATOM   1036 O OE2 . GLU   A 1 137 ? 8.726   0.876   6.487   0.00 72.38  ?  142 GLU   A OE2 1 
ATOM   1037 N N   . ASN   A 1 138 ? 4.392   -0.750  11.487  1.00 51.88  ?  143 ASN   A N   1 
ATOM   1038 C CA  . ASN   A 1 138 ? 3.102   -0.460  12.123  1.00 48.32  ?  143 ASN   A CA  1 
ATOM   1039 C C   . ASN   A 1 138 ? 3.026   -0.839  13.636  1.00 45.34  ?  143 ASN   A C   1 
ATOM   1040 O O   . ASN   A 1 138 ? 1.930   -1.020  14.186  1.00 48.42  ?  143 ASN   A O   1 
ATOM   1041 C CB  . ASN   A 1 138 ? 1.987   -1.175  11.307  1.00 50.07  ?  143 ASN   A CB  1 
ATOM   1042 C CG  . ASN   A 1 138 ? 1.499   -0.374  10.103  1.00 55.70  ?  143 ASN   A CG  1 
ATOM   1043 O OD1 . ASN   A 1 138 ? 1.661   0.835   10.022  1.00 58.28  ?  143 ASN   A OD1 1 
ATOM   1044 N ND2 . ASN   A 1 138 ? 0.857   -1.063  9.164   1.00 62.49  ?  143 ASN   A ND2 1 
ATOM   1045 N N   . ILE   A 1 139 ? 4.172   -0.949  14.302  1.00 46.89  ?  144 ILE   A N   1 
ATOM   1046 C CA  . ILE   A 1 139 ? 4.257   -1.247  15.732  1.00 46.96  ?  144 ILE   A CA  1 
ATOM   1047 C C   . ILE   A 1 139 ? 5.171   -0.162  16.276  1.00 49.12  ?  144 ILE   A C   1 
ATOM   1048 O O   . ILE   A 1 139 ? 6.384   -0.261  16.139  1.00 48.76  ?  144 ILE   A O   1 
ATOM   1049 C CB  . ILE   A 1 139 ? 4.809   -2.668  15.995  1.00 47.46  ?  144 ILE   A CB  1 
ATOM   1050 C CG1 . ILE   A 1 139 ? 3.801   -3.710  15.495  1.00 42.29  ?  144 ILE   A CG1 1 
ATOM   1051 C CG2 . ILE   A 1 139 ? 5.075   -2.885  17.491  1.00 50.43  ?  144 ILE   A CG2 1 
ATOM   1052 C CD1 . ILE   A 1 139 ? 4.371   -5.087  15.342  1.00 47.81  ?  144 ILE   A CD1 1 
ATOM   1053 N N   . LEU   A 1 140 ? 4.578   0.857   16.887  1.00 49.07  ?  145 LEU   A N   1 
ATOM   1054 C CA  . LEU   A 1 140 ? 5.317   2.000   17.410  1.00 49.24  ?  145 LEU   A CA  1 
ATOM   1055 C C   . LEU   A 1 140 ? 5.660   1.774   18.873  1.00 47.17  ?  145 LEU   A C   1 
ATOM   1056 O O   . LEU   A 1 140 ? 4.954   1.057   19.563  1.00 44.11  ?  145 LEU   A O   1 
ATOM   1057 C CB  . LEU   A 1 140 ? 4.496   3.265   17.199  1.00 53.84  ?  145 LEU   A CB  1 
ATOM   1058 C CG  . LEU   A 1 140 ? 4.037   3.535   15.751  1.00 55.64  ?  145 LEU   A CG  1 
ATOM   1059 C CD1 . LEU   A 1 140 ? 3.291   4.861   15.674  1.00 62.28  ?  145 LEU   A CD1 1 
ATOM   1060 C CD2 . LEU   A 1 140 ? 5.190   3.539   14.759  1.00 55.79  ?  145 LEU   A CD2 1 
ATOM   1061 N N   . VAL   A 1 141 ? 6.735   2.418   19.335  1.00 49.48  ?  146 VAL   A N   1 
ATOM   1062 C CA  . VAL   A 1 141 ? 7.369   2.155   20.634  1.00 48.86  ?  146 VAL   A CA  1 
ATOM   1063 C C   . VAL   A 1 141 ? 7.583   3.490   21.356  1.00 51.90  ?  146 VAL   A C   1 
ATOM   1064 O O   . VAL   A 1 141 ? 8.199   4.410   20.790  1.00 50.12  ?  146 VAL   A O   1 
ATOM   1065 C CB  . VAL   A 1 141 ? 8.747   1.452   20.445  1.00 53.84  ?  146 VAL   A CB  1 
ATOM   1066 C CG1 . VAL   A 1 141 ? 9.365   1.038   21.777  1.00 58.05  ?  146 VAL   A CG1 1 
ATOM   1067 C CG2 . VAL   A 1 141 ? 8.622   0.219   19.550  1.00 55.72  ?  146 VAL   A CG2 1 
ATOM   1068 N N   . ASP   A 1 142 ? 7.111   3.574   22.609  1.00 56.83  ?  147 ASP   A N   1 
ATOM   1069 C CA  . ASP   A 1 142 ? 7.335   4.760   23.461  1.00 60.24  ?  147 ASP   A CA  1 
ATOM   1070 C C   . ASP   A 1 142 ? 8.687   4.707   24.181  1.00 60.46  ?  147 ASP   A C   1 
ATOM   1071 O O   . ASP   A 1 142 ? 9.415   3.722   24.038  1.00 67.17  ?  147 ASP   A O   1 
ATOM   1072 C CB  . ASP   A 1 142 ? 6.138   5.018   24.407  1.00 62.28  ?  147 ASP   A CB  1 
ATOM   1073 C CG  . ASP   A 1 142 ? 6.009   4.021   25.549  1.00 61.17  ?  147 ASP   A CG  1 
ATOM   1074 O OD1 . ASP   A 1 142 ? 6.975   3.323   25.926  1.00 62.41  ?  147 ASP   A OD1 1 
ATOM   1075 O OD2 . ASP   A 1 142 ? 4.887   3.965   26.095  1.00 60.55  ?  147 ASP   A OD2 1 
ATOM   1076 N N   . ASN   A 1 143 ? 9.007   5.744   24.957  1.00 63.52  ?  148 ASN   A N   1 
ATOM   1077 C CA  . ASN   A 1 143 ? 10.330  5.843   25.618  1.00 68.32  ?  148 ASN   A CA  1 
ATOM   1078 C C   . ASN   A 1 143 ? 10.604  4.748   26.660  1.00 67.65  ?  148 ASN   A C   1 
ATOM   1079 O O   . ASN   A 1 143 ? 11.743  4.334   26.810  1.00 74.68  ?  148 ASN   A O   1 
ATOM   1080 C CB  . ASN   A 1 143 ? 10.544  7.237   26.236  1.00 73.40  ?  148 ASN   A CB  1 
ATOM   1081 C CG  . ASN   A 1 143 ? 12.017  7.625   26.346  1.00 80.56  ?  148 ASN   A CG  1 
ATOM   1082 O OD1 . ASN   A 1 143 ? 12.828  7.348   25.451  1.00 86.53  ?  148 ASN   A OD1 1 
ATOM   1083 N ND2 . ASN   A 1 143 ? 12.361  8.322   27.424  1.00 84.06  ?  148 ASN   A ND2 1 
ATOM   1084 N N   . ASP   A 1 144 ? 9.547   4.256   27.314  1.00 69.42  ?  149 ASP   A N   1 
ATOM   1085 C CA  . ASP   A 1 144 ? 9.606   3.128   28.263  1.00 69.19  ?  149 ASP   A CA  1 
ATOM   1086 C C   . ASP   A 1 144 ? 9.411   1.735   27.613  1.00 64.62  ?  149 ASP   A C   1 
ATOM   1087 O O   . ASP   A 1 144 ? 9.006   0.792   28.301  1.00 61.26  ?  149 ASP   A O   1 
ATOM   1088 C CB  . ASP   A 1 144 ? 8.545   3.336   29.369  1.00 72.50  ?  149 ASP   A CB  1 
ATOM   1089 C CG  . ASP   A 1 144 ? 8.704   4.667   30.096  1.00 82.16  ?  149 ASP   A CG  1 
ATOM   1090 O OD1 . ASP   A 1 144 ? 9.835   4.951   30.553  1.00 78.72  ?  149 ASP   A OD1 1 
ATOM   1091 O OD2 . ASP   A 1 144 ? 7.706   5.424   30.183  1.00 81.20  ?  149 ASP   A OD2 1 
ATOM   1092 N N   . PHE   A 1 145 ? 9.663   1.602   26.302  1.00 64.64  ?  150 PHE   A N   1 
ATOM   1093 C CA  . PHE   A 1 145 ? 9.554   0.322   25.559  1.00 60.30  ?  150 PHE   A CA  1 
ATOM   1094 C C   . PHE   A 1 145 ? 8.167   -0.350  25.523  1.00 56.64  ?  150 PHE   A C   1 
ATOM   1095 O O   . PHE   A 1 145 ? 8.078   -1.532  25.149  1.00 55.01  ?  150 PHE   A O   1 
ATOM   1096 C CB  . PHE   A 1 145 ? 10.648  -0.677  26.008  1.00 65.98  ?  150 PHE   A CB  1 
ATOM   1097 C CG  . PHE   A 1 145 ? 12.036  -0.260  25.619  1.00 69.86  ?  150 PHE   A CG  1 
ATOM   1098 C CD1 . PHE   A 1 145 ? 12.527  -0.507  24.322  1.00 70.52  ?  150 PHE   A CD1 1 
ATOM   1099 C CD2 . PHE   A 1 145 ? 12.852  0.410   26.527  1.00 66.50  ?  150 PHE   A CD2 1 
ATOM   1100 C CE1 . PHE   A 1 145 ? 13.818  -0.109  23.961  1.00 69.13  ?  150 PHE   A CE1 1 
ATOM   1101 C CE2 . PHE   A 1 145 ? 14.141  0.809   26.168  1.00 68.14  ?  150 PHE   A CE2 1 
ATOM   1102 C CZ  . PHE   A 1 145 ? 14.624  0.551   24.885  1.00 68.63  ?  150 PHE   A CZ  1 
ATOM   1103 N N   . HIS   A 1 146 ? 7.096   0.383   25.868  1.00 49.99  ?  151 HIS   A N   1 
ATOM   1104 C CA  . HIS   A 1 146 ? 5.730   -0.102  25.670  1.00 44.88  ?  151 HIS   A CA  1 
ATOM   1105 C C   . HIS   A 1 146 ? 5.317   0.231   24.244  1.00 44.41  ?  151 HIS   A C   1 
ATOM   1106 O O   . HIS   A 1 146 ? 5.708   1.262   23.704  1.00 48.08  ?  151 HIS   A O   1 
ATOM   1107 C CB  . HIS   A 1 146 ? 4.750   0.515   26.648  1.00 46.31  ?  151 HIS   A CB  1 
ATOM   1108 C CG  . HIS   A 1 146 ? 5.032   0.189   28.081  1.00 55.78  ?  151 HIS   A CG  1 
ATOM   1109 N ND1 . HIS   A 1 146 ? 4.756   -1.043  28.635  1.00 58.56  ?  151 HIS   A ND1 1 
ATOM   1110 C CD2 . HIS   A 1 146 ? 5.541   0.944   29.083  1.00 60.84  ?  151 HIS   A CD2 1 
ATOM   1111 C CE1 . HIS   A 1 146 ? 5.098   -1.039  29.910  1.00 62.01  ?  151 HIS   A CE1 1 
ATOM   1112 N NE2 . HIS   A 1 146 ? 5.578   0.156   30.207  1.00 64.90  ?  151 HIS   A NE2 1 
ATOM   1113 N N   . ILE   A 1 147 ? 4.509   -0.631  23.649  1.00 45.18  ?  152 ILE   A N   1 
ATOM   1114 C CA  . ILE   A 1 147 ? 4.158   -0.535  22.222  1.00 46.19  ?  152 ILE   A CA  1 
ATOM   1115 C C   . ILE   A 1 147 ? 2.716   -0.119  22.009  1.00 46.57  ?  152 ILE   A C   1 
ATOM   1116 O O   . ILE   A 1 147 ? 1.893   -0.202  22.920  1.00 46.15  ?  152 ILE   A O   1 
ATOM   1117 C CB  . ILE   A 1 147 ? 4.479   -1.839  21.432  1.00 47.38  ?  152 ILE   A CB  1 
ATOM   1118 C CG1 . ILE   A 1 147 ? 3.561   -3.021  21.822  1.00 49.82  ?  152 ILE   A CG1 1 
ATOM   1119 C CG2 . ILE   A 1 147 ? 5.948   -2.203  21.619  1.00 48.46  ?  152 ILE   A CG2 1 
ATOM   1120 C CD1 . ILE   A 1 147 ? 2.360   -3.238  20.923  1.00 50.58  ?  152 ILE   A CD1 1 
ATOM   1121 N N   . LYS   A 1 148 ? 2.434   0.309   20.778  1.00 50.07  ?  153 LYS   A N   1 
ATOM   1122 C CA  . LYS   A 1 148 ? 1.073   0.559   20.284  1.00 49.06  ?  153 LYS   A CA  1 
ATOM   1123 C C   . LYS   A 1 148 ? 1.025   0.160   18.812  1.00 45.36  ?  153 LYS   A C   1 
ATOM   1124 O O   . LYS   A 1 148 ? 1.939   0.485   18.045  1.00 47.46  ?  153 LYS   A O   1 
ATOM   1125 C CB  . LYS   A 1 148 ? 0.683   2.037   20.421  1.00 51.55  ?  153 LYS   A CB  1 
ATOM   1126 C CG  . LYS   A 1 148 ? 0.533   2.545   21.841  1.00 56.32  ?  153 LYS   A CG  1 
ATOM   1127 C CD  . LYS   A 1 148 ? -0.070  3.940   21.894  1.00 61.82  ?  153 LYS   A CD  1 
ATOM   1128 C CE  . LYS   A 1 148 ? -0.443  4.371   23.307  1.00 62.36  ?  153 LYS   A CE  1 
ATOM   1129 N NZ  . LYS   A 1 148 ? 0.725   4.595   24.196  1.00 67.71  ?  153 LYS   A NZ  1 
ATOM   1130 N N   . ILE   A 1 149 ? -0.025  -0.552  18.425  1.00 42.91  ?  154 ILE   A N   1 
ATOM   1131 C CA  . ILE   A 1 149 ? -0.249  -0.939  17.029  1.00 42.67  ?  154 ILE   A CA  1 
ATOM   1132 C C   . ILE   A 1 149 ? -0.831  0.247   16.254  1.00 41.08  ?  154 ILE   A C   1 
ATOM   1133 O O   . ILE   A 1 149 ? -1.770  0.895   16.729  1.00 43.74  ?  154 ILE   A O   1 
ATOM   1134 C CB  . ILE   A 1 149 ? -1.175  -2.165  16.951  1.00 43.77  ?  154 ILE   A CB  1 
ATOM   1135 C CG1 . ILE   A 1 149 ? -0.465  -3.366  17.583  1.00 48.75  ?  154 ILE   A CG1 1 
ATOM   1136 C CG2 . ILE   A 1 149 ? -1.566  -2.508  15.505  1.00 46.15  ?  154 ILE   A CG2 1 
ATOM   1137 C CD1 . ILE   A 1 149 ? -1.430  -4.407  18.065  1.00 61.85  ?  154 ILE   A CD1 1 
ATOM   1138 N N   . ALA   A 1 150 ? -0.279  0.483   15.062  1.00 54.16  ?  155 ALA   A N   1 
ATOM   1139 C CA  . ALA   A 1 150 ? -0.665  1.578   14.173  1.00 55.14  ?  155 ALA   A CA  1 
ATOM   1140 C C   . ALA   A 1 150 ? -1.145  1.025   12.849  1.00 56.62  ?  155 ALA   A C   1 
ATOM   1141 O O   . ALA   A 1 150 ? -0.914  -0.132  12.539  1.00 54.55  ?  155 ALA   A O   1 
ATOM   1142 C CB  . ALA   A 1 150 ? 0.521   2.491   13.936  1.00 57.19  ?  155 ALA   A CB  1 
ATOM   1143 N N   . ASP   A 1 151 ? -1.815  1.871   12.074  1.00 61.09  ?  156 ASP   A N   1 
ATOM   1144 C CA  . ASP   A 1 151 ? -2.182  1.564   10.682  1.00 63.22  ?  156 ASP   A CA  1 
ATOM   1145 C C   . ASP   A 1 151 ? -1.757  2.736   9.806   1.00 58.04  ?  156 ASP   A C   1 
ATOM   1146 O O   . ASP   A 1 151 ? -2.587  3.460   9.267   1.00 60.70  ?  156 ASP   A O   1 
ATOM   1147 C CB  . ASP   A 1 151 ? -3.682  1.235   10.570  1.00 60.60  ?  156 ASP   A CB  1 
ATOM   1148 C CG  . ASP   A 1 151 ? -4.108  0.843   9.154   1.00 64.63  ?  156 ASP   A CG  1 
ATOM   1149 O OD1 . ASP   A 1 151 ? -3.284  0.336   8.353   1.00 59.72  ?  156 ASP   A OD1 1 
ATOM   1150 O OD2 . ASP   A 1 151 ? -5.305  1.008   8.837   1.00 67.75  ?  156 ASP   A OD2 1 
ATOM   1151 N N   . LEU   A 1 152 ? -0.443  2.894   9.650   1.00 54.04  ?  157 LEU   A N   1 
ATOM   1152 C CA  . LEU   A 1 152 ? 0.144   4.062   8.968   1.00 52.11  ?  157 LEU   A CA  1 
ATOM   1153 C C   . LEU   A 1 152 ? -0.078  4.080   7.465   1.00 52.72  ?  157 LEU   A C   1 
ATOM   1154 O O   . LEU   A 1 152 ? -0.245  5.143   6.893   1.00 58.61  ?  157 LEU   A O   1 
ATOM   1155 C CB  . LEU   A 1 152 ? 1.628   4.215   9.295   1.00 51.71  ?  157 LEU   A CB  1 
ATOM   1156 C CG  . LEU   A 1 152 ? 1.969   4.348   10.796  1.00 52.74  ?  157 LEU   A CG  1 
ATOM   1157 C CD1 . LEU   A 1 152 ? 3.473   4.431   11.015  1.00 53.80  ?  157 LEU   A CD1 1 
ATOM   1158 C CD2 . LEU   A 1 152 ? 1.275   5.520   11.473  1.00 49.88  ?  157 LEU   A CD2 1 
ATOM   1159 N N   . GLY   A 1 153 ? -0.135  2.909   6.834   1.00 56.47  ?  158 GLY   A N   1 
ATOM   1160 C CA  . GLY   A 1 153 ? -0.594  2.766   5.435   1.00 56.28  ?  158 GLY   A CA  1 
ATOM   1161 C C   . GLY   A 1 153 ? -2.097  2.842   5.169   1.00 54.97  ?  158 GLY   A C   1 
ATOM   1162 O O   . GLY   A 1 153 ? -2.516  2.719   4.028   1.00 60.10  ?  158 GLY   A O   1 
ATOM   1163 N N   . LEU   A 1 154 ? -2.905  2.999   6.215   1.00 57.14  ?  159 LEU   A N   1 
ATOM   1164 C CA  . LEU   A 1 154 ? -4.352  3.225   6.123   1.00 62.64  ?  159 LEU   A CA  1 
ATOM   1165 C C   . LEU   A 1 154 ? -5.097  2.067   5.420   1.00 63.98  ?  159 LEU   A C   1 
ATOM   1166 O O   . LEU   A 1 154 ? -6.004  2.281   4.634   1.00 69.08  ?  159 LEU   A O   1 
ATOM   1167 C CB  . LEU   A 1 154 ? -4.634  4.594   5.479   1.00 66.13  ?  159 LEU   A CB  1 
ATOM   1168 C CG  . LEU   A 1 154 ? -3.985  5.789   6.193   1.00 69.25  ?  159 LEU   A CG  1 
ATOM   1169 C CD1 . LEU   A 1 154 ? -3.950  7.017   5.296   1.00 76.18  ?  159 LEU   A CD1 1 
ATOM   1170 C CD2 . LEU   A 1 154 ? -4.721  6.092   7.491   1.00 69.31  ?  159 LEU   A CD2 1 
ATOM   1171 N N   . ALA   A 1 155 ? -4.675  0.842   5.721   1.00 63.03  ?  160 ALA   A N   1 
ATOM   1172 C CA  . ALA   A 1 155 ? -5.270  -0.385  5.175   1.00 62.87  ?  160 ALA   A CA  1 
ATOM   1173 C C   . ALA   A 1 155 ? -6.747  -0.590  5.542   1.00 64.25  ?  160 ALA   A C   1 
ATOM   1174 O O   . ALA   A 1 155 ? -7.517  -1.102  4.719   1.00 74.43  ?  160 ALA   A O   1 
ATOM   1175 C CB  . ALA   A 1 155 ? -4.445  -1.596  5.605   1.00 67.63  ?  160 ALA   A CB  1 
ATOM   1176 N N   . SER   A 1 156 ? -7.130  -0.186  6.757   1.00 64.21  ?  161 SER   A N   1 
ATOM   1177 C CA  . SER   A 1 156 ? -8.538  -0.248  7.223   1.00 64.68  ?  161 SER   A CA  1 
ATOM   1178 C C   . SER   A 1 156 ? -9.456  0.912   6.821   1.00 62.58  ?  161 SER   A C   1 
ATOM   1179 O O   . SER   A 1 156 ? -10.651 0.868   7.132   1.00 63.33  ?  161 SER   A O   1 
ATOM   1180 C CB  . SER   A 1 156 ? -8.570  -0.427  8.746   1.00 66.41  ?  161 SER   A CB  1 
ATOM   1181 O OG  . SER   A 1 156 ? -8.112  -1.717  9.074   1.00 72.48  ?  161 SER   A OG  1 
ATOM   1182 N N   . PHE   A 1 157 ? -8.916  1.930   6.141   1.00 63.43  ?  162 PHE   A N   1 
ATOM   1183 C CA  . PHE   A 1 157 ? -9.619  3.208   5.906   1.00 61.78  ?  162 PHE   A CA  1 
ATOM   1184 C C   . PHE   A 1 157 ? -9.462  3.620   4.436   1.00 67.36  ?  162 PHE   A C   1 
ATOM   1185 O O   . PHE   A 1 157 ? -8.528  4.353   4.083   1.00 65.25  ?  162 PHE   A O   1 
ATOM   1186 C CB  . PHE   A 1 157 ? -9.090  4.274   6.871   1.00 58.35  ?  162 PHE   A CB  1 
ATOM   1187 C CG  . PHE   A 1 157 ? -9.199  3.863   8.321   1.00 56.51  ?  162 PHE   A CG  1 
ATOM   1188 C CD1 . PHE   A 1 157 ? -10.453 3.759   8.916   1.00 54.76  ?  162 PHE   A CD1 1 
ATOM   1189 C CD2 . PHE   A 1 157 ? -8.065  3.488   9.062   1.00 53.13  ?  162 PHE   A CD2 1 
ATOM   1190 C CE1 . PHE   A 1 157 ? -10.587 3.339   10.238  1.00 54.27  ?  162 PHE   A CE1 1 
ATOM   1191 C CE2 . PHE   A 1 157 ? -8.193  3.065   10.386  1.00 52.30  ?  162 PHE   A CE2 1 
ATOM   1192 C CZ  . PHE   A 1 157 ? -9.460  2.982   10.970  1.00 52.62  ?  162 PHE   A CZ  1 
ATOM   1193 N N   . LYS   A 1 158 ? -10.408 3.154   3.603   1.00 70.96  ?  163 LYS   A N   1 
ATOM   1194 C CA  . LYS   A 1 158 ? -10.308 3.202   2.128   1.00 73.23  ?  163 LYS   A CA  1 
ATOM   1195 C C   . LYS   A 1 158 ? -10.152 4.617   1.535   1.00 74.50  ?  163 LYS   A C   1 
ATOM   1196 O O   . LYS   A 1 158 ? -9.262  4.844   0.709   1.00 72.52  ?  163 LYS   A O   1 
ATOM   1197 C CB  . LYS   A 1 158 ? -11.515 2.495   1.491   1.00 69.12  ?  163 LYS   A CB  1 
ATOM   1198 C CG  . LYS   A 1 158 ? -11.557 0.970   1.710   0.00 69.98  ?  163 LYS   A CG  1 
ATOM   1199 C CD  . LYS   A 1 158 ? -12.963 0.483   2.037   0.00 70.69  ?  163 LYS   A CD  1 
ATOM   1200 C CE  . LYS   A 1 158 ? -13.012 -1.029  2.193   0.00 71.64  ?  163 LYS   A CE  1 
ATOM   1201 N NZ  . LYS   A 1 158 ? -14.267 -1.481  2.855   0.00 72.28  ?  163 LYS   A NZ  1 
ATOM   1202 N N   . MET   A 1 159 ? -11.015 5.544   1.965   1.00 70.10  ?  164 MET   A N   1 
ATOM   1203 C CA  . MET   A 1 159 ? -11.044 6.936   1.463   1.00 72.37  ?  164 MET   A CA  1 
ATOM   1204 C C   . MET   A 1 159 ? -9.778  7.740   1.758   1.00 69.90  ?  164 MET   A C   1 
ATOM   1205 O O   . MET   A 1 159 ? -9.253  8.395   0.848   1.00 71.73  ?  164 MET   A O   1 
ATOM   1206 C CB  . MET   A 1 159 ? -12.277 7.706   1.975   1.00 69.93  ?  164 MET   A CB  1 
ATOM   1207 C CG  . MET   A 1 159 ? -13.595 7.164   1.408   0.00 67.50  ?  164 MET   A CG  1 
ATOM   1208 S SD  . MET   A 1 159 ? -13.848 7.455   -0.349  0.00 67.97  ?  164 MET   A SD  1 
ATOM   1209 C CE  . MET   A 1 159 ? -15.408 6.608   -0.593  0.00 69.21  ?  164 MET   A CE  1 
ATOM   1210 N N   . TRP   A 1 160 ? -9.292  7.683   3.003   1.00 64.92  ?  165 TRP   A N   1 
ATOM   1211 C CA  . TRP   A 1 160 ? -7.995  8.301   3.367   1.00 61.18  ?  165 TRP   A CA  1 
ATOM   1212 C C   . TRP   A 1 160 ? -6.833  7.636   2.631   1.00 66.67  ?  165 TRP   A C   1 
ATOM   1213 O O   . TRP   A 1 160 ? -5.880  8.315   2.276   1.00 68.41  ?  165 TRP   A O   1 
ATOM   1214 C CB  . TRP   A 1 160 ? -7.726  8.238   4.879   1.00 59.73  ?  165 TRP   A CB  1 
ATOM   1215 C CG  . TRP   A 1 160 ? -8.559  9.139   5.720   1.00 55.27  ?  165 TRP   A CG  1 
ATOM   1216 C CD1 . TRP   A 1 160 ? -9.782  8.873   6.239   1.00 53.26  ?  165 TRP   A CD1 1 
ATOM   1217 C CD2 . TRP   A 1 160 ? -8.198  10.441  6.186   1.00 53.66  ?  165 TRP   A CD2 1 
ATOM   1218 N NE1 . TRP   A 1 160 ? -10.227 9.932   6.980   1.00 56.19  ?  165 TRP   A NE1 1 
ATOM   1219 C CE2 . TRP   A 1 160 ? -9.276  10.916  6.962   1.00 55.81  ?  165 TRP   A CE2 1 
ATOM   1220 C CE3 . TRP   A 1 160 ? -7.067  11.265  6.009   1.00 54.51  ?  165 TRP   A CE3 1 
ATOM   1221 C CZ2 . TRP   A 1 160 ? -9.266  12.185  7.570   1.00 56.37  ?  165 TRP   A CZ2 1 
ATOM   1222 C CZ3 . TRP   A 1 160 ? -7.047  12.526  6.605   1.00 55.19  ?  165 TRP   A CZ3 1 
ATOM   1223 C CH2 . TRP   A 1 160 ? -8.143  12.974  7.386   1.00 57.21  ?  165 TRP   A CH2 1 
ATOM   1224 N N   . SER   A 1 161 ? -6.933  6.321   2.396   1.00 73.85  ?  166 SER   A N   1 
ATOM   1225 C CA  . SER   A 1 161 ? -5.932  5.575   1.622   1.00 78.16  ?  166 SER   A CA  1 
ATOM   1226 C C   . SER   A 1 161 ? -5.919  5.983   0.143   1.00 80.39  ?  166 SER   A C   1 
ATOM   1227 O O   . SER   A 1 161 ? -4.846  6.148   -0.443  1.00 81.07  ?  166 SER   A O   1 
ATOM   1228 C CB  . SER   A 1 161 ? -6.165  4.067   1.747   1.00 78.90  ?  166 SER   A CB  1 
ATOM   1229 O OG  . SER   A 1 161 ? -4.968  3.353   1.524   1.00 83.85  ?  166 SER   A OG  1 
ATOM   1230 N N   . LYS   A 1 162 ? -7.108  6.136   -0.445  1.00 85.62  ?  167 LYS   A N   1 
ATOM   1231 C CA  . LYS   A 1 162 ? -7.248  6.667   -1.813  1.00 90.10  ?  167 LYS   A CA  1 
ATOM   1232 C C   . LYS   A 1 162 ? -6.795  8.130   -1.900  1.00 92.81  ?  167 LYS   A C   1 
ATOM   1233 O O   . LYS   A 1 162 ? -6.115  8.509   -2.856  1.00 96.83  ?  167 LYS   A O   1 
ATOM   1234 C CB  . LYS   A 1 162 ? -8.686  6.523   -2.323  1.00 89.61  ?  167 LYS   A CB  1 
ATOM   1235 C CG  . LYS   A 1 162 ? -9.092  5.092   -2.657  0.00 91.54  ?  167 LYS   A CG  1 
ATOM   1236 C CD  . LYS   A 1 162 ? -10.586 4.981   -2.919  0.00 91.94  ?  167 LYS   A CD  1 
ATOM   1237 C CE  . LYS   A 1 162 ? -10.992 3.557   -3.263  0.00 92.42  ?  167 LYS   A CE  1 
ATOM   1238 N NZ  . LYS   A 1 162 ? -12.457 3.438   -3.502  0.00 93.04  ?  167 LYS   A NZ  1 
ATOM   1239 N N   . LEU   A 1 163 ? -7.163  8.929   -0.895  1.00 93.39  ?  168 LEU   A N   1 
ATOM   1240 C CA  . LEU   A 1 163 ? -6.679  10.322  -0.745  1.00 91.74  ?  168 LEU   A CA  1 
ATOM   1241 C C   . LEU   A 1 163 ? -5.153  10.419  -0.641  1.00 87.90  ?  168 LEU   A C   1 
ATOM   1242 O O   . LEU   A 1 163 ? -4.545  11.352  -1.165  1.00 79.98  ?  168 LEU   A O   1 
ATOM   1243 C CB  . LEU   A 1 163 ? -7.317  10.976  0.491   1.00 84.87  ?  168 LEU   A CB  1 
ATOM   1244 C CG  . LEU   A 1 163 ? -6.960  12.419  0.846   1.00 83.98  ?  168 LEU   A CG  1 
ATOM   1245 C CD1 . LEU   A 1 163 ? -7.387  13.350  -0.272  1.00 88.78  ?  168 LEU   A CD1 1 
ATOM   1246 C CD2 . LEU   A 1 163 ? -7.609  12.832  2.156   1.00 89.25  ?  168 LEU   A CD2 1 
ATOM   1247 N N   . ASN   A 1 164 ? -4.564  9.448   0.050   1.00 95.48  ?  169 ASN   A N   1 
ATOM   1248 C CA  . ASN   A 1 164 ? -3.113  9.360   0.225   1.00 106.00 ?  169 ASN   A CA  1 
ATOM   1249 C C   . ASN   A 1 164 ? -2.384  9.109   -1.107  1.00 108.09 ?  169 ASN   A C   1 
ATOM   1250 O O   . ASN   A 1 164 ? -1.321  9.686   -1.331  1.00 97.25  ?  169 ASN   A O   1 
ATOM   1251 C CB  . ASN   A 1 164 ? -2.779  8.255   1.268   1.00 105.54 ?  169 ASN   A CB  1 
ATOM   1252 C CG  . ASN   A 1 164 ? -1.322  8.235   1.777   1.00 103.74 ?  169 ASN   A CG  1 
ATOM   1253 O OD1 . ASN   A 1 164 ? -0.966  7.248   2.428   1.00 90.70  ?  169 ASN   A OD1 1 
ATOM   1254 N ND2 . ASN   A 1 164 ? -0.493  9.277   1.543   1.00 106.27 ?  169 ASN   A ND2 1 
ATOM   1255 N N   . ASN   A 1 165 ? -2.988  8.279   -1.973  1.00 118.35 ?  170 ASN   A N   1 
ATOM   1256 C CA  . ASN   A 1 165 ? -2.436  7.853   -3.265  1.00 112.76 ?  170 ASN   A CA  1 
ATOM   1257 C C   . ASN   A 1 165 ? -3.264  8.407   -4.418  1.00 96.51  ?  170 ASN   A C   1 
ATOM   1258 O O   . ASN   A 1 165 ? -3.094  9.554   -4.812  1.00 89.21  ?  170 ASN   A O   1 
ATOM   1259 C CB  . ASN   A 1 165 ? -2.437  6.323   -3.340  1.00 109.03 ?  170 ASN   A CB  1 
ATOM   1260 C CG  . ASN   A 1 165 ? -1.780  5.659   -2.239  0.00 117.76 ?  170 ASN   A CG  1 
ATOM   1261 O OD1 . ASN   A 1 165 ? -0.832  6.193   -1.662  0.00 117.65 ?  170 ASN   A OD1 1 
ATOM   1262 N ND2 . ASN   A 1 165 ? -2.229  4.450   -1.909  0.00 117.40 ?  170 ASN   A ND2 1 
ATOM   1263 N N   . GLY   A 1 183 ? 5.486   -1.586  0.722   1.00 93.35  ?  188 GLY   A N   1 
ATOM   1264 C CA  . GLY   A 1 183 ? 5.267   -2.744  -0.148  1.00 96.74  ?  188 GLY   A CA  1 
ATOM   1265 C C   . GLY   A 1 183 ? 5.869   -4.069  0.309   1.00 95.86  ?  188 GLY   A C   1 
ATOM   1266 O O   . GLY   A 1 183 ? 6.278   -4.883  -0.535  1.00 89.02  ?  188 GLY   A O   1 
ATOM   1267 N N   . THR   A 1 184 ? 5.891   -4.302  1.629   1.00 99.82  ?  189 THR   A N   1 
ATOM   1268 C CA  . THR   A 1 184 ? 6.434   -5.544  2.204   1.00 96.81  ?  189 THR   A CA  1 
ATOM   1269 C C   . THR   A 1 184 ? 5.365   -6.655  2.167   1.00 89.41  ?  189 THR   A C   1 
ATOM   1270 O O   . THR   A 1 184 ? 4.294   -6.558  2.780   1.00 74.31  ?  189 THR   A O   1 
ATOM   1271 C CB  . THR   A 1 184 ? 7.082   -5.388  3.610   1.00 92.11  ?  189 THR   A CB  1 
ATOM   1272 O OG1 . THR   A 1 184 ? 7.705   -6.628  3.978   1.00 88.47  ?  189 THR   A OG1 1 
ATOM   1273 C CG2 . THR   A 1 184 ? 6.092   -4.979  4.708   1.00 85.24  ?  189 THR   A CG2 1 
ATOM   1274 N N   . LEU   A 1 185 ? 5.695   -7.691  1.401   1.00 82.32  ?  190 LEU   A N   1 
ATOM   1275 C CA  . LEU   A 1 185 ? 4.948   -8.948  1.352   1.00 76.28  ?  190 LEU   A CA  1 
ATOM   1276 C C   . LEU   A 1 185 ? 5.507   -10.031 2.283   1.00 71.41  ?  190 LEU   A C   1 
ATOM   1277 O O   . LEU   A 1 185 ? 5.011   -11.161 2.276   1.00 76.66  ?  190 LEU   A O   1 
ATOM   1278 C CB  . LEU   A 1 185 ? 4.933   -9.471  -0.093  1.00 81.69  ?  190 LEU   A CB  1 
ATOM   1279 C CG  . LEU   A 1 185 ? 4.578   -8.474  -1.201  1.00 81.84  ?  190 LEU   A CG  1 
ATOM   1280 C CD1 . LEU   A 1 185 ? 4.481   -9.180  -2.539  1.00 83.30  ?  190 LEU   A CD1 1 
ATOM   1281 C CD2 . LEU   A 1 185 ? 3.277   -7.744  -0.900  1.00 86.20  ?  190 LEU   A CD2 1 
ATOM   1282 N N   . TYR   A 1 186 ? 6.504   -9.693  3.102   1.00 67.09  ?  191 TYR   A N   1 
ATOM   1283 C CA  . TYR   A 1 186 ? 7.132   -10.648 4.020   1.00 65.35  ?  191 TYR   A CA  1 
ATOM   1284 C C   . TYR   A 1 186 ? 6.223   -11.094 5.170   1.00 60.70  ?  191 TYR   A C   1 
ATOM   1285 O O   . TYR   A 1 186 ? 6.430   -12.173 5.719   1.00 66.51  ?  191 TYR   A O   1 
ATOM   1286 C CB  . TYR   A 1 186 ? 8.407   -10.068 4.629   1.00 61.81  ?  191 TYR   A CB  1 
ATOM   1287 C CG  . TYR   A 1 186 ? 9.515   -9.622  3.672   1.00 65.20  ?  191 TYR   A CG  1 
ATOM   1288 C CD1 . TYR   A 1 186 ? 9.650   -10.141 2.370   1.00 66.04  ?  191 TYR   A CD1 1 
ATOM   1289 C CD2 . TYR   A 1 186 ? 10.464  -8.679  4.096   1.00 69.88  ?  191 TYR   A CD2 1 
ATOM   1290 C CE1 . TYR   A 1 186 ? 10.670  -9.706  1.526   1.00 71.29  ?  191 TYR   A CE1 1 
ATOM   1291 C CE2 . TYR   A 1 186 ? 11.493  -8.250  3.261   1.00 69.08  ?  191 TYR   A CE2 1 
ATOM   1292 C CZ  . TYR   A 1 186 ? 11.593  -8.764  1.978   1.00 71.97  ?  191 TYR   A CZ  1 
ATOM   1293 O OH  . TYR   A 1 186 ? 12.612  -8.335  1.161   1.00 79.07  ?  191 TYR   A OH  1 
ATOM   1294 N N   . TYR   A 1 187 ? 5.255   -10.256 5.534   1.00 54.60  ?  192 TYR   A N   1 
ATOM   1295 C CA  . TYR   A 1 187 ? 4.323   -10.489 6.646   1.00 53.69  ?  192 TYR   A CA  1 
ATOM   1296 C C   . TYR   A 1 187 ? 2.925   -10.862 6.154   1.00 53.27  ?  192 TYR   A C   1 
ATOM   1297 O O   . TYR   A 1 187 ? 2.014   -11.032 6.967   1.00 49.10  ?  192 TYR   A O   1 
ATOM   1298 C CB  . TYR   A 1 187 ? 4.263   -9.230  7.531   1.00 49.00  ?  192 TYR   A CB  1 
ATOM   1299 C CG  . TYR   A 1 187 ? 5.645   -8.811  8.010   1.00 46.81  ?  192 TYR   A CG  1 
ATOM   1300 C CD1 . TYR   A 1 187 ? 6.473   -8.006  7.220   1.00 51.03  ?  192 TYR   A CD1 1 
ATOM   1301 C CD2 . TYR   A 1 187 ? 6.149   -9.271  9.222   1.00 45.98  ?  192 TYR   A CD2 1 
ATOM   1302 C CE1 . TYR   A 1 187 ? 7.761   -7.658  7.641   1.00 54.20  ?  192 TYR   A CE1 1 
ATOM   1303 C CE2 . TYR   A 1 187 ? 7.424   -8.928  9.655   1.00 47.48  ?  192 TYR   A CE2 1 
ATOM   1304 C CZ  . TYR   A 1 187 ? 8.225   -8.128  8.862   1.00 49.22  ?  192 TYR   A CZ  1 
ATOM   1305 O OH  . TYR   A 1 187 ? 9.460   -7.793  9.316   1.00 51.40  ?  192 TYR   A OH  1 
ATOM   1306 N N   . MET   A 1 188 ? 2.770   -10.993 4.834   1.00 59.42  ?  193 MET   A N   1 
ATOM   1307 C CA  . MET   A 1 188 ? 1.495   -11.268 4.184   1.00 61.92  ?  193 MET   A CA  1 
ATOM   1308 C C   . MET   A 1 188 ? 1.338   -12.773 4.090   1.00 63.57  ?  193 MET   A C   1 
ATOM   1309 O O   . MET   A 1 188 ? 2.253   -13.480 3.616   1.00 65.19  ?  193 MET   A O   1 
ATOM   1310 C CB  . MET   A 1 188 ? 1.479   -10.670 2.778   1.00 63.78  ?  193 MET   A CB  1 
ATOM   1311 C CG  . MET   A 1 188 ? 0.133   -10.731 2.093   1.00 69.09  ?  193 MET   A CG  1 
ATOM   1312 S SD  . MET   A 1 188 ? 0.105   -9.731  0.600   1.00 81.32  ?  193 MET   A SD  1 
ATOM   1313 C CE  . MET   A 1 188 ? 0.004   -8.076  1.281   1.00 78.32  ?  193 MET   A CE  1 
ATOM   1314 N N   . ALA   A 1 189 ? 0.164   -13.245 4.498   1.00 61.17  ?  194 ALA   A N   1 
ATOM   1315 C CA  . ALA   A 1 189 ? -0.152  -14.663 4.498   1.00 58.12  ?  194 ALA   A CA  1 
ATOM   1316 C C   . ALA   A 1 189 ? -0.250  -15.186 3.071   1.00 63.61  ?  194 ALA   A C   1 
ATOM   1317 O O   . ALA   A 1 189 ? -0.636  -14.432 2.178   1.00 64.82  ?  194 ALA   A O   1 
ATOM   1318 C CB  . ALA   A 1 189 ? -1.447  -14.917 5.250   1.00 56.44  ?  194 ALA   A CB  1 
ATOM   1319 N N   . PRO   A 1 190 ? 0.116   -16.472 2.844   1.00 74.27  ?  195 PRO   A N   1 
ATOM   1320 C CA  . PRO   A 1 190 ? 0.142   -17.035 1.477   1.00 71.97  ?  195 PRO   A CA  1 
ATOM   1321 C C   . PRO   A 1 190 ? -1.182  -16.959 0.728   1.00 68.46  ?  195 PRO   A C   1 
ATOM   1322 O O   . PRO   A 1 190 ? -1.174  -16.709 -0.470  1.00 70.86  ?  195 PRO   A O   1 
ATOM   1323 C CB  . PRO   A 1 190 ? 0.576   -18.498 1.696   1.00 78.82  ?  195 PRO   A CB  1 
ATOM   1324 C CG  . PRO   A 1 190 ? 0.278   -18.777 3.125   1.00 83.26  ?  195 PRO   A CG  1 
ATOM   1325 C CD  . PRO   A 1 190 ? 0.542   -17.485 3.835   1.00 76.52  ?  195 PRO   A CD  1 
ATOM   1326 N N   . GLU   A 1 191 ? -2.299  -17.152 1.431   1.00 64.94  ?  196 GLU   A N   1 
ATOM   1327 C CA  . GLU   A 1 191 ? -3.644  -16.982 0.833   1.00 68.52  ?  196 GLU   A CA  1 
ATOM   1328 C C   . GLU   A 1 191 ? -3.899  -15.619 0.147   1.00 69.67  ?  196 GLU   A C   1 
ATOM   1329 O O   . GLU   A 1 191 ? -4.749  -15.535 -0.731  1.00 79.79  ?  196 GLU   A O   1 
ATOM   1330 C CB  . GLU   A 1 191 ? -4.769  -17.312 1.839   1.00 68.39  ?  196 GLU   A CB  1 
ATOM   1331 C CG  . GLU   A 1 191 ? -4.872  -16.436 3.088   1.00 66.75  ?  196 GLU   A CG  1 
ATOM   1332 C CD  . GLU   A 1 191 ? -4.141  -16.971 4.309   1.00 65.02  ?  196 GLU   A CD  1 
ATOM   1333 O OE1 . GLU   A 1 191 ? -4.577  -16.654 5.433   1.00 61.74  ?  196 GLU   A OE1 1 
ATOM   1334 O OE2 . GLU   A 1 191 ? -3.118  -17.678 4.166   1.00 65.59  ?  196 GLU   A OE2 1 
ATOM   1335 N N   . HIS   A 1 192 ? -3.183  -14.573 0.567   1.00 67.54  ?  197 HIS   A N   1 
ATOM   1336 C CA  . HIS   A 1 192 ? -3.216  -13.237 -0.070  1.00 63.22  ?  197 HIS   A CA  1 
ATOM   1337 C C   . HIS   A 1 192 ? -2.180  -13.003 -1.161  1.00 62.46  ?  197 HIS   A C   1 
ATOM   1338 O O   . HIS   A 1 192 ? -2.391  -12.166 -2.023  1.00 65.88  ?  197 HIS   A O   1 
ATOM   1339 C CB  . HIS   A 1 192 ? -3.133  -12.164 1.022   1.00 57.23  ?  197 HIS   A CB  1 
ATOM   1340 C CG  . HIS   A 1 192 ? -4.215  -12.307 2.040   1.00 56.94  ?  197 HIS   A CG  1 
ATOM   1341 N ND1 . HIS   A 1 192 ? -5.542  -12.404 1.684   1.00 66.72  ?  197 HIS   A ND1 1 
ATOM   1342 C CD2 . HIS   A 1 192 ? -4.177  -12.449 3.382   1.00 56.64  ?  197 HIS   A CD2 1 
ATOM   1343 C CE1 . HIS   A 1 192 ? -6.279  -12.567 2.763   1.00 61.27  ?  197 HIS   A CE1 1 
ATOM   1344 N NE2 . HIS   A 1 192 ? -5.476  -12.589 3.807   1.00 61.11  ?  197 HIS   A NE2 1 
ATOM   1345 N N   . LEU   A 1 193 ? -1.068  -13.729 -1.118  1.00 65.44  ?  198 LEU   A N   1 
ATOM   1346 C CA  . LEU   A 1 193 ? -0.073  -13.736 -2.200  1.00 67.89  ?  198 LEU   A CA  1 
ATOM   1347 C C   . LEU   A 1 193 ? -0.667  -14.359 -3.466  1.00 73.53  ?  198 LEU   A C   1 
ATOM   1348 O O   . LEU   A 1 193 ? -1.192  -15.471 -3.422  1.00 80.73  ?  198 LEU   A O   1 
ATOM   1349 C CB  . LEU   A 1 193 ? 1.176   -14.507 -1.776  1.00 68.03  ?  198 LEU   A CB  1 
ATOM   1350 C CG  . LEU   A 1 193 ? 1.995   -13.975 -0.590  1.00 66.52  ?  198 LEU   A CG  1 
ATOM   1351 C CD1 . LEU   A 1 193 ? 3.093   -14.958 -0.220  1.00 67.14  ?  198 LEU   A CD1 1 
ATOM   1352 C CD2 . LEU   A 1 193 ? 2.606   -12.609 -0.888  1.00 66.75  ?  198 LEU   A CD2 1 
ATOM   1353 N N   . ASN   A 1 194 ? -0.623  -13.613 -4.570  1.00 77.55  ?  199 ASN   A N   1 
ATOM   1354 C CA  . ASN   A 1 194 ? -1.298  -13.970 -5.836  1.00 84.44  ?  199 ASN   A CA  1 
ATOM   1355 C C   . ASN   A 1 194 ? -2.842  -14.198 -5.775  1.00 85.26  ?  199 ASN   A C   1 
ATOM   1356 O O   . ASN   A 1 194 ? -3.397  -14.802 -6.691  1.00 97.18  ?  199 ASN   A O   1 
ATOM   1357 C CB  . ASN   A 1 194 ? -0.588  -15.164 -6.535  1.00 91.11  ?  199 ASN   A CB  1 
ATOM   1358 C CG  . ASN   A 1 194 ? 0.882   -14.906 -6.940  1.00 95.53  ?  199 ASN   A CG  1 
ATOM   1359 O OD1 . ASN   A 1 194 ? 1.553   -15.870 -7.332  1.00 103.36 ?  199 ASN   A OD1 1 
ATOM   1360 N ND2 . ASN   A 1 194 ? 1.385   -13.656 -6.895  1.00 93.96  ?  199 ASN   A ND2 1 
ATOM   1361 N N   . ASP   A 1 195 ? -3.525  -13.684 -4.747  1.00 80.56  ?  200 ASP   A N   1 
ATOM   1362 C CA  . ASP   A 1 195 ? -4.996  -13.647 -4.689  1.00 78.74  ?  200 ASP   A CA  1 
ATOM   1363 C C   . ASP   A 1 195 ? -5.415  -12.352 -3.986  1.00 77.10  ?  200 ASP   A C   1 
ATOM   1364 O O   . ASP   A 1 195 ? -5.733  -12.331 -2.796  1.00 90.39  ?  200 ASP   A O   1 
ATOM   1365 C CB  . ASP   A 1 195 ? -5.591  -14.905 -4.029  1.00 78.28  ?  200 ASP   A CB  1 
ATOM   1366 C CG  . ASP   A 1 195 ? -7.108  -15.054 -4.271  1.00 85.79  ?  200 ASP   A CG  1 
ATOM   1367 O OD1 . ASP   A 1 195 ? -7.819  -14.049 -4.505  1.00 86.20  ?  200 ASP   A OD1 1 
ATOM   1368 O OD2 . ASP   A 1 195 ? -7.603  -16.202 -4.233  1.00 92.31  ?  200 ASP   A OD2 1 
ATOM   1369 N N   . VAL   A 1 196 ? -5.379  -11.271 -4.756  1.00 73.96  ?  201 VAL   A N   1 
ATOM   1370 C CA  . VAL   A 1 196 ? -5.853  -9.956  -4.319  1.00 69.03  ?  201 VAL   A CA  1 
ATOM   1371 C C   . VAL   A 1 196 ? -7.359  -9.879  -4.047  1.00 74.12  ?  201 VAL   A C   1 
ATOM   1372 O O   . VAL   A 1 196 ? -7.793  -9.040  -3.261  1.00 78.41  ?  201 VAL   A O   1 
ATOM   1373 C CB  . VAL   A 1 196 ? -5.439  -8.815  -5.280  1.00 70.00  ?  201 VAL   A CB  1 
ATOM   1374 C CG1 . VAL   A 1 196 ? -3.932  -8.675  -5.324  1.00 68.42  ?  201 VAL   A CG1 1 
ATOM   1375 C CG2 . VAL   A 1 196 ? -6.007  -8.969  -6.692  1.00 75.82  ?  201 VAL   A CG2 1 
ATOM   1376 N N   . ASN   A 1 197 ? -8.148  -10.738 -4.694  1.00 82.76  ?  202 ASN   A N   1 
ATOM   1377 C CA  . ASN   A 1 197 ? -9.602  -10.835 -4.444  1.00 86.06  ?  202 ASN   A CA  1 
ATOM   1378 C C   . ASN   A 1 197 ? -9.977  -11.481 -3.097  1.00 82.07  ?  202 ASN   A C   1 
ATOM   1379 O O   . ASN   A 1 197 ? -11.080 -11.248 -2.605  1.00 83.37  ?  202 ASN   A O   1 
ATOM   1380 C CB  . ASN   A 1 197 ? -10.305 -11.606 -5.577  1.00 93.32  ?  202 ASN   A CB  1 
ATOM   1381 C CG  . ASN   A 1 197 ? -10.080 -10.989 -6.954  1.00 97.98  ?  202 ASN   A CG  1 
ATOM   1382 O OD1 . ASN   A 1 197 ? -9.774  -9.798  -7.084  1.00 95.66  ?  202 ASN   A OD1 1 
ATOM   1383 N ND2 . ASN   A 1 197 ? -10.219 -11.809 -7.993  1.00 101.45 ?  202 ASN   A ND2 1 
ATOM   1384 N N   . ALA   A 1 198 ? -9.090  -12.305 -2.523  1.00 82.03  ?  203 ALA   A N   1 
ATOM   1385 C CA  . ALA   A 1 198 ? -9.305  -12.963 -1.210  1.00 79.83  ?  203 ALA   A CA  1 
ATOM   1386 C C   . ALA   A 1 198 ? -9.575  -11.983 -0.059  1.00 80.82  ?  203 ALA   A C   1 
ATOM   1387 O O   . ALA   A 1 198 ? -8.771  -11.070 0.180   1.00 79.02  ?  203 ALA   A O   1 
ATOM   1388 C CB  . ALA   A 1 198 ? -8.102  -13.831 -0.851  1.00 74.67  ?  203 ALA   A CB  1 
ATOM   1389 N N   . LYS   A 1 199 ? -10.716 -12.169 0.612   1.00 85.39  ?  204 LYS   A N   1 
ATOM   1390 C CA  . LYS   A 1 199 ? -11.125 -11.326 1.743   1.00 87.01  ?  204 LYS   A CA  1 
ATOM   1391 C C   . LYS   A 1 199 ? -10.265 -11.685 2.978   1.00 81.79  ?  204 LYS   A C   1 
ATOM   1392 O O   . LYS   A 1 199 ? -10.220 -12.860 3.346   1.00 77.19  ?  204 LYS   A O   1 
ATOM   1393 C CB  . LYS   A 1 199 ? -12.616 -11.525 2.061   1.00 89.68  ?  204 LYS   A CB  1 
ATOM   1394 C CG  . LYS   A 1 199 ? -13.590 -11.647 0.919   0.00 92.88  ?  204 LYS   A CG  1 
ATOM   1395 C CD  . LYS   A 1 199 ? -15.028 -11.786 1.401   0.00 95.21  ?  204 LYS   A CD  1 
ATOM   1396 C CE  . LYS   A 1 199 ? -15.863 -12.594 0.421   0.00 99.51  ?  204 LYS   A CE  1 
ATOM   1397 N NZ  . LYS   A 1 199 ? -17.260 -12.779 0.903   0.00 102.26 ?  204 LYS   A NZ  1 
ATOM   1398 N N   . PRO   A 1 200 ? -9.562  -10.697 3.594   1.00 76.72  ?  205 PRO   A N   1 
ATOM   1399 C CA  . PRO   A 1 200 ? -8.798  -10.962 4.830   1.00 71.18  ?  205 PRO   A CA  1 
ATOM   1400 C C   . PRO   A 1 200 ? -9.634  -11.438 6.019   1.00 68.01  ?  205 PRO   A C   1 
ATOM   1401 O O   . PRO   A 1 200 ? -10.815 -11.090 6.119   1.00 75.86  ?  205 PRO   A O   1 
ATOM   1402 C CB  . PRO   A 1 200 ? -8.174  -9.602  5.143   1.00 75.56  ?  205 PRO   A CB  1 
ATOM   1403 C CG  . PRO   A 1 200 ? -8.058  -8.939  3.820   1.00 76.99  ?  205 PRO   A CG  1 
ATOM   1404 C CD  . PRO   A 1 200 ? -9.306  -9.327  3.107   1.00 78.16  ?  205 PRO   A CD  1 
ATOM   1405 N N   . THR   A 1 201 ? -9.014  -12.235 6.892   1.00 67.61  ?  206 THR   A N   1 
ATOM   1406 C CA  . THR   A 1 201 ? -9.650  -12.775 8.116   1.00 68.52  ?  206 THR   A CA  1 
ATOM   1407 C C   . THR   A 1 201 ? -8.765  -12.434 9.295   1.00 58.98  ?  206 THR   A C   1 
ATOM   1408 O O   . THR   A 1 201 ? -7.677  -11.917 9.119   1.00 57.17  ?  206 THR   A O   1 
ATOM   1409 C CB  . THR   A 1 201 ? -9.853  -14.311 8.058   1.00 68.47  ?  206 THR   A CB  1 
ATOM   1410 O OG1 . THR   A 1 201 ? -8.586  -14.971 8.046   1.00 79.56  ?  206 THR   A OG1 1 
ATOM   1411 C CG2 . THR   A 1 201 ? -10.631 -14.714 6.831   1.00 72.37  ?  206 THR   A CG2 1 
ATOM   1412 N N   . GLU   A 1 202 ? -9.229  -12.756 10.495  1.00 63.87  ?  207 GLU   A N   1 
ATOM   1413 C CA  . GLU   A 1 202 ? -8.388  -12.675 11.716  1.00 64.17  ?  207 GLU   A CA  1 
ATOM   1414 C C   . GLU   A 1 202 ? -7.082  -13.473 11.582  1.00 62.39  ?  207 GLU   A C   1 
ATOM   1415 O O   . GLU   A 1 202 ? -6.029  -13.026 12.029  1.00 70.63  ?  207 GLU   A O   1 
ATOM   1416 C CB  . GLU   A 1 202 ? -9.165  -13.124 12.959  1.00 69.66  ?  207 GLU   A CB  1 
ATOM   1417 C CG  . GLU   A 1 202 ? -10.309 -12.171 13.343  1.00 81.43  ?  207 GLU   A CG  1 
ATOM   1418 C CD  . GLU   A 1 202 ? -11.069 -12.552 14.606  1.00 96.55  ?  207 GLU   A CD  1 
ATOM   1419 O OE1 . GLU   A 1 202 ? -10.513 -13.242 15.496  1.00 117.98 ?  207 GLU   A OE1 1 
ATOM   1420 O OE2 . GLU   A 1 202 ? -12.243 -12.134 14.717  1.00 102.76 ?  207 GLU   A OE2 1 
ATOM   1421 N N   . LYS   A 1 203 ? -7.152  -14.620 10.912  1.00 65.26  ?  208 LYS   A N   1 
ATOM   1422 C CA  . LYS   A 1 203 ? -5.995  -15.508 10.716  1.00 62.83  ?  208 LYS   A CA  1 
ATOM   1423 C C   . LYS   A 1 203 ? -4.931  -14.915 9.777   1.00 59.13  ?  208 LYS   A C   1 
ATOM   1424 O O   . LYS   A 1 203 ? -3.753  -15.272 9.886   1.00 62.44  ?  208 LYS   A O   1 
ATOM   1425 C CB  . LYS   A 1 203 ? -6.442  -16.889 10.199  1.00 65.13  ?  208 LYS   A CB  1 
ATOM   1426 C CG  . LYS   A 1 203 ? -7.512  -17.599 11.029  1.00 68.61  ?  208 LYS   A CG  1 
ATOM   1427 C CD  . LYS   A 1 203 ? -7.078  -17.865 12.464  1.00 73.10  ?  208 LYS   A CD  1 
ATOM   1428 C CE  . LYS   A 1 203 ? -8.071  -18.778 13.179  1.00 77.41  ?  208 LYS   A CE  1 
ATOM   1429 N NZ  . LYS   A 1 203 ? -8.078  -20.140 12.806  0.00 73.92  ?  208 LYS   A NZ  1 
ATOM   1430 N N   . SER   A 1 204 ? -5.335  -14.028 8.868   1.00 55.88  ?  209 SER   A N   1 
ATOM   1431 C CA  . SER   A 1 204 ? -4.393  -13.210 8.082   1.00 58.04  ?  209 SER   A CA  1 
ATOM   1432 C C   . SER   A 1 204 ? -3.429  -12.418 8.945   1.00 57.13  ?  209 SER   A C   1 
ATOM   1433 O O   . SER   A 1 204 ? -2.227  -12.421 8.693   1.00 61.37  ?  209 SER   A O   1 
ATOM   1434 C CB  . SER   A 1 204 ? -5.144  -12.233 7.179   1.00 60.66  ?  209 SER   A CB  1 
ATOM   1435 O OG  . SER   A 1 204 ? -6.195  -12.890 6.467   1.00 63.23  ?  209 SER   A OG  1 
ATOM   1436 N N   . ASP   A 1 205 ? -3.969  -11.751 9.965   1.00 64.62  ?  210 ASP   A N   1 
ATOM   1437 C CA  . ASP   A 1 205 ? -3.149  -11.007 10.953  1.00 60.60  ?  210 ASP   A CA  1 
ATOM   1438 C C   . ASP   A 1 205 ? -2.295  -11.880 11.851  1.00 51.60  ?  210 ASP   A C   1 
ATOM   1439 O O   . ASP   A 1 205 ? -1.226  -11.453 12.299  1.00 50.93  ?  210 ASP   A O   1 
ATOM   1440 C CB  . ASP   A 1 205 ? -4.024  -10.126 11.845  1.00 59.27  ?  210 ASP   A CB  1 
ATOM   1441 C CG  . ASP   A 1 205 ? -4.735  -9.032  11.083  1.00 61.42  ?  210 ASP   A CG  1 
ATOM   1442 O OD1 . ASP   A 1 205 ? -4.338  -8.649  9.957   1.00 61.22  ?  210 ASP   A OD1 1 
ATOM   1443 O OD2 . ASP   A 1 205 ? -5.727  -8.535  11.634  1.00 60.61  ?  210 ASP   A OD2 1 
ATOM   1444 N N   . VAL   A 1 206 ? -2.777  -13.083 12.135  1.00 50.56  ?  211 VAL   A N   1 
ATOM   1445 C CA  . VAL   A 1 206 ? -2.013  -14.055 12.930  1.00 49.37  ?  211 VAL   A CA  1 
ATOM   1446 C C   . VAL   A 1 206 ? -0.752  -14.511 12.192  1.00 47.31  ?  211 VAL   A C   1 
ATOM   1447 O O   . VAL   A 1 206 ? 0.301   -14.616 12.815  1.00 47.45  ?  211 VAL   A O   1 
ATOM   1448 C CB  . VAL   A 1 206 ? -2.904  -15.214 13.387  1.00 49.47  ?  211 VAL   A CB  1 
ATOM   1449 C CG1 . VAL   A 1 206 ? -2.098  -16.338 14.047  1.00 53.01  ?  211 VAL   A CG1 1 
ATOM   1450 C CG2 . VAL   A 1 206 ? -3.939  -14.665 14.370  1.00 48.28  ?  211 VAL   A CG2 1 
ATOM   1451 N N   . TYR   A 1 207 ? -0.861  -14.753 10.882  1.00 48.87  ?  212 TYR   A N   1 
ATOM   1452 C CA  . TYR   A 1 207 ? 0.314   -15.020 10.041  1.00 51.78  ?  212 TYR   A CA  1 
ATOM   1453 C C   . TYR   A 1 207 ? 1.348   -13.918 10.184  1.00 54.39  ?  212 TYR   A C   1 
ATOM   1454 O O   . TYR   A 1 207 ? 2.522   -14.189 10.407  1.00 62.40  ?  212 TYR   A O   1 
ATOM   1455 C CB  . TYR   A 1 207 ? -0.048  -15.188 8.560   1.00 54.66  ?  212 TYR   A CB  1 
ATOM   1456 C CG  . TYR   A 1 207 ? 1.154   -15.614 7.740   1.00 56.69  ?  212 TYR   A CG  1 
ATOM   1457 C CD1 . TYR   A 1 207 ? 2.068   -14.656 7.239   1.00 58.01  ?  212 TYR   A CD1 1 
ATOM   1458 C CD2 . TYR   A 1 207 ? 1.427   -16.973 7.504   1.00 55.00  ?  212 TYR   A CD2 1 
ATOM   1459 C CE1 . TYR   A 1 207 ? 3.198   -15.037 6.528   1.00 58.28  ?  212 TYR   A CE1 1 
ATOM   1460 C CE2 . TYR   A 1 207 ? 2.555   -17.361 6.775   1.00 56.43  ?  212 TYR   A CE2 1 
ATOM   1461 C CZ  . TYR   A 1 207 ? 3.441   -16.392 6.290   1.00 57.84  ?  212 TYR   A CZ  1 
ATOM   1462 O OH  . TYR   A 1 207 ? 4.553   -16.746 5.567   1.00 58.25  ?  212 TYR   A OH  1 
ATOM   1463 N N   . SER   A 1 208 ? 0.897   -12.683 10.033  1.00 57.07  ?  213 SER   A N   1 
ATOM   1464 C CA  . SER   A 1 208 ? 1.763   -11.508 10.156  1.00 55.75  ?  213 SER   A CA  1 
ATOM   1465 C C   . SER   A 1 208 ? 2.466   -11.453 11.506  1.00 51.38  ?  213 SER   A C   1 
ATOM   1466 O O   . SER   A 1 208 ? 3.676   -11.265 11.560  1.00 50.57  ?  213 SER   A O   1 
ATOM   1467 C CB  . SER   A 1 208 ? 0.959   -10.228 9.906   1.00 60.78  ?  213 SER   A CB  1 
ATOM   1468 O OG  . SER   A 1 208 ? 0.099   -10.365 8.782   1.00 55.57  ?  213 SER   A OG  1 
ATOM   1469 N N   . PHE   A 1 209 ? 1.705   -11.684 12.577  1.00 51.58  ?  214 PHE   A N   1 
ATOM   1470 C CA  . PHE   A 1 209 ? 2.258   -11.803 13.941  1.00 50.54  ?  214 PHE   A CA  1 
ATOM   1471 C C   . PHE   A 1 209 ? 3.379   -12.853 14.057  1.00 55.20  ?  214 PHE   A C   1 
ATOM   1472 O O   . PHE   A 1 209 ? 4.367   -12.621 14.752  1.00 62.52  ?  214 PHE   A O   1 
ATOM   1473 C CB  . PHE   A 1 209 ? 1.125   -12.054 14.957  1.00 52.77  ?  214 PHE   A CB  1 
ATOM   1474 C CG  . PHE   A 1 209 ? 1.594   -12.477 16.330  1.00 56.37  ?  214 PHE   A CG  1 
ATOM   1475 C CD1 . PHE   A 1 209 ? 2.151   -11.552 17.220  1.00 53.39  ?  214 PHE   A CD1 1 
ATOM   1476 C CD2 . PHE   A 1 209 ? 1.501   -13.817 16.724  1.00 60.22  ?  214 PHE   A CD2 1 
ATOM   1477 C CE1 . PHE   A 1 209 ? 2.595   -11.954 18.479  1.00 58.42  ?  214 PHE   A CE1 1 
ATOM   1478 C CE2 . PHE   A 1 209 ? 1.935   -14.219 17.985  1.00 63.10  ?  214 PHE   A CE2 1 
ATOM   1479 C CZ  . PHE   A 1 209 ? 2.488   -13.287 18.863  1.00 61.43  ?  214 PHE   A CZ  1 
ATOM   1480 N N   . ALA   A 1 210 ? 3.232   -13.990 13.375  1.00 57.98  ?  215 ALA   A N   1 
ATOM   1481 C CA  . ALA   A 1 210 ? 4.297   -15.025 13.317  1.00 57.19  ?  215 ALA   A CA  1 
ATOM   1482 C C   . ALA   A 1 210 ? 5.623   -14.495 12.791  1.00 54.51  ?  215 ALA   A C   1 
ATOM   1483 O O   . ALA   A 1 210 ? 6.679   -14.797 13.349  1.00 55.41  ?  215 ALA   A O   1 
ATOM   1484 C CB  . ALA   A 1 210 ? 3.870   -16.210 12.477  1.00 55.62  ?  215 ALA   A CB  1 
ATOM   1485 N N   . VAL   A 1 211 ? 5.559   -13.695 11.731  1.00 51.52  ?  216 VAL   A N   1 
ATOM   1486 C CA  . VAL   A 1 211 ? 6.776   -13.157 11.110  1.00 53.20  ?  216 VAL   A CA  1 
ATOM   1487 C C   . VAL   A 1 211 ? 7.314   -12.001 11.969  1.00 53.22  ?  216 VAL   A C   1 
ATOM   1488 O O   . VAL   A 1 211 ? 8.516   -11.813 12.053  1.00 54.56  ?  216 VAL   A O   1 
ATOM   1489 C CB  . VAL   A 1 211 ? 6.565   -12.768 9.625   1.00 52.85  ?  216 VAL   A CB  1 
ATOM   1490 C CG1 . VAL   A 1 211 ? 7.890   -12.369 8.972   1.00 51.66  ?  216 VAL   A CG1 1 
ATOM   1491 C CG2 . VAL   A 1 211 ? 5.962   -13.929 8.835   1.00 54.08  ?  216 VAL   A CG2 1 
ATOM   1492 N N   . VAL   A 1 212 ? 6.423   -11.246 12.611  1.00 55.68  ?  217 VAL   A N   1 
ATOM   1493 C CA  . VAL   A 1 212 ? 6.810   -10.243 13.624  1.00 51.34  ?  217 VAL   A CA  1 
ATOM   1494 C C   . VAL   A 1 212 ? 7.546   -10.913 14.795  1.00 53.81  ?  217 VAL   A C   1 
ATOM   1495 O O   . VAL   A 1 212 ? 8.555   -10.395 15.262  1.00 61.33  ?  217 VAL   A O   1 
ATOM   1496 C CB  . VAL   A 1 212 ? 5.590   -9.418  14.111  1.00 47.70  ?  217 VAL   A CB  1 
ATOM   1497 C CG1 . VAL   A 1 212 ? 5.946   -8.500  15.270  1.00 50.86  ?  217 VAL   A CG1 1 
ATOM   1498 C CG2 . VAL   A 1 212 ? 5.045   -8.563  12.979  1.00 48.44  ?  217 VAL   A CG2 1 
ATOM   1499 N N   . LEU   A 1 213 ? 7.033   -12.051 15.251  1.00 53.17  ?  218 LEU   A N   1 
ATOM   1500 C CA  . LEU   A 1 213 ? 7.706   -12.880 16.278  1.00 54.42  ?  218 LEU   A CA  1 
ATOM   1501 C C   . LEU   A 1 213 ? 9.113   -13.255 15.848  1.00 55.91  ?  218 LEU   A C   1 
ATOM   1502 O O   . LEU   A 1 213 ? 10.049  -13.139 16.630  1.00 57.31  ?  218 LEU   A O   1 
ATOM   1503 C CB  . LEU   A 1 213 ? 6.925   -14.160 16.591  1.00 56.07  ?  218 LEU   A CB  1 
ATOM   1504 C CG  . LEU   A 1 213 ? 5.853   -14.140 17.674  1.00 64.25  ?  218 LEU   A CG  1 
ATOM   1505 C CD1 . LEU   A 1 213 ? 5.139   -15.481 17.688  1.00 74.81  ?  218 LEU   A CD1 1 
ATOM   1506 C CD2 . LEU   A 1 213 ? 6.458   -13.856 19.037  1.00 72.79  ?  218 LEU   A CD2 1 
ATOM   1507 N N   . TRP   A 1 214 ? 9.244   -13.689 14.598  1.00 57.34  ?  219 TRP   A N   1 
ATOM   1508 C CA  . TRP   A 1 214 ? 10.547  -13.984 14.012  1.00 63.44  ?  219 TRP   A CA  1 
ATOM   1509 C C   . TRP   A 1 214 ? 11.470  -12.757 14.003  1.00 63.65  ?  219 TRP   A C   1 
ATOM   1510 O O   . TRP   A 1 214 ? 12.623  -12.847 14.439  1.00 69.69  ?  219 TRP   A O   1 
ATOM   1511 C CB  . TRP   A 1 214 ? 10.401  -14.566 12.596  1.00 66.82  ?  219 TRP   A CB  1 
ATOM   1512 C CG  . TRP   A 1 214 ? 11.692  -15.029 12.039  1.00 69.91  ?  219 TRP   A CG  1 
ATOM   1513 C CD1 . TRP   A 1 214 ? 12.227  -16.273 12.160  1.00 70.80  ?  219 TRP   A CD1 1 
ATOM   1514 C CD2 . TRP   A 1 214 ? 12.652  -14.238 11.317  1.00 68.59  ?  219 TRP   A CD2 1 
ATOM   1515 N NE1 . TRP   A 1 214 ? 13.450  -16.318 11.546  1.00 72.00  ?  219 TRP   A NE1 1 
ATOM   1516 C CE2 . TRP   A 1 214 ? 13.745  -15.088 11.023  1.00 70.00  ?  219 TRP   A CE2 1 
ATOM   1517 C CE3 . TRP   A 1 214 ? 12.697  -12.893 10.898  1.00 64.71  ?  219 TRP   A CE3 1 
ATOM   1518 C CZ2 . TRP   A 1 214 ? 14.875  -14.648 10.312  1.00 72.97  ?  219 TRP   A CZ2 1 
ATOM   1519 C CZ3 . TRP   A 1 214 ? 13.828  -12.443 10.192  1.00 68.24  ?  219 TRP   A CZ3 1 
ATOM   1520 C CH2 . TRP   A 1 214 ? 14.900  -13.326 9.900   1.00 72.47  ?  219 TRP   A CH2 1 
ATOM   1521 N N   . ALA   A 1 215 ? 10.951  -11.643 13.493  1.00 58.31  ?  220 ALA   A N   1 
ATOM   1522 C CA  . ALA   A 1 215 ? 11.677  -10.360 13.405  1.00 59.82  ?  220 ALA   A CA  1 
ATOM   1523 C C   . ALA   A 1 215 ? 12.234  -9.882  14.742  1.00 60.73  ?  220 ALA   A C   1 
ATOM   1524 O O   . ALA   A 1 215 ? 13.397  -9.474  14.811  1.00 62.08  ?  220 ALA   A O   1 
ATOM   1525 C CB  . ALA   A 1 215 ? 10.776  -9.282  12.811  1.00 59.25  ?  220 ALA   A CB  1 
ATOM   1526 N N   . ILE   A 1 216 ? 11.401  -9.974  15.785  1.00 61.80  ?  221 ILE   A N   1 
ATOM   1527 C CA  . ILE   A 1 216 ? 11.761  -9.596  17.167  1.00 60.72  ?  221 ILE   A CA  1 
ATOM   1528 C C   . ILE   A 1 216 ? 13.025  -10.301 17.668  1.00 59.90  ?  221 ILE   A C   1 
ATOM   1529 O O   . ILE   A 1 216 ? 13.874  -9.663  18.307  1.00 65.85  ?  221 ILE   A O   1 
ATOM   1530 C CB  . ILE   A 1 216 ? 10.551  -9.791  18.137  1.00 60.77  ?  221 ILE   A CB  1 
ATOM   1531 C CG1 . ILE   A 1 216 ? 9.493   -8.708  17.872  1.00 60.96  ?  221 ILE   A CG1 1 
ATOM   1532 C CG2 . ILE   A 1 216 ? 10.944  -9.681  19.609  1.00 65.61  ?  221 ILE   A CG2 1 
ATOM   1533 C CD1 . ILE   A 1 216 ? 8.089   -9.101  18.278  1.00 60.77  ?  221 ILE   A CD1 1 
ATOM   1534 N N   . PHE   A 1 217 ? 13.146  -11.597 17.379  1.00 59.36  ?  222 PHE   A N   1 
ATOM   1535 C CA  . PHE   A 1 217 ? 14.312  -12.395 17.797  1.00 62.80  ?  222 PHE   A CA  1 
ATOM   1536 C C   . PHE   A 1 217 ? 15.464  -12.425 16.793  1.00 62.28  ?  222 PHE   A C   1 
ATOM   1537 O O   . PHE   A 1 217 ? 16.616  -12.465 17.201  1.00 67.57  ?  222 PHE   A O   1 
ATOM   1538 C CB  . PHE   A 1 217 ? 13.852  -13.789 18.201  1.00 66.35  ?  222 PHE   A CB  1 
ATOM   1539 C CG  . PHE   A 1 217 ? 13.139  -13.795 19.509  1.00 68.85  ?  222 PHE   A CG  1 
ATOM   1540 C CD1 . PHE   A 1 217 ? 13.876  -13.751 20.692  1.00 78.44  ?  222 PHE   A CD1 1 
ATOM   1541 C CD2 . PHE   A 1 217 ? 11.744  -13.773 19.584  1.00 65.52  ?  222 PHE   A CD2 1 
ATOM   1542 C CE1 . PHE   A 1 217 ? 13.238  -13.726 21.927  1.00 77.35  ?  222 PHE   A CE1 1 
ATOM   1543 C CE2 . PHE   A 1 217 ? 11.100  -13.741 20.818  1.00 68.81  ?  222 PHE   A CE2 1 
ATOM   1544 C CZ  . PHE   A 1 217 ? 11.847  -13.725 21.995  1.00 73.40  ?  222 PHE   A CZ  1 
ATOM   1545 N N   . ALA   A 1 218 ? 15.148  -12.389 15.503  1.00 60.24  ?  223 ALA   A N   1 
ATOM   1546 C CA  . ALA   A 1 218 ? 16.161  -12.219 14.448  1.00 62.91  ?  223 ALA   A CA  1 
ATOM   1547 C C   . ALA   A 1 218 ? 16.851  -10.843 14.424  1.00 62.54  ?  223 ALA   A C   1 
ATOM   1548 O O   . ALA   A 1 218 ? 17.989  -10.750 13.953  1.00 65.98  ?  223 ALA   A O   1 
ATOM   1549 C CB  . ALA   A 1 218 ? 15.543  -12.502 13.087  1.00 62.62  ?  223 ALA   A CB  1 
ATOM   1550 N N   . ASN   A 1 219 ? 16.162  -9.801  14.913  1.00 61.85  ?  224 ASN   A N   1 
ATOM   1551 C CA  . ASN   A 1 219 ? 16.618  -8.393  14.888  1.00 63.61  ?  224 ASN   A CA  1 
ATOM   1552 C C   . ASN   A 1 219 ? 16.838  -7.836  13.465  1.00 66.21  ?  224 ASN   A C   1 
ATOM   1553 O O   . ASN   A 1 219 ? 17.711  -6.991  13.244  1.00 73.23  ?  224 ASN   A O   1 
ATOM   1554 C CB  . ASN   A 1 219 ? 17.873  -8.187  15.770  1.00 68.15  ?  224 ASN   A CB  1 
ATOM   1555 C CG  . ASN   A 1 219 ? 17.679  -8.680  17.196  1.00 70.54  ?  224 ASN   A CG  1 
ATOM   1556 O OD1 . ASN   A 1 219 ? 16.620  -8.479  17.790  1.00 70.86  ?  224 ASN   A OD1 1 
ATOM   1557 N ND2 . ASN   A 1 219 ? 18.708  -9.291  17.769  1.00 75.45  ?  224 ASN   A ND2 1 
ATOM   1558 N N   . LYS   A 1 220 ? 16.027  -8.296  12.513  1.00 64.80  ?  225 LYS   A N   1 
ATOM   1559 C CA  . LYS   A 1 220 ? 16.178  -7.935  11.088  1.00 68.19  ?  225 LYS   A CA  1 
ATOM   1560 C C   . LYS   A 1 220 ? 14.948  -8.345  10.294  1.00 71.34  ?  225 LYS   A C   1 
ATOM   1561 O O   . LYS   A 1 220 ? 14.106  -9.109  10.803  1.00 72.82  ?  225 LYS   A O   1 
ATOM   1562 C CB  . LYS   A 1 220 ? 17.433  -8.573  10.463  1.00 72.05  ?  225 LYS   A CB  1 
ATOM   1563 C CG  . LYS   A 1 220 ? 17.480  -10.103 10.452  1.00 73.65  ?  225 LYS   A CG  1 
ATOM   1564 C CD  . LYS   A 1 220 ? 18.843  -10.634 10.000  1.00 78.52  ?  225 LYS   A CD  1 
ATOM   1565 C CE  . LYS   A 1 220 ? 18.838  -12.155 10.028  0.00 74.17  ?  225 LYS   A CE  1 
ATOM   1566 N NZ  . LYS   A 1 220 ? 20.165  -12.735 9.678   0.00 78.78  ?  225 LYS   A NZ  1 
ATOM   1567 N N   . GLU   A 1 221 ? 14.846  -7.822  9.069   1.00 74.35  ?  226 GLU   A N   1 
ATOM   1568 C CA  . GLU   A 1 221 ? 13.757  -8.191  8.153   1.00 73.05  ?  226 GLU   A CA  1 
ATOM   1569 C C   . GLU   A 1 221 ? 14.065  -9.585  7.604   1.00 75.83  ?  226 GLU   A C   1 
ATOM   1570 O O   . GLU   A 1 221 ? 15.245  -9.910  7.424   1.00 81.38  ?  226 GLU   A O   1 
ATOM   1571 C CB  . GLU   A 1 221 ? 13.602  -7.168  7.024   1.00 75.50  ?  226 GLU   A CB  1 
ATOM   1572 C CG  . GLU   A 1 221 ? 13.119  -5.777  7.478   1.00 78.78  ?  226 GLU   A CG  1 
ATOM   1573 C CD  . GLU   A 1 221 ? 11.628  -5.682  7.856   1.00 76.74  ?  226 GLU   A CD  1 
ATOM   1574 O OE1 . GLU   A 1 221 ? 10.842  -6.589  7.511   1.00 80.80  ?  226 GLU   A OE1 1 
ATOM   1575 O OE2 . GLU   A 1 221 ? 11.232  -4.695  8.514   1.00 72.68  ?  226 GLU   A OE2 1 
ATOM   1576 N N   . PRO   A 1 222 ? 13.027  -10.421 7.373   1.00 74.26  ?  227 PRO   A N   1 
ATOM   1577 C CA  . PRO   A 1 222 ? 13.276  -11.790 6.895   1.00 80.66  ?  227 PRO   A CA  1 
ATOM   1578 C C   . PRO   A 1 222 ? 13.636  -11.904 5.414   1.00 90.02  ?  227 PRO   A C   1 
ATOM   1579 O O   . PRO   A 1 222 ? 13.535  -10.930 4.657   1.00 89.91  ?  227 PRO   A O   1 
ATOM   1580 C CB  . PRO   A 1 222 ? 11.946  -12.495 7.164   1.00 74.22  ?  227 PRO   A CB  1 
ATOM   1581 C CG  . PRO   A 1 222 ? 10.962  -11.416 6.972   1.00 72.26  ?  227 PRO   A CG  1 
ATOM   1582 C CD  . PRO   A 1 222 ? 11.586  -10.191 7.571   1.00 69.54  ?  227 PRO   A CD  1 
ATOM   1583 N N   . TYR   A 1 223 ? 14.073  -13.113 5.047   1.00 93.57  ?  228 TYR   A N   1 
ATOM   1584 C CA  . TYR   A 1 223 ? 14.435  -13.498 3.671   1.00 89.69  ?  228 TYR   A CA  1 
ATOM   1585 C C   . TYR   A 1 223 ? 15.630  -12.725 3.074   1.00 98.19  ?  228 TYR   A C   1 
ATOM   1586 O O   . TYR   A 1 223 ? 15.670  -12.462 1.871   1.00 109.19 ?  228 TYR   A O   1 
ATOM   1587 C CB  . TYR   A 1 223 ? 13.212  -13.415 2.749   1.00 81.48  ?  228 TYR   A CB  1 
ATOM   1588 C CG  . TYR   A 1 223 ? 11.974  -14.128 3.257   1.00 75.46  ?  228 TYR   A CG  1 
ATOM   1589 C CD1 . TYR   A 1 223 ? 11.926  -15.522 3.325   1.00 71.47  ?  228 TYR   A CD1 1 
ATOM   1590 C CD2 . TYR   A 1 223 ? 10.829  -13.409 3.647   1.00 74.94  ?  228 TYR   A CD2 1 
ATOM   1591 C CE1 . TYR   A 1 223 ? 10.782  -16.187 3.772   1.00 69.93  ?  228 TYR   A CE1 1 
ATOM   1592 C CE2 . TYR   A 1 223 ? 9.676   -14.066 4.094   1.00 70.89  ?  228 TYR   A CE2 1 
ATOM   1593 C CZ  . TYR   A 1 223 ? 9.654   -15.454 4.157   1.00 68.84  ?  228 TYR   A CZ  1 
ATOM   1594 O OH  . TYR   A 1 223 ? 8.516   -16.097 4.595   1.00 64.37  ?  228 TYR   A OH  1 
ATOM   1595 N N   . GLU   A 1 224 ? 16.585  -12.352 3.933   1.00 106.85 ?  229 GLU   A N   1 
ATOM   1596 C CA  . GLU   A 1 224 ? 17.811  -11.624 3.542   1.00 105.47 ?  229 GLU   A CA  1 
ATOM   1597 C C   . GLU   A 1 224 ? 17.569  -10.290 2.789   1.00 108.32 ?  229 GLU   A C   1 
ATOM   1598 O O   . GLU   A 1 224 ? 18.404  -9.875  1.982   1.00 112.30 ?  229 GLU   A O   1 
ATOM   1599 C CB  . GLU   A 1 224 ? 18.732  -12.562 2.735   1.00 98.39  ?  229 GLU   A CB  1 
ATOM   1600 C CG  . GLU   A 1 224 ? 19.119  -13.892 3.412   0.00 106.95 ?  229 GLU   A CG  1 
ATOM   1601 C CD  . GLU   A 1 224 ? 20.230  -13.797 4.457   0.00 108.16 ?  229 GLU   A CD  1 
ATOM   1602 O OE1 . GLU   A 1 224 ? 20.891  -14.831 4.693   0.00 110.55 ?  229 GLU   A OE1 1 
ATOM   1603 O OE2 . GLU   A 1 224 ? 20.457  -12.717 5.046   0.00 106.98 ?  229 GLU   A OE2 1 
ATOM   1604 N N   . ASN   A 1 225 ? 16.442  -9.614  3.073   1.00 109.66 ?  230 ASN   A N   1 
ATOM   1605 C CA  . ASN   A 1 225 ? 15.933  -8.445  2.322   1.00 113.08 ?  230 ASN   A CA  1 
ATOM   1606 C C   . ASN   A 1 225 ? 15.784  -8.632  0.771   1.00 122.50 ?  230 ASN   A C   1 
ATOM   1607 O O   . ASN   A 1 225 ? 15.955  -7.684  -0.014  1.00 126.96 ?  230 ASN   A O   1 
ATOM   1608 C CB  . ASN   A 1 225 ? 16.738  -7.186  2.713   1.00 111.76 ?  230 ASN   A CB  1 
ATOM   1609 C CG  . ASN   A 1 225 ? 16.194  -6.611  4.036   0.00 111.53 ?  230 ASN   A CG  1 
ATOM   1610 O OD1 . ASN   A 1 225 ? 16.850  -6.744  5.070   0.00 111.60 ?  230 ASN   A OD1 1 
ATOM   1611 N ND2 . ASN   A 1 225 ? 15.025  -5.974  4.004   0.00 108.57 ?  230 ASN   A ND2 1 
ATOM   1612 N N   . ALA   A 1 226 ? 15.470  -9.869  0.365   1.00 124.52 ?  231 ALA   A N   1 
ATOM   1613 C CA  . ALA   A 1 226 ? 15.352  -10.230 -1.063  1.00 114.78 ?  231 ALA   A CA  1 
ATOM   1614 C C   . ALA   A 1 226 ? 14.103  -9.589  -1.681  1.00 110.55 ?  231 ALA   A C   1 
ATOM   1615 O O   . ALA   A 1 226 ? 13.040  -9.604  -1.052  1.00 92.59  ?  231 ALA   A O   1 
ATOM   1616 C CB  . ALA   A 1 226 ? 15.301  -11.746 -1.237  1.00 104.27 ?  231 ALA   A CB  1 
ATOM   1617 N N   . ILE   A 1 227 ? 14.233  -9.035  -2.900  1.00 116.10 ?  232 ILE   A N   1 
ATOM   1618 C CA  . ILE   A 1 227 ? 13.110  -8.391  -3.622  1.00 116.90 ?  232 ILE   A CA  1 
ATOM   1619 C C   . ILE   A 1 227 ? 11.958  -9.377  -3.810  1.00 123.80 ?  232 ILE   A C   1 
ATOM   1620 O O   . ILE   A 1 227 ? 12.189  -10.557 -4.118  1.00 132.20 ?  232 ILE   A O   1 
ATOM   1621 C CB  . ILE   A 1 227 ? 13.522  -7.845  -5.008  1.00 112.65 ?  232 ILE   A CB  1 
ATOM   1622 C CG1 . ILE   A 1 227 ? 14.798  -7.080  -5.051  0.00 123.21 ?  232 ILE   A CG1 1 
ATOM   1623 C CG2 . ILE   A 1 227 ? 12.404  -7.046  -5.636  0.00 119.33 ?  232 ILE   A CG2 1 
ATOM   1624 C CD1 . ILE   A 1 227 ? 15.325  -6.850  -6.452  0.00 128.58 ?  232 ILE   A CD1 1 
ATOM   1625 N N   . ALA   A 1 228 ? 10.729  -8.901  -3.602  1.00 127.58 ?  233 ALA   A N   1 
ATOM   1626 C CA  . ALA   A 1 228 ? 9.540   -9.776  -3.503  1.00 121.61 ?  233 ALA   A CA  1 
ATOM   1627 C C   . ALA   A 1 228 ? 9.086   -10.311 -4.879  1.00 124.61 ?  233 ALA   A C   1 
ATOM   1628 O O   . ALA   A 1 228 ? 7.981   -10.040 -5.373  1.00 123.94 ?  233 ALA   A O   1 
ATOM   1629 C CB  . ALA   A 1 228 ? 8.411   -9.070  -2.760  1.00 116.22 ?  233 ALA   A CB  1 
ATOM   1630 N N   . GLU   A 1 229 ? 9.956   -11.138 -5.450  1.00 121.42 ?  234 GLU   A N   1 
ATOM   1631 C CA  . GLU   A 1 229 ? 9.832   -11.634 -6.808  1.00 118.36 ?  234 GLU   A CA  1 
ATOM   1632 C C   . GLU   A 1 229 ? 8.941   -12.866 -6.783  1.00 109.85 ?  234 GLU   A C   1 
ATOM   1633 O O   . GLU   A 1 229 ? 8.620   -13.396 -5.712  1.00 105.04 ?  234 GLU   A O   1 
ATOM   1634 C CB  . GLU   A 1 229 ? 11.219  -11.983 -7.365  1.00 128.09 ?  234 GLU   A CB  1 
ATOM   1635 C CG  . GLU   A 1 229 ? 12.075  -10.695 -7.683  0.00 132.28 ?  234 GLU   A CG  1 
ATOM   1636 C CD  . GLU   A 1 229 ? 11.527  -9.729  -8.738  0.00 134.01 ?  234 GLU   A CD  1 
ATOM   1637 O OE1 . GLU   A 1 229 ? 10.864  -10.159 -9.719  0.00 135.76 ?  234 GLU   A OE1 1 
ATOM   1638 O OE2 . GLU   A 1 229 ? 11.778  -8.509  -8.585  0.00 133.73 ?  234 GLU   A OE2 1 
ATOM   1639 N N   . GLN   A 1 230 ? 8.574   -13.324 -7.976  1.00 107.63 ?  235 GLN   A N   1 
ATOM   1640 C CA  . GLN   A 1 230 ? 7.726   -14.499 -8.149  1.00 107.14 ?  235 GLN   A CA  1 
ATOM   1641 C C   . GLN   A 1 230 ? 8.342   -15.786 -7.589  1.00 102.84 ?  235 GLN   A C   1 
ATOM   1642 O O   . GLN   A 1 230 ? 7.602   -16.630 -7.108  1.00 99.76  ?  235 GLN   A O   1 
ATOM   1643 C CB  . GLN   A 1 230 ? 7.347   -14.690 -9.632  1.00 114.94 ?  235 GLN   A CB  1 
ATOM   1644 C CG  . GLN   A 1 230 ? 6.039   -15.448 -9.873  1.00 114.99 ?  235 GLN   A CG  1 
ATOM   1645 C CD  . GLN   A 1 230 ? 4.784   -14.655 -9.499  1.00 106.24 ?  235 GLN   A CD  1 
ATOM   1646 O OE1 . GLN   A 1 230 ? 4.180   -14.920 -8.467  1.00 92.47  ?  235 GLN   A OE1 1 
ATOM   1647 N NE2 . GLN   A 1 230 ? 4.391   -13.684 -10.336 1.00 109.04 ?  235 GLN   A NE2 1 
ATOM   1648 N N   . GLN   A 1 231 ? 9.668   -15.940 -7.666  1.00 102.86 ?  236 GLN   A N   1 
ATOM   1649 C CA  . GLN   A 1 231 ? 10.367  -17.077 -7.030  1.00 105.75 ?  236 GLN   A CA  1 
ATOM   1650 C C   . GLN   A 1 231 ? 10.112  -17.115 -5.521  1.00 102.30 ?  236 GLN   A C   1 
ATOM   1651 O O   . GLN   A 1 231 ? 9.754   -18.166 -4.975  1.00 109.91 ?  236 GLN   A O   1 
ATOM   1652 C CB  . GLN   A 1 231 ? 11.870  -17.027 -7.294  1.00 105.74 ?  236 GLN   A CB  1 
ATOM   1653 C CG  . GLN   A 1 231 ? 12.257  -17.344 -8.701  0.00 110.36 ?  236 GLN   A CG  1 
ATOM   1654 C CD  . GLN   A 1 231 ? 13.759  -17.492 -8.911  0.00 114.17 ?  236 GLN   A CD  1 
ATOM   1655 O OE1 . GLN   A 1 231 ? 14.575  -17.067 -8.087  0.00 112.73 ?  236 GLN   A OE1 1 
ATOM   1656 N NE2 . GLN   A 1 231 ? 14.131  -18.096 -10.035 0.00 119.39 ?  236 GLN   A NE2 1 
ATOM   1657 N N   . LEU   A 1 232 ? 10.269  -15.963 -4.868  1.00 96.70  ?  237 LEU   A N   1 
ATOM   1658 C CA  . LEU   A 1 232 ? 10.037  -15.852 -3.419  1.00 93.60  ?  237 LEU   A CA  1 
ATOM   1659 C C   . LEU   A 1 232 ? 8.562   -16.049 -3.076  1.00 95.85  ?  237 LEU   A C   1 
ATOM   1660 O O   . LEU   A 1 232 ? 8.236   -16.849 -2.187  1.00 96.53  ?  237 LEU   A O   1 
ATOM   1661 C CB  . LEU   A 1 232 ? 10.529  -14.503 -2.865  1.00 90.79  ?  237 LEU   A CB  1 
ATOM   1662 C CG  . LEU   A 1 232 ? 10.391  -14.257 -1.347  1.00 86.45  ?  237 LEU   A CG  1 
ATOM   1663 C CD1 . LEU   A 1 232 ? 11.135  -15.309 -0.529  1.00 85.47  ?  237 LEU   A CD1 1 
ATOM   1664 C CD2 . LEU   A 1 232 ? 10.866  -12.863 -0.962  1.00 81.85  ?  237 LEU   A CD2 1 
ATOM   1665 N N   . ILE   A 1 233 ? 7.694   -15.316 -3.785  1.00 95.61  ?  238 ILE   A N   1 
ATOM   1666 C CA  . ILE   A 1 233 ? 6.233   -15.379 -3.600  1.00 87.33  ?  238 ILE   A CA  1 
ATOM   1667 C C   . ILE   A 1 233 ? 5.755   -16.830 -3.696  1.00 83.65  ?  238 ILE   A C   1 
ATOM   1668 O O   . ILE   A 1 233 ? 5.113   -17.322 -2.782  1.00 78.46  ?  238 ILE   A O   1 
ATOM   1669 C CB  . ILE   A 1 233 ? 5.482   -14.470 -4.615  1.00 91.53  ?  238 ILE   A CB  1 
ATOM   1670 C CG1 . ILE   A 1 233 ? 5.719   -12.980 -4.295  1.00 87.18  ?  238 ILE   A CG1 1 
ATOM   1671 C CG2 . ILE   A 1 233 ? 3.975   -14.729 -4.609  1.00 91.26  ?  238 ILE   A CG2 1 
ATOM   1672 C CD1 . ILE   A 1 233 ? 5.454   -12.018 -5.417  0.00 84.25  ?  238 ILE   A CD1 1 
ATOM   1673 N N   . MET   A 1 234 ? 6.112   -17.500 -4.785  1.00 88.41  ?  239 MET   A N   1 
ATOM   1674 C CA  . MET   A 1 234 ? 5.718   -18.910 -5.011  1.00 90.66  ?  239 MET   A CA  1 
ATOM   1675 C C   . MET   A 1 234 ? 6.376   -19.908 -4.057  1.00 87.84  ?  239 MET   A C   1 
ATOM   1676 O O   . MET   A 1 234 ? 5.784   -20.965 -3.773  1.00 92.39  ?  239 MET   A O   1 
ATOM   1677 C CB  . MET   A 1 234 ? 5.945   -19.341 -6.473  1.00 96.33  ?  239 MET   A CB  1 
ATOM   1678 C CG  . MET   A 1 234 ? 5.055   -18.613 -7.464  1.00 99.10  ?  239 MET   A CG  1 
ATOM   1679 S SD  . MET   A 1 234 ? 3.317   -19.097 -7.324  1.00 104.40 ?  239 MET   A SD  1 
ATOM   1680 C CE  . MET   A 1 234 ? 3.330   -20.643 -8.230  1.00 110.88 ?  239 MET   A CE  1 
ATOM   1681 N N   . ALA   A 1 235 ? 7.580   -19.597 -3.562  1.00 82.68  ?  240 ALA   A N   1 
ATOM   1682 C CA  . ALA   A 1 235 ? 8.213   -20.400 -2.497  1.00 78.47  ?  240 ALA   A CA  1 
ATOM   1683 C C   . ALA   A 1 235 ? 7.418   -20.339 -1.188  1.00 75.51  ?  240 ALA   A C   1 
ATOM   1684 O O   . ALA   A 1 235 ? 7.151   -21.368 -0.581  1.00 73.45  ?  240 ALA   A O   1 
ATOM   1685 C CB  . ALA   A 1 235 ? 9.652   -19.966 -2.265  1.00 76.68  ?  240 ALA   A CB  1 
ATOM   1686 N N   . ILE   A 1 236 ? 7.003   -19.134 -0.801  1.00 72.91  ?  241 ILE   A N   1 
ATOM   1687 C CA  . ILE   A 1 236 ? 6.192   -18.923 0.406   1.00 68.71  ?  241 ILE   A CA  1 
ATOM   1688 C C   . ILE   A 1 236 ? 4.830   -19.623 0.316   1.00 68.04  ?  241 ILE   A C   1 
ATOM   1689 O O   . ILE   A 1 236 ? 4.419   -20.271 1.280   1.00 63.39  ?  241 ILE   A O   1 
ATOM   1690 C CB  . ILE   A 1 236 ? 6.051   -17.415 0.749   1.00 65.41  ?  241 ILE   A CB  1 
ATOM   1691 C CG1 . ILE   A 1 236 ? 7.428   -16.831 1.156   1.00 66.13  ?  241 ILE   A CG1 1 
ATOM   1692 C CG2 . ILE   A 1 236 ? 5.047   -17.169 1.883   1.00 61.02  ?  241 ILE   A CG2 1 
ATOM   1693 C CD1 . ILE   A 1 236 ? 7.555   -15.332 0.985   1.00 68.13  ?  241 ILE   A CD1 1 
ATOM   1694 N N   . LYS   A 1 237 ? 4.161   -19.489 -0.830  1.00 68.28  ?  242 LYS   A N   1 
ATOM   1695 C CA  . LYS   A 1 237 ? 2.911   -20.226 -1.143  1.00 72.98  ?  242 LYS   A CA  1 
ATOM   1696 C C   . LYS   A 1 237 ? 3.069   -21.755 -1.007  1.00 81.34  ?  242 LYS   A C   1 
ATOM   1697 O O   . LYS   A 1 237 ? 2.188   -22.432 -0.468  1.00 82.65  ?  242 LYS   A O   1 
ATOM   1698 C CB  . LYS   A 1 237 ? 2.434   -19.916 -2.574  1.00 78.44  ?  242 LYS   A CB  1 
ATOM   1699 C CG  . LYS   A 1 237 ? 1.947   -18.506 -2.812  1.00 77.17  ?  242 LYS   A CG  1 
ATOM   1700 C CD  . LYS   A 1 237 ? 0.462   -18.376 -2.578  1.00 77.04  ?  242 LYS   A CD  1 
ATOM   1701 C CE  . LYS   A 1 237 ? -0.371  -18.772 -3.775  1.00 80.40  ?  242 LYS   A CE  1 
ATOM   1702 N NZ  . LYS   A 1 237 ? -1.743  -18.201 -3.656  1.00 83.49  ?  242 LYS   A NZ  1 
ATOM   1703 N N   . SER   A 1 238 ? 4.204   -22.278 -1.477  1.00 85.14  ?  243 SER   A N   1 
ATOM   1704 C CA  . SER   A 1 238 ? 4.526   -23.708 -1.378  1.00 91.20  ?  243 SER   A CA  1 
ATOM   1705 C C   . SER   A 1 238 ? 4.885   -24.218 0.036   1.00 92.21  ?  243 SER   A C   1 
ATOM   1706 O O   . SER   A 1 238 ? 4.952   -25.436 0.221   1.00 113.24 ?  243 SER   A O   1 
ATOM   1707 C CB  . SER   A 1 238 ? 5.646   -24.085 -2.367  1.00 94.15  ?  243 SER   A CB  1 
ATOM   1708 O OG  . SER   A 1 238 ? 6.936   -23.714 -1.905  1.00 92.64  ?  243 SER   A OG  1 
ATOM   1709 N N   . GLY   A 1 239 ? 5.116   -23.318 1.003   1.00 82.68  ?  244 GLY   A N   1 
ATOM   1710 C CA  . GLY   A 1 239 ? 5.526   -23.677 2.375   1.00 80.59  ?  244 GLY   A CA  1 
ATOM   1711 C C   . GLY   A 1 239 ? 6.720   -22.949 2.983   1.00 75.30  ?  244 GLY   A C   1 
ATOM   1712 O O   . GLY   A 1 239 ? 6.946   -23.087 4.183   1.00 68.32  ?  244 GLY   A O   1 
ATOM   1713 N N   . ASN   A 1 240 ? 7.464   -22.172 2.185   1.00 78.73  ?  245 ASN   A N   1 
ATOM   1714 C CA  . ASN   A 1 240 ? 8.727   -21.546 2.627   1.00 82.55  ?  245 ASN   A CA  1 
ATOM   1715 C C   . ASN   A 1 240 ? 8.467   -20.410 3.629   1.00 81.22  ?  245 ASN   A C   1 
ATOM   1716 O O   . ASN   A 1 240 ? 7.481   -19.684 3.516   1.00 89.09  ?  245 ASN   A O   1 
ATOM   1717 C CB  . ASN   A 1 240 ? 9.531   -21.027 1.418   1.00 90.37  ?  245 ASN   A CB  1 
ATOM   1718 C CG  . ASN   A 1 240 ? 11.019  -21.086 1.635   1.00 102.24 ?  245 ASN   A CG  1 
ATOM   1719 O OD1 . ASN   A 1 240 ? 11.664  -22.052 1.216   1.00 120.06 ?  245 ASN   A OD1 1 
ATOM   1720 N ND2 . ASN   A 1 240 ? 11.578  -20.068 2.286   1.00 95.56  ?  245 ASN   A ND2 1 
ATOM   1721 N N   . ARG   A 1 241 ? 9.336   -20.305 4.630   1.00 76.74  ?  246 ARG   A N   1 
ATOM   1722 C CA  . ARG   A 1 241 ? 9.152   -19.404 5.785   1.00 69.87  ?  246 ARG   A CA  1 
ATOM   1723 C C   . ARG   A 1 241 ? 10.490  -18.761 6.161   1.00 71.90  ?  246 ARG   A C   1 
ATOM   1724 O O   . ARG   A 1 241 ? 11.525  -19.143 5.603   1.00 74.00  ?  246 ARG   A O   1 
ATOM   1725 C CB  . ARG   A 1 241 ? 8.571   -20.193 6.973   1.00 67.12  ?  246 ARG   A CB  1 
ATOM   1726 C CG  . ARG   A 1 241 ? 7.152   -20.736 6.780   1.00 65.25  ?  246 ARG   A CG  1 
ATOM   1727 C CD  . ARG   A 1 241 ? 6.114   -19.632 6.709   1.00 60.32  ?  246 ARG   A CD  1 
ATOM   1728 N NE  . ARG   A 1 241 ? 4.776   -20.177 6.489   1.00 55.28  ?  246 ARG   A NE  1 
ATOM   1729 C CZ  . ARG   A 1 241 ? 4.204   -20.423 5.301   1.00 60.31  ?  246 ARG   A CZ  1 
ATOM   1730 N NH1 . ARG   A 1 241 ? 4.823   -20.179 4.137   1.00 59.88  ?  246 ARG   A NH1 1 
ATOM   1731 N NH2 . ARG   A 1 241 ? 2.957   -20.927 5.270   1.00 63.32  ?  246 ARG   A NH2 1 
ATOM   1732 N N   . PRO   A 1 242 ? 10.486  -17.766 7.085   1.00 77.33  ?  247 PRO   A N   1 
ATOM   1733 C CA  . PRO   A 1 242 ? 11.769  -17.193 7.519   1.00 77.91  ?  247 PRO   A CA  1 
ATOM   1734 C C   . PRO   A 1 242 ? 12.642  -18.210 8.252   1.00 83.78  ?  247 PRO   A C   1 
ATOM   1735 O O   . PRO   A 1 242 ? 12.119  -19.072 8.974   1.00 88.12  ?  247 PRO   A O   1 
ATOM   1736 C CB  . PRO   A 1 242 ? 11.347  -16.044 8.451   1.00 77.83  ?  247 PRO   A CB  1 
ATOM   1737 C CG  . PRO   A 1 242 ? 9.980   -15.689 8.009   1.00 72.61  ?  247 PRO   A CG  1 
ATOM   1738 C CD  . PRO   A 1 242 ? 9.364   -17.019 7.687   1.00 76.80  ?  247 PRO   A CD  1 
ATOM   1739 N N   . ASP   A 1 243 ? 13.955  -18.099 8.049   1.00 83.68  ?  248 ASP   A N   1 
ATOM   1740 C CA  . ASP   A 1 243 ? 14.916  -19.093 8.517   1.00 85.09  ?  248 ASP   A CA  1 
ATOM   1741 C C   . ASP   A 1 243 ? 15.051  -18.981 10.043  1.00 86.50  ?  248 ASP   A C   1 
ATOM   1742 O O   . ASP   A 1 243 ? 15.458  -17.935 10.558  1.00 84.02  ?  248 ASP   A O   1 
ATOM   1743 C CB  . ASP   A 1 243 ? 16.272  -18.865 7.821   1.00 89.72  ?  248 ASP   A CB  1 
ATOM   1744 C CG  . ASP   A 1 243 ? 17.189  -20.087 7.854   1.00 91.88  ?  248 ASP   A CG  1 
ATOM   1745 O OD1 . ASP   A 1 243 ? 16.996  -21.016 8.672   1.00 92.97  ?  248 ASP   A OD1 1 
ATOM   1746 O OD2 . ASP   A 1 243 ? 18.133  -20.106 7.035   1.00 90.01  ?  248 ASP   A OD2 1 
ATOM   1747 N N   . VAL   A 1 244 ? 14.667  -20.037 10.756  1.00 87.04  ?  249 VAL   A N   1 
ATOM   1748 C CA  . VAL   A 1 244 ? 14.709  -20.052 12.229  1.00 85.34  ?  249 VAL   A CA  1 
ATOM   1749 C C   . VAL   A 1 244 ? 16.172  -20.107 12.737  1.00 89.70  ?  249 VAL   A C   1 
ATOM   1750 O O   . VAL   A 1 244 ? 16.476  -19.533 13.787  1.00 94.17  ?  249 VAL   A O   1 
ATOM   1751 C CB  . VAL   A 1 244 ? 13.844  -21.202 12.812  1.00 86.09  ?  249 VAL   A CB  1 
ATOM   1752 C CG1 . VAL   A 1 244 ? 13.888  -21.224 14.343  1.00 88.03  ?  249 VAL   A CG1 1 
ATOM   1753 C CG2 . VAL   A 1 244 ? 12.392  -21.071 12.347  1.00 81.74  ?  249 VAL   A CG2 1 
ATOM   1754 N N   . ASP   A 1 245 ? 17.060  -20.785 11.999  1.00 89.33  ?  250 ASP   A N   1 
ATOM   1755 C CA  . ASP   A 1 245 ? 18.507  -20.807 12.299  1.00 94.48  ?  250 ASP   A CA  1 
ATOM   1756 C C   . ASP   A 1 245 ? 19.229  -19.453 12.148  1.00 95.94  ?  250 ASP   A C   1 
ATOM   1757 O O   . ASP   A 1 245 ? 20.324  -19.299 12.689  1.00 106.87 ?  250 ASP   A O   1 
ATOM   1758 C CB  . ASP   A 1 245 ? 19.229  -21.872 11.451  1.00 98.76  ?  250 ASP   A CB  1 
ATOM   1759 C CG  . ASP   A 1 245 ? 18.714  -23.302 11.681  0.00 96.57  ?  250 ASP   A CG  1 
ATOM   1760 O OD1 . ASP   A 1 245 ? 18.355  -23.652 12.826  0.00 95.69  ?  250 ASP   A OD1 1 
ATOM   1761 O OD2 . ASP   A 1 245 ? 18.670  -24.077 10.702  0.00 98.81  ?  250 ASP   A OD2 1 
ATOM   1762 N N   . ASP   A 1 246 ? 18.654  -18.499 11.402  1.00 98.28  ?  251 ASP   A N   1 
ATOM   1763 C CA  . ASP   A 1 246 ? 19.148  -17.084 11.375  1.00 101.75 ?  251 ASP   A CA  1 
ATOM   1764 C C   . ASP   A 1 246 ? 18.993  -16.332 12.710  1.00 95.31  ?  251 ASP   A C   1 
ATOM   1765 O O   . ASP   A 1 246 ? 19.690  -15.340 12.924  1.00 96.95  ?  251 ASP   A O   1 
ATOM   1766 C CB  . ASP   A 1 246 ? 18.497  -16.235 10.244  1.00 105.54 ?  251 ASP   A CB  1 
ATOM   1767 C CG  . ASP   A 1 246 ? 19.198  -16.365 8.891   1.00 111.40 ?  251 ASP   A CG  1 
ATOM   1768 O OD1 . ASP   A 1 246 ? 19.932  -17.345 8.632   1.00 124.61 ?  251 ASP   A OD1 1 
ATOM   1769 O OD2 . ASP   A 1 246 ? 18.983  -15.461 8.065   1.00 113.61 ?  251 ASP   A OD2 1 
ATOM   1770 N N   . ILE   A 1 247 ? 18.095  -16.794 13.590  1.00 89.95  ?  252 ILE   A N   1 
ATOM   1771 C CA  . ILE   A 1 247 ? 18.035  -16.312 14.985  1.00 84.88  ?  252 ILE   A CA  1 
ATOM   1772 C C   . ILE   A 1 247 ? 19.261  -16.892 15.718  1.00 88.46  ?  252 ILE   A C   1 
ATOM   1773 O O   . ILE   A 1 247 ? 19.294  -18.099 16.014  1.00 84.70  ?  252 ILE   A O   1 
ATOM   1774 C CB  . ILE   A 1 247 ? 16.715  -16.704 15.704  1.00 76.35  ?  252 ILE   A CB  1 
ATOM   1775 C CG1 . ILE   A 1 247 ? 15.512  -16.091 14.982  1.00 73.18  ?  252 ILE   A CG1 1 
ATOM   1776 C CG2 . ILE   A 1 247 ? 16.716  -16.222 17.159  1.00 72.09  ?  252 ILE   A CG2 1 
ATOM   1777 C CD1 . ILE   A 1 247 ? 14.184  -16.717 15.348  1.00 77.18  ?  252 ILE   A CD1 1 
ATOM   1778 N N   . THR   A 1 248 ? 20.248  -16.027 15.975  1.00 89.88  ?  253 THR   A N   1 
ATOM   1779 C CA  . THR   A 1 248 ? 21.492  -16.395 16.665  1.00 97.46  ?  253 THR   A CA  1 
ATOM   1780 C C   . THR   A 1 248 ? 21.376  -16.261 18.190  1.00 98.85  ?  253 THR   A C   1 
ATOM   1781 O O   . THR   A 1 248 ? 21.899  -17.107 18.921  1.00 102.12 ?  253 THR   A O   1 
ATOM   1782 C CB  . THR   A 1 248 ? 22.676  -15.555 16.158  1.00 101.64 ?  253 THR   A CB  1 
ATOM   1783 O OG1 . THR   A 1 248 ? 22.408  -14.160 16.360  1.00 96.78  ?  253 THR   A OG1 1 
ATOM   1784 C CG2 . THR   A 1 248 ? 22.919  -15.824 14.667  1.00 102.33 ?  253 THR   A CG2 1 
ATOM   1785 N N   . GLU   A 1 249 ? 20.715  -15.199 18.659  1.00 98.46  ?  254 GLU   A N   1 
ATOM   1786 C CA  . GLU   A 1 249 ? 20.412  -15.020 20.096  1.00 94.73  ?  254 GLU   A CA  1 
ATOM   1787 C C   . GLU   A 1 249 ? 19.420  -16.050 20.656  1.00 86.05  ?  254 GLU   A C   1 
ATOM   1788 O O   . GLU   A 1 249 ? 18.755  -16.749 19.904  1.00 80.10  ?  254 GLU   A O   1 
ATOM   1789 C CB  . GLU   A 1 249 ? 19.929  -13.586 20.388  1.00 91.38  ?  254 GLU   A CB  1 
ATOM   1790 C CG  . GLU   A 1 249 ? 18.582  -13.175 19.812  1.00 90.14  ?  254 GLU   A CG  1 
ATOM   1791 C CD  . GLU   A 1 249 ? 18.072  -11.871 20.409  1.00 91.57  ?  254 GLU   A CD  1 
ATOM   1792 O OE1 . GLU   A 1 249 ? 18.812  -10.859 20.372  1.00 92.13  ?  254 GLU   A OE1 1 
ATOM   1793 O OE2 . GLU   A 1 249 ? 16.924  -11.851 20.913  1.00 86.53  ?  254 GLU   A OE2 1 
ATOM   1794 N N   . TYR   A 1 250 ? 19.329  -16.107 21.987  1.00 86.92  ?  255 TYR   A N   1 
ATOM   1795 C CA  . TYR   A 1 250 ? 18.446  -17.028 22.692  1.00 87.41  ?  255 TYR   A CA  1 
ATOM   1796 C C   . TYR   A 1 250 ? 16.981  -16.658 22.502  1.00 86.33  ?  255 TYR   A C   1 
ATOM   1797 O O   . TYR   A 1 250 ? 16.510  -15.636 23.014  1.00 84.18  ?  255 TYR   A O   1 
ATOM   1798 C CB  . TYR   A 1 250 ? 18.760  -17.066 24.195  1.00 93.48  ?  255 TYR   A CB  1 
ATOM   1799 C CG  . TYR   A 1 250 ? 17.783  -17.919 24.986  1.00 99.83  ?  255 TYR   A CG  1 
ATOM   1800 C CD1 . TYR   A 1 250 ? 17.701  -19.307 24.770  1.00 107.60 ?  255 TYR   A CD1 1 
ATOM   1801 C CD2 . TYR   A 1 250 ? 16.906  -17.343 25.921  1.00 101.79 ?  255 TYR   A CD2 1 
ATOM   1802 C CE1 . TYR   A 1 250 ? 16.793  -20.100 25.476  1.00 108.48 ?  255 TYR   A CE1 1 
ATOM   1803 C CE2 . TYR   A 1 250 ? 15.993  -18.127 26.635  1.00 107.31 ?  255 TYR   A CE2 1 
ATOM   1804 C CZ  . TYR   A 1 250 ? 15.940  -19.507 26.409  1.00 111.53 ?  255 TYR   A CZ  1 
ATOM   1805 O OH  . TYR   A 1 250 ? 15.049  -20.301 27.095  1.00 116.23 ?  255 TYR   A OH  1 
ATOM   1806 N N   . CYS   A 1 251 ? 16.302  -17.481 21.714  1.00 87.69  ?  256 CYS   A N   1 
ATOM   1807 C CA  . CYS   A 1 251 ? 14.845  -17.508 21.656  1.00 82.42  ?  256 CYS   A CA  1 
ATOM   1808 C C   . CYS   A 1 251 ? 14.395  -18.789 22.363  1.00 80.44  ?  256 CYS   A C   1 
ATOM   1809 O O   . CYS   A 1 251 ? 14.938  -19.870 22.080  1.00 88.13  ?  256 CYS   A O   1 
ATOM   1810 C CB  . CYS   A 1 251 ? 14.349  -17.505 20.214  1.00 81.22  ?  256 CYS   A CB  1 
ATOM   1811 S SG  . CYS   A 1 251 ? 12.552  -17.390 20.089  1.00 77.40  ?  256 CYS   A SG  1 
ATOM   1812 N N   . PRO   A 1 252 ? 13.423  -18.692 23.301  1.00 75.85  ?  257 PRO   A N   1 
ATOM   1813 C CA  . PRO   A 1 252 ? 12.826  -19.898 23.905  1.00 76.35  ?  257 PRO   A CA  1 
ATOM   1814 C C   . PRO   A 1 252 ? 12.131  -20.846 22.926  1.00 74.21  ?  257 PRO   A C   1 
ATOM   1815 O O   . PRO   A 1 252 ? 11.703  -20.426 21.857  1.00 75.51  ?  257 PRO   A O   1 
ATOM   1816 C CB  . PRO   A 1 252 ? 11.800  -19.324 24.885  1.00 75.58  ?  257 PRO   A CB  1 
ATOM   1817 C CG  . PRO   A 1 252 ? 12.392  -18.032 25.301  1.00 78.37  ?  257 PRO   A CG  1 
ATOM   1818 C CD  . PRO   A 1 252 ? 13.060  -17.485 24.072  1.00 76.16  ?  257 PRO   A CD  1 
ATOM   1819 N N   . ARG   A 1 253 ? 12.034  -22.115 23.322  1.00 78.59  ?  258 ARG   A N   1 
ATOM   1820 C CA  . ARG   A 1 253 ? 11.353  -23.167 22.551  1.00 79.39  ?  258 ARG   A CA  1 
ATOM   1821 C C   . ARG   A 1 253 ? 9.863   -22.871 22.323  1.00 73.60  ?  258 ARG   A C   1 
ATOM   1822 O O   . ARG   A 1 253 ? 9.354   -23.083 21.219  1.00 74.11  ?  258 ARG   A O   1 
ATOM   1823 C CB  . ARG   A 1 253 ? 11.516  -24.534 23.250  1.00 82.91  ?  258 ARG   A CB  1 
ATOM   1824 C CG  . ARG   A 1 253 ? 12.914  -25.076 23.267  0.00 84.17  ?  258 ARG   A CG  1 
ATOM   1825 C CD  . ARG   A 1 253 ? 12.984  -26.360 24.080  0.00 88.68  ?  258 ARG   A CD  1 
ATOM   1826 N NE  . ARG   A 1 253 ? 14.353  -26.842 24.239  0.00 92.69  ?  258 ARG   A NE  1 
ATOM   1827 C CZ  . ARG   A 1 253 ? 14.686  -27.932 24.924  0.00 97.35  ?  258 ARG   A CZ  1 
ATOM   1828 N NH1 . ARG   A 1 253 ? 13.748  -28.659 25.516  0.00 98.60  ?  258 ARG   A NH1 1 
ATOM   1829 N NH2 . ARG   A 1 253 ? 15.958  -28.295 25.017  0.00 101.27 ?  258 ARG   A NH2 1 
ATOM   1830 N N   . GLU   A 1 254 ? 9.200   -22.360 23.363  1.00 70.60  ?  259 GLU   A N   1 
ATOM   1831 C CA  . GLU   A 1 254 ? 7.777   -21.988 23.314  1.00 72.02  ?  259 GLU   A CA  1 
ATOM   1832 C C   . GLU   A 1 254 ? 7.455   -20.964 22.221  1.00 68.69  ?  259 GLU   A C   1 
ATOM   1833 O O   . GLU   A 1 254 ? 6.485   -21.148 21.490  1.00 73.06  ?  259 GLU   A O   1 
ATOM   1834 C CB  . GLU   A 1 254 ? 7.292   -21.456 24.676  1.00 70.99  ?  259 GLU   A CB  1 
ATOM   1835 C CG  . GLU   A 1 254 ? 6.939   -22.509 25.724  1.00 78.12  ?  259 GLU   A CG  1 
ATOM   1836 C CD  . GLU   A 1 254 ? 8.112   -23.174 26.448  1.00 81.37  ?  259 GLU   A CD  1 
ATOM   1837 O OE1 . GLU   A 1 254 ? 9.255   -22.656 26.448  1.00 75.14  ?  259 GLU   A OE1 1 
ATOM   1838 O OE2 . GLU   A 1 254 ? 7.867   -24.256 27.026  1.00 87.19  ?  259 GLU   A OE2 1 
ATOM   1839 N N   . ILE   A 1 255 ? 8.290   -19.928 22.109  1.00 65.89  ?  260 ILE   A N   1 
ATOM   1840 C CA  . ILE   A 1 255 ? 8.119   -18.878 21.096  1.00 64.54  ?  260 ILE   A CA  1 
ATOM   1841 C C   . ILE   A 1 255 ? 8.364   -19.406 19.660  1.00 67.68  ?  260 ILE   A C   1 
ATOM   1842 O O   . ILE   A 1 255 ? 7.649   -19.007 18.738  1.00 65.05  ?  260 ILE   A O   1 
ATOM   1843 C CB  . ILE   A 1 255 ? 8.994   -17.626 21.412  1.00 61.57  ?  260 ILE   A CB  1 
ATOM   1844 C CG1 . ILE   A 1 255 ? 8.468   -16.896 22.659  1.00 56.18  ?  260 ILE   A CG1 1 
ATOM   1845 C CG2 . ILE   A 1 255 ? 9.002   -16.634 20.254  1.00 59.93  ?  260 ILE   A CG2 1 
ATOM   1846 C CD1 . ILE   A 1 255 ? 9.344   -15.918 23.326  0.00 53.68  ?  260 ILE   A CD1 1 
ATOM   1847 N N   . ILE   A 1 256 ? 9.358   -20.277 19.483  1.00 67.40  ?  261 ILE   A N   1 
ATOM   1848 C CA  . ILE   A 1 256 ? 9.617   -20.908 18.170  1.00 69.99  ?  261 ILE   A CA  1 
ATOM   1849 C C   . ILE   A 1 256 ? 8.440   -21.805 17.736  1.00 72.57  ?  261 ILE   A C   1 
ATOM   1850 O O   . ILE   A 1 256 ? 8.085   -21.829 16.545  1.00 72.97  ?  261 ILE   A O   1 
ATOM   1851 C CB  . ILE   A 1 256 ? 10.986  -21.633 18.137  1.00 73.96  ?  261 ILE   A CB  1 
ATOM   1852 C CG1 . ILE   A 1 256 ? 12.113  -20.589 18.195  1.00 75.78  ?  261 ILE   A CG1 1 
ATOM   1853 C CG2 . ILE   A 1 256 ? 11.180  -22.462 16.863  1.00 74.90  ?  261 ILE   A CG2 1 
ATOM   1854 C CD1 . ILE   A 1 256 ? 13.417  -21.126 18.745  1.00 87.57  ?  261 ILE   A CD1 1 
ATOM   1855 N N   . SER   A 1 257 ? 7.847   -22.538 18.685  1.00 74.18  ?  262 SER   A N   1 
ATOM   1856 C CA  . SER   A 1 257 ? 6.607   -23.303 18.425  1.00 78.30  ?  262 SER   A CA  1 
ATOM   1857 C C   . SER   A 1 257 ? 5.413   -22.413 18.052  1.00 77.37  ?  262 SER   A C   1 
ATOM   1858 O O   . SER   A 1 257 ? 4.640   -22.754 17.157  1.00 79.03  ?  262 SER   A O   1 
ATOM   1859 C CB  . SER   A 1 257 ? 6.236   -24.159 19.627  1.00 76.27  ?  262 SER   A CB  1 
ATOM   1860 O OG  . SER   A 1 257 ? 7.250   -25.110 19.861  1.00 86.96  ?  262 SER   A OG  1 
ATOM   1861 N N   . LEU   A 1 258 ? 5.293   -21.279 18.741  1.00 70.35  ?  263 LEU   A N   1 
ATOM   1862 C CA  . LEU   A 1 258 ? 4.218   -20.327 18.515  1.00 67.55  ?  263 LEU   A CA  1 
ATOM   1863 C C   . LEU   A 1 258 ? 4.274   -19.712 17.116  1.00 64.47  ?  263 LEU   A C   1 
ATOM   1864 O O   . LEU   A 1 258 ? 3.246   -19.669 16.444  1.00 68.53  ?  263 LEU   A O   1 
ATOM   1865 C CB  . LEU   A 1 258 ? 4.249   -19.218 19.573  1.00 69.47  ?  263 LEU   A CB  1 
ATOM   1866 C CG  . LEU   A 1 258 ? 3.060   -18.252 19.620  1.00 69.99  ?  263 LEU   A CG  1 
ATOM   1867 C CD1 . LEU   A 1 258 ? 1.800   -18.981 20.081  1.00 70.11  ?  263 LEU   A CD1 1 
ATOM   1868 C CD2 . LEU   A 1 258 ? 3.376   -17.071 20.529  1.00 71.95  ?  263 LEU   A CD2 1 
ATOM   1869 N N   . MET   A 1 259 ? 5.451   -19.254 16.683  1.00 56.99  ?  264 MET   A N   1 
ATOM   1870 C CA  . MET   A 1 259 ? 5.599   -18.686 15.335  1.00 57.39  ?  264 MET   A CA  1 
ATOM   1871 C C   . MET   A 1 259 ? 5.352   -19.746 14.258  1.00 53.88  ?  264 MET   A C   1 
ATOM   1872 O O   . MET   A 1 259 ? 4.661   -19.476 13.284  1.00 53.95  ?  264 MET   A O   1 
ATOM   1873 C CB  . MET   A 1 259 ? 6.939   -17.937 15.143  1.00 61.04  ?  264 MET   A CB  1 
ATOM   1874 C CG  . MET   A 1 259 ? 8.199   -18.779 15.065  1.00 68.64  ?  264 MET   A CG  1 
ATOM   1875 S SD  . MET   A 1 259 ? 9.688   -17.802 14.754  1.00 74.98  ?  264 MET   A SD  1 
ATOM   1876 C CE  . MET   A 1 259 ? 10.011  -17.175 16.395  1.00 72.96  ?  264 MET   A CE  1 
ATOM   1877 N N   . LYS   A 1 260 ? 5.887   -20.949 14.466  1.00 59.81  ?  265 LYS   A N   1 
ATOM   1878 C CA  . LYS   A 1 260 ? 5.640   -22.102 13.571  1.00 63.38  ?  265 LYS   A CA  1 
ATOM   1879 C C   . LYS   A 1 260 ? 4.145   -22.441 13.466  1.00 65.65  ?  265 LYS   A C   1 
ATOM   1880 O O   . LYS   A 1 260 ? 3.657   -22.714 12.372  1.00 71.19  ?  265 LYS   A O   1 
ATOM   1881 C CB  . LYS   A 1 260 ? 6.464   -23.341 13.978  1.00 67.10  ?  265 LYS   A CB  1 
ATOM   1882 C CG  . LYS   A 1 260 ? 7.930   -23.303 13.522  1.00 68.26  ?  265 LYS   A CG  1 
ATOM   1883 C CD  . LYS   A 1 260 ? 8.724   -24.546 13.924  1.00 70.96  ?  265 LYS   A CD  1 
ATOM   1884 C CE  . LYS   A 1 260 ? 10.162  -24.472 13.562  0.00 68.79  ?  265 LYS   A CE  1 
ATOM   1885 N NZ  . LYS   A 1 260 ? 10.905  -25.677 14.024  0.00 72.85  ?  265 LYS   A NZ  1 
ATOM   1886 N N   . LEU   A 1 261 ? 3.437   -22.382 14.593  1.00 65.59  ?  266 LEU   A N   1 
ATOM   1887 C CA  . LEU   A 1 261 ? 1.972   -22.562 14.632  1.00 68.55  ?  266 LEU   A CA  1 
ATOM   1888 C C   . LEU   A 1 261 ? 1.229   -21.436 13.905  1.00 70.05  ?  266 LEU   A C   1 
ATOM   1889 O O   . LEU   A 1 261 ? 0.321   -21.684 13.105  1.00 68.89  ?  266 LEU   A O   1 
ATOM   1890 C CB  . LEU   A 1 261 ? 1.473   -22.632 16.090  1.00 72.10  ?  266 LEU   A CB  1 
ATOM   1891 C CG  . LEU   A 1 261 ? 0.003   -23.020 16.331  1.00 78.00  ?  266 LEU   A CG  1 
ATOM   1892 C CD1 . LEU   A 1 261 ? -0.238  -24.478 15.976  1.00 83.88  ?  266 LEU   A CD1 1 
ATOM   1893 C CD2 . LEU   A 1 261 ? -0.414  -22.733 17.764  1.00 76.71  ?  266 LEU   A CD2 1 
ATOM   1894 N N   . CYS   A 1 262 ? 1.602   -20.200 14.222  1.00 69.79  ?  267 CYS   A N   1 
ATOM   1895 C CA  . CYS   A 1 262 ? 0.955   -19.013 13.644  1.00 64.23  ?  267 CYS   A CA  1 
ATOM   1896 C C   . CYS   A 1 262 ? 1.237   -18.767 12.162  1.00 63.82  ?  267 CYS   A C   1 
ATOM   1897 O O   . CYS   A 1 262 ? 0.441   -18.075 11.529  1.00 67.17  ?  267 CYS   A O   1 
ATOM   1898 C CB  . CYS   A 1 262 ? 1.264   -17.760 14.453  1.00 61.02  ?  267 CYS   A CB  1 
ATOM   1899 S SG  . CYS   A 1 262 ? 0.496   -17.799 16.077  1.00 64.93  ?  267 CYS   A SG  1 
ATOM   1900 N N   . TRP   A 1 263 ? 2.325   -19.320 11.607  1.00 59.41  ?  268 TRP   A N   1 
ATOM   1901 C CA  . TRP   A 1 263 ? 2.553   -19.266 10.149  1.00 60.26  ?  268 TRP   A CA  1 
ATOM   1902 C C   . TRP   A 1 263 ? 2.189   -20.523 9.355   1.00 63.00  ?  268 TRP   A C   1 
ATOM   1903 O O   . TRP   A 1 263 ? 2.661   -20.686 8.236   1.00 60.89  ?  268 TRP   A O   1 
ATOM   1904 C CB  . TRP   A 1 263 ? 3.953   -18.721 9.799   1.00 59.24  ?  268 TRP   A CB  1 
ATOM   1905 C CG  . TRP   A 1 263 ? 5.180   -19.516 10.082  1.00 60.19  ?  268 TRP   A CG  1 
ATOM   1906 C CD1 . TRP   A 1 263 ? 5.392   -20.860 9.902   1.00 66.31  ?  268 TRP   A CD1 1 
ATOM   1907 C CD2 . TRP   A 1 263 ? 6.436   -18.969 10.476  1.00 60.81  ?  268 TRP   A CD2 1 
ATOM   1908 N NE1 . TRP   A 1 263 ? 6.688   -21.183 10.214  1.00 69.17  ?  268 TRP   A NE1 1 
ATOM   1909 C CE2 . TRP   A 1 263 ? 7.357   -20.041 10.561  1.00 63.98  ?  268 TRP   A CE2 1 
ATOM   1910 C CE3 . TRP   A 1 263 ? 6.876   -17.672 10.780  1.00 60.25  ?  268 TRP   A CE3 1 
ATOM   1911 C CZ2 . TRP   A 1 263 ? 8.693   -19.856 10.950  1.00 63.88  ?  268 TRP   A CZ2 1 
ATOM   1912 C CZ3 . TRP   A 1 263 ? 8.206   -17.486 11.174  1.00 60.82  ?  268 TRP   A CZ3 1 
ATOM   1913 C CH2 . TRP   A 1 263 ? 9.098   -18.573 11.247  1.00 63.95  ?  268 TRP   A CH2 1 
ATOM   1914 N N   . GLU   A 1 264 ? 1.319   -21.382 9.903   1.00 67.26  ?  269 GLU   A N   1 
ATOM   1915 C CA  . GLU   A 1 264 ? 0.747   -22.531 9.162   1.00 70.89  ?  269 GLU   A CA  1 
ATOM   1916 C C   . GLU   A 1 264 ? 0.116   -22.077 7.836   1.00 75.98  ?  269 GLU   A C   1 
ATOM   1917 O O   . GLU   A 1 264 ? -0.503  -21.010 7.780   1.00 82.92  ?  269 GLU   A O   1 
ATOM   1918 C CB  . GLU   A 1 264 ? -0.305  -23.274 10.004  1.00 72.59  ?  269 GLU   A CB  1 
ATOM   1919 C CG  . GLU   A 1 264 ? 0.269   -24.167 11.107  1.00 81.51  ?  269 GLU   A CG  1 
ATOM   1920 C CD  . GLU   A 1 264 ? 0.857   -25.498 10.632  1.00 89.00  ?  269 GLU   A CD  1 
ATOM   1921 O OE1 . GLU   A 1 264 ? 0.663   -25.892 9.457   1.00 98.70  ?  269 GLU   A OE1 1 
ATOM   1922 O OE2 . GLU   A 1 264 ? 1.522   -26.161 11.455  1.00 84.05  ?  269 GLU   A OE2 1 
ATOM   1923 N N   . ALA   A 1 265 ? 0.319   -22.865 6.778   1.00 80.41  ?  270 ALA   A N   1 
ATOM   1924 C CA  . ALA   A 1 265 ? -0.259  -22.587 5.459   1.00 75.32  ?  270 ALA   A CA  1 
ATOM   1925 C C   . ALA   A 1 265 ? -1.779  -22.470 5.536   1.00 78.05  ?  270 ALA   A C   1 
ATOM   1926 O O   . ALA   A 1 265 ? -2.355  -21.487 5.039   1.00 77.99  ?  270 ALA   A O   1 
ATOM   1927 C CB  . ALA   A 1 265 ? 0.128   -23.668 4.467   1.00 81.25  ?  270 ALA   A CB  1 
ATOM   1928 N N   . ASN   A 1 266 ? -2.400  -23.452 6.200   1.00 79.20  ?  271 ASN   A N   1 
ATOM   1929 C CA  . ASN   A 1 266 ? -3.850  -23.496 6.393   1.00 82.94  ?  271 ASN   A CA  1 
ATOM   1930 C C   . ASN   A 1 266 ? -4.245  -22.478 7.475   1.00 77.81  ?  271 ASN   A C   1 
ATOM   1931 O O   . ASN   A 1 266 ? -3.749  -22.582 8.596   1.00 75.78  ?  271 ASN   A O   1 
ATOM   1932 C CB  . ASN   A 1 266 ? -4.300  -24.908 6.804   1.00 83.59  ?  271 ASN   A CB  1 
ATOM   1933 C CG  . ASN   A 1 266 ? -5.815  -25.101 6.761   1.00 90.44  ?  271 ASN   A CG  1 
ATOM   1934 O OD1 . ASN   A 1 266 ? -6.583  -24.233 6.336   1.00 89.97  ?  271 ASN   A OD1 1 
ATOM   1935 N ND2 . ASN   A 1 266 ? -6.251  -26.276 7.196   1.00 99.28  ?  271 ASN   A ND2 1 
ATOM   1936 N N   . PRO   A 1 267 ? -5.119  -21.487 7.142   1.00 74.68  ?  272 PRO   A N   1 
ATOM   1937 C CA  . PRO   A 1 267 ? -5.604  -20.536 8.159   1.00 73.27  ?  272 PRO   A CA  1 
ATOM   1938 C C   . PRO   A 1 267 ? -6.338  -21.153 9.360   1.00 74.24  ?  272 PRO   A C   1 
ATOM   1939 O O   . PRO   A 1 267 ? -6.175  -20.655 10.477  1.00 74.32  ?  272 PRO   A O   1 
ATOM   1940 C CB  . PRO   A 1 267 ? -6.563  -19.638 7.363   1.00 71.86  ?  272 PRO   A CB  1 
ATOM   1941 C CG  . PRO   A 1 267 ? -6.063  -19.710 5.980   1.00 68.53  ?  272 PRO   A CG  1 
ATOM   1942 C CD  . PRO   A 1 267 ? -5.663  -21.135 5.814   1.00 71.73  ?  272 PRO   A CD  1 
ATOM   1943 N N   . GLU   A 1 268 ? -7.108  -22.223 9.123   1.00 79.71  ?  273 GLU   A N   1 
ATOM   1944 C CA  . GLU   A 1 268 ? -7.803  -22.975 10.190  1.00 79.31  ?  273 GLU   A CA  1 
ATOM   1945 C C   . GLU   A 1 268 ? -6.862  -23.579 11.248  1.00 77.31  ?  273 GLU   A C   1 
ATOM   1946 O O   . GLU   A 1 268 ? -7.245  -23.664 12.416  1.00 77.49  ?  273 GLU   A O   1 
ATOM   1947 C CB  . GLU   A 1 268 ? -8.709  -24.068 9.597   1.00 80.37  ?  273 GLU   A CB  1 
ATOM   1948 C CG  . GLU   A 1 268 ? -9.866  -23.625 8.756   0.00 81.09  ?  273 GLU   A CG  1 
ATOM   1949 C CD  . GLU   A 1 268 ? -10.762 -24.765 8.295   0.00 85.76  ?  273 GLU   A CD  1 
ATOM   1950 O OE1 . GLU   A 1 268 ? -11.996 -24.563 8.260   0.00 87.44  ?  273 GLU   A OE1 1 
ATOM   1951 O OE2 . GLU   A 1 268 ? -10.249 -25.859 7.964   0.00 87.99  ?  273 GLU   A OE2 1 
ATOM   1952 N N   . ALA   A 1 269 ? -5.645  -23.965 10.843  1.00 77.50  ?  274 ALA   A N   1 
ATOM   1953 C CA  . ALA   A 1 269 ? -4.605  -24.424 11.783  1.00 79.25  ?  274 ALA   A CA  1 
ATOM   1954 C C   . ALA   A 1 269 ? -4.087  -23.349 12.738  1.00 74.77  ?  274 ALA   A C   1 
ATOM   1955 O O   . ALA   A 1 269 ? -3.679  -23.682 13.848  1.00 83.29  ?  274 ALA   A O   1 
ATOM   1956 C CB  . ALA   A 1 269 ? -3.432  -25.051 11.031  1.00 80.11  ?  274 ALA   A CB  1 
ATOM   1957 N N   . ARG   A 1 270 ? -4.103  -22.082 12.314  1.00 71.49  ?  275 ARG   A N   1 
ATOM   1958 C CA  . ARG   A 1 270 ? -3.554  -20.980 13.118  1.00 70.00  ?  275 ARG   A CA  1 
ATOM   1959 C C   . ARG   A 1 270 ? -4.499  -20.617 14.264  1.00 68.61  ?  275 ARG   A C   1 
ATOM   1960 O O   . ARG   A 1 270 ? -5.719  -20.651 14.072  1.00 67.89  ?  275 ARG   A O   1 
ATOM   1961 C CB  . ARG   A 1 270 ? -3.348  -19.724 12.273  1.00 67.06  ?  275 ARG   A CB  1 
ATOM   1962 C CG  . ARG   A 1 270 ? -2.360  -19.855 11.127  1.00 65.76  ?  275 ARG   A CG  1 
ATOM   1963 C CD  . ARG   A 1 270 ? -2.466  -18.649 10.218  1.00 63.75  ?  275 ARG   A CD  1 
ATOM   1964 N NE  . ARG   A 1 270 ? -1.966  -18.931 8.876   1.00 63.55  ?  275 ARG   A NE  1 
ATOM   1965 C CZ  . ARG   A 1 270 ? -2.356  -18.329 7.745   1.00 62.75  ?  275 ARG   A CZ  1 
ATOM   1966 N NH1 . ARG   A 1 270 ? -3.278  -17.373 7.741   1.00 65.18  ?  275 ARG   A NH1 1 
ATOM   1967 N NH2 . ARG   A 1 270 ? -1.819  -18.707 6.581   1.00 65.97  ?  275 ARG   A NH2 1 
ATOM   1968 N N   . PRO   A 1 271 ? -3.947  -20.219 15.437  1.00 66.29  ?  276 PRO   A N   1 
ATOM   1969 C CA  . PRO   A 1 271 ? -4.811  -19.852 16.557  1.00 66.89  ?  276 PRO   A CA  1 
ATOM   1970 C C   . PRO   A 1 271 ? -5.368  -18.436 16.422  1.00 69.31  ?  276 PRO   A C   1 
ATOM   1971 O O   . PRO   A 1 271 ? -5.041  -17.717 15.472  1.00 66.32  ?  276 PRO   A O   1 
ATOM   1972 C CB  . PRO   A 1 271 ? -3.875  -19.952 17.762  1.00 62.44  ?  276 PRO   A CB  1 
ATOM   1973 C CG  . PRO   A 1 271 ? -2.546  -19.589 17.214  1.00 61.22  ?  276 PRO   A CG  1 
ATOM   1974 C CD  . PRO   A 1 271 ? -2.531  -19.931 15.746  1.00 62.20  ?  276 PRO   A CD  1 
ATOM   1975 N N   . THR   A 1 272 ? -6.250  -18.090 17.354  1.00 67.26  ?  277 THR   A N   1 
ATOM   1976 C CA  . THR   A 1 272 ? -6.763  -16.738 17.522  1.00 59.44  ?  277 THR   A CA  1 
ATOM   1977 C C   . THR   A 1 272 ? -5.891  -16.044 18.550  1.00 59.53  ?  277 THR   A C   1 
ATOM   1978 O O   . THR   A 1 272 ? -5.268  -16.717 19.377  1.00 61.62  ?  277 THR   A O   1 
ATOM   1979 C CB  . THR   A 1 272 ? -8.203  -16.753 18.043  1.00 57.46  ?  277 THR   A CB  1 
ATOM   1980 O OG1 . THR   A 1 272 ? -8.263  -17.473 19.277  1.00 58.46  ?  277 THR   A OG1 1 
ATOM   1981 C CG2 . THR   A 1 272 ? -9.118  -17.401 17.050  1.00 58.78  ?  277 THR   A CG2 1 
ATOM   1982 N N   . PHE   A 1 273 ? -5.849  -14.711 18.502  1.00 52.86  ?  278 PHE   A N   1 
ATOM   1983 C CA  . PHE   A 1 273 ? -5.085  -13.931 19.489  1.00 54.47  ?  278 PHE   A CA  1 
ATOM   1984 C C   . PHE   A 1 273 ? -5.518  -14.163 20.962  1.00 56.66  ?  278 PHE   A C   1 
ATOM   1985 O O   . PHE   A 1 273 ? -4.649  -14.289 21.829  1.00 53.84  ?  278 PHE   A O   1 
ATOM   1986 C CB  . PHE   A 1 273 ? -5.063  -12.429 19.139  1.00 57.51  ?  278 PHE   A CB  1 
ATOM   1987 C CG  . PHE   A 1 273 ? -4.108  -12.087 18.026  1.00 54.56  ?  278 PHE   A CG  1 
ATOM   1988 C CD1 . PHE   A 1 273 ? -2.747  -12.010 18.262  1.00 49.62  ?  278 PHE   A CD1 1 
ATOM   1989 C CD2 . PHE   A 1 273 ? -4.572  -11.857 16.734  1.00 58.83  ?  278 PHE   A CD2 1 
ATOM   1990 C CE1 . PHE   A 1 273 ? -1.860  -11.701 17.231  1.00 48.32  ?  278 PHE   A CE1 1 
ATOM   1991 C CE2 . PHE   A 1 273 ? -3.701  -11.553 15.694  1.00 54.41  ?  278 PHE   A CE2 1 
ATOM   1992 C CZ  . PHE   A 1 273 ? -2.335  -11.479 15.943  1.00 49.04  ?  278 PHE   A CZ  1 
ATOM   1993 N N   . PRO   A 1 274 ? -6.841  -14.242 21.245  1.00 57.64  ?  279 PRO   A N   1 
ATOM   1994 C CA  . PRO   A 1 274 ? -7.301  -14.749 22.545  1.00 64.39  ?  279 PRO   A CA  1 
ATOM   1995 C C   . PRO   A 1 274 ? -6.736  -16.134 22.904  1.00 68.43  ?  279 PRO   A C   1 
ATOM   1996 O O   . PRO   A 1 274 ? -6.337  -16.351 24.055  1.00 68.07  ?  279 PRO   A O   1 
ATOM   1997 C CB  . PRO   A 1 274 ? -8.819  -14.825 22.370  1.00 60.80  ?  279 PRO   A CB  1 
ATOM   1998 C CG  . PRO   A 1 274 ? -9.122  -13.737 21.433  1.00 59.62  ?  279 PRO   A CG  1 
ATOM   1999 C CD  . PRO   A 1 274 ? -7.954  -13.633 20.498  1.00 61.44  ?  279 PRO   A CD  1 
ATOM   2000 N N   . GLY   A 1 275 ? -6.708  -17.036 21.916  1.00 64.01  ?  280 GLY   A N   1 
ATOM   2001 C CA  . GLY   A 1 275 ? -6.026  -18.321 22.019  1.00 66.58  ?  280 GLY   A CA  1 
ATOM   2002 C C   . GLY   A 1 275 ? -4.548  -18.207 22.350  1.00 68.66  ?  280 GLY   A C   1 
ATOM   2003 O O   . GLY   A 1 275 ? -4.053  -18.930 23.221  1.00 77.77  ?  280 GLY   A O   1 
ATOM   2004 N N   . ILE   A 1 276 ? -3.857  -17.296 21.663  1.00 61.76  ?  281 ILE   A N   1 
ATOM   2005 C CA  . ILE   A 1 276 ? -2.440  -17.011 21.919  1.00 62.05  ?  281 ILE   A CA  1 
ATOM   2006 C C   . ILE   A 1 276 ? -2.237  -16.432 23.337  1.00 63.89  ?  281 ILE   A C   1 
ATOM   2007 O O   . ILE   A 1 276 ? -1.361  -16.900 24.057  1.00 69.70  ?  281 ILE   A O   1 
ATOM   2008 C CB  . ILE   A 1 276 ? -1.827  -16.083 20.822  1.00 59.32  ?  281 ILE   A CB  1 
ATOM   2009 C CG1 . ILE   A 1 276 ? -1.818  -16.788 19.450  1.00 62.94  ?  281 ILE   A CG1 1 
ATOM   2010 C CG2 . ILE   A 1 276 ? -0.388  -15.687 21.151  1.00 58.56  ?  281 ILE   A CG2 1 
ATOM   2011 C CD1 . ILE   A 1 276 ? -1.671  -15.864 18.253  1.00 61.28  ?  281 ILE   A CD1 1 
ATOM   2012 N N   . GLU   A 1 277 ? -3.044  -15.432 23.700  1.00 62.47  ?  282 GLU   A N   1 
ATOM   2013 C CA  . GLU   A 1 277 ? -2.948  -14.711 24.990  1.00 62.54  ?  282 GLU   A CA  1 
ATOM   2014 C C   . GLU   A 1 277 ? -3.093  -15.617 26.216  1.00 69.14  ?  282 GLU   A C   1 
ATOM   2015 O O   . GLU   A 1 277 ? -2.383  -15.414 27.211  1.00 67.22  ?  282 GLU   A O   1 
ATOM   2016 C CB  . GLU   A 1 277 ? -4.023  -13.602 25.078  1.00 67.06  ?  282 GLU   A CB  1 
ATOM   2017 C CG  . GLU   A 1 277 ? -3.870  -12.597 26.234  1.00 69.65  ?  282 GLU   A CG  1 
ATOM   2018 C CD  . GLU   A 1 277 ? -4.952  -11.508 26.272  1.00 84.08  ?  282 GLU   A CD  1 
ATOM   2019 O OE1 . GLU   A 1 277 ? -6.028  -11.651 25.644  1.00 92.23  ?  282 GLU   A OE1 1 
ATOM   2020 O OE2 . GLU   A 1 277 ? -4.730  -10.484 26.952  1.00 90.14  ?  282 GLU   A OE2 1 
ATOM   2021 N N   . GLU   A 1 278 ? -4.044  -16.565 26.158  1.00 69.76  ?  283 GLU   A N   1 
ATOM   2022 C CA  . GLU   A 1 278 ? -4.293  -17.547 27.231  1.00 70.50  ?  283 GLU   A CA  1 
ATOM   2023 C C   . GLU   A 1 278 ? -3.072  -18.404 27.586  1.00 73.11  ?  283 GLU   A C   1 
ATOM   2024 O O   . GLU   A 1 278 ? -2.866  -18.699 28.763  1.00 77.61  ?  283 GLU   A O   1 
ATOM   2025 C CB  . GLU   A 1 278 ? -5.479  -18.470 26.875  1.00 70.55  ?  283 GLU   A CB  1 
ATOM   2026 C CG  . GLU   A 1 278 ? -6.822  -17.984 26.877  0.00 70.69  ?  283 GLU   A CG  1 
ATOM   2027 C CD  . GLU   A 1 278 ? -7.799  -18.810 26.051  0.00 72.43  ?  283 GLU   A CD  1 
ATOM   2028 O OE1 . GLU   A 1 278 ? -7.810  -20.052 26.197  0.00 75.24  ?  283 GLU   A OE1 1 
ATOM   2029 O OE2 . GLU   A 1 278 ? -8.558  -18.215 25.255  0.00 71.29  ?  283 GLU   A OE2 1 
ATOM   2030 N N   . LYS   A 1 279 ? -2.293  -18.777 26.568  1.00 70.72  ?  284 LYS   A N   1 
ATOM   2031 C CA  . LYS   A 1 279 ? -1.064  -19.552 26.750  1.00 68.22  ?  284 LYS   A CA  1 
ATOM   2032 C C   . LYS   A 1 279 ? 0.151   -18.658 26.972  1.00 62.13  ?  284 LYS   A C   1 
ATOM   2033 O O   . LYS   A 1 279 ? 0.970   -18.934 27.858  1.00 67.10  ?  284 LYS   A O   1 
ATOM   2034 C CB  . LYS   A 1 279 ? -0.848  -20.502 25.565  1.00 67.57  ?  284 LYS   A CB  1 
ATOM   2035 C CG  . LYS   A 1 279 ? -1.812  -21.686 25.584  1.00 71.63  ?  284 LYS   A CG  1 
ATOM   2036 C CD  . LYS   A 1 279 ? -1.708  -22.668 24.556  0.00 71.02  ?  284 LYS   A CD  1 
ATOM   2037 C CE  . LYS   A 1 279 ? -2.995  -23.458 24.352  0.00 73.60  ?  284 LYS   A CE  1 
ATOM   2038 N NZ  . LYS   A 1 279 ? -2.837  -24.589 23.397  0.00 75.48  ?  284 LYS   A NZ  1 
ATOM   2039 N N   . PHE   A 1 280 ? 0.282   -17.591 26.184  1.00 59.85  ?  285 PHE   A N   1 
ATOM   2040 C CA  . PHE   A 1 280 ? 1.459   -16.702 26.260  1.00 60.20  ?  285 PHE   A CA  1 
ATOM   2041 C C   . PHE   A 1 280 ? 1.586   -15.878 27.552  1.00 63.03  ?  285 PHE   A C   1 
ATOM   2042 O O   . PHE   A 1 280 ? 2.698   -15.720 28.048  1.00 72.49  ?  285 PHE   A O   1 
ATOM   2043 C CB  . PHE   A 1 280 ? 1.588   -15.784 25.031  1.00 54.38  ?  285 PHE   A CB  1 
ATOM   2044 C CG  . PHE   A 1 280 ? 2.954   -15.163 24.899  1.00 57.23  ?  285 PHE   A CG  1 
ATOM   2045 C CD1 . PHE   A 1 280 ? 4.012   -15.885 24.353  1.00 58.47  ?  285 PHE   A CD1 1 
ATOM   2046 C CD2 . PHE   A 1 280 ? 3.205   -13.863 25.362  1.00 60.78  ?  285 PHE   A CD2 1 
ATOM   2047 C CE1 . PHE   A 1 280 ? 5.287   -15.330 24.260  1.00 60.48  ?  285 PHE   A CE1 1 
ATOM   2048 C CE2 . PHE   A 1 280 ? 4.479   -13.299 25.269  1.00 58.95  ?  285 PHE   A CE2 1 
ATOM   2049 C CZ  . PHE   A 1 280 ? 5.523   -14.038 24.720  1.00 61.01  ?  285 PHE   A CZ  1 
ATOM   2050 N N   . ARG   A 1 281 ? 0.473   -15.394 28.101  1.00 65.20  ?  286 ARG   A N   1 
ATOM   2051 C CA  . ARG   A 1 281 ? 0.526   -14.579 29.329  1.00 65.28  ?  286 ARG   A CA  1 
ATOM   2052 C C   . ARG   A 1 281 ? 1.157   -15.311 30.539  1.00 69.10  ?  286 ARG   A C   1 
ATOM   2053 O O   . ARG   A 1 281 ? 2.074   -14.758 31.156  1.00 70.78  ?  286 ARG   A O   1 
ATOM   2054 C CB  . ARG   A 1 281 ? -0.839  -13.968 29.686  1.00 62.71  ?  286 ARG   A CB  1 
ATOM   2055 C CG  . ARG   A 1 281 ? -0.768  -12.913 30.787  1.00 62.94  ?  286 ARG   A CG  1 
ATOM   2056 C CD  . ARG   A 1 281 ? -2.143  -12.437 31.207  1.00 65.08  ?  286 ARG   A CD  1 
ATOM   2057 N NE  . ARG   A 1 281 ? -2.772  -11.583 30.198  1.00 64.36  ?  286 ARG   A NE  1 
ATOM   2058 C CZ  . ARG   A 1 281 ? -2.494  -10.299 29.961  1.00 63.21  ?  286 ARG   A CZ  1 
ATOM   2059 N NH1 . ARG   A 1 281 ? -1.551  -9.640  30.652  1.00 61.36  ?  286 ARG   A NH1 1 
ATOM   2060 N NH2 . ARG   A 1 281 ? -3.162  -9.667  28.995  1.00 65.19  ?  286 ARG   A NH2 1 
ATOM   2061 N N   . PRO   A 1 282 ? 0.690   -16.540 30.864  1.00 72.54  ?  287 PRO   A N   1 
ATOM   2062 C CA  . PRO   A 1 282 ? 1.373   -17.287 31.946  1.00 75.98  ?  287 PRO   A CA  1 
ATOM   2063 C C   . PRO   A 1 282 ? 2.837   -17.658 31.651  1.00 72.29  ?  287 PRO   A C   1 
ATOM   2064 O O   . PRO   A 1 282 ? 3.650   -17.704 32.582  1.00 73.17  ?  287 PRO   A O   1 
ATOM   2065 C CB  . PRO   A 1 282 ? 0.507   -18.545 32.126  1.00 81.46  ?  287 PRO   A CB  1 
ATOM   2066 C CG  . PRO   A 1 282 ? -0.268  -18.679 30.878  1.00 79.56  ?  287 PRO   A CG  1 
ATOM   2067 C CD  . PRO   A 1 282 ? -0.485  -17.281 30.364  1.00 76.87  ?  287 PRO   A CD  1 
ATOM   2068 N N   . PHE   A 1 283 ? 3.152   -17.912 30.377  1.00 67.49  ?  288 PHE   A N   1 
ATOM   2069 C CA  . PHE   A 1 283 ? 4.532   -18.123 29.937  1.00 65.94  ?  288 PHE   A CA  1 
ATOM   2070 C C   . PHE   A 1 283 ? 5.406   -16.885 30.161  1.00 67.51  ?  288 PHE   A C   1 
ATOM   2071 O O   . PHE   A 1 283 ? 6.499   -17.004 30.708  1.00 69.20  ?  288 PHE   A O   1 
ATOM   2072 C CB  . PHE   A 1 283 ? 4.579   -18.553 28.467  1.00 65.11  ?  288 PHE   A CB  1 
ATOM   2073 C CG  . PHE   A 1 283 ? 5.974   -18.767 27.945  1.00 68.69  ?  288 PHE   A CG  1 
ATOM   2074 C CD1 . PHE   A 1 283 ? 6.742   -19.850 28.386  1.00 71.42  ?  288 PHE   A CD1 1 
ATOM   2075 C CD2 . PHE   A 1 283 ? 6.548   -17.853 27.055  1.00 68.44  ?  288 PHE   A CD2 1 
ATOM   2076 C CE1 . PHE   A 1 283 ? 8.037   -20.038 27.917  1.00 72.41  ?  288 PHE   A CE1 1 
ATOM   2077 C CE2 . PHE   A 1 283 ? 7.848   -18.041 26.580  1.00 67.89  ?  288 PHE   A CE2 1 
ATOM   2078 C CZ  . PHE   A 1 283 ? 8.596   -19.128 27.023  1.00 70.07  ?  288 PHE   A CZ  1 
ATOM   2079 N N   . TYR   A 1 284 ? 4.910   -15.717 29.753  1.00 65.48  ?  289 TYR   A N   1 
ATOM   2080 C CA  . TYR   A 1 284 ? 5.579   -14.436 30.021  1.00 62.52  ?  289 TYR   A CA  1 
ATOM   2081 C C   . TYR   A 1 284 ? 5.868   -14.225 31.518  1.00 65.12  ?  289 TYR   A C   1 
ATOM   2082 O O   . TYR   A 1 284 ? 6.982   -13.827 31.884  1.00 69.49  ?  289 TYR   A O   1 
ATOM   2083 C CB  . TYR   A 1 284 ? 4.779   -13.248 29.442  1.00 59.68  ?  289 TYR   A CB  1 
ATOM   2084 C CG  . TYR   A 1 284 ? 5.280   -11.884 29.910  1.00 60.66  ?  289 TYR   A CG  1 
ATOM   2085 C CD1 . TYR   A 1 284 ? 6.509   -11.387 29.469  1.00 60.39  ?  289 TYR   A CD1 1 
ATOM   2086 C CD2 . TYR   A 1 284 ? 4.553   -11.117 30.834  1.00 58.78  ?  289 TYR   A CD2 1 
ATOM   2087 C CE1 . TYR   A 1 284 ? 6.987   -10.153 29.902  1.00 64.27  ?  289 TYR   A CE1 1 
ATOM   2088 C CE2 . TYR   A 1 284 ? 5.015   -9.877  31.269  1.00 59.16  ?  289 TYR   A CE2 1 
ATOM   2089 C CZ  . TYR   A 1 284 ? 6.237   -9.396  30.808  1.00 66.31  ?  289 TYR   A CZ  1 
ATOM   2090 O OH  . TYR   A 1 284 ? 6.724   -8.168  31.233  1.00 70.25  ?  289 TYR   A OH  1 
ATOM   2091 N N   . LEU   A 1 285 ? 4.875   -14.517 32.358  1.00 66.70  ?  290 LEU   A N   1 
ATOM   2092 C CA  . LEU   A 1 285 ? 4.975   -14.279 33.806  1.00 70.53  ?  290 LEU   A CA  1 
ATOM   2093 C C   . LEU   A 1 285 ? 5.951   -15.221 34.503  1.00 74.37  ?  290 LEU   A C   1 
ATOM   2094 O O   . LEU   A 1 285 ? 6.781   -14.764 35.295  1.00 81.40  ?  290 LEU   A O   1 
ATOM   2095 C CB  . LEU   A 1 285 ? 3.594   -14.361 34.476  1.00 76.79  ?  290 LEU   A CB  1 
ATOM   2096 C CG  . LEU   A 1 285 ? 2.590   -13.244 34.133  1.00 76.83  ?  290 LEU   A CG  1 
ATOM   2097 C CD1 . LEU   A 1 285 ? 1.178   -13.635 34.561  1.00 76.41  ?  290 LEU   A CD1 1 
ATOM   2098 C CD2 . LEU   A 1 285 ? 2.998   -11.904 34.738  1.00 77.57  ?  290 LEU   A CD2 1 
ATOM   2099 N N   . SER   A 1 286 ? 5.858   -16.515 34.195  1.00 75.07  ?  291 SER   A N   1 
ATOM   2100 C CA  . SER   A 1 286 ? 6.757   -17.522 34.774  1.00 81.02  ?  291 SER   A CA  1 
ATOM   2101 C C   . SER   A 1 286 ? 8.199   -17.411 34.263  1.00 82.96  ?  291 SER   A C   1 
ATOM   2102 O O   . SER   A 1 286 ? 9.128   -17.422 35.069  1.00 90.79  ?  291 SER   A O   1 
ATOM   2103 C CB  . SER   A 1 286 ? 6.221   -18.946 34.535  1.00 84.30  ?  291 SER   A CB  1 
ATOM   2104 O OG  . SER   A 1 286 ? 6.082   -19.231 33.153  1.00 83.42  ?  291 SER   A OG  1 
ATOM   2105 N N   . GLN   A 1 287 ? 8.365   -17.294 32.942  1.00 81.93  ?  292 GLN   A N   1 
ATOM   2106 C CA  . GLN   A 1 287 ? 9.678   -17.430 32.274  1.00 81.74  ?  292 GLN   A CA  1 
ATOM   2107 C C   . GLN   A 1 287 ? 10.350  -16.122 31.870  1.00 76.08  ?  292 GLN   A C   1 
ATOM   2108 O O   . GLN   A 1 287 ? 11.547  -15.929 32.140  1.00 85.02  ?  292 GLN   A O   1 
ATOM   2109 C CB  . GLN   A 1 287 ? 9.547   -18.313 31.030  1.00 85.52  ?  292 GLN   A CB  1 
ATOM   2110 C CG  . GLN   A 1 287 ? 9.142   -19.755 31.326  1.00 87.41  ?  292 GLN   A CG  1 
ATOM   2111 C CD  . GLN   A 1 287 ? 10.233  -20.539 32.027  1.00 96.91  ?  292 GLN   A CD  1 
ATOM   2112 O OE1 . GLN   A 1 287 ? 10.201  -20.698 33.248  1.00 105.35 ?  292 GLN   A OE1 1 
ATOM   2113 N NE2 . GLN   A 1 287 ? 11.212  -21.028 31.261  1.00 99.35  ?  292 GLN   A NE2 1 
ATOM   2114 N N   . LEU   A 1 288 ? 9.607   -15.231 31.216  1.00 73.33  ?  293 LEU   A N   1 
ATOM   2115 C CA  . LEU   A 1 288 ? 10.217  -14.077 30.533  1.00 72.90  ?  293 LEU   A CA  1 
ATOM   2116 C C   . LEU   A 1 288 ? 10.529  -12.859 31.409  1.00 73.08  ?  293 LEU   A C   1 
ATOM   2117 O O   . LEU   A 1 288 ? 11.628  -12.305 31.271  1.00 78.86  ?  293 LEU   A O   1 
ATOM   2118 C CB  . LEU   A 1 288 ? 9.406   -13.697 29.302  1.00 71.63  ?  293 LEU   A CB  1 
ATOM   2119 C CG  . LEU   A 1 288 ? 9.198   -14.845 28.297  1.00 71.50  ?  293 LEU   A CG  1 
ATOM   2120 C CD1 . LEU   A 1 288 ? 8.321   -14.372 27.152  1.00 70.87  ?  293 LEU   A CD1 1 
ATOM   2121 C CD2 . LEU   A 1 288 ? 10.510  -15.403 27.761  1.00 72.15  ?  293 LEU   A CD2 1 
ATOM   2122 N N   . GLU   A 1 289 ? 9.616   -12.445 32.299  1.00 74.21  ?  294 GLU   A N   1 
ATOM   2123 C CA  . GLU   A 1 289 ? 9.922   -11.326 33.251  1.00 82.65  ?  294 GLU   A CA  1 
ATOM   2124 C C   . GLU   A 1 289 ? 10.619  -11.832 34.509  1.00 89.44  ?  294 GLU   A C   1 
ATOM   2125 O O   . GLU   A 1 289 ? 11.518  -11.178 35.034  1.00 99.78  ?  294 GLU   A O   1 
ATOM   2126 C CB  . GLU   A 1 289 ? 8.705   -10.451 33.599  1.00 81.23  ?  294 GLU   A CB  1 
ATOM   2127 C CG  . GLU   A 1 289 ? 7.635   -11.049 34.514  1.00 83.29  ?  294 GLU   A CG  1 
ATOM   2128 C CD  . GLU   A 1 289 ? 6.674   -10.004 35.074  1.00 84.52  ?  294 GLU   A CD  1 
ATOM   2129 O OE1 . GLU   A 1 289 ? 6.059   -10.278 36.121  1.00 88.75  ?  294 GLU   A OE1 1 
ATOM   2130 O OE2 . GLU   A 1 289 ? 6.520   -8.911  34.486  1.00 91.02  ?  294 GLU   A OE2 1 
ATOM   2131 N N   . SER   B 1 1   ? -15.310 -23.840 21.129  0.00 172.51 ?  6   SER   B N   1 
ATOM   2132 C CA  . SER   B 1 1   ? -14.199 -22.948 21.649  1.00 134.76 ?  6   SER   B CA  1 
ATOM   2133 C C   . SER   B 1 1   ? -14.763 -21.892 22.596  1.00 142.17 ?  6   SER   B C   1 
ATOM   2134 O O   . SER   B 1 1   ? -14.532 -21.956 23.809  1.00 131.78 ?  6   SER   B O   1 
ATOM   2135 C CB  . SER   B 1 1   ? -13.351 -22.403 20.594  0.00 172.84 ?  6   SER   B CB  1 
ATOM   2136 O OG  . SER   B 1 1   ? -12.687 -23.433 19.883  0.00 177.74 ?  6   SER   B OG  1 
ATOM   2137 N N   . LEU   B 1 2   ? -15.488 -20.928 22.017  1.00 151.21 ?  7   LEU   B N   1 
ATOM   2138 C CA  . LEU   B 1 2   ? -16.198 -19.850 22.766  1.00 147.57 ?  7   LEU   B CA  1 
ATOM   2139 C C   . LEU   B 1 2   ? -17.527 -20.250 23.491  1.00 143.79 ?  7   LEU   B C   1 
ATOM   2140 O O   . LEU   B 1 2   ? -18.119 -19.413 24.195  1.00 122.06 ?  7   LEU   B O   1 
ATOM   2141 C CB  . LEU   B 1 2   ? -16.436 -18.648 21.832  1.00 139.08 ?  7   LEU   B CB  1 
ATOM   2142 C CG  . LEU   B 1 2   ? -15.216 -18.023 21.164  0.00 168.38 ?  7   LEU   B CG  1 
ATOM   2143 C CD1 . LEU   B 1 2   ? -15.665 -16.940 20.196  0.00 171.58 ?  7   LEU   B CD1 1 
ATOM   2144 C CD2 . LEU   B 1 2   ? -14.203 -17.463 22.154  0.00 163.37 ?  7   LEU   B CD2 1 
ATOM   2145 N N   . ASN   B 1 3   ? -17.972 -21.510 23.340  1.00 153.18 ?  8   ASN   B N   1 
ATOM   2146 C CA  . ASN   B 1 3   ? -19.189 -22.031 23.998  1.00 143.96 ?  8   ASN   B CA  1 
ATOM   2147 C C   . ASN   B 1 3   ? -18.946 -22.289 25.481  1.00 131.66 ?  8   ASN   B C   1 
ATOM   2148 O O   . ASN   B 1 3   ? -17.799 -22.406 25.910  1.00 118.80 ?  8   ASN   B O   1 
ATOM   2149 C CB  . ASN   B 1 3   ? -19.651 -23.330 23.328  1.00 136.20 ?  8   ASN   B CB  1 
ATOM   2150 C CG  . ASN   B 1 3   ? -19.990 -23.151 21.833  0.00 159.56 ?  8   ASN   B CG  1 
ATOM   2151 O OD1 . ASN   B 1 3   ? -20.311 -22.052 21.360  0.00 159.97 ?  8   ASN   B OD1 1 
ATOM   2152 N ND2 . ASN   B 1 3   ? -19.933 -24.258 21.090  0.00 163.98 ?  8   ASN   B ND2 1 
ATOM   2153 N N   . VAL   B 1 4   ? -20.030 -22.406 26.248  1.00 128.83 ?  9   VAL   B N   1 
ATOM   2154 C CA  . VAL   B 1 4   ? -19.934 -22.687 27.694  1.00 124.10 ?  9   VAL   B CA  1 
ATOM   2155 C C   . VAL   B 1 4   ? -19.578 -24.167 27.834  1.00 121.07 ?  9   VAL   B C   1 
ATOM   2156 O O   . VAL   B 1 4   ? -20.221 -25.050 27.227  1.00 132.30 ?  9   VAL   B O   1 
ATOM   2157 C CB  . VAL   B 1 4   ? -21.220 -22.388 28.512  1.00 118.60 ?  9   VAL   B CB  1 
ATOM   2158 C CG1 . VAL   B 1 4   ? -20.948 -22.459 30.013  1.00 104.41 ?  9   VAL   B CG1 1 
ATOM   2159 C CG2 . VAL   B 1 4   ? -21.742 -21.016 28.214  1.00 127.69 ?  9   VAL   B CG2 1 
ATOM   2160 N N   . ILE   B 1 5   ? -18.552 -24.429 28.640  1.00 107.67 ?  10  ILE   B N   1 
ATOM   2161 C CA  . ILE   B 1 5   ? -18.188 -25.790 29.025  1.00 103.85 ?  10  ILE   B CA  1 
ATOM   2162 C C   . ILE   B 1 5   ? -19.193 -26.246 30.107  1.00 94.28  ?  10  ILE   B C   1 
ATOM   2163 O O   . ILE   B 1 5   ? -19.157 -25.772 31.244  1.00 83.11  ?  10  ILE   B O   1 
ATOM   2164 C CB  . ILE   B 1 5   ? -16.704 -25.886 29.483  1.00 102.35 ?  10  ILE   B CB  1 
ATOM   2165 C CG1 . ILE   B 1 5   ? -15.762 -25.537 28.322  1.00 95.91  ?  10  ILE   B CG1 1 
ATOM   2166 C CG2 . ILE   B 1 5   ? -16.371 -27.284 29.992  1.00 106.93 ?  10  ILE   B CG2 1 
ATOM   2167 C CD1 . ILE   B 1 5   ? -14.305 -25.450 28.611  0.00 100.85 ?  10  ILE   B CD1 1 
ATOM   2168 N N   . LYS   B 1 6   ? -20.099 -27.142 29.723  1.00 97.26  ?  11  LYS   B N   1 
ATOM   2169 C CA  . LYS   B 1 6   ? -21.038 -27.767 30.649  1.00 95.96  ?  11  LYS   B CA  1 
ATOM   2170 C C   . LYS   B 1 6   ? -20.250 -28.831 31.402  1.00 86.40  ?  11  LYS   B C   1 
ATOM   2171 O O   . LYS   B 1 6   ? -19.751 -29.775 30.789  1.00 94.02  ?  11  LYS   B O   1 
ATOM   2172 C CB  . LYS   B 1 6   ? -22.237 -28.370 29.895  1.00 105.70 ?  11  LYS   B CB  1 
ATOM   2173 C CG  . LYS   B 1 6   ? -23.135 -27.312 29.240  1.00 109.34 ?  11  LYS   B CG  1 
ATOM   2174 C CD  . LYS   B 1 6   ? -23.786 -27.763 27.937  1.00 109.38 ?  11  LYS   B CD  1 
ATOM   2175 C CE  . LYS   B 1 6   ? -24.308 -26.576 27.138  1.00 103.41 ?  11  LYS   B CE  1 
ATOM   2176 N NZ  . LYS   B 1 6   ? -25.145 -26.994 25.982  1.00 109.37 ?  11  LYS   B NZ  1 
ATOM   2177 N N   . MET   B 1 7   ? -20.120 -28.655 32.715  1.00 79.33  ?  12  MET   B N   1 
ATOM   2178 C CA  . MET   B 1 7   ? -19.411 -29.604 33.589  1.00 75.54  ?  12  MET   B CA  1 
ATOM   2179 C C   . MET   B 1 7   ? -20.365 -30.481 34.390  1.00 73.42  ?  12  MET   B C   1 
ATOM   2180 O O   . MET   B 1 7   ? -21.546 -30.173 34.520  1.00 73.97  ?  12  MET   B O   1 
ATOM   2181 C CB  . MET   B 1 7   ? -18.506 -28.845 34.544  1.00 76.35  ?  12  MET   B CB  1 
ATOM   2182 C CG  . MET   B 1 7   ? -17.376 -28.124 33.832  1.00 79.05  ?  12  MET   B CG  1 
ATOM   2183 S SD  . MET   B 1 7   ? -16.333 -27.179 34.947  1.00 73.28  ?  12  MET   B SD  1 
ATOM   2184 C CE  . MET   B 1 7   ? -15.042 -26.718 33.791  1.00 79.67  ?  12  MET   B CE  1 
ATOM   2185 N N   . LYS   B 1 8   ? -19.819 -31.573 34.916  1.00 74.44  ?  13  LYS   B N   1 
ATOM   2186 C CA  . LYS   B 1 8   ? -20.541 -32.539 35.743  1.00 77.65  ?  13  LYS   B CA  1 
ATOM   2187 C C   . LYS   B 1 8   ? -19.874 -32.589 37.108  1.00 76.13  ?  13  LYS   B C   1 
ATOM   2188 O O   . LYS   B 1 8   ? -18.665 -32.443 37.198  1.00 80.25  ?  13  LYS   B O   1 
ATOM   2189 C CB  . LYS   B 1 8   ? -20.496 -33.925 35.091  1.00 79.32  ?  13  LYS   B CB  1 
ATOM   2190 C CG  . LYS   B 1 8   ? -21.115 -33.952 33.715  0.00 78.95  ?  13  LYS   B CG  1 
ATOM   2191 C CD  . LYS   B 1 8   ? -21.229 -35.370 33.168  0.00 83.57  ?  13  LYS   B CD  1 
ATOM   2192 C CE  . LYS   B 1 8   ? -19.894 -35.906 32.665  0.00 86.53  ?  13  LYS   B CE  1 
ATOM   2193 N NZ  . LYS   B 1 8   ? -20.025 -37.267 32.075  0.00 91.78  ?  13  LYS   B NZ  1 
ATOM   2194 N N   . SER   B 1 9   ? -20.651 -32.828 38.164  1.00 76.88  ?  14  SER   B N   1 
ATOM   2195 C CA  . SER   B 1 9   ? -20.112 -33.099 39.514  1.00 76.85  ?  14  SER   B CA  1 
ATOM   2196 C C   . SER   B 1 9   ? -19.114 -34.262 39.553  1.00 79.22  ?  14  SER   B C   1 
ATOM   2197 O O   . SER   B 1 9   ? -18.129 -34.207 40.301  1.00 78.63  ?  14  SER   B O   1 
ATOM   2198 C CB  . SER   B 1 9   ? -21.245 -33.361 40.509  1.00 75.63  ?  14  SER   B CB  1 
ATOM   2199 O OG  . SER   B 1 9   ? -22.078 -32.217 40.621  1.00 67.95  ?  14  SER   B OG  1 
ATOM   2200 N N   . SER   B 1 10  ? -19.369 -35.290 38.736  1.00 85.48  ?  15  SER   B N   1 
ATOM   2201 C CA  . SER   B 1 10  ? -18.448 -36.436 38.537  1.00 85.60  ?  15  SER   B CA  1 
ATOM   2202 C C   . SER   B 1 10  ? -17.062 -36.096 37.944  1.00 83.24  ?  15  SER   B C   1 
ATOM   2203 O O   . SER   B 1 10  ? -16.159 -36.901 38.066  1.00 81.51  ?  15  SER   B O   1 
ATOM   2204 C CB  . SER   B 1 10  ? -19.104 -37.510 37.664  1.00 88.18  ?  15  SER   B CB  1 
ATOM   2205 O OG  . SER   B 1 10  ? -19.131 -37.125 36.298  1.00 90.19  ?  15  SER   B OG  1 
ATOM   2206 N N   . ASP   B 1 11  ? -16.910 -34.933 37.303  1.00 81.93  ?  16  ASP   B N   1 
ATOM   2207 C CA  . ASP   B 1 11  ? -15.578 -34.413 36.900  1.00 85.97  ?  16  ASP   B CA  1 
ATOM   2208 C C   . ASP   B 1 11  ? -14.653 -34.009 38.069  1.00 85.13  ?  16  ASP   B C   1 
ATOM   2209 O O   . ASP   B 1 11  ? -13.441 -33.819 37.838  1.00 92.16  ?  16  ASP   B O   1 
ATOM   2210 C CB  . ASP   B 1 11  ? -15.690 -33.198 35.960  1.00 85.09  ?  16  ASP   B CB  1 
ATOM   2211 C CG  . ASP   B 1 11  ? -16.456 -33.494 34.667  1.00 91.29  ?  16  ASP   B CG  1 
ATOM   2212 O OD1 . ASP   B 1 11  ? -16.538 -34.673 34.250  1.00 89.35  ?  16  ASP   B OD1 1 
ATOM   2213 O OD2 . ASP   B 1 11  ? -16.966 -32.519 34.060  1.00 88.41  ?  16  ASP   B OD2 1 
ATOM   2214 N N   . PHE   B 1 12  ? -15.201 -33.846 39.282  1.00 79.40  ?  17  PHE   B N   1 
ATOM   2215 C CA  . PHE   B 1 12  ? -14.454 -33.333 40.435  1.00 78.62  ?  17  PHE   B CA  1 
ATOM   2216 C C   . PHE   B 1 12  ? -14.098 -34.406 41.466  1.00 87.23  ?  17  PHE   B C   1 
ATOM   2217 O O   . PHE   B 1 12  ? -14.932 -35.223 41.842  1.00 93.07  ?  17  PHE   B O   1 
ATOM   2218 C CB  . PHE   B 1 12  ? -15.251 -32.190 41.051  1.00 73.03  ?  17  PHE   B CB  1 
ATOM   2219 C CG  . PHE   B 1 12  ? -15.386 -31.028 40.123  1.00 67.04  ?  17  PHE   B CG  1 
ATOM   2220 C CD1 . PHE   B 1 12  ? -16.407 -30.981 39.177  1.00 66.19  ?  17  PHE   B CD1 1 
ATOM   2221 C CD2 . PHE   B 1 12  ? -14.450 -30.009 40.142  1.00 65.89  ?  17  PHE   B CD2 1 
ATOM   2222 C CE1 . PHE   B 1 12  ? -16.509 -29.920 38.284  1.00 58.32  ?  17  PHE   B CE1 1 
ATOM   2223 C CE2 . PHE   B 1 12  ? -14.547 -28.947 39.268  1.00 62.89  ?  17  PHE   B CE2 1 
ATOM   2224 C CZ  . PHE   B 1 12  ? -15.577 -28.900 38.329  1.00 59.47  ?  17  PHE   B CZ  1 
ATOM   2225 N N   . LEU   B 1 13  ? -12.851 -34.368 41.925  1.00 98.19  ?  18  LEU   B N   1 
ATOM   2226 C CA  . LEU   B 1 13  ? -12.256 -35.397 42.784  1.00 105.35 ?  18  LEU   B CA  1 
ATOM   2227 C C   . LEU   B 1 13  ? -12.643 -35.162 44.251  1.00 117.73 ?  18  LEU   B C   1 
ATOM   2228 O O   . LEU   B 1 13  ? -12.873 -36.132 44.986  1.00 119.72 ?  18  LEU   B O   1 
ATOM   2229 C CB  . LEU   B 1 13  ? -10.722 -35.464 42.588  1.00 107.02 ?  18  LEU   B CB  1 
ATOM   2230 C CG  . LEU   B 1 13  ? -10.249 -36.269 41.360  1.00 116.81 ?  18  LEU   B CG  1 
ATOM   2231 C CD1 . LEU   B 1 13  ? -10.825 -35.755 40.046  1.00 116.06 ?  18  LEU   B CD1 1 
ATOM   2232 C CD2 . LEU   B 1 13  ? -8.732  -36.324 41.251  1.00 120.24 ?  18  LEU   B CD2 1 
ATOM   2233 N N   . GLU   B 1 14  ? -12.688 -33.884 44.662  1.00 137.00 ?  19  GLU   B N   1 
ATOM   2234 C CA  . GLU   B 1 14  ? -12.988 -33.418 46.039  1.00 154.49 ?  19  GLU   B CA  1 
ATOM   2235 C C   . GLU   B 1 14  ? -12.101 -34.037 47.135  1.00 177.26 ?  19  GLU   B C   1 
ATOM   2236 O O   . GLU   B 1 14  ? -12.303 -33.809 48.335  1.00 193.34 ?  19  GLU   B O   1 
ATOM   2237 C CB  . GLU   B 1 14  ? -14.495 -33.513 46.385  1.00 155.74 ?  19  GLU   B CB  1 
ATOM   2238 C CG  . GLU   B 1 14  ? -15.068 -34.905 46.682  1.00 148.53 ?  19  GLU   B CG  1 
ATOM   2239 C CD  . GLU   B 1 14  ? -16.278 -34.881 47.604  1.00 144.69 ?  19  GLU   B CD  1 
ATOM   2240 O OE1 . GLU   B 1 14  ? -17.104 -33.944 47.511  1.00 138.46 ?  19  GLU   B OE1 1 
ATOM   2241 O OE2 . GLU   B 1 14  ? -16.404 -35.813 48.424  1.00 136.51 ?  19  GLU   B OE2 1 
ATOM   2242 N N   . LYS   B 1 25  ? -22.680 -21.865 48.977  1.00 95.86  ?  30  LYS   B N   1 
ATOM   2243 C CA  . LYS   B 1 25  ? -21.483 -22.660 49.265  1.00 108.67 ?  30  LYS   B CA  1 
ATOM   2244 C C   . LYS   B 1 25  ? -20.356 -22.457 48.225  1.00 107.32 ?  30  LYS   B C   1 
ATOM   2245 O O   . LYS   B 1 25  ? -20.350 -23.112 47.177  1.00 97.59  ?  30  LYS   B O   1 
ATOM   2246 C CB  . LYS   B 1 25  ? -21.852 -24.149 49.395  1.00 101.60 ?  30  LYS   B CB  1 
ATOM   2247 C CG  . LYS   B 1 25  ? -22.416 -24.554 50.696  0.00 103.92 ?  30  LYS   B CG  1 
ATOM   2248 C CD  . LYS   B 1 25  ? -22.810 -26.024 50.708  0.00 105.12 ?  30  LYS   B CD  1 
ATOM   2249 C CE  . LYS   B 1 25  ? -23.304 -26.471 52.074  0.00 109.46 ?  30  LYS   B CE  1 
ATOM   2250 N NZ  . LYS   B 1 25  ? -23.666 -27.916 52.086  0.00 111.19 ?  30  LYS   B NZ  1 
ATOM   2251 N N   . VAL   B 1 26  ? -19.420 -21.544 48.537  1.00 105.17 ?  31  VAL   B N   1 
ATOM   2252 C CA  . VAL   B 1 26  ? -18.155 -21.353 47.783  1.00 93.62  ?  31  VAL   B CA  1 
ATOM   2253 C C   . VAL   B 1 26  ? -17.116 -22.333 48.321  1.00 88.67  ?  31  VAL   B C   1 
ATOM   2254 O O   . VAL   B 1 26  ? -16.861 -22.351 49.523  1.00 98.27  ?  31  VAL   B O   1 
ATOM   2255 C CB  . VAL   B 1 26  ? -17.578 -19.919 47.931  1.00 99.51  ?  31  VAL   B CB  1 
ATOM   2256 C CG1 . VAL   B 1 26  ? -16.305 -19.743 47.095  1.00 91.51  ?  31  VAL   B CG1 1 
ATOM   2257 C CG2 . VAL   B 1 26  ? -18.614 -18.867 47.536  1.00 114.00 ?  31  VAL   B CG2 1 
ATOM   2258 N N   . SER   B 1 27  ? -16.513 -23.122 47.430  1.00 80.87  ?  32  SER   B N   1 
ATOM   2259 C CA  . SER   B 1 27  ? -15.595 -24.206 47.821  1.00 82.23  ?  32  SER   B CA  1 
ATOM   2260 C C   . SER   B 1 27  ? -14.492 -24.436 46.789  1.00 80.90  ?  32  SER   B C   1 
ATOM   2261 O O   . SER   B 1 27  ? -14.664 -24.155 45.599  1.00 83.28  ?  32  SER   B O   1 
ATOM   2262 C CB  . SER   B 1 27  ? -16.369 -25.518 48.054  1.00 86.01  ?  32  SER   B CB  1 
ATOM   2263 O OG  . SER   B 1 27  ? -17.001 -25.983 46.872  1.00 86.76  ?  32  SER   B OG  1 
ATOM   2264 N N   . LEU   B 1 28  ? -13.363 -24.956 47.264  1.00 81.81  ?  33  LEU   B N   1 
ATOM   2265 C CA  . LEU   B 1 28  ? -12.247 -25.333 46.408  1.00 83.59  ?  33  LEU   B CA  1 
ATOM   2266 C C   . LEU   B 1 28  ? -12.532 -26.708 45.819  1.00 81.73  ?  33  LEU   B C   1 
ATOM   2267 O O   . LEU   B 1 28  ? -13.021 -27.582 46.531  1.00 93.99  ?  33  LEU   B O   1 
ATOM   2268 C CB  . LEU   B 1 28  ? -10.946 -25.354 47.214  1.00 88.67  ?  33  LEU   B CB  1 
ATOM   2269 C CG  . LEU   B 1 28  ? -9.654  -25.380 46.393  1.00 92.09  ?  33  LEU   B CG  1 
ATOM   2270 C CD1 . LEU   B 1 28  ? -9.413  -24.064 45.672  1.00 89.65  ?  33  LEU   B CD1 1 
ATOM   2271 C CD2 . LEU   B 1 28  ? -8.486  -25.671 47.300  1.00 93.98  ?  33  LEU   B CD2 1 
ATOM   2272 N N   . ALA   B 1 29  ? -12.219 -26.885 44.534  1.00 77.79  ?  34  ALA   B N   1 
ATOM   2273 C CA  . ALA   B 1 29  ? -12.578 -28.099 43.798  1.00 80.42  ?  34  ALA   B CA  1 
ATOM   2274 C C   . ALA   B 1 29  ? -11.547 -28.426 42.740  1.00 81.13  ?  34  ALA   B C   1 
ATOM   2275 O O   . ALA   B 1 29  ? -11.140 -27.533 41.993  1.00 83.62  ?  34  ALA   B O   1 
ATOM   2276 C CB  . ALA   B 1 29  ? -13.935 -27.911 43.150  1.00 79.56  ?  34  ALA   B CB  1 
ATOM   2277 N N   . PHE   B 1 30  ? -11.149 -29.701 42.665  1.00 87.16  ?  35  PHE   B N   1 
ATOM   2278 C CA  . PHE   B 1 30  ? -10.153 -30.162 41.690  1.00 93.79  ?  35  PHE   B CA  1 
ATOM   2279 C C   . PHE   B 1 30  ? -10.774 -30.957 40.535  1.00 85.42  ?  35  PHE   B C   1 
ATOM   2280 O O   . PHE   B 1 30  ? -11.282 -32.052 40.741  1.00 80.59  ?  35  PHE   B O   1 
ATOM   2281 C CB  . PHE   B 1 30  ? -9.057  -30.988 42.362  1.00 110.40 ?  35  PHE   B CB  1 
ATOM   2282 C CG  . PHE   B 1 30  ? -7.948  -31.365 41.418  1.00 124.13 ?  35  PHE   B CG  1 
ATOM   2283 C CD1 . PHE   B 1 30  ? -6.988  -30.430 41.031  1.00 122.48 ?  35  PHE   B CD1 1 
ATOM   2284 C CD2 . PHE   B 1 30  ? -7.907  -32.639 40.846  1.00 138.84 ?  35  PHE   B CD2 1 
ATOM   2285 C CE1 . PHE   B 1 30  ? -5.994  -30.780 40.129  1.00 124.26 ?  35  PHE   B CE1 1 
ATOM   2286 C CE2 . PHE   B 1 30  ? -6.896  -32.996 39.950  1.00 140.64 ?  35  PHE   B CE2 1 
ATOM   2287 C CZ  . PHE   B 1 30  ? -5.947  -32.051 39.579  1.00 131.76 ?  35  PHE   B CZ  1 
ATOM   2288 N N   . HIS   B 1 31  ? -10.673 -30.404 39.328  1.00 80.66  ?  36  HIS   B N   1 
ATOM   2289 C CA  . HIS   B 1 31  ? -11.114 -31.064 38.092  1.00 87.67  ?  36  HIS   B CA  1 
ATOM   2290 C C   . HIS   B 1 31  ? -10.091 -32.123 37.669  1.00 97.65  ?  36  HIS   B C   1 
ATOM   2291 O O   . HIS   B 1 31  ? -8.879  -31.869 37.740  1.00 98.67  ?  36  HIS   B O   1 
ATOM   2292 C CB  . HIS   B 1 31  ? -11.250 -30.014 36.994  1.00 86.95  ?  36  HIS   B CB  1 
ATOM   2293 C CG  . HIS   B 1 31  ? -12.076 -30.433 35.825  1.00 92.35  ?  36  HIS   B CG  1 
ATOM   2294 N ND1 . HIS   B 1 31  ? -11.558 -31.172 34.792  1.00 94.94  ?  36  HIS   B ND1 1 
ATOM   2295 C CD2 . HIS   B 1 31  ? -13.358 -30.161 35.486  1.00 100.26 ?  36  HIS   B CD2 1 
ATOM   2296 C CE1 . HIS   B 1 31  ? -12.488 -31.374 33.878  1.00 106.02 ?  36  HIS   B CE1 1 
ATOM   2297 N NE2 . HIS   B 1 31  ? -13.592 -30.768 34.274  1.00 108.47 ?  36  HIS   B NE2 1 
ATOM   2298 N N   . ARG   B 1 32  ? -10.591 -33.268 37.183  1.00 97.28  ?  37  ARG   B N   1 
ATOM   2299 C CA  . ARG   B 1 32  ? -9.782  -34.483 36.957  1.00 98.50  ?  37  ARG   B CA  1 
ATOM   2300 C C   . ARG   B 1 32  ? -8.620  -34.314 35.973  1.00 99.33  ?  37  ARG   B C   1 
ATOM   2301 O O   . ARG   B 1 32  ? -7.526  -34.823 36.238  1.00 105.45 ?  37  ARG   B O   1 
ATOM   2302 C CB  . ARG   B 1 32  ? -10.694 -35.646 36.521  1.00 99.21  ?  37  ARG   B CB  1 
ATOM   2303 C CG  . ARG   B 1 32  ? -10.027 -37.019 36.417  1.00 112.93 ?  37  ARG   B CG  1 
ATOM   2304 C CD  . ARG   B 1 32  ? -11.019 -38.172 36.224  1.00 111.35 ?  37  ARG   B CD  1 
ATOM   2305 N NE  . ARG   B 1 32  ? -11.651 -38.616 37.479  1.00 103.64 ?  37  ARG   B NE  1 
ATOM   2306 C CZ  . ARG   B 1 32  ? -12.796 -38.162 38.011  1.00 92.84  ?  37  ARG   B CZ  1 
ATOM   2307 N NH1 . ARG   B 1 32  ? -13.515 -37.191 37.434  1.00 88.13  ?  37  ARG   B NH1 1 
ATOM   2308 N NH2 . ARG   B 1 32  ? -13.227 -38.678 39.161  1.00 88.20  ?  37  ARG   B NH2 1 
ATOM   2309 N N   . THR   B 1 33  ? -8.878  -33.648 34.845  1.00 96.05  ?  38  THR   B N   1 
ATOM   2310 C CA  . THR   B 1 33  ? -7.840  -33.270 33.865  1.00 102.68 ?  38  THR   B CA  1 
ATOM   2311 C C   . THR   B 1 33  ? -7.334  -31.830 34.096  1.00 105.06 ?  38  THR   B C   1 
ATOM   2312 O O   . THR   B 1 33  ? -6.155  -31.606 34.367  1.00 111.99 ?  38  THR   B O   1 
ATOM   2313 C CB  . THR   B 1 33  ? -8.343  -33.448 32.398  1.00 104.39 ?  38  THR   B CB  1 
ATOM   2314 O OG1 . THR   B 1 33  ? -9.337  -32.467 32.078  1.00 105.33 ?  38  THR   B OG1 1 
ATOM   2315 C CG2 . THR   B 1 33  ? -8.946  -34.839 32.173  1.00 107.25 ?  38  THR   B CG2 1 
ATOM   2316 N N   . GLN   B 1 34  ? -8.256  -30.878 33.971  1.00 102.87 ?  39  GLN   B N   1 
ATOM   2317 C CA  . GLN   B 1 34  ? -7.998  -29.425 33.929  1.00 94.14  ?  39  GLN   B CA  1 
ATOM   2318 C C   . GLN   B 1 34  ? -7.395  -28.720 35.139  1.00 88.95  ?  39  GLN   B C   1 
ATOM   2319 O O   . GLN   B 1 34  ? -6.891  -27.618 34.960  1.00 89.56  ?  39  GLN   B O   1 
ATOM   2320 C CB  . GLN   B 1 34  ? -9.286  -28.655 33.563  1.00 93.02  ?  39  GLN   B CB  1 
ATOM   2321 C CG  . GLN   B 1 34  ? -9.805  -28.890 32.150  1.00 94.31  ?  39  GLN   B CG  1 
ATOM   2322 C CD  . GLN   B 1 34  ? -10.915 -27.873 31.800  0.00 92.38  ?  39  GLN   B CD  1 
ATOM   2323 O OE1 . GLN   B 1 34  ? -11.073 -26.783 32.363  0.00 88.52  ?  39  GLN   B OE1 1 
ATOM   2324 N NE2 . GLN   B 1 34  ? -11.705 -28.275 30.807  0.00 94.16  ?  39  GLN   B NE2 1 
ATOM   2325 N N   . GLY   B 1 35  ? -7.492  -29.278 36.347  1.00 85.84  ?  40  GLY   B N   1 
ATOM   2326 C CA  . GLY   B 1 35  ? -6.785  -28.696 37.523  1.00 80.50  ?  40  GLY   B CA  1 
ATOM   2327 C C   . GLY   B 1 35  ? -7.621  -28.104 38.660  1.00 73.90  ?  40  GLY   B C   1 
ATOM   2328 O O   . GLY   B 1 35  ? -8.804  -28.370 38.759  1.00 72.83  ?  40  GLY   B O   1 
ATOM   2329 N N   . LEU   B 1 36  ? -6.984  -27.304 39.520  1.00 76.08  ?  41  LEU   B N   1 
ATOM   2330 C CA  . LEU   B 1 36  ? -7.635  -26.687 40.698  1.00 74.49  ?  41  LEU   B CA  1 
ATOM   2331 C C   . LEU   B 1 36  ? -8.508  -25.514 40.281  1.00 67.63  ?  41  LEU   B C   1 
ATOM   2332 O O   . LEU   B 1 36  ? -8.098  -24.706 39.452  1.00 67.73  ?  41  LEU   B O   1 
ATOM   2333 C CB  . LEU   B 1 36  ? -6.600  -26.197 41.718  1.00 80.50  ?  41  LEU   B CB  1 
ATOM   2334 C CG  . LEU   B 1 36  ? -7.113  -25.899 43.136  1.00 82.30  ?  41  LEU   B CG  1 
ATOM   2335 C CD1 . LEU   B 1 36  ? -7.540  -27.169 43.851  1.00 84.03  ?  41  LEU   B CD1 1 
ATOM   2336 C CD2 . LEU   B 1 36  ? -6.037  -25.191 43.951  1.00 88.20  ?  41  LEU   B CD2 1 
ATOM   2337 N N   . MET   B 1 37  ? -9.725  -25.460 40.827  1.00 63.94  ?  42  MET   B N   1 
ATOM   2338 C CA  . MET   B 1 37  ? -10.755 -24.462 40.460  1.00 59.06  ?  42  MET   B CA  1 
ATOM   2339 C C   . MET   B 1 37  ? -11.538 -24.063 41.714  1.00 54.59  ?  42  MET   B C   1 
ATOM   2340 O O   . MET   B 1 37  ? -11.349 -24.641 42.780  1.00 63.05  ?  42  MET   B O   1 
ATOM   2341 C CB  . MET   B 1 37  ? -11.721 -25.042 39.405  1.00 61.47  ?  42  MET   B CB  1 
ATOM   2342 C CG  . MET   B 1 37  ? -11.073 -25.909 38.320  1.00 63.84  ?  42  MET   B CG  1 
ATOM   2343 S SD  . MET   B 1 37  ? -11.788 -26.014 36.686  1.00 66.14  ?  42  MET   B SD  1 
ATOM   2344 C CE  . MET   B 1 37  ? -13.234 -26.910 37.071  1.00 69.66  ?  42  MET   B CE  1 
ATOM   2345 N N   . ILE   B 1 38  ? -12.426 -23.095 41.575  1.00 49.90  ?  43  ILE   B N   1 
ATOM   2346 C CA  . ILE   B 1 38  ? -13.324 -22.657 42.664  1.00 55.02  ?  43  ILE   B CA  1 
ATOM   2347 C C   . ILE   B 1 38  ? -14.752 -22.913 42.207  1.00 55.68  ?  43  ILE   B C   1 
ATOM   2348 O O   . ILE   B 1 38  ? -15.122 -22.490 41.119  1.00 63.79  ?  43  ILE   B O   1 
ATOM   2349 C CB  . ILE   B 1 38  ? -13.114 -21.159 43.022  1.00 56.88  ?  43  ILE   B CB  1 
ATOM   2350 C CG1 . ILE   B 1 38  ? -11.783 -20.950 43.775  1.00 57.31  ?  43  ILE   B CG1 1 
ATOM   2351 C CG2 . ILE   B 1 38  ? -14.285 -20.593 43.836  1.00 60.01  ?  43  ILE   B CG2 1 
ATOM   2352 C CD1 . ILE   B 1 38  ? -11.748 -21.408 45.227  1.00 61.35  ?  43  ILE   B CD1 1 
ATOM   2353 N N   . MET   B 1 39  ? -15.546 -23.571 43.053  1.00 58.28  ?  44  MET   B N   1 
ATOM   2354 C CA  . MET   B 1 39  ? -16.937 -23.896 42.756  1.00 55.83  ?  44  MET   B CA  1 
ATOM   2355 C C   . MET   B 1 39  ? -17.849 -23.131 43.692  1.00 51.93  ?  44  MET   B C   1 
ATOM   2356 O O   . MET   B 1 39  ? -17.866 -23.404 44.886  1.00 56.50  ?  44  MET   B O   1 
ATOM   2357 C CB  . MET   B 1 39  ? -17.184 -25.394 42.883  1.00 59.38  ?  44  MET   B CB  1 
ATOM   2358 C CG  . MET   B 1 39  ? -18.546 -25.801 42.343  1.00 63.41  ?  44  MET   B CG  1 
ATOM   2359 S SD  . MET   B 1 39  ? -18.924 -27.544 42.452  1.00 72.06  ?  44  MET   B SD  1 
ATOM   2360 C CE  . MET   B 1 39  ? -17.663 -28.262 41.394  1.00 79.73  ?  44  MET   B CE  1 
ATOM   2361 N N   . LYS   B 1 40  ? -18.594 -22.173 43.142  1.00 51.38  ?  45  LYS   B N   1 
ATOM   2362 C CA  . LYS   B 1 40  ? -19.700 -21.522 43.847  1.00 54.11  ?  45  LYS   B CA  1 
ATOM   2363 C C   . LYS   B 1 40  ? -20.961 -22.321 43.513  1.00 57.16  ?  45  LYS   B C   1 
ATOM   2364 O O   . LYS   B 1 40  ? -21.471 -22.247 42.388  1.00 54.78  ?  45  LYS   B O   1 
ATOM   2365 C CB  . LYS   B 1 40  ? -19.860 -20.049 43.442  1.00 56.77  ?  45  LYS   B CB  1 
ATOM   2366 C CG  . LYS   B 1 40  ? -21.140 -19.401 43.969  1.00 67.27  ?  45  LYS   B CG  1 
ATOM   2367 C CD  . LYS   B 1 40  ? -21.056 -17.914 44.272  1.00 74.88  ?  45  LYS   B CD  1 
ATOM   2368 C CE  . LYS   B 1 40  ? -22.383 -17.443 44.877  1.00 84.40  ?  45  LYS   B CE  1 
ATOM   2369 N NZ  . LYS   B 1 40  ? -22.201 -16.643 46.117  1.00 88.78  ?  45  LYS   B NZ  1 
ATOM   2370 N N   . THR   B 1 41  ? -21.443 -23.072 44.498  1.00 56.60  ?  46  THR   B N   1 
ATOM   2371 C CA  . THR   B 1 41  ? -22.677 -23.836 44.385  1.00 58.45  ?  46  THR   B CA  1 
ATOM   2372 C C   . THR   B 1 41  ? -23.818 -22.935 44.843  1.00 56.99  ?  46  THR   B C   1 
ATOM   2373 O O   . THR   B 1 41  ? -23.947 -22.629 46.027  1.00 55.27  ?  46  THR   B O   1 
ATOM   2374 C CB  . THR   B 1 41  ? -22.601 -25.157 45.178  1.00 63.28  ?  46  THR   B CB  1 
ATOM   2375 O OG1 . THR   B 1 41  ? -21.540 -25.950 44.638  1.00 68.34  ?  46  THR   B OG1 1 
ATOM   2376 C CG2 . THR   B 1 41  ? -23.893 -25.966 45.067  1.00 64.39  ?  46  THR   B CG2 1 
ATOM   2377 N N   . VAL   B 1 42  ? -24.658 -22.558 43.885  1.00 59.14  ?  47  VAL   B N   1 
ATOM   2378 C CA  . VAL   B 1 42  ? -25.681 -21.535 44.060  1.00 57.66  ?  47  VAL   B CA  1 
ATOM   2379 C C   . VAL   B 1 42  ? -26.916 -22.148 44.706  1.00 61.55  ?  47  VAL   B C   1 
ATOM   2380 O O   . VAL   B 1 42  ? -27.418 -21.591 45.678  1.00 66.20  ?  47  VAL   B O   1 
ATOM   2381 C CB  . VAL   B 1 42  ? -25.997 -20.861 42.710  1.00 54.55  ?  47  VAL   B CB  1 
ATOM   2382 C CG1 . VAL   B 1 42  ? -27.075 -19.797 42.846  1.00 57.50  ?  47  VAL   B CG1 1 
ATOM   2383 C CG2 . VAL   B 1 42  ? -24.725 -20.218 42.165  1.00 58.52  ?  47  VAL   B CG2 1 
ATOM   2384 N N   . TYR   B 1 43  ? -27.399 -23.266 44.148  1.00 61.48  ?  48  TYR   B N   1 
ATOM   2385 C CA  . TYR   B 1 43  ? -28.604 -23.968 44.601  1.00 61.48  ?  48  TYR   B CA  1 
ATOM   2386 C C   . TYR   B 1 43  ? -28.333 -25.465 44.779  1.00 64.15  ?  48  TYR   B C   1 
ATOM   2387 O O   . TYR   B 1 43  ? -27.726 -26.100 43.908  1.00 58.92  ?  48  TYR   B O   1 
ATOM   2388 C CB  . TYR   B 1 43  ? -29.747 -23.756 43.603  1.00 61.97  ?  48  TYR   B CB  1 
ATOM   2389 C CG  . TYR   B 1 43  ? -31.058 -24.449 43.958  1.00 64.58  ?  48  TYR   B CG  1 
ATOM   2390 C CD1 . TYR   B 1 43  ? -31.326 -25.764 43.550  1.00 60.95  ?  48  TYR   B CD1 1 
ATOM   2391 C CD2 . TYR   B 1 43  ? -32.046 -23.780 44.687  1.00 65.93  ?  48  TYR   B CD2 1 
ATOM   2392 C CE1 . TYR   B 1 43  ? -32.525 -26.393 43.878  1.00 65.10  ?  48  TYR   B CE1 1 
ATOM   2393 C CE2 . TYR   B 1 43  ? -33.250 -24.398 45.014  1.00 67.58  ?  48  TYR   B CE2 1 
ATOM   2394 C CZ  . TYR   B 1 43  ? -33.489 -25.701 44.610  1.00 69.42  ?  48  TYR   B CZ  1 
ATOM   2395 O OH  . TYR   B 1 43  ? -34.680 -26.303 44.948  1.00 74.17  ?  48  TYR   B OH  1 
ATOM   2396 N N   . LYS   B 1 44  ? -28.808 -25.994 45.912  1.00 68.51  ?  49  LYS   B N   1 
ATOM   2397 C CA  . LYS   B 1 44  ? -28.877 -27.430 46.204  1.00 67.86  ?  49  LYS   B CA  1 
ATOM   2398 C C   . LYS   B 1 44  ? -30.258 -27.705 46.826  1.00 69.01  ?  49  LYS   B C   1 
ATOM   2399 O O   . LYS   B 1 44  ? -30.624 -27.051 47.806  1.00 67.13  ?  49  LYS   B O   1 
ATOM   2400 C CB  . LYS   B 1 44  ? -27.751 -27.851 47.145  1.00 69.56  ?  49  LYS   B CB  1 
ATOM   2401 C CG  . LYS   B 1 44  ? -27.460 -29.349 47.167  1.00 68.51  ?  49  LYS   B CG  1 
ATOM   2402 C CD  . LYS   B 1 44  ? -26.435 -29.688 48.230  0.00 66.45  ?  49  LYS   B CD  1 
ATOM   2403 C CE  . LYS   B 1 44  ? -25.023 -29.330 47.788  0.00 64.24  ?  49  LYS   B CE  1 
ATOM   2404 N NZ  . LYS   B 1 44  ? -24.010 -29.671 48.824  0.00 66.63  ?  49  LYS   B NZ  1 
ATOM   2405 N N   . GLY   B 1 45  ? -31.009 -28.652 46.255  1.00 73.19  ?  50  GLY   B N   1 
ATOM   2406 C CA  . GLY   B 1 45  ? -32.408 -28.920 46.668  1.00 79.95  ?  50  GLY   B CA  1 
ATOM   2407 C C   . GLY   B 1 45  ? -33.245 -29.679 45.633  1.00 83.68  ?  50  GLY   B C   1 
ATOM   2408 O O   . GLY   B 1 45  ? -32.677 -30.389 44.807  1.00 82.38  ?  50  GLY   B O   1 
ATOM   2409 N N   . PRO   B 1 46  ? -34.599 -29.550 45.674  1.00 89.69  ?  51  PRO   B N   1 
ATOM   2410 C CA  . PRO   B 1 46  ? -35.459 -30.146 44.633  1.00 90.95  ?  51  PRO   B CA  1 
ATOM   2411 C C   . PRO   B 1 46  ? -35.257 -29.515 43.259  1.00 89.55  ?  51  PRO   B C   1 
ATOM   2412 O O   . PRO   B 1 46  ? -35.170 -28.290 43.174  1.00 98.84  ?  51  PRO   B O   1 
ATOM   2413 C CB  . PRO   B 1 46  ? -36.885 -29.860 45.141  1.00 99.12  ?  51  PRO   B CB  1 
ATOM   2414 C CG  . PRO   B 1 46  ? -36.747 -29.679 46.603  1.00 101.28 ?  51  PRO   B CG  1 
ATOM   2415 C CD  . PRO   B 1 46  ? -35.405 -29.040 46.803  1.00 96.74  ?  51  PRO   B CD  1 
ATOM   2416 N N   . ASN   B 1 47  ? -35.188 -30.333 42.208  1.00 92.06  ?  52  ASN   B N   1 
ATOM   2417 C CA  . ASN   B 1 47  ? -34.932 -29.817 40.848  1.00 104.97 ?  52  ASN   B CA  1 
ATOM   2418 C C   . ASN   B 1 47  ? -36.173 -29.158 40.227  1.00 114.16 ?  52  ASN   B C   1 
ATOM   2419 O O   . ASN   B 1 47  ? -37.289 -29.595 40.487  1.00 102.72 ?  52  ASN   B O   1 
ATOM   2420 C CB  . ASN   B 1 47  ? -34.317 -30.884 39.927  1.00 103.61 ?  52  ASN   B CB  1 
ATOM   2421 C CG  . ASN   B 1 47  ? -35.283 -31.968 39.511  1.00 101.72 ?  52  ASN   B CG  1 
ATOM   2422 O OD1 . ASN   B 1 47  ? -36.140 -32.376 40.285  1.00 112.55 ?  52  ASN   B OD1 1 
ATOM   2423 N ND2 . ASN   B 1 47  ? -35.117 -32.477 38.293  1.00 107.83 ?  52  ASN   B ND2 1 
ATOM   2424 N N   . CYS   B 1 48  ? -35.951 -28.108 39.428  1.00 131.65 ?  53  CYS   B N   1 
ATOM   2425 C CA  . CYS   B 1 48  ? -36.993 -27.455 38.611  1.00 137.51 ?  53  CYS   B CA  1 
ATOM   2426 C C   . CYS   B 1 48  ? -36.414 -27.078 37.231  1.00 138.34 ?  53  CYS   B C   1 
ATOM   2427 O O   . CYS   B 1 48  ? -35.681 -26.081 37.111  1.00 128.76 ?  53  CYS   B O   1 
ATOM   2428 C CB  . CYS   B 1 48  ? -37.555 -26.223 39.333  1.00 136.36 ?  53  CYS   B CB  1 
ATOM   2429 S SG  . CYS   B 1 48  ? -38.653 -26.577 40.736  1.00 123.66 ?  53  CYS   B SG  1 
ATOM   2430 N N   . ILE   B 1 49  ? -36.746 -27.895 36.223  1.00 144.84 ?  54  ILE   B N   1 
ATOM   2431 C CA  . ILE   B 1 49  ? -36.198 -27.790 34.856  1.00 144.37 ?  54  ILE   B CA  1 
ATOM   2432 C C   . ILE   B 1 49  ? -36.747 -26.631 33.996  1.00 146.52 ?  54  ILE   B C   1 
ATOM   2433 O O   . ILE   B 1 49  ? -36.165 -26.309 32.941  1.00 150.88 ?  54  ILE   B O   1 
ATOM   2434 C CB  . ILE   B 1 49  ? -36.411 -29.110 34.079  1.00 129.77 ?  54  ILE   B CB  1 
ATOM   2435 C CG1 . ILE   B 1 49  ? -35.827 -30.339 34.892  0.00 150.26 ?  54  ILE   B CG1 1 
ATOM   2436 C CG2 . ILE   B 1 49  ? -35.564 -29.128 32.743  0.00 151.95 ?  54  ILE   B CG2 1 
ATOM   2437 C CD1 . ILE   B 1 49  ? -35.635 -31.622 34.104  0.00 152.45 ?  54  ILE   B CD1 1 
ATOM   2438 N N   . GLU   B 1 50  ? -37.859 -26.038 34.449  1.00 140.58 ?  55  GLU   B N   1 
ATOM   2439 C CA  . GLU   B 1 50  ? -38.480 -24.833 33.854  1.00 137.09 ?  55  GLU   B CA  1 
ATOM   2440 C C   . GLU   B 1 50  ? -37.545 -23.635 33.617  1.00 120.24 ?  55  GLU   B C   1 
ATOM   2441 O O   . GLU   B 1 50  ? -37.677 -22.989 32.581  1.00 121.42 ?  55  GLU   B O   1 
ATOM   2442 C CB  . GLU   B 1 50  ? -39.706 -24.390 34.670  1.00 147.72 ?  55  GLU   B CB  1 
ATOM   2443 C CG  . GLU   B 1 50  ? -39.416 -23.939 36.104  1.00 142.86 ?  55  GLU   B CG  1 
ATOM   2444 C CD  . GLU   B 1 50  ? -40.603 -24.097 37.049  1.00 144.22 ?  55  GLU   B CD  1 
ATOM   2445 O OE1 . GLU   B 1 50  ? -41.767 -23.942 36.614  1.00 134.97 ?  55  GLU   B OE1 1 
ATOM   2446 O OE2 . GLU   B 1 50  ? -40.366 -24.375 38.243  1.00 143.90 ?  55  GLU   B OE2 1 
ATOM   2447 N N   . HIS   B 1 51  ? -36.620 -23.354 34.547  1.00 99.37  ?  56  HIS   B N   1 
ATOM   2448 C CA  . HIS   B 1 51  ? -35.648 -22.222 34.412  1.00 93.76  ?  56  HIS   B CA  1 
ATOM   2449 C C   . HIS   B 1 51  ? -34.220 -22.589 33.916  1.00 84.30  ?  56  HIS   B C   1 
ATOM   2450 O O   . HIS   B 1 51  ? -33.365 -21.690 33.715  1.00 79.64  ?  56  HIS   B O   1 
ATOM   2451 C CB  . HIS   B 1 51  ? -35.594 -21.414 35.724  1.00 95.12  ?  56  HIS   B CB  1 
ATOM   2452 C CG  . HIS   B 1 51  ? -36.853 -20.658 36.014  1.00 103.11 ?  56  HIS   B CG  1 
ATOM   2453 N ND1 . HIS   B 1 51  ? -37.723 -21.021 37.020  1.00 110.29 ?  56  HIS   B ND1 1 
ATOM   2454 C CD2 . HIS   B 1 51  ? -37.400 -19.571 35.418  1.00 106.63 ?  56  HIS   B CD2 1 
ATOM   2455 C CE1 . HIS   B 1 51  ? -38.752 -20.191 37.033  1.00 109.78 ?  56  HIS   B CE1 1 
ATOM   2456 N NE2 . HIS   B 1 51  ? -38.579 -19.301 36.071  1.00 112.30 ?  56  HIS   B NE2 1 
ATOM   2457 N N   . ASN   B 1 52  ? -33.977 -23.880 33.653  1.00 79.54  ?  57  ASN   B N   1 
ATOM   2458 C CA  . ASN   B 1 52  ? -32.666 -24.356 33.150  1.00 77.77  ?  57  ASN   B CA  1 
ATOM   2459 C C   . ASN   B 1 52  ? -32.194 -23.742 31.843  1.00 80.19  ?  57  ASN   B C   1 
ATOM   2460 O O   . ASN   B 1 52  ? -31.004 -23.486 31.678  1.00 78.93  ?  57  ASN   B O   1 
ATOM   2461 C CB  . ASN   B 1 52  ? -32.657 -25.883 33.002  1.00 79.28  ?  57  ASN   B CB  1 
ATOM   2462 C CG  . ASN   B 1 52  ? -32.649 -26.610 34.344  1.00 81.96  ?  57  ASN   B CG  1 
ATOM   2463 O OD1 . ASN   B 1 52  ? -32.798 -26.000 35.411  1.00 71.44  ?  57  ASN   B OD1 1 
ATOM   2464 N ND2 . ASN   B 1 52  ? -32.506 -27.933 34.292  1.00 90.22  ?  57  ASN   B ND2 1 
ATOM   2465 N N   . GLU   B 1 53  ? -33.132 -23.484 30.940  1.00 85.45  ?  58  GLU   B N   1 
ATOM   2466 C CA  . GLU   B 1 53  ? -32.836 -22.849 29.661  1.00 90.08  ?  58  GLU   B CA  1 
ATOM   2467 C C   . GLU   B 1 53  ? -32.358 -21.404 29.887  1.00 86.33  ?  58  GLU   B C   1 
ATOM   2468 O O   . GLU   B 1 53  ? -31.352 -20.984 29.307  1.00 81.44  ?  58  GLU   B O   1 
ATOM   2469 C CB  . GLU   B 1 53  ? -34.060 -22.871 28.740  1.00 103.82 ?  58  GLU   B CB  1 
ATOM   2470 C CG  . GLU   B 1 53  ? -34.481 -24.263 28.250  1.00 112.39 ?  58  GLU   B CG  1 
ATOM   2471 C CD  . GLU   B 1 53  ? -35.362 -25.041 29.228  1.00 121.65 ?  58  GLU   B CD  1 
ATOM   2472 O OE1 . GLU   B 1 53  ? -35.082 -26.237 29.469  1.00 121.74 ?  58  GLU   B OE1 1 
ATOM   2473 O OE2 . GLU   B 1 53  ? -36.321 -24.462 29.783  1.00 130.81 ?  58  GLU   B OE2 1 
ATOM   2474 N N   . ALA   B 1 54  ? -33.073 -20.674 30.748  1.00 84.02  ?  59  ALA   B N   1 
ATOM   2475 C CA  . ALA   B 1 54  ? -32.707 -19.291 31.122  1.00 81.49  ?  59  ALA   B CA  1 
ATOM   2476 C C   . ALA   B 1 54  ? -31.414 -19.196 31.937  1.00 78.46  ?  59  ALA   B C   1 
ATOM   2477 O O   . ALA   B 1 54  ? -30.615 -18.263 31.732  1.00 76.86  ?  59  ALA   B O   1 
ATOM   2478 C CB  . ALA   B 1 54  ? -33.844 -18.626 31.882  1.00 84.39  ?  59  ALA   B CB  1 
ATOM   2479 N N   . LEU   B 1 55  ? -31.227 -20.147 32.863  1.00 72.77  ?  60  LEU   B N   1 
ATOM   2480 C CA  . LEU   B 1 55  ? -29.979 -20.270 33.644  1.00 64.60  ?  60  LEU   B CA  1 
ATOM   2481 C C   . LEU   B 1 55  ? -28.755 -20.540 32.759  1.00 62.34  ?  60  LEU   B C   1 
ATOM   2482 O O   . LEU   B 1 55  ? -27.709 -19.923 32.944  1.00 61.04  ?  60  LEU   B O   1 
ATOM   2483 C CB  . LEU   B 1 55  ? -30.100 -21.383 34.696  1.00 62.69  ?  60  LEU   B CB  1 
ATOM   2484 C CG  . LEU   B 1 55  ? -31.036 -21.136 35.898  1.00 62.34  ?  60  LEU   B CG  1 
ATOM   2485 C CD1 . LEU   B 1 55  ? -31.397 -22.443 36.593  1.00 57.91  ?  60  LEU   B CD1 1 
ATOM   2486 C CD2 . LEU   B 1 55  ? -30.425 -20.150 36.884  1.00 59.13  ?  60  LEU   B CD2 1 
ATOM   2487 N N   . LEU   B 1 56  ? -28.904 -21.460 31.808  1.00 65.99  ?  61  LEU   B N   1 
ATOM   2488 C CA  . LEU   B 1 56  ? -27.841 -21.783 30.854  1.00 66.10  ?  61  LEU   B CA  1 
ATOM   2489 C C   . LEU   B 1 56  ? -27.509 -20.598 29.979  1.00 68.81  ?  61  LEU   B C   1 
ATOM   2490 O O   . LEU   B 1 56  ? -26.343 -20.341 29.719  1.00 73.37  ?  61  LEU   B O   1 
ATOM   2491 C CB  . LEU   B 1 56  ? -28.213 -22.982 29.965  1.00 71.18  ?  61  LEU   B CB  1 
ATOM   2492 C CG  . LEU   B 1 56  ? -27.092 -23.565 29.076  1.00 73.50  ?  61  LEU   B CG  1 
ATOM   2493 C CD1 . LEU   B 1 56  ? -26.035 -24.264 29.923  1.00 71.37  ?  61  LEU   B CD1 1 
ATOM   2494 C CD2 . LEU   B 1 56  ? -27.647 -24.518 28.026  1.00 78.14  ?  61  LEU   B CD2 1 
ATOM   2495 N N   . GLU   B 1 57  ? -28.535 -19.894 29.511  1.00 77.34  ?  62  GLU   B N   1 
ATOM   2496 C CA  . GLU   B 1 57  ? -28.350 -18.688 28.713  1.00 79.29  ?  62  GLU   B CA  1 
ATOM   2497 C C   . GLU   B 1 57  ? -27.604 -17.584 29.481  1.00 73.79  ?  62  GLU   B C   1 
ATOM   2498 O O   . GLU   B 1 57  ? -26.746 -16.923 28.907  1.00 72.89  ?  62  GLU   B O   1 
ATOM   2499 C CB  . GLU   B 1 57  ? -29.689 -18.198 28.140  1.00 86.05  ?  62  GLU   B CB  1 
ATOM   2500 C CG  . GLU   B 1 57  ? -29.591 -17.000 27.186  1.00 99.09  ?  62  GLU   B CG  1 
ATOM   2501 C CD  . GLU   B 1 57  ? -28.570 -17.176 26.056  1.00 104.99 ?  62  GLU   B CD  1 
ATOM   2502 O OE1 . GLU   B 1 57  ? -28.548 -18.274 25.456  1.00 109.60 ?  62  GLU   B OE1 1 
ATOM   2503 O OE2 . GLU   B 1 57  ? -27.793 -16.233 25.772  1.00 98.59  ?  62  GLU   B OE2 1 
ATOM   2504 N N   . GLU   B 1 58  ? -27.902 -17.416 30.772  1.00 70.44  ?  63  GLU   B N   1 
ATOM   2505 C CA  . GLU   B 1 58  ? -27.104 -16.526 31.645  1.00 65.77  ?  63  GLU   B CA  1 
ATOM   2506 C C   . GLU   B 1 58  ? -25.665 -16.971 31.818  1.00 63.11  ?  63  GLU   B C   1 
ATOM   2507 O O   . GLU   B 1 58  ? -24.774 -16.130 31.850  1.00 73.54  ?  63  GLU   B O   1 
ATOM   2508 C CB  . GLU   B 1 58  ? -27.750 -16.304 33.028  1.00 70.62  ?  63  GLU   B CB  1 
ATOM   2509 C CG  . GLU   B 1 58  ? -28.481 -14.985 33.091  1.00 79.83  ?  63  GLU   B CG  1 
ATOM   2510 C CD  . GLU   B 1 58  ? -29.306 -14.819 34.346  1.00 83.64  ?  63  GLU   B CD  1 
ATOM   2511 O OE1 . GLU   B 1 58  ? -28.813 -15.132 35.450  1.00 79.22  ?  63  GLU   B OE1 1 
ATOM   2512 O OE2 . GLU   B 1 58  ? -30.470 -14.368 34.238  1.00 93.75  ?  63  GLU   B OE2 1 
ATOM   2513 N N   . ALA   B 1 59  ? -25.444 -18.276 31.941  1.00 62.07  ?  64  ALA   B N   1 
ATOM   2514 C CA  . ALA   B 1 59  ? -24.073 -18.836 31.942  1.00 57.51  ?  64  ALA   B CA  1 
ATOM   2515 C C   . ALA   B 1 59  ? -23.330 -18.619 30.619  1.00 59.31  ?  64  ALA   B C   1 
ATOM   2516 O O   . ALA   B 1 59  ? -22.111 -18.429 30.627  1.00 60.78  ?  64  ALA   B O   1 
ATOM   2517 C CB  . ALA   B 1 59  ? -24.086 -20.314 32.306  1.00 63.64  ?  64  ALA   B CB  1 
ATOM   2518 N N   . LYS   B 1 60  ? -24.060 -18.643 29.497  1.00 64.89  ?  65  LYS   B N   1 
ATOM   2519 C CA  . LYS   B 1 60  ? -23.530 -18.226 28.186  1.00 68.42  ?  65  LYS   B CA  1 
ATOM   2520 C C   . LYS   B 1 60  ? -23.090 -16.767 28.163  1.00 69.69  ?  65  LYS   B C   1 
ATOM   2521 O O   . LYS   B 1 60  ? -22.037 -16.473 27.608  1.00 79.37  ?  65  LYS   B O   1 
ATOM   2522 C CB  . LYS   B 1 60  ? -24.504 -18.550 27.026  1.00 76.84  ?  65  LYS   B CB  1 
ATOM   2523 C CG  . LYS   B 1 60  ? -24.656 -20.046 26.710  1.00 83.95  ?  65  LYS   B CG  1 
ATOM   2524 C CD  . LYS   B 1 60  ? -25.722 -20.367 25.662  1.00 93.19  ?  65  LYS   B CD  1 
ATOM   2525 C CE  . LYS   B 1 60  ? -26.634 -21.496 25.999  0.00 88.98  ?  65  LYS   B CE  1 
ATOM   2526 N NZ  . LYS   B 1 60  ? -27.663 -21.739 24.949  0.00 94.40  ?  65  LYS   B NZ  1 
ATOM   2527 N N   . MET   B 1 61  ? -23.871 -15.878 28.778  1.00 66.11  ?  66  MET   B N   1 
ATOM   2528 C CA  . MET   B 1 61  ? -23.517 -14.454 28.899  1.00 67.98  ?  66  MET   B CA  1 
ATOM   2529 C C   . MET   B 1 61  ? -22.277 -14.243 29.764  1.00 65.50  ?  66  MET   B C   1 
ATOM   2530 O O   . MET   B 1 61  ? -21.403 -13.462 29.392  1.00 66.11  ?  66  MET   B O   1 
ATOM   2531 C CB  . MET   B 1 61  ? -24.696 -13.625 29.442  1.00 73.35  ?  66  MET   B CB  1 
ATOM   2532 C CG  . MET   B 1 61  ? -25.853 -13.470 28.458  1.00 81.68  ?  66  MET   B CG  1 
ATOM   2533 S SD  . MET   B 1 61  ? -27.117 -12.298 28.921  0.00 80.38  ?  66  MET   B SD  1 
ATOM   2534 C CE  . MET   B 1 61  ? -28.464 -13.397 29.351  0.00 81.29  ?  66  MET   B CE  1 
ATOM   2535 N N   . MET   B 1 62  ? -22.210 -14.952 30.896  1.00 63.04  ?  67  MET   B N   1 
ATOM   2536 C CA  . MET   B 1 62  ? -21.019 -14.987 31.757  1.00 61.72  ?  67  MET   B CA  1 
ATOM   2537 C C   . MET   B 1 62  ? -19.744 -15.407 31.026  1.00 62.24  ?  67  MET   B C   1 
ATOM   2538 O O   . MET   B 1 62  ? -18.693 -14.809 31.211  1.00 73.70  ?  67  MET   B O   1 
ATOM   2539 C CB  . MET   B 1 62  ? -21.217 -15.955 32.921  1.00 64.91  ?  67  MET   B CB  1 
ATOM   2540 C CG  . MET   B 1 62  ? -22.170 -15.492 34.003  1.00 69.43  ?  67  MET   B CG  1 
ATOM   2541 S SD  . MET   B 1 62  ? -22.467 -16.824 35.172  1.00 71.37  ?  67  MET   B SD  1 
ATOM   2542 C CE  . MET   B 1 62  ? -24.004 -16.293 35.919  1.00 76.48  ?  67  MET   B CE  1 
ATOM   2543 N N   . ASN   B 1 63  ? -19.873 -16.425 30.191  1.00 64.42  ?  68  ASN   B N   1 
ATOM   2544 C CA  . ASN   B 1 63  ? -18.750 -16.965 29.418  1.00 62.25  ?  68  ASN   B CA  1 
ATOM   2545 C C   . ASN   B 1 63  ? -18.198 -15.988 28.362  1.00 62.90  ?  68  ASN   B C   1 
ATOM   2546 O O   . ASN   B 1 63  ? -17.013 -16.028 28.076  1.00 63.23  ?  68  ASN   B O   1 
ATOM   2547 C CB  . ASN   B 1 63  ? -19.182 -18.280 28.759  1.00 69.33  ?  68  ASN   B CB  1 
ATOM   2548 C CG  . ASN   B 1 63  ? -18.015 -19.128 28.325  1.00 71.69  ?  68  ASN   B CG  1 
ATOM   2549 O OD1 . ASN   B 1 63  ? -17.805 -19.359 27.131  1.00 77.19  ?  68  ASN   B OD1 1 
ATOM   2550 N ND2 . ASN   B 1 63  ? -17.263 -19.633 29.300  1.00 67.90  ?  68  ASN   B ND2 1 
ATOM   2551 N N   . ARG   B 1 64  ? -19.059 -15.132 27.804  1.00 68.09  ?  69  ARG   B N   1 
ATOM   2552 C CA  . ARG   B 1 64  ? -18.663 -14.104 26.819  1.00 70.79  ?  69  ARG   B CA  1 
ATOM   2553 C C   . ARG   B 1 64  ? -17.745 -13.007 27.369  1.00 65.81  ?  69  ARG   B C   1 
ATOM   2554 O O   . ARG   B 1 64  ? -17.007 -12.389 26.599  1.00 73.69  ?  69  ARG   B O   1 
ATOM   2555 C CB  . ARG   B 1 64  ? -19.897 -13.441 26.185  1.00 76.27  ?  69  ARG   B CB  1 
ATOM   2556 C CG  . ARG   B 1 64  ? -20.643 -14.328 25.195  1.00 82.58  ?  69  ARG   B CG  1 
ATOM   2557 C CD  . ARG   B 1 64  ? -21.930 -13.737 24.732  0.00 83.24  ?  69  ARG   B CD  1 
ATOM   2558 N NE  . ARG   B 1 64  ? -21.742 -12.506 23.957  0.00 86.16  ?  69  ARG   B NE  1 
ATOM   2559 C CZ  . ARG   B 1 64  ? -22.691 -11.900 23.235  0.00 90.67  ?  69  ARG   B CZ  1 
ATOM   2560 N NH1 . ARG   B 1 64  ? -23.929 -12.388 23.151  0.00 92.85  ?  69  ARG   B NH1 1 
ATOM   2561 N NH2 . ARG   B 1 64  ? -22.395 -10.789 22.575  0.00 93.51  ?  69  ARG   B NH2 1 
ATOM   2562 N N   . LEU   B 1 65  ? -17.819 -12.746 28.674  1.00 61.49  ?  70  LEU   B N   1 
ATOM   2563 C CA  . LEU   B 1 65  ? -17.033 -11.696 29.335  1.00 62.64  ?  70  LEU   B CA  1 
ATOM   2564 C C   . LEU   B 1 65  ? -15.625 -12.183 29.711  1.00 62.24  ?  70  LEU   B C   1 
ATOM   2565 O O   . LEU   B 1 65  ? -15.396 -12.631 30.833  1.00 66.70  ?  70  LEU   B O   1 
ATOM   2566 C CB  . LEU   B 1 65  ? -17.788 -11.176 30.567  1.00 62.36  ?  70  LEU   B CB  1 
ATOM   2567 C CG  . LEU   B 1 65  ? -19.185 -10.621 30.287  1.00 62.37  ?  70  LEU   B CG  1 
ATOM   2568 C CD1 . LEU   B 1 65  ? -19.928 -10.440 31.599  1.00 59.99  ?  70  LEU   B CD1 1 
ATOM   2569 C CD2 . LEU   B 1 65  ? -19.105 -9.316  29.507  1.00 65.89  ?  70  LEU   B CD2 1 
ATOM   2570 N N   . ARG   B 1 66  ? -14.705 -12.079 28.750  1.00 64.84  ?  71  ARG   B N   1 
ATOM   2571 C CA  . ARG   B 1 66  ? -13.334 -12.570 28.853  1.00 66.34  ?  71  ARG   B CA  1 
ATOM   2572 C C   . ARG   B 1 66  ? -12.352 -11.397 28.835  1.00 64.20  ?  71  ARG   B C   1 
ATOM   2573 O O   . ARG   B 1 66  ? -12.316 -10.618 27.895  1.00 68.47  ?  71  ARG   B O   1 
ATOM   2574 C CB  . ARG   B 1 66  ? -13.037 -13.494 27.683  1.00 73.95  ?  71  ARG   B CB  1 
ATOM   2575 C CG  . ARG   B 1 66  ? -13.888 -14.759 27.667  1.00 81.75  ?  71  ARG   B CG  1 
ATOM   2576 C CD  . ARG   B 1 66  ? -13.520 -15.638 26.474  1.00 93.91  ?  71  ARG   B CD  1 
ATOM   2577 N NE  . ARG   B 1 66  ? -13.890 -17.052 26.632  1.00 97.55  ?  71  ARG   B NE  1 
ATOM   2578 C CZ  . ARG   B 1 66  ? -14.908 -17.695 26.038  1.00 108.27 ?  71  ARG   B CZ  1 
ATOM   2579 N NH1 . ARG   B 1 66  ? -15.764 -17.077 25.210  1.00 120.77 ?  71  ARG   B NH1 1 
ATOM   2580 N NH2 . ARG   B 1 66  ? -15.085 -19.000 26.286  1.00 103.60 ?  71  ARG   B NH2 1 
ATOM   2581 N N   . HIS   B 1 67  ? -11.549 -11.288 29.884  1.00 62.44  ?  72  HIS   B N   1 
ATOM   2582 C CA  . HIS   B 1 67  ? -10.599 -10.191 30.061  1.00 54.05  ?  72  HIS   B CA  1 
ATOM   2583 C C   . HIS   B 1 67  ? -9.641  -10.586 31.176  1.00 52.57  ?  72  HIS   B C   1 
ATOM   2584 O O   . HIS   B 1 67  ? -10.079 -11.169 32.178  1.00 52.37  ?  72  HIS   B O   1 
ATOM   2585 C CB  . HIS   B 1 67  ? -11.354 -8.909  30.424  1.00 55.12  ?  72  HIS   B CB  1 
ATOM   2586 C CG  . HIS   B 1 67  ? -10.482 -7.698  30.548  1.00 60.40  ?  72  HIS   B CG  1 
ATOM   2587 N ND1 . HIS   B 1 67  ? -9.932  -7.057  29.459  1.00 62.23  ?  72  HIS   B ND1 1 
ATOM   2588 C CD2 . HIS   B 1 67  ? -10.084 -6.997  31.632  1.00 60.99  ?  72  HIS   B CD2 1 
ATOM   2589 C CE1 . HIS   B 1 67  ? -9.220  -6.025  29.870  1.00 62.34  ?  72  HIS   B CE1 1 
ATOM   2590 N NE2 . HIS   B 1 67  ? -9.286  -5.974  31.187  1.00 60.22  ?  72  HIS   B NE2 1 
ATOM   2591 N N   . SER   B 1 68  ? -8.357  -10.259 31.020  1.00 50.75  ?  73  SER   B N   1 
ATOM   2592 C CA  . SER   B 1 68  ? -7.307  -10.640 32.005  1.00 52.54  ?  73  SER   B CA  1 
ATOM   2593 C C   . SER   B 1 68  ? -7.539  -10.183 33.463  1.00 49.80  ?  73  SER   B C   1 
ATOM   2594 O O   . SER   B 1 68  ? -7.039  -10.800 34.400  1.00 56.73  ?  73  SER   B O   1 
ATOM   2595 C CB  . SER   B 1 68  ? -5.936  -10.156 31.524  1.00 57.25  ?  73  SER   B CB  1 
ATOM   2596 O OG  . SER   B 1 68  ? -5.970  -8.779  31.212  1.00 64.85  ?  73  SER   B OG  1 
ATOM   2597 N N   . ARG   B 1 69  ? -8.271  -9.083  33.619  1.00 52.02  ?  74  ARG   B N   1 
ATOM   2598 C CA  . ARG   B 1 69  ? -8.708  -8.525  34.909  1.00 50.38  ?  74  ARG   B CA  1 
ATOM   2599 C C   . ARG   B 1 69  ? -10.186 -8.761  35.256  1.00 49.05  ?  74  ARG   B C   1 
ATOM   2600 O O   . ARG   B 1 69  ? -10.740 -8.035  36.081  1.00 53.94  ?  74  ARG   B O   1 
ATOM   2601 C CB  . ARG   B 1 69  ? -8.404  -7.007  34.944  1.00 51.30  ?  74  ARG   B CB  1 
ATOM   2602 C CG  . ARG   B 1 69  ? -7.047  -6.580  34.371  1.00 55.53  ?  74  ARG   B CG  1 
ATOM   2603 C CD  . ARG   B 1 69  ? -5.882  -7.354  34.964  1.00 58.76  ?  74  ARG   B CD  1 
ATOM   2604 N NE  . ARG   B 1 69  ? -4.626  -7.152  34.246  1.00 70.59  ?  74  ARG   B NE  1 
ATOM   2605 C CZ  . ARG   B 1 69  ? -3.526  -7.916  34.367  1.00 70.35  ?  74  ARG   B CZ  1 
ATOM   2606 N NH1 . ARG   B 1 69  ? -3.473  -8.977  35.190  1.00 70.77  ?  74  ARG   B NH1 1 
ATOM   2607 N NH2 . ARG   B 1 69  ? -2.434  -7.599  33.670  1.00 71.80  ?  74  ARG   B NH2 1 
ATOM   2608 N N   . VAL   B 1 70  ? -10.805 -9.780  34.664  1.00 50.03  ?  75  VAL   B N   1 
ATOM   2609 C CA  . VAL   B 1 70  ? -12.179 -10.197 34.988  1.00 48.02  ?  75  VAL   B CA  1 
ATOM   2610 C C   . VAL   B 1 70  ? -12.134 -11.704 35.237  1.00 47.71  ?  75  VAL   B C   1 
ATOM   2611 O O   . VAL   B 1 70  ? -11.480 -12.446 34.497  1.00 52.31  ?  75  VAL   B O   1 
ATOM   2612 C CB  . VAL   B 1 70  ? -13.146 -9.843  33.842  1.00 48.90  ?  75  VAL   B CB  1 
ATOM   2613 C CG1 . VAL   B 1 70  ? -14.548 -10.381 34.091  1.00 50.10  ?  75  VAL   B CG1 1 
ATOM   2614 C CG2 . VAL   B 1 70  ? -13.212 -8.330  33.673  1.00 51.77  ?  75  VAL   B CG2 1 
ATOM   2615 N N   . VAL   B 1 71  ? -12.833 -12.143 36.274  1.00 47.83  ?  76  VAL   B N   1 
ATOM   2616 C CA  . VAL   B 1 71  ? -12.879 -13.550 36.661  1.00 50.55  ?  76  VAL   B CA  1 
ATOM   2617 C C   . VAL   B 1 71  ? -13.556 -14.341 35.543  1.00 55.77  ?  76  VAL   B C   1 
ATOM   2618 O O   . VAL   B 1 71  ? -14.663 -13.992 35.148  1.00 59.00  ?  76  VAL   B O   1 
ATOM   2619 C CB  . VAL   B 1 71  ? -13.625 -13.726 38.007  1.00 46.80  ?  76  VAL   B CB  1 
ATOM   2620 C CG1 . VAL   B 1 71  ? -13.925 -15.183 38.320  1.00 55.82  ?  76  VAL   B CG1 1 
ATOM   2621 C CG2 . VAL   B 1 71  ? -12.781 -13.138 39.131  1.00 48.92  ?  76  VAL   B CG2 1 
ATOM   2622 N N   . LYS   B 1 72  ? -12.881 -15.383 35.047  1.00 50.60  ?  77  LYS   B N   1 
ATOM   2623 C CA  . LYS   B 1 72  ? -13.423 -16.226 33.976  1.00 57.43  ?  77  LYS   B CA  1 
ATOM   2624 C C   . LYS   B 1 72  ? -14.307 -17.311 34.598  1.00 60.64  ?  77  LYS   B C   1 
ATOM   2625 O O   . LYS   B 1 72  ? -13.952 -17.893 35.630  1.00 62.26  ?  77  LYS   B O   1 
ATOM   2626 C CB  . LYS   B 1 72  ? -12.294 -16.850 33.127  1.00 63.84  ?  77  LYS   B CB  1 
ATOM   2627 C CG  . LYS   B 1 72  ? -12.731 -17.385 31.760  1.00 64.55  ?  77  LYS   B CG  1 
ATOM   2628 C CD  . LYS   B 1 72  ? -11.553 -17.824 30.983  0.00 63.88  ?  77  LYS   B CD  1 
ATOM   2629 C CE  . LYS   B 1 72  ? -11.979 -18.349 29.626  0.00 66.74  ?  77  LYS   B CE  1 
ATOM   2630 N NZ  . LYS   B 1 72  ? -10.812 -18.779 28.808  0.00 69.43  ?  77  LYS   B NZ  1 
ATOM   2631 N N   . LEU   B 1 73  ? -15.470 -17.539 33.983  1.00 65.78  ?  78  LEU   B N   1 
ATOM   2632 C CA  . LEU   B 1 73  ? -16.295 -18.712 34.251  1.00 62.77  ?  78  LEU   B CA  1 
ATOM   2633 C C   . LEU   B 1 73  ? -15.683 -19.847 33.451  1.00 58.08  ?  78  LEU   B C   1 
ATOM   2634 O O   . LEU   B 1 73  ? -15.722 -19.828 32.225  1.00 62.61  ?  78  LEU   B O   1 
ATOM   2635 C CB  . LEU   B 1 73  ? -17.756 -18.491 33.818  1.00 63.21  ?  78  LEU   B CB  1 
ATOM   2636 C CG  . LEU   B 1 73  ? -18.747 -19.626 34.135  1.00 65.39  ?  78  LEU   B CG  1 
ATOM   2637 C CD1 . LEU   B 1 73  ? -19.095 -19.632 35.617  1.00 71.59  ?  78  LEU   B CD1 1 
ATOM   2638 C CD2 . LEU   B 1 73  ? -20.012 -19.505 33.311  1.00 69.27  ?  78  LEU   B CD2 1 
ATOM   2639 N N   . LEU   B 1 74  ? -15.117 -20.823 34.150  1.00 56.23  ?  79  LEU   B N   1 
ATOM   2640 C CA  . LEU   B 1 74  ? -14.561 -22.030 33.519  1.00 59.19  ?  79  LEU   B CA  1 
ATOM   2641 C C   . LEU   B 1 74  ? -15.634 -23.023 33.086  1.00 59.92  ?  79  LEU   B C   1 
ATOM   2642 O O   . LEU   B 1 74  ? -15.436 -23.771 32.127  1.00 68.12  ?  79  LEU   B O   1 
ATOM   2643 C CB  . LEU   B 1 74  ? -13.563 -22.717 34.456  1.00 59.11  ?  79  LEU   B CB  1 
ATOM   2644 C CG  . LEU   B 1 74  ? -12.379 -21.852 34.890  1.00 61.82  ?  79  LEU   B CG  1 
ATOM   2645 C CD1 . LEU   B 1 74  ? -11.502 -22.643 35.846  1.00 63.44  ?  79  LEU   B CD1 1 
ATOM   2646 C CD2 . LEU   B 1 74  ? -11.562 -21.350 33.704  1.00 65.41  ?  79  LEU   B CD2 1 
ATOM   2647 N N   . GLY   B 1 75  ? -16.757 -23.033 33.791  1.00 55.44  ?  80  GLY   B N   1 
ATOM   2648 C CA  . GLY   B 1 75  ? -17.889 -23.849 33.402  1.00 60.24  ?  80  GLY   B CA  1 
ATOM   2649 C C   . GLY   B 1 75  ? -19.042 -23.720 34.363  1.00 57.94  ?  80  GLY   B C   1 
ATOM   2650 O O   . GLY   B 1 75  ? -18.994 -22.911 35.287  1.00 57.13  ?  80  GLY   B O   1 
ATOM   2651 N N   . VAL   B 1 76  ? -20.059 -24.545 34.140  1.00 60.45  ?  81  VAL   B N   1 
ATOM   2652 C CA  . VAL   B 1 76  ? -21.300 -24.542 34.925  1.00 59.13  ?  81  VAL   B CA  1 
ATOM   2653 C C   . VAL   B 1 76  ? -21.776 -26.000 35.112  1.00 60.10  ?  81  VAL   B C   1 
ATOM   2654 O O   . VAL   B 1 76  ? -21.669 -26.816 34.182  1.00 55.53  ?  81  VAL   B O   1 
ATOM   2655 C CB  . VAL   B 1 76  ? -22.381 -23.650 34.235  1.00 61.71  ?  81  VAL   B CB  1 
ATOM   2656 C CG1 . VAL   B 1 76  ? -22.792 -24.185 32.859  1.00 64.63  ?  81  VAL   B CG1 1 
ATOM   2657 C CG2 . VAL   B 1 76  ? -23.610 -23.451 35.116  1.00 64.61  ?  81  VAL   B CG2 1 
ATOM   2658 N N   . ILE   B 1 77  ? -22.263 -26.316 36.316  1.00 60.09  ?  82  ILE   B N   1 
ATOM   2659 C CA  . ILE   B 1 77  ? -22.898 -27.610 36.618  1.00 64.45  ?  82  ILE   B CA  1 
ATOM   2660 C C   . ILE   B 1 77  ? -24.387 -27.319 36.726  1.00 67.49  ?  82  ILE   B C   1 
ATOM   2661 O O   . ILE   B 1 77  ? -24.805 -26.539 37.584  1.00 66.15  ?  82  ILE   B O   1 
ATOM   2662 C CB  . ILE   B 1 77  ? -22.384 -28.252 37.928  1.00 66.42  ?  82  ILE   B CB  1 
ATOM   2663 C CG1 . ILE   B 1 77  ? -20.861 -28.433 37.875  1.00 71.12  ?  82  ILE   B CG1 1 
ATOM   2664 C CG2 . ILE   B 1 77  ? -23.049 -29.611 38.172  1.00 66.60  ?  82  ILE   B CG2 1 
ATOM   2665 C CD1 . ILE   B 1 77  ? -20.224 -28.732 39.211  1.00 75.28  ?  82  ILE   B CD1 1 
ATOM   2666 N N   . ILE   B 1 78  ? -25.162 -27.901 35.811  1.00 71.33  ?  83  ILE   B N   1 
ATOM   2667 C CA  . ILE   B 1 78  ? -26.616 -27.837 35.823  1.00 72.42  ?  83  ILE   B CA  1 
ATOM   2668 C C   . ILE   B 1 78  ? -27.038 -29.298 35.887  1.00 72.60  ?  83  ILE   B C   1 
ATOM   2669 O O   . ILE   B 1 78  ? -26.952 -30.021 34.890  1.00 75.28  ?  83  ILE   B O   1 
ATOM   2670 C CB  . ILE   B 1 78  ? -27.167 -27.117 34.566  1.00 80.61  ?  83  ILE   B CB  1 
ATOM   2671 C CG1 . ILE   B 1 78  ? -26.785 -25.636 34.581  1.00 76.39  ?  83  ILE   B CG1 1 
ATOM   2672 C CG2 . ILE   B 1 78  ? -28.689 -27.196 34.482  1.00 91.52  ?  83  ILE   B CG2 1 
ATOM   2673 C CD1 . ILE   B 1 78  ? -27.031 -24.832 33.335  0.00 73.83  ?  83  ILE   B CD1 1 
ATOM   2674 N N   . GLU   B 1 79  ? -27.439 -29.725 37.081  1.00 73.54  ?  84  GLU   B N   1 
ATOM   2675 C CA  . GLU   B 1 79  ? -27.868 -31.101 37.349  1.00 78.48  ?  84  GLU   B CA  1 
ATOM   2676 C C   . GLU   B 1 79  ? -29.210 -31.123 38.060  1.00 84.32  ?  84  GLU   B C   1 
ATOM   2677 O O   . GLU   B 1 79  ? -29.759 -30.067 38.428  1.00 86.26  ?  84  GLU   B O   1 
ATOM   2678 C CB  . GLU   B 1 79  ? -26.794 -31.825 38.165  1.00 78.79  ?  84  GLU   B CB  1 
ATOM   2679 C CG  . GLU   B 1 79  ? -25.553 -32.089 37.323  1.00 81.50  ?  84  GLU   B CG  1 
ATOM   2680 C CD  . GLU   B 1 79  ? -24.471 -32.872 38.035  1.00 79.69  ?  84  GLU   B CD  1 
ATOM   2681 O OE1 . GLU   B 1 79  ? -24.404 -32.850 39.286  1.00 79.24  ?  84  GLU   B OE1 1 
ATOM   2682 O OE2 . GLU   B 1 79  ? -23.663 -33.498 37.318  1.00 82.47  ?  84  GLU   B OE2 1 
ATOM   2683 N N   . GLU   B 1 80  ? -29.748 -32.334 38.219  1.00 83.80  ?  85  GLU   B N   1 
ATOM   2684 C CA  . GLU   B 1 80  ? -30.976 -32.557 38.982  1.00 83.17  ?  85  GLU   B CA  1 
ATOM   2685 C C   . GLU   B 1 80  ? -30.734 -32.154 40.439  1.00 77.93  ?  85  GLU   B C   1 
ATOM   2686 O O   . GLU   B 1 80  ? -30.142 -32.900 41.223  1.00 79.81  ?  85  GLU   B O   1 
ATOM   2687 C CB  . GLU   B 1 80  ? -31.446 -34.016 38.888  1.00 88.82  ?  85  GLU   B CB  1 
ATOM   2688 C CG  . GLU   B 1 80  ? -31.941 -34.395 37.486  0.00 88.80  ?  85  GLU   B CG  1 
ATOM   2689 C CD  . GLU   B 1 80  ? -32.585 -35.769 37.440  0.00 92.15  ?  85  GLU   B CD  1 
ATOM   2690 O OE1 . GLU   B 1 80  ? -31.994 -36.730 37.979  0.00 92.97  ?  85  GLU   B OE1 1 
ATOM   2691 O OE2 . GLU   B 1 80  ? -33.682 -35.891 36.854  0.00 94.18  ?  85  GLU   B OE2 1 
ATOM   2692 N N   . GLY   B 1 81  ? -31.099 -30.908 40.746  1.00 74.67  ?  86  GLY   B N   1 
ATOM   2693 C CA  . GLY   B 1 81  ? -31.065 -30.375 42.098  1.00 74.42  ?  86  GLY   B CA  1 
ATOM   2694 C C   . GLY   B 1 81  ? -29.857 -29.544 42.487  1.00 72.09  ?  86  GLY   B C   1 
ATOM   2695 O O   . GLY   B 1 81  ? -29.969 -28.793 43.429  1.00 68.98  ?  86  GLY   B O   1 
ATOM   2696 N N   . LYS   B 1 82  ? -28.722 -29.693 41.787  1.00 71.03  ?  87  LYS   B N   1 
ATOM   2697 C CA  . LYS   B 1 82  ? -27.474 -28.975 42.071  1.00 68.69  ?  87  LYS   B CA  1 
ATOM   2698 C C   . LYS   B 1 82  ? -27.196 -27.996 40.937  1.00 59.94  ?  87  LYS   B C   1 
ATOM   2699 O O   . LYS   B 1 82  ? -27.261 -28.371 39.758  1.00 58.06  ?  87  LYS   B O   1 
ATOM   2700 C CB  . LYS   B 1 82  ? -26.284 -29.939 42.232  1.00 75.22  ?  87  LYS   B CB  1 
ATOM   2701 C CG  . LYS   B 1 82  ? -25.006 -29.273 42.764  1.00 80.16  ?  87  LYS   B CG  1 
ATOM   2702 C CD  . LYS   B 1 82  ? -23.838 -30.246 42.891  1.00 87.24  ?  87  LYS   B CD  1 
ATOM   2703 C CE  . LYS   B 1 82  ? -22.518 -29.525 43.137  1.00 85.24  ?  87  LYS   B CE  1 
ATOM   2704 N NZ  . LYS   B 1 82  ? -21.380 -30.459 43.190  0.00 86.00  ?  87  LYS   B NZ  1 
ATOM   2705 N N   . TYR   B 1 83  ? -26.901 -26.748 41.310  1.00 54.06  ?  88  TYR   B N   1 
ATOM   2706 C CA  . TYR   B 1 83  ? -26.544 -25.689 40.359  1.00 56.71  ?  88  TYR   B CA  1 
ATOM   2707 C C   . TYR   B 1 83  ? -25.306 -24.958 40.867  1.00 52.09  ?  88  TYR   B C   1 
ATOM   2708 O O   . TYR   B 1 83  ? -25.312 -24.445 41.982  1.00 49.59  ?  88  TYR   B O   1 
ATOM   2709 C CB  . TYR   B 1 83  ? -27.694 -24.698 40.163  1.00 58.89  ?  88  TYR   B CB  1 
ATOM   2710 C CG  . TYR   B 1 83  ? -28.930 -25.312 39.541  1.00 60.09  ?  88  TYR   B CG  1 
ATOM   2711 C CD1 . TYR   B 1 83  ? -29.842 -26.019 40.323  1.00 64.14  ?  88  TYR   B CD1 1 
ATOM   2712 C CD2 . TYR   B 1 83  ? -29.200 -25.181 38.174  1.00 61.79  ?  88  TYR   B CD2 1 
ATOM   2713 C CE1 . TYR   B 1 83  ? -30.974 -26.608 39.770  1.00 68.24  ?  88  TYR   B CE1 1 
ATOM   2714 C CE2 . TYR   B 1 83  ? -30.338 -25.757 37.607  1.00 67.48  ?  88  TYR   B CE2 1 
ATOM   2715 C CZ  . TYR   B 1 83  ? -31.223 -26.470 38.407  1.00 69.05  ?  88  TYR   B CZ  1 
ATOM   2716 O OH  . TYR   B 1 83  ? -32.350 -27.044 37.867  1.00 79.58  ?  88  TYR   B OH  1 
ATOM   2717 N N   . SER   B 1 84  ? -24.254 -24.937 40.051  1.00 47.57  ?  89  SER   B N   1 
ATOM   2718 C CA  . SER   B 1 84  ? -22.949 -24.412 40.451  1.00 48.57  ?  89  SER   B CA  1 
ATOM   2719 C C   . SER   B 1 84  ? -22.287 -23.690 39.307  1.00 49.94  ?  89  SER   B C   1 
ATOM   2720 O O   . SER   B 1 84  ? -22.456 -24.052 38.137  1.00 49.28  ?  89  SER   B O   1 
ATOM   2721 C CB  . SER   B 1 84  ? -22.013 -25.524 40.930  1.00 50.75  ?  89  SER   B CB  1 
ATOM   2722 O OG  . SER   B 1 84  ? -22.542 -26.234 42.048  1.00 54.03  ?  89  SER   B OG  1 
ATOM   2723 N N   . LEU   B 1 85  ? -21.546 -22.651 39.676  1.00 50.93  ?  90  LEU   B N   1 
ATOM   2724 C CA  . LEU   B 1 85  ? -20.677 -21.922 38.781  1.00 47.67  ?  90  LEU   B CA  1 
ATOM   2725 C C   . LEU   B 1 85  ? -19.266 -22.295 39.178  1.00 50.16  ?  90  LEU   B C   1 
ATOM   2726 O O   . LEU   B 1 85  ? -18.953 -22.422 40.380  1.00 53.15  ?  90  LEU   B O   1 
ATOM   2727 C CB  . LEU   B 1 85  ? -20.885 -20.427 38.956  1.00 47.28  ?  90  LEU   B CB  1 
ATOM   2728 C CG  . LEU   B 1 85  ? -22.269 -19.896 38.625  1.00 51.54  ?  90  LEU   B CG  1 
ATOM   2729 C CD1 . LEU   B 1 85  ? -22.348 -18.433 39.039  1.00 50.43  ?  90  LEU   B CD1 1 
ATOM   2730 C CD2 . LEU   B 1 85  ? -22.580 -20.051 37.138  1.00 53.11  ?  90  LEU   B CD2 1 
ATOM   2731 N N   . VAL   B 1 86  ? -18.424 -22.471 38.171  1.00 47.29  ?  91  VAL   B N   1 
ATOM   2732 C CA  . VAL   B 1 86  ? -17.060 -22.901 38.357  1.00 50.20  ?  91  VAL   B CA  1 
ATOM   2733 C C   . VAL   B 1 86  ? -16.177 -21.828 37.748  1.00 48.74  ?  91  VAL   B C   1 
ATOM   2734 O O   . VAL   B 1 86  ? -16.278 -21.539 36.554  1.00 53.30  ?  91  VAL   B O   1 
ATOM   2735 C CB  . VAL   B 1 86  ? -16.855 -24.245 37.672  1.00 60.13  ?  91  VAL   B CB  1 
ATOM   2736 C CG1 . VAL   B 1 86  ? -15.417 -24.668 37.755  1.00 70.02  ?  91  VAL   B CG1 1 
ATOM   2737 C CG2 . VAL   B 1 86  ? -17.738 -25.325 38.307  1.00 60.14  ?  91  VAL   B CG2 1 
ATOM   2738 N N   . MET   B 1 87  ? -15.286 -21.290 38.563  1.00 52.09  ?  92  MET   B N   1 
ATOM   2739 C CA  . MET   B 1 87  ? -14.403 -20.175 38.184  1.00 57.71  ?  92  MET   B CA  1 
ATOM   2740 C C   . MET   B 1 87  ? -12.990 -20.444 38.659  1.00 57.93  ?  92  MET   B C   1 
ATOM   2741 O O   . MET   B 1 87  ? -12.749 -21.401 39.397  1.00 63.46  ?  92  MET   B O   1 
ATOM   2742 C CB  . MET   B 1 87  ? -14.932 -18.867 38.752  1.00 57.16  ?  92  MET   B CB  1 
ATOM   2743 C CG  . MET   B 1 87  ? -14.877 -18.766 40.267  1.00 70.14  ?  92  MET   B CG  1 
ATOM   2744 S SD  . MET   B 1 87  ? -16.326 -17.966 40.983  1.00 80.61  ?  92  MET   B SD  1 
ATOM   2745 C CE  . MET   B 1 87  ? -15.564 -17.362 42.483  1.00 84.79  ?  92  MET   B CE  1 
ATOM   2746 N N   . GLU   B 1 88  ? -12.065 -19.605 38.208  1.00 59.41  ?  93  GLU   B N   1 
ATOM   2747 C CA  . GLU   B 1 88  ? -10.643 -19.827 38.456  1.00 60.88  ?  93  GLU   B CA  1 
ATOM   2748 C C   . GLU   B 1 88  ? -10.227 -19.471 39.884  1.00 55.11  ?  93  GLU   B C   1 
ATOM   2749 O O   . GLU   B 1 88  ? -10.819 -18.604 40.518  1.00 61.31  ?  93  GLU   B O   1 
ATOM   2750 C CB  . GLU   B 1 88  ? -9.765  -19.153 37.392  1.00 72.03  ?  93  GLU   B CB  1 
ATOM   2751 C CG  . GLU   B 1 88  ? -9.804  -17.630 37.306  1.00 79.96  ?  93  GLU   B CG  1 
ATOM   2752 C CD  . GLU   B 1 88  ? -9.558  -17.128 35.885  1.00 79.97  ?  93  GLU   B CD  1 
ATOM   2753 O OE1 . GLU   B 1 88  ? -8.638  -17.635 35.211  1.00 75.55  ?  93  GLU   B OE1 1 
ATOM   2754 O OE2 . GLU   B 1 88  ? -10.294 -16.228 35.439  1.00 78.70  ?  93  GLU   B OE2 1 
ATOM   2755 N N   . TYR   B 1 89  ? -9.217  -20.192 40.372  1.00 52.31  ?  94  TYR   B N   1 
ATOM   2756 C CA  . TYR   B 1 89  ? -8.654  -20.043 41.712  1.00 53.14  ?  94  TYR   B CA  1 
ATOM   2757 C C   . TYR   B 1 89  ? -7.814  -18.765 41.805  1.00 57.49  ?  94  TYR   B C   1 
ATOM   2758 O O   . TYR   B 1 89  ? -7.013  -18.501 40.913  1.00 61.13  ?  94  TYR   B O   1 
ATOM   2759 C CB  . TYR   B 1 89  ? -7.756  -21.248 42.010  1.00 53.93  ?  94  TYR   B CB  1 
ATOM   2760 C CG  . TYR   B 1 89  ? -7.095  -21.255 43.371  1.00 55.78  ?  94  TYR   B CG  1 
ATOM   2761 C CD1 . TYR   B 1 89  ? -7.858  -21.371 44.526  1.00 55.51  ?  94  TYR   B CD1 1 
ATOM   2762 C CD2 . TYR   B 1 89  ? -5.701  -21.146 43.508  1.00 58.67  ?  94  TYR   B CD2 1 
ATOM   2763 C CE1 . TYR   B 1 89  ? -7.269  -21.402 45.792  1.00 59.15  ?  94  TYR   B CE1 1 
ATOM   2764 C CE2 . TYR   B 1 89  ? -5.095  -21.159 44.771  1.00 61.92  ?  94  TYR   B CE2 1 
ATOM   2765 C CZ  . TYR   B 1 89  ? -5.880  -21.297 45.914  1.00 62.91  ?  94  TYR   B CZ  1 
ATOM   2766 O OH  . TYR   B 1 89  ? -5.286  -21.311 47.164  1.00 63.40  ?  94  TYR   B OH  1 
ATOM   2767 N N   . MET   B 1 90  ? -8.007  -18.002 42.886  1.00 60.13  ?  95  MET   B N   1 
ATOM   2768 C CA  . MET   B 1 90  ? -7.251  -16.777 43.184  1.00 55.31  ?  95  MET   B CA  1 
ATOM   2769 C C   . MET   B 1 90  ? -6.683  -16.939 44.591  1.00 57.32  ?  95  MET   B C   1 
ATOM   2770 O O   . MET   B 1 90  ? -7.421  -16.839 45.573  1.00 66.69  ?  95  MET   B O   1 
ATOM   2771 C CB  . MET   B 1 90  ? -8.167  -15.553 43.087  1.00 50.76  ?  95  MET   B CB  1 
ATOM   2772 C CG  . MET   B 1 90  ? -8.843  -15.400 41.725  1.00 53.00  ?  95  MET   B CG  1 
ATOM   2773 S SD  . MET   B 1 90  ? -7.712  -15.157 40.340  1.00 57.26  ?  95  MET   B SD  1 
ATOM   2774 C CE  . MET   B 1 90  ? -7.152  -13.480 40.609  1.00 55.10  ?  95  MET   B CE  1 
ATOM   2775 N N   . GLU   B 1 91  ? -5.382  -17.210 44.672  1.00 54.15  ?  96  GLU   B N   1 
ATOM   2776 C CA  . GLU   B 1 91  ? -4.753  -17.718 45.895  1.00 57.56  ?  96  GLU   B CA  1 
ATOM   2777 C C   . GLU   B 1 91  ? -4.812  -16.791 47.110  1.00 58.33  ?  96  GLU   B C   1 
ATOM   2778 O O   . GLU   B 1 91  ? -5.101  -17.257 48.210  1.00 61.93  ?  96  GLU   B O   1 
ATOM   2779 C CB  . GLU   B 1 91  ? -3.313  -18.125 45.612  1.00 60.77  ?  96  GLU   B CB  1 
ATOM   2780 C CG  . GLU   B 1 91  ? -2.622  -18.798 46.781  1.00 65.95  ?  96  GLU   B CG  1 
ATOM   2781 C CD  . GLU   B 1 91  ? -1.451  -19.674 46.364  1.00 71.39  ?  96  GLU   B CD  1 
ATOM   2782 O OE1 . GLU   B 1 91  ? -1.076  -20.553 47.169  1.00 79.69  ?  96  GLU   B OE1 1 
ATOM   2783 O OE2 . GLU   B 1 91  ? -0.894  -19.501 45.253  1.00 66.69  ?  96  GLU   B OE2 1 
ATOM   2784 N N   . LYS   B 1 92  ? -4.565  -15.494 46.901  1.00 58.59  ?  97  LYS   B N   1 
ATOM   2785 C CA  . LYS   B 1 92  ? -4.524  -14.497 47.994  1.00 57.85  ?  97  LYS   B CA  1 
ATOM   2786 C C   . LYS   B 1 92  ? -5.896  -13.958 48.448  1.00 59.67  ?  97  LYS   B C   1 
ATOM   2787 O O   . LYS   B 1 92  ? -5.958  -13.157 49.392  1.00 71.59  ?  97  LYS   B O   1 
ATOM   2788 C CB  . LYS   B 1 92  ? -3.567  -13.343 47.641  1.00 59.62  ?  97  LYS   B CB  1 
ATOM   2789 C CG  . LYS   B 1 92  ? -2.119  -13.819 47.503  1.00 70.85  ?  97  LYS   B CG  1 
ATOM   2790 C CD  . LYS   B 1 92  ? -1.088  -12.702 47.346  1.00 69.27  ?  97  LYS   B CD  1 
ATOM   2791 C CE  . LYS   B 1 92  ? 0.321   -13.289 47.574  0.00 68.37  ?  97  LYS   B CE  1 
ATOM   2792 N NZ  . LYS   B 1 92  ? 0.631   -13.568 49.004  0.00 71.11  ?  97  LYS   B NZ  1 
ATOM   2793 N N   . GLY   B 1 93  ? -6.980  -14.390 47.802  1.00 54.08  ?  98  GLY   B N   1 
ATOM   2794 C CA  . GLY   B 1 93  ? -8.330  -14.058 48.239  1.00 52.23  ?  98  GLY   B CA  1 
ATOM   2795 C C   . GLY   B 1 93  ? -8.708  -12.683 47.762  1.00 49.33  ?  98  GLY   B C   1 
ATOM   2796 O O   . GLY   B 1 93  ? -8.158  -12.204 46.786  1.00 53.47  ?  98  GLY   B O   1 
ATOM   2797 N N   . ASN   B 1 94  ? -9.640  -12.050 48.464  1.00 52.61  ?  99  ASN   B N   1 
ATOM   2798 C CA  . ASN   B 1 94  ? -10.133 -10.720 48.084  1.00 48.61  ?  99  ASN   B CA  1 
ATOM   2799 C C   . ASN   B 1 94  ? -9.141  -9.622  48.455  1.00 51.21  ?  99  ASN   B C   1 
ATOM   2800 O O   . ASN   B 1 94  ? -8.207  -9.860  49.238  1.00 48.29  ?  99  ASN   B O   1 
ATOM   2801 C CB  . ASN   B 1 94  ? -11.561 -10.468 48.598  1.00 50.14  ?  99  ASN   B CB  1 
ATOM   2802 C CG  . ASN   B 1 94  ? -11.640 -10.176 50.092  1.00 53.78  ?  99  ASN   B CG  1 
ATOM   2803 O OD1 . ASN   B 1 94  ? -10.970 -9.273  50.605  1.00 57.87  ?  99  ASN   B OD1 1 
ATOM   2804 N ND2 . ASN   B 1 94  ? -12.493 -10.914 50.789  1.00 57.65  ?  99  ASN   B ND2 1 
ATOM   2805 N N   . LEU   B 1 95  ? -9.368  -8.431  47.891  1.00 49.63  ?  100 LEU   B N   1 
ATOM   2806 C CA  . LEU   B 1 95  ? -8.458  -7.285  48.056  1.00 48.69  ?  100 LEU   B CA  1 
ATOM   2807 C C   . LEU   B 1 95  ? -8.285  -6.845  49.517  1.00 55.69  ?  100 LEU   B C   1 
ATOM   2808 O O   . LEU   B 1 95  ? -7.161  -6.538  49.942  1.00 57.59  ?  100 LEU   B O   1 
ATOM   2809 C CB  . LEU   B 1 95  ? -8.915  -6.098  47.203  1.00 48.12  ?  100 LEU   B CB  1 
ATOM   2810 C CG  . LEU   B 1 95  ? -8.106  -4.787  47.273  1.00 50.40  ?  100 LEU   B CG  1 
ATOM   2811 C CD1 . LEU   B 1 95  ? -6.643  -5.023  46.925  1.00 51.67  ?  100 LEU   B CD1 1 
ATOM   2812 C CD2 . LEU   B 1 95  ? -8.709  -3.707  46.380  1.00 46.26  ?  100 LEU   B CD2 1 
ATOM   2813 N N   . MET   B 1 96  ? -9.383  -6.823  50.276  1.00 57.27  ?  101 MET   B N   1 
ATOM   2814 C CA  . MET   B 1 96  ? -9.330  -6.423  51.696  1.00 56.15  ?  101 MET   B CA  1 
ATOM   2815 C C   . MET   B 1 96  ? -8.519  -7.377  52.572  1.00 58.90  ?  101 MET   B C   1 
ATOM   2816 O O   . MET   B 1 96  ? -7.798  -6.932  53.462  1.00 61.37  ?  101 MET   B O   1 
ATOM   2817 C CB  . MET   B 1 96  ? -10.737 -6.248  52.267  1.00 57.11  ?  101 MET   B CB  1 
ATOM   2818 C CG  . MET   B 1 96  ? -10.807 -5.576  53.636  1.00 60.40  ?  101 MET   B CG  1 
ATOM   2819 S SD  . MET   B 1 96  ? -9.964  -3.983  53.776  1.00 64.40  ?  101 MET   B SD  1 
ATOM   2820 C CE  . MET   B 1 96  ? -10.957 -3.008  52.654  1.00 64.69  ?  101 MET   B CE  1 
ATOM   2821 N N   . HIS   B 1 97  ? -8.646  -8.680  52.318  1.00 64.07  ?  102 HIS   B N   1 
ATOM   2822 C CA  . HIS   B 1 97  ? -7.799  -9.703  52.951  1.00 58.57  ?  102 HIS   B CA  1 
ATOM   2823 C C   . HIS   B 1 97  ? -6.306  -9.444  52.708  1.00 57.38  ?  102 HIS   B C   1 
ATOM   2824 O O   . HIS   B 1 97  ? -5.503  -9.588  53.625  1.00 64.18  ?  102 HIS   B O   1 
ATOM   2825 C CB  . HIS   B 1 97  ? -8.200  -11.091 52.449  1.00 61.60  ?  102 HIS   B CB  1 
ATOM   2826 C CG  . HIS   B 1 97  ? -7.514  -12.220 53.143  1.00 68.11  ?  102 HIS   B CG  1 
ATOM   2827 N ND1 . HIS   B 1 97  ? -6.465  -12.908 52.575  1.00 72.66  ?  102 HIS   B ND1 1 
ATOM   2828 C CD2 . HIS   B 1 97  ? -7.746  -12.804 54.342  1.00 68.75  ?  102 HIS   B CD2 1 
ATOM   2829 C CE1 . HIS   B 1 97  ? -6.066  -13.858 53.403  1.00 77.29  ?  102 HIS   B CE1 1 
ATOM   2830 N NE2 . HIS   B 1 97  ? -6.829  -13.817 54.481  1.00 75.92  ?  102 HIS   B NE2 1 
ATOM   2831 N N   . VAL   B 1 98  ? -5.960  -9.041  51.489  1.00 58.19  ?  103 VAL   B N   1 
ATOM   2832 C CA  . VAL   B 1 98  ? -4.577  -8.693  51.118  1.00 61.52  ?  103 VAL   B CA  1 
ATOM   2833 C C   . VAL   B 1 98  ? -4.098  -7.408  51.817  1.00 66.58  ?  103 VAL   B C   1 
ATOM   2834 O O   . VAL   B 1 98  ? -2.969  -7.368  52.319  1.00 72.28  ?  103 VAL   B O   1 
ATOM   2835 C CB  . VAL   B 1 98  ? -4.428  -8.611  49.576  1.00 62.11  ?  103 VAL   B CB  1 
ATOM   2836 C CG1 . VAL   B 1 98  ? -3.076  -8.043  49.145  1.00 68.85  ?  103 VAL   B CG1 1 
ATOM   2837 C CG2 . VAL   B 1 98  ? -4.649  -9.997  48.968  1.00 64.44  ?  103 VAL   B CG2 1 
ATOM   2838 N N   . LEU   B 1 99  ? -4.948  -6.382  51.845  1.00 62.64  ?  104 LEU   B N   1 
ATOM   2839 C CA  . LEU   B 1 99  ? -4.631  -5.107  52.525  1.00 62.17  ?  104 LEU   B CA  1 
ATOM   2840 C C   . LEU   B 1 99  ? -4.501  -5.221  54.052  1.00 66.35  ?  104 LEU   B C   1 
ATOM   2841 O O   . LEU   B 1 99  ? -3.626  -4.593  54.640  1.00 73.74  ?  104 LEU   B O   1 
ATOM   2842 C CB  . LEU   B 1 99  ? -5.688  -4.053  52.201  1.00 61.66  ?  104 LEU   B CB  1 
ATOM   2843 C CG  . LEU   B 1 99  ? -5.815  -3.634  50.738  1.00 62.52  ?  104 LEU   B CG  1 
ATOM   2844 C CD1 . LEU   B 1 99  ? -7.121  -2.874  50.531  1.00 59.84  ?  104 LEU   B CD1 1 
ATOM   2845 C CD2 . LEU   B 1 99  ? -4.601  -2.828  50.290  1.00 65.95  ?  104 LEU   B CD2 1 
ATOM   2846 N N   . LYS   B 1 100 ? -5.384  -6.001  54.680  1.00 69.24  ?  105 LYS   B N   1 
ATOM   2847 C CA  . LYS   B 1 100 ? -5.312  -6.294  56.127  1.00 72.13  ?  105 LYS   B CA  1 
ATOM   2848 C C   . LYS   B 1 100 ? -4.215  -7.296  56.550  1.00 79.18  ?  105 LYS   B C   1 
ATOM   2849 O O   . LYS   B 1 100 ? -3.983  -7.437  57.747  1.00 90.67  ?  105 LYS   B O   1 
ATOM   2850 C CB  . LYS   B 1 100 ? -6.688  -6.755  56.670  1.00 72.95  ?  105 LYS   B CB  1 
ATOM   2851 C CG  . LYS   B 1 100 ? -7.685  -5.625  56.921  1.00 68.12  ?  105 LYS   B CG  1 
ATOM   2852 C CD  . LYS   B 1 100 ? -9.031  -6.236  57.311  0.00 65.08  ?  105 LYS   B CD  1 
ATOM   2853 C CE  . LYS   B 1 100 ? -10.072 -5.153  57.529  0.00 64.13  ?  105 LYS   B CE  1 
ATOM   2854 N NZ  . LYS   B 1 100 ? -11.441 -5.728  57.637  0.00 63.47  ?  105 LYS   B NZ  1 
ATOM   2855 N N   . ALA   B 1 101 ? -3.563  -7.985  55.603  1.00 84.92  ?  106 ALA   B N   1 
ATOM   2856 C CA  . ALA   B 1 101 ? -2.465  -8.935  55.910  1.00 90.80  ?  106 ALA   B CA  1 
ATOM   2857 C C   . ALA   B 1 101 ? -1.234  -8.269  56.539  1.00 103.89 ?  106 ALA   B C   1 
ATOM   2858 O O   . ALA   B 1 101 ? -0.969  -7.089  56.289  1.00 103.44 ?  106 ALA   B O   1 
ATOM   2859 C CB  . ALA   B 1 101 ? -2.048  -9.702  54.660  1.00 88.68  ?  106 ALA   B CB  1 
ATOM   2860 N N   . GLU   B 1 102 ? -0.501  -9.048  57.344  1.00 119.15 ?  107 GLU   B N   1 
ATOM   2861 C CA  . GLU   B 1 102 ? 0.693   -8.578  58.092  1.00 126.87 ?  107 GLU   B CA  1 
ATOM   2862 C C   . GLU   B 1 102 ? 1.833   -8.060  57.193  1.00 134.72 ?  107 GLU   B C   1 
ATOM   2863 O O   . GLU   B 1 102 ? 2.533   -7.113  57.572  1.00 149.07 ?  107 GLU   B O   1 
ATOM   2864 C CB  . GLU   B 1 102 ? 1.223   -9.682  59.024  1.00 129.56 ?  107 GLU   B CB  1 
ATOM   2865 C CG  . GLU   B 1 102 ? 0.356   -9.919  60.226  0.00 137.39 ?  107 GLU   B CG  1 
ATOM   2866 C CD  . GLU   B 1 102 ? 0.977   -10.886 61.219  0.00 142.25 ?  107 GLU   B CD  1 
ATOM   2867 O OE1 . GLU   B 1 102 ? 1.441   -11.969 60.797  0.00 142.82 ?  107 GLU   B OE1 1 
ATOM   2868 O OE2 . GLU   B 1 102 ? 0.991   -10.567 62.427  0.00 145.52 ?  107 GLU   B OE2 1 
ATOM   2869 N N   . MET   B 1 103 ? 2.025   -8.691  56.029  1.00 133.54 ?  108 MET   B N   1 
ATOM   2870 C CA  . MET   B 1 103 ? 2.924   -8.185  54.974  1.00 128.96 ?  108 MET   B CA  1 
ATOM   2871 C C   . MET   B 1 103 ? 2.280   -6.969  54.288  1.00 123.09 ?  108 MET   B C   1 
ATOM   2872 O O   . MET   B 1 103 ? 1.198   -7.089  53.699  1.00 111.52 ?  108 MET   B O   1 
ATOM   2873 C CB  . MET   B 1 103 ? 3.219   -9.288  53.936  1.00 128.40 ?  108 MET   B CB  1 
ATOM   2874 C CG  . MET   B 1 103 ? 4.357   -8.992  52.961  1.00 127.48 ?  108 MET   B CG  1 
ATOM   2875 S SD  . MET   B 1 103 ? 3.987   -9.429  51.227  0.00 130.38 ?  108 MET   B SD  1 
ATOM   2876 C CE  . MET   B 1 103 ? 3.593   -11.170 51.379  0.00 130.33 ?  108 MET   B CE  1 
ATOM   2877 N N   . SER   B 1 104 ? 2.944   -5.809  54.393  1.00 120.42 ?  109 SER   B N   1 
ATOM   2878 C CA  . SER   B 1 104 ? 2.469   -4.553  53.795  1.00 106.43 ?  109 SER   B CA  1 
ATOM   2879 C C   . SER   B 1 104 ? 2.764   -4.558  52.294  1.00 100.20 ?  109 SER   B C   1 
ATOM   2880 O O   . SER   B 1 104 ? 3.908   -4.779  51.878  1.00 100.24 ?  109 SER   B O   1 
ATOM   2881 C CB  . SER   B 1 104 ? 3.121   -3.333  54.453  1.00 102.91 ?  109 SER   B CB  1 
ATOM   2882 O OG  . SER   B 1 104 ? 4.527   -3.412  54.427  0.00 107.77 ?  109 SER   B OG  1 
ATOM   2883 N N   . THR   B 1 105 ? 1.720   -4.327  51.498  1.00 88.85  ?  110 THR   B N   1 
ATOM   2884 C CA  . THR   B 1 105 ? 1.800   -4.357  50.032  1.00 80.04  ?  110 THR   B CA  1 
ATOM   2885 C C   . THR   B 1 105 ? 2.387   -3.018  49.546  1.00 77.30  ?  110 THR   B C   1 
ATOM   2886 O O   . THR   B 1 105 ? 1.848   -1.970  49.910  1.00 78.07  ?  110 THR   B O   1 
ATOM   2887 C CB  . THR   B 1 105 ? 0.397   -4.563  49.409  1.00 82.65  ?  110 THR   B CB  1 
ATOM   2888 O OG1 . THR   B 1 105 ? -0.306  -5.603  50.105  1.00 77.93  ?  110 THR   B OG1 1 
ATOM   2889 C CG2 . THR   B 1 105 ? 0.505   -4.934  47.934  1.00 88.04  ?  110 THR   B CG2 1 
ATOM   2890 N N   . PRO   B 1 106 ? 3.486   -3.032  48.746  1.00 79.22  ?  111 PRO   B N   1 
ATOM   2891 C CA  . PRO   B 1 106 ? 4.128   -1.752  48.363  1.00 83.08  ?  111 PRO   B CA  1 
ATOM   2892 C C   . PRO   B 1 106 ? 3.296   -0.869  47.419  1.00 83.43  ?  111 PRO   B C   1 
ATOM   2893 O O   . PRO   B 1 106 ? 2.381   -1.359  46.745  1.00 77.63  ?  111 PRO   B O   1 
ATOM   2894 C CB  . PRO   B 1 106 ? 5.435   -2.190  47.688  1.00 83.78  ?  111 PRO   B CB  1 
ATOM   2895 C CG  . PRO   B 1 106 ? 5.147   -3.545  47.163  1.00 81.42  ?  111 PRO   B CG  1 
ATOM   2896 C CD  . PRO   B 1 106 ? 4.185   -4.180  48.135  1.00 81.88  ?  111 PRO   B CD  1 
ATOM   2897 N N   . LEU   B 1 107 ? 3.615   0.427   47.415  1.00 82.36  ?  112 LEU   B N   1 
ATOM   2898 C CA  . LEU   B 1 107 ? 2.918   1.445   46.591  1.00 78.48  ?  112 LEU   B CA  1 
ATOM   2899 C C   . LEU   B 1 107 ? 2.868   1.104   45.087  1.00 74.86  ?  112 LEU   B C   1 
ATOM   2900 O O   . LEU   B 1 107 ? 1.864   1.368   44.418  1.00 62.90  ?  112 LEU   B O   1 
ATOM   2901 C CB  . LEU   B 1 107 ? 3.589   2.815   46.788  1.00 86.14  ?  112 LEU   B CB  1 
ATOM   2902 C CG  . LEU   B 1 107 ? 3.217   4.025   45.919  1.00 89.85  ?  112 LEU   B CG  1 
ATOM   2903 C CD1 . LEU   B 1 107 ? 1.733   4.308   45.993  1.00 84.41  ?  112 LEU   B CD1 1 
ATOM   2904 C CD2 . LEU   B 1 107 ? 4.000   5.249   46.375  1.00 93.09  ?  112 LEU   B CD2 1 
ATOM   2905 N N   . SER   B 1 108 ? 3.971   0.553   44.573  1.00 77.51  ?  113 SER   B N   1 
ATOM   2906 C CA  . SER   B 1 108 ? 4.093   0.121   43.175  1.00 75.94  ?  113 SER   B CA  1 
ATOM   2907 C C   . SER   B 1 108 ? 3.073   -0.951  42.802  1.00 71.79  ?  113 SER   B C   1 
ATOM   2908 O O   . SER   B 1 108 ? 2.467   -0.870  41.734  1.00 72.28  ?  113 SER   B O   1 
ATOM   2909 C CB  . SER   B 1 108 ? 5.512   -0.398  42.891  1.00 84.46  ?  113 SER   B CB  1 
ATOM   2910 O OG  . SER   B 1 108 ? 5.881   -1.420  43.802  1.00 93.50  ?  113 SER   B OG  1 
ATOM   2911 N N   . VAL   B 1 109 ? 2.879   -1.934  43.685  1.00 69.65  ?  114 VAL   B N   1 
ATOM   2912 C CA  . VAL   B 1 109 ? 1.844   -2.962  43.519  1.00 65.38  ?  114 VAL   B CA  1 
ATOM   2913 C C   . VAL   B 1 109 ? 0.440   -2.360  43.654  1.00 62.91  ?  114 VAL   B C   1 
ATOM   2914 O O   . VAL   B 1 109 ? -0.449  -2.696  42.870  1.00 69.51  ?  114 VAL   B O   1 
ATOM   2915 C CB  . VAL   B 1 109 ? 2.052   -4.145  44.500  1.00 70.88  ?  114 VAL   B CB  1 
ATOM   2916 C CG1 . VAL   B 1 109 ? 0.879   -5.131  44.485  1.00 69.68  ?  114 VAL   B CG1 1 
ATOM   2917 C CG2 . VAL   B 1 109 ? 3.341   -4.886  44.150  1.00 74.01  ?  114 VAL   B CG2 1 
ATOM   2918 N N   . LYS   B 1 110 ? 0.232   -1.498  44.649  1.00 62.33  ?  115 LYS   B N   1 
ATOM   2919 C CA  . LYS   B 1 110 ? -1.062  -0.796  44.832  1.00 62.50  ?  115 LYS   B CA  1 
ATOM   2920 C C   . LYS   B 1 110 ? -1.469  0.033   43.618  1.00 59.08  ?  115 LYS   B C   1 
ATOM   2921 O O   . LYS   B 1 110 ? -2.635  0.014   43.244  1.00 58.73  ?  115 LYS   B O   1 
ATOM   2922 C CB  . LYS   B 1 110 ? -1.052  0.087   46.085  1.00 62.94  ?  115 LYS   B CB  1 
ATOM   2923 C CG  . LYS   B 1 110 ? -1.063  -0.716  47.364  1.00 65.44  ?  115 LYS   B CG  1 
ATOM   2924 C CD  . LYS   B 1 110 ? -0.982  0.174   48.583  1.00 68.48  ?  115 LYS   B CD  1 
ATOM   2925 C CE  . LYS   B 1 110 ? -1.296  -0.606  49.842  1.00 65.54  ?  115 LYS   B CE  1 
ATOM   2926 N NZ  . LYS   B 1 110 ? -1.315  0.298   51.014  1.00 69.62  ?  115 LYS   B NZ  1 
ATOM   2927 N N   . GLY   B 1 111 ? -0.494  0.718   43.007  1.00 62.69  ?  116 GLY   B N   1 
ATOM   2928 C CA  . GLY   B 1 111 ? -0.676  1.418   41.733  1.00 63.32  ?  116 GLY   B CA  1 
ATOM   2929 C C   . GLY   B 1 111 ? -1.135  0.504   40.611  1.00 58.01  ?  116 GLY   B C   1 
ATOM   2930 O O   . GLY   B 1 111 ? -2.096  0.809   39.912  1.00 60.05  ?  116 GLY   B O   1 
ATOM   2931 N N   . ARG   B 1 112 ? -0.481  -0.642  40.494  1.00 59.08  ?  117 ARG   B N   1 
ATOM   2932 C CA  . ARG   B 1 112 ? -0.830  -1.637  39.476  1.00 57.39  ?  117 ARG   B CA  1 
ATOM   2933 C C   . ARG   B 1 112 ? -2.222  -2.227  39.692  1.00 53.55  ?  117 ARG   B C   1 
ATOM   2934 O O   . ARG   B 1 112 ? -2.969  -2.395  38.726  1.00 60.56  ?  117 ARG   B O   1 
ATOM   2935 C CB  . ARG   B 1 112 ? 0.207   -2.746  39.437  1.00 60.79  ?  117 ARG   B CB  1 
ATOM   2936 C CG  . ARG   B 1 112 ? 0.233   -3.505  38.127  1.00 65.21  ?  117 ARG   B CG  1 
ATOM   2937 C CD  . ARG   B 1 112 ? 1.304   -4.586  38.200  1.00 72.49  ?  117 ARG   B CD  1 
ATOM   2938 N NE  . ARG   B 1 112 ? 0.937   -5.605  39.187  1.00 76.96  ?  117 ARG   B NE  1 
ATOM   2939 C CZ  . ARG   B 1 112 ? 1.723   -6.579  39.643  1.00 74.76  ?  117 ARG   B CZ  1 
ATOM   2940 N NH1 . ARG   B 1 112 ? 2.982   -6.722  39.220  1.00 75.24  ?  117 ARG   B NH1 1 
ATOM   2941 N NH2 . ARG   B 1 112 ? 1.228   -7.429  40.543  1.00 81.79  ?  117 ARG   B NH2 1 
ATOM   2942 N N   . ILE   B 1 113 ? -2.558  -2.512  40.949  1.00 50.89  ?  118 ILE   B N   1 
ATOM   2943 C CA  . ILE   B 1 113 ? -3.895  -3.002  41.335  1.00 52.78  ?  118 ILE   B CA  1 
ATOM   2944 C C   . ILE   B 1 113 ? -4.984  -2.041  40.883  1.00 51.40  ?  118 ILE   B C   1 
ATOM   2945 O O   . ILE   B 1 113 ? -5.945  -2.464  40.247  1.00 57.53  ?  118 ILE   B O   1 
ATOM   2946 C CB  . ILE   B 1 113 ? -3.991  -3.265  42.867  1.00 56.33  ?  118 ILE   B CB  1 
ATOM   2947 C CG1 . ILE   B 1 113 ? -3.188  -4.522  43.216  1.00 58.00  ?  118 ILE   B CG1 1 
ATOM   2948 C CG2 . ILE   B 1 113 ? -5.438  -3.462  43.336  1.00 50.34  ?  118 ILE   B CG2 1 
ATOM   2949 C CD1 . ILE   B 1 113 ? -2.783  -4.597  44.660  1.00 61.79  ?  118 ILE   B CD1 1 
ATOM   2950 N N   . ILE   B 1 114 ? -4.808  -0.761  41.203  1.00 52.99  ?  119 ILE   B N   1 
ATOM   2951 C CA  . ILE   B 1 114 ? -5.757  0.301   40.830  1.00 50.25  ?  119 ILE   B CA  1 
ATOM   2952 C C   . ILE   B 1 114 ? -5.916  0.365   39.309  1.00 53.61  ?  119 ILE   B C   1 
ATOM   2953 O O   . ILE   B 1 114 ? -7.043  0.430   38.803  1.00 54.20  ?  119 ILE   B O   1 
ATOM   2954 C CB  . ILE   B 1 114 ? -5.302  1.680   41.378  1.00 51.60  ?  119 ILE   B CB  1 
ATOM   2955 C CG1 . ILE   B 1 114 ? -5.417  1.708   42.906  1.00 52.35  ?  119 ILE   B CG1 1 
ATOM   2956 C CG2 . ILE   B 1 114 ? -6.115  2.844   40.790  1.00 52.99  ?  119 ILE   B CG2 1 
ATOM   2957 C CD1 . ILE   B 1 114 ? -4.496  2.708   43.566  1.00 59.72  ?  119 ILE   B CD1 1 
ATOM   2958 N N   . LEU   B 1 115 ? -4.786  0.357   38.601  1.00 52.80  ?  120 LEU   B N   1 
ATOM   2959 C CA  . LEU   B 1 115 ? -4.786  0.355   37.141  1.00 52.98  ?  120 LEU   B CA  1 
ATOM   2960 C C   . LEU   B 1 115 ? -5.510  -0.870  36.591  1.00 55.06  ?  120 LEU   B C   1 
ATOM   2961 O O   . LEU   B 1 115 ? -6.330  -0.739  35.687  1.00 60.00  ?  120 LEU   B O   1 
ATOM   2962 C CB  . LEU   B 1 115 ? -3.363  0.422   36.592  1.00 50.43  ?  120 LEU   B CB  1 
ATOM   2963 C CG  . LEU   B 1 115 ? -3.162  0.528   35.079  1.00 55.58  ?  120 LEU   B CG  1 
ATOM   2964 C CD1 . LEU   B 1 115 ? -3.922  1.692   34.450  1.00 54.86  ?  120 LEU   B CD1 1 
ATOM   2965 C CD2 . LEU   B 1 115 ? -1.671  0.664   34.791  1.00 60.30  ?  120 LEU   B CD2 1 
ATOM   2966 N N   . GLU   B 1 116 ? -5.228  -2.041  37.161  1.00 52.46  ?  121 GLU   B N   1 
ATOM   2967 C CA  . GLU   B 1 116 ? -5.912  -3.274  36.760  1.00 50.86  ?  121 GLU   B CA  1 
ATOM   2968 C C   . GLU   B 1 116 ? -7.419  -3.253  37.026  1.00 49.02  ?  121 GLU   B C   1 
ATOM   2969 O O   . GLU   B 1 116 ? -8.181  -3.737  36.198  1.00 55.51  ?  121 GLU   B O   1 
ATOM   2970 C CB  . GLU   B 1 116 ? -5.265  -4.499  37.399  1.00 50.79  ?  121 GLU   B CB  1 
ATOM   2971 C CG  . GLU   B 1 116 ? -3.943  -4.875  36.747  1.00 54.50  ?  121 GLU   B CG  1 
ATOM   2972 C CD  . GLU   B 1 116 ? -3.213  -6.042  37.414  1.00 60.65  ?  121 GLU   B CD  1 
ATOM   2973 O OE1 . GLU   B 1 116 ? -3.671  -6.544  38.461  1.00 64.65  ?  121 GLU   B OE1 1 
ATOM   2974 O OE2 . GLU   B 1 116 ? -2.150  -6.459  36.894  1.00 60.54  ?  121 GLU   B OE2 1 
ATOM   2975 N N   . ILE   B 1 117 ? -7.836  -2.690  38.160  1.00 48.54  ?  122 ILE   B N   1 
ATOM   2976 C CA  . ILE   B 1 117 ? -9.278  -2.483  38.460  1.00 45.38  ?  122 ILE   B CA  1 
ATOM   2977 C C   . ILE   B 1 117 ? -9.935  -1.582  37.409  1.00 47.51  ?  122 ILE   B C   1 
ATOM   2978 O O   . ILE   B 1 117 ? -11.029 -1.881  36.957  1.00 49.25  ?  122 ILE   B O   1 
ATOM   2979 C CB  . ILE   B 1 117 ? -9.515  -1.924  39.892  1.00 44.74  ?  122 ILE   B CB  1 
ATOM   2980 C CG1 . ILE   B 1 117 ? -9.136  -2.964  40.956  1.00 45.41  ?  122 ILE   B CG1 1 
ATOM   2981 C CG2 . ILE   B 1 117 ? -10.978 -1.574  40.131  1.00 46.25  ?  122 ILE   B CG2 1 
ATOM   2982 C CD1 . ILE   B 1 117 ? -8.768  -2.346  42.285  1.00 50.60  ?  122 ILE   B CD1 1 
ATOM   2983 N N   . ILE   B 1 118 ? -9.259  -0.492  37.033  1.00 54.60  ?  123 ILE   B N   1 
ATOM   2984 C CA  . ILE   B 1 118 ? -9.746  0.441   35.991  1.00 50.72  ?  123 ILE   B CA  1 
ATOM   2985 C C   . ILE   B 1 118 ? -9.903  -0.284  34.646  1.00 51.58  ?  123 ILE   B C   1 
ATOM   2986 O O   . ILE   B 1 118 ? -10.960 -0.185  34.025  1.00 51.74  ?  123 ILE   B O   1 
ATOM   2987 C CB  . ILE   B 1 118 ? -8.804  1.674   35.830  1.00 51.52  ?  123 ILE   B CB  1 
ATOM   2988 C CG1 . ILE   B 1 118 ? -8.828  2.563   37.090  1.00 49.66  ?  123 ILE   B CG1 1 
ATOM   2989 C CG2 . ILE   B 1 118 ? -9.165  2.519   34.604  1.00 52.84  ?  123 ILE   B CG2 1 
ATOM   2990 C CD1 . ILE   B 1 118 ? -7.535  3.326   37.290  1.00 51.79  ?  123 ILE   B CD1 1 
ATOM   2991 N N   . GLU   B 1 119 ? -8.848  -0.988  34.217  1.00 53.70  ?  124 GLU   B N   1 
ATOM   2992 C CA  . GLU   B 1 119 ? -8.850  -1.821  32.995  1.00 54.01  ?  124 GLU   B CA  1 
ATOM   2993 C C   . GLU   B 1 119 ? -10.058 -2.775  32.966  1.00 56.24  ?  124 GLU   B C   1 
ATOM   2994 O O   . GLU   B 1 119 ? -10.813 -2.815  31.985  1.00 60.54  ?  124 GLU   B O   1 
ATOM   2995 C CB  . GLU   B 1 119 ? -7.561  -2.670  32.890  1.00 55.78  ?  124 GLU   B CB  1 
ATOM   2996 C CG  . GLU   B 1 119 ? -6.278  -1.953  32.476  1.00 56.99  ?  124 GLU   B CG  1 
ATOM   2997 C CD  . GLU   B 1 119 ? -5.038  -2.877  32.467  1.00 65.53  ?  124 GLU   B CD  1 
ATOM   2998 O OE1 . GLU   B 1 119 ? -5.035  -3.989  33.059  1.00 64.60  ?  124 GLU   B OE1 1 
ATOM   2999 O OE2 . GLU   B 1 119 ? -4.025  -2.499  31.855  1.00 72.91  ?  124 GLU   B OE2 1 
ATOM   3000 N N   . GLY   B 1 120 ? -10.231 -3.512  34.062  1.00 55.26  ?  125 GLY   B N   1 
ATOM   3001 C CA  . GLY   B 1 120 ? -11.314 -4.493  34.212  1.00 54.47  ?  125 GLY   B CA  1 
ATOM   3002 C C   . GLY   B 1 120 ? -12.698 -3.868  34.163  1.00 54.20  ?  125 GLY   B C   1 
ATOM   3003 O O   . GLY   B 1 120 ? -13.570 -4.342  33.425  1.00 56.55  ?  125 GLY   B O   1 
ATOM   3004 N N   . MET   B 1 121 ? -12.888 -2.792  34.928  1.00 48.06  ?  126 MET   B N   1 
ATOM   3005 C CA  . MET   B 1 121 ? -14.155 -2.036  34.909  1.00 52.85  ?  126 MET   B CA  1 
ATOM   3006 C C   . MET   B 1 121 ? -14.429 -1.357  33.567  1.00 58.56  ?  126 MET   B C   1 
ATOM   3007 O O   . MET   B 1 121 ? -15.588 -1.287  33.145  1.00 60.71  ?  126 MET   B O   1 
ATOM   3008 C CB  . MET   B 1 121 ? -14.202 -0.984  36.030  1.00 49.82  ?  126 MET   B CB  1 
ATOM   3009 C CG  . MET   B 1 121 ? -14.340 -1.555  37.431  1.00 51.59  ?  126 MET   B CG  1 
ATOM   3010 S SD  . MET   B 1 121 ? -15.764 -2.637  37.673  1.00 61.30  ?  126 MET   B SD  1 
ATOM   3011 C CE  . MET   B 1 121 ? -17.093 -1.569  37.149  1.00 67.86  ?  126 MET   B CE  1 
ATOM   3012 N N   . ALA   B 1 122 ? -13.376 -0.862  32.915  1.00 53.95  ?  127 ALA   B N   1 
ATOM   3013 C CA  . ALA   B 1 122 ? -13.497 -0.291  31.569  1.00 56.91  ?  127 ALA   B CA  1 
ATOM   3014 C C   . ALA   B 1 122 ? -13.956 -1.329  30.547  1.00 55.28  ?  127 ALA   B C   1 
ATOM   3015 O O   . ALA   B 1 122 ? -14.777 -1.012  29.691  1.00 61.84  ?  127 ALA   B O   1 
ATOM   3016 C CB  . ALA   B 1 122 ? -12.185 0.350   31.120  1.00 58.99  ?  127 ALA   B CB  1 
ATOM   3017 N N   . TYR   B 1 123 ? -13.444 -2.556  30.654  1.00 53.48  ?  128 TYR   B N   1 
ATOM   3018 C CA  . TYR   B 1 123 ? -13.894 -3.669  29.799  1.00 55.01  ?  128 TYR   B CA  1 
ATOM   3019 C C   . TYR   B 1 123 ? -15.392 -3.957  29.969  1.00 56.51  ?  128 TYR   B C   1 
ATOM   3020 O O   . TYR   B 1 123 ? -16.117 -4.035  28.977  1.00 60.80  ?  128 TYR   B O   1 
ATOM   3021 C CB  . TYR   B 1 123 ? -13.057 -4.939  30.046  1.00 54.07  ?  128 TYR   B CB  1 
ATOM   3022 C CG  . TYR   B 1 123 ? -13.603 -6.167  29.369  1.00 55.98  ?  128 TYR   B CG  1 
ATOM   3023 C CD1 . TYR   B 1 123 ? -13.333 -6.422  28.022  1.00 56.61  ?  128 TYR   B CD1 1 
ATOM   3024 C CD2 . TYR   B 1 123 ? -14.406 -7.088  30.072  1.00 56.86  ?  128 TYR   B CD2 1 
ATOM   3025 C CE1 . TYR   B 1 123 ? -13.847 -7.556  27.386  1.00 59.87  ?  128 TYR   B CE1 1 
ATOM   3026 C CE2 . TYR   B 1 123 ? -14.930 -8.220  29.443  1.00 57.80  ?  128 TYR   B CE2 1 
ATOM   3027 C CZ  . TYR   B 1 123 ? -14.653 -8.448  28.106  1.00 59.94  ?  128 TYR   B CZ  1 
ATOM   3028 O OH  . TYR   B 1 123 ? -15.162 -9.553  27.484  1.00 68.08  ?  128 TYR   B OH  1 
ATOM   3029 N N   . LEU   B 1 124 ? -15.824 -4.110  31.222  1.00 59.91  ?  129 LEU   B N   1 
ATOM   3030 C CA  . LEU   B 1 124 ? -17.216 -4.465  31.558  1.00 62.53  ?  129 LEU   B CA  1 
ATOM   3031 C C   . LEU   B 1 124 ? -18.227 -3.407  31.113  1.00 61.14  ?  129 LEU   B C   1 
ATOM   3032 O O   . LEU   B 1 124 ? -19.243 -3.734  30.508  1.00 62.63  ?  129 LEU   B O   1 
ATOM   3033 C CB  . LEU   B 1 124 ? -17.366 -4.730  33.065  1.00 66.27  ?  129 LEU   B CB  1 
ATOM   3034 C CG  . LEU   B 1 124 ? -16.655 -5.955  33.669  1.00 65.27  ?  129 LEU   B CG  1 
ATOM   3035 C CD1 . LEU   B 1 124 ? -16.768 -5.919  35.188  1.00 67.15  ?  129 LEU   B CD1 1 
ATOM   3036 C CD2 . LEU   B 1 124 ? -17.211 -7.272  33.143  1.00 63.25  ?  129 LEU   B CD2 1 
ATOM   3037 N N   . HIS   B 1 125 ? -17.914 -2.143  31.375  1.00 62.69  ?  130 HIS   B N   1 
ATOM   3038 C CA  . HIS   B 1 125 ? -18.731 -1.009  30.901  1.00 61.05  ?  130 HIS   B CA  1 
ATOM   3039 C C   . HIS   B 1 125 ? -18.809 -0.956  29.372  1.00 61.51  ?  130 HIS   B C   1 
ATOM   3040 O O   . HIS   B 1 125 ? -19.889 -0.768  28.822  1.00 63.28  ?  130 HIS   B O   1 
ATOM   3041 C CB  . HIS   B 1 125 ? -18.199 0.304   31.466  1.00 60.25  ?  130 HIS   B CB  1 
ATOM   3042 C CG  . HIS   B 1 125 ? -18.494 0.492   32.920  1.00 58.56  ?  130 HIS   B CG  1 
ATOM   3043 N ND1 . HIS   B 1 125 ? -18.441 1.724   33.534  1.00 61.67  ?  130 HIS   B ND1 1 
ATOM   3044 C CD2 . HIS   B 1 125 ? -18.876 -0.385  33.876  1.00 59.12  ?  130 HIS   B CD2 1 
ATOM   3045 C CE1 . HIS   B 1 125 ? -18.758 1.594   34.810  1.00 60.26  ?  130 HIS   B CE1 1 
ATOM   3046 N NE2 . HIS   B 1 125 ? -19.033 0.323   35.043  1.00 62.38  ?  130 HIS   B NE2 1 
ATOM   3047 N N   . GLY   B 1 126 ? -17.676 -1.178  28.708  1.00 61.04  ?  131 GLY   B N   1 
ATOM   3048 C CA  . GLY   B 1 126 ? -17.616 -1.378  27.253  1.00 67.48  ?  131 GLY   B CA  1 
ATOM   3049 C C   . GLY   B 1 126 ? -18.452 -2.524  26.692  1.00 74.87  ?  131 GLY   B C   1 
ATOM   3050 O O   . GLY   B 1 126 ? -18.861 -2.456  25.535  1.00 94.84  ?  131 GLY   B O   1 
ATOM   3051 N N   . LYS   B 1 127 ? -18.672 -3.575  27.493  1.00 72.41  ?  132 LYS   B N   1 
ATOM   3052 C CA  . LYS   B 1 127 ? -19.602 -4.681  27.173  1.00 70.37  ?  132 LYS   B CA  1 
ATOM   3053 C C   . LYS   B 1 127 ? -21.055 -4.483  27.701  1.00 71.94  ?  132 LYS   B C   1 
ATOM   3054 O O   . LYS   B 1 127 ? -21.857 -5.429  27.693  1.00 76.12  ?  132 LYS   B O   1 
ATOM   3055 C CB  . LYS   B 1 127 ? -19.002 -6.028  27.646  1.00 68.93  ?  132 LYS   B CB  1 
ATOM   3056 C CG  . LYS   B 1 127 ? -17.720 -6.442  26.922  1.00 70.86  ?  132 LYS   B CG  1 
ATOM   3057 C CD  . LYS   B 1 127 ? -17.951 -6.965  25.499  1.00 77.60  ?  132 LYS   B CD  1 
ATOM   3058 C CE  . LYS   B 1 127 ? -18.247 -8.463  25.448  1.00 86.56  ?  132 LYS   B CE  1 
ATOM   3059 N NZ  . LYS   B 1 127 ? -18.467 -9.084  24.176  0.00 84.78  ?  132 LYS   B NZ  1 
ATOM   3060 N N   . GLY   B 1 128 ? -21.407 -3.263  28.113  1.00 70.13  ?  133 GLY   B N   1 
ATOM   3061 C CA  . GLY   B 1 128 ? -22.744 -2.942  28.610  1.00 74.08  ?  133 GLY   B CA  1 
ATOM   3062 C C   . GLY   B 1 128 ? -23.124 -3.491  29.969  1.00 73.33  ?  133 GLY   B C   1 
ATOM   3063 O O   . GLY   B 1 128 ? -24.313 -3.596  30.274  1.00 77.10  ?  133 GLY   B O   1 
ATOM   3064 N N   . VAL   B 1 129 ? -22.122 -3.824  30.784  1.00 70.70  ?  134 VAL   B N   1 
ATOM   3065 C CA  . VAL   B 1 129 ? -22.309 -4.470  32.086  1.00 70.78  ?  134 VAL   B CA  1 
ATOM   3066 C C   . VAL   B 1 129 ? -22.025 -3.414  33.145  1.00 70.58  ?  134 VAL   B C   1 
ATOM   3067 O O   . VAL   B 1 129 ? -20.892 -2.950  33.250  1.00 78.74  ?  134 VAL   B O   1 
ATOM   3068 C CB  . VAL   B 1 129 ? -21.341 -5.671  32.273  1.00 68.86  ?  134 VAL   B CB  1 
ATOM   3069 C CG1 . VAL   B 1 129 ? -21.448 -6.279  33.678  1.00 70.42  ?  134 VAL   B CG1 1 
ATOM   3070 C CG2 . VAL   B 1 129 ? -21.581 -6.723  31.193  1.00 67.64  ?  134 VAL   B CG2 1 
ATOM   3071 N N   . ILE   B 1 130 ? -23.057 -3.032  33.895  1.00 70.08  ?  135 ILE   B N   1 
ATOM   3072 C CA  . ILE   B 1 130 ? -22.902 -2.292  35.142  1.00 67.12  ?  135 ILE   B CA  1 
ATOM   3073 C C   . ILE   B 1 130 ? -22.728 -3.351  36.243  1.00 67.02  ?  135 ILE   B C   1 
ATOM   3074 O O   . ILE   B 1 130 ? -23.528 -4.294  36.345  1.00 73.03  ?  135 ILE   B O   1 
ATOM   3075 C CB  . ILE   B 1 130 ? -24.124 -1.383  35.440  1.00 67.27  ?  135 ILE   B CB  1 
ATOM   3076 C CG1 . ILE   B 1 130 ? -24.330 -0.356  34.314  1.00 66.90  ?  135 ILE   B CG1 1 
ATOM   3077 C CG2 . ILE   B 1 130 ? -23.946 -0.633  36.755  1.00 65.42  ?  135 ILE   B CG2 1 
ATOM   3078 C CD1 . ILE   B 1 130 ? -25.623 0.313   34.219  0.00 67.58  ?  135 ILE   B CD1 1 
ATOM   3079 N N   . HIS   B 1 131 ? -21.685 -3.185  37.059  1.00 62.21  ?  136 HIS   B N   1 
ATOM   3080 C CA  . HIS   B 1 131 ? -21.423 -4.092  38.184  1.00 60.90  ?  136 HIS   B CA  1 
ATOM   3081 C C   . HIS   B 1 131 ? -22.504 -4.026  39.260  1.00 63.52  ?  136 HIS   B C   1 
ATOM   3082 O O   . HIS   B 1 131 ? -22.985 -5.066  39.716  1.00 68.68  ?  136 HIS   B O   1 
ATOM   3083 C CB  . HIS   B 1 131 ? -20.064 -3.819  38.825  1.00 56.94  ?  136 HIS   B CB  1 
ATOM   3084 C CG  . HIS   B 1 131 ? -19.491 -5.004  39.531  1.00 61.29  ?  136 HIS   B CG  1 
ATOM   3085 N ND1 . HIS   B 1 131 ? -20.090 -5.599  40.622  1.00 66.35  ?  136 HIS   B ND1 1 
ATOM   3086 C CD2 . HIS   B 1 131 ? -18.368 -5.718  39.286  1.00 64.38  ?  136 HIS   B CD2 1 
ATOM   3087 C CE1 . HIS   B 1 131 ? -19.359 -6.624  41.022  1.00 63.98  ?  136 HIS   B CE1 1 
ATOM   3088 N NE2 . HIS   B 1 131 ? -18.310 -6.720  40.226  1.00 65.97  ?  136 HIS   B NE2 1 
ATOM   3089 N N   . LYS   B 1 132 ? -22.834 -2.802  39.681  1.00 62.14  ?  137 LYS   B N   1 
ATOM   3090 C CA  . LYS   B 1 132 ? -23.824 -2.499  40.745  1.00 67.46  ?  137 LYS   B CA  1 
ATOM   3091 C C   . LYS   B 1 132 ? -23.336 -2.756  42.197  1.00 66.75  ?  137 LYS   B C   1 
ATOM   3092 O O   . LYS   B 1 132 ? -23.978 -2.290  43.133  1.00 62.90  ?  137 LYS   B O   1 
ATOM   3093 C CB  . LYS   B 1 132 ? -25.189 -3.196  40.518  1.00 73.62  ?  137 LYS   B CB  1 
ATOM   3094 C CG  . LYS   B 1 132 ? -25.772 -3.119  39.097  1.00 75.67  ?  137 LYS   B CG  1 
ATOM   3095 C CD  . LYS   B 1 132 ? -26.795 -4.222  38.834  1.00 76.83  ?  137 LYS   B CD  1 
ATOM   3096 C CE  . LYS   B 1 132 ? -27.160 -4.319  37.362  1.00 83.30  ?  137 LYS   B CE  1 
ATOM   3097 N NZ  . LYS   B 1 132 ? -28.097 -5.376  37.007  0.00 84.85  ?  137 LYS   B NZ  1 
ATOM   3098 N N   . ASP   B 1 133 ? -22.184 -3.413  42.372  1.00 66.25  ?  138 ASP   B N   1 
ATOM   3099 C CA  . ASP   B 1 133 ? -21.732 -3.966  43.664  1.00 59.93  ?  138 ASP   B CA  1 
ATOM   3100 C C   . ASP   B 1 133 ? -20.210 -4.170  43.684  1.00 49.44  ?  138 ASP   B C   1 
ATOM   3101 O O   . ASP   B 1 133 ? -19.700 -5.213  44.092  1.00 54.90  ?  138 ASP   B O   1 
ATOM   3102 C CB  . ASP   B 1 133 ? -22.494 -5.271  44.000  1.00 68.55  ?  138 ASP   B CB  1 
ATOM   3103 C CG  . ASP   B 1 133 ? -22.346 -5.703  45.491  1.00 74.54  ?  138 ASP   B CG  1 
ATOM   3104 O OD1 . ASP   B 1 133 ? -22.148 -4.838  46.391  1.00 64.14  ?  138 ASP   B OD1 1 
ATOM   3105 O OD2 . ASP   B 1 133 ? -22.423 -6.928  45.749  1.00 77.30  ?  138 ASP   B OD2 1 
ATOM   3106 N N   . LEU   B 1 134 ? -19.492 -3.139  43.255  1.00 47.58  ?  139 LEU   B N   1 
ATOM   3107 C CA  . LEU   B 1 134 ? -18.036 -3.159  43.212  1.00 50.58  ?  139 LEU   B CA  1 
ATOM   3108 C C   . LEU   B 1 134 ? -17.548 -2.862  44.623  1.00 49.90  ?  139 LEU   B C   1 
ATOM   3109 O O   . LEU   B 1 134 ? -17.959 -1.879  45.232  1.00 53.26  ?  139 LEU   B O   1 
ATOM   3110 C CB  . LEU   B 1 134 ? -17.485 -2.134  42.213  1.00 53.70  ?  139 LEU   B CB  1 
ATOM   3111 C CG  . LEU   B 1 134 ? -15.964 -1.990  42.104  1.00 53.23  ?  139 LEU   B CG  1 
ATOM   3112 C CD1 . LEU   B 1 134 ? -15.331 -3.265  41.565  1.00 56.31  ?  139 LEU   B CD1 1 
ATOM   3113 C CD2 . LEU   B 1 134 ? -15.624 -0.804  41.220  1.00 55.78  ?  139 LEU   B CD2 1 
ATOM   3114 N N   . LYS   B 1 135 ? -16.679 -3.728  45.135  1.00 49.34  ?  140 LYS   B N   1 
ATOM   3115 C CA  . LYS   B 1 135 ? -16.116 -3.590  46.491  1.00 47.51  ?  140 LYS   B CA  1 
ATOM   3116 C C   . LYS   B 1 135 ? -14.884 -4.482  46.611  1.00 45.97  ?  140 LYS   B C   1 
ATOM   3117 O O   . LYS   B 1 135 ? -14.650 -5.303  45.721  1.00 43.96  ?  140 LYS   B O   1 
ATOM   3118 C CB  . LYS   B 1 135 ? -17.176 -3.941  47.541  1.00 49.71  ?  140 LYS   B CB  1 
ATOM   3119 C CG  . LYS   B 1 135 ? -17.888 -5.252  47.289  1.00 56.85  ?  140 LYS   B CG  1 
ATOM   3120 C CD  . LYS   B 1 135 ? -19.082 -5.417  48.195  1.00 60.03  ?  140 LYS   B CD  1 
ATOM   3121 C CE  . LYS   B 1 135 ? -19.730 -6.770  47.962  1.00 64.53  ?  140 LYS   B CE  1 
ATOM   3122 N NZ  . LYS   B 1 135 ? -20.992 -6.895  48.737  1.00 74.82  ?  140 LYS   B NZ  1 
ATOM   3123 N N   . PRO   B 1 136 ? -14.078 -4.330  47.683  1.00 47.53  ?  141 PRO   B N   1 
ATOM   3124 C CA  . PRO   B 1 136 ? -12.915 -5.206  47.856  1.00 50.03  ?  141 PRO   B CA  1 
ATOM   3125 C C   . PRO   B 1 136 ? -13.214 -6.712  47.872  1.00 51.39  ?  141 PRO   B C   1 
ATOM   3126 O O   . PRO   B 1 136 ? -12.434 -7.454  47.299  1.00 56.45  ?  141 PRO   B O   1 
ATOM   3127 C CB  . PRO   B 1 136 ? -12.331 -4.742  49.189  1.00 51.34  ?  141 PRO   B CB  1 
ATOM   3128 C CG  . PRO   B 1 136 ? -12.662 -3.297  49.222  1.00 50.24  ?  141 PRO   B CG  1 
ATOM   3129 C CD  . PRO   B 1 136 ? -14.054 -3.233  48.668  1.00 47.68  ?  141 PRO   B CD  1 
ATOM   3130 N N   . GLU   B 1 137 ? -14.337 -7.126  48.466  1.00 54.80  ?  142 GLU   B N   1 
ATOM   3131 C CA  . GLU   B 1 137 ? -14.831 -8.523  48.390  1.00 57.89  ?  142 GLU   B CA  1 
ATOM   3132 C C   . GLU   B 1 137 ? -14.989 -9.096  46.970  1.00 52.37  ?  142 GLU   B C   1 
ATOM   3133 O O   . GLU   B 1 137 ? -14.814 -10.297 46.778  1.00 58.61  ?  142 GLU   B O   1 
ATOM   3134 C CB  . GLU   B 1 137 ? -16.166 -8.675  49.149  1.00 70.08  ?  142 GLU   B CB  1 
ATOM   3135 C CG  . GLU   B 1 137 ? -16.009 -9.098  50.596  1.00 81.60  ?  142 GLU   B CG  1 
ATOM   3136 C CD  . GLU   B 1 137 ? -17.346 -9.145  51.314  1.00 96.64  ?  142 GLU   B CD  1 
ATOM   3137 O OE1 . GLU   B 1 137 ? -17.838 -8.057  51.706  1.00 105.54 ?  142 GLU   B OE1 1 
ATOM   3138 O OE2 . GLU   B 1 137 ? -17.905 -10.258 51.477  1.00 100.71 ?  142 GLU   B OE2 1 
ATOM   3139 N N   . ASN   B 1 138 ? -15.331 -8.235  46.012  1.00 51.08  ?  143 ASN   B N   1 
ATOM   3140 C CA  . ASN   B 1 138 ? -15.440 -8.589  44.578  1.00 48.38  ?  143 ASN   B CA  1 
ATOM   3141 C C   . ASN   B 1 138 ? -14.175 -8.302  43.726  1.00 44.57  ?  143 ASN   B C   1 
ATOM   3142 O O   . ASN   B 1 138 ? -14.233 -8.350  42.497  1.00 48.21  ?  143 ASN   B O   1 
ATOM   3143 C CB  . ASN   B 1 138 ? -16.679 -7.882  43.980  1.00 50.08  ?  143 ASN   B CB  1 
ATOM   3144 C CG  . ASN   B 1 138 ? -17.976 -8.646  44.224  1.00 53.93  ?  143 ASN   B CG  1 
ATOM   3145 O OD1 . ASN   B 1 138 ? -17.986 -9.878  44.302  1.00 52.30  ?  143 ASN   B OD1 1 
ATOM   3146 N ND2 . ASN   B 1 138 ? -19.091 -7.915  44.316  1.00 53.99  ?  143 ASN   B ND2 1 
ATOM   3147 N N   . ILE   B 1 139 ? -13.037 -8.050  44.372  1.00 41.39  ?  144 ILE   B N   1 
ATOM   3148 C CA  . ILE   B 1 139 ? -11.754 -7.822  43.704  1.00 45.36  ?  144 ILE   B CA  1 
ATOM   3149 C C   . ILE   B 1 139 ? -10.854 -8.932  44.231  1.00 49.38  ?  144 ILE   B C   1 
ATOM   3150 O O   . ILE   B 1 139 ? -10.360 -8.838  45.361  1.00 52.80  ?  144 ILE   B O   1 
ATOM   3151 C CB  . ILE   B 1 139 ? -11.188 -6.415  44.035  1.00 46.00  ?  144 ILE   B CB  1 
ATOM   3152 C CG1 . ILE   B 1 139 ? -12.085 -5.338  43.412  1.00 47.33  ?  144 ILE   B CG1 1 
ATOM   3153 C CG2 . ILE   B 1 139 ? -9.747  -6.245  43.538  1.00 46.36  ?  144 ILE   B CG2 1 
ATOM   3154 C CD1 . ILE   B 1 139 ? -11.860 -3.939  43.954  1.00 50.39  ?  144 ILE   B CD1 1 
ATOM   3155 N N   . LEU   B 1 140 ? -10.705 -9.992  43.433  1.00 48.34  ?  145 LEU   B N   1 
ATOM   3156 C CA  . LEU   B 1 140 ? -9.907  -11.162 43.812  1.00 50.13  ?  145 LEU   B CA  1 
ATOM   3157 C C   . LEU   B 1 140 ? -8.465  -10.969 43.372  1.00 51.54  ?  145 LEU   B C   1 
ATOM   3158 O O   . LEU   B 1 140 ? -8.223  -10.278 42.391  1.00 56.00  ?  145 LEU   B O   1 
ATOM   3159 C CB  . LEU   B 1 140 ? -10.502 -12.433 43.202  1.00 50.12  ?  145 LEU   B CB  1 
ATOM   3160 C CG  . LEU   B 1 140 ? -11.997 -12.676 43.458  1.00 53.47  ?  145 LEU   B CG  1 
ATOM   3161 C CD1 . LEU   B 1 140 ? -12.435 -13.999 42.846  1.00 52.03  ?  145 LEU   B CD1 1 
ATOM   3162 C CD2 . LEU   B 1 140 ? -12.326 -12.679 44.947  1.00 55.92  ?  145 LEU   B CD2 1 
ATOM   3163 N N   . VAL   B 1 141 ? -7.536  -11.581 44.107  1.00 51.15  ?  146 VAL   B N   1 
ATOM   3164 C CA  . VAL   B 1 141 ? -6.085  -11.338 43.972  1.00 52.02  ?  146 VAL   B CA  1 
ATOM   3165 C C   . VAL   B 1 141 ? -5.364  -12.687 43.867  1.00 56.43  ?  146 VAL   B C   1 
ATOM   3166 O O   . VAL   B 1 141 ? -5.553  -13.563 44.730  1.00 59.88  ?  146 VAL   B O   1 
ATOM   3167 C CB  . VAL   B 1 141 ? -5.522  -10.569 45.199  1.00 52.84  ?  146 VAL   B CB  1 
ATOM   3168 C CG1 . VAL   B 1 141 ? -4.081  -10.129 44.960  1.00 54.01  ?  146 VAL   B CG1 1 
ATOM   3169 C CG2 . VAL   B 1 141 ? -6.377  -9.356  45.549  1.00 52.57  ?  146 VAL   B CG2 1 
ATOM   3170 N N   . ASP   B 1 142 ? -4.548  -12.851 42.824  1.00 56.67  ?  147 ASP   B N   1 
ATOM   3171 C CA  . ASP   B 1 142 ? -3.738  -14.077 42.636  1.00 58.17  ?  147 ASP   B CA  1 
ATOM   3172 C C   . ASP   B 1 142 ? -2.413  -14.005 43.397  1.00 63.09  ?  147 ASP   B C   1 
ATOM   3173 O O   . ASP   B 1 142 ? -2.122  -12.997 44.031  1.00 65.03  ?  147 ASP   B O   1 
ATOM   3174 C CB  . ASP   B 1 142 ? -3.573  -14.430 41.142  1.00 57.67  ?  147 ASP   B CB  1 
ATOM   3175 C CG  . ASP   B 1 142 ? -2.680  -13.478 40.367  1.00 59.29  ?  147 ASP   B CG  1 
ATOM   3176 O OD1 . ASP   B 1 142 ? -1.829  -12.770 40.941  1.00 64.57  ?  147 ASP   B OD1 1 
ATOM   3177 O OD2 . ASP   B 1 142 ? -2.846  -13.462 39.131  1.00 63.67  ?  147 ASP   B OD2 1 
ATOM   3178 N N   . ASN   B 1 143 ? -1.614  -15.070 43.320  1.00 74.04  ?  148 ASN   B N   1 
ATOM   3179 C CA  . ASN   B 1 143 ? -0.352  -15.167 44.081  1.00 73.44  ?  148 ASN   B CA  1 
ATOM   3180 C C   . ASN   B 1 143 ? 0.705   -14.121 43.680  1.00 75.57  ?  148 ASN   B C   1 
ATOM   3181 O O   . ASN   B 1 143 ? 1.475   -13.686 44.535  1.00 80.11  ?  148 ASN   B O   1 
ATOM   3182 C CB  . ASN   B 1 143 ? 0.230   -16.583 43.977  1.00 71.39  ?  148 ASN   B CB  1 
ATOM   3183 C CG  . ASN   B 1 143 ? 1.128   -16.942 45.147  1.00 70.96  ?  148 ASN   B CG  1 
ATOM   3184 O OD1 . ASN   B 1 143 ? 0.774   -16.713 46.300  1.00 75.19  ?  148 ASN   B OD1 1 
ATOM   3185 N ND2 . ASN   B 1 143 ? 2.283   -17.534 44.859  1.00 73.06  ?  148 ASN   B ND2 1 
ATOM   3186 N N   . ASP   B 1 144 ? 0.698   -13.696 42.409  1.00 71.25  ?  149 ASP   B N   1 
ATOM   3187 C CA  . ASP   B 1 144 ? 1.568   -12.614 41.904  1.00 70.20  ?  149 ASP   B CA  1 
ATOM   3188 C C   . ASP   B 1 144 ? 0.941   -11.200 42.021  1.00 66.04  ?  149 ASP   B C   1 
ATOM   3189 O O   . ASP   B 1 144 ? 1.330   -10.296 41.277  1.00 77.20  ?  149 ASP   B O   1 
ATOM   3190 C CB  . ASP   B 1 144 ? 1.939   -12.877 40.432  1.00 75.43  ?  149 ASP   B CB  1 
ATOM   3191 C CG  . ASP   B 1 144 ? 2.607   -14.214 40.210  1.00 95.54  ?  149 ASP   B CG  1 
ATOM   3192 O OD1 . ASP   B 1 144 ? 3.526   -14.590 40.976  1.00 111.77 ?  149 ASP   B OD1 1 
ATOM   3193 O OD2 . ASP   B 1 144 ? 2.235   -14.877 39.214  1.00 107.57 ?  149 ASP   B OD2 1 
ATOM   3194 N N   . PHE   B 1 145 ? -0.032  -11.004 42.920  1.00 56.17  ?  150 PHE   B N   1 
ATOM   3195 C CA  . PHE   B 1 145 ? -0.681  -9.700  43.176  1.00 55.03  ?  150 PHE   B CA  1 
ATOM   3196 C C   . PHE   B 1 145 ? -1.442  -9.057  42.007  1.00 55.50  ?  150 PHE   B C   1 
ATOM   3197 O O   . PHE   B 1 145 ? -1.774  -7.865  42.080  1.00 63.68  ?  150 PHE   B O   1 
ATOM   3198 C CB  . PHE   B 1 145 ? 0.314   -8.705  43.822  1.00 56.17  ?  150 PHE   B CB  1 
ATOM   3199 C CG  . PHE   B 1 145 ? 0.680   -9.063  45.224  1.00 58.89  ?  150 PHE   B CG  1 
ATOM   3200 C CD1 . PHE   B 1 145 ? -0.137  -8.656  46.285  1.00 57.96  ?  150 PHE   B CD1 1 
ATOM   3201 C CD2 . PHE   B 1 145 ? 1.823   -9.831  45.505  1.00 62.07  ?  150 PHE   B CD2 1 
ATOM   3202 C CE1 . PHE   B 1 145 ? 0.189   -8.989  47.606  1.00 62.65  ?  150 PHE   B CE1 1 
ATOM   3203 C CE2 . PHE   B 1 145 ? 2.144   -10.175 46.820  1.00 66.90  ?  150 PHE   B CE2 1 
ATOM   3204 C CZ  . PHE   B 1 145 ? 1.328   -9.753  47.873  1.00 66.59  ?  150 PHE   B CZ  1 
ATOM   3205 N N   . HIS   B 1 146 ? -1.748  -9.826  40.956  1.00 53.60  ?  151 HIS   B N   1 
ATOM   3206 C CA  . HIS   B 1 146 ? -2.623  -9.355  39.884  1.00 52.82  ?  151 HIS   B CA  1 
ATOM   3207 C C   . HIS   B 1 146 ? -4.053  -9.621  40.296  1.00 49.18  ?  151 HIS   B C   1 
ATOM   3208 O O   . HIS   B 1 146 ? -4.340  -10.637 40.935  1.00 56.37  ?  151 HIS   B O   1 
ATOM   3209 C CB  . HIS   B 1 146 ? -2.325  -10.033 38.555  1.00 53.41  ?  151 HIS   B CB  1 
ATOM   3210 C CG  . HIS   B 1 146 ? -0.950  -9.761  38.045  1.00 57.86  ?  151 HIS   B CG  1 
ATOM   3211 N ND1 . HIS   B 1 146 ? -0.598  -8.566  37.456  1.00 57.25  ?  151 HIS   B ND1 1 
ATOM   3212 C CD2 . HIS   B 1 146 ? 0.164   -10.523 38.048  1.00 61.25  ?  151 HIS   B CD2 1 
ATOM   3213 C CE1 . HIS   B 1 146 ? 0.670   -8.611  37.100  1.00 63.57  ?  151 HIS   B CE1 1 
ATOM   3214 N NE2 . HIS   B 1 146 ? 1.157   -9.788  37.448  1.00 66.11  ?  151 HIS   B NE2 1 
ATOM   3215 N N   . ILE   B 1 147 ? -4.939  -8.703  39.921  1.00 49.75  ?  152 ILE   B N   1 
ATOM   3216 C CA  . ILE   B 1 147 ? -6.338  -8.747  40.330  1.00 49.67  ?  152 ILE   B CA  1 
ATOM   3217 C C   . ILE   B 1 147 ? -7.264  -9.145  39.194  1.00 50.55  ?  152 ILE   B C   1 
ATOM   3218 O O   . ILE   B 1 147 ? -6.908  -9.050  38.020  1.00 50.86  ?  152 ILE   B O   1 
ATOM   3219 C CB  . ILE   B 1 147 ? -6.834  -7.428  40.997  1.00 48.46  ?  152 ILE   B CB  1 
ATOM   3220 C CG1 . ILE   B 1 147 ? -6.936  -6.246  40.016  1.00 49.04  ?  152 ILE   B CG1 1 
ATOM   3221 C CG2 . ILE   B 1 147 ? -5.943  -7.089  42.167  1.00 49.66  ?  152 ILE   B CG2 1 
ATOM   3222 C CD1 . ILE   B 1 147 ? -8.328  -6.014  39.450  1.00 50.16  ?  152 ILE   B CD1 1 
ATOM   3223 N N   . LYS   B 1 148 ? -8.451  -9.600  39.592  1.00 57.23  ?  153 LYS   B N   1 
ATOM   3224 C CA  . LYS   B 1 148 ? -9.557  -9.917  38.694  1.00 55.89  ?  153 LYS   B CA  1 
ATOM   3225 C C   . LYS   B 1 148 ? -10.867 -9.521  39.366  1.00 56.07  ?  153 LYS   B C   1 
ATOM   3226 O O   . LYS   B 1 148 ? -11.067 -9.808  40.550  1.00 63.11  ?  153 LYS   B O   1 
ATOM   3227 C CB  . LYS   B 1 148 ? -9.580  -11.407 38.342  1.00 55.99  ?  153 LYS   B CB  1 
ATOM   3228 C CG  . LYS   B 1 148 ? -8.478  -11.831 37.380  1.00 57.94  ?  153 LYS   B CG  1 
ATOM   3229 C CD  . LYS   B 1 148 ? -8.535  -13.327 37.113  1.00 60.22  ?  153 LYS   B CD  1 
ATOM   3230 C CE  . LYS   B 1 148 ? -7.439  -13.782 36.169  1.00 60.83  ?  153 LYS   B CE  1 
ATOM   3231 N NZ  . LYS   B 1 148 ? -7.959  -13.765 34.776  1.00 72.28  ?  153 LYS   B NZ  1 
ATOM   3232 N N   . ILE   B 1 149 ? -11.741 -8.857  38.615  1.00 54.72  ?  154 ILE   B N   1 
ATOM   3233 C CA  . ILE   B 1 149 ? -13.029 -8.402  39.131  1.00 53.30  ?  154 ILE   B CA  1 
ATOM   3234 C C   . ILE   B 1 149 ? -14.020 -9.554  39.044  1.00 50.28  ?  154 ILE   B C   1 
ATOM   3235 O O   . ILE   B 1 149 ? -14.156 -10.190 37.988  1.00 51.08  ?  154 ILE   B O   1 
ATOM   3236 C CB  . ILE   B 1 149 ? -13.536 -7.157  38.370  1.00 57.19  ?  154 ILE   B CB  1 
ATOM   3237 C CG1 . ILE   B 1 149 ? -12.570 -5.994  38.632  1.00 60.88  ?  154 ILE   B CG1 1 
ATOM   3238 C CG2 . ILE   B 1 149 ? -14.962 -6.770  38.793  1.00 52.75  ?  154 ILE   B CG2 1 
ATOM   3239 C CD1 . ILE   B 1 149 ? -12.666 -4.900  37.603  1.00 71.54  ?  154 ILE   B CD1 1 
ATOM   3240 N N   . ALA   B 1 150 ? -14.738 -9.764  40.147  1.00 62.10  ?  155 ALA   B N   1 
ATOM   3241 C CA  . ALA   B 1 150 ? -15.725 -10.826 40.307  1.00 57.70  ?  155 ALA   B CA  1 
ATOM   3242 C C   . ALA   B 1 150 ? -17.091 -10.225 40.582  1.00 53.22  ?  155 ALA   B C   1 
ATOM   3243 O O   . ALA   B 1 150 ? -17.190 -9.060  40.910  1.00 47.87  ?  155 ALA   B O   1 
ATOM   3244 C CB  . ALA   B 1 150 ? -15.326 -11.726 41.465  1.00 57.61  ?  155 ALA   B CB  1 
ATOM   3245 N N   . ASP   B 1 151 ? -18.130 -11.050 40.453  1.00 57.39  ?  156 ASP   B N   1 
ATOM   3246 C CA  . ASP   B 1 151 ? -19.510 -10.706 40.836  1.00 60.06  ?  156 ASP   B CA  1 
ATOM   3247 C C   . ASP   B 1 151 ? -20.077 -11.854 41.678  1.00 60.32  ?  156 ASP   B C   1 
ATOM   3248 O O   . ASP   B 1 151 ? -20.948 -12.613 41.229  1.00 65.43  ?  156 ASP   B O   1 
ATOM   3249 C CB  . ASP   B 1 151 ? -20.354 -10.427 39.584  1.00 65.58  ?  156 ASP   B CB  1 
ATOM   3250 C CG  . ASP   B 1 151 ? -21.814 -10.055 39.897  1.00 75.42  ?  156 ASP   B CG  1 
ATOM   3251 O OD1 . ASP   B 1 151 ? -22.087 -9.487  40.974  1.00 75.39  ?  156 ASP   B OD1 1 
ATOM   3252 O OD2 . ASP   B 1 151 ? -22.704 -10.357 39.068  1.00 86.89  ?  156 ASP   B OD2 1 
ATOM   3253 N N   . LEU   B 1 152 ? -19.587 -11.953 42.911  1.00 59.43  ?  157 LEU   B N   1 
ATOM   3254 C CA  . LEU   B 1 152 ? -19.823 -13.145 43.752  1.00 60.90  ?  157 LEU   B CA  1 
ATOM   3255 C C   . LEU   B 1 152 ? -21.259 -13.279 44.273  1.00 60.06  ?  157 LEU   B C   1 
ATOM   3256 O O   . LEU   B 1 152 ? -21.746 -14.396 44.423  1.00 59.45  ?  157 LEU   B O   1 
ATOM   3257 C CB  . LEU   B 1 152 ? -18.822 -13.200 44.914  1.00 58.28  ?  157 LEU   B CB  1 
ATOM   3258 C CG  . LEU   B 1 152 ? -17.349 -13.272 44.514  1.00 56.76  ?  157 LEU   B CG  1 
ATOM   3259 C CD1 . LEU   B 1 152 ? -16.463 -13.135 45.742  1.00 59.81  ?  157 LEU   B CD1 1 
ATOM   3260 C CD2 . LEU   B 1 152 ? -17.041 -14.558 43.783  1.00 56.24  ?  157 LEU   B CD2 1 
ATOM   3261 N N   . GLY   B 1 153 ? -21.905 -12.147 44.540  1.00 59.50  ?  158 GLY   B N   1 
ATOM   3262 C CA  . GLY   B 1 153 ? -23.325 -12.103 44.868  1.00 59.35  ?  158 GLY   B CA  1 
ATOM   3263 C C   . GLY   B 1 153 ? -24.290 -12.044 43.691  1.00 62.42  ?  158 GLY   B C   1 
ATOM   3264 O O   . GLY   B 1 153 ? -25.484 -11.801 43.913  1.00 66.69  ?  158 GLY   B O   1 
ATOM   3265 N N   . LEU   B 1 154 ? -23.804 -12.247 42.455  1.00 60.33  ?  159 LEU   B N   1 
ATOM   3266 C CA  . LEU   B 1 154 ? -24.657 -12.427 41.265  1.00 58.96  ?  159 LEU   B CA  1 
ATOM   3267 C C   . LEU   B 1 154 ? -25.581 -11.231 40.962  1.00 61.13  ?  159 LEU   B C   1 
ATOM   3268 O O   . LEU   B 1 154 ? -26.736 -11.397 40.519  1.00 66.14  ?  159 LEU   B O   1 
ATOM   3269 C CB  . LEU   B 1 154 ? -25.450 -13.746 41.385  1.00 59.20  ?  159 LEU   B CB  1 
ATOM   3270 C CG  . LEU   B 1 154 ? -24.678 -15.020 41.757  1.00 56.12  ?  159 LEU   B CG  1 
ATOM   3271 C CD1 . LEU   B 1 154 ? -25.641 -16.161 42.001  1.00 55.17  ?  159 LEU   B CD1 1 
ATOM   3272 C CD2 . LEU   B 1 154 ? -23.680 -15.392 40.673  1.00 57.99  ?  159 LEU   B CD2 1 
ATOM   3273 N N   . ALA   B 1 155 ? -25.048 -10.031 41.191  1.00 62.20  ?  160 ALA   B N   1 
ATOM   3274 C CA  . ALA   B 1 155 ? -25.781 -8.782  41.007  1.00 65.82  ?  160 ALA   B CA  1 
ATOM   3275 C C   . ALA   B 1 155 ? -26.170 -8.499  39.551  1.00 70.97  ?  160 ALA   B C   1 
ATOM   3276 O O   . ALA   B 1 155 ? -27.250 -7.946  39.293  1.00 81.97  ?  160 ALA   B O   1 
ATOM   3277 C CB  . ALA   B 1 155 ? -24.974 -7.624  41.577  1.00 68.32  ?  160 ALA   B CB  1 
ATOM   3278 N N   . SER   B 1 156 ? -25.301 -8.899  38.619  1.00 68.09  ?  161 SER   B N   1 
ATOM   3279 C CA  . SER   B 1 156 ? -25.519 -8.740  37.175  1.00 71.83  ?  161 SER   B CA  1 
ATOM   3280 C C   . SER   B 1 156 ? -26.326 -9.872  36.495  1.00 69.38  ?  161 SER   B C   1 
ATOM   3281 O O   . SER   B 1 156 ? -26.560 -9.802  35.290  1.00 73.76  ?  161 SER   B O   1 
ATOM   3282 C CB  . SER   B 1 156 ? -24.158 -8.592  36.464  1.00 77.72  ?  161 SER   B CB  1 
ATOM   3283 O OG  . SER   B 1 156 ? -23.422 -7.464  36.935  1.00 86.65  ?  161 SER   B OG  1 
ATOM   3284 N N   . PHE   B 1 157 ? -26.757 -10.893 37.247  1.00 72.12  ?  162 PHE   B N   1 
ATOM   3285 C CA  . PHE   B 1 157 ? -27.321 -12.132 36.694  1.00 74.98  ?  162 PHE   B CA  1 
ATOM   3286 C C   . PHE   B 1 157 ? -28.599 -12.535 37.422  1.00 77.87  ?  162 PHE   B C   1 
ATOM   3287 O O   . PHE   B 1 157 ? -28.539 -13.260 38.414  1.00 79.63  ?  162 PHE   B O   1 
ATOM   3288 C CB  . PHE   B 1 157 ? -26.237 -13.222 36.745  1.00 69.68  ?  162 PHE   B CB  1 
ATOM   3289 C CG  . PHE   B 1 157 ? -25.051 -12.899 35.886  1.00 68.20  ?  162 PHE   B CG  1 
ATOM   3290 C CD1 . PHE   B 1 157 ? -25.186 -12.827 34.489  1.00 69.50  ?  162 PHE   B CD1 1 
ATOM   3291 C CD2 . PHE   B 1 157 ? -23.801 -12.634 36.451  1.00 68.11  ?  162 PHE   B CD2 1 
ATOM   3292 C CE1 . PHE   B 1 157 ? -24.102 -12.512 33.679  1.00 70.81  ?  162 PHE   B CE1 1 
ATOM   3293 C CE2 . PHE   B 1 157 ? -22.711 -12.309 35.640  1.00 70.03  ?  162 PHE   B CE2 1 
ATOM   3294 C CZ  . PHE   B 1 157 ? -22.866 -12.244 34.251  1.00 69.92  ?  162 PHE   B CZ  1 
ATOM   3295 N N   . LYS   B 1 158 ? -29.739 -12.055 36.902  1.00 78.62  ?  163 LYS   B N   1 
ATOM   3296 C CA  . LYS   B 1 158 ? -31.053 -12.103 37.590  1.00 80.71  ?  163 LYS   B CA  1 
ATOM   3297 C C   . LYS   B 1 158 ? -31.532 -13.509 37.988  1.00 81.44  ?  163 LYS   B C   1 
ATOM   3298 O O   . LYS   B 1 158 ? -31.909 -13.727 39.147  1.00 83.24  ?  163 LYS   B O   1 
ATOM   3299 C CB  . LYS   B 1 158 ? -32.141 -11.409 36.743  1.00 79.65  ?  163 LYS   B CB  1 
ATOM   3300 C CG  . LYS   B 1 158 ? -32.479 -11.831 35.383  0.00 82.45  ?  163 LYS   B CG  1 
ATOM   3301 C CD  . LYS   B 1 158 ? -33.788 -11.253 34.858  0.00 88.39  ?  163 LYS   B CD  1 
ATOM   3302 C CE  . LYS   B 1 158 ? -33.715 -9.754  34.612  0.00 92.42  ?  163 LYS   B CE  1 
ATOM   3303 N NZ  . LYS   B 1 158 ? -34.950 -9.248  33.951  0.00 99.55  ?  163 LYS   B NZ  1 
ATOM   3304 N N   . MET   B 1 159 ? -31.499 -14.441 37.033  1.00 82.53  ?  164 MET   B N   1 
ATOM   3305 C CA  . MET   B 1 159 ? -32.013 -15.814 37.228  1.00 82.52  ?  164 MET   B CA  1 
ATOM   3306 C C   . MET   B 1 159 ? -31.226 -16.644 38.230  1.00 76.56  ?  164 MET   B C   1 
ATOM   3307 O O   . MET   B 1 159 ? -31.834 -17.303 39.086  1.00 77.19  ?  164 MET   B O   1 
ATOM   3308 C CB  . MET   B 1 159 ? -32.146 -16.562 35.894  1.00 86.26  ?  164 MET   B CB  1 
ATOM   3309 C CG  . MET   B 1 159 ? -33.201 -15.963 34.962  1.00 95.54  ?  164 MET   B CG  1 
ATOM   3310 S SD  . MET   B 1 159 ? -34.908 -16.060 35.577  1.00 105.01 ?  164 MET   B SD  1 
ATOM   3311 C CE  . MET   B 1 159 ? -35.832 -15.420 34.173  1.00 116.85 ?  164 MET   B CE  1 
ATOM   3312 N N   . TRP   B 1 160 ? -29.895 -16.610 38.132  1.00 70.88  ?  165 TRP   B N   1 
ATOM   3313 C CA  . TRP   B 1 160 ? -29.022 -17.226 39.154  1.00 65.50  ?  165 TRP   B CA  1 
ATOM   3314 C C   . TRP   B 1 160 ? -29.171 -16.563 40.527  1.00 65.14  ?  165 TRP   B C   1 
ATOM   3315 O O   . TRP   B 1 160 ? -29.047 -17.230 41.560  1.00 68.87  ?  165 TRP   B O   1 
ATOM   3316 C CB  . TRP   B 1 160 ? -27.550 -17.216 38.735  1.00 62.07  ?  165 TRP   B CB  1 
ATOM   3317 C CG  . TRP   B 1 160 ? -27.204 -18.187 37.644  1.00 61.20  ?  165 TRP   B CG  1 
ATOM   3318 C CD1 . TRP   B 1 160 ? -27.264 -17.968 36.300  1.00 63.17  ?  165 TRP   B CD1 1 
ATOM   3319 C CD2 . TRP   B 1 160 ? -26.722 -19.522 37.811  1.00 59.98  ?  165 TRP   B CD2 1 
ATOM   3320 N NE1 . TRP   B 1 160 ? -26.853 -19.082 35.615  1.00 63.23  ?  165 TRP   B NE1 1 
ATOM   3321 C CE2 . TRP   B 1 160 ? -26.518 -20.056 36.517  1.00 63.09  ?  165 TRP   B CE2 1 
ATOM   3322 C CE3 . TRP   B 1 160 ? -26.441 -20.326 38.931  1.00 59.43  ?  165 TRP   B CE3 1 
ATOM   3323 C CZ2 . TRP   B 1 160 ? -26.051 -21.370 36.307  1.00 63.91  ?  165 TRP   B CZ2 1 
ATOM   3324 C CZ3 . TRP   B 1 160 ? -25.974 -21.642 38.722  1.00 59.29  ?  165 TRP   B CZ3 1 
ATOM   3325 C CH2 . TRP   B 1 160 ? -25.784 -22.142 37.415  1.00 61.07  ?  165 TRP   B CH2 1 
ATOM   3326 N N   . SER   B 1 161 ? -29.421 -15.255 40.531  1.00 68.71  ?  166 SER   B N   1 
ATOM   3327 C CA  . SER   B 1 161 ? -29.684 -14.504 41.771  1.00 69.83  ?  166 SER   B CA  1 
ATOM   3328 C C   . SER   B 1 161 ? -31.026 -14.901 42.400  1.00 68.54  ?  166 SER   B C   1 
ATOM   3329 O O   . SER   B 1 161 ? -31.110 -15.083 43.610  1.00 70.41  ?  166 SER   B O   1 
ATOM   3330 C CB  . SER   B 1 161 ? -29.628 -12.994 41.522  1.00 69.08  ?  166 SER   B CB  1 
ATOM   3331 O OG  . SER   B 1 161 ? -29.352 -12.296 42.712  1.00 75.93  ?  166 SER   B OG  1 
ATOM   3332 N N   . LYS   B 1 162 ? -32.059 -15.035 41.570  1.00 69.97  ?  167 LYS   B N   1 
ATOM   3333 C CA  . LYS   B 1 162 ? -33.364 -15.588 41.998  1.00 75.98  ?  167 LYS   B CA  1 
ATOM   3334 C C   . LYS   B 1 162 ? -33.257 -17.048 42.461  1.00 72.14  ?  167 LYS   B C   1 
ATOM   3335 O O   . LYS   B 1 162 ? -33.893 -17.436 43.447  1.00 75.80  ?  167 LYS   B O   1 
ATOM   3336 C CB  . LYS   B 1 162 ? -34.419 -15.472 40.877  1.00 75.97  ?  167 LYS   B CB  1 
ATOM   3337 C CG  . LYS   B 1 162 ? -34.897 -14.020 40.716  0.00 76.00  ?  167 LYS   B CG  1 
ATOM   3338 C CD  . LYS   B 1 162 ? -35.763 -13.849 39.479  0.00 80.02  ?  167 LYS   B CD  1 
ATOM   3339 C CE  . LYS   B 1 162 ? -36.182 -12.397 39.306  0.00 84.12  ?  167 LYS   B CE  1 
ATOM   3340 N NZ  . LYS   B 1 162 ? -37.010 -12.182 38.087  0.00 89.18  ?  167 LYS   B NZ  1 
ATOM   3341 N N   . LEU   B 1 163 ? -32.462 -17.835 41.733  1.00 69.66  ?  168 LEU   B N   1 
ATOM   3342 C CA  . LEU   B 1 163 ? -32.154 -19.226 42.091  1.00 68.08  ?  168 LEU   B CA  1 
ATOM   3343 C C   . LEU   B 1 163 ? -31.465 -19.363 43.451  1.00 69.73  ?  168 LEU   B C   1 
ATOM   3344 O O   . LEU   B 1 163 ? -31.740 -20.312 44.187  1.00 67.62  ?  168 LEU   B O   1 
ATOM   3345 C CB  . LEU   B 1 163 ? -31.291 -19.870 41.002  1.00 63.97  ?  168 LEU   B CB  1 
ATOM   3346 C CG  . LEU   B 1 163 ? -30.877 -21.332 41.158  1.00 63.64  ?  168 LEU   B CG  1 
ATOM   3347 C CD1 . LEU   B 1 163 ? -32.078 -22.257 41.264  1.00 64.12  ?  168 LEU   B CD1 1 
ATOM   3348 C CD2 . LEU   B 1 163 ? -30.006 -21.744 39.993  1.00 66.01  ?  168 LEU   B CD2 1 
ATOM   3349 N N   . ASN   B 1 164 ? -30.558 -18.434 43.756  1.00 73.88  ?  169 ASN   B N   1 
ATOM   3350 C CA  . ASN   B 1 164 ? -29.851 -18.406 45.045  1.00 75.71  ?  169 ASN   B CA  1 
ATOM   3351 C C   . ASN   B 1 164 ? -30.778 -18.122 46.241  1.00 78.44  ?  169 ASN   B C   1 
ATOM   3352 O O   . ASN   B 1 164 ? -30.575 -18.697 47.312  1.00 74.31  ?  169 ASN   B O   1 
ATOM   3353 C CB  . ASN   B 1 164 ? -28.697 -17.374 44.996  1.00 78.45  ?  169 ASN   B CB  1 
ATOM   3354 C CG  . ASN   B 1 164 ? -27.701 -17.449 46.179  1.00 82.73  ?  169 ASN   B CG  1 
ATOM   3355 O OD1 . ASN   B 1 164 ? -26.921 -16.511 46.334  1.00 101.38 ?  169 ASN   B OD1 1 
ATOM   3356 N ND2 . ASN   B 1 164 ? -27.677 -18.528 46.979  1.00 85.33  ?  169 ASN   B ND2 1 
ATOM   3357 N N   . ASN   B 1 165 ? -31.792 -17.269 46.043  1.00 82.33  ?  170 ASN   B N   1 
ATOM   3358 C CA  . ASN   B 1 165 ? -32.728 -16.835 47.104  1.00 91.43  ?  170 ASN   B CA  1 
ATOM   3359 C C   . ASN   B 1 165 ? -34.098 -17.544 47.007  1.00 91.18  ?  170 ASN   B C   1 
ATOM   3360 O O   . ASN   B 1 165 ? -35.136 -16.976 47.361  1.00 103.69 ?  170 ASN   B O   1 
ATOM   3361 C CB  . ASN   B 1 165 ? -32.883 -15.298 47.048  1.00 101.17 ?  170 ASN   B CB  1 
ATOM   3362 C CG  . ASN   B 1 165 ? -31.561 -14.564 47.229  1.00 101.00 ?  170 ASN   B CG  1 
ATOM   3363 O OD1 . ASN   B 1 165 ? -31.167 -13.757 46.390  1.00 92.89  ?  170 ASN   B OD1 1 
ATOM   3364 N ND2 . ASN   B 1 165 ? -30.866 -14.850 48.323  1.00 107.17 ?  170 ASN   B ND2 1 
ATOM   3365 N N   . GLU   B 1 166 ? -34.077 -18.814 46.603  1.00 89.62  ?  171 GLU   B N   1 
ATOM   3366 C CA  . GLU   B 1 166 ? -35.285 -19.592 46.288  1.00 85.07  ?  171 GLU   B CA  1 
ATOM   3367 C C   . GLU   B 1 166 ? -35.731 -20.289 47.580  1.00 84.54  ?  171 GLU   B C   1 
ATOM   3368 O O   . GLU   B 1 166 ? -34.895 -20.782 48.342  1.00 81.32  ?  171 GLU   B O   1 
ATOM   3369 C CB  . GLU   B 1 166 ? -35.006 -20.566 45.115  1.00 85.97  ?  171 GLU   B CB  1 
ATOM   3370 C CG  . GLU   B 1 166 ? -35.758 -21.898 45.043  1.00 93.78  ?  171 GLU   B CG  1 
ATOM   3371 C CD  . GLU   B 1 166 ? -37.261 -21.800 44.910  1.00 99.34  ?  171 GLU   B CD  1 
ATOM   3372 O OE1 . GLU   B 1 166 ? -37.794 -20.707 44.627  1.00 116.43 ?  171 GLU   B OE1 1 
ATOM   3373 O OE2 . GLU   B 1 166 ? -37.910 -22.848 45.110  1.00 92.99  ?  171 GLU   B OE2 1 
ATOM   3374 N N   . GLU   B 1 167 ? -37.051 -20.322 47.790  1.00 89.24  ?  172 GLU   B N   1 
ATOM   3375 C CA  . GLU   B 1 167 ? -37.722 -20.875 49.000  1.00 87.39  ?  172 GLU   B CA  1 
ATOM   3376 C C   . GLU   B 1 167 ? -37.270 -22.302 49.400  1.00 83.39  ?  172 GLU   B C   1 
ATOM   3377 O O   . GLU   B 1 167 ? -37.119 -22.591 50.582  1.00 83.38  ?  172 GLU   B O   1 
ATOM   3378 C CB  . GLU   B 1 167 ? -39.257 -20.840 48.798  1.00 91.34  ?  172 GLU   B CB  1 
ATOM   3379 C CG  . GLU   B 1 167 ? -40.088 -20.938 50.062  1.00 97.61  ?  172 GLU   B CG  1 
ATOM   3380 C CD  . GLU   B 1 167 ? -41.573 -20.597 49.828  0.00 97.65  ?  172 GLU   B CD  1 
ATOM   3381 O OE1 . GLU   B 1 167 ? -42.157 -19.888 50.675  0.00 101.00 ?  172 GLU   B OE1 1 
ATOM   3382 O OE2 . GLU   B 1 167 ? -42.145 -21.035 48.806  0.00 97.87  ?  172 GLU   B OE2 1 
ATOM   3383 N N   . HIS   B 1 168 ? -37.044 -23.157 48.398  1.00 80.84  ?  173 HIS   B N   1 
ATOM   3384 C CA  . HIS   B 1 168 ? -36.599 -24.563 48.562  1.00 78.19  ?  173 HIS   B CA  1 
ATOM   3385 C C   . HIS   B 1 168 ? -35.088 -24.829 48.608  1.00 74.66  ?  173 HIS   B C   1 
ATOM   3386 O O   . HIS   B 1 168 ? -34.674 -25.975 48.795  1.00 76.79  ?  173 HIS   B O   1 
ATOM   3387 C CB  . HIS   B 1 168 ? -37.192 -25.414 47.428  1.00 78.66  ?  173 HIS   B CB  1 
ATOM   3388 C CG  . HIS   B 1 168 ? -38.681 -25.416 47.413  1.00 78.37  ?  173 HIS   B CG  1 
ATOM   3389 N ND1 . HIS   B 1 168 ? -39.420 -24.793 46.433  1.00 77.75  ?  173 HIS   B ND1 1 
ATOM   3390 C CD2 . HIS   B 1 168 ? -39.569 -25.932 48.289  1.00 80.13  ?  173 HIS   B CD2 1 
ATOM   3391 C CE1 . HIS   B 1 168 ? -40.703 -24.944 46.697  1.00 80.99  ?  173 HIS   B CE1 1 
ATOM   3392 N NE2 . HIS   B 1 168 ? -40.819 -25.628 47.820  1.00 81.70  ?  173 HIS   B NE2 1 
ATOM   3393 N N   . ASN   B 1 169 ? -34.268 -23.800 48.429  1.00 73.05  ?  174 ASN   B N   1 
ATOM   3394 C CA  . ASN   B 1 169 ? -32.806 -23.956 48.440  1.00 73.47  ?  174 ASN   B CA  1 
ATOM   3395 C C   . ASN   B 1 169 ? -32.277 -24.286 49.842  1.00 77.56  ?  174 ASN   B C   1 
ATOM   3396 O O   . ASN   B 1 169 ? -32.290 -23.423 50.730  1.00 82.00  ?  174 ASN   B O   1 
ATOM   3397 C CB  . ASN   B 1 169 ? -32.137 -22.667 47.925  1.00 70.06  ?  174 ASN   B CB  1 
ATOM   3398 C CG  . ASN   B 1 169 ? -30.652 -22.837 47.614  1.00 71.43  ?  174 ASN   B CG  1 
ATOM   3399 O OD1 . ASN   B 1 169 ? -30.054 -23.911 47.791  1.00 73.09  ?  174 ASN   B OD1 1 
ATOM   3400 N ND2 . ASN   B 1 169 ? -30.044 -21.757 47.139  1.00 69.91  ?  174 ASN   B ND2 1 
ATOM   3401 N N   . GLU   B 1 170 ? -31.737 -25.493 50.034  1.00 80.14  ?  175 GLU   B N   1 
ATOM   3402 C CA  . GLU   B 1 170 ? -31.193 -25.882 51.353  1.00 88.83  ?  175 GLU   B CA  1 
ATOM   3403 C C   . GLU   B 1 170 ? -29.788 -25.277 51.642  1.00 89.60  ?  175 GLU   B C   1 
ATOM   3404 O O   . GLU   B 1 170 ? -28.874 -25.982 52.066  1.00 93.64  ?  175 GLU   B O   1 
ATOM   3405 C CB  . GLU   B 1 170 ? -31.277 -27.421 51.585  1.00 94.32  ?  175 GLU   B CB  1 
ATOM   3406 C CG  . GLU   B 1 170 ? -30.458 -28.342 50.682  1.00 93.36  ?  175 GLU   B CG  1 
ATOM   3407 C CD  . GLU   B 1 170 ? -30.203 -29.696 51.344  0.00 97.35  ?  175 GLU   B CD  1 
ATOM   3408 O OE1 . GLU   B 1 170 ? -30.676 -30.720 50.804  0.00 99.44  ?  175 GLU   B OE1 1 
ATOM   3409 O OE2 . GLU   B 1 170 ? -29.506 -29.743 52.380  0.00 100.47 ?  175 GLU   B OE2 1 
ATOM   3410 N N   . LEU   B 1 171 ? -29.670 -23.953 51.487  1.00 88.10  ?  176 LEU   B N   1 
ATOM   3411 C CA  . LEU   B 1 171 ? -28.413 -23.201 51.619  1.00 92.62  ?  176 LEU   B CA  1 
ATOM   3412 C C   . LEU   B 1 171 ? -28.718 -21.782 52.125  1.00 102.44 ?  176 LEU   B C   1 
ATOM   3413 O O   . LEU   B 1 171 ? -29.590 -21.087 51.581  1.00 104.22 ?  176 LEU   B O   1 
ATOM   3414 C CB  . LEU   B 1 171 ? -27.670 -23.114 50.276  1.00 83.63  ?  176 LEU   B CB  1 
ATOM   3415 C CG  . LEU   B 1 171 ? -27.118 -24.380 49.613  1.00 82.33  ?  176 LEU   B CG  1 
ATOM   3416 C CD1 . LEU   B 1 171 ? -26.458 -24.002 48.303  1.00 79.73  ?  176 LEU   B CD1 1 
ATOM   3417 C CD2 . LEU   B 1 171 ? -26.102 -25.114 50.471  1.00 84.29  ?  176 LEU   B CD2 1 
ATOM   3418 N N   . GLY   B 1 183 ? -25.312 -7.089  52.978  1.00 92.23  ?  188 GLY   B N   1 
ATOM   3419 C CA  . GLY   B 1 183 ? -24.156 -6.524  52.281  1.00 100.08 ?  188 GLY   B CA  1 
ATOM   3420 C C   . GLY   B 1 183 ? -23.631 -5.215  52.868  1.00 107.32 ?  188 GLY   B C   1 
ATOM   3421 O O   . GLY   B 1 183 ? -24.341 -4.514  53.598  1.00 115.03 ?  188 GLY   B O   1 
ATOM   3422 N N   . THR   B 1 184 ? -22.376 -4.905  52.549  1.00 105.16 ?  189 THR   B N   1 
ATOM   3423 C CA  . THR   B 1 184 ? -21.712 -3.655  52.977  1.00 94.43  ?  189 THR   B CA  1 
ATOM   3424 C C   . THR   B 1 184 ? -22.152 -2.427  52.138  1.00 89.45  ?  189 THR   B C   1 
ATOM   3425 O O   . THR   B 1 184 ? -22.062 -2.446  50.902  1.00 83.88  ?  189 THR   B O   1 
ATOM   3426 C CB  . THR   B 1 184 ? -20.156 -3.798  53.013  1.00 97.62  ?  189 THR   B CB  1 
ATOM   3427 O OG1 . THR   B 1 184 ? -19.579 -2.645  53.638  1.00 93.14  ?  189 THR   B OG1 1 
ATOM   3428 C CG2 . THR   B 1 184 ? -19.497 -3.999  51.619  1.00 93.41  ?  189 THR   B CG2 1 
ATOM   3429 N N   . LEU   B 1 185 ? -22.635 -1.380  52.823  1.00 81.89  ?  190 LEU   B N   1 
ATOM   3430 C CA  . LEU   B 1 185 ? -23.108 -0.132  52.205  1.00 76.78  ?  190 LEU   B CA  1 
ATOM   3431 C C   . LEU   B 1 185 ? -22.027 0.951   52.047  1.00 70.18  ?  190 LEU   B C   1 
ATOM   3432 O O   . LEU   B 1 185 ? -22.342 2.045   51.569  1.00 75.61  ?  190 LEU   B O   1 
ATOM   3433 C CB  . LEU   B 1 185 ? -24.282 0.433   53.025  1.00 79.35  ?  190 LEU   B CB  1 
ATOM   3434 C CG  . LEU   B 1 185 ? -25.465 -0.547  53.213  0.00 78.17  ?  190 LEU   B CG  1 
ATOM   3435 C CD1 . LEU   B 1 185 ? -26.538 0.117   54.062  0.00 81.41  ?  190 LEU   B CD1 1 
ATOM   3436 C CD2 . LEU   B 1 185 ? -26.051 -1.014  51.892  0.00 78.20  ?  190 LEU   B CD2 1 
ATOM   3437 N N   . TYR   B 1 186 ? -20.781 0.657   52.435  1.00 66.70  ?  191 TYR   B N   1 
ATOM   3438 C CA  . TYR   B 1 186 ? -19.684 1.633   52.378  1.00 61.64  ?  191 TYR   B CA  1 
ATOM   3439 C C   . TYR   B 1 186 ? -19.274 2.083   50.981  1.00 59.38  ?  191 TYR   B C   1 
ATOM   3440 O O   . TYR   B 1 186 ? -18.760 3.192   50.832  1.00 66.28  ?  191 TYR   B O   1 
ATOM   3441 C CB  . TYR   B 1 186 ? -18.424 1.067   53.052  1.00 61.44  ?  191 TYR   B CB  1 
ATOM   3442 C CG  . TYR   B 1 186 ? -18.509 0.700   54.522  1.00 60.52  ?  191 TYR   B CG  1 
ATOM   3443 C CD1 . TYR   B 1 186 ? -19.440 1.286   55.402  1.00 57.29  ?  191 TYR   B CD1 1 
ATOM   3444 C CD2 . TYR   B 1 186 ? -17.595 -0.218  55.055  1.00 58.84  ?  191 TYR   B CD2 1 
ATOM   3445 C CE1 . TYR   B 1 186 ? -19.456 0.936   56.757  1.00 59.95  ?  191 TYR   B CE1 1 
ATOM   3446 C CE2 . TYR   B 1 186 ? -17.608 -0.565  56.403  1.00 58.89  ?  191 TYR   B CE2 1 
ATOM   3447 C CZ  . TYR   B 1 186 ? -18.538 0.009   57.248  1.00 61.61  ?  191 TYR   B CZ  1 
ATOM   3448 O OH  . TYR   B 1 186 ? -18.547 -0.338  58.574  1.00 66.28  ?  191 TYR   B OH  1 
ATOM   3449 N N   . TYR   B 1 187 ? -19.479 1.220   49.986  1.00 62.64  ?  192 TYR   B N   1 
ATOM   3450 C CA  . TYR   B 1 187 ? -19.045 1.445   48.591  1.00 58.74  ?  192 TYR   B CA  1 
ATOM   3451 C C   . TYR   B 1 187 ? -20.215 1.758   47.678  1.00 54.82  ?  192 TYR   B C   1 
ATOM   3452 O O   . TYR   B 1 187 ? -20.023 1.888   46.466  1.00 56.44  ?  192 TYR   B O   1 
ATOM   3453 C CB  . TYR   B 1 187 ? -18.278 0.190   48.076  1.00 59.41  ?  192 TYR   B CB  1 
ATOM   3454 C CG  . TYR   B 1 187 ? -17.141 -0.176  48.988  1.00 53.75  ?  192 TYR   B CG  1 
ATOM   3455 C CD1 . TYR   B 1 187 ? -17.353 -0.986  50.106  1.00 54.69  ?  192 TYR   B CD1 1 
ATOM   3456 C CD2 . TYR   B 1 187 ? -15.862 0.344   48.784  1.00 54.95  ?  192 TYR   B CD2 1 
ATOM   3457 C CE1 . TYR   B 1 187 ? -16.320 -1.286  50.983  1.00 56.28  ?  192 TYR   B CE1 1 
ATOM   3458 C CE2 . TYR   B 1 187 ? -14.814 0.044   49.653  1.00 59.51  ?  192 TYR   B CE2 1 
ATOM   3459 C CZ  . TYR   B 1 187 ? -15.048 -0.766  50.753  1.00 56.09  ?  192 TYR   B CZ  1 
ATOM   3460 O OH  . TYR   B 1 187 ? -14.018 -1.056  51.605  1.00 60.23  ?  192 TYR   B OH  1 
ATOM   3461 N N   . MET   B 1 188 ? -21.414 1.877   48.256  1.00 57.33  ?  193 MET   B N   1 
ATOM   3462 C CA  . MET   B 1 188 ? -22.637 2.149   47.519  1.00 62.03  ?  193 MET   B CA  1 
ATOM   3463 C C   . MET   B 1 188 ? -22.791 3.654   47.391  1.00 63.93  ?  193 MET   B C   1 
ATOM   3464 O O   . MET   B 1 188 ? -22.637 4.389   48.379  1.00 68.41  ?  193 MET   B O   1 
ATOM   3465 C CB  . MET   B 1 188 ? -23.829 1.581   48.270  1.00 69.82  ?  193 MET   B CB  1 
ATOM   3466 C CG  . MET   B 1 188 ? -25.120 1.597   47.486  1.00 78.98  ?  193 MET   B CG  1 
ATOM   3467 S SD  . MET   B 1 188 ? -26.392 0.602   48.281  1.00 97.68  ?  193 MET   B SD  1 
ATOM   3468 C CE  . MET   B 1 188 ? -25.832 -1.061  47.893  1.00 102.00 ?  193 MET   B CE  1 
ATOM   3469 N N   . ALA   B 1 189 ? -23.092 4.098   46.173  1.00 62.82  ?  194 ALA   B N   1 
ATOM   3470 C CA  . ALA   B 1 189 ? -23.266 5.513   45.868  1.00 62.13  ?  194 ALA   B CA  1 
ATOM   3471 C C   . ALA   B 1 189 ? -24.495 6.064   46.591  1.00 66.34  ?  194 ALA   B C   1 
ATOM   3472 O O   . ALA   B 1 189 ? -25.470 5.315   46.799  1.00 65.66  ?  194 ALA   B O   1 
ATOM   3473 C CB  . ALA   B 1 189 ? -23.394 5.724   44.368  1.00 61.92  ?  194 ALA   B CB  1 
ATOM   3474 N N   . PRO   B 1 190 ? -24.445 7.352   47.005  1.00 70.66  ?  195 PRO   B N   1 
ATOM   3475 C CA  . PRO   B 1 190 ? -25.523 7.918   47.833  1.00 71.54  ?  195 PRO   B CA  1 
ATOM   3476 C C   . PRO   B 1 190 ? -26.915 7.870   47.205  1.00 71.29  ?  195 PRO   B C   1 
ATOM   3477 O O   . PRO   B 1 190 ? -27.893 7.610   47.915  1.00 79.65  ?  195 PRO   B O   1 
ATOM   3478 C CB  . PRO   B 1 190 ? -25.070 9.366   48.074  1.00 76.30  ?  195 PRO   B CB  1 
ATOM   3479 C CG  . PRO   B 1 190 ? -24.088 9.651   46.998  1.00 73.74  ?  195 PRO   B CG  1 
ATOM   3480 C CD  . PRO   B 1 190 ? -23.391 8.356   46.750  1.00 71.34  ?  195 PRO   B CD  1 
ATOM   3481 N N   . GLU   B 1 191 ? -26.988 8.080   45.893  1.00 66.29  ?  196 GLU   B N   1 
ATOM   3482 C CA  . GLU   B 1 191 ? -28.237 7.930   45.132  1.00 72.35  ?  196 GLU   B CA  1 
ATOM   3483 C C   . GLU   B 1 191 ? -28.973 6.590   45.321  1.00 75.99  ?  196 GLU   B C   1 
ATOM   3484 O O   . GLU   B 1 191 ? -30.191 6.566   45.214  1.00 87.62  ?  196 GLU   B O   1 
ATOM   3485 C CB  . GLU   B 1 191 ? -28.053 8.235   43.623  1.00 71.81  ?  196 GLU   B CB  1 
ATOM   3486 C CG  . GLU   B 1 191 ? -27.044 7.370   42.857  1.00 69.99  ?  196 GLU   B CG  1 
ATOM   3487 C CD  . GLU   B 1 191 ? -25.651 7.998   42.741  1.00 70.91  ?  196 GLU   B CD  1 
ATOM   3488 O OE1 . GLU   B 1 191 ? -24.960 7.772   41.723  1.00 70.94  ?  196 GLU   B OE1 1 
ATOM   3489 O OE2 . GLU   B 1 191 ? -25.217 8.716   43.675  1.00 72.23  ?  196 GLU   B OE2 1 
ATOM   3490 N N   . HIS   B 1 192 ? -28.241 5.517   45.633  1.00 74.73  ?  197 HIS   B N   1 
ATOM   3491 C CA  . HIS   B 1 192 ? -28.816 4.183   45.904  1.00 75.93  ?  197 HIS   B CA  1 
ATOM   3492 C C   . HIS   B 1 192 ? -29.127 3.899   47.380  1.00 79.47  ?  197 HIS   B C   1 
ATOM   3493 O O   . HIS   B 1 192 ? -29.974 3.038   47.675  1.00 82.83  ?  197 HIS   B O   1 
ATOM   3494 C CB  . HIS   B 1 192 ? -27.899 3.110   45.334  1.00 72.21  ?  197 HIS   B CB  1 
ATOM   3495 C CG  . HIS   B 1 192 ? -27.614 3.305   43.883  1.00 69.95  ?  197 HIS   B CG  1 
ATOM   3496 N ND1 . HIS   B 1 192 ? -28.620 3.456   42.958  1.00 80.51  ?  197 HIS   B ND1 1 
ATOM   3497 C CD2 . HIS   B 1 192 ? -26.452 3.438   43.204  1.00 66.01  ?  197 HIS   B CD2 1 
ATOM   3498 C CE1 . HIS   B 1 192 ? -28.090 3.644   41.764  1.00 83.30  ?  197 HIS   B CE1 1 
ATOM   3499 N NE2 . HIS   B 1 192 ? -26.774 3.631   41.885  1.00 70.63  ?  197 HIS   B NE2 1 
ATOM   3500 N N   . LEU   B 1 193 ? -28.467 4.620   48.293  1.00 78.38  ?  198 LEU   B N   1 
ATOM   3501 C CA  . LEU   B 1 193 ? -28.813 4.570   49.723  1.00 82.24  ?  198 LEU   B CA  1 
ATOM   3502 C C   . LEU   B 1 193 ? -30.228 5.125   49.985  1.00 89.24  ?  198 LEU   B C   1 
ATOM   3503 O O   . LEU   B 1 193 ? -30.541 6.232   49.547  1.00 89.17  ?  198 LEU   B O   1 
ATOM   3504 C CB  . LEU   B 1 193 ? -27.795 5.361   50.549  1.00 80.22  ?  198 LEU   B CB  1 
ATOM   3505 C CG  . LEU   B 1 193 ? -26.338 4.903   50.560  1.00 74.86  ?  198 LEU   B CG  1 
ATOM   3506 C CD1 . LEU   B 1 193 ? -25.449 5.926   51.257  1.00 73.70  ?  198 LEU   B CD1 1 
ATOM   3507 C CD2 . LEU   B 1 193 ? -26.208 3.549   51.239  1.00 75.99  ?  198 LEU   B CD2 1 
ATOM   3508 N N   . ASN   B 1 194 ? -31.063 4.338   50.673  1.00 92.04  ?  199 ASN   B N   1 
ATOM   3509 C CA  . ASN   B 1 194 ? -32.493 4.638   50.903  1.00 105.53 ?  199 ASN   B CA  1 
ATOM   3510 C C   . ASN   B 1 194 ? -33.369 4.855   49.633  1.00 114.13 ?  199 ASN   B C   1 
ATOM   3511 O O   . ASN   B 1 194 ? -34.436 5.478   49.717  1.00 129.42 ?  199 ASN   B O   1 
ATOM   3512 C CB  . ASN   B 1 194 ? -32.660 5.828   51.893  1.00 114.41 ?  199 ASN   B CB  1 
ATOM   3513 C CG  . ASN   B 1 194 ? -32.191 5.520   53.311  1.00 115.70 ?  199 ASN   B CG  1 
ATOM   3514 O OD1 . ASN   B 1 194 ? -31.924 4.373   53.682  1.00 114.07 ?  199 ASN   B OD1 1 
ATOM   3515 N ND2 . ASN   B 1 194 ? -32.114 6.570   54.130  1.00 113.36 ?  199 ASN   B ND2 1 
ATOM   3516 N N   . ASP   B 1 195 ? -32.951 4.322   48.476  1.00 117.44 ?  200 ASP   B N   1 
ATOM   3517 C CA  . ASP   B 1 195 ? -33.716 4.468   47.211  1.00 125.73 ?  200 ASP   B CA  1 
ATOM   3518 C C   . ASP   B 1 195 ? -33.577 3.209   46.354  1.00 133.46 ?  200 ASP   B C   1 
ATOM   3519 O O   . ASP   B 1 195 ? -32.669 3.091   45.517  1.00 137.81 ?  200 ASP   B O   1 
ATOM   3520 C CB  . ASP   B 1 195 ? -33.319 5.737   46.441  1.00 116.47 ?  200 ASP   B CB  1 
ATOM   3521 C CG  . ASP   B 1 195 ? -34.421 6.265   45.580  0.00 126.20 ?  200 ASP   B CG  1 
ATOM   3522 O OD1 . ASP   B 1 195 ? -35.521 6.513   46.117  0.00 130.39 ?  200 ASP   B OD1 1 
ATOM   3523 O OD2 . ASP   B 1 195 ? -34.207 6.449   44.365  0.00 125.88 ?  200 ASP   B OD2 1 
ATOM   3524 N N   . VAL   B 1 196 ? -34.469 2.256   46.625  1.00 138.91 ?  201 VAL   B N   1 
ATOM   3525 C CA  . VAL   B 1 196 ? -34.558 1.007   45.846  1.00 138.59 ?  201 VAL   B CA  1 
ATOM   3526 C C   . VAL   B 1 196 ? -34.957 1.192   44.370  1.00 139.17 ?  201 VAL   B C   1 
ATOM   3527 O O   . VAL   B 1 196 ? -34.599 0.354   43.542  1.00 136.57 ?  201 VAL   B O   1 
ATOM   3528 C CB  . VAL   B 1 196 ? -35.490 -0.057  46.505  1.00 142.46 ?  201 VAL   B CB  1 
ATOM   3529 C CG1 . VAL   B 1 196 ? -34.950 -0.465  47.871  1.00 138.54 ?  201 VAL   B CG1 1 
ATOM   3530 C CG2 . VAL   B 1 196 ? -36.952 0.396   46.612  1.00 144.22 ?  201 VAL   B CG2 1 
ATOM   3531 N N   . ASN   B 1 197 ? -35.699 2.261   44.066  1.00 139.10 ?  202 ASN   B N   1 
ATOM   3532 C CA  . ASN   B 1 197 ? -36.171 2.532   42.701  1.00 143.27 ?  202 ASN   B CA  1 
ATOM   3533 C C   . ASN   B 1 197 ? -35.089 3.022   41.723  1.00 147.03 ?  202 ASN   B C   1 
ATOM   3534 O O   . ASN   B 1 197 ? -35.266 2.867   40.511  1.00 156.43 ?  202 ASN   B O   1 
ATOM   3535 C CB  . ASN   B 1 197 ? -37.326 3.537   42.723  1.00 140.19 ?  202 ASN   B CB  1 
ATOM   3536 C CG  . ASN   B 1 197 ? -38.552 2.978   43.483  0.00 149.24 ?  202 ASN   B CG  1 
ATOM   3537 O OD1 . ASN   B 1 197 ? -38.704 1.777   43.725  0.00 149.43 ?  202 ASN   B OD1 1 
ATOM   3538 N ND2 . ASN   B 1 197 ? -39.421 3.900   43.891  0.00 153.31 ?  202 ASN   B ND2 1 
ATOM   3539 N N   . ALA   B 1 198 ? -33.997 3.607   42.234  1.00 142.03 ?  203 ALA   B N   1 
ATOM   3540 C CA  . ALA   B 1 198 ? -32.952 4.210   41.378  1.00 129.73 ?  203 ALA   B CA  1 
ATOM   3541 C C   . ALA   B 1 198 ? -32.179 3.159   40.570  1.00 118.65 ?  203 ALA   B C   1 
ATOM   3542 O O   . ALA   B 1 198 ? -31.548 2.268   41.152  1.00 105.37 ?  203 ALA   B O   1 
ATOM   3543 C CB  . ALA   B 1 198 ? -31.987 5.048   42.204  1.00 123.40 ?  203 ALA   B CB  1 
ATOM   3544 N N   . LYS   B 1 199 ? -32.197 3.304   39.241  1.00 115.37 ?  204 LYS   B N   1 
ATOM   3545 C CA  . LYS   B 1 199 ? -31.541 2.369   38.321  1.00 106.21 ?  204 LYS   B CA  1 
ATOM   3546 C C   . LYS   B 1 199 ? -30.033 2.673   38.324  1.00 101.36 ?  204 LYS   B C   1 
ATOM   3547 O O   . LYS   B 1 199 ? -29.654 3.821   38.054  1.00 100.35 ?  204 LYS   B O   1 
ATOM   3548 C CB  . LYS   B 1 199 ? -32.113 2.503   36.902  1.00 105.63 ?  204 LYS   B CB  1 
ATOM   3549 C CG  . LYS   B 1 199 ? -31.740 1.449   35.900  0.00 109.33 ?  204 LYS   B CG  1 
ATOM   3550 C CD  . LYS   B 1 199 ? -32.427 1.681   34.561  0.00 113.88 ?  204 LYS   B CD  1 
ATOM   3551 C CE  . LYS   B 1 199 ? -32.109 0.583   33.558  0.00 113.90 ?  204 LYS   B CE  1 
ATOM   3552 N NZ  . LYS   B 1 199 ? -32.800 0.800   32.256  0.00 119.01 ?  204 LYS   B NZ  1 
ATOM   3553 N N   . PRO   B 1 200 ? -29.171 1.671   38.647  1.00 99.38  ?  205 PRO   B N   1 
ATOM   3554 C CA  . PRO   B 1 200 ? -27.712 1.899   38.600  1.00 94.68  ?  205 PRO   B CA  1 
ATOM   3555 C C   . PRO   B 1 200 ? -27.162 2.240   37.216  1.00 90.89  ?  205 PRO   B C   1 
ATOM   3556 O O   . PRO   B 1 200 ? -27.716 1.800   36.211  1.00 93.68  ?  205 PRO   B O   1 
ATOM   3557 C CB  . PRO   B 1 200 ? -27.125 0.571   39.092  1.00 94.55  ?  205 PRO   B CB  1 
ATOM   3558 C CG  . PRO   B 1 200 ? -28.205 -0.035  39.911  1.00 95.71  ?  205 PRO   B CG  1 
ATOM   3559 C CD  . PRO   B 1 200 ? -29.469 0.335   39.204  1.00 101.82 ?  205 PRO   B CD  1 
ATOM   3560 N N   . THR   B 1 201 ? -26.104 3.047   37.205  1.00 84.50  ?  206 THR   B N   1 
ATOM   3561 C CA  . THR   B 1 201 ? -25.444 3.524   35.986  1.00 87.94  ?  206 THR   B CA  1 
ATOM   3562 C C   . THR   B 1 201 ? -23.966 3.198   36.092  1.00 84.90  ?  206 THR   B C   1 
ATOM   3563 O O   . THR   B 1 201 ? -23.518 2.712   37.129  1.00 86.91  ?  206 THR   B O   1 
ATOM   3564 C CB  . THR   B 1 201 ? -25.608 5.058   35.803  1.00 86.40  ?  206 THR   B CB  1 
ATOM   3565 O OG1 . THR   B 1 201 ? -24.903 5.766   36.830  1.00 81.39  ?  206 THR   B OG1 1 
ATOM   3566 C CG2 . THR   B 1 201 ? -27.086 5.478   35.831  1.00 88.47  ?  206 THR   B CG2 1 
ATOM   3567 N N   . GLU   B 1 202 ? -23.211 3.490   35.030  1.00 83.01  ?  207 GLU   B N   1 
ATOM   3568 C CA  . GLU   B 1 202 ? -21.735 3.431   35.063  1.00 72.04  ?  207 GLU   B CA  1 
ATOM   3569 C C   . GLU   B 1 202 ? -21.149 4.247   36.228  1.00 71.12  ?  207 GLU   B C   1 
ATOM   3570 O O   . GLU   B 1 202 ? -20.218 3.791   36.881  1.00 87.22  ?  207 GLU   B O   1 
ATOM   3571 C CB  . GLU   B 1 202 ? -21.110 3.928   33.736  1.00 75.20  ?  207 GLU   B CB  1 
ATOM   3572 C CG  . GLU   B 1 202 ? -21.415 3.090   32.503  1.00 76.37  ?  207 GLU   B CG  1 
ATOM   3573 C CD  . GLU   B 1 202 ? -20.723 3.532   31.226  0.00 75.25  ?  207 GLU   B CD  1 
ATOM   3574 O OE1 . GLU   B 1 202 ? -19.983 4.545   31.223  0.00 74.95  ?  207 GLU   B OE1 1 
ATOM   3575 O OE2 . GLU   B 1 202 ? -20.928 2.863   30.192  0.00 76.75  ?  207 GLU   B OE2 1 
ATOM   3576 N N   . LYS   B 1 203 ? -21.741 5.410   36.510  1.00 73.94  ?  208 LYS   B N   1 
ATOM   3577 C CA  . LYS   B 1 203 ? -21.266 6.303   37.568  1.00 72.52  ?  208 LYS   B CA  1 
ATOM   3578 C C   . LYS   B 1 203 ? -21.476 5.755   38.984  1.00 70.48  ?  208 LYS   B C   1 
ATOM   3579 O O   . LYS   B 1 203 ? -20.733 6.133   39.897  1.00 69.01  ?  208 LYS   B O   1 
ATOM   3580 C CB  . LYS   B 1 203 ? -21.907 7.693   37.434  1.00 79.30  ?  208 LYS   B CB  1 
ATOM   3581 C CG  . LYS   B 1 203 ? -21.671 8.401   36.099  1.00 83.57  ?  208 LYS   B CG  1 
ATOM   3582 C CD  . LYS   B 1 203 ? -20.196 8.587   35.726  1.00 81.31  ?  208 LYS   B CD  1 
ATOM   3583 C CE  . LYS   B 1 203 ? -20.012 9.367   34.433  1.00 84.36  ?  208 LYS   B CE  1 
ATOM   3584 N NZ  . LYS   B 1 203 ? -20.397 10.804  34.556  1.00 98.20  ?  208 LYS   B NZ  1 
ATOM   3585 N N   . SER   B 1 204 ? -22.469 4.881   39.168  1.00 66.15  ?  209 SER   B N   1 
ATOM   3586 C CA  . SER   B 1 204 ? -22.616 4.101   40.410  1.00 62.07  ?  209 SER   B CA  1 
ATOM   3587 C C   . SER   B 1 204 ? -21.358 3.307   40.764  1.00 56.18  ?  209 SER   B C   1 
ATOM   3588 O O   . SER   B 1 204 ? -20.901 3.347   41.908  1.00 62.42  ?  209 SER   B O   1 
ATOM   3589 C CB  . SER   B 1 204 ? -23.777 3.115   40.310  1.00 68.32  ?  209 SER   B CB  1 
ATOM   3590 O OG  . SER   B 1 204 ? -24.935 3.739   39.802  1.00 76.86  ?  209 SER   B OG  1 
ATOM   3591 N N   . ASP   B 1 205 ? -20.810 2.600   39.776  1.00 50.54  ?  210 ASP   B N   1 
ATOM   3592 C CA  . ASP   B 1 205 ? -19.546 1.846   39.947  1.00 52.30  ?  210 ASP   B CA  1 
ATOM   3593 C C   . ASP   B 1 205 ? -18.317 2.731   40.140  1.00 54.76  ?  210 ASP   B C   1 
ATOM   3594 O O   . ASP   B 1 205 ? -17.355 2.321   40.794  1.00 57.36  ?  210 ASP   B O   1 
ATOM   3595 C CB  . ASP   B 1 205 ? -19.271 0.923   38.754  1.00 55.09  ?  210 ASP   B CB  1 
ATOM   3596 C CG  . ASP   B 1 205 ? -20.372 -0.115  38.519  1.00 61.45  ?  210 ASP   B CG  1 
ATOM   3597 O OD1 . ASP   B 1 205 ? -21.039 -0.518  39.508  1.00 57.10  ?  210 ASP   B OD1 1 
ATOM   3598 O OD2 . ASP   B 1 205 ? -20.561 -0.521  37.331  1.00 63.42  ?  210 ASP   B OD2 1 
ATOM   3599 N N   . VAL   B 1 206 ? -18.339 3.919   39.536  1.00 55.90  ?  211 VAL   B N   1 
ATOM   3600 C CA  . VAL   B 1 206 ? -17.265 4.902   39.702  1.00 54.51  ?  211 VAL   B CA  1 
ATOM   3601 C C   . VAL   B 1 206 ? -17.166 5.388   41.152  1.00 52.94  ?  211 VAL   B C   1 
ATOM   3602 O O   . VAL   B 1 206 ? -16.052 5.496   41.679  1.00 48.34  ?  211 VAL   B O   1 
ATOM   3603 C CB  . VAL   B 1 206 ? -17.414 6.071   38.702  1.00 60.03  ?  211 VAL   B CB  1 
ATOM   3604 C CG1 . VAL   B 1 206 ? -16.434 7.214   38.993  1.00 61.54  ?  211 VAL   B CG1 1 
ATOM   3605 C CG2 . VAL   B 1 206 ? -17.212 5.533   37.292  1.00 63.26  ?  211 VAL   B CG2 1 
ATOM   3606 N N   . TYR   B 1 207 ? -18.316 5.672   41.779  1.00 53.82  ?  212 TYR   B N   1 
ATOM   3607 C CA  . TYR   B 1 207 ? -18.366 5.979   43.217  1.00 54.03  ?  212 TYR   B CA  1 
ATOM   3608 C C   . TYR   B 1 207 ? -17.674 4.888   44.027  1.00 51.56  ?  212 TYR   B C   1 
ATOM   3609 O O   . TYR   B 1 207 ? -16.833 5.180   44.866  1.00 54.29  ?  212 TYR   B O   1 
ATOM   3610 C CB  . TYR   B 1 207 ? -19.804 6.154   43.739  1.00 55.54  ?  212 TYR   B CB  1 
ATOM   3611 C CG  . TYR   B 1 207 ? -19.824 6.585   45.193  1.00 58.87  ?  212 TYR   B CG  1 
ATOM   3612 C CD1 . TYR   B 1 207 ? -19.745 5.640   46.234  1.00 57.99  ?  212 TYR   B CD1 1 
ATOM   3613 C CD2 . TYR   B 1 207 ? -19.860 7.939   45.538  1.00 64.19  ?  212 TYR   B CD2 1 
ATOM   3614 C CE1 . TYR   B 1 207 ? -19.726 6.034   47.570  1.00 64.43  ?  212 TYR   B CE1 1 
ATOM   3615 C CE2 . TYR   B 1 207 ? -19.839 8.342   46.872  1.00 69.22  ?  212 TYR   B CE2 1 
ATOM   3616 C CZ  . TYR   B 1 207 ? -19.765 7.392   47.889  1.00 67.25  ?  212 TYR   B CZ  1 
ATOM   3617 O OH  . TYR   B 1 207 ? -19.745 7.783   49.212  1.00 70.42  ?  212 TYR   B OH  1 
ATOM   3618 N N   . SER   B 1 208 ? -18.065 3.646   43.773  1.00 47.94  ?  213 SER   B N   1 
ATOM   3619 C CA  . SER   B 1 208 ? -17.510 2.494   44.463  1.00 47.60  ?  213 SER   B CA  1 
ATOM   3620 C C   . SER   B 1 208 ? -15.981 2.420   44.302  1.00 43.96  ?  213 SER   B C   1 
ATOM   3621 O O   . SER   B 1 208 ? -15.270 2.250   45.286  1.00 47.23  ?  213 SER   B O   1 
ATOM   3622 C CB  . SER   B 1 208 ? -18.163 1.211   43.944  1.00 49.94  ?  213 SER   B CB  1 
ATOM   3623 O OG  . SER   B 1 208 ? -19.576 1.320   43.859  1.00 46.94  ?  213 SER   B OG  1 
ATOM   3624 N N   . PHE   B 1 209 ? -15.501 2.603   43.074  1.00 44.89  ?  214 PHE   B N   1 
ATOM   3625 C CA  . PHE   B 1 209 ? -14.055 2.692   42.783  1.00 50.81  ?  214 PHE   B CA  1 
ATOM   3626 C C   . PHE   B 1 209 ? -13.325 3.750   43.642  1.00 52.75  ?  214 PHE   B C   1 
ATOM   3627 O O   . PHE   B 1 209 ? -12.219 3.488   44.118  1.00 51.30  ?  214 PHE   B O   1 
ATOM   3628 C CB  . PHE   B 1 209 ? -13.824 2.922   41.274  1.00 52.91  ?  214 PHE   B CB  1 
ATOM   3629 C CG  . PHE   B 1 209 ? -12.404 3.256   40.911  1.00 54.83  ?  214 PHE   B CG  1 
ATOM   3630 C CD1 . PHE   B 1 209 ? -11.444 2.246   40.804  1.00 51.86  ?  214 PHE   B CD1 1 
ATOM   3631 C CD2 . PHE   B 1 209 ? -12.023 4.581   40.634  1.00 57.84  ?  214 PHE   B CD2 1 
ATOM   3632 C CE1 . PHE   B 1 209 ? -10.126 2.550   40.459  1.00 51.77  ?  214 PHE   B CE1 1 
ATOM   3633 C CE2 . PHE   B 1 209 ? -10.706 4.886   40.295  1.00 55.26  ?  214 PHE   B CE2 1 
ATOM   3634 C CZ  . PHE   B 1 209 ? -9.760  3.868   40.206  1.00 51.94  ?  214 PHE   B CZ  1 
ATOM   3635 N N   . ALA   B 1 210 ? -13.956 4.912   43.843  1.00 56.63  ?  215 ALA   B N   1 
ATOM   3636 C CA  . ALA   B 1 210 ? -13.405 5.956   44.727  1.00 58.29  ?  215 ALA   B CA  1 
ATOM   3637 C C   . ALA   B 1 210 ? -13.138 5.468   46.160  1.00 59.33  ?  215 ALA   B C   1 
ATOM   3638 O O   . ALA   B 1 210 ? -12.094 5.774   46.748  1.00 52.89  ?  215 ALA   B O   1 
ATOM   3639 C CB  . ALA   B 1 210 ? -14.324 7.164   44.781  1.00 56.59  ?  215 ALA   B CB  1 
ATOM   3640 N N   . VAL   B 1 211 ? -14.084 4.706   46.702  1.00 55.72  ?  216 VAL   B N   1 
ATOM   3641 C CA  . VAL   B 1 211 ? -13.986 4.226   48.079  1.00 54.64  ?  216 VAL   B CA  1 
ATOM   3642 C C   . VAL   B 1 211 ? -12.996 3.056   48.143  1.00 55.35  ?  216 VAL   B C   1 
ATOM   3643 O O   . VAL   B 1 211 ? -12.271 2.917   49.137  1.00 69.14  ?  216 VAL   B O   1 
ATOM   3644 C CB  . VAL   B 1 211 ? -15.359 3.880   48.705  1.00 53.19  ?  216 VAL   B CB  1 
ATOM   3645 C CG1 . VAL   B 1 211 ? -15.202 3.613   50.207  1.00 54.94  ?  216 VAL   B CG1 1 
ATOM   3646 C CG2 . VAL   B 1 211 ? -16.382 5.002   48.498  1.00 49.75  ?  216 VAL   B CG2 1 
ATOM   3647 N N   . VAL   B 1 212 ? -12.942 2.245   47.087  1.00 53.60  ?  217 VAL   B N   1 
ATOM   3648 C CA  . VAL   B 1 212 ? -11.914 1.199   46.948  1.00 48.59  ?  217 VAL   B CA  1 
ATOM   3649 C C   . VAL   B 1 212 ? -10.516 1.831   46.901  1.00 56.02  ?  217 VAL   B C   1 
ATOM   3650 O O   . VAL   B 1 212 ? -9.581  1.303   47.531  1.00 59.03  ?  217 VAL   B O   1 
ATOM   3651 C CB  . VAL   B 1 212 ? -12.173 0.321   45.701  1.00 48.59  ?  217 VAL   B CB  1 
ATOM   3652 C CG1 . VAL   B 1 212 ? -11.015 -0.626  45.404  1.00 55.16  ?  217 VAL   B CG1 1 
ATOM   3653 C CG2 . VAL   B 1 212 ? -13.442 -0.494  45.888  1.00 47.90  ?  217 VAL   B CG2 1 
ATOM   3654 N N   . LEU   B 1 213 ? -10.376 2.934   46.146  1.00 60.06  ?  218 LEU   B N   1 
ATOM   3655 C CA  . LEU   B 1 213 ? -9.131  3.722   46.128  1.00 56.07  ?  218 LEU   B CA  1 
ATOM   3656 C C   . LEU   B 1 213 ? -8.706  4.141   47.516  1.00 55.96  ?  218 LEU   B C   1 
ATOM   3657 O O   . LEU   B 1 213 ? -7.540  3.983   47.885  1.00 55.63  ?  218 LEU   B O   1 
ATOM   3658 C CB  . LEU   B 1 213 ? -9.260  4.976   45.259  1.00 66.22  ?  218 LEU   B CB  1 
ATOM   3659 C CG  . LEU   B 1 213 ? -8.689  4.921   43.861  1.00 74.99  ?  218 LEU   B CG  1 
ATOM   3660 C CD1 . LEU   B 1 213 ? -9.121  6.158   43.083  1.00 87.36  ?  218 LEU   B CD1 1 
ATOM   3661 C CD2 . LEU   B 1 213 ? -7.179  4.886   43.911  1.00 74.55  ?  218 LEU   B CD2 1 
ATOM   3662 N N   . TRP   B 1 214 ? -9.670  4.657   48.279  1.00 57.22  ?  219 TRP   B N   1 
ATOM   3663 C CA  . TRP   B 1 214 ? -9.436  5.044   49.671  1.00 57.33  ?  219 TRP   B CA  1 
ATOM   3664 C C   . TRP   B 1 214 ? -8.974  3.857   50.524  1.00 54.70  ?  219 TRP   B C   1 
ATOM   3665 O O   . TRP   B 1 214 ? -7.969  3.969   51.245  1.00 52.32  ?  219 TRP   B O   1 
ATOM   3666 C CB  . TRP   B 1 214 ? -10.691 5.696   50.279  1.00 59.43  ?  219 TRP   B CB  1 
ATOM   3667 C CG  . TRP   B 1 214 ? -10.435 6.239   51.655  1.00 63.69  ?  219 TRP   B CG  1 
ATOM   3668 C CD1 . TRP   B 1 214 ? -9.993  7.490   51.975  1.00 62.50  ?  219 TRP   B CD1 1 
ATOM   3669 C CD2 . TRP   B 1 214 ? -10.540 5.521   52.885  1.00 60.97  ?  219 TRP   B CD2 1 
ATOM   3670 N NE1 . TRP   B 1 214 ? -9.845  7.605   53.336  1.00 65.09  ?  219 TRP   B NE1 1 
ATOM   3671 C CE2 . TRP   B 1 214 ? -10.169 6.410   53.921  1.00 64.36  ?  219 TRP   B CE2 1 
ATOM   3672 C CE3 . TRP   B 1 214 ? -10.916 4.207   53.218  1.00 60.84  ?  219 TRP   B CE3 1 
ATOM   3673 C CZ2 . TRP   B 1 214 ? -10.165 6.026   55.278  1.00 65.42  ?  219 TRP   B CZ2 1 
ATOM   3674 C CZ3 . TRP   B 1 214 ? -10.920 3.826   54.569  1.00 61.15  ?  219 TRP   B CZ3 1 
ATOM   3675 C CH2 . TRP   B 1 214 ? -10.536 4.732   55.578  1.00 63.71  ?  219 TRP   B CH2 1 
ATOM   3676 N N   . ALA   B 1 215 ? -9.719  2.750   50.429  1.00 51.42  ?  220 ALA   B N   1 
ATOM   3677 C CA  . ALA   B 1 215 ? -9.411  1.502   51.153  1.00 54.27  ?  220 ALA   B CA  1 
ATOM   3678 C C   . ALA   B 1 215 ? -7.993  0.975   50.915  1.00 58.62  ?  220 ALA   B C   1 
ATOM   3679 O O   . ALA   B 1 215 ? -7.307  0.550   51.865  1.00 61.38  ?  220 ALA   B O   1 
ATOM   3680 C CB  . ALA   B 1 215 ? -10.419 0.419   50.795  1.00 55.16  ?  220 ALA   B CB  1 
ATOM   3681 N N   . ILE   B 1 216 ? -7.575  1.002   49.645  1.00 58.01  ?  221 ILE   B N   1 
ATOM   3682 C CA  . ILE   B 1 216 ? -6.231  0.562   49.224  1.00 57.74  ?  221 ILE   B CA  1 
ATOM   3683 C C   . ILE   B 1 216 ? -5.108  1.276   49.993  1.00 58.27  ?  221 ILE   B C   1 
ATOM   3684 O O   . ILE   B 1 216 ? -4.170  0.622   50.430  1.00 55.63  ?  221 ILE   B O   1 
ATOM   3685 C CB  . ILE   B 1 216 ? -6.067  0.669   47.679  1.00 57.58  ?  221 ILE   B CB  1 
ATOM   3686 C CG1 . ILE   B 1 216 ? -6.874  -0.449  47.009  1.00 56.58  ?  221 ILE   B CG1 1 
ATOM   3687 C CG2 . ILE   B 1 216 ? -4.612  0.526   47.234  1.00 64.70  ?  221 ILE   B CG2 1 
ATOM   3688 C CD1 . ILE   B 1 216 ? -7.281  -0.160  45.590  1.00 59.28  ?  221 ILE   B CD1 1 
ATOM   3689 N N   . PHE   B 1 217 ? -5.245  2.588   50.175  1.00 61.79  ?  222 PHE   B N   1 
ATOM   3690 C CA  . PHE   B 1 217 ? -4.240  3.401   50.890  1.00 68.50  ?  222 PHE   B CA  1 
ATOM   3691 C C   . PHE   B 1 217 ? -4.467  3.534   52.399  1.00 75.82  ?  222 PHE   B C   1 
ATOM   3692 O O   . PHE   B 1 217 ? -3.503  3.696   53.172  1.00 75.34  ?  222 PHE   B O   1 
ATOM   3693 C CB  . PHE   B 1 217 ? -4.117  4.763   50.215  1.00 72.31  ?  222 PHE   B CB  1 
ATOM   3694 C CG  . PHE   B 1 217 ? -3.428  4.682   48.891  1.00 72.94  ?  222 PHE   B CG  1 
ATOM   3695 C CD1 . PHE   B 1 217 ? -2.044  4.576   48.841  1.00 75.42  ?  222 PHE   B CD1 1 
ATOM   3696 C CD2 . PHE   B 1 217 ? -4.149  4.638   47.696  1.00 66.87  ?  222 PHE   B CD2 1 
ATOM   3697 C CE1 . PHE   B 1 217 ? -1.389  4.469   47.625  1.00 75.54  ?  222 PHE   B CE1 1 
ATOM   3698 C CE2 . PHE   B 1 217 ? -3.493  4.527   46.469  1.00 63.42  ?  222 PHE   B CE2 1 
ATOM   3699 C CZ  . PHE   B 1 217 ? -2.109  4.447   46.432  1.00 67.59  ?  222 PHE   B CZ  1 
ATOM   3700 N N   . ALA   B 1 218 ? -5.730  3.475   52.818  1.00 74.55  ?  223 ALA   B N   1 
ATOM   3701 C CA  . ALA   B 1 218 ? -6.073  3.344   54.238  1.00 74.15  ?  223 ALA   B CA  1 
ATOM   3702 C C   . ALA   B 1 218 ? -5.664  2.003   54.867  1.00 72.35  ?  223 ALA   B C   1 
ATOM   3703 O O   . ALA   B 1 218 ? -5.399  1.971   56.062  1.00 81.12  ?  223 ALA   B O   1 
ATOM   3704 C CB  . ALA   B 1 218 ? -7.565  3.587   54.445  1.00 73.56  ?  223 ALA   B CB  1 
ATOM   3705 N N   . ASN   B 1 219 ? -5.641  0.921   54.072  1.00 69.45  ?  224 ASN   B N   1 
ATOM   3706 C CA  . ASN   B 1 219 ? -5.530  -0.482  54.563  1.00 73.02  ?  224 ASN   B CA  1 
ATOM   3707 C C   . ASN   B 1 219 ? -6.627  -0.909  55.558  1.00 75.07  ?  224 ASN   B C   1 
ATOM   3708 O O   . ASN   B 1 219 ? -6.393  -1.708  56.479  1.00 75.76  ?  224 ASN   B O   1 
ATOM   3709 C CB  . ASN   B 1 219 ? -4.134  -0.765  55.137  1.00 76.88  ?  224 ASN   B CB  1 
ATOM   3710 C CG  . ASN   B 1 219 ? -3.024  -0.463  54.155  1.00 85.10  ?  224 ASN   B CG  1 
ATOM   3711 O OD1 . ASN   B 1 219 ? -3.137  -0.764  52.964  1.00 101.73 ?  224 ASN   B OD1 1 
ATOM   3712 N ND2 . ASN   B 1 219 ? -1.940  0.135   54.641  1.00 100.44 ?  224 ASN   B ND2 1 
ATOM   3713 N N   . LYS   B 1 220 ? -7.829  -0.382  55.340  1.00 75.05  ?  225 LYS   B N   1 
ATOM   3714 C CA  . LYS   B 1 220 ? -8.973  -0.640  56.212  1.00 75.89  ?  225 LYS   B CA  1 
ATOM   3715 C C   . LYS   B 1 220 ? -10.264 -0.217  55.538  1.00 66.91  ?  225 LYS   B C   1 
ATOM   3716 O O   . LYS   B 1 220 ? -10.250 0.511   54.547  1.00 57.49  ?  225 LYS   B O   1 
ATOM   3717 C CB  . LYS   B 1 220 ? -8.830  0.067   57.583  1.00 79.06  ?  225 LYS   B CB  1 
ATOM   3718 C CG  . LYS   B 1 220 ? -8.747  1.592   57.545  1.00 79.00  ?  225 LYS   B CG  1 
ATOM   3719 C CD  . LYS   B 1 220 ? -8.555  2.187   58.933  1.00 78.44  ?  225 LYS   B CD  1 
ATOM   3720 C CE  . LYS   B 1 220 ? -8.384  3.662   58.878  0.00 77.23  ?  225 LYS   B CE  1 
ATOM   3721 N NZ  . LYS   B 1 220 ? -7.920  4.215   60.179  0.00 81.32  ?  225 LYS   B NZ  1 
ATOM   3722 N N   . GLU   B 1 221 ? -11.372 -0.692  56.107  1.00 68.19  ?  226 GLU   B N   1 
ATOM   3723 C CA  . GLU   B 1 221 ? -12.716 -0.296  55.710  1.00 64.43  ?  226 GLU   B CA  1 
ATOM   3724 C C   . GLU   B 1 221 ? -12.940 1.136   56.229  1.00 64.72  ?  226 GLU   B C   1 
ATOM   3725 O O   . GLU   B 1 221 ? -12.425 1.489   57.298  1.00 76.05  ?  226 GLU   B O   1 
ATOM   3726 C CB  . GLU   B 1 221 ? -13.772 -1.242  56.305  1.00 67.40  ?  226 GLU   B CB  1 
ATOM   3727 C CG  . GLU   B 1 221 ? -13.726 -2.694  55.807  1.00 73.86  ?  226 GLU   B CG  1 
ATOM   3728 C CD  . GLU   B 1 221 ? -14.295 -2.922  54.407  1.00 85.52  ?  226 GLU   B CD  1 
ATOM   3729 O OE1 . GLU   B 1 221 ? -14.907 -2.023  53.816  1.00 96.13  ?  226 GLU   B OE1 1 
ATOM   3730 O OE2 . GLU   B 1 221 ? -14.158 -4.048  53.882  1.00 95.67  ?  226 GLU   B OE2 1 
ATOM   3731 N N   . PRO   B 1 222 ? -13.691 1.975   55.483  1.00 62.81  ?  227 PRO   B N   1 
ATOM   3732 C CA  . PRO   B 1 222 ? -13.984 3.328   55.950  1.00 59.24  ?  227 PRO   B CA  1 
ATOM   3733 C C   . PRO   B 1 222 ? -15.046 3.414   57.054  1.00 59.84  ?  227 PRO   B C   1 
ATOM   3734 O O   . PRO   B 1 222 ? -15.712 2.426   57.375  1.00 63.86  ?  227 PRO   B O   1 
ATOM   3735 C CB  . PRO   B 1 222 ? -14.482 4.012   54.677  1.00 58.77  ?  227 PRO   B CB  1 
ATOM   3736 C CG  . PRO   B 1 222 ? -15.183 2.933   53.956  1.00 56.63  ?  227 PRO   B CG  1 
ATOM   3737 C CD  . PRO   B 1 222 ? -14.289 1.746   54.151  1.00 60.89  ?  227 PRO   B CD  1 
ATOM   3738 N N   . TYR   B 1 223 ? -15.189 4.625   57.582  1.00 59.45  ?  228 TYR   B N   1 
ATOM   3739 C CA  . TYR   B 1 223 ? -16.258 5.023   58.504  1.00 63.92  ?  228 TYR   B CA  1 
ATOM   3740 C C   . TYR   B 1 223 ? -16.235 4.336   59.880  1.00 69.05  ?  228 TYR   B C   1 
ATOM   3741 O O   . TYR   B 1 223 ? -17.288 4.170   60.509  1.00 78.72  ?  228 TYR   B O   1 
ATOM   3742 C CB  . TYR   B 1 223 ? -17.635 4.863   57.842  1.00 60.18  ?  228 TYR   B CB  1 
ATOM   3743 C CG  . TYR   B 1 223 ? -17.771 5.476   56.469  1.00 57.51  ?  228 TYR   B CG  1 
ATOM   3744 C CD1 . TYR   B 1 223 ? -17.734 6.871   56.292  1.00 59.20  ?  228 TYR   B CD1 1 
ATOM   3745 C CD2 . TYR   B 1 223 ? -18.017 4.677   55.349  1.00 53.04  ?  228 TYR   B CD2 1 
ATOM   3746 C CE1 . TYR   B 1 223 ? -17.907 7.440   55.026  1.00 59.93  ?  228 TYR   B CE1 1 
ATOM   3747 C CE2 . TYR   B 1 223 ? -18.188 5.230   54.084  1.00 53.56  ?  228 TYR   B CE2 1 
ATOM   3748 C CZ  . TYR   B 1 223 ? -18.136 6.608   53.912  1.00 55.92  ?  228 TYR   B CZ  1 
ATOM   3749 O OH  . TYR   B 1 223 ? -18.312 7.131   52.644  1.00 52.38  ?  228 TYR   B OH  1 
ATOM   3750 N N   . GLU   B 1 224 ? -15.039 3.974   60.351  1.00 71.33  ?  229 GLU   B N   1 
ATOM   3751 C CA  . GLU   B 1 224 ? -14.835 3.311   61.662  1.00 72.70  ?  229 GLU   B CA  1 
ATOM   3752 C C   . GLU   B 1 224 ? -15.482 4.003   62.882  1.00 72.25  ?  229 GLU   B C   1 
ATOM   3753 O O   . GLU   B 1 224 ? -16.041 3.335   63.752  1.00 73.54  ?  229 GLU   B O   1 
ATOM   3754 C CB  . GLU   B 1 224 ? -13.333 3.053   61.913  1.00 74.31  ?  229 GLU   B CB  1 
ATOM   3755 C CG  . GLU   B 1 224 ? -12.414 4.276   61.897  1.00 79.67  ?  229 GLU   B CG  1 
ATOM   3756 C CD  . GLU   B 1 224 ? -11.016 3.962   62.404  1.00 86.73  ?  229 GLU   B CD  1 
ATOM   3757 O OE1 . GLU   B 1 224 ? -10.503 4.725   63.260  1.00 94.79  ?  229 GLU   B OE1 1 
ATOM   3758 O OE2 . GLU   B 1 224 ? -10.432 2.948   61.955  1.00 81.90  ?  229 GLU   B OE2 1 
ATOM   3759 N N   . ASN   B 1 225 ? -15.446 5.329   62.875  1.00 75.96  ?  230 ASN   B N   1 
ATOM   3760 C CA  . ASN   B 1 225 ? -16.078 6.140   63.941  1.00 79.53  ?  230 ASN   B CA  1 
ATOM   3761 C C   . ASN   B 1 225 ? -17.607 6.219   63.913  1.00 79.64  ?  230 ASN   B C   1 
ATOM   3762 O O   . ASN   B 1 225 ? -18.174 6.815   64.833  1.00 92.69  ?  230 ASN   B O   1 
ATOM   3763 C CB  . ASN   B 1 225 ? -15.490 7.561   63.971  1.00 82.02  ?  230 ASN   B CB  1 
ATOM   3764 C CG  . ASN   B 1 225 ? -14.064 7.603   64.487  1.00 85.73  ?  230 ASN   B CG  1 
ATOM   3765 O OD1 . ASN   B 1 225 ? -13.497 6.600   64.940  1.00 85.15  ?  230 ASN   B OD1 1 
ATOM   3766 N ND2 . ASN   B 1 225 ? -13.471 8.785   64.421  1.00 89.92  ?  230 ASN   B ND2 1 
ATOM   3767 N N   . ALA   B 1 226 ? -18.283 5.670   62.897  1.00 75.93  ?  231 ALA   B N   1 
ATOM   3768 C CA  . ALA   B 1 226 ? -19.755 5.632   62.830  1.00 74.50  ?  231 ALA   B CA  1 
ATOM   3769 C C   . ALA   B 1 226 ? -20.320 4.707   63.911  1.00 76.92  ?  231 ALA   B C   1 
ATOM   3770 O O   . ALA   B 1 226 ? -19.820 3.605   64.098  1.00 80.35  ?  231 ALA   B O   1 
ATOM   3771 C CB  . ALA   B 1 226 ? -20.219 5.178   61.452  1.00 69.68  ?  231 ALA   B CB  1 
ATOM   3772 N N   . ILE   B 1 227 ? -21.336 5.186   64.626  1.00 82.62  ?  232 ILE   B N   1 
ATOM   3773 C CA  . ILE   B 1 227 ? -21.952 4.483   65.767  1.00 86.00  ?  232 ILE   B CA  1 
ATOM   3774 C C   . ILE   B 1 227 ? -23.190 3.672   65.355  1.00 88.56  ?  232 ILE   B C   1 
ATOM   3775 O O   . ILE   B 1 227 ? -23.441 2.635   65.960  1.00 94.60  ?  232 ILE   B O   1 
ATOM   3776 C CB  . ILE   B 1 227 ? -22.346 5.458   66.915  1.00 86.33  ?  232 ILE   B CB  1 
ATOM   3777 C CG1 . ILE   B 1 227 ? -21.205 6.434   67.240  1.00 88.08  ?  232 ILE   B CG1 1 
ATOM   3778 C CG2 . ILE   B 1 227 ? -22.717 4.703   68.183  1.00 90.66  ?  232 ILE   B CG2 1 
ATOM   3779 C CD1 . ILE   B 1 227 ? -19.862 5.844   67.568  0.00 82.87  ?  232 ILE   B CD1 1 
ATOM   3780 N N   . ALA   B 1 228 ? -23.971 4.163   64.383  1.00 88.33  ?  233 ALA   B N   1 
ATOM   3781 C CA  . ALA   B 1 228 ? -25.212 3.512   63.929  1.00 87.03  ?  233 ALA   B CA  1 
ATOM   3782 C C   . ALA   B 1 228 ? -25.300 3.529   62.417  1.00 81.74  ?  233 ALA   B C   1 
ATOM   3783 O O   . ALA   B 1 228 ? -24.629 4.327   61.764  1.00 75.42  ?  233 ALA   B O   1 
ATOM   3784 C CB  . ALA   B 1 228 ? -26.422 4.221   64.520  1.00 89.91  ?  233 ALA   B CB  1 
ATOM   3785 N N   . GLU   B 1 229 ? -26.161 2.661   61.885  1.00 82.22  ?  234 GLU   B N   1 
ATOM   3786 C CA  . GLU   B 1 229 ? -26.324 2.476   60.437  1.00 80.39  ?  234 GLU   B CA  1 
ATOM   3787 C C   . GLU   B 1 229 ? -27.085 3.638   59.785  1.00 82.17  ?  234 GLU   B C   1 
ATOM   3788 O O   . GLU   B 1 229 ? -26.634 4.190   58.780  1.00 81.77  ?  234 GLU   B O   1 
ATOM   3789 C CB  . GLU   B 1 229 ? -27.036 1.155   60.133  1.00 81.23  ?  234 GLU   B CB  1 
ATOM   3790 C CG  . GLU   B 1 229 ? -26.718 0.610   58.747  1.00 82.84  ?  234 GLU   B CG  1 
ATOM   3791 C CD  . GLU   B 1 229 ? -27.433 -0.697  58.449  1.00 92.78  ?  234 GLU   B CD  1 
ATOM   3792 O OE1 . GLU   B 1 229 ? -28.684 -0.698  58.443  1.00 98.41  ?  234 GLU   B OE1 1 
ATOM   3793 O OE2 . GLU   B 1 229 ? -26.749 -1.722  58.217  1.00 97.10  ?  234 GLU   B OE2 1 
ATOM   3794 N N   . GLN   B 1 230 ? -28.219 4.010   60.380  1.00 84.06  ?  235 GLN   B N   1 
ATOM   3795 C CA  . GLN   B 1 230 ? -28.981 5.210   59.959  1.00 87.92  ?  235 GLN   B CA  1 
ATOM   3796 C C   . GLN   B 1 230 ? -28.165 6.508   60.028  1.00 88.50  ?  235 GLN   B C   1 
ATOM   3797 O O   . GLN   B 1 230 ? -28.311 7.364   59.147  1.00 95.55  ?  235 GLN   B O   1 
ATOM   3798 C CB  . GLN   B 1 230 ? -30.299 5.386   60.747  1.00 99.29  ?  235 GLN   B CB  1 
ATOM   3799 C CG  . GLN   B 1 230 ? -31.538 4.801   60.085  1.00 105.27 ?  235 GLN   B CG  1 
ATOM   3800 C CD  . GLN   B 1 230 ? -32.021 5.637   58.908  1.00 105.45 ?  235 GLN   B CD  1 
ATOM   3801 O OE1 . GLN   B 1 230 ? -32.695 6.657   59.088  1.00 108.95 ?  235 GLN   B OE1 1 
ATOM   3802 N NE2 . GLN   B 1 230 ? -31.681 5.209   57.696  1.00 99.88  ?  235 GLN   B NE2 1 
ATOM   3803 N N   . GLN   B 1 231 ? -27.305 6.640   61.047  1.00 84.85  ?  236 GLN   B N   1 
ATOM   3804 C CA  . GLN   B 1 231 ? -26.349 7.771   61.139  1.00 81.79  ?  236 GLN   B CA  1 
ATOM   3805 C C   . GLN   B 1 231 ? -25.442 7.816   59.913  1.00 73.35  ?  236 GLN   B C   1 
ATOM   3806 O O   . GLN   B 1 231 ? -25.266 8.873   59.320  1.00 77.91  ?  236 GLN   B O   1 
ATOM   3807 C CB  . GLN   B 1 231 ? -25.474 7.680   62.412  1.00 81.15  ?  236 GLN   B CB  1 
ATOM   3808 C CG  . GLN   B 1 231 ? -24.412 8.787   62.612  1.00 79.45  ?  236 GLN   B CG  1 
ATOM   3809 C CD  . GLN   B 1 231 ? -23.169 8.345   63.403  1.00 79.99  ?  236 GLN   B CD  1 
ATOM   3810 O OE1 . GLN   B 1 231 ? -22.907 7.155   63.588  1.00 82.48  ?  236 GLN   B OE1 1 
ATOM   3811 N NE2 . GLN   B 1 231 ? -22.384 9.316   63.855  1.00 81.57  ?  236 GLN   B NE2 1 
ATOM   3812 N N   . LEU   B 1 232 ? -24.869 6.669   59.573  1.00 69.01  ?  237 LEU   B N   1 
ATOM   3813 C CA  . LEU   B 1 232 ? -23.940 6.554   58.462  1.00 68.71  ?  237 LEU   B CA  1 
ATOM   3814 C C   . LEU   B 1 232 ? -24.606 6.815   57.122  1.00 69.78  ?  237 LEU   B C   1 
ATOM   3815 O O   . LEU   B 1 232 ? -24.112 7.634   56.348  1.00 69.76  ?  237 LEU   B O   1 
ATOM   3816 C CB  . LEU   B 1 232 ? -23.248 5.177   58.457  1.00 63.48  ?  237 LEU   B CB  1 
ATOM   3817 C CG  . LEU   B 1 232 ? -22.185 4.933   57.373  1.00 60.05  ?  237 LEU   B CG  1 
ATOM   3818 C CD1 . LEU   B 1 232 ? -21.059 5.949   57.391  1.00 59.48  ?  237 LEU   B CD1 1 
ATOM   3819 C CD2 . LEU   B 1 232 ? -21.605 3.550   57.508  1.00 58.55  ?  237 LEU   B CD2 1 
ATOM   3820 N N   . ILE   B 1 233 ? -25.720 6.122   56.878  1.00 72.71  ?  238 ILE   B N   1 
ATOM   3821 C CA  . ILE   B 1 233 ? -26.502 6.239   55.637  1.00 72.28  ?  238 ILE   B CA  1 
ATOM   3822 C C   . ILE   B 1 233 ? -26.852 7.709   55.389  1.00 76.15  ?  238 ILE   B C   1 
ATOM   3823 O O   . ILE   B 1 233 ? -26.531 8.251   54.319  1.00 83.75  ?  238 ILE   B O   1 
ATOM   3824 C CB  . ILE   B 1 233 ? -27.794 5.371   55.670  1.00 74.13  ?  238 ILE   B CB  1 
ATOM   3825 C CG1 . ILE   B 1 233 ? -27.461 3.867   55.656  1.00 66.81  ?  238 ILE   B CG1 1 
ATOM   3826 C CG2 . ILE   B 1 233 ? -28.735 5.698   54.503  1.00 76.18  ?  238 ILE   B CG2 1 
ATOM   3827 C CD1 . ILE   B 1 233 ? -28.541 2.960   56.153  0.00 66.50  ?  238 ILE   B CD1 1 
ATOM   3828 N N   . MET   B 1 234 ? -27.457 8.343   56.393  1.00 76.80  ?  239 MET   B N   1 
ATOM   3829 C CA  . MET   B 1 234 ? -27.842 9.756   56.296  1.00 84.48  ?  239 MET   B CA  1 
ATOM   3830 C C   . MET   B 1 234 ? -26.660 10.738  56.210  1.00 81.09  ?  239 MET   B C   1 
ATOM   3831 O O   . MET   B 1 234 ? -26.805 11.786  55.586  1.00 89.17  ?  239 MET   B O   1 
ATOM   3832 C CB  . MET   B 1 234 ? -28.799 10.145  57.443  1.00 94.31  ?  239 MET   B CB  1 
ATOM   3833 C CG  . MET   B 1 234 ? -30.152 9.415   57.442  1.00 102.21 ?  239 MET   B CG  1 
ATOM   3834 S SD  . MET   B 1 234 ? -31.151 9.536   55.939  1.00 109.08 ?  239 MET   B SD  1 
ATOM   3835 C CE  . MET   B 1 234 ? -31.770 11.197  56.123  1.00 125.19 ?  239 MET   B CE  1 
ATOM   3836 N N   . ALA   B 1 235 ? -25.520 10.394  56.808  1.00 73.93  ?  240 ALA   B N   1 
ATOM   3837 C CA  . ALA   B 1 235 ? -24.288 11.180  56.657  1.00 70.13  ?  240 ALA   B CA  1 
ATOM   3838 C C   . ALA   B 1 235 ? -23.754 11.142  55.229  1.00 67.08  ?  240 ALA   B C   1 
ATOM   3839 O O   . ALA   B 1 235 ? -23.395 12.194  54.682  1.00 66.42  ?  240 ALA   B O   1 
ATOM   3840 C CB  . ALA   B 1 235 ? -23.218 10.713  57.632  1.00 69.04  ?  240 ALA   B CB  1 
ATOM   3841 N N   . ILE   B 1 236 ? -23.707 9.947   54.628  1.00 65.10  ?  241 ILE   B N   1 
ATOM   3842 C CA  . ILE   B 1 236 ? -23.176 9.783   53.252  1.00 64.08  ?  241 ILE   B CA  1 
ATOM   3843 C C   . ILE   B 1 236 ? -24.050 10.530  52.234  1.00 65.21  ?  241 ILE   B C   1 
ATOM   3844 O O   . ILE   B 1 236 ? -23.522 11.238  51.365  1.00 63.30  ?  241 ILE   B O   1 
ATOM   3845 C CB  . ILE   B 1 236 ? -23.003 8.291   52.827  1.00 59.81  ?  241 ILE   B CB  1 
ATOM   3846 C CG1 . ILE   B 1 236 ? -21.963 7.574   53.700  1.00 59.99  ?  241 ILE   B CG1 1 
ATOM   3847 C CG2 . ILE   B 1 236 ? -22.545 8.179   51.369  1.00 56.27  ?  241 ILE   B CG2 1 
ATOM   3848 C CD1 . ILE   B 1 236 ? -22.248 6.117   53.885  0.00 52.28  ?  241 ILE   B CD1 1 
ATOM   3849 N N   . LYS   B 1 237 ? -25.370 10.356  52.359  1.00 72.31  ?  242 LYS   B N   1 
ATOM   3850 C CA  . LYS   B 1 237 ? -26.373 11.106  51.588  1.00 73.53  ?  242 LYS   B CA  1 
ATOM   3851 C C   . LYS   B 1 237 ? -26.222 12.624  51.719  1.00 75.62  ?  242 LYS   B C   1 
ATOM   3852 O O   . LYS   B 1 237 ? -26.348 13.335  50.722  1.00 82.54  ?  242 LYS   B O   1 
ATOM   3853 C CB  . LYS   B 1 237 ? -27.792 10.679  51.999  1.00 75.97  ?  242 LYS   B CB  1 
ATOM   3854 C CG  . LYS   B 1 237 ? -28.178 9.270   51.513  1.00 74.57  ?  242 LYS   B CG  1 
ATOM   3855 C CD  . LYS   B 1 237 ? -29.683 9.054   51.372  1.00 80.57  ?  242 LYS   B CD  1 
ATOM   3856 C CE  . LYS   B 1 237 ? -30.276 9.720   50.128  1.00 88.01  ?  242 LYS   B CE  1 
ATOM   3857 N NZ  . LYS   B 1 237 ? -30.129 8.906   48.891  1.00 87.21  ?  242 LYS   B NZ  1 
ATOM   3858 N N   . SER   B 1 238 ? -25.926 13.105  52.931  1.00 76.97  ?  243 SER   B N   1 
ATOM   3859 C CA  . SER   B 1 238 ? -25.661 14.553  53.170  1.00 79.63  ?  243 SER   B CA  1 
ATOM   3860 C C   . SER   B 1 238 ? -24.340 15.115  52.594  1.00 78.06  ?  243 SER   B C   1 
ATOM   3861 O O   . SER   B 1 238 ? -24.157 16.335  52.581  1.00 79.70  ?  243 SER   B O   1 
ATOM   3862 C CB  . SER   B 1 238 ? -25.749 14.899  54.675  1.00 79.85  ?  243 SER   B CB  1 
ATOM   3863 O OG  . SER   B 1 238 ? -24.582 14.517  55.392  1.00 74.69  ?  243 SER   B OG  1 
ATOM   3864 N N   . GLY   B 1 239 ? -23.429 14.243  52.155  1.00 78.51  ?  244 GLY   B N   1 
ATOM   3865 C CA  . GLY   B 1 239 ? -22.113 14.615  51.608  1.00 81.85  ?  244 GLY   B CA  1 
ATOM   3866 C C   . GLY   B 1 239 ? -20.877 14.072  52.320  1.00 77.36  ?  244 GLY   B C   1 
ATOM   3867 O O   . GLY   B 1 239 ? -19.766 14.320  51.859  1.00 74.61  ?  244 GLY   B O   1 
ATOM   3868 N N   . ASN   B 1 240 ? -21.052 13.330  53.416  1.00 80.24  ?  245 ASN   B N   1 
ATOM   3869 C CA  . ASN   B 1 240 ? -19.931 12.815  54.206  1.00 79.69  ?  245 ASN   B CA  1 
ATOM   3870 C C   . ASN   B 1 240 ? -19.245 11.648  53.475  1.00 72.98  ?  245 ASN   B C   1 
ATOM   3871 O O   . ASN   B 1 240 ? -19.907 10.847  52.797  1.00 68.34  ?  245 ASN   B O   1 
ATOM   3872 C CB  . ASN   B 1 240 ? -20.408 12.407  55.606  1.00 89.74  ?  245 ASN   B CB  1 
ATOM   3873 C CG  . ASN   B 1 240 ? -19.336 12.575  56.656  1.00 102.66 ?  245 ASN   B CG  1 
ATOM   3874 O OD1 . ASN   B 1 240 ? -19.257 13.616  57.313  1.00 107.55 ?  245 ASN   B OD1 1 
ATOM   3875 N ND2 . ASN   B 1 240 ? -18.485 11.567  56.805  1.00 115.93 ?  245 ASN   B ND2 1 
ATOM   3876 N N   . ARG   B 1 241 ? -17.921 11.573  53.612  1.00 67.75  ?  246 ARG   B N   1 
ATOM   3877 C CA  . ARG   B 1 241 ? -17.059 10.690  52.811  1.00 62.99  ?  246 ARG   B CA  1 
ATOM   3878 C C   . ARG   B 1 241 ? -15.963 10.069  53.675  1.00 63.08  ?  246 ARG   B C   1 
ATOM   3879 O O   . ARG   B 1 241 ? -15.869 10.417  54.862  1.00 68.69  ?  246 ARG   B O   1 
ATOM   3880 C CB  . ARG   B 1 241 ? -16.439 11.513  51.661  1.00 68.02  ?  246 ARG   B CB  1 
ATOM   3881 C CG  . ARG   B 1 241 ? -17.410 11.945  50.568  1.00 65.43  ?  246 ARG   B CG  1 
ATOM   3882 C CD  . ARG   B 1 241 ? -17.941 10.759  49.777  1.00 63.53  ?  246 ARG   B CD  1 
ATOM   3883 N NE  . ARG   B 1 241 ? -18.915 11.148  48.764  1.00 61.36  ?  246 ARG   B NE  1 
ATOM   3884 C CZ  . ARG   B 1 241 ? -20.222 11.351  48.961  1.00 63.86  ?  246 ARG   B CZ  1 
ATOM   3885 N NH1 . ARG   B 1 241 ? -20.800 11.252  50.181  1.00 68.15  ?  246 ARG   B NH1 1 
ATOM   3886 N NH2 . ARG   B 1 241 ? -20.977 11.679  47.912  1.00 69.87  ?  246 ARG   B NH2 1 
ATOM   3887 N N   . PRO   B 1 242 ? -15.166 9.121   53.118  1.00 57.54  ?  247 PRO   B N   1 
ATOM   3888 C CA  . PRO   B 1 242 ? -14.081 8.554   53.921  1.00 60.49  ?  247 PRO   B CA  1 
ATOM   3889 C C   . PRO   B 1 242 ? -13.020 9.579   54.305  1.00 60.94  ?  247 PRO   B C   1 
ATOM   3890 O O   . PRO   B 1 242 ? -12.709 10.465  53.524  1.00 63.00  ?  247 PRO   B O   1 
ATOM   3891 C CB  . PRO   B 1 242 ? -13.499 7.453   53.014  1.00 56.63  ?  247 PRO   B CB  1 
ATOM   3892 C CG  . PRO   B 1 242 ? -14.637 7.066   52.159  1.00 57.04  ?  247 PRO   B CG  1 
ATOM   3893 C CD  . PRO   B 1 242 ? -15.310 8.376   51.854  1.00 58.44  ?  247 PRO   B CD  1 
ATOM   3894 N N   . ASP   B 1 243 ? -12.505 9.450   55.521  1.00 69.82  ?  248 ASP   B N   1 
ATOM   3895 C CA  . ASP   B 1 243 ? -11.614 10.449  56.111  1.00 78.09  ?  248 ASP   B CA  1 
ATOM   3896 C C   . ASP   B 1 243 ? -10.243 10.328  55.444  1.00 79.14  ?  248 ASP   B C   1 
ATOM   3897 O O   . ASP   B 1 243 ? -9.595  9.286   55.541  1.00 79.80  ?  248 ASP   B O   1 
ATOM   3898 C CB  . ASP   B 1 243 ? -11.518 10.248  57.641  1.00 79.95  ?  248 ASP   B CB  1 
ATOM   3899 C CG  . ASP   B 1 243 ? -10.958 11.466  58.391  1.00 88.79  ?  248 ASP   B CG  1 
ATOM   3900 O OD1 . ASP   B 1 243 ? -10.514 12.456  57.761  1.00 87.50  ?  248 ASP   B OD1 1 
ATOM   3901 O OD2 . ASP   B 1 243 ? -10.963 11.415  59.645  1.00 94.26  ?  248 ASP   B OD2 1 
ATOM   3902 N N   . VAL   B 1 244 ? -9.816  11.382  54.755  1.00 83.23  ?  249 VAL   B N   1 
ATOM   3903 C CA  . VAL   B 1 244 ? -8.498  11.405  54.093  1.00 89.21  ?  249 VAL   B CA  1 
ATOM   3904 C C   . VAL   B 1 244 ? -7.346  11.449  55.128  1.00 93.47  ?  249 VAL   B C   1 
ATOM   3905 O O   . VAL   B 1 244 ? -6.291  10.856  54.893  1.00 99.26  ?  249 VAL   B O   1 
ATOM   3906 C CB  . VAL   B 1 244 ? -8.396  12.548  53.050  1.00 92.31  ?  249 VAL   B CB  1 
ATOM   3907 C CG1 . VAL   B 1 244 ? -7.038  12.536  52.342  1.00 100.59 ?  249 VAL   B CG1 1 
ATOM   3908 C CG2 . VAL   B 1 244 ? -9.510  12.426  52.005  1.00 85.56  ?  249 VAL   B CG2 1 
ATOM   3909 N N   . ASP   B 1 245 ? -7.567  12.120  56.260  1.00 95.92  ?  250 ASP   B N   1 
ATOM   3910 C CA  . ASP   B 1 245 ? -6.601  12.142  57.386  1.00 108.54 ?  250 ASP   B CA  1 
ATOM   3911 C C   . ASP   B 1 245 ? -6.380  10.781  58.086  1.00 116.52 ?  250 ASP   B C   1 
ATOM   3912 O O   . ASP   B 1 245 ? -5.359  10.615  58.760  1.00 116.25 ?  250 ASP   B O   1 
ATOM   3913 C CB  . ASP   B 1 245 ? -6.997  13.187  58.460  1.00 110.47 ?  250 ASP   B CB  1 
ATOM   3914 C CG  . ASP   B 1 245 ? -7.115  14.605  57.909  1.00 105.99 ?  250 ASP   B CG  1 
ATOM   3915 O OD1 . ASP   B 1 245 ? -6.324  14.998  57.022  1.00 105.66 ?  250 ASP   B OD1 1 
ATOM   3916 O OD2 . ASP   B 1 245 ? -8.020  15.326  58.376  1.00 102.70 ?  250 ASP   B OD2 1 
ATOM   3917 N N   . ASP   B 1 246 ? -7.328  9.839   57.951  1.00 125.07 ?  251 ASP   B N   1 
ATOM   3918 C CA  . ASP   B 1 246 ? -7.138  8.438   58.404  1.00 123.00 ?  251 ASP   B CA  1 
ATOM   3919 C C   . ASP   B 1 246 ? -6.082  7.643   57.615  1.00 128.52 ?  251 ASP   B C   1 
ATOM   3920 O O   . ASP   B 1 246 ? -5.639  6.594   58.107  1.00 141.91 ?  251 ASP   B O   1 
ATOM   3921 C CB  . ASP   B 1 246 ? -8.474  7.649   58.422  1.00 115.23 ?  251 ASP   B CB  1 
ATOM   3922 C CG  . ASP   B 1 246 ? -9.216  7.748   59.758  1.00 124.12 ?  251 ASP   B CG  1 
ATOM   3923 O OD1 . ASP   B 1 246 ? -9.101  8.771   60.474  1.00 117.30 ?  251 ASP   B OD1 1 
ATOM   3924 O OD2 . ASP   B 1 246 ? -9.935  6.779   60.088  1.00 124.03 ?  251 ASP   B OD2 1 
ATOM   3925 N N   . ILE   B 1 247 ? -5.710  8.106   56.413  1.00 125.41 ?  252 ILE   B N   1 
ATOM   3926 C CA  . ILE   B 1 247 ? -4.634  7.497   55.621  1.00 129.46 ?  252 ILE   B CA  1 
ATOM   3927 C C   . ILE   B 1 247 ? -3.289  7.808   56.305  1.00 154.30 ?  252 ILE   B C   1 
ATOM   3928 O O   . ILE   B 1 247 ? -2.812  8.942   56.250  1.00 163.16 ?  252 ILE   B O   1 
ATOM   3929 C CB  . ILE   B 1 247 ? -4.638  7.975   54.138  1.00 118.93 ?  252 ILE   B CB  1 
ATOM   3930 C CG1 . ILE   B 1 247 ? -5.966  7.596   53.451  1.00 113.58 ?  252 ILE   B CG1 1 
ATOM   3931 C CG2 . ILE   B 1 247 ? -3.491  7.340   53.349  1.00 124.42 ?  252 ILE   B CG2 1 
ATOM   3932 C CD1 . ILE   B 1 247 ? -6.231  8.274   52.121  1.00 109.60 ?  252 ILE   B CD1 1 
ATOM   3933 N N   . THR   B 1 248 ? -2.706  6.785   56.940  1.00 169.25 ?  253 THR   B N   1 
ATOM   3934 C CA  . THR   B 1 248 ? -1.408  6.867   57.646  1.00 162.39 ?  253 THR   B CA  1 
ATOM   3935 C C   . THR   B 1 248 ? -0.198  6.740   56.705  1.00 161.08 ?  253 THR   B C   1 
ATOM   3936 O O   . THR   B 1 248 ? 0.815   7.425   56.899  1.00 162.47 ?  253 THR   B O   1 
ATOM   3937 C CB  . THR   B 1 248 ? -1.296  5.776   58.740  1.00 147.42 ?  253 THR   B CB  1 
ATOM   3938 O OG1 . THR   B 1 248 ? -1.440  4.468   58.156  0.00 156.29 ?  253 THR   B OG1 1 
ATOM   3939 C CG2 . THR   B 1 248 ? -2.316  5.983   59.816  0.00 160.30 ?  253 THR   B CG2 1 
ATOM   3940 N N   . GLU   B 1 249 ? -0.311  5.866   55.698  1.00 153.44 ?  254 GLU   B N   1 
ATOM   3941 C CA  . GLU   B 1 249 ? 0.704   5.733   54.633  1.00 149.11 ?  254 GLU   B CA  1 
ATOM   3942 C C   . GLU   B 1 249 ? 0.808   6.979   53.743  1.00 150.32 ?  254 GLU   B C   1 
ATOM   3943 O O   . GLU   B 1 249 ? -0.089  7.834   53.722  1.00 149.79 ?  254 GLU   B O   1 
ATOM   3944 C CB  . GLU   B 1 249 ? 0.428   4.497   53.752  1.00 137.67 ?  254 GLU   B CB  1 
ATOM   3945 C CG  . GLU   B 1 249 ? 0.814   3.160   54.223  0.00 138.79 ?  254 GLU   B CG  1 
ATOM   3946 C CD  . GLU   B 1 249 ? 0.785   2.067   53.155  0.00 134.36 ?  254 GLU   B CD  1 
ATOM   3947 O OE1 . GLU   B 1 249 ? 1.346   2.259   52.055  0.00 133.88 ?  254 GLU   B OE1 1 
ATOM   3948 O OE2 . GLU   B 1 249 ? 0.197   0.996   53.401  0.00 131.50 ?  254 GLU   B OE2 1 
ATOM   3949 N N   . TYR   B 1 250 ? 1.928   7.079   53.030  1.00 147.77 ?  255 TYR   B N   1 
ATOM   3950 C CA  . TYR   B 1 250 ? 2.113   8.138   52.023  1.00 139.04 ?  255 TYR   B CA  1 
ATOM   3951 C C   . TYR   B 1 250 ? 1.256   7.808   50.793  1.00 124.69 ?  255 TYR   B C   1 
ATOM   3952 O O   . TYR   B 1 250 ? 1.620   6.927   50.003  1.00 114.00 ?  255 TYR   B O   1 
ATOM   3953 C CB  . TYR   B 1 250 ? 3.591   8.295   51.639  1.00 139.92 ?  255 TYR   B CB  1 
ATOM   3954 C CG  . TYR   B 1 250 ? 3.760   9.271   50.475  0.00 141.56 ?  255 TYR   B CG  1 
ATOM   3955 C CD1 . TYR   B 1 250 ? 3.477   10.630  50.605  0.00 143.56 ?  255 TYR   B CD1 1 
ATOM   3956 C CD2 . TYR   B 1 250 ? 4.223   8.811   49.242  0.00 140.20 ?  255 TYR   B CD2 1 
ATOM   3957 C CE1 . TYR   B 1 250 ? 3.652   11.504  49.542  0.00 144.54 ?  255 TYR   B CE1 1 
ATOM   3958 C CE2 . TYR   B 1 250 ? 4.401   9.677   48.175  0.00 141.14 ?  255 TYR   B CE2 1 
ATOM   3959 C CZ  . TYR   B 1 250 ? 4.116   11.021  48.329  0.00 143.34 ?  255 TYR   B CZ  1 
ATOM   3960 O OH  . TYR   B 1 250 ? 4.293   11.883  47.271  0.00 144.79 ?  255 TYR   B OH  1 
ATOM   3961 N N   . CYS   B 1 251 ? 0.109   8.486   50.660  1.00 114.61 ?  256 CYS   B N   1 
ATOM   3962 C CA  . CYS   B 1 251 ? -0.699  8.468   49.438  1.00 105.48 ?  256 CYS   B CA  1 
ATOM   3963 C C   . CYS   B 1 251 ? -0.389  9.754   48.647  1.00 109.07 ?  256 CYS   B C   1 
ATOM   3964 O O   . CYS   B 1 251 ? -0.368  10.834  49.252  1.00 115.84 ?  256 CYS   B O   1 
ATOM   3965 C CB  . CYS   B 1 251 ? -2.186  8.402   49.755  1.00 96.28  ?  256 CYS   B CB  1 
ATOM   3966 S SG  . CYS   B 1 251 ? -3.177  8.184   48.257  1.00 92.39  ?  256 CYS   B SG  1 
ATOM   3967 N N   . PRO   B 1 252 ? -0.121  9.641   47.321  1.00 102.21 ?  257 PRO   B N   1 
ATOM   3968 C CA  . PRO   B 1 252 ? 0.088   10.843  46.494  1.00 103.62 ?  257 PRO   B CA  1 
ATOM   3969 C C   . PRO   B 1 252 ? -1.101  11.811  46.419  1.00 99.90  ?  257 PRO   B C   1 
ATOM   3970 O O   . PRO   B 1 252 ? -2.245  11.400  46.619  1.00 96.41  ?  257 PRO   B O   1 
ATOM   3971 C CB  . PRO   B 1 252 ? 0.368   10.261  45.109  1.00 102.66 ?  257 PRO   B CB  1 
ATOM   3972 C CG  . PRO   B 1 252 ? 0.968   8.927   45.371  1.00 95.75  ?  257 PRO   B CG  1 
ATOM   3973 C CD  . PRO   B 1 252 ? 0.295   8.414   46.604  1.00 93.28  ?  257 PRO   B CD  1 
ATOM   3974 N N   . ARG   B 1 253 ? -0.802  13.076  46.123  1.00 106.04 ?  258 ARG   B N   1 
ATOM   3975 C CA  . ARG   B 1 253 ? -1.824  14.142  45.975  1.00 109.58 ?  258 ARG   B CA  1 
ATOM   3976 C C   . ARG   B 1 253 ? -2.807  13.862  44.817  1.00 104.76 ?  258 ARG   B C   1 
ATOM   3977 O O   . ARG   B 1 253 ? -4.019  14.099  44.939  1.00 93.30  ?  258 ARG   B O   1 
ATOM   3978 C CB  . ARG   B 1 253 ? -1.155  15.514  45.760  1.00 112.69 ?  258 ARG   B CB  1 
ATOM   3979 C CG  . ARG   B 1 253 ? -0.301  16.016  46.921  1.00 114.32 ?  258 ARG   B CG  1 
ATOM   3980 C CD  . ARG   B 1 253 ? 0.421   17.292  46.501  0.00 122.15 ?  258 ARG   B CD  1 
ATOM   3981 N NE  . ARG   B 1 253 ? 1.309   17.787  47.549  0.00 127.21 ?  258 ARG   B NE  1 
ATOM   3982 C CZ  . ARG   B 1 253 ? 2.094   18.852  47.418  0.00 133.15 ?  258 ARG   B CZ  1 
ATOM   3983 N NH1 . ARG   B 1 253 ? 2.102   19.536  46.282  0.00 134.57 ?  258 ARG   B NH1 1 
ATOM   3984 N NH2 . ARG   B 1 253 ? 2.871   19.233  48.422  0.00 138.09 ?  258 ARG   B NH2 1 
ATOM   3985 N N   . GLU   B 1 254 ? -2.265  13.357  43.706  1.00 104.17 ?  259 GLU   B N   1 
ATOM   3986 C CA  . GLU   B 1 254 ? -3.051  12.998  42.510  1.00 104.06 ?  259 GLU   B CA  1 
ATOM   3987 C C   . GLU   B 1 254 ? -4.142  11.954  42.795  1.00 94.26  ?  259 GLU   B C   1 
ATOM   3988 O O   . GLU   B 1 254 ? -5.267  12.079  42.296  1.00 94.28  ?  259 GLU   B O   1 
ATOM   3989 C CB  . GLU   B 1 254 ? -2.141  12.497  41.369  1.00 107.08 ?  259 GLU   B CB  1 
ATOM   3990 C CG  . GLU   B 1 254 ? -1.438  13.592  40.566  1.00 115.80 ?  259 GLU   B CG  1 
ATOM   3991 C CD  . GLU   B 1 254 ? -0.125  14.040  41.181  1.00 122.52 ?  259 GLU   B CD  1 
ATOM   3992 O OE1 . GLU   B 1 254 ? 0.885   14.096  40.446  1.00 123.88 ?  259 GLU   B OE1 1 
ATOM   3993 O OE2 . GLU   B 1 254 ? -0.091  14.317  42.397  1.00 128.23 ?  259 GLU   B OE2 1 
ATOM   3994 N N   . ILE   B 1 255 ? -3.797  10.928  43.575  1.00 86.63  ?  260 ILE   B N   1 
ATOM   3995 C CA  . ILE   B 1 255 ? -4.753  9.872   43.978  1.00 88.15  ?  260 ILE   B CA  1 
ATOM   3996 C C   . ILE   B 1 255 ? -5.865  10.407  44.906  1.00 87.15  ?  260 ILE   B C   1 
ATOM   3997 O O   . ILE   B 1 255 ? -7.033  9.999   44.776  1.00 88.93  ?  260 ILE   B O   1 
ATOM   3998 C CB  . ILE   B 1 255 ? -4.032  8.639   44.600  1.00 87.92  ?  260 ILE   B CB  1 
ATOM   3999 C CG1 . ILE   B 1 255 ? -3.223  7.898   43.530  1.00 89.62  ?  260 ILE   B CG1 1 
ATOM   4000 C CG2 . ILE   B 1 255 ? -5.020  7.641   45.184  1.00 84.33  ?  260 ILE   B CG2 1 
ATOM   4001 C CD1 . ILE   B 1 255 ? -2.249  6.847   43.889  0.00 84.21  ?  260 ILE   B CD1 1 
ATOM   4002 N N   . ILE   B 1 256 ? -5.505  11.306  45.827  1.00 81.19  ?  261 ILE   B N   1 
ATOM   4003 C CA  . ILE   B 1 256 ? -6.479  11.982  46.691  1.00 80.53  ?  261 ILE   B CA  1 
ATOM   4004 C C   . ILE   B 1 256 ? -7.472  12.829  45.860  1.00 80.17  ?  261 ILE   B C   1 
ATOM   4005 O O   . ILE   B 1 256 ? -8.661  12.826  46.162  1.00 77.46  ?  261 ILE   B O   1 
ATOM   4006 C CB  . ILE   B 1 256 ? -5.779  12.823  47.809  1.00 86.78  ?  261 ILE   B CB  1 
ATOM   4007 C CG1 . ILE   B 1 256 ? -5.029  11.904  48.790  1.00 90.12  ?  261 ILE   B CG1 1 
ATOM   4008 C CG2 . ILE   B 1 256 ? -6.777  13.664  48.605  1.00 84.02  ?  261 ILE   B CG2 1 
ATOM   4009 C CD1 . ILE   B 1 256 ? -3.934  12.531  49.586  0.00 87.77  ?  261 ILE   B CD1 1 
ATOM   4010 N N   . SER   B 1 257 ? -6.979  13.529  44.833  1.00 83.24  ?  262 SER   B N   1 
ATOM   4011 C CA  . SER   B 1 257 ? -7.846  14.260  43.875  1.00 79.20  ?  262 SER   B CA  1 
ATOM   4012 C C   . SER   B 1 257 ? -8.775  13.346  43.079  1.00 72.19  ?  262 SER   B C   1 
ATOM   4013 O O   . SER   B 1 257 ? -9.946  13.686  42.847  1.00 72.04  ?  262 SER   B O   1 
ATOM   4014 C CB  . SER   B 1 257 ? -7.011  15.082  42.895  1.00 75.10  ?  262 SER   B CB  1 
ATOM   4015 O OG  . SER   B 1 257 ? -6.234  16.015  43.592  1.00 81.63  ?  262 SER   B OG  1 
ATOM   4016 N N   . LEU   B 1 258 ? -8.243  12.201  42.661  1.00 68.97  ?  263 LEU   B N   1 
ATOM   4017 C CA  . LEU   B 1 258 ? -8.998  11.237  41.862  1.00 74.53  ?  263 LEU   B CA  1 
ATOM   4018 C C   . LEU   B 1 258 ? -10.178 10.642  42.628  1.00 70.82  ?  263 LEU   B C   1 
ATOM   4019 O O   . LEU   B 1 258 ? -11.294 10.590  42.091  1.00 74.67  ?  263 LEU   B O   1 
ATOM   4020 C CB  . LEU   B 1 258 ? -8.084  10.113  41.346  1.00 71.68  ?  263 LEU   B CB  1 
ATOM   4021 C CG  . LEU   B 1 258 ? -8.656  9.144   40.312  1.00 72.07  ?  263 LEU   B CG  1 
ATOM   4022 C CD1 . LEU   B 1 258 ? -8.905  9.883   38.999  1.00 75.92  ?  263 LEU   B CD1 1 
ATOM   4023 C CD2 . LEU   B 1 258 ? -7.714  7.958   40.097  1.00 69.15  ?  263 LEU   B CD2 1 
ATOM   4024 N N   . MET   B 1 259 ? -9.935  10.204  43.867  1.00 68.00  ?  264 MET   B N   1 
ATOM   4025 C CA  . MET   B 1 259 ? -11.019 9.657   44.706  1.00 68.54  ?  264 MET   B CA  1 
ATOM   4026 C C   . MET   B 1 259 ? -12.053 10.734  45.038  1.00 66.26  ?  264 MET   B C   1 
ATOM   4027 O O   . MET   B 1 259 ? -13.249 10.468  44.953  1.00 65.68  ?  264 MET   B O   1 
ATOM   4028 C CB  . MET   B 1 259 ? -10.502 8.920   45.967  1.00 65.65  ?  264 MET   B CB  1 
ATOM   4029 C CG  . MET   B 1 259 ? -9.864  9.780   47.047  1.00 73.61  ?  264 MET   B CG  1 
ATOM   4030 S SD  . MET   B 1 259 ? -9.198  8.830   48.428  1.00 75.81  ?  264 MET   B SD  1 
ATOM   4031 C CE  . MET   B 1 259 ? -7.718  8.098   47.730  1.00 74.18  ?  264 MET   B CE  1 
ATOM   4032 N N   . LYS   B 1 260 ? -11.583 11.943  45.368  1.00 71.05  ?  265 LYS   B N   1 
ATOM   4033 C CA  . LYS   B 1 260 ? -12.463 13.114  45.585  1.00 72.70  ?  265 LYS   B CA  1 
ATOM   4034 C C   . LYS   B 1 260 ? -13.347 13.432  44.376  1.00 70.22  ?  265 LYS   B C   1 
ATOM   4035 O O   . LYS   B 1 260 ? -14.527 13.757  44.538  1.00 68.25  ?  265 LYS   B O   1 
ATOM   4036 C CB  . LYS   B 1 260 ? -11.663 14.371  46.011  1.00 75.07  ?  265 LYS   B CB  1 
ATOM   4037 C CG  . LYS   B 1 260 ? -11.311 14.424  47.490  1.00 77.84  ?  265 LYS   B CG  1 
ATOM   4038 C CD  . LYS   B 1 260 ? -10.782 15.799  47.909  1.00 78.38  ?  265 LYS   B CD  1 
ATOM   4039 C CE  . LYS   B 1 260 ? -10.139 15.701  49.304  0.00 79.97  ?  265 LYS   B CE  1 
ATOM   4040 N NZ  . LYS   B 1 260 ? -9.351  16.918  49.644  0.00 84.44  ?  265 LYS   B NZ  1 
ATOM   4041 N N   . LEU   B 1 261 ? -12.771 13.321  43.179  1.00 74.31  ?  266 LEU   B N   1 
ATOM   4042 C CA  . LEU   B 1 261 ? -13.516 13.484  41.930  1.00 77.59  ?  266 LEU   B CA  1 
ATOM   4043 C C   . LEU   B 1 261 ? -14.538 12.361  41.714  1.00 74.09  ?  266 LEU   B C   1 
ATOM   4044 O O   . LEU   B 1 261 ? -15.707 12.630  41.435  1.00 75.54  ?  266 LEU   B O   1 
ATOM   4045 C CB  . LEU   B 1 261 ? -12.549 13.537  40.751  1.00 79.22  ?  266 LEU   B CB  1 
ATOM   4046 C CG  . LEU   B 1 261 ? -13.090 13.989  39.398  1.00 88.37  ?  266 LEU   B CG  1 
ATOM   4047 C CD1 . LEU   B 1 261 ? -13.524 15.455  39.402  1.00 94.29  ?  266 LEU   B CD1 1 
ATOM   4048 C CD2 . LEU   B 1 261 ? -12.014 13.769  38.338  1.00 88.97  ?  266 LEU   B CD2 1 
ATOM   4049 N N   . CYS   B 1 262 ? -14.080 11.119  41.856  1.00 70.49  ?  267 CYS   B N   1 
ATOM   4050 C CA  . CYS   B 1 262 ? -14.927 9.939   41.654  1.00 68.40  ?  267 CYS   B CA  1 
ATOM   4051 C C   . CYS   B 1 262 ? -16.031 9.709   42.702  1.00 66.57  ?  267 CYS   B C   1 
ATOM   4052 O O   . CYS   B 1 262 ? -16.973 8.971   42.405  1.00 59.61  ?  267 CYS   B O   1 
ATOM   4053 C CB  . CYS   B 1 262 ? -14.065 8.674   41.547  1.00 67.17  ?  267 CYS   B CB  1 
ATOM   4054 S SG  . CYS   B 1 262 ? -13.063 8.593   40.068  1.00 76.56  ?  267 CYS   B SG  1 
ATOM   4055 N N   . TRP   B 1 263 ? -15.915 10.282  43.909  1.00 63.92  ?  268 TRP   B N   1 
ATOM   4056 C CA  . TRP   B 1 263 ? -17.023 10.223  44.899  1.00 64.95  ?  268 TRP   B CA  1 
ATOM   4057 C C   . TRP   B 1 263 ? -17.933 11.459  45.005  1.00 65.00  ?  268 TRP   B C   1 
ATOM   4058 O O   . TRP   B 1 263 ? -18.627 11.634  46.028  1.00 61.15  ?  268 TRP   B O   1 
ATOM   4059 C CB  . TRP   B 1 263 ? -16.539 9.739   46.280  1.00 64.02  ?  268 TRP   B CB  1 
ATOM   4060 C CG  . TRP   B 1 263 ? -15.648 10.594  47.124  1.00 62.48  ?  268 TRP   B CG  1 
ATOM   4061 C CD1 . TRP   B 1 263 ? -15.722 11.937  47.356  1.00 67.50  ?  268 TRP   B CD1 1 
ATOM   4062 C CD2 . TRP   B 1 263 ? -14.614 10.103  47.972  1.00 65.86  ?  268 TRP   B CD2 1 
ATOM   4063 N NE1 . TRP   B 1 263 ? -14.760 12.319  48.254  1.00 70.00  ?  268 TRP   B NE1 1 
ATOM   4064 C CE2 . TRP   B 1 263 ? -14.057 11.216  48.645  1.00 65.45  ?  268 TRP   B CE2 1 
ATOM   4065 C CE3 . TRP   B 1 263 ? -14.065 8.827   48.192  1.00 61.59  ?  268 TRP   B CE3 1 
ATOM   4066 C CZ2 . TRP   B 1 263 ? -12.981 11.097  49.539  1.00 66.83  ?  268 TRP   B CZ2 1 
ATOM   4067 C CZ3 . TRP   B 1 263 ? -12.993 8.705   49.074  1.00 63.86  ?  268 TRP   B CZ3 1 
ATOM   4068 C CH2 . TRP   B 1 263 ? -12.460 9.837   49.740  1.00 63.68  ?  268 TRP   B CH2 1 
ATOM   4069 N N   . GLU   B 1 264 ? -17.937 12.298  43.964  1.00 68.17  ?  269 GLU   B N   1 
ATOM   4070 C CA  . GLU   B 1 264 ? -18.834 13.463  43.883  1.00 77.31  ?  269 GLU   B CA  1 
ATOM   4071 C C   . GLU   B 1 264 ? -20.300 13.078  44.103  1.00 74.90  ?  269 GLU   B C   1 
ATOM   4072 O O   . GLU   B 1 264 ? -20.737 12.015  43.649  1.00 73.65  ?  269 GLU   B O   1 
ATOM   4073 C CB  . GLU   B 1 264 ? -18.684 14.163  42.518  1.00 84.53  ?  269 GLU   B CB  1 
ATOM   4074 C CG  . GLU   B 1 264 ? -17.476 15.090  42.435  1.00 88.84  ?  269 GLU   B CG  1 
ATOM   4075 C CD  . GLU   B 1 264 ? -17.692 16.474  43.054  1.00 89.72  ?  269 GLU   B CD  1 
ATOM   4076 O OE1 . GLU   B 1 264 ? -18.798 16.808  43.550  1.00 83.95  ?  269 GLU   B OE1 1 
ATOM   4077 O OE2 . GLU   B 1 264 ? -16.720 17.256  43.034  1.00 88.93  ?  269 GLU   B OE2 1 
ATOM   4078 N N   . ALA   B 1 265 ? -21.030 13.928  44.825  1.00 74.69  ?  270 ALA   B N   1 
ATOM   4079 C CA  . ALA   B 1 265 ? -22.463 13.727  45.074  1.00 78.32  ?  270 ALA   B CA  1 
ATOM   4080 C C   . ALA   B 1 265 ? -23.238 13.607  43.763  1.00 81.00  ?  270 ALA   B C   1 
ATOM   4081 O O   . ALA   B 1 265 ? -24.015 12.663  43.583  1.00 78.77  ?  270 ALA   B O   1 
ATOM   4082 C CB  . ALA   B 1 265 ? -23.026 14.871  45.910  1.00 81.37  ?  270 ALA   B CB  1 
ATOM   4083 N N   . ASN   B 1 266 ? -22.984 14.552  42.854  1.00 85.16  ?  271 ASN   B N   1 
ATOM   4084 C CA  . ASN   B 1 266 ? -23.615 14.567  41.531  1.00 90.24  ?  271 ASN   B CA  1 
ATOM   4085 C C   . ASN   B 1 266 ? -22.923 13.526  40.640  1.00 88.02  ?  271 ASN   B C   1 
ATOM   4086 O O   . ASN   B 1 266 ? -21.707 13.631  40.450  1.00 89.52  ?  271 ASN   B O   1 
ATOM   4087 C CB  . ASN   B 1 266 ? -23.518 15.961  40.899  1.00 95.17  ?  271 ASN   B CB  1 
ATOM   4088 C CG  . ASN   B 1 266 ? -24.350 16.108  39.627  1.00 103.21 ?  271 ASN   B CG  1 
ATOM   4089 O OD1 . ASN   B 1 266 ? -25.184 15.259  39.293  1.00 97.76  ?  271 ASN   B OD1 1 
ATOM   4090 N ND2 . ASN   B 1 266 ? -24.120 17.202  38.909  1.00 117.71 ?  271 ASN   B ND2 1 
ATOM   4091 N N   . PRO   B 1 267 ? -23.674 12.527  40.104  1.00 86.56  ?  272 PRO   B N   1 
ATOM   4092 C CA  . PRO   B 1 267 ? -23.047 11.518  39.219  1.00 83.68  ?  272 PRO   B CA  1 
ATOM   4093 C C   . PRO   B 1 267 ? -22.407 12.057  37.932  1.00 89.90  ?  272 PRO   B C   1 
ATOM   4094 O O   . PRO   B 1 267 ? -21.382 11.508  37.488  1.00 90.22  ?  272 PRO   B O   1 
ATOM   4095 C CB  . PRO   B 1 267 ? -24.211 10.581  38.875  1.00 86.59  ?  272 PRO   B CB  1 
ATOM   4096 C CG  . PRO   B 1 267 ? -25.157 10.739  40.001  1.00 89.16  ?  272 PRO   B CG  1 
ATOM   4097 C CD  . PRO   B 1 267 ? -25.087 12.182  40.366  1.00 88.33  ?  272 PRO   B CD  1 
ATOM   4098 N N   . GLU   B 1 268 ? -23.007 13.099  37.344  1.00 90.77  ?  273 GLU   B N   1 
ATOM   4099 C CA  . GLU   B 1 268 ? -22.448 13.784  36.159  1.00 89.57  ?  273 GLU   B CA  1 
ATOM   4100 C C   . GLU   B 1 268 ? -21.047 14.397  36.370  1.00 83.99  ?  273 GLU   B C   1 
ATOM   4101 O O   . GLU   B 1 268 ? -20.260 14.470  35.423  1.00 84.42  ?  273 GLU   B O   1 
ATOM   4102 C CB  . GLU   B 1 268 ? -23.429 14.838  35.629  1.00 98.33  ?  273 GLU   B CB  1 
ATOM   4103 C CG  . GLU   B 1 268 ? -24.640 14.235  34.925  1.00 98.96  ?  273 GLU   B CG  1 
ATOM   4104 C CD  . GLU   B 1 268 ? -24.313 13.937  33.398  0.00 102.48 ?  273 GLU   B CD  1 
ATOM   4105 O OE1 . GLU   B 1 268 ? -25.273 14.007  32.601  0.00 106.22 ?  273 GLU   B OE1 1 
ATOM   4106 O OE2 . GLU   B 1 268 ? -23.155 13.646  33.020  0.00 100.03 ?  273 GLU   B OE2 1 
ATOM   4107 N N   . ALA   B 1 269 ? -20.748 14.835  37.593  1.00 80.66  ?  274 ALA   B N   1 
ATOM   4108 C CA  . ALA   B 1 269 ? -19.387 15.290  37.961  1.00 80.12  ?  274 ALA   B CA  1 
ATOM   4109 C C   . ALA   B 1 269 ? -18.312 14.185  37.950  1.00 76.37  ?  274 ALA   B C   1 
ATOM   4110 O O   . ALA   B 1 269 ? -17.129 14.479  37.755  1.00 74.13  ?  274 ALA   B O   1 
ATOM   4111 C CB  . ALA   B 1 269 ? -19.401 15.975  39.322  1.00 82.62  ?  274 ALA   B CB  1 
ATOM   4112 N N   . ARG   B 1 270 ? -18.708 12.933  38.191  1.00 76.36  ?  275 ARG   B N   1 
ATOM   4113 C CA  . ARG   B 1 270 ? -17.761 11.802  38.231  1.00 71.92  ?  275 ARG   B CA  1 
ATOM   4114 C C   . ARG   B 1 270 ? -17.333 11.417  36.811  1.00 68.21  ?  275 ARG   B C   1 
ATOM   4115 O O   . ARG   B 1 270 ? -18.163 11.438  35.904  1.00 71.06  ?  275 ARG   B O   1 
ATOM   4116 C CB  . ARG   B 1 270 ? -18.361 10.561  38.894  1.00 71.56  ?  275 ARG   B CB  1 
ATOM   4117 C CG  . ARG   B 1 270 ? -18.865 10.738  40.325  1.00 70.24  ?  275 ARG   B CG  1 
ATOM   4118 C CD  . ARG   B 1 270 ? -19.713 9.544   40.773  1.00 67.94  ?  275 ARG   B CD  1 
ATOM   4119 N NE  . ARG   B 1 270 ? -20.643 9.928   41.834  1.00 68.53  ?  275 ARG   B NE  1 
ATOM   4120 C CZ  . ARG   B 1 270 ? -21.810 9.335   42.121  1.00 69.23  ?  275 ARG   B CZ  1 
ATOM   4121 N NH1 . ARG   B 1 270 ? -22.250 8.270   41.445  1.00 67.05  ?  275 ARG   B NH1 1 
ATOM   4122 N NH2 . ARG   B 1 270 ? -22.566 9.827   43.111  1.00 74.13  ?  275 ARG   B NH2 1 
ATOM   4123 N N   . PRO   B 1 271 ? -16.057 11.023  36.620  1.00 62.72  ?  276 PRO   B N   1 
ATOM   4124 C CA  . PRO   B 1 271 ? -15.599 10.624  35.296  1.00 60.84  ?  276 PRO   B CA  1 
ATOM   4125 C C   . PRO   B 1 271 ? -16.010 9.201   34.929  1.00 58.78  ?  276 PRO   B C   1 
ATOM   4126 O O   . PRO   B 1 271 ? -16.621 8.511   35.717  1.00 64.62  ?  276 PRO   B O   1 
ATOM   4127 C CB  . PRO   B 1 271 ? -14.080 10.743  35.420  1.00 61.94  ?  276 PRO   B CB  1 
ATOM   4128 C CG  . PRO   B 1 271 ? -13.805 10.392  36.830  1.00 61.04  ?  276 PRO   B CG  1 
ATOM   4129 C CD  . PRO   B 1 271 ? -15.012 10.776  37.632  1.00 61.36  ?  276 PRO   B CD  1 
ATOM   4130 N N   . THR   B 1 272 ? -15.677 8.800   33.711  1.00 62.25  ?  277 THR   B N   1 
ATOM   4131 C CA  . THR   B 1 272 ? -15.823 7.435   33.220  1.00 60.61  ?  277 THR   B CA  1 
ATOM   4132 C C   . THR   B 1 272 ? -14.507 6.724   33.459  1.00 62.86  ?  277 THR   B C   1 
ATOM   4133 O O   . THR   B 1 272 ? -13.469 7.382   33.576  1.00 65.90  ?  277 THR   B O   1 
ATOM   4134 C CB  . THR   B 1 272 ? -16.117 7.424   31.714  1.00 61.97  ?  277 THR   B CB  1 
ATOM   4135 O OG1 . THR   B 1 272 ? -15.055 8.074   31.013  1.00 65.98  ?  277 THR   B OG1 1 
ATOM   4136 C CG2 . THR   B 1 272 ? -17.416 8.139   31.412  1.00 67.27  ?  277 THR   B CG2 1 
ATOM   4137 N N   . PHE   B 1 273 ? -14.545 5.391   33.496  1.00 60.66  ?  278 PHE   B N   1 
ATOM   4138 C CA  . PHE   B 1 273 ? -13.318 4.591   33.652  1.00 59.58  ?  278 PHE   B CA  1 
ATOM   4139 C C   . PHE   B 1 273 ? -12.259 4.810   32.555  1.00 59.23  ?  278 PHE   B C   1 
ATOM   4140 O O   . PHE   B 1 273 ? -11.071 4.930   32.880  1.00 63.84  ?  278 PHE   B O   1 
ATOM   4141 C CB  . PHE   B 1 273 ? -13.634 3.095   33.857  1.00 61.57  ?  278 PHE   B CB  1 
ATOM   4142 C CG  . PHE   B 1 273 ? -14.151 2.770   35.242  1.00 55.53  ?  278 PHE   B CG  1 
ATOM   4143 C CD1 . PHE   B 1 273 ? -13.287 2.773   36.332  1.00 51.78  ?  278 PHE   B CD1 1 
ATOM   4144 C CD2 . PHE   B 1 273 ? -15.504 2.474   35.462  1.00 57.38  ?  278 PHE   B CD2 1 
ATOM   4145 C CE1 . PHE   B 1 273 ? -13.748 2.487   37.605  1.00 53.56  ?  278 PHE   B CE1 1 
ATOM   4146 C CE2 . PHE   B 1 273 ? -15.966 2.187   36.744  1.00 57.97  ?  278 PHE   B CE2 1 
ATOM   4147 C CZ  . PHE   B 1 273 ? -15.085 2.186   37.815  1.00 54.47  ?  278 PHE   B CZ  1 
ATOM   4148 N N   . PRO   B 1 274 ? -12.675 4.900   31.275  1.00 62.79  ?  279 PRO   B N   1 
ATOM   4149 C CA  . PRO   B 1 274 ? -11.756 5.398   30.231  1.00 65.84  ?  279 PRO   B CA  1 
ATOM   4150 C C   . PRO   B 1 274 ? -11.158 6.777   30.538  1.00 67.52  ?  279 PRO   B C   1 
ATOM   4151 O O   . PRO   B 1 274 ? -9.970  6.989   30.301  1.00 70.95  ?  279 PRO   B O   1 
ATOM   4152 C CB  . PRO   B 1 274 ? -12.646 5.450   28.995  1.00 65.36  ?  279 PRO   B CB  1 
ATOM   4153 C CG  . PRO   B 1 274 ? -13.588 4.314   29.198  1.00 63.72  ?  279 PRO   B CG  1 
ATOM   4154 C CD  . PRO   B 1 274 ? -13.886 4.307   30.672  1.00 64.44  ?  279 PRO   B CD  1 
ATOM   4155 N N   . GLY   B 1 275 ? -11.988 7.684   31.058  1.00 69.22  ?  280 GLY   B N   1 
ATOM   4156 C CA  . GLY   B 1 275 ? -11.538 8.972   31.602  1.00 71.64  ?  280 GLY   B CA  1 
ATOM   4157 C C   . GLY   B 1 275 ? -10.511 8.838   32.715  1.00 70.30  ?  280 GLY   B C   1 
ATOM   4158 O O   . GLY   B 1 275 ? -9.485  9.521   32.702  1.00 76.31  ?  280 GLY   B O   1 
ATOM   4159 N N   . ILE   B 1 276 ? -10.778 7.933   33.657  1.00 69.04  ?  281 ILE   B N   1 
ATOM   4160 C CA  . ILE   B 1 276 ? -9.847  7.631   34.769  1.00 69.37  ?  281 ILE   B CA  1 
ATOM   4161 C C   . ILE   B 1 276 ? -8.527  7.034   34.244  1.00 70.71  ?  281 ILE   B C   1 
ATOM   4162 O O   . ILE   B 1 276 ? -7.446  7.470   34.661  1.00 72.58  ?  281 ILE   B O   1 
ATOM   4163 C CB  . ILE   B 1 276 ? -10.492 6.709   35.849  1.00 68.00  ?  281 ILE   B CB  1 
ATOM   4164 C CG1 . ILE   B 1 276 ? -11.677 7.417   36.524  1.00 67.18  ?  281 ILE   B CG1 1 
ATOM   4165 C CG2 . ILE   B 1 276 ? -9.490  6.335   36.946  1.00 71.51  ?  281 ILE   B CG2 1 
ATOM   4166 C CD1 . ILE   B 1 276 ? -12.646 6.501   37.241  1.00 66.85  ?  281 ILE   B CD1 1 
ATOM   4167 N N   . GLU   B 1 277 ? -8.633  6.059   33.334  1.00 70.81  ?  282 GLU   B N   1 
ATOM   4168 C CA  . GLU   B 1 277 ? -7.478  5.366   32.744  1.00 68.00  ?  282 GLU   B CA  1 
ATOM   4169 C C   . GLU   B 1 277 ? -6.499  6.302   32.027  1.00 69.08  ?  282 GLU   B C   1 
ATOM   4170 O O   . GLU   B 1 277 ? -5.300  6.134   32.182  1.00 68.33  ?  282 GLU   B O   1 
ATOM   4171 C CB  . GLU   B 1 277 ? -7.938  4.281   31.771  1.00 71.03  ?  282 GLU   B CB  1 
ATOM   4172 C CG  . GLU   B 1 277 ? -6.863  3.271   31.392  1.00 78.84  ?  282 GLU   B CG  1 
ATOM   4173 C CD  . GLU   B 1 277 ? -7.312  2.306   30.301  1.00 92.61  ?  282 GLU   B CD  1 
ATOM   4174 O OE1 . GLU   B 1 277 ? -6.432  1.762   29.600  1.00 110.16 ?  282 GLU   B OE1 1 
ATOM   4175 O OE2 . GLU   B 1 277 ? -8.534  2.083   30.130  1.00 100.37 ?  282 GLU   B OE2 1 
ATOM   4176 N N   . GLU   B 1 278 ? -7.023  7.257   31.254  1.00 78.95  ?  283 GLU   B N   1 
ATOM   4177 C CA  . GLU   B 1 278 ? -6.195  8.250   30.525  1.00 85.05  ?  283 GLU   B CA  1 
ATOM   4178 C C   . GLU   B 1 278 ? -5.386  9.160   31.463  1.00 88.67  ?  283 GLU   B C   1 
ATOM   4179 O O   . GLU   B 1 278 ? -4.263  9.552   31.126  1.00 90.38  ?  283 GLU   B O   1 
ATOM   4180 C CB  . GLU   B 1 278 ? -7.045  9.098   29.566  1.00 83.30  ?  283 GLU   B CB  1 
ATOM   4181 C CG  . GLU   B 1 278 ? -8.152  9.838   29.846  0.00 84.38  ?  283 GLU   B CG  1 
ATOM   4182 C CD  . GLU   B 1 278 ? -8.803  10.577  28.682  0.00 87.22  ?  283 GLU   B CD  1 
ATOM   4183 O OE1 . GLU   B 1 278 ? -8.907  10.011  27.569  0.00 87.56  ?  283 GLU   B OE1 1 
ATOM   4184 O OE2 . GLU   B 1 278 ? -9.233  11.734  28.888  0.00 88.97  ?  283 GLU   B OE2 1 
ATOM   4185 N N   . LYS   B 1 279 ? -5.948  9.484   32.634  1.00 89.56  ?  284 LYS   B N   1 
ATOM   4186 C CA  . LYS   B 1 279 ? -5.248  10.251  33.687  1.00 87.13  ?  284 LYS   B CA  1 
ATOM   4187 C C   . LYS   B 1 279 ? -4.296  9.363   34.506  1.00 74.76  ?  284 LYS   B C   1 
ATOM   4188 O O   . LYS   B 1 279 ? -3.131  9.710   34.684  1.00 74.65  ?  284 LYS   B O   1 
ATOM   4189 C CB  . LYS   B 1 279 ? -6.244  10.971  34.617  1.00 78.76  ?  284 LYS   B CB  1 
ATOM   4190 C CG  . LYS   B 1 279 ? -7.403  11.724  34.104  0.00 82.30  ?  284 LYS   B CG  1 
ATOM   4191 C CD  . LYS   B 1 279 ? -8.330  12.267  35.193  0.00 81.40  ?  284 LYS   B CD  1 
ATOM   4192 C CE  . LYS   B 1 279 ? -9.800  12.118  34.824  0.00 80.10  ?  284 LYS   B CE  1 
ATOM   4193 N NZ  . LYS   B 1 279 ? -10.155 12.805  33.552  0.00 82.86  ?  284 LYS   B NZ  1 
ATOM   4194 N N   . PHE   B 1 280 ? -4.786  8.214   34.955  1.00 63.83  ?  285 PHE   B N   1 
ATOM   4195 C CA  . PHE   B 1 280 ? -4.043  7.394   35.916  1.00 63.74  ?  285 PHE   B CA  1 
ATOM   4196 C C   . PHE   B 1 280 ? -2.862  6.617   35.319  1.00 68.68  ?  285 PHE   B C   1 
ATOM   4197 O O   . PHE   B 1 280 ? -1.846  6.436   35.998  1.00 83.75  ?  285 PHE   B O   1 
ATOM   4198 C CB  . PHE   B 1 280 ? -4.997  6.463   36.667  1.00 61.19  ?  285 PHE   B CB  1 
ATOM   4199 C CG  . PHE   B 1 280 ? -4.370  5.786   37.851  1.00 62.26  ?  285 PHE   B CG  1 
ATOM   4200 C CD1 . PHE   B 1 280 ? -4.233  6.453   39.068  1.00 63.81  ?  285 PHE   B CD1 1 
ATOM   4201 C CD2 . PHE   B 1 280 ? -3.885  4.480   37.744  1.00 64.35  ?  285 PHE   B CD2 1 
ATOM   4202 C CE1 . PHE   B 1 280 ? -3.633  5.822   40.161  1.00 67.38  ?  285 PHE   B CE1 1 
ATOM   4203 C CE2 . PHE   B 1 280 ? -3.294  3.847   38.834  1.00 63.98  ?  285 PHE   B CE2 1 
ATOM   4204 C CZ  . PHE   B 1 280 ? -3.170  4.511   40.048  1.00 62.83  ?  285 PHE   B CZ  1 
ATOM   4205 N N   . ARG   B 1 281 ? -2.993  6.113   34.092  1.00 67.13  ?  286 ARG   B N   1 
ATOM   4206 C CA  . ARG   B 1 281 ? -1.930  5.314   33.467  1.00 65.01  ?  286 ARG   B CA  1 
ATOM   4207 C C   . ARG   B 1 281 ? -0.579  6.047   33.349  1.00 68.18  ?  286 ARG   B C   1 
ATOM   4208 O O   . ARG   B 1 281 ? 0.436   5.481   33.766  1.00 69.13  ?  286 ARG   B O   1 
ATOM   4209 C CB  . ARG   B 1 281 ? -2.372  4.732   32.113  1.00 65.03  ?  286 ARG   B CB  1 
ATOM   4210 C CG  . ARG   B 1 281 ? -1.458  3.627   31.620  1.00 65.61  ?  286 ARG   B CG  1 
ATOM   4211 C CD  . ARG   B 1 281 ? -1.860  3.070   30.268  1.00 66.27  ?  286 ARG   B CD  1 
ATOM   4212 N NE  . ARG   B 1 281 ? -1.801  1.616   30.352  1.00 65.31  ?  286 ARG   B NE  1 
ATOM   4213 C CZ  . ARG   B 1 281 ? -2.808  0.804   30.674  1.00 58.09  ?  286 ARG   B CZ  1 
ATOM   4214 N NH1 . ARG   B 1 281 ? -4.060  1.231   30.838  1.00 59.39  ?  286 ARG   B NH1 1 
ATOM   4215 N NH2 . ARG   B 1 281 ? -2.553  -0.497  30.774  1.00 59.83  ?  286 ARG   B NH2 1 
ATOM   4216 N N   . PRO   B 1 282 ? -0.556  7.295   32.805  1.00 74.94  ?  287 PRO   B N   1 
ATOM   4217 C CA  . PRO   B 1 282 ? 0.721   8.048   32.798  1.00 78.63  ?  287 PRO   B CA  1 
ATOM   4218 C C   . PRO   B 1 282 ? 1.287   8.362   34.194  1.00 77.27  ?  287 PRO   B C   1 
ATOM   4219 O O   . PRO   B 1 282 ? 2.508   8.375   34.357  1.00 82.71  ?  287 PRO   B O   1 
ATOM   4220 C CB  . PRO   B 1 282 ? 0.386   9.349   32.037  1.00 79.50  ?  287 PRO   B CB  1 
ATOM   4221 C CG  . PRO   B 1 282 ? -0.936  9.134   31.396  1.00 75.74  ?  287 PRO   B CG  1 
ATOM   4222 C CD  . PRO   B 1 282 ? -1.641  8.072   32.169  1.00 72.09  ?  287 PRO   B CD  1 
ATOM   4223 N N   . PHE   B 1 283 ? 0.403   8.598   35.167  1.00 72.36  ?  288 PHE   B N   1 
ATOM   4224 C CA  . PHE   B 1 283 ? 0.797   8.768   36.562  1.00 74.41  ?  288 PHE   B CA  1 
ATOM   4225 C C   . PHE   B 1 283 ? 1.444   7.509   37.146  1.00 71.89  ?  288 PHE   B C   1 
ATOM   4226 O O   . PHE   B 1 283 ? 2.495   7.588   37.798  1.00 79.73  ?  288 PHE   B O   1 
ATOM   4227 C CB  . PHE   B 1 283 ? -0.402  9.196   37.414  1.00 77.05  ?  288 PHE   B CB  1 
ATOM   4228 C CG  . PHE   B 1 283 ? -0.053  9.440   38.847  1.00 87.47  ?  288 PHE   B CG  1 
ATOM   4229 C CD1 . PHE   B 1 283 ? 0.650   10.592  39.205  1.00 95.84  ?  288 PHE   B CD1 1 
ATOM   4230 C CD2 . PHE   B 1 283 ? -0.393  8.514   39.848  1.00 86.07  ?  288 PHE   B CD2 1 
ATOM   4231 C CE1 . PHE   B 1 283 ? 0.982   10.834  40.535  1.00 103.28 ?  288 PHE   B CE1 1 
ATOM   4232 C CE2 . PHE   B 1 283 ? -0.039  8.744   41.173  1.00 89.29  ?  288 PHE   B CE2 1 
ATOM   4233 C CZ  . PHE   B 1 283 ? 0.650   9.903   41.516  1.00 96.75  ?  288 PHE   B CZ  1 
ATOM   4234 N N   . TYR   B 1 284 ? 0.804   6.362   36.932  1.00 67.53  ?  289 TYR   B N   1 
ATOM   4235 C CA  . TYR   B 1 284 ? 1.365   5.066   37.340  1.00 69.29  ?  289 TYR   B CA  1 
ATOM   4236 C C   . TYR   B 1 284 ? 2.768   4.825   36.745  1.00 78.34  ?  289 TYR   B C   1 
ATOM   4237 O O   . TYR   B 1 284 ? 3.672   4.383   37.455  1.00 82.85  ?  289 TYR   B O   1 
ATOM   4238 C CB  . TYR   B 1 284 ? 0.404   3.916   36.985  1.00 67.50  ?  289 TYR   B CB  1 
ATOM   4239 C CG  . TYR   B 1 284 ? 1.011   2.544   37.175  1.00 70.24  ?  289 TYR   B CG  1 
ATOM   4240 C CD1 . TYR   B 1 284 ? 1.256   2.041   38.453  1.00 71.10  ?  289 TYR   B CD1 1 
ATOM   4241 C CD2 . TYR   B 1 284 ? 1.377   1.754   36.071  1.00 74.69  ?  289 TYR   B CD2 1 
ATOM   4242 C CE1 . TYR   B 1 284 ? 1.847   0.793   38.634  1.00 76.80  ?  289 TYR   B CE1 1 
ATOM   4243 C CE2 . TYR   B 1 284 ? 1.964   0.504   36.243  1.00 75.65  ?  289 TYR   B CE2 1 
ATOM   4244 C CZ  . TYR   B 1 284 ? 2.196   0.022   37.526  1.00 76.49  ?  289 TYR   B CZ  1 
ATOM   4245 O OH  . TYR   B 1 284 ? 2.780   -1.214  37.705  1.00 79.34  ?  289 TYR   B OH  1 
ATOM   4246 N N   . LEU   B 1 285 ? 2.934   5.149   35.462  1.00 84.66  ?  290 LEU   B N   1 
ATOM   4247 C CA  . LEU   B 1 285 ? 4.202   4.958   34.751  1.00 93.50  ?  290 LEU   B CA  1 
ATOM   4248 C C   . LEU   B 1 285 ? 5.328   5.877   35.228  1.00 99.74  ?  290 LEU   B C   1 
ATOM   4249 O O   . LEU   B 1 285 ? 6.457   5.418   35.443  1.00 99.58  ?  290 LEU   B O   1 
ATOM   4250 C CB  . LEU   B 1 285 ? 4.001   5.123   33.234  1.00 98.55  ?  290 LEU   B CB  1 
ATOM   4251 C CG  . LEU   B 1 285 ? 3.239   3.999   32.525  1.00 95.58  ?  290 LEU   B CG  1 
ATOM   4252 C CD1 . LEU   B 1 285 ? 2.806   4.443   31.132  1.00 96.20  ?  290 LEU   B CD1 1 
ATOM   4253 C CD2 . LEU   B 1 285 ? 4.105   2.742   32.433  1.00 96.16  ?  290 LEU   B CD2 1 
ATOM   4254 N N   . SER   B 1 286 ? 5.019   7.164   35.372  1.00 101.78 ?  291 SER   B N   1 
ATOM   4255 C CA  . SER   B 1 286 ? 6.007   8.166   35.806  1.00 104.07 ?  291 SER   B CA  1 
ATOM   4256 C C   . SER   B 1 286 ? 6.386   8.012   37.281  1.00 102.67 ?  291 SER   B C   1 
ATOM   4257 O O   . SER   B 1 286 ? 7.580   8.008   37.602  1.00 102.86 ?  291 SER   B O   1 
ATOM   4258 C CB  . SER   B 1 286 ? 5.517   9.595   35.533  1.00 103.22 ?  291 SER   B CB  1 
ATOM   4259 O OG  . SER   B 1 286 ? 4.287   9.860   36.180  1.00 98.35  ?  291 SER   B OG  1 
ATOM   4260 N N   . GLN   B 1 287 ? 5.380   7.867   38.160  1.00 95.32  ?  292 GLN   B N   1 
ATOM   4261 C CA  . GLN   B 1 287 ? 5.577   7.867   39.623  1.00 94.89  ?  292 GLN   B CA  1 
ATOM   4262 C C   . GLN   B 1 287 ? 5.673   6.487   40.278  1.00 90.71  ?  292 GLN   B C   1 
ATOM   4263 O O   . GLN   B 1 287 ? 6.631   6.208   40.985  1.00 91.79  ?  292 GLN   B O   1 
ATOM   4264 C CB  . GLN   B 1 287 ? 4.447   8.641   40.320  1.00 91.94  ?  292 GLN   B CB  1 
ATOM   4265 C CG  . GLN   B 1 287 ? 4.202   10.079  39.889  1.00 92.37  ?  292 GLN   B CG  1 
ATOM   4266 C CD  . GLN   B 1 287 ? 5.406   10.979  40.029  1.00 96.89  ?  292 GLN   B CD  1 
ATOM   4267 O OE1 . GLN   B 1 287 ? 5.571   11.668  41.036  1.00 98.88  ?  292 GLN   B OE1 1 
ATOM   4268 N NE2 . GLN   B 1 287 ? 6.263   10.969  39.023  1.00 100.39 ?  292 GLN   B NE2 1 
ATOM   4269 N N   . LEU   B 1 288 ? 4.682   5.639   40.042  1.00 90.28  ?  293 LEU   B N   1 
ATOM   4270 C CA  . LEU   B 1 288 ? 4.439   4.477   40.921  1.00 95.07  ?  293 LEU   B CA  1 
ATOM   4271 C C   . LEU   B 1 288 ? 5.271   3.218   40.619  1.00 105.22 ?  293 LEU   B C   1 
ATOM   4272 O O   . LEU   B 1 288 ? 5.738   2.570   41.553  1.00 118.24 ?  293 LEU   B O   1 
ATOM   4273 C CB  . LEU   B 1 288 ? 2.942   4.163   40.965  1.00 85.10  ?  293 LEU   B CB  1 
ATOM   4274 C CG  . LEU   B 1 288 ? 2.010   5.342   41.309  1.00 86.39  ?  293 LEU   B CG  1 
ATOM   4275 C CD1 . LEU   B 1 288 ? 0.568   4.863   41.393  1.00 81.47  ?  293 LEU   B CD1 1 
ATOM   4276 C CD2 . LEU   B 1 288 ? 2.398   6.072   42.595  1.00 90.36  ?  293 LEU   B CD2 1 
ATOM   4277 N N   . GLU   B 1 289 ? 5.465   2.882   39.341  1.00 110.40 ?  294 GLU   B N   1 
ATOM   4278 C CA  . GLU   B 1 289 ? 6.320   1.749   38.927  1.00 107.18 ?  294 GLU   B CA  1 
ATOM   4279 C C   . GLU   B 1 289 ? 7.813   2.120   38.883  1.00 112.93 ?  294 GLU   B C   1 
ATOM   4280 O O   . GLU   B 1 289 ? 8.250   3.132   39.443  1.00 115.35 ?  294 GLU   B O   1 
ATOM   4281 C CB  . GLU   B 1 289 ? 5.877   1.233   37.548  1.00 104.66 ?  294 GLU   B CB  1 
ATOM   4282 C CG  . GLU   B 1 289 ? 6.565   -0.046  37.084  1.00 103.91 ?  294 GLU   B CG  1 
ATOM   4283 C CD  . GLU   B 1 289 ? 5.779   -0.899  36.145  0.00 97.91  ?  294 GLU   B CD  1 
ATOM   4284 O OE1 . GLU   B 1 289 ? 5.917   -2.140  36.178  0.00 97.22  ?  294 GLU   B OE1 1 
ATOM   4285 O OE2 . GLU   B 1 289 ? 5.009   -0.328  35.342  0.00 96.28  ?  294 GLU   B OE2 1 
HETATM 4286 C C1  . A1BU4 C 2 .   ? -4.974  -0.422  13.563  1.00 48.42  ?  301 A1BU4 A C1  1 
HETATM 4287 C C2  . A1BU4 C 2 .   ? -6.152  -0.524  12.817  1.00 52.53  ?  301 A1BU4 A C2  1 
HETATM 4288 C C3  . A1BU4 C 2 .   ? -7.066  0.528   12.811  1.00 52.82  ?  301 A1BU4 A C3  1 
HETATM 4289 C C4  . A1BU4 C 2 .   ? -6.789  1.684   13.552  1.00 47.61  ?  301 A1BU4 A C4  1 
HETATM 4290 C C5  . A1BU4 C 2 .   ? -5.612  1.779   14.287  1.00 43.18  ?  301 A1BU4 A C5  1 
HETATM 4291 C C6  . A1BU4 C 2 .   ? -4.707  0.732   14.298  1.00 44.95  ?  301 A1BU4 A C6  1 
HETATM 4292 C C7  . A1BU4 C 2 .   ? -5.370  3.058   15.088  1.00 49.29  ?  301 A1BU4 A C7  1 
HETATM 4293 C C12 . A1BU4 C 2 .   ? -6.739  3.333   15.804  1.00 48.64  ?  301 A1BU4 A C12 1 
HETATM 4294 O O14 . A1BU4 C 2 .   ? -3.090  3.868   13.713  1.00 49.54  ?  301 A1BU4 A O14 1 
HETATM 4295 C C15 . A1BU4 C 2 .   ? -3.884  5.760   12.511  1.00 49.15  ?  301 A1BU4 A C15 1 
HETATM 4296 C C16 . A1BU4 C 2 .   ? -4.632  5.541   11.192  1.00 45.67  ?  301 A1BU4 A C16 1 
HETATM 4297 C C17 . A1BU4 C 2 .   ? -4.271  7.102   13.153  1.00 51.70  ?  301 A1BU4 A C17 1 
HETATM 4298 C C18 . A1BU4 C 2 .   ? -2.410  5.930   12.098  1.00 49.53  ?  301 A1BU4 A C18 1 
HETATM 4299 N N8  . A1BU4 C 2 .   ? -5.222  4.192   14.098  1.00 48.30  ?  301 A1BU4 A N8  1 
HETATM 4300 C C9  . A1BU4 C 2 .   ? -6.549  4.835   14.059  1.00 49.35  ?  301 A1BU4 A C9  1 
HETATM 4301 C C10 . A1BU4 C 2 .   ? -7.548  3.782   14.556  1.00 49.40  ?  301 A1BU4 A C10 1 
HETATM 4302 O O11 . A1BU4 C 2 .   ? -7.664  2.723   13.576  1.00 50.26  ?  301 A1BU4 A O11 1 
HETATM 4303 C C13 . A1BU4 C 2 .   ? -4.062  4.569   13.473  1.00 52.77  ?  301 A1BU4 A C13 1 
HETATM 4304 I I   . IOD   D 3 .   ? 3.184   -19.729 24.462  0.80 86.27  -1 302 IOD   A I   1 
HETATM 4305 I I   . IOD   E 3 .   ? -5.536  -14.074 29.918  1.00 144.50 -1 303 IOD   A I   1 
HETATM 4306 C C1  . A1BU4 F 2 .   ? -18.388 -8.789  37.080  1.00 57.73  ?  301 A1BU4 B C1  1 
HETATM 4307 C C2  . A1BU4 F 2 .   ? -19.634 -8.669  36.466  1.00 56.05  ?  301 A1BU4 B C2  1 
HETATM 4308 C C3  . A1BU4 F 2 .   ? -20.090 -9.679  35.626  1.00 59.84  ?  301 A1BU4 B C3  1 
HETATM 4309 C C4  . A1BU4 F 2 .   ? -19.297 -10.814 35.414  1.00 57.36  ?  301 A1BU4 B C4  1 
HETATM 4310 C C5  . A1BU4 F 2 .   ? -18.057 -10.932 36.036  1.00 59.17  ?  301 A1BU4 B C5  1 
HETATM 4311 C C6  . A1BU4 F 2 .   ? -17.604 -9.922  36.868  1.00 63.82  ?  301 A1BU4 B C6  1 
HETATM 4312 C C7  . A1BU4 F 2 .   ? -17.222 -12.187 35.761  1.00 57.13  ?  301 A1BU4 B C7  1 
HETATM 4313 C C12 . A1BU4 F 2 .   ? -17.331 -12.402 34.211  1.00 55.64  ?  301 A1BU4 B C12 1 
HETATM 4314 O O14 . A1BU4 F 2 .   ? -17.393 -12.950 38.428  1.00 61.02  ?  301 A1BU4 B O14 1 
HETATM 4315 C C15 . A1BU4 F 2 .   ? -18.719 -14.901 38.324  1.00 46.19  ?  301 A1BU4 B C15 1 
HETATM 4316 C C16 . A1BU4 F 2 .   ? -20.230 -14.660 38.378  1.00 50.55  ?  301 A1BU4 B C16 1 
HETATM 4317 C C17 . A1BU4 F 2 .   ? -18.429 -16.246 37.642  1.00 50.83  ?  301 A1BU4 B C17 1 
HETATM 4318 C C18 . A1BU4 F 2 .   ? -18.304 -15.102 39.797  1.00 45.13  ?  301 A1BU4 B C18 1 
HETATM 4319 N N8  . A1BU4 F 2 .   ? -17.971 -13.355 36.358  1.00 55.62  ?  301 A1BU4 B N8  1 
HETATM 4320 C C9  . A1BU4 F 2 .   ? -18.730 -13.935 35.230  1.00 57.52  ?  301 A1BU4 B C9  1 
HETATM 4321 C C10 . A1BU4 F 2 .   ? -18.817 -12.852 34.145  1.00 58.60  ?  301 A1BU4 B C10 1 
HETATM 4322 O O11 . A1BU4 F 2 .   ? -19.714 -11.806 34.584  1.00 61.14  ?  301 A1BU4 B O11 1 
HETATM 4323 C C13 . A1BU4 F 2 .   ? -17.974 -13.716 37.684  1.00 53.96  ?  301 A1BU4 B C13 1 
HETATM 4324 I I   . IOD   G 3 .   ? -4.207  10.555  38.209  0.90 130.77 -1 302 IOD   B I   1 
HETATM 4325 I I   . IOD   H 3 .   ? -4.545  4.716   28.005  0.90 159.98 -1 303 IOD   B I   1 
HETATM 4326 I I   . IOD   I 3 .   ? -29.800 -27.258 30.231  1.00 184.02 -1 304 IOD   B I   1 
HETATM 4327 I I   . IOD   J 3 .   ? -35.799 -19.951 40.606  0.90 108.92 -1 305 IOD   B I   1 
HETATM 4328 I I   . IOD   K 3 .   ? 1.303   0.379   31.382  0.75 128.21 -1 306 IOD   B I   1 
HETATM 4329 O O   . HOH   L 4 .   ? -5.647  -1.763  9.162   1.00 52.24  ?  401 HOH   A O   1 
HETATM 4330 O O   . HOH   L 4 .   ? -10.542 12.293  18.503  1.00 63.38  ?  402 HOH   A O   1 
HETATM 4331 O O   . HOH   L 4 .   ? 5.976   -14.542 5.002   1.00 62.01  ?  403 HOH   A O   1 
HETATM 4332 O O   . HOH   L 4 .   ? 6.796   -3.653  25.652  1.00 64.34  ?  404 HOH   A O   1 
HETATM 4333 O O   . HOH   L 4 .   ? -0.944  -0.012  7.394   1.00 48.38  ?  405 HOH   A O   1 
HETATM 4334 O O   . HOH   L 4 .   ? 9.076   -3.462  9.177   1.00 60.12  ?  406 HOH   A O   1 
HETATM 4335 O O   . HOH   L 4 .   ? -6.986  -16.116 6.374   1.00 76.00  ?  407 HOH   A O   1 
HETATM 4336 O O   . HOH   L 4 .   ? -1.824  -8.255  8.966   1.00 48.28  ?  408 HOH   A O   1 
HETATM 4337 O O   . HOH   L 4 .   ? -6.827  -9.128  28.184  1.00 56.89  ?  409 HOH   A O   1 
HETATM 4338 O O   . HOH   L 4 .   ? 15.217  -15.640 6.931   1.00 65.29  ?  410 HOH   A O   1 
HETATM 4339 O O   . HOH   L 4 .   ? 14.412  -13.411 31.215  1.00 71.43  ?  411 HOH   A O   1 
HETATM 4340 O O   . HOH   L 4 .   ? 4.688   -25.565 15.979  1.00 56.89  ?  412 HOH   A O   1 
HETATM 4341 O O   . HOH   L 4 .   ? 0.023   -9.592  33.370  1.00 47.25  ?  413 HOH   A O   1 
HETATM 4342 O O   . HOH   L 4 .   ? 3.341   16.832  26.004  1.00 64.26  ?  414 HOH   A O   1 
HETATM 4343 O O   . HOH   L 4 .   ? 1.029   -6.058  29.754  1.00 58.05  ?  415 HOH   A O   1 
HETATM 4344 O O   . HOH   L 4 .   ? 2.825   1.502   6.594   1.00 53.29  ?  416 HOH   A O   1 
HETATM 4345 O O   . HOH   L 4 .   ? -7.312  -20.675 19.273  1.00 45.78  ?  417 HOH   A O   1 
HETATM 4346 O O   . HOH   L 4 .   ? -12.555 0.455   9.882   1.00 64.55  ?  418 HOH   A O   1 
HETATM 4347 O O   . HOH   L 4 .   ? -12.534 -13.287 10.034  1.00 64.29  ?  419 HOH   A O   1 
HETATM 4348 O O   . HOH   M 4 .   ? -21.805 -9.225  43.429  1.00 60.27  ?  401 HOH   B O   1 
HETATM 4349 O O   . HOH   M 4 .   ? -3.501  -17.515 42.618  1.00 65.95  ?  402 HOH   B O   1 
HETATM 4350 O O   . HOH   M 4 .   ? -21.053 5.098   51.020  1.00 54.34  ?  403 HOH   B O   1 
HETATM 4351 O O   . HOH   M 4 .   ? -15.783 -5.758  50.790  1.00 54.07  ?  404 HOH   B O   1 
HETATM 4352 O O   . HOH   M 4 .   ? -1.040  -2.706  32.586  1.00 62.83  ?  405 HOH   B O   1 
HETATM 4353 O O   . HOH   M 4 .   ? -38.561 -23.058 28.140  1.00 61.24  ?  406 HOH   B O   1 
HETATM 4354 O O   . HOH   M 4 .   ? -27.869 11.667  48.001  1.00 61.79  ?  407 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 1.3796 1.4000 1.5926 0.1748  0.2293  0.0046  6   SER A N   
2    C CA  . SER A 1   ? 1.3698 1.4115 1.5847 0.1678  0.2571  0.0258  6   SER A CA  
3    C C   . SER A 1   ? 1.3424 1.4419 1.6720 0.1553  0.2643  0.0580  6   SER A C   
4    O O   . SER A 1   ? 1.5710 1.6966 1.9738 0.1702  0.2807  0.0675  6   SER A O   
5    C CB  . SER A 1   ? 1.4832 1.5000 1.6296 0.1989  0.3079  0.0234  6   SER A CB  
6    O OG  . SER A 1   ? 1.5387 1.4923 1.5746 0.2081  0.2896  -0.0062 6   SER A OG  
7    N N   . LEU A 2   ? 1.3423 1.4575 1.6930 0.1284  0.2456  0.0734  7   LEU A N   
8    C CA  . LEU A 2   ? 1.2954 1.4550 1.7546 0.1091  0.2329  0.1028  7   LEU A CA  
9    C C   . LEU A 2   ? 1.1921 1.3634 1.7112 0.0931  0.1827  0.1010  7   LEU A C   
10   O O   . LEU A 2   ? 1.0797 1.2684 1.6591 0.0719  0.1530  0.1169  7   LEU A O   
11   C CB  . LEU A 2   ? 1.3153 1.5158 1.8552 0.1238  0.2854  0.1370  7   LEU A CB  
12   C CG  . LEU A 2   ? 1.3367 1.5301 1.8212 0.1343  0.3366  0.1520  7   LEU A CG  
13   C CD1 . LEU A 2   ? 1.4197 1.6572 1.9786 0.1572  0.4028  0.1850  7   LEU A CD1 
14   C CD2 . LEU A 2   ? 1.2291 1.4205 1.7157 0.1042  0.3118  0.1694  7   LEU A CD2 
15   N N   . ASN A 3   ? 1.1005 1.2569 1.6013 0.1029  0.1695  0.0836  8   ASN A N   
16   C CA  . ASN A 3   ? 1.0419 1.2002 1.5787 0.0885  0.1202  0.0836  8   ASN A CA  
17   C C   . ASN A 3   ? 0.9084 1.0320 1.3541 0.0798  0.0932  0.0591  8   ASN A C   
18   O O   . ASN A 3   ? 0.8620 0.9610 1.2369 0.0897  0.1116  0.0414  8   ASN A O   
19   C CB  . ASN A 3   ? 1.0273 1.1988 1.6339 0.1067  0.1257  0.0918  8   ASN A CB  
20   C CG  . ASN A 3   ? 0.9843 1.1965 1.6883 0.1238  0.1692  0.1163  8   ASN A CG  
21   O OD1 . ASN A 3   ? 0.9291 1.1696 1.6937 0.1097  0.1707  0.1402  8   ASN A OD1 
22   N ND2 . ASN A 3   ? 0.9710 1.1865 1.6959 0.1555  0.2058  0.1116  8   ASN A ND2 
23   N N   . VAL A 4   ? 0.7758 0.8960 1.2239 0.0618  0.0488  0.0603  9   VAL A N   
24   C CA  . VAL A 4   ? 0.7974 0.8932 1.1684 0.0521  0.0283  0.0444  9   VAL A CA  
25   C C   . VAL A 4   ? 0.8136 0.8935 1.1745 0.0640  0.0319  0.0413  9   VAL A C   
26   O O   . VAL A 4   ? 0.8381 0.9231 1.2534 0.0702  0.0208  0.0535  9   VAL A O   
27   C CB  . VAL A 4   ? 0.7711 0.8631 1.1291 0.0324  -0.0152 0.0470  9   VAL A CB  
28   C CG1 . VAL A 4   ? 0.8485 0.9404 1.2518 0.0289  -0.0489 0.0644  9   VAL A CG1 
29   C CG2 . VAL A 4   ? 0.7812 0.8567 1.0562 0.0245  -0.0196 0.0320  9   VAL A CG2 
30   N N   . ILE A 5   ? 0.7778 0.8362 1.0795 0.0683  0.0439  0.0256  10  ILE A N   
31   C CA  . ILE A 5   ? 0.7682 0.8023 1.0587 0.0780  0.0396  0.0209  10  ILE A CA  
32   C C   . ILE A 5   ? 0.7246 0.7550 1.0046 0.0580  0.0058  0.0329  10  ILE A C   
33   O O   . ILE A 5   ? 0.6941 0.7244 0.9298 0.0425  0.0002  0.0309  10  ILE A O   
34   C CB  . ILE A 5   ? 0.8334 0.8392 1.0692 0.0886  0.0557  0.0011  10  ILE A CB  
35   C CG1 . ILE A 5   ? 0.9673 0.9709 1.2034 0.1130  0.0919  -0.0062 10  ILE A CG1 
36   C CG2 . ILE A 5   ? 0.8806 0.8529 1.1052 0.0938  0.0378  -0.0044 10  ILE A CG2 
37   C CD1 . ILE A 5   ? 1.1375 1.1030 1.3054 0.1268  0.1044  -0.0263 10  ILE A CD1 
38   N N   . LYS A 6   ? 0.7370 0.7655 1.0601 0.0597  -0.0147 0.0478  11  LYS A N   
39   C CA  . LYS A 6   ? 0.7347 0.7511 1.0429 0.0427  -0.0468 0.0650  11  LYS A CA  
40   C C   . LYS A 6   ? 0.7893 0.7794 1.0792 0.0461  -0.0458 0.0598  11  LYS A C   
41   O O   . LYS A 6   ? 0.9767 0.9469 1.2940 0.0666  -0.0422 0.0499  11  LYS A O   
42   C CB  . LYS A 6   ? 0.7451 0.7602 1.1107 0.0441  -0.0762 0.0847  11  LYS A CB  
43   C CG  . LYS A 6   ? 0.7871 0.8227 1.1886 0.0396  -0.0903 0.0931  11  LYS A CG  
44   C CD  . LYS A 6   ? 0.7656 0.8009 1.2468 0.0456  -0.1196 0.1114  11  LYS A CD  
45   C CE  . LYS A 6   ? 0.7599 0.8164 1.2976 0.0418  -0.1363 0.1203  11  LYS A CE  
46   N NZ  . LYS A 6   ? 0.7766 0.8355 1.4114 0.0481  -0.1691 0.1405  11  LYS A NZ  
47   N N   . MET A 7   ? 0.7889 0.7784 1.0356 0.0282  -0.0478 0.0646  12  MET A N   
48   C CA  . MET A 7   ? 0.7355 0.7020 0.9763 0.0248  -0.0545 0.0658  12  MET A CA  
49   C C   . MET A 7   ? 0.7483 0.7104 0.9937 0.0039  -0.0801 0.0989  12  MET A C   
50   O O   . MET A 7   ? 0.7522 0.7293 0.9800 -0.0097 -0.0882 0.1188  12  MET A O   
51   C CB  . MET A 7   ? 0.7533 0.7285 0.9611 0.0180  -0.0372 0.0541  12  MET A CB  
52   C CG  . MET A 7   ? 0.7661 0.7392 0.9596 0.0355  -0.0156 0.0261  12  MET A CG  
53   S SD  . MET A 7   ? 0.7659 0.7471 0.9316 0.0254  -0.0057 0.0163  12  MET A SD  
54   C CE  . MET A 7   ? 0.7352 0.6827 0.8795 0.0489  0.0028  -0.0122 12  MET A CE  
55   N N   . LYS A 8   ? 0.7365 0.6720 1.0011 0.0011  -0.0961 0.1058  13  LYS A N   
56   C CA  . LYS A 8   ? 0.7198 0.6465 0.9979 -0.0205 -0.1214 0.1433  13  LYS A CA  
57   C C   . LYS A 8   ? 0.6954 0.6307 0.9693 -0.0387 -0.1137 0.1557  13  LYS A C   
58   O O   . LYS A 8   ? 0.6926 0.6186 0.9709 -0.0295 -0.1068 0.1309  13  LYS A O   
59   C CB  . LYS A 8   ? 0.7943 0.6784 1.1209 -0.0082 -0.1540 0.1437  13  LYS A CB  
60   C CG  . LYS A 8   ? 0.8455 0.7257 1.1983 0.0126  -0.1605 0.1341  13  LYS A CG  
61   C CD  . LYS A 8   ? 0.9285 0.7686 1.3351 0.0213  -0.1985 0.1438  13  LYS A CD  
62   C CE  . LYS A 8   ? 1.1032 0.9419 1.5171 -0.0072 -0.2319 0.1927  13  LYS A CE  
63   N NZ  . LYS A 8   ? 1.2439 1.0376 1.7130 -0.0056 -0.2766 0.2095  13  LYS A NZ  
64   N N   . SER A 9   ? 0.7408 0.6930 1.0084 -0.0642 -0.1152 0.1969  14  SER A N   
65   C CA  . SER A 9   ? 0.7924 0.7587 1.0812 -0.0843 -0.1077 0.2208  14  SER A CA  
66   C C   . SER A 9   ? 0.8052 0.7305 1.1541 -0.0834 -0.1414 0.2178  14  SER A C   
67   O O   . SER A 9   ? 0.7929 0.7228 1.1673 -0.0888 -0.1384 0.2139  14  SER A O   
68   C CB  . SER A 9   ? 0.8514 0.8391 1.1270 -0.1113 -0.1029 0.2755  14  SER A CB  
69   O OG  . SER A 9   ? 0.8312 0.8440 1.0356 -0.1100 -0.0788 0.2761  14  SER A OG  
70   N N   . SER A 10  ? 0.9074 0.7890 1.2807 -0.0744 -0.1776 0.2172  15  SER A N   
71   C CA  . SER A 10  ? 0.9254 0.7513 1.3460 -0.0657 -0.2182 0.2041  15  SER A CA  
72   C C   . SER A 10  ? 0.9255 0.7228 1.3276 -0.0372 -0.2158 0.1497  15  SER A C   
73   O O   . SER A 10  ? 1.0607 0.8076 1.4894 -0.0317 -0.2515 0.1369  15  SER A O   
74   C CB  . SER A 10  ? 0.9520 0.7355 1.3987 -0.0549 -0.2547 0.2085  15  SER A CB  
75   O OG  . SER A 10  ? 1.0032 0.7793 1.4264 -0.0212 -0.2416 0.1677  15  SER A OG  
76   N N   . ASP A 11  ? 0.8760 0.6980 1.2295 -0.0191 -0.1789 0.1191  16  ASP A N   
77   C CA  . ASP A 11  ? 0.8837 0.6843 1.2058 0.0034  -0.1703 0.0755  16  ASP A CA  
78   C C   . ASP A 11  ? 0.9430 0.7528 1.2751 -0.0132 -0.1727 0.0795  16  ASP A C   
79   O O   . ASP A 11  ? 1.0604 0.8353 1.3695 0.0030  -0.1825 0.0472  16  ASP A O   
80   C CB  . ASP A 11  ? 0.8247 0.6540 1.1011 0.0221  -0.1297 0.0511  16  ASP A CB  
81   C CG  . ASP A 11  ? 0.7865 0.6095 1.0680 0.0427  -0.1256 0.0440  16  ASP A CG  
82   O OD1 . ASP A 11  ? 0.8611 0.6426 1.1689 0.0556  -0.1529 0.0405  16  ASP A OD1 
83   O OD2 . ASP A 11  ? 0.6988 0.5579 0.9667 0.0470  -0.0976 0.0418  16  ASP A OD2 
84   N N   . PHE A 12  ? 0.8817 0.7373 1.2468 -0.0435 -0.1631 0.1197  17  PHE A N   
85   C CA  . PHE A 12  ? 0.8381 0.7159 1.2346 -0.0599 -0.1601 0.1298  17  PHE A CA  
86   C C   . PHE A 12  ? 0.9089 0.7689 1.3831 -0.0837 -0.1992 0.1650  17  PHE A C   
87   O O   . PHE A 12  ? 0.8531 0.7221 1.3588 -0.1024 -0.2062 0.2059  17  PHE A O   
88   C CB  . PHE A 12  ? 0.7289 0.6770 1.1100 -0.0713 -0.1112 0.1460  17  PHE A CB  
89   C CG  . PHE A 12  ? 0.6739 0.6333 0.9903 -0.0504 -0.0827 0.1126  17  PHE A CG  
90   C CD1 . PHE A 12  ? 0.6775 0.6302 0.9722 -0.0355 -0.0757 0.0785  17  PHE A CD1 
91   C CD2 . PHE A 12  ? 0.6924 0.6618 0.9752 -0.0461 -0.0708 0.1171  17  PHE A CD2 
92   C CE1 . PHE A 12  ? 0.6326 0.5940 0.8773 -0.0188 -0.0523 0.0533  17  PHE A CE1 
93   C CE2 . PHE A 12  ? 0.6467 0.6251 0.8859 -0.0290 -0.0507 0.0900  17  PHE A CE2 
94   C CZ  . PHE A 12  ? 0.6330 0.6089 0.8552 -0.0160 -0.0396 0.0595  17  PHE A CZ  
95   N N   . LEU A 13  ? 0.9951 0.8268 1.5024 -0.0841 -0.2291 0.1517  18  LEU A N   
96   C CA  . LEU A 13  ? 1.0985 0.8986 1.6915 -0.1051 -0.2812 0.1797  18  LEU A CA  
97   C C   . LEU A 13  ? 1.2242 1.0953 1.8992 -0.1401 -0.2573 0.2376  18  LEU A C   
98   O O   . LEU A 13  ? 1.6151 1.4889 2.3591 -0.1656 -0.2770 0.2862  18  LEU A O   
99   C CB  . LEU A 13  ? 1.1211 0.8557 1.7163 -0.0914 -0.3311 0.1419  18  LEU A CB  
100  C CG  . LEU A 13  ? 1.2497 0.8904 1.7794 -0.0582 -0.3725 0.0927  18  LEU A CG  
101  C CD1 . LEU A 13  ? 1.2841 0.9315 1.7199 -0.0274 -0.3269 0.0595  18  LEU A CD1 
102  C CD2 . LEU A 13  ? 1.3388 0.9094 1.8498 -0.0442 -0.4226 0.0556  18  LEU A CD2 
103  N N   . GLU A 14  ? 1.2268 1.1539 1.8974 -0.1394 -0.2144 0.2327  19  GLU A N   
104  C CA  . GLU A 14  ? 1.2909 1.3011 2.0142 -0.1626 -0.1657 0.2813  19  GLU A CA  
105  C C   . GLU A 14  ? 1.2851 1.3470 1.9465 -0.1460 -0.1065 0.2562  19  GLU A C   
106  O O   . GLU A 14  ? 1.0215 1.0564 1.6211 -0.1218 -0.1101 0.2059  19  GLU A O   
107  C CB  . GLU A 14  ? 1.2475 1.2714 2.0968 -0.1862 -0.1920 0.3150  19  GLU A CB  
108  C CG  . GLU A 14  ? 1.2682 1.2680 2.2117 -0.2137 -0.2390 0.3625  19  GLU A CG  
109  C CD  . GLU A 14  ? 1.2803 1.3266 2.2313 -0.2361 -0.2011 0.4231  19  GLU A CD  
110  O OE1 . GLU A 14  ? 1.2592 1.3810 2.1875 -0.2389 -0.1305 0.4456  19  GLU A OE1 
111  O OE2 . GLU A 14  ? 1.3173 1.3187 2.2919 -0.2495 -0.2447 0.4481  19  GLU A OE2 
112  N N   . SER A 15  ? 1.3689 1.5016 2.0438 -0.1586 -0.0523 0.2936  20  SER A N   
113  C CA  . SER A 15  ? 1.1518 1.3342 1.7706 -0.1431 0.0051  0.2742  20  SER A CA  
114  C C   . SER A 15  ? 1.0989 1.3533 1.8010 -0.1559 0.0473  0.3112  20  SER A C   
115  O O   . SER A 15  ? 1.1732 1.4739 1.8778 -0.1691 0.0897  0.3572  20  SER A O   
116  C CB  . SER A 15  ? 1.1154 1.3033 1.6348 -0.1373 0.0335  0.2767  20  SER A CB  
117  O OG  . SER A 15  ? 1.0724 1.2031 1.5323 -0.1226 -0.0006 0.2419  20  SER A OG  
118  N N   . ALA A 16  ? 0.9441 1.2058 1.7170 -0.1514 0.0345  0.2939  21  ALA A N   
119  C CA  . ALA A 16  ? 0.9645 1.2998 1.8352 -0.1581 0.0762  0.3231  21  ALA A CA  
120  C C   . ALA A 16  ? 0.9719 1.3497 1.7768 -0.1323 0.1361  0.2916  21  ALA A C   
121  O O   . ALA A 16  ? 0.8782 1.2214 1.6175 -0.1112 0.1204  0.2388  21  ALA A O   
122  C CB  . ALA A 16  ? 0.9218 1.2408 1.9086 -0.1647 0.0255  0.3188  21  ALA A CB  
123  N N   . GLU A 17  ? 1.0975 1.5468 1.9181 -0.1328 0.2046  0.3245  22  GLU A N   
124  C CA  . GLU A 17  ? 1.1195 1.6057 1.8726 -0.1042 0.2635  0.2927  22  GLU A CA  
125  C C   . GLU A 17  ? 0.9839 1.4912 1.8148 -0.0874 0.2634  0.2612  22  GLU A C   
126  O O   . GLU A 17  ? 0.8854 1.4109 1.6663 -0.0606 0.2998  0.2255  22  GLU A O   
127  C CB  . GLU A 17  ? 1.1833 1.7356 1.9185 -0.1043 0.3416  0.3356  22  GLU A CB  
128  C CG  . GLU A 17  ? 1.2612 1.7863 1.8609 -0.1077 0.3512  0.3479  22  GLU A CG  
129  C CD  . GLU A 17  ? 1.3544 1.9339 1.8939 -0.0975 0.4325  0.3758  22  GLU A CD  
130  O OE1 . GLU A 17  ? 1.2789 1.9265 1.9140 -0.1049 0.4834  0.4223  22  GLU A OE1 
131  O OE2 . GLU A 17  ? 1.4841 2.0367 1.8795 -0.0810 0.4454  0.3520  22  GLU A OE2 
132  N N   . LYS A 25  ? 1.3483 1.6842 1.1797 0.0225  0.3624  0.1141  30  LYS A N   
133  C CA  . LYS A 25  ? 1.3021 1.6743 1.2641 -0.0011 0.3645  0.1528  30  LYS A CA  
134  C C   . LYS A 25  ? 1.2010 1.5500 1.2480 -0.0075 0.3120  0.1268  30  LYS A C   
135  O O   . LYS A 25  ? 1.1444 1.4528 1.1855 -0.0215 0.2638  0.1299  30  LYS A O   
136  C CB  . LYS A 25  ? 1.2729 1.6411 1.2259 -0.0298 0.3572  0.2129  30  LYS A CB  
137  C CG  . LYS A 25  ? 1.4294 1.8247 1.3054 -0.0284 0.4143  0.2538  30  LYS A CG  
138  C CD  . LYS A 25  ? 1.4671 1.8435 1.3200 -0.0584 0.3933  0.3133  30  LYS A CD  
139  C CE  . LYS A 25  ? 1.5872 1.9953 1.3677 -0.0593 0.4572  0.3640  30  LYS A CE  
140  N NZ  . LYS A 25  ? 1.6285 2.0195 1.3994 -0.0925 0.4351  0.4310  30  LYS A NZ  
141  N N   . VAL A 26  ? 1.1100 1.4832 1.2307 0.0054  0.3234  0.1016  31  VAL A N   
142  C CA  . VAL A 26  ? 1.0104 1.3620 1.2070 0.0007  0.2784  0.0806  31  VAL A CA  
143  C C   . VAL A 26  ? 0.9434 1.3172 1.2518 -0.0215 0.2711  0.1200  31  VAL A C   
144  O O   . VAL A 26  ? 1.1171 1.5433 1.4947 -0.0225 0.3102  0.1444  31  VAL A O   
145  C CB  . VAL A 26  ? 0.9137 1.2725 1.1363 0.0243  0.2844  0.0363  31  VAL A CB  
146  C CG1 . VAL A 26  ? 0.7777 1.1054 1.0588 0.0184  0.2351  0.0192  31  VAL A CG1 
147  C CG2 . VAL A 26  ? 1.0493 1.3820 1.1684 0.0470  0.2870  -0.0037 31  VAL A CG2 
148  N N   . SER A 27  ? 0.8540 1.1866 1.1847 -0.0370 0.2202  0.1244  32  SER A N   
149  C CA  . SER A 27  ? 0.8461 1.1814 1.2786 -0.0573 0.1963  0.1550  32  SER A CA  
150  C C   . SER A 27  ? 0.7742 1.0539 1.2219 -0.0572 0.1387  0.1285  32  SER A C   
151  O O   . SER A 27  ? 0.8900 1.1289 1.2667 -0.0477 0.1187  0.1003  32  SER A O   
152  C CB  . SER A 27  ? 0.9249 1.2635 1.3604 -0.0802 0.1971  0.2060  32  SER A CB  
153  O OG  . SER A 27  ? 0.9364 1.2249 1.2992 -0.0825 0.1645  0.1992  32  SER A OG  
154  N N   . LEU A 28  ? 0.7375 1.0154 1.2790 -0.0672 0.1127  0.1398  33  LEU A N   
155  C CA  . LEU A 28  ? 0.7026 0.9200 1.2515 -0.0662 0.0555  0.1172  33  LEU A CA  
156  C C   . LEU A 28  ? 0.7052 0.8802 1.2426 -0.0793 0.0217  0.1355  33  LEU A C   
157  O O   . LEU A 28  ? 0.8699 1.0667 1.4545 -0.0981 0.0276  0.1774  33  LEU A O   
158  C CB  . LEU A 28  ? 0.7031 0.9290 1.3577 -0.0718 0.0326  0.1229  33  LEU A CB  
159  C CG  . LEU A 28  ? 0.7435 0.9022 1.3937 -0.0662 -0.0277 0.0942  33  LEU A CG  
160  C CD1 . LEU A 28  ? 0.8206 0.9613 1.3978 -0.0449 -0.0222 0.0528  33  LEU A CD1 
161  C CD2 . LEU A 28  ? 0.7518 0.9181 1.5219 -0.0771 -0.0599 0.1101  33  LEU A CD2 
162  N N   . ALA A 29  ? 0.6472 0.7619 1.1262 -0.0682 -0.0121 0.1059  34  ALA A N   
163  C CA  . ALA A 29  ? 0.6889 0.7598 1.1425 -0.0720 -0.0394 0.1135  34  ALA A CA  
164  C C   . ALA A 29  ? 0.7616 0.7610 1.1851 -0.0574 -0.0842 0.0802  34  ALA A C   
165  O O   . ALA A 29  ? 0.7861 0.7707 1.1594 -0.0401 -0.0795 0.0479  34  ALA A O   
166  C CB  . ALA A 29  ? 0.6709 0.7528 1.0526 -0.0656 -0.0120 0.1120  34  ALA A CB  
167  N N   . PHE A 30  ? 0.8383 0.7900 1.2869 -0.0630 -0.1272 0.0887  35  PHE A N   
168  C CA  . PHE A 30  ? 0.8610 0.7340 1.2664 -0.0443 -0.1705 0.0544  35  PHE A CA  
169  C C   . PHE A 30  ? 0.7947 0.6332 1.1464 -0.0292 -0.1716 0.0433  35  PHE A C   
170  O O   . PHE A 30  ? 0.7375 0.5661 1.1237 -0.0397 -0.1894 0.0661  35  PHE A O   
171  C CB  . PHE A 30  ? 0.9397 0.7674 1.4095 -0.0555 -0.2292 0.0625  35  PHE A CB  
172  C CG  . PHE A 30  ? 1.1445 0.8808 1.5511 -0.0321 -0.2767 0.0218  35  PHE A CG  
173  C CD1 . PHE A 30  ? 1.1879 0.8983 1.5492 -0.0183 -0.2860 -0.0066 35  PHE A CD1 
174  C CD2 . PHE A 30  ? 1.3033 0.9737 1.6859 -0.0208 -0.3118 0.0105  35  PHE A CD2 
175  C CE1 . PHE A 30  ? 1.3257 0.9445 1.6073 0.0059  -0.3276 -0.0437 35  PHE A CE1 
176  C CE2 . PHE A 30  ? 1.3651 0.9447 1.6711 0.0073  -0.3509 -0.0321 35  PHE A CE2 
177  C CZ  . PHE A 30  ? 1.3155 0.8682 1.5642 0.0205  -0.3576 -0.0585 35  PHE A CZ  
178  N N   . HIS A 31  ? 0.8005 0.6209 1.0771 -0.0045 -0.1538 0.0109  36  HIS A N   
179  C CA  . HIS A 31  ? 0.8820 0.6705 1.1159 0.0161  -0.1515 -0.0040 36  HIS A CA  
180  C C   . HIS A 31  ? 1.0745 0.7792 1.2889 0.0342  -0.1980 -0.0281 36  HIS A C   
181  O O   . HIS A 31  ? 1.1261 0.7877 1.3119 0.0425  -0.2225 -0.0494 36  HIS A O   
182  C CB  . HIS A 31  ? 0.8554 0.6586 1.0294 0.0359  -0.1130 -0.0255 36  HIS A CB  
183  C CG  . HIS A 31  ? 0.8856 0.6882 1.0446 0.0518  -0.0962 -0.0286 36  HIS A CG  
184  N ND1 . HIS A 31  ? 0.9347 0.6834 1.0616 0.0803  -0.1050 -0.0529 36  HIS A ND1 
185  C CD2 . HIS A 31  ? 0.9430 0.7904 1.1182 0.0451  -0.0731 -0.0109 36  HIS A CD2 
186  C CE1 . HIS A 31  ? 0.9938 0.7616 1.1318 0.0904  -0.0847 -0.0483 36  HIS A CE1 
187  N NE2 . HIS A 31  ? 0.9901 0.8157 1.1584 0.0676  -0.0698 -0.0219 36  HIS A NE2 
188  N N   . ARG A 32  ? 1.1195 0.7953 1.3441 0.0426  -0.2137 -0.0268 37  ARG A N   
189  C CA  . ARG A 32  ? 1.1949 0.7833 1.4080 0.0605  -0.2657 -0.0501 37  ARG A CA  
190  C C   . ARG A 32  ? 1.2595 0.7849 1.3765 0.0991  -0.2650 -0.0982 37  ARG A C   
191  O O   . ARG A 32  ? 1.3904 0.8424 1.4795 0.1085  -0.3131 -0.1205 37  ARG A O   
192  C CB  . ARG A 32  ? 1.2522 0.8239 1.4985 0.0655  -0.2797 -0.0406 37  ARG A CB  
193  C CG  . ARG A 32  ? 1.4898 0.9679 1.7423 0.0794  -0.3445 -0.0609 37  ARG A CG  
194  C CD  . ARG A 32  ? 1.3681 0.8261 1.6761 0.0779  -0.3715 -0.0443 37  ARG A CD  
195  N NE  . ARG A 32  ? 1.2232 0.7275 1.6223 0.0327  -0.3858 0.0141  37  ARG A NE  
196  C CZ  . ARG A 32  ? 1.1134 0.6943 1.5381 0.0103  -0.3461 0.0542  37  ARG A CZ  
197  N NH1 . ARG A 32  ? 0.9936 0.6180 1.3736 0.0256  -0.2945 0.0436  37  ARG A NH1 
198  N NH2 . ARG A 32  ? 1.0243 0.6371 1.5204 -0.0288 -0.3599 0.1088  37  ARG A NH2 
199  N N   . THR A 33  ? 1.3029 0.8551 1.3705 0.1206  -0.2123 -0.1108 38  THR A N   
200  C CA  . THR A 33  ? 1.3531 0.8616 1.3228 0.1564  -0.1930 -0.1475 38  THR A CA  
201  C C   . THR A 33  ? 1.2743 0.8141 1.2036 0.1502  -0.1638 -0.1459 38  THR A C   
202  O O   . THR A 33  ? 1.4172 0.9076 1.2584 0.1761  -0.1586 -0.1718 38  THR A O   
203  C CB  . THR A 33  ? 1.3424 0.8547 1.2880 0.1905  -0.1501 -0.1618 38  THR A CB  
204  O OG1 . THR A 33  ? 1.2795 0.8775 1.2662 0.1763  -0.1016 -0.1356 38  THR A OG1 
205  C CG2 . THR A 33  ? 1.3733 0.8463 1.3579 0.2029  -0.1815 -0.1681 38  THR A CG2 
206  N N   . GLN A 34  ? 1.1633 0.7762 1.1491 0.1187  -0.1473 -0.1171 39  GLN A N   
207  C CA  . GLN A 34  ? 1.1425 0.7943 1.1041 0.1134  -0.1151 -0.1135 39  GLN A CA  
208  C C   . GLN A 34  ? 1.0108 0.6814 1.0086 0.0872  -0.1378 -0.1016 39  GLN A C   
209  O O   . GLN A 34  ? 1.0370 0.7414 1.0274 0.0816  -0.1152 -0.0978 39  GLN A O   
210  C CB  . GLN A 34  ? 1.1540 0.8777 1.1448 0.1082  -0.0665 -0.0961 39  GLN A CB  
211  C CG  . GLN A 34  ? 1.2818 0.9988 1.2456 0.1364  -0.0345 -0.1059 39  GLN A CG  
212  C CD  . GLN A 34  ? 1.3975 1.1841 1.4055 0.1268  0.0016  -0.0853 39  GLN A CD  
213  O OE1 . GLN A 34  ? 1.3771 1.2001 1.3874 0.1135  0.0174  -0.0764 39  GLN A OE1 
214  N NE2 . GLN A 34  ? 1.5425 1.3425 1.5891 0.1338  0.0081  -0.0783 39  GLN A NE2 
215  N N   . GLY A 35  ? 0.9788 0.6277 1.0251 0.0720  -0.1834 -0.0945 40  GLY A N   
216  C CA  . GLY A 35  ? 0.9968 0.6612 1.0920 0.0508  -0.2070 -0.0831 40  GLY A CA  
217  C C   . GLY A 35  ? 0.9365 0.6892 1.1095 0.0259  -0.1754 -0.0539 40  GLY A C   
218  O O   . GLY A 35  ? 0.8270 0.6243 1.0249 0.0182  -0.1470 -0.0361 40  GLY A O   
219  N N   . LEU A 36  ? 0.9795 0.7524 1.1853 0.0159  -0.1817 -0.0504 41  LEU A N   
220  C CA  . LEU A 36  ? 0.8859 0.7354 1.1697 -0.0037 -0.1554 -0.0261 41  LEU A CA  
221  C C   . LEU A 36  ? 0.7643 0.6628 1.0157 0.0020  -0.1047 -0.0300 41  LEU A C   
222  O O   . LEU A 36  ? 0.8367 0.7173 1.0344 0.0153  -0.0987 -0.0490 41  LEU A O   
223  C CB  . LEU A 36  ? 0.9526 0.8034 1.2968 -0.0124 -0.1842 -0.0234 41  LEU A CB  
224  C CG  . LEU A 36  ? 1.1135 1.0421 1.5606 -0.0306 -0.1595 0.0046  41  LEU A CG  
225  C CD1 . LEU A 36  ? 1.1570 1.1034 1.6749 -0.0498 -0.1664 0.0379  41  LEU A CD1 
226  C CD2 . LEU A 36  ? 1.1976 1.1269 1.7076 -0.0334 -0.1870 0.0023  41  LEU A CD2 
227  N N   . MET A 37  ? 0.6790 0.6345 0.9620 -0.0090 -0.0723 -0.0098 42  MET A N   
228  C CA  . MET A 37  ? 0.6410 0.6377 0.8943 -0.0048 -0.0321 -0.0129 42  MET A CA  
229  C C   . MET A 37  ? 0.5855 0.6435 0.8846 -0.0164 -0.0035 0.0063  42  MET A C   
230  O O   . MET A 37  ? 0.6109 0.6873 0.9733 -0.0292 -0.0087 0.0279  42  MET A O   
231  C CB  . MET A 37  ? 0.7380 0.7252 0.9510 0.0000  -0.0231 -0.0103 42  MET A CB  
232  C CG  . MET A 37  ? 0.7825 0.7147 0.9508 0.0166  -0.0398 -0.0284 42  MET A CG  
233  S SD  . MET A 37  ? 0.7460 0.6816 0.8914 0.0246  -0.0233 -0.0240 42  MET A SD  
234  C CE  . MET A 37  ? 0.8366 0.7090 0.9316 0.0508  -0.0335 -0.0485 42  MET A CE  
235  N N   . ILE A 38  ? 0.5320 0.6194 0.7987 -0.0103 0.0265  -0.0016 43  ILE A N   
236  C CA  . ILE A 38  ? 0.5700 0.7092 0.8516 -0.0144 0.0603  0.0112  43  ILE A CA  
237  C C   . ILE A 38  ? 0.5822 0.7255 0.8100 -0.0159 0.0733  0.0201  43  ILE A C   
238  O O   . ILE A 38  ? 0.5945 0.7169 0.7780 -0.0077 0.0663  0.0038  43  ILE A O   
239  C CB  . ILE A 38  ? 0.5088 0.6683 0.7925 -0.0016 0.0764  -0.0124 43  ILE A CB  
240  C CG1 . ILE A 38  ? 0.4565 0.6268 0.8172 -0.0033 0.0666  -0.0106 43  ILE A CG1 
241  C CG2 . ILE A 38  ? 0.5227 0.7226 0.7829 0.0039  0.1149  -0.0114 43  ILE A CG2 
242  C CD1 . ILE A 38  ? 0.4052 0.6244 0.8401 -0.0121 0.0894  0.0165  43  ILE A CD1 
243  N N   . MET A 39  ? 0.5870 0.7575 0.8233 -0.0271 0.0909  0.0497  44  MET A N   
244  C CA  . MET A 39  ? 0.6339 0.8045 0.8159 -0.0306 0.0978  0.0639  44  MET A CA  
245  C C   . MET A 39  ? 0.6323 0.8374 0.7760 -0.0249 0.1345  0.0645  44  MET A C   
246  O O   . MET A 39  ? 0.6635 0.9052 0.8359 -0.0305 0.1636  0.0880  44  MET A O   
247  C CB  . MET A 39  ? 0.6895 0.8541 0.8974 -0.0483 0.0853  0.1022  44  MET A CB  
248  C CG  . MET A 39  ? 0.7803 0.9353 0.9334 -0.0530 0.0816  0.1198  44  MET A CG  
249  S SD  . MET A 39  ? 0.9850 1.1208 1.1752 -0.0731 0.0552  0.1637  44  MET A SD  
250  C CE  . MET A 39  ? 0.9235 1.0098 1.1467 -0.0621 0.0151  0.1350  44  MET A CE  
251  N N   . LYS A 40  ? 0.6274 0.8194 0.7091 -0.0122 0.1328  0.0389  45  LYS A N   
252  C CA  . LYS A 40  ? 0.7889 0.9963 0.8064 -0.0026 0.1598  0.0342  45  LYS A CA  
253  C C   . LYS A 40  ? 0.8041 0.9931 0.7611 -0.0123 0.1473  0.0587  45  LYS A C   
254  O O   . LYS A 40  ? 0.7874 0.9442 0.7164 -0.0110 0.1149  0.0471  45  LYS A O   
255  C CB  . LYS A 40  ? 0.8271 1.0198 0.8116 0.0168  0.1536  -0.0094 45  LYS A CB  
256  C CG  . LYS A 40  ? 0.9590 1.1500 0.8574 0.0310  0.1714  -0.0220 45  LYS A CG  
257  C CD  . LYS A 40  ? 0.9733 1.1591 0.8590 0.0541  0.1755  -0.0660 45  LYS A CD  
258  C CE  . LYS A 40  ? 1.0999 1.2745 0.8846 0.0730  0.1923  -0.0828 45  LYS A CE  
259  N NZ  . LYS A 40  ? 1.1997 1.3976 0.9906 0.0988  0.2301  -0.1118 45  LYS A NZ  
260  N N   . THR A 41  ? 0.8155 1.0257 0.7616 -0.0231 0.1714  0.0968  46  THR A N   
261  C CA  . THR A 41  ? 0.9329 1.1237 0.8135 -0.0334 0.1595  0.1262  46  THR A CA  
262  C C   . THR A 41  ? 1.0150 1.2004 0.7874 -0.0171 0.1798  0.1113  46  THR A C   
263  O O   . THR A 41  ? 0.9920 1.2096 0.7395 -0.0088 0.2288  0.1187  46  THR A O   
264  C CB  . THR A 41  ? 0.9524 1.1624 0.8702 -0.0554 0.1717  0.1812  46  THR A CB  
265  O OG1 . THR A 41  ? 0.8895 1.0921 0.9021 -0.0667 0.1443  0.1869  46  THR A OG1 
266  C CG2 . THR A 41  ? 0.9875 1.1696 0.8360 -0.0674 0.1513  0.2147  46  THR A CG2 
267  N N   . VAL A 42  ? 1.0170 1.1595 0.7281 -0.0115 0.1404  0.0911  47  VAL A N   
268  C CA  . VAL A 42  ? 1.0786 1.1967 0.6807 0.0073  0.1414  0.0644  47  VAL A CA  
269  C C   . VAL A 42  ? 1.2075 1.3122 0.7077 0.0017  0.1507  0.1004  47  VAL A C   
270  O O   . VAL A 42  ? 1.3072 1.4183 0.7210 0.0186  0.1911  0.0940  47  VAL A O   
271  C CB  . VAL A 42  ? 1.0985 1.1725 0.6918 0.0130  0.0854  0.0308  47  VAL A CB  
272  C CG1 . VAL A 42  ? 1.2312 1.2679 0.7110 0.0334  0.0744  -0.0016 47  VAL A CG1 
273  C CG2 . VAL A 42  ? 1.0488 1.1372 0.7368 0.0174  0.0824  0.0026  47  VAL A CG2 
274  N N   . TYR A 43  ? 1.2497 1.3332 0.7566 -0.0198 0.1142  0.1377  48  TYR A N   
275  C CA  . TYR A 43  ? 1.3577 1.4203 0.7670 -0.0298 0.1131  0.1809  48  TYR A CA  
276  C C   . TYR A 43  ? 1.3265 1.4051 0.8084 -0.0577 0.1094  0.2378  48  TYR A C   
277  O O   . TYR A 43  ? 1.2278 1.3004 0.8047 -0.0682 0.0730  0.2379  48  TYR A O   
278  C CB  . TYR A 43  ? 1.4811 1.4788 0.8020 -0.0265 0.0499  0.1677  48  TYR A CB  
279  C CG  . TYR A 43  ? 1.6556 1.6172 0.8627 -0.0374 0.0344  0.2124  48  TYR A CG  
280  C CD1 . TYR A 43  ? 1.8177 1.7843 0.9025 -0.0280 0.0868  0.2299  48  TYR A CD1 
281  C CD2 . TYR A 43  ? 1.6888 1.6098 0.9084 -0.0555 -0.0319 0.2391  48  TYR A CD2 
282  C CE1 . TYR A 43  ? 1.9509 1.8791 0.9174 -0.0385 0.0727  0.2755  48  TYR A CE1 
283  C CE2 . TYR A 43  ? 1.8317 1.7129 0.9445 -0.0668 -0.0537 0.2829  48  TYR A CE2 
284  C CZ  . TYR A 43  ? 1.9489 1.8314 0.9287 -0.0594 -0.0022 0.3024  48  TYR A CZ  
285  O OH  . TYR A 43  ? 2.1083 1.9467 0.9700 -0.0712 -0.0236 0.3502  48  TYR A OH  
286  N N   . LYS A 44  ? 1.4850 1.5822 0.9201 -0.0678 0.1488  0.2863  49  LYS A N   
287  C CA  . LYS A 44  ? 1.5142 1.6213 1.0077 -0.0970 0.1435  0.3498  49  LYS A CA  
288  C C   . LYS A 44  ? 1.6949 1.7810 1.0599 -0.1053 0.1544  0.3991  49  LYS A C   
289  O O   . LYS A 44  ? 1.8023 1.9068 1.0735 -0.0904 0.2115  0.4004  49  LYS A O   
290  C CB  . LYS A 44  ? 1.4428 1.6114 1.0499 -0.1054 0.1930  0.3691  49  LYS A CB  
291  C CG  . LYS A 44  ? 1.3559 1.5274 1.0686 -0.1351 0.1681  0.4202  49  LYS A CG  
292  C CD  . LYS A 44  ? 1.2409 1.4643 1.0830 -0.1428 0.2003  0.4303  49  LYS A CD  
293  C CE  . LYS A 44  ? 1.0272 1.2479 0.9476 -0.1281 0.1786  0.3714  49  LYS A CE  
294  N NZ  . LYS A 44  ? 0.9021 1.1598 0.9461 -0.1358 0.1940  0.3785  49  LYS A NZ  
295  N N   . GLY A 45  ? 1.8059 1.8506 1.1615 -0.1261 0.1002  0.4384  50  GLY A N   
296  C CA  . GLY A 45  ? 1.9741 1.9888 1.2031 -0.1380 0.0999  0.4935  50  GLY A CA  
297  C C   . GLY A 45  ? 2.0662 2.0139 1.2703 -0.1507 0.0143  0.5089  50  GLY A C   
298  O O   . GLY A 45  ? 1.9190 1.8612 1.2476 -0.1611 -0.0319 0.5058  50  GLY A O   
299  N N   . PRO A 46  ? 2.3110 2.2043 1.3542 -0.1482 -0.0091 0.5254  51  PRO A N   
300  C CA  . PRO A 46  ? 2.3580 2.1837 1.3832 -0.1600 -0.0996 0.5407  51  PRO A CA  
301  C C   . PRO A 46  ? 2.3043 2.1060 1.3860 -0.1434 -0.1573 0.4760  51  PRO A C   
302  O O   . PRO A 46  ? 2.3000 2.1029 1.3329 -0.1193 -0.1408 0.4206  51  PRO A O   
303  C CB  . PRO A 46  ? 2.5178 2.2893 1.3373 -0.1569 -0.1046 0.5675  51  PRO A CB  
304  C CG  . PRO A 46  ? 2.5575 2.3564 1.2793 -0.1289 -0.0289 0.5294  51  PRO A CG  
305  C CD  . PRO A 46  ? 2.4633 2.3491 1.3297 -0.1316 0.0435  0.5293  51  PRO A CD  
306  N N   . ASN A 47  ? 2.2515 2.0331 1.4418 -0.1553 -0.2221 0.4850  52  ASN A N   
307  C CA  . ASN A 47  ? 2.1999 1.9706 1.4743 -0.1412 -0.2697 0.4325  52  ASN A CA  
308  C C   . ASN A 47  ? 2.2929 1.9981 1.4591 -0.1328 -0.3344 0.4155  52  ASN A C   
309  O O   . ASN A 47  ? 2.3485 2.0011 1.4059 -0.1439 -0.3731 0.4558  52  ASN A O   
310  C CB  . ASN A 47  ? 2.1150 1.8901 1.5478 -0.1518 -0.3097 0.4474  52  ASN A CB  
311  C CG  . ASN A 47  ? 2.2760 2.0033 1.7048 -0.1713 -0.3734 0.5025  52  ASN A CG  
312  O OD1 . ASN A 47  ? 2.4082 2.1035 1.7138 -0.1846 -0.3797 0.5471  52  ASN A OD1 
313  N ND2 . ASN A 47  ? 2.2021 1.9246 1.7686 -0.1719 -0.4185 0.5021  52  ASN A ND2 
314  N N   . CYS A 48  ? 2.2655 1.9708 1.4590 -0.1141 -0.3480 0.3580  53  CYS A N   
315  C CA  . CYS A 48  ? 2.3497 1.9918 1.4610 -0.1048 -0.4163 0.3330  53  CYS A CA  
316  C C   . CYS A 48  ? 2.2004 1.8541 1.4531 -0.0967 -0.4540 0.2927  53  CYS A C   
317  O O   . CYS A 48  ? 1.9378 1.6220 1.2225 -0.0819 -0.4191 0.2479  53  CYS A O   
318  C CB  . CYS A 48  ? 2.4210 2.0405 1.3601 -0.0858 -0.3838 0.3025  53  CYS A CB  
319  S SG  . CYS A 48  ? 2.5009 2.0788 1.2295 -0.0918 -0.3629 0.3542  53  CYS A SG  
320  N N   . ILE A 49  ? 2.3075 1.9374 1.6491 -0.1066 -0.5246 0.3132  54  ILE A N   
321  C CA  . ILE A 49  ? 2.2190 1.8606 1.7075 -0.1005 -0.5646 0.2871  54  ILE A CA  
322  C C   . ILE A 49  ? 2.2491 1.8313 1.6664 -0.0945 -0.6341 0.2616  54  ILE A C   
323  O O   . ILE A 49  ? 2.3380 1.8554 1.6023 -0.0973 -0.6747 0.2736  54  ILE A O   
324  C CB  . ILE A 49  ? 2.1888 1.8365 1.8192 -0.1104 -0.6042 0.3222  54  ILE A CB  
325  C CG1 . ILE A 49  ? 1.9765 1.6755 1.6773 -0.1128 -0.5387 0.3374  54  ILE A CG1 
326  C CG2 . ILE A 49  ? 2.1130 1.7792 1.9058 -0.1024 -0.6391 0.3025  54  ILE A CG2 
327  C CD1 . ILE A 49  ? 2.0595 1.7590 1.8830 -0.1182 -0.5710 0.3681  54  ILE A CD1 
328  N N   . GLU A 50  ? 2.0730 1.6750 1.6036 -0.0867 -0.6492 0.2293  55  GLU A N   
329  C CA  . GLU A 50  ? 2.0703 1.6253 1.5731 -0.0806 -0.7125 0.1979  55  GLU A CA  
330  C C   . GLU A 50  ? 1.9927 1.5732 1.4707 -0.0651 -0.6577 0.1494  55  GLU A C   
331  O O   . GLU A 50  ? 2.1324 1.6776 1.5993 -0.0589 -0.7041 0.1185  55  GLU A O   
332  C CB  . GLU A 50  ? 2.1812 1.6412 1.5229 -0.0839 -0.7954 0.2064  55  GLU A CB  
333  C CG  . GLU A 50  ? 2.4071 1.8117 1.5271 -0.0713 -0.7843 0.1825  55  GLU A CG  
334  C CD  . GLU A 50  ? 2.6010 1.9022 1.5691 -0.0749 -0.8791 0.1966  55  GLU A CD  
335  O OE1 . GLU A 50  ? 2.6324 1.8869 1.6648 -0.0809 -0.9778 0.1942  55  GLU A OE1 
336  O OE2 . GLU A 50  ? 2.7288 1.9937 1.5125 -0.0718 -0.8559 0.2125  55  GLU A OE2 
337  N N   . HIS A 51  ? 1.7934 1.4303 1.2680 -0.0596 -0.5664 0.1441  56  HIS A N   
338  C CA  . HIS A 51  ? 1.7297 1.4108 1.2517 -0.0477 -0.5113 0.1067  56  HIS A CA  
339  C C   . HIS A 51  ? 1.5841 1.3358 1.2741 -0.0504 -0.4661 0.1148  56  HIS A C   
340  O O   . HIS A 51  ? 1.5269 1.3071 1.2746 -0.0428 -0.4391 0.0879  56  HIS A O   
341  C CB  . HIS A 51  ? 1.8172 1.5063 1.2078 -0.0359 -0.4432 0.0895  56  HIS A CB  
342  C CG  . HIS A 51  ? 1.9643 1.5845 1.1815 -0.0234 -0.4747 0.0664  56  HIS A CG  
343  N ND1 . HIS A 51  ? 2.0056 1.6006 1.1684 -0.0047 -0.4794 0.0170  56  HIS A ND1 
344  C CD2 . HIS A 51  ? 2.1117 1.6738 1.1875 -0.0259 -0.5090 0.0877  56  HIS A CD2 
345  C CE1 . HIS A 51  ? 2.1736 1.6962 1.1631 0.0070  -0.5129 0.0040  56  HIS A CE1 
346  N NE2 . HIS A 51  ? 2.2427 1.7441 1.1708 -0.0060 -0.5301 0.0479  56  HIS A NE2 
347  N N   . ASN A 52  ? 1.4395 1.2128 1.1988 -0.0590 -0.4595 0.1496  57  ASN A N   
348  C CA  . ASN A 52  ? 1.2519 1.0841 1.1441 -0.0561 -0.4099 0.1528  57  ASN A CA  
349  C C   . ASN A 52  ? 1.1502 1.0073 1.1783 -0.0506 -0.4206 0.1401  57  ASN A C   
350  O O   . ASN A 52  ? 1.1903 1.0902 1.2813 -0.0428 -0.3677 0.1265  57  ASN A O   
351  C CB  . ASN A 52  ? 1.2378 1.0748 1.1801 -0.0633 -0.4153 0.1898  57  ASN A CB  
352  C CG  . ASN A 52  ? 1.2448 1.0779 1.0893 -0.0705 -0.3818 0.2092  57  ASN A CG  
353  O OD1 . ASN A 52  ? 1.3148 1.1319 1.0339 -0.0709 -0.3661 0.2024  57  ASN A OD1 
354  N ND2 . ASN A 52  ? 1.1882 1.0356 1.0947 -0.0751 -0.3700 0.2347  57  ASN A ND2 
355  N N   . GLU A 53  ? 1.1858 1.0150 1.2597 -0.0555 -0.4900 0.1483  58  GLU A N   
356  C CA  . GLU A 53  ? 1.0869 0.9418 1.3008 -0.0529 -0.5035 0.1439  58  GLU A CA  
357  C C   . GLU A 53  ? 1.0464 0.9054 1.2317 -0.0485 -0.4833 0.1111  58  GLU A C   
358  O O   . GLU A 53  ? 1.0215 0.9246 1.2969 -0.0433 -0.4411 0.1051  58  GLU A O   
359  C CB  . GLU A 53  ? 1.1428 0.9630 1.4179 -0.0616 -0.5927 0.1635  58  GLU A CB  
360  C CG  . GLU A 53  ? 1.1693 0.9769 1.4866 -0.0664 -0.6310 0.1986  58  GLU A CG  
361  C CD  . GLU A 53  ? 1.0711 0.9366 1.5435 -0.0566 -0.5887 0.2148  58  GLU A CD  
362  O OE1 . GLU A 53  ? 1.0838 0.9416 1.5656 -0.0566 -0.5974 0.2369  58  GLU A OE1 
363  O OE2 . GLU A 53  ? 0.9908 0.9055 1.5709 -0.0474 -0.5468 0.2061  58  GLU A OE2 
364  N N   . ALA A 54  ? 1.1175 0.9266 1.1698 -0.0486 -0.5123 0.0899  59  ALA A N   
365  C CA  . ALA A 54  ? 1.1449 0.9471 1.1526 -0.0415 -0.4979 0.0539  59  ALA A CA  
366  C C   . ALA A 54  ? 1.0696 0.9143 1.0489 -0.0322 -0.4122 0.0378  59  ALA A C   
367  O O   . ALA A 54  ? 1.0135 0.8775 1.0337 -0.0276 -0.3889 0.0187  59  ALA A O   
368  C CB  . ALA A 54  ? 1.2783 1.0087 1.1362 -0.0377 -0.5498 0.0310  59  ALA A CB  
369  N N   . LEU A 55  ? 1.0179 0.8729 0.9304 -0.0312 -0.3723 0.0484  60  LEU A N   
370  C CA  . LEU A 55  ? 0.9414 0.8357 0.8386 -0.0245 -0.2981 0.0387  60  LEU A CA  
371  C C   . LEU A 55  ? 0.8561 0.7970 0.8762 -0.0234 -0.2622 0.0455  60  LEU A C   
372  O O   . LEU A 55  ? 0.8589 0.8224 0.8908 -0.0170 -0.2219 0.0272  60  LEU A O   
373  C CB  . LEU A 55  ? 0.9553 0.8510 0.7765 -0.0277 -0.2710 0.0582  60  LEU A CB  
374  C CG  . LEU A 55  ? 1.0673 0.9273 0.7399 -0.0237 -0.2748 0.0498  60  LEU A CG  
375  C CD1 . LEU A 55  ? 1.1361 0.9944 0.7562 -0.0331 -0.2627 0.0864  60  LEU A CD1 
376  C CD2 . LEU A 55  ? 1.1042 0.9818 0.7286 -0.0098 -0.2233 0.0177  60  LEU A CD2 
377  N N   . LEU A 56  ? 0.8786 0.8303 0.9850 -0.0272 -0.2773 0.0713  61  LEU A N   
378  C CA  . LEU A 56  ? 0.8362 0.8272 1.0520 -0.0210 -0.2421 0.0772  61  LEU A CA  
379  C C   . LEU A 56  ? 0.7768 0.7808 1.0605 -0.0193 -0.2448 0.0677  61  LEU A C   
380  O O   . LEU A 56  ? 0.7218 0.7524 1.0362 -0.0126 -0.1994 0.0604  61  LEU A O   
381  C CB  . LEU A 56  ? 0.8910 0.8888 1.1906 -0.0204 -0.2595 0.1043  61  LEU A CB  
382  C CG  . LEU A 56  ? 0.9060 0.9403 1.3023 -0.0069 -0.2148 0.1083  61  LEU A CG  
383  C CD1 . LEU A 56  ? 0.8787 0.9180 1.2250 -0.0002 -0.1672 0.0984  61  LEU A CD1 
384  C CD2 . LEU A 56  ? 0.9695 1.0091 1.4639 -0.0023 -0.2397 0.1320  61  LEU A CD2 
385  N N   . GLU A 57  ? 0.8573 0.8379 1.1632 -0.0267 -0.3024 0.0705  62  GLU A N   
386  C CA  . GLU A 57  ? 0.8891 0.8775 1.2683 -0.0294 -0.3154 0.0666  62  GLU A CA  
387  C C   . GLU A 57  ? 0.8966 0.8788 1.2087 -0.0254 -0.2895 0.0368  62  GLU A C   
388  O O   . GLU A 57  ? 0.8806 0.8861 1.2557 -0.0249 -0.2654 0.0380  62  GLU A O   
389  C CB  . GLU A 57  ? 1.0310 0.9836 1.4413 -0.0399 -0.3969 0.0742  62  GLU A CB  
390  C CG  . GLU A 57  ? 1.2402 1.1938 1.7390 -0.0470 -0.4259 0.0752  62  GLU A CG  
391  C CD  . GLU A 57  ? 1.3387 1.3522 1.9772 -0.0459 -0.3773 0.1008  62  GLU A CD  
392  O OE1 . GLU A 57  ? 1.1768 1.2242 1.8924 -0.0410 -0.3551 0.1253  62  GLU A OE1 
393  O OE2 . GLU A 57  ? 1.3728 1.3971 2.0409 -0.0484 -0.3604 0.0968  62  GLU A OE2 
394  N N   . GLU A 58  ? 0.9136 0.8660 1.1022 -0.0216 -0.2920 0.0131  63  GLU A N   
395  C CA  . GLU A 58  ? 0.8790 0.8286 1.0084 -0.0137 -0.2629 -0.0169 63  GLU A CA  
396  C C   . GLU A 58  ? 0.8386 0.8275 0.9862 -0.0085 -0.1976 -0.0149 63  GLU A C   
397  O O   . GLU A 58  ? 0.9293 0.9260 1.0905 -0.0050 -0.1777 -0.0283 63  GLU A O   
398  C CB  . GLU A 58  ? 0.9297 0.8433 0.9255 -0.0061 -0.2722 -0.0420 63  GLU A CB  
399  C CG  . GLU A 58  ? 1.0035 0.8647 0.9580 -0.0032 -0.3326 -0.0667 63  GLU A CG  
400  C CD  . GLU A 58  ? 1.0876 0.9066 0.8942 0.0093  -0.3409 -0.0913 63  GLU A CD  
401  O OE1 . GLU A 58  ? 1.1015 0.9411 0.8444 0.0190  -0.2850 -0.0993 63  GLU A OE1 
402  O OE2 . GLU A 58  ? 1.1572 0.9197 0.9083 0.0106  -0.4044 -0.1025 63  GLU A OE2 
403  N N   . ALA A 59  ? 0.8028 0.8093 0.9491 -0.0080 -0.1710 0.0016  64  ALA A N   
404  C CA  . ALA A 59  ? 0.7196 0.7540 0.8872 -0.0024 -0.1194 0.0040  64  ALA A CA  
405  C C   . ALA A 59  ? 0.6530 0.7084 0.9120 -0.0001 -0.1041 0.0162  64  ALA A C   
406  O O   . ALA A 59  ? 0.5285 0.5949 0.7885 0.0056  -0.0690 0.0101  64  ALA A O   
407  C CB  . ALA A 59  ? 0.7628 0.8019 0.9140 -0.0025 -0.1057 0.0190  64  ALA A CB  
408  N N   . LYS A 60  ? 0.6626 0.7235 0.9980 -0.0040 -0.1301 0.0358  65  LYS A N   
409  C CA  . LYS A 60  ? 0.6414 0.7275 1.0724 -0.0023 -0.1131 0.0529  65  LYS A CA  
410  C C   . LYS A 60  ? 0.6326 0.7138 1.0691 -0.0077 -0.1175 0.0445  65  LYS A C   
411  O O   . LYS A 60  ? 0.6830 0.7826 1.1526 -0.0041 -0.0810 0.0538  65  LYS A O   
412  C CB  . LYS A 60  ? 0.6973 0.7961 1.2296 -0.0061 -0.1426 0.0797  65  LYS A CB  
413  C CG  . LYS A 60  ? 0.6900 0.8001 1.2495 0.0035  -0.1304 0.0928  65  LYS A CG  
414  C CD  . LYS A 60  ? 0.6779 0.8058 1.3562 0.0024  -0.1567 0.1201  65  LYS A CD  
415  C CE  . LYS A 60  ? 0.6752 0.8096 1.3795 0.0151  -0.1465 0.1292  65  LYS A CE  
416  N NZ  . LYS A 60  ? 0.6727 0.8349 1.5184 0.0197  -0.1606 0.1572  65  LYS A NZ  
417  N N   A MET A 61  ? 0.6783 0.7294 1.0770 -0.0148 -0.1631 0.0271  66  MET A N   
418  N N   B MET A 61  ? 0.6434 0.6946 1.0420 -0.0148 -0.1628 0.0271  66  MET A N   
419  C CA  A MET A 61  ? 0.7090 0.7458 1.1083 -0.0185 -0.1756 0.0139  66  MET A CA  
420  C CA  B MET A 61  ? 0.6500 0.6874 1.0499 -0.0184 -0.1749 0.0142  66  MET A CA  
421  C C   A MET A 61  ? 0.6949 0.7332 1.0324 -0.0100 -0.1344 -0.0058 66  MET A C   
422  C C   B MET A 61  ? 0.6606 0.6989 0.9980 -0.0100 -0.1344 -0.0058 66  MET A C   
423  O O   A MET A 61  ? 0.6821 0.7250 1.0496 -0.0116 -0.1210 -0.0011 66  MET A O   
424  O O   B MET A 61  ? 0.6488 0.6915 1.0160 -0.0116 -0.1211 -0.0012 66  MET A O   
425  C CB  A MET A 61  ? 0.8135 0.8065 1.1692 -0.0219 -0.2369 -0.0094 66  MET A CB  
426  C CB  B MET A 61  ? 0.7042 0.6987 1.0659 -0.0224 -0.2372 -0.0072 66  MET A CB  
427  C CG  A MET A 61  ? 0.9057 0.8835 1.3307 -0.0332 -0.2982 0.0078  66  MET A CG  
428  C CG  B MET A 61  ? 0.7437 0.7286 1.1815 -0.0337 -0.2934 0.0139  66  MET A CG  
429  S SD  A MET A 61  ? 1.0468 0.9539 1.3723 -0.0304 -0.3720 -0.0309 66  MET A SD  
430  S SD  B MET A 61  ? 0.6721 0.6926 1.2759 -0.0470 -0.2936 0.0563  66  MET A SD  
431  C CE  A MET A 61  ? 1.0626 0.9532 1.3881 -0.0365 -0.4200 -0.0120 66  MET A CE  
432  C CE  B MET A 61  ? 0.7294 0.7014 1.3416 -0.0569 -0.3606 0.0380  66  MET A CE  
433  N N   . MET A 62  ? 0.6568 0.6908 0.9151 -0.0023 -0.1175 -0.0236 67  MET A N   
434  C CA  . MET A 62  ? 0.6497 0.6890 0.8640 0.0054  -0.0800 -0.0384 67  MET A CA  
435  C C   . MET A 62  ? 0.6895 0.7472 0.9389 0.0079  -0.0423 -0.0204 67  MET A C   
436  O O   . MET A 62  ? 0.7776 0.8318 1.0166 0.0108  -0.0260 -0.0265 67  MET A O   
437  C CB  . MET A 62  ? 0.6618 0.7025 0.8106 0.0102  -0.0650 -0.0479 67  MET A CB  
438  C CG  . MET A 62  ? 0.7455 0.7671 0.8277 0.0134  -0.0855 -0.0687 67  MET A CG  
439  S SD  . MET A 62  ? 0.7696 0.8013 0.7893 0.0151  -0.0606 -0.0634 67  MET A SD  
440  C CE  . MET A 62  ? 0.8349 0.8358 0.7697 0.0192  -0.0918 -0.0786 67  MET A CE  
441  N N   . ASN A 63  ? 0.6474 0.7200 0.9325 0.0094  -0.0303 0.0005  68  ASN A N   
442  C CA  . ASN A 63  ? 0.6322 0.7168 0.9383 0.0177  0.0078  0.0149  68  ASN A CA  
443  C C   . ASN A 63  ? 0.6522 0.7451 1.0070 0.0155  0.0203  0.0333  68  ASN A C   
444  O O   . ASN A 63  ? 0.6749 0.7668 1.0128 0.0241  0.0545  0.0394  68  ASN A O   
445  C CB  . ASN A 63  ? 0.6706 0.7682 1.0114 0.0239  0.0152  0.0301  68  ASN A CB  
446  C CG  . ASN A 63  ? 0.6669 0.7654 0.9977 0.0401  0.0555  0.0329  68  ASN A CG  
447  O OD1 . ASN A 63  ? 0.6206 0.7353 1.0017 0.0497  0.0802  0.0507  68  ASN A OD1 
448  N ND2 . ASN A 63  ? 0.6731 0.7525 0.9401 0.0447  0.0627  0.0154  68  ASN A ND2 
449  N N   . ARG A 64  ? 0.6895 0.7862 1.1019 0.0036  -0.0096 0.0446  69  ARG A N   
450  C CA  . ARG A 64  ? 0.6402 0.7451 1.1104 -0.0036 -0.0027 0.0691  69  ARG A CA  
451  C C   . ARG A 64  ? 0.6317 0.7153 1.0549 -0.0047 0.0017  0.0582  69  ARG A C   
452  O O   . ARG A 64  ? 0.6381 0.7265 1.0856 -0.0073 0.0232  0.0832  69  ARG A O   
453  C CB  . ARG A 64  ? 0.7683 0.8729 1.3161 -0.0193 -0.0509 0.0815  69  ARG A CB  
454  C CG  . ARG A 64  ? 0.9619 1.0877 1.5882 -0.0223 -0.0668 0.1020  69  ARG A CG  
455  C CD  . ARG A 64  ? 1.1503 1.2672 1.8588 -0.0401 -0.1260 0.1150  69  ARG A CD  
456  N NE  . ARG A 64  ? 1.2993 1.3693 1.9391 -0.0440 -0.1789 0.0780  69  ARG A NE  
457  C CZ  . ARG A 64  ? 1.2086 1.2531 1.8397 -0.0497 -0.2007 0.0666  69  ARG A CZ  
458  N NH1 . ARG A 64  ? 1.1604 1.2193 1.8499 -0.0578 -0.1800 0.0951  69  ARG A NH1 
459  N NH2 . ARG A 64  ? 1.2487 1.2489 1.8082 -0.0458 -0.2446 0.0261  69  ARG A NH2 
460  N N   . LEU A 65  ? 0.6142 0.6753 0.9744 -0.0023 -0.0179 0.0241  70  LEU A N   
461  C CA  . LEU A 65  ? 0.5719 0.6111 0.9017 -0.0027 -0.0254 0.0099  70  LEU A CA  
462  C C   . LEU A 65  ? 0.5752 0.6080 0.8505 0.0070  0.0069  0.0063  70  LEU A C   
463  O O   . LEU A 65  ? 0.6503 0.6767 0.8787 0.0141  0.0076  -0.0181 70  LEU A O   
464  C CB  . LEU A 65  ? 0.5409 0.5614 0.8399 -0.0006 -0.0601 -0.0262 70  LEU A CB  
465  C CG  . LEU A 65  ? 0.5708 0.5811 0.9067 -0.0081 -0.1043 -0.0291 70  LEU A CG  
466  C CD1 . LEU A 65  ? 0.5935 0.5817 0.8696 0.0015  -0.1287 -0.0696 70  LEU A CD1 
467  C CD2 . LEU A 65  ? 0.6134 0.6121 1.0160 -0.0202 -0.1301 -0.0104 70  LEU A CD2 
468  N N   . ARG A 66  ? 0.6015 0.6337 0.8834 0.0072  0.0319  0.0334  71  ARG A N   
469  C CA  . ARG A 66  ? 0.6483 0.6618 0.8677 0.0176  0.0566  0.0324  71  ARG A CA  
470  C C   . ARG A 66  ? 0.6206 0.6088 0.8294 0.0113  0.0439  0.0409  71  ARG A C   
471  O O   . ARG A 66  ? 0.6631 0.6545 0.9081 0.0024  0.0488  0.0724  71  ARG A O   
472  C CB  . ARG A 66  ? 0.7744 0.7972 0.9857 0.0285  0.0995  0.0561  71  ARG A CB  
473  C CG  . ARG A 66  ? 0.8391 0.8893 1.0854 0.0347  0.1122  0.0574  71  ARG A CG  
474  C CD  . ARG A 66  ? 0.9093 0.9491 1.1110 0.0433  0.1053  0.0288  71  ARG A CD  
475  N NE  . ARG A 66  ? 1.0067 1.0691 1.2475 0.0484  0.1130  0.0345  71  ARG A NE  
476  C CZ  . ARG A 66  ? 1.0427 1.1136 1.2954 0.0643  0.1467  0.0473  71  ARG A CZ  
477  N NH1 . ARG A 66  ? 1.0900 1.1460 1.3021 0.0794  0.1822  0.0552  71  ARG A NH1 
478  N NH2 . ARG A 66  ? 1.0710 1.1624 1.3730 0.0677  0.1444  0.0515  71  ARG A NH2 
479  N N   . HIS A 67  ? 0.5855 0.5497 0.7535 0.0151  0.0264  0.0169  72  HIS A N   
480  C CA  . HIS A 67  ? 0.5575 0.4923 0.7170 0.0102  0.0059  0.0223  72  HIS A CA  
481  C C   . HIS A 67  ? 0.5736 0.4858 0.6900 0.0185  -0.0080 -0.0038 72  HIS A C   
482  O O   . HIS A 67  ? 0.5625 0.4896 0.6849 0.0233  -0.0126 -0.0302 72  HIS A O   
483  C CB  . HIS A 67  ? 0.5368 0.4728 0.7556 -0.0002 -0.0283 0.0173  72  HIS A CB  
484  C CG  . HIS A 67  ? 0.6309 0.5354 0.8547 -0.0068 -0.0525 0.0294  72  HIS A CG  
485  N ND1 . HIS A 67  ? 0.6731 0.5575 0.9012 -0.0023 -0.0854 0.0008  72  HIS A ND1 
486  C CD2 . HIS A 67  ? 0.6749 0.5637 0.9014 -0.0170 -0.0477 0.0700  72  HIS A CD2 
487  C CE1 . HIS A 67  ? 0.7246 0.5784 0.9600 -0.0101 -0.1066 0.0217  72  HIS A CE1 
488  N NE2 . HIS A 67  ? 0.7651 0.6199 0.9953 -0.0205 -0.0842 0.0658  72  HIS A NE2 
489  N N   . SER A 68  ? 0.6749 0.5507 0.7512 0.0193  -0.0163 0.0074  73  SER A N   
490  C CA  . SER A 68  ? 0.6691 0.5174 0.7133 0.0259  -0.0380 -0.0126 73  SER A CA  
491  C C   . SER A 68  ? 0.6217 0.4827 0.7179 0.0266  -0.0657 -0.0422 73  SER A C   
492  O O   . SER A 68  ? 0.7115 0.5679 0.8057 0.0322  -0.0770 -0.0594 73  SER A O   
493  C CB  . SER A 68  ? 0.7566 0.5547 0.7484 0.0246  -0.0526 0.0089  73  SER A CB  
494  O OG  . SER A 68  ? 0.8613 0.6532 0.8884 0.0132  -0.0683 0.0289  73  SER A OG  
495  N N   . ARG A 69  ? 0.6152 0.4882 0.7606 0.0222  -0.0783 -0.0468 74  ARG A N   
496  C CA  . ARG A 69  ? 0.6236 0.5104 0.8154 0.0290  -0.0967 -0.0790 74  ARG A CA  
497  C C   . ARG A 69  ? 0.6117 0.5329 0.8191 0.0330  -0.0819 -0.0979 74  ARG A C   
498  O O   . ARG A 69  ? 0.6687 0.5952 0.9047 0.0411  -0.0953 -0.1240 74  ARG A O   
499  C CB  . ARG A 69  ? 0.6232 0.4840 0.8515 0.0264  -0.1315 -0.0783 74  ARG A CB  
500  C CG  . ARG A 69  ? 0.6527 0.4715 0.8585 0.0189  -0.1513 -0.0503 74  ARG A CG  
501  C CD  . ARG A 69  ? 0.7257 0.5273 0.9008 0.0248  -0.1586 -0.0552 74  ARG A CD  
502  N NE  . ARG A 69  ? 0.8871 0.6396 1.0114 0.0177  -0.1755 -0.0241 74  ARG A NE  
503  C CZ  . ARG A 69  ? 0.9285 0.6470 0.9953 0.0207  -0.1853 -0.0185 74  ARG A CZ  
504  N NH1 . ARG A 69  ? 0.8668 0.5969 0.9319 0.0285  -0.1824 -0.0398 74  ARG A NH1 
505  N NH2 . ARG A 69  ? 1.0812 0.7483 1.0869 0.0150  -0.2010 0.0120  74  ARG A NH2 
506  N N   . VAL A 70  ? 0.5559 0.4955 0.7398 0.0299  -0.0565 -0.0868 75  VAL A N   
507  C CA  . VAL A 70  ? 0.5440 0.5104 0.7310 0.0325  -0.0461 -0.1003 75  VAL A CA  
508  C C   . VAL A 70  ? 0.5758 0.5593 0.7368 0.0346  -0.0220 -0.0979 75  VAL A C   
509  O O   . VAL A 70  ? 0.6144 0.5880 0.7538 0.0325  -0.0109 -0.0798 75  VAL A O   
510  C CB  . VAL A 70  ? 0.5298 0.4982 0.7330 0.0236  -0.0501 -0.0831 75  VAL A CB  
511  C CG1 . VAL A 70  ? 0.5823 0.5693 0.7794 0.0259  -0.0480 -0.0959 75  VAL A CG1 
512  C CG2 . VAL A 70  ? 0.5663 0.5128 0.8054 0.0190  -0.0816 -0.0827 75  VAL A CG2 
513  N N   . VAL A 71  ? 0.6366 0.6420 0.7965 0.0401  -0.0139 -0.1153 76  VAL A N   
514  C CA  . VAL A 71  ? 0.6195 0.6410 0.7645 0.0395  0.0047  -0.1093 76  VAL A CA  
515  C C   . VAL A 71  ? 0.5482 0.5720 0.6787 0.0342  0.0134  -0.0916 76  VAL A C   
516  O O   . VAL A 71  ? 0.5195 0.5496 0.6539 0.0321  0.0081  -0.0917 76  VAL A O   
517  C CB  . VAL A 71  ? 0.6286 0.6769 0.7762 0.0452  0.0166  -0.1243 76  VAL A CB  
518  C CG1 . VAL A 71  ? 0.6751 0.7393 0.8138 0.0401  0.0327  -0.1099 76  VAL A CG1 
519  C CG2 . VAL A 71  ? 0.6180 0.6714 0.7973 0.0537  0.0139  -0.1403 76  VAL A CG2 
520  N N   . LYS A 72  ? 0.5394 0.5537 0.6564 0.0341  0.0225  -0.0782 77  LYS A N   
521  C CA  . LYS A 72  ? 0.5473 0.5638 0.6600 0.0339  0.0338  -0.0624 77  LYS A CA  
522  C C   . LYS A 72  ? 0.5704 0.6035 0.6814 0.0321  0.0377  -0.0619 77  LYS A C   
523  O O   . LYS A 72  ? 0.5179 0.5537 0.6249 0.0314  0.0381  -0.0664 77  LYS A O   
524  C CB  . LYS A 72  ? 0.5731 0.5646 0.6616 0.0406  0.0435  -0.0529 77  LYS A CB  
525  C CG  . LYS A 72  ? 0.6790 0.6745 0.7727 0.0457  0.0626  -0.0361 77  LYS A CG  
526  C CD  . LYS A 72  ? 0.6225 0.5910 0.6782 0.0589  0.0788  -0.0315 77  LYS A CD  
527  C CE  . LYS A 72  ? 0.6294 0.6099 0.7009 0.0693  0.1021  -0.0204 77  LYS A CE  
528  N NZ  . LYS A 72  ? 0.6837 0.6349 0.7079 0.0890  0.1268  -0.0177 77  LYS A NZ  
529  N N   . LEU A 73  ? 0.5372 0.5811 0.6586 0.0297  0.0369  -0.0527 78  LEU A N   
530  C CA  . LEU A 73  ? 0.5564 0.6094 0.6742 0.0272  0.0370  -0.0453 78  LEU A CA  
531  C C   . LEU A 73  ? 0.5372 0.5778 0.6594 0.0340  0.0463  -0.0356 78  LEU A C   
532  O O   . LEU A 73  ? 0.5514 0.5912 0.6912 0.0398  0.0541  -0.0270 78  LEU A O   
533  C CB  . LEU A 73  ? 0.5775 0.6388 0.7048 0.0227  0.0231  -0.0393 78  LEU A CB  
534  C CG  . LEU A 73  ? 0.5736 0.6391 0.6924 0.0184  0.0160  -0.0277 78  LEU A CG  
535  C CD1 . LEU A 73  ? 0.5975 0.6691 0.6782 0.0147  0.0192  -0.0327 78  LEU A CD1 
536  C CD2 . LEU A 73  ? 0.6507 0.7157 0.7864 0.0147  -0.0069 -0.0197 78  LEU A CD2 
537  N N   . LEU A 74  ? 0.5402 0.5704 0.6508 0.0347  0.0456  -0.0371 79  LEU A N   
538  C CA  . LEU A 74  ? 0.5962 0.6033 0.7028 0.0448  0.0483  -0.0344 79  LEU A CA  
539  C C   . LEU A 74  ? 0.5997 0.6132 0.7280 0.0455  0.0450  -0.0220 79  LEU A C   
540  O O   . LEU A 74  ? 0.6240 0.6223 0.7592 0.0595  0.0513  -0.0213 79  LEU A O   
541  C CB  . LEU A 74  ? 0.6119 0.5972 0.7065 0.0438  0.0368  -0.0407 79  LEU A CB  
542  C CG  . LEU A 74  ? 0.6373 0.6102 0.7176 0.0439  0.0318  -0.0520 79  LEU A CG  
543  C CD1 . LEU A 74  ? 0.7227 0.6737 0.8082 0.0408  0.0115  -0.0546 79  LEU A CD1 
544  C CD2 . LEU A 74  ? 0.6051 0.5526 0.6536 0.0568  0.0403  -0.0569 79  LEU A CD2 
545  N N   . GLY A 75  ? 0.6057 0.6378 0.7404 0.0325  0.0346  -0.0126 80  GLY A N   
546  C CA  . GLY A 75  ? 0.6376 0.6736 0.7925 0.0305  0.0237  0.0027  80  GLY A CA  
547  C C   . GLY A 75  ? 0.6096 0.6593 0.7475 0.0156  0.0113  0.0132  80  GLY A C   
548  O O   . GLY A 75  ? 0.5414 0.6012 0.6533 0.0101  0.0175  0.0059  80  GLY A O   
549  N N   . VAL A 76  ? 0.6571 0.7041 0.8067 0.0115  -0.0059 0.0305  81  VAL A N   
550  C CA  . VAL A 76  ? 0.7150 0.7657 0.8321 -0.0015 -0.0210 0.0447  81  VAL A CA  
551  C C   . VAL A 76  ? 0.6857 0.7251 0.8117 -0.0089 -0.0364 0.0701  81  VAL A C   
552  O O   . VAL A 76  ? 0.7628 0.7902 0.9322 -0.0010 -0.0459 0.0741  81  VAL A O   
553  C CB  . VAL A 76  ? 0.7240 0.7745 0.8415 -0.0014 -0.0409 0.0422  81  VAL A CB  
554  C CG1 . VAL A 76  ? 0.7783 0.8245 0.9555 0.0034  -0.0596 0.0549  81  VAL A CG1 
555  C CG2 . VAL A 76  ? 0.8082 0.8521 0.8636 -0.0109 -0.0570 0.0484  81  VAL A CG2 
556  N N   . ILE A 77  ? 0.6847 0.7275 0.7712 -0.0225 -0.0365 0.0881  82  ILE A N   
557  C CA  . ILE A 77  ? 0.6802 0.7103 0.7695 -0.0342 -0.0557 0.1205  82  ILE A CA  
558  C C   . ILE A 77  ? 0.7296 0.7519 0.7690 -0.0415 -0.0772 0.1350  82  ILE A C   
559  O O   . ILE A 77  ? 0.7812 0.8109 0.7567 -0.0442 -0.0644 0.1313  82  ILE A O   
560  C CB  . ILE A 77  ? 0.7034 0.7426 0.7881 -0.0468 -0.0392 0.1399  82  ILE A CB  
561  C CG1 . ILE A 77  ? 0.6392 0.6742 0.7725 -0.0391 -0.0313 0.1227  82  ILE A CG1 
562  C CG2 . ILE A 77  ? 0.7697 0.7940 0.8584 -0.0627 -0.0615 0.1814  82  ILE A CG2 
563  C CD1 . ILE A 77  ? 0.6715 0.7193 0.8199 -0.0518 -0.0180 0.1385  82  ILE A CD1 
564  N N   . ILE A 78  ? 0.8004 0.8035 0.8683 -0.0419 -0.1123 0.1494  83  ILE A N   
565  C CA  . ILE A 78  ? 0.8768 0.8602 0.8977 -0.0510 -0.1471 0.1697  83  ILE A CA  
566  C C   . ILE A 78  ? 0.9271 0.8918 0.9741 -0.0614 -0.1722 0.2062  83  ILE A C   
567  O O   . ILE A 78  ? 0.9445 0.8995 1.0667 -0.0536 -0.1947 0.2073  83  ILE A O   
568  C CB  . ILE A 78  ? 0.8507 0.8263 0.9007 -0.0425 -0.1773 0.1543  83  ILE A CB  
569  C CG1 . ILE A 78  ? 0.8295 0.8191 0.8557 -0.0345 -0.1562 0.1208  83  ILE A CG1 
570  C CG2 . ILE A 78  ? 0.9353 0.8790 0.9388 -0.0525 -0.2278 0.1768  83  ILE A CG2 
571  C CD1 . ILE A 78  ? 0.8032 0.7918 0.8850 -0.0275 -0.1809 0.1074  83  ILE A CD1 
572  N N   . GLU A 79  ? 0.9859 0.9471 0.9758 -0.0776 -0.1655 0.2371  84  GLU A N   
573  C CA  . GLU A 79  ? 1.0809 1.0211 1.0886 -0.0924 -0.1919 0.2800  84  GLU A CA  
574  C C   . GLU A 79  ? 1.2503 1.1690 1.1631 -0.1086 -0.2126 0.3172  84  GLU A C   
575  O O   . GLU A 79  ? 1.3718 1.2892 1.1969 -0.1053 -0.2043 0.3045  84  GLU A O   
576  C CB  . GLU A 79  ? 1.0654 1.0208 1.1072 -0.1001 -0.1633 0.2922  84  GLU A CB  
577  C CG  . GLU A 79  ? 1.0264 0.9837 1.1527 -0.0833 -0.1578 0.2595  84  GLU A CG  
578  C CD  . GLU A 79  ? 1.0274 0.9863 1.1936 -0.0918 -0.1463 0.2716  84  GLU A CD  
579  O OE1 . GLU A 79  ? 1.0827 1.0595 1.2209 -0.1103 -0.1261 0.3008  84  GLU A OE1 
580  O OE2 . GLU A 79  ? 0.9666 0.9069 1.1945 -0.0785 -0.1583 0.2520  84  GLU A OE2 
581  N N   . GLU A 80  ? 1.3929 1.2873 1.3188 -0.1244 -0.2437 0.3623  85  GLU A N   
582  C CA  . GLU A 80  ? 1.5417 1.4093 1.3690 -0.1421 -0.2643 0.4074  85  GLU A CA  
583  C C   . GLU A 80  ? 1.5015 1.3969 1.2453 -0.1504 -0.2056 0.4229  85  GLU A C   
584  O O   . GLU A 80  ? 1.4227 1.3362 1.1999 -0.1655 -0.1812 0.4570  85  GLU A O   
585  C CB  . GLU A 80  ? 1.6073 1.4424 1.4805 -0.1589 -0.3113 0.4572  85  GLU A CB  
586  C CG  . GLU A 80  ? 1.5657 1.3717 1.5151 -0.1471 -0.3728 0.4437  85  GLU A CG  
587  C CD  . GLU A 80  ? 1.6232 1.3891 1.6094 -0.1624 -0.4287 0.4937  85  GLU A CD  
588  O OE1 . GLU A 80  ? 1.6180 1.3843 1.6471 -0.1744 -0.4207 0.5218  85  GLU A OE1 
589  O OE2 . GLU A 80  ? 1.6751 1.4057 1.6547 -0.1629 -0.4869 0.5060  85  GLU A OE2 
590  N N   . GLY A 81  ? 1.4494 1.3491 1.0971 -0.1385 -0.1835 0.3952  86  GLY A N   
591  C CA  . GLY A 81  ? 1.4999 1.4257 1.0573 -0.1395 -0.1236 0.4055  86  GLY A CA  
592  C C   . GLY A 81  ? 1.4200 1.3939 1.0138 -0.1243 -0.0669 0.3635  86  GLY A C   
593  O O   . GLY A 81  ? 1.5047 1.4961 1.0149 -0.1149 -0.0213 0.3546  86  GLY A O   
594  N N   . LYS A 82  ? 1.2723 1.2642 0.9844 -0.1197 -0.0694 0.3381  87  LYS A N   
595  C CA  . LYS A 82  ? 1.1616 1.1933 0.9194 -0.1072 -0.0251 0.3012  87  LYS A CA  
596  C C   . LYS A 82  ? 1.0897 1.1127 0.8681 -0.0875 -0.0430 0.2466  87  LYS A C   
597  O O   . LYS A 82  ? 1.1180 1.1194 0.9486 -0.0857 -0.0834 0.2401  87  LYS A O   
598  C CB  . LYS A 82  ? 1.1243 1.1750 0.9924 -0.1177 -0.0181 0.3169  87  LYS A CB  
599  C CG  . LYS A 82  ? 1.1190 1.2076 1.0354 -0.1086 0.0226  0.2884  87  LYS A CG  
600  C CD  . LYS A 82  ? 1.0950 1.1865 1.1166 -0.1179 0.0129  0.2994  87  LYS A CD  
601  C CE  . LYS A 82  ? 1.1077 1.2228 1.1759 -0.1057 0.0363  0.2622  87  LYS A CE  
602  N NZ  . LYS A 82  ? 1.1558 1.2634 1.3163 -0.1131 0.0190  0.2685  87  LYS A NZ  
603  N N   . TYR A 83  ? 1.0282 1.0699 0.7744 -0.0724 -0.0115 0.2103  88  TYR A N   
604  C CA  . TYR A 83  ? 0.9032 0.9397 0.6734 -0.0559 -0.0243 0.1626  88  TYR A CA  
605  C C   . TYR A 83  ? 0.8016 0.8722 0.6067 -0.0461 0.0179  0.1356  88  TYR A C   
606  O O   . TYR A 83  ? 0.8007 0.8927 0.5615 -0.0415 0.0565  0.1348  88  TYR A O   
607  C CB  . TYR A 83  ? 0.9884 0.9956 0.6677 -0.0464 -0.0467 0.1430  88  TYR A CB  
608  C CG  . TYR A 83  ? 1.0541 1.0201 0.6990 -0.0554 -0.1002 0.1669  88  TYR A CG  
609  C CD1 . TYR A 83  ? 1.1430 1.0917 0.7061 -0.0667 -0.1027 0.2064  88  TYR A CD1 
610  C CD2 . TYR A 83  ? 1.0403 0.9848 0.7384 -0.0530 -0.1496 0.1541  88  TYR A CD2 
611  C CE1 . TYR A 83  ? 1.2180 1.1221 0.7456 -0.0758 -0.1597 0.2308  88  TYR A CE1 
612  C CE2 . TYR A 83  ? 1.1011 1.0070 0.7799 -0.0613 -0.2057 0.1775  88  TYR A CE2 
613  C CZ  . TYR A 83  ? 1.2061 1.0880 0.7955 -0.0728 -0.2143 0.2149  88  TYR A CZ  
614  O OH  . TYR A 83  ? 1.3001 1.1373 0.8650 -0.0821 -0.2765 0.2412  88  TYR A OH  
615  N N   . SER A 84  ? 0.7175 0.7919 0.6003 -0.0411 0.0112  0.1150  89  SER A N   
616  C CA  . SER A 84  ? 0.6876 0.7866 0.6119 -0.0338 0.0405  0.0931  89  SER A CA  
617  C C   . SER A 84  ? 0.6422 0.7322 0.6025 -0.0223 0.0276  0.0601  89  SER A C   
618  O O   . SER A 84  ? 0.6125 0.6850 0.6005 -0.0216 0.0020  0.0611  89  SER A O   
619  C CB  . SER A 84  ? 0.6720 0.7841 0.6606 -0.0444 0.0501  0.1153  89  SER A CB  
620  O OG  . SER A 84  ? 0.7340 0.8594 0.7072 -0.0590 0.0643  0.1553  89  SER A OG  
621  N N   . LEU A 85  ? 0.6465 0.7504 0.6105 -0.0126 0.0476  0.0341  90  LEU A N   
622  C CA  . LEU A 85  ? 0.5865 0.6839 0.5876 -0.0039 0.0410  0.0088  90  LEU A CA  
623  C C   . LEU A 85  ? 0.5379 0.6449 0.5842 -0.0046 0.0551  0.0091  90  LEU A C   
624  O O   . LEU A 85  ? 0.5319 0.6599 0.5849 -0.0076 0.0752  0.0157  90  LEU A O   
625  C CB  . LEU A 85  ? 0.5902 0.6866 0.5631 0.0070  0.0427  -0.0200 90  LEU A CB  
626  C CG  . LEU A 85  ? 0.6536 0.7298 0.5742 0.0087  0.0185  -0.0248 90  LEU A CG  
627  C CD1 . LEU A 85  ? 0.7017 0.7708 0.5842 0.0221  0.0197  -0.0566 90  LEU A CD1 
628  C CD2 . LEU A 85  ? 0.6445 0.7044 0.6040 0.0050  -0.0130 -0.0192 90  LEU A CD2 
629  N N   . VAL A 86  ? 0.5504 0.6405 0.6284 -0.0009 0.0439  0.0033  91  VAL A N   
630  C CA  . VAL A 86  ? 0.5661 0.6492 0.6763 -0.0001 0.0451  0.0011  91  VAL A CA  
631  C C   . VAL A 86  ? 0.5830 0.6560 0.6946 0.0102  0.0452  -0.0220 91  VAL A C   
632  O O   . VAL A 86  ? 0.5636 0.6238 0.6709 0.0166  0.0406  -0.0272 91  VAL A O   
633  C CB  . VAL A 86  ? 0.5588 0.6176 0.6877 -0.0007 0.0297  0.0130  91  VAL A CB  
634  C CG1 . VAL A 86  ? 0.5395 0.5783 0.6900 0.0018  0.0217  0.0061  91  VAL A CG1 
635  C CG2 . VAL A 86  ? 0.6115 0.6770 0.7435 -0.0137 0.0243  0.0415  91  VAL A CG2 
636  N N   . MET A 87  ? 0.6358 0.7164 0.7609 0.0111  0.0505  -0.0315 92  MET A N   
637  C CA  . MET A 87  ? 0.6155 0.6848 0.7411 0.0189  0.0469  -0.0502 92  MET A CA  
638  C C   . MET A 87  ? 0.6639 0.7190 0.8127 0.0190  0.0366  -0.0527 92  MET A C   
639  O O   . MET A 87  ? 0.8169 0.8762 0.9920 0.0120  0.0325  -0.0404 92  MET A O   
640  C CB  . MET A 87  ? 0.6225 0.7109 0.7414 0.0228  0.0551  -0.0643 92  MET A CB  
641  C CG  . MET A 87  ? 0.6343 0.7504 0.7727 0.0233  0.0706  -0.0658 92  MET A CG  
642  S SD  . MET A 87  ? 0.7462 0.8814 0.8478 0.0323  0.0871  -0.0803 92  MET A SD  
643  C CE  . MET A 87  ? 0.8841 1.0490 1.0339 0.0412  0.1079  -0.0901 92  MET A CE  
644  N N   . GLU A 88  ? 0.7227 0.7571 0.8644 0.0255  0.0275  -0.0655 93  GLU A N   
645  C CA  . GLU A 88  ? 0.7775 0.7835 0.9295 0.0267  0.0068  -0.0688 93  GLU A CA  
646  C C   . GLU A 88  ? 0.6294 0.6598 0.8343 0.0229  0.0035  -0.0705 93  GLU A C   
647  O O   . GLU A 88  ? 0.5948 0.6583 0.8163 0.0254  0.0209  -0.0769 93  GLU A O   
648  C CB  . GLU A 88  ? 0.8569 0.8248 0.9707 0.0349  -0.0032 -0.0764 93  GLU A CB  
649  C CG  . GLU A 88  ? 0.9750 0.9517 1.0930 0.0366  -0.0009 -0.0837 93  GLU A CG  
650  C CD  . GLU A 88  ? 1.0398 0.9887 1.1182 0.0414  0.0008  -0.0791 93  GLU A CD  
651  O OE1 . GLU A 88  ? 1.2534 1.1635 1.2914 0.0473  -0.0059 -0.0759 93  GLU A OE1 
652  O OE2 . GLU A 88  ? 1.0883 1.0519 1.1752 0.0398  0.0083  -0.0777 93  GLU A OE2 
653  N N   . TYR A 89  ? 0.6847 0.6956 0.9188 0.0188  -0.0207 -0.0655 94  TYR A N   
654  C CA  . TYR A 89  ? 0.6261 0.6637 0.9348 0.0138  -0.0264 -0.0604 94  TYR A CA  
655  C C   . TYR A 89  ? 0.5750 0.6007 0.8984 0.0211  -0.0430 -0.0754 94  TYR A C   
656  O O   . TYR A 89  ? 0.5996 0.5739 0.8807 0.0247  -0.0713 -0.0823 94  TYR A O   
657  C CB  . TYR A 89  ? 0.5958 0.6084 0.9407 0.0043  -0.0589 -0.0467 94  TYR A CB  
658  C CG  . TYR A 89  ? 0.5083 0.5506 0.9535 -0.0038 -0.0696 -0.0344 94  TYR A CG  
659  C CD1 . TYR A 89  ? 0.4562 0.5675 0.9636 -0.0083 -0.0292 -0.0181 94  TYR A CD1 
660  C CD2 . TYR A 89  ? 0.5327 0.5330 1.0126 -0.0063 -0.1208 -0.0362 94  TYR A CD2 
661  C CE1 . TYR A 89  ? 0.4587 0.6069 1.0752 -0.0146 -0.0316 -0.0019 94  TYR A CE1 
662  C CE2 . TYR A 89  ? 0.5471 0.5791 1.1417 -0.0150 -0.1344 -0.0207 94  TYR A CE2 
663  C CZ  . TYR A 89  ? 0.5018 0.6128 1.1725 -0.0192 -0.0861 -0.0019 94  TYR A CZ  
664  O OH  . TYR A 89  ? 0.4940 0.6451 1.2933 -0.0267 -0.0926 0.0177  94  TYR A OH  
665  N N   . MET A 90  ? 0.5625 0.6333 0.9441 0.0250  -0.0248 -0.0794 95  MET A N   
666  C CA  . MET A 90  ? 0.5470 0.6119 0.9663 0.0330  -0.0431 -0.0930 95  MET A CA  
667  C C   . MET A 90  ? 0.5449 0.6481 1.0711 0.0306  -0.0443 -0.0830 95  MET A C   
668  O O   . MET A 90  ? 0.4866 0.6484 1.0576 0.0355  -0.0026 -0.0799 95  MET A O   
669  C CB  . MET A 90  ? 0.5696 0.6528 0.9677 0.0453  -0.0189 -0.1118 95  MET A CB  
670  C CG  . MET A 90  ? 0.6662 0.7221 0.9805 0.0448  -0.0157 -0.1153 95  MET A CG  
671  S SD  . MET A 90  ? 0.7515 0.7402 1.0123 0.0415  -0.0532 -0.1107 95  MET A SD  
672  C CE  . MET A 90  ? 0.7980 0.7766 1.0896 0.0492  -0.0733 -0.1245 95  MET A CE  
673  N N   . GLU A 91  ? 0.7726 0.6243 1.0560 -0.1729 -0.0644 -0.0451 96  GLU A N   
674  C CA  . GLU A 91  ? 0.7792 0.6494 1.0949 -0.2080 -0.0670 -0.0471 96  GLU A CA  
675  C C   . GLU A 91  ? 0.7749 0.7142 1.1208 -0.2140 -0.0604 -0.0336 96  GLU A C   
676  O O   . GLU A 91  ? 0.7874 0.7357 1.1575 -0.2394 -0.0494 -0.0203 96  GLU A O   
677  C CB  . GLU A 91  ? 0.7845 0.6548 1.1033 -0.2217 -0.0867 -0.0774 96  GLU A CB  
678  C CG  . GLU A 91  ? 0.9118 0.8086 1.2704 -0.2610 -0.0934 -0.0841 96  GLU A CG  
679  C CD  . GLU A 91  ? 1.0808 0.9521 1.4361 -0.2794 -0.1141 -0.1153 96  GLU A CD  
680  O OE1 . GLU A 91  ? 1.1969 1.0485 1.5181 -0.2578 -0.1256 -0.1351 96  GLU A OE1 
681  O OE2 . GLU A 91  ? 1.1199 0.9917 1.5063 -0.3178 -0.1185 -0.1208 96  GLU A OE2 
682  N N   . LYS A 92  ? 0.7674 0.7522 1.1098 -0.1904 -0.0661 -0.0369 97  LYS A N   
683  C CA  . LYS A 92  ? 0.7329 0.7855 1.1029 -0.1887 -0.0621 -0.0287 97  LYS A CA  
684  C C   . LYS A 92  ? 0.7371 0.7958 1.1001 -0.1754 -0.0424 -0.0043 97  LYS A C   
685  O O   . LYS A 92  ? 0.8118 0.9247 1.1953 -0.1714 -0.0363 0.0016  97  LYS A O   
686  C CB  . LYS A 92  ? 0.7363 0.8270 1.1011 -0.1670 -0.0793 -0.0431 97  LYS A CB  
687  C CG  . LYS A 92  ? 0.7567 0.8574 1.1314 -0.1816 -0.1010 -0.0675 97  LYS A CG  
688  C CD  . LYS A 92  ? 0.7655 0.9131 1.1391 -0.1614 -0.1193 -0.0778 97  LYS A CD  
689  C CE  . LYS A 92  ? 0.8415 1.0108 1.2313 -0.1788 -0.1436 -0.1019 97  LYS A CE  
690  N NZ  . LYS A 92  ? 0.8572 1.0834 1.3064 -0.2063 -0.1448 -0.1040 97  LYS A NZ  
691  N N   . GLY A 93  ? 0.6788 0.6845 1.0126 -0.1665 -0.0337 0.0083  98  GLY A N   
692  C CA  . GLY A 93  ? 0.6062 0.6104 0.9288 -0.1577 -0.0168 0.0314  98  GLY A CA  
693  C C   . GLY A 93  ? 0.5830 0.6062 0.8875 -0.1266 -0.0196 0.0317  98  GLY A C   
694  O O   . GLY A 93  ? 0.6206 0.6382 0.9130 -0.1118 -0.0323 0.0182  98  GLY A O   
695  N N   . ASN A 94  ? 0.5991 0.6421 0.8984 -0.1175 -0.0071 0.0467  99  ASN A N   
696  C CA  . ASN A 94  ? 0.5905 0.6444 0.8698 -0.0892 -0.0106 0.0462  99  ASN A CA  
697  C C   . ASN A 94  ? 0.5999 0.7008 0.8949 -0.0793 -0.0191 0.0331  99  ASN A C   
698  O O   . ASN A 94  ? 0.5778 0.7156 0.9044 -0.0936 -0.0208 0.0258  99  ASN A O   
699  C CB  . ASN A 94  ? 0.6338 0.6825 0.8925 -0.0797 0.0026  0.0638  99  ASN A CB  
700  C CG  . ASN A 94  ? 0.6266 0.7209 0.9002 -0.0851 0.0181  0.0708  99  ASN A CG  
701  O OD1 . ASN A 94  ? 0.6827 0.8231 0.9767 -0.0786 0.0160  0.0602  99  ASN A OD1 
702  N ND2 . ASN A 94  ? 0.7081 0.7898 0.9678 -0.0933 0.0343  0.0895  99  ASN A ND2 
703  N N   . LEU A 95  ? 0.5509 0.6492 0.8245 -0.0553 -0.0256 0.0302  100 LEU A N   
704  C CA  . LEU A 95  ? 0.5342 0.6629 0.8127 -0.0399 -0.0367 0.0193  100 LEU A CA  
705  C C   . LEU A 95  ? 0.5965 0.7790 0.9014 -0.0367 -0.0293 0.0193  100 LEU A C   
706  O O   . LEU A 95  ? 0.6448 0.8645 0.9732 -0.0344 -0.0395 0.0085  100 LEU A O   
707  C CB  . LEU A 95  ? 0.5654 0.6698 0.8112 -0.0174 -0.0430 0.0192  100 LEU A CB  
708  C CG  . LEU A 95  ? 0.5085 0.6286 0.7485 0.0023  -0.0555 0.0110  100 LEU A CG  
709  C CD1 . LEU A 95  ? 0.5080 0.6369 0.7563 -0.0027 -0.0702 0.0006  100 LEU A CD1 
710  C CD2 . LEU A 95  ? 0.5452 0.6288 0.7506 0.0170  -0.0596 0.0132  100 LEU A CD2 
711  N N   . MET A 96  ? 0.6253 0.8149 0.9260 -0.0354 -0.0118 0.0306  101 MET A N   
712  C CA  . MET A 96  ? 0.6073 0.8533 0.9330 -0.0311 0.0007  0.0304  101 MET A CA  
713  C C   . MET A 96  ? 0.6034 0.8939 0.9765 -0.0584 0.0066  0.0287  101 MET A C   
714  O O   . MET A 96  ? 0.7009 1.0513 1.1087 -0.0528 0.0064  0.0198  101 MET A O   
715  C CB  . MET A 96  ? 0.6677 0.9075 0.9697 -0.0247 0.0203  0.0433  101 MET A CB  
716  C CG  . MET A 96  ? 0.7878 1.0848 1.1059 -0.0113 0.0353  0.0406  101 MET A CG  
717  S SD  . MET A 96  ? 0.8629 1.1870 1.1852 0.0264  0.0189  0.0213  101 MET A SD  
718  C CE  . MET A 96  ? 0.8541 1.1070 1.1166 0.0479  0.0066  0.0215  101 MET A CE  
719  N N   . HIS A 97  ? 0.5802 0.8412 0.9564 -0.0874 0.0108  0.0360  102 HIS A N   
720  C CA  . HIS A 97  ? 0.6107 0.9023 1.0311 -0.1199 0.0124  0.0321  102 HIS A CA  
721  C C   . HIS A 97  ? 0.6201 0.9420 1.0663 -0.1168 -0.0120 0.0112  102 HIS A C   
722  O O   . HIS A 97  ? 0.6602 1.0435 1.1535 -0.1294 -0.0131 0.0030  102 HIS A O   
723  C CB  . HIS A 97  ? 0.6659 0.8993 1.0743 -0.1482 0.0162  0.0417  102 HIS A CB  
724  C CG  . HIS A 97  ? 0.7074 0.9619 1.1579 -0.1870 0.0193  0.0389  102 HIS A CG  
725  N ND1 . HIS A 97  ? 0.7772 1.0162 1.2407 -0.2030 -0.0007 0.0222  102 HIS A ND1 
726  C CD2 . HIS A 97  ? 0.6950 0.9854 1.1775 -0.2152 0.0403  0.0498  102 HIS A CD2 
727  C CE1 . HIS A 97  ? 0.7606 1.0228 1.2640 -0.2405 0.0053  0.0216  102 HIS A CE1 
728  N NE2 . HIS A 97  ? 0.7548 1.0499 1.2725 -0.2500 0.0313  0.0394  102 HIS A NE2 
729  N N   . VAL A 98  ? 0.6493 0.9311 1.0637 -0.0997 -0.0311 0.0032  103 VAL A N   
730  C CA  . VAL A 98  ? 0.6964 0.9969 1.1200 -0.0923 -0.0562 -0.0148 103 VAL A CA  
731  C C   . VAL A 98  ? 0.7057 1.0608 1.1442 -0.0636 -0.0637 -0.0210 103 VAL A C   
732  O O   . VAL A 98  ? 0.6593 1.0648 1.1321 -0.0647 -0.0792 -0.0341 103 VAL A O   
733  C CB  . VAL A 98  ? 0.7581 0.9974 1.1364 -0.0824 -0.0699 -0.0190 103 VAL A CB  
734  C CG1 . VAL A 98  ? 0.7098 0.9633 1.0838 -0.0703 -0.0953 -0.0347 103 VAL A CG1 
735  C CG2 . VAL A 98  ? 0.8288 1.0217 1.2005 -0.1082 -0.0655 -0.0182 103 VAL A CG2 
736  N N   . LEU A 99  ? 0.6825 1.0265 1.0951 -0.0371 -0.0546 -0.0130 104 LEU A N   
737  C CA  . LEU A 99  ? 0.6924 1.0785 1.1138 -0.0050 -0.0600 -0.0190 104 LEU A CA  
738  C C   . LEU A 99  ? 0.7242 1.1909 1.2007 -0.0096 -0.0464 -0.0220 104 LEU A C   
739  O O   . LEU A 99  ? 0.7943 1.3151 1.3004 0.0091  -0.0597 -0.0338 104 LEU A O   
740  C CB  . LEU A 99  ? 0.6457 0.9926 1.0234 0.0214  -0.0524 -0.0116 104 LEU A CB  
741  C CG  . LEU A 99  ? 0.6291 0.9070 0.9570 0.0296  -0.0652 -0.0093 104 LEU A CG  
742  C CD1 . LEU A 99  ? 0.6383 0.8819 0.9309 0.0463  -0.0548 -0.0021 104 LEU A CD1 
743  C CD2 . LEU A 99  ? 0.6707 0.9455 0.9873 0.0488  -0.0899 -0.0183 104 LEU A CD2 
744  N N   . LYS A 100 ? 0.6858 1.1610 1.1750 -0.0336 -0.0200 -0.0105 105 LYS A N   
745  C CA  . LYS A 100 ? 0.6673 1.2222 1.2112 -0.0460 -0.0007 -0.0110 105 LYS A CA  
746  C C   . LYS A 100 ? 0.6640 1.2669 1.2655 -0.0813 -0.0086 -0.0194 105 LYS A C   
747  O O   . LYS A 100 ? 0.7720 1.4521 1.4283 -0.0937 0.0061  -0.0216 105 LYS A O   
748  C CB  . LYS A 100 ? 0.7103 1.2545 1.2386 -0.0586 0.0333  0.0073  105 LYS A CB  
749  C CG  . LYS A 100 ? 0.7763 1.3153 1.2691 -0.0207 0.0443  0.0091  105 LYS A CG  
750  C CD  . LYS A 100 ? 0.8085 1.3398 1.2801 -0.0324 0.0770  0.0268  105 LYS A CD  
751  C CE  . LYS A 100 ? 0.8040 1.3343 1.2393 0.0062  0.0867  0.0240  105 LYS A CE  
752  N NZ  . LYS A 100 ? 0.8148 1.3278 1.2154 -0.0020 0.1145  0.0409  105 LYS A NZ  
753  N N   . ALA A 101 ? 0.6954 1.2571 1.2866 -0.0982 -0.0309 -0.0258 106 ALA A N   
754  C CA  . ALA A 101 ? 0.7777 1.3783 1.4192 -0.1323 -0.0440 -0.0381 106 ALA A CA  
755  C C   . ALA A 101 ? 0.8648 1.5511 1.5560 -0.1146 -0.0653 -0.0569 106 ALA A C   
756  O O   . ALA A 101 ? 0.8388 1.5296 1.5099 -0.0716 -0.0797 -0.0620 106 ALA A O   
757  C CB  . ALA A 101 ? 0.7865 1.3164 1.3944 -0.1473 -0.0644 -0.0440 106 ALA A CB  
758  N N   . GLU A 102 ? 0.9486 1.6997 1.7043 -0.1485 -0.0684 -0.0668 107 GLU A N   
759  C CA  . GLU A 102 ? 1.0307 1.8816 1.8495 -0.1362 -0.0884 -0.0856 107 GLU A CA  
760  C C   . GLU A 102 ? 1.1418 1.9792 1.9360 -0.1057 -0.1314 -0.1019 107 GLU A C   
761  O O   . GLU A 102 ? 1.1573 2.0517 1.9720 -0.0681 -0.1477 -0.1112 107 GLU A O   
762  C CB  . GLU A 102 ? 0.9332 1.8531 1.8284 -0.1874 -0.0848 -0.0937 107 GLU A CB  
763  C CG  . GLU A 102 ? 0.9743 1.9285 1.9060 -0.2211 -0.0420 -0.0777 107 GLU A CG  
764  C CD  . GLU A 102 ? 0.9915 2.0179 2.0040 -0.2753 -0.0403 -0.0866 107 GLU A CD  
765  O OE1 . GLU A 102 ? 1.0087 1.9989 2.0218 -0.3094 -0.0628 -0.0970 107 GLU A OE1 
766  O OE2 . GLU A 102 ? 0.9883 2.1085 2.0641 -0.2851 -0.0152 -0.0842 107 GLU A OE2 
767  N N   . MET A 103 ? 1.2294 1.9900 1.9763 -0.1196 -0.1485 -0.1046 108 MET A N   
768  C CA  . MET A 103 ? 1.2152 1.9432 1.9173 -0.0898 -0.1841 -0.1150 108 MET A CA  
769  C C   . MET A 103 ? 1.2038 1.8693 1.8396 -0.0485 -0.1764 -0.1005 108 MET A C   
770  O O   . MET A 103 ? 1.0149 1.6105 1.6080 -0.0568 -0.1553 -0.0865 108 MET A O   
771  C CB  . MET A 103 ? 1.2143 1.8832 1.8861 -0.1191 -0.2007 -0.1243 108 MET A CB  
772  C CG  . MET A 103 ? 1.2156 1.8750 1.8540 -0.0959 -0.2405 -0.1394 108 MET A CG  
773  S SD  . MET A 103 ? 1.3853 2.1485 2.0901 -0.0969 -0.2791 -0.1641 108 MET A SD  
774  C CE  . MET A 103 ? 1.4163 2.1345 2.0456 -0.0581 -0.3204 -0.1720 108 MET A CE  
775  N N   . SER A 104 ? 1.3160 2.0059 1.9444 -0.0047 -0.1952 -0.1044 109 SER A N   
776  C CA  . SER A 104 ? 1.2498 1.8789 1.8158 0.0342  -0.1921 -0.0923 109 SER A CA  
777  C C   . SER A 104 ? 1.1742 1.7210 1.6708 0.0359  -0.2093 -0.0903 109 SER A C   
778  O O   . SER A 104 ? 1.2780 1.8332 1.7692 0.0359  -0.2387 -0.1021 109 SER A O   
779  C CB  . SER A 104 ? 1.1691 1.8465 1.7496 0.0815  -0.2082 -0.0976 109 SER A CB  
780  O OG  . SER A 104 ? 1.2031 1.9199 1.8002 0.0917  -0.2452 -0.1119 109 SER A OG  
781  N N   . THR A 105 ? 0.9229 1.3955 1.3671 0.0381  -0.1911 -0.0761 110 THR A N   
782  C CA  . THR A 105 ? 0.8527 1.2501 1.2333 0.0370  -0.1997 -0.0726 110 THR A CA  
783  C C   . THR A 105 ? 0.7353 1.1099 1.0716 0.0761  -0.2210 -0.0694 110 THR A C   
784  O O   . THR A 105 ? 0.6806 1.0484 1.0083 0.1026  -0.2141 -0.0613 110 THR A O   
785  C CB  . THR A 105 ? 0.7897 1.1257 1.1393 0.0249  -0.1719 -0.0588 110 THR A CB  
786  O OG1 . THR A 105 ? 0.7823 1.1374 1.1706 -0.0058 -0.1517 -0.0580 110 THR A OG1 
787  C CG2 . THR A 105 ? 0.7637 1.0355 1.0610 0.0171  -0.1761 -0.0577 110 THR A CG2 
788  N N   . PRO A 106 ? 0.7403 1.0958 1.0419 0.0799  -0.2466 -0.0752 111 PRO A N   
789  C CA  . PRO A 106 ? 0.7405 1.0675 0.9933 0.1168  -0.2676 -0.0686 111 PRO A CA  
790  C C   . PRO A 106 ? 0.7012 0.9493 0.8935 0.1259  -0.2517 -0.0510 111 PRO A C   
791  O O   . PRO A 106 ? 0.7869 0.9993 0.9674 0.1024  -0.2283 -0.0456 111 PRO A O   
792  C CB  . PRO A 106 ? 0.7220 1.0461 0.9476 0.1120  -0.2960 -0.0786 111 PRO A CB  
793  C CG  . PRO A 106 ? 0.7158 1.0293 0.9496 0.0722  -0.2819 -0.0868 111 PRO A CG  
794  C CD  . PRO A 106 ? 0.7161 1.0671 1.0130 0.0518  -0.2575 -0.0876 111 PRO A CD  
795  N N   . LEU A 107 ? 0.7142 0.9365 0.8707 0.1601  -0.2661 -0.0425 112 LEU A N   
796  C CA  . LEU A 107 ? 0.7430 0.8896 0.8424 0.1692  -0.2547 -0.0258 112 LEU A CA  
797  C C   . LEU A 107 ? 0.7640 0.8543 0.8131 0.1452  -0.2452 -0.0184 112 LEU A C   
798  O O   . LEU A 107 ? 0.7822 0.8295 0.8122 0.1341  -0.2235 -0.0087 112 LEU A O   
799  C CB  . LEU A 107 ? 0.7714 0.8931 0.8345 0.2099  -0.2782 -0.0183 112 LEU A CB  
800  C CG  . LEU A 107 ? 0.8250 0.8612 0.8241 0.2204  -0.2718 -0.0002 112 LEU A CG  
801  C CD1 . LEU A 107 ? 0.7947 0.8127 0.8079 0.2101  -0.2441 0.0024  112 LEU A CD1 
802  C CD2 . LEU A 107 ? 0.9120 0.9284 0.8833 0.2645  -0.2984 0.0053  112 LEU A CD2 
803  N N   . SER A 108 ? 0.8507 0.9461 0.8800 0.1382  -0.2617 -0.0249 113 SER A N   
804  C CA  . SER A 108 ? 0.8686 0.9179 0.8492 0.1177  -0.2515 -0.0210 113 SER A CA  
805  C C   . SER A 108 ? 0.8143 0.8651 0.8230 0.0869  -0.2238 -0.0262 113 SER A C   
806  O O   . SER A 108 ? 0.8950 0.9027 0.8731 0.0756  -0.2043 -0.0173 113 SER A O   
807  C CB  . SER A 108 ? 0.9149 0.9741 0.8676 0.1185  -0.2762 -0.0309 113 SER A CB  
808  O OG  . SER A 108 ? 0.9992 1.1203 1.0085 0.1069  -0.2875 -0.0514 113 SER A OG  
809  N N   . VAL A 109 ? 0.7374 0.8379 0.8049 0.0739  -0.2220 -0.0394 114 VAL A N   
810  C CA  . VAL A 109 ? 0.7469 0.8459 0.8425 0.0478  -0.1974 -0.0423 114 VAL A CA  
811  C C   . VAL A 109 ? 0.7446 0.8261 0.8475 0.0515  -0.1761 -0.0289 114 VAL A C   
812  O O   . VAL A 109 ? 0.8412 0.8924 0.9330 0.0382  -0.1573 -0.0241 114 VAL A O   
813  C CB  . VAL A 109 ? 0.7671 0.9168 0.9197 0.0299  -0.2007 -0.0573 114 VAL A CB  
814  C CG1 . VAL A 109 ? 0.7390 0.8766 0.9142 0.0059  -0.1755 -0.0564 114 VAL A CG1 
815  C CG2 . VAL A 109 ? 0.7845 0.9465 0.9276 0.0218  -0.2231 -0.0742 114 VAL A CG2 
816  N N   . LYS A 110 ? 0.7068 0.8086 0.8276 0.0712  -0.1805 -0.0251 115 LYS A N   
817  C CA  . LYS A 110 ? 0.6999 0.7816 0.8200 0.0777  -0.1638 -0.0149 115 LYS A CA  
818  C C   . LYS A 110 ? 0.7098 0.7305 0.7788 0.0796  -0.1581 -0.0030 115 LYS A C   
819  O O   . LYS A 110 ? 0.7195 0.7194 0.7880 0.0705  -0.1412 0.0025  115 LYS A O   
820  C CB  . LYS A 110 ? 0.6936 0.8050 0.8344 0.1038  -0.1711 -0.0160 115 LYS A CB  
821  C CG  . LYS A 110 ? 0.6702 0.8470 0.8705 0.0965  -0.1658 -0.0252 115 LYS A CG  
822  C CD  . LYS A 110 ? 0.6684 0.8831 0.8922 0.1253  -0.1701 -0.0284 115 LYS A CD  
823  C CE  . LYS A 110 ? 0.6628 0.9449 0.9470 0.1122  -0.1571 -0.0353 115 LYS A CE  
824  N NZ  . LYS A 110 ? 0.7159 1.0457 1.0284 0.1414  -0.1574 -0.0406 115 LYS A NZ  
825  N N   . GLY A 111 ? 0.7275 0.7211 0.7535 0.0908  -0.1731 0.0016  116 GLY A N   
826  C CA  . GLY A 111 ? 0.7189 0.6546 0.6935 0.0866  -0.1663 0.0144  116 GLY A CA  
827  C C   . GLY A 111 ? 0.7167 0.6430 0.6888 0.0602  -0.1471 0.0134  116 GLY A C   
828  O O   . GLY A 111 ? 0.6780 0.5773 0.6411 0.0499  -0.1313 0.0210  116 GLY A O   
829  N N   . ARG A 112 ? 0.7696 0.7202 0.7524 0.0501  -0.1496 0.0019  117 ARG A N   
830  C CA  . ARG A 112 ? 0.7484 0.6927 0.7317 0.0296  -0.1321 -0.0030 117 ARG A CA  
831  C C   . ARG A 112 ? 0.6811 0.6361 0.7052 0.0191  -0.1154 -0.0038 117 ARG A C   
832  O O   . ARG A 112 ? 0.6728 0.6114 0.6924 0.0090  -0.0991 -0.0007 117 ARG A O   
833  C CB  . ARG A 112 ? 0.7678 0.7311 0.7521 0.0232  -0.1415 -0.0186 117 ARG A CB  
834  C CG  . ARG A 112 ? 0.7856 0.7321 0.7509 0.0092  -0.1259 -0.0249 117 ARG A CG  
835  C CD  . ARG A 112 ? 0.8427 0.8036 0.8083 0.0032  -0.1373 -0.0444 117 ARG A CD  
836  N NE  . ARG A 112 ? 0.7993 0.7894 0.8182 -0.0050 -0.1422 -0.0545 117 ARG A NE  
837  C CZ  . ARG A 112 ? 0.8131 0.8204 0.8457 -0.0138 -0.1560 -0.0724 117 ARG A CZ  
838  N NH1 . ARG A 112 ? 0.9638 0.9631 0.9582 -0.0131 -0.1689 -0.0854 117 ARG A NH1 
839  N NH2 . ARG A 112 ? 0.8322 0.8639 0.9155 -0.0254 -0.1566 -0.0775 117 ARG A NH2 
840  N N   . ILE A 113 ? 0.5918 0.5766 0.6546 0.0224  -0.1194 -0.0074 118 ILE A N   
841  C CA  . ILE A 113 ? 0.5340 0.5268 0.6287 0.0153  -0.1052 -0.0053 118 ILE A CA  
842  C C   . ILE A 113 ? 0.5563 0.5231 0.6361 0.0190  -0.0966 0.0053  118 ILE A C   
843  O O   . ILE A 113 ? 0.6173 0.5759 0.7041 0.0094  -0.0842 0.0071  118 ILE A O   
844  C CB  . ILE A 113 ? 0.5385 0.5692 0.6707 0.0191  -0.1089 -0.0083 118 ILE A CB  
845  C CG1 . ILE A 113 ? 0.5382 0.5943 0.6948 0.0051  -0.1140 -0.0198 118 ILE A CG1 
846  C CG2 . ILE A 113 ? 0.5460 0.5787 0.6970 0.0165  -0.0944 -0.0019 118 ILE A CG2 
847  C CD1 . ILE A 113 ? 0.5702 0.6726 0.7682 0.0038  -0.1180 -0.0239 118 ILE A CD1 
848  N N   . ILE A 114 ? 0.5954 0.5486 0.6551 0.0337  -0.1053 0.0109  119 ILE A N   
849  C CA  . ILE A 114 ? 0.5941 0.5162 0.6361 0.0360  -0.1008 0.0191  119 ILE A CA  
850  C C   . ILE A 114 ? 0.6101 0.5065 0.6315 0.0204  -0.0909 0.0240  119 ILE A C   
851  O O   . ILE A 114 ? 0.6818 0.5714 0.7116 0.0111  -0.0813 0.0262  119 ILE A O   
852  C CB  . ILE A 114 ? 0.6518 0.5534 0.6691 0.0565  -0.1145 0.0231  119 ILE A CB  
853  C CG1 . ILE A 114 ? 0.6438 0.5787 0.6892 0.0738  -0.1194 0.0166  119 ILE A CG1 
854  C CG2 . ILE A 114 ? 0.7403 0.5966 0.7310 0.0545  -0.1117 0.0308  119 ILE A CG2 
855  C CD1 . ILE A 114 ? 0.6952 0.6260 0.7258 0.1005  -0.1363 0.0161  119 ILE A CD1 
856  N N   . LEU A 115 ? 0.6113 0.4976 0.6058 0.0180  -0.0933 0.0251  120 LEU A N   
857  C CA  . LEU A 115 ? 0.6348 0.5042 0.6094 0.0028  -0.0799 0.0292  120 LEU A CA  
858  C C   . LEU A 115 ? 0.6513 0.5437 0.6577 -0.0088 -0.0656 0.0211  120 LEU A C   
859  O O   . LEU A 115 ? 0.6475 0.5365 0.6599 -0.0195 -0.0530 0.0240  120 LEU A O   
860  C CB  . LEU A 115 ? 0.6650 0.5222 0.5992 0.0044  -0.0845 0.0308  120 LEU A CB  
861  C CG  . LEU A 115 ? 0.6791 0.5205 0.5840 -0.0104 -0.0676 0.0359  120 LEU A CG  
862  C CD1 . LEU A 115 ? 0.7325 0.5469 0.6268 -0.0223 -0.0570 0.0495  120 LEU A CD1 
863  C CD2 . LEU A 115 ? 0.7337 0.5589 0.5882 -0.0041 -0.0762 0.0391  120 LEU A CD2 
864  N N   . GLU A 116 ? 0.6798 0.5952 0.7085 -0.0065 -0.0688 0.0108  121 GLU A N   
865  C CA  . GLU A 116 ? 0.6603 0.5896 0.7172 -0.0137 -0.0576 0.0033  121 GLU A CA  
866  C C   . GLU A 116 ? 0.6563 0.5909 0.7403 -0.0141 -0.0533 0.0078  121 GLU A C   
867  O O   . GLU A 116 ? 0.7684 0.7072 0.8668 -0.0189 -0.0433 0.0062  121 GLU A O   
868  C CB  . GLU A 116 ? 0.6885 0.6316 0.7596 -0.0137 -0.0635 -0.0081 121 GLU A CB  
869  C CG  . GLU A 116 ? 0.7364 0.6741 0.7798 -0.0153 -0.0658 -0.0176 121 GLU A CG  
870  C CD  . GLU A 116 ? 0.8023 0.7508 0.8592 -0.0184 -0.0749 -0.0319 121 GLU A CD  
871  O OE1 . GLU A 116 ? 0.7651 0.7272 0.8542 -0.0209 -0.0794 -0.0322 121 GLU A OE1 
872  O OE2 . GLU A 116 ? 0.8826 0.8249 0.9153 -0.0199 -0.0772 -0.0435 121 GLU A OE2 
873  N N   . ILE A 117 ? 0.6156 0.5523 0.7054 -0.0071 -0.0615 0.0123  122 ILE A N   
874  C CA  . ILE A 117 ? 0.5219 0.4599 0.6266 -0.0059 -0.0595 0.0165  122 ILE A CA  
875  C C   . ILE A 117 ? 0.5539 0.4776 0.6491 -0.0126 -0.0557 0.0206  122 ILE A C   
876  O O   . ILE A 117 ? 0.6092 0.5406 0.7221 -0.0166 -0.0517 0.0203  122 ILE A O   
877  C CB  . ILE A 117 ? 0.5185 0.4608 0.6238 0.0052  -0.0672 0.0186  122 ILE A CB  
878  C CG1 . ILE A 117 ? 0.5344 0.5006 0.6610 0.0063  -0.0670 0.0154  122 ILE A CG1 
879  C CG2 . ILE A 117 ? 0.5520 0.4898 0.6604 0.0075  -0.0666 0.0215  122 ILE A CG2 
880  C CD1 . ILE A 117 ? 0.5263 0.5090 0.6572 0.0181  -0.0722 0.0153  122 ILE A CD1 
881  N N   . ILE A 118 ? 0.5777 0.4804 0.6452 -0.0146 -0.0581 0.0249  123 ILE A N   
882  C CA  . ILE A 118 ? 0.5989 0.4847 0.6561 -0.0269 -0.0533 0.0300  123 ILE A CA  
883  C C   . ILE A 118 ? 0.5935 0.4982 0.6669 -0.0392 -0.0386 0.0273  123 ILE A C   
884  O O   . ILE A 118 ? 0.6363 0.5515 0.7300 -0.0480 -0.0346 0.0268  123 ILE A O   
885  C CB  . ILE A 118 ? 0.6611 0.5118 0.6780 -0.0275 -0.0577 0.0382  123 ILE A CB  
886  C CG1 . ILE A 118 ? 0.6902 0.5205 0.6943 -0.0117 -0.0726 0.0391  123 ILE A CG1 
887  C CG2 . ILE A 118 ? 0.6947 0.5264 0.6995 -0.0475 -0.0484 0.0454  123 ILE A CG2 
888  C CD1 . ILE A 118 ? 0.7313 0.5326 0.6975 -0.0008 -0.0821 0.0455  123 ILE A CD1 
889  N N   . GLU A 119 ? 0.6268 0.5375 0.6908 -0.0385 -0.0319 0.0237  124 GLU A N   
890  C CA  . GLU A 119 ? 0.6957 0.6264 0.7729 -0.0450 -0.0159 0.0177  124 GLU A CA  
891  C C   . GLU A 119 ? 0.6909 0.6460 0.8094 -0.0406 -0.0146 0.0112  124 GLU A C   
892  O O   . GLU A 119 ? 0.6357 0.6102 0.7764 -0.0469 -0.0055 0.0096  124 GLU A O   
893  C CB  . GLU A 119 ? 0.7335 0.6642 0.7918 -0.0396 -0.0129 0.0100  124 GLU A CB  
894  C CG  . GLU A 119 ? 0.7767 0.6871 0.7883 -0.0440 -0.0105 0.0162  124 GLU A CG  
895  C CD  . GLU A 119 ? 0.8804 0.7904 0.8686 -0.0371 -0.0130 0.0060  124 GLU A CD  
896  O OE1 . GLU A 119 ? 0.8537 0.7762 0.8631 -0.0308 -0.0166 -0.0071 124 GLU A OE1 
897  O OE2 . GLU A 119 ? 1.0236 0.9167 0.9674 -0.0388 -0.0123 0.0114  124 GLU A OE2 
898  N N   . GLY A 120 ? 0.6529 0.6077 0.7814 -0.0298 -0.0242 0.0085  125 GLY A N   
899  C CA  . GLY A 120 ? 0.6316 0.5999 0.7902 -0.0230 -0.0256 0.0057  125 GLY A CA  
900  C C   . GLY A 120 ? 0.6119 0.5881 0.7859 -0.0247 -0.0310 0.0104  125 GLY A C   
901  O O   . GLY A 120 ? 0.6871 0.6827 0.8868 -0.0226 -0.0286 0.0073  125 GLY A O   
902  N N   . MET A 121 ? 0.5729 0.5346 0.7310 -0.0268 -0.0399 0.0160  126 MET A N   
903  C CA  . MET A 121 ? 0.5964 0.5600 0.7618 -0.0303 -0.0477 0.0178  126 MET A CA  
904  C C   . MET A 121 ? 0.5477 0.5214 0.7239 -0.0460 -0.0420 0.0168  126 MET A C   
905  O O   . MET A 121 ? 0.6154 0.6071 0.8146 -0.0495 -0.0476 0.0142  126 MET A O   
906  C CB  . MET A 121 ? 0.6831 0.6232 0.8238 -0.0268 -0.0579 0.0209  126 MET A CB  
907  C CG  . MET A 121 ? 0.6746 0.6157 0.8126 -0.0127 -0.0626 0.0220  126 MET A CG  
908  S SD  . MET A 121 ? 0.6520 0.6094 0.8091 -0.0054 -0.0661 0.0231  126 MET A SD  
909  C CE  . MET A 121 ? 0.7055 0.6650 0.8657 -0.0115 -0.0770 0.0197  126 MET A CE  
910  N N   . ALA A 122 ? 0.5765 0.5406 0.7356 -0.0565 -0.0314 0.0192  127 ALA A N   
911  C CA  . ALA A 122 ? 0.6205 0.5974 0.7902 -0.0758 -0.0202 0.0201  127 ALA A CA  
912  C C   . ALA A 122 ? 0.5737 0.5950 0.7835 -0.0735 -0.0095 0.0123  127 ALA A C   
913  O O   . ALA A 122 ? 0.5513 0.6003 0.7911 -0.0855 -0.0072 0.0099  127 ALA A O   
914  C CB  . ALA A 122 ? 0.6781 0.6318 0.8126 -0.0861 -0.0090 0.0270  127 ALA A CB  
915  N N   . TYR A 123 ? 0.5703 0.5982 0.7824 -0.0573 -0.0045 0.0069  128 TYR A N   
916  C CA  . TYR A 123 ? 0.5400 0.6041 0.7882 -0.0475 0.0036  -0.0024 128 TYR A CA  
917  C C   . TYR A 123 ? 0.5670 0.6514 0.8489 -0.0388 -0.0113 -0.0040 128 TYR A C   
918  O O   . TYR A 123 ? 0.5858 0.7100 0.9054 -0.0405 -0.0078 -0.0095 128 TYR A O   
919  C CB  . TYR A 123 ? 0.5116 0.5654 0.7494 -0.0310 0.0083  -0.0092 128 TYR A CB  
920  C CG  . TYR A 123 ? 0.5381 0.6183 0.8101 -0.0141 0.0128  -0.0196 128 TYR A CG  
921  C CD1 . TYR A 123 ? 0.5091 0.6219 0.7991 -0.0139 0.0320  -0.0292 128 TYR A CD1 
922  C CD2 . TYR A 123 ? 0.5129 0.5849 0.7978 0.0033  -0.0016 -0.0193 128 TYR A CD2 
923  C CE1 . TYR A 123 ? 0.5262 0.6641 0.8495 0.0069  0.0354  -0.0407 128 TYR A CE1 
924  C CE2 . TYR A 123 ? 0.5214 0.6109 0.8349 0.0228  0.0002  -0.0281 128 TYR A CE2 
925  C CZ  . TYR A 123 ? 0.5188 0.6421 0.8532 0.0264  0.0179  -0.0400 128 TYR A CZ  
926  O OH  . TYR A 123 ? 0.5275 0.6692 0.8915 0.0503  0.0196  -0.0507 128 TYR A OH  
927  N N   . LEU A 124 ? 0.5669 0.6277 0.8348 -0.0290 -0.0276 0.0006  129 LEU A N   
928  C CA  . LEU A 124 ? 0.5190 0.5918 0.8066 -0.0177 -0.0440 0.0010  129 LEU A CA  
929  C C   . LEU A 124 ? 0.5205 0.6135 0.8252 -0.0314 -0.0536 -0.0004 129 LEU A C   
930  O O   . LEU A 124 ? 0.6165 0.7446 0.9563 -0.0255 -0.0616 -0.0053 129 LEU A O   
931  C CB  . LEU A 124 ? 0.5130 0.5546 0.7738 -0.0074 -0.0553 0.0080  129 LEU A CB  
932  C CG  . LEU A 124 ? 0.5039 0.5266 0.7543 0.0045  -0.0500 0.0095  129 LEU A CG  
933  C CD1 . LEU A 124 ? 0.4964 0.4952 0.7224 0.0077  -0.0578 0.0179  129 LEU A CD1 
934  C CD2 . LEU A 124 ? 0.4757 0.5086 0.7493 0.0213  -0.0504 0.0064  129 LEU A CD2 
935  N N   . HIS A 125 ? 0.5963 0.6670 0.8777 -0.0495 -0.0544 0.0028  130 HIS A N   
936  C CA  . HIS A 125 ? 0.5881 0.6705 0.8834 -0.0692 -0.0629 -0.0001 130 HIS A CA  
937  C C   . HIS A 125 ? 0.5238 0.6524 0.8614 -0.0846 -0.0500 -0.0052 130 HIS A C   
938  O O   . HIS A 125 ? 0.5675 0.7319 0.9413 -0.0910 -0.0609 -0.0116 130 HIS A O   
939  C CB  . HIS A 125 ? 0.6116 0.6493 0.8682 -0.0845 -0.0648 0.0045  130 HIS A CB  
940  C CG  . HIS A 125 ? 0.6704 0.6743 0.8942 -0.0696 -0.0796 0.0060  130 HIS A CG  
941  N ND1 . HIS A 125 ? 0.7566 0.7191 0.9458 -0.0759 -0.0857 0.0072  130 HIS A ND1 
942  C CD2 . HIS A 125 ? 0.6844 0.6898 0.9034 -0.0482 -0.0880 0.0065  130 HIS A CD2 
943  C CE1 . HIS A 125 ? 0.7285 0.6750 0.8960 -0.0575 -0.0958 0.0066  130 HIS A CE1 
944  N NE2 . HIS A 125 ? 0.6906 0.6630 0.8748 -0.0426 -0.0964 0.0073  130 HIS A NE2 
945  N N   . GLY A 126 ? 0.5038 0.6358 0.8373 -0.0891 -0.0270 -0.0035 131 GLY A N   
946  C CA  . GLY A 126 ? 0.5097 0.6928 0.8834 -0.0987 -0.0079 -0.0091 131 GLY A CA  
947  C C   . GLY A 126 ? 0.5387 0.7747 0.9627 -0.0775 -0.0120 -0.0194 131 GLY A C   
948  O O   . GLY A 126 ? 0.5431 0.8354 1.0154 -0.0873 -0.0042 -0.0263 131 GLY A O   
949  N N   . LYS A 127 ? 0.5362 0.7547 0.9499 -0.0486 -0.0242 -0.0197 132 LYS A N   
950  C CA  . LYS A 127 ? 0.5273 0.7809 0.9792 -0.0221 -0.0344 -0.0269 132 LYS A CA  
951  C C   . LYS A 127 ? 0.5925 0.8550 1.0571 -0.0162 -0.0642 -0.0261 132 LYS A C   
952  O O   . LYS A 127 ? 0.6863 0.9663 1.1712 0.0101  -0.0779 -0.0286 132 LYS A O   
953  C CB  . LYS A 127 ? 0.5227 0.7438 0.9515 0.0046  -0.0308 -0.0262 132 LYS A CB  
954  C CG  . LYS A 127 ? 0.5461 0.7704 0.9705 0.0056  -0.0043 -0.0330 132 LYS A CG  
955  C CD  . LYS A 127 ? 0.5810 0.8625 1.0557 0.0208  0.0072  -0.0464 132 LYS A CD  
956  C CE  . LYS A 127 ? 0.6185 0.9049 1.0831 0.0205  0.0363  -0.0552 132 LYS A CE  
957  N NZ  . LYS A 127 ? 0.5565 0.9053 1.0719 0.0360  0.0513  -0.0701 132 LYS A NZ  
958  N N   . GLY A 128 ? 0.6122 0.8605 1.0620 -0.0391 -0.0754 -0.0235 133 GLY A N   
959  C CA  . GLY A 128 ? 0.6006 0.8547 1.0547 -0.0356 -0.1047 -0.0253 133 GLY A CA  
960  C C   . GLY A 128 ? 0.5987 0.8092 1.0100 -0.0128 -0.1207 -0.0175 133 GLY A C   
961  O O   . GLY A 128 ? 0.5839 0.8033 0.9968 -0.0016 -0.1452 -0.0188 133 GLY A O   
962  N N   . VAL A 129 ? 0.5481 0.7141 0.9205 -0.0075 -0.1072 -0.0093 134 VAL A N   
963  C CA  . VAL A 129 ? 0.5395 0.6683 0.8751 0.0119  -0.1154 -0.0003 134 VAL A CA  
964  C C   . VAL A 129 ? 0.5852 0.6758 0.8784 -0.0005 -0.1165 0.0033  134 VAL A C   
965  O O   . VAL A 129 ? 0.5641 0.6345 0.8415 -0.0117 -0.1014 0.0049  134 VAL A O   
966  C CB  . VAL A 129 ? 0.5376 0.6485 0.8669 0.0262  -0.0995 0.0043  134 VAL A CB  
967  C CG1 . VAL A 129 ? 0.5552 0.6270 0.8474 0.0397  -0.1053 0.0157  134 VAL A CG1 
968  C CG2 . VAL A 129 ? 0.5426 0.6871 0.9122 0.0435  -0.0980 -0.0017 134 VAL A CG2 
969  N N   . ILE A 130 ? 0.6255 0.7065 0.8982 0.0045  -0.1354 0.0038  135 ILE A N   
970  C CA  . ILE A 130 ? 0.5632 0.6068 0.7914 0.0020  -0.1368 0.0064  135 ILE A CA  
971  C C   . ILE A 130 ? 0.5276 0.5516 0.7310 0.0205  -0.1316 0.0179  135 ILE A C   
972  O O   . ILE A 130 ? 0.6007 0.6309 0.8051 0.0363  -0.1408 0.0235  135 ILE A O   
973  C CB  . ILE A 130 ? 0.5658 0.6079 0.7803 -0.0026 -0.1585 -0.0018 135 ILE A CB  
974  C CG1 . ILE A 130 ? 0.5754 0.6341 0.8185 -0.0280 -0.1615 -0.0126 135 ILE A CG1 
975  C CG2 . ILE A 130 ? 0.6091 0.6122 0.7752 0.0004  -0.1582 -0.0014 135 ILE A CG2 
976  C CD1 . ILE A 130 ? 0.6768 0.7474 0.9236 -0.0352 -0.1873 -0.0244 135 ILE A CD1 
977  N N   . HIS A 131 ? 0.5330 0.5337 0.7151 0.0179  -0.1174 0.0219  136 HIS A N   
978  C CA  . HIS A 131 ? 0.5720 0.5568 0.7344 0.0290  -0.1095 0.0326  136 HIS A CA  
979  C C   . HIS A 131 ? 0.6241 0.5990 0.7538 0.0397  -0.1191 0.0377  136 HIS A C   
980  O O   . HIS A 131 ? 0.7431 0.7127 0.8631 0.0508  -0.1197 0.0489  136 HIS A O   
981  C CB  . HIS A 131 ? 0.5265 0.4981 0.6795 0.0225  -0.0944 0.0333  136 HIS A CB  
982  C CG  . HIS A 131 ? 0.5630 0.5271 0.7136 0.0269  -0.0835 0.0424  136 HIS A CG  
983  N ND1 . HIS A 131 ? 0.6388 0.5946 0.7699 0.0348  -0.0828 0.0530  136 HIS A ND1 
984  C CD2 . HIS A 131 ? 0.5689 0.5308 0.7326 0.0221  -0.0726 0.0423  136 HIS A CD2 
985  C CE1 . HIS A 131 ? 0.6057 0.5540 0.7419 0.0319  -0.0716 0.0597  136 HIS A CE1 
986  N NE2 . HIS A 131 ? 0.6105 0.5622 0.7668 0.0248  -0.0668 0.0519  136 HIS A NE2 
987  N N   . LYS A 132 ? 0.7261 0.6938 0.8341 0.0367  -0.1257 0.0297  137 LYS A N   
988  C CA  . LYS A 132 ? 0.7966 0.7541 0.8652 0.0475  -0.1339 0.0304  137 LYS A CA  
989  C C   . LYS A 132 ? 0.7429 0.6899 0.7848 0.0545  -0.1169 0.0395  137 LYS A C   
990  O O   . LYS A 132 ? 0.7847 0.7248 0.7909 0.0633  -0.1190 0.0377  137 LYS A O   
991  C CB  . LYS A 132 ? 0.7956 0.7615 0.8581 0.0584  -0.1516 0.0350  137 LYS A CB  
992  C CG  . LYS A 132 ? 0.7967 0.7859 0.8949 0.0532  -0.1694 0.0257  137 LYS A CG  
993  C CD  . LYS A 132 ? 0.9340 0.9352 1.0335 0.0697  -0.1861 0.0335  137 LYS A CD  
994  C CE  . LYS A 132 ? 1.0071 1.0434 1.1574 0.0668  -0.1992 0.0248  137 LYS A CE  
995  N NZ  . LYS A 132 ? 1.0306 1.0754 1.2180 0.0665  -0.1817 0.0292  137 LYS A NZ  
996  N N   . ASP A 133 ? 0.6713 0.6202 0.7313 0.0495  -0.1002 0.0467  138 ASP A N   
997  C CA  . ASP A 133 ? 0.7158 0.6639 0.7627 0.0520  -0.0831 0.0570  138 ASP A CA  
998  C C   . ASP A 133 ? 0.6868 0.6408 0.7598 0.0425  -0.0698 0.0563  138 ASP A C   
999  O O   . ASP A 133 ? 0.7115 0.6669 0.7939 0.0376  -0.0584 0.0660  138 ASP A O   
1000 C CB  . ASP A 133 ? 0.8068 0.7482 0.8409 0.0569  -0.0812 0.0741  138 ASP A CB  
1001 C CG  . ASP A 133 ? 0.9705 0.9124 0.9826 0.0570  -0.0625 0.0863  138 ASP A CG  
1002 O OD1 . ASP A 133 ? 1.0042 0.9567 1.0024 0.0601  -0.0543 0.0793  138 ASP A OD1 
1003 O OD2 . ASP A 133 ? 1.1756 1.1066 1.1845 0.0540  -0.0551 0.1032  138 ASP A OD2 
1004 N N   . LEU A 134 ? 0.6941 0.6484 0.7753 0.0391  -0.0729 0.0445  139 LEU A N   
1005 C CA  . LEU A 134 ? 0.7059 0.6654 0.8048 0.0327  -0.0648 0.0419  139 LEU A CA  
1006 C C   . LEU A 134 ? 0.7127 0.6833 0.8024 0.0391  -0.0553 0.0420  139 LEU A C   
1007 O O   . LEU A 134 ? 0.6578 0.6260 0.7264 0.0498  -0.0578 0.0360  139 LEU A O   
1008 C CB  . LEU A 134 ? 0.7463 0.6972 0.8488 0.0282  -0.0721 0.0322  139 LEU A CB  
1009 C CG  . LEU A 134 ? 0.7509 0.7021 0.8602 0.0250  -0.0679 0.0290  139 LEU A CG  
1010 C CD1 . LEU A 134 ? 0.7073 0.6675 0.8375 0.0169  -0.0610 0.0324  139 LEU A CD1 
1011 C CD2 . LEU A 134 ? 0.6961 0.6299 0.7979 0.0201  -0.0750 0.0233  139 LEU A CD2 
1012 N N   . LYS A 135 ? 0.7007 0.6855 0.8087 0.0326  -0.0448 0.0469  140 LYS A N   
1013 C CA  . LYS A 135 ? 0.6968 0.7050 0.8083 0.0362  -0.0339 0.0469  140 LYS A CA  
1014 C C   . LYS A 135 ? 0.6986 0.7217 0.8398 0.0227  -0.0281 0.0487  140 LYS A C   
1015 O O   . LYS A 135 ? 0.7622 0.7707 0.9132 0.0123  -0.0311 0.0509  140 LYS A O   
1016 C CB  . LYS A 135 ? 0.7836 0.7988 0.8768 0.0402  -0.0230 0.0562  140 LYS A CB  
1017 C CG  . LYS A 135 ? 0.9058 0.9060 0.9961 0.0304  -0.0202 0.0712  140 LYS A CG  
1018 C CD  . LYS A 135 ? 0.9639 0.9649 1.0247 0.0353  -0.0102 0.0830  140 LYS A CD  
1019 C CE  . LYS A 135 ? 0.9770 0.9533 1.0279 0.0291  -0.0114 0.0999  140 LYS A CE  
1020 N NZ  . LYS A 135 ? 1.0772 1.0480 1.0870 0.0370  -0.0053 0.1125  140 LYS A NZ  
1021 N N   . PRO A 136 ? 0.7019 0.7557 0.8589 0.0235  -0.0211 0.0457  141 PRO A N   
1022 C CA  . PRO A 136 ? 0.6918 0.7623 0.8791 0.0080  -0.0192 0.0447  141 PRO A CA  
1023 C C   . PRO A 136 ? 0.6857 0.7455 0.8822 -0.0114 -0.0107 0.0556  141 PRO A C   
1024 O O   . PRO A 136 ? 0.7662 0.8174 0.9780 -0.0242 -0.0152 0.0520  141 PRO A O   
1025 C CB  . PRO A 136 ? 0.6709 0.7857 0.8767 0.0141  -0.0128 0.0397  141 PRO A CB  
1026 C CG  . PRO A 136 ? 0.6606 0.7712 0.8431 0.0383  -0.0176 0.0329  141 PRO A CG  
1027 C CD  . PRO A 136 ? 0.6487 0.7251 0.7996 0.0407  -0.0177 0.0390  141 PRO A CD  
1028 N N   . GLU A 137 ? 0.7146 0.7696 0.8966 -0.0127 0.0008  0.0688  142 GLU A N   
1029 C CA  . GLU A 137 ? 0.7167 0.7468 0.8972 -0.0287 0.0076  0.0832  142 GLU A CA  
1030 C C   . GLU A 137 ? 0.6977 0.6882 0.8724 -0.0276 -0.0048 0.0819  142 GLU A C   
1031 O O   . GLU A 137 ? 0.7142 0.6819 0.8967 -0.0406 -0.0031 0.0869  142 GLU A O   
1032 C CB  . GLU A 137 ? 0.7787 0.8034 0.9314 -0.0254 0.0200  0.1001  142 GLU A CB  
1033 C CG  . GLU A 137 ? 0.8405 0.9026 1.0022 -0.0351 0.0412  0.1072  142 GLU A CG  
1034 C CD  . GLU A 137 ? 0.8232 0.8789 0.9477 -0.0298 0.0550  0.1239  142 GLU A CD  
1035 O OE1 . GLU A 137 ? 0.8321 0.8765 0.9228 -0.0087 0.0470  0.1212  142 GLU A OE1 
1036 O OE2 . GLU A 137 ? 0.8541 0.9154 0.9805 -0.0488 0.0744  0.1403  142 GLU A OE2 
1037 N N   . ASN A 138 ? 0.6084 0.5918 0.7710 -0.0122 -0.0164 0.0743  143 ASN A N   
1038 C CA  . ASN A 138 ? 0.5711 0.5307 0.7342 -0.0085 -0.0267 0.0698  143 ASN A CA  
1039 C C   . ASN A 138 ? 0.5267 0.4917 0.7043 -0.0112 -0.0327 0.0544  143 ASN A C   
1040 O O   . ASN A 138 ? 0.5693 0.5244 0.7459 -0.0060 -0.0390 0.0485  143 ASN A O   
1041 C CB  . ASN A 138 ? 0.6018 0.5553 0.7453 0.0064  -0.0352 0.0714  143 ASN A CB  
1042 C CG  . ASN A 138 ? 0.6852 0.6203 0.8106 0.0114  -0.0352 0.0866  143 ASN A CG  
1043 O OD1 . ASN A 138 ? 0.7237 0.6399 0.8509 0.0047  -0.0298 0.0971  143 ASN A OD1 
1044 N ND2 . ASN A 138 ? 0.7779 0.7142 0.8823 0.0237  -0.0433 0.0877  143 ASN A ND2 
1045 N N   . ILE A 139 ? 0.5358 0.5195 0.7263 -0.0192 -0.0307 0.0483  144 ILE A N   
1046 C CA  . ILE A 139 ? 0.5331 0.5209 0.7301 -0.0213 -0.0376 0.0352  144 ILE A CA  
1047 C C   . ILE A 139 ? 0.5530 0.5448 0.7684 -0.0374 -0.0355 0.0317  144 ILE A C   
1048 O O   . ILE A 139 ? 0.5345 0.5538 0.7645 -0.0438 -0.0332 0.0315  144 ILE A O   
1049 C CB  . ILE A 139 ? 0.5351 0.5422 0.7259 -0.0115 -0.0429 0.0298  144 ILE A CB  
1050 C CG1 . ILE A 139 ? 0.4805 0.4746 0.6517 0.0002  -0.0463 0.0317  144 ILE A CG1 
1051 C CG2 . ILE A 139 ? 0.5715 0.5814 0.7632 -0.0137 -0.0511 0.0189  144 ILE A CG2 
1052 C CD1 . ILE A 139 ? 0.5515 0.5538 0.7112 0.0121  -0.0508 0.0285  144 ILE A CD1 
1053 N N   . LEU A 140 ? 0.5607 0.5266 0.7772 -0.0438 -0.0367 0.0272  145 LEU A N   
1054 C CA  . LEU A 140 ? 0.5602 0.5193 0.7915 -0.0617 -0.0366 0.0216  145 LEU A CA  
1055 C C   . LEU A 140 ? 0.5301 0.4992 0.7628 -0.0643 -0.0466 0.0038  145 LEU A C   
1056 O O   . LEU A 140 ? 0.4975 0.4643 0.7143 -0.0522 -0.0508 -0.0023 145 LEU A O   
1057 C CB  . LEU A 140 ? 0.6341 0.5509 0.8605 -0.0641 -0.0336 0.0254  145 LEU A CB  
1058 C CG  . LEU A 140 ? 0.6653 0.5665 0.8823 -0.0582 -0.0266 0.0451  145 LEU A CG  
1059 C CD1 . LEU A 140 ? 0.7672 0.6209 0.9782 -0.0576 -0.0268 0.0484  145 LEU A CD1 
1060 C CD2 . LEU A 140 ? 0.6588 0.5792 0.8818 -0.0710 -0.0172 0.0588  145 LEU A CD2 
1061 N N   . VAL A 141 ? 0.5499 0.5297 0.8003 -0.0819 -0.0507 -0.0041 146 VAL A N   
1062 C CA  . VAL A 141 ? 0.5355 0.5335 0.7875 -0.0850 -0.0640 -0.0212 146 VAL A CA  
1063 C C   . VAL A 141 ? 0.5799 0.5541 0.8379 -0.1040 -0.0692 -0.0352 146 VAL A C   
1064 O O   . VAL A 141 ? 0.5520 0.5215 0.8309 -0.1243 -0.0647 -0.0310 146 VAL A O   
1065 C CB  . VAL A 141 ? 0.5739 0.6227 0.8489 -0.0874 -0.0689 -0.0206 146 VAL A CB  
1066 C CG1 . VAL A 141 ? 0.6211 0.6907 0.8939 -0.0850 -0.0872 -0.0372 146 VAL A CG1 
1067 C CG2 . VAL A 141 ? 0.5944 0.6601 0.8625 -0.0680 -0.0627 -0.0080 146 VAL A CG2 
1068 N N   . ASP A 142 ? 0.6548 0.6126 0.8917 -0.0987 -0.0780 -0.0522 147 ASP A N   
1069 C CA  . ASP A 142 ? 0.7067 0.6391 0.9429 -0.1146 -0.0860 -0.0714 147 ASP A CA  
1070 C C   . ASP A 142 ? 0.6923 0.6598 0.9450 -0.1300 -0.1032 -0.0855 147 ASP A C   
1071 O O   . ASP A 142 ? 0.7579 0.7711 1.0233 -0.1244 -0.1082 -0.0797 147 ASP A O   
1072 C CB  . ASP A 142 ? 0.7554 0.6524 0.9585 -0.1003 -0.0851 -0.0852 147 ASP A CB  
1073 C CG  . ASP A 142 ? 0.7442 0.6601 0.9200 -0.0870 -0.0928 -0.0945 147 ASP A CG  
1074 O OD1 . ASP A 142 ? 0.7475 0.6970 0.9266 -0.0894 -0.1057 -0.0964 147 ASP A OD1 
1075 O OD2 . ASP A 142 ? 0.7517 0.6478 0.9013 -0.0729 -0.0853 -0.0998 147 ASP A OD2 
1076 N N   . ASN A 143 ? 0.7382 0.6844 0.9908 -0.1476 -0.1138 -0.1058 148 ASN A N   
1077 C CA  . ASN A 143 ? 0.7796 0.7623 1.0538 -0.1663 -0.1338 -0.1220 148 ASN A CA  
1078 C C   . ASN A 143 ? 0.7667 0.7834 1.0202 -0.1482 -0.1512 -0.1314 148 ASN A C   
1079 O O   . ASN A 143 ? 0.8306 0.8973 1.1097 -0.1538 -0.1663 -0.1353 148 ASN A O   
1080 C CB  . ASN A 143 ? 0.8565 0.8012 1.1312 -0.1911 -0.1437 -0.1445 148 ASN A CB  
1081 C CG  . ASN A 143 ? 0.9195 0.9044 1.2369 -0.2226 -0.1598 -0.1554 148 ASN A CG  
1082 O OD1 . ASN A 143 ? 0.9661 0.9966 1.3253 -0.2342 -0.1530 -0.1398 148 ASN A OD1 
1083 N ND2 . ASN A 143 ? 0.9720 0.9415 1.2805 -0.2378 -0.1806 -0.1840 148 ASN A ND2 
1084 N N   . ASP A 144 ? 0.8128 0.8039 1.0209 -0.1256 -0.1478 -0.1330 149 ASP A N   
1085 C CA  . ASP A 144 ? 0.8139 0.8250 0.9899 -0.1061 -0.1607 -0.1359 149 ASP A CA  
1086 C C   . ASP A 144 ? 0.7497 0.7816 0.9241 -0.0856 -0.1522 -0.1125 149 ASP A C   
1087 O O   . ASP A 144 ? 0.7213 0.7488 0.8577 -0.0674 -0.1558 -0.1094 149 ASP A O   
1088 C CB  . ASP A 144 ? 0.8870 0.8577 1.0102 -0.0954 -0.1582 -0.1495 149 ASP A CB  
1089 C CG  . ASP A 144 ? 1.0207 0.9637 1.1372 -0.1120 -0.1682 -0.1770 149 ASP A CG  
1090 O OD1 . ASP A 144 ? 0.9646 0.9306 1.0957 -0.1272 -0.1912 -0.1924 149 ASP A OD1 
1091 O OD2 . ASP A 144 ? 1.0290 0.9285 1.1278 -0.1090 -0.1541 -0.1843 149 ASP A OD2 
1092 N N   . PHE A 145 ? 0.7323 0.7815 0.9424 -0.0888 -0.1403 -0.0961 150 PHE A N   
1093 C CA  . PHE A 145 ? 0.6718 0.7377 0.8814 -0.0699 -0.1331 -0.0768 150 PHE A CA  
1094 C C   . PHE A 145 ? 0.6486 0.6812 0.8222 -0.0539 -0.1196 -0.0659 150 PHE A C   
1095 O O   . PHE A 145 ? 0.6284 0.6683 0.7934 -0.0386 -0.1180 -0.0532 150 PHE A O   
1096 C CB  . PHE A 145 ? 0.7287 0.8361 0.9422 -0.0574 -0.1528 -0.0789 150 PHE A CB  
1097 C CG  . PHE A 145 ? 0.7437 0.9017 1.0088 -0.0712 -0.1616 -0.0851 150 PHE A CG  
1098 C CD1 . PHE A 145 ? 0.7297 0.9183 1.0315 -0.0712 -0.1481 -0.0723 150 PHE A CD1 
1099 C CD2 . PHE A 145 ? 0.6902 0.8684 0.9682 -0.0861 -0.1824 -0.1048 150 PHE A CD2 
1100 C CE1 . PHE A 145 ? 0.6762 0.9199 1.0305 -0.0864 -0.1523 -0.0777 150 PHE A CE1 
1101 C CE2 . PHE A 145 ? 0.6742 0.9070 1.0078 -0.1031 -0.1900 -0.1113 150 PHE A CE2 
1102 C CZ  . PHE A 145 ? 0.6553 0.9232 1.0292 -0.1037 -0.1733 -0.0970 150 PHE A CZ  
1103 N N   . HIS A 146 ? 0.5820 0.5796 0.7377 -0.0573 -0.1099 -0.0717 151 HIS A N   
1104 C CA  . HIS A 146 ? 0.5318 0.5071 0.6665 -0.0460 -0.0945 -0.0617 151 HIS A CA  
1105 C C   . HIS A 146 ? 0.5186 0.4896 0.6794 -0.0481 -0.0812 -0.0489 151 HIS A C   
1106 O O   . HIS A 146 ? 0.5585 0.5257 0.7426 -0.0602 -0.0796 -0.0506 151 HIS A O   
1107 C CB  . HIS A 146 ? 0.5678 0.5163 0.6757 -0.0451 -0.0884 -0.0747 151 HIS A CB  
1108 C CG  . HIS A 146 ? 0.6999 0.6485 0.7708 -0.0419 -0.1000 -0.0867 151 HIS A CG  
1109 N ND1 . HIS A 146 ? 0.7460 0.6956 0.7833 -0.0310 -0.1002 -0.0773 151 HIS A ND1 
1110 C CD2 . HIS A 146 ? 0.7704 0.7140 0.8272 -0.0483 -0.1126 -0.1073 151 HIS A CD2 
1111 C CE1 . HIS A 146 ? 0.8028 0.7490 0.8042 -0.0293 -0.1121 -0.0895 151 HIS A CE1 
1112 N NE2 . HIS A 146 ? 0.8362 0.7808 0.8490 -0.0392 -0.1207 -0.1095 151 HIS A NE2 
1113 N N   . ILE A 147 ? 0.5315 0.4999 0.6853 -0.0376 -0.0726 -0.0359 152 ILE A N   
1114 C CA  . ILE A 147 ? 0.5384 0.5058 0.7108 -0.0365 -0.0634 -0.0228 152 ILE A CA  
1115 C C   . ILE A 147 ? 0.5512 0.4982 0.7201 -0.0318 -0.0531 -0.0213 152 ILE A C   
1116 O O   . ILE A 147 ? 0.5539 0.4930 0.7068 -0.0280 -0.0496 -0.0288 152 ILE A O   
1117 C CB  . ILE A 147 ? 0.5483 0.5322 0.7199 -0.0275 -0.0648 -0.0109 152 ILE A CB  
1118 C CG1 . ILE A 147 ? 0.5910 0.5642 0.7376 -0.0183 -0.0638 -0.0072 152 ILE A CG1 
1119 C CG2 . ILE A 147 ? 0.5496 0.5607 0.7309 -0.0276 -0.0753 -0.0139 152 ILE A CG2 
1120 C CD1 . ILE A 147 ? 0.6030 0.5670 0.7520 -0.0154 -0.0553 0.0007  152 ILE A CD1 
1121 N N   . LYS A 148 ? 0.5924 0.5342 0.7759 -0.0310 -0.0481 -0.0111 153 LYS A N   
1122 C CA  . LYS A 148 ? 0.5828 0.5128 0.7682 -0.0223 -0.0416 -0.0072 153 LYS A CA  
1123 C C   . LYS A 148 ? 0.5323 0.4681 0.7233 -0.0183 -0.0414 0.0079  153 LYS A C   
1124 O O   . LYS A 148 ? 0.5563 0.4939 0.7531 -0.0239 -0.0413 0.0154  153 LYS A O   
1125 C CB  . LYS A 148 ? 0.6206 0.5256 0.8125 -0.0223 -0.0390 -0.0138 153 LYS A CB  
1126 C CG  . LYS A 148 ? 0.6879 0.5825 0.8696 -0.0232 -0.0384 -0.0326 153 LYS A CG  
1127 C CD  . LYS A 148 ? 0.7664 0.6301 0.9525 -0.0176 -0.0355 -0.0409 153 LYS A CD  
1128 C CE  . LYS A 148 ? 0.7815 0.6352 0.9527 -0.0136 -0.0328 -0.0629 153 LYS A CE  
1129 N NZ  . LYS A 148 ? 0.8552 0.7035 1.0141 -0.0282 -0.0414 -0.0759 153 LYS A NZ  
1130 N N   . ILE A 149 ? 0.5004 0.4412 0.6890 -0.0102 -0.0409 0.0117  154 ILE A N   
1131 C CA  . ILE A 149 ? 0.4961 0.4404 0.6847 -0.0047 -0.0431 0.0232  154 ILE A CA  
1132 C C   . ILE A 149 ? 0.4788 0.4080 0.6742 0.0011  -0.0428 0.0294  154 ILE A C   
1133 O O   . ILE A 149 ? 0.5120 0.4341 0.7158 0.0073  -0.0419 0.0233  154 ILE A O   
1134 C CB  . ILE A 149 ? 0.5082 0.4625 0.6925 -0.0010 -0.0459 0.0226  154 ILE A CB  
1135 C CG1 . ILE A 149 ? 0.5747 0.5327 0.7450 -0.0049 -0.0476 0.0200  154 ILE A CG1 
1136 C CG2 . ILE A 149 ? 0.5385 0.4948 0.7201 0.0054  -0.0515 0.0309  154 ILE A CG2 
1137 C CD1 . ILE A 149 ? 0.7425 0.7011 0.9067 -0.0075 -0.0475 0.0178  154 ILE A CD1 
1138 N N   . ALA A 150 ? 0.6701 0.7630 0.6247 0.0548  0.0394  0.0274  155 ALA A N   
1139 C CA  . ALA A 150 ? 0.6715 0.7785 0.6451 0.0391  0.0352  0.0302  155 ALA A CA  
1140 C C   . ALA A 150 ? 0.7006 0.7929 0.6576 0.0454  0.0382  0.0263  155 ALA A C   
1141 O O   . ALA A 150 ? 0.6895 0.7645 0.6188 0.0626  0.0440  0.0231  155 ALA A O   
1142 C CB  . ALA A 150 ? 0.6752 0.8303 0.6674 0.0361  0.0335  0.0426  155 ALA A CB  
1143 N N   . ASP A 151 ? 0.7513 0.8482 0.7216 0.0320  0.0348  0.0267  156 ASP A N   
1144 C CA  . ASP A 151 ? 0.7834 0.8763 0.7423 0.0356  0.0370  0.0247  156 ASP A CA  
1145 C C   . ASP A 151 ? 0.6997 0.8261 0.6793 0.0298  0.0346  0.0343  156 ASP A C   
1146 O O   . ASP A 151 ? 0.7314 0.8556 0.7194 0.0190  0.0319  0.0337  156 ASP A O   
1147 C CB  . ASP A 151 ? 0.7640 0.8263 0.7122 0.0246  0.0358  0.0143  156 ASP A CB  
1148 C CG  . ASP A 151 ? 0.8213 0.8797 0.7545 0.0259  0.0379  0.0115  156 ASP A CG  
1149 O OD1 . ASP A 151 ? 0.7620 0.8257 0.6814 0.0403  0.0421  0.0145  156 ASP A OD1 
1150 O OD2 . ASP A 151 ? 0.8629 0.9151 0.7964 0.0131  0.0354  0.0065  156 ASP A OD2 
1151 N N   . LEU A 152 ? 0.6362 0.7959 0.6213 0.0379  0.0361  0.0439  157 LEU A N   
1152 C CA  . LEU A 152 ? 0.5945 0.7883 0.5972 0.0286  0.0337  0.0545  157 LEU A CA  
1153 C C   . LEU A 152 ? 0.6018 0.8009 0.6006 0.0326  0.0353  0.0555  157 LEU A C   
1154 O O   . LEU A 152 ? 0.6692 0.8782 0.6797 0.0206  0.0327  0.0607  157 LEU A O   
1155 C CB  . LEU A 152 ? 0.5728 0.8098 0.5822 0.0325  0.0344  0.0653  157 LEU A CB  
1156 C CG  . LEU A 152 ? 0.5830 0.8229 0.5982 0.0259  0.0323  0.0658  157 LEU A CG  
1157 C CD1 . LEU A 152 ? 0.5764 0.8706 0.5972 0.0297  0.0332  0.0777  157 LEU A CD1 
1158 C CD2 . LEU A 152 ? 0.5497 0.7698 0.5758 0.0018  0.0268  0.0644  157 LEU A CD2 
1159 N N   . GLY A 153 ? 0.6602 0.8471 0.6381 0.0494  0.0400  0.0503  158 GLY A N   
1160 C CA  . GLY A 153 ? 0.6616 0.8453 0.6314 0.0522  0.0415  0.0485  158 GLY A CA  
1161 C C   . GLY A 153 ? 0.6552 0.8114 0.6220 0.0401  0.0392  0.0395  158 GLY A C   
1162 O O   . GLY A 153 ? 0.7225 0.8788 0.6823 0.0410  0.0402  0.0379  158 GLY A O   
1163 N N   . LEU A 154 ? 0.6878 0.8246 0.6589 0.0293  0.0363  0.0340  159 LEU A N   
1164 C CA  . LEU A 154 ? 0.7621 0.8844 0.7337 0.0174  0.0336  0.0276  159 LEU A CA  
1165 C C   . LEU A 154 ? 0.7943 0.8968 0.7396 0.0181  0.0362  0.0180  159 LEU A C   
1166 O O   . LEU A 154 ? 0.8570 0.9652 0.8023 0.0107  0.0349  0.0160  159 LEU A O   
1167 C CB  . LEU A 154 ? 0.7934 0.9356 0.7837 0.0107  0.0309  0.0353  159 LEU A CB  
1168 C CG  . LEU A 154 ? 0.8245 0.9757 0.8312 0.0050  0.0285  0.0442  159 LEU A CG  
1169 C CD1 . LEU A 154 ? 0.9049 1.0700 0.9194 0.0008  0.0277  0.0532  159 LEU A CD1 
1170 C CD2 . LEU A 154 ? 0.8305 0.9627 0.8402 -0.0023 0.0260  0.0401  159 LEU A CD2 
1171 N N   . ALA A 155 ? 0.7993 0.8773 0.7181 0.0269  0.0404  0.0124  160 ALA A N   
1172 C CA  . ALA A 155 ? 0.8201 0.8668 0.7019 0.0254  0.0438  0.0024  160 ALA A CA  
1173 C C   . ALA A 155 ? 0.8450 0.8767 0.7195 0.0048  0.0407  -0.0066 160 ALA A C   
1174 O O   . ALA A 155 ? 0.9837 1.0070 0.8372 -0.0052 0.0413  -0.0126 160 ALA A O   
1175 C CB  . ALA A 155 ? 0.9024 0.9172 0.7501 0.0418  0.0500  -0.0006 160 ALA A CB  
1176 N N   . SER A 156 ? 0.8387 0.8711 0.7297 -0.0023 0.0375  -0.0069 161 SER A N   
1177 C CA  . SER A 156 ? 0.8467 0.8756 0.7354 -0.0212 0.0342  -0.0136 161 SER A CA  
1178 C C   . SER A 156 ? 0.7989 0.8643 0.7147 -0.0287 0.0297  -0.0089 161 SER A C   
1179 O O   . SER A 156 ? 0.8066 0.8790 0.7206 -0.0424 0.0273  -0.0130 161 SER A O   
1180 C CB  . SER A 156 ? 0.8737 0.8855 0.7641 -0.0234 0.0333  -0.0163 161 SER A CB  
1181 O OG  . SER A 156 ? 0.9760 0.9478 0.8302 -0.0189 0.0381  -0.0226 161 SER A OG  
1182 N N   . PHE A 157 ? 0.7944 0.8838 0.7319 -0.0191 0.0292  0.0004  162 PHE A N   
1183 C CA  . PHE A 157 ? 0.7564 0.8743 0.7167 -0.0204 0.0262  0.0071  162 PHE A CA  
1184 C C   . PHE A 157 ? 0.8193 0.9577 0.7826 -0.0154 0.0272  0.0125  162 PHE A C   
1185 O O   . PHE A 157 ? 0.7860 0.9316 0.7616 -0.0066 0.0279  0.0208  162 PHE A O   
1186 C CB  . PHE A 157 ? 0.7064 0.8238 0.6867 -0.0149 0.0247  0.0143  162 PHE A CB  
1187 C CG  . PHE A 157 ? 0.6902 0.7886 0.6682 -0.0190 0.0237  0.0091  162 PHE A CG  
1188 C CD1 . PHE A 157 ? 0.6680 0.7688 0.6438 -0.0273 0.0218  0.0044  162 PHE A CD1 
1189 C CD2 . PHE A 157 ? 0.6533 0.7358 0.6297 -0.0142 0.0250  0.0092  162 PHE A CD2 
1190 C CE1 . PHE A 157 ? 0.6686 0.7521 0.6412 -0.0317 0.0210  -0.0005 162 PHE A CE1 
1191 C CE2 . PHE A 157 ? 0.6498 0.7147 0.6228 -0.0175 0.0243  0.0043  162 PHE A CE2 
1192 C CZ  . PHE A 157 ? 0.6551 0.7181 0.6261 -0.0268 0.0223  -0.0009 162 PHE A CZ  
1193 N N   . LYS A 158 ? 0.8650 1.0150 0.8160 -0.0235 0.0270  0.0079  163 LYS A N   
1194 C CA  . LYS A 158 ? 0.8896 1.0560 0.8370 -0.0205 0.0284  0.0105  163 LYS A CA  
1195 C C   . LYS A 158 ? 0.8898 1.0812 0.8597 -0.0104 0.0278  0.0222  163 LYS A C   
1196 O O   . LYS A 158 ? 0.8626 1.0578 0.8351 -0.0026 0.0295  0.0275  163 LYS A O   
1197 C CB  . LYS A 158 ? 0.8398 1.0178 0.7687 -0.0353 0.0276  0.0032  163 LYS A CB  
1198 C CG  . LYS A 158 ? 0.8742 1.0174 0.7673 -0.0482 0.0294  -0.0088 163 LYS A CG  
1199 C CD  . LYS A 158 ? 0.8843 1.0378 0.7636 -0.0705 0.0269  -0.0158 163 LYS A CD  
1200 C CE  . LYS A 158 ? 0.9258 1.0357 0.7603 -0.0870 0.0293  -0.0279 163 LYS A CE  
1201 N NZ  . LYS A 158 ? 0.9357 1.0534 0.7571 -0.1120 0.0265  -0.0342 163 LYS A NZ  
1202 N N   . MET A 159 ? 0.8252 1.0314 0.8069 -0.0094 0.0260  0.0267  164 MET A N   
1203 C CA  . MET A 159 ? 0.8448 1.0663 0.8386 0.0013  0.0264  0.0380  164 MET A CA  
1204 C C   . MET A 159 ? 0.8169 1.0207 0.8183 0.0070  0.0273  0.0457  164 MET A C   
1205 O O   . MET A 159 ? 0.8367 1.0479 0.8406 0.0121  0.0287  0.0535  164 MET A O   
1206 C CB  . MET A 159 ? 0.8078 1.0442 0.8049 0.0054  0.0255  0.0414  164 MET A CB  
1207 C CG  . MET A 159 ? 0.7675 1.0387 0.7586 -0.0006 0.0246  0.0374  164 MET A CG  
1208 S SD  . MET A 159 ? 0.7629 1.0669 0.7528 0.0050  0.0260  0.0430  164 MET A SD  
1209 C CE  . MET A 159 ? 0.7673 1.1145 0.7479 -0.0096 0.0239  0.0363  164 MET A CE  
1210 N N   . TRP A 160 ? 0.7601 0.9431 0.7637 0.0040  0.0264  0.0438  165 TRP A N   
1211 C CA  . TRP A 160 ? 0.7151 0.8858 0.7237 0.0043  0.0268  0.0505  165 TRP A CA  
1212 C C   . TRP A 160 ? 0.7822 0.9609 0.7901 0.0055  0.0283  0.0510  165 TRP A C   
1213 O O   . TRP A 160 ? 0.8007 0.9855 0.8129 0.0057  0.0289  0.0596  165 TRP A O   
1214 C CB  . TRP A 160 ? 0.7026 0.8538 0.7130 -0.0002 0.0254  0.0477  165 TRP A CB  
1215 C CG  . TRP A 160 ? 0.6504 0.7898 0.6597 0.0007  0.0244  0.0497  165 TRP A CG  
1216 C CD1 . TRP A 160 ? 0.6248 0.7668 0.6322 0.0019  0.0236  0.0444  165 TRP A CD1 
1217 C CD2 . TRP A 160 ? 0.6375 0.7587 0.6427 0.0003  0.0247  0.0579  165 TRP A CD2 
1218 N NE1 . TRP A 160 ? 0.6676 0.7961 0.6712 0.0066  0.0237  0.0492  165 TRP A NE1 
1219 C CE2 . TRP A 160 ? 0.6702 0.7805 0.6696 0.0054  0.0246  0.0571  165 TRP A CE2 
1220 C CE3 . TRP A 160 ? 0.6522 0.7648 0.6541 -0.0055 0.0253  0.0663  165 TRP A CE3 
1221 C CZ2 . TRP A 160 ? 0.6908 0.7737 0.6772 0.0076  0.0258  0.0639  165 TRP A CZ2 
1222 C CZ3 . TRP A 160 ? 0.6747 0.7595 0.6629 -0.0084 0.0260  0.0727  165 TRP A CZ3 
1223 C CH2 . TRP A 160 ? 0.7097 0.7757 0.6882 -0.0005 0.0265  0.0712  165 TRP A CH2 
1224 N N   . SER A 161 ? 0.8767 1.0542 0.8750 0.0062  0.0293  0.0423  166 SER A N   
1225 C CA  . SER A 161 ? 0.9319 1.1149 0.9229 0.0124  0.0319  0.0424  166 SER A CA  
1226 C C   . SER A 161 ? 0.9529 1.1561 0.9454 0.0160  0.0330  0.0479  166 SER A C   
1227 O O   . SER A 161 ? 0.9563 1.1724 0.9516 0.0213  0.0346  0.0547  166 SER A O   
1228 C CB  . SER A 161 ? 0.9547 1.1192 0.9240 0.0130  0.0338  0.0311  166 SER A CB  
1229 O OG  . SER A 161 ? 1.0218 1.1837 0.9804 0.0241  0.0373  0.0322  166 SER A OG  
1230 N N   . LYS A 162 ? 1.0174 1.2278 1.0078 0.0132  0.0322  0.0456  167 LYS A N   
1231 C CA  . LYS A 162 ? 1.0664 1.2977 1.0591 0.0169  0.0331  0.0515  167 LYS A CA  
1232 C C   . LYS A 162 ? 1.0950 1.3318 1.0995 0.0192  0.0330  0.0640  167 LYS A C   
1233 O O   . LYS A 162 ? 1.1409 1.3908 1.1474 0.0224  0.0344  0.0711  167 LYS A O   
1234 C CB  . LYS A 162 ? 1.0578 1.3019 1.0451 0.0133  0.0322  0.0470  167 LYS A CB  
1235 C CG  . LYS A 162 ? 1.0907 1.3293 1.0582 0.0062  0.0327  0.0354  167 LYS A CG  
1236 C CD  . LYS A 162 ? 1.0909 1.3491 1.0532 -0.0029 0.0309  0.0312  167 LYS A CD  
1237 C CE  . LYS A 162 ? 1.1097 1.3573 1.0447 -0.0162 0.0314  0.0192  167 LYS A CE  
1238 N NZ  . LYS A 162 ? 1.1100 1.3857 1.0393 -0.0299 0.0290  0.0157  167 LYS A NZ  
1239 N N   . LEU A 163 ? 1.1057 1.3290 1.1135 0.0167  0.0317  0.0665  168 LEU A N   
1240 C CA  . LEU A 163 ? 1.0876 1.3019 1.0964 0.0157  0.0322  0.0776  168 LEU A CA  
1241 C C   . LEU A 163 ? 1.0372 1.2533 1.0493 0.0096  0.0323  0.0831  168 LEU A C   
1242 O O   . LEU A 163 ? 0.9368 1.1554 0.9465 0.0060  0.0332  0.0930  168 LEU A O   
1243 C CB  . LEU A 163 ? 1.0092 1.2010 1.0144 0.0145  0.0312  0.0775  168 LEU A CB  
1244 C CG  . LEU A 163 ? 1.0092 1.1774 1.0043 0.0118  0.0323  0.0876  168 LEU A CG  
1245 C CD1 . LEU A 163 ? 1.0727 1.2430 1.0576 0.0202  0.0351  0.0963  168 LEU A CD1 
1246 C CD2 . LEU A 163 ? 1.0866 1.2297 1.0748 0.0125  0.0317  0.0855  168 LEU A CD2 
1247 N N   . ASN A 164 ? 1.1320 1.3487 1.1470 0.0083  0.0317  0.0771  169 ASN A N   
1248 C CA  . ASN A 164 ? 1.2598 1.4893 1.2784 0.0049  0.0320  0.0824  169 ASN A CA  
1249 C C   . ASN A 164 ? 1.2771 1.5335 1.2962 0.0109  0.0341  0.0875  169 ASN A C   
1250 O O   . ASN A 164 ? 1.1328 1.4073 1.1550 0.0051  0.0343  0.0973  169 ASN A O   
1251 C CB  . ASN A 164 ? 1.2557 1.4802 1.2739 0.0077  0.0318  0.0747  169 ASN A CB  
1252 C CG  . ASN A 164 ? 1.2253 1.4686 1.2476 0.0051  0.0319  0.0813  169 ASN A CG  
1253 O OD1 . ASN A 164 ? 1.0613 1.3044 1.0805 0.0124  0.0329  0.0762  169 ASN A OD1 
1254 N ND2 . ASN A 164 ? 1.2505 1.5107 1.2767 -0.0058 0.0312  0.0926  169 ASN A ND2 
1255 N N   . ASN A 165 ? 1.4077 1.6673 1.4215 0.0204  0.0356  0.0809  170 ASN A N   
1256 C CA  . ASN A 165 ? 1.3306 1.6123 1.3414 0.0288  0.0381  0.0837  170 ASN A CA  
1257 C C   . ASN A 165 ? 1.1233 1.4101 1.1337 0.0293  0.0383  0.0858  170 ASN A C   
1258 O O   . ASN A 165 ? 1.0274 1.3202 1.0420 0.0247  0.0381  0.0956  170 ASN A O   
1259 C CB  . ASN A 165 ? 1.2906 1.5651 1.2871 0.0396  0.0404  0.0735  170 ASN A CB  
1260 C CG  . ASN A 165 ? 1.4051 1.6718 1.3975 0.0433  0.0411  0.0707  170 ASN A CG  
1261 O OD1 . ASN A 165 ? 1.3949 1.6774 1.3977 0.0403  0.0404  0.0789  170 ASN A OD1 
1262 N ND2 . ASN A 165 ? 1.4149 1.6570 1.3887 0.0490  0.0429  0.0596  170 ASN A ND2 
1263 N N   . GLY A 183 ? 1.2315 1.2168 1.0986 0.0509  0.0507  0.1575  188 GLY A N   
1264 C CA  . GLY A 183 ? 1.2867 1.2772 1.1117 0.0738  0.0436  0.1420  188 GLY A CA  
1265 C C   . GLY A 183 ? 1.2585 1.2787 1.1050 0.0847  0.0449  0.1145  188 GLY A C   
1266 O O   . GLY A 183 ? 1.1794 1.2122 0.9907 0.1017  0.0528  0.1035  188 GLY A O   
1267 N N   . THR A 184 ? 1.2891 1.3161 1.1875 0.0776  0.0359  0.1029  189 THR A N   
1268 C CA  . THR A 184 ? 1.2374 1.2850 1.1560 0.0895  0.0337  0.0790  189 THR A CA  
1269 C C   . THR A 184 ? 1.1608 1.1790 1.0573 0.1041  0.0063  0.0601  189 THR A C   
1270 O O   . THR A 184 ? 0.9727 0.9681 0.8827 0.0968  -0.0143 0.0594  189 THR A O   
1271 C CB  . THR A 184 ? 1.1511 1.2203 1.1283 0.0770  0.0364  0.0753  189 THR A CB  
1272 O OG1 . THR A 184 ? 1.0956 1.1830 1.0829 0.0941  0.0344  0.0543  189 THR A OG1 
1273 C CG2 . THR A 184 ? 1.0648 1.1074 1.0666 0.0646  0.0164  0.0766  189 THR A CG2 
1274 N N   . LEU A 185 ? 1.0816 1.1022 0.9441 0.1241  0.0082  0.0441  190 LEU A N   
1275 C CA  . LEU A 185 ? 1.0216 1.0137 0.8631 0.1372  -0.0158 0.0217  190 LEU A CA  
1276 C C   . LEU A 185 ? 0.9508 0.9448 0.8178 0.1459  -0.0188 0.0033  190 LEU A C   
1277 O O   . LEU A 185 ? 1.0336 0.9976 0.8817 0.1558  -0.0371 -0.0154 190 LEU A O   
1278 C CB  . LEU A 185 ? 1.1135 1.0969 0.8934 0.1561  -0.0149 0.0121  190 LEU A CB  
1279 C CG  . LEU A 185 ? 1.1294 1.1106 0.8696 0.1530  -0.0098 0.0318  190 LEU A CG  
1280 C CD1 . LEU A 185 ? 1.1745 1.1433 0.8472 0.1738  -0.0136 0.0174  190 LEU A CD1 
1281 C CD2 . LEU A 185 ? 1.1880 1.1473 0.9401 0.1385  -0.0330 0.0445  190 LEU A CD2 
1282 N N   . TYR A 186 ? 0.8716 0.8972 0.7803 0.1415  -0.0036 0.0087  191 TYR A N   
1283 C CA  . TYR A 186 ? 0.8407 0.8700 0.7724 0.1531  -0.0078 -0.0062 191 TYR A CA  
1284 C C   . TYR A 186 ? 0.7884 0.7830 0.7351 0.1429  -0.0311 -0.0097 191 TYR A C   
1285 O O   . TYR A 186 ? 0.8681 0.8451 0.8137 0.1554  -0.0408 -0.0233 191 TYR A O   
1286 C CB  . TYR A 186 ? 0.7645 0.8433 0.7408 0.1496  0.0113  0.0008  191 TYR A CB  
1287 C CG  . TYR A 186 ? 0.7924 0.9184 0.7665 0.1560  0.0401  0.0053  191 TYR A CG  
1288 C CD1 . TYR A 186 ? 0.8189 0.9441 0.7462 0.1762  0.0501  -0.0035 191 TYR A CD1 
1289 C CD2 . TYR A 186 ? 0.8205 0.9946 0.8398 0.1401  0.0587  0.0176  191 TYR A CD2 
1290 C CE1 . TYR A 186 ? 0.8703 1.0434 0.7952 0.1804  0.0810  0.0021  191 TYR A CE1 
1291 C CE2 . TYR A 186 ? 0.7929 1.0159 0.8157 0.1410  0.0885  0.0233  191 TYR A CE2 
1292 C CZ  . TYR A 186 ? 0.8452 1.0690 0.8204 0.1616  0.1013  0.0165  191 TYR A CZ  
1293 O OH  . TYR A 186 ? 0.9169 1.1930 0.8942 0.1615  0.1348  0.0232  191 TYR A OH  
1294 N N   . TYR A 187 ? 0.7101 0.6948 0.6695 0.1213  -0.0384 0.0030  192 TYR A N   
1295 C CA  . TYR A 187 ? 0.7012 0.6610 0.6778 0.1080  -0.0554 0.0021  192 TYR A CA  
1296 C C   . TYR A 187 ? 0.7136 0.6426 0.6680 0.1025  -0.0737 -0.0028 192 TYR A C   
1297 O O   . TYR A 187 ? 0.6610 0.5739 0.6307 0.0888  -0.0857 -0.0031 192 TYR A O   
1298 C CB  . TYR A 187 ? 0.6238 0.6012 0.6369 0.0890  -0.0493 0.0172  192 TYR A CB  
1299 C CG  . TYR A 187 ? 0.5757 0.5878 0.6151 0.0904  -0.0339 0.0205  192 TYR A CG  
1300 C CD1 . TYR A 187 ? 0.6181 0.6606 0.6602 0.0896  -0.0149 0.0293  192 TYR A CD1 
1301 C CD2 . TYR A 187 ? 0.5568 0.5730 0.6172 0.0921  -0.0388 0.0148  192 TYR A CD2 
1302 C CE1 . TYR A 187 ? 0.6346 0.7168 0.7079 0.0877  -0.0011 0.0307  192 TYR A CE1 
1303 C CE2 . TYR A 187 ? 0.5537 0.6083 0.6421 0.0939  -0.0286 0.0154  192 TYR A CE2 
1304 C CZ  . TYR A 187 ? 0.5603 0.6507 0.6590 0.0907  -0.0097 0.0223  192 TYR A CZ  
1305 O OH  . TYR A 187 ? 0.5614 0.6962 0.6953 0.0889  -0.0004 0.0217  192 TYR A OH  
1306 N N   . MET A 188 ? 0.8050 0.7293 0.7235 0.1126  -0.0755 -0.0074 193 MET A N   
1307 C CA  . MET A 188 ? 0.8514 0.7534 0.7480 0.1081  -0.0956 -0.0136 193 MET A CA  
1308 C C   . MET A 188 ? 0.8915 0.7597 0.7644 0.1155  -0.1101 -0.0353 193 MET A C   
1309 O O   . MET A 188 ? 0.9227 0.7847 0.7696 0.1356  -0.1033 -0.0472 193 MET A O   
1310 C CB  . MET A 188 ? 0.8838 0.7946 0.7449 0.1171  -0.0923 -0.0082 193 MET A CB  
1311 C CG  . MET A 188 ? 0.9625 0.8581 0.8044 0.1129  -0.1165 -0.0129 193 MET A CG  
1312 S SD  . MET A 188 ? 1.1288 1.0342 0.9268 0.1236  -0.1130 0.0011  193 MET A SD  
1313 C CE  . MET A 188 ? 1.0714 0.9943 0.9102 0.1102  -0.1013 0.0298  193 MET A CE  
1314 N N   . ALA A 189 ? 0.8652 0.7116 0.7473 0.0994  -0.1294 -0.0409 194 ALA A N   
1315 C CA  . ALA A 189 ? 0.8473 0.6522 0.7086 0.0994  -0.1454 -0.0604 194 ALA A CA  
1316 C C   . ALA A 189 ? 0.9386 0.7270 0.7514 0.1134  -0.1566 -0.0778 194 ALA A C   
1317 O O   . ALA A 189 ? 0.9514 0.7599 0.7516 0.1148  -0.1595 -0.0729 194 ALA A O   
1318 C CB  . ALA A 189 ? 0.8215 0.6139 0.7091 0.0727  -0.1608 -0.0600 194 ALA A CB  
1319 N N   . PRO A 190 ? 1.0978 0.8456 0.8785 0.1260  -0.1638 -0.0986 195 PRO A N   
1320 C CA  . PRO A 190 ? 1.0932 0.8214 0.8201 0.1431  -0.1736 -0.1197 195 PRO A CA  
1321 C C   . PRO A 190 ? 1.0545 0.7779 0.7688 0.1270  -0.1988 -0.1271 195 PRO A C   
1322 O O   . PRO A 190 ? 1.0955 0.8267 0.7700 0.1406  -0.2025 -0.1335 195 PRO A O   
1323 C CB  . PRO A 190 ? 1.2060 0.8801 0.9085 0.1553  -0.1806 -0.1415 195 PRO A CB  
1324 C CG  . PRO A 190 ? 1.2545 0.9124 0.9964 0.1347  -0.1831 -0.1306 195 PRO A CG  
1325 C CD  . PRO A 190 ? 1.1362 0.8484 0.9227 0.1278  -0.1641 -0.1043 195 PRO A CD  
1326 N N   . GLU A 191 ? 1.0014 0.7164 0.7497 0.0987  -0.2156 -0.1258 196 GLU A N   
1327 C CA  . GLU A 191 ? 1.0427 0.7668 0.7939 0.0811  -0.2415 -0.1320 196 GLU A CA  
1328 C C   . GLU A 191 ? 1.0414 0.8118 0.7939 0.0884  -0.2397 -0.1156 196 GLU A C   
1329 O O   . GLU A 191 ? 1.1733 0.9496 0.9087 0.0861  -0.2632 -0.1243 196 GLU A O   
1330 C CB  . GLU A 191 ? 1.0260 0.7467 0.8258 0.0472  -0.2541 -0.1305 196 GLU A CB  
1331 C CG  . GLU A 191 ? 0.9753 0.7305 0.8306 0.0348  -0.2358 -0.1056 196 GLU A CG  
1332 C CD  . GLU A 191 ? 0.9582 0.6882 0.8241 0.0324  -0.2186 -0.0992 196 GLU A CD  
1333 O OE1 . GLU A 191 ? 0.8975 0.6431 0.8051 0.0136  -0.2110 -0.0855 196 GLU A OE1 
1334 O OE2 . GLU A 191 ? 0.9879 0.6845 0.8196 0.0519  -0.2127 -0.1078 196 GLU A OE2 
1335 N N   . HIS A 192 ? 0.9982 0.7978 0.7700 0.0964  -0.2141 -0.0920 197 HIS A N   
1336 C CA  . HIS A 192 ? 0.9346 0.7671 0.7004 0.1053  -0.2082 -0.0728 197 HIS A CA  
1337 C C   . HIS A 192 ? 0.9429 0.7761 0.6541 0.1299  -0.1926 -0.0711 197 HIS A C   
1338 O O   . HIS A 192 ? 0.9900 0.8371 0.6759 0.1375  -0.1952 -0.0595 197 HIS A O   
1339 C CB  . HIS A 192 ? 0.8321 0.6915 0.6507 0.0956  -0.1904 -0.0485 197 HIS A CB  
1340 C CG  . HIS A 192 ? 0.8097 0.6747 0.6790 0.0728  -0.2027 -0.0498 197 HIS A CG  
1341 N ND1 . HIS A 192 ? 0.9269 0.8008 0.8073 0.0621  -0.2295 -0.0582 197 HIS A ND1 
1342 C CD2 . HIS A 192 ? 0.7923 0.6576 0.7022 0.0585  -0.1920 -0.0452 197 HIS A CD2 
1343 C CE1 . HIS A 192 ? 0.8383 0.7216 0.7683 0.0409  -0.2315 -0.0581 197 HIS A CE1 
1344 N NE2 . HIS A 192 ? 0.8339 0.7094 0.7786 0.0386  -0.2084 -0.0495 197 HIS A NE2 
1345 N N   . LEU A 193 ? 0.9916 0.8108 0.6839 0.1434  -0.1756 -0.0817 198 LEU A N   
1346 C CA  . LEU A 193 ? 1.0397 0.8620 0.6779 0.1681  -0.1587 -0.0857 198 LEU A CA  
1347 C C   . LEU A 193 ? 1.1395 0.9379 0.7163 0.1781  -0.1828 -0.1080 198 LEU A C   
1348 O O   . LEU A 193 ? 1.2447 1.0095 0.8133 0.1734  -0.2058 -0.1333 198 LEU A O   
1349 C CB  . LEU A 193 ? 1.0430 0.8592 0.6826 0.1832  -0.1379 -0.0966 198 LEU A CB  
1350 C CG  . LEU A 193 ? 0.9967 0.8398 0.6908 0.1774  -0.1144 -0.0780 198 LEU A CG  
1351 C CD1 . LEU A 193 ? 1.0078 0.8420 0.7011 0.1966  -0.1025 -0.0938 198 LEU A CD1 
1352 C CD2 . LEU A 193 ? 0.9837 0.8678 0.6845 0.1771  -0.0891 -0.0522 198 LEU A CD2 
1353 N N   . ASN A 194 ? 1.2006 1.0134 0.7326 0.1897  -0.1791 -0.0977 199 ASN A N   
1354 C CA  . ASN A 194 ? 1.3150 1.1098 0.7834 0.1992  -0.2056 -0.1157 199 ASN A CA  
1355 C C   . ASN A 194 ? 1.3223 1.1078 0.8096 0.1802  -0.2485 -0.1264 199 ASN A C   
1356 O O   . ASN A 194 ? 1.4957 1.2617 0.9350 0.1856  -0.2760 -0.1499 199 ASN A O   
1357 C CB  . ASN A 194 ? 1.4285 1.1947 0.8385 0.2213  -0.2017 -0.1477 199 ASN A CB  
1358 C CG  . ASN A 194 ? 1.4873 1.2739 0.8687 0.2449  -0.1598 -0.1400 199 ASN A CG  
1359 O OD1 . ASN A 194 ? 1.6050 1.3729 0.9492 0.2661  -0.1524 -0.1665 199 ASN A OD1 
1360 N ND2 . ASN A 194 ? 1.4497 1.2735 0.8468 0.2418  -0.1324 -0.1062 199 ASN A ND2 
1361 N N   . ASP A 195 ? 1.2337 1.0373 0.7899 0.1588  -0.2539 -0.1106 200 ASP A N   
1362 C CA  . ASP A 195 ? 1.1982 1.0103 0.7832 0.1412  -0.2903 -0.1160 200 ASP A CA  
1363 C C   . ASP A 195 ? 1.1475 0.9941 0.7879 0.1328  -0.2830 -0.0855 200 ASP A C   
1364 O O   . ASP A 195 ? 1.2912 1.1481 0.9950 0.1144  -0.2784 -0.0806 200 ASP A O   
1365 C CB  . ASP A 195 ? 1.1899 0.9789 0.8056 0.1195  -0.3093 -0.1419 200 ASP A CB  
1366 C CG  . ASP A 195 ? 1.2735 1.0754 0.9108 0.1010  -0.3502 -0.1548 200 ASP A CG  
1367 O OD1 . ASP A 195 ? 1.2609 1.0987 0.9156 0.1029  -0.3623 -0.1388 200 ASP A OD1 
1368 O OD2 . ASP A 195 ? 1.3645 1.1401 1.0027 0.0843  -0.3718 -0.1819 200 ASP A OD2 
1369 N N   . VAL A 196 ? 1.1136 0.9733 0.7231 0.1480  -0.2811 -0.0649 201 VAL A N   
1370 C CA  . VAL A 196 ? 1.0296 0.9138 0.6794 0.1455  -0.2791 -0.0369 201 VAL A CA  
1371 C C   . VAL A 196 ? 1.0708 0.9773 0.7681 0.1343  -0.3138 -0.0436 201 VAL A C   
1372 O O   . VAL A 196 ? 1.1002 1.0278 0.8511 0.1289  -0.3094 -0.0270 201 VAL A O   
1373 C CB  . VAL A 196 ? 1.0600 0.9429 0.6569 0.1651  -0.2693 -0.0107 201 VAL A CB  
1374 C CG1 . VAL A 196 ? 1.0519 0.9261 0.6217 0.1709  -0.2279 0.0008  201 VAL A CG1 
1375 C CG2 . VAL A 196 ? 1.1590 1.0344 0.6875 0.1813  -0.3000 -0.0198 201 VAL A CG2 
1376 N N   . ASN A 197 ? 1.1869 1.0913 0.8663 0.1311  -0.3480 -0.0694 202 ASN A N   
1377 C CA  . ASN A 197 ? 1.2010 1.1355 0.9336 0.1169  -0.3825 -0.0806 202 ASN A CA  
1378 C C   . ASN A 197 ? 1.1225 1.0667 0.9289 0.0879  -0.3754 -0.0906 202 ASN A C   
1379 O O   . ASN A 197 ? 1.1068 1.0874 0.9736 0.0753  -0.3917 -0.0916 202 ASN A O   
1380 C CB  . ASN A 197 ? 1.3082 1.2386 0.9991 0.1187  -0.4238 -0.1079 202 ASN A CB  
1381 C CG  . ASN A 197 ? 1.3969 1.3185 1.0073 0.1480  -0.4350 -0.0983 202 ASN A CG  
1382 O OD1 . ASN A 197 ? 1.3701 1.2966 0.9679 0.1653  -0.4199 -0.0677 202 ASN A OD1 
1383 N ND2 . ASN A 197 ? 1.4671 1.3705 1.0171 0.1531  -0.4615 -0.1246 202 ASN A ND2 
1384 N N   . ALA A 198 ? 1.1346 1.0475 0.9347 0.0786  -0.3518 -0.0979 203 ALA A N   
1385 C CA  . ALA A 198 ? 1.0877 0.9999 0.9458 0.0516  -0.3417 -0.1037 203 ALA A CA  
1386 C C   . ALA A 198 ? 1.0679 1.0134 0.9897 0.0454  -0.3233 -0.0816 203 ALA A C   
1387 O O   . ALA A 198 ? 1.0473 0.9923 0.9627 0.0601  -0.2983 -0.0603 203 ALA A O   
1388 C CB  . ALA A 198 ? 1.0463 0.9148 0.8759 0.0521  -0.3180 -0.1099 203 ALA A CB  
1389 N N   . LYS A 199 ? 1.0955 1.0711 1.0778 0.0232  -0.3357 -0.0883 204 LYS A N   
1390 C CA  . LYS A 199 ? 1.0838 1.0940 1.1281 0.0174  -0.3192 -0.0722 204 LYS A CA  
1391 C C   . LYS A 199 ? 1.0228 1.0082 1.0767 0.0055  -0.2864 -0.0655 204 LYS A C   
1392 O O   . LYS A 199 ? 0.9736 0.9340 1.0255 -0.0144 -0.2866 -0.0786 204 LYS A O   
1393 C CB  . LYS A 199 ? 1.0812 1.1378 1.1885 -0.0035 -0.3403 -0.0839 204 LYS A CB  
1394 C CG  . LYS A 199 ? 1.1143 1.1966 1.2183 -0.0002 -0.3806 -0.0993 204 LYS A CG  
1395 C CD  . LYS A 199 ? 1.0984 1.2392 1.2798 -0.0230 -0.3972 -0.1103 204 LYS A CD  
1396 C CE  . LYS A 199 ? 1.1500 1.3037 1.3273 -0.0359 -0.4389 -0.1358 204 LYS A CE  
1397 N NZ  . LYS A 199 ? 1.1347 1.3544 1.3963 -0.0625 -0.4541 -0.1477 204 LYS A NZ  
1398 N N   . PRO A 200 ? 0.9556 0.9436 1.0160 0.0178  -0.2605 -0.0455 205 PRO A N   
1399 C CA  . PRO A 200 ? 0.8875 0.8578 0.9590 0.0077  -0.2330 -0.0395 205 PRO A CA  
1400 C C   . PRO A 200 ? 0.8255 0.8118 0.9470 -0.0188 -0.2289 -0.0439 205 PRO A C   
1401 O O   . PRO A 200 ? 0.8968 0.9237 1.0618 -0.0266 -0.2398 -0.0466 205 PRO A O   
1402 C CB  . PRO A 200 ? 0.9386 0.9180 1.0143 0.0244  -0.2132 -0.0195 205 PRO A CB  
1403 C CG  . PRO A 200 ? 0.9689 0.9479 1.0086 0.0458  -0.2252 -0.0137 205 PRO A CG  
1404 C CD  . PRO A 200 ? 0.9743 0.9729 1.0226 0.0420  -0.2565 -0.0275 205 PRO A CD  
1405 N N   . THR A 201 ? 0.8330 0.7890 0.9469 -0.0313 -0.2132 -0.0440 206 THR A N   
1406 C CA  . THR A 201 ? 0.8304 0.7924 0.9806 -0.0585 -0.2041 -0.0446 206 THR A CA  
1407 C C   . THR A 201 ? 0.7142 0.6642 0.8625 -0.0545 -0.1775 -0.0311 206 THR A C   
1408 O O   . THR A 201 ? 0.7039 0.6414 0.8270 -0.0339 -0.1687 -0.0238 206 THR A O   
1409 C CB  . THR A 201 ? 0.8477 0.7720 0.9817 -0.0817 -0.2153 -0.0583 206 THR A CB  
1410 O OG1 . THR A 201 ? 1.0222 0.8932 1.1075 -0.0700 -0.2083 -0.0583 206 THR A OG1 
1411 C CG2 . THR A 201 ? 0.8958 0.8279 1.0262 -0.0864 -0.2452 -0.0756 206 THR A CG2 
1412 N N   . GLU A 202 ? 0.7661 0.7210 0.9397 -0.0757 -0.1648 -0.0280 207 GLU A N   
1413 C CA  . GLU A 202 ? 0.7794 0.7160 0.9429 -0.0744 -0.1426 -0.0169 207 GLU A CA  
1414 C C   . GLU A 202 ? 0.7897 0.6754 0.9056 -0.0637 -0.1426 -0.0169 207 GLU A C   
1415 O O   . GLU A 202 ? 0.9005 0.7798 1.0032 -0.0483 -0.1306 -0.0092 207 GLU A O   
1416 C CB  . GLU A 202 ? 0.8383 0.7823 1.0261 -0.1015 -0.1298 -0.0137 207 GLU A CB  
1417 C CG  . GLU A 202 ? 0.9504 0.9535 1.1900 -0.1066 -0.1227 -0.0136 207 GLU A CG  
1418 C CD  . GLU A 202 ? 1.1291 1.1468 1.3925 -0.1334 -0.1044 -0.0100 207 GLU A CD  
1419 O OE1 . GLU A 202 ? 1.4232 1.4021 1.6572 -0.1440 -0.0920 -0.0021 207 GLU A OE1 
1420 O OE2 . GLU A 202 ? 1.1739 1.2449 1.4856 -0.1426 -0.1018 -0.0145 207 GLU A OE2 
1421 N N   . LYS A 203 ? 0.8453 0.6971 0.9372 -0.0702 -0.1578 -0.0277 208 LYS A N   
1422 C CA  . LYS A 203 ? 0.8466 0.6477 0.8932 -0.0565 -0.1598 -0.0312 208 LYS A CA  
1423 C C   . LYS A 203 ? 0.8048 0.6128 0.8291 -0.0256 -0.1595 -0.0326 208 LYS A C   
1424 O O   . LYS A 203 ? 0.8634 0.6474 0.8614 -0.0084 -0.1535 -0.0321 208 LYS A O   
1425 C CB  . LYS A 203 ? 0.8977 0.6546 0.9225 -0.0715 -0.1775 -0.0455 208 LYS A CB  
1426 C CG  . LYS A 203 ? 0.9384 0.6847 0.9840 -0.1082 -0.1770 -0.0435 208 LYS A CG  
1427 C CD  . LYS A 203 ? 1.0056 0.7281 1.0437 -0.1147 -0.1585 -0.0277 208 LYS A CD  
1428 C CE  . LYS A 203 ? 1.0646 0.7646 1.1120 -0.1539 -0.1567 -0.0245 208 LYS A CE  
1429 N NZ  . LYS A 203 ? 1.0535 0.6871 1.0679 -0.1665 -0.1716 -0.0336 208 LYS A NZ  
1430 N N   . SER A 204 ? 0.7490 0.5907 0.7836 -0.0183 -0.1655 -0.0336 209 SER A N   
1431 C CA  . SER A 204 ? 0.7781 0.6325 0.7947 0.0068  -0.1597 -0.0293 209 SER A CA  
1432 C C   . SER A 204 ? 0.7586 0.6257 0.7865 0.0150  -0.1394 -0.0158 209 SER A C   
1433 O O   . SER A 204 ? 0.8208 0.6823 0.8286 0.0319  -0.1312 -0.0148 209 SER A O   
1434 C CB  . SER A 204 ? 0.7972 0.6835 0.8242 0.0109  -0.1689 -0.0271 209 SER A CB  
1435 O OG  . SER A 204 ? 0.8316 0.7151 0.8559 0.0006  -0.1916 -0.0410 209 SER A OG  
1436 N N   . ASP A 205 ? 0.8356 0.7226 0.8969 0.0027  -0.1315 -0.0073 210 ASP A N   
1437 C CA  . ASP A 205 ? 0.7778 0.6746 0.8503 0.0068  -0.1148 0.0028  210 ASP A CA  
1438 C C   . ASP A 205 ? 0.6770 0.5489 0.7347 0.0076  -0.1098 0.0025  210 ASP A C   
1439 O O   . ASP A 205 ? 0.6662 0.5451 0.7236 0.0176  -0.1004 0.0073  210 ASP A O   
1440 C CB  . ASP A 205 ? 0.7414 0.6621 0.8484 -0.0048 -0.1083 0.0084  210 ASP A CB  
1441 C CG  . ASP A 205 ? 0.7546 0.7005 0.8786 0.0007  -0.1131 0.0109  210 ASP A CG  
1442 O OD1 . ASP A 205 ? 0.7580 0.7036 0.8645 0.0140  -0.1178 0.0132  210 ASP A OD1 
1443 O OD2 . ASP A 205 ? 0.7275 0.6941 0.8815 -0.0068 -0.1116 0.0112  210 ASP A OD2 
1444 N N   . VAL A 206 ? 0.6777 0.5198 0.7236 -0.0036 -0.1173 -0.0028 211 VAL A N   
1445 C CA  . VAL A 206 ? 0.6816 0.4891 0.7051 0.0000  -0.1161 -0.0018 211 VAL A CA  
1446 C C   . VAL A 206 ? 0.6688 0.4625 0.6662 0.0255  -0.1191 -0.0083 211 VAL A C   
1447 O O   . VAL A 206 ? 0.6736 0.4645 0.6650 0.0389  -0.1144 -0.0050 211 VAL A O   
1448 C CB  . VAL A 206 ? 0.6982 0.4693 0.7123 -0.0211 -0.1227 -0.0035 211 VAL A CB  
1449 C CG1 . VAL A 206 ? 0.7705 0.4923 0.7514 -0.0135 -0.1250 -0.0014 211 VAL A CG1 
1450 C CG2 . VAL A 206 ? 0.6649 0.4607 0.7087 -0.0442 -0.1128 0.0045  211 VAL A CG2 
1451 N N   . TYR A 207 ? 0.6950 0.4845 0.6774 0.0335  -0.1270 -0.0185 212 TYR A N   
1452 C CA  . TYR A 207 ? 0.7405 0.5275 0.6995 0.0601  -0.1257 -0.0262 212 TYR A CA  
1453 C C   . TYR A 207 ? 0.7533 0.5824 0.7308 0.0716  -0.1104 -0.0172 212 TYR A C   
1454 O O   . TYR A 207 ? 0.8551 0.6877 0.8281 0.0895  -0.1054 -0.0189 212 TYR A O   
1455 C CB  . TYR A 207 ? 0.7854 0.5687 0.7226 0.0662  -0.1344 -0.0381 212 TYR A CB  
1456 C CG  . TYR A 207 ? 0.8222 0.6011 0.7306 0.0951  -0.1300 -0.0482 212 TYR A CG  
1457 C CD1 . TYR A 207 ? 0.8225 0.6439 0.7376 0.1093  -0.1140 -0.0418 212 TYR A CD1 
1458 C CD2 . TYR A 207 ? 0.8276 0.5595 0.7026 0.1085  -0.1401 -0.0643 212 TYR A CD2 
1459 C CE1 . TYR A 207 ? 0.8314 0.6583 0.7247 0.1358  -0.1058 -0.0514 212 TYR A CE1 
1460 C CE2 . TYR A 207 ? 0.8539 0.5861 0.7041 0.1395  -0.1341 -0.0759 212 TYR A CE2 
1461 C CZ  . TYR A 207 ? 0.8506 0.6353 0.7119 0.1532  -0.1157 -0.0695 212 TYR A CZ  
1462 O OH  . TYR A 207 ? 0.8590 0.6540 0.7001 0.1834  -0.1059 -0.0813 212 TYR A OH  
1463 N N   . SER A 208 ? 0.7695 0.6301 0.7690 0.0614  -0.1044 -0.0084 213 SER A N   
1464 C CA  . SER A 208 ? 0.7344 0.6307 0.7532 0.0658  -0.0901 0.0009  213 SER A CA  
1465 C C   . SER A 208 ? 0.6716 0.5737 0.7068 0.0647  -0.0855 0.0049  213 SER A C   
1466 O O   . SER A 208 ? 0.6521 0.5753 0.6939 0.0765  -0.0782 0.0050  213 SER A O   
1467 C CB  . SER A 208 ? 0.7859 0.7010 0.8223 0.0538  -0.0875 0.0102  213 SER A CB  
1468 O OG  . SER A 208 ? 0.7278 0.6358 0.7477 0.0545  -0.0974 0.0064  213 SER A OG  
1469 N N   . PHE A 209 ? 0.6779 0.5635 0.7186 0.0506  -0.0901 0.0072  214 PHE A N   
1470 C CA  . PHE A 209 ? 0.6637 0.5472 0.7092 0.0501  -0.0890 0.0106  214 PHE A CA  
1471 C C   . PHE A 209 ? 0.7338 0.6028 0.7609 0.0709  -0.0944 0.0054  214 PHE A C   
1472 O O   . PHE A 209 ? 0.8169 0.7046 0.8539 0.0794  -0.0931 0.0070  214 PHE A O   
1473 C CB  . PHE A 209 ? 0.6990 0.5624 0.7438 0.0312  -0.0911 0.0144  214 PHE A CB  
1474 C CG  . PHE A 209 ? 0.7529 0.6020 0.7871 0.0320  -0.0923 0.0184  214 PHE A CG  
1475 C CD1 . PHE A 209 ? 0.7020 0.5761 0.7505 0.0314  -0.0872 0.0213  214 PHE A CD1 
1476 C CD2 . PHE A 209 ? 0.8258 0.6315 0.8308 0.0335  -0.1003 0.0193  214 PHE A CD2 
1477 C CE1 . PHE A 209 ? 0.7754 0.6363 0.8080 0.0340  -0.0912 0.0246  214 PHE A CE1 
1478 C CE2 . PHE A 209 ? 0.8741 0.6619 0.8615 0.0363  -0.1029 0.0256  214 PHE A CE2 
1479 C CZ  . PHE A 209 ? 0.8385 0.6565 0.8390 0.0376  -0.0990 0.0281  214 PHE A CZ  
1480 N N   . ALA A 210 ? 0.7886 0.6246 0.7897 0.0805  -0.1023 -0.0022 215 ALA A N   
1481 C CA  . ALA A 210 ? 0.7911 0.6095 0.7725 0.1068  -0.1082 -0.0096 215 ALA A CA  
1482 C C   . ALA A 210 ? 0.7355 0.6013 0.7342 0.1272  -0.0992 -0.0134 215 ALA A C   
1483 O O   . ALA A 210 ? 0.7414 0.6187 0.7454 0.1457  -0.1019 -0.0152 215 ALA A O   
1484 C CB  . ALA A 210 ? 0.7976 0.5696 0.7463 0.1140  -0.1177 -0.0205 215 ALA A CB  
1485 N N   . VAL A 211 ? 0.6848 0.5800 0.6929 0.1234  -0.0887 -0.0138 216 VAL A N   
1486 C CA  . VAL A 211 ? 0.6843 0.6278 0.7092 0.1381  -0.0756 -0.0159 216 VAL A CA  
1487 C C   . VAL A 211 ? 0.6584 0.6430 0.7208 0.1248  -0.0687 -0.0065 216 VAL A C   
1488 O O   . VAL A 211 ? 0.6547 0.6794 0.7388 0.1362  -0.0626 -0.0089 216 VAL A O   
1489 C CB  . VAL A 211 ? 0.6804 0.6353 0.6924 0.1388  -0.0655 -0.0176 216 VAL A CB  
1490 C CG1 . VAL A 211 ? 0.6437 0.6491 0.6699 0.1538  -0.0479 -0.0194 216 VAL A CG1 
1491 C CG2 . VAL A 211 ? 0.7243 0.6345 0.6959 0.1502  -0.0762 -0.0305 216 VAL A CG2 
1492 N N   . VAL A 212 ? 0.6896 0.6654 0.7608 0.1012  -0.0701 0.0021  217 VAL A N   
1493 C CA  . VAL A 212 ? 0.6161 0.6182 0.7163 0.0879  -0.0675 0.0078  217 VAL A CA  
1494 C C   . VAL A 212 ? 0.6470 0.6490 0.7484 0.0997  -0.0786 0.0040  217 VAL A C   
1495 O O   . VAL A 212 ? 0.7209 0.7610 0.8483 0.1012  -0.0777 0.0026  217 VAL A O   
1496 C CB  . VAL A 212 ? 0.5742 0.5604 0.6779 0.0649  -0.0673 0.0147  217 VAL A CB  
1497 C CG1 . VAL A 212 ? 0.6010 0.6047 0.7268 0.0530  -0.0668 0.0166  217 VAL A CG1 
1498 C CG2 . VAL A 212 ? 0.5809 0.5727 0.6869 0.0569  -0.0585 0.0201  217 VAL A CG2 
1499 N N   . LEU A 213 ? 0.6634 0.6213 0.7355 0.1070  -0.0902 0.0028  218 LEU A N   
1500 C CA  . LEU A 213 ? 0.6867 0.6329 0.7481 0.1236  -0.1035 0.0012  218 LEU A CA  
1501 C C   . LEU A 213 ? 0.6894 0.6702 0.7649 0.1519  -0.1049 -0.0073 218 LEU A C   
1502 O O   . LEU A 213 ? 0.6914 0.7015 0.7845 0.1615  -0.1124 -0.0088 218 LEU A O   
1503 C CB  . LEU A 213 ? 0.7421 0.6250 0.7631 0.1270  -0.1141 0.0033  218 LEU A CB  
1504 C CG  . LEU A 213 ? 0.8620 0.7124 0.8669 0.1044  -0.1163 0.0128  218 LEU A CG  
1505 C CD1 . LEU A 213 ? 1.0296 0.8167 0.9962 0.1048  -0.1239 0.0151  218 LEU A CD1 
1506 C CD2 . LEU A 213 ? 0.9658 0.8284 0.9714 0.1067  -0.1231 0.0170  218 LEU A CD2 
1507 N N   . TRP A 214 ? 0.7099 0.6908 0.7781 0.1659  -0.0978 -0.0142 219 TRP A N   
1508 C CA  . TRP A 214 ? 0.7677 0.7902 0.8525 0.1942  -0.0937 -0.0242 219 TRP A CA  
1509 C C   . TRP A 214 ? 0.7297 0.8257 0.8631 0.1838  -0.0814 -0.0227 219 TRP A C   
1510 O O   . TRP A 214 ? 0.7825 0.9221 0.9434 0.2005  -0.0862 -0.0284 219 TRP A O   
1511 C CB  . TRP A 214 ? 0.8228 0.8311 0.8849 0.2089  -0.0851 -0.0332 219 TRP A CB  
1512 C CG  . TRP A 214 ? 0.8442 0.8928 0.9192 0.2428  -0.0794 -0.0457 219 TRP A CG  
1513 C CD1 . TRP A 214 ? 0.8694 0.8945 0.9263 0.2790  -0.0918 -0.0571 219 TRP A CD1 
1514 C CD2 . TRP A 214 ? 0.7906 0.9133 0.9023 0.2445  -0.0588 -0.0481 219 TRP A CD2 
1515 N NE1 . TRP A 214 ? 0.8559 0.9411 0.9387 0.3066  -0.0801 -0.0687 219 TRP A NE1 
1516 C CE2 . TRP A 214 ? 0.7976 0.9465 0.9155 0.2842  -0.0584 -0.0630 219 TRP A CE2 
1517 C CE3 . TRP A 214 ? 0.7175 0.8847 0.8566 0.2160  -0.0398 -0.0384 219 TRP A CE3 
1518 C CZ2 . TRP A 214 ? 0.7968 1.0243 0.9516 0.2950  -0.0371 -0.0693 219 TRP A CZ2 
1519 C CZ3 . TRP A 214 ? 0.7276 0.9656 0.8995 0.2231  -0.0189 -0.0421 219 TRP A CZ3 
1520 C CH2 . TRP A 214 ? 0.7666 1.0387 0.9482 0.2616  -0.0163 -0.0578 219 TRP A CH2 
1521 N N   . ALA A 215 ? 0.6547 0.7623 0.7985 0.1564  -0.0670 -0.0152 220 ALA A N   
1522 C CA  . ALA A 215 ? 0.6402 0.8061 0.8265 0.1385  -0.0533 -0.0114 220 ALA A CA  
1523 C C   . ALA A 215 ? 0.6340 0.8244 0.8492 0.1296  -0.0653 -0.0120 220 ALA A C   
1524 O O   . ALA A 215 ? 0.6177 0.8677 0.8734 0.1307  -0.0616 -0.0165 220 ALA A O   
1525 C CB  . ALA A 215 ? 0.6394 0.7913 0.8207 0.1107  -0.0407 -0.0005 220 ALA A CB  
1526 N N   . ILE A 216 ? 0.6693 0.8160 0.8628 0.1208  -0.0796 -0.0085 221 ILE A N   
1527 C CA  . ILE A 216 ? 0.6470 0.8059 0.8543 0.1134  -0.0940 -0.0101 221 ILE A CA  
1528 C C   . ILE A 216 ? 0.6191 0.8142 0.8427 0.1404  -0.1089 -0.0188 221 ILE A C   
1529 O O   . ILE A 216 ? 0.6672 0.9093 0.9257 0.1335  -0.1158 -0.0237 221 ILE A O   
1530 C CB  . ILE A 216 ? 0.6793 0.7802 0.8494 0.1036  -0.1038 -0.0045 221 ILE A CB  
1531 C CG1 . ILE A 216 ? 0.6866 0.7719 0.8576 0.0756  -0.0908 0.0014  221 ILE A CG1 
1532 C CG2 . ILE A 216 ? 0.7393 0.8454 0.9084 0.1030  -0.1211 -0.0072 221 ILE A CG2 
1533 C CD1 . ILE A 216 ? 0.7133 0.7459 0.8497 0.0688  -0.0928 0.0066  221 ILE A CD1 
1534 N N   . PHE A 217 ? 0.6278 0.8003 0.8271 0.1718  -0.1155 -0.0218 222 PHE A N   
1535 C CA  . PHE A 217 ? 0.6572 0.8597 0.8692 0.2057  -0.1318 -0.0303 222 PHE A CA  
1536 C C   . PHE A 217 ? 0.6142 0.8846 0.8676 0.2245  -0.1190 -0.0405 222 PHE A C   
1537 O O   . PHE A 217 ? 0.6492 0.9781 0.9402 0.2412  -0.1291 -0.0487 222 PHE A O   
1538 C CB  . PHE A 217 ? 0.7428 0.8759 0.9024 0.2316  -0.1485 -0.0279 222 PHE A CB  
1539 C CG  . PHE A 217 ? 0.8011 0.8874 0.9276 0.2176  -0.1634 -0.0183 222 PHE A CG  
1540 C CD1 . PHE A 217 ? 0.9129 1.0215 1.0460 0.2275  -0.1845 -0.0196 222 PHE A CD1 
1541 C CD2 . PHE A 217 ? 0.7906 0.8175 0.8814 0.1934  -0.1561 -0.0086 222 PHE A CD2 
1542 C CE1 . PHE A 217 ? 0.9257 0.9919 1.0215 0.2149  -0.1966 -0.0107 222 PHE A CE1 
1543 C CE2 . PHE A 217 ? 0.8546 0.8448 0.9152 0.1797  -0.1657 0.0001  222 PHE A CE2 
1544 C CZ  . PHE A 217 ? 0.9076 0.9145 0.9665 0.1907  -0.1851 -0.0004 222 PHE A CZ  
1545 N N   . ALA A 218 ? 0.5918 0.8585 0.8387 0.2217  -0.0969 -0.0403 223 ALA A N   
1546 C CA  . ALA A 218 ? 0.5898 0.9258 0.8745 0.2331  -0.0769 -0.0483 223 ALA A CA  
1547 C C   . ALA A 218 ? 0.5419 0.9511 0.8834 0.2018  -0.0626 -0.0457 223 ALA A C   
1548 O O   . ALA A 218 ? 0.5454 1.0298 0.9319 0.2122  -0.0506 -0.0535 223 ALA A O   
1549 C CB  . ALA A 218 ? 0.6075 0.9131 0.8589 0.2364  -0.0573 -0.0478 223 ALA A CB  
1550 N N   . ASN A 219 ? 0.5412 0.9278 0.8810 0.1639  -0.0630 -0.0356 224 ASN A N   
1551 C CA  . ASN A 219 ? 0.5320 0.9677 0.9173 0.1275  -0.0500 -0.0317 224 ASN A CA  
1552 C C   . ASN A 219 ? 0.5507 1.0165 0.9484 0.1149  -0.0176 -0.0254 224 ASN A C   
1553 O O   . ASN A 219 ? 0.6026 1.1312 1.0487 0.0940  -0.0030 -0.0247 224 ASN A O   
1554 C CB  . ASN A 219 ? 0.5474 1.0542 0.9877 0.1289  -0.0647 -0.0424 224 ASN A CB  
1555 C CG  . ASN A 219 ? 0.5949 1.0703 1.0150 0.1415  -0.0978 -0.0469 224 ASN A CG  
1556 O OD1 . ASN A 219 ? 0.6337 1.0447 1.0141 0.1270  -0.1057 -0.0400 224 ASN A OD1 
1557 N ND2 . ASN A 219 ? 0.6319 1.1556 1.0791 0.1691  -0.1171 -0.0582 224 ASN A ND2 
1558 N N   . LYS A 220 ? 0.5637 0.9831 0.9152 0.1253  -0.0068 -0.0205 225 LYS A N   
1559 C CA  . LYS A 220 ? 0.6006 1.0414 0.9489 0.1196  0.0233  -0.0141 225 LYS A CA  
1560 C C   . LYS A 220 ? 0.6838 1.0555 0.9710 0.1265  0.0254  -0.0086 225 LYS A C   
1561 O O   . LYS A 220 ? 0.7328 1.0477 0.9864 0.1392  0.0047  -0.0124 225 LYS A O   
1562 C CB  . LYS A 220 ? 0.6162 1.1282 0.9932 0.1477  0.0378  -0.0261 225 LYS A CB  
1563 C CG  . LYS A 220 ? 0.6523 1.1442 1.0019 0.1956  0.0237  -0.0417 225 LYS A CG  
1564 C CD  . LYS A 220 ? 0.6739 1.2470 1.0625 0.2267  0.0369  -0.0564 225 LYS A CD  
1565 C CE  . LYS A 220 ? 0.6410 1.1805 0.9968 0.2774  0.0201  -0.0725 225 LYS A CE  
1566 N NZ  . LYS A 220 ? 0.6593 1.2787 1.0551 0.3153  0.0305  -0.0898 225 LYS A NZ  
1567 N N   . GLU A 221 ? 0.7250 1.1024 0.9976 0.1162  0.0497  0.0009  226 GLU A N   
1568 C CA  . GLU A 221 ? 0.7468 1.0672 0.9614 0.1241  0.0509  0.0045  226 GLU A CA  
1569 C C   . GLU A 221 ? 0.7900 1.1109 0.9804 0.1642  0.0498  -0.0128 226 GLU A C   
1570 O O   . GLU A 221 ? 0.8309 1.2111 1.0501 0.1827  0.0619  -0.0227 226 GLU A O   
1571 C CB  . GLU A 221 ? 0.7811 1.1059 0.9815 0.1025  0.0754  0.0213  226 GLU A CB  
1572 C CG  . GLU A 221 ? 0.8244 1.1301 1.0387 0.0650  0.0745  0.0389  226 GLU A CG  
1573 C CD  . GLU A 221 ? 0.8324 1.0686 1.0146 0.0597  0.0534  0.0433  226 GLU A CD  
1574 O OE1 . GLU A 221 ? 0.9085 1.1090 1.0527 0.0793  0.0420  0.0364  226 GLU A OE1 
1575 O OE2 . GLU A 221 ? 0.7820 1.0006 0.9790 0.0357  0.0480  0.0522  226 GLU A OE2 
1576 N N   . PRO A 222 ? 0.8083 1.0646 0.9488 0.1779  0.0344  -0.0184 227 PRO A N   
1577 C CA  . PRO A 222 ? 0.9029 1.1467 1.0152 0.2163  0.0304  -0.0373 227 PRO A CA  
1578 C C   . PRO A 222 ? 1.0230 1.2888 1.1086 0.2314  0.0546  -0.0426 227 PRO A C   
1579 O O   . PRO A 222 ? 1.0178 1.3004 1.0978 0.2100  0.0744  -0.0282 227 PRO A O   
1580 C CB  . PRO A 222 ? 0.8624 1.0260 0.9317 0.2162  0.0057  -0.0399 227 PRO A CB  
1581 C CG  . PRO A 222 ? 0.8458 0.9917 0.9081 0.1829  0.0080  -0.0228 227 PRO A CG  
1582 C CD  . PRO A 222 ? 0.7794 0.9725 0.8901 0.1593  0.0190  -0.0096 227 PRO A CD  
1583 N N   . TYR A 223 ? 1.0759 1.3376 1.1416 0.2701  0.0527  -0.0636 228 TYR A N   
1584 C CA  . TYR A 223 ? 1.0331 1.3104 1.0643 0.2936  0.0741  -0.0754 228 TYR A CA  
1585 C C   . TYR A 223 ? 1.0992 1.4654 1.1661 0.2904  0.1106  -0.0697 228 TYR A C   
1586 O O   . TYR A 223 ? 1.2452 1.6243 1.2793 0.2909  0.1347  -0.0673 228 TYR A O   
1587 C CB  . TYR A 223 ? 0.9692 1.1880 0.9385 0.2820  0.0699  -0.0712 228 TYR A CB  
1588 C CG  . TYR A 223 ? 0.9300 1.0681 0.8691 0.2792  0.0363  -0.0765 228 TYR A CG  
1589 C CD1 . TYR A 223 ? 0.9035 0.9970 0.8148 0.3102  0.0189  -0.0993 228 TYR A CD1 
1590 C CD2 . TYR A 223 ? 0.9345 1.0398 0.8729 0.2450  0.0228  -0.0590 228 TYR A CD2 
1591 C CE1 . TYR A 223 ? 0.9180 0.9365 0.8024 0.3021  -0.0100 -0.1029 228 TYR A CE1 
1592 C CE2 . TYR A 223 ? 0.9127 0.9524 0.8286 0.2395  -0.0051 -0.0639 228 TYR A CE2 
1593 C CZ  . TYR A 223 ? 0.9100 0.9064 0.7992 0.2653  -0.0209 -0.0850 228 TYR A CZ  
1594 O OH  . TYR A 223 ? 0.8818 0.8134 0.7506 0.2543  -0.0464 -0.0884 228 TYR A OH  
1595 N N   . GLU A 224 ? 1.1660 1.5942 1.2996 0.2849  0.1141  -0.0671 229 GLU A N   
1596 C CA  . GLU A 224 ? 1.1005 1.6236 1.2832 0.2769  0.1481  -0.0622 229 GLU A CA  
1597 C C   . GLU A 224 ? 1.1363 1.6698 1.3095 0.2354  0.1744  -0.0369 229 GLU A C   
1598 O O   . GLU A 224 ? 1.1608 1.7586 1.3476 0.2320  0.2097  -0.0329 229 GLU A O   
1599 C CB  . GLU A 224 ? 0.9974 1.5664 1.1744 0.3226  0.1678  -0.0855 229 GLU A CB  
1600 C CG  . GLU A 224 ? 1.1059 1.6652 1.2924 0.3698  0.1429  -0.1108 229 GLU A CG  
1601 C CD  . GLU A 224 ? 1.0693 1.7042 1.3362 0.3760  0.1369  -0.1146 229 GLU A CD  
1602 O OE1 . GLU A 224 ? 1.0896 1.7419 1.3690 0.4228  0.1270  -0.1365 229 GLU A OE1 
1603 O OE2 . GLU A 224 ? 1.0242 1.6997 1.3410 0.3363  0.1399  -0.0975 229 GLU A OE2 
1604 N N   . ASN A 225 ? 1.1818 1.6527 1.3321 0.2046  0.1580  -0.0191 230 ASN A N   
1605 C CA  . ASN A 225 ? 1.2394 1.6940 1.3633 0.1708  0.1755  0.0060  230 ASN A CA  
1606 C C   . ASN A 225 ? 1.3828 1.8296 1.4418 0.1852  0.1986  0.0070  230 ASN A C   
1607 O O   . ASN A 225 ? 1.4379 1.9023 1.4839 0.1622  0.2262  0.0280  230 ASN A O   
1608 C CB  . ASN A 225 ? 1.1836 1.6949 1.3679 0.1329  0.1949  0.0239  230 ASN A CB  
1609 C CG  . ASN A 225 ? 1.1819 1.6597 1.3963 0.1075  0.1665  0.0307  230 ASN A CG  
1610 O OD1 . ASN A 225 ? 1.1523 1.6671 1.4209 0.1080  0.1552  0.0205  230 ASN A OD1 
1611 N ND2 . ASN A 225 ? 1.1783 1.5896 1.3573 0.0878  0.1546  0.0464  230 ASN A ND2 
1612 N N   . ALA A 226 ? 1.4336 1.8493 1.4484 0.2228  0.1863  -0.0160 231 ALA A N   
1613 C CA  . ALA A 226 ? 1.3360 1.7421 1.2831 0.2428  0.2043  -0.0219 231 ALA A CA  
1614 C C   . ALA A 226 ? 1.3230 1.6660 1.2113 0.2217  0.1942  -0.0026 231 ALA A C   
1615 O O   . ALA A 226 ? 1.1159 1.4022 1.0000 0.2115  0.1615  -0.0003 231 ALA A O   
1616 C CB  . ALA A 226 ? 1.2224 1.6021 1.1372 0.2883  0.1885  -0.0551 231 ALA A CB  
1617 N N   . ILE A 227 ? 1.4043 1.7597 1.2472 0.2165  0.2224  0.0115  232 ILE A N   
1618 C CA  . ILE A 227 ? 1.4541 1.7528 1.2349 0.2010  0.2128  0.0314  232 ILE A CA  
1619 C C   . ILE A 227 ? 1.5805 1.8133 1.3099 0.2231  0.1760  0.0102  232 ILE A C   
1620 O O   . ILE A 227 ? 1.6955 1.9262 1.4014 0.2561  0.1727  -0.0191 232 ILE A O   
1621 C CB  . ILE A 227 ? 1.4110 1.7317 1.1374 0.1992  0.2498  0.0477  232 ILE A CB  
1622 C CG1 . ILE A 227 ? 1.5052 1.8994 1.2769 0.1794  0.2932  0.0647  232 ILE A CG1 
1623 C CG2 . ILE A 227 ? 1.5351 1.7972 1.2017 0.1826  0.2367  0.0726  232 ILE A CG2 
1624 C CD1 . ILE A 227 ? 1.5833 2.0057 1.2966 0.1844  0.3346  0.0752  232 ILE A CD1 
1625 N N   . ALA A 228 ? 1.6508 1.8307 1.3659 0.2051  0.1478  0.0235  233 ALA A N   
1626 C CA  . ALA A 228 ? 1.6043 1.7260 1.2902 0.2173  0.1084  0.0041  233 ALA A CA  
1627 C C   . ALA A 228 ? 1.6793 1.7740 1.2811 0.2387  0.1041  -0.0087 233 ALA A C   
1628 O O   . ALA A 228 ? 1.6981 1.7528 1.2581 0.2324  0.0817  -0.0017 233 ALA A O   
1629 C CB  . ALA A 228 ? 1.5401 1.6268 1.2490 0.1915  0.0815  0.0209  233 ALA A CB  
1630 N N   . GLU A 229 ? 1.6389 1.7571 1.2176 0.2670  0.1235  -0.0310 234 GLU A N   
1631 C CA  . GLU A 229 ? 1.6329 1.7355 1.1285 0.2907  0.1278  -0.0460 234 GLU A CA  
1632 C C   . GLU A 229 ? 1.5545 1.5992 1.0201 0.3080  0.0880  -0.0785 234 GLU A C   
1633 O O   . GLU A 229 ? 1.4853 1.5087 0.9971 0.3033  0.0643  -0.0885 234 GLU A O   
1634 C CB  . GLU A 229 ? 1.7400 1.8981 1.2286 0.3154  0.1694  -0.0583 234 GLU A CB  
1635 C CG  . GLU A 229 ? 1.7677 1.9849 1.2735 0.2933  0.2137  -0.0236 234 GLU A CG  
1636 C CD  . GLU A 229 ? 1.8192 2.0158 1.2568 0.2777  0.2215  0.0052  234 GLU A CD  
1637 O OE1 . GLU A 229 ? 1.8817 2.0392 1.2373 0.2958  0.2069  -0.0069 234 GLU A OE1 
1638 O OE2 . GLU A 229 ? 1.8000 2.0171 1.2640 0.2469  0.2414  0.0407  234 GLU A OE2 
1639 N N   . GLN A 230 ? 1.5621 1.5804 0.9470 0.3268  0.0817  -0.0952 235 GLN A N   
1640 C CA  . GLN A 230 ? 1.5880 1.5480 0.9349 0.3413  0.0436  -0.1288 235 GLN A CA  
1641 C C   . GLN A 230 ? 1.5297 1.4795 0.8984 0.3665  0.0416  -0.1619 235 GLN A C   
1642 O O   . GLN A 230 ? 1.5068 1.4047 0.8790 0.3650  0.0069  -0.1812 235 GLN A O   
1643 C CB  . GLN A 230 ? 1.7267 1.6646 0.9761 0.3583  0.0391  -0.1422 235 GLN A CB  
1644 C CG  . GLN A 230 ? 1.7614 1.6359 0.9719 0.3573  -0.0102 -0.1667 235 GLN A CG  
1645 C CD  . GLN A 230 ? 1.6470 1.5069 0.8826 0.3251  -0.0412 -0.1421 235 GLN A CD  
1646 O OE1 . GLN A 230 ? 1.4599 1.3016 0.7521 0.3075  -0.0651 -0.1442 235 GLN A OE1 
1647 N NE2 . GLN A 230 ? 1.6946 1.5623 0.8862 0.3190  -0.0401 -0.1184 235 GLN A NE2 
1648 N N   . GLN A 231 ? 1.5091 1.5074 0.8920 0.3897  0.0780  -0.1682 236 GLN A N   
1649 C CA  . GLN A 231 ? 1.5377 1.5310 0.9493 0.4179  0.0767  -0.1966 236 GLN A CA  
1650 C C   . GLN A 231 ? 1.4734 1.4539 0.9596 0.3974  0.0553  -0.1857 236 GLN A C   
1651 O O   . GLN A 231 ? 1.5874 1.5146 1.0741 0.4072  0.0275  -0.2072 236 GLN A O   
1652 C CB  . GLN A 231 ? 1.5076 1.5731 0.9370 0.4446  0.1217  -0.2006 236 GLN A CB  
1653 C CG  . GLN A 231 ? 1.5889 1.6636 0.9407 0.4751  0.1448  -0.2210 236 GLN A CG  
1654 C CD  . GLN A 231 ? 1.6042 1.7547 0.9793 0.5068  0.1899  -0.2314 236 GLN A CD  
1655 O OE1 . GLN A 231 ? 1.5392 1.7501 0.9941 0.4990  0.2082  -0.2157 236 GLN A OE1 
1656 N NE2 . GLN A 231 ? 1.6932 1.8445 0.9986 0.5435  0.2079  -0.2598 236 GLN A NE2 
1657 N N   . LEU A 232 ? 1.3689 1.3930 0.9122 0.3680  0.0681  -0.1521 237 LEU A N   
1658 C CA  . LEU A 232 ? 1.3097 1.3264 0.9203 0.3470  0.0503  -0.1397 237 LEU A CA  
1659 C C   . LEU A 232 ? 1.3640 1.3159 0.9621 0.3244  0.0112  -0.1392 237 LEU A C   
1660 O O   . LEU A 232 ? 1.3791 1.2918 0.9967 0.3244  -0.0120 -0.1502 237 LEU A O   
1661 C CB  . LEU A 232 ? 1.2348 1.3107 0.9042 0.3197  0.0726  -0.1064 237 LEU A CB  
1662 C CG  . LEU A 232 ? 1.1575 1.2326 0.8945 0.2983  0.0573  -0.0936 237 LEU A CG  
1663 C CD1 . LEU A 232 ? 1.1349 1.2114 0.9012 0.3244  0.0513  -0.1137 237 LEU A CD1 
1664 C CD2 . LEU A 232 ? 1.0649 1.1939 0.8511 0.2704  0.0790  -0.0637 237 LEU A CD2 
1665 N N   . ILE A 233 ? 1.3745 1.3176 0.9406 0.3057  0.0047  -0.1254 238 ILE A N   
1666 C CA  . ILE A 233 ? 1.2885 1.1832 0.8465 0.2835  -0.0315 -0.1246 238 ILE A CA  
1667 C C   . ILE A 233 ? 1.2729 1.1081 0.7975 0.2979  -0.0592 -0.1586 238 ILE A C   
1668 O O   . ILE A 233 ? 1.2091 1.0100 0.7621 0.2830  -0.0825 -0.1618 238 ILE A O   
1669 C CB  . ILE A 233 ? 1.3547 1.2518 0.8714 0.2716  -0.0352 -0.1090 238 ILE A CB  
1670 C CG1 . ILE A 233 ? 1.2728 1.2117 0.8280 0.2502  -0.0143 -0.0717 238 ILE A CG1 
1671 C CG2 . ILE A 233 ? 1.3698 1.2226 0.8749 0.2551  -0.0757 -0.1158 238 ILE A CG2 
1672 C CD1 . ILE A 233 ? 1.2490 1.1959 0.7561 0.2467  -0.0062 -0.0522 238 ILE A CD1 
1673 N N   . MET A 234 ? 1.3580 1.1799 0.8212 0.3263  -0.0546 -0.1838 239 MET A N   
1674 C CA  . MET A 234 ? 1.4218 1.1788 0.8442 0.3419  -0.0812 -0.2202 239 MET A CA  
1675 C C   . MET A 234 ? 1.3839 1.1176 0.8359 0.3589  -0.0818 -0.2347 239 MET A C   
1676 O O   . MET A 234 ? 1.4685 1.1362 0.9059 0.3574  -0.1102 -0.2554 239 MET A O   
1677 C CB  . MET A 234 ? 1.5243 1.2703 0.8655 0.3708  -0.0761 -0.2466 239 MET A CB  
1678 C CG  . MET A 234 ? 1.5735 1.3225 0.8696 0.3557  -0.0877 -0.2372 239 MET A CG  
1679 S SD  . MET A 234 ? 1.6625 1.3512 0.9530 0.3257  -0.1420 -0.2495 239 MET A SD  
1680 C CE  . MET A 234 ? 1.7932 1.4155 1.0040 0.3548  -0.1617 -0.3020 239 MET A CE  
1681 N N   . ALA A 235 ? 1.2879 1.0730 0.7806 0.3744  -0.0527 -0.2238 240 ALA A N   
1682 C CA  . ALA A 235 ? 1.2281 0.9971 0.7563 0.3906  -0.0558 -0.2317 240 ALA A CA  
1683 C C   . ALA A 235 ? 1.1849 0.9260 0.7583 0.3569  -0.0785 -0.2136 240 ALA A C   
1684 O O   . ALA A 235 ? 1.1805 0.8612 0.7490 0.3604  -0.0999 -0.2266 240 ALA A O   
1685 C CB  . ALA A 235 ? 1.1673 1.0103 0.7360 0.4126  -0.0216 -0.2233 240 ALA A CB  
1686 N N   . ILE A 236 ? 1.1260 0.9066 0.7376 0.3243  -0.0731 -0.1838 241 ILE A N   
1687 C CA  . ILE A 236 ? 1.0648 0.8275 0.7184 0.2913  -0.0906 -0.1658 241 ILE A CA  
1688 C C   . ILE A 236 ? 1.0871 0.7842 0.7138 0.2715  -0.1227 -0.1779 241 ILE A C   
1689 O O   . ILE A 236 ? 1.0368 0.6921 0.6796 0.2592  -0.1389 -0.1780 241 ILE A O   
1690 C CB  . ILE A 236 ? 0.9900 0.8085 0.6868 0.2641  -0.0768 -0.1342 241 ILE A CB  
1691 C CG1 . ILE A 236 ? 0.9654 0.8455 0.7016 0.2769  -0.0484 -0.1226 241 ILE A CG1 
1692 C CG2 . ILE A 236 ? 0.9285 0.7283 0.6617 0.2310  -0.0947 -0.1189 241 ILE A CG2 
1693 C CD1 . ILE A 236 ? 0.9642 0.8989 0.7255 0.2565  -0.0283 -0.0966 241 ILE A CD1 
1694 N N   . LYS A 237 ? 1.1062 0.7964 0.6919 0.2677  -0.1315 -0.1874 242 LYS A N   
1695 C CA  . LYS A 237 ? 1.1945 0.8273 0.7512 0.2503  -0.1641 -0.2050 242 LYS A CA  
1696 C C   . LYS A 237 ? 1.3344 0.8951 0.8610 0.2663  -0.1797 -0.2338 242 LYS A C   
1697 O O   . LYS A 237 ? 1.3663 0.8756 0.8983 0.2423  -0.2037 -0.2389 242 LYS A O   
1698 C CB  . LYS A 237 ? 1.2780 0.9180 0.7843 0.2539  -0.1713 -0.2157 242 LYS A CB  
1699 C CG  . LYS A 237 ? 1.2383 0.9301 0.7638 0.2354  -0.1655 -0.1883 242 LYS A CG  
1700 C CD  . LYS A 237 ? 1.2344 0.9129 0.7797 0.2022  -0.1956 -0.1845 242 LYS A CD  
1701 C CE  . LYS A 237 ? 1.3032 0.9572 0.7945 0.2026  -0.2233 -0.2074 242 LYS A CE  
1702 N NZ  . LYS A 237 ? 1.3272 0.9965 0.8487 0.1725  -0.2479 -0.1964 242 LYS A NZ  
1703 N N   . SER A 238 ? 1.3938 0.9511 0.8899 0.3067  -0.1647 -0.2519 243 SER A N   
1704 C CA  . SER A 238 ? 1.5054 0.9907 0.9692 0.3306  -0.1776 -0.2802 243 SER A CA  
1705 C C   . SER A 238 ? 1.5147 0.9730 1.0158 0.3306  -0.1797 -0.2685 243 SER A C   
1706 O O   . SER A 238 ? 1.8155 1.1990 1.2881 0.3451  -0.1954 -0.2887 243 SER A O   
1707 C CB  . SER A 238 ? 1.5545 1.0493 0.9733 0.3798  -0.1594 -0.3055 243 SER A CB  
1708 O OG  . SER A 238 ? 1.5041 1.0565 0.9594 0.4063  -0.1302 -0.2932 243 SER A OG  
1709 N N   . GLY A 239 ? 1.3568 0.8694 0.9152 0.3156  -0.1654 -0.2373 244 GLY A N   
1710 C CA  . GLY A 239 ? 1.3252 0.8205 0.9163 0.3173  -0.1667 -0.2236 244 GLY A CA  
1711 C C   . GLY A 239 ? 1.2195 0.7863 0.8553 0.3359  -0.1427 -0.2060 244 GLY A C   
1712 O O   . GLY A 239 ? 1.1246 0.6829 0.7885 0.3328  -0.1464 -0.1915 244 GLY A O   
1713 N N   . ASN A 240 ? 1.2377 0.8744 0.8792 0.3527  -0.1186 -0.2064 245 ASN A N   
1714 C CA  . ASN A 240 ? 1.2468 0.9571 0.9328 0.3715  -0.0949 -0.1943 245 ASN A CA  
1715 C C   . ASN A 240 ? 1.1975 0.9508 0.9377 0.3358  -0.0906 -0.1628 245 ASN A C   
1716 O O   . ASN A 240 ? 1.2950 1.0509 1.0390 0.3013  -0.0941 -0.1494 245 ASN A O   
1717 C CB  . ASN A 240 ? 1.3284 1.1015 1.0036 0.3938  -0.0673 -0.2028 245 ASN A CB  
1718 C CG  . ASN A 240 ? 1.4493 1.2797 1.1558 0.4303  -0.0466 -0.2074 245 ASN A CG  
1719 O OD1 . ASN A 240 ? 1.6901 1.5018 1.3697 0.4726  -0.0456 -0.2334 245 ASN A OD1 
1720 N ND2 . ASN A 240 ? 1.3216 1.2229 1.0862 0.4155  -0.0311 -0.1843 245 ASN A ND2 
1721 N N   . ARG A 241 ? 1.1172 0.9011 0.8975 0.3465  -0.0855 -0.1532 246 ARG A N   
1722 C CA  . ARG A 241 ? 1.0047 0.8181 0.8321 0.3162  -0.0854 -0.1273 246 ARG A CA  
1723 C C   . ARG A 241 ? 0.9885 0.8801 0.8631 0.3315  -0.0670 -0.1207 246 ARG A C   
1724 O O   . ARG A 241 ? 1.0055 0.9271 0.8790 0.3670  -0.0551 -0.1361 246 ARG A O   
1725 C CB  . ARG A 241 ? 0.9938 0.7414 0.8149 0.3067  -0.1089 -0.1225 246 ARG A CB  
1726 C CG  . ARG A 241 ? 1.0053 0.6821 0.7918 0.2810  -0.1269 -0.1260 246 ARG A CG  
1727 C CD  . ARG A 241 ? 0.9276 0.6310 0.7334 0.2407  -0.1236 -0.1101 246 ARG A CD  
1728 N NE  . ARG A 241 ? 0.8912 0.5378 0.6714 0.2165  -0.1416 -0.1157 246 ARG A NE  
1729 C CZ  . ARG A 241 ? 0.9718 0.6001 0.7196 0.2156  -0.1485 -0.1318 246 ARG A CZ  
1730 N NH1 . ARG A 241 ? 0.9627 0.6213 0.6912 0.2392  -0.1367 -0.1435 246 ARG A NH1 
1731 N NH2 . ARG A 241 ? 1.0304 0.6113 0.7641 0.1889  -0.1678 -0.1367 246 ARG A NH2 
1732 N N   . PRO A 242 ? 1.0306 0.9590 0.9486 0.3047  -0.0642 -0.0997 247 PRO A N   
1733 C CA  . PRO A 242 ? 0.9967 0.9998 0.9637 0.3159  -0.0505 -0.0954 247 PRO A CA  
1734 C C   . PRO A 242 ? 1.0716 1.0668 1.0448 0.3527  -0.0638 -0.1064 247 PRO A C   
1735 O O   . PRO A 242 ? 1.1580 1.0846 1.1055 0.3563  -0.0863 -0.1066 247 PRO A O   
1736 C CB  . PRO A 242 ? 0.9776 1.0004 0.9792 0.2772  -0.0516 -0.0736 247 PRO A CB  
1737 C CG  . PRO A 242 ? 0.9336 0.9165 0.9086 0.2483  -0.0546 -0.0663 247 PRO A CG  
1738 C CD  . PRO A 242 ? 1.0261 0.9384 0.9534 0.2636  -0.0713 -0.0812 247 PRO A CD  
1739 N N   . ASP A 243 ? 1.0354 1.1015 1.0428 0.3797  -0.0495 -0.1145 248 ASP A N   
1740 C CA  . ASP A 243 ? 1.0501 1.1184 1.0646 0.4248  -0.0612 -0.1286 248 ASP A CA  
1741 C C   . ASP A 243 ? 1.0596 1.1265 1.1004 0.4167  -0.0820 -0.1148 248 ASP A C   
1742 O O   . ASP A 243 ? 0.9906 1.1223 1.0795 0.3946  -0.0753 -0.1033 248 ASP A O   
1743 C CB  . ASP A 243 ? 1.0646 1.2264 1.1180 0.4536  -0.0369 -0.1415 248 ASP A CB  
1744 C CG  . ASP A 243 ? 1.0943 1.2532 1.1437 0.5123  -0.0463 -0.1636 248 ASP A CG  
1745 O OD1 . ASP A 243 ? 1.1386 1.2296 1.1641 0.5314  -0.0747 -0.1651 248 ASP A OD1 
1746 O OD2 . ASP A 243 ? 1.0413 1.2675 1.1112 0.5409  -0.0237 -0.1792 248 ASP A OD2 
1747 N N   . VAL A 244 ? 1.1051 1.0928 1.1093 0.4319  -0.1075 -0.1155 249 VAL A N   
1748 C CA  . VAL A 244 ? 1.0849 1.0586 1.0991 0.4261  -0.1290 -0.1012 249 VAL A CA  
1749 C C   . VAL A 244 ? 1.1010 1.1464 1.1608 0.4631  -0.1348 -0.1082 249 VAL A C   
1750 O O   . VAL A 244 ? 1.1359 1.2159 1.2263 0.4502  -0.1449 -0.0969 249 VAL A O   
1751 C CB  . VAL A 244 ? 1.1513 1.0131 1.1065 0.4294  -0.1527 -0.0968 249 VAL A CB  
1752 C CG1 . VAL A 244 ? 1.1811 1.0261 1.1375 0.4241  -0.1733 -0.0799 249 VAL A CG1 
1753 C CG2 . VAL A 244 ? 1.1259 0.9317 1.0480 0.3886  -0.1476 -0.0909 249 VAL A CG2 
1754 N N   . ASP A 245 ? 1.0864 1.1567 1.1512 0.5096  -0.1292 -0.1284 250 ASP A N   
1755 C CA  . ASP A 245 ? 1.1050 1.2612 1.2236 0.5480  -0.1319 -0.1385 250 ASP A CA  
1756 C C   . ASP A 245 ? 1.0594 1.3352 1.2506 0.5224  -0.1095 -0.1354 250 ASP A C   
1757 O O   . ASP A 245 ? 1.1544 1.5069 1.3993 0.5422  -0.1166 -0.1402 250 ASP A O   
1758 C CB  . ASP A 245 ? 1.1634 1.3189 1.2699 0.6069  -0.1279 -0.1636 250 ASP A CB  
1759 C CG  . ASP A 245 ? 1.1999 1.2329 1.2365 0.6383  -0.1539 -0.1688 250 ASP A CG  
1760 O OD1 . ASP A 245 ? 1.2167 1.1888 1.2301 0.6334  -0.1810 -0.1532 250 ASP A OD1 
1761 O OD2 . ASP A 245 ? 1.2531 1.2472 1.2541 0.6672  -0.1466 -0.1885 250 ASP A OD2 
1762 N N   . ASP A 246 ? 1.0830 1.3746 1.2765 0.4797  -0.0839 -0.1279 251 ASP A N   
1763 C CA  . ASP A 246 ? 1.0746 1.4610 1.3303 0.4435  -0.0637 -0.1194 251 ASP A CA  
1764 C C   . ASP A 246 ? 0.9833 1.3754 1.2628 0.4108  -0.0828 -0.1041 251 ASP A C   
1765 O O   . ASP A 246 ? 0.9570 1.4313 1.2951 0.3898  -0.0740 -0.1017 251 ASP A O   
1766 C CB  . ASP A 246 ? 1.1265 1.5146 1.3688 0.4065  -0.0334 -0.1120 251 ASP A CB  
1767 C CG  . ASP A 246 ? 1.1800 1.6228 1.4301 0.4296  -0.0028 -0.1264 251 ASP A CG  
1768 O OD1 . ASP A 246 ? 1.3421 1.8001 1.5924 0.4793  -0.0044 -0.1460 251 ASP A OD1 
1769 O OD2 . ASP A 246 ? 1.1989 1.6671 1.4509 0.3985  0.0240  -0.1174 251 ASP A OD2 
1770 N N   . ILE A 247 ? 0.9596 1.2652 1.1928 0.4051  -0.1075 -0.0946 252 ILE A N   
1771 C CA  . ILE A 247 ? 0.8910 1.1969 1.1370 0.3849  -0.1291 -0.0833 252 ILE A CA  
1772 C C   . ILE A 247 ? 0.9108 1.2630 1.1873 0.4273  -0.1518 -0.0933 252 ILE A C   
1773 O O   . ILE A 247 ? 0.8943 1.1911 1.1329 0.4675  -0.1722 -0.0971 252 ILE A O   
1774 C CB  . ILE A 247 ? 0.8384 1.0404 1.0223 0.3678  -0.1454 -0.0697 252 ILE A CB  
1775 C CG1 . ILE A 247 ? 0.8170 0.9844 0.9793 0.3282  -0.1254 -0.0614 252 ILE A CG1 
1776 C CG2 . ILE A 247 ? 0.7810 0.9860 0.9723 0.3506  -0.1660 -0.0596 252 ILE A CG2 
1777 C CD1 . ILE A 247 ? 0.9201 0.9893 1.0232 0.3164  -0.1366 -0.0521 252 ILE A CD1 
1778 N N   . THR A 248 ? 0.8729 1.3245 1.2175 0.4177  -0.1489 -0.0976 253 THR A N   
1779 C CA  . THR A 248 ? 0.9328 1.4497 1.3206 0.4551  -0.1719 -0.1086 253 THR A CA  
1780 C C   . THR A 248 ? 0.9624 1.4557 1.3378 0.4464  -0.2062 -0.0995 253 THR A C   
1781 O O   . THR A 248 ? 1.0100 1.4948 1.3754 0.4883  -0.2362 -0.1031 253 THR A O   
1782 C CB  . THR A 248 ? 0.9136 1.5599 1.3881 0.4474  -0.1521 -0.1199 253 THR A CB  
1783 O OG1 . THR A 248 ? 0.8342 1.5074 1.3357 0.3887  -0.1407 -0.1100 253 THR A OG1 
1784 C CG2 . THR A 248 ? 0.9108 1.5850 1.3923 0.4644  -0.1174 -0.1299 253 THR A CG2 
1785 N N   . GLU A 249 ? 0.9620 1.4439 1.3351 0.3951  -0.2021 -0.0883 254 GLU A N   
1786 C CA  . GLU A 249 ? 0.9345 1.3826 1.2823 0.3827  -0.2313 -0.0797 254 GLU A CA  
1787 C C   . GLU A 249 ? 0.8910 1.2237 1.1548 0.3973  -0.2473 -0.0667 254 GLU A C   
1788 O O   . GLU A 249 ? 0.8494 1.1200 1.0741 0.4059  -0.2343 -0.0637 254 GLU A O   
1789 C CB  . GLU A 249 ? 0.8814 1.3442 1.2465 0.3254  -0.2200 -0.0739 254 GLU A CB  
1790 C CG  . GLU A 249 ? 0.9008 1.2969 1.2272 0.2900  -0.1950 -0.0621 254 GLU A CG  
1791 C CD  . GLU A 249 ? 0.9164 1.3128 1.2500 0.2420  -0.1919 -0.0570 254 GLU A CD  
1792 O OE1 . GLU A 249 ? 0.8800 1.3492 1.2711 0.2203  -0.1869 -0.0642 254 GLU A OE1 
1793 O OE2 . GLU A 249 ? 0.8940 1.2173 1.1765 0.2255  -0.1938 -0.0465 254 GLU A OE2 
1794 N N   . TYR A 250 ? 0.9206 1.2259 1.1559 0.3972  -0.2753 -0.0591 255 TYR A N   
1795 C CA  . TYR A 250 ? 0.9894 1.1878 1.1439 0.4068  -0.2905 -0.0436 255 TYR A CA  
1796 C C   . TYR A 250 ? 1.0111 1.1426 1.1264 0.3627  -0.2680 -0.0312 255 TYR A C   
1797 O O   . TYR A 250 ? 0.9786 1.1205 1.0992 0.3240  -0.2623 -0.0273 255 TYR A O   
1798 C CB  . TYR A 250 ? 1.0759 1.2687 1.2073 0.4157  -0.3246 -0.0376 255 TYR A CB  
1799 C CG  . TYR A 250 ? 1.2235 1.3036 1.2661 0.4183  -0.3360 -0.0176 255 TYR A CG  
1800 C CD1 . TYR A 250 ? 1.3623 1.3688 1.3574 0.4566  -0.3451 -0.0109 255 TYR A CD1 
1801 C CD2 . TYR A 250 ? 1.2733 1.3168 1.2775 0.3810  -0.3350 -0.0054 255 TYR A CD2 
1802 C CE1 . TYR A 250 ? 1.4366 1.3356 1.3495 0.4538  -0.3532 0.0099  255 TYR A CE1 
1803 C CE2 . TYR A 250 ? 1.4034 1.3473 1.3267 0.3797  -0.3408 0.0146  255 TYR A CE2 
1804 C CZ  . TYR A 250 ? 1.4962 1.3673 1.3744 0.4140  -0.3497 0.0236  255 TYR A CZ  
1805 O OH  . TYR A 250 ? 1.6163 1.3855 1.4142 0.4087  -0.3538 0.0456  255 TYR A OH  
1806 N N   . CYS A 251 ? 1.0616 1.1289 1.1414 0.3705  -0.2558 -0.0276 256 CYS A N   
1807 C CA  . CYS A 251 ? 1.0359 1.0266 1.0689 0.3370  -0.2415 -0.0148 256 CYS A CA  
1808 C C   . CYS A 251 ? 1.0659 0.9616 1.0289 0.3564  -0.2603 -0.0015 256 CYS A C   
1809 O O   . CYS A 251 ? 1.1776 1.0464 1.1246 0.3977  -0.2730 -0.0057 256 CYS A O   
1810 C CB  . CYS A 251 ? 1.0193 1.0050 1.0619 0.3273  -0.2159 -0.0210 256 CYS A CB  
1811 S SG  . CYS A 251 ? 1.0101 0.9206 1.0100 0.2834  -0.1999 -0.0079 256 CYS A SG  
1812 N N   . PRO A 252 ? 1.0404 0.8826 0.9592 0.3279  -0.2615 0.0148  257 PRO A N   
1813 C CA  . PRO A 252 ? 1.1039 0.8464 0.9507 0.3374  -0.2736 0.0314  257 PRO A CA  
1814 C C   . PRO A 252 ? 1.1085 0.7824 0.9287 0.3386  -0.2633 0.0314  257 PRO A C   
1815 O O   . PRO A 252 ? 1.1078 0.8042 0.9570 0.3200  -0.2427 0.0214  257 PRO A O   
1816 C CB  . PRO A 252 ? 1.1122 0.8302 0.9295 0.2963  -0.2659 0.0465  257 PRO A CB  
1817 C CG  . PRO A 252 ? 1.1035 0.9065 0.9675 0.2860  -0.2672 0.0367  257 PRO A CG  
1818 C CD  . PRO A 252 ? 1.0290 0.9045 0.9604 0.2918  -0.2558 0.0182  257 PRO A CD  
1819 N N   . ARG A 253 ? 1.2125 0.7993 0.9741 0.3603  -0.2796 0.0426  258 ARG A N   
1820 C CA  . ARG A 253 ? 1.2621 0.7662 0.9881 0.3605  -0.2746 0.0427  258 ARG A CA  
1821 C C   . ARG A 253 ? 1.2021 0.6762 0.9182 0.3069  -0.2524 0.0502  258 ARG A C   
1822 O O   . ARG A 253 ? 1.2107 0.6703 0.9347 0.2972  -0.2408 0.0393  258 ARG A O   
1823 C CB  . ARG A 253 ? 1.3623 0.7677 1.0203 0.3904  -0.2985 0.0575  258 ARG A CB  
1824 C CG  . ARG A 253 ? 1.3700 0.7929 1.0351 0.4516  -0.3230 0.0475  258 ARG A CG  
1825 C CD  . ARG A 253 ? 1.4881 0.8033 1.0780 0.4799  -0.3484 0.0665  258 ARG A CD  
1826 N NE  . ARG A 253 ? 1.5294 0.8657 1.1268 0.5441  -0.3760 0.0579  258 ARG A NE  
1827 C CZ  . ARG A 253 ? 1.6375 0.8882 1.1733 0.5823  -0.4037 0.0727  258 ARG A CZ  
1828 N NH1 . ARG A 253 ? 1.7177 0.8518 1.1769 0.5586  -0.4052 0.0987  258 ARG A NH1 
1829 N NH2 . ARG A 253 ? 1.6713 0.9537 1.2229 0.6445  -0.4298 0.0623  258 ARG A NH2 
1830 N N   . GLU A 254 ? 1.1704 0.6413 0.8710 0.2746  -0.2471 0.0669  259 GLU A N   
1831 C CA  . GLU A 254 ? 1.1946 0.6496 0.8922 0.2245  -0.2254 0.0743  259 GLU A CA  
1832 C C   . GLU A 254 ? 1.1101 0.6338 0.8659 0.2049  -0.2063 0.0576  259 GLU A C   
1833 O O   . GLU A 254 ? 1.1737 0.6729 0.9294 0.1810  -0.1947 0.0551  259 GLU A O   
1834 C CB  . GLU A 254 ? 1.1881 0.6450 0.8640 0.1993  -0.2210 0.0919  259 GLU A CB  
1835 C CG  . GLU A 254 ? 1.3329 0.6996 0.9358 0.1977  -0.2301 0.1161  259 GLU A CG  
1836 C CD  . GLU A 254 ? 1.3955 0.7350 0.9611 0.2433  -0.2588 0.1235  259 GLU A CD  
1837 O OE1 . GLU A 254 ? 1.2829 0.6888 0.8833 0.2744  -0.2728 0.1102  259 GLU A OE1 
1838 O OE2 . GLU A 254 ? 1.5216 0.7698 1.0216 0.2473  -0.2681 0.1438  259 GLU A OE2 
1839 N N   . ILE A 255 ? 1.0315 0.6378 0.8344 0.2153  -0.2049 0.0468  260 ILE A N   
1840 C CA  . ILE A 255 ? 0.9758 0.6459 0.8304 0.1991  -0.1873 0.0337  260 ILE A CA  
1841 C C   . ILE A 255 ? 1.0138 0.6801 0.8777 0.2176  -0.1848 0.0189  260 ILE A C   
1842 O O   . ILE A 255 ? 0.9715 0.6487 0.8512 0.1970  -0.1708 0.0132  260 ILE A O   
1843 C CB  . ILE A 255 ? 0.8952 0.6488 0.7955 0.2017  -0.1863 0.0274  260 ILE A CB  
1844 C CG1 . ILE A 255 ? 0.8289 0.5862 0.7194 0.1759  -0.1842 0.0377  260 ILE A CG1 
1845 C CG2 . ILE A 255 ? 0.8387 0.6506 0.7876 0.1896  -0.1688 0.0158  260 ILE A CG2 
1846 C CD1 . ILE A 255 ? 0.7674 0.5859 0.6864 0.1795  -0.1910 0.0322  260 ILE A CD1 
1847 N N   . ILE A 256 ? 1.0190 0.6708 0.8713 0.2584  -0.1991 0.0119  261 ILE A N   
1848 C CA  . ILE A 256 ? 1.0554 0.6963 0.9075 0.2809  -0.1969 -0.0045 261 ILE A CA  
1849 C C   . ILE A 256 ? 1.1303 0.6868 0.9402 0.2627  -0.1969 -0.0030 261 ILE A C   
1850 O O   . ILE A 256 ? 1.1329 0.6912 0.9483 0.2582  -0.1884 -0.0163 261 ILE A O   
1851 C CB  . ILE A 256 ? 1.1035 0.7517 0.9551 0.3338  -0.2121 -0.0147 261 ILE A CB  
1852 C CG1 . ILE A 256 ? 1.0722 0.8249 0.9823 0.3451  -0.2076 -0.0215 261 ILE A CG1 
1853 C CG2 . ILE A 256 ? 1.1283 0.7502 0.9673 0.3608  -0.2102 -0.0334 261 ILE A CG2 
1854 C CD1 . ILE A 256 ? 1.2130 0.9852 1.1292 0.3922  -0.2279 -0.0260 261 ILE A CD1 
1855 N N   . SER A 257 ? 1.1896 0.6728 0.9561 0.2509  -0.2067 0.0131  262 SER A N   
1856 C CA  . SER A 257 ? 1.2791 0.6851 1.0109 0.2224  -0.2055 0.0170  262 SER A CA  
1857 C C   . SER A 257 ? 1.2463 0.6873 1.0063 0.1768  -0.1880 0.0176  262 SER A C   
1858 O O   . SER A 257 ? 1.2774 0.6926 1.0325 0.1608  -0.1858 0.0084  262 SER A O   
1859 C CB  . SER A 257 ? 1.2971 0.6227 0.9781 0.2139  -0.2158 0.0383  262 SER A CB  
1860 O OG  . SER A 257 ? 1.4584 0.7383 1.1072 0.2595  -0.2355 0.0376  262 SER A OG  
1861 N N   . LEU A 258 ? 1.1284 0.6275 0.9171 0.1588  -0.1777 0.0268  263 LEU A N   
1862 C CA  . LEU A 258 ? 1.0706 0.6074 0.8887 0.1212  -0.1619 0.0280  263 LEU A CA  
1863 C C   . LEU A 258 ? 1.0049 0.5891 0.8556 0.1250  -0.1550 0.0114  263 LEU A C   
1864 O O   . LEU A 258 ? 1.0570 0.6345 0.9125 0.1015  -0.1505 0.0074  263 LEU A O   
1865 C CB  . LEU A 258 ? 1.0717 0.6576 0.9102 0.1085  -0.1537 0.0383  263 LEU A CB  
1866 C CG  . LEU A 258 ? 1.0587 0.6769 0.9235 0.0720  -0.1375 0.0413  263 LEU A CG  
1867 C CD1 . LEU A 258 ? 1.0862 0.6521 0.9255 0.0418  -0.1338 0.0521  263 LEU A CD1 
1868 C CD2 . LEU A 258 ? 1.0599 0.7288 0.9450 0.0687  -0.1310 0.0455  263 LEU A CD2 
1869 N N   . MET A 259 ? 0.8865 0.5199 0.7588 0.1534  -0.1541 0.0024  264 MET A N   
1870 C CA  . MET A 259 ? 0.8693 0.5458 0.7653 0.1582  -0.1452 -0.0110 264 MET A CA  
1871 C C   . MET A 259 ? 0.8511 0.4788 0.7173 0.1693  -0.1520 -0.0250 264 MET A C   
1872 O O   . MET A 259 ? 0.8480 0.4835 0.7181 0.1552  -0.1474 -0.0322 264 MET A O   
1873 C CB  . MET A 259 ? 0.8821 0.6268 0.8104 0.1819  -0.1391 -0.0161 264 MET A CB  
1874 C CG  . MET A 259 ? 0.9827 0.7235 0.9017 0.2236  -0.1482 -0.0255 264 MET A CG  
1875 S SD  . MET A 259 ? 1.0137 0.8514 0.9836 0.2441  -0.1373 -0.0324 264 MET A SD  
1876 C CE  . MET A 259 ? 0.9742 0.8355 0.9624 0.2333  -0.1461 -0.0190 264 MET A CE  
1877 N N   . LYS A 260 ? 0.9553 0.5285 0.7886 0.1953  -0.1649 -0.0293 265 LYS A N   
1878 C CA  . LYS A 260 ? 1.0338 0.5439 0.8305 0.2066  -0.1743 -0.0447 265 LYS A CA  
1879 C C   . LYS A 260 ? 1.0838 0.5457 0.8649 0.1663  -0.1779 -0.0420 265 LYS A C   
1880 O O   . LYS A 260 ? 1.1625 0.6094 0.9330 0.1617  -0.1808 -0.0575 265 LYS A O   
1881 C CB  . LYS A 260 ? 1.1129 0.5626 0.8741 0.2435  -0.1895 -0.0483 265 LYS A CB  
1882 C CG  . LYS A 260 ? 1.1070 0.6035 0.8829 0.2920  -0.1877 -0.0623 265 LYS A CG  
1883 C CD  . LYS A 260 ? 1.1730 0.6088 0.9146 0.3344  -0.2052 -0.0668 265 LYS A CD  
1884 C CE  . LYS A 260 ? 1.1180 0.6125 0.8832 0.3834  -0.2027 -0.0811 265 LYS A CE  
1885 N NZ  . LYS A 260 ? 1.2004 0.6347 0.9330 0.4292  -0.2225 -0.0851 265 LYS A NZ  
1886 N N   . LEU A 261 ? 1.0888 0.5331 0.8701 0.1369  -0.1771 -0.0231 266 LEU A N   
1887 C CA  . LEU A 261 ? 1.1367 0.5524 0.9157 0.0933  -0.1769 -0.0185 266 LEU A CA  
1888 C C   . LEU A 261 ? 1.1206 0.6023 0.9387 0.0720  -0.1672 -0.0232 266 LEU A C   
1889 O O   . LEU A 261 ? 1.1108 0.5790 0.9276 0.0529  -0.1726 -0.0335 266 LEU A O   
1890 C CB  . LEU A 261 ? 1.1910 0.5852 0.9634 0.0683  -0.1728 0.0044  266 LEU A CB  
1891 C CG  . LEU A 261 ? 1.2778 0.6386 1.0472 0.0218  -0.1705 0.0116  266 LEU A CG  
1892 C CD1 . LEU A 261 ? 1.3973 0.6656 1.1241 0.0179  -0.1854 0.0049  266 LEU A CD1 
1893 C CD2 . LEU A 261 ? 1.2599 0.6252 1.0296 -0.0012 -0.1588 0.0347  266 LEU A CD2 
1894 N N   . CYS A 262 ? 1.0833 0.6332 0.9350 0.0752  -0.1550 -0.0157 267 CYS A N   
1895 C CA  . CYS A 262 ? 0.9814 0.5907 0.8685 0.0585  -0.1459 -0.0170 267 CYS A CA  
1896 C C   . CYS A 262 ? 0.9685 0.6006 0.8558 0.0751  -0.1472 -0.0325 267 CYS A C   
1897 O O   . CYS A 262 ? 0.9950 0.6570 0.9002 0.0593  -0.1454 -0.0342 267 CYS A O   
1898 C CB  . CYS A 262 ? 0.9118 0.5766 0.8302 0.0561  -0.1332 -0.0048 267 CYS A CB  
1899 S SG  . CYS A 262 ? 0.9671 0.6152 0.8848 0.0286  -0.1282 0.0124  267 CYS A SG  
1900 N N   . TRP A 263 ? 0.9240 0.5434 0.7899 0.1079  -0.1502 -0.0438 268 TRP A N   
1901 C CA  . TRP A 263 ? 0.9338 0.5671 0.7886 0.1243  -0.1502 -0.0601 268 TRP A CA  
1902 C C   . TRP A 263 ? 1.0030 0.5736 0.8172 0.1294  -0.1656 -0.0792 268 TRP A C   
1903 O O   . TRP A 263 ? 0.9816 0.5561 0.7758 0.1523  -0.1656 -0.0956 268 TRP A O   
1904 C CB  . TRP A 263 ? 0.9011 0.5832 0.7664 0.1557  -0.1374 -0.0623 268 TRP A CB  
1905 C CG  . TRP A 263 ? 0.9228 0.5896 0.7747 0.1904  -0.1394 -0.0692 268 TRP A CG  
1906 C CD1 . TRP A 263 ? 1.0338 0.6379 0.8478 0.2119  -0.1521 -0.0834 268 TRP A CD1 
1907 C CD2 . TRP A 263 ? 0.9039 0.6238 0.7826 0.2113  -0.1289 -0.0647 268 TRP A CD2 
1908 N NE1 . TRP A 263 ? 1.0652 0.6813 0.8815 0.2483  -0.1505 -0.0869 268 TRP A NE1 
1909 C CE2 . TRP A 263 ? 0.9603 0.6520 0.8188 0.2477  -0.1365 -0.0760 268 TRP A CE2 
1910 C CE3 . TRP A 263 ? 0.8607 0.6485 0.7801 0.2021  -0.1150 -0.0530 268 TRP A CE3 
1911 C CZ2 . TRP A 263 ? 0.9349 0.6740 0.8181 0.2760  -0.1313 -0.0761 268 TRP A CZ2 
1912 C CZ3 . TRP A 263 ? 0.8454 0.6771 0.7885 0.2254  -0.1096 -0.0533 268 TRP A CZ3 
1913 C CH2 . TRP A 263 ? 0.8968 0.7089 0.8242 0.2624  -0.1180 -0.0650 268 TRP A CH2 
1914 N N   . GLU A 264 ? 1.0808 0.5935 0.8812 0.1060  -0.1778 -0.0777 269 GLU A N   
1915 C CA  . GLU A 264 ? 1.1606 0.6081 0.9247 0.1009  -0.1951 -0.0968 269 GLU A CA  
1916 C C   . GLU A 264 ? 1.2151 0.6920 0.9798 0.0939  -0.1998 -0.1115 269 GLU A C   
1917 O O   . GLU A 264 ? 1.2735 0.8059 1.0713 0.0752  -0.1938 -0.1013 269 GLU A O   
1918 C CB  . GLU A 264 ? 1.2018 0.5942 0.9621 0.0638  -0.2044 -0.0885 269 GLU A CB  
1919 C CG  . GLU A 264 ? 1.3434 0.6745 1.0790 0.0737  -0.2064 -0.0775 269 GLU A CG  
1920 C CD  . GLU A 264 ? 1.4822 0.7317 1.1675 0.1015  -0.2213 -0.0960 269 GLU A CD  
1921 O OE1 . GLU A 264 ? 1.6183 0.8482 1.2835 0.1072  -0.2315 -0.1201 269 GLU A OE1 
1922 O OE2 . GLU A 264 ? 1.4432 0.6446 1.1056 0.1201  -0.2242 -0.0869 269 GLU A OE2 
1923 N N   . ALA A 265 ? 1.2976 0.7358 1.0219 0.1124  -0.2113 -0.1357 270 ALA A N   
1924 C CA  . ALA A 265 ? 1.2309 0.6878 0.9432 0.1086  -0.2198 -0.1522 270 ALA A CA  
1925 C C   . ALA A 265 ? 1.2570 0.7164 0.9921 0.0645  -0.2337 -0.1495 270 ALA A C   
1926 O O   . ALA A 265 ? 1.2301 0.7455 0.9876 0.0545  -0.2333 -0.1451 270 ALA A O   
1927 C CB  . ALA A 265 ? 1.3432 0.7432 1.0009 0.1337  -0.2326 -0.1820 270 ALA A CB  
1928 N N   . ASN A 266 ? 1.2927 0.6930 1.0237 0.0385  -0.2453 -0.1506 271 ASN A N   
1929 C CA  . ASN A 266 ? 1.3295 0.7334 1.0884 -0.0074 -0.2572 -0.1487 271 ASN A CA  
1930 C C   . ASN A 266 ? 1.2272 0.6902 1.0389 -0.0268 -0.2396 -0.1211 271 ASN A C   
1931 O O   . ASN A 266 ? 1.2053 0.6538 1.0204 -0.0246 -0.2261 -0.1041 271 ASN A O   
1932 C CB  . ASN A 266 ? 1.3743 0.6915 1.1101 -0.0318 -0.2717 -0.1567 271 ASN A CB  
1933 C CG  . ASN A 266 ? 1.4500 0.7719 1.2145 -0.0820 -0.2865 -0.1611 271 ASN A CG  
1934 O OD1 . ASN A 266 ? 1.4089 0.7996 1.2100 -0.0952 -0.2897 -0.1613 271 ASN A OD1 
1935 N ND2 . ASN A 266 ? 1.5923 0.8390 1.3407 -0.1106 -0.2965 -0.1648 271 ASN A ND2 
1936 N N   . PRO A 267 ? 1.1532 0.6814 1.0030 -0.0424 -0.2407 -0.1178 272 PRO A N   
1937 C CA  . PRO A 267 ? 1.1009 0.6827 1.0005 -0.0601 -0.2246 -0.0953 272 PRO A CA  
1938 C C   . PRO A 267 ? 1.1154 0.6723 1.0333 -0.0965 -0.2202 -0.0844 272 PRO A C   
1939 O O   . PRO A 267 ? 1.1032 0.6803 1.0404 -0.0994 -0.2014 -0.0648 272 PRO A O   
1940 C CB  . PRO A 267 ? 1.0525 0.6949 0.9830 -0.0686 -0.2341 -0.1000 272 PRO A CB  
1941 C CG  . PRO A 267 ? 1.0267 0.6599 0.9174 -0.0420 -0.2470 -0.1175 272 PRO A CG  
1942 C CD  . PRO A 267 ? 1.1076 0.6644 0.9535 -0.0399 -0.2576 -0.1345 272 PRO A CD  
1943 N N   . GLU A 268 ? 1.2027 0.7145 1.1114 -0.1249 -0.2369 -0.0973 273 GLU A N   
1944 C CA  . GLU A 268 ? 1.2053 0.6832 1.1247 -0.1643 -0.2318 -0.0863 273 GLU A CA  
1945 C C   . GLU A 268 ? 1.2123 0.6295 1.0957 -0.1526 -0.2189 -0.0701 273 GLU A C   
1946 O O   . GLU A 268 ? 1.2115 0.6251 1.1077 -0.1773 -0.2042 -0.0506 273 GLU A O   
1947 C CB  . GLU A 268 ? 1.2360 0.6693 1.1484 -0.1985 -0.2546 -0.1055 273 GLU A CB  
1948 C CG  . GLU A 268 ? 1.2110 0.7050 1.1650 -0.2193 -0.2709 -0.1207 273 GLU A CG  
1949 C CD  . GLU A 268 ? 1.2862 0.7354 1.2370 -0.2590 -0.2947 -0.1406 273 GLU A CD  
1950 O OE1 . GLU A 268 ? 1.2719 0.7747 1.2758 -0.2953 -0.3014 -0.1442 273 GLU A OE1 
1951 O OE2 . GLU A 268 ? 1.3615 0.7228 1.2588 -0.2540 -0.3077 -0.1541 273 GLU A OE2 
1952 N N   . ALA A 269 ? 1.2437 0.6182 1.0825 -0.1132 -0.2240 -0.0779 274 ALA A N   
1953 C CA  . ALA A 269 ? 1.2931 0.6190 1.0992 -0.0918 -0.2150 -0.0632 274 ALA A CA  
1954 C C   . ALA A 269 ? 1.2093 0.5926 1.0391 -0.0784 -0.1943 -0.0420 274 ALA A C   
1955 O O   . ALA A 269 ? 1.3339 0.6849 1.1460 -0.0770 -0.1864 -0.0247 274 ALA A O   
1956 C CB  . ALA A 269 ? 1.3355 0.6133 1.0952 -0.0484 -0.2262 -0.0803 274 ALA A CB  
1957 N N   . ARG A 270 ? 1.1295 0.5920 0.9947 -0.0687 -0.1871 -0.0434 275 ARG A N   
1958 C CA  . ARG A 270 ? 1.0858 0.6011 0.9729 -0.0551 -0.1693 -0.0272 275 ARG A CA  
1959 C C   . ARG A 270 ? 1.0511 0.5895 0.9664 -0.0886 -0.1556 -0.0104 275 ARG A C   
1960 O O   . ARG A 270 ? 1.0280 0.5826 0.9690 -0.1203 -0.1575 -0.0138 275 ARG A O   
1961 C CB  . ARG A 270 ? 1.0167 0.6009 0.9303 -0.0375 -0.1659 -0.0332 275 ARG A CB  
1962 C CG  . ARG A 270 ? 1.0111 0.5884 0.8991 -0.0032 -0.1731 -0.0482 275 ARG A CG  
1963 C CD  . ARG A 270 ? 0.9573 0.5969 0.8682 0.0046  -0.1698 -0.0513 275 ARG A CD  
1964 N NE  . ARG A 270 ? 0.9677 0.5976 0.8493 0.0278  -0.1785 -0.0685 275 ARG A NE  
1965 C CZ  . ARG A 270 ? 0.9465 0.6077 0.8299 0.0303  -0.1838 -0.0760 275 ARG A CZ  
1966 N NH1 . ARG A 270 ? 0.9512 0.6567 0.8685 0.0129  -0.1835 -0.0680 275 ARG A NH1 
1967 N NH2 . ARG A 270 ? 1.0043 0.6509 0.8512 0.0532  -0.1901 -0.0924 275 ARG A NH2 
1968 N N   . PRO A 271 ? 1.0199 0.5667 0.9322 -0.0809 -0.1418 0.0062  276 PRO A N   
1969 C CA  . PRO A 271 ? 1.0127 0.5827 0.9461 -0.1100 -0.1257 0.0210  276 PRO A CA  
1970 C C   . PRO A 271 ? 1.0003 0.6503 0.9827 -0.1127 -0.1156 0.0188  276 PRO A C   
1971 O O   . PRO A 271 ? 0.9465 0.6298 0.9434 -0.0927 -0.1215 0.0087  276 PRO A O   
1972 C CB  . PRO A 271 ? 0.9749 0.5201 0.8775 -0.0944 -0.1185 0.0365  276 PRO A CB  
1973 C CG  . PRO A 271 ? 0.9581 0.5146 0.8534 -0.0541 -0.1263 0.0284  276 PRO A CG  
1974 C CD  . PRO A 271 ? 0.9733 0.5218 0.8683 -0.0445 -0.1399 0.0100  276 PRO A CD  
1975 N N   . THR A 272 ? 0.9580 0.6348 0.9628 -0.1374 -0.0998 0.0284  277 THR A N   
1976 C CA  . THR A 272 ? 0.8212 0.5680 0.8691 -0.1369 -0.0877 0.0276  277 THR A CA  
1977 C C   . THR A 272 ? 0.8245 0.5786 0.8586 -0.1189 -0.0757 0.0370  277 THR A C   
1978 O O   . THR A 272 ? 0.8783 0.5891 0.8740 -0.1166 -0.0740 0.0472  277 THR A O   
1979 C CB  . THR A 272 ? 0.7749 0.5519 0.8563 -0.1716 -0.0749 0.0306  277 THR A CB  
1980 O OG1 . THR A 272 ? 0.8091 0.5498 0.8622 -0.1909 -0.0607 0.0457  277 THR A OG1 
1981 C CG2 . THR A 272 ? 0.7849 0.5620 0.8866 -0.1929 -0.0895 0.0193  277 THR A CG2 
1982 N N   . PHE A 273 ? 0.7135 0.5186 0.7764 -0.1058 -0.0695 0.0333  278 PHE A N   
1983 C CA  . PHE A 273 ? 0.7337 0.5492 0.7869 -0.0916 -0.0595 0.0388  278 PHE A CA  
1984 C C   . PHE A 273 ? 0.7694 0.5767 0.8067 -0.1090 -0.0428 0.0496  278 PHE A C   
1985 O O   . PHE A 273 ? 0.7530 0.5367 0.7561 -0.0987 -0.0421 0.0567  278 PHE A O   
1986 C CB  . PHE A 273 ? 0.7447 0.6090 0.8313 -0.0777 -0.0561 0.0319  278 PHE A CB  
1987 C CG  . PHE A 273 ? 0.7075 0.5726 0.7930 -0.0557 -0.0685 0.0267  278 PHE A CG  
1988 C CD1 . PHE A 273 ? 0.6556 0.5087 0.7209 -0.0379 -0.0713 0.0285  278 PHE A CD1 
1989 C CD2 . PHE A 273 ? 0.7499 0.6310 0.8542 -0.0531 -0.0771 0.0202  278 PHE A CD2 
1990 C CE1 . PHE A 273 ? 0.6362 0.4965 0.7033 -0.0199 -0.0785 0.0242  278 PHE A CE1 
1991 C CE2 . PHE A 273 ? 0.6961 0.5778 0.7936 -0.0339 -0.0851 0.0171  278 PHE A CE2 
1992 C CZ  . PHE A 273 ? 0.6369 0.5094 0.7171 -0.0183 -0.0838 0.0193  278 PHE A CZ  
1993 N N   . PRO A 274 ? 0.7667 0.5959 0.8274 -0.1350 -0.0296 0.0507  279 PRO A N   
1994 C CA  . PRO A 274 ? 0.8650 0.6790 0.9026 -0.1562 -0.0115 0.0633  279 PRO A CA  
1995 C C   . PRO A 274 ? 0.9579 0.7004 0.9417 -0.1626 -0.0187 0.0769  279 PRO A C   
1996 O O   . PRO A 274 ? 0.9758 0.6922 0.9184 -0.1619 -0.0105 0.0895  279 PRO A O   
1997 C CB  . PRO A 274 ? 0.7923 0.6445 0.8732 -0.1854 0.0006  0.0602  279 PRO A CB  
1998 C CG  . PRO A 274 ? 0.7436 0.6486 0.8731 -0.1697 -0.0066 0.0452  279 PRO A CG  
1999 C CD  . PRO A 274 ? 0.7805 0.6606 0.8933 -0.1430 -0.0283 0.0405  279 PRO A CD  
2000 N N   . GLY A 275 ? 0.9144 0.6227 0.8951 -0.1666 -0.0355 0.0733  280 GLY A N   
2001 C CA  . GLY A 275 ? 0.9896 0.6217 0.9185 -0.1641 -0.0477 0.0828  280 GLY A CA  
2002 C C   . GLY A 275 ? 1.0350 0.6449 0.9287 -0.1282 -0.0585 0.0854  280 GLY A C   
2003 O O   . GLY A 275 ? 1.1838 0.7426 1.0287 -0.1250 -0.0599 0.0999  280 GLY A O   
2004 N N   . ILE A 276 ? 0.9260 0.5756 0.8448 -0.1019 -0.0663 0.0722  281 ILE A N   
2005 C CA  . ILE A 276 ? 0.9373 0.5839 0.8366 -0.0692 -0.0760 0.0718  281 ILE A CA  
2006 C C   . ILE A 276 ? 0.9618 0.6214 0.8443 -0.0686 -0.0653 0.0809  281 ILE A C   
2007 O O   . ILE A 276 ? 1.0596 0.6865 0.9021 -0.0531 -0.0739 0.0894  281 ILE A O   
2008 C CB  . ILE A 276 ? 0.8760 0.5676 0.8105 -0.0476 -0.0828 0.0566  281 ILE A CB  
2009 C CG1 . ILE A 276 ? 0.9281 0.5991 0.8643 -0.0422 -0.0955 0.0470  281 ILE A CG1 
2010 C CG2 . ILE A 276 ? 0.8663 0.5676 0.7912 -0.0187 -0.0905 0.0554  281 ILE A CG2 
2011 C CD1 . ILE A 276 ? 0.8804 0.5974 0.8507 -0.0306 -0.0974 0.0344  281 ILE A CD1 
2012 N N   . GLU A 277 ? 0.9186 0.6250 0.8298 -0.0829 -0.0483 0.0777  282 GLU A N   
2013 C CA  . GLU A 277 ? 0.9185 0.6427 0.8149 -0.0820 -0.0367 0.0814  282 GLU A CA  
2014 C C   . GLU A 277 ? 1.0358 0.7141 0.8771 -0.0939 -0.0299 0.0997  282 GLU A C   
2015 O O   . GLU A 277 ? 1.0257 0.6964 0.8320 -0.0806 -0.0329 0.1042  282 GLU A O   
2016 C CB  . GLU A 277 ? 0.9441 0.7222 0.8816 -0.0957 -0.0174 0.0728  282 GLU A CB  
2017 C CG  . GLU A 277 ? 0.9726 0.7745 0.8995 -0.0897 -0.0063 0.0693  282 GLU A CG  
2018 C CD  . GLU A 277 ? 1.1247 0.9769 1.0929 -0.0981 0.0126  0.0583  282 GLU A CD  
2019 O OE1 . GLU A 277 ? 1.2094 1.0819 1.2128 -0.1132 0.0206  0.0568  282 GLU A OE1 
2020 O OE2 . GLU A 277 ? 1.1956 1.0679 1.1615 -0.0881 0.0183  0.0494  282 GLU A OE2 
2021 N N   . GLU A 278 ? 1.0562 0.7052 0.8893 -0.1208 -0.0208 0.1102  283 GLU A N   
2022 C CA  . GLU A 278 ? 1.1021 0.6979 0.8787 -0.1379 -0.0118 0.1319  283 GLU A CA  
2023 C C   . GLU A 278 ? 1.1759 0.7077 0.8942 -0.1137 -0.0336 0.1436  283 GLU A C   
2024 O O   . GLU A 278 ? 1.2614 0.7622 0.9254 -0.1134 -0.0296 0.1600  283 GLU A O   
2025 C CB  . GLU A 278 ? 1.1074 0.6802 0.8930 -0.1749 -0.0006 0.1400  283 GLU A CB  
2026 C CG  . GLU A 278 ? 1.0759 0.7028 0.9071 -0.2044 0.0234  0.1353  283 GLU A CG  
2027 C CD  . GLU A 278 ? 1.0922 0.7080 0.9518 -0.2366 0.0239  0.1350  283 GLU A CD  
2028 O OE1 . GLU A 278 ? 1.1646 0.7106 0.9835 -0.2542 0.0200  0.1505  283 GLU A OE1 
2029 O OE2 . GLU A 278 ? 1.0375 0.7121 0.9589 -0.2441 0.0262  0.1188  283 GLU A OE2 
2030 N N   . LYS A 279 ? 1.1477 0.6627 0.8766 -0.0915 -0.0560 0.1345  284 LYS A N   
2031 C CA  . LYS A 279 ? 1.1487 0.6111 0.8322 -0.0611 -0.0793 0.1414  284 LYS A CA  
2032 C C   . LYS A 279 ? 1.0540 0.5594 0.7473 -0.0274 -0.0925 0.1306  284 LYS A C   
2033 O O   . LYS A 279 ? 1.1401 0.6205 0.7891 -0.0075 -0.1052 0.1402  284 LYS A O   
2034 C CB  . LYS A 279 ? 1.1531 0.5737 0.8406 -0.0528 -0.0954 0.1353  284 LYS A CB  
2035 C CG  . LYS A 279 ? 1.2363 0.5898 0.8957 -0.0851 -0.0889 0.1495  284 LYS A CG  
2036 C CD  . LYS A 279 ? 1.2472 0.5492 0.9018 -0.0805 -0.1046 0.1425  284 LYS A CD  
2037 C CE  . LYS A 279 ? 1.2938 0.5560 0.9467 -0.1256 -0.0940 0.1492  284 LYS A CE  
2038 N NZ  . LYS A 279 ? 1.3463 0.5392 0.9823 -0.1206 -0.1133 0.1413  284 LYS A NZ  
2039 N N   . PHE A 280 ? 0.9851 0.5539 0.7349 -0.0217 -0.0909 0.1112  285 PHE A N   
2040 C CA  . PHE A 280 ? 0.9690 0.5819 0.7366 0.0054  -0.1031 0.0993  285 PHE A CA  
2041 C C   . PHE A 280 ? 1.0027 0.6392 0.7530 0.0040  -0.0982 0.1009  285 PHE A C   
2042 O O   . PHE A 280 ? 1.1246 0.7687 0.8611 0.0273  -0.1156 0.0984  285 PHE A O   
2043 C CB  . PHE A 280 ? 0.8570 0.5242 0.6850 0.0094  -0.1015 0.0808  285 PHE A CB  
2044 C CG  . PHE A 280 ? 0.8745 0.5784 0.7214 0.0360  -0.1158 0.0700  285 PHE A CG  
2045 C CD1 . PHE A 280 ? 0.8959 0.5871 0.7385 0.0634  -0.1332 0.0674  285 PHE A CD1 
2046 C CD2 . PHE A 280 ? 0.8958 0.6478 0.7656 0.0337  -0.1119 0.0613  285 PHE A CD2 
2047 C CE1 . PHE A 280 ? 0.8989 0.6335 0.7656 0.0861  -0.1450 0.0571  285 PHE A CE1 
2048 C CE2 . PHE A 280 ? 0.8534 0.6418 0.7447 0.0531  -0.1253 0.0511  285 PHE A CE2 
2049 C CZ  . PHE A 280 ? 0.8804 0.6647 0.7729 0.0785  -0.1412 0.0496  285 PHE A CZ  
2050 N N   . ARG A 281 ? 1.0258 0.6752 0.7764 -0.0216 -0.0758 0.1034  286 ARG A N   
2051 C CA  . ARG A 281 ? 1.0270 0.6971 0.7564 -0.0223 -0.0694 0.1016  286 ARG A CA  
2052 C C   . ARG A 281 ? 1.1136 0.7394 0.7724 -0.0100 -0.0822 0.1175  286 ARG A C   
2053 O O   . ARG A 281 ? 1.1324 0.7772 0.7796 0.0085  -0.0976 0.1099  286 ARG A O   
2054 C CB  . ARG A 281 ? 0.9821 0.6761 0.7243 -0.0491 -0.0401 0.0998  286 ARG A CB  
2055 C CG  . ARG A 281 ? 0.9810 0.7027 0.7078 -0.0462 -0.0329 0.0906  286 ARG A CG  
2056 C CD  . ARG A 281 ? 0.9978 0.7419 0.7332 -0.0689 -0.0016 0.0888  286 ARG A CD  
2057 N NE  . ARG A 281 ? 0.9512 0.7395 0.7548 -0.0737 0.0071  0.0730  286 ARG A NE  
2058 C CZ  . ARG A 281 ? 0.9130 0.7374 0.7512 -0.0624 0.0038  0.0534  286 ARG A CZ  
2059 N NH1 . ARG A 281 ? 0.8958 0.7228 0.7128 -0.0478 -0.0088 0.0436  286 ARG A NH1 
2060 N NH2 . ARG A 281 ? 0.9090 0.7647 0.8031 -0.0662 0.0111  0.0435  286 ARG A NH2 
2061 N N   . PRO A 282 ? 1.1934 0.7588 0.8041 -0.0206 -0.0778 0.1396  287 PRO A N   
2062 C CA  . PRO A 282 ? 1.2783 0.7934 0.8153 -0.0043 -0.0938 0.1576  287 PRO A CA  
2063 C C   . PRO A 282 ? 1.2353 0.7415 0.7700 0.0342  -0.1288 0.1534  287 PRO A C   
2064 O O   . PRO A 282 ? 1.2639 0.7608 0.7553 0.0554  -0.1478 0.1583  287 PRO A O   
2065 C CB  . PRO A 282 ? 1.3858 0.8317 0.8778 -0.0272 -0.0804 0.1833  287 PRO A CB  
2066 C CG  . PRO A 282 ? 1.3390 0.7961 0.8878 -0.0471 -0.0687 0.1751  287 PRO A CG  
2067 C CD  . PRO A 282 ? 1.2554 0.7931 0.8722 -0.0494 -0.0591 0.1503  287 PRO A CD  
2068 N N   . PHE A 283 ? 1.1569 0.6699 0.7376 0.0442  -0.1370 0.1433  288 PHE A N   
2069 C CA  . PHE A 283 ? 1.1296 0.6521 0.7239 0.0818  -0.1659 0.1344  288 PHE A CA  
2070 C C   . PHE A 283 ? 1.1134 0.7079 0.7439 0.0950  -0.1761 0.1150  288 PHE A C   
2071 O O   . PHE A 283 ? 1.1388 0.7388 0.7516 0.1227  -0.2013 0.1142  288 PHE A O   
2072 C CB  . PHE A 283 ? 1.1057 0.6263 0.7420 0.0873  -0.1669 0.1249  288 PHE A CB  
2073 C CG  . PHE A 283 ? 1.1386 0.6771 0.7941 0.1271  -0.1920 0.1139  288 PHE A CG  
2074 C CD1 . PHE A 283 ? 1.2064 0.6930 0.8145 0.1586  -0.2158 0.1253  288 PHE A CD1 
2075 C CD2 . PHE A 283 ? 1.0901 0.6995 0.8107 0.1343  -0.1914 0.0926  288 PHE A CD2 
2076 C CE1 . PHE A 283 ? 1.2023 0.7147 0.8342 0.1988  -0.2383 0.1130  288 PHE A CE1 
2077 C CE2 . PHE A 283 ? 1.0667 0.7026 0.8102 0.1700  -0.2111 0.0818  288 PHE A CE2 
2078 C CZ  . PHE A 283 ? 1.1229 0.7146 0.8249 0.2035  -0.2347 0.0907  288 PHE A CZ  
2079 N N   . TYR A 284 ? 1.0535 0.7006 0.7340 0.0748  -0.1581 0.0997  289 TYR A N   
2080 C CA  . TYR A 284 ? 0.9846 0.6930 0.6978 0.0792  -0.1647 0.0812  289 TYR A CA  
2081 C C   . TYR A 284 ? 1.0370 0.7391 0.6981 0.0840  -0.1754 0.0846  289 TYR A C   
2082 O O   . TYR A 284 ? 1.0794 0.8130 0.7478 0.1028  -0.1990 0.0737  289 TYR A O   
2083 C CB  . TYR A 284 ? 0.9184 0.6674 0.6818 0.0549  -0.1414 0.0675  289 TYR A CB  
2084 C CG  . TYR A 284 ? 0.9070 0.7044 0.6934 0.0536  -0.1457 0.0494  289 TYR A CG  
2085 C CD1 . TYR A 284 ? 0.8760 0.7154 0.7031 0.0681  -0.1638 0.0357  289 TYR A CD1 
2086 C CD2 . TYR A 284 ? 0.8890 0.6894 0.6550 0.0376  -0.1316 0.0449  289 TYR A CD2 
2087 C CE1 . TYR A 284 ? 0.9048 0.7837 0.7533 0.0627  -0.1693 0.0184  289 TYR A CE1 
2088 C CE2 . TYR A 284 ? 0.8762 0.7123 0.6592 0.0361  -0.1375 0.0257  289 TYR A CE2 
2089 C CZ  . TYR A 284 ? 0.9408 0.8138 0.7650 0.0469  -0.1575 0.0127  289 TYR A CZ  
2090 O OH  . TYR A 284 ? 0.9740 0.8788 0.8165 0.0414  -0.1650 -0.0072 289 TYR A OH  
2091 N N   . LEU A 285 ? 1.0873 0.7511 0.6958 0.0664  -0.1583 0.0994  290 LEU A N   
2092 C CA  . LEU A 285 ? 1.1586 0.8136 0.7077 0.0684  -0.1638 0.1029  290 LEU A CA  
2093 C C   . LEU A 285 ? 1.2385 0.8567 0.7304 0.0974  -0.1950 0.1172  290 LEU A C   
2094 O O   . LEU A 285 ? 1.3260 0.9667 0.8000 0.1133  -0.2178 0.1079  290 LEU A O   
2095 C CB  . LEU A 285 ? 1.2608 0.8882 0.7685 0.0407  -0.1316 0.1160  290 LEU A CB  
2096 C CG  . LEU A 285 ? 1.2309 0.9012 0.7873 0.0165  -0.1021 0.0993  290 LEU A CG  
2097 C CD1 . LEU A 285 ? 1.2438 0.8896 0.7699 -0.0102 -0.0684 0.1150  290 LEU A CD1 
2098 C CD2 . LEU A 285 ? 1.2230 0.9363 0.7881 0.0209  -0.1077 0.0755  290 LEU A CD2 
2099 N N   . SER A 286 ? 1.2761 0.8366 0.7398 0.1051  -0.1983 0.1383  291 SER A N   
2100 C CA  . SER A 286 ? 1.3854 0.9008 0.7923 0.1375  -0.2296 0.1544  291 SER A CA  
2101 C C   . SER A 286 ? 1.3794 0.9396 0.8331 0.1733  -0.2631 0.1371  291 SER A C   
2102 O O   . SER A 286 ? 1.4852 1.0543 0.9102 0.1993  -0.2931 0.1362  291 SER A O   
2103 C CB  . SER A 286 ? 1.4695 0.9009 0.8325 0.1351  -0.2234 0.1813  291 SER A CB  
2104 O OG  . SER A 286 ? 1.4376 0.8732 0.8587 0.1324  -0.2165 0.1729  291 SER A OG  
2105 N N   . GLN A 287 ? 1.3320 0.9240 0.8570 0.1743  -0.2574 0.1231  292 GLN A N   
2106 C CA  . GLN A 287 ? 1.3009 0.9321 0.8725 0.2090  -0.2838 0.1093  292 GLN A CA  
2107 C C   . GLN A 287 ? 1.1737 0.8960 0.8210 0.2051  -0.2862 0.0819  292 GLN A C   
2108 O O   . GLN A 287 ? 1.2655 1.0325 0.9323 0.2302  -0.3143 0.0707  292 GLN A O   
2109 C CB  . GLN A 287 ? 1.3517 0.9529 0.9448 0.2172  -0.2768 0.1122  292 GLN A CB  
2110 C CG  . GLN A 287 ? 1.4322 0.9359 0.9531 0.2265  -0.2812 0.1379  292 GLN A CG  
2111 C CD  . GLN A 287 ? 1.5762 1.0527 1.0530 0.2712  -0.3179 0.1472  292 GLN A CD  
2112 O OE1 . GLN A 287 ? 1.7161 1.1596 1.1274 0.2739  -0.3291 0.1637  292 GLN A OE1 
2113 N NE2 . GLN A 287 ? 1.5908 1.0827 1.1015 0.3092  -0.3372 0.1362  292 GLN A NE2 
2114 N N   . LEU A 288 ? 1.1149 0.8651 0.8062 0.1738  -0.2583 0.0716  293 LEU A N   
2115 C CA  . LEU A 288 ? 1.0588 0.8854 0.8258 0.1681  -0.2571 0.0483  293 LEU A CA  
2116 C C   . LEU A 288 ? 1.0440 0.9139 0.8187 0.1560  -0.2649 0.0331  293 LEU A C   
2117 O O   . LEU A 288 ? 1.0820 1.0107 0.9035 0.1654  -0.2828 0.0166  293 LEU A O   
2118 C CB  . LEU A 288 ? 1.0258 0.8597 0.8363 0.1453  -0.2277 0.0445  293 LEU A CB  
2119 C CG  . LEU A 288 ? 1.0376 0.8336 0.8456 0.1573  -0.2228 0.0539  293 LEU A CG  
2120 C CD1 . LEU A 288 ? 1.0137 0.8193 0.8597 0.1332  -0.1962 0.0492  293 LEU A CD1 
2121 C CD2 . LEU A 288 ? 1.0291 0.8500 0.8621 0.1933  -0.2440 0.0471  293 LEU A CD2 
2122 N N   . GLU A 289 ? 1.0815 0.9254 0.8127 0.1353  -0.2519 0.0366  294 GLU A N   
2123 C CA  . GLU A 289 ? 1.1789 1.0554 0.9061 0.1262  -0.2622 0.0193  294 GLU A CA  
2124 C C   . GLU A 289 ? 1.2894 1.1522 0.9565 0.1490  -0.2941 0.0242  294 GLU A C   
2125 O O   . GLU A 289 ? 1.4014 1.3072 1.0824 0.1547  -0.3191 0.0063  294 GLU A O   
2126 C CB  . GLU A 289 ? 1.1695 1.0340 0.8829 0.0967  -0.2335 0.0145  294 GLU A CB  
2127 C CG  . GLU A 289 ? 1.2397 1.0484 0.8765 0.0901  -0.2177 0.0328  294 GLU A CG  
2128 C CD  . GLU A 289 ? 1.2576 1.0704 0.8832 0.0670  -0.1938 0.0210  294 GLU A CD  
2129 O OE1 . GLU A 289 ? 1.3447 1.1249 0.9025 0.0635  -0.1848 0.0307  294 GLU A OE1 
2130 O OE2 . GLU A 289 ? 1.3105 1.1566 0.9914 0.0535  -0.1829 0.0024  294 GLU A OE2 
2131 N N   . SER B 1   ? 2.4481 2.2981 1.8083 -0.3847 0.0594  -0.3953 6   SER B N   
2132 C CA  . SER B 1   ? 1.9547 1.8060 1.3597 -0.3423 0.0796  -0.3779 6   SER B CA  
2133 C C   . SER B 1   ? 2.0277 1.9014 1.4729 -0.2993 0.0315  -0.3027 6   SER B C   
2134 O O   . SER B 1   ? 1.8709 1.7326 1.4036 -0.2473 0.0301  -0.2898 6   SER B O   
2135 C CB  . SER B 1   ? 2.4590 2.3179 1.7904 -0.3796 0.1141  -0.4002 6   SER B CB  
2136 O OG  . SER B 1   ? 2.5357 2.3680 1.8498 -0.4139 0.1724  -0.4801 6   SER B OG  
2137 N N   . LEU B 2   ? 2.1521 2.0583 1.5348 -0.3255 -0.0066 -0.2537 7   LEU B N   
2138 C CA  . LEU B 2   ? 2.0845 2.0138 1.5088 -0.2922 -0.0510 -0.1819 7   LEU B CA  
2139 C C   . LEU B 2   ? 2.0191 1.9534 1.4909 -0.2767 -0.0910 -0.1534 7   LEU B C   
2140 O O   . LEU B 2   ? 1.7227 1.6730 1.2422 -0.2478 -0.1193 -0.1007 7   LEU B O   
2141 C CB  . LEU B 2   ? 1.9883 1.9506 1.3457 -0.3261 -0.0760 -0.1350 7   LEU B CB  
2142 C CG  . LEU B 2   ? 2.3748 2.3366 1.6864 -0.3415 -0.0397 -0.1501 7   LEU B CG  
2143 C CD1 . LEU B 2   ? 2.4272 2.4232 1.6690 -0.3826 -0.0734 -0.0942 7   LEU B CD1 
2144 C CD2 . LEU B 2   ? 2.2896 2.2381 1.6796 -0.2861 -0.0135 -0.1497 7   LEU B CD2 
2145 N N   . ASN B 3   ? 2.1451 2.0643 1.6107 -0.2963 -0.0883 -0.1907 8   ASN B N   
2146 C CA  . ASN B 3   ? 2.0118 1.9335 1.5247 -0.2849 -0.1207 -0.1697 8   ASN B CA  
2147 C C   . ASN B 3   ? 1.8329 1.7324 1.4373 -0.2276 -0.1081 -0.1672 8   ASN B C   
2148 O O   . ASN B 3   ? 1.6682 1.5463 1.2995 -0.2024 -0.0743 -0.1927 8   ASN B O   
2149 C CB  . ASN B 3   ? 1.9295 1.8392 1.4065 -0.3279 -0.1180 -0.2151 8   ASN B CB  
2150 C CG  . ASN B 3   ? 2.2527 2.1871 1.6227 -0.3970 -0.1352 -0.2186 8   ASN B CG  
2151 O OD1 . ASN B 3   ? 2.2587 2.2272 1.5923 -0.4126 -0.1676 -0.1668 8   ASN B OD1 
2152 N ND2 . ASN B 3   ? 2.3311 2.2477 1.6518 -0.4423 -0.1138 -0.2793 8   ASN B ND2 
2153 N N   . VAL B 4   ? 1.7788 1.6851 1.4312 -0.2113 -0.1359 -0.1355 9   VAL B N   
2154 C CA  . VAL B 4   ? 1.7003 1.5871 1.4279 -0.1652 -0.1267 -0.1292 9   VAL B CA  
2155 C C   . VAL B 4   ? 1.6664 1.5196 1.4144 -0.1676 -0.1041 -0.1765 9   VAL B C   
2156 O O   . VAL B 4   ? 1.8160 1.6651 1.5455 -0.1994 -0.1106 -0.1984 9   VAL B O   
2157 C CB  . VAL B 4   ? 1.6095 1.5123 1.3843 -0.1502 -0.1555 -0.0841 9   VAL B CB  
2158 C CG1 . VAL B 4   ? 1.4164 1.3008 1.2501 -0.1083 -0.1414 -0.0765 9   VAL B CG1 
2159 C CG2 . VAL B 4   ? 1.7147 1.6512 1.4858 -0.1531 -0.1787 -0.0374 9   VAL B CG2 
2160 N N   . ILE B 5   ? 1.4894 1.3192 1.2824 -0.1354 -0.0790 -0.1902 10  ILE B N   
2161 C CA  . ILE B 5   ? 1.4361 1.2325 1.2771 -0.1286 -0.0597 -0.2233 10  ILE B CA  
2162 C C   . ILE B 5   ? 1.3010 1.0935 1.1878 -0.1126 -0.0816 -0.1927 10  ILE B C   
2163 O O   . ILE B 5   ? 1.1482 0.9437 1.0659 -0.0828 -0.0888 -0.1592 10  ILE B O   
2164 C CB  . ILE B 5   ? 1.4087 1.1861 1.2939 -0.1016 -0.0305 -0.2407 10  ILE B CB  
2165 C CG1 . ILE B 5   ? 1.3404 1.1208 1.1830 -0.1225 -0.0017 -0.2771 10  ILE B CG1 
2166 C CG2 . ILE B 5   ? 1.4540 1.1976 1.4112 -0.0911 -0.0152 -0.2637 10  ILE B CG2 
2167 C CD1 . ILE B 5   ? 1.3911 1.1603 1.2805 -0.0990 0.0274  -0.2929 10  ILE B CD1 
2168 N N   . LYS B 6   ? 1.3410 1.1275 1.2269 -0.1374 -0.0905 -0.2062 11  LYS B N   
2169 C CA  . LYS B 6   ? 1.3113 1.0907 1.2438 -0.1274 -0.1058 -0.1831 11  LYS B CA  
2170 C C   . LYS B 6   ? 1.1818 0.9246 1.1766 -0.1070 -0.0854 -0.1986 11  LYS B C   
2171 O O   . LYS B 6   ? 1.2813 0.9994 1.2918 -0.1213 -0.0638 -0.2423 11  LYS B O   
2172 C CB  . LYS B 6   ? 1.4382 1.2251 1.3529 -0.1644 -0.1231 -0.1935 11  LYS B CB  
2173 C CG  . LYS B 6   ? 1.4855 1.3143 1.3546 -0.1849 -0.1532 -0.1641 11  LYS B CG  
2174 C CD  . LYS B 6   ? 1.4982 1.3388 1.3188 -0.2363 -0.1686 -0.1881 11  LYS B CD  
2175 C CE  . LYS B 6   ? 1.4247 1.3089 1.1956 -0.2586 -0.2000 -0.1543 11  LYS B CE  
2176 N NZ  . LYS B 6   ? 1.5097 1.4128 1.2331 -0.3144 -0.2269 -0.1658 11  LYS B NZ  
2177 N N   . MET B 7   ? 1.0808 0.8205 1.1129 -0.0768 -0.0915 -0.1624 12  MET B N   
2178 C CA  . MET B 7   ? 1.0210 0.7305 1.1186 -0.0577 -0.0819 -0.1607 12  MET B CA  
2179 C C   . MET B 7   ? 0.9861 0.6824 1.1211 -0.0591 -0.0941 -0.1381 12  MET B C   
2180 O O   . MET B 7   ? 0.9943 0.7085 1.1075 -0.0687 -0.1092 -0.1183 12  MET B O   
2181 C CB  . MET B 7   ? 1.0260 0.7422 1.1326 -0.0301 -0.0839 -0.1325 12  MET B CB  
2182 C CG  . MET B 7   ? 1.0641 0.7887 1.1506 -0.0265 -0.0680 -0.1557 12  MET B CG  
2183 S SD  . MET B 7   ? 0.9836 0.7193 1.0814 0.0016  -0.0738 -0.1234 12  MET B SD  
2184 C CE  . MET B 7   ? 1.0657 0.8054 1.1560 -0.0002 -0.0477 -0.1630 12  MET B CE  
2185 N N   . LYS B 8   ? 0.9874 0.6529 1.1881 -0.0497 -0.0868 -0.1388 13  LYS B N   
2186 C CA  . LYS B 8   ? 1.0189 0.6665 1.2649 -0.0510 -0.0962 -0.1140 13  LYS B CA  
2187 C C   . LYS B 8   ? 0.9904 0.6307 1.2714 -0.0287 -0.1056 -0.0698 13  LYS B C   
2188 O O   . LYS B 8   ? 1.0360 0.6725 1.3405 -0.0135 -0.1009 -0.0718 13  LYS B O   
2189 C CB  . LYS B 8   ? 1.0323 0.6460 1.3353 -0.0653 -0.0804 -0.1521 13  LYS B CB  
2190 C CG  . LYS B 8   ? 1.0402 0.6609 1.2987 -0.0967 -0.0725 -0.1996 13  LYS B CG  
2191 C CD  . LYS B 8   ? 1.0922 0.6766 1.4066 -0.1167 -0.0543 -0.2412 13  LYS B CD  
2192 C CE  . LYS B 8   ? 1.1219 0.6778 1.4881 -0.1114 -0.0206 -0.2849 13  LYS B CE  
2193 N NZ  . LYS B 8   ? 1.1812 0.6983 1.6078 -0.1340 0.0045  -0.3338 13  LYS B NZ  
2194 N N   . SER B 9   ? 0.9988 0.6383 1.2840 -0.0305 -0.1192 -0.0291 14  SER B N   
2195 C CA  . SER B 9   ? 0.9918 0.6221 1.3062 -0.0193 -0.1323 0.0181  14  SER B CA  
2196 C C   . SER B 9   ? 1.0019 0.6009 1.4072 -0.0103 -0.1314 0.0187  14  SER B C   
2197 O O   . SER B 9   ? 0.9851 0.5841 1.4182 0.0024  -0.1442 0.0497  14  SER B O   
2198 C CB  . SER B 9   ? 0.9800 0.6109 1.2826 -0.0313 -0.1413 0.0567  14  SER B CB  
2199 O OG  . SER B 9   ? 0.8951 0.5555 1.1310 -0.0371 -0.1384 0.0592  14  SER B OG  
2200 N N   . SER B 10  ? 1.0722 0.6458 1.5298 -0.0189 -0.1164 -0.0160 15  SER B N   
2201 C CA  . SER B 10  ? 1.0496 0.5890 1.6138 -0.0108 -0.1057 -0.0281 15  SER B CA  
2202 C C   . SER B 10  ? 1.0092 0.5504 1.6032 0.0042  -0.0899 -0.0578 15  SER B C   
2203 O O   . SER B 10  ? 0.9605 0.4784 1.6581 0.0160  -0.0841 -0.0544 15  SER B O   
2204 C CB  . SER B 10  ? 1.0778 0.5887 1.6839 -0.0287 -0.0852 -0.0721 15  SER B CB  
2205 O OG  . SER B 10  ? 1.1163 0.6346 1.6760 -0.0426 -0.0619 -0.1365 15  SER B OG  
2206 N N   . ASP B 11  ? 1.0100 0.5785 1.5243 0.0031  -0.0819 -0.0848 16  ASP B N   
2207 C CA  . ASP B 11  ? 1.0521 0.6284 1.5858 0.0172  -0.0683 -0.1050 16  ASP B CA  
2208 C C   . ASP B 11  ? 1.0277 0.6173 1.5896 0.0374  -0.0940 -0.0510 16  ASP B C   
2209 O O   . ASP B 11  ? 1.0997 0.6925 1.7096 0.0507  -0.0844 -0.0627 16  ASP B O   
2210 C CB  . ASP B 11  ? 1.0645 0.6682 1.5004 0.0081  -0.0558 -0.1401 16  ASP B CB  
2211 C CG  . ASP B 11  ? 1.1582 0.7548 1.5558 -0.0189 -0.0341 -0.1943 16  ASP B CG  
2212 O OD1 . ASP B 11  ? 1.1234 0.6890 1.5823 -0.0296 -0.0157 -0.2249 16  ASP B OD1 
2213 O OD2 . ASP B 11  ? 1.1429 0.7659 1.4504 -0.0321 -0.0367 -0.2051 16  ASP B OD2 
2214 N N   . PHE B 12  ? 0.9626 0.5620 1.4921 0.0355  -0.1251 0.0052  17  PHE B N   
2215 C CA  . PHE B 12  ? 0.9471 0.5642 1.4758 0.0445  -0.1539 0.0572  17  PHE B CA  
2216 C C   . PHE B 12  ? 1.0324 0.6320 1.6498 0.0469  -0.1806 0.1131  17  PHE B C   
2217 O O   . PHE B 12  ? 1.1078 0.6891 1.7392 0.0365  -0.1867 0.1341  17  PHE B O   
2218 C CB  . PHE B 12  ? 0.9056 0.5495 1.3198 0.0339  -0.1656 0.0763  17  PHE B CB  
2219 C CG  . PHE B 12  ? 0.8461 0.5102 1.1907 0.0342  -0.1456 0.0335  17  PHE B CG  
2220 C CD1 . PHE B 12  ? 0.8483 0.5115 1.1550 0.0235  -0.1278 -0.0018 17  PHE B CD1 
2221 C CD2 . PHE B 12  ? 0.8317 0.5165 1.1553 0.0431  -0.1468 0.0309  17  PHE B CD2 
2222 C CE1 . PHE B 12  ? 0.7619 0.4452 1.0089 0.0211  -0.1142 -0.0332 17  PHE B CE1 
2223 C CE2 . PHE B 12  ? 0.8073 0.5093 1.0729 0.0425  -0.1289 -0.0035 17  PHE B CE2 
2224 C CZ  . PHE B 12  ? 0.7770 0.4785 1.0040 0.0313  -0.1136 -0.0333 17  PHE B CZ  
2225 N N   . LEU B 13  ? 1.1477 0.7553 1.8279 0.0589  -0.1992 0.1413  18  LEU B N   
2226 C CA  . LEU B 13  ? 1.2065 0.8002 1.9962 0.0625  -0.2292 0.1998  18  LEU B CA  
2227 C C   . LEU B 13  ? 1.3807 0.9906 2.1018 0.0436  -0.2719 0.2713  18  LEU B C   
2228 O O   . LEU B 13  ? 1.3943 0.9877 2.1668 0.0350  -0.2951 0.3233  18  LEU B O   
2229 C CB  . LEU B 13  ? 1.1884 0.7877 2.0904 0.0820  -0.2326 0.2013  18  LEU B CB  
2230 C CG  . LEU B 13  ? 1.2822 0.8528 2.3032 0.0970  -0.1884 0.1426  18  LEU B CG  
2231 C CD1 . LEU B 13  ? 1.3015 0.8692 2.2390 0.0911  -0.1407 0.0607  18  LEU B CD1 
2232 C CD2 . LEU B 13  ? 1.2811 0.8594 2.4280 0.1164  -0.1888 0.1470  18  LEU B CD2 
2233 N N   . GLU B 14  ? 1.6524 1.2931 2.2597 0.0343  -0.2795 0.2726  19  GLU B N   
2234 C CA  . GLU B 14  ? 1.8971 1.5568 2.4160 0.0091  -0.3124 0.3284  19  GLU B CA  
2235 C C   . GLU B 14  ? 2.1620 1.8263 2.7467 0.0002  -0.3625 0.4049  19  GLU B C   
2236 O O   . GLU B 14  ? 2.3856 2.0644 2.8960 -0.0286 -0.3933 0.4569  19  GLU B O   
2237 C CB  . GLU B 14  ? 1.9431 1.5943 2.3798 -0.0113 -0.2996 0.3307  19  GLU B CB  
2238 C CG  . GLU B 14  ? 1.8397 1.4619 2.3419 -0.0184 -0.3077 0.3655  19  GLU B CG  
2239 C CD  . GLU B 14  ? 1.8206 1.4441 2.2328 -0.0481 -0.3092 0.3953  19  GLU B CD  
2240 O OE1 . GLU B 14  ? 1.7693 1.4072 2.0846 -0.0566 -0.2846 0.3621  19  GLU B OE1 
2241 O OE2 . GLU B 14  ? 1.7103 1.3202 2.1562 -0.0641 -0.3335 0.4537  19  GLU B OE2 
2242 N N   . LYS B 25  ? 1.3648 1.1537 1.1236 -0.1376 0.0081  0.0935  30  LYS B N   
2243 C CA  . LYS B 25  ? 1.5377 1.3204 1.2710 -0.1411 -0.0355 0.1213  30  LYS B CA  
2244 C C   . LYS B 25  ? 1.5073 1.2947 1.2755 -0.1095 -0.0627 0.1129  30  LYS B C   
2245 O O   . LYS B 25  ? 1.3674 1.1511 1.1894 -0.0845 -0.0782 0.1137  30  LYS B O   
2246 C CB  . LYS B 25  ? 1.4457 1.2157 1.1989 -0.1456 -0.0562 0.1552  30  LYS B CB  
2247 C CG  . LYS B 25  ? 1.4951 1.2592 1.1941 -0.1855 -0.0434 0.1780  30  LYS B CG  
2248 C CD  . LYS B 25  ? 1.5040 1.2541 1.2362 -0.1871 -0.0638 0.2135  30  LYS B CD  
2249 C CE  . LYS B 25  ? 1.5817 1.3259 1.2513 -0.2326 -0.0531 0.2436  30  LYS B CE  
2250 N NZ  . LYS B 25  ? 1.5955 1.3240 1.3051 -0.2342 -0.0738 0.2824  30  LYS B NZ  
2251 N N   . VAL B 26  ? 1.4885 1.2837 1.2237 -0.1150 -0.0647 0.1019  31  VAL B N   
2252 C CA  . VAL B 26  ? 1.3314 1.1322 1.0935 -0.0916 -0.0903 0.0974  31  VAL B CA  
2253 C C   . VAL B 26  ? 1.2703 1.0679 1.0309 -0.0997 -0.1324 0.1329  31  VAL B C   
2254 O O   . VAL B 26  ? 1.4093 1.2093 1.1151 -0.1323 -0.1433 0.1539  31  VAL B O   
2255 C CB  . VAL B 26  ? 1.4115 1.2229 1.1466 -0.0961 -0.0747 0.0716  31  VAL B CB  
2256 C CG1 . VAL B 26  ? 1.2966 1.1147 1.0658 -0.0720 -0.0979 0.0672  31  VAL B CG1 
2257 C CG2 . VAL B 26  ? 1.5893 1.4034 1.3386 -0.0902 -0.0317 0.0417  31  VAL B CG2 
2258 N N   . SER B 27  ? 1.1520 0.9450 0.9757 -0.0733 -0.1552 0.1397  32  SER B N   
2259 C CA  . SER B 27  ? 1.1605 0.9488 1.0151 -0.0757 -0.1950 0.1776  32  SER B CA  
2260 C C   . SER B 27  ? 1.1191 0.9086 1.0461 -0.0455 -0.2090 0.1676  32  SER B C   
2261 O O   . SER B 27  ? 1.1409 0.9290 1.0944 -0.0230 -0.1882 0.1334  32  SER B O   
2262 C CB  . SER B 27  ? 1.2066 0.9779 1.0833 -0.0819 -0.2021 0.2056  32  SER B CB  
2263 O OG  . SER B 27  ? 1.2025 0.9630 1.1312 -0.0576 -0.1859 0.1820  32  SER B OG  
2264 N N   . LEU B 28  ? 1.1180 0.9113 1.0790 -0.0486 -0.2444 0.1995  33  LEU B N   
2265 C CA  . LEU B 28  ? 1.1118 0.9053 1.1588 -0.0219 -0.2556 0.1931  33  LEU B CA  
2266 C C   . LEU B 28  ? 1.0705 0.8419 1.1931 -0.0067 -0.2559 0.1992  33  LEU B C   
2267 O O   . LEU B 28  ? 1.2285 0.9886 1.3540 -0.0209 -0.2717 0.2351  33  LEU B O   
2268 C CB  . LEU B 28  ? 1.1631 0.9726 1.2335 -0.0325 -0.2956 0.2297  33  LEU B CB  
2269 C CG  . LEU B 28  ? 1.1738 0.9905 1.3347 -0.0065 -0.3008 0.2169  33  LEU B CG  
2270 C CD1 . LEU B 28  ? 1.1496 0.9784 1.2782 0.0032  -0.2719 0.1702  33  LEU B CD1 
2271 C CD2 . LEU B 28  ? 1.1776 1.0112 1.3820 -0.0190 -0.3492 0.2664  33  LEU B CD2 
2272 N N   . ALA B 29  ? 1.0035 0.7678 1.1844 0.0180  -0.2362 0.1628  34  ALA B N   
2273 C CA  . ALA B 29  ? 1.0224 0.7627 1.2704 0.0295  -0.2264 0.1530  34  ALA B CA  
2274 C C   . ALA B 29  ? 1.0046 0.7396 1.3385 0.0508  -0.2141 0.1240  34  ALA B C   
2275 O O   . ALA B 29  ? 1.0386 0.7861 1.3523 0.0584  -0.1947 0.0890  34  ALA B O   
2276 C CB  . ALA B 29  ? 1.0306 0.7644 1.2279 0.0261  -0.1985 0.1220  34  ALA B CB  
2277 N N   . PHE B 30  ? 1.0541 0.7695 1.4882 0.0587  -0.2214 0.1374  35  PHE B N   
2278 C CA  . PHE B 30  ? 1.1076 0.8140 1.6420 0.0772  -0.2019 0.1059  35  PHE B CA  
2279 C C   . PHE B 30  ? 1.0014 0.6806 1.5635 0.0794  -0.1661 0.0586  35  PHE B C   
2280 O O   . PHE B 30  ? 0.9326 0.5885 1.5411 0.0762  -0.1707 0.0733  35  PHE B O   
2281 C CB  . PHE B 30  ? 1.2787 0.9829 1.9332 0.0852  -0.2317 0.1511  35  PHE B CB  
2282 C CG  . PHE B 30  ? 1.4157 1.1130 2.1875 0.1047  -0.2057 0.1163  35  PHE B CG  
2283 C CD1 . PHE B 30  ? 1.3871 1.1072 2.1592 0.1123  -0.1953 0.0942  35  PHE B CD1 
2284 C CD2 . PHE B 30  ? 1.5754 1.2412 2.4586 0.1133  -0.1839 0.0984  35  PHE B CD2 
2285 C CE1 . PHE B 30  ? 1.3753 1.0888 2.2574 0.1278  -0.1633 0.0574  35  PHE B CE1 
2286 C CE2 . PHE B 30  ? 1.5632 1.2201 2.5605 0.1286  -0.1497 0.0581  35  PHE B CE2 
2287 C CZ  . PHE B 30  ? 1.4435 1.1254 2.4375 0.1355  -0.1380 0.0369  35  PHE B CZ  
2288 N N   . HIS B 31  ? 0.9494 0.6322 1.4832 0.0814  -0.1313 0.0030  36  HIS B N   
2289 C CA  . HIS B 31  ? 1.0404 0.7006 1.5901 0.0761  -0.0948 -0.0505 36  HIS B CA  
2290 C C   . HIS B 31  ? 1.1293 0.7669 1.8142 0.0872  -0.0742 -0.0705 36  HIS B C   
2291 O O   . HIS B 31  ? 1.1174 0.7661 1.8654 0.1005  -0.0731 -0.0665 36  HIS B O   
2292 C CB  . HIS B 31  ? 1.0542 0.7302 1.5193 0.0682  -0.0683 -0.0964 36  HIS B CB  
2293 C CG  . HIS B 31  ? 1.1384 0.7995 1.5710 0.0505  -0.0407 -0.1443 36  HIS B CG  
2294 N ND1 . HIS B 31  ? 1.1593 0.7996 1.6482 0.0449  -0.0035 -0.1961 36  HIS B ND1 
2295 C CD2 . HIS B 31  ? 1.2646 0.9313 1.6137 0.0333  -0.0444 -0.1504 36  HIS B CD2 
2296 C CE1 . HIS B 31  ? 1.3215 0.9544 1.7525 0.0212  0.0124  -0.2326 36  HIS B CE1 
2297 N NE2 . HIS B 31  ? 1.3737 1.0242 1.7233 0.0149  -0.0153 -0.2024 36  HIS B NE2 
2298 N N   . ARG B 32  ? 1.1186 0.7247 1.8531 0.0804  -0.0544 -0.0958 37  ARG B N   
2299 C CA  . ARG B 32  ? 1.0932 0.6702 1.9793 0.0905  -0.0335 -0.1102 37  ARG B CA  
2300 C C   . ARG B 32  ? 1.0840 0.6611 2.0290 0.0964  0.0105  -0.1643 37  ARG B C   
2301 O O   . ARG B 32  ? 1.1176 0.6888 2.2004 0.1140  0.0134  -0.1512 37  ARG B O   
2302 C CB  . ARG B 32  ? 1.1052 0.6463 2.0182 0.0766  -0.0144 -0.1374 37  ARG B CB  
2303 C CG  . ARG B 32  ? 1.2339 0.7384 2.3184 0.0862  0.0077  -0.1484 37  ARG B CG  
2304 C CD  . ARG B 32  ? 1.2170 0.6848 2.3289 0.0712  0.0192  -0.1647 37  ARG B CD  
2305 N NE  . ARG B 32  ? 1.1162 0.5811 2.2404 0.0745  -0.0289 -0.0887 37  ARG B NE  
2306 C CZ  . ARG B 32  ? 1.0141 0.4949 2.0186 0.0617  -0.0584 -0.0575 37  ARG B CZ  
2307 N NH1 . ARG B 32  ? 0.9932 0.4965 1.8589 0.0471  -0.0508 -0.0899 37  ARG B NH1 
2308 N NH2 . ARG B 32  ? 0.9488 0.4239 1.9786 0.0620  -0.0957 0.0106  37  ARG B NH2 
2309 N N   . THR B 33  ? 1.0725 0.6566 1.9202 0.0794  0.0447  -0.2221 38  THR B N   
2310 C CA  . THR B 33  ? 1.1466 0.7355 2.0195 0.0786  0.0903  -0.2753 38  THR B CA  
2311 C C   . THR B 33  ? 1.1876 0.8155 1.9886 0.0858  0.0722  -0.2526 38  THR B C   
2312 O O   . THR B 33  ? 1.2441 0.8845 2.1266 0.1029  0.0729  -0.2405 38  THR B O   
2313 C CB  . THR B 33  ? 1.1959 0.7683 2.0021 0.0472  0.1420  -0.3543 38  THR B CB  
2314 O OG1 . THR B 33  ? 1.2536 0.8487 1.8997 0.0278  0.1246  -0.3517 38  THR B OG1 
2315 C CG2 . THR B 33  ? 1.2246 0.7572 2.0931 0.0352  0.1601  -0.3814 38  THR B CG2 
2316 N N   . GLN B 34  ? 1.2013 0.8479 1.8594 0.0718  0.0565  -0.2471 39  GLN B N   
2317 C CA  . GLN B 34  ? 1.1083 0.7878 1.6808 0.0722  0.0482  -0.2375 39  GLN B CA  
2318 C C   . GLN B 34  ? 1.0285 0.7323 1.6189 0.0913  0.0083  -0.1813 39  GLN B C   
2319 O O   . GLN B 34  ? 1.0425 0.7693 1.5912 0.0921  0.0121  -0.1845 39  GLN B O   
2320 C CB  . GLN B 34  ? 1.1368 0.8282 1.5694 0.0526  0.0379  -0.2385 39  GLN B CB  
2321 C CG  . GLN B 34  ? 1.1752 0.8558 1.5523 0.0239  0.0741  -0.2955 39  GLN B CG  
2322 C CD  . GLN B 34  ? 1.1862 0.8888 1.4351 0.0058  0.0560  -0.2843 39  GLN B CD  
2323 O OE1 . GLN B 34  ? 1.1446 0.8708 1.3479 0.0154  0.0308  -0.2470 39  GLN B OE1 
2324 N NE2 . GLN B 34  ? 1.2287 0.9228 1.4260 -0.0239 0.0705  -0.3191 39  GLN B NE2 
2325 N N   . GLY B 35  ? 0.9737 0.6739 1.6141 0.1014  -0.0306 -0.1297 40  GLY B N   
2326 C CA  . GLY B 35  ? 0.8913 0.6158 1.5517 0.1123  -0.0706 -0.0767 40  GLY B CA  
2327 C C   . GLY B 35  ? 0.8338 0.5722 1.4019 0.1043  -0.1123 -0.0289 40  GLY B C   
2328 O O   . GLY B 35  ? 0.8431 0.5701 1.3541 0.0944  -0.1160 -0.0252 40  GLY B O   
2329 N N   . LEU B 36  ? 0.8569 0.6203 1.4137 0.1056  -0.1409 0.0047  41  LEU B N   
2330 C CA  . LEU B 36  ? 0.8613 0.6382 1.3310 0.0925  -0.1755 0.0457  41  LEU B CA  
2331 C C   . LEU B 36  ? 0.8100 0.5953 1.1645 0.0839  -0.1565 0.0198  41  LEU B C   
2332 O O   . LEU B 36  ? 0.8134 0.6085 1.1514 0.0876  -0.1327 -0.0122 41  LEU B O   
2333 C CB  . LEU B 36  ? 0.9212 0.7227 1.4146 0.0902  -0.2114 0.0850  41  LEU B CB  
2334 C CG  . LEU B 36  ? 0.9653 0.7772 1.3845 0.0690  -0.2503 0.1324  41  LEU B CG  
2335 C CD1 . LEU B 36  ? 0.9798 0.7754 1.4377 0.0628  -0.2766 0.1756  41  LEU B CD1 
2336 C CD2 . LEU B 36  ? 1.0284 0.8688 1.4542 0.0602  -0.2825 0.1600  41  LEU B CD2 
2337 N N   . MET B 37  ? 0.7879 0.5690 1.0724 0.0717  -0.1653 0.0354  42  MET B N   
2338 C CA  . MET B 37  ? 0.7542 0.5418 0.9479 0.0639  -0.1477 0.0160  42  MET B CA  
2339 C C   . MET B 37  ? 0.7162 0.5096 0.8483 0.0487  -0.1653 0.0471  42  MET B C   
2340 O O   . MET B 37  ? 0.8193 0.6105 0.9658 0.0405  -0.1914 0.0831  42  MET B O   
2341 C CB  . MET B 37  ? 0.7922 0.5643 0.9792 0.0624  -0.1263 -0.0117 42  MET B CB  
2342 C CG  . MET B 37  ? 0.8048 0.5621 1.0588 0.0695  -0.1060 -0.0441 42  MET B CG  
2343 S SD  . MET B 37  ? 0.8481 0.5975 1.0675 0.0585  -0.0735 -0.0938 42  MET B SD  
2344 C CE  . MET B 37  ? 0.9017 0.6357 1.1093 0.0483  -0.0864 -0.0784 42  MET B CE  
2345 N N   . ILE B 38  ? 0.6760 0.4766 0.7434 0.0423  -0.1495 0.0343  43  ILE B N   
2346 C CA  . ILE B 38  ? 0.7588 0.5628 0.7690 0.0254  -0.1530 0.0532  43  ILE B CA  
2347 C C   . ILE B 38  ? 0.7749 0.5711 0.7697 0.0229  -0.1376 0.0448  43  ILE B C   
2348 O O   . ILE B 38  ? 0.8770 0.6770 0.8699 0.0297  -0.1215 0.0211  43  ILE B O   
2349 C CB  . ILE B 38  ? 0.7922 0.6123 0.7566 0.0188  -0.1433 0.0442  43  ILE B CB  
2350 C CG1 . ILE B 38  ? 0.7911 0.6217 0.7646 0.0131  -0.1655 0.0588  43  ILE B CG1 
2351 C CG2 . ILE B 38  ? 0.8496 0.6703 0.7600 0.0009  -0.1300 0.0483  43  ILE B CG2 
2352 C CD1 . ILE B 38  ? 0.8508 0.6819 0.7984 -0.0106 -0.1921 0.0945  43  ILE B CD1 
2353 N N   . MET B 39  ? 0.8145 0.6020 0.7980 0.0099  -0.1443 0.0673  44  MET B N   
2354 C CA  . MET B 39  ? 0.7871 0.5689 0.7652 0.0054  -0.1317 0.0632  44  MET B CA  
2355 C C   . MET B 39  ? 0.7507 0.5400 0.6825 -0.0110 -0.1177 0.0711  44  MET B C   
2356 O O   . MET B 39  ? 0.8182 0.6038 0.7248 -0.0285 -0.1246 0.0941  44  MET B O   
2357 C CB  . MET B 39  ? 0.8258 0.5887 0.8418 0.0029  -0.1446 0.0798  44  MET B CB  
2358 C CG  . MET B 39  ? 0.8767 0.6349 0.8978 -0.0015 -0.1329 0.0706  44  MET B CG  
2359 S SD  . MET B 39  ? 0.9779 0.7109 1.0490 -0.0065 -0.1442 0.0866  44  MET B SD  
2360 C CE  . MET B 39  ? 1.0590 0.7782 1.1923 0.0100  -0.1481 0.0632  44  MET B CE  
2361 N N   . LYS B 40  ? 0.7424 0.5428 0.6670 -0.0078 -0.0970 0.0529  45  LYS B N   
2362 C CA  . LYS B 40  ? 0.7821 0.5879 0.6858 -0.0217 -0.0743 0.0544  45  LYS B CA  
2363 C C   . LYS B 40  ? 0.8130 0.6151 0.7439 -0.0242 -0.0714 0.0601  45  LYS B C   
2364 O O   . LYS B 40  ? 0.7708 0.5803 0.7302 -0.0147 -0.0718 0.0499  45  LYS B O   
2365 C CB  . LYS B 40  ? 0.8109 0.6308 0.7155 -0.0158 -0.0533 0.0361  45  LYS B CB  
2366 C CG  . LYS B 40  ? 0.9402 0.7652 0.8506 -0.0270 -0.0231 0.0335  45  LYS B CG  
2367 C CD  . LYS B 40  ? 1.0354 0.8675 0.9423 -0.0294 0.0039  0.0172  45  LYS B CD  
2368 C CE  . LYS B 40  ? 1.1480 0.9823 1.0765 -0.0420 0.0406  0.0123  45  LYS B CE  
2369 N NZ  . LYS B 40  ? 1.2182 1.0466 1.1086 -0.0645 0.0727  -0.0050 45  LYS B NZ  
2370 N N   . THR B 41  ? 0.8129 0.6052 0.7322 -0.0408 -0.0703 0.0786  46  THR B N   
2371 C CA  . THR B 41  ? 0.8285 0.6172 0.7750 -0.0470 -0.0651 0.0860  46  THR B CA  
2372 C C   . THR B 41  ? 0.8059 0.6067 0.7528 -0.0575 -0.0323 0.0801  46  THR B C   
2373 O O   . THR B 41  ? 0.7970 0.5951 0.7079 -0.0771 -0.0120 0.0843  46  THR B O   
2374 C CB  . THR B 41  ? 0.8972 0.6676 0.8396 -0.0604 -0.0794 0.1122  46  THR B CB  
2375 O OG1 . THR B 41  ? 0.9572 0.7160 0.9233 -0.0471 -0.1063 0.1151  46  THR B OG1 
2376 C CG2 . THR B 41  ? 0.9020 0.6678 0.8767 -0.0683 -0.0724 0.1191  46  THR B CG2 
2377 N N   . VAL B 42  ? 0.8135 0.6282 0.8051 -0.0477 -0.0270 0.0711  47  VAL B N   
2378 C CA  . VAL B 42  ? 0.7800 0.6100 0.8007 -0.0513 0.0040  0.0649  47  VAL B CA  
2379 C C   . VAL B 42  ? 0.8221 0.6508 0.8656 -0.0678 0.0226  0.0750  47  VAL B C   
2380 O O   . VAL B 42  ? 0.8827 0.7122 0.9205 -0.0829 0.0593  0.0699  47  VAL B O   
2381 C CB  . VAL B 42  ? 0.7182 0.5677 0.7867 -0.0351 -0.0062 0.0604  47  VAL B CB  
2382 C CG1 . VAL B 42  ? 0.7313 0.5980 0.8555 -0.0361 0.0239  0.0598  47  VAL B CG1 
2383 C CG2 . VAL B 42  ? 0.7779 0.6273 0.8183 -0.0222 -0.0189 0.0505  47  VAL B CG2 
2384 N N   . TYR B 43  ? 0.8129 0.6391 0.8839 -0.0676 0.0013  0.0856  48  TYR B N   
2385 C CA  . TYR B 43  ? 0.8024 0.6284 0.9053 -0.0829 0.0153  0.0968  48  TYR B CA  
2386 C C   . TYR B 43  ? 0.8488 0.6532 0.9353 -0.0906 -0.0072 0.1117  48  TYR B C   
2387 O O   . TYR B 43  ? 0.7835 0.5804 0.8748 -0.0797 -0.0377 0.1087  48  TYR B O   
2388 C CB  . TYR B 43  ? 0.7755 0.6249 0.9541 -0.0770 0.0112  0.0969  48  TYR B CB  
2389 C CG  . TYR B 43  ? 0.7909 0.6445 1.0182 -0.0923 0.0251  0.1080  48  TYR B CG  
2390 C CD1 . TYR B 43  ? 0.7436 0.5882 0.9840 -0.0986 -0.0002 0.1166  48  TYR B CD1 
2391 C CD2 . TYR B 43  ? 0.7901 0.6561 1.0590 -0.1017 0.0677  0.1071  48  TYR B CD2 
2392 C CE1 . TYR B 43  ? 0.7785 0.6274 1.0676 -0.1138 0.0129  0.1273  48  TYR B CE1 
2393 C CE2 . TYR B 43  ? 0.7917 0.6633 1.1126 -0.1165 0.0840  0.1169  48  TYR B CE2 
2394 C CZ  . TYR B 43  ? 0.8148 0.6788 1.1442 -0.1225 0.0547  0.1287  48  TYR B CZ  
2395 O OH  . TYR B 43  ? 0.8545 0.7246 1.2391 -0.1384 0.0716  0.1388  48  TYR B OH  
2396 N N   . LYS B 44  ? 0.9126 0.7065 0.9840 -0.1119 0.0120  0.1270  49  LYS B N   
2397 C CA  . LYS B 44  ? 0.9102 0.6841 0.9840 -0.1232 -0.0038 0.1483  49  LYS B CA  
2398 C C   . LYS B 44  ? 0.9134 0.6920 1.0165 -0.1440 0.0263  0.1576  49  LYS B C   
2399 O O   . LYS B 44  ? 0.8967 0.6803 0.9736 -0.1613 0.0636  0.1561  49  LYS B O   
2400 C CB  . LYS B 44  ? 0.9586 0.7127 0.9718 -0.1331 -0.0161 0.1684  49  LYS B CB  
2401 C CG  . LYS B 44  ? 0.9467 0.6772 0.9790 -0.1365 -0.0438 0.1936  49  LYS B CG  
2402 C CD  . LYS B 44  ? 0.9425 0.6586 0.9235 -0.1504 -0.0590 0.2246  49  LYS B CD  
2403 C CE  . LYS B 44  ? 0.9176 0.6340 0.8891 -0.1301 -0.0845 0.2164  49  LYS B CE  
2404 N NZ  . LYS B 44  ? 0.9641 0.6714 0.8962 -0.1456 -0.1070 0.2530  49  LYS B NZ  
2405 N N   . GLY B 45  ? 0.9486 0.7254 1.1068 -0.1451 0.0137  0.1636  50  GLY B N   
2406 C CA  . GLY B 45  ? 1.0161 0.8015 1.2202 -0.1633 0.0415  0.1713  50  GLY B CA  
2407 C C   . GLY B 45  ? 1.0359 0.8288 1.3148 -0.1602 0.0205  0.1695  50  GLY B C   
2408 O O   . GLY B 45  ? 1.0225 0.8029 1.3046 -0.1511 -0.0141 0.1651  50  GLY B O   
2409 N N   . PRO B 46  ? 1.0836 0.8972 1.4270 -0.1707 0.0431  0.1709  51  PRO B N   
2410 C CA  . PRO B 46  ? 1.0699 0.8976 1.4881 -0.1716 0.0190  0.1690  51  PRO B CA  
2411 C C   . PRO B 46  ? 1.0386 0.8886 1.4752 -0.1549 -0.0135 0.1530  51  PRO B C   
2412 O O   . PRO B 46  ? 1.1494 1.0191 1.5871 -0.1432 -0.0028 0.1475  51  PRO B O   
2413 C CB  . PRO B 46  ? 1.1423 0.9933 1.6306 -0.1859 0.0557  0.1761  51  PRO B CB  
2414 C CG  . PRO B 46  ? 1.1922 1.0273 1.6285 -0.2008 0.1013  0.1833  51  PRO B CG  
2415 C CD  . PRO B 46  ? 1.1674 0.9895 1.5189 -0.1885 0.0946  0.1752  51  PRO B CD  
2416 N N   . ASN B 47  ? 1.0675 0.9134 1.5171 -0.1575 -0.0505 0.1452  52  ASN B N   
2417 C CA  . ASN B 47  ? 1.2241 1.0903 1.6741 -0.1498 -0.0836 0.1305  52  ASN B CA  
2418 C C   . ASN B 47  ? 1.3002 1.2105 1.8269 -0.1562 -0.0925 0.1397  52  ASN B C   
2419 O O   . ASN B 47  ? 1.1298 1.0517 1.7213 -0.1703 -0.0846 0.1510  52  ASN B O   
2420 C CB  . ASN B 47  ? 1.2220 1.0665 1.6483 -0.1563 -0.1150 0.1118  52  ASN B CB  
2421 C CG  . ASN B 47  ? 1.1802 1.0254 1.6595 -0.1789 -0.1291 0.1104  52  ASN B CG  
2422 O OD1 . ASN B 47  ? 1.3027 1.1477 1.8258 -0.1883 -0.1107 0.1272  52  ASN B OD1 
2423 N ND2 . ASN B 47  ? 1.2602 1.1047 1.7322 -0.1914 -0.1595 0.0875  52  ASN B ND2 
2424 N N   . CYS B 48  ? 1.5139 1.4492 2.0389 -0.1465 -0.1099 0.1387  53  CYS B N   
2425 C CA  . CYS B 48  ? 1.5472 1.5282 2.1494 -0.1534 -0.1321 0.1549  53  CYS B CA  
2426 C C   . CYS B 48  ? 1.5660 1.5615 2.1290 -0.1561 -0.1755 0.1496  53  CYS B C   
2427 O O   . CYS B 48  ? 1.4544 1.4524 1.9854 -0.1398 -0.1717 0.1497  53  CYS B O   
2428 C CB  . CYS B 48  ? 1.5041 1.5069 2.1700 -0.1400 -0.0967 0.1707  53  CYS B CB  
2429 S SG  . CYS B 48  ? 1.3217 1.3212 2.0558 -0.1484 -0.0434 0.1776  53  CYS B SG  
2430 N N   . ILE B 49  ? 1.6458 1.6496 2.2079 -0.1808 -0.2139 0.1434  54  ILE B N   
2431 C CA  . ILE B 49  ? 1.6549 1.6688 2.1617 -0.1952 -0.2541 0.1325  54  ILE B CA  
2432 C C   . ILE B 49  ? 1.6521 1.7161 2.1991 -0.2016 -0.2874 0.1636  54  ILE B C   
2433 O O   . ILE B 49  ? 1.7238 1.7969 2.2122 -0.2136 -0.3167 0.1594  54  ILE B O   
2434 C CB  . ILE B 49  ? 1.4795 1.4840 1.9670 -0.2281 -0.2808 0.1096  54  ILE B CB  
2435 C CG1 . ILE B 49  ? 1.7654 1.7168 2.2269 -0.2216 -0.2497 0.0829  54  ILE B CG1 
2436 C CG2 . ILE B 49  ? 1.7893 1.7925 2.1918 -0.2480 -0.3097 0.0848  54  ILE B CG2 
2437 C CD1 . ILE B 49  ? 1.8105 1.7389 2.2431 -0.2501 -0.2661 0.0483  54  ILE B CD1 
2438 N N   . GLU B 50  ? 1.5312 1.6271 2.1830 -0.1958 -0.2814 0.1961  55  GLU B N   
2439 C CA  . GLU B 50  ? 1.4465 1.5913 2.1711 -0.1961 -0.3086 0.2362  55  GLU B CA  
2440 C C   . GLU B 50  ? 1.2471 1.3911 1.9305 -0.1768 -0.3050 0.2423  55  GLU B C   
2441 O O   . GLU B 50  ? 1.2474 1.4256 1.9404 -0.1904 -0.3480 0.2702  55  GLU B O   
2442 C CB  . GLU B 50  ? 1.5270 1.6971 2.3884 -0.1853 -0.2841 0.2638  55  GLU B CB  
2443 C CG  . GLU B 50  ? 1.4713 1.6123 2.3445 -0.1552 -0.2157 0.2498  55  GLU B CG  
2444 C CD  . GLU B 50  ? 1.4480 1.5998 2.4321 -0.1549 -0.1788 0.2589  55  GLU B CD  
2445 O OE1 . GLU B 50  ? 1.2775 1.4730 2.3776 -0.1664 -0.2032 0.2895  55  GLU B OE1 
2446 O OE2 . GLU B 50  ? 1.4644 1.5824 2.4206 -0.1458 -0.1251 0.2370  55  GLU B OE2 
2447 N N   . HIS B 51  ? 1.0103 1.1174 1.6479 -0.1493 -0.2577 0.2195  56  HIS B N   
2448 C CA  . HIS B 51  ? 0.9539 1.0563 1.5524 -0.1303 -0.2495 0.2212  56  HIS B CA  
2449 C C   . HIS B 51  ? 0.8861 0.9580 1.3587 -0.1325 -0.2555 0.1896  56  HIS B C   
2450 O O   . HIS B 51  ? 0.8399 0.9088 1.2772 -0.1196 -0.2508 0.1905  56  HIS B O   
2451 C CB  . HIS B 51  ? 0.9610 1.0493 1.6037 -0.1018 -0.1935 0.2185  56  HIS B CB  
2452 C CG  . HIS B 51  ? 1.0050 1.1271 1.7855 -0.0972 -0.1825 0.2498  56  HIS B CG  
2453 N ND1 . HIS B 51  ? 1.0742 1.1936 1.9229 -0.0964 -0.1448 0.2454  56  HIS B ND1 
2454 C CD2 . HIS B 51  ? 1.0060 1.1660 1.8794 -0.0942 -0.2032 0.2880  56  HIS B CD2 
2455 C CE1 . HIS B 51  ? 1.0112 1.1653 1.9947 -0.0919 -0.1386 0.2751  56  HIS B CE1 
2456 N NE2 . HIS B 51  ? 1.0271 1.2065 2.0332 -0.0893 -0.1759 0.3037  56  HIS B NE2 
2457 N N   . ASN B 52  ? 0.8520 0.9026 1.2677 -0.1503 -0.2650 0.1618  57  ASN B N   
2458 C CA  . ASN B 52  ? 0.8735 0.8944 1.1868 -0.1543 -0.2657 0.1274  57  ASN B CA  
2459 C C   . ASN B 52  ? 0.9142 0.9554 1.1772 -0.1712 -0.2970 0.1327  57  ASN B C   
2460 O O   . ASN B 52  ? 0.9266 0.9482 1.1243 -0.1620 -0.2837 0.1130  57  ASN B O   
2461 C CB  . ASN B 52  ? 0.9107 0.9065 1.1949 -0.1742 -0.2693 0.0965  57  ASN B CB  
2462 C CG  . ASN B 52  ? 0.9483 0.9113 1.2545 -0.1566 -0.2338 0.0875  57  ASN B CG  
2463 O OD1 . ASN B 52  ? 0.8041 0.7665 1.1437 -0.1349 -0.2062 0.1034  57  ASN B OD1 
2464 N ND2 . ASN B 52  ? 1.0680 1.0031 1.3566 -0.1702 -0.2333 0.0621  57  ASN B ND2 
2465 N N   . GLU B 53  ? 0.9561 1.0384 1.2520 -0.1980 -0.3393 0.1629  58  GLU B N   
2466 C CA  . GLU B 53  ? 1.0225 1.1304 1.2696 -0.2222 -0.3753 0.1784  58  GLU B CA  
2467 C C   . GLU B 53  ? 0.9654 1.0814 1.2333 -0.1941 -0.3626 0.2054  58  GLU B C   
2468 O O   . GLU B 53  ? 0.9302 1.0386 1.1255 -0.1974 -0.3621 0.1959  58  GLU B O   
2469 C CB  . GLU B 53  ? 1.1669 1.3228 1.4550 -0.2608 -0.4307 0.2154  58  GLU B CB  
2470 C CG  . GLU B 53  ? 1.2886 1.4393 1.5425 -0.2995 -0.4497 0.1853  58  GLU B CG  
2471 C CD  . GLU B 53  ? 1.3814 1.5234 1.7173 -0.2873 -0.4324 0.1812  58  GLU B CD  
2472 O OE1 . GLU B 53  ? 1.4066 1.5124 1.7066 -0.2934 -0.4125 0.1376  58  GLU B OE1 
2473 O OE2 . GLU B 53  ? 1.4526 1.6222 1.8956 -0.2714 -0.4348 0.2214  58  GLU B OE2 
2474 N N   . ALA B 54  ? 0.8975 1.0264 1.2685 -0.1681 -0.3472 0.2350  59  ALA B N   
2475 C CA  . ALA B 54  ? 0.8515 0.9837 1.2610 -0.1399 -0.3271 0.2565  59  ALA B CA  
2476 C C   . ALA B 54  ? 0.8479 0.9373 1.1959 -0.1127 -0.2799 0.2175  59  ALA B C   
2477 O O   . ALA B 54  ? 0.8362 0.9232 1.1609 -0.1021 -0.2733 0.2226  59  ALA B O   
2478 C CB  . ALA B 54  ? 0.8359 0.9893 1.3814 -0.1221 -0.3136 0.2891  59  ALA B CB  
2479 N N   . LEU B 55  ? 0.7933 0.8509 1.1206 -0.1035 -0.2502 0.1833  60  LEU B N   
2480 C CA  . LEU B 55  ? 0.7231 0.7418 0.9895 -0.0832 -0.2135 0.1489  60  LEU B CA  
2481 C C   . LEU B 55  ? 0.7298 0.7349 0.9039 -0.0930 -0.2243 0.1251  60  LEU B C   
2482 O O   . LEU B 55  ? 0.7286 0.7202 0.8703 -0.0773 -0.2061 0.1151  60  LEU B O   
2483 C CB  . LEU B 55  ? 0.7090 0.6999 0.9730 -0.0789 -0.1897 0.1264  60  LEU B CB  
2484 C CG  . LEU B 55  ? 0.6786 0.6726 1.0176 -0.0680 -0.1606 0.1391  60  LEU B CG  
2485 C CD1 . LEU B 55  ? 0.6304 0.6041 0.9659 -0.0756 -0.1502 0.1257  60  LEU B CD1 
2486 C CD2 . LEU B 55  ? 0.6429 0.6233 0.9803 -0.0468 -0.1220 0.1330  60  LEU B CD2 
2487 N N   . LEU B 56  ? 0.7878 0.7963 0.9234 -0.1217 -0.2506 0.1131  61  LEU B N   
2488 C CA  . LEU B 56  ? 0.8213 0.8179 0.8722 -0.1382 -0.2554 0.0848  61  LEU B CA  
2489 C C   . LEU B 56  ? 0.8552 0.8758 0.8836 -0.1458 -0.2713 0.1083  61  LEU B C   
2490 O O   . LEU B 56  ? 0.9358 0.9416 0.9102 -0.1414 -0.2556 0.0886  61  LEU B O   
2491 C CB  . LEU B 56  ? 0.8974 0.8939 0.9134 -0.1754 -0.2773 0.0630  61  LEU B CB  
2492 C CG  . LEU B 56  ? 0.9620 0.9377 0.8929 -0.1961 -0.2687 0.0189  61  LEU B CG  
2493 C CD1 . LEU B 56  ? 0.9505 0.8830 0.8784 -0.1694 -0.2299 -0.0179 61  LEU B CD1 
2494 C CD2 . LEU B 56  ? 1.0304 1.0132 0.9253 -0.2434 -0.2928 -0.0012 61  LEU B CD2 
2495 N N   . GLU B 57  ? 0.9343 0.9929 1.0112 -0.1585 -0.3035 0.1538  62  GLU B N   
2496 C CA  . GLU B 57  ? 0.9525 1.0369 1.0230 -0.1666 -0.3235 0.1891  62  GLU B CA  
2497 C C   . GLU B 57  ? 0.8786 0.9493 0.9756 -0.1296 -0.2899 0.1934  62  GLU B C   
2498 O O   . GLU B 57  ? 0.8821 0.9530 0.9343 -0.1331 -0.2890 0.1960  62  GLU B O   
2499 C CB  . GLU B 57  ? 0.9997 1.1302 1.1394 -0.1870 -0.3698 0.2459  62  GLU B CB  
2500 C CG  . GLU B 57  ? 1.1554 1.3167 1.2929 -0.2023 -0.4007 0.2943  62  GLU B CG  
2501 C CD  . GLU B 57  ? 1.2741 1.4300 1.2850 -0.2359 -0.4089 0.2734  62  GLU B CD  
2502 O OE1 . GLU B 57  ? 1.3592 1.5100 1.2952 -0.2705 -0.4192 0.2399  62  GLU B OE1 
2503 O OE2 . GLU B 57  ? 1.2007 1.3561 1.1891 -0.2300 -0.4010 0.2873  62  GLU B OE2 
2504 N N   . GLU B 58  ? 0.8183 0.8760 0.9820 -0.0985 -0.2601 0.1906  63  GLU B N   
2505 C CA  . GLU B 58  ? 0.7611 0.7998 0.9381 -0.0678 -0.2227 0.1820  63  GLU B CA  
2506 C C   . GLU B 58  ? 0.7653 0.7723 0.8605 -0.0609 -0.2000 0.1394  63  GLU B C   
2507 O O   . GLU B 58  ? 0.9043 0.9051 0.9849 -0.0493 -0.1852 0.1374  63  GLU B O   
2508 C CB  . GLU B 58  ? 0.7994 0.8301 1.0539 -0.0446 -0.1911 0.1820  63  GLU B CB  
2509 C CG  . GLU B 58  ? 0.8751 0.9289 1.2290 -0.0350 -0.1892 0.2207  63  GLU B CG  
2510 C CD  . GLU B 58  ? 0.8972 0.9458 1.3350 -0.0194 -0.1535 0.2171  63  GLU B CD  
2511 O OE1 . GLU B 58  ? 0.8621 0.8817 1.2662 -0.0089 -0.1163 0.1821  63  GLU B OE1 
2512 O OE2 . GLU B 58  ? 0.9817 1.0569 1.5235 -0.0205 -0.1619 0.2508  63  GLU B OE2 
2513 N N   . ALA B 59  ? 0.7723 0.7597 0.8264 -0.0679 -0.1969 0.1073  64  ALA B N   
2514 C CA  . ALA B 59  ? 0.7449 0.7048 0.7355 -0.0641 -0.1790 0.0688  64  ALA B CA  
2515 C C   . ALA B 59  ? 0.7853 0.7528 0.7156 -0.0849 -0.1894 0.0617  64  ALA B C   
2516 O O   . ALA B 59  ? 0.8195 0.7719 0.7180 -0.0757 -0.1694 0.0405  64  ALA B O   
2517 C CB  . ALA B 59  ? 0.8341 0.7710 0.8129 -0.0681 -0.1740 0.0403  64  ALA B CB  
2518 N N   . LYS B 60  ? 0.8530 0.8457 0.7669 -0.1164 -0.2208 0.0803  65  LYS B N   
2519 C CA  . LYS B 60  ? 0.9141 0.9207 0.7648 -0.1448 -0.2334 0.0835  65  LYS B CA  
2520 C C   . LYS B 60  ? 0.9207 0.9387 0.7885 -0.1304 -0.2294 0.1143  65  LYS B C   
2521 O O   . LYS B 60  ? 1.0628 1.0747 0.8781 -0.1377 -0.2162 0.0997  65  LYS B O   
2522 C CB  . LYS B 60  ? 1.0202 1.0555 0.8440 -0.1896 -0.2748 0.1031  65  LYS B CB  
2523 C CG  . LYS B 60  ? 1.1287 1.1488 0.9121 -0.2153 -0.2747 0.0598  65  LYS B CG  
2524 C CD  . LYS B 60  ? 1.2436 1.2947 1.0024 -0.2641 -0.3194 0.0792  65  LYS B CD  
2525 C CE  . LYS B 60  ? 1.1812 1.2273 0.9724 -0.2716 -0.3287 0.0649  65  LYS B CE  
2526 N NZ  . LYS B 60  ? 1.2461 1.3270 1.0138 -0.3237 -0.3773 0.0859  65  LYS B NZ  
2527 N N   . MET B 61  ? 0.8438 0.8763 0.7916 -0.1108 -0.2358 0.1535  66  MET B N   
2528 C CA  . MET B 61  ? 0.8533 0.8924 0.8371 -0.0941 -0.2274 0.1817  66  MET B CA  
2529 C C   . MET B 61  ? 0.8358 0.8454 0.8077 -0.0663 -0.1868 0.1466  66  MET B C   
2530 O O   . MET B 61  ? 0.8506 0.8594 0.8017 -0.0655 -0.1777 0.1496  66  MET B O   
2531 C CB  . MET B 61  ? 0.8794 0.9372 0.9705 -0.0791 -0.2361 0.2253  66  MET B CB  
2532 C CG  . MET B 61  ? 0.9616 1.0578 1.0841 -0.1073 -0.2844 0.2769  66  MET B CG  
2533 S SD  . MET B 61  ? 0.8857 1.0074 1.1609 -0.0889 -0.2932 0.3353  66  MET B SD  
2534 C CE  . MET B 61  ? 0.8774 1.0102 1.2011 -0.0944 -0.3063 0.3321  66  MET B CE  
2535 N N   . MET B 62  ? 0.8077 0.7951 0.7925 -0.0470 -0.1656 0.1169  67  MET B N   
2536 C CA  . MET B 62  ? 0.8051 0.7665 0.7733 -0.0263 -0.1345 0.0839  67  MET B CA  
2537 C C   . MET B 62  ? 0.8366 0.7880 0.7403 -0.0362 -0.1275 0.0553  67  MET B C   
2538 O O   . MET B 62  ? 0.9863 0.9302 0.8836 -0.0250 -0.1094 0.0454  67  MET B O   
2539 C CB  . MET B 62  ? 0.8481 0.7902 0.8280 -0.0144 -0.1225 0.0626  67  MET B CB  
2540 C CG  . MET B 62  ? 0.8841 0.8286 0.9252 -0.0019 -0.1122 0.0784  67  MET B CG  
2541 S SD  . MET B 62  ? 0.9167 0.8405 0.9546 0.0015  -0.1027 0.0584  67  MET B SD  
2542 C CE  . MET B 62  ? 0.9520 0.8887 1.0653 0.0041  -0.0928 0.0818  67  MET B CE  
2543 N N   . ASN B 63  ? 0.8781 0.8299 0.7398 -0.0596 -0.1392 0.0397  68  ASN B N   
2544 C CA  . ASN B 63  ? 0.8729 0.8137 0.6785 -0.0739 -0.1253 0.0049  68  ASN B CA  
2545 C C   . ASN B 63  ? 0.8886 0.8448 0.6566 -0.0914 -0.1252 0.0182  68  ASN B C   
2546 O O   . ASN B 63  ? 0.9055 0.8510 0.6459 -0.0925 -0.1017 -0.0093 68  ASN B O   
2547 C CB  . ASN B 63  ? 0.9752 0.9113 0.7478 -0.1006 -0.1340 -0.0190 68  ASN B CB  
2548 C CG  . ASN B 63  ? 1.0236 0.9383 0.7621 -0.1092 -0.1071 -0.0679 68  ASN B CG  
2549 O OD1 . ASN B 63  ? 1.1106 1.0299 0.7923 -0.1435 -0.1037 -0.0868 68  ASN B OD1 
2550 N ND2 . ASN B 63  ? 0.9705 0.8622 0.7470 -0.0813 -0.0870 -0.0888 68  ASN B ND2 
2551 N N   . ARG B 64  ? 0.9434 0.9254 0.7184 -0.1058 -0.1517 0.0633  69  ARG B N   
2552 C CA  . ARG B 64  ? 0.9823 0.9813 0.7260 -0.1252 -0.1572 0.0891  69  ARG B CA  
2553 C C   . ARG B 64  ? 0.9110 0.9023 0.6872 -0.0984 -0.1334 0.0937  69  ARG B C   
2554 O O   . ARG B 64  ? 1.0206 1.0176 0.7617 -0.1134 -0.1260 0.0997  69  ARG B O   
2555 C CB  . ARG B 64  ? 1.0347 1.0656 0.7975 -0.1460 -0.1985 0.1478  69  ARG B CB  
2556 C CG  . ARG B 64  ? 1.1279 1.1750 0.8347 -0.1894 -0.2289 0.1487  69  ARG B CG  
2557 C CD  . ARG B 64  ? 1.1121 1.1944 0.8563 -0.2076 -0.2765 0.2126  69  ARG B CD  
2558 N NE  . ARG B 64  ? 1.1440 1.2478 0.8817 -0.2240 -0.2935 0.2632  69  ARG B NE  
2559 C CZ  . ARG B 64  ? 1.1816 1.3215 0.9420 -0.2507 -0.3421 0.3297  69  ARG B CZ  
2560 N NH1 . ARG B 64  ? 1.1909 1.3528 0.9841 -0.2651 -0.3803 0.3529  69  ARG B NH1 
2561 N NH2 . ARG B 64  ? 1.2135 1.3695 0.9698 -0.2648 -0.3553 0.3777  69  ARG B NH2 
2562 N N   . LEU B 65  ? 0.8393 0.8184 0.6786 -0.0637 -0.1211 0.0911  70  LEU B N   
2563 C CA  . LEU B 65  ? 0.8448 0.8158 0.7194 -0.0406 -0.0990 0.0921  70  LEU B CA  
2564 C C   . LEU B 65  ? 0.8543 0.8058 0.7047 -0.0303 -0.0716 0.0473  70  LEU B C   
2565 O O   . LEU B 65  ? 0.9081 0.8444 0.7819 -0.0101 -0.0613 0.0259  70  LEU B O   
2566 C CB  . LEU B 65  ? 0.8180 0.7852 0.7662 -0.0160 -0.0954 0.1055  70  LEU B CB  
2567 C CG  . LEU B 65  ? 0.7937 0.7814 0.7948 -0.0219 -0.1189 0.1519  70  LEU B CG  
2568 C CD1 . LEU B 65  ? 0.7429 0.7224 0.8142 0.0001  -0.1045 0.1497  70  LEU B CD1 
2569 C CD2 . LEU B 65  ? 0.8251 0.8281 0.8502 -0.0298 -0.1271 0.1935  70  LEU B CD2 
2570 N N   . ARG B 66  ? 0.9009 0.8551 0.7075 -0.0474 -0.0608 0.0367  71  ARG B N   
2571 C CA  . ARG B 66  ? 0.9291 0.8692 0.7224 -0.0418 -0.0338 -0.0046 71  ARG B CA  
2572 C C   . ARG B 66  ? 0.8961 0.8387 0.7045 -0.0354 -0.0165 0.0019  71  ARG B C   
2573 O O   . ARG B 66  ? 0.9538 0.9088 0.7389 -0.0544 -0.0178 0.0252  71  ARG B O   
2574 C CB  . ARG B 66  ? 1.0454 0.9853 0.7790 -0.0716 -0.0259 -0.0311 71  ARG B CB  
2575 C CG  . ARG B 66  ? 1.1506 1.0847 0.8710 -0.0808 -0.0395 -0.0454 71  ARG B CG  
2576 C CD  . ARG B 66  ? 1.3258 1.2567 0.9855 -0.1158 -0.0242 -0.0808 71  ARG B CD  
2577 N NE  . ARG B 66  ? 1.3761 1.2915 1.0389 -0.1193 -0.0237 -0.1123 71  ARG B NE  
2578 C CZ  . ARG B 66  ? 1.5223 1.4429 1.1488 -0.1476 -0.0432 -0.1120 71  ARG B CZ  
2579 N NH1 . ARG B 66  ? 1.6873 1.6326 1.2688 -0.1778 -0.0716 -0.0761 71  ARG B NH1 
2580 N NH2 . ARG B 66  ? 1.4645 1.3661 1.1060 -0.1475 -0.0369 -0.1453 71  ARG B NH2 
2581 N N   . HIS B 67  ? 0.8645 0.7962 0.7116 -0.0117 -0.0025 -0.0166 72  HIS B N   
2582 C CA  . HIS B 67  ? 0.7498 0.6827 0.6210 -0.0043 0.0137  -0.0139 72  HIS B CA  
2583 C C   . HIS B 67  ? 0.7237 0.6463 0.6276 0.0150  0.0236  -0.0427 72  HIS B C   
2584 O O   . HIS B 67  ? 0.7186 0.6335 0.6376 0.0269  0.0124  -0.0472 72  HIS B O   
2585 C CB  . HIS B 67  ? 0.7501 0.6875 0.6568 0.0022  0.0052  0.0218  72  HIS B CB  
2586 C CG  . HIS B 67  ? 0.8074 0.7444 0.7431 0.0068  0.0221  0.0260  72  HIS B CG  
2587 N ND1 . HIS B 67  ? 0.8338 0.7794 0.7512 -0.0097 0.0310  0.0402  72  HIS B ND1 
2588 C CD2 . HIS B 67  ? 0.8029 0.7319 0.7825 0.0222  0.0323  0.0173  72  HIS B CD2 
2589 C CE1 . HIS B 67  ? 0.8234 0.7654 0.7800 -0.0014 0.0462  0.0409  72  HIS B CE1 
2590 N NE2 . HIS B 67  ? 0.7873 0.7192 0.7814 0.0173  0.0470  0.0248  72  HIS B NE2 
2591 N N   . SER B 68  ? 0.6957 0.6200 0.6127 0.0156  0.0425  -0.0582 73  SER B N   
2592 C CA  . SER B 68  ? 0.7067 0.6265 0.6630 0.0306  0.0467  -0.0809 73  SER B CA  
2593 C C   . SER B 68  ? 0.6645 0.5803 0.6472 0.0433  0.0331  -0.0735 73  SER B C   
2594 O O   . SER B 68  ? 0.7464 0.6595 0.7497 0.0508  0.0244  -0.0848 73  SER B O   
2595 C CB  . SER B 68  ? 0.7576 0.6842 0.7334 0.0270  0.0695  -0.0943 73  SER B CB  
2596 O OG  . SER B 68  ? 0.8526 0.7846 0.8268 0.0211  0.0761  -0.0739 73  SER B OG  
2597 N N   . ARG B 69  ? 0.6920 0.6079 0.6766 0.0421  0.0329  -0.0538 74  ARG B N   
2598 C CA  . ARG B 69  ? 0.6671 0.5768 0.6704 0.0475  0.0289  -0.0515 74  ARG B CA  
2599 C C   . ARG B 69  ? 0.6543 0.5589 0.6507 0.0483  0.0201  -0.0381 74  ARG B C   
2600 O O   . ARG B 69  ? 0.7116 0.6107 0.7272 0.0489  0.0266  -0.0356 74  ARG B O   
2601 C CB  . ARG B 69  ? 0.6693 0.5793 0.7004 0.0453  0.0443  -0.0455 74  ARG B CB  
2602 C CG  . ARG B 69  ? 0.7166 0.6338 0.7597 0.0422  0.0564  -0.0537 74  ARG B CG  
2603 C CD  . ARG B 69  ? 0.7531 0.6743 0.8054 0.0451  0.0509  -0.0769 74  ARG B CD  
2604 N NE  . ARG B 69  ? 0.8933 0.8238 0.9648 0.0422  0.0655  -0.0857 74  ARG B NE  
2605 C CZ  . ARG B 69  ? 0.8797 0.8177 0.9758 0.0452  0.0643  -0.1028 74  ARG B CZ  
2606 N NH1 . ARG B 69  ? 0.8822 0.8196 0.9870 0.0511  0.0442  -0.1087 74  ARG B NH1 
2607 N NH2 . ARG B 69  ? 0.8864 0.8336 1.0081 0.0414  0.0839  -0.1115 74  ARG B NH2 
2608 N N   . VAL B 70  ? 0.6737 0.5797 0.6475 0.0463  0.0087  -0.0333 75  VAL B N   
2609 C CA  . VAL B 70  ? 0.6497 0.5529 0.6219 0.0464  -0.0013 -0.0214 75  VAL B CA  
2610 C C   . VAL B 70  ? 0.6542 0.5517 0.6070 0.0472  -0.0131 -0.0346 75  VAL B C   
2611 O O   . VAL B 70  ? 0.7166 0.6147 0.6564 0.0445  -0.0136 -0.0465 75  VAL B O   
2612 C CB  . VAL B 70  ? 0.6575 0.5709 0.6295 0.0388  -0.0080 0.0054  75  VAL B CB  
2613 C CG1 . VAL B 70  ? 0.6698 0.5841 0.6495 0.0380  -0.0203 0.0181  75  VAL B CG1 
2614 C CG2 . VAL B 70  ? 0.6804 0.5979 0.6887 0.0393  0.0025  0.0252  75  VAL B CG2 
2615 N N   . VAL B 71  ? 0.6572 0.5478 0.6124 0.0489  -0.0187 -0.0333 76  VAL B N   
2616 C CA  . VAL B 71  ? 0.6975 0.5806 0.6427 0.0493  -0.0311 -0.0399 76  VAL B CA  
2617 C C   . VAL B 71  ? 0.7671 0.6519 0.7003 0.0439  -0.0382 -0.0373 76  VAL B C   
2618 O O   . VAL B 71  ? 0.8054 0.6970 0.7394 0.0389  -0.0417 -0.0213 76  VAL B O   
2619 C CB  . VAL B 71  ? 0.6525 0.5287 0.5968 0.0470  -0.0333 -0.0347 76  VAL B CB  
2620 C CG1 . VAL B 71  ? 0.7718 0.6395 0.7096 0.0457  -0.0475 -0.0332 76  VAL B CG1 
2621 C CG2 . VAL B 71  ? 0.6808 0.5552 0.6228 0.0437  -0.0290 -0.0425 76  VAL B CG2 
2622 N N   . LYS B 72  ? 0.7049 0.5842 0.6337 0.0427  -0.0397 -0.0537 77  LYS B N   
2623 C CA  . LYS B 72  ? 0.7975 0.6759 0.7086 0.0312  -0.0431 -0.0601 77  LYS B CA  
2624 C C   . LYS B 72  ? 0.8390 0.7074 0.7577 0.0314  -0.0553 -0.0566 77  LYS B C   
2625 O O   . LYS B 72  ? 0.8567 0.7145 0.7942 0.0398  -0.0590 -0.0572 77  LYS B O   
2626 C CB  . LYS B 72  ? 0.8809 0.7545 0.7904 0.0265  -0.0294 -0.0875 77  LYS B CB  
2627 C CG  . LYS B 72  ? 0.9011 0.7760 0.7756 0.0045  -0.0255 -0.1009 77  LYS B CG  
2628 C CD  . LYS B 72  ? 0.8942 0.7634 0.7696 -0.0028 -0.0011 -0.1339 77  LYS B CD  
2629 C CE  . LYS B 72  ? 0.9464 0.8159 0.7734 -0.0334 0.0067  -0.1534 77  LYS B CE  
2630 N NZ  . LYS B 72  ? 0.9830 0.8450 0.8100 -0.0454 0.0413  -0.1939 77  LYS B NZ  
2631 N N   . LEU B 73  ? 0.9068 0.7804 0.8122 0.0195  -0.0642 -0.0484 78  LEU B N   
2632 C CA  . LEU B 73  ? 0.8694 0.7334 0.7820 0.0152  -0.0740 -0.0492 78  LEU B CA  
2633 C C   . LEU B 73  ? 0.8159 0.6676 0.7233 0.0064  -0.0681 -0.0781 78  LEU B C   
2634 O O   . LEU B 73  ? 0.8809 0.7391 0.7589 -0.0118 -0.0646 -0.0907 78  LEU B O   
2635 C CB  . LEU B 73  ? 0.8716 0.7496 0.7805 0.0030  -0.0871 -0.0298 78  LEU B CB  
2636 C CG  . LEU B 73  ? 0.8975 0.7677 0.8191 -0.0030 -0.0972 -0.0285 78  LEU B CG  
2637 C CD1 . LEU B 73  ? 0.9705 0.8331 0.9164 0.0095  -0.0933 -0.0150 78  LEU B CD1 
2638 C CD2 . LEU B 73  ? 0.9413 0.8301 0.8608 -0.0208 -0.1139 -0.0128 78  LEU B CD2 
2639 N N   . LEU B 74  ? 0.7882 0.6219 0.7266 0.0162  -0.0658 -0.0877 79  LEU B N   
2640 C CA  . LEU B 74  ? 0.8254 0.6422 0.7814 0.0098  -0.0546 -0.1182 79  LEU B CA  
2641 C C   . LEU B 74  ? 0.8395 0.6477 0.7895 -0.0068 -0.0611 -0.1262 79  LEU B C   
2642 O O   . LEU B 74  ? 0.9483 0.7462 0.8937 -0.0232 -0.0475 -0.1589 79  LEU B O   
2643 C CB  . LEU B 74  ? 0.8109 0.6125 0.8226 0.0273  -0.0534 -0.1181 79  LEU B CB  
2644 C CG  . LEU B 74  ? 0.8373 0.6489 0.8629 0.0407  -0.0498 -0.1123 79  LEU B CG  
2645 C CD1 . LEU B 74  ? 0.8405 0.6409 0.9289 0.0542  -0.0581 -0.1033 79  LEU B CD1 
2646 C CD2 . LEU B 74  ? 0.8844 0.7030 0.8980 0.0342  -0.0264 -0.1394 79  LEU B CD2 
2647 N N   . GLY B 75  ? 0.7810 0.5929 0.7326 -0.0055 -0.0782 -0.1000 80  GLY B N   
2648 C CA  . GLY B 75  ? 0.8441 0.6523 0.7927 -0.0228 -0.0873 -0.1036 80  GLY B CA  
2649 C C   . GLY B 75  ? 0.8086 0.6231 0.7696 -0.0182 -0.1018 -0.0716 80  GLY B C   
2650 O O   . GLY B 75  ? 0.7948 0.6166 0.7592 -0.0043 -0.1017 -0.0497 80  GLY B O   
2651 N N   . VAL B 76  ? 0.8389 0.6497 0.8081 -0.0329 -0.1107 -0.0730 81  VAL B N   
2652 C CA  . VAL B 76  ? 0.8138 0.6317 0.8013 -0.0329 -0.1208 -0.0455 81  VAL B CA  
2653 C C   . VAL B 76  ? 0.8237 0.6204 0.8393 -0.0418 -0.1236 -0.0532 81  VAL B C   
2654 O O   . VAL B 76  ? 0.7702 0.5561 0.7838 -0.0577 -0.1225 -0.0818 81  VAL B O   
2655 C CB  . VAL B 76  ? 0.8400 0.6882 0.8167 -0.0459 -0.1339 -0.0294 81  VAL B CB  
2656 C CG1 . VAL B 76  ? 0.8818 0.7370 0.8367 -0.0744 -0.1472 -0.0474 81  VAL B CG1 
2657 C CG2 . VAL B 76  ? 0.8619 0.7203 0.8729 -0.0430 -0.1371 -0.0014 81  VAL B CG2 
2658 N N   . ILE B 77  ? 0.8179 0.6071 0.8582 -0.0347 -0.1240 -0.0297 82  ILE B N   
2659 C CA  . ILE B 77  ? 0.8686 0.6391 0.9412 -0.0440 -0.1274 -0.0283 82  ILE B CA  
2660 C C   . ILE B 77  ? 0.8975 0.6886 0.9784 -0.0551 -0.1343 -0.0096 82  ILE B C   
2661 O O   . ILE B 77  ? 0.8759 0.6797 0.9580 -0.0478 -0.1282 0.0139  82  ILE B O   
2662 C CB  . ILE B 77  ? 0.8931 0.6410 0.9896 -0.0326 -0.1241 -0.0087 82  ILE B CB  
2663 C CG1 . ILE B 77  ? 0.9545 0.6874 1.0603 -0.0194 -0.1204 -0.0209 82  ILE B CG1 
2664 C CG2 . ILE B 77  ? 0.8893 0.6160 1.0252 -0.0435 -0.1273 -0.0042 82  ILE B CG2 
2665 C CD1 . ILE B 77  ? 1.0052 0.7256 1.1293 -0.0097 -0.1258 0.0094  82  ILE B CD1 
2666 N N   . ILE B 78  ? 0.9416 0.7374 1.0314 -0.0754 -0.1452 -0.0227 83  ILE B N   
2667 C CA  . ILE B 78  ? 0.9402 0.7568 1.0548 -0.0888 -0.1554 -0.0047 83  ILE B CA  
2668 C C   . ILE B 78  ? 0.9402 0.7333 1.0849 -0.1027 -0.1571 -0.0149 83  ILE B C   
2669 O O   . ILE B 78  ? 0.9790 0.7632 1.1181 -0.1213 -0.1638 -0.0443 83  ILE B O   
2670 C CB  . ILE B 78  ? 1.0381 0.8876 1.1374 -0.1060 -0.1750 -0.0062 83  ILE B CB  
2671 C CG1 . ILE B 78  ? 0.9832 0.8537 1.0656 -0.0908 -0.1720 0.0096  83  ILE B CG1 
2672 C CG2 . ILE B 78  ? 1.1539 1.0278 1.2957 -0.1226 -0.1911 0.0142  83  ILE B CG2 
2673 C CD1 . ILE B 78  ? 0.9470 0.8483 1.0100 -0.1070 -0.1933 0.0152  83  ILE B CD1 
2674 N N   . GLU B 79  ? 0.9464 0.7275 1.1204 -0.0966 -0.1479 0.0078  84  GLU B N   
2675 C CA  . GLU B 79  ? 1.0046 0.7610 1.2164 -0.1083 -0.1477 0.0062  84  GLU B CA  
2676 C C   . GLU B 79  ? 1.0627 0.8332 1.3079 -0.1166 -0.1452 0.0334  84  GLU B C   
2677 O O   . GLU B 79  ? 1.0785 0.8761 1.3228 -0.1115 -0.1396 0.0519  84  GLU B O   
2678 C CB  . GLU B 79  ? 1.0174 0.7385 1.2378 -0.0945 -0.1380 0.0113  84  GLU B CB  
2679 C CG  . GLU B 79  ? 1.0600 0.7642 1.2724 -0.0894 -0.1364 -0.0220 84  GLU B CG  
2680 C CD  . GLU B 79  ? 1.0373 0.7086 1.2819 -0.0754 -0.1306 -0.0138 84  GLU B CD  
2681 O OE1 . GLU B 79  ? 1.0316 0.6989 1.2803 -0.0673 -0.1321 0.0244  84  GLU B OE1 
2682 O OE2 . GLU B 79  ? 1.0718 0.7221 1.3397 -0.0753 -0.1240 -0.0455 84  GLU B OE2 
2683 N N   . GLU B 80  ? 1.0499 0.8009 1.3332 -0.1305 -0.1460 0.0336  85  GLU B N   
2684 C CA  . GLU B 80  ? 1.0262 0.7858 1.3481 -0.1404 -0.1390 0.0592  85  GLU B CA  
2685 C C   . GLU B 80  ? 0.9673 0.7206 1.2729 -0.1283 -0.1178 0.0891  85  GLU B C   
2686 O O   . GLU B 80  ? 1.0022 0.7257 1.3045 -0.1264 -0.1128 0.1026  85  GLU B O   
2687 C CB  . GLU B 80  ? 1.0913 0.8258 1.4578 -0.1584 -0.1427 0.0532  85  GLU B CB  
2688 C CG  . GLU B 80  ? 1.0832 0.8283 1.4626 -0.1809 -0.1628 0.0211  85  GLU B CG  
2689 C CD  . GLU B 80  ? 1.1159 0.8384 1.5469 -0.2024 -0.1642 0.0136  85  GLU B CD  
2690 O OE1 . GLU B 80  ? 1.1331 0.8151 1.5843 -0.1971 -0.1527 0.0150  85  GLU B OE1 
2691 O OE2 . GLU B 80  ? 1.1247 0.8706 1.5831 -0.2258 -0.1789 0.0086  85  GLU B OE2 
2692 N N   . GLY B 81  ? 0.9205 0.7023 1.2143 -0.1223 -0.1062 0.0986  86  GLY B N   
2693 C CA  . GLY B 81  ? 0.9249 0.7054 1.1973 -0.1194 -0.0803 0.1200  86  GLY B CA  
2694 C C   . GLY B 81  ? 0.9151 0.6918 1.1322 -0.1044 -0.0756 0.1181  86  GLY B C   
2695 O O   . GLY B 81  ? 0.8805 0.6643 1.0761 -0.1064 -0.0524 0.1283  86  GLY B O   
2696 N N   . LYS B 82  ? 0.9123 0.6775 1.1091 -0.0926 -0.0942 0.1024  87  LYS B N   
2697 C CA  . LYS B 82  ? 0.8987 0.6609 1.0504 -0.0786 -0.0934 0.1001  87  LYS B CA  
2698 C C   . LYS B 82  ? 0.7837 0.5668 0.9268 -0.0678 -0.1004 0.0782  87  LYS B C   
2699 O O   . LYS B 82  ? 0.7546 0.5399 0.9115 -0.0707 -0.1159 0.0601  87  LYS B O   
2700 C CB  . LYS B 82  ? 0.9924 0.7251 1.1407 -0.0735 -0.1072 0.1035  87  LYS B CB  
2701 C CG  . LYS B 82  ? 1.0684 0.8001 1.1773 -0.0625 -0.1086 0.1087  87  LYS B CG  
2702 C CD  . LYS B 82  ? 1.1602 0.8664 1.2882 -0.0564 -0.1252 0.1172  87  LYS B CD  
2703 C CE  . LYS B 82  ? 1.1425 0.8537 1.2427 -0.0446 -0.1312 0.1180  87  LYS B CE  
2704 N NZ  . LYS B 82  ? 1.1457 0.8357 1.2860 -0.0369 -0.1483 0.1284  87  LYS B NZ  
2705 N N   . TYR B 83  ? 0.7129 0.5103 0.8307 -0.0596 -0.0878 0.0798  88  TYR B N   
2706 C CA  . TYR B 83  ? 0.7431 0.5597 0.8521 -0.0494 -0.0932 0.0657  88  TYR B CA  
2707 C C   . TYR B 83  ? 0.6996 0.5106 0.7688 -0.0379 -0.0863 0.0627  88  TYR B C   
2708 O O   . TYR B 83  ? 0.6739 0.4843 0.7261 -0.0408 -0.0682 0.0721  88  TYR B O   
2709 C CB  . TYR B 83  ? 0.7498 0.5953 0.8926 -0.0519 -0.0841 0.0731  88  TYR B CB  
2710 C CG  . TYR B 83  ? 0.7449 0.6033 0.9349 -0.0650 -0.0970 0.0784  88  TYR B CG  
2711 C CD1 . TYR B 83  ? 0.7880 0.6407 1.0082 -0.0761 -0.0847 0.0899  88  TYR B CD1 
2712 C CD2 . TYR B 83  ? 0.7559 0.6341 0.9579 -0.0710 -0.1227 0.0737  88  TYR B CD2 
2713 C CE1 . TYR B 83  ? 0.8190 0.6850 1.0888 -0.0899 -0.0978 0.0948  88  TYR B CE1 
2714 C CE2 . TYR B 83  ? 0.8088 0.7020 1.0533 -0.0882 -0.1396 0.0797  88  TYR B CE2 
2715 C CZ  . TYR B 83  ? 0.8178 0.7050 1.1008 -0.0961 -0.1271 0.0895  88  TYR B CZ  
2716 O OH  . TYR B 83  ? 0.9296 0.8332 1.2610 -0.1143 -0.1447 0.0955  88  TYR B OH  
2717 N N   . SER B 84  ? 0.6487 0.4560 0.7028 -0.0288 -0.0988 0.0474  89  SER B N   
2718 C CA  . SER B 84  ? 0.6729 0.4747 0.6978 -0.0184 -0.0964 0.0442  89  SER B CA  
2719 C C   . SER B 84  ? 0.6895 0.5026 0.7052 -0.0099 -0.1006 0.0265  89  SER B C   
2720 O O   . SER B 84  ? 0.6780 0.4943 0.7002 -0.0146 -0.1101 0.0132  89  SER B O   
2721 C CB  . SER B 84  ? 0.7077 0.4857 0.7349 -0.0170 -0.1068 0.0492  89  SER B CB  
2722 O OG  . SER B 84  ? 0.7519 0.5184 0.7825 -0.0285 -0.1055 0.0725  89  SER B OG  
2723 N N   . LEU B 85  ? 0.7066 0.5258 0.7024 -0.0019 -0.0925 0.0260  90  LEU B N   
2724 C CA  . LEU B 85  ? 0.6666 0.4940 0.6508 0.0060  -0.0938 0.0121  90  LEU B CA  
2725 C C   . LEU B 85  ? 0.7049 0.5186 0.6822 0.0134  -0.0971 0.0064  90  LEU B C   
2726 O O   . LEU B 85  ? 0.7475 0.5538 0.7182 0.0120  -0.0978 0.0200  90  LEU B O   
2727 C CB  . LEU B 85  ? 0.6571 0.5013 0.6381 0.0095  -0.0809 0.0173  90  LEU B CB  
2728 C CG  . LEU B 85  ? 0.6956 0.5573 0.7055 0.0043  -0.0775 0.0289  90  LEU B CG  
2729 C CD1 . LEU B 85  ? 0.6737 0.5460 0.6964 0.0095  -0.0583 0.0330  90  LEU B CD1 
2730 C CD2 . LEU B 85  ? 0.7095 0.5843 0.7242 -0.0018 -0.0963 0.0281  90  LEU B CD2 
2731 N N   . VAL B 86  ? 0.6683 0.4800 0.6486 0.0177  -0.0991 -0.0123 91  VAL B N   
2732 C CA  . VAL B 86  ? 0.7040 0.5046 0.6986 0.0260  -0.1013 -0.0190 91  VAL B CA  
2733 C C   . VAL B 86  ? 0.6857 0.4991 0.6670 0.0320  -0.0929 -0.0321 91  VAL B C   
2734 O O   . VAL B 86  ? 0.7450 0.5658 0.7143 0.0274  -0.0866 -0.0478 91  VAL B O   
2735 C CB  . VAL B 86  ? 0.8252 0.6081 0.8513 0.0238  -0.1024 -0.0358 91  VAL B CB  
2736 C CG1 . VAL B 86  ? 0.9416 0.7146 1.0045 0.0342  -0.1013 -0.0434 91  VAL B CG1 
2737 C CG2 . VAL B 86  ? 0.8237 0.5922 0.8693 0.0171  -0.1109 -0.0201 91  VAL B CG2 
2738 N N   . MET B 87  ? 0.7270 0.5434 0.7086 0.0384  -0.0943 -0.0244 92  MET B N   
2739 C CA  . MET B 87  ? 0.7969 0.6255 0.7702 0.0437  -0.0857 -0.0341 92  MET B CA  
2740 C C   . MET B 87  ? 0.7912 0.6171 0.7927 0.0507  -0.0921 -0.0342 92  MET B C   
2741 O O   . MET B 87  ? 0.8559 0.6719 0.8833 0.0510  -0.1066 -0.0205 92  MET B O   
2742 C CB  . MET B 87  ? 0.7942 0.6343 0.7432 0.0408  -0.0791 -0.0241 92  MET B CB  
2743 C CG  . MET B 87  ? 0.9633 0.8006 0.9013 0.0349  -0.0839 -0.0100 92  MET B CG  
2744 S SD  . MET B 87  ? 1.1010 0.9418 1.0201 0.0243  -0.0674 -0.0028 92  MET B SD  
2745 C CE  . MET B 87  ? 1.1638 1.0044 1.0535 0.0109  -0.0657 -0.0012 92  MET B CE  
2746 N N   . GLU B 88  ? 0.8058 0.6420 0.8096 0.0553  -0.0830 -0.0460 93  GLU B N   
2747 C CA  . GLU B 88  ? 0.8101 0.6480 0.8552 0.0623  -0.0883 -0.0479 93  GLU B CA  
2748 C C   . GLU B 88  ? 0.7360 0.5807 0.7772 0.0579  -0.1080 -0.0248 93  GLU B C   
2749 O O   . GLU B 88  ? 0.8273 0.6770 0.8253 0.0488  -0.1064 -0.0184 93  GLU B O   
2750 C CB  . GLU B 88  ? 0.9454 0.7922 0.9993 0.0661  -0.0685 -0.0706 93  GLU B CB  
2751 C CG  . GLU B 88  ? 1.0529 0.9134 1.0719 0.0632  -0.0597 -0.0699 93  GLU B CG  
2752 C CD  . GLU B 88  ? 1.0547 0.9206 1.0633 0.0606  -0.0376 -0.0889 93  GLU B CD  
2753 O OE1 . GLU B 88  ? 0.9892 0.8534 1.0277 0.0623  -0.0246 -0.1083 93  GLU B OE1 
2754 O OE2 . GLU B 88  ? 1.0479 0.9202 1.0222 0.0547  -0.0322 -0.0830 93  GLU B OE2 
2755 N N   . TYR B 89  ? 0.6838 0.5287 0.7751 0.0613  -0.1263 -0.0125 94  TYR B N   
2756 C CA  . TYR B 89  ? 0.6915 0.5460 0.7816 0.0509  -0.1539 0.0147  94  TYR B CA  
2757 C C   . TYR B 89  ? 0.7442 0.6161 0.8240 0.0478  -0.1501 0.0051  94  TYR B C   
2758 O O   . TYR B 89  ? 0.7759 0.6536 0.8934 0.0594  -0.1357 -0.0136 94  TYR B O   
2759 C CB  . TYR B 89  ? 0.6763 0.5287 0.8443 0.0566  -0.1786 0.0363  94  TYR B CB  
2760 C CG  . TYR B 89  ? 0.6935 0.5598 0.8660 0.0411  -0.2176 0.0741  94  TYR B CG  
2761 C CD1 . TYR B 89  ? 0.7112 0.5751 0.8229 0.0187  -0.2365 0.1012  94  TYR B CD1 
2762 C CD2 . TYR B 89  ? 0.7027 0.5868 0.9396 0.0445  -0.2363 0.0840  94  TYR B CD2 
2763 C CE1 . TYR B 89  ? 0.7558 0.6342 0.8574 -0.0044 -0.2759 0.1389  94  TYR B CE1 
2764 C CE2 . TYR B 89  ? 0.7377 0.6390 0.9758 0.0242  -0.2801 0.1241  94  TYR B CE2 
2765 C CZ  . TYR B 89  ? 0.7760 0.6742 0.9402 -0.0024 -0.3014 0.1524  94  TYR B CZ  
2766 O OH  . TYR B 89  ? 0.7801 0.6972 0.9317 -0.0308 -0.3476 0.1942  94  TYR B OH  
2767 N N   . MET B 90  ? 0.7923 0.6714 0.8210 0.0288  -0.1598 0.0153  95  MET B N   
2768 C CA  . MET B 90  ? 0.7304 0.6245 0.7465 0.0200  -0.1582 0.0058  95  MET B CA  
2769 C C   . MET B 90  ? 0.7564 0.6619 0.7595 -0.0042 -0.1948 0.0329  95  MET B C   
2770 O O   . MET B 90  ? 0.8973 0.7987 0.8379 -0.0277 -0.1994 0.0420  95  MET B O   
2771 C CB  . MET B 90  ? 0.6923 0.5820 0.6544 0.0137  -0.1282 -0.0146 95  MET B CB  
2772 C CG  . MET B 90  ? 0.7203 0.6024 0.6909 0.0319  -0.1005 -0.0310 95  MET B CG  
2773 S SD  . MET B 90  ? 0.7554 0.6456 0.7745 0.0488  -0.0874 -0.0478 95  MET B SD  
2774 C CE  . MET B 90  ? 0.7283 0.6293 0.7361 0.0402  -0.0753 -0.0585 95  MET B CE  
2775 N N   . GLU B 91  ? 0.8755 0.5566 0.6252 0.1887  0.0716  0.1126  96  GLU B N   
2776 C CA  . GLU B 91  ? 0.9301 0.6073 0.6497 0.2293  0.0717  0.1263  96  GLU B CA  
2777 C C   . GLU B 91  ? 0.9218 0.6419 0.6527 0.2314  0.0511  0.1260  96  GLU B C   
2778 O O   . GLU B 91  ? 0.9932 0.6783 0.6817 0.2503  0.0580  0.1370  96  GLU B O   
2779 C CB  . GLU B 91  ? 0.9599 0.6659 0.6831 0.2686  0.0693  0.1314  96  GLU B CB  
2780 C CG  . GLU B 91  ? 1.0402 0.7399 0.7258 0.3189  0.0680  0.1469  96  GLU B CG  
2781 C CD  . GLU B 91  ? 1.1127 0.8128 0.7869 0.3633  0.0773  0.1557  96  GLU B CD  
2782 O OE1 . GLU B 91  ? 1.2451 0.9124 0.8704 0.4090  0.0845  0.1716  96  GLU B OE1 
2783 O OE2 . GLU B 91  ? 1.0314 0.7615 0.7412 0.3567  0.0797  0.1481  96  GLU B OE2 
2784 N N   . LYS B 92  ? 0.8861 0.6728 0.6671 0.2118  0.0286  0.1133  97  LYS B N   
2785 C CA  . LYS B 92  ? 0.8598 0.6874 0.6509 0.2118  0.0069  0.1088  97  LYS B CA  
2786 C C   . LYS B 92  ? 0.8942 0.6955 0.6776 0.1836  0.0121  0.1063  97  LYS B C   
2787 O O   . LYS B 92  ? 1.0382 0.8618 0.8201 0.1844  -0.0024 0.1024  97  LYS B O   
2788 C CB  . LYS B 92  ? 0.8376 0.7436 0.6841 0.2029  -0.0167 0.0950  97  LYS B CB  
2789 C CG  . LYS B 92  ? 0.9606 0.9090 0.8222 0.2365  -0.0236 0.0977  97  LYS B CG  
2790 C CD  . LYS B 92  ? 0.8920 0.9253 0.8147 0.2266  -0.0459 0.0829  97  LYS B CD  
2791 C CE  . LYS B 92  ? 0.8582 0.9432 0.7966 0.2681  -0.0556 0.0867  97  LYS B CE  
2792 N NZ  . LYS B 92  ? 0.8994 0.9967 0.8057 0.3038  -0.0768 0.0907  97  LYS B NZ  
2793 N N   . GLY B 93  ? 0.8398 0.5962 0.6190 0.1595  0.0324  0.1071  98  GLY B N   
2794 C CA  . GLY B 93  ? 0.8246 0.5586 0.6012 0.1362  0.0417  0.1064  98  GLY B CA  
2795 C C   . GLY B 93  ? 0.7588 0.5360 0.5795 0.1084  0.0261  0.0933  98  GLY B C   
2796 O O   . GLY B 93  ? 0.7913 0.5991 0.6412 0.0996  0.0152  0.0854  98  GLY B O   
2797 N N   . ASN B 94  ? 0.8010 0.5758 0.6220 0.0973  0.0284  0.0924  99  ASN B N   
2798 C CA  . ASN B 94  ? 0.7280 0.5348 0.5842 0.0746  0.0169  0.0816  99  ASN B CA  
2799 C C   . ASN B 94  ? 0.7444 0.5916 0.6099 0.0813  -0.0052 0.0735  99  ASN B C   
2800 O O   . ASN B 94  ? 0.7108 0.5676 0.5566 0.1042  -0.0145 0.0753  99  ASN B O   
2801 C CB  . ASN B 94  ? 0.7525 0.5428 0.6099 0.0614  0.0309  0.0835  99  ASN B CB  
2802 C CG  . ASN B 94  ? 0.8128 0.5925 0.6380 0.0783  0.0344  0.0883  99  ASN B CG  
2803 O OD1 . ASN B 94  ? 0.8587 0.6615 0.6786 0.0868  0.0162  0.0817  99  ASN B OD1 
2804 N ND2 . ASN B 94  ? 0.8822 0.6241 0.6841 0.0814  0.0594  0.0985  99  ASN B ND2 
2805 N N   . LEU B 95  ? 0.7073 0.5767 0.6016 0.0615  -0.0136 0.0640  100 LEU B N   
2806 C CA  . LEU B 95  ? 0.6793 0.5829 0.5879 0.0590  -0.0317 0.0530  100 LEU B CA  
2807 C C   . LEU B 95  ? 0.7761 0.6812 0.6588 0.0714  -0.0413 0.0493  100 LEU B C   
2808 O O   . LEU B 95  ? 0.7892 0.7243 0.6746 0.0789  -0.0594 0.0408  100 LEU B O   
2809 C CB  . LEU B 95  ? 0.6615 0.5716 0.5950 0.0363  -0.0327 0.0458  100 LEU B CB  
2810 C CG  . LEU B 95  ? 0.6776 0.6117 0.6257 0.0262  -0.0455 0.0332  100 LEU B CG  
2811 C CD1 . LEU B 95  ? 0.6753 0.6439 0.6441 0.0290  -0.0540 0.0286  100 LEU B CD1 
2812 C CD2 . LEU B 95  ? 0.6240 0.5485 0.5852 0.0081  -0.0404 0.0302  100 LEU B CD2 
2813 N N   . MET B 96  ? 0.8142 0.6894 0.6723 0.0737  -0.0292 0.0544  101 MET B N   
2814 C CA  . MET B 96  ? 0.8155 0.6816 0.6364 0.0881  -0.0354 0.0511  101 MET B CA  
2815 C C   . MET B 96  ? 0.8637 0.7266 0.6477 0.1174  -0.0425 0.0571  101 MET B C   
2816 O O   . MET B 96  ? 0.8971 0.7750 0.6596 0.1299  -0.0628 0.0479  101 MET B O   
2817 C CB  . MET B 96  ? 0.8451 0.6773 0.6473 0.0865  -0.0143 0.0574  101 MET B CB  
2818 C CG  . MET B 96  ? 0.9067 0.7228 0.6656 0.0993  -0.0180 0.0520  101 MET B CG  
2819 S SD  . MET B 96  ? 0.9471 0.7877 0.7122 0.0871  -0.0457 0.0286  101 MET B SD  
2820 C CE  . MET B 96  ? 0.9378 0.7761 0.7440 0.0622  -0.0318 0.0273  101 MET B CE  
2821 N N   . HIS B 97  ? 0.9402 0.7808 0.7134 0.1294  -0.0265 0.0718  102 HIS B N   
2822 C CA  . HIS B 97  ? 0.8850 0.7187 0.6216 0.1627  -0.0313 0.0807  102 HIS B CA  
2823 C C   . HIS B 97  ? 0.8424 0.7327 0.6051 0.1716  -0.0607 0.0698  102 HIS B C   
2824 O O   . HIS B 97  ? 0.9326 0.8385 0.6675 0.1992  -0.0796 0.0682  102 HIS B O   
2825 C CB  . HIS B 97  ? 0.9408 0.7340 0.6659 0.1687  -0.0051 0.0969  102 HIS B CB  
2826 C CG  . HIS B 97  ? 1.0477 0.8170 0.7233 0.2079  -0.0027 0.1103  102 HIS B CG  
2827 N ND1 . HIS B 97  ? 1.0961 0.8835 0.7810 0.2261  -0.0103 0.1131  102 HIS B ND1 
2828 C CD2 . HIS B 97  ? 1.0923 0.8162 0.7037 0.2362  0.0093  0.1235  102 HIS B CD2 
2829 C CE1 . HIS B 97  ? 1.1838 0.9398 0.8129 0.2660  -0.0054 0.1275  102 HIS B CE1 
2830 N NE2 . HIS B 97  ? 1.1965 0.9109 0.7773 0.2726  0.0065  0.1344  102 HIS B NE2 
2831 N N   . VAL B 98  ? 0.8242 0.7467 0.6401 0.1488  -0.0639 0.0619  103 VAL B N   
2832 C CA  . VAL B 98  ? 0.8334 0.8161 0.6881 0.1504  -0.0861 0.0505  103 VAL B CA  
2833 C C   . VAL B 98  ? 0.8815 0.9010 0.7471 0.1391  -0.1118 0.0307  103 VAL B C   
2834 O O   . VAL B 98  ? 0.9350 1.0016 0.8097 0.1542  -0.1364 0.0214  103 VAL B O   
2835 C CB  . VAL B 98  ? 0.8205 0.8171 0.7223 0.1283  -0.0753 0.0492  103 VAL B CB  
2836 C CG1 . VAL B 98  ? 0.8680 0.9289 0.8189 0.1229  -0.0920 0.0363  103 VAL B CG1 
2837 C CG2 . VAL B 98  ? 0.8674 0.8287 0.7523 0.1433  -0.0544 0.0651  103 VAL B CG2 
2838 N N   . LEU B 99  ? 0.8389 0.8374 0.7036 0.1136  -0.1064 0.0232  104 LEU B N   
2839 C CA  . LEU B 99  ? 0.8265 0.8437 0.6921 0.0996  -0.1269 0.0026  104 LEU B CA  
2840 C C   . LEU B 99  ? 0.9004 0.9091 0.7114 0.1254  -0.1445 -0.0014 104 LEU B C   
2841 O O   . LEU B 99  ? 0.9801 1.0260 0.7957 0.1237  -0.1729 -0.0210 104 LEU B O   
2842 C CB  . LEU B 99  ? 0.8305 0.8145 0.6976 0.0725  -0.1119 -0.0013 104 LEU B CB  
2843 C CG  . LEU B 99  ? 0.8247 0.8140 0.7369 0.0470  -0.0985 -0.0004 104 LEU B CG  
2844 C CD1 . LEU B 99  ? 0.8079 0.7566 0.7090 0.0333  -0.0817 0.0022  104 LEU B CD1 
2845 C CD2 . LEU B 99  ? 0.8390 0.8728 0.7940 0.0269  -0.1125 -0.0176 104 LEU B CD2 
2846 N N   . LYS B 100 ? 0.9717 0.9297 0.7295 0.1479  -0.1267 0.0162  105 LYS B N   
2847 C CA  . LYS B 100 ? 1.0372 0.9750 0.7282 0.1798  -0.1382 0.0174  105 LYS B CA  
2848 C C   . LYS B 100 ? 1.1227 1.0888 0.7969 0.2177  -0.1581 0.0230  105 LYS B C   
2849 O O   . LYS B 100 ? 1.2912 1.2469 0.9071 0.2472  -0.1746 0.0215  105 LYS B O   
2850 C CB  . LYS B 100 ? 1.0887 0.9565 0.7265 0.1903  -0.1048 0.0360  105 LYS B CB  
2851 C CG  . LYS B 100 ? 1.0393 0.8799 0.6692 0.1687  -0.0931 0.0275  105 LYS B CG  
2852 C CD  . LYS B 100 ? 1.0323 0.8148 0.6256 0.1784  -0.0549 0.0480  105 LYS B CD  
2853 C CE  . LYS B 100 ? 1.0291 0.7884 0.6190 0.1618  -0.0397 0.0416  105 LYS B CE  
2854 N NZ  . LYS B 100 ? 1.0377 0.7562 0.6175 0.1643  0.0012  0.0611  105 LYS B NZ  
2855 N N   . ALA B 101 ? 1.1698 1.1682 0.8885 0.2211  -0.1562 0.0300  106 ALA B N   
2856 C CA  . ALA B 101 ? 1.2369 1.2676 0.9456 0.2618  -0.1742 0.0365  106 ALA B CA  
2857 C C   . ALA B 101 ? 1.3720 1.4762 1.0994 0.2689  -0.2197 0.0127  106 ALA B C   
2858 O O   . ALA B 101 ? 1.3379 1.4804 1.1119 0.2321  -0.2346 -0.0109 106 ALA B O   
2859 C CB  . ALA B 101 ? 1.1881 1.2370 0.9443 0.2617  -0.1589 0.0472  106 ALA B CB  
2860 N N   . GLU B 102 ? 1.5721 1.6935 1.2616 0.3168  -0.2409 0.0188  107 GLU B N   
2861 C CA  . GLU B 102 ? 1.6401 1.8383 1.3422 0.3314  -0.2906 -0.0045 107 GLU B CA  
2862 C C   . GLU B 102 ? 1.6726 1.9681 1.4783 0.3053  -0.3095 -0.0244 107 GLU B C   
2863 O O   . GLU B 102 ? 1.8222 2.1800 1.6620 0.2860  -0.3450 -0.0540 107 GLU B O   
2864 C CB  . GLU B 102 ? 1.6963 1.8924 1.3341 0.3968  -0.3078 0.0109  107 GLU B CB  
2865 C CG  . GLU B 102 ? 1.8597 1.9715 1.3889 0.4236  -0.2993 0.0229  107 GLU B CG  
2866 C CD  . GLU B 102 ? 1.9463 2.0557 1.4029 0.4920  -0.3207 0.0367  107 GLU B CD  
2867 O OE1 . GLU B 102 ? 1.9494 2.0648 1.4122 0.5267  -0.3104 0.0574  107 GLU B OE1 
2868 O OE2 . GLU B 102 ? 2.0156 2.1116 1.4018 0.5141  -0.3471 0.0273  107 GLU B OE2 
2869 N N   . MET B 103 ? 1.6382 1.9442 1.4914 0.3042  -0.2842 -0.0094 108 MET B N   
2870 C CA  . MET B 103 ? 1.5211 1.9055 1.4732 0.2739  -0.2878 -0.0243 108 MET B CA  
2871 C C   . MET B 103 ? 1.4435 1.8056 1.4277 0.2137  -0.2704 -0.0379 108 MET B C   
2872 O O   . MET B 103 ? 1.3281 1.6199 1.2891 0.1995  -0.2361 -0.0224 108 MET B O   
2873 C CB  . MET B 103 ? 1.5051 1.8912 1.4822 0.2955  -0.2604 -0.0017 108 MET B CB  
2874 C CG  . MET B 103 ? 1.4313 1.9061 1.5061 0.2787  -0.2631 -0.0137 108 MET B CG  
2875 S SD  . MET B 103 ? 1.4718 1.9066 1.5753 0.2597  -0.2125 0.0045  108 MET B SD  
2876 C CE  . MET B 103 ? 1.5202 1.8846 1.5472 0.3180  -0.1919 0.0371  108 MET B CE  
2877 N N   . SER B 104 ? 1.3730 1.7941 1.4085 0.1796  -0.2947 -0.0676 109 SER B N   
2878 C CA  . SER B 104 ? 1.1941 1.5927 1.2570 0.1244  -0.2790 -0.0820 109 SER B CA  
2879 C C   . SER B 104 ? 1.0865 1.5044 1.2163 0.1017  -0.2498 -0.0748 109 SER B C   
2880 O O   . SER B 104 ? 1.0401 1.5344 1.2342 0.1059  -0.2574 -0.0803 109 SER B O   
2881 C CB  . SER B 104 ? 1.1248 1.5711 1.2144 0.0939  -0.3125 -0.1178 109 SER B CB  
2882 O OG  . SER B 104 ? 1.1281 1.6775 1.2891 0.0969  -0.3396 -0.1342 109 SER B OG  
2883 N N   . THR B 105 ? 0.9712 1.3209 1.0836 0.0808  -0.2164 -0.0623 110 THR B N   
2884 C CA  . THR B 105 ? 0.8453 1.1944 1.0014 0.0625  -0.1858 -0.0529 110 THR B CA  
2885 C C   . THR B 105 ? 0.7798 1.1628 0.9943 0.0156  -0.1848 -0.0754 110 THR B C   
2886 O O   . THR B 105 ? 0.8079 1.1560 1.0022 -0.0116 -0.1874 -0.0886 110 THR B O   
2887 C CB  . THR B 105 ? 0.9218 1.1860 1.0326 0.0587  -0.1554 -0.0333 110 THR B CB  
2888 O OG1 . THR B 105 ? 0.8957 1.1183 0.9469 0.0934  -0.1554 -0.0166 110 THR B OG1 
2889 C CG2 . THR B 105 ? 0.9818 1.2417 1.1218 0.0525  -0.1272 -0.0208 110 THR B CG2 
2890 N N   . PRO B 106 ? 0.7595 1.2060 1.0445 0.0061  -0.1774 -0.0798 111 PRO B N   
2891 C CA  . PRO B 106 ? 0.7780 1.2570 1.1215 -0.0418 -0.1733 -0.1026 111 PRO B CA  
2892 C C   . PRO B 106 ? 0.8130 1.2185 1.1386 -0.0753 -0.1396 -0.0972 111 PRO B C   
2893 O O   . PRO B 106 ? 0.7730 1.1187 1.0578 -0.0612 -0.1175 -0.0746 111 PRO B O   
2894 C CB  . PRO B 106 ? 0.7324 1.2961 1.1548 -0.0372 -0.1667 -0.1033 111 PRO B CB  
2895 C CG  . PRO B 106 ? 0.7201 1.2603 1.1132 0.0060  -0.1504 -0.0747 111 PRO B CG  
2896 C CD  . PRO B 106 ? 0.7701 1.2567 1.0841 0.0375  -0.1676 -0.0642 111 PRO B CD  
2897 N N   . LEU B 107 ? 0.7890 1.1981 1.1424 -0.1188 -0.1376 -0.1190 112 LEU B N   
2898 C CA  . LEU B 107 ? 0.7709 1.1072 1.1039 -0.1501 -0.1059 -0.1155 112 LEU B CA  
2899 C C   . LEU B 107 ? 0.7286 1.0443 1.0715 -0.1473 -0.0682 -0.0934 112 LEU B C   
2900 O O   . LEU B 107 ? 0.6170 0.8591 0.9137 -0.1480 -0.0468 -0.0785 112 LEU B O   
2901 C CB  . LEU B 107 ? 0.8500 1.2014 1.2214 -0.1989 -0.1064 -0.1446 112 LEU B CB  
2902 C CG  . LEU B 107 ? 0.9241 1.2061 1.2840 -0.2357 -0.0702 -0.1443 112 LEU B CG  
2903 C CD1 . LEU B 107 ? 0.9135 1.1015 1.1921 -0.2220 -0.0631 -0.1300 112 LEU B CD1 
2904 C CD2 . LEU B 107 ? 0.9456 1.2469 1.3443 -0.2846 -0.0752 -0.1776 112 LEU B CD2 
2905 N N   . SER B 108 ? 0.7199 1.1027 1.1223 -0.1426 -0.0609 -0.0923 113 SER B N   
2906 C CA  . SER B 108 ? 0.7021 1.0706 1.1126 -0.1359 -0.0249 -0.0726 113 SER B CA  
2907 C C   . SER B 108 ? 0.6882 1.0030 1.0365 -0.0986 -0.0206 -0.0479 113 SER B C   
2908 O O   . SER B 108 ? 0.7242 0.9813 1.0406 -0.1004 0.0058  -0.0334 113 SER B O   
2909 C CB  . SER B 108 ? 0.7538 1.2135 1.2417 -0.1308 -0.0199 -0.0768 113 SER B CB  
2910 O OG  . SER B 108 ? 0.8458 1.3634 1.3435 -0.0945 -0.0525 -0.0779 113 SER B OG  
2911 N N   . VAL B 109 ? 0.6624 0.9933 0.9907 -0.0658 -0.0465 -0.0442 114 VAL B N   
2912 C CA  . VAL B 109 ? 0.6460 0.9228 0.9151 -0.0351 -0.0436 -0.0240 114 VAL B CA  
2913 C C   . VAL B 109 ? 0.6571 0.8615 0.8718 -0.0460 -0.0432 -0.0211 114 VAL B C   
2914 O O   . VAL B 109 ? 0.7700 0.9224 0.9486 -0.0391 -0.0278 -0.0065 114 VAL B O   
2915 C CB  . VAL B 109 ? 0.7093 1.0160 0.9679 0.0029  -0.0670 -0.0201 114 VAL B CB  
2916 C CG1 . VAL B 109 ? 0.7369 0.9788 0.9318 0.0277  -0.0622 -0.0017 114 VAL B CG1 
2917 C CG2 . VAL B 109 ? 0.7100 1.0836 1.0185 0.0228  -0.0627 -0.0181 114 VAL B CG2 
2918 N N   . LYS B 110 ? 0.6524 0.8550 0.8609 -0.0612 -0.0608 -0.0357 115 LYS B N   
2919 C CA  . LYS B 110 ? 0.6921 0.8295 0.8531 -0.0699 -0.0581 -0.0337 115 LYS B CA  
2920 C C   . LYS B 110 ? 0.6662 0.7586 0.8201 -0.0898 -0.0316 -0.0280 115 LYS B C   
2921 O O   . LYS B 110 ? 0.6919 0.7336 0.8061 -0.0817 -0.0243 -0.0160 115 LYS B O   
2922 C CB  . LYS B 110 ? 0.6989 0.8397 0.8527 -0.0834 -0.0786 -0.0531 115 LYS B CB  
2923 C CG  . LYS B 110 ? 0.7301 0.8924 0.8640 -0.0564 -0.1049 -0.0549 115 LYS B CG  
2924 C CD  . LYS B 110 ? 0.7728 0.9363 0.8927 -0.0691 -0.1265 -0.0766 115 LYS B CD  
2925 C CE  . LYS B 110 ? 0.7496 0.9129 0.8276 -0.0370 -0.1480 -0.0738 115 LYS B CE  
2926 N NZ  . LYS B 110 ? 0.8132 0.9670 0.8650 -0.0479 -0.1683 -0.0958 115 LYS B NZ  
2927 N N   . GLY B 111 ? 0.6919 0.8052 0.8849 -0.1141 -0.0167 -0.0362 116 GLY B N   
2928 C CA  . GLY B 111 ? 0.7182 0.7869 0.9009 -0.1292 0.0136  -0.0280 116 GLY B CA  
2929 C C   . GLY B 111 ? 0.6671 0.7121 0.8249 -0.1065 0.0277  -0.0078 116 GLY B C   
2930 O O   . GLY B 111 ? 0.7254 0.7147 0.8413 -0.1029 0.0381  0.0029  116 GLY B O   
2931 N N   . ARG B 112 ? 0.6592 0.7461 0.8394 -0.0885 0.0255  -0.0036 117 ARG B N   
2932 C CA  . ARG B 112 ? 0.6551 0.7175 0.8082 -0.0668 0.0379  0.0125  117 ARG B CA  
2933 C C   . ARG B 112 ? 0.6360 0.6576 0.7409 -0.0495 0.0240  0.0206  117 ARG B C   
2934 O O   . ARG B 112 ? 0.7507 0.7295 0.8207 -0.0438 0.0336  0.0301  117 ARG B O   
2935 C CB  . ARG B 112 ? 0.6705 0.7836 0.8558 -0.0484 0.0396  0.0142  117 ARG B CB  
2936 C CG  . ARG B 112 ? 0.7430 0.8290 0.9056 -0.0332 0.0626  0.0274  117 ARG B CG  
2937 C CD  . ARG B 112 ? 0.8076 0.9440 1.0026 -0.0108 0.0658  0.0291  117 ARG B CD  
2938 N NE  . ARG B 112 ? 0.8675 1.0101 1.0466 0.0135  0.0420  0.0309  117 ARG B NE  
2939 C CZ  . ARG B 112 ? 0.8188 1.0033 1.0183 0.0399  0.0367  0.0328  117 ARG B CZ  
2940 N NH1 . ARG B 112 ? 0.7919 1.0284 1.0386 0.0470  0.0520  0.0321  117 ARG B NH1 
2941 N NH2 . ARG B 112 ? 0.9213 1.0940 1.0923 0.0618  0.0181  0.0365  117 ARG B NH2 
2942 N N   . ILE B 113 ? 0.5981 0.6340 0.7015 -0.0420 0.0022  0.0159  118 ILE B N   
2943 C CA  . ILE B 113 ? 0.6460 0.6478 0.7117 -0.0295 -0.0079 0.0224  118 ILE B CA  
2944 C C   . ILE B 113 ? 0.6514 0.6098 0.6919 -0.0400 -0.0031 0.0246  118 ILE B C   
2945 O O   . ILE B 113 ? 0.7470 0.6768 0.7622 -0.0319 -0.0013 0.0327  118 ILE B O   
2946 C CB  . ILE B 113 ? 0.6849 0.7055 0.7498 -0.0207 -0.0275 0.0170  118 ILE B CB  
2947 C CG1 . ILE B 113 ? 0.6921 0.7447 0.7670 0.0013  -0.0327 0.0203  118 ILE B CG1 
2948 C CG2 . ILE B 113 ? 0.6325 0.6166 0.6634 -0.0138 -0.0317 0.0228  118 ILE B CG2 
2949 C CD1 . ILE B 113 ? 0.7290 0.8117 0.8072 0.0114  -0.0530 0.0129  118 ILE B CD1 
2950 N N   . ILE B 114 ? 0.6705 0.6247 0.7179 -0.0574 -0.0014 0.0163  119 ILE B N   
2951 C CA  . ILE B 114 ? 0.6598 0.5692 0.6803 -0.0634 0.0052  0.0191  119 ILE B CA  
2952 C C   . ILE B 114 ? 0.7183 0.5986 0.7199 -0.0608 0.0215  0.0296  119 ILE B C   
2953 O O   . ILE B 114 ? 0.7458 0.5958 0.7178 -0.0501 0.0195  0.0373  119 ILE B O   
2954 C CB  . ILE B 114 ? 0.6770 0.5788 0.7050 -0.0846 0.0091  0.0069  119 ILE B CB  
2955 C CG1 . ILE B 114 ? 0.6801 0.5987 0.7101 -0.0837 -0.0100 -0.0043 119 ILE B CG1 
2956 C CG2 . ILE B 114 ? 0.7241 0.5703 0.7190 -0.0875 0.0226  0.0123  119 ILE B CG2 
2957 C CD1 . ILE B 114 ? 0.7638 0.6934 0.8121 -0.1079 -0.0120 -0.0231 119 ILE B CD1 
2958 N N   . LEU B 115 ? 0.6985 0.5904 0.7172 -0.0691 0.0376  0.0294  120 LEU B N   
2959 C CA  . LEU B 115 ? 0.7197 0.5802 0.7130 -0.0642 0.0563  0.0397  120 LEU B CA  
2960 C C   . LEU B 115 ? 0.7567 0.6098 0.7256 -0.0438 0.0466  0.0468  120 LEU B C   
2961 O O   . LEU B 115 ? 0.8441 0.6609 0.7750 -0.0349 0.0474  0.0536  120 LEU B O   
2962 C CB  . LEU B 115 ? 0.6714 0.5518 0.6929 -0.0759 0.0793  0.0381  120 LEU B CB  
2963 C CG  . LEU B 115 ? 0.7595 0.6021 0.7500 -0.0715 0.1060  0.0491  120 LEU B CG  
2964 C CD1 . LEU B 115 ? 0.7866 0.5676 0.7300 -0.0728 0.1166  0.0564  120 LEU B CD1 
2965 C CD2 . LEU B 115 ? 0.7952 0.6681 0.8279 -0.0865 0.1326  0.0461  120 LEU B CD2 
2966 N N   . GLU B 116 ? 0.7068 0.5918 0.6946 -0.0359 0.0366  0.0442  121 GLU B N   
2967 C CA  . GLU B 116 ? 0.6983 0.5711 0.6631 -0.0207 0.0287  0.0482  121 GLU B CA  
2968 C C   . GLU B 116 ? 0.6868 0.5424 0.6332 -0.0176 0.0120  0.0487  121 GLU B C   
2969 O O   . GLU B 116 ? 0.7848 0.6190 0.7052 -0.0110 0.0076  0.0507  121 GLU B O   
2970 C CB  . GLU B 116 ? 0.6813 0.5831 0.6654 -0.0112 0.0255  0.0466  121 GLU B CB  
2971 C CG  . GLU B 116 ? 0.7185 0.6360 0.7162 -0.0062 0.0439  0.0482  121 GLU B CG  
2972 C CD  . GLU B 116 ? 0.7798 0.7282 0.7964 0.0098  0.0411  0.0481  121 GLU B CD  
2973 O OE1 . GLU B 116 ? 0.8287 0.7831 0.8445 0.0162  0.0254  0.0471  121 GLU B OE1 
2974 O OE2 . GLU B 116 ? 0.7682 0.7336 0.7986 0.0189  0.0571  0.0501  121 GLU B OE2 
2975 N N   . ILE B 117 ? 0.6722 0.5393 0.6329 -0.0221 0.0030  0.0455  122 ILE B N   
2976 C CA  . ILE B 117 ? 0.6391 0.4955 0.5897 -0.0184 -0.0086 0.0466  122 ILE B CA  
2977 C C   . ILE B 117 ? 0.6836 0.5123 0.6091 -0.0149 -0.0069 0.0510  122 ILE B C   
2978 O O   . ILE B 117 ? 0.7113 0.5348 0.6252 -0.0072 -0.0177 0.0524  122 ILE B O   
2979 C CB  . ILE B 117 ? 0.6223 0.4907 0.5870 -0.0213 -0.0137 0.0427  122 ILE B CB  
2980 C CG1 . ILE B 117 ? 0.6190 0.5096 0.5967 -0.0177 -0.0184 0.0405  122 ILE B CG1 
2981 C CG2 . ILE B 117 ? 0.6465 0.5061 0.6046 -0.0154 -0.0201 0.0451  122 ILE B CG2 
2982 C CD1 . ILE B 117 ? 0.6780 0.5809 0.6634 -0.0206 -0.0225 0.0343  122 ILE B CD1 
2983 N N   . ILE B 118 ? 0.7821 0.5932 0.6992 -0.0204 0.0069  0.0527  123 ILE B N   
2984 C CA  . ILE B 118 ? 0.7570 0.5310 0.6392 -0.0128 0.0127  0.0598  123 ILE B CA  
2985 C C   . ILE B 118 ? 0.7826 0.5420 0.6353 -0.0021 0.0108  0.0637  123 ILE B C   
2986 O O   . ILE B 118 ? 0.7973 0.5437 0.6247 0.0115  -0.0020 0.0667  123 ILE B O   
2987 C CB  . ILE B 118 ? 0.7777 0.5262 0.6535 -0.0243 0.0355  0.0612  123 ILE B CB  
2988 C CG1 . ILE B 118 ? 0.7474 0.4988 0.6407 -0.0349 0.0350  0.0544  123 ILE B CG1 
2989 C CG2 . ILE B 118 ? 0.8273 0.5257 0.6546 -0.0123 0.0471  0.0718  123 ILE B CG2 
2990 C CD1 . ILE B 118 ? 0.7707 0.5173 0.6797 -0.0577 0.0544  0.0478  123 ILE B CD1 
2991 N N   . GLU B 119 ? 0.8074 0.5704 0.6626 -0.0067 0.0228  0.0628  124 GLU B N   
2992 C CA  . GLU B 119 ? 0.8286 0.5730 0.6503 0.0033  0.0233  0.0644  124 GLU B CA  
2993 C C   . GLU B 119 ? 0.8557 0.6089 0.6722 0.0096  -0.0023 0.0586  124 GLU B C   
2994 O O   . GLU B 119 ? 0.9290 0.6620 0.7092 0.0203  -0.0139 0.0586  124 GLU B O   
2995 C CB  . GLU B 119 ? 0.8424 0.5988 0.6783 -0.0006 0.0400  0.0628  124 GLU B CB  
2996 C CG  . GLU B 119 ? 0.8585 0.6077 0.6990 -0.0073 0.0698  0.0676  124 GLU B CG  
2997 C CD  . GLU B 119 ? 0.9500 0.7244 0.8156 -0.0071 0.0853  0.0658  124 GLU B CD  
2998 O OE1 . GLU B 119 ? 0.9243 0.7229 0.8075 -0.0019 0.0730  0.0612  124 GLU B OE1 
2999 O OE2 . GLU B 119 ? 1.0445 0.8136 0.9123 -0.0105 0.1131  0.0699  124 GLU B OE2 
3000 N N   . GLY B 120 ? 0.8215 0.6044 0.6738 0.0026  -0.0105 0.0532  125 GLY B N   
3001 C CA  . GLY B 120 ? 0.8065 0.5993 0.6638 0.0020  -0.0292 0.0465  125 GLY B CA  
3002 C C   . GLY B 120 ? 0.7999 0.6007 0.6587 0.0066  -0.0472 0.0458  125 GLY B C   
3003 O O   . GLY B 120 ? 0.8346 0.6345 0.6796 0.0096  -0.0641 0.0399  125 GLY B O   
3004 N N   . MET B 121 ? 0.7137 0.5234 0.5888 0.0083  -0.0441 0.0507  126 MET B N   
3005 C CA  . MET B 121 ? 0.7709 0.5891 0.6482 0.0187  -0.0578 0.0525  126 MET B CA  
3006 C C   . MET B 121 ? 0.8662 0.6587 0.7001 0.0355  -0.0640 0.0572  126 MET B C   
3007 O O   . MET B 121 ? 0.8893 0.6962 0.7212 0.0475  -0.0844 0.0553  126 MET B O   
3008 C CB  . MET B 121 ? 0.7251 0.5475 0.6202 0.0196  -0.0487 0.0568  126 MET B CB  
3009 C CG  . MET B 121 ? 0.7269 0.5752 0.6580 0.0098  -0.0470 0.0527  126 MET B CG  
3010 S SD  . MET B 121 ? 0.8286 0.7104 0.7903 0.0074  -0.0615 0.0470  126 MET B SD  
3011 C CE  . MET B 121 ? 0.9072 0.8014 0.8698 0.0265  -0.0747 0.0503  126 MET B CE  
3012 N N   . ALA B 122 ? 0.8312 0.5876 0.6311 0.0374  -0.0458 0.0636  127 ALA B N   
3013 C CA  . ALA B 122 ? 0.8993 0.6191 0.6440 0.0557  -0.0467 0.0703  127 ALA B CA  
3014 C C   . ALA B 122 ? 0.8867 0.6074 0.6062 0.0613  -0.0672 0.0622  127 ALA B C   
3015 O O   . ALA B 122 ? 0.9840 0.6964 0.6694 0.0807  -0.0860 0.0631  127 ALA B O   
3016 C CB  . ALA B 122 ? 0.9490 0.6273 0.6649 0.0526  -0.0156 0.0790  127 ALA B CB  
3017 N N   . TYR B 123 ? 0.8567 0.5855 0.5897 0.0460  -0.0646 0.0533  128 TYR B N   
3018 C CA  . TYR B 123 ? 0.8852 0.6105 0.5946 0.0463  -0.0838 0.0413  128 TYR B CA  
3019 C C   . TYR B 123 ? 0.8820 0.6463 0.6187 0.0455  -0.1165 0.0305  128 TYR B C   
3020 O O   . TYR B 123 ? 0.9480 0.7093 0.6527 0.0569  -0.1408 0.0236  128 TYR B O   
3021 C CB  . TYR B 123 ? 0.8713 0.5923 0.5909 0.0308  -0.0705 0.0345  128 TYR B CB  
3022 C CG  . TYR B 123 ? 0.9051 0.6181 0.6037 0.0260  -0.0893 0.0187  128 TYR B CG  
3023 C CD1 . TYR B 123 ? 0.9485 0.6200 0.5823 0.0372  -0.0907 0.0150  128 TYR B CD1 
3024 C CD2 . TYR B 123 ? 0.8931 0.6347 0.6328 0.0087  -0.1037 0.0064  128 TYR B CD2 
3025 C CE1 . TYR B 123 ? 1.0024 0.6611 0.6113 0.0306  -0.1098 -0.0033 128 TYR B CE1 
3026 C CE2 . TYR B 123 ? 0.9152 0.6450 0.6360 -0.0011 -0.1202 -0.0114 128 TYR B CE2 
3027 C CZ  . TYR B 123 ? 0.9779 0.6666 0.6330 0.0094  -0.1252 -0.0175 128 TYR B CZ  
3028 O OH  . TYR B 123 ? 1.0944 0.7665 0.7258 -0.0022 -0.1429 -0.0382 128 TYR B OH  
3029 N N   . LEU B 124 ? 0.8930 0.6951 0.6884 0.0324  -0.1162 0.0287  129 LEU B N   
3030 C CA  . LEU B 124 ? 0.8971 0.7446 0.7340 0.0269  -0.1406 0.0182  129 LEU B CA  
3031 C C   . LEU B 124 ? 0.8745 0.7416 0.7068 0.0502  -0.1611 0.0223  129 LEU B C   
3032 O O   . LEU B 124 ? 0.8822 0.7776 0.7200 0.0536  -0.1905 0.0105  129 LEU B O   
3033 C CB  . LEU B 124 ? 0.9159 0.7919 0.8102 0.0113  -0.1275 0.0192  129 LEU B CB  
3034 C CG  . LEU B 124 ? 0.9039 0.7677 0.8083 -0.0086 -0.1113 0.0146  129 LEU B CG  
3035 C CD1 . LEU B 124 ? 0.9062 0.7911 0.8539 -0.0159 -0.0969 0.0198  129 LEU B CD1 
3036 C CD2 . LEU B 124 ? 0.8783 0.7422 0.7828 -0.0247 -0.1249 -0.0021 129 LEU B CD2 
3037 N N   . HIS B 125 ? 0.9042 0.7542 0.7236 0.0671  -0.1460 0.0380  130 HIS B N   
3038 C CA  . HIS B 125 ? 0.8879 0.7425 0.6892 0.0971  -0.1603 0.0460  130 HIS B CA  
3039 C C   . HIS B 125 ? 0.9244 0.7518 0.6607 0.1177  -0.1792 0.0450  130 HIS B C   
3040 O O   . HIS B 125 ? 0.9379 0.7945 0.6719 0.1378  -0.2098 0.0408  130 HIS B O   
3041 C CB  . HIS B 125 ? 0.8926 0.7156 0.6812 0.1086  -0.1336 0.0628  130 HIS B CB  
3042 C CG  . HIS B 125 ? 0.8427 0.6954 0.6869 0.0985  -0.1227 0.0632  130 HIS B CG  
3043 N ND1 . HIS B 125 ? 0.8909 0.7232 0.7293 0.1114  -0.1054 0.0744  130 HIS B ND1 
3044 C CD2 . HIS B 125 ? 0.8175 0.7118 0.7172 0.0783  -0.1246 0.0538  130 HIS B CD2 
3045 C CE1 . HIS B 125 ? 0.8473 0.7090 0.7335 0.1004  -0.0986 0.0712  130 HIS B CE1 
3046 N NE2 . HIS B 125 ? 0.8487 0.7487 0.7728 0.0811  -0.1091 0.0599  130 HIS B NE2 
3047 N N   . GLY B 126 ? 0.9531 0.7283 0.6377 0.1135  -0.1615 0.0479  131 GLY B N   
3048 C CA  . GLY B 126 ? 1.0698 0.8106 0.6834 0.1301  -0.1759 0.0449  131 GLY B CA  
3049 C C   . GLY B 126 ? 1.1507 0.9240 0.7702 0.1222  -0.2134 0.0224  131 GLY B C   
3050 O O   . GLY B 126 ? 1.4271 1.1861 0.9903 0.1438  -0.2384 0.0180  131 GLY B O   
3051 N N   . LYS B 127 ? 1.0861 0.8973 0.7678 0.0910  -0.2163 0.0077  132 LYS B N   
3052 C CA  . LYS B 127 ? 1.0405 0.8888 0.7445 0.0747  -0.2502 -0.0170 132 LYS B CA  
3053 C C   . LYS B 127 ? 1.0110 0.9364 0.7860 0.0748  -0.2781 -0.0247 132 LYS B C   
3054 O O   . LYS B 127 ? 1.0367 1.0037 0.8520 0.0523  -0.3016 -0.0469 132 LYS B O   
3055 C CB  . LYS B 127 ? 1.0203 0.8549 0.7440 0.0401  -0.2328 -0.0289 132 LYS B CB  
3056 C CG  . LYS B 127 ? 1.0901 0.8571 0.7452 0.0424  -0.2109 -0.0260 132 LYS B CG  
3057 C CD  . LYS B 127 ? 1.2082 0.9455 0.7946 0.0501  -0.2368 -0.0427 132 LYS B CD  
3058 C CE  . LYS B 127 ? 1.3180 1.0551 0.9158 0.0197  -0.2488 -0.0689 132 LYS B CE  
3059 N NZ  . LYS B 127 ? 1.3283 1.0334 0.8594 0.0221  -0.2745 -0.0898 132 LYS B NZ  
3060 N N   . GLY B 128 ? 0.9771 0.9204 0.7670 0.1000  -0.2740 -0.0076 133 GLY B N   
3061 C CA  . GLY B 128 ? 0.9800 0.9977 0.8372 0.1072  -0.2957 -0.0116 133 GLY B CA  
3062 C C   . GLY B 128 ? 0.9268 0.9896 0.8699 0.0771  -0.2800 -0.0167 133 GLY B C   
3063 O O   . GLY B 128 ? 0.9295 1.0622 0.9377 0.0744  -0.2991 -0.0263 133 GLY B O   
3064 N N   . VAL B 129 ? 0.9061 0.9309 0.8493 0.0565  -0.2446 -0.0097 134 VAL B N   
3065 C CA  . VAL B 129 ? 0.8766 0.9281 0.8848 0.0286  -0.2251 -0.0130 134 VAL B CA  
3066 C C   . VAL B 129 ? 0.8729 0.9170 0.8918 0.0432  -0.1982 0.0067  134 VAL B C   
3067 O O   . VAL B 129 ? 1.0073 1.0004 0.9839 0.0485  -0.1769 0.0187  134 VAL B O   
3068 C CB  . VAL B 129 ? 0.8717 0.8812 0.8636 -0.0006 -0.2061 -0.0195 134 VAL B CB  
3069 C CG1 . VAL B 129 ? 0.8683 0.8933 0.9142 -0.0239 -0.1817 -0.0188 134 VAL B CG1 
3070 C CG2 . VAL B 129 ? 0.8650 0.8691 0.8360 -0.0158 -0.2306 -0.0411 134 VAL B CG2 
3071 N N   . ILE B 130 ? 0.8306 0.9262 0.9061 0.0492  -0.1990 0.0083  135 ILE B N   
3072 C CA  . ILE B 130 ? 0.7897 0.8790 0.8815 0.0563  -0.1706 0.0226  135 ILE B CA  
3073 C C   . ILE B 130 ? 0.7752 0.8681 0.9030 0.0246  -0.1492 0.0174  135 ILE B C   
3074 O O   . ILE B 130 ? 0.8222 0.9550 0.9977 0.0039  -0.1560 0.0046  135 ILE B O   
3075 C CB  . ILE B 130 ? 0.7618 0.9011 0.8931 0.0826  -0.1773 0.0280  135 ILE B CB  
3076 C CG1 . ILE B 130 ? 0.7748 0.9052 0.8621 0.1203  -0.1991 0.0351  135 ILE B CG1 
3077 C CG2 . ILE B 130 ? 0.7413 0.8641 0.8800 0.0902  -0.1457 0.0411  135 ILE B CG2 
3078 C CD1 . ILE B 130 ? 0.7517 0.9404 0.8758 0.1510  -0.2165 0.0374  135 ILE B CD1 
3079 N N   . HIS B 131 ? 0.7367 0.7869 0.8402 0.0210  -0.1234 0.0268  136 HIS B N   
3080 C CA  . HIS B 131 ? 0.7150 0.7597 0.8394 -0.0013 -0.1015 0.0254  136 HIS B CA  
3081 C C   . HIS B 131 ? 0.7170 0.8017 0.8946 -0.0019 -0.0888 0.0271  136 HIS B C   
3082 O O   . HIS B 131 ? 0.7648 0.8670 0.9777 -0.0239 -0.0800 0.0204  136 HIS B O   
3083 C CB  . HIS B 131 ? 0.6933 0.6909 0.7793 0.0001  -0.0818 0.0343  136 HIS B CB  
3084 C CG  . HIS B 131 ? 0.7537 0.7346 0.8405 -0.0190 -0.0665 0.0321  136 HIS B CG  
3085 N ND1 . HIS B 131 ? 0.8030 0.7973 0.9207 -0.0289 -0.0505 0.0324  136 HIS B ND1 
3086 C CD2 . HIS B 131 ? 0.8137 0.7622 0.8704 -0.0266 -0.0625 0.0309  136 HIS B CD2 
3087 C CE1 . HIS B 131 ? 0.7879 0.7539 0.8890 -0.0405 -0.0382 0.0323  136 HIS B CE1 
3088 N NE2 . HIS B 131 ? 0.8332 0.7739 0.8996 -0.0383 -0.0463 0.0311  136 HIS B NE2 
3089 N N   . LYS B 132 ? 0.6968 0.7886 0.8757 0.0223  -0.0832 0.0368  137 LYS B N   
3090 C CA  . LYS B 132 ? 0.7382 0.8637 0.9613 0.0294  -0.0662 0.0410  137 LYS B CA  
3091 C C   . LYS B 132 ? 0.7426 0.8379 0.9556 0.0211  -0.0351 0.0469  137 LYS B C   
3092 O O   . LYS B 132 ? 0.6829 0.7915 0.9156 0.0324  -0.0166 0.0526  137 LYS B O   
3093 C CB  . LYS B 132 ? 0.7703 0.9636 1.0633 0.0178  -0.0753 0.0309  137 LYS B CB  
3094 C CG  . LYS B 132 ? 0.7788 1.0114 1.0848 0.0249  -0.1123 0.0212  137 LYS B CG  
3095 C CD  . LYS B 132 ? 0.7510 1.0441 1.1240 -0.0024 -0.1239 0.0040  137 LYS B CD  
3096 C CE  . LYS B 132 ? 0.8232 1.1466 1.1953 0.0009  -0.1663 -0.0100 137 LYS B CE  
3097 N NZ  . LYS B 132 ? 0.8022 1.1840 1.2378 -0.0299 -0.1827 -0.0315 137 LYS B NZ  
3098 N N   . ASP B 133 ? 0.7621 0.8156 0.9394 0.0064  -0.0299 0.0462  138 ASP B N   
3099 C CA  . ASP B 133 ? 0.6949 0.7221 0.8599 -0.0015 -0.0051 0.0503  138 ASP B CA  
3100 C C   . ASP B 133 ? 0.5934 0.5760 0.7089 -0.0045 -0.0070 0.0512  138 ASP B C   
3101 O O   . ASP B 133 ? 0.6726 0.6363 0.7771 -0.0159 0.0022  0.0511  138 ASP B O   
3102 C CB  . ASP B 133 ? 0.7849 0.8311 0.9886 -0.0230 0.0083  0.0464  138 ASP B CB  
3103 C CG  . ASP B 133 ? 0.8749 0.8934 1.0639 -0.0238 0.0399  0.0545  138 ASP B CG  
3104 O OD1 . ASP B 133 ? 0.7565 0.7591 0.9215 -0.0053 0.0512  0.0616  138 ASP B OD1 
3105 O OD2 . ASP B 133 ? 0.9119 0.9182 1.1070 -0.0424 0.0542  0.0533  138 ASP B OD2 
3106 N N   . LEU B 134 ? 0.5851 0.5510 0.6719 0.0070  -0.0168 0.0525  139 LEU B N   
3107 C CA  . LEU B 134 ? 0.6456 0.5802 0.6960 0.0041  -0.0187 0.0521  139 LEU B CA  
3108 C C   . LEU B 134 ? 0.6492 0.5658 0.6808 0.0093  -0.0049 0.0546  139 LEU B C   
3109 O O   . LEU B 134 ? 0.6946 0.6073 0.7218 0.0203  0.0017  0.0563  139 LEU B O   
3110 C CB  . LEU B 134 ? 0.6962 0.6183 0.7258 0.0111  -0.0300 0.0520  139 LEU B CB  
3111 C CG  . LEU B 134 ? 0.7078 0.6052 0.7096 0.0061  -0.0292 0.0508  139 LEU B CG  
3112 C CD1 . LEU B 134 ? 0.7474 0.6445 0.7478 -0.0037 -0.0324 0.0484  139 LEU B CD1 
3113 C CD2 . LEU B 134 ? 0.7526 0.6323 0.7347 0.0122  -0.0325 0.0523  139 LEU B CD2 
3114 N N   . LYS B 135 ? 0.6519 0.5550 0.6678 0.0041  -0.0011 0.0545  140 LYS B N   
3115 C CA  . LYS B 135 ? 0.6428 0.5291 0.6334 0.0113  0.0074  0.0556  140 LYS B CA  
3116 C C   . LYS B 135 ? 0.6322 0.5095 0.6050 0.0097  0.0034  0.0551  140 LYS B C   
3117 O O   . LYS B 135 ? 0.6033 0.4831 0.5840 0.0030  -0.0004 0.0552  140 LYS B O   
3118 C CB  . LYS B 135 ? 0.6690 0.5545 0.6652 0.0161  0.0264  0.0609  140 LYS B CB  
3119 C CG  . LYS B 135 ? 0.7487 0.6422 0.7690 0.0052  0.0362  0.0639  140 LYS B CG  
3120 C CD  . LYS B 135 ? 0.7823 0.6801 0.8183 0.0072  0.0599  0.0693  140 LYS B CD  
3121 C CE  . LYS B 135 ? 0.8293 0.7312 0.8914 -0.0099 0.0728  0.0703  140 LYS B CE  
3122 N NZ  . LYS B 135 ? 0.9467 0.8600 1.0361 -0.0118 0.1000  0.0752  140 LYS B NZ  
3123 N N   . PRO B 136 ? 0.6641 0.5313 0.6105 0.0183  0.0028  0.0538  141 PRO B N   
3124 C CA  . PRO B 136 ? 0.7013 0.5668 0.6329 0.0230  -0.0025 0.0544  141 PRO B CA  
3125 C C   . PRO B 136 ? 0.7244 0.5763 0.6517 0.0252  0.0097  0.0626  141 PRO B C   
3126 O O   . PRO B 136 ? 0.7893 0.6408 0.7148 0.0264  0.0055  0.0631  141 PRO B O   
3127 C CB  . PRO B 136 ? 0.7297 0.5892 0.6319 0.0348  -0.0068 0.0508  141 PRO B CB  
3128 C CG  . PRO B 136 ? 0.7151 0.5738 0.6200 0.0291  -0.0095 0.0433  141 PRO B CG  
3129 C CD  . PRO B 136 ? 0.6758 0.5337 0.6022 0.0253  0.0031  0.0494  141 PRO B CD  
3130 N N   . GLU B 137 ? 0.7723 0.6108 0.6989 0.0248  0.0275  0.0685  142 GLU B N   
3131 C CA  . GLU B 137 ? 0.8182 0.6368 0.7443 0.0200  0.0445  0.0750  142 GLU B CA  
3132 C C   . GLU B 137 ? 0.7381 0.5628 0.6888 0.0035  0.0390  0.0702  142 GLU B C   
3133 O O   . GLU B 137 ? 0.8293 0.6298 0.7679 0.0014  0.0483  0.0729  142 GLU B O   
3134 C CB  . GLU B 137 ? 0.9730 0.7827 0.9069 0.0160  0.0684  0.0805  142 GLU B CB  
3135 C CG  . GLU B 137 ? 1.1451 0.9214 1.0341 0.0340  0.0868  0.0904  142 GLU B CG  
3136 C CD  . GLU B 137 ? 1.3349 1.1030 1.2341 0.0295  0.1161  0.0966  142 GLU B CD  
3137 O OE1 . GLU B 137 ? 1.4396 1.2236 1.3467 0.0343  0.1162  0.0942  142 GLU B OE1 
3138 O OE2 . GLU B 137 ? 1.3945 1.1381 1.2941 0.0209  0.1417  0.1036  142 GLU B OE2 
3139 N N   . ASN B 138 ? 0.7042 0.5548 0.6819 -0.0057 0.0250  0.0631  143 ASN B N   
3140 C CA  . ASN B 138 ? 0.6631 0.5194 0.6558 -0.0185 0.0149  0.0566  143 ASN B CA  
3141 C C   . ASN B 138 ? 0.6192 0.4761 0.5981 -0.0129 0.0012  0.0539  143 ASN B C   
3142 O O   . ASN B 138 ? 0.6631 0.5221 0.6464 -0.0201 -0.0075 0.0486  143 ASN B O   
3143 C CB  . ASN B 138 ? 0.6640 0.5481 0.6906 -0.0278 0.0076  0.0515  143 ASN B CB  
3144 C CG  . ASN B 138 ? 0.7011 0.5918 0.7561 -0.0422 0.0209  0.0501  143 ASN B CG  
3145 O OD1 . ASN B 138 ? 0.6908 0.5577 0.7389 -0.0526 0.0332  0.0497  143 ASN B OD1 
3146 N ND2 . ASN B 138 ? 0.6797 0.6028 0.7689 -0.0430 0.0203  0.0489  143 ASN B ND2 
3147 N N   . ILE B 139 ? 0.5847 0.4411 0.5469 -0.0001 -0.0001 0.0567  144 ILE B N   
3148 C CA  . ILE B 139 ? 0.6341 0.4977 0.5916 0.0044  -0.0083 0.0543  144 ILE B CA  
3149 C C   . ILE B 139 ? 0.6953 0.5470 0.6340 0.0184  -0.0022 0.0592  144 ILE B C   
3150 O O   . ILE B 139 ? 0.7405 0.5974 0.6684 0.0313  -0.0033 0.0620  144 ILE B O   
3151 C CB  . ILE B 139 ? 0.6342 0.5164 0.5974 0.0056  -0.0166 0.0508  144 ILE B CB  
3152 C CG1 . ILE B 139 ? 0.6466 0.5312 0.6205 -0.0029 -0.0199 0.0484  144 ILE B CG1 
3153 C CG2 . ILE B 139 ? 0.6331 0.5289 0.5994 0.0079  -0.0209 0.0480  144 ILE B CG2 
3154 C CD1 . ILE B 139 ? 0.6844 0.5729 0.6572 -0.0029 -0.0228 0.0449  144 ILE B CD1 
3155 N N   . LEU B 140 ? 0.6918 0.5238 0.6212 0.0182  0.0041  0.0599  145 LEU B N   
3156 C CA  . LEU B 140 ? 0.7287 0.5412 0.6349 0.0361  0.0131  0.0662  145 LEU B CA  
3157 C C   . LEU B 140 ? 0.7371 0.5729 0.6483 0.0494  0.0071  0.0654  145 LEU B C   
3158 O O   . LEU B 140 ? 0.7832 0.6345 0.7100 0.0395  0.0022  0.0600  145 LEU B O   
3159 C CB  . LEU B 140 ? 0.7481 0.5188 0.6375 0.0288  0.0266  0.0661  145 LEU B CB  
3160 C CG  . LEU B 140 ? 0.7933 0.5481 0.6903 0.0088  0.0345  0.0640  145 LEU B CG  
3161 C CD1 . LEU B 140 ? 0.7953 0.5059 0.6756 -0.0025 0.0479  0.0604  145 LEU B CD1 
3162 C CD2 . LEU B 140 ? 0.8291 0.5781 0.7177 0.0176  0.0449  0.0729  145 LEU B CD2 
3163 N N   . VAL B 141 ? 0.7356 0.5744 0.6335 0.0734  0.0088  0.0716  146 VAL B N   
3164 C CA  . VAL B 141 ? 0.7282 0.6058 0.6425 0.0888  0.0016  0.0704  146 VAL B CA  
3165 C C   . VAL B 141 ? 0.7985 0.6557 0.6899 0.1160  0.0132  0.0787  146 VAL B C   
3166 O O   . VAL B 141 ? 0.8630 0.6899 0.7224 0.1343  0.0198  0.0874  146 VAL B O   
3167 C CB  . VAL B 141 ? 0.7216 0.6388 0.6471 0.0975  -0.0148 0.0676  146 VAL B CB  
3168 C CG1 . VAL B 141 ? 0.7074 0.6785 0.6662 0.1049  -0.0244 0.0620  146 VAL B CG1 
3169 C CG2 . VAL B 141 ? 0.7138 0.6351 0.6485 0.0751  -0.0223 0.0607  146 VAL B CG2 
3170 N N   . ASP B 142 ? 0.7940 0.6622 0.6968 0.1210  0.0191  0.0772  147 ASP B N   
3171 C CA  . ASP B 142 ? 0.8261 0.6763 0.7077 0.1517  0.0324  0.0852  147 ASP B CA  
3172 C C   . ASP B 142 ? 0.8626 0.7688 0.7656 0.1821  0.0219  0.0887  147 ASP B C   
3173 O O   . ASP B 142 ? 0.8597 0.8173 0.7939 0.1745  0.0031  0.0822  147 ASP B O   
3174 C CB  . ASP B 142 ? 0.8298 0.6565 0.7050 0.1463  0.0476  0.0823  147 ASP B CB  
3175 C CG  . ASP B 142 ? 0.8197 0.6979 0.7352 0.1402  0.0457  0.0769  147 ASP B CG  
3176 O OD1 . ASP B 142 ? 0.8530 0.7922 0.8080 0.1457  0.0346  0.0754  147 ASP B OD1 
3177 O OD2 . ASP B 142 ? 0.8869 0.7406 0.7916 0.1287  0.0566  0.0733  147 ASP B OD2 
3178 N N   . ASN B 143 ? 1.0103 0.9068 0.8961 0.2172  0.0332  0.0976  148 ASN B N   
3179 C CA  . ASN B 143 ? 0.9763 0.9314 0.8826 0.2537  0.0210  0.1017  148 ASN B CA  
3180 C C   . ASN B 143 ? 0.9519 0.9930 0.9264 0.2441  0.0096  0.0910  148 ASN B C   
3181 O O   . ASN B 143 ? 0.9770 1.0836 0.9833 0.2570  -0.0120 0.0868  148 ASN B O   
3182 C CB  . ASN B 143 ? 0.9739 0.8946 0.8439 0.2982  0.0392  0.1153  148 ASN B CB  
3183 C CG  . ASN B 143 ? 0.9558 0.9168 0.8235 0.3445  0.0238  0.1237  148 ASN B CG  
3184 O OD1 . ASN B 143 ? 1.0150 0.9772 0.8648 0.3479  0.0066  0.1248  148 ASN B OD1 
3185 N ND2 . ASN B 143 ? 0.9673 0.9599 0.8489 0.3842  0.0301  0.1301  148 ASN B ND2 
3186 N N   . ASP B 144 ? 0.8915 0.9299 0.8859 0.2197  0.0242  0.0856  149 ASP B N   
3187 C CA  . ASP B 144 ? 0.8339 0.9421 0.8914 0.2022  0.0214  0.0756  149 ASP B CA  
3188 C C   . ASP B 144 ? 0.7712 0.8896 0.8483 0.1596  0.0084  0.0638  149 ASP B C   
3189 O O   . ASP B 144 ? 0.8914 1.0367 1.0052 0.1363  0.0157  0.0568  149 ASP B O   
3190 C CB  . ASP B 144 ? 0.9051 0.9964 0.9645 0.2018  0.0497  0.0781  149 ASP B CB  
3191 C CG  . ASP B 144 ? 1.1718 1.2483 1.2101 0.2453  0.0670  0.0892  149 ASP B CG  
3192 O OD1 . ASP B 144 ? 1.3519 1.4807 1.4141 0.2793  0.0578  0.0933  149 ASP B OD1 
3193 O OD2 . ASP B 144 ? 1.3599 1.3716 1.3555 0.2471  0.0898  0.0930  149 ASP B OD2 
3194 N N   . PHE B 145 ? 0.6645 0.7558 0.7140 0.1507  -0.0065 0.0628  150 PHE B N   
3195 C CA  . PHE B 145 ? 0.6450 0.7399 0.7060 0.1163  -0.0182 0.0525  150 PHE B CA  
3196 C C   . PHE B 145 ? 0.6649 0.7239 0.7201 0.0869  -0.0044 0.0506  150 PHE B C   
3197 O O   . PHE B 145 ? 0.7619 0.8271 0.8306 0.0614  -0.0107 0.0427  150 PHE B O   
3198 C CB  . PHE B 145 ? 0.6182 0.7859 0.7301 0.1081  -0.0365 0.0394  150 PHE B CB  
3199 C CG  . PHE B 145 ? 0.6453 0.8421 0.7502 0.1335  -0.0601 0.0381  150 PHE B CG  
3200 C CD1 . PHE B 145 ? 0.6517 0.8251 0.7253 0.1273  -0.0755 0.0345  150 PHE B CD1 
3201 C CD2 . PHE B 145 ? 0.6629 0.9086 0.7871 0.1685  -0.0664 0.0415  150 PHE B CD2 
3202 C CE1 . PHE B 145 ? 0.7106 0.9041 0.7658 0.1542  -0.0975 0.0337  150 PHE B CE1 
3203 C CE2 . PHE B 145 ? 0.7209 0.9913 0.8296 0.1976  -0.0913 0.0411  150 PHE B CE2 
3204 C CZ  . PHE B 145 ? 0.7393 0.9809 0.8098 0.1901  -0.1071 0.0371  150 PHE B CZ  
3205 N N   . HIS B 146 ? 0.6637 0.6804 0.6926 0.0920  0.0134  0.0573  151 HIS B N   
3206 C CA  . HIS B 146 ? 0.6729 0.6499 0.6839 0.0697  0.0218  0.0558  151 HIS B CA  
3207 C C   . HIS B 146 ? 0.6516 0.5865 0.6306 0.0626  0.0141  0.0568  151 HIS B C   
3208 O O   . HIS B 146 ? 0.7567 0.6711 0.7139 0.0775  0.0140  0.0617  151 HIS B O   
3209 C CB  . HIS B 146 ? 0.6960 0.6455 0.6878 0.0779  0.0420  0.0596  151 HIS B CB  
3210 C CG  . HIS B 146 ? 0.7265 0.7182 0.7536 0.0846  0.0562  0.0597  151 HIS B CG  
3211 N ND1 . HIS B 146 ? 0.7039 0.7146 0.7566 0.0636  0.0640  0.0556  151 HIS B ND1 
3212 C CD2 . HIS B 146 ? 0.7546 0.7744 0.7982 0.1106  0.0668  0.0638  151 HIS B CD2 
3213 C CE1 . HIS B 146 ? 0.7587 0.8099 0.8466 0.0728  0.0804  0.0565  151 HIS B CE1 
3214 N NE2 . HIS B 146 ? 0.7881 0.8500 0.8738 0.1029  0.0812  0.0613  151 HIS B NE2 
3215 N N   . ILE B 147 ? 0.6639 0.5857 0.6407 0.0412  0.0100  0.0530  152 ILE B N   
3216 C CA  . ILE B 147 ? 0.6774 0.5728 0.6371 0.0324  0.0026  0.0528  152 ILE B CA  
3217 C C   . ILE B 147 ? 0.7088 0.5670 0.6448 0.0242  0.0063  0.0515  152 ILE B C   
3218 O O   . ILE B 147 ? 0.7192 0.5675 0.6457 0.0234  0.0129  0.0505  152 ILE B O   
3219 C CB  . ILE B 147 ? 0.6519 0.5631 0.6264 0.0189  -0.0078 0.0488  152 ILE B CB  
3220 C CG1 . ILE B 147 ? 0.6586 0.5669 0.6377 0.0046  -0.0056 0.0460  152 ILE B CG1 
3221 C CG2 . ILE B 147 ? 0.6495 0.5953 0.6421 0.0254  -0.0154 0.0461  152 ILE B CG2 
3222 C CD1 . ILE B 147 ? 0.6871 0.5693 0.6496 -0.0024 -0.0095 0.0464  152 ILE B CD1 
3223 N N   . LYS B 148 ? 0.8029 0.6419 0.7296 0.0181  0.0021  0.0508  153 LYS B N   
3224 C CA  . LYS B 148 ? 0.7994 0.6126 0.7114 0.0061  -0.0009 0.0457  153 LYS B CA  
3225 C C   . LYS B 148 ? 0.7939 0.6154 0.7212 -0.0052 -0.0089 0.0442  153 LYS B C   
3226 O O   . LYS B 148 ? 0.8802 0.7042 0.8135 -0.0025 -0.0048 0.0480  153 LYS B O   
3227 C CB  . LYS B 148 ? 0.8216 0.5978 0.7078 0.0094  0.0085  0.0440  153 LYS B CB  
3228 C CG  . LYS B 148 ? 0.8583 0.6196 0.7237 0.0221  0.0187  0.0444  153 LYS B CG  
3229 C CD  . LYS B 148 ? 0.9139 0.6281 0.7463 0.0268  0.0302  0.0420  153 LYS B CD  
3230 C CE  . LYS B 148 ? 0.9361 0.6316 0.7437 0.0437  0.0440  0.0430  153 LYS B CE  
3231 N NZ  . LYS B 148 ? 1.1008 0.7670 0.8787 0.0322  0.0397  0.0325  153 LYS B NZ  
3232 N N   . ILE B 149 ? 0.7741 0.5999 0.7053 -0.0145 -0.0193 0.0395  154 ILE B N   
3233 C CA  . ILE B 149 ? 0.7440 0.5853 0.6960 -0.0224 -0.0262 0.0381  154 ILE B CA  
3234 C C   . ILE B 149 ? 0.7085 0.5381 0.6641 -0.0349 -0.0256 0.0317  154 ILE B C   
3235 O O   . ILE B 149 ? 0.7296 0.5418 0.6694 -0.0414 -0.0308 0.0237  154 ILE B O   
3236 C CB  . ILE B 149 ? 0.7880 0.6419 0.7430 -0.0217 -0.0383 0.0368  154 ILE B CB  
3237 C CG1 . ILE B 149 ? 0.8341 0.6925 0.7867 -0.0144 -0.0335 0.0422  154 ILE B CG1 
3238 C CG2 . ILE B 149 ? 0.7161 0.5916 0.6967 -0.0258 -0.0456 0.0351  154 ILE B CG2 
3239 C CD1 . ILE B 149 ? 0.9759 0.8278 0.9146 -0.0106 -0.0385 0.0433  154 ILE B CD1 
3240 N N   . ALA B 150 ? 0.7613 0.5241 1.0740 0.0791  0.0524  -0.0019 155 ALA B N   
3241 C CA  . ALA B 150 ? 0.6975 0.4754 1.0194 0.0931  0.0273  0.0125  155 ALA B CA  
3242 C C   . ALA B 150 ? 0.6617 0.4201 0.9402 0.1074  0.0360  0.0499  155 ALA B C   
3243 O O   . ALA B 150 ? 0.6130 0.3385 0.8672 0.1090  0.0591  0.0623  155 ALA B O   
3244 C CB  . ALA B 150 ? 0.6845 0.4607 1.0439 0.0933  -0.0072 0.0048  155 ALA B CB  
3245 N N   . ASP B 151 ? 0.7070 0.4875 0.9859 0.1166  0.0204  0.0632  156 ASP B N   
3246 C CA  . ASP B 151 ? 0.7506 0.5255 1.0060 0.1312  0.0246  0.0933  156 ASP B CA  
3247 C C   . ASP B 151 ? 0.7494 0.5311 1.0116 0.1287  -0.0015 0.0905  156 ASP B C   
3248 O O   . ASP B 151 ? 0.8033 0.6158 1.0669 0.1316  -0.0106 0.0969  156 ASP B O   
3249 C CB  . ASP B 151 ? 0.8133 0.6217 1.0567 0.1397  0.0335  0.1191  156 ASP B CB  
3250 C CG  . ASP B 151 ? 0.9370 0.7518 1.1768 0.1597  0.0366  0.1508  156 ASP B CG  
3251 O OD1 . ASP B 151 ? 0.9476 0.7269 1.1899 0.1668  0.0488  0.1511  156 ASP B OD1 
3252 O OD2 . ASP B 151 ? 1.0665 0.9299 1.3051 0.1642  0.0284  0.1714  156 ASP B OD2 
3253 N N   . LEU B 152 ? 0.7472 0.5024 1.0084 0.1171  -0.0136 0.0829  157 LEU B N   
3254 C CA  . LEU B 152 ? 0.7642 0.5195 1.0302 0.1061  -0.0454 0.0846  157 LEU B CA  
3255 C C   . LEU B 152 ? 0.7620 0.5212 0.9988 0.1044  -0.0419 0.0992  157 LEU B C   
3256 O O   . LEU B 152 ? 0.7506 0.5185 0.9897 0.0973  -0.0630 0.1025  157 LEU B O   
3257 C CB  . LEU B 152 ? 0.7367 0.4722 1.0055 0.0862  -0.0668 0.0810  157 LEU B CB  
3258 C CG  . LEU B 152 ? 0.6996 0.4422 1.0147 0.0870  -0.0764 0.0630  157 LEU B CG  
3259 C CD1 . LEU B 152 ? 0.7408 0.4766 1.0550 0.0641  -0.0996 0.0658  157 LEU B CD1 
3260 C CD2 . LEU B 152 ? 0.6675 0.4272 1.0420 0.0968  -0.0972 0.0528  157 LEU B CD2 
3261 N N   . GLY B 153 ? 0.7637 0.5154 0.9815 0.1096  -0.0118 0.1043  158 GLY B N   
3262 C CA  . GLY B 153 ? 0.7606 0.5268 0.9675 0.1118  0.0003  0.1118  158 GLY B CA  
3263 C C   . GLY B 153 ? 0.7799 0.5867 1.0053 0.1373  0.0083  0.1270  158 GLY B C   
3264 O O   . GLY B 153 ? 0.8253 0.6523 1.0565 0.1443  0.0218  0.1332  158 GLY B O   
3265 N N   . LEU B 154 ? 0.7427 0.5701 0.9796 0.1464  0.0009  0.1315  159 LEU B N   
3266 C CA  . LEU B 154 ? 0.7044 0.5865 0.9492 0.1574  -0.0004 0.1478  159 LEU B CA  
3267 C C   . LEU B 154 ? 0.7213 0.6197 0.9816 0.1824  0.0186  0.1781  159 LEU B C   
3268 O O   . LEU B 154 ? 0.7625 0.7147 1.0358 0.1914  0.0137  0.1958  159 LEU B O   
3269 C CB  . LEU B 154 ? 0.6980 0.6125 0.9390 0.1432  -0.0176 0.1385  159 LEU B CB  
3270 C CG  . LEU B 154 ? 0.6666 0.5567 0.9089 0.1219  -0.0380 0.1153  159 LEU B CG  
3271 C CD1 . LEU B 154 ? 0.6501 0.5605 0.8857 0.1062  -0.0486 0.1102  159 LEU B CD1 
3272 C CD2 . LEU B 154 ? 0.6799 0.5809 0.9426 0.1175  -0.0398 0.0987  159 LEU B CD2 
3273 N N   . ALA B 155 ? 0.7478 0.6007 1.0147 0.1933  0.0402  0.1844  160 ALA B N   
3274 C CA  . ALA B 155 ? 0.7839 0.6333 1.0836 0.2211  0.0621  0.2147  160 ALA B CA  
3275 C C   . ALA B 155 ? 0.8300 0.7276 1.1391 0.2355  0.0495  0.2592  160 ALA B C   
3276 O O   . ALA B 155 ? 0.9455 0.8737 1.2954 0.2614  0.0510  0.2943  160 ALA B O   
3277 C CB  . ALA B 155 ? 0.8376 0.6169 1.1413 0.2222  0.0928  0.2055  160 ALA B CB  
3278 N N   . SER B 156 ? 0.8001 0.7113 1.0757 0.2148  0.0365  0.2571  161 SER B N   
3279 C CA  . SER B 156 ? 0.8330 0.7987 1.0975 0.2102  0.0225  0.2965  161 SER B CA  
3280 C C   . SER B 156 ? 0.7757 0.8301 1.0303 0.1932  -0.0019 0.2966  161 SER B C   
3281 O O   . SER B 156 ? 0.8168 0.9313 1.0543 0.1788  -0.0157 0.3288  161 SER B O   
3282 C CB  . SER B 156 ? 0.9269 0.8706 1.1556 0.1833  0.0286  0.2842  161 SER B CB  
3283 O OG  . SER B 156 ? 1.0635 0.9315 1.2973 0.1935  0.0530  0.2866  161 SER B OG  
3284 N N   . PHE B 157 ? 0.8051 0.8699 1.0650 0.1878  -0.0064 0.2623  162 PHE B N   
3285 C CA  . PHE B 157 ? 0.8219 0.9588 1.0684 0.1622  -0.0225 0.2468  162 PHE B CA  
3286 C C   . PHE B 157 ? 0.8410 1.0073 1.1104 0.1734  -0.0266 0.2457  162 PHE B C   
3287 O O   . PHE B 157 ? 0.8763 1.0071 1.1421 0.1652  -0.0231 0.2110  162 PHE B O   
3288 C CB  . PHE B 157 ? 0.7694 0.8796 0.9987 0.1322  -0.0202 0.1946  162 PHE B CB  
3289 C CG  . PHE B 157 ? 0.7591 0.8598 0.9723 0.1144  -0.0122 0.1872  162 PHE B CG  
3290 C CD1 . PHE B 157 ? 0.7611 0.9310 0.9487 0.0871  -0.0150 0.2037  162 PHE B CD1 
3291 C CD2 . PHE B 157 ? 0.7787 0.8103 0.9990 0.1179  -0.0017 0.1635  162 PHE B CD2 
3292 C CE1 . PHE B 157 ? 0.7865 0.9515 0.9526 0.0610  -0.0032 0.1927  162 PHE B CE1 
3293 C CE2 . PHE B 157 ? 0.8079 0.8368 1.0162 0.0975  0.0097  0.1514  162 PHE B CE2 
3294 C CZ  . PHE B 157 ? 0.7948 0.8877 0.9741 0.0679  0.0111  0.1644  162 PHE B CZ  
3295 N N   . LYS B 158 ? 0.8188 1.0545 1.1140 0.1893  -0.0361 0.2868  163 LYS B N   
3296 C CA  . LYS B 158 ? 0.8200 1.0913 1.1555 0.2068  -0.0351 0.2894  163 LYS B CA  
3297 C C   . LYS B 158 ? 0.8269 1.1265 1.1410 0.1757  -0.0383 0.2469  163 LYS B C   
3298 O O   . LYS B 158 ? 0.8573 1.1250 1.1804 0.1772  -0.0263 0.2224  163 LYS B O   
3299 C CB  . LYS B 158 ? 0.7621 1.1218 1.1425 0.2290  -0.0520 0.3466  163 LYS B CB  
3300 C CG  . LYS B 158 ? 0.7720 1.2328 1.1280 0.2019  -0.0791 0.3737  163 LYS B CG  
3301 C CD  . LYS B 158 ? 0.7940 1.3547 1.2097 0.2262  -0.1024 0.4325  163 LYS B CD  
3302 C CE  . LYS B 158 ? 0.8377 1.3681 1.3057 0.2706  -0.1073 0.4994  163 LYS B CE  
3303 N NZ  . LYS B 158 ? 0.8686 1.5075 1.4062 0.2946  -0.1397 0.5683  163 LYS B NZ  
3304 N N   . MET B 159 ? 0.8321 1.1886 1.1152 0.1411  -0.0506 0.2359  164 MET B N   
3305 C CA  . MET B 159 ? 0.8280 1.2140 1.0935 0.1068  -0.0508 0.1965  164 MET B CA  
3306 C C   . MET B 159 ? 0.7895 1.0833 1.0361 0.0924  -0.0418 0.1547  164 MET B C   
3307 O O   . MET B 159 ? 0.8021 1.0855 1.0452 0.0804  -0.0386 0.1353  164 MET B O   
3308 C CB  . MET B 159 ? 0.8551 1.3269 1.0955 0.0663  -0.0589 0.1889  164 MET B CB  
3309 C CG  . MET B 159 ? 0.9282 1.5173 1.1846 0.0702  -0.0776 0.2365  164 MET B CG  
3310 S SD  . MET B 159 ? 1.0075 1.6729 1.3095 0.0842  -0.0828 0.2436  164 MET B SD  
3311 C CE  . MET B 159 ? 1.0992 1.9160 1.4247 0.0835  -0.1157 0.3085  164 MET B CE  
3312 N N   . TRP B 160 ? 0.7415 0.9727 0.9787 0.0913  -0.0398 0.1441  165 TRP B N   
3313 C CA  . TRP B 160 ? 0.7045 0.8472 0.9372 0.0846  -0.0392 0.1173  165 TRP B CA  
3314 C C   . TRP B 160 ? 0.7172 0.8072 0.9504 0.1025  -0.0357 0.1276  165 TRP B C   
3315 O O   . TRP B 160 ? 0.7849 0.8269 1.0049 0.0862  -0.0405 0.1130  165 TRP B O   
3316 C CB  . TRP B 160 ? 0.6732 0.7734 0.9116 0.0826  -0.0383 0.1038  165 TRP B CB  
3317 C CG  . TRP B 160 ? 0.6489 0.7842 0.8920 0.0518  -0.0335 0.0726  165 TRP B CG  
3318 C CD1 . TRP B 160 ? 0.6543 0.8598 0.8863 0.0343  -0.0266 0.0734  165 TRP B CD1 
3319 C CD2 . TRP B 160 ? 0.6378 0.7390 0.9023 0.0296  -0.0319 0.0337  165 TRP B CD2 
3320 N NE1 . TRP B 160 ? 0.6460 0.8679 0.8885 -0.0027 -0.0143 0.0272  165 TRP B NE1 
3321 C CE2 . TRP B 160 ? 0.6572 0.8114 0.9285 -0.0018 -0.0160 0.0016  165 TRP B CE2 
3322 C CE3 . TRP B 160 ? 0.6487 0.6789 0.9303 0.0297  -0.0428 0.0255  165 TRP B CE3 
3323 C CZ2 . TRP B 160 ? 0.6622 0.7957 0.9704 -0.0288 -0.0033 -0.0471 165 TRP B CZ2 
3324 C CZ3 . TRP B 160 ? 0.6426 0.6480 0.9620 0.0078  -0.0384 -0.0107 165 TRP B CZ3 
3325 C CH2 . TRP B 160 ? 0.6423 0.6969 0.9813 -0.0188 -0.0151 -0.0506 165 TRP B CH2 
3326 N N   . SER B 161 ? 0.7543 0.8524 1.0039 0.1309  -0.0260 0.1528  166 SER B N   
3327 C CA  . SER B 161 ? 0.7793 0.8375 1.0366 0.1424  -0.0115 0.1532  166 SER B CA  
3328 C C   . SER B 161 ? 0.7484 0.8452 1.0108 0.1310  -0.0052 0.1431  166 SER B C   
3329 O O   . SER B 161 ? 0.7911 0.8493 1.0348 0.1114  0.0026  0.1248  166 SER B O   
3330 C CB  . SER B 161 ? 0.7611 0.8133 1.0503 0.1763  0.0045  0.1788  166 SER B CB  
3331 O OG  . SER B 161 ? 0.8669 0.8596 1.1586 0.1775  0.0254  0.1656  166 SER B OG  
3332 N N   . LYS B 162 ? 0.7310 0.9112 1.0161 0.1370  -0.0093 0.1545  167 LYS B N   
3333 C CA  . LYS B 162 ? 0.7870 1.0205 1.0794 0.1205  -0.0040 0.1392  167 LYS B CA  
3334 C C   . LYS B 162 ? 0.7637 0.9702 1.0070 0.0760  -0.0119 0.1108  167 LYS B C   
3335 O O   . LYS B 162 ? 0.8178 1.0166 1.0457 0.0516  -0.0025 0.0919  167 LYS B O   
3336 C CB  . LYS B 162 ? 0.7375 1.0812 1.0678 0.1332  -0.0127 0.1608  167 LYS B CB  
3337 C CG  . LYS B 162 ? 0.7050 1.0772 1.1052 0.1800  -0.0047 0.1949  167 LYS B CG  
3338 C CD  . LYS B 162 ? 0.7047 1.1908 1.1448 0.1938  -0.0258 0.2327  167 LYS B CD  
3339 C CE  . LYS B 162 ? 0.7222 1.2269 1.2473 0.2459  -0.0226 0.2775  167 LYS B CE  
3340 N NZ  . LYS B 162 ? 0.7322 1.3555 1.3008 0.2595  -0.0533 0.3290  167 LYS B NZ  
3341 N N   . LEU B 163 ? 0.7438 0.9352 0.9677 0.0630  -0.0263 0.1067  168 LEU B N   
3342 C CA  . LEU B 163 ? 0.7484 0.8964 0.9419 0.0260  -0.0339 0.0839  168 LEU B CA  
3343 C C   . LEU B 163 ? 0.8080 0.8644 0.9769 0.0141  -0.0399 0.0833  168 LEU B C   
3344 O O   . LEU B 163 ? 0.8005 0.8271 0.9417 -0.0198 -0.0450 0.0741  168 LEU B O   
3345 C CB  . LEU B 163 ? 0.6950 0.8410 0.8947 0.0193  -0.0407 0.0740  168 LEU B CB  
3346 C CG  . LEU B 163 ? 0.7092 0.8062 0.9027 -0.0133 -0.0451 0.0492  168 LEU B CG  
3347 C CD1 . LEU B 163 ? 0.7088 0.8428 0.8847 -0.0479 -0.0374 0.0321  168 LEU B CD1 
3348 C CD2 . LEU B 163 ? 0.7286 0.8331 0.9465 -0.0177 -0.0412 0.0298  168 LEU B CD2 
3349 N N   . ASN B 164 ? 0.8723 0.8871 1.0476 0.0363  -0.0407 0.0955  169 ASN B N   
3350 C CA  . ASN B 164 ? 0.9285 0.8709 1.0774 0.0202  -0.0491 0.0984  169 ASN B CA  
3351 C C   . ASN B 164 ? 0.9710 0.9172 1.0921 -0.0049 -0.0334 0.0909  169 ASN B C   
3352 O O   . ASN B 164 ? 0.9478 0.8485 1.0271 -0.0429 -0.0456 0.0921  169 ASN B O   
3353 C CB  . ASN B 164 ? 0.9688 0.8796 1.1324 0.0456  -0.0483 0.1074  169 ASN B CB  
3354 C CG  . ASN B 164 ? 1.0530 0.8989 1.1914 0.0242  -0.0650 0.1123  169 ASN B CG  
3355 O OD1 . ASN B 164 ? 1.2935 1.1204 1.4380 0.0369  -0.0587 0.1144  169 ASN B OD1 
3356 N ND2 . ASN B 164 ? 1.1060 0.9197 1.2164 -0.0108 -0.0881 0.1181  169 ASN B ND2 
3357 N N   . ASN B 165 ? 0.9919 0.9955 1.1409 0.0131  -0.0069 0.0839  170 ASN B N   
3358 C CA  . ASN B 165 ? 1.1048 1.1232 1.2461 -0.0094 0.0198  0.0648  170 ASN B CA  
3359 C C   . ASN B 165 ? 1.0799 1.1615 1.2232 -0.0299 0.0279  0.0489  170 ASN B C   
3360 O O   . ASN B 165 ? 1.2119 1.3425 1.3853 -0.0306 0.0568  0.0296  170 ASN B O   
3361 C CB  . ASN B 165 ? 1.2046 1.2396 1.3996 0.0277  0.0503  0.0625  170 ASN B CB  
3362 C CG  . ASN B 165 ? 1.2260 1.1985 1.4131 0.0392  0.0486  0.0718  170 ASN B CG  
3363 O OD1 . ASN B 165 ? 1.1091 1.0843 1.3359 0.0805  0.0520  0.0882  170 ASN B OD1 
3364 N ND2 . ASN B 165 ? 1.3398 1.2598 1.4726 -0.0022 0.0411  0.0641  170 ASN B ND2 
3365 N N   . GLU B 166 ? 1.0703 1.1483 1.1865 -0.0511 0.0061  0.0518  171 GLU B N   
3366 C CA  . GLU B 166 ? 0.9910 1.1333 1.1079 -0.0731 0.0128  0.0354  171 GLU B CA  
3367 C C   . GLU B 166 ? 1.0151 1.1237 1.0732 -0.1330 0.0195  0.0187  171 GLU B C   
3368 O O   . GLU B 166 ? 1.0181 1.0458 1.0260 -0.1617 0.0007  0.0320  171 GLU B O   
3369 C CB  . GLU B 166 ? 0.9975 1.1520 1.1170 -0.0715 -0.0060 0.0403  171 GLU B CB  
3370 C CG  . GLU B 166 ? 1.0992 1.2724 1.1917 -0.1167 -0.0046 0.0208  171 GLU B CG  
3371 C CD  . GLU B 166 ? 1.1298 1.4046 1.2401 -0.1285 0.0158  0.0003  171 GLU B CD  
3372 O OE1 . GLU B 166 ? 1.3055 1.6510 1.4674 -0.0925 0.0257  0.0051  171 GLU B OE1 
3373 O OE2 . GLU B 166 ? 1.0574 1.3398 1.1361 -0.1749 0.0219  -0.0201 171 GLU B OE2 
3374 N N   . GLU B 167 ? 1.0486 1.2260 1.1161 -0.1541 0.0441  -0.0077 172 GLU B N   
3375 C CA  . GLU B 167 ? 1.0488 1.2128 1.0589 -0.2202 0.0597  -0.0311 172 GLU B CA  
3376 C C   . GLU B 167 ? 1.0493 1.1352 0.9838 -0.2720 0.0333  -0.0158 172 GLU B C   
3377 O O   . GLU B 167 ? 1.0896 1.1205 0.9581 -0.3255 0.0303  -0.0120 172 GLU B O   
3378 C CB  . GLU B 167 ? 1.0505 1.3203 1.0998 -0.2297 0.0896  -0.0659 172 GLU B CB  
3379 C CG  . GLU B 167 ? 1.1400 1.4189 1.1500 -0.2935 0.1209  -0.1026 172 GLU B CG  
3380 C CD  . GLU B 167 ? 1.0763 1.4764 1.1574 -0.2894 0.1557  -0.1427 172 GLU B CD  
3381 O OE1 . GLU B 167 ? 1.1008 1.5303 1.2063 -0.3080 0.1944  -0.1796 172 GLU B OE1 
3382 O OE2 . GLU B 167 ? 1.0431 1.5147 1.1606 -0.2711 0.1460  -0.1406 172 GLU B OE2 
3383 N N   . HIS B 168 ? 1.0136 1.0956 0.9623 -0.2586 0.0154  -0.0062 173 HIS B N   
3384 C CA  . HIS B 168 ? 1.0213 1.0240 0.9256 -0.2977 -0.0070 0.0086  173 HIS B CA  
3385 C C   . HIS B 168 ? 1.0071 0.9153 0.9142 -0.2789 -0.0423 0.0449  173 HIS B C   
3386 O O   . HIS B 168 ? 1.0647 0.9002 0.9529 -0.3063 -0.0627 0.0622  173 HIS B O   
3387 C CB  . HIS B 168 ? 1.0026 1.0539 0.9322 -0.3001 0.0019  -0.0121 173 HIS B CB  
3388 C CG  . HIS B 168 ? 0.9678 1.1147 0.8951 -0.3279 0.0316  -0.0469 173 HIS B CG  
3389 N ND1 . HIS B 168 ? 0.9013 1.1658 0.8873 -0.2942 0.0458  -0.0644 173 HIS B ND1 
3390 C CD2 . HIS B 168 ? 1.0064 1.1549 0.8831 -0.3889 0.0485  -0.0660 173 HIS B CD2 
3391 C CE1 . HIS B 168 ? 0.9186 1.2581 0.9006 -0.3289 0.0697  -0.0951 173 HIS B CE1 
3392 N NE2 . HIS B 168 ? 0.9736 1.2436 0.8871 -0.3883 0.0752  -0.1008 173 HIS B NE2 
3393 N N   . ASN B 169 ? 0.9759 0.8844 0.9152 -0.2326 -0.0490 0.0566  174 ASN B N   
3394 C CA  . ASN B 169 ? 1.0011 0.8349 0.9554 -0.2122 -0.0815 0.0867  174 ASN B CA  
3395 C C   . ASN B 169 ? 1.0972 0.8553 0.9943 -0.2563 -0.1092 0.1187  174 ASN B C   
3396 O O   . ASN B 169 ? 1.1626 0.9288 1.0241 -0.2727 -0.1031 0.1199  174 ASN B O   
3397 C CB  . ASN B 169 ? 0.9347 0.7957 0.9316 -0.1582 -0.0768 0.0872  174 ASN B CB  
3398 C CG  . ASN B 169 ? 0.9595 0.7645 0.9899 -0.1315 -0.1050 0.1078  174 ASN B CG  
3399 O OD1 . ASN B 169 ? 0.9989 0.7430 1.0352 -0.1469 -0.1309 0.1243  174 ASN B OD1 
3400 N ND2 . ASN B 169 ? 0.9231 0.7484 0.9848 -0.0907 -0.0988 0.1067  174 ASN B ND2 
3401 N N   . GLU B 170 ? 1.1554 0.8402 1.0493 -0.2769 -0.1406 0.1469  175 GLU B N   
3402 C CA  . GLU B 170 ? 1.3070 0.9218 1.1463 -0.3228 -0.1783 0.1923  175 GLU B CA  
3403 C C   . GLU B 170 ? 1.3170 0.9054 1.1819 -0.2949 -0.2116 0.2230  175 GLU B C   
3404 O O   . GLU B 170 ? 1.3854 0.9095 1.2630 -0.3029 -0.2574 0.2688  175 GLU B O   
3405 C CB  . GLU B 170 ? 1.4052 0.9464 1.2323 -0.3612 -0.2021 0.2206  175 GLU B CB  
3406 C CG  . GLU B 170 ? 1.3801 0.8702 1.2970 -0.3222 -0.2190 0.2296  175 GLU B CG  
3407 C CD  . GLU B 170 ? 1.4660 0.8574 1.3754 -0.3617 -0.2560 0.2792  175 GLU B CD  
3408 O OE1 . GLU B 170 ? 1.4938 0.8562 1.4283 -0.3729 -0.2384 0.2622  175 GLU B OE1 
3409 O OE2 . GLU B 170 ? 1.5308 0.8737 1.4130 -0.3833 -0.3038 0.3376  175 GLU B OE2 
3410 N N   . LEU B 171 ? 1.2780 0.9177 1.1517 -0.2664 -0.1885 0.1994  176 LEU B N   
3411 C CA  . LEU B 171 ? 1.3300 0.9595 1.2298 -0.2392 -0.2090 0.2159  176 LEU B CA  
3412 C C   . LEU B 171 ? 1.4509 1.1260 1.3154 -0.2480 -0.1755 0.1903  176 LEU B C   
3413 O O   . LEU B 171 ? 1.4507 1.1777 1.3316 -0.2267 -0.1315 0.1525  176 LEU B O   
3414 C CB  . LEU B 171 ? 1.1835 0.8210 1.1730 -0.1732 -0.2063 0.2026  176 LEU B CB  
3415 C CG  . LEU B 171 ? 1.1600 0.7539 1.2141 -0.1563 -0.2298 0.2143  176 LEU B CG  
3416 C CD1 . LEU B 171 ? 1.0921 0.7134 1.2238 -0.1018 -0.2136 0.1864  176 LEU B CD1 
3417 C CD2 . LEU B 171 ? 1.2028 0.7303 1.2697 -0.1734 -0.2845 0.2661  176 LEU B CD2 
3418 N N   . GLY B 183 ? 1.1416 1.0648 1.2980 0.0033  0.2576  0.1087  188 GLY B N   
3419 C CA  . GLY B 183 ? 1.2553 1.1702 1.3773 0.0114  0.2139  0.1012  188 GLY B CA  
3420 C C   . GLY B 183 ? 1.3708 1.2647 1.4423 0.0400  0.2048  0.1017  188 GLY B C   
3421 O O   . GLY B 183 ? 1.4676 1.3636 1.5395 0.0566  0.2274  0.1062  188 GLY B O   
3422 N N   . THR B 184 ? 1.3648 1.2372 1.3937 0.0444  0.1736  0.0960  189 THR B N   
3423 C CA  . THR B 184 ? 1.2521 1.1022 1.2334 0.0645  0.1600  0.0918  189 THR B CA  
3424 C C   . THR B 184 ? 1.1677 1.0490 1.1819 0.0697  0.1443  0.0861  189 THR B C   
3425 O O   . THR B 184 ? 1.0765 0.9864 1.1244 0.0583  0.1209  0.0813  189 THR B O   
3426 C CB  . THR B 184 ? 1.3197 1.1403 1.2492 0.0649  0.1343  0.0865  189 THR B CB  
3427 O OG1 . THR B 184 ? 1.2867 1.0829 1.1695 0.0801  0.1251  0.0798  189 THR B OG1 
3428 C CG2 . THR B 184 ? 1.2495 1.0934 1.2063 0.0488  0.1043  0.0798  189 THR B CG2 
3429 N N   . LEU B 185 ? 1.0819 0.9510 1.0787 0.0901  0.1592  0.0873  190 LEU B N   
3430 C CA  . LEU B 185 ? 1.0049 0.8915 1.0210 0.1030  0.1505  0.0845  190 LEU B CA  
3431 C C   . LEU B 185 ? 0.9508 0.7995 0.9161 0.1080  0.1284  0.0756  190 LEU B C   
3432 O O   . LEU B 185 ? 1.0185 0.8670 0.9873 0.1207  0.1244  0.0743  190 LEU B O   
3433 C CB  . LEU B 185 ? 1.0333 0.9235 1.0582 0.1252  0.1837  0.0911  190 LEU B CB  
3434 C CG  . LEU B 185 ? 0.9830 0.9172 1.0697 0.1178  0.2118  0.0994  190 LEU B CG  
3435 C CD1 . LEU B 185 ? 1.0205 0.9582 1.1144 0.1433  0.2482  0.1064  190 LEU B CD1 
3436 C CD2 . LEU B 185 ? 0.9353 0.9354 1.1006 0.1010  0.1928  0.0967  190 LEU B CD2 
3437 N N   . TYR B 186 ? 0.9322 0.7498 0.8525 0.0986  0.1155  0.0694  191 TYR B N   
3438 C CA  . TYR B 186 ? 0.8930 0.6782 0.7709 0.0973  0.0961  0.0579  191 TYR B CA  
3439 C C   . TYR B 186 ? 0.8517 0.6514 0.7530 0.0869  0.0743  0.0546  191 TYR B C   
3440 O O   . TYR B 186 ? 0.9577 0.7286 0.8319 0.0879  0.0676  0.0470  191 TYR B O   
3441 C CB  . TYR B 186 ? 0.9107 0.6756 0.7479 0.0890  0.0835  0.0511  191 TYR B CB  
3442 C CG  . TYR B 186 ? 0.9244 0.6604 0.7148 0.1025  0.1007  0.0529  191 TYR B CG  
3443 C CD1 . TYR B 186 ? 0.8991 0.6113 0.6664 0.1215  0.1275  0.0561  191 TYR B CD1 
3444 C CD2 . TYR B 186 ? 0.9151 0.6436 0.6768 0.1003  0.0905  0.0520  191 TYR B CD2 
3445 C CE1 . TYR B 186 ? 0.9623 0.6404 0.6752 0.1359  0.1448  0.0583  191 TYR B CE1 
3446 C CE2 . TYR B 186 ? 0.9450 0.6407 0.6518 0.1169  0.1048  0.0548  191 TYR B CE2 
3447 C CZ  . TYR B 186 ? 0.9974 0.6659 0.6775 0.1337  0.1324  0.0578  191 TYR B CZ  
3448 O OH  . TYR B 186 ? 1.0907 0.7203 0.7073 0.1523  0.1487  0.0613  191 TYR B OH  
3449 N N   . TYR B 187 ? 0.8658 0.7032 0.8111 0.0762  0.0653  0.0595  192 TYR B N   
3450 C CA  . TYR B 187 ? 0.8072 0.6561 0.7684 0.0672  0.0452  0.0575  192 TYR B CA  
3451 C C   . TYR B 187 ? 0.7353 0.6137 0.7338 0.0781  0.0449  0.0637  192 TYR B C   
3452 O O   . TYR B 187 ? 0.7500 0.6372 0.7573 0.0747  0.0288  0.0636  192 TYR B O   
3453 C CB  . TYR B 187 ? 0.8064 0.6711 0.7797 0.0489  0.0323  0.0565  192 TYR B CB  
3454 C CG  . TYR B 187 ? 0.7528 0.5968 0.6925 0.0440  0.0302  0.0515  192 TYR B CG  
3455 C CD1 . TYR B 187 ? 0.7711 0.6091 0.6979 0.0491  0.0435  0.0554  192 TYR B CD1 
3456 C CD2 . TYR B 187 ? 0.7792 0.6099 0.6986 0.0360  0.0158  0.0427  192 TYR B CD2 
3457 C CE1 . TYR B 187 ? 0.8099 0.6295 0.6991 0.0508  0.0381  0.0511  192 TYR B CE1 
3458 C CE2 . TYR B 187 ? 0.8485 0.6706 0.7419 0.0338  0.0092  0.0361  192 TYR B CE2 
3459 C CZ  . TYR B 187 ? 0.8131 0.6296 0.6885 0.0436  0.0182  0.0405  192 TYR B CZ  
3460 O OH  . TYR B 187 ? 0.8782 0.6876 0.7226 0.0470  0.0081  0.0343  192 TYR B OH  
3461 N N   . MET B 188 ? 0.7545 0.6500 0.7739 0.0934  0.0627  0.0691  193 MET B N   
3462 C CA  . MET B 188 ? 0.7856 0.7221 0.8492 0.1079  0.0615  0.0745  193 MET B CA  
3463 C C   . MET B 188 ? 0.8292 0.7361 0.8638 0.1330  0.0646  0.0767  193 MET B C   
3464 O O   . MET B 188 ? 0.9130 0.7780 0.9084 0.1435  0.0818  0.0754  193 MET B O   
3465 C CB  . MET B 188 ? 0.8578 0.8310 0.9641 0.1127  0.0836  0.0792  193 MET B CB  
3466 C CG  . MET B 188 ? 0.9316 0.9677 1.1016 0.1234  0.0784  0.0822  193 MET B CG  
3467 S SD  . MET B 188 ? 1.1284 1.2180 1.3651 0.1160  0.1066  0.0852  193 MET B SD  
3468 C CE  . MET B 188 ? 1.1764 1.2717 1.4273 0.0755  0.0955  0.0785  193 MET B CE  
3469 N N   . ALA B 189 ? 0.8057 0.7285 0.8526 0.1439  0.0485  0.0799  194 ALA B N   
3470 C CA  . ALA B 189 ? 0.8194 0.7076 0.8338 0.1713  0.0522  0.0846  194 ALA B CA  
3471 C C   . ALA B 189 ? 0.8616 0.7653 0.8937 0.2020  0.0736  0.0911  194 ALA B C   
3472 O O   . ALA B 189 ? 0.8131 0.7783 0.9036 0.2036  0.0783  0.0935  194 ALA B O   
3473 C CB  . ALA B 189 ? 0.8098 0.7130 0.8300 0.1807  0.0300  0.0888  194 ALA B CB  
3474 N N   . PRO B 190 ? 0.9522 0.7981 0.9345 0.2251  0.0899  0.0932  195 PRO B N   
3475 C CA  . PRO B 190 ? 0.9592 0.8098 0.9492 0.2574  0.1159  0.0993  195 PRO B CA  
3476 C C   . PRO B 190 ? 0.9094 0.8349 0.9644 0.2868  0.1120  0.1093  195 PRO B C   
3477 O O   . PRO B 190 ? 0.9864 0.9551 1.0849 0.2997  0.1320  0.1129  195 PRO B O   
3478 C CB  . PRO B 190 ? 1.0736 0.8367 0.9887 0.2757  0.1297  0.0983  195 PRO B CB  
3479 C CG  . PRO B 190 ? 1.0621 0.7921 0.9473 0.2600  0.1091  0.0960  195 PRO B CG  
3480 C CD  . PRO B 190 ? 1.0086 0.7777 0.9243 0.2214  0.0888  0.0892  195 PRO B CD  
3481 N N   . GLU B 191 ? 0.8377 0.7811 0.9001 0.2971  0.0866  0.1132  196 GLU B N   
3482 C CA  . GLU B 191 ? 0.8647 0.8914 0.9929 0.3233  0.0722  0.1198  196 GLU B CA  
3483 C C   . GLU B 191 ? 0.8510 0.9695 1.0667 0.3006  0.0680  0.1143  196 GLU B C   
3484 O O   . GLU B 191 ? 0.9519 1.1446 1.2327 0.3236  0.0685  0.1181  196 GLU B O   
3485 C CB  . GLU B 191 ? 0.8639 0.8901 0.9743 0.3354  0.0402  0.1232  196 GLU B CB  
3486 C CG  . GLU B 191 ? 0.8469 0.8662 0.9463 0.2950  0.0157  0.1146  196 GLU B CG  
3487 C CD  . GLU B 191 ? 0.9172 0.8414 0.9358 0.2814  0.0218  0.1137  196 GLU B CD  
3488 O OE1 . GLU B 191 ? 0.9295 0.8396 0.9264 0.2677  0.0025  0.1123  196 GLU B OE1 
3489 O OE2 . GLU B 191 ? 0.9685 0.8310 0.9448 0.2823  0.0470  0.1131  196 GLU B OE2 
3490 N N   . HIS B 192 ? 0.8370 0.9484 1.0539 0.2570  0.0665  0.1055  197 HIS B N   
3491 C CA  . HIS B 192 ? 0.8053 0.9851 1.0946 0.2294  0.0690  0.0998  197 HIS B CA  
3492 C C   . HIS B 192 ? 0.8493 1.0222 1.1479 0.2250  0.1087  0.1021  197 HIS B C   
3493 O O   . HIS B 192 ? 0.8477 1.0833 1.2161 0.2121  0.1209  0.1009  197 HIS B O   
3494 C CB  . HIS B 192 ? 0.7640 0.9350 1.0448 0.1888  0.0471  0.0905  197 HIS B CB  
3495 C CG  . HIS B 192 ? 0.7384 0.9136 1.0058 0.1932  0.0113  0.0883  197 HIS B CG  
3496 N ND1 . HIS B 192 ? 0.8348 1.0756 1.1486 0.2142  -0.0112 0.0884  197 HIS B ND1 
3497 C CD2 . HIS B 192 ? 0.7257 0.8471 0.9353 0.1830  -0.0045 0.0864  197 HIS B CD2 
3498 C CE1 . HIS B 192 ? 0.8892 1.1100 1.1660 0.2176  -0.0399 0.0872  197 HIS B CE1 
3499 N NE2 . HIS B 192 ? 0.7737 0.9214 0.9885 0.1978  -0.0337 0.0865  197 HIS B NE2 
3500 N N   . LEU B 193 ? 0.8851 0.9806 1.1122 0.2347  0.1297  0.1045  198 LEU B N   
3501 C CA  . LEU B 193 ? 0.9425 1.0205 1.1618 0.2405  0.1693  0.1079  198 LEU B CA  
3502 C C   . LEU B 193 ? 0.9970 1.1259 1.2680 0.2772  0.1932  0.1166  198 LEU B C   
3503 O O   . LEU B 193 ? 1.0030 1.1248 1.2603 0.3131  0.1883  0.1216  198 LEU B O   
3504 C CB  . LEU B 193 ? 0.9805 0.9626 1.1048 0.2457  0.1805  0.1052  198 LEU B CB  
3505 C CG  . LEU B 193 ? 0.9462 0.8792 1.0189 0.2131  0.1619  0.0961  198 LEU B CG  
3506 C CD1 . LEU B 193 ? 0.9885 0.8363 0.9755 0.2207  0.1685  0.0901  198 LEU B CD1 
3507 C CD2 . LEU B 193 ? 0.9502 0.8977 1.0392 0.1867  0.1722  0.0951  198 LEU B CD2 
3508 N N   . ASN B 194 ? 0.9961 1.1748 1.3262 0.2690  0.2211  0.1191  199 ASN B N   
3509 C CA  . ASN B 194 ? 1.1197 1.3682 1.5219 0.2992  0.2466  0.1268  199 ASN B CA  
3510 C C   . ASN B 194 ? 1.1716 1.5123 1.6526 0.3172  0.2156  0.1266  199 ASN B C   
3511 O O   . ASN B 194 ? 1.3325 1.7245 1.8605 0.3557  0.2312  0.1340  199 ASN B O   
3512 C CB  . ASN B 194 ? 1.2725 1.4601 1.6146 0.3415  0.2826  0.1349  199 ASN B CB  
3513 C CG  . ASN B 194 ? 1.3325 1.4504 1.6132 0.3297  0.3194  0.1349  199 ASN B CG  
3514 O OD1 . ASN B 194 ? 1.3066 1.4289 1.5985 0.2943  0.3256  0.1324  199 ASN B OD1 
3515 N ND2 . ASN B 194 ? 1.3506 1.3977 1.5588 0.3626  0.3451  0.1380  199 ASN B ND2 
3516 N N   . ASP B 195 ? 1.2010 1.5652 1.6961 0.2923  0.1720  0.1181  200 ASP B N   
3517 C CA  . ASP B 195 ? 1.2559 1.7054 1.8160 0.3093  0.1357  0.1157  200 ASP B CA  
3518 C C   . ASP B 195 ? 1.3219 1.8201 1.9288 0.2634  0.1024  0.1018  200 ASP B C   
3519 O O   . ASP B 195 ? 1.4068 1.8653 1.9640 0.2489  0.0698  0.0964  200 ASP B O   
3520 C CB  . ASP B 195 ? 1.1772 1.5783 1.6697 0.3494  0.1125  0.1223  200 ASP B CB  
3521 C CG  . ASP B 195 ? 1.2527 1.7377 1.8046 0.3914  0.0909  0.1264  200 ASP B CG  
3522 O OD1 . ASP B 195 ? 1.2643 1.8110 1.8790 0.4195  0.1155  0.1324  200 ASP B OD1 
3523 O OD2 . ASP B 195 ? 1.2522 1.7433 1.7872 0.4000  0.0499  0.1244  200 ASP B OD2 
3524 N N   . VAL B 196 ? 1.3329 1.9117 2.0334 0.2388  0.1158  0.0955  201 VAL B N   
3525 C CA  . VAL B 196 ? 1.2922 1.9246 2.0489 0.1931  0.0876  0.0792  201 VAL B CA  
3526 C C   . VAL B 196 ? 1.2659 1.9652 2.0567 0.2062  0.0334  0.0699  201 VAL B C   
3527 O O   . VAL B 196 ? 1.2299 1.9359 2.0233 0.1720  0.0016  0.0557  201 VAL B O   
3528 C CB  . VAL B 196 ? 1.2854 1.9876 2.1398 0.1593  0.1194  0.0731  201 VAL B CB  
3529 C CG1 . VAL B 196 ? 1.2788 1.9018 2.0834 0.1419  0.1700  0.0819  201 VAL B CG1 
3530 C CG2 . VAL B 196 ? 1.2372 2.0482 2.1945 0.1884  0.1316  0.0755  201 VAL B CG2 
3531 N N   . ASN B 197 ? 1.2430 1.9875 2.0545 0.2580  0.0242  0.0780  202 ASN B N   
3532 C CA  . ASN B 197 ? 1.2645 2.0754 2.1036 0.2806  -0.0283 0.0711  202 ASN B CA  
3533 C C   . ASN B 197 ? 1.3745 2.1031 2.1088 0.2927  -0.0623 0.0737  202 ASN B C   
3534 O O   . ASN B 197 ? 1.4761 2.2466 2.2208 0.2965  -0.1089 0.0641  202 ASN B O   
3535 C CB  . ASN B 197 ? 1.1832 2.0683 2.0751 0.3396  -0.0255 0.0815  202 ASN B CB  
3536 C CG  . ASN B 197 ? 1.2199 2.2125 2.2379 0.3265  0.0044  0.0764  202 ASN B CG  
3537 O OD1 . ASN B 197 ? 1.1903 2.2186 2.2688 0.2712  0.0133  0.0620  202 ASN B OD1 
3538 N ND2 . ASN B 197 ? 1.2441 2.2822 2.2986 0.3800  0.0251  0.0898  202 ASN B ND2 
3539 N N   . ALA B 198 ? 1.3822 1.9967 2.0176 0.2983  -0.0391 0.0855  203 ALA B N   
3540 C CA  . ALA B 198 ? 1.2869 1.8188 1.8236 0.3112  -0.0625 0.0901  203 ALA B CA  
3541 C C   . ALA B 198 ? 1.1572 1.6747 1.6762 0.2662  -0.0913 0.0756  203 ALA B C   
3542 O O   . ALA B 198 ? 1.0010 1.4873 1.5152 0.2225  -0.0740 0.0692  203 ALA B O   
3543 C CB  . ALA B 198 ? 1.2737 1.6942 1.7206 0.3210  -0.0285 0.1025  203 ALA B CB  
3544 N N   . LYS B 199 ? 1.1172 1.6495 1.6168 0.2817  -0.1334 0.0718  204 LYS B N   
3545 C CA  . LYS B 199 ? 1.0132 1.5318 1.4904 0.2457  -0.1629 0.0574  204 LYS B CA  
3546 C C   . LYS B 199 ? 1.0239 1.4275 1.3998 0.2371  -0.1486 0.0656  204 LYS B C   
3547 O O   . LYS B 199 ? 1.0519 1.3990 1.3620 0.2730  -0.1455 0.0797  204 LYS B O   
3548 C CB  . LYS B 199 ? 0.9868 1.5577 1.4690 0.2711  -0.2129 0.0506  204 LYS B CB  
3549 C CG  . LYS B 199 ? 1.0360 1.6107 1.5075 0.2359  -0.2470 0.0316  204 LYS B CG  
3550 C CD  . LYS B 199 ? 1.0746 1.7050 1.5474 0.2679  -0.2988 0.0243  204 LYS B CD  
3551 C CE  . LYS B 199 ? 1.0791 1.7112 1.5373 0.2316  -0.3337 0.0019  204 LYS B CE  
3552 N NZ  . LYS B 199 ? 1.1273 1.8143 1.5804 0.2647  -0.3884 -0.0073 204 LYS B NZ  
3553 N N   . PRO B 200 ? 1.0145 1.3826 1.3787 0.1907  -0.1378 0.0571  205 PRO B N   
3554 C CA  . PRO B 200 ? 1.0153 1.2877 1.2945 0.1813  -0.1268 0.0630  205 PRO B CA  
3555 C C   . PRO B 200 ? 0.9996 1.2371 1.2167 0.1957  -0.1542 0.0641  205 PRO B C   
3556 O O   . PRO B 200 ? 1.0132 1.2974 1.2490 0.1983  -0.1879 0.0545  205 PRO B O   
3557 C CB  . PRO B 200 ? 1.0120 1.2749 1.3056 0.1333  -0.1159 0.0522  205 PRO B CB  
3558 C CG  . PRO B 200 ? 0.9773 1.3070 1.3523 0.1205  -0.1027 0.0468  205 PRO B CG  
3559 C CD  . PRO B 200 ? 1.0104 1.4198 1.4383 0.1465  -0.1290 0.0435  205 PRO B CD  
3560 N N   . THR B 201 ? 0.9705 1.1260 1.1140 0.2049  -0.1381 0.0752  206 THR B N   
3561 C CA  . THR B 201 ? 1.0545 1.1595 1.1274 0.2202  -0.1528 0.0804  206 THR B CA  
3562 C C   . THR B 201 ? 1.0532 1.0917 1.0811 0.1888  -0.1354 0.0791  206 THR B C   
3563 O O   . THR B 201 ? 1.0733 1.1068 1.1222 0.1616  -0.1155 0.0751  206 THR B O   
3564 C CB  . THR B 201 ? 1.0653 1.1282 1.0893 0.2669  -0.1439 0.0978  206 THR B CB  
3565 O OG1 . THR B 201 ? 1.0315 1.0328 1.0281 0.2614  -0.1079 0.1050  206 THR B OG1 
3566 C CG2 . THR B 201 ? 1.0520 1.1851 1.1244 0.3057  -0.1580 0.1013  206 THR B CG2 
3567 N N   . GLU B 202 ? 1.0670 1.0553 1.0319 0.1957  -0.1416 0.0833  207 GLU B N   
3568 C CA  . GLU B 202 ? 0.9638 0.8881 0.8853 0.1717  -0.1210 0.0845  207 GLU B CA  
3569 C C   . GLU B 202 ? 0.9686 0.8523 0.8812 0.1670  -0.0894 0.0906  207 GLU B C   
3570 O O   . GLU B 202 ? 1.1761 1.0446 1.0933 0.1378  -0.0750 0.0851  207 GLU B O   
3571 C CB  . GLU B 202 ? 1.0458 0.9157 0.8958 0.1873  -0.1247 0.0921  207 GLU B CB  
3572 C CG  . GLU B 202 ? 1.0561 0.9500 0.8956 0.1896  -0.1556 0.0839  207 GLU B CG  
3573 C CD  . GLU B 202 ? 1.0895 0.9211 0.8487 0.2058  -0.1544 0.0926  207 GLU B CD  
3574 O OE1 . GLU B 202 ? 1.1229 0.8897 0.8350 0.2144  -0.1266 0.1064  207 GLU B OE1 
3575 O OE2 . GLU B 202 ? 1.1112 0.9547 0.8504 0.2094  -0.1799 0.0848  207 GLU B OE2 
3576 N N   . LYS B 203 ? 1.0138 0.8821 0.9135 0.1974  -0.0803 0.1005  208 LYS B N   
3577 C CA  . LYS B 203 ? 1.0173 0.8387 0.8994 0.1950  -0.0513 0.1040  208 LYS B CA  
3578 C C   . LYS B 203 ? 0.9642 0.8191 0.8944 0.1763  -0.0415 0.0959  208 LYS B C   
3579 O O   . LYS B 203 ? 0.9642 0.7804 0.8773 0.1618  -0.0214 0.0931  208 LYS B O   
3580 C CB  . LYS B 203 ? 1.1264 0.9131 0.9736 0.2368  -0.0421 0.1171  208 LYS B CB  
3581 C CG  . LYS B 203 ? 1.2186 0.9547 1.0022 0.2611  -0.0456 0.1288  208 LYS B CG  
3582 C CD  . LYS B 203 ? 1.2288 0.8963 0.9643 0.2338  -0.0271 0.1285  208 LYS B CD  
3583 C CE  . LYS B 203 ? 1.3115 0.9181 0.9757 0.2607  -0.0231 0.1429  208 LYS B CE  
3584 N NZ  . LYS B 203 ? 1.5235 1.0677 1.1398 0.2961  -0.0025 0.1569  208 LYS B NZ  
3585 N N   . SER B 204 ? 0.8672 0.7914 0.8547 0.1759  -0.0549 0.0913  209 SER B N   
3586 C CA  . SER B 204 ? 0.7915 0.7451 0.8217 0.1546  -0.0435 0.0844  209 SER B CA  
3587 C C   . SER B 204 ? 0.7289 0.6589 0.7468 0.1198  -0.0381 0.0770  209 SER B C   
3588 O O   . SER B 204 ? 0.8162 0.7269 0.8285 0.1092  -0.0210 0.0747  209 SER B O   
3589 C CB  . SER B 204 ? 0.8233 0.8536 0.9191 0.1518  -0.0578 0.0792  209 SER B CB  
3590 O OG  . SER B 204 ? 0.9122 0.9799 1.0281 0.1856  -0.0696 0.0846  209 SER B OG  
3591 N N   . ASP B 205 ? 0.6594 0.5910 0.6700 0.1056  -0.0534 0.0733  210 ASP B N   
3592 C CA  . ASP B 205 ? 0.6927 0.6037 0.6908 0.0779  -0.0488 0.0676  210 ASP B CA  
3593 C C   . ASP B 205 ? 0.7555 0.6133 0.7118 0.0735  -0.0347 0.0692  210 ASP B C   
3594 O O   . ASP B 205 ? 0.7920 0.6407 0.7469 0.0543  -0.0275 0.0639  210 ASP B O   
3595 C CB  . ASP B 205 ? 0.7259 0.6463 0.7211 0.0675  -0.0658 0.0633  210 ASP B CB  
3596 C CG  . ASP B 205 ? 0.7746 0.7470 0.8134 0.0625  -0.0817 0.0564  210 ASP B CG  
3597 O OD1 . ASP B 205 ? 0.6965 0.6982 0.7750 0.0565  -0.0732 0.0546  210 ASP B OD1 
3598 O OD2 . ASP B 205 ? 0.7989 0.7807 0.8302 0.0635  -0.1017 0.0519  210 ASP B OD2 
3599 N N   . VAL B 206 ? 0.7928 0.6157 0.7152 0.0914  -0.0309 0.0760  211 VAL B N   
3600 C CA  . VAL B 206 ? 0.8061 0.5740 0.6908 0.0841  -0.0138 0.0761  211 VAL B CA  
3601 C C   . VAL B 206 ? 0.7902 0.5449 0.6762 0.0790  -0.0001 0.0706  211 VAL B C   
3602 O O   . VAL B 206 ? 0.7419 0.4765 0.6184 0.0576  0.0074  0.0626  211 VAL B O   
3603 C CB  . VAL B 206 ? 0.9059 0.6285 0.7466 0.1062  -0.0084 0.0864  211 VAL B CB  
3604 C CG1 . VAL B 206 ? 0.9587 0.6174 0.7620 0.0955  0.0149  0.0853  211 VAL B CG1 
3605 C CG2 . VAL B 206 ? 0.9500 0.6765 0.7770 0.1081  -0.0209 0.0901  211 VAL B CG2 
3606 N N   . TYR B 207 ? 0.7927 0.5613 0.6908 0.0993  0.0028  0.0739  212 TYR B N   
3607 C CA  . TYR B 207 ? 0.8001 0.5570 0.6956 0.0974  0.0164  0.0682  212 TYR B CA  
3608 C C   . TYR B 207 ? 0.7554 0.5348 0.6687 0.0731  0.0129  0.0594  212 TYR B C   
3609 O O   . TYR B 207 ? 0.8050 0.5593 0.6985 0.0601  0.0187  0.0507  212 TYR B O   
3610 C CB  . TYR B 207 ? 0.8046 0.5856 0.7200 0.1242  0.0222  0.0743  212 TYR B CB  
3611 C CG  . TYR B 207 ? 0.8607 0.6167 0.7595 0.1258  0.0401  0.0689  212 TYR B CG  
3612 C CD1 . TYR B 207 ? 0.8357 0.6154 0.7522 0.1122  0.0426  0.0635  212 TYR B CD1 
3613 C CD2 . TYR B 207 ? 0.9613 0.6605 0.8171 0.1413  0.0561  0.0688  212 TYR B CD2 
3614 C CE1 . TYR B 207 ? 0.9357 0.6867 0.8258 0.1160  0.0584  0.0581  212 TYR B CE1 
3615 C CE2 . TYR B 207 ? 1.0432 0.7123 0.8745 0.1426  0.0719  0.0613  212 TYR B CE2 
3616 C CZ  . TYR B 207 ? 1.0038 0.7002 0.8511 0.1304  0.0719  0.0557  212 TYR B CZ  
3617 O OH  . TYR B 207 ? 1.0668 0.7290 0.8800 0.1345  0.0869  0.0481  212 TYR B OH  
3618 N N   . SER B 208 ? 0.6827 0.5076 0.6310 0.0685  0.0028  0.0612  213 SER B N   
3619 C CA  . SER B 208 ? 0.6684 0.5107 0.6295 0.0508  0.0012  0.0559  213 SER B CA  
3620 C C   . SER B 208 ? 0.6341 0.4588 0.5775 0.0324  -0.0032 0.0493  213 SER B C   
3621 O O   . SER B 208 ? 0.6803 0.4995 0.6146 0.0240  -0.0014 0.0426  213 SER B O   
3622 C CB  . SER B 208 ? 0.6722 0.5558 0.6693 0.0468  -0.0071 0.0585  213 SER B CB  
3623 O OG  . SER B 208 ? 0.6154 0.5274 0.6407 0.0617  -0.0057 0.0630  213 SER B OG  
3624 N N   . PHE B 209 ? 0.6503 0.4673 0.5880 0.0283  -0.0084 0.0511  214 PHE B N   
3625 C CA  . PHE B 209 ? 0.7333 0.5367 0.6605 0.0111  -0.0080 0.0454  214 PHE B CA  
3626 C C   . PHE B 209 ? 0.7739 0.5485 0.6820 0.0021  -0.0001 0.0362  214 PHE B C   
3627 O O   . PHE B 209 ? 0.7506 0.5344 0.6641 -0.0135 -0.0034 0.0270  214 PHE B O   
3628 C CB  . PHE B 209 ? 0.7679 0.5582 0.6843 0.0120  -0.0083 0.0511  214 PHE B CB  
3629 C CG  . PHE B 209 ? 0.8004 0.5741 0.7087 -0.0054 -0.0005 0.0465  214 PHE B CG  
3630 C CD1 . PHE B 209 ? 0.7484 0.5475 0.6746 -0.0173 -0.0041 0.0428  214 PHE B CD1 
3631 C CD2 . PHE B 209 ? 0.8609 0.5920 0.7446 -0.0095 0.0135  0.0463  214 PHE B CD2 
3632 C CE1 . PHE B 209 ? 0.7482 0.5419 0.6770 -0.0332 0.0052  0.0384  214 PHE B CE1 
3633 C CE2 . PHE B 209 ? 0.8317 0.5517 0.7163 -0.0302 0.0245  0.0410  214 PHE B CE2 
3634 C CZ  . PHE B 209 ? 0.7684 0.5253 0.6799 -0.0419 0.0198  0.0369  214 PHE B CZ  
3635 N N   . ALA B 210 ? 0.8416 0.5825 0.7275 0.0130  0.0093  0.0375  215 ALA B N   
3636 C CA  . ALA B 210 ? 0.8828 0.5875 0.7444 0.0033  0.0174  0.0258  215 ALA B CA  
3637 C C   . ALA B 210 ? 0.8901 0.6111 0.7532 -0.0017 0.0109  0.0151  215 ALA B C   
3638 O O   . ALA B 210 ? 0.8134 0.5274 0.6690 -0.0198 0.0069  0.0003  215 ALA B O   
3639 C CB  . ALA B 210 ? 0.8860 0.5464 0.7179 0.0222  0.0310  0.0304  215 ALA B CB  
3640 N N   . VAL B 211 ? 0.8337 0.5771 0.7062 0.0145  0.0100  0.0220  216 VAL B N   
3641 C CA  . VAL B 211 ? 0.8211 0.5712 0.6837 0.0160  0.0076  0.0154  216 VAL B CA  
3642 C C   . VAL B 211 ? 0.8132 0.5970 0.6929 0.0049  -0.0060 0.0125  216 VAL B C   
3643 O O   . VAL B 211 ? 0.9923 0.7778 0.8570 0.0010  -0.0139 0.0021  216 VAL B O   
3644 C CB  . VAL B 211 ? 0.8004 0.5562 0.6645 0.0372  0.0190  0.0250  216 VAL B CB  
3645 C CG1 . VAL B 211 ? 0.8350 0.5808 0.6715 0.0415  0.0213  0.0183  216 VAL B CG1 
3646 C CG2 . VAL B 211 ? 0.7690 0.4989 0.6224 0.0544  0.0329  0.0301  216 VAL B CG2 
3647 N N   . VAL B 212 ? 0.7738 0.5824 0.6803 0.0022  -0.0095 0.0210  217 VAL B N   
3648 C CA  . VAL B 212 ? 0.6963 0.5323 0.6176 -0.0056 -0.0196 0.0193  217 VAL B CA  
3649 C C   . VAL B 212 ? 0.7893 0.6272 0.7120 -0.0225 -0.0265 0.0063  217 VAL B C   
3650 O O   . VAL B 212 ? 0.8185 0.6792 0.7453 -0.0250 -0.0375 -0.0011 217 VAL B O   
3651 C CB  . VAL B 212 ? 0.6837 0.5359 0.6266 -0.0052 -0.0195 0.0294  217 VAL B CB  
3652 C CG1 . VAL B 212 ? 0.7559 0.6295 0.7105 -0.0108 -0.0262 0.0279  217 VAL B CG1 
3653 C CG2 . VAL B 212 ? 0.6701 0.5295 0.6206 0.0055  -0.0146 0.0382  217 VAL B CG2 
3654 N N   . LEU B 213 ? 0.8490 0.6640 0.7692 -0.0332 -0.0190 0.0036  218 LEU B N   
3655 C CA  . LEU B 213 ? 0.7977 0.6100 0.7229 -0.0552 -0.0202 -0.0109 218 LEU B CA  
3656 C C   . LEU B 213 ? 0.8022 0.6121 0.7121 -0.0612 -0.0304 -0.0283 218 LEU B C   
3657 O O   . LEU B 213 ? 0.7821 0.6224 0.7093 -0.0746 -0.0433 -0.0418 218 LEU B O   
3658 C CB  . LEU B 213 ? 0.9447 0.7145 0.8570 -0.0644 -0.0039 -0.0097 218 LEU B CB  
3659 C CG  . LEU B 213 ? 1.0497 0.8221 0.9772 -0.0731 0.0056  -0.0026 218 LEU B CG  
3660 C CD1 . LEU B 213 ? 1.2345 0.9511 1.1336 -0.0733 0.0245  0.0032  218 LEU B CD1 
3661 C CD2 . LEU B 213 ? 1.0246 0.8263 0.9818 -0.0974 0.0037  -0.0160 218 LEU B CD2 
3662 N N   . TRP B 214 ? 0.8403 0.6165 0.7175 -0.0491 -0.0253 -0.0285 219 TRP B N   
3663 C CA  . TRP B 214 ? 0.8551 0.6192 0.7038 -0.0503 -0.0347 -0.0453 219 TRP B CA  
3664 C C   . TRP B 214 ? 0.8077 0.6116 0.6592 -0.0398 -0.0526 -0.0467 219 TRP B C   
3665 O O   . TRP B 214 ? 0.7726 0.5940 0.6211 -0.0497 -0.0709 -0.0650 219 TRP B O   
3666 C CB  . TRP B 214 ? 0.9105 0.6279 0.7197 -0.0329 -0.0205 -0.0416 219 TRP B CB  
3667 C CG  . TRP B 214 ? 0.9863 0.6790 0.7545 -0.0345 -0.0281 -0.0610 219 TRP B CG  
3668 C CD1 . TRP B 214 ? 0.9935 0.6455 0.7358 -0.0530 -0.0273 -0.0817 219 TRP B CD1 
3669 C CD2 . TRP B 214 ? 0.9573 0.6596 0.6997 -0.0178 -0.0379 -0.0631 219 TRP B CD2 
3670 N NE1 . TRP B 214 ? 1.0448 0.6824 0.7458 -0.0487 -0.0391 -0.0986 219 TRP B NE1 
3671 C CE2 . TRP B 214 ? 1.0265 0.6943 0.7245 -0.0251 -0.0456 -0.0864 219 TRP B CE2 
3672 C CE3 . TRP B 214 ? 0.9449 0.6748 0.6917 0.0028  -0.0390 -0.0476 219 TRP B CE3 
3673 C CZ2 . TRP B 214 ? 1.0567 0.7188 0.7102 -0.0088 -0.0566 -0.0940 219 TRP B CZ2 
3674 C CZ3 . TRP B 214 ? 0.9665 0.6871 0.6697 0.0191  -0.0457 -0.0527 219 TRP B CZ3 
3675 C CH2 . TRP B 214 ? 1.0255 0.7139 0.6811 0.0148  -0.0557 -0.0755 219 TRP B CH2 
3676 N N   . ALA B 215 ? 0.7606 0.5768 0.6164 -0.0197 -0.0473 -0.0282 220 ALA B N   
3677 C CA  . ALA B 215 ? 0.7897 0.6321 0.6404 -0.0045 -0.0582 -0.0242 220 ALA B CA  
3678 C C   . ALA B 215 ? 0.8205 0.7075 0.6992 -0.0123 -0.0764 -0.0315 220 ALA B C   
3679 O O   . ALA B 215 ? 0.8539 0.7601 0.7183 -0.0027 -0.0942 -0.0395 220 ALA B O   
3680 C CB  . ALA B 215 ? 0.7982 0.6415 0.6562 0.0110  -0.0440 -0.0033 220 ALA B CB  
3681 N N   . ILE B 216 ? 0.7948 0.6984 0.7111 -0.0263 -0.0713 -0.0281 221 ILE B N   
3682 C CA  . ILE B 216 ? 0.7639 0.7138 0.7160 -0.0338 -0.0827 -0.0338 221 ILE B CA  
3683 C C   . ILE B 216 ? 0.7599 0.7347 0.7194 -0.0489 -0.1025 -0.0578 221 ILE B C   
3684 O O   . ILE B 216 ? 0.7063 0.7266 0.6809 -0.0404 -0.1210 -0.0635 221 ILE B O   
3685 C CB  . ILE B 216 ? 0.7504 0.7032 0.7342 -0.0471 -0.0675 -0.0261 221 ILE B CB  
3686 C CG1 . ILE B 216 ? 0.7416 0.6865 0.7217 -0.0299 -0.0575 -0.0063 221 ILE B CG1 
3687 C CG2 . ILE B 216 ? 0.8109 0.8109 0.8364 -0.0589 -0.0735 -0.0345 221 ILE B CG2 
3688 C CD1 . ILE B 216 ? 0.7789 0.7059 0.7675 -0.0378 -0.0423 0.0022  221 ILE B CD1 
3689 N N   . PHE B 217 ? 0.8190 0.7627 0.7658 -0.0694 -0.0991 -0.0725 222 PHE B N   
3690 C CA  . PHE B 217 ? 0.8959 0.8576 0.8492 -0.0911 -0.1181 -0.1005 222 PHE B CA  
3691 C C   . PHE B 217 ? 1.0107 0.9561 0.9138 -0.0782 -0.1370 -0.1138 222 PHE B C   
3692 O O   . PHE B 217 ? 0.9917 0.9713 0.8995 -0.0863 -0.1640 -0.1368 222 PHE B O   
3693 C CB  . PHE B 217 ? 0.9515 0.8807 0.9154 -0.1247 -0.1014 -0.1117 222 PHE B CB  
3694 C CG  . PHE B 217 ? 0.9334 0.8895 0.9485 -0.1411 -0.0870 -0.1051 222 PHE B CG  
3695 C CD1 . PHE B 217 ? 0.9266 0.9451 0.9941 -0.1598 -0.0997 -0.1208 222 PHE B CD1 
3696 C CD2 . PHE B 217 ? 0.8686 0.7925 0.8798 -0.1348 -0.0616 -0.0830 222 PHE B CD2 
3697 C CE1 . PHE B 217 ? 0.9042 0.9473 1.0186 -0.1732 -0.0815 -0.1135 222 PHE B CE1 
3698 C CE2 . PHE B 217 ? 0.8058 0.7490 0.8549 -0.1470 -0.0463 -0.0762 222 PHE B CE2 
3699 C CZ  . PHE B 217 ? 0.8224 0.8230 0.9229 -0.1664 -0.0535 -0.0908 222 PHE B CZ  
3700 N N   . ALA B 218 ? 1.0272 0.9228 0.8825 -0.0575 -0.1231 -0.1004 223 ALA B N   
3701 C CA  . ALA B 218 ? 1.0480 0.9229 0.8465 -0.0366 -0.1352 -0.1066 223 ALA B CA  
3702 C C   . ALA B 218 ? 1.0154 0.9279 0.8057 -0.0080 -0.1530 -0.0983 223 ALA B C   
3703 O O   . ALA B 218 ? 1.1416 1.0517 0.8887 0.0057  -0.1733 -0.1108 223 ALA B O   
3704 C CB  . ALA B 218 ? 1.0744 0.8897 0.8310 -0.0207 -0.1089 -0.0918 223 ALA B CB  
3705 N N   . ASN B 219 ? 0.9587 0.8981 0.7820 0.0032  -0.1444 -0.0772 224 ASN B N   
3706 C CA  . ASN B 219 ? 1.0042 0.9601 0.8100 0.0362  -0.1508 -0.0618 224 ASN B CA  
3707 C C   . ASN B 219 ? 1.0683 0.9740 0.8099 0.0630  -0.1372 -0.0486 224 ASN B C   
3708 O O   . ASN B 219 ? 1.0903 0.9961 0.7921 0.0913  -0.1478 -0.0439 224 ASN B O   
3709 C CB  . ASN B 219 ? 1.0312 1.0429 0.8469 0.0439  -0.1854 -0.0777 224 ASN B CB  
3710 C CG  . ASN B 219 ? 1.0920 1.1612 0.9801 0.0181  -0.1939 -0.0892 224 ASN B CG  
3711 O OD1 . ASN B 219 ? 1.2884 1.3622 1.2145 0.0103  -0.1735 -0.0748 224 ASN B OD1 
3712 N ND2 . ASN B 219 ? 1.2649 1.3790 1.1726 0.0038  -0.2235 -0.1163 224 ASN B ND2 
3713 N N   . LYS B 220 ? 1.0855 0.9484 0.8176 0.0560  -0.1114 -0.0413 225 LYS B N   
3714 C CA  . LYS B 220 ? 1.1291 0.9453 0.8089 0.0776  -0.0911 -0.0289 225 LYS B CA  
3715 C C   . LYS B 220 ? 1.0180 0.8085 0.7159 0.0686  -0.0613 -0.0176 225 LYS B C   
3716 O O   . LYS B 220 ? 0.8831 0.6820 0.6192 0.0475  -0.0598 -0.0223 225 LYS B O   
3717 C CB  . LYS B 220 ? 1.1999 0.9878 0.8161 0.0870  -0.1044 -0.0469 225 LYS B CB  
3718 C CG  . LYS B 220 ? 1.2051 0.9760 0.8204 0.0621  -0.1098 -0.0703 225 LYS B CG  
3719 C CD  . LYS B 220 ? 1.2324 0.9711 0.7768 0.0719  -0.1253 -0.0908 225 LYS B CD  
3720 C CE  . LYS B 220 ? 1.2261 0.9415 0.7670 0.0443  -0.1302 -0.1166 225 LYS B CE  
3721 N NZ  . LYS B 220 ? 1.3085 0.9993 0.7821 0.0488  -0.1542 -0.1436 225 LYS B NZ  
3722 N N   . GLU B 221 ? 1.0539 0.8137 0.7233 0.0868  -0.0368 -0.0021 226 GLU B N   
3723 C CA  . GLU B 221 ? 1.0073 0.7483 0.6925 0.0840  -0.0086 0.0080  226 GLU B CA  
3724 C C   . GLU B 221 ? 1.0321 0.7409 0.6861 0.0817  -0.0072 -0.0074 226 GLU B C   
3725 O O   . GLU B 221 ? 1.2000 0.8877 0.8018 0.0893  -0.0197 -0.0216 226 GLU B O   
3726 C CB  . GLU B 221 ? 1.0575 0.7789 0.7245 0.1027  0.0200  0.0274  226 GLU B CB  
3727 C CG  . GLU B 221 ? 1.1252 0.8642 0.8171 0.1037  0.0255  0.0430  226 GLU B CG  
3728 C CD  . GLU B 221 ? 1.2428 1.0079 0.9988 0.0855  0.0327  0.0498  226 GLU B CD  
3729 O OE1 . GLU B 221 ? 1.3660 1.1376 1.1490 0.0761  0.0365  0.0464  226 GLU B OE1 
3730 O OE2 . GLU B 221 ? 1.3614 1.1372 1.1364 0.0828  0.0348  0.0587  226 GLU B OE2 
3731 N N   . PRO B 222 ? 1.0017 0.7030 0.6819 0.0734  0.0070  -0.0055 227 PRO B N   
3732 C CA  . PRO B 222 ? 0.9818 0.6421 0.6270 0.0746  0.0137  -0.0183 227 PRO B CA  
3733 C C   . PRO B 222 ? 1.0172 0.6399 0.6165 0.0992  0.0399  -0.0117 227 PRO B C   
3734 O O   . PRO B 222 ? 1.0644 0.6951 0.6670 0.1136  0.0577  0.0054  227 PRO B O   
3735 C CB  . PRO B 222 ? 0.9596 0.6253 0.6481 0.0644  0.0226  -0.0131 227 PRO B CB  
3736 C CG  . PRO B 222 ? 0.9048 0.6068 0.6402 0.0690  0.0323  0.0072  227 PRO B CG  
3737 C CD  . PRO B 222 ? 0.9496 0.6765 0.6874 0.0653  0.0163  0.0078  227 PRO B CD  
3738 N N   . TYR B 223 ? 1.0415 0.6193 0.5979 0.1026  0.0453  -0.0257 228 TYR B N   
3739 C CA  . TYR B 223 ? 1.1275 0.6622 0.6389 0.1273  0.0754  -0.0208 228 TYR B CA  
3740 C C   . TYR B 223 ? 1.2207 0.7326 0.6703 0.1473  0.0809  -0.0196 228 TYR B C   
3741 O O   . TYR B 223 ? 1.3576 0.8476 0.7859 0.1699  0.1146  -0.0060 228 TYR B O   
3742 C CB  . TYR B 223 ? 1.0563 0.6114 0.6190 0.1389  0.1059  0.0015  228 TYR B CB  
3743 C CG  . TYR B 223 ? 0.9979 0.5735 0.6135 0.1266  0.1008  0.0035  228 TYR B CG  
3744 C CD1 . TYR B 223 ? 1.0416 0.5754 0.6324 0.1262  0.1030  -0.0082 228 TYR B CD1 
3745 C CD2 . TYR B 223 ? 0.9012 0.5299 0.5842 0.1180  0.0965  0.0176  228 TYR B CD2 
3746 C CE1 . TYR B 223 ? 1.0342 0.5787 0.6641 0.1203  0.1015  -0.0032 228 TYR B CE1 
3747 C CE2 . TYR B 223 ? 0.8897 0.5334 0.6118 0.1115  0.0915  0.0205  228 TYR B CE2 
3748 C CZ  . TYR B 223 ? 0.9427 0.5443 0.6377 0.1143  0.0946  0.0117  228 TYR B CZ  
3749 O OH  . TYR B 223 ? 0.8850 0.4950 0.6103 0.1122  0.0917  0.0173  228 TYR B OH  
3750 N N   . GLU B 224 ? 1.2578 0.7750 0.6773 0.1411  0.0490  -0.0336 229 GLU B N   
3751 C CA  . GLU B 224 ? 1.3069 0.7995 0.6557 0.1638  0.0478  -0.0332 229 GLU B CA  
3752 C C   . GLU B 224 ? 1.3513 0.7773 0.6167 0.1871  0.0707  -0.0394 229 GLU B C   
3753 O O   . GLU B 224 ? 1.3910 0.7920 0.6112 0.2131  0.0953  -0.0246 229 GLU B O   
3754 C CB  . GLU B 224 ? 1.3257 0.8407 0.6569 0.1549  0.0017  -0.0523 229 GLU B CB  
3755 C CG  . GLU B 224 ? 1.3997 0.9076 0.7197 0.1313  -0.0294 -0.0854 229 GLU B CG  
3756 C CD  . GLU B 224 ? 1.4867 1.0228 0.7859 0.1274  -0.0750 -0.1058 229 GLU B CD  
3757 O OE1 . GLU B 224 ? 1.6183 1.1252 0.8582 0.1250  -0.0967 -0.1340 229 GLU B OE1 
3758 O OE2 . GLU B 224 ? 1.3939 0.9823 0.7354 0.1281  -0.0898 -0.0948 229 GLU B OE2 
3759 N N   . ASN B 225 ? 1.4160 0.8088 0.6612 0.1778  0.0674  -0.0598 230 ASN B N   
3760 C CA  . ASN B 225 ? 1.5123 0.8340 0.6753 0.1999  0.0915  -0.0680 230 ASN B CA  
3761 C C   . ASN B 225 ? 1.5140 0.8200 0.6919 0.2226  0.1440  -0.0440 230 ASN B C   
3762 O O   . ASN B 225 ? 1.7227 0.9686 0.8305 0.2454  0.1695  -0.0483 230 ASN B O   
3763 C CB  . ASN B 225 ? 1.5686 0.8498 0.6981 0.1813  0.0719  -0.1004 230 ASN B CB  
3764 C CG  . ASN B 225 ? 1.6270 0.9123 0.7181 0.1641  0.0227  -0.1307 230 ASN B CG  
3765 O OD1 . ASN B 225 ? 1.6141 0.9288 0.6922 0.1732  0.0014  -0.1272 230 ASN B OD1 
3766 N ND2 . ASN B 225 ? 1.6960 0.9514 0.7690 0.1393  0.0044  -0.1616 230 ASN B ND2 
3767 N N   . ALA B 226 ? 1.4197 0.7791 0.6863 0.2174  0.1603  -0.0208 231 ALA B N   
3768 C CA  . ALA B 226 ? 1.3902 0.7530 0.6876 0.2378  0.2080  0.0018  231 ALA B CA  
3769 C C   . ALA B 226 ? 1.4409 0.7851 0.6967 0.2619  0.2404  0.0182  231 ALA B C   
3770 O O   . ALA B 226 ? 1.4801 0.8408 0.7320 0.2582  0.2289  0.0251  231 ALA B O   
3771 C CB  . ALA B 226 ? 1.2704 0.7027 0.6744 0.2226  0.2088  0.0184  231 ALA B CB  
3772 N N   . ILE B 227 ? 1.5381 0.8426 0.7582 0.2888  0.2836  0.0249  232 ILE B N   
3773 C CA  . ILE B 227 ? 1.6093 0.8816 0.7768 0.3150  0.3242  0.0406  232 ILE B CA  
3774 C C   . ILE B 227 ? 1.5962 0.9190 0.8495 0.3174  0.3682  0.0690  232 ILE B C   
3775 O O   . ILE B 227 ? 1.6812 0.9962 0.9170 0.3252  0.3944  0.0853  232 ILE B O   
3776 C CB  . ILE B 227 ? 1.6728 0.8655 0.7417 0.3455  0.3521  0.0309  232 ILE B CB  
3777 C CG1 . ILE B 227 ? 1.7379 0.8804 0.7283 0.3377  0.3078  -0.0027 232 ILE B CG1 
3778 C CG2 . ILE B 227 ? 1.7680 0.9157 0.7609 0.3732  0.3896  0.0451  232 ILE B CG2 
3779 C CD1 . ILE B 227 ? 1.6860 0.8295 0.6332 0.3244  0.2589  -0.0175 232 ILE B CD1 
3780 N N   . ALA B 228 ? 1.5482 0.9190 0.8890 0.3119  0.3776  0.0741  233 ALA B N   
3781 C CA  . ALA B 228 ? 1.4806 0.9112 0.9151 0.3118  0.4157  0.0967  233 ALA B CA  
3782 C C   . ALA B 228 ? 1.3538 0.8590 0.8932 0.2882  0.3879  0.0967  233 ALA B C   
3783 O O   . ALA B 228 ? 1.2761 0.7778 0.8119 0.2794  0.3509  0.0818  233 ALA B O   
3784 C CB  . ALA B 228 ? 1.5255 0.9380 0.9526 0.3435  0.4675  0.1048  233 ALA B CB  
3785 N N   . GLU B 229 ? 1.3084 0.8776 0.9380 0.2777  0.4081  0.1127  234 GLU B N   
3786 C CA  . GLU B 229 ? 1.2272 0.8710 0.9562 0.2552  0.3815  0.1131  234 GLU B CA  
3787 C C   . GLU B 229 ? 1.2256 0.8978 0.9989 0.2723  0.3836  0.1119  234 GLU B C   
3788 O O   . GLU B 229 ? 1.2090 0.8964 1.0016 0.2637  0.3471  0.1034  234 GLU B O   
3789 C CB  . GLU B 229 ? 1.1925 0.8930 1.0008 0.2364  0.4022  0.1271  234 GLU B CB  
3790 C CG  . GLU B 229 ? 1.1696 0.9280 1.0501 0.2061  0.3630  0.1230  234 GLU B CG  
3791 C CD  . GLU B 229 ? 1.2535 1.0620 1.2096 0.1834  0.3834  0.1330  234 GLU B CD  
3792 O OE1 . GLU B 229 ? 1.2862 1.1422 1.3106 0.1880  0.4162  0.1406  234 GLU B OE1 
3793 O OE2 . GLU B 229 ? 1.3130 1.1138 1.2624 0.1605  0.3678  0.1326  234 GLU B OE2 
3794 N N   . GLN B 230 ? 1.2446 0.9202 1.0293 0.2995  0.4290  0.1215  235 GLN B N   
3795 C CA  . GLN B 230 ? 1.2785 0.9708 1.0910 0.3270  0.4370  0.1221  235 GLN B CA  
3796 C C   . GLN B 230 ? 1.3392 0.9574 1.0662 0.3397  0.4148  0.1070  235 GLN B C   
3797 O O   . GLN B 230 ? 1.4152 1.0477 1.1678 0.3490  0.3984  0.1048  235 GLN B O   
3798 C CB  . GLN B 230 ? 1.4120 1.1160 1.2447 0.3589  0.4955  0.1355  235 GLN B CB  
3799 C CG  . GLN B 230 ? 1.4094 1.2192 1.3712 0.3550  0.5132  0.1481  235 GLN B CG  
3800 C CD  . GLN B 230 ? 1.3708 1.2378 1.3978 0.3702  0.4887  0.1470  235 GLN B CD  
3801 O OE1 . GLN B 230 ? 1.4188 1.2798 1.4412 0.4096  0.5112  0.1512  235 GLN B OE1 
3802 N NE2 . GLN B 230 ? 1.2649 1.1833 1.3468 0.3426  0.4437  0.1421  235 GLN B NE2 
3803 N N   . GLN B 231 ? 1.3536 0.8920 0.9784 0.3395  0.4135  0.0958  236 GLN B N   
3804 C CA  . GLN B 231 ? 1.3668 0.8321 0.9089 0.3408  0.3877  0.0760  236 GLN B CA  
3805 C C   . GLN B 231 ? 1.2402 0.7313 0.8156 0.3106  0.3383  0.0670  236 GLN B C   
3806 O O   . GLN B 231 ? 1.3090 0.7770 0.8740 0.3151  0.3257  0.0595  236 GLN B O   
3807 C CB  . GLN B 231 ? 1.4205 0.8090 0.8538 0.3392  0.3855  0.0622  236 GLN B CB  
3808 C CG  . GLN B 231 ? 1.4524 0.7661 0.8001 0.3333  0.3566  0.0363  236 GLN B CG  
3809 C CD  . GLN B 231 ? 1.4975 0.7723 0.7696 0.3156  0.3277  0.0189  236 GLN B CD  
3810 O OE1 . GLN B 231 ? 1.5136 0.8201 0.8004 0.3054  0.3210  0.0274  236 GLN B OE1 
3811 N NE2 . GLN B 231 ? 1.5677 0.7733 0.7581 0.3122  0.3091  -0.0066 236 GLN B NE2 
3812 N N   . LEU B 232 ? 1.1605 0.6920 0.7694 0.2818  0.3149  0.0688  237 LEU B N   
3813 C CA  . LEU B 232 ? 1.1389 0.6950 0.7769 0.2529  0.2712  0.0611  237 LEU B CA  
3814 C C   . LEU B 232 ? 1.1074 0.7193 0.8247 0.2550  0.2648  0.0701  237 LEU B C   
3815 O O   . LEU B 232 ? 1.1155 0.7106 0.8245 0.2505  0.2432  0.0626  237 LEU B O   
3816 C CB  . LEU B 232 ? 1.0580 0.6425 0.7112 0.2272  0.2528  0.0627  237 LEU B CB  
3817 C CG  . LEU B 232 ? 0.9974 0.6068 0.6774 0.1980  0.2102  0.0548  237 LEU B CG  
3818 C CD1 . LEU B 232 ? 1.0251 0.5857 0.6492 0.1892  0.1850  0.0349  237 LEU B CD1 
3819 C CD2 . LEU B 232 ? 0.9685 0.5995 0.6568 0.1806  0.1989  0.0583  237 LEU B CD2 
3820 N N   . ILE B 233 ? 1.0983 0.7748 0.8896 0.2619  0.2843  0.0855  238 ILE B N   
3821 C CA  . ILE B 233 ? 1.0435 0.7862 0.9165 0.2670  0.2759  0.0938  238 ILE B CA  
3822 C C   . ILE B 233 ? 1.1116 0.8221 0.9598 0.2983  0.2820  0.0934  238 ILE B C   
3823 O O   . ILE B 233 ? 1.2047 0.9169 1.0605 0.2961  0.2563  0.0912  238 ILE B O   
3824 C CB  . ILE B 233 ? 1.0139 0.8319 0.9709 0.2716  0.3019  0.1074  238 ILE B CB  
3825 C CG1 . ILE B 233 ? 0.9017 0.7488 0.8878 0.2372  0.2948  0.1083  238 ILE B CG1 
3826 C CG2 . ILE B 233 ? 0.9888 0.8787 1.0270 0.2853  0.2923  0.1138  238 ILE B CG2 
3827 C CD1 . ILE B 233 ? 0.8632 0.7564 0.9070 0.2359  0.3318  0.1192  238 ILE B CD1 
3828 N N   . MET B 234 ? 1.1453 0.8174 0.9551 0.3286  0.3183  0.0958  239 MET B N   
3829 C CA  . MET B 234 ? 1.2683 0.8973 1.0442 0.3637  0.3310  0.0961  239 MET B CA  
3830 C C   . MET B 234 ? 1.2831 0.8238 0.9743 0.3533  0.3108  0.0797  239 MET B C   
3831 O O   . MET B 234 ? 1.3994 0.9122 1.0764 0.3730  0.3099  0.0812  239 MET B O   
3832 C CB  . MET B 234 ? 1.4084 1.0142 1.1607 0.4008  0.3797  0.1026  239 MET B CB  
3833 C CG  . MET B 234 ? 1.4452 1.1442 1.2941 0.4158  0.4072  0.1197  239 MET B CG  
3834 S SD  . MET B 234 ? 1.4597 1.2634 1.4216 0.4327  0.3896  0.1318  239 MET B SD  
3835 C CE  . MET B 234 ? 1.6983 1.4469 1.6115 0.4925  0.4169  0.1371  239 MET B CE  
3836 N N   . ALA B 235 ? 1.2239 0.7233 0.8618 0.3230  0.2952  0.0645  240 ALA B N   
3837 C CA  . ALA B 235 ? 1.2201 0.6507 0.7938 0.3025  0.2718  0.0456  240 ALA B CA  
3838 C C   . ALA B 235 ? 1.1562 0.6190 0.7734 0.2811  0.2400  0.0472  240 ALA B C   
3839 O O   . ALA B 235 ? 1.1753 0.5881 0.7603 0.2828  0.2357  0.0416  240 ALA B O   
3840 C CB  . ALA B 235 ? 1.2362 0.6328 0.7543 0.2764  0.2584  0.0281  240 ALA B CB  
3841 N N   . ILE B 236 ? 1.0838 0.6218 0.7679 0.2617  0.2212  0.0548  241 ILE B N   
3842 C CA  . ILE B 236 ? 1.0479 0.6169 0.7698 0.2416  0.1915  0.0564  241 ILE B CA  
3843 C C   . ILE B 236 ? 1.0488 0.6314 0.7975 0.2709  0.1963  0.0695  241 ILE B C   
3844 O O   . ILE B 236 ? 1.0423 0.5924 0.7703 0.2668  0.1839  0.0676  241 ILE B O   
3845 C CB  . ILE B 236 ? 0.9493 0.5911 0.7322 0.2168  0.1723  0.0610  241 ILE B CB  
3846 C CG1 . ILE B 236 ? 0.9683 0.5927 0.7182 0.1912  0.1631  0.0492  241 ILE B CG1 
3847 C CG2 . ILE B 236 ? 0.8847 0.5533 0.6999 0.2011  0.1450  0.0629  241 ILE B CG2 
3848 C CD1 . ILE B 236 ? 0.8378 0.5167 0.6319 0.1818  0.1642  0.0574  241 ILE B CD1 
3849 N N   . LYS B 237 ? 1.1072 0.7386 0.9015 0.3012  0.2154  0.0831  242 LYS B N   
3850 C CA  . LYS B 237 ? 1.1081 0.7584 0.9275 0.3400  0.2221  0.0965  242 LYS B CA  
3851 C C   . LYS B 237 ? 1.1911 0.7482 0.9338 0.3657  0.2385  0.0941  242 LYS B C   
3852 O O   . LYS B 237 ? 1.2850 0.8289 1.0221 0.3846  0.2312  0.1018  242 LYS B O   
3853 C CB  . LYS B 237 ? 1.0941 0.8150 0.9774 0.3681  0.2449  0.1087  242 LYS B CB  
3854 C CG  . LYS B 237 ? 1.0133 0.8337 0.9862 0.3451  0.2282  0.1124  242 LYS B CG  
3855 C CD  . LYS B 237 ? 1.0320 0.9402 1.0891 0.3740  0.2427  0.1245  242 LYS B CD  
3856 C CE  . LYS B 237 ? 1.1040 1.0488 1.1912 0.4057  0.2229  0.1327  242 LYS B CE  
3857 N NZ  . LYS B 237 ? 1.0556 1.0633 1.1946 0.3810  0.1830  0.1303  242 LYS B NZ  
3858 N N   . SER B 238 ? 1.2539 0.7399 0.9307 0.3662  0.2607  0.0829  243 SER B N   
3859 C CA  . SER B 238 ? 1.3512 0.7315 0.9429 0.3840  0.2783  0.0758  243 SER B CA  
3860 C C   . SER B 238 ? 1.3696 0.6838 0.9123 0.3500  0.2587  0.0619  243 SER B C   
3861 O O   . SER B 238 ? 1.4423 0.6669 0.9189 0.3625  0.2742  0.0570  243 SER B O   
3862 C CB  . SER B 238 ? 1.3955 0.7143 0.9242 0.3939  0.3076  0.0646  243 SER B CB  
3863 O OG  . SER B 238 ? 1.3549 0.6409 0.8421 0.3516  0.2924  0.0434  243 SER B OG  
3864 N N   . GLY B 239 ? 1.3517 0.7060 0.9254 0.3076  0.2288  0.0553  244 GLY B N   
3865 C CA  . GLY B 239 ? 1.4203 0.7275 0.9623 0.2703  0.2113  0.0418  244 GLY B CA  
3866 C C   . GLY B 239 ? 1.3703 0.6719 0.8971 0.2245  0.1939  0.0197  244 GLY B C   
3867 O O   . GLY B 239 ? 1.3488 0.6242 0.8620 0.1912  0.1797  0.0077  244 GLY B O   
3868 N N   . ASN B 240 ? 1.3971 0.7248 0.9268 0.2242  0.1957  0.0150  245 ASN B N   
3869 C CA  . ASN B 240 ? 1.3989 0.7219 0.9071 0.1890  0.1774  -0.0055 245 ASN B CA  
3870 C C   . ASN B 240 ? 1.2697 0.6653 0.8377 0.1603  0.1486  -0.0021 245 ASN B C   
3871 O O   . ASN B 240 ? 1.1697 0.6301 0.7969 0.1705  0.1459  0.0162  245 ASN B O   
3872 C CB  . ASN B 240 ? 1.5369 0.8557 1.0171 0.2052  0.1917  -0.0084 245 ASN B CB  
3873 C CG  . ASN B 240 ? 1.7378 1.0084 1.1545 0.1813  0.1789  -0.0353 245 ASN B CG  
3874 O OD1 . ASN B 240 ? 1.8492 1.0411 1.1963 0.1868  0.1917  -0.0515 245 ASN B OD1 
3875 N ND2 . ASN B 240 ? 1.8836 1.1997 1.3215 0.1558  0.1519  -0.0416 245 ASN B ND2 
3876 N N   . ARG B 241 ? 1.2121 0.5970 0.7650 0.1248  0.1273  -0.0212 246 ARG B N   
3877 C CA  . ARG B 241 ? 1.1168 0.5577 0.7188 0.0971  0.1020  -0.0202 246 ARG B CA  
3878 C C   . ARG B 241 ? 1.1175 0.5720 0.7073 0.0730  0.0806  -0.0386 246 ARG B C   
3879 O O   . ARG B 241 ? 1.2190 0.6345 0.7565 0.0766  0.0836  -0.0536 246 ARG B O   
3880 C CB  . ARG B 241 ? 1.1891 0.6024 0.7927 0.0795  0.0998  -0.0228 246 ARG B CB  
3881 C CG  . ARG B 241 ? 1.1525 0.5625 0.7710 0.1063  0.1142  -0.0014 246 ARG B CG  
3882 C CD  . ARG B 241 ? 1.0812 0.5705 0.7623 0.1146  0.1025  0.0171  246 ARG B CD  
3883 N NE  . ARG B 241 ? 1.0474 0.5415 0.7425 0.1435  0.1107  0.0357  246 ARG B NE  
3884 C CZ  . ARG B 241 ? 1.0734 0.5776 0.7756 0.1804  0.1252  0.0481  246 ARG B CZ  
3885 N NH1 . ARG B 241 ? 1.1311 0.6344 0.8241 0.1941  0.1397  0.0453  246 ARG B NH1 
3886 N NH2 . ARG B 241 ? 1.1402 0.6567 0.8577 0.2069  0.1260  0.0640  246 ARG B NH2 
3887 N N   . PRO B 242 ? 1.0144 0.5238 0.6481 0.0525  0.0589  -0.0373 247 PRO B N   
3888 C CA  . PRO B 242 ? 1.0496 0.5764 0.6725 0.0348  0.0364  -0.0542 247 PRO B CA  
3889 C C   . PRO B 242 ? 1.0806 0.5663 0.6686 0.0085  0.0254  -0.0826 247 PRO B C   
3890 O O   . PRO B 242 ? 1.1141 0.5725 0.7070 -0.0086 0.0315  -0.0876 247 PRO B O   
3891 C CB  . PRO B 242 ? 0.9602 0.5508 0.6408 0.0219  0.0200  -0.0446 247 PRO B CB  
3892 C CG  . PRO B 242 ? 0.9474 0.5581 0.6616 0.0401  0.0350  -0.0209 247 PRO B CG  
3893 C CD  . PRO B 242 ? 0.9895 0.5503 0.6808 0.0507  0.0539  -0.0196 247 PRO B CD  
3894 N N   . ASP B 243 ? 1.2081 0.6867 0.7579 0.0059  0.0101  -0.1014 248 ASP B N   
3895 C CA  . ASP B 243 ? 1.3402 0.7770 0.8500 -0.0193 -0.0023 -0.1337 248 ASP B CA  
3896 C C   . ASP B 243 ? 1.3217 0.8041 0.8813 -0.0563 -0.0260 -0.1474 248 ASP B C   
3897 O O   . ASP B 243 ? 1.2984 0.8440 0.8897 -0.0578 -0.0488 -0.1462 248 ASP B O   
3898 C CB  . ASP B 243 ? 1.3894 0.8097 0.8387 -0.0066 -0.0157 -0.1502 248 ASP B CB  
3899 C CG  . ASP B 243 ? 1.5419 0.8995 0.9320 -0.0274 -0.0236 -0.1859 248 ASP B CG  
3900 O OD1 . ASP B 243 ? 1.5323 0.8599 0.9323 -0.0571 -0.0189 -0.2000 248 ASP B OD1 
3901 O OD2 . ASP B 243 ? 1.6400 0.9734 0.9679 -0.0141 -0.0337 -0.2007 248 ASP B OD2 
3902 N N   . VAL B 244 ? 1.3825 0.8309 0.9488 -0.0842 -0.0169 -0.1589 249 VAL B N   
3903 C CA  . VAL B 244 ? 1.4278 0.9165 1.0451 -0.1231 -0.0326 -0.1731 249 VAL B CA  
3904 C C   . VAL B 244 ? 1.4768 0.9889 1.0859 -0.1478 -0.0660 -0.2085 249 VAL B C   
3905 O O   . VAL B 244 ? 1.5090 1.0911 1.1714 -0.1662 -0.0888 -0.2160 249 VAL B O   
3906 C CB  . VAL B 244 ? 1.4826 0.9197 1.1052 -0.1468 -0.0070 -0.1737 249 VAL B CB  
3907 C CG1 . VAL B 244 ? 1.5532 1.0347 1.2340 -0.1882 -0.0169 -0.1869 249 VAL B CG1 
3908 C CG2 . VAL B 244 ? 1.3993 0.8227 1.0289 -0.1168 0.0194  -0.1386 249 VAL B CG2 
3909 N N   . ASP B 245 ? 1.5488 1.0049 1.0907 -0.1452 -0.0696 -0.2303 250 ASP B N   
3910 C CA  . ASP B 245 ? 1.7089 1.1849 1.2301 -0.1629 -0.1067 -0.2663 250 ASP B CA  
3911 C C   . ASP B 245 ? 1.7851 1.3309 1.3114 -0.1350 -0.1366 -0.2588 250 ASP B C   
3912 O O   . ASP B 245 ? 1.7666 1.3544 1.2961 -0.1492 -0.1738 -0.2859 250 ASP B O   
3913 C CB  . ASP B 245 ? 1.7926 1.1794 1.2253 -0.1625 -0.1019 -0.2917 250 ASP B CB  
3914 C CG  . ASP B 245 ? 1.7692 1.0735 1.1843 -0.1906 -0.0724 -0.3033 250 ASP B CG  
3915 O OD1 . ASP B 245 ? 1.7417 1.0623 1.2106 -0.2299 -0.0695 -0.3114 250 ASP B OD1 
3916 O OD2 . ASP B 245 ? 1.7802 0.9983 1.1237 -0.1709 -0.0484 -0.3031 250 ASP B OD2 
3917 N N   . ASP B 246 ? 1.8903 1.4463 1.4154 -0.0955 -0.1203 -0.2235 251 ASP B N   
3918 C CA  . ASP B 246 ? 1.8411 1.4576 1.3746 -0.0683 -0.1410 -0.2100 251 ASP B CA  
3919 C C   . ASP B 246 ? 1.8563 1.5583 1.4687 -0.0826 -0.1608 -0.2064 251 ASP B C   
3920 O O   . ASP B 246 ? 2.0087 1.7599 1.6234 -0.0625 -0.1840 -0.2024 251 ASP B O   
3921 C CB  . ASP B 246 ? 1.7546 1.3541 1.2696 -0.0277 -0.1126 -0.1740 251 ASP B CB  
3922 C CG  . ASP B 246 ? 1.9139 1.4583 1.3436 0.0015  -0.1055 -0.1768 251 ASP B CG  
3923 O OD1 . ASP B 246 ? 1.8637 1.3555 1.2378 -0.0081 -0.1102 -0.2037 251 ASP B OD1 
3924 O OD2 . ASP B 246 ? 1.9159 1.4653 1.3313 0.0340  -0.0921 -0.1520 251 ASP B OD2 
3925 N N   . ILE B 247 ? 1.7933 1.5078 1.4638 -0.1125 -0.1486 -0.2056 252 ILE B N   
3926 C CA  . ILE B 247 ? 1.7935 1.5858 1.5396 -0.1287 -0.1628 -0.2047 252 ILE B CA  
3927 C C   . ILE B 247 ? 2.0880 1.9252 1.8496 -0.1549 -0.2006 -0.2422 252 ILE B C   
3928 O O   . ILE B 247 ? 2.2055 2.0205 1.9732 -0.1939 -0.2006 -0.2697 252 ILE B O   
3929 C CB  . ILE B 247 ? 1.6463 1.4307 1.4418 -0.1525 -0.1343 -0.1929 252 ILE B CB  
3930 C CG1 . ILE B 247 ? 1.5936 1.3450 1.3768 -0.1240 -0.1041 -0.1577 252 ILE B CG1 
3931 C CG2 . ILE B 247 ? 1.6643 1.5278 1.5354 -0.1676 -0.1452 -0.1922 252 ILE B CG2 
3932 C CD1 . ILE B 247 ? 1.5458 1.2673 1.3512 -0.1395 -0.0751 -0.1460 252 ILE B CD1 
3933 N N   . THR B 248 ? 2.2548 2.1541 2.0219 -0.1324 -0.2324 -0.2432 253 THR B N   
3934 C CA  . THR B 248 ? 2.1404 2.1021 1.9276 -0.1487 -0.2764 -0.2779 253 THR B CA  
3935 C C   . THR B 248 ? 2.0629 2.1084 1.9491 -0.1780 -0.2836 -0.2849 253 THR B C   
3936 O O   . THR B 248 ? 2.0555 2.1392 1.9783 -0.2158 -0.3063 -0.3203 253 THR B O   
3937 C CB  . THR B 248 ? 1.9544 1.9475 1.6994 -0.1034 -0.3082 -0.2731 253 THR B CB  
3938 O OG1 . THR B 248 ? 2.0453 2.0739 1.8191 -0.0713 -0.2967 -0.2374 253 THR B OG1 
3939 C CG2 . THR B 248 ? 2.1777 2.0907 1.8222 -0.0775 -0.3023 -0.2718 253 THR B CG2 
3940 N N   . GLU B 249 ? 1.9425 2.0160 1.8718 -0.1617 -0.2630 -0.2526 254 GLU B N   
3941 C CA  . GLU B 249 ? 1.8340 1.9769 1.8545 -0.1861 -0.2583 -0.2533 254 GLU B CA  
3942 C C   . GLU B 249 ? 1.8515 1.9582 1.9019 -0.2355 -0.2288 -0.2645 254 GLU B C   
3943 O O   . GLU B 249 ? 1.8908 1.9108 1.8898 -0.2440 -0.2056 -0.2630 254 GLU B O   
3944 C CB  . GLU B 249 ? 1.6745 1.8385 1.7178 -0.1537 -0.2392 -0.2152 254 GLU B CB  
3945 C CG  . GLU B 249 ? 1.6688 1.8900 1.7144 -0.1123 -0.2632 -0.2036 254 GLU B CG  
3946 C CD  . GLU B 249 ? 1.5940 1.8371 1.6740 -0.0911 -0.2412 -0.1719 254 GLU B CD  
3947 O OE1 . GLU B 249 ? 1.5576 1.8295 1.6997 -0.1147 -0.2236 -0.1707 254 GLU B OE1 
3948 O OE2 . GLU B 249 ? 1.5763 1.8027 1.6176 -0.0510 -0.2388 -0.1481 254 GLU B OE2 
3949 N N   . TYR B 250 ? 1.7699 1.9422 1.9024 -0.2659 -0.2275 -0.2751 255 TYR B N   
3950 C CA  . TYR B 250 ? 1.6602 1.7978 1.8249 -0.3118 -0.1919 -0.2806 255 TYR B CA  
3951 C C   . TYR B 250 ? 1.4982 1.5885 1.6508 -0.2920 -0.1504 -0.2408 255 TYR B C   
3952 O O   . TYR B 250 ? 1.3311 1.4718 1.5287 -0.2775 -0.1426 -0.2211 255 TYR B O   
3953 C CB  . TYR B 250 ? 1.6093 1.8363 1.8706 -0.3508 -0.1990 -0.3035 255 TYR B CB  
3954 C CG  . TYR B 250 ? 1.6343 1.8184 1.9259 -0.3953 -0.1529 -0.3027 255 TYR B CG  
3955 C CD1 . TYR B 250 ? 1.7000 1.8000 1.9547 -0.4340 -0.1352 -0.3225 255 TYR B CD1 
3956 C CD2 . TYR B 250 ? 1.5849 1.8066 1.9356 -0.3961 -0.1242 -0.2813 255 TYR B CD2 
3957 C CE1 . TYR B 250 ? 1.7214 1.7740 1.9965 -0.4721 -0.0894 -0.3195 255 TYR B CE1 
3958 C CE2 . TYR B 250 ? 1.6047 1.7822 1.9757 -0.4338 -0.0789 -0.2785 255 TYR B CE2 
3959 C CZ  . TYR B 250 ? 1.6738 1.7660 2.0066 -0.4716 -0.0612 -0.2968 255 TYR B CZ  
3960 O OH  . TYR B 250 ? 1.7060 1.7444 2.0510 -0.5069 -0.0123 -0.2918 255 TYR B OH  
3961 N N   . CYS B 251 ? 1.4236 1.4184 1.5127 -0.2881 -0.1260 -0.2297 256 CYS B N   
3962 C CA  . CYS B 251 ? 1.3293 1.2735 1.4051 -0.2757 -0.0878 -0.1974 256 CYS B CA  
3963 C C   . CYS B 251 ? 1.3881 1.2820 1.4741 -0.3184 -0.0549 -0.2067 256 CYS B C   
3964 O O   . CYS B 251 ? 1.4990 1.3450 1.5576 -0.3453 -0.0549 -0.2314 256 CYS B O   
3965 C CB  . CYS B 251 ? 1.2592 1.1361 1.2630 -0.2404 -0.0810 -0.1780 256 CYS B CB  
3966 S SG  . CYS B 251 ? 1.2275 1.0620 1.2210 -0.2193 -0.0444 -0.1395 256 CYS B SG  
3967 N N   . PRO B 252 ? 1.2885 1.1869 1.4081 -0.3246 -0.0251 -0.1878 257 PRO B N   
3968 C CA  . PRO B 252 ? 1.3275 1.1640 1.4455 -0.3608 0.0135  -0.1913 257 PRO B CA  
3969 C C   . PRO B 252 ? 1.3441 1.0688 1.3829 -0.3514 0.0363  -0.1816 257 PRO B C   
3970 O O   . PRO B 252 ? 1.3237 1.0235 1.3158 -0.3104 0.0294  -0.1625 257 PRO B O   
3971 C CB  . PRO B 252 ? 1.2966 1.1557 1.4483 -0.3527 0.0396  -0.1652 257 PRO B CB  
3972 C CG  . PRO B 252 ? 1.1584 1.1182 1.3616 -0.3335 0.0107  -0.1640 257 PRO B CG  
3973 C CD  . PRO B 252 ? 1.1370 1.1044 1.3030 -0.3039 -0.0261 -0.1681 257 PRO B CD  
3974 N N   . ARG B 253 ? 1.4475 1.1070 1.4746 -0.3892 0.0655  -0.1947 258 ARG B N   
3975 C CA  . ARG B 253 ? 1.5569 1.1006 1.5059 -0.3803 0.0929  -0.1856 258 ARG B CA  
3976 C C   . ARG B 253 ? 1.5204 1.0253 1.4349 -0.3386 0.1165  -0.1451 258 ARG B C   
3977 O O   . ARG B 253 ? 1.4142 0.8620 1.2688 -0.3038 0.1198  -0.1299 258 ARG B O   
3978 C CB  . ARG B 253 ? 1.6200 1.0966 1.5650 -0.4325 0.1254  -0.2069 258 ARG B CB  
3979 C CG  . ARG B 253 ? 1.6249 1.1243 1.5943 -0.4787 0.1020  -0.2524 258 ARG B CG  
3980 C CD  . ARG B 253 ? 1.7439 1.1782 1.7191 -0.5364 0.1407  -0.2722 258 ARG B CD  
3981 N NE  . ARG B 253 ? 1.7887 1.2501 1.7946 -0.5877 0.1167  -0.3205 258 ARG B NE  
3982 C CZ  . ARG B 253 ? 1.8721 1.2910 1.8960 -0.6494 0.1436  -0.3482 258 ARG B CZ  
3983 N NH1 . ARG B 253 ? 1.9211 1.2618 1.9303 -0.6647 0.1996  -0.3290 258 ARG B NH1 
3984 N NH2 . ARG B 253 ? 1.9135 1.3657 1.9676 -0.6962 0.1147  -0.3958 258 ARG B NH2 
3985 N N   . GLU B 254 ? 1.4883 1.0280 1.4417 -0.3414 0.1321  -0.1291 259 GLU B N   
3986 C CA  . GLU B 254 ? 1.5065 1.0180 1.4294 -0.3038 0.1505  -0.0934 259 GLU B CA  
3987 C C   . GLU B 254 ? 1.3768 0.9209 1.2838 -0.2554 0.1216  -0.0764 259 GLU B C   
3988 O O   . GLU B 254 ? 1.4090 0.9054 1.2680 -0.2213 0.1302  -0.0542 259 GLU B O   
3989 C CB  . GLU B 254 ? 1.5162 1.0675 1.4848 -0.3160 0.1696  -0.0829 259 GLU B CB  
3990 C CG  . GLU B 254 ? 1.6486 1.1382 1.6130 -0.3528 0.2160  -0.0849 259 GLU B CG  
3991 C CD  . GLU B 254 ? 1.6994 1.2284 1.7274 -0.4099 0.2175  -0.1191 259 GLU B CD  
3992 O OE1 . GLU B 254 ? 1.6936 1.2447 1.7685 -0.4394 0.2455  -0.1201 259 GLU B OE1 
3993 O OE2 . GLU B 254 ? 1.7660 1.3073 1.7988 -0.4254 0.1904  -0.1460 259 GLU B OE2 
3994 N N   . ILE B 255 ? 1.2392 0.8650 1.1874 -0.2522 0.0885  -0.0866 260 ILE B N   
3995 C CA  . ILE B 255 ? 1.2517 0.9088 1.1886 -0.2117 0.0635  -0.0730 260 ILE B CA  
3996 C C   . ILE B 255 ? 1.2722 0.8811 1.1581 -0.1932 0.0572  -0.0755 260 ILE B C   
3997 O O   . ILE B 255 ? 1.3059 0.9055 1.1674 -0.1577 0.0547  -0.0563 260 ILE B O   
3998 C CB  . ILE B 255 ? 1.2021 0.9496 1.1887 -0.2109 0.0338  -0.0819 260 ILE B CB  
3999 C CG1 . ILE B 255 ? 1.1937 0.9871 1.2245 -0.2146 0.0431  -0.0715 260 ILE B CG1 
4000 C CG2 . ILE B 255 ? 1.1564 0.9229 1.1248 -0.1738 0.0127  -0.0699 260 ILE B CG2 
4001 C CD1 . ILE B 255 ? 1.0788 0.9575 1.1635 -0.2159 0.0223  -0.0797 260 ILE B CD1 
4002 N N   . ILE B 256 ? 1.2112 0.7910 1.0826 -0.2176 0.0555  -0.1004 261 ILE B N   
4003 C CA  . ILE B 256 ? 1.2409 0.7624 1.0566 -0.2012 0.0560  -0.1047 261 ILE B CA  
4004 C C   . ILE B 256 ? 1.2791 0.7201 1.0467 -0.1803 0.0863  -0.0837 261 ILE B C   
4005 O O   . ILE B 256 ? 1.2633 0.6823 0.9974 -0.1452 0.0859  -0.0712 261 ILE B O   
4006 C CB  . ILE B 256 ? 1.3314 0.8308 1.1352 -0.2354 0.0479  -0.1399 261 ILE B CB  
4007 C CG1 . ILE B 256 ? 1.3335 0.9162 1.1743 -0.2424 0.0105  -0.1587 261 ILE B CG1 
4008 C CG2 . ILE B 256 ? 1.3449 0.7671 1.0804 -0.2178 0.0558  -0.1443 261 ILE B CG2 
4009 C CD1 . ILE B 256 ? 1.2967 0.8878 1.1502 -0.2847 -0.0043 -0.1967 261 ILE B CD1 
4010 N N   . SER B 257 ? 1.3330 0.7324 1.0975 -0.1996 0.1136  -0.0793 262 SER B N   
4011 C CA  . SER B 257 ? 1.3237 0.6471 1.0383 -0.1740 0.1423  -0.0554 262 SER B CA  
4012 C C   . SER B 257 ? 1.2219 0.5805 0.9404 -0.1313 0.1337  -0.0265 262 SER B C   
4013 O O   . SER B 257 ? 1.2462 0.5662 0.9250 -0.0942 0.1404  -0.0092 262 SER B O   
4014 C CB  . SER B 257 ? 1.2913 0.5625 0.9997 -0.2040 0.1759  -0.0549 262 SER B CB  
4015 O OG  . SER B 257 ? 1.3884 0.6203 1.0928 -0.2472 0.1863  -0.0837 262 SER B OG  
4016 N N   . LEU B 258 ? 1.1406 0.5726 0.9074 -0.1364 0.1186  -0.0228 263 LEU B N   
4017 C CA  . LEU B 258 ? 1.1972 0.6643 0.9701 -0.1029 0.1085  0.0001  263 LEU B CA  
4018 C C   . LEU B 258 ? 1.1409 0.6372 0.9128 -0.0719 0.0874  0.0047  263 LEU B C   
4019 O O   . LEU B 258 ? 1.1991 0.6858 0.9523 -0.0385 0.0877  0.0228  263 LEU B O   
4020 C CB  . LEU B 258 ? 1.1228 0.6564 0.9443 -0.1169 0.0990  0.0001  263 LEU B CB  
4021 C CG  . LEU B 258 ? 1.1184 0.6783 0.9415 -0.0894 0.0921  0.0207  263 LEU B CG  
4022 C CD1 . LEU B 258 ? 1.2025 0.7005 0.9818 -0.0770 0.1163  0.0380  263 LEU B CD1 
4023 C CD2 . LEU B 258 ? 1.0445 0.6691 0.9139 -0.1024 0.0821  0.0170  263 LEU B CD2 
4024 N N   . MET B 259 ? 1.0865 0.6190 0.8782 -0.0820 0.0699  -0.0116 264 MET B N   
4025 C CA  . MET B 259 ? 1.0869 0.6419 0.8756 -0.0548 0.0561  -0.0074 264 MET B CA  
4026 C C   . MET B 259 ? 1.0932 0.5874 0.8369 -0.0327 0.0711  -0.0035 264 MET B C   
4027 O O   . MET B 259 ? 1.0831 0.5881 0.8245 -0.0004 0.0697  0.0114  264 MET B O   
4028 C CB  . MET B 259 ? 1.0285 0.6285 0.8376 -0.0663 0.0362  -0.0238 264 MET B CB  
4029 C CG  . MET B 259 ? 1.1465 0.7160 0.9343 -0.0883 0.0356  -0.0482 264 MET B CG  
4030 S SD  . MET B 259 ? 1.1497 0.7763 0.9546 -0.0954 0.0070  -0.0661 264 MET B SD  
4031 C CE  . MET B 259 ? 1.0889 0.7788 0.9509 -0.1213 -0.0046 -0.0712 264 MET B CE  
4032 N N   . LYS B 260 ? 1.1862 0.6170 0.8963 -0.0505 0.0868  -0.0173 265 LYS B N   
4033 C CA  . LYS B 260 ? 1.2493 0.6061 0.9070 -0.0282 0.1069  -0.0133 265 LYS B CA  
4034 C C   . LYS B 260 ? 1.2323 0.5640 0.8718 0.0055  0.1201  0.0125  265 LYS B C   
4035 O O   . LYS B 260 ? 1.2203 0.5349 0.8381 0.0427  0.1257  0.0241  265 LYS B O   
4036 C CB  . LYS B 260 ? 1.3166 0.5984 0.9373 -0.0592 0.1243  -0.0348 265 LYS B CB  
4037 C CG  . LYS B 260 ? 1.3537 0.6377 0.9662 -0.0768 0.1115  -0.0615 265 LYS B CG  
4038 C CD  . LYS B 260 ? 1.4054 0.6017 0.9711 -0.1042 0.1304  -0.0843 265 LYS B CD  
4039 C CE  . LYS B 260 ? 1.4207 0.6333 0.9844 -0.1298 0.1091  -0.1166 265 LYS B CE  
4040 N NZ  . LYS B 260 ? 1.5129 0.6519 1.0433 -0.1700 0.1220  -0.1458 265 LYS B NZ  
4041 N N   . LEU B 261 ? 1.2812 0.6135 0.9288 -0.0051 0.1247  0.0213  266 LEU B N   
4042 C CA  . LEU B 261 ? 1.3356 0.6500 0.9623 0.0284  0.1319  0.0457  266 LEU B CA  
4043 C C   . LEU B 261 ? 1.2549 0.6440 0.9160 0.0586  0.1076  0.0586  266 LEU B C   
4044 O O   . LEU B 261 ? 1.2806 0.6637 0.9259 0.0980  0.1077  0.0733  266 LEU B O   
4045 C CB  . LEU B 261 ? 1.3634 0.6599 0.9866 0.0077  0.1440  0.0507  266 LEU B CB  
4046 C CG  . LEU B 261 ? 1.5087 0.7606 1.0886 0.0403  0.1573  0.0748  266 LEU B CG  
4047 C CD1 . LEU B 261 ? 1.6388 0.7913 1.1524 0.0600  0.1858  0.0818  266 LEU B CD1 
4048 C CD2 . LEU B 261 ? 1.5173 0.7634 1.0999 0.0160  0.1691  0.0781  266 LEU B CD2 
4049 N N   . CYS B 262 ? 1.1701 0.6291 0.8790 0.0397  0.0878  0.0520  267 CYS B N   
4050 C CA  . CYS B 262 ? 1.1087 0.6366 0.8536 0.0592  0.0662  0.0608  267 CYS B CA  
4051 C C   . CYS B 262 ? 1.0711 0.6272 0.8311 0.0795  0.0603  0.0602  267 CYS B C   
4052 O O   . CYS B 262 ? 0.9572 0.5624 0.7451 0.0991  0.0474  0.0692  267 CYS B O   
4053 C CB  . CYS B 262 ? 1.0617 0.6443 0.8463 0.0335  0.0514  0.0539  267 CYS B CB  
4054 S SG  . CYS B 262 ? 1.1882 0.7564 0.9642 0.0195  0.0582  0.0597  267 CYS B SG  
4055 N N   . TRP B 263 ? 1.0528 0.5800 0.7959 0.0733  0.0703  0.0486  268 TRP B N   
4056 C CA  . TRP B 263 ? 1.0590 0.6016 0.8073 0.0972  0.0724  0.0501  268 TRP B CA  
4057 C C   . TRP B 263 ? 1.0901 0.5796 0.7999 0.1305  0.0916  0.0578  268 TRP B C   
4058 O O   . TRP B 263 ? 1.0440 0.5308 0.7485 0.1469  0.1005  0.0556  268 TRP B O   
4059 C CB  . TRP B 263 ? 1.0407 0.5970 0.7947 0.0776  0.0687  0.0342  268 TRP B CB  
4060 C CG  . TRP B 263 ? 1.0523 0.5540 0.7677 0.0565  0.0766  0.0154  268 TRP B CG  
4061 C CD1 . TRP B 263 ? 1.1568 0.5844 0.8233 0.0620  0.0956  0.0100  268 TRP B CD1 
4062 C CD2 . TRP B 263 ? 1.0875 0.6062 0.8087 0.0281  0.0640  -0.0028 268 TRP B CD2 
4063 N NE1 . TRP B 263 ? 1.2063 0.6036 0.8497 0.0331  0.0944  -0.0131 268 TRP B NE1 
4064 C CE2 . TRP B 263 ? 1.1172 0.5743 0.7952 0.0131  0.0730  -0.0214 268 TRP B CE2 
4065 C CE3 . TRP B 263 ? 1.0018 0.5802 0.7583 0.0149  0.0453  -0.0055 268 TRP B CE3 
4066 C CZ2 . TRP B 263 ? 1.1344 0.5969 0.8079 -0.0155 0.0593  -0.0446 268 TRP B CZ2 
4067 C CZ3 . TRP B 263 ? 1.0314 0.6139 0.7812 -0.0082 0.0334  -0.0253 268 TRP B CZ3 
4068 C CH2 . TRP B 263 ? 1.0597 0.5892 0.7707 -0.0237 0.0382  -0.0456 268 TRP B CH2 
4069 N N   . GLU B 264 ? 1.1561 0.5996 0.8346 0.1437  0.1006  0.0681  269 GLU B N   
4070 C CA  . GLU B 264 ? 1.3036 0.6931 0.9408 0.1833  0.1194  0.0792  269 GLU B CA  
4071 C C   . GLU B 264 ? 1.2422 0.6901 0.9137 0.2232  0.1136  0.0908  269 GLU B C   
4072 O O   . GLU B 264 ? 1.1830 0.7088 0.9066 0.2251  0.0927  0.0960  269 GLU B O   
4073 C CB  . GLU B 264 ? 1.4236 0.7646 1.0234 0.1971  0.1266  0.0934  269 GLU B CB  
4074 C CG  . GLU B 264 ? 1.5240 0.7771 1.0745 0.1659  0.1485  0.0839  269 GLU B CG  
4075 C CD  . GLU B 264 ? 1.5872 0.7455 1.0764 0.1803  0.1776  0.0808  269 GLU B CD  
4076 O OE1 . GLU B 264 ? 1.5183 0.6738 0.9975 0.2205  0.1834  0.0881  269 GLU B OE1 
4077 O OE2 . GLU B 264 ? 1.6153 0.6981 1.0657 0.1498  0.1974  0.0702  269 GLU B OE2 
4078 N N   . ALA B 265 ? 1.2614 0.6714 0.9052 0.2529  0.1337  0.0931  270 ALA B N   
4079 C CA  . ALA B 265 ? 1.2772 0.7422 0.9565 0.2945  0.1342  0.1046  270 ALA B CA  
4080 C C   . ALA B 265 ? 1.2883 0.7980 0.9914 0.3271  0.1176  0.1223  270 ALA B C   
4081 O O   . ALA B 265 ? 1.2083 0.8085 0.9758 0.3346  0.0991  0.1258  270 ALA B O   
4082 C CB  . ALA B 265 ? 1.3527 0.7534 0.9855 0.3265  0.1637  0.1058  270 ALA B CB  
4083 N N   . ASN B 266 ? 1.3818 0.8245 1.0296 0.3445  0.1244  0.1320  271 ASN B N   
4084 C CA  . ASN B 266 ? 1.4352 0.9063 1.0872 0.3800  0.1070  0.1491  271 ASN B CA  
4085 C C   . ASN B 266 ? 1.3843 0.8981 1.0620 0.3457  0.0807  0.1448  271 ASN B C   
4086 O O   . ASN B 266 ? 1.4318 0.8928 1.0768 0.3102  0.0884  0.1380  271 ASN B O   
4087 C CB  . ASN B 266 ? 1.5592 0.9283 1.1286 0.4129  0.1281  0.1629  271 ASN B CB  
4088 C CG  . ASN B 266 ? 1.6546 1.0495 1.2175 0.4638  0.1101  0.1830  271 ASN B CG  
4089 O OD1 . ASN B 266 ? 1.5303 1.0272 1.1570 0.4786  0.0805  0.1850  271 ASN B OD1 
4090 N ND2 . ASN B 266 ? 1.8970 1.1962 1.3792 0.4907  0.1281  0.1973  271 ASN B ND2 
4091 N N   . PRO B 267 ? 1.3144 0.9229 1.0516 0.3547  0.0513  0.1471  272 PRO B N   
4092 C CA  . PRO B 267 ? 1.2611 0.9030 1.0153 0.3246  0.0274  0.1421  272 PRO B CA  
4093 C C   . PRO B 267 ? 1.3820 0.9614 1.0723 0.3324  0.0273  0.1519  272 PRO B C   
4094 O O   . PRO B 267 ? 1.3917 0.9608 1.0753 0.2968  0.0239  0.1456  272 PRO B O   
4095 C CB  . PRO B 267 ? 1.2406 0.9866 1.0630 0.3406  -0.0024 0.1422  272 PRO B CB  
4096 C CG  . PRO B 267 ? 1.2480 1.0290 1.1106 0.3580  0.0106  0.1419  272 PRO B CG  
4097 C CD  . PRO B 267 ? 1.2882 0.9816 1.0863 0.3869  0.0399  0.1511  272 PRO B CD  
4098 N N   . GLU B 268 ? 1.4234 0.9603 1.0652 0.3813  0.0335  0.1685  273 GLU B N   
4099 C CA  . GLU B 268 ? 1.4596 0.9186 1.0249 0.3955  0.0413  0.1816  273 GLU B CA  
4100 C C   . GLU B 268 ? 1.4381 0.8002 0.9528 0.3568  0.0755  0.1770  273 GLU B C   
4101 O O   . GLU B 268 ? 1.4726 0.7897 0.9453 0.3458  0.0816  0.1823  273 GLU B O   
4102 C CB  . GLU B 268 ? 1.5976 1.0236 1.1150 0.4621  0.0442  0.2021  273 GLU B CB  
4103 C CG  . GLU B 268 ? 1.5592 1.0823 1.1183 0.5018  0.0033  0.2071  273 GLU B CG  
4104 C CD  . GLU B 268 ? 1.6231 1.1343 1.1365 0.5103  -0.0188 0.2142  273 GLU B CD  
4105 O OE1 . GLU B 268 ? 1.6596 1.2099 1.1664 0.5607  -0.0471 0.2243  273 GLU B OE1 
4106 O OE2 . GLU B 268 ? 1.6162 1.0830 1.1013 0.4703  -0.0083 0.2096  273 GLU B OE2 
4107 N N   . ALA B 269 ? 1.4048 0.7362 0.9237 0.3359  0.0980  0.1663  274 ALA B N   
4108 C CA  . ALA B 269 ? 1.4327 0.6902 0.9212 0.2894  0.1255  0.1550  274 ALA B CA  
4109 C C   . ALA B 269 ? 1.3547 0.6594 0.8875 0.2362  0.1130  0.1399  274 ALA B C   
4110 O O   . ALA B 269 ? 1.3511 0.6048 0.8607 0.2017  0.1319  0.1342  274 ALA B O   
4111 C CB  . ALA B 269 ? 1.4798 0.6985 0.9610 0.2812  0.1468  0.1434  274 ALA B CB  
4112 N N   . ARG B 270 ? 1.3013 0.7014 0.8988 0.2294  0.0842  0.1331  275 ARG B N   
4113 C CA  . ARG B 270 ? 1.2162 0.6620 0.8546 0.1852  0.0724  0.1199  275 ARG B CA  
4114 C C   . ARG B 270 ? 1.1765 0.6192 0.7960 0.1854  0.0653  0.1284  275 ARG B C   
4115 O O   . ARG B 270 ? 1.2158 0.6672 0.8169 0.2221  0.0515  0.1415  275 ARG B O   
4116 C CB  . ARG B 270 ? 1.1590 0.6959 0.8640 0.1798  0.0480  0.1116  275 ARG B CB  
4117 C CG  . ARG B 270 ? 1.1320 0.6799 0.8570 0.1818  0.0551  0.1041  275 ARG B CG  
4118 C CD  . ARG B 270 ? 1.0531 0.6880 0.8404 0.1842  0.0353  0.1010  275 ARG B CD  
4119 N NE  . ARG B 270 ? 1.0544 0.6970 0.8526 0.2052  0.0458  0.1014  275 ARG B NE  
4120 C CZ  . ARG B 270 ? 1.0247 0.7340 0.8719 0.2229  0.0370  0.1043  275 ARG B CZ  
4121 N NH1 . ARG B 270 ? 0.9590 0.7365 0.8523 0.2195  0.0139  0.1047  275 ARG B NH1 
4122 N NH2 . ARG B 270 ? 1.0864 0.7929 0.9372 0.2437  0.0538  0.1056  275 ARG B NH2 
4123 N N   . PRO B 271 ? 1.1077 0.5428 0.7326 0.1466  0.0734  0.1203  276 PRO B N   
4124 C CA  . PRO B 271 ? 1.0936 0.5217 0.6966 0.1470  0.0711  0.1281  276 PRO B CA  
4125 C C   . PRO B 271 ? 1.0275 0.5342 0.6715 0.1484  0.0388  0.1241  276 PRO B C   
4126 O O   . PRO B 271 ? 1.0651 0.6319 0.7583 0.1461  0.0205  0.1158  276 PRO B O   
4127 C CB  . PRO B 271 ? 1.1168 0.5151 0.7216 0.1035  0.0955  0.1190  276 PRO B CB  
4128 C CG  . PRO B 271 ? 1.0748 0.5138 0.7307 0.0761  0.0894  0.1011  276 PRO B CG  
4129 C CD  . PRO B 271 ? 1.0763 0.5215 0.7334 0.1029  0.0813  0.1025  276 PRO B CD  
4130 N N   . THR B 272 ? 1.0833 0.5812 0.7006 0.1523  0.0351  0.1300  277 THR B N   
4131 C CA  . THR B 272 ? 1.0337 0.5903 0.6788 0.1474  0.0087  0.1237  277 THR B CA  
4132 C C   . THR B 272 ? 1.0505 0.6166 0.7212 0.1082  0.0208  0.1135  277 THR B C   
4133 O O   . THR B 272 ? 1.1078 0.6313 0.7648 0.0891  0.0489  0.1140  277 THR B O   
4134 C CB  . THR B 272 ? 1.0774 0.6102 0.6672 0.1759  -0.0011 0.1346  277 THR B CB  
4135 O OG1 . THR B 272 ? 1.1703 0.6307 0.7059 0.1698  0.0311  0.1440  277 THR B OG1 
4136 C CG2 . THR B 272 ? 1.1545 0.6836 0.7180 0.2213  -0.0167 0.1455  277 THR B CG2 
4137 N N   . PHE B 273 ? 0.9920 0.6130 0.6999 0.0967  0.0007  0.1040  278 PHE B N   
4138 C CA  . PHE B 273 ? 0.9660 0.6003 0.6974 0.0664  0.0105  0.0957  278 PHE B CA  
4139 C C   . PHE B 273 ? 0.9900 0.5794 0.6811 0.0619  0.0335  0.1024  278 PHE B C   
4140 O O   . PHE B 273 ? 1.0447 0.6281 0.7530 0.0370  0.0556  0.0984  278 PHE B O   
4141 C CB  . PHE B 273 ? 0.9596 0.6503 0.7295 0.0591  -0.0126 0.0858  278 PHE B CB  
4142 C CG  . PHE B 273 ? 0.8531 0.5852 0.6715 0.0510  -0.0218 0.0782  278 PHE B CG  
4143 C CD1 . PHE B 273 ? 0.7949 0.5336 0.6387 0.0302  -0.0096 0.0719  278 PHE B CD1 
4144 C CD2 . PHE B 273 ? 0.8586 0.6245 0.6970 0.0650  -0.0420 0.0769  278 PHE B CD2 
4145 C CE1 . PHE B 273 ? 0.7967 0.5651 0.6733 0.0261  -0.0160 0.0662  278 PHE B CE1 
4146 C CE2 . PHE B 273 ? 0.8416 0.6400 0.7209 0.0580  -0.0439 0.0716  278 PHE B CE2 
4147 C CZ  . PHE B 273 ? 0.7940 0.5890 0.6867 0.0398  -0.0303 0.0670  278 PHE B CZ  
4148 N N   . PRO B 274 ? 1.0631 0.6222 0.7005 0.0867  0.0292  0.1121  279 PRO B N   
4149 C CA  . PRO B 274 ? 1.1388 0.6387 0.7242 0.0873  0.0593  0.1224  279 PRO B CA  
4150 C C   . PRO B 274 ? 1.1833 0.6292 0.7530 0.0774  0.0943  0.1294  279 PRO B C   
4151 O O   . PRO B 274 ? 1.2354 0.6565 0.8039 0.0555  0.1261  0.1302  279 PRO B O   
4152 C CB  . PRO B 274 ? 1.1630 0.6362 0.6842 0.1243  0.0425  0.1324  279 PRO B CB  
4153 C CG  . PRO B 274 ? 1.1085 0.6468 0.6657 0.1287  0.0017  0.1200  279 PRO B CG  
4154 C CD  . PRO B 274 ? 1.0799 0.6640 0.7046 0.1119  -0.0045 0.1115  279 PRO B CD  
4155 N N   . GLY B 275 ? 1.2140 0.6423 0.7738 0.0928  0.0899  0.1333  280 GLY B N   
4156 C CA  . GLY B 275 ? 1.2658 0.6415 0.8146 0.0799  0.1209  0.1356  280 GLY B CA  
4157 C C   . GLY B 275 ? 1.2182 0.6248 0.8282 0.0367  0.1314  0.1187  280 GLY B C   
4158 O O   . GLY B 275 ? 1.3081 0.6768 0.9146 0.0110  0.1641  0.1171  280 GLY B O   
4159 N N   . ILE B 276 ? 1.1604 0.6367 0.8260 0.0287  0.1038  0.1058  281 ILE B N   
4160 C CA  . ILE B 276 ? 1.1325 0.6482 0.8550 -0.0066 0.1058  0.0890  281 ILE B CA  
4161 C C   . ILE B 276 ? 1.1366 0.6697 0.8803 -0.0291 0.1211  0.0858  281 ILE B C   
4162 O O   . ILE B 276 ? 1.1518 0.6843 0.9218 -0.0592 0.1407  0.0765  281 ILE B O   
4163 C CB  . ILE B 276 ? 1.0792 0.6590 0.8457 -0.0039 0.0746  0.0791  281 ILE B CB  
4164 C CG1 . ILE B 276 ? 1.0781 0.6431 0.8312 0.0156  0.0666  0.0811  281 ILE B CG1 
4165 C CG2 . ILE B 276 ? 1.0940 0.7134 0.9097 -0.0340 0.0738  0.0629  281 ILE B CG2 
4166 C CD1 . ILE B 276 ? 1.0444 0.6653 0.8304 0.0271  0.0398  0.0772  281 ILE B CD1 
4167 N N   . GLU B 277 ? 1.1362 0.6853 0.8692 -0.0143 0.1123  0.0921  282 GLU B N   
4168 C CA  . GLU B 277 ? 1.0898 0.6553 0.8385 -0.0281 0.1279  0.0909  282 GLU B CA  
4169 C C   . GLU B 277 ? 1.1279 0.6423 0.8544 -0.0428 0.1699  0.0975  282 GLU B C   
4170 O O   . GLU B 277 ? 1.0956 0.6364 0.8644 -0.0684 0.1882  0.0901  282 GLU B O   
4171 C CB  . GLU B 277 ? 1.1345 0.7075 0.8568 -0.0052 0.1128  0.0968  282 GLU B CB  
4172 C CG  . GLU B 277 ? 1.2168 0.8172 0.9615 -0.0152 0.1238  0.0933  282 GLU B CG  
4173 C CD  . GLU B 277 ? 1.4086 0.9986 1.1116 0.0074  0.1125  0.0979  282 GLU B CD  
4174 O OE1 . GLU B 277 ? 1.6346 1.2204 1.3307 0.0060  0.1323  0.0997  282 GLU B OE1 
4175 O OE2 . GLU B 277 ? 1.5160 1.1036 1.1941 0.0265  0.0843  0.0983  282 GLU B OE2 
4176 N N   . GLU B 278 ? 1.2984 0.7415 0.9598 -0.0249 0.1858  0.1119  283 GLU B N   
4177 C CA  . GLU B 278 ? 1.4084 0.7860 1.0369 -0.0377 0.2325  0.1211  283 GLU B CA  
4178 C C   . GLU B 278 ? 1.4413 0.8154 1.1125 -0.0774 0.2543  0.1082  283 GLU B C   
4179 O O   . GLU B 278 ? 1.4635 0.8214 1.1491 -0.1049 0.2923  0.1072  283 GLU B O   
4180 C CB  . GLU B 278 ? 1.4444 0.7378 0.9829 -0.0036 0.2434  0.1412  283 GLU B CB  
4181 C CG  . GLU B 278 ? 1.4809 0.7413 0.9840 0.0202  0.2293  0.1469  283 GLU B CG  
4182 C CD  . GLU B 278 ? 1.5765 0.7532 0.9840 0.0600  0.2430  0.1696  283 GLU B CD  
4183 O OE1 . GLU B 278 ? 1.5987 0.7658 0.9624 0.0835  0.2391  0.1797  283 GLU B OE1 
4184 O OE2 . GLU B 278 ? 1.6316 0.7476 1.0013 0.0708  0.2571  0.1773  283 GLU B OE2 
4185 N N   . LYS B 279 ? 1.4403 0.8303 1.1324 -0.0815 0.2314  0.0968  284 LYS B N   
4186 C CA  . LYS B 279 ? 1.3951 0.7877 1.1279 -0.1203 0.2430  0.0788  284 LYS B CA  
4187 C C   . LYS B 279 ? 1.1804 0.6641 0.9960 -0.1478 0.2266  0.0590  284 LYS B C   
4188 O O   . LYS B 279 ? 1.1604 0.6581 1.0179 -0.1844 0.2484  0.0468  284 LYS B O   
4189 C CB  . LYS B 279 ? 1.3051 0.6707 1.0167 -0.1097 0.2265  0.0742  284 LYS B CB  
4190 C CG  . LYS B 279 ? 1.3987 0.6918 1.0366 -0.0728 0.2313  0.0924  284 LYS B CG  
4191 C CD  . LYS B 279 ? 1.3932 0.6758 1.0237 -0.0614 0.2139  0.0856  284 LYS B CD  
4192 C CE  . LYS B 279 ? 1.3921 0.6687 0.9829 -0.0105 0.1921  0.1024  284 LYS B CE  
4193 N NZ  . LYS B 279 ? 1.4773 0.6773 0.9935 0.0196  0.2142  0.1252  284 LYS B NZ  
4194 N N   . PHE B 280 ? 1.0142 0.5588 0.8523 -0.1292 0.1896  0.0563  285 PHE B N   
4195 C CA  . PHE B 280 ? 0.9630 0.5888 0.8699 -0.1471 0.1694  0.0388  285 PHE B CA  
4196 C C   . PHE B 280 ? 0.9970 0.6682 0.9445 -0.1573 0.1836  0.0387  285 PHE B C   
4197 O O   . PHE B 280 ? 1.1481 0.8769 1.1571 -0.1815 0.1808  0.0227  285 PHE B O   
4198 C CB  . PHE B 280 ? 0.9165 0.5811 0.8275 -0.1232 0.1304  0.0375  285 PHE B CB  
4199 C CG  . PHE B 280 ? 0.8881 0.6225 0.8551 -0.1364 0.1086  0.0205  285 PHE B CG  
4200 C CD1 . PHE B 280 ? 0.9008 0.6406 0.8831 -0.1548 0.0991  0.0033  285 PHE B CD1 
4201 C CD2 . PHE B 280 ? 0.8856 0.6758 0.8838 -0.1280 0.0979  0.0214  285 PHE B CD2 
4202 C CE1 . PHE B 280 ? 0.9098 0.7138 0.9364 -0.1628 0.0760  -0.0124 285 PHE B CE1 
4203 C CE2 . PHE B 280 ? 0.8451 0.6972 0.8885 -0.1340 0.0773  0.0077  285 PHE B CE2 
4204 C CZ  . PHE B 280 ? 0.8229 0.6842 0.8802 -0.1505 0.0647  -0.0090 285 PHE B CZ  
4205 N N   . ARG B 281 ? 0.9958 0.6455 0.9094 -0.1363 0.1966  0.0553  286 ARG B N   
4206 C CA  . ARG B 281 ? 0.9455 0.6334 0.8911 -0.1401 0.2134  0.0568  286 ARG B CA  
4207 C C   . ARG B 281 ? 0.9683 0.6645 0.9579 -0.1763 0.2511  0.0495  286 ARG B C   
4208 O O   . ARG B 281 ? 0.9332 0.7023 0.9913 -0.1904 0.2490  0.0380  286 ARG B O   
4209 C CB  . ARG B 281 ? 0.9782 0.6276 0.8651 -0.1100 0.2227  0.0751  286 ARG B CB  
4210 C CG  . ARG B 281 ? 0.9616 0.6541 0.8773 -0.1057 0.2333  0.0758  286 ARG B CG  
4211 C CD  . ARG B 281 ? 1.0075 0.6541 0.8562 -0.0768 0.2431  0.0911  286 ARG B CD  
4212 N NE  . ARG B 281 ? 0.9747 0.6664 0.8405 -0.0606 0.2226  0.0872  286 ARG B NE  
4213 C CZ  . ARG B 281 ? 0.8861 0.5859 0.7352 -0.0428 0.1854  0.0844  286 ARG B CZ  
4214 N NH1 . ARG B 281 ? 0.9233 0.5951 0.7380 -0.0344 0.1619  0.0860  286 ARG B NH1 
4215 N NH2 . ARG B 281 ? 0.8907 0.6255 0.7572 -0.0319 0.1748  0.0805  286 ARG B NH2 
4216 N N   . PRO B 282 ? 1.0903 0.7138 1.0433 -0.1911 0.2862  0.0559  287 PRO B N   
4217 C CA  . PRO B 282 ? 1.1173 0.7498 1.1207 -0.2335 0.3244  0.0457  287 PRO B CA  
4218 C C   . PRO B 282 ? 1.0552 0.7489 1.1320 -0.2689 0.3035  0.0181  287 PRO B C   
4219 O O   . PRO B 282 ? 1.0802 0.8319 1.2305 -0.3003 0.3188  0.0041  287 PRO B O   
4220 C CB  . PRO B 282 ? 1.1876 0.7121 1.1209 -0.2388 0.3646  0.0593  287 PRO B CB  
4221 C CG  . PRO B 282 ? 1.1883 0.6554 1.0340 -0.1920 0.3487  0.0798  287 PRO B CG  
4222 C CD  . PRO B 282 ? 1.1140 0.6448 0.9802 -0.1697 0.2949  0.0725  287 PRO B CD  
4223 N N   . PHE B 283 ? 1.0034 0.6863 1.0597 -0.2620 0.2689  0.0099  288 PHE B N   
4224 C CA  . PHE B 283 ? 0.9925 0.7307 1.1040 -0.2879 0.2411  -0.0170 288 PHE B CA  
4225 C C   . PHE B 283 ? 0.9031 0.7469 1.0813 -0.2805 0.2106  -0.0268 288 PHE B C   
4226 O O   . PHE B 283 ? 0.9564 0.8672 1.2058 -0.3101 0.2049  -0.0484 288 PHE B O   
4227 C CB  . PHE B 283 ? 1.0562 0.7524 1.1189 -0.2738 0.2135  -0.0201 288 PHE B CB  
4228 C CG  . PHE B 283 ? 1.1602 0.8998 1.2636 -0.2982 0.1857  -0.0483 288 PHE B CG  
4229 C CD1 . PHE B 283 ? 1.2660 0.9850 1.3904 -0.3438 0.2040  -0.0695 288 PHE B CD1 
4230 C CD2 . PHE B 283 ? 1.1182 0.9160 1.2359 -0.2771 0.1422  -0.0549 288 PHE B CD2 
4231 C CE1 . PHE B 283 ? 1.3367 1.0943 1.4931 -0.3670 0.1746  -0.0991 288 PHE B CE1 
4232 C CE2 . PHE B 283 ? 1.1372 0.9719 1.2834 -0.2966 0.1154  -0.0813 288 PHE B CE2 
4233 C CZ  . PHE B 283 ? 1.2313 1.0480 1.3966 -0.3414 0.1291  -0.1045 288 PHE B CZ  
4234 N N   . TYR B 284 ? 0.8513 0.7091 1.0056 -0.2407 0.1901  -0.0120 289 TYR B N   
4235 C CA  . TYR B 284 ? 0.8283 0.7720 1.0324 -0.2258 0.1665  -0.0162 289 TYR B CA  
4236 C C   . TYR B 284 ? 0.9036 0.9019 1.1713 -0.2414 0.1941  -0.0187 289 TYR B C   
4237 O O   . TYR B 284 ? 0.9094 0.9926 1.2461 -0.2491 0.1774  -0.0341 289 TYR B O   
4238 C CB  . TYR B 284 ? 0.8255 0.7557 0.9836 -0.1834 0.1495  0.0016  289 TYR B CB  
4239 C CG  . TYR B 284 ? 0.8236 0.8244 1.0209 -0.1644 0.1349  0.0014  289 TYR B CG  
4240 C CD1 . TYR B 284 ? 0.8021 0.8637 1.0355 -0.1609 0.1014  -0.0122 289 TYR B CD1 
4241 C CD2 . TYR B 284 ? 0.8814 0.8831 1.0735 -0.1469 0.1564  0.0152  289 TYR B CD2 
4242 C CE1 . TYR B 284 ? 0.8442 0.9654 1.1085 -0.1387 0.0899  -0.0106 289 TYR B CE1 
4243 C CE2 . TYR B 284 ? 0.8634 0.9234 1.0876 -0.1264 0.1464  0.0155  289 TYR B CE2 
4244 C CZ  . TYR B 284 ? 0.8419 0.9616 1.1027 -0.1212 0.1133  0.0035  289 TYR B CZ  
4245 O OH  . TYR B 284 ? 0.8521 1.0239 1.1386 -0.0956 0.1047  0.0059  289 TYR B OH  
4246 N N   . LEU B 285 ? 1.0080 0.9577 1.2509 -0.2439 0.2369  -0.0034 290 LEU B N   
4247 C CA  . LEU B 285 ? 1.0872 1.0801 1.3854 -0.2567 0.2726  -0.0024 290 LEU B CA  
4248 C C   . LEU B 285 ? 1.1248 1.1631 1.5019 -0.3062 0.2888  -0.0247 290 LEU B C   
4249 O O   . LEU B 285 ? 1.0640 1.1946 1.5251 -0.3157 0.2896  -0.0359 290 LEU B O   
4250 C CB  . LEU B 285 ? 1.1977 1.1128 1.4341 -0.2445 0.3178  0.0212  290 LEU B CB  
4251 C CG  . LEU B 285 ? 1.1897 1.0783 1.3635 -0.1979 0.3067  0.0401  290 LEU B CG  
4252 C CD1 . LEU B 285 ? 1.2562 1.0505 1.3485 -0.1861 0.3443  0.0611  290 LEU B CD1 
4253 C CD2 . LEU B 285 ? 1.1549 1.1191 1.3796 -0.1807 0.3064  0.0398  290 LEU B CD2 
4254 N N   . SER B 286 ? 1.1810 1.1546 1.5316 -0.3369 0.3022  -0.0317 291 SER B N   
4255 C CA  . SER B 286 ? 1.1775 1.1799 1.5969 -0.3916 0.3199  -0.0562 291 SER B CA  
4256 C C   . SER B 286 ? 1.1089 1.1996 1.5924 -0.4065 0.2697  -0.0864 291 SER B C   
4257 O O   . SER B 286 ? 1.0499 1.2308 1.6274 -0.4358 0.2706  -0.1069 291 SER B O   
4258 C CB  . SER B 286 ? 1.2234 1.1150 1.5836 -0.4188 0.3514  -0.0548 291 SER B CB  
4259 O OG  . SER B 286 ? 1.2038 1.0387 1.4946 -0.3997 0.3183  -0.0543 291 SER B OG  
4260 N N   . GLN B 287 ? 1.0402 1.1080 1.4734 -0.3845 0.2264  -0.0892 292 GLN B N   
4261 C CA  . GLN B 287 ? 1.0018 1.1315 1.4723 -0.3962 0.1785  -0.1177 292 GLN B CA  
4262 C C   . GLN B 287 ? 0.9121 1.1270 1.4076 -0.3571 0.1349  -0.1168 292 GLN B C   
4263 O O   . GLN B 287 ? 0.8691 1.1797 1.4386 -0.3682 0.1113  -0.1379 292 GLN B O   
4264 C CB  . GLN B 287 ? 1.0166 1.0640 1.4129 -0.3967 0.1614  -0.1228 292 GLN B CB  
4265 C CG  . GLN B 287 ? 1.0687 1.0165 1.4245 -0.4305 0.2001  -0.1246 292 GLN B CG  
4266 C CD  . GLN B 287 ? 1.0932 1.0689 1.5192 -0.4910 0.2214  -0.1527 292 GLN B CD  
4267 O OE1 . GLN B 287 ? 1.1130 1.0922 1.5516 -0.5229 0.2007  -0.1828 292 GLN B OE1 
4268 N NE2 . GLN B 287 ? 1.1153 1.1113 1.5878 -0.5085 0.2639  -0.1446 292 GLN B NE2 
4269 N N   . LEU B 288 ? 0.9394 1.1182 1.3725 -0.3115 0.1245  -0.0931 293 LEU B N   
4270 C CA  . LEU B 288 ? 0.9837 1.2134 1.4150 -0.2744 0.0809  -0.0928 293 LEU B CA  
4271 C C   . LEU B 288 ? 1.0691 1.3786 1.5503 -0.2480 0.0792  -0.0848 293 LEU B C   
4272 O O   . LEU B 288 ? 1.1979 1.5807 1.7141 -0.2334 0.0447  -0.0960 293 LEU B O   
4273 C CB  . LEU B 288 ? 0.9109 1.0662 1.2564 -0.2419 0.0697  -0.0745 293 LEU B CB  
4274 C CG  . LEU B 288 ? 0.9716 1.0475 1.2631 -0.2582 0.0710  -0.0797 293 LEU B CG  
4275 C CD1 . LEU B 288 ? 0.9499 0.9736 1.1720 -0.2221 0.0578  -0.0617 293 LEU B CD1 
4276 C CD2 . LEU B 288 ? 1.0062 1.1067 1.3205 -0.2862 0.0463  -0.1097 293 LEU B CD2 
4277 N N   . GLU B 289 ? 1.1413 1.4333 1.6201 -0.2387 0.1165  -0.0656 294 GLU B N   
4278 C CA  . GLU B 289 ? 1.0625 1.4230 1.5868 -0.2130 0.1233  -0.0574 294 GLU B CA  
4279 C C   . GLU B 289 ? 1.0715 1.5219 1.6974 -0.2429 0.1395  -0.0744 294 GLU B C   
4280 O O   . GLU B 289 ? 1.0798 1.5543 1.7488 -0.2851 0.1342  -0.0979 294 GLU B O   
4281 C CB  . GLU B 289 ? 1.0694 1.3668 1.5405 -0.1895 0.1582  -0.0308 294 GLU B CB  
4282 C CG  . GLU B 289 ? 1.0341 1.3822 1.5318 -0.1553 0.1670  -0.0199 294 GLU B CG  
4283 C CD  . GLU B 289 ? 1.0062 1.2854 1.4283 -0.1211 0.1801  0.0027  294 GLU B CD  
4284 O OE1 . GLU B 289 ? 0.9906 1.2938 1.4094 -0.0851 0.1710  0.0102  294 GLU B OE1 
4285 O OE2 . GLU B 289 ? 1.0334 1.2301 1.3947 -0.1290 0.1996  0.0126  294 GLU B OE2 
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