data_9LID
# 
_entry.id   9LID 
# 
_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   9LID         pdb_00009lid 10.2210/pdb9lid/pdb 
WWPDB D_1300055612 ?            ?                   
# 
_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       2025-05-14 
_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                        9LID 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9LGL unspecified 
PDB . 9LGN unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bruce.xu@roche.com 
_pdbx_contact_author.name_first         Bruce 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7301-015X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, Z.H.' 1 ? 
'Chen, S.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                8497 
_citation.page_last                 8515 
_citation.title                     
'Discovery of Naphthyridinone Derivatives as Selective and Potent PKMYT1 Inhibitors with Antitumor Efficacy.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00114 
_citation.pdbx_database_id_PubMed   40198752 
_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, B.'   1  ?                   
primary 'Liu, X.'    2  ?                   
primary 'Mu, T.'     3  ?                   
primary 'Xu, J.'     4  ?                   
primary 'Zhao, D.'   5  ?                   
primary 'Dey, F.'    6  0000-0002-4903-2869 
primary 'Tang, Y.'   7  ?                   
primary 'Xu, Z.'     8  ?                   
primary 'Yang, J.'   9  ?                   
primary 'Huang, K.'  10 ?                   
primary 'Li, C.'     11 ?                   
primary 'Chen, S.'   12 0000-0003-0519-816X 
primary 'Zhu, S.'    13 ?                   
primary 'Wang, S.'   14 ?                   
primary 'Yao, X.'    15 ?                   
primary 'Yan, Z.'    16 ?                   
primary 'Tu, Y.'     17 ?                   
primary 'Dai, Y.'    18 ?                   
primary 'Qiu, H.'    19 ?                   
primary 'Yang, J.'   20 ?                   
primary 'Jiang, T.'  21 ?                   
primary 'Qi, Y.'     22 ?                   
primary 'Li, Y.'     23 ?                   
primary 'Shen, H.C.' 24 0000-0002-3477-8932 
primary 'Zhu, W.'    25 0000-0003-4701-2474 
primary 'Tan, X.'    26 0000-0001-7629-2255 
primary 'Wu, J.'     27 0000-0002-5971-5057 
# 
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 'Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase'                                  
31808.197 2   2.7.11.1 ? ? ? 
2 non-polymer syn '4-[7-azanyl-8-(7-fluoranyl-1H-indazol-4-yl)-6-oxidanylidene-5H-1,5-naphthyridin-3-yl]-N,N-dimethyl-benzamide' 
442.445   2   ?        ? ? ? 
3 non-polymer nat 'SULFATE ION'                                                                                                  
96.063    10  ?        ? ? ? 
4 water       nat water                                                                                                          
18.015    111 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Myt1 kinase' 
# 
_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       
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_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 '4-[7-azanyl-8-(7-fluoranyl-1H-indazol-4-yl)-6-oxidanylidene-5H-1,5-naphthyridin-3-yl]-N,N-dimethyl-benzamide' A1EJX 
3 'SULFATE ION'                                                                                                  SO4   
4 water                                                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   GLN n 
1 3   LEU n 
1 4   GLN n 
1 5   PRO n 
1 6   ARG n 
1 7   ARG n 
1 8   VAL n 
1 9   SER n 
1 10  PHE n 
1 11  ARG n 
1 12  GLY n 
1 13  GLU n 
1 14  ALA n 
1 15  SER n 
1 16  GLU n 
1 17  THR n 
1 18  LEU n 
1 19  GLN n 
1 20  SER n 
1 21  PRO n 
1 22  GLY n 
1 23  TYR n 
1 24  ASP n 
1 25  PRO n 
1 26  SER n 
1 27  ARG n 
1 28  PRO n 
1 29  GLU n 
1 30  SER n 
1 31  PHE n 
1 32  PHE n 
1 33  GLN n 
1 34  GLN n 
1 35  SER n 
1 36  PHE n 
1 37  GLN n 
1 38  ARG n 
1 39  LEU n 
1 40  SER n 
1 41  ARG n 
1 42  LEU n 
1 43  GLY n 
1 44  HIS n 
1 45  GLY n 
1 46  SER n 
1 47  TYR n 
1 48  GLY n 
1 49  GLU n 
1 50  VAL n 
1 51  PHE n 
1 52  LYS n 
1 53  VAL n 
1 54  ARG n 
1 55  SER n 
1 56  LYS n 
1 57  GLU n 
1 58  ASP n 
1 59  GLY n 
1 60  ARG n 
1 61  LEU n 
1 62  TYR n 
1 63  ALA n 
1 64  VAL n 
1 65  LYS n 
1 66  ARG n 
1 67  SER n 
1 68  MET n 
1 69  SER n 
1 70  PRO n 
1 71  PHE n 
1 72  ARG n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  ARG n 
1 78  ALA n 
1 79  ARG n 
1 80  LYS n 
1 81  LEU n 
1 82  ALA n 
1 83  GLU n 
1 84  VAL n 
1 85  GLY n 
1 86  SER n 
1 87  HIS n 
1 88  GLU n 
1 89  LYS n 
1 90  VAL n 
1 91  GLY n 
1 92  GLN n 
1 93  HIS n 
1 94  PRO n 
1 95  CYS n 
1 96  CYS n 
1 97  VAL n 
1 98  ARG n 
1 99  LEU n 
1 100 GLU n 
1 101 GLN n 
1 102 ALA n 
1 103 TRP n 
1 104 GLU n 
1 105 GLU n 
1 106 GLY n 
1 107 GLY n 
1 108 ILE n 
1 109 LEU n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 THR n 
1 114 GLU n 
1 115 LEU n 
1 116 CYS n 
1 117 GLY n 
1 118 PRO n 
1 119 SER n 
1 120 LEU n 
1 121 GLN n 
1 122 GLN n 
1 123 HIS n 
1 124 CYS n 
1 125 GLU n 
1 126 ALA n 
1 127 TRP n 
1 128 GLY n 
1 129 ALA n 
1 130 SER n 
1 131 LEU n 
1 132 PRO n 
1 133 GLU n 
1 134 ALA n 
1 135 GLN n 
1 136 VAL n 
1 137 TRP n 
1 138 GLY n 
1 139 TYR n 
1 140 LEU n 
1 141 ARG n 
1 142 ASP n 
1 143 THR n 
1 144 LEU n 
1 145 LEU n 
1 146 ALA n 
1 147 LEU n 
1 148 ALA n 
1 149 HIS n 
1 150 LEU n 
1 151 HIS n 
1 152 SER n 
1 153 GLN n 
1 154 GLY n 
1 155 LEU n 
1 156 VAL n 
1 157 HIS n 
1 158 LEU n 
1 159 ASP n 
1 160 VAL n 
1 161 LYS n 
1 162 PRO n 
1 163 ALA n 
1 164 ASN n 
1 165 ILE n 
1 166 PHE n 
1 167 LEU n 
1 168 GLY n 
1 169 PRO n 
1 170 ARG n 
1 171 GLY n 
1 172 ARG n 
1 173 CYS n 
1 174 LYS n 
1 175 LEU n 
1 176 GLY n 
1 177 ASP n 
1 178 PHE n 
1 179 GLY n 
1 180 LEU n 
1 181 LEU n 
1 182 VAL n 
1 183 GLU n 
1 184 LEU n 
1 185 GLY n 
1 186 THR n 
1 187 ALA n 
1 188 GLY n 
1 189 ALA n 
1 190 GLY n 
1 191 GLU n 
1 192 VAL n 
1 193 GLN n 
1 194 GLU n 
1 195 GLY n 
1 196 ASP n 
1 197 PRO n 
1 198 ARG n 
1 199 TYR n 
1 200 MET n 
1 201 ALA n 
1 202 PRO n 
1 203 GLU n 
1 204 LEU n 
1 205 LEU n 
1 206 GLN n 
1 207 GLY n 
1 208 SER n 
1 209 TYR n 
1 210 GLY n 
1 211 THR n 
1 212 ALA n 
1 213 ALA n 
1 214 ASP n 
1 215 VAL n 
1 216 PHE n 
1 217 SER n 
1 218 LEU n 
1 219 GLY n 
1 220 LEU n 
1 221 THR n 
1 222 ILE n 
1 223 LEU n 
1 224 GLU n 
1 225 VAL n 
1 226 ALA n 
1 227 CYS n 
1 228 ASN n 
1 229 MET n 
1 230 GLU n 
1 231 LEU n 
1 232 PRO n 
1 233 HIS n 
1 234 GLY n 
1 235 GLY n 
1 236 GLU n 
1 237 GLY n 
1 238 TRP n 
1 239 GLN n 
1 240 GLN n 
1 241 LEU n 
1 242 ARG n 
1 243 GLN n 
1 244 GLY n 
1 245 TYR n 
1 246 LEU n 
1 247 PRO n 
1 248 PRO n 
1 249 GLU n 
1 250 PHE n 
1 251 THR n 
1 252 ALA n 
1 253 GLY n 
1 254 LEU n 
1 255 SER n 
1 256 SER n 
1 257 GLU n 
1 258 LEU n 
1 259 ARG n 
1 260 SER n 
1 261 VAL n 
1 262 LEU n 
1 263 VAL n 
1 264 MET n 
1 265 MET n 
1 266 LEU n 
1 267 GLU n 
1 268 PRO n 
1 269 ASP n 
1 270 PRO n 
1 271 LYS n 
1 272 LEU n 
1 273 ARG n 
1 274 ALA n 
1 275 THR n 
1 276 ALA n 
1 277 GLU n 
1 278 ALA n 
1 279 LEU n 
1 280 LEU n 
1 281 ALA n 
1 282 LEU n 
1 283 PRO n 
1 284 VAL n 
1 285 LEU n 
1 286 ARG n 
1 287 GLN n 
1 288 PRO 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                   288 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PKMYT1, MYT1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'Homo sapiens' 
_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              9606 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              'Escherichia coli' 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 469008 
_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 
A1EJX non-polymer         . 
'4-[7-azanyl-8-(7-fluoranyl-1H-indazol-4-yl)-6-oxidanylidene-5H-1,5-naphthyridin-3-yl]-N,N-dimethyl-benzamide' ? 'C24 H19 F N6 O2' 
442.445 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   75  ?   ?   ?   A . n 
A 1 2   GLN 2   76  ?   ?   ?   A . n 
A 1 3   LEU 3   77  77  LEU LEU A . n 
A 1 4   GLN 4   78  78  GLN GLN A . n 
A 1 5   PRO 5   79  79  PRO PRO A . n 
A 1 6   ARG 6   80  80  ARG ARG A . n 
A 1 7   ARG 7   81  81  ARG ARG A . n 
A 1 8   VAL 8   82  82  VAL VAL A . n 
A 1 9   SER 9   83  83  SER SER A . n 
A 1 10  PHE 10  84  84  PHE PHE A . n 
A 1 11  ARG 11  85  85  ARG ARG A . n 
A 1 12  GLY 12  86  ?   ?   ?   A . n 
A 1 13  GLU 13  87  ?   ?   ?   A . n 
A 1 14  ALA 14  88  ?   ?   ?   A . n 
A 1 15  SER 15  89  ?   ?   ?   A . n 
A 1 16  GLU 16  90  ?   ?   ?   A . n 
A 1 17  THR 17  91  ?   ?   ?   A . n 
A 1 18  LEU 18  92  ?   ?   ?   A . n 
A 1 19  GLN 19  93  ?   ?   ?   A . n 
A 1 20  SER 20  94  94  SER SER A . n 
A 1 21  PRO 21  95  95  PRO PRO A . n 
A 1 22  GLY 22  96  96  GLY GLY A . n 
A 1 23  TYR 23  97  97  TYR TYR A . n 
A 1 24  ASP 24  98  98  ASP ASP A . n 
A 1 25  PRO 25  99  99  PRO PRO A . n 
A 1 26  SER 26  100 100 SER SER A . n 
A 1 27  ARG 27  101 101 ARG ARG A . n 
A 1 28  PRO 28  102 102 PRO PRO A . n 
A 1 29  GLU 29  103 103 GLU GLU A . n 
A 1 30  SER 30  104 104 SER SER A . n 
A 1 31  PHE 31  105 105 PHE PHE A . n 
A 1 32  PHE 32  106 106 PHE PHE A . n 
A 1 33  GLN 33  107 107 GLN GLN A . n 
A 1 34  GLN 34  108 108 GLN GLN A . n 
A 1 35  SER 35  109 109 SER SER A . n 
A 1 36  PHE 36  110 110 PHE PHE A . n 
A 1 37  GLN 37  111 111 GLN GLN A . n 
A 1 38  ARG 38  112 112 ARG ARG A . n 
A 1 39  LEU 39  113 113 LEU LEU A . n 
A 1 40  SER 40  114 114 SER SER A . n 
A 1 41  ARG 41  115 115 ARG ARG A . n 
A 1 42  LEU 42  116 116 LEU LEU A . n 
A 1 43  GLY 43  117 117 GLY GLY A . n 
A 1 44  HIS 44  118 118 HIS HIS A . n 
A 1 45  GLY 45  119 119 GLY GLY A . n 
A 1 46  SER 46  120 120 SER SER A . n 
A 1 47  TYR 47  121 121 TYR TYR A . n 
A 1 48  GLY 48  122 122 GLY GLY A . n 
A 1 49  GLU 49  123 123 GLU GLU A . n 
A 1 50  VAL 50  124 124 VAL VAL A . n 
A 1 51  PHE 51  125 125 PHE PHE A . n 
A 1 52  LYS 52  126 126 LYS LYS A . n 
A 1 53  VAL 53  127 127 VAL VAL A . n 
A 1 54  ARG 54  128 128 ARG ARG A . n 
A 1 55  SER 55  129 129 SER SER A . n 
A 1 56  LYS 56  130 130 LYS LYS A . n 
A 1 57  GLU 57  131 131 GLU GLU A . n 
A 1 58  ASP 58  132 132 ASP ASP A . n 
A 1 59  GLY 59  133 133 GLY GLY A . n 
A 1 60  ARG 60  134 134 ARG ARG A . n 
A 1 61  LEU 61  135 135 LEU LEU A . n 
A 1 62  TYR 62  136 136 TYR TYR A . n 
A 1 63  ALA 63  137 137 ALA ALA A . n 
A 1 64  VAL 64  138 138 VAL VAL A . n 
A 1 65  LYS 65  139 139 LYS LYS A . n 
A 1 66  ARG 66  140 140 ARG ARG A . n 
A 1 67  SER 67  141 141 SER SER A . n 
A 1 68  MET 68  142 142 MET MET A . n 
A 1 69  SER 69  143 143 SER SER A . n 
A 1 70  PRO 70  144 144 PRO PRO A . n 
A 1 71  PHE 71  145 145 PHE PHE A . n 
A 1 72  ARG 72  146 146 ARG ARG A . n 
A 1 73  GLY 73  147 147 GLY GLY A . n 
A 1 74  PRO 74  148 148 PRO PRO A . n 
A 1 75  LYS 75  149 149 LYS LYS A . n 
A 1 76  ASP 76  150 150 ASP ASP A . n 
A 1 77  ARG 77  151 151 ARG ARG A . n 
A 1 78  ALA 78  152 152 ALA ALA A . n 
A 1 79  ARG 79  153 153 ARG ARG A . n 
A 1 80  LYS 80  154 154 LYS LYS A . n 
A 1 81  LEU 81  155 155 LEU LEU A . n 
A 1 82  ALA 82  156 156 ALA ALA A . n 
A 1 83  GLU 83  157 157 GLU GLU A . n 
A 1 84  VAL 84  158 158 VAL VAL A . n 
A 1 85  GLY 85  159 159 GLY GLY A . n 
A 1 86  SER 86  160 160 SER SER A . n 
A 1 87  HIS 87  161 161 HIS HIS A . n 
A 1 88  GLU 88  162 162 GLU GLU A . n 
A 1 89  LYS 89  163 163 LYS LYS A . n 
A 1 90  VAL 90  164 164 VAL VAL A . n 
A 1 91  GLY 91  165 165 GLY GLY A . n 
A 1 92  GLN 92  166 166 GLN GLN A . n 
A 1 93  HIS 93  167 167 HIS HIS A . n 
A 1 94  PRO 94  168 168 PRO PRO A . n 
A 1 95  CYS 95  169 169 CYS CYS A . n 
A 1 96  CYS 96  170 170 CYS CYS A . n 
A 1 97  VAL 97  171 171 VAL VAL A . n 
A 1 98  ARG 98  172 172 ARG ARG A . n 
A 1 99  LEU 99  173 173 LEU LEU A . n 
A 1 100 GLU 100 174 174 GLU GLU A . n 
A 1 101 GLN 101 175 175 GLN GLN A . n 
A 1 102 ALA 102 176 176 ALA ALA A . n 
A 1 103 TRP 103 177 177 TRP TRP A . n 
A 1 104 GLU 104 178 178 GLU GLU A . n 
A 1 105 GLU 105 179 179 GLU GLU A . n 
A 1 106 GLY 106 180 180 GLY GLY A . n 
A 1 107 GLY 107 181 181 GLY GLY A . n 
A 1 108 ILE 108 182 182 ILE ILE A . n 
A 1 109 LEU 109 183 183 LEU LEU A . n 
A 1 110 TYR 110 184 184 TYR TYR A . n 
A 1 111 LEU 111 185 185 LEU LEU A . n 
A 1 112 GLN 112 186 186 GLN GLN A . n 
A 1 113 THR 113 187 187 THR THR A . n 
A 1 114 GLU 114 188 188 GLU GLU A . n 
A 1 115 LEU 115 189 189 LEU LEU A . n 
A 1 116 CYS 116 190 190 CYS CYS A . n 
A 1 117 GLY 117 191 191 GLY GLY A . n 
A 1 118 PRO 118 192 192 PRO PRO A . n 
A 1 119 SER 119 193 193 SER SER A . n 
A 1 120 LEU 120 194 194 LEU LEU A . n 
A 1 121 GLN 121 195 195 GLN GLN A . n 
A 1 122 GLN 122 196 196 GLN GLN A . n 
A 1 123 HIS 123 197 197 HIS HIS A . n 
A 1 124 CYS 124 198 198 CYS CYS A . n 
A 1 125 GLU 125 199 199 GLU GLU A . n 
A 1 126 ALA 126 200 200 ALA ALA A . n 
A 1 127 TRP 127 201 201 TRP TRP A . n 
A 1 128 GLY 128 202 202 GLY GLY A . n 
A 1 129 ALA 129 203 203 ALA ALA A . n 
A 1 130 SER 130 204 204 SER SER A . n 
A 1 131 LEU 131 205 205 LEU LEU A . n 
A 1 132 PRO 132 206 206 PRO PRO A . n 
A 1 133 GLU 133 207 207 GLU GLU A . n 
A 1 134 ALA 134 208 208 ALA ALA A . n 
A 1 135 GLN 135 209 209 GLN GLN A . n 
A 1 136 VAL 136 210 210 VAL VAL A . n 
A 1 137 TRP 137 211 211 TRP TRP A . n 
A 1 138 GLY 138 212 212 GLY GLY A . n 
A 1 139 TYR 139 213 213 TYR TYR A . n 
A 1 140 LEU 140 214 214 LEU LEU A . n 
A 1 141 ARG 141 215 215 ARG ARG A . n 
A 1 142 ASP 142 216 216 ASP ASP A . n 
A 1 143 THR 143 217 217 THR THR A . n 
A 1 144 LEU 144 218 218 LEU LEU A . n 
A 1 145 LEU 145 219 219 LEU LEU A . n 
A 1 146 ALA 146 220 220 ALA ALA A . n 
A 1 147 LEU 147 221 221 LEU LEU A . n 
A 1 148 ALA 148 222 222 ALA ALA A . n 
A 1 149 HIS 149 223 223 HIS HIS A . n 
A 1 150 LEU 150 224 224 LEU LEU A . n 
A 1 151 HIS 151 225 225 HIS HIS A . n 
A 1 152 SER 152 226 226 SER SER A . n 
A 1 153 GLN 153 227 227 GLN GLN A . n 
A 1 154 GLY 154 228 228 GLY GLY A . n 
A 1 155 LEU 155 229 229 LEU LEU A . n 
A 1 156 VAL 156 230 230 VAL VAL A . n 
A 1 157 HIS 157 231 231 HIS HIS A . n 
A 1 158 LEU 158 232 232 LEU LEU A . n 
A 1 159 ASP 159 233 233 ASP ASP A . n 
A 1 160 VAL 160 234 234 VAL VAL A . n 
A 1 161 LYS 161 235 235 LYS LYS A . n 
A 1 162 PRO 162 236 236 PRO PRO A . n 
A 1 163 ALA 163 237 237 ALA ALA A . n 
A 1 164 ASN 164 238 238 ASN ASN A . n 
A 1 165 ILE 165 239 239 ILE ILE A . n 
A 1 166 PHE 166 240 240 PHE PHE A . n 
A 1 167 LEU 167 241 241 LEU LEU A . n 
A 1 168 GLY 168 242 242 GLY GLY A . n 
A 1 169 PRO 169 243 243 PRO PRO A . n 
A 1 170 ARG 170 244 244 ARG ARG A . n 
A 1 171 GLY 171 245 245 GLY GLY A . n 
A 1 172 ARG 172 246 246 ARG ARG A . n 
A 1 173 CYS 173 247 247 CYS CYS A . n 
A 1 174 LYS 174 248 248 LYS LYS A . n 
A 1 175 LEU 175 249 249 LEU LEU A . n 
A 1 176 GLY 176 250 250 GLY GLY A . n 
A 1 177 ASP 177 251 251 ASP ASP A . n 
A 1 178 PHE 178 252 252 PHE PHE A . n 
A 1 179 GLY 179 253 253 GLY GLY A . n 
A 1 180 LEU 180 254 254 LEU LEU A . n 
A 1 181 LEU 181 255 255 LEU LEU A . n 
A 1 182 VAL 182 256 256 VAL VAL A . n 
A 1 183 GLU 183 257 257 GLU GLU A . n 
A 1 184 LEU 184 258 258 LEU LEU A . n 
A 1 185 GLY 185 259 259 GLY GLY A . n 
A 1 186 THR 186 260 ?   ?   ?   A . n 
A 1 187 ALA 187 261 ?   ?   ?   A . n 
A 1 188 GLY 188 262 ?   ?   ?   A . n 
A 1 189 ALA 189 263 ?   ?   ?   A . n 
A 1 190 GLY 190 264 ?   ?   ?   A . n 
A 1 191 GLU 191 265 265 GLU GLU A . n 
A 1 192 VAL 192 266 266 VAL VAL A . n 
A 1 193 GLN 193 267 267 GLN GLN A . n 
A 1 194 GLU 194 268 268 GLU GLU A . n 
A 1 195 GLY 195 269 269 GLY GLY A . n 
A 1 196 ASP 196 270 270 ASP ASP A . n 
A 1 197 PRO 197 271 271 PRO PRO A . n 
A 1 198 ARG 198 272 272 ARG ARG A . n 
A 1 199 TYR 199 273 273 TYR TYR A . n 
A 1 200 MET 200 274 274 MET MET A . n 
A 1 201 ALA 201 275 275 ALA ALA A . n 
A 1 202 PRO 202 276 276 PRO PRO A . n 
A 1 203 GLU 203 277 277 GLU GLU A . n 
A 1 204 LEU 204 278 278 LEU LEU A . n 
A 1 205 LEU 205 279 279 LEU LEU A . n 
A 1 206 GLN 206 280 280 GLN GLN A . n 
A 1 207 GLY 207 281 281 GLY GLY A . n 
A 1 208 SER 208 282 282 SER SER A . n 
A 1 209 TYR 209 283 283 TYR TYR A . n 
A 1 210 GLY 210 284 284 GLY GLY A . n 
A 1 211 THR 211 285 285 THR THR A . n 
A 1 212 ALA 212 286 286 ALA ALA A . n 
A 1 213 ALA 213 287 287 ALA ALA A . n 
A 1 214 ASP 214 288 288 ASP ASP A . n 
A 1 215 VAL 215 289 289 VAL VAL A . n 
A 1 216 PHE 216 290 290 PHE PHE A . n 
A 1 217 SER 217 291 291 SER SER A . n 
A 1 218 LEU 218 292 292 LEU LEU A . n 
A 1 219 GLY 219 293 293 GLY GLY A . n 
A 1 220 LEU 220 294 294 LEU LEU A . n 
A 1 221 THR 221 295 295 THR THR A . n 
A 1 222 ILE 222 296 296 ILE ILE A . n 
A 1 223 LEU 223 297 297 LEU LEU A . n 
A 1 224 GLU 224 298 298 GLU GLU A . n 
A 1 225 VAL 225 299 299 VAL VAL A . n 
A 1 226 ALA 226 300 300 ALA ALA A . n 
A 1 227 CYS 227 301 301 CYS CYS A . n 
A 1 228 ASN 228 302 302 ASN ASN A . n 
A 1 229 MET 229 303 303 MET MET A . n 
A 1 230 GLU 230 304 304 GLU GLU A . n 
A 1 231 LEU 231 305 305 LEU LEU A . n 
A 1 232 PRO 232 306 306 PRO PRO A . n 
A 1 233 HIS 233 307 307 HIS HIS A . n 
A 1 234 GLY 234 308 308 GLY GLY A . n 
A 1 235 GLY 235 309 309 GLY GLY A . n 
A 1 236 GLU 236 310 310 GLU GLU A . n 
A 1 237 GLY 237 311 311 GLY GLY A . n 
A 1 238 TRP 238 312 312 TRP TRP A . n 
A 1 239 GLN 239 313 313 GLN GLN A . n 
A 1 240 GLN 240 314 314 GLN GLN A . n 
A 1 241 LEU 241 315 315 LEU LEU A . n 
A 1 242 ARG 242 316 316 ARG ARG A . n 
A 1 243 GLN 243 317 317 GLN GLN A . n 
A 1 244 GLY 244 318 318 GLY GLY A . n 
A 1 245 TYR 245 319 319 TYR TYR A . n 
A 1 246 LEU 246 320 320 LEU LEU A . n 
A 1 247 PRO 247 321 321 PRO PRO A . n 
A 1 248 PRO 248 322 322 PRO PRO A . n 
A 1 249 GLU 249 323 323 GLU GLU A . n 
A 1 250 PHE 250 324 324 PHE PHE A . n 
A 1 251 THR 251 325 325 THR THR A . n 
A 1 252 ALA 252 326 326 ALA ALA A . n 
A 1 253 GLY 253 327 327 GLY GLY A . n 
A 1 254 LEU 254 328 328 LEU LEU A . n 
A 1 255 SER 255 329 329 SER SER A . n 
A 1 256 SER 256 330 330 SER SER A . n 
A 1 257 GLU 257 331 331 GLU GLU A . n 
A 1 258 LEU 258 332 332 LEU LEU A . n 
A 1 259 ARG 259 333 333 ARG ARG A . n 
A 1 260 SER 260 334 334 SER SER A . n 
A 1 261 VAL 261 335 335 VAL VAL A . n 
A 1 262 LEU 262 336 336 LEU LEU A . n 
A 1 263 VAL 263 337 337 VAL VAL A . n 
A 1 264 MET 264 338 338 MET MET A . n 
A 1 265 MET 265 339 339 MET MET A . n 
A 1 266 LEU 266 340 340 LEU LEU A . n 
A 1 267 GLU 267 341 341 GLU GLU A . n 
A 1 268 PRO 268 342 342 PRO PRO A . n 
A 1 269 ASP 269 343 343 ASP ASP A . n 
A 1 270 PRO 270 344 344 PRO PRO A . n 
A 1 271 LYS 271 345 345 LYS LYS A . n 
A 1 272 LEU 272 346 346 LEU LEU A . n 
A 1 273 ARG 273 347 347 ARG ARG A . n 
A 1 274 ALA 274 348 348 ALA ALA A . n 
A 1 275 THR 275 349 349 THR THR A . n 
A 1 276 ALA 276 350 350 ALA ALA A . n 
A 1 277 GLU 277 351 351 GLU GLU A . n 
A 1 278 ALA 278 352 352 ALA ALA A . n 
A 1 279 LEU 279 353 353 LEU LEU A . n 
A 1 280 LEU 280 354 354 LEU LEU A . n 
A 1 281 ALA 281 355 355 ALA ALA A . n 
A 1 282 LEU 282 356 356 LEU LEU A . n 
A 1 283 PRO 283 357 357 PRO PRO A . n 
A 1 284 VAL 284 358 358 VAL VAL A . n 
A 1 285 LEU 285 359 359 LEU LEU A . n 
A 1 286 ARG 286 360 360 ARG ARG A . n 
A 1 287 GLN 287 361 361 GLN GLN A . n 
A 1 288 PRO 288 362 ?   ?   ?   A . n 
B 1 1   HIS 1   75  ?   ?   ?   B . n 
B 1 2   GLN 2   76  ?   ?   ?   B . n 
B 1 3   LEU 3   77  77  LEU LEU B . n 
B 1 4   GLN 4   78  78  GLN GLN B . n 
B 1 5   PRO 5   79  79  PRO PRO B . n 
B 1 6   ARG 6   80  80  ARG ARG B . n 
B 1 7   ARG 7   81  81  ARG ARG B . n 
B 1 8   VAL 8   82  82  VAL VAL B . n 
B 1 9   SER 9   83  83  SER SER B . n 
B 1 10  PHE 10  84  84  PHE PHE B . n 
B 1 11  ARG 11  85  85  ARG ARG B . n 
B 1 12  GLY 12  86  86  GLY GLY B . n 
B 1 13  GLU 13  87  ?   ?   ?   B . n 
B 1 14  ALA 14  88  ?   ?   ?   B . n 
B 1 15  SER 15  89  ?   ?   ?   B . n 
B 1 16  GLU 16  90  ?   ?   ?   B . n 
B 1 17  THR 17  91  ?   ?   ?   B . n 
B 1 18  LEU 18  92  ?   ?   ?   B . n 
B 1 19  GLN 19  93  93  GLN GLN B . n 
B 1 20  SER 20  94  94  SER SER B . n 
B 1 21  PRO 21  95  95  PRO PRO B . n 
B 1 22  GLY 22  96  96  GLY GLY B . n 
B 1 23  TYR 23  97  97  TYR TYR B . n 
B 1 24  ASP 24  98  98  ASP ASP B . n 
B 1 25  PRO 25  99  99  PRO PRO B . n 
B 1 26  SER 26  100 100 SER SER B . n 
B 1 27  ARG 27  101 101 ARG ARG B . n 
B 1 28  PRO 28  102 102 PRO PRO B . n 
B 1 29  GLU 29  103 103 GLU GLU B . n 
B 1 30  SER 30  104 104 SER SER B . n 
B 1 31  PHE 31  105 105 PHE PHE B . n 
B 1 32  PHE 32  106 106 PHE PHE B . n 
B 1 33  GLN 33  107 107 GLN GLN B . n 
B 1 34  GLN 34  108 108 GLN GLN B . n 
B 1 35  SER 35  109 109 SER SER B . n 
B 1 36  PHE 36  110 110 PHE PHE B . n 
B 1 37  GLN 37  111 111 GLN GLN B . n 
B 1 38  ARG 38  112 112 ARG ARG B . n 
B 1 39  LEU 39  113 113 LEU LEU B . n 
B 1 40  SER 40  114 114 SER SER B . n 
B 1 41  ARG 41  115 115 ARG ARG B . n 
B 1 42  LEU 42  116 116 LEU LEU B . n 
B 1 43  GLY 43  117 117 GLY GLY B . n 
B 1 44  HIS 44  118 118 HIS HIS B . n 
B 1 45  GLY 45  119 119 GLY GLY B . n 
B 1 46  SER 46  120 120 SER SER B . n 
B 1 47  TYR 47  121 121 TYR TYR B . n 
B 1 48  GLY 48  122 122 GLY GLY B . n 
B 1 49  GLU 49  123 123 GLU GLU B . n 
B 1 50  VAL 50  124 124 VAL VAL B . n 
B 1 51  PHE 51  125 125 PHE PHE B . n 
B 1 52  LYS 52  126 126 LYS LYS B . n 
B 1 53  VAL 53  127 127 VAL VAL B . n 
B 1 54  ARG 54  128 128 ARG ARG B . n 
B 1 55  SER 55  129 129 SER SER B . n 
B 1 56  LYS 56  130 130 LYS LYS B . n 
B 1 57  GLU 57  131 131 GLU GLU B . n 
B 1 58  ASP 58  132 132 ASP ASP B . n 
B 1 59  GLY 59  133 133 GLY GLY B . n 
B 1 60  ARG 60  134 134 ARG ARG B . n 
B 1 61  LEU 61  135 135 LEU LEU B . n 
B 1 62  TYR 62  136 136 TYR TYR B . n 
B 1 63  ALA 63  137 137 ALA ALA B . n 
B 1 64  VAL 64  138 138 VAL VAL B . n 
B 1 65  LYS 65  139 139 LYS LYS B . n 
B 1 66  ARG 66  140 140 ARG ARG B . n 
B 1 67  SER 67  141 141 SER SER B . n 
B 1 68  MET 68  142 142 MET MET B . n 
B 1 69  SER 69  143 143 SER SER B . n 
B 1 70  PRO 70  144 144 PRO PRO B . n 
B 1 71  PHE 71  145 145 PHE PHE B . n 
B 1 72  ARG 72  146 146 ARG ARG B . n 
B 1 73  GLY 73  147 147 GLY GLY B . n 
B 1 74  PRO 74  148 148 PRO PRO B . n 
B 1 75  LYS 75  149 149 LYS LYS B . n 
B 1 76  ASP 76  150 150 ASP ASP B . n 
B 1 77  ARG 77  151 151 ARG ARG B . n 
B 1 78  ALA 78  152 152 ALA ALA B . n 
B 1 79  ARG 79  153 153 ARG ARG B . n 
B 1 80  LYS 80  154 154 LYS LYS B . n 
B 1 81  LEU 81  155 155 LEU LEU B . n 
B 1 82  ALA 82  156 156 ALA ALA B . n 
B 1 83  GLU 83  157 157 GLU GLU B . n 
B 1 84  VAL 84  158 158 VAL VAL B . n 
B 1 85  GLY 85  159 159 GLY GLY B . n 
B 1 86  SER 86  160 160 SER SER B . n 
B 1 87  HIS 87  161 161 HIS HIS B . n 
B 1 88  GLU 88  162 162 GLU GLU B . n 
B 1 89  LYS 89  163 163 LYS LYS B . n 
B 1 90  VAL 90  164 164 VAL VAL B . n 
B 1 91  GLY 91  165 165 GLY GLY B . n 
B 1 92  GLN 92  166 166 GLN GLN B . n 
B 1 93  HIS 93  167 167 HIS HIS B . n 
B 1 94  PRO 94  168 168 PRO PRO B . n 
B 1 95  CYS 95  169 169 CYS CYS B . n 
B 1 96  CYS 96  170 170 CYS CYS B . n 
B 1 97  VAL 97  171 171 VAL VAL B . n 
B 1 98  ARG 98  172 172 ARG ARG B . n 
B 1 99  LEU 99  173 173 LEU LEU B . n 
B 1 100 GLU 100 174 174 GLU GLU B . n 
B 1 101 GLN 101 175 175 GLN GLN B . n 
B 1 102 ALA 102 176 176 ALA ALA B . n 
B 1 103 TRP 103 177 177 TRP TRP B . n 
B 1 104 GLU 104 178 178 GLU GLU B . n 
B 1 105 GLU 105 179 179 GLU GLU B . n 
B 1 106 GLY 106 180 180 GLY GLY B . n 
B 1 107 GLY 107 181 181 GLY GLY B . n 
B 1 108 ILE 108 182 182 ILE ILE B . n 
B 1 109 LEU 109 183 183 LEU LEU B . n 
B 1 110 TYR 110 184 184 TYR TYR B . n 
B 1 111 LEU 111 185 185 LEU LEU B . n 
B 1 112 GLN 112 186 186 GLN GLN B . n 
B 1 113 THR 113 187 187 THR THR B . n 
B 1 114 GLU 114 188 188 GLU GLU B . n 
B 1 115 LEU 115 189 189 LEU LEU B . n 
B 1 116 CYS 116 190 190 CYS CYS B . n 
B 1 117 GLY 117 191 191 GLY GLY B . n 
B 1 118 PRO 118 192 192 PRO PRO B . n 
B 1 119 SER 119 193 193 SER SER B . n 
B 1 120 LEU 120 194 194 LEU LEU B . n 
B 1 121 GLN 121 195 195 GLN GLN B . n 
B 1 122 GLN 122 196 196 GLN GLN B . n 
B 1 123 HIS 123 197 197 HIS HIS B . n 
B 1 124 CYS 124 198 198 CYS CYS B . n 
B 1 125 GLU 125 199 199 GLU GLU B . n 
B 1 126 ALA 126 200 200 ALA ALA B . n 
B 1 127 TRP 127 201 201 TRP TRP B . n 
B 1 128 GLY 128 202 202 GLY GLY B . n 
B 1 129 ALA 129 203 203 ALA ALA B . n 
B 1 130 SER 130 204 204 SER SER B . n 
B 1 131 LEU 131 205 205 LEU LEU B . n 
B 1 132 PRO 132 206 206 PRO PRO B . n 
B 1 133 GLU 133 207 207 GLU GLU B . n 
B 1 134 ALA 134 208 208 ALA ALA B . n 
B 1 135 GLN 135 209 209 GLN GLN B . n 
B 1 136 VAL 136 210 210 VAL VAL B . n 
B 1 137 TRP 137 211 211 TRP TRP B . n 
B 1 138 GLY 138 212 212 GLY GLY B . n 
B 1 139 TYR 139 213 213 TYR TYR B . n 
B 1 140 LEU 140 214 214 LEU LEU B . n 
B 1 141 ARG 141 215 215 ARG ARG B . n 
B 1 142 ASP 142 216 216 ASP ASP B . n 
B 1 143 THR 143 217 217 THR THR B . n 
B 1 144 LEU 144 218 218 LEU LEU B . n 
B 1 145 LEU 145 219 219 LEU LEU B . n 
B 1 146 ALA 146 220 220 ALA ALA B . n 
B 1 147 LEU 147 221 221 LEU LEU B . n 
B 1 148 ALA 148 222 222 ALA ALA B . n 
B 1 149 HIS 149 223 223 HIS HIS B . n 
B 1 150 LEU 150 224 224 LEU LEU B . n 
B 1 151 HIS 151 225 225 HIS HIS B . n 
B 1 152 SER 152 226 226 SER SER B . n 
B 1 153 GLN 153 227 227 GLN GLN B . n 
B 1 154 GLY 154 228 228 GLY GLY B . n 
B 1 155 LEU 155 229 229 LEU LEU B . n 
B 1 156 VAL 156 230 230 VAL VAL B . n 
B 1 157 HIS 157 231 231 HIS HIS B . n 
B 1 158 LEU 158 232 232 LEU LEU B . n 
B 1 159 ASP 159 233 233 ASP ASP B . n 
B 1 160 VAL 160 234 234 VAL VAL B . n 
B 1 161 LYS 161 235 235 LYS LYS B . n 
B 1 162 PRO 162 236 236 PRO PRO B . n 
B 1 163 ALA 163 237 237 ALA ALA B . n 
B 1 164 ASN 164 238 238 ASN ASN B . n 
B 1 165 ILE 165 239 239 ILE ILE B . n 
B 1 166 PHE 166 240 240 PHE PHE B . n 
B 1 167 LEU 167 241 241 LEU LEU B . n 
B 1 168 GLY 168 242 242 GLY GLY B . n 
B 1 169 PRO 169 243 243 PRO PRO B . n 
B 1 170 ARG 170 244 244 ARG ARG B . n 
B 1 171 GLY 171 245 245 GLY GLY B . n 
B 1 172 ARG 172 246 246 ARG ARG B . n 
B 1 173 CYS 173 247 247 CYS CYS B . n 
B 1 174 LYS 174 248 248 LYS LYS B . n 
B 1 175 LEU 175 249 249 LEU LEU B . n 
B 1 176 GLY 176 250 250 GLY GLY B . n 
B 1 177 ASP 177 251 251 ASP ASP B . n 
B 1 178 PHE 178 252 252 PHE PHE B . n 
B 1 179 GLY 179 253 253 GLY GLY B . n 
B 1 180 LEU 180 254 254 LEU LEU B . n 
B 1 181 LEU 181 255 255 LEU LEU B . n 
B 1 182 VAL 182 256 256 VAL VAL B . n 
B 1 183 GLU 183 257 257 GLU GLU B . n 
B 1 184 LEU 184 258 258 LEU LEU B . n 
B 1 185 GLY 185 259 259 GLY GLY B . n 
B 1 186 THR 186 260 260 THR THR B . n 
B 1 187 ALA 187 261 261 ALA ALA B . n 
B 1 188 GLY 188 262 262 GLY ALA B . n 
B 1 189 ALA 189 263 263 ALA ALA B . n 
B 1 190 GLY 190 264 264 GLY GLY B . n 
B 1 191 GLU 191 265 265 GLU GLU B . n 
B 1 192 VAL 192 266 266 VAL VAL B . n 
B 1 193 GLN 193 267 267 GLN GLN B . n 
B 1 194 GLU 194 268 268 GLU GLU B . n 
B 1 195 GLY 195 269 269 GLY GLY B . n 
B 1 196 ASP 196 270 270 ASP ASP B . n 
B 1 197 PRO 197 271 271 PRO PRO B . n 
B 1 198 ARG 198 272 272 ARG ARG B . n 
B 1 199 TYR 199 273 273 TYR TYR B . n 
B 1 200 MET 200 274 274 MET MET B . n 
B 1 201 ALA 201 275 275 ALA ALA B . n 
B 1 202 PRO 202 276 276 PRO PRO B . n 
B 1 203 GLU 203 277 277 GLU GLU B . n 
B 1 204 LEU 204 278 278 LEU LEU B . n 
B 1 205 LEU 205 279 279 LEU LEU B . n 
B 1 206 GLN 206 280 280 GLN GLN B . n 
B 1 207 GLY 207 281 281 GLY GLY B . n 
B 1 208 SER 208 282 282 SER SER B . n 
B 1 209 TYR 209 283 283 TYR TYR B . n 
B 1 210 GLY 210 284 284 GLY GLY B . n 
B 1 211 THR 211 285 285 THR THR B . n 
B 1 212 ALA 212 286 286 ALA ALA B . n 
B 1 213 ALA 213 287 287 ALA ALA B . n 
B 1 214 ASP 214 288 288 ASP ASP B . n 
B 1 215 VAL 215 289 289 VAL VAL B . n 
B 1 216 PHE 216 290 290 PHE PHE B . n 
B 1 217 SER 217 291 291 SER SER B . n 
B 1 218 LEU 218 292 292 LEU LEU B . n 
B 1 219 GLY 219 293 293 GLY GLY B . n 
B 1 220 LEU 220 294 294 LEU LEU B . n 
B 1 221 THR 221 295 295 THR THR B . n 
B 1 222 ILE 222 296 296 ILE ILE B . n 
B 1 223 LEU 223 297 297 LEU LEU B . n 
B 1 224 GLU 224 298 298 GLU GLU B . n 
B 1 225 VAL 225 299 299 VAL VAL B . n 
B 1 226 ALA 226 300 300 ALA ALA B . n 
B 1 227 CYS 227 301 301 CYS CYS B . n 
B 1 228 ASN 228 302 302 ASN ASN B . n 
B 1 229 MET 229 303 303 MET MET B . n 
B 1 230 GLU 230 304 304 GLU GLU B . n 
B 1 231 LEU 231 305 305 LEU LEU B . n 
B 1 232 PRO 232 306 306 PRO PRO B . n 
B 1 233 HIS 233 307 307 HIS HIS B . n 
B 1 234 GLY 234 308 308 GLY GLY B . n 
B 1 235 GLY 235 309 309 GLY GLY B . n 
B 1 236 GLU 236 310 310 GLU GLU B . n 
B 1 237 GLY 237 311 311 GLY GLY B . n 
B 1 238 TRP 238 312 312 TRP TRP B . n 
B 1 239 GLN 239 313 313 GLN GLN B . n 
B 1 240 GLN 240 314 314 GLN GLN B . n 
B 1 241 LEU 241 315 315 LEU LEU B . n 
B 1 242 ARG 242 316 316 ARG ARG B . n 
B 1 243 GLN 243 317 317 GLN GLN B . n 
B 1 244 GLY 244 318 318 GLY GLY B . n 
B 1 245 TYR 245 319 319 TYR TYR B . n 
B 1 246 LEU 246 320 320 LEU LEU B . n 
B 1 247 PRO 247 321 321 PRO PRO B . n 
B 1 248 PRO 248 322 322 PRO PRO B . n 
B 1 249 GLU 249 323 323 GLU GLU B . n 
B 1 250 PHE 250 324 324 PHE PHE B . n 
B 1 251 THR 251 325 325 THR THR B . n 
B 1 252 ALA 252 326 326 ALA ALA B . n 
B 1 253 GLY 253 327 327 GLY GLY B . n 
B 1 254 LEU 254 328 328 LEU LEU B . n 
B 1 255 SER 255 329 329 SER SER B . n 
B 1 256 SER 256 330 330 SER SER B . n 
B 1 257 GLU 257 331 331 GLU GLU B . n 
B 1 258 LEU 258 332 332 LEU LEU B . n 
B 1 259 ARG 259 333 333 ARG ARG B . n 
B 1 260 SER 260 334 334 SER SER B . n 
B 1 261 VAL 261 335 335 VAL VAL B . n 
B 1 262 LEU 262 336 336 LEU LEU B . n 
B 1 263 VAL 263 337 337 VAL VAL B . n 
B 1 264 MET 264 338 338 MET MET B . n 
B 1 265 MET 265 339 339 MET MET B . n 
B 1 266 LEU 266 340 340 LEU LEU B . n 
B 1 267 GLU 267 341 341 GLU GLU B . n 
B 1 268 PRO 268 342 342 PRO PRO B . n 
B 1 269 ASP 269 343 343 ASP ASP B . n 
B 1 270 PRO 270 344 344 PRO PRO B . n 
B 1 271 LYS 271 345 345 LYS LYS B . n 
B 1 272 LEU 272 346 346 LEU LEU B . n 
B 1 273 ARG 273 347 347 ARG ARG B . n 
B 1 274 ALA 274 348 348 ALA ALA B . n 
B 1 275 THR 275 349 349 THR THR B . n 
B 1 276 ALA 276 350 350 ALA ALA B . n 
B 1 277 GLU 277 351 351 GLU GLU B . n 
B 1 278 ALA 278 352 352 ALA ALA B . n 
B 1 279 LEU 279 353 353 LEU LEU B . n 
B 1 280 LEU 280 354 354 LEU LEU B . n 
B 1 281 ALA 281 355 355 ALA ALA B . n 
B 1 282 LEU 282 356 356 LEU LEU B . n 
B 1 283 PRO 283 357 357 PRO PRO B . n 
B 1 284 VAL 284 358 358 VAL VAL B . n 
B 1 285 LEU 285 359 359 LEU LEU B . n 
B 1 286 ARG 286 360 360 ARG ARG B . n 
B 1 287 GLN 287 361 361 GLN GLN B . n 
B 1 288 PRO 288 362 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EJX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EJX 
_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 A1EJX 1  401 401 A1EJX L0R A . 
D 3 SO4   1  402 2   SO4   SO4 A . 
E 3 SO4   1  403 3   SO4   SO4 A . 
F 3 SO4   1  404 5   SO4   SO4 A . 
G 3 SO4   1  405 8   SO4   SO4 A . 
H 3 SO4   1  406 9   SO4   SO4 A . 
I 3 SO4   1  407 10  SO4   SO4 A . 
J 2 A1EJX 1  401 401 A1EJX L0R B . 
K 3 SO4   1  402 1   SO4   SO4 B . 
L 3 SO4   1  403 4   SO4   SO4 B . 
M 3 SO4   1  404 6   SO4   SO4 B . 
N 3 SO4   1  405 7   SO4   SO4 B . 
O 4 HOH   1  501 86  HOH   HOH A . 
O 4 HOH   2  502 76  HOH   HOH A . 
O 4 HOH   3  503 40  HOH   HOH A . 
O 4 HOH   4  504 47  HOH   HOH A . 
O 4 HOH   5  505 27  HOH   HOH A . 
O 4 HOH   6  506 71  HOH   HOH A . 
O 4 HOH   7  507 58  HOH   HOH A . 
O 4 HOH   8  508 66  HOH   HOH A . 
O 4 HOH   9  509 72  HOH   HOH A . 
O 4 HOH   10 510 79  HOH   HOH A . 
O 4 HOH   11 511 85  HOH   HOH A . 
O 4 HOH   12 512 96  HOH   HOH A . 
O 4 HOH   13 513 36  HOH   HOH A . 
O 4 HOH   14 514 49  HOH   HOH A . 
O 4 HOH   15 515 95  HOH   HOH A . 
O 4 HOH   16 516 34  HOH   HOH A . 
O 4 HOH   17 517 1   HOH   HOH A . 
O 4 HOH   18 518 21  HOH   HOH A . 
O 4 HOH   19 519 23  HOH   HOH A . 
O 4 HOH   20 520 7   HOH   HOH A . 
O 4 HOH   21 521 3   HOH   HOH A . 
O 4 HOH   22 522 97  HOH   HOH A . 
O 4 HOH   23 523 100 HOH   HOH A . 
O 4 HOH   24 524 103 HOH   HOH A . 
O 4 HOH   25 525 12  HOH   HOH A . 
O 4 HOH   26 526 16  HOH   HOH A . 
O 4 HOH   27 527 78  HOH   HOH A . 
O 4 HOH   28 528 2   HOH   HOH A . 
O 4 HOH   29 529 99  HOH   HOH A . 
O 4 HOH   30 530 108 HOH   HOH A . 
O 4 HOH   31 531 44  HOH   HOH A . 
O 4 HOH   32 532 88  HOH   HOH A . 
O 4 HOH   33 533 32  HOH   HOH A . 
O 4 HOH   34 534 26  HOH   HOH A . 
O 4 HOH   35 535 70  HOH   HOH A . 
O 4 HOH   36 536 57  HOH   HOH A . 
O 4 HOH   37 537 29  HOH   HOH A . 
O 4 HOH   38 538 112 HOH   HOH A . 
O 4 HOH   39 539 77  HOH   HOH A . 
O 4 HOH   40 540 33  HOH   HOH A . 
O 4 HOH   41 541 41  HOH   HOH A . 
O 4 HOH   42 542 42  HOH   HOH A . 
O 4 HOH   43 543 28  HOH   HOH A . 
O 4 HOH   44 544 67  HOH   HOH A . 
O 4 HOH   45 545 101 HOH   HOH A . 
O 4 HOH   46 546 87  HOH   HOH A . 
O 4 HOH   47 547 89  HOH   HOH A . 
P 4 HOH   1  501 110 HOH   HOH B . 
P 4 HOH   2  502 37  HOH   HOH B . 
P 4 HOH   3  503 104 HOH   HOH B . 
P 4 HOH   4  504 45  HOH   HOH B . 
P 4 HOH   5  505 17  HOH   HOH B . 
P 4 HOH   6  506 30  HOH   HOH B . 
P 4 HOH   7  507 14  HOH   HOH B . 
P 4 HOH   8  508 50  HOH   HOH B . 
P 4 HOH   9  509 107 HOH   HOH B . 
P 4 HOH   10 510 62  HOH   HOH B . 
P 4 HOH   11 511 35  HOH   HOH B . 
P 4 HOH   12 512 8   HOH   HOH B . 
P 4 HOH   13 513 18  HOH   HOH B . 
P 4 HOH   14 514 19  HOH   HOH B . 
P 4 HOH   15 515 39  HOH   HOH B . 
P 4 HOH   16 516 69  HOH   HOH B . 
P 4 HOH   17 517 111 HOH   HOH B . 
P 4 HOH   18 518 6   HOH   HOH B . 
P 4 HOH   19 519 105 HOH   HOH B . 
P 4 HOH   20 520 25  HOH   HOH B . 
P 4 HOH   21 521 56  HOH   HOH B . 
P 4 HOH   22 522 75  HOH   HOH B . 
P 4 HOH   23 523 20  HOH   HOH B . 
P 4 HOH   24 524 11  HOH   HOH B . 
P 4 HOH   25 525 48  HOH   HOH B . 
P 4 HOH   26 526 74  HOH   HOH B . 
P 4 HOH   27 527 31  HOH   HOH B . 
P 4 HOH   28 528 61  HOH   HOH B . 
P 4 HOH   29 529 55  HOH   HOH B . 
P 4 HOH   30 530 83  HOH   HOH B . 
P 4 HOH   31 531 4   HOH   HOH B . 
P 4 HOH   32 532 10  HOH   HOH B . 
P 4 HOH   33 533 51  HOH   HOH B . 
P 4 HOH   34 534 60  HOH   HOH B . 
P 4 HOH   35 535 24  HOH   HOH B . 
P 4 HOH   36 536 73  HOH   HOH B . 
P 4 HOH   37 537 52  HOH   HOH B . 
P 4 HOH   38 538 98  HOH   HOH B . 
P 4 HOH   39 539 63  HOH   HOH B . 
P 4 HOH   40 540 15  HOH   HOH B . 
P 4 HOH   41 541 53  HOH   HOH B . 
P 4 HOH   42 542 64  HOH   HOH B . 
P 4 HOH   43 543 46  HOH   HOH B . 
P 4 HOH   44 544 92  HOH   HOH B . 
P 4 HOH   45 545 106 HOH   HOH B . 
P 4 HOH   46 546 5   HOH   HOH B . 
P 4 HOH   47 547 80  HOH   HOH B . 
P 4 HOH   48 548 54  HOH   HOH B . 
P 4 HOH   49 549 109 HOH   HOH B . 
P 4 HOH   50 550 13  HOH   HOH B . 
P 4 HOH   51 551 81  HOH   HOH B . 
P 4 HOH   52 552 82  HOH   HOH B . 
P 4 HOH   53 553 65  HOH   HOH B . 
P 4 HOH   54 554 94  HOH   HOH B . 
P 4 HOH   55 555 113 HOH   HOH B . 
P 4 HOH   56 556 59  HOH   HOH B . 
P 4 HOH   57 557 90  HOH   HOH B . 
P 4 HOH   58 558 91  HOH   HOH B . 
P 4 HOH   59 559 43  HOH   HOH B . 
P 4 HOH   60 560 9   HOH   HOH B . 
P 4 HOH   61 561 38  HOH   HOH B . 
P 4 HOH   62 562 68  HOH   HOH B . 
P 4 HOH   63 563 93  HOH   HOH B . 
P 4 HOH   64 564 84  HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21.2_5419: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   110.33 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LID 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.484 
_cell.length_a_esd                 ? 
_cell.length_b                     112.359 
_cell.length_b_esd                 ? 
_cell.length_c                     72.390 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9LID 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9LID 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.36 
_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    
'6.9 MG/ML MYT1, 25 mM HEPES, 100 MM SODIUM CHLORIDE, 0.5 mM DTT, 0.1 M CALCIUM CHLORIDE, 0.05 M TRIS pH 8.5, 10 % PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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         2023-04-26 
_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   0.9793 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LID 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.06 
_reflns.d_resolution_low                               68.027 
_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                                     28634 
_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                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.076 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.059 
_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                                    2.06 
_reflns_shell.d_res_low                                     2.117 
_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                             264 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.941 
_reflns_shell.pdbx_Rpim_I_all                               0.496 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          59.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.798 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LID 
_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                            2.06 
_refine.ls_d_res_low                             32.30 
_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                     28634 
_refine.ls_number_reflns_R_free                  1484 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    61.57 
_refine.ls_percent_reflns_R_free                 5.18 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2046 
_refine.ls_R_factor_R_free                       0.2307 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2032 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.85 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.28 
_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                       2.06 
_refine_hist.d_res_low                        32.30 
_refine_hist.number_atoms_solvent             111 
_refine_hist.number_atoms_total               4522 
_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        4295 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         116 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 4510 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.637  ? 6112 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.215 ? 1720 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040  ? 626  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 799  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.30 2.40 . . 53  905  23.00  . . . . 0.3260 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 2.40 2.53 . . 107 1984 50.00  . . . . 0.3237 . . . . . . . . . . . 0.3462 
'X-RAY DIFFRACTION' 2.53 2.68 . . 200 3367 85.00  . . . . 0.3086 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 2.68 2.89 . . 206 3978 100.00 . . . . 0.2930 . . . . . . . . . . . 0.3361 
'X-RAY DIFFRACTION' 2.89 3.18 . . 225 3985 100.00 . . . . 0.2658 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 3.18 3.64 . . 215 3988 99.00  . . . . 0.2066 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 3.64 4.59 . . 204 3969 98.00  . . . . 0.1639 . . . . . . . . . . . 0.1983 
'X-RAY DIFFRACTION' 4.59 10   . . 221 4001 99.00  . . . . 0.1636 . . . . . . . . . . . 0.1862 
# 
_struct.entry_id                     9LID 
_struct.title                        
'Crystal structure of human PKMYT1 protein kinase domain with Naphthyridinone Inhibitor compound 27' 
_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        9LID 
_struct_keywords.text            'inhibitor, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 4 ? 
P N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PMYT1_HUMAN 
_struct_ref.pdbx_db_accession          Q99640 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_struct_ref.pdbx_align_begin           75 
# 
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 9LID A 1 ? 288 ? Q99640 75 ? 362 ? 75 362 
2 1 9LID B 1 ? 288 ? Q99640 75 ? 362 ? 75 362 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 380   ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  13810 ? 
2 'ABSA (A^2)' 400   ? 
2 MORE         -29   ? 
2 'SSA (A^2)'  14040 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,O 
2 1 B,J,K,L,M,N,P     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 SER A 30  ? SER A 35  ? SER A 104 SER A 109 1 ? 6  
HELX_P HELX_P2  AA2 GLY A 73  ? GLY A 91  ? GLY A 147 GLY A 165 1 ? 19 
HELX_P HELX_P3  AA3 SER A 119 ? GLY A 128 ? SER A 193 GLY A 202 1 ? 10 
HELX_P HELX_P4  AA4 PRO A 132 ? SER A 152 ? PRO A 206 SER A 226 1 ? 21 
HELX_P HELX_P5  AA5 LYS A 161 ? ALA A 163 ? LYS A 235 ALA A 237 5 ? 3  
HELX_P HELX_P6  AA6 PRO A 169 ? GLY A 171 ? PRO A 243 GLY A 245 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 196 ? MET A 200 ? ASP A 270 MET A 274 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 201 ? GLY A 207 ? ALA A 275 GLY A 281 5 ? 7  
HELX_P HELX_P9  AA9 THR A 211 ? ASN A 228 ? THR A 285 ASN A 302 1 ? 18 
HELX_P HELX_P10 AB1 GLY A 234 ? LEU A 241 ? GLY A 308 LEU A 315 1 ? 8  
HELX_P HELX_P11 AB2 PRO A 247 ? ALA A 252 ? PRO A 321 ALA A 326 1 ? 6  
HELX_P HELX_P12 AB3 SER A 255 ? LEU A 266 ? SER A 329 LEU A 340 1 ? 12 
HELX_P HELX_P13 AB4 THR A 275 ? ALA A 281 ? THR A 349 ALA A 355 1 ? 7  
HELX_P HELX_P14 AB5 SER B 30  ? SER B 35  ? SER B 104 SER B 109 1 ? 6  
HELX_P HELX_P15 AB6 GLY B 73  ? GLY B 91  ? GLY B 147 GLY B 165 1 ? 19 
HELX_P HELX_P16 AB7 SER B 119 ? GLY B 128 ? SER B 193 GLY B 202 1 ? 10 
HELX_P HELX_P17 AB8 PRO B 132 ? SER B 152 ? PRO B 206 SER B 226 1 ? 21 
HELX_P HELX_P18 AB9 LYS B 161 ? ALA B 163 ? LYS B 235 ALA B 237 5 ? 3  
HELX_P HELX_P19 AC1 PRO B 169 ? GLY B 171 ? PRO B 243 GLY B 245 5 ? 3  
HELX_P HELX_P20 AC2 ASP B 196 ? MET B 200 ? ASP B 270 MET B 274 5 ? 5  
HELX_P HELX_P21 AC3 ALA B 201 ? GLY B 207 ? ALA B 275 GLY B 281 5 ? 7  
HELX_P HELX_P22 AC4 THR B 211 ? ASN B 228 ? THR B 285 ASN B 302 1 ? 18 
HELX_P HELX_P23 AC5 GLY B 234 ? LEU B 241 ? GLY B 308 LEU B 315 1 ? 8  
HELX_P HELX_P24 AC6 GLU B 249 ? LEU B 254 ? GLU B 323 LEU B 328 5 ? 6  
HELX_P HELX_P25 AC7 SER B 255 ? LEU B 266 ? SER B 329 LEU B 340 1 ? 12 
HELX_P HELX_P26 AC8 THR B 275 ? LEU B 280 ? THR B 349 LEU B 354 1 ? 6  
HELX_P HELX_P27 AC9 ALA B 281 ? ARG B 286 ? ALA B 355 ARG B 360 5 ? 6  
# 
_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 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 6   ? ARG A 7   ? ARG A 80  ARG A 81  
AA1 2 LEU A 99  ? GLU A 105 ? LEU A 173 GLU A 179 
AA1 3 ILE A 108 ? GLU A 114 ? ILE A 182 GLU A 188 
AA1 4 LEU A 61  ? SER A 67  ? LEU A 135 SER A 141 
AA1 5 GLY A 48  ? SER A 55  ? GLY A 122 SER A 129 
AA1 6 PHE A 36  ? GLY A 45  ? PHE A 110 GLY A 119 
AA2 1 LEU A 155 ? VAL A 156 ? LEU A 229 VAL A 230 
AA2 2 VAL A 182 ? GLU A 183 ? VAL A 256 GLU A 257 
AA3 1 ILE A 165 ? LEU A 167 ? ILE A 239 LEU A 241 
AA3 2 CYS A 173 ? LEU A 175 ? CYS A 247 LEU A 249 
AA4 1 ARG B 6   ? ARG B 7   ? ARG B 80  ARG B 81  
AA4 2 LEU B 99  ? GLU B 105 ? LEU B 173 GLU B 179 
AA4 3 ILE B 108 ? GLU B 114 ? ILE B 182 GLU B 188 
AA4 4 LEU B 61  ? SER B 67  ? LEU B 135 SER B 141 
AA4 5 GLY B 48  ? SER B 55  ? GLY B 122 SER B 129 
AA4 6 PHE B 36  ? HIS B 44  ? PHE B 110 HIS B 118 
AA5 1 LEU B 155 ? VAL B 156 ? LEU B 229 VAL B 230 
AA5 2 VAL B 182 ? GLU B 183 ? VAL B 256 GLU B 257 
AA6 1 ILE B 165 ? LEU B 167 ? ILE B 239 LEU B 241 
AA6 2 CYS B 173 ? LEU B 175 ? CYS B 247 LEU B 249 
# 
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 ARG A 6   ? N ARG A 80  O GLU A 104 ? O GLU A 178 
AA1 2 3 N TRP A 103 ? N TRP A 177 O TYR A 110 ? O TYR A 184 
AA1 3 4 O THR A 113 ? O THR A 187 N ALA A 63  ? N ALA A 137 
AA1 4 5 O VAL A 64  ? O VAL A 138 N PHE A 51  ? N PHE A 125 
AA1 5 6 O LYS A 52  ? O LYS A 126 N SER A 40  ? N SER A 114 
AA2 1 2 N VAL A 156 ? N VAL A 230 O VAL A 182 ? O VAL A 256 
AA3 1 2 N PHE A 166 ? N PHE A 240 O LYS A 174 ? O LYS A 248 
AA4 1 2 N ARG B 6   ? N ARG B 80  O GLU B 104 ? O GLU B 178 
AA4 2 3 N TRP B 103 ? N TRP B 177 O TYR B 110 ? O TYR B 184 
AA4 3 4 O THR B 113 ? O THR B 187 N ALA B 63  ? N ALA B 137 
AA4 4 5 O VAL B 64  ? O VAL B 138 N PHE B 51  ? N PHE B 125 
AA4 5 6 O LYS B 52  ? O LYS B 126 N SER B 40  ? N SER B 114 
AA5 1 2 N VAL B 156 ? N VAL B 230 O VAL B 182 ? O VAL B 256 
AA6 1 2 N PHE B 166 ? N PHE B 240 O LYS B 174 ? O LYS B 248 
# 
_pdbx_entry_details.entry_id                   9LID 
_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 
# 
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 PHE A 84  ? ? -104.46 44.69  
2  1 PRO A 99  ? ? -57.47  -7.46  
3  1 GLU A 131 ? ? -90.19  -64.34 
4  1 ASP A 233 ? ? -150.87 35.62  
5  1 ASP A 251 ? ? 44.66   82.65  
6  1 LEU A 315 ? ? -68.87  0.24   
7  1 LEU A 359 ? ? -99.96  57.78  
8  1 SER B 100 ? ? -122.39 -62.49 
9  1 ASP B 233 ? ? -147.65 45.30  
10 1 ASP B 251 ? ? 50.80   79.94  
11 1 PHE B 252 ? ? -95.85  31.40  
12 1 PRO B 322 ? ? -68.08  0.79   
# 
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 23.2847  12.5102 39.9245 0.9006 ? -0.1016 ? -0.4074 ? 0.9021 ? 0.0092  ? 1.3749 ? 4.1901 ? 1.2243 
? -0.0459 ? 8.3852 ? 2.6391  ? 3.2666 ? -0.0641 ? -0.2439 ? 0.1629  ? 1.3680  ? 0.5684  ? -1.9022 ? -0.3594 ? 2.0686  ? -0.4640 ? 
2  'X-RAY DIFFRACTION' ? refined 11.4533  20.7625 34.6630 1.0923 ? -0.0159 ? -0.4131 ? 0.3092 ? -0.1006 ? 1.1208 ? 1.9966 ? 1.1134 
? 0.6631  ? 1.1232 ? -1.0017 ? 4.2674 ? -0.0224 ? -0.4211 ? 0.7462  ? 1.7991  ? -0.5286 ? -0.2965 ? -1.7942 ? -0.1353 ? 0.5427  ? 
3  'X-RAY DIFFRACTION' ? refined 12.2792  8.5335  33.6442 0.3401 ? 0.0071  ? -0.0757 ? 0.2755 ? -0.0259 ? 0.5457 ? 2.1559 ? 0.8279 
? 2.1788  ? 6.0701 ? -0.7789 ? 4.7630 ? -0.2453 ? 0.1640  ? 0.5506  ? 0.5029  ? 0.0372  ? -0.3409 ? -0.9218 ? -0.0384 ? 0.1167  ? 
4  'X-RAY DIFFRACTION' ? refined 6.2708   12.7274 19.2365 0.3167 ? -0.0293 ? 0.1074  ? 0.3917 ? -0.0416 ? 0.3794 ? 3.5451 ? 
-0.5157 ? 1.3997  ? 6.1643 ? -1.5478 ? 4.6060 ? -0.1523 ? 0.7623  ? 0.1478  ? -0.3399 ? -0.0090 ? -0.7875 ? -0.4592 ? 0.3913  ? 
0.0991  ? 
5  'X-RAY DIFFRACTION' ? refined -1.2800  4.1495  19.8553 0.3086 ? 0.0247  ? 0.0218  ? 0.3772 ? -0.0508 ? 0.2010 ? 4.5515 ? 1.9378 
? -0.6258 ? 8.9476 ? -0.0667 ? 3.0943 ? -0.0428 ? 0.1614  ? -0.2690 ? -0.0004 ? 0.2000  ? -0.1445 ? 0.2327  ? -0.2676 ? -0.1671 ? 
6  'X-RAY DIFFRACTION' ? refined -17.3204 6.8298  15.0391 0.5772 ? 0.0458  ? -0.1444 ? 0.9453 ? 0.1965  ? 0.8621 ? 3.3313 ? 2.6204 
? -0.8176 ? 6.4278 ? -4.4472 ? 5.0112 ? 0.0741  ? 0.3720  ? 0.3497  ? -0.4941 ? 0.7969  ? 1.7862  ? -0.3618 ? -1.7386 ? -0.8885 ? 
7  'X-RAY DIFFRACTION' ? refined -4.5113  1.9416  4.8068  0.9043 ? -0.0721 ? -0.0684 ? 0.7939 ? -0.0836 ? 0.3344 ? 4.9914 ? 
-1.1611 ? 1.2187  ? 7.0903 ? -1.7382 ? 5.5910 ? 0.0559  ? 0.7874  ? 0.0531  ? -2.0586 ? 0.1771  ? 0.0463  ? 0.3234  ? -0.1412 ? 
-0.2736 ? 
8  'X-RAY DIFFRACTION' ? refined -16.7181 35.5505 32.8445 0.4872 ? -0.0628 ? 0.1048  ? 0.3969 ? 0.1330  ? 1.3181 ? 2.1388 ? 1.1840 
? -1.0684 ? 5.9084 ? 3.3060  ? 5.6062 ? -0.1736 ? -0.3737 ? -1.0099 ? 0.9665  ? -0.4485 ? 0.4781  ? 0.6547  ? -0.5286 ? 0.4261  ? 
9  'X-RAY DIFFRACTION' ? refined -6.7248  41.4366 18.0110 0.3129 ? 0.0084  ? -0.1474 ? 0.2854 ? 0.0340  ? 0.4088 ? 1.8994 ? 
-0.3996 ? -1.5790 ? 3.3696 ? 0.8138  ? 3.7431 ? -0.1013 ? 0.2124  ? -0.1613 ? -0.5779 ? -0.1390 ? 0.8117  ? -0.0833 ? -0.2805 ? 
0.2169  ? 
10 'X-RAY DIFFRACTION' ? refined -3.9211  55.3033 23.0191 0.6945 ? 0.0294  ? -0.0037 ? 0.4461 ? -0.0349 ? 0.7363 ? 9.5763 ? 
-5.8133 ? 3.9673  ? 3.8107 ? -3.4360 ? 6.5754 ? -0.7037 ? -0.4534 ? 1.2973  ? 1.1384  ? 0.4018  ? -0.2678 ? -1.5024 ? -0.3639 ? 
0.2812  ? 
11 'X-RAY DIFFRACTION' ? refined 9.3757   48.1400 9.6057  0.6021 ? -0.0651 ? 0.0532  ? 0.4577 ? 0.0809  ? 0.2738 ? 3.5006 ? 
-0.9358 ? 0.9778  ? 5.1032 ? -0.0723 ? 5.8235 ? -0.1848 ? 0.3003  ? 0.1035  ? -1.0804 ? 0.1682  ? -0.4858 ? 0.0404  ? 0.6166  ? 
0.0562  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 104 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 105 through 129 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 130 through 164 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 165 through 227 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 228 through 301 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 302 through 329 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 330 through 361 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 77 through 147 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 148 through 249 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 250 through 269 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 270 through 361 )
;
# 
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 HIS 75  ? A HIS 1   
2  1 Y 1 A GLN 76  ? A GLN 2   
3  1 Y 1 A GLY 86  ? A GLY 12  
4  1 Y 1 A GLU 87  ? A GLU 13  
5  1 Y 1 A ALA 88  ? A ALA 14  
6  1 Y 1 A SER 89  ? A SER 15  
7  1 Y 1 A GLU 90  ? A GLU 16  
8  1 Y 1 A THR 91  ? A THR 17  
9  1 Y 1 A LEU 92  ? A LEU 18  
10 1 Y 1 A GLN 93  ? A GLN 19  
11 1 Y 1 A THR 260 ? A THR 186 
12 1 Y 1 A ALA 261 ? A ALA 187 
13 1 Y 1 A GLY 262 ? A GLY 188 
14 1 Y 1 A ALA 263 ? A ALA 189 
15 1 Y 1 A GLY 264 ? A GLY 190 
16 1 Y 1 A PRO 362 ? A PRO 288 
17 1 Y 1 B HIS 75  ? B HIS 1   
18 1 Y 1 B GLN 76  ? B GLN 2   
19 1 Y 1 B GLU 87  ? B GLU 13  
20 1 Y 1 B ALA 88  ? B ALA 14  
21 1 Y 1 B SER 89  ? B SER 15  
22 1 Y 1 B GLU 90  ? B GLU 16  
23 1 Y 1 B THR 91  ? B THR 17  
24 1 Y 1 B LEU 92  ? B LEU 18  
25 1 Y 1 B PRO 362 ? B PRO 288 
# 
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 
A1EJX C10  C Y N 1   
A1EJX C11  C Y N 2   
A1EJX C13  C Y N 3   
A1EJX C15  C Y N 4   
A1EJX C16  C Y N 5   
A1EJX C17  C Y N 6   
A1EJX C19  C Y N 7   
A1EJX C22  C Y N 8   
A1EJX C24  C Y N 9   
A1EJX C25  C Y N 10  
A1EJX C26  C Y N 11  
A1EJX C27  C Y N 12  
A1EJX C28  C Y N 13  
A1EJX C1   C N N 14  
A1EJX C2   C N N 15  
A1EJX C29  C N N 16  
A1EJX C32  C N N 17  
A1EJX C33  C N N 18  
A1EJX C4   C N N 19  
A1EJX C5   C Y N 20  
A1EJX C6   C Y N 21  
A1EJX C7   C Y N 22  
A1EJX C8   C Y N 23  
A1EJX C9   C Y N 24  
A1EJX F12  F N N 25  
A1EJX N14  N Y N 26  
A1EJX N20  N N N 27  
A1EJX N21  N Y N 28  
A1EJX N23  N Y N 29  
A1EJX N3   N N N 30  
A1EJX N30  N N N 31  
A1EJX O18  O N N 32  
A1EJX O31  O N N 33  
A1EJX H1   H N N 34  
A1EJX H2   H N N 35  
A1EJX H3   H N N 36  
A1EJX H4   H N N 37  
A1EJX H5   H N N 38  
A1EJX H6   H N N 39  
A1EJX H7   H N N 40  
A1EJX H8   H N N 41  
A1EJX H9   H N N 42  
A1EJX H10  H N N 43  
A1EJX H11  H N N 44  
A1EJX H12  H N N 45  
A1EJX H13  H N N 46  
A1EJX H14  H N N 47  
A1EJX H15  H N N 48  
A1EJX H16  H N N 49  
A1EJX H17  H N N 50  
A1EJX H18  H N N 51  
A1EJX H19  H N N 52  
ALA   N    N N N 53  
ALA   CA   C N S 54  
ALA   C    C N N 55  
ALA   O    O N N 56  
ALA   CB   C N N 57  
ALA   OXT  O N N 58  
ALA   H    H N N 59  
ALA   H2   H N N 60  
ALA   HA   H N N 61  
ALA   HB1  H N N 62  
ALA   HB2  H N N 63  
ALA   HB3  H N N 64  
ALA   HXT  H N N 65  
ARG   N    N N N 66  
ARG   CA   C N S 67  
ARG   C    C N N 68  
ARG   O    O N N 69  
ARG   CB   C N N 70  
ARG   CG   C N N 71  
ARG   CD   C N N 72  
ARG   NE   N N N 73  
ARG   CZ   C N N 74  
ARG   NH1  N N N 75  
ARG   NH2  N N N 76  
ARG   OXT  O N N 77  
ARG   H    H N N 78  
ARG   H2   H N N 79  
ARG   HA   H N N 80  
ARG   HB2  H N N 81  
ARG   HB3  H N N 82  
ARG   HG2  H N N 83  
ARG   HG3  H N N 84  
ARG   HD2  H N N 85  
ARG   HD3  H N N 86  
ARG   HE   H N N 87  
ARG   HH11 H N N 88  
ARG   HH12 H N N 89  
ARG   HH21 H N N 90  
ARG   HH22 H N N 91  
ARG   HXT  H N N 92  
ASN   N    N N N 93  
ASN   CA   C N S 94  
ASN   C    C N N 95  
ASN   O    O N N 96  
ASN   CB   C N N 97  
ASN   CG   C N N 98  
ASN   OD1  O N N 99  
ASN   ND2  N N N 100 
ASN   OXT  O N N 101 
ASN   H    H N N 102 
ASN   H2   H N N 103 
ASN   HA   H N N 104 
ASN   HB2  H N N 105 
ASN   HB3  H N N 106 
ASN   HD21 H N N 107 
ASN   HD22 H N N 108 
ASN   HXT  H N N 109 
ASP   N    N N N 110 
ASP   CA   C N S 111 
ASP   C    C N N 112 
ASP   O    O N N 113 
ASP   CB   C N N 114 
ASP   CG   C N N 115 
ASP   OD1  O N N 116 
ASP   OD2  O N N 117 
ASP   OXT  O N N 118 
ASP   H    H N N 119 
ASP   H2   H N N 120 
ASP   HA   H N N 121 
ASP   HB2  H N N 122 
ASP   HB3  H N N 123 
ASP   HD2  H N N 124 
ASP   HXT  H N N 125 
CYS   N    N N N 126 
CYS   CA   C N R 127 
CYS   C    C N N 128 
CYS   O    O N N 129 
CYS   CB   C N N 130 
CYS   SG   S N N 131 
CYS   OXT  O N N 132 
CYS   H    H N N 133 
CYS   H2   H N N 134 
CYS   HA   H N N 135 
CYS   HB2  H N N 136 
CYS   HB3  H N N 137 
CYS   HG   H N N 138 
CYS   HXT  H N N 139 
GLN   N    N N N 140 
GLN   CA   C N S 141 
GLN   C    C N N 142 
GLN   O    O N N 143 
GLN   CB   C N N 144 
GLN   CG   C N N 145 
GLN   CD   C N N 146 
GLN   OE1  O N N 147 
GLN   NE2  N N N 148 
GLN   OXT  O N N 149 
GLN   H    H N N 150 
GLN   H2   H N N 151 
GLN   HA   H N N 152 
GLN   HB2  H N N 153 
GLN   HB3  H N N 154 
GLN   HG2  H N N 155 
GLN   HG3  H N N 156 
GLN   HE21 H N N 157 
GLN   HE22 H N N 158 
GLN   HXT  H N N 159 
GLU   N    N N N 160 
GLU   CA   C N S 161 
GLU   C    C N N 162 
GLU   O    O N N 163 
GLU   CB   C N N 164 
GLU   CG   C N N 165 
GLU   CD   C N N 166 
GLU   OE1  O N N 167 
GLU   OE2  O N N 168 
GLU   OXT  O N N 169 
GLU   H    H N N 170 
GLU   H2   H N N 171 
GLU   HA   H N N 172 
GLU   HB2  H N N 173 
GLU   HB3  H N N 174 
GLU   HG2  H N N 175 
GLU   HG3  H N N 176 
GLU   HE2  H N N 177 
GLU   HXT  H N N 178 
GLY   N    N N N 179 
GLY   CA   C N N 180 
GLY   C    C N N 181 
GLY   O    O N N 182 
GLY   OXT  O N N 183 
GLY   H    H N N 184 
GLY   H2   H N N 185 
GLY   HA2  H N N 186 
GLY   HA3  H N N 187 
GLY   HXT  H N N 188 
HIS   N    N N N 189 
HIS   CA   C N S 190 
HIS   C    C N N 191 
HIS   O    O N N 192 
HIS   CB   C N N 193 
HIS   CG   C Y N 194 
HIS   ND1  N Y N 195 
HIS   CD2  C Y N 196 
HIS   CE1  C Y N 197 
HIS   NE2  N Y N 198 
HIS   OXT  O N N 199 
HIS   H    H N N 200 
HIS   H2   H N N 201 
HIS   HA   H N N 202 
HIS   HB2  H N N 203 
HIS   HB3  H N N 204 
HIS   HD1  H N N 205 
HIS   HD2  H N N 206 
HIS   HE1  H N N 207 
HIS   HE2  H N N 208 
HIS   HXT  H N N 209 
HOH   O    O N N 210 
HOH   H1   H N N 211 
HOH   H2   H N N 212 
ILE   N    N N N 213 
ILE   CA   C N S 214 
ILE   C    C N N 215 
ILE   O    O N N 216 
ILE   CB   C N S 217 
ILE   CG1  C N N 218 
ILE   CG2  C N N 219 
ILE   CD1  C N N 220 
ILE   OXT  O N N 221 
ILE   H    H N N 222 
ILE   H2   H N N 223 
ILE   HA   H N N 224 
ILE   HB   H N N 225 
ILE   HG12 H N N 226 
ILE   HG13 H N N 227 
ILE   HG21 H N N 228 
ILE   HG22 H N N 229 
ILE   HG23 H N N 230 
ILE   HD11 H N N 231 
ILE   HD12 H N N 232 
ILE   HD13 H N N 233 
ILE   HXT  H N N 234 
LEU   N    N N N 235 
LEU   CA   C N S 236 
LEU   C    C N N 237 
LEU   O    O N N 238 
LEU   CB   C N N 239 
LEU   CG   C N N 240 
LEU   CD1  C N N 241 
LEU   CD2  C N N 242 
LEU   OXT  O N N 243 
LEU   H    H N N 244 
LEU   H2   H N N 245 
LEU   HA   H N N 246 
LEU   HB2  H N N 247 
LEU   HB3  H N N 248 
LEU   HG   H N N 249 
LEU   HD11 H N N 250 
LEU   HD12 H N N 251 
LEU   HD13 H N N 252 
LEU   HD21 H N N 253 
LEU   HD22 H N N 254 
LEU   HD23 H N N 255 
LEU   HXT  H N N 256 
LYS   N    N N N 257 
LYS   CA   C N S 258 
LYS   C    C N N 259 
LYS   O    O N N 260 
LYS   CB   C N N 261 
LYS   CG   C N N 262 
LYS   CD   C N N 263 
LYS   CE   C N N 264 
LYS   NZ   N N N 265 
LYS   OXT  O N N 266 
LYS   H    H N N 267 
LYS   H2   H N N 268 
LYS   HA   H N N 269 
LYS   HB2  H N N 270 
LYS   HB3  H N N 271 
LYS   HG2  H N N 272 
LYS   HG3  H N N 273 
LYS   HD2  H N N 274 
LYS   HD3  H N N 275 
LYS   HE2  H N N 276 
LYS   HE3  H N N 277 
LYS   HZ1  H N N 278 
LYS   HZ2  H N N 279 
LYS   HZ3  H N N 280 
LYS   HXT  H N N 281 
MET   N    N N N 282 
MET   CA   C N S 283 
MET   C    C N N 284 
MET   O    O N N 285 
MET   CB   C N N 286 
MET   CG   C N N 287 
MET   SD   S N N 288 
MET   CE   C N N 289 
MET   OXT  O N N 290 
MET   H    H N N 291 
MET   H2   H N N 292 
MET   HA   H N N 293 
MET   HB2  H N N 294 
MET   HB3  H N N 295 
MET   HG2  H N N 296 
MET   HG3  H N N 297 
MET   HE1  H N N 298 
MET   HE2  H N N 299 
MET   HE3  H N N 300 
MET   HXT  H N N 301 
PHE   N    N N N 302 
PHE   CA   C N S 303 
PHE   C    C N N 304 
PHE   O    O N N 305 
PHE   CB   C N N 306 
PHE   CG   C Y N 307 
PHE   CD1  C Y N 308 
PHE   CD2  C Y N 309 
PHE   CE1  C Y N 310 
PHE   CE2  C Y N 311 
PHE   CZ   C Y N 312 
PHE   OXT  O N N 313 
PHE   H    H N N 314 
PHE   H2   H N N 315 
PHE   HA   H N N 316 
PHE   HB2  H N N 317 
PHE   HB3  H N N 318 
PHE   HD1  H N N 319 
PHE   HD2  H N N 320 
PHE   HE1  H N N 321 
PHE   HE2  H N N 322 
PHE   HZ   H N N 323 
PHE   HXT  H N N 324 
PRO   N    N N N 325 
PRO   CA   C N S 326 
PRO   C    C N N 327 
PRO   O    O N N 328 
PRO   CB   C N N 329 
PRO   CG   C N N 330 
PRO   CD   C N N 331 
PRO   OXT  O N N 332 
PRO   H    H N N 333 
PRO   HA   H N N 334 
PRO   HB2  H N N 335 
PRO   HB3  H N N 336 
PRO   HG2  H N N 337 
PRO   HG3  H N N 338 
PRO   HD2  H N N 339 
PRO   HD3  H N N 340 
PRO   HXT  H N N 341 
SER   N    N N N 342 
SER   CA   C N S 343 
SER   C    C N N 344 
SER   O    O N N 345 
SER   CB   C N N 346 
SER   OG   O N N 347 
SER   OXT  O N N 348 
SER   H    H N N 349 
SER   H2   H N N 350 
SER   HA   H N N 351 
SER   HB2  H N N 352 
SER   HB3  H N N 353 
SER   HG   H N N 354 
SER   HXT  H N N 355 
SO4   S    S N N 356 
SO4   O1   O N N 357 
SO4   O2   O N N 358 
SO4   O3   O N N 359 
SO4   O4   O N N 360 
THR   N    N N N 361 
THR   CA   C N S 362 
THR   C    C N N 363 
THR   O    O N N 364 
THR   CB   C N R 365 
THR   OG1  O N N 366 
THR   CG2  C N N 367 
THR   OXT  O N N 368 
THR   H    H N N 369 
THR   H2   H N N 370 
THR   HA   H N N 371 
THR   HB   H N N 372 
THR   HG1  H N N 373 
THR   HG21 H N N 374 
THR   HG22 H N N 375 
THR   HG23 H N N 376 
THR   HXT  H N N 377 
TRP   N    N N N 378 
TRP   CA   C N S 379 
TRP   C    C N N 380 
TRP   O    O N N 381 
TRP   CB   C N N 382 
TRP   CG   C Y N 383 
TRP   CD1  C Y N 384 
TRP   CD2  C Y N 385 
TRP   NE1  N Y N 386 
TRP   CE2  C Y N 387 
TRP   CE3  C Y N 388 
TRP   CZ2  C Y N 389 
TRP   CZ3  C Y N 390 
TRP   CH2  C Y N 391 
TRP   OXT  O N N 392 
TRP   H    H N N 393 
TRP   H2   H N N 394 
TRP   HA   H N N 395 
TRP   HB2  H N N 396 
TRP   HB3  H N N 397 
TRP   HD1  H N N 398 
TRP   HE1  H N N 399 
TRP   HE3  H N N 400 
TRP   HZ2  H N N 401 
TRP   HZ3  H N N 402 
TRP   HH2  H N N 403 
TRP   HXT  H N N 404 
TYR   N    N N N 405 
TYR   CA   C N S 406 
TYR   C    C N N 407 
TYR   O    O N N 408 
TYR   CB   C N N 409 
TYR   CG   C Y N 410 
TYR   CD1  C Y N 411 
TYR   CD2  C Y N 412 
TYR   CE1  C Y N 413 
TYR   CE2  C Y N 414 
TYR   CZ   C Y N 415 
TYR   OH   O N N 416 
TYR   OXT  O N N 417 
TYR   H    H N N 418 
TYR   H2   H N N 419 
TYR   HA   H N N 420 
TYR   HB2  H N N 421 
TYR   HB3  H N N 422 
TYR   HD1  H N N 423 
TYR   HD2  H N N 424 
TYR   HE1  H N N 425 
TYR   HE2  H N N 426 
TYR   HH   H N N 427 
TYR   HXT  H N N 428 
VAL   N    N N N 429 
VAL   CA   C N S 430 
VAL   C    C N N 431 
VAL   O    O N N 432 
VAL   CB   C N N 433 
VAL   CG1  C N N 434 
VAL   CG2  C N N 435 
VAL   OXT  O N N 436 
VAL   H    H N N 437 
VAL   H2   H N N 438 
VAL   HA   H N N 439 
VAL   HB   H N N 440 
VAL   HG11 H N N 441 
VAL   HG12 H N N 442 
VAL   HG13 H N N 443 
VAL   HG21 H N N 444 
VAL   HG22 H N N 445 
VAL   HG23 H N N 446 
VAL   HXT  H N N 447 
# 
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 
A1EJX O18 C1   doub N N 1   
A1EJX C1  N3   sing N N 2   
A1EJX C1  C2   sing N N 3   
A1EJX N23 C22  doub Y N 4   
A1EJX N23 N21  sing Y N 5   
A1EJX N20 C2   sing N N 6   
A1EJX C22 C7   sing Y N 7   
A1EJX N3  C13  sing N N 8   
A1EJX C2  C4   doub N N 9   
A1EJX N21 C8   sing Y N 10  
A1EJX C7  C8   doub Y N 11  
A1EJX C7  C6   sing Y N 12  
A1EJX C13 C15  doub Y N 13  
A1EJX C13 C5   sing Y N 14  
A1EJX C4  C5   sing N N 15  
A1EJX C4  C6   sing N N 16  
A1EJX C15 C17  sing Y N 17  
A1EJX C5  N14  doub Y N 18  
A1EJX C8  C9   sing Y N 19  
A1EJX C6  C11  doub Y N 20  
A1EJX C28 C27  doub Y N 21  
A1EJX C28 C19  sing Y N 22  
A1EJX C27 C26  sing Y N 23  
A1EJX C17 C19  sing N N 24  
A1EJX C17 C16  doub Y N 25  
A1EJX N14 C16  sing Y N 26  
A1EJX C19 C24  doub Y N 27  
A1EJX O31 C29  doub N N 28  
A1EJX C9  F12  sing N N 29  
A1EJX C9  C10  doub Y N 30  
A1EJX C11 C10  sing Y N 31  
A1EJX C26 C29  sing N N 32  
A1EJX C26 C25  doub Y N 33  
A1EJX C29 N30  sing N N 34  
A1EJX C24 C25  sing Y N 35  
A1EJX N30 C32  sing N N 36  
A1EJX N30 C33  sing N N 37  
A1EJX C10 H1   sing N N 38  
A1EJX C11 H2   sing N N 39  
A1EJX C15 H3   sing N N 40  
A1EJX C16 H4   sing N N 41  
A1EJX C22 H5   sing N N 42  
A1EJX C24 H6   sing N N 43  
A1EJX C25 H7   sing N N 44  
A1EJX C27 H8   sing N N 45  
A1EJX C28 H9   sing N N 46  
A1EJX C32 H10  sing N N 47  
A1EJX C32 H11  sing N N 48  
A1EJX C32 H12  sing N N 49  
A1EJX C33 H13  sing N N 50  
A1EJX C33 H14  sing N N 51  
A1EJX C33 H15  sing N N 52  
A1EJX N20 H16  sing N N 53  
A1EJX N20 H17  sing N N 54  
A1EJX N21 H18  sing N N 55  
A1EJX N3  H19  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
SO4   S   O1   doub N N 346 
SO4   S   O2   doub N N 347 
SO4   S   O3   sing N N 348 
SO4   S   O4   sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_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   5VCV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LID 
_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]   0.019808 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007339 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008900 
_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]   0.014732 
_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 
F 
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   . LEU   A 1 3   ? 22.186  11.646  49.281 1.00 102.37 ? 77  LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 3   ? 21.482  10.976  48.193 1.00 101.73 ? 77  LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 3   ? 22.037  11.395  46.837 1.00 103.74 ? 77  LEU   A C   1 
ATOM   4    O O   . LEU   A 1 3   ? 22.181  12.580  46.552 1.00 104.61 ? 77  LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 3   ? 19.982  11.264  48.260 1.00 92.06  ? 77  LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 3   ? 19.189  10.313  49.162 1.00 95.21  ? 77  LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 3   ? 19.496  10.539  50.646 1.00 98.62  ? 77  LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 3   ? 17.698  10.430  48.877 1.00 94.07  ? 77  LEU   A CD2 1 
ATOM   9    N N   . GLN   A 1 4   ? 22.338  10.409  45.996 1.00 117.86 ? 78  GLN   A N   1 
ATOM   10   C CA  . GLN   A 1 4   ? 23.069  10.660  44.770 1.00 114.45 ? 78  GLN   A CA  1 
ATOM   11   C C   . GLN   A 1 4   ? 22.269  10.205  43.557 1.00 110.53 ? 78  GLN   A C   1 
ATOM   12   O O   . GLN   A 1 4   ? 21.540  9.211   43.625 1.00 108.63 ? 78  GLN   A O   1 
ATOM   13   C CB  . GLN   A 1 4   ? 24.421  9.937   44.794 1.00 114.53 ? 78  GLN   A CB  1 
ATOM   14   C CG  . GLN   A 1 4   ? 25.162  10.082  46.117 1.00 118.26 ? 78  GLN   A CG  1 
ATOM   15   C CD  . GLN   A 1 4   ? 25.522  11.525  46.431 1.00 122.19 ? 78  GLN   A CD  1 
ATOM   16   O OE1 . GLN   A 1 4   ? 25.625  12.364  45.533 1.00 121.08 ? 78  GLN   A OE1 1 
ATOM   17   N NE2 . GLN   A 1 4   ? 25.714  11.822  47.714 1.00 124.39 ? 78  GLN   A NE2 1 
ATOM   18   N N   . PRO   A 1 5   ? 22.383  10.919  42.436 1.00 99.57  ? 79  PRO   A N   1 
ATOM   19   C CA  . PRO   A 1 5   ? 21.658  10.523  41.220 1.00 94.26  ? 79  PRO   A CA  1 
ATOM   20   C C   . PRO   A 1 5   ? 22.348  9.352   40.533 1.00 92.44  ? 79  PRO   A C   1 
ATOM   21   O O   . PRO   A 1 5   ? 23.559  9.373   40.299 1.00 95.62  ? 79  PRO   A O   1 
ATOM   22   C CB  . PRO   A 1 5   ? 21.701  11.785  40.353 1.00 93.70  ? 79  PRO   A CB  1 
ATOM   23   C CG  . PRO   A 1 5   ? 22.945  12.480  40.790 1.00 96.17  ? 79  PRO   A CG  1 
ATOM   24   C CD  . PRO   A 1 5   ? 23.103  12.191  42.261 1.00 103.35 ? 79  PRO   A CD  1 
ATOM   25   N N   . ARG   A 1 6   ? 21.565  8.329   40.212 1.00 86.09  ? 80  ARG   A N   1 
ATOM   26   C CA  . ARG   A 1 6   ? 22.056  7.107   39.593 1.00 77.76  ? 80  ARG   A CA  1 
ATOM   27   C C   . ARG   A 1 6   ? 21.541  7.050   38.163 1.00 73.83  ? 80  ARG   A C   1 
ATOM   28   O O   . ARG   A 1 6   ? 20.358  7.306   37.919 1.00 69.58  ? 80  ARG   A O   1 
ATOM   29   C CB  . ARG   A 1 6   ? 21.589  5.894   40.396 1.00 77.79  ? 80  ARG   A CB  1 
ATOM   30   C CG  . ARG   A 1 6   ? 21.957  4.549   39.819 1.00 78.52  ? 80  ARG   A CG  1 
ATOM   31   C CD  . ARG   A 1 6   ? 21.331  3.441   40.657 1.00 78.50  ? 80  ARG   A CD  1 
ATOM   32   N NE  . ARG   A 1 6   ? 21.735  2.111   40.217 1.00 79.93  ? 80  ARG   A NE  1 
ATOM   33   C CZ  . ARG   A 1 6   ? 21.178  1.460   39.206 1.00 76.55  ? 80  ARG   A CZ  1 
ATOM   34   N NH1 . ARG   A 1 6   ? 20.202  2.000   38.493 1.00 72.41  ? 80  ARG   A NH1 1 
ATOM   35   N NH2 . ARG   A 1 6   ? 21.613  0.240   38.901 1.00 78.56  ? 80  ARG   A NH2 1 
ATOM   36   N N   . ARG   A 1 7   ? 22.421  6.742   37.217 1.00 75.74  ? 81  ARG   A N   1 
ATOM   37   C CA  . ARG   A 1 7   ? 21.995  6.736   35.827 1.00 72.78  ? 81  ARG   A CA  1 
ATOM   38   C C   . ARG   A 1 7   ? 21.154  5.500   35.532 1.00 69.71  ? 81  ARG   A C   1 
ATOM   39   O O   . ARG   A 1 7   ? 21.334  4.440   36.139 1.00 71.13  ? 81  ARG   A O   1 
ATOM   40   C CB  . ARG   A 1 7   ? 23.192  6.787   34.880 1.00 76.37  ? 81  ARG   A CB  1 
ATOM   41   C CG  . ARG   A 1 7   ? 22.790  7.211   33.485 1.00 74.14  ? 81  ARG   A CG  1 
ATOM   42   C CD  . ARG   A 1 7   ? 23.755  6.742   32.424 1.00 77.37  ? 81  ARG   A CD  1 
ATOM   43   N NE  . ARG   A 1 7   ? 23.125  6.791   31.110 1.00 76.55  ? 81  ARG   A NE  1 
ATOM   44   C CZ  . ARG   A 1 7   ? 23.736  6.494   29.971 1.00 84.17  ? 81  ARG   A CZ  1 
ATOM   45   N NH1 . ARG   A 1 7   ? 25.010  6.130   29.946 1.00 84.27  ? 81  ARG   A NH1 1 
ATOM   46   N NH2 . ARG   A 1 7   ? 23.052  6.564   28.831 1.00 75.26  ? 81  ARG   A NH2 1 
ATOM   47   N N   . VAL   A 1 8   ? 20.225  5.644   34.590 1.00 66.74  ? 82  VAL   A N   1 
ATOM   48   C CA  . VAL   A 1 8   ? 19.303  4.573   34.220 1.00 64.69  ? 82  VAL   A CA  1 
ATOM   49   C C   . VAL   A 1 8   ? 19.451  4.287   32.732 1.00 65.71  ? 82  VAL   A C   1 
ATOM   50   O O   . VAL   A 1 8   ? 19.155  5.148   31.891 1.00 66.52  ? 82  VAL   A O   1 
ATOM   51   C CB  . VAL   A 1 8   ? 17.847  4.922   34.565 1.00 61.88  ? 82  VAL   A CB  1 
ATOM   52   C CG1 . VAL   A 1 8   ? 16.905  3.897   33.955 1.00 57.10  ? 82  VAL   A CG1 1 
ATOM   53   C CG2 . VAL   A 1 8   ? 17.663  4.976   36.073 1.00 65.99  ? 82  VAL   A CG2 1 
ATOM   54   N N   . SER   A 1 9   ? 19.898  3.075   32.411 1.00 65.63  ? 83  SER   A N   1 
ATOM   55   C CA  . SER   A 1 9   ? 20.008  2.614   31.036 1.00 70.77  ? 83  SER   A CA  1 
ATOM   56   C C   . SER   A 1 9   ? 19.907  1.096   31.043 1.00 73.80  ? 83  SER   A C   1 
ATOM   57   O O   . SER   A 1 9   ? 20.217  0.444   32.044 1.00 77.86  ? 83  SER   A O   1 
ATOM   58   C CB  . SER   A 1 9   ? 21.324  3.075   30.390 1.00 72.96  ? 83  SER   A CB  1 
ATOM   59   O OG  . SER   A 1 9   ? 21.338  2.825   28.992 1.00 73.92  ? 83  SER   A OG  1 
ATOM   60   N N   . PHE   A 1 10  ? 19.463  0.537   29.919 1.00 76.73  ? 84  PHE   A N   1 
ATOM   61   C CA  . PHE   A 1 10  ? 19.358  -0.912  29.749 1.00 76.04  ? 84  PHE   A CA  1 
ATOM   62   C C   . PHE   A 1 10  ? 20.471  -1.470  28.868 1.00 82.34  ? 84  PHE   A C   1 
ATOM   63   O O   . PHE   A 1 10  ? 20.221  -2.295  27.984 1.00 87.17  ? 84  PHE   A O   1 
ATOM   64   C CB  . PHE   A 1 10  ? 17.992  -1.285  29.181 1.00 72.42  ? 84  PHE   A CB  1 
ATOM   65   C CG  . PHE   A 1 10  ? 16.885  -1.267  30.193 1.00 67.42  ? 84  PHE   A CG  1 
ATOM   66   C CD1 . PHE   A 1 10  ? 16.360  -0.069  30.650 1.00 68.57  ? 84  PHE   A CD1 1 
ATOM   67   C CD2 . PHE   A 1 10  ? 16.367  -2.450  30.687 1.00 68.36  ? 84  PHE   A CD2 1 
ATOM   68   C CE1 . PHE   A 1 10  ? 15.333  -0.054  31.578 1.00 63.00  ? 84  PHE   A CE1 1 
ATOM   69   C CE2 . PHE   A 1 10  ? 15.345  -2.442  31.618 1.00 67.46  ? 84  PHE   A CE2 1 
ATOM   70   C CZ  . PHE   A 1 10  ? 14.828  -1.244  32.064 1.00 62.92  ? 84  PHE   A CZ  1 
ATOM   71   N N   . ARG   A 1 11  ? 21.711  -1.039  29.088 1.00 88.29  ? 85  ARG   A N   1 
ATOM   72   C CA  . ARG   A 1 11  ? 22.859  -1.567  28.354 1.00 89.07  ? 85  ARG   A CA  1 
ATOM   73   C C   . ARG   A 1 11  ? 24.055  -1.737  29.292 1.00 96.05  ? 85  ARG   A C   1 
ATOM   74   O O   . ARG   A 1 11  ? 24.670  -2.805  29.351 1.00 96.32  ? 85  ARG   A O   1 
ATOM   75   C CB  . ARG   A 1 11  ? 23.227  -0.648  27.180 1.00 93.75  ? 85  ARG   A CB  1 
ATOM   76   C CG  . ARG   A 1 11  ? 22.218  -0.666  26.031 1.00 96.06  ? 85  ARG   A CG  1 
ATOM   77   C CD  . ARG   A 1 11  ? 22.466  0.439   25.000 1.00 96.38  ? 85  ARG   A CD  1 
ATOM   78   N NE  . ARG   A 1 11  ? 21.962  1.741   25.430 1.00 93.77  ? 85  ARG   A NE  1 
ATOM   79   C CZ  . ARG   A 1 11  ? 21.955  2.832   24.675 1.00 95.58  ? 85  ARG   A CZ  1 
ATOM   80   N NH1 . ARG   A 1 11  ? 22.393  2.813   23.427 1.00 100.52 ? 85  ARG   A NH1 1 
ATOM   81   N NH2 . ARG   A 1 11  ? 21.503  3.974   25.188 1.00 93.83  ? 85  ARG   A NH2 1 
ATOM   82   N N   . SER   A 1 20  ? 27.810  16.377  34.137 1.00 112.89 ? 94  SER   A N   1 
ATOM   83   C CA  . SER   A 1 20  ? 27.306  17.049  35.329 1.00 111.92 ? 94  SER   A CA  1 
ATOM   84   C C   . SER   A 1 20  ? 28.310  18.057  35.890 1.00 124.55 ? 94  SER   A C   1 
ATOM   85   O O   . SER   A 1 20  ? 28.882  17.834  36.960 1.00 122.04 ? 94  SER   A O   1 
ATOM   86   C CB  . SER   A 1 20  ? 26.951  16.017  36.400 1.00 107.56 ? 94  SER   A CB  1 
ATOM   87   O OG  . SER   A 1 20  ? 28.031  15.129  36.628 1.00 114.46 ? 94  SER   A OG  1 
ATOM   88   N N   . PRO   A 1 21  ? 28.528  19.170  35.168 1.00 137.63 ? 95  PRO   A N   1 
ATOM   89   C CA  . PRO   A 1 21  ? 29.478  20.186  35.647 1.00 139.99 ? 95  PRO   A CA  1 
ATOM   90   C C   . PRO   A 1 21  ? 28.870  21.110  36.690 1.00 139.61 ? 95  PRO   A C   1 
ATOM   91   O O   . PRO   A 1 21  ? 29.524  21.452  37.680 1.00 141.95 ? 95  PRO   A O   1 
ATOM   92   C CB  . PRO   A 1 21  ? 29.848  20.958  34.370 1.00 141.77 ? 95  PRO   A CB  1 
ATOM   93   C CG  . PRO   A 1 21  ? 29.243  20.182  33.228 1.00 137.98 ? 95  PRO   A CG  1 
ATOM   94   C CD  . PRO   A 1 21  ? 28.063  19.474  33.808 1.00 132.97 ? 95  PRO   A CD  1 
ATOM   95   N N   . GLY   A 1 22  ? 27.623  21.531  36.470 1.00 125.77 ? 96  GLY   A N   1 
ATOM   96   C CA  . GLY   A 1 22  ? 26.938  22.382  37.428 1.00 113.99 ? 96  GLY   A CA  1 
ATOM   97   C C   . GLY   A 1 22  ? 26.511  21.680  38.701 1.00 113.83 ? 96  GLY   A C   1 
ATOM   98   O O   . GLY   A 1 22  ? 26.054  22.353  39.632 1.00 111.67 ? 96  GLY   A O   1 
ATOM   99   N N   . TYR   A 1 23  ? 26.657  20.356  38.766 1.00 113.50 ? 97  TYR   A N   1 
ATOM   100  C CA  . TYR   A 1 23  ? 26.232  19.575  39.921 1.00 107.96 ? 97  TYR   A CA  1 
ATOM   101  C C   . TYR   A 1 23  ? 27.388  19.418  40.901 1.00 111.73 ? 97  TYR   A C   1 
ATOM   102  O O   . TYR   A 1 23  ? 28.417  18.817  40.570 1.00 110.41 ? 97  TYR   A O   1 
ATOM   103  C CB  . TYR   A 1 23  ? 25.716  18.203  39.489 1.00 103.91 ? 97  TYR   A CB  1 
ATOM   104  C CG  . TYR   A 1 23  ? 25.292  17.311  40.641 1.00 99.11  ? 97  TYR   A CG  1 
ATOM   105  C CD1 . TYR   A 1 23  ? 24.198  17.642  41.435 1.00 98.97  ? 97  TYR   A CD1 1 
ATOM   106  C CD2 . TYR   A 1 23  ? 25.974  16.134  40.925 1.00 97.88  ? 97  TYR   A CD2 1 
ATOM   107  C CE1 . TYR   A 1 23  ? 23.799  16.830  42.486 1.00 98.32  ? 97  TYR   A CE1 1 
ATOM   108  C CE2 . TYR   A 1 23  ? 25.582  15.313  41.976 1.00 99.08  ? 97  TYR   A CE2 1 
ATOM   109  C CZ  . TYR   A 1 23  ? 24.493  15.667  42.752 1.00 99.49  ? 97  TYR   A CZ  1 
ATOM   110  O OH  . TYR   A 1 23  ? 24.095  14.860  43.797 1.00 97.39  ? 97  TYR   A OH  1 
ATOM   111  N N   . ASP   A 1 24  ? 27.212  19.956  42.106 1.00 115.25 ? 98  ASP   A N   1 
ATOM   112  C CA  . ASP   A 1 24  ? 28.140  19.730  43.200 1.00 116.84 ? 98  ASP   A CA  1 
ATOM   113  C C   . ASP   A 1 24  ? 27.565  18.649  44.101 1.00 118.10 ? 98  ASP   A C   1 
ATOM   114  O O   . ASP   A 1 24  ? 26.591  18.917  44.822 1.00 118.04 ? 98  ASP   A O   1 
ATOM   115  C CB  . ASP   A 1 24  ? 28.366  21.018  43.987 1.00 120.84 ? 98  ASP   A CB  1 
ATOM   116  C CG  . ASP   A 1 24  ? 29.132  20.787  45.272 1.00 128.92 ? 98  ASP   A CG  1 
ATOM   117  O OD1 . ASP   A 1 24  ? 30.330  20.436  45.200 1.00 131.77 ? 98  ASP   A OD1 1 
ATOM   118  O OD2 . ASP   A 1 24  ? 28.535  20.959  46.356 1.00 130.66 ? 98  ASP   A OD2 1 
ATOM   119  N N   . PRO   A 1 25  ? 28.116  17.429  44.103 1.00 119.40 ? 99  PRO   A N   1 
ATOM   120  C CA  . PRO   A 1 25  ? 27.533  16.351  44.924 1.00 117.16 ? 99  PRO   A CA  1 
ATOM   121  C C   . PRO   A 1 25  ? 27.442  16.672  46.413 1.00 122.30 ? 99  PRO   A C   1 
ATOM   122  O O   . PRO   A 1 25  ? 26.830  15.889  47.154 1.00 115.16 ? 99  PRO   A O   1 
ATOM   123  C CB  . PRO   A 1 25  ? 28.476  15.165  44.669 1.00 115.29 ? 99  PRO   A CB  1 
ATOM   124  C CG  . PRO   A 1 25  ? 29.102  15.459  43.343 1.00 115.44 ? 99  PRO   A CG  1 
ATOM   125  C CD  . PRO   A 1 25  ? 29.242  16.952  43.280 1.00 116.96 ? 99  PRO   A CD  1 
ATOM   126  N N   . SER   A 1 26  ? 28.015  17.792  46.868 1.00 124.24 ? 100 SER   A N   1 
ATOM   127  C CA  . SER   A 1 26  ? 27.962  18.190  48.269 1.00 124.27 ? 100 SER   A CA  1 
ATOM   128  C C   . SER   A 1 26  ? 26.790  19.108  48.597 1.00 120.95 ? 100 SER   A C   1 
ATOM   129  O O   . SER   A 1 26  ? 26.442  19.245  49.776 1.00 123.19 ? 100 SER   A O   1 
ATOM   130  C CB  . SER   A 1 26  ? 29.265  18.889  48.665 1.00 131.86 ? 100 SER   A CB  1 
ATOM   131  O OG  . SER   A 1 26  ? 30.389  18.121  48.279 1.00 135.52 ? 100 SER   A OG  1 
ATOM   132  N N   . ARG   A 1 27  ? 26.182  19.750  47.594 1.00 120.72 ? 101 ARG   A N   1 
ATOM   133  C CA  . ARG   A 1 27  ? 25.036  20.607  47.853 1.00 114.67 ? 101 ARG   A CA  1 
ATOM   134  C C   . ARG   A 1 27  ? 23.770  19.766  48.034 1.00 115.27 ? 101 ARG   A C   1 
ATOM   135  O O   . ARG   A 1 27  ? 23.649  18.680  47.460 1.00 105.85 ? 101 ARG   A O   1 
ATOM   136  C CB  . ARG   A 1 27  ? 24.842  21.604  46.713 1.00 115.77 ? 101 ARG   A CB  1 
ATOM   137  C CG  . ARG   A 1 27  ? 25.812  22.780  46.737 1.00 120.32 ? 101 ARG   A CG  1 
ATOM   138  C CD  . ARG   A 1 27  ? 25.638  23.617  48.000 1.00 125.75 ? 101 ARG   A CD  1 
ATOM   139  N NE  . ARG   A 1 27  ? 24.382  24.360  47.993 1.00 126.60 ? 101 ARG   A NE  1 
ATOM   140  C CZ  . ARG   A 1 27  ? 24.289  25.681  47.904 1.00 131.94 ? 101 ARG   A CZ  1 
ATOM   141  N NH1 . ARG   A 1 27  ? 25.367  26.450  47.850 1.00 122.77 ? 101 ARG   A NH1 1 
ATOM   142  N NH2 . ARG   A 1 27  ? 23.084  26.244  47.876 1.00 131.67 ? 101 ARG   A NH2 1 
ATOM   143  N N   . PRO   A 1 28  ? 22.811  20.249  48.835 1.00 118.81 ? 102 PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 28  ? 21.594  19.456  49.085 1.00 110.81 ? 102 PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 28  ? 20.588  19.451  47.941 1.00 112.18 ? 102 PRO   A C   1 
ATOM   146  O O   . PRO   A 1 28  ? 19.780  18.516  47.865 1.00 109.98 ? 102 PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 28  ? 20.994  20.122  50.332 1.00 111.67 ? 102 PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 28  ? 21.468  21.538  50.252 1.00 109.97 ? 102 PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 28  ? 22.849  21.477  49.650 1.00 111.49 ? 102 PRO   A CD  1 
ATOM   150  N N   . GLU   A 1 29  ? 20.593  20.459  47.067 1.00 113.76 ? 103 GLU   A N   1 
ATOM   151  C CA  . GLU   A 1 29  ? 19.636  20.498  45.966 1.00 109.04 ? 103 GLU   A CA  1 
ATOM   152  C C   . GLU   A 1 29  ? 19.846  19.314  45.027 1.00 106.45 ? 103 GLU   A C   1 
ATOM   153  O O   . GLU   A 1 29  ? 20.962  18.817  44.856 1.00 107.05 ? 103 GLU   A O   1 
ATOM   154  C CB  . GLU   A 1 29  ? 19.761  21.811  45.186 1.00 109.24 ? 103 GLU   A CB  1 
ATOM   155  C CG  . GLU   A 1 29  ? 19.310  23.048  45.950 1.00 109.96 ? 103 GLU   A CG  1 
ATOM   156  C CD  . GLU   A 1 29  ? 20.359  23.559  46.916 1.00 118.63 ? 103 GLU   A CD  1 
ATOM   157  O OE1 . GLU   A 1 29  ? 21.558  23.289  46.694 1.00 122.64 ? 103 GLU   A OE1 1 
ATOM   158  O OE2 . GLU   A 1 29  ? 19.984  24.234  47.898 1.00 122.57 ? 103 GLU   A OE2 1 
ATOM   159  N N   . SER   A 1 30  ? 18.756  18.864  44.410 1.00 99.87  ? 104 SER   A N   1 
ATOM   160  C CA  . SER   A 1 30  ? 18.814  17.674  43.574 1.00 94.69  ? 104 SER   A CA  1 
ATOM   161  C C   . SER   A 1 30  ? 19.613  17.942  42.300 1.00 86.95  ? 104 SER   A C   1 
ATOM   162  O O   . SER   A 1 30  ? 19.813  19.088  41.887 1.00 90.65  ? 104 SER   A O   1 
ATOM   163  C CB  . SER   A 1 30  ? 17.404  17.195  43.219 1.00 87.93  ? 104 SER   A CB  1 
ATOM   164  O OG  . SER   A 1 30  ? 16.745  18.125  42.378 1.00 86.43  ? 104 SER   A OG  1 
ATOM   165  N N   . PHE   A 1 31  ? 20.080  16.853  41.682 1.00 84.50  ? 105 PHE   A N   1 
ATOM   166  C CA  . PHE   A 1 31  ? 20.780  16.957  40.405 1.00 82.97  ? 105 PHE   A CA  1 
ATOM   167  C C   . PHE   A 1 31  ? 19.931  17.665  39.359 1.00 84.49  ? 105 PHE   A C   1 
ATOM   168  O O   . PHE   A 1 31  ? 20.467  18.358  38.482 1.00 85.89  ? 105 PHE   A O   1 
ATOM   169  C CB  . PHE   A 1 31  ? 21.176  15.563  39.914 1.00 81.69  ? 105 PHE   A CB  1 
ATOM   170  C CG  . PHE   A 1 31  ? 21.713  15.544  38.514 1.00 77.83  ? 105 PHE   A CG  1 
ATOM   171  C CD1 . PHE   A 1 31  ? 23.038  15.847  38.263 1.00 82.27  ? 105 PHE   A CD1 1 
ATOM   172  C CD2 . PHE   A 1 31  ? 20.892  15.227  37.445 1.00 76.10  ? 105 PHE   A CD2 1 
ATOM   173  C CE1 . PHE   A 1 31  ? 23.535  15.832  36.975 1.00 81.42  ? 105 PHE   A CE1 1 
ATOM   174  C CE2 . PHE   A 1 31  ? 21.383  15.214  36.154 1.00 70.80  ? 105 PHE   A CE2 1 
ATOM   175  C CZ  . PHE   A 1 31  ? 22.706  15.515  35.920 1.00 81.06  ? 105 PHE   A CZ  1 
ATOM   176  N N   . PHE   A 1 32  ? 18.611  17.499  39.431 1.00 80.33  ? 106 PHE   A N   1 
ATOM   177  C CA  . PHE   A 1 32  ? 17.721  18.215  38.526 1.00 79.00  ? 106 PHE   A CA  1 
ATOM   178  C C   . PHE   A 1 32  ? 17.825  19.719  38.744 1.00 83.04  ? 106 PHE   A C   1 
ATOM   179  O O   . PHE   A 1 32  ? 17.951  20.491  37.787 1.00 85.36  ? 106 PHE   A O   1 
ATOM   180  C CB  . PHE   A 1 32  ? 16.285  17.724  38.725 1.00 75.95  ? 106 PHE   A CB  1 
ATOM   181  C CG  . PHE   A 1 32  ? 15.281  18.378  37.816 1.00 72.86  ? 106 PHE   A CG  1 
ATOM   182  C CD1 . PHE   A 1 32  ? 15.545  18.535  36.465 1.00 70.10  ? 106 PHE   A CD1 1 
ATOM   183  C CD2 . PHE   A 1 32  ? 14.061  18.811  38.310 1.00 72.62  ? 106 PHE   A CD2 1 
ATOM   184  C CE1 . PHE   A 1 32  ? 14.616  19.127  35.626 1.00 71.98  ? 106 PHE   A CE1 1 
ATOM   185  C CE2 . PHE   A 1 32  ? 13.127  19.402  37.476 1.00 74.53  ? 106 PHE   A CE2 1 
ATOM   186  C CZ  . PHE   A 1 32  ? 13.405  19.559  36.131 1.00 71.62  ? 106 PHE   A CZ  1 
ATOM   187  N N   . GLN   A 1 33  ? 17.801  20.153  40.004 1.00 80.66  ? 107 GLN   A N   1 
ATOM   188  C CA  . GLN   A 1 33  ? 17.811  21.578  40.302 1.00 88.46  ? 107 GLN   A CA  1 
ATOM   189  C C   . GLN   A 1 33  ? 19.184  22.211  40.126 1.00 84.97  ? 107 GLN   A C   1 
ATOM   190  O O   . GLN   A 1 33  ? 19.269  23.433  39.964 1.00 89.83  ? 107 GLN   A O   1 
ATOM   191  C CB  . GLN   A 1 33  ? 17.292  21.804  41.722 1.00 86.75  ? 107 GLN   A CB  1 
ATOM   192  C CG  . GLN   A 1 33  ? 15.902  21.219  41.914 1.00 93.89  ? 107 GLN   A CG  1 
ATOM   193  C CD  . GLN   A 1 33  ? 15.482  21.149  43.363 1.00 98.23  ? 107 GLN   A CD  1 
ATOM   194  O OE1 . GLN   A 1 33  ? 16.229  21.543  44.259 1.00 93.57  ? 107 GLN   A OE1 1 
ATOM   195  N NE2 . GLN   A 1 33  ? 14.275  20.640  43.603 1.00 98.90  ? 107 GLN   A NE2 1 
ATOM   196  N N   . GLN   A 1 34  ? 20.253  21.415  40.131 1.00 85.25  ? 108 GLN   A N   1 
ATOM   197  C CA  . GLN   A 1 34  ? 21.600  21.954  39.994 1.00 87.16  ? 108 GLN   A CA  1 
ATOM   198  C C   . GLN   A 1 34  ? 22.125  21.932  38.567 1.00 85.40  ? 108 GLN   A C   1 
ATOM   199  O O   . GLN   A 1 34  ? 23.016  22.721  38.242 1.00 90.43  ? 108 GLN   A O   1 
ATOM   200  C CB  . GLN   A 1 34  ? 22.580  21.183  40.885 1.00 93.94  ? 108 GLN   A CB  1 
ATOM   201  C CG  . GLN   A 1 34  ? 22.260  21.244  42.364 1.00 98.89  ? 108 GLN   A CG  1 
ATOM   202  C CD  . GLN   A 1 34  ? 23.393  20.719  43.218 1.00 103.15 ? 108 GLN   A CD  1 
ATOM   203  O OE1 . GLN   A 1 34  ? 24.564  20.986  42.945 1.00 107.01 ? 108 GLN   A OE1 1 
ATOM   204  N NE2 . GLN   A 1 34  ? 23.053  19.963  44.255 1.00 103.26 ? 108 GLN   A NE2 1 
ATOM   205  N N   . SER   A 1 35  ? 21.620  21.050  37.715 1.00 83.93  ? 109 SER   A N   1 
ATOM   206  C CA  . SER   A 1 35  ? 22.136  20.942  36.360 1.00 80.24  ? 109 SER   A CA  1 
ATOM   207  C C   . SER   A 1 35  ? 21.203  21.541  35.319 1.00 80.06  ? 109 SER   A C   1 
ATOM   208  O O   . SER   A 1 35  ? 21.504  21.465  34.123 1.00 78.98  ? 109 SER   A O   1 
ATOM   209  C CB  . SER   A 1 35  ? 22.427  19.475  36.022 1.00 77.93  ? 109 SER   A CB  1 
ATOM   210  O OG  . SER   A 1 35  ? 23.578  19.012  36.712 1.00 87.26  ? 109 SER   A OG  1 
ATOM   211  N N   . PHE   A 1 36  ? 20.091  22.147  35.736 1.00 80.59  ? 110 PHE   A N   1 
ATOM   212  C CA  . PHE   A 1 36  ? 19.084  22.628  34.801 1.00 80.19  ? 110 PHE   A CA  1 
ATOM   213  C C   . PHE   A 1 36  ? 18.519  23.959  35.262 1.00 84.10  ? 110 PHE   A C   1 
ATOM   214  O O   . PHE   A 1 36  ? 18.538  24.293  36.451 1.00 88.83  ? 110 PHE   A O   1 
ATOM   215  C CB  . PHE   A 1 36  ? 17.936  21.627  34.639 1.00 77.74  ? 110 PHE   A CB  1 
ATOM   216  C CG  . PHE   A 1 36  ? 18.360  20.322  34.041 1.00 73.74  ? 110 PHE   A CG  1 
ATOM   217  C CD1 . PHE   A 1 36  ? 18.375  20.152  32.666 1.00 66.05  ? 110 PHE   A CD1 1 
ATOM   218  C CD2 . PHE   A 1 36  ? 18.761  19.272  34.852 1.00 71.04  ? 110 PHE   A CD2 1 
ATOM   219  C CE1 . PHE   A 1 36  ? 18.775  18.957  32.109 1.00 69.85  ? 110 PHE   A CE1 1 
ATOM   220  C CE2 . PHE   A 1 36  ? 19.165  18.070  34.304 1.00 69.23  ? 110 PHE   A CE2 1 
ATOM   221  C CZ  . PHE   A 1 36  ? 19.172  17.910  32.930 1.00 68.11  ? 110 PHE   A CZ  1 
ATOM   222  N N   . GLN   A 1 37  ? 18.015  24.714  34.296 1.00 80.27  ? 111 GLN   A N   1 
ATOM   223  C CA  . GLN   A 1 37  ? 17.254  25.931  34.540 1.00 86.36  ? 111 GLN   A CA  1 
ATOM   224  C C   . GLN   A 1 37  ? 15.817  25.641  34.117 1.00 85.20  ? 111 GLN   A C   1 
ATOM   225  O O   . GLN   A 1 37  ? 15.548  25.429  32.930 1.00 84.31  ? 111 GLN   A O   1 
ATOM   226  C CB  . GLN   A 1 37  ? 17.848  27.104  33.762 1.00 89.59  ? 111 GLN   A CB  1 
ATOM   227  C CG  . GLN   A 1 37  ? 17.220  28.458  34.060 1.00 97.93  ? 111 GLN   A CG  1 
ATOM   228  C CD  . GLN   A 1 37  ? 17.553  29.504  33.005 1.00 105.54 ? 111 GLN   A CD  1 
ATOM   229  O OE1 . GLN   A 1 37  ? 18.247  29.220  32.027 1.00 103.63 ? 111 GLN   A OE1 1 
ATOM   230  N NE2 . GLN   A 1 37  ? 17.054  30.720  33.198 1.00 115.22 ? 111 GLN   A NE2 1 
ATOM   231  N N   . ARG   A 1 38  ? 14.905  25.588  35.088 1.00 84.21  ? 112 ARG   A N   1 
ATOM   232  C CA  . ARG   A 1 38  ? 13.491  25.401  34.779 1.00 80.94  ? 112 ARG   A CA  1 
ATOM   233  C C   . ARG   A 1 38  ? 12.966  26.629  34.049 1.00 80.68  ? 112 ARG   A C   1 
ATOM   234  O O   . ARG   A 1 38  ? 13.078  27.749  34.554 1.00 85.06  ? 112 ARG   A O   1 
ATOM   235  C CB  . ARG   A 1 38  ? 12.681  25.167  36.052 1.00 80.75  ? 112 ARG   A CB  1 
ATOM   236  C CG  . ARG   A 1 38  ? 12.951  23.857  36.757 1.00 82.15  ? 112 ARG   A CG  1 
ATOM   237  C CD  . ARG   A 1 38  ? 12.042  23.702  37.970 1.00 85.98  ? 112 ARG   A CD  1 
ATOM   238  N NE  . ARG   A 1 38  ? 12.501  22.650  38.872 1.00 88.93  ? 112 ARG   A NE  1 
ATOM   239  C CZ  . ARG   A 1 38  ? 11.848  22.255  39.957 1.00 89.65  ? 112 ARG   A CZ  1 
ATOM   240  N NH1 . ARG   A 1 38  ? 10.691  22.800  40.303 1.00 90.91  ? 112 ARG   A NH1 1 
ATOM   241  N NH2 . ARG   A 1 38  ? 12.366  21.289  40.713 1.00 89.07  ? 112 ARG   A NH2 1 
ATOM   242  N N   . LEU   A 1 39  ? 12.393  26.428  32.865 1.00 80.06  ? 113 LEU   A N   1 
ATOM   243  C CA  . LEU   A 1 39  ? 11.791  27.531  32.126 1.00 79.22  ? 113 LEU   A CA  1 
ATOM   244  C C   . LEU   A 1 39  ? 10.273  27.564  32.264 1.00 79.57  ? 113 LEU   A C   1 
ATOM   245  O O   . LEU   A 1 39  ? 9.710   28.617  32.570 1.00 83.47  ? 113 LEU   A O   1 
ATOM   246  C CB  . LEU   A 1 39  ? 12.191  27.464  30.646 1.00 76.23  ? 113 LEU   A CB  1 
ATOM   247  C CG  . LEU   A 1 39  ? 13.690  27.622  30.381 1.00 78.28  ? 113 LEU   A CG  1 
ATOM   248  C CD1 . LEU   A 1 39  ? 13.990  27.551  28.895 1.00 75.56  ? 113 LEU   A CD1 1 
ATOM   249  C CD2 . LEU   A 1 39  ? 14.207  28.922  30.975 1.00 81.55  ? 113 LEU   A CD2 1 
ATOM   250  N N   . SER   A 1 40  ? 9.596   26.435  32.058 1.00 75.92  ? 114 SER   A N   1 
ATOM   251  C CA  . SER   A 1 40  ? 8.143   26.408  32.174 1.00 76.24  ? 114 SER   A CA  1 
ATOM   252  C C   . SER   A 1 40  ? 7.681   24.976  32.398 1.00 72.72  ? 114 SER   A C   1 
ATOM   253  O O   . SER   A 1 40  ? 8.356   24.021  32.004 1.00 72.16  ? 114 SER   A O   1 
ATOM   254  C CB  . SER   A 1 40  ? 7.462   26.996  30.930 1.00 75.63  ? 114 SER   A CB  1 
ATOM   255  O OG  . SER   A 1 40  ? 7.628   26.152  29.800 1.00 77.60  ? 114 SER   A OG  1 
ATOM   256  N N   . ARG   A 1 41  ? 6.519   24.844  33.037 1.00 73.99  ? 115 ARG   A N   1 
ATOM   257  C CA  . ARG   A 1 41  ? 5.909   23.543  33.294 1.00 71.16  ? 115 ARG   A CA  1 
ATOM   258  C C   . ARG   A 1 41  ? 5.051   23.177  32.088 1.00 71.49  ? 115 ARG   A C   1 
ATOM   259  O O   . ARG   A 1 41  ? 4.042   23.834  31.814 1.00 69.74  ? 115 ARG   A O   1 
ATOM   260  C CB  . ARG   A 1 41  ? 5.083   23.571  34.581 1.00 74.29  ? 115 ARG   A CB  1 
ATOM   261  C CG  . ARG   A 1 41  ? 4.746   22.185  35.150 1.00 71.97  ? 115 ARG   A CG  1 
ATOM   262  C CD  . ARG   A 1 41  ? 4.096   22.260  36.538 1.00 78.12  ? 115 ARG   A CD  1 
ATOM   263  N NE  . ARG   A 1 41  ? 2.896   23.090  36.547 1.00 83.12  ? 115 ARG   A NE  1 
ATOM   264  C CZ  . ARG   A 1 41  ? 2.808   24.280  37.128 1.00 93.96  ? 115 ARG   A CZ  1 
ATOM   265  N NH1 . ARG   A 1 41  ? 3.820   24.791  37.815 1.00 95.51  ? 115 ARG   A NH1 1 
ATOM   266  N NH2 . ARG   A 1 41  ? 1.679   24.977  37.017 1.00 94.34  ? 115 ARG   A NH2 1 
ATOM   267  N N   . LEU   A 1 42  ? 5.456   22.131  31.362 1.00 68.64  ? 116 LEU   A N   1 
ATOM   268  C CA  . LEU   A 1 42  ? 4.711   21.722  30.175 1.00 63.30  ? 116 LEU   A CA  1 
ATOM   269  C C   . LEU   A 1 42  ? 3.437   20.972  30.540 1.00 65.32  ? 116 LEU   A C   1 
ATOM   270  O O   . LEU   A 1 42  ? 2.401   21.154  29.891 1.00 71.88  ? 116 LEU   A O   1 
ATOM   271  C CB  . LEU   A 1 42  ? 5.585   20.857  29.268 1.00 56.62  ? 116 LEU   A CB  1 
ATOM   272  C CG  . LEU   A 1 42  ? 6.746   21.573  28.585 1.00 58.74  ? 116 LEU   A CG  1 
ATOM   273  C CD1 . LEU   A 1 42  ? 7.604   20.581  27.816 1.00 60.57  ? 116 LEU   A CD1 1 
ATOM   274  C CD2 . LEU   A 1 42  ? 6.218   22.650  27.668 1.00 57.91  ? 116 LEU   A CD2 1 
ATOM   275  N N   . GLY   A 1 43  ? 3.488   20.127  31.565 1.00 66.78  ? 117 GLY   A N   1 
ATOM   276  C CA  . GLY   A 1 43  ? 2.309   19.379  31.958 1.00 65.21  ? 117 GLY   A CA  1 
ATOM   277  C C   . GLY   A 1 43  ? 2.476   18.736  33.314 1.00 69.08  ? 117 GLY   A C   1 
ATOM   278  O O   . GLY   A 1 43  ? 3.594   18.474  33.765 1.00 70.06  ? 117 GLY   A O   1 
ATOM   279  N N   . HIS   A 1 44  ? 1.340   18.490  33.967 1.00 74.57  ? 118 HIS   A N   1 
ATOM   280  C CA  . HIS   A 1 44  ? 1.322   17.750  35.224 1.00 77.40  ? 118 HIS   A CA  1 
ATOM   281  C C   . HIS   A 1 44  ? 0.082   16.869  35.269 1.00 78.46  ? 118 HIS   A C   1 
ATOM   282  O O   . HIS   A 1 44  ? -1.024  17.329  34.967 1.00 85.65  ? 118 HIS   A O   1 
ATOM   283  C CB  . HIS   A 1 44  ? 1.372   18.694  36.439 1.00 76.30  ? 118 HIS   A CB  1 
ATOM   284  C CG  . HIS   A 1 44  ? 0.274   19.712  36.483 1.00 77.42  ? 118 HIS   A CG  1 
ATOM   285  N ND1 . HIS   A 1 44  ? -1.062  19.375  36.442 1.00 80.23  ? 118 HIS   A ND1 1 
ATOM   286  C CD2 . HIS   A 1 44  ? 0.316   21.062  36.601 1.00 84.38  ? 118 HIS   A CD2 1 
ATOM   287  C CE1 . HIS   A 1 44  ? -1.795  20.472  36.515 1.00 83.48  ? 118 HIS   A CE1 1 
ATOM   288  N NE2 . HIS   A 1 44  ? -0.983  21.511  36.613 1.00 78.40  ? 118 HIS   A NE2 1 
ATOM   289  N N   . GLY   A 1 45  ? 0.280   15.608  35.632 1.00 80.15  ? 119 GLY   A N   1 
ATOM   290  C CA  . GLY   A 1 45  ? -0.809  14.679  35.861 1.00 84.22  ? 119 GLY   A CA  1 
ATOM   291  C C   . GLY   A 1 45  ? -0.444  13.703  36.959 1.00 84.99  ? 119 GLY   A C   1 
ATOM   292  O O   . GLY   A 1 45  ? 0.423   13.998  37.785 1.00 85.25  ? 119 GLY   A O   1 
ATOM   293  N N   . SER   A 1 46  ? -1.094  12.537  36.989 1.00 87.24  ? 120 SER   A N   1 
ATOM   294  C CA  . SER   A 1 46  ? -0.690  11.508  37.943 1.00 89.74  ? 120 SER   A CA  1 
ATOM   295  C C   . SER   A 1 46  ? 0.704   10.971  37.630 1.00 89.98  ? 120 SER   A C   1 
ATOM   296  O O   . SER   A 1 46  ? 1.435   10.578  38.548 1.00 87.49  ? 120 SER   A O   1 
ATOM   297  C CB  . SER   A 1 46  ? -1.711  10.368  37.955 1.00 92.67  ? 120 SER   A CB  1 
ATOM   298  O OG  . SER   A 1 46  ? -1.796  9.740   36.684 1.00 93.75  ? 120 SER   A OG  1 
ATOM   299  N N   . TYR   A 1 47  ? 1.083   10.956  36.344 1.00 88.40  ? 121 TYR   A N   1 
ATOM   300  C CA  . TYR   A 1 47  ? 2.408   10.489  35.936 1.00 81.83  ? 121 TYR   A CA  1 
ATOM   301  C C   . TYR   A 1 47  ? 3.519   11.318  36.565 1.00 78.25  ? 121 TYR   A C   1 
ATOM   302  O O   . TYR   A 1 47  ? 4.623   10.810  36.791 1.00 75.88  ? 121 TYR   A O   1 
ATOM   303  C CB  . TYR   A 1 47  ? 2.537   10.530  34.409 1.00 81.98  ? 121 TYR   A CB  1 
ATOM   304  C CG  . TYR   A 1 47  ? 2.237   11.893  33.811 1.00 84.48  ? 121 TYR   A CG  1 
ATOM   305  C CD1 . TYR   A 1 47  ? 3.241   12.841  33.636 1.00 80.28  ? 121 TYR   A CD1 1 
ATOM   306  C CD2 . TYR   A 1 47  ? 0.943   12.235  33.433 1.00 86.96  ? 121 TYR   A CD2 1 
ATOM   307  C CE1 . TYR   A 1 47  ? 2.958   14.092  33.098 1.00 76.05  ? 121 TYR   A CE1 1 
ATOM   308  C CE2 . TYR   A 1 47  ? 0.655   13.478  32.894 1.00 84.74  ? 121 TYR   A CE2 1 
ATOM   309  C CZ  . TYR   A 1 47  ? 1.661   14.402  32.729 1.00 79.43  ? 121 TYR   A CZ  1 
ATOM   310  O OH  . TYR   A 1 47  ? 1.357   15.638  32.196 1.00 77.15  ? 121 TYR   A OH  1 
ATOM   311  N N   . GLY   A 1 48  ? 3.249   12.587  36.847 1.00 78.99  ? 122 GLY   A N   1 
ATOM   312  C CA  . GLY   A 1 48  ? 4.252   13.479  37.382 1.00 73.42  ? 122 GLY   A CA  1 
ATOM   313  C C   . GLY   A 1 48  ? 4.200   14.835  36.715 1.00 72.36  ? 122 GLY   A C   1 
ATOM   314  O O   . GLY   A 1 48  ? 3.115   15.340  36.413 1.00 76.89  ? 122 GLY   A O   1 
ATOM   315  N N   . GLU   A 1 49  ? 5.359   15.436  36.476 1.00 64.98  ? 123 GLU   A N   1 
ATOM   316  C CA  . GLU   A 1 49  ? 5.435   16.734  35.828 1.00 67.64  ? 123 GLU   A CA  1 
ATOM   317  C C   . GLU   A 1 49  ? 6.396   16.666  34.652 1.00 59.41  ? 123 GLU   A C   1 
ATOM   318  O O   . GLU   A 1 49  ? 7.338   15.869  34.646 1.00 59.16  ? 123 GLU   A O   1 
ATOM   319  C CB  . GLU   A 1 49  ? 5.892   17.835  36.799 1.00 70.45  ? 123 GLU   A CB  1 
ATOM   320  C CG  . GLU   A 1 49  ? 4.861   18.239  37.842 1.00 75.84  ? 123 GLU   A CG  1 
ATOM   321  C CD  . GLU   A 1 49  ? 5.116   17.613  39.202 1.00 81.55  ? 123 GLU   A CD  1 
ATOM   322  O OE1 . GLU   A 1 49  ? 5.482   16.417  39.259 1.00 80.66  ? 123 GLU   A OE1 1 
ATOM   323  O OE2 . GLU   A 1 49  ? 4.956   18.327  40.217 1.00 87.02  ? 123 GLU   A OE2 1 
ATOM   324  N N   . VAL   A 1 50  ? 6.153   17.521  33.661 1.00 61.26  ? 124 VAL   A N   1 
ATOM   325  C CA  . VAL   A 1 50  ? 7.036   17.685  32.513 1.00 56.27  ? 124 VAL   A CA  1 
ATOM   326  C C   . VAL   A 1 50  ? 7.413   19.154  32.428 1.00 59.67  ? 124 VAL   A C   1 
ATOM   327  O O   . VAL   A 1 50  ? 6.535   20.015  32.295 1.00 63.01  ? 124 VAL   A O   1 
ATOM   328  C CB  . VAL   A 1 50  ? 6.375   17.220  31.208 1.00 55.98  ? 124 VAL   A CB  1 
ATOM   329  C CG1 . VAL   A 1 50  ? 7.377   17.277  30.073 1.00 55.60  ? 124 VAL   A CG1 1 
ATOM   330  C CG2 . VAL   A 1 50  ? 5.814   15.820  31.362 1.00 53.76  ? 124 VAL   A CG2 1 
ATOM   331  N N   . PHE   A 1 51  ? 8.709   19.443  32.504 1.00 58.94  ? 125 PHE   A N   1 
ATOM   332  C CA  . PHE   A 1 51  ? 9.214   20.808  32.498 1.00 62.03  ? 125 PHE   A CA  1 
ATOM   333  C C   . PHE   A 1 51  ? 9.973   21.089  31.210 1.00 60.22  ? 125 PHE   A C   1 
ATOM   334  O O   . PHE   A 1 51  ? 10.721  20.238  30.722 1.00 58.22  ? 125 PHE   A O   1 
ATOM   335  C CB  . PHE   A 1 51  ? 10.151  21.070  33.685 1.00 65.01  ? 125 PHE   A CB  1 
ATOM   336  C CG  . PHE   A 1 51  ? 9.493   20.936  35.023 1.00 67.42  ? 125 PHE   A CG  1 
ATOM   337  C CD1 . PHE   A 1 51  ? 8.788   21.994  35.570 1.00 71.22  ? 125 PHE   A CD1 1 
ATOM   338  C CD2 . PHE   A 1 51  ? 9.590   19.754  35.740 1.00 66.16  ? 125 PHE   A CD2 1 
ATOM   339  C CE1 . PHE   A 1 51  ? 8.183   21.873  36.801 1.00 73.67  ? 125 PHE   A CE1 1 
ATOM   340  C CE2 . PHE   A 1 51  ? 8.987   19.625  36.972 1.00 68.51  ? 125 PHE   A CE2 1 
ATOM   341  C CZ  . PHE   A 1 51  ? 8.282   20.684  37.504 1.00 74.87  ? 125 PHE   A CZ  1 
ATOM   342  N N   . LYS   A 1 52  ? 9.782   22.287  30.667 1.00 62.06  ? 126 LYS   A N   1 
ATOM   343  C CA  . LYS   A 1 52  ? 10.685  22.804  29.650 1.00 63.99  ? 126 LYS   A CA  1 
ATOM   344  C C   . LYS   A 1 52  ? 11.909  23.366  30.359 1.00 69.90  ? 126 LYS   A C   1 
ATOM   345  O O   . LYS   A 1 52  ? 11.801  24.326  31.130 1.00 74.67  ? 126 LYS   A O   1 
ATOM   346  C CB  . LYS   A 1 52  ? 9.999   23.877  28.806 1.00 69.92  ? 126 LYS   A CB  1 
ATOM   347  C CG  . LYS   A 1 52  ? 10.929  24.616  27.847 1.00 67.58  ? 126 LYS   A CG  1 
ATOM   348  C CD  . LYS   A 1 52  ? 10.180  25.689  27.060 1.00 71.43  ? 126 LYS   A CD  1 
ATOM   349  C CE  . LYS   A 1 52  ? 10.788  27.066  27.282 1.00 75.97  ? 126 LYS   A CE  1 
ATOM   350  N NZ  . LYS   A 1 52  ? 10.063  28.137  26.544 1.00 81.51  ? 126 LYS   A NZ  1 
ATOM   351  N N   . VAL   A 1 53  ? 13.069  22.763  30.127 1.00 71.22  ? 127 VAL   A N   1 
ATOM   352  C CA  . VAL   A 1 53  ? 14.276  23.147  30.844 1.00 71.93  ? 127 VAL   A CA  1 
ATOM   353  C C   . VAL   A 1 53  ? 15.372  23.501  29.850 1.00 71.56  ? 127 VAL   A C   1 
ATOM   354  O O   . VAL   A 1 53  ? 15.384  23.037  28.705 1.00 71.60  ? 127 VAL   A O   1 
ATOM   355  C CB  . VAL   A 1 53  ? 14.759  22.028  31.794 1.00 68.42  ? 127 VAL   A CB  1 
ATOM   356  C CG1 . VAL   A 1 53  ? 13.652  21.621  32.755 1.00 67.86  ? 127 VAL   A CG1 1 
ATOM   357  C CG2 . VAL   A 1 53  ? 15.242  20.836  30.992 1.00 66.08  ? 127 VAL   A CG2 1 
ATOM   358  N N   . ARG   A 1 54  ? 16.292  24.346  30.298 1.00 76.51  ? 128 ARG   A N   1 
ATOM   359  C CA  . ARG   A 1 54  ? 17.558  24.568  29.618 1.00 77.42  ? 128 ARG   A CA  1 
ATOM   360  C C   . ARG   A 1 54  ? 18.650  24.053  30.540 1.00 72.92  ? 128 ARG   A C   1 
ATOM   361  O O   . ARG   A 1 54  ? 18.630  24.327  31.746 1.00 74.73  ? 128 ARG   A O   1 
ATOM   362  C CB  . ARG   A 1 54  ? 17.771  26.051  29.280 1.00 86.82  ? 128 ARG   A CB  1 
ATOM   363  C CG  . ARG   A 1 54  ? 18.812  26.300  28.179 1.00 86.60  ? 128 ARG   A CG  1 
ATOM   364  C CD  . ARG   A 1 54  ? 19.055  27.789  27.888 1.00 92.62  ? 128 ARG   A CD  1 
ATOM   365  N NE  . ARG   A 1 54  ? 18.015  28.407  27.070 1.00 93.13  ? 128 ARG   A NE  1 
ATOM   366  C CZ  . ARG   A 1 54  ? 17.933  28.308  25.748 1.00 88.81  ? 128 ARG   A CZ  1 
ATOM   367  N NH1 . ARG   A 1 54  ? 18.783  27.567  25.055 1.00 86.85  ? 128 ARG   A NH1 1 
ATOM   368  N NH2 . ARG   A 1 54  ? 16.974  28.968  25.105 1.00 82.36  ? 128 ARG   A NH2 1 
ATOM   369  N N   . SER   A 1 55  ? 19.574  23.280  29.988 1.00 73.86  ? 129 SER   A N   1 
ATOM   370  C CA  . SER   A 1 55  ? 20.616  22.685  30.810 1.00 80.64  ? 129 SER   A CA  1 
ATOM   371  C C   . SER   A 1 55  ? 21.612  23.743  31.264 1.00 91.82  ? 129 SER   A C   1 
ATOM   372  O O   . SER   A 1 55  ? 22.049  24.584  30.476 1.00 99.00  ? 129 SER   A O   1 
ATOM   373  C CB  . SER   A 1 55  ? 21.336  21.593  30.028 1.00 85.67  ? 129 SER   A CB  1 
ATOM   374  O OG  . SER   A 1 55  ? 22.572  21.274  30.636 1.00 93.62  ? 129 SER   A OG  1 
ATOM   375  N N   . LYS   A 1 56  ? 21.975  23.701  32.552 1.00 95.35  ? 130 LYS   A N   1 
ATOM   376  C CA  . LYS   A 1 56  ? 23.062  24.557  33.027 1.00 84.21  ? 130 LYS   A CA  1 
ATOM   377  C C   . LYS   A 1 56  ? 24.419  24.088  32.530 1.00 85.13  ? 130 LYS   A C   1 
ATOM   378  O O   . LYS   A 1 56  ? 25.416  24.760  32.791 1.00 96.95  ? 130 LYS   A O   1 
ATOM   379  C CB  . LYS   A 1 56  ? 23.082  24.626  34.557 1.00 77.71  ? 130 LYS   A CB  1 
ATOM   380  C CG  . LYS   A 1 56  ? 21.977  25.469  35.160 1.00 79.48  ? 130 LYS   A CG  1 
ATOM   381  C CD  . LYS   A 1 56  ? 22.031  25.449  36.683 1.00 84.72  ? 130 LYS   A CD  1 
ATOM   382  C CE  . LYS   A 1 56  ? 20.930  26.315  37.296 1.00 91.90  ? 130 LYS   A CE  1 
ATOM   383  N NZ  . LYS   A 1 56  ? 20.962  26.304  38.792 1.00 96.18  ? 130 LYS   A NZ  1 
ATOM   384  N N   . GLU   A 1 57  ? 24.482  22.952  31.835 1.00 105.29 ? 131 GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 57  ? 25.731  22.440  31.279 1.00 107.75 ? 131 GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 57  ? 25.964  22.964  29.864 1.00 108.51 ? 131 GLU   A C   1 
ATOM   387  O O   . GLU   A 1 57  ? 26.921  23.704  29.623 1.00 113.63 ? 131 GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 57  ? 25.724  20.904  31.304 1.00 117.53 ? 131 GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 57  ? 26.883  20.248  30.561 1.00 120.37 ? 131 GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 57  ? 26.540  19.888  29.126 1.00 114.36 ? 131 GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 57  ? 25.491  19.245  28.909 1.00 112.70 ? 131 GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 57  ? 27.314  20.258  28.217 1.00 111.87 ? 131 GLU   A OE2 1 
ATOM   393  N N   . ASP   A 1 58  ? 25.094  22.594  28.920 1.00 100.09 ? 132 ASP   A N   1 
ATOM   394  C CA  . ASP   A 1 58  ? 25.265  23.011  27.534 1.00 102.32 ? 132 ASP   A CA  1 
ATOM   395  C C   . ASP   A 1 58  ? 24.333  24.140  27.117 1.00 100.31 ? 132 ASP   A C   1 
ATOM   396  O O   . ASP   A 1 58  ? 24.589  24.786  26.093 1.00 93.70  ? 132 ASP   A O   1 
ATOM   397  C CB  . ASP   A 1 58  ? 25.071  21.818  26.585 1.00 99.08  ? 132 ASP   A CB  1 
ATOM   398  C CG  . ASP   A 1 58  ? 23.669  21.228  26.645 1.00 97.54  ? 132 ASP   A CG  1 
ATOM   399  O OD1 . ASP   A 1 58  ? 22.789  21.803  27.321 1.00 94.34  ? 132 ASP   A OD1 1 
ATOM   400  O OD2 . ASP   A 1 58  ? 23.449  20.177  26.003 1.00 90.73  ? 132 ASP   A OD2 1 
ATOM   401  N N   . GLY   A 1 59  ? 23.265  24.386  27.871 1.00 99.14  ? 133 GLY   A N   1 
ATOM   402  C CA  . GLY   A 1 59  ? 22.353  25.458  27.531 1.00 97.14  ? 133 GLY   A CA  1 
ATOM   403  C C   . GLY   A 1 59  ? 21.459  25.176  26.351 1.00 96.70  ? 133 GLY   A C   1 
ATOM   404  O O   . GLY   A 1 59  ? 21.019  26.116  25.681 1.00 97.93  ? 133 GLY   A O   1 
ATOM   405  N N   . ARG   A 1 60  ? 21.188  23.906  26.069 1.00 89.43  ? 134 ARG   A N   1 
ATOM   406  C CA  . ARG   A 1 60  ? 20.217  23.534  25.056 1.00 83.00  ? 134 ARG   A CA  1 
ATOM   407  C C   . ARG   A 1 60  ? 18.855  23.312  25.700 1.00 79.58  ? 134 ARG   A C   1 
ATOM   408  O O   . ARG   A 1 60  ? 18.732  23.131  26.915 1.00 78.76  ? 134 ARG   A O   1 
ATOM   409  C CB  . ARG   A 1 60  ? 20.654  22.271  24.307 1.00 86.40  ? 134 ARG   A CB  1 
ATOM   410  C CG  . ARG   A 1 60  ? 21.905  22.443  23.462 1.00 89.74  ? 134 ARG   A CG  1 
ATOM   411  C CD  . ARG   A 1 60  ? 22.142  21.247  22.545 1.00 92.59  ? 134 ARG   A CD  1 
ATOM   412  N NE  . ARG   A 1 60  ? 23.334  21.440  21.727 1.00 107.34 ? 134 ARG   A NE  1 
ATOM   413  C CZ  . ARG   A 1 60  ? 23.340  22.022  20.535 1.00 118.05 ? 134 ARG   A CZ  1 
ATOM   414  N NH1 . ARG   A 1 60  ? 22.219  22.422  19.954 1.00 113.86 ? 134 ARG   A NH1 1 
ATOM   415  N NH2 . ARG   A 1 60  ? 24.502  22.215  19.912 1.00 118.43 ? 134 ARG   A NH2 1 
ATOM   416  N N   . LEU   A 1 61  ? 17.826  23.327  24.864 1.00 79.12  ? 135 LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 61  ? 16.460  23.140  25.324 1.00 74.49  ? 135 LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 61  ? 16.122  21.655  25.334 1.00 66.69  ? 135 LEU   A C   1 
ATOM   419  O O   . LEU   A 1 61  ? 16.257  20.966  24.315 1.00 67.95  ? 135 LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 61  ? 15.495  23.922  24.439 1.00 73.05  ? 135 LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 61  ? 15.739  25.424  24.541 1.00 74.30  ? 135 LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 61  ? 14.865  26.187  23.567 1.00 74.67  ? 135 LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 61  ? 15.479  25.866  25.966 1.00 75.90  ? 135 LEU   A CD2 1 
ATOM   424  N N   . TYR   A 1 62  ? 15.700  21.162  26.490 1.00 63.65  ? 136 TYR   A N   1 
ATOM   425  C CA  . TYR   A 1 62  ? 15.199  19.808  26.618 1.00 67.32  ? 136 TYR   A CA  1 
ATOM   426  C C   . TYR   A 1 62  ? 13.880  19.841  27.374 1.00 64.33  ? 136 TYR   A C   1 
ATOM   427  O O   . TYR   A 1 62  ? 13.469  20.871  27.919 1.00 59.49  ? 136 TYR   A O   1 
ATOM   428  C CB  . TYR   A 1 62  ? 16.203  18.899  27.336 1.00 65.79  ? 136 TYR   A CB  1 
ATOM   429  C CG  . TYR   A 1 62  ? 17.544  18.794  26.652 1.00 70.36  ? 136 TYR   A CG  1 
ATOM   430  C CD1 . TYR   A 1 62  ? 17.759  17.867  25.638 1.00 71.03  ? 136 TYR   A CD1 1 
ATOM   431  C CD2 . TYR   A 1 62  ? 18.602  19.612  27.029 1.00 72.13  ? 136 TYR   A CD2 1 
ATOM   432  C CE1 . TYR   A 1 62  ? 18.992  17.767  25.011 1.00 75.38  ? 136 TYR   A CE1 1 
ATOM   433  C CE2 . TYR   A 1 62  ? 19.837  19.517  26.410 1.00 73.15  ? 136 TYR   A CE2 1 
ATOM   434  C CZ  . TYR   A 1 62  ? 20.027  18.596  25.402 1.00 73.97  ? 136 TYR   A CZ  1 
ATOM   435  O OH  . TYR   A 1 62  ? 21.256  18.502  24.785 1.00 76.13  ? 136 TYR   A OH  1 
ATOM   436  N N   . ALA   A 1 63  ? 13.212  18.692  27.394 1.00 58.67  ? 137 ALA   A N   1 
ATOM   437  C CA  . ALA   A 1 63  ? 12.021  18.485  28.201 1.00 55.25  ? 137 ALA   A CA  1 
ATOM   438  C C   . ALA   A 1 63  ? 12.318  17.381  29.197 1.00 53.57  ? 137 ALA   A C   1 
ATOM   439  O O   . ALA   A 1 63  ? 12.740  16.288  28.806 1.00 58.45  ? 137 ALA   A O   1 
ATOM   440  C CB  . ALA   A 1 63  ? 10.816  18.113  27.336 1.00 54.05  ? 137 ALA   A CB  1 
ATOM   441  N N   . VAL   A 1 64  ? 12.112  17.660  30.478 1.00 52.42  ? 138 VAL   A N   1 
ATOM   442  C CA  . VAL   A 1 64  ? 12.360  16.683  31.531 1.00 53.12  ? 138 VAL   A CA  1 
ATOM   443  C C   . VAL   A 1 64  ? 11.033  16.290  32.162 1.00 53.19  ? 138 VAL   A C   1 
ATOM   444  O O   . VAL   A 1 64  ? 10.219  17.158  32.507 1.00 57.53  ? 138 VAL   A O   1 
ATOM   445  C CB  . VAL   A 1 64  ? 13.335  17.228  32.586 1.00 54.71  ? 138 VAL   A CB  1 
ATOM   446  C CG1 . VAL   A 1 64  ? 13.431  16.265  33.742 1.00 56.27  ? 138 VAL   A CG1 1 
ATOM   447  C CG2 . VAL   A 1 64  ? 14.699  17.452  31.964 1.00 56.87  ? 138 VAL   A CG2 1 
ATOM   448  N N   . LYS   A 1 65  ? 10.814  14.986  32.298 1.00 50.68  ? 139 LYS   A N   1 
ATOM   449  C CA  . LYS   A 1 65  ? 9.651   14.427  32.972 1.00 54.77  ? 139 LYS   A CA  1 
ATOM   450  C C   . LYS   A 1 65  ? 10.101  13.771  34.270 1.00 57.15  ? 139 LYS   A C   1 
ATOM   451  O O   . LYS   A 1 65  ? 11.037  12.965  34.266 1.00 56.93  ? 139 LYS   A O   1 
ATOM   452  C CB  . LYS   A 1 65  ? 8.942   13.399  32.084 1.00 45.27  ? 139 LYS   A CB  1 
ATOM   453  C CG  . LYS   A 1 65  ? 7.685   12.820  32.709 1.00 52.71  ? 139 LYS   A CG  1 
ATOM   454  C CD  . LYS   A 1 65  ? 6.847   12.038  31.705 1.00 55.40  ? 139 LYS   A CD  1 
ATOM   455  C CE  . LYS   A 1 65  ? 7.453   10.680  31.404 1.00 54.00  ? 139 LYS   A CE  1 
ATOM   456  N NZ  . LYS   A 1 65  ? 6.695   9.972   30.329 1.00 62.15  ? 139 LYS   A NZ  1 
ATOM   457  N N   . ARG   A 1 66  ? 9.442   14.110  35.377 1.00 54.78  ? 140 ARG   A N   1 
ATOM   458  C CA  . ARG   A 1 66  ? 9.740   13.493  36.661 1.00 56.98  ? 140 ARG   A CA  1 
ATOM   459  C C   . ARG   A 1 66  ? 8.489   12.819  37.209 1.00 57.83  ? 140 ARG   A C   1 
ATOM   460  O O   . ARG   A 1 66  ? 7.375   13.323  37.037 1.00 63.69  ? 140 ARG   A O   1 
ATOM   461  C CB  . ARG   A 1 66  ? 10.304  14.524  37.662 1.00 59.47  ? 140 ARG   A CB  1 
ATOM   462  C CG  . ARG   A 1 66  ? 9.296   15.180  38.582 1.00 63.04  ? 140 ARG   A CG  1 
ATOM   463  C CD  . ARG   A 1 66  ? 9.960   16.223  39.478 1.00 69.94  ? 140 ARG   A CD  1 
ATOM   464  N NE  . ARG   A 1 66  ? 8.987   17.197  39.964 1.00 81.88  ? 140 ARG   A NE  1 
ATOM   465  C CZ  . ARG   A 1 66  ? 9.294   18.353  40.538 1.00 79.28  ? 140 ARG   A CZ  1 
ATOM   466  N NH1 . ARG   A 1 66  ? 10.552  18.724  40.721 1.00 79.27  ? 140 ARG   A NH1 1 
ATOM   467  N NH2 . ARG   A 1 66  ? 8.314   19.161  40.937 1.00 79.37  ? 140 ARG   A NH2 1 
ATOM   468  N N   . SER   A 1 67  ? 8.674   11.657  37.834 1.00 59.22  ? 141 SER   A N   1 
ATOM   469  C CA  . SER   A 1 67  ? 7.558   10.945  38.436 1.00 63.15  ? 141 SER   A CA  1 
ATOM   470  C C   . SER   A 1 67  ? 7.041   11.709  39.651 1.00 60.86  ? 141 SER   A C   1 
ATOM   471  O O   . SER   A 1 67  ? 7.745   12.524  40.252 1.00 63.36  ? 141 SER   A O   1 
ATOM   472  C CB  . SER   A 1 67  ? 7.971   9.526   38.833 1.00 62.23  ? 141 SER   A CB  1 
ATOM   473  O OG  . SER   A 1 67  ? 9.044   9.531   39.756 1.00 59.26  ? 141 SER   A OG  1 
ATOM   474  N N   . MET   A 1 68  ? 5.787   11.437  40.012 1.00 64.80  ? 142 MET   A N   1 
ATOM   475  C CA  . MET   A 1 68  ? 5.142   12.249  41.040 1.00 71.13  ? 142 MET   A CA  1 
ATOM   476  C C   . MET   A 1 68  ? 5.634   11.885  42.437 1.00 72.11  ? 142 MET   A C   1 
ATOM   477  O O   . MET   A 1 68  ? 6.086   12.756  43.188 1.00 69.56  ? 142 MET   A O   1 
ATOM   478  C CB  . MET   A 1 68  ? 3.620   12.107  40.951 1.00 79.12  ? 142 MET   A CB  1 
ATOM   479  C CG  . MET   A 1 68  ? 2.862   13.135  41.784 1.00 81.20  ? 142 MET   A CG  1 
ATOM   480  S SD  . MET   A 1 68  ? 1.089   12.820  41.859 1.00 108.32 ? 142 MET   A SD  1 
ATOM   481  C CE  . MET   A 1 68  ? 0.560   14.115  42.989 1.00 81.85  ? 142 MET   A CE  1 
ATOM   482  N N   . SER   A 1 69  ? 5.564   10.610  42.799 1.00 74.21  ? 143 SER   A N   1 
ATOM   483  C CA  . SER   A 1 69  ? 5.848   10.139  44.144 1.00 71.47  ? 143 SER   A CA  1 
ATOM   484  C C   . SER   A 1 69  ? 7.041   9.187   44.147 1.00 72.05  ? 143 SER   A C   1 
ATOM   485  O O   . SER   A 1 69  ? 7.387   8.604   43.111 1.00 70.17  ? 143 SER   A O   1 
ATOM   486  C CB  . SER   A 1 69  ? 4.612   9.436   44.725 1.00 73.52  ? 143 SER   A CB  1 
ATOM   487  O OG  . SER   A 1 69  ? 4.041   8.553   43.772 1.00 82.53  ? 143 SER   A OG  1 
ATOM   488  N N   . PRO   A 1 70  ? 7.703   9.015   45.296 1.00 71.82  ? 144 PRO   A N   1 
ATOM   489  C CA  . PRO   A 1 70  ? 8.814   8.058   45.370 1.00 66.42  ? 144 PRO   A CA  1 
ATOM   490  C C   . PRO   A 1 70  ? 8.344   6.646   45.058 1.00 66.47  ? 144 PRO   A C   1 
ATOM   491  O O   . PRO   A 1 70  ? 7.159   6.321   45.153 1.00 69.84  ? 144 PRO   A O   1 
ATOM   492  C CB  . PRO   A 1 70  ? 9.295   8.174   46.822 1.00 67.22  ? 144 PRO   A CB  1 
ATOM   493  C CG  . PRO   A 1 70  ? 8.799   9.504   47.291 1.00 63.52  ? 144 PRO   A CG  1 
ATOM   494  C CD  . PRO   A 1 70  ? 7.508   9.734   46.568 1.00 67.00  ? 144 PRO   A CD  1 
ATOM   495  N N   . PHE   A 1 71  ? 9.300   5.804   44.670 1.00 67.10  ? 145 PHE   A N   1 
ATOM   496  C CA  . PHE   A 1 71  ? 8.990   4.429   44.297 1.00 63.71  ? 145 PHE   A CA  1 
ATOM   497  C C   . PHE   A 1 71  ? 8.277   3.710   45.431 1.00 62.39  ? 145 PHE   A C   1 
ATOM   498  O O   . PHE   A 1 71  ? 8.764   3.678   46.565 1.00 62.52  ? 145 PHE   A O   1 
ATOM   499  C CB  . PHE   A 1 71  ? 10.270  3.686   43.925 1.00 59.01  ? 145 PHE   A CB  1 
ATOM   500  C CG  . PHE   A 1 71  ? 10.883  4.154   42.643 1.00 57.96  ? 145 PHE   A CG  1 
ATOM   501  C CD1 . PHE   A 1 71  ? 10.090  4.397   41.531 1.00 57.72  ? 145 PHE   A CD1 1 
ATOM   502  C CD2 . PHE   A 1 71  ? 12.246  4.365   42.550 1.00 55.56  ? 145 PHE   A CD2 1 
ATOM   503  C CE1 . PHE   A 1 71  ? 10.646  4.833   40.346 1.00 52.60  ? 145 PHE   A CE1 1 
ATOM   504  C CE2 . PHE   A 1 71  ? 12.810  4.804   41.366 1.00 58.27  ? 145 PHE   A CE2 1 
ATOM   505  C CZ  . PHE   A 1 71  ? 12.007  5.040   40.262 1.00 55.72  ? 145 PHE   A CZ  1 
ATOM   506  N N   . ARG   A 1 72  ? 7.109   3.142   45.120 1.00 63.39  ? 146 ARG   A N   1 
ATOM   507  C CA  . ARG   A 1 72  ? 6.323   2.451   46.136 1.00 66.32  ? 146 ARG   A CA  1 
ATOM   508  C C   . ARG   A 1 72  ? 6.906   1.084   46.460 1.00 63.64  ? 146 ARG   A C   1 
ATOM   509  O O   . ARG   A 1 72  ? 6.762   0.608   47.590 1.00 62.61  ? 146 ARG   A O   1 
ATOM   510  C CB  . ARG   A 1 72  ? 4.863   2.313   45.683 1.00 70.23  ? 146 ARG   A CB  1 
ATOM   511  C CG  . ARG   A 1 72  ? 4.061   3.623   45.702 1.00 81.60  ? 146 ARG   A CG  1 
ATOM   512  C CD  . ARG   A 1 72  ? 2.584   3.406   45.342 1.00 98.17  ? 146 ARG   A CD  1 
ATOM   513  N NE  . ARG   A 1 72  ? 2.365   3.279   43.904 1.00 101.46 ? 146 ARG   A NE  1 
ATOM   514  C CZ  . ARG   A 1 72  ? 1.695   4.151   43.162 1.00 105.12 ? 146 ARG   A CZ  1 
ATOM   515  N NH1 . ARG   A 1 72  ? 1.124   5.221   43.695 1.00 102.77 ? 146 ARG   A NH1 1 
ATOM   516  N NH2 . ARG   A 1 72  ? 1.589   3.941   41.851 1.00 106.79 ? 146 ARG   A NH2 1 
ATOM   517  N N   . GLY   A 1 73  ? 7.570   0.450   45.497 1.00 58.16  ? 147 GLY   A N   1 
ATOM   518  C CA  . GLY   A 1 73  ? 8.135   -0.862  45.692 1.00 56.19  ? 147 GLY   A CA  1 
ATOM   519  C C   . GLY   A 1 73  ? 8.951   -1.301  44.493 1.00 59.51  ? 147 GLY   A C   1 
ATOM   520  O O   . GLY   A 1 73  ? 9.169   -0.533  43.549 1.00 57.96  ? 147 GLY   A O   1 
ATOM   521  N N   . PRO   A 1 74  ? 9.428   -2.550  44.512 1.00 53.91  ? 148 PRO   A N   1 
ATOM   522  C CA  . PRO   A 1 74  ? 10.197  -3.048  43.357 1.00 55.01  ? 148 PRO   A CA  1 
ATOM   523  C C   . PRO   A 1 74  ? 9.411   -3.038  42.054 1.00 55.45  ? 148 PRO   A C   1 
ATOM   524  O O   . PRO   A 1 74  ? 9.903   -2.526  41.038 1.00 52.93  ? 148 PRO   A O   1 
ATOM   525  C CB  . PRO   A 1 74  ? 10.580  -4.471  43.792 1.00 51.22  ? 148 PRO   A CB  1 
ATOM   526  C CG  . PRO   A 1 74  ? 10.581  -4.420  45.270 1.00 49.46  ? 148 PRO   A CG  1 
ATOM   527  C CD  . PRO   A 1 74  ? 9.462   -3.489  45.643 1.00 50.63  ? 148 PRO   A CD  1 
ATOM   528  N N   . LYS   A 1 75  ? 8.196   -3.595  42.053 1.00 56.40  ? 149 LYS   A N   1 
ATOM   529  C CA  . LYS   A 1 75  ? 7.403   -3.633  40.828 1.00 56.45  ? 149 LYS   A CA  1 
ATOM   530  C C   . LYS   A 1 75  ? 7.099   -2.227  40.324 1.00 56.65  ? 149 LYS   A C   1 
ATOM   531  O O   . LYS   A 1 75  ? 7.173   -1.964  39.117 1.00 57.55  ? 149 LYS   A O   1 
ATOM   532  C CB  . LYS   A 1 75  ? 6.106   -4.409  41.061 1.00 59.45  ? 149 LYS   A CB  1 
ATOM   533  C CG  . LYS   A 1 75  ? 6.287   -5.801  41.670 1.00 67.55  ? 149 LYS   A CG  1 
ATOM   534  C CD  . LYS   A 1 75  ? 6.785   -6.829  40.658 1.00 71.80  ? 149 LYS   A CD  1 
ATOM   535  C CE  . LYS   A 1 75  ? 6.871   -8.220  41.289 1.00 69.81  ? 149 LYS   A CE  1 
ATOM   536  N NZ  . LYS   A 1 75  ? 7.379   -9.250  40.337 1.00 73.97  ? 149 LYS   A NZ  1 
ATOM   537  N N   . ASP   A 1 76  ? 6.757   -1.307  41.233 1.00 58.40  ? 150 ASP   A N   1 
ATOM   538  C CA  . ASP   A 1 76  ? 6.501   0.071   40.821 1.00 54.48  ? 150 ASP   A CA  1 
ATOM   539  C C   . ASP   A 1 76  ? 7.743   0.699   40.205 1.00 54.22  ? 150 ASP   A C   1 
ATOM   540  O O   . ASP   A 1 76  ? 7.651   1.419   39.204 1.00 57.22  ? 150 ASP   A O   1 
ATOM   541  C CB  . ASP   A 1 76  ? 6.018   0.908   42.002 1.00 57.73  ? 150 ASP   A CB  1 
ATOM   542  C CG  . ASP   A 1 76  ? 5.765   2.354   41.618 1.00 67.14  ? 150 ASP   A CG  1 
ATOM   543  O OD1 . ASP   A 1 76  ? 5.079   2.586   40.596 1.00 74.52  ? 150 ASP   A OD1 1 
ATOM   544  O OD2 . ASP   A 1 76  ? 6.246   3.258   42.334 1.00 67.39  ? 150 ASP   A OD2 1 
ATOM   545  N N   . ARG   A 1 77  ? 8.914   0.434   40.787 1.00 52.23  ? 151 ARG   A N   1 
ATOM   546  C CA  . ARG   A 1 77  ? 10.157  0.917   40.194 1.00 52.01  ? 151 ARG   A CA  1 
ATOM   547  C C   . ARG   A 1 77  ? 10.384  0.302   38.817 1.00 48.93  ? 151 ARG   A C   1 
ATOM   548  O O   . ARG   A 1 77  ? 10.656  1.016   37.843 1.00 46.96  ? 151 ARG   A O   1 
ATOM   549  C CB  . ARG   A 1 77  ? 11.330  0.615   41.127 1.00 49.65  ? 151 ARG   A CB  1 
ATOM   550  C CG  . ARG   A 1 77  ? 12.671  1.087   40.603 1.00 47.22  ? 151 ARG   A CG  1 
ATOM   551  C CD  . ARG   A 1 77  ? 13.773  0.863   41.621 1.00 51.88  ? 151 ARG   A CD  1 
ATOM   552  N NE  . ARG   A 1 77  ? 15.086  1.204   41.087 1.00 55.96  ? 151 ARG   A NE  1 
ATOM   553  C CZ  . ARG   A 1 77  ? 15.913  0.332   40.527 1.00 61.43  ? 151 ARG   A CZ  1 
ATOM   554  N NH1 . ARG   A 1 77  ? 15.598  -0.949  40.424 1.00 62.46  ? 151 ARG   A NH1 1 
ATOM   555  N NH2 . ARG   A 1 77  ? 17.084  0.754   40.061 1.00 64.48  ? 151 ARG   A NH2 1 
ATOM   556  N N   . ALA   A 1 78  ? 10.257  -1.025  38.711 1.00 49.92  ? 152 ALA   A N   1 
ATOM   557  C CA  . ALA   A 1 78  ? 10.479  -1.694  37.430 1.00 47.53  ? 152 ALA   A CA  1 
ATOM   558  C C   . ALA   A 1 78  ? 9.502   -1.206  36.368 1.00 49.20  ? 152 ALA   A C   1 
ATOM   559  O O   . ALA   A 1 78  ? 9.871   -1.053  35.197 1.00 47.26  ? 152 ALA   A O   1 
ATOM   560  C CB  . ALA   A 1 78  ? 10.362  -3.208  37.600 1.00 42.67  ? 152 ALA   A CB  1 
ATOM   561  N N   . ARG   A 1 79  ? 8.249   -0.963  36.755 1.00 51.36  ? 153 ARG   A N   1 
ATOM   562  C CA  . ARG   A 1 79  ? 7.268   -0.473  35.796 1.00 46.58  ? 153 ARG   A CA  1 
ATOM   563  C C   . ARG   A 1 79  ? 7.657   0.900   35.271 1.00 51.55  ? 153 ARG   A C   1 
ATOM   564  O O   . ARG   A 1 79  ? 7.523   1.178   34.073 1.00 51.37  ? 153 ARG   A O   1 
ATOM   565  C CB  . ARG   A 1 79  ? 5.887   -0.429  36.444 1.00 54.53  ? 153 ARG   A CB  1 
ATOM   566  C CG  . ARG   A 1 79  ? 4.730   -0.333  35.469 1.00 63.51  ? 153 ARG   A CG  1 
ATOM   567  C CD  . ARG   A 1 79  ? 3.407   -0.220  36.218 1.00 75.36  ? 153 ARG   A CD  1 
ATOM   568  N NE  . ARG   A 1 79  ? 3.419   -0.957  37.480 1.00 82.20  ? 153 ARG   A NE  1 
ATOM   569  C CZ  . ARG   A 1 79  ? 2.976   -2.199  37.636 1.00 81.53  ? 153 ARG   A CZ  1 
ATOM   570  N NH1 . ARG   A 1 79  ? 2.480   -2.890  36.620 1.00 77.98  ? 153 ARG   A NH1 1 
ATOM   571  N NH2 . ARG   A 1 79  ? 3.028   -2.759  38.843 1.00 72.99  ? 153 ARG   A NH2 1 
ATOM   572  N N   . LYS   A 1 80  ? 8.159   1.769   36.150 1.00 51.36  ? 154 LYS   A N   1 
ATOM   573  C CA  . LYS   A 1 80  ? 8.525   3.116   35.724 1.00 46.38  ? 154 LYS   A CA  1 
ATOM   574  C C   . LYS   A 1 80  ? 9.802   3.113   34.893 1.00 46.03  ? 154 LYS   A C   1 
ATOM   575  O O   . LYS   A 1 80  ? 9.886   3.823   33.889 1.00 51.35  ? 154 LYS   A O   1 
ATOM   576  C CB  . LYS   A 1 80  ? 8.661   4.038   36.937 1.00 41.88  ? 154 LYS   A CB  1 
ATOM   577  C CG  . LYS   A 1 80  ? 7.326   4.342   37.605 1.00 49.06  ? 154 LYS   A CG  1 
ATOM   578  C CD  . LYS   A 1 80  ? 7.474   5.227   38.831 1.00 53.48  ? 154 LYS   A CD  1 
ATOM   579  C CE  . LYS   A 1 80  ? 6.111   5.536   39.442 1.00 58.24  ? 154 LYS   A CE  1 
ATOM   580  N NZ  . LYS   A 1 80  ? 6.219   6.258   40.749 1.00 68.69  ? 154 LYS   A NZ  1 
ATOM   581  N N   . LEU   A 1 81  ? 10.806  2.322   35.280 1.00 45.29  ? 155 LEU   A N   1 
ATOM   582  C CA  . LEU   A 1 81  ? 12.051  2.320   34.515 1.00 46.36  ? 155 LEU   A CA  1 
ATOM   583  C C   . LEU   A 1 81  ? 11.893  1.664   33.147 1.00 50.45  ? 155 LEU   A C   1 
ATOM   584  O O   . LEU   A 1 81  ? 12.744  1.871   32.275 1.00 50.52  ? 155 LEU   A O   1 
ATOM   585  C CB  . LEU   A 1 81  ? 13.164  1.613   35.292 1.00 47.35  ? 155 LEU   A CB  1 
ATOM   586  C CG  . LEU   A 1 81  ? 13.520  2.057   36.715 1.00 49.57  ? 155 LEU   A CG  1 
ATOM   587  C CD1 . LEU   A 1 81  ? 14.693  1.240   37.229 1.00 55.71  ? 155 LEU   A CD1 1 
ATOM   588  C CD2 . LEU   A 1 81  ? 13.843  3.528   36.797 1.00 47.03  ? 155 LEU   A CD2 1 
ATOM   589  N N   . ALA   A 1 82  ? 10.828  0.885   32.939 1.00 48.83  ? 156 ALA   A N   1 
ATOM   590  C CA  . ALA   A 1 82  ? 10.637  0.213   31.659 1.00 43.76  ? 156 ALA   A CA  1 
ATOM   591  C C   . ALA   A 1 82  ? 10.462  1.204   30.516 1.00 46.79  ? 156 ALA   A C   1 
ATOM   592  O O   . ALA   A 1 82  ? 10.790  0.881   29.366 1.00 49.06  ? 156 ALA   A O   1 
ATOM   593  C CB  . ALA   A 1 82  ? 9.431   -0.723  31.729 1.00 45.94  ? 156 ALA   A CB  1 
ATOM   594  N N   . GLU   A 1 83  ? 9.931   2.400   30.799 1.00 45.82  ? 157 GLU   A N   1 
ATOM   595  C CA  . GLU   A 1 83  ? 9.813   3.413   29.755 1.00 42.81  ? 157 GLU   A CA  1 
ATOM   596  C C   . GLU   A 1 83  ? 11.179  3.762   29.189 1.00 49.27  ? 157 GLU   A C   1 
ATOM   597  O O   . GLU   A 1 83  ? 11.317  4.020   27.987 1.00 49.26  ? 157 GLU   A O   1 
ATOM   598  C CB  . GLU   A 1 83  ? 9.128   4.669   30.293 1.00 42.32  ? 157 GLU   A CB  1 
ATOM   599  C CG  . GLU   A 1 83  ? 8.867   5.723   29.217 1.00 47.96  ? 157 GLU   A CG  1 
ATOM   600  C CD  . GLU   A 1 83  ? 8.080   6.926   29.727 1.00 54.81  ? 157 GLU   A CD  1 
ATOM   601  O OE1 . GLU   A 1 83  ? 7.795   6.970   30.945 1.00 56.24  ? 157 GLU   A OE1 1 
ATOM   602  O OE2 . GLU   A 1 83  ? 7.746   7.825   28.909 1.00 50.96  ? 157 GLU   A OE2 1 
ATOM   603  N N   . VAL   A 1 84  ? 12.204  3.766   30.043 1.00 44.29  ? 158 VAL   A N   1 
ATOM   604  C CA  . VAL   A 1 84  ? 13.555  4.038   29.571 1.00 47.99  ? 158 VAL   A CA  1 
ATOM   605  C C   . VAL   A 1 84  ? 14.032  2.912   28.667 1.00 55.11  ? 158 VAL   A C   1 
ATOM   606  O O   . VAL   A 1 84  ? 14.608  3.156   27.599 1.00 56.99  ? 158 VAL   A O   1 
ATOM   607  C CB  . VAL   A 1 84  ? 14.502  4.255   30.764 1.00 48.26  ? 158 VAL   A CB  1 
ATOM   608  C CG1 . VAL   A 1 84  ? 15.927  4.424   30.277 1.00 51.47  ? 158 VAL   A CG1 1 
ATOM   609  C CG2 . VAL   A 1 84  ? 14.065  5.470   31.568 1.00 46.04  ? 158 VAL   A CG2 1 
ATOM   610  N N   . GLY   A 1 85  ? 13.799  1.662   29.074 1.00 53.80  ? 159 GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 85  ? 14.113  0.544   28.204 1.00 51.21  ? 159 GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 85  ? 13.381  0.622   26.880 1.00 48.21  ? 159 GLY   A C   1 
ATOM   613  O O   . GLY   A 1 85  ? 13.954  0.333   25.828 1.00 52.22  ? 159 GLY   A O   1 
ATOM   614  N N   . SER   A 1 86  ? 12.112  1.039   26.913 1.00 47.32  ? 160 SER   A N   1 
ATOM   615  C CA  . SER   A 1 86  ? 11.341  1.181   25.683 1.00 48.27  ? 160 SER   A CA  1 
ATOM   616  C C   . SER   A 1 86  ? 11.935  2.245   24.762 1.00 50.52  ? 160 SER   A C   1 
ATOM   617  O O   . SER   A 1 86  ? 12.002  2.044   23.544 1.00 53.50  ? 160 SER   A O   1 
ATOM   618  C CB  . SER   A 1 86  ? 9.884   1.502   26.015 1.00 49.10  ? 160 SER   A CB  1 
ATOM   619  O OG  . SER   A 1 86  ? 9.258   0.408   26.672 1.00 48.72  ? 160 SER   A OG  1 
ATOM   620  N N   . HIS   A 1 87  ? 12.369  3.386   25.314 1.00 50.87  ? 161 HIS   A N   1 
ATOM   621  C CA  . HIS   A 1 87  ? 12.999  4.411   24.478 1.00 50.58  ? 161 HIS   A CA  1 
ATOM   622  C C   . HIS   A 1 87  ? 14.262  3.891   23.809 1.00 57.27  ? 161 HIS   A C   1 
ATOM   623  O O   . HIS   A 1 87  ? 14.588  4.298   22.685 1.00 58.31  ? 161 HIS   A O   1 
ATOM   624  C CB  . HIS   A 1 87  ? 13.353  5.650   25.298 1.00 52.23  ? 161 HIS   A CB  1 
ATOM   625  C CG  . HIS   A 1 87  ? 12.269  6.676   25.358 1.00 48.22  ? 161 HIS   A CG  1 
ATOM   626  N ND1 . HIS   A 1 87  ? 11.179  6.551   26.191 1.00 59.09  ? 161 HIS   A ND1 1 
ATOM   627  C CD2 . HIS   A 1 87  ? 12.113  7.853   24.706 1.00 42.18  ? 161 HIS   A CD2 1 
ATOM   628  C CE1 . HIS   A 1 87  ? 10.392  7.602   26.046 1.00 57.12  ? 161 HIS   A CE1 1 
ATOM   629  N NE2 . HIS   A 1 87  ? 10.939  8.409   25.153 1.00 55.71  ? 161 HIS   A NE2 1 
ATOM   630  N N   . GLU   A 1 88  ? 14.997  3.012   24.489 1.00 54.43  ? 162 GLU   A N   1 
ATOM   631  C CA  . GLU   A 1 88  ? 16.244  2.516   23.922 1.00 56.06  ? 162 GLU   A CA  1 
ATOM   632  C C   . GLU   A 1 88  ? 15.984  1.525   22.792 1.00 56.10  ? 162 GLU   A C   1 
ATOM   633  O O   . GLU   A 1 88  ? 16.659  1.572   21.757 1.00 63.67  ? 162 GLU   A O   1 
ATOM   634  C CB  . GLU   A 1 88  ? 17.102  1.892   25.022 1.00 63.06  ? 162 GLU   A CB  1 
ATOM   635  C CG  . GLU   A 1 88  ? 17.499  2.885   26.109 1.00 67.62  ? 162 GLU   A CG  1 
ATOM   636  C CD  . GLU   A 1 88  ? 18.482  2.303   27.106 1.00 76.50  ? 162 GLU   A CD  1 
ATOM   637  O OE1 . GLU   A 1 88  ? 18.553  1.058   27.190 1.00 78.85  ? 162 GLU   A OE1 1 
ATOM   638  O OE2 . GLU   A 1 88  ? 19.183  3.089   27.791 1.00 73.37  ? 162 GLU   A OE2 1 
ATOM   639  N N   . LYS   A 1 89  ? 15.005  0.630   22.961 1.00 57.53  ? 163 LYS   A N   1 
ATOM   640  C CA  . LYS   A 1 89  ? 14.681  -0.315  21.891 1.00 53.05  ? 163 LYS   A CA  1 
ATOM   641  C C   . LYS   A 1 89  ? 14.214  0.404   20.635 1.00 50.85  ? 163 LYS   A C   1 
ATOM   642  O O   . LYS   A 1 89  ? 14.413  -0.096  19.523 1.00 57.99  ? 163 LYS   A O   1 
ATOM   643  C CB  . LYS   A 1 89  ? 13.615  -1.304  22.358 1.00 51.72  ? 163 LYS   A CB  1 
ATOM   644  C CG  . LYS   A 1 89  ? 14.047  -2.175  23.522 1.00 54.64  ? 163 LYS   A CG  1 
ATOM   645  C CD  . LYS   A 1 89  ? 12.885  -3.002  24.044 1.00 59.40  ? 163 LYS   A CD  1 
ATOM   646  C CE  . LYS   A 1 89  ? 13.291  -3.807  25.266 1.00 66.87  ? 163 LYS   A CE  1 
ATOM   647  N NZ  . LYS   A 1 89  ? 12.117  -4.480  25.891 1.00 72.33  ? 163 LYS   A NZ  1 
ATOM   648  N N   . VAL   A 1 90  ? 13.594  1.574   20.788 1.00 59.43  ? 164 VAL   A N   1 
ATOM   649  C CA  . VAL   A 1 90  ? 13.170  2.345   19.626 1.00 59.33  ? 164 VAL   A CA  1 
ATOM   650  C C   . VAL   A 1 90  ? 14.370  2.992   18.957 1.00 61.79  ? 164 VAL   A C   1 
ATOM   651  O O   . VAL   A 1 90  ? 14.481  3.010   17.725 1.00 68.32  ? 164 VAL   A O   1 
ATOM   652  C CB  . VAL   A 1 90  ? 12.116  3.385   20.040 1.00 53.90  ? 164 VAL   A CB  1 
ATOM   653  C CG1 . VAL   A 1 90  ? 11.813  4.325   18.886 1.00 54.08  ? 164 VAL   A CG1 1 
ATOM   654  C CG2 . VAL   A 1 90  ? 10.853  2.680   20.506 1.00 48.82  ? 164 VAL   A CG2 1 
ATOM   655  N N   . GLY   A 1 91  ? 15.292  3.520   19.751 1.00 62.43  ? 165 GLY   A N   1 
ATOM   656  C CA  . GLY   A 1 91  ? 16.500  4.060   19.172 1.00 66.22  ? 165 GLY   A CA  1 
ATOM   657  C C   . GLY   A 1 91  ? 16.251  5.355   18.417 1.00 72.72  ? 165 GLY   A C   1 
ATOM   658  O O   . GLY   A 1 91  ? 15.280  6.086   18.649 1.00 72.34  ? 165 GLY   A O   1 
ATOM   659  N N   . GLN   A 1 92  ? 17.155  5.621   17.483 1.00 81.60  ? 166 GLN   A N   1 
ATOM   660  C CA  . GLN   A 1 92  ? 17.193  6.889   16.772 1.00 81.44  ? 166 GLN   A CA  1 
ATOM   661  C C   . GLN   A 1 92  ? 16.316  6.817   15.529 1.00 80.59  ? 166 GLN   A C   1 
ATOM   662  O O   . GLN   A 1 92  ? 16.537  5.969   14.657 1.00 79.00  ? 166 GLN   A O   1 
ATOM   663  C CB  . GLN   A 1 92  ? 18.632  7.233   16.392 1.00 85.20  ? 166 GLN   A CB  1 
ATOM   664  C CG  . GLN   A 1 92  ? 18.935  8.703   16.505 1.00 88.75  ? 166 GLN   A CG  1 
ATOM   665  C CD  . GLN   A 1 92  ? 18.434  9.271   17.813 1.00 89.85  ? 166 GLN   A CD  1 
ATOM   666  O OE1 . GLN   A 1 92  ? 17.494  10.066  17.835 1.00 89.14  ? 166 GLN   A OE1 1 
ATOM   667  N NE2 . GLN   A 1 92  ? 19.051  8.854   18.916 1.00 88.95  ? 166 GLN   A NE2 1 
ATOM   668  N N   . HIS   A 1 93  ? 15.330  7.715   15.449 1.00 69.77  ? 167 HIS   A N   1 
ATOM   669  C CA  . HIS   A 1 93  ? 14.497  7.863   14.269 1.00 62.96  ? 167 HIS   A CA  1 
ATOM   670  C C   . HIS   A 1 93  ? 13.975  9.292   14.213 1.00 59.99  ? 167 HIS   A C   1 
ATOM   671  O O   . HIS   A 1 93  ? 13.641  9.863   15.263 1.00 59.56  ? 167 HIS   A O   1 
ATOM   672  C CB  . HIS   A 1 93  ? 13.324  6.881   14.267 1.00 65.40  ? 167 HIS   A CB  1 
ATOM   673  C CG  . HIS   A 1 93  ? 12.619  6.789   12.950 1.00 59.84  ? 167 HIS   A CG  1 
ATOM   674  N ND1 . HIS   A 1 93  ? 11.433  7.443   12.693 1.00 59.11  ? 167 HIS   A ND1 1 
ATOM   675  C CD2 . HIS   A 1 93  ? 12.936  6.122   11.815 1.00 56.71  ? 167 HIS   A CD2 1 
ATOM   676  C CE1 . HIS   A 1 93  ? 11.047  7.179   11.458 1.00 58.74  ? 167 HIS   A CE1 1 
ATOM   677  N NE2 . HIS   A 1 93  ? 11.941  6.380   10.903 1.00 57.07  ? 167 HIS   A NE2 1 
ATOM   678  N N   . PRO   A 1 94  ? 13.898  9.891   13.022 1.00 57.19  ? 168 PRO   A N   1 
ATOM   679  C CA  . PRO   A 1 94  ? 13.462  11.294  12.938 1.00 55.83  ? 168 PRO   A CA  1 
ATOM   680  C C   . PRO   A 1 94  ? 12.058  11.532  13.451 1.00 59.90  ? 168 PRO   A C   1 
ATOM   681  O O   . PRO   A 1 94  ? 11.770  12.630  13.946 1.00 64.60  ? 168 PRO   A O   1 
ATOM   682  C CB  . PRO   A 1 94  ? 13.570  11.601  11.438 1.00 57.53  ? 168 PRO   A CB  1 
ATOM   683  C CG  . PRO   A 1 94  ? 14.601  10.639  10.931 1.00 58.38  ? 168 PRO   A CG  1 
ATOM   684  C CD  . PRO   A 1 94  ? 14.397  9.385   11.731 1.00 60.77  ? 168 PRO   A CD  1 
ATOM   685  N N   . CYS   A 1 95  ? 11.170  10.544  13.355 1.00 57.46  ? 169 CYS   A N   1 
ATOM   686  C CA  . CYS   A 1 95  ? 9.783   10.712  13.765 1.00 50.77  ? 169 CYS   A CA  1 
ATOM   687  C C   . CYS   A 1 95  ? 9.513   10.147  15.150 1.00 54.45  ? 169 CYS   A C   1 
ATOM   688  O O   . CYS   A 1 95  ? 8.349   9.912   15.500 1.00 52.93  ? 169 CYS   A O   1 
ATOM   689  C CB  . CYS   A 1 95  ? 8.846   10.071  12.742 1.00 53.02  ? 169 CYS   A CB  1 
ATOM   690  S SG  . CYS   A 1 95  ? 9.111   10.678  11.061 1.00 62.71  ? 169 CYS   A SG  1 
ATOM   691  N N   . CYS   A 1 96  ? 10.554  9.929   15.947 1.00 55.17  ? 170 CYS   A N   1 
ATOM   692  C CA  . CYS   A 1 96  ? 10.398  9.465   17.319 1.00 52.01  ? 170 CYS   A CA  1 
ATOM   693  C C   . CYS   A 1 96  ? 11.092  10.432  18.263 1.00 52.00  ? 170 CYS   A C   1 
ATOM   694  O O   . CYS   A 1 96  ? 12.214  10.874  17.995 1.00 58.04  ? 170 CYS   A O   1 
ATOM   695  C CB  . CYS   A 1 96  ? 10.972  8.056   17.499 1.00 58.21  ? 170 CYS   A CB  1 
ATOM   696  S SG  . CYS   A 1 96  ? 10.084  6.764   16.587 1.00 59.98  ? 170 CYS   A SG  1 
ATOM   697  N N   . VAL   A 1 97  ? 10.412  10.764  19.361 1.00 50.32  ? 171 VAL   A N   1 
ATOM   698  C CA  . VAL   A 1 97  ? 11.008  11.615  20.386 1.00 52.37  ? 171 VAL   A CA  1 
ATOM   699  C C   . VAL   A 1 97  ? 12.243  10.927  20.947 1.00 51.83  ? 171 VAL   A C   1 
ATOM   700  O O   . VAL   A 1 97  ? 12.147  9.858   21.563 1.00 53.32  ? 171 VAL   A O   1 
ATOM   701  C CB  . VAL   A 1 97  ? 9.994   11.917  21.491 1.00 49.67  ? 171 VAL   A CB  1 
ATOM   702  C CG1 . VAL   A 1 97  ? 10.645  12.754  22.578 1.00 53.73  ? 171 VAL   A CG1 1 
ATOM   703  C CG2 . VAL   A 1 97  ? 8.784   12.624  20.923 1.00 46.07  ? 171 VAL   A CG2 1 
ATOM   704  N N   . ARG   A 1 98  ? 13.408  11.545  20.751 1.00 54.91  ? 172 ARG   A N   1 
ATOM   705  C CA  . ARG   A 1 98  ? 14.668  10.960  21.192 1.00 57.90  ? 172 ARG   A CA  1 
ATOM   706  C C   . ARG   A 1 98  ? 14.858  11.120  22.693 1.00 55.55  ? 172 ARG   A C   1 
ATOM   707  O O   . ARG   A 1 98  ? 14.617  12.192  23.254 1.00 58.76  ? 172 ARG   A O   1 
ATOM   708  C CB  . ARG   A 1 98  ? 15.852  11.607  20.473 1.00 59.79  ? 172 ARG   A CB  1 
ATOM   709  C CG  . ARG   A 1 98  ? 17.205  11.103  20.981 1.00 68.48  ? 172 ARG   A CG  1 
ATOM   710  C CD  . ARG   A 1 98  ? 18.402  11.784  20.315 1.00 73.86  ? 172 ARG   A CD  1 
ATOM   711  N NE  . ARG   A 1 98  ? 18.477  13.209  20.613 1.00 72.40  ? 172 ARG   A NE  1 
ATOM   712  C CZ  . ARG   A 1 98  ? 18.034  14.164  19.806 1.00 75.82  ? 172 ARG   A CZ  1 
ATOM   713  N NH1 . ARG   A 1 98  ? 17.486  13.879  18.634 1.00 77.93  ? 172 ARG   A NH1 1 
ATOM   714  N NH2 . ARG   A 1 98  ? 18.140  15.436  20.186 1.00 68.78  ? 172 ARG   A NH2 1 
ATOM   715  N N   . LEU   A 1 99  ? 15.310  10.048  23.338 1.00 55.66  ? 173 LEU   A N   1 
ATOM   716  C CA  . LEU   A 1 99  ? 15.731  10.101  24.731 1.00 54.22  ? 173 LEU   A CA  1 
ATOM   717  C C   . LEU   A 1 99  ? 17.198  10.503  24.794 1.00 59.75  ? 173 LEU   A C   1 
ATOM   718  O O   . LEU   A 1 99  ? 18.035  9.910   24.107 1.00 62.37  ? 173 LEU   A O   1 
ATOM   719  C CB  . LEU   A 1 99  ? 15.530  8.749   25.414 1.00 52.13  ? 173 LEU   A CB  1 
ATOM   720  C CG  . LEU   A 1 99  ? 15.872  8.713   26.905 1.00 50.50  ? 173 LEU   A CG  1 
ATOM   721  C CD1 . LEU   A 1 99  ? 14.927  9.605   27.698 1.00 49.18  ? 173 LEU   A CD1 1 
ATOM   722  C CD2 . LEU   A 1 99  ? 15.842  7.289   27.434 1.00 45.93  ? 173 LEU   A CD2 1 
ATOM   723  N N   . GLU   A 1 100 ? 17.507  11.512  25.611 1.00 57.12  ? 174 GLU   A N   1 
ATOM   724  C CA  . GLU   A 1 100 ? 18.890  11.936  25.800 1.00 60.16  ? 174 GLU   A CA  1 
ATOM   725  C C   . GLU   A 1 100 ? 19.547  11.212  26.968 1.00 58.16  ? 174 GLU   A C   1 
ATOM   726  O O   . GLU   A 1 100 ? 20.629  10.635  26.819 1.00 57.88  ? 174 GLU   A O   1 
ATOM   727  C CB  . GLU   A 1 100 ? 18.961  13.451  26.015 1.00 63.91  ? 174 GLU   A CB  1 
ATOM   728  C CG  . GLU   A 1 100 ? 18.729  14.272  24.754 1.00 71.02  ? 174 GLU   A CG  1 
ATOM   729  C CD  . GLU   A 1 100 ? 19.888  14.180  23.772 1.00 77.86  ? 174 GLU   A CD  1 
ATOM   730  O OE1 . GLU   A 1 100 ? 21.061  14.211  24.221 1.00 75.76  ? 174 GLU   A OE1 1 
ATOM   731  O OE2 . GLU   A 1 100 ? 19.620  14.073  22.550 1.00 77.33  ? 174 GLU   A OE2 1 
ATOM   732  N N   . GLN   A 1 101 ? 18.914  11.242  28.136 1.00 58.63  ? 175 GLN   A N   1 
ATOM   733  C CA  . GLN   A 1 101 ? 19.417  10.491  29.275 1.00 58.76  ? 175 GLN   A CA  1 
ATOM   734  C C   . GLN   A 1 101 ? 18.326  10.389  30.323 1.00 61.09  ? 175 GLN   A C   1 
ATOM   735  O O   . GLN   A 1 101 ? 17.385  11.189  30.357 1.00 58.09  ? 175 GLN   A O   1 
ATOM   736  C CB  . GLN   A 1 101 ? 20.659  11.136  29.875 1.00 57.97  ? 175 GLN   A CB  1 
ATOM   737  C CG  . GLN   A 1 101 ? 20.401  12.474  30.510 1.00 63.29  ? 175 GLN   A CG  1 
ATOM   738  C CD  . GLN   A 1 101 ? 21.689  13.127  30.941 1.00 66.18  ? 175 GLN   A CD  1 
ATOM   739  O OE1 . GLN   A 1 101 ? 22.757  12.522  30.846 1.00 69.64  ? 175 GLN   A OE1 1 
ATOM   740  N NE2 . GLN   A 1 101 ? 21.605  14.366  31.411 1.00 71.52  ? 175 GLN   A NE2 1 
ATOM   741  N N   . ALA   A 1 102 ? 18.471  9.388   31.181 1.00 58.83  ? 176 ALA   A N   1 
ATOM   742  C CA  . ALA   A 1 102 ? 17.558  9.182   32.286 1.00 54.13  ? 176 ALA   A CA  1 
ATOM   743  C C   . ALA   A 1 102 ? 18.362  8.891   33.538 1.00 58.78  ? 176 ALA   A C   1 
ATOM   744  O O   . ALA   A 1 102 ? 19.435  8.282   33.484 1.00 62.58  ? 176 ALA   A O   1 
ATOM   745  C CB  . ALA   A 1 102 ? 16.583  8.046   32.004 1.00 53.07  ? 176 ALA   A CB  1 
ATOM   746  N N   . TRP   A 1 103 ? 17.839  9.347   34.669 1.00 56.83  ? 177 TRP   A N   1 
ATOM   747  C CA  . TRP   A 1 103 ? 18.461  9.054   35.947 1.00 58.44  ? 177 TRP   A CA  1 
ATOM   748  C C   . TRP   A 1 103 ? 17.374  8.924   36.998 1.00 58.28  ? 177 TRP   A C   1 
ATOM   749  O O   . TRP   A 1 103 ? 16.203  9.227   36.756 1.00 61.47  ? 177 TRP   A O   1 
ATOM   750  C CB  . TRP   A 1 103 ? 19.480  10.127  36.336 1.00 61.53  ? 177 TRP   A CB  1 
ATOM   751  C CG  . TRP   A 1 103 ? 18.899  11.486  36.632 1.00 63.37  ? 177 TRP   A CG  1 
ATOM   752  C CD1 . TRP   A 1 103 ? 18.581  11.993  37.862 1.00 64.54  ? 177 TRP   A CD1 1 
ATOM   753  C CD2 . TRP   A 1 103 ? 18.594  12.520  35.683 1.00 61.52  ? 177 TRP   A CD2 1 
ATOM   754  N NE1 . TRP   A 1 103 ? 18.089  13.270  37.737 1.00 66.57  ? 177 TRP   A NE1 1 
ATOM   755  C CE2 . TRP   A 1 103 ? 18.088  13.618  36.411 1.00 65.94  ? 177 TRP   A CE2 1 
ATOM   756  C CE3 . TRP   A 1 103 ? 18.697  12.622  34.291 1.00 60.36  ? 177 TRP   A CE3 1 
ATOM   757  C CZ2 . TRP   A 1 103 ? 17.687  14.804  35.792 1.00 64.33  ? 177 TRP   A CZ2 1 
ATOM   758  C CZ3 . TRP   A 1 103 ? 18.295  13.802  33.677 1.00 60.69  ? 177 TRP   A CZ3 1 
ATOM   759  C CH2 . TRP   A 1 103 ? 17.798  14.875  34.428 1.00 61.71  ? 177 TRP   A CH2 1 
ATOM   760  N N   . GLU   A 1 104 ? 17.774  8.457   38.170 1.00 61.07  ? 178 GLU   A N   1 
ATOM   761  C CA  . GLU   A 1 104 ? 16.880  8.353   39.310 1.00 64.48  ? 178 GLU   A CA  1 
ATOM   762  C C   . GLU   A 1 104 ? 17.565  8.958   40.524 1.00 61.39  ? 178 GLU   A C   1 
ATOM   763  O O   . GLU   A 1 104 ? 18.776  8.802   40.709 1.00 68.54  ? 178 GLU   A O   1 
ATOM   764  C CB  . GLU   A 1 104 ? 16.475  6.889   39.576 1.00 65.18  ? 178 GLU   A CB  1 
ATOM   765  C CG  . GLU   A 1 104 ? 17.627  5.941   39.925 1.00 70.51  ? 178 GLU   A CG  1 
ATOM   766  C CD  . GLU   A 1 104 ? 17.170  4.493   40.031 1.00 69.20  ? 178 GLU   A CD  1 
ATOM   767  O OE1 . GLU   A 1 104 ? 15.945  4.274   40.105 1.00 66.92  ? 178 GLU   A OE1 1 
ATOM   768  O OE2 . GLU   A 1 104 ? 18.023  3.576   40.032 1.00 69.54  ? 178 GLU   A OE2 1 
ATOM   769  N N   . GLU   A 1 105 ? 16.790  9.672   41.336 1.00 63.28  ? 179 GLU   A N   1 
ATOM   770  C CA  . GLU   A 1 105 ? 17.309  10.266  42.561 1.00 68.47  ? 179 GLU   A CA  1 
ATOM   771  C C   . GLU   A 1 105 ? 16.185  10.330  43.582 1.00 65.30  ? 179 GLU   A C   1 
ATOM   772  O O   . GLU   A 1 105 ? 15.105  10.849  43.283 1.00 69.78  ? 179 GLU   A O   1 
ATOM   773  C CB  . GLU   A 1 105 ? 17.881  11.663  42.299 1.00 76.36  ? 179 GLU   A CB  1 
ATOM   774  C CG  . GLU   A 1 105 ? 18.682  12.249  43.453 1.00 84.24  ? 179 GLU   A CG  1 
ATOM   775  C CD  . GLU   A 1 105 ? 19.283  13.600  43.109 1.00 91.20  ? 179 GLU   A CD  1 
ATOM   776  O OE1 . GLU   A 1 105 ? 19.113  14.042  41.951 1.00 91.88  ? 179 GLU   A OE1 1 
ATOM   777  O OE2 . GLU   A 1 105 ? 19.919  14.220  43.990 1.00 94.32  ? 179 GLU   A OE2 1 
ATOM   778  N N   . GLY   A 1 106 ? 16.439  9.794   44.773 1.00 69.55  ? 180 GLY   A N   1 
ATOM   779  C CA  . GLY   A 1 106 ? 15.443  9.804   45.832 1.00 68.41  ? 180 GLY   A CA  1 
ATOM   780  C C   . GLY   A 1 106 ? 14.169  9.056   45.506 1.00 71.26  ? 180 GLY   A C   1 
ATOM   781  O O   . GLY   A 1 106 ? 13.101  9.416   46.013 1.00 74.20  ? 180 GLY   A O   1 
ATOM   782  N N   . GLY   A 1 107 ? 14.247  8.015   44.678 1.00 71.68  ? 181 GLY   A N   1 
ATOM   783  C CA  . GLY   A 1 107 ? 13.061  7.282   44.281 1.00 64.93  ? 181 GLY   A CA  1 
ATOM   784  C C   . GLY   A 1 107 ? 12.244  7.935   43.191 1.00 64.56  ? 181 GLY   A C   1 
ATOM   785  O O   . GLY   A 1 107 ? 11.197  7.392   42.812 1.00 62.67  ? 181 GLY   A O   1 
ATOM   786  N N   . ILE   A 1 108 ? 12.684  9.082   42.679 1.00 64.14  ? 182 ILE   A N   1 
ATOM   787  C CA  . ILE   A 1 108 ? 12.020  9.780   41.586 1.00 61.96  ? 182 ILE   A CA  1 
ATOM   788  C C   . ILE   A 1 108 ? 12.774  9.480   40.297 1.00 56.34  ? 182 ILE   A C   1 
ATOM   789  O O   . ILE   A 1 108 ? 14.008  9.543   40.262 1.00 62.75  ? 182 ILE   A O   1 
ATOM   790  C CB  . ILE   A 1 108 ? 11.966  11.295  41.854 1.00 64.09  ? 182 ILE   A CB  1 
ATOM   791  C CG1 . ILE   A 1 108 ? 11.319  11.574  43.212 1.00 63.23  ? 182 ILE   A CG1 1 
ATOM   792  C CG2 . ILE   A 1 108 ? 11.209  12.004  40.752 1.00 56.67  ? 182 ILE   A CG2 1 
ATOM   793  C CD1 . ILE   A 1 108 ? 9.886   11.079  43.308 1.00 64.82  ? 182 ILE   A CD1 1 
ATOM   794  N N   . LEU   A 1 109 ? 12.039  9.159   39.239 1.00 55.05  ? 183 LEU   A N   1 
ATOM   795  C CA  . LEU   A 1 109 ? 12.620  8.863   37.936 1.00 55.56  ? 183 LEU   A CA  1 
ATOM   796  C C   . LEU   A 1 109 ? 12.555  10.097  37.042 1.00 56.72  ? 183 LEU   A C   1 
ATOM   797  O O   . LEU   A 1 109 ? 11.502  10.734  36.936 1.00 57.96  ? 183 LEU   A O   1 
ATOM   798  C CB  . LEU   A 1 109 ? 11.890  7.697   37.273 1.00 52.45  ? 183 LEU   A CB  1 
ATOM   799  C CG  . LEU   A 1 109 ? 12.346  7.425   35.846 1.00 48.33  ? 183 LEU   A CG  1 
ATOM   800  C CD1 . LEU   A 1 109 ? 13.806  7.000   35.831 1.00 52.94  ? 183 LEU   A CD1 1 
ATOM   801  C CD2 . LEU   A 1 109 ? 11.475  6.371   35.247 1.00 45.96  ? 183 LEU   A CD2 1 
ATOM   802  N N   . TYR   A 1 110 ? 13.678  10.423  36.398 1.00 56.95  ? 184 TYR   A N   1 
ATOM   803  C CA  . TYR   A 1 110 ? 13.807  11.592  35.532 1.00 55.00  ? 184 TYR   A CA  1 
ATOM   804  C C   . TYR   A 1 110 ? 14.181  11.152  34.118 1.00 52.65  ? 184 TYR   A C   1 
ATOM   805  O O   . TYR   A 1 110 ? 15.177  10.448  33.931 1.00 59.51  ? 184 TYR   A O   1 
ATOM   806  C CB  . TYR   A 1 110 ? 14.877  12.559  36.068 1.00 61.54  ? 184 TYR   A CB  1 
ATOM   807  C CG  . TYR   A 1 110 ? 14.583  13.223  37.407 1.00 62.04  ? 184 TYR   A CG  1 
ATOM   808  C CD1 . TYR   A 1 110 ? 14.800  12.549  38.606 1.00 63.09  ? 184 TYR   A CD1 1 
ATOM   809  C CD2 . TYR   A 1 110 ? 14.121  14.534  37.469 1.00 61.41  ? 184 TYR   A CD2 1 
ATOM   810  C CE1 . TYR   A 1 110 ? 14.546  13.156  39.829 1.00 63.31  ? 184 TYR   A CE1 1 
ATOM   811  C CE2 . TYR   A 1 110 ? 13.864  15.151  38.689 1.00 64.21  ? 184 TYR   A CE2 1 
ATOM   812  C CZ  . TYR   A 1 110 ? 14.080  14.455  39.864 1.00 67.88  ? 184 TYR   A CZ  1 
ATOM   813  O OH  . TYR   A 1 110 ? 13.828  15.062  41.076 1.00 72.13  ? 184 TYR   A OH  1 
ATOM   814  N N   . LEU   A 1 111 ? 13.395  11.573  33.126 1.00 54.64  ? 185 LEU   A N   1 
ATOM   815  C CA  . LEU   A 1 111 ? 13.681  11.328  31.714 1.00 53.53  ? 185 LEU   A CA  1 
ATOM   816  C C   . LEU   A 1 111 ? 13.895  12.661  31.013 1.00 54.93  ? 185 LEU   A C   1 
ATOM   817  O O   . LEU   A 1 111 ? 13.061  13.563  31.133 1.00 54.36  ? 185 LEU   A O   1 
ATOM   818  C CB  . LEU   A 1 111 ? 12.541  10.575  31.016 1.00 46.73  ? 185 LEU   A CB  1 
ATOM   819  C CG  . LEU   A 1 111 ? 12.421  9.057   31.106 1.00 50.02  ? 185 LEU   A CG  1 
ATOM   820  C CD1 . LEU   A 1 111 ? 11.941  8.650   32.471 1.00 58.37  ? 185 LEU   A CD1 1 
ATOM   821  C CD2 . LEU   A 1 111 ? 11.477  8.529   30.043 1.00 50.77  ? 185 LEU   A CD2 1 
ATOM   822  N N   . GLN   A 1 112 ? 14.985  12.773  30.257 1.00 58.55  ? 186 GLN   A N   1 
ATOM   823  C CA  . GLN   A 1 112 ? 15.331  14.005  29.548 1.00 56.76  ? 186 GLN   A CA  1 
ATOM   824  C C   . GLN   A 1 112 ? 15.326  13.745  28.045 1.00 55.35  ? 186 GLN   A C   1 
ATOM   825  O O   . GLN   A 1 112 ? 16.221  13.073  27.523 1.00 58.31  ? 186 GLN   A O   1 
ATOM   826  C CB  . GLN   A 1 112 ? 16.691  14.528  30.002 1.00 56.88  ? 186 GLN   A CB  1 
ATOM   827  C CG  . GLN   A 1 112 ? 17.155  15.765  29.265 1.00 60.50  ? 186 GLN   A CG  1 
ATOM   828  C CD  . GLN   A 1 112 ? 18.606  16.072  29.544 1.00 59.29  ? 186 GLN   A CD  1 
ATOM   829  O OE1 . GLN   A 1 112 ? 19.210  15.484  30.439 1.00 60.76  ? 186 GLN   A OE1 1 
ATOM   830  N NE2 . GLN   A 1 112 ? 19.180  16.986  28.774 1.00 67.81  ? 186 GLN   A NE2 1 
ATOM   831  N N   . THR   A 1 113 ? 14.332  14.288  27.351 1.00 57.83  ? 187 THR   A N   1 
ATOM   832  C CA  . THR   A 1 113 ? 14.182  14.114  25.914 1.00 55.79  ? 187 THR   A CA  1 
ATOM   833  C C   . THR   A 1 113 ? 14.463  15.427  25.199 1.00 56.99  ? 187 THR   A C   1 
ATOM   834  O O   . THR   A 1 113 ? 14.614  16.486  25.817 1.00 59.92  ? 187 THR   A O   1 
ATOM   835  C CB  . THR   A 1 113 ? 12.770  13.627  25.564 1.00 54.94  ? 187 THR   A CB  1 
ATOM   836  O OG1 . THR   A 1 113 ? 11.820  14.628  25.945 1.00 55.92  ? 187 THR   A OG1 1 
ATOM   837  C CG2 . THR   A 1 113 ? 12.443  12.330  26.292 1.00 53.24  ? 187 THR   A CG2 1 
ATOM   838  N N   . GLU   A 1 114 ? 14.532  15.350  23.876 1.00 56.23  ? 188 GLU   A N   1 
ATOM   839  C CA  . GLU   A 1 114 ? 14.586  16.567  23.080 1.00 56.81  ? 188 GLU   A CA  1 
ATOM   840  C C   . GLU   A 1 114 ? 13.290  17.356  23.249 1.00 59.95  ? 188 GLU   A C   1 
ATOM   841  O O   . GLU   A 1 114 ? 12.210  16.790  23.440 1.00 58.97  ? 188 GLU   A O   1 
ATOM   842  C CB  . GLU   A 1 114 ? 14.814  16.231  21.607 1.00 55.07  ? 188 GLU   A CB  1 
ATOM   843  C CG  . GLU   A 1 114 ? 13.891  15.145  21.091 1.00 58.74  ? 188 GLU   A CG  1 
ATOM   844  C CD  . GLU   A 1 114 ? 13.686  15.201  19.589 1.00 66.03  ? 188 GLU   A CD  1 
ATOM   845  O OE1 . GLU   A 1 114 ? 13.779  16.309  19.010 1.00 64.98  ? 188 GLU   A OE1 1 
ATOM   846  O OE2 . GLU   A 1 114 ? 13.426  14.133  18.989 1.00 67.41  ? 188 GLU   A OE2 1 
ATOM   847  N N   . LEU   A 1 115 ? 13.405  18.678  23.195 1.00 61.23  ? 189 LEU   A N   1 
ATOM   848  C CA  . LEU   A 1 115 ? 12.235  19.535  23.308 1.00 56.17  ? 189 LEU   A CA  1 
ATOM   849  C C   . LEU   A 1 115 ? 11.495  19.566  21.979 1.00 57.19  ? 189 LEU   A C   1 
ATOM   850  O O   . LEU   A 1 115 ? 12.089  19.841  20.930 1.00 54.65  ? 189 LEU   A O   1 
ATOM   851  C CB  . LEU   A 1 115 ? 12.634  20.951  23.727 1.00 60.46  ? 189 LEU   A CB  1 
ATOM   852  C CG  . LEU   A 1 115 ? 11.463  21.899  24.013 1.00 55.78  ? 189 LEU   A CG  1 
ATOM   853  C CD1 . LEU   A 1 115 ? 10.511  21.266  25.007 1.00 58.24  ? 189 LEU   A CD1 1 
ATOM   854  C CD2 . LEU   A 1 115 ? 11.949  23.230  24.536 1.00 60.17  ? 189 LEU   A CD2 1 
ATOM   855  N N   . CYS   A 1 116 ? 10.202  19.277  22.029 1.00 57.43  ? 190 CYS   A N   1 
ATOM   856  C CA  . CYS   A 1 116 ? 9.341   19.280  20.860 1.00 54.32  ? 190 CYS   A CA  1 
ATOM   857  C C   . CYS   A 1 116 ? 8.374   20.457  20.932 1.00 55.47  ? 190 CYS   A C   1 
ATOM   858  O O   . CYS   A 1 116 ? 8.443   21.304  21.828 1.00 56.39  ? 190 CYS   A O   1 
ATOM   859  C CB  . CYS   A 1 116 ? 8.595   17.953  20.750 1.00 50.22  ? 190 CYS   A CB  1 
ATOM   860  S SG  . CYS   A 1 116 ? 9.692   16.541  20.577 1.00 56.73  ? 190 CYS   A SG  1 
ATOM   861  N N   . GLY   A 1 117 ? 7.472   20.516  19.959 1.00 56.68  ? 191 GLY   A N   1 
ATOM   862  C CA  . GLY   A 1 117 ? 6.428   21.510  19.964 1.00 47.70  ? 191 GLY   A CA  1 
ATOM   863  C C   . GLY   A 1 117 ? 5.279   21.043  20.826 1.00 49.22  ? 191 GLY   A C   1 
ATOM   864  O O   . GLY   A 1 117 ? 5.437   20.171  21.688 1.00 47.63  ? 191 GLY   A O   1 
ATOM   865  N N   . PRO   A 1 118 ? 4.099   21.615  20.618 1.00 51.94  ? 192 PRO   A N   1 
ATOM   866  C CA  . PRO   A 1 118 ? 2.919   21.141  21.347 1.00 48.55  ? 192 PRO   A CA  1 
ATOM   867  C C   . PRO   A 1 118 ? 2.528   19.743  20.900 1.00 48.98  ? 192 PRO   A C   1 
ATOM   868  O O   . PRO   A 1 118 ? 2.878   19.285  19.808 1.00 47.48  ? 192 PRO   A O   1 
ATOM   869  C CB  . PRO   A 1 118 ? 1.835   22.163  20.986 1.00 47.54  ? 192 PRO   A CB  1 
ATOM   870  C CG  . PRO   A 1 118 ? 2.304   22.801  19.718 1.00 52.26  ? 192 PRO   A CG  1 
ATOM   871  C CD  . PRO   A 1 118 ? 3.807   22.791  19.781 1.00 50.66  ? 192 PRO   A CD  1 
ATOM   872  N N   . SER   A 1 119 ? 1.806   19.054  21.777 1.00 44.63  ? 193 SER   A N   1 
ATOM   873  C CA  . SER   A 1 119 ? 1.204   17.795  21.380 1.00 42.96  ? 193 SER   A CA  1 
ATOM   874  C C   . SER   A 1 119 ? 0.169   18.055  20.297 1.00 43.31  ? 193 SER   A C   1 
ATOM   875  O O   . SER   A 1 119 ? -0.400  19.143  20.202 1.00 46.94  ? 193 SER   A O   1 
ATOM   876  C CB  . SER   A 1 119 ? 0.548   17.105  22.575 1.00 46.58  ? 193 SER   A CB  1 
ATOM   877  O OG  . SER   A 1 119 ? -0.691  17.721  22.888 1.00 50.40  ? 193 SER   A OG  1 
ATOM   878  N N   . LEU   A 1 120 ? -0.065  17.044  19.461 1.00 44.74  ? 194 LEU   A N   1 
ATOM   879  C CA  . LEU   A 1 120 ? -1.116  17.162  18.462 1.00 43.20  ? 194 LEU   A CA  1 
ATOM   880  C C   . LEU   A 1 120 ? -2.451  17.496  19.115 1.00 48.16  ? 194 LEU   A C   1 
ATOM   881  O O   . LEU   A 1 120 ? -3.277  18.197  18.522 1.00 54.03  ? 194 LEU   A O   1 
ATOM   882  C CB  . LEU   A 1 120 ? -1.208  15.866  17.654 1.00 47.02  ? 194 LEU   A CB  1 
ATOM   883  C CG  . LEU   A 1 120 ? -2.208  15.799  16.500 1.00 48.12  ? 194 LEU   A CG  1 
ATOM   884  C CD1 . LEU   A 1 120 ? -1.903  16.862  15.460 1.00 54.24  ? 194 LEU   A CD1 1 
ATOM   885  C CD2 . LEU   A 1 120 ? -2.214  14.417  15.869 1.00 41.17  ? 194 LEU   A CD2 1 
ATOM   886  N N   . GLN   A 1 121 ? -2.668  17.027  20.347 1.00 48.60  ? 195 GLN   A N   1 
ATOM   887  C CA  . GLN   A 1 121 ? -3.895  17.361  21.061 1.00 44.71  ? 195 GLN   A CA  1 
ATOM   888  C C   . GLN   A 1 121 ? -3.952  18.849  21.368 1.00 49.87  ? 195 GLN   A C   1 
ATOM   889  O O   . GLN   A 1 121 ? -4.985  19.496  21.161 1.00 54.87  ? 195 GLN   A O   1 
ATOM   890  C CB  . GLN   A 1 121 ? -3.994  16.540  22.346 1.00 47.66  ? 195 GLN   A CB  1 
ATOM   891  C CG  . GLN   A 1 121 ? -5.245  16.801  23.164 1.00 46.13  ? 195 GLN   A CG  1 
ATOM   892  C CD  . GLN   A 1 121 ? -5.237  16.037  24.481 1.00 51.26  ? 195 GLN   A CD  1 
ATOM   893  O OE1 . GLN   A 1 121 ? -4.177  15.777  25.056 1.00 52.30  ? 195 GLN   A OE1 1 
ATOM   894  N NE2 . GLN   A 1 121 ? -6.419  15.663  24.957 1.00 47.62  ? 195 GLN   A NE2 1 
ATOM   895  N N   . GLN   A 1 122 ? -2.846  19.413  21.859 1.00 48.18  ? 196 GLN   A N   1 
ATOM   896  C CA  . GLN   A 1 122 ? -2.800  20.851  22.110 1.00 46.53  ? 196 GLN   A CA  1 
ATOM   897  C C   . GLN   A 1 122 ? -2.969  21.645  20.823 1.00 50.30  ? 196 GLN   A C   1 
ATOM   898  O O   . GLN   A 1 122 ? -3.622  22.695  20.811 1.00 56.04  ? 196 GLN   A O   1 
ATOM   899  C CB  . GLN   A 1 122 ? -1.485  21.228  22.791 1.00 48.55  ? 196 GLN   A CB  1 
ATOM   900  C CG  . GLN   A 1 122 ? -1.418  20.886  24.267 1.00 52.50  ? 196 GLN   A CG  1 
ATOM   901  C CD  . GLN   A 1 122 ? -0.053  21.163  24.864 1.00 52.29  ? 196 GLN   A CD  1 
ATOM   902  O OE1 . GLN   A 1 122 ? 0.972   20.805  24.282 1.00 54.17  ? 196 GLN   A OE1 1 
ATOM   903  N NE2 . GLN   A 1 122 ? -0.031  21.801  26.033 1.00 54.01  ? 196 GLN   A NE2 1 
ATOM   904  N N   . HIS   A 1 123 ? -2.371  21.173  19.731 1.00 50.79  ? 197 HIS   A N   1 
ATOM   905  C CA  . HIS   A 1 123 ? -2.505  21.875  18.460 1.00 51.22  ? 197 HIS   A CA  1 
ATOM   906  C C   . HIS   A 1 123 ? -3.960  21.909  18.009 1.00 54.05  ? 197 HIS   A C   1 
ATOM   907  O O   . HIS   A 1 123 ? -4.489  22.974  17.664 1.00 57.48  ? 197 HIS   A O   1 
ATOM   908  C CB  . HIS   A 1 123 ? -1.614  21.209  17.409 1.00 49.54  ? 197 HIS   A CB  1 
ATOM   909  C CG  . HIS   A 1 123 ? -1.747  21.793  16.041 1.00 49.05  ? 197 HIS   A CG  1 
ATOM   910  N ND1 . HIS   A 1 123 ? -1.406  23.094  15.750 1.00 54.05  ? 197 HIS   A ND1 1 
ATOM   911  C CD2 . HIS   A 1 123 ? -2.177  21.247  14.878 1.00 55.99  ? 197 HIS   A CD2 1 
ATOM   912  C CE1 . HIS   A 1 123 ? -1.627  23.329  14.468 1.00 61.13  ? 197 HIS   A CE1 1 
ATOM   913  N NE2 . HIS   A 1 123 ? -2.092  22.223  13.915 1.00 60.33  ? 197 HIS   A NE2 1 
ATOM   914  N N   . CYS   A 1 124 ? -4.632  20.750  18.027 1.00 54.92  ? 198 CYS   A N   1 
ATOM   915  C CA  . CYS   A 1 124 ? -6.036  20.690  17.618 1.00 56.58  ? 198 CYS   A CA  1 
ATOM   916  C C   . CYS   A 1 124 ? -6.915  21.542  18.523 1.00 58.38  ? 198 CYS   A C   1 
ATOM   917  O O   . CYS   A 1 124 ? -7.810  22.250  18.047 1.00 62.01  ? 198 CYS   A O   1 
ATOM   918  C CB  . CYS   A 1 124 ? -6.523  19.241  17.623 1.00 54.32  ? 198 CYS   A CB  1 
ATOM   919  S SG  . CYS   A 1 124 ? -5.906  18.237  16.256 1.00 60.81  ? 198 CYS   A SG  1 
ATOM   920  N N   . GLU   A 1 125 ? -6.678  21.472  19.834 1.00 58.97  ? 199 GLU   A N   1 
ATOM   921  C CA  . GLU   A 1 125 ? -7.389  22.323  20.781 1.00 58.61  ? 199 GLU   A CA  1 
ATOM   922  C C   . GLU   A 1 125 ? -7.261  23.793  20.404 1.00 59.52  ? 199 GLU   A C   1 
ATOM   923  O O   . GLU   A 1 125 ? -8.248  24.535  20.404 1.00 67.23  ? 199 GLU   A O   1 
ATOM   924  C CB  . GLU   A 1 125 ? -6.847  22.085  22.190 1.00 59.95  ? 199 GLU   A CB  1 
ATOM   925  C CG  . GLU   A 1 125 ? -7.636  22.760  23.286 1.00 71.92  ? 199 GLU   A CG  1 
ATOM   926  C CD  . GLU   A 1 125 ? -8.870  21.972  23.675 1.00 78.98  ? 199 GLU   A CD  1 
ATOM   927  O OE1 . GLU   A 1 125 ? -8.818  20.724  23.598 1.00 80.41  ? 199 GLU   A OE1 1 
ATOM   928  O OE2 . GLU   A 1 125 ? -9.887  22.600  24.054 1.00 79.57  ? 199 GLU   A OE2 1 
ATOM   929  N N   . ALA   A 1 126 ? -6.045  24.229  20.067 1.00 59.63  ? 200 ALA   A N   1 
ATOM   930  C CA  . ALA   A 1 126 ? -5.835  25.634  19.735 1.00 59.75  ? 200 ALA   A CA  1 
ATOM   931  C C   . ALA   A 1 126 ? -6.603  26.028  18.483 1.00 61.06  ? 200 ALA   A C   1 
ATOM   932  O O   . ALA   A 1 126 ? -7.171  27.124  18.414 1.00 64.53  ? 200 ALA   A O   1 
ATOM   933  C CB  . ALA   A 1 126 ? -4.344  25.919  19.561 1.00 57.43  ? 200 ALA   A CB  1 
ATOM   934  N N   . TRP   A 1 127 ? -6.632  25.155  17.479 1.00 59.11  ? 201 TRP   A N   1 
ATOM   935  C CA  . TRP   A 1 127 ? -7.356  25.495  16.265 1.00 61.18  ? 201 TRP   A CA  1 
ATOM   936  C C   . TRP   A 1 127 ? -8.854  25.301  16.427 1.00 67.68  ? 201 TRP   A C   1 
ATOM   937  O O   . TRP   A 1 127 ? -9.636  25.960  15.732 1.00 67.44  ? 201 TRP   A O   1 
ATOM   938  C CB  . TRP   A 1 127 ? -6.821  24.681  15.091 1.00 61.37  ? 201 TRP   A CB  1 
ATOM   939  C CG  . TRP   A 1 127 ? -5.695  25.387  14.429 1.00 63.58  ? 201 TRP   A CG  1 
ATOM   940  C CD1 . TRP   A 1 127 ? -4.356  25.182  14.627 1.00 63.08  ? 201 TRP   A CD1 1 
ATOM   941  C CD2 . TRP   A 1 127 ? -5.804  26.457  13.491 1.00 64.53  ? 201 TRP   A CD2 1 
ATOM   942  N NE1 . TRP   A 1 127 ? -3.625  26.053  13.847 1.00 63.66  ? 201 TRP   A NE1 1 
ATOM   943  C CE2 . TRP   A 1 127 ? -4.493  26.843  13.140 1.00 63.36  ? 201 TRP   A CE2 1 
ATOM   944  C CE3 . TRP   A 1 127 ? -6.885  27.118  12.900 1.00 66.53  ? 201 TRP   A CE3 1 
ATOM   945  C CZ2 . TRP   A 1 127 ? -4.236  27.859  12.228 1.00 68.51  ? 201 TRP   A CZ2 1 
ATOM   946  C CZ3 . TRP   A 1 127 ? -6.628  28.129  11.991 1.00 66.98  ? 201 TRP   A CZ3 1 
ATOM   947  C CH2 . TRP   A 1 127 ? -5.314  28.489  11.664 1.00 68.56  ? 201 TRP   A CH2 1 
ATOM   948  N N   . GLY   A 1 128 ? -9.266  24.411  17.329 1.00 67.78  ? 202 GLY   A N   1 
ATOM   949  C CA  . GLY   A 1 128 ? -10.658 24.308  17.726 1.00 74.24  ? 202 GLY   A CA  1 
ATOM   950  C C   . GLY   A 1 128 ? -11.611 23.921  16.618 1.00 78.16  ? 202 GLY   A C   1 
ATOM   951  O O   . GLY   A 1 128 ? -12.833 23.924  16.808 1.00 83.41  ? 202 GLY   A O   1 
ATOM   952  N N   . ALA   A 1 129 ? -11.062 23.601  15.451 1.00 73.39  ? 203 ALA   A N   1 
ATOM   953  C CA  . ALA   A 1 129 ? -11.817 23.103  14.315 1.00 74.69  ? 203 ALA   A CA  1 
ATOM   954  C C   . ALA   A 1 129 ? -11.115 21.862  13.789 1.00 75.76  ? 203 ALA   A C   1 
ATOM   955  O O   . ALA   A 1 129 ? -10.117 21.401  14.353 1.00 76.22  ? 203 ALA   A O   1 
ATOM   956  C CB  . ALA   A 1 129 ? -11.949 24.171  13.223 1.00 70.65  ? 203 ALA   A CB  1 
ATOM   957  N N   . SER   A 1 130 ? -11.641 21.310  12.700 1.00 72.41  ? 204 SER   A N   1 
ATOM   958  C CA  . SER   A 1 130 ? -10.947 20.211  12.049 1.00 70.03  ? 204 SER   A CA  1 
ATOM   959  C C   . SER   A 1 130 ? -9.598  20.693  11.523 1.00 72.12  ? 204 SER   A C   1 
ATOM   960  O O   . SER   A 1 130 ? -9.368  21.889  11.325 1.00 79.10  ? 204 SER   A O   1 
ATOM   961  C CB  . SER   A 1 130 ? -11.788 19.644  10.905 1.00 68.51  ? 204 SER   A CB  1 
ATOM   962  O OG  . SER   A 1 130 ? -13.053 19.210  11.366 1.00 74.83  ? 204 SER   A OG  1 
ATOM   963  N N   . LEU   A 1 131 ? -8.699  19.753  11.316 1.00 67.98  ? 205 LEU   A N   1 
ATOM   964  C CA  . LEU   A 1 131 ? -7.488  20.229  10.662 1.00 67.32  ? 205 LEU   A CA  1 
ATOM   965  C C   . LEU   A 1 131 ? -7.624  20.120  9.148  1.00 68.94  ? 205 LEU   A C   1 
ATOM   966  O O   . LEU   A 1 131 ? -8.277  19.201  8.640  1.00 73.13  ? 205 LEU   A O   1 
ATOM   967  C CB  . LEU   A 1 131 ? -6.273  19.426  11.118 1.00 66.65  ? 205 LEU   A CB  1 
ATOM   968  C CG  . LEU   A 1 131 ? -5.833  19.567  12.572 1.00 66.83  ? 205 LEU   A CG  1 
ATOM   969  C CD1 . LEU   A 1 131 ? -4.601  18.714  12.792 1.00 65.18  ? 205 LEU   A CD1 1 
ATOM   970  C CD2 . LEU   A 1 131 ? -5.560  21.028  12.921 1.00 64.30  ? 205 LEU   A CD2 1 
ATOM   971  N N   . PRO   A 1 132 ? -7.036  21.053  8.401  1.00 71.39  ? 206 PRO   A N   1 
ATOM   972  C CA  . PRO   A 1 132 ? -7.017  20.912  6.941  1.00 65.48  ? 206 PRO   A CA  1 
ATOM   973  C C   . PRO   A 1 132 ? -6.278  19.647  6.532  1.00 65.52  ? 206 PRO   A C   1 
ATOM   974  O O   . PRO   A 1 132 ? -5.297  19.243  7.159  1.00 65.84  ? 206 PRO   A O   1 
ATOM   975  C CB  . PRO   A 1 132 ? -6.286  22.175  6.465  1.00 64.41  ? 206 PRO   A CB  1 
ATOM   976  C CG  . PRO   A 1 132 ? -5.580  22.699  7.674  1.00 67.29  ? 206 PRO   A CG  1 
ATOM   977  C CD  . PRO   A 1 132 ? -6.424  22.315  8.846  1.00 70.31  ? 206 PRO   A CD  1 
ATOM   978  N N   . GLU   A 1 133 ? -6.770  19.014  5.464  1.00 64.97  ? 207 GLU   A N   1 
ATOM   979  C CA  . GLU   A 1 133 ? -6.263  17.699  5.083  1.00 67.36  ? 207 GLU   A CA  1 
ATOM   980  C C   . GLU   A 1 133 ? -4.777  17.706  4.746  1.00 68.73  ? 207 GLU   A C   1 
ATOM   981  O O   . GLU   A 1 133 ? -4.126  16.663  4.866  1.00 69.08  ? 207 GLU   A O   1 
ATOM   982  C CB  . GLU   A 1 133 ? -7.059  17.143  3.901  1.00 70.05  ? 207 GLU   A CB  1 
ATOM   983  C CG  . GLU   A 1 133 ? -8.441  16.629  4.282  1.00 77.36  ? 207 GLU   A CG  1 
ATOM   984  C CD  . GLU   A 1 133 ? -8.904  15.482  3.401  1.00 84.57  ? 207 GLU   A CD  1 
ATOM   985  O OE1 . GLU   A 1 133 ? -8.067  14.919  2.663  1.00 82.46  ? 207 GLU   A OE1 1 
ATOM   986  O OE2 . GLU   A 1 133 ? -10.106 15.141  3.445  1.00 89.98  ? 207 GLU   A OE2 1 
ATOM   987  N N   . ALA   A 1 134 ? -4.223  18.844  4.326  1.00 73.32  ? 208 ALA   A N   1 
ATOM   988  C CA  . ALA   A 1 134 ? -2.793  18.896  4.032  1.00 72.35  ? 208 ALA   A CA  1 
ATOM   989  C C   . ALA   A 1 134 ? -1.964  18.606  5.282  1.00 71.25  ? 208 ALA   A C   1 
ATOM   990  O O   . ALA   A 1 134 ? -1.013  17.816  5.241  1.00 71.82  ? 208 ALA   A O   1 
ATOM   991  C CB  . ALA   A 1 134 ? -2.425  20.254  3.432  1.00 71.30  ? 208 ALA   A CB  1 
ATOM   992  N N   . GLN   A 1 135 ? -2.316  19.229  6.412  1.00 70.85  ? 209 GLN   A N   1 
ATOM   993  C CA  . GLN   A 1 135 ? -1.627  18.916  7.663  1.00 66.50  ? 209 GLN   A CA  1 
ATOM   994  C C   . GLN   A 1 135 ? -1.868  17.471  8.076  1.00 63.29  ? 209 GLN   A C   1 
ATOM   995  O O   . GLN   A 1 135 ? -0.969  16.806  8.609  1.00 61.30  ? 209 GLN   A O   1 
ATOM   996  C CB  . GLN   A 1 135 ? -2.088  19.854  8.781  1.00 68.67  ? 209 GLN   A CB  1 
ATOM   997  C CG  . GLN   A 1 135 ? -1.896  21.336  8.514  1.00 72.97  ? 209 GLN   A CG  1 
ATOM   998  C CD  . GLN   A 1 135 ? -2.261  22.178  9.725  1.00 73.71  ? 209 GLN   A CD  1 
ATOM   999  O OE1 . GLN   A 1 135 ? -2.413  21.658  10.832 1.00 68.77  ? 209 GLN   A OE1 1 
ATOM   1000 N NE2 . GLN   A 1 135 ? -2.406  23.484  9.519  1.00 81.36  ? 209 GLN   A NE2 1 
ATOM   1001 N N   . VAL   A 1 136 ? -3.086  16.974  7.850  1.00 61.83  ? 210 VAL   A N   1 
ATOM   1002 C CA  . VAL   A 1 136 ? -3.442  15.626  8.281  1.00 62.92  ? 210 VAL   A CA  1 
ATOM   1003 C C   . VAL   A 1 136 ? -2.566  14.595  7.578  1.00 64.49  ? 210 VAL   A C   1 
ATOM   1004 O O   . VAL   A 1 136 ? -1.977  13.715  8.220  1.00 57.72  ? 210 VAL   A O   1 
ATOM   1005 C CB  . VAL   A 1 136 ? -4.941  15.371  8.035  1.00 67.01  ? 210 VAL   A CB  1 
ATOM   1006 C CG1 . VAL   A 1 136 ? -5.307  13.927  8.346  1.00 65.89  ? 210 VAL   A CG1 1 
ATOM   1007 C CG2 . VAL   A 1 136 ? -5.780  16.328  8.874  1.00 64.84  ? 210 VAL   A CG2 1 
ATOM   1008 N N   . TRP   A 1 137 ? -2.449  14.701  6.250  1.00 60.74  ? 211 TRP   A N   1 
ATOM   1009 C CA  . TRP   A 1 137 ? -1.630  13.750  5.504  1.00 60.94  ? 211 TRP   A CA  1 
ATOM   1010 C C   . TRP   A 1 137 ? -0.188  13.752  5.997  1.00 59.75  ? 211 TRP   A C   1 
ATOM   1011 O O   . TRP   A 1 137 ? 0.432   12.689  6.132  1.00 62.69  ? 211 TRP   A O   1 
ATOM   1012 C CB  . TRP   A 1 137 ? -1.685  14.060  4.008  1.00 62.50  ? 211 TRP   A CB  1 
ATOM   1013 C CG  . TRP   A 1 137 ? -2.960  13.633  3.345  1.00 62.55  ? 211 TRP   A CG  1 
ATOM   1014 C CD1 . TRP   A 1 137 ? -3.936  14.443  2.845  1.00 68.04  ? 211 TRP   A CD1 1 
ATOM   1015 C CD2 . TRP   A 1 137 ? -3.396  12.289  3.109  1.00 65.36  ? 211 TRP   A CD2 1 
ATOM   1016 N NE1 . TRP   A 1 137 ? -4.952  13.688  2.312  1.00 68.94  ? 211 TRP   A NE1 1 
ATOM   1017 C CE2 . TRP   A 1 137 ? -4.645  12.362  2.463  1.00 67.13  ? 211 TRP   A CE2 1 
ATOM   1018 C CE3 . TRP   A 1 137 ? -2.851  11.031  3.385  1.00 69.47  ? 211 TRP   A CE3 1 
ATOM   1019 C CZ2 . TRP   A 1 137 ? -5.358  11.225  2.084  1.00 78.19  ? 211 TRP   A CZ2 1 
ATOM   1020 C CZ3 . TRP   A 1 137 ? -3.559  9.904   3.011  1.00 73.09  ? 211 TRP   A CZ3 1 
ATOM   1021 C CH2 . TRP   A 1 137 ? -4.800  10.008  2.368  1.00 78.40  ? 211 TRP   A CH2 1 
ATOM   1022 N N   . GLY   A 1 138 ? 0.363   14.935  6.273  1.00 57.78  ? 212 GLY   A N   1 
ATOM   1023 C CA  . GLY   A 1 138 ? 1.716   14.998  6.802  1.00 56.24  ? 212 GLY   A CA  1 
ATOM   1024 C C   . GLY   A 1 138 ? 1.839   14.304  8.143  1.00 59.56  ? 212 GLY   A C   1 
ATOM   1025 O O   . GLY   A 1 138 ? 2.756   13.510  8.365  1.00 60.14  ? 212 GLY   A O   1 
ATOM   1026 N N   . TYR   A 1 139 ? 0.906   14.587  9.055  1.00 53.83  ? 213 TYR   A N   1 
ATOM   1027 C CA  . TYR   A 1 139 ? 0.946   13.944  10.363 1.00 56.50  ? 213 TYR   A CA  1 
ATOM   1028 C C   . TYR   A 1 139 ? 0.693   12.447  10.246 1.00 57.50  ? 213 TYR   A C   1 
ATOM   1029 O O   . TYR   A 1 139 ? 1.288   11.653  10.985 1.00 60.24  ? 213 TYR   A O   1 
ATOM   1030 C CB  . TYR   A 1 139 ? -0.072  14.590  11.301 1.00 53.27  ? 213 TYR   A CB  1 
ATOM   1031 C CG  . TYR   A 1 139 ? 0.230   16.032  11.653 1.00 50.85  ? 213 TYR   A CG  1 
ATOM   1032 C CD1 . TYR   A 1 139 ? 1.524   16.530  11.578 1.00 55.52  ? 213 TYR   A CD1 1 
ATOM   1033 C CD2 . TYR   A 1 139 ? -0.779  16.892  12.062 1.00 54.16  ? 213 TYR   A CD2 1 
ATOM   1034 C CE1 . TYR   A 1 139 ? 1.806   17.850  11.897 1.00 55.81  ? 213 TYR   A CE1 1 
ATOM   1035 C CE2 . TYR   A 1 139 ? -0.506  18.213  12.388 1.00 59.00  ? 213 TYR   A CE2 1 
ATOM   1036 C CZ  . TYR   A 1 139 ? 0.790   18.684  12.305 1.00 55.93  ? 213 TYR   A CZ  1 
ATOM   1037 O OH  . TYR   A 1 139 ? 1.068   19.994  12.622 1.00 55.21  ? 213 TYR   A OH  1 
ATOM   1038 N N   . LEU   A 1 140 ? -0.188  12.041  9.331  1.00 56.14  ? 214 LEU   A N   1 
ATOM   1039 C CA  . LEU   A 1 140 ? -0.402  10.615  9.110  1.00 56.47  ? 214 LEU   A CA  1 
ATOM   1040 C C   . LEU   A 1 140 ? 0.869   9.952   8.599  1.00 59.48  ? 214 LEU   A C   1 
ATOM   1041 O O   . LEU   A 1 140 ? 1.249   8.870   9.065  1.00 58.18  ? 214 LEU   A O   1 
ATOM   1042 C CB  . LEU   A 1 140 ? -1.559  10.398  8.131  1.00 59.39  ? 214 LEU   A CB  1 
ATOM   1043 C CG  . LEU   A 1 140 ? -1.849  8.962   7.667  1.00 60.92  ? 214 LEU   A CG  1 
ATOM   1044 C CD1 . LEU   A 1 140 ? -2.327  8.080   8.811  1.00 52.91  ? 214 LEU   A CD1 1 
ATOM   1045 C CD2 . LEU   A 1 140 ? -2.861  8.944   6.527  1.00 56.05  ? 214 LEU   A CD2 1 
ATOM   1046 N N   . ARG   A 1 141 ? 1.560   10.598  7.661  1.00 57.01  ? 215 ARG   A N   1 
ATOM   1047 C CA  . ARG   A 1 141 ? 2.763   9.989   7.111  1.00 56.88  ? 215 ARG   A CA  1 
ATOM   1048 C C   . ARG   A 1 141 ? 3.876   9.923   8.149  1.00 53.03  ? 215 ARG   A C   1 
ATOM   1049 O O   . ARG   A 1 141 ? 4.615   8.935   8.208  1.00 62.30  ? 215 ARG   A O   1 
ATOM   1050 C CB  . ARG   A 1 141 ? 3.230   10.752  5.875  1.00 61.15  ? 215 ARG   A CB  1 
ATOM   1051 C CG  . ARG   A 1 141 ? 4.400   10.085  5.179  1.00 62.18  ? 215 ARG   A CG  1 
ATOM   1052 C CD  . ARG   A 1 141 ? 4.838   10.860  3.950  1.00 76.25  ? 215 ARG   A CD  1 
ATOM   1053 N NE  . ARG   A 1 141 ? 6.053   10.303  3.362  1.00 81.61  ? 215 ARG   A NE  1 
ATOM   1054 C CZ  . ARG   A 1 141 ? 7.282   10.558  3.795  1.00 82.58  ? 215 ARG   A CZ  1 
ATOM   1055 N NH1 . ARG   A 1 141 ? 7.500   11.357  4.828  1.00 82.46  ? 215 ARG   A NH1 1 
ATOM   1056 N NH2 . ARG   A 1 141 ? 8.318   9.997   3.177  1.00 84.48  ? 215 ARG   A NH2 1 
ATOM   1057 N N   . ASP   A 1 142 ? 4.015   10.956  8.977  1.00 57.98  ? 216 ASP   A N   1 
ATOM   1058 C CA  . ASP   A 1 142 ? 5.087   10.949  9.969  1.00 58.00  ? 216 ASP   A CA  1 
ATOM   1059 C C   . ASP   A 1 142 ? 4.853   9.876   11.023 1.00 52.15  ? 216 ASP   A C   1 
ATOM   1060 O O   . ASP   A 1 142 ? 5.770   9.123   11.370 1.00 54.50  ? 216 ASP   A O   1 
ATOM   1061 C CB  . ASP   A 1 142 ? 5.220   12.325  10.617 1.00 54.00  ? 216 ASP   A CB  1 
ATOM   1062 C CG  . ASP   A 1 142 ? 5.909   13.332  9.707  1.00 65.05  ? 216 ASP   A CG  1 
ATOM   1063 O OD1 . ASP   A 1 142 ? 6.100   13.020  8.508  1.00 63.74  ? 216 ASP   A OD1 1 
ATOM   1064 O OD2 . ASP   A 1 142 ? 6.267   14.430  10.194 1.00 67.10  ? 216 ASP   A OD2 1 
ATOM   1065 N N   . THR   A 1 143 ? 3.631   9.788   11.544 1.00 51.33  ? 217 THR   A N   1 
ATOM   1066 C CA  . THR   A 1 143 ? 3.354   8.773   12.548 1.00 50.74  ? 217 THR   A CA  1 
ATOM   1067 C C   . THR   A 1 143 ? 3.354   7.377   11.941 1.00 55.00  ? 217 THR   A C   1 
ATOM   1068 O O   . THR   A 1 143 ? 3.706   6.408   12.624 1.00 56.43  ? 217 THR   A O   1 
ATOM   1069 C CB  . THR   A 1 143 ? 2.022   9.061   13.236 1.00 53.56  ? 217 THR   A CB  1 
ATOM   1070 O OG1 . THR   A 1 143 ? 1.933   10.461  13.525 1.00 49.40  ? 217 THR   A OG1 1 
ATOM   1071 C CG2 . THR   A 1 143 ? 1.922   8.285   14.542 1.00 46.26  ? 217 THR   A CG2 1 
ATOM   1072 N N   . LEU   A 1 144 ? 2.975   7.244   10.668 1.00 54.74  ? 218 LEU   A N   1 
ATOM   1073 C CA  . LEU   A 1 144 ? 3.098   5.941   10.027 1.00 52.06  ? 218 LEU   A CA  1 
ATOM   1074 C C   . LEU   A 1 144 ? 4.560   5.546   9.880  1.00 56.10  ? 218 LEU   A C   1 
ATOM   1075 O O   . LEU   A 1 144 ? 4.907   4.367   10.022 1.00 59.23  ? 218 LEU   A O   1 
ATOM   1076 C CB  . LEU   A 1 144 ? 2.405   5.939   8.665  1.00 63.70  ? 218 LEU   A CB  1 
ATOM   1077 C CG  . LEU   A 1 144 ? 0.905   5.636   8.624  1.00 60.26  ? 218 LEU   A CG  1 
ATOM   1078 C CD1 . LEU   A 1 144 ? 0.427   5.696   7.193  1.00 58.00  ? 218 LEU   A CD1 1 
ATOM   1079 C CD2 . LEU   A 1 144 ? 0.598   4.274   9.220  1.00 52.36  ? 218 LEU   A CD2 1 
ATOM   1080 N N   . LEU   A 1 145 ? 5.433   6.518   9.594  1.00 57.11  ? 219 LEU   A N   1 
ATOM   1081 C CA  . LEU   A 1 145 ? 6.861   6.223   9.531  1.00 55.15  ? 219 LEU   A CA  1 
ATOM   1082 C C   . LEU   A 1 145 ? 7.378   5.773   10.888 1.00 56.55  ? 219 LEU   A C   1 
ATOM   1083 O O   . LEU   A 1 145 ? 8.188   4.843   10.973 1.00 56.42  ? 219 LEU   A O   1 
ATOM   1084 C CB  . LEU   A 1 145 ? 7.639   7.442   9.041  1.00 55.80  ? 219 LEU   A CB  1 
ATOM   1085 C CG  . LEU   A 1 145 ? 7.566   7.792   7.555  1.00 58.47  ? 219 LEU   A CG  1 
ATOM   1086 C CD1 . LEU   A 1 145 ? 8.227   9.135   7.318  1.00 65.38  ? 219 LEU   A CD1 1 
ATOM   1087 C CD2 . LEU   A 1 145 ? 8.213   6.722   6.685  1.00 57.36  ? 219 LEU   A CD2 1 
ATOM   1088 N N   . ALA   A 1 146 ? 6.917   6.420   11.962 1.00 52.47  ? 220 ALA   A N   1 
ATOM   1089 C CA  . ALA   A 1 146 ? 7.308   5.993   13.299 1.00 50.39  ? 220 ALA   A CA  1 
ATOM   1090 C C   . ALA   A 1 146 ? 6.830   4.576   13.570 1.00 52.01  ? 220 ALA   A C   1 
ATOM   1091 O O   . ALA   A 1 146 ? 7.613   3.710   13.975 1.00 55.24  ? 220 ALA   A O   1 
ATOM   1092 C CB  . ALA   A 1 146 ? 6.754   6.961   14.344 1.00 47.54  ? 220 ALA   A CB  1 
ATOM   1093 N N   . LEU   A 1 147 ? 5.543   4.315   13.319 1.00 52.61  ? 221 LEU   A N   1 
ATOM   1094 C CA  . LEU   A 1 147 ? 4.986   2.992   13.577 1.00 50.16  ? 221 LEU   A CA  1 
ATOM   1095 C C   . LEU   A 1 147 ? 5.684   1.919   12.749 1.00 53.30  ? 221 LEU   A C   1 
ATOM   1096 O O   . LEU   A 1 147 ? 5.934   0.812   13.238 1.00 57.73  ? 221 LEU   A O   1 
ATOM   1097 C CB  . LEU   A 1 147 ? 3.484   2.996   13.300 1.00 50.80  ? 221 LEU   A CB  1 
ATOM   1098 C CG  . LEU   A 1 147 ? 2.600   3.818   14.239 1.00 44.39  ? 221 LEU   A CG  1 
ATOM   1099 C CD1 . LEU   A 1 147 ? 1.142   3.536   13.945 1.00 43.73  ? 221 LEU   A CD1 1 
ATOM   1100 C CD2 . LEU   A 1 147 ? 2.918   3.513   15.692 1.00 44.07  ? 221 LEU   A CD2 1 
ATOM   1101 N N   . ALA   A 1 148 ? 6.010   2.222   11.494 1.00 52.23  ? 222 ALA   A N   1 
ATOM   1102 C CA  . ALA   A 1 148 ? 6.730   1.245   10.687 1.00 53.03  ? 222 ALA   A CA  1 
ATOM   1103 C C   . ALA   A 1 148 ? 8.094   0.943   11.293 1.00 55.96  ? 222 ALA   A C   1 
ATOM   1104 O O   . ALA   A 1 148 ? 8.555   -0.206  11.268 1.00 63.87  ? 222 ALA   A O   1 
ATOM   1105 C CB  . ALA   A 1 148 ? 6.874   1.746   9.252  1.00 53.14  ? 222 ALA   A CB  1 
ATOM   1106 N N   . HIS   A 1 149 ? 8.752   1.961   11.850 1.00 54.88  ? 223 HIS   A N   1 
ATOM   1107 C CA  . HIS   A 1 149 ? 10.044  1.744   12.496 1.00 56.18  ? 223 HIS   A CA  1 
ATOM   1108 C C   . HIS   A 1 149 ? 9.889   0.907   13.761 1.00 59.77  ? 223 HIS   A C   1 
ATOM   1109 O O   . HIS   A 1 149 ? 10.711  0.023   14.033 1.00 61.00  ? 223 HIS   A O   1 
ATOM   1110 C CB  . HIS   A 1 149 ? 10.694  3.090   12.811 1.00 57.90  ? 223 HIS   A CB  1 
ATOM   1111 C CG  . HIS   A 1 149 ? 11.911  2.993   13.676 1.00 56.96  ? 223 HIS   A CG  1 
ATOM   1112 N ND1 . HIS   A 1 149 ? 13.126  2.543   13.206 1.00 57.47  ? 223 HIS   A ND1 1 
ATOM   1113 C CD2 . HIS   A 1 149 ? 12.104  3.308   14.978 1.00 55.56  ? 223 HIS   A CD2 1 
ATOM   1114 C CE1 . HIS   A 1 149 ? 14.014  2.579   14.184 1.00 59.47  ? 223 HIS   A CE1 1 
ATOM   1115 N NE2 . HIS   A 1 149 ? 13.418  3.039   15.270 1.00 58.25  ? 223 HIS   A NE2 1 
ATOM   1116 N N   . LEU   A 1 150 ? 8.836   1.164   14.540 1.00 48.28  ? 224 LEU   A N   1 
ATOM   1117 C CA  . LEU   A 1 150 ? 8.588   0.354   15.727 1.00 52.91  ? 224 LEU   A CA  1 
ATOM   1118 C C   . LEU   A 1 150 ? 8.240   -1.077  15.349 1.00 53.68  ? 224 LEU   A C   1 
ATOM   1119 O O   . LEU   A 1 150 ? 8.786   -2.031  15.914 1.00 60.73  ? 224 LEU   A O   1 
ATOM   1120 C CB  . LEU   A 1 150 ? 7.467   0.969   16.569 1.00 50.98  ? 224 LEU   A CB  1 
ATOM   1121 C CG  . LEU   A 1 150 ? 7.878   1.857   17.742 1.00 44.83  ? 224 LEU   A CG  1 
ATOM   1122 C CD1 . LEU   A 1 150 ? 8.637   3.068   17.255 1.00 46.03  ? 224 LEU   A CD1 1 
ATOM   1123 C CD2 . LEU   A 1 150 ? 6.659   2.284   18.547 1.00 48.43  ? 224 LEU   A CD2 1 
ATOM   1124 N N   . HIS   A 1 151 ? 7.344   -1.251  14.380 1.00 51.95  ? 225 HIS   A N   1 
ATOM   1125 C CA  . HIS   A 1 151 ? 6.863   -2.593  14.086 1.00 52.21  ? 225 HIS   A CA  1 
ATOM   1126 C C   . HIS   A 1 151 ? 7.939   -3.452  13.445 1.00 59.67  ? 225 HIS   A C   1 
ATOM   1127 O O   . HIS   A 1 151 ? 7.921   -4.678  13.607 1.00 61.40  ? 225 HIS   A O   1 
ATOM   1128 C CB  . HIS   A 1 151 ? 5.623   -2.523  13.200 1.00 52.43  ? 225 HIS   A CB  1 
ATOM   1129 C CG  . HIS   A 1 151 ? 4.480   -1.796  13.834 1.00 54.47  ? 225 HIS   A CG  1 
ATOM   1130 N ND1 . HIS   A 1 151 ? 3.310   -1.510  13.162 1.00 49.23  ? 225 HIS   A ND1 1 
ATOM   1131 C CD2 . HIS   A 1 151 ? 4.333   -1.290  15.081 1.00 45.26  ? 225 HIS   A CD2 1 
ATOM   1132 C CE1 . HIS   A 1 151 ? 2.491   -0.859  13.969 1.00 49.86  ? 225 HIS   A CE1 1 
ATOM   1133 N NE2 . HIS   A 1 151 ? 3.088   -0.713  15.140 1.00 47.91  ? 225 HIS   A NE2 1 
ATOM   1134 N N   . SER   A 1 152 ? 8.887   -2.843  12.728 1.00 60.71  ? 226 SER   A N   1 
ATOM   1135 C CA  . SER   A 1 152 ? 9.958   -3.644  12.138 1.00 60.76  ? 226 SER   A CA  1 
ATOM   1136 C C   . SER   A 1 152 ? 10.847  -4.283  13.199 1.00 60.76  ? 226 SER   A C   1 
ATOM   1137 O O   . SER   A 1 152 ? 11.583  -5.219  12.882 1.00 68.45  ? 226 SER   A O   1 
ATOM   1138 C CB  . SER   A 1 152 ? 10.809  -2.800  11.187 1.00 63.07  ? 226 SER   A CB  1 
ATOM   1139 O OG  . SER   A 1 152 ? 11.794  -2.071  11.898 1.00 66.20  ? 226 SER   A OG  1 
ATOM   1140 N N   . GLN   A 1 153 ? 10.797  -3.809  14.445 1.00 60.63  ? 227 GLN   A N   1 
ATOM   1141 C CA  . GLN   A 1 153 ? 11.546  -4.409  15.541 1.00 58.20  ? 227 GLN   A CA  1 
ATOM   1142 C C   . GLN   A 1 153 ? 10.628  -5.115  16.534 1.00 59.51  ? 227 GLN   A C   1 
ATOM   1143 O O   . GLN   A 1 153 ? 10.961  -5.240  17.716 1.00 60.58  ? 227 GLN   A O   1 
ATOM   1144 C CB  . GLN   A 1 153 ? 12.379  -3.352  16.263 1.00 59.79  ? 227 GLN   A CB  1 
ATOM   1145 C CG  . GLN   A 1 153 ? 13.351  -2.601  15.384 1.00 56.55  ? 227 GLN   A CG  1 
ATOM   1146 C CD  . GLN   A 1 153 ? 13.921  -1.404  16.107 1.00 55.98  ? 227 GLN   A CD  1 
ATOM   1147 O OE1 . GLN   A 1 153 ? 13.231  -0.404  16.308 1.00 56.07  ? 227 GLN   A OE1 1 
ATOM   1148 N NE2 . GLN   A 1 153 ? 15.178  -1.504  16.524 1.00 62.40  ? 227 GLN   A NE2 1 
ATOM   1149 N N   . GLY   A 1 154 ? 9.462   -5.564  16.073 1.00 62.58  ? 228 GLY   A N   1 
ATOM   1150 C CA  . GLY   A 1 154 ? 8.535   -6.281  16.933 1.00 59.46  ? 228 GLY   A CA  1 
ATOM   1151 C C   . GLY   A 1 154 ? 8.083   -5.499  18.146 1.00 60.02  ? 228 GLY   A C   1 
ATOM   1152 O O   . GLY   A 1 154 ? 7.767   -6.100  19.179 1.00 59.52  ? 228 GLY   A O   1 
ATOM   1153 N N   . LEU   A 1 155 ? 8.052   -4.172  18.052 1.00 59.72  ? 229 LEU   A N   1 
ATOM   1154 C CA  . LEU   A 1 155 ? 7.604   -3.311  19.138 1.00 52.11  ? 229 LEU   A CA  1 
ATOM   1155 C C   . LEU   A 1 155 ? 6.205   -2.796  18.828 1.00 53.79  ? 229 LEU   A C   1 
ATOM   1156 O O   . LEU   A 1 155 ? 5.909   -2.427  17.687 1.00 54.79  ? 229 LEU   A O   1 
ATOM   1157 C CB  . LEU   A 1 155 ? 8.563   -2.134  19.337 1.00 49.20  ? 229 LEU   A CB  1 
ATOM   1158 C CG  . LEU   A 1 155 ? 10.060  -2.446  19.471 1.00 51.82  ? 229 LEU   A CG  1 
ATOM   1159 C CD1 . LEU   A 1 155 ? 10.882  -1.180  19.702 1.00 46.48  ? 229 LEU   A CD1 1 
ATOM   1160 C CD2 . LEU   A 1 155 ? 10.305  -3.441  20.583 1.00 54.80  ? 229 LEU   A CD2 1 
ATOM   1161 N N   . VAL   A 1 156 ? 5.348   -2.777  19.845 1.00 49.35  ? 230 VAL   A N   1 
ATOM   1162 C CA  . VAL   A 1 156 ? 3.981   -2.284  19.724 1.00 46.18  ? 230 VAL   A CA  1 
ATOM   1163 C C   . VAL   A 1 156 ? 3.801   -1.131  20.703 1.00 47.64  ? 230 VAL   A C   1 
ATOM   1164 O O   . VAL   A 1 156 ? 4.045   -1.290  21.905 1.00 51.46  ? 230 VAL   A O   1 
ATOM   1165 C CB  . VAL   A 1 156 ? 2.957   -3.398  19.994 1.00 43.83  ? 230 VAL   A CB  1 
ATOM   1166 C CG1 . VAL   A 1 156 ? 1.545   -2.901  19.716 1.00 48.94  ? 230 VAL   A CG1 1 
ATOM   1167 C CG2 . VAL   A 1 156 ? 3.281   -4.619  19.150 1.00 54.93  ? 230 VAL   A CG2 1 
ATOM   1168 N N   . HIS   A 1 157 ? 3.369   0.025   20.193 1.00 42.88  ? 231 HIS   A N   1 
ATOM   1169 C CA  . HIS   A 1 157 ? 3.328   1.226   21.023 1.00 41.23  ? 231 HIS   A CA  1 
ATOM   1170 C C   . HIS   A 1 157 ? 2.212   1.149   22.054 1.00 44.94  ? 231 HIS   A C   1 
ATOM   1171 O O   . HIS   A 1 157 ? 2.438   1.407   23.243 1.00 45.10  ? 231 HIS   A O   1 
ATOM   1172 C CB  . HIS   A 1 157 ? 3.161   2.468   20.148 1.00 42.18  ? 231 HIS   A CB  1 
ATOM   1173 C CG  . HIS   A 1 157 ? 3.225   3.752   20.913 1.00 44.72  ? 231 HIS   A CG  1 
ATOM   1174 N ND1 . HIS   A 1 157 ? 2.115   4.332   21.492 1.00 47.02  ? 231 HIS   A ND1 1 
ATOM   1175 C CD2 . HIS   A 1 157 ? 4.269   4.565   21.204 1.00 44.87  ? 231 HIS   A CD2 1 
ATOM   1176 C CE1 . HIS   A 1 157 ? 2.471   5.454   22.095 1.00 44.98  ? 231 HIS   A CE1 1 
ATOM   1177 N NE2 . HIS   A 1 157 ? 3.775   5.616   21.941 1.00 45.03  ? 231 HIS   A NE2 1 
ATOM   1178 N N   . LEU   A 1 158 ? 0.994   0.829   21.606 1.00 46.37  ? 232 LEU   A N   1 
ATOM   1179 C CA  . LEU   A 1 158 ? -0.190  0.579   22.427 1.00 43.68  ? 232 LEU   A CA  1 
ATOM   1180 C C   . LEU   A 1 158 ? -0.794  1.839   23.025 1.00 41.53  ? 232 LEU   A C   1 
ATOM   1181 O O   . LEU   A 1 158 ? -1.688  1.737   23.870 1.00 50.83  ? 232 LEU   A O   1 
ATOM   1182 C CB  . LEU   A 1 158 ? 0.091   -0.419  23.556 1.00 41.72  ? 232 LEU   A CB  1 
ATOM   1183 C CG  . LEU   A 1 158 ? 0.227   -1.883  23.134 1.00 45.64  ? 232 LEU   A CG  1 
ATOM   1184 C CD1 . LEU   A 1 158 ? 0.505   -2.739  24.349 1.00 46.75  ? 232 LEU   A CD1 1 
ATOM   1185 C CD2 . LEU   A 1 158 ? -1.027  -2.358  22.410 1.00 46.80  ? 232 LEU   A CD2 1 
ATOM   1186 N N   . ASP   A 1 159 ? -0.355  3.025   22.604 1.00 46.55  ? 233 ASP   A N   1 
ATOM   1187 C CA  . ASP   A 1 159 ? -0.894  4.265   23.153 1.00 40.92  ? 233 ASP   A CA  1 
ATOM   1188 C C   . ASP   A 1 159 ? -0.821  5.376   22.115 1.00 45.33  ? 233 ASP   A C   1 
ATOM   1189 O O   . ASP   A 1 159 ? -0.564  6.538   22.448 1.00 46.67  ? 233 ASP   A O   1 
ATOM   1190 C CB  . ASP   A 1 159 ? -0.156  4.686   24.425 1.00 46.26  ? 233 ASP   A CB  1 
ATOM   1191 C CG  . ASP   A 1 159 ? -1.031  5.503   25.365 1.00 50.59  ? 233 ASP   A CG  1 
ATOM   1192 O OD1 . ASP   A 1 159 ? -2.270  5.353   25.288 1.00 56.77  ? 233 ASP   A OD1 1 
ATOM   1193 O OD2 . ASP   A 1 159 ? -0.490  6.290   26.179 1.00 48.39  ? 233 ASP   A OD2 1 
ATOM   1194 N N   . VAL   A 1 160 ? -1.024  5.032   20.845 1.00 42.60  ? 234 VAL   A N   1 
ATOM   1195 C CA  . VAL   A 1 160 ? -1.057  6.048   19.800 1.00 40.41  ? 234 VAL   A CA  1 
ATOM   1196 C C   . VAL   A 1 160 ? -2.321  6.880   19.966 1.00 41.92  ? 234 VAL   A C   1 
ATOM   1197 O O   . VAL   A 1 160 ? -3.438  6.355   19.902 1.00 47.77  ? 234 VAL   A O   1 
ATOM   1198 C CB  . VAL   A 1 160 ? -1.003  5.415   18.408 1.00 37.74  ? 234 VAL   A CB  1 
ATOM   1199 C CG1 . VAL   A 1 160 ? -1.202  6.488   17.360 1.00 40.52  ? 234 VAL   A CG1 1 
ATOM   1200 C CG2 . VAL   A 1 160 ? 0.314   4.691   18.196 1.00 42.63  ? 234 VAL   A CG2 1 
ATOM   1201 N N   . LYS   A 1 161 ? -2.151  8.178   20.180 1.00 41.37  ? 235 LYS   A N   1 
ATOM   1202 C CA  . LYS   A 1 161 ? -3.268  9.099   20.337 1.00 40.11  ? 235 LYS   A CA  1 
ATOM   1203 C C   . LYS   A 1 161 ? -2.727  10.520  20.242 1.00 41.96  ? 235 LYS   A C   1 
ATOM   1204 O O   . LYS   A 1 161 ? -1.515  10.729  20.372 1.00 41.54  ? 235 LYS   A O   1 
ATOM   1205 C CB  . LYS   A 1 161 ? -3.994  8.881   21.676 1.00 43.98  ? 235 LYS   A CB  1 
ATOM   1206 C CG  . LYS   A 1 161 ? -3.139  9.119   22.898 1.00 42.49  ? 235 LYS   A CG  1 
ATOM   1207 C CD  . LYS   A 1 161 ? -3.959  8.937   24.164 1.00 48.07  ? 235 LYS   A CD  1 
ATOM   1208 C CE  . LYS   A 1 161 ? -3.056  8.776   25.378 1.00 55.30  ? 235 LYS   A CE  1 
ATOM   1209 N NZ  . LYS   A 1 161 ? -3.824  8.478   26.619 1.00 57.97  ? 235 LYS   A NZ  1 
ATOM   1210 N N   . PRO   A 1 162 ? -3.604  11.506  20.005 1.00 45.98  ? 236 PRO   A N   1 
ATOM   1211 C CA  . PRO   A 1 162 ? -3.123  12.891  19.845 1.00 42.51  ? 236 PRO   A CA  1 
ATOM   1212 C C   . PRO   A 1 162 ? -2.208  13.362  20.957 1.00 45.23  ? 236 PRO   A C   1 
ATOM   1213 O O   . PRO   A 1 162 ? -1.207  14.033  20.675 1.00 45.74  ? 236 PRO   A O   1 
ATOM   1214 C CB  . PRO   A 1 162 ? -4.425  13.696  19.801 1.00 45.56  ? 236 PRO   A CB  1 
ATOM   1215 C CG  . PRO   A 1 162 ? -5.401  12.765  19.163 1.00 44.86  ? 236 PRO   A CG  1 
ATOM   1216 C CD  . PRO   A 1 162 ? -5.038  11.385  19.670 1.00 47.48  ? 236 PRO   A CD  1 
ATOM   1217 N N   . ALA   A 1 163 ? -2.512  13.015  22.213 1.00 42.62  ? 237 ALA   A N   1 
ATOM   1218 C CA  . ALA   A 1 163 ? -1.704  13.484  23.330 1.00 40.75  ? 237 ALA   A CA  1 
ATOM   1219 C C   . ALA   A 1 163 ? -0.288  12.934  23.302 1.00 43.23  ? 237 ALA   A C   1 
ATOM   1220 O O   . ALA   A 1 163 ? 0.587   13.473  23.987 1.00 42.21  ? 237 ALA   A O   1 
ATOM   1221 C CB  . ALA   A 1 163 ? -2.361  13.100  24.658 1.00 43.32  ? 237 ALA   A CB  1 
ATOM   1222 N N   . ASN   A 1 164 ? -0.041  11.870  22.544 1.00 46.01  ? 238 ASN   A N   1 
ATOM   1223 C CA  . ASN   A 1 164 ? 1.273   11.248  22.498 1.00 43.86  ? 238 ASN   A CA  1 
ATOM   1224 C C   . ASN   A 1 164 ? 1.971   11.476  21.163 1.00 41.34  ? 238 ASN   A C   1 
ATOM   1225 O O   . ASN   A 1 164 ? 3.001   10.848  20.894 1.00 39.45  ? 238 ASN   A O   1 
ATOM   1226 C CB  . ASN   A 1 164 ? 1.159   9.753   22.809 1.00 40.43  ? 238 ASN   A CB  1 
ATOM   1227 C CG  . ASN   A 1 164 ? 0.745   9.487   24.248 1.00 45.59  ? 238 ASN   A CG  1 
ATOM   1228 O OD1 . ASN   A 1 164 ? 0.899   10.346  25.124 1.00 46.69  ? 238 ASN   A OD1 1 
ATOM   1229 N ND2 . ASN   A 1 164 ? 0.225   8.290   24.504 1.00 45.88  ? 238 ASN   A ND2 1 
ATOM   1230 N N   . ILE   A 1 165 ? 1.442   12.363  20.326 1.00 43.99  ? 239 ILE   A N   1 
ATOM   1231 C CA  . ILE   A 1 165 ? 2.123   12.824  19.121 1.00 39.17  ? 239 ILE   A CA  1 
ATOM   1232 C C   . ILE   A 1 165 ? 2.495   14.285  19.324 1.00 45.66  ? 239 ILE   A C   1 
ATOM   1233 O O   . ILE   A 1 165 ? 1.666   15.083  19.782 1.00 44.53  ? 239 ILE   A O   1 
ATOM   1234 C CB  . ILE   A 1 165 ? 1.247   12.651  17.875 1.00 41.28  ? 239 ILE   A CB  1 
ATOM   1235 C CG1 . ILE   A 1 165 ? 0.831   11.189  17.724 1.00 42.71  ? 239 ILE   A CG1 1 
ATOM   1236 C CG2 . ILE   A 1 165 ? 1.995   13.126  16.649 1.00 38.62  ? 239 ILE   A CG2 1 
ATOM   1237 C CD1 . ILE   A 1 165 ? -0.156  10.964  16.612 1.00 44.19  ? 239 ILE   A CD1 1 
ATOM   1238 N N   . PHE   A 1 166 ? 3.735   14.639  18.988 1.00 45.19  ? 240 PHE   A N   1 
ATOM   1239 C CA  . PHE   A 1 166 ? 4.255   15.973  19.257 1.00 42.23  ? 240 PHE   A CA  1 
ATOM   1240 C C   . PHE   A 1 166 ? 4.760   16.629  17.981 1.00 47.65  ? 240 PHE   A C   1 
ATOM   1241 O O   . PHE   A 1 166 ? 5.445   15.998  17.169 1.00 46.26  ? 240 PHE   A O   1 
ATOM   1242 C CB  . PHE   A 1 166 ? 5.363   15.913  20.290 1.00 42.35  ? 240 PHE   A CB  1 
ATOM   1243 C CG  . PHE   A 1 166 ? 4.930   15.289  21.577 1.00 43.77  ? 240 PHE   A CG  1 
ATOM   1244 C CD1 . PHE   A 1 166 ? 5.010   13.919  21.753 1.00 38.53  ? 240 PHE   A CD1 1 
ATOM   1245 C CD2 . PHE   A 1 166 ? 4.420   16.068  22.599 1.00 43.83  ? 240 PHE   A CD2 1 
ATOM   1246 C CE1 . PHE   A 1 166 ? 4.605   13.334  22.933 1.00 43.76  ? 240 PHE   A CE1 1 
ATOM   1247 C CE2 . PHE   A 1 166 ? 4.011   15.490  23.786 1.00 45.21  ? 240 PHE   A CE2 1 
ATOM   1248 C CZ  . PHE   A 1 166 ? 4.105   14.118  23.952 1.00 43.90  ? 240 PHE   A CZ  1 
ATOM   1249 N N   . LEU   A 1 167 ? 4.433   17.906  17.827 1.00 46.42  ? 241 LEU   A N   1 
ATOM   1250 C CA  . LEU   A 1 167 ? 4.755   18.628  16.610 1.00 48.70  ? 241 LEU   A CA  1 
ATOM   1251 C C   . LEU   A 1 167 ? 6.256   18.869  16.486 1.00 52.42  ? 241 LEU   A C   1 
ATOM   1252 O O   . LEU   A 1 167 ? 6.978   18.996  17.479 1.00 51.92  ? 241 LEU   A O   1 
ATOM   1253 C CB  . LEU   A 1 167 ? 4.013   19.960  16.579 1.00 46.91  ? 241 LEU   A CB  1 
ATOM   1254 C CG  . LEU   A 1 167 ? 2.633   19.992  15.920 1.00 49.52  ? 241 LEU   A CG  1 
ATOM   1255 C CD1 . LEU   A 1 167 ? 1.706   18.941  16.494 1.00 44.48  ? 241 LEU   A CD1 1 
ATOM   1256 C CD2 . LEU   A 1 167 ? 2.032   21.378  16.079 1.00 50.38  ? 241 LEU   A CD2 1 
ATOM   1257 N N   . GLY   A 1 168 ? 6.721   18.917  15.241 1.00 51.10  ? 242 GLY   A N   1 
ATOM   1258 C CA  . GLY   A 1 168 ? 8.074   19.307  14.931 1.00 52.79  ? 242 GLY   A CA  1 
ATOM   1259 C C   . GLY   A 1 168 ? 8.085   20.517  14.018 1.00 53.88  ? 242 GLY   A C   1 
ATOM   1260 O O   . GLY   A 1 168 ? 7.033   20.999  13.579 1.00 52.26  ? 242 GLY   A O   1 
ATOM   1261 N N   . PRO   A 1 169 ? 9.268   21.040  13.719 1.00 52.41  ? 243 PRO   A N   1 
ATOM   1262 C CA  . PRO   A 1 169 ? 9.343   22.227  12.863 1.00 53.41  ? 243 PRO   A CA  1 
ATOM   1263 C C   . PRO   A 1 169 ? 8.870   21.914  11.452 1.00 52.95  ? 243 PRO   A C   1 
ATOM   1264 O O   . PRO   A 1 169 ? 8.893   20.768  10.996 1.00 56.88  ? 243 PRO   A O   1 
ATOM   1265 C CB  . PRO   A 1 169 ? 10.833  22.597  12.887 1.00 55.87  ? 243 PRO   A CB  1 
ATOM   1266 C CG  . PRO   A 1 169 ? 11.394  21.881  14.099 1.00 53.91  ? 243 PRO   A CG  1 
ATOM   1267 C CD  . PRO   A 1 169 ? 10.597  20.615  14.193 1.00 50.75  ? 243 PRO   A CD  1 
ATOM   1268 N N   . ARG   A 1 170 ? 8.413   22.964  10.770 1.00 54.54  ? 244 ARG   A N   1 
ATOM   1269 C CA  . ARG   A 1 170 ? 7.953   22.885  9.384  1.00 55.38  ? 244 ARG   A CA  1 
ATOM   1270 C C   . ARG   A 1 170 ? 6.926   21.773  9.187  1.00 58.83  ? 244 ARG   A C   1 
ATOM   1271 O O   . ARG   A 1 170 ? 7.003   20.979  8.248  1.00 55.89  ? 244 ARG   A O   1 
ATOM   1272 C CB  . ARG   A 1 170 ? 9.133   22.711  8.439  1.00 53.57  ? 244 ARG   A CB  1 
ATOM   1273 C CG  . ARG   A 1 170 ? 10.168  23.778  8.628  1.00 57.78  ? 244 ARG   A CG  1 
ATOM   1274 C CD  . ARG   A 1 170 ? 11.210  23.721  7.547  1.00 62.11  ? 244 ARG   A CD  1 
ATOM   1275 N NE  . ARG   A 1 170 ? 12.315  24.629  7.826  1.00 74.47  ? 244 ARG   A NE  1 
ATOM   1276 C CZ  . ARG   A 1 170 ? 13.294  24.371  8.684  1.00 76.58  ? 244 ARG   A CZ  1 
ATOM   1277 N NH1 . ARG   A 1 170 ? 13.307  23.256  9.404  1.00 67.73  ? 244 ARG   A NH1 1 
ATOM   1278 N NH2 . ARG   A 1 170 ? 14.286  25.249  8.821  1.00 73.46  ? 244 ARG   A NH2 1 
ATOM   1279 N N   . GLY   A 1 171 ? 5.953   21.718  10.094 1.00 53.62  ? 245 GLY   A N   1 
ATOM   1280 C CA  . GLY   A 1 171 ? 4.820   20.840  9.895  1.00 49.72  ? 245 GLY   A CA  1 
ATOM   1281 C C   . GLY   A 1 171 ? 5.078   19.368  10.109 1.00 56.32  ? 245 GLY   A C   1 
ATOM   1282 O O   . GLY   A 1 171 ? 4.219   18.553  9.757  1.00 59.52  ? 245 GLY   A O   1 
ATOM   1283 N N   . ARG   A 1 172 ? 6.225   18.994  10.671 1.00 57.59  ? 246 ARG   A N   1 
ATOM   1284 C CA  . ARG   A 1 172 ? 6.479   17.600  11.003 1.00 57.59  ? 246 ARG   A CA  1 
ATOM   1285 C C   . ARG   A 1 172 ? 5.884   17.269  12.373 1.00 54.11  ? 246 ARG   A C   1 
ATOM   1286 O O   . ARG   A 1 172 ? 5.465   18.151  13.127 1.00 54.02  ? 246 ARG   A O   1 
ATOM   1287 C CB  . ARG   A 1 172 ? 7.982   17.311  10.998 1.00 55.95  ? 246 ARG   A CB  1 
ATOM   1288 C CG  . ARG   A 1 172 ? 8.721   17.794  9.756  1.00 56.77  ? 246 ARG   A CG  1 
ATOM   1289 C CD  . ARG   A 1 172 ? 8.186   17.123  8.502  1.00 61.33  ? 246 ARG   A CD  1 
ATOM   1290 N NE  . ARG   A 1 172 ? 8.103   15.675  8.657  1.00 65.70  ? 246 ARG   A NE  1 
ATOM   1291 C CZ  . ARG   A 1 172 ? 9.079   14.827  8.358  1.00 69.32  ? 246 ARG   A CZ  1 
ATOM   1292 N NH1 . ARG   A 1 172 ? 10.238  15.248  7.876  1.00 67.81  ? 246 ARG   A NH1 1 
ATOM   1293 N NH2 . ARG   A 1 172 ? 8.886   13.523  8.545  1.00 65.55  ? 246 ARG   A NH2 1 
ATOM   1294 N N   . CYS   A 1 173 ? 5.849   15.979  12.699 1.00 50.68  ? 247 CYS   A N   1 
ATOM   1295 C CA  . CYS   A 1 173 ? 5.505   15.568  14.054 1.00 55.19  ? 247 CYS   A CA  1 
ATOM   1296 C C   . CYS   A 1 173 ? 6.243   14.279  14.389 1.00 47.63  ? 247 CYS   A C   1 
ATOM   1297 O O   . CYS   A 1 173 ? 6.730   13.570  13.505 1.00 45.44  ? 247 CYS   A O   1 
ATOM   1298 C CB  . CYS   A 1 173 ? 3.995   15.386  14.237 1.00 50.18  ? 247 CYS   A CB  1 
ATOM   1299 S SG  . CYS   A 1 173 ? 3.328   13.979  13.334 1.00 59.93  ? 247 CYS   A SG  1 
ATOM   1300 N N   . LYS   A 1 174 ? 6.322   13.990  15.686 1.00 46.26  ? 248 LYS   A N   1 
ATOM   1301 C CA  . LYS   A 1 174 ? 7.090   12.874  16.216 1.00 46.55  ? 248 LYS   A CA  1 
ATOM   1302 C C   . LYS   A 1 174 ? 6.238   12.093  17.204 1.00 42.28  ? 248 LYS   A C   1 
ATOM   1303 O O   . LYS   A 1 174 ? 5.513   12.685  18.006 1.00 44.15  ? 248 LYS   A O   1 
ATOM   1304 C CB  . LYS   A 1 174 ? 8.370   13.367  16.917 1.00 49.87  ? 248 LYS   A CB  1 
ATOM   1305 C CG  . LYS   A 1 174 ? 9.289   14.199  16.031 1.00 55.39  ? 248 LYS   A CG  1 
ATOM   1306 C CD  . LYS   A 1 174 ? 10.608  14.521  16.729 1.00 61.15  ? 248 LYS   A CD  1 
ATOM   1307 C CE  . LYS   A 1 174 ? 10.824  16.032  16.850 1.00 69.05  ? 248 LYS   A CE  1 
ATOM   1308 N NZ  . LYS   A 1 174 ? 9.749   16.701  17.653 1.00 61.98  ? 248 LYS   A NZ  1 
ATOM   1309 N N   . LEU   A 1 175 ? 6.332   10.767  17.150 1.00 42.93  ? 249 LEU   A N   1 
ATOM   1310 C CA  . LEU   A 1 175 ? 5.610   9.919   18.090 1.00 39.52  ? 249 LEU   A CA  1 
ATOM   1311 C C   . LEU   A 1 175 ? 6.352   9.850   19.418 1.00 42.69  ? 249 LEU   A C   1 
ATOM   1312 O O   . LEU   A 1 175 ? 7.584   9.785   19.452 1.00 46.24  ? 249 LEU   A O   1 
ATOM   1313 C CB  . LEU   A 1 175 ? 5.437   8.518   17.508 1.00 46.46  ? 249 LEU   A CB  1 
ATOM   1314 C CG  . LEU   A 1 175 ? 4.659   7.474   18.313 1.00 46.60  ? 249 LEU   A CG  1 
ATOM   1315 C CD1 . LEU   A 1 175 ? 3.241   7.928   18.593 1.00 39.86  ? 249 LEU   A CD1 1 
ATOM   1316 C CD2 . LEU   A 1 175 ? 4.647   6.167   17.555 1.00 44.89  ? 249 LEU   A CD2 1 
ATOM   1317 N N   . GLY   A 1 176 ? 5.601   9.856   20.519 1.00 42.38  ? 250 GLY   A N   1 
ATOM   1318 C CA  . GLY   A 1 176 ? 6.227   9.851   21.829 1.00 42.75  ? 250 GLY   A CA  1 
ATOM   1319 C C   . GLY   A 1 176 ? 5.527   9.003   22.873 1.00 41.23  ? 250 GLY   A C   1 
ATOM   1320 O O   . GLY   A 1 176 ? 4.746   8.110   22.537 1.00 39.52  ? 250 GLY   A O   1 
ATOM   1321 N N   . ASP   A 1 177 ? 5.808   9.290   24.148 1.00 46.09  ? 251 ASP   A N   1 
ATOM   1322 C CA  . ASP   A 1 177 ? 5.274   8.568   25.303 1.00 43.73  ? 251 ASP   A CA  1 
ATOM   1323 C C   . ASP   A 1 177 ? 5.326   7.058   25.111 1.00 43.62  ? 251 ASP   A C   1 
ATOM   1324 O O   . ASP   A 1 177 ? 4.325   6.438   24.736 1.00 49.01  ? 251 ASP   A O   1 
ATOM   1325 C CB  . ASP   A 1 177 ? 3.838   9.002   25.603 1.00 51.65  ? 251 ASP   A CB  1 
ATOM   1326 C CG  . ASP   A 1 177 ? 3.447   8.750   27.054 1.00 59.03  ? 251 ASP   A CG  1 
ATOM   1327 O OD1 . ASP   A 1 177 ? 4.068   7.858   27.681 1.00 56.50  ? 251 ASP   A OD1 1 
ATOM   1328 O OD2 . ASP   A 1 177 ? 2.530   9.445   27.566 1.00 60.67  ? 251 ASP   A OD2 1 
ATOM   1329 N N   . PHE   A 1 178 ? 6.484   6.458   25.380 1.00 46.02  ? 252 PHE   A N   1 
ATOM   1330 C CA  . PHE   A 1 178 ? 6.701   5.028   25.199 1.00 43.55  ? 252 PHE   A CA  1 
ATOM   1331 C C   . PHE   A 1 178 ? 6.518   4.253   26.497 1.00 44.40  ? 252 PHE   A C   1 
ATOM   1332 O O   . PHE   A 1 178 ? 7.093   3.174   26.667 1.00 48.06  ? 252 PHE   A O   1 
ATOM   1333 C CB  . PHE   A 1 178 ? 8.094   4.785   24.616 1.00 43.47  ? 252 PHE   A CB  1 
ATOM   1334 C CG  . PHE   A 1 178 ? 8.281   5.369   23.240 1.00 45.44  ? 252 PHE   A CG  1 
ATOM   1335 C CD1 . PHE   A 1 178 ? 7.369   5.105   22.232 1.00 46.84  ? 252 PHE   A CD1 1 
ATOM   1336 C CD2 . PHE   A 1 178 ? 9.350   6.198   22.962 1.00 47.31  ? 252 PHE   A CD2 1 
ATOM   1337 C CE1 . PHE   A 1 178 ? 7.531   5.642   20.965 1.00 45.21  ? 252 PHE   A CE1 1 
ATOM   1338 C CE2 . PHE   A 1 178 ? 9.514   6.743   21.701 1.00 47.26  ? 252 PHE   A CE2 1 
ATOM   1339 C CZ  . PHE   A 1 178 ? 8.604   6.464   20.703 1.00 46.92  ? 252 PHE   A CZ  1 
ATOM   1340 N N   . GLY   A 1 179 ? 5.727   4.792   27.424 1.00 43.36  ? 253 GLY   A N   1 
ATOM   1341 C CA  . GLY   A 1 179 ? 5.551   4.130   28.704 1.00 44.50  ? 253 GLY   A CA  1 
ATOM   1342 C C   . GLY   A 1 179 ? 4.773   2.834   28.612 1.00 48.09  ? 253 GLY   A C   1 
ATOM   1343 O O   . GLY   A 1 179 ? 4.935   1.955   29.461 1.00 53.33  ? 253 GLY   A O   1 
ATOM   1344 N N   . LEU   A 1 180 ? 3.918   2.697   27.596 1.00 41.64  ? 254 LEU   A N   1 
ATOM   1345 C CA  . LEU   A 1 180 ? 3.096   1.505   27.413 1.00 48.07  ? 254 LEU   A CA  1 
ATOM   1346 C C   . LEU   A 1 180 ? 3.649   0.557   26.366 1.00 49.71  ? 254 LEU   A C   1 
ATOM   1347 O O   . LEU   A 1 180 ? 3.027   -0.475  26.096 1.00 49.32  ? 254 LEU   A O   1 
ATOM   1348 C CB  . LEU   A 1 180 ? 1.661   1.884   27.017 1.00 50.14  ? 254 LEU   A CB  1 
ATOM   1349 C CG  . LEU   A 1 180 ? 0.756   2.589   28.032 1.00 47.55  ? 254 LEU   A CG  1 
ATOM   1350 C CD1 . LEU   A 1 180 ? -0.705  2.413   27.652 1.00 49.45  ? 254 LEU   A CD1 1 
ATOM   1351 C CD2 . LEU   A 1 180 ? 1.014   2.077   29.429 1.00 56.46  ? 254 LEU   A CD2 1 
ATOM   1352 N N   . LEU   A 1 181 ? 4.788   0.881   25.768 1.00 50.92  ? 255 LEU   A N   1 
ATOM   1353 C CA  . LEU   A 1 181 ? 5.316   0.068   24.685 1.00 49.20  ? 255 LEU   A CA  1 
ATOM   1354 C C   . LEU   A 1 181 ? 5.696   -1.317  25.199 1.00 51.73  ? 255 LEU   A C   1 
ATOM   1355 O O   . LEU   A 1 181 ? 6.218   -1.467  26.306 1.00 51.63  ? 255 LEU   A O   1 
ATOM   1356 C CB  . LEU   A 1 181 ? 6.517   0.771   24.050 1.00 44.15  ? 255 LEU   A CB  1 
ATOM   1357 C CG  . LEU   A 1 181 ? 7.260   0.121   22.886 1.00 47.74  ? 255 LEU   A CG  1 
ATOM   1358 C CD1 . LEU   A 1 181 ? 7.829   1.192   21.975 1.00 43.93  ? 255 LEU   A CD1 1 
ATOM   1359 C CD2 . LEU   A 1 181 ? 8.377   -0.772  23.401 1.00 46.68  ? 255 LEU   A CD2 1 
ATOM   1360 N N   . VAL   A 1 182 ? 5.405   -2.339  24.394 1.00 51.79  ? 256 VAL   A N   1 
ATOM   1361 C CA  . VAL   A 1 182 ? 5.772   -3.710  24.716 1.00 51.92  ? 256 VAL   A CA  1 
ATOM   1362 C C   . VAL   A 1 182 ? 6.548   -4.283  23.543 1.00 54.75  ? 256 VAL   A C   1 
ATOM   1363 O O   . VAL   A 1 182 ? 6.479   -3.787  22.417 1.00 55.43  ? 256 VAL   A O   1 
ATOM   1364 C CB  . VAL   A 1 182 ? 4.551   -4.606  25.031 1.00 53.51  ? 256 VAL   A CB  1 
ATOM   1365 C CG1 . VAL   A 1 182 ? 3.858   -4.141  26.296 1.00 63.26  ? 256 VAL   A CG1 1 
ATOM   1366 C CG2 . VAL   A 1 182 ? 3.585   -4.613  23.864 1.00 53.82  ? 256 VAL   A CG2 1 
ATOM   1367 N N   . GLU   A 1 183 ? 7.288   -5.348  23.823 1.00 59.32  ? 257 GLU   A N   1 
ATOM   1368 C CA  . GLU   A 1 183 ? 8.066   -6.063  22.824 1.00 60.45  ? 257 GLU   A CA  1 
ATOM   1369 C C   . GLU   A 1 183 ? 7.463   -7.451  22.658 1.00 63.54  ? 257 GLU   A C   1 
ATOM   1370 O O   . GLU   A 1 183 ? 7.360   -8.206  23.631 1.00 64.44  ? 257 GLU   A O   1 
ATOM   1371 C CB  . GLU   A 1 183 ? 9.533   -6.150  23.241 1.00 61.91  ? 257 GLU   A CB  1 
ATOM   1372 C CG  . GLU   A 1 183 ? 10.449  -6.760  22.194 1.00 66.94  ? 257 GLU   A CG  1 
ATOM   1373 C CD  . GLU   A 1 183 ? 11.890  -6.827  22.665 1.00 78.94  ? 257 GLU   A CD  1 
ATOM   1374 O OE1 . GLU   A 1 183 ? 12.154  -6.408  23.813 1.00 81.42  ? 257 GLU   A OE1 1 
ATOM   1375 O OE2 . GLU   A 1 183 ? 12.757  -7.297  21.894 1.00 81.23  ? 257 GLU   A OE2 1 
ATOM   1376 N N   . LEU   A 1 184 ? 7.057   -7.780  21.436 1.00 63.01  ? 258 LEU   A N   1 
ATOM   1377 C CA  . LEU   A 1 184 ? 6.443   -9.074  21.183 1.00 62.57  ? 258 LEU   A CA  1 
ATOM   1378 C C   . LEU   A 1 184 ? 7.463   -10.189 21.386 1.00 66.73  ? 258 LEU   A C   1 
ATOM   1379 O O   . LEU   A 1 184 ? 8.591   -10.111 20.891 1.00 68.85  ? 258 LEU   A O   1 
ATOM   1380 C CB  . LEU   A 1 184 ? 5.874   -9.111  19.768 1.00 61.22  ? 258 LEU   A CB  1 
ATOM   1381 C CG  . LEU   A 1 184 ? 4.881   -7.989  19.464 1.00 64.49  ? 258 LEU   A CG  1 
ATOM   1382 C CD1 . LEU   A 1 184 ? 4.500   -7.991  17.993 1.00 62.54  ? 258 LEU   A CD1 1 
ATOM   1383 C CD2 . LEU   A 1 184 ? 3.644   -8.112  20.347 1.00 58.84  ? 258 LEU   A CD2 1 
ATOM   1384 N N   . GLY   A 1 185 ? 7.071   -11.223 22.124 1.00 69.02  ? 259 GLY   A N   1 
ATOM   1385 C CA  . GLY   A 1 185 ? 7.963   -12.333 22.402 1.00 70.77  ? 259 GLY   A CA  1 
ATOM   1386 C C   . GLY   A 1 185 ? 7.531   -13.161 23.596 1.00 85.52  ? 259 GLY   A C   1 
ATOM   1387 O O   . GLY   A 1 185 ? 7.769   -14.372 23.642 1.00 93.66  ? 259 GLY   A O   1 
ATOM   1388 N N   . GLU   A 1 191 ? 2.538   -8.174  31.299 1.00 89.06  ? 265 GLU   A N   1 
ATOM   1389 C CA  . GLU   A 1 191 ? 3.504   -7.457  30.469 1.00 90.12  ? 265 GLU   A CA  1 
ATOM   1390 C C   . GLU   A 1 191 ? 2.878   -6.236  29.789 1.00 78.89  ? 265 GLU   A C   1 
ATOM   1391 O O   . GLU   A 1 191 ? 3.583   -5.311  29.384 1.00 74.33  ? 265 GLU   A O   1 
ATOM   1392 C CB  . GLU   A 1 191 ? 4.104   -8.399  29.416 1.00 95.82  ? 265 GLU   A CB  1 
ATOM   1393 C CG  . GLU   A 1 191 ? 3.088   -9.035  28.472 1.00 92.46  ? 265 GLU   A CG  1 
ATOM   1394 C CD  . GLU   A 1 191 ? 3.730   -9.998  27.483 1.00 96.93  ? 265 GLU   A CD  1 
ATOM   1395 O OE1 . GLU   A 1 191 ? 4.897   -10.392 27.706 1.00 98.60  ? 265 GLU   A OE1 1 
ATOM   1396 O OE2 . GLU   A 1 191 ? 3.069   -10.356 26.483 1.00 91.27  ? 265 GLU   A OE2 1 
ATOM   1397 N N   . VAL   A 1 192 ? 1.552   -6.239  29.674 1.00 79.60  ? 266 VAL   A N   1 
ATOM   1398 C CA  . VAL   A 1 192 ? 0.810   -5.177  29.004 1.00 71.56  ? 266 VAL   A CA  1 
ATOM   1399 C C   . VAL   A 1 192 ? -0.006  -4.416  30.041 1.00 73.02  ? 266 VAL   A C   1 
ATOM   1400 O O   . VAL   A 1 192 ? -0.473  -4.985  31.036 1.00 73.09  ? 266 VAL   A O   1 
ATOM   1401 C CB  . VAL   A 1 192 ? -0.099  -5.742  27.892 1.00 67.29  ? 266 VAL   A CB  1 
ATOM   1402 C CG1 . VAL   A 1 192 ? -0.845  -4.630  27.180 1.00 67.19  ? 266 VAL   A CG1 1 
ATOM   1403 C CG2 . VAL   A 1 192 ? 0.722   -6.544  26.902 1.00 71.71  ? 266 VAL   A CG2 1 
ATOM   1404 N N   . GLN   A 1 193 ? -0.172  -3.119  29.805 1.00 68.02  ? 267 GLN   A N   1 
ATOM   1405 C CA  . GLN   A 1 193 ? -0.948  -2.253  30.677 1.00 62.99  ? 267 GLN   A CA  1 
ATOM   1406 C C   . GLN   A 1 193 ? -2.195  -1.750  29.962 1.00 63.62  ? 267 GLN   A C   1 
ATOM   1407 O O   . GLN   A 1 193 ? -2.338  -1.863  28.739 1.00 54.13  ? 267 GLN   A O   1 
ATOM   1408 C CB  . GLN   A 1 193 ? -0.103  -1.073  31.152 1.00 63.26  ? 267 GLN   A CB  1 
ATOM   1409 C CG  . GLN   A 1 193 ? 1.226   -1.481  31.739 1.00 66.14  ? 267 GLN   A CG  1 
ATOM   1410 C CD  . GLN   A 1 193 ? 2.118   -0.290  31.983 1.00 74.25  ? 267 GLN   A CD  1 
ATOM   1411 O OE1 . GLN   A 1 193 ? 1.970   0.417   32.981 1.00 84.51  ? 267 GLN   A OE1 1 
ATOM   1412 N NE2 . GLN   A 1 193 ? 3.043   -0.046  31.060 1.00 69.04  ? 267 GLN   A NE2 1 
ATOM   1413 N N   . GLU   A 1 194 ? -3.097  -1.175  30.758 1.00 64.09  ? 268 GLU   A N   1 
ATOM   1414 C CA  . GLU   A 1 194 ? -4.363  -0.661  30.248 1.00 62.93  ? 268 GLU   A CA  1 
ATOM   1415 C C   . GLU   A 1 194 ? -4.123  0.519   29.315 1.00 59.12  ? 268 GLU   A C   1 
ATOM   1416 O O   . GLU   A 1 194 ? -3.582  1.548   29.734 1.00 61.86  ? 268 GLU   A O   1 
ATOM   1417 C CB  . GLU   A 1 194 ? -5.261  -0.235  31.407 1.00 65.10  ? 268 GLU   A CB  1 
ATOM   1418 C CG  . GLU   A 1 194 ? -5.623  -1.349  32.378 1.00 70.29  ? 268 GLU   A CG  1 
ATOM   1419 C CD  . GLU   A 1 194 ? -6.650  -2.323  31.815 1.00 74.36  ? 268 GLU   A CD  1 
ATOM   1420 O OE1 . GLU   A 1 194 ? -7.112  -2.120  30.667 1.00 70.71  ? 268 GLU   A OE1 1 
ATOM   1421 O OE2 . GLU   A 1 194 ? -6.996  -3.294  32.530 1.00 76.71  ? 268 GLU   A OE2 1 
ATOM   1422 N N   . GLY   A 1 195 ? -4.532  0.376   28.056 1.00 62.68  ? 269 GLY   A N   1 
ATOM   1423 C CA  . GLY   A 1 195 ? -4.479  1.474   27.116 1.00 59.77  ? 269 GLY   A CA  1 
ATOM   1424 C C   . GLY   A 1 195 ? -5.708  2.359   27.220 1.00 59.80  ? 269 GLY   A C   1 
ATOM   1425 O O   . GLY   A 1 195 ? -6.625  2.125   28.009 1.00 57.18  ? 269 GLY   A O   1 
ATOM   1426 N N   . ASP   A 1 196 ? -5.716  3.407   26.407 1.00 59.09  ? 270 ASP   A N   1 
ATOM   1427 C CA  . ASP   A 1 196 ? -6.869  4.299   26.352 1.00 56.57  ? 270 ASP   A CA  1 
ATOM   1428 C C   . ASP   A 1 196 ? -7.993  3.615   25.581 1.00 51.90  ? 270 ASP   A C   1 
ATOM   1429 O O   . ASP   A 1 196 ? -7.795  3.250   24.419 1.00 52.47  ? 270 ASP   A O   1 
ATOM   1430 C CB  . ASP   A 1 196 ? -6.490  5.620   25.688 1.00 56.17  ? 270 ASP   A CB  1 
ATOM   1431 C CG  . ASP   A 1 196 ? -7.457  6.747   26.016 1.00 55.09  ? 270 ASP   A CG  1 
ATOM   1432 O OD1 . ASP   A 1 196 ? -8.667  6.481   26.167 1.00 55.83  ? 270 ASP   A OD1 1 
ATOM   1433 O OD2 . ASP   A 1 196 ? -7.003  7.908   26.124 1.00 59.45  ? 270 ASP   A OD2 1 
ATOM   1434 N N   . PRO   A 1 197 ? -9.170  3.414   26.180 1.00 51.86  ? 271 PRO   A N   1 
ATOM   1435 C CA  . PRO   A 1 197 ? -10.234 2.700   25.458 1.00 52.94  ? 271 PRO   A CA  1 
ATOM   1436 C C   . PRO   A 1 197 ? -10.754 3.456   24.251 1.00 51.76  ? 271 PRO   A C   1 
ATOM   1437 O O   . PRO   A 1 197 ? -11.199 2.820   23.287 1.00 54.55  ? 271 PRO   A O   1 
ATOM   1438 C CB  . PRO   A 1 197 ? -11.324 2.521   26.523 1.00 48.59  ? 271 PRO   A CB  1 
ATOM   1439 C CG  . PRO   A 1 197 ? -11.071 3.612   27.502 1.00 54.62  ? 271 PRO   A CG  1 
ATOM   1440 C CD  . PRO   A 1 197 ? -9.585  3.799   27.537 1.00 52.61  ? 271 PRO   A CD  1 
ATOM   1441 N N   . ARG   A 1 198 ? -10.713 4.790   24.272 1.00 51.55  ? 272 ARG   A N   1 
ATOM   1442 C CA  . ARG   A 1 198 ? -11.191 5.564   23.132 1.00 50.07  ? 272 ARG   A CA  1 
ATOM   1443 C C   . ARG   A 1 198 ? -10.474 5.174   21.850 1.00 50.61  ? 272 ARG   A C   1 
ATOM   1444 O O   . ARG   A 1 198 ? -11.086 5.171   20.776 1.00 48.67  ? 272 ARG   A O   1 
ATOM   1445 C CB  . ARG   A 1 198 ? -11.020 7.059   23.402 1.00 51.98  ? 272 ARG   A CB  1 
ATOM   1446 C CG  . ARG   A 1 198 ? -11.897 7.574   24.534 1.00 61.63  ? 272 ARG   A CG  1 
ATOM   1447 C CD  . ARG   A 1 198 ? -11.625 9.033   24.832 1.00 63.56  ? 272 ARG   A CD  1 
ATOM   1448 N NE  . ARG   A 1 198 ? -10.432 9.209   25.649 1.00 65.13  ? 272 ARG   A NE  1 
ATOM   1449 C CZ  . ARG   A 1 198 ? -9.754  10.344  25.744 1.00 72.11  ? 272 ARG   A CZ  1 
ATOM   1450 N NH1 . ARG   A 1 198 ? -10.116 11.423  25.067 1.00 74.02  ? 272 ARG   A NH1 1 
ATOM   1451 N NH2 . ARG   A 1 198 ? -8.680  10.395  26.528 1.00 71.48  ? 272 ARG   A NH2 1 
ATOM   1452 N N   . TYR   A 1 199 ? -9.192  4.821   21.944 1.00 50.84  ? 273 TYR   A N   1 
ATOM   1453 C CA  . TYR   A 1 199 ? -8.374  4.488   20.784 1.00 49.38  ? 273 TYR   A CA  1 
ATOM   1454 C C   . TYR   A 1 199 ? -8.070  2.999   20.704 1.00 49.02  ? 273 TYR   A C   1 
ATOM   1455 O O   . TYR   A 1 199 ? -7.222  2.591   19.909 1.00 51.99  ? 273 TYR   A O   1 
ATOM   1456 C CB  . TYR   A 1 199 ? -7.070  5.289   20.812 1.00 48.78  ? 273 TYR   A CB  1 
ATOM   1457 C CG  . TYR   A 1 199 ? -7.282  6.772   21.019 1.00 47.39  ? 273 TYR   A CG  1 
ATOM   1458 C CD1 . TYR   A 1 199 ? -7.384  7.303   22.297 1.00 48.30  ? 273 TYR   A CD1 1 
ATOM   1459 C CD2 . TYR   A 1 199 ? -7.396  7.638   19.939 1.00 46.14  ? 273 TYR   A CD2 1 
ATOM   1460 C CE1 . TYR   A 1 199 ? -7.587  8.650   22.497 1.00 50.09  ? 273 TYR   A CE1 1 
ATOM   1461 C CE2 . TYR   A 1 199 ? -7.598  8.995   20.130 1.00 48.79  ? 273 TYR   A CE2 1 
ATOM   1462 C CZ  . TYR   A 1 199 ? -7.695  9.493   21.417 1.00 53.13  ? 273 TYR   A CZ  1 
ATOM   1463 O OH  . TYR   A 1 199 ? -7.900  10.838  21.636 1.00 62.16  ? 273 TYR   A OH  1 
ATOM   1464 N N   . MET   A 1 200 ? -8.744  2.182   21.503 1.00 53.34  ? 274 MET   A N   1 
ATOM   1465 C CA  . MET   A 1 200 ? -8.409  0.771   21.584 1.00 52.22  ? 274 MET   A CA  1 
ATOM   1466 C C   . MET   A 1 200 ? -8.851  0.032   20.327 1.00 54.69  ? 274 MET   A C   1 
ATOM   1467 O O   . MET   A 1 200 ? -9.957  0.241   19.820 1.00 57.30  ? 274 MET   A O   1 
ATOM   1468 C CB  . MET   A 1 200 ? -9.067  0.161   22.817 1.00 52.31  ? 274 MET   A CB  1 
ATOM   1469 C CG  . MET   A 1 200 ? -8.936  -1.336  22.932 1.00 56.45  ? 274 MET   A CG  1 
ATOM   1470 S SD  . MET   A 1 200 ? -9.682  -1.892  24.472 1.00 68.62  ? 274 MET   A SD  1 
ATOM   1471 C CE  . MET   A 1 200 ? -8.701  -0.960  25.650 1.00 67.49  ? 274 MET   A CE  1 
ATOM   1472 N N   . ALA   A 1 201 ? -7.972  -0.831  19.822 1.00 53.17  ? 275 ALA   A N   1 
ATOM   1473 C CA  . ALA   A 1 201 ? -8.344  -1.720  18.731 1.00 52.86  ? 275 ALA   A CA  1 
ATOM   1474 C C   . ALA   A 1 201 ? -9.275  -2.813  19.252 1.00 58.81  ? 275 ALA   A C   1 
ATOM   1475 O O   . ALA   A 1 201 ? -9.110  -3.277  20.384 1.00 61.69  ? 275 ALA   A O   1 
ATOM   1476 C CB  . ALA   A 1 201 ? -7.101  -2.350  18.104 1.00 56.57  ? 275 ALA   A CB  1 
ATOM   1477 N N   . PRO   A 1 202 ? -10.255 -3.253  18.452 1.00 56.08  ? 276 PRO   A N   1 
ATOM   1478 C CA  . PRO   A 1 202 ? -11.240 -4.209  18.987 1.00 55.04  ? 276 PRO   A CA  1 
ATOM   1479 C C   . PRO   A 1 202 ? -10.621 -5.513  19.458 1.00 58.68  ? 276 PRO   A C   1 
ATOM   1480 O O   . PRO   A 1 202 ? -11.072 -6.074  20.466 1.00 60.58  ? 276 PRO   A O   1 
ATOM   1481 C CB  . PRO   A 1 202 ? -12.201 -4.417  17.808 1.00 55.73  ? 276 PRO   A CB  1 
ATOM   1482 C CG  . PRO   A 1 202 ? -11.400 -4.068  16.597 1.00 56.96  ? 276 PRO   A CG  1 
ATOM   1483 C CD  . PRO   A 1 202 ? -10.486 -2.956  17.028 1.00 55.92  ? 276 PRO   A CD  1 
ATOM   1484 N N   . GLU   A 1 203 ? -9.584  -6.009  18.777 1.00 60.26  ? 277 GLU   A N   1 
ATOM   1485 C CA  . GLU   A 1 203 ? -9.015  -7.295  19.163 1.00 59.46  ? 277 GLU   A CA  1 
ATOM   1486 C C   . GLU   A 1 203 ? -8.318  -7.240  20.519 1.00 59.52  ? 277 GLU   A C   1 
ATOM   1487 O O   . GLU   A 1 203 ? -8.139  -8.291  21.143 1.00 57.05  ? 277 GLU   A O   1 
ATOM   1488 C CB  . GLU   A 1 203 ? -8.047  -7.806  18.088 1.00 55.26  ? 277 GLU   A CB  1 
ATOM   1489 C CG  . GLU   A 1 203 ? -6.678  -7.131  18.072 1.00 65.51  ? 277 GLU   A CG  1 
ATOM   1490 C CD  . GLU   A 1 203 ? -6.612  -5.920  17.157 1.00 60.32  ? 277 GLU   A CD  1 
ATOM   1491 O OE1 . GLU   A 1 203 ? -7.682  -5.427  16.738 1.00 59.93  ? 277 GLU   A OE1 1 
ATOM   1492 O OE2 . GLU   A 1 203 ? -5.484  -5.467  16.852 1.00 59.61  ? 277 GLU   A OE2 1 
ATOM   1493 N N   . LEU   A 1 204 ? -7.934  -6.049  20.997 1.00 58.90  ? 278 LEU   A N   1 
ATOM   1494 C CA  . LEU   A 1 204 ? -7.331  -5.956  22.325 1.00 60.55  ? 278 LEU   A CA  1 
ATOM   1495 C C   . LEU   A 1 204 ? -8.300  -6.414  23.408 1.00 59.00  ? 278 LEU   A C   1 
ATOM   1496 O O   . LEU   A 1 204 ? -7.873  -6.892  24.466 1.00 57.58  ? 278 LEU   A O   1 
ATOM   1497 C CB  . LEU   A 1 204 ? -6.859  -4.525  22.617 1.00 62.51  ? 278 LEU   A CB  1 
ATOM   1498 C CG  . LEU   A 1 204 ? -5.648  -3.941  21.876 1.00 59.62  ? 278 LEU   A CG  1 
ATOM   1499 C CD1 . LEU   A 1 204 ? -4.981  -2.863  22.706 1.00 52.55  ? 278 LEU   A CD1 1 
ATOM   1500 C CD2 . LEU   A 1 204 ? -4.644  -5.015  21.511 1.00 61.80  ? 278 LEU   A CD2 1 
ATOM   1501 N N   . LEU   A 1 205 ? -9.604  -6.287  23.158 1.00 60.54  ? 279 LEU   A N   1 
ATOM   1502 C CA  . LEU   A 1 205 ? -10.585 -6.690  24.153 1.00 58.96  ? 279 LEU   A CA  1 
ATOM   1503 C C   . LEU   A 1 205 ? -10.565 -8.190  24.399 1.00 64.95  ? 279 LEU   A C   1 
ATOM   1504 O O   . LEU   A 1 205 ? -10.919 -8.636  25.495 1.00 69.72  ? 279 LEU   A O   1 
ATOM   1505 C CB  . LEU   A 1 205 ? -11.980 -6.253  23.724 1.00 61.87  ? 279 LEU   A CB  1 
ATOM   1506 C CG  . LEU   A 1 205 ? -12.475 -4.920  24.270 1.00 62.07  ? 279 LEU   A CG  1 
ATOM   1507 C CD1 . LEU   A 1 205 ? -13.953 -4.811  24.004 1.00 63.09  ? 279 LEU   A CD1 1 
ATOM   1508 C CD2 . LEU   A 1 205 ? -12.202 -4.818  25.756 1.00 65.50  ? 279 LEU   A CD2 1 
ATOM   1509 N N   . GLN   A 1 206 ? -10.166 -8.985  23.403 1.00 68.80  ? 280 GLN   A N   1 
ATOM   1510 C CA  . GLN   A 1 206 ? -10.102 -10.436 23.547 1.00 69.54  ? 280 GLN   A CA  1 
ATOM   1511 C C   . GLN   A 1 206 ? -8.662  -10.948 23.595 1.00 70.74  ? 280 GLN   A C   1 
ATOM   1512 O O   . GLN   A 1 206 ? -8.375  -12.055 23.137 1.00 73.08  ? 280 GLN   A O   1 
ATOM   1513 C CB  . GLN   A 1 206 ? -10.879 -11.128 22.429 1.00 72.48  ? 280 GLN   A CB  1 
ATOM   1514 C CG  . GLN   A 1 206 ? -12.387 -10.893 22.474 1.00 76.18  ? 280 GLN   A CG  1 
ATOM   1515 C CD  . GLN   A 1 206 ? -12.804 -9.654  21.700 1.00 80.16  ? 280 GLN   A CD  1 
ATOM   1516 O OE1 . GLN   A 1 206 ? -12.120 -9.237  20.762 1.00 79.79  ? 280 GLN   A OE1 1 
ATOM   1517 N NE2 . GLN   A 1 206 ? -13.927 -9.056  22.092 1.00 77.11  ? 280 GLN   A NE2 1 
ATOM   1518 N N   . GLY   A 1 207 ? -7.748  -10.150 24.144 1.00 68.42  ? 281 GLY   A N   1 
ATOM   1519 C CA  . GLY   A 1 207 ? -6.405  -10.616 24.425 1.00 68.48  ? 281 GLY   A CA  1 
ATOM   1520 C C   . GLY   A 1 207 ? -5.497  -10.791 23.230 1.00 65.70  ? 281 GLY   A C   1 
ATOM   1521 O O   . GLY   A 1 207 ? -4.443  -11.418 23.366 1.00 72.12  ? 281 GLY   A O   1 
ATOM   1522 N N   . SER   A 1 208 ? -5.859  -10.259 22.067 1.00 63.91  ? 282 SER   A N   1 
ATOM   1523 C CA  . SER   A 1 208 ? -5.046  -10.383 20.859 1.00 61.56  ? 282 SER   A CA  1 
ATOM   1524 C C   . SER   A 1 208 ? -4.200  -9.121  20.733 1.00 63.96  ? 282 SER   A C   1 
ATOM   1525 O O   . SER   A 1 208 ? -4.697  -8.064  20.337 1.00 64.44  ? 282 SER   A O   1 
ATOM   1526 C CB  . SER   A 1 208 ? -5.928  -10.598 19.633 1.00 61.87  ? 282 SER   A CB  1 
ATOM   1527 O OG  . SER   A 1 208 ? -5.149  -10.710 18.455 1.00 69.10  ? 282 SER   A OG  1 
ATOM   1528 N N   . TYR   A 1 209 ? -2.922  -9.228  21.080 1.00 64.25  ? 283 TYR   A N   1 
ATOM   1529 C CA  . TYR   A 1 209 ? -1.999  -8.104  21.031 1.00 59.54  ? 283 TYR   A CA  1 
ATOM   1530 C C   . TYR   A 1 209 ? -1.026  -8.291  19.876 1.00 59.02  ? 283 TYR   A C   1 
ATOM   1531 O O   . TYR   A 1 209 ? -0.536  -9.399  19.634 1.00 57.56  ? 283 TYR   A O   1 
ATOM   1532 C CB  . TYR   A 1 209 ? -1.237  -7.955  22.351 1.00 59.95  ? 283 TYR   A CB  1 
ATOM   1533 C CG  . TYR   A 1 209 ? -2.131  -7.632  23.533 1.00 66.14  ? 283 TYR   A CG  1 
ATOM   1534 C CD1 . TYR   A 1 209 ? -2.701  -8.646  24.302 1.00 66.84  ? 283 TYR   A CD1 1 
ATOM   1535 C CD2 . TYR   A 1 209 ? -2.408  -6.313  23.879 1.00 66.91  ? 283 TYR   A CD2 1 
ATOM   1536 C CE1 . TYR   A 1 209 ? -3.525  -8.351  25.385 1.00 69.50  ? 283 TYR   A CE1 1 
ATOM   1537 C CE2 . TYR   A 1 209 ? -3.231  -6.007  24.957 1.00 69.53  ? 283 TYR   A CE2 1 
ATOM   1538 C CZ  . TYR   A 1 209 ? -3.787  -7.029  25.708 1.00 72.70  ? 283 TYR   A CZ  1 
ATOM   1539 O OH  . TYR   A 1 209 ? -4.602  -6.724  26.781 1.00 76.10  ? 283 TYR   A OH  1 
ATOM   1540 N N   . GLY   A 1 210 ? -0.761  -7.209  19.159 1.00 58.99  ? 284 GLY   A N   1 
ATOM   1541 C CA  . GLY   A 1 210 ? 0.086   -7.280  17.985 1.00 52.58  ? 284 GLY   A CA  1 
ATOM   1542 C C   . GLY   A 1 210 ? 0.217   -5.905  17.374 1.00 51.61  ? 284 GLY   A C   1 
ATOM   1543 O O   . GLY   A 1 210 ? -0.428  -4.942  17.805 1.00 49.00  ? 284 GLY   A O   1 
ATOM   1544 N N   . THR   A 1 211 ? 1.072   -5.826  16.353 1.00 51.66  ? 285 THR   A N   1 
ATOM   1545 C CA  . THR   A 1 211 ? 1.339   -4.536  15.733 1.00 47.15  ? 285 THR   A CA  1 
ATOM   1546 C C   . THR   A 1 211 ? 0.113   -3.971  15.039 1.00 47.95  ? 285 THR   A C   1 
ATOM   1547 O O   . THR   A 1 211 ? 0.026   -2.752  14.865 1.00 50.90  ? 285 THR   A O   1 
ATOM   1548 C CB  . THR   A 1 211 ? 2.495   -4.648  14.743 1.00 48.22  ? 285 THR   A CB  1 
ATOM   1549 O OG1 . THR   A 1 211 ? 2.203   -5.671  13.785 1.00 54.06  ? 285 THR   A OG1 1 
ATOM   1550 C CG2 . THR   A 1 211 ? 3.785   -4.991  15.474 1.00 46.67  ? 285 THR   A CG2 1 
ATOM   1551 N N   . ALA   A 1 212 ? -0.839  -4.824  14.648 1.00 51.98  ? 286 ALA   A N   1 
ATOM   1552 C CA  . ALA   A 1 212 ? -2.073  -4.331  14.045 1.00 52.85  ? 286 ALA   A CA  1 
ATOM   1553 C C   . ALA   A 1 212 ? -2.763  -3.309  14.937 1.00 50.98  ? 286 ALA   A C   1 
ATOM   1554 O O   . ALA   A 1 212 ? -3.373  -2.358  14.434 1.00 52.76  ? 286 ALA   A O   1 
ATOM   1555 C CB  . ALA   A 1 212 ? -3.018  -5.497  13.751 1.00 52.52  ? 286 ALA   A CB  1 
ATOM   1556 N N   . ALA   A 1 213 ? -2.651  -3.473  16.259 1.00 52.26  ? 287 ALA   A N   1 
ATOM   1557 C CA  . ALA   A 1 213 ? -3.367  -2.602  17.186 1.00 47.44  ? 287 ALA   A CA  1 
ATOM   1558 C C   . ALA   A 1 213 ? -2.962  -1.144  17.013 1.00 51.56  ? 287 ALA   A C   1 
ATOM   1559 O O   . ALA   A 1 213 ? -3.802  -0.244  17.131 1.00 56.00  ? 287 ALA   A O   1 
ATOM   1560 C CB  . ALA   A 1 213 ? -3.126  -3.058  18.623 1.00 50.70  ? 287 ALA   A CB  1 
ATOM   1561 N N   . ASP   A 1 214 ? -1.678  -0.889  16.734 1.00 53.12  ? 288 ASP   A N   1 
ATOM   1562 C CA  . ASP   A 1 214 ? -1.211  0.482   16.538 1.00 47.81  ? 288 ASP   A CA  1 
ATOM   1563 C C   . ASP   A 1 214 ? -1.826  1.125   15.305 1.00 51.00  ? 288 ASP   A C   1 
ATOM   1564 O O   . ASP   A 1 214 ? -2.056  2.340   15.292 1.00 50.82  ? 288 ASP   A O   1 
ATOM   1565 C CB  . ASP   A 1 214 ? 0.307   0.514   16.414 1.00 47.35  ? 288 ASP   A CB  1 
ATOM   1566 C CG  . ASP   A 1 214 ? 0.992   0.322   17.727 1.00 47.97  ? 288 ASP   A CG  1 
ATOM   1567 O OD1 . ASP   A 1 214 ? 0.293   0.434   18.762 1.00 44.37  ? 288 ASP   A OD1 1 
ATOM   1568 O OD2 . ASP   A 1 214 ? 2.220   0.061   17.718 1.00 47.85  ? 288 ASP   A OD2 1 
ATOM   1569 N N   . VAL   A 1 215 ? -2.073  0.339   14.256 1.00 52.94  ? 289 VAL   A N   1 
ATOM   1570 C CA  . VAL   A 1 215 ? -2.663  0.893   13.044 1.00 50.90  ? 289 VAL   A CA  1 
ATOM   1571 C C   . VAL   A 1 215 ? -4.087  1.366   13.309 1.00 50.99  ? 289 VAL   A C   1 
ATOM   1572 O O   . VAL   A 1 215 ? -4.497  2.434   12.843 1.00 52.45  ? 289 VAL   A O   1 
ATOM   1573 C CB  . VAL   A 1 215 ? -2.610  -0.144  11.912 1.00 51.79  ? 289 VAL   A CB  1 
ATOM   1574 C CG1 . VAL   A 1 215 ? -3.209  0.431   10.650 1.00 53.28  ? 289 VAL   A CG1 1 
ATOM   1575 C CG2 . VAL   A 1 215 ? -1.172  -0.585  11.679 1.00 54.22  ? 289 VAL   A CG2 1 
ATOM   1576 N N   . PHE   A 1 216 ? -4.862  0.586   14.065 1.00 50.47  ? 290 PHE   A N   1 
ATOM   1577 C CA  . PHE   A 1 216 ? -6.217  1.006   14.397 1.00 49.73  ? 290 PHE   A CA  1 
ATOM   1578 C C   . PHE   A 1 216 ? -6.206  2.288   15.218 1.00 47.55  ? 290 PHE   A C   1 
ATOM   1579 O O   . PHE   A 1 216 ? -7.006  3.198   14.972 1.00 50.21  ? 290 PHE   A O   1 
ATOM   1580 C CB  . PHE   A 1 216 ? -6.940  -0.106  15.152 1.00 53.33  ? 290 PHE   A CB  1 
ATOM   1581 C CG  . PHE   A 1 216 ? -8.438  0.032   15.152 1.00 55.56  ? 290 PHE   A CG  1 
ATOM   1582 C CD1 . PHE   A 1 216 ? -9.086  0.727   16.160 1.00 53.65  ? 290 PHE   A CD1 1 
ATOM   1583 C CD2 . PHE   A 1 216 ? -9.197  -0.538  14.145 1.00 53.85  ? 290 PHE   A CD2 1 
ATOM   1584 C CE1 . PHE   A 1 216 ? -10.469 0.847   16.158 1.00 53.47  ? 290 PHE   A CE1 1 
ATOM   1585 C CE2 . PHE   A 1 216 ? -10.575 -0.416  14.139 1.00 53.24  ? 290 PHE   A CE2 1 
ATOM   1586 C CZ  . PHE   A 1 216 ? -11.209 0.276   15.148 1.00 52.97  ? 290 PHE   A CZ  1 
ATOM   1587 N N   . SER   A 1 217 ? -5.295  2.383   16.188 1.00 48.19  ? 291 SER   A N   1 
ATOM   1588 C CA  . SER   A 1 217 ? -5.238  3.563   17.045 1.00 48.05  ? 291 SER   A CA  1 
ATOM   1589 C C   . SER   A 1 217 ? -4.911  4.816   16.245 1.00 46.35  ? 291 SER   A C   1 
ATOM   1590 O O   . SER   A 1 217 ? -5.440  5.898   16.528 1.00 47.31  ? 291 SER   A O   1 
ATOM   1591 C CB  . SER   A 1 217 ? -4.212  3.352   18.158 1.00 47.21  ? 291 SER   A CB  1 
ATOM   1592 O OG  . SER   A 1 217 ? -4.573  2.249   18.977 1.00 49.38  ? 291 SER   A OG  1 
ATOM   1593 N N   . LEU   A 1 218 ? -4.047  4.695   15.239 1.00 47.50  ? 292 LEU   A N   1 
ATOM   1594 C CA  . LEU   A 1 218 ? -3.741  5.854   14.409 1.00 47.50  ? 292 LEU   A CA  1 
ATOM   1595 C C   . LEU   A 1 218 ? -4.950  6.271   13.579 1.00 48.59  ? 292 LEU   A C   1 
ATOM   1596 O O   . LEU   A 1 218 ? -5.223  7.468   13.430 1.00 51.03  ? 292 LEU   A O   1 
ATOM   1597 C CB  . LEU   A 1 218 ? -2.545  5.556   13.509 1.00 48.04  ? 292 LEU   A CB  1 
ATOM   1598 C CG  . LEU   A 1 218 ? -1.995  6.765   12.753 1.00 47.65  ? 292 LEU   A CG  1 
ATOM   1599 C CD1 . LEU   A 1 218 ? -1.626  7.866   13.722 1.00 41.98  ? 292 LEU   A CD1 1 
ATOM   1600 C CD2 . LEU   A 1 218 ? -0.792  6.353   11.938 1.00 49.93  ? 292 LEU   A CD2 1 
ATOM   1601 N N   . GLY   A 1 219 ? -5.686  5.302   13.032 1.00 45.28  ? 293 GLY   A N   1 
ATOM   1602 C CA  . GLY   A 1 219 ? -6.867  5.638   12.255 1.00 46.15  ? 293 GLY   A CA  1 
ATOM   1603 C C   . GLY   A 1 219 ? -7.895  6.409   13.059 1.00 49.77  ? 293 GLY   A C   1 
ATOM   1604 O O   . GLY   A 1 219 ? -8.496  7.368   12.566 1.00 55.47  ? 293 GLY   A O   1 
ATOM   1605 N N   . LEU   A 1 220 ? -8.122  5.996   14.304 1.00 49.37  ? 294 LEU   A N   1 
ATOM   1606 C CA  . LEU   A 1 220 ? -9.008  6.762   15.172 1.00 48.36  ? 294 LEU   A CA  1 
ATOM   1607 C C   . LEU   A 1 220 ? -8.398  8.111   15.531 1.00 48.40  ? 294 LEU   A C   1 
ATOM   1608 O O   . LEU   A 1 220 ? -9.117  9.109   15.644 1.00 52.12  ? 294 LEU   A O   1 
ATOM   1609 C CB  . LEU   A 1 220 ? -9.326  5.956   16.428 1.00 47.56  ? 294 LEU   A CB  1 
ATOM   1610 C CG  . LEU   A 1 220 ? -10.323 4.822   16.183 1.00 48.44  ? 294 LEU   A CG  1 
ATOM   1611 C CD1 . LEU   A 1 220 ? -10.585 4.052   17.461 1.00 54.98  ? 294 LEU   A CD1 1 
ATOM   1612 C CD2 . LEU   A 1 220 ? -11.618 5.379   15.629 1.00 49.19  ? 294 LEU   A CD2 1 
ATOM   1613 N N   . THR   A 1 221 ? -7.073  8.161   15.702 1.00 46.45  ? 295 THR   A N   1 
ATOM   1614 C CA  . THR   A 1 221 ? -6.396  9.434   15.927 1.00 45.34  ? 295 THR   A CA  1 
ATOM   1615 C C   . THR   A 1 221 ? -6.656  10.395  14.780 1.00 51.81  ? 295 THR   A C   1 
ATOM   1616 O O   . THR   A 1 221 ? -6.992  11.567  14.994 1.00 50.09  ? 295 THR   A O   1 
ATOM   1617 C CB  . THR   A 1 221 ? -4.890  9.210   16.087 1.00 46.29  ? 295 THR   A CB  1 
ATOM   1618 O OG1 . THR   A 1 221 ? -4.633  8.478   17.290 1.00 45.79  ? 295 THR   A OG1 1 
ATOM   1619 C CG2 . THR   A 1 221 ? -4.162  10.540  16.155 1.00 48.52  ? 295 THR   A CG2 1 
ATOM   1620 N N   . ILE   A 1 222 ? -6.498  9.905   13.548 1.00 47.09  ? 296 ILE   A N   1 
ATOM   1621 C CA  . ILE   A 1 222 ? -6.706  10.727  12.364 1.00 50.74  ? 296 ILE   A CA  1 
ATOM   1622 C C   . ILE   A 1 222 ? -8.179  11.064  12.199 1.00 54.58  ? 296 ILE   A C   1 
ATOM   1623 O O   . ILE   A 1 222 ? -8.539  12.173  11.785 1.00 57.73  ? 296 ILE   A O   1 
ATOM   1624 C CB  . ILE   A 1 222 ? -6.153  9.994   11.129 1.00 52.52  ? 296 ILE   A CB  1 
ATOM   1625 C CG1 . ILE   A 1 222 ? -4.641  9.830   11.261 1.00 50.43  ? 296 ILE   A CG1 1 
ATOM   1626 C CG2 . ILE   A 1 222 ? -6.536  10.712  9.850  1.00 54.84  ? 296 ILE   A CG2 1 
ATOM   1627 C CD1 . ILE   A 1 222 ? -3.927  11.114  11.615 1.00 54.30  ? 296 ILE   A CD1 1 
ATOM   1628 N N   . LEU   A 1 223 ? -9.057  10.113  12.504 1.00 54.04  ? 297 LEU   A N   1 
ATOM   1629 C CA  . LEU   A 1 223 ? -10.480 10.395  12.409 1.00 54.83  ? 297 LEU   A CA  1 
ATOM   1630 C C   . LEU   A 1 223 ? -10.880 11.499  13.373 1.00 56.84  ? 297 LEU   A C   1 
ATOM   1631 O O   . LEU   A 1 223 ? -11.789 12.278  13.080 1.00 63.24  ? 297 LEU   A O   1 
ATOM   1632 C CB  . LEU   A 1 223 ? -11.274 9.121   12.681 1.00 58.19  ? 297 LEU   A CB  1 
ATOM   1633 C CG  . LEU   A 1 223 ? -12.754 9.137   12.328 1.00 57.18  ? 297 LEU   A CG  1 
ATOM   1634 C CD1 . LEU   A 1 223 ? -12.938 9.480   10.865 1.00 62.77  ? 297 LEU   A CD1 1 
ATOM   1635 C CD2 . LEU   A 1 223 ? -13.339 7.782   12.634 1.00 58.10  ? 297 LEU   A CD2 1 
ATOM   1636 N N   . GLU   A 1 224 ? -10.192 11.605  14.508 1.00 56.31  ? 298 GLU   A N   1 
ATOM   1637 C CA  . GLU   A 1 224 ? -10.545 12.607  15.507 1.00 57.64  ? 298 GLU   A CA  1 
ATOM   1638 C C   . GLU   A 1 224 ? -10.045 13.995  15.123 1.00 58.75  ? 298 GLU   A C   1 
ATOM   1639 O O   . GLU   A 1 224 ? -10.766 14.985  15.285 1.00 58.68  ? 298 GLU   A O   1 
ATOM   1640 C CB  . GLU   A 1 224 ? -9.981  12.196  16.868 1.00 58.15  ? 298 GLU   A CB  1 
ATOM   1641 C CG  . GLU   A 1 224 ? -10.034 13.281  17.924 1.00 59.36  ? 298 GLU   A CG  1 
ATOM   1642 C CD  . GLU   A 1 224 ? -9.351  12.869  19.215 1.00 63.93  ? 298 GLU   A CD  1 
ATOM   1643 O OE1 . GLU   A 1 224 ? -8.911  11.702  19.310 1.00 59.41  ? 298 GLU   A OE1 1 
ATOM   1644 O OE2 . GLU   A 1 224 ? -9.253  13.709  20.137 1.00 71.85  ? 298 GLU   A OE2 1 
ATOM   1645 N N   . VAL   A 1 225 ? -8.816  14.094  14.618 1.00 56.87  ? 299 VAL   A N   1 
ATOM   1646 C CA  . VAL   A 1 225 ? -8.271  15.413  14.329 1.00 55.77  ? 299 VAL   A CA  1 
ATOM   1647 C C   . VAL   A 1 225 ? -8.819  15.960  13.017 1.00 61.50  ? 299 VAL   A C   1 
ATOM   1648 O O   . VAL   A 1 225 ? -8.989  17.177  12.873 1.00 62.51  ? 299 VAL   A O   1 
ATOM   1649 C CB  . VAL   A 1 225 ? -6.735  15.364  14.326 1.00 54.53  ? 299 VAL   A CB  1 
ATOM   1650 C CG1 . VAL   A 1 225 ? -6.243  14.650  15.562 1.00 52.55  ? 299 VAL   A CG1 1 
ATOM   1651 C CG2 . VAL   A 1 225 ? -6.218  14.677  13.080 1.00 58.02  ? 299 VAL   A CG2 1 
ATOM   1652 N N   . ALA   A 1 226 ? -9.121  15.090  12.051 1.00 61.77  ? 300 ALA   A N   1 
ATOM   1653 C CA  . ALA   A 1 226 ? -9.649  15.534  10.768 1.00 61.63  ? 300 ALA   A CA  1 
ATOM   1654 C C   . ALA   A 1 226 ? -11.149 15.782  10.792 1.00 66.99  ? 300 ALA   A C   1 
ATOM   1655 O O   . ALA   A 1 226 ? -11.670 16.409  9.864  1.00 72.31  ? 300 ALA   A O   1 
ATOM   1656 C CB  . ALA   A 1 226 ? -9.331  14.510  9.677  1.00 60.30  ? 300 ALA   A CB  1 
ATOM   1657 N N   . CYS   A 1 227 ? -11.857 15.297  11.811 1.00 65.91  ? 301 CYS   A N   1 
ATOM   1658 C CA  . CYS   A 1 227 ? -13.292 15.508  11.916 1.00 68.19  ? 301 CYS   A CA  1 
ATOM   1659 C C   . CYS   A 1 227 ? -13.694 16.296  13.146 1.00 70.17  ? 301 CYS   A C   1 
ATOM   1660 O O   . CYS   A 1 227 ? -14.873 16.647  13.273 1.00 72.91  ? 301 CYS   A O   1 
ATOM   1661 C CB  . CYS   A 1 227 ? -14.039 14.167  11.922 1.00 76.08  ? 301 CYS   A CB  1 
ATOM   1662 S SG  . CYS   A 1 227 ? -13.839 13.217  10.401 1.00 87.19  ? 301 CYS   A SG  1 
ATOM   1663 N N   . ASN   A 1 228 ? -12.755 16.577  14.051 1.00 67.67  ? 302 ASN   A N   1 
ATOM   1664 C CA  . ASN   A 1 228 ? -13.019 17.347  15.264 1.00 72.93  ? 302 ASN   A CA  1 
ATOM   1665 C C   . ASN   A 1 228 ? -14.112 16.704  16.114 1.00 76.32  ? 302 ASN   A C   1 
ATOM   1666 O O   . ASN   A 1 228 ? -14.909 17.398  16.752 1.00 77.69  ? 302 ASN   A O   1 
ATOM   1667 C CB  . ASN   A 1 228 ? -13.378 18.797  14.930 1.00 70.11  ? 302 ASN   A CB  1 
ATOM   1668 C CG  . ASN   A 1 228 ? -13.095 19.736  16.074 1.00 75.94  ? 302 ASN   A CG  1 
ATOM   1669 O OD1 . ASN   A 1 228 ? -12.242 19.459  16.920 1.00 78.97  ? 302 ASN   A OD1 1 
ATOM   1670 N ND2 . ASN   A 1 228 ? -13.807 20.855  16.114 1.00 77.64  ? 302 ASN   A ND2 1 
ATOM   1671 N N   . MET   A 1 229 ? -14.157 15.375  16.121 1.00 77.65  ? 303 MET   A N   1 
ATOM   1672 C CA  . MET   A 1 229 ? -15.148 14.619  16.872 1.00 80.45  ? 303 MET   A CA  1 
ATOM   1673 C C   . MET   A 1 229 ? -14.477 13.935  18.051 1.00 80.31  ? 303 MET   A C   1 
ATOM   1674 O O   . MET   A 1 229 ? -13.328 13.491  17.953 1.00 78.60  ? 303 MET   A O   1 
ATOM   1675 C CB  . MET   A 1 229 ? -15.839 13.573  15.991 1.00 91.77  ? 303 MET   A CB  1 
ATOM   1676 C CG  . MET   A 1 229 ? -14.917 12.471  15.478 1.00 82.92  ? 303 MET   A CG  1 
ATOM   1677 S SD  . MET   A 1 229 ? -15.812 11.136  14.654 1.00 107.93 ? 303 MET   A SD  1 
ATOM   1678 C CE  . MET   A 1 229 ? -16.925 10.616  15.962 1.00 103.34 ? 303 MET   A CE  1 
ATOM   1679 N N   . GLU   A 1 230 ? -15.193 13.853  19.165 1.00 76.86  ? 304 GLU   A N   1 
ATOM   1680 C CA  . GLU   A 1 230 ? -14.656 13.230  20.363 1.00 76.46  ? 304 GLU   A CA  1 
ATOM   1681 C C   . GLU   A 1 230 ? -14.990 11.747  20.380 1.00 69.80  ? 304 GLU   A C   1 
ATOM   1682 O O   . GLU   A 1 230 ? -16.110 11.341  20.059 1.00 72.03  ? 304 GLU   A O   1 
ATOM   1683 C CB  . GLU   A 1 230 ? -15.191 13.920  21.616 1.00 78.71  ? 304 GLU   A CB  1 
ATOM   1684 C CG  . GLU   A 1 230 ? -14.534 15.269  21.862 1.00 89.24  ? 304 GLU   A CG  1 
ATOM   1685 C CD  . GLU   A 1 230 ? -15.259 16.094  22.900 1.00 103.86 ? 304 GLU   A CD  1 
ATOM   1686 O OE1 . GLU   A 1 230 ? -16.029 15.507  23.693 1.00 108.54 ? 304 GLU   A OE1 1 
ATOM   1687 O OE2 . GLU   A 1 230 ? -15.065 17.330  22.916 1.00 101.52 ? 304 GLU   A OE2 1 
ATOM   1688 N N   . LEU   A 1 231 ? -14.010 10.946  20.743 1.00 64.97  ? 305 LEU   A N   1 
ATOM   1689 C CA  . LEU   A 1 231 ? -14.199 9.512   20.643 1.00 60.73  ? 305 LEU   A CA  1 
ATOM   1690 C C   . LEU   A 1 231 ? -14.931 8.989   21.874 1.00 61.79  ? 305 LEU   A C   1 
ATOM   1691 O O   . LEU   A 1 231 ? -14.717 9.487   22.983 1.00 62.88  ? 305 LEU   A O   1 
ATOM   1692 C CB  . LEU   A 1 231 ? -12.857 8.807   20.496 1.00 61.24  ? 305 LEU   A CB  1 
ATOM   1693 C CG  . LEU   A 1 231 ? -12.099 9.186   19.226 1.00 57.04  ? 305 LEU   A CG  1 
ATOM   1694 C CD1 . LEU   A 1 231 ? -10.816 8.401   19.123 1.00 51.97  ? 305 LEU   A CD1 1 
ATOM   1695 C CD2 . LEU   A 1 231 ? -12.971 8.945   18.011 1.00 61.92  ? 305 LEU   A CD2 1 
ATOM   1696 N N   . PRO   A 1 232 ? -15.803 7.998   21.701 1.00 61.38  ? 306 PRO   A N   1 
ATOM   1697 C CA  . PRO   A 1 232 ? -16.548 7.457   22.845 1.00 62.27  ? 306 PRO   A CA  1 
ATOM   1698 C C   . PRO   A 1 232 ? -15.705 6.513   23.691 1.00 62.75  ? 306 PRO   A C   1 
ATOM   1699 O O   . PRO   A 1 232 ? -14.966 5.670   23.176 1.00 57.17  ? 306 PRO   A O   1 
ATOM   1700 C CB  . PRO   A 1 232 ? -17.714 6.714   22.179 1.00 62.18  ? 306 PRO   A CB  1 
ATOM   1701 C CG  . PRO   A 1 232 ? -17.200 6.355   20.818 1.00 59.91  ? 306 PRO   A CG  1 
ATOM   1702 C CD  . PRO   A 1 232 ? -16.297 7.479   20.413 1.00 58.27  ? 306 PRO   A CD  1 
ATOM   1703 N N   . HIS   A 1 233 ? -15.828 6.668   25.014 1.00 69.23  ? 307 HIS   A N   1 
ATOM   1704 C CA  . HIS   A 1 233 ? -15.115 5.795   25.940 1.00 66.44  ? 307 HIS   A CA  1 
ATOM   1705 C C   . HIS   A 1 233 ? -15.679 4.381   25.927 1.00 63.96  ? 307 HIS   A C   1 
ATOM   1706 O O   . HIS   A 1 233 ? -14.968 3.429   26.266 1.00 64.11  ? 307 HIS   A O   1 
ATOM   1707 C CB  . HIS   A 1 233 ? -15.172 6.366   27.363 1.00 66.93  ? 307 HIS   A CB  1 
ATOM   1708 C CG  . HIS   A 1 233 ? -14.071 7.338   27.676 1.00 75.37  ? 307 HIS   A CG  1 
ATOM   1709 N ND1 . HIS   A 1 233 ? -14.256 8.706   27.688 1.00 78.91  ? 307 HIS   A ND1 1 
ATOM   1710 C CD2 . HIS   A 1 233 ? -12.768 7.135   27.995 1.00 73.38  ? 307 HIS   A CD2 1 
ATOM   1711 C CE1 . HIS   A 1 233 ? -13.117 9.303   27.996 1.00 75.91  ? 307 HIS   A CE1 1 
ATOM   1712 N NE2 . HIS   A 1 233 ? -12.198 8.372   28.187 1.00 74.66  ? 307 HIS   A NE2 1 
ATOM   1713 N N   . GLY   A 1 234 ? -16.939 4.223   25.548 1.00 64.55  ? 308 GLY   A N   1 
ATOM   1714 C CA  . GLY   A 1 234 ? -17.557 2.914   25.568 1.00 62.40  ? 308 GLY   A CA  1 
ATOM   1715 C C   . GLY   A 1 234 ? -18.989 3.009   25.099 1.00 66.32  ? 308 GLY   A C   1 
ATOM   1716 O O   . GLY   A 1 234 ? -19.449 4.062   24.653 1.00 70.30  ? 308 GLY   A O   1 
ATOM   1717 N N   . GLY   A 1 235 ? -19.688 1.884   25.192 1.00 64.94  ? 309 GLY   A N   1 
ATOM   1718 C CA  . GLY   A 1 235 ? -21.099 1.874   24.862 1.00 71.57  ? 309 GLY   A CA  1 
ATOM   1719 C C   . GLY   A 1 235 ? -21.371 1.855   23.365 1.00 74.80  ? 309 GLY   A C   1 
ATOM   1720 O O   . GLY   A 1 235 ? -20.575 1.364   22.561 1.00 72.18  ? 309 GLY   A O   1 
ATOM   1721 N N   . GLU   A 1 236 ? -22.520 2.429   22.997 1.00 76.16  ? 310 GLU   A N   1 
ATOM   1722 C CA  . GLU   A 1 236 ? -23.053 2.268   21.646 1.00 81.48  ? 310 GLU   A CA  1 
ATOM   1723 C C   . GLU   A 1 236 ? -22.118 2.856   20.593 1.00 76.10  ? 310 GLU   A C   1 
ATOM   1724 O O   . GLU   A 1 236 ? -21.773 2.187   19.612 1.00 73.80  ? 310 GLU   A O   1 
ATOM   1725 C CB  . GLU   A 1 236 ? -24.446 2.902   21.562 1.00 93.79  ? 310 GLU   A CB  1 
ATOM   1726 C CG  . GLU   A 1 236 ? -24.543 4.372   22.025 1.00 103.54 ? 310 GLU   A CG  1 
ATOM   1727 C CD  . GLU   A 1 236 ? -24.681 4.552   23.543 1.00 102.90 ? 310 GLU   A CD  1 
ATOM   1728 O OE1 . GLU   A 1 236 ? -24.407 3.596   24.304 1.00 93.17  ? 310 GLU   A OE1 1 
ATOM   1729 O OE2 . GLU   A 1 236 ? -25.068 5.664   23.971 1.00 104.46 ? 310 GLU   A OE2 1 
ATOM   1730 N N   . GLY   A 1 237 ? -21.695 4.108   20.781 1.00 74.31  ? 311 GLY   A N   1 
ATOM   1731 C CA  . GLY   A 1 237 ? -20.820 4.736   19.806 1.00 70.89  ? 311 GLY   A CA  1 
ATOM   1732 C C   . GLY   A 1 237 ? -19.493 4.019   19.665 1.00 69.76  ? 311 GLY   A C   1 
ATOM   1733 O O   . GLY   A 1 237 ? -18.947 3.919   18.564 1.00 73.00  ? 311 GLY   A O   1 
ATOM   1734 N N   . TRP   A 1 238 ? -18.959 3.508   20.779 1.00 70.14  ? 312 TRP   A N   1 
ATOM   1735 C CA  . TRP   A 1 238 ? -17.717 2.740   20.736 1.00 65.44  ? 312 TRP   A CA  1 
ATOM   1736 C C   . TRP   A 1 238 ? -17.826 1.569   19.768 1.00 67.38  ? 312 TRP   A C   1 
ATOM   1737 O O   . TRP   A 1 238 ? -16.893 1.293   19.004 1.00 65.68  ? 312 TRP   A O   1 
ATOM   1738 C CB  . TRP   A 1 238 ? -17.373 2.244   22.143 1.00 63.45  ? 312 TRP   A CB  1 
ATOM   1739 C CG  . TRP   A 1 238 ? -16.000 1.649   22.282 1.00 58.20  ? 312 TRP   A CG  1 
ATOM   1740 C CD1 . TRP   A 1 238 ? -14.853 2.304   22.626 1.00 57.62  ? 312 TRP   A CD1 1 
ATOM   1741 C CD2 . TRP   A 1 238 ? -15.634 0.276   22.090 1.00 55.71  ? 312 TRP   A CD2 1 
ATOM   1742 N NE1 . TRP   A 1 238 ? -13.794 1.425   22.657 1.00 55.90  ? 312 TRP   A NE1 1 
ATOM   1743 C CE2 . TRP   A 1 238 ? -14.248 0.174   22.329 1.00 53.12  ? 312 TRP   A CE2 1 
ATOM   1744 C CE3 . TRP   A 1 238 ? -16.344 -0.876  21.735 1.00 59.65  ? 312 TRP   A CE3 1 
ATOM   1745 C CZ2 . TRP   A 1 238 ? -13.560 -1.030  22.225 1.00 51.82  ? 312 TRP   A CZ2 1 
ATOM   1746 C CZ3 . TRP   A 1 238 ? -15.659 -2.072  21.633 1.00 61.63  ? 312 TRP   A CZ3 1 
ATOM   1747 C CH2 . TRP   A 1 238 ? -14.278 -2.139  21.874 1.00 55.05  ? 312 TRP   A CH2 1 
ATOM   1748 N N   . GLN   A 1 239 ? -18.966 0.871   19.784 1.00 70.69  ? 313 GLN   A N   1 
ATOM   1749 C CA  . GLN   A 1 239 ? -19.163 -0.260  18.885 1.00 68.82  ? 313 GLN   A CA  1 
ATOM   1750 C C   . GLN   A 1 239 ? -19.277 0.187   17.433 1.00 74.52  ? 313 GLN   A C   1 
ATOM   1751 O O   . GLN   A 1 239 ? -18.843 -0.540  16.534 1.00 73.94  ? 313 GLN   A O   1 
ATOM   1752 C CB  . GLN   A 1 239 ? -20.410 -1.048  19.296 1.00 67.09  ? 313 GLN   A CB  1 
ATOM   1753 C CG  . GLN   A 1 239 ? -20.430 -1.514  20.751 1.00 67.65  ? 313 GLN   A CG  1 
ATOM   1754 C CD  . GLN   A 1 239 ? -19.413 -2.610  21.037 1.00 72.97  ? 313 GLN   A CD  1 
ATOM   1755 O OE1 . GLN   A 1 239 ? -18.981 -3.326  20.131 1.00 75.85  ? 313 GLN   A OE1 1 
ATOM   1756 N NE2 . GLN   A 1 239 ? -19.023 -2.742  22.304 1.00 69.14  ? 313 GLN   A NE2 1 
ATOM   1757 N N   . GLN   A 1 240 ? -19.850 1.372   17.186 1.00 76.17  ? 314 GLN   A N   1 
ATOM   1758 C CA  . GLN   A 1 240 ? -20.050 1.844   15.816 1.00 78.72  ? 314 GLN   A CA  1 
ATOM   1759 C C   . GLN   A 1 240 ? -18.723 1.994   15.080 1.00 78.29  ? 314 GLN   A C   1 
ATOM   1760 O O   . GLN   A 1 240 ? -18.589 1.570   13.925 1.00 81.22  ? 314 GLN   A O   1 
ATOM   1761 C CB  . GLN   A 1 240 ? -20.802 3.177   15.818 1.00 84.15  ? 314 GLN   A CB  1 
ATOM   1762 C CG  . GLN   A 1 240 ? -22.020 3.238   16.725 1.00 84.94  ? 314 GLN   A CG  1 
ATOM   1763 C CD  . GLN   A 1 240 ? -23.264 2.657   16.093 1.00 96.77  ? 314 GLN   A CD  1 
ATOM   1764 O OE1 . GLN   A 1 240 ? -23.199 1.989   15.061 1.00 107.05 ? 314 GLN   A OE1 1 
ATOM   1765 N NE2 . GLN   A 1 240 ? -24.413 2.914   16.709 1.00 102.33 ? 314 GLN   A NE2 1 
ATOM   1766 N N   . LEU   A 1 241 ? -17.730 2.607   15.734 1.00 71.70  ? 315 LEU   A N   1 
ATOM   1767 C CA  . LEU   A 1 241 ? -16.417 2.835   15.135 1.00 70.12  ? 315 LEU   A CA  1 
ATOM   1768 C C   . LEU   A 1 241 ? -15.624 1.553   14.923 1.00 68.67  ? 315 LEU   A C   1 
ATOM   1769 O O   . LEU   A 1 241 ? -14.495 1.618   14.425 1.00 63.87  ? 315 LEU   A O   1 
ATOM   1770 C CB  . LEU   A 1 241 ? -15.597 3.793   16.005 1.00 59.01  ? 315 LEU   A CB  1 
ATOM   1771 C CG  . LEU   A 1 241 ? -16.140 5.211   16.177 1.00 59.52  ? 315 LEU   A CG  1 
ATOM   1772 C CD1 . LEU   A 1 241 ? -15.287 5.997   17.154 1.00 58.85  ? 315 LEU   A CD1 1 
ATOM   1773 C CD2 . LEU   A 1 241 ? -16.217 5.930   14.841 1.00 68.50  ? 315 LEU   A CD2 1 
ATOM   1774 N N   . ARG   A 1 242 ? -16.172 0.392   15.280 1.00 68.37  ? 316 ARG   A N   1 
ATOM   1775 C CA  . ARG   A 1 242 ? -15.418 -0.850  15.211 1.00 66.39  ? 316 ARG   A CA  1 
ATOM   1776 C C   . ARG   A 1 242 ? -16.169 -1.928  14.440 1.00 70.55  ? 316 ARG   A C   1 
ATOM   1777 O O   . ARG   A 1 242 ? -15.899 -3.121  14.632 1.00 68.31  ? 316 ARG   A O   1 
ATOM   1778 C CB  . ARG   A 1 242 ? -15.053 -1.313  16.623 1.00 62.77  ? 316 ARG   A CB  1 
ATOM   1779 C CG  . ARG   A 1 242 ? -14.026 -0.381  17.251 1.00 62.64  ? 316 ARG   A CG  1 
ATOM   1780 C CD  . ARG   A 1 242 ? -13.945 -0.455  18.759 1.00 58.86  ? 316 ARG   A CD  1 
ATOM   1781 N NE  . ARG   A 1 242 ? -12.806 0.324   19.236 1.00 56.73  ? 316 ARG   A NE  1 
ATOM   1782 C CZ  . ARG   A 1 242 ? -12.863 1.603   19.583 1.00 56.43  ? 316 ARG   A CZ  1 
ATOM   1783 N NH1 . ARG   A 1 242 ? -14.006 2.274   19.573 1.00 56.57  ? 316 ARG   A NH1 1 
ATOM   1784 N NH2 . ARG   A 1 242 ? -11.745 2.226   19.949 1.00 51.27  ? 316 ARG   A NH2 1 
ATOM   1785 N N   . GLN   A 1 243 ? -17.095 -1.528  13.563 1.00 74.15  ? 317 GLN   A N   1 
ATOM   1786 C CA  . GLN   A 1 243 ? -17.807 -2.441  12.677 1.00 78.20  ? 317 GLN   A CA  1 
ATOM   1787 C C   . GLN   A 1 243 ? -17.338 -2.345  11.232 1.00 81.04  ? 317 GLN   A C   1 
ATOM   1788 O O   . GLN   A 1 243 ? -17.877 -3.051  10.374 1.00 86.03  ? 317 GLN   A O   1 
ATOM   1789 C CB  . GLN   A 1 243 ? -19.322 -2.182  12.729 1.00 87.11  ? 317 GLN   A CB  1 
ATOM   1790 C CG  . GLN   A 1 243 ? -19.937 -2.168  14.118 1.00 83.74  ? 317 GLN   A CG  1 
ATOM   1791 C CD  . GLN   A 1 243 ? -19.956 -3.531  14.775 1.00 79.02  ? 317 GLN   A CD  1 
ATOM   1792 O OE1 . GLN   A 1 243 ? -19.255 -3.767  15.761 1.00 84.75  ? 317 GLN   A OE1 1 
ATOM   1793 N NE2 . GLN   A 1 243 ? -20.774 -4.434  14.243 1.00 87.40  ? 317 GLN   A NE2 1 
ATOM   1794 N N   . GLY   A 1 244 ? -16.385 -1.471  10.930 1.00 83.23  ? 318 GLY   A N   1 
ATOM   1795 C CA  . GLY   A 1 244 ? -15.860 -1.347  9.586  1.00 88.41  ? 318 GLY   A CA  1 
ATOM   1796 C C   . GLY   A 1 244 ? -16.508 -0.289  8.718  1.00 98.69  ? 318 GLY   A C   1 
ATOM   1797 O O   . GLY   A 1 244 ? -16.213 -0.241  7.517  1.00 99.61  ? 318 GLY   A O   1 
ATOM   1798 N N   . TYR   A 1 245 ? -17.384 0.546   9.271  1.00 109.97 ? 319 TYR   A N   1 
ATOM   1799 C CA  . TYR   A 1 245 ? -17.924 1.699   8.557  1.00 111.66 ? 319 TYR   A CA  1 
ATOM   1800 C C   . TYR   A 1 245 ? -17.572 2.968   9.319  1.00 111.01 ? 319 TYR   A C   1 
ATOM   1801 O O   . TYR   A 1 245 ? -17.728 3.025   10.542 1.00 113.17 ? 319 TYR   A O   1 
ATOM   1802 C CB  . TYR   A 1 245 ? -19.446 1.601   8.351  1.00 114.99 ? 319 TYR   A CB  1 
ATOM   1803 C CG  . TYR   A 1 245 ? -20.283 1.318   9.584  1.00 115.72 ? 319 TYR   A CG  1 
ATOM   1804 C CD1 . TYR   A 1 245 ? -20.638 2.334   10.470 1.00 115.46 ? 319 TYR   A CD1 1 
ATOM   1805 C CD2 . TYR   A 1 245 ? -20.765 0.039   9.834  1.00 117.30 ? 319 TYR   A CD2 1 
ATOM   1806 C CE1 . TYR   A 1 245 ? -21.421 2.073   11.590 1.00 118.58 ? 319 TYR   A CE1 1 
ATOM   1807 C CE2 . TYR   A 1 245 ? -21.554 -0.230  10.948 1.00 119.98 ? 319 TYR   A CE2 1 
ATOM   1808 C CZ  . TYR   A 1 245 ? -21.876 0.788   11.822 1.00 120.90 ? 319 TYR   A CZ  1 
ATOM   1809 O OH  . TYR   A 1 245 ? -22.658 0.511   12.924 1.00 119.53 ? 319 TYR   A OH  1 
ATOM   1810 N N   . LEU   A 1 246 ? -17.061 3.963   8.604  1.00 95.90  ? 320 LEU   A N   1 
ATOM   1811 C CA  . LEU   A 1 246 ? -16.818 5.255   9.219  1.00 96.73  ? 320 LEU   A CA  1 
ATOM   1812 C C   . LEU   A 1 246 ? -18.157 5.907   9.573  1.00 102.93 ? 320 LEU   A C   1 
ATOM   1813 O O   . LEU   A 1 246 ? -19.169 5.650   8.916  1.00 100.93 ? 320 LEU   A O   1 
ATOM   1814 C CB  . LEU   A 1 246 ? -16.024 6.160   8.280  1.00 95.79  ? 320 LEU   A CB  1 
ATOM   1815 C CG  . LEU   A 1 246 ? -14.716 5.598   7.717  1.00 88.92  ? 320 LEU   A CG  1 
ATOM   1816 C CD1 . LEU   A 1 246 ? -13.969 6.660   6.926  1.00 85.72  ? 320 LEU   A CD1 1 
ATOM   1817 C CD2 . LEU   A 1 246 ? -13.843 5.053   8.824  1.00 77.89  ? 320 LEU   A CD2 1 
ATOM   1818 N N   . PRO   A 1 247 ? -18.188 6.743   10.613 1.00 102.04 ? 321 PRO   A N   1 
ATOM   1819 C CA  . PRO   A 1 247 ? -19.447 7.403   10.991 1.00 100.76 ? 321 PRO   A CA  1 
ATOM   1820 C C   . PRO   A 1 247 ? -19.918 8.331   9.887  1.00 102.12 ? 321 PRO   A C   1 
ATOM   1821 O O   . PRO   A 1 247 ? -19.141 9.148   9.372  1.00 106.80 ? 321 PRO   A O   1 
ATOM   1822 C CB  . PRO   A 1 247 ? -19.075 8.182   12.261 1.00 100.70 ? 321 PRO   A CB  1 
ATOM   1823 C CG  . PRO   A 1 247 ? -17.605 8.380   12.161 1.00 101.33 ? 321 PRO   A CG  1 
ATOM   1824 C CD  . PRO   A 1 247 ? -17.078 7.150   11.487 1.00 94.76  ? 321 PRO   A CD  1 
ATOM   1825 N N   . PRO   A 1 248 ? -21.194 8.235   9.502  1.00 107.11 ? 322 PRO   A N   1 
ATOM   1826 C CA  . PRO   A 1 248 ? -21.632 8.922   8.276  1.00 107.25 ? 322 PRO   A CA  1 
ATOM   1827 C C   . PRO   A 1 248 ? -21.572 10.433  8.372  1.00 115.56 ? 322 PRO   A C   1 
ATOM   1828 O O   . PRO   A 1 248 ? -21.256 11.093  7.375  1.00 114.26 ? 322 PRO   A O   1 
ATOM   1829 C CB  . PRO   A 1 248 ? -23.069 8.418   8.096  1.00 95.03  ? 322 PRO   A CB  1 
ATOM   1830 C CG  . PRO   A 1 248 ? -23.516 8.080   9.480  1.00 99.42  ? 322 PRO   A CG  1 
ATOM   1831 C CD  . PRO   A 1 248 ? -22.302 7.544   10.181 1.00 103.62 ? 322 PRO   A CD  1 
ATOM   1832 N N   . GLU   A 1 249 ? -21.868 11.001  9.541  1.00 129.20 ? 323 GLU   A N   1 
ATOM   1833 C CA  . GLU   A 1 249 ? -21.879 12.452  9.684  1.00 132.46 ? 323 GLU   A CA  1 
ATOM   1834 C C   . GLU   A 1 249 ? -20.491 13.031  9.502  1.00 132.94 ? 323 GLU   A C   1 
ATOM   1835 O O   . GLU   A 1 249 ? -20.290 13.970  8.725  1.00 135.54 ? 323 GLU   A O   1 
ATOM   1836 C CB  . GLU   A 1 249 ? -22.411 12.832  11.062 1.00 138.09 ? 323 GLU   A CB  1 
ATOM   1837 C CG  . GLU   A 1 249 ? -23.854 12.445  11.318 1.00 148.62 ? 323 GLU   A CG  1 
ATOM   1838 C CD  . GLU   A 1 249 ? -24.276 12.747  12.738 1.00 156.98 ? 323 GLU   A CD  1 
ATOM   1839 O OE1 . GLU   A 1 249 ? -23.378 12.968  13.581 1.00 150.12 ? 323 GLU   A OE1 1 
ATOM   1840 O OE2 . GLU   A 1 249 ? -25.497 12.768  13.006 1.00 162.21 ? 323 GLU   A OE2 1 
ATOM   1841 N N   . PHE   A 1 250 ? -19.515 12.470  10.206 1.00 121.86 ? 324 PHE   A N   1 
ATOM   1842 C CA  . PHE   A 1 250 ? -18.189 13.066  10.254 1.00 120.73 ? 324 PHE   A CA  1 
ATOM   1843 C C   . PHE   A 1 250 ? -17.381 12.783  8.995  1.00 118.26 ? 324 PHE   A C   1 
ATOM   1844 O O   . PHE   A 1 250 ? -16.545 13.608  8.603  1.00 112.82 ? 324 PHE   A O   1 
ATOM   1845 C CB  . PHE   A 1 250 ? -17.484 12.564  11.510 1.00 116.88 ? 324 PHE   A CB  1 
ATOM   1846 C CG  . PHE   A 1 250 ? -18.328 12.701  12.748 1.00 121.17 ? 324 PHE   A CG  1 
ATOM   1847 C CD1 . PHE   A 1 250 ? -18.358 13.899  13.445 1.00 117.27 ? 324 PHE   A CD1 1 
ATOM   1848 C CD2 . PHE   A 1 250 ? -19.120 11.649  13.196 1.00 122.81 ? 324 PHE   A CD2 1 
ATOM   1849 C CE1 . PHE   A 1 250 ? -19.141 14.043  14.571 1.00 122.65 ? 324 PHE   A CE1 1 
ATOM   1850 C CE2 . PHE   A 1 250 ? -19.912 11.791  14.330 1.00 126.10 ? 324 PHE   A CE2 1 
ATOM   1851 C CZ  . PHE   A 1 250 ? -19.918 12.991  15.015 1.00 128.02 ? 324 PHE   A CZ  1 
ATOM   1852 N N   . THR   A 1 251 ? -17.656 11.660  8.328  1.00 124.09 ? 325 THR   A N   1 
ATOM   1853 C CA  . THR   A 1 251 ? -16.847 11.230  7.194  1.00 121.47 ? 325 THR   A CA  1 
ATOM   1854 C C   . THR   A 1 251 ? -17.029 12.119  5.967  1.00 117.68 ? 325 THR   A C   1 
ATOM   1855 O O   . THR   A 1 251 ? -16.181 12.084  5.070  1.00 115.20 ? 325 THR   A O   1 
ATOM   1856 C CB  . THR   A 1 251 ? -17.182 9.772   6.843  1.00 120.64 ? 325 THR   A CB  1 
ATOM   1857 O OG1 . THR   A 1 251 ? -16.124 9.207   6.058  1.00 123.15 ? 325 THR   A OG1 1 
ATOM   1858 C CG2 . THR   A 1 251 ? -18.485 9.683   6.076  1.00 120.10 ? 325 THR   A CG2 1 
ATOM   1859 N N   . ALA   A 1 252 ? -18.104 12.912  5.903  1.00 112.80 ? 326 ALA   A N   1 
ATOM   1860 C CA  . ALA   A 1 252 ? -18.474 13.563  4.645  1.00 114.73 ? 326 ALA   A CA  1 
ATOM   1861 C C   . ALA   A 1 252 ? -17.425 14.570  4.188  1.00 111.41 ? 326 ALA   A C   1 
ATOM   1862 O O   . ALA   A 1 252 ? -17.132 14.664  2.988  1.00 110.87 ? 326 ALA   A O   1 
ATOM   1863 C CB  . ALA   A 1 252 ? -19.832 14.244  4.782  1.00 108.40 ? 326 ALA   A CB  1 
ATOM   1864 N N   . GLY   A 1 253 ? -16.842 15.325  5.125  1.00 107.70 ? 327 GLY   A N   1 
ATOM   1865 C CA  . GLY   A 1 253 ? -15.863 16.333  4.751  1.00 99.15  ? 327 GLY   A CA  1 
ATOM   1866 C C   . GLY   A 1 253 ? -14.605 15.745  4.147  1.00 96.20  ? 327 GLY   A C   1 
ATOM   1867 O O   . GLY   A 1 253 ? -13.999 16.352  3.260  1.00 94.34  ? 327 GLY   A O   1 
ATOM   1868 N N   . LEU   A 1 254 ? -14.197 14.565  4.613  1.00 96.73  ? 328 LEU   A N   1 
ATOM   1869 C CA  . LEU   A 1 254 ? -12.970 13.924  4.155  1.00 90.23  ? 328 LEU   A CA  1 
ATOM   1870 C C   . LEU   A 1 254 ? -13.007 13.652  2.650  1.00 93.17  ? 328 LEU   A C   1 
ATOM   1871 O O   . LEU   A 1 254 ? -14.072 13.550  2.035  1.00 97.20  ? 328 LEU   A O   1 
ATOM   1872 C CB  . LEU   A 1 254 ? -12.748 12.609  4.903  1.00 86.56  ? 328 LEU   A CB  1 
ATOM   1873 C CG  . LEU   A 1 254 ? -13.077 12.677  6.391  1.00 89.61  ? 328 LEU   A CG  1 
ATOM   1874 C CD1 . LEU   A 1 254 ? -12.969 11.301  7.032  1.00 87.35  ? 328 LEU   A CD1 1 
ATOM   1875 C CD2 . LEU   A 1 254 ? -12.166 13.679  7.082  1.00 83.60  ? 328 LEU   A CD2 1 
ATOM   1876 N N   . SER   A 1 255 ? -11.824 13.528  2.058  1.00 86.67  ? 329 SER   A N   1 
ATOM   1877 C CA  . SER   A 1 255 ? -11.704 13.148  0.659  1.00 84.55  ? 329 SER   A CA  1 
ATOM   1878 C C   . SER   A 1 255 ? -11.884 11.640  0.500  1.00 87.34  ? 329 SER   A C   1 
ATOM   1879 O O   . SER   A 1 255 ? -11.801 10.875  1.466  1.00 90.04  ? 329 SER   A O   1 
ATOM   1880 C CB  . SER   A 1 255 ? -10.344 13.575  0.110  1.00 84.26  ? 329 SER   A CB  1 
ATOM   1881 O OG  . SER   A 1 255 ? -9.295  13.004  0.878  1.00 84.65  ? 329 SER   A OG  1 
ATOM   1882 N N   . SER   A 1 256 ? -12.123 11.215  -0.745 1.00 85.74  ? 330 SER   A N   1 
ATOM   1883 C CA  . SER   A 1 256 ? -12.312 9.793   -1.010 1.00 84.50  ? 330 SER   A CA  1 
ATOM   1884 C C   . SER   A 1 256 ? -11.062 8.997   -0.654 1.00 91.31  ? 330 SER   A C   1 
ATOM   1885 O O   . SER   A 1 256 ? -11.156 7.903   -0.083 1.00 88.90  ? 330 SER   A O   1 
ATOM   1886 C CB  . SER   A 1 256 ? -12.697 9.571   -2.473 1.00 87.20  ? 330 SER   A CB  1 
ATOM   1887 O OG  . SER   A 1 256 ? -11.602 9.791   -3.342 1.00 86.90  ? 330 SER   A OG  1 
ATOM   1888 N N   . GLU   A 1 257 ? -9.881  9.539   -0.965 1.00 93.95  ? 331 GLU   A N   1 
ATOM   1889 C CA  . GLU   A 1 257 ? -8.631  8.862   -0.626 1.00 89.85  ? 331 GLU   A CA  1 
ATOM   1890 C C   . GLU   A 1 257 ? -8.471  8.723   0.884  1.00 88.95  ? 331 GLU   A C   1 
ATOM   1891 O O   . GLU   A 1 257 ? -8.136  7.644   1.387  1.00 87.39  ? 331 GLU   A O   1 
ATOM   1892 C CB  . GLU   A 1 257 ? -7.446  9.621   -1.224 1.00 92.65  ? 331 GLU   A CB  1 
ATOM   1893 C CG  . GLU   A 1 257 ? -7.640  10.047  -2.675 1.00 97.84  ? 331 GLU   A CG  1 
ATOM   1894 C CD  . GLU   A 1 257 ? -8.181  11.465  -2.816 1.00 100.61 ? 331 GLU   A CD  1 
ATOM   1895 O OE1 . GLU   A 1 257 ? -8.078  12.249  -1.847 1.00 99.80  ? 331 GLU   A OE1 1 
ATOM   1896 O OE2 . GLU   A 1 257 ? -8.712  11.796  -3.898 1.00 104.83 ? 331 GLU   A OE2 1 
ATOM   1897 N N   . LEU   A 1 258 ? -8.703  9.808   1.626  1.00 80.31  ? 332 LEU   A N   1 
ATOM   1898 C CA  . LEU   A 1 258 ? -8.607  9.737   3.080  1.00 78.45  ? 332 LEU   A CA  1 
ATOM   1899 C C   . LEU   A 1 258 ? -9.641  8.776   3.648  1.00 77.13  ? 332 LEU   A C   1 
ATOM   1900 O O   . LEU   A 1 258 ? -9.317  7.917   4.476  1.00 76.89  ? 332 LEU   A O   1 
ATOM   1901 C CB  . LEU   A 1 258 ? -8.776  11.127  3.691  1.00 76.07  ? 332 LEU   A CB  1 
ATOM   1902 C CG  . LEU   A 1 258 ? -8.588  11.177  5.206  1.00 73.28  ? 332 LEU   A CG  1 
ATOM   1903 C CD1 . LEU   A 1 258 ? -7.190  10.703  5.586  1.00 67.02  ? 332 LEU   A CD1 1 
ATOM   1904 C CD2 . LEU   A 1 258 ? -8.844  12.580  5.725  1.00 77.86  ? 332 LEU   A CD2 1 
ATOM   1905 N N   . ARG   A 1 259 ? -10.898 8.908   3.213  1.00 78.68  ? 333 ARG   A N   1 
ATOM   1906 C CA  . ARG   A 1 259 ? -11.928 7.967   3.637  1.00 78.30  ? 333 ARG   A CA  1 
ATOM   1907 C C   . ARG   A 1 259 ? -11.519 6.536   3.313  1.00 78.89  ? 333 ARG   A C   1 
ATOM   1908 O O   . ARG   A 1 259 ? -11.738 5.620   4.115  1.00 76.68  ? 333 ARG   A O   1 
ATOM   1909 C CB  . ARG   A 1 259 ? -13.262 8.317   2.973  1.00 83.57  ? 333 ARG   A CB  1 
ATOM   1910 C CG  . ARG   A 1 259 ? -14.446 7.511   3.482  1.00 89.05  ? 333 ARG   A CG  1 
ATOM   1911 C CD  . ARG   A 1 259 ? -15.768 7.955   2.855  1.00 90.70  ? 333 ARG   A CD  1 
ATOM   1912 N NE  . ARG   A 1 259 ? -16.055 9.364   3.098  1.00 97.33  ? 333 ARG   A NE  1 
ATOM   1913 C CZ  . ARG   A 1 259 ? -16.027 10.309  2.166  1.00 103.33 ? 333 ARG   A CZ  1 
ATOM   1914 N NH1 . ARG   A 1 259 ? -15.743 10.030  0.903  1.00 97.26  ? 333 ARG   A NH1 1 
ATOM   1915 N NH2 . ARG   A 1 259 ? -16.293 11.567  2.510  1.00 106.98 ? 333 ARG   A NH2 1 
ATOM   1916 N N   . SER   A 1 260 ? -10.891 6.335   2.151  1.00 80.85  ? 334 SER   A N   1 
ATOM   1917 C CA  . SER   A 1 260 ? -10.433 5.007   1.758  1.00 79.73  ? 334 SER   A CA  1 
ATOM   1918 C C   . SER   A 1 260 ? -9.346  4.485   2.689  1.00 77.77  ? 334 SER   A C   1 
ATOM   1919 O O   . SER   A 1 260 ? -9.366  3.310   3.072  1.00 79.39  ? 334 SER   A O   1 
ATOM   1920 C CB  . SER   A 1 260 ? -9.923  5.035   0.317  1.00 82.26  ? 334 SER   A CB  1 
ATOM   1921 O OG  . SER   A 1 260 ? -9.064  3.936   0.060  1.00 83.59  ? 334 SER   A OG  1 
ATOM   1922 N N   . VAL   A 1 261 ? -8.380  5.332   3.052  1.00 73.16  ? 335 VAL   A N   1 
ATOM   1923 C CA  . VAL   A 1 261 ? -7.282  4.864   3.893  1.00 72.79  ? 335 VAL   A CA  1 
ATOM   1924 C C   . VAL   A 1 261 ? -7.764  4.628   5.322  1.00 71.34  ? 335 VAL   A C   1 
ATOM   1925 O O   . VAL   A 1 261 ? -7.358  3.658   5.975  1.00 67.71  ? 335 VAL   A O   1 
ATOM   1926 C CB  . VAL   A 1 261 ? -6.102  5.852   3.834  1.00 68.04  ? 335 VAL   A CB  1 
ATOM   1927 C CG1 . VAL   A 1 261 ? -5.000  5.431   4.792  1.00 69.04  ? 335 VAL   A CG1 1 
ATOM   1928 C CG2 . VAL   A 1 261 ? -5.553  5.930   2.418  1.00 73.53  ? 335 VAL   A CG2 1 
ATOM   1929 N N   . LEU   A 1 262 ? -8.653  5.492   5.823  1.00 70.47  ? 336 LEU   A N   1 
ATOM   1930 C CA  . LEU   A 1 262 ? -9.217  5.281   7.155  1.00 70.17  ? 336 LEU   A CA  1 
ATOM   1931 C C   . LEU   A 1 262 ? -9.973  3.960   7.236  1.00 71.82  ? 336 LEU   A C   1 
ATOM   1932 O O   . LEU   A 1 262 ? -9.889  3.251   8.245  1.00 70.38  ? 336 LEU   A O   1 
ATOM   1933 C CB  . LEU   A 1 262 ? -10.132 6.444   7.532  1.00 63.43  ? 336 LEU   A CB  1 
ATOM   1934 C CG  . LEU   A 1 262 ? -9.412  7.767   7.783  1.00 65.34  ? 336 LEU   A CG  1 
ATOM   1935 C CD1 . LEU   A 1 262 ? -10.411 8.864   8.115  1.00 68.35  ? 336 LEU   A CD1 1 
ATOM   1936 C CD2 . LEU   A 1 262 ? -8.385  7.614   8.892  1.00 61.32  ? 336 LEU   A CD2 1 
ATOM   1937 N N   . VAL   A 1 263 ? -10.716 3.612   6.182  1.00 75.54  ? 337 VAL   A N   1 
ATOM   1938 C CA  . VAL   A 1 263 ? -11.405 2.324   6.159  1.00 71.87  ? 337 VAL   A CA  1 
ATOM   1939 C C   . VAL   A 1 263 ? -10.398 1.179   6.230  1.00 74.78  ? 337 VAL   A C   1 
ATOM   1940 O O   . VAL   A 1 263 ? -10.603 0.195   6.955  1.00 72.17  ? 337 VAL   A O   1 
ATOM   1941 C CB  . VAL   A 1 263 ? -12.312 2.230   4.918  1.00 75.41  ? 337 VAL   A CB  1 
ATOM   1942 C CG1 . VAL   A 1 263 ? -12.773 0.801   4.688  1.00 77.78  ? 337 VAL   A CG1 1 
ATOM   1943 C CG2 . VAL   A 1 263 ? -13.513 3.143   5.090  1.00 74.25  ? 337 VAL   A CG2 1 
ATOM   1944 N N   . MET   A 1 264 ? -9.275  1.305   5.512  1.00 73.98  ? 338 MET   A N   1 
ATOM   1945 C CA  . MET   A 1 264 ? -8.227  0.287   5.582  1.00 65.24  ? 338 MET   A CA  1 
ATOM   1946 C C   . MET   A 1 264 ? -7.654  0.167   6.987  1.00 67.38  ? 338 MET   A C   1 
ATOM   1947 O O   . MET   A 1 264 ? -7.462  -0.944  7.494  1.00 70.34  ? 338 MET   A O   1 
ATOM   1948 C CB  . MET   A 1 264 ? -7.113  0.605   4.587  1.00 67.79  ? 338 MET   A CB  1 
ATOM   1949 C CG  . MET   A 1 264 ? -7.558  0.571   3.143  1.00 72.96  ? 338 MET   A CG  1 
ATOM   1950 S SD  . MET   A 1 264 ? -6.202  0.776   1.973  1.00 81.56  ? 338 MET   A SD  1 
ATOM   1951 C CE  . MET   A 1 264 ? -5.071  -0.496  2.530  1.00 72.14  ? 338 MET   A CE  1 
ATOM   1952 N N   . MET   A 1 265 ? -7.360  1.302   7.630  1.00 67.94  ? 339 MET   A N   1 
ATOM   1953 C CA  . MET   A 1 265 ? -6.785  1.270   8.971  1.00 62.91  ? 339 MET   A CA  1 
ATOM   1954 C C   . MET   A 1 265 ? -7.787  0.783   10.007 1.00 62.06  ? 339 MET   A C   1 
ATOM   1955 O O   . MET   A 1 265 ? -7.398  0.132   10.984 1.00 58.56  ? 339 MET   A O   1 
ATOM   1956 C CB  . MET   A 1 265 ? -6.273  2.659   9.354  1.00 61.23  ? 339 MET   A CB  1 
ATOM   1957 C CG  . MET   A 1 265 ? -5.360  3.278   8.308  1.00 66.84  ? 339 MET   A CG  1 
ATOM   1958 S SD  . MET   A 1 265 ? -4.655  4.855   8.807  1.00 60.39  ? 339 MET   A SD  1 
ATOM   1959 C CE  . MET   A 1 265 ? -3.717  4.343   10.239 1.00 56.36  ? 339 MET   A CE  1 
ATOM   1960 N N   . LEU   A 1 266 ? -9.073  1.085   9.814  1.00 62.51  ? 340 LEU   A N   1 
ATOM   1961 C CA  . LEU   A 1 266 ? -10.111 0.764   10.783 1.00 62.03  ? 340 LEU   A CA  1 
ATOM   1962 C C   . LEU   A 1 266 ? -10.795 -0.567  10.499 1.00 66.64  ? 340 LEU   A C   1 
ATOM   1963 O O   . LEU   A 1 266 ? -11.921 -0.785  10.965 1.00 67.84  ? 340 LEU   A O   1 
ATOM   1964 C CB  . LEU   A 1 266 ? -11.142 1.893   10.838 1.00 56.78  ? 340 LEU   A CB  1 
ATOM   1965 C CG  . LEU   A 1 266 ? -10.581 3.212   11.374 1.00 58.40  ? 340 LEU   A CG  1 
ATOM   1966 C CD1 . LEU   A 1 266 ? -11.663 4.263   11.516 1.00 58.61  ? 340 LEU   A CD1 1 
ATOM   1967 C CD2 . LEU   A 1 266 ? -9.874  2.996   12.704 1.00 53.32  ? 340 LEU   A CD2 1 
ATOM   1968 N N   . GLU   A 1 267 ? -10.146 -1.454  9.751  1.00 67.44  ? 341 GLU   A N   1 
ATOM   1969 C CA  . GLU   A 1 267 ? -10.680 -2.787  9.503  1.00 67.85  ? 341 GLU   A CA  1 
ATOM   1970 C C   . GLU   A 1 267 ? -10.752 -3.569  10.811 1.00 68.76  ? 341 GLU   A C   1 
ATOM   1971 O O   . GLU   A 1 267 ? -9.725  -3.716  11.492 1.00 71.14  ? 341 GLU   A O   1 
ATOM   1972 C CB  . GLU   A 1 267 ? -9.812  -3.526  8.487  1.00 67.27  ? 341 GLU   A CB  1 
ATOM   1973 C CG  . GLU   A 1 267 ? -9.922  -5.041  8.555  1.00 70.23  ? 341 GLU   A CG  1 
ATOM   1974 C CD  . GLU   A 1 267 ? -11.316 -5.552  8.234  1.00 78.27  ? 341 GLU   A CD  1 
ATOM   1975 O OE1 . GLU   A 1 267 ? -12.027 -4.908  7.432  1.00 83.98  ? 341 GLU   A OE1 1 
ATOM   1976 O OE2 . GLU   A 1 267 ? -11.706 -6.602  8.790  1.00 80.63  ? 341 GLU   A OE2 1 
ATOM   1977 N N   . PRO   A 1 268 ? -11.923 -4.080  11.199 1.00 67.95  ? 342 PRO   A N   1 
ATOM   1978 C CA  . PRO   A 1 268 ? -12.042 -4.711  12.524 1.00 69.19  ? 342 PRO   A CA  1 
ATOM   1979 C C   . PRO   A 1 268 ? -11.138 -5.919  12.723 1.00 71.84  ? 342 PRO   A C   1 
ATOM   1980 O O   . PRO   A 1 268 ? -10.732 -6.191  13.860 1.00 68.24  ? 342 PRO   A O   1 
ATOM   1981 C CB  . PRO   A 1 268 ? -13.525 -5.100  12.589 1.00 71.94  ? 342 PRO   A CB  1 
ATOM   1982 C CG  . PRO   A 1 268 ? -14.205 -4.189  11.617 1.00 69.25  ? 342 PRO   A CG  1 
ATOM   1983 C CD  . PRO   A 1 268 ? -13.222 -3.974  10.512 1.00 71.45  ? 342 PRO   A CD  1 
ATOM   1984 N N   . ASP   A 1 269 ? -10.800 -6.645  11.658 1.00 72.76  ? 343 ASP   A N   1 
ATOM   1985 C CA  . ASP   A 1 269 ? -10.043 -7.885  11.791 1.00 70.83  ? 343 ASP   A CA  1 
ATOM   1986 C C   . ASP   A 1 269 ? -8.548  -7.603  11.686 1.00 68.68  ? 343 ASP   A C   1 
ATOM   1987 O O   . ASP   A 1 269 ? -8.088  -7.162  10.624 1.00 71.51  ? 343 ASP   A O   1 
ATOM   1988 C CB  . ASP   A 1 269 ? -10.462 -8.878  10.717 1.00 72.04  ? 343 ASP   A CB  1 
ATOM   1989 C CG  . ASP   A 1 269 ? -10.229 -10.324 11.127 1.00 73.58  ? 343 ASP   A CG  1 
ATOM   1990 O OD1 . ASP   A 1 269 ? -9.252  -10.601 11.862 1.00 69.74  ? 343 ASP   A OD1 1 
ATOM   1991 O OD2 . ASP   A 1 269 ? -11.032 -11.187 10.707 1.00 72.05  ? 343 ASP   A OD2 1 
ATOM   1992 N N   . PRO   A 1 270 ? -7.758  -7.859  12.732 1.00 67.31  ? 344 PRO   A N   1 
ATOM   1993 C CA  . PRO   A 1 270 ? -6.311  -7.597  12.639 1.00 66.65  ? 344 PRO   A CA  1 
ATOM   1994 C C   . PRO   A 1 270 ? -5.610  -8.432  11.585 1.00 67.26  ? 344 PRO   A C   1 
ATOM   1995 O O   . PRO   A 1 270 ? -4.550  -8.023  11.095 1.00 69.02  ? 344 PRO   A O   1 
ATOM   1996 C CB  . PRO   A 1 270 ? -5.804  -7.942  14.045 1.00 61.47  ? 344 PRO   A CB  1 
ATOM   1997 C CG  . PRO   A 1 270 ? -6.789  -8.948  14.548 1.00 60.88  ? 344 PRO   A CG  1 
ATOM   1998 C CD  . PRO   A 1 270 ? -8.119  -8.499  14.009 1.00 65.99  ? 344 PRO   A CD  1 
ATOM   1999 N N   . LYS   A 1 271 ? -6.159  -9.595  11.227 1.00 70.03  ? 345 LYS   A N   1 
ATOM   2000 C CA  . LYS   A 1 271 ? -5.530  -10.421 10.205 1.00 69.62  ? 345 LYS   A CA  1 
ATOM   2001 C C   . LYS   A 1 271 ? -5.615  -9.770  8.833  1.00 67.74  ? 345 LYS   A C   1 
ATOM   2002 O O   . LYS   A 1 271 ? -4.746  -9.998  7.984  1.00 73.55  ? 345 LYS   A O   1 
ATOM   2003 C CB  . LYS   A 1 271 ? -6.176  -11.807 10.182 1.00 74.16  ? 345 LYS   A CB  1 
ATOM   2004 C CG  . LYS   A 1 271 ? -6.119  -12.539 11.519 1.00 78.01  ? 345 LYS   A CG  1 
ATOM   2005 C CD  . LYS   A 1 271 ? -6.788  -13.901 11.429 1.00 84.31  ? 345 LYS   A CD  1 
ATOM   2006 C CE  . LYS   A 1 271 ? -6.775  -14.625 12.768 1.00 94.41  ? 345 LYS   A CE  1 
ATOM   2007 N NZ  . LYS   A 1 271 ? -7.358  -15.998 12.659 1.00 100.28 ? 345 LYS   A NZ  1 
ATOM   2008 N N   . LEU   A 1 272 ? -6.641  -8.953  8.604  1.00 70.26  ? 346 LEU   A N   1 
ATOM   2009 C CA  . LEU   A 1 272 ? -6.857  -8.295  7.324  1.00 69.24  ? 346 LEU   A CA  1 
ATOM   2010 C C   . LEU   A 1 272 ? -6.488  -6.816  7.343  1.00 69.16  ? 346 LEU   A C   1 
ATOM   2011 O O   . LEU   A 1 272 ? -6.511  -6.174  6.289  1.00 72.52  ? 346 LEU   A O   1 
ATOM   2012 C CB  . LEU   A 1 272 ? -8.326  -8.442  6.900  1.00 72.91  ? 346 LEU   A CB  1 
ATOM   2013 C CG  . LEU   A 1 272 ? -9.011  -9.798  7.113  1.00 74.83  ? 346 LEU   A CG  1 
ATOM   2014 C CD1 . LEU   A 1 272 ? -10.524 -9.668  6.964  1.00 79.42  ? 346 LEU   A CD1 1 
ATOM   2015 C CD2 . LEU   A 1 272 ? -8.474  -10.846 6.146  1.00 71.75  ? 346 LEU   A CD2 1 
ATOM   2016 N N   . ARG   A 1 273 ? -6.158  -6.264  8.506  1.00 72.70  ? 347 ARG   A N   1 
ATOM   2017 C CA  . ARG   A 1 273 ? -5.861  -4.842  8.609  1.00 72.30  ? 347 ARG   A CA  1 
ATOM   2018 C C   . ARG   A 1 273 ? -4.536  -4.517  7.927  1.00 67.10  ? 347 ARG   A C   1 
ATOM   2019 O O   . ARG   A 1 273 ? -3.529  -5.202  8.138  1.00 61.15  ? 347 ARG   A O   1 
ATOM   2020 C CB  . ARG   A 1 273 ? -5.817  -4.423  10.079 1.00 63.61  ? 347 ARG   A CB  1 
ATOM   2021 C CG  . ARG   A 1 273 ? -5.758  -2.924  10.306 1.00 56.67  ? 347 ARG   A CG  1 
ATOM   2022 C CD  . ARG   A 1 273 ? -5.791  -2.625  11.790 1.00 57.29  ? 347 ARG   A CD  1 
ATOM   2023 N NE  . ARG   A 1 273 ? -6.963  -3.212  12.426 1.00 58.76  ? 347 ARG   A NE  1 
ATOM   2024 C CZ  . ARG   A 1 273 ? -6.974  -3.725  13.650 1.00 61.42  ? 347 ARG   A CZ  1 
ATOM   2025 N NH1 . ARG   A 1 273 ? -5.884  -3.748  14.400 1.00 52.82  ? 347 ARG   A NH1 1 
ATOM   2026 N NH2 . ARG   A 1 273 ? -8.106  -4.238  14.127 1.00 62.15  ? 347 ARG   A NH2 1 
ATOM   2027 N N   . ALA   A 1 274 ? -4.545  -3.462  7.111  1.00 63.59  ? 348 ALA   A N   1 
ATOM   2028 C CA  . ALA   A 1 274 ? -3.326  -2.985  6.471  1.00 65.38  ? 348 ALA   A CA  1 
ATOM   2029 C C   . ALA   A 1 274 ? -2.235  -2.726  7.502  1.00 64.93  ? 348 ALA   A C   1 
ATOM   2030 O O   . ALA   A 1 274 ? -2.503  -2.260  8.612  1.00 67.18  ? 348 ALA   A O   1 
ATOM   2031 C CB  . ALA   A 1 274 ? -3.610  -1.702  5.687  1.00 65.25  ? 348 ALA   A CB  1 
ATOM   2032 N N   . THR   A 1 275 ? -0.999  -3.037  7.132  1.00 64.39  ? 349 THR   A N   1 
ATOM   2033 C CA  . THR   A 1 275 ? 0.132   -2.728  7.992  1.00 61.07  ? 349 THR   A CA  1 
ATOM   2034 C C   . THR   A 1 275 ? 0.689   -1.353  7.649  1.00 62.87  ? 349 THR   A C   1 
ATOM   2035 O O   . THR   A 1 275 ? 0.431   -0.804  6.575  1.00 64.65  ? 349 THR   A O   1 
ATOM   2036 C CB  . THR   A 1 275 ? 1.229   -3.781  7.852  1.00 60.14  ? 349 THR   A CB  1 
ATOM   2037 O OG1 . THR   A 1 275 ? 1.701   -3.797  6.501  1.00 61.59  ? 349 THR   A OG1 1 
ATOM   2038 C CG2 . THR   A 1 275 ? 0.693   -5.154  8.217  1.00 63.75  ? 349 THR   A CG2 1 
ATOM   2039 N N   . ALA   A 1 276 ? 1.464   -0.797  8.586  1.00 59.08  ? 350 ALA   A N   1 
ATOM   2040 C CA  . ALA   A 1 276 ? 2.058   0.518   8.369  1.00 56.91  ? 350 ALA   A CA  1 
ATOM   2041 C C   . ALA   A 1 276 ? 2.962   0.519   7.142  1.00 61.77  ? 350 ALA   A C   1 
ATOM   2042 O O   . ALA   A 1 276 ? 3.020   1.512   6.408  1.00 64.04  ? 350 ALA   A O   1 
ATOM   2043 C CB  . ALA   A 1 276 ? 2.831   0.955   9.611  1.00 55.56  ? 350 ALA   A CB  1 
ATOM   2044 N N   . GLU   A 1 277 ? 3.674   -0.585  6.901  1.00 59.23  ? 351 GLU   A N   1 
ATOM   2045 C CA  . GLU   A 1 277 ? 4.468   -0.693  5.681  1.00 68.54  ? 351 GLU   A CA  1 
ATOM   2046 C C   . GLU   A 1 277 ? 3.579   -0.716  4.445  1.00 64.90  ? 351 GLU   A C   1 
ATOM   2047 O O   . GLU   A 1 277 ? 3.903   -0.087  3.429  1.00 67.80  ? 351 GLU   A O   1 
ATOM   2048 C CB  . GLU   A 1 277 ? 5.337   -1.949  5.717  1.00 73.33  ? 351 GLU   A CB  1 
ATOM   2049 C CG  . GLU   A 1 277 ? 6.658   -1.783  6.432  1.00 77.00  ? 351 GLU   A CG  1 
ATOM   2050 C CD  . GLU   A 1 277 ? 7.675   -2.822  6.000  1.00 92.57  ? 351 GLU   A CD  1 
ATOM   2051 O OE1 . GLU   A 1 277 ? 7.324   -3.679  5.156  1.00 84.75  ? 351 GLU   A OE1 1 
ATOM   2052 O OE2 . GLU   A 1 277 ? 8.822   -2.775  6.498  1.00 102.65 ? 351 GLU   A OE2 1 
ATOM   2053 N N   . ALA   A 1 278 ? 2.467   -1.455  4.509  1.00 66.06  ? 352 ALA   A N   1 
ATOM   2054 C CA  . ALA   A 1 278 ? 1.536   -1.502  3.385  1.00 70.19  ? 352 ALA   A CA  1 
ATOM   2055 C C   . ALA   A 1 278 ? 0.949   -0.125  3.104  1.00 65.56  ? 352 ALA   A C   1 
ATOM   2056 O O   . ALA   A 1 278 ? 0.864   0.296   1.945  1.00 64.69  ? 352 ALA   A O   1 
ATOM   2057 C CB  . ALA   A 1 278 ? 0.425   -2.521  3.662  1.00 61.70  ? 352 ALA   A CB  1 
ATOM   2058 N N   . LEU   A 1 279 ? 0.555   0.596   4.158  1.00 64.64  ? 353 LEU   A N   1 
ATOM   2059 C CA  . LEU   A 1 279 ? 0.018   1.943   3.991  1.00 66.14  ? 353 LEU   A CA  1 
ATOM   2060 C C   . LEU   A 1 279 ? 1.042   2.871   3.346  1.00 66.59  ? 353 LEU   A C   1 
ATOM   2061 O O   . LEU   A 1 279 ? 0.767   3.498   2.317  1.00 68.77  ? 353 LEU   A O   1 
ATOM   2062 C CB  . LEU   A 1 279 ? -0.437  2.490   5.346  1.00 63.33  ? 353 LEU   A CB  1 
ATOM   2063 C CG  . LEU   A 1 279 ? -1.607  1.740   5.987  1.00 61.26  ? 353 LEU   A CG  1 
ATOM   2064 C CD1 . LEU   A 1 279 ? -1.933  2.307   7.366  1.00 65.88  ? 353 LEU   A CD1 1 
ATOM   2065 C CD2 . LEU   A 1 279 ? -2.833  1.775   5.079  1.00 68.12  ? 353 LEU   A CD2 1 
ATOM   2066 N N   . LEU   A 1 280 ? 2.242   2.957   3.928  1.00 64.35  ? 354 LEU   A N   1 
ATOM   2067 C CA  . LEU   A 1 280 ? 3.267   3.842   3.389  1.00 63.58  ? 354 LEU   A CA  1 
ATOM   2068 C C   . LEU   A 1 280 ? 3.630   3.506   1.950  1.00 68.83  ? 354 LEU   A C   1 
ATOM   2069 O O   . LEU   A 1 280 ? 4.259   4.329   1.276  1.00 75.98  ? 354 LEU   A O   1 
ATOM   2070 C CB  . LEU   A 1 280 ? 4.517   3.794   4.267  1.00 64.91  ? 354 LEU   A CB  1 
ATOM   2071 C CG  . LEU   A 1 280 ? 4.427   4.546   5.600  1.00 62.25  ? 354 LEU   A CG  1 
ATOM   2072 C CD1 . LEU   A 1 280 ? 5.602   4.193   6.489  1.00 58.10  ? 354 LEU   A CD1 1 
ATOM   2073 C CD2 . LEU   A 1 280 ? 4.365   6.050   5.363  1.00 59.61  ? 354 LEU   A CD2 1 
ATOM   2074 N N   . ALA   A 1 281 ? 3.245   2.325   1.463  1.00 69.66  ? 355 ALA   A N   1 
ATOM   2075 C CA  . ALA   A 1 281 ? 3.508   1.921   0.085  1.00 73.90  ? 355 ALA   A CA  1 
ATOM   2076 C C   . ALA   A 1 281 ? 2.363   2.255   -0.863 1.00 75.74  ? 355 ALA   A C   1 
ATOM   2077 O O   . ALA   A 1 281 ? 2.445   1.922   -2.051 1.00 80.65  ? 355 ALA   A O   1 
ATOM   2078 C CB  . ALA   A 1 281 ? 3.805   0.418   0.017  1.00 75.16  ? 355 ALA   A CB  1 
ATOM   2079 N N   . LEU   A 1 282 ? 1.303   2.894   -0.372 1.00 75.45  ? 356 LEU   A N   1 
ATOM   2080 C CA  . LEU   A 1 282 ? 0.193   3.291   -1.219 1.00 76.71  ? 356 LEU   A CA  1 
ATOM   2081 C C   . LEU   A 1 282 ? 0.546   4.544   -2.014 1.00 83.76  ? 356 LEU   A C   1 
ATOM   2082 O O   . LEU   A 1 282 ? 1.452   5.296   -1.638 1.00 80.10  ? 356 LEU   A O   1 
ATOM   2083 C CB  . LEU   A 1 282 ? -1.051  3.532   -0.370 1.00 79.07  ? 356 LEU   A CB  1 
ATOM   2084 C CG  . LEU   A 1 282 ? -1.666  2.272   0.240  1.00 78.06  ? 356 LEU   A CG  1 
ATOM   2085 C CD1 . LEU   A 1 282 ? -2.882  2.605   1.104  1.00 69.03  ? 356 LEU   A CD1 1 
ATOM   2086 C CD2 . LEU   A 1 282 ? -2.024  1.272   -0.858 1.00 72.17  ? 356 LEU   A CD2 1 
ATOM   2087 N N   . PRO   A 1 283 ? -0.145  4.778   -3.138 1.00 89.73  ? 357 PRO   A N   1 
ATOM   2088 C CA  . PRO   A 1 283 ? 0.132   5.998   -3.922 1.00 88.42  ? 357 PRO   A CA  1 
ATOM   2089 C C   . PRO   A 1 283 ? -0.122  7.291   -3.157 1.00 88.80  ? 357 PRO   A C   1 
ATOM   2090 O O   . PRO   A 1 283 ? 0.704   8.212   -3.214 1.00 90.45  ? 357 PRO   A O   1 
ATOM   2091 C CB  . PRO   A 1 283 ? -0.810  5.854   -5.128 1.00 90.02  ? 357 PRO   A CB  1 
ATOM   2092 C CG  . PRO   A 1 283 ? -1.078  4.386   -5.235 1.00 90.17  ? 357 PRO   A CG  1 
ATOM   2093 C CD  . PRO   A 1 283 ? -1.079  3.870   -3.833 1.00 84.00  ? 357 PRO   A CD  1 
ATOM   2094 N N   . VAL   A 1 284 ? -1.241  7.382   -2.431 1.00 84.44  ? 358 VAL   A N   1 
ATOM   2095 C CA  . VAL   A 1 284 ? -1.615  8.636   -1.782 1.00 87.37  ? 358 VAL   A CA  1 
ATOM   2096 C C   . VAL   A 1 284 ? -0.612  9.023   -0.705 1.00 88.20  ? 358 VAL   A C   1 
ATOM   2097 O O   . VAL   A 1 284 ? -0.465  10.208  -0.381 1.00 89.66  ? 358 VAL   A O   1 
ATOM   2098 C CB  . VAL   A 1 284 ? -3.043  8.535   -1.208 1.00 89.50  ? 358 VAL   A CB  1 
ATOM   2099 C CG1 . VAL   A 1 284 ? -4.054  8.337   -2.330 1.00 88.19  ? 358 VAL   A CG1 1 
ATOM   2100 C CG2 . VAL   A 1 284 ? -3.131  7.401   -0.191 1.00 77.15  ? 358 VAL   A CG2 1 
ATOM   2101 N N   . LEU   A 1 285 ? 0.087   8.046   -0.136 1.00 83.85  ? 359 LEU   A N   1 
ATOM   2102 C CA  . LEU   A 1 285 ? 1.086   8.305   0.900  1.00 85.86  ? 359 LEU   A CA  1 
ATOM   2103 C C   . LEU   A 1 285 ? 2.494   8.291   0.304  1.00 92.07  ? 359 LEU   A C   1 
ATOM   2104 O O   . LEU   A 1 285 ? 3.374   7.530   0.710  1.00 92.89  ? 359 LEU   A O   1 
ATOM   2105 C CB  . LEU   A 1 285 ? 0.943   7.292   2.034  1.00 79.37  ? 359 LEU   A CB  1 
ATOM   2106 C CG  . LEU   A 1 285 ? -0.296  7.496   2.907  1.00 76.18  ? 359 LEU   A CG  1 
ATOM   2107 C CD1 . LEU   A 1 285 ? -0.613  6.259   3.742  1.00 69.64  ? 359 LEU   A CD1 1 
ATOM   2108 C CD2 . LEU   A 1 285 ? -0.105  8.715   3.799  1.00 71.47  ? 359 LEU   A CD2 1 
ATOM   2109 N N   . ARG   A 1 286 ? 2.696   9.162   -0.679 1.00 94.72  ? 360 ARG   A N   1 
ATOM   2110 C CA  . ARG   A 1 286 ? 3.993   9.337   -1.311 1.00 95.76  ? 360 ARG   A CA  1 
ATOM   2111 C C   . ARG   A 1 286 ? 4.821   10.376  -0.556 1.00 96.12  ? 360 ARG   A C   1 
ATOM   2112 O O   . ARG   A 1 286 ? 4.337   11.060  0.349  1.00 90.83  ? 360 ARG   A O   1 
ATOM   2113 C CB  . ARG   A 1 286 ? 3.814   9.747   -2.772 1.00 101.79 ? 360 ARG   A CB  1 
ATOM   2114 C CG  . ARG   A 1 286 ? 2.829   10.889  -2.970 1.00 104.53 ? 360 ARG   A CG  1 
ATOM   2115 C CD  . ARG   A 1 286 ? 2.512   11.092  -4.442 1.00 109.89 ? 360 ARG   A CD  1 
ATOM   2116 N NE  . ARG   A 1 286 ? 3.683   11.499  -5.209 1.00 113.76 ? 360 ARG   A NE  1 
ATOM   2117 C CZ  . ARG   A 1 286 ? 3.692   11.684  -6.523 1.00 123.55 ? 360 ARG   A CZ  1 
ATOM   2118 N NH1 . ARG   A 1 286 ? 2.607   11.491  -7.256 1.00 122.22 ? 360 ARG   A NH1 1 
ATOM   2119 N NH2 . ARG   A 1 286 ? 4.818   12.073  -7.118 1.00 122.96 ? 360 ARG   A NH2 1 
ATOM   2120 N N   . GLN   A 1 287 ? 6.089   10.488  -0.947 1.00 100.54 ? 361 GLN   A N   1 
ATOM   2121 C CA  . GLN   A 1 287 ? 7.035   11.401  -0.305 1.00 98.07  ? 361 GLN   A CA  1 
ATOM   2122 C C   . GLN   A 1 287 ? 6.539   12.842  -0.319 1.00 98.22  ? 361 GLN   A C   1 
ATOM   2123 O O   . GLN   A 1 287 ? 6.143   13.374  0.716  1.00 90.49  ? 361 GLN   A O   1 
ATOM   2124 C CB  . GLN   A 1 287 ? 8.399   11.323  -0.992 1.00 98.75  ? 361 GLN   A CB  1 
ATOM   2125 C CG  . GLN   A 1 287 ? 8.461   12.042  -2.334 1.00 103.12 ? 361 GLN   A CG  1 
ATOM   2126 C CD  . GLN   A 1 287 ? 9.696   11.666  -3.135 1.00 110.65 ? 361 GLN   A CD  1 
ATOM   2127 O OE1 . GLN   A 1 287 ? 10.212  10.556  -3.008 1.00 110.23 ? 361 GLN   A OE1 1 
ATOM   2128 N NE2 . GLN   A 1 287 ? 10.178  12.592  -3.962 1.00 113.09 ? 361 GLN   A NE2 1 
ATOM   2129 N N   . LEU   B 1 3   ? -23.018 40.203  46.136 1.00 89.74  ? 77  LEU   B N   1 
ATOM   2130 C CA  . LEU   B 1 3   ? -22.141 40.565  45.026 1.00 88.43  ? 77  LEU   B CA  1 
ATOM   2131 C C   . LEU   B 1 3   ? -22.658 39.956  43.728 1.00 89.05  ? 77  LEU   B C   1 
ATOM   2132 O O   . LEU   B 1 3   ? -22.992 38.772  43.685 1.00 94.41  ? 77  LEU   B O   1 
ATOM   2133 C CB  . LEU   B 1 3   ? -20.708 40.102  45.297 1.00 84.85  ? 77  LEU   B CB  1 
ATOM   2134 C CG  . LEU   B 1 3   ? -19.680 40.342  44.192 1.00 85.45  ? 77  LEU   B CG  1 
ATOM   2135 C CD1 . LEU   B 1 3   ? -19.393 41.835  44.025 1.00 82.15  ? 77  LEU   B CD1 1 
ATOM   2136 C CD2 . LEU   B 1 3   ? -18.396 39.555  44.458 1.00 80.68  ? 77  LEU   B CD2 1 
ATOM   2137 N N   . GLN   B 1 4   ? -22.733 40.763  42.675 1.00 84.13  ? 78  GLN   B N   1 
ATOM   2138 C CA  . GLN   B 1 4   ? -23.268 40.303  41.402 1.00 85.27  ? 78  GLN   B CA  1 
ATOM   2139 C C   . GLN   B 1 4   ? -22.675 41.153  40.289 1.00 79.76  ? 78  GLN   B C   1 
ATOM   2140 O O   . GLN   B 1 4   ? -22.160 42.249  40.547 1.00 72.94  ? 78  GLN   B O   1 
ATOM   2141 C CB  . GLN   B 1 4   ? -24.805 40.353  41.394 1.00 86.07  ? 78  GLN   B CB  1 
ATOM   2142 C CG  . GLN   B 1 4   ? -25.426 41.615  41.957 1.00 88.78  ? 78  GLN   B CG  1 
ATOM   2143 C CD  . GLN   B 1 4   ? -26.942 41.522  42.000 1.00 90.31  ? 78  GLN   B CD  1 
ATOM   2144 O OE1 . GLN   B 1 4   ? -27.555 40.886  41.143 1.00 90.07  ? 78  GLN   B OE1 1 
ATOM   2145 N NE2 . GLN   B 1 4   ? -27.552 42.143  43.006 1.00 94.25  ? 78  GLN   B NE2 1 
ATOM   2146 N N   . PRO   B 1 5   ? -22.711 40.673  39.044 1.00 76.71  ? 79  PRO   B N   1 
ATOM   2147 C CA  . PRO   B 1 5   ? -21.997 41.362  37.965 1.00 66.69  ? 79  PRO   B CA  1 
ATOM   2148 C C   . PRO   B 1 5   ? -22.683 42.652  37.555 1.00 68.04  ? 79  PRO   B C   1 
ATOM   2149 O O   . PRO   B 1 5   ? -23.847 42.915  37.861 1.00 72.09  ? 79  PRO   B O   1 
ATOM   2150 C CB  . PRO   B 1 5   ? -22.030 40.350  36.822 1.00 68.36  ? 79  PRO   B CB  1 
ATOM   2151 C CG  . PRO   B 1 5   ? -23.300 39.625  37.050 1.00 75.20  ? 79  PRO   B CG  1 
ATOM   2152 C CD  . PRO   B 1 5   ? -23.377 39.457  38.542 1.00 75.97  ? 79  PRO   B CD  1 
ATOM   2153 N N   . ARG   B 1 6   ? -21.923 43.452  36.812 1.00 64.97  ? 80  ARG   B N   1 
ATOM   2154 C CA  . ARG   B 1 6   ? -22.371 44.736  36.296 1.00 61.32  ? 80  ARG   B CA  1 
ATOM   2155 C C   . ARG   B 1 6   ? -21.785 44.898  34.904 1.00 59.48  ? 80  ARG   B C   1 
ATOM   2156 O O   . ARG   B 1 6   ? -20.562 44.845  34.746 1.00 64.42  ? 80  ARG   B O   1 
ATOM   2157 C CB  . ARG   B 1 6   ? -21.916 45.871  37.215 1.00 60.94  ? 80  ARG   B CB  1 
ATOM   2158 C CG  . ARG   B 1 6   ? -22.128 47.254  36.649 1.00 64.78  ? 80  ARG   B CG  1 
ATOM   2159 C CD  . ARG   B 1 6   ? -21.545 48.304  37.575 1.00 66.59  ? 80  ARG   B CD  1 
ATOM   2160 N NE  . ARG   B 1 6   ? -21.736 49.648  37.047 1.00 72.57  ? 80  ARG   B NE  1 
ATOM   2161 C CZ  . ARG   B 1 6   ? -20.930 50.224  36.167 1.00 73.64  ? 80  ARG   B CZ  1 
ATOM   2162 N NH1 . ARG   B 1 6   ? -19.867 49.595  35.690 1.00 66.27  ? 80  ARG   B NH1 1 
ATOM   2163 N NH2 . ARG   B 1 6   ? -21.198 51.462  35.754 1.00 71.21  ? 80  ARG   B NH2 1 
ATOM   2164 N N   . ARG   B 1 7   ? -22.640 45.080  33.897 1.00 62.17  ? 81  ARG   B N   1 
ATOM   2165 C CA  . ARG   B 1 7   ? -22.143 45.175  32.528 1.00 61.54  ? 81  ARG   B CA  1 
ATOM   2166 C C   . ARG   B 1 7   ? -21.327 46.446  32.335 1.00 61.63  ? 81  ARG   B C   1 
ATOM   2167 O O   . ARG   B 1 7   ? -21.651 47.504  32.880 1.00 65.45  ? 81  ARG   B O   1 
ATOM   2168 C CB  . ARG   B 1 7   ? -23.289 45.151  31.514 1.00 63.01  ? 81  ARG   B CB  1 
ATOM   2169 C CG  . ARG   B 1 7   ? -22.809 44.797  30.099 1.00 73.28  ? 81  ARG   B CG  1 
ATOM   2170 C CD  . ARG   B 1 7   ? -23.633 45.452  28.993 1.00 80.13  ? 81  ARG   B CD  1 
ATOM   2171 N NE  . ARG   B 1 7   ? -23.267 44.951  27.669 1.00 84.41  ? 81  ARG   B NE  1 
ATOM   2172 C CZ  . ARG   B 1 7   ? -23.803 45.371  26.529 1.00 78.99  ? 81  ARG   B CZ  1 
ATOM   2173 N NH1 . ARG   B 1 7   ? -24.721 46.322  26.505 1.00 77.17  ? 81  ARG   B NH1 1 
ATOM   2174 N NH2 . ARG   B 1 7   ? -23.408 44.820  25.383 1.00 72.45  ? 81  ARG   B NH2 1 
ATOM   2175 N N   . VAL   B 1 8   ? -20.260 46.337  31.552 1.00 65.42  ? 82  VAL   B N   1 
ATOM   2176 C CA  . VAL   B 1 8   ? -19.416 47.474  31.205 1.00 64.96  ? 82  VAL   B CA  1 
ATOM   2177 C C   . VAL   B 1 8   ? -19.655 47.805  29.740 1.00 69.25  ? 82  VAL   B C   1 
ATOM   2178 O O   . VAL   B 1 8   ? -19.425 46.969  28.856 1.00 69.16  ? 82  VAL   B O   1 
ATOM   2179 C CB  . VAL   B 1 8   ? -17.928 47.192  31.461 1.00 56.72  ? 82  VAL   B CB  1 
ATOM   2180 C CG1 . VAL   B 1 8   ? -17.099 48.395  31.054 1.00 55.90  ? 82  VAL   B CG1 1 
ATOM   2181 C CG2 . VAL   B 1 8   ? -17.690 46.851  32.919 1.00 57.69  ? 82  VAL   B CG2 1 
ATOM   2182 N N   . SER   B 1 9   ? -20.117 49.021  29.482 1.00 78.87  ? 83  SER   B N   1 
ATOM   2183 C CA  . SER   B 1 9   ? -20.242 49.500  28.119 1.00 79.47  ? 83  SER   B CA  1 
ATOM   2184 C C   . SER   B 1 9   ? -20.061 51.007  28.120 1.00 84.93  ? 83  SER   B C   1 
ATOM   2185 O O   . SER   B 1 9   ? -20.319 51.681  29.121 1.00 85.16  ? 83  SER   B O   1 
ATOM   2186 C CB  . SER   B 1 9   ? -21.593 49.119  27.500 1.00 74.61  ? 83  SER   B CB  1 
ATOM   2187 O OG  . SER   B 1 9   ? -21.621 49.453  26.122 1.00 74.35  ? 83  SER   B OG  1 
ATOM   2188 N N   . PHE   B 1 10  ? -19.596 51.524  26.986 1.00 90.05  ? 84  PHE   B N   1 
ATOM   2189 C CA  . PHE   B 1 10  ? -19.564 52.955  26.717 1.00 91.93  ? 84  PHE   B CA  1 
ATOM   2190 C C   . PHE   B 1 10  ? -20.652 53.332  25.710 1.00 99.85  ? 84  PHE   B C   1 
ATOM   2191 O O   . PHE   B 1 10  ? -20.471 54.231  24.884 1.00 99.13  ? 84  PHE   B O   1 
ATOM   2192 C CB  . PHE   B 1 10  ? -18.169 53.373  26.250 1.00 87.20  ? 84  PHE   B CB  1 
ATOM   2193 C CG  . PHE   B 1 10  ? -17.088 53.139  27.284 1.00 85.69  ? 84  PHE   B CG  1 
ATOM   2194 C CD1 . PHE   B 1 10  ? -16.603 51.858  27.530 1.00 80.43  ? 84  PHE   B CD1 1 
ATOM   2195 C CD2 . PHE   B 1 10  ? -16.568 54.196  28.020 1.00 84.16  ? 84  PHE   B CD2 1 
ATOM   2196 C CE1 . PHE   B 1 10  ? -15.617 51.638  28.489 1.00 74.36  ? 84  PHE   B CE1 1 
ATOM   2197 C CE2 . PHE   B 1 10  ? -15.577 53.980  28.980 1.00 78.36  ? 84  PHE   B CE2 1 
ATOM   2198 C CZ  . PHE   B 1 10  ? -15.104 52.701  29.212 1.00 73.56  ? 84  PHE   B CZ  1 
ATOM   2199 N N   . ARG   B 1 11  ? -21.791 52.627  25.793 1.00 113.92 ? 85  ARG   B N   1 
ATOM   2200 C CA  . ARG   B 1 11  ? -22.980 52.825  24.956 1.00 112.10 ? 85  ARG   B CA  1 
ATOM   2201 C C   . ARG   B 1 11  ? -22.733 52.409  23.503 1.00 112.57 ? 85  ARG   B C   1 
ATOM   2202 O O   . ARG   B 1 11  ? -23.169 53.074  22.561 1.00 115.18 ? 85  ARG   B O   1 
ATOM   2203 C CB  . ARG   B 1 11  ? -23.506 54.260  25.057 1.00 114.87 ? 85  ARG   B CB  1 
ATOM   2204 C CG  . ARG   B 1 11  ? -24.338 54.473  26.318 1.00 116.69 ? 85  ARG   B CG  1 
ATOM   2205 C CD  . ARG   B 1 11  ? -24.466 55.934  26.705 1.00 125.81 ? 85  ARG   B CD  1 
ATOM   2206 N NE  . ARG   B 1 11  ? -25.580 56.153  27.621 1.00 128.27 ? 85  ARG   B NE  1 
ATOM   2207 C CZ  . ARG   B 1 11  ? -25.894 57.326  28.156 1.00 129.47 ? 85  ARG   B CZ  1 
ATOM   2208 N NH1 . ARG   B 1 11  ? -25.166 58.407  27.927 1.00 135.05 ? 85  ARG   B NH1 1 
ATOM   2209 N NH2 . ARG   B 1 11  ? -26.969 57.419  28.936 1.00 126.82 ? 85  ARG   B NH2 1 
ATOM   2210 N N   . GLY   B 1 12  ? -22.049 51.281  23.330 1.00 102.22 ? 86  GLY   B N   1 
ATOM   2211 C CA  . GLY   B 1 12  ? -21.827 50.692  22.023 1.00 92.78  ? 86  GLY   B CA  1 
ATOM   2212 C C   . GLY   B 1 12  ? -21.849 49.177  22.075 1.00 76.21  ? 86  GLY   B C   1 
ATOM   2213 O O   . GLY   B 1 12  ? -21.907 48.511  21.044 1.00 77.52  ? 86  GLY   B O   1 
ATOM   2214 N N   . GLN   B 1 19  ? -27.645 40.744  30.978 1.00 95.18  ? 93  GLN   B N   1 
ATOM   2215 C CA  . GLN   B 1 19  ? -26.985 39.593  31.584 1.00 99.46  ? 93  GLN   B CA  1 
ATOM   2216 C C   . GLN   B 1 19  ? -27.754 38.290  31.340 1.00 105.62 ? 93  GLN   B C   1 
ATOM   2217 O O   . GLN   B 1 19  ? -28.940 38.314  31.006 1.00 118.69 ? 93  GLN   B O   1 
ATOM   2218 C CB  . GLN   B 1 19  ? -26.794 39.830  33.081 1.00 93.45  ? 93  GLN   B CB  1 
ATOM   2219 C CG  . GLN   B 1 19  ? -25.786 40.926  33.381 1.00 92.78  ? 93  GLN   B CG  1 
ATOM   2220 C CD  . GLN   B 1 19  ? -24.390 40.591  32.870 1.00 89.53  ? 93  GLN   B CD  1 
ATOM   2221 O OE1 . GLN   B 1 19  ? -23.882 41.224  31.944 1.00 86.77  ? 93  GLN   B OE1 1 
ATOM   2222 N NE2 . GLN   B 1 19  ? -23.762 39.592  33.478 1.00 87.31  ? 93  GLN   B NE2 1 
ATOM   2223 N N   . SER   B 1 20  ? -27.065 37.164  31.521 1.00 100.96 ? 94  SER   B N   1 
ATOM   2224 C CA  . SER   B 1 20  ? -27.623 35.865  31.169 1.00 106.14 ? 94  SER   B CA  1 
ATOM   2225 C C   . SER   B 1 20  ? -28.887 35.572  31.973 1.00 118.56 ? 94  SER   B C   1 
ATOM   2226 O O   . SER   B 1 20  ? -28.970 35.924  33.157 1.00 118.47 ? 94  SER   B O   1 
ATOM   2227 C CB  . SER   B 1 20  ? -26.594 34.764  31.409 1.00 103.77 ? 94  SER   B CB  1 
ATOM   2228 O OG  . SER   B 1 20  ? -25.583 34.801  30.421 1.00 109.08 ? 94  SER   B OG  1 
ATOM   2229 N N   . PRO   B 1 21  ? -29.883 34.912  31.370 1.00 125.47 ? 95  PRO   B N   1 
ATOM   2230 C CA  . PRO   B 1 21  ? -31.144 34.655  32.088 1.00 126.97 ? 95  PRO   B CA  1 
ATOM   2231 C C   . PRO   B 1 21  ? -31.093 33.492  33.067 1.00 128.52 ? 95  PRO   B C   1 
ATOM   2232 O O   . PRO   B 1 21  ? -31.914 33.455  33.996 1.00 126.23 ? 95  PRO   B O   1 
ATOM   2233 C CB  . PRO   B 1 21  ? -32.130 34.355  30.952 1.00 125.85 ? 95  PRO   B CB  1 
ATOM   2234 C CG  . PRO   B 1 21  ? -31.273 33.767  29.879 1.00 122.40 ? 95  PRO   B CG  1 
ATOM   2235 C CD  . PRO   B 1 21  ? -29.957 34.498  29.956 1.00 122.73 ? 95  PRO   B CD  1 
ATOM   2236 N N   . GLY   B 1 22  ? -30.186 32.527  32.883 1.00 143.39 ? 96  GLY   B N   1 
ATOM   2237 C CA  . GLY   B 1 22  ? -30.127 31.390  33.790 1.00 145.54 ? 96  GLY   B CA  1 
ATOM   2238 C C   . GLY   B 1 22  ? -29.444 31.678  35.113 1.00 145.07 ? 96  GLY   B C   1 
ATOM   2239 O O   . GLY   B 1 22  ? -29.828 31.115  36.145 1.00 148.91 ? 96  GLY   B O   1 
ATOM   2240 N N   . TYR   B 1 23  ? -28.437 32.549  35.105 1.00 121.76 ? 97  TYR   B N   1 
ATOM   2241 C CA  . TYR   B 1 23  ? -27.703 32.899  36.317 1.00 110.65 ? 97  TYR   B CA  1 
ATOM   2242 C C   . TYR   B 1 23  ? -28.633 33.450  37.391 1.00 107.73 ? 97  TYR   B C   1 
ATOM   2243 O O   . TYR   B 1 23  ? -29.385 34.400  37.156 1.00 102.85 ? 97  TYR   B O   1 
ATOM   2244 C CB  . TYR   B 1 23  ? -26.615 33.925  35.982 1.00 104.35 ? 97  TYR   B CB  1 
ATOM   2245 C CG  . TYR   B 1 23  ? -26.129 34.787  37.137 1.00 95.44  ? 97  TYR   B CG  1 
ATOM   2246 C CD1 . TYR   B 1 23  ? -25.107 34.353  37.971 1.00 94.26  ? 97  TYR   B CD1 1 
ATOM   2247 C CD2 . TYR   B 1 23  ? -26.670 36.050  37.368 1.00 91.68  ? 97  TYR   B CD2 1 
ATOM   2248 C CE1 . TYR   B 1 23  ? -24.651 35.139  39.015 1.00 91.91  ? 97  TYR   B CE1 1 
ATOM   2249 C CE2 . TYR   B 1 23  ? -26.221 36.843  38.413 1.00 91.32  ? 97  TYR   B CE2 1 
ATOM   2250 C CZ  . TYR   B 1 23  ? -25.210 36.381  39.232 1.00 90.99  ? 97  TYR   B CZ  1 
ATOM   2251 O OH  . TYR   B 1 23  ? -24.755 37.161  40.273 1.00 87.90  ? 97  TYR   B OH  1 
ATOM   2252 N N   . ASP   B 1 24  ? -28.578 32.844  38.574 1.00 105.25 ? 98  ASP   B N   1 
ATOM   2253 C CA  . ASP   B 1 24  ? -29.346 33.291  39.722 1.00 107.64 ? 98  ASP   B CA  1 
ATOM   2254 C C   . ASP   B 1 24  ? -28.403 33.841  40.780 1.00 106.25 ? 98  ASP   B C   1 
ATOM   2255 O O   . ASP   B 1 24  ? -27.438 33.160  41.152 1.00 108.75 ? 98  ASP   B O   1 
ATOM   2256 C CB  . ASP   B 1 24  ? -30.173 32.139  40.300 1.00 111.03 ? 98  ASP   B CB  1 
ATOM   2257 C CG  . ASP   B 1 24  ? -31.041 32.571  41.462 1.00 114.71 ? 98  ASP   B CG  1 
ATOM   2258 O OD1 . ASP   B 1 24  ? -31.868 33.491  41.280 1.00 115.48 ? 98  ASP   B OD1 1 
ATOM   2259 O OD2 . ASP   B 1 24  ? -30.902 31.982  42.554 1.00 121.18 ? 98  ASP   B OD2 1 
ATOM   2260 N N   . PRO   B 1 25  ? -28.635 35.056  41.281 1.00 105.05 ? 99  PRO   B N   1 
ATOM   2261 C CA  . PRO   B 1 25  ? -27.678 35.698  42.203 1.00 104.18 ? 99  PRO   B CA  1 
ATOM   2262 C C   . PRO   B 1 25  ? -27.794 35.182  43.634 1.00 116.12 ? 99  PRO   B C   1 
ATOM   2263 O O   . PRO   B 1 25  ? -27.990 35.946  44.582 1.00 119.10 ? 99  PRO   B O   1 
ATOM   2264 C CB  . PRO   B 1 25  ? -28.057 37.184  42.090 1.00 97.11  ? 99  PRO   B CB  1 
ATOM   2265 C CG  . PRO   B 1 25  ? -29.120 37.283  41.017 1.00 93.74  ? 99  PRO   B CG  1 
ATOM   2266 C CD  . PRO   B 1 25  ? -29.755 35.947  40.949 1.00 100.37 ? 99  PRO   B CD  1 
ATOM   2267 N N   . SER   B 1 26  ? -27.665 33.863  43.803 1.00 122.59 ? 100 SER   B N   1 
ATOM   2268 C CA  . SER   B 1 26  ? -27.774 33.243  45.121 1.00 124.67 ? 100 SER   B CA  1 
ATOM   2269 C C   . SER   B 1 26  ? -26.526 32.455  45.494 1.00 128.67 ? 100 SER   B C   1 
ATOM   2270 O O   . SER   B 1 26  ? -25.872 32.787  46.489 1.00 131.42 ? 100 SER   B O   1 
ATOM   2271 C CB  . SER   B 1 26  ? -29.014 32.341  45.187 1.00 130.45 ? 100 SER   B CB  1 
ATOM   2272 O OG  . SER   B 1 26  ? -28.781 31.095  44.551 1.00 133.64 ? 100 SER   B OG  1 
ATOM   2273 N N   . ARG   B 1 27  ? -26.186 31.409  44.744 1.00 127.09 ? 101 ARG   B N   1 
ATOM   2274 C CA  . ARG   B 1 27  ? -24.973 30.659  45.030 1.00 127.02 ? 101 ARG   B CA  1 
ATOM   2275 C C   . ARG   B 1 27  ? -23.764 31.589  44.939 1.00 126.20 ? 101 ARG   B C   1 
ATOM   2276 O O   . ARG   B 1 27  ? -23.748 32.508  44.111 1.00 120.97 ? 101 ARG   B O   1 
ATOM   2277 C CB  . ARG   B 1 27  ? -24.823 29.484  44.060 1.00 120.23 ? 101 ARG   B CB  1 
ATOM   2278 C CG  . ARG   B 1 27  ? -25.854 28.383  44.251 1.00 122.33 ? 101 ARG   B CG  1 
ATOM   2279 C CD  . ARG   B 1 27  ? -25.827 27.393  43.096 1.00 126.19 ? 101 ARG   B CD  1 
ATOM   2280 N NE  . ARG   B 1 27  ? -24.687 26.483  43.147 1.00 127.65 ? 101 ARG   B NE  1 
ATOM   2281 C CZ  . ARG   B 1 27  ? -24.765 25.199  43.474 1.00 125.19 ? 101 ARG   B CZ  1 
ATOM   2282 N NH1 . ARG   B 1 27  ? -25.918 24.638  43.809 1.00 122.33 ? 101 ARG   B NH1 1 
ATOM   2283 N NH2 . ARG   B 1 27  ? -23.661 24.457  43.456 1.00 118.40 ? 101 ARG   B NH2 1 
ATOM   2284 N N   . PRO   B 1 28  ? -22.744 31.394  45.780 1.00 135.20 ? 102 PRO   B N   1 
ATOM   2285 C CA  . PRO   B 1 28  ? -21.639 32.365  45.836 1.00 130.40 ? 102 PRO   B CA  1 
ATOM   2286 C C   . PRO   B 1 28  ? -20.789 32.419  44.578 1.00 126.86 ? 102 PRO   B C   1 
ATOM   2287 O O   . PRO   B 1 28  ? -20.011 33.371  44.431 1.00 128.08 ? 102 PRO   B O   1 
ATOM   2288 C CB  . PRO   B 1 28  ? -20.813 31.886  47.037 1.00 136.17 ? 102 PRO   B CB  1 
ATOM   2289 C CG  . PRO   B 1 28  ? -21.110 30.425  47.132 1.00 137.59 ? 102 PRO   B CG  1 
ATOM   2290 C CD  . PRO   B 1 28  ? -22.549 30.276  46.720 1.00 137.08 ? 102 PRO   B CD  1 
ATOM   2291 N N   . GLU   B 1 29  ? -20.906 31.448  43.674 1.00 119.99 ? 103 GLU   B N   1 
ATOM   2292 C CA  . GLU   B 1 29  ? -20.063 31.433  42.486 1.00 115.95 ? 103 GLU   B CA  1 
ATOM   2293 C C   . GLU   B 1 29  ? -20.317 32.666  41.624 1.00 104.34 ? 103 GLU   B C   1 
ATOM   2294 O O   . GLU   B 1 29  ? -21.436 33.183  41.548 1.00 100.08 ? 103 GLU   B O   1 
ATOM   2295 C CB  . GLU   B 1 29  ? -20.302 30.161  41.668 1.00 111.90 ? 103 GLU   B CB  1 
ATOM   2296 C CG  . GLU   B 1 29  ? -19.770 28.884  42.306 1.00 115.38 ? 103 GLU   B CG  1 
ATOM   2297 C CD  . GLU   B 1 29  ? -20.732 28.281  43.318 1.00 127.20 ? 103 GLU   B CD  1 
ATOM   2298 O OE1 . GLU   B 1 29  ? -21.694 28.971  43.716 1.00 123.77 ? 103 GLU   B OE1 1 
ATOM   2299 O OE2 . GLU   B 1 29  ? -20.527 27.111  43.712 1.00 131.20 ? 103 GLU   B OE2 1 
ATOM   2300 N N   . SER   B 1 30  ? -19.255 33.137  40.976 1.00 91.84  ? 104 SER   B N   1 
ATOM   2301 C CA  . SER   B 1 30  ? -19.342 34.318  40.132 1.00 86.89  ? 104 SER   B CA  1 
ATOM   2302 C C   . SER   B 1 30  ? -20.242 34.056  38.925 1.00 85.15  ? 104 SER   B C   1 
ATOM   2303 O O   . SER   B 1 30  ? -20.521 32.912  38.558 1.00 91.55  ? 104 SER   B O   1 
ATOM   2304 C CB  . SER   B 1 30  ? -17.947 34.741  39.668 1.00 79.02  ? 104 SER   B CB  1 
ATOM   2305 O OG  . SER   B 1 30  ? -17.306 33.701  38.948 1.00 72.67  ? 104 SER   B OG  1 
ATOM   2306 N N   . PHE   B 1 31  ? -20.709 35.149  38.312 1.00 81.84  ? 105 PHE   B N   1 
ATOM   2307 C CA  . PHE   B 1 31  ? -21.438 35.045  37.050 1.00 77.21  ? 105 PHE   B CA  1 
ATOM   2308 C C   . PHE   B 1 31  ? -20.627 34.300  35.999 1.00 77.33  ? 105 PHE   B C   1 
ATOM   2309 O O   . PHE   B 1 31  ? -21.194 33.583  35.165 1.00 82.08  ? 105 PHE   B O   1 
ATOM   2310 C CB  . PHE   B 1 31  ? -21.802 36.444  36.549 1.00 73.59  ? 105 PHE   B CB  1 
ATOM   2311 C CG  . PHE   B 1 31  ? -22.382 36.467  35.162 1.00 72.19  ? 105 PHE   B CG  1 
ATOM   2312 C CD1 . PHE   B 1 31  ? -23.721 36.203  34.953 1.00 79.13  ? 105 PHE   B CD1 1 
ATOM   2313 C CD2 . PHE   B 1 31  ? -21.591 36.771  34.071 1.00 67.03  ? 105 PHE   B CD2 1 
ATOM   2314 C CE1 . PHE   B 1 31  ? -24.254 36.232  33.679 1.00 82.39  ? 105 PHE   B CE1 1 
ATOM   2315 C CE2 . PHE   B 1 31  ? -22.120 36.799  32.800 1.00 67.12  ? 105 PHE   B CE2 1 
ATOM   2316 C CZ  . PHE   B 1 31  ? -23.450 36.529  32.604 1.00 77.81  ? 105 PHE   B CZ  1 
ATOM   2317 N N   . PHE   B 1 32  ? -19.303 34.464  36.021 1.00 73.18  ? 106 PHE   B N   1 
ATOM   2318 C CA  . PHE   B 1 32  ? -18.433 33.727  35.113 1.00 72.98  ? 106 PHE   B CA  1 
ATOM   2319 C C   . PHE   B 1 32  ? -18.534 32.226  35.356 1.00 78.51  ? 106 PHE   B C   1 
ATOM   2320 O O   . PHE   B 1 32  ? -18.661 31.439  34.411 1.00 79.08  ? 106 PHE   B O   1 
ATOM   2321 C CB  . PHE   B 1 32  ? -16.994 34.217  35.284 1.00 71.01  ? 106 PHE   B CB  1 
ATOM   2322 C CG  . PHE   B 1 32  ? -15.997 33.512  34.417 1.00 63.47  ? 106 PHE   B CG  1 
ATOM   2323 C CD1 . PHE   B 1 32  ? -16.145 33.493  33.041 1.00 62.13  ? 106 PHE   B CD1 1 
ATOM   2324 C CD2 . PHE   B 1 32  ? -14.895 32.892  34.975 1.00 68.61  ? 106 PHE   B CD2 1 
ATOM   2325 C CE1 . PHE   B 1 32  ? -15.221 32.852  32.238 1.00 62.97  ? 106 PHE   B CE1 1 
ATOM   2326 C CE2 . PHE   B 1 32  ? -13.969 32.248  34.179 1.00 69.13  ? 106 PHE   B CE2 1 
ATOM   2327 C CZ  . PHE   B 1 32  ? -14.132 32.226  32.809 1.00 64.58  ? 106 PHE   B CZ  1 
ATOM   2328 N N   . GLN   B 1 33  ? -18.496 31.810  36.626 1.00 80.18  ? 107 GLN   B N   1 
ATOM   2329 C CA  . GLN   B 1 33  ? -18.524 30.390  36.952 1.00 80.99  ? 107 GLN   B CA  1 
ATOM   2330 C C   . GLN   B 1 33  ? -19.884 29.756  36.691 1.00 80.96  ? 107 GLN   B C   1 
ATOM   2331 O O   . GLN   B 1 33  ? -19.962 28.539  36.493 1.00 83.67  ? 107 GLN   B O   1 
ATOM   2332 C CB  . GLN   B 1 33  ? -18.124 30.179  38.415 1.00 87.52  ? 107 GLN   B CB  1 
ATOM   2333 C CG  . GLN   B 1 33  ? -17.858 28.721  38.791 1.00 99.41  ? 107 GLN   B CG  1 
ATOM   2334 C CD  . GLN   B 1 33  ? -16.666 28.129  38.045 1.00 103.97 ? 107 GLN   B CD  1 
ATOM   2335 O OE1 . GLN   B 1 33  ? -15.793 28.858  37.563 1.00 101.39 ? 107 GLN   B OE1 1 
ATOM   2336 N NE2 . GLN   B 1 33  ? -16.627 26.803  37.948 1.00 92.03  ? 107 GLN   B NE2 1 
ATOM   2337 N N   . GLN   B 1 34  ? -20.952 30.547  36.672 1.00 82.62  ? 108 GLN   B N   1 
ATOM   2338 C CA  . GLN   B 1 34  ? -22.292 30.000  36.520 1.00 81.92  ? 108 GLN   B CA  1 
ATOM   2339 C C   . GLN   B 1 34  ? -22.782 29.978  35.081 1.00 80.27  ? 108 GLN   B C   1 
ATOM   2340 O O   . GLN   B 1 34  ? -23.674 29.185  34.762 1.00 89.08  ? 108 GLN   B O   1 
ATOM   2341 C CB  . GLN   B 1 34  ? -23.285 30.799  37.367 1.00 83.61  ? 108 GLN   B CB  1 
ATOM   2342 C CG  . GLN   B 1 34  ? -22.973 30.773  38.847 1.00 86.32  ? 108 GLN   B CG  1 
ATOM   2343 C CD  . GLN   B 1 34  ? -24.022 31.479  39.676 1.00 94.95  ? 108 GLN   B CD  1 
ATOM   2344 O OE1 . GLN   B 1 34  ? -25.195 31.536  39.301 1.00 96.11  ? 108 GLN   B OE1 1 
ATOM   2345 N NE2 . GLN   B 1 34  ? -23.604 32.027  40.812 1.00 102.41 ? 108 GLN   B NE2 1 
ATOM   2346 N N   . SER   B 1 35  ? -22.228 30.816  34.205 1.00 78.81  ? 109 SER   B N   1 
ATOM   2347 C CA  . SER   B 1 35  ? -22.792 31.019  32.878 1.00 75.08  ? 109 SER   B CA  1 
ATOM   2348 C C   . SER   B 1 35  ? -21.859 30.595  31.754 1.00 73.09  ? 109 SER   B C   1 
ATOM   2349 O O   . SER   B 1 35  ? -22.103 30.953  30.595 1.00 74.18  ? 109 SER   B O   1 
ATOM   2350 C CB  . SER   B 1 35  ? -23.189 32.484  32.706 1.00 73.58  ? 109 SER   B CB  1 
ATOM   2351 O OG  . SER   B 1 35  ? -24.138 32.836  33.697 1.00 85.13  ? 109 SER   B OG  1 
ATOM   2352 N N   . PHE   B 1 36  ? -20.808 29.838  32.058 1.00 73.37  ? 110 PHE   B N   1 
ATOM   2353 C CA  . PHE   B 1 36  ? -19.872 29.389  31.038 1.00 75.79  ? 110 PHE   B CA  1 
ATOM   2354 C C   . PHE   B 1 36  ? -19.316 28.022  31.404 1.00 81.59  ? 110 PHE   B C   1 
ATOM   2355 O O   . PHE   B 1 36  ? -19.018 27.752  32.572 1.00 80.57  ? 110 PHE   B O   1 
ATOM   2356 C CB  . PHE   B 1 36  ? -18.720 30.383  30.860 1.00 67.63  ? 110 PHE   B CB  1 
ATOM   2357 C CG  . PHE   B 1 36  ? -19.142 31.693  30.282 1.00 64.24  ? 110 PHE   B CG  1 
ATOM   2358 C CD1 . PHE   B 1 36  ? -19.341 31.827  28.918 1.00 64.11  ? 110 PHE   B CD1 1 
ATOM   2359 C CD2 . PHE   B 1 36  ? -19.350 32.792  31.101 1.00 67.68  ? 110 PHE   B CD2 1 
ATOM   2360 C CE1 . PHE   B 1 36  ? -19.738 33.039  28.376 1.00 62.84  ? 110 PHE   B CE1 1 
ATOM   2361 C CE2 . PHE   B 1 36  ? -19.747 34.009  30.569 1.00 64.25  ? 110 PHE   B CE2 1 
ATOM   2362 C CZ  . PHE   B 1 36  ? -19.942 34.132  29.203 1.00 60.80  ? 110 PHE   B CZ  1 
ATOM   2363 N N   . GLN   B 1 37  ? -19.196 27.159  30.398 1.00 79.39  ? 111 GLN   B N   1 
ATOM   2364 C CA  . GLN   B 1 37  ? -18.386 25.953  30.515 1.00 79.97  ? 111 GLN   B CA  1 
ATOM   2365 C C   . GLN   B 1 37  ? -16.928 26.328  30.282 1.00 78.31  ? 111 GLN   B C   1 
ATOM   2366 O O   . GLN   B 1 37  ? -16.591 26.899  29.240 1.00 76.34  ? 111 GLN   B O   1 
ATOM   2367 C CB  . GLN   B 1 37  ? -18.838 24.899  29.508 1.00 81.57  ? 111 GLN   B CB  1 
ATOM   2368 C CG  . GLN   B 1 37  ? -19.669 23.781  30.105 1.00 98.29  ? 111 GLN   B CG  1 
ATOM   2369 C CD  . GLN   B 1 37  ? -20.524 23.077  29.069 1.00 104.70 ? 111 GLN   B CD  1 
ATOM   2370 O OE1 . GLN   B 1 37  ? -20.702 23.572  27.954 1.00 101.41 ? 111 GLN   B OE1 1 
ATOM   2371 N NE2 . GLN   B 1 37  ? -21.061 21.917  29.432 1.00 107.48 ? 111 GLN   B NE2 1 
ATOM   2372 N N   . ARG   B 1 38  ? -16.070 26.032  31.252 1.00 75.08  ? 112 ARG   B N   1 
ATOM   2373 C CA  . ARG   B 1 38  ? -14.643 26.306  31.131 1.00 75.59  ? 112 ARG   B CA  1 
ATOM   2374 C C   . ARG   B 1 38  ? -13.991 25.121  30.427 1.00 75.32  ? 112 ARG   B C   1 
ATOM   2375 O O   . ARG   B 1 38  ? -13.921 24.021  30.982 1.00 80.07  ? 112 ARG   B O   1 
ATOM   2376 C CB  . ARG   B 1 38  ? -14.026 26.555  32.506 1.00 81.03  ? 112 ARG   B CB  1 
ATOM   2377 C CG  . ARG   B 1 38  ? -12.686 27.274  32.471 1.00 81.12  ? 112 ARG   B CG  1 
ATOM   2378 C CD  . ARG   B 1 38  ? -12.197 27.644  33.873 1.00 79.00  ? 112 ARG   B CD  1 
ATOM   2379 N NE  . ARG   B 1 38  ? -13.080 28.590  34.552 1.00 80.20  ? 112 ARG   B NE  1 
ATOM   2380 C CZ  . ARG   B 1 38  ? -12.851 29.098  35.758 1.00 85.11  ? 112 ARG   B CZ  1 
ATOM   2381 N NH1 . ARG   B 1 38  ? -11.754 28.798  36.440 1.00 83.12  ? 112 ARG   B NH1 1 
ATOM   2382 N NH2 . ARG   B 1 38  ? -13.748 29.923  36.298 1.00 79.52  ? 112 ARG   B NH2 1 
ATOM   2383 N N   . LEU   B 1 39  ? -13.526 25.339  29.196 1.00 78.72  ? 113 LEU   B N   1 
ATOM   2384 C CA  . LEU   B 1 39  ? -12.953 24.255  28.402 1.00 77.86  ? 113 LEU   B CA  1 
ATOM   2385 C C   . LEU   B 1 39  ? -11.447 24.133  28.603 1.00 80.06  ? 113 LEU   B C   1 
ATOM   2386 O O   . LEU   B 1 39  ? -10.947 23.045  28.903 1.00 80.17  ? 113 LEU   B O   1 
ATOM   2387 C CB  . LEU   B 1 39  ? -13.276 24.462  26.920 1.00 77.15  ? 113 LEU   B CB  1 
ATOM   2388 C CG  . LEU   B 1 39  ? -14.768 24.520  26.585 1.00 76.45  ? 113 LEU   B CG  1 
ATOM   2389 C CD1 . LEU   B 1 39  ? -14.985 24.881  25.123 1.00 70.56  ? 113 LEU   B CD1 1 
ATOM   2390 C CD2 . LEU   B 1 39  ? -15.429 23.199  26.923 1.00 76.55  ? 113 LEU   B CD2 1 
ATOM   2391 N N   . SER   B 1 40  ? -10.715 25.233  28.443 1.00 80.59  ? 114 SER   B N   1 
ATOM   2392 C CA  . SER   B 1 40  ? -9.273  25.209  28.638 1.00 78.77  ? 114 SER   B CA  1 
ATOM   2393 C C   . SER   B 1 40  ? -8.780  26.634  28.816 1.00 75.53  ? 114 SER   B C   1 
ATOM   2394 O O   . SER   B 1 40  ? -9.416  27.593  28.370 1.00 72.86  ? 114 SER   B O   1 
ATOM   2395 C CB  . SER   B 1 40  ? -8.550  24.538  27.464 1.00 82.93  ? 114 SER   B CB  1 
ATOM   2396 O OG  . SER   B 1 40  ? -8.459  25.418  26.356 1.00 83.05  ? 114 SER   B OG  1 
ATOM   2397 N N   . ARG   B 1 41  ? -7.634  26.757  29.478 1.00 74.62  ? 115 ARG   B N   1 
ATOM   2398 C CA  . ARG   B 1 41  ? -6.983  28.044  29.659 1.00 69.00  ? 115 ARG   B CA  1 
ATOM   2399 C C   . ARG   B 1 41  ? -6.116  28.325  28.441 1.00 69.79  ? 115 ARG   B C   1 
ATOM   2400 O O   . ARG   B 1 41  ? -5.245  27.520  28.096 1.00 73.94  ? 115 ARG   B O   1 
ATOM   2401 C CB  . ARG   B 1 41  ? -6.139  28.062  30.932 1.00 71.72  ? 115 ARG   B CB  1 
ATOM   2402 C CG  . ARG   B 1 41  ? -5.541  29.425  31.232 1.00 72.20  ? 115 ARG   B CG  1 
ATOM   2403 C CD  . ARG   B 1 41  ? -4.390  29.333  32.221 1.00 83.74  ? 115 ARG   B CD  1 
ATOM   2404 N NE  . ARG   B 1 41  ? -4.853  29.112  33.585 1.00 86.60  ? 115 ARG   B NE  1 
ATOM   2405 C CZ  . ARG   B 1 41  ? -4.053  28.896  34.619 1.00 89.50  ? 115 ARG   B CZ  1 
ATOM   2406 N NH1 . ARG   B 1 41  ? -2.737  28.866  34.481 1.00 84.86  ? 115 ARG   B NH1 1 
ATOM   2407 N NH2 . ARG   B 1 41  ? -4.587  28.700  35.821 1.00 96.26  ? 115 ARG   B NH2 1 
ATOM   2408 N N   . LEU   B 1 42  ? -6.358  29.462  27.788 1.00 68.86  ? 116 LEU   B N   1 
ATOM   2409 C CA  . LEU   B 1 42  ? -5.556  29.835  26.631 1.00 64.49  ? 116 LEU   B CA  1 
ATOM   2410 C C   . LEU   B 1 42  ? -4.218  30.428  27.037 1.00 63.71  ? 116 LEU   B C   1 
ATOM   2411 O O   . LEU   B 1 42  ? -3.229  30.259  26.318 1.00 64.84  ? 116 LEU   B O   1 
ATOM   2412 C CB  . LEU   B 1 42  ? -6.325  30.819  25.753 1.00 60.07  ? 116 LEU   B CB  1 
ATOM   2413 C CG  . LEU   B 1 42  ? -7.575  30.216  25.116 1.00 63.14  ? 116 LEU   B CG  1 
ATOM   2414 C CD1 . LEU   B 1 42  ? -8.357  31.280  24.366 1.00 65.67  ? 116 LEU   B CD1 1 
ATOM   2415 C CD2 . LEU   B 1 42  ? -7.191  29.070  24.196 1.00 61.01  ? 116 LEU   B CD2 1 
ATOM   2416 N N   . GLY   B 1 43  ? -4.167  31.113  28.170 1.00 63.51  ? 117 GLY   B N   1 
ATOM   2417 C CA  . GLY   B 1 43  ? -2.920  31.674  28.648 1.00 64.76  ? 117 GLY   B CA  1 
ATOM   2418 C C   . GLY   B 1 43  ? -3.150  32.507  29.885 1.00 67.84  ? 117 GLY   B C   1 
ATOM   2419 O O   . GLY   B 1 43  ? -4.283  32.824  30.254 1.00 67.45  ? 117 GLY   B O   1 
ATOM   2420 N N   . HIS   B 1 44  ? -2.039  32.868  30.524 1.00 73.70  ? 118 HIS   B N   1 
ATOM   2421 C CA  . HIS   B 1 44  ? -2.076  33.621  31.768 1.00 74.87  ? 118 HIS   B CA  1 
ATOM   2422 C C   . HIS   B 1 44  ? -0.819  34.462  31.894 1.00 77.01  ? 118 HIS   B C   1 
ATOM   2423 O O   . HIS   B 1 44  ? 0.264   34.039  31.481 1.00 80.35  ? 118 HIS   B O   1 
ATOM   2424 C CB  . HIS   B 1 44  ? -2.197  32.691  32.982 1.00 78.62  ? 118 HIS   B CB  1 
ATOM   2425 C CG  . HIS   B 1 44  ? -1.070  31.716  33.114 1.00 79.40  ? 118 HIS   B CG  1 
ATOM   2426 N ND1 . HIS   B 1 44  ? -1.126  30.439  32.596 1.00 85.60  ? 118 HIS   B ND1 1 
ATOM   2427 C CD2 . HIS   B 1 44  ? 0.140   31.824  33.714 1.00 79.54  ? 118 HIS   B CD2 1 
ATOM   2428 C CE1 . HIS   B 1 44  ? 0.001   29.803  32.869 1.00 81.01  ? 118 HIS   B CE1 1 
ATOM   2429 N NE2 . HIS   B 1 44  ? 0.786   30.622  33.547 1.00 82.03  ? 118 HIS   B NE2 1 
ATOM   2430 N N   . GLY   B 1 45  ? -0.968  35.634  32.478 1.00 78.24  ? 119 GLY   B N   1 
ATOM   2431 C CA  . GLY   B 1 45  ? 0.155   36.509  32.749 1.00 79.78  ? 119 GLY   B CA  1 
ATOM   2432 C C   . GLY   B 1 45  ? -0.201  37.527  33.808 1.00 85.49  ? 119 GLY   B C   1 
ATOM   2433 O O   . GLY   B 1 45  ? -1.103  37.315  34.622 1.00 87.35  ? 119 GLY   B O   1 
ATOM   2434 N N   . SER   B 1 46  ? 0.516   38.652  33.792 1.00 88.01  ? 120 SER   B N   1 
ATOM   2435 C CA  . SER   B 1 46  ? 0.258   39.719  34.757 1.00 89.05  ? 120 SER   B CA  1 
ATOM   2436 C C   . SER   B 1 46  ? -1.117  40.348  34.558 1.00 87.04  ? 120 SER   B C   1 
ATOM   2437 O O   . SER   B 1 46  ? -1.765  40.745  35.536 1.00 84.12  ? 120 SER   B O   1 
ATOM   2438 C CB  . SER   B 1 46  ? 1.351   40.784  34.651 1.00 90.01  ? 120 SER   B CB  1 
ATOM   2439 O OG  . SER   B 1 46  ? 1.527   41.180  33.300 1.00 86.43  ? 120 SER   B OG  1 
ATOM   2440 N N   . TYR   B 1 47  ? -1.564  40.463  33.302 1.00 85.96  ? 121 TYR   B N   1 
ATOM   2441 C CA  . TYR   B 1 47  ? -2.909  40.959  33.015 1.00 82.55  ? 121 TYR   B CA  1 
ATOM   2442 C C   . TYR   B 1 47  ? -3.971  40.125  33.717 1.00 80.93  ? 121 TYR   B C   1 
ATOM   2443 O O   . TYR   B 1 47  ? -4.930  40.668  34.277 1.00 76.65  ? 121 TYR   B O   1 
ATOM   2444 C CB  . TYR   B 1 47  ? -3.157  40.955  31.504 1.00 79.03  ? 121 TYR   B CB  1 
ATOM   2445 C CG  . TYR   B 1 47  ? -2.917  39.603  30.856 1.00 83.99  ? 121 TYR   B CG  1 
ATOM   2446 C CD1 . TYR   B 1 47  ? -1.632  39.203  30.500 1.00 87.20  ? 121 TYR   B CD1 1 
ATOM   2447 C CD2 . TYR   B 1 47  ? -3.969  38.721  30.610 1.00 78.92  ? 121 TYR   B CD2 1 
ATOM   2448 C CE1 . TYR   B 1 47  ? -1.398  37.972  29.919 1.00 85.85  ? 121 TYR   B CE1 1 
ATOM   2449 C CE2 . TYR   B 1 47  ? -3.741  37.480  30.028 1.00 71.34  ? 121 TYR   B CE2 1 
ATOM   2450 C CZ  . TYR   B 1 47  ? -2.453  37.115  29.683 1.00 78.87  ? 121 TYR   B CZ  1 
ATOM   2451 O OH  . TYR   B 1 47  ? -2.198  35.892  29.104 1.00 83.58  ? 121 TYR   B OH  1 
ATOM   2452 N N   . GLY   B 1 48  ? -3.815  38.803  33.696 1.00 85.82  ? 122 GLY   B N   1 
ATOM   2453 C CA  . GLY   B 1 48  ? -4.801  37.901  34.253 1.00 82.65  ? 122 GLY   B CA  1 
ATOM   2454 C C   . GLY   B 1 48  ? -4.784  36.536  33.598 1.00 81.83  ? 122 GLY   B C   1 
ATOM   2455 O O   . GLY   B 1 48  ? -3.720  35.939  33.421 1.00 85.69  ? 122 GLY   B O   1 
ATOM   2456 N N   . GLU   B 1 49  ? -5.959  36.034  33.230 1.00 69.47  ? 123 GLU   B N   1 
ATOM   2457 C CA  . GLU   B 1 49  ? -6.104  34.726  32.613 1.00 64.63  ? 123 GLU   B CA  1 
ATOM   2458 C C   . GLU   B 1 49  ? -7.017  34.838  31.402 1.00 59.88  ? 123 GLU   B C   1 
ATOM   2459 O O   . GLU   B 1 49  ? -7.967  35.624  31.399 1.00 58.15  ? 123 GLU   B O   1 
ATOM   2460 C CB  . GLU   B 1 49  ? -6.689  33.707  33.595 1.00 68.99  ? 123 GLU   B CB  1 
ATOM   2461 C CG  . GLU   B 1 49  ? -5.793  33.335  34.768 1.00 77.22  ? 123 GLU   B CG  1 
ATOM   2462 C CD  . GLU   B 1 49  ? -6.390  32.210  35.615 1.00 81.54  ? 123 GLU   B CD  1 
ATOM   2463 O OE1 . GLU   B 1 49  ? -7.529  32.375  36.110 1.00 80.66  ? 123 GLU   B OE1 1 
ATOM   2464 O OE2 . GLU   B 1 49  ? -5.730  31.156  35.771 1.00 74.43  ? 123 GLU   B OE2 1 
ATOM   2465 N N   . VAL   B 1 50  ? -6.732  34.040  30.375 1.00 60.93  ? 124 VAL   B N   1 
ATOM   2466 C CA  . VAL   B 1 50  ? -7.572  33.945  29.185 1.00 55.74  ? 124 VAL   B CA  1 
ATOM   2467 C C   . VAL   B 1 50  ? -8.055  32.510  29.072 1.00 63.40  ? 124 VAL   B C   1 
ATOM   2468 O O   . VAL   B 1 50  ? -7.239  31.585  28.978 1.00 65.84  ? 124 VAL   B O   1 
ATOM   2469 C CB  . VAL   B 1 50  ? -6.825  34.354  27.908 1.00 57.40  ? 124 VAL   B CB  1 
ATOM   2470 C CG1 . VAL   B 1 50  ? -7.768  34.299  26.713 1.00 56.63  ? 124 VAL   B CG1 1 
ATOM   2471 C CG2 . VAL   B 1 50  ? -6.218  35.728  28.062 1.00 54.64  ? 124 VAL   B CG2 1 
ATOM   2472 N N   . PHE   B 1 51  ? -9.373  32.325  29.060 1.00 60.14  ? 125 PHE   B N   1 
ATOM   2473 C CA  . PHE   B 1 51  ? -9.981  31.005  29.045 1.00 59.63  ? 125 PHE   B CA  1 
ATOM   2474 C C   . PHE   B 1 51  ? -10.755 30.780  27.758 1.00 62.61  ? 125 PHE   B C   1 
ATOM   2475 O O   . PHE   B 1 51  ? -11.405 31.696  27.244 1.00 60.40  ? 125 PHE   B O   1 
ATOM   2476 C CB  . PHE   B 1 51  ? -10.936 30.819  30.217 1.00 65.53  ? 125 PHE   B CB  1 
ATOM   2477 C CG  . PHE   B 1 51  ? -10.260 30.731  31.543 1.00 63.27  ? 125 PHE   B CG  1 
ATOM   2478 C CD1 . PHE   B 1 51  ? -9.702  29.545  31.966 1.00 66.82  ? 125 PHE   B CD1 1 
ATOM   2479 C CD2 . PHE   B 1 51  ? -10.205 31.829  32.379 1.00 67.26  ? 125 PHE   B CD2 1 
ATOM   2480 C CE1 . PHE   B 1 51  ? -9.086  29.458  33.195 1.00 71.96  ? 125 PHE   B CE1 1 
ATOM   2481 C CE2 . PHE   B 1 51  ? -9.592  31.749  33.608 1.00 69.45  ? 125 PHE   B CE2 1 
ATOM   2482 C CZ  . PHE   B 1 51  ? -9.031  30.561  34.017 1.00 72.11  ? 125 PHE   B CZ  1 
ATOM   2483 N N   . LYS   B 1 52  ? -10.696 29.548  27.257 1.00 69.27  ? 126 LYS   B N   1 
ATOM   2484 C CA  . LYS   B 1 52  ? -11.578 29.089  26.191 1.00 70.72  ? 126 LYS   B CA  1 
ATOM   2485 C C   . LYS   B 1 52  ? -12.843 28.526  26.831 1.00 68.24  ? 126 LYS   B C   1 
ATOM   2486 O O   . LYS   B 1 52  ? -12.772 27.583  27.627 1.00 70.49  ? 126 LYS   B O   1 
ATOM   2487 C CB  . LYS   B 1 52  ? -10.880 28.036  25.327 1.00 71.76  ? 126 LYS   B CB  1 
ATOM   2488 C CG  . LYS   B 1 52  ? -11.748 27.436  24.215 1.00 73.96  ? 126 LYS   B CG  1 
ATOM   2489 C CD  . LYS   B 1 52  ? -10.984 26.386  23.393 1.00 75.09  ? 126 LYS   B CD  1 
ATOM   2490 C CE  . LYS   B 1 52  ? -11.902 25.674  22.397 1.00 69.85  ? 126 LYS   B CE  1 
ATOM   2491 N NZ  . LYS   B 1 52  ? -11.218 24.604  21.615 1.00 68.76  ? 126 LYS   B NZ  1 
ATOM   2492 N N   . VAL   B 1 53  ? -13.997 29.109  26.495 1.00 71.18  ? 127 VAL   B N   1 
ATOM   2493 C CA  . VAL   B 1 53  ? -15.259 28.768  27.137 1.00 64.08  ? 127 VAL   B CA  1 
ATOM   2494 C C   . VAL   B 1 53  ? -16.322 28.498  26.081 1.00 67.71  ? 127 VAL   B C   1 
ATOM   2495 O O   . VAL   B 1 53  ? -16.226 28.942  24.935 1.00 71.23  ? 127 VAL   B O   1 
ATOM   2496 C CB  . VAL   B 1 53  ? -15.752 29.881  28.088 1.00 64.15  ? 127 VAL   B CB  1 
ATOM   2497 C CG1 . VAL   B 1 53  ? -14.717 30.179  29.159 1.00 68.21  ? 127 VAL   B CG1 1 
ATOM   2498 C CG2 . VAL   B 1 53  ? -16.092 31.136  27.297 1.00 60.10  ? 127 VAL   B CG2 1 
ATOM   2499 N N   . ARG   B 1 54  ? -17.355 27.766  26.496 1.00 68.90  ? 128 ARG   B N   1 
ATOM   2500 C CA  . ARG   B 1 54  ? -18.588 27.612  25.734 1.00 73.05  ? 128 ARG   B CA  1 
ATOM   2501 C C   . ARG   B 1 54  ? -19.728 28.263  26.507 1.00 69.87  ? 128 ARG   B C   1 
ATOM   2502 O O   . ARG   B 1 54  ? -19.891 28.018  27.707 1.00 70.02  ? 128 ARG   B O   1 
ATOM   2503 C CB  . ARG   B 1 54  ? -18.903 26.136  25.461 1.00 76.56  ? 128 ARG   B CB  1 
ATOM   2504 C CG  . ARG   B 1 54  ? -20.290 25.905  24.859 1.00 80.74  ? 128 ARG   B CG  1 
ATOM   2505 C CD  . ARG   B 1 54  ? -20.454 24.516  24.239 1.00 82.18  ? 128 ARG   B CD  1 
ATOM   2506 N NE  . ARG   B 1 54  ? -19.962 24.469  22.866 1.00 81.24  ? 128 ARG   B NE  1 
ATOM   2507 C CZ  . ARG   B 1 54  ? -19.130 23.550  22.394 1.00 87.53  ? 128 ARG   B CZ  1 
ATOM   2508 N NH1 . ARG   B 1 54  ? -18.699 22.553  23.153 1.00 83.94  ? 128 ARG   B NH1 1 
ATOM   2509 N NH2 . ARG   B 1 54  ? -18.728 23.627  21.127 1.00 88.84  ? 128 ARG   B NH2 1 
ATOM   2510 N N   . SER   B 1 55  ? -20.502 29.098  25.817 1.00 73.73  ? 129 SER   B N   1 
ATOM   2511 C CA  . SER   B 1 55  ? -21.584 29.838  26.455 1.00 73.01  ? 129 SER   B CA  1 
ATOM   2512 C C   . SER   B 1 55  ? -22.672 28.884  26.921 1.00 83.55  ? 129 SER   B C   1 
ATOM   2513 O O   . SER   B 1 55  ? -23.180 28.074  26.138 1.00 89.64  ? 129 SER   B O   1 
ATOM   2514 C CB  . SER   B 1 55  ? -22.163 30.861  25.478 1.00 76.85  ? 129 SER   B CB  1 
ATOM   2515 O OG  . SER   B 1 55  ? -23.201 31.617  26.074 1.00 82.02  ? 129 SER   B OG  1 
ATOM   2516 N N   . LYS   B 1 56  ? -23.033 28.969  28.204 1.00 88.32  ? 130 LYS   B N   1 
ATOM   2517 C CA  . LYS   B 1 56  ? -24.122 28.124  28.686 1.00 85.58  ? 130 LYS   B CA  1 
ATOM   2518 C C   . LYS   B 1 56  ? -25.470 28.590  28.153 1.00 86.20  ? 130 LYS   B C   1 
ATOM   2519 O O   . LYS   B 1 56  ? -26.351 27.766  27.913 1.00 101.54 ? 130 LYS   B O   1 
ATOM   2520 C CB  . LYS   B 1 56  ? -24.142 28.077  30.214 1.00 80.26  ? 130 LYS   B CB  1 
ATOM   2521 C CG  . LYS   B 1 56  ? -23.254 26.997  30.816 1.00 81.58  ? 130 LYS   B CG  1 
ATOM   2522 C CD  . LYS   B 1 56  ? -23.190 27.133  32.326 1.00 83.25  ? 130 LYS   B CD  1 
ATOM   2523 C CE  . LYS   B 1 56  ? -22.261 26.100  32.946 1.00 85.09  ? 130 LYS   B CE  1 
ATOM   2524 N NZ  . LYS   B 1 56  ? -22.257 26.182  34.437 1.00 87.47  ? 130 LYS   B NZ  1 
ATOM   2525 N N   . GLU   B 1 57  ? -25.651 29.891  27.943 1.00 89.30  ? 131 GLU   B N   1 
ATOM   2526 C CA  . GLU   B 1 57  ? -26.943 30.368  27.462 1.00 94.00  ? 131 GLU   B CA  1 
ATOM   2527 C C   . GLU   B 1 57  ? -27.104 30.185  25.960 1.00 91.55  ? 131 GLU   B C   1 
ATOM   2528 O O   . GLU   B 1 57  ? -28.221 29.954  25.484 1.00 99.96  ? 131 GLU   B O   1 
ATOM   2529 C CB  . GLU   B 1 57  ? -27.129 31.843  27.824 1.00 99.53  ? 131 GLU   B CB  1 
ATOM   2530 C CG  . GLU   B 1 57  ? -27.086 32.123  29.314 1.00 103.84 ? 131 GLU   B CG  1 
ATOM   2531 C CD  . GLU   B 1 57  ? -28.273 31.547  30.080 1.00 111.90 ? 131 GLU   B CD  1 
ATOM   2532 O OE1 . GLU   B 1 57  ? -29.261 31.105  29.449 1.00 108.29 ? 131 GLU   B OE1 1 
ATOM   2533 O OE2 . GLU   B 1 57  ? -28.213 31.545  31.327 1.00 114.45 ? 131 GLU   B OE2 1 
ATOM   2534 N N   . ASP   B 1 58  ? -26.011 30.273  25.211 1.00 87.13  ? 132 ASP   B N   1 
ATOM   2535 C CA  . ASP   B 1 58  ? -26.033 30.320  23.755 1.00 90.20  ? 132 ASP   B CA  1 
ATOM   2536 C C   . ASP   B 1 58  ? -25.505 29.052  23.099 1.00 90.29  ? 132 ASP   B C   1 
ATOM   2537 O O   . ASP   B 1 58  ? -26.032 28.630  22.066 1.00 91.48  ? 132 ASP   B O   1 
ATOM   2538 C CB  . ASP   B 1 58  ? -25.226 31.542  23.284 1.00 95.97  ? 132 ASP   B CB  1 
ATOM   2539 C CG  . ASP   B 1 58  ? -24.915 31.523  21.801 1.00 96.11  ? 132 ASP   B CG  1 
ATOM   2540 O OD1 . ASP   B 1 58  ? -25.812 31.177  20.998 1.00 93.57  ? 132 ASP   B OD1 1 
ATOM   2541 O OD2 . ASP   B 1 58  ? -23.772 31.893  21.446 1.00 87.95  ? 132 ASP   B OD2 1 
ATOM   2542 N N   . GLY   B 1 59  ? -24.494 28.414  23.682 1.00 88.69  ? 133 GLY   B N   1 
ATOM   2543 C CA  . GLY   B 1 59  ? -23.926 27.204  23.141 1.00 82.71  ? 133 GLY   B CA  1 
ATOM   2544 C C   . GLY   B 1 59  ? -22.682 27.406  22.299 1.00 85.66  ? 133 GLY   B C   1 
ATOM   2545 O O   . GLY   B 1 59  ? -21.926 26.448  22.105 1.00 81.74  ? 133 GLY   B O   1 
ATOM   2546 N N   . ARG   B 1 60  ? -22.445 28.620  21.802 1.00 82.46  ? 134 ARG   B N   1 
ATOM   2547 C CA  . ARG   B 1 60  ? -21.303 28.891  20.937 1.00 81.52  ? 134 ARG   B CA  1 
ATOM   2548 C C   . ARG   B 1 60  ? -20.012 28.947  21.754 1.00 79.58  ? 134 ARG   B C   1 
ATOM   2549 O O   . ARG   B 1 60  ? -19.992 28.693  22.962 1.00 75.21  ? 134 ARG   B O   1 
ATOM   2550 C CB  . ARG   B 1 60  ? -21.518 30.182  20.148 1.00 84.10  ? 134 ARG   B CB  1 
ATOM   2551 C CG  . ARG   B 1 60  ? -22.610 30.115  19.087 1.00 85.95  ? 134 ARG   B CG  1 
ATOM   2552 C CD  . ARG   B 1 60  ? -22.149 30.784  17.795 1.00 93.32  ? 134 ARG   B CD  1 
ATOM   2553 N NE  . ARG   B 1 60  ? -23.264 31.109  16.913 1.00 97.38  ? 134 ARG   B NE  1 
ATOM   2554 C CZ  . ARG   B 1 60  ? -23.648 32.342  16.608 1.00 103.77 ? 134 ARG   B CZ  1 
ATOM   2555 N NH1 . ARG   B 1 60  ? -22.998 33.403  17.064 1.00 96.48  ? 134 ARG   B NH1 1 
ATOM   2556 N NH2 . ARG   B 1 60  ? -24.709 32.515  15.822 1.00 105.72 ? 134 ARG   B NH2 1 
ATOM   2557 N N   . LEU   B 1 61  ? -18.911 29.289  21.087 1.00 78.34  ? 135 LEU   B N   1 
ATOM   2558 C CA  . LEU   B 1 61  ? -17.580 29.247  21.673 1.00 73.50  ? 135 LEU   B CA  1 
ATOM   2559 C C   . LEU   B 1 61  ? -17.014 30.655  21.757 1.00 70.34  ? 135 LEU   B C   1 
ATOM   2560 O O   . LEU   B 1 61  ? -17.062 31.412  20.780 1.00 71.66  ? 135 LEU   B O   1 
ATOM   2561 C CB  . LEU   B 1 61  ? -16.649 28.343  20.856 1.00 75.74  ? 135 LEU   B CB  1 
ATOM   2562 C CG  . LEU   B 1 61  ? -16.811 26.852  21.146 1.00 72.53  ? 135 LEU   B CG  1 
ATOM   2563 C CD1 . LEU   B 1 61  ? -15.751 26.020  20.441 1.00 65.72  ? 135 LEU   B CD1 1 
ATOM   2564 C CD2 . LEU   B 1 61  ? -16.747 26.639  22.637 1.00 71.73  ? 135 LEU   B CD2 1 
ATOM   2565 N N   . TYR   B 1 62  ? -16.487 31.008  22.928 1.00 68.16  ? 136 TYR   B N   1 
ATOM   2566 C CA  . TYR   B 1 62  ? -15.927 32.331  23.145 1.00 65.12  ? 136 TYR   B CA  1 
ATOM   2567 C C   . TYR   B 1 62  ? -14.633 32.200  23.934 1.00 63.83  ? 136 TYR   B C   1 
ATOM   2568 O O   . TYR   B 1 62  ? -14.322 31.147  24.500 1.00 65.40  ? 136 TYR   B O   1 
ATOM   2569 C CB  . TYR   B 1 62  ? -16.921 33.249  23.872 1.00 62.95  ? 136 TYR   B CB  1 
ATOM   2570 C CG  . TYR   B 1 62  ? -18.267 33.357  23.189 1.00 65.86  ? 136 TYR   B CG  1 
ATOM   2571 C CD1 . TYR   B 1 62  ? -18.510 34.332  22.230 1.00 67.89  ? 136 TYR   B CD1 1 
ATOM   2572 C CD2 . TYR   B 1 62  ? -19.292 32.488  23.507 1.00 69.99  ? 136 TYR   B CD2 1 
ATOM   2573 C CE1 . TYR   B 1 62  ? -19.741 34.427  21.605 1.00 67.19  ? 136 TYR   B CE1 1 
ATOM   2574 C CE2 . TYR   B 1 62  ? -20.521 32.576  22.891 1.00 73.24  ? 136 TYR   B CE2 1 
ATOM   2575 C CZ  . TYR   B 1 62  ? -20.743 33.543  21.941 1.00 71.19  ? 136 TYR   B CZ  1 
ATOM   2576 O OH  . TYR   B 1 62  ? -21.980 33.614  21.335 1.00 79.82  ? 136 TYR   B OH  1 
ATOM   2577 N N   . ALA   B 1 63  ? -13.865 33.284  23.941 1.00 60.56  ? 137 ALA   B N   1 
ATOM   2578 C CA  . ALA   B 1 63  ? -12.685 33.431  24.779 1.00 56.73  ? 137 ALA   B CA  1 
ATOM   2579 C C   . ALA   B 1 63  ? -12.971 34.521  25.795 1.00 54.69  ? 137 ALA   B C   1 
ATOM   2580 O O   . ALA   B 1 63  ? -13.431 35.606  25.425 1.00 62.97  ? 137 ALA   B O   1 
ATOM   2581 C CB  . ALA   B 1 63  ? -11.453 33.796  23.949 1.00 51.79  ? 137 ALA   B CB  1 
ATOM   2582 N N   . VAL   B 1 64  ? -12.722 34.240  27.068 1.00 52.19  ? 138 VAL   B N   1 
ATOM   2583 C CA  . VAL   B 1 64  ? -12.968 35.209  28.128 1.00 53.16  ? 138 VAL   B CA  1 
ATOM   2584 C C   . VAL   B 1 64  ? -11.657 35.500  28.837 1.00 54.25  ? 138 VAL   B C   1 
ATOM   2585 O O   . VAL   B 1 64  ? -10.952 34.574  29.254 1.00 62.75  ? 138 VAL   B O   1 
ATOM   2586 C CB  . VAL   B 1 64  ? -14.034 34.725  29.124 1.00 56.36  ? 138 VAL   B CB  1 
ATOM   2587 C CG1 . VAL   B 1 64  ? -14.212 35.752  30.228 1.00 53.04  ? 138 VAL   B CG1 1 
ATOM   2588 C CG2 . VAL   B 1 64  ? -15.349 34.486  28.407 1.00 55.66  ? 138 VAL   B CG2 1 
ATOM   2589 N N   . LYS   B 1 65  ? -11.329 36.782  28.951 1.00 55.82  ? 139 LYS   B N   1 
ATOM   2590 C CA  . LYS   B 1 65  ? -10.150 37.251  29.662 1.00 53.56  ? 139 LYS   B CA  1 
ATOM   2591 C C   . LYS   B 1 65  ? -10.585 37.838  31.000 1.00 55.06  ? 139 LYS   B C   1 
ATOM   2592 O O   . LYS   B 1 65  ? -11.414 38.755  31.042 1.00 54.59  ? 139 LYS   B O   1 
ATOM   2593 C CB  . LYS   B 1 65  ? -9.392  38.300  28.846 1.00 51.18  ? 139 LYS   B CB  1 
ATOM   2594 C CG  . LYS   B 1 65  ? -8.078  38.722  29.481 1.00 55.09  ? 139 LYS   B CG  1 
ATOM   2595 C CD  . LYS   B 1 65  ? -7.330  39.750  28.642 1.00 54.97  ? 139 LYS   B CD  1 
ATOM   2596 C CE  . LYS   B 1 65  ? -8.074  41.068  28.607 1.00 51.25  ? 139 LYS   B CE  1 
ATOM   2597 N NZ  . LYS   B 1 65  ? -7.237  42.145  28.027 1.00 60.88  ? 139 LYS   B NZ  1 
ATOM   2598 N N   . ARG   B 1 66  ? -10.025 37.309  32.081 1.00 58.67  ? 140 ARG   B N   1 
ATOM   2599 C CA  . ARG   B 1 66  ? -10.296 37.761  33.438 1.00 55.99  ? 140 ARG   B CA  1 
ATOM   2600 C C   . ARG   B 1 66  ? -9.052  38.446  33.990 1.00 58.41  ? 140 ARG   B C   1 
ATOM   2601 O O   . ARG   B 1 66  ? -7.949  37.897  33.899 1.00 63.01  ? 140 ARG   B O   1 
ATOM   2602 C CB  . ARG   B 1 66  ? -10.692 36.568  34.314 1.00 57.50  ? 140 ARG   B CB  1 
ATOM   2603 C CG  . ARG   B 1 66  ? -10.551 36.811  35.795 1.00 63.51  ? 140 ARG   B CG  1 
ATOM   2604 C CD  . ARG   B 1 66  ? -11.150 35.678  36.592 1.00 61.32  ? 140 ARG   B CD  1 
ATOM   2605 N NE  . ARG   B 1 66  ? -10.365 34.464  36.437 1.00 66.35  ? 140 ARG   B NE  1 
ATOM   2606 C CZ  . ARG   B 1 66  ? -10.698 33.290  36.952 1.00 70.76  ? 140 ARG   B CZ  1 
ATOM   2607 N NH1 . ARG   B 1 66  ? -11.810 33.132  37.654 1.00 76.47  ? 140 ARG   B NH1 1 
ATOM   2608 N NH2 . ARG   B 1 66  ? -9.897  32.247  36.757 1.00 81.40  ? 140 ARG   B NH2 1 
ATOM   2609 N N   . SER   B 1 67  ? -9.217  39.641  34.549 1.00 59.54  ? 141 SER   B N   1 
ATOM   2610 C CA  . SER   B 1 67  ? -8.062  40.327  35.116 1.00 61.31  ? 141 SER   B CA  1 
ATOM   2611 C C   . SER   B 1 67  ? -7.623  39.629  36.399 1.00 66.51  ? 141 SER   B C   1 
ATOM   2612 O O   . SER   B 1 67  ? -8.414  38.966  37.076 1.00 70.00  ? 141 SER   B O   1 
ATOM   2613 C CB  . SER   B 1 67  ? -8.368  41.805  35.379 1.00 59.94  ? 141 SER   B CB  1 
ATOM   2614 O OG  . SER   B 1 67  ? -9.338  41.977  36.396 1.00 59.99  ? 141 SER   B OG  1 
ATOM   2615 N N   . MET   B 1 68  ? -6.337  39.768  36.721 1.00 69.59  ? 142 MET   B N   1 
ATOM   2616 C CA  . MET   B 1 68  ? -5.756  38.970  37.797 1.00 75.32  ? 142 MET   B CA  1 
ATOM   2617 C C   . MET   B 1 68  ? -6.183  39.481  39.168 1.00 70.95  ? 142 MET   B C   1 
ATOM   2618 O O   . MET   B 1 68  ? -6.765  38.738  39.966 1.00 70.83  ? 142 MET   B O   1 
ATOM   2619 C CB  . MET   B 1 68  ? -4.229  38.957  37.683 1.00 80.94  ? 142 MET   B CB  1 
ATOM   2620 C CG  . MET   B 1 68  ? -3.545  38.155  38.777 1.00 84.62  ? 142 MET   B CG  1 
ATOM   2621 S SD  . MET   B 1 68  ? -1.752  38.359  38.771 1.00 112.75 ? 142 MET   B SD  1 
ATOM   2622 C CE  . MET   B 1 68  ? -1.233  36.882  37.894 1.00 96.45  ? 142 MET   B CE  1 
ATOM   2623 N N   . SER   B 1 69  ? -5.898  40.748  39.455 1.00 75.22  ? 143 SER   B N   1 
ATOM   2624 C CA  . SER   B 1 69  ? -6.092  41.342  40.765 1.00 76.90  ? 143 SER   B CA  1 
ATOM   2625 C C   . SER   B 1 69  ? -7.271  42.309  40.754 1.00 75.94  ? 143 SER   B C   1 
ATOM   2626 O O   . SER   B 1 69  ? -7.536  42.956  39.737 1.00 73.95  ? 143 SER   B O   1 
ATOM   2627 C CB  . SER   B 1 69  ? -4.831  42.095  41.203 1.00 84.27  ? 143 SER   B CB  1 
ATOM   2628 O OG  . SER   B 1 69  ? -3.663  41.366  40.860 1.00 93.02  ? 143 SER   B OG  1 
ATOM   2629 N N   . PRO   B 1 70  ? -7.997  42.431  41.866 1.00 67.12  ? 144 PRO   B N   1 
ATOM   2630 C CA  . PRO   B 1 70  ? -9.081  43.417  41.939 1.00 61.82  ? 144 PRO   B CA  1 
ATOM   2631 C C   . PRO   B 1 70  ? -8.558  44.824  41.708 1.00 69.76  ? 144 PRO   B C   1 
ATOM   2632 O O   . PRO   B 1 70  ? -7.353  45.088  41.696 1.00 77.63  ? 144 PRO   B O   1 
ATOM   2633 C CB  . PRO   B 1 70  ? -9.631  43.246  43.358 1.00 63.98  ? 144 PRO   B CB  1 
ATOM   2634 C CG  . PRO   B 1 70  ? -9.268  41.853  43.731 1.00 66.93  ? 144 PRO   B CG  1 
ATOM   2635 C CD  . PRO   B 1 70  ? -7.944  41.583  43.069 1.00 67.93  ? 144 PRO   B CD  1 
ATOM   2636 N N   . PHE   B 1 71  ? -9.497  45.743  41.514 1.00 62.76  ? 145 PHE   B N   1 
ATOM   2637 C CA  . PHE   B 1 71  ? -9.145  47.121  41.214 1.00 64.70  ? 145 PHE   B CA  1 
ATOM   2638 C C   . PHE   B 1 71  ? -8.398  47.747  42.381 1.00 71.54  ? 145 PHE   B C   1 
ATOM   2639 O O   . PHE   B 1 71  ? -8.897  47.775  43.510 1.00 73.72  ? 145 PHE   B O   1 
ATOM   2640 C CB  . PHE   B 1 71  ? -10.405 47.914  40.896 1.00 58.14  ? 145 PHE   B CB  1 
ATOM   2641 C CG  . PHE   B 1 71  ? -11.131 47.420  39.685 1.00 59.06  ? 145 PHE   B CG  1 
ATOM   2642 C CD1 . PHE   B 1 71  ? -10.432 47.053  38.549 1.00 58.67  ? 145 PHE   B CD1 1 
ATOM   2643 C CD2 . PHE   B 1 71  ? -12.511 47.308  39.683 1.00 57.83  ? 145 PHE   B CD2 1 
ATOM   2644 C CE1 . PHE   B 1 71  ? -11.099 46.594  37.425 1.00 57.74  ? 145 PHE   B CE1 1 
ATOM   2645 C CE2 . PHE   B 1 71  ? -13.183 46.850  38.564 1.00 56.73  ? 145 PHE   B CE2 1 
ATOM   2646 C CZ  . PHE   B 1 71  ? -12.477 46.494  37.433 1.00 54.04  ? 145 PHE   B CZ  1 
ATOM   2647 N N   . ARG   B 1 72  ? -7.194  48.244  42.107 1.00 79.90  ? 146 ARG   B N   1 
ATOM   2648 C CA  . ARG   B 1 72  ? -6.378  48.847  43.149 1.00 85.68  ? 146 ARG   B CA  1 
ATOM   2649 C C   . ARG   B 1 72  ? -6.872  50.231  43.539 1.00 86.29  ? 146 ARG   B C   1 
ATOM   2650 O O   . ARG   B 1 72  ? -6.631  50.669  44.668 1.00 90.40  ? 146 ARG   B O   1 
ATOM   2651 C CB  . ARG   B 1 72  ? -4.920  48.903  42.681 1.00 89.89  ? 146 ARG   B CB  1 
ATOM   2652 C CG  . ARG   B 1 72  ? -4.382  47.536  42.248 1.00 89.77  ? 146 ARG   B CG  1 
ATOM   2653 C CD  . ARG   B 1 72  ? -2.969  47.607  41.678 1.00 96.23  ? 146 ARG   B CD  1 
ATOM   2654 N NE  . ARG   B 1 72  ? -2.434  46.276  41.406 1.00 108.99 ? 146 ARG   B NE  1 
ATOM   2655 C CZ  . ARG   B 1 72  ? -2.604  45.612  40.269 1.00 103.57 ? 146 ARG   B CZ  1 
ATOM   2656 N NH1 . ARG   B 1 72  ? -3.279  46.134  39.256 1.00 97.81  ? 146 ARG   B NH1 1 
ATOM   2657 N NH2 . ARG   B 1 72  ? -2.084  44.393  40.146 1.00 101.30 ? 146 ARG   B NH2 1 
ATOM   2658 N N   . GLY   B 1 73  ? -7.579  50.907  42.644 1.00 68.68  ? 147 GLY   B N   1 
ATOM   2659 C CA  . GLY   B 1 73  ? -8.019  52.264  42.846 1.00 59.29  ? 147 GLY   B CA  1 
ATOM   2660 C C   . GLY   B 1 73  ? -8.766  52.716  41.611 1.00 61.71  ? 147 GLY   B C   1 
ATOM   2661 O O   . GLY   B 1 73  ? -8.843  51.985  40.619 1.00 62.44  ? 147 GLY   B O   1 
ATOM   2662 N N   . PRO   B 1 74  ? -9.341  53.920  41.636 1.00 56.78  ? 148 PRO   B N   1 
ATOM   2663 C CA  . PRO   B 1 74  ? -10.116 54.366  40.466 1.00 53.16  ? 148 PRO   B CA  1 
ATOM   2664 C C   . PRO   B 1 74  ? -9.278  54.516  39.207 1.00 56.45  ? 148 PRO   B C   1 
ATOM   2665 O O   . PRO   B 1 74  ? -9.773  54.223  38.110 1.00 53.30  ? 148 PRO   B O   1 
ATOM   2666 C CB  . PRO   B 1 74  ? -10.729 55.698  40.923 1.00 51.94  ? 148 PRO   B CB  1 
ATOM   2667 C CG  . PRO   B 1 74  ? -9.989  56.089  42.154 1.00 57.07  ? 148 PRO   B CG  1 
ATOM   2668 C CD  . PRO   B 1 74  ? -9.457  54.842  42.775 1.00 57.28  ? 148 PRO   B CD  1 
ATOM   2669 N N   . LYS   B 1 75  ? -8.015  54.939  39.325 1.00 63.09  ? 149 LYS   B N   1 
ATOM   2670 C CA  . LYS   B 1 75  ? -7.151  54.990  38.148 1.00 55.39  ? 149 LYS   B CA  1 
ATOM   2671 C C   . LYS   B 1 75  ? -6.914  53.595  37.586 1.00 56.47  ? 149 LYS   B C   1 
ATOM   2672 O O   . LYS   B 1 75  ? -6.947  53.395  36.365 1.00 56.78  ? 149 LYS   B O   1 
ATOM   2673 C CB  . LYS   B 1 75  ? -5.815  55.654  38.487 1.00 61.50  ? 149 LYS   B CB  1 
ATOM   2674 C CG  . LYS   B 1 75  ? -5.882  57.127  38.879 1.00 66.66  ? 149 LYS   B CG  1 
ATOM   2675 C CD  . LYS   B 1 75  ? -4.472  57.738  38.893 1.00 77.90  ? 149 LYS   B CD  1 
ATOM   2676 C CE  . LYS   B 1 75  ? -4.442  59.116  39.549 1.00 79.71  ? 149 LYS   B CE  1 
ATOM   2677 N NZ  . LYS   B 1 75  ? -5.359  60.081  38.879 1.00 81.80  ? 149 LYS   B NZ  1 
ATOM   2678 N N   . ASP   B 1 76  ? -6.660  52.618  38.459 1.00 58.85  ? 150 ASP   B N   1 
ATOM   2679 C CA  . ASP   B 1 76  ? -6.506  51.242  37.996 1.00 60.85  ? 150 ASP   B CA  1 
ATOM   2680 C C   . ASP   B 1 76  ? -7.760  50.779  37.270 1.00 56.48  ? 150 ASP   B C   1 
ATOM   2681 O O   . ASP   B 1 76  ? -7.688  50.212  36.173 1.00 53.98  ? 150 ASP   B O   1 
ATOM   2682 C CB  . ASP   B 1 76  ? -6.197  50.316  39.175 1.00 60.00  ? 150 ASP   B CB  1 
ATOM   2683 C CG  . ASP   B 1 76  ? -5.828  48.915  38.728 1.00 64.50  ? 150 ASP   B CG  1 
ATOM   2684 O OD1 . ASP   B 1 76  ? -5.265  48.783  37.623 1.00 68.04  ? 150 ASP   B OD1 1 
ATOM   2685 O OD2 . ASP   B 1 76  ? -6.110  47.948  39.467 1.00 69.88  ? 150 ASP   B OD2 1 
ATOM   2686 N N   . ARG   B 1 77  ? -8.924  51.036  37.865 1.00 55.72  ? 151 ARG   B N   1 
ATOM   2687 C CA  . ARG   B 1 77  ? -10.180 50.629  37.248 1.00 53.95  ? 151 ARG   B CA  1 
ATOM   2688 C C   . ARG   B 1 77  ? -10.380 51.323  35.908 1.00 52.07  ? 151 ARG   B C   1 
ATOM   2689 O O   . ARG   B 1 77  ? -10.719 50.680  34.909 1.00 50.27  ? 151 ARG   B O   1 
ATOM   2690 C CB  . ARG   B 1 77  ? -11.334 50.929  38.195 1.00 48.36  ? 151 ARG   B CB  1 
ATOM   2691 C CG  . ARG   B 1 77  ? -12.680 50.544  37.663 1.00 51.12  ? 151 ARG   B CG  1 
ATOM   2692 C CD  . ARG   B 1 77  ? -13.746 50.843  38.689 1.00 56.52  ? 151 ARG   B CD  1 
ATOM   2693 N NE  . ARG   B 1 77  ? -15.050 50.371  38.249 1.00 60.65  ? 151 ARG   B NE  1 
ATOM   2694 C CZ  . ARG   B 1 77  ? -15.892 51.088  37.521 1.00 65.20  ? 151 ARG   B CZ  1 
ATOM   2695 N NH1 . ARG   B 1 77  ? -15.606 52.328  37.157 1.00 64.69  ? 151 ARG   B NH1 1 
ATOM   2696 N NH2 . ARG   B 1 77  ? -17.047 50.544  37.143 1.00 68.14  ? 151 ARG   B NH2 1 
ATOM   2697 N N   . ALA   B 1 78  ? -10.150 52.639  35.861 1.00 50.13  ? 152 ALA   B N   1 
ATOM   2698 C CA  . ALA   B 1 78  ? -10.327 53.372  34.612 1.00 44.77  ? 152 ALA   B CA  1 
ATOM   2699 C C   . ALA   B 1 78  ? -9.371  52.887  33.534 1.00 50.59  ? 152 ALA   B C   1 
ATOM   2700 O O   . ALA   B 1 78  ? -9.721  52.885  32.347 1.00 51.10  ? 152 ALA   B O   1 
ATOM   2701 C CB  . ALA   B 1 78  ? -10.140 54.869  34.848 1.00 52.49  ? 152 ALA   B CB  1 
ATOM   2702 N N   . ARG   B 1 79  ? -8.158  52.485  33.920 1.00 53.48  ? 153 ARG   B N   1 
ATOM   2703 C CA  . ARG   B 1 79  ? -7.202  51.984  32.938 1.00 47.54  ? 153 ARG   B CA  1 
ATOM   2704 C C   . ARG   B 1 79  ? -7.662  50.645  32.373 1.00 48.78  ? 153 ARG   B C   1 
ATOM   2705 O O   . ARG   B 1 79  ? -7.575  50.414  31.161 1.00 48.54  ? 153 ARG   B O   1 
ATOM   2706 C CB  . ARG   B 1 79  ? -5.815  51.865  33.576 1.00 54.16  ? 153 ARG   B CB  1 
ATOM   2707 C CG  . ARG   B 1 79  ? -4.662  52.395  32.726 1.00 62.19  ? 153 ARG   B CG  1 
ATOM   2708 C CD  . ARG   B 1 79  ? -3.281  52.148  33.374 1.00 71.58  ? 153 ARG   B CD  1 
ATOM   2709 N NE  . ARG   B 1 79  ? -3.074  52.884  34.621 1.00 72.25  ? 153 ARG   B NE  1 
ATOM   2710 C CZ  . ARG   B 1 79  ? -2.960  52.325  35.822 1.00 71.89  ? 153 ARG   B CZ  1 
ATOM   2711 N NH1 . ARG   B 1 79  ? -2.996  51.008  35.981 1.00 69.95  ? 153 ARG   B NH1 1 
ATOM   2712 N NH2 . ARG   B 1 79  ? -2.804  53.105  36.890 1.00 65.13  ? 153 ARG   B NH2 1 
ATOM   2713 N N   . LYS   B 1 80  ? -8.176  49.758  33.233 1.00 49.93  ? 154 LYS   B N   1 
ATOM   2714 C CA  . LYS   B 1 80  ? -8.607  48.440  32.778 1.00 47.79  ? 154 LYS   B CA  1 
ATOM   2715 C C   . LYS   B 1 80  ? -9.899  48.522  31.968 1.00 49.00  ? 154 LYS   B C   1 
ATOM   2716 O O   . LYS   B 1 80  ? -10.025 47.868  30.927 1.00 49.51  ? 154 LYS   B O   1 
ATOM   2717 C CB  . LYS   B 1 80  ? -8.784  47.496  33.971 1.00 51.50  ? 154 LYS   B CB  1 
ATOM   2718 C CG  . LYS   B 1 80  ? -7.507  47.170  34.767 1.00 53.56  ? 154 LYS   B CG  1 
ATOM   2719 C CD  . LYS   B 1 80  ? -7.821  46.164  35.885 1.00 57.44  ? 154 LYS   B CD  1 
ATOM   2720 C CE  . LYS   B 1 80  ? -6.697  46.016  36.911 1.00 60.56  ? 154 LYS   B CE  1 
ATOM   2721 N NZ  . LYS   B 1 80  ? -5.470  45.378  36.355 1.00 68.14  ? 154 LYS   B NZ  1 
ATOM   2722 N N   . LEU   B 1 81  ? -10.871 49.314  32.428 1.00 47.55  ? 155 LEU   B N   1 
ATOM   2723 C CA  . LEU   B 1 81  ? -12.117 49.473  31.680 1.00 51.42  ? 155 LEU   B CA  1 
ATOM   2724 C C   . LEU   B 1 81  ? -11.906 50.123  30.318 1.00 54.22  ? 155 LEU   B C   1 
ATOM   2725 O O   . LEU   B 1 81  ? -12.751 49.958  29.430 1.00 54.91  ? 155 LEU   B O   1 
ATOM   2726 C CB  . LEU   B 1 81  ? -13.120 50.315  32.470 1.00 50.94  ? 155 LEU   B CB  1 
ATOM   2727 C CG  . LEU   B 1 81  ? -13.696 49.785  33.779 1.00 47.20  ? 155 LEU   B CG  1 
ATOM   2728 C CD1 . LEU   B 1 81  ? -14.713 50.771  34.315 1.00 51.16  ? 155 LEU   B CD1 1 
ATOM   2729 C CD2 . LEU   B 1 81  ? -14.337 48.446  33.563 1.00 50.41  ? 155 LEU   B CD2 1 
ATOM   2730 N N   . ALA   B 1 82  ? -10.816 50.871  30.136 1.00 49.95  ? 156 ALA   B N   1 
ATOM   2731 C CA  . ALA   B 1 82  ? -10.599 51.545  28.863 1.00 46.44  ? 156 ALA   B CA  1 
ATOM   2732 C C   . ALA   B 1 82  ? -10.491 50.554  27.709 1.00 51.30  ? 156 ALA   B C   1 
ATOM   2733 O O   . ALA   B 1 82  ? -10.810 50.904  26.567 1.00 56.82  ? 156 ALA   B O   1 
ATOM   2734 C CB  . ALA   B 1 82  ? -9.347  52.419  28.940 1.00 51.75  ? 156 ALA   B CB  1 
ATOM   2735 N N   . GLU   B 1 83  ? -10.059 49.318  27.980 1.00 49.41  ? 157 GLU   B N   1 
ATOM   2736 C CA  . GLU   B 1 83  ? -9.960  48.320  26.918 1.00 46.05  ? 157 GLU   B CA  1 
ATOM   2737 C C   . GLU   B 1 83  ? -11.322 48.037  26.303 1.00 52.42  ? 157 GLU   B C   1 
ATOM   2738 O O   . GLU   B 1 83  ? -11.430 47.798  25.094 1.00 53.96  ? 157 GLU   B O   1 
ATOM   2739 C CB  . GLU   B 1 83  ? -9.340  47.026  27.453 1.00 47.81  ? 157 GLU   B CB  1 
ATOM   2740 C CG  . GLU   B 1 83  ? -9.244  45.914  26.405 1.00 51.61  ? 157 GLU   B CG  1 
ATOM   2741 C CD  . GLU   B 1 83  ? -8.299  44.787  26.804 1.00 55.18  ? 157 GLU   B CD  1 
ATOM   2742 O OE1 . GLU   B 1 83  ? -7.731  44.837  27.919 1.00 54.96  ? 157 GLU   B OE1 1 
ATOM   2743 O OE2 . GLU   B 1 83  ? -8.120  43.847  25.993 1.00 53.93  ? 157 GLU   B OE2 1 
ATOM   2744 N N   . VAL   B 1 84  ? -12.376 48.057  27.121 1.00 50.15  ? 158 VAL   B N   1 
ATOM   2745 C CA  . VAL   B 1 84  ? -13.723 47.883  26.595 1.00 49.67  ? 158 VAL   B CA  1 
ATOM   2746 C C   . VAL   B 1 84  ? -14.098 49.060  25.706 1.00 57.87  ? 158 VAL   B C   1 
ATOM   2747 O O   . VAL   B 1 84  ? -14.772 48.895  24.682 1.00 57.95  ? 158 VAL   B O   1 
ATOM   2748 C CB  . VAL   B 1 84  ? -14.720 47.693  27.751 1.00 53.59  ? 158 VAL   B CB  1 
ATOM   2749 C CG1 . VAL   B 1 84  ? -16.125 47.504  27.219 1.00 55.49  ? 158 VAL   B CG1 1 
ATOM   2750 C CG2 . VAL   B 1 84  ? -14.315 46.504  28.601 1.00 52.98  ? 158 VAL   B CG2 1 
ATOM   2751 N N   . GLY   B 1 85  ? -13.656 50.265  26.072 1.00 56.95  ? 159 GLY   B N   1 
ATOM   2752 C CA  . GLY   B 1 85  ? -13.944 51.424  25.245 1.00 56.93  ? 159 GLY   B CA  1 
ATOM   2753 C C   . GLY   B 1 85  ? -13.271 51.352  23.888 1.00 54.91  ? 159 GLY   B C   1 
ATOM   2754 O O   . GLY   B 1 85  ? -13.845 51.772  22.880 1.00 57.99  ? 159 GLY   B O   1 
ATOM   2755 N N   . SER   B 1 86  ? -12.051 50.813  23.841 1.00 53.47  ? 160 SER   B N   1 
ATOM   2756 C CA  . SER   B 1 86  ? -11.320 50.729  22.580 1.00 51.42  ? 160 SER   B CA  1 
ATOM   2757 C C   . SER   B 1 86  ? -11.944 49.705  21.642 1.00 55.36  ? 160 SER   B C   1 
ATOM   2758 O O   . SER   B 1 86  ? -12.015 49.928  20.428 1.00 57.27  ? 160 SER   B O   1 
ATOM   2759 C CB  . SER   B 1 86  ? -9.856  50.388  22.850 1.00 52.37  ? 160 SER   B CB  1 
ATOM   2760 O OG  . SER   B 1 86  ? -9.244  51.386  23.647 1.00 49.00  ? 160 SER   B OG  1 
ATOM   2761 N N   . HIS   B 1 87  ? -12.393 48.569  22.184 1.00 57.79  ? 161 HIS   B N   1 
ATOM   2762 C CA  . HIS   B 1 87  ? -13.092 47.581  21.367 1.00 55.42  ? 161 HIS   B CA  1 
ATOM   2763 C C   . HIS   B 1 87  ? -14.357 48.154  20.758 1.00 59.59  ? 161 HIS   B C   1 
ATOM   2764 O O   . HIS   B 1 87  ? -14.779 47.724  19.677 1.00 67.13  ? 161 HIS   B O   1 
ATOM   2765 C CB  . HIS   B 1 87  ? -13.447 46.359  22.206 1.00 57.82  ? 161 HIS   B CB  1 
ATOM   2766 C CG  . HIS   B 1 87  ? -12.553 45.183  21.981 1.00 51.63  ? 161 HIS   B CG  1 
ATOM   2767 N ND1 . HIS   B 1 87  ? -12.788 44.250  20.995 1.00 52.01  ? 161 HIS   B ND1 1 
ATOM   2768 C CD2 . HIS   B 1 87  ? -11.437 44.778  22.627 1.00 50.28  ? 161 HIS   B CD2 1 
ATOM   2769 C CE1 . HIS   B 1 87  ? -11.848 43.324  21.038 1.00 51.59  ? 161 HIS   B CE1 1 
ATOM   2770 N NE2 . HIS   B 1 87  ? -11.017 43.620  22.021 1.00 52.99  ? 161 HIS   B NE2 1 
ATOM   2771 N N   . GLU   B 1 88  ? -14.989 49.108  21.441 1.00 62.11  ? 162 GLU   B N   1 
ATOM   2772 C CA  . GLU   B 1 88  ? -16.222 49.687  20.927 1.00 58.76  ? 162 GLU   B CA  1 
ATOM   2773 C C   . GLU   B 1 88  ? -15.968 50.784  19.904 1.00 60.29  ? 162 GLU   B C   1 
ATOM   2774 O O   . GLU   B 1 88  ? -16.833 51.034  19.060 1.00 66.20  ? 162 GLU   B O   1 
ATOM   2775 C CB  . GLU   B 1 88  ? -17.070 50.212  22.089 1.00 59.62  ? 162 GLU   B CB  1 
ATOM   2776 C CG  . GLU   B 1 88  ? -17.503 49.108  23.056 1.00 70.63  ? 162 GLU   B CG  1 
ATOM   2777 C CD  . GLU   B 1 88  ? -18.497 49.580  24.109 1.00 83.53  ? 162 GLU   B CD  1 
ATOM   2778 O OE1 . GLU   B 1 88  ? -18.561 50.806  24.351 1.00 89.06  ? 162 GLU   B OE1 1 
ATOM   2779 O OE2 . GLU   B 1 88  ? -19.216 48.724  24.686 1.00 75.17  ? 162 GLU   B OE2 1 
ATOM   2780 N N   . LYS   B 1 89  ? -14.809 51.447  19.962 1.00 63.25  ? 163 LYS   B N   1 
ATOM   2781 C CA  . LYS   B 1 89  ? -14.431 52.400  18.922 1.00 58.98  ? 163 LYS   B CA  1 
ATOM   2782 C C   . LYS   B 1 89  ? -14.001 51.706  17.636 1.00 59.31  ? 163 LYS   B C   1 
ATOM   2783 O O   . LYS   B 1 89  ? -14.082 52.307  16.559 1.00 64.04  ? 163 LYS   B O   1 
ATOM   2784 C CB  . LYS   B 1 89  ? -13.304 53.313  19.421 1.00 57.16  ? 163 LYS   B CB  1 
ATOM   2785 C CG  . LYS   B 1 89  ? -13.767 54.371  20.408 1.00 59.81  ? 163 LYS   B CG  1 
ATOM   2786 C CD  . LYS   B 1 89  ? -12.595 55.080  21.060 1.00 63.65  ? 163 LYS   B CD  1 
ATOM   2787 C CE  . LYS   B 1 89  ? -13.069 56.035  22.146 1.00 66.05  ? 163 LYS   B CE  1 
ATOM   2788 N NZ  . LYS   B 1 89  ? -11.962 56.395  23.079 1.00 69.77  ? 163 LYS   B NZ  1 
ATOM   2789 N N   . VAL   B 1 90  ? -13.546 50.458  17.730 1.00 61.14  ? 164 VAL   B N   1 
ATOM   2790 C CA  . VAL   B 1 90  ? -13.206 49.680  16.545 1.00 61.33  ? 164 VAL   B CA  1 
ATOM   2791 C C   . VAL   B 1 90  ? -14.459 49.094  15.913 1.00 64.93  ? 164 VAL   B C   1 
ATOM   2792 O O   . VAL   B 1 90  ? -14.607 49.091  14.686 1.00 69.51  ? 164 VAL   B O   1 
ATOM   2793 C CB  . VAL   B 1 90  ? -12.193 48.580  16.912 1.00 56.20  ? 164 VAL   B CB  1 
ATOM   2794 C CG1 . VAL   B 1 90  ? -12.055 47.582  15.776 1.00 57.85  ? 164 VAL   B CG1 1 
ATOM   2795 C CG2 . VAL   B 1 90  ? -10.850 49.191  17.259 1.00 52.58  ? 164 VAL   B CG2 1 
ATOM   2796 N N   . GLY   B 1 91  ? -15.378 48.593  16.734 1.00 63.97  ? 165 GLY   B N   1 
ATOM   2797 C CA  . GLY   B 1 91  ? -16.569 47.992  16.180 1.00 63.41  ? 165 GLY   B CA  1 
ATOM   2798 C C   . GLY   B 1 91  ? -16.257 46.655  15.528 1.00 64.76  ? 165 GLY   B C   1 
ATOM   2799 O O   . GLY   B 1 91  ? -15.249 46.001  15.815 1.00 73.43  ? 165 GLY   B O   1 
ATOM   2800 N N   . GLN   B 1 92  ? -17.146 46.260  14.622 1.00 66.00  ? 166 GLN   B N   1 
ATOM   2801 C CA  . GLN   B 1 92  ? -17.073 44.969  13.952 1.00 65.28  ? 166 GLN   B CA  1 
ATOM   2802 C C   . GLN   B 1 92  ? -16.392 45.131  12.600 1.00 63.34  ? 166 GLN   B C   1 
ATOM   2803 O O   . GLN   B 1 92  ? -16.847 45.912  11.757 1.00 62.12  ? 166 GLN   B O   1 
ATOM   2804 C CB  . GLN   B 1 92  ? -18.467 44.370  13.779 1.00 65.71  ? 166 GLN   B CB  1 
ATOM   2805 C CG  . GLN   B 1 92  ? -19.236 44.238  15.079 1.00 72.71  ? 166 GLN   B CG  1 
ATOM   2806 C CD  . GLN   B 1 92  ? -20.533 43.470  14.910 1.00 87.23  ? 166 GLN   B CD  1 
ATOM   2807 O OE1 . GLN   B 1 92  ? -20.898 42.655  15.759 1.00 89.41  ? 166 GLN   B OE1 1 
ATOM   2808 N NE2 . GLN   B 1 92  ? -21.238 43.725  13.810 1.00 86.26  ? 166 GLN   B NE2 1 
ATOM   2809 N N   . HIS   B 1 93  ? -15.304 44.394  12.399 1.00 61.84  ? 167 HIS   B N   1 
ATOM   2810 C CA  . HIS   B 1 93  ? -14.603 44.394  11.137 1.00 61.53  ? 167 HIS   B CA  1 
ATOM   2811 C C   . HIS   B 1 93  ? -14.024 42.998  10.988 1.00 61.63  ? 167 HIS   B C   1 
ATOM   2812 O O   . HIS   B 1 93  ? -13.542 42.431  11.980 1.00 57.47  ? 167 HIS   B O   1 
ATOM   2813 C CB  . HIS   B 1 93  ? -13.492 45.447  11.085 1.00 63.09  ? 167 HIS   B CB  1 
ATOM   2814 C CG  . HIS   B 1 93  ? -12.814 45.549  9.754  1.00 61.20  ? 167 HIS   B CG  1 
ATOM   2815 N ND1 . HIS   B 1 93  ? -11.696 44.809  9.429  1.00 59.16  ? 167 HIS   B ND1 1 
ATOM   2816 C CD2 . HIS   B 1 93  ? -13.097 46.305  8.666  1.00 62.40  ? 167 HIS   B CD2 1 
ATOM   2817 C CE1 . HIS   B 1 93  ? -11.319 45.105  8.197  1.00 58.96  ? 167 HIS   B CE1 1 
ATOM   2818 N NE2 . HIS   B 1 93  ? -12.153 46.010  7.712  1.00 64.66  ? 167 HIS   B NE2 1 
ATOM   2819 N N   . PRO   B 1 94  ? -14.055 42.423  9.781  1.00 62.93  ? 168 PRO   B N   1 
ATOM   2820 C CA  . PRO   B 1 94  ? -13.645 41.016  9.617  1.00 59.80  ? 168 PRO   B CA  1 
ATOM   2821 C C   . PRO   B 1 94  ? -12.211 40.720  10.027 1.00 59.27  ? 168 PRO   B C   1 
ATOM   2822 O O   . PRO   B 1 94  ? -11.866 39.540  10.164 1.00 67.71  ? 168 PRO   B O   1 
ATOM   2823 C CB  . PRO   B 1 94  ? -13.844 40.764  8.118  1.00 59.63  ? 168 PRO   B CB  1 
ATOM   2824 C CG  . PRO   B 1 94  ? -14.829 41.802  7.685  1.00 63.59  ? 168 PRO   B CG  1 
ATOM   2825 C CD  . PRO   B 1 94  ? -14.560 43.005  8.527  1.00 57.26  ? 168 PRO   B CD  1 
ATOM   2826 N N   . CYS   B 1 95  ? -11.365 41.728  10.229 1.00 61.09  ? 169 CYS   B N   1 
ATOM   2827 C CA  . CYS   B 1 95  ? -9.974  41.489  10.588 1.00 54.56  ? 169 CYS   B CA  1 
ATOM   2828 C C   . CYS   B 1 95  ? -9.633  41.970  11.991 1.00 51.43  ? 169 CYS   B C   1 
ATOM   2829 O O   . CYS   B 1 95  ? -8.450  42.035  12.338 1.00 55.32  ? 169 CYS   B O   1 
ATOM   2830 C CB  . CYS   B 1 95  ? -9.043  42.144  9.565  1.00 55.10  ? 169 CYS   B CB  1 
ATOM   2831 S SG  . CYS   B 1 95  ? -9.331  41.620  7.859  1.00 65.65  ? 169 CYS   B SG  1 
ATOM   2832 N N   . CYS   B 1 96  ? -10.629 42.300  12.811 1.00 50.18  ? 170 CYS   B N   1 
ATOM   2833 C CA  . CYS   B 1 96  ? -10.403 42.673  14.204 1.00 51.95  ? 170 CYS   B CA  1 
ATOM   2834 C C   . CYS   B 1 96  ? -11.189 41.739  15.114 1.00 54.47  ? 170 CYS   B C   1 
ATOM   2835 O O   . CYS   B 1 96  ? -12.337 41.396  14.817 1.00 58.18  ? 170 CYS   B O   1 
ATOM   2836 C CB  . CYS   B 1 96  ? -10.820 44.124  14.468 1.00 60.56  ? 170 CYS   B CB  1 
ATOM   2837 S SG  . CYS   B 1 96  ? -10.035 45.367  13.404 1.00 60.65  ? 170 CYS   B SG  1 
ATOM   2838 N N   . VAL   B 1 97  ? -10.574 41.336  16.231 1.00 53.18  ? 171 VAL   B N   1 
ATOM   2839 C CA  . VAL   B 1 97  ? -11.260 40.465  17.183 1.00 53.12  ? 171 VAL   B CA  1 
ATOM   2840 C C   . VAL   B 1 97  ? -12.518 41.159  17.682 1.00 59.70  ? 171 VAL   B C   1 
ATOM   2841 O O   . VAL   B 1 97  ? -12.472 42.307  18.139 1.00 59.30  ? 171 VAL   B O   1 
ATOM   2842 C CB  . VAL   B 1 97  ? -10.333 40.100  18.351 1.00 49.67  ? 171 VAL   B CB  1 
ATOM   2843 C CG1 . VAL   B 1 97  ? -11.068 39.212  19.345 1.00 54.02  ? 171 VAL   B CG1 1 
ATOM   2844 C CG2 . VAL   B 1 97  ? -9.076  39.409  17.848 1.00 48.64  ? 171 VAL   B CG2 1 
ATOM   2845 N N   . ARG   B 1 98  ? -13.650 40.467  17.597 1.00 53.98  ? 172 ARG   B N   1 
ATOM   2846 C CA  . ARG   B 1 98  ? -14.934 41.045  17.974 1.00 54.29  ? 172 ARG   B CA  1 
ATOM   2847 C C   . ARG   B 1 98  ? -15.226 40.788  19.450 1.00 55.81  ? 172 ARG   B C   1 
ATOM   2848 O O   . ARG   B 1 98  ? -15.124 39.651  19.919 1.00 60.87  ? 172 ARG   B O   1 
ATOM   2849 C CB  . ARG   B 1 98  ? -16.054 40.469  17.112 1.00 58.56  ? 172 ARG   B CB  1 
ATOM   2850 C CG  . ARG   B 1 98  ? -17.422 41.042  17.417 1.00 67.35  ? 172 ARG   B CG  1 
ATOM   2851 C CD  . ARG   B 1 98  ? -18.518 40.312  16.660 1.00 67.02  ? 172 ARG   B CD  1 
ATOM   2852 N NE  . ARG   B 1 98  ? -18.596 38.908  17.045 1.00 73.74  ? 172 ARG   B NE  1 
ATOM   2853 C CZ  . ARG   B 1 98  ? -18.175 37.894  16.298 1.00 81.00  ? 172 ARG   B CZ  1 
ATOM   2854 N NH1 . ARG   B 1 98  ? -17.661 38.088  15.092 1.00 78.43  ? 172 ARG   B NH1 1 
ATOM   2855 N NH2 . ARG   B 1 98  ? -18.273 36.652  16.772 1.00 77.79  ? 172 ARG   B NH2 1 
ATOM   2856 N N   . LEU   B 1 99  ? -15.589 41.846  20.175 1.00 55.88  ? 173 LEU   B N   1 
ATOM   2857 C CA  . LEU   B 1 99  ? -15.961 41.745  21.582 1.00 54.61  ? 173 LEU   B CA  1 
ATOM   2858 C C   . LEU   B 1 99  ? -17.468 41.556  21.691 1.00 56.80  ? 173 LEU   B C   1 
ATOM   2859 O O   . LEU   B 1 99  ? -18.236 42.384  21.188 1.00 57.08  ? 173 LEU   B O   1 
ATOM   2860 C CB  . LEU   B 1 99  ? -15.536 42.994  22.354 1.00 54.31  ? 173 LEU   B CB  1 
ATOM   2861 C CG  . LEU   B 1 99  ? -15.965 43.070  23.828 1.00 55.15  ? 173 LEU   B CG  1 
ATOM   2862 C CD1 . LEU   B 1 99  ? -15.072 42.206  24.701 1.00 50.29  ? 173 LEU   B CD1 1 
ATOM   2863 C CD2 . LEU   B 1 99  ? -15.981 44.506  24.344 1.00 53.87  ? 173 LEU   B CD2 1 
ATOM   2864 N N   . GLU   B 1 100 ? -17.888 40.476  22.351 1.00 57.81  ? 174 GLU   B N   1 
ATOM   2865 C CA  . GLU   B 1 100 ? -19.302 40.181  22.570 1.00 55.85  ? 174 GLU   B CA  1 
ATOM   2866 C C   . GLU   B 1 100 ? -19.859 40.896  23.795 1.00 53.47  ? 174 GLU   B C   1 
ATOM   2867 O O   . GLU   B 1 100 ? -20.943 41.481  23.738 1.00 58.09  ? 174 GLU   B O   1 
ATOM   2868 C CB  . GLU   B 1 100 ? -19.513 38.671  22.730 1.00 59.97  ? 174 GLU   B CB  1 
ATOM   2869 C CG  . GLU   B 1 100 ? -19.265 37.866  21.471 1.00 68.92  ? 174 GLU   B CG  1 
ATOM   2870 C CD  . GLU   B 1 100 ? -20.359 38.037  20.431 1.00 78.15  ? 174 GLU   B CD  1 
ATOM   2871 O OE1 . GLU   B 1 100 ? -21.549 38.203  20.810 1.00 74.12  ? 174 GLU   B OE1 1 
ATOM   2872 O OE2 . GLU   B 1 100 ? -20.017 38.003  19.226 1.00 80.97  ? 174 GLU   B OE2 1 
ATOM   2873 N N   . GLN   B 1 101 ? -19.135 40.851  24.909 1.00 58.34  ? 175 GLN   B N   1 
ATOM   2874 C CA  . GLN   B 1 101 ? -19.655 41.360  26.169 1.00 55.50  ? 175 GLN   B CA  1 
ATOM   2875 C C   . GLN   B 1 101 ? -18.492 41.633  27.110 1.00 52.01  ? 175 GLN   B C   1 
ATOM   2876 O O   . GLN   B 1 101 ? -17.404 41.070  26.964 1.00 50.39  ? 175 GLN   B O   1 
ATOM   2877 C CB  . GLN   B 1 101 ? -20.636 40.367  26.793 1.00 50.40  ? 175 GLN   B CB  1 
ATOM   2878 C CG  . GLN   B 1 101 ? -21.370 40.904  27.986 1.00 59.02  ? 175 GLN   B CG  1 
ATOM   2879 C CD  . GLN   B 1 101 ? -22.592 40.097  28.298 1.00 67.05  ? 175 GLN   B CD  1 
ATOM   2880 O OE1 . GLN   B 1 101 ? -22.829 39.052  27.688 1.00 73.51  ? 175 GLN   B OE1 1 
ATOM   2881 N NE2 . GLN   B 1 101 ? -23.388 40.572  29.248 1.00 78.35  ? 175 GLN   B NE2 1 
ATOM   2882 N N   . ALA   B 1 102 ? -18.736 42.513  28.075 1.00 50.21  ? 176 ALA   B N   1 
ATOM   2883 C CA  . ALA   B 1 102 ? -17.784 42.763  29.140 1.00 48.38  ? 176 ALA   B CA  1 
ATOM   2884 C C   . ALA   B 1 102 ? -18.561 43.083  30.406 1.00 50.98  ? 176 ALA   B C   1 
ATOM   2885 O O   . ALA   B 1 102 ? -19.667 43.628  30.349 1.00 53.84  ? 176 ALA   B O   1 
ATOM   2886 C CB  . ALA   B 1 102 ? -16.828 43.901  28.783 1.00 49.22  ? 176 ALA   B CB  1 
ATOM   2887 N N   . TRP   B 1 103 ? -17.983 42.724  31.550 1.00 49.76  ? 177 TRP   B N   1 
ATOM   2888 C CA  . TRP   B 1 103 ? -18.630 42.991  32.826 1.00 51.90  ? 177 TRP   B CA  1 
ATOM   2889 C C   . TRP   B 1 103 ? -17.585 42.979  33.927 1.00 50.49  ? 177 TRP   B C   1 
ATOM   2890 O O   . TRP   B 1 103 ? -16.467 42.489  33.746 1.00 46.54  ? 177 TRP   B O   1 
ATOM   2891 C CB  . TRP   B 1 103 ? -19.736 41.976  33.126 1.00 55.16  ? 177 TRP   B CB  1 
ATOM   2892 C CG  . TRP   B 1 103 ? -19.260 40.561  33.345 1.00 53.79  ? 177 TRP   B CG  1 
ATOM   2893 C CD1 . TRP   B 1 103 ? -19.011 39.953  34.545 1.00 50.39  ? 177 TRP   B CD1 1 
ATOM   2894 C CD2 . TRP   B 1 103 ? -18.999 39.572  32.334 1.00 52.02  ? 177 TRP   B CD2 1 
ATOM   2895 N NE1 . TRP   B 1 103 ? -18.601 38.654  34.343 1.00 51.60  ? 177 TRP   B NE1 1 
ATOM   2896 C CE2 . TRP   B 1 103 ? -18.587 38.396  32.996 1.00 50.01  ? 177 TRP   B CE2 1 
ATOM   2897 C CE3 . TRP   B 1 103 ? -19.070 39.569  30.937 1.00 51.31  ? 177 TRP   B CE3 1 
ATOM   2898 C CZ2 . TRP   B 1 103 ? -18.246 37.234  32.307 1.00 50.78  ? 177 TRP   B CZ2 1 
ATOM   2899 C CZ3 . TRP   B 1 103 ? -18.730 38.413  30.256 1.00 47.33  ? 177 TRP   B CZ3 1 
ATOM   2900 C CH2 . TRP   B 1 103 ? -18.323 37.263  30.941 1.00 49.30  ? 177 TRP   B CH2 1 
ATOM   2901 N N   . GLU   B 1 104 ? -17.967 43.528  35.075 1.00 50.90  ? 178 GLU   B N   1 
ATOM   2902 C CA  . GLU   B 1 104 ? -17.112 43.546  36.249 1.00 53.53  ? 178 GLU   B CA  1 
ATOM   2903 C C   . GLU   B 1 104 ? -17.857 42.928  37.421 1.00 54.46  ? 178 GLU   B C   1 
ATOM   2904 O O   . GLU   B 1 104 ? -19.059 43.154  37.598 1.00 58.30  ? 178 GLU   B O   1 
ATOM   2905 C CB  . GLU   B 1 104 ? -16.646 44.975  36.605 1.00 52.08  ? 178 GLU   B CB  1 
ATOM   2906 C CG  . GLU   B 1 104 ? -17.742 45.903  37.120 1.00 64.56  ? 178 GLU   B CG  1 
ATOM   2907 C CD  . GLU   B 1 104 ? -17.228 47.296  37.470 1.00 68.26  ? 178 GLU   B CD  1 
ATOM   2908 O OE1 . GLU   B 1 104 ? -16.080 47.407  37.953 1.00 67.24  ? 178 GLU   B OE1 1 
ATOM   2909 O OE2 . GLU   B 1 104 ? -17.972 48.279  37.259 1.00 68.44  ? 178 GLU   B OE2 1 
ATOM   2910 N N   . GLU   B 1 105 ? -17.140 42.133  38.208 1.00 53.32  ? 179 GLU   B N   1 
ATOM   2911 C CA  . GLU   B 1 105 ? -17.706 41.534  39.407 1.00 59.52  ? 179 GLU   B CA  1 
ATOM   2912 C C   . GLU   B 1 105 ? -16.601 41.393  40.440 1.00 60.80  ? 179 GLU   B C   1 
ATOM   2913 O O   . GLU   B 1 105 ? -15.539 40.838  40.139 1.00 59.31  ? 179 GLU   B O   1 
ATOM   2914 C CB  . GLU   B 1 105 ? -18.333 40.172  39.104 1.00 65.16  ? 179 GLU   B CB  1 
ATOM   2915 C CG  . GLU   B 1 105 ? -19.136 39.601  40.253 1.00 69.88  ? 179 GLU   B CG  1 
ATOM   2916 C CD  . GLU   B 1 105 ? -19.761 38.273  39.901 1.00 75.03  ? 179 GLU   B CD  1 
ATOM   2917 O OE1 . GLU   B 1 105 ? -19.235 37.600  38.986 1.00 81.48  ? 179 GLU   B OE1 1 
ATOM   2918 O OE2 . GLU   B 1 105 ? -20.776 37.906  40.531 1.00 80.99  ? 179 GLU   B OE2 1 
ATOM   2919 N N   . GLY   B 1 106 ? -16.850 41.905  41.643 1.00 60.77  ? 180 GLY   B N   1 
ATOM   2920 C CA  . GLY   B 1 106 ? -15.861 41.836  42.707 1.00 61.23  ? 180 GLY   B CA  1 
ATOM   2921 C C   . GLY   B 1 106 ? -14.556 42.537  42.401 1.00 66.31  ? 180 GLY   B C   1 
ATOM   2922 O O   . GLY   B 1 106 ? -13.510 42.141  42.926 1.00 69.77  ? 180 GLY   B O   1 
ATOM   2923 N N   . GLY   B 1 107 ? -14.583 43.577  41.570 1.00 65.18  ? 181 GLY   B N   1 
ATOM   2924 C CA  . GLY   B 1 107 ? -13.366 44.266  41.202 1.00 60.30  ? 181 GLY   B CA  1 
ATOM   2925 C C   . GLY   B 1 107 ? -12.571 43.607  40.101 1.00 58.43  ? 181 GLY   B C   1 
ATOM   2926 O O   . GLY   B 1 107 ? -11.495 44.114  39.748 1.00 57.48  ? 181 GLY   B O   1 
ATOM   2927 N N   . ILE   B 1 108 ? -13.059 42.498  39.552 1.00 54.61  ? 182 ILE   B N   1 
ATOM   2928 C CA  . ILE   B 1 108 ? -12.432 41.808  38.431 1.00 53.43  ? 182 ILE   B CA  1 
ATOM   2929 C C   . ILE   B 1 108 ? -13.146 42.213  37.149 1.00 49.35  ? 182 ILE   B C   1 
ATOM   2930 O O   . ILE   B 1 108 ? -14.372 42.377  37.136 1.00 53.16  ? 182 ILE   B O   1 
ATOM   2931 C CB  . ILE   B 1 108 ? -12.488 40.283  38.631 1.00 55.38  ? 182 ILE   B CB  1 
ATOM   2932 C CG1 . ILE   B 1 108 ? -11.844 39.891  39.959 1.00 53.01  ? 182 ILE   B CG1 1 
ATOM   2933 C CG2 . ILE   B 1 108 ? -11.782 39.579  37.494 1.00 53.11  ? 182 ILE   B CG2 1 
ATOM   2934 C CD1 . ILE   B 1 108 ? -10.323 39.956  39.928 1.00 58.33  ? 182 ILE   B CD1 1 
ATOM   2935 N N   . LEU   B 1 109 ? -12.391 42.362  36.065 1.00 48.07  ? 183 LEU   B N   1 
ATOM   2936 C CA  . LEU   B 1 109 ? -12.943 42.762  34.775 1.00 45.89  ? 183 LEU   B CA  1 
ATOM   2937 C C   . LEU   B 1 109 ? -12.889 41.583  33.812 1.00 46.28  ? 183 LEU   B C   1 
ATOM   2938 O O   . LEU   B 1 109 ? -11.802 41.068  33.522 1.00 47.89  ? 183 LEU   B O   1 
ATOM   2939 C CB  . LEU   B 1 109 ? -12.184 43.952  34.195 1.00 46.88  ? 183 LEU   B CB  1 
ATOM   2940 C CG  . LEU   B 1 109 ? -12.607 44.305  32.769 1.00 46.29  ? 183 LEU   B CG  1 
ATOM   2941 C CD1 . LEU   B 1 109 ? -13.986 44.949  32.769 1.00 49.53  ? 183 LEU   B CD1 1 
ATOM   2942 C CD2 . LEU   B 1 109 ? -11.589 45.207  32.105 1.00 42.24  ? 183 LEU   B CD2 1 
ATOM   2943 N N   . TYR   B 1 110 ? -14.056 41.175  33.307 1.00 46.46  ? 184 TYR   B N   1 
ATOM   2944 C CA  . TYR   B 1 110 ? -14.187 40.084  32.348 1.00 45.55  ? 184 TYR   B CA  1 
ATOM   2945 C C   . TYR   B 1 110 ? -14.479 40.632  30.955 1.00 47.58  ? 184 TYR   B C   1 
ATOM   2946 O O   . TYR   B 1 110 ? -15.361 41.481  30.791 1.00 52.70  ? 184 TYR   B O   1 
ATOM   2947 C CB  . TYR   B 1 110 ? -15.306 39.127  32.760 1.00 49.18  ? 184 TYR   B CB  1 
ATOM   2948 C CG  . TYR   B 1 110 ? -15.100 38.470  34.101 1.00 49.55  ? 184 TYR   B CG  1 
ATOM   2949 C CD1 . TYR   B 1 110 ? -15.386 39.150  35.278 1.00 48.56  ? 184 TYR   B CD1 1 
ATOM   2950 C CD2 . TYR   B 1 110 ? -14.619 37.169  34.192 1.00 50.66  ? 184 TYR   B CD2 1 
ATOM   2951 C CE1 . TYR   B 1 110 ? -15.199 38.552  36.508 1.00 53.01  ? 184 TYR   B CE1 1 
ATOM   2952 C CE2 . TYR   B 1 110 ? -14.425 36.564  35.418 1.00 53.88  ? 184 TYR   B CE2 1 
ATOM   2953 C CZ  . TYR   B 1 110 ? -14.719 37.262  36.574 1.00 54.25  ? 184 TYR   B CZ  1 
ATOM   2954 O OH  . TYR   B 1 110 ? -14.533 36.669  37.803 1.00 65.94  ? 184 TYR   B OH  1 
ATOM   2955 N N   . LEU   B 1 111 ? -13.760 40.126  29.955 1.00 47.74  ? 185 LEU   B N   1 
ATOM   2956 C CA  . LEU   B 1 111 ? -13.981 40.466  28.554 1.00 44.09  ? 185 LEU   B CA  1 
ATOM   2957 C C   . LEU   B 1 111 ? -14.259 39.189  27.779 1.00 48.03  ? 185 LEU   B C   1 
ATOM   2958 O O   . LEU   B 1 111 ? -13.419 38.285  27.759 1.00 51.08  ? 185 LEU   B O   1 
ATOM   2959 C CB  . LEU   B 1 111 ? -12.769 41.178  27.957 1.00 45.33  ? 185 LEU   B CB  1 
ATOM   2960 C CG  . LEU   B 1 111 ? -12.801 42.698  27.959 1.00 50.47  ? 185 LEU   B CG  1 
ATOM   2961 C CD1 . LEU   B 1 111 ? -12.742 43.203  29.376 1.00 52.32  ? 185 LEU   B CD1 1 
ATOM   2962 C CD2 . LEU   B 1 111 ? -11.650 43.249  27.139 1.00 55.01  ? 185 LEU   B CD2 1 
ATOM   2963 N N   . GLN   B 1 112 ? -15.419 39.124  27.131 1.00 50.10  ? 186 GLN   B N   1 
ATOM   2964 C CA  . GLN   B 1 112 ? -15.810 37.980  26.313 1.00 50.74  ? 186 GLN   B CA  1 
ATOM   2965 C C   . GLN   B 1 112 ? -15.677 38.352  24.838 1.00 53.31  ? 186 GLN   B C   1 
ATOM   2966 O O   . GLN   B 1 112 ? -16.335 39.287  24.371 1.00 57.79  ? 186 GLN   B O   1 
ATOM   2967 C CB  . GLN   B 1 112 ? -17.245 37.554  26.636 1.00 51.66  ? 186 GLN   B CB  1 
ATOM   2968 C CG  . GLN   B 1 112 ? -17.790 36.442  25.749 1.00 55.63  ? 186 GLN   B CG  1 
ATOM   2969 C CD  . GLN   B 1 112 ? -19.197 36.005  26.135 1.00 59.47  ? 186 GLN   B CD  1 
ATOM   2970 O OE1 . GLN   B 1 112 ? -19.800 36.556  27.057 1.00 60.71  ? 186 GLN   B OE1 1 
ATOM   2971 N NE2 . GLN   B 1 112 ? -19.724 35.007  25.430 1.00 56.16  ? 186 GLN   B NE2 1 
ATOM   2972 N N   . THR   B 1 113 ? -14.829 37.631  24.106 1.00 52.80  ? 187 THR   B N   1 
ATOM   2973 C CA  . THR   B 1 113 ? -14.638 37.873  22.681 1.00 53.16  ? 187 THR   B CA  1 
ATOM   2974 C C   . THR   B 1 113 ? -14.933 36.612  21.886 1.00 55.29  ? 187 THR   B C   1 
ATOM   2975 O O   . THR   B 1 113 ? -15.108 35.521  22.436 1.00 60.01  ? 187 THR   B O   1 
ATOM   2976 C CB  . THR   B 1 113 ? -13.214 38.333  22.369 1.00 53.09  ? 187 THR   B CB  1 
ATOM   2977 O OG1 . THR   B 1 113 ? -12.302 37.288  22.722 1.00 56.68  ? 187 THR   B OG1 1 
ATOM   2978 C CG2 . THR   B 1 113 ? -12.878 39.589  23.146 1.00 51.38  ? 187 THR   B CG2 1 
ATOM   2979 N N   . GLU   B 1 114 ? -14.993 36.774  20.569 1.00 53.74  ? 188 GLU   B N   1 
ATOM   2980 C CA  . GLU   B 1 114 ? -15.075 35.610  19.704 1.00 54.06  ? 188 GLU   B CA  1 
ATOM   2981 C C   . GLU   B 1 114 ? -13.809 34.783  19.859 1.00 61.10  ? 188 GLU   B C   1 
ATOM   2982 O O   . GLU   B 1 114 ? -12.730 35.308  20.151 1.00 63.99  ? 188 GLU   B O   1 
ATOM   2983 C CB  . GLU   B 1 114 ? -15.243 36.028  18.248 1.00 52.54  ? 188 GLU   B CB  1 
ATOM   2984 C CG  . GLU   B 1 114 ? -14.035 36.773  17.697 1.00 59.60  ? 188 GLU   B CG  1 
ATOM   2985 C CD  . GLU   B 1 114 ? -14.189 37.113  16.231 1.00 65.41  ? 188 GLU   B CD  1 
ATOM   2986 O OE1 . GLU   B 1 114 ? -14.723 36.268  15.478 1.00 69.17  ? 188 GLU   B OE1 1 
ATOM   2987 O OE2 . GLU   B 1 114 ? -13.788 38.230  15.837 1.00 67.37  ? 188 GLU   B OE2 1 
ATOM   2988 N N   . LEU   B 1 115 ? -13.946 33.477  19.669 1.00 57.58  ? 189 LEU   B N   1 
ATOM   2989 C CA  . LEU   B 1 115 ? -12.797 32.589  19.756 1.00 58.74  ? 189 LEU   B CA  1 
ATOM   2990 C C   . LEU   B 1 115 ? -12.084 32.568  18.411 1.00 58.00  ? 189 LEU   B C   1 
ATOM   2991 O O   . LEU   B 1 115 ? -12.700 32.275  17.380 1.00 55.25  ? 189 LEU   B O   1 
ATOM   2992 C CB  . LEU   B 1 115 ? -13.237 31.187  20.168 1.00 62.33  ? 189 LEU   B CB  1 
ATOM   2993 C CG  . LEU   B 1 115 ? -12.130 30.186  20.513 1.00 58.01  ? 189 LEU   B CG  1 
ATOM   2994 C CD1 . LEU   B 1 115 ? -11.232 30.731  21.594 1.00 54.83  ? 189 LEU   B CD1 1 
ATOM   2995 C CD2 . LEU   B 1 115 ? -12.740 28.873  20.957 1.00 63.27  ? 189 LEU   B CD2 1 
ATOM   2996 N N   . CYS   B 1 116 ? -10.800 32.905  18.420 1.00 57.65  ? 190 CYS   B N   1 
ATOM   2997 C CA  . CYS   B 1 116 ? -9.950  32.797  17.249 1.00 56.48  ? 190 CYS   B CA  1 
ATOM   2998 C C   . CYS   B 1 116 ? -9.024  31.594  17.413 1.00 59.25  ? 190 CYS   B C   1 
ATOM   2999 O O   . CYS   B 1 116 ? -9.132  30.821  18.371 1.00 62.22  ? 190 CYS   B O   1 
ATOM   3000 C CB  . CYS   B 1 116 ? -9.161  34.091  17.048 1.00 56.36  ? 190 CYS   B CB  1 
ATOM   3001 S SG  . CYS   B 1 116 ? -10.171 35.561  16.798 1.00 60.90  ? 190 CYS   B SG  1 
ATOM   3002 N N   . GLY   B 1 117 ? -8.097  31.424  16.478 1.00 59.32  ? 191 GLY   B N   1 
ATOM   3003 C CA  . GLY   B 1 117 ? -7.112  30.379  16.589 1.00 53.01  ? 191 GLY   B CA  1 
ATOM   3004 C C   . GLY   B 1 117 ? -5.936  30.829  17.427 1.00 54.92  ? 191 GLY   B C   1 
ATOM   3005 O O   . GLY   B 1 117 ? -6.051  31.732  18.259 1.00 55.30  ? 191 GLY   B O   1 
ATOM   3006 N N   . PRO   B 1 118 ? -4.778  30.208  17.221 1.00 54.89  ? 192 PRO   B N   1 
ATOM   3007 C CA  . PRO   B 1 118 ? -3.583  30.608  17.966 1.00 51.27  ? 192 PRO   B CA  1 
ATOM   3008 C C   . PRO   B 1 118 ? -3.073  31.970  17.526 1.00 47.51  ? 192 PRO   B C   1 
ATOM   3009 O O   . PRO   B 1 118 ? -3.364  32.457  16.433 1.00 50.37  ? 192 PRO   B O   1 
ATOM   3010 C CB  . PRO   B 1 118 ? -2.573  29.514  17.618 1.00 49.34  ? 192 PRO   B CB  1 
ATOM   3011 C CG  . PRO   B 1 118 ? -2.996  29.071  16.259 1.00 52.50  ? 192 PRO   B CG  1 
ATOM   3012 C CD  . PRO   B 1 118 ? -4.498  29.098  16.296 1.00 54.94  ? 192 PRO   B CD  1 
ATOM   3013 N N   . SER   B 1 119 ? -2.283  32.582  18.402 1.00 45.62  ? 193 SER   B N   1 
ATOM   3014 C CA  . SER   B 1 119 ? -1.628  33.819  18.033 1.00 45.11  ? 193 SER   B CA  1 
ATOM   3015 C C   . SER   B 1 119 ? -0.540  33.545  17.006 1.00 42.12  ? 193 SER   B C   1 
ATOM   3016 O O   . SER   B 1 119 ? -0.036  32.430  16.873 1.00 45.69  ? 193 SER   B O   1 
ATOM   3017 C CB  . SER   B 1 119 ? -1.013  34.497  19.248 1.00 40.95  ? 193 SER   B CB  1 
ATOM   3018 O OG  . SER   B 1 119 ? 0.234   33.905  19.540 1.00 42.95  ? 193 SER   B OG  1 
ATOM   3019 N N   . LEU   B 1 120 ? -0.174  34.592  16.276 1.00 42.86  ? 194 LEU   B N   1 
ATOM   3020 C CA  . LEU   B 1 120 ? 0.903   34.464  15.306 1.00 42.91  ? 194 LEU   B CA  1 
ATOM   3021 C C   . LEU   B 1 120 ? 2.224   34.129  15.986 1.00 44.69  ? 194 LEU   B C   1 
ATOM   3022 O O   . LEU   B 1 120 ? 3.097   33.506  15.373 1.00 48.49  ? 194 LEU   B O   1 
ATOM   3023 C CB  . LEU   B 1 120 ? 1.022   35.753  14.497 1.00 41.71  ? 194 LEU   B CB  1 
ATOM   3024 C CG  . LEU   B 1 120 ? 2.003   35.738  13.330 1.00 43.14  ? 194 LEU   B CG  1 
ATOM   3025 C CD1 . LEU   B 1 120 ? 1.593   34.679  12.333 1.00 48.94  ? 194 LEU   B CD1 1 
ATOM   3026 C CD2 . LEU   B 1 120 ? 2.060   37.100  12.675 1.00 41.47  ? 194 LEU   B CD2 1 
ATOM   3027 N N   . GLN   B 1 121 ? 2.388   34.528  17.250 1.00 38.29  ? 195 GLN   B N   1 
ATOM   3028 C CA  . GLN   B 1 121 ? 3.581   34.149  18.003 1.00 39.37  ? 195 GLN   B CA  1 
ATOM   3029 C C   . GLN   B 1 121 ? 3.644   32.640  18.188 1.00 43.18  ? 195 GLN   B C   1 
ATOM   3030 O O   . GLN   B 1 121 ? 4.671   32.007  17.917 1.00 47.62  ? 195 GLN   B O   1 
ATOM   3031 C CB  . GLN   B 1 121 ? 3.578   34.853  19.359 1.00 39.05  ? 195 GLN   B CB  1 
ATOM   3032 C CG  . GLN   B 1 121 ? 4.865   34.754  20.154 1.00 36.98  ? 195 GLN   B CG  1 
ATOM   3033 C CD  . GLN   B 1 121 ? 4.756   35.486  21.482 1.00 45.79  ? 195 GLN   B CD  1 
ATOM   3034 O OE1 . GLN   B 1 121 ? 3.659   35.646  22.021 1.00 51.93  ? 195 GLN   B OE1 1 
ATOM   3035 N NE2 . GLN   B 1 121 ? 5.886   35.944  22.012 1.00 45.26  ? 195 GLN   B NE2 1 
ATOM   3036 N N   . GLN   B 1 122 ? 2.545   32.046  18.651 1.00 45.12  ? 196 GLN   B N   1 
ATOM   3037 C CA  . GLN   B 1 122 ? 2.502   30.605  18.858 1.00 40.99  ? 196 GLN   B CA  1 
ATOM   3038 C C   . GLN   B 1 122 ? 2.730   29.857  17.556 1.00 41.98  ? 196 GLN   B C   1 
ATOM   3039 O O   . GLN   B 1 122 ? 3.515   28.904  17.503 1.00 53.17  ? 196 GLN   B O   1 
ATOM   3040 C CB  . GLN   B 1 122 ? 1.161   30.213  19.466 1.00 42.29  ? 196 GLN   B CB  1 
ATOM   3041 C CG  . GLN   B 1 122 ? 0.934   30.770  20.856 1.00 47.05  ? 196 GLN   B CG  1 
ATOM   3042 C CD  . GLN   B 1 122 ? -0.400  30.344  21.426 1.00 49.01  ? 196 GLN   B CD  1 
ATOM   3043 O OE1 . GLN   B 1 122 ? -1.434  30.460  20.766 1.00 51.09  ? 196 GLN   B OE1 1 
ATOM   3044 N NE2 . GLN   B 1 122 ? -0.386  29.835  22.653 1.00 60.17  ? 196 GLN   B NE2 1 
ATOM   3045 N N   . HIS   B 1 123 ? 2.045   30.273  16.495 1.00 42.14  ? 197 HIS   B N   1 
ATOM   3046 C CA  . HIS   B 1 123 ? 2.194   29.615  15.202 1.00 43.73  ? 197 HIS   B CA  1 
ATOM   3047 C C   . HIS   B 1 123 ? 3.649   29.604  14.753 1.00 48.22  ? 197 HIS   B C   1 
ATOM   3048 O O   . HIS   B 1 123 ? 4.184   28.557  14.370 1.00 51.10  ? 197 HIS   B O   1 
ATOM   3049 C CB  . HIS   B 1 123 ? 1.316   30.320  14.175 1.00 42.70  ? 197 HIS   B CB  1 
ATOM   3050 C CG  . HIS   B 1 123 ? 1.493   29.817  12.781 1.00 48.67  ? 197 HIS   B CG  1 
ATOM   3051 N ND1 . HIS   B 1 123 ? 1.410   28.481  12.454 1.00 55.14  ? 197 HIS   B ND1 1 
ATOM   3052 C CD2 . HIS   B 1 123 ? 1.736   30.475  11.622 1.00 51.78  ? 197 HIS   B CD2 1 
ATOM   3053 C CE1 . HIS   B 1 123 ? 1.605   28.335  11.154 1.00 53.69  ? 197 HIS   B CE1 1 
ATOM   3054 N NE2 . HIS   B 1 123 ? 1.803   29.530  10.625 1.00 55.76  ? 197 HIS   B NE2 1 
ATOM   3055 N N   . CYS   B 1 124 ? 4.313   30.760  14.803 1.00 48.57  ? 198 CYS   B N   1 
ATOM   3056 C CA  . CYS   B 1 124 ? 5.712   30.825  14.393 1.00 48.72  ? 198 CYS   B CA  1 
ATOM   3057 C C   . CYS   B 1 124 ? 6.579   29.953  15.279 1.00 49.26  ? 198 CYS   B C   1 
ATOM   3058 O O   . CYS   B 1 124 ? 7.420   29.189  14.790 1.00 52.66  ? 198 CYS   B O   1 
ATOM   3059 C CB  . CYS   B 1 124 ? 6.209   32.265  14.437 1.00 50.27  ? 198 CYS   B CB  1 
ATOM   3060 S SG  . CYS   B 1 124 ? 5.506   33.283  13.158 1.00 53.72  ? 198 CYS   B SG  1 
ATOM   3061 N N   . GLU   B 1 125 ? 6.374   30.047  16.592 1.00 47.75  ? 199 GLU   B N   1 
ATOM   3062 C CA  . GLU   B 1 125 ? 7.182   29.277  17.525 1.00 48.52  ? 199 GLU   B CA  1 
ATOM   3063 C C   . GLU   B 1 125 ? 7.056   27.778  17.275 1.00 50.49  ? 199 GLU   B C   1 
ATOM   3064 O O   . GLU   B 1 125 ? 8.028   27.037  17.456 1.00 56.25  ? 199 GLU   B O   1 
ATOM   3065 C CB  . GLU   B 1 125 ? 6.787   29.642  18.954 1.00 47.49  ? 199 GLU   B CB  1 
ATOM   3066 C CG  . GLU   B 1 125 ? 7.495   28.843  20.030 1.00 54.84  ? 199 GLU   B CG  1 
ATOM   3067 C CD  . GLU   B 1 125 ? 7.044   29.247  21.421 1.00 71.23  ? 199 GLU   B CD  1 
ATOM   3068 O OE1 . GLU   B 1 125 ? 6.333   30.274  21.538 1.00 70.54  ? 199 GLU   B OE1 1 
ATOM   3069 O OE2 . GLU   B 1 125 ? 7.392   28.537  22.391 1.00 64.81  ? 199 GLU   B OE2 1 
ATOM   3070 N N   . ALA   B 1 126 ? 5.884   27.310  16.839 1.00 50.35  ? 200 ALA   B N   1 
ATOM   3071 C CA  . ALA   B 1 126 ? 5.744   25.895  16.502 1.00 51.18  ? 200 ALA   B CA  1 
ATOM   3072 C C   . ALA   B 1 126 ? 6.228   25.575  15.093 1.00 55.40  ? 200 ALA   B C   1 
ATOM   3073 O O   . ALA   B 1 126 ? 6.573   24.422  14.818 1.00 56.45  ? 200 ALA   B O   1 
ATOM   3074 C CB  . ALA   B 1 126 ? 4.290   25.446  16.656 1.00 47.17  ? 200 ALA   B CB  1 
ATOM   3075 N N   . TRP   B 1 127 ? 6.244   26.555  14.187 1.00 52.75  ? 201 TRP   B N   1 
ATOM   3076 C CA  . TRP   B 1 127 ? 6.817   26.308  12.870 1.00 51.60  ? 201 TRP   B CA  1 
ATOM   3077 C C   . TRP   B 1 127 ? 8.327   26.144  12.960 1.00 55.31  ? 201 TRP   B C   1 
ATOM   3078 O O   . TRP   B 1 127 ? 8.918   25.378  12.185 1.00 53.51  ? 201 TRP   B O   1 
ATOM   3079 C CB  . TRP   B 1 127 ? 6.443   27.444  11.914 1.00 50.59  ? 201 TRP   B CB  1 
ATOM   3080 C CG  . TRP   B 1 127 ? 6.781   27.197  10.473 1.00 51.84  ? 201 TRP   B CG  1 
ATOM   3081 C CD1 . TRP   B 1 127 ? 7.740   27.833  9.743  1.00 54.83  ? 201 TRP   B CD1 1 
ATOM   3082 C CD2 . TRP   B 1 127 ? 6.156   26.257  9.582  1.00 51.78  ? 201 TRP   B CD2 1 
ATOM   3083 N NE1 . TRP   B 1 127 ? 7.757   27.348  8.454  1.00 53.95  ? 201 TRP   B NE1 1 
ATOM   3084 C CE2 . TRP   B 1 127 ? 6.794   26.382  8.329  1.00 53.35  ? 201 TRP   B CE2 1 
ATOM   3085 C CE3 . TRP   B 1 127 ? 5.123   25.325  9.721  1.00 51.66  ? 201 TRP   B CE3 1 
ATOM   3086 C CZ2 . TRP   B 1 127 ? 6.436   25.608  7.224  1.00 56.02  ? 201 TRP   B CZ2 1 
ATOM   3087 C CZ3 . TRP   B 1 127 ? 4.768   24.554  8.618  1.00 53.71  ? 201 TRP   B CZ3 1 
ATOM   3088 C CH2 . TRP   B 1 127 ? 5.425   24.701  7.389  1.00 56.26  ? 201 TRP   B CH2 1 
ATOM   3089 N N   . GLY   B 1 128 ? 8.959   26.833  13.910 1.00 52.18  ? 202 GLY   B N   1 
ATOM   3090 C CA  . GLY   B 1 128 ? 10.380  26.671  14.149 1.00 52.39  ? 202 GLY   B CA  1 
ATOM   3091 C C   . GLY   B 1 128 ? 11.271  27.108  13.013 1.00 52.61  ? 202 GLY   B C   1 
ATOM   3092 O O   . GLY   B 1 128 ? 12.404  26.633  12.908 1.00 57.33  ? 202 GLY   B O   1 
ATOM   3093 N N   . ALA   B 1 129 ? 10.796  27.996  12.154 1.00 49.89  ? 203 ALA   B N   1 
ATOM   3094 C CA  . ALA   B 1 129 ? 11.584  28.485  11.030 1.00 56.40  ? 203 ALA   B CA  1 
ATOM   3095 C C   . ALA   B 1 129 ? 10.892  29.729  10.496 1.00 53.24  ? 203 ALA   B C   1 
ATOM   3096 O O   . ALA   B 1 129 ? 9.851   30.154  11.006 1.00 49.43  ? 203 ALA   B O   1 
ATOM   3097 C CB  . ALA   B 1 129 ? 11.740  27.419  9.944  1.00 57.87  ? 203 ALA   B CB  1 
ATOM   3098 N N   . SER   B 1 130 ? 11.479  30.317  9.464  1.00 54.76  ? 204 SER   B N   1 
ATOM   3099 C CA  . SER   B 1 130 ? 10.801  31.406  8.788  1.00 53.37  ? 204 SER   B CA  1 
ATOM   3100 C C   . SER   B 1 130 ? 9.495   30.894  8.199  1.00 50.15  ? 204 SER   B C   1 
ATOM   3101 O O   . SER   B 1 130 ? 9.418   29.761  7.720  1.00 56.58  ? 204 SER   B O   1 
ATOM   3102 C CB  . SER   B 1 130 ? 11.699  31.982  7.698  1.00 57.69  ? 204 SER   B CB  1 
ATOM   3103 O OG  . SER   B 1 130 ? 13.005  32.201  8.205  1.00 60.77  ? 204 SER   B OG  1 
ATOM   3104 N N   . LEU   B 1 131 ? 8.455   31.714  8.270  1.00 53.32  ? 205 LEU   B N   1 
ATOM   3105 C CA  . LEU   B 1 131 ? 7.189   31.335  7.661  1.00 54.92  ? 205 LEU   B CA  1 
ATOM   3106 C C   . LEU   B 1 131 ? 7.329   31.324  6.142  1.00 58.81  ? 205 LEU   B C   1 
ATOM   3107 O O   . LEU   B 1 131 ? 8.020   32.179  5.579  1.00 61.53  ? 205 LEU   B O   1 
ATOM   3108 C CB  . LEU   B 1 131 ? 6.078   32.303  8.061  1.00 52.66  ? 205 LEU   B CB  1 
ATOM   3109 C CG  . LEU   B 1 131 ? 5.474   32.155  9.454  1.00 50.00  ? 205 LEU   B CG  1 
ATOM   3110 C CD1 . LEU   B 1 131 ? 4.230   33.011  9.552  1.00 52.56  ? 205 LEU   B CD1 1 
ATOM   3111 C CD2 . LEU   B 1 131 ? 5.142   30.706  9.723  1.00 50.89  ? 205 LEU   B CD2 1 
ATOM   3112 N N   . PRO   B 1 132 ? 6.709   30.367  5.453  1.00 54.45  ? 206 PRO   B N   1 
ATOM   3113 C CA  . PRO   B 1 132 ? 6.662   30.446  3.990  1.00 58.65  ? 206 PRO   B CA  1 
ATOM   3114 C C   . PRO   B 1 132 ? 5.998   31.744  3.562  1.00 60.10  ? 206 PRO   B C   1 
ATOM   3115 O O   . PRO   B 1 132 ? 5.032   32.203  4.178  1.00 60.87  ? 206 PRO   B O   1 
ATOM   3116 C CB  . PRO   B 1 132 ? 5.843   29.215  3.583  1.00 57.63  ? 206 PRO   B CB  1 
ATOM   3117 C CG  . PRO   B 1 132 ? 5.199   28.721  4.851  1.00 59.60  ? 206 PRO   B CG  1 
ATOM   3118 C CD  . PRO   B 1 132 ? 6.112   29.123  5.961  1.00 60.12  ? 206 PRO   B CD  1 
ATOM   3119 N N   . GLU   B 1 133 ? 6.553   32.353  2.512  1.00 57.62  ? 207 GLU   B N   1 
ATOM   3120 C CA  . GLU   B 1 133 ? 6.192   33.720  2.163  1.00 55.77  ? 207 GLU   B CA  1 
ATOM   3121 C C   . GLU   B 1 133 ? 4.754   33.839  1.679  1.00 59.35  ? 207 GLU   B C   1 
ATOM   3122 O O   . GLU   B 1 133 ? 4.198   34.943  1.690  1.00 62.85  ? 207 GLU   B O   1 
ATOM   3123 C CB  . GLU   B 1 133 ? 7.160   34.260  1.103  1.00 60.33  ? 207 GLU   B CB  1 
ATOM   3124 C CG  . GLU   B 1 133 ? 7.277   35.785  1.090  1.00 68.32  ? 207 GLU   B CG  1 
ATOM   3125 C CD  . GLU   B 1 133 ? 8.422   36.291  0.227  1.00 70.73  ? 207 GLU   B CD  1 
ATOM   3126 O OE1 . GLU   B 1 133 ? 9.527   35.710  0.292  1.00 74.18  ? 207 GLU   B OE1 1 
ATOM   3127 O OE2 . GLU   B 1 133 ? 8.214   37.273  -0.520 1.00 68.05  ? 207 GLU   B OE2 1 
ATOM   3128 N N   . ALA   B 1 134 ? 4.136   32.736  1.256  1.00 63.88  ? 208 ALA   B N   1 
ATOM   3129 C CA  . ALA   B 1 134 ? 2.723   32.785  0.899  1.00 60.05  ? 208 ALA   B CA  1 
ATOM   3130 C C   . ALA   B 1 134 ? 1.870   33.154  2.108  1.00 58.91  ? 208 ALA   B C   1 
ATOM   3131 O O   . ALA   B 1 134 ? 0.954   33.977  2.001  1.00 63.91  ? 208 ALA   B O   1 
ATOM   3132 C CB  . ALA   B 1 134 ? 2.285   31.446  0.306  1.00 56.37  ? 208 ALA   B CB  1 
ATOM   3133 N N   . GLN   B 1 135 ? 2.165   32.569  3.271  1.00 59.45  ? 209 GLN   B N   1 
ATOM   3134 C CA  . GLN   B 1 135 ? 1.411   32.912  4.473  1.00 58.51  ? 209 GLN   B CA  1 
ATOM   3135 C C   . GLN   B 1 135 ? 1.635   34.368  4.860  1.00 58.07  ? 209 GLN   B C   1 
ATOM   3136 O O   . GLN   B 1 135 ? 0.678   35.097  5.150  1.00 58.86  ? 209 GLN   B O   1 
ATOM   3137 C CB  . GLN   B 1 135 ? 1.806   31.994  5.630  1.00 56.73  ? 209 GLN   B CB  1 
ATOM   3138 C CG  . GLN   B 1 135 ? 1.642   30.514  5.363  1.00 60.61  ? 209 GLN   B CG  1 
ATOM   3139 C CD  . GLN   B 1 135 ? 1.766   29.693  6.632  1.00 62.72  ? 209 GLN   B CD  1 
ATOM   3140 O OE1 . GLN   B 1 135 ? 1.490   30.183  7.730  1.00 58.53  ? 209 GLN   B OE1 1 
ATOM   3141 N NE2 . GLN   B 1 135 ? 2.186   28.437  6.491  1.00 67.85  ? 209 GLN   B NE2 1 
ATOM   3142 N N   . VAL   B 1 136 ? 2.899   34.803  4.860  1.00 55.72  ? 210 VAL   B N   1 
ATOM   3143 C CA  . VAL   B 1 136 ? 3.256   36.160  5.269  1.00 53.67  ? 210 VAL   B CA  1 
ATOM   3144 C C   . VAL   B 1 136 ? 2.415   37.194  4.531  1.00 58.05  ? 210 VAL   B C   1 
ATOM   3145 O O   . VAL   B 1 136 ? 1.928   38.160  5.131  1.00 56.23  ? 210 VAL   B O   1 
ATOM   3146 C CB  . VAL   B 1 136 ? 4.765   36.395  5.050  1.00 57.22  ? 210 VAL   B CB  1 
ATOM   3147 C CG1 . VAL   B 1 136 ? 5.139   37.825  5.374  1.00 58.54  ? 210 VAL   B CG1 1 
ATOM   3148 C CG2 . VAL   B 1 136 ? 5.582   35.435  5.900  1.00 56.18  ? 210 VAL   B CG2 1 
ATOM   3149 N N   . TRP   B 1 137 ? 2.215   37.000  3.223  1.00 57.21  ? 211 TRP   B N   1 
ATOM   3150 C CA  . TRP   B 1 137 ? 1.442   37.962  2.439  1.00 56.32  ? 211 TRP   B CA  1 
ATOM   3151 C C   . TRP   B 1 137 ? -0.009  38.020  2.897  1.00 57.72  ? 211 TRP   B C   1 
ATOM   3152 O O   . TRP   B 1 137 ? -0.614  39.099  2.931  1.00 60.36  ? 211 TRP   B O   1 
ATOM   3153 C CB  . TRP   B 1 137 ? 1.505   37.613  0.951  1.00 60.54  ? 211 TRP   B CB  1 
ATOM   3154 C CG  . TRP   B 1 137 ? 2.778   38.017  0.268  1.00 61.70  ? 211 TRP   B CG  1 
ATOM   3155 C CD1 . TRP   B 1 137 ? 3.773   37.190  -0.164 1.00 63.69  ? 211 TRP   B CD1 1 
ATOM   3156 C CD2 . TRP   B 1 137 ? 3.189   39.348  -0.068 1.00 63.77  ? 211 TRP   B CD2 1 
ATOM   3157 N NE1 . TRP   B 1 137 ? 4.779   37.921  -0.747 1.00 61.80  ? 211 TRP   B NE1 1 
ATOM   3158 C CE2 . TRP   B 1 137 ? 4.444   39.249  -0.702 1.00 62.83  ? 211 TRP   B CE2 1 
ATOM   3159 C CE3 . TRP   B 1 137 ? 2.620   40.611  0.107  1.00 64.41  ? 211 TRP   B CE3 1 
ATOM   3160 C CZ2 . TRP   B 1 137 ? 5.138   40.365  -1.161 1.00 64.63  ? 211 TRP   B CZ2 1 
ATOM   3161 C CZ3 . TRP   B 1 137 ? 3.311   41.720  -0.351 1.00 67.69  ? 211 TRP   B CZ3 1 
ATOM   3162 C CH2 . TRP   B 1 137 ? 4.557   41.589  -0.976 1.00 70.20  ? 211 TRP   B CH2 1 
ATOM   3163 N N   . GLY   B 1 138 ? -0.595  36.869  3.228  1.00 55.55  ? 212 GLY   B N   1 
ATOM   3164 C CA  . GLY   B 1 138 ? -1.951  36.875  3.752  1.00 56.02  ? 212 GLY   B CA  1 
ATOM   3165 C C   . GLY   B 1 138 ? -2.052  37.618  5.071  1.00 57.26  ? 212 GLY   B C   1 
ATOM   3166 O O   . GLY   B 1 138 ? -2.911  38.486  5.247  1.00 62.73  ? 212 GLY   B O   1 
ATOM   3167 N N   . TYR   B 1 139 ? -1.162  37.295  6.011  1.00 59.28  ? 213 TYR   B N   1 
ATOM   3168 C CA  . TYR   B 1 139 ? -1.198  37.939  7.320  1.00 52.73  ? 213 TYR   B CA  1 
ATOM   3169 C C   . TYR   B 1 139 ? -0.887  39.423  7.221  1.00 56.59  ? 213 TYR   B C   1 
ATOM   3170 O O   . TYR   B 1 139 ? -1.447  40.226  7.978  1.00 57.15  ? 213 TYR   B O   1 
ATOM   3171 C CB  . TYR   B 1 139 ? -0.218  37.254  8.268  1.00 53.23  ? 213 TYR   B CB  1 
ATOM   3172 C CG  . TYR   B 1 139 ? -0.506  35.789  8.464  1.00 51.86  ? 213 TYR   B CG  1 
ATOM   3173 C CD1 . TYR   B 1 139 ? -1.799  35.296  8.327  1.00 55.42  ? 213 TYR   B CD1 1 
ATOM   3174 C CD2 . TYR   B 1 139 ? 0.509   34.896  8.778  1.00 47.62  ? 213 TYR   B CD2 1 
ATOM   3175 C CE1 . TYR   B 1 139 ? -2.073  33.955  8.501  1.00 57.13  ? 213 TYR   B CE1 1 
ATOM   3176 C CE2 . TYR   B 1 139 ? 0.244   33.551  8.954  1.00 50.64  ? 213 TYR   B CE2 1 
ATOM   3177 C CZ  . TYR   B 1 139 ? -1.050  33.089  8.815  1.00 53.41  ? 213 TYR   B CZ  1 
ATOM   3178 O OH  . TYR   B 1 139 ? -1.329  31.755  8.985  1.00 60.81  ? 213 TYR   B OH  1 
ATOM   3179 N N   . LEU   B 1 140 ? 0.003   39.809  6.304  1.00 56.55  ? 214 LEU   B N   1 
ATOM   3180 C CA  . LEU   B 1 140 ? 0.250   41.230  6.090  1.00 54.30  ? 214 LEU   B CA  1 
ATOM   3181 C C   . LEU   B 1 140 ? -0.989  41.917  5.536  1.00 57.52  ? 214 LEU   B C   1 
ATOM   3182 O O   . LEU   B 1 140 ? -1.345  43.014  5.977  1.00 61.76  ? 214 LEU   B O   1 
ATOM   3183 C CB  . LEU   B 1 140 ? 1.441   41.436  5.153  1.00 55.60  ? 214 LEU   B CB  1 
ATOM   3184 C CG  . LEU   B 1 140 ? 1.709   42.877  4.695  1.00 53.87  ? 214 LEU   B CG  1 
ATOM   3185 C CD1 . LEU   B 1 140 ? 1.995   43.783  5.874  1.00 49.24  ? 214 LEU   B CD1 1 
ATOM   3186 C CD2 . LEU   B 1 140 ? 2.853   42.931  3.698  1.00 53.12  ? 214 LEU   B CD2 1 
ATOM   3187 N N   . ARG   B 1 141 ? -1.670  41.283  4.580  1.00 61.37  ? 215 ARG   B N   1 
ATOM   3188 C CA  . ARG   B 1 141 ? -2.833  41.932  3.987  1.00 58.11  ? 215 ARG   B CA  1 
ATOM   3189 C C   . ARG   B 1 141 ? -3.970  42.051  4.991  1.00 53.42  ? 215 ARG   B C   1 
ATOM   3190 O O   . ARG   B 1 141 ? -4.655  43.078  5.040  1.00 59.22  ? 215 ARG   B O   1 
ATOM   3191 C CB  . ARG   B 1 141 ? -3.303  41.181  2.746  1.00 60.54  ? 215 ARG   B CB  1 
ATOM   3192 C CG  . ARG   B 1 141 ? -4.512  41.843  2.121  1.00 62.61  ? 215 ARG   B CG  1 
ATOM   3193 C CD  . ARG   B 1 141 ? -4.906  41.233  0.805  1.00 75.30  ? 215 ARG   B CD  1 
ATOM   3194 N NE  . ARG   B 1 141 ? -5.865  42.089  0.114  1.00 88.83  ? 215 ARG   B NE  1 
ATOM   3195 C CZ  . ARG   B 1 141 ? -7.179  42.047  0.295  1.00 91.60  ? 215 ARG   B CZ  1 
ATOM   3196 N NH1 . ARG   B 1 141 ? -7.734  41.183  1.133  1.00 92.72  ? 215 ARG   B NH1 1 
ATOM   3197 N NH2 . ARG   B 1 141 ? -7.955  42.889  -0.383 1.00 88.78  ? 215 ARG   B NH2 1 
ATOM   3198 N N   . ASP   B 1 142 ? -4.189  41.019  5.804  1.00 52.98  ? 216 ASP   B N   1 
ATOM   3199 C CA  . ASP   B 1 142 ? -5.304  41.085  6.741  1.00 57.87  ? 216 ASP   B CA  1 
ATOM   3200 C C   . ASP   B 1 142 ? -5.019  42.062  7.871  1.00 56.64  ? 216 ASP   B C   1 
ATOM   3201 O O   . ASP   B 1 142 ? -5.901  42.832  8.270  1.00 59.67  ? 216 ASP   B O   1 
ATOM   3202 C CB  . ASP   B 1 142 ? -5.630  39.697  7.285  1.00 56.82  ? 216 ASP   B CB  1 
ATOM   3203 C CG  . ASP   B 1 142 ? -6.772  39.032  6.522  1.00 71.39  ? 216 ASP   B CG  1 
ATOM   3204 O OD1 . ASP   B 1 142 ? -7.173  39.572  5.463  1.00 68.52  ? 216 ASP   B OD1 1 
ATOM   3205 O OD2 . ASP   B 1 142 ? -7.279  37.985  6.985  1.00 72.27  ? 216 ASP   B OD2 1 
ATOM   3206 N N   . THR   B 1 143 ? -3.795  42.060  8.396  1.00 57.10  ? 217 THR   B N   1 
ATOM   3207 C CA  . THR   B 1 143 ? -3.469  43.042  9.421  1.00 53.67  ? 217 THR   B CA  1 
ATOM   3208 C C   . THR   B 1 143 ? -3.466  44.453  8.849  1.00 54.65  ? 217 THR   B C   1 
ATOM   3209 O O   . THR   B 1 143 ? -3.817  45.406  9.554  1.00 55.90  ? 217 THR   B O   1 
ATOM   3210 C CB  . THR   B 1 143 ? -2.126  42.710  10.066 1.00 49.01  ? 217 THR   B CB  1 
ATOM   3211 O OG1 . THR   B 1 143 ? -2.098  41.317  10.406 1.00 51.09  ? 217 THR   B OG1 1 
ATOM   3212 C CG2 . THR   B 1 143 ? -1.938  43.524  11.332 1.00 48.70  ? 217 THR   B CG2 1 
ATOM   3213 N N   . LEU   B 1 144 ? -3.097  44.606  7.572  1.00 53.58  ? 218 LEU   B N   1 
ATOM   3214 C CA  . LEU   B 1 144 ? -3.195  45.916  6.932  1.00 55.08  ? 218 LEU   B CA  1 
ATOM   3215 C C   . LEU   B 1 144 ? -4.643  46.367  6.813  1.00 54.60  ? 218 LEU   B C   1 
ATOM   3216 O O   . LEU   B 1 144 ? -4.937  47.557  6.973  1.00 58.01  ? 218 LEU   B O   1 
ATOM   3217 C CB  . LEU   B 1 144 ? -2.532  45.893  5.554  1.00 54.62  ? 218 LEU   B CB  1 
ATOM   3218 C CG  . LEU   B 1 144 ? -1.024  46.149  5.528  1.00 51.98  ? 218 LEU   B CG  1 
ATOM   3219 C CD1 . LEU   B 1 144 ? -0.518  46.209  4.100  1.00 55.95  ? 218 LEU   B CD1 1 
ATOM   3220 C CD2 . LEU   B 1 144 ? -0.695  47.430  6.265  1.00 53.40  ? 218 LEU   B CD2 1 
ATOM   3221 N N   . LEU   B 1 145 ? -5.563  45.440  6.524  1.00 55.10  ? 219 LEU   B N   1 
ATOM   3222 C CA  . LEU   B 1 145 ? -6.977  45.801  6.485  1.00 53.03  ? 219 LEU   B CA  1 
ATOM   3223 C C   . LEU   B 1 145 ? -7.459  46.267  7.852  1.00 55.06  ? 219 LEU   B C   1 
ATOM   3224 O O   . LEU   B 1 145 ? -8.230  47.228  7.951  1.00 57.61  ? 219 LEU   B O   1 
ATOM   3225 C CB  . LEU   B 1 145 ? -7.819  44.622  6.007  1.00 55.27  ? 219 LEU   B CB  1 
ATOM   3226 C CG  . LEU   B 1 145 ? -7.661  44.208  4.553  1.00 59.19  ? 219 LEU   B CG  1 
ATOM   3227 C CD1 . LEU   B 1 145 ? -8.518  42.989  4.293  1.00 59.97  ? 219 LEU   B CD1 1 
ATOM   3228 C CD2 . LEU   B 1 145 ? -8.039  45.359  3.624  1.00 56.74  ? 219 LEU   B CD2 1 
ATOM   3229 N N   . ALA   B 1 146 ? -7.016  45.597  8.918  1.00 53.85  ? 220 ALA   B N   1 
ATOM   3230 C CA  . ALA   B 1 146 ? -7.385  46.025  10.263 1.00 52.56  ? 220 ALA   B CA  1 
ATOM   3231 C C   . ALA   B 1 146 ? -6.848  47.420  10.556 1.00 53.18  ? 220 ALA   B C   1 
ATOM   3232 O O   . ALA   B 1 146 ? -7.600  48.319  10.953 1.00 59.77  ? 220 ALA   B O   1 
ATOM   3233 C CB  . ALA   B 1 146 ? -6.873  45.018  11.294 1.00 48.55  ? 220 ALA   B CB  1 
ATOM   3234 N N   . LEU   B 1 147 ? -5.546  47.626  10.347 1.00 55.06  ? 221 LEU   B N   1 
ATOM   3235 C CA  . LEU   B 1 147 ? -4.958  48.937  10.608 1.00 51.13  ? 221 LEU   B CA  1 
ATOM   3236 C C   . LEU   B 1 147 ? -5.634  50.020  9.776  1.00 54.75  ? 221 LEU   B C   1 
ATOM   3237 O O   . LEU   B 1 147 ? -5.947  51.101  10.289 1.00 58.17  ? 221 LEU   B O   1 
ATOM   3238 C CB  . LEU   B 1 147 ? -3.455  48.899  10.336 1.00 48.26  ? 221 LEU   B CB  1 
ATOM   3239 C CG  . LEU   B 1 147 ? -2.645  48.011  11.273 1.00 46.61  ? 221 LEU   B CG  1 
ATOM   3240 C CD1 . LEU   B 1 147 ? -1.165  48.141  10.991 1.00 45.17  ? 221 LEU   B CD1 1 
ATOM   3241 C CD2 . LEU   B 1 147 ? -2.937  48.377  12.709 1.00 46.30  ? 221 LEU   B CD2 1 
ATOM   3242 N N   . ALA   B 1 148 ? -5.873  49.747  8.492  1.00 54.40  ? 222 ALA   B N   1 
ATOM   3243 C CA  . ALA   B 1 148 ? -6.568  50.720  7.656  1.00 53.19  ? 222 ALA   B CA  1 
ATOM   3244 C C   . ALA   B 1 148 ? -7.958  51.027  8.199  1.00 57.21  ? 222 ALA   B C   1 
ATOM   3245 O O   . ALA   B 1 148 ? -8.432  52.162  8.094  1.00 57.87  ? 222 ALA   B O   1 
ATOM   3246 C CB  . ALA   B 1 148 ? -6.653  50.210  6.218  1.00 53.05  ? 222 ALA   B CB  1 
ATOM   3247 N N   . HIS   B 1 149 ? -8.624  50.032  8.784  1.00 57.73  ? 223 HIS   B N   1 
ATOM   3248 C CA  . HIS   B 1 149 ? -9.913  50.282  9.418  1.00 60.05  ? 223 HIS   B CA  1 
ATOM   3249 C C   . HIS   B 1 149 ? -9.745  51.117  10.681 1.00 60.62  ? 223 HIS   B C   1 
ATOM   3250 O O   . HIS   B 1 149 ? -10.493 52.073  10.913 1.00 65.04  ? 223 HIS   B O   1 
ATOM   3251 C CB  . HIS   B 1 149 ? -10.601 48.955  9.738  1.00 61.24  ? 223 HIS   B CB  1 
ATOM   3252 C CG  . HIS   B 1 149 ? -11.863 49.110  10.523 1.00 60.98  ? 223 HIS   B CG  1 
ATOM   3253 N ND1 . HIS   B 1 149 ? -12.999 49.689  9.999  1.00 58.84  ? 223 HIS   B ND1 1 
ATOM   3254 C CD2 . HIS   B 1 149 ? -12.166 48.769  11.798 1.00 58.33  ? 223 HIS   B CD2 1 
ATOM   3255 C CE1 . HIS   B 1 149 ? -13.951 49.692  10.916 1.00 63.78  ? 223 HIS   B CE1 1 
ATOM   3256 N NE2 . HIS   B 1 149 ? -13.471 49.139  12.017 1.00 59.91  ? 223 HIS   B NE2 1 
ATOM   3257 N N   . LEU   B 1 150 ? -8.763  50.763  11.511 1.00 58.08  ? 224 LEU   B N   1 
ATOM   3258 C CA  . LEU   B 1 150 ? -8.496  51.534  12.722 1.00 58.19  ? 224 LEU   B CA  1 
ATOM   3259 C C   . LEU   B 1 150 ? -8.081  52.960  12.395 1.00 55.36  ? 224 LEU   B C   1 
ATOM   3260 O O   . LEU   B 1 150 ? -8.516  53.908  13.056 1.00 59.06  ? 224 LEU   B O   1 
ATOM   3261 C CB  . LEU   B 1 150 ? -7.404  50.852  13.543 1.00 55.65  ? 224 LEU   B CB  1 
ATOM   3262 C CG  . LEU   B 1 150 ? -7.765  49.858  14.640 1.00 51.37  ? 224 LEU   B CG  1 
ATOM   3263 C CD1 . LEU   B 1 150 ? -8.687  48.782  14.115 1.00 53.70  ? 224 LEU   B CD1 1 
ATOM   3264 C CD2 . LEU   B 1 150 ? -6.483  49.249  15.162 1.00 51.90  ? 224 LEU   B CD2 1 
ATOM   3265 N N   . HIS   B 1 151 ? -7.226  53.134  11.393 1.00 55.22  ? 225 HIS   B N   1 
ATOM   3266 C CA  . HIS   B 1 151 ? -6.700  54.461  11.111 1.00 53.56  ? 225 HIS   B CA  1 
ATOM   3267 C C   . HIS   B 1 151 ? -7.711  55.358  10.425 1.00 61.62  ? 225 HIS   B C   1 
ATOM   3268 O O   . HIS   B 1 151 ? -7.568  56.583  10.486 1.00 66.24  ? 225 HIS   B O   1 
ATOM   3269 C CB  . HIS   B 1 151 ? -5.437  54.353  10.261 1.00 54.84  ? 225 HIS   B CB  1 
ATOM   3270 C CG  . HIS   B 1 151 ? -4.330  53.611  10.934 1.00 53.09  ? 225 HIS   B CG  1 
ATOM   3271 N ND1 . HIS   B 1 151 ? -3.207  53.181  10.264 1.00 49.07  ? 225 HIS   B ND1 1 
ATOM   3272 C CD2 . HIS   B 1 151 ? -4.176  53.221  12.221 1.00 45.78  ? 225 HIS   B CD2 1 
ATOM   3273 C CE1 . HIS   B 1 151 ? -2.408  52.554  11.109 1.00 49.34  ? 225 HIS   B CE1 1 
ATOM   3274 N NE2 . HIS   B 1 151 ? -2.972  52.566  12.304 1.00 49.32  ? 225 HIS   B NE2 1 
ATOM   3275 N N   . SER   B 1 152 ? -8.726  54.787  9.773  1.00 63.18  ? 226 SER   B N   1 
ATOM   3276 C CA  . SER   B 1 152 ? -9.767  55.616  9.175  1.00 58.83  ? 226 SER   B CA  1 
ATOM   3277 C C   . SER   B 1 152 ? -10.620 56.310  10.222 1.00 55.70  ? 226 SER   B C   1 
ATOM   3278 O O   . SER   B 1 152 ? -11.346 57.248  9.886  1.00 69.29  ? 226 SER   B O   1 
ATOM   3279 C CB  . SER   B 1 152 ? -10.665 54.774  8.272  1.00 55.45  ? 226 SER   B CB  1 
ATOM   3280 O OG  . SER   B 1 152 ? -11.440 53.884  9.057  1.00 65.96  ? 226 SER   B OG  1 
ATOM   3281 N N   . GLN   B 1 153 ? -10.551 55.874  11.476 1.00 60.89  ? 227 GLN   B N   1 
ATOM   3282 C CA  . GLN   B 1 153 ? -11.311 56.468  12.565 1.00 59.76  ? 227 GLN   B CA  1 
ATOM   3283 C C   . GLN   B 1 153 ? -10.426 57.186  13.578 1.00 60.59  ? 227 GLN   B C   1 
ATOM   3284 O O   . GLN   B 1 153 ? -10.893 57.513  14.675 1.00 60.75  ? 227 GLN   B O   1 
ATOM   3285 C CB  . GLN   B 1 153 ? -12.129 55.385  13.263 1.00 63.17  ? 227 GLN   B CB  1 
ATOM   3286 C CG  . GLN   B 1 153 ? -12.903 54.516  12.304 1.00 65.00  ? 227 GLN   B CG  1 
ATOM   3287 C CD  . GLN   B 1 153 ? -13.697 53.460  13.023 1.00 70.34  ? 227 GLN   B CD  1 
ATOM   3288 O OE1 . GLN   B 1 153 ? -13.242 52.324  13.175 1.00 69.72  ? 227 GLN   B OE1 1 
ATOM   3289 N NE2 . GLN   B 1 153 ? -14.888 53.827  13.485 1.00 74.54  ? 227 GLN   B NE2 1 
ATOM   3290 N N   . GLY   B 1 154 ? -9.158  57.421  13.250 1.00 60.04  ? 228 GLY   B N   1 
ATOM   3291 C CA  . GLY   B 1 154 ? -8.282  58.133  14.159 1.00 56.40  ? 228 GLY   B CA  1 
ATOM   3292 C C   . GLY   B 1 154 ? -7.877  57.335  15.371 1.00 58.76  ? 228 GLY   B C   1 
ATOM   3293 O O   . GLY   B 1 154 ? -7.683  57.910  16.448 1.00 61.61  ? 228 GLY   B O   1 
ATOM   3294 N N   . LEU   B 1 155 ? -7.754  56.020  15.226 1.00 58.40  ? 229 LEU   B N   1 
ATOM   3295 C CA  . LEU   B 1 155 ? -7.310  55.131  16.290 1.00 55.12  ? 229 LEU   B CA  1 
ATOM   3296 C C   . LEU   B 1 155 ? -5.934  54.585  15.940 1.00 50.45  ? 229 LEU   B C   1 
ATOM   3297 O O   . LEU   B 1 155 ? -5.667  54.253  14.780 1.00 52.12  ? 229 LEU   B O   1 
ATOM   3298 C CB  . LEU   B 1 155 ? -8.296  53.971  16.489 1.00 50.74  ? 229 LEU   B CB  1 
ATOM   3299 C CG  . LEU   B 1 155 ? -9.776  54.381  16.493 1.00 56.55  ? 229 LEU   B CG  1 
ATOM   3300 C CD1 . LEU   B 1 155 ? -10.700 53.180  16.559 1.00 48.19  ? 229 LEU   B CD1 1 
ATOM   3301 C CD2 . LEU   B 1 155 ? -10.055 55.337  17.643 1.00 59.25  ? 229 LEU   B CD2 1 
ATOM   3302 N N   . VAL   B 1 156 ? -5.065  54.502  16.942 1.00 42.22  ? 230 VAL   B N   1 
ATOM   3303 C CA  . VAL   B 1 156 ? -3.723  53.952  16.796 1.00 43.96  ? 230 VAL   B CA  1 
ATOM   3304 C C   . VAL   B 1 156 ? -3.600  52.772  17.748 1.00 47.52  ? 230 VAL   B C   1 
ATOM   3305 O O   . VAL   B 1 156 ? -3.767  52.936  18.964 1.00 49.14  ? 230 VAL   B O   1 
ATOM   3306 C CB  . VAL   B 1 156 ? -2.645  55.007  17.089 1.00 47.32  ? 230 VAL   B CB  1 
ATOM   3307 C CG1 . VAL   B 1 156 ? -1.260  54.466  16.753 1.00 47.57  ? 230 VAL   B CG1 1 
ATOM   3308 C CG2 . VAL   B 1 156 ? -2.934  56.282  16.312 1.00 57.53  ? 230 VAL   B CG2 1 
ATOM   3309 N N   . HIS   B 1 157 ? -3.313  51.583  17.202 1.00 41.85  ? 231 HIS   B N   1 
ATOM   3310 C CA  . HIS   B 1 157 ? -3.248  50.385  18.035 1.00 43.07  ? 231 HIS   B CA  1 
ATOM   3311 C C   . HIS   B 1 157 ? -2.127  50.490  19.061 1.00 43.77  ? 231 HIS   B C   1 
ATOM   3312 O O   . HIS   B 1 157 ? -2.330  50.217  20.250 1.00 44.42  ? 231 HIS   B O   1 
ATOM   3313 C CB  . HIS   B 1 157 ? -3.064  49.143  17.162 1.00 42.89  ? 231 HIS   B CB  1 
ATOM   3314 C CG  . HIS   B 1 157 ? -3.255  47.852  17.897 1.00 41.70  ? 231 HIS   B CG  1 
ATOM   3315 N ND1 . HIS   B 1 157 ? -2.304  47.327  18.747 1.00 43.13  ? 231 HIS   B ND1 1 
ATOM   3316 C CD2 . HIS   B 1 157 ? -4.289  46.974  17.903 1.00 44.06  ? 231 HIS   B CD2 1 
ATOM   3317 C CE1 . HIS   B 1 157 ? -2.743  46.182  19.244 1.00 43.55  ? 231 HIS   B CE1 1 
ATOM   3318 N NE2 . HIS   B 1 157 ? -3.947  45.947  18.750 1.00 41.36  ? 231 HIS   B NE2 1 
ATOM   3319 N N   . LEU   B 1 158 ? -0.933  50.877  18.614 1.00 47.43  ? 232 LEU   B N   1 
ATOM   3320 C CA  . LEU   B 1 158 ? 0.260   51.051  19.439 1.00 44.34  ? 232 LEU   B CA  1 
ATOM   3321 C C   . LEU   B 1 158 ? 0.797   49.750  20.026 1.00 41.83  ? 232 LEU   B C   1 
ATOM   3322 O O   . LEU   B 1 158 ? 1.724   49.792  20.834 1.00 49.03  ? 232 LEU   B O   1 
ATOM   3323 C CB  . LEU   B 1 158 ? 0.024   52.051  20.579 1.00 44.90  ? 232 LEU   B CB  1 
ATOM   3324 C CG  . LEU   B 1 158 ? -0.095  53.541  20.232 1.00 45.68  ? 232 LEU   B CG  1 
ATOM   3325 C CD1 . LEU   B 1 158 ? -0.285  54.356  21.503 1.00 42.55  ? 232 LEU   B CD1 1 
ATOM   3326 C CD2 . LEU   B 1 158 ? 1.122   54.037  19.459 1.00 42.09  ? 232 LEU   B CD2 1 
ATOM   3327 N N   . ASP   B 1 159 ? 0.259   48.593  19.651 1.00 43.81  ? 233 ASP   B N   1 
ATOM   3328 C CA  . ASP   B 1 159 ? 0.776   47.328  20.178 1.00 46.28  ? 233 ASP   B CA  1 
ATOM   3329 C C   . ASP   B 1 159 ? 0.629   46.240  19.119 1.00 46.85  ? 233 ASP   B C   1 
ATOM   3330 O O   . ASP   B 1 159 ? 0.183   45.122  19.398 1.00 44.58  ? 233 ASP   B O   1 
ATOM   3331 C CB  . ASP   B 1 159 ? 0.068   46.938  21.477 1.00 43.70  ? 233 ASP   B CB  1 
ATOM   3332 C CG  . ASP   B 1 159 ? 0.915   46.031  22.363 1.00 50.32  ? 233 ASP   B CG  1 
ATOM   3333 O OD1 . ASP   B 1 159 ? 2.162   46.093  22.288 1.00 52.38  ? 233 ASP   B OD1 1 
ATOM   3334 O OD2 . ASP   B 1 159 ? 0.330   45.249  23.144 1.00 57.61  ? 233 ASP   B OD2 1 
ATOM   3335 N N   . VAL   B 1 160 ? 0.999   46.565  17.883 1.00 42.84  ? 234 VAL   B N   1 
ATOM   3336 C CA  . VAL   B 1 160 ? 0.998   45.586  16.802 1.00 40.20  ? 234 VAL   B CA  1 
ATOM   3337 C C   . VAL   B 1 160 ? 2.241   44.713  16.941 1.00 44.65  ? 234 VAL   B C   1 
ATOM   3338 O O   . VAL   B 1 160 ? 3.371   45.216  16.960 1.00 47.14  ? 234 VAL   B O   1 
ATOM   3339 C CB  . VAL   B 1 160 ? 0.947   46.273  15.433 1.00 41.95  ? 234 VAL   B CB  1 
ATOM   3340 C CG1 . VAL   B 1 160 ? 0.902   45.242  14.330 1.00 40.49  ? 234 VAL   B CG1 1 
ATOM   3341 C CG2 . VAL   B 1 160 ? -0.269  47.181  15.349 1.00 44.00  ? 234 VAL   B CG2 1 
ATOM   3342 N N   . LYS   B 1 161 ? 2.034   43.409  17.054 1.00 43.28  ? 235 LYS   B N   1 
ATOM   3343 C CA  . LYS   B 1 161 ? 3.105   42.443  17.251 1.00 41.11  ? 235 LYS   B CA  1 
ATOM   3344 C C   . LYS   B 1 161 ? 2.503   41.046  17.141 1.00 44.56  ? 235 LYS   B C   1 
ATOM   3345 O O   . LYS   B 1 161 ? 1.278   40.895  17.210 1.00 47.09  ? 235 LYS   B O   1 
ATOM   3346 C CB  . LYS   B 1 161 ? 3.796   42.636  18.610 1.00 43.20  ? 235 LYS   B CB  1 
ATOM   3347 C CG  . LYS   B 1 161 ? 2.910   42.477  19.820 1.00 42.53  ? 235 LYS   B CG  1 
ATOM   3348 C CD  . LYS   B 1 161 ? 3.784   42.482  21.057 1.00 46.65  ? 235 LYS   B CD  1 
ATOM   3349 C CE  . LYS   B 1 161 ? 3.000   42.698  22.329 1.00 52.12  ? 235 LYS   B CE  1 
ATOM   3350 N NZ  . LYS   B 1 161 ? 3.955   42.796  23.474 1.00 58.59  ? 235 LYS   B NZ  1 
ATOM   3351 N N   . PRO   B 1 162 ? 3.332   40.020  16.946 1.00 43.66  ? 236 PRO   B N   1 
ATOM   3352 C CA  . PRO   B 1 162 ? 2.768   38.686  16.688 1.00 40.57  ? 236 PRO   B CA  1 
ATOM   3353 C C   . PRO   B 1 162 ? 1.904   38.159  17.815 1.00 42.31  ? 236 PRO   B C   1 
ATOM   3354 O O   . PRO   B 1 162 ? 1.007   37.349  17.557 1.00 46.68  ? 236 PRO   B O   1 
ATOM   3355 C CB  . PRO   B 1 162 ? 4.015   37.818  16.478 1.00 42.28  ? 236 PRO   B CB  1 
ATOM   3356 C CG  . PRO   B 1 162 ? 5.051   38.773  15.990 1.00 44.23  ? 236 PRO   B CG  1 
ATOM   3357 C CD  . PRO   B 1 162 ? 4.794   40.040  16.756 1.00 44.12  ? 236 PRO   B CD  1 
ATOM   3358 N N   . ALA   B 1 163 ? 2.142   38.588  19.056 1.00 41.78  ? 237 ALA   B N   1 
ATOM   3359 C CA  . ALA   B 1 163 ? 1.329   38.139  20.181 1.00 37.64  ? 237 ALA   B CA  1 
ATOM   3360 C C   . ALA   B 1 163 ? -0.098  38.674  20.129 1.00 44.89  ? 237 ALA   B C   1 
ATOM   3361 O O   . ALA   B 1 163 ? -0.984  38.104  20.775 1.00 48.25  ? 237 ALA   B O   1 
ATOM   3362 C CB  . ALA   B 1 163 ? 1.979   38.564  21.496 1.00 40.05  ? 237 ALA   B CB  1 
ATOM   3363 N N   . ASN   B 1 164 ? -0.337  39.755  19.384 1.00 44.97  ? 238 ASN   B N   1 
ATOM   3364 C CA  . ASN   B 1 164 ? -1.641  40.404  19.304 1.00 44.09  ? 238 ASN   B CA  1 
ATOM   3365 C C   . ASN   B 1 164 ? -2.309  40.198  17.952 1.00 47.82  ? 238 ASN   B C   1 
ATOM   3366 O O   . ASN   B 1 164 ? -3.251  40.920  17.607 1.00 49.86  ? 238 ASN   B O   1 
ATOM   3367 C CB  . ASN   B 1 164 ? -1.500  41.892  19.602 1.00 42.35  ? 238 ASN   B CB  1 
ATOM   3368 C CG  . ASN   B 1 164 ? -0.978  42.143  20.989 1.00 44.73  ? 238 ASN   B CG  1 
ATOM   3369 O OD1 . ASN   B 1 164 ? -1.144  41.306  21.881 1.00 46.71  ? 238 ASN   B OD1 1 
ATOM   3370 N ND2 . ASN   B 1 164 ? -0.338  43.289  21.188 1.00 45.75  ? 238 ASN   B ND2 1 
ATOM   3371 N N   . ILE   B 1 165 ? -1.828  39.235  17.176 1.00 44.80  ? 239 ILE   B N   1 
ATOM   3372 C CA  . ILE   B 1 165 ? -2.434  38.843  15.915 1.00 43.76  ? 239 ILE   B CA  1 
ATOM   3373 C C   . ILE   B 1 165 ? -2.841  37.388  16.050 1.00 47.78  ? 239 ILE   B C   1 
ATOM   3374 O O   . ILE   B 1 165 ? -2.039  36.558  16.493 1.00 46.41  ? 239 ILE   B O   1 
ATOM   3375 C CB  . ILE   B 1 165 ? -1.463  39.041  14.744 1.00 43.37  ? 239 ILE   B CB  1 
ATOM   3376 C CG1 . ILE   B 1 165 ? -1.135  40.527  14.605 1.00 41.24  ? 239 ILE   B CG1 1 
ATOM   3377 C CG2 . ILE   B 1 165 ? -2.041  38.457  13.462 1.00 40.84  ? 239 ILE   B CG2 1 
ATOM   3378 C CD1 . ILE   B 1 165 ? -0.018  40.806  13.640 1.00 43.81  ? 239 ILE   B CD1 1 
ATOM   3379 N N   . PHE   B 1 166 ? -4.085  37.080  15.695 1.00 45.50  ? 240 PHE   B N   1 
ATOM   3380 C CA  . PHE   B 1 166 ? -4.654  35.766  15.965 1.00 47.71  ? 240 PHE   B CA  1 
ATOM   3381 C C   . PHE   B 1 166 ? -5.158  35.142  14.675 1.00 51.33  ? 240 PHE   B C   1 
ATOM   3382 O O   . PHE   B 1 166 ? -5.904  35.774  13.920 1.00 55.57  ? 240 PHE   B O   1 
ATOM   3383 C CB  . PHE   B 1 166 ? -5.769  35.872  16.997 1.00 46.08  ? 240 PHE   B CB  1 
ATOM   3384 C CG  . PHE   B 1 166 ? -5.319  36.476  18.292 1.00 45.71  ? 240 PHE   B CG  1 
ATOM   3385 C CD1 . PHE   B 1 166 ? -4.791  35.682  19.295 1.00 47.76  ? 240 PHE   B CD1 1 
ATOM   3386 C CD2 . PHE   B 1 166 ? -5.409  37.837  18.503 1.00 47.94  ? 240 PHE   B CD2 1 
ATOM   3387 C CE1 . PHE   B 1 166 ? -4.375  36.239  20.495 1.00 47.75  ? 240 PHE   B CE1 1 
ATOM   3388 C CE2 . PHE   B 1 166 ? -4.992  38.401  19.699 1.00 44.26  ? 240 PHE   B CE2 1 
ATOM   3389 C CZ  . PHE   B 1 166 ? -4.477  37.602  20.694 1.00 44.55  ? 240 PHE   B CZ  1 
ATOM   3390 N N   . LEU   B 1 167 ? -4.759  33.901  14.434 1.00 50.90  ? 241 LEU   B N   1 
ATOM   3391 C CA  . LEU   B 1 167 ? -4.972  33.282  13.139 1.00 52.25  ? 241 LEU   B CA  1 
ATOM   3392 C C   . LEU   B 1 167 ? -6.382  32.726  13.015 1.00 54.48  ? 241 LEU   B C   1 
ATOM   3393 O O   . LEU   B 1 167 ? -6.959  32.223  13.982 1.00 52.20  ? 241 LEU   B O   1 
ATOM   3394 C CB  . LEU   B 1 167 ? -3.954  32.169  12.917 1.00 50.60  ? 241 LEU   B CB  1 
ATOM   3395 C CG  . LEU   B 1 167 ? -2.508  32.562  13.213 1.00 51.59  ? 241 LEU   B CG  1 
ATOM   3396 C CD1 . LEU   B 1 167 ? -1.596  31.478  12.701 1.00 53.00  ? 241 LEU   B CD1 1 
ATOM   3397 C CD2 . LEU   B 1 167 ? -2.149  33.909  12.587 1.00 49.31  ? 241 LEU   B CD2 1 
ATOM   3398 N N   . GLY   B 1 168 ? -6.934  32.827  11.812 1.00 57.44  ? 242 GLY   B N   1 
ATOM   3399 C CA  . GLY   B 1 168 ? -8.210  32.235  11.501 1.00 60.87  ? 242 GLY   B CA  1 
ATOM   3400 C C   . GLY   B 1 168 ? -8.061  31.190  10.416 1.00 63.29  ? 242 GLY   B C   1 
ATOM   3401 O O   . GLY   B 1 168 ? -6.960  30.938  9.913  1.00 65.31  ? 242 GLY   B O   1 
ATOM   3402 N N   . PRO   B 1 169 ? -9.164  30.553  10.036 1.00 62.84  ? 243 PRO   B N   1 
ATOM   3403 C CA  . PRO   B 1 169 ? -9.092  29.541  8.980  1.00 60.16  ? 243 PRO   B CA  1 
ATOM   3404 C C   . PRO   B 1 169 ? -8.774  30.170  7.633  1.00 60.73  ? 243 PRO   B C   1 
ATOM   3405 O O   . PRO   B 1 169 ? -8.918  31.376  7.423  1.00 65.37  ? 243 PRO   B O   1 
ATOM   3406 C CB  . PRO   B 1 169 ? -10.490 28.912  8.990  1.00 60.68  ? 243 PRO   B CB  1 
ATOM   3407 C CG  . PRO   B 1 169 ? -11.372 29.940  9.629  1.00 56.63  ? 243 PRO   B CG  1 
ATOM   3408 C CD  . PRO   B 1 169 ? -10.516 30.676  10.609 1.00 59.51  ? 243 PRO   B CD  1 
ATOM   3409 N N   . ARG   B 1 170 ? -8.318  29.319  6.714  1.00 62.73  ? 244 ARG   B N   1 
ATOM   3410 C CA  . ARG   B 1 170 ? -8.048  29.709  5.331  1.00 62.61  ? 244 ARG   B CA  1 
ATOM   3411 C C   . ARG   B 1 170 ? -6.987  30.799  5.238  1.00 62.81  ? 244 ARG   B C   1 
ATOM   3412 O O   . ARG   B 1 170 ? -7.031  31.641  4.339  1.00 66.53  ? 244 ARG   B O   1 
ATOM   3413 C CB  . ARG   B 1 170 ? -9.330  30.151  4.621  1.00 65.82  ? 244 ARG   B CB  1 
ATOM   3414 C CG  . ARG   B 1 170 ? -10.325 29.028  4.381  1.00 72.49  ? 244 ARG   B CG  1 
ATOM   3415 C CD  . ARG   B 1 170 ? -11.596 29.563  3.751  1.00 74.21  ? 244 ARG   B CD  1 
ATOM   3416 N NE  . ARG   B 1 170 ? -12.391 28.502  3.144  1.00 90.70  ? 244 ARG   B NE  1 
ATOM   3417 C CZ  . ARG   B 1 170 ? -13.493 28.703  2.433  1.00 92.47  ? 244 ARG   B CZ  1 
ATOM   3418 N NH1 . ARG   B 1 170 ? -13.968 29.922  2.221  1.00 91.62  ? 244 ARG   B NH1 1 
ATOM   3419 N NH2 . ARG   B 1 170 ? -14.134 27.656  1.920  1.00 85.10  ? 244 ARG   B NH2 1 
ATOM   3420 N N   . GLY   B 1 171 ? -6.030  30.797  6.164  1.00 61.89  ? 245 GLY   B N   1 
ATOM   3421 C CA  . GLY   B 1 171 ? -4.924  31.732  6.114  1.00 58.96  ? 245 GLY   B CA  1 
ATOM   3422 C C   . GLY   B 1 171 ? -5.236  33.152  6.541  1.00 63.29  ? 245 GLY   B C   1 
ATOM   3423 O O   . GLY   B 1 171 ? -4.349  34.016  6.450  1.00 58.61  ? 245 GLY   B O   1 
ATOM   3424 N N   . ARG   B 1 172 ? -6.457  33.430  6.996  1.00 63.65  ? 246 ARG   B N   1 
ATOM   3425 C CA  . ARG   B 1 172 ? -6.801  34.743  7.521  1.00 61.98  ? 246 ARG   B CA  1 
ATOM   3426 C C   . ARG   B 1 172 ? -6.216  34.933  8.921  1.00 57.03  ? 246 ARG   B C   1 
ATOM   3427 O O   . ARG   B 1 172 ? -5.786  33.983  9.581  1.00 56.86  ? 246 ARG   B O   1 
ATOM   3428 C CB  . ARG   B 1 172 ? -8.319  34.925  7.567  1.00 65.64  ? 246 ARG   B CB  1 
ATOM   3429 C CG  . ARG   B 1 172 ? -9.050  34.513  6.304  1.00 66.94  ? 246 ARG   B CG  1 
ATOM   3430 C CD  . ARG   B 1 172 ? -8.495  35.227  5.084  1.00 70.50  ? 246 ARG   B CD  1 
ATOM   3431 N NE  . ARG   B 1 172 ? -8.547  36.680  5.203  1.00 71.56  ? 246 ARG   B NE  1 
ATOM   3432 C CZ  . ARG   B 1 172 ? -9.610  37.419  4.911  1.00 73.12  ? 246 ARG   B CZ  1 
ATOM   3433 N NH1 . ARG   B 1 172 ? -10.760 36.869  4.557  1.00 71.46  ? 246 ARG   B NH1 1 
ATOM   3434 N NH2 . ARG   B 1 172 ? -9.514  38.745  4.970  1.00 71.19  ? 246 ARG   B NH2 1 
ATOM   3435 N N   . CYS   B 1 173 ? -6.209  36.184  9.379  1.00 57.84  ? 247 CYS   B N   1 
ATOM   3436 C CA  . CYS   B 1 173 ? -5.820  36.497  10.748 1.00 54.76  ? 247 CYS   B CA  1 
ATOM   3437 C C   . CYS   B 1 173 ? -6.497  37.794  11.162 1.00 51.08  ? 247 CYS   B C   1 
ATOM   3438 O O   . CYS   B 1 173 ? -6.985  38.554  10.322 1.00 53.32  ? 247 CYS   B O   1 
ATOM   3439 C CB  . CYS   B 1 173 ? -4.301  36.613  10.908 1.00 54.04  ? 247 CYS   B CB  1 
ATOM   3440 S SG  . CYS   B 1 173 ? -3.578  38.073  10.134 1.00 58.00  ? 247 CYS   B SG  1 
ATOM   3441 N N   . LYS   B 1 174 ? -6.516  38.043  12.472 1.00 53.06  ? 248 LYS   B N   1 
ATOM   3442 C CA  . LYS   B 1 174 ? -7.215  39.187  13.043 1.00 48.00  ? 248 LYS   B CA  1 
ATOM   3443 C C   . LYS   B 1 174 ? -6.311  39.918  14.019 1.00 46.38  ? 248 LYS   B C   1 
ATOM   3444 O O   . LYS   B 1 174 ? -5.523  39.295  14.735 1.00 51.89  ? 248 LYS   B O   1 
ATOM   3445 C CB  . LYS   B 1 174 ? -8.500  38.758  13.762 1.00 48.97  ? 248 LYS   B CB  1 
ATOM   3446 C CG  . LYS   B 1 174 ? -9.471  37.997  12.880 1.00 52.60  ? 248 LYS   B CG  1 
ATOM   3447 C CD  . LYS   B 1 174 ? -10.819 37.820  13.549 1.00 52.21  ? 248 LYS   B CD  1 
ATOM   3448 C CE  . LYS   B 1 174 ? -11.688 36.859  12.764 1.00 57.53  ? 248 LYS   B CE  1 
ATOM   3449 N NZ  . LYS   B 1 174 ? -13.083 36.810  13.280 1.00 67.21  ? 248 LYS   B NZ  1 
ATOM   3450 N N   . LEU   B 1 175 ? -6.431  41.243  14.043 1.00 47.12  ? 249 LEU   B N   1 
ATOM   3451 C CA  . LEU   B 1 175 ? -5.724  42.067  15.013 1.00 44.76  ? 249 LEU   B CA  1 
ATOM   3452 C C   . LEU   B 1 175 ? -6.538  42.141  16.298 1.00 45.53  ? 249 LEU   B C   1 
ATOM   3453 O O   . LEU   B 1 175 ? -7.757  42.323  16.266 1.00 50.81  ? 249 LEU   B O   1 
ATOM   3454 C CB  . LEU   B 1 175 ? -5.480  43.469  14.456 1.00 44.49  ? 249 LEU   B CB  1 
ATOM   3455 C CG  . LEU   B 1 175 ? -4.640  44.434  15.297 1.00 47.33  ? 249 LEU   B CG  1 
ATOM   3456 C CD1 . LEU   B 1 175 ? -3.240  43.886  15.579 1.00 40.53  ? 249 LEU   B CD1 1 
ATOM   3457 C CD2 . LEU   B 1 175 ? -4.563  45.772  14.591 1.00 51.76  ? 249 LEU   B CD2 1 
ATOM   3458 N N   . GLY   B 1 176 ? -5.861  41.982  17.431 1.00 43.54  ? 250 GLY   B N   1 
ATOM   3459 C CA  . GLY   B 1 176 ? -6.555  41.992  18.702 1.00 43.82  ? 250 GLY   B CA  1 
ATOM   3460 C C   . GLY   B 1 176 ? -5.811  42.752  19.778 1.00 45.59  ? 250 GLY   B C   1 
ATOM   3461 O O   . GLY   B 1 176 ? -4.905  43.535  19.478 1.00 44.42  ? 250 GLY   B O   1 
ATOM   3462 N N   . ASP   B 1 177 ? -6.190  42.512  21.037 1.00 49.40  ? 251 ASP   B N   1 
ATOM   3463 C CA  . ASP   B 1 177 ? -5.583  43.143  22.205 1.00 49.12  ? 251 ASP   B CA  1 
ATOM   3464 C C   . ASP   B 1 177 ? -5.539  44.653  22.021 1.00 46.13  ? 251 ASP   B C   1 
ATOM   3465 O O   . ASP   B 1 177 ? -4.507  45.219  21.642 1.00 41.57  ? 251 ASP   B O   1 
ATOM   3466 C CB  . ASP   B 1 177 ? -4.180  42.579  22.468 1.00 47.67  ? 251 ASP   B CB  1 
ATOM   3467 C CG  . ASP   B 1 177 ? -3.665  42.907  23.872 1.00 57.57  ? 251 ASP   B CG  1 
ATOM   3468 O OD1 . ASP   B 1 177 ? -4.321  43.704  24.584 1.00 60.72  ? 251 ASP   B OD1 1 
ATOM   3469 O OD2 . ASP   B 1 177 ? -2.605  42.364  24.265 1.00 64.12  ? 251 ASP   B OD2 1 
ATOM   3470 N N   . PHE   B 1 178 ? -6.672  45.309  22.264 1.00 47.93  ? 252 PHE   B N   1 
ATOM   3471 C CA  . PHE   B 1 178 ? -6.791  46.750  22.100 1.00 46.24  ? 252 PHE   B CA  1 
ATOM   3472 C C   . PHE   B 1 178 ? -6.582  47.496  23.414 1.00 43.99  ? 252 PHE   B C   1 
ATOM   3473 O O   . PHE   B 1 178 ? -7.179  48.552  23.636 1.00 47.23  ? 252 PHE   B O   1 
ATOM   3474 C CB  . PHE   B 1 178 ? -8.152  47.090  21.492 1.00 44.88  ? 252 PHE   B CB  1 
ATOM   3475 C CG  . PHE   B 1 178 ? -8.378  46.487  20.125 1.00 46.53  ? 252 PHE   B CG  1 
ATOM   3476 C CD1 . PHE   B 1 178 ? -7.511  46.763  19.077 1.00 46.67  ? 252 PHE   B CD1 1 
ATOM   3477 C CD2 . PHE   B 1 178 ? -9.470  45.668  19.883 1.00 50.78  ? 252 PHE   B CD2 1 
ATOM   3478 C CE1 . PHE   B 1 178 ? -7.723  46.219  17.817 1.00 48.05  ? 252 PHE   B CE1 1 
ATOM   3479 C CE2 . PHE   B 1 178 ? -9.687  45.122  18.626 1.00 49.04  ? 252 PHE   B CE2 1 
ATOM   3480 C CZ  . PHE   B 1 178 ? -8.813  45.399  17.593 1.00 47.53  ? 252 PHE   B CZ  1 
ATOM   3481 N N   . GLY   B 1 179 ? -5.749  46.955  24.302 1.00 48.91  ? 253 GLY   B N   1 
ATOM   3482 C CA  . GLY   B 1 179 ? -5.557  47.592  25.595 1.00 44.81  ? 253 GLY   B CA  1 
ATOM   3483 C C   . GLY   B 1 179 ? -4.787  48.896  25.501 1.00 43.43  ? 253 GLY   B C   1 
ATOM   3484 O O   . GLY   B 1 179 ? -5.063  49.835  26.248 1.00 50.64  ? 253 GLY   B O   1 
ATOM   3485 N N   . LEU   B 1 180 ? -3.812  48.975  24.591 1.00 42.75  ? 254 LEU   B N   1 
ATOM   3486 C CA  . LEU   B 1 180 ? -3.014  50.183  24.424 1.00 43.04  ? 254 LEU   B CA  1 
ATOM   3487 C C   . LEU   B 1 180 ? -3.628  51.182  23.449 1.00 46.01  ? 254 LEU   B C   1 
ATOM   3488 O O   . LEU   B 1 180 ? -3.034  52.238  23.214 1.00 47.38  ? 254 LEU   B O   1 
ATOM   3489 C CB  . LEU   B 1 180 ? -1.594  49.834  23.951 1.00 44.09  ? 254 LEU   B CB  1 
ATOM   3490 C CG  . LEU   B 1 180 ? -0.617  49.114  24.891 1.00 51.87  ? 254 LEU   B CG  1 
ATOM   3491 C CD1 . LEU   B 1 180 ? 0.802   49.105  24.325 1.00 55.58  ? 254 LEU   B CD1 1 
ATOM   3492 C CD2 . LEU   B 1 180 ? -0.618  49.741  26.258 1.00 50.40  ? 254 LEU   B CD2 1 
ATOM   3493 N N   . LEU   B 1 181 ? -4.795  50.890  22.882 1.00 47.54  ? 255 LEU   B N   1 
ATOM   3494 C CA  . LEU   B 1 181 ? -5.316  51.725  21.810 1.00 49.31  ? 255 LEU   B CA  1 
ATOM   3495 C C   . LEU   B 1 181 ? -5.642  53.125  22.322 1.00 52.24  ? 255 LEU   B C   1 
ATOM   3496 O O   . LEU   B 1 181 ? -6.177  53.295  23.422 1.00 49.67  ? 255 LEU   B O   1 
ATOM   3497 C CB  . LEU   B 1 181 ? -6.556  51.075  21.193 1.00 43.66  ? 255 LEU   B CB  1 
ATOM   3498 C CG  . LEU   B 1 181 ? -7.109  51.761  19.943 1.00 45.64  ? 255 LEU   B CG  1 
ATOM   3499 C CD1 . LEU   B 1 181 ? -7.497  50.734  18.887 1.00 44.63  ? 255 LEU   B CD1 1 
ATOM   3500 C CD2 . LEU   B 1 181 ? -8.294  52.645  20.302 1.00 46.71  ? 255 LEU   B CD2 1 
ATOM   3501 N N   . VAL   B 1 182 ? -5.293  54.137  21.522 1.00 49.93  ? 256 VAL   B N   1 
ATOM   3502 C CA  . VAL   B 1 182 ? -5.643  55.521  21.815 1.00 51.66  ? 256 VAL   B CA  1 
ATOM   3503 C C   . VAL   B 1 182 ? -6.387  56.103  20.623 1.00 54.77  ? 256 VAL   B C   1 
ATOM   3504 O O   . VAL   B 1 182 ? -6.181  55.696  19.475 1.00 55.43  ? 256 VAL   B O   1 
ATOM   3505 C CB  . VAL   B 1 182 ? -4.412  56.404  22.145 1.00 52.46  ? 256 VAL   B CB  1 
ATOM   3506 C CG1 . VAL   B 1 182 ? -3.629  55.831  23.312 1.00 59.96  ? 256 VAL   B CG1 1 
ATOM   3507 C CG2 . VAL   B 1 182 ? -3.529  56.589  20.919 1.00 51.44  ? 256 VAL   B CG2 1 
ATOM   3508 N N   . GLU   B 1 183 ? -7.253  57.072  20.904 1.00 56.16  ? 257 GLU   B N   1 
ATOM   3509 C CA  . GLU   B 1 183 ? -7.917  57.854  19.873 1.00 58.60  ? 257 GLU   B CA  1 
ATOM   3510 C C   . GLU   B 1 183 ? -7.227  59.208  19.761 1.00 62.27  ? 257 GLU   B C   1 
ATOM   3511 O O   . GLU   B 1 183 ? -6.961  59.858  20.777 1.00 66.23  ? 257 GLU   B O   1 
ATOM   3512 C CB  . GLU   B 1 183 ? -9.399  58.037  20.195 1.00 59.07  ? 257 GLU   B CB  1 
ATOM   3513 C CG  . GLU   B 1 183 ? -10.161 58.766  19.104 1.00 67.59  ? 257 GLU   B CG  1 
ATOM   3514 C CD  . GLU   B 1 183 ? -11.605 59.028  19.471 1.00 76.84  ? 257 GLU   B CD  1 
ATOM   3515 O OE1 . GLU   B 1 183 ? -12.004 58.680  20.603 1.00 82.92  ? 257 GLU   B OE1 1 
ATOM   3516 O OE2 . GLU   B 1 183 ? -12.341 59.584  18.626 1.00 85.15  ? 257 GLU   B OE2 1 
ATOM   3517 N N   . LEU   B 1 184 ? -6.930  59.626  18.533 1.00 61.96  ? 258 LEU   B N   1 
ATOM   3518 C CA  . LEU   B 1 184 ? -6.285  60.916  18.305 1.00 69.27  ? 258 LEU   B CA  1 
ATOM   3519 C C   . LEU   B 1 184 ? -7.340  62.016  18.369 1.00 77.82  ? 258 LEU   B C   1 
ATOM   3520 O O   . LEU   B 1 184 ? -8.186  62.126  17.478 1.00 81.65  ? 258 LEU   B O   1 
ATOM   3521 C CB  . LEU   B 1 184 ? -5.563  60.917  16.964 1.00 66.54  ? 258 LEU   B CB  1 
ATOM   3522 C CG  . LEU   B 1 184 ? -4.608  59.743  16.745 1.00 63.72  ? 258 LEU   B CG  1 
ATOM   3523 C CD1 . LEU   B 1 184 ? -3.963  59.832  15.370 1.00 58.11  ? 258 LEU   B CD1 1 
ATOM   3524 C CD2 . LEU   B 1 184 ? -3.553  59.704  17.842 1.00 61.45  ? 258 LEU   B CD2 1 
ATOM   3525 N N   . GLY   B 1 185 ? -7.290  62.834  19.415 1.00 85.40  ? 259 GLY   B N   1 
ATOM   3526 C CA  . GLY   B 1 185 ? -8.276  63.873  19.599 1.00 89.54  ? 259 GLY   B CA  1 
ATOM   3527 C C   . GLY   B 1 185 ? -8.045  65.047  18.660 1.00 109.48 ? 259 GLY   B C   1 
ATOM   3528 O O   . GLY   B 1 185 ? -7.274  64.988  17.700 1.00 110.76 ? 259 GLY   B O   1 
ATOM   3529 N N   . THR   B 1 186 ? -8.751  66.145  18.954 1.00 117.71 ? 260 THR   B N   1 
ATOM   3530 C CA  . THR   B 1 186 ? -8.587  67.358  18.158 1.00 120.68 ? 260 THR   B CA  1 
ATOM   3531 C C   . THR   B 1 186 ? -7.152  67.867  18.226 1.00 123.08 ? 260 THR   B C   1 
ATOM   3532 O O   . THR   B 1 186 ? -6.570  68.252  17.204 1.00 125.61 ? 260 THR   B O   1 
ATOM   3533 C CB  . THR   B 1 186 ? -9.563  68.449  18.621 1.00 113.35 ? 260 THR   B CB  1 
ATOM   3534 O OG1 . THR   B 1 186 ? -9.319  68.770  19.996 1.00 111.42 ? 260 THR   B OG1 1 
ATOM   3535 C CG2 . THR   B 1 186 ? -11.007 67.997  18.453 1.00 108.54 ? 260 THR   B CG2 1 
ATOM   3536 N N   . ALA   B 1 187 ? -6.557  67.859  19.417 1.00 121.37 ? 261 ALA   B N   1 
ATOM   3537 C CA  . ALA   B 1 187 ? -5.201  68.354  19.609 1.00 125.71 ? 261 ALA   B CA  1 
ATOM   3538 C C   . ALA   B 1 187 ? -4.220  67.240  19.951 1.00 130.30 ? 261 ALA   B C   1 
ATOM   3539 O O   . ALA   B 1 187 ? -3.257  67.016  19.211 1.00 132.21 ? 261 ALA   B O   1 
ATOM   3540 C CB  . ALA   B 1 187 ? -5.185  69.436  20.699 1.00 123.09 ? 261 ALA   B CB  1 
ATOM   3541 N N   . GLY   B 1 188 ? -4.444  66.524  21.050 1.00 135.81 ? 262 GLY   B N   1 
ATOM   3542 C CA  . GLY   B 1 188 ? -3.470  65.591  21.598 1.00 135.43 ? 262 GLY   B CA  1 
ATOM   3543 C C   . GLY   B 1 188 ? -3.995  64.161  21.561 1.00 132.03 ? 262 GLY   B C   1 
ATOM   3544 O O   . GLY   B 1 188 ? -5.186  63.910  21.353 1.00 128.21 ? 262 GLY   B O   1 
ATOM   3545 N N   . ALA   B 1 189 ? -3.071  63.217  21.768 1.00 113.51 ? 263 ALA   B N   1 
ATOM   3546 C CA  . ALA   B 1 189 ? -3.445  61.817  21.920 1.00 100.32 ? 263 ALA   B CA  1 
ATOM   3547 C C   . ALA   B 1 189 ? -3.900  61.506  23.339 1.00 103.97 ? 263 ALA   B C   1 
ATOM   3548 O O   . ALA   B 1 189 ? -4.682  60.570  23.543 1.00 96.18  ? 263 ALA   B O   1 
ATOM   3549 C CB  . ALA   B 1 189 ? -2.276  60.909  21.533 1.00 87.08  ? 263 ALA   B CB  1 
ATOM   3550 N N   . GLY   B 1 190 ? -3.429  62.262  24.317 1.00 108.74 ? 264 GLY   B N   1 
ATOM   3551 C CA  . GLY   B 1 190 ? -3.898  62.119  25.695 1.00 108.67 ? 264 GLY   B CA  1 
ATOM   3552 C C   . GLY   B 1 190 ? -3.055  61.122  26.484 1.00 105.37 ? 264 GLY   B C   1 
ATOM   3553 O O   . GLY   B 1 190 ? -1.848  61.321  26.647 1.00 102.83 ? 264 GLY   B O   1 
ATOM   3554 N N   . GLU   B 1 191 ? -3.696  60.058  26.971 1.00 97.56  ? 265 GLU   B N   1 
ATOM   3555 C CA  . GLU   B 1 191 ? -3.046  59.077  27.835 1.00 92.98  ? 265 GLU   B CA  1 
ATOM   3556 C C   . GLU   B 1 191 ? -2.542  57.913  26.988 1.00 83.41  ? 265 GLU   B C   1 
ATOM   3557 O O   . GLU   B 1 191 ? -3.330  57.079  26.529 1.00 80.75  ? 265 GLU   B O   1 
ATOM   3558 C CB  . GLU   B 1 191 ? -4.005  58.596  28.926 1.00 97.83  ? 265 GLU   B CB  1 
ATOM   3559 C CG  . GLU   B 1 191 ? -3.417  57.519  29.846 1.00 102.78 ? 265 GLU   B CG  1 
ATOM   3560 C CD  . GLU   B 1 191 ? -4.064  57.483  31.229 1.00 109.52 ? 265 GLU   B CD  1 
ATOM   3561 O OE1 . GLU   B 1 191 ? -5.050  58.223  31.452 1.00 102.22 ? 265 GLU   B OE1 1 
ATOM   3562 O OE2 . GLU   B 1 191 ? -3.576  56.715  32.094 1.00 105.79 ? 265 GLU   B OE2 1 
ATOM   3563 N N   . VAL   B 1 192 ? -1.228  57.856  26.788 1.00 82.67  ? 266 VAL   B N   1 
ATOM   3564 C CA  . VAL   B 1 192 ? -0.564  56.765  26.084 1.00 75.43  ? 266 VAL   B CA  1 
ATOM   3565 C C   . VAL   B 1 192 ? 0.234   55.961  27.099 1.00 72.26  ? 266 VAL   B C   1 
ATOM   3566 O O   . VAL   B 1 192 ? 0.951   56.536  27.929 1.00 74.86  ? 266 VAL   B O   1 
ATOM   3567 C CB  . VAL   B 1 192 ? 0.356   57.292  24.969 1.00 67.73  ? 266 VAL   B CB  1 
ATOM   3568 C CG1 . VAL   B 1 192 ? 1.183   56.157  24.397 1.00 68.34  ? 266 VAL   B CG1 1 
ATOM   3569 C CG2 . VAL   B 1 192 ? -0.455  57.964  23.886 1.00 72.12  ? 266 VAL   B CG2 1 
ATOM   3570 N N   . GLN   B 1 193 ? 0.125   54.640  27.028 1.00 65.47  ? 267 GLN   B N   1 
ATOM   3571 C CA  . GLN   B 1 193 ? 0.901   53.759  27.885 1.00 64.62  ? 267 GLN   B CA  1 
ATOM   3572 C C   . GLN   B 1 193 ? 2.152   53.268  27.163 1.00 62.53  ? 267 GLN   B C   1 
ATOM   3573 O O   . GLN   B 1 193 ? 2.282   53.378  25.941 1.00 60.33  ? 267 GLN   B O   1 
ATOM   3574 C CB  . GLN   B 1 193 ? 0.058   52.571  28.347 1.00 65.30  ? 267 GLN   B CB  1 
ATOM   3575 C CG  . GLN   B 1 193 ? -1.216  52.972  29.063 1.00 70.66  ? 267 GLN   B CG  1 
ATOM   3576 C CD  . GLN   B 1 193 ? -1.941  51.781  29.648 1.00 75.92  ? 267 GLN   B CD  1 
ATOM   3577 O OE1 . GLN   B 1 193 ? -1.314  50.870  30.188 1.00 85.81  ? 267 GLN   B OE1 1 
ATOM   3578 N NE2 . GLN   B 1 193 ? -3.266  51.774  29.536 1.00 74.82  ? 267 GLN   B NE2 1 
ATOM   3579 N N   . GLU   B 1 194 ? 3.079   52.724  27.950 1.00 68.20  ? 268 GLU   B N   1 
ATOM   3580 C CA  . GLU   B 1 194 ? 4.361   52.275  27.423 1.00 60.92  ? 268 GLU   B CA  1 
ATOM   3581 C C   . GLU   B 1 194 ? 4.169   51.039  26.559 1.00 58.04  ? 268 GLU   B C   1 
ATOM   3582 O O   . GLU   B 1 194 ? 3.512   50.078  26.971 1.00 59.24  ? 268 GLU   B O   1 
ATOM   3583 C CB  . GLU   B 1 194 ? 5.324   51.972  28.571 1.00 62.55  ? 268 GLU   B CB  1 
ATOM   3584 C CG  . GLU   B 1 194 ? 5.469   53.104  29.591 1.00 69.02  ? 268 GLU   B CG  1 
ATOM   3585 C CD  . GLU   B 1 194 ? 6.770   53.881  29.437 1.00 74.81  ? 268 GLU   B CD  1 
ATOM   3586 O OE1 . GLU   B 1 194 ? 7.488   53.633  28.441 1.00 67.57  ? 268 GLU   B OE1 1 
ATOM   3587 O OE2 . GLU   B 1 194 ? 7.074   54.731  30.312 1.00 72.95  ? 268 GLU   B OE2 1 
ATOM   3588 N N   . GLY   B 1 195 ? 4.741   51.060  25.355 1.00 58.18  ? 269 GLY   B N   1 
ATOM   3589 C CA  . GLY   B 1 195 ? 4.637   49.948  24.438 1.00 53.43  ? 269 GLY   B CA  1 
ATOM   3590 C C   . GLY   B 1 195 ? 5.864   49.043  24.469 1.00 55.89  ? 269 GLY   B C   1 
ATOM   3591 O O   . GLY   B 1 195 ? 6.844   49.278  25.173 1.00 57.85  ? 269 GLY   B O   1 
ATOM   3592 N N   . ASP   B 1 196 ? 5.789   47.985  23.678 1.00 57.63  ? 270 ASP   B N   1 
ATOM   3593 C CA  . ASP   B 1 196 ? 6.916   47.070  23.542 1.00 51.14  ? 270 ASP   B CA  1 
ATOM   3594 C C   . ASP   B 1 196 ? 8.013   47.764  22.744 1.00 49.04  ? 270 ASP   B C   1 
ATOM   3595 O O   . ASP   B 1 196 ? 7.790   48.109  21.577 1.00 48.35  ? 270 ASP   B O   1 
ATOM   3596 C CB  . ASP   B 1 196 ? 6.463   45.784  22.849 1.00 50.18  ? 270 ASP   B CB  1 
ATOM   3597 C CG  . ASP   B 1 196 ? 7.420   44.623  23.071 1.00 50.75  ? 270 ASP   B CG  1 
ATOM   3598 O OD1 . ASP   B 1 196 ? 8.650   44.839  23.058 1.00 51.75  ? 270 ASP   B OD1 1 
ATOM   3599 O OD2 . ASP   B 1 196 ? 6.938   43.483  23.251 1.00 57.67  ? 270 ASP   B OD2 1 
ATOM   3600 N N   . PRO   B 1 197 ? 9.194   48.001  23.319 1.00 51.56  ? 271 PRO   B N   1 
ATOM   3601 C CA  . PRO   B 1 197 ? 10.236  48.716  22.567 1.00 48.77  ? 271 PRO   B CA  1 
ATOM   3602 C C   . PRO   B 1 197 ? 10.717  47.975  21.336 1.00 50.41  ? 271 PRO   B C   1 
ATOM   3603 O O   . PRO   B 1 197 ? 11.180  48.619  20.386 1.00 51.06  ? 271 PRO   B O   1 
ATOM   3604 C CB  . PRO   B 1 197 ? 11.357  48.885  23.599 1.00 50.60  ? 271 PRO   B CB  1 
ATOM   3605 C CG  . PRO   B 1 197 ? 11.129  47.788  24.580 1.00 52.61  ? 271 PRO   B CG  1 
ATOM   3606 C CD  . PRO   B 1 197 ? 9.642   47.643  24.674 1.00 51.64  ? 271 PRO   B CD  1 
ATOM   3607 N N   . ARG   B 1 198 ? 10.626  46.642  21.312 1.00 53.34  ? 272 ARG   B N   1 
ATOM   3608 C CA  . ARG   B 1 198 ? 11.093  45.901  20.142 1.00 46.48  ? 272 ARG   B CA  1 
ATOM   3609 C C   . ARG   B 1 198 ? 10.358  46.326  18.878 1.00 48.45  ? 272 ARG   B C   1 
ATOM   3610 O O   . ARG   B 1 198 ? 10.959  46.373  17.796 1.00 45.04  ? 272 ARG   B O   1 
ATOM   3611 C CB  . ARG   B 1 198 ? 10.933  44.399  20.378 1.00 46.68  ? 272 ARG   B CB  1 
ATOM   3612 C CG  . ARG   B 1 198 ? 11.714  43.904  21.581 1.00 53.89  ? 272 ARG   B CG  1 
ATOM   3613 C CD  . ARG   B 1 198 ? 11.454  42.439  21.879 1.00 55.27  ? 272 ARG   B CD  1 
ATOM   3614 N NE  . ARG   B 1 198 ? 10.095  42.205  22.349 1.00 57.68  ? 272 ARG   B NE  1 
ATOM   3615 C CZ  . ARG   B 1 198 ? 9.712   41.118  23.004 1.00 59.88  ? 272 ARG   B CZ  1 
ATOM   3616 N NH1 . ARG   B 1 198 ? 10.572  40.165  23.323 1.00 62.67  ? 272 ARG   B NH1 1 
ATOM   3617 N NH2 . ARG   B 1 198 ? 8.433   40.983  23.344 1.00 57.31  ? 272 ARG   B NH2 1 
ATOM   3618 N N   . TYR   B 1 199 ? 9.073   46.662  18.995 1.00 47.59  ? 273 TYR   B N   1 
ATOM   3619 C CA  . TYR   B 1 199 ? 8.240   46.991  17.844 1.00 43.31  ? 273 TYR   B CA  1 
ATOM   3620 C C   . TYR   B 1 199 ? 7.973   48.485  17.730 1.00 45.57  ? 273 TYR   B C   1 
ATOM   3621 O O   . TYR   B 1 199 ? 7.148   48.897  16.909 1.00 48.47  ? 273 TYR   B O   1 
ATOM   3622 C CB  . TYR   B 1 199 ? 6.919   46.222  17.917 1.00 43.62  ? 273 TYR   B CB  1 
ATOM   3623 C CG  . TYR   B 1 199 ? 7.105   44.737  18.126 1.00 42.93  ? 273 TYR   B CG  1 
ATOM   3624 C CD1 . TYR   B 1 199 ? 7.183   44.200  19.406 1.00 42.83  ? 273 TYR   B CD1 1 
ATOM   3625 C CD2 . TYR   B 1 199 ? 7.217   43.876  17.047 1.00 39.96  ? 273 TYR   B CD2 1 
ATOM   3626 C CE1 . TYR   B 1 199 ? 7.367   42.844  19.602 1.00 45.48  ? 273 TYR   B CE1 1 
ATOM   3627 C CE2 . TYR   B 1 199 ? 7.397   42.522  17.233 1.00 42.63  ? 273 TYR   B CE2 1 
ATOM   3628 C CZ  . TYR   B 1 199 ? 7.474   42.008  18.510 1.00 47.74  ? 273 TYR   B CZ  1 
ATOM   3629 O OH  . TYR   B 1 199 ? 7.658   40.654  18.701 1.00 49.89  ? 273 TYR   B OH  1 
ATOM   3630 N N   . MET   B 1 200 ? 8.669   49.302  18.516 1.00 46.83  ? 274 MET   B N   1 
ATOM   3631 C CA  . MET   B 1 200 ? 8.379   50.725  18.611 1.00 43.71  ? 274 MET   B CA  1 
ATOM   3632 C C   . MET   B 1 200 ? 8.917   51.486  17.404 1.00 50.42  ? 274 MET   B C   1 
ATOM   3633 O O   . MET   B 1 200 ? 10.091  51.344  17.044 1.00 47.59  ? 274 MET   B O   1 
ATOM   3634 C CB  . MET   B 1 200 ? 8.986   51.284  19.893 1.00 48.99  ? 274 MET   B CB  1 
ATOM   3635 C CG  . MET   B 1 200 ? 8.876   52.778  20.032 1.00 52.85  ? 274 MET   B CG  1 
ATOM   3636 S SD  . MET   B 1 200 ? 9.263   53.258  21.720 1.00 64.78  ? 274 MET   B SD  1 
ATOM   3637 C CE  . MET   B 1 200 ? 11.028  52.976  21.755 1.00 59.00  ? 274 MET   B CE  1 
ATOM   3638 N N   . ALA   B 1 201 ? 8.056   52.305  16.791 1.00 47.79  ? 275 ALA   B N   1 
ATOM   3639 C CA  . ALA   B 1 201 ? 8.482   53.182  15.713 1.00 49.29  ? 275 ALA   B CA  1 
ATOM   3640 C C   . ALA   B 1 201 ? 9.422   54.261  16.248 1.00 51.48  ? 275 ALA   B C   1 
ATOM   3641 O O   . ALA   B 1 201 ? 9.262   54.726  17.381 1.00 53.57  ? 275 ALA   B O   1 
ATOM   3642 C CB  . ALA   B 1 201 ? 7.277   53.833  15.041 1.00 50.28  ? 275 ALA   B CB  1 
ATOM   3643 N N   . PRO   B 1 202 ? 10.404  54.686  15.443 1.00 49.32  ? 276 PRO   B N   1 
ATOM   3644 C CA  . PRO   B 1 202 ? 11.427  55.616  15.963 1.00 47.19  ? 276 PRO   B CA  1 
ATOM   3645 C C   . PRO   B 1 202 ? 10.863  56.921  16.500 1.00 53.77  ? 276 PRO   B C   1 
ATOM   3646 O O   . PRO   B 1 202 ? 11.363  57.433  17.509 1.00 55.93  ? 276 PRO   B O   1 
ATOM   3647 C CB  . PRO   B 1 202 ? 12.327  55.863  14.745 1.00 52.94  ? 276 PRO   B CB  1 
ATOM   3648 C CG  . PRO   B 1 202 ? 12.025  54.749  13.793 1.00 52.33  ? 276 PRO   B CG  1 
ATOM   3649 C CD  . PRO   B 1 202 ? 10.607  54.365  14.023 1.00 46.18  ? 276 PRO   B CD  1 
ATOM   3650 N N   . GLU   B 1 203 ? 9.836   57.482  15.854 1.00 54.91  ? 277 GLU   B N   1 
ATOM   3651 C CA  . GLU   B 1 203 ? 9.346   58.793  16.266 1.00 52.89  ? 277 GLU   B CA  1 
ATOM   3652 C C   . GLU   B 1 203 ? 8.678   58.759  17.634 1.00 57.11  ? 277 GLU   B C   1 
ATOM   3653 O O   . GLU   B 1 203 ? 8.573   59.810  18.277 1.00 55.08  ? 277 GLU   B O   1 
ATOM   3654 C CB  . GLU   B 1 203 ? 8.374   59.358  15.229 1.00 52.74  ? 277 GLU   B CB  1 
ATOM   3655 C CG  . GLU   B 1 203 ? 7.040   58.622  15.141 1.00 56.59  ? 277 GLU   B CG  1 
ATOM   3656 C CD  . GLU   B 1 203 ? 7.070   57.478  14.153 1.00 54.69  ? 277 GLU   B CD  1 
ATOM   3657 O OE1 . GLU   B 1 203 ? 8.185   57.112  13.726 1.00 55.89  ? 277 GLU   B OE1 1 
ATOM   3658 O OE2 . GLU   B 1 203 ? 5.989   56.952  13.791 1.00 53.00  ? 277 GLU   B OE2 1 
ATOM   3659 N N   . LEU   B 1 204 ? 8.234   57.584  18.097 1.00 56.48  ? 278 LEU   B N   1 
ATOM   3660 C CA  . LEU   B 1 204 ? 7.567   57.510  19.395 1.00 52.91  ? 278 LEU   B CA  1 
ATOM   3661 C C   . LEU   B 1 204 ? 8.487   57.938  20.522 1.00 54.20  ? 278 LEU   B C   1 
ATOM   3662 O O   . LEU   B 1 204 ? 8.015   58.393  21.569 1.00 59.22  ? 278 LEU   B O   1 
ATOM   3663 C CB  . LEU   B 1 204 ? 7.048   56.096  19.659 1.00 55.88  ? 278 LEU   B CB  1 
ATOM   3664 C CG  . LEU   B 1 204 ? 5.804   55.669  18.879 1.00 55.06  ? 278 LEU   B CG  1 
ATOM   3665 C CD1 . LEU   B 1 204 ? 5.139   54.494  19.562 1.00 51.85  ? 278 LEU   B CD1 1 
ATOM   3666 C CD2 . LEU   B 1 204 ? 4.839   56.831  18.748 1.00 55.43  ? 278 LEU   B CD2 1 
ATOM   3667 N N   . LEU   B 1 205 ? 9.799   57.814  20.326 1.00 57.20  ? 279 LEU   B N   1 
ATOM   3668 C CA  . LEU   B 1 205 ? 10.727  58.256  21.354 1.00 57.65  ? 279 LEU   B CA  1 
ATOM   3669 C C   . LEU   B 1 205 ? 10.628  59.754  21.587 1.00 61.77  ? 279 LEU   B C   1 
ATOM   3670 O O   . LEU   B 1 205 ? 10.896  60.225  22.697 1.00 67.57  ? 279 LEU   B O   1 
ATOM   3671 C CB  . LEU   B 1 205 ? 12.151  57.876  20.967 1.00 60.73  ? 279 LEU   B CB  1 
ATOM   3672 C CG  . LEU   B 1 205 ? 12.606  56.468  21.325 1.00 58.21  ? 279 LEU   B CG  1 
ATOM   3673 C CD1 . LEU   B 1 205 ? 14.054  56.315  20.933 1.00 55.98  ? 279 LEU   B CD1 1 
ATOM   3674 C CD2 . LEU   B 1 205 ? 12.430  56.228  22.807 1.00 57.83  ? 279 LEU   B CD2 1 
ATOM   3675 N N   . GLN   B 1 206 ? 10.248  60.514  20.561 1.00 59.09  ? 280 GLN   B N   1 
ATOM   3676 C CA  . GLN   B 1 206 ? 10.141  61.964  20.653 1.00 62.22  ? 280 GLN   B CA  1 
ATOM   3677 C C   . GLN   B 1 206 ? 8.704   62.429  20.836 1.00 65.01  ? 280 GLN   B C   1 
ATOM   3678 O O   . GLN   B 1 206 ? 8.381   63.572  20.495 1.00 70.27  ? 280 GLN   B O   1 
ATOM   3679 C CB  . GLN   B 1 206 ? 10.757  62.621  19.417 1.00 62.68  ? 280 GLN   B CB  1 
ATOM   3680 C CG  . GLN   B 1 206 ? 12.284  62.675  19.438 1.00 74.81  ? 280 GLN   B CG  1 
ATOM   3681 C CD  . GLN   B 1 206 ? 12.926  61.301  19.310 1.00 72.45  ? 280 GLN   B CD  1 
ATOM   3682 O OE1 . GLN   B 1 206 ? 12.633  60.551  18.374 1.00 71.70  ? 280 GLN   B OE1 1 
ATOM   3683 N NE2 . GLN   B 1 206 ? 13.803  60.963  20.256 1.00 63.78  ? 280 GLN   B NE2 1 
ATOM   3684 N N   . GLY   B 1 207 ? 7.836   61.565  21.357 1.00 65.33  ? 281 GLY   B N   1 
ATOM   3685 C CA  . GLY   B 1 207 ? 6.464   61.947  21.642 1.00 69.81  ? 281 GLY   B CA  1 
ATOM   3686 C C   . GLY   B 1 207 ? 5.608   62.229  20.428 1.00 64.98  ? 281 GLY   B C   1 
ATOM   3687 O O   . GLY   B 1 207 ? 4.636   62.984  20.527 1.00 71.64  ? 281 GLY   B O   1 
ATOM   3688 N N   . SER   B 1 208 ? 5.934   61.638  19.283 1.00 61.60  ? 282 SER   B N   1 
ATOM   3689 C CA  . SER   B 1 208 ? 5.223   61.913  18.037 1.00 61.91  ? 282 SER   B CA  1 
ATOM   3690 C C   . SER   B 1 208 ? 4.326   60.720  17.729 1.00 62.38  ? 282 SER   B C   1 
ATOM   3691 O O   . SER   B 1 208 ? 4.710   59.792  17.020 1.00 63.53  ? 282 SER   B O   1 
ATOM   3692 C CB  . SER   B 1 208 ? 6.208   62.196  16.913 1.00 62.64  ? 282 SER   B CB  1 
ATOM   3693 O OG  . SER   B 1 208 ? 5.536   62.688  15.768 1.00 71.99  ? 282 SER   B OG  1 
ATOM   3694 N N   . TYR   B 1 209 ? 3.108   60.754  18.261 1.00 62.94  ? 283 TYR   B N   1 
ATOM   3695 C CA  . TYR   B 1 209 ? 2.180   59.638  18.162 1.00 58.54  ? 283 TYR   B CA  1 
ATOM   3696 C C   . TYR   B 1 209 ? 1.231   59.861  16.997 1.00 57.40  ? 283 TYR   B C   1 
ATOM   3697 O O   . TYR   B 1 209 ? 0.604   60.918  16.892 1.00 56.14  ? 283 TYR   B O   1 
ATOM   3698 C CB  . TYR   B 1 209 ? 1.396   59.465  19.464 1.00 60.80  ? 283 TYR   B CB  1 
ATOM   3699 C CG  . TYR   B 1 209 ? 2.277   59.127  20.644 1.00 61.85  ? 283 TYR   B CG  1 
ATOM   3700 C CD1 . TYR   B 1 209 ? 2.918   60.126  21.371 1.00 64.16  ? 283 TYR   B CD1 1 
ATOM   3701 C CD2 . TYR   B 1 209 ? 2.478   57.806  21.029 1.00 66.45  ? 283 TYR   B CD2 1 
ATOM   3702 C CE1 . TYR   B 1 209 ? 3.735   59.817  22.450 1.00 65.70  ? 283 TYR   B CE1 1 
ATOM   3703 C CE2 . TYR   B 1 209 ? 3.299   57.486  22.105 1.00 60.94  ? 283 TYR   B CE2 1 
ATOM   3704 C CZ  . TYR   B 1 209 ? 3.921   58.495  22.815 1.00 68.70  ? 283 TYR   B CZ  1 
ATOM   3705 O OH  . TYR   B 1 209 ? 4.732   58.181  23.890 1.00 76.80  ? 283 TYR   B OH  1 
ATOM   3706 N N   . GLY   B 1 210 ? 1.136   58.867  16.122 1.00 55.89  ? 284 GLY   B N   1 
ATOM   3707 C CA  . GLY   B 1 210 ? 0.238   58.944  14.988 1.00 54.29  ? 284 GLY   B CA  1 
ATOM   3708 C C   . GLY   B 1 210 ? -0.026  57.554  14.455 1.00 56.18  ? 284 GLY   B C   1 
ATOM   3709 O O   . GLY   B 1 210 ? 0.538   56.564  14.926 1.00 55.39  ? 284 GLY   B O   1 
ATOM   3710 N N   . THR   B 1 211 ? -0.905  57.489  13.453 1.00 53.66  ? 285 THR   B N   1 
ATOM   3711 C CA  . THR   B 1 211 ? -1.219  56.200  12.854 1.00 50.92  ? 285 THR   B CA  1 
ATOM   3712 C C   . THR   B 1 211 ? 0.009   55.569  12.216 1.00 49.69  ? 285 THR   B C   1 
ATOM   3713 O O   . THR   B 1 211 ? 0.160   54.344  12.244 1.00 50.74  ? 285 THR   B O   1 
ATOM   3714 C CB  . THR   B 1 211 ? -2.336  56.361  11.836 1.00 50.06  ? 285 THR   B CB  1 
ATOM   3715 O OG1 . THR   B 1 211 ? -1.977  57.386  10.906 1.00 56.22  ? 285 THR   B OG1 1 
ATOM   3716 C CG2 . THR   B 1 211 ? -3.616  56.765  12.542 1.00 51.35  ? 285 THR   B CG2 1 
ATOM   3717 N N   . ALA   B 1 212 ? 0.914   56.390  11.679 1.00 51.85  ? 286 ALA   B N   1 
ATOM   3718 C CA  . ALA   B 1 212 ? 2.150   55.887  11.086 1.00 46.14  ? 286 ALA   B CA  1 
ATOM   3719 C C   . ALA   B 1 212 ? 2.918   54.965  12.018 1.00 48.79  ? 286 ALA   B C   1 
ATOM   3720 O O   . ALA   B 1 212 ? 3.712   54.144  11.546 1.00 48.49  ? 286 ALA   B O   1 
ATOM   3721 C CB  . ALA   B 1 212 ? 3.049   57.054  10.681 1.00 46.85  ? 286 ALA   B CB  1 
ATOM   3722 N N   . ALA   B 1 213 ? 2.708   55.084  13.330 1.00 48.95  ? 287 ALA   B N   1 
ATOM   3723 C CA  . ALA   B 1 213 ? 3.430   54.231  14.269 1.00 50.28  ? 287 ALA   B CA  1 
ATOM   3724 C C   . ALA   B 1 213 ? 3.071   52.765  14.072 1.00 51.06  ? 287 ALA   B C   1 
ATOM   3725 O O   . ALA   B 1 213 ? 3.940   51.887  14.156 1.00 48.67  ? 287 ALA   B O   1 
ATOM   3726 C CB  . ALA   B 1 213 ? 3.136   54.668  15.702 1.00 48.73  ? 287 ALA   B CB  1 
ATOM   3727 N N   . ASP   B 1 214 ? 1.792   52.481  13.813 1.00 51.31  ? 288 ASP   B N   1 
ATOM   3728 C CA  . ASP   B 1 214 ? 1.354   51.099  13.642 1.00 43.82  ? 288 ASP   B CA  1 
ATOM   3729 C C   . ASP   B 1 214 ? 1.950   50.482  12.384 1.00 46.55  ? 288 ASP   B C   1 
ATOM   3730 O O   . ASP   B 1 214 ? 2.297   49.296  12.373 1.00 51.28  ? 288 ASP   B O   1 
ATOM   3731 C CB  . ASP   B 1 214 ? -0.174  51.035  13.595 1.00 43.63  ? 288 ASP   B CB  1 
ATOM   3732 C CG  . ASP   B 1 214 ? -0.812  51.179  14.973 1.00 48.35  ? 288 ASP   B CG  1 
ATOM   3733 O OD1 . ASP   B 1 214 ? -0.094  51.012  15.988 1.00 42.21  ? 288 ASP   B OD1 1 
ATOM   3734 O OD2 . ASP   B 1 214 ? -2.038  51.443  15.038 1.00 49.15  ? 288 ASP   B OD2 1 
ATOM   3735 N N   . VAL   B 1 215 ? 2.075   51.265  11.314 1.00 48.16  ? 289 VAL   B N   1 
ATOM   3736 C CA  . VAL   B 1 215 ? 2.640   50.729  10.080 1.00 50.75  ? 289 VAL   B CA  1 
ATOM   3737 C C   . VAL   B 1 215 ? 4.078   50.267  10.307 1.00 49.78  ? 289 VAL   B C   1 
ATOM   3738 O O   . VAL   B 1 215 ? 4.495   49.222  9.793  1.00 52.79  ? 289 VAL   B O   1 
ATOM   3739 C CB  . VAL   B 1 215 ? 2.532   51.770  8.950  1.00 49.29  ? 289 VAL   B CB  1 
ATOM   3740 C CG1 . VAL   B 1 215 ? 3.318   51.328  7.728  1.00 50.65  ? 289 VAL   B CG1 1 
ATOM   3741 C CG2 . VAL   B 1 215 ? 1.066   51.989  8.579  1.00 45.80  ? 289 VAL   B CG2 1 
ATOM   3742 N N   . PHE   B 1 216 ? 4.846   51.006  11.112 1.00 47.00  ? 290 PHE   B N   1 
ATOM   3743 C CA  . PHE   B 1 216 ? 6.212   50.576  11.400 1.00 46.05  ? 290 PHE   B CA  1 
ATOM   3744 C C   . PHE   B 1 216 ? 6.218   49.309  12.250 1.00 46.36  ? 290 PHE   B C   1 
ATOM   3745 O O   . PHE   B 1 216 ? 6.948   48.355  11.954 1.00 45.66  ? 290 PHE   B O   1 
ATOM   3746 C CB  . PHE   B 1 216 ? 6.982   51.696  12.098 1.00 46.78  ? 290 PHE   B CB  1 
ATOM   3747 C CG  . PHE   B 1 216 ? 8.459   51.438  12.211 1.00 46.29  ? 290 PHE   B CG  1 
ATOM   3748 C CD1 . PHE   B 1 216 ? 8.973   50.712  13.275 1.00 45.78  ? 290 PHE   B CD1 1 
ATOM   3749 C CD2 . PHE   B 1 216 ? 9.336   51.936  11.258 1.00 44.51  ? 290 PHE   B CD2 1 
ATOM   3750 C CE1 . PHE   B 1 216 ? 10.332  50.477  13.378 1.00 47.27  ? 290 PHE   B CE1 1 
ATOM   3751 C CE2 . PHE   B 1 216 ? 10.694  51.704  11.352 1.00 47.78  ? 290 PHE   B CE2 1 
ATOM   3752 C CZ  . PHE   B 1 216 ? 11.195  50.975  12.413 1.00 48.90  ? 290 PHE   B CZ  1 
ATOM   3753 N N   . SER   B 1 217 ? 5.409   49.284  13.315 1.00 43.52  ? 291 SER   B N   1 
ATOM   3754 C CA  . SER   B 1 217 ? 5.321   48.092  14.149 1.00 42.69  ? 291 SER   B CA  1 
ATOM   3755 C C   . SER   B 1 217 ? 4.983   46.868  13.316 1.00 42.81  ? 291 SER   B C   1 
ATOM   3756 O O   . SER   B 1 217 ? 5.576   45.797  13.502 1.00 45.03  ? 291 SER   B O   1 
ATOM   3757 C CB  . SER   B 1 217 ? 4.277   48.288  15.251 1.00 43.28  ? 291 SER   B CB  1 
ATOM   3758 O OG  . SER   B 1 217 ? 4.638   49.348  16.124 1.00 45.91  ? 291 SER   B OG  1 
ATOM   3759 N N   . LEU   B 1 218 ? 4.041   47.005  12.385 1.00 44.49  ? 292 LEU   B N   1 
ATOM   3760 C CA  . LEU   B 1 218 ? 3.730   45.891  11.497 1.00 48.46  ? 292 LEU   B CA  1 
ATOM   3761 C C   . LEU   B 1 218 ? 4.939   45.509  10.652 1.00 46.90  ? 292 LEU   B C   1 
ATOM   3762 O O   . LEU   B 1 218 ? 5.176   44.323  10.397 1.00 50.09  ? 292 LEU   B O   1 
ATOM   3763 C CB  . LEU   B 1 218 ? 2.548   46.244  10.601 1.00 46.73  ? 292 LEU   B CB  1 
ATOM   3764 C CG  . LEU   B 1 218 ? 1.979   45.072  9.807  1.00 46.21  ? 292 LEU   B CG  1 
ATOM   3765 C CD1 . LEU   B 1 218 ? 1.767   43.882  10.715 1.00 40.86  ? 292 LEU   B CD1 1 
ATOM   3766 C CD2 . LEU   B 1 218 ? 0.672   45.488  9.179  1.00 46.52  ? 292 LEU   B CD2 1 
ATOM   3767 N N   . GLY   B 1 219 ? 5.720   46.502  10.215 1.00 47.34  ? 293 GLY   B N   1 
ATOM   3768 C CA  . GLY   B 1 219 ? 6.898   46.203  9.416  1.00 47.02  ? 293 GLY   B CA  1 
ATOM   3769 C C   . GLY   B 1 219 ? 7.886   45.316  10.149 1.00 49.00  ? 293 GLY   B C   1 
ATOM   3770 O O   . GLY   B 1 219 ? 8.459   44.392  9.566  1.00 46.13  ? 293 GLY   B O   1 
ATOM   3771 N N   . LEU   B 1 220 ? 8.089   45.573  11.440 1.00 46.34  ? 294 LEU   B N   1 
ATOM   3772 C CA  . LEU   B 1 220 ? 8.954   44.700  12.222 1.00 44.60  ? 294 LEU   B CA  1 
ATOM   3773 C C   . LEU   B 1 220 ? 8.277   43.374  12.537 1.00 47.48  ? 294 LEU   B C   1 
ATOM   3774 O O   . LEU   B 1 220 ? 8.959   42.351  12.676 1.00 50.23  ? 294 LEU   B O   1 
ATOM   3775 C CB  . LEU   B 1 220 ? 9.378   45.402  13.504 1.00 45.91  ? 294 LEU   B CB  1 
ATOM   3776 C CG  . LEU   B 1 220 ? 10.263  46.617  13.266 1.00 42.29  ? 294 LEU   B CG  1 
ATOM   3777 C CD1 . LEU   B 1 220 ? 10.723  47.161  14.592 1.00 46.41  ? 294 LEU   B CD1 1 
ATOM   3778 C CD2 . LEU   B 1 220 ? 11.445  46.226  12.406 1.00 47.20  ? 294 LEU   B CD2 1 
ATOM   3779 N N   . THR   B 1 221 ? 6.946   43.372  12.658 1.00 50.06  ? 295 THR   B N   1 
ATOM   3780 C CA  . THR   B 1 221 ? 6.217   42.119  12.849 1.00 47.61  ? 295 THR   B CA  1 
ATOM   3781 C C   . THR   B 1 221 ? 6.425   41.181  11.666 1.00 47.74  ? 295 THR   B C   1 
ATOM   3782 O O   . THR   B 1 221 ? 6.678   39.985  11.844 1.00 51.12  ? 295 THR   B O   1 
ATOM   3783 C CB  . THR   B 1 221 ? 4.725   42.403  13.056 1.00 47.97  ? 295 THR   B CB  1 
ATOM   3784 O OG1 . THR   B 1 221 ? 4.533   43.098  14.294 1.00 47.29  ? 295 THR   B OG1 1 
ATOM   3785 C CG2 . THR   B 1 221 ? 3.931   41.107  13.094 1.00 44.82  ? 295 THR   B CG2 1 
ATOM   3786 N N   . ILE   B 1 222 ? 6.328   41.710  10.446 1.00 52.59  ? 296 ILE   B N   1 
ATOM   3787 C CA  . ILE   B 1 222 ? 6.497   40.874  9.260  1.00 46.25  ? 296 ILE   B CA  1 
ATOM   3788 C C   . ILE   B 1 222 ? 7.956   40.469  9.093  1.00 47.06  ? 296 ILE   B C   1 
ATOM   3789 O O   . ILE   B 1 222 ? 8.261   39.337  8.699  1.00 52.45  ? 296 ILE   B O   1 
ATOM   3790 C CB  . ILE   B 1 222 ? 5.958   41.607  8.020  1.00 51.34  ? 296 ILE   B CB  1 
ATOM   3791 C CG1 . ILE   B 1 222 ? 4.435   41.702  8.096  1.00 47.36  ? 296 ILE   B CG1 1 
ATOM   3792 C CG2 . ILE   B 1 222 ? 6.387   40.897  6.750  1.00 54.40  ? 296 ILE   B CG2 1 
ATOM   3793 C CD1 . ILE   B 1 222 ? 3.775   40.350  8.340  1.00 46.78  ? 296 ILE   B CD1 1 
ATOM   3794 N N   . LEU   B 1 223 ? 8.881   41.378  9.393  1.00 50.87  ? 297 LEU   B N   1 
ATOM   3795 C CA  . LEU   B 1 223 ? 10.297  41.036  9.317  1.00 51.11  ? 297 LEU   B CA  1 
ATOM   3796 C C   . LEU   B 1 223 ? 10.652  39.948  10.326 1.00 55.44  ? 297 LEU   B C   1 
ATOM   3797 O O   . LEU   B 1 223 ? 11.429  39.036  10.020 1.00 57.69  ? 297 LEU   B O   1 
ATOM   3798 C CB  . LEU   B 1 223 ? 11.139  42.292  9.545  1.00 50.69  ? 297 LEU   B CB  1 
ATOM   3799 C CG  . LEU   B 1 223 ? 12.640  42.221  9.275  1.00 50.05  ? 297 LEU   B CG  1 
ATOM   3800 C CD1 . LEU   B 1 223 ? 12.908  42.258  7.782  1.00 55.93  ? 297 LEU   B CD1 1 
ATOM   3801 C CD2 . LEU   B 1 223 ? 13.348  43.361  9.984  1.00 48.76  ? 297 LEU   B CD2 1 
ATOM   3802 N N   . GLU   B 1 224 ? 10.076  40.017  11.529 1.00 50.12  ? 298 GLU   B N   1 
ATOM   3803 C CA  . GLU   B 1 224 ? 10.377  39.023  12.555 1.00 47.33  ? 298 GLU   B CA  1 
ATOM   3804 C C   . GLU   B 1 224 ? 9.921   37.628  12.142 1.00 49.48  ? 298 GLU   B C   1 
ATOM   3805 O O   . GLU   B 1 224 ? 10.646  36.647  12.345 1.00 52.56  ? 298 GLU   B O   1 
ATOM   3806 C CB  . GLU   B 1 224 ? 9.728   39.429  13.880 1.00 50.03  ? 298 GLU   B CB  1 
ATOM   3807 C CG  . GLU   B 1 224 ? 9.683   38.325  14.929 1.00 46.53  ? 298 GLU   B CG  1 
ATOM   3808 C CD  . GLU   B 1 224 ? 8.903   38.724  16.181 1.00 53.62  ? 298 GLU   B CD  1 
ATOM   3809 O OE1 . GLU   B 1 224 ? 8.525   39.907  16.304 1.00 53.95  ? 298 GLU   B OE1 1 
ATOM   3810 O OE2 . GLU   B 1 224 ? 8.664   37.852  17.045 1.00 60.81  ? 298 GLU   B OE2 1 
ATOM   3811 N N   . VAL   B 1 225 ? 8.728   37.510  11.563 1.00 50.48  ? 299 VAL   B N   1 
ATOM   3812 C CA  . VAL   B 1 225 ? 8.204   36.182  11.253 1.00 49.74  ? 299 VAL   B CA  1 
ATOM   3813 C C   . VAL   B 1 225 ? 8.672   35.674  9.889  1.00 50.62  ? 299 VAL   B C   1 
ATOM   3814 O O   . VAL   B 1 225 ? 8.875   34.470  9.719  1.00 56.20  ? 299 VAL   B O   1 
ATOM   3815 C CB  . VAL   B 1 225 ? 6.667   36.162  11.351 1.00 48.42  ? 299 VAL   B CB  1 
ATOM   3816 C CG1 . VAL   B 1 225 ? 6.208   36.788  12.659 1.00 47.51  ? 299 VAL   B CG1 1 
ATOM   3817 C CG2 . VAL   B 1 225 ? 6.021   36.861  10.162 1.00 50.90  ? 299 VAL   B CG2 1 
ATOM   3818 N N   . ALA   B 1 226 ? 8.856   36.558  8.907  1.00 51.89  ? 300 ALA   B N   1 
ATOM   3819 C CA  . ALA   B 1 226 ? 9.315   36.104  7.600  1.00 54.69  ? 300 ALA   B CA  1 
ATOM   3820 C C   . ALA   B 1 226 ? 10.789  35.739  7.607  1.00 54.38  ? 300 ALA   B C   1 
ATOM   3821 O O   . ALA   B 1 226 ? 11.249  35.043  6.696  1.00 60.08  ? 300 ALA   B O   1 
ATOM   3822 C CB  . ALA   B 1 226 ? 9.056   37.175  6.539  1.00 56.98  ? 300 ALA   B CB  1 
ATOM   3823 N N   . CYS   B 1 227 ? 11.542  36.199  8.605  1.00 60.84  ? 301 CYS   B N   1 
ATOM   3824 C CA  . CYS   B 1 227 ? 12.957  35.892  8.716  1.00 59.18  ? 301 CYS   B CA  1 
ATOM   3825 C C   . CYS   B 1 227 ? 13.301  35.114  9.967  1.00 56.98  ? 301 CYS   B C   1 
ATOM   3826 O O   . CYS   B 1 227 ? 14.441  34.652  10.089 1.00 63.61  ? 301 CYS   B O   1 
ATOM   3827 C CB  . CYS   B 1 227 ? 13.793  37.180  8.692  1.00 67.06  ? 301 CYS   B CB  1 
ATOM   3828 S SG  . CYS   B 1 227 ? 13.612  38.122  7.161  1.00 74.69  ? 301 CYS   B SG  1 
ATOM   3829 N N   . ASN   B 1 228 ? 12.359  34.958  10.895 1.00 58.86  ? 302 ASN   B N   1 
ATOM   3830 C CA  . ASN   B 1 228 ? 12.597  34.221  12.131 1.00 55.35  ? 302 ASN   B CA  1 
ATOM   3831 C C   . ASN   B 1 228 ? 13.787  34.813  12.882 1.00 57.32  ? 302 ASN   B C   1 
ATOM   3832 O O   . ASN   B 1 228 ? 14.701  34.108  13.312 1.00 62.62  ? 302 ASN   B O   1 
ATOM   3833 C CB  . ASN   B 1 228 ? 12.797  32.731  11.850 1.00 52.99  ? 302 ASN   B CB  1 
ATOM   3834 C CG  . ASN   B 1 228 ? 12.765  31.898  13.107 1.00 56.14  ? 302 ASN   B CG  1 
ATOM   3835 O OD1 . ASN   B 1 228 ? 12.090  32.248  14.077 1.00 55.77  ? 302 ASN   B OD1 1 
ATOM   3836 N ND2 . ASN   B 1 228 ? 13.508  30.794  13.108 1.00 57.30  ? 302 ASN   B ND2 1 
ATOM   3837 N N   . MET   B 1 229 ? 13.784  36.134  13.012 1.00 59.59  ? 303 MET   B N   1 
ATOM   3838 C CA  . MET   B 1 229 ? 14.812  36.832  13.763 1.00 66.10  ? 303 MET   B CA  1 
ATOM   3839 C C   . MET   B 1 229 ? 14.219  37.381  15.052 1.00 61.50  ? 303 MET   B C   1 
ATOM   3840 O O   . MET   B 1 229 ? 13.017  37.640  15.143 1.00 61.45  ? 303 MET   B O   1 
ATOM   3841 C CB  . MET   B 1 229 ? 15.437  37.967  12.944 1.00 69.70  ? 303 MET   B CB  1 
ATOM   3842 C CG  . MET   B 1 229 ? 14.555  39.184  12.738 1.00 65.88  ? 303 MET   B CG  1 
ATOM   3843 S SD  . MET   B 1 229 ? 15.400  40.453  11.757 1.00 81.83  ? 303 MET   B SD  1 
ATOM   3844 C CE  . MET   B 1 229 ? 16.923  40.639  12.687 1.00 83.27  ? 303 MET   B CE  1 
ATOM   3845 N N   . GLU   B 1 230 ? 15.076  37.544  16.052 1.00 61.21  ? 304 GLU   B N   1 
ATOM   3846 C CA  . GLU   B 1 230 ? 14.664  38.101  17.330 1.00 59.29  ? 304 GLU   B CA  1 
ATOM   3847 C C   . GLU   B 1 230 ? 14.901  39.606  17.335 1.00 59.63  ? 304 GLU   B C   1 
ATOM   3848 O O   . GLU   B 1 230 ? 16.013  40.068  17.057 1.00 64.59  ? 304 GLU   B O   1 
ATOM   3849 C CB  . GLU   B 1 230 ? 15.424  37.436  18.475 1.00 57.61  ? 304 GLU   B CB  1 
ATOM   3850 C CG  . GLU   B 1 230 ? 14.919  37.866  19.833 1.00 71.72  ? 304 GLU   B CG  1 
ATOM   3851 C CD  . GLU   B 1 230 ? 15.736  37.296  20.969 1.00 80.82  ? 304 GLU   B CD  1 
ATOM   3852 O OE1 . GLU   B 1 230 ? 16.675  36.515  20.696 1.00 85.97  ? 304 GLU   B OE1 1 
ATOM   3853 O OE2 . GLU   B 1 230 ? 15.435  37.635  22.136 1.00 88.96  ? 304 GLU   B OE2 1 
ATOM   3854 N N   . LEU   B 1 231 ? 13.853  40.367  17.650 1.00 59.49  ? 305 LEU   B N   1 
ATOM   3855 C CA  . LEU   B 1 231 ? 13.934  41.823  17.637 1.00 53.33  ? 305 LEU   B CA  1 
ATOM   3856 C C   . LEU   B 1 231 ? 14.628  42.330  18.899 1.00 54.16  ? 305 LEU   B C   1 
ATOM   3857 O O   . LEU   B 1 231 ? 14.318  41.874  20.003 1.00 55.45  ? 305 LEU   B O   1 
ATOM   3858 C CB  . LEU   B 1 231 ? 12.544  42.437  17.538 1.00 52.65  ? 305 LEU   B CB  1 
ATOM   3859 C CG  . LEU   B 1 231 ? 11.855  42.221  16.198 1.00 43.93  ? 305 LEU   B CG  1 
ATOM   3860 C CD1 . LEU   B 1 231 ? 10.603  43.057  16.129 1.00 44.07  ? 305 LEU   B CD1 1 
ATOM   3861 C CD2 . LEU   B 1 231 ? 12.801  42.568  15.064 1.00 49.02  ? 305 LEU   B CD2 1 
ATOM   3862 N N   . PRO   B 1 232 ? 15.556  43.272  18.762 1.00 53.59  ? 306 PRO   B N   1 
ATOM   3863 C CA  . PRO   B 1 232 ? 16.288  43.773  19.929 1.00 53.94  ? 306 PRO   B CA  1 
ATOM   3864 C C   . PRO   B 1 232 ? 15.479  44.785  20.723 1.00 52.78  ? 306 PRO   B C   1 
ATOM   3865 O O   . PRO   B 1 232 ? 14.615  45.481  20.188 1.00 49.51  ? 306 PRO   B O   1 
ATOM   3866 C CB  . PRO   B 1 232 ? 17.524  44.430  19.305 1.00 53.07  ? 306 PRO   B CB  1 
ATOM   3867 C CG  . PRO   B 1 232 ? 17.059  44.862  17.953 1.00 54.92  ? 306 PRO   B CG  1 
ATOM   3868 C CD  . PRO   B 1 232 ? 16.066  43.832  17.498 1.00 53.35  ? 306 PRO   B CD  1 
ATOM   3869 N N   . HIS   B 1 233 ? 15.780  44.862  22.024 1.00 57.59  ? 307 HIS   B N   1 
ATOM   3870 C CA  . HIS   B 1 233 ? 15.146  45.833  22.914 1.00 53.77  ? 307 HIS   B CA  1 
ATOM   3871 C C   . HIS   B 1 233 ? 15.826  47.195  22.890 1.00 53.78  ? 307 HIS   B C   1 
ATOM   3872 O O   . HIS   B 1 233 ? 15.160  48.214  23.093 1.00 57.74  ? 307 HIS   B O   1 
ATOM   3873 C CB  . HIS   B 1 233 ? 15.146  45.326  24.360 1.00 56.06  ? 307 HIS   B CB  1 
ATOM   3874 C CG  . HIS   B 1 233 ? 14.382  44.056  24.560 1.00 64.62  ? 307 HIS   B CG  1 
ATOM   3875 N ND1 . HIS   B 1 233 ? 14.982  42.813  24.529 1.00 64.86  ? 307 HIS   B ND1 1 
ATOM   3876 C CD2 . HIS   B 1 233 ? 13.066  43.835  24.802 1.00 62.40  ? 307 HIS   B CD2 1 
ATOM   3877 C CE1 . HIS   B 1 233 ? 14.068  41.881  24.741 1.00 64.13  ? 307 HIS   B CE1 1 
ATOM   3878 N NE2 . HIS   B 1 233 ? 12.898  42.474  24.911 1.00 70.97  ? 307 HIS   B NE2 1 
ATOM   3879 N N   . GLY   B 1 234 ? 17.130  47.230  22.672 1.00 52.86  ? 308 GLY   B N   1 
ATOM   3880 C CA  . GLY   B 1 234 ? 17.871  48.467  22.692 1.00 52.37  ? 308 GLY   B CA  1 
ATOM   3881 C C   . GLY   B 1 234 ? 19.212  48.274  22.024 1.00 62.36  ? 308 GLY   B C   1 
ATOM   3882 O O   . GLY   B 1 234 ? 19.377  47.382  21.193 1.00 65.84  ? 308 GLY   B O   1 
ATOM   3883 N N   . GLY   B 1 235 ? 20.172  49.120  22.399 1.00 66.05  ? 309 GLY   B N   1 
ATOM   3884 C CA  . GLY   B 1 235 ? 21.511  49.036  21.842 1.00 59.29  ? 309 GLY   B CA  1 
ATOM   3885 C C   . GLY   B 1 235 ? 21.546  49.287  20.345 1.00 63.65  ? 309 GLY   B C   1 
ATOM   3886 O O   . GLY   B 1 235 ? 20.528  49.626  19.730 1.00 59.70  ? 309 GLY   B O   1 
ATOM   3887 N N   . GLU   B 1 236 ? 22.731  49.110  19.741 1.00 68.39  ? 310 GLU   B N   1 
ATOM   3888 C CA  . GLU   B 1 236 ? 22.889  49.392  18.314 1.00 66.61  ? 310 GLU   B CA  1 
ATOM   3889 C C   . GLU   B 1 236 ? 22.030  48.479  17.450 1.00 62.87  ? 310 GLU   B C   1 
ATOM   3890 O O   . GLU   B 1 236 ? 21.656  48.855  16.332 1.00 62.45  ? 310 GLU   B O   1 
ATOM   3891 C CB  . GLU   B 1 236 ? 24.359  49.273  17.907 1.00 68.78  ? 310 GLU   B CB  1 
ATOM   3892 C CG  . GLU   B 1 236 ? 25.157  50.546  18.146 1.00 82.14  ? 310 GLU   B CG  1 
ATOM   3893 C CD  . GLU   B 1 236 ? 24.508  51.767  17.504 1.00 88.01  ? 310 GLU   B CD  1 
ATOM   3894 O OE1 . GLU   B 1 236 ? 24.082  51.675  16.331 1.00 85.58  ? 310 GLU   B OE1 1 
ATOM   3895 O OE2 . GLU   B 1 236 ? 24.415  52.816  18.179 1.00 92.62  ? 310 GLU   B OE2 1 
ATOM   3896 N N   . GLY   B 1 237 ? 21.709  47.282  17.940 1.00 61.25  ? 311 GLY   B N   1 
ATOM   3897 C CA  . GLY   B 1 237 ? 20.800  46.426  17.201 1.00 57.97  ? 311 GLY   B CA  1 
ATOM   3898 C C   . GLY   B 1 237 ? 19.459  47.093  16.977 1.00 55.22  ? 311 GLY   B C   1 
ATOM   3899 O O   . GLY   B 1 237 ? 18.927  47.097  15.865 1.00 58.64  ? 311 GLY   B O   1 
ATOM   3900 N N   . TRP   B 1 238 ? 18.905  47.683  18.036 1.00 57.67  ? 312 TRP   B N   1 
ATOM   3901 C CA  . TRP   B 1 238 ? 17.661  48.435  17.914 1.00 55.69  ? 312 TRP   B CA  1 
ATOM   3902 C C   . TRP   B 1 238 ? 17.824  49.607  16.955 1.00 56.92  ? 312 TRP   B C   1 
ATOM   3903 O O   . TRP   B 1 238 ? 16.905  49.938  16.199 1.00 51.47  ? 312 TRP   B O   1 
ATOM   3904 C CB  . TRP   B 1 238 ? 17.231  48.919  19.300 1.00 54.62  ? 312 TRP   B CB  1 
ATOM   3905 C CG  . TRP   B 1 238 ? 15.899  49.602  19.368 1.00 51.71  ? 312 TRP   B CG  1 
ATOM   3906 C CD1 . TRP   B 1 238 ? 14.699  49.036  19.703 1.00 44.18  ? 312 TRP   B CD1 1 
ATOM   3907 C CD2 . TRP   B 1 238 ? 15.636  50.988  19.121 1.00 53.46  ? 312 TRP   B CD2 1 
ATOM   3908 N NE1 . TRP   B 1 238 ? 13.704  49.984  19.666 1.00 47.52  ? 312 TRP   B NE1 1 
ATOM   3909 C CE2 . TRP   B 1 238 ? 14.251  51.190  19.310 1.00 52.00  ? 312 TRP   B CE2 1 
ATOM   3910 C CE3 . TRP   B 1 238 ? 16.435  52.076  18.750 1.00 51.71  ? 312 TRP   B CE3 1 
ATOM   3911 C CZ2 . TRP   B 1 238 ? 13.648  52.437  19.140 1.00 50.62  ? 312 TRP   B CZ2 1 
ATOM   3912 C CZ3 . TRP   B 1 238 ? 15.835  53.315  18.580 1.00 53.38  ? 312 TRP   B CZ3 1 
ATOM   3913 C CH2 . TRP   B 1 238 ? 14.453  53.484  18.774 1.00 51.55  ? 312 TRP   B CH2 1 
ATOM   3914 N N   . GLN   B 1 239 ? 19.000  50.235  16.967 1.00 58.92  ? 313 GLN   B N   1 
ATOM   3915 C CA  . GLN   B 1 239 ? 19.236  51.410  16.140 1.00 54.48  ? 313 GLN   B CA  1 
ATOM   3916 C C   . GLN   B 1 239 ? 19.322  51.042  14.664 1.00 58.38  ? 313 GLN   B C   1 
ATOM   3917 O O   . GLN   B 1 239 ? 18.867  51.805  13.802 1.00 63.37  ? 313 GLN   B O   1 
ATOM   3918 C CB  . GLN   B 1 239 ? 20.522  52.100  16.596 1.00 62.93  ? 313 GLN   B CB  1 
ATOM   3919 C CG  . GLN   B 1 239 ? 20.466  53.608  16.592 1.00 64.44  ? 313 GLN   B CG  1 
ATOM   3920 C CD  . GLN   B 1 239 ? 19.552  54.148  17.668 1.00 64.75  ? 313 GLN   B CD  1 
ATOM   3921 O OE1 . GLN   B 1 239 ? 18.590  54.864  17.378 1.00 73.29  ? 313 GLN   B OE1 1 
ATOM   3922 N NE2 . GLN   B 1 239 ? 19.845  53.809  18.921 1.00 53.31  ? 313 GLN   B NE2 1 
ATOM   3923 N N   . GLN   B 1 240 ? 19.896  49.875  14.353 1.00 58.23  ? 314 GLN   B N   1 
ATOM   3924 C CA  . GLN   B 1 240 ? 20.150  49.509  12.961 1.00 61.72  ? 314 GLN   B CA  1 
ATOM   3925 C C   . GLN   B 1 240 ? 18.870  49.194  12.199 1.00 61.62  ? 314 GLN   B C   1 
ATOM   3926 O O   . GLN   B 1 240 ? 18.833  49.338  10.971 1.00 67.58  ? 314 GLN   B O   1 
ATOM   3927 C CB  . GLN   B 1 240 ? 21.093  48.315  12.899 1.00 56.89  ? 314 GLN   B CB  1 
ATOM   3928 C CG  . GLN   B 1 240 ? 22.526  48.656  13.213 1.00 61.24  ? 314 GLN   B CG  1 
ATOM   3929 C CD  . GLN   B 1 240 ? 23.399  47.428  13.211 1.00 70.42  ? 314 GLN   B CD  1 
ATOM   3930 O OE1 . GLN   B 1 240 ? 22.901  46.302  13.272 1.00 71.73  ? 314 GLN   B OE1 1 
ATOM   3931 N NE2 . GLN   B 1 240 ? 24.710  47.630  13.132 1.00 70.62  ? 314 GLN   B NE2 1 
ATOM   3932 N N   . LEU   B 1 241 ? 17.828  48.746  12.894 1.00 55.53  ? 315 LEU   B N   1 
ATOM   3933 C CA  . LEU   B 1 241 ? 16.534  48.501  12.270 1.00 55.23  ? 315 LEU   B CA  1 
ATOM   3934 C C   . LEU   B 1 241 ? 15.733  49.775  12.058 1.00 57.38  ? 315 LEU   B C   1 
ATOM   3935 O O   . LEU   B 1 241 ? 14.589  49.699  11.598 1.00 54.69  ? 315 LEU   B O   1 
ATOM   3936 C CB  . LEU   B 1 241 ? 15.712  47.531  13.117 1.00 53.22  ? 315 LEU   B CB  1 
ATOM   3937 C CG  . LEU   B 1 241 ? 16.128  46.066  13.076 1.00 55.29  ? 315 LEU   B CG  1 
ATOM   3938 C CD1 . LEU   B 1 241 ? 15.413  45.299  14.167 1.00 53.93  ? 315 LEU   B CD1 1 
ATOM   3939 C CD2 . LEU   B 1 241 ? 15.801  45.484  11.718 1.00 61.25  ? 315 LEU   B CD2 1 
ATOM   3940 N N   . ARG   B 1 242 ? 16.293  50.939  12.386 1.00 59.22  ? 316 ARG   B N   1 
ATOM   3941 C CA  . ARG   B 1 242 ? 15.536  52.179  12.347 1.00 54.82  ? 316 ARG   B CA  1 
ATOM   3942 C C   . ARG   B 1 242 ? 16.273  53.257  11.572 1.00 59.46  ? 316 ARG   B C   1 
ATOM   3943 O O   . ARG   B 1 242 ? 16.079  54.448  11.818 1.00 59.12  ? 316 ARG   B O   1 
ATOM   3944 C CB  . ARG   B 1 242 ? 15.205  52.639  13.761 1.00 51.06  ? 316 ARG   B CB  1 
ATOM   3945 C CG  . ARG   B 1 242 ? 14.064  51.827  14.317 1.00 51.18  ? 316 ARG   B CG  1 
ATOM   3946 C CD  . ARG   B 1 242 ? 14.049  51.764  15.811 1.00 45.99  ? 316 ARG   B CD  1 
ATOM   3947 N NE  . ARG   B 1 242 ? 12.931  50.948  16.267 1.00 44.95  ? 316 ARG   B NE  1 
ATOM   3948 C CZ  . ARG   B 1 242 ? 13.010  49.651  16.537 1.00 47.95  ? 316 ARG   B CZ  1 
ATOM   3949 N NH1 . ARG   B 1 242 ? 14.148  48.985  16.406 1.00 47.91  ? 316 ARG   B NH1 1 
ATOM   3950 N NH2 . ARG   B 1 242 ? 11.924  49.009  16.963 1.00 44.84  ? 316 ARG   B NH2 1 
ATOM   3951 N N   . GLN   B 1 243 ? 17.110  52.847  10.621 1.00 64.76  ? 317 GLN   B N   1 
ATOM   3952 C CA  . GLN   B 1 243 ? 17.806  53.769  9.739  1.00 66.25  ? 317 GLN   B CA  1 
ATOM   3953 C C   . GLN   B 1 243 ? 17.259  53.750  8.321  1.00 68.60  ? 317 GLN   B C   1 
ATOM   3954 O O   . GLN   B 1 243 ? 17.769  54.482  7.470  1.00 70.60  ? 317 GLN   B O   1 
ATOM   3955 C CB  . GLN   B 1 243 ? 19.305  53.451  9.705  1.00 69.33  ? 317 GLN   B CB  1 
ATOM   3956 C CG  . GLN   B 1 243 ? 19.963  53.320  11.066 1.00 68.65  ? 317 GLN   B CG  1 
ATOM   3957 C CD  . GLN   B 1 243 ? 20.117  54.649  11.783 1.00 70.60  ? 317 GLN   B CD  1 
ATOM   3958 O OE1 . GLN   B 1 243 ? 19.609  54.829  12.892 1.00 73.01  ? 317 GLN   B OE1 1 
ATOM   3959 N NE2 . GLN   B 1 243 ? 20.836  55.583  11.160 1.00 72.40  ? 317 GLN   B NE2 1 
ATOM   3960 N N   . GLY   B 1 244 ? 16.252  52.927  8.037  1.00 73.75  ? 318 GLY   B N   1 
ATOM   3961 C CA  . GLY   B 1 244 ? 15.657  52.886  6.719  1.00 79.26  ? 318 GLY   B CA  1 
ATOM   3962 C C   . GLY   B 1 244 ? 16.220  51.845  5.776  1.00 85.29  ? 318 GLY   B C   1 
ATOM   3963 O O   . GLY   B 1 244 ? 15.739  51.737  4.639  1.00 86.66  ? 318 GLY   B O   1 
ATOM   3964 N N   . TYR   B 1 245 ? 17.225  51.085  6.197  1.00 87.95  ? 319 TYR   B N   1 
ATOM   3965 C CA  . TYR   B 1 245 ? 17.745  49.972  5.422  1.00 90.93  ? 319 TYR   B CA  1 
ATOM   3966 C C   . TYR   B 1 245 ? 17.463  48.669  6.158  1.00 93.81  ? 319 TYR   B C   1 
ATOM   3967 O O   . TYR   B 1 245 ? 17.399  48.634  7.391  1.00 93.33  ? 319 TYR   B O   1 
ATOM   3968 C CB  . TYR   B 1 245 ? 19.251  50.120  5.175  1.00 89.65  ? 319 TYR   B CB  1 
ATOM   3969 C CG  . TYR   B 1 245 ? 20.088  49.938  6.420  1.00 92.00  ? 319 TYR   B CG  1 
ATOM   3970 C CD1 . TYR   B 1 245 ? 20.303  50.994  7.293  1.00 91.99  ? 319 TYR   B CD1 1 
ATOM   3971 C CD2 . TYR   B 1 245 ? 20.662  48.709  6.724  1.00 96.10  ? 319 TYR   B CD2 1 
ATOM   3972 C CE1 . TYR   B 1 245 ? 21.068  50.833  8.438  1.00 94.44  ? 319 TYR   B CE1 1 
ATOM   3973 C CE2 . TYR   B 1 245 ? 21.427  48.536  7.868  1.00 98.07  ? 319 TYR   B CE2 1 
ATOM   3974 C CZ  . TYR   B 1 245 ? 21.627  49.603  8.723  1.00 95.79  ? 319 TYR   B CZ  1 
ATOM   3975 O OH  . TYR   B 1 245 ? 22.388  49.448  9.864  1.00 90.79  ? 319 TYR   B OH  1 
ATOM   3976 N N   . LEU   B 1 246 ? 17.288  47.599  5.399  1.00 90.09  ? 320 LEU   B N   1 
ATOM   3977 C CA  . LEU   B 1 246 ? 17.121  46.292  6.022  1.00 89.33  ? 320 LEU   B CA  1 
ATOM   3978 C C   . LEU   B 1 246 ? 18.489  45.688  6.319  1.00 93.18  ? 320 LEU   B C   1 
ATOM   3979 O O   . LEU   B 1 246 ? 19.382  45.747  5.466  1.00 96.46  ? 320 LEU   B O   1 
ATOM   3980 C CB  . LEU   B 1 246 ? 16.323  45.355  5.120  1.00 87.88  ? 320 LEU   B CB  1 
ATOM   3981 C CG  . LEU   B 1 246 ? 14.936  45.815  4.667  1.00 80.81  ? 320 LEU   B CG  1 
ATOM   3982 C CD1 . LEU   B 1 246 ? 14.222  44.702  3.921  1.00 79.34  ? 320 LEU   B CD1 1 
ATOM   3983 C CD2 . LEU   B 1 246 ? 14.111  46.278  5.847  1.00 75.03  ? 320 LEU   B CD2 1 
ATOM   3984 N N   . PRO   B 1 247 ? 18.700  45.136  7.512  1.00 93.00  ? 321 PRO   B N   1 
ATOM   3985 C CA  . PRO   B 1 247 ? 19.948  44.405  7.794  1.00 92.58  ? 321 PRO   B CA  1 
ATOM   3986 C C   . PRO   B 1 247 ? 20.158  43.282  6.794  1.00 94.95  ? 321 PRO   B C   1 
ATOM   3987 O O   . PRO   B 1 247 ? 19.387  42.310  6.766  1.00 96.36  ? 321 PRO   B O   1 
ATOM   3988 C CB  . PRO   B 1 247 ? 19.719  43.860  9.211  1.00 92.45  ? 321 PRO   B CB  1 
ATOM   3989 C CG  . PRO   B 1 247 ? 18.792  44.860  9.830  1.00 86.16  ? 321 PRO   B CG  1 
ATOM   3990 C CD  . PRO   B 1 247 ? 17.880  45.324  8.721  1.00 84.26  ? 321 PRO   B CD  1 
ATOM   3991 N N   . PRO   B 1 248 ? 21.211  43.367  5.974  1.00 95.05  ? 322 PRO   B N   1 
ATOM   3992 C CA  . PRO   B 1 248 ? 21.301  42.522  4.770  1.00 94.81  ? 322 PRO   B CA  1 
ATOM   3993 C C   . PRO   B 1 248 ? 21.488  41.037  5.038  1.00 94.85  ? 322 PRO   B C   1 
ATOM   3994 O O   . PRO   B 1 248 ? 21.585  40.266  4.075  1.00 90.37  ? 322 PRO   B O   1 
ATOM   3995 C CB  . PRO   B 1 248 ? 22.523  43.097  4.041  1.00 89.13  ? 322 PRO   B CB  1 
ATOM   3996 C CG  . PRO   B 1 248 ? 23.371  43.641  5.142  1.00 90.41  ? 322 PRO   B CG  1 
ATOM   3997 C CD  . PRO   B 1 248 ? 22.407  44.209  6.148  1.00 89.87  ? 322 PRO   B CD  1 
ATOM   3998 N N   . GLU   B 1 249 ? 21.541  40.601  6.296  1.00 94.68  ? 323 GLU   B N   1 
ATOM   3999 C CA  . GLU   B 1 249 ? 21.759  39.183  6.581  1.00 94.31  ? 323 GLU   B CA  1 
ATOM   4000 C C   . GLU   B 1 249 ? 20.454  38.393  6.503  1.00 99.84  ? 323 GLU   B C   1 
ATOM   4001 O O   . GLU   B 1 249 ? 20.258  37.587  5.587  1.00 98.31  ? 323 GLU   B O   1 
ATOM   4002 C CB  . GLU   B 1 249 ? 22.423  39.024  7.953  1.00 94.73  ? 323 GLU   B CB  1 
ATOM   4003 C CG  . GLU   B 1 249 ? 21.920  39.994  9.009  1.00 97.63  ? 323 GLU   B CG  1 
ATOM   4004 C CD  . GLU   B 1 249 ? 22.347  39.592  10.406 1.00 106.32 ? 323 GLU   B CD  1 
ATOM   4005 O OE1 . GLU   B 1 249 ? 23.182  38.669  10.521 1.00 106.22 ? 323 GLU   B OE1 1 
ATOM   4006 O OE2 . GLU   B 1 249 ? 21.846  40.189  11.385 1.00 111.79 ? 323 GLU   B OE2 1 
ATOM   4007 N N   . PHE   B 1 250 ? 19.548  38.618  7.463  1.00 101.27 ? 324 PHE   B N   1 
ATOM   4008 C CA  . PHE   B 1 250 ? 18.299  37.861  7.509  1.00 98.59  ? 324 PHE   B CA  1 
ATOM   4009 C C   . PHE   B 1 250 ? 17.432  38.121  6.284  1.00 98.82  ? 324 PHE   B C   1 
ATOM   4010 O O   . PHE   B 1 250 ? 16.703  37.226  5.840  1.00 98.69  ? 324 PHE   B O   1 
ATOM   4011 C CB  . PHE   B 1 250 ? 17.519  38.203  8.779  1.00 96.01  ? 324 PHE   B CB  1 
ATOM   4012 C CG  . PHE   B 1 250 ? 18.106  37.620  10.036 1.00 99.76  ? 324 PHE   B CG  1 
ATOM   4013 C CD1 . PHE   B 1 250 ? 19.056  38.320  10.765 1.00 103.81 ? 324 PHE   B CD1 1 
ATOM   4014 C CD2 . PHE   B 1 250 ? 17.693  36.381  10.498 1.00 94.36  ? 324 PHE   B CD2 1 
ATOM   4015 C CE1 . PHE   B 1 250 ? 19.590  37.788  11.930 1.00 104.93 ? 324 PHE   B CE1 1 
ATOM   4016 C CE2 . PHE   B 1 250 ? 18.222  35.843  11.661 1.00 97.04  ? 324 PHE   B CE2 1 
ATOM   4017 C CZ  . PHE   B 1 250 ? 19.173  36.548  12.377 1.00 103.08 ? 324 PHE   B CZ  1 
ATOM   4018 N N   . THR   B 1 251 ? 17.503  39.327  5.722  1.00 95.48  ? 325 THR   B N   1 
ATOM   4019 C CA  . THR   B 1 251 ? 16.658  39.693  4.593  1.00 92.58  ? 325 THR   B CA  1 
ATOM   4020 C C   . THR   B 1 251 ? 17.036  38.981  3.299  1.00 89.19  ? 325 THR   B C   1 
ATOM   4021 O O   . THR   B 1 251 ? 16.349  39.174  2.290  1.00 90.41  ? 325 THR   B O   1 
ATOM   4022 C CB  . THR   B 1 251 ? 16.711  41.207  4.378  1.00 95.54  ? 325 THR   B CB  1 
ATOM   4023 O OG1 . THR   B 1 251 ? 15.618  41.609  3.544  1.00 96.39  ? 325 THR   B OG1 1 
ATOM   4024 C CG2 . THR   B 1 251 ? 18.022  41.606  3.711  1.00 92.65  ? 325 THR   B CG2 1 
ATOM   4025 N N   . ALA   B 1 252 ? 18.094  38.165  3.297  1.00 90.09  ? 326 ALA   B N   1 
ATOM   4026 C CA  . ALA   B 1 252 ? 18.542  37.541  2.055  1.00 92.20  ? 326 ALA   B CA  1 
ATOM   4027 C C   . ALA   B 1 252 ? 17.488  36.595  1.494  1.00 90.14  ? 326 ALA   B C   1 
ATOM   4028 O O   . ALA   B 1 252 ? 17.276  36.541  0.275  1.00 89.37  ? 326 ALA   B O   1 
ATOM   4029 C CB  . ALA   B 1 252 ? 19.859  36.800  2.286  1.00 92.95  ? 326 ALA   B CB  1 
ATOM   4030 N N   . GLY   B 1 253 ? 16.812  35.844  2.367  1.00 92.09  ? 327 GLY   B N   1 
ATOM   4031 C CA  . GLY   B 1 253 ? 15.823  34.882  1.913  1.00 84.93  ? 327 GLY   B CA  1 
ATOM   4032 C C   . GLY   B 1 253 ? 14.584  35.506  1.306  1.00 77.02  ? 327 GLY   B C   1 
ATOM   4033 O O   . GLY   B 1 253 ? 13.912  34.857  0.498  1.00 78.87  ? 327 GLY   B O   1 
ATOM   4034 N N   . LEU   B 1 254 ? 14.267  36.744  1.674  1.00 77.50  ? 328 LEU   B N   1 
ATOM   4035 C CA  . LEU   B 1 254 ? 13.048  37.386  1.200  1.00 74.77  ? 328 LEU   B CA  1 
ATOM   4036 C C   . LEU   B 1 254 ? 13.091  37.616  -0.309 1.00 82.08  ? 328 LEU   B C   1 
ATOM   4037 O O   . LEU   B 1 254 ? 14.149  37.596  -0.946 1.00 87.48  ? 328 LEU   B O   1 
ATOM   4038 C CB  . LEU   B 1 254 ? 12.828  38.720  1.910  1.00 75.59  ? 328 LEU   B CB  1 
ATOM   4039 C CG  . LEU   B 1 254 ? 12.785  38.637  3.431  1.00 75.38  ? 328 LEU   B CG  1 
ATOM   4040 C CD1 . LEU   B 1 254 ? 12.228  39.933  3.995  1.00 72.19  ? 328 LEU   B CD1 1 
ATOM   4041 C CD2 . LEU   B 1 254 ? 11.960  37.433  3.874  1.00 66.77  ? 328 LEU   B CD2 1 
ATOM   4042 N N   . SER   B 1 255 ? 11.912  37.835  -0.879 1.00 76.29  ? 329 SER   B N   1 
ATOM   4043 C CA  . SER   B 1 255 ? 11.796  38.137  -2.293 1.00 74.87  ? 329 SER   B CA  1 
ATOM   4044 C C   . SER   B 1 255 ? 11.954  39.635  -2.520 1.00 78.41  ? 329 SER   B C   1 
ATOM   4045 O O   . SER   B 1 255 ? 11.892  40.444  -1.592 1.00 74.36  ? 329 SER   B O   1 
ATOM   4046 C CB  . SER   B 1 255 ? 10.453  37.655  -2.833 1.00 73.75  ? 329 SER   B CB  1 
ATOM   4047 O OG  . SER   B 1 255 ? 9.393   38.346  -2.198 1.00 70.65  ? 329 SER   B OG  1 
ATOM   4048 N N   . SER   B 1 256 ? 12.156  40.000  -3.786 1.00 75.26  ? 330 SER   B N   1 
ATOM   4049 C CA  . SER   B 1 256 ? 12.299  41.409  -4.136 1.00 74.20  ? 330 SER   B CA  1 
ATOM   4050 C C   . SER   B 1 256 ? 11.061  42.213  -3.753 1.00 72.82  ? 330 SER   B C   1 
ATOM   4051 O O   . SER   B 1 256 ? 11.173  43.355  -3.289 1.00 75.44  ? 330 SER   B O   1 
ATOM   4052 C CB  . SER   B 1 256 ? 12.575  41.545  -5.629 1.00 78.00  ? 330 SER   B CB  1 
ATOM   4053 O OG  . SER   B 1 256 ? 12.420  42.891  -6.032 1.00 78.05  ? 330 SER   B OG  1 
ATOM   4054 N N   . GLU   B 1 257 ? 9.871   41.636  -3.943 1.00 73.58  ? 331 GLU   B N   1 
ATOM   4055 C CA  . GLU   B 1 257 ? 8.637   42.372  -3.685 1.00 70.68  ? 331 GLU   B CA  1 
ATOM   4056 C C   . GLU   B 1 257 ? 8.440   42.618  -2.195 1.00 69.91  ? 331 GLU   B C   1 
ATOM   4057 O O   . GLU   B 1 257 ? 8.208   43.756  -1.767 1.00 71.61  ? 331 GLU   B O   1 
ATOM   4058 C CB  . GLU   B 1 257 ? 7.440   41.617  -4.267 1.00 69.19  ? 331 GLU   B CB  1 
ATOM   4059 C CG  . GLU   B 1 257 ? 7.483   41.435  -5.782 1.00 82.15  ? 331 GLU   B CG  1 
ATOM   4060 C CD  . GLU   B 1 257 ? 8.098   40.111  -6.214 1.00 80.15  ? 331 GLU   B CD  1 
ATOM   4061 O OE1 . GLU   B 1 257 ? 8.289   39.223  -5.356 1.00 83.14  ? 331 GLU   B OE1 1 
ATOM   4062 O OE2 . GLU   B 1 257 ? 8.384   39.955  -7.421 1.00 90.14  ? 331 GLU   B OE2 1 
ATOM   4063 N N   . LEU   B 1 258 ? 8.521   41.560  -1.386 1.00 73.24  ? 332 LEU   B N   1 
ATOM   4064 C CA  . LEU   B 1 258 ? 8.325   41.717  0.052  1.00 66.85  ? 332 LEU   B CA  1 
ATOM   4065 C C   . LEU   B 1 258 ? 9.366   42.653  0.651  1.00 66.83  ? 332 LEU   B C   1 
ATOM   4066 O O   . LEU   B 1 258 ? 9.063   43.440  1.556  1.00 69.90  ? 332 LEU   B O   1 
ATOM   4067 C CB  . LEU   B 1 258 ? 8.377   40.354  0.736  1.00 66.04  ? 332 LEU   B CB  1 
ATOM   4068 C CG  . LEU   B 1 258 ? 8.131   40.380  2.237  1.00 59.49  ? 332 LEU   B CG  1 
ATOM   4069 C CD1 . LEU   B 1 258 ? 6.760   40.967  2.515  1.00 60.17  ? 332 LEU   B CD1 1 
ATOM   4070 C CD2 . LEU   B 1 258 ? 8.256   38.982  2.819  1.00 65.87  ? 332 LEU   B CD2 1 
ATOM   4071 N N   . ARG   B 1 259 ? 10.603  42.576  0.159  1.00 66.52  ? 333 ARG   B N   1 
ATOM   4072 C CA  . ARG   B 1 259 ? 11.641  43.492  0.613  1.00 66.91  ? 333 ARG   B CA  1 
ATOM   4073 C C   . ARG   B 1 259 ? 11.269  44.935  0.296  1.00 69.95  ? 333 ARG   B C   1 
ATOM   4074 O O   . ARG   B 1 259 ? 11.473  45.836  1.118  1.00 68.68  ? 333 ARG   B O   1 
ATOM   4075 C CB  . ARG   B 1 259 ? 12.971  43.109  -0.033 1.00 73.90  ? 333 ARG   B CB  1 
ATOM   4076 C CG  . ARG   B 1 259 ? 14.153  43.941  0.403  1.00 79.37  ? 333 ARG   B CG  1 
ATOM   4077 C CD  . ARG   B 1 259 ? 15.360  43.057  0.662  1.00 85.16  ? 333 ARG   B CD  1 
ATOM   4078 N NE  . ARG   B 1 259 ? 15.531  42.040  -0.369 1.00 85.39  ? 333 ARG   B NE  1 
ATOM   4079 C CZ  . ARG   B 1 259 ? 16.511  41.146  -0.377 1.00 91.57  ? 333 ARG   B CZ  1 
ATOM   4080 N NH1 . ARG   B 1 259 ? 17.424  41.116  0.579  1.00 95.12  ? 333 ARG   B NH1 1 
ATOM   4081 N NH2 . ARG   B 1 259 ? 16.577  40.262  -1.371 1.00 85.87  ? 333 ARG   B NH2 1 
ATOM   4082 N N   . SER   B 1 260 ? 10.704  45.167  -0.889 1.00 70.22  ? 334 SER   B N   1 
ATOM   4083 C CA  . SER   B 1 260 ? 10.252  46.505  -1.255 1.00 65.39  ? 334 SER   B CA  1 
ATOM   4084 C C   . SER   B 1 260 ? 9.177   47.005  -0.296 1.00 66.03  ? 334 SER   B C   1 
ATOM   4085 O O   . SER   B 1 260 ? 9.228   48.149  0.168  1.00 67.03  ? 334 SER   B O   1 
ATOM   4086 C CB  . SER   B 1 260 ? 9.738   46.497  -2.696 1.00 69.79  ? 334 SER   B CB  1 
ATOM   4087 O OG  . SER   B 1 260 ? 9.374   47.793  -3.131 1.00 76.00  ? 334 SER   B OG  1 
ATOM   4088 N N   . VAL   B 1 261 ? 8.196   46.155  0.024  1.00 66.42  ? 335 VAL   B N   1 
ATOM   4089 C CA  . VAL   B 1 261 ? 7.124   46.577  0.922  1.00 65.15  ? 335 VAL   B CA  1 
ATOM   4090 C C   . VAL   B 1 261 ? 7.690   46.915  2.295  1.00 63.07  ? 335 VAL   B C   1 
ATOM   4091 O O   . VAL   B 1 261 ? 7.306   47.916  2.912  1.00 61.82  ? 335 VAL   B O   1 
ATOM   4092 C CB  . VAL   B 1 261 ? 6.028   45.496  1.006  1.00 61.27  ? 335 VAL   B CB  1 
ATOM   4093 C CG1 . VAL   B 1 261 ? 5.029   45.830  2.102  1.00 61.19  ? 335 VAL   B CG1 1 
ATOM   4094 C CG2 . VAL   B 1 261 ? 5.304   45.369  -0.315 1.00 60.77  ? 335 VAL   B CG2 1 
ATOM   4095 N N   . LEU   B 1 262 ? 8.631   46.103  2.784  1.00 64.85  ? 336 LEU   B N   1 
ATOM   4096 C CA  . LEU   B 1 262 ? 9.172   46.311  4.126  1.00 65.32  ? 336 LEU   B CA  1 
ATOM   4097 C C   . LEU   B 1 262 ? 9.966   47.610  4.223  1.00 67.09  ? 336 LEU   B C   1 
ATOM   4098 O O   . LEU   B 1 262 ? 9.927   48.287  5.258  1.00 60.09  ? 336 LEU   B O   1 
ATOM   4099 C CB  . LEU   B 1 262 ? 10.039  45.122  4.528  1.00 59.63  ? 336 LEU   B CB  1 
ATOM   4100 C CG  . LEU   B 1 262 ? 9.257   43.885  4.951  1.00 59.69  ? 336 LEU   B CG  1 
ATOM   4101 C CD1 . LEU   B 1 262 ? 10.213  42.733  5.168  1.00 63.29  ? 336 LEU   B CD1 1 
ATOM   4102 C CD2 . LEU   B 1 262 ? 8.457   44.175  6.215  1.00 55.49  ? 336 LEU   B CD2 1 
ATOM   4103 N N   . VAL   B 1 263 ? 10.702  47.971  3.166  1.00 62.17  ? 337 VAL   B N   1 
ATOM   4104 C CA  . VAL   B 1 263 ? 11.450  49.226  3.181  1.00 59.60  ? 337 VAL   B CA  1 
ATOM   4105 C C   . VAL   B 1 263 ? 10.497  50.410  3.283  1.00 61.84  ? 337 VAL   B C   1 
ATOM   4106 O O   . VAL   B 1 263 ? 10.776  51.393  3.982  1.00 61.81  ? 337 VAL   B O   1 
ATOM   4107 C CB  . VAL   B 1 263 ? 12.354  49.329  1.940  1.00 60.80  ? 337 VAL   B CB  1 
ATOM   4108 C CG1 . VAL   B 1 263 ? 12.879  50.743  1.781  1.00 55.07  ? 337 VAL   B CG1 1 
ATOM   4109 C CG2 . VAL   B 1 263 ? 13.501  48.348  2.051  1.00 64.18  ? 337 VAL   B CG2 1 
ATOM   4110 N N   . MET   B 1 264 ? 9.357   50.337  2.591  1.00 60.69  ? 338 MET   B N   1 
ATOM   4111 C CA  . MET   B 1 264 ? 8.353   51.388  2.718  1.00 58.31  ? 338 MET   B CA  1 
ATOM   4112 C C   . MET   B 1 264 ? 7.796   51.443  4.130  1.00 56.15  ? 338 MET   B C   1 
ATOM   4113 O O   . MET   B 1 264 ? 7.612   52.528  4.692  1.00 60.11  ? 338 MET   B O   1 
ATOM   4114 C CB  . MET   B 1 264 ? 7.221   51.170  1.716  1.00 58.92  ? 338 MET   B CB  1 
ATOM   4115 C CG  . MET   B 1 264 ? 7.673   51.159  0.270  1.00 68.63  ? 338 MET   B CG  1 
ATOM   4116 S SD  . MET   B 1 264 ? 6.315   50.831  -0.872 1.00 80.36  ? 338 MET   B SD  1 
ATOM   4117 C CE  . MET   B 1 264 ? 5.579   52.461  -0.993 1.00 76.19  ? 338 MET   B CE  1 
ATOM   4118 N N   . MET   B 1 265 ? 7.532   50.279  4.725  1.00 60.93  ? 339 MET   B N   1 
ATOM   4119 C CA  . MET   B 1 265 ? 6.918   50.242  6.048  1.00 56.89  ? 339 MET   B CA  1 
ATOM   4120 C C   . MET   B 1 265 ? 7.886   50.684  7.133  1.00 54.23  ? 339 MET   B C   1 
ATOM   4121 O O   . MET   B 1 265 ? 7.465   51.292  8.122  1.00 54.64  ? 339 MET   B O   1 
ATOM   4122 C CB  . MET   B 1 265 ? 6.395   48.837  6.341  1.00 51.33  ? 339 MET   B CB  1 
ATOM   4123 C CG  . MET   B 1 265 ? 5.384   48.362  5.312  1.00 55.72  ? 339 MET   B CG  1 
ATOM   4124 S SD  . MET   B 1 265 ? 4.532   46.843  5.750  1.00 55.37  ? 339 MET   B SD  1 
ATOM   4125 C CE  . MET   B 1 265 ? 3.766   47.332  7.281  1.00 47.13  ? 339 MET   B CE  1 
ATOM   4126 N N   . LEU   B 1 266 ? 9.176   50.392  6.970  1.00 57.30  ? 340 LEU   B N   1 
ATOM   4127 C CA  . LEU   B 1 266 ? 10.184  50.706  7.974  1.00 55.73  ? 340 LEU   B CA  1 
ATOM   4128 C C   . LEU   B 1 266 ? 10.836  52.060  7.743  1.00 54.57  ? 340 LEU   B C   1 
ATOM   4129 O O   . LEU   B 1 266 ? 11.894  52.334  8.321  1.00 58.96  ? 340 LEU   B O   1 
ATOM   4130 C CB  . LEU   B 1 266 ? 11.244  49.604  8.016  1.00 50.28  ? 340 LEU   B CB  1 
ATOM   4131 C CG  . LEU   B 1 266 ? 10.687  48.242  8.419  1.00 47.88  ? 340 LEU   B CG  1 
ATOM   4132 C CD1 . LEU   B 1 266 ? 11.770  47.182  8.442  1.00 50.34  ? 340 LEU   B CD1 1 
ATOM   4133 C CD2 . LEU   B 1 266 ? 10.011  48.351  9.776  1.00 49.86  ? 340 LEU   B CD2 1 
ATOM   4134 N N   . GLU   B 1 267 ? 10.235  52.900  6.912  1.00 59.93  ? 341 GLU   B N   1 
ATOM   4135 C CA  . GLU   B 1 267 ? 10.760  54.237  6.685  1.00 58.31  ? 341 GLU   B CA  1 
ATOM   4136 C C   . GLU   B 1 267 ? 10.794  55.002  8.005  1.00 56.30  ? 341 GLU   B C   1 
ATOM   4137 O O   . GLU   B 1 267 ? 9.775   55.064  8.704  1.00 58.24  ? 341 GLU   B O   1 
ATOM   4138 C CB  . GLU   B 1 267 ? 9.891   54.967  5.663  1.00 54.74  ? 341 GLU   B CB  1 
ATOM   4139 C CG  . GLU   B 1 267 ? 9.954   56.477  5.745  1.00 60.60  ? 341 GLU   B CG  1 
ATOM   4140 C CD  . GLU   B 1 267 ? 11.252  57.046  5.212  1.00 65.18  ? 341 GLU   B CD  1 
ATOM   4141 O OE1 . GLU   B 1 267 ? 11.725  56.576  4.150  1.00 68.33  ? 341 GLU   B OE1 1 
ATOM   4142 O OE2 . GLU   B 1 267 ? 11.799  57.967  5.857  1.00 68.45  ? 341 GLU   B OE2 1 
ATOM   4143 N N   . PRO   B 1 268 ? 11.935  55.584  8.387  1.00 56.91  ? 342 PRO   B N   1 
ATOM   4144 C CA  . PRO   B 1 268 ? 12.021  56.184  9.729  1.00 58.14  ? 342 PRO   B CA  1 
ATOM   4145 C C   . PRO   B 1 268 ? 11.197  57.449  9.885  1.00 60.53  ? 342 PRO   B C   1 
ATOM   4146 O O   . PRO   B 1 268 ? 10.653  57.689  10.970 1.00 56.72  ? 342 PRO   B O   1 
ATOM   4147 C CB  . PRO   B 1 268 ? 13.523  56.462  9.896  1.00 59.95  ? 342 PRO   B CB  1 
ATOM   4148 C CG  . PRO   B 1 268 ? 14.205  55.685  8.797  1.00 62.07  ? 342 PRO   B CG  1 
ATOM   4149 C CD  . PRO   B 1 268 ? 13.222  55.627  7.678  1.00 62.81  ? 342 PRO   B CD  1 
ATOM   4150 N N   . ASP   B 1 269 ? 11.090  58.273  8.839  1.00 62.88  ? 343 ASP   B N   1 
ATOM   4151 C CA  . ASP   B 1 269 ? 10.371  59.540  8.931  1.00 60.96  ? 343 ASP   B CA  1 
ATOM   4152 C C   . ASP   B 1 269 ? 8.866   59.311  8.796  1.00 61.70  ? 343 ASP   B C   1 
ATOM   4153 O O   . ASP   B 1 269 ? 8.393   58.957  7.708  1.00 62.06  ? 343 ASP   B O   1 
ATOM   4154 C CB  . ASP   B 1 269 ? 10.865  60.509  7.853  1.00 60.59  ? 343 ASP   B CB  1 
ATOM   4155 C CG  . ASP   B 1 269 ? 10.514  61.954  8.159  1.00 65.49  ? 343 ASP   B CG  1 
ATOM   4156 O OD1 . ASP   B 1 269 ? 9.548   62.187  8.918  1.00 65.65  ? 343 ASP   B OD1 1 
ATOM   4157 O OD2 . ASP   B 1 269 ? 11.205  62.861  7.640  1.00 68.28  ? 343 ASP   B OD2 1 
ATOM   4158 N N   . PRO   B 1 270 ? 8.081   59.519  9.861  1.00 62.05  ? 344 PRO   B N   1 
ATOM   4159 C CA  . PRO   B 1 270 ? 6.635   59.256  9.760  1.00 58.90  ? 344 PRO   B CA  1 
ATOM   4160 C C   . PRO   B 1 270 ? 5.938   60.115  8.723  1.00 61.56  ? 344 PRO   B C   1 
ATOM   4161 O O   . PRO   B 1 270 ? 4.889   59.711  8.204  1.00 63.00  ? 344 PRO   B O   1 
ATOM   4162 C CB  . PRO   B 1 270 ? 6.127   59.557  11.176 1.00 52.21  ? 344 PRO   B CB  1 
ATOM   4163 C CG  . PRO   B 1 270 ? 7.101   60.545  11.710 1.00 55.62  ? 344 PRO   B CG  1 
ATOM   4164 C CD  . PRO   B 1 270 ? 8.437   60.115  11.160 1.00 59.30  ? 344 PRO   B CD  1 
ATOM   4165 N N   . LYS   B 1 271 ? 6.489   61.289  8.402  1.00 65.67  ? 345 LYS   B N   1 
ATOM   4166 C CA  . LYS   B 1 271 ? 5.943   62.088  7.312  1.00 62.24  ? 345 LYS   B CA  1 
ATOM   4167 C C   . LYS   B 1 271 ? 6.074   61.373  5.978  1.00 63.90  ? 345 LYS   B C   1 
ATOM   4168 O O   . LYS   B 1 271 ? 5.256   61.587  5.075  1.00 65.34  ? 345 LYS   B O   1 
ATOM   4169 C CB  . LYS   B 1 271 ? 6.654   63.440  7.228  1.00 64.65  ? 345 LYS   B CB  1 
ATOM   4170 C CG  . LYS   B 1 271 ? 6.682   64.236  8.513  1.00 69.37  ? 345 LYS   B CG  1 
ATOM   4171 C CD  . LYS   B 1 271 ? 7.571   65.465  8.356  1.00 73.46  ? 345 LYS   B CD  1 
ATOM   4172 C CE  . LYS   B 1 271 ? 8.265   65.787  9.676  1.00 82.43  ? 345 LYS   B CE  1 
ATOM   4173 N NZ  . LYS   B 1 271 ? 8.743   64.538  10.372 1.00 66.62  ? 345 LYS   B NZ  1 
ATOM   4174 N N   . LEU   B 1 272 ? 7.106   60.545  5.824  1.00 64.22  ? 346 LEU   B N   1 
ATOM   4175 C CA  . LEU   B 1 272 ? 7.392   59.897  4.552  1.00 66.94  ? 346 LEU   B CA  1 
ATOM   4176 C C   . LEU   B 1 272 ? 6.984   58.432  4.541  1.00 63.21  ? 346 LEU   B C   1 
ATOM   4177 O O   . LEU   B 1 272 ? 7.142   57.764  3.516  1.00 64.66  ? 346 LEU   B O   1 
ATOM   4178 C CB  . LEU   B 1 272 ? 8.885   60.027  4.214  1.00 66.89  ? 346 LEU   B CB  1 
ATOM   4179 C CG  . LEU   B 1 272 ? 9.514   61.426  4.230  1.00 69.52  ? 346 LEU   B CG  1 
ATOM   4180 C CD1 . LEU   B 1 272 ? 11.022  61.345  4.038  1.00 72.27  ? 346 LEU   B CD1 1 
ATOM   4181 C CD2 . LEU   B 1 272 ? 8.891   62.321  3.172  1.00 71.21  ? 346 LEU   B CD2 1 
ATOM   4182 N N   . ARG   B 1 273 ? 6.457   57.923  5.649  1.00 62.50  ? 347 ARG   B N   1 
ATOM   4183 C CA  . ARG   B 1 273 ? 6.087   56.519  5.741  1.00 64.13  ? 347 ARG   B CA  1 
ATOM   4184 C C   . ARG   B 1 273 ? 4.760   56.268  5.035  1.00 63.68  ? 347 ARG   B C   1 
ATOM   4185 O O   . ARG   B 1 273 ? 3.826   57.070  5.130  1.00 60.13  ? 347 ARG   B O   1 
ATOM   4186 C CB  . ARG   B 1 273 ? 5.996   56.095  7.208  1.00 60.38  ? 347 ARG   B CB  1 
ATOM   4187 C CG  . ARG   B 1 273 ? 5.703   54.622  7.437  1.00 57.02  ? 347 ARG   B CG  1 
ATOM   4188 C CD  . ARG   B 1 273 ? 5.789   54.336  8.918  1.00 53.53  ? 347 ARG   B CD  1 
ATOM   4189 N NE  . ARG   B 1 273 ? 7.025   54.884  9.464  1.00 50.84  ? 347 ARG   B NE  1 
ATOM   4190 C CZ  . ARG   B 1 273 ? 7.163   55.351  10.696 1.00 50.59  ? 347 ARG   B CZ  1 
ATOM   4191 N NH1 . ARG   B 1 273 ? 6.153   55.359  11.550 1.00 50.03  ? 347 ARG   B NH1 1 
ATOM   4192 N NH2 . ARG   B 1 273 ? 8.343   55.830  11.078 1.00 51.61  ? 347 ARG   B NH2 1 
ATOM   4193 N N   . ALA   B 1 274 ? 4.689   55.148  4.319  1.00 66.03  ? 348 ALA   B N   1 
ATOM   4194 C CA  . ALA   B 1 274 ? 3.461   54.778  3.634  1.00 60.08  ? 348 ALA   B CA  1 
ATOM   4195 C C   . ALA   B 1 274 ? 2.335   54.563  4.636  1.00 62.02  ? 348 ALA   B C   1 
ATOM   4196 O O   . ALA   B 1 274 ? 2.561   54.225  5.802  1.00 62.22  ? 348 ALA   B O   1 
ATOM   4197 C CB  . ALA   B 1 274 ? 3.671   53.512  2.806  1.00 60.96  ? 348 ALA   B CB  1 
ATOM   4198 N N   . THR   B 1 275 ? 1.112   54.783  4.175  1.00 63.70  ? 349 THR   B N   1 
ATOM   4199 C CA  . THR   B 1 275 ? -0.070  54.483  4.960  1.00 57.99  ? 349 THR   B CA  1 
ATOM   4200 C C   . THR   B 1 275 ? -0.541  53.072  4.638  1.00 59.17  ? 349 THR   B C   1 
ATOM   4201 O O   . THR   B 1 275 ? -0.218  52.513  3.588  1.00 56.64  ? 349 THR   B O   1 
ATOM   4202 C CB  . THR   B 1 275 ? -1.175  55.493  4.663  1.00 58.89  ? 349 THR   B CB  1 
ATOM   4203 O OG1 . THR   B 1 275 ? -1.329  55.610  3.248  1.00 59.89  ? 349 THR   B OG1 1 
ATOM   4204 C CG2 . THR   B 1 275 ? -0.808  56.855  5.215  1.00 65.99  ? 349 THR   B CG2 1 
ATOM   4205 N N   . ALA   B 1 276 ? -1.297  52.485  5.567  1.00 56.61  ? 350 ALA   B N   1 
ATOM   4206 C CA  . ALA   B 1 276 ? -1.835  51.154  5.313  1.00 56.70  ? 350 ALA   B CA  1 
ATOM   4207 C C   . ALA   B 1 276 ? -2.767  51.169  4.114  1.00 56.10  ? 350 ALA   B C   1 
ATOM   4208 O O   . ALA   B 1 276 ? -2.776  50.231  3.308  1.00 59.96  ? 350 ALA   B O   1 
ATOM   4209 C CB  . ALA   B 1 276 ? -2.555  50.624  6.552  1.00 57.25  ? 350 ALA   B CB  1 
ATOM   4210 N N   . GLU   B 1 277 ? -3.550  52.238  3.969  1.00 57.65  ? 351 GLU   B N   1 
ATOM   4211 C CA  . GLU   B 1 277 ? -4.432  52.355  2.814  1.00 59.06  ? 351 GLU   B CA  1 
ATOM   4212 C C   . GLU   B 1 277 ? -3.631  52.463  1.523  1.00 58.78  ? 351 GLU   B C   1 
ATOM   4213 O O   . GLU   B 1 277 ? -4.040  51.939  0.480  1.00 59.26  ? 351 GLU   B O   1 
ATOM   4214 C CB  . GLU   B 1 277 ? -5.348  53.566  2.992  1.00 56.44  ? 351 GLU   B CB  1 
ATOM   4215 C CG  . GLU   B 1 277 ? -6.504  53.638  2.023  1.00 60.34  ? 351 GLU   B CG  1 
ATOM   4216 C CD  . GLU   B 1 277 ? -7.012  55.061  1.851  1.00 72.70  ? 351 GLU   B CD  1 
ATOM   4217 O OE1 . GLU   B 1 277 ? -6.705  55.908  2.717  1.00 78.05  ? 351 GLU   B OE1 1 
ATOM   4218 O OE2 . GLU   B 1 277 ? -7.705  55.338  0.847  1.00 75.85  ? 351 GLU   B OE2 1 
ATOM   4219 N N   . ALA   B 1 278 ? -2.479  53.136  1.571  1.00 60.39  ? 352 ALA   B N   1 
ATOM   4220 C CA  . ALA   B 1 278 ? -1.630  53.203  0.386  1.00 56.90  ? 352 ALA   B CA  1 
ATOM   4221 C C   . ALA   B 1 278 ? -1.017  51.845  0.073  1.00 61.41  ? 352 ALA   B C   1 
ATOM   4222 O O   . ALA   B 1 278 ? -0.953  51.442  -1.093 1.00 67.77  ? 352 ALA   B O   1 
ATOM   4223 C CB  . ALA   B 1 278 ? -0.538  54.258  0.571  1.00 56.96  ? 352 ALA   B CB  1 
ATOM   4224 N N   . LEU   B 1 279 ? -0.565  51.122  1.101  1.00 59.34  ? 353 LEU   B N   1 
ATOM   4225 C CA  . LEU   B 1 279 ? 0.042   49.815  0.876  1.00 57.64  ? 353 LEU   B CA  1 
ATOM   4226 C C   . LEU   B 1 279 ? -0.952  48.855  0.239  1.00 58.26  ? 353 LEU   B C   1 
ATOM   4227 O O   . LEU   B 1 279 ? -0.630  48.168  -0.737 1.00 64.64  ? 353 LEU   B O   1 
ATOM   4228 C CB  . LEU   B 1 279 ? 0.575   49.259  2.191  1.00 56.71  ? 353 LEU   B CB  1 
ATOM   4229 C CG  . LEU   B 1 279 ? 1.719   50.082  2.778  1.00 59.91  ? 353 LEU   B CG  1 
ATOM   4230 C CD1 . LEU   B 1 279 ? 2.107   49.560  4.152  1.00 58.32  ? 353 LEU   B CD1 1 
ATOM   4231 C CD2 . LEU   B 1 279 ? 2.911   50.077  1.832  1.00 64.28  ? 353 LEU   B CD2 1 
ATOM   4232 N N   . LEU   B 1 280 ? -2.185  48.828  0.754  1.00 59.37  ? 354 LEU   B N   1 
ATOM   4233 C CA  . LEU   B 1 280 ? -3.225  47.976  0.186  1.00 59.32  ? 354 LEU   B CA  1 
ATOM   4234 C C   . LEU   B 1 280 ? -3.533  48.316  -1.261 1.00 63.11  ? 354 LEU   B C   1 
ATOM   4235 O O   . LEU   B 1 280 ? -4.166  47.511  -1.950 1.00 73.18  ? 354 LEU   B O   1 
ATOM   4236 C CB  . LEU   B 1 280 ? -4.498  48.090  1.014  1.00 56.24  ? 354 LEU   B CB  1 
ATOM   4237 C CG  . LEU   B 1 280 ? -4.376  47.521  2.425  1.00 59.58  ? 354 LEU   B CG  1 
ATOM   4238 C CD1 . LEU   B 1 280 ? -5.507  48.018  3.302  1.00 55.71  ? 354 LEU   B CD1 1 
ATOM   4239 C CD2 . LEU   B 1 280 ? -4.372  46.010  2.362  1.00 58.27  ? 354 LEU   B CD2 1 
ATOM   4240 N N   . ALA   B 1 281 ? -3.122  49.487  -1.736 1.00 63.50  ? 355 ALA   B N   1 
ATOM   4241 C CA  . ALA   B 1 281 ? -3.317  49.841  -3.135 1.00 67.72  ? 355 ALA   B CA  1 
ATOM   4242 C C   . ALA   B 1 281 ? -2.191  49.350  -4.029 1.00 67.08  ? 355 ALA   B C   1 
ATOM   4243 O O   . ALA   B 1 281 ? -2.340  49.369  -5.256 1.00 73.61  ? 355 ALA   B O   1 
ATOM   4244 C CB  . ALA   B 1 281 ? -3.458  51.358  -3.285 1.00 68.27  ? 355 ALA   B CB  1 
ATOM   4245 N N   . LEU   B 1 282 ? -1.073  48.923  -3.450 1.00 69.20  ? 356 LEU   B N   1 
ATOM   4246 C CA  . LEU   B 1 282 ? 0.034   48.433  -4.249 1.00 69.90  ? 356 LEU   B CA  1 
ATOM   4247 C C   . LEU   B 1 282 ? -0.380  47.158  -4.981 1.00 75.13  ? 356 LEU   B C   1 
ATOM   4248 O O   . LEU   B 1 282 ? -1.235  46.407  -4.496 1.00 74.26  ? 356 LEU   B O   1 
ATOM   4249 C CB  . LEU   B 1 282 ? 1.253   48.170  -3.365 1.00 72.16  ? 356 LEU   B CB  1 
ATOM   4250 C CG  . LEU   B 1 282 ? 1.913   49.403  -2.739 1.00 68.51  ? 356 LEU   B CG  1 
ATOM   4251 C CD1 . LEU   B 1 282 ? 3.031   49.004  -1.781 1.00 65.03  ? 356 LEU   B CD1 1 
ATOM   4252 C CD2 . LEU   B 1 282 ? 2.434   50.354  -3.817 1.00 62.44  ? 356 LEU   B CD2 1 
ATOM   4253 N N   . PRO   B 1 283 ? 0.199   46.898  -6.159 1.00 73.84  ? 357 PRO   B N   1 
ATOM   4254 C CA  . PRO   B 1 283 ? -0.202  45.706  -6.926 1.00 75.47  ? 357 PRO   B CA  1 
ATOM   4255 C C   . PRO   B 1 283 ? -0.048  44.405  -6.157 1.00 77.38  ? 357 PRO   B C   1 
ATOM   4256 O O   . PRO   B 1 283 ? -0.870  43.494  -6.321 1.00 84.30  ? 357 PRO   B O   1 
ATOM   4257 C CB  . PRO   B 1 283 ? 0.727   45.752  -8.149 1.00 78.09  ? 357 PRO   B CB  1 
ATOM   4258 C CG  . PRO   B 1 283 ? 1.111   47.190  -8.289 1.00 75.33  ? 357 PRO   B CG  1 
ATOM   4259 C CD  . PRO   B 1 283 ? 1.188   47.719  -6.883 1.00 75.37  ? 357 PRO   B CD  1 
ATOM   4260 N N   . VAL   B 1 284 ? 0.973   44.294  -5.305 1.00 77.08  ? 358 VAL   B N   1 
ATOM   4261 C CA  . VAL   B 1 284 ? 1.213   43.050  -4.586 1.00 72.86  ? 358 VAL   B CA  1 
ATOM   4262 C C   . VAL   B 1 284 ? 0.170   42.782  -3.505 1.00 74.68  ? 358 VAL   B C   1 
ATOM   4263 O O   . VAL   B 1 284 ? 0.018   41.633  -3.076 1.00 77.53  ? 358 VAL   B O   1 
ATOM   4264 C CB  . VAL   B 1 284 ? 2.627   43.073  -3.975 1.00 73.87  ? 358 VAL   B CB  1 
ATOM   4265 C CG1 . VAL   B 1 284 ? 3.672   43.270  -5.059 1.00 70.06  ? 358 VAL   B CG1 1 
ATOM   4266 C CG2 . VAL   B 1 284 ? 2.734   44.177  -2.944 1.00 74.05  ? 358 VAL   B CG2 1 
ATOM   4267 N N   . LEU   B 1 285 ? -0.559  43.802  -3.048 1.00 78.30  ? 359 LEU   B N   1 
ATOM   4268 C CA  . LEU   B 1 285 ? -1.455  43.673  -1.902 1.00 80.54  ? 359 LEU   B CA  1 
ATOM   4269 C C   . LEU   B 1 285 ? -2.934  43.772  -2.272 1.00 86.77  ? 359 LEU   B C   1 
ATOM   4270 O O   . LEU   B 1 285 ? -3.787  43.767  -1.376 1.00 85.63  ? 359 LEU   B O   1 
ATOM   4271 C CB  . LEU   B 1 285 ? -1.107  44.727  -0.844 1.00 70.22  ? 359 LEU   B CB  1 
ATOM   4272 C CG  . LEU   B 1 285 ? 0.126   44.395  -0.003 1.00 66.54  ? 359 LEU   B CG  1 
ATOM   4273 C CD1 . LEU   B 1 285 ? 0.673   45.618  0.715  1.00 56.79  ? 359 LEU   B CD1 1 
ATOM   4274 C CD2 . LEU   B 1 285 ? -0.224  43.306  0.994  1.00 66.27  ? 359 LEU   B CD2 1 
ATOM   4275 N N   . ARG   B 1 286 ? -3.264  43.853  -3.560 1.00 91.15  ? 360 ARG   B N   1 
ATOM   4276 C CA  . ARG   B 1 286 ? -4.654  43.983  -3.997 1.00 94.77  ? 360 ARG   B CA  1 
ATOM   4277 C C   . ARG   B 1 286 ? -5.300  42.605  -4.052 1.00 100.54 ? 360 ARG   B C   1 
ATOM   4278 O O   . ARG   B 1 286 ? -5.056  41.830  -4.981 1.00 103.04 ? 360 ARG   B O   1 
ATOM   4279 C CB  . ARG   B 1 286 ? -4.728  44.659  -5.362 1.00 94.71  ? 360 ARG   B CB  1 
ATOM   4280 C CG  . ARG   B 1 286 ? -4.445  46.147  -5.365 1.00 91.50  ? 360 ARG   B CG  1 
ATOM   4281 C CD  . ARG   B 1 286 ? -4.626  46.684  -6.778 1.00 97.98  ? 360 ARG   B CD  1 
ATOM   4282 N NE  . ARG   B 1 286 ? -5.872  46.209  -7.372 1.00 112.37 ? 360 ARG   B NE  1 
ATOM   4283 C CZ  . ARG   B 1 286 ? -6.151  46.234  -8.670 1.00 115.22 ? 360 ARG   B CZ  1 
ATOM   4284 N NH1 . ARG   B 1 286 ? -5.280  46.690  -9.557 1.00 116.99 ? 360 ARG   B NH1 1 
ATOM   4285 N NH2 . ARG   B 1 286 ? -7.332  45.787  -9.090 1.00 109.77 ? 360 ARG   B NH2 1 
ATOM   4286 N N   . GLN   B 1 287 ? -6.142  42.307  -3.064 1.00 99.35  ? 361 GLN   B N   1 
ATOM   4287 C CA  . GLN   B 1 287 ? -6.907  41.057  -3.020 1.00 98.32  ? 361 GLN   B CA  1 
ATOM   4288 C C   . GLN   B 1 287 ? -6.018  39.818  -3.110 1.00 97.07  ? 361 GLN   B C   1 
ATOM   4289 O O   . GLN   B 1 287 ? -6.274  38.810  -2.449 1.00 96.13  ? 361 GLN   B O   1 
ATOM   4290 C CB  . GLN   B 1 287 ? -7.952  41.036  -4.143 1.00 99.42  ? 361 GLN   B CB  1 
ATOM   4291 C CG  . GLN   B 1 287 ? -8.638  39.683  -4.368 1.00 109.88 ? 361 GLN   B CG  1 
ATOM   4292 C CD  . GLN   B 1 287 ? -9.655  39.318  -3.287 1.00 107.79 ? 361 GLN   B CD  1 
ATOM   4293 O OE1 . GLN   B 1 287 ? -9.545  39.741  -2.133 1.00 100.31 ? 361 GLN   B OE1 1 
ATOM   4294 N NE2 . GLN   B 1 287 ? -10.654 38.524  -3.666 1.00 103.49 ? 361 GLN   B NE2 1 
HETATM 4295 C C10 . A1EJX C 2 .   ? 9.522   13.339  28.602 1.00 50.15  ? 401 A1EJX A C10 1 
HETATM 4296 C C11 . A1EJX C 2 .   ? 8.965   14.468  28.030 1.00 50.85  ? 401 A1EJX A C11 1 
HETATM 4297 C C13 . A1EJX C 2 .   ? 5.911   17.352  26.176 1.00 50.06  ? 401 A1EJX A C13 1 
HETATM 4298 C C15 . A1EJX C 2 .   ? 4.644   17.807  26.524 1.00 50.16  ? 401 A1EJX A C15 1 
HETATM 4299 C C16 . A1EJX C 2 .   ? 4.374   15.823  27.809 1.00 49.16  ? 401 A1EJX A C16 1 
HETATM 4300 C C17 . A1EJX C 2 .   ? 3.853   17.038  27.378 1.00 48.58  ? 401 A1EJX A C17 1 
HETATM 4301 C C19 . A1EJX C 2 .   ? 2.479   17.475  27.736 1.00 56.46  ? 401 A1EJX A C19 1 
HETATM 4302 C C22 . A1EJX C 2 .   ? 7.527   12.671  24.986 1.00 46.54  ? 401 A1EJX A C22 1 
HETATM 4303 C C24 . A1EJX C 2 .   ? 1.763   16.854  28.758 1.00 64.59  ? 401 A1EJX A C24 1 
HETATM 4304 C C25 . A1EJX C 2 .   ? 0.468   17.238  29.063 1.00 64.46  ? 401 A1EJX A C25 1 
HETATM 4305 C C26 . A1EJX C 2 .   ? -0.153  18.267  28.358 1.00 64.94  ? 401 A1EJX A C26 1 
HETATM 4306 C C27 . A1EJX C 2 .   ? 0.547   18.868  27.318 1.00 63.44  ? 401 A1EJX A C27 1 
HETATM 4307 C C28 . A1EJX C 2 .   ? 1.839   18.480  27.016 1.00 54.27  ? 401 A1EJX A C28 1 
HETATM 4308 C C1  . A1EJX C 2 .   ? 7.924   17.696  24.830 1.00 52.53  ? 401 A1EJX A C1  1 
HETATM 4309 C C2  . A1EJX C 2 .   ? 8.419   16.449  25.383 1.00 52.46  ? 401 A1EJX A C2  1 
HETATM 4310 C C29 . A1EJX C 2 .   ? -1.555  18.716  28.620 1.00 70.61  ? 401 A1EJX A C29 1 
HETATM 4311 C C32 . A1EJX C 2 .   ? -3.171  19.901  29.989 1.00 70.36  ? 401 A1EJX A C32 1 
HETATM 4312 C C33 . A1EJX C 2 .   ? -0.826  19.823  30.723 1.00 70.60  ? 401 A1EJX A C33 1 
HETATM 4313 C C4  . A1EJX C 2 .   ? 7.700   15.671  26.287 1.00 50.35  ? 401 A1EJX A C4  1 
HETATM 4314 C C5  . A1EJX C 2 .   ? 6.363   16.118  26.690 1.00 48.32  ? 401 A1EJX A C5  1 
HETATM 4315 C C6  . A1EJX C 2 .   ? 8.262   14.395  26.828 1.00 48.28  ? 401 A1EJX A C6  1 
HETATM 4316 C C7  . A1EJX C 2 .   ? 8.129   13.154  26.172 1.00 49.93  ? 401 A1EJX A C7  1 
HETATM 4317 C C8  . A1EJX C 2 .   ? 8.701   12.011  26.759 1.00 53.48  ? 401 A1EJX A C8  1 
HETATM 4318 C C9  . A1EJX C 2 .   ? 9.381   12.136  27.957 1.00 54.72  ? 401 A1EJX A C9  1 
HETATM 4319 F F12 . A1EJX C 2 .   ? 9.925   11.025  28.499 1.00 53.11  ? 401 A1EJX A F12 1 
HETATM 4320 N N14 . A1EJX C 2 .   ? 5.591   15.364  27.490 1.00 51.60  ? 401 A1EJX A N14 1 
HETATM 4321 N N20 . A1EJX C 2 .   ? 9.648   16.088  24.965 1.00 54.90  ? 401 A1EJX A N20 1 
HETATM 4322 N N21 . A1EJX C 2 .   ? 8.422   10.970  25.939 1.00 46.26  ? 401 A1EJX A N21 1 
HETATM 4323 N N23 . A1EJX C 2 .   ? 7.705   11.371  24.848 1.00 46.13  ? 401 A1EJX A N23 1 
HETATM 4324 N N3  . A1EJX C 2 .   ? 6.735   18.107  25.340 1.00 49.19  ? 401 A1EJX A N3  1 
HETATM 4325 N N30 . A1EJX C 2 .   ? -1.811  19.440  29.719 1.00 72.91  ? 401 A1EJX A N30 1 
HETATM 4326 O O18 . A1EJX C 2 .   ? 8.515   18.365  23.981 1.00 53.08  ? 401 A1EJX A O18 1 
HETATM 4327 O O31 . A1EJX C 2 .   ? -2.422  18.435  27.810 1.00 69.70  ? 401 A1EJX A O31 1 
HETATM 4328 S S   . SO4   D 3 .   ? 5.383   -3.217  44.624 1.00 68.04  ? 402 SO4   A S   1 
HETATM 4329 O O1  . SO4   D 3 .   ? 5.582   -2.061  43.684 1.00 59.50  ? 402 SO4   A O1  1 
HETATM 4330 O O2  . SO4   D 3 .   ? 4.047   -3.866  44.373 1.00 68.55  ? 402 SO4   A O2  1 
HETATM 4331 O O3  . SO4   D 3 .   ? 6.483   -4.219  44.417 1.00 58.44  ? 402 SO4   A O3  1 
HETATM 4332 O O4  . SO4   D 3 .   ? 5.436   -2.704  46.035 1.00 68.18  ? 402 SO4   A O4  1 
HETATM 4333 S S   . SO4   E 3 .   ? -8.315  13.750  27.727 0.72 70.36  ? 403 SO4   A S   1 
HETATM 4334 O O1  . SO4   E 3 .   ? -6.950  13.218  27.405 0.72 64.37  ? 403 SO4   A O1  1 
HETATM 4335 O O2  . SO4   E 3 .   ? -9.101  13.958  26.467 0.72 66.76  ? 403 SO4   A O2  1 
HETATM 4336 O O3  . SO4   E 3 .   ? -9.039  12.774  28.611 0.72 65.95  ? 403 SO4   A O3  1 
HETATM 4337 O O4  . SO4   E 3 .   ? -8.170  15.065  28.431 0.72 66.99  ? 403 SO4   A O4  1 
HETATM 4338 S S   . SO4   F 3 .   ? -6.263  -3.703  27.276 0.65 71.50  ? 404 SO4   A S   1 
HETATM 4339 O O1  . SO4   F 3 .   ? -5.716  -3.988  25.910 0.65 69.15  ? 404 SO4   A O1  1 
HETATM 4340 O O2  . SO4   F 3 .   ? -7.707  -4.104  27.321 0.65 68.96  ? 404 SO4   A O2  1 
HETATM 4341 O O3  . SO4   F 3 .   ? -5.490  -4.483  28.301 0.65 69.88  ? 404 SO4   A O3  1 
HETATM 4342 O O4  . SO4   F 3 .   ? -6.145  -2.235  27.569 0.65 70.06  ? 404 SO4   A O4  1 
HETATM 4343 S S   . SO4   G 3 .   ? 27.172  8.341   38.365 0.93 107.68 ? 405 SO4   A S   1 
HETATM 4344 O O1  . SO4   G 3 .   ? 28.564  7.817   38.564 0.93 101.76 ? 405 SO4   A O1  1 
HETATM 4345 O O2  . SO4   G 3 .   ? 27.178  9.435   37.333 0.93 91.76  ? 405 SO4   A O2  1 
HETATM 4346 O O3  . SO4   G 3 .   ? 26.286  7.218   37.904 0.93 89.88  ? 405 SO4   A O3  1 
HETATM 4347 O O4  . SO4   G 3 .   ? 26.662  8.883   39.669 0.93 92.11  ? 405 SO4   A O4  1 
HETATM 4348 S S   . SO4   H 3 .   ? -0.072  25.968  17.812 0.50 58.09  ? 406 SO4   A S   1 
HETATM 4349 O O1  . SO4   H 3 .   ? 0.746   26.827  16.895 0.50 47.78  ? 406 SO4   A O1  1 
HETATM 4350 O O2  . SO4   H 3 .   ? -0.222  24.604  17.210 0.50 55.76  ? 406 SO4   A O2  1 
HETATM 4351 O O3  . SO4   H 3 .   ? 0.583   25.865  19.158 0.50 50.84  ? 406 SO4   A O3  1 
HETATM 4352 O O4  . SO4   H 3 .   ? -1.428  26.573  17.989 0.50 59.17  ? 406 SO4   A O4  1 
HETATM 4353 S S   . SO4   I 3 .   ? -3.391  6.058   29.329 0.64 73.45  ? 407 SO4   A S   1 
HETATM 4354 O O1  . SO4   I 3 .   ? -3.061  5.880   27.876 0.64 59.42  ? 407 SO4   A O1  1 
HETATM 4355 O O2  . SO4   I 3 .   ? -4.656  5.313   29.651 0.64 60.56  ? 407 SO4   A O2  1 
HETATM 4356 O O3  . SO4   I 3 .   ? -2.263  5.531   30.169 0.64 57.49  ? 407 SO4   A O3  1 
HETATM 4357 O O4  . SO4   I 3 .   ? -3.575  7.523   29.610 0.64 68.51  ? 407 SO4   A O4  1 
HETATM 4358 C C10 . A1EJX J 2 .   ? -10.036 38.399  25.357 1.00 49.49  ? 401 A1EJX B C10 1 
HETATM 4359 C C11 . A1EJX J 2 .   ? -9.532  37.271  24.735 1.00 48.71  ? 401 A1EJX B C11 1 
HETATM 4360 C C13 . A1EJX J 2 .   ? -6.538  34.382  22.762 1.00 52.35  ? 401 A1EJX B C13 1 
HETATM 4361 C C15 . A1EJX J 2 .   ? -5.282  33.873  23.081 1.00 51.48  ? 401 A1EJX B C15 1 
HETATM 4362 C C16 . A1EJX J 2 .   ? -4.949  35.796  24.447 1.00 51.54  ? 401 A1EJX B C16 1 
HETATM 4363 C C17 . A1EJX J 2 .   ? -4.467  34.582  23.965 1.00 51.82  ? 401 A1EJX B C17 1 
HETATM 4364 C C19 . A1EJX J 2 .   ? -3.098  34.101  24.293 1.00 53.66  ? 401 A1EJX B C19 1 
HETATM 4365 C C22 . A1EJX J 2 .   ? -7.830  39.151  21.887 1.00 48.42  ? 401 A1EJX B C22 1 
HETATM 4366 C C24 . A1EJX J 2 .   ? -2.372  33.338  23.384 1.00 52.53  ? 401 A1EJX B C24 1 
HETATM 4367 C C25 . A1EJX J 2 .   ? -1.081  32.925  23.661 1.00 55.25  ? 401 A1EJX B C25 1 
HETATM 4368 C C26 . A1EJX J 2 .   ? -0.470  33.266  24.861 1.00 61.90  ? 401 A1EJX B C26 1 
HETATM 4369 C C27 . A1EJX J 2 .   ? -1.174  34.065  25.758 1.00 56.89  ? 401 A1EJX B C27 1 
HETATM 4370 C C28 . A1EJX J 2 .   ? -2.468  34.470  25.480 1.00 54.06  ? 401 A1EJX B C28 1 
HETATM 4371 C C1  . A1EJX J 2 .   ? -8.502  34.229  21.318 1.00 50.92  ? 401 A1EJX B C1  1 
HETATM 4372 C C2  . A1EJX J 2 .   ? -8.985  35.440  21.959 1.00 54.14  ? 401 A1EJX B C2  1 
HETATM 4373 C C29 . A1EJX J 2 .   ? 0.940   32.824  25.109 1.00 69.32  ? 401 A1EJX B C29 1 
HETATM 4374 C C32 . A1EJX J 2 .   ? 0.184   31.367  26.989 1.00 65.62  ? 401 A1EJX B C32 1 
HETATM 4375 C C33 . A1EJX J 2 .   ? 2.556   31.524  26.347 1.00 71.87  ? 401 A1EJX B C33 1 
HETATM 4376 C C4  . A1EJX J 2 .   ? -8.265  36.113  22.946 1.00 53.45  ? 401 A1EJX B C4  1 
HETATM 4377 C C5  . A1EJX J 2 .   ? -6.947  35.608  23.326 1.00 52.57  ? 401 A1EJX B C5  1 
HETATM 4378 C C6  . A1EJX J 2 .   ? -8.775  37.371  23.567 1.00 48.46  ? 401 A1EJX B C6  1 
HETATM 4379 C C7  . A1EJX J 2 .   ? -8.520  38.640  23.010 1.00 49.63  ? 401 A1EJX B C7  1 
HETATM 4380 C C8  . A1EJX J 2 .   ? -9.035  39.781  23.649 1.00 50.13  ? 401 A1EJX B C8  1 
HETATM 4381 C C9  . A1EJX J 2 .   ? -9.780  39.629  24.804 1.00 52.78  ? 401 A1EJX B C9  1 
HETATM 4382 F F12 . A1EJX J 2 .   ? -10.263 40.743  25.403 1.00 52.54  ? 401 A1EJX B F12 1 
HETATM 4383 N N14 . A1EJX J 2 .   ? -6.152  36.304  24.154 1.00 50.12  ? 401 A1EJX B N14 1 
HETATM 4384 N N20 . A1EJX J 2 .   ? -10.197 35.865  21.546 1.00 54.86  ? 401 A1EJX B N20 1 
HETATM 4385 N N21 . A1EJX J 2 .   ? -8.643  40.849  22.914 1.00 46.43  ? 401 A1EJX B N21 1 
HETATM 4386 N N23 . A1EJX J 2 .   ? -7.907  40.467  21.829 1.00 47.00  ? 401 A1EJX B N23 1 
HETATM 4387 N N3  . A1EJX J 2 .   ? -7.399  33.697  21.902 1.00 50.76  ? 401 A1EJX B N3  1 
HETATM 4388 N N30 . A1EJX J 2 .   ? 1.183   31.954  26.101 1.00 71.37  ? 401 A1EJX B N30 1 
HETATM 4389 O O18 . A1EJX J 2 .   ? -9.021  33.697  20.337 1.00 50.35  ? 401 A1EJX B O18 1 
HETATM 4390 O O31 . A1EJX J 2 .   ? 1.830   33.266  24.401 1.00 65.20  ? 401 A1EJX B O31 1 
HETATM 4391 S S   . SO4   K 3 .   ? -5.206  54.459  41.823 1.00 66.87  ? 402 SO4   B S   1 
HETATM 4392 O O1  . SO4   K 3 .   ? -3.861  55.023  41.473 1.00 74.38  ? 402 SO4   B O1  1 
HETATM 4393 O O2  . SO4   K 3 .   ? -5.589  53.403  40.830 1.00 59.36  ? 402 SO4   B O2  1 
HETATM 4394 O O3  . SO4   K 3 .   ? -5.144  53.845  43.191 1.00 66.70  ? 402 SO4   B O3  1 
HETATM 4395 O O4  . SO4   K 3 .   ? -6.227  55.562  41.797 1.00 61.55  ? 402 SO4   B O4  1 
HETATM 4396 S S   . SO4   L 3 .   ? 7.392   37.935  24.892 0.81 79.96  ? 403 SO4   B S   1 
HETATM 4397 O O1  . SO4   L 3 .   ? 8.656   37.733  24.107 0.81 66.38  ? 403 SO4   B O1  1 
HETATM 4398 O O2  . SO4   L 3 .   ? 6.350   38.607  24.042 0.81 70.16  ? 403 SO4   B O2  1 
HETATM 4399 O O3  . SO4   L 3 .   ? 6.868   36.601  25.335 0.81 74.09  ? 403 SO4   B O3  1 
HETATM 4400 O O4  . SO4   L 3 .   ? 7.693   38.786  26.093 0.81 74.65  ? 403 SO4   B O4  1 
HETATM 4401 S S   . SO4   M 3 .   ? 6.637   55.215  24.429 0.56 69.47  ? 404 SO4   B S   1 
HETATM 4402 O O1  . SO4   M 3 .   ? 8.072   55.486  24.089 0.56 61.45  ? 404 SO4   B O1  1 
HETATM 4403 O O2  . SO4   M 3 .   ? 5.875   54.931  23.171 0.56 64.68  ? 404 SO4   B O2  1 
HETATM 4404 O O3  . SO4   M 3 .   ? 6.554   54.024  25.339 0.56 66.34  ? 404 SO4   B O3  1 
HETATM 4405 O O4  . SO4   M 3 .   ? 6.048   56.415  25.114 0.56 65.08  ? 404 SO4   B O4  1 
HETATM 4406 S S   . SO4   N 3 .   ? 2.916   45.552  26.088 0.65 71.69  ? 405 SO4   B S   1 
HETATM 4407 O O1  . SO4   N 3 .   ? 3.257   46.541  25.014 0.65 58.62  ? 405 SO4   B O1  1 
HETATM 4408 O O2  . SO4   N 3 .   ? 1.927   44.556  25.551 0.65 65.72  ? 405 SO4   B O2  1 
HETATM 4409 O O3  . SO4   N 3 .   ? 4.159   44.829  26.520 0.65 64.15  ? 405 SO4   B O3  1 
HETATM 4410 O O4  . SO4   N 3 .   ? 2.328   46.291  27.257 0.65 62.86  ? 405 SO4   B O4  1 
HETATM 4411 O O   . HOH   O 4 .   ? 2.931   21.348  25.290 1.00 53.48  ? 501 HOH   A O   1 
HETATM 4412 O O   . HOH   O 4 .   ? -2.704  -6.720  10.379 1.00 63.08  ? 502 HOH   A O   1 
HETATM 4413 O O   . HOH   O 4 .   ? 11.799  21.055  43.005 1.00 71.23  ? 503 HOH   A O   1 
HETATM 4414 O O   . HOH   O 4 .   ? 11.894  -1.900  34.276 1.00 50.92  ? 504 HOH   A O   1 
HETATM 4415 O O   . HOH   O 4 .   ? 5.352   22.574  12.775 1.00 50.75  ? 505 HOH   A O   1 
HETATM 4416 O O   . HOH   O 4 .   ? 1.648   6.211   27.410 1.00 51.76  ? 506 HOH   A O   1 
HETATM 4417 O O   . HOH   O 4 .   ? 0.666   14.979  25.969 1.00 51.23  ? 507 HOH   A O   1 
HETATM 4418 O O   . HOH   O 4 .   ? 8.391   19.838  6.436  1.00 59.48  ? 508 HOH   A O   1 
HETATM 4419 O O   . HOH   O 4 .   ? 2.037   22.348  27.469 1.00 50.81  ? 509 HOH   A O   1 
HETATM 4420 O O   . HOH   O 4 .   ? -2.479  2.188   31.992 1.00 62.16  ? 510 HOH   A O   1 
HETATM 4421 O O   . HOH   O 4 .   ? -1.801  17.531  25.420 1.00 49.23  ? 511 HOH   A O   1 
HETATM 4422 O O   . HOH   O 4 .   ? 22.483  5.968   23.762 1.00 81.62  ? 512 HOH   A O   1 
HETATM 4423 O O   . HOH   O 4 .   ? 10.604  -2.771  27.271 1.00 59.91  ? 513 HOH   A O   1 
HETATM 4424 O O   . HOH   O 4 .   ? 5.302   20.267  24.362 1.00 50.28  ? 514 HOH   A O   1 
HETATM 4425 O O   . HOH   O 4 .   ? -7.023  -3.567  5.934  1.00 61.23  ? 515 HOH   A O   1 
HETATM 4426 O O   . HOH   O 4 .   ? 1.350   18.138  8.425  1.00 59.40  ? 516 HOH   A O   1 
HETATM 4427 O O   . HOH   O 4 .   ? 3.721   20.530  12.906 1.00 54.31  ? 517 HOH   A O   1 
HETATM 4428 O O   . HOH   O 4 .   ? -13.828 5.091   20.647 1.00 53.42  ? 518 HOH   A O   1 
HETATM 4429 O O   . HOH   O 4 .   ? 14.438  9.215   17.993 1.00 62.96  ? 519 HOH   A O   1 
HETATM 4430 O O   . HOH   O 4 .   ? -1.554  2.152   19.938 1.00 45.22  ? 520 HOH   A O   1 
HETATM 4431 O O   . HOH   O 4 .   ? 3.648   3.543   24.655 1.00 41.89  ? 521 HOH   A O   1 
HETATM 4432 O O   . HOH   O 4 .   ? -11.515 12.063  21.530 1.00 63.22  ? 522 HOH   A O   1 
HETATM 4433 O O   . HOH   O 4 .   ? 19.110  8.896   45.293 1.00 72.44  ? 523 HOH   A O   1 
HETATM 4434 O O   . HOH   O 4 .   ? 19.496  5.937   27.662 1.00 59.86  ? 524 HOH   A O   1 
HETATM 4435 O O   . HOH   O 4 .   ? -5.276  12.294  22.702 1.00 47.21  ? 525 HOH   A O   1 
HETATM 4436 O O   . HOH   O 4 .   ? 7.456   -2.187  9.444  1.00 54.86  ? 526 HOH   A O   1 
HETATM 4437 O O   . HOH   O 4 .   ? 6.725   24.909  37.910 1.00 70.04  ? 527 HOH   A O   1 
HETATM 4438 O O   . HOH   O 4 .   ? -15.030 21.344  11.925 1.00 59.53  ? 528 HOH   A O   1 
HETATM 4439 O O   . HOH   O 4 .   ? 19.902  4.468   17.433 1.00 70.34  ? 529 HOH   A O   1 
HETATM 4440 O O   . HOH   O 4 .   ? 17.128  0.758   16.561 1.00 58.72  ? 530 HOH   A O   1 
HETATM 4441 O O   . HOH   O 4 .   ? 4.336   8.562   40.468 1.00 65.59  ? 531 HOH   A O   1 
HETATM 4442 O O   . HOH   O 4 .   ? 4.726   12.776  28.732 1.00 57.76  ? 532 HOH   A O   1 
HETATM 4443 O O   . HOH   O 4 .   ? 2.140   -8.380  15.102 1.00 55.51  ? 533 HOH   A O   1 
HETATM 4444 O O   . HOH   O 4 .   ? -0.328  -7.965  14.627 1.00 51.41  ? 534 HOH   A O   1 
HETATM 4445 O O   . HOH   O 4 .   ? 1.461   -3.581  46.054 1.00 68.89  ? 535 HOH   A O   1 
HETATM 4446 O O   . HOH   O 4 .   ? -0.781  10.302  27.762 1.00 54.06  ? 536 HOH   A O   1 
HETATM 4447 O O   . HOH   O 4 .   ? 15.986  7.328   21.846 1.00 58.40  ? 537 HOH   A O   1 
HETATM 4448 O O   . HOH   O 4 .   ? -7.005  -3.625  35.724 1.00 68.85  ? 538 HOH   A O   1 
HETATM 4449 O O   . HOH   O 4 .   ? 16.546  25.098  39.458 1.00 71.89  ? 539 HOH   A O   1 
HETATM 4450 O O   . HOH   O 4 .   ? 6.465   8.186   36.323 1.00 63.17  ? 540 HOH   A O   1 
HETATM 4451 O O   . HOH   O 4 .   ? 9.357   21.610  43.013 1.00 68.79  ? 541 HOH   A O   1 
HETATM 4452 O O   . HOH   O 4 .   ? 10.683  11.952  5.167  1.00 66.45  ? 542 HOH   A O   1 
HETATM 4453 O O   . HOH   O 4 .   ? -4.841  1.164   23.025 1.00 51.32  ? 543 HOH   A O   1 
HETATM 4454 O O   . HOH   O 4 .   ? 9.406   24.262  20.641 1.00 57.57  ? 544 HOH   A O   1 
HETATM 4455 O O   . HOH   O 4 .   ? -11.093 28.992  15.602 1.00 62.12  ? 545 HOH   A O   1 
HETATM 4456 O O   . HOH   O 4 .   ? 1.507   12.749  27.715 1.00 59.68  ? 546 HOH   A O   1 
HETATM 4457 O O   . HOH   O 4 .   ? 2.809   12.719  30.270 1.00 67.73  ? 547 HOH   A O   1 
HETATM 4458 O O   . HOH   P 4 .   ? 8.971   39.894  20.365 1.00 58.61  ? 501 HOH   B O   1 
HETATM 4459 O O   . HOH   P 4 .   ? -11.516 53.893  31.333 1.00 54.04  ? 502 HOH   B O   1 
HETATM 4460 O O   . HOH   P 4 .   ? -10.364 29.084  38.283 1.00 63.20  ? 503 HOH   B O   1 
HETATM 4461 O O   . HOH   P 4 .   ? -9.155  43.935  38.288 1.00 56.97  ? 504 HOH   B O   1 
HETATM 4462 O O   . HOH   P 4 .   ? 4.002   47.966  22.059 1.00 56.85  ? 505 HOH   B O   1 
HETATM 4463 O O   . HOH   P 4 .   ? -15.552 37.479  39.879 1.00 57.68  ? 506 HOH   B O   1 
HETATM 4464 O O   . HOH   P 4 .   ? -8.728  43.292  23.393 1.00 52.61  ? 507 HOH   B O   1 
HETATM 4465 O O   . HOH   P 4 .   ? -6.340  31.571  21.120 1.00 47.14  ? 508 HOH   B O   1 
HETATM 4466 O O   . HOH   P 4 .   ? 6.531   59.459  25.081 1.00 66.83  ? 509 HOH   B O   1 
HETATM 4467 O O   . HOH   P 4 .   ? -3.865  30.653  21.463 1.00 51.09  ? 510 HOH   B O   1 
HETATM 4468 O O   . HOH   P 4 .   ? 7.570   55.114  32.784 1.00 62.48  ? 511 HOH   B O   1 
HETATM 4469 O O   . HOH   P 4 .   ? 5.532   51.824  16.906 1.00 45.46  ? 512 HOH   B O   1 
HETATM 4470 O O   . HOH   P 4 .   ? 9.254   34.336  4.808  1.00 56.76  ? 513 HOH   B O   1 
HETATM 4471 O O   . HOH   P 4 .   ? -4.153  53.960  5.863  1.00 54.29  ? 514 HOH   B O   1 
HETATM 4472 O O   . HOH   P 4 .   ? 12.689  38.244  -5.719 1.00 70.27  ? 515 HOH   B O   1 
HETATM 4473 O O   . HOH   P 4 .   ? 17.838  43.509  23.048 1.00 58.64  ? 516 HOH   B O   1 
HETATM 4474 O O   . HOH   P 4 .   ? 2.820   58.164  7.508  1.00 60.81  ? 517 HOH   B O   1 
HETATM 4475 O O   . HOH   P 4 .   ? 4.657   39.130  19.818 1.00 43.78  ? 518 HOH   B O   1 
HETATM 4476 O O   . HOH   P 4 .   ? 16.542  56.007  16.049 1.00 54.53  ? 519 HOH   B O   1 
HETATM 4477 O O   . HOH   P 4 .   ? 8.937   32.534  11.892 1.00 50.08  ? 520 HOH   B O   1 
HETATM 4478 O O   . HOH   P 4 .   ? 1.569   26.428  8.191  1.00 55.02  ? 521 HOH   B O   1 
HETATM 4479 O O   . HOH   P 4 .   ? -6.043  36.969  -4.435 1.00 79.58  ? 522 HOH   B O   1 
HETATM 4480 O O   . HOH   P 4 .   ? -2.260  54.182  7.906  1.00 47.93  ? 523 HOH   B O   1 
HETATM 4481 O O   . HOH   P 4 .   ? 1.574   49.172  17.127 1.00 43.27  ? 524 HOH   B O   1 
HETATM 4482 O O   . HOH   P 4 .   ? 1.097   34.670  22.145 1.00 49.27  ? 525 HOH   B O   1 
HETATM 4483 O O   . HOH   P 4 .   ? -1.771  33.864  4.998  1.00 56.63  ? 526 HOH   B O   1 
HETATM 4484 O O   . HOH   P 4 .   ? 3.758   58.229  14.760 1.00 57.06  ? 527 HOH   B O   1 
HETATM 4485 O O   . HOH   P 4 .   ? -2.156  45.729  24.321 1.00 51.91  ? 528 HOH   B O   1 
HETATM 4486 O O   . HOH   P 4 .   ? -23.200 34.420  25.840 1.00 59.26  ? 529 HOH   B O   1 
HETATM 4487 O O   . HOH   P 4 .   ? -10.060 54.491  23.901 1.00 57.52  ? 530 HOH   B O   1 
HETATM 4488 O O   . HOH   P 4 .   ? -3.665  47.907  21.742 1.00 46.00  ? 531 HOH   B O   1 
HETATM 4489 O O   . HOH   P 4 .   ? 13.770  46.404  17.591 1.00 46.21  ? 532 HOH   B O   1 
HETATM 4490 O O   . HOH   P 4 .   ? -0.961  36.467  23.084 1.00 53.06  ? 533 HOH   B O   1 
HETATM 4491 O O   . HOH   P 4 .   ? -14.170 33.815  39.114 1.00 61.23  ? 534 HOH   B O   1 
HETATM 4492 O O   . HOH   P 4 .   ? 7.335   35.367  16.541 1.00 46.18  ? 535 HOH   B O   1 
HETATM 4493 O O   . HOH   P 4 .   ? -4.158  31.182  9.251  1.00 56.42  ? 536 HOH   B O   1 
HETATM 4494 O O   . HOH   P 4 .   ? -26.569 29.035  34.655 1.00 69.69  ? 537 HOH   B O   1 
HETATM 4495 O O   . HOH   P 4 .   ? 5.536   30.430  0.138  1.00 59.70  ? 538 HOH   B O   1 
HETATM 4496 O O   . HOH   P 4 .   ? 12.901  54.001  3.322  1.00 68.51  ? 539 HOH   B O   1 
HETATM 4497 O O   . HOH   P 4 .   ? 11.273  39.272  18.593 1.00 48.91  ? 540 HOH   B O   1 
HETATM 4498 O O   . HOH   P 4 .   ? 2.994   38.711  32.179 1.00 71.00  ? 541 HOH   B O   1 
HETATM 4499 O O   . HOH   P 4 .   ? -4.540  42.581  36.623 1.00 70.57  ? 542 HOH   B O   1 
HETATM 4500 O O   . HOH   P 4 .   ? 12.646  45.921  -3.548 1.00 63.40  ? 543 HOH   B O   1 
HETATM 4501 O O   . HOH   P 4 .   ? -8.865  34.521  13.813 1.00 55.85  ? 544 HOH   B O   1 
HETATM 4502 O O   . HOH   P 4 .   ? -1.085  55.310  42.704 1.00 65.48  ? 545 HOH   B O   1 
HETATM 4503 O O   . HOH   P 4 .   ? -5.546  38.976  25.503 1.00 51.47  ? 546 HOH   B O   1 
HETATM 4504 O O   . HOH   P 4 .   ? -6.813  54.363  6.719  1.00 57.48  ? 547 HOH   B O   1 
HETATM 4505 O O   . HOH   P 4 .   ? 0.260   59.613  11.513 1.00 49.28  ? 548 HOH   B O   1 
HETATM 4506 O O   . HOH   P 4 .   ? 2.187   64.147  19.004 1.00 75.81  ? 549 HOH   B O   1 
HETATM 4507 O O   . HOH   P 4 .   ? 14.700  29.598  8.874  1.00 42.01  ? 550 HOH   B O   1 
HETATM 4508 O O   . HOH   P 4 .   ? -1.847  60.335  12.188 1.00 53.46  ? 551 HOH   B O   1 
HETATM 4509 O O   . HOH   P 4 .   ? 9.661   27.213  5.707  1.00 59.95  ? 552 HOH   B O   1 
HETATM 4510 O O   . HOH   P 4 .   ? -13.100 54.280  38.004 1.00 50.40  ? 553 HOH   B O   1 
HETATM 4511 O O   . HOH   P 4 .   ? -2.424  45.398  26.683 1.00 56.86  ? 554 HOH   B O   1 
HETATM 4512 O O   . HOH   P 4 .   ? -28.487 28.625  32.872 1.00 84.71  ? 555 HOH   B O   1 
HETATM 4513 O O   . HOH   P 4 .   ? 1.069   30.791  30.131 1.00 72.95  ? 556 HOH   B O   1 
HETATM 4514 O O   . HOH   P 4 .   ? -2.337  39.047  24.028 1.00 55.93  ? 557 HOH   B O   1 
HETATM 4515 O O   . HOH   P 4 .   ? 0.403   39.940  24.508 1.00 57.54  ? 558 HOH   B O   1 
HETATM 4516 O O   . HOH   P 4 .   ? 10.850  29.275  4.523  1.00 56.39  ? 559 HOH   B O   1 
HETATM 4517 O O   . HOH   P 4 .   ? 0.180   56.041  8.191  1.00 51.98  ? 560 HOH   B O   1 
HETATM 4518 O O   . HOH   P 4 .   ? -17.761 45.618  19.411 1.00 58.79  ? 561 HOH   B O   1 
HETATM 4519 O O   . HOH   P 4 .   ? -8.084  56.094  31.325 1.00 58.22  ? 562 HOH   B O   1 
HETATM 4520 O O   . HOH   P 4 .   ? -11.770 33.084  3.931  1.00 65.73  ? 563 HOH   B O   1 
HETATM 4521 O O   . HOH   P 4 .   ? -4.627  60.654  10.980 1.00 60.91  ? 564 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   . LEU A 3   ? 1.5740 1.0151 1.3003 -0.0019 -0.6745 0.0123  77  LEU A N   
2    C CA  . LEU A 3   ? 1.5414 1.0003 1.3236 0.0163  -0.6151 0.0339  77  LEU A CA  
3    C C   . LEU A 3   ? 1.4744 1.0552 1.4122 -0.0032 -0.5954 0.0230  77  LEU A C   
4    O O   . LEU A 3   ? 1.4642 1.0707 1.4399 -0.0462 -0.5818 0.0064  77  LEU A O   
5    C CB  . LEU A 3   ? 1.4822 0.8368 1.1787 0.0042  -0.5451 0.0468  77  LEU A CB  
6    C CG  . LEU A 3   ? 1.6049 0.8448 1.1680 0.0345  -0.5368 0.0671  77  LEU A CG  
7    C CD1 . LEU A 3   ? 1.7194 0.8796 1.1481 0.0291  -0.5861 0.0582  77  LEU A CD1 
8    C CD2 . LEU A 3   ? 1.6269 0.7927 1.1546 0.0260  -0.4570 0.0770  77  LEU A CD2 
9    N N   . GLN A 4   ? 1.6018 1.2516 1.6249 0.0271  -0.5910 0.0320  78  GLN A N   
10   C CA  . GLN A 4   ? 1.4699 1.2410 1.6375 0.0102  -0.5777 0.0183  78  GLN A CA  
11   C C   . GLN A 4   ? 1.4052 1.1850 1.6095 0.0180  -0.5132 0.0361  78  GLN A C   
12   O O   . GLN A 4   ? 1.4149 1.1415 1.5712 0.0535  -0.4973 0.0560  78  GLN A O   
13   C CB  . GLN A 4   ? 1.4070 1.2761 1.6684 0.0367  -0.6371 0.0021  78  GLN A CB  
14   C CG  . GLN A 4   ? 1.4774 1.3267 1.6892 0.0424  -0.7154 -0.0125 78  GLN A CG  
15   C CD  . GLN A 4   ? 1.5225 1.3826 1.7376 -0.0100 -0.7258 -0.0374 78  GLN A CD  
16   O OE1 . GLN A 4   ? 1.4629 1.3794 1.7583 -0.0499 -0.6847 -0.0484 78  GLN A OE1 
17   N NE2 . GLN A 4   ? 1.6019 1.4015 1.7230 -0.0117 -0.7810 -0.0464 78  GLN A NE2 
18   N N   . PRO A 5   ? 1.2190 1.0605 1.5036 -0.0163 -0.4760 0.0293  79  PRO A N   
19   C CA  . PRO A 5   ? 1.1386 0.9890 1.4536 -0.0108 -0.4198 0.0447  79  PRO A CA  
20   C C   . PRO A 5   ? 1.0573 0.9942 1.4608 0.0215  -0.4263 0.0399  79  PRO A C   
21   O O   . PRO A 5   ? 1.0338 1.0679 1.5312 0.0150  -0.4518 0.0178  79  PRO A O   
22   C CB  . PRO A 5   ? 1.1070 0.9876 1.4654 -0.0625 -0.3869 0.0388  79  PRO A CB  
23   C CG  . PRO A 5   ? 1.1009 1.0433 1.5098 -0.0893 -0.4276 0.0130  79  PRO A CG  
24   C CD  . PRO A 5   ? 1.2322 1.1246 1.5699 -0.0656 -0.4823 0.0080  79  PRO A CD  
25   N N   . ARG A 6   ? 0.9964 0.8984 1.3764 0.0558  -0.4012 0.0572  80  ARG A N   
26   C CA  . ARG A 6   ? 0.8435 0.8122 1.2987 0.0912  -0.4033 0.0527  80  ARG A CA  
27   C C   . ARG A 6   ? 0.7701 0.7683 1.2668 0.0787  -0.3455 0.0563  80  ARG A C   
28   O O   . ARG A 6   ? 0.7600 0.6875 1.1960 0.0704  -0.3095 0.0736  80  ARG A O   
29   C CB  . ARG A 6   ? 0.8893 0.7868 1.2795 0.1413  -0.4230 0.0689  80  ARG A CB  
30   C CG  . ARG A 6   ? 0.8575 0.8071 1.3189 0.1826  -0.4241 0.0656  80  ARG A CG  
31   C CD  . ARG A 6   ? 0.9157 0.7717 1.2951 0.2273  -0.4383 0.0869  80  ARG A CD  
32   N NE  . ARG A 6   ? 0.8969 0.7951 1.3450 0.2704  -0.4456 0.0832  80  ARG A NE  
33   C CZ  . ARG A 6   ? 0.8381 0.7495 1.3211 0.2797  -0.3977 0.0840  80  ARG A CZ  
34   N NH1 . ARG A 6   ? 0.8010 0.6891 1.2612 0.2517  -0.3451 0.0900  80  ARG A NH1 
35   N NH2 . ARG A 6   ? 0.8383 0.7883 1.3583 0.3054  -0.3879 0.0743  80  ARG A NH2 
36   N N   . ARG A 7   ? 0.7257 0.8268 1.3253 0.0762  -0.3370 0.0379  81  ARG A N   
37   C CA  . ARG A 7   ? 0.6705 0.7973 1.2976 0.0600  -0.2832 0.0399  81  ARG A CA  
38   C C   . ARG A 7   ? 0.6516 0.7402 1.2567 0.1014  -0.2643 0.0517  81  ARG A C   
39   O O   . ARG A 7   ? 0.6709 0.7512 1.2805 0.1447  -0.2911 0.0513  81  ARG A O   
40   C CB  . ARG A 7   ? 0.6391 0.8849 1.3776 0.0399  -0.2713 0.0129  81  ARG A CB  
41   C CG  . ARG A 7   ? 0.6056 0.8648 1.3464 0.0058  -0.2155 0.0167  81  ARG A CG  
42   C CD  . ARG A 7   ? 0.5773 0.9441 1.4183 -0.0008 -0.1906 -0.0104 81  ARG A CD  
43   N NE  . ARG A 7   ? 0.5789 0.9357 1.3938 -0.0209 -0.1385 -0.0023 81  ARG A NE  
44   C CZ  . ARG A 7   ? 0.6292 1.0630 1.5059 -0.0358 -0.1019 -0.0236 81  ARG A CZ  
45   N NH1 . ARG A 7   ? 0.5609 1.0957 1.5453 -0.0331 -0.1069 -0.0576 81  ARG A NH1 
46   N NH2 . ARG A 7   ? 0.5403 0.9486 1.3704 -0.0540 -0.0597 -0.0129 81  ARG A NH2 
47   N N   . VAL A 8   ? 0.6312 0.6926 1.2119 0.0877  -0.2205 0.0624  82  VAL A N   
48   C CA  . VAL A 8   ? 0.6248 0.6471 1.1859 0.1210  -0.1988 0.0712  82  VAL A CA  
49   C C   . VAL A 8   ? 0.5980 0.6851 1.2136 0.1106  -0.1624 0.0589  82  VAL A C   
50   O O   . VAL A 8   ? 0.6131 0.7005 1.2137 0.0730  -0.1362 0.0634  82  VAL A O   
51   C CB  . VAL A 8   ? 0.6537 0.5697 1.1279 0.1184  -0.1833 0.0931  82  VAL A CB  
52   C CG1 . VAL A 8   ? 0.6038 0.4918 1.0741 0.1454  -0.1560 0.0973  82  VAL A CG1 
53   C CG2 . VAL A 8   ? 0.7509 0.5953 1.1613 0.1325  -0.2129 0.1025  82  VAL A CG2 
54   N N   . SER A 9   ? 0.5617 0.6972 1.2349 0.1440  -0.1613 0.0434  83  SER A N   
55   C CA  . SER A 9   ? 0.5924 0.7847 1.3118 0.1386  -0.1243 0.0274  83  SER A CA  
56   C C   . SER A 9   ? 0.6197 0.8138 1.3707 0.1886  -0.1257 0.0183  83  SER A C   
57   O O   . SER A 9   ? 0.6726 0.8518 1.4338 0.2244  -0.1598 0.0199  83  SER A O   
58   C CB  . SER A 9   ? 0.5593 0.8559 1.3569 0.1076  -0.1147 0.0019  83  SER A CB  
59   O OG  . SER A 9   ? 0.5495 0.8894 1.3699 0.0919  -0.0709 -0.0126 83  SER A OG  
60   N N   . PHE A 10  ? 0.6495 0.8555 1.4104 0.1904  -0.0902 0.0091  84  PHE A N   
61   C CA  . PHE A 10  ? 0.6307 0.8388 1.4199 0.2322  -0.0844 -0.0037 84  PHE A CA  
62   C C   . PHE A 10  ? 0.6486 0.9567 1.5233 0.2323  -0.0666 -0.0389 84  PHE A C   
63   O O   . PHE A 10  ? 0.7100 1.0239 1.5781 0.2377  -0.0375 -0.0535 84  PHE A O   
64   C CB  . PHE A 10  ? 0.6321 0.7718 1.3477 0.2305  -0.0567 0.0059  84  PHE A CB  
65   C CG  . PHE A 10  ? 0.6370 0.6759 1.2488 0.2333  -0.0662 0.0305  84  PHE A CG  
66   C CD1 . PHE A 10  ? 0.6770 0.6702 1.2581 0.2140  -0.0750 0.0513  84  PHE A CD1 
67   C CD2 . PHE A 10  ? 0.6862 0.6796 1.2315 0.2521  -0.0618 0.0308  84  PHE A CD2 
68   C CE1 . PHE A 10  ? 0.6668 0.5771 1.1499 0.2116  -0.0746 0.0654  84  PHE A CE1 
69   C CE2 . PHE A 10  ? 0.7319 0.6463 1.1851 0.2503  -0.0611 0.0469  84  PHE A CE2 
70   C CZ  . PHE A 10  ? 0.6975 0.5737 1.1193 0.2298  -0.0655 0.0614  84  PHE A CZ  
71   N N   . ARG A 11  ? 0.6718 1.0587 1.6239 0.2231  -0.0828 -0.0558 85  ARG A N   
72   C CA  . ARG A 11  ? 0.6251 1.1045 1.6545 0.2201  -0.0632 -0.0926 85  ARG A CA  
73   C C   . ARG A 11  ? 0.6849 1.2026 1.7622 0.2355  -0.1033 -0.1029 85  ARG A C   
74   O O   . ARG A 11  ? 0.6753 1.2094 1.7751 0.2616  -0.1086 -0.1177 85  ARG A O   
75   C CB  . ARG A 11  ? 0.6459 1.1982 1.7181 0.1701  -0.0204 -0.1113 85  ARG A CB  
76   C CG  . ARG A 11  ? 0.7129 1.2243 1.7127 0.1508  0.0222  -0.1045 85  ARG A CG  
77   C CD  . ARG A 11  ? 0.7167 1.2572 1.6882 0.0890  0.0608  -0.1078 85  ARG A CD  
78   N NE  . ARG A 11  ? 0.7302 1.2093 1.6234 0.0562  0.0449  -0.0727 85  ARG A NE  
79   C CZ  . ARG A 11  ? 0.7706 1.2451 1.6158 0.0025  0.0711  -0.0638 85  ARG A CZ  
80   N NH1 . ARG A 11  ? 0.8142 1.3373 1.6676 -0.0285 0.1174  -0.0854 85  ARG A NH1 
81   N NH2 . ARG A 11  ? 0.7893 1.2036 1.5724 -0.0217 0.0518  -0.0328 85  ARG A NH2 
82   N N   . SER A 20  ? 0.9701 1.4028 1.9166 -0.3841 -0.2208 -0.0735 94  SER A N   
83   C CA  . SER A 20  ? 1.0091 1.3588 1.8846 -0.3820 -0.2616 -0.0659 94  SER A CA  
84   C C   . SER A 20  ? 1.1349 1.5251 2.0722 -0.4277 -0.2846 -0.0968 94  SER A C   
85   O O   . SER A 20  ? 1.0824 1.5034 2.0512 -0.4077 -0.3409 -0.1215 94  SER A O   
86   C CB  . SER A 20  ? 0.9743 1.2998 1.8128 -0.3177 -0.3121 -0.0644 94  SER A CB  
87   O OG  . SER A 20  ? 0.9945 1.4226 1.9320 -0.2912 -0.3444 -0.0946 94  SER A OG  
88   N N   . PRO A 21  ? 1.2973 1.6831 2.2491 -0.4902 -0.2430 -0.0953 95  PRO A N   
89   C CA  . PRO A 21  ? 1.2932 1.7160 2.3098 -0.5397 -0.2598 -0.1268 95  PRO A CA  
90   C C   . PRO A 21  ? 1.3494 1.6721 2.2832 -0.5486 -0.2919 -0.1198 95  PRO A C   
91   O O   . PRO A 21  ? 1.3586 1.7066 2.3282 -0.5567 -0.3390 -0.1511 95  PRO A O   
92   C CB  . PRO A 21  ? 1.2991 1.7414 2.3461 -0.6030 -0.1928 -0.1226 95  PRO A CB  
93   C CG  . PRO A 21  ? 1.2653 1.6992 2.2783 -0.5834 -0.1481 -0.0945 95  PRO A CG  
94   C CD  . PRO A 21  ? 1.2590 1.6155 2.1779 -0.5204 -0.1788 -0.0679 95  PRO A CD  
95   N N   . GLY A 22  ? 1.2477 1.4567 2.0742 -0.5476 -0.2678 -0.0822 96  GLY A N   
96   C CA  . GLY A 22  ? 1.1586 1.2665 1.9060 -0.5537 -0.2915 -0.0774 96  GLY A CA  
97   C C   . GLY A 22  ? 1.1869 1.2608 1.8771 -0.4994 -0.3425 -0.0827 96  GLY A C   
98   O O   . GLY A 22  ? 1.2070 1.2028 1.8332 -0.5053 -0.3640 -0.0869 96  GLY A O   
99   N N   . TYR A 23  ? 1.1595 1.2851 1.8677 -0.4486 -0.3605 -0.0835 97  TYR A N   
100  C CA  . TYR A 23  ? 1.1251 1.2097 1.7673 -0.3959 -0.4059 -0.0833 97  TYR A CA  
101  C C   . TYR A 23  ? 1.1324 1.2842 1.8288 -0.3914 -0.4690 -0.1209 97  TYR A C   
102  O O   . TYR A 23  ? 1.0446 1.3050 1.8454 -0.3841 -0.4833 -0.1412 97  TYR A O   
103  C CB  . TYR A 23  ? 1.0765 1.1685 1.7033 -0.3418 -0.3939 -0.0615 97  TYR A CB  
104  C CG  . TYR A 23  ? 1.0558 1.0999 1.6100 -0.2883 -0.4366 -0.0581 97  TYR A CG  
105  C CD1 . TYR A 23  ? 1.1308 1.0587 1.5710 -0.2804 -0.4364 -0.0442 97  TYR A CD1 
106  C CD2 . TYR A 23  ? 1.0037 1.1133 1.6020 -0.2462 -0.4745 -0.0690 97  TYR A CD2 
107  C CE1 . TYR A 23  ? 1.1664 1.0414 1.5281 -0.2362 -0.4687 -0.0400 97  TYR A CE1 
108  C CE2 . TYR A 23  ? 1.0641 1.1173 1.5831 -0.1988 -0.5135 -0.0615 97  TYR A CE2 
109  C CZ  . TYR A 23  ? 1.1502 1.0842 1.5457 -0.1961 -0.5081 -0.0463 97  TYR A CZ  
110  O OH  . TYR A 23  ? 1.1753 1.0445 1.4804 -0.1538 -0.5403 -0.0380 97  TYR A OH  
111  N N   . ASP A 24  ? 1.2219 1.3083 1.8488 -0.3952 -0.5079 -0.1326 98  ASP A N   
112  C CA  . ASP A 24  ? 1.2201 1.3494 1.8701 -0.3830 -0.5795 -0.1655 98  ASP A CA  
113  C C   . ASP A 24  ? 1.2887 1.3585 1.8401 -0.3226 -0.6156 -0.1502 98  ASP A C   
114  O O   . ASP A 24  ? 1.3661 1.3240 1.7949 -0.3170 -0.6118 -0.1371 98  ASP A O   
115  C CB  . ASP A 24  ? 1.2912 1.3821 1.9179 -0.4288 -0.6024 -0.1915 98  ASP A CB  
116  C CG  . ASP A 24  ? 1.3893 1.5007 2.0083 -0.4123 -0.6845 -0.2238 98  ASP A CG  
117  O OD1 . ASP A 24  ? 1.3500 1.5732 2.0834 -0.4098 -0.7222 -0.2514 98  ASP A OD1 
118  O OD2 . ASP A 24  ? 1.4845 1.4986 1.9814 -0.4017 -0.7107 -0.2230 98  ASP A OD2 
119  N N   . PRO A 25  ? 1.2675 1.4027 1.8665 -0.2776 -0.6482 -0.1519 99  PRO A N   
120  C CA  . PRO A 25  ? 1.2961 1.3628 1.7925 -0.2204 -0.6791 -0.1323 99  PRO A CA  
121  C C   . PRO A 25  ? 1.4260 1.4110 1.8098 -0.2179 -0.7348 -0.1434 99  PRO A C   
122  O O   . PRO A 25  ? 1.3989 1.3046 1.6722 -0.1771 -0.7527 -0.1241 99  PRO A O   
123  C CB  . PRO A 25  ? 1.2047 1.3735 1.8022 -0.1801 -0.7155 -0.1416 99  PRO A CB  
124  C CG  . PRO A 25  ? 1.1232 1.4004 1.8626 -0.2124 -0.6703 -0.1549 99  PRO A CG  
125  C CD  . PRO A 25  ? 1.1410 1.4111 1.8918 -0.2770 -0.6509 -0.1713 99  PRO A CD  
126  N N   . SER A 26  ? 1.4402 1.4373 1.8429 -0.2622 -0.7601 -0.1745 100 SER A N   
127  C CA  . SER A 26  ? 1.5041 1.4226 1.7949 -0.2656 -0.8127 -0.1902 100 SER A CA  
128  C C   . SER A 26  ? 1.5416 1.3387 1.7154 -0.2935 -0.7655 -0.1811 100 SER A C   
129  O O   . SER A 26  ? 1.6419 1.3486 1.6903 -0.2890 -0.7951 -0.1880 100 SER A O   
130  C CB  . SER A 26  ? 1.5440 1.5429 1.9230 -0.2981 -0.8729 -0.2358 100 SER A CB  
131  O OG  . SER A 26  ? 1.5055 1.6280 2.0157 -0.2735 -0.9069 -0.2488 100 SER A OG  
132  N N   . ARG A 27  ? 1.5288 1.3187 1.7392 -0.3222 -0.6941 -0.1674 101 ARG A N   
133  C CA  . ARG A 27  ? 1.5219 1.1982 1.6366 -0.3446 -0.6495 -0.1601 101 ARG A CA  
134  C C   . ARG A 27  ? 1.5950 1.1808 1.6039 -0.3027 -0.6170 -0.1277 101 ARG A C   
135  O O   . ARG A 27  ? 1.4557 1.0749 1.4911 -0.2653 -0.6062 -0.1038 101 ARG A O   
136  C CB  . ARG A 27  ? 1.5043 1.1985 1.6958 -0.3884 -0.5915 -0.1550 101 ARG A CB  
137  C CG  . ARG A 27  ? 1.5206 1.2635 1.7875 -0.4433 -0.6106 -0.1896 101 ARG A CG  
138  C CD  . ARG A 27  ? 1.6476 1.3069 1.8233 -0.4645 -0.6387 -0.2174 101 ARG A CD  
139  N NE  . ARG A 27  ? 1.7206 1.2682 1.8214 -0.4786 -0.5850 -0.2047 101 ARG A NE  
140  C CZ  . ARG A 27  ? 1.7940 1.3080 1.9111 -0.5254 -0.5610 -0.2200 101 ARG A CZ  
141  N NH1 . ARG A 27  ? 1.6269 1.2149 1.8230 -0.5583 -0.5713 -0.2470 101 ARG A NH1 
142  N NH2 . ARG A 27  ? 1.8424 1.2618 1.8988 -0.5247 -0.5073 -0.2063 101 ARG A NH2 
143  N N   . PRO A 28  ? 1.7172 1.1876 1.6096 -0.3099 -0.5981 -0.1300 102 PRO A N   
144  C CA  . PRO A 28  ? 1.6779 1.0602 1.4724 -0.2735 -0.5633 -0.1039 102 PRO A CA  
145  C C   . PRO A 28  ? 1.6850 1.0562 1.5212 -0.2702 -0.4943 -0.0774 102 PRO A C   
146  O O   . PRO A 28  ? 1.6839 1.0170 1.4779 -0.2344 -0.4688 -0.0542 102 PRO A O   
147  C CB  . PRO A 28  ? 1.7695 1.0375 1.4359 -0.2905 -0.5625 -0.1239 102 PRO A CB  
148  C CG  . PRO A 28  ? 1.7238 1.0109 1.4434 -0.3419 -0.5669 -0.1530 102 PRO A CG  
149  C CD  . PRO A 28  ? 1.6590 1.0742 1.5030 -0.3512 -0.6097 -0.1615 102 PRO A CD  
150  N N   . GLU A 29  ? 1.6708 1.0678 1.5839 -0.3068 -0.4652 -0.0797 103 GLU A N   
151  C CA  . GLU A 29  ? 1.6051 0.9859 1.5518 -0.3034 -0.4078 -0.0538 103 GLU A CA  
152  C C   . GLU A 29  ? 1.5279 0.9832 1.5334 -0.2703 -0.4028 -0.0300 103 GLU A C   
153  O O   . GLU A 29  ? 1.4857 1.0312 1.5507 -0.2644 -0.4376 -0.0363 103 GLU A O   
154  C CB  . GLU A 29  ? 1.5813 0.9743 1.5950 -0.3505 -0.3861 -0.0583 103 GLU A CB  
155  C CG  . GLU A 29  ? 1.6365 0.9426 1.5990 -0.3826 -0.3789 -0.0805 103 GLU A CG  
156  C CD  . GLU A 29  ? 1.7440 1.0694 1.6939 -0.4085 -0.4280 -0.1156 103 GLU A CD  
157  O OE1 . GLU A 29  ? 1.7404 1.1620 1.7572 -0.4141 -0.4644 -0.1233 103 GLU A OE1 
158  O OE2 . GLU A 29  ? 1.8449 1.0904 1.7220 -0.4238 -0.4304 -0.1390 103 GLU A OE2 
159  N N   . SER A 30  ? 1.4602 0.8787 1.4556 -0.2486 -0.3595 -0.0059 104 SER A N   
160  C CA  . SER A 30  ? 1.3604 0.8372 1.4001 -0.2150 -0.3517 0.0146  104 SER A CA  
161  C C   . SER A 30  ? 1.1959 0.7682 1.3396 -0.2379 -0.3454 0.0177  104 SER A C   
162  O O   . SER A 30  ? 1.2309 0.8067 1.4067 -0.2800 -0.3347 0.0122  104 SER A O   
163  C CB  . SER A 30  ? 1.3076 0.7193 1.3140 -0.1899 -0.3070 0.0356  104 SER A CB  
164  O OG  . SER A 30  ? 1.2865 0.6742 1.3231 -0.2150 -0.2725 0.0433  104 SER A OG  
165  N N   . PHE A 31  ? 1.3405 0.6692 1.2009 -0.2534 -0.5829 0.0807  105 PHE A N   
166  C CA  . PHE A 31  ? 1.2779 0.6626 1.2118 -0.2452 -0.5871 0.1050  105 PHE A CA  
167  C C   . PHE A 31  ? 1.2897 0.6740 1.2464 -0.2221 -0.5685 0.0845  105 PHE A C   
168  O O   . PHE A 31  ? 1.2928 0.6925 1.2779 -0.2222 -0.5771 0.0989  105 PHE A O   
169  C CB  . PHE A 31  ? 1.2114 0.6717 1.2209 -0.2344 -0.5798 0.1275  105 PHE A CB  
170  C CG  . PHE A 31  ? 1.1174 0.6361 1.2038 -0.2200 -0.5743 0.1477  105 PHE A CG  
171  C CD1 . PHE A 31  ? 1.1640 0.6966 1.2651 -0.2354 -0.5930 0.1798  105 PHE A CD1 
172  C CD2 . PHE A 31  ? 1.0640 0.6222 1.2054 -0.1922 -0.5481 0.1350  105 PHE A CD2 
173  C CE1 . PHE A 31  ? 1.1154 0.6968 1.2812 -0.2229 -0.5827 0.1970  105 PHE A CE1 
174  C CE2 . PHE A 31  ? 0.9585 0.5664 1.1652 -0.1794 -0.5394 0.1531  105 PHE A CE2 
175  C CZ  . PHE A 31  ? 1.0820 0.6993 1.2987 -0.1948 -0.5551 0.1832  105 PHE A CZ  
176  N N   . PHE A 32  ? 1.2471 0.6139 1.1911 -0.2026 -0.5427 0.0523  106 PHE A N   
177  C CA  . PHE A 32  ? 1.2277 0.5866 1.1873 -0.1794 -0.5236 0.0318  106 PHE A CA  
178  C C   . PHE A 32  ? 1.3236 0.6106 1.2208 -0.1886 -0.5358 0.0225  106 PHE A C   
179  O O   . PHE A 32  ? 1.3415 0.6364 1.2655 -0.1823 -0.5382 0.0281  106 PHE A O   
180  C CB  . PHE A 32  ? 1.1968 0.5437 1.1454 -0.1567 -0.4926 -0.0005 106 PHE A CB  
181  C CG  . PHE A 32  ? 1.1540 0.4941 1.1205 -0.1287 -0.4693 -0.0211 106 PHE A CG  
182  C CD1 . PHE A 32  ? 1.0762 0.4716 1.1158 -0.1190 -0.4685 -0.0048 106 PHE A CD1 
183  C CD2 . PHE A 32  ? 1.1896 0.4704 1.0995 -0.1098 -0.4468 -0.0561 106 PHE A CD2 
184  C CE1 . PHE A 32  ? 1.0953 0.4868 1.1527 -0.0933 -0.4471 -0.0215 106 PHE A CE1 
185  C CE2 . PHE A 32  ? 1.2094 0.4856 1.1368 -0.0797 -0.4235 -0.0730 106 PHE A CE2 
186  C CZ  . PHE A 32  ? 1.1291 0.4608 1.1313 -0.0725 -0.4242 -0.0548 106 PHE A CZ  
187  N N   . GLN A 33  ? 1.3457 0.5613 1.1576 -0.2047 -0.5443 0.0092  107 GLN A N   
188  C CA  . GLN A 33  ? 1.4931 0.6310 1.2371 -0.2119 -0.5537 -0.0029 107 GLN A CA  
189  C C   . GLN A 33  ? 1.4478 0.5883 1.1924 -0.2398 -0.5875 0.0289  107 GLN A C   
190  O O   . GLN A 33  ? 1.5386 0.6283 1.2465 -0.2442 -0.5966 0.0243  107 GLN A O   
191  C CB  . GLN A 33  ? 1.5286 0.5890 1.1784 -0.2186 -0.5492 -0.0292 107 GLN A CB  
192  C CG  . GLN A 33  ? 1.6225 0.6790 1.2659 -0.1901 -0.5149 -0.0613 107 GLN A CG  
193  C CD  . GLN A 33  ? 1.7262 0.7230 1.2830 -0.1989 -0.5105 -0.0838 107 GLN A CD  
194  O OE1 . GLN A 33  ? 1.6997 0.6556 1.2001 -0.2274 -0.5333 -0.0753 107 GLN A OE1 
195  N NE2 . GLN A 33  ? 1.7402 0.7334 1.2842 -0.1749 -0.4808 -0.1123 107 GLN A NE2 
196  N N   . GLN A 34  ? 1.4190 0.6163 1.2037 -0.2572 -0.6054 0.0618  108 GLN A N   
197  C CA  . GLN A 34  ? 1.4413 0.6443 1.2261 -0.2836 -0.6366 0.0947  108 GLN A CA  
198  C C   . GLN A 34  ? 1.3687 0.6406 1.2355 -0.2746 -0.6384 0.1189  108 GLN A C   
199  O O   . GLN A 34  ? 1.4366 0.7019 1.2975 -0.2925 -0.6606 0.1405  108 GLN A O   
200  C CB  . GLN A 34  ? 1.5246 0.7445 1.3000 -0.3083 -0.6556 0.1203  108 GLN A CB  
201  C CG  . GLN A 34  ? 1.6386 0.7910 1.3279 -0.3239 -0.6586 0.1018  108 GLN A CG  
202  C CD  . GLN A 34  ? 1.6937 0.8569 1.3685 -0.3538 -0.6831 0.1323  108 GLN A CD  
203  O OE1 . GLN A 34  ? 1.7303 0.9137 1.4220 -0.3728 -0.7061 0.1651  108 GLN A OE1 
204  N NE2 . GLN A 34  ? 1.7099 0.8605 1.3530 -0.3587 -0.6777 0.1229  108 GLN A NE2 
205  N N   . SER A 35  ? 1.3038 0.6408 1.2444 -0.2486 -0.6155 0.1170  109 SER A N   
206  C CA  . SER A 35  ? 1.2085 0.6131 1.2269 -0.2391 -0.6140 0.1407  109 SER A CA  
207  C C   . SER A 35  ? 1.1969 0.6042 1.2409 -0.2162 -0.5966 0.1218  109 SER A C   
208  O O   . SER A 35  ? 1.1428 0.6065 1.2515 -0.2064 -0.5923 0.1393  109 SER A O   
209  C CB  . SER A 35  ? 1.1309 0.6110 1.2191 -0.2267 -0.6000 0.1580  109 SER A CB  
210  O OG  . SER A 35  ? 1.2506 0.7367 1.3283 -0.2487 -0.6180 0.1850  109 SER A OG  
211  N N   . PHE A 36  ? 1.2414 0.5863 1.2342 -0.2063 -0.5841 0.0874  110 PHE A N   
212  C CA  . PHE A 36  ? 1.2278 0.5736 1.2453 -0.1812 -0.5633 0.0684  110 PHE A CA  
213  C C   . PHE A 36  ? 1.3347 0.5867 1.2739 -0.1812 -0.5643 0.0439  110 PHE A C   
214  O O   . PHE A 36  ? 1.4432 0.6268 1.3053 -0.1943 -0.5719 0.0316  110 PHE A O   
215  C CB  . PHE A 36  ? 1.1735 0.5526 1.2276 -0.1533 -0.5304 0.0478  110 PHE A CB  
216  C CG  . PHE A 36  ? 1.0661 0.5355 1.2004 -0.1480 -0.5250 0.0696  110 PHE A CG  
217  C CD1 . PHE A 36  ? 0.9209 0.4566 1.1321 -0.1329 -0.5153 0.0828  110 PHE A CD1 
218  C CD2 . PHE A 36  ? 1.0282 0.5128 1.1581 -0.1571 -0.5283 0.0780  110 PHE A CD2 
219  C CE1 . PHE A 36  ? 0.9222 0.5314 1.2003 -0.1241 -0.5049 0.1026  110 PHE A CE1 
220  C CE2 . PHE A 36  ? 0.9575 0.5165 1.1565 -0.1487 -0.5198 0.0983  110 PHE A CE2 
221  C CZ  . PHE A 36  ? 0.8997 0.5176 1.1704 -0.1309 -0.5058 0.1099  110 PHE A CZ  
222  N N   . GLN A 37  ? 1.2807 0.5295 1.2398 -0.1654 -0.5555 0.0375  111 GLN A N   
223  C CA  . GLN A 37  ? 1.4083 0.5707 1.3024 -0.1545 -0.5481 0.0120  111 GLN A CA  
224  C C   . GLN A 37  ? 1.3824 0.5539 1.3010 -0.1158 -0.5096 -0.0140 111 GLN A C   
225  O O   . GLN A 37  ? 1.3271 0.5595 1.3167 -0.1007 -0.4982 -0.0060 111 GLN A O   
226  C CB  . GLN A 37  ? 1.4543 0.6016 1.3483 -0.1671 -0.5700 0.0284  111 GLN A CB  
227  C CG  . GLN A 37  ? 1.6170 0.6664 1.4373 -0.1581 -0.5665 0.0052  111 GLN A CG  
228  C CD  . GLN A 37  ? 1.7091 0.7553 1.5458 -0.1637 -0.5822 0.0203  111 GLN A CD  
229  O OE1 . GLN A 37  ? 1.6376 0.7582 1.5416 -0.1746 -0.5953 0.0479  111 GLN A OE1 
230  N NE2 . GLN A 37  ? 1.8813 0.8409 1.6555 -0.1552 -0.5805 0.0024  111 GLN A NE2 
231  N N   . ARG A 38  ? 1.4077 0.5234 1.2685 -0.0994 -0.4890 -0.0438 112 ARG A N   
232  C CA  . ARG A 38  ? 1.3605 0.4795 1.2353 -0.0594 -0.4507 -0.0687 112 ARG A CA  
233  C C   . ARG A 38  ? 1.3718 0.4550 1.2388 -0.0393 -0.4423 -0.0759 112 ARG A C   
234  O O   . ARG A 38  ? 1.4767 0.4800 1.2753 -0.0449 -0.4534 -0.0847 112 ARG A O   
235  C CB  . ARG A 38  ? 1.3992 0.4635 1.2055 -0.0461 -0.4318 -0.0991 112 ARG A CB  
236  C CG  . ARG A 38  ? 1.4019 0.5025 1.2168 -0.0611 -0.4346 -0.0950 112 ARG A CG  
237  C CD  . ARG A 38  ? 1.4928 0.5384 1.2358 -0.0467 -0.4143 -0.1274 112 ARG A CD  
238  N NE  . ARG A 38  ? 1.5285 0.5909 1.2595 -0.0706 -0.4253 -0.1215 112 ARG A NE  
239  C CZ  . ARG A 38  ? 1.5678 0.5967 1.2417 -0.0650 -0.4111 -0.1458 112 ARG A CZ  
240  N NH1 . ARG A 38  ? 1.6170 0.5968 1.2402 -0.0335 -0.3833 -0.1791 112 ARG A NH1 
241  N NH2 . ARG A 38  ? 1.5561 0.6048 1.2233 -0.0905 -0.4245 -0.1356 112 ARG A NH2 
242  N N   . LEU A 39  ? 1.3215 0.4632 1.2574 -0.0165 -0.4230 -0.0713 113 LEU A N   
243  C CA  . LEU A 39  ? 1.3212 0.4345 1.2541 0.0058  -0.4121 -0.0768 113 LEU A CA  
244  C C   . LEU A 39  ? 1.3367 0.4325 1.2542 0.0518  -0.3701 -0.1047 113 LEU A C   
245  O O   . LEU A 39  ? 1.4282 0.4530 1.2904 0.0709  -0.3610 -0.1220 113 LEU A O   
246  C CB  . LEU A 39  ? 1.2297 0.4199 1.2468 -0.0005 -0.4199 -0.0505 113 LEU A CB  
247  C CG  . LEU A 39  ? 1.2433 0.4544 1.2766 -0.0423 -0.4613 -0.0211 113 LEU A CG  
248  C CD1 . LEU A 39  ? 1.1543 0.4450 1.2715 -0.0456 -0.4666 0.0023  113 LEU A CD1 
249  C CD2 . LEU A 39  ? 1.3417 0.4610 1.2958 -0.0603 -0.4863 -0.0228 113 LEU A CD2 
250  N N   . SER A 40  ? 1.2527 0.4142 1.2178 0.0710  -0.3441 -0.1090 114 SER A N   
251  C CA  . SER A 40  ? 1.2616 0.4197 1.2156 0.1160  -0.3028 -0.1332 114 SER A CA  
252  C C   . SER A 40  ? 1.1851 0.4055 1.1723 0.1246  -0.2832 -0.1386 114 SER A C   
253  O O   . SER A 40  ? 1.1382 0.4218 1.1819 0.1020  -0.2967 -0.1194 114 SER A O   
254  C CB  . SER A 40  ? 1.2283 0.4182 1.2271 0.1431  -0.2832 -0.1259 114 SER A CB  
255  O OG  . SER A 40  ? 1.1916 0.4789 1.2779 0.1371  -0.2805 -0.1042 114 SER A OG  
256  N N   . ARG A 41  ? 1.2183 0.4227 1.1702 0.1581  -0.2510 -0.1652 115 ARG A N   
257  C CA  . ARG A 41  ? 1.1558 0.4162 1.1318 0.1703  -0.2291 -0.1737 115 ARG A CA  
258  C C   . ARG A 41  ? 1.1059 0.4540 1.1566 0.1985  -0.1980 -0.1646 115 ARG A C   
259  O O   . ARG A 41  ? 1.0868 0.4338 1.1292 0.2327  -0.1693 -0.1740 115 ARG A O   
260  C CB  . ARG A 41  ? 1.2382 0.4475 1.1370 0.1909  -0.2092 -0.2067 115 ARG A CB  
261  C CG  . ARG A 41  ? 1.1931 0.4438 1.0977 0.1912  -0.1977 -0.2165 115 ARG A CG  
262  C CD  . ARG A 41  ? 1.3190 0.5144 1.1347 0.2044  -0.1828 -0.2495 115 ARG A CD  
263  N NE  . ARG A 41  ? 1.3940 0.5800 1.1842 0.2477  -0.1472 -0.2695 115 ARG A NE  
264  C CZ  . ARG A 41  ? 1.5787 0.6879 1.3035 0.2549  -0.1485 -0.2848 115 ARG A CZ  
265  N NH1 . ARG A 41  ? 1.6417 0.6749 1.3124 0.2210  -0.1825 -0.2839 115 ARG A NH1 
266  N NH2 . ARG A 41  ? 1.5850 0.6985 1.3009 0.2959  -0.1149 -0.2997 115 ARG A NH2 
267  N N   . LEU A 42  ? 1.0184 0.4468 1.1426 0.1824  -0.2027 -0.1444 116 LEU A N   
268  C CA  . LEU A 42  ? 0.8970 0.4173 1.0909 0.2022  -0.1733 -0.1327 116 LEU A CA  
269  C C   . LEU A 42  ? 0.9098 0.4718 1.1002 0.2324  -0.1339 -0.1499 116 LEU A C   
270  O O   . LEU A 42  ? 0.9706 0.5805 1.1802 0.2593  -0.1004 -0.1475 116 LEU A O   
271  C CB  . LEU A 42  ? 0.7614 0.3574 1.0324 0.1724  -0.1894 -0.1065 116 LEU A CB  
272  C CG  . LEU A 42  ? 0.7853 0.3697 1.0768 0.1443  -0.2230 -0.0856 116 LEU A CG  
273  C CD1 . LEU A 42  ? 0.7566 0.4217 1.1232 0.1158  -0.2359 -0.0630 116 LEU A CD1 
274  C CD2 . LEU A 42  ? 0.7732 0.3574 1.0698 0.1627  -0.2102 -0.0811 116 LEU A CD2 
275  N N   . GLY A 43  ? 0.9416 0.4899 1.1058 0.2260  -0.1376 -0.1652 117 GLY A N   
276  C CA  . GLY A 43  ? 0.9089 0.5016 1.0674 0.2520  -0.1014 -0.1825 117 GLY A CA  
277  C C   . GLY A 43  ? 0.9912 0.5387 1.0949 0.2432  -0.1125 -0.2050 117 GLY A C   
278  O O   . GLY A 43  ? 1.0202 0.5304 1.1114 0.2073  -0.1471 -0.1965 117 GLY A O   
279  N N   . HIS A 44  ? 1.0683 0.6314 1.1337 0.2697  -0.0792 -0.2281 118 HIS A N   
280  C CA  . HIS A 44  ? 1.1272 0.6787 1.1349 0.2509  -0.0776 -0.2401 118 HIS A CA  
281  C C   . HIS A 44  ? 1.1077 0.7456 1.1279 0.2696  -0.0353 -0.2466 118 HIS A C   
282  O O   . HIS A 44  ? 1.1888 0.8543 1.2114 0.3092  -0.0031 -0.2589 118 HIS A O   
283  C CB  . HIS A 44  ? 1.1821 0.6276 1.0893 0.2557  -0.0874 -0.2671 118 HIS A CB  
284  C CG  . HIS A 44  ? 1.2152 0.6388 1.0876 0.3024  -0.0574 -0.2901 118 HIS A CG  
285  N ND1 . HIS A 44  ? 1.2228 0.7205 1.1049 0.3335  -0.0126 -0.2991 118 HIS A ND1 
286  C CD2 . HIS A 44  ? 1.3384 0.6952 1.1727 0.3105  -0.0612 -0.2949 118 HIS A CD2 
287  C CE1 . HIS A 44  ? 1.2792 0.7567 1.1359 0.3592  0.0085  -0.3078 118 HIS A CE1 
288  N NE2 . HIS A 44  ? 1.2544 0.6435 1.0810 0.3481  -0.0203 -0.3075 118 HIS A NE2 
289  N N   . GLY A 45  ? 1.1118 0.7931 1.1404 0.2404  -0.0367 -0.2368 119 GLY A N   
290  C CA  . GLY A 45  ? 1.1385 0.8948 1.1667 0.2487  -0.0011 -0.2421 119 GLY A CA  
291  C C   . GLY A 45  ? 1.1661 0.9125 1.1507 0.2138  -0.0126 -0.2420 119 GLY A C   
292  O O   . GLY A 45  ? 1.2113 0.8818 1.1460 0.1919  -0.0426 -0.2460 119 GLY A O   
293  N N   . SER A 46  ? 1.1644 0.9854 1.1648 0.2061  0.0095  -0.2362 120 SER A N   
294  C CA  . SER A 46  ? 1.2102 1.0241 1.1754 0.1698  -0.0044 -0.2315 120 SER A CA  
295  C C   . SER A 46  ? 1.2055 1.0022 1.2112 0.1354  -0.0434 -0.2064 120 SER A C   
296  O O   . SER A 46  ? 1.2012 0.9559 1.1670 0.1056  -0.0689 -0.2030 120 SER A O   
297  C CB  . SER A 46  ? 1.2162 1.1140 1.1909 0.1675  0.0269  -0.2285 120 SER A CB  
298  O OG  . SER A 46  ? 1.1789 1.1472 1.2358 0.1675  0.0352  -0.2080 120 SER A OG  
299  N N   . TYR A 47  ? 1.1474 0.9793 1.2322 0.1397  -0.0482 -0.1883 121 TYR A N   
300  C CA  . TYR A 47  ? 1.0517 0.8757 1.1818 0.1114  -0.0831 -0.1643 121 TYR A CA  
301  C C   . TYR A 47  ? 1.0478 0.7861 1.1390 0.0958  -0.1211 -0.1653 121 TYR A C   
302  O O   . TYR A 47  ? 1.0201 0.7421 1.1211 0.0659  -0.1530 -0.1479 121 TYR A O   
303  C CB  . TYR A 47  ? 1.0067 0.8836 1.2245 0.1226  -0.0783 -0.1482 121 TYR A CB  
304  C CG  . TYR A 47  ? 1.0424 0.8998 1.2678 0.1519  -0.0715 -0.1575 121 TYR A CG  
305  C CD1 . TYR A 47  ? 1.0077 0.8069 1.2357 0.1458  -0.1033 -0.1521 121 TYR A CD1 
306  C CD2 . TYR A 47  ? 1.0592 0.9568 1.2879 0.1851  -0.0343 -0.1701 121 TYR A CD2 
307  C CE1 . TYR A 47  ? 0.9611 0.7361 1.1923 0.1717  -0.0988 -0.1596 121 TYR A CE1 
308  C CE2 . TYR A 47  ? 1.0358 0.9129 1.2710 0.2141  -0.0289 -0.1774 121 TYR A CE2 
309  C CZ  . TYR A 47  ? 0.9902 0.8026 1.2253 0.2073  -0.0615 -0.1724 121 TYR A CZ  
310  O OH  . TYR A 47  ? 0.9689 0.7553 1.2071 0.2356  -0.0574 -0.1787 121 TYR A OH  
311  N N   . GLY A 48  ? 1.0908 0.7735 1.1369 0.1155  -0.1189 -0.1847 122 GLY A N   
312  C CA  . GLY A 48  ? 1.0627 0.6594 1.0674 0.0997  -0.1550 -0.1863 122 GLY A CA  
313  C C   . GLY A 48  ? 1.0589 0.6198 1.0708 0.1239  -0.1559 -0.1933 122 GLY A C   
314  O O   . GLY A 48  ? 1.1123 0.6887 1.1205 0.1597  -0.1241 -0.2095 122 GLY A O   
315  N N   . GLU A 49  ? 0.9773 0.4921 0.9996 0.1044  -0.1930 -0.1799 123 GLU A N   
316  C CA  . GLU A 49  ? 1.0229 0.4966 1.0505 0.1220  -0.1997 -0.1831 123 GLU A CA  
317  C C   . GLU A 49  ? 0.8794 0.3887 0.9892 0.1059  -0.2230 -0.1536 123 GLU A C   
318  O O   . GLU A 49  ? 0.8573 0.3917 0.9988 0.0754  -0.2458 -0.1327 123 GLU A O   
319  C CB  . GLU A 49  ? 1.1248 0.4875 1.0646 0.1121  -0.2250 -0.1992 123 GLU A CB  
320  C CG  . GLU A 49  ? 1.2369 0.5543 1.0905 0.1362  -0.1993 -0.2333 123 GLU A CG  
321  C CD  . GLU A 49  ? 1.3398 0.6307 1.1279 0.1080  -0.2092 -0.2407 123 GLU A CD  
322  O OE1 . GLU A 49  ? 1.2981 0.6450 1.1217 0.0836  -0.2151 -0.2221 123 GLU A OE1 
323  O OE2 . GLU A 49  ? 1.4654 0.6766 1.1643 0.1100  -0.2118 -0.2654 123 GLU A OE2 
324  N N   . VAL A 50  ? 0.8907 0.4028 1.0342 0.1276  -0.2172 -0.1517 124 VAL A N   
325  C CA  . VAL A 50  ? 0.7923 0.3401 1.0056 0.1117  -0.2369 -0.1236 124 VAL A CA  
326  C C   . VAL A 50  ? 0.8685 0.3564 1.0422 0.1085  -0.2522 -0.1223 124 VAL A C   
327  O O   . VAL A 50  ? 0.9273 0.3919 1.0747 0.1382  -0.2302 -0.1371 124 VAL A O   
328  C CB  . VAL A 50  ? 0.7297 0.3745 1.0229 0.1315  -0.2065 -0.1129 124 VAL A CB  
329  C CG1 . VAL A 50  ? 0.6873 0.3809 1.0441 0.1077  -0.2250 -0.0837 124 VAL A CG1 
330  C CG2 . VAL A 50  ? 0.6721 0.3790 0.9918 0.1359  -0.1838 -0.1158 124 VAL A CG2 
331  N N   . PHE A 51  ? 0.8674 0.3348 1.0374 0.0731  -0.2888 -0.1034 125 PHE A N   
332  C CA  . PHE A 51  ? 0.9398 0.3480 1.0690 0.0640  -0.3079 -0.1004 125 PHE A CA  
333  C C   . PHE A 51  ? 0.8766 0.3382 1.0734 0.0501  -0.3231 -0.0731 125 PHE A C   
334  O O   . PHE A 51  ? 0.8086 0.3365 1.0669 0.0308  -0.3356 -0.0521 125 PHE A O   
335  C CB  . PHE A 51  ? 1.0223 0.3646 1.0831 0.0319  -0.3392 -0.1001 125 PHE A CB  
336  C CG  . PHE A 51  ? 1.0989 0.3811 1.0817 0.0406  -0.3276 -0.1283 125 PHE A CG  
337  C CD1 . PHE A 51  ? 1.1955 0.4042 1.1064 0.0615  -0.3142 -0.1535 125 PHE A CD1 
338  C CD2 . PHE A 51  ? 1.0778 0.3782 1.0576 0.0273  -0.3300 -0.1297 125 PHE A CD2 
339  C CE1 . PHE A 51  ? 1.2679 0.4265 1.1048 0.0699  -0.3020 -0.1811 125 PHE A CE1 
340  C CE2 . PHE A 51  ? 1.1504 0.3981 1.0545 0.0329  -0.3200 -0.1564 125 PHE A CE2 
341  C CZ  . PHE A 51  ? 1.2780 0.4567 1.1100 0.0546  -0.3053 -0.1829 125 PHE A CZ  
342  N N   . LYS A 52  ? 0.9136 0.3465 1.0979 0.0603  -0.3221 -0.0736 126 LYS A N   
343  C CA  . LYS A 52  ? 0.9135 0.3764 1.1415 0.0399  -0.3454 -0.0489 126 LYS A CA  
344  C C   . LYS A 52  ? 1.0224 0.4317 1.2018 0.0059  -0.3841 -0.0389 126 LYS A C   
345  O O   . LYS A 52  ? 1.1369 0.4607 1.2394 0.0065  -0.3898 -0.0530 126 LYS A O   
346  C CB  . LYS A 52  ? 0.9919 0.4424 1.2222 0.0624  -0.3305 -0.0520 126 LYS A CB  
347  C CG  . LYS A 52  ? 0.9467 0.4127 1.2084 0.0393  -0.3584 -0.0285 126 LYS A CG  
348  C CD  . LYS A 52  ? 1.0027 0.4500 1.2612 0.0621  -0.3434 -0.0318 126 LYS A CD  
349  C CE  . LYS A 52  ? 1.1064 0.4722 1.3081 0.0467  -0.3719 -0.0286 126 LYS A CE  
350  N NZ  . LYS A 52  ? 1.1863 0.5279 1.3827 0.0697  -0.3585 -0.0308 126 LYS A NZ  
351  N N   . VAL A 53  ? 1.0073 0.4692 1.2296 -0.0223 -0.4093 -0.0141 127 VAL A N   
352  C CA  . VAL A 53  ? 1.0434 0.4677 1.2218 -0.0543 -0.4444 -0.0005 127 VAL A CA  
353  C C   . VAL A 53  ? 1.0071 0.4781 1.2338 -0.0739 -0.4704 0.0301  127 VAL A C   
354  O O   . VAL A 53  ? 0.9553 0.5045 1.2605 -0.0668 -0.4633 0.0436  127 VAL A O   
355  C CB  . VAL A 53  ? 0.9969 0.4358 1.1671 -0.0687 -0.4514 0.0037  127 VAL A CB  
356  C CG1 . VAL A 53  ? 1.0196 0.4162 1.1427 -0.0501 -0.4260 -0.0263 127 VAL A CG1 
357  C CG2 . VAL A 53  ? 0.9045 0.4429 1.1634 -0.0702 -0.4504 0.0262  127 VAL A CG2 
358  N N   . ARG A 54  ? 1.1025 0.5250 1.2795 -0.0986 -0.5003 0.0414  128 ARG A N   
359  C CA  . ARG A 54  ? 1.0889 0.5529 1.2999 -0.1207 -0.5286 0.0750  128 ARG A CA  
360  C C   . ARG A 54  ? 1.0406 0.5031 1.2268 -0.1440 -0.5491 0.0922  128 ARG A C   
361  O O   . ARG A 54  ? 1.1107 0.5050 1.2238 -0.1551 -0.5564 0.0785  128 ARG A O   
362  C CB  . ARG A 54  ? 1.2383 0.6484 1.4120 -0.1314 -0.5472 0.0783  128 ARG A CB  
363  C CG  . ARG A 54  ? 1.2000 0.6661 1.4243 -0.1464 -0.5688 0.1133  128 ARG A CG  
364  C CD  . ARG A 54  ? 1.3093 0.7181 1.4917 -0.1608 -0.5907 0.1176  128 ARG A CD  
365  N NE  . ARG A 54  ? 1.3139 0.7124 1.5121 -0.1398 -0.5734 0.1018  128 ARG A NE  
366  C CZ  . ARG A 54  ? 1.2121 0.6795 1.4828 -0.1320 -0.5684 0.1162  128 ARG A CZ  
367  N NH1 . ARG A 54  ? 1.1387 0.6887 1.4725 -0.1376 -0.5746 0.1464  128 ARG A NH1 
368  N NH2 . ARG A 54  ? 1.1347 0.5834 1.4110 -0.1145 -0.5531 0.1019  128 ARG A NH2 
369  N N   . SER A 55  ? 1.0095 0.5436 1.2533 -0.1486 -0.5543 0.1227  129 SER A N   
370  C CA  . SER A 55  ? 1.1006 0.6371 1.3261 -0.1673 -0.5686 0.1418  129 SER A CA  
371  C C   . SER A 55  ? 1.2780 0.7639 1.4468 -0.1977 -0.6013 0.1577  129 SER A C   
372  O O   . SER A 55  ? 1.3655 0.8532 1.5427 -0.2053 -0.6139 0.1732  129 SER A O   
373  C CB  . SER A 55  ? 1.1156 0.7283 1.4111 -0.1590 -0.5543 0.1701  129 SER A CB  
374  O OG  . SER A 55  ? 1.2228 0.8338 1.5005 -0.1807 -0.5690 0.1942  129 SER A OG  
375  N N   . LYS A 56  ? 1.3829 0.8101 1.4301 -0.2923 -0.3849 0.1598  130 LYS A N   
376  C CA  . LYS A 56  ? 1.2515 0.6549 1.2930 -0.3199 -0.4185 0.1746  130 LYS A CA  
377  C C   . LYS A 56  ? 1.2107 0.6973 1.3266 -0.3570 -0.4048 0.1973  130 LYS A C   
378  O O   . LYS A 56  ? 1.3615 0.8386 1.4837 -0.3843 -0.4311 0.2141  130 LYS A O   
379  C CB  . LYS A 56  ? 1.1972 0.5521 1.2032 -0.3001 -0.4454 0.1543  130 LYS A CB  
380  C CG  . LYS A 56  ? 1.2780 0.5402 1.2016 -0.2678 -0.4648 0.1337  130 LYS A CG  
381  C CD  . LYS A 56  ? 1.3724 0.5906 1.2560 -0.2492 -0.4858 0.1133  130 LYS A CD  
382  C CE  . LYS A 56  ? 1.5213 0.6495 1.3209 -0.2145 -0.4999 0.0904  130 LYS A CE  
383  N NZ  . LYS A 56  ? 1.6071 0.6892 1.3579 -0.1970 -0.5171 0.0704  130 LYS A NZ  
384  N N   . GLU A 57  ? 1.4199 0.9882 1.5925 -0.3573 -0.3640 0.1973  131 GLU A N   
385  C CA  . GLU A 57  ? 1.3969 1.0530 1.6442 -0.3874 -0.3429 0.2151  131 GLU A CA  
386  C C   . GLU A 57  ? 1.3962 1.0761 1.6506 -0.4176 -0.3242 0.2399  131 GLU A C   
387  O O   . GLU A 57  ? 1.4546 1.1400 1.7226 -0.4514 -0.3370 0.2623  131 GLU A O   
388  C CB  . GLU A 57  ? 1.4772 1.2097 1.7789 -0.3692 -0.3079 0.1992  131 GLU A CB  
389  C CG  . GLU A 57  ? 1.4537 1.2854 1.8344 -0.3926 -0.2762 0.2124  131 GLU A CG  
390  C CD  . GLU A 57  ? 1.3578 1.2372 1.7502 -0.3987 -0.2330 0.2193  131 GLU A CD  
391  O OE1 . GLU A 57  ? 1.3439 1.2204 1.7176 -0.3735 -0.2160 0.2049  131 GLU A OE1 
392  O OE2 . GLU A 57  ? 1.3051 1.2229 1.7225 -0.4296 -0.2164 0.2400  131 GLU A OE2 
393  N N   . ASP A 58  ? 1.2896 0.9817 1.5318 -0.4071 -0.2949 0.2376  132 ASP A N   
394  C CA  . ASP A 58  ? 1.3115 1.0243 1.5518 -0.4351 -0.2744 0.2610  132 ASP A CA  
395  C C   . ASP A 58  ? 1.3400 0.9664 1.5049 -0.4331 -0.2985 0.2684  132 ASP A C   
396  O O   . ASP A 58  ? 1.2615 0.8865 1.4121 -0.4617 -0.2938 0.2914  132 ASP A O   
397  C CB  . ASP A 58  ? 1.2328 1.0227 1.5092 -0.4293 -0.2237 0.2572  132 ASP A CB  
398  C CG  . ASP A 58  ? 1.2326 0.9959 1.4776 -0.3927 -0.2179 0.2379  132 ASP A CG  
399  O OD1 . ASP A 58  ? 1.2352 0.9200 1.4294 -0.3708 -0.2495 0.2271  132 ASP A OD1 
400  O OD2 . ASP A 58  ? 1.1179 0.9401 1.3892 -0.3849 -0.1807 0.2330  132 ASP A OD2 
401  N N   . GLY A 59  ? 1.3653 0.9204 1.4813 -0.3987 -0.3233 0.2484  133 GLY A N   
402  C CA  . GLY A 59  ? 1.3904 0.8629 1.4376 -0.3904 -0.3481 0.2518  133 GLY A CA  
403  C C   . GLY A 59  ? 1.3877 0.8675 1.4188 -0.3832 -0.3241 0.2567  133 GLY A C   
404  O O   . GLY A 59  ? 1.4371 0.8639 1.4200 -0.3897 -0.3415 0.2694  133 GLY A O   
405  N N   . ARG A 60  ? 1.2625 0.8048 1.3305 -0.3705 -0.2873 0.2478  134 ARG A N   
406  C CA  . ARG A 60  ? 1.1868 0.7315 1.2352 -0.3590 -0.2676 0.2506  134 ARG A CA  
407  C C   . ARG A 60  ? 1.1675 0.6656 1.1906 -0.3119 -0.2795 0.2261  134 ARG A C   
408  O O   . ARG A 60  ? 1.1605 0.6428 1.1894 -0.2880 -0.2911 0.2042  134 ARG A O   
409  C CB  . ARG A 60  ? 1.1821 0.8203 1.2803 -0.3714 -0.2203 0.2551  134 ARG A CB  
410  C CG  . ARG A 60  ? 1.1986 0.8896 1.3215 -0.4140 -0.1987 0.2782  134 ARG A CG  
411  C CD  . ARG A 60  ? 1.1949 0.9706 1.3527 -0.4196 -0.1479 0.2796  134 ARG A CD  
412  N NE  . ARG A 60  ? 1.3572 1.1833 1.5380 -0.4571 -0.1225 0.2993  134 ARG A NE  
413  C CZ  . ARG A 60  ? 1.5115 1.3223 1.6515 -0.4817 -0.1131 0.3209  134 ARG A CZ  
414  N NH1 . ARG A 60  ? 1.5011 1.2495 1.5754 -0.4724 -0.1284 0.3260  134 ARG A NH1 
415  N NH2 . ARG A 60  ? 1.4919 1.3501 1.6579 -0.5161 -0.0888 0.3379  134 ARG A NH2 
416  N N   . LEU A 61  ? 1.1787 0.6554 1.1722 -0.2978 -0.2761 0.2301  135 LEU A N   
417  C CA  . LEU A 61  ? 1.1391 0.5774 1.1138 -0.2505 -0.2849 0.2087  135 LEU A CA  
418  C C   . LEU A 61  ? 1.0061 0.5059 1.0219 -0.2358 -0.2533 0.1984  135 LEU A C   
419  O O   . LEU A 61  ? 1.0002 0.5503 1.0312 -0.2544 -0.2271 0.2131  135 LEU A O   
420  C CB  . LEU A 61  ? 1.1542 0.5398 1.0815 -0.2395 -0.3022 0.2184  135 LEU A CB  
421  C CG  . LEU A 61  ? 1.2069 0.5247 1.0916 -0.2504 -0.3385 0.2254  135 LEU A CG  
422  C CD1 . LEU A 61  ? 1.2422 0.5120 1.0830 -0.2432 -0.3573 0.2364  135 LEU A CD1 
423  C CD2 . LEU A 61  ? 1.2458 0.5186 1.1196 -0.2180 -0.3599 0.1987  135 LEU A CD2 
424  N N   . TYR A 62  ? 0.9647 0.4598 0.9942 -0.2029 -0.2552 0.1726  136 TYR A N   
425  C CA  . TYR A 62  ? 0.9765 0.5426 1.0386 -0.1748 -0.2229 0.1534  136 TYR A CA  
426  C C   . TYR A 62  ? 0.9558 0.4894 0.9990 -0.1228 -0.2303 0.1282  136 TYR A C   
427  O O   . TYR A 62  ? 0.9326 0.3873 0.9403 -0.1068 -0.2594 0.1228  136 TYR A O   
428  C CB  . TYR A 62  ? 0.9215 0.5478 1.0303 -0.1867 -0.2062 0.1435  136 TYR A CB  
429  C CG  . TYR A 62  ? 0.9527 0.6257 1.0948 -0.2347 -0.1941 0.1667  136 TYR A CG  
430  C CD1 . TYR A 62  ? 0.9275 0.6760 1.0954 -0.2438 -0.1576 0.1732  136 TYR A CD1 
431  C CD2 . TYR A 62  ? 0.9815 0.6326 1.1266 -0.2649 -0.2147 0.1782  136 TYR A CD2 
432  C CE1 . TYR A 62  ? 0.9548 0.7526 1.1566 -0.2851 -0.1405 0.1931  136 TYR A CE1 
433  C CE2 . TYR A 62  ? 0.9627 0.6740 1.1427 -0.3007 -0.1964 0.1957  136 TYR A CE2 
434  C CZ  . TYR A 62  ? 0.9388 0.7224 1.1492 -0.3115 -0.1582 0.2034  136 TYR A CZ  
435  O OH  . TYR A 62  ? 0.9341 0.7794 1.1790 -0.3418 -0.1346 0.2173  136 TYR A OH  
436  N N   . ALA A 63  ? 0.8554 0.4509 0.9229 -0.0962 -0.2030 0.1128  137 ALA A N   
437  C CA  . ALA A 63  ? 0.8165 0.4036 0.8793 -0.0489 -0.2011 0.0884  137 ALA A CA  
438  C C   . ALA A 63  ? 0.7701 0.4060 0.8594 -0.0410 -0.1812 0.0683  137 ALA A C   
439  O O   . ALA A 63  ? 0.7987 0.5025 0.9196 -0.0544 -0.1584 0.0707  137 ALA A O   
440  C CB  . ALA A 63  ? 0.7903 0.4051 0.8583 -0.0260 -0.1910 0.0910  137 ALA A CB  
441  N N   . VAL A 64  ? 0.7751 0.3709 0.8458 -0.0193 -0.1907 0.0483  138 VAL A N   
442  C CA  . VAL A 64  ? 0.7681 0.3971 0.8530 -0.0126 -0.1765 0.0297  138 VAL A CA  
443  C C   . VAL A 64  ? 0.7687 0.4060 0.8463 0.0305  -0.1612 0.0088  138 VAL A C   
444  O O   . VAL A 64  ? 0.8504 0.4357 0.8997 0.0588  -0.1710 -0.0001 138 VAL A O   
445  C CB  . VAL A 64  ? 0.8132 0.3885 0.8770 -0.0287 -0.2000 0.0245  138 VAL A CB  
446  C CG1 . VAL A 64  ? 0.8244 0.4219 0.8919 -0.0182 -0.1893 0.0045  138 VAL A CG1 
447  C CG2 . VAL A 64  ? 0.8291 0.4156 0.9161 -0.0751 -0.2116 0.0476  138 VAL A CG2 
448  N N   . LYS A 65  ? 0.7059 0.4090 0.8106 0.0354  -0.1371 0.0016  139 LYS A N   
449  C CA  . LYS A 65  ? 0.7512 0.4747 0.8550 0.0694  -0.1188 -0.0160 139 LYS A CA  
450  C C   . LYS A 65  ? 0.7860 0.5081 0.8773 0.0677  -0.1138 -0.0323 139 LYS A C   
451  O O   . LYS A 65  ? 0.7665 0.5194 0.8770 0.0431  -0.1131 -0.0281 139 LYS A O   
452  C CB  . LYS A 65  ? 0.5952 0.3904 0.7345 0.0731  -0.0990 -0.0087 139 LYS A CB  
453  C CG  . LYS A 65  ? 0.6773 0.5018 0.8238 0.1040  -0.0802 -0.0226 139 LYS A CG  
454  C CD  . LYS A 65  ? 0.6799 0.5647 0.8602 0.1070  -0.0690 -0.0119 139 LYS A CD  
455  C CE  . LYS A 65  ? 0.6402 0.5741 0.8375 0.0832  -0.0587 -0.0080 139 LYS A CE  
456  N NZ  . LYS A 65  ? 0.7201 0.7007 0.9408 0.0829  -0.0532 0.0033  139 LYS A NZ  
457  N N   . ARG A 66  ? 0.7800 0.4643 0.8372 0.0948  -0.1105 -0.0512 140 ARG A N   
458  C CA  . ARG A 66  ? 0.8191 0.4939 0.8520 0.0939  -0.1060 -0.0668 140 ARG A CA  
459  C C   . ARG A 66  ? 0.8187 0.5280 0.8505 0.1223  -0.0770 -0.0800 140 ARG A C   
460  O O   . ARG A 66  ? 0.8914 0.6024 0.9261 0.1519  -0.0655 -0.0841 140 ARG A O   
461  C CB  . ARG A 66  ? 0.8990 0.4842 0.8764 0.0937  -0.1299 -0.0779 140 ARG A CB  
462  C CG  . ARG A 66  ? 0.9776 0.5119 0.9056 0.1318  -0.1205 -0.0995 140 ARG A CG  
463  C CD  . ARG A 66  ? 1.1201 0.5534 0.9838 0.1286  -0.1495 -0.1103 140 ARG A CD  
464  N NE  . ARG A 66  ? 1.2976 0.6919 1.1217 0.1643  -0.1389 -0.1251 140 ARG A NE  
465  C CZ  . ARG A 66  ? 1.3029 0.6320 1.0775 0.1629  -0.1575 -0.1293 140 ARG A CZ  
466  N NH1 . ARG A 66  ? 1.3201 0.6147 1.0771 0.1274  -0.1895 -0.1187 140 ARG A NH1 
467  N NH2 . ARG A 66  ? 1.3224 0.6246 1.0686 0.1983  -0.1443 -0.1441 140 ARG A NH2 
468  N N   . SER A 67  ? 0.8262 0.5659 0.8581 0.1121  -0.0662 -0.0847 141 SER A N   
469  C CA  . SER A 67  ? 0.8658 0.6394 0.8943 0.1321  -0.0382 -0.0947 141 SER A CA  
470  C C   . SER A 67  ? 0.8750 0.5902 0.8470 0.1583  -0.0303 -0.1151 141 SER A C   
471  O O   . SER A 67  ? 0.9470 0.5882 0.8722 0.1552  -0.0510 -0.1235 141 SER A O   
472  C CB  . SER A 67  ? 0.8405 0.6495 0.8744 0.1108  -0.0336 -0.0932 141 SER A CB  
473  O OG  . SER A 67  ? 0.8329 0.5907 0.8280 0.0940  -0.0533 -0.1000 141 SER A OG  
474  N N   . MET A 68  ? 0.9123 0.6614 0.8883 0.1841  0.0004  -0.1232 142 MET A N   
475  C CA  . MET A 68  ? 1.0262 0.7251 0.9514 0.2163  0.0152  -0.1444 142 MET A CA  
476  C C   . MET A 68  ? 1.0777 0.7286 0.9335 0.2059  0.0171  -0.1590 142 MET A C   
477  O O   . MET A 68  ? 1.0949 0.6610 0.8870 0.2124  0.0024  -0.1736 142 MET A O   
478  C CB  . MET A 68  ? 1.0951 0.8551 1.0560 0.2487  0.0511  -0.1475 142 MET A CB  
479  C CG  . MET A 68  ? 1.1507 0.8641 1.0705 0.2911  0.0696  -0.1706 142 MET A CG  
480  S SD  . MET A 68  ? 1.4475 1.2485 1.4198 0.3283  0.1178  -0.1743 142 MET A SD  
481  C CE  . MET A 68  ? 1.1498 0.8902 1.0700 0.3568  0.1329  -0.1992 142 MET A CE  
482  N N   . SER A 69  ? 1.0874 0.7836 0.9485 0.1880  0.0313  -0.1545 143 SER A N   
483  C CA  . SER A 69  ? 1.0898 0.7441 0.8815 0.1778  0.0355  -0.1665 143 SER A CA  
484  C C   . SER A 69  ? 1.0960 0.7503 0.8913 0.1384  0.0066  -0.1547 143 SER A C   
485  O O   . SER A 69  ? 1.0330 0.7413 0.8917 0.1219  -0.0037 -0.1379 143 SER A O   
486  C CB  . SER A 69  ? 1.1004 0.8047 0.8883 0.1916  0.0793  -0.1713 143 SER A CB  
487  O OG  . SER A 69  ? 1.1579 0.9547 1.0232 0.1839  0.0906  -0.1529 143 SER A OG  
488  N N   . PRO A 70  ? 1.1372 0.7282 0.8635 0.1239  -0.0082 -0.1637 144 PRO A N   
489  C CA  . PRO A 70  ? 1.0657 0.6578 0.8000 0.0893  -0.0381 -0.1529 144 PRO A CA  
490  C C   . PRO A 70  ? 1.0279 0.6954 0.8022 0.0782  -0.0206 -0.1413 144 PRO A C   
491  O O   . PRO A 70  ? 1.0559 0.7646 0.8332 0.0920  0.0149  -0.1425 144 PRO A O   
492  C CB  . PRO A 70  ? 1.1364 0.6407 0.7768 0.0807  -0.0538 -0.1664 144 PRO A CB  
493  C CG  . PRO A 70  ? 1.1289 0.5709 0.7137 0.1090  -0.0427 -0.1846 144 PRO A CG  
494  C CD  . PRO A 70  ? 1.1343 0.6429 0.7684 0.1395  -0.0018 -0.1850 144 PRO A CD  
495  N N   . PHE A 71  ? 1.0187 0.7042 0.8266 0.0529  -0.0472 -0.1295 145 PHE A N   
496  C CA  . PHE A 71  ? 0.9434 0.6904 0.7867 0.0409  -0.0383 -0.1184 145 PHE A CA  
497  C C   . PHE A 71  ? 0.9502 0.6852 0.7352 0.0368  -0.0196 -0.1228 145 PHE A C   
498  O O   . PHE A 71  ? 0.9963 0.6665 0.7127 0.0264  -0.0348 -0.1304 145 PHE A O   
499  C CB  . PHE A 71  ? 0.8715 0.6230 0.7477 0.0179  -0.0731 -0.1096 145 PHE A CB  
500  C CG  . PHE A 71  ? 0.8260 0.6084 0.7679 0.0186  -0.0832 -0.1018 145 PHE A CG  
501  C CD1 . PHE A 71  ? 0.7911 0.6252 0.7769 0.0321  -0.0604 -0.0958 145 PHE A CD1 
502  C CD2 . PHE A 71  ? 0.7969 0.5573 0.7568 0.0040  -0.1158 -0.0991 145 PHE A CD2 
503  C CE1 . PHE A 71  ? 0.7017 0.5591 0.7379 0.0300  -0.0684 -0.0876 145 PHE A CE1 
504  C CE2 . PHE A 71  ? 0.8011 0.5933 0.8197 0.0019  -0.1203 -0.0905 145 PHE A CE2 
505  C CZ  . PHE A 71  ? 0.7427 0.5803 0.7941 0.0145  -0.0958 -0.0849 145 PHE A CZ  
506  N N   . ARG A 72  ? 0.9338 0.7301 0.7444 0.0426  0.0123  -0.1165 146 ARG A N   
507  C CA  . ARG A 72  ? 0.9884 0.7832 0.7481 0.0358  0.0357  -0.1175 146 ARG A CA  
508  C C   . ARG A 72  ? 0.9627 0.7488 0.7066 0.0052  0.0111  -0.1076 146 ARG A C   
509  O O   . ARG A 72  ? 0.9850 0.7339 0.6600 -0.0083 0.0148  -0.1096 146 ARG A O   
510  C CB  . ARG A 72  ? 0.9988 0.8689 0.8007 0.0496  0.0766  -0.1111 146 ARG A CB  
511  C CG  . ARG A 72  ? 1.1411 1.0140 0.9455 0.0845  0.1063  -0.1236 146 ARG A CG  
512  C CD  . ARG A 72  ? 1.3068 1.2619 1.1614 0.0978  0.1458  -0.1158 146 ARG A CD  
513  N NE  . ARG A 72  ? 1.2994 1.3159 1.2395 0.0999  0.1357  -0.1014 146 ARG A NE  
514  C CZ  . ARG A 72  ? 1.3182 1.3674 1.3084 0.1275  0.1473  -0.1021 146 ARG A CZ  
515  N NH1 . ARG A 72  ? 1.3006 1.3323 1.2717 0.1594  0.1715  -0.1176 146 ARG A NH1 
516  N NH2 . ARG A 72  ? 1.3017 1.3973 1.3586 0.1241  0.1328  -0.0874 146 ARG A NH2 
517  N N   . GLY A 73  ? 0.8643 0.6796 0.6661 -0.0051 -0.0142 -0.0976 147 GLY A N   
518  C CA  . GLY A 73  ? 0.8448 0.6513 0.6387 -0.0295 -0.0407 -0.0892 147 GLY A CA  
519  C C   . GLY A 73  ? 0.8534 0.6911 0.7165 -0.0318 -0.0653 -0.0829 147 GLY A C   
520  O O   . GLY A 73  ? 0.8094 0.6714 0.7212 -0.0180 -0.0625 -0.0841 147 GLY A O   
521  N N   . PRO A 74  ? 0.7833 0.6171 0.6481 -0.0491 -0.0897 -0.0764 148 PRO A N   
522  C CA  . PRO A 74  ? 0.7657 0.6299 0.6944 -0.0479 -0.1092 -0.0728 148 PRO A CA  
523  C C   . PRO A 74  ? 0.7327 0.6600 0.7140 -0.0379 -0.0856 -0.0666 148 PRO A C   
524  O O   . PRO A 74  ? 0.6776 0.6275 0.7062 -0.0276 -0.0868 -0.0676 148 PRO A O   
525  C CB  . PRO A 74  ? 0.7323 0.5736 0.6401 -0.0657 -0.1371 -0.0680 148 PRO A CB  
526  C CG  . PRO A 74  ? 0.7555 0.5365 0.5872 -0.0782 -0.1455 -0.0705 148 PRO A CG  
527  C CD  . PRO A 74  ? 0.7772 0.5672 0.5794 -0.0696 -0.1050 -0.0734 148 PRO A CD  
528  N N   . LYS A 75  ? 0.7380 0.6937 0.7112 -0.0431 -0.0655 -0.0584 149 LYS A N   
529  C CA  . LYS A 75  ? 0.7036 0.7159 0.7253 -0.0359 -0.0489 -0.0507 149 LYS A CA  
530  C C   . LYS A 75  ? 0.6915 0.7222 0.7387 -0.0154 -0.0290 -0.0545 149 LYS A C   
531  O O   . LYS A 75  ? 0.6790 0.7381 0.7693 -0.0076 -0.0290 -0.0513 149 LYS A O   
532  C CB  . LYS A 75  ? 0.7359 0.7763 0.7465 -0.0483 -0.0329 -0.0390 149 LYS A CB  
533  C CG  . LYS A 75  ? 0.8595 0.8729 0.8340 -0.0723 -0.0542 -0.0330 149 LYS A CG  
534  C CD  . LYS A 75  ? 0.9024 0.9211 0.9045 -0.0774 -0.0802 -0.0294 149 LYS A CD  
535  C CE  . LYS A 75  ? 0.9018 0.8867 0.8641 -0.1008 -0.1048 -0.0227 149 LYS A CE  
536  N NZ  . LYS A 75  ? 0.9488 0.9297 0.9319 -0.1019 -0.1317 -0.0223 149 LYS A NZ  
537  N N   . ASP A 76  ? 0.7317 0.7405 0.7468 -0.0062 -0.0130 -0.0617 150 ASP A N   
538  C CA  . ASP A 76  ? 0.6734 0.6887 0.7077 0.0154  0.0015  -0.0665 150 ASP A CA  
539  C C   . ASP A 76  ? 0.6706 0.6647 0.7247 0.0177  -0.0200 -0.0701 150 ASP A C   
540  O O   . ASP A 76  ? 0.6900 0.7047 0.7794 0.0285  -0.0156 -0.0670 150 ASP A O   
541  C CB  . ASP A 76  ? 0.7412 0.7247 0.7277 0.0272  0.0207  -0.0770 150 ASP A CB  
542  C CG  . ASP A 76  ? 0.8563 0.8363 0.8582 0.0523  0.0317  -0.0836 150 ASP A CG  
543  O OD1 . ASP A 76  ? 0.9177 0.9446 0.9691 0.0634  0.0417  -0.0759 150 ASP A OD1 
544  O OD2 . ASP A 76  ? 0.8917 0.8163 0.8526 0.0603  0.0267  -0.0958 150 ASP A OD2 
545  N N   . ARG A 77  ? 0.6658 0.6198 0.6991 0.0060  -0.0447 -0.0750 151 ARG A N   
546  C CA  . ARG A 77  ? 0.6565 0.6007 0.7190 0.0044  -0.0649 -0.0759 151 ARG A CA  
547  C C   . ARG A 77  ? 0.5847 0.5753 0.6993 0.0023  -0.0659 -0.0681 151 ARG A C   
548  O O   . ARG A 77  ? 0.5439 0.5504 0.6901 0.0074  -0.0627 -0.0648 151 ARG A O   
549  C CB  . ARG A 77  ? 0.6500 0.5483 0.6882 -0.0087 -0.0944 -0.0810 151 ARG A CB  
550  C CG  . ARG A 77  ? 0.6071 0.5025 0.6844 -0.0129 -0.1158 -0.0801 151 ARG A CG  
551  C CD  . ARG A 77  ? 0.6881 0.5378 0.7454 -0.0256 -0.1493 -0.0839 151 ARG A CD  
552  N NE  . ARG A 77  ? 0.7191 0.5789 0.8282 -0.0315 -0.1697 -0.0807 151 ARG A NE  
553  C CZ  . ARG A 77  ? 0.7606 0.6534 0.9200 -0.0350 -0.1817 -0.0779 151 ARG A CZ  
554  N NH1 . ARG A 77  ? 0.7681 0.6777 0.9274 -0.0331 -0.1801 -0.0786 151 ARG A NH1 
555  N NH2 . ARG A 77  ? 0.7769 0.6872 0.9860 -0.0389 -0.1926 -0.0728 151 ARG A NH2 
556  N N   . ALA A 78  ? 0.5908 0.5978 0.7080 -0.0060 -0.0709 -0.0649 152 ALA A N   
557  C CA  . ALA A 78  ? 0.5361 0.5781 0.6919 -0.0065 -0.0724 -0.0602 152 ALA A CA  
558  C C   . ALA A 78  ? 0.5393 0.6157 0.7143 0.0018  -0.0525 -0.0529 152 ALA A C   
559  O O   . ALA A 78  ? 0.4994 0.5945 0.7020 0.0040  -0.0512 -0.0499 152 ALA A O   
560  C CB  . ALA A 78  ? 0.4781 0.5205 0.6227 -0.0160 -0.0840 -0.0588 152 ALA A CB  
561  N N   . ARG A 79  ? 0.5682 0.6539 0.7295 0.0063  -0.0369 -0.0495 153 ARG A N   
562  C CA  . ARG A 79  ? 0.4888 0.6073 0.6736 0.0154  -0.0227 -0.0413 153 ARG A CA  
563  C C   . ARG A 79  ? 0.5510 0.6595 0.7484 0.0261  -0.0206 -0.0424 153 ARG A C   
564  O O   . ARG A 79  ? 0.5353 0.6621 0.7545 0.0284  -0.0195 -0.0351 153 ARG A O   
565  C CB  . ARG A 79  ? 0.5863 0.7225 0.7631 0.0203  -0.0054 -0.0378 153 ARG A CB  
566  C CG  . ARG A 79  ? 0.6749 0.8538 0.8842 0.0262  0.0032  -0.0262 153 ARG A CG  
567  C CD  . ARG A 79  ? 0.8153 1.0204 1.0275 0.0328  0.0234  -0.0229 153 ARG A CD  
568  N NE  . ARG A 79  ? 0.9183 1.1096 1.0953 0.0204  0.0283  -0.0265 153 ARG A NE  
569  C CZ  . ARG A 79  ? 0.9052 1.1145 1.0781 0.0008  0.0249  -0.0171 153 ARG A CZ  
570  N NH1 . ARG A 79  ? 0.8399 1.0810 1.0419 -0.0085 0.0152  -0.0043 153 ARG A NH1 
571  N NH2 . ARG A 79  ? 0.8172 1.0059 0.9499 -0.0119 0.0287  -0.0197 153 ARG A NH2 
572  N N   . LYS A 80  ? 0.5671 0.6397 0.7447 0.0304  -0.0230 -0.0505 154 LYS A N   
573  C CA  . LYS A 80  ? 0.5077 0.5624 0.6921 0.0379  -0.0249 -0.0503 154 LYS A CA  
574  C C   . LYS A 80  ? 0.4958 0.5515 0.7018 0.0259  -0.0371 -0.0467 154 LYS A C   
575  O O   . LYS A 80  ? 0.5559 0.6177 0.7775 0.0267  -0.0354 -0.0394 154 LYS A O   
576  C CB  . LYS A 80  ? 0.4778 0.4856 0.6277 0.0452  -0.0269 -0.0605 154 LYS A CB  
577  C CG  . LYS A 80  ? 0.5743 0.5843 0.7055 0.0631  -0.0071 -0.0651 154 LYS A CG  
578  C CD  . LYS A 80  ? 0.6644 0.6186 0.7490 0.0725  -0.0074 -0.0785 154 LYS A CD  
579  C CE  . LYS A 80  ? 0.7269 0.6898 0.7962 0.0946  0.0191  -0.0849 154 LYS A CE  
580  N NZ  . LYS A 80  ? 0.8995 0.8013 0.9090 0.1049  0.0221  -0.1011 154 LYS A NZ  
581  N N   . LEU A 81  ? 0.4870 0.5381 0.6955 0.0146  -0.0492 -0.0511 155 LEU A N   
582  C CA  . LEU A 81  ? 0.4874 0.5487 0.7254 0.0051  -0.0566 -0.0482 155 LEU A CA  
583  C C   . LEU A 81  ? 0.5203 0.6183 0.7784 0.0046  -0.0464 -0.0423 155 LEU A C   
584  O O   . LEU A 81  ? 0.5093 0.6205 0.7897 -0.0013 -0.0441 -0.0385 155 LEU A O   
585  C CB  . LEU A 81  ? 0.5017 0.5521 0.7455 -0.0033 -0.0744 -0.0549 155 LEU A CB  
586  C CG  . LEU A 81  ? 0.5542 0.5593 0.7701 -0.0068 -0.0916 -0.0612 155 LEU A CG  
587  C CD1 . LEU A 81  ? 0.6282 0.6284 0.8601 -0.0160 -0.1142 -0.0649 155 LEU A CD1 
588  C CD2 . LEU A 81  ? 0.5328 0.5100 0.7441 -0.0086 -0.0964 -0.0588 155 LEU A CD2 
589  N N   . ALA A 82  ? 0.4980 0.6114 0.7461 0.0090  -0.0402 -0.0407 156 ALA A N   
590  C CA  . ALA A 82  ? 0.4226 0.5607 0.6793 0.0076  -0.0346 -0.0358 156 ALA A CA  
591  C C   . ALA A 82  ? 0.4577 0.6009 0.7193 0.0081  -0.0266 -0.0262 156 ALA A C   
592  O O   . ALA A 82  ? 0.4813 0.6369 0.7459 0.0039  -0.0217 -0.0229 156 ALA A O   
593  C CB  . ALA A 82  ? 0.4510 0.6000 0.6947 0.0086  -0.0348 -0.0333 156 ALA A CB  
594  N N   . GLU A 83  ? 0.4518 0.5805 0.7087 0.0138  -0.0259 -0.0220 157 GLU A N   
595  C CA  . GLU A 83  ? 0.4148 0.5393 0.6723 0.0130  -0.0235 -0.0113 157 GLU A CA  
596  C C   . GLU A 83  ? 0.4941 0.6166 0.7613 0.0000  -0.0218 -0.0089 157 GLU A C   
597  O O   . GLU A 83  ? 0.4933 0.6211 0.7572 -0.0070 -0.0160 0.0004  157 GLU A O   
598  C CB  . GLU A 83  ? 0.4188 0.5199 0.6692 0.0243  -0.0265 -0.0095 157 GLU A CB  
599  C CG  . GLU A 83  ? 0.4951 0.5846 0.7425 0.0241  -0.0294 0.0032  157 GLU A CG  
600  C CD  . GLU A 83  ? 0.5930 0.6556 0.8340 0.0409  -0.0349 0.0033  157 GLU A CD  
601  O OE1 . GLU A 83  ? 0.6158 0.6692 0.8519 0.0528  -0.0325 -0.0081 157 GLU A OE1 
602  O OE2 . GLU A 83  ? 0.5509 0.5976 0.7877 0.0431  -0.0420 0.0143  157 GLU A OE2 
603  N N   . VAL A 84  ? 0.4292 0.5449 0.7085 -0.0051 -0.0272 -0.0161 158 VAL A N   
604  C CA  . VAL A 84  ? 0.4660 0.5906 0.7670 -0.0190 -0.0249 -0.0125 158 VAL A CA  
605  C C   . VAL A 84  ? 0.5413 0.6984 0.8544 -0.0207 -0.0124 -0.0153 158 VAL A C   
606  O O   . VAL A 84  ? 0.5581 0.7297 0.8776 -0.0299 0.0004  -0.0081 158 VAL A O   
607  C CB  . VAL A 84  ? 0.4690 0.5794 0.7852 -0.0243 -0.0391 -0.0186 158 VAL A CB  
608  C CG1 . VAL A 84  ? 0.4903 0.6224 0.8429 -0.0399 -0.0366 -0.0134 158 VAL A CG1 
609  C CG2 . VAL A 84  ? 0.4629 0.5305 0.7561 -0.0219 -0.0512 -0.0173 158 VAL A CG2 
610  N N   . GLY A 85  ? 0.5226 0.6876 0.8340 -0.0121 -0.0155 -0.0258 159 GLY A N   
611  C CA  . GLY A 85  ? 0.4818 0.6680 0.7958 -0.0095 -0.0056 -0.0310 159 GLY A CA  
612  C C   . GLY A 85  ? 0.4527 0.6395 0.7396 -0.0108 0.0053  -0.0227 159 GLY A C   
613  O O   . GLY A 85  ? 0.5001 0.6996 0.7843 -0.0137 0.0200  -0.0231 159 GLY A O   
614  N N   . SER A 86  ? 0.4532 0.6257 0.7191 -0.0084 -0.0018 -0.0151 160 SER A N   
615  C CA  . SER A 86  ? 0.4755 0.6435 0.7151 -0.0109 0.0016  -0.0050 160 SER A CA  
616  C C   . SER A 86  ? 0.5074 0.6705 0.7416 -0.0220 0.0117  0.0060  160 SER A C   
617  O O   . SER A 86  ? 0.5537 0.7159 0.7634 -0.0280 0.0212  0.0107  160 SER A O   
618  C CB  . SER A 86  ? 0.4913 0.6512 0.7232 -0.0045 -0.0107 0.0021  160 SER A CB  
619  O OG  . SER A 86  ? 0.4836 0.6514 0.7162 0.0007  -0.0177 -0.0046 160 SER A OG  
620  N N   . HIS A 87  ? 0.5095 0.6637 0.7596 -0.0270 0.0086  0.0111  161 HIS A N   
621  C CA  . HIS A 87  ? 0.5101 0.6573 0.7542 -0.0426 0.0163  0.0242  161 HIS A CA  
622  C C   . HIS A 87  ? 0.5818 0.7561 0.8380 -0.0525 0.0377  0.0212  161 HIS A C   
623  O O   . HIS A 87  ? 0.6017 0.7754 0.8384 -0.0662 0.0517  0.0321  161 HIS A O   
624  C CB  . HIS A 87  ? 0.5325 0.6605 0.7916 -0.0482 0.0053  0.0294  161 HIS A CB  
625  C CG  . HIS A 87  ? 0.5001 0.5938 0.7381 -0.0419 -0.0101 0.0383  161 HIS A CG  
626  N ND1 . HIS A 87  ? 0.6406 0.7266 0.8779 -0.0225 -0.0205 0.0309  161 HIS A ND1 
627  C CD2 . HIS A 87  ? 0.4398 0.5046 0.6582 -0.0513 -0.0172 0.0541  161 HIS A CD2 
628  C CE1 . HIS A 87  ? 0.6298 0.6872 0.8533 -0.0164 -0.0322 0.0398  161 HIS A CE1 
629  N NE2 . HIS A 87  ? 0.6224 0.6623 0.8322 -0.0337 -0.0332 0.0541  161 HIS A NE2 
630  N N   . GLU A 88  ? 0.5273 0.7254 0.8155 -0.0453 0.0407  0.0067  162 GLU A N   
631  C CA  . GLU A 88  ? 0.5293 0.7602 0.8405 -0.0498 0.0627  0.0019  162 GLU A CA  
632  C C   . GLU A 88  ? 0.5403 0.7743 0.8169 -0.0427 0.0789  -0.0046 162 GLU A C   
633  O O   . GLU A 88  ? 0.6339 0.8830 0.9022 -0.0507 0.1039  -0.0017 162 GLU A O   
634  C CB  . GLU A 88  ? 0.5945 0.8470 0.9544 -0.0418 0.0555  -0.0115 162 GLU A CB  
635  C CG  . GLU A 88  ? 0.6461 0.8892 1.0340 -0.0517 0.0373  -0.0050 162 GLU A CG  
636  C CD  . GLU A 88  ? 0.7359 0.9987 1.1722 -0.0471 0.0268  -0.0159 162 GLU A CD  
637  O OE1 . GLU A 88  ? 0.7594 1.0344 1.2020 -0.0314 0.0279  -0.0302 162 GLU A OE1 
638  O OE2 . GLU A 88  ? 0.6867 0.9480 1.1528 -0.0598 0.0137  -0.0094 162 GLU A OE2 
639  N N   . LYS A 89  ? 0.5723 0.7896 0.8241 -0.0293 0.0653  -0.0130 163 LYS A N   
640  C CA  . LYS A 89  ? 0.5324 0.7411 0.7420 -0.0237 0.0747  -0.0192 163 LYS A CA  
641  C C   . LYS A 89  ? 0.5274 0.7156 0.6889 -0.0373 0.0822  -0.0037 163 LYS A C   
642  O O   . LYS A 89  ? 0.6329 0.8148 0.7556 -0.0381 0.0993  -0.0073 163 LYS A O   
643  C CB  . LYS A 89  ? 0.5276 0.7181 0.7196 -0.0124 0.0524  -0.0266 163 LYS A CB  
644  C CG  . LYS A 89  ? 0.5494 0.7508 0.7758 -0.0006 0.0426  -0.0415 163 LYS A CG  
645  C CD  . LYS A 89  ? 0.6229 0.8048 0.8292 0.0041  0.0194  -0.0436 163 LYS A CD  
646  C CE  . LYS A 89  ? 0.7075 0.8926 0.9405 0.0123  0.0066  -0.0557 163 LYS A CE  
647  N NZ  . LYS A 89  ? 0.7889 0.9568 1.0027 0.0112  -0.0149 -0.0536 163 LYS A NZ  
648  N N   . VAL A 90  ? 0.6426 0.8145 0.8009 -0.0471 0.0682  0.0130  164 VAL A N   
649  C CA  . VAL A 90  ? 0.6654 0.8117 0.7771 -0.0615 0.0698  0.0302  164 VAL A CA  
650  C C   . VAL A 90  ? 0.6921 0.8516 0.8042 -0.0789 0.0969  0.0378  164 VAL A C   
651  O O   . VAL A 90  ? 0.7954 0.9415 0.8587 -0.0900 0.1131  0.0444  164 VAL A O   
652  C CB  . VAL A 90  ? 0.6043 0.7270 0.7166 -0.0627 0.0432  0.0448  164 VAL A CB  
653  C CG1 . VAL A 90  ? 0.6322 0.7235 0.6990 -0.0791 0.0403  0.0648  164 VAL A CG1 
654  C CG2 . VAL A 90  ? 0.5419 0.6594 0.6537 -0.0477 0.0214  0.0396  164 VAL A CG2 
655  N N   . GLY A 91  ? 0.5335 0.8379 1.0005 0.0694  0.1796  -0.1165 165 GLY A N   
656  C CA  . GLY A 91  ? 0.5495 0.9071 1.0597 0.0672  0.2005  -0.0989 165 GLY A CA  
657  C C   . GLY A 91  ? 0.6348 1.0068 1.1213 0.0465  0.2179  -0.0842 165 GLY A C   
658  O O   . GLY A 91  ? 0.6504 0.9944 1.1037 0.0299  0.2073  -0.0836 165 GLY A O   
659  N N   . GLN A 92  ? 0.7262 1.1442 1.2300 0.0486  0.2464  -0.0714 166 GLN A N   
660  C CA  . GLN A 92  ? 0.7208 1.1599 1.2135 0.0264  0.2637  -0.0510 166 GLN A CA  
661  C C   . GLN A 92  ? 0.7449 1.1631 1.1541 0.0347  0.2870  -0.0613 166 GLN A C   
662  O O   . GLN A 92  ? 0.7306 1.1573 1.1138 0.0589  0.3087  -0.0739 166 GLN A O   
663  C CB  . GLN A 92  ? 0.7263 1.2300 1.2809 0.0216  0.2821  -0.0300 166 GLN A CB  
664  C CG  . GLN A 92  ? 0.7563 1.2769 1.3389 -0.0143 0.2771  -0.0012 166 GLN A CG  
665  C CD  . GLN A 92  ? 0.7779 1.2593 1.3767 -0.0340 0.2363  0.0025  166 GLN A CD  
666  O OE1 . GLN A 92  ? 0.7948 1.2399 1.3523 -0.0503 0.2297  0.0058  166 GLN A OE1 
667  N NE2 . GLN A 92  ? 0.7457 1.2321 1.4019 -0.0312 0.2075  0.0016  166 GLN A NE2 
668  N N   . HIS A 93  ? 0.6321 1.0210 0.9979 0.0156  0.2810  -0.0561 167 HIS A N   
669  C CA  . HIS A 93  ? 0.5790 0.9481 0.8652 0.0188  0.2986  -0.0609 167 HIS A CA  
670  C C   . HIS A 93  ? 0.5510 0.9095 0.8187 -0.0097 0.2962  -0.0403 167 HIS A C   
671  O O   . HIS A 93  ? 0.5432 0.8839 0.8361 -0.0264 0.2728  -0.0361 167 HIS A O   
672  C CB  . HIS A 93  ? 0.6455 0.9653 0.8741 0.0351  0.2841  -0.0896 167 HIS A CB  
673  C CG  . HIS A 93  ? 0.6083 0.9089 0.7564 0.0428  0.2994  -0.0971 167 HIS A CG  
674  N ND1 . HIS A 93  ? 0.6278 0.8978 0.7203 0.0291  0.2894  -0.0962 167 HIS A ND1 
675  C CD2 . HIS A 93  ? 0.5790 0.8856 0.6901 0.0639  0.3223  -0.1063 167 HIS A CD2 
676  C CE1 . HIS A 93  ? 0.6501 0.9066 0.6751 0.0396  0.3026  -0.1035 167 HIS A CE1 
677  N NE2 . HIS A 93  ? 0.6199 0.8962 0.6522 0.0612  0.3233  -0.1106 167 HIS A NE2 
678  N N   . PRO A 94  ? 0.5285 0.8944 0.7499 -0.0153 0.3195  -0.0266 168 PRO A N   
679  C CA  . PRO A 94  ? 0.5227 0.8735 0.7252 -0.0435 0.3174  -0.0026 168 PRO A CA  
680  C C   . PRO A 94  ? 0.6066 0.9055 0.7637 -0.0483 0.2922  -0.0147 168 PRO A C   
681  O O   . PRO A 94  ? 0.6748 0.9490 0.8306 -0.0668 0.2680  0.0052  168 PRO A O   
682  C CB  . PRO A 94  ? 0.5581 0.9226 0.7053 -0.0421 0.3465  0.0107  168 PRO A CB  
683  C CG  . PRO A 94  ? 0.5457 0.9553 0.7173 -0.0202 0.3682  0.0012  168 PRO A CG  
684  C CD  . PRO A 94  ? 0.5756 0.9675 0.7658 0.0030  0.3498  -0.0288 168 PRO A CD  
685  N N   . CYS A 95  ? 0.5978 0.8733 0.7122 -0.0288 0.2843  -0.0435 169 CYS A N   
686  C CA  . CYS A 95  ? 0.5434 0.7731 0.6127 -0.0290 0.2504  -0.0499 169 CYS A CA  
687  C C   . CYS A 95  ? 0.5832 0.7976 0.6882 -0.0228 0.2212  -0.0637 169 CYS A C   
688  O O   . CYS A 95  ? 0.5844 0.7685 0.6581 -0.0175 0.1988  -0.0738 169 CYS A O   
689  C CB  . CYS A 95  ? 0.6015 0.8138 0.5994 -0.0166 0.2554  -0.0683 169 CYS A CB  
690  S SG  . CYS A 95  ? 0.7410 0.9636 0.6780 -0.0212 0.2882  -0.0518 169 CYS A SG  
691  N N   . CYS A 96  ? 0.5630 0.7993 0.7340 -0.0237 0.2206  -0.0618 170 CYS A N   
692  C CA  . CYS A 96  ? 0.5190 0.7379 0.7194 -0.0190 0.1917  -0.0710 170 CYS A CA  
693  C C   . CYS A 96  ? 0.5047 0.7231 0.7479 -0.0359 0.1733  -0.0507 170 CYS A C   
694  O O   . CYS A 96  ? 0.5550 0.8069 0.8432 -0.0472 0.1870  -0.0347 170 CYS A O   
695  C CB  . CYS A 96  ? 0.5794 0.8165 0.8158 -0.0008 0.1998  -0.0917 170 CYS A CB  
696  S SG  . CYS A 96  ? 0.6273 0.8453 0.8064 0.0189  0.2085  -0.1192 170 CYS A SG  
697  N N   . VAL A 97  ? 0.5014 0.6811 0.7295 -0.0377 0.1422  -0.0509 171 VAL A N   
698  C CA  . VAL A 97  ? 0.5221 0.6880 0.7796 -0.0523 0.1177  -0.0364 171 VAL A CA  
699  C C   . VAL A 97  ? 0.4816 0.6793 0.8084 -0.0512 0.1141  -0.0382 171 VAL A C   
700  O O   . VAL A 97  ? 0.4986 0.6928 0.8347 -0.0358 0.1058  -0.0541 171 VAL A O   
701  C CB  . VAL A 97  ? 0.5183 0.6330 0.7360 -0.0477 0.0885  -0.0412 171 VAL A CB  
702  C CG1 . VAL A 97  ? 0.5712 0.6617 0.8085 -0.0614 0.0597  -0.0301 171 VAL A CG1 
703  C CG2 . VAL A 97  ? 0.5005 0.5898 0.6601 -0.0458 0.0918  -0.0374 171 VAL A CG2 
704  N N   . ARG A 98  ? 0.4924 0.7217 0.8721 -0.0683 0.1187  -0.0193 172 ARG A N   
705  C CA  . ARG A 98  ? 0.4903 0.7603 0.9492 -0.0674 0.1153  -0.0171 172 ARG A CA  
706  C C   . ARG A 98  ? 0.4666 0.7040 0.9400 -0.0736 0.0701  -0.0161 172 ARG A C   
707  O O   . ARG A 98  ? 0.5299 0.7261 0.9765 -0.0904 0.0439  -0.0063 172 ARG A O   
708  C CB  . ARG A 98  ? 0.4764 0.7990 0.9964 -0.0862 0.1358  0.0072  172 ARG A CB  
709  C CG  . ARG A 98  ? 0.5374 0.9102 1.1542 -0.0863 0.1290  0.0137  172 ARG A CG  
710  C CD  . ARG A 98  ? 0.5747 0.9954 1.2363 -0.1045 0.1441  0.0408  172 ARG A CD  
711  N NE  . ARG A 98  ? 0.5626 0.9596 1.2287 -0.1395 0.1201  0.0647  172 ARG A NE  
712  C CZ  . ARG A 98  ? 0.6224 1.0065 1.2520 -0.1567 0.1377  0.0800  172 ARG A CZ  
713  N NH1 . ARG A 98  ? 0.6604 1.0565 1.2440 -0.1426 0.1798  0.0742  172 ARG A NH1 
714  N NH2 . ARG A 98  ? 0.5439 0.8948 1.1746 -0.1881 0.1088  0.1013  172 ARG A NH2 
715  N N   . LEU A 99  ? 0.4509 0.7018 0.9622 -0.0587 0.0597  -0.0267 173 LEU A N   
716  C CA  . LEU A 99  ? 0.4341 0.6605 0.9655 -0.0645 0.0158  -0.0235 173 LEU A CA  
717  C C   . LEU A 99  ? 0.4582 0.7321 1.0801 -0.0827 0.0052  -0.0033 173 LEU A C   
718  O O   . LEU A 99  ? 0.4476 0.7849 1.1374 -0.0748 0.0324  0.0003  173 LEU A O   
719  C CB  . LEU A 99  ? 0.4116 0.6279 0.9413 -0.0407 0.0062  -0.0406 173 LEU A CB  
720  C CG  . LEU A 99  ? 0.3999 0.5834 0.9356 -0.0442 -0.0412 -0.0375 173 LEU A CG  
721  C CD1 . LEU A 99  ? 0.4329 0.5483 0.8875 -0.0528 -0.0653 -0.0384 173 LEU A CD1 
722  C CD2 . LEU A 99  ? 0.3401 0.5208 0.8843 -0.0208 -0.0472 -0.0498 173 LEU A CD2 
723  N N   . GLU A 100 ? 0.4346 0.6774 1.0583 -0.1066 -0.0344 0.0100  174 GLU A N   
724  C CA  . GLU A 100 ? 0.4318 0.7143 1.1396 -0.1276 -0.0533 0.0316  174 GLU A CA  
725  C C   . GLU A 100 ? 0.4001 0.6761 1.1335 -0.1174 -0.0912 0.0280  174 GLU A C   
726  O O   . GLU A 100 ? 0.3600 0.6856 1.1536 -0.1092 -0.0836 0.0357  174 GLU A O   
727  C CB  . GLU A 100 ? 0.5001 0.7428 1.1854 -0.1601 -0.0798 0.0484  174 GLU A CB  
728  C CG  . GLU A 100 ? 0.5874 0.8469 1.2641 -0.1748 -0.0429 0.0623  174 GLU A CG  
729  C CD  . GLU A 100 ? 0.6288 0.9630 1.3666 -0.1780 -0.0086 0.0800  174 GLU A CD  
730  O OE1 . GLU A 100 ? 0.5758 0.9351 1.3677 -0.1860 -0.0289 0.0915  174 GLU A OE1 
731  O OE2 . GLU A 100 ? 0.6149 0.9811 1.3423 -0.1716 0.0388  0.0819  174 GLU A OE2 
732  N N   . GLN A 101 ? 0.4439 0.6565 1.1274 -0.1169 -0.1320 0.0172  175 GLN A N   
733  C CA  . GLN A 101 ? 0.4465 0.6452 1.1411 -0.1054 -0.1685 0.0143  175 GLN A CA  
734  C C   . GLN A 101 ? 0.5306 0.6529 1.1376 -0.0974 -0.1967 -0.0019 175 GLN A C   
735  O O   . GLN A 101 ? 0.5369 0.6065 1.0636 -0.1022 -0.1935 -0.0077 175 GLN A O   
736  C CB  . GLN A 101 ? 0.4245 0.6244 1.1537 -0.1242 -0.2043 0.0336  175 GLN A CB  
737  C CG  . GLN A 101 ? 0.5338 0.6672 1.2037 -0.1480 -0.2402 0.0379  175 GLN A CG  
738  C CD  . GLN A 101 ? 0.5535 0.6947 1.2664 -0.1679 -0.2722 0.0577  175 GLN A CD  
739  O OE1 . GLN A 101 ? 0.5532 0.7506 1.3422 -0.1636 -0.2696 0.0685  175 GLN A OE1 
740  N NE2 . GLN A 101 ? 0.6565 0.7398 1.3212 -0.1887 -0.3028 0.0624  175 GLN A NE2 
741  N N   . ALA A 102 ? 0.5049 0.6167 1.1138 -0.0805 -0.2191 -0.0075 176 ALA A N   
742  C CA  . ALA A 102 ? 0.5023 0.5392 1.0151 -0.0692 -0.2415 -0.0190 176 ALA A CA  
743  C C   . ALA A 102 ? 0.5626 0.5789 1.0919 -0.0719 -0.2970 -0.0123 176 ALA A C   
744  O O   . ALA A 102 ? 0.5706 0.6328 1.1744 -0.0668 -0.3005 -0.0017 176 ALA A O   
745  C CB  . ALA A 102 ? 0.5016 0.5368 0.9779 -0.0422 -0.2058 -0.0327 176 ALA A CB  
746  N N   . TRP A 103 ? 0.5943 0.5327 1.0322 -0.0745 -0.3311 -0.0172 177 TRP A N   
747  C CA  . TRP A 103 ? 0.6330 0.5353 1.0520 -0.0715 -0.3777 -0.0102 177 TRP A CA  
748  C C   . TRP A 103 ? 0.6961 0.5183 0.9997 -0.0602 -0.3944 -0.0225 177 TRP A C   
749  O O   . TRP A 103 ? 0.7693 0.5635 1.0028 -0.0524 -0.3613 -0.0332 177 TRP A O   
750  C CB  . TRP A 103 ? 0.6725 0.5618 1.1036 -0.0922 -0.4085 0.0042  177 TRP A CB  
751  C CG  . TRP A 103 ? 0.7456 0.5704 1.0917 -0.1044 -0.4184 -0.0009 177 TRP A CG  
752  C CD1 . TRP A 103 ? 0.8212 0.5627 1.0685 -0.1016 -0.4525 -0.0056 177 TRP A CD1 
753  C CD2 . TRP A 103 ? 0.7177 0.5527 1.0671 -0.1187 -0.3928 -0.0012 177 TRP A CD2 
754  N NE1 . TRP A 103 ? 0.8794 0.5796 1.0701 -0.1104 -0.4483 -0.0103 177 TRP A NE1 
755  C CE2 . TRP A 103 ? 0.8326 0.5875 1.0852 -0.1221 -0.4139 -0.0070 177 TRP A CE2 
756  C CE3 . TRP A 103 ? 0.6572 0.5588 1.0776 -0.1273 -0.3527 0.0038  177 TRP A CE3 
757  C CZ2 . TRP A 103 ? 0.8257 0.5637 1.0550 -0.1339 -0.3989 -0.0079 177 TRP A CZ2 
758  C CZ3 . TRP A 103 ? 0.6758 0.5599 1.0703 -0.1421 -0.3387 0.0047  177 TRP A CZ3 
759  C CH2 . TRP A 103 ? 0.7472 0.5490 1.0486 -0.1452 -0.3631 -0.0011 177 TRP A CH2 
760  N N   . GLU A 104 ? 0.7537 0.5391 1.0274 -0.0534 -0.4320 -0.0163 178 GLU A N   
761  C CA  . GLU A 104 ? 0.8631 0.5686 1.0180 -0.0418 -0.4483 -0.0239 178 GLU A CA  
762  C C   . GLU A 104 ? 0.8594 0.5072 0.9658 -0.0485 -0.4933 -0.0152 178 GLU A C   
763  O O   . GLU A 104 ? 0.9191 0.5916 1.0934 -0.0569 -0.5197 -0.0018 178 GLU A O   
764  C CB  . GLU A 104 ? 0.8720 0.5833 1.0210 -0.0202 -0.4372 -0.0220 178 GLU A CB  
765  C CG  . GLU A 104 ? 0.9050 0.6450 1.1291 -0.0170 -0.4712 -0.0084 178 GLU A CG  
766  C CD  . GLU A 104 ? 0.8880 0.6321 1.1091 0.0056  -0.4540 -0.0053 178 GLU A CD  
767  O OE1 . GLU A 104 ? 0.8955 0.6082 1.0392 0.0159  -0.4191 -0.0110 178 GLU A OE1 
768  O OE2 . GLU A 104 ? 0.8564 0.6334 1.1523 0.0132  -0.4695 0.0042  178 GLU A OE2 
769  N N   . GLU A 105 ? 0.9484 0.5187 0.9374 -0.0436 -0.4993 -0.0235 179 GLU A N   
770  C CA  . GLU A 105 ? 1.0569 0.5604 0.9844 -0.0477 -0.5411 -0.0182 179 GLU A CA  
771  C C   . GLU A 105 ? 1.0902 0.5119 0.8791 -0.0292 -0.5359 -0.0283 179 GLU A C   
772  O O   . GLU A 105 ? 1.1715 0.5762 0.9034 -0.0199 -0.5023 -0.0401 179 GLU A O   
773  C CB  . GLU A 105 ? 1.1524 0.6508 1.0981 -0.0666 -0.5536 -0.0154 179 GLU A CB  
774  C CG  . GLU A 105 ? 1.2854 0.7234 1.1920 -0.0753 -0.6040 -0.0083 179 GLU A CG  
775  C CD  . GLU A 105 ? 1.3651 0.8013 1.2986 -0.0962 -0.6187 -0.0035 179 GLU A CD  
776  O OE1 . GLU A 105 ? 1.3400 0.8254 1.3255 -0.1045 -0.5878 -0.0044 179 GLU A OE1 
777  O OE2 . GLU A 105 ? 1.4333 0.8162 1.3341 -0.1054 -0.6622 0.0015  179 GLU A OE2 
778  N N   . GLY A 106 ? 1.1776 0.5508 0.9143 -0.0230 -0.5651 -0.0230 180 GLY A N   
779  C CA  . GLY A 106 ? 1.2333 0.5292 0.8368 -0.0046 -0.5562 -0.0304 180 GLY A CA  
780  C C   . GLY A 106 ? 1.2773 0.5863 0.8438 0.0134  -0.5113 -0.0357 180 GLY A C   
781  O O   . GLY A 106 ? 1.3650 0.6248 0.8295 0.0299  -0.4849 -0.0436 180 GLY A O   
782  N N   . GLY A 107 ? 1.2328 0.6084 0.8821 0.0125  -0.5005 -0.0302 181 GLY A N   
783  C CA  . GLY A 107 ? 1.1510 0.5430 0.7730 0.0282  -0.4599 -0.0319 181 GLY A CA  
784  C C   . GLY A 107 ? 1.1273 0.5538 0.7719 0.0294  -0.4072 -0.0432 181 GLY A C   
785  O O   . GLY A 107 ? 1.0973 0.5478 0.7362 0.0424  -0.3563 -0.0409 181 GLY A O   
786  N N   . ILE A 108 ? 1.1125 0.5409 0.7836 0.0147  -0.4204 -0.0534 182 ILE A N   
787  C CA  . ILE A 108 ? 1.0662 0.5257 0.7623 0.0142  -0.3762 -0.0620 182 ILE A CA  
788  C C   . ILE A 108 ? 0.9231 0.4668 0.7507 -0.0010 -0.3667 -0.0565 182 ILE A C   
789  O O   . ILE A 108 ? 0.9757 0.5389 0.8696 -0.0182 -0.4060 -0.0507 182 ILE A O   
790  C CB  . ILE A 108 ? 1.1277 0.5392 0.7685 0.0115  -0.3859 -0.0690 182 ILE A CB  
791  C CG1 . ILE A 108 ? 1.1845 0.5180 0.7001 0.0318  -0.3882 -0.0709 182 ILE A CG1 
792  C CG2 . ILE A 108 ? 1.0193 0.4560 0.6778 0.0127  -0.3443 -0.0771 182 ILE A CG2 
793  C CD1 . ILE A 108 ? 1.2294 0.5538 0.6798 0.0557  -0.3409 -0.0760 182 ILE A CD1 
794  N N   . LEU A 109 ? 0.8773 0.4719 0.7426 0.0058  -0.3150 -0.0576 183 LEU A N   
795  C CA  . LEU A 109 ? 0.8212 0.4927 0.7971 -0.0044 -0.2972 -0.0544 183 LEU A CA  
796  C C   . LEU A 109 ? 0.8274 0.5094 0.8183 -0.0169 -0.2836 -0.0592 183 LEU A C   
797  O O   . LEU A 109 ? 0.8725 0.5272 0.8026 -0.0082 -0.2591 -0.0662 183 LEU A O   
798  C CB  . LEU A 109 ? 0.7584 0.4732 0.7612 0.0094  -0.2532 -0.0534 183 LEU A CB  
799  C CG  . LEU A 109 ? 0.6498 0.4371 0.7494 0.0032  -0.2283 -0.0540 183 LEU A CG  
800  C CD1 . LEU A 109 ? 0.6685 0.4905 0.8525 -0.0047 -0.2582 -0.0468 183 LEU A CD1 
801  C CD2 . LEU A 109 ? 0.6086 0.4222 0.7155 0.0165  -0.1891 -0.0565 183 LEU A CD2 
802  N N   . TYR A 110 ? 0.7883 0.5119 0.8635 -0.0366 -0.2987 -0.0531 184 TYR A N   
803  C CA  . TYR A 110 ? 0.7524 0.4870 0.8503 -0.0532 -0.2899 -0.0525 184 TYR A CA  
804  C C   . TYR A 110 ? 0.6631 0.4814 0.8560 -0.0579 -0.2542 -0.0464 184 TYR A C   
805  O O   . TYR A 110 ? 0.7063 0.5746 0.9801 -0.0619 -0.2624 -0.0390 184 TYR A O   
806  C CB  . TYR A 110 ? 0.8411 0.5462 0.9508 -0.0773 -0.3417 -0.0465 184 TYR A CB  
807  C CG  . TYR A 110 ? 0.9103 0.5329 0.9139 -0.0685 -0.3698 -0.0503 184 TYR A CG  
808  C CD1 . TYR A 110 ? 0.9470 0.5378 0.9122 -0.0582 -0.3990 -0.0491 184 TYR A CD1 
809  C CD2 . TYR A 110 ? 0.9388 0.5139 0.8808 -0.0695 -0.3676 -0.0540 184 TYR A CD2 
810  C CE1 . TYR A 110 ? 1.0092 0.5228 0.8735 -0.0491 -0.4224 -0.0521 184 TYR A CE1 
811  C CE2 . TYR A 110 ? 1.0311 0.5316 0.8769 -0.0585 -0.3909 -0.0583 184 TYR A CE2 
812  C CZ  . TYR A 110 ? 1.1011 0.5711 0.9071 -0.0485 -0.4171 -0.0575 184 TYR A CZ  
813  O OH  . TYR A 110 ? 1.2140 0.6064 0.9201 -0.0367 -0.4382 -0.0614 184 TYR A OH  
814  N N   . LEU A 111 ? 0.6876 0.5198 0.8686 -0.0554 -0.2150 -0.0494 185 LEU A N   
815  C CA  . LEU A 111 ? 0.6261 0.5285 0.8792 -0.0600 -0.1794 -0.0445 185 LEU A CA  
816  C C   . LEU A 111 ? 0.6412 0.5428 0.9032 -0.0806 -0.1772 -0.0362 185 LEU A C   
817  O O   . LEU A 111 ? 0.6731 0.5246 0.8676 -0.0792 -0.1767 -0.0402 185 LEU A O   
818  C CB  . LEU A 111 ? 0.5417 0.4622 0.7715 -0.0403 -0.1359 -0.0534 185 LEU A CB  
819  C CG  . LEU A 111 ? 0.5695 0.5130 0.8182 -0.0230 -0.1245 -0.0589 185 LEU A CG  
820  C CD1 . LEU A 111 ? 0.7122 0.6038 0.9019 -0.0122 -0.1472 -0.0613 185 LEU A CD1 
821  C CD2 . LEU A 111 ? 0.5728 0.5418 0.8143 -0.0122 -0.0830 -0.0662 185 LEU A CD2 
822  N N   . GLN A 112 ? 0.6399 0.5981 0.9867 -0.0984 -0.1733 -0.0231 186 GLN A N   
823  C CA  . GLN A 112 ? 0.6097 0.5719 0.9751 -0.1228 -0.1713 -0.0095 186 GLN A CA  
824  C C   . GLN A 112 ? 0.5559 0.5836 0.9634 -0.1213 -0.1216 -0.0034 186 GLN A C   
825  O O   . GLN A 112 ? 0.5450 0.6392 1.0312 -0.1224 -0.1064 0.0033  186 GLN A O   
826  C CB  . GLN A 112 ? 0.5866 0.5577 1.0167 -0.1509 -0.2126 0.0062  186 GLN A CB  
827  C CG  . GLN A 112 ? 0.6203 0.5987 1.0798 -0.1809 -0.2115 0.0252  186 GLN A CG  
828  C CD  . GLN A 112 ? 0.5751 0.5829 1.0947 -0.1975 -0.2345 0.0440  186 GLN A CD  
829  O OE1 . GLN A 112 ? 0.5876 0.5970 1.1239 -0.1900 -0.2621 0.0420  186 GLN A OE1 
830  N NE2 . GLN A 112 ? 0.6641 0.6947 1.2176 -0.2205 -0.2240 0.0641  186 GLN A NE2 
831  N N   . THR A 113 ? 0.6121 0.6201 0.9653 -0.1170 -0.0967 -0.0057 187 THR A N   
832  C CA  . THR A 113 ? 0.5631 0.6213 0.9354 -0.1148 -0.0517 -0.0009 187 THR A CA  
833  C C   . THR A 113 ? 0.5776 0.6321 0.9556 -0.1401 -0.0486 0.0193  187 THR A C   
834  O O   . THR A 113 ? 0.6371 0.6419 0.9977 -0.1579 -0.0820 0.0271  187 THR A O   
835  C CB  . THR A 113 ? 0.5795 0.6213 0.8865 -0.0906 -0.0272 -0.0168 187 THR A CB  
836  O OG1 . THR A 113 ? 0.6357 0.6156 0.8734 -0.0898 -0.0408 -0.0177 187 THR A OG1 
837  C CG2 . THR A 113 ? 0.5606 0.6013 0.8609 -0.0689 -0.0311 -0.0336 187 THR A CG2 
838  N N   . GLU A 114 ? 0.5456 0.6479 0.9429 -0.1417 -0.0088 0.0282  188 GLU A N   
839  C CA  . GLU A 114 ? 0.5587 0.6525 0.9474 -0.1638 -0.0009 0.0496  188 GLU A CA  
840  C C   . GLU A 114 ? 0.6516 0.6738 0.9526 -0.1555 -0.0118 0.0431  188 GLU A C   
841  O O   . GLU A 114 ? 0.6619 0.6658 0.9128 -0.1297 -0.0054 0.0238  188 GLU A O   
842  C CB  . GLU A 114 ? 0.5081 0.6644 0.9199 -0.1629 0.0476  0.0594  188 GLU A CB  
843  C CG  . GLU A 114 ? 0.5647 0.7320 0.9349 -0.1323 0.0754  0.0366  188 GLU A CG  
844  C CD  . GLU A 114 ? 0.6541 0.8510 1.0039 -0.1313 0.1167  0.0449  188 GLU A CD  
845  O OE1 . GLU A 114 ? 0.6479 0.8347 0.9862 -0.1518 0.1206  0.0682  188 GLU A OE1 
846  O OE2 . GLU A 114 ? 0.6655 0.8902 1.0056 -0.1103 0.1433  0.0281  188 GLU A OE2 
847  N N   . LEU A 115 ? 0.6860 0.6676 0.9729 -0.1776 -0.0292 0.0608  189 LEU A N   
848  C CA  . LEU A 115 ? 0.6712 0.5835 0.8796 -0.1674 -0.0393 0.0566  189 LEU A CA  
849  C C   . LEU A 115 ? 0.6865 0.6197 0.8667 -0.1587 -0.0034 0.0635  189 LEU A C   
850  O O   . LEU A 115 ? 0.6325 0.6024 0.8414 -0.1774 0.0181  0.0851  189 LEU A O   
851  C CB  . LEU A 115 ? 0.7491 0.5996 0.9485 -0.1932 -0.0746 0.0722  189 LEU A CB  
852  C CG  . LEU A 115 ? 0.7451 0.5127 0.8617 -0.1778 -0.0895 0.0654  189 LEU A CG  
853  C CD1 . LEU A 115 ? 0.8017 0.5418 0.8693 -0.1433 -0.0954 0.0366  189 LEU A CD1 
854  C CD2 . LEU A 115 ? 0.8281 0.5241 0.9340 -0.2030 -0.1297 0.0772  189 LEU A CD2 
855  N N   . CYS A 116 ? 0.7156 0.6269 0.8397 -0.1308 0.0025  0.0468  190 CYS A N   
856  C CA  . CYS A 116 ? 0.6830 0.6076 0.7733 -0.1202 0.0286  0.0513  190 CYS A CA  
857  C C   . CYS A 116 ? 0.7383 0.5979 0.7713 -0.1132 0.0123  0.0575  190 CYS A C   
858  O O   . CYS A 116 ? 0.7747 0.5760 0.7920 -0.1171 -0.0166 0.0576  190 CYS A O   
859  C CB  . CYS A 116 ? 0.6231 0.5808 0.7042 -0.0948 0.0465  0.0296  190 CYS A CB  
860  S SG  . CYS A 116 ? 0.6615 0.6882 0.8059 -0.0974 0.0666  0.0207  190 CYS A SG  
861  N N   . GLY A 117 ? 0.7626 0.6290 0.7620 -0.1014 0.0291  0.0622  191 GLY A N   
862  C CA  . GLY A 117 ? 0.6842 0.4952 0.6330 -0.0879 0.0154  0.0675  191 GLY A CA  
863  C C   . GLY A 117 ? 0.7168 0.5128 0.6405 -0.0558 0.0094  0.0449  191 GLY A C   
864  O O   . GLY A 117 ? 0.6858 0.4970 0.6267 -0.0489 0.0082  0.0270  191 GLY A O   
865  N N   . PRO A 118 ? 0.7735 0.5413 0.6584 -0.0351 0.0059  0.0478  192 PRO A N   
866  C CA  . PRO A 118 ? 0.7369 0.5024 0.6053 -0.0034 0.0060  0.0302  192 PRO A CA  
867  C C   . PRO A 118 ? 0.7140 0.5437 0.6033 0.0021  0.0251  0.0201  192 PRO A C   
868  O O   . PRO A 118 ? 0.6779 0.5468 0.5795 -0.0117 0.0387  0.0263  192 PRO A O   
869  C CB  . PRO A 118 ? 0.7483 0.4770 0.5810 0.0161  -0.0009 0.0411  192 PRO A CB  
870  C CG  . PRO A 118 ? 0.8092 0.5381 0.6383 -0.0060 0.0004  0.0649  192 PRO A CG  
871  C CD  . PRO A 118 ? 0.7779 0.5121 0.6351 -0.0391 0.0003  0.0702  192 PRO A CD  
872  N N   . SER A 119 ? 0.6565 0.4929 0.5462 0.0225  0.0263  0.0045  193 SER A N   
873  C CA  . SER A 119 ? 0.6123 0.5007 0.5191 0.0286  0.0399  -0.0036 193 SER A CA  
874  C C   . SER A 119 ? 0.6168 0.5192 0.5096 0.0371  0.0419  0.0070  193 SER A C   
875  O O   . SER A 119 ? 0.6809 0.5514 0.5512 0.0486  0.0331  0.0185  193 SER A O   
876  C CB  . SER A 119 ? 0.6565 0.5467 0.5667 0.0472  0.0408  -0.0170 193 SER A CB  
877  O OG  . SER A 119 ? 0.7172 0.5902 0.6074 0.0722  0.0391  -0.0129 193 SER A OG  
878  N N   . LEU A 120 ? 0.6165 0.5629 0.5205 0.0320  0.0505  0.0029  194 LEU A N   
879  C CA  . LEU A 120 ? 0.5966 0.5579 0.4868 0.0396  0.0468  0.0120  194 LEU A CA  
880  C C   . LEU A 120 ? 0.6604 0.6162 0.5531 0.0653  0.0392  0.0148  194 LEU A C   
881  O O   . LEU A 120 ? 0.7406 0.6914 0.6207 0.0766  0.0303  0.0285  194 LEU A O   
882  C CB  . LEU A 120 ? 0.6283 0.6315 0.5270 0.0309  0.0530  0.0019  194 LEU A CB  
883  C CG  . LEU A 120 ? 0.6423 0.6624 0.5237 0.0340  0.0439  0.0094  194 LEU A CG  
884  C CD1 . LEU A 120 ? 0.7385 0.7381 0.5841 0.0270  0.0413  0.0280  194 LEU A CD1 
885  C CD2 . LEU A 120 ? 0.5428 0.5935 0.4278 0.0247  0.0468  -0.0061 194 LEU A CD2 
886  N N   . GLN A 121 ? 0.6604 0.6173 0.5690 0.0766  0.0436  0.0039  195 GLN A N   
887  C CA  . GLN A 121 ? 0.6103 0.5654 0.5230 0.1041  0.0432  0.0076  195 GLN A CA  
888  C C   . GLN A 121 ? 0.7028 0.6054 0.5869 0.1205  0.0363  0.0159  195 GLN A C   
889  O O   . GLN A 121 ? 0.7671 0.6682 0.6495 0.1428  0.0321  0.0266  195 GLN A O   
890  C CB  . GLN A 121 ? 0.6399 0.6036 0.5674 0.1112  0.0532  -0.0042 195 GLN A CB  
891  C CG  . GLN A 121 ? 0.6169 0.5854 0.5503 0.1414  0.0602  0.0006  195 GLN A CG  
892  C CD  . GLN A 121 ? 0.6796 0.6507 0.6174 0.1471  0.0728  -0.0084 195 GLN A CD  
893  O OE1 . GLN A 121 ? 0.7061 0.6519 0.6291 0.1344  0.0711  -0.0188 195 GLN A OE1 
894  N NE2 . GLN A 121 ? 0.6149 0.6190 0.5753 0.1655  0.0849  -0.0017 195 GLN A NE2 
895  N N   . GLN A 122 ? 0.7034 0.5604 0.5670 0.1100  0.0324  0.0115  196 GLN A N   
896  C CA  . GLN A 122 ? 0.7137 0.5087 0.5454 0.1221  0.0214  0.0184  196 GLN A CA  
897  C C   . GLN A 122 ? 0.7673 0.5552 0.5886 0.1168  0.0121  0.0377  196 GLN A C   
898  O O   . GLN A 122 ? 0.8585 0.6099 0.6608 0.1386  0.0034  0.0472  196 GLN A O   
899  C CB  . GLN A 122 ? 0.7601 0.5085 0.5760 0.1041  0.0132  0.0112  196 GLN A CB  
900  C CG  . GLN A 122 ? 0.8201 0.5488 0.6260 0.1169  0.0153  -0.0060 196 GLN A CG  
901  C CD  . GLN A 122 ? 0.8349 0.5220 0.6300 0.0947  0.0005  -0.0122 196 GLN A CD  
902  O OE1 . GLN A 122 ? 0.8421 0.5528 0.6632 0.0647  -0.0015 -0.0077 196 GLN A OE1 
903  N NE2 . GLN A 122 ? 0.8901 0.5152 0.6467 0.1102  -0.0105 -0.0226 196 GLN A NE2 
904  N N   . HIS A 123 ? 0.7607 0.5793 0.5898 0.0898  0.0144  0.0441  197 HIS A N   
905  C CA  . HIS A 123 ? 0.7747 0.5858 0.5855 0.0831  0.0064  0.0647  197 HIS A CA  
906  C C   . HIS A 123 ? 0.8018 0.6354 0.6165 0.1082  -0.0002 0.0728  197 HIS A C   
907  O O   . HIS A 123 ? 0.8622 0.6632 0.6585 0.1233  -0.0130 0.0891  197 HIS A O   
908  C CB  . HIS A 123 ? 0.7416 0.5859 0.5546 0.0524  0.0155  0.0678  197 HIS A CB  
909  C CG  . HIS A 123 ? 0.7462 0.5858 0.5315 0.0442  0.0097  0.0900  197 HIS A CG  
910  N ND1 . HIS A 123 ? 0.8349 0.6238 0.5947 0.0383  0.0001  0.1112  197 HIS A ND1 
911  C CD2 . HIS A 123 ? 0.8265 0.7007 0.6000 0.0401  0.0102  0.0952  197 HIS A CD2 
912  C CE1 . HIS A 123 ? 0.9315 0.7263 0.6648 0.0314  -0.0032 0.1307  197 HIS A CE1 
913  N NE2 . HIS A 123 ? 0.9028 0.7486 0.6410 0.0329  0.0023  0.1203  197 HIS A NE2 
914  N N   . CYS A 124 ? 0.7852 0.6737 0.6279 0.1129  0.0059  0.0630  198 CYS A N   
915  C CA  . CYS A 124 ? 0.7903 0.7101 0.6493 0.1339  -0.0032 0.0724  198 CYS A CA  
916  C C   . CYS A 124 ? 0.8186 0.7152 0.6844 0.1704  -0.0043 0.0761  198 CYS A C   
917  O O   . CYS A 124 ? 0.8651 0.7590 0.7320 0.1912  -0.0171 0.0922  198 CYS A O   
918  C CB  . CYS A 124 ? 0.7301 0.7101 0.6237 0.1279  0.0021  0.0610  198 CYS A CB  
919  S SG  . CYS A 124 ? 0.8080 0.8153 0.6871 0.0946  -0.0010 0.0565  198 CYS A SG  
920  N N   . GLU A 125 ? 0.8315 0.7100 0.6992 0.1811  0.0089  0.0611  199 GLU A N   
921  C CA  . GLU A 125 ? 0.8393 0.6859 0.7015 0.2191  0.0124  0.0609  199 GLU A CA  
922  C C   . GLU A 125 ? 0.8845 0.6655 0.7113 0.2298  -0.0035 0.0734  199 GLU A C   
923  O O   . GLU A 125 ? 0.9844 0.7552 0.8149 0.2640  -0.0084 0.0834  199 GLU A O   
924  C CB  . GLU A 125 ? 0.8691 0.6901 0.7184 0.2230  0.0267  0.0413  199 GLU A CB  
925  C CG  . GLU A 125 ? 1.0347 0.8261 0.8719 0.2660  0.0365  0.0368  199 GLU A CG  
926  C CD  . GLU A 125 ? 1.0865 0.9458 0.9684 0.2887  0.0552  0.0396  199 GLU A CD  
927  O OE1 . GLU A 125 ? 1.0759 0.9902 0.9890 0.2661  0.0618  0.0373  199 GLU A OE1 
928  O OE2 . GLU A 125 ? 1.0924 0.9500 0.9809 0.3293  0.0636  0.0452  199 GLU A OE2 
929  N N   . ALA A 126 ? 0.9110 0.6476 0.7072 0.2007  -0.0120 0.0751  200 ALA A N   
930  C CA  . ALA A 126 ? 0.9475 0.6138 0.7088 0.2057  -0.0290 0.0893  200 ALA A CA  
931  C C   . ALA A 126 ? 0.9579 0.6401 0.7219 0.2127  -0.0428 0.1135  200 ALA A C   
932  O O   . ALA A 126 ? 1.0223 0.6590 0.7706 0.2394  -0.0559 0.1258  200 ALA A O   
933  C CB  . ALA A 126 ? 0.9390 0.5656 0.6775 0.1664  -0.0347 0.0909  200 ALA A CB  
934  N N   . TRP A 127 ? 0.9084 0.6497 0.6877 0.1903  -0.0425 0.1201  201 TRP A N   
935  C CA  . TRP A 127 ? 0.9320 0.6861 0.7066 0.1955  -0.0601 0.1434  201 TRP A CA  
936  C C   . TRP A 127 ? 0.9863 0.7846 0.8005 0.2320  -0.0646 0.1462  201 TRP A C   
937  O O   . TRP A 127 ? 0.9854 0.7785 0.7985 0.2503  -0.0841 0.1671  201 TRP A O   
938  C CB  . TRP A 127 ? 0.9249 0.7174 0.6896 0.1592  -0.0600 0.1483  201 TRP A CB  
939  C CG  . TRP A 127 ? 0.9825 0.7280 0.7051 0.1312  -0.0622 0.1633  201 TRP A CG  
940  C CD1 . TRP A 127 ? 0.9824 0.7169 0.6975 0.1008  -0.0472 0.1555  201 TRP A CD1 
941  C CD2 . TRP A 127 ? 1.0205 0.7243 0.7071 0.1308  -0.0806 0.1923  201 TRP A CD2 
942  N NE1 . TRP A 127 ? 1.0152 0.7083 0.6954 0.0794  -0.0526 0.1793  201 TRP A NE1 
943  C CE2 . TRP A 127 ? 1.0264 0.6966 0.6842 0.0967  -0.0730 0.2024  201 TRP A CE2 
944  C CE3 . TRP A 127 ? 1.0520 0.7453 0.7307 0.1558  -0.1036 0.2134  201 TRP A CE3 
945  C CZ2 . TRP A 127 ? 1.1206 0.7446 0.7379 0.0849  -0.0858 0.2338  201 TRP A CZ2 
946  C CZ3 . TRP A 127 ? 1.0890 0.7322 0.7238 0.1461  -0.1193 0.2432  201 TRP A CZ3 
947  C CH2 . TRP A 127 ? 1.1317 0.7392 0.7340 0.1099  -0.1094 0.2538  201 TRP A CH2 
948  N N   . GLY A 128 ? 0.9598 0.8035 0.8121 0.2424  -0.0473 0.1284  202 GLY A N   
949  C CA  . GLY A 128 ? 1.0116 0.8988 0.9105 0.2794  -0.0457 0.1325  202 GLY A CA  
950  C C   . GLY A 128 ? 1.0314 0.9766 0.9617 0.2784  -0.0664 0.1507  202 GLY A C   
951  O O   . GLY A 128 ? 1.0673 1.0553 1.0465 0.3088  -0.0693 0.1598  202 GLY A O   
952  N N   . ALA A 129 ? 0.9799 0.9268 0.8817 0.2441  -0.0813 0.1567  203 ALA A N   
953  C CA  . ALA A 129 ? 0.9750 0.9702 0.8926 0.2359  -0.1057 0.1708  203 ALA A CA  
954  C C   . ALA A 129 ? 0.9849 1.0059 0.8877 0.1956  -0.1016 0.1560  203 ALA A C   
955  O O   . ALA A 129 ? 0.9992 1.0073 0.8896 0.1780  -0.0789 0.1369  203 ALA A O   
956  C CB  . ALA A 129 ? 0.9499 0.9060 0.8285 0.2408  -0.1332 0.1967  203 ALA A CB  
957  N N   . SER A 130 ? 0.9313 0.9863 0.8338 0.1826  -0.1260 0.1641  204 SER A N   
958  C CA  . SER A 130 ? 0.9064 0.9736 0.7810 0.1472  -0.1240 0.1488  204 SER A CA  
959  C C   . SER A 130 ? 0.9727 0.9875 0.7799 0.1270  -0.1120 0.1491  204 SER A C   
960  O O   . SER A 130 ? 1.0862 1.0558 0.8635 0.1353  -0.1160 0.1673  204 SER A O   
961  C CB  . SER A 130 ? 0.8759 0.9774 0.7498 0.1380  -0.1581 0.1573  204 SER A CB  
962  O OG  . SER A 130 ? 0.9128 1.0700 0.8605 0.1537  -0.1710 0.1614  204 SER A OG  
963  N N   . LEU A 131 ? 0.9247 0.9460 0.7121 0.1007  -0.0964 0.1301  205 LEU A N   
964  C CA  . LEU A 131 ? 0.9492 0.9306 0.6779 0.0816  -0.0842 0.1356  205 LEU A CA  
965  C C   . LEU A 131 ? 0.9891 0.9685 0.6617 0.0686  -0.1033 0.1472  205 LEU A C   
966  O O   . LEU A 131 ? 1.0310 1.0417 0.7059 0.0644  -0.1209 0.1381  205 LEU A O   
967  C CB  . LEU A 131 ? 0.9386 0.9243 0.6695 0.0622  -0.0543 0.1123  205 LEU A CB  
968  C CG  . LEU A 131 ? 0.9307 0.9077 0.7008 0.0700  -0.0355 0.1010  205 LEU A CG  
969  C CD1 . LEU A 131 ? 0.9070 0.8917 0.6777 0.0492  -0.0114 0.0810  205 LEU A CD1 
970  C CD2 . LEU A 131 ? 0.9197 0.8469 0.6763 0.0795  -0.0366 0.1190  205 LEU A CD2 
971  N N   . PRO A 132 ? 1.0518 0.9910 0.6696 0.0608  -0.1021 0.1686  206 PRO A N   
972  C CA  . PRO A 132 ? 1.0020 0.9344 0.5514 0.0470  -0.1155 0.1794  206 PRO A CA  
973  C C   . PRO A 132 ? 1.0042 0.9562 0.5288 0.0268  -0.0954 0.1531  206 PRO A C   
974  O O   . PRO A 132 ? 0.9998 0.9574 0.5446 0.0180  -0.0635 0.1359  206 PRO A O   
975  C CB  . PRO A 132 ? 1.0211 0.9044 0.5218 0.0399  -0.1076 0.2086  206 PRO A CB  
976  C CG  . PRO A 132 ? 1.0489 0.9155 0.5924 0.0417  -0.0845 0.2045  206 PRO A CG  
977  C CD  . PRO A 132 ? 1.0552 0.9488 0.6673 0.0640  -0.0915 0.1860  206 PRO A CD  
978  N N   . GLU A 133 ? 1.0100 0.9696 0.4888 0.0211  -0.1170 0.1493  207 GLU A N   
979  C CA  . GLU A 133 ? 1.0438 1.0177 0.4977 0.0071  -0.1029 0.1194  207 GLU A CA  
980  C C   . GLU A 133 ? 1.0808 1.0393 0.4914 -0.0071 -0.0602 0.1160  207 GLU A C   
981  O O   . GLU A 133 ? 1.0791 1.0521 0.4935 -0.0135 -0.0373 0.0880  207 GLU A O   
982  C CB  . GLU A 133 ? 1.0973 1.0695 0.4948 0.0033  -0.1389 0.1168  207 GLU A CB  
983  C CG  . GLU A 133 ? 1.1596 1.1630 0.6166 0.0116  -0.1791 0.1112  207 GLU A CG  
984  C CD  . GLU A 133 ? 1.2642 1.2699 0.6790 0.0001  -0.2080 0.0909  207 GLU A CD  
985  O OE1 . GLU A 133 ? 1.2697 1.2524 0.6110 -0.0111 -0.1896 0.0731  207 GLU A OE1 
986  O OE2 . GLU A 133 ? 1.3110 1.3411 0.7669 0.0024  -0.2494 0.0927  207 GLU A OE2 
987  N N   . ALA A 134 ? 1.1603 1.0911 0.5343 -0.0119 -0.0486 0.1455  208 ALA A N   
988  C CA  . ALA A 134 ? 1.1598 1.0847 0.5046 -0.0270 -0.0051 0.1473  208 ALA A CA  
989  C C   . ALA A 134 ? 1.1143 1.0591 0.5339 -0.0290 0.0233  0.1300  208 ALA A C   
990  O O   . ALA A 134 ? 1.1155 1.0779 0.5356 -0.0363 0.0548  0.1107  208 ALA A O   
991  C CB  . ALA A 134 ? 1.1725 1.0634 0.4731 -0.0350 -0.0009 0.1881  208 ALA A CB  
992  N N   . GLN A 135 ? 1.0902 1.0305 0.5711 -0.0203 0.0117  0.1362  209 GLN A N   
993  C CA  . GLN A 135 ? 1.0084 0.9635 0.5548 -0.0212 0.0320  0.1187  209 GLN A CA  
994  C C   . GLN A 135 ? 0.9473 0.9341 0.5233 -0.0160 0.0329  0.0838  209 GLN A C   
995  O O   . GLN A 135 ? 0.9068 0.9096 0.5126 -0.0213 0.0573  0.0654  209 GLN A O   
996  C CB  . GLN A 135 ? 1.0269 0.9630 0.6194 -0.0093 0.0165  0.1296  209 GLN A CB  
997  C CG  . GLN A 135 ? 1.1036 0.9975 0.6714 -0.0134 0.0108  0.1637  209 GLN A CG  
998  C CD  . GLN A 135 ? 1.1078 0.9752 0.7177 0.0015  -0.0026 0.1676  209 GLN A CD  
999  O OE1 . GLN A 135 ? 1.0243 0.9076 0.6811 0.0118  -0.0002 0.1452  209 GLN A OE1 
1000 N NE2 . GLN A 135 ? 1.2271 1.0491 0.8150 0.0040  -0.0167 0.1961  209 GLN A NE2 
1001 N N   . VAL A 136 ? 0.9269 0.9228 0.4994 -0.0065 0.0037  0.0763  210 VAL A N   
1002 C CA  . VAL A 136 ? 0.9216 0.9431 0.5260 -0.0040 -0.0007 0.0464  210 VAL A CA  
1003 C C   . VAL A 136 ? 0.9527 0.9779 0.5195 -0.0137 0.0212  0.0242  210 VAL A C   
1004 O O   . VAL A 136 ? 0.8508 0.8898 0.4526 -0.0145 0.0389  0.0015  210 VAL A O   
1005 C CB  . VAL A 136 ? 0.9681 1.0001 0.5778 0.0040  -0.0399 0.0480  210 VAL A CB  
1006 C CG1 . VAL A 136 ? 0.9367 0.9912 0.5754 0.0012  -0.0470 0.0196  210 VAL A CG1 
1007 C CG2 . VAL A 136 ? 0.9240 0.9581 0.5818 0.0197  -0.0551 0.0679  210 VAL A CG2 
1008 N N   . TRP A 137 ? 0.9356 0.9457 0.4267 -0.0190 0.0212  0.0307  211 TRP A N   
1009 C CA  . TRP A 137 ? 0.9536 0.9632 0.3986 -0.0235 0.0455  0.0081  211 TRP A CA  
1010 C C   . TRP A 137 ? 0.9237 0.9464 0.4002 -0.0269 0.0896  0.0051  211 TRP A C   
1011 O O   . TRP A 137 ? 0.9532 0.9874 0.4415 -0.0242 0.1092  -0.0220 211 TRP A O   
1012 C CB  . TRP A 137 ? 1.0135 1.0002 0.3610 -0.0272 0.0421  0.0200  211 TRP A CB  
1013 C CG  . TRP A 137 ? 1.0319 1.0060 0.3389 -0.0251 -0.0035 0.0131  211 TRP A CG  
1014 C CD1 . TRP A 137 ? 1.1146 1.0759 0.3948 -0.0243 -0.0400 0.0389  211 TRP A CD1 
1015 C CD2 . TRP A 137 ? 1.0732 1.0448 0.3653 -0.0247 -0.0218 -0.0208 211 TRP A CD2 
1016 N NE1 . TRP A 137 ? 1.1366 1.0928 0.3899 -0.0246 -0.0813 0.0240  211 TRP A NE1 
1017 C CE2 . TRP A 137 ? 1.1108 1.0705 0.3693 -0.0264 -0.0716 -0.0131 211 TRP A CE2 
1018 C CE3 . TRP A 137 ? 1.1198 1.0948 0.4251 -0.0232 -0.0039 -0.0563 211 TRP A CE3 
1019 C CZ2 . TRP A 137 ? 1.2608 1.2115 0.4987 -0.0301 -0.1054 -0.0399 211 TRP A CZ2 
1020 C CZ3 . TRP A 137 ? 1.1786 1.1390 0.4593 -0.0251 -0.0357 -0.0837 211 TRP A CZ3 
1021 C CH2 . TRP A 137 ? 1.2611 1.2093 0.5085 -0.0302 -0.0868 -0.0754 211 TRP A CH2 
1022 N N   . GLY A 138 ? 0.8939 0.9137 0.3877 -0.0331 0.1032  0.0334  212 GLY A N   
1023 C CA  . GLY A 138 ? 0.8548 0.8915 0.3905 -0.0393 0.1396  0.0341  212 GLY A CA  
1024 C C   . GLY A 138 ? 0.8661 0.9194 0.4776 -0.0338 0.1376  0.0123  212 GLY A C   
1025 O O   . GLY A 138 ? 0.8586 0.9310 0.4955 -0.0329 0.1623  -0.0057 212 GLY A O   
1026 N N   . TYR A 139 ? 0.7839 0.8301 0.4312 -0.0280 0.1089  0.0146  213 TYR A N   
1027 C CA  . TYR A 139 ? 0.7925 0.8509 0.5034 -0.0225 0.1065  -0.0035 213 TYR A CA  
1028 C C   . TYR A 139 ? 0.8014 0.8712 0.5119 -0.0172 0.1040  -0.0340 213 TYR A C   
1029 O O   . TYR A 139 ? 0.8187 0.9001 0.5700 -0.0151 0.1155  -0.0515 213 TYR A O   
1030 C CB  . TYR A 139 ? 0.7452 0.7931 0.4856 -0.0146 0.0805  0.0068  213 TYR A CB  
1031 C CG  . TYR A 139 ? 0.7203 0.7463 0.4655 -0.0177 0.0803  0.0325  213 TYR A CG  
1032 C CD1 . TYR A 139 ? 0.7790 0.8022 0.5283 -0.0314 0.1023  0.0433  213 TYR A CD1 
1033 C CD2 . TYR A 139 ? 0.7673 0.7745 0.5159 -0.0065 0.0575  0.0466  213 TYR A CD2 
1034 C CE1 . TYR A 139 ? 0.7905 0.7864 0.5438 -0.0378 0.0977  0.0673  213 TYR A CE1 
1035 C CE2 . TYR A 139 ? 0.8392 0.8154 0.5870 -0.0079 0.0547  0.0680  213 TYR A CE2 
1036 C CZ  . TYR A 139 ? 0.8030 0.7705 0.5515 -0.0255 0.0729  0.0781  213 TYR A CZ  
1037 O OH  . TYR A 139 ? 0.8068 0.7368 0.5541 -0.0306 0.0659  0.0998  213 TYR A OH  
1038 N N   . LEU A 140 ? 0.8022 0.8647 0.4662 -0.0157 0.0855  -0.0402 214 LEU A N   
1039 C CA  . LEU A 140 ? 0.8087 0.8724 0.4647 -0.0131 0.0797  -0.0701 214 LEU A CA  
1040 C C   . LEU A 140 ? 0.8532 0.9188 0.4881 -0.0114 0.1138  -0.0879 214 LEU A C   
1041 O O   . LEU A 140 ? 0.8258 0.8955 0.4891 -0.0064 0.1209  -0.1118 214 LEU A O   
1042 C CB  . LEU A 140 ? 0.8672 0.9179 0.4714 -0.0146 0.0480  -0.0721 214 LEU A CB  
1043 C CG  . LEU A 140 ? 0.8985 0.9382 0.4781 -0.0150 0.0351  -0.1037 214 LEU A CG  
1044 C CD1 . LEU A 140 ? 0.7707 0.8211 0.4185 -0.0153 0.0211  -0.1166 214 LEU A CD1 
1045 C CD2 . LEU A 140 ? 0.8638 0.8859 0.3800 -0.0194 0.0007  -0.1024 214 LEU A CD2 
1046 N N   . ARG A 141 ? 0.8383 0.9020 0.4259 -0.0142 0.1372  -0.0745 215 ARG A N   
1047 C CA  . ARG A 141 ? 0.8404 0.9121 0.4089 -0.0091 0.1754  -0.0898 215 ARG A CA  
1048 C C   . ARG A 141 ? 0.7571 0.8548 0.4031 -0.0081 0.1996  -0.0896 215 ARG A C   
1049 O O   . ARG A 141 ? 0.8658 0.9733 0.5281 0.0018  0.2199  -0.1126 215 ARG A O   
1050 C CB  . ARG A 141 ? 0.9186 0.9863 0.4185 -0.0131 0.1989  -0.0704 215 ARG A CB  
1051 C CG  . ARG A 141 ? 0.9318 1.0090 0.4218 0.0026  0.2345  -0.0813 215 ARG A CG  
1052 C CD  . ARG A 141 ? 1.1276 1.2080 0.5617 0.0029  0.2544  -0.0562 215 ARG A CD  
1053 N NE  . ARG A 141 ? 1.1838 1.2930 0.6240 0.0194  0.2906  -0.0632 215 ARG A NE  
1054 C CZ  . ARG A 141 ? 1.1608 1.3096 0.6671 0.0184  0.3224  -0.0486 215 ARG A CZ  
1055 N NH1 . ARG A 141 ? 1.1347 1.2934 0.7049 0.0006  0.3220  -0.0279 215 ARG A NH1 
1056 N NH2 . ARG A 141 ? 1.1712 1.3554 0.6832 0.0322  0.3519  -0.0571 215 ARG A NH2 
1057 N N   . ASP A 142 ? 0.8013 0.9071 0.4946 -0.0170 0.1951  -0.0645 216 ASP A N   
1058 C CA  . ASP A 142 ? 0.7702 0.8983 0.5352 -0.0185 0.2119  -0.0628 216 ASP A CA  
1059 C C   . ASP A 142 ? 0.6808 0.8088 0.4918 -0.0096 0.1965  -0.0870 216 ASP A C   
1060 O O   . ASP A 142 ? 0.6925 0.8371 0.5412 -0.0029 0.2140  -0.1011 216 ASP A O   
1061 C CB  . ASP A 142 ? 0.7104 0.8357 0.5057 -0.0314 0.2040  -0.0323 216 ASP A CB  
1062 C CG  . ASP A 142 ? 0.8576 0.9882 0.6257 -0.0439 0.2272  -0.0044 216 ASP A CG  
1063 O OD1 . ASP A 142 ? 0.8572 0.9929 0.5716 -0.0408 0.2492  -0.0074 216 ASP A OD1 
1064 O OD2 . ASP A 142 ? 0.8755 1.0017 0.6724 -0.0572 0.2234  0.0210  216 ASP A OD2 
1065 N N   . THR A 143 ? 0.6759 0.7872 0.4870 -0.0088 0.1645  -0.0897 217 THR A N   
1066 C CA  . THR A 143 ? 0.6554 0.7653 0.5072 -0.0027 0.1507  -0.1083 217 THR A CA  
1067 C C   . THR A 143 ? 0.7193 0.8222 0.5484 0.0055  0.1540  -0.1375 217 THR A C   
1068 O O   . THR A 143 ? 0.7252 0.8284 0.5907 0.0118  0.1545  -0.1540 217 THR A O   
1069 C CB  . THR A 143 ? 0.6917 0.7912 0.5524 -0.0041 0.1203  -0.1001 217 THR A CB  
1070 O OG1 . THR A 143 ? 0.6390 0.7352 0.5027 -0.0082 0.1171  -0.0747 217 THR A OG1 
1071 C CG2 . THR A 143 ? 0.5824 0.6827 0.4924 -0.0002 0.1113  -0.1101 217 THR A CG2 
1072 N N   . LEU A 144 ? 0.7418 0.8321 0.5061 0.0060  0.1538  -0.1446 218 LEU A N   
1073 C CA  . LEU A 144 ? 0.7237 0.7980 0.4563 0.0154  0.1578  -0.1757 218 LEU A CA  
1074 C C   . LEU A 144 ? 0.7649 0.8500 0.5167 0.0291  0.1918  -0.1806 218 LEU A C   
1075 O O   . LEU A 144 ? 0.8045 0.8756 0.5703 0.0421  0.1913  -0.1999 218 LEU A O   
1076 C CB  . LEU A 144 ? 0.9066 0.9582 0.5554 0.0137  0.1468  -0.1818 218 LEU A CB  
1077 C CG  . LEU A 144 ? 0.8745 0.9069 0.5082 0.0051  0.1021  -0.1849 218 LEU A CG  
1078 C CD1 . LEU A 144 ? 0.8837 0.8921 0.4281 0.0035  0.0908  -0.1903 218 LEU A CD1 
1079 C CD2 . LEU A 144 ? 0.7694 0.7867 0.4334 0.0066  0.0846  -0.2098 218 LEU A CD2 
1080 N N   . LEU A 145 ? 0.7679 0.8763 0.5257 0.0273  0.2179  -0.1577 219 LEU A N   
1081 C CA  . LEU A 145 ? 0.7244 0.8537 0.5172 0.0410  0.2470  -0.1545 219 LEU A CA  
1082 C C   . LEU A 145 ? 0.7109 0.8542 0.5833 0.0429  0.2407  -0.1575 219 LEU A C   
1083 O O   . LEU A 145 ? 0.6998 0.8466 0.5974 0.0596  0.2502  -0.1684 219 LEU A O   
1084 C CB  . LEU A 145 ? 0.7228 0.8811 0.5162 0.0331  0.2737  -0.1252 219 LEU A CB  
1085 C CG  . LEU A 145 ? 0.7855 0.9357 0.5005 0.0370  0.2890  -0.1179 219 LEU A CG  
1086 C CD1 . LEU A 145 ? 0.8591 1.0386 0.5862 0.0222  0.3109  -0.0826 219 LEU A CD1 
1087 C CD2 . LEU A 145 ? 0.7814 0.9302 0.4678 0.0636  0.3081  -0.1368 219 LEU A CD2 
1088 N N   . ALA A 146 ? 0.6455 0.7943 0.5537 0.0279  0.2239  -0.1477 220 ALA A N   
1089 C CA  . ALA A 146 ? 0.5948 0.7504 0.5693 0.0298  0.2134  -0.1503 220 ALA A CA  
1090 C C   . ALA A 146 ? 0.6249 0.7543 0.5970 0.0408  0.1957  -0.1740 220 ALA A C   
1091 O O   . ALA A 146 ? 0.6538 0.7845 0.6608 0.0530  0.1984  -0.1812 220 ALA A O   
1092 C CB  . ALA A 146 ? 0.5507 0.7069 0.5486 0.0148  0.1962  -0.1354 220 ALA A CB  
1093 N N   . LEU A 147 ? 0.6538 0.7596 0.5856 0.0356  0.1764  -0.1856 221 LEU A N   
1094 C CA  . LEU A 147 ? 0.6322 0.7106 0.5630 0.0408  0.1571  -0.2071 221 LEU A CA  
1095 C C   . LEU A 147 ? 0.6859 0.7457 0.5934 0.0583  0.1689  -0.2243 221 LEU A C   
1096 O O   . LEU A 147 ? 0.7400 0.7826 0.6708 0.0675  0.1614  -0.2367 221 LEU A O   
1097 C CB  . LEU A 147 ? 0.6584 0.7202 0.5517 0.0290  0.1324  -0.2138 221 LEU A CB  
1098 C CG  . LEU A 147 ? 0.5649 0.6363 0.4854 0.0168  0.1123  -0.1888 221 LEU A CG  
1099 C CD1 . LEU A 147 ? 0.5689 0.6263 0.4663 0.0075  0.0831  -0.1898 221 LEU A CD1 
1100 C CD2 . LEU A 147 ? 0.5407 0.6156 0.5184 0.0186  0.1084  -0.1837 221 LEU A CD2 
1101 N N   . ALA A 148 ? 0.6893 0.7488 0.5466 0.0651  0.1882  -0.2245 222 ALA A N   
1102 C CA  . ALA A 148 ? 0.7152 0.7551 0.5444 0.0871  0.2040  -0.2410 222 ALA A CA  
1103 C C   . ALA A 148 ? 0.7230 0.7890 0.6142 0.1024  0.2230  -0.2345 222 ALA A C   
1104 O O   . ALA A 148 ? 0.8293 0.8746 0.7230 0.1212  0.2252  -0.2508 222 ALA A O   
1105 C CB  . ALA A 148 ? 0.7406 0.7780 0.5005 0.0938  0.2246  -0.2389 222 ALA A CB  
1106 N N   . HIS A 149 ? 0.6781 0.7876 0.6197 0.0940  0.2344  -0.2106 223 HIS A N   
1107 C CA  . HIS A 149 ? 0.6622 0.8024 0.6700 0.1051  0.2471  -0.2028 223 HIS A CA  
1108 C C   . HIS A 149 ? 0.6987 0.8221 0.7503 0.1049  0.2217  -0.2107 223 HIS A C   
1109 O O   . HIS A 149 ? 0.7037 0.8279 0.7860 0.1227  0.2259  -0.2174 223 HIS A O   
1110 C CB  . HIS A 149 ? 0.6544 0.8408 0.7047 0.0906  0.2595  -0.1753 223 HIS A CB  
1111 C CG  . HIS A 149 ? 0.6052 0.8260 0.7330 0.0956  0.2636  -0.1653 223 HIS A CG  
1112 N ND1 . HIS A 149 ? 0.5935 0.8447 0.7455 0.1162  0.2882  -0.1645 223 HIS A ND1 
1113 C CD2 . HIS A 149 ? 0.5647 0.7957 0.7506 0.0833  0.2449  -0.1556 223 HIS A CD2 
1114 C CE1 . HIS A 149 ? 0.5840 0.8650 0.8107 0.1146  0.2823  -0.1538 223 HIS A CE1 
1115 N NE2 . HIS A 149 ? 0.5671 0.8332 0.8128 0.0943  0.2552  -0.1487 223 HIS A NE2 
1116 N N   . LEU A 150 ? 0.5573 0.6660 0.6111 0.0866  0.1960  -0.2089 224 LEU A N   
1117 C CA  . LEU A 150 ? 0.6107 0.7009 0.6988 0.0860  0.1722  -0.2144 224 LEU A CA  
1118 C C   . LEU A 150 ? 0.6437 0.6923 0.7034 0.0983  0.1633  -0.2375 224 LEU A C   
1119 O O   . LEU A 150 ? 0.7270 0.7638 0.8165 0.1105  0.1578  -0.2433 224 LEU A O   
1120 C CB  . LEU A 150 ? 0.5868 0.6721 0.6780 0.0664  0.1509  -0.2062 224 LEU A CB  
1121 C CG  . LEU A 150 ? 0.4856 0.5937 0.6239 0.0580  0.1466  -0.1873 224 LEU A CG  
1122 C CD1 . LEU A 150 ? 0.4874 0.6286 0.6330 0.0534  0.1670  -0.1722 224 LEU A CD1 
1123 C CD2 . LEU A 150 ? 0.5377 0.6333 0.6690 0.0450  0.1277  -0.1822 224 LEU A CD2 
1124 N N   . HIS A 151 ? 0.6507 0.6726 0.6507 0.0949  0.1594  -0.2513 225 HIS A N   
1125 C CA  . HIS A 151 ? 0.6803 0.6532 0.6502 0.1017  0.1442  -0.2743 225 HIS A CA  
1126 C C   . HIS A 151 ? 0.7841 0.7418 0.7414 0.1291  0.1642  -0.2872 225 HIS A C   
1127 O O   . HIS A 151 ? 0.8206 0.7377 0.7745 0.1386  0.1523  -0.3027 225 HIS A O   
1128 C CB  . HIS A 151 ? 0.7128 0.6591 0.6204 0.0888  0.1298  -0.2864 225 HIS A CB  
1129 C CG  . HIS A 151 ? 0.7284 0.6901 0.6511 0.0650  0.1096  -0.2756 225 HIS A CG  
1130 N ND1 . HIS A 151 ? 0.6805 0.6315 0.5586 0.0504  0.0930  -0.2822 225 HIS A ND1 
1131 C CD2 . HIS A 151 ? 0.5860 0.5723 0.5612 0.0553  0.1034  -0.2588 225 HIS A CD2 
1132 C CE1 . HIS A 151 ? 0.6712 0.6442 0.5791 0.0340  0.0797  -0.2701 225 HIS A CE1 
1133 N NE2 . HIS A 151 ? 0.6218 0.6133 0.5851 0.0376  0.0875  -0.2561 225 HIS A NE2 
1134 N N   . SER A 152 ? 0.7889 0.7778 0.7400 0.1430  0.1956  -0.2798 226 SER A N   
1135 C CA  . SER A 152 ? 0.7955 0.7753 0.7379 0.1739  0.2193  -0.2910 226 SER A CA  
1136 C C   . SER A 152 ? 0.7678 0.7606 0.7800 0.1862  0.2162  -0.2866 226 SER A C   
1137 O O   . SER A 152 ? 0.8726 0.8474 0.8807 0.2137  0.2294  -0.2991 226 SER A O   
1138 C CB  . SER A 152 ? 0.8157 0.8368 0.7438 0.1869  0.2559  -0.2800 226 SER A CB  
1139 O OG  . SER A 152 ? 0.8097 0.8925 0.8131 0.1848  0.2677  -0.2564 226 SER A OG  
1140 N N   . GLN A 153 ? 0.7374 0.7569 0.8092 0.1682  0.1987  -0.2694 227 GLN A N   
1141 C CA  . GLN A 153 ? 0.6834 0.7102 0.8177 0.1773  0.1893  -0.2643 227 GLN A CA  
1142 C C   . GLN A 153 ? 0.7114 0.6981 0.8518 0.1634  0.1548  -0.2686 227 GLN A C   
1143 O O   . GLN A 153 ? 0.7047 0.7006 0.8964 0.1607  0.1400  -0.2574 227 GLN A O   
1144 C CB  . GLN A 153 ? 0.6628 0.7482 0.8606 0.1693  0.1954  -0.2401 227 GLN A CB  
1145 C CG  . GLN A 153 ? 0.6035 0.7372 0.8080 0.1796  0.2292  -0.2304 227 GLN A CG  
1146 C CD  . GLN A 153 ? 0.5596 0.7447 0.8228 0.1620  0.2287  -0.2054 227 GLN A CD  
1147 O OE1 . GLN A 153 ? 0.5635 0.7514 0.8153 0.1378  0.2203  -0.1953 227 GLN A OE1 
1148 N NE2 . GLN A 153 ? 0.6066 0.8304 0.9340 0.1741  0.2356  -0.1954 227 GLN A NE2 
1149 N N   . GLY A 154 ? 0.6961 0.5923 1.0892 0.0889  0.1623  -0.2126 228 GLY A N   
1150 C CA  . GLY A 154 ? 0.6746 0.5478 1.0369 0.0897  0.1274  -0.1928 228 GLY A CA  
1151 C C   . GLY A 154 ? 0.6847 0.5812 1.0148 0.0910  0.0799  -0.1577 228 GLY A C   
1152 O O   . GLY A 154 ? 0.6844 0.5640 1.0131 0.0966  0.0458  -0.1332 228 GLY A O   
1153 N N   . LEU A 155 ? 0.6798 0.6092 0.9801 0.0848  0.0793  -0.1551 229 LEU A N   
1154 C CA  . LEU A 155 ? 0.5897 0.5373 0.8528 0.0842  0.0413  -0.1276 229 LEU A CA  
1155 C C   . LEU A 155 ? 0.6406 0.5913 0.8119 0.0655  0.0460  -0.1253 229 LEU A C   
1156 O O   . LEU A 155 ? 0.6623 0.6176 0.8018 0.0534  0.0743  -0.1433 229 LEU A O   
1157 C CB  . LEU A 155 ? 0.5285 0.5087 0.8322 0.0907  0.0353  -0.1261 229 LEU A CB  
1158 C CG  . LEU A 155 ? 0.5212 0.5107 0.9368 0.1083  0.0329  -0.1311 229 LEU A CG  
1159 C CD1 . LEU A 155 ? 0.4296 0.4541 0.8823 0.1095  0.0240  -0.1293 229 LEU A CD1 
1160 C CD2 . LEU A 155 ? 0.5528 0.5223 1.0072 0.1228  -0.0085 -0.1089 229 LEU A CD2 
1161 N N   . VAL A 156 ? 0.5995 0.5461 0.7293 0.0625  0.0184  -0.1022 230 VAL A N   
1162 C CA  . VAL A 156 ? 0.5798 0.5345 0.6405 0.0472  0.0203  -0.0969 230 VAL A CA  
1163 C C   . VAL A 156 ? 0.6001 0.5725 0.6374 0.0499  0.0007  -0.0790 230 VAL A C   
1164 O O   . VAL A 156 ? 0.6515 0.6125 0.6913 0.0563  -0.0243 -0.0617 230 VAL A O   
1165 C CB  . VAL A 156 ? 0.5666 0.4970 0.6019 0.0375  0.0157  -0.0896 230 VAL A CB  
1166 C CG1 . VAL A 156 ? 0.6436 0.5897 0.6264 0.0212  0.0197  -0.0866 230 VAL A CG1 
1167 C CG2 . VAL A 156 ? 0.7068 0.6105 0.7697 0.0356  0.0340  -0.1097 230 VAL A CG2 
1168 N N   . HIS A 157 ? 0.5416 0.5362 0.5515 0.0440  0.0113  -0.0829 231 HIS A N   
1169 C CA  . HIS A 157 ? 0.5219 0.5295 0.5153 0.0471  -0.0017 -0.0714 231 HIS A CA  
1170 C C   . HIS A 157 ? 0.5860 0.5849 0.5365 0.0423  -0.0126 -0.0548 231 HIS A C   
1171 O O   . HIS A 157 ? 0.5961 0.5844 0.5329 0.0457  -0.0303 -0.0433 231 HIS A O   
1172 C CB  . HIS A 157 ? 0.5313 0.5594 0.5118 0.0432  0.0146  -0.0786 231 HIS A CB  
1173 C CG  . HIS A 157 ? 0.5641 0.6008 0.5342 0.0466  0.0052  -0.0709 231 HIS A CG  
1174 N ND1 . HIS A 157 ? 0.6051 0.6436 0.5378 0.0439  0.0031  -0.0608 231 HIS A ND1 
1175 C CD2 . HIS A 157 ? 0.5556 0.5974 0.5518 0.0514  -0.0008 -0.0741 231 HIS A CD2 
1176 C CE1 . HIS A 157 ? 0.5801 0.6197 0.5093 0.0472  -0.0021 -0.0598 231 HIS A CE1 
1177 N NE2 . HIS A 157 ? 0.5678 0.6095 0.5338 0.0505  -0.0071 -0.0673 231 HIS A NE2 
1178 N N   . LEU A 158 ? 0.6105 0.6131 0.5383 0.0322  -0.0012 -0.0542 232 LEU A N   
1179 C CA  . LEU A 158 ? 0.5882 0.5848 0.4865 0.0248  -0.0023 -0.0405 232 LEU A CA  
1180 C C   . LEU A 158 ? 0.5642 0.5743 0.4393 0.0258  0.0017  -0.0342 232 LEU A C   
1181 O O   . LEU A 158 ? 0.6921 0.6952 0.5439 0.0202  0.0067  -0.0240 232 LEU A O   
1182 C CB  . LEU A 158 ? 0.5768 0.5411 0.4671 0.0255  -0.0163 -0.0272 232 LEU A CB  
1183 C CG  . LEU A 158 ? 0.6262 0.5694 0.5385 0.0224  -0.0165 -0.0297 232 LEU A CG  
1184 C CD1 . LEU A 158 ? 0.6564 0.5627 0.5571 0.0242  -0.0341 -0.0102 232 LEU A CD1 
1185 C CD2 . LEU A 158 ? 0.6404 0.5918 0.5462 0.0070  -0.0011 -0.0350 232 LEU A CD2 
1186 N N   . ASP A 159 ? 0.6202 0.6461 0.5023 0.0319  0.0042  -0.0409 233 ASP A N   
1187 C CA  . ASP A 159 ? 0.5521 0.5856 0.4171 0.0342  0.0105  -0.0372 233 ASP A CA  
1188 C C   . ASP A 159 ? 0.5962 0.6500 0.4760 0.0378  0.0177  -0.0430 233 ASP A C   
1189 O O   . ASP A 159 ? 0.6146 0.6679 0.4909 0.0429  0.0197  -0.0442 233 ASP A O   
1190 C CB  . ASP A 159 ? 0.6343 0.6459 0.4776 0.0376  -0.0011 -0.0353 233 ASP A CB  
1191 C CG  . ASP A 159 ? 0.7028 0.7070 0.5124 0.0357  0.0116  -0.0323 233 ASP A CG  
1192 O OD1 . ASP A 159 ? 0.7774 0.7923 0.5874 0.0319  0.0293  -0.0278 233 ASP A OD1 
1193 O OD2 . ASP A 159 ? 0.6885 0.6756 0.4744 0.0368  0.0054  -0.0362 233 ASP A OD2 
1194 N N   . VAL A 160 ? 0.5542 0.6201 0.4444 0.0331  0.0211  -0.0464 234 VAL A N   
1195 C CA  . VAL A 160 ? 0.5213 0.6002 0.4137 0.0338  0.0264  -0.0471 234 VAL A CA  
1196 C C   . VAL A 160 ? 0.5353 0.6291 0.4286 0.0363  0.0290  -0.0361 234 VAL A C   
1197 O O   . VAL A 160 ? 0.6032 0.7094 0.5024 0.0309  0.0275  -0.0301 234 VAL A O   
1198 C CB  . VAL A 160 ? 0.4890 0.5691 0.3760 0.0244  0.0283  -0.0536 234 VAL A CB  
1199 C CG1 . VAL A 160 ? 0.5256 0.6132 0.4009 0.0226  0.0309  -0.0485 234 VAL A CG1 
1200 C CG2 . VAL A 160 ? 0.5522 0.6171 0.4505 0.0244  0.0338  -0.0675 234 VAL A CG2 
1201 N N   . LYS A 161 ? 0.5277 0.6204 0.4237 0.0443  0.0338  -0.0338 235 LYS A N   
1202 C CA  . LYS A 161 ? 0.5036 0.6081 0.4122 0.0505  0.0394  -0.0241 235 LYS A CA  
1203 C C   . LYS A 161 ? 0.5294 0.6243 0.4405 0.0583  0.0445  -0.0240 235 LYS A C   
1204 O O   . LYS A 161 ? 0.5317 0.6118 0.4349 0.0573  0.0443  -0.0329 235 LYS A O   
1205 C CB  . LYS A 161 ? 0.5537 0.6551 0.4623 0.0521  0.0497  -0.0243 235 LYS A CB  
1206 C CG  . LYS A 161 ? 0.5527 0.6268 0.4350 0.0537  0.0533  -0.0334 235 LYS A CG  
1207 C CD  . LYS A 161 ? 0.6323 0.6956 0.4986 0.0518  0.0688  -0.0332 235 LYS A CD  
1208 C CE  . LYS A 161 ? 0.7503 0.7792 0.5716 0.0475  0.0632  -0.0404 235 LYS A CE  
1209 N NZ  . LYS A 161 ? 0.8021 0.8111 0.5894 0.0414  0.0814  -0.0395 235 LYS A NZ  
1210 N N   . PRO A 162 ? 0.5713 0.6744 0.5015 0.0661  0.0484  -0.0133 236 PRO A N   
1211 C CA  . PRO A 162 ? 0.5310 0.6191 0.4652 0.0732  0.0541  -0.0115 236 PRO A CA  
1212 C C   . PRO A 162 ? 0.5773 0.6416 0.4998 0.0740  0.0626  -0.0269 236 PRO A C   
1213 O O   . PRO A 162 ? 0.5890 0.6393 0.5096 0.0720  0.0627  -0.0309 236 PRO A O   
1214 C CB  . PRO A 162 ? 0.5547 0.6541 0.5221 0.0847  0.0582  0.0022  236 PRO A CB  
1215 C CG  . PRO A 162 ? 0.5320 0.6597 0.5128 0.0795  0.0443  0.0130  236 PRO A CG  
1216 C CD  . PRO A 162 ? 0.5728 0.7005 0.5308 0.0683  0.0446  -0.0001 236 PRO A CD  
1217 N N   . ALA A 163 ? 0.5505 0.6074 0.4614 0.0742  0.0690  -0.0357 237 ALA A N   
1218 C CA  . ALA A 163 ? 0.5438 0.5726 0.4319 0.0717  0.0716  -0.0507 237 ALA A CA  
1219 C C   . ALA A 163 ? 0.5798 0.6035 0.4592 0.0633  0.0538  -0.0577 237 ALA A C   
1220 O O   . ALA A 163 ? 0.5769 0.5804 0.4464 0.0593  0.0480  -0.0689 237 ALA A O   
1221 C CB  . ALA A 163 ? 0.5897 0.6051 0.4510 0.0699  0.0826  -0.0571 237 ALA A CB  
1222 N N   . ASN A 164 ? 0.6067 0.6473 0.4944 0.0599  0.0448  -0.0528 238 ASN A N   
1223 C CA  . ASN A 164 ? 0.5775 0.6162 0.4728 0.0545  0.0313  -0.0597 238 ASN A CA  
1224 C C   . ASN A 164 ? 0.5343 0.5830 0.4533 0.0523  0.0370  -0.0594 238 ASN A C   
1225 O O   . ASN A 164 ? 0.5028 0.5549 0.4411 0.0487  0.0326  -0.0659 238 ASN A O   
1226 C CB  . ASN A 164 ? 0.5359 0.5771 0.4231 0.0519  0.0214  -0.0576 238 ASN A CB  
1227 C CG  . ASN A 164 ? 0.6189 0.6409 0.4724 0.0502  0.0162  -0.0570 238 ASN A CG  
1228 O OD1 . ASN A 164 ? 0.6461 0.6493 0.4788 0.0492  0.0160  -0.0632 238 ASN A OD1 
1229 N ND2 . ASN A 164 ? 0.6269 0.6479 0.4685 0.0474  0.0138  -0.0504 238 ASN A ND2 
1230 N N   . ILE A 165 ? 0.5674 0.6181 0.4861 0.0541  0.0483  -0.0512 239 ILE A N   
1231 C CA  . ILE A 165 ? 0.5037 0.5537 0.4311 0.0490  0.0578  -0.0491 239 ILE A CA  
1232 C C   . ILE A 165 ? 0.5878 0.6221 0.5251 0.0499  0.0645  -0.0490 239 ILE A C   
1233 O O   . ILE A 165 ? 0.5780 0.6038 0.5102 0.0572  0.0661  -0.0437 239 ILE A O   
1234 C CB  . ILE A 165 ? 0.5344 0.5911 0.4429 0.0470  0.0609  -0.0355 239 ILE A CB  
1235 C CG1 . ILE A 165 ? 0.5518 0.6202 0.4508 0.0434  0.0538  -0.0388 239 ILE A CG1 
1236 C CG2 . ILE A 165 ? 0.5067 0.5532 0.4076 0.0382  0.0743  -0.0327 239 ILE A CG2 
1237 C CD1 . ILE A 165 ? 0.5760 0.6506 0.4526 0.0382  0.0492  -0.0268 239 ILE A CD1 
1238 N N   . PHE A 166 ? 0.5765 0.6060 0.5345 0.0422  0.0714  -0.0561 240 PHE A N   
1239 C CA  . PHE A 166 ? 0.5398 0.5518 0.5128 0.0394  0.0772  -0.0588 240 PHE A CA  
1240 C C   . PHE A 166 ? 0.6096 0.6132 0.5876 0.0311  0.0967  -0.0500 240 PHE A C   
1241 O O   . PHE A 166 ? 0.5870 0.5992 0.5715 0.0230  0.1079  -0.0528 240 PHE A O   
1242 C CB  . PHE A 166 ? 0.5326 0.5441 0.5323 0.0337  0.0642  -0.0764 240 PHE A CB  
1243 C CG  . PHE A 166 ? 0.5578 0.5680 0.5372 0.0384  0.0442  -0.0828 240 PHE A CG  
1244 C CD1 . PHE A 166 ? 0.4867 0.5116 0.4656 0.0401  0.0320  -0.0832 240 PHE A CD1 
1245 C CD2 . PHE A 166 ? 0.5739 0.5620 0.5296 0.0401  0.0411  -0.0883 240 PHE A CD2 
1246 C CE1 . PHE A 166 ? 0.5647 0.5819 0.5163 0.0422  0.0148  -0.0853 240 PHE A CE1 
1247 C CE2 . PHE A 166 ? 0.6048 0.5847 0.5283 0.0412  0.0275  -0.0938 240 PHE A CE2 
1248 C CZ  . PHE A 166 ? 0.5848 0.5790 0.5042 0.0417  0.0133  -0.0903 240 PHE A CZ  
1249 N N   . LEU A 167 ? 0.6026 0.5846 0.5765 0.0326  0.1040  -0.0397 241 LEU A N   
1250 C CA  . LEU A 167 ? 0.6394 0.6046 0.6063 0.0238  0.1228  -0.0252 241 LEU A CA  
1251 C C   . LEU A 167 ? 0.6753 0.6385 0.6781 0.0085  0.1388  -0.0384 241 LEU A C   
1252 O O   . LEU A 167 ? 0.6547 0.6231 0.6950 0.0057  0.1297  -0.0563 241 LEU A O   
1253 C CB  . LEU A 167 ? 0.6280 0.5659 0.5884 0.0312  0.1243  -0.0085 241 LEU A CB  
1254 C CG  . LEU A 167 ? 0.6708 0.6075 0.6032 0.0425  0.1152  0.0168  241 LEU A CG  
1255 C CD1 . LEU A 167 ? 0.5987 0.5637 0.5279 0.0530  0.0987  0.0112  241 LEU A CD1 
1256 C CD2 . LEU A 167 ? 0.6869 0.5951 0.6322 0.0531  0.1169  0.0315  241 LEU A CD2 
1257 N N   . GLY A 168 ? 0.6655 0.6202 0.6560 -0.0036 0.1626  -0.0293 242 GLY A N   
1258 C CA  . GLY A 168 ? 0.6749 0.6258 0.7052 -0.0202 0.1870  -0.0385 242 GLY A CA  
1259 C C   . GLY A 168 ? 0.7086 0.6231 0.7155 -0.0308 0.2098  -0.0177 242 GLY A C   
1260 O O   . GLY A 168 ? 0.7115 0.6038 0.6704 -0.0235 0.2024  0.0059  242 GLY A O   
1261 N N   . PRO A 169 ? 0.6798 0.5866 0.7251 -0.0487 0.2371  -0.0240 243 PRO A N   
1262 C CA  . PRO A 169 ? 0.7144 0.5796 0.7352 -0.0616 0.2619  -0.0019 243 PRO A CA  
1263 C C   . PRO A 169 ? 0.7417 0.5857 0.6844 -0.0682 0.2794  0.0208  243 PRO A C   
1264 O O   . PRO A 169 ? 0.7931 0.6553 0.7128 -0.0697 0.2854  0.0118  243 PRO A O   
1265 C CB  . PRO A 169 ? 0.7210 0.5910 0.8110 -0.0825 0.2908  -0.0183 243 PRO A CB  
1266 C CG  . PRO A 169 ? 0.6584 0.5720 0.8181 -0.0758 0.2658  -0.0480 243 PRO A CG  
1267 C CD  . PRO A 169 ? 0.6235 0.5594 0.7453 -0.0583 0.2451  -0.0499 243 PRO A CD  
1268 N N   . ARG A 170 ? 0.7918 0.5915 0.6891 -0.0728 0.2853  0.0512  244 ARG A N   
1269 C CA  . ARG A 170 ? 0.8429 0.6101 0.6512 -0.0831 0.2968  0.0789  244 ARG A CA  
1270 C C   . ARG A 170 ? 0.8960 0.6837 0.6555 -0.0707 0.2679  0.0804  244 ARG A C   
1271 O O   . ARG A 170 ? 0.8801 0.6618 0.5817 -0.0840 0.2827  0.0794  244 ARG A O   
1272 C CB  . ARG A 170 ? 0.8293 0.5818 0.6242 -0.1110 0.3484  0.0719  244 ARG A CB  
1273 C CG  . ARG A 170 ? 0.8687 0.6045 0.7222 -0.1263 0.3786  0.0699  244 ARG A CG  
1274 C CD  . ARG A 170 ? 0.9353 0.6530 0.7717 -0.1533 0.4301  0.0668  244 ARG A CD  
1275 N NE  . ARG A 170 ? 1.0672 0.7812 0.9810 -0.1673 0.4550  0.0582  244 ARG A NE  
1276 C CZ  . ARG A 170 ? 1.0439 0.8012 1.0647 -0.1692 0.4622  0.0260  244 ARG A CZ  
1277 N NH1 . ARG A 170 ? 0.9006 0.7073 0.9654 -0.1565 0.4466  0.0008  244 ARG A NH1 
1278 N NH2 . ARG A 170 ? 0.9841 0.7357 1.0714 -0.1840 0.4811  0.0196  244 ARG A NH2 
1279 N N   . GLY A 171 ? 0.8148 0.6243 0.5982 -0.0471 0.2290  0.0807  245 GLY A N   
1280 C CA  . GLY A 171 ? 0.7732 0.5996 0.5163 -0.0364 0.1989  0.0874  245 GLY A CA  
1281 C C   . GLY A 171 ? 0.8421 0.7047 0.5930 -0.0374 0.2004  0.0581  245 GLY A C   
1282 O O   . GLY A 171 ? 0.8929 0.7650 0.6036 -0.0345 0.1795  0.0625  245 GLY A O   
1283 N N   . ARG A 172 ? 0.8330 0.7154 0.6398 -0.0418 0.2218  0.0293  246 ARG A N   
1284 C CA  . ARG A 172 ? 0.8154 0.7305 0.6423 -0.0390 0.2204  0.0030  246 ARG A CA  
1285 C C   . ARG A 172 ? 0.7475 0.6925 0.6160 -0.0185 0.1860  -0.0061 246 ARG A C   
1286 O O   . ARG A 172 ? 0.7409 0.6821 0.6295 -0.0079 0.1704  0.0017  246 ARG A O   
1287 C CB  . ARG A 172 ? 0.7736 0.6984 0.6537 -0.0511 0.2558  -0.0214 246 ARG A CB  
1288 C CG  . ARG A 172 ? 0.8059 0.6980 0.6531 -0.0743 0.3013  -0.0147 246 ARG A CG  
1289 C CD  . ARG A 172 ? 0.9035 0.7711 0.6557 -0.0860 0.3120  -0.0074 246 ARG A CD  
1290 N NE  . ARG A 172 ? 0.9479 0.8405 0.7078 -0.0800 0.3063  -0.0313 246 ARG A NE  
1291 C CZ  . ARG A 172 ? 0.9775 0.8803 0.7762 -0.0846 0.3269  -0.0557 246 ARG A CZ  
1292 N NH1 . ARG A 172 ? 0.9513 0.8434 0.7818 -0.0972 0.3613  -0.0621 246 ARG A NH1 
1293 N NH2 . ARG A 172 ? 0.9205 0.8412 0.7288 -0.0764 0.3139  -0.0733 246 ARG A NH2 
1294 N N   . CYS A 173 ? 0.6926 0.6623 0.5708 -0.0140 0.1776  -0.0233 247 CYS A N   
1295 C CA  . CYS A 173 ? 0.7294 0.7232 0.6444 0.0015  0.1508  -0.0334 247 CYS A CA  
1296 C C   . CYS A 173 ? 0.6157 0.6303 0.5638 0.0013  0.1533  -0.0557 247 CYS A C   
1297 O O   . CYS A 173 ? 0.5920 0.6039 0.5306 -0.0082 0.1754  -0.0642 247 CYS A O   
1298 C CB  . CYS A 173 ? 0.6750 0.6734 0.5582 0.0129  0.1248  -0.0191 247 CYS A CB  
1299 S SG  . CYS A 173 ? 0.8115 0.8168 0.6486 0.0067  0.1195  -0.0195 247 CYS A SG  
1300 N N   . LYS A 174 ? 0.5809 0.6113 0.5656 0.0115  0.1312  -0.0650 248 LYS A N   
1301 C CA  . LYS A 174 ? 0.5645 0.6125 0.5917 0.0140  0.1258  -0.0820 248 LYS A CA  
1302 C C   . LYS A 174 ? 0.5125 0.5679 0.5259 0.0251  0.0972  -0.0806 248 LYS A C   
1303 O O   . LYS A 174 ? 0.5432 0.5942 0.5400 0.0309  0.0812  -0.0735 248 LYS A O   
1304 C CB  . LYS A 174 ? 0.5817 0.6380 0.6752 0.0113  0.1234  -0.0931 248 LYS A CB  
1305 C CG  . LYS A 174 ? 0.6455 0.6952 0.7641 -0.0023 0.1562  -0.0949 248 LYS A CG  
1306 C CD  . LYS A 174 ? 0.6856 0.7509 0.8869 -0.0069 0.1507  -0.1080 248 LYS A CD  
1307 C CE  . LYS A 174 ? 0.7889 0.8384 0.9963 -0.0167 0.1553  -0.1033 248 LYS A CE  
1308 N NZ  . LYS A 174 ? 0.7218 0.7533 0.8799 -0.0088 0.1296  -0.0945 248 LYS A NZ  
1309 N N   . LEU A 175 ? 0.5157 0.5786 0.5368 0.0271  0.0948  -0.0881 249 LEU A N   
1310 C CA  . LEU A 175 ? 0.4755 0.5416 0.4845 0.0350  0.0705  -0.0855 249 LEU A CA  
1311 C C   . LEU A 175 ? 0.5027 0.5716 0.5478 0.0399  0.0473  -0.0900 249 LEU A C   
1312 O O   . LEU A 175 ? 0.5271 0.6036 0.6260 0.0386  0.0476  -0.0990 249 LEU A O   
1313 C CB  . LEU A 175 ? 0.5654 0.6315 0.5683 0.0338  0.0765  -0.0912 249 LEU A CB  
1314 C CG  . LEU A 175 ? 0.5720 0.6371 0.5616 0.0389  0.0560  -0.0871 249 LEU A CG  
1315 C CD1 . LEU A 175 ? 0.5002 0.5660 0.4483 0.0393  0.0477  -0.0739 249 LEU A CD1 
1316 C CD2 . LEU A 175 ? 0.5523 0.6121 0.5412 0.0352  0.0667  -0.0961 249 LEU A CD2 
1317 N N   . GLY A 176 ? 0.5108 0.5727 0.5265 0.0440  0.0268  -0.0836 250 GLY A N   
1318 C CA  . GLY A 176 ? 0.5129 0.5691 0.5424 0.0451  -0.0001 -0.0862 250 GLY A CA  
1319 C C   . GLY A 176 ? 0.5099 0.5539 0.5028 0.0481  -0.0196 -0.0790 250 GLY A C   
1320 O O   . GLY A 176 ? 0.4936 0.5386 0.4692 0.0499  -0.0123 -0.0736 250 GLY A O   
1321 N N   . ASP A 177 ? 0.5822 0.6107 0.5585 0.0456  -0.0443 -0.0789 251 ASP A N   
1322 C CA  . ASP A 177 ? 0.5748 0.5824 0.5044 0.0449  -0.0630 -0.0706 251 ASP A CA  
1323 C C   . ASP A 177 ? 0.5671 0.5769 0.5133 0.0493  -0.0700 -0.0626 251 ASP A C   
1324 O O   . ASP A 177 ? 0.6423 0.6524 0.5675 0.0500  -0.0531 -0.0576 251 ASP A O   
1325 C CB  . ASP A 177 ? 0.6975 0.6938 0.5711 0.0437  -0.0427 -0.0676 251 ASP A CB  
1326 C CG  . ASP A 177 ? 0.8218 0.7865 0.6344 0.0378  -0.0567 -0.0631 251 ASP A CG  
1327 O OD1 . ASP A 177 ? 0.7960 0.7476 0.6034 0.0357  -0.0852 -0.0557 251 ASP A OD1 
1328 O OD2 . ASP A 177 ? 0.8620 0.8119 0.6315 0.0351  -0.0381 -0.0663 251 ASP A OD2 
1329 N N   . PHE A 178 ? 0.5825 0.5931 0.5731 0.0522  -0.0962 -0.0613 252 PHE A N   
1330 C CA  . PHE A 178 ? 0.5423 0.5506 0.5616 0.0586  -0.1033 -0.0544 252 PHE A CA  
1331 C C   . PHE A 178 ? 0.5779 0.5551 0.5541 0.0570  -0.1354 -0.0373 252 PHE A C   
1332 O O   . PHE A 178 ? 0.6153 0.5845 0.6262 0.0634  -0.1563 -0.0279 252 PHE A O   
1333 C CB  . PHE A 178 ? 0.5045 0.5329 0.6142 0.0654  -0.1088 -0.0623 252 PHE A CB  
1334 C CG  . PHE A 178 ? 0.5103 0.5621 0.6541 0.0644  -0.0699 -0.0781 252 PHE A CG  
1335 C CD1 . PHE A 178 ? 0.5379 0.5900 0.6519 0.0624  -0.0369 -0.0820 252 PHE A CD1 
1336 C CD2 . PHE A 178 ? 0.5086 0.5791 0.7097 0.0625  -0.0677 -0.0879 252 PHE A CD2 
1337 C CE1 . PHE A 178 ? 0.5079 0.5732 0.6365 0.0585  -0.0035 -0.0938 252 PHE A CE1 
1338 C CE2 . PHE A 178 ? 0.4964 0.5812 0.7180 0.0587  -0.0283 -0.1000 252 PHE A CE2 
1339 C CZ  . PHE A 178 ? 0.5081 0.5876 0.6870 0.0567  0.0033  -0.1021 252 PHE A CZ  
1340 N N   . GLY A 179 ? 0.5977 0.5527 0.4971 0.0481  -0.1376 -0.0325 253 GLY A N   
1341 C CA  . GLY A 179 ? 0.6443 0.5614 0.4852 0.0425  -0.1653 -0.0150 253 GLY A CA  
1342 C C   . GLY A 179 ? 0.6993 0.6023 0.5255 0.0436  -0.1536 -0.0016 253 GLY A C   
1343 O O   . GLY A 179 ? 0.7853 0.6560 0.5849 0.0416  -0.1807 0.0172  253 GLY A O   
1344 N N   . LEU A 180 ? 0.6057 0.5294 0.4469 0.0449  -0.1163 -0.0097 254 LEU A N   
1345 C CA  . LEU A 180 ? 0.6941 0.6062 0.5261 0.0424  -0.1029 -0.0002 254 LEU A CA  
1346 C C   . LEU A 180 ? 0.6882 0.6122 0.5884 0.0510  -0.1002 -0.0059 254 LEU A C   
1347 O O   . LEU A 180 ? 0.6876 0.6000 0.5863 0.0478  -0.0889 -0.0014 254 LEU A O   
1348 C CB  . LEU A 180 ? 0.7249 0.6507 0.5297 0.0351  -0.0666 -0.0056 254 LEU A CB  
1349 C CG  . LEU A 180 ? 0.7192 0.6291 0.4584 0.0259  -0.0543 -0.0013 254 LEU A CG  
1350 C CD1 . LEU A 180 ? 0.7398 0.6634 0.4757 0.0195  -0.0209 -0.0011 254 LEU A CD1 
1351 C CD2 . LEU A 180 ? 0.8673 0.7312 0.5469 0.0186  -0.0771 0.0155  254 LEU A CD2 
1352 N N   . LEU A 181 ? 0.6764 0.6208 0.6376 0.0601  -0.1063 -0.0176 255 LEU A N   
1353 C CA  . LEU A 181 ? 0.6299 0.5836 0.6558 0.0676  -0.0932 -0.0286 255 LEU A CA  
1354 C C   . LEU A 181 ? 0.6642 0.5881 0.7131 0.0740  -0.1149 -0.0139 255 LEU A C   
1355 O O   . LEU A 181 ? 0.6717 0.5758 0.7142 0.0773  -0.1520 0.0048  255 LEU A O   
1356 C CB  . LEU A 181 ? 0.5354 0.5162 0.6260 0.0748  -0.0902 -0.0441 255 LEU A CB  
1357 C CG  . LEU A 181 ? 0.5535 0.5441 0.7162 0.0822  -0.0678 -0.0609 255 LEU A CG  
1358 C CD1 . LEU A 181 ? 0.4860 0.5051 0.6780 0.0804  -0.0435 -0.0791 255 LEU A CD1 
1359 C CD2 . LEU A 181 ? 0.5195 0.4999 0.7543 0.0959  -0.0949 -0.0529 255 LEU A CD2 
1360 N N   . VAL A 182 ? 0.6604 0.5759 0.7315 0.0745  -0.0937 -0.0216 256 VAL A N   
1361 C CA  . VAL A 182 ? 0.6619 0.5451 0.7655 0.0821  -0.1092 -0.0093 256 VAL A CA  
1362 C C   . VAL A 182 ? 0.6686 0.5597 0.8520 0.0922  -0.0864 -0.0321 256 VAL A C   
1363 O O   . VAL A 182 ? 0.6676 0.5818 0.8569 0.0876  -0.0533 -0.0567 256 VAL A O   
1364 C CB  . VAL A 182 ? 0.7110 0.5622 0.7598 0.0697  -0.1020 0.0035  256 VAL A CB  
1365 C CG1 . VAL A 182 ? 0.8655 0.7018 0.8362 0.0593  -0.1187 0.0262  256 VAL A CG1 
1366 C CG2 . VAL A 182 ? 0.7145 0.5812 0.7492 0.0575  -0.0641 -0.0182 256 VAL A CG2 
1367 N N   . GLU A 183 ? 0.7148 0.5815 0.9574 0.1058  -0.1031 -0.0231 257 GLU A N   
1368 C CA  . GLU A 183 ? 0.7014 0.5671 1.0282 0.1175  -0.0777 -0.0455 257 GLU A CA  
1369 C C   . GLU A 183 ? 0.7577 0.5800 1.0767 0.1146  -0.0666 -0.0444 257 GLU A C   
1370 O O   . GLU A 183 ? 0.7828 0.5708 1.0948 0.1185  -0.0975 -0.0160 257 GLU A O   
1371 C CB  . GLU A 183 ? 0.6832 0.5584 1.1107 0.1390  -0.1051 -0.0378 257 GLU A CB  
1372 C CG  . GLU A 183 ? 0.7113 0.5903 1.2417 0.1530  -0.0703 -0.0650 257 GLU A CG  
1373 C CD  . GLU A 183 ? 0.8197 0.7163 1.4634 0.1733  -0.0994 -0.0546 257 GLU A CD  
1374 O OE1 . GLU A 183 ? 0.8520 0.7543 1.4874 0.1756  -0.1532 -0.0257 257 GLU A OE1 
1375 O OE2 . GLU A 183 ? 0.8212 0.7304 1.5348 0.1753  -0.0666 -0.0734 257 GLU A OE2 
1376 N N   . LEU A 184 ? 0.7540 0.5727 1.0675 0.1051  -0.0238 -0.0747 258 LEU A N   
1377 C CA  . LEU A 184 ? 0.7658 0.5410 1.0705 0.0983  -0.0108 -0.0789 258 LEU A CA  
1378 C C   . LEU A 184 ? 0.7986 0.5415 1.1954 0.1204  -0.0183 -0.0748 258 LEU A C   
1379 O O   . LEU A 184 ? 0.7928 0.5507 1.2727 0.1372  -0.0042 -0.0924 258 LEU A O   
1380 C CB  . LEU A 184 ? 0.7582 0.5349 1.0329 0.0806  0.0335  -0.1161 258 LEU A CB  
1381 C CG  . LEU A 184 ? 0.8149 0.6252 1.0103 0.0609  0.0376  -0.1183 258 LEU A CG  
1382 C CD1 . LEU A 184 ? 0.8004 0.6098 0.9662 0.0436  0.0745  -0.1535 258 LEU A CD1 
1383 C CD2 . LEU A 184 ? 0.7656 0.5678 0.9021 0.0474  0.0159  -0.0920 258 LEU A CD2 
1384 N N   . GLY A 185 ? 0.8456 0.5433 1.2336 0.1206  -0.0391 -0.0501 259 GLY A N   
1385 C CA  . GLY A 185 ? 0.8504 0.5109 1.3277 0.1433  -0.0515 -0.0401 259 GLY A CA  
1386 C C   . GLY A 185 ? 1.0632 0.6750 1.5111 0.1426  -0.0900 0.0029  259 GLY A C   
1387 O O   . GLY A 185 ? 1.1659 0.7298 1.6631 0.1528  -0.0904 0.0094  259 GLY A O   
1388 N N   . GLU A 191 ? 1.3529 0.9390 1.0918 0.0242  -0.2041 0.1750  265 GLU A N   
1389 C CA  . GLU A 191 ? 1.3231 0.9611 1.1401 0.0431  -0.2124 0.1483  265 GLU A CA  
1390 C C   . GLU A 191 ? 1.1659 0.8579 0.9737 0.0364  -0.1760 0.1166  265 GLU A C   
1391 O O   . GLU A 191 ? 1.0833 0.8137 0.9271 0.0466  -0.1826 0.0985  265 GLU A O   
1392 C CB  . GLU A 191 ? 1.3591 1.0027 1.2791 0.0600  -0.2070 0.1353  265 GLU A CB  
1393 C CG  . GLU A 191 ? 1.3122 0.9581 1.2429 0.0487  -0.1615 0.1163  265 GLU A CG  
1394 C CD  . GLU A 191 ? 1.3401 0.9801 1.3625 0.0635  -0.1539 0.1001  265 GLU A CD  
1395 O OE1 . GLU A 191 ? 1.3460 0.9718 1.4286 0.0842  -0.1844 0.1114  265 GLU A OE1 
1396 O OE2 . GLU A 191 ? 1.2609 0.9094 1.2974 0.0539  -0.1177 0.0750  265 GLU A OE2 
1397 N N   . VAL A 192 ? 1.1882 0.8822 0.9540 0.0190  -0.1385 0.1119  266 VAL A N   
1398 C CA  . VAL A 192 ? 1.0709 0.8136 0.8346 0.0132  -0.1054 0.0862  266 VAL A CA  
1399 C C   . VAL A 192 ? 1.1207 0.8525 0.8012 -0.0016 -0.0936 0.0956  266 VAL A C   
1400 O O   . VAL A 192 ? 1.1572 0.8434 0.7764 -0.0149 -0.0934 0.1192  266 VAL A O   
1401 C CB  . VAL A 192 ? 0.9987 0.7602 0.7979 0.0052  -0.0721 0.0697  266 VAL A CB  
1402 C CG1 . VAL A 192 ? 0.9800 0.7915 0.7814 0.0006  -0.0461 0.0479  266 VAL A CG1 
1403 C CG2 . VAL A 192 ? 1.0308 0.7922 0.9016 0.0177  -0.0780 0.0566  266 VAL A CG2 
1404 N N   . GLN A 193 ? 1.0462 0.8154 0.7229 0.0001  -0.0803 0.0768  267 GLN A N   
1405 C CA  . GLN A 193 ? 1.0082 0.7697 0.6152 -0.0120 -0.0611 0.0785  267 GLN A CA  
1406 C C   . GLN A 193 ? 0.9947 0.7972 0.6255 -0.0176 -0.0189 0.0619  267 GLN A C   
1407 O O   . GLN A 193 ? 0.8412 0.6808 0.5346 -0.0123 -0.0117 0.0478  267 GLN A O   
1408 C CB  . GLN A 193 ? 1.0190 0.7828 0.6018 -0.0056 -0.0828 0.0710  267 GLN A CB  
1409 C CG  . GLN A 193 ? 1.0672 0.8008 0.6452 0.0010  -0.1337 0.0866  267 GLN A CG  
1410 C CD  . GLN A 193 ? 1.1669 0.9128 0.7416 0.0060  -0.1576 0.0745  267 GLN A CD  
1411 O OE1 . GLN A 193 ? 1.3324 1.0509 0.8278 -0.0057 -0.1610 0.0756  267 GLN A OE1 
1412 N NE2 . GLN A 193 ? 1.0597 0.8442 0.7193 0.0211  -0.1708 0.0606  267 GLN A NE2 
1413 N N   . GLU A 194 ? 1.0211 0.8142 0.5998 -0.0292 0.0086  0.0637  268 GLU A N   
1414 C CA  . GLU A 194 ? 0.9832 0.8154 0.5926 -0.0338 0.0479  0.0514  268 GLU A CA  
1415 C C   . GLU A 194 ? 0.9037 0.7827 0.5597 -0.0192 0.0460  0.0310  268 GLU A C   
1416 O O   . GLU A 194 ? 0.9490 0.8228 0.5787 -0.0129 0.0397  0.0237  268 GLU A O   
1417 C CB  . GLU A 194 ? 1.0394 0.8473 0.5869 -0.0477 0.0826  0.0559  268 GLU A CB  
1418 C CG  . GLU A 194 ? 1.1419 0.8974 0.6315 -0.0664 0.0921  0.0787  268 GLU A CG  
1419 C CD  . GLU A 194 ? 1.1695 0.9433 0.7126 -0.0778 0.1153  0.0839  268 GLU A CD  
1420 O OE1 . GLU A 194 ? 1.0787 0.9073 0.7009 -0.0717 0.1206  0.0691  268 GLU A OE1 
1421 O OE2 . GLU A 194 ? 1.2273 0.9573 0.7299 -0.0951 0.1264  0.1039  268 GLU A OE2 
1422 N N   . GLY A 195 ? 0.9140 0.8338 0.6335 -0.0162 0.0505  0.0223  269 GLY A N   
1423 C CA  . GLY A 195 ? 0.8509 0.8111 0.6088 -0.0051 0.0512  0.0075  269 GLY A CA  
1424 C C   . GLY A 195 ? 0.8389 0.8238 0.6095 -0.0068 0.0812  0.0042  269 GLY A C   
1425 O O   . GLY A 195 ? 0.8146 0.7890 0.5691 -0.0174 0.1068  0.0107  269 GLY A O   
1426 N N   . ASP A 196 ? 0.8080 0.8249 0.6123 0.0040  0.0802  -0.0052 270 ASP A N   
1427 C CA  . ASP A 196 ? 0.7566 0.8011 0.5918 0.0066  0.1053  -0.0071 270 ASP A CA  
1428 C C   . ASP A 196 ? 0.6682 0.7468 0.5570 -0.0022 0.1092  -0.0018 270 ASP A C   
1429 O O   . ASP A 196 ? 0.6613 0.7580 0.5745 -0.0031 0.0871  -0.0034 270 ASP A O   
1430 C CB  . ASP A 196 ? 0.7389 0.8014 0.5941 0.0212  0.0985  -0.0146 270 ASP A CB  
1431 C CG  . ASP A 196 ? 0.7123 0.7887 0.5922 0.0283  0.1262  -0.0169 270 ASP A CG  
1432 O OD1 . ASP A 196 ? 0.7037 0.7994 0.6183 0.0232  0.1477  -0.0121 270 ASP A OD1 
1433 O OD2 . ASP A 196 ? 0.7732 0.8408 0.6449 0.0389  0.1283  -0.0242 270 ASP A OD2 
1434 N N   . PRO A 197 ? 0.6587 0.7453 0.5665 -0.0112 0.1376  0.0031  271 PRO A N   
1435 C CA  . PRO A 197 ? 0.6406 0.7623 0.6086 -0.0229 0.1368  0.0080  271 PRO A CA  
1436 C C   . PRO A 197 ? 0.5890 0.7583 0.6191 -0.0146 0.1209  0.0071  271 PRO A C   
1437 O O   . PRO A 197 ? 0.6044 0.7981 0.6700 -0.0251 0.1006  0.0091  271 PRO A O   
1438 C CB  . PRO A 197 ? 0.5822 0.7018 0.5621 -0.0337 0.1780  0.0130  271 PRO A CB  
1439 C CG  . PRO A 197 ? 0.6798 0.7759 0.6196 -0.0224 0.2030  0.0070  271 PRO A CG  
1440 C CD  . PRO A 197 ? 0.6874 0.7492 0.5623 -0.0139 0.1740  0.0029  271 PRO A CD  
1441 N N   . ARG A 198 ? 0.5798 0.7583 0.6205 0.0025  0.1273  0.0050  272 ARG A N   
1442 C CA  . ARG A 198 ? 0.5294 0.7474 0.6257 0.0116  0.1082  0.0094  272 ARG A CA  
1443 C C   . ARG A 198 ? 0.5431 0.7610 0.6189 0.0071  0.0704  0.0086  272 ARG A C   
1444 O O   . ARG A 198 ? 0.4957 0.7441 0.6094 0.0025  0.0470  0.0147  272 ARG A O   
1445 C CB  . ARG A 198 ? 0.5533 0.7676 0.6540 0.0317  0.1211  0.0074  272 ARG A CB  
1446 C CG  . ARG A 198 ? 0.6655 0.8811 0.7952 0.0367  0.1646  0.0047  272 ARG A CG  
1447 C CD  . ARG A 198 ? 0.6953 0.8969 0.8228 0.0560  0.1792  -0.0015 272 ARG A CD  
1448 N NE  . ARG A 198 ? 0.7606 0.9117 0.8022 0.0550  0.1849  -0.0137 272 ARG A NE  
1449 C CZ  . ARG A 198 ? 0.8632 0.9928 0.8839 0.0672  0.1852  -0.0215 272 ARG A CZ  
1450 N NH1 . ARG A 198 ? 0.8627 1.0119 0.9379 0.0831  0.1824  -0.0167 272 ARG A NH1 
1451 N NH2 . ARG A 198 ? 0.8950 0.9807 0.8403 0.0624  0.1850  -0.0328 272 ARG A NH2 
1452 N N   . TYR A 199 ? 0.5774 0.7600 0.5942 0.0070  0.0639  0.0008  273 TYR A N   
1453 C CA  . TYR A 199 ? 0.5688 0.7449 0.5627 0.0032  0.0383  -0.0041 273 TYR A CA  
1454 C C   . TYR A 199 ? 0.5770 0.7340 0.5517 -0.0122 0.0326  -0.0104 273 TYR A C   
1455 O O   . TYR A 199 ? 0.6275 0.7695 0.5783 -0.0152 0.0196  -0.0190 273 TYR A O   
1456 C CB  . TYR A 199 ? 0.5803 0.7339 0.5393 0.0161  0.0378  -0.0099 273 TYR A CB  
1457 C CG  . TYR A 199 ? 0.5545 0.7168 0.5293 0.0311  0.0466  -0.0052 273 TYR A CG  
1458 C CD1 . TYR A 199 ? 0.5720 0.7213 0.5418 0.0384  0.0694  -0.0075 273 TYR A CD1 
1459 C CD2 . TYR A 199 ? 0.5287 0.7059 0.5183 0.0365  0.0329  0.0016  273 TYR A CD2 
1460 C CE1 . TYR A 199 ? 0.5885 0.7399 0.5748 0.0520  0.0810  -0.0065 273 TYR A CE1 
1461 C CE2 . TYR A 199 ? 0.5548 0.7349 0.5643 0.0514  0.0414  0.0073  273 TYR A CE2 
1462 C CZ  . TYR A 199 ? 0.6132 0.7808 0.6248 0.0597  0.0669  0.0014  273 TYR A CZ  
1463 O OH  . TYR A 199 ? 0.7213 0.8860 0.7543 0.0744  0.0792  0.0035  273 TYR A OH  
1464 N N   . MET A 200 ? 0.6289 0.7827 0.6151 -0.0224 0.0457  -0.0065 274 MET A N   
1465 C CA  . MET A 200 ? 0.6298 0.7565 0.5978 -0.0358 0.0425  -0.0105 274 MET A CA  
1466 C C   . MET A 200 ? 0.6508 0.7905 0.6366 -0.0524 0.0236  -0.0172 274 MET A C   
1467 O O   . MET A 200 ? 0.6589 0.8337 0.6844 -0.0610 0.0155  -0.0129 274 MET A O   
1468 C CB  . MET A 200 ? 0.6342 0.7486 0.6047 -0.0448 0.0646  -0.0015 274 MET A CB  
1469 C CG  . MET A 200 ? 0.7004 0.7846 0.6596 -0.0605 0.0622  -0.0014 274 MET A CG  
1470 S SD  . MET A 200 ? 0.8652 0.9272 0.8147 -0.0724 0.0933  0.0137  274 MET A SD  
1471 C CE  . MET A 200 ? 0.8818 0.9127 0.7699 -0.0538 0.1009  0.0178  274 MET A CE  
1472 N N   . ALA A 201 ? 0.6506 0.7604 0.6093 -0.0574 0.0155  -0.0288 275 ALA A N   
1473 C CA  . ALA A 201 ? 0.6456 0.7544 0.6084 -0.0774 0.0009  -0.0400 275 ALA A CA  
1474 C C   . ALA A 201 ? 0.7130 0.8189 0.7027 -0.0965 0.0068  -0.0357 275 ALA A C   
1475 O O   . ALA A 201 ? 0.7590 0.8415 0.7436 -0.0937 0.0239  -0.0273 275 ALA A O   
1476 C CB  . ALA A 201 ? 0.7164 0.7878 0.6452 -0.0766 -0.0006 -0.0574 275 ALA A CB  
1477 N N   . PRO A 202 ? 0.6629 0.7891 0.6790 -0.1183 -0.0086 -0.0403 276 PRO A N   
1478 C CA  . PRO A 202 ? 0.6365 0.7648 0.6900 -0.1390 -0.0004 -0.0352 276 PRO A CA  
1479 C C   . PRO A 202 ? 0.7084 0.7833 0.7380 -0.1461 0.0116  -0.0403 276 PRO A C   
1480 O O   . PRO A 202 ? 0.7313 0.7943 0.7761 -0.1535 0.0303  -0.0277 276 PRO A O   
1481 C CB  . PRO A 202 ? 0.6255 0.7835 0.7086 -0.1628 -0.0287 -0.0430 276 PRO A CB  
1482 C CG  . PRO A 202 ? 0.6622 0.8071 0.6948 -0.1591 -0.0493 -0.0576 276 PRO A CG  
1483 C CD  . PRO A 202 ? 0.6576 0.8011 0.6661 -0.1286 -0.0361 -0.0500 276 PRO A CD  
1484 N N   . GLU A 203 ? 0.7522 0.7911 0.7461 -0.1435 0.0042  -0.0573 277 GLU A N   
1485 C CA  . GLU A 203 ? 0.7635 0.7493 0.7464 -0.1485 0.0139  -0.0616 277 GLU A CA  
1486 C C   . GLU A 203 ? 0.7776 0.7380 0.7460 -0.1286 0.0287  -0.0425 277 GLU A C   
1487 O O   . GLU A 203 ? 0.7613 0.6792 0.7272 -0.1340 0.0361  -0.0354 277 GLU A O   
1488 C CB  . GLU A 203 ? 0.7302 0.6827 0.6869 -0.1485 0.0078  -0.0874 277 GLU A CB  
1489 C CG  . GLU A 203 ? 0.8706 0.8141 0.8045 -0.1208 0.0124  -0.0906 277 GLU A CG  
1490 C CD  . GLU A 203 ? 0.7992 0.7769 0.7156 -0.1158 0.0035  -0.0975 277 GLU A CD  
1491 O OE1 . GLU A 203 ? 0.7796 0.7933 0.7041 -0.1289 -0.0100 -0.0930 277 GLU A OE1 
1492 O OE2 . GLU A 203 ? 0.7994 0.7671 0.6985 -0.0992 0.0096  -0.1057 277 GLU A OE2 
1493 N N   . LEU A 204 ? 0.7672 0.7482 0.7226 -0.1075 0.0308  -0.0331 278 LEU A N   
1494 C CA  . LEU A 204 ? 0.8047 0.7593 0.7368 -0.0928 0.0396  -0.0151 278 LEU A CA  
1495 C C   . LEU A 204 ? 0.7877 0.7325 0.7215 -0.1078 0.0573  0.0040  278 LEU A C   
1496 O O   . LEU A 204 ? 0.7937 0.6964 0.6977 -0.1050 0.0627  0.0204  278 LEU A O   
1497 C CB  . LEU A 204 ? 0.8268 0.8048 0.7433 -0.0720 0.0387  -0.0120 278 LEU A CB  
1498 C CG  . LEU A 204 ? 0.7918 0.7723 0.7013 -0.0547 0.0267  -0.0258 278 LEU A CG  
1499 C CD1 . LEU A 204 ? 0.7081 0.6907 0.5979 -0.0363 0.0264  -0.0173 278 LEU A CD1 
1500 C CD2 . LEU A 204 ? 0.8312 0.7738 0.7431 -0.0525 0.0209  -0.0358 278 LEU A CD2 
1501 N N   . LEU A 205 ? 0.7827 0.7647 0.7527 -0.1251 0.0662  0.0036  279 LEU A N   
1502 C CA  . LEU A 205 ? 0.7614 0.7375 0.7412 -0.1418 0.0911  0.0203  279 LEU A CA  
1503 C C   . LEU A 205 ? 0.8558 0.7816 0.8303 -0.1601 0.0942  0.0264  279 LEU A C   
1504 O O   . LEU A 205 ? 0.9321 0.8283 0.8887 -0.1704 0.1163  0.0460  279 LEU A O   
1505 C CB  . LEU A 205 ? 0.7585 0.7926 0.7997 -0.1562 0.0987  0.0172  279 LEU A CB  
1506 C CG  . LEU A 205 ? 0.7440 0.8160 0.7982 -0.1430 0.1172  0.0237  279 LEU A CG  
1507 C CD1 . LEU A 205 ? 0.7128 0.8377 0.8465 -0.1601 0.1277  0.0245  279 LEU A CD1 
1508 C CD2 . LEU A 205 ? 0.8184 0.8506 0.8196 -0.1380 0.1467  0.0388  279 LEU A CD2 
1509 N N   . GLN A 206 ? 0.9062 0.8160 0.8920 -0.1657 0.0755  0.0096  280 GLN A N   
1510 C CA  . GLN A 206 ? 0.9333 0.7894 0.9194 -0.1820 0.0782  0.0129  280 GLN A CA  
1511 C C   . GLN A 206 ? 0.9759 0.7793 0.9325 -0.1620 0.0653  0.0120  280 GLN A C   
1512 O O   . GLN A 206 ? 1.0150 0.7786 0.9830 -0.1700 0.0609  0.0022  280 GLN A O   
1513 C CB  . GLN A 206 ? 0.9519 0.8217 0.9803 -0.2089 0.0704  -0.0081 280 GLN A CB  
1514 C CG  . GLN A 206 ? 0.9656 0.8854 1.0434 -0.2330 0.0809  -0.0036 280 GLN A CG  
1515 C CD  . GLN A 206 ? 0.9853 0.9730 1.0875 -0.2254 0.0655  -0.0141 280 GLN A CD  
1516 O OE1 . GLN A 206 ? 0.9856 0.9791 1.0670 -0.2128 0.0436  -0.0310 280 GLN A OE1 
1517 N NE2 . GLN A 206 ? 0.9145 0.9515 1.0636 -0.2331 0.0792  -0.0030 280 GLN A NE2 
1518 N N   . GLY A 207 ? 0.9570 0.7597 0.8828 -0.1360 0.0589  0.0212  281 GLY A N   
1519 C CA  . GLY A 207 ? 0.9786 0.7345 0.8887 -0.1161 0.0448  0.0268  281 GLY A CA  
1520 C C   . GLY A 207 ? 0.9355 0.6909 0.8698 -0.1041 0.0337  -0.0009 281 GLY A C   
1521 O O   . GLY A 207 ? 1.0281 0.7425 0.9696 -0.0891 0.0251  0.0016  281 GLY A O   
1522 N N   . SER A 208 ? 0.8948 0.6916 0.8417 -0.1106 0.0345  -0.0264 282 SER A N   
1523 C CA  . SER A 208 ? 0.8631 0.6553 0.8205 -0.1036 0.0311  -0.0557 282 SER A CA  
1524 C C   . SER A 208 ? 0.8860 0.7097 0.8345 -0.0802 0.0260  -0.0585 282 SER A C   
1525 O O   . SER A 208 ? 0.8803 0.7486 0.8193 -0.0825 0.0248  -0.0622 282 SER A O   
1526 C CB  . SER A 208 ? 0.8600 0.6691 0.8219 -0.1293 0.0321  -0.0810 282 SER A CB  
1527 O OG  . SER A 208 ? 0.9576 0.7540 0.9140 -0.1258 0.0341  -0.1115 282 SER A OG  
1528 N N   . TYR A 209 ? 0.8942 0.6943 0.8527 -0.0577 0.0215  -0.0551 283 TYR A N   
1529 C CA  . TYR A 209 ? 0.8257 0.6522 0.7844 -0.0368 0.0166  -0.0576 283 TYR A CA  
1530 C C   . TYR A 209 ? 0.8137 0.6329 0.7957 -0.0293 0.0263  -0.0864 283 TYR A C   
1531 O O   . TYR A 209 ? 0.7997 0.5798 0.8076 -0.0276 0.0327  -0.0970 283 TYR A O   
1532 C CB  . TYR A 209 ? 0.8364 0.6470 0.7943 -0.0185 0.0012  -0.0314 283 TYR A CB  
1533 C CG  . TYR A 209 ? 0.9269 0.7393 0.8466 -0.0273 -0.0018 -0.0051 283 TYR A CG  
1534 C CD1 . TYR A 209 ? 0.9530 0.7270 0.8596 -0.0399 -0.0005 0.0146  283 TYR A CD1 
1535 C CD2 . TYR A 209 ? 0.9329 0.7808 0.8286 -0.0243 -0.0011 -0.0009 283 TYR A CD2 
1536 C CE1 . TYR A 209 ? 1.0009 0.7725 0.8673 -0.0505 0.0051  0.0372  283 TYR A CE1 
1537 C CE2 . TYR A 209 ? 0.9790 0.8244 0.8384 -0.0330 0.0045  0.0189  283 TYR A CE2 
1538 C CZ  . TYR A 209 ? 1.0373 0.8450 0.8801 -0.0468 0.0093  0.0376  283 TYR A CZ  
1539 O OH  . TYR A 209 ? 1.0962 0.8975 0.8979 -0.0578 0.0227  0.0559  283 TYR A OH  
1540 N N   . GLY A 210 ? 0.8052 0.6581 0.7779 -0.0255 0.0313  -0.0994 284 GLY A N   
1541 C CA  . GLY A 210 ? 0.7224 0.5680 0.7073 -0.0225 0.0485  -0.1285 284 GLY A CA  
1542 C C   . GLY A 210 ? 0.7047 0.5878 0.6683 -0.0208 0.0524  -0.1340 284 GLY A C   
1543 O O   . GLY A 210 ? 0.6680 0.5820 0.6117 -0.0217 0.0405  -0.1168 284 GLY A O   
1544 N N   . THR A 211 ? 0.7061 0.5818 0.6750 -0.0188 0.0733  -0.1588 285 THR A N   
1545 C CA  . THR A 211 ? 0.6466 0.5504 0.5944 -0.0179 0.0803  -0.1625 285 THR A CA  
1546 C C   . THR A 211 ? 0.6693 0.5905 0.5620 -0.0384 0.0719  -0.1610 285 THR A C   
1547 O O   . THR A 211 ? 0.7037 0.6516 0.5786 -0.0360 0.0680  -0.1517 285 THR A O   
1548 C CB  . THR A 211 ? 0.6611 0.5480 0.6230 -0.0150 0.1118  -0.1903 285 THR A CB  
1549 O OG1 . THR A 211 ? 0.7558 0.6069 0.6915 -0.0332 0.1294  -0.2171 285 THR A OG1 
1550 C CG2 . THR A 211 ? 0.6182 0.4995 0.6554 0.0091  0.1156  -0.1880 285 THR A CG2 
1551 N N   . ALA A 212 ? 0.7327 0.6387 0.6037 -0.0586 0.0663  -0.1687 286 ALA A N   
1552 C CA  . ALA A 212 ? 0.7501 0.6772 0.5808 -0.0785 0.0496  -0.1639 286 ALA A CA  
1553 C C   . ALA A 212 ? 0.7081 0.6762 0.5526 -0.0689 0.0315  -0.1343 286 ALA A C   
1554 O O   . ALA A 212 ? 0.7293 0.7228 0.5524 -0.0743 0.0202  -0.1263 286 ALA A O   
1555 C CB  . ALA A 212 ? 0.7555 0.6632 0.5770 -0.1025 0.0412  -0.1744 286 ALA A CB  
1556 N N   . ALA A 213 ? 0.7128 0.6829 0.5901 -0.0545 0.0293  -0.1177 287 ALA A N   
1557 C CA  . ALA A 213 ? 0.6385 0.6398 0.5242 -0.0477 0.0189  -0.0937 287 ALA A CA  
1558 C C   . ALA A 213 ? 0.6859 0.7098 0.5635 -0.0350 0.0194  -0.0883 287 ALA A C   
1559 O O   . ALA A 213 ? 0.7329 0.7847 0.6102 -0.0349 0.0117  -0.0748 287 ALA A O   
1560 C CB  . ALA A 213 ? 0.6783 0.6652 0.5826 -0.0369 0.0192  -0.0789 287 ALA A CB  
1561 N N   . ASP A 214 ? 0.7092 0.7211 0.5881 -0.0244 0.0303  -0.0987 288 ASP A N   
1562 C CA  . ASP A 214 ? 0.6382 0.6670 0.5113 -0.0148 0.0332  -0.0941 288 ASP A CA  
1563 C C   . ASP A 214 ? 0.6865 0.7255 0.5258 -0.0274 0.0303  -0.0952 288 ASP A C   
1564 O O   . ASP A 214 ? 0.6795 0.7369 0.5145 -0.0215 0.0255  -0.0821 288 ASP A O   
1565 C CB  . ASP A 214 ? 0.6307 0.6458 0.5224 -0.0043 0.0482  -0.1065 288 ASP A CB  
1566 C CG  . ASP A 214 ? 0.6283 0.6394 0.5551 0.0111  0.0405  -0.0982 288 ASP A CG  
1567 O OD1 . ASP A 214 ? 0.5825 0.5993 0.5039 0.0132  0.0270  -0.0817 288 ASP A OD1 
1568 O OD2 . ASP A 214 ? 0.6190 0.6202 0.5791 0.0200  0.0481  -0.1078 288 ASP A OD2 
1569 N N   . VAL A 215 ? 0.7259 0.7482 0.5374 -0.0456 0.0315  -0.1104 289 VAL A N   
1570 C CA  . VAL A 215 ? 0.7138 0.7396 0.4805 -0.0611 0.0218  -0.1094 289 VAL A CA  
1571 C C   . VAL A 215 ? 0.6998 0.7578 0.4796 -0.0640 -0.0052 -0.0877 289 VAL A C   
1572 O O   . VAL A 215 ? 0.7176 0.7910 0.4844 -0.0631 -0.0179 -0.0727 289 VAL A O   
1573 C CB  . VAL A 215 ? 0.7502 0.7434 0.4741 -0.0838 0.0280  -0.1340 289 VAL A CB  
1574 C CG1 . VAL A 215 ? 0.7904 0.7809 0.4531 -0.1032 0.0119  -0.1308 289 VAL A CG1 
1575 C CG2 . VAL A 215 ? 0.7906 0.7532 0.5163 -0.0780 0.0626  -0.1573 289 VAL A CG2 
1576 N N   . PHE A 216 ? 0.6793 0.7472 0.4913 -0.0672 -0.0129 -0.0843 290 PHE A N   
1577 C CA  . PHE A 216 ? 0.6480 0.7513 0.4900 -0.0692 -0.0325 -0.0649 290 PHE A CA  
1578 C C   . PHE A 216 ? 0.6047 0.7295 0.4725 -0.0471 -0.0269 -0.0469 290 PHE A C   
1579 O O   . PHE A 216 ? 0.6249 0.7753 0.5077 -0.0444 -0.0412 -0.0310 290 PHE A O   
1580 C CB  . PHE A 216 ? 0.6817 0.7879 0.5567 -0.0782 -0.0326 -0.0656 290 PHE A CB  
1581 C CG  . PHE A 216 ? 0.6850 0.8282 0.5977 -0.0888 -0.0523 -0.0515 290 PHE A CG  
1582 C CD1 . PHE A 216 ? 0.6353 0.8084 0.5946 -0.0749 -0.0452 -0.0335 290 PHE A CD1 
1583 C CD2 . PHE A 216 ? 0.6646 0.8120 0.5697 -0.1138 -0.0772 -0.0577 290 PHE A CD2 
1584 C CE1 . PHE A 216 ? 0.6028 0.8146 0.6143 -0.0834 -0.0594 -0.0212 290 PHE A CE1 
1585 C CE2 . PHE A 216 ? 0.6265 0.8142 0.5822 -0.1240 -0.0992 -0.0437 290 PHE A CE2 
1586 C CZ  . PHE A 216 ? 0.5914 0.8139 0.6074 -0.1074 -0.0887 -0.0250 290 PHE A CZ  
1587 N N   . SER A 217 ? 0.6149 0.7268 0.4892 -0.0316 -0.0083 -0.0493 291 SER A N   
1588 C CA  . SER A 217 ? 0.6031 0.7278 0.4948 -0.0134 -0.0016 -0.0369 291 SER A CA  
1589 C C   . SER A 217 ? 0.5855 0.7134 0.4622 -0.0075 -0.0048 -0.0315 291 SER A C   
1590 O O   . SER A 217 ? 0.5856 0.7301 0.4820 0.0030  -0.0067 -0.0176 291 SER A O   
1591 C CB  . SER A 217 ? 0.5991 0.7037 0.4908 -0.0024 0.0118  -0.0420 291 SER A CB  
1592 O OG  . SER A 217 ? 0.6269 0.7226 0.5267 -0.0080 0.0139  -0.0414 291 SER A OG  
1593 N N   . LEU A 218 ? 0.6181 0.7263 0.4606 -0.0145 -0.0017 -0.0423 292 LEU A N   
1594 C CA  . LEU A 218 ? 0.6266 0.7314 0.4466 -0.0125 -0.0024 -0.0346 292 LEU A CA  
1595 C C   . LEU A 218 ? 0.6379 0.7583 0.4500 -0.0208 -0.0277 -0.0176 292 LEU A C   
1596 O O   . LEU A 218 ? 0.6639 0.7919 0.4832 -0.0116 -0.0346 0.0003  292 LEU A O   
1597 C CB  . LEU A 218 ? 0.6556 0.7322 0.4376 -0.0213 0.0139  -0.0513 292 LEU A CB  
1598 C CG  . LEU A 218 ? 0.6631 0.7288 0.4184 -0.0207 0.0215  -0.0432 292 LEU A CG  
1599 C CD1 . LEU A 218 ? 0.5759 0.6509 0.3682 -0.0020 0.0281  -0.0339 292 LEU A CD1 
1600 C CD2 . LEU A 218 ? 0.7122 0.7496 0.4355 -0.0312 0.0473  -0.0631 292 LEU A CD2 
1601 N N   . GLY A 219 ? 0.5983 0.7223 0.3999 -0.0386 -0.0449 -0.0221 293 GLY A N   
1602 C CA  . GLY A 219 ? 0.6033 0.7456 0.4044 -0.0482 -0.0779 -0.0045 293 GLY A CA  
1603 C C   . GLY A 219 ? 0.6139 0.7932 0.4839 -0.0316 -0.0869 0.0164  293 GLY A C   
1604 O O   . GLY A 219 ? 0.6778 0.8702 0.5597 -0.0266 -0.1082 0.0381  293 GLY A O   
1605 N N   . LEU A 220 ? 0.5888 0.7821 0.5047 -0.0231 -0.0692 0.0109  294 LEU A N   
1606 C CA  . LEU A 220 ? 0.5446 0.7677 0.5250 -0.0067 -0.0653 0.0261  294 LEU A CA  
1607 C C   . LEU A 220 ? 0.5492 0.7612 0.5287 0.0141  -0.0498 0.0327  294 LEU A C   
1608 O O   . LEU A 220 ? 0.5757 0.8059 0.5989 0.0276  -0.0545 0.0493  294 LEU A O   
1609 C CB  . LEU A 220 ? 0.5211 0.7518 0.5339 -0.0067 -0.0439 0.0173  294 LEU A CB  
1610 C CG  . LEU A 220 ? 0.5169 0.7674 0.5564 -0.0269 -0.0594 0.0160  294 LEU A CG  
1611 C CD1 . LEU A 220 ? 0.5912 0.8418 0.6561 -0.0285 -0.0330 0.0101  294 LEU A CD1 
1612 C CD2 . LEU A 220 ? 0.4935 0.7847 0.5907 -0.0279 -0.0867 0.0348  294 LEU A CD2 
1613 N N   . THR A 221 ? 0.5484 0.7303 0.4861 0.0167  -0.0316 0.0195  295 THR A N   
1614 C CA  . THR A 221 ? 0.5403 0.7079 0.4746 0.0319  -0.0189 0.0238  295 THR A CA  
1615 C C   . THR A 221 ? 0.6262 0.7919 0.5503 0.0324  -0.0379 0.0435  295 THR A C   
1616 O O   . THR A 221 ? 0.5932 0.7621 0.5478 0.0478  -0.0367 0.0580  295 THR A O   
1617 C CB  . THR A 221 ? 0.5736 0.7134 0.4719 0.0299  -0.0017 0.0065  295 THR A CB  
1618 O OG1 . THR A 221 ? 0.5647 0.7020 0.4732 0.0321  0.0108  -0.0063 295 THR A OG1 
1619 C CG2 . THR A 221 ? 0.6078 0.7321 0.5037 0.0407  0.0090  0.0105  295 THR A CG2 
1620 N N   . ILE A 222 ? 0.5861 0.7409 0.4623 0.0147  -0.0550 0.0443  296 ILE A N   
1621 C CA  . ILE A 222 ? 0.6454 0.7896 0.4927 0.0107  -0.0771 0.0661  296 ILE A CA  
1622 C C   . ILE A 222 ? 0.6665 0.8424 0.5650 0.0159  -0.1102 0.0904  296 ILE A C   
1623 O O   . ILE A 222 ? 0.7028 0.8765 0.6144 0.0261  -0.1263 0.1157  296 ILE A O   
1624 C CB  . ILE A 222 ? 0.7033 0.8205 0.4717 -0.0140 -0.0834 0.0568  296 ILE A CB  
1625 C CG1 . ILE A 222 ? 0.6970 0.7858 0.4334 -0.0157 -0.0462 0.0344  296 ILE A CG1 
1626 C CG2 . ILE A 222 ? 0.7533 0.8547 0.4757 -0.0235 -0.1130 0.0827  296 ILE A CG2 
1627 C CD1 . ILE A 222 ? 0.7455 0.8224 0.4953 -0.0007 -0.0272 0.0427  296 ILE A CD1 
1628 N N   . LEU A 223 ? 0.6374 0.8431 0.5728 0.0088  -0.1218 0.0845  297 LEU A N   
1629 C CA  . LEU A 223 ? 0.6115 0.8555 0.6161 0.0138  -0.1525 0.1067  297 LEU A CA  
1630 C C   . LEU A 223 ? 0.6064 0.8662 0.6869 0.0421  -0.1332 0.1174  297 LEU A C   
1631 O O   . LEU A 223 ? 0.6616 0.9423 0.7989 0.0537  -0.1572 0.1427  297 LEU A O   
1632 C CB  . LEU A 223 ? 0.6329 0.9063 0.6716 -0.0013 -0.1610 0.0951  297 LEU A CB  
1633 C CG  . LEU A 223 ? 0.5807 0.8986 0.6934 -0.0046 -0.2010 0.1160  297 LEU A CG  
1634 C CD1 . LEU A 223 ? 0.6713 0.9777 0.7361 -0.0180 -0.2522 0.1376  297 LEU A CD1 
1635 C CD2 . LEU A 223 ? 0.5758 0.9163 0.7156 -0.0242 -0.2022 0.0998  297 LEU A CD2 
1636 N N   . GLU A 224 ? 0.6040 0.8504 0.6852 0.0530  -0.0913 0.0983  298 GLU A N   
1637 C CA  . GLU A 224 ? 0.5978 0.8512 0.7409 0.0770  -0.0666 0.1018  298 GLU A CA  
1638 C C   . GLU A 224 ? 0.6252 0.8510 0.7560 0.0912  -0.0669 0.1164  298 GLU A C   
1639 O O   . GLU A 224 ? 0.5998 0.8355 0.7944 0.1105  -0.0680 0.1330  298 GLU A O   
1640 C CB  . GLU A 224 ? 0.6118 0.8531 0.7445 0.0790  -0.0259 0.0756  298 GLU A CB  
1641 C CG  . GLU A 224 ? 0.6189 0.8502 0.7864 0.0998  0.0059  0.0716  298 GLU A CG  
1642 C CD  . GLU A 224 ? 0.6950 0.9049 0.8292 0.0970  0.0393  0.0466  298 GLU A CD  
1643 O OE1 . GLU A 224 ? 0.6516 0.8584 0.7474 0.0815  0.0365  0.0358  298 GLU A OE1 
1644 O OE2 . GLU A 224 ? 0.7982 0.9901 0.9418 0.1095  0.0668  0.0379  298 GLU A OE2 
1645 N N   . VAL A 225 ? 0.6382 0.8282 0.6944 0.0819  -0.0631 0.1105  299 VAL A N   
1646 C CA  . VAL A 225 ? 0.6383 0.7976 0.6829 0.0927  -0.0581 0.1237  299 VAL A CA  
1647 C C   . VAL A 225 ? 0.7146 0.8704 0.7517 0.0909  -0.0972 0.1579  299 VAL A C   
1648 O O   . VAL A 225 ? 0.7236 0.8643 0.7872 0.1068  -0.1006 0.1794  299 VAL A O   
1649 C CB  . VAL A 225 ? 0.6562 0.7805 0.6352 0.0823  -0.0355 0.1049  299 VAL A CB  
1650 C CG1 . VAL A 225 ? 0.6282 0.7572 0.6114 0.0818  -0.0090 0.0751  299 VAL A CG1 
1651 C CG2 . VAL A 225 ? 0.7282 0.8392 0.6370 0.0599  -0.0512 0.1068  299 VAL A CG2 
1652 N N   . ALA A 226 ? 0.7279 0.8929 0.7262 0.0708  -0.1293 0.1643  300 ALA A N   
1653 C CA  . ALA A 226 ? 0.7363 0.8932 0.7120 0.0646  -0.1743 0.1987  300 ALA A CA  
1654 C C   . ALA A 226 ? 0.7590 0.9579 0.8282 0.0785  -0.2100 0.2237  300 ALA A C   
1655 O O   . ALA A 226 ? 0.8289 1.0213 0.8974 0.0798  -0.2526 0.2592  300 ALA A O   
1656 C CB  . ALA A 226 ? 0.7553 0.8973 0.6386 0.0332  -0.1953 0.1926  300 ALA A CB  
1657 N N   . CYS A 227 ? 0.7040 0.9450 0.8554 0.0880  -0.1944 0.2080  301 CYS A N   
1658 C CA  . CYS A 227 ? 0.6809 0.9686 0.9416 0.1019  -0.2213 0.2290  301 CYS A CA  
1659 C C   . CYS A 227 ? 0.6686 0.9705 1.0271 0.1320  -0.1810 0.2233  301 CYS A C   
1660 O O   . CYS A 227 ? 0.6544 0.9949 1.1210 0.1484  -0.1959 0.2412  301 CYS A O   
1661 C CB  . CYS A 227 ? 0.7581 1.0883 1.0442 0.0824  -0.2393 0.2173  301 CYS A CB  
1662 S SG  . CYS A 227 ? 0.9405 1.2535 1.1187 0.0445  -0.2925 0.2225  301 CYS A SG  
1663 N N   . ASN A 228 ? 0.9244 0.7978 0.8488 0.2401  -0.0105 0.1562  302 ASN A N   
1664 C CA  . ASN A 228 ? 1.0085 0.8371 0.9255 0.2696  0.0394  0.1504  302 ASN A CA  
1665 C C   . ASN A 228 ? 1.0066 0.8986 0.9945 0.2821  0.0627  0.1587  302 ASN A C   
1666 O O   . ASN A 228 ? 1.0163 0.9006 1.0347 0.3215  0.1038  0.1709  302 ASN A O   
1667 C CB  . ASN A 228 ? 0.9869 0.7726 0.9044 0.3115  0.0552  0.1704  302 ASN A CB  
1668 C CG  . ASN A 228 ? 1.1120 0.8031 0.9702 0.3304  0.1069  0.1515  302 ASN A CG  
1669 O OD1 . ASN A 228 ? 1.1895 0.8310 0.9801 0.3011  0.1194  0.1216  302 ASN A OD1 
1670 N ND2 . ASN A 228 ? 1.1363 0.7972 1.0164 0.3777  0.1376  0.1709  302 ASN A ND2 
1671 N N   . MET A 229 ? 0.9945 0.9467 1.0090 0.2496  0.0398  0.1534  303 MET A N   
1672 C CA  . MET A 229 ? 0.9842 1.0047 1.0679 0.2541  0.0557  0.1635  303 MET A CA  
1673 C C   . MET A 229 ? 1.0071 0.9987 1.0456 0.2264  0.0767  0.1325  303 MET A C   
1674 O O   . MET A 229 ? 1.0167 0.9727 0.9970 0.1915  0.0585  0.1103  303 MET A O   
1675 C CB  . MET A 229 ? 1.0738 1.1873 1.2258 0.2336  0.0094  0.1864  303 MET A CB  
1676 C CG  . MET A 229 ? 0.9792 1.0859 1.0856 0.1844  -0.0275 0.1632  303 MET A CG  
1677 S SD  . MET A 229 ? 1.2433 1.4431 1.4145 0.1532  -0.0768 0.1856  303 MET A SD  
1678 C CE  . MET A 229 ? 1.1346 1.4031 1.3886 0.1655  -0.0462 0.2005  303 MET A CE  
1679 N N   . GLU A 230 ? 0.9475 0.9569 1.0159 0.2420  0.1164  0.1350  304 GLU A N   
1680 C CA  . GLU A 230 ? 0.9649 0.9495 0.9907 0.2140  0.1366  0.1101  304 GLU A CA  
1681 C C   . GLU A 230 ? 0.8343 0.9011 0.9168 0.1840  0.1104  0.1157  304 GLU A C   
1682 O O   . GLU A 230 ? 0.8072 0.9553 0.9743 0.1960  0.1008  0.1424  304 GLU A O   
1683 C CB  . GLU A 230 ? 1.0108 0.9582 1.0214 0.2423  0.1978  0.1066  304 GLU A CB  
1684 C CG  . GLU A 230 ? 1.2124 1.0466 1.1317 0.2572  0.2262  0.0899  304 GLU A CG  
1685 C CD  . GLU A 230 ? 1.4184 1.2059 1.3220 0.2945  0.2932  0.0887  304 GLU A CD  
1686 O OE1 . GLU A 230 ? 1.4471 1.2832 1.3938 0.2994  0.3213  0.0946  304 GLU A OE1 
1687 O OE2 . GLU A 230 ? 1.4379 1.1358 1.2837 0.3192  0.3204  0.0822  304 GLU A OE2 
1688 N N   . LEU A 231 ? 0.7947 0.8402 0.8336 0.1435  0.0974  0.0947  305 LEU A N   
1689 C CA  . LEU A 231 ? 0.7037 0.8146 0.7893 0.1129  0.0696  0.0986  305 LEU A CA  
1690 C C   . LEU A 231 ? 0.6917 0.8424 0.8137 0.1115  0.0989  0.1037  305 LEU A C   
1691 O O   . LEU A 231 ? 0.7364 0.8400 0.8127 0.1160  0.1383  0.0920  305 LEU A O   
1692 C CB  . LEU A 231 ? 0.7390 0.8138 0.7742 0.0735  0.0467  0.0794  305 LEU A CB  
1693 C CG  . LEU A 231 ? 0.7090 0.7491 0.7094 0.0723  0.0198  0.0755  305 LEU A CG  
1694 C CD1 . LEU A 231 ? 0.6662 0.6781 0.6305 0.0374  0.0048  0.0619  305 LEU A CD1 
1695 C CD2 . LEU A 231 ? 0.7366 0.8298 0.7864 0.0798  -0.0110 0.0927  305 LEU A CD2 
1696 N N   . PRO A 232 ? 0.6338 0.8670 0.8314 0.1019  0.0800  0.1221  306 PRO A N   
1697 C CA  . PRO A 232 ? 0.6161 0.8953 0.8548 0.0996  0.1075  0.1310  306 PRO A CA  
1698 C C   . PRO A 232 ? 0.6418 0.9003 0.8420 0.0579  0.1052  0.1122  306 PRO A C   
1699 O O   . PRO A 232 ? 0.5764 0.8300 0.7657 0.0261  0.0694  0.1038  306 PRO A O   
1700 C CB  . PRO A 232 ? 0.5502 0.9271 0.8855 0.0981  0.0777  0.1624  306 PRO A CB  
1701 C CG  . PRO A 232 ? 0.5298 0.8972 0.8491 0.0767  0.0255  0.1580  306 PRO A CG  
1702 C CD  . PRO A 232 ? 0.5594 0.8471 0.8076 0.0944  0.0339  0.1402  306 PRO A CD  
1703 N N   . HIS A 233 ? 0.7363 0.9797 0.9145 0.0585  0.1466  0.1077  307 HIS A N   
1704 C CA  . HIS A 233 ? 0.7160 0.9461 0.8623 0.0168  0.1447  0.0968  307 HIS A CA  
1705 C C   . HIS A 233 ? 0.6333 0.9434 0.8534 -0.0076 0.1194  0.1123  307 HIS A C   
1706 O O   . HIS A 233 ? 0.6411 0.9458 0.8488 -0.0453 0.1013  0.1067  307 HIS A O   
1707 C CB  . HIS A 233 ? 0.7542 0.9425 0.8465 0.0195  0.1957  0.0891  307 HIS A CB  
1708 C CG  . HIS A 233 ? 0.9297 1.0162 0.9176 0.0129  0.2085  0.0682  307 HIS A CG  
1709 N ND1 . HIS A 233 ? 1.0106 1.0360 0.9516 0.0480  0.2434  0.0604  307 HIS A ND1 
1710 C CD2 . HIS A 233 ? 0.9433 0.9783 0.8665 -0.0273 0.1896  0.0577  307 HIS A CD2 
1711 C CE1 . HIS A 233 ? 1.0344 0.9710 0.8789 0.0261  0.2429  0.0434  307 HIS A CE1 
1712 N NE2 . HIS A 233 ? 1.0184 0.9642 0.8541 -0.0203 0.2093  0.0439  307 HIS A NE2 
1713 N N   . GLY A 234 ? 0.5894 0.9740 0.8892 0.0116  0.1168  0.1357  308 GLY A N   
1714 C CA  . GLY A 234 ? 0.5145 0.9739 0.8828 -0.0150 0.0917  0.1534  308 GLY A CA  
1715 C C   . GLY A 234 ? 0.5064 1.0492 0.9642 0.0091  0.0890  0.1866  308 GLY A C   
1716 O O   . GLY A 234 ? 0.5522 1.0953 1.0234 0.0481  0.1041  0.1971  308 GLY A O   
1717 N N   . GLY A 235 ? 0.4428 1.0584 0.9665 -0.0164 0.0673  0.2078  309 GLY A N   
1718 C CA  . GLY A 235 ? 0.4635 1.1721 1.0839 0.0000  0.0621  0.2488  309 GLY A CA  
1719 C C   . GLY A 235 ? 0.4885 1.2180 1.1354 -0.0047 0.0100  0.2636  309 GLY A C   
1720 O O   . GLY A 235 ? 0.4873 1.1704 1.0848 -0.0336 -0.0297 0.2419  309 GLY A O   
1721 N N   . GLU A 236 ? 0.4563 1.2557 1.1818 0.0247  0.0131  0.3041  310 GLU A N   
1722 C CA  . GLU A 236 ? 0.4959 1.3377 1.2622 0.0109  -0.0433 0.3318  310 GLU A CA  
1723 C C   . GLU A 236 ? 0.4808 1.2424 1.1682 0.0134  -0.0655 0.3040  310 GLU A C   
1724 O O   . GLU A 236 ? 0.4692 1.2107 1.1240 -0.0247 -0.1166 0.2951  310 GLU A O   
1725 C CB  . GLU A 236 ? 0.5830 1.5211 1.4593 0.0465  -0.0308 0.3893  310 GLU A CB  
1726 C CG  . GLU A 236 ? 0.7142 1.6272 1.5926 0.1115  0.0331  0.3915  310 GLU A CG  
1727 C CD  . GLU A 236 ? 0.7077 1.6154 1.5867 0.1367  0.1053  0.3830  310 GLU A CD  
1728 O OE1 . GLU A 236 ? 0.5919 1.4986 1.4493 0.1022  0.1062  0.3656  310 GLU A OE1 
1729 O OE2 . GLU A 236 ? 0.7244 1.6235 1.6213 0.1909  0.1633  0.3943  310 GLU A OE2 
1730 N N   . GLY A 237 ? 0.4880 1.1971 1.1383 0.0567  -0.0256 0.2899  311 GLY A N   
1731 C CA  . GLY A 237 ? 0.4927 1.1293 1.0715 0.0602  -0.0447 0.2673  311 GLY A CA  
1732 C C   . GLY A 237 ? 0.5334 1.0938 1.0235 0.0230  -0.0623 0.2233  311 GLY A C   
1733 O O   . GLY A 237 ? 0.6019 1.1248 1.0469 0.0054  -0.0978 0.2116  311 GLY A O   
1734 N N   . TRP A 238 ? 0.5541 1.0912 1.0196 0.0106  -0.0358 0.2017  312 TRP A N   
1735 C CA  . TRP A 238 ? 0.5380 1.0122 0.9363 -0.0235 -0.0499 0.1683  312 TRP A CA  
1736 C C   . TRP A 238 ? 0.5552 1.0439 0.9611 -0.0635 -0.1000 0.1712  312 TRP A C   
1737 O O   . TRP A 238 ? 0.5738 1.0018 0.9199 -0.0807 -0.1185 0.1484  312 TRP A O   
1738 C CB  . TRP A 238 ? 0.5174 0.9853 0.9083 -0.0355 -0.0194 0.1576  312 TRP A CB  
1739 C CG  . TRP A 238 ? 0.4930 0.8959 0.8222 -0.0635 -0.0254 0.1300  312 TRP A CG  
1740 C CD1 . TRP A 238 ? 0.5307 0.8646 0.7941 -0.0571 -0.0051 0.1098  312 TRP A CD1 
1741 C CD2 . TRP A 238 ? 0.4607 0.8623 0.7939 -0.1022 -0.0527 0.1248  312 TRP A CD2 
1742 N NE1 . TRP A 238 ? 0.5294 0.8288 0.7658 -0.0878 -0.0181 0.0971  312 TRP A NE1 
1743 C CE2 . TRP A 238 ? 0.4682 0.8042 0.7459 -0.1131 -0.0443 0.1043  312 TRP A CE2 
1744 C CE3 . TRP A 238 ? 0.4806 0.9269 0.8588 -0.1300 -0.0834 0.1379  312 TRP A CE3 
1745 C CZ2 . TRP A 238 ? 0.4604 0.7752 0.7332 -0.1445 -0.0602 0.0975  312 TRP A CZ2 
1746 C CZ3 . TRP A 238 ? 0.5220 0.9365 0.8831 -0.1640 -0.0999 0.1258  312 TRP A CZ3 
1747 C CH2 . TRP A 238 ? 0.4767 0.8263 0.7887 -0.1679 -0.0857 0.1061  312 TRP A CH2 
1748 N N   . GLN A 239 ? 0.5484 1.1133 1.0242 -0.0801 -0.1207 0.2004  313 GLN A N   
1749 C CA  . GLN A 239 ? 0.5234 1.0941 0.9975 -0.1246 -0.1704 0.2040  313 GLN A CA  
1750 C C   . GLN A 239 ? 0.6099 1.1647 1.0569 -0.1274 -0.2064 0.2101  313 GLN A C   
1751 O O   . GLN A 239 ? 0.6364 1.1436 1.0294 -0.1625 -0.2385 0.1935  313 GLN A O   
1752 C CB  . GLN A 239 ? 0.4437 1.1040 1.0014 -0.1455 -0.1869 0.2397  313 GLN A CB  
1753 C CG  . GLN A 239 ? 0.4326 1.1171 1.0205 -0.1454 -0.1519 0.2388  313 GLN A CG  
1754 C CD  . GLN A 239 ? 0.5372 1.1610 1.0744 -0.1795 -0.1564 0.2079  313 GLN A CD  
1755 O OE1 . GLN A 239 ? 0.6032 1.1802 1.0987 -0.2098 -0.1894 0.1931  313 GLN A OE1 
1756 N NE2 . GLN A 239 ? 0.4895 1.1098 1.0277 -0.1752 -0.1210 0.2001  313 GLN A NE2 
1757 N N   . GLN A 240 ? 0.6085 1.1973 1.0884 -0.0913 -0.1993 0.2344  314 GLN A N   
1758 C CA  . GLN A 240 ? 0.6495 1.2319 1.1095 -0.0959 -0.2372 0.2478  314 GLN A CA  
1759 C C   . GLN A 240 ? 0.7118 1.1942 1.0685 -0.1018 -0.2384 0.2068  314 GLN A C   
1760 O O   . GLN A 240 ? 0.7761 1.2268 1.0831 -0.1344 -0.2771 0.2017  314 GLN A O   
1761 C CB  . GLN A 240 ? 0.6815 1.3143 1.2016 -0.0488 -0.2213 0.2833  314 GLN A CB  
1762 C CG  . GLN A 240 ? 0.6229 1.3526 1.2520 -0.0280 -0.2006 0.3252  314 GLN A CG  
1763 C CD  . GLN A 240 ? 0.7166 1.5377 1.4224 -0.0592 -0.2522 0.3771  314 GLN A CD  
1764 O OE1 . GLN A 240 ? 0.8694 1.6682 1.5300 -0.1065 -0.3051 0.3741  314 GLN A OE1 
1765 N NE2 . GLN A 240 ? 0.7303 1.6286 1.5291 -0.0340 -0.2288 0.4186  314 GLN A NE2 
1766 N N   . LEU A 241 ? 0.6584 1.0880 0.9780 -0.0729 -0.1956 0.1793  315 LEU A N   
1767 C CA  . LEU A 241 ? 0.6967 1.0388 0.9288 -0.0744 -0.1911 0.1461  315 LEU A CA  
1768 C C   . LEU A 241 ? 0.7114 1.0029 0.8948 -0.1128 -0.2005 0.1189  315 LEU A C   
1769 O O   . LEU A 241 ? 0.6967 0.9173 0.8128 -0.1142 -0.1925 0.0940  315 LEU A O   
1770 C CB  . LEU A 241 ? 0.5756 0.8799 0.7865 -0.0393 -0.1458 0.1303  315 LEU A CB  
1771 C CG  . LEU A 241 ? 0.5663 0.8906 0.8047 0.0041  -0.1263 0.1500  315 LEU A CG  
1772 C CD1 . LEU A 241 ? 0.5875 0.8597 0.7889 0.0280  -0.0821 0.1302  315 LEU A CD1 
1773 C CD2 . LEU A 241 ? 0.6917 1.0034 0.9077 0.0108  -0.1538 0.1613  315 LEU A CD2 
1774 N N   . ARG A 242 ? 0.6855 1.0093 0.9029 -0.1425 -0.2146 0.1252  316 ARG A N   
1775 C CA  . ARG A 242 ? 0.6922 0.9618 0.8684 -0.1749 -0.2166 0.1003  316 ARG A CA  
1776 C C   . ARG A 242 ? 0.7444 1.0207 0.9154 -0.2201 -0.2593 0.1082  316 ARG A C   
1777 O O   . ARG A 242 ? 0.7304 0.9767 0.8884 -0.2490 -0.2608 0.0947  316 ARG A O   
1778 C CB  . ARG A 242 ? 0.6313 0.9124 0.8412 -0.1711 -0.1856 0.0954  316 ARG A CB  
1779 C CG  . ARG A 242 ? 0.6484 0.8965 0.8352 -0.1395 -0.1479 0.0829  316 ARG A CG  
1780 C CD  . ARG A 242 ? 0.5799 0.8541 0.8023 -0.1334 -0.1192 0.0873  316 ARG A CD  
1781 N NE  . ARG A 242 ? 0.5816 0.8091 0.7647 -0.1153 -0.0905 0.0750  316 ARG A NE  
1782 C CZ  . ARG A 242 ? 0.5813 0.8079 0.7548 -0.0861 -0.0708 0.0780  316 ARG A CZ  
1783 N NH1 . ARG A 242 ? 0.5558 0.8288 0.7648 -0.0648 -0.0699 0.0943  316 ARG A NH1 
1784 N NH2 . ARG A 242 ? 0.5477 0.7238 0.6766 -0.0787 -0.0508 0.0676  316 ARG A NH2 
1785 N N   . GLN A 243 ? 0.7757 1.0872 0.9543 -0.2293 -0.2959 0.1324  317 GLN A N   
1786 C CA  . GLN A 243 ? 0.8346 1.1445 0.9921 -0.2806 -0.3446 0.1428  317 GLN A CA  
1787 C C   . GLN A 243 ? 0.9297 1.1618 0.9876 -0.3011 -0.3661 0.1252  317 GLN A C   
1788 O O   . GLN A 243 ? 1.0123 1.2264 1.0299 -0.3501 -0.4091 0.1313  317 GLN A O   
1789 C CB  . GLN A 243 ? 0.8829 1.2995 1.1272 -0.2874 -0.3790 0.1938  317 GLN A CB  
1790 C CG  . GLN A 243 ? 0.7780 1.2795 1.1243 -0.2643 -0.3540 0.2168  317 GLN A CG  
1791 C CD  . GLN A 243 ? 0.7194 1.2112 1.0718 -0.2957 -0.3520 0.2062  317 GLN A CD  
1792 O OE1 . GLN A 243 ? 0.7949 1.2712 1.1542 -0.2824 -0.3166 0.1862  317 GLN A OE1 
1793 N NE2 . GLN A 243 ? 0.8327 1.3173 1.1709 -0.3306 -0.3802 0.2183  317 GLN A NE2 
1794 N N   . GLY A 244 ? 0.9884 1.1730 1.0010 -0.2687 -0.3390 0.1059  318 GLY A N   
1795 C CA  . GLY A 244 ? 1.1127 1.2206 1.0259 -0.2862 -0.3527 0.0884  318 GLY A CA  
1796 C C   . GLY A 244 ? 1.2313 1.3746 1.1440 -0.2824 -0.3855 0.1178  318 GLY A C   
1797 O O   . GLY A 244 ? 1.2930 1.3751 1.1165 -0.3058 -0.4042 0.1072  318 GLY A O   
1798 N N   . TYR A 245 ? 1.3111 1.5482 1.3190 -0.2539 -0.3909 0.1562  319 TYR A N   
1799 C CA  . TYR A 245 ? 1.3150 1.5896 1.3379 -0.2397 -0.4151 0.1894  319 TYR A CA  
1800 C C   . TYR A 245 ? 1.2841 1.5792 1.3547 -0.1770 -0.3714 0.1922  319 TYR A C   
1801 O O   . TYR A 245 ? 1.2752 1.6106 1.4141 -0.1491 -0.3393 0.1950  319 TYR A O   
1802 C CB  . TYR A 245 ? 1.3001 1.6700 1.3991 -0.2645 -0.4657 0.2444  319 TYR A CB  
1803 C CG  . TYR A 245 ? 1.2411 1.7009 1.4548 -0.2496 -0.4532 0.2705  319 TYR A CG  
1804 C CD1 . TYR A 245 ? 1.1855 1.7104 1.4911 -0.1924 -0.4181 0.2942  319 TYR A CD1 
1805 C CD2 . TYR A 245 ? 1.2568 1.7222 1.4780 -0.2895 -0.4656 0.2689  319 TYR A CD2 
1806 C CE1 . TYR A 245 ? 1.1650 1.7698 1.5705 -0.1787 -0.4011 0.3186  319 TYR A CE1 
1807 C CE2 . TYR A 245 ? 1.2322 1.7742 1.5522 -0.2747 -0.4477 0.2924  319 TYR A CE2 
1808 C CZ  . TYR A 245 ? 1.1876 1.8047 1.6014 -0.2213 -0.4178 0.3185  319 TYR A CZ  
1809 O OH  . TYR A 245 ? 1.1183 1.8033 1.6201 -0.2066 -0.3934 0.3398  319 TYR A OH  
1810 N N   . LEU A 246 ? 1.1200 1.3788 1.1449 -0.1583 -0.3690 0.1898  320 LEU A N   
1811 C CA  . LEU A 246 ? 1.1137 1.3848 1.1769 -0.1027 -0.3328 0.1961  320 LEU A CA  
1812 C C   . LEU A 246 ? 1.1242 1.4917 1.2949 -0.0784 -0.3430 0.2475  320 LEU A C   
1813 O O   . LEU A 246 ? 1.0691 1.4921 1.2737 -0.1059 -0.3897 0.2858  320 LEU A O   
1814 C CB  . LEU A 246 ? 1.1460 1.3572 1.1365 -0.0924 -0.3329 0.1866  320 LEU A CB  
1815 C CG  . LEU A 246 ? 1.1252 1.2431 1.0101 -0.1147 -0.3213 0.1430  320 LEU A CG  
1816 C CD1 . LEU A 246 ? 1.1202 1.1902 0.9465 -0.0981 -0.3162 0.1396  320 LEU A CD1 
1817 C CD2 . LEU A 246 ? 0.9939 1.0835 0.8819 -0.1034 -0.2772 0.1111  320 LEU A CD2 
1818 N N   . PRO A 247 ? 1.0886 1.4751 1.3132 -0.0283 -0.2986 0.2519  321 PRO A N   
1819 C CA  . PRO A 247 ? 1.0074 1.4816 1.3396 0.0032  -0.2965 0.3025  321 PRO A CA  
1820 C C   . PRO A 247 ? 1.0137 1.5080 1.3583 0.0113  -0.3292 0.3419  321 PRO A C   
1821 O O   . PRO A 247 ? 1.1141 1.5466 1.3970 0.0262  -0.3222 0.3262  321 PRO A O   
1822 C CB  . PRO A 247 ? 1.0078 1.4607 1.3575 0.0546  -0.2327 0.2857  321 PRO A CB  
1823 C CG  . PRO A 247 ? 1.0825 1.4372 1.3303 0.0524  -0.2150 0.2378  321 PRO A CG  
1824 C CD  . PRO A 247 ? 1.0297 1.3545 1.2163 0.0004  -0.2471 0.2137  321 PRO A CD  
1825 N N   . PRO A 248 ? 1.0189 1.6034 1.4473 -0.0002 -0.3676 0.3988  322 PRO A N   
1826 C CA  . PRO A 248 ? 1.0118 1.6177 1.4453 -0.0075 -0.4130 0.4419  322 PRO A CA  
1827 C C   . PRO A 248 ? 1.1096 1.7069 1.5743 0.0534  -0.3802 0.4597  322 PRO A C   
1828 O O   . PRO A 248 ? 1.1198 1.6843 1.5374 0.0493  -0.4048 0.4679  322 PRO A O   
1829 C CB  . PRO A 248 ? 0.8027 1.4906 1.3174 -0.0336 -0.4381 0.4872  322 PRO A CB  
1830 C CG  . PRO A 248 ? 0.8125 1.5534 1.4114 -0.0064 -0.3975 0.4915  322 PRO A CG  
1831 C CD  . PRO A 248 ? 0.9105 1.5875 1.4391 -0.0077 -0.3723 0.4331  322 PRO A CD  
1832 N N   . GLU A 249 ? 1.2511 1.8701 1.7877 0.1084  -0.3235 0.4655  323 GLU A N   
1833 C CA  . GLU A 249 ? 1.2888 1.8899 1.8541 0.1683  -0.2872 0.4830  323 GLU A CA  
1834 C C   . GLU A 249 ? 1.3714 1.8595 1.8203 0.1744  -0.2677 0.4302  323 GLU A C   
1835 O O   . GLU A 249 ? 1.4207 1.8815 1.8479 0.1879  -0.2804 0.4458  323 GLU A O   
1836 C CB  . GLU A 249 ? 1.3240 1.9528 1.9700 0.2224  -0.2216 0.4910  323 GLU A CB  
1837 C CG  . GLU A 249 ? 1.3805 2.1182 2.1483 0.2232  -0.2264 0.5444  323 GLU A CG  
1838 C CD  . GLU A 249 ? 1.4598 2.2134 2.2915 0.2755  -0.1531 0.5456  323 GLU A CD  
1839 O OE1 . GLU A 249 ? 1.4199 2.0971 2.1868 0.2972  -0.1055 0.4967  323 GLU A OE1 
1840 O OE2 . GLU A 249 ? 1.4743 2.2943 2.3946 0.2847  -0.1375 0.5844  323 GLU A OE2 
1841 N N   . PHE A 250 ? 1.2759 1.7013 1.6530 0.1625  -0.2388 0.3722  324 PHE A N   
1842 C CA  . PHE A 250 ? 1.3274 1.6522 1.6075 0.1719  -0.2131 0.3274  324 PHE A CA  
1843 C C   . PHE A 250 ? 1.3410 1.6210 1.5313 0.1304  -0.2553 0.3107  324 PHE A C   
1844 O O   . PHE A 250 ? 1.3140 1.5295 1.4431 0.1419  -0.2473 0.2970  324 PHE A O   
1845 C CB  . PHE A 250 ? 1.3034 1.5872 1.5503 0.1720  -0.1691 0.2813  324 PHE A CB  
1846 C CG  . PHE A 250 ? 1.3171 1.6440 1.6428 0.2065  -0.1263 0.2963  324 PHE A CG  
1847 C CD1 . PHE A 250 ? 1.2779 1.5672 1.6108 0.2565  -0.0763 0.2983  324 PHE A CD1 
1848 C CD2 . PHE A 250 ? 1.2923 1.6929 1.6812 0.1884  -0.1340 0.3096  324 PHE A CD2 
1849 C CE1 . PHE A 250 ? 1.3142 1.6347 1.7110 0.2898  -0.0293 0.3110  324 PHE A CE1 
1850 C CE2 . PHE A 250 ? 1.2957 1.7381 1.7575 0.2214  -0.0899 0.3258  324 PHE A CE2 
1851 C CZ  . PHE A 250 ? 1.3333 1.7340 1.7969 0.2732  -0.0350 0.3256  324 PHE A CZ  
1852 N N   . THR A 251 ? 1.4089 1.7187 1.5874 0.0814  -0.2991 0.3138  325 THR A N   
1853 C CA  . THR A 251 ? 1.4274 1.6822 1.5058 0.0387  -0.3306 0.2910  325 THR A CA  
1854 C C   . THR A 251 ? 1.3858 1.6393 1.4461 0.0375  -0.3657 0.3240  325 THR A C   
1855 O O   . THR A 251 ? 1.4062 1.5987 1.3721 0.0122  -0.3795 0.3026  325 THR A O   
1856 C CB  . THR A 251 ? 1.4152 1.6910 1.4776 -0.0159 -0.3656 0.2851  325 THR A CB  
1857 O OG1 . THR A 251 ? 1.5108 1.7080 1.4605 -0.0518 -0.3733 0.2462  325 THR A OG1 
1858 C CG2 . THR A 251 ? 1.3643 1.7172 1.4818 -0.0402 -0.4212 0.3405  325 THR A CG2 
1859 N N   . ALA A 252 ? 1.2718 1.5916 1.4224 0.0648  -0.3784 0.3787  326 ALA A N   
1860 C CA  . ALA A 252 ? 1.2931 1.6283 1.4376 0.0531  -0.4248 0.4215  326 ALA A CA  
1861 C C   . ALA A 252 ? 1.3028 1.5588 1.3714 0.0711  -0.4092 0.4023  326 ALA A C   
1862 O O   . ALA A 252 ? 1.3274 1.5579 1.3272 0.0387  -0.4469 0.4091  326 ALA A O   
1863 C CB  . ALA A 252 ? 1.1410 1.5645 1.4130 0.0850  -0.4308 0.4854  326 ALA A CB  
1864 N N   . GLY A 253 ? 1.2687 1.4816 1.3419 0.1182  -0.3547 0.3792  327 GLY A N   
1865 C CA  . GLY A 253 ? 1.2075 1.3463 1.2135 0.1342  -0.3408 0.3652  327 GLY A CA  
1866 C C   . GLY A 253 ? 1.2315 1.3022 1.1213 0.0944  -0.3461 0.3207  327 GLY A C   
1867 O O   . GLY A 253 ? 1.2429 1.2710 1.0705 0.0871  -0.3591 0.3232  327 GLY A O   
1868 N N   . LEU A 254 ? 1.2509 1.3107 1.1135 0.0698  -0.3334 0.2825  328 LEU A N   
1869 C CA  . LEU A 254 ? 1.2241 1.2181 0.9863 0.0380  -0.3274 0.2408  328 LEU A CA  
1870 C C   . LEU A 254 ? 1.2880 1.2704 0.9815 -0.0047 -0.3720 0.2518  328 LEU A C   
1871 O O   . LEU A 254 ? 1.3119 1.3460 1.0355 -0.0242 -0.4163 0.2887  328 LEU A O   
1872 C CB  . LEU A 254 ? 1.1777 1.1718 0.9395 0.0194  -0.3091 0.2069  328 LEU A CB  
1873 C CG  . LEU A 254 ? 1.1814 1.2048 1.0188 0.0521  -0.2746 0.2039  328 LEU A CG  
1874 C CD1 . LEU A 254 ? 1.1491 1.1801 0.9899 0.0282  -0.2645 0.1770  328 LEU A CD1 
1875 C CD2 . LEU A 254 ? 1.1288 1.1002 0.9475 0.0854  -0.2344 0.1892  328 LEU A CD2 
1876 N N   . SER A 255 ? 1.2604 1.1737 0.8589 -0.0218 -0.3596 0.2222  329 SER A N   
1877 C CA  . SER A 255 ? 1.2727 1.1570 0.7827 -0.0665 -0.3926 0.2234  329 SER A CA  
1878 C C   . SER A 255 ? 1.3231 1.1992 0.7962 -0.1101 -0.4022 0.1996  329 SER A C   
1879 O O   . SER A 255 ? 1.3430 1.2264 0.8516 -0.1035 -0.3765 0.1765  329 SER A O   
1880 C CB  . SER A 255 ? 1.3223 1.1338 0.7452 -0.0655 -0.3673 0.2016  329 SER A CB  
1881 O OG  . SER A 255 ? 1.3443 1.1183 0.7537 -0.0561 -0.3197 0.1623  329 SER A OG  
1882 N N   . SER A 256 ? 1.4347 1.1758 0.6474 -0.0143 -0.3672 0.1713  330 SER A N   
1883 C CA  . SER A 256 ? 1.4187 1.1769 0.6151 -0.0323 -0.3781 0.1456  330 SER A CA  
1884 C C   . SER A 256 ? 1.5194 1.2621 0.6877 -0.0472 -0.3302 0.1168  330 SER A C   
1885 O O   . SER A 256 ? 1.4619 1.2424 0.6735 -0.0569 -0.3315 0.0915  330 SER A O   
1886 C CB  . SER A 256 ? 1.4913 1.2114 0.6105 -0.0364 -0.3978 0.1520  330 SER A CB  
1887 O OG  . SER A 256 ? 1.5455 1.1964 0.5599 -0.0405 -0.3587 0.1550  330 SER A OG  
1888 N N   . GLU A 257 ? 1.5833 1.2820 0.7045 -0.0473 -0.2789 0.1204  331 GLU A N   
1889 C CA  . GLU A 257 ? 1.5314 1.2300 0.6525 -0.0566 -0.2236 0.0937  331 GLU A CA  
1890 C C   . GLU A 257 ? 1.4559 1.2227 0.7010 -0.0530 -0.2066 0.0749  331 GLU A C   
1891 O O   . GLU A 257 ? 1.4204 1.2114 0.6887 -0.0602 -0.1936 0.0485  331 GLU A O   
1892 C CB  . GLU A 257 ? 1.6019 1.2519 0.6665 -0.0578 -0.1718 0.1089  331 GLU A CB  
1893 C CG  . GLU A 257 ? 1.7329 1.3133 0.6715 -0.0575 -0.1860 0.1368  331 GLU A CG  
1894 C CD  . GLU A 257 ? 1.7685 1.3329 0.7211 -0.0472 -0.2083 0.1753  331 GLU A CD  
1895 O OE1 . GLU A 257 ? 1.7147 1.3104 0.7669 -0.0407 -0.1969 0.1787  331 GLU A OE1 
1896 O OE2 . GLU A 257 ? 1.8627 1.3850 0.7353 -0.0430 -0.2365 0.1994  331 GLU A OE2 
1897 N N   . LEU A 258 ? 1.3131 1.1057 0.6327 -0.0397 -0.2074 0.0879  332 LEU A N   
1898 C CA  . LEU A 258 ? 1.2339 1.0873 0.6593 -0.0330 -0.1938 0.0695  332 LEU A CA  
1899 C C   . LEU A 258 ? 1.1826 1.0916 0.6565 -0.0326 -0.2280 0.0590  332 LEU A C   
1900 O O   . LEU A 258 ? 1.1529 1.0983 0.6703 -0.0378 -0.2120 0.0373  332 LEU A O   
1901 C CB  . LEU A 258 ? 1.1833 1.0419 0.6651 -0.0151 -0.1934 0.0832  332 LEU A CB  
1902 C CG  . LEU A 258 ? 1.0987 1.0106 0.6748 -0.0051 -0.1775 0.0620  332 LEU A CG  
1903 C CD1 . LEU A 258 ? 1.0176 0.9294 0.5995 -0.0201 -0.1338 0.0407  332 LEU A CD1 
1904 C CD2 . LEU A 258 ? 1.1457 1.0488 0.7637 0.0161  -0.1821 0.0722  332 LEU A CD2 
1905 N N   . ARG A 259 ? 1.1999 1.1182 0.6712 -0.0272 -0.2765 0.0777  333 ARG A N   
1906 C CA  . ARG A 259 ? 1.1596 1.1338 0.6818 -0.0322 -0.3115 0.0736  333 ARG A CA  
1907 C C   . ARG A 259 ? 1.1886 1.1440 0.6648 -0.0560 -0.3092 0.0519  333 ARG A C   
1908 O O   . ARG A 259 ? 1.1265 1.1271 0.6600 -0.0634 -0.3109 0.0392  333 ARG A O   
1909 C CB  . ARG A 259 ? 1.2242 1.2070 0.7440 -0.0263 -0.3682 0.1003  333 ARG A CB  
1910 C CG  . ARG A 259 ? 1.2441 1.2989 0.8406 -0.0321 -0.4064 0.1036  333 ARG A CG  
1911 C CD  . ARG A 259 ? 1.2488 1.3264 0.8710 -0.0210 -0.4500 0.1285  333 ARG A CD  
1912 N NE  . ARG A 259 ? 1.3209 1.4062 0.9710 0.0098  -0.4569 0.1525  333 ARG A NE  
1913 C CZ  . ARG A 259 ? 1.4365 1.4653 1.0242 0.0210  -0.4688 0.1714  333 ARG A CZ  
1914 N NH1 . ARG A 259 ? 1.4122 1.3793 0.9041 0.0042  -0.4734 0.1700  333 ARG A NH1 
1915 N NH2 . ARG A 259 ? 1.4689 1.5019 1.0941 0.0527  -0.4700 0.1906  333 ARG A NH2 
1916 N N   . SER A 260 ? 1.2728 1.1573 0.6417 -0.0660 -0.3024 0.0478  334 SER A N   
1917 C CA  . SER A 260 ? 1.2884 1.1407 0.6002 -0.0832 -0.2977 0.0234  334 SER A CA  
1918 C C   . SER A 260 ? 1.2423 1.1145 0.5980 -0.0825 -0.2471 0.0003  334 SER A C   
1919 O O   . SER A 260 ? 1.2533 1.1366 0.6264 -0.0928 -0.2518 -0.0178 334 SER A O   
1920 C CB  . SER A 260 ? 1.3823 1.1613 0.5820 -0.0836 -0.2852 0.0227  334 SER A CB  
1921 O OG  . SER A 260 ? 1.4236 1.1716 0.5807 -0.0894 -0.2550 -0.0052 334 SER A OG  
1922 N N   . VAL A 261 ? 1.1767 1.0510 0.5521 -0.0717 -0.2016 0.0020  335 VAL A N   
1923 C CA  . VAL A 261 ? 1.1511 1.0458 0.5687 -0.0707 -0.1573 -0.0185 335 VAL A CA  
1924 C C   . VAL A 261 ? 1.0752 1.0393 0.5961 -0.0664 -0.1662 -0.0230 335 VAL A C   
1925 O O   . VAL A 261 ? 1.0134 0.9964 0.5629 -0.0702 -0.1531 -0.0401 335 VAL A O   
1926 C CB  . VAL A 261 ? 1.0973 0.9762 0.5116 -0.0648 -0.1110 -0.0133 335 VAL A CB  
1927 C CG1 . VAL A 261 ? 1.0800 0.9904 0.5527 -0.0634 -0.0720 -0.0325 335 VAL A CG1 
1928 C CG2 . VAL A 261 ? 1.2247 1.0378 0.5314 -0.0690 -0.0934 -0.0064 335 VAL A CG2 
1929 N N   . LEU A 262 ? 1.0338 1.0353 0.6085 -0.0556 -0.1875 -0.0065 336 LEU A N   
1930 C CA  . LEU A 262 ? 0.9772 1.0470 0.6420 -0.0480 -0.1934 -0.0083 336 LEU A CA  
1931 C C   . LEU A 262 ? 0.9864 1.0782 0.6643 -0.0631 -0.2212 -0.0101 336 LEU A C   
1932 O O   . LEU A 262 ? 0.9377 1.0689 0.6676 -0.0643 -0.2108 -0.0179 336 LEU A O   
1933 C CB  . LEU A 262 ? 0.8655 0.9674 0.5772 -0.0286 -0.2108 0.0101  336 LEU A CB  
1934 C CG  . LEU A 262 ? 0.8950 0.9764 0.6113 -0.0132 -0.1848 0.0097  336 LEU A CG  
1935 C CD1 . LEU A 262 ? 0.9116 1.0161 0.6694 0.0109  -0.2049 0.0261  336 LEU A CD1 
1936 C CD2 . LEU A 262 ? 0.8246 0.9259 0.5794 -0.0110 -0.1500 -0.0115 336 LEU A CD2 
1937 N N   . VAL A 263 ? 1.0590 1.1226 0.6886 -0.0764 -0.2597 -0.0014 337 VAL A N   
1938 C CA  . VAL A 263 ? 1.0057 1.0795 0.6453 -0.0969 -0.2918 -0.0035 337 VAL A CA  
1939 C C   . VAL A 263 ? 1.0659 1.1031 0.6724 -0.1071 -0.2667 -0.0286 337 VAL A C   
1940 O O   . VAL A 263 ? 1.0086 1.0726 0.6610 -0.1172 -0.2715 -0.0320 337 VAL A O   
1941 C CB  . VAL A 263 ? 1.0789 1.1199 0.6666 -0.1095 -0.3413 0.0073  337 VAL A CB  
1942 C CG1 . VAL A 263 ? 1.1103 1.1400 0.7048 -0.1291 -0.3608 -0.0031 337 VAL A CG1 
1943 C CG2 . VAL A 263 ? 1.0235 1.1210 0.6766 -0.0966 -0.3688 0.0349  337 VAL A CG2 
1944 N N   . MET A 264 ? 1.1009 1.0787 0.6314 -0.1024 -0.2365 -0.0439 338 MET A N   
1945 C CA  . MET A 264 ? 1.0098 0.9554 0.5136 -0.1047 -0.2072 -0.0679 338 MET A CA  
1946 C C   . MET A 264 ? 0.9913 0.9907 0.5783 -0.0952 -0.1764 -0.0719 338 MET A C   
1947 O O   . MET A 264 ? 1.0219 1.0228 0.6278 -0.1008 -0.1745 -0.0822 338 MET A O   
1948 C CB  . MET A 264 ? 1.0911 0.9763 0.5083 -0.0966 -0.1726 -0.0789 338 MET A CB  
1949 C CG  . MET A 264 ? 1.2135 1.0334 0.5251 -0.1042 -0.2008 -0.0779 338 MET A CG  
1950 S SD  . MET A 264 ? 1.3831 1.1325 0.5834 -0.0923 -0.1504 -0.0893 338 MET A SD  
1951 C CE  . MET A 264 ? 1.2594 1.0035 0.4782 -0.0852 -0.1102 -0.1192 338 MET A CE  
1952 N N   . MET A 265 ? 0.9704 1.0079 0.6029 -0.0805 -0.1548 -0.0640 339 MET A N   
1953 C CA  . MET A 265 ? 0.8679 0.9528 0.5697 -0.0703 -0.1296 -0.0695 339 MET A CA  
1954 C C   . MET A 265 ? 0.8165 0.9577 0.5839 -0.0726 -0.1513 -0.0586 339 MET A C   
1955 O O   . MET A 265 ? 0.7510 0.9177 0.5563 -0.0699 -0.1377 -0.0638 339 MET A O   
1956 C CB  . MET A 265 ? 0.8327 0.9345 0.5593 -0.0557 -0.1078 -0.0663 339 MET A CB  
1957 C CG  . MET A 265 ? 0.9393 0.9912 0.6089 -0.0566 -0.0846 -0.0685 339 MET A CG  
1958 S SD  . MET A 265 ? 0.8411 0.9052 0.5484 -0.0463 -0.0614 -0.0639 339 MET A SD  
1959 C CE  . MET A 265 ? 0.7524 0.8616 0.5272 -0.0405 -0.0404 -0.0816 339 MET A CE  
1960 N N   . LEU A 266 ? 0.8090 0.9732 0.5929 -0.0766 -0.1840 -0.0403 340 LEU A N   
1961 C CA  . LEU A 266 ? 0.7573 0.9869 0.6128 -0.0774 -0.1999 -0.0236 340 LEU A CA  
1962 C C   . LEU A 266 ? 0.8177 1.0400 0.6744 -0.1034 -0.2306 -0.0172 340 LEU A C   
1963 O O   . LEU A 266 ? 0.7949 1.0717 0.7110 -0.1107 -0.2523 0.0045  340 LEU A O   
1964 C CB  . LEU A 266 ? 0.6653 0.9363 0.5557 -0.0635 -0.2157 -0.0044 340 LEU A CB  
1965 C CG  . LEU A 266 ? 0.6801 0.9585 0.5804 -0.0367 -0.1881 -0.0107 340 LEU A CG  
1966 C CD1 . LEU A 266 ? 0.6572 0.9742 0.5954 -0.0172 -0.2033 0.0075  340 LEU A CD1 
1967 C CD2 . LEU A 266 ? 0.5945 0.9026 0.5289 -0.0259 -0.1583 -0.0226 340 LEU A CD2 
1968 N N   . GLU A 267 ? 0.8706 1.0263 0.6654 -0.1172 -0.2322 -0.0352 341 GLU A N   
1969 C CA  . GLU A 267 ? 0.8851 1.0177 0.6750 -0.1434 -0.2634 -0.0338 341 GLU A CA  
1970 C C   . GLU A 267 ? 0.8582 1.0371 0.7174 -0.1464 -0.2524 -0.0233 341 GLU A C   
1971 O O   . GLU A 267 ? 0.8880 1.0652 0.7498 -0.1313 -0.2177 -0.0350 341 GLU A O   
1972 C CB  . GLU A 267 ? 0.9386 0.9799 0.6375 -0.1494 -0.2606 -0.0611 341 GLU A CB  
1973 C CG  . GLU A 267 ? 0.9898 0.9941 0.6845 -0.1703 -0.2800 -0.0678 341 GLU A CG  
1974 C CD  . GLU A 267 ? 1.0822 1.0930 0.7987 -0.2016 -0.3362 -0.0503 341 GLU A CD  
1975 O OE1 . GLU A 267 ? 1.1576 1.1708 0.8626 -0.2000 -0.3552 -0.0430 341 GLU A OE1 
1976 O OE2 . GLU A 267 ? 1.0959 1.1123 0.8553 -0.2219 -0.3524 -0.0411 341 GLU A OE2 
1977 N N   . PRO A 268 ? 0.8134 1.0367 0.7316 -0.1660 -0.2810 0.0017  342 PRO A N   
1978 C CA  . PRO A 268 ? 0.7897 1.0644 0.7746 -0.1672 -0.2655 0.0190  342 PRO A CA  
1979 C C   . PRO A 268 ? 0.8511 1.0702 0.8084 -0.1740 -0.2549 0.0043  342 PRO A C   
1980 O O   . PRO A 268 ? 0.7834 1.0341 0.7754 -0.1628 -0.2292 0.0119  342 PRO A O   
1981 C CB  . PRO A 268 ? 0.7861 1.1112 0.8359 -0.1937 -0.3026 0.0517  342 PRO A CB  
1982 C CG  . PRO A 268 ? 0.7561 1.0827 0.7926 -0.1905 -0.3267 0.0529  342 PRO A CG  
1983 C CD  . PRO A 268 ? 0.8463 1.0866 0.7820 -0.1862 -0.3275 0.0204  342 PRO A CD  
1984 N N   . ASP A 269 ? 0.9133 1.0470 0.8041 -0.1886 -0.2742 -0.0172 343 ASP A N   
1985 C CA  . ASP A 269 ? 0.9173 0.9909 0.7832 -0.1931 -0.2679 -0.0311 343 ASP A CA  
1986 C C   . ASP A 269 ? 0.9172 0.9567 0.7358 -0.1624 -0.2270 -0.0596 343 ASP A C   
1987 O O   . ASP A 269 ? 0.9905 0.9835 0.7432 -0.1545 -0.2224 -0.0817 343 ASP A O   
1988 C CB  . ASP A 269 ? 0.9768 0.9683 0.7919 -0.2222 -0.3109 -0.0428 343 ASP A CB  
1989 C CG  . ASP A 269 ? 1.0107 0.9533 0.8315 -0.2362 -0.3180 -0.0431 343 ASP A CG  
1990 O OD1 . ASP A 269 ? 0.9602 0.9016 0.7881 -0.2136 -0.2826 -0.0482 343 ASP A OD1 
1991 O OD2 . ASP A 269 ? 1.0052 0.9077 0.8249 -0.2706 -0.3629 -0.0371 343 ASP A OD2 
1992 N N   . PRO A 270 ? 0.8817 0.9439 0.7320 -0.1450 -0.1975 -0.0578 344 PRO A N   
1993 C CA  . PRO A 270 ? 0.8912 0.9304 0.7108 -0.1170 -0.1608 -0.0824 344 PRO A CA  
1994 C C   . PRO A 270 ? 0.9529 0.9009 0.7017 -0.1148 -0.1597 -0.1101 344 PRO A C   
1995 O O   . PRO A 270 ? 0.9933 0.9217 0.7074 -0.0934 -0.1293 -0.1306 344 PRO A O   
1996 C CB  . PRO A 270 ? 0.7935 0.8753 0.6668 -0.1033 -0.1421 -0.0700 344 PRO A CB  
1997 C CG  . PRO A 270 ? 0.7743 0.8595 0.6794 -0.1275 -0.1689 -0.0448 344 PRO A CG  
1998 C CD  . PRO A 270 ? 0.8290 0.9356 0.7426 -0.1510 -0.1979 -0.0311 344 PRO A CD  
1999 N N   . LYS A 271 ? 1.0146 0.9048 0.7414 -0.1359 -0.1910 -0.1114 345 LYS A N   
2000 C CA  . LYS A 271 ? 1.0684 0.8605 0.7165 -0.1299 -0.1909 -0.1425 345 LYS A CA  
2001 C C   . LYS A 271 ? 1.0841 0.8369 0.6530 -0.1301 -0.1953 -0.1616 345 LYS A C   
2002 O O   . LYS A 271 ? 1.2033 0.8917 0.6995 -0.1110 -0.1738 -0.1899 345 LYS A O   
2003 C CB  . LYS A 271 ? 1.1486 0.8789 0.7904 -0.1555 -0.2300 -0.1401 345 LYS A CB  
2004 C CG  . LYS A 271 ? 1.1629 0.9242 0.8770 -0.1567 -0.2262 -0.1157 345 LYS A CG  
2005 C CD  . LYS A 271 ? 1.2679 0.9592 0.9765 -0.1868 -0.2673 -0.1102 345 LYS A CD  
2006 C CE  . LYS A 271 ? 1.3627 1.0835 1.1410 -0.1897 -0.2630 -0.0789 345 LYS A CE  
2007 N NZ  . LYS A 271 ? 1.4649 1.1065 1.2389 -0.2214 -0.3032 -0.0717 345 LYS A NZ  
2008 N N   . LEU A 272 ? 1.0992 0.8909 0.6796 -0.1484 -0.2210 -0.1448 346 LEU A N   
2009 C CA  . LEU A 272 ? 1.1239 0.8797 0.6274 -0.1503 -0.2320 -0.1567 346 LEU A CA  
2010 C C   . LEU A 272 ? 1.0997 0.9118 0.6163 -0.1323 -0.2004 -0.1481 346 LEU A C   
2011 O O   . LEU A 272 ? 1.1749 0.9566 0.6241 -0.1300 -0.2023 -0.1547 346 LEU A O   
2012 C CB  . LEU A 272 ? 1.1719 0.9232 0.6753 -0.1845 -0.2921 -0.1426 346 LEU A CB  
2013 C CG  . LEU A 272 ? 1.2023 0.9166 0.7242 -0.2142 -0.3345 -0.1397 346 LEU A CG  
2014 C CD1 . LEU A 272 ? 1.2282 0.9860 0.8036 -0.2419 -0.3792 -0.1114 346 LEU A CD1 
2015 C CD2 . LEU A 272 ? 1.2319 0.8331 0.6612 -0.2086 -0.3380 -0.1744 346 LEU A CD2 
2016 N N   . ARG A 273 ? 1.0929 0.9800 0.6893 -0.1200 -0.1742 -0.1332 347 ARG A N   
2017 C CA  . ARG A 273 ? 1.0659 1.0009 0.6803 -0.1057 -0.1497 -0.1253 347 ARG A CA  
2018 C C   . ARG A 273 ? 1.0293 0.9286 0.5915 -0.0858 -0.1076 -0.1443 347 ARG A C   
2019 O O   . ARG A 273 ? 0.9593 0.8416 0.5223 -0.0718 -0.0803 -0.1589 347 ARG A O   
2020 C CB  . ARG A 273 ? 0.8990 0.9139 0.6040 -0.0971 -0.1358 -0.1091 347 ARG A CB  
2021 C CG  . ARG A 273 ? 0.7874 0.8487 0.5171 -0.0854 -0.1210 -0.1004 347 ARG A CG  
2022 C CD  . ARG A 273 ? 0.7466 0.8773 0.5528 -0.0756 -0.1120 -0.0889 347 ARG A CD  
2023 N NE  . ARG A 273 ? 0.7403 0.9052 0.5873 -0.0882 -0.1386 -0.0697 347 ARG A NE  
2024 C CZ  . ARG A 273 ? 0.7441 0.9492 0.6404 -0.0844 -0.1328 -0.0597 347 ARG A CZ  
2025 N NH1 . ARG A 273 ? 0.6275 0.8421 0.5371 -0.0676 -0.1070 -0.0693 347 ARG A NH1 
2026 N NH2 . ARG A 273 ? 0.7296 0.9680 0.6640 -0.0986 -0.1543 -0.0369 347 ARG A NH2 
2027 N N   . ALA A 274 ? 1.0013 0.8924 0.5225 -0.0837 -0.1013 -0.1407 348 ALA A N   
2028 C CA  . ALA A 274 ? 1.0452 0.9137 0.5254 -0.0672 -0.0566 -0.1509 348 ALA A CA  
2029 C C   . ALA A 274 ? 0.9967 0.9177 0.5527 -0.0523 -0.0192 -0.1507 348 ALA A C   
2030 O O   . ALA A 274 ? 0.9808 0.9607 0.6110 -0.0535 -0.0273 -0.1386 348 ALA A O   
2031 C CB  . ALA A 274 ? 1.0575 0.9216 0.5001 -0.0699 -0.0574 -0.1371 348 ALA A CB  
2032 N N   . THR A 275 ? 1.0031 0.9039 0.5395 -0.0365 0.0211  -0.1645 349 THR A N   
2033 C CA  . THR A 275 ? 0.9187 0.8719 0.5298 -0.0235 0.0542  -0.1632 349 THR A CA  
2034 C C   . THR A 275 ? 0.9317 0.9059 0.5511 -0.0241 0.0806  -0.1517 349 THR A C   
2035 O O   . THR A 275 ? 0.9883 0.9264 0.5415 -0.0294 0.0840  -0.1461 349 THR A O   
2036 C CB  . THR A 275 ? 0.9162 0.8479 0.5210 -0.0039 0.0851  -0.1805 349 THR A CB  
2037 O OG1 . THR A 275 ? 0.9793 0.8590 0.5019 0.0050  0.1146  -0.1902 349 THR A OG1 
2038 C CG2 . THR A 275 ? 0.9749 0.8754 0.5720 -0.0044 0.0567  -0.1903 349 THR A CG2 
2039 N N   . ALA A 276 ? 0.8381 0.8681 0.5384 -0.0200 0.0963  -0.1469 350 ALA A N   
2040 C CA  . ALA A 276 ? 0.7974 0.8466 0.5183 -0.0248 0.1188  -0.1346 350 ALA A CA  
2041 C C   . ALA A 276 ? 0.8855 0.9045 0.5570 -0.0189 0.1632  -0.1343 350 ALA A C   
2042 O O   . ALA A 276 ? 0.9284 0.9335 0.5711 -0.0275 0.1772  -0.1192 350 ALA A O   
2043 C CB  . ALA A 276 ? 0.7282 0.8379 0.5450 -0.0228 0.1233  -0.1335 350 ALA A CB  
2044 N N   . GLU A 277 ? 0.8615 0.8684 0.5206 -0.0019 0.1881  -0.1490 351 GLU A N   
2045 C CA  . GLU A 277 ? 1.0092 0.9852 0.6099 0.0095  0.2355  -0.1502 351 GLU A CA  
2046 C C   . GLU A 277 ? 1.0273 0.9315 0.5070 0.0048  0.2234  -0.1514 351 GLU A C   
2047 O O   . GLU A 277 ? 1.0900 0.9721 0.5138 0.0044  0.2542  -0.1394 351 GLU A O   
2048 C CB  . GLU A 277 ? 1.0676 1.0410 0.6775 0.0353  0.2632  -0.1690 351 GLU A CB  
2049 C CG  . GLU A 277 ? 1.0543 1.0990 0.7724 0.0452  0.2953  -0.1628 351 GLU A CG  
2050 C CD  . GLU A 277 ? 1.2560 1.2933 0.9680 0.0770  0.3393  -0.1768 351 GLU A CD  
2051 O OE1 . GLU A 277 ? 1.2131 1.1802 0.8269 0.0920  0.3441  -0.1948 351 GLU A OE1 
2052 O OE2 . GLU A 277 ? 1.3314 1.4318 1.1371 0.0884  0.3674  -0.1704 351 GLU A OE2 
2053 N N   . ALA A 278 ? 1.0683 0.9357 0.5061 0.0002  0.1774  -0.1637 352 ALA A N   
2054 C CA  . ALA A 278 ? 1.1805 0.9803 0.5059 -0.0069 0.1539  -0.1656 352 ALA A CA  
2055 C C   . ALA A 278 ? 1.1216 0.9302 0.4390 -0.0235 0.1393  -0.1399 352 ALA A C   
2056 O O   . ALA A 278 ? 1.1559 0.9192 0.3829 -0.0240 0.1494  -0.1317 352 ALA A O   
2057 C CB  . ALA A 278 ? 1.0894 0.8590 0.3958 -0.0148 0.1002  -0.1802 352 ALA A CB  
2058 N N   . LEU A 279 ? 1.0625 0.9250 0.4684 -0.0344 0.1161  -0.1268 353 LEU A N   
2059 C CA  . LEU A 279 ? 1.0793 0.9476 0.4863 -0.0461 0.1017  -0.1030 353 LEU A CA  
2060 C C   . LEU A 279 ? 1.0899 0.9550 0.4852 -0.0458 0.1496  -0.0860 353 LEU A C   
2061 O O   . LEU A 279 ? 1.1566 0.9804 0.4758 -0.0500 0.1516  -0.0693 353 LEU A O   
2062 C CB  . LEU A 279 ? 0.9917 0.9169 0.4975 -0.0514 0.0751  -0.0973 353 LEU A CB  
2063 C CG  . LEU A 279 ? 0.9562 0.8927 0.4787 -0.0541 0.0289  -0.1048 353 LEU A CG  
2064 C CD1 . LEU A 279 ? 0.9643 0.9599 0.5788 -0.0537 0.0130  -0.0993 353 LEU A CD1 
2065 C CD2 . LEU A 279 ? 1.0807 0.9766 0.5311 -0.0622 -0.0095 -0.0968 353 LEU A CD2 
2066 N N   . LEU A 280 ? 1.0213 0.9308 0.4931 -0.0419 0.1878  -0.0870 354 LEU A N   
2067 C CA  . LEU A 280 ? 1.0065 0.9230 0.4861 -0.0461 0.2351  -0.0663 354 LEU A CA  
2068 C C   . LEU A 280 ? 1.1261 0.9919 0.4971 -0.0365 0.2739  -0.0629 354 LEU A C   
2069 O O   . LEU A 280 ? 1.2231 1.0850 0.5786 -0.0422 0.3126  -0.0380 354 LEU A O   
2070 C CB  . LEU A 280 ? 0.9660 0.9455 0.5547 -0.0439 0.2657  -0.0696 354 LEU A CB  
2071 C CG  . LEU A 280 ? 0.8825 0.9093 0.5735 -0.0559 0.2357  -0.0672 354 LEU A CG  
2072 C CD1 . LEU A 280 ? 0.7768 0.8637 0.5670 -0.0513 0.2557  -0.0757 354 LEU A CD1 
2073 C CD2 . LEU A 280 ? 0.8498 0.8659 0.5493 -0.0745 0.2346  -0.0411 354 LEU A CD2 
2074 N N   . ALA A 281 ? 1.1775 1.0004 0.4690 -0.0223 0.2644  -0.0866 355 ALA A N   
2075 C CA  . ALA A 281 ? 1.2921 1.0557 0.4602 -0.0086 0.2977  -0.0896 355 ALA A CA  
2076 C C   . ALA A 281 ? 1.3706 1.0742 0.4330 -0.0164 0.2563  -0.0801 355 ALA A C   
2077 O O   . ALA A 281 ? 1.4699 1.1377 0.4566 -0.0041 0.2638  -0.0813 355 ALA A O   
2078 C CB  . ALA A 281 ? 1.3177 1.0671 0.4710 0.0146  0.3016  -0.1226 355 ALA A CB  
2079 N N   . LEU A 282 ? 1.3577 1.0661 0.4428 -0.0337 0.2047  -0.0692 356 LEU A N   
2080 C CA  . LEU A 282 ? 1.4222 1.0786 0.4138 -0.0408 0.1623  -0.0565 356 LEU A CA  
2081 C C   . LEU A 282 ? 1.5302 1.1704 0.4821 -0.0456 0.1915  -0.0200 356 LEU A C   
2082 O O   . LEU A 282 ? 1.4472 1.1255 0.4706 -0.0509 0.2335  -0.0014 356 LEU A O   
2083 C CB  . LEU A 282 ? 1.4230 1.1047 0.4765 -0.0531 0.0975  -0.0544 356 LEU A CB  
2084 C CG  . LEU A 282 ? 1.4005 1.0886 0.4767 -0.0528 0.0599  -0.0836 356 LEU A CG  
2085 C CD1 . LEU A 282 ? 1.2489 0.9757 0.3984 -0.0638 0.0037  -0.0750 356 LEU A CD1 
2086 C CD2 . LEU A 282 ? 1.3732 1.0072 0.3618 -0.0460 0.0411  -0.1003 356 LEU A CD2 
2087 N N   . PRO A 283 ? 1.6476 1.2448 0.5170 -0.0437 0.1633  -0.0069 357 PRO A N   
2088 C CA  . PRO A 283 ? 1.6516 1.2287 0.4791 -0.0486 0.1880  0.0327  357 PRO A CA  
2089 C C   . PRO A 283 ? 1.6341 1.2236 0.5162 -0.0658 0.1774  0.0620  357 PRO A C   
2090 O O   . PRO A 283 ? 1.6396 1.2409 0.5563 -0.0736 0.2203  0.0905  357 PRO A O   
2091 C CB  . PRO A 283 ? 1.7185 1.2492 0.4526 -0.0427 0.1440  0.0354  357 PRO A CB  
2092 C CG  . PRO A 283 ? 1.7277 1.2517 0.4468 -0.0325 0.1218  -0.0057 357 PRO A CG  
2093 C CD  . PRO A 283 ? 1.6055 1.1697 0.4164 -0.0374 0.1135  -0.0272 357 PRO A CD  
2094 N N   . VAL A 284 ? 1.5553 1.1626 0.4903 -0.0694 0.1154  0.0550  358 VAL A N   
2095 C CA  . VAL A 284 ? 1.5579 1.1875 0.5743 -0.0771 0.0940  0.0793  358 VAL A CA  
2096 C C   . VAL A 284 ? 1.5091 1.1932 0.6488 -0.0837 0.1300  0.0762  358 VAL A C   
2097 O O   . VAL A 284 ? 1.5084 1.1965 0.7016 -0.0921 0.1319  0.0996  358 VAL A O   
2098 C CB  . VAL A 284 ? 1.5687 1.2136 0.6182 -0.0740 0.0246  0.0703  358 VAL A CB  
2099 C CG1 . VAL A 284 ? 1.6084 1.2002 0.5423 -0.0710 -0.0190 0.0794  358 VAL A CG1 
2100 C CG2 . VAL A 284 ? 1.3729 1.0661 0.4923 -0.0719 0.0142  0.0339  358 VAL A CG2 
2101 N N   . LEU A 285 ? 1.4260 1.1483 0.6116 -0.0799 0.1547  0.0475  359 LEU A N   
2102 C CA  . LEU A 285 ? 1.3939 1.1716 0.6966 -0.0860 0.1838  0.0428  359 LEU A CA  
2103 C C   . LEU A 285 ? 1.4734 1.2560 0.7686 -0.0889 0.2514  0.0548  359 LEU A C   
2104 O O   . LEU A 285 ? 1.4543 1.2765 0.7984 -0.0830 0.2827  0.0361  359 LEU A O   
2105 C CB  . LEU A 285 ? 1.2735 1.0975 0.6445 -0.0785 0.1642  0.0080  359 LEU A CB  
2106 C CG  . LEU A 285 ? 1.2141 1.0538 0.6265 -0.0769 0.1067  0.0013  359 LEU A CG  
2107 C CD1 . LEU A 285 ? 1.1084 0.9816 0.5561 -0.0695 0.0873  -0.0284 359 LEU A CD1 
2108 C CD2 . LEU A 285 ? 1.1172 0.9817 0.6165 -0.0833 0.1024  0.0122  359 LEU A CD2 
2109 N N   . ARG A 286 ? 1.5399 1.2838 0.7754 -0.0970 0.2751  0.0902  360 ARG A N   
2110 C CA  . ARG A 286 ? 1.5515 1.3038 0.7832 -0.1019 0.3443  0.1117  360 ARG A CA  
2111 C C   . ARG A 286 ? 1.5002 1.2949 0.8572 -0.1241 0.3611  0.1323  360 ARG A C   
2112 O O   . ARG A 286 ? 1.4075 1.2100 0.8338 -0.1337 0.3179  0.1297  360 ARG A O   
2113 C CB  . ARG A 286 ? 1.6941 1.3816 0.7918 -0.1008 0.3642  0.1442  360 ARG A CB  
2114 C CG  . ARG A 286 ? 1.7537 1.3959 0.8219 -0.1111 0.3176  0.1729  360 ARG A CG  
2115 C CD  . ARG A 286 ? 1.8957 1.4681 0.8116 -0.1057 0.3277  0.2021  360 ARG A CD  
2116 N NE  . ARG A 286 ? 1.9480 1.5241 0.8504 -0.1124 0.3979  0.2359  360 ARG A NE  
2117 C CZ  . ARG A 286 ? 2.1094 1.6583 0.9265 -0.1034 0.4073  0.2584  360 ARG A CZ  
2118 N NH1 . ARG A 286 ? 2.1407 1.6438 0.8594 -0.0895 0.3565  0.2522  360 ARG A NH1 
2119 N NH2 . ARG A 286 ? 2.0876 1.6610 0.9234 -0.1100 0.4680  0.2888  360 ARG A NH2 
2120 N N   . GLN A 287 ? 1.5376 1.3593 0.9234 -0.1319 0.4250  0.1528  361 GLN A N   
2121 C CA  . GLN A 287 ? 1.4495 1.3151 0.9615 -0.1579 0.4436  0.1741  361 GLN A CA  
2122 C C   . GLN A 287 ? 1.4648 1.2856 0.9816 -0.1803 0.4137  0.2062  361 GLN A C   
2123 O O   . GLN A 287 ? 1.3406 1.1671 0.9305 -0.1882 0.3664  0.1929  361 GLN A O   
2124 C CB  . GLN A 287 ? 1.4404 1.3407 0.9708 -0.1633 0.5222  0.2007  361 GLN A CB  
2125 C CG  . GLN A 287 ? 1.5458 1.3941 0.9783 -0.1719 0.5612  0.2492  361 GLN A CG  
2126 C CD  . GLN A 287 ? 1.6248 1.5172 1.0620 -0.1646 0.6350  0.2676  361 GLN A CD  
2127 O OE1 . GLN A 287 ? 1.5954 1.5360 1.0567 -0.1397 0.6514  0.2354  361 GLN A OE1 
2128 N NE2 . GLN A 287 ? 1.6601 1.5464 1.0903 -0.1826 0.6625  0.3157  361 GLN A NE2 
2129 N N   . LEU B 3   ? 1.1161 0.8713 1.4223 -0.2737 0.4080  0.1182  77  LEU B N   
2130 C CA  . LEU B 3   ? 1.0736 0.8627 1.4238 -0.2304 0.3501  0.1293  77  LEU B CA  
2131 C C   . LEU B 3   ? 1.0299 0.8702 1.4833 -0.2210 0.3483  0.1035  77  LEU B C   
2132 O O   . LEU B 3   ? 1.1029 0.9182 1.5660 -0.2445 0.3744  0.1055  77  LEU B O   
2133 C CB  . LEU B 3   ? 1.0743 0.7994 1.3501 -0.2195 0.3112  0.1833  77  LEU B CB  
2134 C CG  . LEU B 3   ? 1.0582 0.8127 1.3758 -0.1806 0.2562  0.1946  77  LEU B CG  
2135 C CD1 . LEU B 3   ? 1.0022 0.7968 1.3224 -0.1584 0.2311  0.1808  77  LEU B CD1 
2136 C CD2 . LEU B 3   ? 1.0363 0.7317 1.2976 -0.1727 0.2248  0.2422  77  LEU B CD2 
2137 N N   . GLN B 4   ? 0.9227 0.8281 1.4459 -0.1881 0.3182  0.0789  78  GLN B N   
2138 C CA  . GLN B 4   ? 0.8878 0.8458 1.5062 -0.1778 0.3123  0.0506  78  GLN B CA  
2139 C C   . GLN B 4   ? 0.7966 0.7886 1.4453 -0.1361 0.2611  0.0483  78  GLN B C   
2140 O O   . GLN B 4   ? 0.7258 0.7119 1.3338 -0.1183 0.2399  0.0567  78  GLN B O   
2141 C CB  . GLN B 4   ? 0.8540 0.8718 1.5444 -0.1949 0.3536  -0.0037 78  GLN B CB  
2142 C CG  . GLN B 4   ? 0.8769 0.9283 1.5681 -0.1877 0.3651  -0.0325 78  GLN B CG  
2143 C CD  . GLN B 4   ? 0.8478 0.9636 1.6201 -0.2064 0.4091  -0.0904 78  GLN B CD  
2144 O OE1 . GLN B 4   ? 0.8016 0.9650 1.6555 -0.2083 0.4117  -0.1188 78  GLN B OE1 
2145 N NE2 . GLN B 4   ? 0.9024 1.0232 1.6554 -0.2224 0.4453  -0.1117 78  GLN B NE2 
2146 N N   . PRO B 5   ? 0.7271 0.7483 1.4392 -0.1229 0.2425  0.0366  79  PRO B N   
2147 C CA  . PRO B 5   ? 0.5915 0.6275 1.3150 -0.0880 0.1954  0.0395  79  PRO B CA  
2148 C C   . PRO B 5   ? 0.5834 0.6662 1.3356 -0.0628 0.1825  0.0043  79  PRO B C   
2149 O O   . PRO B 5   ? 0.6089 0.7310 1.3993 -0.0678 0.2072  -0.0309 79  PRO B O   
2150 C CB  . PRO B 5   ? 0.5888 0.6392 1.3694 -0.0879 0.1877  0.0323  79  PRO B CB  
2151 C CG  . PRO B 5   ? 0.6492 0.7282 1.4800 -0.1146 0.2288  0.0015  79  PRO B CG  
2152 C CD  . PRO B 5   ? 0.6934 0.7298 1.4635 -0.1429 0.2655  0.0191  79  PRO B CD  
2153 N N   . ARG B 6   ? 0.5533 0.6287 1.2865 -0.0348 0.1434  0.0123  80  ARG B N   
2154 C CA  . ARG B 6   ? 0.4954 0.5958 1.2386 -0.0048 0.1232  -0.0147 80  ARG B CA  
2155 C C   . ARG B 6   ? 0.4716 0.5675 1.2209 0.0183  0.0842  -0.0131 80  ARG B C   
2156 O O   . ARG B 6   ? 0.5613 0.6193 1.2671 0.0165  0.0682  0.0166  80  ARG B O   
2157 C CB  . ARG B 6   ? 0.5243 0.5936 1.1977 -0.0007 0.1235  -0.0018 80  ARG B CB  
2158 C CG  . ARG B 6   ? 0.5742 0.6481 1.2391 0.0328  0.0993  -0.0227 80  ARG B CG  
2159 C CD  . ARG B 6   ? 0.6351 0.6704 1.2246 0.0315  0.1024  -0.0080 80  ARG B CD  
2160 N NE  . ARG B 6   ? 0.7197 0.7460 1.2917 0.0637  0.0816  -0.0272 80  ARG B NE  
2161 C CZ  . ARG B 6   ? 0.7569 0.7498 1.2914 0.0802  0.0505  -0.0174 80  ARG B CZ  
2162 N NH1 . ARG B 6   ? 0.6740 0.6493 1.1946 0.0678  0.0369  0.0078  80  ARG B NH1 
2163 N NH2 . ARG B 6   ? 0.7416 0.7142 1.2499 0.1094  0.0345  -0.0351 80  ARG B NH2 
2164 N N   . ARG B 7   ? 0.4752 0.6098 1.2773 0.0389  0.0687  -0.0470 81  ARG B N   
2165 C CA  . ARG B 7   ? 0.4720 0.5951 1.2712 0.0574  0.0334  -0.0468 81  ARG B CA  
2166 C C   . ARG B 7   ? 0.5122 0.5900 1.2395 0.0774  0.0089  -0.0338 81  ARG B C   
2167 O O   . ARG B 7   ? 0.5718 0.6432 1.2718 0.0914  0.0099  -0.0422 81  ARG B O   
2168 C CB  . ARG B 7   ? 0.4529 0.6250 1.3162 0.0772  0.0174  -0.0874 81  ARG B CB  
2169 C CG  . ARG B 7   ? 0.5876 0.7462 1.4505 0.0847  -0.0119 -0.0860 81  ARG B CG  
2170 C CD  . ARG B 7   ? 0.6606 0.8415 1.5424 0.1189  -0.0469 -0.1201 81  ARG B CD  
2171 N NE  . ARG B 7   ? 0.7196 0.8876 1.5998 0.1194  -0.0702 -0.1212 81  ARG B NE  
2172 C CZ  . ARG B 7   ? 0.6529 0.8241 1.5242 0.1439  -0.1052 -0.1448 81  ARG B CZ  
2173 N NH1 . ARG B 7   ? 0.6286 0.8143 1.4891 0.1730  -0.1243 -0.1681 81  ARG B NH1 
2174 N NH2 . ARG B 7   ? 0.5779 0.7328 1.4419 0.1379  -0.1214 -0.1447 81  ARG B NH2 
2175 N N   . VAL B 8   ? 0.5819 0.6258 1.2779 0.0763  -0.0099 -0.0158 82  VAL B N   
2176 C CA  . VAL B 8   ? 0.6156 0.6115 1.2409 0.0891  -0.0300 -0.0066 82  VAL B CA  
2177 C C   . VAL B 8   ? 0.6750 0.6596 1.2966 0.1112  -0.0592 -0.0255 82  VAL B C   
2178 O O   . VAL B 8   ? 0.6638 0.6537 1.3102 0.1035  -0.0659 -0.0261 82  VAL B O   
2179 C CB  . VAL B 8   ? 0.5346 0.4988 1.1218 0.0677  -0.0268 0.0242  82  VAL B CB  
2180 C CG1 . VAL B 8   ? 0.5639 0.4801 1.0797 0.0753  -0.0428 0.0272  82  VAL B CG1 
2181 C CG2 . VAL B 8   ? 0.5472 0.5167 1.1281 0.0484  -0.0041 0.0444  82  VAL B CG2 
2182 N N   . SER B 9   ? 0.8164 0.7793 1.4010 0.1392  -0.0769 -0.0408 83  SER B N   
2183 C CA  . SER B 9   ? 0.8438 0.7764 1.3993 0.1625  -0.1088 -0.0547 83  SER B CA  
2184 C C   . SER B 9   ? 0.9613 0.8323 1.4335 0.1842  -0.1219 -0.0548 83  SER B C   
2185 O O   . SER B 9   ? 0.9678 0.8392 1.4288 0.1900  -0.1091 -0.0554 83  SER B O   
2186 C CB  . SER B 9   ? 0.7425 0.7270 1.3653 0.1849  -0.1257 -0.0866 83  SER B CB  
2187 O OG  . SER B 9   ? 0.7633 0.7125 1.3491 0.2055  -0.1604 -0.0971 83  SER B OG  
2188 N N   . PHE B 10  ? 1.0680 0.8785 1.4748 0.1934  -0.1447 -0.0546 84  PHE B N   
2189 C CA  . PHE B 10  ? 1.1463 0.8830 1.4636 0.2180  -0.1611 -0.0580 84  PHE B CA  
2190 C C   . PHE B 10  ? 1.2511 0.9796 1.5631 0.2597  -0.1979 -0.0818 84  PHE B C   
2191 O O   . PHE B 10  ? 1.2976 0.9533 1.5155 0.2724  -0.2160 -0.0808 84  PHE B O   
2192 C CB  . PHE B 10  ? 1.1413 0.8021 1.3697 0.1931  -0.1555 -0.0403 84  PHE B CB  
2193 C CG  . PHE B 10  ? 1.1164 0.7907 1.3485 0.1558  -0.1244 -0.0202 84  PHE B CG  
2194 C CD1 . PHE B 10  ? 1.0097 0.7383 1.3081 0.1287  -0.1096 -0.0093 84  PHE B CD1 
2195 C CD2 . PHE B 10  ? 1.1331 0.7639 1.3008 0.1495  -0.1120 -0.0135 84  PHE B CD2 
2196 C CE1 . PHE B 10  ? 0.9278 0.6690 1.2286 0.1000  -0.0880 0.0088  84  PHE B CE1 
2197 C CE2 . PHE B 10  ? 1.0524 0.7008 1.2242 0.1163  -0.0886 0.0026  84  PHE B CE2 
2198 C CZ  . PHE B 10  ? 0.9506 0.6552 1.1892 0.0937  -0.0792 0.0141  84  PHE B CZ  
2199 N N   . ARG B 11  ? 1.3710 1.1838 1.7737 0.2704  -0.2020 -0.1020 85  ARG B N   
2200 C CA  . ARG B 11  ? 1.3374 1.1740 1.7479 0.3007  -0.2327 -0.1271 85  ARG B CA  
2201 C C   . ARG B 11  ? 1.3640 1.1711 1.7420 0.2984  -0.2593 -0.1284 85  ARG B C   
2202 O O   . ARG B 11  ? 1.4299 1.1976 1.7488 0.3246  -0.2924 -0.1383 85  ARG B O   
2203 C CB  . ARG B 11  ? 1.4079 1.2019 1.7547 0.3351  -0.2472 -0.1339 85  ARG B CB  
2204 C CG  . ARG B 11  ? 1.3894 1.2426 1.8016 0.3460  -0.2275 -0.1488 85  ARG B CG  
2205 C CD  . ARG B 11  ? 1.5475 1.3427 1.8900 0.3725  -0.2301 -0.1484 85  ARG B CD  
2206 N NE  . ARG B 11  ? 1.5341 1.3932 1.9465 0.3910  -0.2190 -0.1728 85  ARG B NE  
2207 C CZ  . ARG B 11  ? 1.5724 1.3982 1.9486 0.4154  -0.2161 -0.1786 85  ARG B CZ  
2208 N NH1 . ARG B 11  ? 1.7126 1.4390 1.9797 0.4218  -0.2216 -0.1603 85  ARG B NH1 
2209 N NH2 . ARG B 11  ? 1.4920 1.3843 1.9424 0.4308  -0.2043 -0.2055 85  ARG B NH2 
2210 N N   . GLY B 12  ? 1.2139 1.0382 1.6318 0.2673  -0.2451 -0.1194 86  GLY B N   
2211 C CA  . GLY B 12  ? 1.1060 0.9097 1.5094 0.2617  -0.2659 -0.1242 86  GLY B CA  
2212 C C   . GLY B 12  ? 0.8386 0.7131 1.3438 0.2351  -0.2488 -0.1293 86  GLY B C   
2213 O O   . GLY B 12  ? 0.8509 0.7277 1.3667 0.2302  -0.2645 -0.1400 86  GLY B O   
2214 N N   . GLN B 19  ? 0.7003 1.0761 1.8401 -0.0115 0.1060  -0.2166 93  GLN B N   
2215 C CA  . GLN B 19  ? 0.7720 1.1078 1.8992 -0.0486 0.1429  -0.1860 93  GLN B CA  
2216 C C   . GLN B 19  ? 0.8378 1.1862 1.9893 -0.0781 0.1673  -0.2100 93  GLN B C   
2217 O O   . GLN B 19  ? 0.9737 1.3734 2.1624 -0.0759 0.1649  -0.2540 93  GLN B O   
2218 C CB  . GLN B 19  ? 0.7058 1.0258 1.8191 -0.0669 0.1812  -0.1668 93  GLN B CB  
2219 C CG  . GLN B 19  ? 0.7292 1.0113 1.7846 -0.0421 0.1577  -0.1326 93  GLN B CG  
2220 C CD  . GLN B 19  ? 0.7252 0.9484 1.7280 -0.0382 0.1342  -0.0897 93  GLN B CD  
2221 O OE1 . GLN B 19  ? 0.6982 0.9140 1.6846 -0.0107 0.0955  -0.0866 93  GLN B OE1 
2222 N NE2 . GLN B 19  ? 0.7220 0.8995 1.6960 -0.0659 0.1584  -0.0578 93  GLN B NE2 
2223 N N   . SER B 20  ? 0.8031 1.1020 1.9310 -0.1041 0.1899  -0.1810 94  SER B N   
2224 C CA  . SER B 20  ? 0.8644 1.1629 2.0056 -0.1298 0.2115  -0.1999 94  SER B CA  
2225 C C   . SER B 20  ? 1.0028 1.3339 2.1681 -0.1560 0.2515  -0.2351 94  SER B C   
2226 O O   . SER B 20  ? 1.0097 1.3317 2.1601 -0.1682 0.2797  -0.2271 94  SER B O   
2227 C CB  . SER B 20  ? 0.8715 1.0994 1.9719 -0.1492 0.2304  -0.1584 94  SER B CB  
2228 O OG  . SER B 20  ? 0.9505 1.1556 2.0385 -0.1282 0.1956  -0.1376 94  SER B OG  
2229 N N   . PRO B 21  ? 1.0664 1.4340 2.2669 -0.1678 0.2573  -0.2759 95  PRO B N   
2230 C CA  . PRO B 21  ? 1.0644 1.4674 2.2925 -0.1940 0.2959  -0.3159 95  PRO B CA  
2231 C C   . PRO B 21  ? 1.1145 1.4625 2.3060 -0.2380 0.3516  -0.3009 95  PRO B C   
2232 O O   . PRO B 21  ? 1.0799 1.4401 2.2762 -0.2627 0.3906  -0.3244 95  PRO B O   
2233 C CB  . PRO B 21  ? 1.0140 1.4747 2.2929 -0.1892 0.2765  -0.3643 95  PRO B CB  
2234 C CG  . PRO B 21  ? 0.9881 1.4148 2.2475 -0.1814 0.2517  -0.3407 95  PRO B CG  
2235 C CD  . PRO B 21  ? 1.0200 1.4038 2.2393 -0.1567 0.2266  -0.2922 95  PRO B CD  
2236 N N   . GLY B 22  ? 1.3379 1.6214 2.4886 -0.2485 0.3571  -0.2642 96  GLY B N   
2237 C CA  . GLY B 22  ? 1.4026 1.6217 2.5055 -0.2875 0.4066  -0.2472 96  GLY B CA  
2238 C C   . GLY B 22  ? 1.4371 1.5967 2.4781 -0.2966 0.4273  -0.2047 96  GLY B C   
2239 O O   . GLY B 22  ? 1.5123 1.6325 2.5132 -0.3309 0.4731  -0.2042 96  GLY B O   
2240 N N   . TYR B 23  ? 1.1506 1.2988 2.1770 -0.2679 0.3945  -0.1693 97  TYR B N   
2241 C CA  . TYR B 23  ? 1.0500 1.1406 2.0135 -0.2745 0.4083  -0.1264 97  TYR B CA  
2242 C C   . TYR B 23  ? 1.0063 1.1193 1.9676 -0.2951 0.4443  -0.1520 97  TYR B C   
2243 O O   . TYR B 23  ? 0.9001 1.0884 1.9193 -0.2797 0.4338  -0.1912 97  TYR B O   
2244 C CB  . TYR B 23  ? 0.9692 1.0621 1.9335 -0.2382 0.3636  -0.0952 97  TYR B CB  
2245 C CG  . TYR B 23  ? 0.8808 0.9452 1.8004 -0.2392 0.3712  -0.0658 97  TYR B CG  
2246 C CD1 . TYR B 23  ? 0.9223 0.8989 1.7603 -0.2486 0.3773  -0.0127 97  TYR B CD1 
2247 C CD2 . TYR B 23  ? 0.8021 0.9246 1.7566 -0.2275 0.3685  -0.0913 97  TYR B CD2 
2248 C CE1 . TYR B 23  ? 0.9198 0.8653 1.7070 -0.2503 0.3817  0.0150  97  TYR B CE1 
2249 C CE2 . TYR B 23  ? 0.8216 0.9159 1.7320 -0.2308 0.3783  -0.0656 97  TYR B CE2 
2250 C CZ  . TYR B 23  ? 0.8785 0.8821 1.6966 -0.2418 0.3825  -0.0119 97  TYR B CZ  
2251 O OH  . TYR B 23  ? 0.8764 0.8451 1.6184 -0.2372 0.3796  0.0131  97  TYR B OH  
2252 N N   . ASP B 24  ? 1.0229 1.0654 1.9109 -0.3283 0.4854  -0.1304 98  ASP B N   
2253 C CA  . ASP B 24  ? 1.0583 1.1056 1.9260 -0.3527 0.5251  -0.1505 98  ASP B CA  
2254 C C   . ASP B 24  ? 1.0896 1.0716 1.8761 -0.3528 0.5256  -0.1005 98  ASP B C   
2255 O O   . ASP B 24  ? 1.1767 1.0709 1.8844 -0.3576 0.5212  -0.0496 98  ASP B O   
2256 C CB  . ASP B 24  ? 1.1243 1.1353 1.9591 -0.3965 0.5767  -0.1709 98  ASP B CB  
2257 C CG  . ASP B 24  ? 1.1761 1.1921 1.9902 -0.4244 0.6215  -0.1984 98  ASP B CG  
2258 O OD1 . ASP B 24  ? 1.1329 1.2347 2.0202 -0.4128 0.6188  -0.2453 98  ASP B OD1 
2259 O OD2 . ASP B 24  ? 1.3176 1.2483 2.0383 -0.4566 0.6578  -0.1741 98  ASP B OD2 
2260 N N   . PRO B 25  ? 1.0576 1.0769 1.8569 -0.3454 0.5283  -0.1135 99  PRO B N   
2261 C CA  . PRO B 25  ? 1.0925 1.0523 1.8135 -0.3431 0.5238  -0.0661 99  PRO B CA  
2262 C C   . PRO B 25  ? 1.3076 1.1834 1.9211 -0.3825 0.5679  -0.0478 99  PRO B C   
2263 O O   . PRO B 25  ? 1.3605 1.2293 1.9357 -0.3939 0.5890  -0.0515 99  PRO B O   
2264 C CB  . PRO B 25  ? 0.9553 0.9949 1.7395 -0.3205 0.5134  -0.0970 99  PRO B CB  
2265 C CG  . PRO B 25  ? 0.8435 0.9813 1.7369 -0.3035 0.5020  -0.1564 99  PRO B CG  
2266 C CD  . PRO B 25  ? 0.9356 1.0547 1.8233 -0.3335 0.5297  -0.1734 99  PRO B CD  
2267 N N   . SER B 26  ? 1.4317 1.2374 1.9889 -0.4030 0.5815  -0.0281 100 SER B N   
2268 C CA  . SER B 26  ? 1.5259 1.2407 1.9705 -0.4395 0.6201  -0.0095 100 SER B CA  
2269 C C   . SER B 26  ? 1.6476 1.2529 1.9882 -0.4336 0.5959  0.0570  100 SER B C   
2270 O O   . SER B 26  ? 1.7363 1.2759 1.9811 -0.4351 0.5895  0.0957  100 SER B O   
2271 C CB  . SER B 26  ? 1.5893 1.3140 2.0531 -0.4748 0.6680  -0.0561 100 SER B CB  
2272 O OG  . SER B 26  ? 1.6422 1.3315 2.1038 -0.4761 0.6611  -0.0433 100 SER B OG  
2273 N N   . ARG B 27  ? 1.6305 1.2133 1.9849 -0.4255 0.5804  0.0695  101 ARG B N   
2274 C CA  . ARG B 27  ? 1.6925 1.1758 1.9579 -0.4127 0.5515  0.1298  101 ARG B CA  
2275 C C   . ARG B 27  ? 1.6838 1.1691 1.9420 -0.3751 0.5009  0.1677  101 ARG B C   
2276 O O   . ARG B 27  ? 1.5598 1.1286 1.9078 -0.3525 0.4809  0.1474  101 ARG B O   
2277 C CB  . ARG B 27  ? 1.5984 1.0714 1.8985 -0.4055 0.5419  0.1295  101 ARG B CB  
2278 C CG  . ARG B 27  ? 1.6380 1.0861 1.9239 -0.4441 0.5915  0.1000  101 ARG B CG  
2279 C CD  . ARG B 27  ? 1.6650 1.1244 2.0054 -0.4363 0.5831  0.0892  101 ARG B CD  
2280 N NE  . ARG B 27  ? 1.7377 1.1031 2.0094 -0.4191 0.5555  0.1413  101 ARG B NE  
2281 C CZ  . ARG B 27  ? 1.7560 1.0369 1.9637 -0.4388 0.5778  0.1532  101 ARG B CZ  
2282 N NH1 . ARG B 27  ? 1.7254 0.9993 1.9231 -0.4798 0.6319  0.1172  101 ARG B NH1 
2283 N NH2 . ARG B 27  ? 1.7146 0.9155 1.8685 -0.4154 0.5452  0.1998  101 ARG B NH2 
2284 N N   . PRO B 28  ? 1.8630 1.2583 2.0154 -0.3663 0.4773  0.2211  102 PRO B N   
2285 C CA  . PRO B 28  ? 1.8052 1.2042 1.9451 -0.3332 0.4319  0.2534  102 PRO B CA  
2286 C C   . PRO B 28  ? 1.7198 1.1606 1.9396 -0.2925 0.3861  0.2610  102 PRO B C   
2287 O O   . PRO B 28  ? 1.7214 1.1883 1.9570 -0.2648 0.3513  0.2767  102 PRO B O   
2288 C CB  . PRO B 28  ? 1.9603 1.2493 1.9642 -0.3335 0.4150  0.3059  102 PRO B CB  
2289 C CG  . PRO B 28  ? 2.0119 1.2369 1.9790 -0.3509 0.4341  0.3105  102 PRO B CG  
2290 C CD  . PRO B 28  ? 1.9615 1.2470 1.9998 -0.3841 0.4879  0.2535  102 PRO B CD  
2291 N N   . GLU B 29  ? 1.6139 1.0626 1.8826 -0.2889 0.3856  0.2486  103 GLU B N   
2292 C CA  . GLU B 29  ? 1.5276 1.0129 1.8652 -0.2511 0.3428  0.2537  103 GLU B CA  
2293 C C   . GLU B 29  ? 1.3139 0.9003 1.7502 -0.2363 0.3312  0.2225  103 GLU B C   
2294 O O   . GLU B 29  ? 1.2254 0.8687 1.7085 -0.2559 0.3617  0.1823  103 GLU B O   
2295 C CB  . GLU B 29  ? 1.4683 0.9454 1.8379 -0.2553 0.3520  0.2390  103 GLU B CB  
2296 C CG  . GLU B 29  ? 1.5788 0.9493 1.8559 -0.2589 0.3505  0.2752  103 GLU B CG  
2297 C CD  . GLU B 29  ? 1.7711 1.0852 1.9766 -0.3023 0.3985  0.2701  103 GLU B CD  
2298 O OE1 . GLU B 29  ? 1.7095 1.0655 1.9278 -0.3283 0.4320  0.2414  103 GLU B OE1 
2299 O OE2 . GLU B 29  ? 1.8731 1.1013 2.0107 -0.3097 0.4033  0.2927  103 GLU B OE2 
2300 N N   . SER B 30  ? 1.1380 0.7467 1.6048 -0.2000 0.2845  0.2393  104 SER B N   
2301 C CA  . SER B 30  ? 1.0220 0.7187 1.5608 -0.1801 0.2620  0.2114  104 SER B CA  
2302 C C   . SER B 30  ? 0.9479 0.7053 1.5823 -0.1870 0.2771  0.1680  104 SER B C   
2303 O O   . SER B 30  ? 1.0326 0.7721 1.6738 -0.1975 0.2922  0.1595  104 SER B O   
2304 C CB  . SER B 30  ? 0.9202 0.6243 1.4578 -0.1421 0.2081  0.2343  104 SER B CB  
2305 O OG  . SER B 30  ? 0.8394 0.5184 1.4033 -0.1310 0.1959  0.2469  104 SER B OG  
2306 N N   . PHE B 31  ? 0.8625 0.6974 1.5496 -0.1731 0.2635  0.1344  105 PHE B N   
2307 C CA  . PHE B 31  ? 0.7531 0.6513 1.5291 -0.1713 0.2640  0.0932  105 PHE B CA  
2308 C C   . PHE B 31  ? 0.7520 0.6368 1.5496 -0.1556 0.2394  0.1041  105 PHE B C   
2309 O O   . PHE B 31  ? 0.7917 0.6996 1.6274 -0.1606 0.2473  0.0760  105 PHE B O   
2310 C CB  . PHE B 31  ? 0.6724 0.6410 1.4829 -0.1476 0.2399  0.0639  105 PHE B CB  
2311 C CG  . PHE B 31  ? 0.6073 0.6374 1.4984 -0.1371 0.2264  0.0253  105 PHE B CG  
2312 C CD1 . PHE B 31  ? 0.6570 0.7382 1.6113 -0.1560 0.2541  -0.0191 105 PHE B CD1 
2313 C CD2 . PHE B 31  ? 0.5359 0.5734 1.4374 -0.1100 0.1861  0.0304  105 PHE B CD2 
2314 C CE1 . PHE B 31  ? 0.6632 0.7969 1.6704 -0.1399 0.2320  -0.0555 105 PHE B CE1 
2315 C CE2 . PHE B 31  ? 0.5005 0.5865 1.4632 -0.1010 0.1715  -0.0040 105 PHE B CE2 
2316 C CZ  . PHE B 31  ? 0.6035 0.7371 1.6159 -0.1138 0.1914  -0.0461 105 PHE B CZ  
2317 N N   . PHE B 32  ? 0.7215 0.5738 1.4854 -0.1332 0.2068  0.1394  106 PHE B N   
2318 C CA  . PHE B 32  ? 0.7193 0.5599 1.4939 -0.1153 0.1844  0.1468  106 PHE B CA  
2319 C C   . PHE B 32  ? 0.8150 0.6059 1.5622 -0.1292 0.2077  0.1545  106 PHE B C   
2320 O O   . PHE B 32  ? 0.8080 0.6095 1.5872 -0.1285 0.2104  0.1360  106 PHE B O   
2321 C CB  . PHE B 32  ? 0.7111 0.5319 1.4550 -0.0902 0.1478  0.1790  106 PHE B CB  
2322 C CG  . PHE B 32  ? 0.6127 0.4292 1.3698 -0.0709 0.1265  0.1827  106 PHE B CG  
2323 C CD1 . PHE B 32  ? 0.5650 0.4222 1.3736 -0.0652 0.1201  0.1530  106 PHE B CD1 
2324 C CD2 . PHE B 32  ? 0.7057 0.4783 1.4228 -0.0579 0.1120  0.2138  106 PHE B CD2 
2325 C CE1 . PHE B 32  ? 0.5721 0.4272 1.3932 -0.0507 0.1059  0.1536  106 PHE B CE1 
2326 C CE2 . PHE B 32  ? 0.7039 0.4799 1.4427 -0.0408 0.0955  0.2123  106 PHE B CE2 
2327 C CZ  . PHE B 32  ? 0.6147 0.4327 1.4062 -0.0392 0.0953  0.1819  106 PHE B CZ  
2328 N N   . GLN B 33  ? 0.8790 0.6086 1.5589 -0.1433 0.2254  0.1817  107 GLN B N   
2329 C CA  . GLN B 33  ? 0.9247 0.5901 1.5624 -0.1567 0.2461  0.1933  107 GLN B CA  
2330 C C   . GLN B 33  ? 0.9101 0.5923 1.5738 -0.1886 0.2874  0.1563  107 GLN B C   
2331 O O   . GLN B 33  ? 0.9621 0.6054 1.6115 -0.1986 0.3028  0.1554  107 GLN B O   
2332 C CB  . GLN B 33  ? 1.0657 0.6509 1.6088 -0.1633 0.2505  0.2333  107 GLN B CB  
2333 C CG  . GLN B 33  ? 1.2648 0.7647 1.7476 -0.1695 0.2607  0.2541  107 GLN B CG  
2334 C CD  . GLN B 33  ? 1.3196 0.8100 1.8207 -0.1355 0.2261  0.2670  107 GLN B CD  
2335 O OE1 . GLN B 33  ? 1.2597 0.7949 1.7977 -0.1064 0.1902  0.2702  107 GLN B OE1 
2336 N NE2 . GLN B 33  ? 1.1962 0.6287 1.6718 -0.1407 0.2386  0.2717  107 GLN B NE2 
2337 N N   . GLN B 34  ? 0.8978 0.6397 1.6017 -0.2037 0.3047  0.1230  108 GLN B N   
2338 C CA  . GLN B 34  ? 0.8714 0.6388 1.6025 -0.2340 0.3430  0.0823  108 GLN B CA  
2339 C C   . GLN B 34  ? 0.8001 0.6384 1.6116 -0.2250 0.3315  0.0412  108 GLN B C   
2340 O O   . GLN B 34  ? 0.9015 0.7511 1.7320 -0.2468 0.3576  0.0104  108 GLN B O   
2341 C CB  . GLN B 34  ? 0.8827 0.6802 1.6139 -0.2556 0.3705  0.0616  108 GLN B CB  
2342 C CG  . GLN B 34  ? 0.9731 0.6948 1.6117 -0.2712 0.3880  0.0983  108 GLN B CG  
2343 C CD  . GLN B 34  ? 1.0730 0.8245 1.7101 -0.2964 0.4224  0.0719  108 GLN B CD  
2344 O OE1 . GLN B 34  ? 1.0459 0.8621 1.7437 -0.3110 0.4450  0.0223  108 GLN B OE1 
2345 N NE2 . GLN B 34  ? 1.2061 0.9122 1.7727 -0.3003 0.4252  0.1025  108 GLN B NE2 
2346 N N   . SER B 35  ? 0.7538 0.6353 1.6055 -0.1947 0.2926  0.0394  109 SER B N   
2347 C CA  . SER B 35  ? 0.6628 0.6104 1.5794 -0.1853 0.2774  -0.0013 109 SER B CA  
2348 C C   . SER B 35  ? 0.6385 0.5755 1.5633 -0.1638 0.2499  0.0075  109 SER B C   
2349 O O   . SER B 35  ? 0.6234 0.6066 1.5885 -0.1515 0.2291  -0.0201 109 SER B O   
2350 C CB  . SER B 35  ? 0.6103 0.6214 1.5641 -0.1700 0.2566  -0.0212 109 SER B CB  
2351 O OG  . SER B 35  ? 0.7509 0.7796 1.7042 -0.1902 0.2862  -0.0368 109 SER B OG  
2352 N N   . PHE B 36  ? 0.6761 0.5519 1.5599 -0.1583 0.2486  0.0434  110 PHE B N   
2353 C CA  . PHE B 36  ? 0.7059 0.5742 1.5996 -0.1383 0.2266  0.0490  110 PHE B CA  
2354 C C   . PHE B 36  ? 0.8140 0.6157 1.6702 -0.1443 0.2427  0.0722  110 PHE B C   
2355 O O   . PHE B 36  ? 0.8366 0.5835 1.6410 -0.1498 0.2522  0.1029  110 PHE B O   
2356 C CB  . PHE B 36  ? 0.6000 0.4779 1.4916 -0.1095 0.1895  0.0696  110 PHE B CB  
2357 C CG  . PHE B 36  ? 0.5282 0.4614 1.4512 -0.1006 0.1695  0.0468  110 PHE B CG  
2358 C CD1 . PHE B 36  ? 0.5052 0.4715 1.4590 -0.0926 0.1542  0.0177  110 PHE B CD1 
2359 C CD2 . PHE B 36  ? 0.5701 0.5162 1.4852 -0.1004 0.1656  0.0544  110 PHE B CD2 
2360 C CE1 . PHE B 36  ? 0.4693 0.4764 1.4418 -0.0828 0.1320  -0.0024 110 PHE B CE1 
2361 C CE2 . PHE B 36  ? 0.5018 0.4952 1.4442 -0.0903 0.1458  0.0327  110 PHE B CE2 
2362 C CZ  . PHE B 36  ? 0.4399 0.4617 1.4087 -0.0803 0.1272  0.0047  110 PHE B CZ  
2363 N N   . GLN B 37  ? 0.7796 0.5808 1.6560 -0.1430 0.2449  0.0571  111 GLN B N   
2364 C CA  . GLN B 37  ? 0.8170 0.5571 1.6643 -0.1393 0.2511  0.0796  111 GLN B CA  
2365 C C   . GLN B 37  ? 0.7954 0.5355 1.6446 -0.1069 0.2168  0.1026  111 GLN B C   
2366 O O   . GLN B 37  ? 0.7420 0.5298 1.6287 -0.0927 0.1968  0.0859  111 GLN B O   
2367 C CB  . GLN B 37  ? 0.8289 0.5709 1.6994 -0.1523 0.2694  0.0516  111 GLN B CB  
2368 C CG  . GLN B 37  ? 1.0670 0.7608 1.9070 -0.1840 0.3088  0.0474  111 GLN B CG  
2369 C CD  . GLN B 37  ? 1.1281 0.8480 2.0020 -0.2032 0.3280  0.0072  111 GLN B CD  
2370 O OE1 . GLN B 37  ? 1.0520 0.8310 1.9702 -0.1945 0.3109  -0.0201 111 GLN B OE1 
2371 N NE2 . GLN B 37  ? 1.1888 0.8598 2.0353 -0.2305 0.3631  0.0034  111 GLN B NE2 
2372 N N   . ARG B 38  ? 0.7874 0.4730 1.5922 -0.0958 0.2091  0.1390  112 ARG B N   
2373 C CA  . ARG B 38  ? 0.7913 0.4801 1.6009 -0.0658 0.1765  0.1581  112 ARG B CA  
2374 C C   . ARG B 38  ? 0.7913 0.4559 1.6145 -0.0574 0.1798  0.1550  112 ARG B C   
2375 O O   . ARG B 38  ? 0.8871 0.4836 1.6715 -0.0605 0.1934  0.1715  112 ARG B O   
2376 C CB  . ARG B 38  ? 0.8936 0.5370 1.6480 -0.0546 0.1614  0.1960  112 ARG B CB  
2377 C CG  . ARG B 38  ? 0.8820 0.5514 1.6490 -0.0258 0.1235  0.2090  112 ARG B CG  
2378 C CD  . ARG B 38  ? 0.8881 0.5174 1.5963 -0.0151 0.1056  0.2440  112 ARG B CD  
2379 N NE  . ARG B 38  ? 0.9072 0.5469 1.5930 -0.0326 0.1152  0.2457  112 ARG B NE  
2380 C CZ  . ARG B 38  ? 0.9975 0.6074 1.6289 -0.0291 0.1033  0.2731  112 ARG B CZ  
2381 N NH1 . ARG B 38  ? 0.9987 0.5687 1.5908 -0.0055 0.0761  0.3016  112 ARG B NH1 
2382 N NH2 . ARG B 38  ? 0.9282 0.5493 1.5440 -0.0488 0.1185  0.2703  112 ARG B NH2 
2383 N N   . LEU B 39  ? 0.8014 0.5155 1.6740 -0.0479 0.1688  0.1332  113 LEU B N   
2384 C CA  . LEU B 39  ? 0.7894 0.4869 1.6819 -0.0425 0.1757  0.1250  113 LEU B CA  
2385 C C   . LEU B 39  ? 0.8201 0.5048 1.7170 -0.0157 0.1514  0.1447  113 LEU B C   
2386 O O   . LEU B 39  ? 0.8461 0.4749 1.7251 -0.0062 0.1554  0.1590  113 LEU B O   
2387 C CB  . LEU B 39  ? 0.7476 0.4992 1.6847 -0.0494 0.1801  0.0882  113 LEU B CB  
2388 C CG  . LEU B 39  ? 0.7325 0.5012 1.6709 -0.0732 0.1998  0.0623  113 LEU B CG  
2389 C CD1 . LEU B 39  ? 0.6317 0.4481 1.6012 -0.0743 0.1944  0.0281  113 LEU B CD1 
2390 C CD2 . LEU B 39  ? 0.7583 0.4748 1.6754 -0.0931 0.2314  0.0620  113 LEU B CD2 
2391 N N   . SER B 40  ? 0.8033 0.5365 1.7224 -0.0032 0.1259  0.1438  114 SER B N   
2392 C CA  . SER B 40  ? 0.7771 0.5079 1.7080 0.0205  0.1016  0.1569  114 SER B CA  
2393 C C   . SER B 40  ? 0.7176 0.4958 1.6564 0.0259  0.0764  0.1581  114 SER B C   
2394 O O   . SER B 40  ? 0.6682 0.4861 1.6140 0.0130  0.0787  0.1423  114 SER B O   
2395 C CB  . SER B 40  ? 0.8090 0.5540 1.7882 0.0245  0.1076  0.1356  114 SER B CB  
2396 O OG  . SER B 40  ? 0.7773 0.5837 1.7945 0.0154  0.1059  0.1082  114 SER B OG  
2397 N N   . ARG B 41  ? 0.7104 0.4805 1.6445 0.0470  0.0509  0.1755  115 ARG B N   
2398 C CA  . ARG B 41  ? 0.6226 0.4345 1.5647 0.0518  0.0267  0.1748  115 ARG B CA  
2399 C C   . ARG B 41  ? 0.5990 0.4553 1.5974 0.0492  0.0248  0.1463  115 ARG B C   
2400 O O   . ARG B 41  ? 0.6437 0.4927 1.6730 0.0609  0.0235  0.1403  115 ARG B O   
2401 C CB  . ARG B 41  ? 0.6760 0.4621 1.5869 0.0762  -0.0017 0.2030  115 ARG B CB  
2402 C CG  . ARG B 41  ? 0.6672 0.4949 1.5813 0.0789  -0.0257 0.2019  115 ARG B CG  
2403 C CD  . ARG B 41  ? 0.8214 0.6381 1.7221 0.1079  -0.0591 0.2209  115 ARG B CD  
2404 N NE  . ARG B 41  ? 0.8983 0.6623 1.7298 0.1170  -0.0676 0.2551  115 ARG B NE  
2405 C CZ  . ARG B 41  ? 0.9535 0.6932 1.7539 0.1448  -0.0987 0.2774  115 ARG B CZ  
2406 N NH1 . ARG B 41  ? 0.8703 0.6426 1.7114 0.1688  -0.1257 0.2668  115 ARG B NH1 
2407 N NH2 . ARG B 41  ? 1.0841 0.7645 1.8089 0.1483  -0.1027 0.3093  115 ARG B NH2 
2408 N N   . LEU B 42  ? 0.5708 0.4668 1.5786 0.0340  0.0259  0.1276  116 LEU B N   
2409 C CA  . LEU B 42  ? 0.4902 0.4189 1.5413 0.0273  0.0274  0.0994  116 LEU B CA  
2410 C C   . LEU B 42  ? 0.4705 0.4124 1.5375 0.0383  0.0045  0.1000  116 LEU B C   
2411 O O   . LEU B 42  ? 0.4657 0.4213 1.5767 0.0384  0.0063  0.0785  116 LEU B O   
2412 C CB  . LEU B 42  ? 0.4289 0.3833 1.4702 0.0113  0.0362  0.0788  116 LEU B CB  
2413 C CG  . LEU B 42  ? 0.4735 0.4215 1.5042 0.0045  0.0567  0.0684  116 LEU B CG  
2414 C CD1 . LEU B 42  ? 0.5090 0.4735 1.5126 -0.0018 0.0566  0.0494  116 LEU B CD1 
2415 C CD2 . LEU B 42  ? 0.4364 0.3798 1.5019 0.0038  0.0737  0.0521  116 LEU B CD2 
2416 N N   . GLY B 43  ? 0.4802 0.4195 1.5133 0.0478  -0.0159 0.1210  117 GLY B N   
2417 C CA  . GLY B 43  ? 0.4853 0.4436 1.5319 0.0617  -0.0403 0.1198  117 GLY B CA  
2418 C C   . GLY B 43  ? 0.5401 0.4967 1.5408 0.0687  -0.0602 0.1440  117 GLY B C   
2419 O O   . GLY B 43  ? 0.5538 0.4948 1.5144 0.0592  -0.0520 0.1579  117 GLY B O   
2420 N N   . HIS B 44  ? 0.6043 0.5815 1.6143 0.0858  -0.0867 0.1458  118 HIS B N   
2421 C CA  . HIS B 44  ? 0.6325 0.6112 1.6011 0.0945  -0.1098 0.1689  118 HIS B CA  
2422 C C   . HIS B 44  ? 0.6341 0.6607 1.6312 0.1012  -0.1324 0.1514  118 HIS B C   
2423 O O   . HIS B 44  ? 0.6522 0.7040 1.6969 0.1116  -0.1386 0.1300  118 HIS B O   
2424 C CB  . HIS B 44  ? 0.7065 0.6451 1.6356 0.1173  -0.1260 0.2031  118 HIS B CB  
2425 C CG  . HIS B 44  ? 0.7066 0.6459 1.6645 0.1455  -0.1454 0.2010  118 HIS B CG  
2426 N ND1 . HIS B 44  ? 0.7891 0.6993 1.7642 0.1527  -0.1306 0.1984  118 HIS B ND1 
2427 C CD2 . HIS B 44  ? 0.6938 0.6613 1.6672 0.1706  -0.1797 0.1992  118 HIS B CD2 
2428 C CE1 . HIS B 44  ? 0.7210 0.6371 1.7198 0.1832  -0.1548 0.1963  118 HIS B CE1 
2429 N NE2 . HIS B 44  ? 0.7210 0.6749 1.7207 0.1952  -0.1857 0.1957  118 HIS B NE2 
2430 N N   . GLY B 45  ? 0.6536 0.6957 1.6236 0.0947  -0.1435 0.1581  119 GLY B N   
2431 C CA  . GLY B 45  ? 0.6480 0.7423 1.6410 0.0974  -0.1655 0.1408  119 GLY B CA  
2432 C C   . GLY B 45  ? 0.7336 0.8324 1.6821 0.0948  -0.1836 0.1621  119 GLY B C   
2433 O O   . GLY B 45  ? 0.7890 0.8447 1.6852 0.0996  -0.1862 0.1960  119 GLY B O   
2434 N N   . SER B 46  ? 0.7440 0.8932 1.7069 0.0821  -0.1924 0.1389  120 SER B N   
2435 C CA  . SER B 46  ? 0.7819 0.9295 1.6720 0.0684  -0.2021 0.1499  120 SER B CA  
2436 C C   . SER B 46  ? 0.7933 0.8962 1.6175 0.0469  -0.1729 0.1582  120 SER B C   
2437 O O   . SER B 46  ? 0.7862 0.8647 1.5453 0.0438  -0.1775 0.1809  120 SER B O   
2438 C CB  . SER B 46  ? 0.7690 0.9748 1.6761 0.0504  -0.2088 0.1143  120 SER B CB  
2439 O OG  . SER B 46  ? 0.7099 0.9268 1.6474 0.0275  -0.1776 0.0779  120 SER B OG  
2440 N N   . TYR B 47  ? 0.7779 0.8704 1.6177 0.0326  -0.1440 0.1377  121 TYR B N   
2441 C CA  . TYR B 47  ? 0.7650 0.8189 1.5527 0.0186  -0.1209 0.1426  121 TYR B CA  
2442 C C   . TYR B 47  ? 0.7637 0.7807 1.5306 0.0310  -0.1195 0.1755  121 TYR B C   
2443 O O   . TYR B 47  ? 0.7349 0.7303 1.4472 0.0231  -0.1116 0.1868  121 TYR B O   
2444 C CB  . TYR B 47  ? 0.7147 0.7611 1.5269 0.0067  -0.0967 0.1166  121 TYR B CB  
2445 C CG  . TYR B 47  ? 0.7549 0.8022 1.6340 0.0199  -0.0927 0.1147  121 TYR B CG  
2446 C CD1 . TYR B 47  ? 0.7631 0.8457 1.7046 0.0256  -0.0995 0.0954  121 TYR B CD1 
2447 C CD2 . TYR B 47  ? 0.7000 0.7150 1.5837 0.0257  -0.0802 0.1286  121 TYR B CD2 
2448 C CE1 . TYR B 47  ? 0.7300 0.8072 1.7248 0.0376  -0.0933 0.0912  121 TYR B CE1 
2449 C CE2 . TYR B 47  ? 0.5892 0.5991 1.5221 0.0334  -0.0731 0.1245  121 TYR B CE2 
2450 C CZ  . TYR B 47  ? 0.6605 0.6966 1.6396 0.0385  -0.0791 0.1061  121 TYR B CZ  
2451 O OH  . TYR B 47  ? 0.7130 0.7391 1.7236 0.0419  -0.0692 0.0985  121 TYR B OH  
2452 N N   . GLY B 48  ? 0.8151 0.8215 1.6240 0.0488  -0.1239 0.1887  122 GLY B N   
2453 C CA  . GLY B 48  ? 0.7965 0.7593 1.5845 0.0556  -0.1161 0.2169  122 GLY B CA  
2454 C C   . GLY B 48  ? 0.7776 0.7271 1.6045 0.0625  -0.1049 0.2132  122 GLY B C   
2455 O O   . GLY B 48  ? 0.8092 0.7749 1.6718 0.0757  -0.1180 0.2059  122 GLY B O   
2456 N N   . GLU B 49  ? 0.6329 0.5588 1.4480 0.0509  -0.0788 0.2124  123 GLU B N   
2457 C CA  . GLU B 49  ? 0.5673 0.4808 1.4075 0.0517  -0.0636 0.2061  123 GLU B CA  
2458 C C   . GLU B 49  ? 0.4978 0.4221 1.3552 0.0336  -0.0385 0.1811  123 GLU B C   
2459 O O   . GLU B 49  ? 0.4831 0.4087 1.3177 0.0232  -0.0302 0.1773  123 GLU B O   
2460 C CB  . GLU B 49  ? 0.6508 0.5175 1.4530 0.0578  -0.0584 0.2340  123 GLU B CB  
2461 C CG  . GLU B 49  ? 0.7717 0.6159 1.5466 0.0802  -0.0868 0.2608  123 GLU B CG  
2462 C CD  . GLU B 49  ? 0.8646 0.6440 1.5894 0.0844  -0.0776 0.2876  123 GLU B CD  
2463 O OE1 . GLU B 49  ? 0.8765 0.6278 1.5602 0.0670  -0.0572 0.2981  123 GLU B OE1 
2464 O OE2 . GLU B 49  ? 0.7837 0.5359 1.5082 0.1044  -0.0886 0.2964  123 GLU B OE2 
2465 N N   . VAL B 50  ? 0.4957 0.4272 1.3922 0.0316  -0.0281 0.1630  124 VAL B N   
2466 C CA  . VAL B 50  ? 0.4217 0.3633 1.3330 0.0174  -0.0073 0.1393  124 VAL B CA  
2467 C C   . VAL B 50  ? 0.5218 0.4429 1.4443 0.0181  0.0095  0.1427  124 VAL B C   
2468 O O   . VAL B 50  ? 0.5482 0.4597 1.4939 0.0270  0.0079  0.1450  124 VAL B O   
2469 C CB  . VAL B 50  ? 0.4242 0.3894 1.3675 0.0113  -0.0064 0.1109  124 VAL B CB  
2470 C CG1 . VAL B 50  ? 0.4121 0.3847 1.3548 0.0025  0.0104  0.0878  124 VAL B CG1 
2471 C CG2 . VAL B 50  ? 0.3900 0.3654 1.3206 0.0101  -0.0208 0.1068  124 VAL B CG2 
2472 N N   . PHE B 51  ? 0.4881 0.4006 1.3963 0.0090  0.0265  0.1404  125 PHE B N   
2473 C CA  . PHE B 51  ? 0.4892 0.3752 1.4013 0.0059  0.0465  0.1425  125 PHE B CA  
2474 C C   . PHE B 51  ? 0.5129 0.4178 1.4481 -0.0045 0.0631  0.1126  125 PHE B C   
2475 O O   . PHE B 51  ? 0.4788 0.4063 1.4100 -0.0095 0.0607  0.0958  125 PHE B O   
2476 C CB  . PHE B 51  ? 0.5879 0.4401 1.4619 0.0003  0.0571  0.1626  125 PHE B CB  
2477 C CG  . PHE B 51  ? 0.5834 0.4007 1.4199 0.0125  0.0420  0.1952  125 PHE B CG  
2478 C CD1 . PHE B 51  ? 0.6473 0.4208 1.4708 0.0239  0.0412  0.2123  125 PHE B CD1 
2479 C CD2 . PHE B 51  ? 0.6418 0.4645 1.4494 0.0144  0.0273  0.2089  125 PHE B CD2 
2480 C CE1 . PHE B 51  ? 0.7398 0.4752 1.5192 0.0395  0.0221  0.2428  125 PHE B CE1 
2481 C CE2 . PHE B 51  ? 0.6946 0.4836 1.4608 0.0268  0.0104  0.2390  125 PHE B CE2 
2482 C CZ  . PHE B 51  ? 0.7481 0.4932 1.4986 0.0406  0.0060  0.2562  125 PHE B CZ  
2483 N N   . LYS B 52  ? 0.5963 0.4858 1.5498 -0.0057 0.0783  0.1060  126 LYS B N   
2484 C CA  . LYS B 52  ? 0.6079 0.5049 1.5743 -0.0161 0.0962  0.0793  126 LYS B CA  
2485 C C   . LYS B 52  ? 0.5904 0.4625 1.5398 -0.0287 0.1159  0.0832  126 LYS B C   
2486 O O   . LYS B 52  ? 0.6380 0.4685 1.5718 -0.0301 0.1274  0.1024  126 LYS B O   
2487 C CB  . LYS B 52  ? 0.6142 0.5047 1.6075 -0.0140 0.1061  0.0681  126 LYS B CB  
2488 C CG  . LYS B 52  ? 0.6393 0.5316 1.6392 -0.0255 0.1249  0.0401  126 LYS B CG  
2489 C CD  . LYS B 52  ? 0.6484 0.5312 1.6737 -0.0240 0.1370  0.0293  126 LYS B CD  
2490 C CE  . LYS B 52  ? 0.5840 0.4616 1.6082 -0.0380 0.1569  0.0028  126 LYS B CE  
2491 N NZ  . LYS B 52  ? 0.5670 0.4315 1.6139 -0.0382 0.1721  -0.0083 126 LYS B NZ  
2492 N N   . VAL B 53  ? 0.6209 0.5136 1.5700 -0.0387 0.1198  0.0634  127 VAL B N   
2493 C CA  . VAL B 53  ? 0.5387 0.4176 1.4784 -0.0557 0.1403  0.0609  127 VAL B CA  
2494 C C   . VAL B 53  ? 0.5716 0.4708 1.5304 -0.0689 0.1516  0.0251  127 VAL B C   
2495 O O   . VAL B 53  ? 0.6046 0.5280 1.5740 -0.0631 0.1378  0.0044  127 VAL B O   
2496 C CB  . VAL B 53  ? 0.5413 0.4303 1.4659 -0.0575 0.1334  0.0710  127 VAL B CB  
2497 C CG1 . VAL B 53  ? 0.6091 0.4756 1.5068 -0.0456 0.1196  0.1060  127 VAL B CG1 
2498 C CG2 . VAL B 53  ? 0.4719 0.4016 1.4098 -0.0520 0.1144  0.0489  127 VAL B CG2 
2499 N N   . ARG B 54  ? 0.5915 0.4774 1.5489 -0.0892 0.1772  0.0168  128 ARG B N   
2500 C CA  . ARG B 54  ? 0.6284 0.5414 1.6057 -0.1059 0.1875  -0.0202 128 ARG B CA  
2501 C C   . ARG B 54  ? 0.5792 0.5149 1.5607 -0.1188 0.1944  -0.0297 128 ARG B C   
2502 O O   . ARG B 54  ? 0.5961 0.5061 1.5582 -0.1297 0.2134  -0.0111 128 ARG B O   
2503 C CB  . ARG B 54  ? 0.6814 0.5677 1.6597 -0.1240 0.2158  -0.0309 128 ARG B CB  
2504 C CG  . ARG B 54  ? 0.7170 0.6345 1.7164 -0.1463 0.2289  -0.0710 128 ARG B CG  
2505 C CD  . ARG B 54  ? 0.7419 0.6369 1.7436 -0.1629 0.2526  -0.0862 128 ARG B CD  
2506 N NE  . ARG B 54  ? 0.7223 0.6302 1.7343 -0.1528 0.2369  -0.1011 128 ARG B NE  
2507 C CZ  . ARG B 54  ? 0.8143 0.6906 1.8209 -0.1492 0.2457  -0.0940 128 ARG B CZ  
2508 N NH1 . ARG B 54  ? 0.7903 0.6171 1.7819 -0.1529 0.2675  -0.0717 128 ARG B NH1 
2509 N NH2 . ARG B 54  ? 0.8236 0.7148 1.8371 -0.1426 0.2328  -0.1104 128 ARG B NH2 
2510 N N   . SER B 55  ? 0.6051 0.5871 1.6092 -0.1178 0.1787  -0.0594 129 SER B N   
2511 C CA  . SER B 55  ? 0.5801 0.5961 1.5979 -0.1264 0.1822  -0.0744 129 SER B CA  
2512 C C   . SER B 55  ? 0.7101 0.7277 1.7369 -0.1554 0.2181  -0.0938 129 SER B C   
2513 O O   . SER B 55  ? 0.7793 0.8054 1.8213 -0.1683 0.2280  -0.1197 129 SER B O   
2514 C CB  . SER B 55  ? 0.6043 0.6698 1.6458 -0.1157 0.1527  -0.1053 129 SER B CB  
2515 O OG  . SER B 55  ? 0.6497 0.7561 1.7106 -0.1194 0.1535  -0.1234 129 SER B OG  
2516 N N   . LYS B 56  ? 0.7784 0.7855 1.7920 -0.1687 0.2401  -0.0823 130 LYS B N   
2517 C CA  . LYS B 56  ? 0.7421 0.7496 1.7600 -0.2005 0.2784  -0.1043 130 LYS B CA  
2518 C C   . LYS B 56  ? 0.7102 0.7899 1.7751 -0.2076 0.2748  -0.1542 130 LYS B C   
2519 O O   . LYS B 56  ? 0.8944 0.9876 1.9762 -0.2310 0.2980  -0.1848 130 LYS B O   
2520 C CB  . LYS B 56  ? 0.6997 0.6690 1.6806 -0.2162 0.3060  -0.0793 130 LYS B CB  
2521 C CG  . LYS B 56  ? 0.7621 0.6485 1.6892 -0.2224 0.3227  -0.0400 130 LYS B CG  
2522 C CD  . LYS B 56  ? 0.8154 0.6564 1.6914 -0.2352 0.3426  -0.0111 130 LYS B CD  
2523 C CE  . LYS B 56  ? 0.8908 0.6402 1.7022 -0.2364 0.3510  0.0309  130 LYS B CE  
2524 N NZ  . LYS B 56  ? 0.9614 0.6551 1.7070 -0.2512 0.3693  0.0596  130 LYS B NZ  
2525 N N   . GLU B 57  ? 0.7267 0.8532 1.8130 -0.1866 0.2444  -0.1647 131 GLU B N   
2526 C CA  . GLU B 57  ? 0.7476 0.9450 1.8791 -0.1881 0.2356  -0.2131 131 GLU B CA  
2527 C C   . GLU B 57  ? 0.7009 0.9239 1.8537 -0.1795 0.2090  -0.2391 131 GLU B C   
2528 O O   . GLU B 57  ? 0.7794 1.0509 1.9677 -0.1905 0.2114  -0.2818 131 GLU B O   
2529 C CB  . GLU B 57  ? 0.8012 1.0364 1.9441 -0.1660 0.2116  -0.2158 131 GLU B CB  
2530 C CG  . GLU B 57  ? 0.8685 1.0850 1.9921 -0.1767 0.2393  -0.1952 131 GLU B CG  
2531 C CD  . GLU B 57  ? 0.9590 1.1946 2.0980 -0.2088 0.2822  -0.2248 131 GLU B CD  
2532 O OE1 . GLU B 57  ? 0.8872 1.1647 2.0625 -0.2194 0.2862  -0.2672 131 GLU B OE1 
2533 O OE2 . GLU B 57  ? 1.0102 1.2166 2.1216 -0.2251 0.3128  -0.2066 131 GLU B OE2 
2534 N N   . ASP B 58  ? 0.6626 0.8542 1.7937 -0.1617 0.1849  -0.2158 132 ASP B N   
2535 C CA  . ASP B 58  ? 0.6910 0.9022 1.8340 -0.1519 0.1559  -0.2374 132 ASP B CA  
2536 C C   . ASP B 58  ? 0.7095 0.8822 1.8390 -0.1652 0.1720  -0.2322 132 ASP B C   
2537 O O   . ASP B 58  ? 0.7101 0.9074 1.8583 -0.1731 0.1658  -0.2633 132 ASP B O   
2538 C CB  . ASP B 58  ? 0.7711 0.9775 1.8977 -0.1222 0.1156  -0.2206 132 ASP B CB  
2539 C CG  . ASP B 58  ? 0.7738 0.9801 1.8978 -0.1146 0.0888  -0.2339 132 ASP B CG  
2540 O OD1 . ASP B 58  ? 0.7204 0.9643 1.8706 -0.1230 0.0828  -0.2710 132 ASP B OD1 
2541 O OD2 . ASP B 58  ? 0.6921 0.8622 1.7875 -0.1011 0.0737  -0.2086 132 ASP B OD2 
2542 N N   . GLY B 59  ? 0.7191 0.8334 1.8171 -0.1671 0.1918  -0.1949 133 GLY B N   
2543 C CA  . GLY B 59  ? 0.6611 0.7362 1.7452 -0.1760 0.2079  -0.1886 133 GLY B CA  
2544 C C   . GLY B 59  ? 0.7131 0.7636 1.7781 -0.1552 0.1850  -0.1702 133 GLY B C   
2545 O O   . GLY B 59  ? 0.6816 0.6928 1.7314 -0.1573 0.1999  -0.1562 133 GLY B O   
2546 N N   . ARG B 60  ? 0.6656 0.7372 1.7301 -0.1358 0.1508  -0.1717 134 ARG B N   
2547 C CA  . ARG B 60  ? 0.6679 0.7179 1.7116 -0.1200 0.1315  -0.1592 134 ARG B CA  
2548 C C   . ARG B 60  ? 0.6640 0.6758 1.6840 -0.1054 0.1356  -0.1182 134 ARG B C   
2549 O O   . ARG B 60  ? 0.6148 0.6113 1.6315 -0.1082 0.1524  -0.0975 134 ARG B O   
2550 C CB  . ARG B 60  ? 0.6899 0.7692 1.7362 -0.1076 0.0945  -0.1756 134 ARG B CB  
2551 C CG  . ARG B 60  ? 0.6918 0.8116 1.7623 -0.1179 0.0813  -0.2181 134 ARG B CG  
2552 C CD  . ARG B 60  ? 0.7914 0.9085 1.8459 -0.1091 0.0494  -0.2277 134 ARG B CD  
2553 N NE  . ARG B 60  ? 0.8191 0.9829 1.8981 -0.1119 0.0227  -0.2685 134 ARG B NE  
2554 C CZ  . ARG B 60  ? 0.8896 1.0797 1.9736 -0.0946 -0.0180 -0.2825 134 ARG B CZ  
2555 N NH1 . ARG B 60  ? 0.8103 0.9809 1.8746 -0.0767 -0.0339 -0.2589 134 ARG B NH1 
2556 N NH2 . ARG B 60  ? 0.8904 1.1280 1.9983 -0.0930 -0.0462 -0.3223 134 ARG B NH2 
2557 N N   . LEU B 61  ? 0.6587 0.6566 1.6611 -0.0912 0.1201  -0.1080 135 LEU B N   
2558 C CA  . LEU B 61  ? 0.6115 0.5830 1.5983 -0.0770 0.1217  -0.0752 135 LEU B CA  
2559 C C   . LEU B 61  ? 0.5740 0.5532 1.5453 -0.0616 0.0957  -0.0641 135 LEU B C   
2560 O O   . LEU B 61  ? 0.5905 0.5798 1.5524 -0.0600 0.0767  -0.0809 135 LEU B O   
2561 C CB  . LEU B 61  ? 0.6470 0.6001 1.6306 -0.0762 0.1310  -0.0764 135 LEU B CB  
2562 C CG  . LEU B 61  ? 0.6100 0.5408 1.6050 -0.0880 0.1601  -0.0750 135 LEU B CG  
2563 C CD1 . LEU B 61  ? 0.5291 0.4417 1.5263 -0.0839 0.1689  -0.0744 135 LEU B CD1 
2564 C CD2 . LEU B 61  ? 0.6069 0.5187 1.5997 -0.0863 0.1705  -0.0466 135 LEU B CD2 
2565 N N   . TYR B 62  ? 0.5511 0.5223 1.5162 -0.0529 0.0948  -0.0360 136 TYR B N   
2566 C CA  . TYR B 62  ? 0.5164 0.4930 1.4647 -0.0409 0.0729  -0.0244 136 TYR B CA  
2567 C C   . TYR B 62  ? 0.5067 0.4708 1.4479 -0.0314 0.0736  0.0049  136 TYR B C   
2568 O O   . TYR B 62  ? 0.5282 0.4775 1.4793 -0.0329 0.0888  0.0191  136 TYR B O   
2569 C CB  . TYR B 62  ? 0.4823 0.4743 1.4352 -0.0425 0.0655  -0.0262 136 TYR B CB  
2570 C CG  . TYR B 62  ? 0.5042 0.5212 1.4769 -0.0514 0.0616  -0.0597 136 TYR B CG  
2571 C CD1 . TYR B 62  ? 0.5262 0.5570 1.4965 -0.0464 0.0352  -0.0798 136 TYR B CD1 
2572 C CD2 . TYR B 62  ? 0.5452 0.5743 1.5399 -0.0660 0.0827  -0.0735 136 TYR B CD2 
2573 C CE1 . TYR B 62  ? 0.4984 0.5614 1.4930 -0.0514 0.0249  -0.1133 136 TYR B CE1 
2574 C CE2 . TYR B 62  ? 0.5668 0.6308 1.5853 -0.0739 0.0770  -0.1087 136 TYR B CE2 
2575 C CZ  . TYR B 62  ? 0.5334 0.6175 1.5538 -0.0645 0.0458  -0.1286 136 TYR B CZ  
2576 O OH  . TYR B 62  ? 0.6194 0.7460 1.6676 -0.0685 0.0344  -0.1660 136 TYR B OH  
2577 N N   . ALA B 63  ? 0.4696 0.4384 1.3930 -0.0233 0.0556  0.0121  137 ALA B N   
2578 C CA  . ALA B 63  ? 0.4235 0.3890 1.3431 -0.0161 0.0505  0.0366  137 ALA B CA  
2579 C C   . ALA B 63  ? 0.4026 0.3704 1.3049 -0.0147 0.0396  0.0513  137 ALA B C   
2580 O O   . ALA B 63  ? 0.5104 0.4841 1.3981 -0.0150 0.0281  0.0394  137 ALA B O   
2581 C CB  . ALA B 63  ? 0.3618 0.3312 1.2748 -0.0127 0.0426  0.0282  137 ALA B CB  
2582 N N   . VAL B 64  ? 0.3754 0.3327 1.2750 -0.0137 0.0428  0.0773  138 VAL B N   
2583 C CA  . VAL B 64  ? 0.3960 0.3502 1.2735 -0.0137 0.0354  0.0928  138 VAL B CA  
2584 C C   . VAL B 64  ? 0.4176 0.3651 1.2785 -0.0068 0.0215  0.1144  138 VAL B C   
2585 O O   . VAL B 64  ? 0.5270 0.4619 1.3953 -0.0026 0.0227  0.1295  138 VAL B O   
2586 C CB  . VAL B 64  ? 0.4412 0.3819 1.3182 -0.0226 0.0535  0.1028  138 VAL B CB  
2587 C CG1 . VAL B 64  ? 0.4098 0.3447 1.2609 -0.0236 0.0482  0.1189  138 VAL B CG1 
2588 C CG2 . VAL B 64  ? 0.4190 0.3747 1.3211 -0.0321 0.0666  0.0744  138 VAL B CG2 
2589 N N   . LYS B 65  ? 0.4435 0.3960 1.2815 -0.0049 0.0070  0.1140  139 LYS B N   
2590 C CA  . LYS B 65  ? 0.4215 0.3698 1.2439 0.0007  -0.0080 0.1307  139 LYS B CA  
2591 C C   . LYS B 65  ? 0.4566 0.3898 1.2456 0.0017  -0.0109 0.1525  139 LYS B C   
2592 O O   . LYS B 65  ? 0.4565 0.3890 1.2287 -0.0019 -0.0086 0.1454  139 LYS B O   
2593 C CB  . LYS B 65  ? 0.3909 0.3480 1.2056 -0.0010 -0.0183 0.1127  139 LYS B CB  
2594 C CG  . LYS B 65  ? 0.4405 0.3975 1.2553 0.0036  -0.0332 0.1245  139 LYS B CG  
2595 C CD  . LYS B 65  ? 0.4408 0.3990 1.2489 -0.0043 -0.0368 0.1026  139 LYS B CD  
2596 C CE  . LYS B 65  ? 0.4165 0.3645 1.1662 -0.0100 -0.0375 0.0950  139 LYS B CE  
2597 N NZ  . LYS B 65  ? 0.5503 0.4943 1.2687 -0.0213 -0.0390 0.0755  139 LYS B NZ  
2598 N N   . ARG B 66  ? 0.5116 0.4288 1.2890 0.0076  -0.0169 0.1787  140 ARG B N   
2599 C CA  . ARG B 66  ? 0.4981 0.3942 1.2351 0.0072  -0.0197 0.2034  140 ARG B CA  
2600 C C   . ARG B 66  ? 0.5327 0.4402 1.2462 0.0154  -0.0447 0.2121  140 ARG B C   
2601 O O   . ARG B 66  ? 0.5808 0.4920 1.3213 0.0270  -0.0601 0.2177  140 ARG B O   
2602 C CB  . ARG B 66  ? 0.5333 0.3965 1.2550 0.0054  -0.0075 0.2257  140 ARG B CB  
2603 C CG  . ARG B 66  ? 0.6375 0.4726 1.3032 0.0059  -0.0151 0.2553  140 ARG B CG  
2604 C CD  . ARG B 66  ? 0.6351 0.4208 1.2738 -0.0014 0.0037  0.2766  140 ARG B CD  
2605 N NE  . ARG B 66  ? 0.7021 0.4697 1.3491 0.0132  -0.0060 0.2845  140 ARG B NE  
2606 C CZ  . ARG B 66  ? 0.7851 0.5015 1.4021 0.0099  0.0088  0.2999  140 ARG B CZ  
2607 N NH1 . ARG B 66  ? 0.8825 0.5627 1.4603 -0.0117 0.0376  0.3075  140 ARG B NH1 
2608 N NH2 . ARG B 66  ? 0.9235 0.6209 1.5483 0.0271  -0.0030 0.3058  140 ARG B NH2 
2609 N N   . SER B 67  ? 0.5596 0.4755 1.2272 0.0097  -0.0484 0.2099  141 SER B N   
2610 C CA  . SER B 67  ? 0.5852 0.5150 1.2292 0.0131  -0.0710 0.2147  141 SER B CA  
2611 C C   . SER B 67  ? 0.6658 0.5759 1.2854 0.0217  -0.0857 0.2458  141 SER B C   
2612 O O   . SER B 67  ? 0.7294 0.6055 1.3247 0.0191  -0.0730 0.2650  141 SER B O   
2613 C CB  . SER B 67  ? 0.5818 0.5185 1.1771 0.0028  -0.0688 0.2029  141 SER B CB  
2614 O OG  . SER B 67  ? 0.6033 0.5212 1.1550 -0.0028 -0.0570 0.2158  141 SER B OG  
2615 N N   . MET B 68  ? 0.6968 0.6265 1.3207 0.0312  -0.1131 0.2488  142 MET B N   
2616 C CA  . MET B 68  ? 0.7823 0.6918 1.3875 0.0466  -0.1363 0.2781  142 MET B CA  
2617 C C   . MET B 68  ? 0.7621 0.6470 1.2867 0.0374  -0.1389 0.2982  142 MET B C   
2618 O O   . MET B 68  ? 0.7901 0.6270 1.2741 0.0377  -0.1320 0.3243  142 MET B O   
2619 C CB  . MET B 68  ? 0.8268 0.7759 1.4725 0.0625  -0.1690 0.2695  142 MET B CB  
2620 C CG  . MET B 68  ? 0.8862 0.8159 1.5130 0.0857  -0.2024 0.2989  142 MET B CG  
2621 S SD  . MET B 68  ? 1.2026 1.1976 1.8837 0.1052  -0.2459 0.2806  142 MET B SD  
2622 C CE  . MET B 68  ? 0.9688 0.9603 1.7354 0.1339  -0.2492 0.2777  142 MET B CE  
2623 N N   . SER B 69  ? 0.8172 0.7286 1.3122 0.0262  -0.1456 0.2850  143 SER B N   
2624 C CA  . SER B 69  ? 0.8706 0.7633 1.2879 0.0162  -0.1508 0.3001  143 SER B CA  
2625 C C   . SER B 69  ? 0.8722 0.7572 1.2561 -0.0042 -0.1184 0.2863  143 SER B C   
2626 O O   . SER B 69  ? 0.8293 0.7359 1.2446 -0.0087 -0.1045 0.2603  143 SER B O   
2627 C CB  . SER B 69  ? 0.9551 0.8848 1.3618 0.0175  -0.1836 0.2923  143 SER B CB  
2628 O OG  . SER B 69  ? 1.0374 0.9946 1.5023 0.0390  -0.2133 0.2913  143 SER B OG  
2629 N N   . PRO B 70  ? 0.7939 0.6450 1.1116 -0.0157 -0.1059 0.3019  144 PRO B N   
2630 C CA  . PRO B 70  ? 0.7367 0.5852 1.0272 -0.0323 -0.0759 0.2848  144 PRO B CA  
2631 C C   . PRO B 70  ? 0.8315 0.7083 1.1107 -0.0380 -0.0839 0.2620  144 PRO B C   
2632 O O   . PRO B 70  ? 0.9219 0.8219 1.2059 -0.0350 -0.1109 0.2593  144 PRO B O   
2633 C CB  . PRO B 70  ? 0.8032 0.6095 1.0182 -0.0455 -0.0646 0.3063  144 PRO B CB  
2634 C CG  . PRO B 70  ? 0.8534 0.6262 1.0635 -0.0353 -0.0785 0.3363  144 PRO B CG  
2635 C CD  . PRO B 70  ? 0.8375 0.6434 1.1002 -0.0137 -0.1157 0.3352  144 PRO B CD  
2636 N N   . PHE B 71  ? 0.7485 0.6225 1.0137 -0.0463 -0.0590 0.2428  145 PHE B N   
2637 C CA  . PHE B 71  ? 0.7753 0.6616 1.0215 -0.0522 -0.0611 0.2200  145 PHE B CA  
2638 C C   . PHE B 71  ? 0.8837 0.7668 1.0675 -0.0650 -0.0755 0.2271  145 PHE B C   
2639 O O   . PHE B 71  ? 0.9372 0.7967 1.0672 -0.0745 -0.0660 0.2398  145 PHE B O   
2640 C CB  . PHE B 71  ? 0.6984 0.5737 0.9368 -0.0531 -0.0334 0.2001  145 PHE B CB  
2641 C CG  . PHE B 71  ? 0.6873 0.5710 0.9858 -0.0403 -0.0240 0.1884  145 PHE B CG  
2642 C CD1 . PHE B 71  ? 0.6625 0.5606 1.0062 -0.0326 -0.0383 0.1828  145 PHE B CD1 
2643 C CD2 . PHE B 71  ? 0.6683 0.5486 0.9803 -0.0376 -0.0003 0.1795  145 PHE B CD2 
2644 C CE1 . PHE B 71  ? 0.6324 0.5361 1.0253 -0.0227 -0.0310 0.1710  145 PHE B CE1 
2645 C CE2 . PHE B 71  ? 0.6311 0.5244 1.0000 -0.0263 0.0047  0.1657  145 PHE B CE2 
2646 C CZ  . PHE B 71  ? 0.5819 0.4842 0.9871 -0.0190 -0.0116 0.1628  145 PHE B CZ  
2647 N N   . ARG B 72  ? 0.9793 0.8870 1.1695 -0.0681 -0.0970 0.2159  146 ARG B N   
2648 C CA  . ARG B 72  ? 1.0683 0.9818 1.2055 -0.0818 -0.1146 0.2178  146 ARG B CA  
2649 C C   . ARG B 72  ? 1.1030 0.9961 1.1796 -0.0993 -0.0931 0.2007  146 ARG B C   
2650 O O   . ARG B 72  ? 1.1779 1.0628 1.1941 -0.1137 -0.0988 0.2057  146 ARG B O   
2651 C CB  . ARG B 72  ? 1.0947 1.0504 1.2702 -0.0818 -0.1423 0.2045  146 ARG B CB  
2652 C CG  . ARG B 72  ? 1.0638 1.0407 1.3062 -0.0606 -0.1637 0.2181  146 ARG B CG  
2653 C CD  . ARG B 72  ? 1.1114 1.1386 1.4064 -0.0604 -0.1867 0.1970  146 ARG B CD  
2654 N NE  . ARG B 72  ? 1.2454 1.2917 1.6042 -0.0365 -0.2089 0.2098  146 ARG B NE  
2655 C CZ  . ARG B 72  ? 1.1556 1.2037 1.5760 -0.0255 -0.1967 0.2042  146 ARG B CZ  
2656 N NH1 . ARG B 72  ? 1.0856 1.1192 1.5114 -0.0354 -0.1662 0.1867  146 ARG B NH1 
2657 N NH2 . ARG B 72  ? 1.1045 1.1656 1.5787 -0.0026 -0.2171 0.2161  146 ARG B NH2 
2658 N N   . GLY B 73  ? 0.8806 0.7608 0.9681 -0.0968 -0.0696 0.1808  147 GLY B N   
2659 C CA  . GLY B 73  ? 0.7881 0.6428 0.8219 -0.1083 -0.0495 0.1617  147 GLY B CA  
2660 C C   . GLY B 73  ? 0.8158 0.6546 0.8742 -0.0952 -0.0323 0.1431  147 GLY B C   
2661 O O   . GLY B 73  ? 0.8020 0.6535 0.9169 -0.0812 -0.0372 0.1442  147 GLY B O   
2662 N N   . PRO B 74  ? 0.7342 0.6643 0.7591 0.0058  0.1809  -0.0196 148 PRO B N   
2663 C CA  . PRO B 74  ? 0.6766 0.5985 0.7448 0.0147  0.1718  -0.0177 148 PRO B CA  
2664 C C   . PRO B 74  ? 0.7185 0.6450 0.7814 0.0082  0.1450  -0.0141 148 PRO B C   
2665 O O   . PRO B 74  ? 0.6641 0.5974 0.7636 0.0170  0.1309  -0.0069 148 PRO B O   
2666 C CB  . PRO B 74  ? 0.6749 0.5624 0.7361 0.0181  0.1899  -0.0295 148 PRO B CB  
2667 C CG  . PRO B 74  ? 0.7622 0.6380 0.7683 0.0048  0.2036  -0.0400 148 PRO B CG  
2668 C CD  . PRO B 74  ? 0.7601 0.6648 0.7514 0.0017  0.2024  -0.0327 148 PRO B CD  
2669 N N   . LYS B 75  ? 0.8180 0.7426 0.8366 -0.0077 0.1376  -0.0196 149 LYS B N   
2670 C CA  . LYS B 75  ? 0.7204 0.6508 0.7335 -0.0153 0.1153  -0.0160 149 LYS B CA  
2671 C C   . LYS B 75  ? 0.7164 0.6795 0.7499 -0.0108 0.1009  -0.0032 149 LYS B C   
2672 O O   . LYS B 75  ? 0.7133 0.6783 0.7657 -0.0073 0.0847  0.0034  149 LYS B O   
2673 C CB  . LYS B 75  ? 0.8141 0.7425 0.7803 -0.0359 0.1130  -0.0267 149 LYS B CB  
2674 C CG  . LYS B 75  ? 0.9013 0.7904 0.8413 -0.0449 0.1270  -0.0416 149 LYS B CG  
2675 C CD  . LYS B 75  ? 1.0562 0.9472 0.9564 -0.0697 0.1212  -0.0534 149 LYS B CD  
2676 C CE  . LYS B 75  ? 1.1034 0.9548 0.9704 -0.0830 0.1389  -0.0717 149 LYS B CE  
2677 N NZ  . LYS B 75  ? 1.1427 0.9449 1.0204 -0.0721 0.1477  -0.0703 149 LYS B NZ  
2678 N N   . ASP B 76  ? 0.7419 0.7270 0.7672 -0.0100 0.1074  0.0007  150 ASP B N   
2679 C CA  . ASP B 76  ? 0.7532 0.7629 0.7961 -0.0040 0.0979  0.0132  150 ASP B CA  
2680 C C   . ASP B 76  ? 0.6823 0.6891 0.7745 0.0077  0.0975  0.0188  150 ASP B C   
2681 O O   . ASP B 76  ? 0.6415 0.6574 0.7523 0.0096  0.0814  0.0251  150 ASP B O   
2682 C CB  . ASP B 76  ? 0.7440 0.7693 0.7666 -0.0012 0.1096  0.0176  150 ASP B CB  
2683 C CG  . ASP B 76  ? 0.7910 0.8368 0.8228 0.0048  0.1012  0.0307  150 ASP B CG  
2684 O OD1 . ASP B 76  ? 0.8307 0.8853 0.8692 0.0017  0.0831  0.0336  150 ASP B OD1 
2685 O OD2 . ASP B 76  ? 0.8586 0.9078 0.8886 0.0128  0.1148  0.0382  150 ASP B OD2 
2686 N N   . ARG B 77  ? 0.6688 0.6646 0.7835 0.0151  0.1152  0.0150  151 ARG B N   
2687 C CA  . ARG B 77  ? 0.6272 0.6274 0.7954 0.0255  0.1150  0.0175  151 ARG B CA  
2688 C C   . ARG B 77  ? 0.6001 0.5931 0.7851 0.0292  0.0940  0.0165  151 ARG B C   
2689 O O   . ARG B 77  ? 0.5632 0.5689 0.7780 0.0334  0.0788  0.0211  151 ARG B O   
2690 C CB  . ARG B 77  ? 0.5519 0.5439 0.7418 0.0326  0.1401  0.0118  151 ARG B CB  
2691 C CG  . ARG B 77  ? 0.5620 0.5661 0.8142 0.0425  0.1414  0.0117  151 ARG B CG  
2692 C CD  . ARG B 77  ? 0.6250 0.6233 0.8990 0.0489  0.1702  0.0053  151 ARG B CD  
2693 N NE  . ARG B 77  ? 0.6483 0.6666 0.9895 0.0569  0.1730  0.0035  151 ARG B NE  
2694 C CZ  . ARG B 77  ? 0.6906 0.7141 1.0725 0.0685  0.1625  -0.0014 151 ARG B CZ  
2695 N NH1 . ARG B 77  ? 0.6990 0.7013 1.0577 0.0745  0.1516  -0.0034 151 ARG B NH1 
2696 N NH2 . ARG B 77  ? 0.6972 0.7477 1.1443 0.0744  0.1633  -0.0046 151 ARG B NH2 
2697 N N   . ALA B 78  ? 0.5914 0.5604 0.7530 0.0277  0.0934  0.0105  152 ALA B N   
2698 C CA  . ALA B 78  ? 0.5258 0.4803 0.6949 0.0336  0.0754  0.0113  152 ALA B CA  
2699 C C   . ALA B 78  ? 0.6022 0.5645 0.7554 0.0263  0.0536  0.0177  152 ALA B C   
2700 O O   . ALA B 78  ? 0.6038 0.5641 0.7737 0.0339  0.0359  0.0216  152 ALA B O   
2701 C CB  . ALA B 78  ? 0.6456 0.5647 0.7839 0.0318  0.0835  0.0040  152 ALA B CB  
2702 N N   . ARG B 79  ? 0.6465 0.6188 0.7666 0.0128  0.0544  0.0185  153 ARG B N   
2703 C CA  . ARG B 79  ? 0.5727 0.5545 0.6791 0.0063  0.0368  0.0242  153 ARG B CA  
2704 C C   . ARG B 79  ? 0.5708 0.5734 0.7093 0.0134  0.0281  0.0315  153 ARG B C   
2705 O O   . ARG B 79  ? 0.5664 0.5682 0.7097 0.0152  0.0108  0.0353  153 ARG B O   
2706 C CB  . ARG B 79  ? 0.6649 0.6592 0.7338 -0.0080 0.0405  0.0221  153 ARG B CB  
2707 C CG  . ARG B 79  ? 0.7779 0.7662 0.8188 -0.0201 0.0291  0.0208  153 ARG B CG  
2708 C CD  . ARG B 79  ? 0.8979 0.9110 0.9107 -0.0336 0.0311  0.0175  153 ARG B CD  
2709 N NE  . ARG B 79  ? 0.9146 0.9248 0.9057 -0.0423 0.0445  0.0066  153 ARG B NE  
2710 C CZ  . ARG B 79  ? 0.9055 0.9363 0.8895 -0.0402 0.0527  0.0059  153 ARG B CZ  
2711 N NH1 . ARG B 79  ? 0.8692 0.9231 0.8655 -0.0295 0.0509  0.0165  153 ARG B NH1 
2712 N NH2 . ARG B 79  ? 0.8302 0.8543 0.7900 -0.0490 0.0641  -0.0059 153 ARG B NH2 
2713 N N   . LYS B 80  ? 0.5736 0.5915 0.7319 0.0168  0.0416  0.0328  154 LYS B N   
2714 C CA  . LYS B 80  ? 0.5315 0.5654 0.7191 0.0207  0.0373  0.0381  154 LYS B CA  
2715 C C   . LYS B 80  ? 0.5316 0.5660 0.7642 0.0293  0.0281  0.0351  154 LYS B C   
2716 O O   . LYS B 80  ? 0.5307 0.5723 0.7784 0.0302  0.0122  0.0370  154 LYS B O   
2717 C CB  . LYS B 80  ? 0.5738 0.6176 0.7654 0.0212  0.0583  0.0408  154 LYS B CB  
2718 C CG  . LYS B 80  ? 0.6126 0.6623 0.7602 0.0164  0.0644  0.0453  154 LYS B CG  
2719 C CD  . LYS B 80  ? 0.6602 0.7136 0.8087 0.0207  0.0859  0.0503  154 LYS B CD  
2720 C CE  . LYS B 80  ? 0.7133 0.7728 0.8150 0.0202  0.0924  0.0542  154 LYS B CE  
2721 N NZ  . LYS B 80  ? 0.8112 0.8853 0.8925 0.0201  0.0779  0.0612  154 LYS B NZ  
2722 N N   . LEU B 81  ? 0.5078 0.5365 0.7625 0.0366  0.0373  0.0294  155 LEU B N   
2723 C CA  . LEU B 81  ? 0.5389 0.5746 0.8404 0.0477  0.0266  0.0257  155 LEU B CA  
2724 C C   . LEU B 81  ? 0.5827 0.6061 0.8713 0.0529  0.0005  0.0275  155 LEU B C   
2725 O O   . LEU B 81  ? 0.5764 0.6110 0.8990 0.0619  -0.0162 0.0257  155 LEU B O   
2726 C CB  . LEU B 81  ? 0.5260 0.5576 0.8519 0.0572  0.0431  0.0195  155 LEU B CB  
2727 C CG  . LEU B 81  ? 0.4683 0.5101 0.8152 0.0551  0.0718  0.0164  155 LEU B CG  
2728 C CD1 . LEU B 81  ? 0.5117 0.5478 0.8842 0.0669  0.0859  0.0095  155 LEU B CD1 
2729 C CD2 . LEU B 81  ? 0.4861 0.5531 0.8763 0.0521  0.0730  0.0161  155 LEU B CD2 
2730 N N   . ALA B 82  ? 0.5526 0.5531 0.7921 0.0472  -0.0029 0.0303  156 ALA B N   
2731 C CA  . ALA B 82  ? 0.5210 0.5023 0.7413 0.0522  -0.0238 0.0332  156 ALA B CA  
2732 C C   . ALA B 82  ? 0.5758 0.5703 0.8030 0.0512  -0.0442 0.0365  156 ALA B C   
2733 O O   . ALA B 82  ? 0.6495 0.6342 0.8753 0.0605  -0.0643 0.0380  156 ALA B O   
2734 C CB  . ALA B 82  ? 0.6152 0.5696 0.7813 0.0414  -0.0188 0.0344  156 ALA B CB  
2735 N N   . GLU B 83  ? 0.5442 0.5579 0.7754 0.0413  -0.0389 0.0377  157 GLU B N   
2736 C CA  . GLU B 83  ? 0.4970 0.5198 0.7331 0.0394  -0.0555 0.0394  157 GLU B CA  
2737 C C   . GLU B 83  ? 0.5567 0.5949 0.8402 0.0492  -0.0697 0.0338  157 GLU B C   
2738 O O   . GLU B 83  ? 0.5771 0.6145 0.8585 0.0520  -0.0917 0.0333  157 GLU B O   
2739 C CB  . GLU B 83  ? 0.5154 0.5524 0.7487 0.0294  -0.0430 0.0418  157 GLU B CB  
2740 C CG  . GLU B 83  ? 0.5605 0.6028 0.7977 0.0266  -0.0566 0.0423  157 GLU B CG  
2741 C CD  . GLU B 83  ? 0.6101 0.6571 0.8295 0.0192  -0.0440 0.0474  157 GLU B CD  
2742 O OE1 . GLU B 83  ? 0.6111 0.6610 0.8160 0.0172  -0.0266 0.0510  157 GLU B OE1 
2743 O OE2 . GLU B 83  ? 0.5947 0.6416 0.8126 0.0166  -0.0517 0.0476  157 GLU B OE2 
2744 N N   . VAL B 84  ? 0.5080 0.5624 0.8350 0.0540  -0.0575 0.0283  158 VAL B N   
2745 C CA  . VAL B 84  ? 0.4767 0.5536 0.8568 0.0634  -0.0711 0.0206  158 VAL B CA  
2746 C C   . VAL B 84  ? 0.5872 0.6516 0.9600 0.0804  -0.0931 0.0217  158 VAL B C   
2747 O O   . VAL B 84  ? 0.5765 0.6547 0.9709 0.0889  -0.1176 0.0178  158 VAL B O   
2748 C CB  . VAL B 84  ? 0.5029 0.6008 0.9327 0.0642  -0.0484 0.0142  158 VAL B CB  
2749 C CG1 . VAL B 84  ? 0.4953 0.6249 0.9883 0.0728  -0.0623 0.0040  158 VAL B CG1 
2750 C CG2 . VAL B 84  ? 0.4940 0.5967 0.9222 0.0491  -0.0254 0.0154  158 VAL B CG2 
2751 N N   . GLY B 85  ? 0.5964 0.6323 0.9352 0.0860  -0.0847 0.0267  159 GLY B N   
2752 C CA  . GLY B 85  ? 0.6085 0.6228 0.9316 0.1039  -0.1024 0.0300  159 GLY B CA  
2753 C C   . GLY B 85  ? 0.6029 0.5988 0.8846 0.1033  -0.1257 0.0356  159 GLY B C   
2754 O O   . GLY B 85  ? 0.6433 0.6345 0.9257 0.1202  -0.1493 0.0369  159 GLY B O   
2755 N N   . SER B 86  ? 0.6006 0.5864 0.8447 0.0853  -0.1193 0.0391  160 SER B N   
2756 C CA  . SER B 86  ? 0.5955 0.5613 0.7968 0.0832  -0.1371 0.0442  160 SER B CA  
2757 C C   . SER B 86  ? 0.6289 0.6186 0.8558 0.0858  -0.1599 0.0393  160 SER B C   
2758 O O   . SER B 86  ? 0.6657 0.6411 0.8692 0.0950  -0.1830 0.0417  160 SER B O   
2759 C CB  . SER B 86  ? 0.6245 0.5795 0.7859 0.0638  -0.1219 0.0480  160 SER B CB  
2760 O OG  . SER B 86  ? 0.5971 0.5315 0.7331 0.0590  -0.1031 0.0499  160 SER B OG  
2761 N N   . HIS B 87  ? 0.6337 0.6570 0.9049 0.0769  -0.1529 0.0319  161 HIS B N   
2762 C CA  . HIS B 87  ? 0.5856 0.6332 0.8867 0.0763  -0.1728 0.0236  161 HIS B CA  
2763 C C   . HIS B 87  ? 0.6224 0.6857 0.9560 0.0959  -0.1972 0.0182  161 HIS B C   
2764 O O   . HIS B 87  ? 0.7162 0.7879 1.0464 0.0968  -0.2182 0.0121  161 HIS B O   
2765 C CB  . HIS B 87  ? 0.5915 0.6681 0.9373 0.0625  -0.1552 0.0158  161 HIS B CB  
2766 C CG  . HIS B 87  ? 0.5232 0.5933 0.8452 0.0465  -0.1490 0.0168  161 HIS B CG  
2767 N ND1 . HIS B 87  ? 0.5236 0.6010 0.8516 0.0411  -0.1659 0.0092  161 HIS B ND1 
2768 C CD2 . HIS B 87  ? 0.5202 0.5777 0.8127 0.0363  -0.1275 0.0240  161 HIS B CD2 
2769 C CE1 . HIS B 87  ? 0.5308 0.5963 0.8329 0.0287  -0.1529 0.0124  161 HIS B CE1 
2770 N NE2 . HIS B 87  ? 0.5588 0.6143 0.8404 0.0269  -0.1303 0.0220  161 HIS B NE2 
2771 N N   . GLU B 88  ? 0.6460 0.7120 1.0021 0.1097  -0.1893 0.0192  162 GLU B N   
2772 C CA  . GLU B 88  ? 0.5921 0.6734 0.9670 0.1266  -0.2031 0.0139  162 GLU B CA  
2773 C C   . GLU B 88  ? 0.6420 0.6873 0.9614 0.1437  -0.2198 0.0237  162 GLU B C   
2774 O O   . GLU B 88  ? 0.7116 0.7692 1.0347 0.1575  -0.2382 0.0207  162 GLU B O   
2775 C CB  . GLU B 88  ? 0.5817 0.6808 1.0029 0.1349  -0.1840 0.0105  162 GLU B CB  
2776 C CG  . GLU B 88  ? 0.6912 0.8254 1.1672 0.1180  -0.1644 0.0003  162 GLU B CG  
2777 C CD  . GLU B 88  ? 0.8327 0.9864 1.3545 0.1259  -0.1445 -0.0047 162 GLU B CD  
2778 O OE1 . GLU B 88  ? 0.9144 1.0478 1.4218 0.1436  -0.1407 0.0015  162 GLU B OE1 
2779 O OE2 . GLU B 88  ? 0.7004 0.8858 1.2700 0.1142  -0.1307 -0.0151 162 GLU B OE2 
2780 N N   . LYS B 89  ? 0.7117 0.7122 0.9792 0.1430  -0.2125 0.0354  163 LYS B N   
2781 C CA  . LYS B 89  ? 0.6920 0.6505 0.8984 0.1556  -0.2241 0.0454  163 LYS B CA  
2782 C C   . LYS B 89  ? 0.7099 0.6629 0.8805 0.1478  -0.2418 0.0448  163 LYS B C   
2783 O O   . LYS B 89  ? 0.7911 0.7211 0.9211 0.1603  -0.2550 0.0502  163 LYS B O   
2784 C CB  . LYS B 89  ? 0.7010 0.6090 0.8618 0.1533  -0.2073 0.0565  163 LYS B CB  
2785 C CG  . LYS B 89  ? 0.7327 0.6294 0.9103 0.1659  -0.1902 0.0578  163 LYS B CG  
2786 C CD  . LYS B 89  ? 0.8111 0.6666 0.9408 0.1497  -0.1618 0.0624  163 LYS B CD  
2787 C CE  . LYS B 89  ? 0.8396 0.6844 0.9855 0.1585  -0.1407 0.0606  163 LYS B CE  
2788 N NZ  . LYS B 89  ? 0.9053 0.7270 1.0188 0.1353  -0.1114 0.0593  163 LYS B NZ  
2789 N N   . VAL B 90  ? 0.7228 0.6941 0.9063 0.1283  -0.2404 0.0388  164 VAL B N   
2790 C CA  . VAL B 90  ? 0.7366 0.7036 0.8901 0.1205  -0.2555 0.0360  164 VAL B CA  
2791 C C   . VAL B 90  ? 0.7577 0.7618 0.9476 0.1254  -0.2748 0.0233  164 VAL B C   
2792 O O   . VAL B 90  ? 0.8291 0.8243 0.9878 0.1313  -0.2935 0.0223  164 VAL B O   
2793 C CB  . VAL B 90  ? 0.6718 0.6405 0.8230 0.0992  -0.2448 0.0352  164 VAL B CB  
2794 C CG1 . VAL B 90  ? 0.6988 0.6687 0.8307 0.0911  -0.2595 0.0288  164 VAL B CG1 
2795 C CG2 . VAL B 90  ? 0.6542 0.5856 0.7580 0.0930  -0.2274 0.0475  164 VAL B CG2 
2796 N N   . GLY B 91  ? 0.7096 0.7557 0.9652 0.1221  -0.2697 0.0129  165 GLY B N   
2797 C CA  . GLY B 91  ? 0.6770 0.7615 0.9708 0.1236  -0.2870 -0.0010 165 GLY B CA  
2798 C C   . GLY B 91  ? 0.6940 0.7841 0.9823 0.1053  -0.2952 -0.0105 165 GLY B C   
2799 O O   . GLY B 91  ? 0.8145 0.8886 1.0867 0.0901  -0.2832 -0.0077 165 GLY B O   
2800 N N   . GLN B 92  ? 0.6975 0.8113 0.9990 0.1078  -0.3166 -0.0221 166 GLN B N   
2801 C CA  . GLN B 92  ? 0.6855 0.8077 0.9871 0.0906  -0.3260 -0.0347 166 GLN B CA  
2802 C C   . GLN B 92  ? 0.6961 0.7827 0.9277 0.0956  -0.3428 -0.0291 166 GLN B C   
2803 O O   . GLN B 92  ? 0.6900 0.7723 0.8979 0.1133  -0.3605 -0.0257 166 GLN B O   
2804 C CB  . GLN B 92  ? 0.6553 0.8267 1.0146 0.0872  -0.3384 -0.0532 166 GLN B CB  
2805 C CG  . GLN B 92  ? 0.7092 0.9154 1.1378 0.0822  -0.3189 -0.0594 166 GLN B CG  
2806 C CD  . GLN B 92  ? 0.8575 1.1127 1.3442 0.0734  -0.3276 -0.0796 166 GLN B CD  
2807 O OE1 . GLN B 92  ? 0.8611 1.1381 1.3977 0.0560  -0.3083 -0.0900 166 GLN B OE1 
2808 N NE2 . GLN B 92  ? 0.8419 1.1144 1.3213 0.0847  -0.3557 -0.0852 166 GLN B NE2 
2809 N N   . HIS B 93  ? 0.6971 0.7575 0.8949 0.0809  -0.3359 -0.0276 167 HIS B N   
2810 C CA  . HIS B 93  ? 0.7273 0.7523 0.8582 0.0827  -0.3477 -0.0237 167 HIS B CA  
2811 C C   . HIS B 93  ? 0.7310 0.7521 0.8586 0.0615  -0.3439 -0.0332 167 HIS B C   
2812 O O   . HIS B 93  ? 0.6687 0.6937 0.8210 0.0488  -0.3254 -0.0324 167 HIS B O   
2813 C CB  . HIS B 93  ? 0.7822 0.7611 0.8540 0.0914  -0.3360 -0.0045 167 HIS B CB  
2814 C CG  . HIS B 93  ? 0.7945 0.7347 0.7961 0.0941  -0.3446 0.0000  167 HIS B CG  
2815 N ND1 . HIS B 93  ? 0.7899 0.7041 0.7538 0.0800  -0.3358 0.0010  167 HIS B ND1 
2816 C CD2 . HIS B 93  ? 0.8292 0.7515 0.7904 0.1100  -0.3597 0.0042  167 HIS B CD2 
2817 C CE1 . HIS B 93  ? 0.8185 0.6997 0.7222 0.0860  -0.3435 0.0048  167 HIS B CE1 
2818 N NE2 . HIS B 93  ? 0.8906 0.7754 0.7909 0.1041  -0.3583 0.0070  167 HIS B NE2 
2819 N N   . PRO B 94  ? 0.7608 0.7731 0.8570 0.0579  -0.3606 -0.0422 168 PRO B N   
2820 C CA  . PRO B 94  ? 0.7224 0.7312 0.8184 0.0369  -0.3575 -0.0545 168 PRO B CA  
2821 C C   . PRO B 94  ? 0.7385 0.7130 0.8006 0.0284  -0.3378 -0.0433 168 PRO B C   
2822 O O   . PRO B 94  ? 0.8436 0.8157 0.9134 0.0110  -0.3316 -0.0529 168 PRO B O   
2823 C CB  . PRO B 94  ? 0.7386 0.7357 0.7916 0.0387  -0.3793 -0.0633 168 PRO B CB  
2824 C CG  . PRO B 94  ? 0.7803 0.7961 0.8398 0.0587  -0.3974 -0.0610 168 PRO B CG  
2825 C CD  . PRO B 94  ? 0.7025 0.7090 0.7643 0.0728  -0.3833 -0.0428 168 PRO B CD  
2826 N N   . CYS B 95  ? 0.7828 0.7306 0.8079 0.0389  -0.3268 -0.0244 169 CYS B N   
2827 C CA  . CYS B 95  ? 0.7204 0.6402 0.7123 0.0311  -0.3082 -0.0134 169 CYS B CA  
2828 C C   . CYS B 95  ? 0.6672 0.5981 0.6889 0.0313  -0.2830 -0.0018 169 CYS B C   
2829 O O   . CYS B 95  ? 0.7324 0.6439 0.7255 0.0267  -0.2585 0.0094  169 CYS B O   
2830 C CB  . CYS B 95  ? 0.7672 0.6431 0.6832 0.0381  -0.3062 -0.0021 169 CYS B CB  
2831 S SG  . CYS B 95  ? 0.9219 0.7795 0.7929 0.0383  -0.3265 -0.0144 169 CYS B SG  
2832 N N   . CYS B 96  ? 0.6214 0.5850 0.7001 0.0361  -0.2864 -0.0053 170 CYS B N   
2833 C CA  . CYS B 96  ? 0.6306 0.6052 0.7380 0.0350  -0.2600 0.0034  170 CYS B CA  
2834 C C   . CYS B 96  ? 0.6293 0.6385 0.8017 0.0245  -0.2487 -0.0079 170 CYS B C   
2835 O O   . CYS B 96  ? 0.6542 0.6896 0.8670 0.0238  -0.2674 -0.0224 170 CYS B O   
2836 C CB  . CYS B 96  ? 0.7389 0.7129 0.8493 0.0521  -0.2679 0.0118  170 CYS B CB  
2837 S SG  . CYS B 96  ? 0.7824 0.7086 0.8134 0.0636  -0.2721 0.0249  170 CYS B SG  
2838 N N   . VAL B 97  ? 0.6096 0.6194 0.7916 0.0162  -0.2178 -0.0016 171 VAL B N   
2839 C CA  . VAL B 97  ? 0.5820 0.6172 0.8193 0.0064  -0.2015 -0.0100 171 VAL B CA  
2840 C C   . VAL B 97  ? 0.6374 0.7032 0.9279 0.0143  -0.2104 -0.0156 171 VAL B C   
2841 O O   . VAL B 97  ? 0.6343 0.6982 0.9205 0.0264  -0.2089 -0.0062 171 VAL B O   
2842 C CB  . VAL B 97  ? 0.5434 0.5708 0.7730 0.0013  -0.1677 0.0010  171 VAL B CB  
2843 C CG1 . VAL B 97  ? 0.5752 0.6217 0.8557 -0.0079 -0.1480 -0.0061 171 VAL B CG1 
2844 C CG2 . VAL B 97  ? 0.5552 0.5566 0.7364 -0.0035 -0.1586 0.0066  171 VAL B CG2 
2845 N N   . ARG B 98  ? 0.5380 0.6323 0.8805 0.0069  -0.2182 -0.0323 172 ARG B N   
2846 C CA  . ARG B 98  ? 0.5104 0.6409 0.9114 0.0149  -0.2278 -0.0401 172 ARG B CA  
2847 C C   . ARG B 98  ? 0.5106 0.6553 0.9546 0.0080  -0.1947 -0.0391 172 ARG B C   
2848 O O   . ARG B 98  ? 0.5714 0.7137 1.0278 -0.0084 -0.1723 -0.0436 172 ARG B O   
2849 C CB  . ARG B 98  ? 0.5468 0.7021 0.9759 0.0093  -0.2476 -0.0598 172 ARG B CB  
2850 C CG  . ARG B 98  ? 0.6312 0.8209 1.1069 0.0183  -0.2495 -0.0672 172 ARG B CG  
2851 C CD  . ARG B 98  ? 0.6073 0.8263 1.1129 0.0092  -0.2646 -0.0877 172 ARG B CD  
2852 N NE  . ARG B 98  ? 0.6800 0.9051 1.2168 -0.0160 -0.2459 -0.1008 172 ARG B NE  
2853 C CZ  . ARG B 98  ? 0.7842 0.9941 1.2996 -0.0317 -0.2520 -0.1099 172 ARG B CZ  
2854 N NH1 . ARG B 98  ? 0.7759 0.9659 1.2382 -0.0248 -0.2775 -0.1080 172 ARG B NH1 
2855 N NH2 . ARG B 98  ? 0.7339 0.9439 1.2780 -0.0550 -0.2291 -0.1211 172 ARG B NH2 
2856 N N   . LEU B 99  ? 0.5018 0.6568 0.9644 0.0214  -0.1898 -0.0329 173 LEU B N   
2857 C CA  . LEU B 99  ? 0.4686 0.6364 0.9699 0.0171  -0.1588 -0.0323 173 LEU B CA  
2858 C C   . LEU B 99  ? 0.4635 0.6679 1.0267 0.0150  -0.1599 -0.0487 173 LEU B C   
2859 O O   . LEU B 99  ? 0.4612 0.6784 1.0291 0.0291  -0.1785 -0.0521 173 LEU B O   
2860 C CB  . LEU B 99  ? 0.4770 0.6305 0.9559 0.0312  -0.1478 -0.0182 173 LEU B CB  
2861 C CG  . LEU B 99  ? 0.4725 0.6370 0.9860 0.0295  -0.1164 -0.0175 173 LEU B CG  
2862 C CD1 . LEU B 99  ? 0.4263 0.5711 0.9133 0.0164  -0.0860 -0.0099 173 LEU B CD1 
2863 C CD2 . LEU B 99  ? 0.4619 0.6191 0.9658 0.0461  -0.1140 -0.0097 173 LEU B CD2 
2864 N N   . GLU B 100 ? 0.4599 0.6758 1.0609 -0.0026 -0.1359 -0.0577 174 GLU B N   
2865 C CA  . GLU B 100 ? 0.4074 0.6540 1.0606 -0.0082 -0.1293 -0.0736 174 GLU B CA  
2866 C C   . GLU B 100 ? 0.3654 0.6213 1.0448 0.0002  -0.1062 -0.0695 174 GLU B C   
2867 O O   . GLU B 100 ? 0.4054 0.6868 1.1150 0.0093  -0.1140 -0.0770 174 GLU B O   
2868 C CB  . GLU B 100 ? 0.4516 0.6990 1.1280 -0.0326 -0.1098 -0.0856 174 GLU B CB  
2869 C CG  . GLU B 100 ? 0.5728 0.8146 1.2311 -0.0435 -0.1320 -0.0955 174 GLU B CG  
2870 C CD  . GLU B 100 ? 0.6732 0.9458 1.3505 -0.0404 -0.1618 -0.1115 174 GLU B CD  
2871 O OE1 . GLU B 100 ? 0.5961 0.9004 1.3195 -0.0398 -0.1563 -0.1212 174 GLU B OE1 
2872 O OE2 . GLU B 100 ? 0.7223 0.9877 1.3666 -0.0382 -0.1904 -0.1142 174 GLU B OE2 
2873 N N   . GLN B 101 ? 0.4376 0.6739 1.1050 -0.0023 -0.0772 -0.0576 175 GLN B N   
2874 C CA  . GLN B 101 ? 0.3930 0.6340 1.0818 0.0025  -0.0501 -0.0551 175 GLN B CA  
2875 C C   . GLN B 101 ? 0.3691 0.5837 1.0233 0.0056  -0.0286 -0.0381 175 GLN B C   
2876 O O   . GLN B 101 ? 0.3685 0.5612 0.9848 -0.0006 -0.0265 -0.0294 175 GLN B O   
2877 C CB  . GLN B 101 ? 0.3098 0.5641 1.0410 -0.0138 -0.0240 -0.0677 175 GLN B CB  
2878 C CG  . GLN B 101 ? 0.4090 0.6697 1.1639 -0.0086 0.0019  -0.0676 175 GLN B CG  
2879 C CD  . GLN B 101 ? 0.4885 0.7688 1.2903 -0.0226 0.0192  -0.0833 175 GLN B CD  
2880 O OE1 . GLN B 101 ? 0.5638 0.8504 1.3789 -0.0382 0.0148  -0.0944 175 GLN B OE1 
2881 N NE2 . GLN B 101 ? 0.6203 0.9095 1.4471 -0.0181 0.0401  -0.0853 175 GLN B NE2 
2882 N N   . ALA B 102 ? 0.3456 0.5589 1.0034 0.0158  -0.0120 -0.0336 176 ALA B N   
2883 C CA  . ALA B 102 ? 0.3417 0.5314 0.9652 0.0179  0.0126  -0.0197 176 ALA B CA  
2884 C C   . ALA B 102 ? 0.3657 0.5591 1.0124 0.0197  0.0429  -0.0223 176 ALA B C   
2885 O O   . ALA B 102 ? 0.3851 0.5962 1.0642 0.0260  0.0378  -0.0317 176 ALA B O   
2886 C CB  . ALA B 102 ? 0.3783 0.5459 0.9460 0.0308  -0.0062 -0.0088 176 ALA B CB  
2887 N N   . TRP B 103 ? 0.3644 0.5387 0.9876 0.0148  0.0747  -0.0136 177 TRP B N   
2888 C CA  . TRP B 103 ? 0.3903 0.5597 1.0218 0.0160  0.1058  -0.0151 177 TRP B CA  
2889 C C   . TRP B 103 ? 0.3992 0.5408 0.9785 0.0166  0.1308  -0.0017 177 TRP B C   
2890 O O   . TRP B 103 ? 0.3724 0.4948 0.9012 0.0132  0.1243  0.0082  177 TRP B O   
2891 C CB  . TRP B 103 ? 0.4175 0.5940 1.0842 0.0026  0.1242  -0.0258 177 TRP B CB  
2892 C CG  . TRP B 103 ? 0.4125 0.5700 1.0613 -0.0119 0.1431  -0.0214 177 TRP B CG  
2893 C CD1 . TRP B 103 ? 0.3879 0.5181 1.0085 -0.0164 0.1788  -0.0132 177 TRP B CD1 
2894 C CD2 . TRP B 103 ? 0.3877 0.5476 1.0414 -0.0225 0.1282  -0.0247 177 TRP B CD2 
2895 N NE1 . TRP B 103 ? 0.4134 0.5271 1.0202 -0.0275 0.1878  -0.0100 177 TRP B NE1 
2896 C CE2 . TRP B 103 ? 0.3799 0.5116 1.0087 -0.0326 0.1582  -0.0176 177 TRP B CE2 
2897 C CE3 . TRP B 103 ? 0.3663 0.5457 1.0376 -0.0236 0.0927  -0.0329 177 TRP B CE3 
2898 C CZ2 . TRP B 103 ? 0.3943 0.5163 1.0190 -0.0444 0.1558  -0.0189 177 TRP B CZ2 
2899 C CZ3 . TRP B 103 ? 0.3198 0.4917 0.9870 -0.0368 0.0891  -0.0354 177 TRP B CZ3 
2900 C CH2 . TRP B 103 ? 0.3614 0.5045 1.0074 -0.0475 0.1215  -0.0287 177 TRP B CH2 
2901 N N   . GLU B 104 ? 0.4068 0.5416 0.9854 0.0211  0.1566  -0.0019 178 GLU B N   
2902 C CA  . GLU B 104 ? 0.4689 0.5754 0.9895 0.0218  0.1801  0.0091  178 GLU B CA  
2903 C C   . GLU B 104 ? 0.4820 0.5774 1.0098 0.0159  0.2168  0.0074  178 GLU B C   
2904 O O   . GLU B 104 ? 0.5147 0.6197 1.0809 0.0150  0.2230  -0.0032 178 GLU B O   
2905 C CB  . GLU B 104 ? 0.4663 0.5612 0.9514 0.0327  0.1735  0.0107  178 GLU B CB  
2906 C CG  . GLU B 104 ? 0.6085 0.7116 1.1328 0.0410  0.1887  0.0013  178 GLU B CG  
2907 C CD  . GLU B 104 ? 0.6758 0.7593 1.1586 0.0503  0.1846  0.0022  178 GLU B CD  
2908 O OE1 . GLU B 104 ? 0.6912 0.7529 1.1105 0.0467  0.1855  0.0094  178 GLU B OE1 
2909 O OE2 . GLU B 104 ? 0.6653 0.7556 1.1796 0.0614  0.1807  -0.0050 178 GLU B OE2 
2910 N N   . GLU B 105 ? 0.4911 0.5621 0.9728 0.0125  0.2380  0.0184  179 GLU B N   
2911 C CA  . GLU B 105 ? 0.5819 0.6297 1.0498 0.0082  0.2708  0.0193  179 GLU B CA  
2912 C C   . GLU B 105 ? 0.6310 0.6512 1.0278 0.0139  0.2876  0.0339  179 GLU B C   
2913 O O   . GLU B 105 ? 0.6249 0.6399 0.9887 0.0153  0.2802  0.0449  179 GLU B O   
2914 C CB  . GLU B 105 ? 0.6463 0.6898 1.1398 -0.0039 0.2790  0.0154  179 GLU B CB  
2915 C CG  . GLU B 105 ? 0.7154 0.7352 1.2047 -0.0087 0.3129  0.0136  179 GLU B CG  
2916 C CD  . GLU B 105 ? 0.7737 0.7875 1.2898 -0.0218 0.3225  0.0075  179 GLU B CD  
2917 O OE1 . GLU B 105 ? 0.8541 0.8711 1.3708 -0.0262 0.3076  0.0095  179 GLU B OE1 
2918 O OE2 . GLU B 105 ? 0.8452 0.8502 1.3819 -0.0284 0.3462  -0.0002 179 GLU B OE2 
2919 N N   . GLY B 106 ? 0.6448 0.6481 1.0162 0.0180  0.3088  0.0336  180 GLY B N   
2920 C CA  . GLY B 106 ? 0.6831 0.6613 0.9821 0.0246  0.3223  0.0458  180 GLY B CA  
2921 C C   . GLY B 106 ? 0.7558 0.7446 1.0190 0.0311  0.3038  0.0516  180 GLY B C   
2922 O O   . GLY B 106 ? 0.8248 0.7995 1.0268 0.0360  0.3034  0.0632  180 GLY B O   
2923 N N   . GLY B 107 ? 0.7273 0.7346 1.0148 0.0314  0.2763  0.0424  181 GLY B N   
2924 C CA  . GLY B 107 ? 0.6790 0.6888 0.9234 0.0338  0.2466  0.0448  181 GLY B CA  
2925 C C   . GLY B 107 ? 0.6532 0.6730 0.8940 0.0318  0.2195  0.0512  181 GLY B C   
2926 O O   . GLY B 107 ? 0.6510 0.6750 0.8578 0.0325  0.1961  0.0530  181 GLY B O   
2927 N N   . ILE B 108 ? 0.5924 0.6153 0.8672 0.0280  0.2237  0.0534  182 ILE B N   
2928 C CA  . ILE B 108 ? 0.5752 0.6048 0.8501 0.0257  0.2004  0.0579  182 ILE B CA  
2929 C C   . ILE B 108 ? 0.4989 0.5476 0.8284 0.0216  0.1777  0.0468  182 ILE B C   
2930 O O   . ILE B 108 ? 0.5265 0.5852 0.9081 0.0194  0.1874  0.0371  182 ILE B O   
2931 C CB  . ILE B 108 ? 0.6058 0.6209 0.8775 0.0237  0.2207  0.0665  182 ILE B CB  
2932 C CG1 . ILE B 108 ? 0.6025 0.5961 0.8156 0.0319  0.2437  0.0792  182 ILE B CG1 
2933 C CG2 . ILE B 108 ? 0.5775 0.5959 0.8446 0.0223  0.1982  0.0706  182 ILE B CG2 
2934 C CD1 . ILE B 108 ? 0.6875 0.6843 0.8443 0.0404  0.2229  0.0891  182 ILE B CD1 
2935 N N   . LEU B 109 ? 0.4845 0.5397 0.8022 0.0216  0.1478  0.0482  183 LEU B N   
2936 C CA  . LEU B 109 ? 0.4383 0.5086 0.7965 0.0200  0.1226  0.0392  183 LEU B CA  
2937 C C   . LEU B 109 ? 0.4380 0.5109 0.8097 0.0139  0.1129  0.0398  183 LEU B C   
2938 O O   . LEU B 109 ? 0.4742 0.5382 0.8070 0.0142  0.1054  0.0484  183 LEU B O   
2939 C CB  . LEU B 109 ? 0.4603 0.5301 0.7909 0.0241  0.0972  0.0392  183 LEU B CB  
2940 C CG  . LEU B 109 ? 0.4395 0.5196 0.7995 0.0252  0.0690  0.0329  183 LEU B CG  
2941 C CD1 . LEU B 109 ? 0.4589 0.5517 0.8714 0.0306  0.0708  0.0228  183 LEU B CD1 
2942 C CD2 . LEU B 109 ? 0.4046 0.4757 0.7247 0.0272  0.0469  0.0361  183 LEU B CD2 
2943 N N   . TYR B 110 ? 0.4169 0.5036 0.8448 0.0082  0.1130  0.0293  184 TYR B N   
2944 C CA  . TYR B 110 ? 0.3985 0.4877 0.8446 -0.0005 0.1041  0.0256  184 TYR B CA  
2945 C C   . TYR B 110 ? 0.4105 0.5175 0.8798 0.0006  0.0687  0.0165  184 TYR B C   
2946 O O   . TYR B 110 ? 0.4565 0.5824 0.9636 0.0055  0.0594  0.0078  184 TYR B O   
2947 C CB  . TYR B 110 ? 0.4273 0.5205 0.9208 -0.0112 0.1303  0.0175  184 TYR B CB  
2948 C CG  . TYR B 110 ? 0.4489 0.5180 0.9157 -0.0118 0.1683  0.0276  184 TYR B CG  
2949 C CD1 . TYR B 110 ? 0.4387 0.5055 0.9011 -0.0059 0.1892  0.0298  184 TYR B CD1 
2950 C CD2 . TYR B 110 ? 0.4796 0.5242 0.9210 -0.0166 0.1843  0.0354  184 TYR B CD2 
2951 C CE1 . TYR B 110 ? 0.5138 0.5556 0.9449 -0.0050 0.2238  0.0397  184 TYR B CE1 
2952 C CE2 . TYR B 110 ? 0.5395 0.5575 0.9500 -0.0140 0.2192  0.0467  184 TYR B CE2 
2953 C CZ  . TYR B 110 ? 0.5465 0.5637 0.9509 -0.0082 0.2382  0.0489  184 TYR B CZ  
2954 O OH  . TYR B 110 ? 0.7173 0.7048 1.0832 -0.0041 0.2720  0.0606  184 TYR B OH  
2955 N N   . LEU B 111 ? 0.4230 0.5226 0.8683 -0.0021 0.0499  0.0188  185 LEU B N   
2956 C CA  . LEU B 111 ? 0.3685 0.4798 0.8270 -0.0013 0.0165  0.0109  185 LEU B CA  
2957 C C   . LEU B 111 ? 0.4122 0.5241 0.8885 -0.0134 0.0132  0.0028  185 LEU B C   
2958 O O   . LEU B 111 ? 0.4694 0.5601 0.9113 -0.0176 0.0227  0.0100  185 LEU B O   
2959 C CB  . LEU B 111 ? 0.4066 0.5040 0.8116 0.0060  -0.0035 0.0201  185 LEU B CB  
2960 C CG  . LEU B 111 ? 0.4736 0.5728 0.8714 0.0166  -0.0159 0.0211  185 LEU B CG  
2961 C CD1 . LEU B 111 ? 0.5006 0.5959 0.8914 0.0196  0.0090  0.0256  185 LEU B CD1 
2962 C CD2 . LEU B 111 ? 0.5530 0.6364 0.9006 0.0197  -0.0351 0.0280  185 LEU B CD2 
2963 N N   . GLN B 112 ? 0.4124 0.5492 0.9420 -0.0186 -0.0006 -0.0130 186 GLN B N   
2964 C CA  . GLN B 112 ? 0.4122 0.5525 0.9632 -0.0331 -0.0064 -0.0253 186 GLN B CA  
2965 C C   . GLN B 112 ? 0.4466 0.5932 0.9856 -0.0290 -0.0459 -0.0309 186 GLN B C   
2966 O O   . GLN B 112 ? 0.4872 0.6575 1.0510 -0.0195 -0.0697 -0.0371 186 GLN B O   
2967 C CB  . GLN B 112 ? 0.3903 0.5589 1.0135 -0.0449 0.0064  -0.0424 186 GLN B CB  
2968 C CG  . GLN B 112 ? 0.4281 0.6049 1.0807 -0.0634 -0.0013 -0.0601 186 GLN B CG  
2969 C CD  . GLN B 112 ? 0.4544 0.6505 1.1547 -0.0737 0.0143  -0.0766 186 GLN B CD  
2970 O OE1 . GLN B 112 ? 0.4607 0.6664 1.1794 -0.0669 0.0305  -0.0750 186 GLN B OE1 
2971 N NE2 . GLN B 112 ? 0.4059 0.6058 1.1223 -0.0904 0.0102  -0.0933 186 GLN B NE2 
2972 N N   . THR B 113 ? 0.4615 0.5849 0.9596 -0.0342 -0.0520 -0.0282 187 THR B N   
2973 C CA  . THR B 113 ? 0.4728 0.5960 0.9509 -0.0313 -0.0868 -0.0334 187 THR B CA  
2974 C C   . THR B 113 ? 0.4974 0.6173 0.9862 -0.0480 -0.0906 -0.0483 187 THR B C   
2975 O O   . THR B 113 ? 0.5548 0.6658 1.0595 -0.0620 -0.0636 -0.0525 187 THR B O   
2976 C CB  . THR B 113 ? 0.5038 0.5990 0.9145 -0.0214 -0.0923 -0.0170 187 THR B CB  
2977 O OG1 . THR B 113 ? 0.5679 0.6381 0.9477 -0.0277 -0.0688 -0.0093 187 THR B OG1 
2978 C CG2 . THR B 113 ? 0.4862 0.5822 0.8838 -0.0081 -0.0877 -0.0046 187 THR B CG2 
2979 N N   . GLU B 114 ? 0.4806 0.6042 0.9569 -0.0467 -0.1236 -0.0568 188 GLU B N   
2980 C CA  . GLU B 114 ? 0.4892 0.6029 0.9621 -0.0630 -0.1288 -0.0713 188 GLU B CA  
2981 C C   . GLU B 114 ? 0.6104 0.6816 1.0296 -0.0657 -0.1051 -0.0587 188 GLU B C   
2982 O O   . GLU B 114 ? 0.6675 0.7213 1.0427 -0.0525 -0.0991 -0.0399 188 GLU B O   
2983 C CB  . GLU B 114 ? 0.4727 0.5941 0.9295 -0.0582 -0.1700 -0.0809 188 GLU B CB  
2984 C CG  . GLU B 114 ? 0.5947 0.6873 0.9828 -0.0426 -0.1814 -0.0633 188 GLU B CG  
2985 C CD  . GLU B 114 ? 0.6763 0.7691 1.0399 -0.0376 -0.2197 -0.0718 188 GLU B CD  
2986 O OE1 . GLU B 114 ? 0.7176 0.8167 1.0938 -0.0512 -0.2324 -0.0910 188 GLU B OE1 
2987 O OE2 . GLU B 114 ? 0.7154 0.7999 1.0445 -0.0204 -0.2364 -0.0599 188 GLU B OE2 
2988 N N   . LEU B 115 ? 0.5693 0.6247 0.9938 -0.0830 -0.0907 -0.0701 189 LEU B N   
2989 C CA  . LEU B 115 ? 0.6145 0.6280 0.9894 -0.0833 -0.0675 -0.0588 189 LEU B CA  
2990 C C   . LEU B 115 ? 0.6275 0.6225 0.9540 -0.0805 -0.0907 -0.0608 189 LEU B C   
2991 O O   . LEU B 115 ? 0.5875 0.5883 0.9234 -0.0916 -0.1126 -0.0802 189 LEU B O   
2992 C CB  . LEU B 115 ? 0.6587 0.6543 1.0552 -0.1021 -0.0372 -0.0691 189 LEU B CB  
2993 C CG  . LEU B 115 ? 0.6354 0.5846 0.9843 -0.0988 -0.0061 -0.0549 189 LEU B CG  
2994 C CD1 . LEU B 115 ? 0.6047 0.5503 0.9281 -0.0788 0.0100  -0.0295 189 LEU B CD1 
2995 C CD2 . LEU B 115 ? 0.7014 0.6288 1.0740 -0.1180 0.0259  -0.0658 189 LEU B CD2 
2996 N N   . CYS B 116 ? 0.6467 0.6216 0.9219 -0.0661 -0.0861 -0.0420 190 CYS B N   
2997 C CA  . CYS B 116 ? 0.6569 0.6084 0.8807 -0.0629 -0.0997 -0.0416 190 CYS B CA  
2998 C C   . CYS B 116 ? 0.7145 0.6301 0.9066 -0.0643 -0.0703 -0.0351 190 CYS B C   
2999 O O   . CYS B 116 ? 0.7495 0.6563 0.9583 -0.0678 -0.0414 -0.0316 190 CYS B O   
3000 C CB  . CYS B 116 ? 0.6649 0.6208 0.8558 -0.0465 -0.1147 -0.0265 190 CYS B CB  
3001 S SG  . CYS B 116 ? 0.7020 0.6909 0.9210 -0.0398 -0.1478 -0.0313 190 CYS B SG  
3002 N N   . GLY B 117 ? 0.7395 0.6314 0.8830 -0.0598 -0.0757 -0.0327 191 GLY B N   
3003 C CA  . GLY B 117 ? 0.6817 0.5401 0.7925 -0.0563 -0.0481 -0.0248 191 GLY B CA  
3004 C C   . GLY B 117 ? 0.7111 0.5741 0.8016 -0.0378 -0.0327 -0.0013 191 GLY B C   
3005 O O   . GLY B 117 ? 0.7008 0.5901 0.8102 -0.0316 -0.0354 0.0076  191 GLY B O   
3006 N N   . PRO B 118 ? 0.7313 0.5705 0.7835 -0.0285 -0.0163 0.0077  192 PRO B N   
3007 C CA  . PRO B 118 ? 0.6877 0.5380 0.7224 -0.0106 -0.0037 0.0282  192 PRO B CA  
3008 C C   . PRO B 118 ? 0.6377 0.5093 0.6582 -0.0061 -0.0252 0.0327  192 PRO B C   
3009 O O   . PRO B 118 ? 0.6792 0.5465 0.6882 -0.0128 -0.0473 0.0227  192 PRO B O   
3010 C CB  . PRO B 118 ? 0.6850 0.5047 0.6851 -0.0019 0.0172  0.0333  192 PRO B CB  
3011 C CG  . PRO B 118 ? 0.7385 0.5326 0.7238 -0.0155 0.0053  0.0150  192 PRO B CG  
3012 C CD  . PRO B 118 ? 0.7537 0.5559 0.7777 -0.0335 -0.0079 -0.0016 192 PRO B CD  
3013 N N   . SER B 119 ? 0.6075 0.5001 0.6258 0.0053  -0.0177 0.0476  193 SER B N   
3014 C CA  . SER B 119 ? 0.6013 0.5098 0.6028 0.0081  -0.0321 0.0519  193 SER B CA  
3015 C C   . SER B 119 ? 0.5817 0.4738 0.5447 0.0119  -0.0289 0.0531  193 SER B C   
3016 O O   . SER B 119 ? 0.6373 0.5116 0.5870 0.0174  -0.0117 0.0546  193 SER B O   
3017 C CB  . SER B 119 ? 0.5367 0.4733 0.5459 0.0166  -0.0238 0.0647  193 SER B CB  
3018 O OG  . SER B 119 ? 0.5671 0.5068 0.5580 0.0286  -0.0059 0.0751  193 SER B OG  
3019 N N   . LEU B 120 ? 0.5966 0.4918 0.5399 0.0095  -0.0435 0.0526  194 LEU B N   
3020 C CA  . LEU B 120 ? 0.6146 0.4952 0.5206 0.0123  -0.0381 0.0538  194 LEU B CA  
3021 C C   . LEU B 120 ? 0.6319 0.5307 0.5353 0.0244  -0.0160 0.0658  194 LEU B C   
3022 O O   . LEU B 120 ? 0.6921 0.5783 0.5721 0.0302  -0.0034 0.0668  194 LEU B O   
3023 C CB  . LEU B 120 ? 0.6076 0.4857 0.4916 0.0070  -0.0550 0.0524  194 LEU B CB  
3024 C CG  . LEU B 120 ? 0.6466 0.5044 0.4880 0.0073  -0.0497 0.0521  194 LEU B CG  
3025 C CD1 . LEU B 120 ? 0.7381 0.5623 0.5591 0.0048  -0.0518 0.0415  194 LEU B CD1 
3026 C CD2 . LEU B 120 ? 0.6355 0.4866 0.4535 0.0021  -0.0637 0.0526  194 LEU B CD2 
3027 N N   . GLN B 121 ? 0.5329 0.4625 0.4594 0.0295  -0.0113 0.0741  195 GLN B N   
3028 C CA  . GLN B 121 ? 0.5386 0.4917 0.4655 0.0434  0.0069  0.0850  195 GLN B CA  
3029 C C   . GLN B 121 ? 0.5940 0.5281 0.5187 0.0554  0.0250  0.0885  195 GLN B C   
3030 O O   . GLN B 121 ? 0.6556 0.5888 0.5648 0.0676  0.0395  0.0934  195 GLN B O   
3031 C CB  . GLN B 121 ? 0.5156 0.5033 0.4648 0.0456  0.0057  0.0914  195 GLN B CB  
3032 C CG  . GLN B 121 ? 0.4775 0.5002 0.4274 0.0594  0.0182  0.1013  195 GLN B CG  
3033 C CD  . GLN B 121 ? 0.5727 0.6269 0.5403 0.0595  0.0147  0.1051  195 GLN B CD  
3034 O OE1 . GLN B 121 ? 0.6490 0.6939 0.6302 0.0543  0.0100  0.1032  195 GLN B OE1 
3035 N NE2 . GLN B 121 ? 0.5527 0.6461 0.5209 0.0646  0.0174  0.1089  195 GLN B NE2 
3036 N N   . GLN B 122 ? 0.6189 0.5360 0.5593 0.0522  0.0266  0.0857  196 GLN B N   
3037 C CA  . GLN B 122 ? 0.5771 0.4674 0.5130 0.0618  0.0470  0.0887  196 GLN B CA  
3038 C C   . GLN B 122 ? 0.6100 0.4651 0.5198 0.0596  0.0517  0.0804  196 GLN B C   
3039 O O   . GLN B 122 ? 0.7620 0.6027 0.6556 0.0745  0.0717  0.0866  196 GLN B O   
3040 C CB  . GLN B 122 ? 0.5908 0.4665 0.5497 0.0529  0.0485  0.0840  196 GLN B CB  
3041 C CG  . GLN B 122 ? 0.6344 0.5386 0.6148 0.0573  0.0495  0.0929  196 GLN B CG  
3042 C CD  . GLN B 122 ? 0.6565 0.5449 0.6609 0.0477  0.0551  0.0875  196 GLN B CD  
3043 O OE1 . GLN B 122 ? 0.6813 0.5592 0.7007 0.0305  0.0427  0.0729  196 GLN B OE1 
3044 N NE2 . GLN B 122 ? 0.7969 0.6845 0.8048 0.0590  0.0743  0.0991  196 GLN B NE2 
3045 N N   . HIS B 123 ? 0.6193 0.4592 0.5226 0.0425  0.0334  0.0663  197 HIS B N   
3046 C CA  . HIS B 123 ? 0.6614 0.4653 0.5348 0.0384  0.0360  0.0562  197 HIS B CA  
3047 C C   . HIS B 123 ? 0.7253 0.5339 0.5727 0.0519  0.0485  0.0639  197 HIS B C   
3048 O O   . HIS B 123 ? 0.7772 0.5595 0.6049 0.0613  0.0678  0.0641  197 HIS B O   
3049 C CB  . HIS B 123 ? 0.6536 0.4483 0.5204 0.0204  0.0094  0.0413  197 HIS B CB  
3050 C CG  . HIS B 123 ? 0.7539 0.5125 0.5829 0.0153  0.0086  0.0299  197 HIS B CG  
3051 N ND1 . HIS B 123 ? 0.8524 0.5744 0.6683 0.0149  0.0254  0.0224  197 HIS B ND1 
3052 C CD2 . HIS B 123 ? 0.8070 0.5560 0.6042 0.0103  -0.0055 0.0244  197 HIS B CD2 
3053 C CE1 . HIS B 123 ? 0.8562 0.5496 0.6341 0.0095  0.0208  0.0116  197 HIS B CE1 
3054 N NE2 . HIS B 123 ? 0.8816 0.5907 0.6464 0.0071  0.0019  0.0132  197 HIS B NE2 
3055 N N   . CYS B 124 ? 0.7185 0.5602 0.5668 0.0526  0.0399  0.0695  198 CYS B N   
3056 C CA  . CYS B 124 ? 0.7226 0.5758 0.5527 0.0632  0.0530  0.0753  198 CYS B CA  
3057 C C   . CYS B 124 ? 0.7207 0.5901 0.5609 0.0857  0.0756  0.0877  198 CYS B C   
3058 O O   . CYS B 124 ? 0.7738 0.6305 0.5964 0.0986  0.0938  0.0897  198 CYS B O   
3059 C CB  . CYS B 124 ? 0.7293 0.6170 0.5636 0.0567  0.0416  0.0779  198 CYS B CB  
3060 S SG  . CYS B 124 ? 0.7905 0.6517 0.5989 0.0367  0.0192  0.0663  198 CYS B SG  
3061 N N   . GLU B 125 ? 0.6840 0.5802 0.5503 0.0925  0.0750  0.0967  199 GLU B N   
3062 C CA  . GLU B 125 ? 0.6856 0.5993 0.5585 0.1173  0.0939  0.1105  199 GLU B CA  
3063 C C   . GLU B 125 ? 0.7319 0.5985 0.5879 0.1293  0.1148  0.1115  199 GLU B C   
3064 O O   . GLU B 125 ? 0.8060 0.6765 0.6545 0.1532  0.1339  0.1214  199 GLU B O   
3065 C CB  . GLU B 125 ? 0.6550 0.5974 0.5518 0.1207  0.0882  0.1187  199 GLU B CB  
3066 C CG  . GLU B 125 ? 0.7419 0.7004 0.6413 0.1488  0.1052  0.1344  199 GLU B CG  
3067 C CD  . GLU B 125 ? 0.9358 0.9185 0.8522 0.1509  0.0992  0.1417  199 GLU B CD  
3068 O OE1 . GLU B 125 ? 0.9190 0.9126 0.8487 0.1305  0.0821  0.1341  199 GLU B OE1 
3069 O OE2 . GLU B 125 ? 0.8537 0.8417 0.7672 0.1744  0.1122  0.1554  199 GLU B OE2 
3070 N N   . ALA B 126 ? 0.7470 0.5692 0.5971 0.1133  0.1124  0.1003  200 ALA B N   
3071 C CA  . ALA B 126 ? 0.7810 0.5516 0.6119 0.1205  0.1342  0.0981  200 ALA B CA  
3072 C C   . ALA B 126 ? 0.8543 0.5959 0.6548 0.1175  0.1397  0.0878  200 ALA B C   
3073 O O   . ALA B 126 ? 0.8868 0.5908 0.6671 0.1305  0.1631  0.0888  200 ALA B O   
3074 C CB  . ALA B 126 ? 0.7387 0.4748 0.5786 0.1020  0.1318  0.0878  200 ALA B CB  
3075 N N   . TRP B 127 ? 0.8194 0.5726 0.6123 0.1014  0.1206  0.0782  201 TRP B N   
3076 C CA  . TRP B 127 ? 0.8252 0.5513 0.5841 0.1002  0.1278  0.0697  201 TRP B CA  
3077 C C   . TRP B 127 ? 0.8652 0.6157 0.6206 0.1246  0.1481  0.0819  201 TRP B C   
3078 O O   . TRP B 127 ? 0.8614 0.5815 0.5903 0.1339  0.1675  0.0788  201 TRP B O   
3079 C CB  . TRP B 127 ? 0.8155 0.5447 0.5620 0.0785  0.1030  0.0582  201 TRP B CB  
3080 C CG  . TRP B 127 ? 0.8579 0.5499 0.5621 0.0734  0.1082  0.0470  201 TRP B CG  
3081 C CD1 . TRP B 127 ? 0.8989 0.6014 0.5828 0.0752  0.1118  0.0484  201 TRP B CD1 
3082 C CD2 . TRP B 127 ? 0.8856 0.5221 0.5599 0.0641  0.1118  0.0314  201 TRP B CD2 
3083 N NE1 . TRP B 127 ? 0.9182 0.5734 0.5584 0.0694  0.1178  0.0359  201 TRP B NE1 
3084 C CE2 . TRP B 127 ? 0.9265 0.5412 0.5594 0.0624  0.1167  0.0247  201 TRP B CE2 
3085 C CE3 . TRP B 127 ? 0.8941 0.4966 0.5721 0.0552  0.1128  0.0211  201 TRP B CE3 
3086 C CZ2 . TRP B 127 ? 0.9922 0.5520 0.5844 0.0533  0.1207  0.0079  201 TRP B CZ2 
3087 C CZ3 . TRP B 127 ? 0.9498 0.4998 0.5910 0.0442  0.1166  0.0031  201 TRP B CZ3 
3088 C CH2 . TRP B 127 ? 1.0038 0.5328 0.6011 0.0439  0.1196  -0.0034 201 TRP B CH2 
3089 N N   . GLY B 128 ? 0.7977 0.6043 0.5806 0.1353  0.1443  0.0946  202 GLY B N   
3090 C CA  . GLY B 128 ? 0.7867 0.6283 0.5755 0.1598  0.1616  0.1057  202 GLY B CA  
3091 C C   . GLY B 128 ? 0.7934 0.6405 0.5651 0.1557  0.1672  0.0993  202 GLY B C   
3092 O O   . GLY B 128 ? 0.8481 0.7104 0.6198 0.1770  0.1877  0.1051  202 GLY B O   
3093 N N   . ALA B 129 ? 0.7684 0.6027 0.5246 0.1304  0.1507  0.0878  203 ALA B N   
3094 C CA  . ALA B 129 ? 0.8588 0.6915 0.5926 0.1241  0.1577  0.0818  203 ALA B CA  
3095 C C   . ALA B 129 ? 0.8248 0.6514 0.5469 0.0973  0.1336  0.0736  203 ALA B C   
3096 O O   . ALA B 129 ? 0.7719 0.5991 0.5070 0.0861  0.1122  0.0725  203 ALA B O   
3097 C CB  . ALA B 129 ? 0.9086 0.6863 0.6041 0.1300  0.1776  0.0743  203 ALA B CB  
3098 N N   . SER B 130 ? 0.8552 0.6742 0.5514 0.0886  0.1388  0.0684  204 SER B N   
3099 C CA  . SER B 130 ? 0.8514 0.6515 0.5248 0.0661  0.1180  0.0615  204 SER B CA  
3100 C C   . SER B 130 ? 0.8371 0.5845 0.4839 0.0572  0.1019  0.0513  204 SER B C   
3101 O O   . SER B 130 ? 0.9374 0.6485 0.5639 0.0634  0.1139  0.0454  204 SER B O   
3102 C CB  . SER B 130 ? 0.9198 0.7108 0.5614 0.0597  0.1316  0.0583  204 SER B CB  
3103 O OG  . SER B 130 ? 0.9314 0.7747 0.6028 0.0689  0.1511  0.0651  204 SER B OG  
3104 N N   . LEU B 131 ? 0.8772 0.6222 0.5266 0.0428  0.0748  0.0481  205 LEU B N   
3105 C CA  . LEU B 131 ? 0.9184 0.6216 0.5466 0.0329  0.0558  0.0362  205 LEU B CA  
3106 C C   . LEU B 131 ? 1.0023 0.6597 0.5725 0.0264  0.0570  0.0264  205 LEU B C   
3107 O O   . LEU B 131 ? 1.0444 0.7025 0.5910 0.0235  0.0619  0.0298  205 LEU B O   
3108 C CB  . LEU B 131 ? 0.8791 0.5957 0.5259 0.0217  0.0260  0.0355  205 LEU B CB  
3109 C CG  . LEU B 131 ? 0.8178 0.5662 0.5157 0.0248  0.0206  0.0406  205 LEU B CG  
3110 C CD1 . LEU B 131 ? 0.8452 0.5970 0.5547 0.0135  -0.0088 0.0362  205 LEU B CD1 
3111 C CD2 . LEU B 131 ? 0.8324 0.5621 0.5390 0.0305  0.0328  0.0363  205 LEU B CD2 
3112 N N   . PRO B 132 ? 0.9701 0.5850 0.5138 0.0230  0.0545  0.0135  206 PRO B N   
3113 C CA  . PRO B 132 ? 1.0591 0.6279 0.5416 0.0154  0.0500  0.0025  206 PRO B CA  
3114 C C   . PRO B 132 ? 1.0834 0.6516 0.5486 0.0051  0.0203  0.0022  206 PRO B C   
3115 O O   . PRO B 132 ? 1.0755 0.6647 0.5725 0.0005  -0.0043 0.0025  206 PRO B O   
3116 C CB  . PRO B 132 ? 1.0638 0.5942 0.5315 0.0105  0.0462  -0.0139 206 PRO B CB  
3117 C CG  . PRO B 132 ? 1.0610 0.6180 0.5856 0.0121  0.0431  -0.0112 206 PRO B CG  
3118 C CD  . PRO B 132 ? 1.0388 0.6423 0.6030 0.0256  0.0592  0.0076  206 PRO B CD  
3119 N N   . GLU B 133 ? 1.0779 0.6202 0.4910 0.0029  0.0250  0.0025  207 GLU B N   
3120 C CA  . GLU B 133 ? 1.0623 0.6020 0.4547 -0.0031 0.0035  0.0071  207 GLU B CA  
3121 C C   . GLU B 133 ? 1.1199 0.6398 0.4953 -0.0090 -0.0343 -0.0038 207 GLU B C   
3122 O O   . GLU B 133 ? 1.1630 0.6889 0.5363 -0.0104 -0.0570 0.0013  207 GLU B O   
3123 C CB  . GLU B 133 ? 1.1497 0.6587 0.4838 -0.0039 0.0221  0.0103  207 GLU B CB  
3124 C CG  . GLU B 133 ? 1.2527 0.7669 0.5763 -0.0081 0.0151  0.0211  207 GLU B CG  
3125 C CD  . GLU B 133 ? 1.3024 0.7965 0.5883 -0.0104 0.0422  0.0249  207 GLU B CD  
3126 O OE1 . GLU B 133 ? 1.3399 0.8448 0.6338 -0.0073 0.0746  0.0256  207 GLU B OE1 
3127 O OE2 . GLU B 133 ? 1.2824 0.7571 0.5459 -0.0139 0.0315  0.0265  207 GLU B OE2 
3128 N N   . ALA B 134 ? 1.1886 0.6859 0.5527 -0.0123 -0.0413 -0.0195 208 ALA B N   
3129 C CA  . ALA B 134 ? 1.1441 0.6341 0.5036 -0.0189 -0.0793 -0.0324 208 ALA B CA  
3130 C C   . ALA B 134 ? 1.0915 0.6275 0.5194 -0.0195 -0.0970 -0.0282 208 ALA B C   
3131 O O   . ALA B 134 ? 1.1511 0.6957 0.5816 -0.0201 -0.1281 -0.0290 208 ALA B O   
3132 C CB  . ALA B 134 ? 1.1139 0.5739 0.4539 -0.0258 -0.0799 -0.0529 208 ALA B CB  
3133 N N   . GLN B 135 ? 1.0706 0.6356 0.5525 -0.0172 -0.0768 -0.0228 209 GLN B N   
3134 C CA  . GLN B 135 ? 1.0240 0.6306 0.5684 -0.0177 -0.0896 -0.0182 209 GLN B CA  
3135 C C   . GLN B 135 ? 1.0085 0.6375 0.5605 -0.0132 -0.0964 -0.0032 209 GLN B C   
3136 O O   . GLN B 135 ? 1.0057 0.6514 0.5794 -0.0141 -0.1217 -0.0033 209 GLN B O   
3137 C CB  . GLN B 135 ? 0.9792 0.6066 0.5698 -0.0140 -0.0634 -0.0134 209 GLN B CB  
3138 C CG  . GLN B 135 ? 1.0398 0.6395 0.6236 -0.0179 -0.0506 -0.0271 209 GLN B CG  
3139 C CD  . GLN B 135 ? 1.0443 0.6629 0.6760 -0.0127 -0.0284 -0.0208 209 GLN B CD  
3140 O OE1 . GLN B 135 ? 0.9642 0.6191 0.6406 -0.0102 -0.0325 -0.0112 209 GLN B OE1 
3141 N NE2 . GLN B 135 ? 1.1233 0.7132 0.7417 -0.0098 -0.0035 -0.0257 209 GLN B NE2 
3142 N N   . VAL B 136 ? 0.9843 0.6135 0.5194 -0.0089 -0.0725 0.0088  210 VAL B N   
3143 C CA  . VAL B 136 ? 0.9500 0.5976 0.4916 -0.0076 -0.0731 0.0219  210 VAL B CA  
3144 C C   . VAL B 136 ? 1.0232 0.6497 0.5325 -0.0085 -0.1024 0.0207  210 VAL B C   
3145 O O   . VAL B 136 ? 0.9858 0.6313 0.5193 -0.0071 -0.1157 0.0271  210 VAL B O   
3146 C CB  . VAL B 136 ? 1.0034 0.6481 0.5225 -0.0063 -0.0423 0.0304  210 VAL B CB  
3147 C CG1 . VAL B 136 ? 1.0151 0.6731 0.5362 -0.0090 -0.0413 0.0412  210 VAL B CG1 
3148 C CG2 . VAL B 136 ? 0.9681 0.6416 0.5250 -0.0007 -0.0159 0.0332  210 VAL B CG2 
3149 N N   . TRP B 137 ? 1.0457 0.6309 0.4972 -0.0091 -0.1130 0.0125  211 TRP B N   
3150 C CA  . TRP B 137 ? 1.0550 0.6171 0.4677 -0.0059 -0.1422 0.0127  211 TRP B CA  
3151 C C   . TRP B 137 ? 1.0501 0.6377 0.5053 -0.0042 -0.1756 0.0056  211 TRP B C   
3152 O O   . TRP B 137 ? 1.0822 0.6732 0.5378 0.0022  -0.1957 0.0118  211 TRP B O   
3153 C CB  . TRP B 137 ? 1.1465 0.6624 0.4912 -0.0059 -0.1465 0.0040  211 TRP B CB  
3154 C CG  . TRP B 137 ? 1.1816 0.6735 0.4893 -0.0060 -0.1152 0.0122  211 TRP B CG  
3155 C CD1 . TRP B 137 ? 1.2228 0.6948 0.5022 -0.0089 -0.0872 0.0089  211 TRP B CD1 
3156 C CD2 . TRP B 137 ? 1.2138 0.6983 0.5110 -0.0036 -0.1068 0.0236  211 TRP B CD2 
3157 N NE1 . TRP B 137 ? 1.2110 0.6688 0.4682 -0.0092 -0.0630 0.0173  211 TRP B NE1 
3158 C CE2 . TRP B 137 ? 1.2197 0.6825 0.4850 -0.0070 -0.0746 0.0258  211 TRP B CE2 
3159 C CE3 . TRP B 137 ? 1.2148 0.7066 0.5257 0.0012  -0.1216 0.0310  211 TRP B CE3 
3160 C CZ2 . TRP B 137 ? 1.2537 0.7016 0.5004 -0.0081 -0.0577 0.0344  211 TRP B CZ2 
3161 C CZ3 . TRP B 137 ? 1.2710 0.7430 0.5580 0.0011  -0.1040 0.0399  211 TRP B CZ3 
3162 C CH2 . TRP B 137 ? 1.3205 0.7708 0.5760 -0.0046 -0.0728 0.0411  211 TRP B CH2 
3163 N N   . GLY B 138 ? 1.0046 0.6092 0.4968 -0.0095 -0.1799 -0.0078 212 GLY B N   
3164 C CA  . GLY B 138 ? 0.9839 0.6189 0.5258 -0.0101 -0.2075 -0.0159 212 GLY B CA  
3165 C C   . GLY B 138 ? 0.9686 0.6409 0.5662 -0.0066 -0.2022 -0.0037 212 GLY B C   
3166 O O   . GLY B 138 ? 1.0275 0.7139 0.6418 -0.0007 -0.2254 -0.0016 212 GLY B O   
3167 N N   . TYR B 139 ? 0.9796 0.6682 0.6045 -0.0087 -0.1716 0.0045  213 TYR B N   
3168 C CA  . TYR B 139 ? 0.8685 0.5920 0.5430 -0.0064 -0.1651 0.0148  213 TYR B CA  
3169 C C   . TYR B 139 ? 0.9277 0.6435 0.5788 -0.0013 -0.1683 0.0272  213 TYR B C   
3170 O O   . TYR B 139 ? 0.9172 0.6536 0.6005 0.0020  -0.1771 0.0318  213 TYR B O   
3171 C CB  . TYR B 139 ? 0.8601 0.6017 0.5606 -0.0078 -0.1331 0.0209  213 TYR B CB  
3172 C CG  . TYR B 139 ? 0.8353 0.5780 0.5570 -0.0115 -0.1253 0.0107  213 TYR B CG  
3173 C CD1 . TYR B 139 ? 0.8726 0.6174 0.6156 -0.0170 -0.1460 -0.0034 213 TYR B CD1 
3174 C CD2 . TYR B 139 ? 0.7823 0.5235 0.5034 -0.0093 -0.0962 0.0147  213 TYR B CD2 
3175 C CE1 . TYR B 139 ? 0.8898 0.6302 0.6507 -0.0232 -0.1356 -0.0141 213 TYR B CE1 
3176 C CE2 . TYR B 139 ? 0.8181 0.5521 0.5539 -0.0117 -0.0860 0.0062  213 TYR B CE2 
3177 C CZ  . TYR B 139 ? 0.8480 0.5790 0.6025 -0.0202 -0.1047 -0.0085 213 TYR B CZ  
3178 O OH  . TYR B 139 ? 0.9413 0.6602 0.7091 -0.0255 -0.0917 -0.0183 213 TYR B OH  
3179 N N   . LEU B 140 ? 0.9572 0.6400 0.5513 -0.0011 -0.1586 0.0322  214 LEU B N   
3180 C CA  . LEU B 140 ? 0.9443 0.6100 0.5088 0.0023  -0.1600 0.0432  214 LEU B CA  
3181 C C   . LEU B 140 ? 0.9923 0.6465 0.5465 0.0114  -0.1921 0.0407  214 LEU B C   
3182 O O   . LEU B 140 ? 1.0371 0.6998 0.6097 0.0165  -0.1950 0.0470  214 LEU B O   
3183 C CB  . LEU B 140 ? 0.9931 0.6225 0.4970 -0.0009 -0.1394 0.0481  214 LEU B CB  
3184 C CG  . LEU B 140 ? 0.9857 0.5952 0.4657 0.0007  -0.1327 0.0556  214 LEU B CG  
3185 C CD1 . LEU B 140 ? 0.9089 0.5409 0.4210 -0.0029 -0.1222 0.0644  214 LEU B CD1 
3186 C CD2 . LEU B 140 ? 1.0020 0.5812 0.4351 -0.0042 -0.1081 0.0567  214 LEU B CD2 
3187 N N   . ARG B 141 ? 1.0511 0.6932 0.5874 0.0137  -0.2114 0.0291  215 ARG B N   
3188 C CA  . ARG B 141 ? 1.0084 0.6514 0.5480 0.0241  -0.2366 0.0252  215 ARG B CA  
3189 C C   . ARG B 141 ? 0.9147 0.5979 0.5171 0.0279  -0.2550 0.0220  215 ARG B C   
3190 O O   . ARG B 141 ? 0.9816 0.6716 0.5968 0.0385  -0.2649 0.0262  215 ARG B O   
3191 C CB  . ARG B 141 ? 1.0551 0.6814 0.5637 0.0247  -0.2535 0.0123  215 ARG B CB  
3192 C CG  . ARG B 141 ? 1.0780 0.7107 0.5904 0.0373  -0.2805 0.0090  215 ARG B CG  
3193 C CD  . ARG B 141 ? 1.2563 0.8724 0.7322 0.0383  -0.2970 -0.0029 215 ARG B CD  
3194 N NE  . ARG B 141 ? 1.4295 1.0479 0.8979 0.0536  -0.3198 -0.0019 215 ARG B NE  
3195 C CZ  . ARG B 141 ? 1.4371 1.0936 0.9495 0.0595  -0.3466 -0.0111 215 ARG B CZ  
3196 N NH1 . ARG B 141 ? 1.4195 1.1143 0.9890 0.0494  -0.3536 -0.0232 215 ARG B NH1 
3197 N NH2 . ARG B 141 ? 1.4058 1.0624 0.9051 0.0758  -0.3659 -0.0084 215 ARG B NH2 
3198 N N   . ASP B 142 ? 0.8877 0.5961 0.5291 0.0197  -0.2582 0.0143  216 ASP B N   
3199 C CA  . ASP B 142 ? 0.9149 0.6631 0.6209 0.0221  -0.2735 0.0097  216 ASP B CA  
3200 C C   . ASP B 142 ? 0.8862 0.6478 0.6182 0.0257  -0.2586 0.0236  216 ASP B C   
3201 O O   . ASP B 142 ? 0.9074 0.6878 0.6721 0.0344  -0.2688 0.0245  216 ASP B O   
3202 C CB  . ASP B 142 ? 0.8770 0.6513 0.6306 0.0097  -0.2672 -0.0041 216 ASP B CB  
3203 C CG  . ASP B 142 ? 1.0566 0.8384 0.8176 0.0071  -0.2974 -0.0236 216 ASP B CG  
3204 O OD1 . ASP B 142 ? 1.0354 0.8044 0.7634 0.0163  -0.3159 -0.0251 216 ASP B OD1 
3205 O OD2 . ASP B 142 ? 1.0449 0.8492 0.8517 -0.0046 -0.2933 -0.0372 216 ASP B OD2 
3206 N N   . THR B 143 ? 0.8959 0.6531 0.6207 0.0186  -0.2275 0.0326  217 THR B N   
3207 C CA  . THR B 143 ? 0.8419 0.6105 0.5867 0.0199  -0.2129 0.0436  217 THR B CA  
3208 C C   . THR B 143 ? 0.8774 0.6165 0.5826 0.0288  -0.2186 0.0523  217 THR B C   
3209 O O   . THR B 143 ? 0.8832 0.6308 0.6100 0.0339  -0.2176 0.0574  217 THR B O   
3210 C CB  . THR B 143 ? 0.7796 0.5558 0.5265 0.0100  -0.1802 0.0491  217 THR B CB  
3211 O OG1 . THR B 143 ? 0.7900 0.5856 0.5654 0.0046  -0.1719 0.0415  217 THR B OG1 
3212 C CG2 . THR B 143 ? 0.7580 0.5558 0.5365 0.0089  -0.1671 0.0561  217 THR B CG2 
3213 N N   . LEU B 144 ? 0.8923 0.5983 0.5453 0.0304  -0.2175 0.0520  218 LEU B N   
3214 C CA  . LEU B 144 ? 0.9312 0.6096 0.5519 0.0393  -0.2173 0.0581  218 LEU B CA  
3215 C C   . LEU B 144 ? 0.9128 0.6044 0.5575 0.0542  -0.2429 0.0541  218 LEU B C   
3216 O O   . LEU B 144 ? 0.9603 0.6420 0.6017 0.0636  -0.2423 0.0610  218 LEU B O   
3217 C CB  . LEU B 144 ? 0.9585 0.5981 0.5187 0.0383  -0.2106 0.0583  218 LEU B CB  
3218 C CG  . LEU B 144 ? 0.9428 0.5611 0.4710 0.0266  -0.1792 0.0655  218 LEU B CG  
3219 C CD1 . LEU B 144 ? 1.0260 0.6042 0.4958 0.0273  -0.1728 0.0651  218 LEU B CD1 
3220 C CD2 . LEU B 144 ? 0.9609 0.5743 0.4938 0.0249  -0.1648 0.0747  218 LEU B CD2 
3221 N N   . LEU B 145 ? 0.9036 0.6175 0.5722 0.0563  -0.2648 0.0423  219 LEU B N   
3222 C CA  . LEU B 145 ? 0.8593 0.5959 0.5598 0.0699  -0.2886 0.0370  219 LEU B CA  
3223 C C   . LEU B 145 ? 0.8568 0.6230 0.6121 0.0723  -0.2850 0.0399  219 LEU B C   
3224 O O   . LEU B 145 ? 0.8841 0.6542 0.6507 0.0864  -0.2930 0.0432  219 LEU B O   
3225 C CB  . LEU B 145 ? 0.8725 0.6330 0.5946 0.0673  -0.3107 0.0211  219 LEU B CB  
3226 C CG  . LEU B 145 ? 0.9488 0.6823 0.6179 0.0678  -0.3202 0.0159  219 LEU B CG  
3227 C CD1 . LEU B 145 ? 0.9393 0.7016 0.6379 0.0615  -0.3409 -0.0025 219 LEU B CD1 
3228 C CD2 . LEU B 145 ? 0.9379 0.6488 0.5690 0.0853  -0.3303 0.0228  219 LEU B CD2 
3229 N N   . ALA B 146 ? 0.8240 0.6098 0.6121 0.0600  -0.2725 0.0392  220 ALA B N   
3230 C CA  . ALA B 146 ? 0.7826 0.5942 0.6202 0.0616  -0.2664 0.0423  220 ALA B CA  
3231 C C   . ALA B 146 ? 0.8080 0.5934 0.6190 0.0668  -0.2515 0.0551  220 ALA B C   
3232 O O   . ALA B 146 ? 0.8833 0.6740 0.7136 0.0786  -0.2560 0.0575  220 ALA B O   
3233 C CB  . ALA B 146 ? 0.7138 0.5471 0.5838 0.0478  -0.2545 0.0408  220 ALA B CB  
3234 N N   . LEU B 147 ? 0.8568 0.6125 0.6229 0.0574  -0.2325 0.0629  221 LEU B N   
3235 C CA  . LEU B 147 ? 0.8258 0.5528 0.5641 0.0583  -0.2163 0.0735  221 LEU B CA  
3236 C C   . LEU B 147 ? 0.8896 0.5902 0.6005 0.0750  -0.2265 0.0766  221 LEU B C   
3237 O O   . LEU B 147 ? 0.9350 0.6254 0.6499 0.0833  -0.2226 0.0824  221 LEU B O   
3238 C CB  . LEU B 147 ? 0.8123 0.5143 0.5071 0.0434  -0.1936 0.0788  221 LEU B CB  
3239 C CG  . LEU B 147 ? 0.7745 0.5028 0.4935 0.0285  -0.1799 0.0784  221 LEU B CG  
3240 C CD1 . LEU B 147 ? 0.7751 0.4850 0.4562 0.0142  -0.1541 0.0823  221 LEU B CD1 
3241 C CD2 . LEU B 147 ? 0.7437 0.5025 0.5130 0.0265  -0.1709 0.0774  221 LEU B CD2 
3242 N N   . ALA B 148 ? 0.8998 0.5868 0.5803 0.0811  -0.2394 0.0733  222 ALA B N   
3243 C CA  . ALA B 148 ? 0.9013 0.5650 0.5545 0.0995  -0.2512 0.0772  222 ALA B CA  
3244 C C   . ALA B 148 ? 0.9254 0.6209 0.6276 0.1155  -0.2693 0.0743  222 ALA B C   
3245 O O   . ALA B 148 ? 0.9438 0.6213 0.6335 0.1316  -0.2713 0.0815  222 ALA B O   
3246 C CB  . ALA B 148 ? 0.9172 0.5662 0.5324 0.1033  -0.2649 0.0728  222 ALA B CB  
3247 N N   . HIS B 149 ? 0.8976 0.6396 0.6565 0.1115  -0.2806 0.0638  223 HIS B N   
3248 C CA  . HIS B 149 ? 0.8971 0.6744 0.7103 0.1246  -0.2937 0.0599  223 HIS B CA  
3249 C C   . HIS B 149 ? 0.8985 0.6731 0.7317 0.1254  -0.2762 0.0672  223 HIS B C   
3250 O O   . HIS B 149 ? 0.9511 0.7246 0.7954 0.1422  -0.2796 0.0714  223 HIS B O   
3251 C CB  . HIS B 149 ? 0.8771 0.7031 0.7466 0.1164  -0.3062 0.0453  223 HIS B CB  
3252 C CG  . HIS B 149 ? 0.8388 0.7063 0.7720 0.1261  -0.3147 0.0396  223 HIS B CG  
3253 N ND1 . HIS B 149 ? 0.8044 0.6844 0.7470 0.1456  -0.3334 0.0381  223 HIS B ND1 
3254 C CD2 . HIS B 149 ? 0.7751 0.6749 0.7661 0.1195  -0.3055 0.0351  223 HIS B CD2 
3255 C CE1 . HIS B 149 ? 0.8327 0.7526 0.8381 0.1501  -0.3345 0.0324  223 HIS B CE1 
3256 N NE2 . HIS B 149 ? 0.7701 0.7011 0.8052 0.1339  -0.3169 0.0302  223 HIS B NE2 
3257 N N   . LEU B 150 ? 0.8656 0.6387 0.7026 0.1080  -0.2573 0.0690  224 LEU B N   
3258 C CA  . LEU B 150 ? 0.8644 0.6315 0.7152 0.1067  -0.2403 0.0753  224 LEU B CA  
3259 C C   . LEU B 150 ? 0.8626 0.5791 0.6617 0.1143  -0.2290 0.0864  224 LEU B C   
3260 O O   . LEU B 150 ? 0.9085 0.6164 0.7190 0.1247  -0.2235 0.0906  224 LEU B O   
3261 C CB  . LEU B 150 ? 0.8280 0.6018 0.6847 0.0861  -0.2237 0.0759  224 LEU B CB  
3262 C CG  . LEU B 150 ? 0.7377 0.5574 0.6566 0.0793  -0.2241 0.0688  224 LEU B CG  
3263 C CD1 . LEU B 150 ? 0.7453 0.5981 0.6970 0.0815  -0.2424 0.0571  224 LEU B CD1 
3264 C CD2 . LEU B 150 ? 0.7446 0.5708 0.6564 0.0576  -0.1987 0.0686  224 LEU B CD2 
3265 N N   . HIS B 151 ? 0.8923 0.5722 0.6337 0.1086  -0.2226 0.0910  225 HIS B N   
3266 C CA  . HIS B 151 ? 0.9058 0.5333 0.5960 0.1117  -0.2065 0.1009  225 HIS B CA  
3267 C C   . HIS B 151 ? 1.0178 0.6289 0.6947 0.1365  -0.2196 0.1052  225 HIS B C   
3268 O O   . HIS B 151 ? 1.0998 0.6702 0.7466 0.1430  -0.2059 0.1135  225 HIS B O   
3269 C CB  . HIS B 151 ? 0.9515 0.5458 0.5866 0.0963  -0.1920 0.1035  225 HIS B CB  
3270 C CG  . HIS B 151 ? 0.9215 0.5301 0.5656 0.0727  -0.1760 0.1011  225 HIS B CG  
3271 N ND1 . HIS B 151 ? 0.8874 0.4813 0.4959 0.0576  -0.1632 0.1010  225 HIS B ND1 
3272 C CD2 . HIS B 151 ? 0.8060 0.4432 0.4904 0.0627  -0.1706 0.0992  225 HIS B CD2 
3273 C CE1 . HIS B 151 ? 0.8769 0.4929 0.5049 0.0397  -0.1509 0.0995  225 HIS B CE1 
3274 N NE2 . HIS B 151 ? 0.8534 0.4948 0.5255 0.0424  -0.1559 0.0988  225 HIS B NE2 
3275 N N   . SER B 152 ? 1.0207 0.6616 0.7181 0.1502  -0.2452 0.0996  226 SER B N   
3276 C CA  . SER B 152 ? 0.9711 0.6035 0.6606 0.1760  -0.2600 0.1044  226 SER B CA  
3277 C C   . SER B 152 ? 0.9118 0.5598 0.6448 0.1899  -0.2585 0.1063  226 SER B C   
3278 O O   . SER B 152 ? 1.0924 0.7253 0.8151 0.2125  -0.2646 0.1133  226 SER B O   
3279 C CB  . SER B 152 ? 0.9119 0.5782 0.6168 0.1854  -0.2890 0.0961  226 SER B CB  
3280 O OG  . SER B 152 ? 1.0024 0.7265 0.7771 0.1821  -0.3000 0.0848  226 SER B OG  
3281 N N   . GLN B 153 ? 0.9521 0.6288 0.7325 0.1782  -0.2497 0.1008  227 GLN B N   
3282 C CA  . GLN B 153 ? 0.9185 0.6098 0.7423 0.1900  -0.2449 0.1013  227 GLN B CA  
3283 C C   . GLN B 153 ? 0.9461 0.6019 0.7541 0.1783  -0.2172 0.1063  227 GLN B C   
3284 O O   . GLN B 153 ? 0.9316 0.5992 0.7776 0.1835  -0.2095 0.1046  227 GLN B O   
3285 C CB  . GLN B 153 ? 0.9160 0.6714 0.8129 0.1872  -0.2569 0.0889  227 GLN B CB  
3286 C CG  . GLN B 153 ? 0.9218 0.7131 0.8350 0.1921  -0.2827 0.0805  227 GLN B CG  
3287 C CD  . GLN B 153 ? 0.9450 0.7967 0.9311 0.1857  -0.2902 0.0668  227 GLN B CD  
3288 O OE1 . GLN B 153 ? 0.9266 0.7963 0.9263 0.1659  -0.2890 0.0588  227 GLN B OE1 
3289 N NE2 . GLN B 153 ? 0.9720 0.8543 1.0059 0.2023  -0.2958 0.0639  227 GLN B NE2 
3290 N N   . GLY B 154 ? 0.9715 0.5847 0.7251 0.1612  -0.2005 0.1110  228 GLY B N   
3291 C CA  . GLY B 154 ? 0.9435 0.5212 0.6783 0.1466  -0.1733 0.1139  228 GLY B CA  
3292 C C   . GLY B 154 ? 0.9503 0.5584 0.7239 0.1285  -0.1671 0.1072  228 GLY B C   
3293 O O   . GLY B 154 ? 0.9892 0.5824 0.7694 0.1225  -0.1492 0.1064  228 GLY B O   
3294 N N   . LEU B 155 ? 0.9238 0.5732 0.7221 0.1191  -0.1800 0.1015  229 LEU B N   
3295 C CA  . LEU B 155 ? 0.8548 0.5457 0.6939 0.0985  -0.1693 0.0934  229 LEU B CA  
3296 C C   . LEU B 155 ? 0.8075 0.4942 0.6151 0.0744  -0.1565 0.0930  229 LEU B C   
3297 O O   . LEU B 155 ? 0.8464 0.5155 0.6186 0.0766  -0.1680 0.0970  229 LEU B O   
3298 C CB  . LEU B 155 ? 0.7601 0.5076 0.6604 0.1056  -0.1890 0.0854  229 LEU B CB  
3299 C CG  . LEU B 155 ? 0.8174 0.5782 0.7529 0.1320  -0.2066 0.0843  229 LEU B CG  
3300 C CD1 . LEU B 155 ? 0.6718 0.4915 0.6676 0.1328  -0.2222 0.0733  229 LEU B CD1 
3301 C CD2 . LEU B 155 ? 0.8491 0.6000 0.8022 0.1371  -0.1883 0.0848  229 LEU B CD2 
3302 N N   . VAL B 156 ? 0.6934 0.3974 0.5133 0.0524  -0.1327 0.0876  230 VAL B N   
3303 C CA  . VAL B 156 ? 0.7194 0.4306 0.5202 0.0299  -0.1187 0.0858  230 VAL B CA  
3304 C C   . VAL B 156 ? 0.7291 0.4970 0.5793 0.0204  -0.1154 0.0784  230 VAL B C   
3305 O O   . VAL B 156 ? 0.7325 0.5216 0.6131 0.0166  -0.1048 0.0737  230 VAL B O   
3306 C CB  . VAL B 156 ? 0.7840 0.4641 0.5499 0.0116  -0.0925 0.0857  230 VAL B CB  
3307 C CG1 . VAL B 156 ? 0.7901 0.4801 0.5374 -0.0097 -0.0795 0.0836  230 VAL B CG1 
3308 C CG2 . VAL B 156 ? 0.9512 0.5669 0.6679 0.0234  -0.0921 0.0941  230 VAL B CG2 
3309 N N   . HIS B 157 ? 0.6493 0.4374 0.5034 0.0175  -0.1230 0.0775  231 HIS B N   
3310 C CA  . HIS B 157 ? 0.6348 0.4702 0.5314 0.0116  -0.1192 0.0722  231 HIS B CA  
3311 C C   . HIS B 157 ? 0.6367 0.4907 0.5356 -0.0053 -0.0965 0.0696  231 HIS B C   
3312 O O   . HIS B 157 ? 0.6240 0.5076 0.5561 -0.0069 -0.0896 0.0661  231 HIS B O   
3313 C CB  . HIS B 157 ? 0.6309 0.4753 0.5234 0.0117  -0.1289 0.0717  231 HIS B CB  
3314 C CG  . HIS B 157 ? 0.5884 0.4728 0.5232 0.0097  -0.1265 0.0673  231 HIS B CG  
3315 N ND1 . HIS B 157 ? 0.5952 0.5044 0.5389 -0.0006 -0.1082 0.0669  231 HIS B ND1 
3316 C CD2 . HIS B 157 ? 0.6009 0.5032 0.5701 0.0169  -0.1390 0.0628  231 HIS B CD2 
3317 C CE1 . HIS B 157 ? 0.5810 0.5158 0.5580 0.0021  -0.1083 0.0645  231 HIS B CE1 
3318 N NE2 . HIS B 157 ? 0.5489 0.4794 0.5431 0.0107  -0.1254 0.0611  231 HIS B NE2 
3319 N N   . LEU B 158 ? 0.7000 0.5386 0.5635 -0.0183 -0.0846 0.0707  232 LEU B N   
3320 C CA  . LEU B 158 ? 0.6536 0.5137 0.5176 -0.0361 -0.0649 0.0664  232 LEU B CA  
3321 C C   . LEU B 158 ? 0.5971 0.5042 0.4882 -0.0382 -0.0614 0.0647  232 LEU B C   
3322 O O   . LEU B 158 ? 0.6773 0.6116 0.5741 -0.0498 -0.0483 0.0607  232 LEU B O   
3323 C CB  . LEU B 158 ? 0.6578 0.5168 0.5313 -0.0408 -0.0554 0.0617  232 LEU B CB  
3324 C CG  . LEU B 158 ? 0.6955 0.5045 0.5356 -0.0436 -0.0493 0.0622  232 LEU B CG  
3325 C CD1 . LEU B 158 ? 0.6508 0.4627 0.5032 -0.0495 -0.0377 0.0553  232 LEU B CD1 
3326 C CD2 . LEU B 158 ? 0.6711 0.4568 0.4712 -0.0607 -0.0359 0.0620  232 LEU B CD2 
3327 N N   . ASP B 159 ? 0.6137 0.5308 0.5202 -0.0272 -0.0726 0.0671  233 ASP B N   
3328 C CA  . ASP B 159 ? 0.6258 0.5797 0.5530 -0.0270 -0.0668 0.0671  233 ASP B CA  
3329 C C   . ASP B 159 ? 0.6376 0.5835 0.5590 -0.0201 -0.0753 0.0692  233 ASP B C   
3330 O O   . ASP B 159 ? 0.5958 0.5574 0.5406 -0.0134 -0.0777 0.0691  233 ASP B O   
3331 C CB  . ASP B 159 ? 0.5728 0.5518 0.5358 -0.0213 -0.0653 0.0659  233 ASP B CB  
3332 C CG  . ASP B 159 ? 0.6403 0.6561 0.6154 -0.0221 -0.0538 0.0669  233 ASP B CG  
3333 O OD1 . ASP B 159 ? 0.6665 0.6965 0.6271 -0.0296 -0.0457 0.0666  233 ASP B OD1 
3334 O OD2 . ASP B 159 ? 0.7198 0.7504 0.7189 -0.0144 -0.0522 0.0683  233 ASP B OD2 
3335 N N   . VAL B 160 ? 0.6081 0.5251 0.4945 -0.0227 -0.0783 0.0705  234 VAL B N   
3336 C CA  . VAL B 160 ? 0.5830 0.4886 0.4556 -0.0180 -0.0850 0.0710  234 VAL B CA  
3337 C C   . VAL B 160 ? 0.6314 0.5608 0.5044 -0.0219 -0.0690 0.0717  234 VAL B C   
3338 O O   . VAL B 160 ? 0.6652 0.6017 0.5244 -0.0311 -0.0553 0.0719  234 VAL B O   
3339 C CB  . VAL B 160 ? 0.6343 0.4969 0.4628 -0.0178 -0.0931 0.0727  234 VAL B CB  
3340 C CG1 . VAL B 160 ? 0.6260 0.4755 0.4368 -0.0133 -0.1007 0.0714  234 VAL B CG1 
3341 C CG2 . VAL B 160 ? 0.6674 0.5086 0.4960 -0.0094 -0.1097 0.0734  234 VAL B CG2 
3342 N N   . LYS B 161 ? 0.6039 0.5462 0.4943 -0.0148 -0.0694 0.0714  235 LYS B N   
3343 C CA  . LYS B 161 ? 0.5679 0.5327 0.4614 -0.0131 -0.0543 0.0734  235 LYS B CA  
3344 C C   . LYS B 161 ? 0.6087 0.5698 0.5147 -0.0043 -0.0570 0.0726  235 LYS B C   
3345 O O   . LYS B 161 ? 0.6386 0.5905 0.5602 -0.0021 -0.0692 0.0695  235 LYS B O   
3346 C CB  . LYS B 161 ? 0.5739 0.5783 0.4894 -0.0145 -0.0427 0.0751  235 LYS B CB  
3347 C CG  . LYS B 161 ? 0.5505 0.5696 0.4957 -0.0093 -0.0459 0.0757  235 LYS B CG  
3348 C CD  . LYS B 161 ? 0.5853 0.6436 0.5435 -0.0087 -0.0345 0.0777  235 LYS B CD  
3349 C CE  . LYS B 161 ? 0.6439 0.7133 0.6233 -0.0063 -0.0356 0.0777  235 LYS B CE  
3350 N NZ  . LYS B 161 ? 0.7112 0.8192 0.6957 -0.0061 -0.0267 0.0785  235 LYS B NZ  
3351 N N   . PRO B 162 ? 0.5970 0.5644 0.4973 0.0006  -0.0444 0.0746  236 PRO B N   
3352 C CA  . PRO B 162 ? 0.5607 0.5144 0.4663 0.0072  -0.0444 0.0726  236 PRO B CA  
3353 C C   . PRO B 162 ? 0.5673 0.5337 0.5066 0.0115  -0.0438 0.0735  236 PRO B C   
3354 O O   . PRO B 162 ? 0.6256 0.5750 0.5732 0.0118  -0.0479 0.0685  236 PRO B O   
3355 C CB  . PRO B 162 ? 0.5841 0.5448 0.4775 0.0140  -0.0263 0.0763  236 PRO B CB  
3356 C CG  . PRO B 162 ? 0.6134 0.5804 0.4868 0.0074  -0.0220 0.0769  236 PRO B CG  
3357 C CD  . PRO B 162 ? 0.6023 0.5853 0.4889 -0.0002 -0.0291 0.0772  236 PRO B CD  
3358 N N   . ALA B 163 ? 0.5452 0.5397 0.5026 0.0136  -0.0377 0.0784  237 ALA B N   
3359 C CA  . ALA B 163 ? 0.4804 0.4840 0.4657 0.0178  -0.0342 0.0800  237 ALA B CA  
3360 C C   . ALA B 163 ? 0.5699 0.5625 0.5732 0.0116  -0.0487 0.0732  237 ALA B C   
3361 O O   . ALA B 163 ? 0.6040 0.5974 0.6320 0.0131  -0.0450 0.0719  237 ALA B O   
3362 C CB  . ALA B 163 ? 0.4974 0.5331 0.4911 0.0217  -0.0253 0.0862  237 ALA B CB  
3363 N N   . ASN B 164 ? 0.5783 0.5604 0.5699 0.0058  -0.0635 0.0693  238 ASN B N   
3364 C CA  . ASN B 164 ? 0.5637 0.5390 0.5727 0.0036  -0.0790 0.0636  238 ASN B CA  
3365 C C   . ASN B 164 ? 0.6222 0.5745 0.6202 0.0021  -0.0967 0.0563  238 ASN B C   
3366 O O   . ASN B 164 ? 0.6474 0.5943 0.6529 0.0027  -0.1139 0.0519  238 ASN B O   
3367 C CB  . ASN B 164 ? 0.5428 0.5212 0.5451 0.0013  -0.0828 0.0655  238 ASN B CB  
3368 C CG  . ASN B 164 ? 0.5611 0.5638 0.5747 0.0013  -0.0680 0.0697  238 ASN B CG  
3369 O OD1 . ASN B 164 ? 0.5749 0.5918 0.6080 0.0054  -0.0578 0.0717  238 ASN B OD1 
3370 N ND2 . ASN B 164 ? 0.5781 0.5836 0.5766 -0.0039 -0.0660 0.0705  238 ASN B ND2 
3371 N N   . ILE B 165 ? 0.5949 0.5337 0.5735 0.0016  -0.0931 0.0546  239 ILE B N   
3372 C CA  . ILE B 165 ? 0.5938 0.5104 0.5585 -0.0008 -0.1093 0.0457  239 ILE B CA  
3373 C C   . ILE B 165 ? 0.6392 0.5537 0.6225 -0.0031 -0.1011 0.0394  239 ILE B C   
3374 O O   . ILE B 165 ? 0.6231 0.5381 0.6021 -0.0003 -0.0804 0.0448  239 ILE B O   
3375 C CB  . ILE B 165 ? 0.6125 0.5063 0.5289 -0.0012 -0.1100 0.0476  239 ILE B CB  
3376 C CG1 . ILE B 165 ? 0.5936 0.4832 0.4902 -0.0009 -0.1156 0.0533  239 ILE B CG1 
3377 C CG2 . ILE B 165 ? 0.5954 0.4645 0.4919 -0.0034 -0.1258 0.0372  239 ILE B CG2 
3378 C CD1 . ILE B 165 ? 0.6488 0.5171 0.4986 -0.0030 -0.1090 0.0567  239 ILE B CD1 
3379 N N   . PHE B 166 ? 0.6037 0.5165 0.6085 -0.0078 -0.1163 0.0276  240 PHE B N   
3380 C CA  . PHE B 166 ? 0.6243 0.5349 0.6536 -0.0137 -0.1062 0.0194  240 PHE B CA  
3381 C C   . PHE B 166 ? 0.6816 0.5724 0.6963 -0.0213 -0.1219 0.0043  240 PHE B C   
3382 O O   . PHE B 166 ? 0.7344 0.6281 0.7488 -0.0224 -0.1484 -0.0040 240 PHE B O   
3383 C CB  . PHE B 166 ? 0.5792 0.5127 0.6591 -0.0163 -0.1051 0.0161  240 PHE B CB  
3384 C CG  . PHE B 166 ? 0.5654 0.5160 0.6552 -0.0094 -0.0898 0.0294  240 PHE B CG  
3385 C CD1 . PHE B 166 ? 0.5900 0.5412 0.6834 -0.0064 -0.0639 0.0375  240 PHE B CD1 
3386 C CD2 . PHE B 166 ? 0.5889 0.5521 0.6804 -0.0050 -0.1011 0.0336  240 PHE B CD2 
3387 C CE1 . PHE B 166 ? 0.5825 0.5507 0.6811 0.0003  -0.0520 0.0486  240 PHE B CE1 
3388 C CE2 . PHE B 166 ? 0.5354 0.5131 0.6333 -0.0005 -0.0872 0.0434  240 PHE B CE2 
3389 C CZ  . PHE B 166 ? 0.5363 0.5186 0.6377 0.0018  -0.0639 0.0504  240 PHE B CZ  
3390 N N   . LEU B 167 ? 0.6877 0.5577 0.6888 -0.0252 -0.1058 0.0005  241 LEU B N   
3391 C CA  . LEU B 167 ? 0.7216 0.5669 0.6968 -0.0329 -0.1178 -0.0141 241 LEU B CA  
3392 C C   . LEU B 167 ? 0.7348 0.5879 0.7473 -0.0464 -0.1306 -0.0336 241 LEU B C   
3393 O O   . LEU B 167 ? 0.6878 0.5532 0.7424 -0.0518 -0.1160 -0.0356 241 LEU B O   
3394 C CB  . LEU B 167 ? 0.7207 0.5370 0.6646 -0.0314 -0.0927 -0.0114 241 LEU B CB  
3395 C CG  . LEU B 167 ? 0.7416 0.5592 0.6594 -0.0180 -0.0758 0.0070  241 LEU B CG  
3396 C CD1 . LEU B 167 ? 0.7804 0.5681 0.6651 -0.0148 -0.0550 0.0069  241 LEU B CD1 
3397 C CD2 . LEU B 167 ? 0.7194 0.5422 0.6118 -0.0144 -0.0940 0.0119  241 LEU B CD2 
3398 N N   . GLY B 168 ? 0.7799 0.6263 0.7761 -0.0521 -0.1577 -0.0486 242 GLY B N   
3399 C CA  . GLY B 168 ? 0.8089 0.6656 0.8384 -0.0670 -0.1729 -0.0712 242 GLY B CA  
3400 C C   . GLY B 168 ? 0.8626 0.6859 0.8563 -0.0783 -0.1734 -0.0875 242 GLY B C   
3401 O O   . GLY B 168 ? 0.9160 0.7069 0.8584 -0.0726 -0.1606 -0.0798 242 GLY B O   
3402 N N   . PRO B 169 ? 0.8452 0.6764 0.8661 -0.0955 -0.1871 -0.1117 243 PRO B N   
3403 C CA  . PRO B 169 ? 0.8345 0.6318 0.8195 -0.1090 -0.1883 -0.1308 243 PRO B CA  
3404 C C   . PRO B 169 ? 0.8658 0.6489 0.7927 -0.1011 -0.2172 -0.1329 243 PRO B C   
3405 O O   . PRO B 169 ? 0.9197 0.7228 0.8413 -0.0877 -0.2422 -0.1238 243 PRO B O   
3406 C CB  . PRO B 169 ? 0.8159 0.6360 0.8538 -0.1313 -0.2000 -0.1584 243 PRO B CB  
3407 C CG  . PRO B 169 ? 0.7287 0.6009 0.8220 -0.1247 -0.2194 -0.1545 243 PRO B CG  
3408 C CD  . PRO B 169 ? 0.7665 0.6393 0.8553 -0.1051 -0.1991 -0.1245 243 PRO B CD  
3409 N N   . ARG B 170 ? 0.9208 0.6635 0.7992 -0.1090 -0.2110 -0.1445 244 ARG B N   
3410 C CA  . ARG B 170 ? 0.9478 0.6686 0.7626 -0.1042 -0.2358 -0.1499 244 ARG B CA  
3411 C C   . ARG B 170 ? 0.9672 0.6787 0.7408 -0.0827 -0.2325 -0.1235 244 ARG B C   
3412 O O   . ARG B 170 ? 1.0291 0.7359 0.7629 -0.0741 -0.2595 -0.1222 244 ARG B O   
3413 C CB  . ARG B 170 ? 0.9735 0.7242 0.8030 -0.1100 -0.2817 -0.1702 244 ARG B CB  
3414 C CG  . ARG B 170 ? 1.0458 0.8028 0.9056 -0.1356 -0.2887 -0.2027 244 ARG B CG  
3415 C CD  . ARG B 170 ? 1.0432 0.8483 0.9281 -0.1363 -0.3288 -0.2179 244 ARG B CD  
3416 N NE  . ARG B 170 ? 1.2457 1.0581 1.1425 -0.1603 -0.3309 -0.2479 244 ARG B NE  
3417 C CZ  . ARG B 170 ? 1.2478 1.1041 1.1616 -0.1638 -0.3581 -0.2626 244 ARG B CZ  
3418 N NH1 . ARG B 170 ? 1.2221 1.1159 1.1431 -0.1421 -0.3848 -0.2491 244 ARG B NH1 
3419 N NH2 . ARG B 170 ? 1.1507 1.0107 1.0722 -0.1900 -0.3574 -0.2914 244 ARG B NH2 
3420 N N   . GLY B 171 ? 0.9537 0.6623 0.7353 -0.0740 -0.1991 -0.1026 245 GLY B N   
3421 C CA  . GLY B 171 ? 0.9312 0.6320 0.6771 -0.0576 -0.1910 -0.0801 245 GLY B CA  
3422 C C   . GLY B 171 ? 0.9690 0.7007 0.7349 -0.0466 -0.2096 -0.0666 245 GLY B C   
3423 O O   . GLY B 171 ? 0.9230 0.6462 0.6577 -0.0355 -0.2031 -0.0495 245 GLY B O   
3424 N N   . ARG B 172 ? 0.9450 0.7112 0.7623 -0.0499 -0.2304 -0.0745 246 ARG B N   
3425 C CA  . ARG B 172 ? 0.9068 0.7009 0.7473 -0.0381 -0.2446 -0.0618 246 ARG B CA  
3426 C C   . ARG B 172 ? 0.8276 0.6379 0.7014 -0.0339 -0.2152 -0.0444 246 ARG B C   
3427 O O   . ARG B 172 ? 0.8215 0.6283 0.7106 -0.0394 -0.1875 -0.0433 246 ARG B O   
3428 C CB  . ARG B 172 ? 0.9252 0.7544 0.8143 -0.0414 -0.2750 -0.0770 246 ARG B CB  
3429 C CG  . ARG B 172 ? 0.9514 0.7739 0.8182 -0.0483 -0.3062 -0.0993 246 ARG B CG  
3430 C CD  . ARG B 172 ? 1.0327 0.8222 0.8236 -0.0360 -0.3234 -0.0924 246 ARG B CD  
3431 N NE  . ARG B 172 ? 1.0454 0.8435 0.8302 -0.0172 -0.3366 -0.0746 246 ARG B NE  
3432 C CZ  . ARG B 172 ? 1.0473 0.8747 0.8563 -0.0059 -0.3561 -0.0757 246 ARG B CZ  
3433 N NH1 . ARG B 172 ? 1.0049 0.8623 0.8480 -0.0127 -0.3739 -0.0955 246 ARG B NH1 
3434 N NH2 . ARG B 172 ? 1.0274 0.8527 0.8248 0.0121  -0.3562 -0.0573 246 ARG B NH2 
3435 N N   . CYS B 173 ? 0.8298 0.6560 0.7119 -0.0231 -0.2215 -0.0308 247 CYS B N   
3436 C CA  . CYS B 173 ? 0.7729 0.6191 0.6885 -0.0197 -0.1987 -0.0167 247 CYS B CA  
3437 C C   . CYS B 173 ? 0.7112 0.5794 0.6502 -0.0110 -0.2157 -0.0111 247 CYS B C   
3438 O O   . CYS B 173 ? 0.7483 0.6106 0.6670 -0.0041 -0.2424 -0.0135 247 CYS B O   
3439 C CB  . CYS B 173 ? 0.7809 0.6110 0.6614 -0.0153 -0.1731 -0.0014 247 CYS B CB  
3440 S SG  . CYS B 173 ? 0.8553 0.6661 0.6825 -0.0067 -0.1822 0.0106  247 CYS B SG  
3441 N N   . LYS B 174 ? 0.7156 0.6066 0.6940 -0.0096 -0.1993 -0.0031 248 LYS B N   
3442 C CA  . LYS B 174 ? 0.6351 0.5468 0.6417 -0.0016 -0.2105 0.0011  248 LYS B CA  
3443 C C   . LYS B 174 ? 0.6155 0.5293 0.6175 0.0023  -0.1888 0.0169  248 LYS B C   
3444 O O   . LYS B 174 ? 0.6834 0.5998 0.6882 -0.0018 -0.1642 0.0221  248 LYS B O   
3445 C CB  . LYS B 174 ? 0.6154 0.5590 0.6862 -0.0062 -0.2140 -0.0102 248 LYS B CB  
3446 C CG  . LYS B 174 ? 0.6547 0.6042 0.7394 -0.0136 -0.2359 -0.0297 248 LYS B CG  
3447 C CD  . LYS B 174 ? 0.6143 0.6013 0.7682 -0.0181 -0.2411 -0.0419 248 LYS B CD  
3448 C CE  . LYS B 174 ? 0.6724 0.6687 0.8449 -0.0310 -0.2584 -0.0646 248 LYS B CE  
3449 N NZ  . LYS B 174 ? 0.7566 0.7958 1.0012 -0.0358 -0.2669 -0.0790 248 LYS B NZ  
3450 N N   . LEU B 175 ? 0.6284 0.5402 0.6219 0.0110  -0.1984 0.0238  249 LEU B N   
3451 C CA  . LEU B 175 ? 0.5976 0.5130 0.5901 0.0126  -0.1799 0.0355  249 LEU B CA  
3452 C C   . LEU B 175 ? 0.5799 0.5239 0.6262 0.0134  -0.1732 0.0337  249 LEU B C   
3453 O O   . LEU B 175 ? 0.6313 0.5890 0.7102 0.0180  -0.1893 0.0264  249 LEU B O   
3454 C CB  . LEU B 175 ? 0.6143 0.5069 0.5692 0.0199  -0.1893 0.0429  249 LEU B CB  
3455 C CG  . LEU B 175 ? 0.6539 0.5445 0.5997 0.0181  -0.1700 0.0526  249 LEU B CG  
3456 C CD1 . LEU B 175 ? 0.5724 0.4659 0.5018 0.0087  -0.1469 0.0567  249 LEU B CD1 
3457 C CD2 . LEU B 175 ? 0.7338 0.5931 0.6397 0.0248  -0.1792 0.0586  249 LEU B CD2 
3458 N N   . GLY B 176 ? 0.3713 0.5047 0.7784 -0.0300 -0.0911 -0.0007 250 GLY B N   
3459 C CA  . GLY B 176 ? 0.3660 0.4964 0.8024 -0.0490 -0.0633 0.0347  250 GLY B CA  
3460 C C   . GLY B 176 ? 0.4110 0.5325 0.7887 -0.0494 -0.0251 0.0440  250 GLY B C   
3461 O O   . GLY B 176 ? 0.4155 0.5324 0.7400 -0.0421 -0.0184 0.0274  250 GLY B O   
3462 N N   . ASP B 177 ? 0.4537 0.5779 0.8454 -0.0558 -0.0031 0.0737  251 ASP B N   
3463 C CA  . ASP B 177 ? 0.4719 0.5884 0.8061 -0.0487 0.0276  0.0787  251 ASP B CA  
3464 C C   . ASP B 177 ? 0.4525 0.5608 0.7395 -0.0367 0.0443  0.0645  251 ASP B C   
3465 O O   . ASP B 177 ? 0.4143 0.5045 0.6606 -0.0384 0.0368  0.0427  251 ASP B O   
3466 C CB  . ASP B 177 ? 0.4725 0.5693 0.7696 -0.0530 0.0157  0.0621  251 ASP B CB  
3467 C CG  . ASP B 177 ? 0.6148 0.7082 0.8645 -0.0449 0.0409  0.0701  251 ASP B CG  
3468 O OD1 . ASP B 177 ? 0.6570 0.7593 0.8907 -0.0298 0.0660  0.0820  251 ASP B OD1 
3469 O OD2 . ASP B 177 ? 0.7093 0.7937 0.9332 -0.0476 0.0336  0.0624  251 ASP B OD2 
3470 N N   . PHE B 178 ? 0.4660 0.5901 0.7648 -0.0236 0.0647  0.0816  252 PHE B N   
3471 C CA  . PHE B 178 ? 0.4636 0.5709 0.7223 -0.0083 0.0767  0.0693  252 PHE B CA  
3472 C C   . PHE B 178 ? 0.4612 0.5480 0.6622 0.0133  0.0956  0.0660  252 PHE B C   
3473 O O   . PHE B 178 ? 0.5142 0.5908 0.6896 0.0376  0.1083  0.0637  252 PHE B O   
3474 C CB  . PHE B 178 ? 0.4237 0.5593 0.7220 0.0016  0.0841  0.0848  252 PHE B CB  
3475 C CG  . PHE B 178 ? 0.4219 0.5759 0.7703 -0.0121 0.0579  0.0792  252 PHE B CG  
3476 C CD1 . PHE B 178 ? 0.4346 0.5763 0.7624 -0.0148 0.0397  0.0555  252 PHE B CD1 
3477 C CD2 . PHE B 178 ? 0.4401 0.6302 0.8590 -0.0182 0.0485  0.0999  252 PHE B CD2 
3478 C CE1 . PHE B 178 ? 0.4328 0.5980 0.7950 -0.0138 0.0131  0.0454  252 PHE B CE1 
3479 C CE2 . PHE B 178 ? 0.4003 0.6022 0.8609 -0.0247 0.0148  0.0856  252 PHE B CE2 
3480 C CZ  . PHE B 178 ? 0.3971 0.5866 0.8221 -0.0177 -0.0025 0.0547  252 PHE B CZ  
3481 N N   . GLY B 179 ? 0.5342 0.6143 0.7099 0.0109  0.0947  0.0626  253 GLY B N   
3482 C CA  . GLY B 179 ? 0.5073 0.5723 0.6228 0.0399  0.1071  0.0541  253 GLY B CA  
3483 C C   . GLY B 179 ? 0.5256 0.5336 0.5908 0.0421  0.0896  0.0188  253 GLY B C   
3484 O O   . GLY B 179 ? 0.6412 0.6239 0.6591 0.0754  0.0928  0.0042  253 GLY B O   
3485 N N   . LEU B 180 ? 0.5191 0.5083 0.5970 0.0102  0.0676  0.0073  254 LEU B N   
3486 C CA  . LEU B 180 ? 0.5477 0.4874 0.6001 0.0030  0.0460  -0.0138 254 LEU B CA  
3487 C C   . LEU B 180 ? 0.5842 0.5079 0.6561 0.0043  0.0446  -0.0089 254 LEU B C   
3488 O O   . LEU B 180 ? 0.6183 0.4984 0.6837 -0.0049 0.0239  -0.0176 254 LEU B O   
3489 C CB  . LEU B 180 ? 0.5556 0.5001 0.6195 -0.0298 0.0254  -0.0155 254 LEU B CB  
3490 C CG  . LEU B 180 ? 0.6608 0.6109 0.6989 -0.0337 0.0190  -0.0245 254 LEU B CG  
3491 C CD1 . LEU B 180 ? 0.7009 0.6591 0.7516 -0.0632 -0.0034 -0.0230 254 LEU B CD1 
3492 C CD2 . LEU B 180 ? 0.6719 0.5860 0.6571 -0.0076 0.0145  -0.0471 254 LEU B CD2 
3493 N N   . LEU B 181 ? 0.5820 0.5405 0.6838 0.0146  0.0630  0.0081  255 LEU B N   
3494 C CA  . LEU B 181 ? 0.5989 0.5525 0.7223 0.0160  0.0622  0.0157  255 LEU B CA  
3495 C C   . LEU B 181 ? 0.6676 0.5632 0.7539 0.0412  0.0583  0.0022  255 LEU B C   
3496 O O   . LEU B 181 ? 0.6529 0.5352 0.6992 0.0748  0.0674  -0.0094 255 LEU B O   
3497 C CB  . LEU B 181 ? 0.4961 0.5028 0.6600 0.0243  0.0789  0.0342  255 LEU B CB  
3498 C CG  . LEU B 181 ? 0.5094 0.5262 0.6985 0.0282  0.0786  0.0435  255 LEU B CG  
3499 C CD1 . LEU B 181 ? 0.4613 0.5354 0.6991 0.0193  0.0740  0.0529  255 LEU B CD1 
3500 C CD2 . LEU B 181 ? 0.5320 0.5369 0.7061 0.0609  0.0953  0.0472  255 LEU B CD2 
3501 N N   . VAL B 182 ? 0.6450 0.5074 0.7447 0.0298  0.0423  0.0058  256 VAL B N   
3502 C CA  . VAL B 182 ? 0.6983 0.4931 0.7714 0.0535  0.0307  -0.0066 256 VAL B CA  
3503 C C   . VAL B 182 ? 0.7219 0.5309 0.8281 0.0585  0.0403  0.0164  256 VAL B C   
3504 O O   . VAL B 182 ? 0.6986 0.5587 0.8486 0.0367  0.0448  0.0403  256 VAL B O   
3505 C CB  . VAL B 182 ? 0.7357 0.4571 0.8004 0.0333  -0.0088 -0.0213 256 VAL B CB  
3506 C CG1 . VAL B 182 ? 0.8454 0.5579 0.8750 0.0307  -0.0210 -0.0465 256 VAL B CG1 
3507 C CG2 . VAL B 182 ? 0.6963 0.4381 0.8201 -0.0088 -0.0210 0.0119  256 VAL B CG2 
3508 N N   . GLU B 183 ? 0.7626 0.5290 0.8422 0.0951  0.0422  0.0077  257 GLU B N   
3509 C CA  . GLU B 183 ? 0.7850 0.5516 0.8899 0.1048  0.0481  0.0287  257 GLU B CA  
3510 C C   . GLU B 183 ? 0.8603 0.5377 0.9680 0.0961  0.0139  0.0276  257 GLU B C   
3511 O O   . GLU B 183 ? 0.9515 0.5472 1.0176 0.1120  -0.0131 -0.0042 257 GLU B O   
3512 C CB  . GLU B 183 ? 0.7941 0.5774 0.8729 0.1545  0.0728  0.0254  257 GLU B CB  
3513 C CG  . GLU B 183 ? 0.8901 0.6833 0.9947 0.1680  0.0816  0.0482  257 GLU B CG  
3514 C CD  . GLU B 183 ? 1.0097 0.8229 1.0870 0.2212  0.1052  0.0469  257 GLU B CD  
3515 O OE1 . GLU B 183 ? 1.0964 0.9196 1.1344 0.2509  0.1155  0.0318  257 GLU B OE1 
3516 O OE2 . GLU B 183 ? 1.1039 0.9322 1.1993 0.2376  0.1150  0.0654  257 GLU B OE2 
3517 N N   . LEU B 184 ? 0.8333 0.5278 0.9931 0.0734  0.0109  0.0641  258 LEU B N   
3518 C CA  . LEU B 184 ? 0.9439 0.5595 1.1286 0.0584  -0.0234 0.0788  258 LEU B CA  
3519 C C   . LEU B 184 ? 1.0814 0.6337 1.2417 0.1019  -0.0254 0.0706  258 LEU B C   
3520 O O   . LEU B 184 ? 1.1085 0.7081 1.2859 0.1199  0.0010  0.0963  258 LEU B O   
3521 C CB  . LEU B 184 ? 0.8656 0.5423 1.1204 0.0232  -0.0210 0.1339  258 LEU B CB  
3522 C CG  . LEU B 184 ? 0.7972 0.5532 1.0705 -0.0078 -0.0149 0.1437  258 LEU B CG  
3523 C CD1 . LEU B 184 ? 0.6804 0.5115 1.0161 -0.0265 -0.0102 0.2028  258 LEU B CD1 
3524 C CD2 . LEU B 184 ? 0.7915 0.4923 1.0511 -0.0335 -0.0465 0.1188  258 LEU B CD2 
3525 N N   . GLY B 185 ? 1.2277 0.6728 1.3443 0.1243  -0.0601 0.0319  259 GLY B N   
3526 C CA  . GLY B 185 ? 1.3152 0.6913 1.3956 0.1765  -0.0666 0.0162  259 GLY B CA  
3527 C C   . GLY B 185 ? 1.5673 0.8874 1.7051 0.1593  -0.0907 0.0552  259 GLY B C   
3528 O O   . GLY B 185 ? 1.5449 0.9075 1.7562 0.1104  -0.0910 0.1059  259 GLY B O   
3529 N N   . THR B 186 ? 1.7143 0.9410 1.8170 0.2068  -0.1110 0.0347  260 THR B N   
3530 C CA  . THR B 186 ? 1.7564 0.9133 1.9156 0.1945  -0.1391 0.0735  260 THR B CA  
3531 C C   . THR B 186 ? 1.7900 0.8722 2.0142 0.1345  -0.1971 0.0899  260 THR B C   
3532 O O   . THR B 186 ? 1.7830 0.9013 2.0882 0.0892  -0.1970 0.1543  260 THR B O   
3533 C CB  . THR B 186 ? 1.7182 0.7699 1.8187 0.2630  -0.1593 0.0389  260 THR B CB  
3534 O OG1 . THR B 186 ? 1.7445 0.7124 1.7765 0.2869  -0.1997 -0.0293 260 THR B OG1 
3535 C CG2 . THR B 186 ? 1.6437 0.7864 1.6940 0.3209  -0.0998 0.0360  260 THR B CG2 
3536 N N   . ALA B 187 ? 1.8022 0.8278 1.9815 0.1309  -0.2341 0.0338  261 ALA B N   
3537 C CA  . ALA B 187 ? 1.8498 0.8461 2.0803 0.0714  -0.2820 0.0423  261 ALA B CA  
3538 C C   . ALA B 187 ? 1.8838 0.9386 2.1285 0.0311  -0.2811 0.0397  261 ALA B C   
3539 O O   . ALA B 187 ? 1.8589 0.9804 2.1840 -0.0266 -0.2791 0.0962  261 ALA B O   
3540 C CB  . ALA B 187 ? 1.8706 0.7555 2.0508 0.0988  -0.3378 -0.0187 261 ALA B CB  
3541 N N   . GLY B 188 ? 1.9840 1.0266 2.1496 0.0654  -0.2796 -0.0216 262 GLY B N   
3542 C CA  . GLY B 188 ? 1.9662 1.0461 2.1335 0.0322  -0.2872 -0.0347 262 GLY B CA  
3543 C C   . GLY B 188 ? 1.8969 1.0932 2.0265 0.0489  -0.2222 -0.0352 262 GLY B C   
3544 O O   . GLY B 188 ? 1.8460 1.0868 1.9384 0.0923  -0.1770 -0.0365 262 GLY B O   
3545 N N   . ALA B 189 ? 1.6372 0.8950 1.7808 0.0117  -0.2175 -0.0310 263 ALA B N   
3546 C CA  . ALA B 189 ? 1.4469 0.8111 1.5538 0.0249  -0.1635 -0.0366 263 ALA B CA  
3547 C C   . ALA B 189 ? 1.5322 0.8696 1.5484 0.0767  -0.1646 -0.0969 263 ALA B C   
3548 O O   . ALA B 189 ? 1.4195 0.8334 1.4014 0.1052  -0.1172 -0.0987 263 ALA B O   
3549 C CB  . ALA B 189 ? 1.2371 0.6791 1.3926 -0.0289 -0.1578 -0.0059 263 ALA B CB  
3550 N N   . GLY B 190 ? 1.6384 0.8739 1.6192 0.0921  -0.2205 -0.1433 264 GLY B N   
3551 C CA  . GLY B 190 ? 1.6781 0.8892 1.5615 0.1581  -0.2249 -0.2026 264 GLY B CA  
3552 C C   . GLY B 190 ? 1.6272 0.8852 1.4913 0.1429  -0.2245 -0.2181 264 GLY B C   
3553 O O   . GLY B 190 ? 1.5978 0.8161 1.4931 0.1001  -0.2717 -0.2257 264 GLY B O   
3554 N N   . GLU B 191 ? 1.5138 0.8595 1.3337 0.1773  -0.1728 -0.2174 265 GLU B N   
3555 C CA  . GLU B 191 ? 1.4492 0.8422 1.2414 0.1754  -0.1675 -0.2310 265 GLU B CA  
3556 C C   . GLU B 191 ? 1.2748 0.7601 1.1343 0.1139  -0.1321 -0.1814 265 GLU B C   
3557 O O   . GLU B 191 ? 1.2094 0.7745 1.0843 0.1180  -0.0813 -0.1497 265 GLU B O   
3558 C CB  . GLU B 191 ? 1.5225 0.9614 1.2330 0.2528  -0.1341 -0.2507 265 GLU B CB  
3559 C CG  . GLU B 191 ? 1.5748 1.0732 1.2572 0.2570  -0.1224 -0.2565 265 GLU B CG  
3560 C CD  . GLU B 191 ? 1.6859 1.2031 1.2722 0.3482  -0.1132 -0.2883 265 GLU B CD  
3561 O OE1 . GLU B 191 ? 1.6174 1.1104 1.1562 0.4125  -0.1113 -0.3046 265 GLU B OE1 
3562 O OE2 . GLU B 191 ? 1.6337 1.1965 1.1893 0.3615  -0.1069 -0.2943 265 GLU B OE2 
3563 N N   . VAL B 192 ? 1.2549 0.7301 1.1560 0.0601  -0.1635 -0.1753 266 VAL B N   
3564 C CA  . VAL B 192 ? 1.1178 0.6774 1.0709 0.0113  -0.1379 -0.1353 266 VAL B CA  
3565 C C   . VAL B 192 ? 1.0810 0.6643 1.0001 0.0129  -0.1446 -0.1562 266 VAL B C   
3566 O O   . VAL B 192 ? 1.1424 0.6666 1.0354 0.0172  -0.1916 -0.1922 266 VAL B O   
3567 C CB  . VAL B 192 ? 0.9958 0.5493 1.0283 -0.0468 -0.1629 -0.0989 266 VAL B CB  
3568 C CG1 . VAL B 192 ? 0.9609 0.6046 1.0312 -0.0837 -0.1422 -0.0651 266 VAL B CG1 
3569 C CG2 . VAL B 192 ? 1.0419 0.5884 1.1100 -0.0453 -0.1491 -0.0700 266 VAL B CG2 
3570 N N   . GLN B 193 ? 0.9666 0.6323 0.8885 0.0101  -0.1030 -0.1345 267 GLN B N   
3571 C CA  . GLN B 193 ? 0.9541 0.6515 0.8497 0.0102  -0.1041 -0.1455 267 GLN B CA  
3572 C C   . GLN B 193 ? 0.8974 0.6321 0.8465 -0.0442 -0.1143 -0.1195 267 GLN B C   
3573 O O   . GLN B 193 ? 0.8435 0.6000 0.8486 -0.0758 -0.1098 -0.0865 267 GLN B O   
3574 C CB  . GLN B 193 ? 0.9490 0.7118 0.8201 0.0428  -0.0561 -0.1325 267 GLN B CB  
3575 C CG  . GLN B 193 ? 1.0366 0.7896 0.8585 0.1035  -0.0387 -0.1458 267 GLN B CG  
3576 C CD  . GLN B 193 ? 1.0812 0.9112 0.8924 0.1328  0.0062  -0.1200 267 GLN B CD  
3577 O OE1 . GLN B 193 ? 1.1967 1.0622 1.0016 0.1274  0.0118  -0.1139 267 GLN B OE1 
3578 N NE2 . GLN B 193 ? 1.0550 0.9160 0.8718 0.1631  0.0379  -0.0985 267 GLN B NE2 
3579 N N   . GLU B 194 ? 0.9711 0.7219 0.8983 -0.0477 -0.1272 -0.1329 268 GLU B N   
3580 C CA  . GLU B 194 ? 0.8505 0.6433 0.8210 -0.0917 -0.1392 -0.1093 268 GLU B CA  
3581 C C   . GLU B 194 ? 0.7811 0.6481 0.7759 -0.0984 -0.0985 -0.0753 268 GLU B C   
3582 O O   . GLU B 194 ? 0.7967 0.6892 0.7651 -0.0727 -0.0680 -0.0769 268 GLU B O   
3583 C CB  . GLU B 194 ? 0.8827 0.6767 0.8174 -0.0868 -0.1628 -0.1351 268 GLU B CB  
3584 C CG  . GLU B 194 ? 1.0033 0.7178 0.9013 -0.0682 -0.2126 -0.1825 268 GLU B CG  
3585 C CD  . GLU B 194 ? 1.0687 0.7562 1.0176 -0.1156 -0.2711 -0.1812 268 GLU B CD  
3586 O OE1 . GLU B 194 ? 0.9368 0.6777 0.9528 -0.1612 -0.2656 -0.1343 268 GLU B OE1 
3587 O OE2 . GLU B 194 ? 1.0767 0.6941 1.0009 -0.1040 -0.3257 -0.2256 268 GLU B OE2 
3588 N N   . GLY B 195 ? 0.7528 0.6568 0.8010 -0.1295 -0.1015 -0.0421 269 GLY B N   
3589 C CA  . GLY B 195 ? 0.6649 0.6341 0.7312 -0.1282 -0.0737 -0.0176 269 GLY B CA  
3590 C C   . GLY B 195 ? 0.6779 0.7006 0.7450 -0.1384 -0.0786 -0.0077 269 GLY B C   
3591 O O   . GLY B 195 ? 0.7067 0.7248 0.7665 -0.1514 -0.1018 -0.0151 269 GLY B O   
3592 N N   . ASP B 196 ? 0.7395 0.8572 0.5928 0.0767  -0.0541 0.0813  270 ASP B N   
3593 C CA  . ASP B 196 ? 0.6561 0.7718 0.5152 0.0775  -0.0505 0.0832  270 ASP B CA  
3594 C C   . ASP B 196 ? 0.6242 0.7375 0.5014 0.0661  -0.0534 0.0694  270 ASP B C   
3595 O O   . ASP B 196 ? 0.6222 0.7155 0.4995 0.0489  -0.0485 0.0692  270 ASP B O   
3596 C CB  . ASP B 196 ? 0.6535 0.7478 0.5053 0.0692  -0.0387 0.0988  270 ASP B CB  
3597 C CG  . ASP B 196 ? 0.6629 0.7524 0.5130 0.0803  -0.0349 0.1035  270 ASP B CG  
3598 O OD1 . ASP B 196 ? 0.6661 0.7689 0.5314 0.0871  -0.0384 0.0921  270 ASP B OD1 
3599 O OD2 . ASP B 196 ? 0.7613 0.8333 0.5966 0.0821  -0.0290 0.1191  270 ASP B OD2 
3600 N N   . PRO B 197 ? 0.6438 0.7786 0.5367 0.0738  -0.0616 0.0586  271 PRO B N   
3601 C CA  . PRO B 197 ? 0.5985 0.7383 0.5162 0.0581  -0.0621 0.0473  271 PRO B CA  
3602 C C   . PRO B 197 ? 0.6201 0.7505 0.5449 0.0486  -0.0443 0.0529  271 PRO B C   
3603 O O   . PRO B 197 ? 0.6262 0.7518 0.5620 0.0301  -0.0377 0.0485  271 PRO B O   
3604 C CB  . PRO B 197 ? 0.6034 0.7773 0.5419 0.0702  -0.0770 0.0358  271 PRO B CB  
3605 C CG  . PRO B 197 ? 0.6324 0.8135 0.5528 0.0951  -0.0788 0.0454  271 PRO B CG  
3606 C CD  . PRO B 197 ? 0.6383 0.7961 0.5275 0.0959  -0.0720 0.0572  271 PRO B CD  
3607 N N   . ARG B 198 ? 0.6631 0.7863 0.5775 0.0609  -0.0356 0.0626  272 ARG B N   
3608 C CA  . ARG B 198 ? 0.5810 0.6898 0.4952 0.0562  -0.0187 0.0645  272 ARG B CA  
3609 C C   . ARG B 198 ? 0.6236 0.6996 0.5178 0.0347  -0.0108 0.0669  272 ARG B C   
3610 O O   . ARG B 198 ? 0.5823 0.6517 0.4773 0.0250  0.0029  0.0636  272 ARG B O   
3611 C CB  . ARG B 198 ? 0.5948 0.6867 0.4923 0.0737  -0.0143 0.0742  272 ARG B CB  
3612 C CG  . ARG B 198 ? 0.6722 0.7918 0.5834 0.0986  -0.0236 0.0742  272 ARG B CG  
3613 C CD  . ARG B 198 ? 0.7073 0.7982 0.5943 0.1159  -0.0208 0.0873  272 ARG B CD  
3614 N NE  . ARG B 198 ? 0.7552 0.8221 0.6143 0.1089  -0.0235 0.1017  272 ARG B NE  
3615 C CZ  . ARG B 198 ? 0.7980 0.8425 0.6345 0.1205  -0.0242 0.1174  272 ARG B CZ  
3616 N NH1 . ARG B 198 ? 0.8370 0.8737 0.6704 0.1437  -0.0256 0.1203  272 ARG B NH1 
3617 N NH2 . ARG B 198 ? 0.7766 0.8066 0.5944 0.1087  -0.0231 0.1316  272 ARG B NH2 
3618 N N   . TYR B 199 ? 0.6248 0.6831 0.5004 0.0287  -0.0192 0.0727  273 TYR B N   
3619 C CA  . TYR B 199 ? 0.5882 0.6150 0.4423 0.0116  -0.0172 0.0762  273 TYR B CA  
3620 C C   . TYR B 199 ? 0.6168 0.6417 0.4728 0.0010  -0.0265 0.0719  273 TYR B C   
3621 O O   . TYR B 199 ? 0.6689 0.6677 0.5052 -0.0096 -0.0298 0.0759  273 TYR B O   
3622 C CB  . TYR B 199 ? 0.6037 0.6134 0.4403 0.0120  -0.0218 0.0867  273 TYR B CB  
3623 C CG  . TYR B 199 ? 0.6003 0.6003 0.4304 0.0212  -0.0152 0.0925  273 TYR B CG  
3624 C CD1 . TYR B 199 ? 0.5903 0.6087 0.4285 0.0372  -0.0178 0.0983  273 TYR B CD1 
3625 C CD2 . TYR B 199 ? 0.5811 0.5469 0.3904 0.0155  -0.0072 0.0921  273 TYR B CD2 
3626 C CE1 . TYR B 199 ? 0.6335 0.6336 0.4611 0.0464  -0.0131 0.1058  273 TYR B CE1 
3627 C CE2 . TYR B 199 ? 0.6247 0.5711 0.4239 0.0254  -0.0030 0.0963  273 TYR B CE2 
3628 C CZ  . TYR B 199 ? 0.6808 0.6429 0.4901 0.0404  -0.0062 0.1043  273 TYR B CZ  
3629 O OH  . TYR B 199 ? 0.7224 0.6560 0.5171 0.0511  -0.0033 0.1107  273 TYR B OH  
3630 N N   . MET B 200 ? 0.6182 0.6660 0.4953 0.0041  -0.0333 0.0633  274 MET B N   
3631 C CA  . MET B 200 ? 0.5824 0.6202 0.4581 -0.0033 -0.0457 0.0578  274 MET B CA  
3632 C C   . MET B 200 ? 0.6768 0.6915 0.5474 -0.0255 -0.0385 0.0583  274 MET B C   
3633 O O   . MET B 200 ? 0.6301 0.6597 0.5183 -0.0346 -0.0258 0.0561  274 MET B O   
3634 C CB  . MET B 200 ? 0.6340 0.6979 0.5295 0.0062  -0.0583 0.0461  274 MET B CB  
3635 C CG  . MET B 200 ? 0.6900 0.7356 0.5825 -0.0015 -0.0730 0.0369  274 MET B CG  
3636 S SD  . MET B 200 ? 0.8295 0.8998 0.7321 0.0157  -0.0930 0.0202  274 MET B SD  
3637 C CE  . MET B 200 ? 0.7312 0.8369 0.6736 0.0038  -0.0908 0.0140  274 MET B CE  
3638 N N   . ALA B 201 ? 0.6629 0.6432 0.5099 -0.0330 -0.0461 0.0624  275 ALA B N   
3639 C CA  . ALA B 201 ? 0.6964 0.6463 0.5300 -0.0544 -0.0409 0.0661  275 ALA B CA  
3640 C C   . ALA B 201 ? 0.7143 0.6705 0.5713 -0.0658 -0.0470 0.0575  275 ALA B C   
3641 O O   . ALA B 201 ? 0.7335 0.6996 0.6022 -0.0543 -0.0642 0.0471  275 ALA B O   
3642 C CB  . ALA B 201 ? 0.7344 0.6423 0.5339 -0.0553 -0.0530 0.0733  275 ALA B CB  
3643 N N   . PRO B 202 ? 0.6871 0.6371 0.5498 -0.0898 -0.0331 0.0615  276 PRO B N   
3644 C CA  . PRO B 202 ? 0.6454 0.6076 0.5400 -0.1068 -0.0391 0.0534  276 PRO B CA  
3645 C C   . PRO B 202 ? 0.7464 0.6694 0.6272 -0.1079 -0.0645 0.0470  276 PRO B C   
3646 O O   . PRO B 202 ? 0.7608 0.6983 0.6661 -0.1084 -0.0805 0.0329  276 PRO B O   
3647 C CB  . PRO B 202 ? 0.7199 0.6759 0.6157 -0.1359 -0.0150 0.0646  276 PRO B CB  
3648 C CG  . PRO B 202 ? 0.7214 0.6761 0.5907 -0.1266 0.0059  0.0737  276 PRO B CG  
3649 C CD  . PRO B 202 ? 0.6617 0.5930 0.4999 -0.1040 -0.0109 0.0737  276 PRO B CD  
3650 N N   . GLU B 203 ? 0.7919 0.6630 0.6317 -0.1060 -0.0712 0.0556  277 GLU B N   
3651 C CA  . GLU B 203 ? 0.7870 0.6125 0.6103 -0.1044 -0.0950 0.0491  277 GLU B CA  
3652 C C   . GLU B 203 ? 0.8326 0.6758 0.6614 -0.0734 -0.1144 0.0324  277 GLU B C   
3653 O O   . GLU B 203 ? 0.8191 0.6327 0.6408 -0.0695 -0.1349 0.0198  277 GLU B O   
3654 C CB  . GLU B 203 ? 0.8200 0.5868 0.5973 -0.1040 -0.0993 0.0632  277 GLU B CB  
3655 C CG  . GLU B 203 ? 0.8715 0.6473 0.6315 -0.0757 -0.1033 0.0667  277 GLU B CG  
3656 C CD  . GLU B 203 ? 0.8449 0.6370 0.5962 -0.0822 -0.0830 0.0791  277 GLU B CD  
3657 O OE1 . GLU B 203 ? 0.8510 0.6586 0.6141 -0.1022 -0.0624 0.0825  277 GLU B OE1 
3658 O OE2 . GLU B 203 ? 0.8301 0.6202 0.5635 -0.0673 -0.0881 0.0846  277 GLU B OE2 
3659 N N   . LEU B 204 ? 0.8074 0.6942 0.6446 -0.0514 -0.1077 0.0321  278 LEU B N   
3660 C CA  . LEU B 204 ? 0.7555 0.6618 0.5930 -0.0218 -0.1213 0.0194  278 LEU B CA  
3661 C C   . LEU B 204 ? 0.7606 0.6823 0.6165 -0.0224 -0.1344 0.0010  278 LEU B C   
3662 O O   . LEU B 204 ? 0.8294 0.7473 0.6734 -0.0003 -0.1506 -0.0136 278 LEU B O   
3663 C CB  . LEU B 204 ? 0.7768 0.7258 0.6206 -0.0044 -0.1088 0.0266  278 LEU B CB  
3664 C CG  . LEU B 204 ? 0.7756 0.7143 0.6019 0.0022  -0.1040 0.0403  278 LEU B CG  
3665 C CD1 . LEU B 204 ? 0.7189 0.6977 0.5533 0.0207  -0.0974 0.0444  278 LEU B CD1 
3666 C CD2 . LEU B 204 ? 0.7994 0.7016 0.6052 0.0128  -0.1202 0.0377  278 LEU B CD2 
3667 N N   . LEU B 205 ? 0.7824 0.7236 0.6673 -0.0466 -0.1283 0.0005  279 LEU B N   
3668 C CA  . LEU B 205 ? 0.7749 0.7336 0.6819 -0.0505 -0.1458 -0.0180 279 LEU B CA  
3669 C C   . LEU B 205 ? 0.8513 0.7550 0.7405 -0.0592 -0.1691 -0.0315 279 LEU B C   
3670 O O   . LEU B 205 ? 0.9246 0.8290 0.8138 -0.0505 -0.1916 -0.0523 279 LEU B O   
3671 C CB  . LEU B 205 ? 0.7864 0.7837 0.7372 -0.0768 -0.1344 -0.0147 279 LEU B CB  
3672 C CG  . LEU B 205 ? 0.7263 0.7840 0.7013 -0.0606 -0.1225 -0.0118 279 LEU B CG  
3673 C CD1 . LEU B 205 ? 0.6681 0.7665 0.6924 -0.0849 -0.1129 -0.0111 279 LEU B CD1 
3674 C CD2 . LEU B 205 ? 0.7165 0.7956 0.6852 -0.0319 -0.1427 -0.0264 279 LEU B CD2 
3675 N N   . GLN B 206 ? 0.8424 0.6921 0.7107 -0.0749 -0.1661 -0.0204 280 GLN B N   
3676 C CA  . GLN B 206 ? 0.9116 0.6948 0.7576 -0.0840 -0.1885 -0.0307 280 GLN B CA  
3677 C C   . GLN B 206 ? 0.9751 0.7167 0.7783 -0.0492 -0.1996 -0.0345 280 GLN B C   
3678 O O   . GLN B 206 ? 1.0738 0.7469 0.8494 -0.0535 -0.2138 -0.0359 280 GLN B O   
3679 C CB  . GLN B 206 ? 0.9302 0.6733 0.7781 -0.1256 -0.1793 -0.0139 280 GLN B CB  
3680 C CG  . GLN B 206 ? 1.0567 0.8329 0.9527 -0.1644 -0.1755 -0.0161 280 GLN B CG  
3681 C CD  . GLN B 206 ? 0.9864 0.8443 0.9220 -0.1632 -0.1510 -0.0089 280 GLN B CD  
3682 O OE1 . GLN B 206 ? 0.9766 0.8449 0.9028 -0.1604 -0.1256 0.0096  280 GLN B OE1 
3683 N NE2 . GLN B 206 ? 0.8446 0.7573 0.8216 -0.1631 -0.1612 -0.0246 280 GLN B NE2 
3684 N N   . GLY B 207 ? 0.9669 0.7493 0.7659 -0.0148 -0.1928 -0.0351 281 GLY B N   
3685 C CA  . GLY B 207 ? 1.0414 0.8013 0.8098 0.0213  -0.2011 -0.0398 281 GLY B CA  
3686 C C   . GLY B 207 ? 0.9990 0.7217 0.7483 0.0211  -0.1972 -0.0213 281 GLY B C   
3687 O O   . GLY B 207 ? 1.1038 0.7902 0.8278 0.0473  -0.2108 -0.0271 281 GLY B O   
3688 N N   . SER B 208 ? 0.9508 0.6812 0.7086 -0.0044 -0.1799 -0.0001 282 SER B N   
3689 C CA  . SER B 208 ? 0.9763 0.6668 0.7091 -0.0072 -0.1790 0.0183  282 SER B CA  
3690 C C   . SER B 208 ? 0.9640 0.7022 0.7040 0.0089  -0.1662 0.0299  282 SER B C   
3691 O O   . SER B 208 ? 0.9681 0.7294 0.7163 -0.0095 -0.1487 0.0429  282 SER B O   
3692 C CB  . SER B 208 ? 0.9987 0.6556 0.7258 -0.0483 -0.1691 0.0338  282 SER B CB  
3693 O OG  . SER B 208 ? 1.1470 0.7507 0.8374 -0.0493 -0.1732 0.0510  282 SER B OG  
3694 N N   . TYR B 209 ? 0.9671 0.7197 0.7044 0.0434  -0.1752 0.0243  283 TYR B N   
3695 C CA  . TYR B 209 ? 0.8895 0.6934 0.6412 0.0571  -0.1654 0.0339  283 TYR B CA  
3696 C C   . TYR B 209 ? 0.8899 0.6674 0.6238 0.0606  -0.1742 0.0483  283 TYR B C   
3697 O O   . TYR B 209 ? 0.8931 0.6313 0.6085 0.0792  -0.1923 0.0451  283 TYR B O   
3698 C CB  . TYR B 209 ? 0.8987 0.7470 0.6644 0.0911  -0.1664 0.0214  283 TYR B CB  
3699 C CG  . TYR B 209 ? 0.8992 0.7753 0.6757 0.0906  -0.1599 0.0082  283 TYR B CG  
3700 C CD1 . TYR B 209 ? 0.9431 0.7877 0.7069 0.0943  -0.1737 -0.0113 283 TYR B CD1 
3701 C CD2 . TYR B 209 ? 0.9332 0.8621 0.7294 0.0865  -0.1431 0.0151  283 TYR B CD2 
3702 C CE1 . TYR B 209 ? 0.9513 0.8223 0.7227 0.0945  -0.1724 -0.0244 283 TYR B CE1 
3703 C CE2 . TYR B 209 ? 0.8534 0.8063 0.6556 0.0888  -0.1402 0.0043  283 TYR B CE2 
3704 C CZ  . TYR B 209 ? 0.9643 0.8912 0.7546 0.0933  -0.1558 -0.0158 283 TYR B CZ  
3705 O OH  . TYR B 209 ? 1.0573 1.0092 0.8515 0.0966  -0.1576 -0.0274 283 TYR B OH  
3706 N N   . GLY B 210 ? 0.8640 0.6594 0.6003 0.0447  -0.1640 0.0631  284 GLY B N   
3707 C CA  . GLY B 210 ? 0.8571 0.6315 0.5744 0.0471  -0.1755 0.0764  284 GLY B CA  
3708 C C   . GLY B 210 ? 0.8649 0.6768 0.5930 0.0352  -0.1649 0.0862  284 GLY B C   
3709 O O   . GLY B 210 ? 0.8366 0.6837 0.5842 0.0253  -0.1474 0.0840  284 GLY B O   
3710 N N   . THR B 211 ? 0.8422 0.6418 0.5547 0.0371  -0.1789 0.0967  285 THR B N   
3711 C CA  . THR B 211 ? 0.7973 0.6228 0.5146 0.0237  -0.1739 0.1042  285 THR B CA  
3712 C C   . THR B 211 ? 0.7965 0.6003 0.4914 -0.0039 -0.1541 0.1074  285 THR B C   
3713 O O   . THR B 211 ? 0.7968 0.6275 0.5035 -0.0133 -0.1419 0.1073  285 THR B O   
3714 C CB  . THR B 211 ? 0.7966 0.6083 0.4971 0.0302  -0.1981 0.1132  285 THR B CB  
3715 O OG1 . THR B 211 ? 0.9095 0.6587 0.5679 0.0255  -0.2039 0.1176  285 THR B OG1 
3716 C CG2 . THR B 211 ? 0.7871 0.6401 0.5239 0.0606  -0.2146 0.1094  285 THR B CG2 
3717 N N   . ALA B 212 ? 0.8503 0.6058 0.5141 -0.0165 -0.1493 0.1103  286 ALA B N   
3718 C CA  . ALA B 212 ? 0.7880 0.5304 0.4348 -0.0409 -0.1262 0.1132  286 ALA B CA  
3719 C C   . ALA B 212 ? 0.7934 0.5825 0.4778 -0.0431 -0.1064 0.1041  286 ALA B C   
3720 O O   . ALA B 212 ? 0.7909 0.5831 0.4685 -0.0566 -0.0874 0.1051  286 ALA B O   
3721 C CB  . ALA B 212 ? 0.8214 0.5159 0.4428 -0.0555 -0.1212 0.1182  286 ALA B CB  
3722 N N   . ALA B 213 ? 0.7721 0.5957 0.4920 -0.0273 -0.1106 0.0949  287 ALA B N   
3723 C CA  . ALA B 213 ? 0.7651 0.6299 0.5154 -0.0266 -0.0951 0.0877  287 ALA B CA  
3724 C C   . ALA B 213 ? 0.7662 0.6530 0.5207 -0.0276 -0.0877 0.0919  287 ALA B C   
3725 O O   . ALA B 213 ? 0.7296 0.6288 0.4910 -0.0336 -0.0712 0.0901  287 ALA B O   
3726 C CB  . ALA B 213 ? 0.7274 0.6203 0.5036 -0.0066 -0.1031 0.0777  287 ALA B CB  
3727 N N   . ASP B 214 ? 0.7686 0.6599 0.5212 -0.0216 -0.1013 0.0972  288 ASP B N   
3728 C CA  . ASP B 214 ? 0.6671 0.5736 0.4243 -0.0267 -0.0979 0.1012  288 ASP B CA  
3729 C C   . ASP B 214 ? 0.7252 0.5963 0.4472 -0.0430 -0.0897 0.1028  288 ASP B C   
3730 O O   . ASP B 214 ? 0.7840 0.6586 0.5060 -0.0474 -0.0785 0.1015  288 ASP B O   
3731 C CB  . ASP B 214 ? 0.6546 0.5788 0.4242 -0.0205 -0.1169 0.1064  288 ASP B CB  
3732 C CG  . ASP B 214 ? 0.6855 0.6579 0.4938 -0.0027 -0.1168 0.1053  288 ASP B CG  
3733 O OD1 . ASP B 214 ? 0.5981 0.5876 0.4183 0.0033  -0.1027 0.1010  288 ASP B OD1 
3734 O OD2 . ASP B 214 ? 0.6817 0.6778 0.5080 0.0068  -0.1309 0.1088  288 ASP B OD2 
3735 N N   . VAL B 215 ? 0.7704 0.6029 0.4566 -0.0502 -0.0945 0.1057  289 VAL B N   
3736 C CA  . VAL B 215 ? 0.8289 0.6265 0.4727 -0.0633 -0.0839 0.1068  289 VAL B CA  
3737 C C   . VAL B 215 ? 0.8107 0.6181 0.4628 -0.0667 -0.0559 0.1015  289 VAL B C   
3738 O O   . VAL B 215 ? 0.8577 0.6557 0.4923 -0.0696 -0.0431 0.0981  289 VAL B O   
3739 C CB  . VAL B 215 ? 0.8408 0.5933 0.4387 -0.0696 -0.0928 0.1141  289 VAL B CB  
3740 C CG1 . VAL B 215 ? 0.8832 0.6042 0.4371 -0.0810 -0.0740 0.1135  289 VAL B CG1 
3741 C CG2 . VAL B 215 ? 0.7972 0.5478 0.3953 -0.0618 -0.1214 0.1158  289 VAL B CG2 
3742 N N   . PHE B 216 ? 0.7589 0.5867 0.4400 -0.0647 -0.0479 0.0991  290 PHE B N   
3743 C CA  . PHE B 216 ? 0.7337 0.5824 0.4334 -0.0665 -0.0243 0.0937  290 PHE B CA  
3744 C C   . PHE B 216 ? 0.7194 0.5975 0.4446 -0.0540 -0.0211 0.0888  290 PHE B C   
3745 O O   . PHE B 216 ? 0.7120 0.5907 0.4324 -0.0519 -0.0045 0.0853  290 PHE B O   
3746 C CB  . PHE B 216 ? 0.7281 0.5930 0.4561 -0.0701 -0.0224 0.0912  290 PHE B CB  
3747 C CG  . PHE B 216 ? 0.7052 0.5966 0.4571 -0.0753 0.0003  0.0865  290 PHE B CG  
3748 C CD1 . PHE B 216 ? 0.6722 0.6052 0.4620 -0.0619 0.0031  0.0789  290 PHE B CD1 
3749 C CD2 . PHE B 216 ? 0.6918 0.5698 0.4294 -0.0929 0.0191  0.0912  290 PHE B CD2 
3750 C CE1 . PHE B 216 ? 0.6710 0.6358 0.4893 -0.0637 0.0212  0.0741  290 PHE B CE1 
3751 C CE2 . PHE B 216 ? 0.7108 0.6248 0.4800 -0.0974 0.0415  0.0871  290 PHE B CE2 
3752 C CZ  . PHE B 216 ? 0.6953 0.6549 0.5077 -0.0817 0.0410  0.0775  290 PHE B CZ  
3753 N N   . SER B 217 ? 0.6680 0.5683 0.4174 -0.0438 -0.0357 0.0893  291 SER B N   
3754 C CA  . SER B 217 ? 0.6440 0.5662 0.4117 -0.0336 -0.0329 0.0891  291 SER B CA  
3755 C C   . SER B 217 ? 0.6633 0.5582 0.4049 -0.0387 -0.0306 0.0909  291 SER B C   
3756 O O   . SER B 217 ? 0.6912 0.5856 0.4341 -0.0324 -0.0195 0.0886  291 SER B O   
3757 C CB  . SER B 217 ? 0.6359 0.5834 0.4252 -0.0242 -0.0468 0.0926  291 SER B CB  
3758 O OG  . SER B 217 ? 0.6565 0.6240 0.4640 -0.0160 -0.0502 0.0872  291 SER B OG  
3759 N N   . LEU B 218 ? 0.7023 0.5707 0.4176 -0.0487 -0.0436 0.0941  292 LEU B N   
3760 C CA  . LEU B 218 ? 0.7742 0.6091 0.4581 -0.0558 -0.0454 0.0927  292 LEU B CA  
3761 C C   . LEU B 218 ? 0.7728 0.5828 0.4263 -0.0546 -0.0244 0.0851  292 LEU B C   
3762 O O   . LEU B 218 ? 0.8259 0.6146 0.4625 -0.0512 -0.0180 0.0799  292 LEU B O   
3763 C CB  . LEU B 218 ? 0.7675 0.5806 0.4273 -0.0665 -0.0676 0.0961  292 LEU B CB  
3764 C CG  . LEU B 218 ? 0.7824 0.5613 0.4121 -0.0764 -0.0780 0.0931  292 LEU B CG  
3765 C CD1 . LEU B 218 ? 0.7014 0.4927 0.3585 -0.0761 -0.0764 0.0951  292 LEU B CD1 
3766 C CD2 . LEU B 218 ? 0.7915 0.5641 0.4119 -0.0859 -0.1067 0.0971  292 LEU B CD2 
3767 N N   . GLY B 219 ? 0.7804 0.5918 0.4266 -0.0570 -0.0123 0.0847  293 GLY B N   
3768 C CA  . GLY B 219 ? 0.7886 0.5870 0.4110 -0.0556 0.0128  0.0787  293 GLY B CA  
3769 C C   . GLY B 219 ? 0.7949 0.6195 0.4474 -0.0402 0.0297  0.0722  293 GLY B C   
3770 O O   . GLY B 219 ? 0.7725 0.5787 0.4017 -0.0317 0.0451  0.0646  293 GLY B O   
3771 N N   . LEU B 220 ? 0.7314 0.5969 0.4323 -0.0333 0.0254  0.0742  294 LEU B N   
3772 C CA  . LEU B 220 ? 0.6920 0.5821 0.4205 -0.0155 0.0359  0.0696  294 LEU B CA  
3773 C C   . LEU B 220 ? 0.7410 0.6063 0.4567 -0.0074 0.0265  0.0709  294 LEU B C   
3774 O O   . LEU B 220 ? 0.7777 0.6377 0.4931 0.0090  0.0367  0.0662  294 LEU B O   
3775 C CB  . LEU B 220 ? 0.6767 0.6145 0.4533 -0.0104 0.0306  0.0709  294 LEU B CB  
3776 C CG  . LEU B 220 ? 0.6167 0.5781 0.4121 -0.0210 0.0401  0.0686  294 LEU B CG  
3777 C CD1 . LEU B 220 ? 0.6394 0.6441 0.4800 -0.0151 0.0305  0.0661  294 LEU B CD1 
3778 C CD2 . LEU B 220 ? 0.6776 0.6454 0.4702 -0.0182 0.0667  0.0633  294 LEU B CD2 
3779 N N   . THR B 221 ? 0.7813 0.6318 0.4888 -0.0188 0.0069  0.0780  295 THR B N   
3780 C CA  . THR B 221 ? 0.7636 0.5864 0.4591 -0.0189 -0.0024 0.0815  295 THR B CA  
3781 C C   . THR B 221 ? 0.7981 0.5683 0.4475 -0.0189 0.0032  0.0718  295 THR B C   
3782 O O   . THR B 221 ? 0.8531 0.5970 0.4923 -0.0083 0.0063  0.0692  295 THR B O   
3783 C CB  . THR B 221 ? 0.7648 0.5909 0.4669 -0.0348 -0.0234 0.0910  295 THR B CB  
3784 O OG1 . THR B 221 ? 0.7281 0.6004 0.4684 -0.0290 -0.0262 0.0983  295 THR B OG1 
3785 C CG2 . THR B 221 ? 0.7392 0.5340 0.4299 -0.0431 -0.0334 0.0958  295 THR B CG2 
3786 N N   . ILE B 222 ? 0.8783 0.6268 0.4933 -0.0290 0.0040  0.0663  296 ILE B N   
3787 C CA  . ILE B 222 ? 0.8341 0.5284 0.3946 -0.0274 0.0089  0.0545  296 ILE B CA  
3788 C C   . ILE B 222 ? 0.8441 0.5429 0.4010 -0.0048 0.0377  0.0443  296 ILE B C   
3789 O O   . ILE B 222 ? 0.9365 0.5944 0.4619 0.0085  0.0437  0.0335  296 ILE B O   
3790 C CB  . ILE B 222 ? 0.9211 0.5909 0.4386 -0.0429 0.0006  0.0529  296 ILE B CB  
3791 C CG1 . ILE B 222 ? 0.8717 0.5347 0.3932 -0.0616 -0.0320 0.0605  296 ILE B CG1 
3792 C CG2 . ILE B 222 ? 0.9994 0.6156 0.4519 -0.0369 0.0112  0.0382  296 ILE B CG2 
3793 C CD1 . ILE B 222 ? 0.8758 0.5081 0.3935 -0.0672 -0.0472 0.0583  296 ILE B CD1 
3794 N N   . LEU B 223 ? 0.8642 0.6131 0.4554 0.0005  0.0552  0.0466  297 LEU B N   
3795 C CA  . LEU B 223 ? 0.8567 0.6263 0.4591 0.0225  0.0829  0.0377  297 LEU B CA  
3796 C C   . LEU B 223 ? 0.9014 0.6759 0.5293 0.0453  0.0805  0.0362  297 LEU B C   
3797 O O   . LEU B 223 ? 0.9400 0.6984 0.5536 0.0690  0.0959  0.0253  297 LEU B O   
3798 C CB  . LEU B 223 ? 0.8176 0.6462 0.4623 0.0171  0.0976  0.0423  297 LEU B CB  
3799 C CG  . LEU B 223 ? 0.7902 0.6561 0.4556 0.0338  0.1295  0.0345  297 LEU B CG  
3800 C CD1 . LEU B 223 ? 0.8927 0.7289 0.5034 0.0306  0.1530  0.0285  297 LEU B CD1 
3801 C CD2 . LEU B 223 ? 0.7315 0.6628 0.4582 0.0246  0.1335  0.0409  297 LEU B CD2 
3802 N N   . GLU B 224 ? 0.8165 0.6101 0.4776 0.0411  0.0615  0.0476  298 GLU B N   
3803 C CA  . GLU B 224 ? 0.7749 0.5691 0.4542 0.0625  0.0576  0.0503  298 GLU B CA  
3804 C C   . GLU B 224 ? 0.8408 0.5642 0.4748 0.0681  0.0516  0.0461  298 GLU B C   
3805 O O   . GLU B 224 ? 0.8874 0.5930 0.5167 0.0950  0.0589  0.0406  298 GLU B O   
3806 C CB  . GLU B 224 ? 0.7876 0.6124 0.5007 0.0548  0.0400  0.0650  298 GLU B CB  
3807 C CG  . GLU B 224 ? 0.7470 0.5572 0.4639 0.0714  0.0321  0.0734  298 GLU B CG  
3808 C CD  . GLU B 224 ? 0.8198 0.6577 0.5598 0.0625  0.0176  0.0892  298 GLU B CD  
3809 O OE1 . GLU B 224 ? 0.8061 0.6793 0.5645 0.0482  0.0135  0.0904  298 GLU B OE1 
3810 O OE2 . GLU B 224 ? 0.9178 0.7389 0.6538 0.0711  0.0112  0.1008  298 GLU B OE2 
3811 N N   . VAL B 225 ? 0.8790 0.5591 0.4797 0.0436  0.0359  0.0480  299 VAL B N   
3812 C CA  . VAL B 225 ? 0.9075 0.5154 0.4670 0.0430  0.0249  0.0441  299 VAL B CA  
3813 C C   . VAL B 225 ? 0.9545 0.5106 0.4582 0.0537  0.0362  0.0234  299 VAL B C   
3814 O O   . VAL B 225 ? 1.0555 0.5533 0.5264 0.0698  0.0356  0.0141  299 VAL B O   
3815 C CB  . VAL B 225 ? 0.8983 0.4871 0.4544 0.0098  -0.0007 0.0556  299 VAL B CB  
3816 C CG1 . VAL B 225 ? 0.8502 0.4968 0.4583 0.0024  -0.0068 0.0749  299 VAL B CG1 
3817 C CG2 . VAL B 225 ? 0.9426 0.5209 0.4706 -0.0115 -0.0092 0.0484  299 VAL B CG2 
3818 N N   . ALA B 226 ? 0.9715 0.5424 0.4577 0.0467  0.0471  0.0159  300 ALA B N   
3819 C CA  . ALA B 226 ? 1.0434 0.5661 0.4686 0.0591  0.0611  -0.0040 300 ALA B CA  
3820 C C   . ALA B 226 ? 1.0292 0.5728 0.4643 0.0967  0.0923  -0.0150 300 ALA B C   
3821 O O   . ALA B 226 ? 1.1339 0.6316 0.5171 0.1166  0.1063  -0.0337 300 ALA B O   
3822 C CB  . ALA B 226 ? 1.0795 0.6095 0.4760 0.0403  0.0647  -0.0053 300 ALA B CB  
3823 N N   . CYS B 227 ? 1.0658 0.6797 0.5661 0.1086  0.1026  -0.0053 301 CYS B N   
3824 C CA  . CYS B 227 ? 1.0251 0.6741 0.5496 0.1451  0.1295  -0.0146 301 CYS B CA  
3825 C C   . CYS B 227 ? 0.9821 0.6394 0.5434 0.1694  0.1197  -0.0087 301 CYS B C   
3826 O O   . CYS B 227 ? 1.0520 0.7324 0.6323 0.2059  0.1374  -0.0176 301 CYS B O   
3827 C CB  . CYS B 227 ? 1.0804 0.8140 0.6536 0.1395  0.1515  -0.0101 301 CYS B CB  
3828 S SG  . CYS B 227 ? 1.1975 0.9196 0.7208 0.1152  0.1692  -0.0138 301 CYS B SG  
3829 N N   . ASN B 228 ? 1.0079 0.6495 0.5792 0.1519  0.0928  0.0071  302 ASN B N   
3830 C CA  . ASN B 228 ? 0.9545 0.5970 0.5513 0.1732  0.0821  0.0169  302 ASN B CA  
3831 C C   . ASN B 228 ? 0.9300 0.6586 0.5895 0.1956  0.0938  0.0188  302 ASN B C   
3832 O O   . ASN B 228 ? 0.9895 0.7258 0.6639 0.2330  0.0987  0.0148  302 ASN B O   
3833 C CB  . ASN B 228 ? 0.9666 0.5294 0.5175 0.2015  0.0812  0.0063  302 ASN B CB  
3834 C CG  . ASN B 228 ? 1.0090 0.5520 0.5719 0.2176  0.0649  0.0216  302 ASN B CG  
3835 O OD1 . ASN B 228 ? 0.9892 0.5539 0.5760 0.1962  0.0495  0.0420  302 ASN B OD1 
3836 N ND2 . ASN B 228 ? 1.0446 0.5447 0.5877 0.2583  0.0692  0.0124  302 ASN B ND2 
3837 N N   . MET B 229 ? 0.9250 0.7174 0.6215 0.1729  0.0962  0.0242  303 MET B N   
3838 C CA  . MET B 229 ? 0.9588 0.8345 0.7183 0.1855  0.1017  0.0258  303 MET B CA  
3839 C C   . MET B 229 ? 0.8828 0.7845 0.6693 0.1705  0.0786  0.0418  303 MET B C   
3840 O O   . MET B 229 ? 0.8987 0.7723 0.6640 0.1434  0.0651  0.0514  303 MET B O   
3841 C CB  . MET B 229 ? 0.9792 0.9075 0.7614 0.1712  0.1237  0.0184  303 MET B CB  
3842 C CG  . MET B 229 ? 0.9314 0.8633 0.7086 0.1306  0.1157  0.0267  303 MET B CG  
3843 S SD  . MET B 229 ? 1.1092 1.0926 0.9073 0.1134  0.1436  0.0217  303 MET B SD  
3844 C CE  . MET B 229 ? 1.0693 1.1445 0.9502 0.1357  0.1507  0.0185  303 MET B CE  
3845 N N   . GLU B 230 ? 0.8447 0.8030 0.6780 0.1905  0.0735  0.0437  304 GLU B N   
3846 C CA  . GLU B 230 ? 0.8037 0.7902 0.6586 0.1815  0.0525  0.0562  304 GLU B CA  
3847 C C   . GLU B 230 ? 0.7754 0.8217 0.6685 0.1583  0.0536  0.0524  304 GLU B C   
3848 O O   . GLU B 230 ? 0.8075 0.9063 0.7405 0.1642  0.0656  0.0426  304 GLU B O   
3849 C CB  . GLU B 230 ? 0.7684 0.7762 0.6442 0.2168  0.0407  0.0603  304 GLU B CB  
3850 C CG  . GLU B 230 ? 0.9389 0.9650 0.8213 0.2107  0.0188  0.0735  304 GLU B CG  
3851 C CD  . GLU B 230 ? 1.0410 1.0902 0.9397 0.2470  0.0042  0.0779  304 GLU B CD  
3852 O OE1 . GLU B 230 ? 1.1023 1.1530 1.0110 0.2789  0.0102  0.0709  304 GLU B OE1 
3853 O OE2 . GLU B 230 ? 1.1385 1.2043 1.0372 0.2462  -0.0138 0.0878  304 GLU B OE2 
3854 N N   . LEU B 231 ? 0.7798 0.8180 0.6625 0.1320  0.0413  0.0603  305 LEU B N   
3855 C CA  . LEU B 231 ? 0.6793 0.7579 0.5891 0.1091  0.0396  0.0568  305 LEU B CA  
3856 C C   . LEU B 231 ? 0.6574 0.7912 0.6091 0.1200  0.0240  0.0550  305 LEU B C   
3857 O O   . LEU B 231 ? 0.6779 0.8075 0.6214 0.1351  0.0079  0.0624  305 LEU B O   
3858 C CB  . LEU B 231 ? 0.6899 0.7382 0.5723 0.0833  0.0303  0.0642  305 LEU B CB  
3859 C CG  . LEU B 231 ? 0.6087 0.6085 0.4519 0.0674  0.0405  0.0641  305 LEU B CG  
3860 C CD1 . LEU B 231 ? 0.6201 0.6055 0.4490 0.0438  0.0283  0.0705  305 LEU B CD1 
3861 C CD2 . LEU B 231 ? 0.6676 0.6792 0.5157 0.0638  0.0619  0.0545  305 LEU B CD2 
3862 N N   . PRO B 232 ? 0.6192 0.8034 0.6137 0.1108  0.0276  0.0458  306 PRO B N   
3863 C CA  . PRO B 232 ? 0.5918 0.8297 0.6281 0.1193  0.0083  0.0409  306 PRO B CA  
3864 C C   . PRO B 232 ? 0.5827 0.8147 0.6081 0.1027  -0.0119 0.0423  306 PRO B C   
3865 O O   . PRO B 232 ? 0.5584 0.7610 0.5616 0.0794  -0.0083 0.0447  306 PRO B O   
3866 C CB  . PRO B 232 ? 0.5453 0.8372 0.6339 0.1083  0.0216  0.0307  306 PRO B CB  
3867 C CG  . PRO B 232 ? 0.5885 0.8469 0.6515 0.0820  0.0443  0.0330  306 PRO B CG  
3868 C CD  . PRO B 232 ? 0.6089 0.8035 0.6147 0.0922  0.0503  0.0400  306 PRO B CD  
3869 N N   . HIS B 233 ? 0.6299 0.8898 0.6683 0.1185  -0.0346 0.0397  307 HIS B N   
3870 C CA  . HIS B 233 ? 0.5863 0.8441 0.6126 0.1090  -0.0546 0.0371  307 HIS B CA  
3871 C C   . HIS B 233 ? 0.5629 0.8534 0.6270 0.0869  -0.0642 0.0230  307 HIS B C   
3872 O O   . HIS B 233 ? 0.6247 0.8963 0.6729 0.0709  -0.0739 0.0192  307 HIS B O   
3873 C CB  . HIS B 233 ? 0.6167 0.8843 0.6289 0.1368  -0.0757 0.0402  307 HIS B CB  
3874 C CG  . HIS B 233 ? 0.7520 0.9808 0.7227 0.1547  -0.0683 0.0575  307 HIS B CG  
3875 N ND1 . HIS B 233 ? 0.7556 0.9812 0.7275 0.1791  -0.0641 0.0639  307 HIS B ND1 
3876 C CD2 . HIS B 233 ? 0.7505 0.9414 0.6791 0.1507  -0.0646 0.0705  307 HIS B CD2 
3877 C CE1 . HIS B 233 ? 0.7761 0.9558 0.7046 0.1864  -0.0591 0.0809  307 HIS B CE1 
3878 N NE2 . HIS B 233 ? 0.8762 1.0390 0.7813 0.1678  -0.0584 0.0857  307 HIS B NE2 
3879 N N   . GLY B 234 ? 0.5180 0.8571 0.6334 0.0861  -0.0624 0.0151  308 GLY B N   
3880 C CA  . GLY B 234 ? 0.4861 0.8593 0.6444 0.0607  -0.0728 0.0027  308 GLY B CA  
3881 C C   . GLY B 234 ? 0.5738 1.0030 0.7926 0.0563  -0.0575 -0.0009 308 GLY B C   
3882 O O   . GLY B 234 ? 0.6190 1.0466 0.8359 0.0681  -0.0314 0.0058  308 GLY B O   
3883 N N   . GLY B 235 ? 0.5852 1.0654 0.8590 0.0393  -0.0739 -0.0126 309 GLY B N   
3884 C CA  . GLY B 235 ? 0.4530 1.0021 0.7977 0.0326  -0.0593 -0.0161 309 GLY B CA  
3885 C C   . GLY B 235 ? 0.5116 1.0490 0.8579 0.0062  -0.0198 -0.0076 309 GLY B C   
3886 O O   . GLY B 235 ? 0.5015 0.9738 0.7929 -0.0091 -0.0084 0.0004  309 GLY B O   
3887 N N   . GLU B 236 ? 0.5285 1.1325 0.9376 0.0026  0.0019  -0.0089 310 GLU B N   
3888 C CA  . GLU B 236 ? 0.5074 1.1065 0.9170 -0.0231 0.0429  -0.0001 310 GLU B CA  
3889 C C   . GLU B 236 ? 0.5042 1.0409 0.8435 -0.0030 0.0689  0.0087  310 GLU B C   
3890 O O   . GLU B 236 ? 0.5226 1.0219 0.8283 -0.0258 0.0951  0.0173  310 GLU B O   
3891 C CB  . GLU B 236 ? 0.4749 1.1686 0.9697 -0.0260 0.0646  -0.0033 310 GLU B CB  
3892 C CG  . GLU B 236 ? 0.6037 1.3498 1.1676 -0.0707 0.0520  -0.0072 310 GLU B CG  
3893 C CD  . GLU B 236 ? 0.7127 1.3943 1.2368 -0.1185 0.0597  0.0024  310 GLU B CD  
3894 O OE1 . GLU B 236 ? 0.7113 1.3511 1.1894 -0.1258 0.0957  0.0151  310 GLU B OE1 
3895 O OE2 . GLU B 236 ? 0.7727 1.4402 1.3064 -0.1467 0.0277  -0.0034 310 GLU B OE2 
3896 N N   . GLY B 237 ? 0.4978 1.0184 0.8109 0.0384  0.0604  0.0073  311 GLY B N   
3897 C CA  . GLY B 237 ? 0.5019 0.9550 0.7457 0.0536  0.0786  0.0142  311 GLY B CA  
3898 C C   . GLY B 237 ? 0.5119 0.8919 0.6945 0.0290  0.0711  0.0216  311 GLY B C   
3899 O O   . GLY B 237 ? 0.5844 0.9201 0.7236 0.0170  0.0927  0.0278  311 GLY B O   
3900 N N   . TRP B 238 ? 0.5487 0.9168 0.7259 0.0235  0.0393  0.0200  312 TRP B N   
3901 C CA  . TRP B 238 ? 0.5603 0.8678 0.6879 0.0033  0.0302  0.0255  312 TRP B CA  
3902 C C   . TRP B 238 ? 0.5775 0.8762 0.7090 -0.0344 0.0445  0.0290  312 TRP B C   
3903 O O   . TRP B 238 ? 0.5433 0.7866 0.6258 -0.0477 0.0511  0.0370  312 TRP B O   
3904 C CB  . TRP B 238 ? 0.5473 0.8540 0.6743 0.0083  -0.0045 0.0201  312 TRP B CB  
3905 C CG  . TRP B 238 ? 0.5450 0.7956 0.6241 -0.0030 -0.0156 0.0241  312 TRP B CG  
3906 C CD1 . TRP B 238 ? 0.4769 0.6901 0.5115 0.0133  -0.0217 0.0304  312 TRP B CD1 
3907 C CD2 . TRP B 238 ? 0.5763 0.8042 0.6508 -0.0318 -0.0226 0.0224  312 TRP B CD2 
3908 N NE1 . TRP B 238 ? 0.5407 0.7172 0.5476 -0.0007 -0.0311 0.0315  312 TRP B NE1 
3909 C CE2 . TRP B 238 ? 0.5898 0.7692 0.6167 -0.0265 -0.0330 0.0264  312 TRP B CE2 
3910 C CE3 . TRP B 238 ? 0.5385 0.7808 0.6453 -0.0623 -0.0209 0.0189  312 TRP B CE3 
3911 C CZ2 . TRP B 238 ? 0.5909 0.7334 0.5989 -0.0449 -0.0431 0.0255  312 TRP B CZ2 
3912 C CZ3 . TRP B 238 ? 0.5826 0.7796 0.6660 -0.0847 -0.0314 0.0196  312 TRP B CZ3 
3913 C CH2 . TRP B 238 ? 0.5931 0.7395 0.6260 -0.0732 -0.0430 0.0221  312 TRP B CH2 
3914 N N   . GLN B 239 ? 0.5649 0.9184 0.7555 -0.0528 0.0486  0.0245  313 GLN B N   
3915 C CA  . GLN B 239 ? 0.5100 0.8538 0.7064 -0.0932 0.0621  0.0308  313 GLN B CA  
3916 C C   . GLN B 239 ? 0.5731 0.9022 0.7427 -0.0988 0.1021  0.0415  313 GLN B C   
3917 O O   . GLN B 239 ? 0.6645 0.9469 0.7961 -0.1250 0.1126  0.0520  313 GLN B O   
3918 C CB  . GLN B 239 ? 0.5680 0.9807 0.8423 -0.1146 0.0555  0.0237  313 GLN B CB  
3919 C CG  . GLN B 239 ? 0.5950 0.9808 0.8727 -0.1571 0.0423  0.0256  313 GLN B CG  
3920 C CD  . GLN B 239 ? 0.6250 0.9647 0.8706 -0.1502 0.0022  0.0164  313 GLN B CD  
3921 O OE1 . GLN B 239 ? 0.7732 1.0443 0.9671 -0.1618 -0.0037 0.0219  313 GLN B OE1 
3922 N NE2 . GLN B 239 ? 0.4583 0.8356 0.7315 -0.1283 -0.0259 0.0021  313 GLN B NE2 
3923 N N   . GLN B 240 ? 0.5553 0.9190 0.7380 -0.0717 0.1239  0.0385  314 GLN B N   
3924 C CA  . GLN B 240 ? 0.6104 0.9666 0.7680 -0.0740 0.1647  0.0453  314 GLN B CA  
3925 C C   . GLN B 240 ? 0.6663 0.9384 0.7366 -0.0693 0.1669  0.0517  314 GLN B C   
3926 O O   . GLN B 240 ? 0.7637 1.0092 0.7948 -0.0823 0.1945  0.0596  314 GLN B O   
3927 C CB  . GLN B 240 ? 0.5185 0.9315 0.7116 -0.0397 0.1854  0.0369  314 GLN B CB  
3928 C CG  . GLN B 240 ? 0.5107 1.0200 0.7962 -0.0480 0.1943  0.0326  314 GLN B CG  
3929 C CD  . GLN B 240 ? 0.5959 1.1622 0.9174 -0.0058 0.2118  0.0233  314 GLN B CD  
3930 O OE1 . GLN B 240 ? 0.6404 1.1672 0.9177 0.0316  0.2080  0.0186  314 GLN B OE1 
3931 N NE2 . GLN B 240 ? 0.5400 1.1995 0.9438 -0.0114 0.2308  0.0207  314 GLN B NE2 
3932 N N   . LEU B 241 ? 0.6129 0.8451 0.6518 -0.0514 0.1386  0.0488  315 LEU B N   
3933 C CA  . LEU B 241 ? 0.6582 0.8168 0.6235 -0.0502 0.1343  0.0545  315 LEU B CA  
3934 C C   . LEU B 241 ? 0.7088 0.8249 0.6463 -0.0790 0.1201  0.0635  315 LEU B C   
3935 O O   . LEU B 241 ? 0.7120 0.7720 0.5939 -0.0785 0.1112  0.0684  315 LEU B O   
3936 C CB  . LEU B 241 ? 0.6448 0.7831 0.5942 -0.0232 0.1110  0.0503  315 LEU B CB  
3937 C CG  . LEU B 241 ? 0.6688 0.8151 0.6169 0.0090  0.1231  0.0437  315 LEU B CG  
3938 C CD1 . LEU B 241 ? 0.6592 0.7894 0.6004 0.0297  0.0972  0.0435  315 LEU B CD1 
3939 C CD2 . LEU B 241 ? 0.7796 0.8781 0.6694 0.0106  0.1446  0.0441  315 LEU B CD2 
3940 N N   . ARG B 242 ? 0.7116 0.8513 0.6870 -0.1035 0.1154  0.0653  316 ARG B N   
3941 C CA  . ARG B 242 ? 0.6803 0.7731 0.6296 -0.1264 0.0971  0.0725  316 ARG B CA  
3942 C C   . ARG B 242 ? 0.7364 0.8288 0.6940 -0.1620 0.1161  0.0829  316 ARG B C   
3943 O O   . ARG B 242 ? 0.7406 0.8070 0.6986 -0.1844 0.0988  0.0867  316 ARG B O   
3944 C CB  . ARG B 242 ? 0.6210 0.7223 0.5966 -0.1204 0.0625  0.0633  316 ARG B CB  
3945 C CG  . ARG B 242 ? 0.6393 0.7195 0.5858 -0.0921 0.0450  0.0601  316 ARG B CG  
3946 C CD  . ARG B 242 ? 0.5540 0.6628 0.5307 -0.0756 0.0202  0.0496  316 ARG B CD  
3947 N NE  . ARG B 242 ? 0.5571 0.6465 0.5043 -0.0518 0.0092  0.0507  316 ARG B NE  
3948 C CZ  . ARG B 242 ? 0.5891 0.6944 0.5384 -0.0296 0.0147  0.0503  316 ARG B CZ  
3949 N NH1 . ARG B 242 ? 0.5668 0.7085 0.5452 -0.0219 0.0302  0.0468  316 ARG B NH1 
3950 N NH2 . ARG B 242 ? 0.5654 0.6498 0.4886 -0.0143 0.0046  0.0541  316 ARG B NH2 
3951 N N   . GLN B 243 ? 0.7939 0.9117 0.7549 -0.1671 0.1529  0.0881  317 GLN B N   
3952 C CA  . GLN B 243 ? 0.8121 0.9299 0.7751 -0.2029 0.1788  0.1024  317 GLN B CA  
3953 C C   . GLN B 243 ? 0.8886 0.9468 0.7710 -0.2077 0.2005  0.1169  317 GLN B C   
3954 O O   . GLN B 243 ? 0.9209 0.9707 0.7911 -0.2374 0.2258  0.1328  317 GLN B O   
3955 C CB  . GLN B 243 ? 0.7989 1.0027 0.8327 -0.2081 0.2097  0.0993  317 GLN B CB  
3956 C CG  . GLN B 243 ? 0.7407 1.0120 0.8559 -0.1991 0.1868  0.0837  317 GLN B CG  
3957 C CD  . GLN B 243 ? 0.7549 1.0229 0.9048 -0.2331 0.1599  0.0843  317 GLN B CD  
3958 O OE1 . GLN B 243 ? 0.7880 1.0430 0.9432 -0.2222 0.1214  0.0726  317 GLN B OE1 
3959 N NE2 . GLN B 243 ? 0.7673 1.0448 0.9386 -0.2751 0.1806  0.0977  317 GLN B NE2 
3960 N N   . GLY B 244 ? 0.9866 1.0031 0.8123 -0.1811 0.1907  0.1126  318 GLY B N   
3961 C CA  . GLY B 244 ? 1.1041 1.0604 0.8473 -0.1837 0.2041  0.1239  318 GLY B CA  
3962 C C   . GLY B 244 ? 1.1839 1.1557 0.9012 -0.1682 0.2418  0.1203  318 GLY B C   
3963 O O   . GLY B 244 ? 1.2448 1.1637 0.8844 -0.1681 0.2525  0.1277  318 GLY B O   
3964 N N   . TYR B 245 ? 1.1749 1.2155 0.9512 -0.1523 0.2611  0.1083  319 TYR B N   
3965 C CA  . TYR B 245 ? 1.2153 1.2708 0.9687 -0.1284 0.2953  0.1002  319 TYR B CA  
3966 C C   . TYR B 245 ? 1.2448 1.3079 1.0118 -0.0904 0.2767  0.0811  319 TYR B C   
3967 O O   . TYR B 245 ? 1.2113 1.3021 1.0326 -0.0840 0.2493  0.0751  319 TYR B O   
3968 C CB  . TYR B 245 ? 1.1537 1.2870 0.9655 -0.1375 0.3389  0.1030  319 TYR B CB  
3969 C CG  . TYR B 245 ? 1.1221 1.3376 1.0359 -0.1288 0.3292  0.0919  319 TYR B CG  
3970 C CD1 . TYR B 245 ? 1.0931 1.3352 1.0668 -0.1576 0.3069  0.0973  319 TYR B CD1 
3971 C CD2 . TYR B 245 ? 1.1479 1.4096 1.0937 -0.0898 0.3392  0.0750  319 TYR B CD2 
3972 C CE1 . TYR B 245 ? 1.0697 1.3863 1.1325 -0.1491 0.2934  0.0858  319 TYR B CE1 
3973 C CE2 . TYR B 245 ? 1.1177 1.4544 1.1539 -0.0789 0.3264  0.0656  319 TYR B CE2 
3974 C CZ  . TYR B 245 ? 1.0598 1.4258 1.1542 -0.1094 0.3027  0.0709  319 TYR B CZ  
3975 O OH  . TYR B 245 ? 0.9431 1.3830 1.1234 -0.0986 0.2856  0.0604  319 TYR B OH  
3976 N N   . LEU B 246 ? 1.2263 1.2586 0.9379 -0.0656 0.2911  0.0719  320 LEU B N   
3977 C CA  . LEU B 246 ? 1.2135 1.2460 0.9345 -0.0302 0.2767  0.0551  320 LEU B CA  
3978 C C   . LEU B 246 ? 1.2159 1.3237 1.0009 -0.0068 0.3045  0.0450  320 LEU B C   
3979 O O   . LEU B 246 ? 1.2475 1.3858 1.0316 -0.0066 0.3458  0.0457  320 LEU B O   
3980 C CB  . LEU B 246 ? 1.2489 1.2081 0.8819 -0.0134 0.2750  0.0469  320 LEU B CB  
3981 C CG  . LEU B 246 ? 1.2057 1.0925 0.7722 -0.0327 0.2462  0.0554  320 LEU B CG  
3982 C CD1 . LEU B 246 ? 1.2347 1.0555 0.7244 -0.0145 0.2390  0.0429  320 LEU B CD1 
3983 C CD2 . LEU B 246 ? 1.1184 1.0080 0.7243 -0.0427 0.2057  0.0609  320 LEU B CD2 
3984 N N   . PRO B 247 ? 1.1832 1.3258 1.0247 0.0141  0.2838  0.0367  321 PRO B N   
3985 C CA  . PRO B 247 ? 1.1354 1.3470 1.0352 0.0448  0.3056  0.0256  321 PRO B CA  
3986 C C   . PRO B 247 ? 1.1933 1.3756 1.0386 0.0774  0.3348  0.0130  321 PRO B C   
3987 O O   . PRO B 247 ? 1.2519 1.3673 1.0422 0.0986  0.3172  0.0043  321 PRO B O   
3988 C CB  . PRO B 247 ? 1.1178 1.3388 1.0562 0.0650  0.2680  0.0204  321 PRO B CB  
3989 C CG  . PRO B 247 ? 1.0470 1.2438 0.9829 0.0328  0.2348  0.0313  321 PRO B CG  
3990 C CD  . PRO B 247 ? 1.0708 1.1997 0.9310 0.0094  0.2401  0.0392  321 PRO B CD  
3991 N N   . PRO B 248 ? 1.1735 1.4048 1.0331 0.0823  0.3803  0.0112  322 PRO B N   
3992 C CA  . PRO B 248 ? 1.2083 1.3991 0.9947 0.1088  0.4128  -0.0007 322 PRO B CA  
3993 C C   . PRO B 248 ? 1.2171 1.3912 0.9957 0.1612  0.4089  -0.0213 322 PRO B C   
3994 O O   . PRO B 248 ? 1.1950 1.3296 0.9092 0.1879  0.4342  -0.0352 322 PRO B O   
3995 C CB  . PRO B 248 ? 1.0983 1.3671 0.9213 0.1006  0.4656  0.0048  322 PRO B CB  
3996 C CG  . PRO B 248 ? 1.0425 1.4097 0.9830 0.0904  0.4575  0.0103  322 PRO B CG  
3997 C CD  . PRO B 248 ? 1.0456 1.3762 0.9927 0.0644  0.4047  0.0189  322 PRO B CD  
3998 N N   . GLU B 249 ? 1.1889 1.3850 1.0237 0.1783  0.3777  -0.0240 323 GLU B N   
3999 C CA  . GLU B 249 ? 1.1947 1.3683 1.0203 0.2296  0.3729  -0.0412 323 GLU B CA  
4000 C C   . GLU B 249 ? 1.3316 1.3911 1.0709 0.2325  0.3416  -0.0458 323 GLU B C   
4001 O O   . GLU B 249 ? 1.3588 1.3533 1.0234 0.2533  0.3548  -0.0603 323 GLU B O   
4002 C CB  . GLU B 249 ? 1.1458 1.3898 1.0637 0.2488  0.3524  -0.0400 323 GLU B CB  
4003 C CG  . GLU B 249 ? 1.1622 1.4257 1.1218 0.2107  0.3162  -0.0239 323 GLU B CG  
4004 C CD  . GLU B 249 ? 1.2358 1.5431 1.2607 0.2356  0.2876  -0.0246 323 GLU B CD  
4005 O OE1 . GLU B 249 ? 1.2166 1.5525 1.2667 0.2815  0.2981  -0.0360 323 GLU B OE1 
4006 O OE2 . GLU B 249 ? 1.2967 1.6076 1.3432 0.2123  0.2541  -0.0143 323 GLU B OE2 
4007 N N   . PHE B 250 ? 1.3544 1.3898 1.1034 0.2111  0.2999  -0.0342 324 PHE B N   
4008 C CA  . PHE B 250 ? 1.3755 1.3136 1.0568 0.2097  0.2689  -0.0360 324 PHE B CA  
4009 C C   . PHE B 250 ? 1.4286 1.2993 1.0266 0.1848  0.2725  -0.0374 324 PHE B C   
4010 O O   . PHE B 250 ? 1.4780 1.2651 1.0068 0.1931  0.2591  -0.0475 324 PHE B O   
4011 C CB  . PHE B 250 ? 1.3311 1.2713 1.0455 0.1888  0.2292  -0.0207 324 PHE B CB  
4012 C CG  . PHE B 250 ? 1.3474 1.3247 1.1183 0.2185  0.2157  -0.0200 324 PHE B CG  
4013 C CD1 . PHE B 250 ? 1.3408 1.4109 1.1927 0.2199  0.2196  -0.0156 324 PHE B CD1 
4014 C CD2 . PHE B 250 ? 1.3097 1.2252 1.0502 0.2433  0.1962  -0.0229 324 PHE B CD2 
4015 C CE1 . PHE B 250 ? 1.3280 1.4315 1.2273 0.2493  0.2029  -0.0149 324 PHE B CE1 
4016 C CE2 . PHE B 250 ? 1.3196 1.2632 1.1043 0.2724  0.1821  -0.0196 324 PHE B CE2 
4017 C CZ  . PHE B 250 ? 1.3381 1.3772 1.2011 0.2771  0.1846  -0.0160 324 PHE B CZ  
4018 N N   . THR B 251 ? 1.3750 1.2768 0.9758 0.1538  0.2881  -0.0271 325 THR B N   
4019 C CA  . THR B 251 ? 1.3862 1.2254 0.9059 0.1298  0.2875  -0.0255 325 THR B CA  
4020 C C   . THR B 251 ? 1.3818 1.1799 0.8271 0.1541  0.3185  -0.0434 325 THR B C   
4021 O O   . THR B 251 ? 1.4434 1.1824 0.8094 0.1381  0.3163  -0.0443 325 THR B O   
4022 C CB  . THR B 251 ? 1.4033 1.2828 0.9439 0.0921  0.2963  -0.0071 325 THR B CB  
4023 O OG1 . THR B 251 ? 1.4620 1.2741 0.9264 0.0677  0.2810  -0.0016 325 THR B OG1 
4024 C CG2 . THR B 251 ? 1.3394 1.2801 0.9007 0.0977  0.3460  -0.0073 325 THR B CG2 
4025 N N   . ALA B 252 ? 1.3772 1.2036 0.8423 0.1951  0.3460  -0.0587 326 ALA B N   
4026 C CA  . ALA B 252 ? 1.4377 1.2313 0.8341 0.2214  0.3785  -0.0776 326 ALA B CA  
4027 C C   . ALA B 252 ? 1.4803 1.1612 0.7834 0.2260  0.3487  -0.0928 326 ALA B C   
4028 O O   . ALA B 252 ? 1.5050 1.1461 0.7447 0.2190  0.3518  -0.1000 326 ALA B O   
4029 C CB  . ALA B 252 ? 1.4084 1.2615 0.8619 0.2658  0.4043  -0.0915 326 ALA B CB  
4030 N N   . GLY B 253 ? 1.5203 1.1540 0.8248 0.2327  0.3133  -0.0957 327 GLY B N   
4031 C CA  . GLY B 253 ? 1.4944 1.0188 0.7138 0.2347  0.2842  -0.1109 327 GLY B CA  
4032 C C   . GLY B 253 ? 1.4288 0.9052 0.5924 0.1920  0.2574  -0.1026 327 GLY B C   
4033 O O   . GLY B 253 ? 1.5030 0.8999 0.5939 0.1897  0.2374  -0.1165 327 GLY B O   
4034 N N   . LEU B 254 ? 1.4018 0.9311 0.6118 0.1567  0.2498  -0.0788 328 LEU B N   
4035 C CA  . LEU B 254 ? 1.3953 0.8846 0.5610 0.1193  0.2202  -0.0691 328 LEU B CA  
4036 C C   . LEU B 254 ? 1.5186 0.9816 0.6183 0.1155  0.2323  -0.0753 328 LEU B C   
4037 O O   . LEU B 254 ? 1.5755 1.0714 0.6770 0.1348  0.2693  -0.0815 328 LEU B O   
4038 C CB  . LEU B 254 ? 1.3610 0.9156 0.5956 0.0881  0.2116  -0.0429 328 LEU B CB  
4039 C CG  . LEU B 254 ? 1.3140 0.9133 0.6368 0.0878  0.1931  -0.0327 328 LEU B CG  
4040 C CD1 . LEU B 254 ? 1.2450 0.8848 0.6130 0.0552  0.1756  -0.0108 328 LEU B CD1 
4041 C CD2 . LEU B 254 ? 1.2310 0.7697 0.5364 0.0937  0.1602  -0.0410 328 LEU B CD2 
4042 N N   . SER B 255 ? 1.4772 0.8901 0.5315 0.0897  0.1967  -0.0719 329 SER B N   
4043 C CA  . SER B 255 ? 1.4850 0.8754 0.4842 0.0836  0.1991  -0.0741 329 SER B CA  
4044 C C   . SER B 255 ? 1.5030 0.9471 0.5290 0.0601  0.2115  -0.0501 329 SER B C   
4045 O O   . SER B 255 ? 1.4179 0.9061 0.5014 0.0437  0.2083  -0.0324 329 SER B O   
4046 C CB  . SER B 255 ? 1.5156 0.8292 0.4575 0.0691  0.1521  -0.0822 329 SER B CB  
4047 O OG  . SER B 255 ? 1.4636 0.7852 0.4354 0.0392  0.1172  -0.0649 329 SER B OG  
4048 N N   . SER B 256 ? 1.4815 0.9169 0.4611 0.0589  0.2249  -0.0495 330 SER B N   
4049 C CA  . SER B 256 ? 1.4502 0.9243 0.4449 0.0365  0.2356  -0.0259 330 SER B CA  
4050 C C   . SER B 256 ? 1.4332 0.8927 0.4410 0.0090  0.1925  -0.0098 330 SER B C   
4051 O O   . SER B 256 ? 1.4372 0.9383 0.4908 -0.0089 0.1962  0.0110  330 SER B O   
4052 C CB  . SER B 256 ? 1.5273 0.9811 0.4554 0.0412  0.2529  -0.0284 330 SER B CB  
4053 O OG  . SER B 256 ? 1.5217 0.9927 0.4513 0.0172  0.2524  -0.0041 330 SER B OG  
4054 N N   . GLU B 257 ? 1.4741 0.8762 0.4454 0.0054  0.1503  -0.0195 331 GLU B N   
4055 C CA  . GLU B 257 ? 1.4349 0.8290 0.4216 -0.0177 0.1084  -0.0057 331 GLU B CA  
4056 C C   . GLU B 257 ? 1.3882 0.8208 0.4473 -0.0266 0.0983  0.0039  331 GLU B C   
4057 O O   . GLU B 257 ? 1.3854 0.8503 0.4849 -0.0420 0.0911  0.0226  331 GLU B O   
4058 C CB  . GLU B 257 ? 1.4537 0.7850 0.3902 -0.0203 0.0660  -0.0193 331 GLU B CB  
4059 C CG  . GLU B 257 ? 1.6583 0.9466 0.5165 -0.0122 0.0695  -0.0286 331 GLU B CG  
4060 C CD  . GLU B 257 ? 1.6599 0.9128 0.4725 0.0113  0.0873  -0.0536 331 GLU B CD  
4061 O OE1 . GLU B 257 ? 1.6903 0.9405 0.5283 0.0207  0.0886  -0.0649 331 GLU B OE1 
4062 O OE2 . GLU B 257 ? 1.8171 1.0422 0.5657 0.0222  0.0996  -0.0621 331 GLU B OE2 
4063 N N   . LEU B 258 ? 1.4282 0.8537 0.5008 -0.0157 0.0968  -0.0087 332 LEU B N   
4064 C CA  . LEU B 258 ? 1.3150 0.7752 0.4499 -0.0226 0.0872  0.0009  332 LEU B CA  
4065 C C   . LEU B 258 ? 1.2754 0.7998 0.4642 -0.0230 0.1206  0.0152  332 LEU B C   
4066 O O   . LEU B 258 ? 1.2863 0.8441 0.5254 -0.0365 0.1083  0.0302  332 LEU B O   
4067 C CB  . LEU B 258 ? 1.3151 0.7495 0.4444 -0.0076 0.0842  -0.0148 332 LEU B CB  
4068 C CG  . LEU B 258 ? 1.1899 0.6686 0.4020 -0.0127 0.0708  -0.0038 332 LEU B CG  
4069 C CD1 . LEU B 258 ? 1.1928 0.6720 0.4212 -0.0376 0.0301  0.0093  332 LEU B CD1 
4070 C CD2 . LEU B 258 ? 1.2734 0.7310 0.4983 0.0042  0.0671  -0.0172 332 LEU B CD2 
4071 N N   . ARG B 259 ? 1.2669 0.8117 0.4488 -0.0087 0.1624  0.0103  333 ARG B N   
4072 C CA  . ARG B 259 ? 1.2325 0.8417 0.4683 -0.0137 0.1946  0.0241  333 ARG B CA  
4073 C C   . ARG B 259 ? 1.2653 0.8834 0.5092 -0.0393 0.1833  0.0445  333 ARG B C   
4074 O O   . ARG B 259 ? 1.2189 0.8755 0.5154 -0.0532 0.1847  0.0589  333 ARG B O   
4075 C CB  . ARG B 259 ? 1.3150 0.9493 0.5434 0.0057  0.2410  0.0148  333 ARG B CB  
4076 C CG  . ARG B 259 ? 1.3381 1.0472 0.6303 -0.0011 0.2771  0.0277  333 ARG B CG  
4077 C CD  . ARG B 259 ? 1.3871 1.1387 0.7100 0.0292  0.3142  0.0127  333 ARG B CD  
4078 N NE  . ARG B 259 ? 1.4221 1.1365 0.6860 0.0545  0.3251  -0.0070 333 ARG B NE  
4079 C CZ  . ARG B 259 ? 1.4861 1.2272 0.7658 0.0875  0.3545  -0.0239 333 ARG B CZ  
4080 N NH1 . ARG B 259 ? 1.4819 1.2929 0.8395 0.1007  0.3755  -0.0231 333 ARG B NH1 
4081 N NH2 . ARG B 259 ? 1.4486 1.1469 0.6672 0.1097  0.3609  -0.0427 333 ARG B NH2 
4082 N N   . SER B 260 ? 1.3005 0.8781 0.4896 -0.0443 0.1703  0.0455  334 SER B N   
4083 C CA  . SER B 260 ? 1.2402 0.8151 0.4291 -0.0639 0.1561  0.0644  334 SER B CA  
4084 C C   . SER B 260 ? 1.2352 0.8112 0.4623 -0.0746 0.1168  0.0717  334 SER B C   
4085 O O   . SER B 260 ? 1.2286 0.8265 0.4915 -0.0878 0.1145  0.0872  334 SER B O   
4086 C CB  . SER B 260 ? 1.3365 0.8622 0.4530 -0.0624 0.1458  0.0620  334 SER B CB  
4087 O OG  . SER B 260 ? 1.4198 0.9383 0.5297 -0.0776 0.1348  0.0808  334 SER B OG  
4088 N N   . VAL B 261 ? 1.2501 0.8025 0.4709 -0.0693 0.0856  0.0606  335 VAL B N   
4089 C CA  . VAL B 261 ? 1.2175 0.7793 0.4785 -0.0777 0.0497  0.0675  335 VAL B CA  
4090 C C   . VAL B 261 ? 1.1547 0.7635 0.4782 -0.0797 0.0616  0.0746  335 VAL B C   
4091 O O   . VAL B 261 ? 1.1207 0.7478 0.4803 -0.0882 0.0467  0.0860  335 VAL B O   
4092 C CB  . VAL B 261 ? 1.1830 0.7161 0.4289 -0.0749 0.0170  0.0554  335 VAL B CB  
4093 C CG1 . VAL B 261 ? 1.1561 0.7140 0.4550 -0.0819 -0.0138 0.0632  335 VAL B CG1 
4094 C CG2 . VAL B 261 ? 1.2114 0.6986 0.3992 -0.0764 -0.0029 0.0496  335 VAL B CG2 
4095 N N   . LEU B 262 ? 1.1675 0.7947 0.5018 -0.0694 0.0887  0.0668  336 LEU B N   
4096 C CA  . LEU B 262 ? 1.1336 0.8114 0.5368 -0.0685 0.0966  0.0709  336 LEU B CA  
4097 C C   . LEU B 262 ? 1.1364 0.8452 0.5675 -0.0824 0.1159  0.0841  336 LEU B C   
4098 O O   . LEU B 262 ? 1.0174 0.7595 0.5063 -0.0880 0.1038  0.0895  336 LEU B O   
4099 C CB  . LEU B 262 ? 1.0454 0.7462 0.4740 -0.0479 0.1176  0.0565  336 LEU B CB  
4100 C CG  . LEU B 262 ? 1.0552 0.7317 0.4809 -0.0369 0.0935  0.0462  336 LEU B CG  
4101 C CD1 . LEU B 262 ? 1.0937 0.7799 0.5313 -0.0128 0.1159  0.0325  336 LEU B CD1 
4102 C CD2 . LEU B 262 ? 0.9743 0.6778 0.4564 -0.0432 0.0651  0.0546  336 LEU B CD2 
4103 N N   . VAL B 263 ? 1.0886 0.7890 0.4844 -0.0882 0.1446  0.0884  337 VAL B N   
4104 C CA  . VAL B 263 ? 1.0387 0.7643 0.4614 -0.1071 0.1627  0.1033  337 VAL B CA  
4105 C C   . VAL B 263 ? 1.0751 0.7762 0.4984 -0.1203 0.1288  0.1155  337 VAL B C   
4106 O O   . VAL B 263 ? 1.0572 0.7748 0.5166 -0.1355 0.1278  0.1255  337 VAL B O   
4107 C CB  . VAL B 263 ? 1.0628 0.7907 0.4567 -0.1088 0.1979  0.1063  337 VAL B CB  
4108 C CG1 . VAL B 263 ? 0.9796 0.7197 0.3931 -0.1335 0.2093  0.1257  337 VAL B CG1 
4109 C CG2 . VAL B 263 ? 1.0859 0.8544 0.4983 -0.0932 0.2367  0.0940  337 VAL B CG2 
4110 N N   . MET B 264 ? 1.0872 0.7478 0.4710 -0.1140 0.1001  0.1134  338 MET B N   
4111 C CA  . MET B 264 ? 1.0629 0.7030 0.4498 -0.1197 0.0670  0.1223  338 MET B CA  
4112 C C   . MET B 264 ? 1.0124 0.6744 0.4467 -0.1168 0.0442  0.1205  338 MET B C   
4113 O O   . MET B 264 ? 1.0556 0.7172 0.5111 -0.1239 0.0316  0.1290  338 MET B O   
4114 C CB  . MET B 264 ? 1.0991 0.6999 0.4397 -0.1120 0.0408  0.1184  338 MET B CB  
4115 C CG  . MET B 264 ? 1.2502 0.8236 0.5337 -0.1134 0.0601  0.1207  338 MET B CG  
4116 S SD  . MET B 264 ? 1.4339 0.9595 0.6600 -0.1051 0.0253  0.1144  338 MET B SD  
4117 C CE  . MET B 264 ? 1.3873 0.8934 0.6141 -0.1110 0.0003  0.1315  338 MET B CE  
4118 N N   . MET B 265 ? 1.0635 0.7407 0.5109 -0.1058 0.0387  0.1097  339 MET B N   
4119 C CA  . MET B 265 ? 0.9902 0.6909 0.4806 -0.1010 0.0170  0.1089  339 MET B CA  
4120 C C   . MET B 265 ? 0.9199 0.6673 0.4733 -0.1022 0.0313  0.1072  339 MET B C   
4121 O O   . MET B 265 ? 0.9067 0.6715 0.4978 -0.0996 0.0127  0.1076  339 MET B O   
4122 C CB  . MET B 265 ? 0.9152 0.6228 0.4125 -0.0890 0.0076  0.0976  339 MET B CB  
4123 C CG  . MET B 265 ? 0.9981 0.6680 0.4510 -0.0885 -0.0126 0.0938  339 MET B CG  
4124 S SD  . MET B 265 ? 0.9941 0.6600 0.4496 -0.0838 -0.0319 0.0852  339 MET B SD  
4125 C CE  . MET B 265 ? 0.8495 0.5642 0.3769 -0.0809 -0.0512 0.0920  339 MET B CE  
4126 N N   . LEU B 266 ? 0.9469 0.7173 0.5128 -0.1047 0.0632  0.1040  340 LEU B N   
4127 C CA  . LEU B 266 ? 0.8886 0.7100 0.5189 -0.1063 0.0745  0.1006  340 LEU B CA  
4128 C C   . LEU B 266 ? 0.8727 0.6914 0.5092 -0.1290 0.0843  0.1113  340 LEU B C   
4129 O O   . LEU B 266 ? 0.8966 0.7588 0.5847 -0.1362 0.0979  0.1085  340 LEU B O   
4130 C CB  . LEU B 266 ? 0.8001 0.6578 0.4525 -0.0941 0.1013  0.0907  340 LEU B CB  
4131 C CG  . LEU B 266 ? 0.7713 0.6263 0.4215 -0.0724 0.0901  0.0808  340 LEU B CG  
4132 C CD1 . LEU B 266 ? 0.7869 0.6705 0.4553 -0.0554 0.1154  0.0707  340 LEU B CD1 
4133 C CD2 . LEU B 266 ? 0.7763 0.6512 0.4669 -0.0661 0.0628  0.0800  340 LEU B CD2 
4134 N N   . GLU B 267 ? 0.9749 0.7420 0.5603 -0.1413 0.0759  0.1240  341 GLU B N   
4135 C CA  . GLU B 267 ? 0.9599 0.7109 0.5446 -0.1655 0.0827  0.1372  341 GLU B CA  
4136 C C   . GLU B 267 ? 0.9082 0.6811 0.5499 -0.1676 0.0618  0.1313  341 GLU B C   
4137 O O   . GLU B 267 ? 0.9339 0.6987 0.5801 -0.1514 0.0320  0.1254  341 GLU B O   
4138 C CB  . GLU B 267 ? 0.9619 0.6435 0.4744 -0.1723 0.0692  0.1528  341 GLU B CB  
4139 C CG  . GLU B 267 ? 1.0470 0.6962 0.5594 -0.1911 0.0590  0.1656  341 GLU B CG  
4140 C CD  . GLU B 267 ? 1.0987 0.7570 0.6210 -0.2181 0.0928  0.1765  341 GLU B CD  
4141 O OE1 . GLU B 267 ? 1.1437 0.8096 0.6431 -0.2166 0.1197  0.1792  341 GLU B OE1 
4142 O OE2 . GLU B 267 ? 1.1290 0.7879 0.6839 -0.2413 0.0914  0.1819  341 GLU B OE2 
4143 N N   . PRO B 268 ? 0.8910 0.6939 0.5774 -0.1869 0.0761  0.1317  342 PRO B N   
4144 C CA  . PRO B 268 ? 0.8819 0.7066 0.6207 -0.1865 0.0532  0.1212  342 PRO B CA  
4145 C C   . PRO B 268 ? 0.9398 0.7071 0.6530 -0.1916 0.0247  0.1266  342 PRO B C   
4146 O O   . PRO B 268 ? 0.8829 0.6553 0.6171 -0.1758 -0.0017 0.1144  342 PRO B O   
4147 C CB  . PRO B 268 ? 0.8715 0.7429 0.6635 -0.2105 0.0757  0.1208  342 PRO B CB  
4148 C CG  . PRO B 268 ? 0.8969 0.7878 0.6738 -0.2141 0.1146  0.1281  342 PRO B CG  
4149 C CD  . PRO B 268 ? 0.9545 0.7811 0.6509 -0.2090 0.1140  0.1399  342 PRO B CD  
4150 N N   . ASP B 269 ? 1.0051 0.7150 0.6691 -0.2106 0.0297  0.1447  343 ASP B N   
4151 C CA  . ASP B 269 ? 1.0112 0.6577 0.6473 -0.2135 0.0019  0.1510  343 ASP B CA  
4152 C C   . ASP B 269 ? 1.0433 0.6607 0.6402 -0.1831 -0.0239 0.1501  343 ASP B C   
4153 O O   . ASP B 269 ? 1.0739 0.6642 0.6197 -0.1802 -0.0190 0.1618  343 ASP B O   
4154 C CB  . ASP B 269 ? 1.0388 0.6298 0.6336 -0.2462 0.0169  0.1743  343 ASP B CB  
4155 C CG  . ASP B 269 ? 1.1281 0.6529 0.7074 -0.2551 -0.0106 0.1794  343 ASP B CG  
4156 O OD1 . ASP B 269 ? 1.1343 0.6450 0.7150 -0.2274 -0.0430 0.1664  343 ASP B OD1 
4157 O OD2 . ASP B 269 ? 1.1803 0.6674 0.7467 -0.2885 0.0012  0.1960  343 ASP B OD2 
4158 N N   . PRO B 270 ? 1.0382 0.6623 0.6570 -0.1599 -0.0520 0.1361  344 PRO B N   
4159 C CA  . PRO B 270 ? 1.0112 0.6221 0.6048 -0.1311 -0.0749 0.1355  344 PRO B CA  
4160 C C   . PRO B 270 ? 1.0889 0.6283 0.6219 -0.1318 -0.0898 0.1528  344 PRO B C   
4161 O O   . PRO B 270 ? 1.1189 0.6504 0.6244 -0.1137 -0.1041 0.1564  344 PRO B O   
4162 C CB  . PRO B 270 ? 0.9064 0.5395 0.5380 -0.1086 -0.0967 0.1180  344 PRO B CB  
4163 C CG  . PRO B 270 ? 0.9488 0.5660 0.5986 -0.1280 -0.0964 0.1134  344 PRO B CG  
4164 C CD  . PRO B 270 ? 0.9829 0.6237 0.6464 -0.1588 -0.0653 0.1206  344 PRO B CD  
4165 N N   . LYS B 271 ? 1.1663 0.6516 0.6771 -0.1531 -0.0888 0.1644  345 LYS B N   
4166 C CA  . LYS B 271 ? 1.1602 0.5857 0.6188 -0.1512 -0.0990 0.1783  345 LYS B CA  
4167 C C   . LYS B 271 ? 1.1845 0.6251 0.6183 -0.1557 -0.0771 0.1841  345 LYS B C   
4168 O O   . LYS B 271 ? 1.2223 0.6381 0.6222 -0.1416 -0.0901 0.1877  345 LYS B O   
4169 C CB  . LYS B 271 ? 1.2114 0.5846 0.6605 -0.1752 -0.0974 0.1872  345 LYS B CB  
4170 C CG  . LYS B 271 ? 1.2728 0.6194 0.7436 -0.1740 -0.1202 0.1780  345 LYS B CG  
4171 C CD  . LYS B 271 ? 1.3410 0.6411 0.8090 -0.2055 -0.1149 0.1852  345 LYS B CD  
4172 C CE  . LYS B 271 ? 1.4365 0.7448 0.9509 -0.2202 -0.1230 0.1691  345 LYS B CE  
4173 N NZ  . LYS B 271 ? 1.1823 0.5915 0.7575 -0.2150 -0.1056 0.1508  345 LYS B NZ  
4174 N N   . LEU B 272 ? 1.1709 0.6497 0.6194 -0.1738 -0.0447 0.1843  346 LEU B N   
4175 C CA  . LEU B 272 ? 1.2117 0.6992 0.6324 -0.1769 -0.0213 0.1886  346 LEU B CA  
4176 C C   . LEU B 272 ? 1.1485 0.6772 0.5761 -0.1595 -0.0194 0.1758  346 LEU B C   
4177 O O   . LEU B 272 ? 1.1748 0.7068 0.5754 -0.1584 -0.0034 0.1759  346 LEU B O   
4178 C CB  . LEU B 272 ? 1.2030 0.7045 0.6339 -0.2068 0.0174  0.1981  346 LEU B CB  
4179 C CG  . LEU B 272 ? 1.2478 0.7130 0.6808 -0.2325 0.0204  0.2118  346 LEU B CG  
4180 C CD1 . LEU B 272 ? 1.2608 0.7620 0.7232 -0.2633 0.0611  0.2194  346 LEU B CD1 
4181 C CD2 . LEU B 272 ? 1.3070 0.7128 0.6860 -0.2270 0.0075  0.2247  346 LEU B CD2 
4182 N N   . ARG B 273 ? 1.1194 0.6758 0.5794 -0.1457 -0.0361 0.1652  347 ARG B N   
4183 C CA  . ARG B 273 ? 1.1242 0.7179 0.5946 -0.1317 -0.0350 0.1536  347 ARG B CA  
4184 C C   . ARG B 273 ? 1.1303 0.7105 0.5786 -0.1136 -0.0600 0.1498  347 ARG B C   
4185 O O   . ARG B 273 ? 1.0927 0.6533 0.5386 -0.1025 -0.0868 0.1522  347 ARG B O   
4186 C CB  . ARG B 273 ? 1.0502 0.6802 0.5636 -0.1244 -0.0436 0.1461  347 ARG B CB  
4187 C CG  . ARG B 273 ? 0.9886 0.6583 0.5198 -0.1116 -0.0408 0.1344  347 ARG B CG  
4188 C CD  . ARG B 273 ? 0.9055 0.6271 0.5011 -0.1003 -0.0440 0.1216  347 ARG B CD  
4189 N NE  . ARG B 273 ? 0.8548 0.5945 0.4825 -0.1124 -0.0271 0.1190  347 ARG B NE  
4190 C CZ  . ARG B 273 ? 0.8288 0.5936 0.4998 -0.1065 -0.0368 0.1102  347 ARG B CZ  
4191 N NH1 . ARG B 273 ? 0.8127 0.5894 0.4988 -0.0864 -0.0587 0.1039  347 ARG B NH1 
4192 N NH2 . ARG B 273 ? 0.8268 0.6076 0.5266 -0.1214 -0.0241 0.1073  347 ARG B NH2 
4193 N N   . ALA B 274 ? 1.1624 0.7520 0.5943 -0.1107 -0.0519 0.1433  348 ALA B N   
4194 C CA  . ALA B 274 ? 1.0971 0.6757 0.5098 -0.0983 -0.0769 0.1389  348 ALA B CA  
4195 C C   . ALA B 274 ? 1.0983 0.7059 0.5523 -0.0841 -0.1040 0.1330  348 ALA B C   
4196 O O   . ALA B 274 ? 1.0771 0.7174 0.5695 -0.0823 -0.0996 0.1293  348 ALA B O   
4197 C CB  . ALA B 274 ? 1.1174 0.6957 0.5030 -0.0997 -0.0644 0.1309  348 ALA B CB  
4198 N N   . THR B 275 ? 1.1251 0.7237 0.5715 -0.0734 -0.1319 0.1332  349 THR B N   
4199 C CA  . THR B 275 ? 1.0272 0.6613 0.5149 -0.0598 -0.1563 0.1285  349 THR B CA  
4200 C C   . THR B 275 ? 1.0364 0.6869 0.5248 -0.0636 -0.1615 0.1207  349 THR B C   
4201 O O   . THR B 275 ? 1.0272 0.6508 0.4742 -0.0719 -0.1545 0.1179  349 THR B O   
4202 C CB  . THR B 275 ? 1.0437 0.6652 0.5288 -0.0448 -0.1845 0.1333  349 THR B CB  
4203 O OG1 . THR B 275 ? 1.0857 0.6688 0.5211 -0.0486 -0.1907 0.1368  349 THR B OG1 
4204 C CG2 . THR B 275 ? 1.1400 0.7406 0.6269 -0.0392 -0.1836 0.1394  349 THR B CG2 
4205 N N   . ALA B 276 ? 0.9751 0.6676 0.5082 -0.0582 -0.1740 0.1175  350 ALA B N   
4206 C CA  . ALA B 276 ? 0.9726 0.6752 0.5066 -0.0658 -0.1836 0.1117  350 ALA B CA  
4207 C C   . ALA B 276 ? 0.9813 0.6627 0.4874 -0.0658 -0.2093 0.1108  350 ALA B C   
4208 O O   . ALA B 276 ? 1.0485 0.7073 0.5223 -0.0761 -0.2129 0.1045  350 ALA B O   
4209 C CB  . ALA B 276 ? 0.9439 0.6979 0.5334 -0.0627 -0.1934 0.1123  350 ALA B CB  
4210 N N   . GLU B 277 ? 0.9970 0.6821 0.5115 -0.0524 -0.2287 0.1163  351 GLU B N   
4211 C CA  . GLU B 277 ? 1.0302 0.6963 0.5174 -0.0498 -0.2552 0.1165  351 GLU B CA  
4212 C C   . GLU B 277 ? 1.0691 0.6775 0.4868 -0.0571 -0.2428 0.1166  351 GLU B C   
4213 O O   . GLU B 277 ? 1.0947 0.6805 0.4762 -0.0615 -0.2583 0.1124  351 GLU B O   
4214 C CB  . GLU B 277 ? 0.9842 0.6658 0.4945 -0.0295 -0.2765 0.1232  351 GLU B CB  
4215 C CG  . GLU B 277 ? 1.0384 0.7177 0.5366 -0.0230 -0.3098 0.1236  351 GLU B CG  
4216 C CD  . GLU B 277 ? 1.1994 0.8685 0.6944 -0.0010 -0.3247 0.1317  351 GLU B CD  
4217 O OE1 . GLU B 277 ? 1.2585 0.9327 0.7743 0.0103  -0.3133 0.1353  351 GLU B OE1 
4218 O OE2 . GLU B 277 ? 1.2539 0.9057 0.7222 0.0057  -0.3492 0.1341  351 GLU B OE2 
4219 N N   . ALA B 278 ? 1.1036 0.6893 0.5017 -0.0591 -0.2152 0.1216  352 ALA B N   
4220 C CA  . ALA B 278 ? 1.0964 0.6346 0.4309 -0.0668 -0.1980 0.1234  352 ALA B CA  
4221 C C   . ALA B 278 ? 1.1627 0.6950 0.4756 -0.0775 -0.1812 0.1127  352 ALA B C   
4222 O O   . ALA B 278 ? 1.2729 0.7705 0.5315 -0.0803 -0.1825 0.1090  352 ALA B O   
4223 C CB  . ALA B 278 ? 1.1058 0.6272 0.4313 -0.0699 -0.1719 0.1330  352 ALA B CB  
4224 N N   . LEU B 279 ? 1.1139 0.6762 0.4644 -0.0815 -0.1661 0.1073  353 LEU B N   
4225 C CA  . LEU B 279 ? 1.1033 0.6553 0.4315 -0.0886 -0.1502 0.0966  353 LEU B CA  
4226 C C   . LEU B 279 ? 1.1232 0.6596 0.4309 -0.0919 -0.1793 0.0874  353 LEU B C   
4227 O O   . LEU B 279 ? 1.2346 0.7333 0.4880 -0.0947 -0.1744 0.0789  353 LEU B O   
4228 C CB  . LEU B 279 ? 1.0645 0.6514 0.4388 -0.0900 -0.1335 0.0943  353 LEU B CB  
4229 C CG  . LEU B 279 ? 1.0948 0.6953 0.4861 -0.0892 -0.1042 0.1014  353 LEU B CG  
4230 C CD1 . LEU B 279 ? 1.0467 0.6844 0.4850 -0.0883 -0.0933 0.0997  353 LEU B CD1 
4231 C CD2 . LEU B 279 ? 1.1750 0.7484 0.5191 -0.0930 -0.0737 0.1012  353 LEU B CD2 
4232 N N   . LEU B 280 ? 1.1133 0.6790 0.4636 -0.0916 -0.2107 0.0889  354 LEU B N   
4233 C CA  . LEU B 280 ? 1.1194 0.6759 0.4587 -0.0985 -0.2432 0.0813  354 LEU B CA  
4234 C C   . LEU B 280 ? 1.2003 0.7161 0.4815 -0.0950 -0.2587 0.0799  354 LEU B C   
4235 O O   . LEU B 280 ? 1.3424 0.8389 0.5992 -0.1017 -0.2831 0.0708  354 LEU B O   
4236 C CB  . LEU B 280 ? 1.0411 0.6493 0.4465 -0.0982 -0.2723 0.0861  354 LEU B CB  
4237 C CG  . LEU B 280 ? 1.0519 0.7005 0.5113 -0.1039 -0.2620 0.0879  354 LEU B CG  
4238 C CD1 . LEU B 280 ? 0.9600 0.6688 0.4878 -0.0978 -0.2827 0.0960  354 LEU B CD1 
4239 C CD2 . LEU B 280 ? 1.0467 0.6760 0.4911 -0.1218 -0.2678 0.0784  354 LEU B CD2 
4240 N N   . ALA B 281 ? 1.2186 0.7187 0.4752 -0.0858 -0.2471 0.0893  355 ALA B N   
4241 C CA  . ALA B 281 ? 1.3075 0.7649 0.5006 -0.0818 -0.2592 0.0904  355 ALA B CA  
4242 C C   . ALA B 281 ? 1.3370 0.7498 0.4621 -0.0851 -0.2305 0.0844  355 ALA B C   
4243 O O   . ALA B 281 ? 1.4534 0.8270 0.5166 -0.0825 -0.2404 0.0827  355 ALA B O   
4244 C CB  . ALA B 281 ? 1.3157 0.7704 0.5078 -0.0708 -0.2623 0.1055  355 ALA B CB  
4245 N N   . LEU B 282 ? 1.3581 0.7786 0.4927 -0.0887 -0.1949 0.0811  356 LEU B N   
4246 C CA  . LEU B 282 ? 1.3979 0.7846 0.4732 -0.0884 -0.1639 0.0748  356 LEU B CA  
4247 C C   . LEU B 282 ? 1.4903 0.8430 0.5213 -0.0899 -0.1818 0.0576  356 LEU B C   
4248 O O   . LEU B 282 ? 1.4655 0.8290 0.5270 -0.0961 -0.2098 0.0497  356 LEU B O   
4249 C CB  . LEU B 282 ? 1.4088 0.8197 0.5134 -0.0895 -0.1245 0.0740  356 LEU B CB  
4250 C CG  . LEU B 282 ? 1.3415 0.7797 0.4818 -0.0902 -0.1026 0.0897  356 LEU B CG  
4251 C CD1 . LEU B 282 ? 1.2756 0.7440 0.4514 -0.0916 -0.0688 0.0873  356 LEU B CD1 
4252 C CD2 . LEU B 282 ? 1.2911 0.7010 0.3804 -0.0901 -0.0871 0.1014  356 LEU B CD2 
4253 N N   . PRO B 283 ? 1.5123 0.8230 0.4701 -0.0851 -0.1668 0.0517  357 PRO B N   
4254 C CA  . PRO B 283 ? 1.5631 0.8335 0.4709 -0.0851 -0.1862 0.0332  357 PRO B CA  
4255 C C   . PRO B 283 ? 1.5789 0.8511 0.5100 -0.0894 -0.1835 0.0180  357 PRO B C   
4256 O O   . PRO B 283 ? 1.6764 0.9277 0.5990 -0.0961 -0.2162 0.0054  357 PRO B O   
4257 C CB  . PRO B 283 ? 1.6359 0.8678 0.4634 -0.0757 -0.1571 0.0308  357 PRO B CB  
4258 C CG  . PRO B 283 ? 1.5947 0.8419 0.4256 -0.0745 -0.1395 0.0524  357 PRO B CG  
4259 C CD  . PRO B 283 ? 1.5504 0.8477 0.4655 -0.0801 -0.1331 0.0625  357 PRO B CD  
4260 N N   . VAL B 284 ? 1.5572 0.8532 0.5182 -0.0865 -0.1472 0.0194  358 VAL B N   
4261 C CA  . VAL B 284 ? 1.5007 0.7916 0.4759 -0.0878 -0.1425 0.0056  358 VAL B CA  
4262 C C   . VAL B 284 ? 1.4935 0.8120 0.5322 -0.1017 -0.1755 0.0087  358 VAL B C   
4263 O O   . VAL B 284 ? 1.5341 0.8358 0.5757 -0.1075 -0.1850 -0.0030 358 VAL B O   
4264 C CB  . VAL B 284 ? 1.5007 0.8144 0.4916 -0.0780 -0.0940 0.0074  358 VAL B CB  
4265 C CG1 . VAL B 284 ? 1.4783 0.7728 0.4110 -0.0654 -0.0587 0.0049  358 VAL B CG1 
4266 C CG2 . VAL B 284 ? 1.4617 0.8310 0.5210 -0.0827 -0.0857 0.0262  358 VAL B CG2 
4267 N N   . LEU B 285 ? 1.5087 0.8685 0.5979 -0.1066 -0.1929 0.0243  359 LEU B N   
4268 C CA  . LEU B 285 ? 1.5007 0.9008 0.6589 -0.1177 -0.2174 0.0299  359 LEU B CA  
4269 C C   . LEU B 285 ? 1.5716 0.9797 0.7455 -0.1266 -0.2639 0.0314  359 LEU B C   
4270 O O   . LEU B 285 ? 1.5216 0.9730 0.7589 -0.1357 -0.2847 0.0379  359 LEU B O   
4271 C CB  . LEU B 285 ? 1.3330 0.7855 0.5495 -0.1126 -0.1982 0.0457  359 LEU B CB  
4272 C CG  . LEU B 285 ? 1.2788 0.7421 0.5075 -0.1079 -0.1602 0.0448  359 LEU B CG  
4273 C CD1 . LEU B 285 ? 1.1268 0.6325 0.3984 -0.1016 -0.1386 0.0592  359 LEU B CD1 
4274 C CD2 . LEU B 285 ? 1.2626 0.7344 0.5211 -0.1171 -0.1719 0.0407  359 LEU B CD2 
4275 N N   . ARG B 286 ? 1.6572 1.0291 0.7768 -0.1236 -0.2804 0.0258  360 ARG B N   
4276 C CA  . ARG B 286 ? 1.6946 1.0774 0.8287 -0.1299 -0.3259 0.0266  360 ARG B CA  
4277 C C   . ARG B 286 ? 1.7740 1.1382 0.9078 -0.1473 -0.3543 0.0121  360 ARG B C   
4278 O O   . ARG B 286 ? 1.8459 1.1544 0.9147 -0.1477 -0.3577 -0.0030 360 ARG B O   
4279 C CB  . ARG B 286 ? 1.7257 1.0754 0.7973 -0.1188 -0.3337 0.0272  360 ARG B CB  
4280 C CG  . ARG B 286 ? 1.6768 1.0448 0.7548 -0.1054 -0.3178 0.0443  360 ARG B CG  
4281 C CD  . ARG B 286 ? 1.7952 1.1236 0.8040 -0.0966 -0.3306 0.0456  360 ARG B CD  
4282 N NE  . ARG B 286 ? 1.9808 1.3046 0.9840 -0.1016 -0.3781 0.0373  360 ARG B NE  
4283 C CZ  . ARG B 286 ? 2.0535 1.3360 0.9883 -0.0965 -0.3975 0.0326  360 ARG B CZ  
4284 N NH1 . ARG B 286 ? 2.1144 1.3545 0.9762 -0.0864 -0.3720 0.0362  360 ARG B NH1 
4285 N NH2 . ARG B 286 ? 1.9813 1.2679 0.9217 -0.1026 -0.4439 0.0244  360 ARG B NH2 
4286 N N   . GLN B 287 ? 1.7190 1.1299 0.9260 -0.1623 -0.3748 0.0170  361 GLN B N   
4287 C CA  . GLN B 287 ? 1.7047 1.1054 0.9259 -0.1849 -0.4054 0.0064  361 GLN B CA  
4288 C C   . GLN B 287 ? 1.7268 1.0651 0.8963 -0.1893 -0.3876 -0.0091 361 GLN B C   
4289 O O   . GLN B 287 ? 1.7062 1.0420 0.9044 -0.2085 -0.3972 -0.0129 361 GLN B O   
4290 C CB  . GLN B 287 ? 1.7286 1.1189 0.9302 -0.1891 -0.4468 -0.0007 361 GLN B CB  
4291 C CG  . GLN B 287 ? 1.8688 1.2349 1.0712 -0.2136 -0.4789 -0.0151 361 GLN B CG  
4292 C CD  . GLN B 287 ? 1.7887 1.2190 1.0880 -0.2383 -0.4999 -0.0065 361 GLN B CD  
4293 O OE1 . GLN B 287 ? 1.6568 1.1387 1.0156 -0.2378 -0.4813 0.0081  361 GLN B OE1 
4294 N NE2 . GLN B 287 ? 1.7286 1.1582 1.0452 -0.2609 -0.5381 -0.0155 361 GLN B NE2 
# 
