data_9LGN
# 
_entry.id   9LGN 
# 
_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   9LGN         pdb_00009lgn 10.2210/pdb9lgn/pdb 
WWPDB D_1300055594 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-07 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LGN 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_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 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9LGL 
_pdbx_database_related.content_type   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  ? 
primary 'Tang, Y.'   7  ? 
primary 'Xu, Z.'     8  ? 
primary 'Yang, J.'   9  ? 
primary 'Huang, K.'  10 ? 
primary 'Li, C.'     11 ? 
primary 'Chen, S.'   12 ? 
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 ? 
primary 'Zhu, W.'    25 ? 
primary 'Tan, X.'    26 ? 
primary 'Wu, J.'     27 ? 
# 
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'  31515.887 2   2.7.11.1 ? ? ? 
2 non-polymer syn '3-azanyl-4-(7-fluoranyl-2H-indazol-4-yl)-8-methoxy-1H-1,5-naphthyridin-2-one' 325.297   2   ?        ? ? ? 
3 non-polymer syn 'SULFATE ION'                                                                  96.063    7   ?        ? ? ? 
4 water       nat water                                                                          18.015    108 ?        ? ? ? 
# 
_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       
;ALQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKL
AEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDVK
PANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQL
RQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ALQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKL
AEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDVK
PANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQL
RQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQ
;
_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 '3-azanyl-4-(7-fluoranyl-2H-indazol-4-yl)-8-methoxy-1H-1,5-naphthyridin-2-one' A1EJU 
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   ALA n 
1 2   LEU n 
1 3   GLN n 
1 4   PRO n 
1 5   ARG n 
1 6   ARG n 
1 7   VAL n 
1 8   SER n 
1 9   PHE n 
1 10  ARG n 
1 11  GLY n 
1 12  GLU n 
1 13  ALA n 
1 14  SER n 
1 15  GLU n 
1 16  THR n 
1 17  LEU n 
1 18  GLN n 
1 19  SER n 
1 20  PRO n 
1 21  GLY n 
1 22  TYR n 
1 23  ASP n 
1 24  PRO n 
1 25  SER n 
1 26  ARG n 
1 27  PRO n 
1 28  GLU n 
1 29  SER n 
1 30  PHE n 
1 31  PHE n 
1 32  GLN n 
1 33  GLN n 
1 34  SER n 
1 35  PHE n 
1 36  GLN n 
1 37  ARG n 
1 38  LEU n 
1 39  SER n 
1 40  ARG n 
1 41  LEU n 
1 42  GLY n 
1 43  HIS n 
1 44  GLY n 
1 45  SER n 
1 46  TYR n 
1 47  GLY n 
1 48  GLU n 
1 49  VAL n 
1 50  PHE n 
1 51  LYS n 
1 52  VAL n 
1 53  ARG n 
1 54  SER n 
1 55  LYS n 
1 56  GLU n 
1 57  ASP n 
1 58  GLY n 
1 59  ARG n 
1 60  LEU n 
1 61  TYR n 
1 62  ALA n 
1 63  VAL n 
1 64  LYS n 
1 65  ARG n 
1 66  SER n 
1 67  MET n 
1 68  SER n 
1 69  PRO n 
1 70  PHE n 
1 71  ARG n 
1 72  GLY n 
1 73  PRO n 
1 74  LYS n 
1 75  ASP n 
1 76  ARG n 
1 77  ALA n 
1 78  ARG n 
1 79  LYS n 
1 80  LEU n 
1 81  ALA n 
1 82  GLU n 
1 83  VAL n 
1 84  GLY n 
1 85  SER n 
1 86  HIS n 
1 87  GLU n 
1 88  LYS n 
1 89  VAL n 
1 90  GLY n 
1 91  GLN n 
1 92  HIS n 
1 93  PRO n 
1 94  CYS n 
1 95  CYS n 
1 96  VAL n 
1 97  ARG n 
1 98  LEU n 
1 99  GLU n 
1 100 GLN n 
1 101 ALA n 
1 102 TRP n 
1 103 GLU n 
1 104 GLU n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 TYR n 
1 110 LEU n 
1 111 GLN n 
1 112 THR n 
1 113 GLU n 
1 114 LEU n 
1 115 CYS n 
1 116 GLY n 
1 117 PRO n 
1 118 SER n 
1 119 LEU n 
1 120 GLN n 
1 121 GLN n 
1 122 HIS n 
1 123 CYS n 
1 124 GLU n 
1 125 ALA n 
1 126 TRP n 
1 127 GLY n 
1 128 ALA n 
1 129 SER n 
1 130 LEU n 
1 131 PRO n 
1 132 GLU n 
1 133 ALA n 
1 134 GLN n 
1 135 VAL n 
1 136 TRP n 
1 137 GLY n 
1 138 TYR n 
1 139 LEU n 
1 140 ARG n 
1 141 ASP n 
1 142 THR n 
1 143 LEU n 
1 144 LEU n 
1 145 ALA n 
1 146 LEU n 
1 147 ALA n 
1 148 HIS n 
1 149 LEU n 
1 150 HIS n 
1 151 SER n 
1 152 GLN n 
1 153 GLY n 
1 154 LEU n 
1 155 VAL n 
1 156 HIS n 
1 157 LEU n 
1 158 ASP n 
1 159 VAL n 
1 160 LYS n 
1 161 PRO n 
1 162 ALA n 
1 163 ASN n 
1 164 ILE n 
1 165 PHE n 
1 166 LEU n 
1 167 GLY n 
1 168 PRO n 
1 169 ARG n 
1 170 GLY n 
1 171 ARG n 
1 172 CYS n 
1 173 LYS n 
1 174 LEU n 
1 175 GLY n 
1 176 ASP n 
1 177 PHE n 
1 178 GLY n 
1 179 LEU n 
1 180 LEU n 
1 181 VAL n 
1 182 GLU n 
1 183 LEU n 
1 184 GLY n 
1 185 THR n 
1 186 ALA n 
1 187 GLY n 
1 188 ALA n 
1 189 GLY n 
1 190 GLU n 
1 191 VAL n 
1 192 GLN n 
1 193 GLU n 
1 194 GLY n 
1 195 ASP n 
1 196 PRO n 
1 197 ARG n 
1 198 TYR n 
1 199 MET n 
1 200 ALA n 
1 201 PRO n 
1 202 GLU n 
1 203 LEU n 
1 204 LEU n 
1 205 GLN n 
1 206 GLY n 
1 207 SER n 
1 208 TYR n 
1 209 GLY n 
1 210 THR n 
1 211 ALA n 
1 212 ALA n 
1 213 ASP n 
1 214 VAL n 
1 215 PHE n 
1 216 SER n 
1 217 LEU n 
1 218 GLY n 
1 219 LEU n 
1 220 THR n 
1 221 ILE n 
1 222 LEU n 
1 223 GLU n 
1 224 VAL n 
1 225 ALA n 
1 226 CYS n 
1 227 ASN n 
1 228 MET n 
1 229 GLU n 
1 230 LEU n 
1 231 PRO n 
1 232 HIS n 
1 233 GLY n 
1 234 GLY n 
1 235 GLU n 
1 236 GLY n 
1 237 TRP n 
1 238 GLN n 
1 239 GLN n 
1 240 LEU n 
1 241 ARG n 
1 242 GLN n 
1 243 GLY n 
1 244 TYR n 
1 245 LEU n 
1 246 PRO n 
1 247 PRO n 
1 248 GLU n 
1 249 PHE n 
1 250 THR n 
1 251 ALA n 
1 252 GLY n 
1 253 LEU n 
1 254 SER n 
1 255 SER n 
1 256 GLU n 
1 257 LEU n 
1 258 ARG n 
1 259 SER n 
1 260 VAL n 
1 261 LEU n 
1 262 VAL n 
1 263 MET n 
1 264 MET n 
1 265 LEU n 
1 266 GLU n 
1 267 PRO n 
1 268 ASP n 
1 269 PRO n 
1 270 LYS n 
1 271 LEU n 
1 272 ARG n 
1 273 ALA n 
1 274 THR n 
1 275 ALA n 
1 276 GLU n 
1 277 ALA n 
1 278 LEU n 
1 279 LEU n 
1 280 ALA n 
1 281 LEU n 
1 282 PRO n 
1 283 VAL n 
1 284 LEU n 
1 285 ARG n 
1 286 GLN 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                   286 
_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                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EJU non-polymer         . '3-azanyl-4-(7-fluoranyl-2H-indazol-4-yl)-8-methoxy-1H-1,5-naphthyridin-2-one' ? 'C16 H12 F N5 O2' 
325.297 
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   ALA 1   76  76  ALA ALA A . n 
A 1 2   LEU 2   77  77  LEU LEU A . n 
A 1 3   GLN 3   78  78  GLN GLN A . n 
A 1 4   PRO 4   79  79  PRO PRO A . n 
A 1 5   ARG 5   80  80  ARG ARG A . n 
A 1 6   ARG 6   81  81  ARG ARG A . n 
A 1 7   VAL 7   82  82  VAL VAL A . n 
A 1 8   SER 8   83  83  SER SER A . n 
A 1 9   PHE 9   84  84  PHE PHE A . n 
A 1 10  ARG 10  85  85  ARG ARG A . n 
A 1 11  GLY 11  86  86  GLY GLY A . n 
A 1 12  GLU 12  87  87  GLU GLU A . n 
A 1 13  ALA 13  88  88  ALA ALA A . n 
A 1 14  SER 14  89  89  SER SER A . n 
A 1 15  GLU 15  90  90  GLU GLU A . n 
A 1 16  THR 16  91  91  THR THR A . n 
A 1 17  LEU 17  92  92  LEU LEU A . n 
A 1 18  GLN 18  93  93  GLN GLN A . n 
A 1 19  SER 19  94  94  SER SER A . n 
A 1 20  PRO 20  95  95  PRO PRO A . n 
A 1 21  GLY 21  96  96  GLY GLY A . n 
A 1 22  TYR 22  97  97  TYR TYR A . n 
A 1 23  ASP 23  98  98  ASP ASP A . n 
A 1 24  PRO 24  99  99  PRO PRO A . n 
A 1 25  SER 25  100 100 SER SER A . n 
A 1 26  ARG 26  101 101 ARG ARG A . n 
A 1 27  PRO 27  102 102 PRO PRO A . n 
A 1 28  GLU 28  103 103 GLU GLU A . n 
A 1 29  SER 29  104 104 SER SER A . n 
A 1 30  PHE 30  105 105 PHE PHE A . n 
A 1 31  PHE 31  106 106 PHE PHE A . n 
A 1 32  GLN 32  107 107 GLN GLN A . n 
A 1 33  GLN 33  108 108 GLN GLN A . n 
A 1 34  SER 34  109 109 SER SER A . n 
A 1 35  PHE 35  110 110 PHE PHE A . n 
A 1 36  GLN 36  111 111 GLN GLN A . n 
A 1 37  ARG 37  112 112 ARG ARG A . n 
A 1 38  LEU 38  113 113 LEU LEU A . n 
A 1 39  SER 39  114 114 SER SER A . n 
A 1 40  ARG 40  115 115 ARG ARG A . n 
A 1 41  LEU 41  116 116 LEU LEU A . n 
A 1 42  GLY 42  117 117 GLY GLY A . n 
A 1 43  HIS 43  118 118 HIS HIS A . n 
A 1 44  GLY 44  119 119 GLY GLY A . n 
A 1 45  SER 45  120 120 SER SER A . n 
A 1 46  TYR 46  121 121 TYR TYR A . n 
A 1 47  GLY 47  122 122 GLY GLY A . n 
A 1 48  GLU 48  123 123 GLU GLU A . n 
A 1 49  VAL 49  124 124 VAL VAL A . n 
A 1 50  PHE 50  125 125 PHE PHE A . n 
A 1 51  LYS 51  126 126 LYS LYS A . n 
A 1 52  VAL 52  127 127 VAL VAL A . n 
A 1 53  ARG 53  128 128 ARG ARG A . n 
A 1 54  SER 54  129 129 SER SER A . n 
A 1 55  LYS 55  130 130 LYS LYS A . n 
A 1 56  GLU 56  131 131 GLU GLU A . n 
A 1 57  ASP 57  132 132 ASP ASP A . n 
A 1 58  GLY 58  133 133 GLY GLY A . n 
A 1 59  ARG 59  134 134 ARG ARG A . n 
A 1 60  LEU 60  135 135 LEU LEU A . n 
A 1 61  TYR 61  136 136 TYR TYR A . n 
A 1 62  ALA 62  137 137 ALA ALA A . n 
A 1 63  VAL 63  138 138 VAL VAL A . n 
A 1 64  LYS 64  139 139 LYS LYS A . n 
A 1 65  ARG 65  140 140 ARG ARG A . n 
A 1 66  SER 66  141 141 SER SER A . n 
A 1 67  MET 67  142 142 MET MET A . n 
A 1 68  SER 68  143 143 SER SER A . n 
A 1 69  PRO 69  144 144 PRO PRO A . n 
A 1 70  PHE 70  145 145 PHE PHE A . n 
A 1 71  ARG 71  146 146 ARG ARG A . n 
A 1 72  GLY 72  147 147 GLY GLY A . n 
A 1 73  PRO 73  148 148 PRO PRO A . n 
A 1 74  LYS 74  149 149 LYS LYS A . n 
A 1 75  ASP 75  150 150 ASP ASP A . n 
A 1 76  ARG 76  151 151 ARG ARG A . n 
A 1 77  ALA 77  152 152 ALA ALA A . n 
A 1 78  ARG 78  153 153 ARG ARG A . n 
A 1 79  LYS 79  154 154 LYS LYS A . n 
A 1 80  LEU 80  155 155 LEU LEU A . n 
A 1 81  ALA 81  156 156 ALA ALA A . n 
A 1 82  GLU 82  157 157 GLU GLU A . n 
A 1 83  VAL 83  158 158 VAL VAL A . n 
A 1 84  GLY 84  159 159 GLY GLY A . n 
A 1 85  SER 85  160 160 SER SER A . n 
A 1 86  HIS 86  161 161 HIS HIS A . n 
A 1 87  GLU 87  162 162 GLU GLU A . n 
A 1 88  LYS 88  163 163 LYS LYS A . n 
A 1 89  VAL 89  164 164 VAL VAL A . n 
A 1 90  GLY 90  165 165 GLY GLY A . n 
A 1 91  GLN 91  166 166 GLN GLN A . n 
A 1 92  HIS 92  167 167 HIS HIS A . n 
A 1 93  PRO 93  168 168 PRO PRO A . n 
A 1 94  CYS 94  169 169 CYS CYS A . n 
A 1 95  CYS 95  170 170 CYS CYS A . n 
A 1 96  VAL 96  171 171 VAL VAL A . n 
A 1 97  ARG 97  172 172 ARG ARG A . n 
A 1 98  LEU 98  173 173 LEU LEU A . n 
A 1 99  GLU 99  174 174 GLU GLU A . n 
A 1 100 GLN 100 175 175 GLN GLN A . n 
A 1 101 ALA 101 176 176 ALA ALA A . n 
A 1 102 TRP 102 177 177 TRP TRP A . n 
A 1 103 GLU 103 178 178 GLU GLU A . n 
A 1 104 GLU 104 179 179 GLU GLU A . n 
A 1 105 GLY 105 180 180 GLY GLY A . n 
A 1 106 GLY 106 181 181 GLY GLY A . n 
A 1 107 ILE 107 182 182 ILE ILE A . n 
A 1 108 LEU 108 183 183 LEU LEU A . n 
A 1 109 TYR 109 184 184 TYR TYR A . n 
A 1 110 LEU 110 185 185 LEU LEU A . n 
A 1 111 GLN 111 186 186 GLN GLN A . n 
A 1 112 THR 112 187 187 THR THR A . n 
A 1 113 GLU 113 188 188 GLU GLU A . n 
A 1 114 LEU 114 189 189 LEU LEU A . n 
A 1 115 CYS 115 190 190 CYS CYS A . n 
A 1 116 GLY 116 191 191 GLY GLY A . n 
A 1 117 PRO 117 192 192 PRO PRO A . n 
A 1 118 SER 118 193 193 SER SER A . n 
A 1 119 LEU 119 194 194 LEU LEU A . n 
A 1 120 GLN 120 195 195 GLN GLN A . n 
A 1 121 GLN 121 196 196 GLN GLN A . n 
A 1 122 HIS 122 197 197 HIS HIS A . n 
A 1 123 CYS 123 198 198 CYS CYS A . n 
A 1 124 GLU 124 199 199 GLU GLU A . n 
A 1 125 ALA 125 200 200 ALA ALA A . n 
A 1 126 TRP 126 201 201 TRP TRP A . n 
A 1 127 GLY 127 202 202 GLY GLY A . n 
A 1 128 ALA 128 203 203 ALA ALA A . n 
A 1 129 SER 129 204 204 SER SER A . n 
A 1 130 LEU 130 205 205 LEU LEU A . n 
A 1 131 PRO 131 206 206 PRO PRO A . n 
A 1 132 GLU 132 207 207 GLU GLU A . n 
A 1 133 ALA 133 208 208 ALA ALA A . n 
A 1 134 GLN 134 209 209 GLN GLN A . n 
A 1 135 VAL 135 210 210 VAL VAL A . n 
A 1 136 TRP 136 211 211 TRP TRP A . n 
A 1 137 GLY 137 212 212 GLY GLY A . n 
A 1 138 TYR 138 213 213 TYR TYR A . n 
A 1 139 LEU 139 214 214 LEU LEU A . n 
A 1 140 ARG 140 215 215 ARG ARG A . n 
A 1 141 ASP 141 216 216 ASP ASP A . n 
A 1 142 THR 142 217 217 THR THR A . n 
A 1 143 LEU 143 218 218 LEU LEU A . n 
A 1 144 LEU 144 219 219 LEU LEU A . n 
A 1 145 ALA 145 220 220 ALA ALA A . n 
A 1 146 LEU 146 221 221 LEU LEU A . n 
A 1 147 ALA 147 222 222 ALA ALA A . n 
A 1 148 HIS 148 223 223 HIS HIS A . n 
A 1 149 LEU 149 224 224 LEU LEU A . n 
A 1 150 HIS 150 225 225 HIS HIS A . n 
A 1 151 SER 151 226 226 SER SER A . n 
A 1 152 GLN 152 227 227 GLN GLN A . n 
A 1 153 GLY 153 228 228 GLY GLY A . n 
A 1 154 LEU 154 229 229 LEU LEU A . n 
A 1 155 VAL 155 230 230 VAL VAL A . n 
A 1 156 HIS 156 231 231 HIS HIS A . n 
A 1 157 LEU 157 232 232 LEU LEU A . n 
A 1 158 ASP 158 233 233 ASP ASP A . n 
A 1 159 VAL 159 234 234 VAL VAL A . n 
A 1 160 LYS 160 235 235 LYS LYS A . n 
A 1 161 PRO 161 236 236 PRO PRO A . n 
A 1 162 ALA 162 237 237 ALA ALA A . n 
A 1 163 ASN 163 238 238 ASN ASN A . n 
A 1 164 ILE 164 239 239 ILE ILE A . n 
A 1 165 PHE 165 240 240 PHE PHE A . n 
A 1 166 LEU 166 241 241 LEU LEU A . n 
A 1 167 GLY 167 242 242 GLY GLY A . n 
A 1 168 PRO 168 243 243 PRO PRO A . n 
A 1 169 ARG 169 244 244 ARG ARG A . n 
A 1 170 GLY 170 245 245 GLY GLY A . n 
A 1 171 ARG 171 246 246 ARG ARG A . n 
A 1 172 CYS 172 247 247 CYS CYS A . n 
A 1 173 LYS 173 248 248 LYS LYS A . n 
A 1 174 LEU 174 249 249 LEU LEU A . n 
A 1 175 GLY 175 250 250 GLY GLY A . n 
A 1 176 ASP 176 251 251 ASP ASP A . n 
A 1 177 PHE 177 252 252 PHE PHE A . n 
A 1 178 GLY 178 253 253 GLY GLY A . n 
A 1 179 LEU 179 254 254 LEU LEU A . n 
A 1 180 LEU 180 255 255 LEU LEU A . n 
A 1 181 VAL 181 256 256 VAL VAL A . n 
A 1 182 GLU 182 257 257 GLU GLU A . n 
A 1 183 LEU 183 258 258 LEU LEU A . n 
A 1 184 GLY 184 259 259 GLY GLY A . n 
A 1 185 THR 185 260 ?   ?   ?   A . n 
A 1 186 ALA 186 261 ?   ?   ?   A . n 
A 1 187 GLY 187 262 ?   ?   ?   A . n 
A 1 188 ALA 188 263 ?   ?   ?   A . n 
A 1 189 GLY 189 264 ?   ?   ?   A . n 
A 1 190 GLU 190 265 265 GLU GLU A . n 
A 1 191 VAL 191 266 266 VAL VAL A . n 
A 1 192 GLN 192 267 267 GLN GLN A . n 
A 1 193 GLU 193 268 268 GLU GLU A . n 
A 1 194 GLY 194 269 269 GLY GLY A . n 
A 1 195 ASP 195 270 270 ASP ASP A . n 
A 1 196 PRO 196 271 271 PRO PRO A . n 
A 1 197 ARG 197 272 272 ARG ARG A . n 
A 1 198 TYR 198 273 273 TYR TYR A . n 
A 1 199 MET 199 274 274 MET MET A . n 
A 1 200 ALA 200 275 275 ALA ALA A . n 
A 1 201 PRO 201 276 276 PRO PRO A . n 
A 1 202 GLU 202 277 277 GLU GLU A . n 
A 1 203 LEU 203 278 278 LEU LEU A . n 
A 1 204 LEU 204 279 279 LEU LEU A . n 
A 1 205 GLN 205 280 280 GLN GLN A . n 
A 1 206 GLY 206 281 281 GLY GLY A . n 
A 1 207 SER 207 282 282 SER SER A . n 
A 1 208 TYR 208 283 283 TYR TYR A . n 
A 1 209 GLY 209 284 284 GLY GLY A . n 
A 1 210 THR 210 285 285 THR THR A . n 
A 1 211 ALA 211 286 286 ALA ALA A . n 
A 1 212 ALA 212 287 287 ALA ALA A . n 
A 1 213 ASP 213 288 288 ASP ASP A . n 
A 1 214 VAL 214 289 289 VAL VAL A . n 
A 1 215 PHE 215 290 290 PHE PHE A . n 
A 1 216 SER 216 291 291 SER SER A . n 
A 1 217 LEU 217 292 292 LEU LEU A . n 
A 1 218 GLY 218 293 293 GLY GLY A . n 
A 1 219 LEU 219 294 294 LEU LEU A . n 
A 1 220 THR 220 295 295 THR THR A . n 
A 1 221 ILE 221 296 296 ILE ILE A . n 
A 1 222 LEU 222 297 297 LEU LEU A . n 
A 1 223 GLU 223 298 298 GLU GLU A . n 
A 1 224 VAL 224 299 299 VAL VAL A . n 
A 1 225 ALA 225 300 300 ALA ALA A . n 
A 1 226 CYS 226 301 301 CYS CYS A . n 
A 1 227 ASN 227 302 302 ASN ASN A . n 
A 1 228 MET 228 303 303 MET MET A . n 
A 1 229 GLU 229 304 304 GLU GLU A . n 
A 1 230 LEU 230 305 305 LEU LEU A . n 
A 1 231 PRO 231 306 306 PRO PRO A . n 
A 1 232 HIS 232 307 307 HIS HIS A . n 
A 1 233 GLY 233 308 308 GLY GLY A . n 
A 1 234 GLY 234 309 309 GLY GLY A . n 
A 1 235 GLU 235 310 310 GLU GLU A . n 
A 1 236 GLY 236 311 311 GLY GLY A . n 
A 1 237 TRP 237 312 312 TRP TRP A . n 
A 1 238 GLN 238 313 313 GLN GLN A . n 
A 1 239 GLN 239 314 314 GLN GLN A . n 
A 1 240 LEU 240 315 315 LEU LEU A . n 
A 1 241 ARG 241 316 316 ARG ARG A . n 
A 1 242 GLN 242 317 317 GLN GLN A . n 
A 1 243 GLY 243 318 318 GLY GLY A . n 
A 1 244 TYR 244 319 319 TYR TYR A . n 
A 1 245 LEU 245 320 320 LEU LEU A . n 
A 1 246 PRO 246 321 321 PRO PRO A . n 
A 1 247 PRO 247 322 322 PRO PRO A . n 
A 1 248 GLU 248 323 323 GLU GLU A . n 
A 1 249 PHE 249 324 324 PHE PHE A . n 
A 1 250 THR 250 325 325 THR THR A . n 
A 1 251 ALA 251 326 326 ALA ALA A . n 
A 1 252 GLY 252 327 327 GLY GLY A . n 
A 1 253 LEU 253 328 328 LEU LEU A . n 
A 1 254 SER 254 329 329 SER SER A . n 
A 1 255 SER 255 330 330 SER SER A . n 
A 1 256 GLU 256 331 331 GLU GLU A . n 
A 1 257 LEU 257 332 332 LEU LEU A . n 
A 1 258 ARG 258 333 333 ARG ARG A . n 
A 1 259 SER 259 334 334 SER SER A . n 
A 1 260 VAL 260 335 335 VAL VAL A . n 
A 1 261 LEU 261 336 336 LEU LEU A . n 
A 1 262 VAL 262 337 337 VAL VAL A . n 
A 1 263 MET 263 338 338 MET MET A . n 
A 1 264 MET 264 339 339 MET MET A . n 
A 1 265 LEU 265 340 340 LEU LEU A . n 
A 1 266 GLU 266 341 341 GLU GLU A . n 
A 1 267 PRO 267 342 342 PRO PRO A . n 
A 1 268 ASP 268 343 343 ASP ASP A . n 
A 1 269 PRO 269 344 344 PRO PRO A . n 
A 1 270 LYS 270 345 345 LYS LYS A . n 
A 1 271 LEU 271 346 346 LEU LEU A . n 
A 1 272 ARG 272 347 347 ARG ARG A . n 
A 1 273 ALA 273 348 348 ALA ALA A . n 
A 1 274 THR 274 349 349 THR THR A . n 
A 1 275 ALA 275 350 350 ALA ALA A . n 
A 1 276 GLU 276 351 351 GLU GLU A . n 
A 1 277 ALA 277 352 352 ALA ALA A . n 
A 1 278 LEU 278 353 353 LEU LEU A . n 
A 1 279 LEU 279 354 354 LEU LEU A . n 
A 1 280 ALA 280 355 355 ALA ALA A . n 
A 1 281 LEU 281 356 356 LEU LEU A . n 
A 1 282 PRO 282 357 357 PRO PRO A . n 
A 1 283 VAL 283 358 358 VAL VAL A . n 
A 1 284 LEU 284 359 359 LEU LEU A . n 
A 1 285 ARG 285 360 360 ARG ARG A . n 
A 1 286 GLN 286 361 361 GLN GLN A . n 
B 1 1   ALA 1   76  76  ALA ALA B . n 
B 1 2   LEU 2   77  77  LEU LEU B . n 
B 1 3   GLN 3   78  78  GLN GLN B . n 
B 1 4   PRO 4   79  79  PRO PRO B . n 
B 1 5   ARG 5   80  80  ARG ARG B . n 
B 1 6   ARG 6   81  81  ARG ARG B . n 
B 1 7   VAL 7   82  82  VAL VAL B . n 
B 1 8   SER 8   83  83  SER SER B . n 
B 1 9   PHE 9   84  84  PHE PHE B . n 
B 1 10  ARG 10  85  85  ARG ARG B . n 
B 1 11  GLY 11  86  86  GLY GLY B . n 
B 1 12  GLU 12  87  87  GLU GLU B . n 
B 1 13  ALA 13  88  88  ALA ALA B . n 
B 1 14  SER 14  89  89  SER SER B . n 
B 1 15  GLU 15  90  90  GLU GLU B . n 
B 1 16  THR 16  91  91  THR THR B . n 
B 1 17  LEU 17  92  92  LEU LEU B . n 
B 1 18  GLN 18  93  93  GLN GLN B . n 
B 1 19  SER 19  94  94  SER SER B . n 
B 1 20  PRO 20  95  95  PRO PRO B . n 
B 1 21  GLY 21  96  96  GLY GLY B . n 
B 1 22  TYR 22  97  97  TYR TYR B . n 
B 1 23  ASP 23  98  98  ASP ASP B . n 
B 1 24  PRO 24  99  99  PRO PRO B . n 
B 1 25  SER 25  100 100 SER SER B . n 
B 1 26  ARG 26  101 101 ARG ARG B . n 
B 1 27  PRO 27  102 102 PRO PRO B . n 
B 1 28  GLU 28  103 103 GLU GLU B . n 
B 1 29  SER 29  104 104 SER SER B . n 
B 1 30  PHE 30  105 105 PHE PHE B . n 
B 1 31  PHE 31  106 106 PHE PHE B . n 
B 1 32  GLN 32  107 107 GLN GLN B . n 
B 1 33  GLN 33  108 108 GLN GLN B . n 
B 1 34  SER 34  109 109 SER SER B . n 
B 1 35  PHE 35  110 110 PHE PHE B . n 
B 1 36  GLN 36  111 111 GLN GLN B . n 
B 1 37  ARG 37  112 112 ARG ARG B . n 
B 1 38  LEU 38  113 113 LEU LEU B . n 
B 1 39  SER 39  114 114 SER SER B . n 
B 1 40  ARG 40  115 115 ARG ARG B . n 
B 1 41  LEU 41  116 116 LEU LEU B . n 
B 1 42  GLY 42  117 117 GLY GLY B . n 
B 1 43  HIS 43  118 118 HIS HIS B . n 
B 1 44  GLY 44  119 119 GLY GLY B . n 
B 1 45  SER 45  120 120 SER SER B . n 
B 1 46  TYR 46  121 121 TYR TYR B . n 
B 1 47  GLY 47  122 122 GLY GLY B . n 
B 1 48  GLU 48  123 123 GLU GLU B . n 
B 1 49  VAL 49  124 124 VAL VAL B . n 
B 1 50  PHE 50  125 125 PHE PHE B . n 
B 1 51  LYS 51  126 126 LYS LYS B . n 
B 1 52  VAL 52  127 127 VAL VAL B . n 
B 1 53  ARG 53  128 128 ARG ARG B . n 
B 1 54  SER 54  129 129 SER SER B . n 
B 1 55  LYS 55  130 130 LYS LYS B . n 
B 1 56  GLU 56  131 131 GLU GLU B . n 
B 1 57  ASP 57  132 132 ASP ASP B . n 
B 1 58  GLY 58  133 133 GLY GLY B . n 
B 1 59  ARG 59  134 134 ARG ARG B . n 
B 1 60  LEU 60  135 135 LEU LEU B . n 
B 1 61  TYR 61  136 136 TYR TYR B . n 
B 1 62  ALA 62  137 137 ALA ALA B . n 
B 1 63  VAL 63  138 138 VAL VAL B . n 
B 1 64  LYS 64  139 139 LYS LYS B . n 
B 1 65  ARG 65  140 140 ARG ARG B . n 
B 1 66  SER 66  141 141 SER SER B . n 
B 1 67  MET 67  142 142 MET MET B . n 
B 1 68  SER 68  143 143 SER SER B . n 
B 1 69  PRO 69  144 144 PRO PRO B . n 
B 1 70  PHE 70  145 145 PHE PHE B . n 
B 1 71  ARG 71  146 146 ARG ARG B . n 
B 1 72  GLY 72  147 147 GLY GLY B . n 
B 1 73  PRO 73  148 148 PRO PRO B . n 
B 1 74  LYS 74  149 149 LYS LYS B . n 
B 1 75  ASP 75  150 150 ASP ASP B . n 
B 1 76  ARG 76  151 151 ARG ARG B . n 
B 1 77  ALA 77  152 152 ALA ALA B . n 
B 1 78  ARG 78  153 153 ARG ARG B . n 
B 1 79  LYS 79  154 154 LYS LYS B . n 
B 1 80  LEU 80  155 155 LEU LEU B . n 
B 1 81  ALA 81  156 156 ALA ALA B . n 
B 1 82  GLU 82  157 157 GLU GLU B . n 
B 1 83  VAL 83  158 158 VAL VAL B . n 
B 1 84  GLY 84  159 159 GLY GLY B . n 
B 1 85  SER 85  160 160 SER SER B . n 
B 1 86  HIS 86  161 161 HIS HIS B . n 
B 1 87  GLU 87  162 162 GLU GLU B . n 
B 1 88  LYS 88  163 163 LYS LYS B . n 
B 1 89  VAL 89  164 164 VAL VAL B . n 
B 1 90  GLY 90  165 165 GLY GLY B . n 
B 1 91  GLN 91  166 166 GLN GLN B . n 
B 1 92  HIS 92  167 167 HIS HIS B . n 
B 1 93  PRO 93  168 168 PRO PRO B . n 
B 1 94  CYS 94  169 169 CYS CYS B . n 
B 1 95  CYS 95  170 170 CYS CYS B . n 
B 1 96  VAL 96  171 171 VAL VAL B . n 
B 1 97  ARG 97  172 172 ARG ARG B . n 
B 1 98  LEU 98  173 173 LEU LEU B . n 
B 1 99  GLU 99  174 174 GLU GLU B . n 
B 1 100 GLN 100 175 175 GLN GLN B . n 
B 1 101 ALA 101 176 176 ALA ALA B . n 
B 1 102 TRP 102 177 177 TRP TRP B . n 
B 1 103 GLU 103 178 178 GLU GLU B . n 
B 1 104 GLU 104 179 179 GLU GLU B . n 
B 1 105 GLY 105 180 180 GLY GLY B . n 
B 1 106 GLY 106 181 181 GLY GLY B . n 
B 1 107 ILE 107 182 182 ILE ILE B . n 
B 1 108 LEU 108 183 183 LEU LEU B . n 
B 1 109 TYR 109 184 184 TYR TYR B . n 
B 1 110 LEU 110 185 185 LEU LEU B . n 
B 1 111 GLN 111 186 186 GLN GLN B . n 
B 1 112 THR 112 187 187 THR THR B . n 
B 1 113 GLU 113 188 188 GLU GLU B . n 
B 1 114 LEU 114 189 189 LEU LEU B . n 
B 1 115 CYS 115 190 190 CYS CYS B . n 
B 1 116 GLY 116 191 191 GLY GLY B . n 
B 1 117 PRO 117 192 192 PRO PRO B . n 
B 1 118 SER 118 193 193 SER SER B . n 
B 1 119 LEU 119 194 194 LEU LEU B . n 
B 1 120 GLN 120 195 195 GLN GLN B . n 
B 1 121 GLN 121 196 196 GLN GLN B . n 
B 1 122 HIS 122 197 197 HIS HIS B . n 
B 1 123 CYS 123 198 198 CYS CYS B . n 
B 1 124 GLU 124 199 199 GLU GLU B . n 
B 1 125 ALA 125 200 200 ALA ALA B . n 
B 1 126 TRP 126 201 201 TRP TRP B . n 
B 1 127 GLY 127 202 202 GLY GLY B . n 
B 1 128 ALA 128 203 203 ALA ALA B . n 
B 1 129 SER 129 204 204 SER SER B . n 
B 1 130 LEU 130 205 205 LEU LEU B . n 
B 1 131 PRO 131 206 206 PRO PRO B . n 
B 1 132 GLU 132 207 207 GLU GLU B . n 
B 1 133 ALA 133 208 208 ALA ALA B . n 
B 1 134 GLN 134 209 209 GLN GLN B . n 
B 1 135 VAL 135 210 210 VAL VAL B . n 
B 1 136 TRP 136 211 211 TRP TRP B . n 
B 1 137 GLY 137 212 212 GLY GLY B . n 
B 1 138 TYR 138 213 213 TYR TYR B . n 
B 1 139 LEU 139 214 214 LEU LEU B . n 
B 1 140 ARG 140 215 215 ARG ARG B . n 
B 1 141 ASP 141 216 216 ASP ASP B . n 
B 1 142 THR 142 217 217 THR THR B . n 
B 1 143 LEU 143 218 218 LEU LEU B . n 
B 1 144 LEU 144 219 219 LEU LEU B . n 
B 1 145 ALA 145 220 220 ALA ALA B . n 
B 1 146 LEU 146 221 221 LEU LEU B . n 
B 1 147 ALA 147 222 222 ALA ALA B . n 
B 1 148 HIS 148 223 223 HIS HIS B . n 
B 1 149 LEU 149 224 224 LEU LEU B . n 
B 1 150 HIS 150 225 225 HIS HIS B . n 
B 1 151 SER 151 226 226 SER SER B . n 
B 1 152 GLN 152 227 227 GLN GLN B . n 
B 1 153 GLY 153 228 228 GLY GLY B . n 
B 1 154 LEU 154 229 229 LEU LEU B . n 
B 1 155 VAL 155 230 230 VAL VAL B . n 
B 1 156 HIS 156 231 231 HIS HIS B . n 
B 1 157 LEU 157 232 232 LEU LEU B . n 
B 1 158 ASP 158 233 233 ASP ASP B . n 
B 1 159 VAL 159 234 234 VAL VAL B . n 
B 1 160 LYS 160 235 235 LYS LYS B . n 
B 1 161 PRO 161 236 236 PRO PRO B . n 
B 1 162 ALA 162 237 237 ALA ALA B . n 
B 1 163 ASN 163 238 238 ASN ASN B . n 
B 1 164 ILE 164 239 239 ILE ILE B . n 
B 1 165 PHE 165 240 240 PHE PHE B . n 
B 1 166 LEU 166 241 241 LEU LEU B . n 
B 1 167 GLY 167 242 242 GLY GLY B . n 
B 1 168 PRO 168 243 243 PRO PRO B . n 
B 1 169 ARG 169 244 244 ARG ARG B . n 
B 1 170 GLY 170 245 245 GLY GLY B . n 
B 1 171 ARG 171 246 246 ARG ARG B . n 
B 1 172 CYS 172 247 247 CYS CYS B . n 
B 1 173 LYS 173 248 248 LYS LYS B . n 
B 1 174 LEU 174 249 249 LEU LEU B . n 
B 1 175 GLY 175 250 250 GLY GLY B . n 
B 1 176 ASP 176 251 251 ASP ASP B . n 
B 1 177 PHE 177 252 252 PHE PHE B . n 
B 1 178 GLY 178 253 253 GLY GLY B . n 
B 1 179 LEU 179 254 254 LEU LEU B . n 
B 1 180 LEU 180 255 255 LEU LEU B . n 
B 1 181 VAL 181 256 256 VAL VAL B . n 
B 1 182 GLU 182 257 257 GLU GLU B . n 
B 1 183 LEU 183 258 258 LEU LEU B . n 
B 1 184 GLY 184 259 259 GLY GLY B . n 
B 1 185 THR 185 260 260 THR THR B . n 
B 1 186 ALA 186 261 ?   ?   ?   B . n 
B 1 187 GLY 187 262 ?   ?   ?   B . n 
B 1 188 ALA 188 263 ?   ?   ?   B . n 
B 1 189 GLY 189 264 ?   ?   ?   B . n 
B 1 190 GLU 190 265 265 GLU GLU B . n 
B 1 191 VAL 191 266 266 VAL VAL B . n 
B 1 192 GLN 192 267 267 GLN GLN B . n 
B 1 193 GLU 193 268 268 GLU GLU B . n 
B 1 194 GLY 194 269 269 GLY GLY B . n 
B 1 195 ASP 195 270 270 ASP ASP B . n 
B 1 196 PRO 196 271 271 PRO PRO B . n 
B 1 197 ARG 197 272 272 ARG ARG B . n 
B 1 198 TYR 198 273 273 TYR TYR B . n 
B 1 199 MET 199 274 274 MET MET B . n 
B 1 200 ALA 200 275 275 ALA ALA B . n 
B 1 201 PRO 201 276 276 PRO PRO B . n 
B 1 202 GLU 202 277 277 GLU GLU B . n 
B 1 203 LEU 203 278 278 LEU LEU B . n 
B 1 204 LEU 204 279 279 LEU LEU B . n 
B 1 205 GLN 205 280 280 GLN GLN B . n 
B 1 206 GLY 206 281 281 GLY GLY B . n 
B 1 207 SER 207 282 282 SER SER B . n 
B 1 208 TYR 208 283 283 TYR TYR B . n 
B 1 209 GLY 209 284 284 GLY GLY B . n 
B 1 210 THR 210 285 285 THR THR B . n 
B 1 211 ALA 211 286 286 ALA ALA B . n 
B 1 212 ALA 212 287 287 ALA ALA B . n 
B 1 213 ASP 213 288 288 ASP ASP B . n 
B 1 214 VAL 214 289 289 VAL VAL B . n 
B 1 215 PHE 215 290 290 PHE PHE B . n 
B 1 216 SER 216 291 291 SER SER B . n 
B 1 217 LEU 217 292 292 LEU LEU B . n 
B 1 218 GLY 218 293 293 GLY GLY B . n 
B 1 219 LEU 219 294 294 LEU LEU B . n 
B 1 220 THR 220 295 295 THR THR B . n 
B 1 221 ILE 221 296 296 ILE ILE B . n 
B 1 222 LEU 222 297 297 LEU LEU B . n 
B 1 223 GLU 223 298 298 GLU GLU B . n 
B 1 224 VAL 224 299 299 VAL VAL B . n 
B 1 225 ALA 225 300 300 ALA ALA B . n 
B 1 226 CYS 226 301 301 CYS CYS B . n 
B 1 227 ASN 227 302 302 ASN ASN B . n 
B 1 228 MET 228 303 303 MET MET B . n 
B 1 229 GLU 229 304 304 GLU GLU B . n 
B 1 230 LEU 230 305 305 LEU LEU B . n 
B 1 231 PRO 231 306 306 PRO PRO B . n 
B 1 232 HIS 232 307 307 HIS HIS B . n 
B 1 233 GLY 233 308 308 GLY GLY B . n 
B 1 234 GLY 234 309 309 GLY GLY B . n 
B 1 235 GLU 235 310 310 GLU GLU B . n 
B 1 236 GLY 236 311 311 GLY GLY B . n 
B 1 237 TRP 237 312 312 TRP TRP B . n 
B 1 238 GLN 238 313 313 GLN GLN B . n 
B 1 239 GLN 239 314 314 GLN GLN B . n 
B 1 240 LEU 240 315 315 LEU LEU B . n 
B 1 241 ARG 241 316 316 ARG ARG B . n 
B 1 242 GLN 242 317 317 GLN GLN B . n 
B 1 243 GLY 243 318 318 GLY GLY B . n 
B 1 244 TYR 244 319 319 TYR TYR B . n 
B 1 245 LEU 245 320 320 LEU LEU B . n 
B 1 246 PRO 246 321 321 PRO PRO B . n 
B 1 247 PRO 247 322 322 PRO PRO B . n 
B 1 248 GLU 248 323 323 GLU GLU B . n 
B 1 249 PHE 249 324 324 PHE PHE B . n 
B 1 250 THR 250 325 325 THR THR B . n 
B 1 251 ALA 251 326 326 ALA ALA B . n 
B 1 252 GLY 252 327 327 GLY GLY B . n 
B 1 253 LEU 253 328 328 LEU LEU B . n 
B 1 254 SER 254 329 329 SER SER B . n 
B 1 255 SER 255 330 330 SER SER B . n 
B 1 256 GLU 256 331 331 GLU GLU B . n 
B 1 257 LEU 257 332 332 LEU LEU B . n 
B 1 258 ARG 258 333 333 ARG ARG B . n 
B 1 259 SER 259 334 334 SER SER B . n 
B 1 260 VAL 260 335 335 VAL VAL B . n 
B 1 261 LEU 261 336 336 LEU LEU B . n 
B 1 262 VAL 262 337 337 VAL VAL B . n 
B 1 263 MET 263 338 338 MET MET B . n 
B 1 264 MET 264 339 339 MET MET B . n 
B 1 265 LEU 265 340 340 LEU LEU B . n 
B 1 266 GLU 266 341 341 GLU GLU B . n 
B 1 267 PRO 267 342 342 PRO PRO B . n 
B 1 268 ASP 268 343 343 ASP ASP B . n 
B 1 269 PRO 269 344 344 PRO PRO B . n 
B 1 270 LYS 270 345 345 LYS LYS B . n 
B 1 271 LEU 271 346 346 LEU LEU B . n 
B 1 272 ARG 272 347 347 ARG ARG B . n 
B 1 273 ALA 273 348 348 ALA ALA B . n 
B 1 274 THR 274 349 349 THR THR B . n 
B 1 275 ALA 275 350 350 ALA ALA B . n 
B 1 276 GLU 276 351 351 GLU GLU B . n 
B 1 277 ALA 277 352 352 ALA ALA B . n 
B 1 278 LEU 278 353 353 LEU LEU B . n 
B 1 279 LEU 279 354 354 LEU LEU B . n 
B 1 280 ALA 280 355 355 ALA ALA B . n 
B 1 281 LEU 281 356 356 LEU LEU B . n 
B 1 282 PRO 282 357 357 PRO PRO B . n 
B 1 283 VAL 283 358 358 VAL VAL B . n 
B 1 284 LEU 284 359 359 LEU LEU B . n 
B 1 285 ARG 285 360 360 ARG ARG B . n 
B 1 286 GLN 286 361 361 GLN GLN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EJU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EJU 
_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 A1EJU 1  401 404 A1EJU L0R A . 
D 3 SO4   1  402 2   SO4   SO4 A . 
E 3 SO4   1  403 4   SO4   SO4 A . 
F 3 SO4   1  404 6   SO4   SO4 A . 
G 2 A1EJU 1  401 401 A1EJU L0R B . 
H 3 SO4   1  402 1   SO4   SO4 B . 
I 3 SO4   1  403 3   SO4   SO4 B . 
J 3 SO4   1  404 5   SO4   SO4 B . 
K 3 SO4   1  405 7   SO4   SO4 B . 
L 4 HOH   1  501 29  HOH   HOH A . 
L 4 HOH   2  502 50  HOH   HOH A . 
L 4 HOH   3  503 98  HOH   HOH A . 
L 4 HOH   4  504 35  HOH   HOH A . 
L 4 HOH   5  505 102 HOH   HOH A . 
L 4 HOH   6  506 1   HOH   HOH A . 
L 4 HOH   7  507 21  HOH   HOH A . 
L 4 HOH   8  508 44  HOH   HOH A . 
L 4 HOH   9  509 79  HOH   HOH A . 
L 4 HOH   10 510 23  HOH   HOH A . 
L 4 HOH   11 511 20  HOH   HOH A . 
L 4 HOH   12 512 4   HOH   HOH A . 
L 4 HOH   13 513 108 HOH   HOH A . 
L 4 HOH   14 514 17  HOH   HOH A . 
L 4 HOH   15 515 65  HOH   HOH A . 
L 4 HOH   16 516 10  HOH   HOH A . 
L 4 HOH   17 517 101 HOH   HOH A . 
L 4 HOH   18 518 38  HOH   HOH A . 
L 4 HOH   19 519 25  HOH   HOH A . 
L 4 HOH   20 520 22  HOH   HOH A . 
L 4 HOH   21 521 8   HOH   HOH A . 
L 4 HOH   22 522 26  HOH   HOH A . 
L 4 HOH   23 523 100 HOH   HOH A . 
L 4 HOH   24 524 5   HOH   HOH A . 
L 4 HOH   25 525 49  HOH   HOH A . 
L 4 HOH   26 526 84  HOH   HOH A . 
L 4 HOH   27 527 63  HOH   HOH A . 
L 4 HOH   28 528 32  HOH   HOH A . 
L 4 HOH   29 529 53  HOH   HOH A . 
L 4 HOH   30 530 75  HOH   HOH A . 
L 4 HOH   31 531 87  HOH   HOH A . 
L 4 HOH   32 532 3   HOH   HOH A . 
L 4 HOH   33 533 86  HOH   HOH A . 
L 4 HOH   34 534 83  HOH   HOH A . 
L 4 HOH   35 535 42  HOH   HOH A . 
L 4 HOH   36 536 7   HOH   HOH A . 
L 4 HOH   37 537 14  HOH   HOH A . 
L 4 HOH   38 538 59  HOH   HOH A . 
L 4 HOH   39 539 103 HOH   HOH A . 
L 4 HOH   40 540 24  HOH   HOH A . 
L 4 HOH   41 541 13  HOH   HOH A . 
L 4 HOH   42 542 66  HOH   HOH A . 
L 4 HOH   43 543 64  HOH   HOH A . 
L 4 HOH   44 544 99  HOH   HOH A . 
L 4 HOH   45 545 48  HOH   HOH A . 
L 4 HOH   46 546 91  HOH   HOH A . 
L 4 HOH   47 547 36  HOH   HOH A . 
L 4 HOH   48 548 93  HOH   HOH A . 
M 4 HOH   1  501 80  HOH   HOH B . 
M 4 HOH   2  502 78  HOH   HOH B . 
M 4 HOH   3  503 107 HOH   HOH B . 
M 4 HOH   4  504 85  HOH   HOH B . 
M 4 HOH   5  505 89  HOH   HOH B . 
M 4 HOH   6  506 104 HOH   HOH B . 
M 4 HOH   7  507 88  HOH   HOH B . 
M 4 HOH   8  508 2   HOH   HOH B . 
M 4 HOH   9  509 54  HOH   HOH B . 
M 4 HOH   10 510 97  HOH   HOH B . 
M 4 HOH   11 511 68  HOH   HOH B . 
M 4 HOH   12 512 58  HOH   HOH B . 
M 4 HOH   13 513 39  HOH   HOH B . 
M 4 HOH   14 514 43  HOH   HOH B . 
M 4 HOH   15 515 71  HOH   HOH B . 
M 4 HOH   16 516 19  HOH   HOH B . 
M 4 HOH   17 517 16  HOH   HOH B . 
M 4 HOH   18 518 105 HOH   HOH B . 
M 4 HOH   19 519 6   HOH   HOH B . 
M 4 HOH   20 520 61  HOH   HOH B . 
M 4 HOH   21 521 73  HOH   HOH B . 
M 4 HOH   22 522 69  HOH   HOH B . 
M 4 HOH   23 523 27  HOH   HOH B . 
M 4 HOH   24 524 11  HOH   HOH B . 
M 4 HOH   25 525 94  HOH   HOH B . 
M 4 HOH   26 526 9   HOH   HOH B . 
M 4 HOH   27 527 28  HOH   HOH B . 
M 4 HOH   28 528 12  HOH   HOH B . 
M 4 HOH   29 529 34  HOH   HOH B . 
M 4 HOH   30 530 72  HOH   HOH B . 
M 4 HOH   31 531 82  HOH   HOH B . 
M 4 HOH   32 532 74  HOH   HOH B . 
M 4 HOH   33 533 47  HOH   HOH B . 
M 4 HOH   34 534 90  HOH   HOH B . 
M 4 HOH   35 535 70  HOH   HOH B . 
M 4 HOH   36 536 40  HOH   HOH B . 
M 4 HOH   37 537 52  HOH   HOH B . 
M 4 HOH   38 538 33  HOH   HOH B . 
M 4 HOH   39 539 67  HOH   HOH B . 
M 4 HOH   40 540 15  HOH   HOH B . 
M 4 HOH   41 541 18  HOH   HOH B . 
M 4 HOH   42 542 57  HOH   HOH B . 
M 4 HOH   43 543 92  HOH   HOH B . 
M 4 HOH   44 544 62  HOH   HOH B . 
M 4 HOH   45 545 30  HOH   HOH B . 
M 4 HOH   46 546 56  HOH   HOH B . 
M 4 HOH   47 547 46  HOH   HOH B . 
M 4 HOH   48 548 81  HOH   HOH B . 
M 4 HOH   49 549 96  HOH   HOH B . 
M 4 HOH   50 550 55  HOH   HOH B . 
M 4 HOH   51 551 45  HOH   HOH B . 
M 4 HOH   52 552 37  HOH   HOH B . 
M 4 HOH   53 553 41  HOH   HOH B . 
M 4 HOH   54 554 51  HOH   HOH B . 
M 4 HOH   55 555 31  HOH   HOH B . 
M 4 HOH   56 556 95  HOH   HOH B . 
M 4 HOH   57 557 76  HOH   HOH B . 
M 4 HOH   58 558 77  HOH   HOH B . 
M 4 HOH   59 559 60  HOH   HOH B . 
M 4 HOH   60 560 106 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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.97 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LGN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.450 
_cell.length_a_esd                 ? 
_cell.length_b                     110.405 
_cell.length_b_esd                 ? 
_cell.length_c                     72.019 
_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                         9LGN 
_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                   9LGN 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.45 
_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            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2023-04-25 
_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                                       9LGN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.03 
_reflns.d_resolution_low                               46.48 
_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                                     27917 
_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                           88.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.032 
_reflns_shell.d_res_low                                     2.283 
_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                             1421 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.399 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                                 9LGN 
_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                            2.03 
_refine.ls_d_res_low                             46.48 
_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                     27917 
_refine.ls_number_reflns_R_free                  1361 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    59.54 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1961 
_refine.ls_R_factor_R_free                       0.2412 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1937 
_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          SAD 
_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                 36.22 
_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                            0.22 
_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                       2.03 
_refine_hist.d_res_low                        46.48 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               4578 
_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        4387 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         83 
_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' ? 0.002  ? 4608 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.508  ? 6248 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.010 ? 1760 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 647  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 823  ? 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' 2.03 2.10 . . 3   187  20    . . . . 0.1413 . . . . . . . . . . . 0.1413 
'X-RAY DIFFRACTION' 2.10 2.19 . . 26  498  20    . . . . 0.3283 . . . . . . . . . . . 0.4379 
'X-RAY DIFFRACTION' 2.19 2.29 . . 39  672  20    . . . . 0.3012 . . . . . . . . . . . 0.3963 
'X-RAY DIFFRACTION' 2.29 2.41 . . 53  1059 24.00 . . . . 0.2918 . . . . . . . . . . . 0.3118 
'X-RAY DIFFRACTION' 2.41 2.56 . . 121 2489 56.00 . . . . 0.3144 . . . . . . . . . . . 0.3488 
'X-RAY DIFFRACTION' 2.56 2.76 . . 214 4075 91.00 . . . . 0.2930 . . . . . . . . . . . 0.3262 
'X-RAY DIFFRACTION' 2.76 3.03 . . 210 4416 99.00 . . . . 0.2688 . . . . . . . . . . . 0.2999 
'X-RAY DIFFRACTION' 3.03 3.47 . . 225 4455 99.00 . . . . 0.1970 . . . . . . . . . . . 0.2320 
'X-RAY DIFFRACTION' 3.47 4.37 . . 228 4357 98.00 . . . . 0.1570 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 4.37 10   . . 242 4348 96.00 . . . . 0.1599 . . . . . . . . . . . 0.2200 
# 
_struct.entry_id                     9LGN 
_struct.title                        
'Crystal structure of human PKMYT1 protein kinase domain with Naphthyridinone Inhibitor compound 40' 
_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        9LGN 
_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 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    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   
;LQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLA
EVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDVKP
ANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLR
QGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQ
;
_struct_ref.pdbx_align_begin           77 
# 
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 9LGN A 2 ? 286 ? Q99640 77 ? 361 ? 77 361 
2 1 9LGN B 2 ? 286 ? Q99640 77 ? 361 ? 77 361 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9LGN ALA A 1 ? UNP Q99640 ? ? 'expression tag' 76 1 
2 9LGN ALA B 1 ? UNP Q99640 ? ? 'expression tag' 76 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 230   ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  13820 ? 
2 'ABSA (A^2)' 220   ? 
2 MORE         -16   ? 
2 'SSA (A^2)'  13790 ? 
# 
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,L   
2 1 B,G,H,I,J,K,M 
# 
_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 29  ? SER A 34  ? SER A 104 SER A 109 1 ? 6  
HELX_P HELX_P2  AA2 GLY A 72  ? GLY A 90  ? GLY A 147 GLY A 165 1 ? 19 
HELX_P HELX_P3  AA3 SER A 118 ? GLY A 127 ? SER A 193 GLY A 202 1 ? 10 
HELX_P HELX_P4  AA4 PRO A 131 ? SER A 151 ? PRO A 206 SER A 226 1 ? 21 
HELX_P HELX_P5  AA5 LYS A 160 ? ALA A 162 ? LYS A 235 ALA A 237 5 ? 3  
HELX_P HELX_P6  AA6 PRO A 168 ? GLY A 170 ? PRO A 243 GLY A 245 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 195 ? MET A 199 ? ASP A 270 MET A 274 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 200 ? LEU A 204 ? ALA A 275 LEU A 279 5 ? 5  
HELX_P HELX_P9  AA9 THR A 210 ? ASN A 227 ? THR A 285 ASN A 302 1 ? 18 
HELX_P HELX_P10 AB1 GLY A 233 ? LEU A 240 ? GLY A 308 LEU A 315 1 ? 8  
HELX_P HELX_P11 AB2 PRO A 246 ? ALA A 251 ? PRO A 321 ALA A 326 1 ? 6  
HELX_P HELX_P12 AB3 SER A 254 ? LEU A 265 ? SER A 329 LEU A 340 1 ? 12 
HELX_P HELX_P13 AB4 THR A 274 ? ALA A 280 ? THR A 349 ALA A 355 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 281 ? ARG A 285 ? LEU A 356 ARG A 360 5 ? 5  
HELX_P HELX_P15 AB6 SER B 29  ? SER B 34  ? SER B 104 SER B 109 1 ? 6  
HELX_P HELX_P16 AB7 GLY B 72  ? GLY B 90  ? GLY B 147 GLY B 165 1 ? 19 
HELX_P HELX_P17 AB8 SER B 118 ? GLY B 127 ? SER B 193 GLY B 202 1 ? 10 
HELX_P HELX_P18 AB9 PRO B 131 ? SER B 151 ? PRO B 206 SER B 226 1 ? 21 
HELX_P HELX_P19 AC1 LYS B 160 ? ALA B 162 ? LYS B 235 ALA B 237 5 ? 3  
HELX_P HELX_P20 AC2 PRO B 168 ? GLY B 170 ? PRO B 243 GLY B 245 5 ? 3  
HELX_P HELX_P21 AC3 ASP B 195 ? MET B 199 ? ASP B 270 MET B 274 5 ? 5  
HELX_P HELX_P22 AC4 ALA B 200 ? GLN B 205 ? ALA B 275 GLN B 280 1 ? 6  
HELX_P HELX_P23 AC5 THR B 210 ? ASN B 227 ? THR B 285 ASN B 302 1 ? 18 
HELX_P HELX_P24 AC6 GLY B 233 ? LEU B 240 ? GLY B 308 LEU B 315 1 ? 8  
HELX_P HELX_P25 AC7 SER B 254 ? LEU B 265 ? SER B 329 LEU B 340 1 ? 12 
HELX_P HELX_P26 AC8 THR B 274 ? ALA B 280 ? THR B 349 ALA B 355 1 ? 7  
HELX_P HELX_P27 AC9 LEU B 281 ? ARG B 285 ? LEU B 356 ARG B 360 5 ? 5  
# 
_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 5   ? ARG A 6   ? ARG A 80  ARG A 81  
AA1 2 LEU A 98  ? GLU A 104 ? LEU A 173 GLU A 179 
AA1 3 ILE A 107 ? GLU A 113 ? ILE A 182 GLU A 188 
AA1 4 LEU A 60  ? ARG A 65  ? LEU A 135 ARG A 140 
AA1 5 GLY A 47  ? SER A 54  ? GLY A 122 SER A 129 
AA1 6 PHE A 35  ? GLY A 44  ? PHE A 110 GLY A 119 
AA2 1 LEU A 154 ? VAL A 155 ? LEU A 229 VAL A 230 
AA2 2 VAL A 181 ? GLU A 182 ? VAL A 256 GLU A 257 
AA3 1 ILE A 164 ? LEU A 166 ? ILE A 239 LEU A 241 
AA3 2 CYS A 172 ? LEU A 174 ? CYS A 247 LEU A 249 
AA4 1 ARG B 5   ? ARG B 6   ? ARG B 80  ARG B 81  
AA4 2 LEU B 98  ? GLU B 104 ? LEU B 173 GLU B 179 
AA4 3 ILE B 107 ? GLU B 113 ? ILE B 182 GLU B 188 
AA4 4 LEU B 60  ? SER B 66  ? LEU B 135 SER B 141 
AA4 5 GLY B 47  ? SER B 54  ? GLY B 122 SER B 129 
AA4 6 PHE B 35  ? HIS B 43  ? PHE B 110 HIS B 118 
AA5 1 LEU B 154 ? VAL B 155 ? LEU B 229 VAL B 230 
AA5 2 VAL B 181 ? GLU B 182 ? VAL B 256 GLU B 257 
AA6 1 ILE B 164 ? LEU B 166 ? ILE B 239 LEU B 241 
AA6 2 CYS B 172 ? LEU B 174 ? 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 5   ? N ARG A 80  O GLU A 103 ? O GLU A 178 
AA1 2 3 N TRP A 102 ? N TRP A 177 O TYR A 109 ? O TYR A 184 
AA1 3 4 O THR A 112 ? O THR A 187 N ALA A 62  ? N ALA A 137 
AA1 4 5 O VAL A 63  ? O VAL A 138 N PHE A 50  ? N PHE A 125 
AA1 5 6 O LYS A 51  ? O LYS A 126 N SER A 39  ? N SER A 114 
AA2 1 2 N VAL A 155 ? N VAL A 230 O VAL A 181 ? O VAL A 256 
AA3 1 2 N PHE A 165 ? N PHE A 240 O LYS A 173 ? O LYS A 248 
AA4 1 2 N ARG B 5   ? N ARG B 80  O GLU B 103 ? O GLU B 178 
AA4 2 3 N TRP B 102 ? N TRP B 177 O TYR B 109 ? O TYR B 184 
AA4 3 4 O THR B 112 ? O THR B 187 N ALA B 62  ? N ALA B 137 
AA4 4 5 O ARG B 65  ? O ARG B 140 N GLU B 48  ? N GLU B 123 
AA4 5 6 O LYS B 51  ? O LYS B 126 N SER B 39  ? N SER B 114 
AA5 1 2 N VAL B 155 ? N VAL B 230 O VAL B 181 ? O VAL B 256 
AA6 1 2 N PHE B 165 ? N PHE B 240 O LYS B 173 ? O LYS B 248 
# 
_pdbx_entry_details.entry_id                   9LGN 
_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 LEU A 113 ? ? -125.47 -62.90 
2 1 ASP A 233 ? ? -156.26 48.99  
3 1 ASP A 251 ? ? 50.86   84.26  
4 1 LEU A 359 ? ? -108.26 40.97  
5 1 ASP B 233 ? ? -154.71 50.12  
6 1 ASP B 251 ? ? 54.01   79.86  
# 
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 -23.4574 -12.6838 38.0324 0.7081 ? -0.1946 ? 0.1433  ? 0.7290 ? -0.1111 ? 0.9545 ? 4.1589 ? 4.9262 
? -5.0847 ? 6.8079 ? -6.1507 ? 8.7798 ? -0.4269 ? 0.2557  ? 0.2463  ? -0.4288 ? 0.5138  ? 1.1715  ? 1.4891  ? -2.2240 ? -0.1292 ? 
2 'X-RAY DIFFRACTION' ? refined -10.2769 -21.0680 34.6616 0.9777 ? 0.0664  ? 0.3212  ? 0.1929 ? 0.1197  ? 0.8551 ? 4.5611 ? 
-0.6603 ? -3.3367 ? 4.9962 ? 2.3080  ? 6.7490 ? -0.1052 ? -0.6485 ? -0.3088 ? 1.2111  ? -0.4505 ? -0.3659 ? 1.6295  ? 0.6214  ? 
0.2807  ? 
3 'X-RAY DIFFRACTION' ? refined -12.6912 -9.8951  31.6748 0.2325 ? -0.0608 ? 0.0655  ? 0.2529 ? -0.0642 ? 0.3894 ? 1.1369 ? 
-0.5814 ? -2.4927 ? 4.0442 ? 1.3720  ? 5.5597 ? -0.1871 ? 0.2184  ? -0.2680 ? 0.2511  ? 0.0296  ? 0.3281  ? 0.9672  ? -0.2127 ? 
0.0549  ? 
4 'X-RAY DIFFRACTION' ? refined -1.3558  -13.0070 15.1888 0.3143 ? -0.0197 ? -0.0053 ? 0.2432 ? -0.0074 ? 0.2550 ? 2.4141 ? 0.6244 
? 1.1230  ? 5.2718 ? 1.3556  ? 4.3199 ? -0.0526 ? -0.0076 ? -0.3498 ? -0.4263 ? 0.2479  ? 0.1847  ? 0.4201  ? 0.1743  ? -0.0897 ? 
5 'X-RAY DIFFRACTION' ? refined 7.7845   -2.7323  20.7427 0.2415 ? 0.0214  ? -0.0066 ? 0.2760 ? -0.0030 ? 0.1869 ? 4.6862 ? 1.3847 
? 1.0376  ? 5.9973 ? 0.9365  ? 5.3316 ? -0.1662 ? -0.2322 ? 0.1591  ? 0.2477  ? 0.2833  ? -0.4084 ? -0.0050 ? 0.3706  ? -0.0766 ? 
6 'X-RAY DIFFRACTION' ? refined 18.3104  -8.7409  8.7853  0.6468 ? 0.2644  ? 0.1106  ? 0.9109 ? 0.0123  ? 0.8107 ? 0.5493 ? 1.3505 
? 0.9795  ? 4.2435 ? 3.0745  ? 2.5424 ? 0.1598  ? 0.0543  ? -0.7338 ? 0.5598  ? 0.3344  ? -1.8745 ? 0.4067  ? 0.7702  ? -0.4873 ? 
7 'X-RAY DIFFRACTION' ? refined 5.0015   -2.3818  4.9929  0.4520 ? -0.0549 ? 0.0404  ? 0.3414 ? -0.0248 ? 0.1237 ? 6.8761 ? 
-2.0641 ? 0.0585  ? 5.8742 ? 1.0550  ? 7.7763 ? -0.2303 ? 0.6534  ? -0.3931 ? -1.0345 ? 0.4093  ? 0.0750  ? 0.2881  ? 0.2073  ? 
-0.2955 ? 
8 'X-RAY DIFFRACTION' ? refined 15.7744  -39.0802 29.8207 0.1617 ? -0.0015 ? -0.0346 ? 0.2566 ? 0.0421  ? 0.5710 ? 2.7367 ? 1.2127 
? 2.3427  ? 4.4237 ? -1.7557 ? 7.1850 ? -0.1832 ? 0.1362  ? 0.6747  ? 0.2446  ? -0.2180 ? -0.2770 ? -0.6008 ? 0.6074  ? 0.2278  ? 
9 'X-RAY DIFFRACTION' ? refined -4.2427  -45.3466 11.3439 0.2618 ? 0.0213  ? 0.0147  ? 0.2492 ? 0.0079  ? 0.1380 ? 2.5805 ? 0.1704 
? 0.2011  ? 5.5754 ? -0.0248 ? 2.7407 ? -0.0788 ? 0.1485  ? -0.1059 ? -0.4159 ? 0.0397  ? 0.1395  ? 0.0561  ? -0.1619 ? 0.0829  ? 
# 
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 76 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 188 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 189 through 249 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 250 through 316 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 317 through 329 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 330 through 361 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 76 through 188 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 189 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 THR 260 ? A THR 185 
2 1 Y 1 A ALA 261 ? A ALA 186 
3 1 Y 1 A GLY 262 ? A GLY 187 
4 1 Y 1 A ALA 263 ? A ALA 188 
5 1 Y 1 A GLY 264 ? A GLY 189 
6 1 Y 1 B ALA 261 ? B ALA 186 
7 1 Y 1 B GLY 262 ? B GLY 187 
8 1 Y 1 B ALA 263 ? B ALA 188 
9 1 Y 1 B GLY 264 ? B GLY 189 
# 
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 
A1EJU C10  C N N 1   
A1EJU C11  C N N 2   
A1EJU C15  C Y N 3   
A1EJU C16  C Y N 4   
A1EJU C17  C Y N 5   
A1EJU C18  C Y N 6   
A1EJU C19  C Y N 7   
A1EJU C24  C N N 8   
A1EJU C1   C Y N 9   
A1EJU C14  C Y N 10  
A1EJU C2   C Y N 11  
A1EJU C3   C Y N 12  
A1EJU C4   C Y N 13  
A1EJU C5   C Y N 14  
A1EJU C6   C Y N 15  
A1EJU C9   C N N 16  
A1EJU F22  F N N 17  
A1EJU N12  N N N 18  
A1EJU N13  N Y N 19  
A1EJU N20  N Y N 20  
A1EJU N21  N Y N 21  
A1EJU N7   N N N 22  
A1EJU O23  O N N 23  
A1EJU O8   O N N 24  
A1EJU H1   H N N 25  
A1EJU H2   H N N 26  
A1EJU H3   H N N 27  
A1EJU H4   H N N 28  
A1EJU H5   H N N 29  
A1EJU H6   H N N 30  
A1EJU H7   H N N 31  
A1EJU H8   H N N 32  
A1EJU H9   H N N 33  
A1EJU H10  H N N 34  
A1EJU H11  H N N 35  
A1EJU H12  H N N 36  
ALA   N    N N N 37  
ALA   CA   C N S 38  
ALA   C    C N N 39  
ALA   O    O N N 40  
ALA   CB   C N N 41  
ALA   OXT  O N N 42  
ALA   H    H N N 43  
ALA   H2   H N N 44  
ALA   HA   H N N 45  
ALA   HB1  H N N 46  
ALA   HB2  H N N 47  
ALA   HB3  H N N 48  
ALA   HXT  H N N 49  
ARG   N    N N N 50  
ARG   CA   C N S 51  
ARG   C    C N N 52  
ARG   O    O N N 53  
ARG   CB   C N N 54  
ARG   CG   C N N 55  
ARG   CD   C N N 56  
ARG   NE   N N N 57  
ARG   CZ   C N N 58  
ARG   NH1  N N N 59  
ARG   NH2  N N N 60  
ARG   OXT  O N N 61  
ARG   H    H N N 62  
ARG   H2   H N N 63  
ARG   HA   H N N 64  
ARG   HB2  H N N 65  
ARG   HB3  H N N 66  
ARG   HG2  H N N 67  
ARG   HG3  H N N 68  
ARG   HD2  H N N 69  
ARG   HD3  H N N 70  
ARG   HE   H N N 71  
ARG   HH11 H N N 72  
ARG   HH12 H N N 73  
ARG   HH21 H N N 74  
ARG   HH22 H N N 75  
ARG   HXT  H N N 76  
ASN   N    N N N 77  
ASN   CA   C N S 78  
ASN   C    C N N 79  
ASN   O    O N N 80  
ASN   CB   C N N 81  
ASN   CG   C N N 82  
ASN   OD1  O N N 83  
ASN   ND2  N N N 84  
ASN   OXT  O N N 85  
ASN   H    H N N 86  
ASN   H2   H N N 87  
ASN   HA   H N N 88  
ASN   HB2  H N N 89  
ASN   HB3  H N N 90  
ASN   HD21 H N N 91  
ASN   HD22 H N N 92  
ASN   HXT  H N N 93  
ASP   N    N N N 94  
ASP   CA   C N S 95  
ASP   C    C N N 96  
ASP   O    O N N 97  
ASP   CB   C N N 98  
ASP   CG   C N N 99  
ASP   OD1  O N N 100 
ASP   OD2  O N N 101 
ASP   OXT  O N N 102 
ASP   H    H N N 103 
ASP   H2   H N N 104 
ASP   HA   H N N 105 
ASP   HB2  H N N 106 
ASP   HB3  H N N 107 
ASP   HD2  H N N 108 
ASP   HXT  H N N 109 
CYS   N    N N N 110 
CYS   CA   C N R 111 
CYS   C    C N N 112 
CYS   O    O N N 113 
CYS   CB   C N N 114 
CYS   SG   S N N 115 
CYS   OXT  O N N 116 
CYS   H    H N N 117 
CYS   H2   H N N 118 
CYS   HA   H N N 119 
CYS   HB2  H N N 120 
CYS   HB3  H N N 121 
CYS   HG   H N N 122 
CYS   HXT  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
SO4   S    S N N 340 
SO4   O1   O N N 341 
SO4   O2   O N N 342 
SO4   O3   O N N 343 
SO4   O4   O N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
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 
A1EJU O8  C11  doub N N 1   
A1EJU C11 N12  sing N N 2   
A1EJU C11 C10  sing N N 3   
A1EJU N20 C19  sing Y N 4   
A1EJU N20 N21  sing Y N 5   
A1EJU N7  C10  sing N N 6   
A1EJU C19 C2   doub Y N 7   
A1EJU N12 C15  sing N N 8   
A1EJU C10 C9   doub N N 9   
A1EJU O23 C24  sing N N 10  
A1EJU O23 C16  sing N N 11  
A1EJU N21 C3   doub Y N 12  
A1EJU C15 C16  doub Y N 13  
A1EJU C15 C14  sing Y N 14  
A1EJU C2  C3   sing Y N 15  
A1EJU C2  C1   sing Y N 16  
A1EJU C9  C14  sing N N 17  
A1EJU C9  C1   sing N N 18  
A1EJU C16 C17  sing Y N 19  
A1EJU C14 N13  doub Y N 20  
A1EJU C3  C4   sing Y N 21  
A1EJU C1  C6   doub Y N 22  
A1EJU C17 C18  doub Y N 23  
A1EJU N13 C18  sing Y N 24  
A1EJU C4  F22  sing N N 25  
A1EJU C4  C5   doub Y N 26  
A1EJU C6  C5   sing Y N 27  
A1EJU C17 H1   sing N N 28  
A1EJU C18 H2   sing N N 29  
A1EJU C19 H3   sing N N 30  
A1EJU C24 H4   sing N N 31  
A1EJU C24 H5   sing N N 32  
A1EJU C24 H6   sing N N 33  
A1EJU C5  H7   sing N N 34  
A1EJU C6  H8   sing N N 35  
A1EJU N12 H9   sing N N 36  
A1EJU N20 H10  sing N N 37  
A1EJU N7  H11  sing N N 38  
A1EJU N7  H12  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
SO4   S   O1   doub N N 329 
SO4   S   O2   doub N N 330 
SO4   S   O3   sing N N 331 
SO4   S   O4   sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9LGN 
_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]   0.020222 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007348 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009058 
_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]   0.014774 
_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   . ALA   A 1 1   ? -23.587 -14.361 51.840 1.00 89.19  ? 76  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 1   ? -22.233 -14.493 51.314 1.00 79.95  ? 76  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 1   ? -22.000 -13.509 50.170 1.00 77.98  ? 76  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 1   ? -22.939 -12.873 49.690 1.00 87.49  ? 76  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 1   ? -21.979 -15.923 50.852 1.00 70.24  ? 76  ALA   A CB  1 
ATOM   6    N N   . LEU   A 1 2   ? -20.746 -13.389 49.739 1.00 79.09  ? 77  LEU   A N   1 
ATOM   7    C CA  . LEU   A 1 2   ? -20.404 -12.484 48.650 1.00 77.10  ? 77  LEU   A CA  1 
ATOM   8    C C   . LEU   A 1 2   ? -21.051 -12.933 47.345 1.00 70.85  ? 77  LEU   A C   1 
ATOM   9    O O   . LEU   A 1 2   ? -21.328 -14.117 47.134 1.00 95.62  ? 77  LEU   A O   1 
ATOM   10   C CB  . LEU   A 1 2   ? -18.888 -12.402 48.473 1.00 62.58  ? 77  LEU   A CB  1 
ATOM   11   C CG  . LEU   A 1 2   ? -18.106 -11.777 49.627 1.00 71.00  ? 77  LEU   A CG  1 
ATOM   12   C CD1 . LEU   A 1 2   ? -16.634 -11.670 49.266 1.00 74.45  ? 77  LEU   A CD1 1 
ATOM   13   C CD2 . LEU   A 1 2   ? -18.681 -10.416 49.979 1.00 81.13  ? 77  LEU   A CD2 1 
ATOM   14   N N   . GLN   A 1 3   ? -21.289 -11.968 46.463 1.00 61.12  ? 78  GLN   A N   1 
ATOM   15   C CA  . GLN   A 1 3   ? -21.968 -12.201 45.201 1.00 69.45  ? 78  GLN   A CA  1 
ATOM   16   C C   . GLN   A 1 3   ? -21.260 -11.419 44.106 1.00 64.73  ? 78  GLN   A C   1 
ATOM   17   O O   . GLN   A 1 3   ? -20.663 -10.370 44.375 1.00 63.19  ? 78  GLN   A O   1 
ATOM   18   C CB  . GLN   A 1 3   ? -23.446 -11.783 45.276 1.00 70.34  ? 78  GLN   A CB  1 
ATOM   19   C CG  . GLN   A 1 3   ? -24.261 -12.586 46.282 1.00 82.15  ? 78  GLN   A CG  1 
ATOM   20   C CD  . GLN   A 1 3   ? -25.656 -12.032 46.486 1.00 111.54 ? 78  GLN   A CD  1 
ATOM   21   O OE1 . GLN   A 1 3   ? -26.197 -11.345 45.620 1.00 130.50 ? 78  GLN   A OE1 1 
ATOM   22   N NE2 . GLN   A 1 3   ? -26.246 -12.324 47.641 1.00 121.19 ? 78  GLN   A NE2 1 
ATOM   23   N N   . PRO   A 1 4   ? -21.302 -11.906 42.868 1.00 63.12  ? 79  PRO   A N   1 
ATOM   24   C CA  . PRO   A 1 4   ? -20.617 -11.215 41.773 1.00 55.58  ? 79  PRO   A CA  1 
ATOM   25   C C   . PRO   A 1 4   ? -21.345 -9.951  41.342 1.00 56.38  ? 79  PRO   A C   1 
ATOM   26   O O   . PRO   A 1 4   ? -22.513 -9.723  41.662 1.00 81.03  ? 79  PRO   A O   1 
ATOM   27   C CB  . PRO   A 1 4   ? -20.626 -12.253 40.646 1.00 55.26  ? 79  PRO   A CB  1 
ATOM   28   C CG  . PRO   A 1 4   ? -21.840 -13.053 40.911 1.00 57.90  ? 79  PRO   A CG  1 
ATOM   29   C CD  . PRO   A 1 4   ? -21.953 -13.144 42.408 1.00 62.62  ? 79  PRO   A CD  1 
ATOM   30   N N   . ARG   A 1 5   ? -20.620 -9.129  40.586 1.00 55.52  ? 80  ARG   A N   1 
ATOM   31   C CA  . ARG   A 1 5   ? -21.152 -7.893  40.025 1.00 52.87  ? 80  ARG   A CA  1 
ATOM   32   C C   . ARG   A 1 5   ? -20.673 -7.791  38.589 1.00 51.12  ? 80  ARG   A C   1 
ATOM   33   O O   . ARG   A 1 5   ? -19.466 -7.838  38.335 1.00 52.91  ? 80  ARG   A O   1 
ATOM   34   C CB  . ARG   A 1 5   ? -20.703 -6.672  40.831 1.00 52.09  ? 80  ARG   A CB  1 
ATOM   35   C CG  . ARG   A 1 5   ? -21.090 -5.343  40.199 1.00 68.08  ? 80  ARG   A CG  1 
ATOM   36   C CD  . ARG   A 1 5   ? -20.475 -4.168  40.944 1.00 65.66  ? 80  ARG   A CD  1 
ATOM   37   N NE  . ARG   A 1 5   ? -20.848 -2.886  40.356 1.00 70.58  ? 80  ARG   A NE  1 
ATOM   38   C CZ  . ARG   A 1 5   ? -20.169 -2.275  39.395 1.00 56.86  ? 80  ARG   A CZ  1 
ATOM   39   N NH1 . ARG   A 1 5   ? -19.074 -2.807  38.876 1.00 60.53  ? 80  ARG   A NH1 1 
ATOM   40   N NH2 . ARG   A 1 5   ? -20.597 -1.100  38.943 1.00 64.98  ? 80  ARG   A NH2 1 
ATOM   41   N N   . ARG   A 1 6   ? -21.608 -7.662  37.654 1.00 53.76  ? 81  ARG   A N   1 
ATOM   42   C CA  . ARG   A 1 6   ? -21.243 -7.617  36.246 1.00 52.83  ? 81  ARG   A CA  1 
ATOM   43   C C   . ARG   A 1 6   ? -20.533 -6.308  35.933 1.00 50.24  ? 81  ARG   A C   1 
ATOM   44   O O   . ARG   A 1 6   ? -20.992 -5.231  36.321 1.00 64.96  ? 81  ARG   A O   1 
ATOM   45   C CB  . ARG   A 1 6   ? -22.483 -7.768  35.367 1.00 68.52  ? 81  ARG   A CB  1 
ATOM   46   C CG  . ARG   A 1 6   ? -22.176 -7.853  33.879 1.00 71.40  ? 81  ARG   A CG  1 
ATOM   47   C CD  . ARG   A 1 6   ? -23.425 -8.170  33.059 1.00 101.43 ? 81  ARG   A CD  1 
ATOM   48   N NE  . ARG   A 1 6   ? -24.109 -6.975  32.573 1.00 122.85 ? 81  ARG   A NE  1 
ATOM   49   C CZ  . ARG   A 1 6   ? -25.187 -6.440  33.131 1.00 115.75 ? 81  ARG   A CZ  1 
ATOM   50   N NH1 . ARG   A 1 6   ? -25.735 -6.959  34.219 1.00 104.59 ? 81  ARG   A NH1 1 
ATOM   51   N NH2 . ARG   A 1 6   ? -25.735 -5.360  32.581 1.00 87.57  ? 81  ARG   A NH2 1 
ATOM   52   N N   . VAL   A 1 7   ? -19.405 -6.402  35.234 1.00 50.03  ? 82  VAL   A N   1 
ATOM   53   C CA  . VAL   A 1 7   ? -18.678 -5.227  34.764 1.00 55.92  ? 82  VAL   A CA  1 
ATOM   54   C C   . VAL   A 1 7   ? -19.281 -4.854  33.412 1.00 61.13  ? 82  VAL   A C   1 
ATOM   55   O O   . VAL   A 1 7   ? -18.992 -5.482  32.394 1.00 77.65  ? 82  VAL   A O   1 
ATOM   56   C CB  . VAL   A 1 7   ? -17.174 -5.490  34.670 1.00 48.04  ? 82  VAL   A CB  1 
ATOM   57   C CG1 . VAL   A 1 7   ? -16.452 -4.263  34.151 1.00 54.07  ? 82  VAL   A CG1 1 
ATOM   58   C CG2 . VAL   A 1 7   ? -16.624 -5.886  36.032 1.00 54.58  ? 82  VAL   A CG2 1 
ATOM   59   N N   . SER   A 1 8   ? -20.126 -3.826  33.404 1.00 86.68  ? 83  SER   A N   1 
ATOM   60   C CA  . SER   A 1 8   ? -20.938 -3.524  32.233 1.00 86.70  ? 83  SER   A CA  1 
ATOM   61   C C   . SER   A 1 8   ? -20.096 -2.937  31.106 1.00 77.57  ? 83  SER   A C   1 
ATOM   62   O O   . SER   A 1 8   ? -19.189 -2.130  31.334 1.00 69.03  ? 83  SER   A O   1 
ATOM   63   C CB  . SER   A 1 8   ? -22.062 -2.555  32.610 1.00 82.22  ? 83  SER   A CB  1 
ATOM   64   O OG  . SER   A 1 8   ? -22.959 -2.354  31.532 1.00 91.11  ? 83  SER   A OG  1 
ATOM   65   N N   . PHE   A 1 9   ? -20.409 -3.349  29.878 1.00 52.17  ? 84  PHE   A N   1 
ATOM   66   C CA  . PHE   A 1 9   ? -19.754 -2.821  28.690 1.00 75.08  ? 84  PHE   A CA  1 
ATOM   67   C C   . PHE   A 1 9   ? -20.656 -3.073  27.491 1.00 76.61  ? 84  PHE   A C   1 
ATOM   68   O O   . PHE   A 1 9   ? -21.289 -4.129  27.397 1.00 84.29  ? 84  PHE   A O   1 
ATOM   69   C CB  . PHE   A 1 9   ? -18.374 -3.457  28.469 1.00 53.80  ? 84  PHE   A CB  1 
ATOM   70   C CG  . PHE   A 1 9   ? -18.412 -4.949  28.291 1.00 65.35  ? 84  PHE   A CG  1 
ATOM   71   C CD1 . PHE   A 1 9   ? -18.412 -5.790  29.392 1.00 74.39  ? 84  PHE   A CD1 1 
ATOM   72   C CD2 . PHE   A 1 9   ? -18.446 -5.514  27.025 1.00 73.39  ? 84  PHE   A CD2 1 
ATOM   73   C CE1 . PHE   A 1 9   ? -18.445 -7.166  29.236 1.00 50.95  ? 84  PHE   A CE1 1 
ATOM   74   C CE2 . PHE   A 1 9   ? -18.480 -6.891  26.861 1.00 59.04  ? 84  PHE   A CE2 1 
ATOM   75   C CZ  . PHE   A 1 9   ? -18.478 -7.716  27.968 1.00 56.50  ? 84  PHE   A CZ  1 
ATOM   76   N N   . ARG   A 1 10  ? -20.712 -2.098  26.584 1.00 78.98  ? 85  ARG   A N   1 
ATOM   77   C CA  . ARG   A 1 10  ? -21.512 -2.245  25.375 1.00 75.55  ? 85  ARG   A CA  1 
ATOM   78   C C   . ARG   A 1 10  ? -21.007 -3.424  24.552 1.00 79.46  ? 85  ARG   A C   1 
ATOM   79   O O   . ARG   A 1 10  ? -19.801 -3.575  24.335 1.00 75.69  ? 85  ARG   A O   1 
ATOM   80   C CB  . ARG   A 1 10  ? -21.457 -0.958  24.551 1.00 73.43  ? 85  ARG   A CB  1 
ATOM   81   C CG  . ARG   A 1 10  ? -21.705 0.309   25.350 1.00 76.06  ? 85  ARG   A CG  1 
ATOM   82   C CD  . ARG   A 1 10  ? -23.177 0.491   25.697 1.00 69.58  ? 85  ARG   A CD  1 
ATOM   83   N NE  . ARG   A 1 10  ? -23.984 0.766   24.515 1.00 75.80  ? 85  ARG   A NE  1 
ATOM   84   C CZ  . ARG   A 1 10  ? -25.308 0.824   24.508 1.00 83.24  ? 85  ARG   A CZ  1 
ATOM   85   N NH1 . ARG   A 1 10  ? -26.015 0.625   25.609 1.00 85.27  ? 85  ARG   A NH1 1 
ATOM   86   N NH2 . ARG   A 1 10  ? -25.941 1.085   23.367 1.00 89.29  ? 85  ARG   A NH2 1 
ATOM   87   N N   . GLY   A 1 11  ? -21.934 -4.266  24.106 1.00 80.00  ? 86  GLY   A N   1 
ATOM   88   C CA  . GLY   A 1 11  ? -21.605 -5.410  23.288 1.00 74.32  ? 86  GLY   A CA  1 
ATOM   89   C C   . GLY   A 1 11  ? -21.511 -6.731  24.011 1.00 81.59  ? 86  GLY   A C   1 
ATOM   90   O O   . GLY   A 1 11  ? -21.112 -7.722  23.391 1.00 85.89  ? 86  GLY   A O   1 
ATOM   91   N N   . GLU   A 1 12  ? -21.862 -6.786  25.294 1.00 86.49  ? 87  GLU   A N   1 
ATOM   92   C CA  . GLU   A 1 12  ? -21.799 -8.043  26.025 1.00 89.01  ? 87  GLU   A CA  1 
ATOM   93   C C   . GLU   A 1 12  ? -22.932 -8.970  25.600 1.00 93.87  ? 87  GLU   A C   1 
ATOM   94   O O   . GLU   A 1 12  ? -24.029 -8.531  25.244 1.00 90.65  ? 87  GLU   A O   1 
ATOM   95   C CB  . GLU   A 1 12  ? -21.854 -7.793  27.535 1.00 83.08  ? 87  GLU   A CB  1 
ATOM   96   C CG  . GLU   A 1 12  ? -23.013 -6.939  28.006 1.00 92.45  ? 87  GLU   A CG  1 
ATOM   97   C CD  . GLU   A 1 12  ? -23.009 -6.751  29.512 1.00 96.75  ? 87  GLU   A CD  1 
ATOM   98   O OE1 . GLU   A 1 12  ? -22.147 -7.360  30.184 1.00 83.83  ? 87  GLU   A OE1 1 
ATOM   99   O OE2 . GLU   A 1 12  ? -23.863 -5.994  30.022 1.00 107.01 ? 87  GLU   A OE2 1 
ATOM   100  N N   . ALA   A 1 13  ? -22.656 -10.274 25.653 1.00 90.76  ? 88  ALA   A N   1 
ATOM   101  C CA  . ALA   A 1 13  ? -23.601 -11.281 25.196 1.00 93.89  ? 88  ALA   A CA  1 
ATOM   102  C C   . ALA   A 1 13  ? -24.756 -11.499 26.159 1.00 97.59  ? 88  ALA   A C   1 
ATOM   103  O O   . ALA   A 1 13  ? -25.734 -12.152 25.781 1.00 117.51 ? 88  ALA   A O   1 
ATOM   104  C CB  . ALA   A 1 13  ? -22.878 -12.609 24.959 1.00 96.90  ? 88  ALA   A CB  1 
ATOM   105  N N   . SER   A 1 14  ? -24.674 -10.982 27.383 1.00 98.07  ? 89  SER   A N   1 
ATOM   106  C CA  . SER   A 1 14  ? -25.743 -11.177 28.358 1.00 114.47 ? 89  SER   A CA  1 
ATOM   107  C C   . SER   A 1 14  ? -25.697 -10.043 29.366 1.00 125.63 ? 89  SER   A C   1 
ATOM   108  O O   . SER   A 1 14  ? -24.696 -9.886  30.074 1.00 121.21 ? 89  SER   A O   1 
ATOM   109  C CB  . SER   A 1 14  ? -25.605 -12.530 29.059 1.00 103.61 ? 89  SER   A CB  1 
ATOM   110  O OG  . SER   A 1 14  ? -26.627 -12.712 30.023 1.00 113.87 ? 89  SER   A OG  1 
ATOM   111  N N   . GLU   A 1 15  ? -26.767 -9.254  29.428 1.00 145.65 ? 90  GLU   A N   1 
ATOM   112  C CA  . GLU   A 1 15  ? -26.911 -8.221  30.444 1.00 147.36 ? 90  GLU   A CA  1 
ATOM   113  C C   . GLU   A 1 15  ? -27.485 -8.760  31.749 1.00 149.17 ? 90  GLU   A C   1 
ATOM   114  O O   . GLU   A 1 15  ? -27.793 -7.971  32.648 1.00 151.71 ? 90  GLU   A O   1 
ATOM   115  C CB  . GLU   A 1 15  ? -27.782 -7.079  29.914 1.00 146.25 ? 90  GLU   A CB  1 
ATOM   116  C CG  . GLU   A 1 15  ? -27.103 -6.234  28.848 1.00 144.10 ? 90  GLU   A CG  1 
ATOM   117  C CD  . GLU   A 1 15  ? -28.001 -5.141  28.308 1.00 141.99 ? 90  GLU   A CD  1 
ATOM   118  O OE1 . GLU   A 1 15  ? -29.228 -5.360  28.232 1.00 142.75 ? 90  GLU   A OE1 1 
ATOM   119  O OE2 . GLU   A 1 15  ? -27.482 -4.058  27.964 1.00 138.50 ? 90  GLU   A OE2 1 
ATOM   120  N N   . THR   A 1 16  ? -27.638 -10.077 31.865 1.00 142.40 ? 91  THR   A N   1 
ATOM   121  C CA  . THR   A 1 16  ? -28.070 -10.690 33.112 1.00 137.10 ? 91  THR   A CA  1 
ATOM   122  C C   . THR   A 1 16  ? -26.873 -10.873 34.037 1.00 131.56 ? 91  THR   A C   1 
ATOM   123  O O   . THR   A 1 16  ? -25.775 -11.220 33.592 1.00 123.14 ? 91  THR   A O   1 
ATOM   124  C CB  . THR   A 1 16  ? -28.741 -12.039 32.844 1.00 133.83 ? 91  THR   A CB  1 
ATOM   125  O OG1 . THR   A 1 16  ? -29.724 -11.889 31.811 1.00 157.07 ? 91  THR   A OG1 1 
ATOM   126  C CG2 . THR   A 1 16  ? -29.422 -12.560 34.101 1.00 131.21 ? 91  THR   A CG2 1 
ATOM   127  N N   . LEU   A 1 17  ? -27.090 -10.625 35.331 1.00 138.50 ? 92  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 17  ? -25.994 -10.698 36.293 1.00 139.97 ? 92  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 17  ? -25.445 -12.115 36.415 1.00 131.04 ? 92  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 17  ? -24.226 -12.306 36.504 1.00 109.88 ? 92  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 17  ? -26.459 -10.186 37.657 1.00 127.52 ? 92  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 17  ? -26.806 -8.703  37.793 1.00 112.08 ? 92  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 17  ? -27.556 -8.450  39.092 1.00 101.49 ? 92  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 17  ? -25.546 -7.852  37.730 1.00 92.76  ? 92  LEU   A CD2 1 
ATOM   135  N N   . GLN   A 1 18  ? -26.320 -13.119 36.414 1.00 127.77 ? 93  GLN   A N   1 
ATOM   136  C CA  . GLN   A 1 18  ? -25.912 -14.491 36.674 1.00 130.83 ? 93  GLN   A CA  1 
ATOM   137  C C   . GLN   A 1 18  ? -26.658 -15.441 35.747 1.00 141.47 ? 93  GLN   A C   1 
ATOM   138  O O   . GLN   A 1 18  ? -27.592 -15.056 35.039 1.00 136.66 ? 93  GLN   A O   1 
ATOM   139  C CB  . GLN   A 1 18  ? -26.163 -14.883 38.137 1.00 137.30 ? 93  GLN   A CB  1 
ATOM   140  C CG  . GLN   A 1 18  ? -27.625 -15.179 38.472 1.00 146.13 ? 93  GLN   A CG  1 
ATOM   141  C CD  . GLN   A 1 18  ? -28.499 -13.937 38.494 1.00 144.20 ? 93  GLN   A CD  1 
ATOM   142  O OE1 . GLN   A 1 18  ? -28.002 -12.813 38.474 1.00 149.08 ? 93  GLN   A OE1 1 
ATOM   143  N NE2 . GLN   A 1 18  ? -29.812 -14.138 38.539 1.00 137.24 ? 93  GLN   A NE2 1 
ATOM   144  N N   . SER   A 1 19  ? -26.225 -16.707 35.765 1.00 136.16 ? 94  SER   A N   1 
ATOM   145  C CA  . SER   A 1 19  ? -26.788 -17.868 35.101 1.00 110.62 ? 94  SER   A CA  1 
ATOM   146  C C   . SER   A 1 19  ? -27.697 -18.632 36.057 1.00 125.61 ? 94  SER   A C   1 
ATOM   147  O O   . SER   A 1 19  ? -27.507 -18.578 37.277 1.00 127.29 ? 94  SER   A O   1 
ATOM   148  C CB  . SER   A 1 19  ? -25.676 -18.795 34.598 1.00 111.16 ? 94  SER   A CB  1 
ATOM   149  O OG  . SER   A 1 19  ? -24.776 -19.126 35.642 1.00 97.84  ? 94  SER   A OG  1 
ATOM   150  N N   . PRO   A 1 20  ? -28.702 -19.343 35.537 1.00 133.52 ? 95  PRO   A N   1 
ATOM   151  C CA  . PRO   A 1 20  ? -29.634 -20.050 36.433 1.00 133.17 ? 95  PRO   A CA  1 
ATOM   152  C C   . PRO   A 1 20  ? -28.968 -21.090 37.319 1.00 129.43 ? 95  PRO   A C   1 
ATOM   153  O O   . PRO   A 1 20  ? -29.497 -21.399 38.394 1.00 123.00 ? 95  PRO   A O   1 
ATOM   154  C CB  . PRO   A 1 20  ? -30.631 -20.693 35.458 1.00 122.16 ? 95  PRO   A CB  1 
ATOM   155  C CG  . PRO   A 1 20  ? -30.560 -19.842 34.232 1.00 112.34 ? 95  PRO   A CG  1 
ATOM   156  C CD  . PRO   A 1 20  ? -29.128 -19.411 34.129 1.00 118.73 ? 95  PRO   A CD  1 
ATOM   157  N N   . GLY   A 1 21  ? -27.825 -21.638 36.907 1.00 115.62 ? 96  GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 21  ? -27.131 -22.620 37.723 1.00 115.36 ? 96  GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 21  ? -26.452 -22.053 38.953 1.00 110.72 ? 96  GLY   A C   1 
ATOM   160  O O   . GLY   A 1 21  ? -25.995 -22.831 39.799 1.00 102.69 ? 96  GLY   A O   1 
ATOM   161  N N   . TYR   A 1 22  ? -26.381 -20.731 39.076 1.00 88.22  ? 97  TYR   A N   1 
ATOM   162  C CA  . TYR   A 1 22  ? -25.687 -20.091 40.186 1.00 101.74 ? 97  TYR   A CA  1 
ATOM   163  C C   . TYR   A 1 22  ? -26.633 -19.957 41.374 1.00 94.07  ? 97  TYR   A C   1 
ATOM   164  O O   . TYR   A 1 22  ? -27.712 -19.368 41.253 1.00 99.39  ? 97  TYR   A O   1 
ATOM   165  C CB  . TYR   A 1 22  ? -25.145 -18.724 39.767 1.00 91.55  ? 97  TYR   A CB  1 
ATOM   166  C CG  . TYR   A 1 22  ? -24.591 -17.912 40.916 1.00 85.70  ? 97  TYR   A CG  1 
ATOM   167  C CD1 . TYR   A 1 22  ? -23.508 -18.369 41.656 1.00 84.29  ? 97  TYR   A CD1 1 
ATOM   168  C CD2 . TYR   A 1 22  ? -25.149 -16.686 41.260 1.00 71.44  ? 97  TYR   A CD2 1 
ATOM   169  C CE1 . TYR   A 1 22  ? -22.999 -17.632 42.709 1.00 76.34  ? 97  TYR   A CE1 1 
ATOM   170  C CE2 . TYR   A 1 22  ? -24.646 -15.942 42.311 1.00 68.47  ? 97  TYR   A CE2 1 
ATOM   171  C CZ  . TYR   A 1 22  ? -23.571 -16.420 43.032 1.00 66.15  ? 97  TYR   A CZ  1 
ATOM   172  O OH  . TYR   A 1 22  ? -23.067 -15.683 44.079 1.00 70.31  ? 97  TYR   A OH  1 
ATOM   173  N N   . ASP   A 1 23  ? -26.226 -20.510 42.516 1.00 94.02  ? 98  ASP   A N   1 
ATOM   174  C CA  . ASP   A 1 23  ? -26.974 -20.389 43.762 1.00 83.23  ? 98  ASP   A CA  1 
ATOM   175  C C   . ASP   A 1 23  ? -26.221 -19.452 44.697 1.00 90.83  ? 98  ASP   A C   1 
ATOM   176  O O   . ASP   A 1 23  ? -25.143 -19.817 45.191 1.00 92.96  ? 98  ASP   A O   1 
ATOM   177  C CB  . ASP   A 1 23  ? -27.163 -21.760 44.415 1.00 100.29 ? 98  ASP   A CB  1 
ATOM   178  C CG  . ASP   A 1 23  ? -28.207 -21.747 45.518 1.00 108.50 ? 98  ASP   A CG  1 
ATOM   179  O OD1 . ASP   A 1 23  ? -28.444 -20.673 46.109 1.00 96.91  ? 98  ASP   A OD1 1 
ATOM   180  O OD2 . ASP   A 1 23  ? -28.794 -22.816 45.795 1.00 105.87 ? 98  ASP   A OD2 1 
ATOM   181  N N   . PRO   A 1 24  ? -26.738 -18.251 44.978 1.00 100.29 ? 99  PRO   A N   1 
ATOM   182  C CA  . PRO   A 1 24  ? -25.988 -17.300 45.818 1.00 85.69  ? 99  PRO   A CA  1 
ATOM   183  C C   . PRO   A 1 24  ? -25.824 -17.740 47.268 1.00 105.82 ? 99  PRO   A C   1 
ATOM   184  O O   . PRO   A 1 24  ? -25.119 -17.053 48.022 1.00 88.39  ? 99  PRO   A O   1 
ATOM   185  C CB  . PRO   A 1 24  ? -26.822 -16.014 45.725 1.00 77.89  ? 99  PRO   A CB  1 
ATOM   186  C CG  . PRO   A 1 24  ? -27.683 -16.192 44.497 1.00 77.62  ? 99  PRO   A CG  1 
ATOM   187  C CD  . PRO   A 1 24  ? -27.966 -17.657 44.424 1.00 89.28  ? 99  PRO   A CD  1 
ATOM   188  N N   . SER   A 1 25  ? -26.443 -18.850 47.684 1.00 100.84 ? 100 SER   A N   1 
ATOM   189  C CA  . SER   A 1 25  ? -26.350 -19.291 49.071 1.00 78.32  ? 100 SER   A CA  1 
ATOM   190  C C   . SER   A 1 25  ? -25.082 -20.096 49.325 1.00 92.91  ? 100 SER   A C   1 
ATOM   191  O O   . SER   A 1 25  ? -24.612 -20.169 50.467 1.00 87.82  ? 100 SER   A O   1 
ATOM   192  C CB  . SER   A 1 25  ? -27.580 -20.124 49.443 1.00 81.81  ? 100 SER   A CB  1 
ATOM   193  O OG  . SER   A 1 25  ? -28.786 -19.425 49.169 1.00 97.59  ? 100 SER   A OG  1 
ATOM   194  N N   . ARG   A 1 26  ? -24.513 -20.698 48.285 1.00 82.98  ? 101 ARG   A N   1 
ATOM   195  C CA  . ARG   A 1 26  ? -23.338 -21.529 48.465 1.00 76.12  ? 101 ARG   A CA  1 
ATOM   196  C C   . ARG   A 1 26  ? -22.112 -20.659 48.737 1.00 91.53  ? 101 ARG   A C   1 
ATOM   197  O O   . ARG   A 1 26  ? -22.059 -19.498 48.319 1.00 85.97  ? 101 ARG   A O   1 
ATOM   198  C CB  . ARG   A 1 26  ? -23.101 -22.385 47.225 1.00 97.47  ? 101 ARG   A CB  1 
ATOM   199  C CG  . ARG   A 1 26  ? -24.364 -22.969 46.619 1.00 90.30  ? 101 ARG   A CG  1 
ATOM   200  C CD  . ARG   A 1 26  ? -24.717 -24.308 47.236 1.00 95.09  ? 101 ARG   A CD  1 
ATOM   201  N NE  . ARG   A 1 26  ? -23.811 -25.360 46.792 1.00 106.03 ? 101 ARG   A NE  1 
ATOM   202  C CZ  . ARG   A 1 26  ? -23.995 -26.652 47.024 1.00 109.95 ? 101 ARG   A CZ  1 
ATOM   203  N NH1 . ARG   A 1 26  ? -25.048 -27.090 47.696 1.00 97.47  ? 101 ARG   A NH1 1 
ATOM   204  N NH2 . ARG   A 1 26  ? -23.105 -27.528 46.567 1.00 115.03 ? 101 ARG   A NH2 1 
ATOM   205  N N   . PRO   A 1 27  ? -21.110 -21.193 49.440 1.00 99.36  ? 102 PRO   A N   1 
ATOM   206  C CA  . PRO   A 1 27  ? -19.862 -20.442 49.629 1.00 93.20  ? 102 PRO   A CA  1 
ATOM   207  C C   . PRO   A 1 27  ? -18.955 -20.425 48.408 1.00 92.94  ? 102 PRO   A C   1 
ATOM   208  O O   . PRO   A 1 27  ? -17.923 -19.738 48.440 1.00 99.92  ? 102 PRO   A O   1 
ATOM   209  C CB  . PRO   A 1 27  ? -19.190 -21.176 50.796 1.00 91.37  ? 102 PRO   A CB  1 
ATOM   210  C CG  . PRO   A 1 27  ? -19.702 -22.571 50.696 1.00 97.33  ? 102 PRO   A CG  1 
ATOM   211  C CD  . PRO   A 1 27  ? -21.121 -22.449 50.210 1.00 83.12  ? 102 PRO   A CD  1 
ATOM   212  N N   . GLU   A 1 28  ? -19.293 -21.151 47.345 1.00 97.16  ? 103 GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 28  ? -18.473 -21.163 46.143 1.00 89.49  ? 103 GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 28  ? -18.739 -19.925 45.295 1.00 79.09  ? 103 GLU   A C   1 
ATOM   215  O O   . GLU   A 1 28  ? -19.841 -19.368 45.292 1.00 77.74  ? 103 GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 28  ? -18.738 -22.424 45.317 1.00 94.24  ? 103 GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 28  ? -18.127 -23.698 45.893 1.00 86.19  ? 103 GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 28  ? -18.884 -24.230 47.097 1.00 114.65 ? 103 GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 28  ? -20.074 -23.887 47.256 1.00 96.94  ? 103 GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 28  ? -18.286 -24.993 47.885 1.00 117.05 ? 103 GLU   A OE2 1 
ATOM   221  N N   . SER   A 1 29  ? -17.711 -19.498 44.569 1.00 71.17  ? 104 SER   A N   1 
ATOM   222  C CA  . SER   A 1 29  ? -17.816 -18.310 43.741 1.00 64.12  ? 104 SER   A CA  1 
ATOM   223  C C   . SER   A 1 29  ? -18.670 -18.582 42.505 1.00 69.65  ? 104 SER   A C   1 
ATOM   224  O O   . SER   A 1 29  ? -18.913 -19.730 42.122 1.00 78.37  ? 104 SER   A O   1 
ATOM   225  C CB  . SER   A 1 29  ? -16.429 -17.833 43.318 1.00 64.70  ? 104 SER   A CB  1 
ATOM   226  O OG  . SER   A 1 29  ? -15.740 -18.856 42.619 1.00 82.01  ? 104 SER   A OG  1 
ATOM   227  N N   . PHE   A 1 30  ? -19.129 -17.494 41.879 1.00 68.11  ? 105 PHE   A N   1 
ATOM   228  C CA  . PHE   A 1 30  ? -19.841 -17.615 40.610 1.00 68.63  ? 105 PHE   A CA  1 
ATOM   229  C C   . PHE   A 1 30  ? -18.992 -18.325 39.567 1.00 57.63  ? 105 PHE   A C   1 
ATOM   230  O O   . PHE   A 1 30  ? -19.522 -19.053 38.720 1.00 69.11  ? 105 PHE   A O   1 
ATOM   231  C CB  . PHE   A 1 30  ? -20.257 -16.229 40.112 1.00 62.42  ? 105 PHE   A CB  1 
ATOM   232  C CG  . PHE   A 1 30  ? -20.847 -16.227 38.729 1.00 52.40  ? 105 PHE   A CG  1 
ATOM   233  C CD1 . PHE   A 1 30  ? -22.183 -16.536 38.529 1.00 65.34  ? 105 PHE   A CD1 1 
ATOM   234  C CD2 . PHE   A 1 30  ? -20.070 -15.905 37.632 1.00 52.48  ? 105 PHE   A CD2 1 
ATOM   235  C CE1 . PHE   A 1 30  ? -22.728 -16.532 37.256 1.00 80.16  ? 105 PHE   A CE1 1 
ATOM   236  C CE2 . PHE   A 1 30  ? -20.608 -15.901 36.359 1.00 54.89  ? 105 PHE   A CE2 1 
ATOM   237  C CZ  . PHE   A 1 30  ? -21.939 -16.214 36.173 1.00 78.68  ? 105 PHE   A CZ  1 
ATOM   238  N N   . PHE   A 1 31  ? -17.674 -18.128 39.619 1.00 69.30  ? 106 PHE   A N   1 
ATOM   239  C CA  . PHE   A 1 31  ? -16.774 -18.841 38.720 1.00 68.77  ? 106 PHE   A CA  1 
ATOM   240  C C   . PHE   A 1 31  ? -16.812 -20.341 38.983 1.00 67.61  ? 106 PHE   A C   1 
ATOM   241  O O   . PHE   A 1 31  ? -16.932 -21.145 38.052 1.00 85.83  ? 106 PHE   A O   1 
ATOM   242  C CB  . PHE   A 1 31  ? -15.356 -18.295 38.883 1.00 62.75  ? 106 PHE   A CB  1 
ATOM   243  C CG  . PHE   A 1 31  ? -14.331 -18.977 38.029 1.00 53.40  ? 106 PHE   A CG  1 
ATOM   244  C CD1 . PHE   A 1 31  ? -14.329 -18.806 36.655 1.00 54.79  ? 106 PHE   A CD1 1 
ATOM   245  C CD2 . PHE   A 1 31  ? -13.346 -19.759 38.605 1.00 57.43  ? 106 PHE   A CD2 1 
ATOM   246  C CE1 . PHE   A 1 31  ? -13.376 -19.420 35.868 1.00 50.56  ? 106 PHE   A CE1 1 
ATOM   247  C CE2 . PHE   A 1 31  ? -12.388 -20.373 37.824 1.00 73.16  ? 106 PHE   A CE2 1 
ATOM   248  C CZ  . PHE   A 1 31  ? -12.404 -20.202 36.452 1.00 53.36  ? 106 PHE   A CZ  1 
ATOM   249  N N   . GLN   A 1 32  ? -16.726 -20.735 40.255 1.00 60.73  ? 107 GLN   A N   1 
ATOM   250  C CA  . GLN   A 1 32  ? -16.704 -22.155 40.583 1.00 71.31  ? 107 GLN   A CA  1 
ATOM   251  C C   . GLN   A 1 32  ? -18.056 -22.812 40.353 1.00 65.69  ? 107 GLN   A C   1 
ATOM   252  O O   . GLN   A 1 32  ? -18.117 -24.021 40.109 1.00 89.19  ? 107 GLN   A O   1 
ATOM   253  C CB  . GLN   A 1 32  ? -16.259 -22.353 42.031 1.00 79.70  ? 107 GLN   A CB  1 
ATOM   254  C CG  . GLN   A 1 32  ? -14.808 -21.981 42.291 1.00 91.48  ? 107 GLN   A CG  1 
ATOM   255  C CD  . GLN   A 1 32  ? -14.481 -21.937 43.769 1.00 100.68 ? 107 GLN   A CD  1 
ATOM   256  O OE1 . GLN   A 1 32  ? -15.352 -22.147 44.615 1.00 100.57 ? 107 GLN   A OE1 1 
ATOM   257  N NE2 . GLN   A 1 32  ? -13.224 -21.661 44.090 1.00 100.79 ? 107 GLN   A NE2 1 
ATOM   258  N N   . GLN   A 1 33  ? -19.144 -22.046 40.422 1.00 66.16  ? 108 GLN   A N   1 
ATOM   259  C CA  . GLN   A 1 33  ? -20.474 -22.623 40.280 1.00 73.98  ? 108 GLN   A CA  1 
ATOM   260  C C   . GLN   A 1 33  ? -20.950 -22.661 38.835 1.00 63.94  ? 108 GLN   A C   1 
ATOM   261  O O   . GLN   A 1 33  ? -21.614 -23.620 38.432 1.00 80.73  ? 108 GLN   A O   1 
ATOM   262  C CB  . GLN   A 1 33  ? -21.483 -21.845 41.126 1.00 67.06  ? 108 GLN   A CB  1 
ATOM   263  C CG  . GLN   A 1 33  ? -21.237 -21.918 42.620 1.00 73.22  ? 108 GLN   A CG  1 
ATOM   264  C CD  . GLN   A 1 33  ? -22.385 -21.342 43.419 1.00 86.48  ? 108 GLN   A CD  1 
ATOM   265  O OE1 . GLN   A 1 33  ? -23.551 -21.530 43.074 1.00 101.49 ? 108 GLN   A OE1 1 
ATOM   266  N NE2 . GLN   A 1 33  ? -22.061 -20.628 44.491 1.00 77.68  ? 108 GLN   A NE2 1 
ATOM   267  N N   . SER   A 1 34  ? -20.634 -21.640 38.046 1.00 70.18  ? 109 SER   A N   1 
ATOM   268  C CA  . SER   A 1 34  ? -21.147 -21.531 36.689 1.00 78.28  ? 109 SER   A CA  1 
ATOM   269  C C   . SER   A 1 34  ? -20.165 -22.035 35.639 1.00 71.46  ? 109 SER   A C   1 
ATOM   270  O O   . SER   A 1 34  ? -20.439 -21.906 34.440 1.00 58.80  ? 109 SER   A O   1 
ATOM   271  C CB  . SER   A 1 34  ? -21.531 -20.081 36.392 1.00 66.08  ? 109 SER   A CB  1 
ATOM   272  O OG  . SER   A 1 34  ? -21.994 -19.942 35.062 1.00 96.71  ? 109 SER   A OG  1 
ATOM   273  N N   . PHE   A 1 35  ? -19.038 -22.613 36.052 1.00 75.49  ? 110 PHE   A N   1 
ATOM   274  C CA  . PHE   A 1 35  ? -18.019 -23.046 35.106 1.00 64.41  ? 110 PHE   A CA  1 
ATOM   275  C C   . PHE   A 1 35  ? -17.360 -24.333 35.574 1.00 75.05  ? 110 PHE   A C   1 
ATOM   276  O O   . PHE   A 1 35  ? -16.896 -24.423 36.714 1.00 82.76  ? 110 PHE   A O   1 
ATOM   277  C CB  . PHE   A 1 35  ? -16.950 -21.971 34.912 1.00 53.55  ? 110 PHE   A CB  1 
ATOM   278  C CG  . PHE   A 1 35  ? -17.433 -20.775 34.157 1.00 58.22  ? 110 PHE   A CG  1 
ATOM   279  C CD1 . PHE   A 1 35  ? -17.543 -20.811 32.778 1.00 56.06  ? 110 PHE   A CD1 1 
ATOM   280  C CD2 . PHE   A 1 35  ? -17.778 -19.615 34.825 1.00 58.87  ? 110 PHE   A CD2 1 
ATOM   281  C CE1 . PHE   A 1 35  ? -17.989 -19.708 32.076 1.00 56.43  ? 110 PHE   A CE1 1 
ATOM   282  C CE2 . PHE   A 1 35  ? -18.225 -18.509 34.130 1.00 57.71  ? 110 PHE   A CE2 1 
ATOM   283  C CZ  . PHE   A 1 35  ? -18.330 -18.556 32.753 1.00 59.66  ? 110 PHE   A CZ  1 
ATOM   284  N N   . GLN   A 1 36  ? -17.318 -25.318 34.686 1.00 73.09  ? 111 GLN   A N   1 
ATOM   285  C CA  . GLN   A 1 36  ? -16.499 -26.506 34.885 1.00 82.71  ? 111 GLN   A CA  1 
ATOM   286  C C   . GLN   A 1 36  ? -15.109 -26.197 34.343 1.00 76.18  ? 111 GLN   A C   1 
ATOM   287  O O   . GLN   A 1 36  ? -14.936 -26.002 33.136 1.00 63.40  ? 111 GLN   A O   1 
ATOM   288  C CB  . GLN   A 1 36  ? -17.116 -27.713 34.184 1.00 86.54  ? 111 GLN   A CB  1 
ATOM   289  C CG  . GLN   A 1 36  ? -16.382 -29.025 34.429 1.00 91.59  ? 111 GLN   A CG  1 
ATOM   290  C CD  . GLN   A 1 36  ? -16.784 -30.112 33.447 1.00 92.00  ? 111 GLN   A CD  1 
ATOM   291  O OE1 . GLN   A 1 36  ? -16.938 -29.859 32.252 1.00 102.99 ? 111 GLN   A OE1 1 
ATOM   292  N NE2 . GLN   A 1 36  ? -16.956 -31.329 33.949 1.00 118.31 ? 111 GLN   A NE2 1 
ATOM   293  N N   . ARG   A 1 37  ? -14.127 -26.107 35.235 1.00 69.72  ? 112 ARG   A N   1 
ATOM   294  C CA  . ARG   A 1 37  ? -12.759 -25.880 34.799 1.00 62.80  ? 112 ARG   A CA  1 
ATOM   295  C C   . ARG   A 1 37  ? -12.232 -27.092 34.042 1.00 68.54  ? 112 ARG   A C   1 
ATOM   296  O O   . ARG   A 1 37  ? -12.680 -28.223 34.245 1.00 76.07  ? 112 ARG   A O   1 
ATOM   297  C CB  . ARG   A 1 37  ? -11.854 -25.582 35.994 1.00 64.60  ? 112 ARG   A CB  1 
ATOM   298  C CG  . ARG   A 1 37  ? -11.943 -24.159 36.506 1.00 72.18  ? 112 ARG   A CG  1 
ATOM   299  C CD  . ARG   A 1 37  ? -10.638 -23.764 37.175 1.00 83.84  ? 112 ARG   A CD  1 
ATOM   300  N NE  . ARG   A 1 37  ? -10.770 -23.561 38.613 1.00 89.99  ? 112 ARG   A NE  1 
ATOM   301  C CZ  . ARG   A 1 37  ? -9.756  -23.618 39.467 1.00 97.70  ? 112 ARG   A CZ  1 
ATOM   302  N NH1 . ARG   A 1 37  ? -8.531  -23.914 39.065 1.00 98.58  ? 112 ARG   A NH1 1 
ATOM   303  N NH2 . ARG   A 1 37  ? -9.979  -23.380 40.757 1.00 91.91  ? 112 ARG   A NH2 1 
ATOM   304  N N   . LEU   A 1 38  ? -11.269 -26.843 33.155 1.00 63.23  ? 113 LEU   A N   1 
ATOM   305  C CA  . LEU   A 1 38  ? -10.653 -27.913 32.383 1.00 65.42  ? 113 LEU   A CA  1 
ATOM   306  C C   . LEU   A 1 38  ? -9.140  -27.902 32.544 1.00 77.07  ? 113 LEU   A C   1 
ATOM   307  O O   . LEU   A 1 38  ? -8.557  -28.864 33.056 1.00 105.18 ? 113 LEU   A O   1 
ATOM   308  C CB  . LEU   A 1 38  ? -11.016 -27.795 30.902 1.00 62.70  ? 113 LEU   A CB  1 
ATOM   309  C CG  . LEU   A 1 38  ? -12.485 -27.879 30.501 1.00 61.92  ? 113 LEU   A CG  1 
ATOM   310  C CD1 . LEU   A 1 38  ? -12.570 -27.921 28.993 1.00 60.39  ? 113 LEU   A CD1 1 
ATOM   311  C CD2 . LEU   A 1 38  ? -13.153 -29.098 31.111 1.00 77.43  ? 113 LEU   A CD2 1 
ATOM   312  N N   . SER   A 1 39  ? -8.494  -26.824 32.107 1.00 63.72  ? 114 SER   A N   1 
ATOM   313  C CA  . SER   A 1 39  ? -7.043  -26.748 32.142 1.00 70.80  ? 114 SER   A CA  1 
ATOM   314  C C   . SER   A 1 39  ? -6.612  -25.293 32.245 1.00 67.15  ? 114 SER   A C   1 
ATOM   315  O O   . SER   A 1 39  ? -7.367  -24.373 31.915 1.00 62.41  ? 114 SER   A O   1 
ATOM   316  C CB  . SER   A 1 39  ? -6.417  -27.406 30.905 1.00 70.63  ? 114 SER   A CB  1 
ATOM   317  O OG  . SER   A 1 39  ? -6.825  -26.755 29.714 1.00 71.75  ? 114 SER   A OG  1 
ATOM   318  N N   . ARG   A 1 40  ? -5.380  -25.098 32.707 1.00 64.60  ? 115 ARG   A N   1 
ATOM   319  C CA  . ARG   A 1 40  ? -4.796  -23.771 32.840 1.00 62.86  ? 115 ARG   A CA  1 
ATOM   320  C C   . ARG   A 1 40  ? -4.048  -23.424 31.559 1.00 61.29  ? 115 ARG   A C   1 
ATOM   321  O O   . ARG   A 1 40  ? -3.122  -24.138 31.163 1.00 67.40  ? 115 ARG   A O   1 
ATOM   322  C CB  . ARG   A 1 40  ? -3.860  -23.710 34.047 1.00 66.88  ? 115 ARG   A CB  1 
ATOM   323  C CG  . ARG   A 1 40  ? -3.302  -22.325 34.325 1.00 71.64  ? 115 ARG   A CG  1 
ATOM   324  C CD  . ARG   A 1 40  ? -2.696  -22.231 35.718 1.00 89.08  ? 115 ARG   A CD  1 
ATOM   325  N NE  . ARG   A 1 40  ? -1.446  -22.972 35.835 1.00 85.54  ? 115 ARG   A NE  1 
ATOM   326  C CZ  . ARG   A 1 40  ? -0.728  -23.056 36.947 1.00 102.73 ? 115 ARG   A CZ  1 
ATOM   327  N NH1 . ARG   A 1 40  ? -1.114  -22.462 38.065 1.00 106.20 ? 115 ARG   A NH1 1 
ATOM   328  N NH2 . ARG   A 1 40  ? 0.404   -23.754 36.938 1.00 109.02 ? 115 ARG   A NH2 1 
ATOM   329  N N   . LEU   A 1 41  ? -4.450  -22.331 30.914 1.00 65.47  ? 116 LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 41  ? -3.824  -21.907 29.669 1.00 56.09  ? 116 LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 41  ? -2.578  -21.063 29.892 1.00 69.73  ? 116 LEU   A C   1 
ATOM   332  O O   . LEU   A 1 41  ? -1.661  -21.094 29.061 1.00 87.80  ? 116 LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 41  ? -4.827  -21.123 28.819 1.00 52.72  ? 116 LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 41  ? -6.072  -21.896 28.384 1.00 54.23  ? 116 LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 41  ? -7.069  -20.971 27.704 1.00 56.49  ? 116 LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 41  ? -5.691  -23.048 27.466 1.00 53.89  ? 116 LEU   A CD2 1 
ATOM   337  N N   . GLY   A 1 42  ? -2.524  -20.309 30.983 1.00 61.30  ? 117 GLY   A N   1 
ATOM   338  C CA  . GLY   A 1 42  ? -1.345  -19.519 31.287 1.00 70.66  ? 117 GLY   A CA  1 
ATOM   339  C C   . GLY   A 1 42  ? -1.492  -18.863 32.645 1.00 66.05  ? 117 GLY   A C   1 
ATOM   340  O O   . GLY   A 1 42  ? -2.596  -18.736 33.185 1.00 69.86  ? 117 GLY   A O   1 
ATOM   341  N N   . HIS   A 1 43  ? -0.348  -18.453 33.190 1.00 83.17  ? 118 HIS   A N   1 
ATOM   342  C CA  . HIS   A 1 43  ? -0.329  -17.731 34.454 1.00 81.57  ? 118 HIS   A CA  1 
ATOM   343  C C   . HIS   A 1 43  ? 0.805   -16.714 34.423 1.00 78.86  ? 118 HIS   A C   1 
ATOM   344  O O   . HIS   A 1 43  ? 1.580   -16.639 33.465 1.00 89.51  ? 118 HIS   A O   1 
ATOM   345  C CB  . HIS   A 1 43  ? -0.210  -18.691 35.647 1.00 79.02  ? 118 HIS   A CB  1 
ATOM   346  C CG  . HIS   A 1 43  ? 1.133   -19.344 35.780 1.00 93.73  ? 118 HIS   A CG  1 
ATOM   347  N ND1 . HIS   A 1 43  ? 2.271   -18.644 36.120 1.00 104.02 ? 118 HIS   A ND1 1 
ATOM   348  C CD2 . HIS   A 1 43  ? 1.514   -20.636 35.643 1.00 97.04  ? 118 HIS   A CD2 1 
ATOM   349  C CE1 . HIS   A 1 43  ? 3.298   -19.474 36.172 1.00 110.59 ? 118 HIS   A CE1 1 
ATOM   350  N NE2 . HIS   A 1 43  ? 2.865   -20.689 35.888 1.00 100.08 ? 118 HIS   A NE2 1 
ATOM   351  N N   . GLY   A 1 44  ? 0.893   -15.928 35.489 1.00 95.00  ? 119 GLY   A N   1 
ATOM   352  C CA  . GLY   A 1 44  ? 1.908   -14.898 35.602 1.00 91.56  ? 119 GLY   A CA  1 
ATOM   353  C C   . GLY   A 1 44  ? 1.439   -13.808 36.550 1.00 96.91  ? 119 GLY   A C   1 
ATOM   354  O O   . GLY   A 1 44  ? 0.546   -14.022 37.370 1.00 94.79  ? 119 GLY   A O   1 
ATOM   355  N N   . SER   A 1 45  ? 2.069   -12.638 36.416 1.00 94.19  ? 120 SER   A N   1 
ATOM   356  C CA  . SER   A 1 45  ? 1.641   -11.486 37.202 1.00 91.70  ? 120 SER   A CA  1 
ATOM   357  C C   . SER   A 1 45  ? 0.222   -11.061 36.841 1.00 103.83 ? 120 SER   A C   1 
ATOM   358  O O   . SER   A 1 45  ? -0.507  -10.549 37.698 1.00 95.26  ? 120 SER   A O   1 
ATOM   359  C CB  . SER   A 1 45  ? 2.619   -10.324 37.013 1.00 78.60  ? 120 SER   A CB  1 
ATOM   360  O OG  . SER   A 1 45  ? 2.182   -9.181  37.728 1.00 93.74  ? 120 SER   A OG  1 
ATOM   361  N N   . TYR   A 1 46  ? -0.197  -11.295 35.594 1.00 106.34 ? 121 TYR   A N   1 
ATOM   362  C CA  . TYR   A 1 46  ? -1.527  -10.907 35.136 1.00 98.94  ? 121 TYR   A CA  1 
ATOM   363  C C   . TYR   A 1 46  ? -2.628  -11.793 35.707 1.00 99.65  ? 121 TYR   A C   1 
ATOM   364  O O   . TYR   A 1 46  ? -3.807  -11.494 35.528 1.00 83.44  ? 121 TYR   A O   1 
ATOM   365  C CB  . TYR   A 1 46  ? -1.587  -10.944 33.609 1.00 112.93 ? 121 TYR   A CB  1 
ATOM   366  C CG  . TYR   A 1 46  ? -1.334  -12.309 33.006 1.00 111.93 ? 121 TYR   A CG  1 
ATOM   367  C CD1 . TYR   A 1 46  ? -0.046  -12.724 32.691 1.00 105.36 ? 121 TYR   A CD1 1 
ATOM   368  C CD2 . TYR   A 1 46  ? -2.384  -13.182 32.750 1.00 97.24  ? 121 TYR   A CD2 1 
ATOM   369  C CE1 . TYR   A 1 46  ? 0.188   -13.971 32.142 1.00 103.79 ? 121 TYR   A CE1 1 
ATOM   370  C CE2 . TYR   A 1 46  ? -2.159  -14.431 32.201 1.00 76.46  ? 121 TYR   A CE2 1 
ATOM   371  C CZ  . TYR   A 1 46  ? -0.873  -14.820 31.899 1.00 84.88  ? 121 TYR   A CZ  1 
ATOM   372  O OH  . TYR   A 1 46  ? -0.644  -16.062 31.352 1.00 90.08  ? 121 TYR   A OH  1 
ATOM   373  N N   . GLY   A 1 47  ? -2.277  -12.876 36.399 1.00 96.78  ? 122 GLY   A N   1 
ATOM   374  C CA  . GLY   A 1 47  ? -3.238  -13.770 37.009 1.00 87.88  ? 122 GLY   A CA  1 
ATOM   375  C C   . GLY   A 1 47  ? -3.130  -15.169 36.420 1.00 87.28  ? 122 GLY   A C   1 
ATOM   376  O O   . GLY   A 1 47  ? -2.035  -15.712 36.245 1.00 88.97  ? 122 GLY   A O   1 
ATOM   377  N N   . GLU   A 1 48  ? -4.285  -15.745 36.089 1.00 61.09  ? 123 GLU   A N   1 
ATOM   378  C CA  A GLU   A 1 48  ? -4.368  -17.072 35.495 0.60 61.12  ? 123 GLU   A CA  1 
ATOM   379  C CA  B GLU   A 1 48  ? -4.386  -17.085 35.515 0.40 61.21  ? 123 GLU   A CA  1 
ATOM   380  C C   . GLU   A 1 48  ? -5.458  -17.085 34.438 1.00 54.02  ? 123 GLU   A C   1 
ATOM   381  O O   . GLU   A 1 48  ? -6.435  -16.342 34.535 1.00 59.95  ? 123 GLU   A O   1 
ATOM   382  C CB  A GLU   A 1 48  ? -4.629  -18.142 36.560 0.60 63.94  ? 123 GLU   A CB  1 
ATOM   383  C CB  B GLU   A 1 48  ? -4.717  -18.150 36.572 0.40 63.99  ? 123 GLU   A CB  1 
ATOM   384  C CG  A GLU   A 1 48  ? -3.473  -18.380 37.502 0.60 74.89  ? 123 GLU   A CG  1 
ATOM   385  C CG  B GLU   A 1 48  ? -3.896  -18.087 37.839 0.40 71.90  ? 123 GLU   A CG  1 
ATOM   386  C CD  A GLU   A 1 48  ? -3.803  -19.322 38.639 0.60 73.86  ? 123 GLU   A CD  1 
ATOM   387  C CD  B GLU   A 1 48  ? -4.507  -17.185 38.894 0.40 69.58  ? 123 GLU   A CD  1 
ATOM   388  O OE1 A GLU   A 1 48  ? -4.988  -19.419 39.003 0.60 74.47  ? 123 GLU   A OE1 1 
ATOM   389  O OE1 B GLU   A 1 48  ? -5.732  -17.279 39.114 0.40 66.96  ? 123 GLU   A OE1 1 
ATOM   390  O OE2 A GLU   A 1 48  ? -2.874  -19.976 39.159 0.60 80.40  ? 123 GLU   A OE2 1 
ATOM   391  O OE2 B GLU   A 1 48  ? -3.766  -16.373 39.490 0.40 72.44  ? 123 GLU   A OE2 1 
ATOM   392  N N   . VAL   A 1 49  ? -5.270  -17.928 33.427 1.00 53.51  ? 124 VAL   A N   1 
ATOM   393  C CA  . VAL   A 1 49  ? -6.225  -18.100 32.341 1.00 50.38  ? 124 VAL   A CA  1 
ATOM   394  C C   . VAL   A 1 49  ? -6.576  -19.578 32.267 1.00 51.57  ? 124 VAL   A C   1 
ATOM   395  O O   . VAL   A 1 49  ? -5.695  -20.421 32.055 1.00 56.41  ? 124 VAL   A O   1 
ATOM   396  C CB  . VAL   A 1 49  ? -5.664  -17.601 31.002 1.00 48.93  ? 124 VAL   A CB  1 
ATOM   397  C CG1 . VAL   A 1 49  ? -6.736  -17.652 29.939 1.00 50.42  ? 124 VAL   A CG1 1 
ATOM   398  C CG2 . VAL   A 1 49  ? -5.138  -16.193 31.148 1.00 48.81  ? 124 VAL   A CG2 1 
ATOM   399  N N   . PHE   A 1 50  ? -7.858  -19.890 32.431 1.00 50.50  ? 125 PHE   A N   1 
ATOM   400  C CA  . PHE   A 1 50  ? -8.342  -21.261 32.441 1.00 52.10  ? 125 PHE   A CA  1 
ATOM   401  C C   . PHE   A 1 50  ? -9.190  -21.536 31.209 1.00 50.01  ? 125 PHE   A C   1 
ATOM   402  O O   . PHE   A 1 50  ? -10.020 -20.710 30.817 1.00 48.77  ? 125 PHE   A O   1 
ATOM   403  C CB  . PHE   A 1 50  ? -9.180  -21.538 33.693 1.00 54.29  ? 125 PHE   A CB  1 
ATOM   404  C CG  . PHE   A 1 50  ? -8.431  -21.362 34.979 1.00 60.36  ? 125 PHE   A CG  1 
ATOM   405  C CD1 . PHE   A 1 50  ? -7.731  -22.419 35.538 1.00 65.66  ? 125 PHE   A CD1 1 
ATOM   406  C CD2 . PHE   A 1 50  ? -8.437  -20.144 35.636 1.00 55.55  ? 125 PHE   A CD2 1 
ATOM   407  C CE1 . PHE   A 1 50  ? -7.043  -22.261 36.728 1.00 75.05  ? 125 PHE   A CE1 1 
ATOM   408  C CE2 . PHE   A 1 50  ? -7.754  -19.978 36.824 1.00 63.38  ? 125 PHE   A CE2 1 
ATOM   409  C CZ  . PHE   A 1 50  ? -7.056  -21.038 37.371 1.00 71.04  ? 125 PHE   A CZ  1 
ATOM   410  N N   . LYS   A 1 51  ? -8.982  -22.700 30.604 1.00 57.19  ? 126 LYS   A N   1 
ATOM   411  C CA  . LYS   A 1 51  ? -9.934  -23.224 29.636 1.00 54.96  ? 126 LYS   A CA  1 
ATOM   412  C C   . LYS   A 1 51  ? -11.109 -23.807 30.406 1.00 56.53  ? 126 LYS   A C   1 
ATOM   413  O O   . LYS   A 1 51  ? -10.924 -24.706 31.233 1.00 71.73  ? 126 LYS   A O   1 
ATOM   414  C CB  . LYS   A 1 51  ? -9.285  -24.282 28.747 1.00 54.87  ? 126 LYS   A CB  1 
ATOM   415  C CG  . LYS   A 1 51  ? -10.214 -24.836 27.673 1.00 58.02  ? 126 LYS   A CG  1 
ATOM   416  C CD  . LYS   A 1 51  ? -9.459  -25.674 26.648 1.00 69.59  ? 126 LYS   A CD  1 
ATOM   417  C CE  . LYS   A 1 51  ? -8.926  -26.961 27.254 1.00 82.47  ? 126 LYS   A CE  1 
ATOM   418  N NZ  . LYS   A 1 51  ? -8.191  -27.790 26.256 1.00 85.91  ? 126 LYS   A NZ  1 
ATOM   419  N N   . VAL   A 1 52  ? -12.309 -23.289 30.161 1.00 53.18  ? 127 VAL   A N   1 
ATOM   420  C CA  . VAL   A 1 52  ? -13.480 -23.680 30.932 1.00 51.71  ? 127 VAL   A CA  1 
ATOM   421  C C   . VAL   A 1 52  ? -14.608 -24.084 29.996 1.00 58.20  ? 127 VAL   A C   1 
ATOM   422  O O   . VAL   A 1 52  ? -14.679 -23.645 28.843 1.00 60.17  ? 127 VAL   A O   1 
ATOM   423  C CB  . VAL   A 1 52  ? -13.953 -22.547 31.868 1.00 58.71  ? 127 VAL   A CB  1 
ATOM   424  C CG1 . VAL   A 1 52  ? -12.859 -22.171 32.854 1.00 51.07  ? 127 VAL   A CG1 1 
ATOM   425  C CG2 . VAL   A 1 52  ? -14.375 -21.341 31.049 1.00 47.27  ? 127 VAL   A CG2 1 
ATOM   426  N N   . ARG   A 1 53  ? -15.489 -24.938 30.504 1.00 60.24  ? 128 ARG   A N   1 
ATOM   427  C CA  . ARG   A 1 53  ? -16.797 -25.176 29.912 1.00 62.52  ? 128 ARG   A CA  1 
ATOM   428  C C   . ARG   A 1 53  ? -17.842 -24.624 30.867 1.00 67.31  ? 128 ARG   A C   1 
ATOM   429  O O   . ARG   A 1 53  ? -17.837 -24.961 32.056 1.00 63.32  ? 128 ARG   A O   1 
ATOM   430  C CB  . ARG   A 1 53  ? -17.053 -26.664 29.663 1.00 72.90  ? 128 ARG   A CB  1 
ATOM   431  C CG  . ARG   A 1 53  ? -16.035 -27.345 28.774 1.00 96.75  ? 128 ARG   A CG  1 
ATOM   432  C CD  . ARG   A 1 53  ? -16.638 -28.562 28.094 1.00 94.33  ? 128 ARG   A CD  1 
ATOM   433  N NE  . ARG   A 1 53  ? -17.013 -28.270 26.716 1.00 93.72  ? 128 ARG   A NE  1 
ATOM   434  C CZ  . ARG   A 1 53  ? -17.988 -28.880 26.058 1.00 95.03  ? 128 ARG   A CZ  1 
ATOM   435  N NH1 . ARG   A 1 53  ? -18.737 -29.805 26.635 1.00 95.96  ? 128 ARG   A NH1 1 
ATOM   436  N NH2 . ARG   A 1 53  ? -18.231 -28.538 24.795 1.00 77.54  ? 128 ARG   A NH2 1 
ATOM   437  N N   . SER   A 1 54  ? -18.718 -23.766 30.355 1.00 53.65  ? 129 SER   A N   1 
ATOM   438  C CA  . SER   A 1 54  ? -19.771 -23.214 31.191 1.00 59.16  ? 129 SER   A CA  1 
ATOM   439  C C   . SER   A 1 54  ? -20.692 -24.322 31.682 1.00 71.81  ? 129 SER   A C   1 
ATOM   440  O O   . SER   A 1 54  ? -21.079 -25.215 30.923 1.00 73.50  ? 129 SER   A O   1 
ATOM   441  C CB  . SER   A 1 54  ? -20.573 -22.170 30.418 1.00 66.84  ? 129 SER   A CB  1 
ATOM   442  O OG  . SER   A 1 54  ? -21.722 -21.775 31.145 1.00 93.94  ? 129 SER   A OG  1 
ATOM   443  N N   . LYS   A 1 55  ? -21.032 -24.274 32.966 1.00 81.69  ? 130 LYS   A N   1 
ATOM   444  C CA  . LYS   A 1 55  ? -22.047 -25.169 33.500 1.00 65.72  ? 130 LYS   A CA  1 
ATOM   445  C C   . LYS   A 1 55  ? -23.452 -24.700 33.157 1.00 67.32  ? 130 LYS   A C   1 
ATOM   446  O O   . LYS   A 1 55  ? -24.427 -25.254 33.674 1.00 81.35  ? 130 LYS   A O   1 
ATOM   447  C CB  . LYS   A 1 55  ? -21.883 -25.312 35.016 1.00 66.59  ? 130 LYS   A CB  1 
ATOM   448  C CG  . LYS   A 1 55  ? -20.582 -25.991 35.428 1.00 75.48  ? 130 LYS   A CG  1 
ATOM   449  C CD  . LYS   A 1 55  ? -20.491 -26.189 36.934 1.00 81.45  ? 130 LYS   A CD  1 
ATOM   450  C CE  . LYS   A 1 55  ? -19.190 -26.873 37.325 1.00 87.88  ? 130 LYS   A CE  1 
ATOM   451  N NZ  . LYS   A 1 55  ? -19.020 -26.950 38.802 1.00 75.35  ? 130 LYS   A NZ  1 
ATOM   452  N N   . GLU   A 1 56  ? -23.563 -23.690 32.296 1.00 64.75  ? 131 GLU   A N   1 
ATOM   453  C CA  . GLU   A 1 56  ? -24.832 -23.167 31.819 1.00 71.62  ? 131 GLU   A CA  1 
ATOM   454  C C   . GLU   A 1 56  ? -25.121 -23.562 30.379 1.00 79.58  ? 131 GLU   A C   1 
ATOM   455  O O   . GLU   A 1 56  ? -26.217 -24.043 30.082 1.00 99.35  ? 131 GLU   A O   1 
ATOM   456  C CB  . GLU   A 1 56  ? -24.852 -21.636 31.962 1.00 73.62  ? 131 GLU   A CB  1 
ATOM   457  C CG  . GLU   A 1 56  ? -25.954 -20.937 31.177 1.00 95.37  ? 131 GLU   A CG  1 
ATOM   458  C CD  . GLU   A 1 56  ? -25.523 -20.549 29.772 1.00 107.71 ? 131 GLU   A CD  1 
ATOM   459  O OE1 . GLU   A 1 56  ? -24.371 -20.094 29.606 1.00 112.10 ? 131 GLU   A OE1 1 
ATOM   460  O OE2 . GLU   A 1 56  ? -26.332 -20.716 28.834 1.00 90.59  ? 131 GLU   A OE2 1 
ATOM   461  N N   . ASP   A 1 57  ? -24.164 -23.370 29.467 1.00 69.70  ? 132 ASP   A N   1 
ATOM   462  C CA  . ASP   A 1 57  ? -24.360 -23.728 28.070 1.00 79.27  ? 132 ASP   A CA  1 
ATOM   463  C C   . ASP   A 1 57  ? -23.420 -24.821 27.585 1.00 71.27  ? 132 ASP   A C   1 
ATOM   464  O O   . ASP   A 1 57  ? -23.522 -25.227 26.419 1.00 72.21  ? 132 ASP   A O   1 
ATOM   465  C CB  . ASP   A 1 57  ? -24.216 -22.489 27.161 1.00 85.23  ? 132 ASP   A CB  1 
ATOM   466  C CG  . ASP   A 1 57  ? -22.840 -21.827 27.250 1.00 91.71  ? 132 ASP   A CG  1 
ATOM   467  O OD1 . ASP   A 1 57  ? -21.857 -22.487 27.640 1.00 96.70  ? 132 ASP   A OD1 1 
ATOM   468  O OD2 . ASP   A 1 57  ? -22.746 -20.625 26.918 1.00 85.89  ? 132 ASP   A OD2 1 
ATOM   469  N N   . GLY   A 1 58  ? -22.493 -25.285 28.427 1.00 68.78  ? 133 GLY   A N   1 
ATOM   470  C CA  . GLY   A 1 58  ? -21.478 -26.239 28.020 1.00 77.75  ? 133 GLY   A CA  1 
ATOM   471  C C   . GLY   A 1 58  ? -20.503 -25.762 26.964 1.00 75.66  ? 133 GLY   A C   1 
ATOM   472  O O   . GLY   A 1 58  ? -19.568 -26.511 26.635 1.00 80.07  ? 133 GLY   A O   1 
ATOM   473  N N   . ARG   A 1 59  ? -20.685 -24.574 26.391 1.00 82.19  ? 134 ARG   A N   1 
ATOM   474  C CA  . ARG   A 1 59  ? -19.738 -24.032 25.424 1.00 73.17  ? 134 ARG   A CA  1 
ATOM   475  C C   . ARG   A 1 59  ? -18.363 -23.819 26.059 1.00 58.93  ? 134 ARG   A C   1 
ATOM   476  O O   . ARG   A 1 59  ? -18.219 -23.713 27.280 1.00 74.14  ? 134 ARG   A O   1 
ATOM   477  C CB  . ARG   A 1 59  ? -20.232 -22.705 24.838 1.00 69.10  ? 134 ARG   A CB  1 
ATOM   478  C CG  . ARG   A 1 59  ? -21.474 -22.821 23.971 1.00 83.09  ? 134 ARG   A CG  1 
ATOM   479  C CD  . ARG   A 1 59  ? -21.525 -21.654 22.998 1.00 95.30  ? 134 ARG   A CD  1 
ATOM   480  N NE  . ARG   A 1 59  ? -22.879 -21.301 22.591 1.00 120.30 ? 134 ARG   A NE  1 
ATOM   481  C CZ  . ARG   A 1 59  ? -23.674 -20.479 23.265 1.00 106.77 ? 134 ARG   A CZ  1 
ATOM   482  N NH1 . ARG   A 1 59  ? -23.297 -19.935 24.411 1.00 79.76  ? 134 ARG   A NH1 1 
ATOM   483  N NH2 . ARG   A 1 59  ? -24.879 -20.198 22.777 1.00 102.96 ? 134 ARG   A NH2 1 
ATOM   484  N N   . LEU   A 1 60  ? -17.343 -23.766 25.208 1.00 65.94  ? 135 LEU   A N   1 
ATOM   485  C CA  . LEU   A 1 60  ? -15.962 -23.627 25.637 1.00 60.96  ? 135 LEU   A CA  1 
ATOM   486  C C   . LEU   A 1 60  ? -15.577 -22.157 25.586 1.00 60.73  ? 135 LEU   A C   1 
ATOM   487  O O   . LEU   A 1 60  ? -15.717 -21.508 24.544 1.00 68.17  ? 135 LEU   A O   1 
ATOM   488  C CB  . LEU   A 1 60  ? -15.043 -24.467 24.752 1.00 65.88  ? 135 LEU   A CB  1 
ATOM   489  C CG  . LEU   A 1 60  ? -14.732 -25.855 25.300 1.00 69.44  ? 135 LEU   A CG  1 
ATOM   490  C CD1 . LEU   A 1 60  ? -14.197 -26.756 24.202 1.00 58.35  ? 135 LEU   A CD1 1 
ATOM   491  C CD2 . LEU   A 1 60  ? -13.724 -25.721 26.423 1.00 58.19  ? 135 LEU   A CD2 1 
ATOM   492  N N   . TYR   A 1 61  ? -15.115 -21.633 26.714 1.00 48.37  ? 136 TYR   A N   1 
ATOM   493  C CA  . TYR   A 1 61  ? -14.619 -20.273 26.802 1.00 42.79  ? 136 TYR   A CA  1 
ATOM   494  C C   . TYR   A 1 61  ? -13.271 -20.292 27.502 1.00 44.39  ? 136 TYR   A C   1 
ATOM   495  O O   . TYR   A 1 61  ? -12.828 -21.321 28.020 1.00 49.73  ? 136 TYR   A O   1 
ATOM   496  C CB  . TYR   A 1 61  ? -15.588 -19.358 27.565 1.00 46.86  ? 136 TYR   A CB  1 
ATOM   497  C CG  . TYR   A 1 61  ? -16.965 -19.253 26.955 1.00 57.42  ? 136 TYR   A CG  1 
ATOM   498  C CD1 . TYR   A 1 61  ? -17.227 -18.343 25.941 1.00 60.86  ? 136 TYR   A CD1 1 
ATOM   499  C CD2 . TYR   A 1 61  ? -18.005 -20.055 27.402 1.00 45.99  ? 136 TYR   A CD2 1 
ATOM   500  C CE1 . TYR   A 1 61  ? -18.488 -18.240 25.382 1.00 71.24  ? 136 TYR   A CE1 1 
ATOM   501  C CE2 . TYR   A 1 61  ? -19.268 -19.957 26.852 1.00 63.82  ? 136 TYR   A CE2 1 
ATOM   502  C CZ  . TYR   A 1 61  ? -19.504 -19.049 25.842 1.00 60.46  ? 136 TYR   A CZ  1 
ATOM   503  O OH  . TYR   A 1 61  ? -20.762 -18.954 25.293 1.00 71.49  ? 136 TYR   A OH  1 
ATOM   504  N N   . ALA   A 1 62  ? -12.621 -19.131 27.515 1.00 50.85  ? 137 ALA   A N   1 
ATOM   505  C CA  . ALA   A 1 62  ? -11.400 -18.908 28.274 1.00 36.52  ? 137 ALA   A CA  1 
ATOM   506  C C   . ALA   A 1 62  ? -11.654 -17.790 29.268 1.00 36.96  ? 137 ALA   A C   1 
ATOM   507  O O   . ALA   A 1 62  ? -12.106 -16.706 28.882 1.00 49.99  ? 137 ALA   A O   1 
ATOM   508  C CB  . ALA   A 1 62  ? -10.229 -18.541 27.359 1.00 42.03  ? 137 ALA   A CB  1 
ATOM   509  N N   . VAL   A 1 63  ? -11.363 -18.046 30.539 1.00 35.88  ? 138 VAL   A N   1 
ATOM   510  C CA  . VAL   A 1 63  ? -11.607 -17.082 31.603 1.00 33.41  ? 138 VAL   A CA  1 
ATOM   511  C C   . VAL   A 1 63  ? -10.278 -16.706 32.240 1.00 42.23  ? 138 VAL   A C   1 
ATOM   512  O O   . VAL   A 1 63  ? -9.495  -17.584 32.621 1.00 52.09  ? 138 VAL   A O   1 
ATOM   513  C CB  . VAL   A 1 63  ? -12.580 -17.638 32.654 1.00 43.58  ? 138 VAL   A CB  1 
ATOM   514  C CG1 . VAL   A 1 63  ? -12.715 -16.664 33.801 1.00 41.16  ? 138 VAL   A CG1 1 
ATOM   515  C CG2 . VAL   A 1 63  ? -13.933 -17.913 32.019 1.00 52.40  ? 138 VAL   A CG2 1 
ATOM   516  N N   . LYS   A 1 64  ? -10.030 -15.403 32.357 1.00 49.94  ? 139 LYS   A N   1 
ATOM   517  C CA  . LYS   A 1 64  ? -8.851  -14.862 33.021 1.00 41.96  ? 139 LYS   A CA  1 
ATOM   518  C C   . LYS   A 1 64  ? -9.271  -14.175 34.313 1.00 43.48  ? 139 LYS   A C   1 
ATOM   519  O O   . LYS   A 1 64  ? -10.217 -13.380 34.317 1.00 52.97  ? 139 LYS   A O   1 
ATOM   520  C CB  . LYS   A 1 64  ? -8.115  -13.871 32.113 1.00 30.74  ? 139 LYS   A CB  1 
ATOM   521  C CG  . LYS   A 1 64  ? -7.073  -13.027 32.836 1.00 48.17  ? 139 LYS   A CG  1 
ATOM   522  C CD  . LYS   A 1 64  ? -6.135  -12.319 31.870 1.00 47.10  ? 139 LYS   A CD  1 
ATOM   523  C CE  . LYS   A 1 64  ? -6.886  -11.374 30.949 1.00 53.89  ? 139 LYS   A CE  1 
ATOM   524  N NZ  . LYS   A 1 64  ? -5.973  -10.722 29.968 1.00 56.17  ? 139 LYS   A NZ  1 
ATOM   525  N N   . ARG   A 1 65  ? -8.572  -14.480 35.407 1.00 45.09  ? 140 ARG   A N   1 
ATOM   526  C CA  . ARG   A 1 65  ? -8.816  -13.825 36.684 1.00 39.49  ? 140 ARG   A CA  1 
ATOM   527  C C   . ARG   A 1 65  ? -7.515  -13.242 37.214 1.00 40.42  ? 140 ARG   A C   1 
ATOM   528  O O   . ARG   A 1 65  ? -6.428  -13.753 36.935 1.00 64.21  ? 140 ARG   A O   1 
ATOM   529  C CB  . ARG   A 1 65  ? -9.422  -14.789 37.715 1.00 48.76  ? 140 ARG   A CB  1 
ATOM   530  C CG  . ARG   A 1 65  ? -8.458  -15.823 38.254 1.00 59.69  ? 140 ARG   A CG  1 
ATOM   531  C CD  . ARG   A 1 65  ? -9.157  -16.758 39.227 1.00 47.82  ? 140 ARG   A CD  1 
ATOM   532  N NE  . ARG   A 1 65  ? -8.238  -17.745 39.780 1.00 72.14  ? 140 ARG   A NE  1 
ATOM   533  C CZ  . ARG   A 1 65  ? -8.611  -18.809 40.479 1.00 69.70  ? 140 ARG   A CZ  1 
ATOM   534  N NH1 . ARG   A 1 65  ? -9.887  -19.073 40.710 1.00 81.40  ? 140 ARG   A NH1 1 
ATOM   535  N NH2 . ARG   A 1 65  ? -7.679  -19.629 40.957 1.00 71.23  ? 140 ARG   A NH2 1 
ATOM   536  N N   . SER   A 1 66  ? -7.636  -12.154 37.971 1.00 52.57  ? 141 SER   A N   1 
ATOM   537  C CA  . SER   A 1 66  ? -6.472  -11.504 38.550 1.00 57.04  ? 141 SER   A CA  1 
ATOM   538  C C   . SER   A 1 66  ? -5.966  -12.290 39.754 1.00 45.44  ? 141 SER   A C   1 
ATOM   539  O O   . SER   A 1 66  ? -6.719  -13.013 40.411 1.00 51.33  ? 141 SER   A O   1 
ATOM   540  C CB  . SER   A 1 66  ? -6.805  -10.067 38.953 1.00 56.08  ? 141 SER   A CB  1 
ATOM   541  O OG  . SER   A 1 66  ? -7.997  -10.017 39.715 1.00 48.54  ? 141 SER   A OG  1 
ATOM   542  N N   . MET   A 1 67  ? -4.670  -12.139 40.039 1.00 58.54  ? 142 MET   A N   1 
ATOM   543  C CA  . MET   A 1 67  ? -4.028  -12.951 41.070 1.00 52.74  ? 142 MET   A CA  1 
ATOM   544  C C   . MET   A 1 67  ? -4.545  -12.598 42.459 1.00 71.87  ? 142 MET   A C   1 
ATOM   545  O O   . MET   A 1 67  ? -5.040  -13.463 43.191 1.00 80.56  ? 142 MET   A O   1 
ATOM   546  C CB  . MET   A 1 67  ? -2.509  -12.775 40.999 1.00 82.53  ? 142 MET   A CB  1 
ATOM   547  C CG  . MET   A 1 67  ? -1.742  -13.541 42.067 1.00 91.41  ? 142 MET   A CG  1 
ATOM   548  S SD  . MET   A 1 67  ? -1.735  -15.319 41.777 1.00 127.10 ? 142 MET   A SD  1 
ATOM   549  C CE  . MET   A 1 67  ? -0.795  -15.405 40.254 1.00 89.58  ? 142 MET   A CE  1 
ATOM   550  N N   . SER   A 1 68  ? -4.435  -11.332 42.839 1.00 61.21  ? 143 SER   A N   1 
ATOM   551  C CA  . SER   A 1 68  ? -4.776  -10.872 44.173 1.00 60.74  ? 143 SER   A CA  1 
ATOM   552  C C   . SER   A 1 68  ? -5.964  -9.918  44.138 1.00 56.10  ? 143 SER   A C   1 
ATOM   553  O O   . SER   A 1 68  ? -6.248  -9.296  43.108 1.00 58.77  ? 143 SER   A O   1 
ATOM   554  C CB  . SER   A 1 68  ? -3.574  -10.167 44.815 1.00 76.95  ? 143 SER   A CB  1 
ATOM   555  O OG  . SER   A 1 68  ? -3.138  -9.089  44.007 1.00 96.38  ? 143 SER   A OG  1 
ATOM   556  N N   . PRO   A 1 69  ? -6.684  -9.778  45.253 1.00 63.14  ? 144 PRO   A N   1 
ATOM   557  C CA  . PRO   A 1 69  ? -7.771  -8.793  45.315 1.00 50.03  ? 144 PRO   A CA  1 
ATOM   558  C C   . PRO   A 1 69  ? -7.261  -7.380  45.079 1.00 60.48  ? 144 PRO   A C   1 
ATOM   559  O O   . PRO   A 1 69  ? -6.065  -7.090  45.142 1.00 68.69  ? 144 PRO   A O   1 
ATOM   560  C CB  . PRO   A 1 69  ? -8.321  -8.961  46.735 1.00 46.17  ? 144 PRO   A CB  1 
ATOM   561  C CG  . PRO   A 1 69  ? -7.976  -10.363 47.105 1.00 51.44  ? 144 PRO   A CG  1 
ATOM   562  C CD  . PRO   A 1 69  ? -6.652  -10.639 46.449 1.00 54.35  ? 144 PRO   A CD  1 
ATOM   563  N N   . PHE   A 1 70  ? -8.205  -6.484  44.794 1.00 68.90  ? 145 PHE   A N   1 
ATOM   564  C CA  . PHE   A 1 70  ? -7.864  -5.122  44.406 1.00 44.21  ? 145 PHE   A CA  1 
ATOM   565  C C   . PHE   A 1 70  ? -7.073  -4.419  45.500 1.00 55.46  ? 145 PHE   A C   1 
ATOM   566  O O   . PHE   A 1 70  ? -7.504  -4.358  46.656 1.00 51.02  ? 145 PHE   A O   1 
ATOM   567  C CB  . PHE   A 1 70  ? -9.132  -4.334  44.088 1.00 46.71  ? 145 PHE   A CB  1 
ATOM   568  C CG  . PHE   A 1 70  ? -9.832  -4.796  42.848 1.00 49.72  ? 145 PHE   A CG  1 
ATOM   569  C CD1 . PHE   A 1 70  ? -9.110  -5.108  41.708 1.00 42.66  ? 145 PHE   A CD1 1 
ATOM   570  C CD2 . PHE   A 1 70  ? -11.212 -4.929  42.822 1.00 40.63  ? 145 PHE   A CD2 1 
ATOM   571  C CE1 . PHE   A 1 70  ? -9.750  -5.536  40.559 1.00 33.80  ? 145 PHE   A CE1 1 
ATOM   572  C CE2 . PHE   A 1 70  ? -11.861 -5.359  41.675 1.00 42.15  ? 145 PHE   A CE2 1 
ATOM   573  C CZ  . PHE   A 1 70  ? -11.129 -5.663  40.542 1.00 42.76  ? 145 PHE   A CZ  1 
ATOM   574  N N   . ARG   A 1 71  ? -5.908  -3.886  45.122 1.00 60.08  ? 146 ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 71  ? -5.087  -3.126  46.058 1.00 54.49  ? 146 ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 71  ? -5.751  -1.810  46.447 1.00 63.98  ? 146 ARG   A C   1 
ATOM   577  O O   . ARG   A 1 71  ? -5.574  -1.335  47.575 1.00 62.67  ? 146 ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 71  ? -3.706  -2.878  45.445 1.00 68.56  ? 146 ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 71  ? -2.773  -2.000  46.268 1.00 73.36  ? 146 ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 71  ? -1.442  -1.796  45.553 1.00 90.63  ? 146 ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 71  ? -1.602  -1.201  44.230 1.00 103.41 ? 146 ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 71  ? -1.446  0.089   43.961 1.00 98.44  ? 146 ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 71  ? -1.122  0.959   44.905 1.00 81.53  ? 146 ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 71  ? -1.617  0.517   42.713 1.00 67.43  ? 146 ARG   A NH2 1 
ATOM   585  N N   . GLY   A 1 72  ? -6.527  -1.219  45.542 1.00 50.29  ? 147 GLY   A N   1 
ATOM   586  C CA  . GLY   A 1 72  ? -7.195  0.032   45.808 1.00 40.23  ? 147 GLY   A CA  1 
ATOM   587  C C   . GLY   A 1 72  ? -7.975  0.509   44.600 1.00 45.64  ? 147 GLY   A C   1 
ATOM   588  O O   . GLY   A 1 72  ? -8.132  -0.218  43.612 1.00 46.32  ? 147 GLY   A O   1 
ATOM   589  N N   . PRO   A 1 73  ? -8.485  1.745   44.659 1.00 43.24  ? 148 PRO   A N   1 
ATOM   590  C CA  . PRO   A 1 73  ? -9.257  2.271   43.520 1.00 32.44  ? 148 PRO   A CA  1 
ATOM   591  C C   . PRO   A 1 73  ? -8.448  2.389   42.243 1.00 36.79  ? 148 PRO   A C   1 
ATOM   592  O O   . PRO   A 1 73  ? -8.954  2.047   41.167 1.00 42.66  ? 148 PRO   A O   1 
ATOM   593  C CB  . PRO   A 1 73  ? -9.721  3.646   44.022 1.00 36.53  ? 148 PRO   A CB  1 
ATOM   594  C CG  . PRO   A 1 73  ? -9.693  3.536   45.496 1.00 30.05  ? 148 PRO   A CG  1 
ATOM   595  C CD  . PRO   A 1 73  ? -8.515  2.661   45.809 1.00 37.07  ? 148 PRO   A CD  1 
ATOM   596  N N   . LYS   A 1 74  ? -7.205  2.875   42.326 1.00 49.94  ? 149 LYS   A N   1 
ATOM   597  C CA  . LYS   A 1 74  ? -6.375  2.959   41.129 1.00 47.94  ? 149 LYS   A CA  1 
ATOM   598  C C   . LYS   A 1 74  ? -6.085  1.573   40.568 1.00 42.25  ? 149 LYS   A C   1 
ATOM   599  O O   . LYS   A 1 74  ? -6.140  1.364   39.350 1.00 47.86  ? 149 LYS   A O   1 
ATOM   600  C CB  . LYS   A 1 74  ? -5.072  3.701   41.432 1.00 55.92  ? 149 LYS   A CB  1 
ATOM   601  C CG  . LYS   A 1 74  ? -5.257  5.175   41.779 1.00 66.38  ? 149 LYS   A CG  1 
ATOM   602  C CD  . LYS   A 1 74  ? -3.996  6.008   41.512 1.00 98.64  ? 149 LYS   A CD  1 
ATOM   603  C CE  . LYS   A 1 74  ? -2.895  5.796   42.554 1.00 73.71  ? 149 LYS   A CE  1 
ATOM   604  N NZ  . LYS   A 1 74  ? -2.071  4.577   42.310 1.00 65.78  ? 149 LYS   A NZ  1 
ATOM   605  N N   . ASP   A 1 75  ? -5.784  0.609   41.440 1.00 49.32  ? 150 ASP   A N   1 
ATOM   606  C CA  . ASP   A 1 75  ? -5.536  -0.751  40.969 1.00 42.65  ? 150 ASP   A CA  1 
ATOM   607  C C   . ASP   A 1 75  ? -6.790  -1.352  40.351 1.00 42.75  ? 150 ASP   A C   1 
ATOM   608  O O   . ASP   A 1 75  ? -6.713  -2.059  39.339 1.00 54.47  ? 150 ASP   A O   1 
ATOM   609  C CB  . ASP   A 1 75  ? -5.032  -1.622  42.118 1.00 56.77  ? 150 ASP   A CB  1 
ATOM   610  C CG  . ASP   A 1 75  ? -4.731  -3.044  41.684 1.00 61.26  ? 150 ASP   A CG  1 
ATOM   611  O OD1 . ASP   A 1 75  ? -3.773  -3.242  40.903 1.00 86.28  ? 150 ASP   A OD1 1 
ATOM   612  O OD2 . ASP   A 1 75  ? -5.448  -3.965  42.129 1.00 66.43  ? 150 ASP   A OD2 1 
ATOM   613  N N   . ARG   A 1 76  ? -7.954  -1.075  40.941 1.00 40.32  ? 151 ARG   A N   1 
ATOM   614  C CA  . ARG   A 1 76  ? -9.207  -1.580  40.389 1.00 31.86  ? 151 ARG   A CA  1 
ATOM   615  C C   . ARG   A 1 76  ? -9.498  -0.964  39.025 1.00 37.51  ? 151 ARG   A C   1 
ATOM   616  O O   . ARG   A 1 76  ? -9.860  -1.672  38.079 1.00 45.05  ? 151 ARG   A O   1 
ATOM   617  C CB  . ARG   A 1 76  ? -10.356 -1.304  41.357 1.00 39.80  ? 151 ARG   A CB  1 
ATOM   618  C CG  . ARG   A 1 76  ? -11.719 -1.654  40.792 1.00 37.69  ? 151 ARG   A CG  1 
ATOM   619  C CD  . ARG   A 1 76  ? -12.813 -1.407  41.807 1.00 41.90  ? 151 ARG   A CD  1 
ATOM   620  N NE  . ARG   A 1 76  ? -14.120 -1.819  41.311 1.00 53.20  ? 151 ARG   A NE  1 
ATOM   621  C CZ  . ARG   A 1 76  ? -14.987 -1.004  40.728 1.00 45.19  ? 151 ARG   A CZ  1 
ATOM   622  N NH1 . ARG   A 1 76  ? -14.717 0.279   40.554 1.00 51.58  ? 151 ARG   A NH1 1 
ATOM   623  N NH2 . ARG   A 1 76  ? -16.152 -1.489  40.308 1.00 58.09  ? 151 ARG   A NH2 1 
ATOM   624  N N   . ALA   A 1 77  ? -9.353  0.360   38.906 1.00 40.96  ? 152 ALA   A N   1 
ATOM   625  C CA  . ALA   A 1 77  ? -9.586  1.021   37.625 1.00 31.62  ? 152 ALA   A CA  1 
ATOM   626  C C   . ALA   A 1 77  ? -8.591  0.565   36.567 1.00 39.27  ? 152 ALA   A C   1 
ATOM   627  O O   . ALA   A 1 77  ? -8.934  0.494   35.381 1.00 43.27  ? 152 ALA   A O   1 
ATOM   628  C CB  . ALA   A 1 77  ? -9.516  2.538   37.794 1.00 36.55  ? 152 ALA   A CB  1 
ATOM   629  N N   . ARG   A 1 78  ? -7.355  0.264   36.966 1.00 37.39  ? 153 ARG   A N   1 
ATOM   630  C CA  . ARG   A 1 78  ? -6.377  -0.221  36.000 1.00 37.31  ? 153 ARG   A CA  1 
ATOM   631  C C   . ARG   A 1 78  ? -6.774  -1.592  35.465 1.00 42.16  ? 153 ARG   A C   1 
ATOM   632  O O   . ARG   A 1 78  ? -6.690  -1.843  34.257 1.00 42.30  ? 153 ARG   A O   1 
ATOM   633  C CB  . ARG   A 1 78  ? -4.988  -0.261  36.638 1.00 40.91  ? 153 ARG   A CB  1 
ATOM   634  C CG  . ARG   A 1 78  ? -3.852  -0.533  35.663 1.00 53.87  ? 153 ARG   A CG  1 
ATOM   635  C CD  . ARG   A 1 78  ? -2.487  -0.521  36.357 1.00 59.55  ? 153 ARG   A CD  1 
ATOM   636  N NE  . ARG   A 1 78  ? -2.189  0.756   36.999 1.00 67.91  ? 153 ARG   A NE  1 
ATOM   637  C CZ  . ARG   A 1 78  ? -2.163  0.953   38.311 1.00 67.60  ? 153 ARG   A CZ  1 
ATOM   638  N NH1 . ARG   A 1 78  ? -2.394  -0.032  39.166 1.00 63.92  ? 153 ARG   A NH1 1 
ATOM   639  N NH2 . ARG   A 1 78  ? -1.896  2.169   38.779 1.00 65.56  ? 153 ARG   A NH2 1 
ATOM   640  N N   . LYS   A 1 79  ? -7.229  -2.487  36.343 1.00 40.83  ? 154 LYS   A N   1 
ATOM   641  C CA  . LYS   A 1 79  ? -7.649  -3.806  35.884 1.00 34.17  ? 154 LYS   A CA  1 
ATOM   642  C C   . LYS   A 1 79  ? -8.961  -3.735  35.111 1.00 32.88  ? 154 LYS   A C   1 
ATOM   643  O O   . LYS   A 1 79  ? -9.132  -4.430  34.104 1.00 49.21  ? 154 LYS   A O   1 
ATOM   644  C CB  . LYS   A 1 79  ? -7.770  -4.763  37.071 1.00 34.68  ? 154 LYS   A CB  1 
ATOM   645  C CG  . LYS   A 1 79  ? -6.456  -4.999  37.807 1.00 37.21  ? 154 LYS   A CG  1 
ATOM   646  C CD  . LYS   A 1 79  ? -6.618  -5.998  38.946 1.00 41.96  ? 154 LYS   A CD  1 
ATOM   647  C CE  . LYS   A 1 79  ? -5.305  -6.214  39.690 1.00 58.29  ? 154 LYS   A CE  1 
ATOM   648  N NZ  . LYS   A 1 79  ? -5.431  -7.236  40.768 1.00 65.87  ? 154 LYS   A NZ  1 
ATOM   649  N N   . LEU   A 1 80  ? -9.901  -2.902  35.561 1.00 41.67  ? 155 LEU   A N   1 
ATOM   650  C CA  . LEU   A 1 80  ? -11.166 -2.760  34.847 1.00 35.12  ? 155 LEU   A CA  1 
ATOM   651  C C   . LEU   A 1 80  ? -10.999 -2.079  33.495 1.00 40.77  ? 155 LEU   A C   1 
ATOM   652  O O   . LEU   A 1 80  ? -11.897 -2.176  32.652 1.00 39.60  ? 155 LEU   A O   1 
ATOM   653  C CB  . LEU   A 1 80  ? -12.166 -1.970  35.692 1.00 35.70  ? 155 LEU   A CB  1 
ATOM   654  C CG  . LEU   A 1 80  ? -12.746 -2.645  36.936 1.00 47.90  ? 155 LEU   A CG  1 
ATOM   655  C CD1 . LEU   A 1 80  ? -13.731 -1.723  37.627 1.00 56.56  ? 155 LEU   A CD1 1 
ATOM   656  C CD2 . LEU   A 1 80  ? -13.425 -3.938  36.562 1.00 43.23  ? 155 LEU   A CD2 1 
ATOM   657  N N   . ALA   A 1 81  ? -9.881  -1.388  33.272 1.00 50.27  ? 156 ALA   A N   1 
ATOM   658  C CA  . ALA   A 1 81  ? -9.692  -0.690  32.007 1.00 32.99  ? 156 ALA   A CA  1 
ATOM   659  C C   . ALA   A 1 81  ? -9.626  -1.661  30.833 1.00 39.07  ? 156 ALA   A C   1 
ATOM   660  O O   . ALA   A 1 81  ? -9.997  -1.299  29.710 1.00 43.61  ? 156 ALA   A O   1 
ATOM   661  C CB  . ALA   A 1 81  ? -8.425  0.165   32.067 1.00 34.38  ? 156 ALA   A CB  1 
ATOM   662  N N   . GLU   A 1 82  ? -9.168  -2.895  31.071 1.00 37.55  ? 157 GLU   A N   1 
ATOM   663  C CA  . GLU   A 1 82  ? -9.104  -3.877  29.993 1.00 34.24  ? 157 GLU   A CA  1 
ATOM   664  C C   . GLU   A 1 82  ? -10.492 -4.218  29.472 1.00 38.23  ? 157 GLU   A C   1 
ATOM   665  O O   . GLU   A 1 82  ? -10.659 -4.489  28.277 1.00 47.81  ? 157 GLU   A O   1 
ATOM   666  C CB  . GLU   A 1 82  ? -8.387  -5.141  30.470 1.00 38.41  ? 157 GLU   A CB  1 
ATOM   667  C CG  . GLU   A 1 82  ? -8.275  -6.244  29.419 1.00 53.48  ? 157 GLU   A CG  1 
ATOM   668  C CD  . GLU   A 1 82  ? -7.370  -7.388  29.855 1.00 66.34  ? 157 GLU   A CD  1 
ATOM   669  O OE1 . GLU   A 1 82  ? -6.702  -7.259  30.903 1.00 61.23  ? 157 GLU   A OE1 1 
ATOM   670  O OE2 . GLU   A 1 82  ? -7.325  -8.418  29.147 1.00 49.01  ? 157 GLU   A OE2 1 
ATOM   671  N N   . VAL   A 1 83  ? -11.498 -4.208  30.347 1.00 43.16  ? 158 VAL   A N   1 
ATOM   672  C CA  . VAL   A 1 83  ? -12.863 -4.448  29.894 1.00 31.70  ? 158 VAL   A CA  1 
ATOM   673  C C   . VAL   A 1 83  ? -13.336 -3.298  29.017 1.00 34.62  ? 158 VAL   A C   1 
ATOM   674  O O   . VAL   A 1 83  ? -13.936 -3.513  27.958 1.00 44.96  ? 158 VAL   A O   1 
ATOM   675  C CB  . VAL   A 1 83  ? -13.796 -4.663  31.096 1.00 38.62  ? 158 VAL   A CB  1 
ATOM   676  C CG1 . VAL   A 1 83  ? -15.209 -4.956  30.617 1.00 30.67  ? 158 VAL   A CG1 1 
ATOM   677  C CG2 . VAL   A 1 83  ? -13.274 -5.790  31.963 1.00 43.53  ? 158 VAL   A CG2 1 
ATOM   678  N N   . GLY   A 1 84  ? -13.070 -2.060  29.440 1.00 41.21  ? 159 GLY   A N   1 
ATOM   679  C CA  . GLY   A 1 84  ? -13.422 -0.916  28.619 1.00 38.71  ? 159 GLY   A CA  1 
ATOM   680  C C   . GLY   A 1 84  ? -12.697 -0.898  27.289 1.00 35.53  ? 159 GLY   A C   1 
ATOM   681  O O   . GLY   A 1 84  ? -13.254 -0.461  26.280 1.00 49.32  ? 159 GLY   A O   1 
ATOM   682  N N   . SER   A 1 85  ? -11.450 -1.377  27.265 1.00 43.64  ? 160 SER   A N   1 
ATOM   683  C CA  . SER   A 1 85  ? -10.706 -1.441  26.011 1.00 33.58  ? 160 SER   A CA  1 
ATOM   684  C C   . SER   A 1 85  ? -11.328 -2.447  25.049 1.00 45.71  ? 160 SER   A C   1 
ATOM   685  O O   . SER   A 1 85  ? -11.390 -2.199  23.839 1.00 54.75  ? 160 SER   A O   1 
ATOM   686  C CB  . SER   A 1 85  ? -9.248  -1.794  26.293 1.00 41.45  ? 160 SER   A CB  1 
ATOM   687  O OG  . SER   A 1 85  ? -8.666  -0.830  27.152 1.00 50.25  ? 160 SER   A OG  1 
ATOM   688  N N   . HIS   A 1 86  ? -11.784 -3.591  25.564 1.00 51.47  ? 161 HIS   A N   1 
ATOM   689  C CA  . HIS   A 1 86  ? -12.497 -4.551  24.726 1.00 38.70  ? 161 HIS   A CA  1 
ATOM   690  C C   . HIS   A 1 86  ? -13.771 -3.946  24.150 1.00 51.55  ? 161 HIS   A C   1 
ATOM   691  O O   . HIS   A 1 86  ? -14.142 -4.232  23.004 1.00 49.59  ? 161 HIS   A O   1 
ATOM   692  C CB  . HIS   A 1 86  ? -12.826 -5.802  25.534 1.00 53.28  ? 161 HIS   A CB  1 
ATOM   693  C CG  . HIS   A 1 86  ? -11.860 -6.926  25.335 1.00 42.02  ? 161 HIS   A CG  1 
ATOM   694  N ND1 . HIS   A 1 86  ? -12.009 -7.864  24.337 1.00 42.87  ? 161 HIS   A ND1 1 
ATOM   695  C CD2 . HIS   A 1 86  ? -10.743 -7.275  26.016 1.00 37.66  ? 161 HIS   A CD2 1 
ATOM   696  C CE1 . HIS   A 1 86  ? -11.023 -8.740  24.407 1.00 50.47  ? 161 HIS   A CE1 1 
ATOM   697  N NE2 . HIS   A 1 86  ? -10.241 -8.405  25.417 1.00 56.19  ? 161 HIS   A NE2 1 
ATOM   698  N N   . GLU   A 1 87  ? -14.458 -3.120  24.940 1.00 54.87  ? 162 GLU   A N   1 
ATOM   699  C CA  . GLU   A 1 87  ? -15.691 -2.489  24.484 1.00 52.54  ? 162 GLU   A CA  1 
ATOM   700  C C   . GLU   A 1 87  ? -15.424 -1.487  23.365 1.00 59.46  ? 162 GLU   A C   1 
ATOM   701  O O   . GLU   A 1 87  ? -16.239 -1.343  22.447 1.00 57.19  ? 162 GLU   A O   1 
ATOM   702  C CB  . GLU   A 1 87  ? -16.376 -1.814  25.672 1.00 60.17  ? 162 GLU   A CB  1 
ATOM   703  C CG  . GLU   A 1 87  ? -17.386 -0.735  25.334 1.00 65.70  ? 162 GLU   A CG  1 
ATOM   704  C CD  . GLU   A 1 87  ? -17.662 0.178   26.514 1.00 89.12  ? 162 GLU   A CD  1 
ATOM   705  O OE1 . GLU   A 1 87  ? -16.708 0.821   27.002 1.00 92.32  ? 162 GLU   A OE1 1 
ATOM   706  O OE2 . GLU   A 1 87  ? -18.828 0.241   26.960 1.00 95.07  ? 162 GLU   A OE2 1 
ATOM   707  N N   . LYS   A 1 88  ? -14.279 -0.799  23.413 1.00 54.89  ? 163 LYS   A N   1 
ATOM   708  C CA  . LYS   A 1 88  ? -13.957 0.169   22.371 1.00 46.45  ? 163 LYS   A CA  1 
ATOM   709  C C   . LYS   A 1 88  ? -13.534 -0.530  21.087 1.00 51.90  ? 163 LYS   A C   1 
ATOM   710  O O   . LYS   A 1 88  ? -13.841 -0.058  19.987 1.00 53.95  ? 163 LYS   A O   1 
ATOM   711  C CB  . LYS   A 1 88  ? -12.859 1.111   22.859 1.00 44.27  ? 163 LYS   A CB  1 
ATOM   712  C CG  . LYS   A 1 88  ? -13.246 1.953   24.071 1.00 55.03  ? 163 LYS   A CG  1 
ATOM   713  C CD  . LYS   A 1 88  ? -12.046 2.711   24.623 1.00 65.77  ? 163 LYS   A CD  1 
ATOM   714  C CE  . LYS   A 1 88  ? -12.381 3.394   25.939 1.00 71.45  ? 163 LYS   A CE  1 
ATOM   715  N NZ  . LYS   A 1 88  ? -11.173 3.982   26.581 1.00 75.28  ? 163 LYS   A NZ  1 
ATOM   716  N N   . VAL   A 1 89  ? -12.824 -1.655  21.209 1.00 42.22  ? 164 VAL   A N   1 
ATOM   717  C CA  . VAL   A 1 89  ? -12.423 -2.413  20.027 1.00 42.49  ? 164 VAL   A CA  1 
ATOM   718  C C   . VAL   A 1 89  ? -13.647 -2.959  19.305 1.00 50.16  ? 164 VAL   A C   1 
ATOM   719  O O   . VAL   A 1 89  ? -13.718 -2.944  18.070 1.00 59.73  ? 164 VAL   A O   1 
ATOM   720  C CB  . VAL   A 1 89  ? -11.451 -3.542  20.419 1.00 35.20  ? 164 VAL   A CB  1 
ATOM   721  C CG1 . VAL   A 1 89  ? -11.190 -4.451  19.235 1.00 43.17  ? 164 VAL   A CG1 1 
ATOM   722  C CG2 . VAL   A 1 89  ? -10.147 -2.965  20.942 1.00 39.78  ? 164 VAL   A CG2 1 
ATOM   723  N N   . GLY   A 1 90  ? -14.630 -3.442  20.058 1.00 49.84  ? 165 GLY   A N   1 
ATOM   724  C CA  . GLY   A 1 90  ? -15.816 -4.002  19.449 1.00 41.48  ? 165 GLY   A CA  1 
ATOM   725  C C   . GLY   A 1 90  ? -15.571 -5.401  18.911 1.00 49.02  ? 165 GLY   A C   1 
ATOM   726  O O   . GLY   A 1 90  ? -14.614 -6.090  19.280 1.00 70.80  ? 165 GLY   A O   1 
ATOM   727  N N   . GLN   A 1 91  ? -16.457 -5.819  18.014 1.00 60.41  ? 166 GLN   A N   1 
ATOM   728  C CA  . GLN   A 1 91  ? -16.398 -7.148  17.423 1.00 57.82  ? 166 GLN   A CA  1 
ATOM   729  C C   . GLN   A 1 91  ? -15.767 -7.076  16.040 1.00 50.23  ? 166 GLN   A C   1 
ATOM   730  O O   . GLN   A 1 91  ? -16.195 -6.286  15.191 1.00 58.09  ? 166 GLN   A O   1 
ATOM   731  C CB  . GLN   A 1 91  ? -17.789 -7.774  17.340 1.00 52.41  ? 166 GLN   A CB  1 
ATOM   732  C CG  . GLN   A 1 91  ? -18.361 -8.132  18.702 1.00 61.37  ? 166 GLN   A CG  1 
ATOM   733  C CD  . GLN   A 1 91  ? -19.758 -8.710  18.613 1.00 98.36  ? 166 GLN   A CD  1 
ATOM   734  O OE1 . GLN   A 1 91  ? -20.475 -8.488  17.637 1.00 127.42 ? 166 GLN   A OE1 1 
ATOM   735  N NE2 . GLN   A 1 91  ? -20.154 -9.456  19.635 1.00 103.58 ? 166 GLN   A NE2 1 
ATOM   736  N N   . HIS   A 1 92  ? -14.748 -7.907  15.820 1.00 53.46  ? 167 HIS   A N   1 
ATOM   737  C CA  . HIS   A 1 92  ? -14.031 -7.987  14.560 1.00 47.40  ? 167 HIS   A CA  1 
ATOM   738  C C   . HIS   A 1 92  ? -13.501 -9.409  14.466 1.00 49.39  ? 167 HIS   A C   1 
ATOM   739  O O   . HIS   A 1 92  ? -13.058 -9.960  15.483 1.00 49.38  ? 167 HIS   A O   1 
ATOM   740  C CB  . HIS   A 1 92  ? -12.880 -6.977  14.489 1.00 50.52  ? 167 HIS   A CB  1 
ATOM   741  C CG  . HIS   A 1 92  ? -12.233 -6.882  13.143 1.00 43.20  ? 167 HIS   A CG  1 
ATOM   742  N ND1 . HIS   A 1 92  ? -11.159 -7.666  12.778 1.00 48.00  ? 167 HIS   A ND1 1 
ATOM   743  C CD2 . HIS   A 1 92  ? -12.500 -6.090  12.077 1.00 43.28  ? 167 HIS   A CD2 1 
ATOM   744  C CE1 . HIS   A 1 92  ? -10.794 -7.364  11.545 1.00 46.74  ? 167 HIS   A CE1 1 
ATOM   745  N NE2 . HIS   A 1 92  ? -11.592 -6.410  11.097 1.00 52.96  ? 167 HIS   A NE2 1 
ATOM   746  N N   . PRO   A 1 93  ? -13.540 -10.032 13.288 1.00 45.48  ? 168 PRO   A N   1 
ATOM   747  C CA  . PRO   A 1 93  ? -13.089 -11.428 13.182 1.00 45.83  ? 168 PRO   A CA  1 
ATOM   748  C C   . PRO   A 1 93  ? -11.640 -11.633 13.577 1.00 57.09  ? 168 PRO   A C   1 
ATOM   749  O O   . PRO   A 1 93  ? -11.258 -12.765 13.906 1.00 67.92  ? 168 PRO   A O   1 
ATOM   750  C CB  . PRO   A 1 93  ? -13.311 -11.753 11.700 1.00 41.76  ? 168 PRO   A CB  1 
ATOM   751  C CG  . PRO   A 1 93  ? -14.335 -10.774 11.242 1.00 45.61  ? 168 PRO   A CG  1 
ATOM   752  C CD  . PRO   A 1 93  ? -14.066 -9.522  12.016 1.00 42.76  ? 168 PRO   A CD  1 
ATOM   753  N N   . CYS   A 1 94  ? -10.817 -10.585 13.556 1.00 49.81  ? 169 CYS   A N   1 
ATOM   754  C CA  . CYS   A 1 94  ? -9.402  -10.694 13.877 1.00 49.14  ? 169 CYS   A CA  1 
ATOM   755  C C   . CYS   A 1 94  ? -9.081  -10.201 15.281 1.00 43.51  ? 169 CYS   A C   1 
ATOM   756  O O   . CYS   A 1 94  ? -7.914  -9.925  15.581 1.00 42.72  ? 169 CYS   A O   1 
ATOM   757  C CB  . CYS   A 1 94  ? -8.571  -9.931  12.849 1.00 43.95  ? 169 CYS   A CB  1 
ATOM   758  S SG  . CYS   A 1 94  ? -8.733  -10.567 11.173 1.00 58.34  ? 169 CYS   A SG  1 
ATOM   759  N N   . CYS   A 1 95  ? -10.085 -10.088 16.145 1.00 44.66  ? 170 CYS   A N   1 
ATOM   760  C CA  . CYS   A 1 95  ? -9.887  -9.657  17.520 1.00 35.58  ? 170 CYS   A CA  1 
ATOM   761  C C   . CYS   A 1 95  ? -10.596 -10.621 18.458 1.00 37.58  ? 170 CYS   A C   1 
ATOM   762  O O   . CYS   A 1 95  ? -11.724 -11.045 18.187 1.00 49.84  ? 170 CYS   A O   1 
ATOM   763  C CB  . CYS   A 1 95  ? -10.406 -8.233  17.739 1.00 48.74  ? 170 CYS   A CB  1 
ATOM   764  S SG  . CYS   A 1 95  ? -9.582  -6.983  16.728 1.00 58.59  ? 170 CYS   A SG  1 
ATOM   765  N N   . VAL   A 1 96  ? -9.925  -10.965 19.560 1.00 42.95  ? 171 VAL   A N   1 
ATOM   766  C CA  . VAL   A 1 96  ? -10.501 -11.882 20.539 1.00 42.51  ? 171 VAL   A CA  1 
ATOM   767  C C   . VAL   A 1 96  ? -11.775 -11.271 21.105 1.00 43.82  ? 171 VAL   A C   1 
ATOM   768  O O   . VAL   A 1 96  ? -11.760 -10.161 21.652 1.00 50.32  ? 171 VAL   A O   1 
ATOM   769  C CB  . VAL   A 1 96  ? -9.492  -12.192 21.650 1.00 41.69  ? 171 VAL   A CB  1 
ATOM   770  C CG1 . VAL   A 1 96  ? -10.132 -13.074 22.708 1.00 52.97  ? 171 VAL   A CG1 1 
ATOM   771  C CG2 . VAL   A 1 96  ? -8.251  -12.859 21.077 1.00 44.77  ? 171 VAL   A CG2 1 
ATOM   772  N N   . ARG   A 1 97  ? -12.883 -11.995 20.983 1.00 42.73  ? 172 ARG   A N   1 
ATOM   773  C CA  . ARG   A 1 97  ? -14.176 -11.487 21.422 1.00 43.46  ? 172 ARG   A CA  1 
ATOM   774  C C   . ARG   A 1 97  ? -14.327 -11.633 22.931 1.00 46.69  ? 172 ARG   A C   1 
ATOM   775  O O   . ARG   A 1 97  ? -14.061 -12.701 23.491 1.00 50.15  ? 172 ARG   A O   1 
ATOM   776  C CB  . ARG   A 1 97  ? -15.306 -12.230 20.709 1.00 42.81  ? 172 ARG   A CB  1 
ATOM   777  C CG  . ARG   A 1 97  ? -16.696 -11.722 21.056 1.00 62.05  ? 172 ARG   A CG  1 
ATOM   778  C CD  . ARG   A 1 97  ? -17.779 -12.477 20.297 1.00 56.47  ? 172 ARG   A CD  1 
ATOM   779  N NE  . ARG   A 1 97  ? -17.947 -13.846 20.770 1.00 80.87  ? 172 ARG   A NE  1 
ATOM   780  C CZ  . ARG   A 1 97  ? -17.426 -14.915 20.182 1.00 86.47  ? 172 ARG   A CZ  1 
ATOM   781  N NH1 . ARG   A 1 97  ? -16.677 -14.812 19.096 1.00 95.65  ? 172 ARG   A NH1 1 
ATOM   782  N NH2 . ARG   A 1 97  ? -17.665 -16.119 20.695 1.00 73.40  ? 172 ARG   A NH2 1 
ATOM   783  N N   . LEU   A 1 98  ? -14.759 -10.558 23.588 1.00 43.26  ? 173 LEU   A N   1 
ATOM   784  C CA  . LEU   A 1 98  ? -15.075 -10.589 25.011 1.00 40.04  ? 173 LEU   A CA  1 
ATOM   785  C C   . LEU   A 1 98  ? -16.551 -10.929 25.184 1.00 56.82  ? 173 LEU   A C   1 
ATOM   786  O O   . LEU   A 1 98  ? -17.419 -10.230 24.649 1.00 55.90  ? 173 LEU   A O   1 
ATOM   787  C CB  . LEU   A 1 98  ? -14.760 -9.250  25.674 1.00 40.17  ? 173 LEU   A CB  1 
ATOM   788  C CG  . LEU   A 1 98  ? -15.036 -9.183  27.177 1.00 40.91  ? 173 LEU   A CG  1 
ATOM   789  C CD1 . LEU   A 1 98  ? -14.047 -10.051 27.931 1.00 47.61  ? 173 LEU   A CD1 1 
ATOM   790  C CD2 . LEU   A 1 98  ? -14.979 -7.750  27.674 1.00 37.80  ? 173 LEU   A CD2 1 
ATOM   791  N N   . GLU   A 1 99  ? -16.833 -11.995 25.933 1.00 51.37  ? 174 GLU   A N   1 
ATOM   792  C CA  . GLU   A 1 99  ? -18.216 -12.410 26.149 1.00 52.21  ? 174 GLU   A CA  1 
ATOM   793  C C   . GLU   A 1 99  ? -18.853 -11.635 27.297 1.00 51.95  ? 174 GLU   A C   1 
ATOM   794  O O   . GLU   A 1 99  ? -19.864 -10.950 27.110 1.00 55.82  ? 174 GLU   A O   1 
ATOM   795  C CB  . GLU   A 1 99  ? -18.278 -13.918 26.408 1.00 49.38  ? 174 GLU   A CB  1 
ATOM   796  C CG  . GLU   A 1 99  ? -18.008 -14.758 25.172 1.00 65.07  ? 174 GLU   A CG  1 
ATOM   797  C CD  . GLU   A 1 99  ? -19.118 -14.653 24.142 1.00 94.11  ? 174 GLU   A CD  1 
ATOM   798  O OE1 . GLU   A 1 99  ? -20.304 -14.660 24.539 1.00 88.49  ? 174 GLU   A OE1 1 
ATOM   799  O OE2 . GLU   A 1 99  ? -18.806 -14.559 22.935 1.00 86.09  ? 174 GLU   A OE2 1 
ATOM   800  N N   . GLN   A 1 100 ? -18.275 -11.733 28.492 1.00 46.08  ? 175 GLN   A N   1 
ATOM   801  C CA  . GLN   A 1 100 ? -18.788 -10.999 29.640 1.00 49.67  ? 175 GLN   A CA  1 
ATOM   802  C C   . GLN   A 1 100 ? -17.691 -10.892 30.685 1.00 45.59  ? 175 GLN   A C   1 
ATOM   803  O O   . GLN   A 1 100 ? -16.789 -11.730 30.747 1.00 48.38  ? 175 GLN   A O   1 
ATOM   804  C CB  . GLN   A 1 100 ? -20.032 -11.669 30.235 1.00 55.95  ? 175 GLN   A CB  1 
ATOM   805  C CG  . GLN   A 1 100 ? -19.786 -13.044 30.830 1.00 49.17  ? 175 GLN   A CG  1 
ATOM   806  C CD  . GLN   A 1 100 ? -21.049 -13.656 31.406 1.00 76.30  ? 175 GLN   A CD  1 
ATOM   807  O OE1 . GLN   A 1 100 ? -22.131 -13.076 31.312 1.00 81.39  ? 175 GLN   A OE1 1 
ATOM   808  N NE2 . GLN   A 1 100 ? -20.918 -14.834 32.008 1.00 78.02  ? 175 GLN   A NE2 1 
ATOM   809  N N   . ALA   A 1 101 ? -17.782 -9.847  31.503 1.00 48.15  ? 176 ALA   A N   1 
ATOM   810  C CA  . ALA   A 1 101 ? -16.828 -9.605  32.572 1.00 37.47  ? 176 ALA   A CA  1 
ATOM   811  C C   . ALA   A 1 101 ? -17.578 -9.335  33.867 1.00 41.33  ? 176 ALA   A C   1 
ATOM   812  O O   . ALA   A 1 101 ? -18.682 -8.781  33.861 1.00 51.05  ? 176 ALA   A O   1 
ATOM   813  C CB  . ALA   A 1 101 ? -15.905 -8.425  32.254 1.00 44.17  ? 176 ALA   A CB  1 
ATOM   814  N N   . TRP   A 1 102 ? -16.965 -9.731  34.980 1.00 38.56  ? 177 TRP   A N   1 
ATOM   815  C CA  . TRP   A 1 102 ? -17.557 -9.504  36.288 1.00 42.48  ? 177 TRP   A CA  1 
ATOM   816  C C   . TRP   A 1 102 ? -16.451 -9.449  37.330 1.00 37.87  ? 177 TRP   A C   1 
ATOM   817  O O   . TRP   A 1 102 ? -15.276 -9.685  37.038 1.00 47.27  ? 177 TRP   A O   1 
ATOM   818  C CB  . TRP   A 1 102 ? -18.585 -10.585 36.634 1.00 48.37  ? 177 TRP   A CB  1 
ATOM   819  C CG  . TRP   A 1 102 ? -18.005 -11.945 36.912 1.00 44.57  ? 177 TRP   A CG  1 
ATOM   820  C CD1 . TRP   A 1 102 ? -17.664 -12.456 38.132 1.00 37.71  ? 177 TRP   A CD1 1 
ATOM   821  C CD2 . TRP   A 1 102 ? -17.723 -12.977 35.954 1.00 38.06  ? 177 TRP   A CD2 1 
ATOM   822  N NE1 . TRP   A 1 102 ? -17.181 -13.736 37.993 1.00 43.16  ? 177 TRP   A NE1 1 
ATOM   823  C CE2 . TRP   A 1 102 ? -17.207 -14.079 36.666 1.00 40.53  ? 177 TRP   A CE2 1 
ATOM   824  C CE3 . TRP   A 1 102 ? -17.851 -13.073 34.565 1.00 35.52  ? 177 TRP   A CE3 1 
ATOM   825  C CZ2 . TRP   A 1 102 ? -16.820 -15.262 36.036 1.00 46.99  ? 177 TRP   A CZ2 1 
ATOM   826  C CZ3 . TRP   A 1 102 ? -17.466 -14.249 33.939 1.00 48.30  ? 177 TRP   A CZ3 1 
ATOM   827  C CH2 . TRP   A 1 102 ? -16.956 -15.328 34.675 1.00 42.96  ? 177 TRP   A CH2 1 
ATOM   828  N N   . GLU   A 1 103 ? -16.845 -9.126  38.558 1.00 45.48  ? 178 GLU   A N   1 
ATOM   829  C CA  . GLU   A 1 103 ? -15.922 -9.065  39.679 1.00 45.55  ? 178 GLU   A CA  1 
ATOM   830  C C   . GLU   A 1 103 ? -16.590 -9.666  40.907 1.00 47.59  ? 178 GLU   A C   1 
ATOM   831  O O   . GLU   A 1 103 ? -17.804 -9.544  41.097 1.00 49.07  ? 178 GLU   A O   1 
ATOM   832  C CB  . GLU   A 1 103 ? -15.470 -7.624  39.961 1.00 40.85  ? 178 GLU   A CB  1 
ATOM   833  C CG  . GLU   A 1 103 ? -16.607 -6.647  40.233 1.00 70.52  ? 178 GLU   A CG  1 
ATOM   834  C CD  . GLU   A 1 103 ? -16.113 -5.236  40.506 1.00 70.49  ? 178 GLU   A CD  1 
ATOM   835  O OE1 . GLU   A 1 103 ? -14.885 -5.018  40.448 1.00 81.47  ? 178 GLU   A OE1 1 
ATOM   836  O OE2 . GLU   A 1 103 ? -16.948 -4.347  40.780 1.00 72.01  ? 178 GLU   A OE2 1 
ATOM   837  N N   . GLU   A 1 104 ? -15.786 -10.330 41.736 1.00 45.67  ? 179 GLU   A N   1 
ATOM   838  C CA  . GLU   A 1 104 ? -16.288 -10.938 42.961 1.00 43.54  ? 179 GLU   A CA  1 
ATOM   839  C C   . GLU   A 1 104 ? -15.128 -11.085 43.931 1.00 54.49  ? 179 GLU   A C   1 
ATOM   840  O O   . GLU   A 1 104 ? -14.089 -11.646 43.570 1.00 56.68  ? 179 GLU   A O   1 
ATOM   841  C CB  . GLU   A 1 104 ? -16.930 -12.302 42.679 1.00 62.35  ? 179 GLU   A CB  1 
ATOM   842  C CG  . GLU   A 1 104 ? -17.603 -12.934 43.886 1.00 65.42  ? 179 GLU   A CG  1 
ATOM   843  C CD  . GLU   A 1 104 ? -18.132 -14.324 43.592 1.00 73.00  ? 179 GLU   A CD  1 
ATOM   844  O OE1 . GLU   A 1 104 ? -17.791 -14.876 42.525 1.00 104.53 ? 179 GLU   A OE1 1 
ATOM   845  O OE2 . GLU   A 1 104 ? -18.887 -14.867 44.427 1.00 80.56  ? 179 GLU   A OE2 1 
ATOM   846  N N   . GLY   A 1 105 ? -15.305 -10.582 45.151 1.00 46.91  ? 180 GLY   A N   1 
ATOM   847  C CA  . GLY   A 1 105 ? -14.255 -10.669 46.153 1.00 45.56  ? 180 GLY   A CA  1 
ATOM   848  C C   . GLY   A 1 105 ? -12.985 -9.935  45.785 1.00 50.43  ? 180 GLY   A C   1 
ATOM   849  O O   . GLY   A 1 105 ? -11.898 -10.331 46.220 1.00 56.75  ? 180 GLY   A O   1 
ATOM   850  N N   . GLY   A 1 106 ? -13.091 -8.868  44.997 1.00 55.15  ? 181 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 106 ? -11.928 -8.132  44.553 1.00 51.56  ? 181 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 106 ? -11.241 -8.701  43.335 1.00 41.88  ? 181 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 106 ? -10.346 -8.046  42.787 1.00 58.39  ? 181 GLY   A O   1 
ATOM   854  N N   . ILE   A 1 107 ? -11.626 -9.892  42.892 1.00 53.15  ? 182 ILE   A N   1 
ATOM   855  C CA  . ILE   A 1 107 ? -11.027 -10.532 41.730 1.00 44.22  ? 182 ILE   A CA  1 
ATOM   856  C C   . ILE   A 1 107 ? -11.834 -10.157 40.496 1.00 42.53  ? 182 ILE   A C   1 
ATOM   857  O O   . ILE   A 1 107 ? -13.070 -10.185 40.515 1.00 51.23  ? 182 ILE   A O   1 
ATOM   858  C CB  . ILE   A 1 107 ? -10.976 -12.058 41.914 1.00 46.75  ? 182 ILE   A CB  1 
ATOM   859  C CG1 . ILE   A 1 107 ? -10.137 -12.420 43.142 1.00 44.01  ? 182 ILE   A CG1 1 
ATOM   860  C CG2 . ILE   A 1 107 ? -10.410 -12.725 40.679 1.00 44.78  ? 182 ILE   A CG2 1 
ATOM   861  C CD1 . ILE   A 1 107 ? -8.703  -11.915 43.074 1.00 48.04  ? 182 ILE   A CD1 1 
ATOM   862  N N   . LEU   A 1 108 ? -11.138 -9.801  39.421 1.00 45.93  ? 183 LEU   A N   1 
ATOM   863  C CA  . LEU   A 1 108 ? -11.770 -9.469  38.152 1.00 41.62  ? 183 LEU   A CA  1 
ATOM   864  C C   . LEU   A 1 108 ? -11.700 -10.673 37.225 1.00 35.68  ? 183 LEU   A C   1 
ATOM   865  O O   . LEU   A 1 108 ? -10.620 -11.234 37.013 1.00 41.44  ? 183 LEU   A O   1 
ATOM   866  C CB  . LEU   A 1 108 ? -11.090 -8.267  37.496 1.00 41.90  ? 183 LEU   A CB  1 
ATOM   867  C CG  . LEU   A 1 108 ? -11.571 -7.948  36.081 1.00 38.34  ? 183 LEU   A CG  1 
ATOM   868  C CD1 . LEU   A 1 108 ? -13.019 -7.486  36.092 1.00 33.08  ? 183 LEU   A CD1 1 
ATOM   869  C CD2 . LEU   A 1 108 ? -10.681 -6.902  35.452 1.00 33.36  ? 183 LEU   A CD2 1 
ATOM   870  N N   . TYR   A 1 109 ? -12.846 -11.067 36.674 1.00 33.13  ? 184 TYR   A N   1 
ATOM   871  C CA  . TYR   A 1 109 ? -12.927 -12.174 35.732 1.00 30.60  ? 184 TYR   A CA  1 
ATOM   872  C C   . TYR   A 1 109 ? -13.312 -11.655 34.352 1.00 33.34  ? 184 TYR   A C   1 
ATOM   873  O O   . TYR   A 1 109 ? -14.208 -10.814 34.224 1.00 45.32  ? 184 TYR   A O   1 
ATOM   874  C CB  . TYR   A 1 109 ? -13.950 -13.214 36.187 1.00 39.03  ? 184 TYR   A CB  1 
ATOM   875  C CG  . TYR   A 1 109 ? -13.668 -13.837 37.536 1.00 42.40  ? 184 TYR   A CG  1 
ATOM   876  C CD1 . TYR   A 1 109 ? -14.034 -13.196 38.711 1.00 45.70  ? 184 TYR   A CD1 1 
ATOM   877  C CD2 . TYR   A 1 109 ? -13.056 -15.075 37.630 1.00 35.66  ? 184 TYR   A CD2 1 
ATOM   878  C CE1 . TYR   A 1 109 ? -13.786 -13.768 39.943 1.00 55.84  ? 184 TYR   A CE1 1 
ATOM   879  C CE2 . TYR   A 1 109 ? -12.804 -15.654 38.856 1.00 41.95  ? 184 TYR   A CE2 1 
ATOM   880  C CZ  . TYR   A 1 109 ? -13.172 -14.996 40.009 1.00 50.97  ? 184 TYR   A CZ  1 
ATOM   881  O OH  . TYR   A 1 109 ? -12.924 -15.569 41.235 1.00 64.21  ? 184 TYR   A OH  1 
ATOM   882  N N   . LEU   A 1 110 ? -12.634 -12.154 33.321 1.00 40.51  ? 185 LEU   A N   1 
ATOM   883  C CA  . LEU   A 1 110 ? -12.952 -11.831 31.935 1.00 41.27  ? 185 LEU   A CA  1 
ATOM   884  C C   . LEU   A 1 110 ? -13.168 -13.129 31.176 1.00 42.57  ? 185 LEU   A C   1 
ATOM   885  O O   . LEU   A 1 110 ? -12.273 -13.980 31.132 1.00 48.47  ? 185 LEU   A O   1 
ATOM   886  C CB  . LEU   A 1 110 ? -11.843 -11.013 31.271 1.00 39.71  ? 185 LEU   A CB  1 
ATOM   887  C CG  . LEU   A 1 110 ? -11.658 -9.566  31.722 1.00 45.69  ? 185 LEU   A CG  1 
ATOM   888  C CD1 . LEU   A 1 110 ? -10.642 -9.482  32.848 1.00 58.44  ? 185 LEU   A CD1 1 
ATOM   889  C CD2 . LEU   A 1 110 ? -11.244 -8.697  30.546 1.00 53.64  ? 185 LEU   A CD2 1 
ATOM   890  N N   . GLN   A 1 111 ? -14.343 -13.272 30.578 1.00 30.15  ? 186 GLN   A N   1 
ATOM   891  C CA  . GLN   A 1 111 ? -14.720 -14.470 29.840 1.00 35.22  ? 186 GLN   A CA  1 
ATOM   892  C C   . GLN   A 1 111 ? -14.684 -14.138 28.354 1.00 41.09  ? 186 GLN   A C   1 
ATOM   893  O O   . GLN   A 1 111 ? -15.464 -13.306 27.881 1.00 58.99  ? 186 GLN   A O   1 
ATOM   894  C CB  . GLN   A 1 111 ? -16.104 -14.951 30.269 1.00 44.54  ? 186 GLN   A CB  1 
ATOM   895  C CG  . GLN   A 1 111 ? -16.614 -16.167 29.515 1.00 43.74  ? 186 GLN   A CG  1 
ATOM   896  C CD  . GLN   A 1 111 ? -17.984 -16.596 29.996 1.00 52.70  ? 186 GLN   A CD  1 
ATOM   897  O OE1 . GLN   A 1 111 ? -18.532 -16.010 30.928 1.00 51.90  ? 186 GLN   A OE1 1 
ATOM   898  N NE2 . GLN   A 1 111 ? -18.547 -17.620 29.364 1.00 67.55  ? 186 GLN   A NE2 1 
ATOM   899  N N   . THR   A 1 112 ? -13.774 -14.776 27.624 1.00 48.02  ? 187 THR   A N   1 
ATOM   900  C CA  . THR   A 1 112 ? -13.631 -14.562 26.192 1.00 45.17  ? 187 THR   A CA  1 
ATOM   901  C C   . THR   A 1 112 ? -13.912 -15.859 25.448 1.00 46.08  ? 187 THR   A C   1 
ATOM   902  O O   . THR   A 1 112 ? -14.090 -16.923 26.045 1.00 57.66  ? 187 THR   A O   1 
ATOM   903  C CB  . THR   A 1 112 ? -12.225 -14.057 25.833 1.00 44.38  ? 187 THR   A CB  1 
ATOM   904  O OG1 . THR   A 1 112 ? -11.258 -15.070 26.139 1.00 50.99  ? 187 THR   A OG1 1 
ATOM   905  C CG2 . THR   A 1 112 ? -11.887 -12.793 26.604 1.00 42.00  ? 187 THR   A CG2 1 
ATOM   906  N N   . GLU   A 1 113 ? -13.952 -15.758 24.123 1.00 40.17  ? 188 GLU   A N   1 
ATOM   907  C CA  . GLU   A 1 113 ? -13.998 -16.954 23.297 1.00 45.93  ? 188 GLU   A CA  1 
ATOM   908  C C   . GLU   A 1 113 ? -12.705 -17.741 23.461 1.00 43.35  ? 188 GLU   A C   1 
ATOM   909  O O   . GLU   A 1 113 ? -11.628 -17.177 23.674 1.00 58.84  ? 188 GLU   A O   1 
ATOM   910  C CB  . GLU   A 1 113 ? -14.199 -16.580 21.827 1.00 41.30  ? 188 GLU   A CB  1 
ATOM   911  C CG  . GLU   A 1 113 ? -13.119 -15.643 21.288 1.00 63.54  ? 188 GLU   A CG  1 
ATOM   912  C CD  . GLU   A 1 113 ? -13.364 -15.206 19.856 1.00 73.28  ? 188 GLU   A CD  1 
ATOM   913  O OE1 . GLU   A 1 113 ? -14.214 -15.826 19.183 1.00 79.58  ? 188 GLU   A OE1 1 
ATOM   914  O OE2 . GLU   A 1 113 ? -12.708 -14.241 19.405 1.00 73.48  ? 188 GLU   A OE2 1 
ATOM   915  N N   . LEU   A 1 114 ? -12.813 -19.061 23.373 1.00 66.55  ? 189 LEU   A N   1 
ATOM   916  C CA  . LEU   A 1 114 ? -11.630 -19.906 23.439 1.00 50.88  ? 189 LEU   A CA  1 
ATOM   917  C C   . LEU   A 1 114 ? -10.912 -19.856 22.097 1.00 50.00  ? 189 LEU   A C   1 
ATOM   918  O O   . LEU   A 1 114 ? -11.480 -20.234 21.067 1.00 65.37  ? 189 LEU   A O   1 
ATOM   919  C CB  . LEU   A 1 114 ? -12.006 -21.340 23.799 1.00 56.45  ? 189 LEU   A CB  1 
ATOM   920  C CG  . LEU   A 1 114 ? -10.807 -22.285 23.895 1.00 51.65  ? 189 LEU   A CG  1 
ATOM   921  C CD1 . LEU   A 1 114 ? -9.828  -21.803 24.952 1.00 64.43  ? 189 LEU   A CD1 1 
ATOM   922  C CD2 . LEU   A 1 114 ? -11.257 -23.700 24.193 1.00 63.89  ? 189 LEU   A CD2 1 
ATOM   923  N N   . CYS   A 1 115 ? -9.674  -19.378 22.107 1.00 54.60  ? 190 CYS   A N   1 
ATOM   924  C CA  . CYS   A 1 115 ? -8.847  -19.341 20.914 1.00 45.24  ? 190 CYS   A CA  1 
ATOM   925  C C   . CYS   A 1 115 ? -7.871  -20.514 20.927 1.00 53.49  ? 190 CYS   A C   1 
ATOM   926  O O   . CYS   A 1 115 ? -7.836  -21.324 21.857 1.00 51.26  ? 190 CYS   A O   1 
ATOM   927  C CB  . CYS   A 1 115 ? -8.111  -18.006 20.816 1.00 37.42  ? 190 CYS   A CB  1 
ATOM   928  S SG  . CYS   A 1 115 ? -9.209  -16.594 20.608 1.00 54.42  ? 190 CYS   A SG  1 
ATOM   929  N N   . GLY   A 1 116 ? -7.070  -20.610 19.872 1.00 54.57  ? 191 GLY   A N   1 
ATOM   930  C CA  . GLY   A 1 116 ? -6.085  -21.658 19.777 1.00 52.84  ? 191 GLY   A CA  1 
ATOM   931  C C   . GLY   A 1 116 ? -4.843  -21.313 20.569 1.00 46.07  ? 191 GLY   A C   1 
ATOM   932  O O   . GLY   A 1 116 ? -4.848  -20.413 21.415 1.00 48.48  ? 191 GLY   A O   1 
ATOM   933  N N   . PRO   A 1 117 ? -3.749  -22.027 20.309 1.00 46.99  ? 192 PRO   A N   1 
ATOM   934  C CA  . PRO   A 1 117 ? -2.483  -21.691 20.968 1.00 53.78  ? 192 PRO   A CA  1 
ATOM   935  C C   . PRO   A 1 117 ? -2.000  -20.309 20.554 1.00 44.83  ? 192 PRO   A C   1 
ATOM   936  O O   . PRO   A 1 117 ? -2.291  -19.828 19.456 1.00 52.95  ? 192 PRO   A O   1 
ATOM   937  C CB  . PRO   A 1 117 ? -1.528  -22.788 20.482 1.00 49.65  ? 192 PRO   A CB  1 
ATOM   938  C CG  . PRO   A 1 117 ? -2.126  -23.266 19.196 1.00 60.66  ? 192 PRO   A CG  1 
ATOM   939  C CD  . PRO   A 1 117 ? -3.612  -23.166 19.386 1.00 44.51  ? 192 PRO   A CD  1 
ATOM   940  N N   . SER   A 1 118 ? -1.267  -19.659 21.455 1.00 44.02  ? 193 SER   A N   1 
ATOM   941  C CA  . SER   A 1 118 ? -0.691  -18.365 21.125 1.00 37.81  ? 193 SER   A CA  1 
ATOM   942  C C   . SER   A 1 118 ? 0.374   -18.525 20.049 1.00 30.90  ? 193 SER   A C   1 
ATOM   943  O O   . SER   A 1 118 ? 0.947   -19.601 19.859 1.00 44.81  ? 193 SER   A O   1 
ATOM   944  C CB  . SER   A 1 118 ? -0.072  -17.706 22.356 1.00 29.75  ? 193 SER   A CB  1 
ATOM   945  O OG  . SER   A 1 118 ? 1.189   -18.282 22.653 1.00 48.14  ? 193 SER   A OG  1 
ATOM   946  N N   . LEU   A 1 119 ? 0.648   -17.427 19.346 1.00 43.94  ? 194 LEU   A N   1 
ATOM   947  C CA  . LEU   A 1 119 ? 1.699   -17.458 18.337 1.00 39.67  ? 194 LEU   A CA  1 
ATOM   948  C C   . LEU   A 1 119 ? 3.048   -17.802 18.957 1.00 36.58  ? 194 LEU   A C   1 
ATOM   949  O O   . LEU   A 1 119 ? 3.914   -18.375 18.287 1.00 52.78  ? 194 LEU   A O   1 
ATOM   950  C CB  . LEU   A 1 119 ? 1.759   -16.115 17.609 1.00 43.53  ? 194 LEU   A CB  1 
ATOM   951  C CG  . LEU   A 1 119 ? 2.630   -16.044 16.355 1.00 51.86  ? 194 LEU   A CG  1 
ATOM   952  C CD1 . LEU   A 1 119 ? 2.203   -17.106 15.358 1.00 51.70  ? 194 LEU   A CD1 1 
ATOM   953  C CD2 . LEU   A 1 119 ? 2.563   -14.658 15.731 1.00 41.61  ? 194 LEU   A CD2 1 
ATOM   954  N N   . GLN   A 1 120 ? 3.237   -17.478 20.238 1.00 41.99  ? 195 GLN   A N   1 
ATOM   955  C CA  . GLN   A 1 120 ? 4.462   -17.867 20.928 1.00 35.10  ? 195 GLN   A CA  1 
ATOM   956  C C   . GLN   A 1 120 ? 4.503   -19.371 21.149 1.00 38.07  ? 195 GLN   A C   1 
ATOM   957  O O   . GLN   A 1 120 ? 5.514   -20.023 20.866 1.00 55.18  ? 195 GLN   A O   1 
ATOM   958  C CB  . GLN   A 1 120 ? 4.567   -17.126 22.261 1.00 39.21  ? 195 GLN   A CB  1 
ATOM   959  C CG  . GLN   A 1 120 ? 5.854   -17.380 23.026 1.00 42.84  ? 195 GLN   A CG  1 
ATOM   960  C CD  . GLN   A 1 120 ? 5.897   -16.626 24.343 1.00 45.23  ? 195 GLN   A CD  1 
ATOM   961  O OE1 . GLN   A 1 120 ? 4.857   -16.301 24.917 1.00 49.70  ? 195 GLN   A OE1 1 
ATOM   962  N NE2 . GLN   A 1 120 ? 7.101   -16.336 24.823 1.00 52.43  ? 195 GLN   A NE2 1 
ATOM   963  N N   . GLN   A 1 121 ? 3.408   -19.939 21.658 1.00 44.43  ? 196 GLN   A N   1 
ATOM   964  C CA  . GLN   A 1 121 ? 3.351   -21.380 21.873 1.00 33.98  ? 196 GLN   A CA  1 
ATOM   965  C C   . GLN   A 1 121 ? 3.502   -22.138 20.562 1.00 34.88  ? 196 GLN   A C   1 
ATOM   966  O O   . GLN   A 1 121 ? 4.148   -23.190 20.514 1.00 50.08  ? 196 GLN   A O   1 
ATOM   967  C CB  . GLN   A 1 121 ? 2.036   -21.759 22.554 1.00 36.79  ? 196 GLN   A CB  1 
ATOM   968  C CG  . GLN   A 1 121 ? 1.886   -21.249 23.979 1.00 49.55  ? 196 GLN   A CG  1 
ATOM   969  C CD  . GLN   A 1 121 ? 0.511   -21.541 24.559 1.00 47.89  ? 196 GLN   A CD  1 
ATOM   970  O OE1 . GLN   A 1 121 ? -0.508  -21.358 23.892 1.00 51.59  ? 196 GLN   A OE1 1 
ATOM   971  N NE2 . GLN   A 1 121 ? 0.479   -22.000 25.805 1.00 58.28  ? 196 GLN   A NE2 1 
ATOM   972  N N   . HIS   A 1 122 ? 2.913   -21.618 19.485 1.00 44.07  ? 197 HIS   A N   1 
ATOM   973  C CA  . HIS   A 1 122 ? 2.995   -22.296 18.196 1.00 39.24  ? 197 HIS   A CA  1 
ATOM   974  C C   . HIS   A 1 122 ? 4.435   -22.378 17.703 1.00 37.14  ? 197 HIS   A C   1 
ATOM   975  O O   . HIS   A 1 122 ? 4.843   -23.391 17.127 1.00 57.27  ? 197 HIS   A O   1 
ATOM   976  C CB  . HIS   A 1 122 ? 2.112   -21.579 17.175 1.00 40.54  ? 197 HIS   A CB  1 
ATOM   977  C CG  . HIS   A 1 122 ? 2.019   -22.280 15.857 1.00 47.57  ? 197 HIS   A CG  1 
ATOM   978  N ND1 . HIS   A 1 122 ? 2.544   -21.753 14.697 1.00 64.63  ? 197 HIS   A ND1 1 
ATOM   979  C CD2 . HIS   A 1 122 ? 1.456   -23.462 15.513 1.00 43.45  ? 197 HIS   A CD2 1 
ATOM   980  C CE1 . HIS   A 1 122 ? 2.310   -22.581 13.694 1.00 48.12  ? 197 HIS   A CE1 1 
ATOM   981  N NE2 . HIS   A 1 122 ? 1.650   -23.624 14.163 1.00 59.34  ? 197 HIS   A NE2 1 
ATOM   982  N N   . CYS   A 1 123 ? 5.224   -21.324 17.927 1.00 47.58  ? 198 CYS   A N   1 
ATOM   983  C CA  . CYS   A 1 123 ? 6.624   -21.357 17.513 1.00 47.16  ? 198 CYS   A CA  1 
ATOM   984  C C   . CYS   A 1 123 ? 7.450   -22.268 18.412 1.00 49.45  ? 198 CYS   A C   1 
ATOM   985  O O   . CYS   A 1 123 ? 8.359   -22.958 17.934 1.00 67.31  ? 198 CYS   A O   1 
ATOM   986  C CB  . CYS   A 1 123 ? 7.207   -19.946 17.504 1.00 54.48  ? 198 CYS   A CB  1 
ATOM   987  S SG  . CYS   A 1 123 ? 6.483   -18.872 16.254 1.00 68.99  ? 198 CYS   A SG  1 
ATOM   988  N N   . GLU   A 1 124 ? 7.160   -22.278 19.717 1.00 48.17  ? 199 GLU   A N   1 
ATOM   989  C CA  . GLU   A 1 124 ? 7.858   -23.191 20.619 1.00 49.70  ? 199 GLU   A CA  1 
ATOM   990  C C   . GLU   A 1 124 ? 7.630   -24.639 20.214 1.00 60.78  ? 199 GLU   A C   1 
ATOM   991  O O   . GLU   A 1 124 ? 8.537   -25.474 20.316 1.00 62.21  ? 199 GLU   A O   1 
ATOM   992  C CB  . GLU   A 1 124 ? 7.395   -22.973 22.059 1.00 56.63  ? 199 GLU   A CB  1 
ATOM   993  C CG  . GLU   A 1 124 ? 7.652   -21.582 22.608 1.00 70.85  ? 199 GLU   A CG  1 
ATOM   994  C CD  . GLU   A 1 124 ? 7.023   -21.374 23.972 1.00 79.99  ? 199 GLU   A CD  1 
ATOM   995  O OE1 . GLU   A 1 124 ? 6.655   -22.379 24.616 1.00 86.26  ? 199 GLU   A OE1 1 
ATOM   996  O OE2 . GLU   A 1 124 ? 6.891   -20.206 24.399 1.00 78.73  ? 199 GLU   A OE2 1 
ATOM   997  N N   . ALA   A 1 125 ? 6.417   -24.956 19.756 1.00 63.69  ? 200 ALA   A N   1 
ATOM   998  C CA  . ALA   A 1 125 ? 6.099   -26.326 19.373 1.00 52.11  ? 200 ALA   A CA  1 
ATOM   999  C C   . ALA   A 1 125 ? 6.911   -26.755 18.157 1.00 66.17  ? 200 ALA   A C   1 
ATOM   1000 O O   . ALA   A 1 125 ? 7.488   -27.848 18.136 1.00 73.05  ? 200 ALA   A O   1 
ATOM   1001 C CB  . ALA   A 1 125 ? 4.600   -26.455 19.100 1.00 54.02  ? 200 ALA   A CB  1 
ATOM   1002 N N   . TRP   A 1 126 ? 6.975   -25.900 17.136 1.00 56.38  ? 201 TRP   A N   1 
ATOM   1003 C CA  . TRP   A 1 126 ? 7.732   -26.240 15.940 1.00 70.88  ? 201 TRP   A CA  1 
ATOM   1004 C C   . TRP   A 1 126 ? 9.233   -26.080 16.129 1.00 62.97  ? 201 TRP   A C   1 
ATOM   1005 O O   . TRP   A 1 126 ? 10.003  -26.712 15.399 1.00 65.47  ? 201 TRP   A O   1 
ATOM   1006 C CB  . TRP   A 1 126 ? 7.248   -25.395 14.762 1.00 57.30  ? 201 TRP   A CB  1 
ATOM   1007 C CG  . TRP   A 1 126 ? 5.865   -25.764 14.335 1.00 61.14  ? 201 TRP   A CG  1 
ATOM   1008 C CD1 . TRP   A 1 126 ? 4.704   -25.146 14.697 1.00 72.07  ? 201 TRP   A CD1 1 
ATOM   1009 C CD2 . TRP   A 1 126 ? 5.491   -26.855 13.485 1.00 55.13  ? 201 TRP   A CD2 1 
ATOM   1010 N NE1 . TRP   A 1 126 ? 3.631   -25.777 14.115 1.00 71.89  ? 201 TRP   A NE1 1 
ATOM   1011 C CE2 . TRP   A 1 126 ? 4.087   -26.830 13.366 1.00 77.57  ? 201 TRP   A CE2 1 
ATOM   1012 C CE3 . TRP   A 1 126 ? 6.207   -27.846 12.807 1.00 63.02  ? 201 TRP   A CE3 1 
ATOM   1013 C CZ2 . TRP   A 1 126 ? 3.385   -27.756 12.597 1.00 77.91  ? 201 TRP   A CZ2 1 
ATOM   1014 C CZ3 . TRP   A 1 126 ? 5.508   -28.767 12.042 1.00 68.65  ? 201 TRP   A CZ3 1 
ATOM   1015 C CH2 . TRP   A 1 126 ? 4.111   -28.715 11.945 1.00 80.14  ? 201 TRP   A CH2 1 
ATOM   1016 N N   . GLY   A 1 127 ? 9.661   -25.259 17.087 1.00 69.89  ? 202 GLY   A N   1 
ATOM   1017 C CA  . GLY   A 1 127 ? 11.066  -25.186 17.453 1.00 78.73  ? 202 GLY   A CA  1 
ATOM   1018 C C   . GLY   A 1 127 ? 11.992  -24.774 16.333 1.00 95.92  ? 202 GLY   A C   1 
ATOM   1019 O O   . GLY   A 1 127 ? 13.177  -25.128 16.355 1.00 87.06  ? 202 GLY   A O   1 
ATOM   1020 N N   . ALA   A 1 128 ? 11.486  -24.036 15.350 1.00 84.34  ? 203 ALA   A N   1 
ATOM   1021 C CA  . ALA   A 1 128 ? 12.294  -23.578 14.227 1.00 77.93  ? 203 ALA   A CA  1 
ATOM   1022 C C   . ALA   A 1 128 ? 11.606  -22.366 13.609 1.00 92.44  ? 203 ALA   A C   1 
ATOM   1023 O O   . ALA   A 1 128 ? 10.614  -21.854 14.141 1.00 77.48  ? 203 ALA   A O   1 
ATOM   1024 C CB  . ALA   A 1 128 ? 12.507  -24.702 13.208 1.00 67.38  ? 203 ALA   A CB  1 
ATOM   1025 N N   . SER   A 1 129 ? 12.142  -21.898 12.485 1.00 91.13  ? 204 SER   A N   1 
ATOM   1026 C CA  . SER   A 1 129 ? 11.543  -20.771 11.785 1.00 63.09  ? 204 SER   A CA  1 
ATOM   1027 C C   . SER   A 1 129 ? 10.241  -21.206 11.129 1.00 65.50  ? 204 SER   A C   1 
ATOM   1028 O O   . SER   A 1 129 ? 10.200  -22.213 10.415 1.00 85.49  ? 204 SER   A O   1 
ATOM   1029 C CB  . SER   A 1 129 ? 12.507  -20.224 10.733 1.00 73.27  ? 204 SER   A CB  1 
ATOM   1030 O OG  . SER   A 1 129 ? 13.762  -19.900 11.306 1.00 98.41  ? 204 SER   A OG  1 
ATOM   1031 N N   . LEU   A 1 130 ? 9.176   -20.457 11.382 1.00 56.64  ? 205 LEU   A N   1 
ATOM   1032 C CA  . LEU   A 1 130 ? 7.903   -20.744 10.735 1.00 63.95  ? 205 LEU   A CA  1 
ATOM   1033 C C   . LEU   A 1 130 ? 8.028   -20.517 9.233  1.00 72.12  ? 205 LEU   A C   1 
ATOM   1034 O O   . LEU   A 1 130 ? 8.583   -19.495 8.809  1.00 66.81  ? 205 LEU   A O   1 
ATOM   1035 C CB  . LEU   A 1 130 ? 6.792   -19.869 11.308 1.00 53.28  ? 205 LEU   A CB  1 
ATOM   1036 C CG  . LEU   A 1 130 ? 6.119   -20.385 12.581 1.00 60.03  ? 205 LEU   A CG  1 
ATOM   1037 C CD1 . LEU   A 1 130 ? 4.934   -19.510 12.942 1.00 58.63  ? 205 LEU   A CD1 1 
ATOM   1038 C CD2 . LEU   A 1 130 ? 5.684   -21.832 12.406 1.00 56.16  ? 205 LEU   A CD2 1 
ATOM   1039 N N   . PRO   A 1 131 ? 7.543   -21.440 8.402  1.00 67.72  ? 206 PRO   A N   1 
ATOM   1040 C CA  . PRO   A 1 131 ? 7.604   -21.228 6.952  1.00 71.50  ? 206 PRO   A CA  1 
ATOM   1041 C C   . PRO   A 1 131 ? 6.869   -19.957 6.559  1.00 61.06  ? 206 PRO   A C   1 
ATOM   1042 O O   . PRO   A 1 131 ? 5.872   -19.573 7.174  1.00 53.89  ? 206 PRO   A O   1 
ATOM   1043 C CB  . PRO   A 1 131 ? 6.921   -22.476 6.380  1.00 63.97  ? 206 PRO   A CB  1 
ATOM   1044 C CG  . PRO   A 1 131 ? 6.101   -23.018 7.507  1.00 61.81  ? 206 PRO   A CG  1 
ATOM   1045 C CD  . PRO   A 1 131 ? 6.866   -22.698 8.752  1.00 64.37  ? 206 PRO   A CD  1 
ATOM   1046 N N   . GLU   A 1 132 ? 7.388   -19.294 5.521  1.00 71.93  ? 207 GLU   A N   1 
ATOM   1047 C CA  . GLU   A 1 132 ? 6.858   -17.991 5.130  1.00 57.77  ? 207 GLU   A CA  1 
ATOM   1048 C C   . GLU   A 1 132 ? 5.387   -18.050 4.741  1.00 57.63  ? 207 GLU   A C   1 
ATOM   1049 O O   . GLU   A 1 132 ? 4.689   -17.036 4.855  1.00 58.21  ? 207 GLU   A O   1 
ATOM   1050 C CB  . GLU   A 1 132 ? 7.677   -17.408 3.972  1.00 62.84  ? 207 GLU   A CB  1 
ATOM   1051 C CG  . GLU   A 1 132 ? 9.097   -17.029 4.348  1.00 78.86  ? 207 GLU   A CG  1 
ATOM   1052 C CD  . GLU   A 1 132 ? 9.668   -15.948 3.451  1.00 87.62  ? 207 GLU   A CD  1 
ATOM   1053 O OE1 . GLU   A 1 132 ? 8.885   -15.098 2.978  1.00 81.39  ? 207 GLU   A OE1 1 
ATOM   1054 O OE2 . GLU   A 1 132 ? 10.895  -15.946 3.214  1.00 92.85  ? 207 GLU   A OE2 1 
ATOM   1055 N N   . ALA   A 1 133 ? 4.901   -19.205 4.284  1.00 62.16  ? 208 ALA   A N   1 
ATOM   1056 C CA  . ALA   A 1 133 ? 3.492   -19.325 3.916  1.00 49.16  ? 208 ALA   A CA  1 
ATOM   1057 C C   . ALA   A 1 133 ? 2.583   -18.958 5.087  1.00 61.91  ? 208 ALA   A C   1 
ATOM   1058 O O   . ALA   A 1 133 ? 1.708   -18.093 4.963  1.00 62.90  ? 208 ALA   A O   1 
ATOM   1059 C CB  . ALA   A 1 133 ? 3.195   -20.742 3.421  1.00 58.98  ? 208 ALA   A CB  1 
ATOM   1060 N N   . GLN   A 1 134 ? 2.790   -19.593 6.244  1.00 52.20  ? 209 GLN   A N   1 
ATOM   1061 C CA  . GLN   A 1 134 ? 1.972   -19.269 7.408  1.00 50.43  ? 209 GLN   A CA  1 
ATOM   1062 C C   . GLN   A 1 134 ? 2.216   -17.846 7.893  1.00 50.60  ? 209 GLN   A C   1 
ATOM   1063 O O   . GLN   A 1 134 ? 1.303   -17.216 8.440  1.00 51.38  ? 209 GLN   A O   1 
ATOM   1064 C CB  . GLN   A 1 134 ? 2.245   -20.256 8.542  1.00 49.48  ? 209 GLN   A CB  1 
ATOM   1065 C CG  . GLN   A 1 134 ? 2.044   -21.716 8.173  1.00 65.10  ? 209 GLN   A CG  1 
ATOM   1066 C CD  . GLN   A 1 134 ? 2.235   -22.640 9.359  1.00 70.89  ? 209 GLN   A CD  1 
ATOM   1067 O OE1 . GLN   A 1 134 ? 2.237   -22.198 10.508 1.00 71.27  ? 209 GLN   A OE1 1 
ATOM   1068 N NE2 . GLN   A 1 134 ? 2.400   -23.931 9.087  1.00 96.53  ? 209 GLN   A NE2 1 
ATOM   1069 N N   . VAL   A 1 135 ? 3.431   -17.327 7.699  1.00 57.00  ? 210 VAL   A N   1 
ATOM   1070 C CA  . VAL   A 1 135 ? 3.782   -16.018 8.248  1.00 44.82  ? 210 VAL   A CA  1 
ATOM   1071 C C   . VAL   A 1 135 ? 2.928   -14.924 7.621  1.00 49.58  ? 210 VAL   A C   1 
ATOM   1072 O O   . VAL   A 1 135 ? 2.468   -14.005 8.311  1.00 47.27  ? 210 VAL   A O   1 
ATOM   1073 C CB  . VAL   A 1 135 ? 5.285   -15.746 8.055  1.00 55.11  ? 210 VAL   A CB  1 
ATOM   1074 C CG1 . VAL   A 1 135 ? 5.627   -14.333 8.483  1.00 55.25  ? 210 VAL   A CG1 1 
ATOM   1075 C CG2 . VAL   A 1 135 ? 6.111   -16.748 8.844  1.00 52.59  ? 210 VAL   A CG2 1 
ATOM   1076 N N   . TRP   A 1 136 ? 2.692   -15.009 6.309  1.00 53.15  ? 211 TRP   A N   1 
ATOM   1077 C CA  . TRP   A 1 136 ? 1.868   -14.004 5.643  1.00 50.92  ? 211 TRP   A CA  1 
ATOM   1078 C C   . TRP   A 1 136 ? 0.435   -14.026 6.163  1.00 54.54  ? 211 TRP   A C   1 
ATOM   1079 O O   . TRP   A 1 136 ? -0.193  -12.972 6.317  1.00 63.24  ? 211 TRP   A O   1 
ATOM   1080 C CB  . TRP   A 1 136 ? 1.887   -14.223 4.131  1.00 52.27  ? 211 TRP   A CB  1 
ATOM   1081 C CG  . TRP   A 1 136 ? 3.203   -13.914 3.485  1.00 47.03  ? 211 TRP   A CG  1 
ATOM   1082 C CD1 . TRP   A 1 136 ? 4.098   -14.810 2.981  1.00 58.11  ? 211 TRP   A CD1 1 
ATOM   1083 C CD2 . TRP   A 1 136 ? 3.770   -12.615 3.267  1.00 52.69  ? 211 TRP   A CD2 1 
ATOM   1084 N NE1 . TRP   A 1 136 ? 5.188   -14.152 2.464  1.00 57.98  ? 211 TRP   A NE1 1 
ATOM   1085 C CE2 . TRP   A 1 136 ? 5.011   -12.804 2.627  1.00 47.35  ? 211 TRP   A CE2 1 
ATOM   1086 C CE3 . TRP   A 1 136 ? 3.349   -11.313 3.551  1.00 50.83  ? 211 TRP   A CE3 1 
ATOM   1087 C CZ2 . TRP   A 1 136 ? 5.836   -11.739 2.267  1.00 53.99  ? 211 TRP   A CZ2 1 
ATOM   1088 C CZ3 . TRP   A 1 136 ? 4.170   -10.255 3.193  1.00 52.85  ? 211 TRP   A CZ3 1 
ATOM   1089 C CH2 . TRP   A 1 136 ? 5.399   -10.476 2.558  1.00 53.46  ? 211 TRP   A CH2 1 
ATOM   1090 N N   . GLY   A 1 137 ? -0.104  -15.217 6.432  1.00 48.37  ? 212 GLY   A N   1 
ATOM   1091 C CA  . GLY   A 1 137 ? -1.463  -15.299 6.945  1.00 35.18  ? 212 GLY   A CA  1 
ATOM   1092 C C   . GLY   A 1 137 ? -1.614  -14.617 8.290  1.00 36.31  ? 212 GLY   A C   1 
ATOM   1093 O O   . GLY   A 1 137 ? -2.537  -13.825 8.500  1.00 54.33  ? 212 GLY   A O   1 
ATOM   1094 N N   . TYR   A 1 138 ? -0.704  -14.913 9.222  1.00 44.84  ? 213 TYR   A N   1 
ATOM   1095 C CA  . TYR   A 1 138 ? -0.758  -14.269 10.529 1.00 45.67  ? 213 TYR   A CA  1 
ATOM   1096 C C   . TYR   A 1 138 ? -0.467  -12.779 10.415 1.00 47.18  ? 213 TYR   A C   1 
ATOM   1097 O O   . TYR   A 1 138 ? -1.055  -11.967 11.140 1.00 54.19  ? 213 TYR   A O   1 
ATOM   1098 C CB  . TYR   A 1 138 ? 0.227   -14.939 11.487 1.00 38.66  ? 213 TYR   A CB  1 
ATOM   1099 C CG  . TYR   A 1 138 ? -0.037  -16.414 11.698 1.00 48.44  ? 213 TYR   A CG  1 
ATOM   1100 C CD1 . TYR   A 1 138 ? -1.337  -16.904 11.760 1.00 50.00  ? 213 TYR   A CD1 1 
ATOM   1101 C CD2 . TYR   A 1 138 ? 1.012   -17.318 11.822 1.00 51.24  ? 213 TYR   A CD2 1 
ATOM   1102 C CE1 . TYR   A 1 138 ? -1.586  -18.254 11.948 1.00 38.13  ? 213 TYR   A CE1 1 
ATOM   1103 C CE2 . TYR   A 1 138 ? 0.772   -18.673 12.010 1.00 48.85  ? 213 TYR   A CE2 1 
ATOM   1104 C CZ  . TYR   A 1 138 ? -0.530  -19.134 12.072 1.00 51.88  ? 213 TYR   A CZ  1 
ATOM   1105 O OH  . TYR   A 1 138 ? -0.782  -20.477 12.257 1.00 58.19  ? 213 TYR   A OH  1 
ATOM   1106 N N   . LEU   A 1 139 ? 0.435   -12.402 9.508  1.00 45.73  ? 214 LEU   A N   1 
ATOM   1107 C CA  . LEU   A 1 139 ? 0.726   -10.988 9.302  1.00 38.09  ? 214 LEU   A CA  1 
ATOM   1108 C C   . LEU   A 1 139 ? -0.495  -10.247 8.773  1.00 38.90  ? 214 LEU   A C   1 
ATOM   1109 O O   . LEU   A 1 139 ? -0.814  -9.149  9.242  1.00 52.28  ? 214 LEU   A O   1 
ATOM   1110 C CB  . LEU   A 1 139 ? 1.906   -10.832 8.344  1.00 49.13  ? 214 LEU   A CB  1 
ATOM   1111 C CG  . LEU   A 1 139 ? 2.262   -9.404  7.938  1.00 38.07  ? 214 LEU   A CG  1 
ATOM   1112 C CD1 . LEU   A 1 139 ? 2.560   -8.563  9.167  1.00 38.94  ? 214 LEU   A CD1 1 
ATOM   1113 C CD2 . LEU   A 1 139 ? 3.444   -9.408  6.981  1.00 42.77  ? 214 LEU   A CD2 1 
ATOM   1114 N N   . ARG   A 1 140 ? -1.195  -10.832 7.800  1.00 40.43  ? 215 ARG   A N   1 
ATOM   1115 C CA  . ARG   A 1 140 ? -2.378  -10.177 7.254  1.00 38.54  ? 215 ARG   A CA  1 
ATOM   1116 C C   . ARG   A 1 140 ? -3.482  -10.078 8.300  1.00 39.66  ? 215 ARG   A C   1 
ATOM   1117 O O   . ARG   A 1 140 ? -4.106  -9.023  8.459  1.00 54.06  ? 215 ARG   A O   1 
ATOM   1118 C CB  . ARG   A 1 140 ? -2.876  -10.921 6.015  1.00 37.03  ? 215 ARG   A CB  1 
ATOM   1119 C CG  . ARG   A 1 140 ? -4.185  -10.364 5.493  1.00 44.02  ? 215 ARG   A CG  1 
ATOM   1120 C CD  . ARG   A 1 140 ? -4.631  -11.012 4.199  1.00 47.26  ? 215 ARG   A CD  1 
ATOM   1121 N NE  . ARG   A 1 140 ? -5.793  -10.320 3.652  1.00 69.91  ? 215 ARG   A NE  1 
ATOM   1122 C CZ  . ARG   A 1 140 ? -7.052  -10.615 3.948  1.00 83.72  ? 215 ARG   A CZ  1 
ATOM   1123 N NH1 . ARG   A 1 140 ? -7.357  -11.607 4.770  1.00 84.38  ? 215 ARG   A NH1 1 
ATOM   1124 N NH2 . ARG   A 1 140 ? -8.031  -9.898  3.405  1.00 75.32  ? 215 ARG   A NH2 1 
ATOM   1125 N N   . ASP   A 1 141 ? -3.729  -11.166 9.033  1.00 46.24  ? 216 ASP   A N   1 
ATOM   1126 C CA  . ASP   A 1 141 ? -4.796  -11.152 10.030 1.00 39.37  ? 216 ASP   A CA  1 
ATOM   1127 C C   . ASP   A 1 141 ? -4.513  -10.142 11.133 1.00 37.86  ? 216 ASP   A C   1 
ATOM   1128 O O   . ASP   A 1 141 ? -5.431  -9.470  11.621 1.00 47.89  ? 216 ASP   A O   1 
ATOM   1129 C CB  . ASP   A 1 141 ? -4.983  -12.549 10.617 1.00 44.22  ? 216 ASP   A CB  1 
ATOM   1130 C CG  . ASP   A 1 141 ? -5.514  -13.541 9.601  1.00 69.42  ? 216 ASP   A CG  1 
ATOM   1131 O OD1 . ASP   A 1 141 ? -6.162  -13.108 8.624  1.00 79.91  ? 216 ASP   A OD1 1 
ATOM   1132 O OD2 . ASP   A 1 141 ? -5.285  -14.754 9.781  1.00 75.03  ? 216 ASP   A OD2 1 
ATOM   1133 N N   . THR   A 1 142 ? -3.250  -10.015 11.542 1.00 35.02  ? 217 THR   A N   1 
ATOM   1134 C CA  . THR   A 1 142 ? -2.929  -9.069  12.604 1.00 36.71  ? 217 THR   A CA  1 
ATOM   1135 C C   . THR   A 1 142 ? -3.007  -7.635  12.101 1.00 49.63  ? 217 THR   A C   1 
ATOM   1136 O O   . THR   A 1 142 ? -3.429  -6.734  12.836 1.00 47.38  ? 217 THR   A O   1 
ATOM   1137 C CB  . THR   A 1 142 ? -1.546  -9.364  13.172 1.00 42.53  ? 217 THR   A CB  1 
ATOM   1138 O OG1 . THR   A 1 142 ? -1.456  -10.759 13.491 1.00 39.03  ? 217 THR   A OG1 1 
ATOM   1139 C CG2 . THR   A 1 142 ? -1.315  -8.549  14.433 1.00 42.92  ? 217 THR   A CG2 1 
ATOM   1140 N N   . LEU   A 1 143 ? -2.605  -7.403  10.850 1.00 36.28  ? 218 LEU   A N   1 
ATOM   1141 C CA  . LEU   A 1 143 ? -2.772  -6.081  10.256 1.00 32.12  ? 218 LEU   A CA  1 
ATOM   1142 C C   . LEU   A 1 143 ? -4.247  -5.723  10.121 1.00 35.56  ? 218 LEU   A C   1 
ATOM   1143 O O   . LEU   A 1 143 ? -4.625  -4.559  10.294 1.00 54.75  ? 218 LEU   A O   1 
ATOM   1144 C CB  . LEU   A 1 143 ? -2.080  -6.025  8.896  1.00 29.95  ? 218 LEU   A CB  1 
ATOM   1145 C CG  . LEU   A 1 143 ? -0.552  -5.953  8.941  1.00 34.86  ? 218 LEU   A CG  1 
ATOM   1146 C CD1 . LEU   A 1 143 ? 0.032   -6.113  7.552  1.00 30.89  ? 218 LEU   A CD1 1 
ATOM   1147 C CD2 . LEU   A 1 143 ? -0.103  -4.642  9.560  1.00 30.42  ? 218 LEU   A CD2 1 
ATOM   1148 N N   . LEU   A 1 144 ? -5.094  -6.708  9.803  1.00 37.45  ? 219 LEU   A N   1 
ATOM   1149 C CA  . LEU   A 1 144 ? -6.534  -6.468  9.784  1.00 34.64  ? 219 LEU   A CA  1 
ATOM   1150 C C   . LEU   A 1 144 ? -7.026  -5.999  11.146 1.00 35.82  ? 219 LEU   A C   1 
ATOM   1151 O O   . LEU   A 1 144 ? -7.833  -5.067  11.237 1.00 46.68  ? 219 LEU   A O   1 
ATOM   1152 C CB  . LEU   A 1 144 ? -7.279  -7.734  9.356  1.00 33.52  ? 219 LEU   A CB  1 
ATOM   1153 C CG  . LEU   A 1 144 ? -7.182  -8.135  7.887  1.00 34.95  ? 219 LEU   A CG  1 
ATOM   1154 C CD1 . LEU   A 1 144 ? -7.862  -9.470  7.654  1.00 43.92  ? 219 LEU   A CD1 1 
ATOM   1155 C CD2 . LEU   A 1 144 ? -7.805  -7.072  7.006  1.00 38.18  ? 219 LEU   A CD2 1 
ATOM   1156 N N   . ALA   A 1 145 ? -6.550  -6.631  12.220 1.00 39.11  ? 220 ALA   A N   1 
ATOM   1157 C CA  . ALA   A 1 145 ? -6.938  -6.196  13.556 1.00 34.90  ? 220 ALA   A CA  1 
ATOM   1158 C C   . ALA   A 1 145 ? -6.402  -4.803  13.848 1.00 42.57  ? 220 ALA   A C   1 
ATOM   1159 O O   . ALA   A 1 145 ? -7.130  -3.938  14.348 1.00 49.87  ? 220 ALA   A O   1 
ATOM   1160 C CB  . ALA   A 1 145 ? -6.440  -7.191  14.602 1.00 30.48  ? 220 ALA   A CB  1 
ATOM   1161 N N   . LEU   A 1 146 ? -5.125  -4.568  13.545 1.00 39.37  ? 221 LEU   A N   1 
ATOM   1162 C CA  . LEU   A 1 146 ? -4.542  -3.260  13.818 1.00 37.28  ? 221 LEU   A CA  1 
ATOM   1163 C C   . LEU   A 1 146 ? -5.253  -2.174  13.025 1.00 31.48  ? 221 LEU   A C   1 
ATOM   1164 O O   . LEU   A 1 146 ? -5.546  -1.098  13.558 1.00 49.14  ? 221 LEU   A O   1 
ATOM   1165 C CB  . LEU   A 1 146 ? -3.048  -3.272  13.500 1.00 30.82  ? 221 LEU   A CB  1 
ATOM   1166 C CG  . LEU   A 1 146 ? -2.154  -4.075  14.442 1.00 35.95  ? 221 LEU   A CG  1 
ATOM   1167 C CD1 . LEU   A 1 146 ? -0.691  -3.923  14.059 1.00 26.80  ? 221 LEU   A CD1 1 
ATOM   1168 C CD2 . LEU   A 1 146 ? -2.376  -3.614  15.862 1.00 29.63  ? 221 LEU   A CD2 1 
ATOM   1169 N N   . ALA   A 1 147 ? -5.549  -2.441  11.754 1.00 32.98  ? 222 ALA   A N   1 
ATOM   1170 C CA  . ALA   A 1 147 ? -6.304  -1.482  10.957 1.00 32.97  ? 222 ALA   A CA  1 
ATOM   1171 C C   . ALA   A 1 147 ? -7.665  -1.194  11.575 1.00 37.32  ? 222 ALA   A C   1 
ATOM   1172 O O   . ALA   A 1 147 ? -8.163  -0.067  11.478 1.00 49.30  ? 222 ALA   A O   1 
ATOM   1173 C CB  . ALA   A 1 147 ? -6.470  -2.000  9.528  1.00 34.68  ? 222 ALA   A CB  1 
ATOM   1174 N N   . HIS   A 1 148 ? -8.280  -2.195  12.213 1.00 41.73  ? 223 HIS   A N   1 
ATOM   1175 C CA  . HIS   A 1 148 ? -9.551  -1.966  12.893 1.00 37.38  ? 223 HIS   A CA  1 
ATOM   1176 C C   . HIS   A 1 148 ? -9.358  -1.144  14.160 1.00 41.98  ? 223 HIS   A C   1 
ATOM   1177 O O   . HIS   A 1 148 ? -10.146 -0.235  14.443 1.00 53.49  ? 223 HIS   A O   1 
ATOM   1178 C CB  . HIS   A 1 148 ? -10.217 -3.299  13.225 1.00 40.35  ? 223 HIS   A CB  1 
ATOM   1179 C CG  . HIS   A 1 148 ? -11.514 -3.161  13.962 1.00 43.90  ? 223 HIS   A CG  1 
ATOM   1180 N ND1 . HIS   A 1 148 ? -12.653 -2.655  13.373 1.00 57.70  ? 223 HIS   A ND1 1 
ATOM   1181 C CD2 . HIS   A 1 148 ? -11.852 -3.462  15.239 1.00 46.04  ? 223 HIS   A CD2 1 
ATOM   1182 C CE1 . HIS   A 1 148 ? -13.637 -2.652  14.254 1.00 48.78  ? 223 HIS   A CE1 1 
ATOM   1183 N NE2 . HIS   A 1 148 ? -13.177 -3.135  15.395 1.00 51.87  ? 223 HIS   A NE2 1 
ATOM   1184 N N   . LEU   A 1 149 ? -8.322  -1.454  14.941 1.00 42.10  ? 224 LEU   A N   1 
ATOM   1185 C CA  . LEU   A 1 149 ? -8.057  -0.689  16.155 1.00 36.71  ? 224 LEU   A CA  1 
ATOM   1186 C C   . LEU   A 1 149 ? -7.630  0.735   15.830 1.00 38.57  ? 224 LEU   A C   1 
ATOM   1187 O O   . LEU   A 1 149 ? -8.124  1.693   16.436 1.00 48.43  ? 224 LEU   A O   1 
ATOM   1188 C CB  . LEU   A 1 149 ? -6.981  -1.379  16.991 1.00 32.23  ? 224 LEU   A CB  1 
ATOM   1189 C CG  . LEU   A 1 149 ? -7.377  -2.443  18.017 1.00 33.77  ? 224 LEU   A CG  1 
ATOM   1190 C CD1 . LEU   A 1 149 ? -8.089  -3.608  17.368 1.00 33.75  ? 224 LEU   A CD1 1 
ATOM   1191 C CD2 . LEU   A 1 149 ? -6.139  -2.928  18.750 1.00 39.29  ? 224 LEU   A CD2 1 
ATOM   1192 N N   . HIS   A 1 150 ? -6.708  0.893   14.881 1.00 39.43  ? 225 HIS   A N   1 
ATOM   1193 C CA  . HIS   A 1 150 ? -6.201  2.220   14.547 1.00 30.95  ? 225 HIS   A CA  1 
ATOM   1194 C C   . HIS   A 1 150 ? -7.241  3.105   13.876 1.00 38.45  ? 225 HIS   A C   1 
ATOM   1195 O O   . HIS   A 1 150 ? -7.129  4.331   13.964 1.00 50.18  ? 225 HIS   A O   1 
ATOM   1196 C CB  . HIS   A 1 150 ? -4.967  2.089   13.658 1.00 33.61  ? 225 HIS   A CB  1 
ATOM   1197 C CG  . HIS   A 1 150 ? -3.843  1.348   14.309 1.00 40.14  ? 225 HIS   A CG  1 
ATOM   1198 N ND1 . HIS   A 1 150 ? -2.713  0.955   13.625 1.00 28.33  ? 225 HIS   A ND1 1 
ATOM   1199 C CD2 . HIS   A 1 150 ? -3.678  0.930   15.586 1.00 29.74  ? 225 HIS   A CD2 1 
ATOM   1200 C CE1 . HIS   A 1 150 ? -1.899  0.327   14.455 1.00 39.62  ? 225 HIS   A CE1 1 
ATOM   1201 N NE2 . HIS   A 1 150 ? -2.461  0.299   15.650 1.00 36.52  ? 225 HIS   A NE2 1 
ATOM   1202 N N   . SER   A 1 151 ? -8.242  2.525   13.208 1.00 44.46  ? 226 SER   A N   1 
ATOM   1203 C CA  . SER   A 1 151 ? -9.304  3.335   12.622 1.00 40.31  ? 226 SER   A CA  1 
ATOM   1204 C C   . SER   A 1 151 ? -10.160 4.017   13.681 1.00 40.40  ? 226 SER   A C   1 
ATOM   1205 O O   . SER   A 1 151 ? -10.848 4.995   13.369 1.00 57.24  ? 226 SER   A O   1 
ATOM   1206 C CB  . SER   A 1 151 ? -10.197 2.476   11.725 1.00 37.34  ? 226 SER   A CB  1 
ATOM   1207 O OG  . SER   A 1 151 ? -10.891 1.512   12.495 1.00 54.62  ? 226 SER   A OG  1 
ATOM   1208 N N   . GLN   A 1 152 ? -10.136 3.525   14.919 1.00 51.44  ? 227 GLN   A N   1 
ATOM   1209 C CA  . GLN   A 1 152 ? -10.879 4.121   16.020 1.00 35.87  ? 227 GLN   A CA  1 
ATOM   1210 C C   . GLN   A 1 152 ? -9.980  4.904   16.969 1.00 43.23  ? 227 GLN   A C   1 
ATOM   1211 O O   . GLN   A 1 152 ? -10.385 5.194   18.101 1.00 55.97  ? 227 GLN   A O   1 
ATOM   1212 C CB  . GLN   A 1 152 ? -11.636 3.040   16.791 1.00 45.01  ? 227 GLN   A CB  1 
ATOM   1213 C CG  . GLN   A 1 152 ? -12.532 2.167   15.931 1.00 40.94  ? 227 GLN   A CG  1 
ATOM   1214 C CD  . GLN   A 1 152 ? -13.218 1.083   16.739 1.00 63.27  ? 227 GLN   A CD  1 
ATOM   1215 O OE1 . GLN   A 1 152 ? -13.067 -0.107  16.458 1.00 69.59  ? 227 GLN   A OE1 1 
ATOM   1216 N NE2 . GLN   A 1 152 ? -13.974 1.488   17.753 1.00 68.58  ? 227 GLN   A NE2 1 
ATOM   1217 N N   . GLY   A 1 153 ? -8.767  5.245   16.537 1.00 54.63  ? 228 GLY   A N   1 
ATOM   1218 C CA  . GLY   A 1 153 ? -7.856  5.951   17.415 1.00 38.26  ? 228 GLY   A CA  1 
ATOM   1219 C C   . GLY   A 1 153 ? -7.348  5.131   18.576 1.00 46.14  ? 228 GLY   A C   1 
ATOM   1220 O O   . GLY   A 1 153 ? -6.950  5.695   19.599 1.00 48.58  ? 228 GLY   A O   1 
ATOM   1221 N N   . LEU   A 1 154 ? -7.351  3.809   18.448 1.00 47.33  ? 229 LEU   A N   1 
ATOM   1222 C CA  . LEU   A 1 154 ? -6.881  2.917   19.495 1.00 36.79  ? 229 LEU   A CA  1 
ATOM   1223 C C   . LEU   A 1 154 ? -5.511  2.369   19.125 1.00 40.98  ? 229 LEU   A C   1 
ATOM   1224 O O   . LEU   A 1 154 ? -5.276  1.982   17.976 1.00 45.64  ? 229 LEU   A O   1 
ATOM   1225 C CB  . LEU   A 1 154 ? -7.857  1.757   19.705 1.00 37.16  ? 229 LEU   A CB  1 
ATOM   1226 C CG  . LEU   A 1 154 ? -9.344  2.090   19.816 1.00 37.69  ? 229 LEU   A CG  1 
ATOM   1227 C CD1 . LEU   A 1 154 ? -10.166 0.812   19.889 1.00 33.48  ? 229 LEU   A CD1 1 
ATOM   1228 C CD2 . LEU   A 1 154 ? -9.602  2.965   21.028 1.00 39.14  ? 229 LEU   A CD2 1 
ATOM   1229 N N   A VAL   A 1 155 ? -4.614  2.335   20.108 0.49 31.57  ? 230 VAL   A N   1 
ATOM   1230 N N   B VAL   A 1 155 ? -4.602  2.340   20.093 0.51 32.81  ? 230 VAL   A N   1 
ATOM   1231 C CA  A VAL   A 1 155 ? -3.269  1.791   19.954 0.49 35.31  ? 230 VAL   A CA  1 
ATOM   1232 C CA  B VAL   A 1 155 ? -3.277  1.768   19.893 0.51 36.86  ? 230 VAL   A CA  1 
ATOM   1233 C C   A VAL   A 1 155 ? -3.130  0.627   20.924 0.49 39.70  ? 230 VAL   A C   1 
ATOM   1234 C C   B VAL   A 1 155 ? -3.095  0.643   20.904 0.51 39.84  ? 230 VAL   A C   1 
ATOM   1235 O O   A VAL   A 1 155 ? -3.341  0.794   22.131 0.49 39.06  ? 230 VAL   A O   1 
ATOM   1236 O O   B VAL   A 1 155 ? -3.262  0.849   22.113 0.51 38.99  ? 230 VAL   A O   1 
ATOM   1237 C CB  A VAL   A 1 155 ? -2.191  2.853   20.218 0.49 35.32  ? 230 VAL   A CB  1 
ATOM   1238 C CB  B VAL   A 1 155 ? -2.169  2.827   20.011 0.51 35.83  ? 230 VAL   A CB  1 
ATOM   1239 C CG1 A VAL   A 1 155 ? -0.816  2.304   19.886 0.49 42.75  ? 230 VAL   A CG1 1 
ATOM   1240 C CG1 B VAL   A 1 155 ? -2.360  3.666   21.253 0.51 33.96  ? 230 VAL   A CG1 1 
ATOM   1241 C CG2 A VAL   A 1 155 ? -2.480  4.109   19.419 0.49 38.13  ? 230 VAL   A CG2 1 
ATOM   1242 C CG2 B VAL   A 1 155 ? -0.801  2.170   20.003 0.51 42.70  ? 230 VAL   A CG2 1 
ATOM   1243 N N   . HIS   A 1 156 ? -2.773  -0.550  20.401 1.00 36.93  ? 231 HIS   A N   1 
ATOM   1244 C CA  . HIS   A 1 156 ? -2.697  -1.738  21.249 1.00 36.74  ? 231 HIS   A CA  1 
ATOM   1245 C C   . HIS   A 1 156 ? -1.557  -1.634  22.256 1.00 36.58  ? 231 HIS   A C   1 
ATOM   1246 O O   . HIS   A 1 156 ? -1.737  -1.928  23.444 1.00 45.36  ? 231 HIS   A O   1 
ATOM   1247 C CB  . HIS   A 1 156 ? -2.536  -2.982  20.374 1.00 37.48  ? 231 HIS   A CB  1 
ATOM   1248 C CG  . HIS   A 1 156 ? -2.684  -4.274  21.116 1.00 40.30  ? 231 HIS   A CG  1 
ATOM   1249 N ND1 . HIS   A 1 156 ? -1.658  -4.834  21.848 1.00 37.54  ? 231 HIS   A ND1 1 
ATOM   1250 C CD2 . HIS   A 1 156 ? -3.733  -5.125  21.225 1.00 38.37  ? 231 HIS   A CD2 1 
ATOM   1251 C CE1 . HIS   A 1 156 ? -2.072  -5.970  22.382 1.00 41.88  ? 231 HIS   A CE1 1 
ATOM   1252 N NE2 . HIS   A 1 156 ? -3.327  -6.170  22.020 1.00 37.80  ? 231 HIS   A NE2 1 
ATOM   1253 N N   . LEU   A 1 157 ? -0.372  -1.230  21.796 1.00 47.05  ? 232 LEU   A N   1 
ATOM   1254 C CA  . LEU   A 1 157 ? 0.817   -1.045  22.625 1.00 37.17  ? 232 LEU   A CA  1 
ATOM   1255 C C   . LEU   A 1 157 ? 1.333   -2.345  23.232 1.00 40.33  ? 232 LEU   A C   1 
ATOM   1256 O O   . LEU   A 1 157 ? 2.129   -2.310  24.175 1.00 49.21  ? 232 LEU   A O   1 
ATOM   1257 C CB  . LEU   A 1 157 ? 0.575   -0.020  23.740 1.00 37.48  ? 232 LEU   A CB  1 
ATOM   1258 C CG  . LEU   A 1 157 ? 0.508   1.451   23.329 1.00 34.68  ? 232 LEU   A CG  1 
ATOM   1259 C CD1 . LEU   A 1 157 ? 0.325   2.326   24.553 1.00 31.29  ? 232 LEU   A CD1 1 
ATOM   1260 C CD2 . LEU   A 1 157 ? 1.758   1.855   22.563 1.00 34.84  ? 232 LEU   A CD2 1 
ATOM   1261 N N   . ASP   A 1 158 ? 0.917   -3.500  22.712 1.00 40.20  ? 233 ASP   A N   1 
ATOM   1262 C CA  . ASP   A 1 158 ? 1.457   -4.762  23.205 1.00 36.47  ? 233 ASP   A CA  1 
ATOM   1263 C C   . ASP   A 1 158 ? 1.326   -5.858  22.154 1.00 40.03  ? 233 ASP   A C   1 
ATOM   1264 O O   . ASP   A 1 158 ? 0.850   -6.959  22.450 1.00 40.32  ? 233 ASP   A O   1 
ATOM   1265 C CB  . ASP   A 1 158 ? 0.758   -5.174  24.502 1.00 44.62  ? 233 ASP   A CB  1 
ATOM   1266 C CG  . ASP   A 1 158 ? 1.567   -6.176  25.313 1.00 57.79  ? 233 ASP   A CG  1 
ATOM   1267 O OD1 . ASP   A 1 158 ? 2.730   -6.450  24.947 1.00 72.26  ? 233 ASP   A OD1 1 
ATOM   1268 O OD2 . ASP   A 1 158 ? 1.033   -6.693  26.317 1.00 61.89  ? 233 ASP   A OD2 1 
ATOM   1269 N N   . VAL   A 1 159 ? 1.745   -5.567  20.925 1.00 39.18  ? 234 VAL   A N   1 
ATOM   1270 C CA  . VAL   A 1 159 ? 1.710   -6.550  19.847 1.00 31.26  ? 234 VAL   A CA  1 
ATOM   1271 C C   . VAL   A 1 159 ? 2.957   -7.420  19.964 1.00 46.49  ? 234 VAL   A C   1 
ATOM   1272 O O   . VAL   A 1 159 ? 4.080   -6.938  19.804 1.00 48.29  ? 234 VAL   A O   1 
ATOM   1273 C CB  . VAL   A 1 159 ? 1.633   -5.877  18.474 1.00 32.96  ? 234 VAL   A CB  1 
ATOM   1274 C CG1 . VAL   A 1 159 ? 1.791   -6.913  17.376 1.00 38.04  ? 234 VAL   A CG1 1 
ATOM   1275 C CG2 . VAL   A 1 159 ? 0.317   -5.130  18.324 1.00 35.34  ? 234 VAL   A CG2 1 
ATOM   1276 N N   . LYS   A 1 160 ? 2.760   -8.701  20.253 1.00 39.51  ? 235 LYS   A N   1 
ATOM   1277 C CA  . LYS   A 1 160 ? 3.852   -9.657  20.363 1.00 30.72  ? 235 LYS   A CA  1 
ATOM   1278 C C   . LYS   A 1 160 ? 3.267   -11.055 20.237 1.00 35.27  ? 235 LYS   A C   1 
ATOM   1279 O O   . LYS   A 1 160 ? 2.050   -11.232 20.382 1.00 37.70  ? 235 LYS   A O   1 
ATOM   1280 C CB  . LYS   A 1 160 ? 4.606   -9.492  21.692 1.00 34.50  ? 235 LYS   A CB  1 
ATOM   1281 C CG  . LYS   A 1 160 ? 3.748   -9.615  22.932 1.00 29.20  ? 235 LYS   A CG  1 
ATOM   1282 C CD  . LYS   A 1 160 ? 4.601   -9.430  24.172 1.00 34.18  ? 235 LYS   A CD  1 
ATOM   1283 C CE  . LYS   A 1 160 ? 3.782   -9.531  25.443 1.00 54.05  ? 235 LYS   A CE  1 
ATOM   1284 N NZ  . LYS   A 1 160 ? 4.633   -9.302  26.644 1.00 67.64  ? 235 LYS   A NZ  1 
ATOM   1285 N N   . PRO   A 1 161 ? 4.097   -12.064 19.948 1.00 42.72  ? 236 PRO   A N   1 
ATOM   1286 C CA  . PRO   A 1 161 ? 3.548   -13.410 19.714 1.00 44.52  ? 236 PRO   A CA  1 
ATOM   1287 C C   . PRO   A 1 161 ? 2.684   -13.937 20.844 1.00 37.35  ? 236 PRO   A C   1 
ATOM   1288 O O   . PRO   A 1 161 ? 1.755   -14.712 20.584 1.00 46.83  ? 236 PRO   A O   1 
ATOM   1289 C CB  . PRO   A 1 161 ? 4.807   -14.264 19.522 1.00 33.67  ? 236 PRO   A CB  1 
ATOM   1290 C CG  . PRO   A 1 161 ? 5.801   -13.317 18.957 1.00 32.45  ? 236 PRO   A CG  1 
ATOM   1291 C CD  . PRO   A 1 161 ? 5.542   -12.012 19.660 1.00 39.32  ? 236 PRO   A CD  1 
ATOM   1292 N N   . ALA   A 1 162 ? 2.945   -13.536 22.091 1.00 37.23  ? 237 ALA   A N   1 
ATOM   1293 C CA  . ALA   A 1 162 ? 2.140   -14.021 23.205 1.00 24.97  ? 237 ALA   A CA  1 
ATOM   1294 C C   . ALA   A 1 162 ? 0.727   -13.456 23.194 1.00 38.81  ? 237 ALA   A C   1 
ATOM   1295 O O   . ALA   A 1 162 ? -0.144  -13.992 23.889 1.00 42.62  ? 237 ALA   A O   1 
ATOM   1296 C CB  . ALA   A 1 162 ? 2.807   -13.682 24.537 1.00 29.17  ? 237 ALA   A CB  1 
ATOM   1297 N N   . ASN   A 1 163 ? 0.481   -12.385 22.438 1.00 36.93  ? 238 ASN   A N   1 
ATOM   1298 C CA  . ASN   A 1 163 ? -0.832  -11.756 22.375 1.00 38.80  ? 238 ASN   A CA  1 
ATOM   1299 C C   . ASN   A 1 163 ? -1.548  -12.017 21.056 1.00 40.29  ? 238 ASN   A C   1 
ATOM   1300 O O   . ASN   A 1 163 ? -2.596  -11.417 20.805 1.00 40.29  ? 238 ASN   A O   1 
ATOM   1301 C CB  . ASN   A 1 163 ? -0.719  -10.249 22.613 1.00 38.98  ? 238 ASN   A CB  1 
ATOM   1302 C CG  . ASN   A 1 163 ? -0.313  -9.915  24.030 1.00 38.26  ? 238 ASN   A CG  1 
ATOM   1303 O OD1 . ASN   A 1 163 ? -0.426  -10.745 24.931 1.00 41.32  ? 238 ASN   A OD1 1 
ATOM   1304 N ND2 . ASN   A 1 163 ? 0.159   -8.692  24.239 1.00 38.50  ? 238 ASN   A ND2 1 
ATOM   1305 N N   . ILE   A 1 164 ? -1.010  -12.890 20.209 1.00 43.86  ? 239 ILE   A N   1 
ATOM   1306 C CA  . ILE   A 1 164 ? -1.671  -13.326 18.984 1.00 32.95  ? 239 ILE   A CA  1 
ATOM   1307 C C   . ILE   A 1 164 ? -2.017  -14.800 19.144 1.00 41.93  ? 239 ILE   A C   1 
ATOM   1308 O O   . ILE   A 1 164 ? -1.151  -15.611 19.496 1.00 43.98  ? 239 ILE   A O   1 
ATOM   1309 C CB  . ILE   A 1 164 ? -0.780  -13.092 17.753 1.00 41.92  ? 239 ILE   A CB  1 
ATOM   1310 C CG1 . ILE   A 1 164 ? -0.427  -11.608 17.626 1.00 40.41  ? 239 ILE   A CG1 1 
ATOM   1311 C CG2 . ILE   A 1 164 ? -1.468  -13.580 16.496 1.00 35.37  ? 239 ILE   A CG2 1 
ATOM   1312 C CD1 . ILE   A 1 164 ? 0.561   -11.318 16.519 1.00 42.40  ? 239 ILE   A CD1 1 
ATOM   1313 N N   . PHE   A 1 165 ? -3.278  -15.147 18.895 1.00 36.72  ? 240 PHE   A N   1 
ATOM   1314 C CA  . PHE   A 1 165 ? -3.786  -16.485 19.167 1.00 32.62  ? 240 PHE   A CA  1 
ATOM   1315 C C   . PHE   A 1 165 ? -4.285  -17.116 17.879 1.00 37.82  ? 240 PHE   A C   1 
ATOM   1316 O O   . PHE   A 1 165 ? -5.001  -16.473 17.107 1.00 42.64  ? 240 PHE   A O   1 
ATOM   1317 C CB  . PHE   A 1 165 ? -4.908  -16.447 20.206 1.00 39.49  ? 240 PHE   A CB  1 
ATOM   1318 C CG  . PHE   A 1 165 ? -4.502  -15.816 21.501 1.00 34.70  ? 240 PHE   A CG  1 
ATOM   1319 C CD1 . PHE   A 1 165 ? -3.876  -16.561 22.485 1.00 34.32  ? 240 PHE   A CD1 1 
ATOM   1320 C CD2 . PHE   A 1 165 ? -4.736  -14.471 21.730 1.00 38.24  ? 240 PHE   A CD2 1 
ATOM   1321 C CE1 . PHE   A 1 165 ? -3.494  -15.975 23.674 1.00 39.11  ? 240 PHE   A CE1 1 
ATOM   1322 C CE2 . PHE   A 1 165 ? -4.359  -13.882 22.915 1.00 35.79  ? 240 PHE   A CE2 1 
ATOM   1323 C CZ  . PHE   A 1 165 ? -3.737  -14.633 23.890 1.00 38.80  ? 240 PHE   A CZ  1 
ATOM   1324 N N   . LEU   A 1 166 ? -3.910  -18.372 17.655 1.00 42.39  ? 241 LEU   A N   1 
ATOM   1325 C CA  . LEU   A 1 166 ? -4.257  -19.056 16.417 1.00 42.73  ? 241 LEU   A CA  1 
ATOM   1326 C C   . LEU   A 1 166 ? -5.757  -19.307 16.321 1.00 49.75  ? 241 LEU   A C   1 
ATOM   1327 O O   . LEU   A 1 166 ? -6.413  -19.662 17.304 1.00 47.54  ? 241 LEU   A O   1 
ATOM   1328 C CB  . LEU   A 1 166 ? -3.513  -20.385 16.323 1.00 39.45  ? 241 LEU   A CB  1 
ATOM   1329 C CG  . LEU   A 1 166 ? -2.141  -20.384 15.653 1.00 47.37  ? 241 LEU   A CG  1 
ATOM   1330 C CD1 . LEU   A 1 166 ? -1.194  -19.417 16.342 1.00 47.02  ? 241 LEU   A CD1 1 
ATOM   1331 C CD2 . LEU   A 1 166 ? -1.577  -21.796 15.655 1.00 55.11  ? 241 LEU   A CD2 1 
ATOM   1332 N N   . GLY   A 1 167 ? -6.299  -19.133 15.119 1.00 47.27  ? 242 GLY   A N   1 
ATOM   1333 C CA  . GLY   A 1 167 ? -7.682  -19.448 14.858 1.00 31.02  ? 242 GLY   A CA  1 
ATOM   1334 C C   . GLY   A 1 167 ? -7.797  -20.643 13.937 1.00 46.00  ? 242 GLY   A C   1 
ATOM   1335 O O   . GLY   A 1 167 ? -6.793  -21.191 13.468 1.00 54.87  ? 242 GLY   A O   1 
ATOM   1336 N N   . PRO   A 1 168 ? -9.024  -21.079 13.665 1.00 35.29  ? 243 PRO   A N   1 
ATOM   1337 C CA  . PRO   A 1 168 ? -9.212  -22.225 12.772 1.00 38.77  ? 243 PRO   A CA  1 
ATOM   1338 C C   . PRO   A 1 168 ? -8.775  -21.902 11.353 1.00 41.55  ? 243 PRO   A C   1 
ATOM   1339 O O   . PRO   A 1 168 ? -8.853  -20.760 10.898 1.00 46.50  ? 243 PRO   A O   1 
ATOM   1340 C CB  . PRO   A 1 168 ? -10.721 -22.486 12.842 1.00 40.92  ? 243 PRO   A CB  1 
ATOM   1341 C CG  . PRO   A 1 168 ? -11.164 -21.834 14.118 1.00 41.24  ? 243 PRO   A CG  1 
ATOM   1342 C CD  . PRO   A 1 168 ? -10.290 -20.630 14.264 1.00 45.76  ? 243 PRO   A CD  1 
ATOM   1343 N N   . ARG   A 1 169 ? -8.306  -22.937 10.657 1.00 52.24  ? 244 ARG   A N   1 
ATOM   1344 C CA  . ARG   A 1 169 ? -7.865  -22.825 9.266  1.00 46.47  ? 244 ARG   A CA  1 
ATOM   1345 C C   . ARG   A 1 169 ? -6.788  -21.757 9.097  1.00 49.59  ? 244 ARG   A C   1 
ATOM   1346 O O   . ARG   A 1 169 ? -6.822  -20.960 8.157  1.00 47.05  ? 244 ARG   A O   1 
ATOM   1347 C CB  . ARG   A 1 169 ? -9.044  -22.555 8.334  1.00 46.63  ? 244 ARG   A CB  1 
ATOM   1348 C CG  . ARG   A 1 169 ? -9.966  -23.739 8.170  1.00 43.07  ? 244 ARG   A CG  1 
ATOM   1349 C CD  . ARG   A 1 169 ? -11.032 -23.456 7.136  1.00 56.41  ? 244 ARG   A CD  1 
ATOM   1350 N NE  . ARG   A 1 169 ? -11.859 -24.628 6.881  1.00 60.45  ? 244 ARG   A NE  1 
ATOM   1351 C CZ  . ARG   A 1 169 ? -12.892 -24.982 7.631  1.00 74.15  ? 244 ARG   A CZ  1 
ATOM   1352 N NH1 . ARG   A 1 169 ? -13.243 -24.281 8.697  1.00 72.21  ? 244 ARG   A NH1 1 
ATOM   1353 N NH2 . ARG   A 1 169 ? -13.588 -26.068 7.306  1.00 74.23  ? 244 ARG   A NH2 1 
ATOM   1354 N N   . GLY   A 1 170 ? -5.829  -21.732 10.017 1.00 41.88  ? 245 GLY   A N   1 
ATOM   1355 C CA  . GLY   A 1 170 ? -4.663  -20.887 9.850  1.00 38.70  ? 245 GLY   A CA  1 
ATOM   1356 C C   . GLY   A 1 170 ? -4.859  -19.415 10.120 1.00 48.82  ? 245 GLY   A C   1 
ATOM   1357 O O   . GLY   A 1 170 ? -3.937  -18.632 9.861  1.00 62.86  ? 245 GLY   A O   1 
ATOM   1358 N N   . ARG   A 1 171 ? -6.017  -19.000 10.632 1.00 53.30  ? 246 ARG   A N   1 
ATOM   1359 C CA  . ARG   A 1 171 ? -6.227  -17.606 10.983 1.00 44.64  ? 246 ARG   A CA  1 
ATOM   1360 C C   . ARG   A 1 171 ? -5.710  -17.338 12.391 1.00 51.87  ? 246 ARG   A C   1 
ATOM   1361 O O   . ARG   A 1 171 ? -5.256  -18.238 13.101 1.00 54.64  ? 246 ARG   A O   1 
ATOM   1362 C CB  . ARG   A 1 171 ? -7.704  -17.236 10.868 1.00 48.18  ? 246 ARG   A CB  1 
ATOM   1363 C CG  . ARG   A 1 171 ? -8.378  -17.726 9.596  1.00 55.90  ? 246 ARG   A CG  1 
ATOM   1364 C CD  . ARG   A 1 171 ? -7.854  -17.044 8.332  1.00 61.10  ? 246 ARG   A CD  1 
ATOM   1365 N NE  . ARG   A 1 171 ? -7.839  -15.583 8.370  1.00 70.10  ? 246 ARG   A NE  1 
ATOM   1366 C CZ  . ARG   A 1 171 ? -8.901  -14.803 8.537  1.00 82.71  ? 246 ARG   A CZ  1 
ATOM   1367 N NH1 . ARG   A 1 171 ? -10.098 -15.305 8.799  1.00 68.56  ? 246 ARG   A NH1 1 
ATOM   1368 N NH2 . ARG   A 1 171 ? -8.756  -13.483 8.445  1.00 71.04  ? 246 ARG   A NH2 1 
ATOM   1369 N N   . CYS   A 1 172 ? -5.769  -16.075 12.803 1.00 41.65  ? 247 CYS   A N   1 
ATOM   1370 C CA  . CYS   A 1 172 ? -5.372  -15.705 14.152 1.00 53.08  ? 247 CYS   A CA  1 
ATOM   1371 C C   . CYS   A 1 172 ? -6.056  -14.399 14.507 1.00 42.93  ? 247 CYS   A C   1 
ATOM   1372 O O   . CYS   A 1 172 ? -6.583  -13.704 13.636 1.00 45.24  ? 247 CYS   A O   1 
ATOM   1373 C CB  . CYS   A 1 172 ? -3.856  -15.565 14.284 1.00 44.10  ? 247 CYS   A CB  1 
ATOM   1374 S SG  . CYS   A 1 172 ? -3.168  -14.218 13.319 1.00 55.46  ? 247 CYS   A SG  1 
ATOM   1375 N N   . LYS   A 1 173 ? -6.053  -14.084 15.801 1.00 41.18  ? 248 LYS   A N   1 
ATOM   1376 C CA  . LYS   A 1 173 ? -6.739  -12.906 16.319 1.00 39.34  ? 248 LYS   A CA  1 
ATOM   1377 C C   . LYS   A 1 173 ? -5.840  -12.177 17.305 1.00 41.30  ? 248 LYS   A C   1 
ATOM   1378 O O   . LYS   A 1 173 ? -5.245  -12.803 18.186 1.00 41.33  ? 248 LYS   A O   1 
ATOM   1379 C CB  . LYS   A 1 173 ? -8.056  -13.288 17.011 1.00 38.15  ? 248 LYS   A CB  1 
ATOM   1380 C CG  . LYS   A 1 173 ? -8.923  -14.289 16.265 1.00 42.20  ? 248 LYS   A CG  1 
ATOM   1381 C CD  . LYS   A 1 173 ? -10.291 -14.438 16.915 1.00 46.70  ? 248 LYS   A CD  1 
ATOM   1382 C CE  . LYS   A 1 173 ? -10.800 -15.872 16.836 1.00 73.04  ? 248 LYS   A CE  1 
ATOM   1383 N NZ  . LYS   A 1 173 ? -10.025 -16.771 17.739 1.00 71.52  ? 248 LYS   A NZ  1 
ATOM   1384 N N   . LEU   A 1 174 ? -5.761  -10.856 17.172 1.00 30.36  ? 249 LEU   A N   1 
ATOM   1385 C CA  . LEU   A 1 174 ? -5.041  -10.050 18.147 1.00 26.12  ? 249 LEU   A CA  1 
ATOM   1386 C C   . LEU   A 1 174 ? -5.786  -10.065 19.474 1.00 36.74  ? 249 LEU   A C   1 
ATOM   1387 O O   . LEU   A 1 174 ? -7.021  -10.082 19.513 1.00 39.48  ? 249 LEU   A O   1 
ATOM   1388 C CB  . LEU   A 1 174 ? -4.882  -8.618  17.635 1.00 30.19  ? 249 LEU   A CB  1 
ATOM   1389 C CG  . LEU   A 1 174 ? -4.064  -7.651  18.489 1.00 38.71  ? 249 LEU   A CG  1 
ATOM   1390 C CD1 . LEU   A 1 174 ? -2.620  -8.118  18.592 1.00 34.77  ? 249 LEU   A CD1 1 
ATOM   1391 C CD2 . LEU   A 1 174 ? -4.138  -6.250  17.907 1.00 33.41  ? 249 LEU   A CD2 1 
ATOM   1392 N N   . GLY   A 1 175 ? -5.027  -10.049 20.566 1.00 40.19  ? 250 GLY   A N   1 
ATOM   1393 C CA  . GLY   A 1 175 ? -5.611  -10.163 21.887 1.00 36.05  ? 250 GLY   A CA  1 
ATOM   1394 C C   . GLY   A 1 175 ? -4.889  -9.374  22.958 1.00 33.22  ? 250 GLY   A C   1 
ATOM   1395 O O   . GLY   A 1 175 ? -3.989  -8.584  22.661 1.00 40.20  ? 250 GLY   A O   1 
ATOM   1396 N N   . ASP   A 1 176 ? -5.289  -9.596  24.211 1.00 42.95  ? 251 ASP   A N   1 
ATOM   1397 C CA  . ASP   A 1 176 ? -4.769  -8.897  25.380 1.00 39.24  ? 251 ASP   A CA  1 
ATOM   1398 C C   . ASP   A 1 176 ? -4.806  -7.387  25.183 1.00 43.70  ? 251 ASP   A C   1 
ATOM   1399 O O   . ASP   A 1 176 ? -3.801  -6.785  24.792 1.00 45.98  ? 251 ASP   A O   1 
ATOM   1400 C CB  . ASP   A 1 176 ? -3.345  -9.356  25.703 1.00 59.06  ? 251 ASP   A CB  1 
ATOM   1401 C CG  . ASP   A 1 176 ? -2.954  -9.068  27.145 1.00 65.98  ? 251 ASP   A CG  1 
ATOM   1402 O OD1 . ASP   A 1 176 ? -3.448  -8.070  27.717 1.00 66.46  ? 251 ASP   A OD1 1 
ATOM   1403 O OD2 . ASP   A 1 176 ? -2.154  -9.839  27.711 1.00 69.85  ? 251 ASP   A OD2 1 
ATOM   1404 N N   . PHE   A 1 177 ? -5.957  -6.771  25.461 1.00 44.37  ? 252 PHE   A N   1 
ATOM   1405 C CA  . PHE   A 1 177 ? -6.126  -5.332  25.330 1.00 39.16  ? 252 PHE   A CA  1 
ATOM   1406 C C   . PHE   A 1 177 ? -5.963  -4.626  26.667 1.00 36.91  ? 252 PHE   A C   1 
ATOM   1407 O O   . PHE   A 1 177 ? -6.563  -3.571  26.889 1.00 42.82  ? 252 PHE   A O   1 
ATOM   1408 C CB  . PHE   A 1 177 ? -7.486  -5.022  24.703 1.00 34.82  ? 252 PHE   A CB  1 
ATOM   1409 C CG  . PHE   A 1 177 ? -7.702  -5.705  23.376 1.00 32.64  ? 252 PHE   A CG  1 
ATOM   1410 C CD1 . PHE   A 1 177 ? -6.969  -5.334  22.264 1.00 47.97  ? 252 PHE   A CD1 1 
ATOM   1411 C CD2 . PHE   A 1 177 ? -8.633  -6.714  23.242 1.00 55.31  ? 252 PHE   A CD2 1 
ATOM   1412 C CE1 . PHE   A 1 177 ? -7.161  -5.957  21.044 1.00 46.53  ? 252 PHE   A CE1 1 
ATOM   1413 C CE2 . PHE   A 1 177 ? -8.831  -7.341  22.026 1.00 51.15  ? 252 PHE   A CE2 1 
ATOM   1414 C CZ  . PHE   A 1 177 ? -8.094  -6.962  20.926 1.00 36.50  ? 252 PHE   A CZ  1 
ATOM   1415 N N   . GLY   A 1 178 ? -5.155  -5.194  27.563 1.00 32.60  ? 253 GLY   A N   1 
ATOM   1416 C CA  . GLY   A 1 178 ? -4.945  -4.579  28.860 1.00 36.17  ? 253 GLY   A CA  1 
ATOM   1417 C C   . GLY   A 1 178 ? -4.086  -3.338  28.802 1.00 38.00  ? 253 GLY   A C   1 
ATOM   1418 O O   . GLY   A 1 178 ? -4.143  -2.512  29.717 1.00 50.61  ? 253 GLY   A O   1 
ATOM   1419 N N   . LEU   A 1 179 ? -3.277  -3.191  27.752 1.00 30.21  ? 254 LEU   A N   1 
ATOM   1420 C CA  . LEU   A 1 179 ? -2.442  -2.007  27.594 1.00 42.49  ? 254 LEU   A CA  1 
ATOM   1421 C C   . LEU   A 1 179 ? -2.979  -1.031  26.557 1.00 35.61  ? 254 LEU   A C   1 
ATOM   1422 O O   . LEU   A 1 179 ? -2.435  0.072   26.428 1.00 43.25  ? 254 LEU   A O   1 
ATOM   1423 C CB  . LEU   A 1 179 ? -1.006  -2.397  27.201 1.00 35.76  ? 254 LEU   A CB  1 
ATOM   1424 C CG  . LEU   A 1 179 ? -0.207  -3.338  28.105 1.00 44.23  ? 254 LEU   A CG  1 
ATOM   1425 C CD1 . LEU   A 1 179 ? 1.281   -3.044  27.990 1.00 50.18  ? 254 LEU   A CD1 1 
ATOM   1426 C CD2 . LEU   A 1 179 ? -0.658  -3.249  29.553 1.00 48.35  ? 254 LEU   A CD2 1 
ATOM   1427 N N   . LEU   A 1 180 ? -4.012  -1.411  25.810 1.00 50.43  ? 255 LEU   A N   1 
ATOM   1428 C CA  . LEU   A 1 180 ? -4.565  -0.535  24.785 1.00 36.84  ? 255 LEU   A CA  1 
ATOM   1429 C C   . LEU   A 1 180 ? -5.012  0.787   25.395 1.00 44.60  ? 255 LEU   A C   1 
ATOM   1430 O O   . LEU   A 1 180 ? -5.660  0.815   26.445 1.00 47.00  ? 255 LEU   A O   1 
ATOM   1431 C CB  . LEU   A 1 180 ? -5.742  -1.220  24.087 1.00 40.81  ? 255 LEU   A CB  1 
ATOM   1432 C CG  . LEU   A 1 180 ? -6.547  -0.432  23.044 1.00 30.68  ? 255 LEU   A CG  1 
ATOM   1433 C CD1 . LEU   A 1 180 ? -6.997  -1.371  21.948 1.00 35.45  ? 255 LEU   A CD1 1 
ATOM   1434 C CD2 . LEU   A 1 180 ? -7.760  0.267   23.656 1.00 45.85  ? 255 LEU   A CD2 1 
ATOM   1435 N N   . VAL   A 1 181 ? -4.660  1.888   24.733 1.00 44.01  ? 256 VAL   A N   1 
ATOM   1436 C CA  . VAL   A 1 181 ? -5.101  3.214   25.139 1.00 38.58  ? 256 VAL   A CA  1 
ATOM   1437 C C   . VAL   A 1 181 ? -5.759  3.884   23.943 1.00 46.06  ? 256 VAL   A C   1 
ATOM   1438 O O   . VAL   A 1 181 ? -5.471  3.558   22.787 1.00 40.52  ? 256 VAL   A O   1 
ATOM   1439 C CB  . VAL   A 1 181 ? -3.945  4.088   25.683 1.00 39.12  ? 256 VAL   A CB  1 
ATOM   1440 C CG1 . VAL   A 1 181 ? -3.106  3.309   26.678 1.00 62.85  ? 256 VAL   A CG1 1 
ATOM   1441 C CG2 . VAL   A 1 181 ? -3.087  4.603   24.549 1.00 36.55  ? 256 VAL   A CG2 1 
ATOM   1442 N N   . GLU   A 1 182 ? -6.665  4.812   24.229 1.00 44.10  ? 257 GLU   A N   1 
ATOM   1443 C CA  . GLU   A 1 182 ? -7.358  5.576   23.204 1.00 47.77  ? 257 GLU   A CA  1 
ATOM   1444 C C   . GLU   A 1 182 ? -6.709  6.949   23.094 1.00 53.02  ? 257 GLU   A C   1 
ATOM   1445 O O   . GLU   A 1 182 ? -6.501  7.623   24.108 1.00 60.00  ? 257 GLU   A O   1 
ATOM   1446 C CB  . GLU   A 1 182 ? -8.846  5.709   23.535 1.00 44.19  ? 257 GLU   A CB  1 
ATOM   1447 C CG  . GLU   A 1 182 ? -9.656  6.399   22.452 1.00 55.64  ? 257 GLU   A CG  1 
ATOM   1448 C CD  . GLU   A 1 182 ? -11.138 6.430   22.760 1.00 69.17  ? 257 GLU   A CD  1 
ATOM   1449 O OE1 . GLU   A 1 182 ? -11.520 6.043   23.885 1.00 92.35  ? 257 GLU   A OE1 1 
ATOM   1450 O OE2 . GLU   A 1 182 ? -11.923 6.839   21.877 1.00 79.74  ? 257 GLU   A OE2 1 
ATOM   1451 N N   . LEU   A 1 183 ? -6.379  7.353   21.870 1.00 46.08  ? 258 LEU   A N   1 
ATOM   1452 C CA  . LEU   A 1 183 ? -5.716  8.630   21.650 1.00 54.03  ? 258 LEU   A CA  1 
ATOM   1453 C C   . LEU   A 1 183 ? -6.705  9.777   21.821 1.00 60.94  ? 258 LEU   A C   1 
ATOM   1454 O O   . LEU   A 1 183 ? -7.781  9.777   21.215 1.00 73.09  ? 258 LEU   A O   1 
ATOM   1455 C CB  . LEU   A 1 183 ? -5.091  8.662   20.258 1.00 55.99  ? 258 LEU   A CB  1 
ATOM   1456 C CG  . LEU   A 1 183 ? -4.031  7.589   20.020 1.00 46.24  ? 258 LEU   A CG  1 
ATOM   1457 C CD1 . LEU   A 1 183 ? -3.515  7.656   18.595 1.00 55.36  ? 258 LEU   A CD1 1 
ATOM   1458 C CD2 . LEU   A 1 183 ? -2.891  7.746   21.017 1.00 43.96  ? 258 LEU   A CD2 1 
ATOM   1459 N N   . GLY   A 1 184 ? -6.336  10.753  22.650 1.00 61.39  ? 259 GLY   A N   1 
ATOM   1460 C CA  . GLY   A 1 184 ? -7.192  11.897  22.917 1.00 56.62  ? 259 GLY   A CA  1 
ATOM   1461 C C   . GLY   A 1 184 ? -7.613  12.006  24.370 1.00 78.55  ? 259 GLY   A C   1 
ATOM   1462 O O   . GLY   A 1 184 ? -7.630  11.013  25.099 1.00 90.98  ? 259 GLY   A O   1 
ATOM   1463 N N   . GLU   A 1 190 ? -2.584  6.615   31.888 1.00 86.47  ? 265 GLU   A N   1 
ATOM   1464 C CA  . GLU   A 1 190 ? -3.342  5.849   30.905 1.00 81.98  ? 265 GLU   A CA  1 
ATOM   1465 C C   . GLU   A 1 190 ? -2.459  4.825   30.197 1.00 71.01  ? 265 GLU   A C   1 
ATOM   1466 O O   . GLU   A 1 190 ? -2.917  3.740   29.841 1.00 90.04  ? 265 GLU   A O   1 
ATOM   1467 C CB  . GLU   A 1 190 ? -3.990  6.787   29.880 1.00 103.71 ? 265 GLU   A CB  1 
ATOM   1468 C CG  . GLU   A 1 190 ? -3.014  7.733   29.187 1.00 109.96 ? 265 GLU   A CG  1 
ATOM   1469 C CD  . GLU   A 1 190 ? -3.684  8.615   28.148 1.00 111.07 ? 265 GLU   A CD  1 
ATOM   1470 O OE1 . GLU   A 1 190 ? -4.921  8.526   27.997 1.00 123.76 ? 265 GLU   A OE1 1 
ATOM   1471 O OE2 . GLU   A 1 190 ? -2.974  9.398   27.480 1.00 96.24  ? 265 GLU   A OE2 1 
ATOM   1472 N N   . VAL   A 1 191 ? -1.190  5.173   30.001 1.00 61.33  ? 266 VAL   A N   1 
ATOM   1473 C CA  . VAL   A 1 191 ? -0.232  4.324   29.301 1.00 48.60  ? 266 VAL   A CA  1 
ATOM   1474 C C   . VAL   A 1 191 ? 0.612   3.590   30.334 1.00 68.60  ? 266 VAL   A C   1 
ATOM   1475 O O   . VAL   A 1 191 ? 1.094   4.197   31.300 1.00 72.55  ? 266 VAL   A O   1 
ATOM   1476 C CB  . VAL   A 1 191 ? 0.651   5.150   28.349 1.00 60.39  ? 266 VAL   A CB  1 
ATOM   1477 C CG1 . VAL   A 1 191 ? 1.748   4.289   27.752 1.00 66.76  ? 266 VAL   A CG1 1 
ATOM   1478 C CG2 . VAL   A 1 191 ? -0.194  5.769   27.246 1.00 72.22  ? 266 VAL   A CG2 1 
ATOM   1479 N N   . GLN   A 1 192 ? 0.788   2.288   30.135 1.00 56.72  ? 267 GLN   A N   1 
ATOM   1480 C CA  . GLN   A 1 192 ? 1.534   1.440   31.050 1.00 50.53  ? 267 GLN   A CA  1 
ATOM   1481 C C   . GLN   A 1 192 ? 2.816   0.953   30.387 1.00 57.15  ? 267 GLN   A C   1 
ATOM   1482 O O   . GLN   A 1 192 ? 3.034   1.129   29.185 1.00 50.47  ? 267 GLN   A O   1 
ATOM   1483 C CB  . GLN   A 1 192 ? 0.677   0.253   31.501 1.00 64.62  ? 267 GLN   A CB  1 
ATOM   1484 C CG  . GLN   A 1 192 ? -0.648  0.656   32.122 1.00 65.55  ? 267 GLN   A CG  1 
ATOM   1485 C CD  . GLN   A 1 192 ? -1.528  -0.535  32.431 1.00 82.20  ? 267 GLN   A CD  1 
ATOM   1486 O OE1 . GLN   A 1 192 ? -1.327  -1.226  33.429 1.00 106.69 ? 267 GLN   A OE1 1 
ATOM   1487 N NE2 . GLN   A 1 192 ? -2.506  -0.788  31.570 1.00 82.92  ? 267 GLN   A NE2 1 
ATOM   1488 N N   . GLU   A 1 193 ? 3.668   0.328   31.197 1.00 69.72  ? 268 GLU   A N   1 
ATOM   1489 C CA  . GLU   A 1 193 ? 4.955   -0.163  30.720 1.00 56.56  ? 268 GLU   A CA  1 
ATOM   1490 C C   . GLU   A 1 193 ? 4.748   -1.327  29.758 1.00 44.40  ? 268 GLU   A C   1 
ATOM   1491 O O   . GLU   A 1 193 ? 4.175   -2.356  30.133 1.00 65.82  ? 268 GLU   A O   1 
ATOM   1492 C CB  . GLU   A 1 193 ? 5.819   -0.598  31.901 1.00 68.92  ? 268 GLU   A CB  1 
ATOM   1493 C CG  . GLU   A 1 193 ? 5.992   0.459   32.983 1.00 93.26  ? 268 GLU   A CG  1 
ATOM   1494 C CD  . GLU   A 1 193 ? 7.046   1.493   32.636 1.00 84.91  ? 268 GLU   A CD  1 
ATOM   1495 O OE1 . GLU   A 1 193 ? 7.754   1.307   31.623 1.00 73.69  ? 268 GLU   A OE1 1 
ATOM   1496 O OE2 . GLU   A 1 193 ? 7.168   2.489   33.381 1.00 83.96  ? 268 GLU   A OE2 1 
ATOM   1497 N N   . GLY   A 1 194 ? 5.218   -1.168  28.519 1.00 56.37  ? 269 GLY   A N   1 
ATOM   1498 C CA  . GLY   A 1 194 ? 5.177   -2.238  27.545 1.00 47.95  ? 269 GLY   A CA  1 
ATOM   1499 C C   . GLY   A 1 194 ? 6.436   -3.090  27.567 1.00 51.68  ? 269 GLY   A C   1 
ATOM   1500 O O   . GLY   A 1 194 ? 7.340   -2.911  28.382 1.00 56.63  ? 269 GLY   A O   1 
ATOM   1501 N N   . ASP   A 1 195 ? 6.484   -4.041  26.645 1.00 56.02  ? 270 ASP   A N   1 
ATOM   1502 C CA  . ASP   A 1 195 ? 7.638   -4.923  26.541 1.00 47.67  ? 270 ASP   A CA  1 
ATOM   1503 C C   . ASP   A 1 195 ? 8.733   -4.224  25.744 1.00 43.25  ? 270 ASP   A C   1 
ATOM   1504 O O   . ASP   A 1 195 ? 8.496   -3.842  24.592 1.00 48.50  ? 270 ASP   A O   1 
ATOM   1505 C CB  . ASP   A 1 195 ? 7.247   -6.239  25.874 1.00 41.64  ? 270 ASP   A CB  1 
ATOM   1506 C CG  . ASP   A 1 195 ? 8.234   -7.361  26.158 1.00 44.80  ? 270 ASP   A CG  1 
ATOM   1507 O OD1 . ASP   A 1 195 ? 9.456   -7.099  26.186 1.00 55.30  ? 270 ASP   A OD1 1 
ATOM   1508 O OD2 . ASP   A 1 195 ? 7.786   -8.512  26.353 1.00 54.84  ? 270 ASP   A OD2 1 
ATOM   1509 N N   . PRO   A 1 196 ? 9.928   -4.029  26.308 1.00 49.24  ? 271 PRO   A N   1 
ATOM   1510 C CA  . PRO   A 1 196 ? 10.984  -3.330  25.558 1.00 44.26  ? 271 PRO   A CA  1 
ATOM   1511 C C   . PRO   A 1 196 ? 11.473  -4.089  24.338 1.00 47.11  ? 271 PRO   A C   1 
ATOM   1512 O O   . PRO   A 1 196 ? 12.003  -3.460  23.414 1.00 48.72  ? 271 PRO   A O   1 
ATOM   1513 C CB  . PRO   A 1 196 ? 12.102  -3.163  26.594 1.00 50.14  ? 271 PRO   A CB  1 
ATOM   1514 C CG  . PRO   A 1 196 ? 11.865  -4.261  27.579 1.00 53.78  ? 271 PRO   A CG  1 
ATOM   1515 C CD  . PRO   A 1 196 ? 10.374  -4.424  27.655 1.00 51.51  ? 271 PRO   A CD  1 
ATOM   1516 N N   . ARG   A 1 197 ? 11.317  -5.414  24.299 1.00 46.55  ? 272 ARG   A N   1 
ATOM   1517 C CA  . ARG   A 1 197 ? 11.788  -6.175  23.145 1.00 36.49  ? 272 ARG   A CA  1 
ATOM   1518 C C   . ARG   A 1 197 ? 11.050  -5.771  21.877 1.00 41.73  ? 272 ARG   A C   1 
ATOM   1519 O O   . ARG   A 1 197 ? 11.636  -5.756  20.788 1.00 45.85  ? 272 ARG   A O   1 
ATOM   1520 C CB  . ARG   A 1 197 ? 11.627  -7.675  23.401 1.00 46.43  ? 272 ARG   A CB  1 
ATOM   1521 C CG  . ARG   A 1 197 ? 12.501  -8.208  24.524 1.00 58.33  ? 272 ARG   A CG  1 
ATOM   1522 C CD  . ARG   A 1 197 ? 12.164  -9.651  24.861 1.00 51.71  ? 272 ARG   A CD  1 
ATOM   1523 N NE  . ARG   A 1 197 ? 10.807  -9.775  25.378 1.00 60.04  ? 272 ARG   A NE  1 
ATOM   1524 C CZ  . ARG   A 1 197 ? 10.255  -10.914 25.771 1.00 68.14  ? 272 ARG   A CZ  1 
ATOM   1525 N NH1 . ARG   A 1 197 ? 10.919  -12.057 25.719 1.00 74.32  ? 272 ARG   A NH1 1 
ATOM   1526 N NH2 . ARG   A 1 197 ? 9.006   -10.905 26.228 1.00 69.88  ? 272 ARG   A NH2 1 
ATOM   1527 N N   . TYR   A 1 198 ? 9.765   -5.439  21.998 1.00 50.70  ? 273 TYR   A N   1 
ATOM   1528 C CA  . TYR   A 1 198 ? 8.926   -5.100  20.856 1.00 41.82  ? 273 TYR   A CA  1 
ATOM   1529 C C   . TYR   A 1 198 ? 8.598   -3.616  20.801 1.00 44.88  ? 273 TYR   A C   1 
ATOM   1530 O O   . TYR   A 1 198 ? 7.745   -3.202  20.008 1.00 48.84  ? 273 TYR   A O   1 
ATOM   1531 C CB  . TYR   A 1 198 ? 7.637   -5.923  20.892 1.00 41.69  ? 273 TYR   A CB  1 
ATOM   1532 C CG  . TYR   A 1 198 ? 7.861   -7.407  21.101 1.00 33.01  ? 273 TYR   A CG  1 
ATOM   1533 C CD1 . TYR   A 1 198 ? 7.973   -7.940  22.377 1.00 36.58  ? 273 TYR   A CD1 1 
ATOM   1534 C CD2 . TYR   A 1 198 ? 7.959   -8.273  20.020 1.00 38.13  ? 273 TYR   A CD2 1 
ATOM   1535 C CE1 . TYR   A 1 198 ? 8.181   -9.293  22.574 1.00 45.41  ? 273 TYR   A CE1 1 
ATOM   1536 C CE2 . TYR   A 1 198 ? 8.163   -9.629  20.208 1.00 45.26  ? 273 TYR   A CE2 1 
ATOM   1537 C CZ  . TYR   A 1 198 ? 8.276   -10.132 21.486 1.00 38.44  ? 273 TYR   A CZ  1 
ATOM   1538 O OH  . TYR   A 1 198 ? 8.482   -11.483 21.683 1.00 57.21  ? 273 TYR   A OH  1 
ATOM   1539 N N   . MET   A 1 199 ? 9.268   -2.807  21.611 1.00 48.63  ? 274 MET   A N   1 
ATOM   1540 C CA  . MET   A 1 199 ? 8.933   -1.398  21.748 1.00 33.69  ? 274 MET   A CA  1 
ATOM   1541 C C   . MET   A 1 199 ? 9.423   -0.603  20.544 1.00 50.42  ? 274 MET   A C   1 
ATOM   1542 O O   . MET   A 1 199 ? 10.590  -0.707  20.150 1.00 43.99  ? 274 MET   A O   1 
ATOM   1543 C CB  . MET   A 1 199 ? 9.551   -0.854  23.034 1.00 39.30  ? 274 MET   A CB  1 
ATOM   1544 C CG  . MET   A 1 199 ? 9.241   0.588   23.320 1.00 54.80  ? 274 MET   A CG  1 
ATOM   1545 S SD  . MET   A 1 199 ? 9.702   1.006   25.009 1.00 67.69  ? 274 MET   A SD  1 
ATOM   1546 C CE  . MET   A 1 199 ? 11.378  0.378   25.061 1.00 60.79  ? 274 MET   A CE  1 
ATOM   1547 N N   . ALA   A 1 200 ? 8.525   0.187   19.957 1.00 44.47  ? 275 ALA   A N   1 
ATOM   1548 C CA  . ALA   A 1 200 ? 8.919   1.094   18.893 1.00 36.00  ? 275 ALA   A CA  1 
ATOM   1549 C C   . ALA   A 1 200 ? 9.897   2.132   19.435 1.00 45.09  ? 275 ALA   A C   1 
ATOM   1550 O O   . ALA   A 1 200 ? 9.780   2.568   20.586 1.00 47.37  ? 275 ALA   A O   1 
ATOM   1551 C CB  . ALA   A 1 200 ? 7.697   1.785   18.293 1.00 45.04  ? 275 ALA   A CB  1 
ATOM   1552 N N   . PRO   A 1 201 ? 10.870  2.560   18.628 1.00 36.15  ? 276 PRO   A N   1 
ATOM   1553 C CA  . PRO   A 1 201 ? 11.927  3.429   19.163 1.00 38.14  ? 276 PRO   A CA  1 
ATOM   1554 C C   . PRO   A 1 201 ? 11.424  4.783   19.622 1.00 44.90  ? 276 PRO   A C   1 
ATOM   1555 O O   . PRO   A 1 201 ? 12.004  5.364   20.547 1.00 50.58  ? 276 PRO   A O   1 
ATOM   1556 C CB  . PRO   A 1 201 ? 12.904  3.555   17.984 1.00 36.06  ? 276 PRO   A CB  1 
ATOM   1557 C CG  . PRO   A 1 201 ? 12.067  3.324   16.785 1.00 37.97  ? 276 PRO   A CG  1 
ATOM   1558 C CD  . PRO   A 1 201 ? 11.056  2.294   17.191 1.00 41.04  ? 276 PRO   A CD  1 
ATOM   1559 N N   . GLU   A 1 202 ? 10.352  5.298   19.022 1.00 44.44  ? 277 GLU   A N   1 
ATOM   1560 C CA  . GLU   A 1 202 ? 9.866   6.618   19.400 1.00 45.02  ? 277 GLU   A CA  1 
ATOM   1561 C C   . GLU   A 1 202 ? 9.082   6.615   20.706 1.00 46.38  ? 277 GLU   A C   1 
ATOM   1562 O O   . GLU   A 1 202 ? 8.747   7.695   21.205 1.00 56.21  ? 277 GLU   A O   1 
ATOM   1563 C CB  . GLU   A 1 202 ? 9.001   7.208   18.282 1.00 44.02  ? 277 GLU   A CB  1 
ATOM   1564 C CG  . GLU   A 1 202 ? 7.634   6.562   18.125 1.00 56.62  ? 277 GLU   A CG  1 
ATOM   1565 C CD  . GLU   A 1 202 ? 7.680   5.265   17.351 1.00 59.81  ? 277 GLU   A CD  1 
ATOM   1566 O OE1 . GLU   A 1 202 ? 8.792   4.837   16.969 1.00 63.55  ? 277 GLU   A OE1 1 
ATOM   1567 O OE2 . GLU   A 1 202 ? 6.600   4.675   17.119 1.00 48.58  ? 277 GLU   A OE2 1 
ATOM   1568 N N   . LEU   A 1 203 ? 8.785   5.443   21.275 1.00 46.67  ? 278 LEU   A N   1 
ATOM   1569 C CA  . LEU   A 1 203 ? 8.112   5.416   22.570 1.00 38.27  ? 278 LEU   A CA  1 
ATOM   1570 C C   . LEU   A 1 203 ? 9.034   5.881   23.689 1.00 46.13  ? 278 LEU   A C   1 
ATOM   1571 O O   . LEU   A 1 203 ? 8.558   6.382   24.714 1.00 52.59  ? 278 LEU   A O   1 
ATOM   1572 C CB  . LEU   A 1 203 ? 7.581   4.015   22.869 1.00 41.20  ? 278 LEU   A CB  1 
ATOM   1573 C CG  . LEU   A 1 203 ? 6.459   3.507   21.960 1.00 52.28  ? 278 LEU   A CG  1 
ATOM   1574 C CD1 . LEU   A 1 203 ? 5.770   2.305   22.580 1.00 46.24  ? 278 LEU   A CD1 1 
ATOM   1575 C CD2 . LEU   A 1 203 ? 5.454   4.605   21.679 1.00 52.09  ? 278 LEU   A CD2 1 
ATOM   1576 N N   . LEU   A 1 204 ? 10.350  5.726   23.518 1.00 47.57  ? 279 LEU   A N   1 
ATOM   1577 C CA  . LEU   A 1 204 ? 11.278  6.254   24.510 1.00 42.25  ? 279 LEU   A CA  1 
ATOM   1578 C C   . LEU   A 1 204 ? 11.266  7.774   24.535 1.00 44.34  ? 279 LEU   A C   1 
ATOM   1579 O O   . LEU   A 1 204 ? 11.588  8.378   25.564 1.00 65.24  ? 279 LEU   A O   1 
ATOM   1580 C CB  . LEU   A 1 204 ? 12.691  5.748   24.237 1.00 54.08  ? 279 LEU   A CB  1 
ATOM   1581 C CG  . LEU   A 1 204 ? 12.903  4.251   24.435 1.00 61.78  ? 279 LEU   A CG  1 
ATOM   1582 C CD1 . LEU   A 1 204 ? 14.369  3.937   24.295 1.00 54.25  ? 279 LEU   A CD1 1 
ATOM   1583 C CD2 . LEU   A 1 204 ? 12.387  3.817   25.795 1.00 63.68  ? 279 LEU   A CD2 1 
ATOM   1584 N N   . GLN   A 1 205 ? 10.914  8.407   23.419 1.00 51.09  ? 280 GLN   A N   1 
ATOM   1585 C CA  . GLN   A 1 205 ? 10.782  9.854   23.349 1.00 51.94  ? 280 GLN   A CA  1 
ATOM   1586 C C   . GLN   A 1 205 ? 9.382   10.325  23.722 1.00 47.90  ? 280 GLN   A C   1 
ATOM   1587 O O   . GLN   A 1 205 ? 9.066   11.503  23.531 1.00 70.04  ? 280 GLN   A O   1 
ATOM   1588 C CB  . GLN   A 1 205 ? 11.140  10.351  21.945 1.00 57.23  ? 280 GLN   A CB  1 
ATOM   1589 C CG  . GLN   A 1 205 ? 12.217  9.533   21.241 1.00 63.27  ? 280 GLN   A CG  1 
ATOM   1590 C CD  . GLN   A 1 205 ? 13.536  9.514   21.992 1.00 90.40  ? 280 GLN   A CD  1 
ATOM   1591 O OE1 . GLN   A 1 205 ? 13.857  10.441  22.735 1.00 77.99  ? 280 GLN   A OE1 1 
ATOM   1592 N NE2 . GLN   A 1 205 ? 14.307  8.448   21.802 1.00 81.55  ? 280 GLN   A NE2 1 
ATOM   1593 N N   . GLY   A 1 206 ? 8.540   9.435   24.239 1.00 47.53  ? 281 GLY   A N   1 
ATOM   1594 C CA  . GLY   A 1 206 ? 7.203   9.821   24.647 1.00 47.73  ? 281 GLY   A CA  1 
ATOM   1595 C C   . GLY   A 1 206 ? 6.268   10.137  23.504 1.00 44.89  ? 281 GLY   A C   1 
ATOM   1596 O O   . GLY   A 1 206 ? 5.335   10.927  23.676 1.00 60.77  ? 281 GLY   A O   1 
ATOM   1597 N N   . SER   A 1 207 ? 6.491   9.540   22.338 1.00 48.94  ? 282 SER   A N   1 
ATOM   1598 C CA  . SER   A 1 207 ? 5.675   9.775   21.149 1.00 42.27  ? 282 SER   A CA  1 
ATOM   1599 C C   . SER   A 1 207 ? 4.794   8.545   20.944 1.00 52.84  ? 282 SER   A C   1 
ATOM   1600 O O   . SER   A 1 207 ? 5.190   7.577   20.293 1.00 50.36  ? 282 SER   A O   1 
ATOM   1601 C CB  . SER   A 1 207 ? 6.553   10.055  19.928 1.00 55.70  ? 282 SER   A CB  1 
ATOM   1602 O OG  . SER   A 1 207 ? 5.768   10.299  18.774 1.00 68.41  ? 282 SER   A OG  1 
ATOM   1603 N N   . TYR   A 1 208 ? 3.589   8.592   21.504 1.00 56.26  ? 283 TYR   A N   1 
ATOM   1604 C CA  . TYR   A 1 208 ? 2.660   7.472   21.443 1.00 43.72  ? 283 TYR   A CA  1 
ATOM   1605 C C   . TYR   A 1 208 ? 1.702   7.672   20.275 1.00 44.05  ? 283 TYR   A C   1 
ATOM   1606 O O   . TYR   A 1 208 ? 1.033   8.706   20.183 1.00 47.82  ? 283 TYR   A O   1 
ATOM   1607 C CB  . TYR   A 1 208 ? 1.892   7.335   22.757 1.00 52.69  ? 283 TYR   A CB  1 
ATOM   1608 C CG  . TYR   A 1 208 ? 2.787   7.120   23.960 1.00 61.07  ? 283 TYR   A CG  1 
ATOM   1609 C CD1 . TYR   A 1 208 ? 3.235   5.850   24.296 1.00 60.85  ? 283 TYR   A CD1 1 
ATOM   1610 C CD2 . TYR   A 1 208 ? 3.186   8.188   24.755 1.00 65.55  ? 283 TYR   A CD2 1 
ATOM   1611 C CE1 . TYR   A 1 208 ? 4.057   5.648   25.392 1.00 66.27  ? 283 TYR   A CE1 1 
ATOM   1612 C CE2 . TYR   A 1 208 ? 4.008   7.995   25.855 1.00 62.56  ? 283 TYR   A CE2 1 
ATOM   1613 C CZ  . TYR   A 1 208 ? 4.439   6.722   26.168 1.00 68.45  ? 283 TYR   A CZ  1 
ATOM   1614 O OH  . TYR   A 1 208 ? 5.257   6.522   27.259 1.00 95.69  ? 283 TYR   A OH  1 
ATOM   1615 N N   . GLY   A 1 209 ? 1.641   6.684   19.388 1.00 47.95  ? 284 GLY   A N   1 
ATOM   1616 C CA  . GLY   A 1 209 ? 0.753   6.752   18.244 1.00 43.59  ? 284 GLY   A CA  1 
ATOM   1617 C C   . GLY   A 1 209 ? 0.510   5.364   17.700 1.00 40.35  ? 284 GLY   A C   1 
ATOM   1618 O O   . GLY   A 1 209 ? 1.105   4.380   18.147 1.00 51.17  ? 284 GLY   A O   1 
ATOM   1619 N N   . THR   A 1 210 ? -0.384  5.295   16.714 1.00 49.18  ? 285 THR   A N   1 
ATOM   1620 C CA  . THR   A 1 210 ? -0.708  4.009   16.112 1.00 39.25  ? 285 THR   A CA  1 
ATOM   1621 C C   . THR   A 1 210 ? 0.479   3.402   15.382 1.00 38.23  ? 285 THR   A C   1 
ATOM   1622 O O   . THR   A 1 210 ? 0.518   2.182   15.191 1.00 53.77  ? 285 THR   A O   1 
ATOM   1623 C CB  . THR   A 1 210 ? -1.884  4.165   15.153 1.00 41.58  ? 285 THR   A CB  1 
ATOM   1624 O OG1 . THR   A 1 210 ? -1.526  5.086   14.115 1.00 41.98  ? 285 THR   A OG1 1 
ATOM   1625 C CG2 . THR   A 1 210 ? -3.096  4.700   15.892 1.00 36.05  ? 285 THR   A CG2 1 
ATOM   1626 N N   . ALA   A 1 211 ? 1.448   4.223   14.970 1.00 45.75  ? 286 ALA   A N   1 
ATOM   1627 C CA  . ALA   A 1 211 ? 2.634   3.697   14.303 1.00 33.59  ? 286 ALA   A CA  1 
ATOM   1628 C C   . ALA   A 1 211 ? 3.426   2.759   15.199 1.00 40.61  ? 286 ALA   A C   1 
ATOM   1629 O O   . ALA   A 1 211 ? 4.149   1.894   14.689 1.00 49.60  ? 286 ALA   A O   1 
ATOM   1630 C CB  . ALA   A 1 211 ? 3.536   4.844   13.840 1.00 38.26  ? 286 ALA   A CB  1 
ATOM   1631 N N   . ALA   A 1 212 ? 3.323   2.917   16.520 1.00 41.00  ? 287 ALA   A N   1 
ATOM   1632 C CA  . ALA   A 1 212 ? 4.063   2.039   17.422 1.00 43.01  ? 287 ALA   A CA  1 
ATOM   1633 C C   . ALA   A 1 212 ? 3.633   0.583   17.272 1.00 38.70  ? 287 ALA   A C   1 
ATOM   1634 O O   . ALA   A 1 212 ? 4.464   -0.326  17.399 1.00 48.09  ? 287 ALA   A O   1 
ATOM   1635 C CB  . ALA   A 1 212 ? 3.892   2.500   18.871 1.00 43.53  ? 287 ALA   A CB  1 
ATOM   1636 N N   . ASP   A 1 213 ? 2.347   0.339   17.008 1.00 43.60  ? 288 ASP   A N   1 
ATOM   1637 C CA  . ASP   A 1 213 ? 1.878   -1.033  16.828 1.00 34.31  ? 288 ASP   A CA  1 
ATOM   1638 C C   . ASP   A 1 213 ? 2.451   -1.657  15.560 1.00 31.00  ? 288 ASP   A C   1 
ATOM   1639 O O   . ASP   A 1 213 ? 2.732   -2.862  15.527 1.00 46.19  ? 288 ASP   A O   1 
ATOM   1640 C CB  . ASP   A 1 213 ? 0.351   -1.075  16.787 1.00 38.98  ? 288 ASP   A CB  1 
ATOM   1641 C CG  . ASP   A 1 213 ? -0.276  -0.785  18.126 1.00 43.78  ? 288 ASP   A CG  1 
ATOM   1642 O OD1 . ASP   A 1 213 ? 0.413   -0.960  19.158 1.00 38.18  ? 288 ASP   A OD1 1 
ATOM   1643 O OD2 . ASP   A 1 213 ? -1.460  -0.392  18.147 1.00 48.89  ? 288 ASP   A OD2 1 
ATOM   1644 N N   . VAL   A 1 214 ? 2.624   -0.860  14.504 1.00 38.06  ? 289 VAL   A N   1 
ATOM   1645 C CA  . VAL   A 1 214 ? 3.176   -1.395  13.264 1.00 31.03  ? 289 VAL   A CA  1 
ATOM   1646 C C   . VAL   A 1 214 ? 4.617   -1.840  13.475 1.00 36.03  ? 289 VAL   A C   1 
ATOM   1647 O O   . VAL   A 1 214 ? 5.060   -2.846  12.912 1.00 48.17  ? 289 VAL   A O   1 
ATOM   1648 C CB  . VAL   A 1 214 ? 3.056   -0.355  12.138 1.00 38.53  ? 289 VAL   A CB  1 
ATOM   1649 C CG1 . VAL   A 1 214 ? 3.604   -0.911  10.829 1.00 34.55  ? 289 VAL   A CG1 1 
ATOM   1650 C CG2 . VAL   A 1 214 ? 1.605   0.064   11.972 1.00 40.55  ? 289 VAL   A CG2 1 
ATOM   1651 N N   . PHE   A 1 215 ? 5.369   -1.110  14.299 1.00 36.88  ? 290 PHE   A N   1 
ATOM   1652 C CA  . PHE   A 1 215 ? 6.745   -1.506  14.569 1.00 34.04  ? 290 PHE   A CA  1 
ATOM   1653 C C   . PHE   A 1 215 ? 6.790   -2.783  15.396 1.00 34.21  ? 290 PHE   A C   1 
ATOM   1654 O O   . PHE   A 1 215 ? 7.594   -3.680  15.121 1.00 40.46  ? 290 PHE   A O   1 
ATOM   1655 C CB  . PHE   A 1 215 ? 7.487   -0.372  15.277 1.00 40.52  ? 290 PHE   A CB  1 
ATOM   1656 C CG  . PHE   A 1 215 ? 8.980   -0.542  15.297 1.00 35.13  ? 290 PHE   A CG  1 
ATOM   1657 C CD1 . PHE   A 1 215 ? 9.599   -1.267  16.303 1.00 41.98  ? 290 PHE   A CD1 1 
ATOM   1658 C CD2 . PHE   A 1 215 ? 9.766   0.032   14.312 1.00 34.55  ? 290 PHE   A CD2 1 
ATOM   1659 C CE1 . PHE   A 1 215 ? 10.973  -1.419  16.320 1.00 30.66  ? 290 PHE   A CE1 1 
ATOM   1660 C CE2 . PHE   A 1 215 ? 11.137  -0.117  14.325 1.00 25.83  ? 290 PHE   A CE2 1 
ATOM   1661 C CZ  . PHE   A 1 215 ? 11.741  -0.844  15.328 1.00 29.25  ? 290 PHE   A CZ  1 
ATOM   1662 N N   . SER   A 1 216 ? 5.922   -2.889  16.405 1.00 30.93  ? 291 SER   A N   1 
ATOM   1663 C CA  . SER   A 1 216 ? 5.899   -4.088  17.236 1.00 28.13  ? 291 SER   A CA  1 
ATOM   1664 C C   . SER   A 1 216 ? 5.543   -5.315  16.412 1.00 36.57  ? 291 SER   A C   1 
ATOM   1665 O O   . SER   A 1 216 ? 6.077   -6.406  16.645 1.00 41.19  ? 291 SER   A O   1 
ATOM   1666 C CB  . SER   A 1 216 ? 4.908   -3.918  18.386 1.00 31.90  ? 291 SER   A CB  1 
ATOM   1667 O OG  . SER   A 1 216 ? 5.244   -2.802  19.190 1.00 52.33  ? 291 SER   A OG  1 
ATOM   1668 N N   . LEU   A 1 217 ? 4.644   -5.156  15.442 1.00 40.14  ? 292 LEU   A N   1 
ATOM   1669 C CA  . LEU   A 1 217 ? 4.300   -6.280  14.583 1.00 39.54  ? 292 LEU   A CA  1 
ATOM   1670 C C   . LEU   A 1 217 ? 5.463   -6.660  13.674 1.00 33.66  ? 292 LEU   A C   1 
ATOM   1671 O O   . LEU   A 1 217 ? 5.639   -7.843  13.362 1.00 51.99  ? 292 LEU   A O   1 
ATOM   1672 C CB  . LEU   A 1 217 ? 3.058   -5.949  13.758 1.00 35.39  ? 292 LEU   A CB  1 
ATOM   1673 C CG  . LEU   A 1 217 ? 2.451   -7.107  12.974 1.00 32.34  ? 292 LEU   A CG  1 
ATOM   1674 C CD1 . LEU   A 1 217 ? 2.235   -8.287  13.895 1.00 33.72  ? 292 LEU   A CD1 1 
ATOM   1675 C CD2 . LEU   A 1 217 ? 1.141   -6.684  12.347 1.00 47.98  ? 292 LEU   A CD2 1 
ATOM   1676 N N   . GLY   A 1 218 ? 6.265   -5.680  13.247 1.00 44.87  ? 293 GLY   A N   1 
ATOM   1677 C CA  . GLY   A 1 218 ? 7.429   -5.992  12.432 1.00 34.60  ? 293 GLY   A CA  1 
ATOM   1678 C C   . GLY   A 1 218 ? 8.448   -6.837  13.171 1.00 31.96  ? 293 GLY   A C   1 
ATOM   1679 O O   . GLY   A 1 218 ? 8.987   -7.800  12.620 1.00 44.76  ? 293 GLY   A O   1 
ATOM   1680 N N   . LEU   A 1 219 ? 8.725   -6.493  14.431 1.00 33.62  ? 294 LEU   A N   1 
ATOM   1681 C CA  . LEU   A 1 219 ? 9.585   -7.345  15.248 1.00 39.53  ? 294 LEU   A CA  1 
ATOM   1682 C C   . LEU   A 1 219 ? 8.929   -8.691  15.543 1.00 40.15  ? 294 LEU   A C   1 
ATOM   1683 O O   . LEU   A 1 219 ? 9.621   -9.713  15.612 1.00 48.88  ? 294 LEU   A O   1 
ATOM   1684 C CB  . LEU   A 1 219 ? 9.946   -6.633  16.551 1.00 38.96  ? 294 LEU   A CB  1 
ATOM   1685 C CG  . LEU   A 1 219 ? 10.794  -5.371  16.403 1.00 39.62  ? 294 LEU   A CG  1 
ATOM   1686 C CD1 . LEU   A 1 219 ? 10.933  -4.679  17.742 1.00 48.73  ? 294 LEU   A CD1 1 
ATOM   1687 C CD2 . LEU   A 1 219 ? 12.158  -5.713  15.833 1.00 36.34  ? 294 LEU   A CD2 1 
ATOM   1688 N N   . THR   A 1 220 ? 7.608   -8.710  15.737 1.00 45.28  ? 295 THR   A N   1 
ATOM   1689 C CA  . THR   A 1 220 ? 6.897   -9.971  15.945 1.00 37.00  ? 295 THR   A CA  1 
ATOM   1690 C C   . THR   A 1 220 ? 7.076   -10.910 14.758 1.00 38.66  ? 295 THR   A C   1 
ATOM   1691 O O   . THR   A 1 220 ? 7.327   -12.110 14.927 1.00 49.08  ? 295 THR   A O   1 
ATOM   1692 C CB  . THR   A 1 220 ? 5.413   -9.694  16.185 1.00 40.22  ? 295 THR   A CB  1 
ATOM   1693 O OG1 . THR   A 1 220 ? 5.258   -8.962  17.405 1.00 49.79  ? 295 THR   A OG1 1 
ATOM   1694 C CG2 . THR   A 1 220 ? 4.628   -10.992 16.270 1.00 54.84  ? 295 THR   A CG2 1 
ATOM   1695 N N   . ILE   A 1 221 ? 6.937   -10.381 13.543 1.00 45.96  ? 296 ILE   A N   1 
ATOM   1696 C CA  . ILE   A 1 221 ? 7.167   -11.187 12.350 1.00 36.06  ? 296 ILE   A CA  1 
ATOM   1697 C C   . ILE   A 1 221 ? 8.631   -11.594 12.257 1.00 39.60  ? 296 ILE   A C   1 
ATOM   1698 O O   . ILE   A 1 221 ? 8.952   -12.744 11.937 1.00 60.02  ? 296 ILE   A O   1 
ATOM   1699 C CB  . ILE   A 1 221 ? 6.715   -10.419 11.097 1.00 40.06  ? 296 ILE   A CB  1 
ATOM   1700 C CG1 . ILE   A 1 221 ? 5.208   -10.173 11.147 1.00 40.26  ? 296 ILE   A CG1 1 
ATOM   1701 C CG2 . ILE   A 1 221 ? 7.100   -11.180 9.842  1.00 43.24  ? 296 ILE   A CG2 1 
ATOM   1702 C CD1 . ILE   A 1 221 ? 4.391   -11.444 11.252 1.00 56.37  ? 296 ILE   A CD1 1 
ATOM   1703 N N   . LEU   A 1 222 ? 9.542   -10.660 12.535 1.00 49.96  ? 297 LEU   A N   1 
ATOM   1704 C CA  . LEU   A 1 222 ? 10.965  -10.976 12.474 1.00 41.47  ? 297 LEU   A CA  1 
ATOM   1705 C C   . LEU   A 1 222 ? 11.339  -12.061 13.474 1.00 47.21  ? 297 LEU   A C   1 
ATOM   1706 O O   . LEU   A 1 222 ? 12.234  -12.870 13.206 1.00 54.41  ? 297 LEU   A O   1 
ATOM   1707 C CB  . LEU   A 1 222 ? 11.791  -9.713  12.723 1.00 44.27  ? 297 LEU   A CB  1 
ATOM   1708 C CG  . LEU   A 1 222 ? 13.307  -9.826  12.577 1.00 53.93  ? 297 LEU   A CG  1 
ATOM   1709 C CD1 . LEU   A 1 222 ? 13.676  -10.196 11.153 1.00 62.28  ? 297 LEU   A CD1 1 
ATOM   1710 C CD2 . LEU   A 1 222 ? 13.973  -8.523  12.983 1.00 57.12  ? 297 LEU   A CD2 1 
ATOM   1711 N N   . GLU   A 1 223 ? 10.660  -12.104 14.623 1.00 44.12  ? 298 GLU   A N   1 
ATOM   1712 C CA  . GLU   A 1 223 ? 10.959  -13.122 15.624 1.00 45.50  ? 298 GLU   A CA  1 
ATOM   1713 C C   . GLU   A 1 223 ? 10.468  -14.494 15.179 1.00 45.40  ? 298 GLU   A C   1 
ATOM   1714 O O   . GLU   A 1 223 ? 11.193  -15.490 15.288 1.00 56.07  ? 298 GLU   A O   1 
ATOM   1715 C CB  . GLU   A 1 223 ? 10.334  -12.736 16.968 1.00 40.71  ? 298 GLU   A CB  1 
ATOM   1716 C CG  . GLU   A 1 223 ? 10.292  -13.871 17.984 1.00 55.77  ? 298 GLU   A CG  1 
ATOM   1717 C CD  . GLU   A 1 223 ? 9.647   -13.462 19.297 1.00 65.94  ? 298 GLU   A CD  1 
ATOM   1718 O OE1 . GLU   A 1 223 ? 9.602   -12.249 19.586 1.00 54.53  ? 298 GLU   A OE1 1 
ATOM   1719 O OE2 . GLU   A 1 223 ? 9.183   -14.354 20.039 1.00 74.42  ? 298 GLU   A OE2 1 
ATOM   1720 N N   . VAL   A 1 224 ? 9.238   -14.568 14.670 1.00 42.76  ? 299 VAL   A N   1 
ATOM   1721 C CA  . VAL   A 1 224 ? 8.670   -15.867 14.329 1.00 32.48  ? 299 VAL   A CA  1 
ATOM   1722 C C   . VAL   A 1 224 ? 9.226   -16.392 13.011 1.00 37.57  ? 299 VAL   A C   1 
ATOM   1723 O O   . VAL   A 1 224 ? 9.331   -17.610 12.824 1.00 60.05  ? 299 VAL   A O   1 
ATOM   1724 C CB  . VAL   A 1 224 ? 7.133   -15.784 14.297 1.00 47.92  ? 299 VAL   A CB  1 
ATOM   1725 C CG1 . VAL   A 1 224 ? 6.603   -15.350 15.649 1.00 44.61  ? 299 VAL   A CG1 1 
ATOM   1726 C CG2 . VAL   A 1 224 ? 6.666   -14.826 13.211 1.00 53.83  ? 299 VAL   A CG2 1 
ATOM   1727 N N   . ALA   A 1 225 ? 9.593   -15.507 12.085 1.00 43.41  ? 300 ALA   A N   1 
ATOM   1728 C CA  . ALA   A 1 225 ? 10.082  -15.934 10.781 1.00 54.10  ? 300 ALA   A CA  1 
ATOM   1729 C C   . ALA   A 1 225 ? 11.564  -16.277 10.774 1.00 41.77  ? 300 ALA   A C   1 
ATOM   1730 O O   . ALA   A 1 225 ? 12.015  -16.982 9.865  1.00 61.25  ? 300 ALA   A O   1 
ATOM   1731 C CB  . ALA   A 1 225 ? 9.811   -14.853 9.726  1.00 48.11  ? 300 ALA   A CB  1 
ATOM   1732 N N   . CYS   A 1 226 ? 12.332  -15.795 11.751 1.00 50.96  ? 301 CYS   A N   1 
ATOM   1733 C CA  . CYS   A 1 226 ? 13.763  -16.057 11.807 1.00 66.50  ? 301 CYS   A CA  1 
ATOM   1734 C C   . CYS   A 1 226 ? 14.181  -16.896 13.004 1.00 62.78  ? 301 CYS   A C   1 
ATOM   1735 O O   . CYS   A 1 226 ? 15.353  -17.285 13.086 1.00 74.64  ? 301 CYS   A O   1 
ATOM   1736 C CB  . CYS   A 1 226 ? 14.547  -14.736 11.822 1.00 81.07  ? 301 CYS   A CB  1 
ATOM   1737 S SG  . CYS   A 1 226 ? 14.222  -13.672 10.399 1.00 74.53  ? 301 CYS   A SG  1 
ATOM   1738 N N   . ASN   A 1 227 ? 13.261  -17.181 13.928 1.00 64.90  ? 302 ASN   A N   1 
ATOM   1739 C CA  . ASN   A 1 227 ? 13.550  -17.974 15.122 1.00 66.18  ? 302 ASN   A CA  1 
ATOM   1740 C C   . ASN   A 1 227 ? 14.681  -17.351 15.936 1.00 71.03  ? 302 ASN   A C   1 
ATOM   1741 O O   . ASN   A 1 227 ? 15.577  -18.045 16.422 1.00 86.61  ? 302 ASN   A O   1 
ATOM   1742 C CB  . ASN   A 1 227 ? 13.874  -19.426 14.760 1.00 66.36  ? 302 ASN   A CB  1 
ATOM   1743 C CG  . ASN   A 1 227 ? 13.531  -20.392 15.873 1.00 65.76  ? 302 ASN   A CG  1 
ATOM   1744 O OD1 . ASN   A 1 227 ? 12.577  -20.178 16.621 1.00 73.96  ? 302 ASN   A OD1 1 
ATOM   1745 N ND2 . ASN   A 1 227 ? 14.308  -21.462 15.991 1.00 73.75  ? 302 ASN   A ND2 1 
ATOM   1746 N N   . MET   A 1 228 ? 14.648  -16.028 16.073 1.00 77.02  ? 303 MET   A N   1 
ATOM   1747 C CA  . MET   A 1 228 ? 15.638  -15.289 16.841 1.00 84.19  ? 303 MET   A CA  1 
ATOM   1748 C C   . MET   A 1 228 ? 14.996  -14.691 18.084 1.00 58.24  ? 303 MET   A C   1 
ATOM   1749 O O   . MET   A 1 228 ? 13.788  -14.441 18.124 1.00 66.48  ? 303 MET   A O   1 
ATOM   1750 C CB  . MET   A 1 228 ? 16.275  -14.171 16.007 1.00 81.85  ? 303 MET   A CB  1 
ATOM   1751 C CG  . MET   A 1 228 ? 15.358  -12.990 15.731 1.00 73.48  ? 303 MET   A CG  1 
ATOM   1752 S SD  . MET   A 1 228 ? 16.238  -11.592 15.003 1.00 110.79 ? 303 MET   A SD  1 
ATOM   1753 C CE  . MET   A 1 228 ? 17.434  -11.231 16.289 1.00 97.42  ? 303 MET   A CE  1 
ATOM   1754 N N   . GLU   A 1 229 ? 15.819  -14.458 19.101 1.00 66.07  ? 304 GLU   A N   1 
ATOM   1755 C CA  . GLU   A 1 229 ? 15.364  -13.870 20.351 1.00 66.39  ? 304 GLU   A CA  1 
ATOM   1756 C C   . GLU   A 1 229 ? 15.634  -12.373 20.327 1.00 56.29  ? 304 GLU   A C   1 
ATOM   1757 O O   . GLU   A 1 229 ? 16.762  -11.942 20.064 1.00 67.30  ? 304 GLU   A O   1 
ATOM   1758 C CB  . GLU   A 1 229 ? 16.054  -14.523 21.549 1.00 66.45  ? 304 GLU   A CB  1 
ATOM   1759 C CG  . GLU   A 1 229 ? 15.395  -14.204 22.879 1.00 95.50  ? 304 GLU   A CG  1 
ATOM   1760 C CD  . GLU   A 1 229 ? 15.697  -15.238 23.945 1.00 119.86 ? 304 GLU   A CD  1 
ATOM   1761 O OE1 . GLU   A 1 229 ? 16.877  -15.623 24.092 1.00 106.44 ? 304 GLU   A OE1 1 
ATOM   1762 O OE2 . GLU   A 1 229 ? 14.748  -15.674 24.631 1.00 129.12 ? 304 GLU   A OE2 1 
ATOM   1763 N N   . LEU   A 1 230 ? 14.601  -11.591 20.589 1.00 49.93  ? 305 LEU   A N   1 
ATOM   1764 C CA  . LEU   A 1 230 ? 14.750  -10.147 20.546 1.00 44.32  ? 305 LEU   A CA  1 
ATOM   1765 C C   . LEU   A 1 230 ? 15.391  -9.646  21.837 1.00 54.03  ? 305 LEU   A C   1 
ATOM   1766 O O   . LEU   A 1 230 ? 15.021  -10.091 22.928 1.00 56.05  ? 305 LEU   A O   1 
ATOM   1767 C CB  . LEU   A 1 230 ? 13.399  -9.475  20.344 1.00 47.55  ? 305 LEU   A CB  1 
ATOM   1768 C CG  . LEU   A 1 230 ? 12.664  -9.881  19.068 1.00 34.20  ? 305 LEU   A CG  1 
ATOM   1769 C CD1 . LEU   A 1 230 ? 11.356  -9.129  18.962 1.00 40.41  ? 305 LEU   A CD1 1 
ATOM   1770 C CD2 . LEU   A 1 230 ? 13.530  -9.628  17.844 1.00 51.10  ? 305 LEU   A CD2 1 
ATOM   1771 N N   . PRO   A 1 231 ? 16.344  -8.724  21.741 1.00 49.37  ? 306 PRO   A N   1 
ATOM   1772 C CA  . PRO   A 1 231 ? 17.048  -8.257  22.939 1.00 46.02  ? 306 PRO   A CA  1 
ATOM   1773 C C   . PRO   A 1 231 ? 16.194  -7.318  23.775 1.00 53.16  ? 306 PRO   A C   1 
ATOM   1774 O O   . PRO   A 1 231 ? 15.327  -6.603  23.270 1.00 45.61  ? 306 PRO   A O   1 
ATOM   1775 C CB  . PRO   A 1 231 ? 18.263  -7.523  22.361 1.00 41.68  ? 306 PRO   A CB  1 
ATOM   1776 C CG  . PRO   A 1 231 ? 17.777  -7.022  21.042 1.00 44.74  ? 306 PRO   A CG  1 
ATOM   1777 C CD  . PRO   A 1 231 ? 16.835  -8.070  20.515 1.00 43.77  ? 306 PRO   A CD  1 
ATOM   1778 N N   . HIS   A 1 232 ? 16.462  -7.330  25.083 1.00 64.84  ? 307 HIS   A N   1 
ATOM   1779 C CA  . HIS   A 1 232 ? 15.775  -6.427  25.999 1.00 49.93  ? 307 HIS   A CA  1 
ATOM   1780 C C   . HIS   A 1 232 ? 16.348  -5.017  25.950 1.00 51.86  ? 307 HIS   A C   1 
ATOM   1781 O O   . HIS   A 1 232 ? 15.604  -4.042  26.100 1.00 66.17  ? 307 HIS   A O   1 
ATOM   1782 C CB  . HIS   A 1 232 ? 15.852  -6.968  27.430 1.00 60.63  ? 307 HIS   A CB  1 
ATOM   1783 C CG  . HIS   A 1 232 ? 14.915  -8.105  27.701 1.00 78.18  ? 307 HIS   A CG  1 
ATOM   1784 N ND1 . HIS   A 1 232 ? 13.746  -7.949  28.415 1.00 80.91  ? 307 HIS   A ND1 1 
ATOM   1785 C CD2 . HIS   A 1 232 ? 14.976  -9.415  27.361 1.00 76.12  ? 307 HIS   A CD2 1 
ATOM   1786 C CE1 . HIS   A 1 232 ? 13.126  -9.112  28.500 1.00 74.70  ? 307 HIS   A CE1 1 
ATOM   1787 N NE2 . HIS   A 1 232 ? 13.851  -10.018 27.869 1.00 73.86  ? 307 HIS   A NE2 1 
ATOM   1788 N N   . GLY   A 1 233 ? 17.650  -4.889  25.751 1.00 55.79  ? 308 GLY   A N   1 
ATOM   1789 C CA  . GLY   A 1 233 ? 18.265  -3.584  25.689 1.00 46.28  ? 308 GLY   A CA  1 
ATOM   1790 C C   . GLY   A 1 233 ? 19.662  -3.674  25.123 1.00 56.45  ? 308 GLY   A C   1 
ATOM   1791 O O   . GLY   A 1 233 ? 20.012  -4.638  24.441 1.00 67.02  ? 308 GLY   A O   1 
ATOM   1792 N N   . GLY   A 1 234 ? 20.459  -2.652  25.414 1.00 58.94  ? 309 GLY   A N   1 
ATOM   1793 C CA  . GLY   A 1 234 ? 21.839  -2.689  24.983 1.00 68.90  ? 309 GLY   A CA  1 
ATOM   1794 C C   . GLY   A 1 234 ? 22.003  -2.501  23.482 1.00 53.42  ? 309 GLY   A C   1 
ATOM   1795 O O   . GLY   A 1 234 ? 21.126  -1.991  22.778 1.00 59.65  ? 309 GLY   A O   1 
ATOM   1796 N N   . GLU   A 1 235 ? 23.165  -2.945  22.995 1.00 56.93  ? 310 GLU   A N   1 
ATOM   1797 C CA  . GLU   A 1 235 ? 23.540  -2.691  21.608 1.00 65.58  ? 310 GLU   A CA  1 
ATOM   1798 C C   . GLU   A 1 235 ? 22.631  -3.437  20.640 1.00 63.61  ? 310 GLU   A C   1 
ATOM   1799 O O   . GLU   A 1 235 ? 22.234  -2.888  19.605 1.00 60.26  ? 310 GLU   A O   1 
ATOM   1800 C CB  . GLU   A 1 235 ? 25.002  -3.076  21.388 1.00 78.43  ? 310 GLU   A CB  1 
ATOM   1801 C CG  . GLU   A 1 235 ? 25.568  -2.656  20.039 1.00 94.73  ? 310 GLU   A CG  1 
ATOM   1802 C CD  . GLU   A 1 235 ? 27.079  -2.796  19.971 1.00 125.21 ? 310 GLU   A CD  1 
ATOM   1803 O OE1 . GLU   A 1 235 ? 27.692  -3.166  20.995 1.00 119.05 ? 310 GLU   A OE1 1 
ATOM   1804 O OE2 . GLU   A 1 235 ? 27.657  -2.534  18.895 1.00 143.43 ? 310 GLU   A OE2 1 
ATOM   1805 N N   . GLY   A 1 236 ? 22.285  -4.687  20.956 1.00 49.38  ? 311 GLY   A N   1 
ATOM   1806 C CA  . GLY   A 1 236 ? 21.396  -5.432  20.084 1.00 45.97  ? 311 GLY   A CA  1 
ATOM   1807 C C   . GLY   A 1 236 ? 20.038  -4.779  19.925 1.00 50.76  ? 311 GLY   A C   1 
ATOM   1808 O O   . GLY   A 1 236 ? 19.414  -4.885  18.866 1.00 51.80  ? 311 GLY   A O   1 
ATOM   1809 N N   . TRP   A 1 237 ? 19.563  -4.095  20.968 1.00 49.60  ? 312 TRP   A N   1 
ATOM   1810 C CA  . TRP   A 1 237 ? 18.281  -3.402  20.887 1.00 47.01  ? 312 TRP   A CA  1 
ATOM   1811 C C   . TRP   A 1 237 ? 18.356  -2.219  19.930 1.00 39.61  ? 312 TRP   A C   1 
ATOM   1812 O O   . TRP   A 1 237 ? 17.419  -1.973  19.162 1.00 53.94  ? 312 TRP   A O   1 
ATOM   1813 C CB  . TRP   A 1 237 ? 17.859  -2.943  22.283 1.00 47.60  ? 312 TRP   A CB  1 
ATOM   1814 C CG  . TRP   A 1 237 ? 16.491  -2.335  22.364 1.00 37.86  ? 312 TRP   A CG  1 
ATOM   1815 C CD1 . TRP   A 1 237 ? 15.325  -2.979  22.660 1.00 38.51  ? 312 TRP   A CD1 1 
ATOM   1816 C CD2 . TRP   A 1 237 ? 16.149  -0.956  22.166 1.00 37.90  ? 312 TRP   A CD2 1 
ATOM   1817 N NE1 . TRP   A 1 237 ? 14.277  -2.090  22.648 1.00 39.01  ? 312 TRP   A NE1 1 
ATOM   1818 C CE2 . TRP   A 1 237 ? 14.755  -0.843  22.344 1.00 42.26  ? 312 TRP   A CE2 1 
ATOM   1819 C CE3 . TRP   A 1 237 ? 16.884  0.190   21.846 1.00 35.92  ? 312 TRP   A CE3 1 
ATOM   1820 C CZ2 . TRP   A 1 237 ? 14.083  0.373   22.221 1.00 31.11  ? 312 TRP   A CZ2 1 
ATOM   1821 C CZ3 . TRP   A 1 237 ? 16.213  1.396   21.721 1.00 38.17  ? 312 TRP   A CZ3 1 
ATOM   1822 C CH2 . TRP   A 1 237 ? 14.828  1.477   21.906 1.00 38.88  ? 312 TRP   A CH2 1 
ATOM   1823 N N   . GLN   A 1 238 ? 19.465  -1.477  19.961 1.00 56.24  ? 313 GLN   A N   1 
ATOM   1824 C CA  . GLN   A 1 238 ? 19.609  -0.321  19.083 1.00 45.81  ? 313 GLN   A CA  1 
ATOM   1825 C C   . GLN   A 1 238 ? 19.730  -0.737  17.623 1.00 47.01  ? 313 GLN   A C   1 
ATOM   1826 O O   . GLN   A 1 238 ? 19.245  -0.024  16.738 1.00 67.16  ? 313 GLN   A O   1 
ATOM   1827 C CB  . GLN   A 1 238 ? 20.829  0.503   19.495 1.00 44.12  ? 313 GLN   A CB  1 
ATOM   1828 C CG  . GLN   A 1 238 ? 20.955  0.754   20.991 1.00 56.70  ? 313 GLN   A CG  1 
ATOM   1829 C CD  . GLN   A 1 238 ? 20.000  1.819   21.498 1.00 57.94  ? 313 GLN   A CD  1 
ATOM   1830 O OE1 . GLN   A 1 238 ? 19.295  2.463   20.720 1.00 60.76  ? 313 GLN   A OE1 1 
ATOM   1831 N NE2 . GLN   A 1 238 ? 19.979  2.013   22.812 1.00 64.42  ? 313 GLN   A NE2 1 
ATOM   1832 N N   . GLN   A 1 239 ? 20.363  -1.883  17.355 1.00 57.62  ? 314 GLN   A N   1 
ATOM   1833 C CA  . GLN   A 1 239 ? 20.621  -2.287  15.976 1.00 56.30  ? 314 GLN   A CA  1 
ATOM   1834 C C   . GLN   A 1 239 ? 19.341  -2.651  15.235 1.00 53.06  ? 314 GLN   A C   1 
ATOM   1835 O O   . GLN   A 1 239 ? 19.255  -2.450  14.018 1.00 66.56  ? 314 GLN   A O   1 
ATOM   1836 C CB  . GLN   A 1 239 ? 21.603  -3.457  15.948 1.00 73.46  ? 314 GLN   A CB  1 
ATOM   1837 C CG  . GLN   A 1 239 ? 22.994  -3.111  16.460 1.00 68.10  ? 314 GLN   A CG  1 
ATOM   1838 C CD  . GLN   A 1 239 ? 23.950  -4.282  16.372 1.00 75.10  ? 314 GLN   A CD  1 
ATOM   1839 O OE1 . GLN   A 1 239 ? 23.588  -5.355  15.892 1.00 83.00  ? 314 GLN   A OE1 1 
ATOM   1840 N NE2 . GLN   A 1 239 ? 25.181  -4.082  16.834 1.00 71.91  ? 314 GLN   A NE2 1 
ATOM   1841 N N   . LEU   A 1 240 ? 18.343  -3.185  15.936 1.00 49.78  ? 315 LEU   A N   1 
ATOM   1842 C CA  . LEU   A 1 240 ? 17.057  -3.473  15.312 1.00 47.67  ? 315 LEU   A CA  1 
ATOM   1843 C C   . LEU   A 1 240 ? 16.216  -2.226  15.087 1.00 43.22  ? 315 LEU   A C   1 
ATOM   1844 O O   . LEU   A 1 240 ? 15.082  -2.343  14.611 1.00 52.55  ? 315 LEU   A O   1 
ATOM   1845 C CB  . LEU   A 1 240 ? 16.261  -4.466  16.163 1.00 43.87  ? 315 LEU   A CB  1 
ATOM   1846 C CG  . LEU   A 1 240 ? 16.756  -5.910  16.188 1.00 45.57  ? 315 LEU   A CG  1 
ATOM   1847 C CD1 . LEU   A 1 240 ? 15.937  -6.728  17.169 1.00 49.50  ? 315 LEU   A CD1 1 
ATOM   1848 C CD2 . LEU   A 1 240 ? 16.685  -6.515  14.798 1.00 52.74  ? 315 LEU   A CD2 1 
ATOM   1849 N N   . ARG   A 1 241 ? 16.736  -1.041  15.412 1.00 47.70  ? 316 ARG   A N   1 
ATOM   1850 C CA  . ARG   A 1 241 ? 15.963  0.192   15.330 1.00 42.15  ? 316 ARG   A CA  1 
ATOM   1851 C C   . ARG   A 1 241 ? 16.735  1.291   14.611 1.00 41.64  ? 316 ARG   A C   1 
ATOM   1852 O O   . ARG   A 1 241 ? 16.555  2.475   14.904 1.00 50.02  ? 316 ARG   A O   1 
ATOM   1853 C CB  . ARG   A 1 241 ? 15.541  0.648   16.724 1.00 42.44  ? 316 ARG   A CB  1 
ATOM   1854 C CG  . ARG   A 1 241 ? 14.527  -0.289  17.336 1.00 44.82  ? 316 ARG   A CG  1 
ATOM   1855 C CD  . ARG   A 1 241 ? 14.468  -0.194  18.837 1.00 35.91  ? 316 ARG   A CD  1 
ATOM   1856 N NE  . ARG   A 1 241 ? 13.395  -1.031  19.363 1.00 43.34  ? 316 ARG   A NE  1 
ATOM   1857 C CZ  . ARG   A 1 241 ? 13.513  -2.327  19.620 1.00 39.77  ? 316 ARG   A CZ  1 
ATOM   1858 N NH1 . ARG   A 1 241 ? 14.652  -2.972  19.420 1.00 38.45  ? 316 ARG   A NH1 1 
ATOM   1859 N NH2 . ARG   A 1 241 ? 12.464  -2.991  20.096 1.00 37.52  ? 316 ARG   A NH2 1 
ATOM   1860 N N   . GLN   A 1 242 ? 17.593  0.913   13.665 1.00 58.11  ? 317 GLN   A N   1 
ATOM   1861 C CA  . GLN   A 1 242 ? 18.352  1.866   12.868 1.00 54.50  ? 317 GLN   A CA  1 
ATOM   1862 C C   . GLN   A 1 242 ? 17.856  1.961   11.435 1.00 53.09  ? 317 GLN   A C   1 
ATOM   1863 O O   . GLN   A 1 242 ? 18.399  2.751   10.656 1.00 58.02  ? 317 GLN   A O   1 
ATOM   1864 C CB  . GLN   A 1 242 ? 19.840  1.499   12.868 1.00 59.26  ? 317 GLN   A CB  1 
ATOM   1865 C CG  . GLN   A 1 242 ? 20.489  1.542   14.236 1.00 61.50  ? 317 GLN   A CG  1 
ATOM   1866 C CD  . GLN   A 1 242 ? 20.360  2.900   14.898 1.00 77.92  ? 317 GLN   A CD  1 
ATOM   1867 O OE1 . GLN   A 1 242 ? 20.788  3.916   14.348 1.00 86.98  ? 317 GLN   A OE1 1 
ATOM   1868 N NE2 . GLN   A 1 242 ? 19.763  2.925   16.084 1.00 79.25  ? 317 GLN   A NE2 1 
ATOM   1869 N N   . GLY   A 1 243 ? 16.845  1.176   11.063 1.00 56.32  ? 318 GLY   A N   1 
ATOM   1870 C CA  . GLY   A 1 243 ? 16.282  1.188   9.732  1.00 50.15  ? 318 GLY   A CA  1 
ATOM   1871 C C   . GLY   A 1 243 ? 16.584  -0.063  8.934  1.00 60.66  ? 318 GLY   A C   1 
ATOM   1872 O O   . GLY   A 1 243 ? 15.750  -0.484  8.122  1.00 67.93  ? 318 GLY   A O   1 
ATOM   1873 N N   . TYR   A 1 244 ? 17.753  -0.663  9.141  1.00 69.50  ? 319 TYR   A N   1 
ATOM   1874 C CA  . TYR   A 1 244 ? 18.107  -1.885  8.439  1.00 69.59  ? 319 TYR   A CA  1 
ATOM   1875 C C   . TYR   A 1 244 ? 17.710  -3.110  9.263  1.00 72.68  ? 319 TYR   A C   1 
ATOM   1876 O O   . TYR   A 1 244 ? 17.255  -3.009  10.402 1.00 84.33  ? 319 TYR   A O   1 
ATOM   1877 C CB  . TYR   A 1 244 ? 19.604  -1.912  8.111  1.00 59.32  ? 319 TYR   A CB  1 
ATOM   1878 C CG  . TYR   A 1 244 ? 20.528  -1.779  9.304  1.00 73.37  ? 319 TYR   A CG  1 
ATOM   1879 C CD1 . TYR   A 1 244 ? 20.873  -2.888  10.070 1.00 90.00  ? 319 TYR   A CD1 1 
ATOM   1880 C CD2 . TYR   A 1 244 ? 21.075  -0.550  9.649  1.00 81.13  ? 319 TYR   A CD2 1 
ATOM   1881 C CE1 . TYR   A 1 244 ? 21.725  -2.772  11.155 1.00 86.83  ? 319 TYR   A CE1 1 
ATOM   1882 C CE2 . TYR   A 1 244 ? 21.932  -0.425  10.735 1.00 87.09  ? 319 TYR   A CE2 1 
ATOM   1883 C CZ  . TYR   A 1 244 ? 22.252  -1.540  11.483 1.00 90.39  ? 319 TYR   A CZ  1 
ATOM   1884 O OH  . TYR   A 1 244 ? 23.100  -1.429  12.563 1.00 90.85  ? 319 TYR   A OH  1 
ATOM   1885 N N   . LEU   A 1 245 ? 17.895  -4.277  8.666  1.00 82.27  ? 320 LEU   A N   1 
ATOM   1886 C CA  . LEU   A 1 245 ? 17.543  -5.555  9.259  1.00 78.72  ? 320 LEU   A CA  1 
ATOM   1887 C C   . LEU   A 1 245 ? 18.792  -6.300  9.713  1.00 94.68  ? 320 LEU   A C   1 
ATOM   1888 O O   . LEU   A 1 245 ? 19.903  -5.994  9.268  1.00 84.98  ? 320 LEU   A O   1 
ATOM   1889 C CB  . LEU   A 1 245 ? 16.766  -6.408  8.245  1.00 78.63  ? 320 LEU   A CB  1 
ATOM   1890 C CG  . LEU   A 1 245 ? 15.279  -6.083  8.102  1.00 71.61  ? 320 LEU   A CG  1 
ATOM   1891 C CD1 . LEU   A 1 245 ? 14.698  -6.761  6.874  1.00 75.33  ? 320 LEU   A CD1 1 
ATOM   1892 C CD2 . LEU   A 1 245 ? 14.529  -6.513  9.349  1.00 71.83  ? 320 LEU   A CD2 1 
ATOM   1893 N N   . PRO   A 1 246 ? 18.653  -7.272  10.615 1.00 115.29 ? 321 PRO   A N   1 
ATOM   1894 C CA  . PRO   A 1 246 ? 19.811  -8.081  11.019 1.00 114.16 ? 321 PRO   A CA  1 
ATOM   1895 C C   . PRO   A 1 246 ? 20.258  -8.988  9.887  1.00 111.58 ? 321 PRO   A C   1 
ATOM   1896 O O   . PRO   A 1 246 ? 19.581  -9.978  9.571  1.00 110.39 ? 321 PRO   A O   1 
ATOM   1897 C CB  . PRO   A 1 246 ? 19.280  -8.894  12.209 1.00 118.18 ? 321 PRO   A CB  1 
ATOM   1898 C CG  . PRO   A 1 246 ? 17.805  -8.957  11.992 1.00 115.41 ? 321 PRO   A CG  1 
ATOM   1899 C CD  . PRO   A 1 246 ? 17.440  -7.635  11.372 1.00 110.08 ? 321 PRO   A CD  1 
ATOM   1900 N N   . PRO   A 1 247 ? 21.402  -8.692  9.263  1.00 97.70  ? 322 PRO   A N   1 
ATOM   1901 C CA  . PRO   A 1 247 ? 21.823  -9.487  8.098  1.00 88.92  ? 322 PRO   A CA  1 
ATOM   1902 C C   . PRO   A 1 247 ? 22.006  -10.956 8.420  1.00 99.77  ? 322 PRO   A C   1 
ATOM   1903 O O   . PRO   A 1 247 ? 21.769  -11.807 7.552  1.00 103.42 ? 322 PRO   A O   1 
ATOM   1904 C CB  . PRO   A 1 247 ? 23.146  -8.828  7.687  1.00 75.81  ? 322 PRO   A CB  1 
ATOM   1905 C CG  . PRO   A 1 247 ? 23.659  -8.218  8.944  1.00 90.38  ? 322 PRO   A CG  1 
ATOM   1906 C CD  . PRO   A 1 247 ? 22.446  -7.746  9.694  1.00 91.83  ? 322 PRO   A CD  1 
ATOM   1907 N N   . GLU   A 1 248 ? 22.415  -11.277 9.648  1.00 98.75  ? 323 GLU   A N   1 
ATOM   1908 C CA  . GLU   A 1 248 ? 22.579  -12.669 10.050 1.00 103.18 ? 323 GLU   A CA  1 
ATOM   1909 C C   . GLU   A 1 248 ? 21.273  -13.440 9.893  1.00 102.93 ? 323 GLU   A C   1 
ATOM   1910 O O   . GLU   A 1 248 ? 21.202  -14.430 9.156  1.00 101.98 ? 323 GLU   A O   1 
ATOM   1911 C CB  . GLU   A 1 248 ? 23.076  -12.743 11.498 1.00 116.59 ? 323 GLU   A CB  1 
ATOM   1912 C CG  . GLU   A 1 248 ? 24.376  -11.993 11.774 1.00 129.86 ? 323 GLU   A CG  1 
ATOM   1913 C CD  . GLU   A 1 248 ? 24.176  -10.499 11.981 1.00 132.65 ? 323 GLU   A CD  1 
ATOM   1914 O OE1 . GLU   A 1 248 ? 23.017  -10.033 11.937 1.00 107.48 ? 323 GLU   A OE1 1 
ATOM   1915 O OE2 . GLU   A 1 248 ? 25.183  -9.790  12.189 1.00 141.86 ? 323 GLU   A OE2 1 
ATOM   1916 N N   . PHE   A 1 249 ? 20.222  -12.988 10.570 1.00 94.82  ? 324 PHE   A N   1 
ATOM   1917 C CA  . PHE   A 1 249 ? 18.959  -13.715 10.591 1.00 91.90  ? 324 PHE   A CA  1 
ATOM   1918 C C   . PHE   A 1 249 ? 18.044  -13.395 9.416  1.00 90.75  ? 324 PHE   A C   1 
ATOM   1919 O O   . PHE   A 1 249 ? 17.167  -14.206 9.101  1.00 90.34  ? 324 PHE   A O   1 
ATOM   1920 C CB  . PHE   A 1 249 ? 18.220  -13.442 11.906 1.00 96.18  ? 324 PHE   A CB  1 
ATOM   1921 C CG  . PHE   A 1 249 ? 18.852  -14.100 13.102 1.00 114.34 ? 324 PHE   A CG  1 
ATOM   1922 C CD1 . PHE   A 1 249 ? 19.868  -13.468 13.805 1.00 120.59 ? 324 PHE   A CD1 1 
ATOM   1923 C CD2 . PHE   A 1 249 ? 18.433  -15.353 13.521 1.00 109.13 ? 324 PHE   A CD2 1 
ATOM   1924 C CE1 . PHE   A 1 249 ? 20.451  -14.076 14.906 1.00 126.24 ? 324 PHE   A CE1 1 
ATOM   1925 C CE2 . PHE   A 1 249 ? 19.010  -15.966 14.621 1.00 115.15 ? 324 PHE   A CE2 1 
ATOM   1926 C CZ  . PHE   A 1 249 ? 20.021  -15.326 15.314 1.00 121.92 ? 324 PHE   A CZ  1 
ATOM   1927 N N   . THR   A 1 250 ? 18.222  -12.249 8.755  1.00 88.56  ? 325 THR   A N   1 
ATOM   1928 C CA  . THR   A 1 250 ? 17.338  -11.911 7.646  1.00 82.79  ? 325 THR   A CA  1 
ATOM   1929 C C   . THR   A 1 250 ? 17.577  -12.774 6.415  1.00 86.31  ? 325 THR   A C   1 
ATOM   1930 O O   . THR   A 1 250 ? 16.772  -12.720 5.478  1.00 92.05  ? 325 THR   A O   1 
ATOM   1931 C CB  . THR   A 1 250 ? 17.489  -10.439 7.261  1.00 83.97  ? 325 THR   A CB  1 
ATOM   1932 O OG1 . THR   A 1 250 ? 16.355  -10.034 6.484  1.00 101.59 ? 325 THR   A OG1 1 
ATOM   1933 C CG2 . THR   A 1 250 ? 18.755  -10.230 6.441  1.00 91.50  ? 325 THR   A CG2 1 
ATOM   1934 N N   . ALA   A 1 251 ? 18.657  -13.550 6.382  1.00 80.57  ? 326 ALA   A N   1 
ATOM   1935 C CA  . ALA   A 1 251 ? 18.852  -14.488 5.290  1.00 71.70  ? 326 ALA   A CA  1 
ATOM   1936 C C   . ALA   A 1 251 ? 17.755  -15.548 5.312  1.00 94.20  ? 326 ALA   A C   1 
ATOM   1937 O O   . ALA   A 1 251 ? 17.125  -15.810 6.341  1.00 101.34 ? 326 ALA   A O   1 
ATOM   1938 C CB  . ALA   A 1 251 ? 20.228  -15.144 5.384  1.00 73.08  ? 326 ALA   A CB  1 
ATOM   1939 N N   . GLY   A 1 252 ? 17.523  -16.160 4.152  1.00 74.04  ? 327 GLY   A N   1 
ATOM   1940 C CA  . GLY   A 1 252 ? 16.444  -17.110 4.001  1.00 78.04  ? 327 GLY   A CA  1 
ATOM   1941 C C   . GLY   A 1 252 ? 15.066  -16.500 3.899  1.00 85.50  ? 327 GLY   A C   1 
ATOM   1942 O O   . GLY   A 1 252 ? 14.113  -17.218 3.571  1.00 93.98  ? 327 GLY   A O   1 
ATOM   1943 N N   . LEU   A 1 253 ? 14.920  -15.206 4.174  1.00 68.22  ? 328 LEU   A N   1 
ATOM   1944 C CA  . LEU   A 1 253 ? 13.645  -14.526 4.011  1.00 72.38  ? 328 LEU   A CA  1 
ATOM   1945 C C   . LEU   A 1 253 ? 13.497  -14.044 2.576  1.00 72.18  ? 328 LEU   A C   1 
ATOM   1946 O O   . LEU   A 1 253 ? 14.463  -13.584 1.959  1.00 72.12  ? 328 LEU   A O   1 
ATOM   1947 C CB  . LEU   A 1 253 ? 13.525  -13.340 4.969  1.00 72.17  ? 328 LEU   A CB  1 
ATOM   1948 C CG  . LEU   A 1 253 ? 13.478  -13.638 6.468  1.00 72.12  ? 328 LEU   A CG  1 
ATOM   1949 C CD1 . LEU   A 1 253 ? 12.855  -12.467 7.213  1.00 65.11  ? 328 LEU   A CD1 1 
ATOM   1950 C CD2 . LEU   A 1 253 ? 12.719  -14.926 6.747  1.00 80.73  ? 328 LEU   A CD2 1 
ATOM   1951 N N   . SER   A 1 254 ? 12.282  -14.157 2.048  1.00 54.96  ? 329 SER   A N   1 
ATOM   1952 C CA  . SER   A 1 254 ? 12.021  -13.698 0.694  1.00 57.65  ? 329 SER   A CA  1 
ATOM   1953 C C   . SER   A 1 254 ? 12.199  -12.187 0.604  1.00 70.47  ? 329 SER   A C   1 
ATOM   1954 O O   . SER   A 1 254 ? 11.953  -11.452 1.564  1.00 76.97  ? 329 SER   A O   1 
ATOM   1955 C CB  . SER   A 1 254 ? 10.608  -14.084 0.266  1.00 65.51  ? 329 SER   A CB  1 
ATOM   1956 O OG  . SER   A 1 254 ? 9.644   -13.396 1.043  1.00 66.57  ? 329 SER   A OG  1 
ATOM   1957 N N   . SER   A 1 255 ? 12.638  -11.725 -0.570 1.00 83.81  ? 330 SER   A N   1 
ATOM   1958 C CA  . SER   A 1 255 ? 12.780  -10.289 -0.786 1.00 65.76  ? 330 SER   A CA  1 
ATOM   1959 C C   . SER   A 1 255 ? 11.454  -9.567  -0.599 1.00 70.43  ? 330 SER   A C   1 
ATOM   1960 O O   . SER   A 1 255 ? 11.434  -8.402  -0.185 1.00 63.87  ? 330 SER   A O   1 
ATOM   1961 C CB  . SER   A 1 255 ? 13.342  -10.019 -2.183 1.00 65.31  ? 330 SER   A CB  1 
ATOM   1962 O OG  . SER   A 1 255 ? 12.471  -10.510 -3.185 1.00 78.42  ? 330 SER   A OG  1 
ATOM   1963 N N   . GLU   A 1 256 ? 10.339  -10.243 -0.891 1.00 71.71  ? 331 GLU   A N   1 
ATOM   1964 C CA  . GLU   A 1 256 ? 9.027   -9.655  -0.639 1.00 58.36  ? 331 GLU   A CA  1 
ATOM   1965 C C   . GLU   A 1 256 ? 8.797   -9.446  0.851  1.00 66.33  ? 331 GLU   A C   1 
ATOM   1966 O O   . GLU   A 1 256 ? 8.196   -8.446  1.258  1.00 74.09  ? 331 GLU   A O   1 
ATOM   1967 C CB  . GLU   A 1 256 ? 7.928   -10.539 -1.232 1.00 73.71  ? 331 GLU   A CB  1 
ATOM   1968 C CG  . GLU   A 1 256 ? 7.926   -10.636 -2.756 1.00 85.49  ? 331 GLU   A CG  1 
ATOM   1969 C CD  . GLU   A 1 256 ? 8.959   -11.609 -3.295 1.00 97.54  ? 331 GLU   A CD  1 
ATOM   1970 O OE1 . GLU   A 1 256 ? 9.657   -12.254 -2.484 1.00 110.11 ? 331 GLU   A OE1 1 
ATOM   1971 O OE2 . GLU   A 1 256 ? 9.071   -11.728 -4.534 1.00 97.80  ? 331 GLU   A OE2 1 
ATOM   1972 N N   . LEU   A 1 257 ? 9.271   -10.375 1.680  1.00 61.23  ? 332 LEU   A N   1 
ATOM   1973 C CA  . LEU   A 1 257 ? 9.088   -10.230 3.120  1.00 52.14  ? 332 LEU   A CA  1 
ATOM   1974 C C   . LEU   A 1 257 ? 10.029  -9.185  3.703  1.00 48.99  ? 332 LEU   A C   1 
ATOM   1975 O O   . LEU   A 1 257 ? 9.633   -8.418  4.588  1.00 58.77  ? 332 LEU   A O   1 
ATOM   1976 C CB  . LEU   A 1 257 ? 9.289   -11.576 3.817  1.00 54.37  ? 332 LEU   A CB  1 
ATOM   1977 C CG  . LEU   A 1 257 ? 9.035   -11.573 5.326  1.00 50.82  ? 332 LEU   A CG  1 
ATOM   1978 C CD1 . LEU   A 1 257 ? 7.608   -11.135 5.640  1.00 46.25  ? 332 LEU   A CD1 1 
ATOM   1979 C CD2 . LEU   A 1 257 ? 9.324   -12.941 5.923  1.00 52.84  ? 332 LEU   A CD2 1 
ATOM   1980 N N   . ARG   A 1 258 ? 11.274  -9.135  3.219  1.00 54.28  ? 333 ARG   A N   1 
ATOM   1981 C CA  . ARG   A 1 258 ? 12.229  -8.165  3.747  1.00 52.09  ? 333 ARG   A CA  1 
ATOM   1982 C C   . ARG   A 1 258 ? 11.777  -6.736  3.475  1.00 62.50  ? 333 ARG   A C   1 
ATOM   1983 O O   . ARG   A 1 258 ? 11.870  -5.870  4.354  1.00 60.88  ? 333 ARG   A O   1 
ATOM   1984 C CB  . ARG   A 1 258 ? 13.614  -8.408  3.150  1.00 55.90  ? 333 ARG   A CB  1 
ATOM   1985 C CG  . ARG   A 1 258 ? 14.258  -9.714  3.587  1.00 75.92  ? 333 ARG   A CG  1 
ATOM   1986 C CD  . ARG   A 1 258 ? 15.688  -9.840  3.074  1.00 72.13  ? 333 ARG   A CD  1 
ATOM   1987 N NE  . ARG   A 1 258 ? 15.754  -9.950  1.620  1.00 101.04 ? 333 ARG   A NE  1 
ATOM   1988 C CZ  . ARG   A 1 258 ? 16.031  -8.944  0.802  1.00 104.20 ? 333 ARG   A CZ  1 
ATOM   1989 N NH1 . ARG   A 1 258 ? 16.271  -7.725  1.259  1.00 105.80 ? 333 ARG   A NH1 1 
ATOM   1990 N NH2 . ARG   A 1 258 ? 16.072  -9.166  -0.509 1.00 86.51  ? 333 ARG   A NH2 1 
ATOM   1991 N N   . SER   A 1 259 ? 11.281  -6.469  2.265  1.00 53.30  ? 334 SER   A N   1 
ATOM   1992 C CA  . SER   A 1 259 ? 10.832  -5.119  1.941  1.00 52.98  ? 334 SER   A CA  1 
ATOM   1993 C C   . SER   A 1 259 ? 9.666   -4.698  2.826  1.00 50.08  ? 334 SER   A C   1 
ATOM   1994 O O   . SER   A 1 259 ? 9.588   -3.542  3.256  1.00 63.36  ? 334 SER   A O   1 
ATOM   1995 C CB  . SER   A 1 259 ? 10.448  -5.035  0.465  1.00 60.99  ? 334 SER   A CB  1 
ATOM   1996 O OG  . SER   A 1 259 ? 9.433   -5.972  0.156  1.00 71.63  ? 334 SER   A OG  1 
ATOM   1997 N N   . VAL   A 1 260 ? 8.752   -5.624  3.114  1.00 50.83  ? 335 VAL   A N   1 
ATOM   1998 C CA  . VAL   A 1 260 ? 7.656   -5.310  4.025  1.00 53.50  ? 335 VAL   A CA  1 
ATOM   1999 C C   . VAL   A 1 260 ? 8.186   -5.092  5.438  1.00 49.00  ? 335 VAL   A C   1 
ATOM   2000 O O   . VAL   A 1 260 ? 7.707   -4.215  6.166  1.00 48.97  ? 335 VAL   A O   1 
ATOM   2001 C CB  . VAL   A 1 260 ? 6.589   -6.420  3.979  1.00 52.05  ? 335 VAL   A CB  1 
ATOM   2002 C CG1 . VAL   A 1 260 ? 5.500   -6.156  5.004  1.00 49.45  ? 335 VAL   A CG1 1 
ATOM   2003 C CG2 . VAL   A 1 260 ? 5.992   -6.521  2.584  1.00 59.31  ? 335 VAL   A CG2 1 
ATOM   2004 N N   . LEU   A 1 261 ? 9.189   -5.872  5.847  1.00 54.20  ? 336 LEU   A N   1 
ATOM   2005 C CA  . LEU   A 1 261 ? 9.774   -5.681  7.172  1.00 54.97  ? 336 LEU   A CA  1 
ATOM   2006 C C   . LEU   A 1 261 ? 10.456  -4.325  7.290  1.00 49.77  ? 336 LEU   A C   1 
ATOM   2007 O O   . LEU   A 1 261 ? 10.318  -3.645  8.313  1.00 55.93  ? 336 LEU   A O   1 
ATOM   2008 C CB  . LEU   A 1 261 ? 10.767  -6.799  7.482  1.00 51.42  ? 336 LEU   A CB  1 
ATOM   2009 C CG  . LEU   A 1 261 ? 10.173  -8.123  7.953  1.00 46.48  ? 336 LEU   A CG  1 
ATOM   2010 C CD1 . LEU   A 1 261 ? 11.285  -9.079  8.354  1.00 54.32  ? 336 LEU   A CD1 1 
ATOM   2011 C CD2 . LEU   A 1 261 ? 9.213   -7.886  9.107  1.00 54.84  ? 336 LEU   A CD2 1 
ATOM   2012 N N   . VAL   A 1 262 ? 11.207  -3.919  6.263  1.00 52.33  ? 337 VAL   A N   1 
ATOM   2013 C CA  . VAL   A 1 262 ? 11.883  -2.626  6.316  1.00 55.03  ? 337 VAL   A CA  1 
ATOM   2014 C C   . VAL   A 1 262 ? 10.865  -1.499  6.434  1.00 51.65  ? 337 VAL   A C   1 
ATOM   2015 O O   . VAL   A 1 262 ? 11.094  -0.503  7.133  1.00 49.27  ? 337 VAL   A O   1 
ATOM   2016 C CB  . VAL   A 1 262 ? 12.797  -2.455  5.089  1.00 56.66  ? 337 VAL   A CB  1 
ATOM   2017 C CG1 . VAL   A 1 262 ? 13.382  -1.055  5.042  1.00 54.08  ? 337 VAL   A CG1 1 
ATOM   2018 C CG2 . VAL   A 1 262 ? 13.909  -3.491  5.122  1.00 53.56  ? 337 VAL   A CG2 1 
ATOM   2019 N N   . MET   A 1 263 ? 9.711   -1.649  5.779  1.00 56.02  ? 338 MET   A N   1 
ATOM   2020 C CA  . MET   A 1 263 ? 8.669   -0.631  5.876  1.00 42.29  ? 338 MET   A CA  1 
ATOM   2021 C C   . MET   A 1 263 ? 8.104   -0.543  7.284  1.00 40.89  ? 338 MET   A C   1 
ATOM   2022 O O   . MET   A 1 263 ? 7.908   0.557   7.813  1.00 54.31  ? 338 MET   A O   1 
ATOM   2023 C CB  . MET   A 1 263 ? 7.555   -0.924  4.875  1.00 42.42  ? 338 MET   A CB  1 
ATOM   2024 C CG  . MET   A 1 263 ? 7.955   -0.705  3.436  1.00 42.41  ? 338 MET   A CG  1 
ATOM   2025 S SD  . MET   A 1 263 ? 6.642   -1.180  2.304  1.00 63.63  ? 338 MET   A SD  1 
ATOM   2026 C CE  . MET   A 1 263 ? 5.277   -0.231  2.968  1.00 79.57  ? 338 MET   A CE  1 
ATOM   2027 N N   . MET   A 1 264 ? 7.827   -1.689  7.907  1.00 47.36  ? 339 MET   A N   1 
ATOM   2028 C CA  . MET   A 1 264 ? 7.267   -1.680  9.252  1.00 38.34  ? 339 MET   A CA  1 
ATOM   2029 C C   . MET   A 1 264 ? 8.289   -1.220  10.282 1.00 39.41  ? 339 MET   A C   1 
ATOM   2030 O O   . MET   A 1 264 ? 7.916   -0.620  11.297 1.00 44.26  ? 339 MET   A O   1 
ATOM   2031 C CB  . MET   A 1 264 ? 6.747   -3.071  9.615  1.00 33.04  ? 339 MET   A CB  1 
ATOM   2032 C CG  . MET   A 1 264 ? 5.787   -3.649  8.596  1.00 40.75  ? 339 MET   A CG  1 
ATOM   2033 S SD  . MET   A 1 264 ? 5.252   -5.311  9.034  1.00 45.48  ? 339 MET   A SD  1 
ATOM   2034 C CE  . MET   A 1 264 ? 4.308   -4.972  10.514 1.00 48.59  ? 339 MET   A CE  1 
ATOM   2035 N N   . LEU   A 1 265 ? 9.573   -1.481  10.038 1.00 48.46  ? 340 LEU   A N   1 
ATOM   2036 C CA  . LEU   A 1 265 ? 10.633  -1.154  10.981 1.00 47.45  ? 340 LEU   A CA  1 
ATOM   2037 C C   . LEU   A 1 265 ? 11.278  0.200   10.701 1.00 49.68  ? 340 LEU   A C   1 
ATOM   2038 O O   . LEU   A 1 265 ? 12.397  0.449   11.166 1.00 56.26  ? 340 LEU   A O   1 
ATOM   2039 C CB  . LEU   A 1 265 ? 11.695  -2.255  10.976 1.00 43.99  ? 340 LEU   A CB  1 
ATOM   2040 C CG  . LEU   A 1 265 ? 11.220  -3.629  11.458 1.00 43.02  ? 340 LEU   A CG  1 
ATOM   2041 C CD1 . LEU   A 1 265 ? 12.378  -4.607  11.538 1.00 48.88  ? 340 LEU   A CD1 1 
ATOM   2042 C CD2 . LEU   A 1 265 ? 10.522  -3.521  12.804 1.00 48.41  ? 340 LEU   A CD2 1 
ATOM   2043 N N   . GLU   A 1 266 ? 10.608  1.071   9.956  1.00 60.45  ? 341 GLU   A N   1 
ATOM   2044 C CA  . GLU   A 1 266 ? 11.122  2.411   9.718  1.00 47.83  ? 341 GLU   A CA  1 
ATOM   2045 C C   . GLU   A 1 266 ? 11.236  3.155   11.044 1.00 41.89  ? 341 GLU   A C   1 
ATOM   2046 O O   . GLU   A 1 266 ? 10.234  3.272   11.766 1.00 50.44  ? 341 GLU   A O   1 
ATOM   2047 C CB  . GLU   A 1 266 ? 10.212  3.171   8.755  1.00 45.48  ? 341 GLU   A CB  1 
ATOM   2048 C CG  . GLU   A 1 266 ? 10.478  4.666   8.694  1.00 50.60  ? 341 GLU   A CG  1 
ATOM   2049 C CD  . GLU   A 1 266 ? 11.894  4.994   8.268  1.00 63.02  ? 341 GLU   A CD  1 
ATOM   2050 O OE1 . GLU   A 1 266 ? 12.445  4.267   7.413  1.00 73.25  ? 341 GLU   A OE1 1 
ATOM   2051 O OE2 . GLU   A 1 266 ? 12.461  5.975   8.796  1.00 76.02  ? 341 GLU   A OE2 1 
ATOM   2052 N N   . PRO   A 1 267 ? 12.422  3.648   11.411 1.00 42.20  ? 342 PRO   A N   1 
ATOM   2053 C CA  . PRO   A 1 267 ? 12.563  4.303   12.722 1.00 43.86  ? 342 PRO   A CA  1 
ATOM   2054 C C   . PRO   A 1 267 ? 11.675  5.523   12.897 1.00 58.58  ? 342 PRO   A C   1 
ATOM   2055 O O   . PRO   A 1 267 ? 11.071  5.693   13.964 1.00 52.41  ? 342 PRO   A O   1 
ATOM   2056 C CB  . PRO   A 1 267 ? 14.053  4.674   12.766 1.00 55.54  ? 342 PRO   A CB  1 
ATOM   2057 C CG  . PRO   A 1 267 ? 14.708  3.736   11.806 1.00 52.71  ? 342 PRO   A CG  1 
ATOM   2058 C CD  . PRO   A 1 267 ? 13.711  3.520   10.712 1.00 56.33  ? 342 PRO   A CD  1 
ATOM   2059 N N   . ASP   A 1 268 ? 11.576  6.378   11.886 1.00 55.41  ? 343 ASP   A N   1 
ATOM   2060 C CA  . ASP   A 1 268 ? 10.788  7.599   12.011 1.00 46.32  ? 343 ASP   A CA  1 
ATOM   2061 C C   . ASP   A 1 268 ? 9.304   7.267   11.908 1.00 45.57  ? 343 ASP   A C   1 
ATOM   2062 O O   . ASP   A 1 268 ? 8.857   6.805   10.852 1.00 47.60  ? 343 ASP   A O   1 
ATOM   2063 C CB  . ASP   A 1 268 ? 11.185  8.599   10.934 1.00 57.42  ? 343 ASP   A CB  1 
ATOM   2064 C CG  . ASP   A 1 268 ? 10.770  10.016  11.270 1.00 67.33  ? 343 ASP   A CG  1 
ATOM   2065 O OD1 . ASP   A 1 268 ? 9.671   10.202  11.837 1.00 75.51  ? 343 ASP   A OD1 1 
ATOM   2066 O OD2 . ASP   A 1 268 ? 11.548  10.946  10.968 1.00 84.32  ? 343 ASP   A OD2 1 
ATOM   2067 N N   . PRO   A 1 269 ? 8.512   7.488   12.960 1.00 50.87  ? 344 PRO   A N   1 
ATOM   2068 C CA  . PRO   A 1 269 ? 7.085   7.135   12.883 1.00 48.75  ? 344 PRO   A CA  1 
ATOM   2069 C C   . PRO   A 1 269 ? 6.324   7.928   11.841 1.00 47.34  ? 344 PRO   A C   1 
ATOM   2070 O O   . PRO   A 1 269 ? 5.313   7.439   11.320 1.00 59.07  ? 344 PRO   A O   1 
ATOM   2071 C CB  . PRO   A 1 269 ? 6.572   7.430   14.299 1.00 41.65  ? 344 PRO   A CB  1 
ATOM   2072 C CG  . PRO   A 1 269 ? 7.536   8.428   14.851 1.00 46.02  ? 344 PRO   A CG  1 
ATOM   2073 C CD  . PRO   A 1 269 ? 8.870   8.081   14.260 1.00 40.12  ? 344 PRO   A CD  1 
ATOM   2074 N N   . LYS   A 1 270 ? 6.772   9.145   11.526 1.00 60.74  ? 345 LYS   A N   1 
ATOM   2075 C CA  . LYS   A 1 270 ? 6.114   9.923   10.484 1.00 48.99  ? 345 LYS   A CA  1 
ATOM   2076 C C   . LYS   A 1 270 ? 6.223   9.240   9.128  1.00 50.32  ? 345 LYS   A C   1 
ATOM   2077 O O   . LYS   A 1 270 ? 5.305   9.340   8.305  1.00 55.74  ? 345 LYS   A O   1 
ATOM   2078 C CB  . LYS   A 1 270 ? 6.721   11.324  10.419 1.00 56.59  ? 345 LYS   A CB  1 
ATOM   2079 C CG  . LYS   A 1 270 ? 6.802   12.027  11.762 1.00 73.00  ? 345 LYS   A CG  1 
ATOM   2080 C CD  . LYS   A 1 270 ? 7.483   13.378  11.630 1.00 75.37  ? 345 LYS   A CD  1 
ATOM   2081 C CE  . LYS   A 1 270 ? 7.594   14.077  12.974 1.00 82.57  ? 345 LYS   A CE  1 
ATOM   2082 N NZ  . LYS   A 1 270 ? 8.223   15.421  12.843 1.00 106.54 ? 345 LYS   A NZ  1 
ATOM   2083 N N   . LEU   A 1 271 ? 7.329   8.540   8.882  1.00 61.25  ? 346 LEU   A N   1 
ATOM   2084 C CA  . LEU   A 1 271 ? 7.580   7.872   7.614  1.00 47.55  ? 346 LEU   A CA  1 
ATOM   2085 C C   . LEU   A 1 271 ? 7.180   6.404   7.631  1.00 55.21  ? 346 LEU   A C   1 
ATOM   2086 O O   . LEU   A 1 271 ? 7.287   5.734   6.599  1.00 54.54  ? 346 LEU   A O   1 
ATOM   2087 C CB  . LEU   A 1 271 ? 9.062   7.992   7.244  1.00 49.52  ? 346 LEU   A CB  1 
ATOM   2088 C CG  . LEU   A 1 271 ? 9.679   9.384   7.375  1.00 51.48  ? 346 LEU   A CG  1 
ATOM   2089 C CD1 . LEU   A 1 271 ? 11.170  9.341   7.086  1.00 52.27  ? 346 LEU   A CD1 1 
ATOM   2090 C CD2 . LEU   A 1 271 ? 8.981   10.354  6.443  1.00 49.05  ? 346 LEU   A CD2 1 
ATOM   2091 N N   . ARG   A 1 272 ? 6.726   5.889   8.770  1.00 53.30  ? 347 ARG   A N   1 
ATOM   2092 C CA  . ARG   A 1 272 ? 6.381   4.480   8.881  1.00 49.35  ? 347 ARG   A CA  1 
ATOM   2093 C C   . ARG   A 1 272 ? 5.030   4.206   8.235  1.00 44.43  ? 347 ARG   A C   1 
ATOM   2094 O O   . ARG   A 1 272 ? 4.082   4.984   8.383  1.00 59.47  ? 347 ARG   A O   1 
ATOM   2095 C CB  . ARG   A 1 272 ? 6.359   4.056   10.348 1.00 38.47  ? 347 ARG   A CB  1 
ATOM   2096 C CG  . ARG   A 1 272 ? 6.177   2.565   10.573 1.00 49.96  ? 347 ARG   A CG  1 
ATOM   2097 C CD  . ARG   A 1 272 ? 6.297   2.254   12.045 1.00 50.50  ? 347 ARG   A CD  1 
ATOM   2098 N NE  . ARG   A 1 272 ? 7.545   2.777   12.583 1.00 37.27  ? 347 ARG   A NE  1 
ATOM   2099 C CZ  . ARG   A 1 272 ? 7.685   3.253   13.811 1.00 33.78  ? 347 ARG   A CZ  1 
ATOM   2100 N NH1 . ARG   A 1 272 ? 6.664   3.311   14.649 1.00 37.31  ? 347 ARG   A NH1 1 
ATOM   2101 N NH2 . ARG   A 1 272 ? 8.877   3.689   14.205 1.00 47.05  ? 347 ARG   A NH2 1 
ATOM   2102 N N   . ALA   A 1 273 ? 4.947   3.092   7.512  1.00 50.35  ? 348 ALA   A N   1 
ATOM   2103 C CA  . ALA   A 1 273 ? 3.695   2.710   6.876  1.00 49.38  ? 348 ALA   A CA  1 
ATOM   2104 C C   . ALA   A 1 273 ? 2.629   2.398   7.922  1.00 51.32  ? 348 ALA   A C   1 
ATOM   2105 O O   . ALA   A 1 273 ? 2.924   1.977   9.043  1.00 55.49  ? 348 ALA   A O   1 
ATOM   2106 C CB  . ALA   A 1 273 ? 3.904   1.498   5.968  1.00 48.27  ? 348 ALA   A CB  1 
ATOM   2107 N N   . THR   A 1 274 ? 1.374   2.613   7.545  1.00 54.99  ? 349 THR   A N   1 
ATOM   2108 C CA  . THR   A 1 274 ? 0.251   2.308   8.416  1.00 42.61  ? 349 THR   A CA  1 
ATOM   2109 C C   . THR   A 1 274 ? -0.287  0.914   8.106  1.00 55.29  ? 349 THR   A C   1 
ATOM   2110 O O   . THR   A 1 274 ? 0.088   0.277   7.118  1.00 53.53  ? 349 THR   A O   1 
ATOM   2111 C CB  . THR   A 1 274 ? -0.852  3.352   8.254  1.00 46.36  ? 349 THR   A CB  1 
ATOM   2112 O OG1 . THR   A 1 274 ? -1.304  3.355   6.898  1.00 44.15  ? 349 THR   A OG1 1 
ATOM   2113 C CG2 . THR   A 1 274 ? -0.335  4.736   8.604  1.00 44.60  ? 349 THR   A CG2 1 
ATOM   2114 N N   . ALA   A 1 275 ? -1.186  0.440   8.971  1.00 45.80  ? 350 ALA   A N   1 
ATOM   2115 C CA  . ALA   A 1 275 ? -1.786  -0.873  8.761  1.00 34.00  ? 350 ALA   A CA  1 
ATOM   2116 C C   . ALA   A 1 275 ? -2.550  -0.929  7.446  1.00 41.09  ? 350 ALA   A C   1 
ATOM   2117 O O   . ALA   A 1 275 ? -2.489  -1.933  6.726  1.00 52.69  ? 350 ALA   A O   1 
ATOM   2118 C CB  . ALA   A 1 275 ? -2.705  -1.218  9.930  1.00 38.02  ? 350 ALA   A CB  1 
ATOM   2119 N N   . GLU   A 1 276 ? -3.266  0.144   7.106  1.00 44.87  ? 351 GLU   A N   1 
ATOM   2120 C CA  . GLU   A 1 276 ? -4.009  0.157   5.850  1.00 38.43  ? 351 GLU   A CA  1 
ATOM   2121 C C   . GLU   A 1 276 ? -3.073  0.207   4.650  1.00 47.41  ? 351 GLU   A C   1 
ATOM   2122 O O   . GLU   A 1 276 ? -3.338  -0.428  3.622  1.00 51.04  ? 351 GLU   A O   1 
ATOM   2123 C CB  . GLU   A 1 276 ? -4.972  1.342   5.821  1.00 46.36  ? 351 GLU   A CB  1 
ATOM   2124 C CG  . GLU   A 1 276 ? -6.402  0.990   6.184  1.00 75.87  ? 351 GLU   A CG  1 
ATOM   2125 C CD  . GLU   A 1 276 ? -7.303  2.206   6.282  1.00 100.72 ? 351 GLU   A CD  1 
ATOM   2126 O OE1 . GLU   A 1 276 ? -7.107  3.171   5.510  1.00 85.39  ? 351 GLU   A OE1 1 
ATOM   2127 O OE2 . GLU   A 1 276 ? -8.205  2.197   7.144  1.00 97.06  ? 351 GLU   A OE2 1 
ATOM   2128 N N   . ALA   A 1 277 ? -1.974  0.959   4.756  1.00 49.70  ? 352 ALA   A N   1 
ATOM   2129 C CA  . ALA   A 1 277 ? -1.020  1.023   3.653  1.00 50.27  ? 352 ALA   A CA  1 
ATOM   2130 C C   . ALA   A 1 277 ? -0.427  -0.346  3.362  1.00 38.34  ? 352 ALA   A C   1 
ATOM   2131 O O   . ALA   A 1 277 ? -0.325  -0.750  2.199  1.00 52.82  ? 352 ALA   A O   1 
ATOM   2132 C CB  . ALA   A 1 277 ? 0.084   2.029   3.967  1.00 44.32  ? 352 ALA   A CB  1 
ATOM   2133 N N   . LEU   A 1 278 ? -0.054  -1.085  4.408  1.00 48.35  ? 353 LEU   A N   1 
ATOM   2134 C CA  . LEU   A 1 278 ? 0.493   -2.425  4.218  1.00 49.21  ? 353 LEU   A CA  1 
ATOM   2135 C C   . LEU   A 1 278 ? -0.537  -3.362  3.599  1.00 41.42  ? 353 LEU   A C   1 
ATOM   2136 O O   . LEU   A 1 278 ? -0.246  -4.066  2.626  1.00 58.95  ? 353 LEU   A O   1 
ATOM   2137 C CB  . LEU   A 1 278 ? 0.988   -2.973  5.555  1.00 45.23  ? 353 LEU   A CB  1 
ATOM   2138 C CG  . LEU   A 1 278 ? 2.177   -2.235  6.168  1.00 40.62  ? 353 LEU   A CG  1 
ATOM   2139 C CD1 . LEU   A 1 278 ? 2.376   -2.638  7.621  1.00 43.32  ? 353 LEU   A CD1 1 
ATOM   2140 C CD2 . LEU   A 1 278 ? 3.438   -2.499  5.353  1.00 49.72  ? 353 LEU   A CD2 1 
ATOM   2141 N N   . LEU   A 1 279 ? -1.760  -3.373  4.142  1.00 41.14  ? 354 LEU   A N   1 
ATOM   2142 C CA  . LEU   A 1 279 ? -2.799  -4.266  3.634  1.00 34.17  ? 354 LEU   A CA  1 
ATOM   2143 C C   . LEU   A 1 279 ? -3.129  -4.009  2.171  1.00 40.28  ? 354 LEU   A C   1 
ATOM   2144 O O   . LEU   A 1 279 ? -3.749  -4.864  1.528  1.00 47.49  ? 354 LEU   A O   1 
ATOM   2145 C CB  . LEU   A 1 279 ? -4.064  -4.133  4.483  1.00 48.11  ? 354 LEU   A CB  1 
ATOM   2146 C CG  . LEU   A 1 279 ? -4.029  -4.792  5.863  1.00 44.34  ? 354 LEU   A CG  1 
ATOM   2147 C CD1 . LEU   A 1 279 ? -5.153  -4.266  6.742  1.00 38.31  ? 354 LEU   A CD1 1 
ATOM   2148 C CD2 . LEU   A 1 279 ? -4.124  -6.302  5.719  1.00 36.57  ? 354 LEU   A CD2 1 
ATOM   2149 N N   . ALA   A 1 280 ? -2.740  -2.858  1.631  1.00 54.63  ? 355 ALA   A N   1 
ATOM   2150 C CA  . ALA   A 1 280 ? -2.952  -2.566  0.221  1.00 46.67  ? 355 ALA   A CA  1 
ATOM   2151 C C   . ALA   A 1 280 ? -1.766  -2.960  -0.649 1.00 48.45  ? 355 ALA   A C   1 
ATOM   2152 O O   . ALA   A 1 280 ? -1.803  -2.725  -1.862 1.00 46.15  ? 355 ALA   A O   1 
ATOM   2153 C CB  . ALA   A 1 280 ? -3.261  -1.078  0.027  1.00 49.89  ? 355 ALA   A CB  1 
ATOM   2154 N N   . LEU   A 1 281 ? -0.721  -3.544  -0.064 1.00 57.82  ? 356 LEU   A N   1 
ATOM   2155 C CA  . LEU   A 1 281 ? 0.414   -3.997  -0.851 1.00 47.56  ? 356 LEU   A CA  1 
ATOM   2156 C C   . LEU   A 1 281 ? 0.042   -5.255  -1.633 1.00 56.60  ? 356 LEU   A C   1 
ATOM   2157 O O   . LEU   A 1 281 ? -0.827  -6.022  -1.211 1.00 61.95  ? 356 LEU   A O   1 
ATOM   2158 C CB  . LEU   A 1 281 ? 1.617   -4.280  0.047  1.00 57.63  ? 356 LEU   A CB  1 
ATOM   2159 C CG  . LEU   A 1 281 ? 2.287   -3.056  0.674  1.00 58.69  ? 356 LEU   A CG  1 
ATOM   2160 C CD1 . LEU   A 1 281 ? 3.485   -3.457  1.521  1.00 63.40  ? 356 LEU   A CD1 1 
ATOM   2161 C CD2 . LEU   A 1 281 ? 2.700   -2.070  -0.405 1.00 51.19  ? 356 LEU   A CD2 1 
ATOM   2162 N N   . PRO   A 1 282 ? 0.680   -5.483  -2.784 1.00 59.06  ? 357 PRO   A N   1 
ATOM   2163 C CA  . PRO   A 1 282 ? 0.351   -6.682  -3.572 1.00 53.96  ? 357 PRO   A CA  1 
ATOM   2164 C C   . PRO   A 1 282 ? 0.626   -7.987  -2.842 1.00 51.36  ? 357 PRO   A C   1 
ATOM   2165 O O   . PRO   A 1 282 ? -0.094  -8.970  -3.056 1.00 66.07  ? 357 PRO   A O   1 
ATOM   2166 C CB  . PRO   A 1 282 ? 1.236   -6.533  -4.818 1.00 64.43  ? 357 PRO   A CB  1 
ATOM   2167 C CG  . PRO   A 1 282 ? 1.573   -5.070  -4.884 1.00 53.50  ? 357 PRO   A CG  1 
ATOM   2168 C CD  . PRO   A 1 282 ? 1.660   -4.619  -3.464 1.00 58.52  ? 357 PRO   A CD  1 
ATOM   2169 N N   . VAL   A 1 283 ? 1.643   -8.027  -1.978 1.00 57.84  ? 358 VAL   A N   1 
ATOM   2170 C CA  . VAL   A 1 283 ? 1.985   -9.262  -1.282 1.00 66.79  ? 358 VAL   A CA  1 
ATOM   2171 C C   . VAL   A 1 283 ? 0.933   -9.656  -0.252 1.00 70.39  ? 358 VAL   A C   1 
ATOM   2172 O O   . VAL   A 1 283 ? 0.873   -10.824 0.150  1.00 74.65  ? 358 VAL   A O   1 
ATOM   2173 C CB  . VAL   A 1 283 ? 3.365   -9.124  -0.614 1.00 61.47  ? 358 VAL   A CB  1 
ATOM   2174 C CG1 . VAL   A 1 283 ? 4.423   -8.803  -1.655 1.00 76.36  ? 358 VAL   A CG1 1 
ATOM   2175 C CG2 . VAL   A 1 283 ? 3.327   -8.045  0.454  1.00 53.88  ? 358 VAL   A CG2 1 
ATOM   2176 N N   . LEU   A 1 284 ? 0.098   -8.716  0.189  1.00 68.55  ? 359 LEU   A N   1 
ATOM   2177 C CA  . LEU   A 1 284 ? -0.922  -8.963  1.204  1.00 58.41  ? 359 LEU   A CA  1 
ATOM   2178 C C   . LEU   A 1 284 ? -2.324  -8.963  0.602  1.00 85.06  ? 359 LEU   A C   1 
ATOM   2179 O O   . LEU   A 1 284 ? -3.270  -8.430  1.186  1.00 86.81  ? 359 LEU   A O   1 
ATOM   2180 C CB  . LEU   A 1 284 ? -0.818  -7.936  2.326  1.00 53.56  ? 359 LEU   A CB  1 
ATOM   2181 C CG  . LEU   A 1 284 ? 0.461   -8.054  3.155  1.00 38.02  ? 359 LEU   A CG  1 
ATOM   2182 C CD1 . LEU   A 1 284 ? 0.615   -6.872  4.086  1.00 36.00  ? 359 LEU   A CD1 1 
ATOM   2183 C CD2 . LEU   A 1 284 ? 0.447   -9.348  3.943  1.00 54.15  ? 359 LEU   A CD2 1 
ATOM   2184 N N   . ARG   A 1 285 ? -2.469  -9.566  -0.575 1.00 90.26  ? 360 ARG   A N   1 
ATOM   2185 C CA  . ARG   A 1 285 ? -3.767  -9.634  -1.231 1.00 97.72  ? 360 ARG   A CA  1 
ATOM   2186 C C   . ARG   A 1 285 ? -4.693  -10.598 -0.497 1.00 110.83 ? 360 ARG   A C   1 
ATOM   2187 O O   . ARG   A 1 285 ? -4.266  -11.665 -0.045 1.00 97.81  ? 360 ARG   A O   1 
ATOM   2188 C CB  . ARG   A 1 285 ? -3.603  -10.075 -2.688 1.00 105.16 ? 360 ARG   A CB  1 
ATOM   2189 C CG  . ARG   A 1 285 ? -2.913  -11.424 -2.852 1.00 112.50 ? 360 ARG   A CG  1 
ATOM   2190 C CD  . ARG   A 1 285 ? -3.210  -12.065 -4.201 1.00 114.84 ? 360 ARG   A CD  1 
ATOM   2191 N NE  . ARG   A 1 285 ? -2.414  -11.495 -5.282 1.00 119.96 ? 360 ARG   A NE  1 
ATOM   2192 C CZ  . ARG   A 1 285 ? -2.402  -11.958 -6.525 1.00 124.99 ? 360 ARG   A CZ  1 
ATOM   2193 N NH1 . ARG   A 1 285 ? -3.138  -12.998 -6.883 1.00 103.37 ? 360 ARG   A NH1 1 
ATOM   2194 N NH2 . ARG   A 1 285 ? -1.631  -11.364 -7.431 1.00 127.30 ? 360 ARG   A NH2 1 
ATOM   2195 N N   . GLN   A 1 286 ? -5.964  -10.203 -0.386 1.00 116.30 ? 361 GLN   A N   1 
ATOM   2196 C CA  . GLN   A 1 286 ? -7.067  -10.997 0.183  1.00 103.27 ? 361 GLN   A CA  1 
ATOM   2197 C C   . GLN   A 1 286 ? -6.664  -12.186 1.056  1.00 96.89  ? 361 GLN   A C   1 
ATOM   2198 O O   . GLN   A 1 286 ? -7.196  -13.287 0.908  1.00 98.19  ? 361 GLN   A O   1 
ATOM   2199 C CB  . GLN   A 1 286 ? -7.971  -11.496 -0.948 1.00 82.31  ? 361 GLN   A CB  1 
ATOM   2200 C CG  . GLN   A 1 286 ? -7.233  -12.191 -2.082 1.00 110.43 ? 361 GLN   A CG  1 
ATOM   2201 C CD  . GLN   A 1 286 ? -8.148  -12.549 -3.234 1.00 127.13 ? 361 GLN   A CD  1 
ATOM   2202 O OE1 . GLN   A 1 286 ? -9.320  -12.175 -3.249 1.00 140.88 ? 361 GLN   A OE1 1 
ATOM   2203 N NE2 . GLN   A 1 286 ? -7.616  -13.277 -4.209 1.00 116.87 ? 361 GLN   A NE2 1 
ATOM   2204 N N   . ALA   B 1 1   ? 24.100  -38.361 48.231 1.00 87.03  ? 76  ALA   B N   1 
ATOM   2205 C CA  . ALA   B 1 1   ? 23.333  -37.746 47.154 1.00 69.70  ? 76  ALA   B CA  1 
ATOM   2206 C C   . ALA   B 1 1   ? 22.942  -38.784 46.104 1.00 85.45  ? 76  ALA   B C   1 
ATOM   2207 O O   . ALA   B 1 1   ? 23.789  -39.542 45.630 1.00 81.51  ? 76  ALA   B O   1 
ATOM   2208 C CB  . ALA   B 1 1   ? 24.128  -36.616 46.519 1.00 72.96  ? 76  ALA   B CB  1 
ATOM   2209 N N   . LEU   B 1 2   ? 21.656  -38.819 45.753 1.00 87.86  ? 77  LEU   B N   1 
ATOM   2210 C CA  . LEU   B 1 2   ? 21.181  -39.745 44.733 1.00 69.78  ? 77  LEU   B CA  1 
ATOM   2211 C C   . LEU   B 1 2   ? 21.841  -39.452 43.391 1.00 84.23  ? 77  LEU   B C   1 
ATOM   2212 O O   . LEU   B 1 2   ? 22.152  -38.303 43.060 1.00 107.86 ? 77  LEU   B O   1 
ATOM   2213 C CB  . LEU   B 1 2   ? 19.660  -39.659 44.587 1.00 64.40  ? 77  LEU   B CB  1 
ATOM   2214 C CG  . LEU   B 1 2   ? 18.809  -40.233 45.721 1.00 76.89  ? 77  LEU   B CG  1 
ATOM   2215 C CD1 . LEU   B 1 2   ? 17.330  -40.100 45.397 1.00 64.67  ? 77  LEU   B CD1 1 
ATOM   2216 C CD2 . LEU   B 1 2   ? 19.172  -41.685 45.976 1.00 68.79  ? 77  LEU   B CD2 1 
ATOM   2217 N N   . GLN   B 1 3   ? 22.051  -40.507 42.615 1.00 67.63  ? 78  GLN   B N   1 
ATOM   2218 C CA  . GLN   B 1 3   ? 22.695  -40.401 41.319 1.00 63.78  ? 78  GLN   B CA  1 
ATOM   2219 C C   . GLN   B 1 3   ? 21.836  -41.073 40.261 1.00 53.00  ? 78  GLN   B C   1 
ATOM   2220 O O   . GLN   B 1 3   ? 21.090  -42.010 40.562 1.00 57.61  ? 78  GLN   B O   1 
ATOM   2221 C CB  . GLN   B 1 3   ? 24.089  -41.046 41.337 1.00 82.57  ? 78  GLN   B CB  1 
ATOM   2222 C CG  . GLN   B 1 3   ? 25.121  -40.286 42.153 1.00 77.01  ? 78  GLN   B CG  1 
ATOM   2223 C CD  . GLN   B 1 3   ? 26.473  -40.972 42.162 1.00 98.36  ? 78  GLN   B CD  1 
ATOM   2224 O OE1 . GLN   B 1 3   ? 26.591  -42.137 41.785 1.00 114.68 ? 78  GLN   B OE1 1 
ATOM   2225 N NE2 . GLN   B 1 3   ? 27.501  -40.250 42.592 1.00 106.30 ? 78  GLN   B NE2 1 
ATOM   2226 N N   . PRO   B 1 4   ? 21.915  -40.611 39.018 1.00 58.84  ? 79  PRO   B N   1 
ATOM   2227 C CA  . PRO   B 1 4   ? 21.158  -41.255 37.944 1.00 44.43  ? 79  PRO   B CA  1 
ATOM   2228 C C   . PRO   B 1 4   ? 21.817  -42.548 37.501 1.00 46.47  ? 79  PRO   B C   1 
ATOM   2229 O O   . PRO   B 1 4   ? 23.030  -42.736 37.619 1.00 66.63  ? 79  PRO   B O   1 
ATOM   2230 C CB  . PRO   B 1 4   ? 21.193  -40.211 36.825 1.00 43.61  ? 79  PRO   B CB  1 
ATOM   2231 C CG  . PRO   B 1 4   ? 22.489  -39.530 37.030 1.00 55.76  ? 79  PRO   B CG  1 
ATOM   2232 C CD  . PRO   B 1 4   ? 22.685  -39.457 38.523 1.00 60.45  ? 79  PRO   B CD  1 
ATOM   2233 N N   . ARG   B 1 5   ? 20.990  -43.451 36.986 1.00 48.86  ? 80  ARG   B N   1 
ATOM   2234 C CA  . ARG   B 1 5   ? 21.450  -44.721 36.442 1.00 35.81  ? 80  ARG   B CA  1 
ATOM   2235 C C   . ARG   B 1 5   ? 21.016  -44.804 34.988 1.00 36.08  ? 80  ARG   B C   1 
ATOM   2236 O O   . ARG   B 1 5   ? 19.817  -44.763 34.691 1.00 48.08  ? 80  ARG   B O   1 
ATOM   2237 C CB  . ARG   B 1 5   ? 20.895  -45.905 37.235 1.00 43.52  ? 80  ARG   B CB  1 
ATOM   2238 C CG  . ARG   B 1 5   ? 21.250  -47.244 36.618 1.00 57.36  ? 80  ARG   B CG  1 
ATOM   2239 C CD  . ARG   B 1 5   ? 20.626  -48.408 37.360 1.00 52.58  ? 80  ARG   B CD  1 
ATOM   2240 N NE  . ARG   B 1 5   ? 20.985  -49.674 36.733 1.00 59.73  ? 80  ARG   B NE  1 
ATOM   2241 C CZ  . ARG   B 1 5   ? 20.324  -50.219 35.723 1.00 50.14  ? 80  ARG   B CZ  1 
ATOM   2242 N NH1 . ARG   B 1 5   ? 19.245  -49.647 35.216 1.00 56.84  ? 80  ARG   B NH1 1 
ATOM   2243 N NH2 . ARG   B 1 5   ? 20.757  -51.367 35.208 1.00 68.68  ? 80  ARG   B NH2 1 
ATOM   2244 N N   . ARG   B 1 6   ? 21.988  -44.914 34.089 1.00 37.79  ? 81  ARG   B N   1 
ATOM   2245 C CA  . ARG   B 1 6   ? 21.689  -44.992 32.667 1.00 34.15  ? 81  ARG   B CA  1 
ATOM   2246 C C   . ARG   B 1 6   ? 21.012  -46.316 32.341 1.00 39.94  ? 81  ARG   B C   1 
ATOM   2247 O O   . ARG   B 1 6   ? 21.514  -47.388 32.694 1.00 58.02  ? 81  ARG   B O   1 
ATOM   2248 C CB  . ARG   B 1 6   ? 22.974  -44.838 31.858 1.00 43.54  ? 81  ARG   B CB  1 
ATOM   2249 C CG  . ARG   B 1 6   ? 22.830  -45.114 30.375 1.00 51.37  ? 81  ARG   B CG  1 
ATOM   2250 C CD  . ARG   B 1 6   ? 24.149  -44.847 29.661 1.00 80.34  ? 81  ARG   B CD  1 
ATOM   2251 N NE  . ARG   B 1 6   ? 25.276  -45.510 30.307 1.00 103.69 ? 81  ARG   B NE  1 
ATOM   2252 C CZ  . ARG   B 1 6   ? 25.847  -46.626 29.871 1.00 90.33  ? 81  ARG   B CZ  1 
ATOM   2253 N NH1 . ARG   B 1 6   ? 25.428  -47.234 28.772 1.00 76.56  ? 81  ARG   B NH1 1 
ATOM   2254 N NH2 . ARG   B 1 6   ? 26.869  -47.139 30.549 1.00 52.74  ? 81  ARG   B NH2 1 
ATOM   2255 N N   . VAL   B 1 7   ? 19.865  -46.239 31.670 1.00 49.42  ? 82  VAL   B N   1 
ATOM   2256 C CA  . VAL   B 1 7   ? 19.164  -47.426 31.177 1.00 36.74  ? 82  VAL   B CA  1 
ATOM   2257 C C   . VAL   B 1 7   ? 19.715  -47.684 29.779 1.00 55.30  ? 82  VAL   B C   1 
ATOM   2258 O O   . VAL   B 1 7   ? 19.222  -47.161 28.777 1.00 60.52  ? 82  VAL   B O   1 
ATOM   2259 C CB  . VAL   B 1 7   ? 17.650  -47.243 31.186 1.00 37.34  ? 82  VAL   B CB  1 
ATOM   2260 C CG1 . VAL   B 1 7   ? 16.963  -48.485 30.651 1.00 42.59  ? 82  VAL   B CG1 1 
ATOM   2261 C CG2 . VAL   B 1 7   ? 17.176  -46.932 32.595 1.00 39.76  ? 82  VAL   B CG2 1 
ATOM   2262 N N   . SER   B 1 8   ? 20.762  -48.501 29.716 1.00 79.22  ? 83  SER   B N   1 
ATOM   2263 C CA  . SER   B 1 8   ? 21.495  -48.698 28.475 1.00 64.77  ? 83  SER   B CA  1 
ATOM   2264 C C   . SER   B 1 8   ? 20.643  -49.417 27.437 1.00 57.11  ? 83  SER   B C   1 
ATOM   2265 O O   . SER   B 1 8   ? 19.739  -50.195 27.763 1.00 55.20  ? 83  SER   B O   1 
ATOM   2266 C CB  . SER   B 1 8   ? 22.776  -49.490 28.736 1.00 63.95  ? 83  SER   B CB  1 
ATOM   2267 O OG  . SER   B 1 8   ? 22.486  -50.758 29.295 1.00 80.37  ? 83  SER   B OG  1 
ATOM   2268 N N   . PHE   B 1 9   ? 20.946  -49.141 26.171 1.00 43.03  ? 84  PHE   B N   1 
ATOM   2269 C CA  . PHE   B 1 9   ? 20.255  -49.738 25.038 1.00 73.30  ? 84  PHE   B CA  1 
ATOM   2270 C C   . PHE   B 1 9   ? 21.118  -49.545 23.799 1.00 77.36  ? 84  PHE   B C   1 
ATOM   2271 O O   . PHE   B 1 9   ? 21.800  -48.528 23.656 1.00 69.89  ? 84  PHE   B O   1 
ATOM   2272 C CB  . PHE   B 1 9   ? 18.866  -49.119 24.827 1.00 49.48  ? 84  PHE   B CB  1 
ATOM   2273 C CG  . PHE   B 1 9   ? 18.901  -47.660 24.469 1.00 64.90  ? 84  PHE   B CG  1 
ATOM   2274 C CD1 . PHE   B 1 9   ? 19.017  -46.693 25.455 1.00 65.03  ? 84  PHE   B CD1 1 
ATOM   2275 C CD2 . PHE   B 1 9   ? 18.814  -47.253 23.146 1.00 71.69  ? 84  PHE   B CD2 1 
ATOM   2276 C CE1 . PHE   B 1 9   ? 19.052  -45.351 25.130 1.00 60.42  ? 84  PHE   B CE1 1 
ATOM   2277 C CE2 . PHE   B 1 9   ? 18.848  -45.913 22.813 1.00 69.78  ? 84  PHE   B CE2 1 
ATOM   2278 C CZ  . PHE   B 1 9   ? 18.966  -44.960 23.806 1.00 63.94  ? 84  PHE   B CZ  1 
ATOM   2279 N N   . ARG   B 1 10  ? 21.090  -50.538 22.913 1.00 72.70  ? 85  ARG   B N   1 
ATOM   2280 C CA  . ARG   B 1 10  ? 21.821  -50.434 21.660 1.00 70.47  ? 85  ARG   B CA  1 
ATOM   2281 C C   . ARG   B 1 10  ? 21.324  -49.235 20.864 1.00 72.59  ? 85  ARG   B C   1 
ATOM   2282 O O   . ARG   B 1 10  ? 20.124  -49.109 20.597 1.00 75.20  ? 85  ARG   B O   1 
ATOM   2283 C CB  . ARG   B 1 10  ? 21.663  -51.718 20.848 1.00 69.57  ? 85  ARG   B CB  1 
ATOM   2284 C CG  . ARG   B 1 10  ? 22.325  -52.942 21.459 1.00 77.04  ? 85  ARG   B CG  1 
ATOM   2285 C CD  . ARG   B 1 10  ? 22.241  -54.121 20.504 1.00 106.28 ? 85  ARG   B CD  1 
ATOM   2286 N NE  . ARG   B 1 10  ? 22.794  -55.345 21.070 1.00 102.36 ? 85  ARG   B NE  1 
ATOM   2287 C CZ  . ARG   B 1 10  ? 22.787  -56.520 20.455 1.00 116.50 ? 85  ARG   B CZ  1 
ATOM   2288 N NH1 . ARG   B 1 10  ? 22.270  -56.664 19.246 1.00 121.62 ? 85  ARG   B NH1 1 
ATOM   2289 N NH2 . ARG   B 1 10  ? 23.308  -57.578 21.070 1.00 118.79 ? 85  ARG   B NH2 1 
ATOM   2290 N N   . GLY   B 1 11  ? 22.244  -48.348 20.499 1.00 70.61  ? 86  GLY   B N   1 
ATOM   2291 C CA  . GLY   B 1 11  ? 21.902  -47.155 19.759 1.00 66.43  ? 86  GLY   B CA  1 
ATOM   2292 C C   . GLY   B 1 11  ? 21.832  -45.878 20.566 1.00 79.89  ? 86  GLY   B C   1 
ATOM   2293 O O   . GLY   B 1 11  ? 21.371  -44.858 20.037 1.00 73.33  ? 86  GLY   B O   1 
ATOM   2294 N N   . GLU   B 1 12  ? 22.267  -45.897 21.824 1.00 85.76  ? 87  GLU   B N   1 
ATOM   2295 C CA  . GLU   B 1 12  ? 22.272  -44.683 22.626 1.00 73.89  ? 87  GLU   B CA  1 
ATOM   2296 C C   . GLU   B 1 12  ? 23.375  -43.742 22.155 1.00 80.25  ? 87  GLU   B C   1 
ATOM   2297 O O   . GLU   B 1 12  ? 24.410  -44.166 21.630 1.00 80.84  ? 87  GLU   B O   1 
ATOM   2298 C CB  . GLU   B 1 12  ? 22.450  -45.017 24.108 1.00 64.65  ? 87  GLU   B CB  1 
ATOM   2299 C CG  . GLU   B 1 12  ? 23.638  -45.904 24.412 1.00 70.42  ? 87  GLU   B CG  1 
ATOM   2300 C CD  . GLU   B 1 12  ? 23.901  -46.001 25.898 1.00 82.90  ? 87  GLU   B CD  1 
ATOM   2301 O OE1 . GLU   B 1 12  ? 23.251  -45.253 26.661 1.00 78.81  ? 87  GLU   B OE1 1 
ATOM   2302 O OE2 . GLU   B 1 12  ? 24.753  -46.820 26.304 1.00 94.60  ? 87  GLU   B OE2 1 
ATOM   2303 N N   . ALA   B 1 13  ? 23.149  -42.445 22.369 1.00 73.87  ? 88  ALA   B N   1 
ATOM   2304 C CA  . ALA   B 1 13  ? 24.055  -41.434 21.839 1.00 61.39  ? 88  ALA   B CA  1 
ATOM   2305 C C   . ALA   B 1 13  ? 25.345  -41.321 22.639 1.00 75.35  ? 88  ALA   B C   1 
ATOM   2306 O O   . ALA   B 1 13  ? 26.371  -40.907 22.089 1.00 86.26  ? 88  ALA   B O   1 
ATOM   2307 C CB  . ALA   B 1 13  ? 23.356  -40.076 21.792 1.00 69.93  ? 88  ALA   B CB  1 
ATOM   2308 N N   . SER   B 1 14  ? 25.323  -41.670 23.923 1.00 83.52  ? 89  SER   B N   1 
ATOM   2309 C CA  . SER   B 1 14  ? 26.495  -41.515 24.774 1.00 101.32 ? 89  SER   B CA  1 
ATOM   2310 C C   . SER   B 1 14  ? 26.684  -42.763 25.620 1.00 99.71  ? 89  SER   B C   1 
ATOM   2311 O O   . SER   B 1 14  ? 25.736  -43.237 26.254 1.00 97.22  ? 89  SER   B O   1 
ATOM   2312 C CB  . SER   B 1 14  ? 26.368  -40.279 25.674 1.00 98.66  ? 89  SER   B CB  1 
ATOM   2313 O OG  . SER   B 1 14  ? 27.449  -40.192 26.587 1.00 111.21 ? 89  SER   B OG  1 
ATOM   2314 N N   . GLU   B 1 15  ? 27.913  -43.286 25.626 1.00 119.36 ? 90  GLU   B N   1 
ATOM   2315 C CA  . GLU   B 1 15  ? 28.227  -44.450 26.446 1.00 117.74 ? 90  GLU   B CA  1 
ATOM   2316 C C   . GLU   B 1 15  ? 28.258  -44.097 27.926 1.00 112.52 ? 90  GLU   B C   1 
ATOM   2317 O O   . GLU   B 1 15  ? 28.029  -44.965 28.775 1.00 100.62 ? 90  GLU   B O   1 
ATOM   2318 C CB  . GLU   B 1 15  ? 29.571  -45.048 26.023 1.00 125.57 ? 90  GLU   B CB  1 
ATOM   2319 C CG  . GLU   B 1 15  ? 29.736  -45.284 24.522 1.00 119.73 ? 90  GLU   B CG  1 
ATOM   2320 C CD  . GLU   B 1 15  ? 30.173  -44.037 23.766 1.00 116.10 ? 90  GLU   B CD  1 
ATOM   2321 O OE1 . GLU   B 1 15  ? 29.530  -42.980 23.931 1.00 119.62 ? 90  GLU   B OE1 1 
ATOM   2322 O OE2 . GLU   B 1 15  ? 31.166  -44.113 23.010 1.00 95.42  ? 90  GLU   B OE2 1 
ATOM   2323 N N   . THR   B 1 16  ? 28.541  -42.840 28.252 1.00 126.32 ? 91  THR   B N   1 
ATOM   2324 C CA  . THR   B 1 16  ? 28.613  -42.372 29.628 1.00 117.91 ? 91  THR   B CA  1 
ATOM   2325 C C   . THR   B 1 16  ? 27.508  -41.357 29.874 1.00 123.81 ? 91  THR   B C   1 
ATOM   2326 O O   . THR   B 1 16  ? 27.285  -40.461 29.052 1.00 126.21 ? 91  THR   B O   1 
ATOM   2327 C CB  . THR   B 1 16  ? 29.976  -41.742 29.926 1.00 113.32 ? 91  THR   B CB  1 
ATOM   2328 O OG1 . THR   B 1 16  ? 31.015  -42.690 29.651 1.00 136.47 ? 91  THR   B OG1 1 
ATOM   2329 C CG2 . THR   B 1 16  ? 30.061  -41.311 31.387 1.00 119.87 ? 91  THR   B CG2 1 
ATOM   2330 N N   . LEU   B 1 17  ? 26.814  -41.505 30.997 1.00 107.00 ? 92  LEU   B N   1 
ATOM   2331 C CA  . LEU   B 1 17  ? 25.842  -40.507 31.431 1.00 89.16  ? 92  LEU   B CA  1 
ATOM   2332 C C   . LEU   B 1 17  ? 26.611  -39.408 32.150 1.00 100.64 ? 92  LEU   B C   1 
ATOM   2333 O O   . LEU   B 1 17  ? 26.986  -39.552 33.318 1.00 82.28  ? 92  LEU   B O   1 
ATOM   2334 C CB  . LEU   B 1 17  ? 24.786  -41.136 32.330 1.00 64.19  ? 92  LEU   B CB  1 
ATOM   2335 C CG  . LEU   B 1 17  ? 23.489  -40.347 32.475 1.00 51.74  ? 92  LEU   B CG  1 
ATOM   2336 C CD1 . LEU   B 1 17  ? 22.731  -40.341 31.161 1.00 55.92  ? 92  LEU   B CD1 1 
ATOM   2337 C CD2 . LEU   B 1 17  ? 22.645  -40.941 33.583 1.00 47.52  ? 92  LEU   B CD2 1 
ATOM   2338 N N   . GLN   B 1 18  ? 26.866  -38.310 31.445 1.00 96.85  ? 93  GLN   B N   1 
ATOM   2339 C CA  . GLN   B 1 18  ? 27.663  -37.224 31.990 1.00 95.79  ? 93  GLN   B CA  1 
ATOM   2340 C C   . GLN   B 1 18  ? 27.183  -35.912 31.390 1.00 75.21  ? 93  GLN   B C   1 
ATOM   2341 O O   . GLN   B 1 18  ? 26.441  -35.886 30.404 1.00 76.58  ? 93  GLN   B O   1 
ATOM   2342 C CB  . GLN   B 1 18  ? 29.154  -37.430 31.712 1.00 112.78 ? 93  GLN   B CB  1 
ATOM   2343 C CG  . GLN   B 1 18  ? 29.519  -37.314 30.243 1.00 119.14 ? 93  GLN   B CG  1 
ATOM   2344 C CD  . GLN   B 1 18  ? 30.992  -37.552 29.987 1.00 124.79 ? 93  GLN   B CD  1 
ATOM   2345 O OE1 . GLN   B 1 18  ? 31.605  -38.432 30.592 1.00 101.65 ? 93  GLN   B OE1 1 
ATOM   2346 N NE2 . GLN   B 1 18  ? 31.572  -36.763 29.090 1.00 130.66 ? 93  GLN   B NE2 1 
ATOM   2347 N N   . SER   B 1 19  ? 27.630  -34.815 31.999 1.00 92.47  ? 94  SER   B N   1 
ATOM   2348 C CA  . SER   B 1 19  ? 27.266  -33.475 31.565 1.00 93.99  ? 94  SER   B CA  1 
ATOM   2349 C C   . SER   B 1 19  ? 28.188  -32.442 32.201 1.00 85.92  ? 94  SER   B C   1 
ATOM   2350 O O   . SER   B 1 19  ? 28.677  -32.647 33.321 1.00 95.62  ? 94  SER   B O   1 
ATOM   2351 C CB  . SER   B 1 19  ? 25.810  -33.176 31.918 1.00 81.15  ? 94  SER   B CB  1 
ATOM   2352 O OG  . SER   B 1 19  ? 25.451  -31.855 31.553 1.00 91.04  ? 94  SER   B OG  1 
ATOM   2353 N N   . PRO   B 1 20  ? 28.464  -31.328 31.518 1.00 100.41 ? 95  PRO   B N   1 
ATOM   2354 C CA  . PRO   B 1 20  ? 29.237  -30.257 32.161 1.00 107.65 ? 95  PRO   B CA  1 
ATOM   2355 C C   . PRO   B 1 20  ? 28.483  -29.567 33.282 1.00 103.12 ? 95  PRO   B C   1 
ATOM   2356 O O   . PRO   B 1 20  ? 29.120  -28.950 34.145 1.00 90.16  ? 95  PRO   B O   1 
ATOM   2357 C CB  . PRO   B 1 20  ? 29.533  -29.291 31.005 1.00 92.39  ? 95  PRO   B CB  1 
ATOM   2358 C CG  . PRO   B 1 20  ? 28.444  -29.542 30.020 1.00 80.81  ? 95  PRO   B CG  1 
ATOM   2359 C CD  . PRO   B 1 20  ? 28.145  -31.013 30.115 1.00 96.88  ? 95  PRO   B CD  1 
ATOM   2360 N N   . GLY   B 1 21  ? 27.155  -29.667 33.308 1.00 90.86  ? 96  GLY   B N   1 
ATOM   2361 C CA  . GLY   B 1 21  ? 26.362  -29.009 34.326 1.00 64.22  ? 96  GLY   B CA  1 
ATOM   2362 C C   . GLY   B 1 21  ? 26.062  -29.873 35.534 1.00 94.45  ? 96  GLY   B C   1 
ATOM   2363 O O   . GLY   B 1 21  ? 25.687  -29.355 36.591 1.00 102.07 ? 96  GLY   B O   1 
ATOM   2364 N N   . TYR   B 1 22  ? 26.229  -31.188 35.403 1.00 101.09 ? 97  TYR   B N   1 
ATOM   2365 C CA  . TYR   B 1 22  ? 25.878  -32.098 36.485 1.00 92.31  ? 97  TYR   B CA  1 
ATOM   2366 C C   . TYR   B 1 22  ? 26.985  -32.159 37.525 1.00 84.17  ? 97  TYR   B C   1 
ATOM   2367 O O   . TYR   B 1 22  ? 28.146  -32.427 37.200 1.00 83.33  ? 97  TYR   B O   1 
ATOM   2368 C CB  . TYR   B 1 22  ? 25.596  -33.502 35.959 1.00 80.51  ? 97  TYR   B CB  1 
ATOM   2369 C CG  . TYR   B 1 22  ? 25.173  -34.458 37.055 1.00 76.59  ? 97  TYR   B CG  1 
ATOM   2370 C CD1 . TYR   B 1 22  ? 24.084  -34.167 37.868 1.00 83.30  ? 97  TYR   B CD1 1 
ATOM   2371 C CD2 . TYR   B 1 22  ? 25.858  -35.645 37.281 1.00 51.51  ? 97  TYR   B CD2 1 
ATOM   2372 C CE1 . TYR   B 1 22  ? 23.685  -35.031 38.874 1.00 79.00  ? 97  TYR   B CE1 1 
ATOM   2373 C CE2 . TYR   B 1 22  ? 25.465  -36.519 38.287 1.00 62.54  ? 97  TYR   B CE2 1 
ATOM   2374 C CZ  . TYR   B 1 22  ? 24.377  -36.204 39.079 1.00 63.07  ? 97  TYR   B CZ  1 
ATOM   2375 O OH  . TYR   B 1 22  ? 23.978  -37.061 40.081 1.00 55.76  ? 97  TYR   B OH  1 
ATOM   2376 N N   . ASP   B 1 23  ? 26.613  -31.923 38.776 1.00 86.20  ? 98  ASP   B N   1 
ATOM   2377 C CA  . ASP   B 1 23  ? 27.514  -32.061 39.918 1.00 84.21  ? 98  ASP   B CA  1 
ATOM   2378 C C   . ASP   B 1 23  ? 26.942  -33.121 40.847 1.00 81.30  ? 98  ASP   B C   1 
ATOM   2379 O O   . ASP   B 1 23  ? 25.849  -32.920 41.409 1.00 90.63  ? 98  ASP   B O   1 
ATOM   2380 C CB  . ASP   B 1 23  ? 27.669  -30.727 40.647 1.00 88.33  ? 98  ASP   B CB  1 
ATOM   2381 C CG  . ASP   B 1 23  ? 28.567  -30.826 41.859 1.00 104.62 ? 98  ASP   B CG  1 
ATOM   2382 O OD1 . ASP   B 1 23  ? 29.794  -30.977 41.681 1.00 118.60 ? 98  ASP   B OD1 1 
ATOM   2383 O OD2 . ASP   B 1 23  ? 28.045  -30.748 42.991 1.00 103.29 ? 98  ASP   B OD2 1 
ATOM   2384 N N   . PRO   B 1 24  ? 27.620  -34.258 41.038 1.00 93.07  ? 99  PRO   B N   1 
ATOM   2385 C CA  . PRO   B 1 24  ? 27.039  -35.339 41.856 1.00 81.83  ? 99  PRO   B CA  1 
ATOM   2386 C C   . PRO   B 1 24  ? 26.796  -34.962 43.311 1.00 97.16  ? 99  PRO   B C   1 
ATOM   2387 O O   . PRO   B 1 24  ? 26.174  -35.751 44.036 1.00 80.74  ? 99  PRO   B O   1 
ATOM   2388 C CB  . PRO   B 1 24  ? 28.080  -36.464 41.744 1.00 62.33  ? 99  PRO   B CB  1 
ATOM   2389 C CG  . PRO   B 1 24  ? 28.845  -36.155 40.491 1.00 75.97  ? 99  PRO   B CG  1 
ATOM   2390 C CD  . PRO   B 1 24  ? 28.890  -34.658 40.411 1.00 99.95  ? 99  PRO   B CD  1 
ATOM   2391 N N   . SER   B 1 25  ? 27.256  -33.793 43.759 1.00 111.00 ? 100 SER   B N   1 
ATOM   2392 C CA  . SER   B 1 25  ? 27.060  -33.365 45.138 1.00 108.96 ? 100 SER   B CA  1 
ATOM   2393 C C   . SER   B 1 25  ? 25.792  -32.538 45.319 1.00 105.21 ? 100 SER   B C   1 
ATOM   2394 O O   . SER   B 1 25  ? 25.094  -32.696 46.326 1.00 121.03 ? 100 SER   B O   1 
ATOM   2395 C CB  . SER   B 1 25  ? 28.273  -32.562 45.616 1.00 98.12  ? 100 SER   B CB  1 
ATOM   2396 O OG  . SER   B 1 25  ? 29.469  -33.304 45.461 1.00 119.71 ? 100 SER   B OG  1 
ATOM   2397 N N   . ARG   B 1 26  ? 25.483  -31.659 44.370 1.00 95.03  ? 101 ARG   B N   1 
ATOM   2398 C CA  . ARG   B 1 26  ? 24.308  -30.811 44.501 1.00 81.37  ? 101 ARG   B CA  1 
ATOM   2399 C C   . ARG   B 1 26  ? 23.044  -31.669 44.535 1.00 87.39  ? 101 ARG   B C   1 
ATOM   2400 O O   . ARG   B 1 26  ? 22.973  -32.701 43.857 1.00 90.84  ? 101 ARG   B O   1 
ATOM   2401 C CB  . ARG   B 1 26  ? 24.238  -29.806 43.350 1.00 84.59  ? 101 ARG   B CB  1 
ATOM   2402 C CG  . ARG   B 1 26  ? 25.307  -28.723 43.408 1.00 97.23  ? 101 ARG   B CG  1 
ATOM   2403 C CD  . ARG   B 1 26  ? 25.180  -27.749 42.245 1.00 119.94 ? 101 ARG   B CD  1 
ATOM   2404 N NE  . ARG   B 1 26  ? 23.953  -26.962 42.309 1.00 116.97 ? 101 ARG   B NE  1 
ATOM   2405 C CZ  . ARG   B 1 26  ? 23.865  -25.750 42.842 1.00 125.70 ? 101 ARG   B CZ  1 
ATOM   2406 N NH1 . ARG   B 1 26  ? 24.917  -25.150 43.376 1.00 106.17 ? 101 ARG   B NH1 1 
ATOM   2407 N NH2 . ARG   B 1 26  ? 22.692  -25.123 42.837 1.00 105.38 ? 101 ARG   B NH2 1 
ATOM   2408 N N   . PRO   B 1 27  ? 22.031  -31.279 45.316 1.00 93.61  ? 102 PRO   B N   1 
ATOM   2409 C CA  . PRO   B 1 27  ? 20.845  -32.137 45.459 1.00 79.78  ? 102 PRO   B CA  1 
ATOM   2410 C C   . PRO   B 1 27  ? 19.974  -32.192 44.218 1.00 79.98  ? 102 PRO   B C   1 
ATOM   2411 O O   . PRO   B 1 27  ? 19.128  -33.091 44.123 1.00 71.24  ? 102 PRO   B O   1 
ATOM   2412 C CB  . PRO   B 1 27  ? 20.095  -31.503 46.636 1.00 89.54  ? 102 PRO   B CB  1 
ATOM   2413 C CG  . PRO   B 1 27  ? 20.495  -30.066 46.592 1.00 90.46  ? 102 PRO   B CG  1 
ATOM   2414 C CD  . PRO   B 1 27  ? 21.926  -30.050 46.122 1.00 93.31  ? 102 PRO   B CD  1 
ATOM   2415 N N   . GLU   B 1 28  ? 20.145  -31.271 43.272 1.00 85.62  ? 103 GLU   B N   1 
ATOM   2416 C CA  . GLU   B 1 28  ? 19.326  -31.280 42.068 1.00 78.51  ? 103 GLU   B CA  1 
ATOM   2417 C C   . GLU   B 1 28  ? 19.544  -32.568 41.282 1.00 68.93  ? 103 GLU   B C   1 
ATOM   2418 O O   . GLU   B 1 28  ? 20.610  -33.187 41.340 1.00 73.72  ? 103 GLU   B O   1 
ATOM   2419 C CB  . GLU   B 1 28  ? 19.646  -30.069 41.189 1.00 80.26  ? 103 GLU   B CB  1 
ATOM   2420 C CG  . GLU   B 1 28  ? 19.198  -28.730 41.760 1.00 74.90  ? 103 GLU   B CG  1 
ATOM   2421 C CD  . GLU   B 1 28  ? 20.135  -28.197 42.826 1.00 105.52 ? 103 GLU   B CD  1 
ATOM   2422 O OE1 . GLU   B 1 28  ? 21.203  -28.809 43.044 1.00 104.54 ? 103 GLU   B OE1 1 
ATOM   2423 O OE2 . GLU   B 1 28  ? 19.806  -27.163 43.446 1.00 106.47 ? 103 GLU   B OE2 1 
ATOM   2424 N N   . SER   B 1 29  ? 18.514  -32.971 40.542 1.00 73.48  ? 104 SER   B N   1 
ATOM   2425 C CA  . SER   B 1 29  ? 18.593  -34.182 39.745 1.00 65.87  ? 104 SER   B CA  1 
ATOM   2426 C C   . SER   B 1 29  ? 19.497  -33.969 38.532 1.00 50.23  ? 104 SER   B C   1 
ATOM   2427 O O   . SER   B 1 29  ? 19.838  -32.843 38.158 1.00 70.02  ? 104 SER   B O   1 
ATOM   2428 C CB  . SER   B 1 29  ? 17.201  -34.612 39.287 1.00 64.82  ? 104 SER   B CB  1 
ATOM   2429 O OG  . SER   B 1 29  ? 16.644  -33.666 38.389 1.00 55.38  ? 104 SER   B OG  1 
ATOM   2430 N N   . PHE   B 1 30  ? 19.895  -35.085 37.916 1.00 58.45  ? 105 PHE   B N   1 
ATOM   2431 C CA  . PHE   B 1 30  ? 20.652  -35.013 36.672 1.00 52.40  ? 105 PHE   B CA  1 
ATOM   2432 C C   . PHE   B 1 30  ? 19.875  -34.271 35.596 1.00 49.40  ? 105 PHE   B C   1 
ATOM   2433 O O   . PHE   B 1 30  ? 20.469  -33.583 34.760 1.00 59.90  ? 105 PHE   B O   1 
ATOM   2434 C CB  . PHE   B 1 30  ? 21.007  -36.422 36.191 1.00 40.47  ? 105 PHE   B CB  1 
ATOM   2435 C CG  . PHE   B 1 30  ? 21.712  -36.450 34.866 1.00 41.62  ? 105 PHE   B CG  1 
ATOM   2436 C CD1 . PHE   B 1 30  ? 23.071  -36.185 34.779 1.00 48.57  ? 105 PHE   B CD1 1 
ATOM   2437 C CD2 . PHE   B 1 30  ? 21.019  -36.739 33.709 1.00 36.54  ? 105 PHE   B CD2 1 
ATOM   2438 C CE1 . PHE   B 1 30  ? 23.716  -36.209 33.551 1.00 46.31  ? 105 PHE   B CE1 1 
ATOM   2439 C CE2 . PHE   B 1 30  ? 21.657  -36.763 32.486 1.00 43.58  ? 105 PHE   B CE2 1 
ATOM   2440 C CZ  . PHE   B 1 30  ? 23.005  -36.499 32.407 1.00 54.94  ? 105 PHE   B CZ  1 
ATOM   2441 N N   . PHE   B 1 31  ? 18.547  -34.398 35.604 1.00 53.47  ? 106 PHE   B N   1 
ATOM   2442 C CA  . PHE   B 1 31  ? 17.727  -33.714 34.613 1.00 38.52  ? 106 PHE   B CA  1 
ATOM   2443 C C   . PHE   B 1 31  ? 17.809  -32.204 34.777 1.00 64.00  ? 106 PHE   B C   1 
ATOM   2444 O O   . PHE   B 1 31  ? 17.898  -31.470 33.785 1.00 69.36  ? 106 PHE   B O   1 
ATOM   2445 C CB  . PHE   B 1 31  ? 16.281  -34.192 34.728 1.00 46.39  ? 106 PHE   B CB  1 
ATOM   2446 C CG  . PHE   B 1 31  ? 15.323  -33.464 33.831 1.00 42.35  ? 106 PHE   B CG  1 
ATOM   2447 C CD1 . PHE   B 1 31  ? 15.595  -33.305 32.480 1.00 50.68  ? 106 PHE   B CD1 1 
ATOM   2448 C CD2 . PHE   B 1 31  ? 14.135  -32.959 34.336 1.00 54.06  ? 106 PHE   B CD2 1 
ATOM   2449 C CE1 . PHE   B 1 31  ? 14.706  -32.640 31.650 1.00 54.83  ? 106 PHE   B CE1 1 
ATOM   2450 C CE2 . PHE   B 1 31  ? 13.241  -32.296 33.514 1.00 50.49  ? 106 PHE   B CE2 1 
ATOM   2451 C CZ  . PHE   B 1 31  ? 13.526  -32.135 32.168 1.00 45.39  ? 106 PHE   B CZ  1 
ATOM   2452 N N   . GLN   B 1 32  ? 17.795  -31.722 36.019 1.00 67.15  ? 107 GLN   B N   1 
ATOM   2453 C CA  . GLN   B 1 32  ? 17.784  -30.285 36.261 1.00 67.81  ? 107 GLN   B CA  1 
ATOM   2454 C C   . GLN   B 1 32  ? 19.158  -29.655 36.069 1.00 64.93  ? 107 GLN   B C   1 
ATOM   2455 O O   . GLN   B 1 32  ? 19.247  -28.499 35.643 1.00 69.08  ? 107 GLN   B O   1 
ATOM   2456 C CB  . GLN   B 1 32  ? 17.263  -29.999 37.669 1.00 74.40  ? 107 GLN   B CB  1 
ATOM   2457 C CG  . GLN   B 1 32  ? 15.849  -30.499 37.906 1.00 71.41  ? 107 GLN   B CG  1 
ATOM   2458 C CD  . GLN   B 1 32  ? 15.509  -30.615 39.378 1.00 94.68  ? 107 GLN   B CD  1 
ATOM   2459 O OE1 . GLN   B 1 32  ? 16.320  -30.283 40.243 1.00 80.62  ? 107 GLN   B OE1 1 
ATOM   2460 N NE2 . GLN   B 1 32  ? 14.306  -31.096 39.670 1.00 94.97  ? 107 GLN   B NE2 1 
ATOM   2461 N N   . GLN   B 1 33  ? 20.232  -30.390 36.364 1.00 54.68  ? 108 GLN   B N   1 
ATOM   2462 C CA  . GLN   B 1 33  ? 21.574  -29.833 36.242 1.00 55.33  ? 108 GLN   B CA  1 
ATOM   2463 C C   . GLN   B 1 33  ? 22.128  -29.908 34.825 1.00 59.64  ? 108 GLN   B C   1 
ATOM   2464 O O   . GLN   B 1 33  ? 23.046  -29.150 34.497 1.00 84.96  ? 108 GLN   B O   1 
ATOM   2465 C CB  . GLN   B 1 33  ? 22.538  -30.555 37.187 1.00 56.85  ? 108 GLN   B CB  1 
ATOM   2466 C CG  . GLN   B 1 33  ? 22.156  -30.488 38.656 1.00 66.41  ? 108 GLN   B CG  1 
ATOM   2467 C CD  . GLN   B 1 33  ? 23.110  -31.272 39.539 1.00 80.29  ? 108 GLN   B CD  1 
ATOM   2468 O OE1 . GLN   B 1 33  ? 24.320  -31.275 39.315 1.00 83.06  ? 108 GLN   B OE1 1 
ATOM   2469 N NE2 . GLN   B 1 33  ? 22.566  -31.950 40.545 1.00 72.47  ? 108 GLN   B NE2 1 
ATOM   2470 N N   . SER   B 1 34  ? 21.598  -30.792 33.979 1.00 64.16  ? 109 SER   B N   1 
ATOM   2471 C CA  . SER   B 1 34  ? 22.214  -31.089 32.693 1.00 49.28  ? 109 SER   B CA  1 
ATOM   2472 C C   . SER   B 1 34  ? 21.434  -30.571 31.494 1.00 56.45  ? 109 SER   B C   1 
ATOM   2473 O O   . SER   B 1 34  ? 21.888  -30.754 30.359 1.00 51.10  ? 109 SER   B O   1 
ATOM   2474 C CB  . SER   B 1 34  ? 22.412  -32.599 32.550 1.00 57.69  ? 109 SER   B CB  1 
ATOM   2475 O OG  . SER   B 1 34  ? 23.088  -33.114 33.682 1.00 65.99  ? 109 SER   B OG  1 
ATOM   2476 N N   . PHE   B 1 35  ? 20.282  -29.934 31.701 1.00 52.04  ? 110 PHE   B N   1 
ATOM   2477 C CA  . PHE   B 1 35  ? 19.453  -29.491 30.589 1.00 57.72  ? 110 PHE   B CA  1 
ATOM   2478 C C   . PHE   B 1 35  ? 18.924  -28.087 30.839 1.00 68.25  ? 110 PHE   B C   1 
ATOM   2479 O O   . PHE   B 1 35  ? 18.620  -27.717 31.978 1.00 66.40  ? 110 PHE   B O   1 
ATOM   2480 C CB  . PHE   B 1 35  ? 18.280  -30.446 30.354 1.00 48.51  ? 110 PHE   B CB  1 
ATOM   2481 C CG  . PHE   B 1 35  ? 18.689  -31.795 29.838 1.00 53.20  ? 110 PHE   B CG  1 
ATOM   2482 C CD1 . PHE   B 1 35  ? 18.886  -32.001 28.483 1.00 49.13  ? 110 PHE   B CD1 1 
ATOM   2483 C CD2 . PHE   B 1 35  ? 18.875  -32.858 30.706 1.00 42.17  ? 110 PHE   B CD2 1 
ATOM   2484 C CE1 . PHE   B 1 35  ? 19.261  -33.241 28.001 1.00 46.40  ? 110 PHE   B CE1 1 
ATOM   2485 C CE2 . PHE   B 1 35  ? 19.250  -34.101 30.230 1.00 45.40  ? 110 PHE   B CE2 1 
ATOM   2486 C CZ  . PHE   B 1 35  ? 19.443  -34.293 28.875 1.00 42.00  ? 110 PHE   B CZ  1 
ATOM   2487 N N   . GLN   B 1 36  ? 18.818  -27.309 29.764 1.00 64.18  ? 111 GLN   B N   1 
ATOM   2488 C CA  . GLN   B 1 36  ? 18.170  -26.003 29.801 1.00 65.87  ? 111 GLN   B CA  1 
ATOM   2489 C C   . GLN   B 1 36  ? 16.694  -26.209 29.482 1.00 68.34  ? 111 GLN   B C   1 
ATOM   2490 O O   . GLN   B 1 36  ? 16.337  -26.470 28.330 1.00 70.90  ? 111 GLN   B O   1 
ATOM   2491 C CB  . GLN   B 1 36  ? 18.813  -25.046 28.800 1.00 67.06  ? 111 GLN   B CB  1 
ATOM   2492 C CG  . GLN   B 1 36  ? 20.271  -24.728 29.065 1.00 74.06  ? 111 GLN   B CG  1 
ATOM   2493 C CD  . GLN   B 1 36  ? 20.862  -23.822 28.003 1.00 67.31  ? 111 GLN   B CD  1 
ATOM   2494 O OE1 . GLN   B 1 36  ? 20.463  -23.872 26.839 1.00 80.63  ? 111 GLN   B OE1 1 
ATOM   2495 N NE2 . GLN   B 1 36  ? 21.810  -22.982 28.399 1.00 78.48  ? 111 GLN   B NE2 1 
ATOM   2496 N N   . ARG   B 1 37  ? 15.840  -26.104 30.498 1.00 69.93  ? 112 ARG   B N   1 
ATOM   2497 C CA  . ARG   B 1 37  ? 14.410  -26.298 30.288 1.00 62.84  ? 112 ARG   B CA  1 
ATOM   2498 C C   . ARG   B 1 37  ? 13.824  -25.089 29.568 1.00 65.46  ? 112 ARG   B C   1 
ATOM   2499 O O   . ARG   B 1 37  ? 13.853  -23.969 30.089 1.00 78.67  ? 112 ARG   B O   1 
ATOM   2500 C CB  . ARG   B 1 37  ? 13.706  -26.530 31.622 1.00 60.76  ? 112 ARG   B CB  1 
ATOM   2501 C CG  . ARG   B 1 37  ? 12.281  -27.035 31.479 1.00 78.15  ? 112 ARG   B CG  1 
ATOM   2502 C CD  . ARG   B 1 37  ? 11.617  -27.250 32.830 1.00 74.46  ? 112 ARG   B CD  1 
ATOM   2503 N NE  . ARG   B 1 37  ? 12.353  -28.191 33.666 1.00 67.45  ? 112 ARG   B NE  1 
ATOM   2504 C CZ  . ARG   B 1 37  ? 11.868  -28.749 34.767 1.00 95.20  ? 112 ARG   B CZ  1 
ATOM   2505 N NH1 . ARG   B 1 37  ? 10.635  -28.502 35.184 1.00 90.93  ? 112 ARG   B NH1 1 
ATOM   2506 N NH2 . ARG   B 1 37  ? 12.635  -29.581 35.467 1.00 91.28  ? 112 ARG   B NH2 1 
ATOM   2507 N N   . LEU   B 1 38  ? 13.287  -25.314 28.369 1.00 66.77  ? 113 LEU   B N   1 
ATOM   2508 C CA  . LEU   B 1 38  ? 12.740  -24.229 27.559 1.00 62.28  ? 113 LEU   B CA  1 
ATOM   2509 C C   . LEU   B 1 38  ? 11.238  -24.062 27.772 1.00 76.63  ? 113 LEU   B C   1 
ATOM   2510 O O   . LEU   B 1 38  ? 10.773  -22.972 28.120 1.00 93.18  ? 113 LEU   B O   1 
ATOM   2511 C CB  . LEU   B 1 38  ? 13.042  -24.481 26.082 1.00 60.28  ? 113 LEU   B CB  1 
ATOM   2512 C CG  . LEU   B 1 38  ? 14.519  -24.545 25.694 1.00 63.78  ? 113 LEU   B CG  1 
ATOM   2513 C CD1 . LEU   B 1 38  ? 14.653  -24.917 24.232 1.00 64.67  ? 113 LEU   B CD1 1 
ATOM   2514 C CD2 . LEU   B 1 38  ? 15.219  -23.221 25.974 1.00 65.58  ? 113 LEU   B CD2 1 
ATOM   2515 N N   . SER   B 1 39  ? 10.475  -25.133 27.574 1.00 68.63  ? 114 SER   B N   1 
ATOM   2516 C CA  . SER   B 1 39  ? 9.030   -25.094 27.751 1.00 71.98  ? 114 SER   B CA  1 
ATOM   2517 C C   . SER   B 1 39  ? 8.520   -26.522 27.856 1.00 65.33  ? 114 SER   B C   1 
ATOM   2518 O O   . SER   B 1 39  ? 9.259   -27.487 27.646 1.00 69.37  ? 114 SER   B O   1 
ATOM   2519 C CB  . SER   B 1 39  ? 8.344   -24.355 26.600 1.00 85.08  ? 114 SER   B CB  1 
ATOM   2520 O OG  . SER   B 1 39  ? 8.512   -25.053 25.378 1.00 84.84  ? 114 SER   B OG  1 
ATOM   2521 N N   . ARG   B 1 40  ? 7.239   -26.644 28.182 1.00 65.97  ? 115 ARG   B N   1 
ATOM   2522 C CA  . ARG   B 1 40  ? 6.590   -27.940 28.292 1.00 54.43  ? 115 ARG   B CA  1 
ATOM   2523 C C   . ARG   B 1 40  ? 5.867   -28.259 26.993 1.00 53.39  ? 115 ARG   B C   1 
ATOM   2524 O O   . ARG   B 1 40  ? 5.280   -27.375 26.365 1.00 62.29  ? 115 ARG   B O   1 
ATOM   2525 C CB  . ARG   B 1 40  ? 5.611   -27.967 29.468 1.00 52.16  ? 115 ARG   B CB  1 
ATOM   2526 C CG  . ARG   B 1 40  ? 5.123   -29.363 29.815 1.00 57.17  ? 115 ARG   B CG  1 
ATOM   2527 C CD  . ARG   B 1 40  ? 4.601   -29.436 31.241 1.00 65.61  ? 115 ARG   B CD  1 
ATOM   2528 N NE  . ARG   B 1 40  ? 3.335   -28.732 31.409 1.00 75.63  ? 115 ARG   B NE  1 
ATOM   2529 C CZ  . ARG   B 1 40  ? 2.642   -28.701 32.540 1.00 88.16  ? 115 ARG   B CZ  1 
ATOM   2530 N NH1 . ARG   B 1 40  ? 3.070   -29.318 33.630 1.00 87.37  ? 115 ARG   B NH1 1 
ATOM   2531 N NH2 . ARG   B 1 40  ? 1.491   -28.037 32.577 1.00 91.83  ? 115 ARG   B NH2 1 
ATOM   2532 N N   . LEU   B 1 41  ? 5.924   -29.527 26.588 1.00 52.63  ? 116 LEU   B N   1 
ATOM   2533 C CA  . LEU   B 1 41  ? 5.314   -29.986 25.346 1.00 51.64  ? 116 LEU   B CA  1 
ATOM   2534 C C   . LEU   B 1 41  ? 4.004   -30.725 25.571 1.00 49.89  ? 116 LEU   B C   1 
ATOM   2535 O O   . LEU   B 1 41  ? 3.053   -30.544 24.804 1.00 51.11  ? 116 LEU   B O   1 
ATOM   2536 C CB  . LEU   B 1 41  ? 6.289   -30.890 24.586 1.00 42.64  ? 116 LEU   B CB  1 
ATOM   2537 C CG  . LEU   B 1 41  ? 7.550   -30.185 24.077 1.00 56.79  ? 116 LEU   B CG  1 
ATOM   2538 C CD1 . LEU   B 1 41  ? 8.584   -31.189 23.598 1.00 58.17  ? 116 LEU   B CD1 1 
ATOM   2539 C CD2 . LEU   B 1 41  ? 7.205   -29.199 22.969 1.00 66.17  ? 116 LEU   B CD2 1 
ATOM   2540 N N   . GLY   B 1 42  ? 3.932   -31.546 26.608 1.00 46.05  ? 117 GLY   B N   1 
ATOM   2541 C CA  . GLY   B 1 42  ? 2.703   -32.244 26.921 1.00 49.70  ? 117 GLY   B CA  1 
ATOM   2542 C C   . GLY   B 1 42  ? 2.769   -32.829 28.311 1.00 50.59  ? 117 GLY   B C   1 
ATOM   2543 O O   . GLY   B 1 42  ? 3.851   -33.012 28.880 1.00 62.27  ? 117 GLY   B O   1 
ATOM   2544 N N   . HIS   B 1 43  ? 1.589   -33.124 28.851 1.00 73.73  ? 118 HIS   B N   1 
ATOM   2545 C CA  . HIS   B 1 43  ? 1.488   -33.687 30.188 1.00 64.49  ? 118 HIS   B CA  1 
ATOM   2546 C C   . HIS   B 1 43  ? 0.303   -34.639 30.247 1.00 73.07  ? 118 HIS   B C   1 
ATOM   2547 O O   . HIS   B 1 43  ? -0.574  -34.632 29.380 1.00 89.28  ? 118 HIS   B O   1 
ATOM   2548 C CB  . HIS   B 1 43  ? 1.357   -32.589 31.252 1.00 70.08  ? 118 HIS   B CB  1 
ATOM   2549 C CG  . HIS   B 1 43  ? 0.188   -31.677 31.044 1.00 67.90  ? 118 HIS   B CG  1 
ATOM   2550 N ND1 . HIS   B 1 43  ? 0.114   -30.787 29.994 1.00 87.52  ? 118 HIS   B ND1 1 
ATOM   2551 C CD2 . HIS   B 1 43  ? -0.947  -31.507 31.762 1.00 82.98  ? 118 HIS   B CD2 1 
ATOM   2552 C CE1 . HIS   B 1 43  ? -1.021  -30.114 30.069 1.00 90.84  ? 118 HIS   B CE1 1 
ATOM   2553 N NE2 . HIS   B 1 43  ? -1.682  -30.531 31.133 1.00 99.04  ? 118 HIS   B NE2 1 
ATOM   2554 N N   . GLY   B 1 44  ? 0.294   -35.464 31.289 1.00 65.89  ? 119 GLY   B N   1 
ATOM   2555 C CA  . GLY   B 1 44  ? -0.773  -36.429 31.473 1.00 65.06  ? 119 GLY   B CA  1 
ATOM   2556 C C   . GLY   B 1 44  ? -0.454  -37.355 32.630 1.00 78.35  ? 119 GLY   B C   1 
ATOM   2557 O O   . GLY   B 1 44  ? 0.344   -37.021 33.508 1.00 81.08  ? 119 GLY   B O   1 
ATOM   2558 N N   . SER   B 1 45  ? -1.094  -38.525 32.618 1.00 97.97  ? 120 SER   B N   1 
ATOM   2559 C CA  . SER   B 1 45  ? -0.807  -39.534 33.629 1.00 95.26  ? 120 SER   B CA  1 
ATOM   2560 C C   . SER   B 1 45  ? 0.524   -40.232 33.391 1.00 85.30  ? 120 SER   B C   1 
ATOM   2561 O O   . SER   B 1 45  ? 1.112   -40.756 34.344 1.00 87.56  ? 120 SER   B O   1 
ATOM   2562 C CB  . SER   B 1 45  ? -1.933  -40.569 33.680 1.00 102.98 ? 120 SER   B CB  1 
ATOM   2563 O OG  . SER   B 1 45  ? -2.130  -41.166 32.411 1.00 108.05 ? 120 SER   B OG  1 
ATOM   2564 N N   . TYR   B 1 46  ? 1.008   -40.256 32.145 1.00 77.12  ? 121 TYR   B N   1 
ATOM   2565 C CA  . TYR   B 1 46  ? 2.329   -40.810 31.872 1.00 75.99  ? 121 TYR   B CA  1 
ATOM   2566 C C   . TYR   B 1 46  ? 3.428   -39.965 32.503 1.00 73.04  ? 121 TYR   B C   1 
ATOM   2567 O O   . TYR   B 1 46  ? 4.488   -40.492 32.858 1.00 81.65  ? 121 TYR   B O   1 
ATOM   2568 C CB  . TYR   B 1 46  ? 2.549   -40.928 30.361 1.00 82.52  ? 121 TYR   B CB  1 
ATOM   2569 C CG  . TYR   B 1 46  ? 2.419   -39.618 29.608 1.00 80.91  ? 121 TYR   B CG  1 
ATOM   2570 C CD1 . TYR   B 1 46  ? 3.515   -38.780 29.435 1.00 82.12  ? 121 TYR   B CD1 1 
ATOM   2571 C CD2 . TYR   B 1 46  ? 1.202   -39.222 29.065 1.00 85.74  ? 121 TYR   B CD2 1 
ATOM   2572 C CE1 . TYR   B 1 46  ? 3.401   -37.584 28.750 1.00 73.27  ? 121 TYR   B CE1 1 
ATOM   2573 C CE2 . TYR   B 1 46  ? 1.080   -38.026 28.377 1.00 89.15  ? 121 TYR   B CE2 1 
ATOM   2574 C CZ  . TYR   B 1 46  ? 2.184   -37.212 28.223 1.00 79.48  ? 121 TYR   B CZ  1 
ATOM   2575 O OH  . TYR   B 1 46  ? 2.071   -36.022 27.540 1.00 89.31  ? 121 TYR   B OH  1 
ATOM   2576 N N   . GLY   B 1 47  ? 3.191   -38.666 32.657 1.00 65.00  ? 122 GLY   B N   1 
ATOM   2577 C CA  . GLY   B 1 47  ? 4.183   -37.764 33.198 1.00 59.55  ? 122 GLY   B CA  1 
ATOM   2578 C C   . GLY   B 1 47  ? 4.208   -36.436 32.472 1.00 69.84  ? 122 GLY   B C   1 
ATOM   2579 O O   . GLY   B 1 47  ? 3.154   -35.892 32.128 1.00 74.37  ? 122 GLY   B O   1 
ATOM   2580 N N   . GLU   B 1 48  ? 5.402   -35.902 32.227 1.00 56.44  ? 123 GLU   B N   1 
ATOM   2581 C CA  . GLU   B 1 48  ? 5.556   -34.620 31.559 1.00 54.29  ? 123 GLU   B CA  1 
ATOM   2582 C C   . GLU   B 1 48  ? 6.600   -34.739 30.460 1.00 42.62  ? 123 GLU   B C   1 
ATOM   2583 O O   . GLU   B 1 48  ? 7.563   -35.503 30.574 1.00 43.87  ? 123 GLU   B O   1 
ATOM   2584 C CB  . GLU   B 1 48  ? 5.971   -33.505 32.535 1.00 53.39  ? 123 GLU   B CB  1 
ATOM   2585 C CG  . GLU   B 1 48  ? 5.014   -33.264 33.697 1.00 69.75  ? 123 GLU   B CG  1 
ATOM   2586 C CD  . GLU   B 1 48  ? 5.245   -34.212 34.862 1.00 92.22  ? 123 GLU   B CD  1 
ATOM   2587 O OE1 . GLU   B 1 48  ? 6.219   -34.993 34.815 1.00 71.80  ? 123 GLU   B OE1 1 
ATOM   2588 O OE2 . GLU   B 1 48  ? 4.451   -34.172 35.827 1.00 94.35  ? 123 GLU   B OE2 1 
ATOM   2589 N N   . VAL   B 1 49  ? 6.405   -33.968 29.396 1.00 38.77  ? 124 VAL   B N   1 
ATOM   2590 C CA  . VAL   B 1 49  ? 7.347   -33.901 28.287 1.00 36.62  ? 124 VAL   B CA  1 
ATOM   2591 C C   . VAL   B 1 49  ? 7.792   -32.456 28.138 1.00 53.88  ? 124 VAL   B C   1 
ATOM   2592 O O   . VAL   B 1 49  ? 6.964   -31.568 27.891 1.00 53.69  ? 124 VAL   B O   1 
ATOM   2593 C CB  . VAL   B 1 49  ? 6.735   -34.424 26.981 1.00 42.27  ? 124 VAL   B CB  1 
ATOM   2594 C CG1 . VAL   B 1 49  ? 7.741   -34.298 25.851 1.00 43.85  ? 124 VAL   B CG1 1 
ATOM   2595 C CG2 . VAL   B 1 49  ? 6.305   -35.864 27.152 1.00 43.99  ? 124 VAL   B CG2 1 
ATOM   2596 N N   . PHE   B 1 50  ? 9.092   -32.221 28.277 1.00 50.40  ? 125 PHE   B N   1 
ATOM   2597 C CA  . PHE   B 1 50  ? 9.652   -30.882 28.214 1.00 49.22  ? 125 PHE   B CA  1 
ATOM   2598 C C   . PHE   B 1 50  ? 10.507  -30.708 26.966 1.00 49.61  ? 125 PHE   B C   1 
ATOM   2599 O O   . PHE   B 1 50  ? 11.116  -31.661 26.471 1.00 49.33  ? 125 PHE   B O   1 
ATOM   2600 C CB  . PHE   B 1 50  ? 10.505  -30.586 29.449 1.00 64.90  ? 125 PHE   B CB  1 
ATOM   2601 C CG  . PHE   B 1 50  ? 9.767   -30.725 30.743 1.00 49.07  ? 125 PHE   B CG  1 
ATOM   2602 C CD1 . PHE   B 1 50  ? 8.990   -29.687 31.227 1.00 57.76  ? 125 PHE   B CD1 1 
ATOM   2603 C CD2 . PHE   B 1 50  ? 9.858   -31.890 31.483 1.00 56.81  ? 125 PHE   B CD2 1 
ATOM   2604 C CE1 . PHE   B 1 50  ? 8.312   -29.810 32.423 1.00 60.66  ? 125 PHE   B CE1 1 
ATOM   2605 C CE2 . PHE   B 1 50  ? 9.185   -32.019 32.680 1.00 62.79  ? 125 PHE   B CE2 1 
ATOM   2606 C CZ  . PHE   B 1 50  ? 8.410   -30.978 33.150 1.00 53.80  ? 125 PHE   B CZ  1 
ATOM   2607 N N   . LYS   B 1 51  ? 10.546  -29.475 26.467 1.00 55.72  ? 126 LYS   B N   1 
ATOM   2608 C CA  . LYS   B 1 51  ? 11.512  -29.076 25.454 1.00 48.07  ? 126 LYS   B CA  1 
ATOM   2609 C C   . LYS   B 1 51  ? 12.750  -28.538 26.158 1.00 49.73  ? 126 LYS   B C   1 
ATOM   2610 O O   . LYS   B 1 51  ? 12.647  -27.664 27.025 1.00 67.12  ? 126 LYS   B O   1 
ATOM   2611 C CB  . LYS   B 1 51  ? 10.921  -28.016 24.523 1.00 55.78  ? 126 LYS   B CB  1 
ATOM   2612 C CG  . LYS   B 1 51  ? 11.854  -27.567 23.408 1.00 48.46  ? 126 LYS   B CG  1 
ATOM   2613 C CD  . LYS   B 1 51  ? 11.258  -26.408 22.626 1.00 55.79  ? 126 LYS   B CD  1 
ATOM   2614 C CE  . LYS   B 1 51  ? 12.215  -25.919 21.551 1.00 67.02  ? 126 LYS   B CE  1 
ATOM   2615 N NZ  . LYS   B 1 51  ? 11.668  -24.754 20.802 1.00 74.54  ? 126 LYS   B NZ  1 
ATOM   2616 N N   . VAL   B 1 52  ? 13.917  -29.078 25.806 1.00 55.50  ? 127 VAL   B N   1 
ATOM   2617 C CA  . VAL   B 1 52  ? 15.153  -28.757 26.506 1.00 50.00  ? 127 VAL   B CA  1 
ATOM   2618 C C   . VAL   B 1 52  ? 16.282  -28.560 25.506 1.00 56.38  ? 127 VAL   B C   1 
ATOM   2619 O O   . VAL   B 1 52  ? 16.180  -28.927 24.333 1.00 59.64  ? 127 VAL   B O   1 
ATOM   2620 C CB  . VAL   B 1 52  ? 15.548  -29.858 27.521 1.00 56.58  ? 127 VAL   B CB  1 
ATOM   2621 C CG1 . VAL   B 1 52  ? 14.471  -30.035 28.579 1.00 53.20  ? 127 VAL   B CG1 1 
ATOM   2622 C CG2 . VAL   B 1 52  ? 15.806  -31.166 26.799 1.00 43.15  ? 127 VAL   B CG2 1 
ATOM   2623 N N   A ARG   B 1 53  ? 17.378  -27.981 25.997 0.34 65.77  ? 128 ARG   B N   1 
ATOM   2624 N N   B ARG   B 1 53  ? 17.361  -27.944 25.981 0.66 65.84  ? 128 ARG   B N   1 
ATOM   2625 C CA  A ARG   B 1 53  ? 18.632  -27.878 25.258 0.34 65.61  ? 128 ARG   B CA  1 
ATOM   2626 C CA  B ARG   B 1 53  ? 18.620  -27.896 25.251 0.66 65.59  ? 128 ARG   B CA  1 
ATOM   2627 C C   A ARG   B 1 53  ? 19.729  -28.532 26.085 0.34 67.29  ? 128 ARG   B C   1 
ATOM   2628 C C   B ARG   B 1 53  ? 19.690  -28.567 26.096 0.66 67.27  ? 128 ARG   B C   1 
ATOM   2629 O O   A ARG   B 1 53  ? 19.970  -28.133 27.229 0.34 66.67  ? 128 ARG   B O   1 
ATOM   2630 O O   B ARG   B 1 53  ? 19.866  -28.220 27.268 0.66 66.39  ? 128 ARG   B O   1 
ATOM   2631 C CB  A ARG   B 1 53  ? 18.985  -26.420 24.948 0.34 67.62  ? 128 ARG   B CB  1 
ATOM   2632 C CB  B ARG   B 1 53  ? 19.034  -26.463 24.914 0.66 67.63  ? 128 ARG   B CB  1 
ATOM   2633 C CG  A ARG   B 1 53  ? 20.248  -26.254 24.108 0.34 68.78  ? 128 ARG   B CG  1 
ATOM   2634 C CG  B ARG   B 1 53  ? 20.174  -26.391 23.903 0.66 69.23  ? 128 ARG   B CG  1 
ATOM   2635 C CD  A ARG   B 1 53  ? 20.466  -24.806 23.689 0.34 63.69  ? 128 ARG   B CD  1 
ATOM   2636 C CD  B ARG   B 1 53  ? 20.604  -24.962 23.579 0.66 63.47  ? 128 ARG   B CD  1 
ATOM   2637 N NE  A ARG   B 1 53  ? 19.411  -24.324 22.805 0.34 69.64  ? 128 ARG   B NE  1 
ATOM   2638 N NE  B ARG   B 1 53  ? 19.623  -24.228 22.785 0.66 70.01  ? 128 ARG   B NE  1 
ATOM   2639 C CZ  A ARG   B 1 53  ? 19.415  -24.464 21.486 0.34 65.85  ? 128 ARG   B CZ  1 
ATOM   2640 C CZ  B ARG   B 1 53  ? 18.880  -23.230 23.247 0.66 71.23  ? 128 ARG   B CZ  1 
ATOM   2641 N NH1 A ARG   B 1 53  ? 20.396  -25.094 20.861 0.34 69.13  ? 128 ARG   B NH1 1 
ATOM   2642 N NH1 B ARG   B 1 53  ? 18.984  -22.811 24.498 0.66 68.01  ? 128 ARG   B NH1 1 
ATOM   2643 N NH2 A ARG   B 1 53  ? 18.410  -23.960 20.776 0.34 64.80  ? 128 ARG   B NH2 1 
ATOM   2644 N NH2 B ARG   B 1 53  ? 18.012  -22.636 22.432 0.66 67.99  ? 128 ARG   B NH2 1 
ATOM   2645 N N   . SER   B 1 54  ? 20.386  -29.536 25.512 1.00 71.20  ? 129 SER   B N   1 
ATOM   2646 C CA  . SER   B 1 54  ? 21.387  -30.296 26.248 1.00 57.67  ? 129 SER   B CA  1 
ATOM   2647 C C   . SER   B 1 54  ? 22.668  -29.488 26.410 1.00 70.85  ? 129 SER   B C   1 
ATOM   2648 O O   . SER   B 1 54  ? 23.241  -29.010 25.427 1.00 82.05  ? 129 SER   B O   1 
ATOM   2649 C CB  . SER   B 1 54  ? 21.678  -31.613 25.533 1.00 70.14  ? 129 SER   B CB  1 
ATOM   2650 O OG  . SER   B 1 54  ? 22.762  -32.296 26.135 1.00 80.02  ? 129 SER   B OG  1 
ATOM   2651 N N   . LYS   B 1 55  ? 23.121  -29.340 27.657 1.00 77.27  ? 130 LYS   B N   1 
ATOM   2652 C CA  . LYS   B 1 55  ? 24.387  -28.665 27.907 1.00 83.42  ? 130 LYS   B CA  1 
ATOM   2653 C C   . LYS   B 1 55  ? 25.581  -29.487 27.436 1.00 64.05  ? 130 LYS   B C   1 
ATOM   2654 O O   . LYS   B 1 55  ? 26.673  -28.935 27.276 1.00 87.17  ? 130 LYS   B O   1 
ATOM   2655 C CB  . LYS   B 1 55  ? 24.517  -28.342 29.395 1.00 60.16  ? 130 LYS   B CB  1 
ATOM   2656 C CG  . LYS   B 1 55  ? 23.340  -27.553 29.940 1.00 59.91  ? 130 LYS   B CG  1 
ATOM   2657 C CD  . LYS   B 1 55  ? 23.473  -27.318 31.430 1.00 61.21  ? 130 LYS   B CD  1 
ATOM   2658 C CE  . LYS   B 1 55  ? 22.262  -26.584 31.979 1.00 61.43  ? 130 LYS   B CE  1 
ATOM   2659 N NZ  . LYS   B 1 55  ? 22.359  -26.359 33.449 1.00 63.09  ? 130 LYS   B NZ  1 
ATOM   2660 N N   . GLU   B 1 56  ? 25.397  -30.787 27.197 1.00 79.27  ? 131 GLU   B N   1 
ATOM   2661 C CA  . GLU   B 1 56  ? 26.498  -31.612 26.710 1.00 80.77  ? 131 GLU   B CA  1 
ATOM   2662 C C   . GLU   B 1 56  ? 26.875  -31.248 25.277 1.00 78.55  ? 131 GLU   B C   1 
ATOM   2663 O O   . GLU   B 1 56  ? 28.058  -31.274 24.917 1.00 90.86  ? 131 GLU   B O   1 
ATOM   2664 C CB  . GLU   B 1 56  ? 26.127  -33.094 26.811 1.00 87.50  ? 131 GLU   B CB  1 
ATOM   2665 C CG  . GLU   B 1 56  ? 27.225  -34.050 26.361 1.00 83.36  ? 131 GLU   B CG  1 
ATOM   2666 C CD  . GLU   B 1 56  ? 28.403  -34.087 27.318 1.00 108.18 ? 131 GLU   B CD  1 
ATOM   2667 O OE1 . GLU   B 1 56  ? 28.175  -34.216 28.538 1.00 119.01 ? 131 GLU   B OE1 1 
ATOM   2668 O OE2 . GLU   B 1 56  ? 29.558  -33.982 26.851 1.00 115.92 ? 131 GLU   B OE2 1 
ATOM   2669 N N   . ASP   B 1 57  ? 25.888  -30.902 24.443 1.00 72.88  ? 132 ASP   B N   1 
ATOM   2670 C CA  . ASP   B 1 57  ? 26.162  -30.584 23.048 1.00 74.82  ? 132 ASP   B CA  1 
ATOM   2671 C C   . ASP   B 1 57  ? 25.426  -29.355 22.525 1.00 76.81  ? 132 ASP   B C   1 
ATOM   2672 O O   . ASP   B 1 57  ? 25.596  -29.018 21.348 1.00 80.87  ? 132 ASP   B O   1 
ATOM   2673 C CB  . ASP   B 1 57  ? 25.842  -31.797 22.149 1.00 70.89  ? 132 ASP   B CB  1 
ATOM   2674 C CG  . ASP   B 1 57  ? 24.440  -32.340 22.364 1.00 83.00  ? 132 ASP   B CG  1 
ATOM   2675 O OD1 . ASP   B 1 57  ? 23.611  -31.640 22.980 1.00 87.03  ? 132 ASP   B OD1 1 
ATOM   2676 O OD2 . ASP   B 1 57  ? 24.167  -33.477 21.918 1.00 87.37  ? 132 ASP   B OD2 1 
ATOM   2677 N N   . GLY   B 1 58  ? 24.627  -28.674 23.345 1.00 70.21  ? 133 GLY   B N   1 
ATOM   2678 C CA  . GLY   B 1 58  ? 23.961  -27.462 22.905 1.00 68.69  ? 133 GLY   B CA  1 
ATOM   2679 C C   . GLY   B 1 58  ? 22.802  -27.659 21.956 1.00 77.53  ? 133 GLY   B C   1 
ATOM   2680 O O   . GLY   B 1 58  ? 22.298  -26.673 21.410 1.00 93.15  ? 133 GLY   B O   1 
ATOM   2681 N N   . ARG   B 1 59  ? 22.353  -28.892 21.743 1.00 56.92  ? 134 ARG   B N   1 
ATOM   2682 C CA  . ARG   B 1 59  ? 21.296  -29.179 20.785 1.00 57.01  ? 134 ARG   B CA  1 
ATOM   2683 C C   . ARG   B 1 59  ? 19.944  -29.303 21.484 1.00 60.78  ? 134 ARG   B C   1 
ATOM   2684 O O   . ARG   B 1 59  ? 19.853  -29.430 22.707 1.00 55.64  ? 134 ARG   B O   1 
ATOM   2685 C CB  . ARG   B 1 59  ? 21.611  -30.460 20.011 1.00 68.97  ? 134 ARG   B CB  1 
ATOM   2686 C CG  . ARG   B 1 59  ? 22.883  -30.399 19.185 1.00 63.62  ? 134 ARG   B CG  1 
ATOM   2687 C CD  . ARG   B 1 59  ? 23.043  -31.672 18.376 1.00 76.80  ? 134 ARG   B CD  1 
ATOM   2688 N NE  . ARG   B 1 59  ? 23.484  -31.402 17.014 1.00 93.74  ? 134 ARG   B NE  1 
ATOM   2689 C CZ  . ARG   B 1 59  ? 23.328  -32.241 15.999 1.00 107.45 ? 134 ARG   B CZ  1 
ATOM   2690 N NH1 . ARG   B 1 59  ? 22.734  -33.414 16.155 1.00 90.44  ? 134 ARG   B NH1 1 
ATOM   2691 N NH2 . ARG   B 1 59  ? 23.770  -31.892 14.794 1.00 96.94  ? 134 ARG   B NH2 1 
ATOM   2692 N N   . LEU   B 1 60  ? 18.881  -29.278 20.681 1.00 66.17  ? 135 LEU   B N   1 
ATOM   2693 C CA  . LEU   B 1 60  ? 17.516  -29.314 21.193 1.00 52.51  ? 135 LEU   B CA  1 
ATOM   2694 C C   . LEU   B 1 60  ? 17.020  -30.750 21.299 1.00 55.41  ? 135 LEU   B C   1 
ATOM   2695 O O   . LEU   B 1 60  ? 17.193  -31.547 20.370 1.00 59.84  ? 135 LEU   B O   1 
ATOM   2696 C CB  . LEU   B 1 60  ? 16.579  -28.506 20.294 1.00 63.46  ? 135 LEU   B CB  1 
ATOM   2697 C CG  . LEU   B 1 60  ? 16.726  -26.991 20.400 1.00 53.75  ? 135 LEU   B CG  1 
ATOM   2698 C CD1 . LEU   B 1 60  ? 15.651  -26.275 19.595 1.00 55.27  ? 135 LEU   B CD1 1 
ATOM   2699 C CD2 . LEU   B 1 60  ? 16.669  -26.590 21.858 1.00 57.15  ? 135 LEU   B CD2 1 
ATOM   2700 N N   . TYR   B 1 61  ? 16.392  -31.070 22.427 1.00 51.84  ? 136 TYR   B N   1 
ATOM   2701 C CA  . TYR   B 1 61  ? 15.861  -32.402 22.659 1.00 43.79  ? 136 TYR   B CA  1 
ATOM   2702 C C   . TYR   B 1 61  ? 14.523  -32.295 23.370 1.00 44.69  ? 136 TYR   B C   1 
ATOM   2703 O O   . TYR   B 1 61  ? 14.157  -31.243 23.902 1.00 51.51  ? 136 TYR   B O   1 
ATOM   2704 C CB  . TYR   B 1 61  ? 16.814  -33.260 23.500 1.00 49.64  ? 136 TYR   B CB  1 
ATOM   2705 C CG  . TYR   B 1 61  ? 18.149  -33.539 22.851 1.00 45.59  ? 136 TYR   B CG  1 
ATOM   2706 C CD1 . TYR   B 1 61  ? 18.295  -34.574 21.937 1.00 55.41  ? 136 TYR   B CD1 1 
ATOM   2707 C CD2 . TYR   B 1 61  ? 19.265  -32.779 23.163 1.00 49.19  ? 136 TYR   B CD2 1 
ATOM   2708 C CE1 . TYR   B 1 61  ? 19.519  -34.837 21.344 1.00 72.97  ? 136 TYR   B CE1 1 
ATOM   2709 C CE2 . TYR   B 1 61  ? 20.492  -33.034 22.577 1.00 53.69  ? 136 TYR   B CE2 1 
ATOM   2710 C CZ  . TYR   B 1 61  ? 20.614  -34.063 21.669 1.00 62.06  ? 136 TYR   B CZ  1 
ATOM   2711 O OH  . TYR   B 1 61  ? 21.837  -34.316 21.086 1.00 69.03  ? 136 TYR   B OH  1 
ATOM   2712 N N   . ALA   B 1 62  ? 13.795  -33.405 23.368 1.00 49.75  ? 137 ALA   B N   1 
ATOM   2713 C CA  . ALA   B 1 62  ? 12.600  -33.575 24.179 1.00 40.72  ? 137 ALA   B CA  1 
ATOM   2714 C C   . ALA   B 1 62  ? 12.884  -34.633 25.234 1.00 35.95  ? 137 ALA   B C   1 
ATOM   2715 O O   . ALA   B 1 62  ? 13.512  -35.656 24.944 1.00 55.06  ? 137 ALA   B O   1 
ATOM   2716 C CB  . ALA   B 1 62  ? 11.399  -33.992 23.330 1.00 32.49  ? 137 ALA   B CB  1 
ATOM   2717 N N   . VAL   B 1 63  ? 12.435  -34.382 26.460 1.00 38.00  ? 138 VAL   B N   1 
ATOM   2718 C CA  . VAL   B 1 63  ? 12.680  -35.289 27.573 1.00 36.21  ? 138 VAL   B CA  1 
ATOM   2719 C C   . VAL   B 1 63  ? 11.350  -35.597 28.241 1.00 36.33  ? 138 VAL   B C   1 
ATOM   2720 O O   . VAL   B 1 63  ? 10.622  -34.675 28.629 1.00 45.40  ? 138 VAL   B O   1 
ATOM   2721 C CB  . VAL   B 1 63  ? 13.670  -34.697 28.586 1.00 44.84  ? 138 VAL   B CB  1 
ATOM   2722 C CG1 . VAL   B 1 63  ? 13.770  -35.598 29.802 1.00 45.64  ? 138 VAL   B CG1 1 
ATOM   2723 C CG2 . VAL   B 1 63  ? 15.024  -34.516 27.936 1.00 35.08  ? 138 VAL   B CG2 1 
ATOM   2724 N N   . LYS   B 1 64  ? 11.032  -36.885 28.365 1.00 39.63  ? 139 LYS   B N   1 
ATOM   2725 C CA  . LYS   B 1 64  ? 9.821   -37.331 29.042 1.00 40.59  ? 139 LYS   B CA  1 
ATOM   2726 C C   . LYS   B 1 64  ? 10.173  -37.863 30.420 1.00 36.32  ? 139 LYS   B C   1 
ATOM   2727 O O   . LYS   B 1 64  ? 11.126  -38.633 30.573 1.00 38.41  ? 139 LYS   B O   1 
ATOM   2728 C CB  . LYS   B 1 64  ? 9.094   -38.420 28.250 1.00 35.12  ? 139 LYS   B CB  1 
ATOM   2729 C CG  . LYS   B 1 64  ? 7.737   -38.802 28.848 1.00 42.32  ? 139 LYS   B CG  1 
ATOM   2730 C CD  . LYS   B 1 64  ? 6.935   -39.697 27.913 1.00 49.11  ? 139 LYS   B CD  1 
ATOM   2731 C CE  . LYS   B 1 64  ? 7.631   -41.028 27.682 1.00 45.91  ? 139 LYS   B CE  1 
ATOM   2732 N NZ  . LYS   B 1 64  ? 6.956   -41.820 26.617 1.00 68.14  ? 139 LYS   B NZ  1 
ATOM   2733 N N   . ARG   B 1 65  ? 9.383   -37.467 31.416 1.00 44.88  ? 140 ARG   B N   1 
ATOM   2734 C CA  . ARG   B 1 65  ? 9.623   -37.826 32.807 1.00 48.10  ? 140 ARG   B CA  1 
ATOM   2735 C C   . ARG   B 1 65  ? 8.377   -38.482 33.381 1.00 50.59  ? 140 ARG   B C   1 
ATOM   2736 O O   . ARG   B 1 65  ? 7.284   -37.913 33.302 1.00 50.11  ? 140 ARG   B O   1 
ATOM   2737 C CB  . ARG   B 1 65  ? 10.002  -36.585 33.627 1.00 49.30  ? 140 ARG   B CB  1 
ATOM   2738 C CG  . ARG   B 1 65  ? 9.819   -36.745 35.124 1.00 66.42  ? 140 ARG   B CG  1 
ATOM   2739 C CD  . ARG   B 1 65  ? 10.422  -35.583 35.885 1.00 54.17  ? 140 ARG   B CD  1 
ATOM   2740 N NE  . ARG   B 1 65  ? 9.643   -34.361 35.733 1.00 61.83  ? 140 ARG   B NE  1 
ATOM   2741 C CZ  . ARG   B 1 65  ? 10.014  -33.180 36.206 1.00 56.76  ? 140 ARG   B CZ  1 
ATOM   2742 N NH1 . ARG   B 1 65  ? 11.168  -33.019 36.834 1.00 66.07  ? 140 ARG   B NH1 1 
ATOM   2743 N NH2 . ARG   B 1 65  ? 9.208   -32.134 36.046 1.00 54.15  ? 140 ARG   B NH2 1 
ATOM   2744 N N   . SER   B 1 66  ? 8.537   -39.677 33.949 1.00 46.09  ? 141 SER   B N   1 
ATOM   2745 C CA  . SER   B 1 66  ? 7.409   -40.345 34.584 1.00 44.35  ? 141 SER   B CA  1 
ATOM   2746 C C   . SER   B 1 66  ? 6.934   -39.544 35.791 1.00 54.41  ? 141 SER   B C   1 
ATOM   2747 O O   . SER   B 1 66  ? 7.715   -38.858 36.457 1.00 64.41  ? 141 SER   B O   1 
ATOM   2748 C CB  . SER   B 1 66  ? 7.792   -41.765 35.002 1.00 44.72  ? 141 SER   B CB  1 
ATOM   2749 O OG  . SER   B 1 66  ? 8.950   -41.761 35.818 1.00 59.27  ? 141 SER   B OG  1 
ATOM   2750 N N   . MET   B 1 67  ? 5.633   -39.631 36.070 1.00 59.07  ? 142 MET   B N   1 
ATOM   2751 C CA  . MET   B 1 67  ? 5.025   -38.793 37.097 1.00 59.27  ? 142 MET   B CA  1 
ATOM   2752 C C   . MET   B 1 67  ? 5.495   -39.186 38.492 1.00 66.80  ? 142 MET   B C   1 
ATOM   2753 O O   . MET   B 1 67  ? 6.194   -38.415 39.157 1.00 71.55  ? 142 MET   B O   1 
ATOM   2754 C CB  . MET   B 1 67  ? 3.499   -38.866 37.025 1.00 72.07  ? 142 MET   B CB  1 
ATOM   2755 C CG  . MET   B 1 67  ? 2.803   -37.993 38.058 1.00 89.19  ? 142 MET   B CG  1 
ATOM   2756 S SD  . MET   B 1 67  ? 1.019   -38.247 38.124 1.00 129.71 ? 142 MET   B SD  1 
ATOM   2757 C CE  . MET   B 1 67  ? 0.552   -37.043 39.367 1.00 97.44  ? 142 MET   B CE  1 
ATOM   2758 N N   . SER   B 1 68  ? 5.112   -40.373 38.942 1.00 62.03  ? 143 SER   B N   1 
ATOM   2759 C CA  . SER   B 1 68  ? 5.404   -40.852 40.282 1.00 55.80  ? 143 SER   B CA  1 
ATOM   2760 C C   . SER   B 1 68  ? 6.490   -41.919 40.254 1.00 41.15  ? 143 SER   B C   1 
ATOM   2761 O O   . SER   B 1 68  ? 6.703   -42.578 39.230 1.00 60.63  ? 143 SER   B O   1 
ATOM   2762 C CB  . SER   B 1 68  ? 4.138   -41.426 40.932 1.00 70.27  ? 143 SER   B CB  1 
ATOM   2763 O OG  . SER   B 1 68  ? 3.636   -42.512 40.174 1.00 96.29  ? 143 SER   B OG  1 
ATOM   2764 N N   . PRO   B 1 69  ? 7.207   -42.111 41.362 1.00 52.23  ? 144 PRO   B N   1 
ATOM   2765 C CA  . PRO   B 1 69  ? 8.242   -43.151 41.407 1.00 43.42  ? 144 PRO   B CA  1 
ATOM   2766 C C   . PRO   B 1 69  ? 7.657   -44.536 41.177 1.00 56.09  ? 144 PRO   B C   1 
ATOM   2767 O O   . PRO   B 1 69  ? 6.444   -44.755 41.209 1.00 70.77  ? 144 PRO   B O   1 
ATOM   2768 C CB  . PRO   B 1 69  ? 8.826   -43.015 42.817 1.00 47.99  ? 144 PRO   B CB  1 
ATOM   2769 C CG  . PRO   B 1 69  ? 8.540   -41.600 43.205 1.00 49.48  ? 144 PRO   B CG  1 
ATOM   2770 C CD  . PRO   B 1 69  ? 7.217   -41.272 42.573 1.00 44.99  ? 144 PRO   B CD  1 
ATOM   2771 N N   . PHE   B 1 70  ? 8.558   -45.485 40.938 1.00 60.56  ? 145 PHE   B N   1 
ATOM   2772 C CA  . PHE   B 1 70  ? 8.152   -46.854 40.654 1.00 40.36  ? 145 PHE   B CA  1 
ATOM   2773 C C   . PHE   B 1 70  ? 7.396   -47.445 41.835 1.00 54.44  ? 145 PHE   B C   1 
ATOM   2774 O O   . PHE   B 1 70  ? 7.880   -47.427 42.969 1.00 58.04  ? 145 PHE   B O   1 
ATOM   2775 C CB  . PHE   B 1 70  ? 9.378   -47.706 40.341 1.00 39.28  ? 145 PHE   B CB  1 
ATOM   2776 C CG  . PHE   B 1 70  ? 10.155  -47.234 39.150 1.00 43.60  ? 145 PHE   B CG  1 
ATOM   2777 C CD1 . PHE   B 1 70  ? 9.504   -46.760 38.024 1.00 37.32  ? 145 PHE   B CD1 1 
ATOM   2778 C CD2 . PHE   B 1 70  ? 11.540  -47.264 39.158 1.00 51.06  ? 145 PHE   B CD2 1 
ATOM   2779 C CE1 . PHE   B 1 70  ? 10.221  -46.329 36.921 1.00 39.34  ? 145 PHE   B CE1 1 
ATOM   2780 C CE2 . PHE   B 1 70  ? 12.266  -46.834 38.062 1.00 42.56  ? 145 PHE   B CE2 1 
ATOM   2781 C CZ  . PHE   B 1 70  ? 11.606  -46.365 36.941 1.00 41.26  ? 145 PHE   B CZ  1 
ATOM   2782 N N   . ARG   B 1 71  ? 6.199   -47.967 41.563 1.00 53.40  ? 146 ARG   B N   1 
ATOM   2783 C CA  . ARG   B 1 71  ? 5.422   -48.609 42.618 1.00 53.51  ? 146 ARG   B CA  1 
ATOM   2784 C C   . ARG   B 1 71  ? 5.996   -49.971 42.985 1.00 56.13  ? 146 ARG   B C   1 
ATOM   2785 O O   . ARG   B 1 71  ? 5.847   -50.418 44.127 1.00 63.93  ? 146 ARG   B O   1 
ATOM   2786 C CB  . ARG   B 1 71  ? 3.960   -48.747 42.186 1.00 70.71  ? 146 ARG   B CB  1 
ATOM   2787 C CG  . ARG   B 1 71  ? 3.254   -47.421 41.927 1.00 74.95  ? 146 ARG   B CG  1 
ATOM   2788 C CD  . ARG   B 1 71  ? 1.864   -47.633 41.343 1.00 64.58  ? 146 ARG   B CD  1 
ATOM   2789 N NE  . ARG   B 1 71  ? 1.226   -46.372 40.980 1.00 99.94  ? 146 ARG   B NE  1 
ATOM   2790 C CZ  . ARG   B 1 71  ? 1.453   -45.715 39.850 1.00 102.85 ? 146 ARG   B CZ  1 
ATOM   2791 N NH1 . ARG   B 1 71  ? 2.318   -46.159 38.952 1.00 90.58  ? 146 ARG   B NH1 1 
ATOM   2792 N NH2 . ARG   B 1 71  ? 0.796   -44.582 39.615 1.00 90.86  ? 146 ARG   B NH2 1 
ATOM   2793 N N   . GLY   B 1 72  ? 6.652   -50.640 42.043 1.00 52.60  ? 147 GLY   B N   1 
ATOM   2794 C CA  . GLY   B 1 72  ? 7.212   -51.945 42.294 1.00 40.10  ? 147 GLY   B CA  1 
ATOM   2795 C C   . GLY   B 1 72  ? 8.040   -52.444 41.129 1.00 42.78  ? 147 GLY   B C   1 
ATOM   2796 O O   . GLY   B 1 72  ? 8.272   -51.729 40.148 1.00 48.43  ? 147 GLY   B O   1 
ATOM   2797 N N   . PRO   B 1 73  ? 8.513   -53.690 41.225 1.00 39.60  ? 148 PRO   B N   1 
ATOM   2798 C CA  . PRO   B 1 73  ? 9.284   -54.268 40.106 1.00 28.53  ? 148 PRO   B CA  1 
ATOM   2799 C C   . PRO   B 1 73  ? 8.510   -54.346 38.806 1.00 37.86  ? 148 PRO   B C   1 
ATOM   2800 O O   . PRO   B 1 73  ? 9.040   -53.977 37.750 1.00 45.90  ? 148 PRO   B O   1 
ATOM   2801 C CB  . PRO   B 1 73  ? 9.646   -55.663 40.628 1.00 41.93  ? 148 PRO   B CB  1 
ATOM   2802 C CG  . PRO   B 1 73  ? 9.599   -55.538 42.102 1.00 48.41  ? 148 PRO   B CG  1 
ATOM   2803 C CD  . PRO   B 1 73  ? 8.493   -54.577 42.398 1.00 35.27  ? 148 PRO   B CD  1 
ATOM   2804 N N   . LYS   B 1 74  ? 7.272   -54.846 38.849 1.00 47.94  ? 149 LYS   B N   1 
ATOM   2805 C CA  . LYS   B 1 74  ? 6.454   -54.897 37.644 1.00 36.11  ? 149 LYS   B CA  1 
ATOM   2806 C C   . LYS   B 1 74  ? 6.218   -53.497 37.090 1.00 41.24  ? 149 LYS   B C   1 
ATOM   2807 O O   . LYS   B 1 74  ? 6.302   -53.279 35.875 1.00 53.18  ? 149 LYS   B O   1 
ATOM   2808 C CB  . LYS   B 1 74  ? 5.132   -55.600 37.952 1.00 43.78  ? 149 LYS   B CB  1 
ATOM   2809 C CG  . LYS   B 1 74  ? 4.152   -55.665 36.796 1.00 90.52  ? 149 LYS   B CG  1 
ATOM   2810 C CD  . LYS   B 1 74  ? 4.662   -56.561 35.678 1.00 106.61 ? 149 LYS   B CD  1 
ATOM   2811 C CE  . LYS   B 1 74  ? 3.551   -56.901 34.696 1.00 110.00 ? 149 LYS   B CE  1 
ATOM   2812 N NZ  . LYS   B 1 74  ? 4.044   -57.522 33.435 1.00 89.18  ? 149 LYS   B NZ  1 
ATOM   2813 N N   . ASP   B 1 75  ? 5.933   -52.531 37.968 1.00 46.28  ? 150 ASP   B N   1 
ATOM   2814 C CA  . ASP   B 1 75  ? 5.750   -51.152 37.521 1.00 39.12  ? 150 ASP   B CA  1 
ATOM   2815 C C   . ASP   B 1 75  ? 7.023   -50.614 36.882 1.00 42.23  ? 150 ASP   B C   1 
ATOM   2816 O O   . ASP   B 1 75  ? 6.973   -49.921 35.859 1.00 48.95  ? 150 ASP   B O   1 
ATOM   2817 C CB  . ASP   B 1 75  ? 5.328   -50.272 38.699 1.00 43.89  ? 150 ASP   B CB  1 
ATOM   2818 C CG  . ASP   B 1 75  ? 5.056   -48.836 38.291 1.00 50.04  ? 150 ASP   B CG  1 
ATOM   2819 O OD1 . ASP   B 1 75  ? 4.778   -48.592 37.097 1.00 76.00  ? 150 ASP   B OD1 1 
ATOM   2820 O OD2 . ASP   B 1 75  ? 5.121   -47.946 39.167 1.00 61.70  ? 150 ASP   B OD2 1 
ATOM   2821 N N   . ARG   B 1 76  ? 8.177   -50.930 37.470 1.00 35.46  ? 151 ARG   B N   1 
ATOM   2822 C CA  . ARG   B 1 76  ? 9.442   -50.493 36.893 1.00 35.67  ? 151 ARG   B CA  1 
ATOM   2823 C C   . ARG   B 1 76  ? 9.709   -51.187 35.565 1.00 40.31  ? 151 ARG   B C   1 
ATOM   2824 O O   . ARG   B 1 76  ? 10.128  -50.544 34.594 1.00 43.80  ? 151 ARG   B O   1 
ATOM   2825 C CB  . ARG   B 1 76  ? 10.583  -50.755 37.874 1.00 41.73  ? 151 ARG   B CB  1 
ATOM   2826 C CG  . ARG   B 1 76  ? 11.946  -50.372 37.334 1.00 38.30  ? 151 ARG   B CG  1 
ATOM   2827 C CD  . ARG   B 1 76  ? 13.025  -50.585 38.374 1.00 39.55  ? 151 ARG   B CD  1 
ATOM   2828 N NE  . ARG   B 1 76  ? 14.354  -50.364 37.817 1.00 51.08  ? 151 ARG   B NE  1 
ATOM   2829 C CZ  . ARG   B 1 76  ? 15.068  -51.293 37.199 1.00 50.97  ? 151 ARG   B CZ  1 
ATOM   2830 N NH1 . ARG   B 1 76  ? 14.612  -52.526 37.044 1.00 68.80  ? 151 ARG   B NH1 1 
ATOM   2831 N NH2 . ARG   B 1 76  ? 16.268  -50.977 36.720 1.00 60.32  ? 151 ARG   B NH2 1 
ATOM   2832 N N   . ALA   B 1 77  ? 9.480   -52.501 35.502 1.00 40.95  ? 152 ALA   B N   1 
ATOM   2833 C CA  . ALA   B 1 77  ? 9.726   -53.228 34.262 1.00 26.78  ? 152 ALA   B CA  1 
ATOM   2834 C C   . ALA   B 1 77  ? 8.789   -52.773 33.156 1.00 39.23  ? 152 ALA   B C   1 
ATOM   2835 O O   . ALA   B 1 77  ? 9.162   -52.790 31.976 1.00 46.45  ? 152 ALA   B O   1 
ATOM   2836 C CB  . ALA   B 1 77  ? 9.582   -54.731 34.488 1.00 36.32  ? 152 ALA   B CB  1 
ATOM   2837 N N   . ARG   B 1 78  ? 7.573   -52.360 33.515 1.00 49.11  ? 153 ARG   B N   1 
ATOM   2838 C CA  . ARG   B 1 78  ? 6.625   -51.902 32.506 1.00 37.55  ? 153 ARG   B CA  1 
ATOM   2839 C C   . ARG   B 1 78  ? 7.052   -50.560 31.920 1.00 49.54  ? 153 ARG   B C   1 
ATOM   2840 O O   . ARG   B 1 78  ? 7.037   -50.372 30.698 1.00 52.46  ? 153 ARG   B O   1 
ATOM   2841 C CB  . ARG   B 1 78  ? 5.220   -51.818 33.108 1.00 52.73  ? 153 ARG   B CB  1 
ATOM   2842 C CG  . ARG   B 1 78  ? 4.162   -51.309 32.140 1.00 68.76  ? 153 ARG   B CG  1 
ATOM   2843 C CD  . ARG   B 1 78  ? 2.774   -51.284 32.772 1.00 78.35  ? 153 ARG   B CD  1 
ATOM   2844 N NE  . ARG   B 1 78  ? 2.220   -52.621 32.957 1.00 69.06  ? 153 ARG   B NE  1 
ATOM   2845 C CZ  . ARG   B 1 78  ? 2.117   -53.235 34.128 1.00 54.75  ? 153 ARG   B CZ  1 
ATOM   2846 N NH1 . ARG   B 1 78  ? 2.529   -52.663 35.248 1.00 47.20  ? 153 ARG   B NH1 1 
ATOM   2847 N NH2 . ARG   B 1 78  ? 1.576   -54.449 34.178 1.00 80.24  ? 153 ARG   B NH2 1 
ATOM   2848 N N   . LYS   B 1 79  ? 7.446   -49.612 32.774 1.00 40.82  ? 154 LYS   B N   1 
ATOM   2849 C CA  . LYS   B 1 79  ? 7.906   -48.321 32.269 1.00 46.83  ? 154 LYS   B CA  1 
ATOM   2850 C C   . LYS   B 1 79  ? 9.209   -48.463 31.488 1.00 41.48  ? 154 LYS   B C   1 
ATOM   2851 O O   . LYS   B 1 79  ? 9.391   -47.812 30.453 1.00 45.29  ? 154 LYS   B O   1 
ATOM   2852 C CB  . LYS   B 1 79  ? 8.084   -47.332 33.419 1.00 41.46  ? 154 LYS   B CB  1 
ATOM   2853 C CG  . LYS   B 1 79  ? 6.818   -46.998 34.207 1.00 40.02  ? 154 LYS   B CG  1 
ATOM   2854 C CD  . LYS   B 1 79  ? 7.061   -45.782 35.093 1.00 52.18  ? 154 LYS   B CD  1 
ATOM   2855 C CE  . LYS   B 1 79  ? 6.208   -45.788 36.352 1.00 57.62  ? 154 LYS   B CE  1 
ATOM   2856 N NZ  . LYS   B 1 79  ? 4.762   -45.594 36.066 1.00 72.53  ? 154 LYS   B NZ  1 
ATOM   2857 N N   . LEU   B 1 80  ? 10.129  -49.308 31.962 1.00 41.64  ? 155 LEU   B N   1 
ATOM   2858 C CA  . LEU   B 1 80  ? 11.395  -49.494 31.261 1.00 36.39  ? 155 LEU   B CA  1 
ATOM   2859 C C   . LEU   B 1 80  ? 11.228  -50.194 29.920 1.00 44.46  ? 155 LEU   B C   1 
ATOM   2860 O O   . LEU   B 1 80  ? 12.122  -50.098 29.073 1.00 46.63  ? 155 LEU   B O   1 
ATOM   2861 C CB  . LEU   B 1 80  ? 12.372  -50.295 32.120 1.00 32.46  ? 155 LEU   B CB  1 
ATOM   2862 C CG  . LEU   B 1 80  ? 13.021  -49.585 33.306 1.00 39.09  ? 155 LEU   B CG  1 
ATOM   2863 C CD1 . LEU   B 1 80  ? 13.967  -50.528 34.019 1.00 46.97  ? 155 LEU   B CD1 1 
ATOM   2864 C CD2 . LEU   B 1 80  ? 13.762  -48.352 32.842 1.00 47.58  ? 155 LEU   B CD2 1 
ATOM   2865 N N   . ALA   B 1 81  ? 10.114  -50.901 29.709 1.00 40.53  ? 156 ALA   B N   1 
ATOM   2866 C CA  . ALA   B 1 81  ? 9.932   -51.624 28.455 1.00 31.90  ? 156 ALA   B CA  1 
ATOM   2867 C C   . ALA   B 1 81  ? 9.901   -50.680 27.261 1.00 41.38  ? 156 ALA   B C   1 
ATOM   2868 O O   . ALA   B 1 81  ? 10.221  -51.090 26.139 1.00 49.74  ? 156 ALA   B O   1 
ATOM   2869 C CB  . ALA   B 1 81  ? 8.650   -52.457 28.507 1.00 34.80  ? 156 ALA   B CB  1 
ATOM   2870 N N   . GLU   B 1 82  ? 9.522   -49.416 27.477 1.00 39.67  ? 157 GLU   B N   1 
ATOM   2871 C CA  . GLU   B 1 82  ? 9.534   -48.448 26.384 1.00 35.73  ? 157 GLU   B CA  1 
ATOM   2872 C C   . GLU   B 1 82  ? 10.952  -48.187 25.898 1.00 45.08  ? 157 GLU   B C   1 
ATOM   2873 O O   . GLU   B 1 82  ? 11.160  -47.915 24.709 1.00 46.25  ? 157 GLU   B O   1 
ATOM   2874 C CB  . GLU   B 1 82  ? 8.869   -47.144 26.826 1.00 41.34  ? 157 GLU   B CB  1 
ATOM   2875 C CG  . GLU   B 1 82  ? 8.742   -46.096 25.723 1.00 58.07  ? 157 GLU   B CG  1 
ATOM   2876 C CD  . GLU   B 1 82  ? 7.919   -44.887 26.143 1.00 55.15  ? 157 GLU   B CD  1 
ATOM   2877 O OE1 . GLU   B 1 82  ? 7.413   -44.871 27.286 1.00 58.45  ? 157 GLU   B OE1 1 
ATOM   2878 O OE2 . GLU   B 1 82  ? 7.772   -43.951 25.328 1.00 55.81  ? 157 GLU   B OE2 1 
ATOM   2879 N N   . VAL   B 1 83  ? 11.934  -48.267 26.796 1.00 41.72  ? 158 VAL   B N   1 
ATOM   2880 C CA  . VAL   B 1 83  ? 13.324  -48.117 26.383 1.00 36.65  ? 158 VAL   B CA  1 
ATOM   2881 C C   . VAL   B 1 83  ? 13.739  -49.282 25.494 1.00 40.80  ? 158 VAL   B C   1 
ATOM   2882 O O   . VAL   B 1 83  ? 14.394  -49.093 24.463 1.00 52.48  ? 158 VAL   B O   1 
ATOM   2883 C CB  . VAL   B 1 83  ? 14.234  -47.991 27.616 1.00 47.27  ? 158 VAL   B CB  1 
ATOM   2884 C CG1 . VAL   B 1 83  ? 15.650  -47.631 27.195 1.00 43.00  ? 158 VAL   B CG1 1 
ATOM   2885 C CG2 . VAL   B 1 83  ? 13.676  -46.963 28.584 1.00 35.38  ? 158 VAL   B CG2 1 
ATOM   2886 N N   . GLY   B 1 84  ? 13.361  -50.505 25.876 1.00 42.07  ? 159 GLY   B N   1 
ATOM   2887 C CA  . GLY   B 1 84  ? 13.676  -51.656 25.049 1.00 29.40  ? 159 GLY   B CA  1 
ATOM   2888 C C   . GLY   B 1 84  ? 12.957  -51.643 23.716 1.00 38.67  ? 159 GLY   B C   1 
ATOM   2889 O O   . GLY   B 1 84  ? 13.468  -52.176 22.727 1.00 51.24  ? 159 GLY   B O   1 
ATOM   2890 N N   . SER   B 1 85  ? 11.768  -51.034 23.665 1.00 36.57  ? 160 SER   B N   1 
ATOM   2891 C CA  . SER   B 1 85  ? 11.035  -50.948 22.407 1.00 38.41  ? 160 SER   B CA  1 
ATOM   2892 C C   . SER   B 1 85  ? 11.723  -50.003 21.425 1.00 45.43  ? 160 SER   B C   1 
ATOM   2893 O O   . SER   B 1 85  ? 11.804  -50.300 20.227 1.00 51.65  ? 160 SER   B O   1 
ATOM   2894 C CB  . SER   B 1 85  ? 9.596   -50.505 22.673 1.00 47.60  ? 160 SER   B CB  1 
ATOM   2895 O OG  . SER   B 1 85  ? 8.950   -51.393 23.571 1.00 47.99  ? 160 SER   B OG  1 
ATOM   2896 N N   . HIS   B 1 86  ? 12.218  -48.856 21.907 1.00 52.54  ? 161 HIS   B N   1 
ATOM   2897 C CA  . HIS   B 1 86  ? 13.018  -47.979 21.053 1.00 38.93  ? 161 HIS   B CA  1 
ATOM   2898 C C   . HIS   B 1 86  ? 14.267  -48.692 20.553 1.00 53.51  ? 161 HIS   B C   1 
ATOM   2899 O O   . HIS   B 1 86  ? 14.706  -48.476 19.417 1.00 63.69  ? 161 HIS   B O   1 
ATOM   2900 C CB  . HIS   B 1 86  ? 13.411  -46.716 21.814 1.00 44.83  ? 161 HIS   B CB  1 
ATOM   2901 C CG  . HIS   B 1 86  ? 12.433  -45.592 21.677 1.00 35.89  ? 161 HIS   B CG  1 
ATOM   2902 N ND1 . HIS   B 1 86  ? 12.509  -44.661 20.663 1.00 38.55  ? 161 HIS   B ND1 1 
ATOM   2903 C CD2 . HIS   B 1 86  ? 11.367  -45.239 22.434 1.00 31.00  ? 161 HIS   B CD2 1 
ATOM   2904 C CE1 . HIS   B 1 86  ? 11.527  -43.787 20.797 1.00 47.48  ? 161 HIS   B CE1 1 
ATOM   2905 N NE2 . HIS   B 1 86  ? 10.820  -44.115 21.864 1.00 40.59  ? 161 HIS   B NE2 1 
ATOM   2906 N N   . GLU   B 1 87  ? 14.860  -49.536 21.399 1.00 51.90  ? 162 GLU   B N   1 
ATOM   2907 C CA  . GLU   B 1 87  ? 16.053  -50.279 21.008 1.00 47.87  ? 162 GLU   B CA  1 
ATOM   2908 C C   . GLU   B 1 87  ? 15.753  -51.251 19.872 1.00 57.56  ? 162 GLU   B C   1 
ATOM   2909 O O   . GLU   B 1 87  ? 16.583  -51.440 18.974 1.00 63.62  ? 162 GLU   B O   1 
ATOM   2910 C CB  . GLU   B 1 87  ? 16.616  -51.018 22.224 1.00 61.79  ? 162 GLU   B CB  1 
ATOM   2911 C CG  . GLU   B 1 87  ? 17.869  -51.841 21.960 1.00 80.75  ? 162 GLU   B CG  1 
ATOM   2912 C CD  . GLU   B 1 87  ? 18.393  -52.517 23.217 1.00 93.69  ? 162 GLU   B CD  1 
ATOM   2913 O OE1 . GLU   B 1 87  ? 17.742  -52.387 24.276 1.00 94.52  ? 162 GLU   B OE1 1 
ATOM   2914 O OE2 . GLU   B 1 87  ? 19.455  -53.174 23.148 1.00 86.41  ? 162 GLU   B OE2 1 
ATOM   2915 N N   . LYS   B 1 88  ? 14.571  -51.876 19.892 1.00 55.60  ? 163 LYS   B N   1 
ATOM   2916 C CA  . LYS   B 1 88  ? 14.226  -52.837 18.848 1.00 46.73  ? 163 LYS   B CA  1 
ATOM   2917 C C   . LYS   B 1 88  ? 13.869  -52.146 17.540 1.00 45.79  ? 163 LYS   B C   1 
ATOM   2918 O O   . LYS   B 1 88  ? 14.080  -52.715 16.462 1.00 59.93  ? 163 LYS   B O   1 
ATOM   2919 C CB  . LYS   B 1 88  ? 13.066  -53.723 19.304 1.00 44.42  ? 163 LYS   B CB  1 
ATOM   2920 C CG  . LYS   B 1 88  ? 13.383  -54.610 20.495 1.00 51.78  ? 163 LYS   B CG  1 
ATOM   2921 C CD  . LYS   B 1 88  ? 12.178  -55.449 20.888 1.00 52.82  ? 163 LYS   B CD  1 
ATOM   2922 C CE  . LYS   B 1 88  ? 12.498  -56.365 22.057 1.00 56.74  ? 163 LYS   B CE  1 
ATOM   2923 N NZ  . LYS   B 1 88  ? 11.324  -57.193 22.455 1.00 84.06  ? 163 LYS   B NZ  1 
ATOM   2924 N N   . VAL   B 1 89  ? 13.332  -50.930 17.609 1.00 43.87  ? 164 VAL   B N   1 
ATOM   2925 C CA  . VAL   B 1 89  ? 12.936  -50.226 16.393 1.00 52.06  ? 164 VAL   B CA  1 
ATOM   2926 C C   . VAL   B 1 89  ? 14.166  -49.721 15.650 1.00 56.36  ? 164 VAL   B C   1 
ATOM   2927 O O   . VAL   B 1 89  ? 14.282  -49.876 14.428 1.00 68.10  ? 164 VAL   B O   1 
ATOM   2928 C CB  . VAL   B 1 89  ? 11.966  -49.079 16.727 1.00 50.43  ? 164 VAL   B CB  1 
ATOM   2929 C CG1 . VAL   B 1 89  ? 11.749  -48.200 15.511 1.00 53.42  ? 164 VAL   B CG1 1 
ATOM   2930 C CG2 . VAL   B 1 89  ? 10.641  -49.639 17.221 1.00 43.73  ? 164 VAL   B CG2 1 
ATOM   2931 N N   . GLY   B 1 90  ? 15.105  -49.122 16.372 1.00 53.88  ? 165 GLY   B N   1 
ATOM   2932 C CA  . GLY   B 1 90  ? 16.305  -48.620 15.739 1.00 58.44  ? 165 GLY   B CA  1 
ATOM   2933 C C   . GLY   B 1 90  ? 16.100  -47.235 15.154 1.00 54.56  ? 165 GLY   B C   1 
ATOM   2934 O O   . GLY   B 1 90  ? 15.208  -46.477 15.551 1.00 64.05  ? 165 GLY   B O   1 
ATOM   2935 N N   . GLN   B 1 91  ? 16.950  -46.905 14.185 1.00 58.92  ? 166 GLN   B N   1 
ATOM   2936 C CA  . GLN   B 1 91  ? 16.949  -45.592 13.552 1.00 62.18  ? 166 GLN   B CA  1 
ATOM   2937 C C   . GLN   B 1 91  ? 16.284  -45.691 12.184 1.00 49.07  ? 166 GLN   B C   1 
ATOM   2938 O O   . GLN   B 1 91  ? 16.804  -46.345 11.274 1.00 68.72  ? 166 GLN   B O   1 
ATOM   2939 C CB  . GLN   B 1 91  ? 18.369  -45.043 13.429 1.00 49.55  ? 166 GLN   B CB  1 
ATOM   2940 C CG  . GLN   B 1 91  ? 19.012  -44.700 14.762 1.00 68.54  ? 166 GLN   B CG  1 
ATOM   2941 C CD  . GLN   B 1 91  ? 20.355  -44.016 14.603 1.00 100.21 ? 166 GLN   B CD  1 
ATOM   2942 O OE1 . GLN   B 1 91  ? 20.575  -42.926 15.130 1.00 99.66  ? 166 GLN   B OE1 1 
ATOM   2943 N NE2 . GLN   B 1 91  ? 21.264  -44.657 13.877 1.00 104.94 ? 166 GLN   B NE2 1 
ATOM   2944 N N   . HIS   B 1 92  ? 15.131  -45.040 12.045 1.00 55.73  ? 167 HIS   B N   1 
ATOM   2945 C CA  . HIS   B 1 92  ? 14.441  -44.896 10.777 1.00 47.30  ? 167 HIS   B CA  1 
ATOM   2946 C C   . HIS   B 1 92  ? 14.008  -43.444 10.632 1.00 49.41  ? 167 HIS   B C   1 
ATOM   2947 O O   . HIS   B 1 92  ? 13.630  -42.808 11.625 1.00 56.96  ? 167 HIS   B O   1 
ATOM   2948 C CB  . HIS   B 1 92  ? 13.221  -45.827 10.698 1.00 45.48  ? 167 HIS   B CB  1 
ATOM   2949 C CG  . HIS   B 1 92  ? 12.588  -45.884 9.343  1.00 43.19  ? 167 HIS   B CG  1 
ATOM   2950 N ND1 . HIS   B 1 92  ? 11.461  -45.160 9.017  1.00 52.13  ? 167 HIS   B ND1 1 
ATOM   2951 C CD2 . HIS   B 1 92  ? 12.924  -46.577 8.229  1.00 58.80  ? 167 HIS   B CD2 1 
ATOM   2952 C CE1 . HIS   B 1 92  ? 11.130  -45.406 7.761  1.00 53.60  ? 167 HIS   B CE1 1 
ATOM   2953 N NE2 . HIS   B 1 92  ? 12.002  -46.262 7.260  1.00 59.90  ? 167 HIS   B NE2 1 
ATOM   2954 N N   . PRO   B 1 93  ? 14.062  -42.885 9.419  1.00 49.90  ? 168 PRO   B N   1 
ATOM   2955 C CA  . PRO   B 1 93  ? 13.741  -41.456 9.251  1.00 48.40  ? 168 PRO   B CA  1 
ATOM   2956 C C   . PRO   B 1 93  ? 12.329  -41.068 9.674  1.00 54.10  ? 168 PRO   B C   1 
ATOM   2957 O O   . PRO   B 1 93  ? 12.050  -39.867 9.779  1.00 63.72  ? 168 PRO   B O   1 
ATOM   2958 C CB  . PRO   B 1 93  ? 13.944  -41.227 7.748  1.00 48.22  ? 168 PRO   B CB  1 
ATOM   2959 C CG  . PRO   B 1 93  ? 14.890  -42.295 7.329  1.00 66.31  ? 168 PRO   B CG  1 
ATOM   2960 C CD  . PRO   B 1 93  ? 14.564  -43.487 8.173  1.00 50.70  ? 168 PRO   B CD  1 
ATOM   2961 N N   . CYS   B 1 94  ? 11.433  -42.026 9.919  1.00 43.74  ? 169 CYS   B N   1 
ATOM   2962 C CA  . CYS   B 1 94  ? 10.048  -41.717 10.258 1.00 43.30  ? 169 CYS   B CA  1 
ATOM   2963 C C   . CYS   B 1 94  ? 9.665   -42.206 11.649 1.00 42.48  ? 169 CYS   B C   1 
ATOM   2964 O O   . CYS   B 1 94  ? 8.475   -42.372 11.936 1.00 49.05  ? 169 CYS   B O   1 
ATOM   2965 C CB  . CYS   B 1 94  ? 9.098   -42.311 9.217  1.00 40.41  ? 169 CYS   B CB  1 
ATOM   2966 S SG  . CYS   B 1 94  ? 9.325   -41.668 7.551  1.00 58.43  ? 169 CYS   B SG  1 
ATOM   2967 N N   . CYS   B 1 95  ? 10.644  -42.451 12.516 1.00 38.88  ? 170 CYS   B N   1 
ATOM   2968 C CA  . CYS   B 1 95  ? 10.389  -42.902 13.876 1.00 36.99  ? 170 CYS   B CA  1 
ATOM   2969 C C   . CYS   B 1 95  ? 11.147  -42.006 14.841 1.00 38.34  ? 170 CYS   B C   1 
ATOM   2970 O O   . CYS   B 1 95  ? 12.293  -41.627 14.575 1.00 56.51  ? 170 CYS   B O   1 
ATOM   2971 C CB  . CYS   B 1 95  ? 10.807  -44.368 14.078 1.00 49.85  ? 170 CYS   B CB  1 
ATOM   2972 S SG  . CYS   B 1 95  ? 9.859   -45.584 13.124 1.00 55.90  ? 170 CYS   B SG  1 
ATOM   2973 N N   . VAL   B 1 96  ? 10.501  -41.663 15.957 1.00 52.67  ? 171 VAL   B N   1 
ATOM   2974 C CA  . VAL   B 1 96  ? 11.125  -40.788 16.944 1.00 49.05  ? 171 VAL   B CA  1 
ATOM   2975 C C   . VAL   B 1 96  ? 12.348  -41.487 17.515 1.00 46.97  ? 171 VAL   B C   1 
ATOM   2976 O O   . VAL   B 1 96  ? 12.247  -42.586 18.073 1.00 50.84  ? 171 VAL   B O   1 
ATOM   2977 C CB  . VAL   B 1 96  ? 10.132  -40.412 18.048 1.00 36.63  ? 171 VAL   B CB  1 
ATOM   2978 C CG1 . VAL   B 1 96  ? 10.850  -39.662 19.154 1.00 45.19  ? 171 VAL   B CG1 1 
ATOM   2979 C CG2 . VAL   B 1 96  ? 9.005   -39.565 17.487 1.00 35.84  ? 171 VAL   B CG2 1 
ATOM   2980 N N   . ARG   B 1 97  ? 13.510  -40.854 17.376 1.00 41.54  ? 172 ARG   B N   1 
ATOM   2981 C CA  . ARG   B 1 97  ? 14.772  -41.453 17.793 1.00 48.02  ? 172 ARG   B CA  1 
ATOM   2982 C C   . ARG   B 1 97  ? 15.026  -41.194 19.273 1.00 53.20  ? 172 ARG   B C   1 
ATOM   2983 O O   . ARG   B 1 97  ? 14.966  -40.048 19.732 1.00 47.79  ? 172 ARG   B O   1 
ATOM   2984 C CB  . ARG   B 1 97  ? 15.932  -40.900 16.963 1.00 46.10  ? 172 ARG   B CB  1 
ATOM   2985 C CG  . ARG   B 1 97  ? 17.283  -41.477 17.347 1.00 49.01  ? 172 ARG   B CG  1 
ATOM   2986 C CD  . ARG   B 1 97  ? 18.395  -40.920 16.478 1.00 64.89  ? 172 ARG   B CD  1 
ATOM   2987 N NE  . ARG   B 1 97  ? 18.632  -39.504 16.731 1.00 90.76  ? 172 ARG   B NE  1 
ATOM   2988 C CZ  . ARG   B 1 97  ? 18.213  -38.520 15.948 1.00 99.11  ? 172 ARG   B CZ  1 
ATOM   2989 N NH1 . ARG   B 1 97  ? 17.533  -38.760 14.838 1.00 87.70  ? 172 ARG   B NH1 1 
ATOM   2990 N NH2 . ARG   B 1 97  ? 18.487  -37.262 16.285 1.00 93.75  ? 172 ARG   B NH2 1 
ATOM   2991 N N   . LEU   B 1 98  ? 15.312  -42.261 20.015 1.00 47.99  ? 173 LEU   B N   1 
ATOM   2992 C CA  . LEU   B 1 98  ? 15.691  -42.151 21.416 1.00 36.24  ? 173 LEU   B CA  1 
ATOM   2993 C C   . LEU   B 1 98  ? 17.194  -41.935 21.517 1.00 49.89  ? 173 LEU   B C   1 
ATOM   2994 O O   . LEU   B 1 98  ? 17.978  -42.727 20.982 1.00 53.85  ? 173 LEU   B O   1 
ATOM   2995 C CB  . LEU   B 1 98  ? 15.285  -43.407 22.187 1.00 44.35  ? 173 LEU   B CB  1 
ATOM   2996 C CG  . LEU   B 1 98  ? 15.701  -43.482 23.660 1.00 48.03  ? 173 LEU   B CG  1 
ATOM   2997 C CD1 . LEU   B 1 98  ? 14.932  -42.480 24.496 1.00 34.69  ? 173 LEU   B CD1 1 
ATOM   2998 C CD2 . LEU   B 1 98  ? 15.490  -44.883 24.195 1.00 48.20  ? 173 LEU   B CD2 1 
ATOM   2999 N N   . GLU   B 1 99  ? 17.594  -40.865 22.204 1.00 43.80  ? 174 GLU   B N   1 
ATOM   3000 C CA  . GLU   B 1 99  ? 19.012  -40.566 22.390 1.00 46.60  ? 174 GLU   B CA  1 
ATOM   3001 C C   . GLU   B 1 99  ? 19.573  -41.221 23.650 1.00 43.76  ? 174 GLU   B C   1 
ATOM   3002 O O   . GLU   B 1 99  ? 20.487  -42.049 23.575 1.00 59.72  ? 174 GLU   B O   1 
ATOM   3003 C CB  . GLU   B 1 99  ? 19.224  -39.049 22.435 1.00 45.83  ? 174 GLU   B CB  1 
ATOM   3004 C CG  . GLU   B 1 99  ? 18.790  -38.329 21.172 1.00 66.34  ? 174 GLU   B CG  1 
ATOM   3005 C CD  . GLU   B 1 99  ? 19.703  -38.608 19.998 1.00 75.19  ? 174 GLU   B CD  1 
ATOM   3006 O OE1 . GLU   B 1 99  ? 20.923  -38.767 20.217 1.00 70.32  ? 174 GLU   B OE1 1 
ATOM   3007 O OE2 . GLU   B 1 99  ? 19.201  -38.668 18.856 1.00 79.98  ? 174 GLU   B OE2 1 
ATOM   3008 N N   A GLN   B 1 100 ? 19.025  -40.868 24.812 0.59 47.14  ? 175 GLN   B N   1 
ATOM   3009 N N   B GLN   B 1 100 ? 19.050  -40.846 24.814 0.41 47.03  ? 175 GLN   B N   1 
ATOM   3010 C CA  A GLN   B 1 100 ? 19.504  -41.360 26.096 0.59 41.20  ? 175 GLN   B CA  1 
ATOM   3011 C CA  B GLN   B 1 100 ? 19.494  -41.394 26.085 0.41 41.22  ? 175 GLN   B CA  1 
ATOM   3012 C C   A GLN   B 1 100 ? 18.304  -41.680 26.978 0.59 37.11  ? 175 GLN   B C   1 
ATOM   3013 C C   B GLN   B 1 100 ? 18.281  -41.748 26.931 0.41 37.75  ? 175 GLN   B C   1 
ATOM   3014 O O   A GLN   B 1 100 ? 17.207  -41.155 26.781 0.59 42.00  ? 175 GLN   B O   1 
ATOM   3015 O O   B GLN   B 1 100 ? 17.160  -41.307 26.668 0.41 42.08  ? 175 GLN   B O   1 
ATOM   3016 C CB  A GLN   B 1 100 ? 20.413  -40.330 26.786 0.59 41.96  ? 175 GLN   B CB  1 
ATOM   3017 C CB  B GLN   B 1 100 ? 20.388  -40.409 26.854 0.41 41.99  ? 175 GLN   B CB  1 
ATOM   3018 C CG  A GLN   B 1 100 ? 21.287  -40.888 27.898 0.59 44.07  ? 175 GLN   B CG  1 
ATOM   3019 C CG  B GLN   B 1 100 ? 21.752  -40.173 26.232 0.41 55.30  ? 175 GLN   B CG  1 
ATOM   3020 C CD  A GLN   B 1 100 ? 22.486  -41.650 27.371 0.59 58.27  ? 175 GLN   B CD  1 
ATOM   3021 C CD  B GLN   B 1 100 ? 22.539  -39.102 26.960 0.41 52.39  ? 175 GLN   B CD  1 
ATOM   3022 O OE1 A GLN   B 1 100 ? 23.404  -41.063 26.798 0.59 55.86  ? 175 GLN   B OE1 1 
ATOM   3023 O OE1 B GLN   B 1 100 ? 23.750  -38.981 26.786 0.41 68.69  ? 175 GLN   B OE1 1 
ATOM   3024 N NE2 A GLN   B 1 100 ? 22.484  -42.964 27.560 0.59 61.41  ? 175 GLN   B NE2 1 
ATOM   3025 N NE2 B GLN   B 1 100 ? 21.852  -38.315 27.778 0.41 37.82  ? 175 GLN   B NE2 1 
ATOM   3026 N N   . ALA   B 1 101 ? 18.522  -42.551 27.960 1.00 41.35  ? 176 ALA   B N   1 
ATOM   3027 C CA  . ALA   B 1 101 ? 17.473  -42.915 28.900 1.00 33.38  ? 176 ALA   B CA  1 
ATOM   3028 C C   . ALA   B 1 101 ? 18.141  -43.234 30.223 1.00 32.61  ? 176 ALA   B C   1 
ATOM   3029 O O   . ALA   B 1 101 ? 19.174  -43.907 30.244 1.00 40.39  ? 176 ALA   B O   1 
ATOM   3030 C CB  . ALA   B 1 101 ? 16.653  -44.108 28.401 1.00 24.70  ? 176 ALA   B CB  1 
ATOM   3031 N N   . TRP   B 1 102 ? 17.566  -42.739 31.314 1.00 34.67  ? 177 TRP   B N   1 
ATOM   3032 C CA  . TRP   B 1 102 ? 18.146  -42.960 32.629 1.00 36.14  ? 177 TRP   B CA  1 
ATOM   3033 C C   . TRP   B 1 102 ? 17.033  -42.945 33.664 1.00 34.36  ? 177 TRP   B C   1 
ATOM   3034 O O   . TRP   B 1 102 ? 15.881  -42.620 33.367 1.00 38.04  ? 177 TRP   B O   1 
ATOM   3035 C CB  . TRP   B 1 102 ? 19.215  -41.913 32.957 1.00 47.94  ? 177 TRP   B CB  1 
ATOM   3036 C CG  . TRP   B 1 102 ? 18.688  -40.523 33.133 1.00 36.95  ? 177 TRP   B CG  1 
ATOM   3037 C CD1 . TRP   B 1 102 ? 18.357  -39.915 34.308 1.00 38.03  ? 177 TRP   B CD1 1 
ATOM   3038 C CD2 . TRP   B 1 102 ? 18.443  -39.560 32.101 1.00 40.87  ? 177 TRP   B CD2 1 
ATOM   3039 N NE1 . TRP   B 1 102 ? 17.916  -38.635 34.072 1.00 35.45  ? 177 TRP   B NE1 1 
ATOM   3040 C CE2 . TRP   B 1 102 ? 17.961  -38.393 32.725 1.00 36.12  ? 177 TRP   B CE2 1 
ATOM   3041 C CE3 . TRP   B 1 102 ? 18.583  -39.573 30.710 1.00 42.38  ? 177 TRP   B CE3 1 
ATOM   3042 C CZ2 . TRP   B 1 102 ? 17.615  -37.252 32.006 1.00 41.40  ? 177 TRP   B CZ2 1 
ATOM   3043 C CZ3 . TRP   B 1 102 ? 18.240  -38.439 29.999 1.00 38.71  ? 177 TRP   B CZ3 1 
ATOM   3044 C CH2 . TRP   B 1 102 ? 17.762  -37.295 30.647 1.00 37.51  ? 177 TRP   B CH2 1 
ATOM   3045 N N   . GLU   B 1 103 ? 17.389  -43.314 34.889 1.00 41.36  ? 178 GLU   B N   1 
ATOM   3046 C CA  . GLU   B 1 103 ? 16.452  -43.334 36.001 1.00 41.27  ? 178 GLU   B CA  1 
ATOM   3047 C C   . GLU   B 1 103 ? 17.119  -42.725 37.220 1.00 37.43  ? 178 GLU   B C   1 
ATOM   3048 O O   . GLU   B 1 103 ? 18.301  -42.972 37.481 1.00 49.16  ? 178 GLU   B O   1 
ATOM   3049 C CB  . GLU   B 1 103 ? 15.971  -44.762 36.317 1.00 41.22  ? 178 GLU   B CB  1 
ATOM   3050 C CG  . GLU   B 1 103 ? 17.092  -45.767 36.570 1.00 69.24  ? 178 GLU   B CG  1 
ATOM   3051 C CD  . GLU   B 1 103 ? 16.578  -47.171 36.840 1.00 67.31  ? 178 GLU   B CD  1 
ATOM   3052 O OE1 . GLU   B 1 103 ? 15.355  -47.331 37.038 1.00 79.23  ? 178 GLU   B OE1 1 
ATOM   3053 O OE2 . GLU   B 1 103 ? 17.397  -48.116 36.854 1.00 67.64  ? 178 GLU   B OE2 1 
ATOM   3054 N N   . GLU   B 1 104 ? 16.360  -41.922 37.959 1.00 38.74  ? 179 GLU   B N   1 
ATOM   3055 C CA  . GLU   B 1 104 ? 16.855  -41.325 39.191 1.00 30.82  ? 179 GLU   B CA  1 
ATOM   3056 C C   . GLU   B 1 104 ? 15.671  -41.098 40.117 1.00 47.97  ? 179 GLU   B C   1 
ATOM   3057 O O   . GLU   B 1 104 ? 14.644  -40.561 39.690 1.00 54.44  ? 179 GLU   B O   1 
ATOM   3058 C CB  . GLU   B 1 104 ? 17.586  -40.007 38.915 1.00 43.99  ? 179 GLU   B CB  1 
ATOM   3059 C CG  . GLU   B 1 104 ? 18.255  -39.400 40.137 1.00 57.73  ? 179 GLU   B CG  1 
ATOM   3060 C CD  . GLU   B 1 104 ? 18.943  -38.087 39.830 1.00 67.19  ? 179 GLU   B CD  1 
ATOM   3061 O OE1 . GLU   B 1 104 ? 18.868  -37.635 38.667 1.00 78.02  ? 179 GLU   B OE1 1 
ATOM   3062 O OE2 . GLU   B 1 104 ? 19.557  -37.505 40.750 1.00 81.02  ? 179 GLU   B OE2 1 
ATOM   3063 N N   . GLY   B 1 105 ? 15.814  -41.515 41.371 1.00 42.43  ? 180 GLY   B N   1 
ATOM   3064 C CA  . GLY   B 1 105 ? 14.730  -41.364 42.331 1.00 35.31  ? 180 GLY   B CA  1 
ATOM   3065 C C   . GLY   B 1 105 ? 13.465  -42.092 41.936 1.00 33.83  ? 180 GLY   B C   1 
ATOM   3066 O O   . GLY   B 1 105 ? 12.360  -41.605 42.210 1.00 64.49  ? 180 GLY   B O   1 
ATOM   3067 N N   . GLY   B 1 106 ? 13.598  -43.248 41.290 1.00 47.22  ? 181 GLY   B N   1 
ATOM   3068 C CA  . GLY   B 1 106 ? 12.437  -43.997 40.851 1.00 38.67  ? 181 GLY   B CA  1 
ATOM   3069 C C   . GLY   B 1 106 ? 11.712  -43.402 39.669 1.00 40.92  ? 181 GLY   B C   1 
ATOM   3070 O O   . GLY   B 1 106 ? 10.645  -43.899 39.297 1.00 54.73  ? 181 GLY   B O   1 
ATOM   3071 N N   . ILE   B 1 107 ? 12.262  -42.355 39.066 1.00 46.85  ? 182 ILE   B N   1 
ATOM   3072 C CA  . ILE   B 1 107 ? 11.653  -41.668 37.937 1.00 36.68  ? 182 ILE   B CA  1 
ATOM   3073 C C   . ILE   B 1 107 ? 12.430  -42.042 36.683 1.00 40.58  ? 182 ILE   B C   1 
ATOM   3074 O O   . ILE   B 1 107 ? 13.667  -42.007 36.679 1.00 48.91  ? 182 ILE   B O   1 
ATOM   3075 C CB  . ILE   B 1 107 ? 11.650  -40.145 38.149 1.00 45.99  ? 182 ILE   B CB  1 
ATOM   3076 C CG1 . ILE   B 1 107 ? 10.924  -39.782 39.448 1.00 47.44  ? 182 ILE   B CG1 1 
ATOM   3077 C CG2 . ILE   B 1 107 ? 11.001  -39.457 36.980 1.00 49.37  ? 182 ILE   B CG2 1 
ATOM   3078 C CD1 . ILE   B 1 107 ? 9.456   -40.174 39.464 1.00 43.67  ? 182 ILE   B CD1 1 
ATOM   3079 N N   . LEU   B 1 108 ? 11.712  -42.402 35.627 1.00 37.02  ? 183 LEU   B N   1 
ATOM   3080 C CA  . LEU   B 1 108 ? 12.324  -42.747 34.351 1.00 39.46  ? 183 LEU   B CA  1 
ATOM   3081 C C   . LEU   B 1 108 ? 12.322  -41.528 33.437 1.00 40.12  ? 183 LEU   B C   1 
ATOM   3082 O O   . LEU   B 1 108 ? 11.286  -40.875 33.272 1.00 41.62  ? 183 LEU   B O   1 
ATOM   3083 C CB  . LEU   B 1 108 ? 11.579  -43.903 33.687 1.00 36.03  ? 183 LEU   B CB  1 
ATOM   3084 C CG  . LEU   B 1 108 ? 12.039  -44.233 32.271 1.00 34.15  ? 183 LEU   B CG  1 
ATOM   3085 C CD1 . LEU   B 1 108 ? 13.472  -44.753 32.289 1.00 30.55  ? 183 LEU   B CD1 1 
ATOM   3086 C CD2 . LEU   B 1 108 ? 11.089  -45.232 31.633 1.00 33.93  ? 183 LEU   B CD2 1 
ATOM   3087 N N   . TYR   B 1 109 ? 13.479  -41.232 32.845 1.00 42.29  ? 184 TYR   B N   1 
ATOM   3088 C CA  . TYR   B 1 109 ? 13.641  -40.123 31.914 1.00 24.98  ? 184 TYR   B CA  1 
ATOM   3089 C C   . TYR   B 1 109 ? 14.012  -40.667 30.541 1.00 34.77  ? 184 TYR   B C   1 
ATOM   3090 O O   . TYR   B 1 109 ? 14.903  -41.515 30.427 1.00 43.04  ? 184 TYR   B O   1 
ATOM   3091 C CB  . TYR   B 1 109 ? 14.723  -39.158 32.388 1.00 40.42  ? 184 TYR   B CB  1 
ATOM   3092 C CG  . TYR   B 1 109 ? 14.446  -38.479 33.708 1.00 34.79  ? 184 TYR   B CG  1 
ATOM   3093 C CD1 . TYR   B 1 109 ? 14.678  -39.132 34.911 1.00 36.26  ? 184 TYR   B CD1 1 
ATOM   3094 C CD2 . TYR   B 1 109 ? 13.976  -37.175 33.750 1.00 29.94  ? 184 TYR   B CD2 1 
ATOM   3095 C CE1 . TYR   B 1 109 ? 14.434  -38.509 36.120 1.00 42.57  ? 184 TYR   B CE1 1 
ATOM   3096 C CE2 . TYR   B 1 109 ? 13.729  -36.544 34.954 1.00 38.07  ? 184 TYR   B CE2 1 
ATOM   3097 C CZ  . TYR   B 1 109 ? 13.961  -37.215 36.136 1.00 46.51  ? 184 TYR   B CZ  1 
ATOM   3098 O OH  . TYR   B 1 109 ? 13.719  -36.592 37.340 1.00 59.77  ? 184 TYR   B OH  1 
ATOM   3099 N N   . LEU   B 1 110 ? 13.344  -40.169 29.501 1.00 35.47  ? 185 LEU   B N   1 
ATOM   3100 C CA  . LEU   B 1 110 ? 13.597  -40.586 28.123 1.00 31.15  ? 185 LEU   B CA  1 
ATOM   3101 C C   . LEU   B 1 110 ? 13.930  -39.348 27.303 1.00 29.54  ? 185 LEU   B C   1 
ATOM   3102 O O   . LEU   B 1 110 ? 13.074  -38.479 27.108 1.00 42.81  ? 185 LEU   B O   1 
ATOM   3103 C CB  . LEU   B 1 110 ? 12.392  -41.316 27.533 1.00 35.48  ? 185 LEU   B CB  1 
ATOM   3104 C CG  . LEU   B 1 110 ? 11.894  -42.547 28.290 1.00 43.21  ? 185 LEU   B CG  1 
ATOM   3105 C CD1 . LEU   B 1 110 ? 10.826  -43.274 27.492 1.00 53.22  ? 185 LEU   B CD1 1 
ATOM   3106 C CD2 . LEU   B 1 110 ? 13.052  -43.467 28.589 1.00 46.41  ? 185 LEU   B CD2 1 
ATOM   3107 N N   . GLN   B 1 111 ? 15.164  -39.269 26.822 1.00 38.79  ? 186 GLN   B N   1 
ATOM   3108 C CA  . GLN   B 1 111 ? 15.625  -38.140 26.023 1.00 34.86  ? 186 GLN   B CA  1 
ATOM   3109 C C   . GLN   B 1 111 ? 15.585  -38.540 24.551 1.00 50.84  ? 186 GLN   B C   1 
ATOM   3110 O O   . GLN   B 1 111 ? 16.353  -39.407 24.117 1.00 49.49  ? 186 GLN   B O   1 
ATOM   3111 C CB  . GLN   B 1 111 ? 17.032  -37.723 26.434 1.00 36.36  ? 186 GLN   B CB  1 
ATOM   3112 C CG  . GLN   B 1 111 ? 17.595  -36.607 25.585 1.00 42.42  ? 186 GLN   B CG  1 
ATOM   3113 C CD  . GLN   B 1 111 ? 19.037  -36.314 25.915 1.00 40.34  ? 186 GLN   B CD  1 
ATOM   3114 O OE1 . GLN   B 1 111 ? 19.644  -36.995 26.740 1.00 50.59  ? 186 GLN   B OE1 1 
ATOM   3115 N NE2 . GLN   B 1 111 ? 19.597  -35.297 25.272 1.00 53.28  ? 186 GLN   B NE2 1 
ATOM   3116 N N   . THR   B 1 112 ? 14.698  -37.907 23.787 1.00 41.80  ? 187 THR   B N   1 
ATOM   3117 C CA  . THR   B 1 112 ? 14.541  -38.188 22.367 1.00 52.32  ? 187 THR   B CA  1 
ATOM   3118 C C   . THR   B 1 112 ? 14.843  -36.942 21.548 1.00 44.47  ? 187 THR   B C   1 
ATOM   3119 O O   . THR   B 1 112 ? 15.036  -35.844 22.079 1.00 50.85  ? 187 THR   B O   1 
ATOM   3120 C CB  . THR   B 1 112 ? 13.123  -38.673 22.043 1.00 36.30  ? 187 THR   B CB  1 
ATOM   3121 O OG1 . THR   B 1 112 ? 12.198  -37.597 22.247 1.00 52.03  ? 187 THR   B OG1 1 
ATOM   3122 C CG2 . THR   B 1 112 ? 12.736  -39.843 22.926 1.00 37.66  ? 187 THR   B CG2 1 
ATOM   3123 N N   . GLU   B 1 113 ? 14.883  -37.127 20.230 1.00 41.86  ? 188 GLU   B N   1 
ATOM   3124 C CA  . GLU   B 1 113 ? 15.005  -35.993 19.329 1.00 36.43  ? 188 GLU   B CA  1 
ATOM   3125 C C   . GLU   B 1 113 ? 13.780  -35.098 19.460 1.00 51.12  ? 188 GLU   B C   1 
ATOM   3126 O O   . GLU   B 1 113 ? 12.678  -35.555 19.774 1.00 61.39  ? 188 GLU   B O   1 
ATOM   3127 C CB  . GLU   B 1 113 ? 15.143  -36.470 17.886 1.00 45.79  ? 188 GLU   B CB  1 
ATOM   3128 C CG  . GLU   B 1 113 ? 13.997  -37.370 17.440 1.00 57.72  ? 188 GLU   B CG  1 
ATOM   3129 C CD  . GLU   B 1 113 ? 14.000  -37.636 15.949 1.00 69.44  ? 188 GLU   B CD  1 
ATOM   3130 O OE1 . GLU   B 1 113 ? 14.597  -36.831 15.202 1.00 62.41  ? 188 GLU   B OE1 1 
ATOM   3131 O OE2 . GLU   B 1 113 ? 13.406  -38.651 15.523 1.00 70.42  ? 188 GLU   B OE2 1 
ATOM   3132 N N   . LEU   B 1 114 ? 13.978  -33.808 19.214 1.00 55.63  ? 189 LEU   B N   1 
ATOM   3133 C CA  . LEU   B 1 114 ? 12.881  -32.850 19.294 1.00 41.96  ? 189 LEU   B CA  1 
ATOM   3134 C C   . LEU   B 1 114 ? 12.091  -32.881 17.994 1.00 33.79  ? 189 LEU   B C   1 
ATOM   3135 O O   . LEU   B 1 114 ? 12.616  -32.540 16.931 1.00 50.42  ? 189 LEU   B O   1 
ATOM   3136 C CB  . LEU   B 1 114 ? 13.409  -31.448 19.571 1.00 57.09  ? 189 LEU   B CB  1 
ATOM   3137 C CG  . LEU   B 1 114 ? 12.322  -30.381 19.713 1.00 52.85  ? 189 LEU   B CG  1 
ATOM   3138 C CD1 . LEU   B 1 114 ? 11.555  -30.576 21.013 1.00 48.96  ? 189 LEU   B CD1 1 
ATOM   3139 C CD2 . LEU   B 1 114 ? 12.907  -28.980 19.626 1.00 59.24  ? 189 LEU   B CD2 1 
ATOM   3140 N N   . CYS   B 1 115 ? 10.836  -33.306 18.075 1.00 56.41  ? 190 CYS   B N   1 
ATOM   3141 C CA  . CYS   B 1 115 ? 9.912   -33.236 16.957 1.00 43.23  ? 190 CYS   B CA  1 
ATOM   3142 C C   . CYS   B 1 115 ? 8.962   -32.060 17.173 1.00 47.69  ? 190 CYS   B C   1 
ATOM   3143 O O   . CYS   B 1 115 ? 8.972   -31.398 18.214 1.00 64.16  ? 190 CYS   B O   1 
ATOM   3144 C CB  . CYS   B 1 115 ? 9.146   -34.552 16.808 1.00 52.32  ? 190 CYS   B CB  1 
ATOM   3145 S SG  . CYS   B 1 115 ? 10.197  -36.012 16.725 1.00 64.76  ? 190 CYS   B SG  1 
ATOM   3146 N N   . GLY   B 1 116 ? 8.120   -31.796 16.182 1.00 44.68  ? 191 GLY   B N   1 
ATOM   3147 C CA  . GLY   B 1 116 ? 7.160   -30.722 16.292 1.00 56.58  ? 191 GLY   B CA  1 
ATOM   3148 C C   . GLY   B 1 116 ? 5.960   -31.122 17.127 1.00 42.67  ? 191 GLY   B C   1 
ATOM   3149 O O   . GLY   B 1 116 ? 6.019   -32.048 17.943 1.00 43.40  ? 191 GLY   B O   1 
ATOM   3150 N N   . PRO   B 1 117 ? 4.842   -30.428 16.936 1.00 44.12  ? 192 PRO   B N   1 
ATOM   3151 C CA  . PRO   B 1 117 ? 3.623   -30.778 17.668 1.00 38.41  ? 192 PRO   B CA  1 
ATOM   3152 C C   . PRO   B 1 117 ? 3.050   -32.103 17.188 1.00 40.28  ? 192 PRO   B C   1 
ATOM   3153 O O   . PRO   B 1 117 ? 3.354   -32.591 16.097 1.00 45.72  ? 192 PRO   B O   1 
ATOM   3154 C CB  . PRO   B 1 117 ? 2.675   -29.620 17.346 1.00 29.55  ? 192 PRO   B CB  1 
ATOM   3155 C CG  . PRO   B 1 117 ? 3.127   -29.154 15.995 1.00 41.67  ? 192 PRO   B CG  1 
ATOM   3156 C CD  . PRO   B 1 117 ? 4.628   -29.301 16.011 1.00 52.00  ? 192 PRO   B CD  1 
ATOM   3157 N N   . SER   B 1 118 ? 2.208   -32.693 18.031 1.00 38.78  ? 193 SER   B N   1 
ATOM   3158 C CA  . SER   B 1 118 ? 1.558   -33.932 17.645 1.00 29.89  ? 193 SER   B CA  1 
ATOM   3159 C C   . SER   B 1 118 ? 0.484   -33.651 16.602 1.00 28.35  ? 193 SER   B C   1 
ATOM   3160 O O   . SER   B 1 118 ? 0.015   -32.523 16.440 1.00 42.66  ? 193 SER   B O   1 
ATOM   3161 C CB  . SER   B 1 118 ? 0.942   -34.627 18.858 1.00 27.02  ? 193 SER   B CB  1 
ATOM   3162 O OG  . SER   B 1 118 ? -0.232  -33.954 19.277 1.00 41.87  ? 193 SER   B OG  1 
ATOM   3163 N N   . LEU   B 1 119 ? 0.100   -34.703 15.879 1.00 38.53  ? 194 LEU   B N   1 
ATOM   3164 C CA  . LEU   B 1 119 ? -0.983  -34.576 14.910 1.00 33.63  ? 194 LEU   B CA  1 
ATOM   3165 C C   . LEU   B 1 119 ? -2.302  -34.225 15.589 1.00 35.10  ? 194 LEU   B C   1 
ATOM   3166 O O   . LEU   B 1 119 ? -3.167  -33.587 14.978 1.00 40.75  ? 194 LEU   B O   1 
ATOM   3167 C CB  . LEU   B 1 119 ? -1.118  -35.877 14.117 1.00 32.89  ? 194 LEU   B CB  1 
ATOM   3168 C CG  . LEU   B 1 119 ? -2.091  -35.905 12.945 1.00 34.25  ? 194 LEU   B CG  1 
ATOM   3169 C CD1 . LEU   B 1 119 ? -1.679  -34.893 11.897 1.00 37.70  ? 194 LEU   B CD1 1 
ATOM   3170 C CD2 . LEU   B 1 119 ? -2.164  -37.301 12.341 1.00 30.55  ? 194 LEU   B CD2 1 
ATOM   3171 N N   . GLN   B 1 120 ? -2.478  -34.639 16.846 1.00 32.36  ? 195 GLN   B N   1 
ATOM   3172 C CA  . GLN   B 1 120 ? -3.675  -34.269 17.595 1.00 26.95  ? 195 GLN   B CA  1 
ATOM   3173 C C   . GLN   B 1 120 ? -3.719  -32.770 17.855 1.00 37.27  ? 195 GLN   B C   1 
ATOM   3174 O O   . GLN   B 1 120 ? -4.768  -32.135 17.700 1.00 50.82  ? 195 GLN   B O   1 
ATOM   3175 C CB  . GLN   B 1 120 ? -3.716  -35.039 18.914 1.00 27.22  ? 195 GLN   B CB  1 
ATOM   3176 C CG  . GLN   B 1 120 ? -4.934  -34.766 19.774 1.00 33.08  ? 195 GLN   B CG  1 
ATOM   3177 C CD  . GLN   B 1 120 ? -4.873  -35.502 21.099 1.00 39.95  ? 195 GLN   B CD  1 
ATOM   3178 O OE1 . GLN   B 1 120 ? -3.795  -35.696 21.666 1.00 44.57  ? 195 GLN   B OE1 1 
ATOM   3179 N NE2 . GLN   B 1 120 ? -6.029  -35.924 21.597 1.00 52.32  ? 195 GLN   B NE2 1 
ATOM   3180 N N   . GLN   B 1 121 ? -2.589  -32.187 18.261 1.00 44.71  ? 196 GLN   B N   1 
ATOM   3181 C CA  . GLN   B 1 121 ? -2.553  -30.753 18.526 1.00 30.45  ? 196 GLN   B CA  1 
ATOM   3182 C C   . GLN   B 1 121 ? -2.719  -29.952 17.244 1.00 32.03  ? 196 GLN   B C   1 
ATOM   3183 O O   . GLN   B 1 121 ? -3.375  -28.904 17.242 1.00 50.88  ? 196 GLN   B O   1 
ATOM   3184 C CB  . GLN   B 1 121 ? -1.245  -30.380 19.223 1.00 30.14  ? 196 GLN   B CB  1 
ATOM   3185 C CG  . GLN   B 1 121 ? -1.061  -31.003 20.595 1.00 36.90  ? 196 GLN   B CG  1 
ATOM   3186 C CD  . GLN   B 1 121 ? 0.278   -30.652 21.216 1.00 38.79  ? 196 GLN   B CD  1 
ATOM   3187 O OE1 . GLN   B 1 121 ? 1.296   -30.576 20.525 1.00 57.58  ? 196 GLN   B OE1 1 
ATOM   3188 N NE2 . GLN   B 1 121 ? 0.284   -30.433 22.525 1.00 64.68  ? 196 GLN   B NE2 1 
ATOM   3189 N N   . HIS   B 1 122 ? -2.131  -30.421 16.143 1.00 38.20  ? 197 HIS   B N   1 
ATOM   3190 C CA  . HIS   B 1 122 ? -2.269  -29.706 14.880 1.00 37.84  ? 197 HIS   B CA  1 
ATOM   3191 C C   . HIS   B 1 122 ? -3.714  -29.702 14.398 1.00 37.62  ? 197 HIS   B C   1 
ATOM   3192 O O   . HIS   B 1 122 ? -4.185  -28.704 13.839 1.00 49.53  ? 197 HIS   B O   1 
ATOM   3193 C CB  . HIS   B 1 122 ? -1.356  -30.327 13.827 1.00 35.80  ? 197 HIS   B CB  1 
ATOM   3194 C CG  . HIS   B 1 122 ? -1.538  -29.754 12.459 1.00 48.15  ? 197 HIS   B CG  1 
ATOM   3195 N ND1 . HIS   B 1 122 ? -1.591  -28.398 12.222 1.00 61.94  ? 197 HIS   B ND1 1 
ATOM   3196 C CD2 . HIS   B 1 122 ? -1.682  -30.353 11.254 1.00 46.88  ? 197 HIS   B CD2 1 
ATOM   3197 C CE1 . HIS   B 1 122 ? -1.761  -28.185 10.930 1.00 52.31  ? 197 HIS   B CE1 1 
ATOM   3198 N NE2 . HIS   B 1 122 ? -1.818  -29.355 10.320 1.00 51.17  ? 197 HIS   B NE2 1 
ATOM   3199 N N   . CYS   B 1 123 ? -4.435  -30.806 14.598 1.00 38.43  ? 198 CYS   B N   1 
ATOM   3200 C CA  . CYS   B 1 123 ? -5.837  -30.841 14.192 1.00 43.27  ? 198 CYS   B CA  1 
ATOM   3201 C C   . CYS   B 1 123 ? -6.696  -30.007 15.124 1.00 39.40  ? 198 CYS   B C   1 
ATOM   3202 O O   . CYS   B 1 123 ? -7.602  -29.297 14.673 1.00 53.38  ? 198 CYS   B O   1 
ATOM   3203 C CB  . CYS   B 1 123 ? -6.339  -32.279 14.152 1.00 42.59  ? 198 CYS   B CB  1 
ATOM   3204 S SG  . CYS   B 1 123 ? -5.518  -33.244 12.894 1.00 56.43  ? 198 CYS   B SG  1 
ATOM   3205 N N   . GLU   B 1 124 ? -6.431  -30.089 16.429 1.00 39.22  ? 199 GLU   B N   1 
ATOM   3206 C CA  . GLU   B 1 124 ? -7.143  -29.247 17.383 1.00 31.73  ? 199 GLU   B CA  1 
ATOM   3207 C C   . GLU   B 1 124 ? -6.974  -27.772 17.042 1.00 36.46  ? 199 GLU   B C   1 
ATOM   3208 O O   . GLU   B 1 124 ? -7.934  -26.996 17.114 1.00 49.89  ? 199 GLU   B O   1 
ATOM   3209 C CB  . GLU   B 1 124 ? -6.649  -29.546 18.799 1.00 41.53  ? 199 GLU   B CB  1 
ATOM   3210 C CG  . GLU   B 1 124 ? -7.292  -28.714 19.904 1.00 72.75  ? 199 GLU   B CG  1 
ATOM   3211 C CD  . GLU   B 1 124 ? -6.851  -29.151 21.296 1.00 94.46  ? 199 GLU   B CD  1 
ATOM   3212 O OE1 . GLU   B 1 124 ? -6.543  -30.349 21.474 1.00 96.81  ? 199 GLU   B OE1 1 
ATOM   3213 O OE2 . GLU   B 1 124 ? -6.807  -28.298 22.209 1.00 76.07  ? 199 GLU   B OE2 1 
ATOM   3214 N N   . ALA   B 1 125 ? -5.762  -27.367 16.651 1.00 57.25  ? 200 ALA   B N   1 
ATOM   3215 C CA  . ALA   B 1 125 ? -5.540  -25.976 16.269 1.00 43.18  ? 200 ALA   B CA  1 
ATOM   3216 C C   . ALA   B 1 125 ? -6.139  -25.666 14.904 1.00 49.91  ? 200 ALA   B C   1 
ATOM   3217 O O   . ALA   B 1 125 ? -6.593  -24.539 14.669 1.00 42.38  ? 200 ALA   B O   1 
ATOM   3218 C CB  . ALA   B 1 125 ? -4.045  -25.658 16.274 1.00 50.84  ? 200 ALA   B CB  1 
ATOM   3219 N N   . TRP   B 1 126 ? -6.145  -26.640 13.989 1.00 41.58  ? 201 TRP   B N   1 
ATOM   3220 C CA  . TRP   B 1 126 ? -6.737  -26.398 12.679 1.00 43.26  ? 201 TRP   B CA  1 
ATOM   3221 C C   . TRP   B 1 126 ? -8.247  -26.236 12.776 1.00 37.61  ? 201 TRP   B C   1 
ATOM   3222 O O   . TRP   B 1 126 ? -8.844  -25.508 11.975 1.00 44.72  ? 201 TRP   B O   1 
ATOM   3223 C CB  . TRP   B 1 126 ? -6.375  -27.530 11.717 1.00 37.08  ? 201 TRP   B CB  1 
ATOM   3224 C CG  . TRP   B 1 126 ? -6.773  -27.254 10.304 1.00 39.68  ? 201 TRP   B CG  1 
ATOM   3225 C CD1 . TRP   B 1 126 ? -7.782  -27.850 9.606  1.00 50.18  ? 201 TRP   B CD1 1 
ATOM   3226 C CD2 . TRP   B 1 126 ? -6.177  -26.302 9.414  1.00 41.83  ? 201 TRP   B CD2 1 
ATOM   3227 N NE1 . TRP   B 1 126 ? -7.848  -27.331 8.335  1.00 52.35  ? 201 TRP   B NE1 1 
ATOM   3228 C CE2 . TRP   B 1 126 ? -6.874  -26.379 8.192  1.00 44.10  ? 201 TRP   B CE2 1 
ATOM   3229 C CE3 . TRP   B 1 126 ? -5.121  -25.394 9.532  1.00 38.49  ? 201 TRP   B CE3 1 
ATOM   3230 C CZ2 . TRP   B 1 126 ? -6.550  -25.583 7.097  1.00 48.80  ? 201 TRP   B CZ2 1 
ATOM   3231 C CZ3 . TRP   B 1 126 ? -4.800  -24.603 8.442  1.00 39.93  ? 201 TRP   B CZ3 1 
ATOM   3232 C CH2 . TRP   B 1 126 ? -5.512  -24.703 7.241  1.00 46.38  ? 201 TRP   B CH2 1 
ATOM   3233 N N   . GLY   B 1 127 ? -8.874  -26.890 13.751 1.00 41.64  ? 202 GLY   B N   1 
ATOM   3234 C CA  . GLY   B 1 127 ? -10.290 -26.679 14.005 1.00 40.80  ? 202 GLY   B CA  1 
ATOM   3235 C C   . GLY   B 1 127 ? -11.191 -27.074 12.861 1.00 39.33  ? 202 GLY   B C   1 
ATOM   3236 O O   . GLY   B 1 127 ? -12.298 -26.538 12.740 1.00 50.04  ? 202 GLY   B O   1 
ATOM   3237 N N   . ALA   B 1 128 ? -10.750 -27.999 12.016 1.00 40.93  ? 203 ALA   B N   1 
ATOM   3238 C CA  . ALA   B 1 128 ? -11.525 -28.430 10.858 1.00 53.10  ? 203 ALA   B CA  1 
ATOM   3239 C C   . ALA   B 1 128 ? -10.850 -29.662 10.268 1.00 51.15  ? 203 ALA   B C   1 
ATOM   3240 O O   . ALA   B 1 128 ? -9.853  -30.166 10.795 1.00 43.07  ? 203 ALA   B O   1 
ATOM   3241 C CB  . ALA   B 1 128 ? -11.652 -27.313 9.821  1.00 54.22  ? 203 ALA   B CB  1 
ATOM   3242 N N   . SER   B 1 129 ? -11.414 -30.153 9.170  1.00 51.79  ? 204 SER   B N   1 
ATOM   3243 C CA  . SER   B 1 129 ? -10.793 -31.253 8.449  1.00 41.72  ? 204 SER   B CA  1 
ATOM   3244 C C   . SER   B 1 129 ? -9.475  -30.786 7.849  1.00 43.03  ? 204 SER   B C   1 
ATOM   3245 O O   . SER   B 1 129 ? -9.406  -29.716 7.236  1.00 58.64  ? 204 SER   B O   1 
ATOM   3246 C CB  . SER   B 1 129 ? -11.722 -31.758 7.348  1.00 46.96  ? 204 SER   B CB  1 
ATOM   3247 O OG  . SER   B 1 129 ? -12.996 -32.089 7.870  1.00 68.12  ? 204 SER   B OG  1 
ATOM   3248 N N   . LEU   B 1 130 ? -8.429  -31.581 8.030  1.00 41.73  ? 205 LEU   B N   1 
ATOM   3249 C CA  . LEU   B 1 130 ? -7.144  -31.228 7.450  1.00 47.65  ? 205 LEU   B CA  1 
ATOM   3250 C C   . LEU   B 1 130 ? -7.225  -31.273 5.926  1.00 60.34  ? 205 LEU   B C   1 
ATOM   3251 O O   . LEU   B 1 130 ? -7.903  -32.140 5.365  1.00 57.31  ? 205 LEU   B O   1 
ATOM   3252 C CB  . LEU   B 1 130 ? -6.052  -32.174 7.938  1.00 40.13  ? 205 LEU   B CB  1 
ATOM   3253 C CG  . LEU   B 1 130 ? -5.543  -31.940 9.358  1.00 48.32  ? 205 LEU   B CG  1 
ATOM   3254 C CD1 . LEU   B 1 130 ? -4.303  -32.778 9.599  1.00 46.12  ? 205 LEU   B CD1 1 
ATOM   3255 C CD2 . LEU   B 1 130 ? -5.250  -30.468 9.582  1.00 50.02  ? 205 LEU   B CD2 1 
ATOM   3256 N N   . PRO   B 1 131 ? -6.560  -30.350 5.231  1.00 59.89  ? 206 PRO   B N   1 
ATOM   3257 C CA  . PRO   B 1 131 ? -6.504  -30.436 3.769  1.00 51.38  ? 206 PRO   B CA  1 
ATOM   3258 C C   . PRO   B 1 131 ? -5.916  -31.772 3.338  1.00 49.67  ? 206 PRO   B C   1 
ATOM   3259 O O   . PRO   B 1 131 ? -4.956  -32.269 3.931  1.00 56.68  ? 206 PRO   B O   1 
ATOM   3260 C CB  . PRO   B 1 131 ? -5.600  -29.263 3.378  1.00 58.38  ? 206 PRO   B CB  1 
ATOM   3261 C CG  . PRO   B 1 131 ? -5.710  -28.308 4.527  1.00 54.73  ? 206 PRO   B CG  1 
ATOM   3262 C CD  . PRO   B 1 131 ? -5.856  -29.164 5.747  1.00 50.70  ? 206 PRO   B CD  1 
ATOM   3263 N N   . GLU   B 1 132 ? -6.515  -32.359 2.301  1.00 49.51  ? 207 GLU   B N   1 
ATOM   3264 C CA  . GLU   B 1 132 ? -6.168  -33.726 1.931  1.00 41.73  ? 207 GLU   B CA  1 
ATOM   3265 C C   . GLU   B 1 132 ? -4.704  -33.855 1.525  1.00 42.21  ? 207 GLU   B C   1 
ATOM   3266 O O   . GLU   B 1 132 ? -4.103  -34.918 1.715  1.00 52.12  ? 207 GLU   B O   1 
ATOM   3267 C CB  . GLU   B 1 132 ? -7.081  -34.214 0.805  1.00 42.53  ? 207 GLU   B CB  1 
ATOM   3268 C CG  . GLU   B 1 132 ? -6.922  -35.695 0.498  1.00 58.99  ? 207 GLU   B CG  1 
ATOM   3269 C CD  . GLU   B 1 132 ? -8.090  -36.269 -0.278 1.00 71.60  ? 207 GLU   B CD  1 
ATOM   3270 O OE1 . GLU   B 1 132 ? -9.247  -35.896 0.017  1.00 66.43  ? 207 GLU   B OE1 1 
ATOM   3271 O OE2 . GLU   B 1 132 ? -7.850  -37.095 -1.183 1.00 82.69  ? 207 GLU   B OE2 1 
ATOM   3272 N N   . ALA   B 1 133 ? -4.112  -32.791 0.976  1.00 54.76  ? 208 ALA   B N   1 
ATOM   3273 C CA  . ALA   B 1 133 ? -2.701  -32.845 0.607  1.00 47.11  ? 208 ALA   B CA  1 
ATOM   3274 C C   . ALA   B 1 133 ? -1.825  -33.144 1.818  1.00 43.85  ? 208 ALA   B C   1 
ATOM   3275 O O   . ALA   B 1 133 ? -0.875  -33.929 1.726  1.00 61.96  ? 208 ALA   B O   1 
ATOM   3276 C CB  . ALA   B 1 133 ? -2.281  -31.532 -0.055 1.00 53.94  ? 208 ALA   B CB  1 
ATOM   3277 N N   . GLN   B 1 134 ? -2.135  -32.538 2.966  1.00 51.63  ? 209 GLN   B N   1 
ATOM   3278 C CA  . GLN   B 1 134 ? -1.385  -32.845 4.180  1.00 45.19  ? 209 GLN   B CA  1 
ATOM   3279 C C   . GLN   B 1 134 ? -1.592  -34.294 4.601  1.00 47.29  ? 209 GLN   B C   1 
ATOM   3280 O O   . GLN   B 1 134 ? -0.664  -34.945 5.095  1.00 58.24  ? 209 GLN   B O   1 
ATOM   3281 C CB  . GLN   B 1 134 ? -1.799  -31.910 5.316  1.00 50.14  ? 209 GLN   B CB  1 
ATOM   3282 C CG  . GLN   B 1 134 ? -1.374  -30.459 5.159  1.00 52.69  ? 209 GLN   B CG  1 
ATOM   3283 C CD  . GLN   B 1 134 ? -1.525  -29.678 6.456  1.00 63.95  ? 209 GLN   B CD  1 
ATOM   3284 O OE1 . GLN   B 1 134 ? -2.090  -28.584 6.477  1.00 95.65  ? 209 GLN   B OE1 1 
ATOM   3285 N NE2 . GLN   B 1 134 ? -1.016  -30.242 7.547  1.00 61.54  ? 209 GLN   B NE2 1 
ATOM   3286 N N   . VAL   B 1 135 ? -2.807  -34.815 4.413  1.00 42.11  ? 210 VAL   B N   1 
ATOM   3287 C CA  . VAL   B 1 135 ? -3.130  -36.154 4.899  1.00 37.57  ? 210 VAL   B CA  1 
ATOM   3288 C C   . VAL   B 1 135 ? -2.285  -37.203 4.186  1.00 40.82  ? 210 VAL   B C   1 
ATOM   3289 O O   . VAL   B 1 135 ? -1.817  -38.167 4.803  1.00 51.62  ? 210 VAL   B O   1 
ATOM   3290 C CB  . VAL   B 1 135 ? -4.635  -36.428 4.730  1.00 48.40  ? 210 VAL   B CB  1 
ATOM   3291 C CG1 . VAL   B 1 135 ? -4.983  -37.794 5.275  1.00 52.18  ? 210 VAL   B CG1 1 
ATOM   3292 C CG2 . VAL   B 1 135 ? -5.449  -35.350 5.431  1.00 42.57  ? 210 VAL   B CG2 1 
ATOM   3293 N N   . TRP   B 1 136 ? -2.066  -37.030 2.882  1.00 41.18  ? 211 TRP   B N   1 
ATOM   3294 C CA  . TRP   B 1 136 ? -1.276  -38.004 2.137  1.00 47.56  ? 211 TRP   B CA  1 
ATOM   3295 C C   . TRP   B 1 136 ? 0.162   -38.051 2.636  1.00 48.79  ? 211 TRP   B C   1 
ATOM   3296 O O   . TRP   B 1 136 ? 0.767   -39.128 2.714  1.00 56.28  ? 211 TRP   B O   1 
ATOM   3297 C CB  . TRP   B 1 136 ? -1.319  -37.680 0.646  1.00 45.03  ? 211 TRP   B CB  1 
ATOM   3298 C CG  . TRP   B 1 136 ? -2.639  -37.982 0.005  1.00 48.45  ? 211 TRP   B CG  1 
ATOM   3299 C CD1 . TRP   B 1 136 ? -3.557  -37.079 -0.454 1.00 42.68  ? 211 TRP   B CD1 1 
ATOM   3300 C CD2 . TRP   B 1 136 ? -3.191  -39.279 -0.250 1.00 46.82  ? 211 TRP   B CD2 1 
ATOM   3301 N NE1 . TRP   B 1 136 ? -4.643  -37.737 -0.983 1.00 48.08  ? 211 TRP   B NE1 1 
ATOM   3302 C CE2 . TRP   B 1 136 ? -4.443  -39.088 -0.867 1.00 49.06  ? 211 TRP   B CE2 1 
ATOM   3303 C CE3 . TRP   B 1 136 ? -2.746  -40.583 -0.017 1.00 50.69  ? 211 TRP   B CE3 1 
ATOM   3304 C CZ2 . TRP   B 1 136 ? -5.254  -40.152 -1.255 1.00 51.60  ? 211 TRP   B CZ2 1 
ATOM   3305 C CZ3 . TRP   B 1 136 ? -3.553  -41.639 -0.401 1.00 54.30  ? 211 TRP   B CZ3 1 
ATOM   3306 C CH2 . TRP   B 1 136 ? -4.794  -41.416 -1.014 1.00 49.33  ? 211 TRP   B CH2 1 
ATOM   3307 N N   . GLY   B 1 137 ? 0.732   -36.894 2.974  1.00 38.40  ? 212 GLY   B N   1 
ATOM   3308 C CA  . GLY   B 1 137 ? 2.090   -36.884 3.488  1.00 34.25  ? 212 GLY   B CA  1 
ATOM   3309 C C   . GLY   B 1 137 ? 2.194   -37.566 4.835  1.00 33.51  ? 212 GLY   B C   1 
ATOM   3310 O O   . GLY   B 1 137 ? 3.123   -38.340 5.080  1.00 58.11  ? 212 GLY   B O   1 
ATOM   3311 N N   . TYR   B 1 138 ? 1.234   -37.299 5.724  1.00 37.31  ? 213 TYR   B N   1 
ATOM   3312 C CA  . TYR   B 1 138 ? 1.247   -37.939 7.034  1.00 37.75  ? 213 TYR   B CA  1 
ATOM   3313 C C   . TYR   B 1 138 ? 0.915   -39.417 6.923  1.00 42.23  ? 213 TYR   B C   1 
ATOM   3314 O O   . TYR   B 1 138 ? 1.447   -40.232 7.686  1.00 50.66  ? 213 TYR   B O   1 
ATOM   3315 C CB  . TYR   B 1 138 ? 0.262   -37.238 7.977  1.00 37.72  ? 213 TYR   B CB  1 
ATOM   3316 C CG  . TYR   B 1 138 ? 0.542   -35.765 8.184  1.00 41.29  ? 213 TYR   B CG  1 
ATOM   3317 C CD1 . TYR   B 1 138 ? 1.834   -35.262 8.078  1.00 43.51  ? 213 TYR   B CD1 1 
ATOM   3318 C CD2 . TYR   B 1 138 ? -0.484  -34.876 8.477  1.00 42.58  ? 213 TYR   B CD2 1 
ATOM   3319 C CE1 . TYR   B 1 138 ? 2.097   -33.911 8.262  1.00 46.83  ? 213 TYR   B CE1 1 
ATOM   3320 C CE2 . TYR   B 1 138 ? -0.231  -33.521 8.662  1.00 45.55  ? 213 TYR   B CE2 1 
ATOM   3321 C CZ  . TYR   B 1 138 ? 1.063   -33.046 8.553  1.00 50.77  ? 213 TYR   B CZ  1 
ATOM   3322 O OH  . TYR   B 1 138 ? 1.329   -31.705 8.734  1.00 52.26  ? 213 TYR   B OH  1 
ATOM   3323 N N   . LEU   B 1 139 ? 0.044   -39.781 5.984  1.00 39.05  ? 214 LEU   B N   1 
ATOM   3324 C CA  . LEU   B 1 139 ? -0.276  -41.190 5.790  1.00 36.99  ? 214 LEU   B CA  1 
ATOM   3325 C C   . LEU   B 1 139 ? 0.932   -41.958 5.266  1.00 43.61  ? 214 LEU   B C   1 
ATOM   3326 O O   . LEU   B 1 139 ? 1.236   -43.055 5.750  1.00 54.16  ? 214 LEU   B O   1 
ATOM   3327 C CB  . LEU   B 1 139 ? -1.461  -41.331 4.834  1.00 50.74  ? 214 LEU   B CB  1 
ATOM   3328 C CG  . LEU   B 1 139 ? -1.833  -42.744 4.372  1.00 37.96  ? 214 LEU   B CG  1 
ATOM   3329 C CD1 . LEU   B 1 139 ? -2.229  -43.608 5.547  1.00 33.86  ? 214 LEU   B CD1 1 
ATOM   3330 C CD2 . LEU   B 1 139 ? -2.963  -42.682 3.366  1.00 44.21  ? 214 LEU   B CD2 1 
ATOM   3331 N N   . ARG   B 1 140 ? 1.636   -41.397 4.284  1.00 37.41  ? 215 ARG   B N   1 
ATOM   3332 C CA  . ARG   B 1 140 ? 2.771   -42.105 3.701  1.00 35.21  ? 215 ARG   B CA  1 
ATOM   3333 C C   . ARG   B 1 140 ? 3.894   -42.280 4.716  1.00 41.29  ? 215 ARG   B C   1 
ATOM   3334 O O   . ARG   B 1 140 ? 4.414   -43.387 4.897  1.00 52.39  ? 215 ARG   B O   1 
ATOM   3335 C CB  . ARG   B 1 140 ? 3.277   -41.369 2.463  1.00 28.73  ? 215 ARG   B CB  1 
ATOM   3336 C CG  . ARG   B 1 140 ? 4.533   -41.995 1.896  1.00 50.75  ? 215 ARG   B CG  1 
ATOM   3337 C CD  . ARG   B 1 140 ? 4.917   -41.431 0.543  1.00 54.87  ? 215 ARG   B CD  1 
ATOM   3338 N NE  . ARG   B 1 140 ? 5.870   -42.308 -0.128 1.00 76.55  ? 215 ARG   B NE  1 
ATOM   3339 C CZ  . ARG   B 1 140 ? 7.179   -42.299 0.089  1.00 78.20  ? 215 ARG   B CZ  1 
ATOM   3340 N NH1 . ARG   B 1 140 ? 7.735   -41.444 0.933  1.00 84.65  ? 215 ARG   B NH1 1 
ATOM   3341 N NH2 . ARG   B 1 140 ? 7.949   -43.170 -0.556 1.00 76.14  ? 215 ARG   B NH2 1 
ATOM   3342 N N   . ASP   B 1 141 ? 4.282   -41.195 5.391  1.00 42.44  ? 216 ASP   B N   1 
ATOM   3343 C CA  . ASP   B 1 141 ? 5.406   -41.270 6.319  1.00 51.06  ? 216 ASP   B CA  1 
ATOM   3344 C C   . ASP   B 1 141 ? 5.102   -42.201 7.486  1.00 43.42  ? 216 ASP   B C   1 
ATOM   3345 O O   . ASP   B 1 141 ? 5.981   -42.944 7.939  1.00 54.21  ? 216 ASP   B O   1 
ATOM   3346 C CB  . ASP   B 1 141 ? 5.771   -39.873 6.819  1.00 46.70  ? 216 ASP   B CB  1 
ATOM   3347 C CG  . ASP   B 1 141 ? 6.587   -39.090 5.808  1.00 70.16  ? 216 ASP   B CG  1 
ATOM   3348 O OD1 . ASP   B 1 141 ? 6.984   -39.678 4.779  1.00 90.04  ? 216 ASP   B OD1 1 
ATOM   3349 O OD2 . ASP   B 1 141 ? 6.834   -37.889 6.039  1.00 82.30  ? 216 ASP   B OD2 1 
ATOM   3350 N N   . THR   B 1 142 ? 3.863   -42.184 7.982  1.00 40.42  ? 217 THR   B N   1 
ATOM   3351 C CA  . THR   B 1 142 ? 3.500   -43.125 9.035  1.00 37.44  ? 217 THR   B CA  1 
ATOM   3352 C C   . THR   B 1 142 ? 3.477   -44.561 8.524  1.00 50.05  ? 217 THR   B C   1 
ATOM   3353 O O   . THR   B 1 142 ? 3.807   -45.489 9.273  1.00 46.41  ? 217 THR   B O   1 
ATOM   3354 C CB  . THR   B 1 142 ? 2.149   -42.754 9.635  1.00 39.48  ? 217 THR   B CB  1 
ATOM   3355 O OG1 . THR   B 1 142 ? 2.162   -41.370 10.013 1.00 44.62  ? 217 THR   B OG1 1 
ATOM   3356 C CG2 . THR   B 1 142 ? 1.885   -43.590 10.867 1.00 31.67  ? 217 THR   B CG2 1 
ATOM   3357 N N   . LEU   B 1 143 ? 3.095   -44.767 7.260  1.00 38.44  ? 218 LEU   B N   1 
ATOM   3358 C CA  . LEU   B 1 143 ? 3.181   -46.103 6.677  1.00 28.12  ? 218 LEU   B CA  1 
ATOM   3359 C C   . LEU   B 1 143 ? 4.633   -46.550 6.546  1.00 38.39  ? 218 LEU   B C   1 
ATOM   3360 O O   . LEU   B 1 143 ? 4.946   -47.730 6.749  1.00 46.40  ? 218 LEU   B O   1 
ATOM   3361 C CB  . LEU   B 1 143 ? 2.483   -46.134 5.316  1.00 34.08  ? 218 LEU   B CB  1 
ATOM   3362 C CG  . LEU   B 1 143 ? 0.956   -46.235 5.315  1.00 34.10  ? 218 LEU   B CG  1 
ATOM   3363 C CD1 . LEU   B 1 143 ? 0.412   -46.073 3.911  1.00 29.58  ? 218 LEU   B CD1 1 
ATOM   3364 C CD2 . LEU   B 1 143 ? 0.498   -47.559 5.898  1.00 26.65  ? 218 LEU   B CD2 1 
ATOM   3365 N N   . LEU   B 1 144 ? 5.534   -45.622 6.209  1.00 34.52  ? 219 LEU   B N   1 
ATOM   3366 C CA  . LEU   B 1 144 ? 6.954   -45.957 6.156  1.00 37.92  ? 219 LEU   B CA  1 
ATOM   3367 C C   . LEU   B 1 144 ? 7.466   -46.387 7.525  1.00 38.00  ? 219 LEU   B C   1 
ATOM   3368 O O   . LEU   B 1 144 ? 8.300   -47.293 7.629  1.00 51.97  ? 219 LEU   B O   1 
ATOM   3369 C CB  . LEU   B 1 144 ? 7.758   -44.766 5.632  1.00 39.38  ? 219 LEU   B CB  1 
ATOM   3370 C CG  . LEU   B 1 144 ? 7.623   -44.412 4.150  1.00 39.89  ? 219 LEU   B CG  1 
ATOM   3371 C CD1 . LEU   B 1 144 ? 8.381   -43.138 3.831  1.00 45.02  ? 219 LEU   B CD1 1 
ATOM   3372 C CD2 . LEU   B 1 144 ? 8.132   -45.544 3.281  1.00 44.34  ? 219 LEU   B CD2 1 
ATOM   3373 N N   . ALA   B 1 145 ? 6.976   -45.749 8.591  1.00 41.86  ? 220 ALA   B N   1 
ATOM   3374 C CA  . ALA   B 1 145 ? 7.359   -46.158 9.938  1.00 39.60  ? 220 ALA   B CA  1 
ATOM   3375 C C   . ALA   B 1 145 ? 6.768   -47.517 10.287 1.00 43.96  ? 220 ALA   B C   1 
ATOM   3376 O O   . ALA   B 1 145 ? 7.466   -48.384 10.829 1.00 47.85  ? 220 ALA   B O   1 
ATOM   3377 C CB  . ALA   B 1 145 ? 6.918   -45.106 10.956 1.00 36.94  ? 220 ALA   B CB  1 
ATOM   3378 N N   . LEU   B 1 146 ? 5.479   -47.717 9.998  1.00 45.08  ? 221 LEU   B N   1 
ATOM   3379 C CA  . LEU   B 1 146 ? 4.856   -49.009 10.268 1.00 36.42  ? 221 LEU   B CA  1 
ATOM   3380 C C   . LEU   B 1 146 ? 5.517   -50.118 9.458  1.00 42.72  ? 221 LEU   B C   1 
ATOM   3381 O O   . LEU   B 1 146 ? 5.709   -51.232 9.959  1.00 52.83  ? 221 LEU   B O   1 
ATOM   3382 C CB  . LEU   B 1 146 ? 3.358   -48.951 9.970  1.00 34.41  ? 221 LEU   B CB  1 
ATOM   3383 C CG  . LEU   B 1 146 ? 2.504   -48.120 10.927 1.00 30.08  ? 221 LEU   B CG  1 
ATOM   3384 C CD1 . LEU   B 1 146 ? 1.049   -48.196 10.526 1.00 32.44  ? 221 LEU   B CD1 1 
ATOM   3385 C CD2 . LEU   B 1 146 ? 2.675   -48.608 12.350 1.00 29.81  ? 221 LEU   B CD2 1 
ATOM   3386 N N   . ALA   B 1 147 ? 5.875   -49.834 8.203  1.00 38.65  ? 222 ALA   B N   1 
ATOM   3387 C CA  . ALA   B 1 147 ? 6.590   -50.828 7.410  1.00 31.53  ? 222 ALA   B CA  1 
ATOM   3388 C C   . ALA   B 1 147 ? 7.931   -51.172 8.036  1.00 28.67  ? 222 ALA   B C   1 
ATOM   3389 O O   . ALA   B 1 147 ? 8.393   -52.313 7.933  1.00 52.26  ? 222 ALA   B O   1 
ATOM   3390 C CB  . ALA   B 1 147 ? 6.786   -50.328 5.979  1.00 35.65  ? 222 ALA   B CB  1 
ATOM   3391 N N   . HIS   B 1 148 ? 8.567   -50.202 8.694  1.00 43.79  ? 223 HIS   B N   1 
ATOM   3392 C CA  . HIS   B 1 148 ? 9.827   -50.476 9.375  1.00 47.48  ? 223 HIS   B CA  1 
ATOM   3393 C C   . HIS   B 1 148 ? 9.601   -51.313 10.628 1.00 40.02  ? 223 HIS   B C   1 
ATOM   3394 O O   . HIS   B 1 148 ? 10.361  -52.247 10.903 1.00 47.24  ? 223 HIS   B O   1 
ATOM   3395 C CB  . HIS   B 1 148 ? 10.523  -49.161 9.720  1.00 50.43  ? 223 HIS   B CB  1 
ATOM   3396 C CG  . HIS   B 1 148 ? 11.813  -49.333 10.457 1.00 42.78  ? 223 HIS   B CG  1 
ATOM   3397 N ND1 . HIS   B 1 148 ? 12.955  -49.818 9.858  1.00 44.78  ? 223 HIS   B ND1 1 
ATOM   3398 C CD2 . HIS   B 1 148 ? 12.143  -49.077 11.745 1.00 40.46  ? 223 HIS   B CD2 1 
ATOM   3399 C CE1 . HIS   B 1 148 ? 13.933  -49.857 10.745 1.00 38.65  ? 223 HIS   B CE1 1 
ATOM   3400 N NE2 . HIS   B 1 148 ? 13.467  -49.412 11.898 1.00 43.59  ? 223 HIS   B NE2 1 
ATOM   3401 N N   . LEU   B 1 149 ? 8.560   -50.994 11.401 1.00 43.99  ? 224 LEU   B N   1 
ATOM   3402 C CA  . LEU   B 1 149 ? 8.271   -51.772 12.601 1.00 36.66  ? 224 LEU   B CA  1 
ATOM   3403 C C   . LEU   B 1 149 ? 7.823   -53.182 12.249 1.00 39.11  ? 224 LEU   B C   1 
ATOM   3404 O O   . LEU   B 1 149 ? 8.265   -54.154 12.872 1.00 52.18  ? 224 LEU   B O   1 
ATOM   3405 C CB  . LEU   B 1 149 ? 7.198   -51.077 13.438 1.00 27.45  ? 224 LEU   B CB  1 
ATOM   3406 C CG  . LEU   B 1 149 ? 7.635   -50.057 14.491 1.00 42.45  ? 224 LEU   B CG  1 
ATOM   3407 C CD1 . LEU   B 1 149 ? 8.392   -48.886 13.875 1.00 39.67  ? 224 LEU   B CD1 1 
ATOM   3408 C CD2 . LEU   B 1 149 ? 6.422   -49.565 15.261 1.00 43.34  ? 224 LEU   B CD2 1 
ATOM   3409 N N   . HIS   B 1 150 ? 6.942   -53.314 11.256 1.00 45.79  ? 225 HIS   B N   1 
ATOM   3410 C CA  . HIS   B 1 150 ? 6.372   -54.618 10.945 1.00 34.19  ? 225 HIS   B CA  1 
ATOM   3411 C C   . HIS   B 1 150 ? 7.392   -55.543 10.295 1.00 41.50  ? 225 HIS   B C   1 
ATOM   3412 O O   . HIS   B 1 150 ? 7.331   -56.762 10.494 1.00 61.24  ? 225 HIS   B O   1 
ATOM   3413 C CB  . HIS   B 1 150 ? 5.146   -54.448 10.052 1.00 36.60  ? 225 HIS   B CB  1 
ATOM   3414 C CG  . HIS   B 1 150 ? 4.025   -53.708 10.713 1.00 37.28  ? 225 HIS   B CG  1 
ATOM   3415 N ND1 . HIS   B 1 150 ? 2.924   -53.248 10.023 1.00 33.47  ? 225 HIS   B ND1 1 
ATOM   3416 C CD2 . HIS   B 1 150 ? 3.836   -53.349 12.005 1.00 31.73  ? 225 HIS   B CD2 1 
ATOM   3417 C CE1 . HIS   B 1 150 ? 2.105   -52.638 10.862 1.00 48.09  ? 225 HIS   B CE1 1 
ATOM   3418 N NE2 . HIS   B 1 150 ? 2.635   -52.686 12.071 1.00 36.17  ? 225 HIS   B NE2 1 
ATOM   3419 N N   . SER   B 1 151 ? 8.340   -54.996 9.530  1.00 44.66  ? 226 SER   B N   1 
ATOM   3420 C CA  . SER   B 1 151 ? 9.380   -55.834 8.942  1.00 39.76  ? 226 SER   B CA  1 
ATOM   3421 C C   . SER   B 1 151 ? 10.305  -56.432 9.991  1.00 40.95  ? 226 SER   B C   1 
ATOM   3422 O O   . SER   B 1 151 ? 11.146  -57.270 9.645  1.00 55.11  ? 226 SER   B O   1 
ATOM   3423 C CB  . SER   B 1 151 ? 10.205  -55.035 7.935  1.00 37.12  ? 226 SER   B CB  1 
ATOM   3424 O OG  . SER   B 1 151 ? 10.892  -53.979 8.580  1.00 62.61  ? 226 SER   B OG  1 
ATOM   3425 N N   . GLN   B 1 152 ? 10.180  -56.015 11.249 1.00 45.36  ? 227 GLN   B N   1 
ATOM   3426 C CA  . GLN   B 1 152 ? 10.941  -56.582 12.353 1.00 45.37  ? 227 GLN   B CA  1 
ATOM   3427 C C   . GLN   B 1 152 ? 10.060  -57.357 13.322 1.00 42.41  ? 227 GLN   B C   1 
ATOM   3428 O O   . GLN   B 1 152 ? 10.517  -57.709 14.414 1.00 49.21  ? 227 GLN   B O   1 
ATOM   3429 C CB  . GLN   B 1 152 ? 11.685  -55.479 13.104 1.00 47.91  ? 227 GLN   B CB  1 
ATOM   3430 C CG  . GLN   B 1 152 ? 12.533  -54.596 12.219 1.00 57.03  ? 227 GLN   B CG  1 
ATOM   3431 C CD  . GLN   B 1 152 ? 13.337  -53.592 13.014 1.00 54.30  ? 227 GLN   B CD  1 
ATOM   3432 O OE1 . GLN   B 1 152 ? 14.393  -53.916 13.557 1.00 65.48  ? 227 GLN   B OE1 1 
ATOM   3433 N NE2 . GLN   B 1 152 ? 12.839  -52.363 13.090 1.00 53.99  ? 227 GLN   B NE2 1 
ATOM   3434 N N   . GLY   B 1 153 ? 8.809   -57.620 12.957 1.00 45.32  ? 228 GLY   B N   1 
ATOM   3435 C CA  . GLY   B 1 153 ? 7.922   -58.353 13.838 1.00 41.09  ? 228 GLY   B CA  1 
ATOM   3436 C C   . GLY   B 1 153 ? 7.454   -57.557 15.030 1.00 45.39  ? 228 GLY   B C   1 
ATOM   3437 O O   . GLY   B 1 153 ? 7.153   -58.137 16.078 1.00 52.91  ? 228 GLY   B O   1 
ATOM   3438 N N   . LEU   B 1 154 ? 7.394   -56.237 14.903 1.00 48.19  ? 229 LEU   B N   1 
ATOM   3439 C CA  . LEU   B 1 154 ? 6.960   -55.356 15.975 1.00 42.43  ? 229 LEU   B CA  1 
ATOM   3440 C C   . LEU   B 1 154 ? 5.580   -54.804 15.654 1.00 39.25  ? 229 LEU   B C   1 
ATOM   3441 O O   . LEU   B 1 154 ? 5.275   -54.511 14.494 1.00 46.37  ? 229 LEU   B O   1 
ATOM   3442 C CB  . LEU   B 1 154 ? 7.948   -54.200 16.166 1.00 35.74  ? 229 LEU   B CB  1 
ATOM   3443 C CG  . LEU   B 1 154 ? 9.430   -54.567 16.281 1.00 40.64  ? 229 LEU   B CG  1 
ATOM   3444 C CD1 . LEU   B 1 154 ? 10.275  -53.317 16.455 1.00 33.26  ? 229 LEU   B CD1 1 
ATOM   3445 C CD2 . LEU   B 1 154 ? 9.674   -55.545 17.423 1.00 33.23  ? 229 LEU   B CD2 1 
ATOM   3446 N N   . VAL   B 1 155 ? 4.750   -54.661 16.682 1.00 41.89  ? 230 VAL   B N   1 
ATOM   3447 C CA  . VAL   B 1 155 ? 3.423   -54.070 16.554 1.00 38.79  ? 230 VAL   B CA  1 
ATOM   3448 C C   . VAL   B 1 155 ? 3.366   -52.861 17.476 1.00 44.49  ? 230 VAL   B C   1 
ATOM   3449 O O   . VAL   B 1 155 ? 3.631   -52.979 18.678 1.00 45.80  ? 230 VAL   B O   1 
ATOM   3450 C CB  . VAL   B 1 155 ? 2.314   -55.076 16.898 1.00 37.05  ? 230 VAL   B CB  1 
ATOM   3451 C CG1 . VAL   B 1 155 ? 0.963   -54.547 16.459 1.00 41.93  ? 230 VAL   B CG1 1 
ATOM   3452 C CG2 . VAL   B 1 155 ? 2.600   -56.412 16.245 1.00 46.09  ? 230 VAL   B CG2 1 
ATOM   3453 N N   . HIS   B 1 156 ? 3.023   -51.699 16.916 1.00 31.19  ? 231 HIS   B N   1 
ATOM   3454 C CA  . HIS   B 1 156 ? 2.996   -50.476 17.712 1.00 27.95  ? 231 HIS   B CA  1 
ATOM   3455 C C   . HIS   B 1 156 ? 1.869   -50.513 18.738 1.00 34.90  ? 231 HIS   B C   1 
ATOM   3456 O O   . HIS   B 1 156 ? 2.070   -50.176 19.911 1.00 42.27  ? 231 HIS   B O   1 
ATOM   3457 C CB  . HIS   B 1 156 ? 2.861   -49.264 16.790 1.00 29.16  ? 231 HIS   B CB  1 
ATOM   3458 C CG  . HIS   B 1 156 ? 3.101   -47.956 17.475 1.00 32.06  ? 231 HIS   B CG  1 
ATOM   3459 N ND1 . HIS   B 1 156 ? 2.125   -47.307 18.201 1.00 37.41  ? 231 HIS   B ND1 1 
ATOM   3460 C CD2 . HIS   B 1 156 ? 4.204   -47.172 17.541 1.00 39.40  ? 231 HIS   B CD2 1 
ATOM   3461 C CE1 . HIS   B 1 156 ? 2.617   -46.181 18.688 1.00 30.89  ? 231 HIS   B CE1 1 
ATOM   3462 N NE2 . HIS   B 1 156 ? 3.876   -46.075 18.301 1.00 46.25  ? 231 HIS   B NE2 1 
ATOM   3463 N N   . LEU   B 1 157 ? 0.672   -50.918 18.311 1.00 36.68  ? 232 LEU   B N   1 
ATOM   3464 C CA  . LEU   B 1 157 ? -0.506  -51.102 19.157 1.00 38.40  ? 232 LEU   B CA  1 
ATOM   3465 C C   . LEU   B 1 157 ? -1.038  -49.802 19.746 1.00 32.43  ? 232 LEU   B C   1 
ATOM   3466 O O   . LEU   B 1 157 ? -1.924  -49.842 20.609 1.00 45.49  ? 232 LEU   B O   1 
ATOM   3467 C CB  . LEU   B 1 157 ? -0.239  -52.096 20.294 1.00 35.17  ? 232 LEU   B CB  1 
ATOM   3468 C CG  . LEU   B 1 157 ? -0.133  -53.572 19.908 1.00 35.42  ? 232 LEU   B CG  1 
ATOM   3469 C CD1 . LEU   B 1 157 ? 0.119   -54.411 21.146 1.00 37.83  ? 232 LEU   B CD1 1 
ATOM   3470 C CD2 . LEU   B 1 157 ? -1.394  -54.033 19.186 1.00 30.02  ? 232 LEU   B CD2 1 
ATOM   3471 N N   . ASP   B 1 158 ? -0.547  -48.649 19.306 1.00 34.19  ? 233 ASP   B N   1 
ATOM   3472 C CA  . ASP   B 1 158 ? -1.079  -47.379 19.787 1.00 39.33  ? 233 ASP   B CA  1 
ATOM   3473 C C   . ASP   B 1 158 ? -0.835  -46.295 18.744 1.00 41.05  ? 233 ASP   B C   1 
ATOM   3474 O O   . ASP   B 1 158 ? -0.317  -45.217 19.040 1.00 46.72  ? 233 ASP   B O   1 
ATOM   3475 C CB  . ASP   B 1 158 ? -0.471  -47.007 21.138 1.00 44.85  ? 233 ASP   B CB  1 
ATOM   3476 C CG  . ASP   B 1 158 ? -1.396  -46.142 21.974 1.00 62.77  ? 233 ASP   B CG  1 
ATOM   3477 O OD1 . ASP   B 1 158 ? -2.587  -46.501 22.113 1.00 69.43  ? 233 ASP   B OD1 1 
ATOM   3478 O OD2 . ASP   B 1 158 ? -0.931  -45.113 22.509 1.00 66.33  ? 233 ASP   B OD2 1 
ATOM   3479 N N   . VAL   B 1 159 ? -1.207  -46.578 17.499 1.00 34.50  ? 234 VAL   B N   1 
ATOM   3480 C CA  . VAL   B 1 159 ? -1.086  -45.606 16.420 1.00 39.41  ? 234 VAL   B CA  1 
ATOM   3481 C C   . VAL   B 1 159 ? -2.319  -44.710 16.461 1.00 36.69  ? 234 VAL   B C   1 
ATOM   3482 O O   . VAL   B 1 159 ? -3.427  -45.147 16.147 1.00 56.10  ? 234 VAL   B O   1 
ATOM   3483 C CB  . VAL   B 1 159 ? -0.940  -46.289 15.058 1.00 33.00  ? 234 VAL   B CB  1 
ATOM   3484 C CG1 . VAL   B 1 159 ? -0.984  -45.258 13.947 1.00 36.91  ? 234 VAL   B CG1 1 
ATOM   3485 C CG2 . VAL   B 1 159 ? 0.358   -47.076 15.005 1.00 36.98  ? 234 VAL   B CG2 1 
ATOM   3486 N N   . LYS   B 1 160 ? -2.128  -43.460 16.861 1.00 45.99  ? 235 LYS   B N   1 
ATOM   3487 C CA  . LYS   B 1 160 ? -3.212  -42.498 16.977 1.00 31.42  ? 235 LYS   B CA  1 
ATOM   3488 C C   . LYS   B 1 160 ? -2.620  -41.105 16.844 1.00 38.63  ? 235 LYS   B C   1 
ATOM   3489 O O   . LYS   B 1 160 ? -1.400  -40.935 16.956 1.00 37.68  ? 235 LYS   B O   1 
ATOM   3490 C CB  . LYS   B 1 160 ? -3.960  -42.658 18.308 1.00 31.26  ? 235 LYS   B CB  1 
ATOM   3491 C CG  . LYS   B 1 160 ? -3.102  -42.544 19.549 1.00 26.02  ? 235 LYS   B CG  1 
ATOM   3492 C CD  . LYS   B 1 160 ? -3.966  -42.679 20.792 1.00 41.29  ? 235 LYS   B CD  1 
ATOM   3493 C CE  . LYS   B 1 160 ? -3.133  -42.721 22.060 1.00 45.57  ? 235 LYS   B CE  1 
ATOM   3494 N NZ  . LYS   B 1 160 ? -3.984  -42.965 23.258 1.00 57.28  ? 235 LYS   B NZ  1 
ATOM   3495 N N   . PRO   B 1 161 ? -3.451  -40.087 16.583 1.00 43.57  ? 236 PRO   B N   1 
ATOM   3496 C CA  . PRO   B 1 161 ? -2.894  -38.743 16.349 1.00 27.33  ? 236 PRO   B CA  1 
ATOM   3497 C C   . PRO   B 1 161 ? -2.044  -38.223 17.490 1.00 28.60  ? 236 PRO   B C   1 
ATOM   3498 O O   . PRO   B 1 161 ? -1.169  -37.381 17.256 1.00 43.24  ? 236 PRO   B O   1 
ATOM   3499 C CB  . PRO   B 1 161 ? -4.146  -37.880 16.143 1.00 33.71  ? 236 PRO   B CB  1 
ATOM   3500 C CG  . PRO   B 1 161 ? -5.162  -38.827 15.611 1.00 39.88  ? 236 PRO   B CG  1 
ATOM   3501 C CD  . PRO   B 1 161 ? -4.905  -40.122 16.332 1.00 42.05  ? 236 PRO   B CD  1 
ATOM   3502 N N   . ALA   B 1 162 ? -2.269  -38.689 18.719 1.00 31.08  ? 237 ALA   B N   1 
ATOM   3503 C CA  . ALA   B 1 162 ? -1.445  -38.233 19.829 1.00 25.28  ? 237 ALA   B CA  1 
ATOM   3504 C C   . ALA   B 1 162 ? -0.032  -38.792 19.766 1.00 41.00  ? 237 ALA   B C   1 
ATOM   3505 O O   . ALA   B 1 162 ? 0.862   -38.256 20.428 1.00 45.53  ? 237 ALA   B O   1 
ATOM   3506 C CB  . ALA   B 1 162 ? -2.085  -38.616 21.165 1.00 25.48  ? 237 ALA   B CB  1 
ATOM   3507 N N   . ASN   B 1 163 ? 0.189   -39.856 18.994 1.00 42.12  ? 238 ASN   B N   1 
ATOM   3508 C CA  . ASN   B 1 163 ? 1.495   -40.494 18.905 1.00 35.36  ? 238 ASN   B CA  1 
ATOM   3509 C C   . ASN   B 1 163 ? 2.160   -40.276 17.554 1.00 31.07  ? 238 ASN   B C   1 
ATOM   3510 O O   . ASN   B 1 163 ? 3.153   -40.943 17.247 1.00 42.75  ? 238 ASN   B O   1 
ATOM   3511 C CB  . ASN   B 1 163 ? 1.375   -41.989 19.197 1.00 35.39  ? 238 ASN   B CB  1 
ATOM   3512 C CG  . ASN   B 1 163 ? 0.875   -42.266 20.598 1.00 32.61  ? 238 ASN   B CG  1 
ATOM   3513 O OD1 . ASN   B 1 163 ? 0.978   -41.419 21.485 1.00 49.73  ? 238 ASN   B OD1 1 
ATOM   3514 N ND2 . ASN   B 1 163 ? 0.332   -43.458 20.806 1.00 44.26  ? 238 ASN   B ND2 1 
ATOM   3515 N N   . ILE   B 1 164 ? 1.640   -39.363 16.743 1.00 37.66  ? 239 ILE   B N   1 
ATOM   3516 C CA  . ILE   B 1 164 ? 2.265   -38.956 15.491 1.00 27.37  ? 239 ILE   B CA  1 
ATOM   3517 C C   . ILE   B 1 164 ? 2.698   -37.503 15.643 1.00 37.30  ? 239 ILE   B C   1 
ATOM   3518 O O   . ILE   B 1 164 ? 1.895   -36.651 16.043 1.00 41.72  ? 239 ILE   B O   1 
ATOM   3519 C CB  . ILE   B 1 164 ? 1.307   -39.133 14.303 1.00 34.08  ? 239 ILE   B CB  1 
ATOM   3520 C CG1 . ILE   B 1 164 ? 0.959   -40.612 14.128 1.00 34.08  ? 239 ILE   B CG1 1 
ATOM   3521 C CG2 . ILE   B 1 164 ? 1.920   -38.575 13.035 1.00 34.09  ? 239 ILE   B CG2 1 
ATOM   3522 C CD1 . ILE   B 1 164 ? -0.006  -40.874 13.004 1.00 34.50  ? 239 ILE   B CD1 1 
ATOM   3523 N N   . PHE   B 1 165 ? 3.961   -37.220 15.333 1.00 34.75  ? 240 PHE   B N   1 
ATOM   3524 C CA  . PHE   B 1 165 ? 4.553   -35.917 15.604 1.00 31.13  ? 240 PHE   B CA  1 
ATOM   3525 C C   . PHE   B 1 165 ? 5.075   -35.308 14.312 1.00 32.95  ? 240 PHE   B C   1 
ATOM   3526 O O   . PHE   B 1 165 ? 5.867   -35.934 13.600 1.00 52.52  ? 240 PHE   B O   1 
ATOM   3527 C CB  . PHE   B 1 165 ? 5.671   -36.042 16.640 1.00 26.54  ? 240 PHE   B CB  1 
ATOM   3528 C CG  . PHE   B 1 165 ? 5.239   -36.728 17.902 1.00 36.85  ? 240 PHE   B CG  1 
ATOM   3529 C CD1 . PHE   B 1 165 ? 4.560   -36.031 18.891 1.00 35.37  ? 240 PHE   B CD1 1 
ATOM   3530 C CD2 . PHE   B 1 165 ? 5.498   -38.072 18.095 1.00 37.08  ? 240 PHE   B CD2 1 
ATOM   3531 C CE1 . PHE   B 1 165 ? 4.154   -36.666 20.053 1.00 34.42  ? 240 PHE   B CE1 1 
ATOM   3532 C CE2 . PHE   B 1 165 ? 5.095   -38.711 19.252 1.00 34.30  ? 240 PHE   B CE2 1 
ATOM   3533 C CZ  . PHE   B 1 165 ? 4.424   -38.008 20.234 1.00 37.73  ? 240 PHE   B CZ  1 
ATOM   3534 N N   . LEU   B 1 166 ? 4.636   -34.088 14.022 1.00 41.58  ? 241 LEU   B N   1 
ATOM   3535 C CA  . LEU   B 1 166 ? 4.899   -33.470 12.733 1.00 52.53  ? 241 LEU   B CA  1 
ATOM   3536 C C   . LEU   B 1 166 ? 6.312   -32.907 12.674 1.00 49.68  ? 241 LEU   B C   1 
ATOM   3537 O O   . LEU   B 1 166 ? 6.882   -32.490 13.684 1.00 47.37  ? 241 LEU   B O   1 
ATOM   3538 C CB  . LEU   B 1 166 ? 3.892   -32.355 12.458 1.00 40.49  ? 241 LEU   B CB  1 
ATOM   3539 C CG  . LEU   B 1 166 ? 2.420   -32.706 12.674 1.00 32.68  ? 241 LEU   B CG  1 
ATOM   3540 C CD1 . LEU   B 1 166 ? 1.556   -31.590 12.130 1.00 46.71  ? 241 LEU   B CD1 1 
ATOM   3541 C CD2 . LEU   B 1 166 ? 2.068   -34.032 12.018 1.00 32.06  ? 241 LEU   B CD2 1 
ATOM   3542 N N   . GLY   B 1 167 ? 6.874   -32.898 11.468 1.00 61.02  ? 242 GLY   B N   1 
ATOM   3543 C CA  . GLY   B 1 167 ? 8.185   -32.343 11.239 1.00 60.89  ? 242 GLY   B CA  1 
ATOM   3544 C C   . GLY   B 1 167 ? 8.153   -31.265 10.177 1.00 66.91  ? 242 GLY   B C   1 
ATOM   3545 O O   . GLY   B 1 167 ? 7.085   -30.823 9.742  1.00 74.64  ? 242 GLY   B O   1 
ATOM   3546 N N   . PRO   B 1 168 ? 9.325   -30.815 9.740  1.00 59.24  ? 243 PRO   B N   1 
ATOM   3547 C CA  . PRO   B 1 168 ? 9.368   -29.789 8.697  1.00 63.83  ? 243 PRO   B CA  1 
ATOM   3548 C C   . PRO   B 1 168 ? 8.979   -30.360 7.343  1.00 66.09  ? 243 PRO   B C   1 
ATOM   3549 O O   . PRO   B 1 168 ? 9.176   -31.545 7.061  1.00 59.96  ? 243 PRO   B O   1 
ATOM   3550 C CB  . PRO   B 1 168 ? 10.830  -29.332 8.709  1.00 69.10  ? 243 PRO   B CB  1 
ATOM   3551 C CG  . PRO   B 1 168 ? 11.580  -30.518 9.218  1.00 60.10  ? 243 PRO   B CG  1 
ATOM   3552 C CD  . PRO   B 1 168 ? 10.670  -31.185 10.213 1.00 70.50  ? 243 PRO   B CD  1 
ATOM   3553 N N   . ARG   B 1 169 ? 8.402   -29.490 6.509  1.00 69.80  ? 244 ARG   B N   1 
ATOM   3554 C CA  . ARG   B 1 169 ? 8.059   -29.819 5.123  1.00 66.56  ? 244 ARG   B CA  1 
ATOM   3555 C C   . ARG   B 1 169 ? 7.069   -30.979 5.044  1.00 59.71  ? 244 ARG   B C   1 
ATOM   3556 O O   . ARG   B 1 169 ? 7.220   -31.895 4.234  1.00 60.22  ? 244 ARG   B O   1 
ATOM   3557 C CB  . ARG   B 1 169 ? 9.315   -30.117 4.301  1.00 62.43  ? 244 ARG   B CB  1 
ATOM   3558 C CG  . ARG   B 1 169 ? 10.133  -28.881 3.972  1.00 69.42  ? 244 ARG   B CG  1 
ATOM   3559 C CD  . ARG   B 1 169 ? 11.616  -29.196 3.896  1.00 86.83  ? 244 ARG   B CD  1 
ATOM   3560 N NE  . ARG   B 1 169 ? 12.130  -29.686 5.169  1.00 98.83  ? 244 ARG   B NE  1 
ATOM   3561 C CZ  . ARG   B 1 169 ? 13.417  -29.835 5.451  1.00 117.01 ? 244 ARG   B CZ  1 
ATOM   3562 N NH1 . ARG   B 1 169 ? 14.357  -29.531 4.570  1.00 120.57 ? 244 ARG   B NH1 1 
ATOM   3563 N NH2 . ARG   B 1 169 ? 13.771  -30.295 6.647  1.00 110.05 ? 244 ARG   B NH2 1 
ATOM   3564 N N   . GLY   B 1 170 ? 6.047   -30.941 5.897  1.00 59.49  ? 245 GLY   B N   1 
ATOM   3565 C CA  . GLY   B 1 170 ? 4.975   -31.913 5.828  1.00 37.54  ? 245 GLY   B CA  1 
ATOM   3566 C C   . GLY   B 1 170 ? 5.332   -33.325 6.233  1.00 54.49  ? 245 GLY   B C   1 
ATOM   3567 O O   . GLY   B 1 170 ? 4.521   -34.232 6.021  1.00 64.19  ? 245 GLY   B O   1 
ATOM   3568 N N   . ARG   B 1 171 ? 6.512   -33.548 6.804  1.00 53.03  ? 246 ARG   B N   1 
ATOM   3569 C CA  . ARG   B 1 171 ? 6.882   -34.869 7.287  1.00 39.81  ? 246 ARG   B CA  1 
ATOM   3570 C C   . ARG   B 1 171 ? 6.360   -35.079 8.704  1.00 50.62  ? 246 ARG   B C   1 
ATOM   3571 O O   . ARG   B 1 171 ? 5.980   -34.136 9.404  1.00 48.80  ? 246 ARG   B O   1 
ATOM   3572 C CB  . ARG   B 1 171 ? 8.400   -35.054 7.260  1.00 54.04  ? 246 ARG   B CB  1 
ATOM   3573 C CG  . ARG   B 1 171 ? 9.063   -34.634 5.961  1.00 56.81  ? 246 ARG   B CG  1 
ATOM   3574 C CD  . ARG   B 1 171 ? 8.548   -35.445 4.788  1.00 57.67  ? 246 ARG   B CD  1 
ATOM   3575 N NE  . ARG   B 1 171 ? 8.904   -36.855 4.896  1.00 70.47  ? 246 ARG   B NE  1 
ATOM   3576 C CZ  . ARG   B 1 171 ? 9.995   -37.392 4.367  1.00 93.58  ? 246 ARG   B CZ  1 
ATOM   3577 N NH1 . ARG   B 1 171 ? 10.871  -36.660 3.698  1.00 99.05  ? 246 ARG   B NH1 1 
ATOM   3578 N NH2 . ARG   B 1 171 ? 10.212  -38.696 4.512  1.00 80.29  ? 246 ARG   B NH2 1 
ATOM   3579 N N   . CYS   B 1 172 ? 6.343   -36.341 9.125  1.00 52.51  ? 247 CYS   B N   1 
ATOM   3580 C CA  . CYS   B 1 172 ? 5.953   -36.683 10.484 1.00 53.26  ? 247 CYS   B CA  1 
ATOM   3581 C C   . CYS   B 1 172 ? 6.656   -37.972 10.878 1.00 45.27  ? 247 CYS   B C   1 
ATOM   3582 O O   . CYS   B 1 172 ? 7.269   -38.650 10.050 1.00 53.84  ? 247 CYS   B O   1 
ATOM   3583 C CB  . CYS   B 1 172 ? 4.431   -36.813 10.625 1.00 42.84  ? 247 CYS   B CB  1 
ATOM   3584 S SG  . CYS   B 1 172 ? 3.712   -38.256 9.818  1.00 51.93  ? 247 CYS   B SG  1 
ATOM   3585 N N   . LYS   B 1 173 ? 6.571   -38.299 12.163 1.00 38.14  ? 248 LYS   B N   1 
ATOM   3586 C CA  . LYS   B 1 173 ? 7.261   -39.455 12.711 1.00 36.91  ? 248 LYS   B CA  1 
ATOM   3587 C C   . LYS   B 1 173 ? 6.350   -40.151 13.706 1.00 42.70  ? 248 LYS   B C   1 
ATOM   3588 O O   . LYS   B 1 173 ? 5.706   -39.499 14.530 1.00 40.60  ? 248 LYS   B O   1 
ATOM   3589 C CB  . LYS   B 1 173 ? 8.572   -39.053 13.404 1.00 38.36  ? 248 LYS   B CB  1 
ATOM   3590 C CG  . LYS   B 1 173 ? 9.591   -38.386 12.493 1.00 43.87  ? 248 LYS   B CG  1 
ATOM   3591 C CD  . LYS   B 1 173 ? 10.882  -38.064 13.231 1.00 41.77  ? 248 LYS   B CD  1 
ATOM   3592 C CE  . LYS   B 1 173 ? 11.926  -37.520 12.270 1.00 51.08  ? 248 LYS   B CE  1 
ATOM   3593 N NZ  . LYS   B 1 173 ? 13.241  -37.310 12.928 1.00 73.73  ? 248 LYS   B NZ  1 
ATOM   3594 N N   . LEU   B 1 174 ? 6.292   -41.476 13.615 1.00 36.30  ? 249 LEU   B N   1 
ATOM   3595 C CA  . LEU   B 1 174 ? 5.553   -42.272 14.581 1.00 25.83  ? 249 LEU   B CA  1 
ATOM   3596 C C   . LEU   B 1 174 ? 6.335   -42.348 15.880 1.00 32.35  ? 249 LEU   B C   1 
ATOM   3597 O O   . LEU   B 1 174 ? 7.556   -42.522 15.873 1.00 37.55  ? 249 LEU   B O   1 
ATOM   3598 C CB  . LEU   B 1 174 ? 5.301   -43.681 14.041 1.00 33.91  ? 249 LEU   B CB  1 
ATOM   3599 C CG  . LEU   B 1 174 ? 4.492   -44.617 14.936 1.00 38.54  ? 249 LEU   B CG  1 
ATOM   3600 C CD1 . LEU   B 1 174 ? 3.112   -44.035 15.214 1.00 29.55  ? 249 LEU   B CD1 1 
ATOM   3601 C CD2 . LEU   B 1 174 ? 4.382   -45.983 14.286 1.00 40.77  ? 249 LEU   B CD2 1 
ATOM   3602 N N   . GLY   B 1 175 ? 5.629   -42.218 16.997 1.00 39.04  ? 250 GLY   B N   1 
ATOM   3603 C CA  . GLY   B 1 175 ? 6.296   -42.249 18.284 1.00 28.08  ? 250 GLY   B CA  1 
ATOM   3604 C C   . GLY   B 1 175 ? 5.518   -42.961 19.371 1.00 35.73  ? 250 GLY   B C   1 
ATOM   3605 O O   . GLY   B 1 175 ? 4.547   -43.671 19.093 1.00 43.58  ? 250 GLY   B O   1 
ATOM   3606 N N   . ASP   B 1 176 ? 5.948   -42.764 20.618 1.00 41.75  ? 251 ASP   B N   1 
ATOM   3607 C CA  . ASP   B 1 176 ? 5.353   -43.381 21.798 1.00 37.75  ? 251 ASP   B CA  1 
ATOM   3608 C C   . ASP   B 1 176 ? 5.290   -44.895 21.647 1.00 42.52  ? 251 ASP   B C   1 
ATOM   3609 O O   . ASP   B 1 176 ? 4.238   -45.457 21.321 1.00 44.27  ? 251 ASP   B O   1 
ATOM   3610 C CB  . ASP   B 1 176 ? 3.961   -42.808 22.072 1.00 40.96  ? 251 ASP   B CB  1 
ATOM   3611 C CG  . ASP   B 1 176 ? 3.497   -43.065 23.498 1.00 61.48  ? 251 ASP   B CG  1 
ATOM   3612 O OD1 . ASP   B 1 176 ? 4.192   -43.808 24.223 1.00 53.25  ? 251 ASP   B OD1 1 
ATOM   3613 O OD2 . ASP   B 1 176 ? 2.446   -42.517 23.895 1.00 63.95  ? 251 ASP   B OD2 1 
ATOM   3614 N N   . PHE   B 1 177 ? 6.420   -45.561 21.887 1.00 41.01  ? 252 PHE   B N   1 
ATOM   3615 C CA  . PHE   B 1 177 ? 6.525   -47.010 21.783 1.00 33.56  ? 252 PHE   B CA  1 
ATOM   3616 C C   . PHE   B 1 177 ? 6.260   -47.709 23.109 1.00 29.91  ? 252 PHE   B C   1 
ATOM   3617 O O   . PHE   B 1 177 ? 6.799   -48.797 23.355 1.00 46.26  ? 252 PHE   B O   1 
ATOM   3618 C CB  . PHE   B 1 177 ? 7.904   -47.388 21.241 1.00 29.62  ? 252 PHE   B CB  1 
ATOM   3619 C CG  . PHE   B 1 177 ? 8.202   -46.805 19.884 1.00 34.61  ? 252 PHE   B CG  1 
ATOM   3620 C CD1 . PHE   B 1 177 ? 7.259   -46.852 18.875 1.00 37.00  ? 252 PHE   B CD1 1 
ATOM   3621 C CD2 . PHE   B 1 177 ? 9.420   -46.202 19.624 1.00 44.04  ? 252 PHE   B CD2 1 
ATOM   3622 C CE1 . PHE   B 1 177 ? 7.527   -46.318 17.630 1.00 36.78  ? 252 PHE   B CE1 1 
ATOM   3623 C CE2 . PHE   B 1 177 ? 9.691   -45.664 18.381 1.00 44.98  ? 252 PHE   B CE2 1 
ATOM   3624 C CZ  . PHE   B 1 177 ? 8.743   -45.723 17.385 1.00 33.61  ? 252 PHE   B CZ  1 
ATOM   3625 N N   . GLY   B 1 178 ? 5.445   -47.109 23.980 1.00 40.25  ? 253 GLY   B N   1 
ATOM   3626 C CA  . GLY   B 1 178 ? 5.204   -47.701 25.284 1.00 30.41  ? 253 GLY   B CA  1 
ATOM   3627 C C   . GLY   B 1 178 ? 4.384   -48.973 25.222 1.00 43.68  ? 253 GLY   B C   1 
ATOM   3628 O O   . GLY   B 1 178 ? 4.562   -49.868 26.052 1.00 57.48  ? 253 GLY   B O   1 
ATOM   3629 N N   . LEU   B 1 179 ? 3.480   -49.074 24.249 1.00 36.53  ? 254 LEU   B N   1 
ATOM   3630 C CA  . LEU   B 1 179 ? 2.655   -50.261 24.068 1.00 44.91  ? 254 LEU   B CA  1 
ATOM   3631 C C   . LEU   B 1 179 ? 3.222   -51.226 23.037 1.00 44.51  ? 254 LEU   B C   1 
ATOM   3632 O O   . LEU   B 1 179 ? 2.593   -52.251 22.758 1.00 49.90  ? 254 LEU   B O   1 
ATOM   3633 C CB  . LEU   B 1 179 ? 1.232   -49.864 23.659 1.00 39.00  ? 254 LEU   B CB  1 
ATOM   3634 C CG  . LEU   B 1 179 ? 0.370   -49.149 24.705 1.00 42.37  ? 254 LEU   B CG  1 
ATOM   3635 C CD1 . LEU   B 1 179 ? -1.051  -48.969 24.208 1.00 60.73  ? 254 LEU   B CD1 1 
ATOM   3636 C CD2 . LEU   B 1 179 ? 0.368   -49.918 26.001 1.00 41.55  ? 254 LEU   B CD2 1 
ATOM   3637 N N   . LEU   B 1 180 ? 4.387   -50.929 22.470 1.00 47.38  ? 255 LEU   B N   1 
ATOM   3638 C CA  . LEU   B 1 180 ? 4.938   -51.764 21.414 1.00 31.18  ? 255 LEU   B CA  1 
ATOM   3639 C C   . LEU   B 1 180 ? 5.306   -53.136 21.961 1.00 41.68  ? 255 LEU   B C   1 
ATOM   3640 O O   . LEU   B 1 180 ? 5.865   -53.256 23.054 1.00 53.75  ? 255 LEU   B O   1 
ATOM   3641 C CB  . LEU   B 1 180 ? 6.165   -51.088 20.799 1.00 47.33  ? 255 LEU   B CB  1 
ATOM   3642 C CG  . LEU   B 1 180 ? 6.858   -51.766 19.613 1.00 41.09  ? 255 LEU   B CG  1 
ATOM   3643 C CD1 . LEU   B 1 180 ? 7.397   -50.717 18.659 1.00 37.36  ? 255 LEU   B CD1 1 
ATOM   3644 C CD2 . LEU   B 1 180 ? 7.987   -52.674 20.074 1.00 43.22  ? 255 LEU   B CD2 1 
ATOM   3645 N N   . VAL   B 1 181 ? 4.984   -54.178 21.197 1.00 37.82  ? 256 VAL   B N   1 
ATOM   3646 C CA  . VAL   B 1 181 ? 5.332   -55.545 21.562 1.00 38.67  ? 256 VAL   B CA  1 
ATOM   3647 C C   . VAL   B 1 181 ? 6.047   -56.197 20.389 1.00 40.17  ? 256 VAL   B C   1 
ATOM   3648 O O   . VAL   B 1 181 ? 5.863   -55.810 19.231 1.00 49.61  ? 256 VAL   B O   1 
ATOM   3649 C CB  . VAL   B 1 181 ? 4.094   -56.381 21.967 1.00 38.13  ? 256 VAL   B CB  1 
ATOM   3650 C CG1 . VAL   B 1 181 ? 3.297   -55.672 23.047 1.00 66.72  ? 256 VAL   B CG1 1 
ATOM   3651 C CG2 . VAL   B 1 181 ? 3.223   -56.663 20.757 1.00 46.58  ? 256 VAL   B CG2 1 
ATOM   3652 N N   . GLU   B 1 182 ? 6.874   -57.190 20.693 1.00 41.69  ? 257 GLU   B N   1 
ATOM   3653 C CA  . GLU   B 1 182 ? 7.556   -57.971 19.673 1.00 45.57  ? 257 GLU   B CA  1 
ATOM   3654 C C   . GLU   B 1 182 ? 6.861   -59.317 19.538 1.00 43.44  ? 257 GLU   B C   1 
ATOM   3655 O O   . GLU   B 1 182 ? 6.654   -60.017 20.535 1.00 49.98  ? 257 GLU   B O   1 
ATOM   3656 C CB  . GLU   B 1 182 ? 9.033   -58.172 20.012 1.00 45.94  ? 257 GLU   B CB  1 
ATOM   3657 C CG  . GLU   B 1 182 ? 9.797   -58.959 18.954 1.00 43.35  ? 257 GLU   B CG  1 
ATOM   3658 C CD  . GLU   B 1 182 ? 11.251  -59.192 19.324 1.00 79.15  ? 257 GLU   B CD  1 
ATOM   3659 O OE1 . GLU   B 1 182 ? 11.586  -59.076 20.521 1.00 90.97  ? 257 GLU   B OE1 1 
ATOM   3660 O OE2 . GLU   B 1 182 ? 12.059  -59.487 18.418 1.00 82.62  ? 257 GLU   B OE2 1 
ATOM   3661 N N   . LEU   B 1 183 ? 6.496   -59.672 18.313 1.00 44.72  ? 258 LEU   B N   1 
ATOM   3662 C CA  . LEU   B 1 183 ? 5.786   -60.923 18.069 1.00 47.48  ? 258 LEU   B CA  1 
ATOM   3663 C C   . LEU   B 1 183 ? 6.741   -62.085 18.295 1.00 56.93  ? 258 LEU   B C   1 
ATOM   3664 O O   . LEU   B 1 183 ? 7.566   -62.409 17.438 1.00 74.06  ? 258 LEU   B O   1 
ATOM   3665 C CB  . LEU   B 1 183 ? 5.209   -60.938 16.659 1.00 55.46  ? 258 LEU   B CB  1 
ATOM   3666 C CG  . LEU   B 1 183 ? 4.180   -59.836 16.412 1.00 50.90  ? 258 LEU   B CG  1 
ATOM   3667 C CD1 . LEU   B 1 183 ? 3.594   -59.940 15.013 1.00 54.61  ? 258 LEU   B CD1 1 
ATOM   3668 C CD2 . LEU   B 1 183 ? 3.089   -59.903 17.468 1.00 43.92  ? 258 LEU   B CD2 1 
ATOM   3669 N N   . GLY   B 1 184 ? 6.635   -62.714 19.462 1.00 78.11  ? 259 GLY   B N   1 
ATOM   3670 C CA  . GLY   B 1 184 ? 7.468   -63.848 19.801 1.00 61.27  ? 259 GLY   B CA  1 
ATOM   3671 C C   . GLY   B 1 184 ? 6.738   -64.831 20.690 1.00 99.06  ? 259 GLY   B C   1 
ATOM   3672 O O   . GLY   B 1 184 ? 6.105   -64.435 21.674 1.00 104.08 ? 259 GLY   B O   1 
ATOM   3673 N N   . THR   B 1 185 ? 6.815   -66.113 20.348 1.00 109.47 ? 260 THR   B N   1 
ATOM   3674 C CA  . THR   B 1 185 ? 6.106   -67.155 21.081 1.00 99.77  ? 260 THR   B CA  1 
ATOM   3675 C C   . THR   B 1 185 ? 6.591   -67.255 22.524 1.00 100.64 ? 260 THR   B C   1 
ATOM   3676 O O   . THR   B 1 185 ? 5.991   -66.673 23.429 1.00 85.55  ? 260 THR   B O   1 
ATOM   3677 C CB  . THR   B 1 185 ? 6.269   -68.524 20.396 1.00 105.82 ? 260 THR   B CB  1 
ATOM   3678 O OG1 . THR   B 1 185 ? 5.831   -68.431 19.034 1.00 96.35  ? 260 THR   B OG1 1 
ATOM   3679 C CG2 . THR   B 1 185 ? 5.448   -69.581 21.115 1.00 113.65 ? 260 THR   B CG2 1 
ATOM   3680 N N   . GLU   B 1 190 ? 2.027   -60.028 27.671 1.00 82.83  ? 265 GLU   B N   1 
ATOM   3681 C CA  . GLU   B 1 190 ? 2.954   -58.914 27.504 1.00 77.96  ? 265 GLU   B CA  1 
ATOM   3682 C C   . GLU   B 1 190 ? 2.280   -57.710 26.843 1.00 85.65  ? 265 GLU   B C   1 
ATOM   3683 O O   . GLU   B 1 190 ? 2.784   -56.588 26.910 1.00 79.42  ? 265 GLU   B O   1 
ATOM   3684 C CB  . GLU   B 1 190 ? 4.171   -59.358 26.688 1.00 89.08  ? 265 GLU   B CB  1 
ATOM   3685 C CG  . GLU   B 1 190 ? 3.824   -60.053 25.378 1.00 94.75  ? 265 GLU   B CG  1 
ATOM   3686 C CD  . GLU   B 1 190 ? 5.053   -60.503 24.609 1.00 111.89 ? 265 GLU   B CD  1 
ATOM   3687 O OE1 . GLU   B 1 190 ? 6.171   -60.081 24.973 1.00 127.41 ? 265 GLU   B OE1 1 
ATOM   3688 O OE2 . GLU   B 1 190 ? 4.903   -61.281 23.642 1.00 104.09 ? 265 GLU   B OE2 1 
ATOM   3689 N N   . VAL   B 1 191 ? 1.139   -57.949 26.206 1.00 78.99  ? 266 VAL   B N   1 
ATOM   3690 C CA  . VAL   B 1 191 ? 0.374   -56.880 25.574 1.00 53.13  ? 266 VAL   B CA  1 
ATOM   3691 C C   . VAL   B 1 191 ? -0.451  -56.164 26.634 1.00 68.60  ? 266 VAL   B C   1 
ATOM   3692 O O   . VAL   B 1 191 ? -0.961  -56.786 27.575 1.00 71.04  ? 266 VAL   B O   1 
ATOM   3693 C CB  . VAL   B 1 191 ? -0.515  -57.448 24.454 1.00 52.45  ? 266 VAL   B CB  1 
ATOM   3694 C CG1 . VAL   B 1 191 ? -1.410  -56.367 23.867 1.00 64.99  ? 266 VAL   B CG1 1 
ATOM   3695 C CG2 . VAL   B 1 191 ? 0.343   -58.076 23.367 1.00 55.32  ? 266 VAL   B CG2 1 
ATOM   3696 N N   . GLN   B 1 192 ? -0.580  -54.848 26.490 1.00 69.44  ? 267 GLN   B N   1 
ATOM   3697 C CA  . GLN   B 1 192 ? -1.314  -54.015 27.429 1.00 60.12  ? 267 GLN   B CA  1 
ATOM   3698 C C   . GLN   B 1 192 ? -2.565  -53.443 26.771 1.00 66.34  ? 267 GLN   B C   1 
ATOM   3699 O O   . GLN   B 1 192 ? -2.756  -53.518 25.553 1.00 55.26  ? 267 GLN   B O   1 
ATOM   3700 C CB  . GLN   B 1 192 ? -0.424  -52.886 27.955 1.00 55.18  ? 267 GLN   B CB  1 
ATOM   3701 C CG  . GLN   B 1 192 ? 0.948   -53.349 28.414 1.00 68.99  ? 267 GLN   B CG  1 
ATOM   3702 C CD  . GLN   B 1 192 ? 1.788   -52.214 28.960 1.00 77.73  ? 267 GLN   B CD  1 
ATOM   3703 O OE1 . GLN   B 1 192 ? 1.350   -51.471 29.838 1.00 93.63  ? 267 GLN   B OE1 1 
ATOM   3704 N NE2 . GLN   B 1 192 ? 3.000   -52.067 28.436 1.00 74.46  ? 267 GLN   B NE2 1 
ATOM   3705 N N   . GLU   B 1 193 ? -3.423  -52.862 27.606 1.00 70.28  ? 268 GLU   B N   1 
ATOM   3706 C CA  . GLU   B 1 193 ? -4.679  -52.293 27.134 1.00 67.43  ? 268 GLU   B CA  1 
ATOM   3707 C C   . GLU   B 1 193 ? -4.416  -51.119 26.201 1.00 66.00  ? 268 GLU   B C   1 
ATOM   3708 O O   . GLU   B 1 193 ? -3.728  -50.164 26.571 1.00 63.30  ? 268 GLU   B O   1 
ATOM   3709 C CB  . GLU   B 1 193 ? -5.525  -51.845 28.325 1.00 54.79  ? 268 GLU   B CB  1 
ATOM   3710 C CG  . GLU   B 1 193 ? -5.963  -52.973 29.242 1.00 71.31  ? 268 GLU   B CG  1 
ATOM   3711 C CD  . GLU   B 1 193 ? -7.045  -53.840 28.629 1.00 84.51  ? 268 GLU   B CD  1 
ATOM   3712 O OE1 . GLU   B 1 193 ? -7.795  -53.341 27.762 1.00 71.14  ? 268 GLU   B OE1 1 
ATOM   3713 O OE2 . GLU   B 1 193 ? -7.143  -55.024 29.017 1.00 94.48  ? 268 GLU   B OE2 1 
ATOM   3714 N N   . GLY   B 1 194 ? -4.967  -51.190 24.988 1.00 65.50  ? 269 GLY   B N   1 
ATOM   3715 C CA  . GLY   B 1 194 ? -4.855  -50.104 24.039 1.00 51.54  ? 269 GLY   B CA  1 
ATOM   3716 C C   . GLY   B 1 194 ? -6.036  -49.150 24.109 1.00 51.88  ? 269 GLY   B C   1 
ATOM   3717 O O   . GLY   B 1 194 ? -6.958  -49.298 24.909 1.00 57.89  ? 269 GLY   B O   1 
ATOM   3718 N N   . ASP   B 1 195 ? -5.992  -48.144 23.247 1.00 52.09  ? 270 ASP   B N   1 
ATOM   3719 C CA  . ASP   B 1 195 ? -7.087  -47.186 23.159 1.00 41.61  ? 270 ASP   B CA  1 
ATOM   3720 C C   . ASP   B 1 195 ? -8.241  -47.820 22.391 1.00 46.39  ? 270 ASP   B C   1 
ATOM   3721 O O   . ASP   B 1 195 ? -8.059  -48.200 21.229 1.00 42.94  ? 270 ASP   B O   1 
ATOM   3722 C CB  . ASP   B 1 195 ? -6.621  -45.912 22.464 1.00 42.65  ? 270 ASP   B CB  1 
ATOM   3723 C CG  . ASP   B 1 195 ? -7.510  -44.720 22.763 1.00 49.12  ? 270 ASP   B CG  1 
ATOM   3724 O OD1 . ASP   B 1 195 ? -8.739  -44.903 22.909 1.00 47.45  ? 270 ASP   B OD1 1 
ATOM   3725 O OD2 . ASP   B 1 195 ? -6.974  -43.593 22.852 1.00 52.77  ? 270 ASP   B OD2 1 
ATOM   3726 N N   . PRO   B 1 196 ? -9.428  -47.959 22.990 1.00 38.93  ? 271 PRO   B N   1 
ATOM   3727 C CA  . PRO   B 1 196 ? -10.527 -48.637 22.282 1.00 32.27  ? 271 PRO   B CA  1 
ATOM   3728 C C   . PRO   B 1 196 ? -11.022 -47.889 21.059 1.00 36.78  ? 271 PRO   B C   1 
ATOM   3729 O O   . PRO   B 1 196 ? -11.593 -48.520 20.160 1.00 40.33  ? 271 PRO   B O   1 
ATOM   3730 C CB  . PRO   B 1 196 ? -11.624 -48.742 23.348 1.00 35.96  ? 271 PRO   B CB  1 
ATOM   3731 C CG  . PRO   B 1 196 ? -11.318 -47.649 24.310 1.00 43.32  ? 271 PRO   B CG  1 
ATOM   3732 C CD  . PRO   B 1 196 ? -9.823  -47.531 24.341 1.00 49.29  ? 271 PRO   B CD  1 
ATOM   3733 N N   . ARG   B 1 197 ? -10.829 -46.571 20.995 1.00 37.11  ? 272 ARG   B N   1 
ATOM   3734 C CA  . ARG   B 1 197 ? -11.269 -45.819 19.825 1.00 27.20  ? 272 ARG   B CA  1 
ATOM   3735 C C   . ARG   B 1 197 ? -10.534 -46.266 18.569 1.00 35.18  ? 272 ARG   B C   1 
ATOM   3736 O O   . ARG   B 1 197 ? -11.121 -46.309 17.481 1.00 44.51  ? 272 ARG   B O   1 
ATOM   3737 C CB  . ARG   B 1 197 ? -11.069 -44.323 20.059 1.00 35.64  ? 272 ARG   B CB  1 
ATOM   3738 C CG  . ARG   B 1 197 ? -11.894 -43.772 21.203 1.00 47.24  ? 272 ARG   B CG  1 
ATOM   3739 C CD  . ARG   B 1 197 ? -11.501 -42.347 21.540 1.00 46.18  ? 272 ARG   B CD  1 
ATOM   3740 N NE  . ARG   B 1 197 ? -10.119 -42.259 21.994 1.00 57.57  ? 272 ARG   B NE  1 
ATOM   3741 C CZ  . ARG   B 1 197 ? -9.609  -41.220 22.641 1.00 62.11  ? 272 ARG   B CZ  1 
ATOM   3742 N NH1 . ARG   B 1 197 ? -10.346 -40.162 22.937 1.00 60.61  ? 272 ARG   B NH1 1 
ATOM   3743 N NH2 . ARG   B 1 197 ? -8.331  -41.248 23.007 1.00 55.28  ? 272 ARG   B NH2 1 
ATOM   3744 N N   . TYR   B 1 198 ? -9.250  -46.612 18.696 1.00 34.69  ? 273 TYR   B N   1 
ATOM   3745 C CA  . TYR   B 1 198 ? -8.417  -46.959 17.550 1.00 38.93  ? 273 TYR   B CA  1 
ATOM   3746 C C   . TYR   B 1 198 ? -8.139  -48.455 17.472 1.00 35.15  ? 273 TYR   B C   1 
ATOM   3747 O O   . TYR   B 1 198 ? -7.239  -48.882 16.741 1.00 51.63  ? 273 TYR   B O   1 
ATOM   3748 C CB  . TYR   B 1 198 ? -7.104  -46.178 17.597 1.00 42.37  ? 273 TYR   B CB  1 
ATOM   3749 C CG  . TYR   B 1 198 ? -7.289  -44.685 17.764 1.00 35.33  ? 273 TYR   B CG  1 
ATOM   3750 C CD1 . TYR   B 1 198 ? -7.358  -44.113 19.027 1.00 28.39  ? 273 TYR   B CD1 1 
ATOM   3751 C CD2 . TYR   B 1 198 ? -7.401  -43.850 16.659 1.00 34.11  ? 273 TYR   B CD2 1 
ATOM   3752 C CE1 . TYR   B 1 198 ? -7.534  -42.751 19.188 1.00 36.87  ? 273 TYR   B CE1 1 
ATOM   3753 C CE2 . TYR   B 1 198 ? -7.573  -42.485 16.811 1.00 45.84  ? 273 TYR   B CE2 1 
ATOM   3754 C CZ  . TYR   B 1 198 ? -7.641  -41.942 18.077 1.00 43.09  ? 273 TYR   B CZ  1 
ATOM   3755 O OH  . TYR   B 1 198 ? -7.815  -40.584 18.234 1.00 61.46  ? 273 TYR   B OH  1 
ATOM   3756 N N   . MET   B 1 199 ? -8.906  -49.257 18.196 1.00 41.44  ? 274 MET   B N   1 
ATOM   3757 C CA  . MET   B 1 199 ? -8.639  -50.682 18.301 1.00 29.74  ? 274 MET   B CA  1 
ATOM   3758 C C   . MET   B 1 199 ? -9.178  -51.421 17.084 1.00 38.05  ? 274 MET   B C   1 
ATOM   3759 O O   . MET   B 1 199 ? -10.320 -51.204 16.667 1.00 43.32  ? 274 MET   B O   1 
ATOM   3760 C CB  . MET   B 1 199 ? -9.271  -51.229 19.577 1.00 36.15  ? 274 MET   B CB  1 
ATOM   3761 C CG  . MET   B 1 199 ? -9.080  -52.705 19.782 1.00 49.24  ? 274 MET   B CG  1 
ATOM   3762 S SD  . MET   B 1 199 ? -9.758  -53.204 21.371 1.00 71.72  ? 274 MET   B SD  1 
ATOM   3763 C CE  . MET   B 1 199 ? -8.752  -52.230 22.490 1.00 67.35  ? 274 MET   B CE  1 
ATOM   3764 N N   . ALA   B 1 200 ? -8.346  -52.287 16.511 1.00 40.68  ? 275 ALA   B N   1 
ATOM   3765 C CA  . ALA   B 1 200 ? -8.800  -53.167 15.451 1.00 40.10  ? 275 ALA   B CA  1 
ATOM   3766 C C   . ALA   B 1 200 ? -9.770  -54.200 16.019 1.00 44.17  ? 275 ALA   B C   1 
ATOM   3767 O O   . ALA   B 1 200 ? -9.654  -54.594 17.182 1.00 49.74  ? 275 ALA   B O   1 
ATOM   3768 C CB  . ALA   B 1 200 ? -7.614  -53.866 14.795 1.00 39.07  ? 275 ALA   B CB  1 
ATOM   3769 N N   . PRO   B 1 201 ? -10.736 -54.661 15.219 1.00 41.97  ? 276 PRO   B N   1 
ATOM   3770 C CA  . PRO   B 1 201 ? -11.748 -55.581 15.768 1.00 41.84  ? 276 PRO   B CA  1 
ATOM   3771 C C   . PRO   B 1 201 ? -11.175 -56.906 16.242 1.00 46.14  ? 276 PRO   B C   1 
ATOM   3772 O O   . PRO   B 1 201 ? -11.670 -57.468 17.228 1.00 47.16  ? 276 PRO   B O   1 
ATOM   3773 C CB  . PRO   B 1 201 ? -12.722 -55.771 14.596 1.00 40.59  ? 276 PRO   B CB  1 
ATOM   3774 C CG  . PRO   B 1 201 ? -11.911 -55.449 13.366 1.00 39.26  ? 276 PRO   B CG  1 
ATOM   3775 C CD  . PRO   B 1 201 ? -10.960 -54.369 13.792 1.00 32.86  ? 276 PRO   B CD  1 
ATOM   3776 N N   . GLU   B 1 202 ? -10.140 -57.423 15.577 1.00 46.15  ? 277 GLU   B N   1 
ATOM   3777 C CA  . GLU   B 1 202 ? -9.618  -58.735 15.938 1.00 41.77  ? 277 GLU   B CA  1 
ATOM   3778 C C   . GLU   B 1 202 ? -8.853  -58.707 17.252 1.00 40.95  ? 277 GLU   B C   1 
ATOM   3779 O O   . GLU   B 1 202 ? -8.572  -59.771 17.815 1.00 51.56  ? 277 GLU   B O   1 
ATOM   3780 C CB  . GLU   B 1 202 ? -8.719  -59.274 14.824 1.00 39.10  ? 277 GLU   B CB  1 
ATOM   3781 C CG  . GLU   B 1 202 ? -7.388  -58.544 14.680 1.00 46.32  ? 277 GLU   B CG  1 
ATOM   3782 C CD  . GLU   B 1 202 ? -7.492  -57.280 13.850 1.00 56.61  ? 277 GLU   B CD  1 
ATOM   3783 O OE1 . GLU   B 1 202 ? -8.626  -56.884 13.506 1.00 61.27  ? 277 GLU   B OE1 1 
ATOM   3784 O OE2 . GLU   B 1 202 ? -6.436  -56.684 13.536 1.00 44.24  ? 277 GLU   B OE2 1 
ATOM   3785 N N   . LEU   B 1 203 ? -8.503  -57.519 17.749 1.00 41.20  ? 278 LEU   B N   1 
ATOM   3786 C CA  . LEU   B 1 203 ? -7.813  -57.439 19.031 1.00 35.92  ? 278 LEU   B CA  1 
ATOM   3787 C C   . LEU   B 1 203 ? -8.704  -57.933 20.162 1.00 51.01  ? 278 LEU   B C   1 
ATOM   3788 O O   . LEU   B 1 203 ? -8.224  -58.574 21.104 1.00 61.52  ? 278 LEU   B O   1 
ATOM   3789 C CB  . LEU   B 1 203 ? -7.353  -56.007 19.299 1.00 41.33  ? 278 LEU   B CB  1 
ATOM   3790 C CG  . LEU   B 1 203 ? -6.200  -55.470 18.452 1.00 40.48  ? 278 LEU   B CG  1 
ATOM   3791 C CD1 . LEU   B 1 203 ? -5.671  -54.178 19.051 1.00 49.33  ? 278 LEU   B CD1 1 
ATOM   3792 C CD2 . LEU   B 1 203 ? -5.092  -56.502 18.337 1.00 56.26  ? 278 LEU   B CD2 1 
ATOM   3793 N N   . LEU   B 1 204 ? -10.008 -57.645 20.087 1.00 48.82  ? 279 LEU   B N   1 
ATOM   3794 C CA  . LEU   B 1 204 ? -10.932 -58.171 21.086 1.00 48.61  ? 279 LEU   B CA  1 
ATOM   3795 C C   . LEU   B 1 204 ? -10.974 -59.690 21.056 1.00 51.83  ? 279 LEU   B C   1 
ATOM   3796 O O   . LEU   B 1 204 ? -11.213 -60.325 22.089 1.00 64.16  ? 279 LEU   B O   1 
ATOM   3797 C CB  . LEU   B 1 204 ? -12.331 -57.605 20.863 1.00 63.05  ? 279 LEU   B CB  1 
ATOM   3798 C CG  . LEU   B 1 204 ? -12.521 -56.112 21.106 1.00 61.39  ? 279 LEU   B CG  1 
ATOM   3799 C CD1 . LEU   B 1 204 ? -13.986 -55.768 20.987 1.00 57.65  ? 279 LEU   B CD1 1 
ATOM   3800 C CD2 . LEU   B 1 204 ? -11.995 -55.735 22.473 1.00 67.31  ? 279 LEU   B CD2 1 
ATOM   3801 N N   . GLN   B 1 205 ? -10.748 -60.285 19.888 1.00 64.68  ? 280 GLN   B N   1 
ATOM   3802 C CA  . GLN   B 1 205 ? -10.728 -61.730 19.724 1.00 50.39  ? 280 GLN   B CA  1 
ATOM   3803 C C   . GLN   B 1 205 ? -9.364  -62.335 20.030 1.00 48.39  ? 280 GLN   B C   1 
ATOM   3804 O O   . GLN   B 1 205 ? -9.120  -63.494 19.677 1.00 70.89  ? 280 GLN   B O   1 
ATOM   3805 C CB  . GLN   B 1 205 ? -11.157 -62.100 18.301 1.00 56.71  ? 280 GLN   B CB  1 
ATOM   3806 C CG  . GLN   B 1 205 ? -12.462 -61.450 17.879 1.00 65.43  ? 280 GLN   B CG  1 
ATOM   3807 C CD  . GLN   B 1 205 ? -13.574 -61.713 18.871 1.00 79.03  ? 280 GLN   B CD  1 
ATOM   3808 O OE1 . GLN   B 1 205 ? -14.136 -60.786 19.455 1.00 69.00  ? 280 GLN   B OE1 1 
ATOM   3809 N NE2 . GLN   B 1 205 ? -13.894 -62.984 19.073 1.00 84.28  ? 280 GLN   B NE2 1 
ATOM   3810 N N   . GLY   B 1 206 ? -8.473  -61.579 20.669 1.00 51.35  ? 281 GLY   B N   1 
ATOM   3811 C CA  . GLY   B 1 206 ? -7.173  -62.107 21.028 1.00 72.80  ? 281 GLY   B CA  1 
ATOM   3812 C C   . GLY   B 1 206 ? -6.241  -62.355 19.866 1.00 59.16  ? 281 GLY   B C   1 
ATOM   3813 O O   . GLY   B 1 206 ? -5.289  -63.126 20.004 1.00 65.27  ? 281 GLY   B O   1 
ATOM   3814 N N   . SER   B 1 207 ? -6.486  -61.725 18.721 1.00 45.83  ? 282 SER   B N   1 
ATOM   3815 C CA  . SER   B 1 207 ? -5.643  -61.886 17.540 1.00 39.67  ? 282 SER   B CA  1 
ATOM   3816 C C   . SER   B 1 207 ? -4.771  -60.643 17.418 1.00 43.70  ? 282 SER   B C   1 
ATOM   3817 O O   . SER   B 1 207 ? -5.237  -59.581 17.001 1.00 59.33  ? 282 SER   B O   1 
ATOM   3818 C CB  . SER   B 1 207 ? -6.491  -62.103 16.292 1.00 41.48  ? 282 SER   B CB  1 
ATOM   3819 O OG  . SER   B 1 207 ? -5.686  -62.056 15.127 1.00 67.93  ? 282 SER   B OG  1 
ATOM   3820 N N   . TYR   B 1 208 ? -3.501  -60.777 17.786 1.00 57.37  ? 283 TYR   B N   1 
ATOM   3821 C CA  . TYR   B 1 208 ? -2.558  -59.667 17.795 1.00 44.38  ? 283 TYR   B CA  1 
ATOM   3822 C C   . TYR   B 1 208 ? -1.565  -59.858 16.658 1.00 54.94  ? 283 TYR   B C   1 
ATOM   3823 O O   . TYR   B 1 208 ? -0.879  -60.883 16.594 1.00 48.48  ? 283 TYR   B O   1 
ATOM   3824 C CB  . TYR   B 1 208 ? -1.834  -59.575 19.140 1.00 45.85  ? 283 TYR   B CB  1 
ATOM   3825 C CG  . TYR   B 1 208 ? -2.768  -59.382 20.314 1.00 55.50  ? 283 TYR   B CG  1 
ATOM   3826 C CD1 . TYR   B 1 208 ? -3.367  -60.469 20.937 1.00 52.98  ? 283 TYR   B CD1 1 
ATOM   3827 C CD2 . TYR   B 1 208 ? -3.058  -58.111 20.794 1.00 63.47  ? 283 TYR   B CD2 1 
ATOM   3828 C CE1 . TYR   B 1 208 ? -4.227  -60.297 22.007 1.00 63.88  ? 283 TYR   B CE1 1 
ATOM   3829 C CE2 . TYR   B 1 208 ? -3.918  -57.929 21.864 1.00 58.04  ? 283 TYR   B CE2 1 
ATOM   3830 C CZ  . TYR   B 1 208 ? -4.498  -59.026 22.466 1.00 64.82  ? 283 TYR   B CZ  1 
ATOM   3831 O OH  . TYR   B 1 208 ? -5.354  -58.851 23.532 1.00 89.32  ? 283 TYR   B OH  1 
ATOM   3832 N N   . GLY   B 1 209 ? -1.496  -58.877 15.763 1.00 50.13  ? 284 GLY   B N   1 
ATOM   3833 C CA  . GLY   B 1 209 ? -0.579  -58.956 14.644 1.00 44.26  ? 284 GLY   B CA  1 
ATOM   3834 C C   . GLY   B 1 209 ? -0.299  -57.575 14.095 1.00 42.38  ? 284 GLY   B C   1 
ATOM   3835 O O   . GLY   B 1 209 ? -0.841  -56.572 14.563 1.00 45.99  ? 284 GLY   B O   1 
ATOM   3836 N N   . THR   B 1 210 ? 0.566   -57.539 13.078 1.00 51.02  ? 285 THR   B N   1 
ATOM   3837 C CA  . THR   B 1 210 ? 0.919   -56.266 12.460 1.00 31.08  ? 285 THR   B CA  1 
ATOM   3838 C C   . THR   B 1 210 ? -0.291  -55.601 11.820 1.00 36.64  ? 285 THR   B C   1 
ATOM   3839 O O   . THR   B 1 210 ? -0.321  -54.374 11.675 1.00 42.79  ? 285 THR   B O   1 
ATOM   3840 C CB  . THR   B 1 210 ? 2.011   -56.477 11.415 1.00 33.97  ? 285 THR   B CB  1 
ATOM   3841 O OG1 . THR   B 1 210 ? 1.562   -57.434 10.449 1.00 46.68  ? 285 THR   B OG1 1 
ATOM   3842 C CG2 . THR   B 1 210 ? 3.275   -56.994 12.074 1.00 40.75  ? 285 THR   B CG2 1 
ATOM   3843 N N   . ALA   B 1 211 ? -1.298  -56.390 11.437 1.00 42.98  ? 286 ALA   B N   1 
ATOM   3844 C CA  . ALA   B 1 211 ? -2.501  -55.829 10.835 1.00 32.99  ? 286 ALA   B CA  1 
ATOM   3845 C C   . ALA   B 1 211 ? -3.243  -54.900 11.783 1.00 42.11  ? 286 ALA   B C   1 
ATOM   3846 O O   . ALA   B 1 211 ? -4.017  -54.053 11.323 1.00 40.69  ? 286 ALA   B O   1 
ATOM   3847 C CB  . ALA   B 1 211 ? -3.432  -56.953 10.381 1.00 36.48  ? 286 ALA   B CB  1 
ATOM   3848 N N   . ALA   B 1 212 ? -3.030  -55.037 13.094 1.00 41.14  ? 287 ALA   B N   1 
ATOM   3849 C CA  . ALA   B 1 212 ? -3.725  -54.177 14.045 1.00 36.00  ? 287 ALA   B CA  1 
ATOM   3850 C C   . ALA   B 1 212 ? -3.312  -52.719 13.893 1.00 33.72  ? 287 ALA   B C   1 
ATOM   3851 O O   . ALA   B 1 212 ? -4.128  -51.819 14.122 1.00 49.63  ? 287 ALA   B O   1 
ATOM   3852 C CB  . ALA   B 1 212 ? -3.466  -54.659 15.471 1.00 36.42  ? 287 ALA   B CB  1 
ATOM   3853 N N   . ASP   B 1 213 ? -2.060  -52.463 13.508 1.00 51.25  ? 288 ASP   B N   1 
ATOM   3854 C CA  . ASP   B 1 213 ? -1.595  -51.085 13.375 1.00 33.71  ? 288 ASP   B CA  1 
ATOM   3855 C C   . ASP   B 1 213 ? -2.155  -50.428 12.118 1.00 37.76  ? 288 ASP   B C   1 
ATOM   3856 O O   . ASP   B 1 213 ? -2.497  -49.239 12.132 1.00 46.03  ? 288 ASP   B O   1 
ATOM   3857 C CB  . ASP   B 1 213 ? -0.067  -51.043 13.364 1.00 43.07  ? 288 ASP   B CB  1 
ATOM   3858 C CG  . ASP   B 1 213 ? 0.537   -51.378 14.714 1.00 52.79  ? 288 ASP   B CG  1 
ATOM   3859 O OD1 . ASP   B 1 213 ? -0.153  -51.194 15.743 1.00 40.53  ? 288 ASP   B OD1 1 
ATOM   3860 O OD2 . ASP   B 1 213 ? 1.708   -51.815 14.746 1.00 58.44  ? 288 ASP   B OD2 1 
ATOM   3861 N N   . VAL   B 1 214 ? -2.250  -51.180 11.021 1.00 39.59  ? 289 VAL   B N   1 
ATOM   3862 C CA  . VAL   B 1 214 ? -2.803  -50.627 9.788  1.00 32.35  ? 289 VAL   B CA  1 
ATOM   3863 C C   . VAL   B 1 214 ? -4.245  -50.180 10.000 1.00 36.29  ? 289 VAL   B C   1 
ATOM   3864 O O   . VAL   B 1 214 ? -4.683  -49.163 9.451  1.00 43.22  ? 289 VAL   B O   1 
ATOM   3865 C CB  . VAL   B 1 214 ? -2.689  -51.657 8.651  1.00 41.50  ? 289 VAL   B CB  1 
ATOM   3866 C CG1 . VAL   B 1 214 ? -3.378  -51.145 7.408  1.00 35.73  ? 289 VAL   B CG1 1 
ATOM   3867 C CG2 . VAL   B 1 214 ? -1.225  -51.964 8.366  1.00 40.62  ? 289 VAL   B CG2 1 
ATOM   3868 N N   . PHE   B 1 215 ? -5.006  -50.925 10.804 1.00 37.43  ? 290 PHE   B N   1 
ATOM   3869 C CA  . PHE   B 1 215 ? -6.382  -50.523 11.079 1.00 33.55  ? 290 PHE   B CA  1 
ATOM   3870 C C   . PHE   B 1 215 ? -6.418  -49.252 11.915 1.00 34.85  ? 290 PHE   B C   1 
ATOM   3871 O O   . PHE   B 1 215 ? -7.184  -48.326 11.625 1.00 45.23  ? 290 PHE   B O   1 
ATOM   3872 C CB  . PHE   B 1 215 ? -7.131  -51.651 11.782 1.00 38.51  ? 290 PHE   B CB  1 
ATOM   3873 C CG  . PHE   B 1 215 ? -8.617  -51.442 11.847 1.00 38.80  ? 290 PHE   B CG  1 
ATOM   3874 C CD1 . PHE   B 1 215 ? -9.188  -50.714 12.879 1.00 43.60  ? 290 PHE   B CD1 1 
ATOM   3875 C CD2 . PHE   B 1 215 ? -9.442  -51.981 10.878 1.00 34.48  ? 290 PHE   B CD2 1 
ATOM   3876 C CE1 . PHE   B 1 215 ? -10.555 -50.527 12.938 1.00 30.26  ? 290 PHE   B CE1 1 
ATOM   3877 C CE2 . PHE   B 1 215 ? -10.808 -51.798 10.932 1.00 35.71  ? 290 PHE   B CE2 1 
ATOM   3878 C CZ  . PHE   B 1 215 ? -11.364 -51.069 11.962 1.00 37.31  ? 290 PHE   B CZ  1 
ATOM   3879 N N   . SER   B 1 216 ? -5.594  -49.190 12.965 1.00 30.52  ? 291 SER   B N   1 
ATOM   3880 C CA  . SER   B 1 216 ? -5.540  -47.991 13.791 1.00 23.16  ? 291 SER   B CA  1 
ATOM   3881 C C   . SER   B 1 216 ? -5.136  -46.771 12.980 1.00 35.41  ? 291 SER   B C   1 
ATOM   3882 O O   . SER   B 1 216 ? -5.612  -45.661 13.246 1.00 36.14  ? 291 SER   B O   1 
ATOM   3883 C CB  . SER   B 1 216 ? -4.571  -48.201 14.949 1.00 29.75  ? 291 SER   B CB  1 
ATOM   3884 O OG  . SER   B 1 216 ? -4.978  -49.308 15.730 1.00 45.26  ? 291 SER   B OG  1 
ATOM   3885 N N   . LEU   B 1 217 ? -4.262  -46.951 11.989 1.00 34.98  ? 292 LEU   B N   1 
ATOM   3886 C CA  . LEU   B 1 217 ? -3.900  -45.832 11.130 1.00 30.80  ? 292 LEU   B CA  1 
ATOM   3887 C C   . LEU   B 1 217 ? -5.057  -45.430 10.225 1.00 31.75  ? 292 LEU   B C   1 
ATOM   3888 O O   . LEU   B 1 217 ? -5.180  -44.253 9.864  1.00 49.99  ? 292 LEU   B O   1 
ATOM   3889 C CB  . LEU   B 1 217 ? -2.668  -46.185 10.297 1.00 30.86  ? 292 LEU   B CB  1 
ATOM   3890 C CG  . LEU   B 1 217 ? -2.055  -45.016 9.530  1.00 34.43  ? 292 LEU   B CG  1 
ATOM   3891 C CD1 . LEU   B 1 217 ? -1.719  -43.901 10.502 1.00 41.86  ? 292 LEU   B CD1 1 
ATOM   3892 C CD2 . LEU   B 1 217 ? -0.820  -45.459 8.766  1.00 43.93  ? 292 LEU   B CD2 1 
ATOM   3893 N N   . GLY   B 1 218 ? -5.919  -46.381 9.857  1.00 37.10  ? 293 GLY   B N   1 
ATOM   3894 C CA  . GLY   B 1 218 ? -7.072  -46.038 9.040  1.00 26.98  ? 293 GLY   B CA  1 
ATOM   3895 C C   . GLY   B 1 218 ? -8.061  -45.152 9.775  1.00 37.88  ? 293 GLY   B C   1 
ATOM   3896 O O   . GLY   B 1 218 ? -8.593  -44.194 9.206  1.00 40.96  ? 293 GLY   B O   1 
ATOM   3897 N N   . LEU   B 1 219 ? -8.326  -45.461 11.045 1.00 35.45  ? 294 LEU   B N   1 
ATOM   3898 C CA  . LEU   B 1 219 ? -9.179  -44.592 11.847 1.00 36.11  ? 294 LEU   B CA  1 
ATOM   3899 C C   . LEU   B 1 219 ? -8.487  -43.274 12.175 1.00 33.31  ? 294 LEU   B C   1 
ATOM   3900 O O   . LEU   B 1 219 ? -9.151  -42.235 12.265 1.00 39.60  ? 294 LEU   B O   1 
ATOM   3901 C CB  . LEU   B 1 219 ? -9.593  -45.305 13.130 1.00 32.31  ? 294 LEU   B CB  1 
ATOM   3902 C CG  . LEU   B 1 219 ? -10.438 -46.559 12.932 1.00 37.26  ? 294 LEU   B CG  1 
ATOM   3903 C CD1 . LEU   B 1 219 ? -10.747 -47.172 14.275 1.00 43.92  ? 294 LEU   B CD1 1 
ATOM   3904 C CD2 . LEU   B 1 219 ? -11.714 -46.208 12.199 1.00 28.02  ? 294 LEU   B CD2 1 
ATOM   3905 N N   . THR   B 1 220 ? -7.164  -43.298 12.364 1.00 38.65  ? 295 THR   B N   1 
ATOM   3906 C CA  . THR   B 1 220 ? -6.413  -42.060 12.560 1.00 37.52  ? 295 THR   B CA  1 
ATOM   3907 C C   . THR   B 1 220 ? -6.596  -41.116 11.377 1.00 39.00  ? 295 THR   B C   1 
ATOM   3908 O O   . THR   B 1 220 ? -6.898  -39.930 11.551 1.00 48.67  ? 295 THR   B O   1 
ATOM   3909 C CB  . THR   B 1 220 ? -4.931  -42.375 12.766 1.00 39.82  ? 295 THR   B CB  1 
ATOM   3910 O OG1 . THR   B 1 220 ? -4.753  -43.077 14.005 1.00 41.18  ? 295 THR   B OG1 1 
ATOM   3911 C CG2 . THR   B 1 220 ? -4.113  -41.094 12.779 1.00 34.99  ? 295 THR   B CG2 1 
ATOM   3912 N N   . ILE   B 1 221 ? -6.413  -41.630 10.159 1.00 40.85  ? 296 ILE   B N   1 
ATOM   3913 C CA  . ILE   B 1 221 ? -6.615  -40.812 8.966  1.00 31.52  ? 296 ILE   B CA  1 
ATOM   3914 C C   . ILE   B 1 221 ? -8.074  -40.395 8.847  1.00 36.24  ? 296 ILE   B C   1 
ATOM   3915 O O   . ILE   B 1 221 ? -8.385  -39.246 8.514  1.00 48.97  ? 296 ILE   B O   1 
ATOM   3916 C CB  . ILE   B 1 221 ? -6.146  -41.577 7.716  1.00 39.99  ? 296 ILE   B CB  1 
ATOM   3917 C CG1 . ILE   B 1 221 ? -4.634  -41.806 7.773  1.00 48.11  ? 296 ILE   B CG1 1 
ATOM   3918 C CG2 . ILE   B 1 221 ? -6.551  -40.839 6.455  1.00 42.90  ? 296 ILE   B CG2 1 
ATOM   3919 C CD1 . ILE   B 1 221 ? -3.834  -40.540 7.957  1.00 49.13  ? 296 ILE   B CD1 1 
ATOM   3920 N N   . LEU   B 1 222 ? -8.994  -41.320 9.116  1.00 46.78  ? 297 LEU   B N   1 
ATOM   3921 C CA  . LEU   B 1 222 ? -10.411 -40.987 9.031  1.00 40.20  ? 297 LEU   B CA  1 
ATOM   3922 C C   . LEU   B 1 222 ? -10.808 -39.948 10.074 1.00 50.27  ? 297 LEU   B C   1 
ATOM   3923 O O   . LEU   B 1 222 ? -11.731 -39.161 9.842  1.00 54.62  ? 297 LEU   B O   1 
ATOM   3924 C CB  . LEU   B 1 222 ? -11.249 -42.255 9.185  1.00 42.07  ? 297 LEU   B CB  1 
ATOM   3925 C CG  . LEU   B 1 222 ? -12.748 -42.131 8.945  1.00 43.91  ? 297 LEU   B CG  1 
ATOM   3926 C CD1 . LEU   B 1 222 ? -13.004 -41.555 7.564  1.00 39.62  ? 297 LEU   B CD1 1 
ATOM   3927 C CD2 . LEU   B 1 222 ? -13.418 -43.491 9.103  1.00 47.02  ? 297 LEU   B CD2 1 
ATOM   3928 N N   . GLU   B 1 223 ? -10.124 -39.921 11.222 1.00 56.48  ? 298 GLU   B N   1 
ATOM   3929 C CA  . GLU   B 1 223 ? -10.447 -38.929 12.245 1.00 49.66  ? 298 GLU   B CA  1 
ATOM   3930 C C   . GLU   B 1 223 ? -9.997  -37.533 11.832 1.00 44.30  ? 298 GLU   B C   1 
ATOM   3931 O O   . GLU   B 1 223 ? -10.728 -36.555 12.031 1.00 52.13  ? 298 GLU   B O   1 
ATOM   3932 C CB  . GLU   B 1 223 ? -9.807  -39.316 13.578 1.00 47.01  ? 298 GLU   B CB  1 
ATOM   3933 C CG  . GLU   B 1 223 ? -9.924  -38.245 14.653 1.00 49.44  ? 298 GLU   B CG  1 
ATOM   3934 C CD  . GLU   B 1 223 ? -9.246  -38.639 15.951 1.00 65.11  ? 298 GLU   B CD  1 
ATOM   3935 O OE1 . GLU   B 1 223 ? -8.782  -39.793 16.056 1.00 58.75  ? 298 GLU   B OE1 1 
ATOM   3936 O OE2 . GLU   B 1 223 ? -9.176  -37.794 16.868 1.00 77.54  ? 298 GLU   B OE2 1 
ATOM   3937 N N   . VAL   B 1 224 ? -8.795  -37.414 11.267 1.00 44.92  ? 299 VAL   B N   1 
ATOM   3938 C CA  . VAL   B 1 224 ? -8.257  -36.102 10.923 1.00 33.93  ? 299 VAL   B CA  1 
ATOM   3939 C C   . VAL   B 1 224 ? -8.688  -35.621 9.543  1.00 32.66  ? 299 VAL   B C   1 
ATOM   3940 O O   . VAL   B 1 224 ? -8.692  -34.407 9.297  1.00 51.03  ? 299 VAL   B O   1 
ATOM   3941 C CB  . VAL   B 1 224 ? -6.721  -36.102 11.013 1.00 34.67  ? 299 VAL   B CB  1 
ATOM   3942 C CG1 . VAL   B 1 224 ? -6.278  -36.742 12.309 1.00 33.41  ? 299 VAL   B CG1 1 
ATOM   3943 C CG2 . VAL   B 1 224 ? -6.107  -36.828 9.823  1.00 39.57  ? 299 VAL   B CG2 1 
ATOM   3944 N N   . ALA   B 1 225 ? -9.043  -36.532 8.632  1.00 37.63  ? 300 ALA   B N   1 
ATOM   3945 C CA  . ALA   B 1 225 ? -9.513  -36.122 7.316  1.00 33.40  ? 300 ALA   B CA  1 
ATOM   3946 C C   . ALA   B 1 225 ? -10.967 -35.676 7.326  1.00 33.48  ? 300 ALA   B C   1 
ATOM   3947 O O   . ALA   B 1 225 ? -11.389 -34.966 6.407  1.00 44.95  ? 300 ALA   B O   1 
ATOM   3948 C CB  . ALA   B 1 225 ? -9.341  -37.257 6.304  1.00 44.47  ? 300 ALA   B CB  1 
ATOM   3949 N N   . CYS   B 1 226 ? -11.742 -36.078 8.333  1.00 47.62  ? 301 CYS   B N   1 
ATOM   3950 C CA  . CYS   B 1 226 ? -13.149 -35.716 8.422  1.00 44.43  ? 301 CYS   B CA  1 
ATOM   3951 C C   . CYS   B 1 226 ? -13.476 -34.942 9.688  1.00 48.63  ? 301 CYS   B C   1 
ATOM   3952 O O   . CYS   B 1 226 ? -14.621 -34.499 9.848  1.00 66.19  ? 301 CYS   B O   1 
ATOM   3953 C CB  . CYS   B 1 226 ? -14.027 -36.971 8.346  1.00 59.72  ? 301 CYS   B CB  1 
ATOM   3954 S SG  . CYS   B 1 226 ? -13.623 -38.057 6.959  1.00 67.32  ? 301 CYS   B SG  1 
ATOM   3955 N N   . ASN   B 1 227 ? -12.506 -34.766 10.586 1.00 43.38  ? 302 ASN   B N   1 
ATOM   3956 C CA  . ASN   B 1 227 ? -12.698 -34.031 11.836 1.00 49.62  ? 302 ASN   B CA  1 
ATOM   3957 C C   . ASN   B 1 227 ? -13.845 -34.620 12.650 1.00 56.27  ? 302 ASN   B C   1 
ATOM   3958 O O   . ASN   B 1 227 ? -14.680 -33.899 13.199 1.00 56.89  ? 302 ASN   B O   1 
ATOM   3959 C CB  . ASN   B 1 227 ? -12.926 -32.542 11.576 1.00 50.76  ? 302 ASN   B CB  1 
ATOM   3960 C CG  . ASN   B 1 227 ? -12.778 -31.709 12.832 1.00 54.97  ? 302 ASN   B CG  1 
ATOM   3961 O OD1 . ASN   B 1 227 ? -12.086 -32.107 13.769 1.00 54.77  ? 302 ASN   B OD1 1 
ATOM   3962 N ND2 . ASN   B 1 227 ? -13.432 -30.554 12.863 1.00 52.05  ? 302 ASN   B ND2 1 
ATOM   3963 N N   . MET   B 1 228 ? -13.898 -35.943 12.717 1.00 48.09  ? 303 MET   B N   1 
ATOM   3964 C CA  . MET   B 1 228 ? -14.933 -36.627 13.471 1.00 65.91  ? 303 MET   B CA  1 
ATOM   3965 C C   . MET   B 1 228 ? -14.324 -37.271 14.708 1.00 56.54  ? 303 MET   B C   1 
ATOM   3966 O O   . MET   B 1 228 ? -13.134 -37.595 14.739 1.00 51.14  ? 303 MET   B O   1 
ATOM   3967 C CB  . MET   B 1 228 ? -15.639 -37.686 12.620 1.00 65.44  ? 303 MET   B CB  1 
ATOM   3968 C CG  . MET   B 1 228 ? -14.858 -38.975 12.441 1.00 60.99  ? 303 MET   B CG  1 
ATOM   3969 S SD  . MET   B 1 228 ? -15.888 -40.296 11.774 1.00 79.12  ? 303 MET   B SD  1 
ATOM   3970 C CE  . MET   B 1 228 ? -17.233 -40.315 12.960 1.00 70.30  ? 303 MET   B CE  1 
ATOM   3971 N N   . GLU   B 1 229 ? -15.152 -37.436 15.736 1.00 54.96  ? 304 GLU   B N   1 
ATOM   3972 C CA  . GLU   B 1 229 ? -14.733 -38.086 16.968 1.00 43.42  ? 304 GLU   B CA  1 
ATOM   3973 C C   . GLU   B 1 229 ? -14.993 -39.584 16.877 1.00 62.44  ? 304 GLU   B C   1 
ATOM   3974 O O   . GLU   B 1 229 ? -16.014 -40.021 16.338 1.00 57.64  ? 304 GLU   B O   1 
ATOM   3975 C CB  . GLU   B 1 229 ? -15.472 -37.498 18.171 1.00 54.34  ? 304 GLU   B CB  1 
ATOM   3976 C CG  . GLU   B 1 229 ? -15.155 -38.186 19.493 1.00 96.68  ? 304 GLU   B CG  1 
ATOM   3977 C CD  . GLU   B 1 229 ? -16.013 -37.684 20.637 1.00 112.65 ? 304 GLU   B CD  1 
ATOM   3978 O OE1 . GLU   B 1 229 ? -16.305 -36.471 20.673 1.00 127.49 ? 304 GLU   B OE1 1 
ATOM   3979 O OE2 . GLU   B 1 229 ? -16.400 -38.505 21.497 1.00 109.79 ? 304 GLU   B OE2 1 
ATOM   3980 N N   . LEU   B 1 230 ? -14.062 -40.367 17.405 1.00 55.16  ? 305 LEU   B N   1 
ATOM   3981 C CA  . LEU   B 1 230 ? -14.200 -41.817 17.349 1.00 33.93  ? 305 LEU   B CA  1 
ATOM   3982 C C   . LEU   B 1 230 ? -14.896 -42.327 18.606 1.00 54.14  ? 305 LEU   B C   1 
ATOM   3983 O O   . LEU   B 1 230 ? -14.537 -41.915 19.716 1.00 55.45  ? 305 LEU   B O   1 
ATOM   3984 C CB  . LEU   B 1 230 ? -12.839 -42.482 17.207 1.00 38.08  ? 305 LEU   B CB  1 
ATOM   3985 C CG  . LEU   B 1 230 ? -12.130 -42.224 15.880 1.00 27.35  ? 305 LEU   B CG  1 
ATOM   3986 C CD1 . LEU   B 1 230 ? -10.844 -43.022 15.792 1.00 34.59  ? 305 LEU   B CD1 1 
ATOM   3987 C CD2 . LEU   B 1 230 ? -13.050 -42.577 14.732 1.00 33.10  ? 305 LEU   B CD2 1 
ATOM   3988 N N   . PRO   B 1 231 ? -15.882 -43.211 18.472 1.00 39.03  ? 306 PRO   B N   1 
ATOM   3989 C CA  . PRO   B 1 231 ? -16.605 -43.695 19.652 1.00 43.10  ? 306 PRO   B CA  1 
ATOM   3990 C C   . PRO   B 1 231 ? -15.784 -44.695 20.450 1.00 39.18  ? 306 PRO   B C   1 
ATOM   3991 O O   . PRO   B 1 231 ? -14.958 -45.431 19.906 1.00 41.77  ? 306 PRO   B O   1 
ATOM   3992 C CB  . PRO   B 1 231 ? -17.851 -44.354 19.051 1.00 40.12  ? 306 PRO   B CB  1 
ATOM   3993 C CG  . PRO   B 1 231 ? -17.407 -44.792 17.695 1.00 46.41  ? 306 PRO   B CG  1 
ATOM   3994 C CD  . PRO   B 1 231 ? -16.439 -43.746 17.219 1.00 43.48  ? 306 PRO   B CD  1 
ATOM   3995 N N   . HIS   B 1 232 ? -16.027 -44.709 21.765 1.00 56.00  ? 307 HIS   B N   1 
ATOM   3996 C CA  . HIS   B 1 232 ? -15.353 -45.652 22.651 1.00 46.42  ? 307 HIS   B CA  1 
ATOM   3997 C C   . HIS   B 1 232 ? -15.998 -47.030 22.615 1.00 51.63  ? 307 HIS   B C   1 
ATOM   3998 O O   . HIS   B 1 232 ? -15.337 -48.028 22.920 1.00 48.05  ? 307 HIS   B O   1 
ATOM   3999 C CB  . HIS   B 1 232 ? -15.361 -45.131 24.091 1.00 60.41  ? 307 HIS   B CB  1 
ATOM   4000 C CG  . HIS   B 1 232 ? -14.499 -43.924 24.309 1.00 70.42  ? 307 HIS   B CG  1 
ATOM   4001 N ND1 . HIS   B 1 232 ? -15.012 -42.649 24.429 1.00 75.71  ? 307 HIS   B ND1 1 
ATOM   4002 C CD2 . HIS   B 1 232 ? -13.158 -43.802 24.447 1.00 62.37  ? 307 HIS   B CD2 1 
ATOM   4003 C CE1 . HIS   B 1 232 ? -14.023 -41.794 24.622 1.00 72.42  ? 307 HIS   B CE1 1 
ATOM   4004 N NE2 . HIS   B 1 232 ? -12.887 -42.467 24.636 1.00 71.38  ? 307 HIS   B NE2 1 
ATOM   4005 N N   . GLY   B 1 233 ? -17.270 -47.107 22.260 1.00 48.97  ? 308 GLY   B N   1 
ATOM   4006 C CA  . GLY   B 1 233 ? -17.958 -48.376 22.265 1.00 47.49  ? 308 GLY   B CA  1 
ATOM   4007 C C   . GLY   B 1 233 ? -19.345 -48.237 21.690 1.00 50.30  ? 308 GLY   B C   1 
ATOM   4008 O O   . GLY   B 1 233 ? -19.659 -47.256 21.015 1.00 64.93  ? 308 GLY   B O   1 
ATOM   4009 N N   . GLY   B 1 234 ? -20.172 -49.238 21.965 1.00 44.67  ? 309 GLY   B N   1 
ATOM   4010 C CA  . GLY   B 1 234 ? -21.541 -49.175 21.499 1.00 61.35  ? 309 GLY   B CA  1 
ATOM   4011 C C   . GLY   B 1 234 ? -21.649 -49.370 19.993 1.00 52.93  ? 309 GLY   B C   1 
ATOM   4012 O O   . GLY   B 1 234 ? -20.734 -49.862 19.326 1.00 53.06  ? 309 GLY   B O   1 
ATOM   4013 N N   . GLU   B 1 235 ? -22.803 -48.958 19.457 1.00 53.29  ? 310 GLU   B N   1 
ATOM   4014 C CA  . GLU   B 1 235 ? -23.092 -49.198 18.046 1.00 56.11  ? 310 GLU   B CA  1 
ATOM   4015 C C   . GLU   B 1 235 ? -22.153 -48.416 17.140 1.00 53.85  ? 310 GLU   B C   1 
ATOM   4016 O O   . GLU   B 1 235 ? -21.686 -48.941 16.120 1.00 62.16  ? 310 GLU   B O   1 
ATOM   4017 C CB  . GLU   B 1 235 ? -24.547 -48.849 17.737 1.00 58.97  ? 310 GLU   B CB  1 
ATOM   4018 C CG  . GLU   B 1 235 ? -25.492 -50.038 17.817 1.00 92.37  ? 310 GLU   B CG  1 
ATOM   4019 C CD  . GLU   B 1 235 ? -25.128 -51.143 16.838 1.00 110.15 ? 310 GLU   B CD  1 
ATOM   4020 O OE1 . GLU   B 1 235 ? -24.562 -50.834 15.767 1.00 109.20 ? 310 GLU   B OE1 1 
ATOM   4021 O OE2 . GLU   B 1 235 ? -25.403 -52.324 17.141 1.00 105.23 ? 310 GLU   B OE2 1 
ATOM   4022 N N   . GLY   B 1 236 ? -21.868 -47.157 17.485 1.00 46.26  ? 311 GLY   B N   1 
ATOM   4023 C CA  . GLY   B 1 236 ? -20.960 -46.370 16.668 1.00 47.11  ? 311 GLY   B CA  1 
ATOM   4024 C C   . GLY   B 1 236 ? -19.601 -47.019 16.520 1.00 44.08  ? 311 GLY   B C   1 
ATOM   4025 O O   . GLY   B 1 236 ? -18.967 -46.910 15.467 1.00 53.92  ? 311 GLY   B O   1 
ATOM   4026 N N   . TRP   B 1 237 ? -19.138 -47.700 17.568 1.00 50.79  ? 312 TRP   B N   1 
ATOM   4027 C CA  . TRP   B 1 237 ? -17.895 -48.459 17.484 1.00 45.35  ? 312 TRP   B CA  1 
ATOM   4028 C C   . TRP   B 1 237 ? -18.026 -49.616 16.501 1.00 44.42  ? 312 TRP   B C   1 
ATOM   4029 O O   . TRP   B 1 237 ? -17.090 -49.910 15.747 1.00 44.58  ? 312 TRP   B O   1 
ATOM   4030 C CB  . TRP   B 1 237 ? -17.515 -48.970 18.874 1.00 45.26  ? 312 TRP   B CB  1 
ATOM   4031 C CG  . TRP   B 1 237 ? -16.139 -49.541 18.976 1.00 33.57  ? 312 TRP   B CG  1 
ATOM   4032 C CD1 . TRP   B 1 237 ? -14.992 -48.865 19.286 1.00 37.80  ? 312 TRP   B CD1 1 
ATOM   4033 C CD2 . TRP   B 1 237 ? -15.760 -50.908 18.780 1.00 31.11  ? 312 TRP   B CD2 1 
ATOM   4034 N NE1 . TRP   B 1 237 ? -13.922 -49.727 19.289 1.00 31.23  ? 312 TRP   B NE1 1 
ATOM   4035 C CE2 . TRP   B 1 237 ? -14.367 -50.987 18.978 1.00 36.61  ? 312 TRP   B CE2 1 
ATOM   4036 C CE3 . TRP   B 1 237 ? -16.462 -52.071 18.449 1.00 38.35  ? 312 TRP   B CE3 1 
ATOM   4037 C CZ2 . TRP   B 1 237 ? -13.664 -52.188 18.862 1.00 31.47  ? 312 TRP   B CZ2 1 
ATOM   4038 C CZ3 . TRP   B 1 237 ? -15.763 -53.262 18.333 1.00 32.53  ? 312 TRP   B CZ3 1 
ATOM   4039 C CH2 . TRP   B 1 237 ? -14.376 -53.310 18.538 1.00 37.76  ? 312 TRP   B CH2 1 
ATOM   4040 N N   . GLN   B 1 238 ? -19.183 -50.277 16.491 1.00 47.76  ? 313 GLN   B N   1 
ATOM   4041 C CA  . GLN   B 1 238 ? -19.378 -51.422 15.609 1.00 42.57  ? 313 GLN   B CA  1 
ATOM   4042 C C   . GLN   B 1 238 ? -19.451 -50.994 14.149 1.00 47.77  ? 313 GLN   B C   1 
ATOM   4043 O O   . GLN   B 1 238 ? -18.836 -51.625 13.281 1.00 53.42  ? 313 GLN   B O   1 
ATOM   4044 C CB  . GLN   B 1 238 ? -20.647 -52.175 16.006 1.00 48.80  ? 313 GLN   B CB  1 
ATOM   4045 C CG  . GLN   B 1 238 ? -20.713 -52.571 17.471 1.00 43.40  ? 313 GLN   B CG  1 
ATOM   4046 C CD  . GLN   B 1 238 ? -19.809 -53.742 17.805 1.00 55.43  ? 313 GLN   B CD  1 
ATOM   4047 O OE1 . GLN   B 1 238 ? -19.177 -54.325 16.925 1.00 57.48  ? 313 GLN   B OE1 1 
ATOM   4048 N NE2 . GLN   B 1 238 ? -19.748 -54.095 19.083 1.00 69.67  ? 313 GLN   B NE2 1 
ATOM   4049 N N   . GLN   B 1 239 ? -20.198 -49.925 13.859 1.00 46.59  ? 314 GLN   B N   1 
ATOM   4050 C CA  . GLN   B 1 239 ? -20.399 -49.506 12.476 1.00 53.53  ? 314 GLN   B CA  1 
ATOM   4051 C C   . GLN   B 1 239 ? -19.085 -49.150 11.791 1.00 45.00  ? 314 GLN   B C   1 
ATOM   4052 O O   . GLN   B 1 239 ? -18.940 -49.367 10.583 1.00 60.39  ? 314 GLN   B O   1 
ATOM   4053 C CB  . GLN   B 1 239 ? -21.365 -48.323 12.426 1.00 51.63  ? 314 GLN   B CB  1 
ATOM   4054 C CG  . GLN   B 1 239 ? -22.758 -48.647 12.937 1.00 62.64  ? 314 GLN   B CG  1 
ATOM   4055 C CD  . GLN   B 1 239 ? -23.664 -47.433 12.953 1.00 81.73  ? 314 GLN   B CD  1 
ATOM   4056 O OE1 . GLN   B 1 239 ? -23.204 -46.300 12.809 1.00 75.64  ? 314 GLN   B OE1 1 
ATOM   4057 N NE2 . GLN   B 1 239 ? -24.960 -47.664 13.125 1.00 89.72  ? 314 GLN   B NE2 1 
ATOM   4058 N N   . LEU   B 1 240 ? -18.119 -48.613 12.535 1.00 47.77  ? 315 LEU   B N   1 
ATOM   4059 C CA  . LEU   B 1 240 ? -16.805 -48.331 11.969 1.00 39.82  ? 315 LEU   B CA  1 
ATOM   4060 C C   . LEU   B 1 240 ? -15.986 -49.586 11.711 1.00 49.83  ? 315 LEU   B C   1 
ATOM   4061 O O   . LEU   B 1 240 ? -14.870 -49.476 11.190 1.00 50.50  ? 315 LEU   B O   1 
ATOM   4062 C CB  . LEU   B 1 240 ? -16.016 -47.403 12.894 1.00 36.06  ? 315 LEU   B CB  1 
ATOM   4063 C CG  . LEU   B 1 240 ? -16.429 -45.935 12.937 1.00 33.22  ? 315 LEU   B CG  1 
ATOM   4064 C CD1 . LEU   B 1 240 ? -15.584 -45.188 13.949 1.00 36.04  ? 315 LEU   B CD1 1 
ATOM   4065 C CD2 . LEU   B 1 240 ? -16.284 -45.315 11.564 1.00 47.53  ? 315 LEU   B CD2 1 
ATOM   4066 N N   . ARG   B 1 241 ? -16.496 -50.766 12.065 1.00 45.34  ? 316 ARG   B N   1 
ATOM   4067 C CA  . ARG   B 1 241 ? -15.742 -52.006 11.934 1.00 38.15  ? 316 ARG   B CA  1 
ATOM   4068 C C   . ARG   B 1 241 ? -16.559 -53.076 11.225 1.00 43.46  ? 316 ARG   B C   1 
ATOM   4069 O O   . ARG   B 1 241 ? -16.441 -54.264 11.535 1.00 48.96  ? 316 ARG   B O   1 
ATOM   4070 C CB  . ARG   B 1 241 ? -15.274 -52.494 13.303 1.00 35.36  ? 316 ARG   B CB  1 
ATOM   4071 C CG  . ARG   B 1 241 ? -14.220 -51.583 13.902 1.00 39.69  ? 316 ARG   B CG  1 
ATOM   4072 C CD  . ARG   B 1 241 ? -14.135 -51.680 15.406 1.00 36.70  ? 316 ARG   B CD  1 
ATOM   4073 N NE  . ARG   B 1 241 ? -13.081 -50.816 15.928 1.00 35.38  ? 316 ARG   B NE  1 
ATOM   4074 C CZ  . ARG   B 1 241 ? -13.231 -49.521 16.166 1.00 35.43  ? 316 ARG   B CZ  1 
ATOM   4075 N NH1 . ARG   B 1 241 ? -14.376 -48.902 15.927 1.00 40.30  ? 316 ARG   B NH1 1 
ATOM   4076 N NH2 . ARG   B 1 241 ? -12.209 -48.829 16.661 1.00 36.61  ? 316 ARG   B NH2 1 
ATOM   4077 N N   . GLN   B 1 242 ? -17.393 -52.669 10.270 1.00 61.31  ? 317 GLN   B N   1 
ATOM   4078 C CA  . GLN   B 1 242 ? -18.159 -53.598 9.453  1.00 52.81  ? 317 GLN   B CA  1 
ATOM   4079 C C   . GLN   B 1 242 ? -17.609 -53.725 8.041  1.00 43.43  ? 317 GLN   B C   1 
ATOM   4080 O O   . GLN   B 1 242 ? -18.128 -54.529 7.260  1.00 57.80  ? 317 GLN   B O   1 
ATOM   4081 C CB  . GLN   B 1 242 ? -19.627 -53.165 9.387  1.00 63.86  ? 317 GLN   B CB  1 
ATOM   4082 C CG  . GLN   B 1 242 ? -20.293 -52.985 10.735 1.00 66.29  ? 317 GLN   B CG  1 
ATOM   4083 C CD  . GLN   B 1 242 ? -20.555 -54.300 11.434 1.00 64.45  ? 317 GLN   B CD  1 
ATOM   4084 O OE1 . GLN   B 1 242 ? -21.571 -54.951 11.192 1.00 78.80  ? 317 GLN   B OE1 1 
ATOM   4085 N NE2 . GLN   B 1 242 ? -19.639 -54.699 12.308 1.00 72.91  ? 317 GLN   B NE2 1 
ATOM   4086 N N   . GLY   B 1 243 ? -16.583 -52.952 7.690  1.00 46.56  ? 318 GLY   B N   1 
ATOM   4087 C CA  . GLY   B 1 243 ? -16.007 -52.983 6.365  1.00 65.31  ? 318 GLY   B CA  1 
ATOM   4088 C C   . GLY   B 1 243 ? -16.398 -51.824 5.473  1.00 72.58  ? 318 GLY   B C   1 
ATOM   4089 O O   . GLY   B 1 243 ? -15.818 -51.677 4.391  1.00 86.39  ? 318 GLY   B O   1 
ATOM   4090 N N   . TYR   B 1 244 ? -17.355 -51.001 5.890  1.00 76.26  ? 319 TYR   B N   1 
ATOM   4091 C CA  . TYR   B 1 244 ? -17.787 -49.851 5.111  1.00 67.45  ? 319 TYR   B CA  1 
ATOM   4092 C C   . TYR   B 1 244 ? -17.436 -48.551 5.825  1.00 74.54  ? 319 TYR   B C   1 
ATOM   4093 O O   . TYR   B 1 244 ? -17.287 -48.504 7.049  1.00 80.99  ? 319 TYR   B O   1 
ATOM   4094 C CB  . TYR   B 1 244 ? -19.295 -49.906 4.829  1.00 58.31  ? 319 TYR   B CB  1 
ATOM   4095 C CG  . TYR   B 1 244 ? -20.189 -49.996 6.054  1.00 80.16  ? 319 TYR   B CG  1 
ATOM   4096 C CD1 . TYR   B 1 244 ? -20.384 -48.898 6.887  1.00 86.02  ? 319 TYR   B CD1 1 
ATOM   4097 C CD2 . TYR   B 1 244 ? -20.865 -51.171 6.358  1.00 82.52  ? 319 TYR   B CD2 1 
ATOM   4098 C CE1 . TYR   B 1 244 ? -21.206 -48.975 8.000  1.00 82.12  ? 319 TYR   B CE1 1 
ATOM   4099 C CE2 . TYR   B 1 244 ? -21.694 -51.255 7.466  1.00 94.62  ? 319 TYR   B CE2 1 
ATOM   4100 C CZ  . TYR   B 1 244 ? -21.859 -50.155 8.285  1.00 100.59 ? 319 TYR   B CZ  1 
ATOM   4101 O OH  . TYR   B 1 244 ? -22.681 -50.239 9.388  1.00 96.22  ? 319 TYR   B OH  1 
ATOM   4102 N N   . LEU   B 1 245 ? -17.301 -47.493 5.038  1.00 71.76  ? 320 LEU   B N   1 
ATOM   4103 C CA  . LEU   B 1 245 ? -17.111 -46.155 5.585  1.00 76.12  ? 320 LEU   B CA  1 
ATOM   4104 C C   . LEU   B 1 245 ? -18.467 -45.494 5.795  1.00 84.70  ? 320 LEU   B C   1 
ATOM   4105 O O   . LEU   B 1 245 ? -19.299 -45.506 4.879  1.00 86.96  ? 320 LEU   B O   1 
ATOM   4106 C CB  . LEU   B 1 245 ? -16.270 -45.300 4.647  1.00 76.25  ? 320 LEU   B CB  1 
ATOM   4107 C CG  . LEU   B 1 245 ? -14.901 -45.837 4.229  1.00 71.19  ? 320 LEU   B CG  1 
ATOM   4108 C CD1 . LEU   B 1 245 ? -14.321 -44.993 3.107  1.00 67.62  ? 320 LEU   B CD1 1 
ATOM   4109 C CD2 . LEU   B 1 245 ? -13.961 -45.859 5.415  1.00 65.63  ? 320 LEU   B CD2 1 
ATOM   4110 N N   . PRO   B 1 246 ? -18.735 -44.934 6.971  1.00 101.40 ? 321 PRO   B N   1 
ATOM   4111 C CA  . PRO   B 1 246 ? -19.981 -44.186 7.174  1.00 109.17 ? 321 PRO   B CA  1 
ATOM   4112 C C   . PRO   B 1 246 ? -20.091 -43.045 6.180  1.00 106.30 ? 321 PRO   B C   1 
ATOM   4113 O O   . PRO   B 1 246 ? -19.275 -42.110 6.201  1.00 97.07  ? 321 PRO   B O   1 
ATOM   4114 C CB  . PRO   B 1 246 ? -19.850 -43.667 8.613  1.00 101.64 ? 321 PRO   B CB  1 
ATOM   4115 C CG  . PRO   B 1 246 ? -18.958 -44.656 9.275  1.00 90.26  ? 321 PRO   B CG  1 
ATOM   4116 C CD  . PRO   B 1 246 ? -17.967 -45.074 8.220  1.00 90.03  ? 321 PRO   B CD  1 
ATOM   4117 N N   . PRO   B 1 247 ? -21.090 -43.084 5.292  1.00 86.88  ? 322 PRO   B N   1 
ATOM   4118 C CA  . PRO   B 1 247 ? -21.141 -42.109 4.191  1.00 77.31  ? 322 PRO   B CA  1 
ATOM   4119 C C   . PRO   B 1 247 ? -21.404 -40.684 4.637  1.00 85.21  ? 322 PRO   B C   1 
ATOM   4120 O O   . PRO   B 1 247 ? -21.277 -39.768 3.814  1.00 85.70  ? 322 PRO   B O   1 
ATOM   4121 C CB  . PRO   B 1 247 ? -22.287 -42.633 3.317  1.00 80.93  ? 322 PRO   B CB  1 
ATOM   4122 C CG  . PRO   B 1 247 ? -23.173 -43.366 4.272  1.00 85.50  ? 322 PRO   B CG  1 
ATOM   4123 C CD  . PRO   B 1 247 ? -22.249 -43.994 5.284  1.00 83.45  ? 322 PRO   B CD  1 
ATOM   4124 N N   . GLU   B 1 248 ? -21.760 -40.465 5.902  1.00 87.06  ? 323 GLU   B N   1 
ATOM   4125 C CA  . GLU   B 1 248 ? -22.060 -39.116 6.369  1.00 87.02  ? 323 GLU   B CA  1 
ATOM   4126 C C   . GLU   B 1 248 ? -20.810 -38.241 6.377  1.00 101.65 ? 323 GLU   B C   1 
ATOM   4127 O O   . GLU   B 1 248 ? -20.766 -37.191 5.726  1.00 97.47  ? 323 GLU   B O   1 
ATOM   4128 C CB  . GLU   B 1 248 ? -22.696 -39.178 7.759  1.00 91.62  ? 323 GLU   B CB  1 
ATOM   4129 C CG  . GLU   B 1 248 ? -22.074 -40.215 8.682  1.00 83.48  ? 323 GLU   B CG  1 
ATOM   4130 C CD  . GLU   B 1 248 ? -22.621 -40.143 10.090 1.00 107.13 ? 323 GLU   B CD  1 
ATOM   4131 O OE1 . GLU   B 1 248 ? -23.559 -39.350 10.324 1.00 108.75 ? 323 GLU   B OE1 1 
ATOM   4132 O OE2 . GLU   B 1 248 ? -22.112 -40.876 10.964 1.00 115.03 ? 323 GLU   B OE2 1 
ATOM   4133 N N   . PHE   B 1 249 ? -19.775 -38.663 7.106  1.00 100.34 ? 324 PHE   B N   1 
ATOM   4134 C CA  . PHE   B 1 249 ? -18.569 -37.859 7.253  1.00 87.27  ? 324 PHE   B CA  1 
ATOM   4135 C C   . PHE   B 1 249 ? -17.569 -38.055 6.122  1.00 85.08  ? 324 PHE   B C   1 
ATOM   4136 O O   . PHE   B 1 249 ? -16.695 -37.201 5.935  1.00 81.95  ? 324 PHE   B O   1 
ATOM   4137 C CB  . PHE   B 1 249 ? -17.883 -38.168 8.588  1.00 79.92  ? 324 PHE   B CB  1 
ATOM   4138 C CG  . PHE   B 1 249 ? -18.680 -37.751 9.790  1.00 91.13  ? 324 PHE   B CG  1 
ATOM   4139 C CD1 . PHE   B 1 249 ? -18.699 -36.427 10.198 1.00 89.39  ? 324 PHE   B CD1 1 
ATOM   4140 C CD2 . PHE   B 1 249 ? -19.409 -38.681 10.512 1.00 90.82  ? 324 PHE   B CD2 1 
ATOM   4141 C CE1 . PHE   B 1 249 ? -19.432 -36.037 11.303 1.00 89.29  ? 324 PHE   B CE1 1 
ATOM   4142 C CE2 . PHE   B 1 249 ? -20.144 -38.298 11.618 1.00 94.48  ? 324 PHE   B CE2 1 
ATOM   4143 C CZ  . PHE   B 1 249 ? -20.155 -36.974 12.014 1.00 90.18  ? 324 PHE   B CZ  1 
ATOM   4144 N N   . THR   B 1 250 ? -17.672 -39.147 5.365  1.00 86.36  ? 325 THR   B N   1 
ATOM   4145 C CA  . THR   B 1 250 ? -16.741 -39.437 4.283  1.00 86.34  ? 325 THR   B CA  1 
ATOM   4146 C C   . THR   B 1 250 ? -17.140 -38.780 2.965  1.00 80.60  ? 325 THR   B C   1 
ATOM   4147 O O   . THR   B 1 250 ? -16.622 -39.166 1.911  1.00 88.41  ? 325 THR   B O   1 
ATOM   4148 C CB  . THR   B 1 250 ? -16.611 -40.949 4.090  1.00 78.65  ? 325 THR   B CB  1 
ATOM   4149 O OG1 . THR   B 1 250 ? -17.904 -41.510 3.827  1.00 95.54  ? 325 THR   B OG1 1 
ATOM   4150 C CG2 . THR   B 1 250 ? -16.028 -41.595 5.335  1.00 86.53  ? 325 THR   B CG2 1 
ATOM   4151 N N   . ALA   B 1 251 ? -18.040 -37.795 3.001  1.00 79.06  ? 326 ALA   B N   1 
ATOM   4152 C CA  . ALA   B 1 251 ? -18.523 -37.186 1.765  1.00 92.30  ? 326 ALA   B CA  1 
ATOM   4153 C C   . ALA   B 1 251 ? -17.416 -36.422 1.048  1.00 89.04  ? 326 ALA   B C   1 
ATOM   4154 O O   . ALA   B 1 251 ? -17.160 -36.648 -0.140 1.00 94.32  ? 326 ALA   B O   1 
ATOM   4155 C CB  . ALA   B 1 251 ? -19.709 -36.268 2.061  1.00 80.60  ? 326 ALA   B CB  1 
ATOM   4156 N N   . GLY   B 1 252 ? -16.748 -35.511 1.754  1.00 85.11  ? 327 GLY   B N   1 
ATOM   4157 C CA  . GLY   B 1 252 ? -15.732 -34.675 1.137  1.00 83.40  ? 327 GLY   B CA  1 
ATOM   4158 C C   . GLY   B 1 252 ? -14.445 -35.388 0.775  1.00 76.06  ? 327 GLY   B C   1 
ATOM   4159 O O   . GLY   B 1 252 ? -13.573 -34.768 0.160  1.00 80.55  ? 327 GLY   B O   1 
ATOM   4160 N N   . LEU   B 1 253 ? -14.303 -36.659 1.135  1.00 73.15  ? 328 LEU   B N   1 
ATOM   4161 C CA  . LEU   B 1 253 ? -13.092 -37.393 0.808  1.00 58.58  ? 328 LEU   B CA  1 
ATOM   4162 C C   . LEU   B 1 253 ? -13.052 -37.719 -0.680 1.00 69.67  ? 328 LEU   B C   1 
ATOM   4163 O O   . LEU   B 1 253 ? -14.071 -38.059 -1.288 1.00 63.57  ? 328 LEU   B O   1 
ATOM   4164 C CB  . LEU   B 1 253 ? -13.020 -38.679 1.629  1.00 71.70  ? 328 LEU   B CB  1 
ATOM   4165 C CG  . LEU   B 1 253 ? -13.074 -38.521 3.150  1.00 68.21  ? 328 LEU   B CG  1 
ATOM   4166 C CD1 . LEU   B 1 253 ? -12.918 -39.869 3.834  1.00 65.38  ? 328 LEU   B CD1 1 
ATOM   4167 C CD2 . LEU   B 1 253 ? -12.008 -37.548 3.622  1.00 70.52  ? 328 LEU   B CD2 1 
ATOM   4168 N N   . SER   B 1 254 ? -11.862 -37.614 -1.269 1.00 54.07  ? 329 SER   B N   1 
ATOM   4169 C CA  . SER   B 1 254 ? -11.702 -37.956 -2.672 1.00 62.06  ? 329 SER   B CA  1 
ATOM   4170 C C   . SER   B 1 254 ? -11.890 -39.454 -2.886 1.00 62.77  ? 329 SER   B C   1 
ATOM   4171 O O   . SER   B 1 254 ? -11.870 -40.252 -1.945 1.00 58.29  ? 329 SER   B O   1 
ATOM   4172 C CB  . SER   B 1 254 ? -10.323 -37.543 -3.185 1.00 65.12  ? 329 SER   B CB  1 
ATOM   4173 O OG  . SER   B 1 254 ? -9.313  -38.379 -2.644 1.00 56.04  ? 329 SER   B OG  1 
ATOM   4174 N N   . SER   B 1 255 ? -12.065 -39.831 -4.155 1.00 61.84  ? 330 SER   B N   1 
ATOM   4175 C CA  . SER   B 1 255 ? -12.234 -41.242 -4.478 1.00 64.33  ? 330 SER   B CA  1 
ATOM   4176 C C   . SER   B 1 255 ? -10.986 -42.045 -4.128 1.00 58.93  ? 330 SER   B C   1 
ATOM   4177 O O   . SER   B 1 255 ? -11.084 -43.213 -3.731 1.00 66.39  ? 330 SER   B O   1 
ATOM   4178 C CB  . SER   B 1 255 ? -12.579 -41.403 -5.959 1.00 55.81  ? 330 SER   B CB  1 
ATOM   4179 O OG  . SER   B 1 255 ? -12.759 -42.771 -6.286 1.00 77.27  ? 330 SER   B OG  1 
ATOM   4180 N N   . GLU   B 1 256 ? -9.804  -41.439 -4.262 1.00 72.47  ? 331 GLU   B N   1 
ATOM   4181 C CA  . GLU   B 1 256 ? -8.568  -42.160 -3.973 1.00 48.68  ? 331 GLU   B CA  1 
ATOM   4182 C C   . GLU   B 1 256 ? -8.406  -42.412 -2.481 1.00 51.46  ? 331 GLU   B C   1 
ATOM   4183 O O   . GLU   B 1 256 ? -7.964  -43.493 -2.073 1.00 63.08  ? 331 GLU   B O   1 
ATOM   4184 C CB  . GLU   B 1 256 ? -7.362  -41.392 -4.520 1.00 53.67  ? 331 GLU   B CB  1 
ATOM   4185 C CG  . GLU   B 1 256 ? -7.247  -41.373 -6.044 1.00 62.50  ? 331 GLU   B CG  1 
ATOM   4186 C CD  . GLU   B 1 256 ? -8.212  -40.403 -6.702 1.00 86.74  ? 331 GLU   B CD  1 
ATOM   4187 O OE1 . GLU   B 1 256 ? -8.752  -39.526 -5.994 1.00 76.05  ? 331 GLU   B OE1 1 
ATOM   4188 O OE2 . GLU   B 1 256 ? -8.430  -40.518 -7.929 1.00 104.92 ? 331 GLU   B OE2 1 
ATOM   4189 N N   . LEU   B 1 257 ? -8.753  -41.429 -1.648 1.00 49.41  ? 332 LEU   B N   1 
ATOM   4190 C CA  . LEU   B 1 257 ? -8.600  -41.606 -0.208 1.00 43.78  ? 332 LEU   B CA  1 
ATOM   4191 C C   . LEU   B 1 257 ? -9.607  -42.611 0.337  1.00 47.42  ? 332 LEU   B C   1 
ATOM   4192 O O   . LEU   B 1 257 ? -9.263  -43.437 1.190  1.00 50.74  ? 332 LEU   B O   1 
ATOM   4193 C CB  . LEU   B 1 257 ? -8.737  -40.264 0.511  1.00 45.76  ? 332 LEU   B CB  1 
ATOM   4194 C CG  . LEU   B 1 257 ? -8.487  -40.304 2.019  1.00 49.81  ? 332 LEU   B CG  1 
ATOM   4195 C CD1 . LEU   B 1 257 ? -7.087  -40.812 2.303  1.00 40.89  ? 332 LEU   B CD1 1 
ATOM   4196 C CD2 . LEU   B 1 257 ? -8.694  -38.936 2.648  1.00 52.80  ? 332 LEU   B CD2 1 
ATOM   4197 N N   . ARG   B 1 258 ? -10.857 -42.556 -0.135 1.00 44.77  ? 333 ARG   B N   1 
ATOM   4198 C CA  . ARG   B 1 258 ? -11.844 -43.541 0.299  1.00 48.23  ? 333 ARG   B CA  1 
ATOM   4199 C C   . ARG   B 1 258 ? -11.387 -44.955 -0.030 1.00 50.09  ? 333 ARG   B C   1 
ATOM   4200 O O   . ARG   B 1 258 ? -11.538 -45.872 0.786  1.00 59.67  ? 333 ARG   B O   1 
ATOM   4201 C CB  . ARG   B 1 258 ? -13.197 -43.267 -0.356 1.00 58.44  ? 333 ARG   B CB  1 
ATOM   4202 C CG  . ARG   B 1 258 ? -14.066 -42.245 0.351  1.00 67.36  ? 333 ARG   B CG  1 
ATOM   4203 C CD  . ARG   B 1 258 ? -15.522 -42.461 -0.031 1.00 67.51  ? 333 ARG   B CD  1 
ATOM   4204 N NE  . ARG   B 1 258 ? -16.318 -41.246 0.085  1.00 85.28  ? 333 ARG   B NE  1 
ATOM   4205 C CZ  . ARG   B 1 258 ? -16.470 -40.358 -0.888 1.00 102.79 ? 333 ARG   B CZ  1 
ATOM   4206 N NH1 . ARG   B 1 258 ? -15.876 -40.510 -2.061 1.00 97.64  ? 333 ARG   B NH1 1 
ATOM   4207 N NH2 . ARG   B 1 258 ? -17.238 -39.292 -0.681 1.00 98.98  ? 333 ARG   B NH2 1 
ATOM   4208 N N   . SER   B 1 259 ? -10.826 -45.148 -1.225 1.00 54.06  ? 334 SER   B N   1 
ATOM   4209 C CA  . SER   B 1 259 ? -10.367 -46.471 -1.631 1.00 39.81  ? 334 SER   B CA  1 
ATOM   4210 C C   . SER   B 1 259 ? -9.281  -46.988 -0.699 1.00 48.01  ? 334 SER   B C   1 
ATOM   4211 O O   . SER   B 1 259 ? -9.221  -48.188 -0.410 1.00 52.92  ? 334 SER   B O   1 
ATOM   4212 C CB  . SER   B 1 259 ? -9.858  -46.424 -3.071 1.00 43.71  ? 334 SER   B CB  1 
ATOM   4213 O OG  . SER   B 1 259 ? -9.275  -47.660 -3.441 1.00 81.87  ? 334 SER   B OG  1 
ATOM   4214 N N   . VAL   B 1 260 ? -8.414  -46.096 -0.217 1.00 43.53  ? 335 VAL   B N   1 
ATOM   4215 C CA  . VAL   B 1 260 ? -7.334  -46.516 0.670  1.00 45.23  ? 335 VAL   B CA  1 
ATOM   4216 C C   . VAL   B 1 260 ? -7.877  -46.836 2.055  1.00 41.60  ? 335 VAL   B C   1 
ATOM   4217 O O   . VAL   B 1 260 ? -7.453  -47.806 2.694  1.00 50.35  ? 335 VAL   B O   1 
ATOM   4218 C CB  . VAL   B 1 260 ? -6.236  -45.436 0.726  1.00 44.47  ? 335 VAL   B CB  1 
ATOM   4219 C CG1 . VAL   B 1 260 ? -5.173  -45.809 1.750  1.00 53.01  ? 335 VAL   B CG1 1 
ATOM   4220 C CG2 . VAL   B 1 260 ? -5.609  -45.245 -0.642 1.00 52.45  ? 335 VAL   B CG2 1 
ATOM   4221 N N   . LEU   B 1 261 ? -8.826  -46.031 2.542  1.00 63.79  ? 336 LEU   B N   1 
ATOM   4222 C CA  . LEU   B 1 261 ? -9.404  -46.276 3.861  1.00 42.57  ? 336 LEU   B CA  1 
ATOM   4223 C C   . LEU   B 1 261 ? -10.175 -47.589 3.912  1.00 54.25  ? 336 LEU   B C   1 
ATOM   4224 O O   . LEU   B 1 261 ? -10.172 -48.260 4.950  1.00 58.98  ? 336 LEU   B O   1 
ATOM   4225 C CB  . LEU   B 1 261 ? -10.320 -45.123 4.261  1.00 47.98  ? 336 LEU   B CB  1 
ATOM   4226 C CG  . LEU   B 1 261 ? -9.642  -43.764 4.391  1.00 43.91  ? 336 LEU   B CG  1 
ATOM   4227 C CD1 . LEU   B 1 261 ? -10.663 -42.681 4.697  1.00 61.81  ? 336 LEU   B CD1 1 
ATOM   4228 C CD2 . LEU   B 1 261 ? -8.567  -43.821 5.464  1.00 36.54  ? 336 LEU   B CD2 1 
ATOM   4229 N N   . VAL   B 1 262 ? -10.845 -47.968 2.820  1.00 51.25  ? 337 VAL   B N   1 
ATOM   4230 C CA  . VAL   B 1 262 ? -11.563 -49.240 2.806  1.00 42.16  ? 337 VAL   B CA  1 
ATOM   4231 C C   . VAL   B 1 262 ? -10.593 -50.402 2.973  1.00 51.46  ? 337 VAL   B C   1 
ATOM   4232 O O   . VAL   B 1 262 ? -10.842 -51.334 3.750  1.00 54.09  ? 337 VAL   B O   1 
ATOM   4233 C CB  . VAL   B 1 262 ? -12.392 -49.367 1.518  1.00 44.01  ? 337 VAL   B CB  1 
ATOM   4234 C CG1 . VAL   B 1 262 ? -12.884 -50.791 1.328  1.00 55.50  ? 337 VAL   B CG1 1 
ATOM   4235 C CG2 . VAL   B 1 262 ? -13.565 -48.406 1.561  1.00 58.80  ? 337 VAL   B CG2 1 
ATOM   4236 N N   . MET   B 1 263 ? -9.463  -50.356 2.264  1.00 50.09  ? 338 MET   B N   1 
ATOM   4237 C CA  . MET   B 1 263 ? -8.466  -51.413 2.394  1.00 39.91  ? 338 MET   B CA  1 
ATOM   4238 C C   . MET   B 1 263 ? -7.923  -51.493 3.812  1.00 43.15  ? 338 MET   B C   1 
ATOM   4239 O O   . MET   B 1 263 ? -7.726  -52.590 4.349  1.00 52.16  ? 338 MET   B O   1 
ATOM   4240 C CB  . MET   B 1 263 ? -7.327  -51.185 1.404  1.00 42.72  ? 338 MET   B CB  1 
ATOM   4241 C CG  . MET   B 1 263 ? -7.778  -51.063 -0.032 1.00 54.04  ? 338 MET   B CG  1 
ATOM   4242 S SD  . MET   B 1 263 ? -6.392  -50.818 -1.155 1.00 72.92  ? 338 MET   B SD  1 
ATOM   4243 C CE  . MET   B 1 263 ? -5.533  -52.377 -0.965 1.00 70.61  ? 338 MET   B CE  1 
ATOM   4244 N N   . MET   B 1 264 ? -7.673  -50.342 4.436  1.00 39.19  ? 339 MET   B N   1 
ATOM   4245 C CA  . MET   B 1 264 ? -7.113  -50.328 5.783  1.00 39.49  ? 339 MET   B CA  1 
ATOM   4246 C C   . MET   B 1 264 ? -8.134  -50.723 6.840  1.00 40.68  ? 339 MET   B C   1 
ATOM   4247 O O   . MET   B 1 264 ? -7.763  -51.330 7.850  1.00 49.82  ? 339 MET   B O   1 
ATOM   4248 C CB  . MET   B 1 264 ? -6.544  -48.944 6.107  1.00 33.97  ? 339 MET   B CB  1 
ATOM   4249 C CG  . MET   B 1 264 ? -5.528  -48.448 5.094  1.00 45.31  ? 339 MET   B CG  1 
ATOM   4250 S SD  . MET   B 1 264 ? -4.816  -46.842 5.499  1.00 43.06  ? 339 MET   B SD  1 
ATOM   4251 C CE  . MET   B 1 264 ? -3.853  -47.262 6.947  1.00 40.56  ? 339 MET   B CE  1 
ATOM   4252 N N   . LEU   B 1 265 ? -9.411  -50.394 6.634  1.00 57.67  ? 340 LEU   B N   1 
ATOM   4253 C CA  . LEU   B 1 265 ? -10.462 -50.688 7.599  1.00 41.30  ? 340 LEU   B CA  1 
ATOM   4254 C C   . LEU   B 1 265 ? -11.143 -52.027 7.344  1.00 43.50  ? 340 LEU   B C   1 
ATOM   4255 O O   . LEU   B 1 265 ? -12.245 -52.259 7.858  1.00 64.12  ? 340 LEU   B O   1 
ATOM   4256 C CB  . LEU   B 1 265 ? -11.503 -49.565 7.605  1.00 37.78  ? 340 LEU   B CB  1 
ATOM   4257 C CG  . LEU   B 1 265 ? -10.970 -48.194 8.028  1.00 31.09  ? 340 LEU   B CG  1 
ATOM   4258 C CD1 . LEU   B 1 265 ? -12.101 -47.198 8.202  1.00 31.65  ? 340 LEU   B CD1 1 
ATOM   4259 C CD2 . LEU   B 1 265 ? -10.157 -48.307 9.303  1.00 37.65  ? 340 LEU   B CD2 1 
ATOM   4260 N N   . GLU   B 1 266 ? -10.520 -52.906 6.567  1.00 57.50  ? 341 GLU   B N   1 
ATOM   4261 C CA  . GLU   B 1 266 ? -11.048 -54.246 6.356  1.00 41.15  ? 341 GLU   B CA  1 
ATOM   4262 C C   . GLU   B 1 266 ? -11.114 -54.989 7.687  1.00 42.25  ? 341 GLU   B C   1 
ATOM   4263 O O   . GLU   B 1 266 ? -10.087 -55.107 8.373  1.00 47.25  ? 341 GLU   B O   1 
ATOM   4264 C CB  . GLU   B 1 266 ? -10.178 -55.012 5.361  1.00 38.27  ? 341 GLU   B CB  1 
ATOM   4265 C CG  . GLU   B 1 266 ? -10.416 -56.517 5.343  1.00 57.91  ? 341 GLU   B CG  1 
ATOM   4266 C CD  . GLU   B 1 266 ? -11.791 -56.903 4.829  1.00 62.49  ? 341 GLU   B CD  1 
ATOM   4267 O OE1 . GLU   B 1 266 ? -12.416 -56.097 4.105  1.00 75.57  ? 341 GLU   B OE1 1 
ATOM   4268 O OE2 . GLU   B 1 266 ? -12.249 -58.021 5.152  1.00 77.02  ? 341 GLU   B OE2 1 
ATOM   4269 N N   . PRO   B 1 267 ? -12.282 -55.498 8.090  1.00 49.33  ? 342 PRO   B N   1 
ATOM   4270 C CA  . PRO   B 1 267 ? -12.390 -56.101 9.428  1.00 44.86  ? 342 PRO   B CA  1 
ATOM   4271 C C   . PRO   B 1 267 ? -11.586 -57.379 9.598  1.00 56.10  ? 342 PRO   B C   1 
ATOM   4272 O O   . PRO   B 1 267 ? -11.175 -57.683 10.724 1.00 52.61  ? 342 PRO   B O   1 
ATOM   4273 C CB  . PRO   B 1 267 ? -13.896 -56.365 9.575  1.00 45.17  ? 342 PRO   B CB  1 
ATOM   4274 C CG  . PRO   B 1 267 ? -14.554 -55.526 8.519  1.00 48.70  ? 342 PRO   B CG  1 
ATOM   4275 C CD  . PRO   B 1 267 ? -13.577 -55.459 7.393  1.00 43.15  ? 342 PRO   B CD  1 
ATOM   4276 N N   . ASP   B 1 268 ? -11.351 -58.142 8.529  1.00 51.04  ? 343 ASP   B N   1 
ATOM   4277 C CA  . ASP   B 1 268 ? -10.647 -59.415 8.643  1.00 40.09  ? 343 ASP   B CA  1 
ATOM   4278 C C   . ASP   B 1 268 ? -9.149  -59.189 8.492  1.00 52.76  ? 343 ASP   B C   1 
ATOM   4279 O O   . ASP   B 1 268 ? -8.704  -58.770 7.414  1.00 51.86  ? 343 ASP   B O   1 
ATOM   4280 C CB  . ASP   B 1 268 ? -11.135 -60.395 7.589  1.00 42.47  ? 343 ASP   B CB  1 
ATOM   4281 C CG  . ASP   B 1 268 ? -10.806 -61.834 7.933  1.00 55.25  ? 343 ASP   B CG  1 
ATOM   4282 O OD1 . ASP   B 1 268 ? -9.711  -62.085 8.478  1.00 68.19  ? 343 ASP   B OD1 1 
ATOM   4283 O OD2 . ASP   B 1 268 ? -11.649 -62.716 7.662  1.00 79.64  ? 343 ASP   B OD2 1 
ATOM   4284 N N   . PRO   B 1 269 ? -8.340  -59.458 9.520  1.00 57.30  ? 344 PRO   B N   1 
ATOM   4285 C CA  . PRO   B 1 269 ? -6.892  -59.233 9.383  1.00 52.67  ? 344 PRO   B CA  1 
ATOM   4286 C C   . PRO   B 1 269 ? -6.248  -60.096 8.314  1.00 45.72  ? 344 PRO   B C   1 
ATOM   4287 O O   . PRO   B 1 269 ? -5.215  -59.704 7.758  1.00 62.74  ? 344 PRO   B O   1 
ATOM   4288 C CB  . PRO   B 1 269 ? -6.353  -59.562 10.782 1.00 53.42  ? 344 PRO   B CB  1 
ATOM   4289 C CG  . PRO   B 1 269 ? -7.385  -60.469 11.383 1.00 40.41  ? 344 PRO   B CG  1 
ATOM   4290 C CD  . PRO   B 1 269 ? -8.699  -59.987 10.848 1.00 43.60  ? 344 PRO   B CD  1 
ATOM   4291 N N   . LYS   B 1 270 ? -6.826  -61.260 8.007  1.00 53.62  ? 345 LYS   B N   1 
ATOM   4292 C CA  . LYS   B 1 270 ? -6.302  -62.070 6.912  1.00 67.69  ? 345 LYS   B CA  1 
ATOM   4293 C C   . LYS   B 1 270 ? -6.427  -61.346 5.579  1.00 62.03  ? 345 LYS   B C   1 
ATOM   4294 O O   . LYS   B 1 270 ? -5.594  -61.540 4.686  1.00 67.41  ? 345 LYS   B O   1 
ATOM   4295 C CB  . LYS   B 1 270 ? -7.033  -63.411 6.839  1.00 61.56  ? 345 LYS   B CB  1 
ATOM   4296 C CG  . LYS   B 1 270 ? -7.011  -64.234 8.114  1.00 63.41  ? 345 LYS   B CG  1 
ATOM   4297 C CD  . LYS   B 1 270 ? -7.487  -65.652 7.831  1.00 77.88  ? 345 LYS   B CD  1 
ATOM   4298 C CE  . LYS   B 1 270 ? -7.769  -66.421 9.112  1.00 106.41 ? 345 LYS   B CE  1 
ATOM   4299 N NZ  . LYS   B 1 270 ? -8.968  -65.895 9.824  1.00 115.82 ? 345 LYS   B NZ  1 
ATOM   4300 N N   . LEU   B 1 271 ? -7.456  -60.516 5.426  1.00 51.86  ? 346 LEU   B N   1 
ATOM   4301 C CA  . LEU   B 1 271 ? -7.733  -59.827 4.176  1.00 57.52  ? 346 LEU   B CA  1 
ATOM   4302 C C   . LEU   B 1 271 ? -7.264  -58.381 4.186  1.00 48.27  ? 346 LEU   B C   1 
ATOM   4303 O O   . LEU   B 1 271 ? -7.408  -57.689 3.174  1.00 61.41  ? 346 LEU   B O   1 
ATOM   4304 C CB  . LEU   B 1 271 ? -9.236  -59.880 3.870  1.00 55.07  ? 346 LEU   B CB  1 
ATOM   4305 C CG  . LEU   B 1 271 ? -9.918  -61.244 4.005  1.00 52.80  ? 346 LEU   B CG  1 
ATOM   4306 C CD1 . LEU   B 1 271 ? -11.408 -61.156 3.700  1.00 54.45  ? 346 LEU   B CD1 1 
ATOM   4307 C CD2 . LEU   B 1 271 ? -9.247  -62.260 3.103  1.00 49.44  ? 346 LEU   B CD2 1 
ATOM   4308 N N   . ARG   B 1 272 ? -6.707  -57.911 5.296  1.00 54.67  ? 347 ARG   B N   1 
ATOM   4309 C CA  . ARG   B 1 272 ? -6.318  -56.515 5.415  1.00 52.72  ? 347 ARG   B CA  1 
ATOM   4310 C C   . ARG   B 1 272 ? -4.984  -56.269 4.723  1.00 45.98  ? 347 ARG   B C   1 
ATOM   4311 O O   . ARG   B 1 272 ? -4.096  -57.126 4.728  1.00 63.88  ? 347 ARG   B O   1 
ATOM   4312 C CB  . ARG   B 1 272 ? -6.230  -56.119 6.887  1.00 38.04  ? 347 ARG   B CB  1 
ATOM   4313 C CG  . ARG   B 1 272 ? -6.045  -54.636 7.134  1.00 37.36  ? 347 ARG   B CG  1 
ATOM   4314 C CD  . ARG   B 1 272 ? -6.149  -54.366 8.612  1.00 41.24  ? 347 ARG   B CD  1 
ATOM   4315 N NE  . ARG   B 1 272 ? -7.375  -54.945 9.146  1.00 38.02  ? 347 ARG   B NE  1 
ATOM   4316 C CZ  . ARG   B 1 272 ? -7.540  -55.312 10.408 1.00 33.32  ? 347 ARG   B CZ  1 
ATOM   4317 N NH1 . ARG   B 1 272 ? -6.568  -55.182 11.296 1.00 38.34  ? 347 ARG   B NH1 1 
ATOM   4318 N NH2 . ARG   B 1 272 ? -8.704  -55.832 10.785 1.00 38.44  ? 347 ARG   B NH2 1 
ATOM   4319 N N   . ALA   B 1 273 ? -4.852  -55.090 4.122  1.00 55.01  ? 348 ALA   B N   1 
ATOM   4320 C CA  . ALA   B 1 273 ? -3.614  -54.729 3.448  1.00 43.74  ? 348 ALA   B CA  1 
ATOM   4321 C C   . ALA   B 1 273 ? -2.520  -54.422 4.464  1.00 51.19  ? 348 ALA   B C   1 
ATOM   4322 O O   . ALA   B 1 273 ? -2.788  -54.019 5.599  1.00 55.58  ? 348 ALA   B O   1 
ATOM   4323 C CB  . ALA   B 1 273 ? -3.836  -53.523 2.536  1.00 38.37  ? 348 ALA   B CB  1 
ATOM   4324 N N   . THR   B 1 274 ? -1.274  -54.622 4.047  1.00 52.53  ? 349 THR   B N   1 
ATOM   4325 C CA  . THR   B 1 274 ? -0.116  -54.321 4.873  1.00 41.75  ? 349 THR   B CA  1 
ATOM   4326 C C   . THR   B 1 274 ? 0.445   -52.951 4.505  1.00 44.68  ? 349 THR   B C   1 
ATOM   4327 O O   . THR   B 1 274 ? 0.103   -52.364 3.476  1.00 49.62  ? 349 THR   B O   1 
ATOM   4328 C CB  . THR   B 1 274 ? 0.960   -55.399 4.712  1.00 43.34  ? 349 THR   B CB  1 
ATOM   4329 O OG1 . THR   B 1 274 ? 1.319   -55.509 3.332  1.00 53.09  ? 349 THR   B OG1 1 
ATOM   4330 C CG2 . THR   B 1 274 ? 0.447   -56.747 5.186  1.00 44.44  ? 349 THR   B CG2 1 
ATOM   4331 N N   . ALA   B 1 275 ? 1.321   -52.439 5.373  1.00 44.79  ? 350 ALA   B N   1 
ATOM   4332 C CA  . ALA   B 1 275 ? 1.936   -51.140 5.115  1.00 31.05  ? 350 ALA   B CA  1 
ATOM   4333 C C   . ALA   B 1 275 ? 2.762   -51.168 3.837  1.00 51.13  ? 350 ALA   B C   1 
ATOM   4334 O O   . ALA   B 1 275 ? 2.716   -50.226 3.036  1.00 52.32  ? 350 ALA   B O   1 
ATOM   4335 C CB  . ALA   B 1 275 ? 2.798   -50.722 6.306  1.00 38.76  ? 350 ALA   B CB  1 
ATOM   4336 N N   . GLU   B 1 276 ? 3.518   -52.246 3.621  1.00 43.88  ? 351 GLU   B N   1 
ATOM   4337 C CA  . GLU   B 1 276 ? 4.305   -52.353 2.399  1.00 41.15  ? 351 GLU   B CA  1 
ATOM   4338 C C   . GLU   B 1 276 ? 3.403   -52.382 1.171  1.00 40.45  ? 351 GLU   B C   1 
ATOM   4339 O O   . GLU   B 1 276 ? 3.739   -51.809 0.128  1.00 52.90  ? 351 GLU   B O   1 
ATOM   4340 C CB  . GLU   B 1 276 ? 5.185   -53.601 2.455  1.00 40.61  ? 351 GLU   B CB  1 
ATOM   4341 C CG  . GLU   B 1 276 ? 6.091   -53.790 1.251  1.00 68.19  ? 351 GLU   B CG  1 
ATOM   4342 C CD  . GLU   B 1 276 ? 6.801   -55.131 1.264  1.00 91.58  ? 351 GLU   B CD  1 
ATOM   4343 O OE1 . GLU   B 1 276 ? 6.501   -55.954 2.156  1.00 91.54  ? 351 GLU   B OE1 1 
ATOM   4344 O OE2 . GLU   B 1 276 ? 7.656   -55.364 0.382  1.00 83.31  ? 351 GLU   B OE2 1 
ATOM   4345 N N   . ALA   B 1 277 ? 2.242   -53.031 1.282  1.00 43.05  ? 352 ALA   B N   1 
ATOM   4346 C CA  . ALA   B 1 277 ? 1.325   -53.094 0.150  1.00 47.19  ? 352 ALA   B CA  1 
ATOM   4347 C C   . ALA   B 1 277 ? 0.724   -51.727 -0.147 1.00 44.99  ? 352 ALA   B C   1 
ATOM   4348 O O   . ALA   B 1 277 ? 0.635   -51.322 -1.311 1.00 49.51  ? 352 ALA   B O   1 
ATOM   4349 C CB  . ALA   B 1 277 ? 0.226   -54.119 0.424  1.00 49.73  ? 352 ALA   B CB  1 
ATOM   4350 N N   . LEU   B 1 278 ? 0.313   -50.999 0.894  1.00 41.24  ? 353 LEU   B N   1 
ATOM   4351 C CA  . LEU   B 1 278 ? -0.250  -49.668 0.688  1.00 42.19  ? 353 LEU   B CA  1 
ATOM   4352 C C   . LEU   B 1 278 ? 0.778   -48.717 0.092  1.00 45.49  ? 353 LEU   B C   1 
ATOM   4353 O O   . LEU   B 1 278 ? 0.460   -47.941 -0.815 1.00 56.36  ? 353 LEU   B O   1 
ATOM   4354 C CB  . LEU   B 1 278 ? -0.788  -49.118 2.005  1.00 36.05  ? 353 LEU   B CB  1 
ATOM   4355 C CG  . LEU   B 1 278 ? -1.964  -49.893 2.595  1.00 36.75  ? 353 LEU   B CG  1 
ATOM   4356 C CD1 . LEU   B 1 278 ? -2.244  -49.421 4.007  1.00 54.96  ? 353 LEU   B CD1 1 
ATOM   4357 C CD2 . LEU   B 1 278 ? -3.190  -49.727 1.712  1.00 51.20  ? 353 LEU   B CD2 1 
ATOM   4358 N N   . LEU   B 1 279 ? 2.021   -48.763 0.585  1.00 44.92  ? 354 LEU   B N   1 
ATOM   4359 C CA  . LEU   B 1 279 ? 3.076   -47.919 0.029  1.00 42.93  ? 354 LEU   B CA  1 
ATOM   4360 C C   . LEU   B 1 279 ? 3.348   -48.220 -1.437 1.00 46.54  ? 354 LEU   B C   1 
ATOM   4361 O O   . LEU   B 1 279 ? 3.934   -47.382 -2.131 1.00 63.15  ? 354 LEU   B O   1 
ATOM   4362 C CB  . LEU   B 1 279 ? 4.364   -48.080 0.836  1.00 40.05  ? 354 LEU   B CB  1 
ATOM   4363 C CG  . LEU   B 1 279 ? 4.317   -47.494 2.245  1.00 37.62  ? 354 LEU   B CG  1 
ATOM   4364 C CD1 . LEU   B 1 279 ? 5.461   -48.026 3.091  1.00 36.98  ? 354 LEU   B CD1 1 
ATOM   4365 C CD2 . LEU   B 1 279 ? 4.356   -45.978 2.174  1.00 35.88  ? 354 LEU   B CD2 1 
ATOM   4366 N N   . ALA   B 1 280 ? 2.944   -49.392 -1.923 1.00 55.70  ? 355 ALA   B N   1 
ATOM   4367 C CA  . ALA   B 1 280 ? 3.111   -49.748 -3.324 1.00 57.37  ? 355 ALA   B CA  1 
ATOM   4368 C C   . ALA   B 1 280 ? 1.949   -49.293 -4.198 1.00 58.11  ? 355 ALA   B C   1 
ATOM   4369 O O   . ALA   B 1 280 ? 2.037   -49.408 -5.427 1.00 58.73  ? 355 ALA   B O   1 
ATOM   4370 C CB  . ALA   B 1 280 ? 3.290   -51.262 -3.467 1.00 64.93  ? 355 ALA   B CB  1 
ATOM   4371 N N   . LEU   B 1 281 ? 0.868   -48.792 -3.600 1.00 56.16  ? 356 LEU   B N   1 
ATOM   4372 C CA  . LEU   B 1 281 ? -0.263  -48.302 -4.368 1.00 50.65  ? 356 LEU   B CA  1 
ATOM   4373 C C   . LEU   B 1 281 ? 0.131   -47.044 -5.136 1.00 59.33  ? 356 LEU   B C   1 
ATOM   4374 O O   . LEU   B 1 281 ? 1.054   -46.328 -4.739 1.00 75.41  ? 356 LEU   B O   1 
ATOM   4375 C CB  . LEU   B 1 281 ? -1.446  -48.024 -3.444 1.00 49.86  ? 356 LEU   B CB  1 
ATOM   4376 C CG  . LEU   B 1 281 ? -2.130  -49.269 -2.876 1.00 45.99  ? 356 LEU   B CG  1 
ATOM   4377 C CD1 . LEU   B 1 281 ? -3.338  -48.893 -2.030 1.00 59.73  ? 356 LEU   B CD1 1 
ATOM   4378 C CD2 . LEU   B 1 281 ? -2.528  -50.212 -4.001 1.00 50.99  ? 356 LEU   B CD2 1 
ATOM   4379 N N   . PRO   B 1 282 ? -0.550  -46.759 -6.249 1.00 66.62  ? 357 PRO   B N   1 
ATOM   4380 C CA  . PRO   B 1 282 ? -0.151  -45.603 -7.068 1.00 58.41  ? 357 PRO   B CA  1 
ATOM   4381 C C   . PRO   B 1 282 ? -0.234  -44.274 -6.334 1.00 60.89  ? 357 PRO   B C   1 
ATOM   4382 O O   . PRO   B 1 282 ? 0.600   -43.391 -6.573 1.00 73.86  ? 357 PRO   B O   1 
ATOM   4383 C CB  . PRO   B 1 282 ? -1.132  -45.655 -8.249 1.00 67.34  ? 357 PRO   B CB  1 
ATOM   4384 C CG  . PRO   B 1 282 ? -1.597  -47.079 -8.299 1.00 60.22  ? 357 PRO   B CG  1 
ATOM   4385 C CD  . PRO   B 1 282 ? -1.641  -47.529 -6.872 1.00 64.72  ? 357 PRO   B CD  1 
ATOM   4386 N N   . VAL   B 1 283 ? -1.205  -44.106 -5.434 1.00 68.16  ? 358 VAL   B N   1 
ATOM   4387 C CA  . VAL   B 1 283 ? -1.401  -42.817 -4.772 1.00 58.93  ? 358 VAL   B CA  1 
ATOM   4388 C C   . VAL   B 1 283 ? -0.391  -42.534 -3.672 1.00 61.25  ? 358 VAL   B C   1 
ATOM   4389 O O   . VAL   B 1 283 ? -0.389  -41.423 -3.125 1.00 61.92  ? 358 VAL   B O   1 
ATOM   4390 C CB  . VAL   B 1 283 ? -2.816  -42.730 -4.174 1.00 60.88  ? 358 VAL   B CB  1 
ATOM   4391 C CG1 . VAL   B 1 283 ? -3.858  -42.802 -5.274 1.00 68.93  ? 358 VAL   B CG1 1 
ATOM   4392 C CG2 . VAL   B 1 283 ? -3.032  -43.847 -3.174 1.00 61.72  ? 358 VAL   B CG2 1 
ATOM   4393 N N   . LEU   B 1 284 ? 0.471   -43.495 -3.332 1.00 73.12  ? 359 LEU   B N   1 
ATOM   4394 C CA  . LEU   B 1 284 ? 1.397   -43.347 -2.215 1.00 67.41  ? 359 LEU   B CA  1 
ATOM   4395 C C   . LEU   B 1 284 ? 2.861   -43.495 -2.611 1.00 69.38  ? 359 LEU   B C   1 
ATOM   4396 O O   . LEU   B 1 284 ? 3.726   -43.495 -1.728 1.00 74.46  ? 359 LEU   B O   1 
ATOM   4397 C CB  . LEU   B 1 284 ? 1.063   -44.356 -1.113 1.00 46.54  ? 359 LEU   B CB  1 
ATOM   4398 C CG  . LEU   B 1 284 ? -0.181  -44.034 -0.293 1.00 40.35  ? 359 LEU   B CG  1 
ATOM   4399 C CD1 . LEU   B 1 284 ? -0.601  -45.224 0.548  1.00 40.74  ? 359 LEU   B CD1 1 
ATOM   4400 C CD2 . LEU   B 1 284 ? 0.091   -42.831 0.591  1.00 40.22  ? 359 LEU   B CD2 1 
ATOM   4401 N N   . ARG   B 1 285 ? 3.167   -43.624 -3.899 1.00 89.49  ? 360 ARG   B N   1 
ATOM   4402 C CA  . ARG   B 1 285 ? 4.553   -43.723 -4.329 1.00 93.85  ? 360 ARG   B CA  1 
ATOM   4403 C C   . ARG   B 1 285 ? 5.180   -42.339 -4.444 1.00 96.61  ? 360 ARG   B C   1 
ATOM   4404 O O   . ARG   B 1 285 ? 4.519   -41.358 -4.797 1.00 107.79 ? 360 ARG   B O   1 
ATOM   4405 C CB  . ARG   B 1 285 ? 4.656   -44.446 -5.673 1.00 90.28  ? 360 ARG   B CB  1 
ATOM   4406 C CG  . ARG   B 1 285 ? 4.385   -45.942 -5.614 1.00 87.47  ? 360 ARG   B CG  1 
ATOM   4407 C CD  . ARG   B 1 285 ? 4.801   -46.618 -6.915 1.00 99.47  ? 360 ARG   B CD  1 
ATOM   4408 N NE  . ARG   B 1 285 ? 4.466   -48.037 -6.945 1.00 105.44 ? 360 ARG   B NE  1 
ATOM   4409 C CZ  . ARG   B 1 285 ? 5.255   -49.006 -6.499 1.00 109.15 ? 360 ARG   B CZ  1 
ATOM   4410 N NH1 . ARG   B 1 285 ? 6.432   -48.745 -5.954 1.00 111.07 ? 360 ARG   B NH1 1 
ATOM   4411 N NH2 . ARG   B 1 285 ? 4.851   -50.270 -6.600 1.00 91.94  ? 360 ARG   B NH2 1 
ATOM   4412 N N   . GLN   B 1 286 ? 6.473   -42.270 -4.139 1.00 99.34  ? 361 GLN   B N   1 
ATOM   4413 C CA  . GLN   B 1 286 ? 7.239   -41.036 -4.298 1.00 95.46  ? 361 GLN   B CA  1 
ATOM   4414 C C   . GLN   B 1 286 ? 8.370   -41.222 -5.302 1.00 94.70  ? 361 GLN   B C   1 
ATOM   4415 O O   . GLN   B 1 286 ? 8.156   -41.147 -6.512 1.00 104.44 ? 361 GLN   B O   1 
ATOM   4416 C CB  . GLN   B 1 286 ? 7.806   -40.566 -2.956 1.00 78.50  ? 361 GLN   B CB  1 
ATOM   4417 C CG  . GLN   B 1 286 ? 6.841   -39.740 -2.123 1.00 87.15  ? 361 GLN   B CG  1 
ATOM   4418 C CD  . GLN   B 1 286 ? 6.786   -38.287 -2.551 1.00 83.43  ? 361 GLN   B CD  1 
ATOM   4419 O OE1 . GLN   B 1 286 ? 7.100   -37.947 -3.693 1.00 84.37  ? 361 GLN   B OE1 1 
ATOM   4420 N NE2 . GLN   B 1 286 ? 6.393   -37.418 -1.629 1.00 79.85  ? 361 GLN   B NE2 1 
HETATM 4421 C C10 . A1EJU C 2 .   ? -7.664  -16.736 25.439 1.00 44.62  ? 401 A1EJU A C10 1 
HETATM 4422 C C11 . A1EJU C 2 .   ? -7.086  -17.957 24.905 1.00 44.83  ? 401 A1EJU A C11 1 
HETATM 4423 C C15 . A1EJU C 2 .   ? -5.095  -17.441 26.215 1.00 37.33  ? 401 A1EJU A C15 1 
HETATM 4424 C C16 . A1EJU C 2 .   ? -3.764  -17.762 26.498 1.00 47.45  ? 401 A1EJU A C16 1 
HETATM 4425 C C17 . A1EJU C 2 .   ? -3.040  -16.961 27.360 1.00 38.34  ? 401 A1EJU A C17 1 
HETATM 4426 C C18 . A1EJU C 2 .   ? -3.685  -15.867 27.903 1.00 50.34  ? 401 A1EJU A C18 1 
HETATM 4427 C C19 . A1EJU C 2 .   ? -6.909  -12.943 25.085 1.00 38.04  ? 401 A1EJU A C19 1 
HETATM 4428 C C24 . A1EJU C 2 .   ? -1.951  -19.278 26.179 1.00 58.30  ? 401 A1EJU A C24 1 
HETATM 4429 C C1  . A1EJU C 2 .   ? -7.612  -14.689 26.911 1.00 43.35  ? 401 A1EJU A C1  1 
HETATM 4430 C C14 . A1EJU C 2 .   ? -5.671  -16.320 26.814 1.00 42.29  ? 401 A1EJU A C14 1 
HETATM 4431 C C2  . A1EJU C 2 .   ? -7.503  -13.442 26.267 1.00 35.62  ? 401 A1EJU A C2  1 
HETATM 4432 C C3  . A1EJU C 2 .   ? -8.105  -12.317 26.856 1.00 43.36  ? 401 A1EJU A C3  1 
HETATM 4433 C C4  . A1EJU C 2 .   ? -8.786  -12.463 28.051 1.00 43.12  ? 401 A1EJU A C4  1 
HETATM 4434 C C5  . A1EJU C 2 .   ? -8.900  -13.672 28.688 1.00 32.12  ? 401 A1EJU A C5  1 
HETATM 4435 C C6  . A1EJU C 2 .   ? -8.311  -14.785 28.117 1.00 39.55  ? 401 A1EJU A C6  1 
HETATM 4436 C C9  . A1EJU C 2 .   ? -7.000  -15.935 26.364 1.00 45.83  ? 401 A1EJU A C9  1 
HETATM 4437 F F22 . A1EJU C 2 .   ? -9.357  -11.366 28.596 1.00 51.39  ? 401 A1EJU A F22 1 
HETATM 4438 N N12 . A1EJU C 2 .   ? -5.831  -18.228 25.347 1.00 42.91  ? 401 A1EJU A N12 1 
HETATM 4439 N N13 . A1EJU C 2 .   ? -4.960  -15.535 27.644 1.00 50.07  ? 401 A1EJU A N13 1 
HETATM 4440 N N20 . A1EJU C 2 .   ? -7.119  -11.647 24.950 1.00 49.59  ? 401 A1EJU A N20 1 
HETATM 4441 N N21 . A1EJU C 2 .   ? -7.851  -11.267 26.038 1.00 41.29  ? 401 A1EJU A N21 1 
HETATM 4442 N N7  . A1EJU C 2 .   ? -8.896  -16.434 24.982 1.00 47.78  ? 401 A1EJU A N7  1 
HETATM 4443 O O23 . A1EJU C 2 .   ? -3.285  -18.878 25.873 1.00 52.31  ? 401 A1EJU A O23 1 
HETATM 4444 O O8  . A1EJU C 2 .   ? -7.659  -18.719 24.129 1.00 46.69  ? 401 A1EJU A O8  1 
HETATM 4445 S S   . SO4   D 3 .   ? -28.979 0.893   26.340 1.00 64.31  ? 402 SO4   A S   1 
HETATM 4446 O O1  . SO4   D 3 .   ? -28.883 0.918   24.882 1.00 63.25  ? 402 SO4   A O1  1 
HETATM 4447 O O2  . SO4   D 3 .   ? -30.324 0.468   26.720 1.00 61.33  ? 402 SO4   A O2  1 
HETATM 4448 O O3  . SO4   D 3 .   ? -28.000 -0.044  26.893 1.00 84.23  ? 402 SO4   A O3  1 
HETATM 4449 O O4  . SO4   D 3 .   ? -28.717 2.230   26.872 1.00 58.45  ? 402 SO4   A O4  1 
HETATM 4450 S S   . SO4   E 3 .   ? 8.485   -14.497 27.779 0.92 91.27  ? 403 SO4   A S   1 
HETATM 4451 O O1  . SO4   E 3 .   ? 8.956   -14.562 26.397 0.92 70.46  ? 403 SO4   A O1  1 
HETATM 4452 O O2  . SO4   E 3 .   ? 7.543   -13.391 27.934 0.92 71.40  ? 403 SO4   A O2  1 
HETATM 4453 O O3  . SO4   E 3 .   ? 7.817   -15.748 28.123 0.92 91.68  ? 403 SO4   A O3  1 
HETATM 4454 O O4  . SO4   E 3 .   ? 9.624   -14.296 28.670 0.92 81.81  ? 403 SO4   A O4  1 
HETATM 4455 S S   . SO4   F 3 .   ? 6.496   2.691   27.399 0.51 61.70  ? 404 SO4   A S   1 
HETATM 4456 O O1  . SO4   F 3 .   ? 7.640   3.570   27.164 0.51 52.47  ? 404 SO4   A O1  1 
HETATM 4457 O O2  . SO4   F 3 .   ? 5.360   3.149   26.604 0.51 59.70  ? 404 SO4   A O2  1 
HETATM 4458 O O3  . SO4   F 3 .   ? 6.832   1.322   27.013 0.51 59.77  ? 404 SO4   A O3  1 
HETATM 4459 O O4  . SO4   F 3 .   ? 6.141   2.722   28.816 0.51 60.66  ? 404 SO4   A O4  1 
HETATM 4460 C C10 . A1EJU G 2 .   ? 8.783   -35.705 21.476 1.00 47.40  ? 401 A1EJU B C10 1 
HETATM 4461 C C11 . A1EJU G 2 .   ? 8.308   -34.466 20.885 1.00 44.18  ? 401 A1EJU B C11 1 
HETATM 4462 C C15 . A1EJU G 2 .   ? 6.285   -34.772 22.213 1.00 40.97  ? 401 A1EJU B C15 1 
HETATM 4463 C C16 . A1EJU G 2 .   ? 4.951   -34.402 22.397 1.00 40.16  ? 401 A1EJU B C16 1 
HETATM 4464 C C17 . A1EJU G 2 .   ? 4.168   -35.103 23.293 1.00 43.11  ? 401 A1EJU B C17 1 
HETATM 4465 C C18 . A1EJU G 2 .   ? 4.760   -36.153 23.966 1.00 32.85  ? 401 A1EJU B C18 1 
HETATM 4466 C C19 . A1EJU G 2 .   ? 7.681   -39.412 21.359 1.00 33.78  ? 401 A1EJU B C19 1 
HETATM 4467 C C24 . A1EJU G 2 .   ? 3.346   -32.669 22.071 1.00 44.67  ? 401 A1EJU B C24 1 
HETATM 4468 C C1  . A1EJU G 2 .   ? 8.582   -37.645 23.076 1.00 40.32  ? 401 A1EJU B C1  1 
HETATM 4469 C C14 . A1EJU G 2 .   ? 6.807   -35.841 22.943 1.00 44.50  ? 401 A1EJU B C14 1 
HETATM 4470 C C2  . A1EJU G 2 .   ? 8.343   -38.909 22.503 1.00 41.35  ? 401 A1EJU B C2  1 
HETATM 4471 C C3  . A1EJU G 2 .   ? 8.851   -40.053 23.141 1.00 32.60  ? 401 A1EJU B C3  1 
HETATM 4472 C C4  . A1EJU G 2 .   ? 9.569   -39.910 24.314 1.00 42.05  ? 401 A1EJU B C4  1 
HETATM 4473 C C5  . A1EJU G 2 .   ? 9.809   -38.684 24.884 1.00 37.76  ? 401 A1EJU B C5  1 
HETATM 4474 C C6  . A1EJU G 2 .   ? 9.312   -37.553 24.263 1.00 37.73  ? 401 A1EJU B C6  1 
HETATM 4475 C C9  . A1EJU G 2 .   ? 8.076   -36.379 22.471 1.00 42.25  ? 401 A1EJU B C9  1 
HETATM 4476 F F22 . A1EJU G 2 .   ? 10.046  -41.025 24.910 1.00 48.71  ? 401 A1EJU B F22 1 
HETATM 4477 N N12 . A1EJU G 2 .   ? 7.078   -34.082 21.312 1.00 50.77  ? 401 A1EJU B N12 1 
HETATM 4478 N N13 . A1EJU G 2 .   ? 6.037   -36.532 23.804 1.00 51.57  ? 401 A1EJU B N13 1 
HETATM 4479 N N20 . A1EJU G 2 .   ? 7.767   -40.726 21.290 1.00 42.23  ? 401 A1EJU B N20 1 
HETATM 4480 N N21 . A1EJU G 2 .   ? 8.483   -41.116 22.385 1.00 36.32  ? 401 A1EJU B N21 1 
HETATM 4481 N N7  . A1EJU G 2 .   ? 9.963   -36.158 21.004 1.00 45.52  ? 401 A1EJU B N7  1 
HETATM 4482 O O23 . A1EJU G 2 .   ? 4.529   -33.341 21.648 1.00 50.09  ? 401 A1EJU B O23 1 
HETATM 4483 O O8  . A1EJU G 2 .   ? 8.937   -33.786 20.076 1.00 51.29  ? 401 A1EJU B O8  1 
HETATM 4484 S S   . SO4   H 3 .   ? -20.210 -52.751 22.906 1.00 68.32  ? 402 SO4   B S   1 
HETATM 4485 O O1  . SO4   H 3 .   ? -20.372 -53.081 21.494 1.00 53.81  ? 402 SO4   B O1  1 
HETATM 4486 O O2  . SO4   H 3 .   ? -21.453 -52.163 23.404 1.00 78.37  ? 402 SO4   B O2  1 
HETATM 4487 O O3  . SO4   H 3 .   ? -19.915 -53.962 23.665 1.00 55.80  ? 402 SO4   B O3  1 
HETATM 4488 O O4  . SO4   H 3 .   ? -19.103 -51.809 23.062 1.00 53.96  ? 402 SO4   B O4  1 
HETATM 4489 S S   . SO4   I 3 .   ? -7.348  -37.910 24.378 0.90 92.09  ? 403 SO4   B S   1 
HETATM 4490 O O1  . SO4   I 3 .   ? -6.361  -38.591 23.540 0.90 68.68  ? 403 SO4   B O1  1 
HETATM 4491 O O2  . SO4   I 3 .   ? -8.563  -37.657 23.608 0.90 67.57  ? 403 SO4   B O2  1 
HETATM 4492 O O3  . SO4   I 3 .   ? -7.679  -38.746 25.528 0.90 88.81  ? 403 SO4   B O3  1 
HETATM 4493 O O4  . SO4   I 3 .   ? -6.798  -36.640 24.843 0.90 94.22  ? 403 SO4   B O4  1 
HETATM 4494 S S   . SO4   J 3 .   ? -15.044 -29.597 8.428  0.82 83.32  ? 404 SO4   B S   1 
HETATM 4495 O O1  . SO4   J 3 .   ? -13.665 -29.270 8.078  0.82 67.47  ? 404 SO4   B O1  1 
HETATM 4496 O O2  . SO4   J 3 .   ? -15.923 -28.574 7.870  0.82 79.09  ? 404 SO4   B O2  1 
HETATM 4497 O O3  . SO4   J 3 .   ? -15.399 -30.901 7.876  0.82 79.50  ? 404 SO4   B O3  1 
HETATM 4498 O O4  . SO4   J 3 .   ? -15.196 -29.647 9.881  0.82 64.61  ? 404 SO4   B O4  1 
HETATM 4499 S S   . SO4   K 3 .   ? -6.730  -55.031 24.025 0.67 76.15  ? 405 SO4   B S   1 
HETATM 4500 O O1  . SO4   K 3 .   ? -5.644  -54.503 23.201 0.67 70.73  ? 405 SO4   B O1  1 
HETATM 4501 O O2  . SO4   K 3 .   ? -7.863  -55.397 23.177 0.67 68.11  ? 405 SO4   B O2  1 
HETATM 4502 O O3  . SO4   K 3 .   ? -6.275  -56.221 24.744 0.67 67.39  ? 405 SO4   B O3  1 
HETATM 4503 O O4  . SO4   K 3 .   ? -7.149  -54.006 24.979 0.67 70.52  ? 405 SO4   B O4  1 
HETATM 4504 O O   . HOH   L 4 .   ? -15.325 -19.938 22.970 1.00 50.61  ? 501 HOH   A O   1 
HETATM 4505 O O   . HOH   L 4 .   ? -0.631  1.864   46.994 1.00 68.31  ? 502 HOH   A O   1 
HETATM 4506 O O   . HOH   L 4 .   ? -25.221 -6.500  25.628 1.00 66.16  ? 503 HOH   A O   1 
HETATM 4507 O O   . HOH   L 4 .   ? -20.151 0.561   29.070 1.00 57.30  ? 504 HOH   A O   1 
HETATM 4508 O O   . HOH   L 4 .   ? -11.133 -21.632 42.674 1.00 60.76  ? 505 HOH   A O   1 
HETATM 4509 O O   . HOH   L 4 .   ? -7.910  -8.652  26.687 1.00 38.18  ? 506 HOH   A O   1 
HETATM 4510 O O   . HOH   L 4 .   ? 13.271  0.597   7.874  1.00 47.47  ? 507 HOH   A O   1 
HETATM 4511 O O   . HOH   L 4 .   ? 0.274   -11.780 -9.091 1.00 68.93  ? 508 HOH   A O   1 
HETATM 4512 O O   . HOH   L 4 .   ? 23.190  -4.906  13.394 1.00 66.89  ? 509 HOH   A O   1 
HETATM 4513 O O   . HOH   L 4 .   ? 7.329   2.634   6.412  1.00 48.65  ? 510 HOH   A O   1 
HETATM 4514 O O   . HOH   L 4 .   ? 5.994   -0.217  20.461 1.00 43.98  ? 511 HOH   A O   1 
HETATM 4515 O O   . HOH   L 4 .   ? 14.280  -5.612  20.658 1.00 41.28  ? 512 HOH   A O   1 
HETATM 4516 O O   . HOH   L 4 .   ? -4.877  -12.448 28.279 1.00 57.07  ? 513 HOH   A O   1 
HETATM 4517 O O   . HOH   L 4 .   ? -2.128  1.750   11.090 1.00 44.19  ? 514 HOH   A O   1 
HETATM 4518 O O   . HOH   L 4 .   ? 2.074   3.556   11.071 1.00 60.59  ? 515 HOH   A O   1 
HETATM 4519 O O   . HOH   L 4 .   ? 15.619  -21.899 11.599 1.00 61.61  ? 516 HOH   A O   1 
HETATM 4520 O O   . HOH   L 4 .   ? -8.888  -22.176 43.011 1.00 57.16  ? 517 HOH   A O   1 
HETATM 4521 O O   . HOH   L 4 .   ? -17.876 0.042   30.201 1.00 54.25  ? 518 HOH   A O   1 
HETATM 4522 O O   . HOH   L 4 .   ? 2.504   -2.557  20.116 1.00 46.95  ? 519 HOH   A O   1 
HETATM 4523 O O   . HOH   L 4 .   ? -11.745 1.795   41.134 1.00 47.65  ? 520 HOH   A O   1 
HETATM 4524 O O   . HOH   L 4 .   ? -10.194 -11.666 5.168  1.00 54.98  ? 521 HOH   A O   1 
HETATM 4525 O O   . HOH   L 4 .   ? 5.608   -12.783 22.880 1.00 43.97  ? 522 HOH   A O   1 
HETATM 4526 O O   . HOH   L 4 .   ? -12.111 -19.290 42.898 1.00 58.37  ? 523 HOH   A O   1 
HETATM 4527 O O   . HOH   L 4 .   ? -3.240  -9.013  40.167 1.00 52.26  ? 524 HOH   A O   1 
HETATM 4528 O O   . HOH   L 4 .   ? -4.968  -23.191 12.455 1.00 49.82  ? 525 HOH   A O   1 
HETATM 4529 O O   . HOH   L 4 .   ? 2.685   -3.201  32.465 1.00 54.22  ? 526 HOH   A O   1 
HETATM 4530 O O   . HOH   L 4 .   ? 10.599  -17.821 7.469  1.00 58.91  ? 527 HOH   A O   1 
HETATM 4531 O O   . HOH   L 4 .   ? -6.887  2.078   9.967  1.00 46.28  ? 528 HOH   A O   1 
HETATM 4532 O O   . HOH   L 4 .   ? 1.471   -26.691 8.608  1.00 60.96  ? 529 HOH   A O   1 
HETATM 4533 O O   . HOH   L 4 .   ? 4.075   6.649   17.645 1.00 59.58  ? 530 HOH   A O   1 
HETATM 4534 O O   . HOH   L 4 .   ? -3.381  11.229  23.233 1.00 63.46  ? 531 HOH   A O   1 
HETATM 4535 O O   . HOH   L 4 .   ? 13.461  -6.086  -0.150 1.00 55.81  ? 532 HOH   A O   1 
HETATM 4536 O O   . HOH   L 4 .   ? 6.332   -21.391 2.653  1.00 64.63  ? 533 HOH   A O   1 
HETATM 4537 O O   . HOH   L 4 .   ? 16.917  3.990   19.457 1.00 62.28  ? 534 HOH   A O   1 
HETATM 4538 O O   . HOH   L 4 .   ? -1.941  -12.813 26.874 1.00 58.30  ? 535 HOH   A O   1 
HETATM 4539 O O   . HOH   L 4 .   ? 1.932   -17.559 25.635 1.00 54.10  ? 536 HOH   A O   1 
HETATM 4540 O O   . HOH   L 4 .   ? -4.270  1.985   9.551  1.00 38.93  ? 537 HOH   A O   1 
HETATM 4541 O O   . HOH   L 4 .   ? -21.124 -14.106 20.258 1.00 66.81  ? 538 HOH   A O   1 
HETATM 4542 O O   . HOH   L 4 .   ? 0.089   10.419  27.093 1.00 58.89  ? 539 HOH   A O   1 
HETATM 4543 O O   . HOH   L 4 .   ? -15.814 -7.765  22.263 1.00 51.98  ? 540 HOH   A O   1 
HETATM 4544 O O   . HOH   L 4 .   ? 14.126  -23.127 18.815 1.00 56.75  ? 541 HOH   A O   1 
HETATM 4545 O O   . HOH   L 4 .   ? 0.800   7.500   14.482 1.00 45.77  ? 542 HOH   A O   1 
HETATM 4546 O O   . HOH   L 4 .   ? -9.065  -19.398 6.208  1.00 52.38  ? 543 HOH   A O   1 
HETATM 4547 O O   . HOH   L 4 .   ? 1.340   -10.984 27.826 1.00 58.08  ? 544 HOH   A O   1 
HETATM 4548 O O   . HOH   L 4 .   ? 1.294   -19.173 28.316 1.00 61.30  ? 545 HOH   A O   1 
HETATM 4549 O O   . HOH   L 4 .   ? 9.407   -21.636 3.528  1.00 58.29  ? 546 HOH   A O   1 
HETATM 4550 O O   . HOH   L 4 .   ? -15.582 0.439   31.088 1.00 51.51  ? 547 HOH   A O   1 
HETATM 4551 O O   . HOH   L 4 .   ? 0.196   -26.045 16.953 1.00 50.02  ? 548 HOH   A O   1 
HETATM 4552 O O   . HOH   M 4 .   ? -13.536 -65.288 18.631 1.00 61.01  ? 501 HOH   B O   1 
HETATM 4553 O O   . HOH   M 4 .   ? -6.926  -55.702 31.312 1.00 61.17  ? 502 HOH   B O   1 
HETATM 4554 O O   . HOH   M 4 .   ? 8.553   -43.713 23.024 1.00 47.32  ? 503 HOH   B O   1 
HETATM 4555 O O   . HOH   M 4 .   ? 3.728   -62.291 21.727 1.00 72.66  ? 504 HOH   B O   1 
HETATM 4556 O O   . HOH   M 4 .   ? -16.342 -33.122 7.124  1.00 62.36  ? 505 HOH   B O   1 
HETATM 4557 O O   . HOH   M 4 .   ? 4.266   -43.098 36.054 1.00 61.11  ? 506 HOH   B O   1 
HETATM 4558 O O   . HOH   M 4 .   ? 0.407   -41.531 36.734 1.00 69.65  ? 507 HOH   B O   1 
HETATM 4559 O O   . HOH   M 4 .   ? 13.424  -33.324 38.587 1.00 52.81  ? 508 HOH   B O   1 
HETATM 4560 O O   . HOH   M 4 .   ? 10.925  -58.519 24.706 1.00 66.14  ? 509 HOH   B O   1 
HETATM 4561 O O   . HOH   M 4 .   ? 19.896  -53.600 25.768 1.00 55.38  ? 510 HOH   B O   1 
HETATM 4562 O O   . HOH   M 4 .   ? 2.232   -54.242 7.592  1.00 44.74  ? 511 HOH   B O   1 
HETATM 4563 O O   . HOH   M 4 .   ? 8.001   -45.828 -1.168 1.00 65.15  ? 512 HOH   B O   1 
HETATM 4564 O O   . HOH   M 4 .   ? 10.655  -47.643 5.268  1.00 51.21  ? 513 HOH   B O   1 
HETATM 4565 O O   . HOH   M 4 .   ? -9.598  -27.414 5.680  1.00 52.60  ? 514 HOH   B O   1 
HETATM 4566 O O   . HOH   M 4 .   ? 4.076   -31.309 8.970  1.00 53.20  ? 515 HOH   B O   1 
HETATM 4567 O O   . HOH   M 4 .   ? -13.899 -46.365 17.273 1.00 40.64  ? 516 HOH   B O   1 
HETATM 4568 O O   . HOH   M 4 .   ? 9.976   -29.347 37.758 1.00 57.71  ? 517 HOH   B O   1 
HETATM 4569 O O   . HOH   M 4 .   ? -21.227 -45.016 20.334 1.00 51.27  ? 518 HOH   B O   1 
HETATM 4570 O O   . HOH   M 4 .   ? -5.452  -51.895 16.744 1.00 42.22  ? 519 HOH   B O   1 
HETATM 4571 O O   . HOH   M 4 .   ? 23.039  -35.093 25.707 1.00 53.96  ? 520 HOH   B O   1 
HETATM 4572 O O   . HOH   M 4 .   ? -9.720  -33.657 14.312 1.00 46.72  ? 521 HOH   B O   1 
HETATM 4573 O O   . HOH   M 4 .   ? -7.624  -35.443 16.210 1.00 55.97  ? 522 HOH   B O   1 
HETATM 4574 O O   . HOH   M 4 .   ? 2.702   -39.614 22.977 1.00 57.28  ? 523 HOH   B O   1 
HETATM 4575 O O   . HOH   M 4 .   ? -1.027  -34.641 22.030 1.00 46.08  ? 524 HOH   B O   1 
HETATM 4576 O O   . HOH   M 4 .   ? -4.028  -58.224 14.300 1.00 53.12  ? 525 HOH   B O   1 
HETATM 4577 O O   . HOH   M 4 .   ? 1.484   -60.153 11.654 1.00 49.11  ? 526 HOH   B O   1 
HETATM 4578 O O   . HOH   M 4 .   ? -4.988  -39.472 19.641 1.00 45.65  ? 527 HOH   B O   1 
HETATM 4579 O O   . HOH   M 4 .   ? 12.172  -54.133 37.711 1.00 44.92  ? 528 HOH   B O   1 
HETATM 4580 O O   . HOH   M 4 .   ? 24.913  -48.113 21.920 1.00 56.54  ? 529 HOH   B O   1 
HETATM 4581 O O   . HOH   M 4 .   ? 8.972   -34.691 13.398 1.00 54.30  ? 530 HOH   B O   1 
HETATM 4582 O O   . HOH   M 4 .   ? -11.789 -38.024 -6.611 1.00 61.87  ? 531 HOH   B O   1 
HETATM 4583 O O   . HOH   M 4 .   ? 16.628  -51.858 13.120 1.00 49.25  ? 532 HOH   B O   1 
HETATM 4584 O O   . HOH   M 4 .   ? 5.200   -39.460 24.203 1.00 48.99  ? 533 HOH   B O   1 
HETATM 4585 O O   . HOH   M 4 .   ? 14.288  -55.826 16.316 1.00 52.98  ? 534 HOH   B O   1 
HETATM 4586 O O   . HOH   M 4 .   ? 13.904  -37.402 40.359 1.00 57.86  ? 535 HOH   B O   1 
HETATM 4587 O O   . HOH   M 4 .   ? -9.057  -32.953 12.072 1.00 45.74  ? 536 HOH   B O   1 
HETATM 4588 O O   . HOH   M 4 .   ? -0.588  -59.024 29.796 1.00 60.35  ? 537 HOH   B O   1 
HETATM 4589 O O   . HOH   M 4 .   ? -3.704  -60.466 13.157 1.00 48.15  ? 538 HOH   B O   1 
HETATM 4590 O O   . HOH   M 4 .   ? -13.997 -29.022 15.638 1.00 51.96  ? 539 HOH   B O   1 
HETATM 4591 O O   . HOH   M 4 .   ? 8.067   -62.369 23.731 1.00 64.63  ? 540 HOH   B O   1 
HETATM 4592 O O   . HOH   M 4 .   ? -0.966  -59.583 10.984 1.00 48.03  ? 541 HOH   B O   1 
HETATM 4593 O O   . HOH   M 4 .   ? -6.100  -30.192 24.744 1.00 62.73  ? 542 HOH   B O   1 
HETATM 4594 O O   . HOH   M 4 .   ? 18.840  -45.085 39.883 1.00 55.88  ? 543 HOH   B O   1 
HETATM 4595 O O   . HOH   M 4 .   ? 21.707  -36.964 16.599 1.00 67.03  ? 544 HOH   B O   1 
HETATM 4596 O O   . HOH   M 4 .   ? 15.695  -45.104 18.472 1.00 44.76  ? 545 HOH   B O   1 
HETATM 4597 O O   . HOH   M 4 .   ? 4.627   -54.264 6.002  1.00 46.73  ? 546 HOH   B O   1 
HETATM 4598 O O   . HOH   M 4 .   ? -13.354 -33.215 16.641 1.00 62.76  ? 547 HOH   B O   1 
HETATM 4599 O O   . HOH   M 4 .   ? 23.328  -51.180 32.495 1.00 69.78  ? 548 HOH   B O   1 
HETATM 4600 O O   . HOH   M 4 .   ? 16.758  -53.174 27.406 1.00 49.85  ? 549 HOH   B O   1 
HETATM 4601 O O   . HOH   M 4 .   ? 12.509  -33.696 3.745  1.00 72.08  ? 550 HOH   B O   1 
HETATM 4602 O O   . HOH   M 4 .   ? 8.571   -35.935 38.554 1.00 57.26  ? 551 HOH   B O   1 
HETATM 4603 O O   . HOH   M 4 .   ? 8.941   -54.816 23.948 1.00 53.24  ? 552 HOH   B O   1 
HETATM 4604 O O   . HOH   M 4 .   ? -0.661  -56.067 30.931 1.00 55.44  ? 553 HOH   B O   1 
HETATM 4605 O O   . HOH   M 4 .   ? 10.989  -40.904 1.957  1.00 69.56  ? 554 HOH   B O   1 
HETATM 4606 O O   . HOH   M 4 .   ? 17.758  -45.935 19.434 1.00 54.15  ? 555 HOH   B O   1 
HETATM 4607 O O   . HOH   M 4 .   ? -2.109  -24.886 11.706 1.00 52.81  ? 556 HOH   B O   1 
HETATM 4608 O O   . HOH   M 4 .   ? -7.229  -32.810 24.458 1.00 71.63  ? 557 HOH   B O   1 
HETATM 4609 O O   . HOH   M 4 .   ? -14.651 -39.531 -7.613 1.00 64.60  ? 558 HOH   B O   1 
HETATM 4610 O O   . HOH   M 4 .   ? -4.345  -32.772 24.888 1.00 59.92  ? 559 HOH   B O   1 
HETATM 4611 O O   . HOH   M 4 .   ? -15.166 -41.081 -9.727 1.00 58.68  ? 560 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   . ALA A 1   ? 1.1327 1.0797 1.1763 -0.2838 0.4075  -0.1502 76  ALA A N   
2    C CA  . ALA A 1   ? 1.0391 0.9445 1.0541 -0.2670 0.3742  -0.1280 76  ALA A CA  
3    C C   . ALA A 1   ? 0.9966 0.9121 1.0542 -0.2250 0.3588  -0.1372 76  ALA A C   
4    O O   . ALA A 1   ? 1.0832 1.0423 1.1987 -0.2086 0.3711  -0.1550 76  ALA A O   
5    C CB  . ALA A 1   ? 0.9312 0.8058 0.9318 -0.2764 0.3593  -0.1036 76  ALA A CB  
6    N N   . LEU A 2   ? 1.0295 0.9109 1.0646 -0.2065 0.3333  -0.1182 77  LEU A N   
7    C CA  . LEU A 2   ? 0.9922 0.8769 1.0605 -0.1680 0.3169  -0.1254 77  LEU A CA  
8    C C   . LEU A 2   ? 0.8921 0.7930 1.0070 -0.1558 0.3044  -0.1291 77  LEU A C   
9    O O   . LEU A 2   ? 1.2156 1.1003 1.3171 -0.1777 0.3030  -0.1201 77  LEU A O   
10   C CB  . LEU A 2   ? 0.8314 0.6797 0.8666 -0.1545 0.2925  -0.0976 77  LEU A CB  
11   C CG  . LEU A 2   ? 0.9583 0.7996 0.9399 -0.1772 0.2943  -0.0871 77  LEU A CG  
12   C CD1 . LEU A 2   ? 1.0118 0.8382 0.9787 -0.1626 0.2648  -0.0493 77  LEU A CD1 
13   C CD2 . LEU A 2   ? 1.0859 0.9333 1.0632 -0.1783 0.3198  -0.1251 77  LEU A CD2 
14   N N   . GLN A 3   ? 0.7440 0.6725 0.9057 -0.1265 0.2967  -0.1407 78  GLN A N   
15   C CA  . GLN A 3   ? 0.8255 0.7831 1.0302 -0.1238 0.2802  -0.1407 78  GLN A CA  
16   C C   . GLN A 3   ? 0.7657 0.7099 0.9840 -0.0884 0.2575  -0.1396 78  GLN A C   
17   O O   . GLN A 3   ? 0.7488 0.6853 0.9669 -0.0616 0.2616  -0.1447 78  GLN A O   
18   C CB  . GLN A 3   ? 0.7854 0.8273 1.0600 -0.1294 0.2970  -0.1465 78  GLN A CB  
19   C CG  . GLN A 3   ? 0.9313 0.9927 1.1974 -0.1670 0.3205  -0.1473 78  GLN A CG  
20   C CD  . GLN A 3   ? 1.2461 1.3985 1.5933 -0.1648 0.3460  -0.1451 78  GLN A CD  
21   O OE1 . GLN A 3   ? 1.4411 1.6565 1.8608 -0.1426 0.3380  -0.1333 78  GLN A OE1 
22   N NE2 . GLN A 3   ? 1.3667 1.5308 1.7073 -0.1864 0.3796  -0.1500 78  GLN A NE2 
23   N N   . PRO A 4   ? 0.7487 0.6820 0.9677 -0.0939 0.2355  -0.1340 79  PRO A N   
24   C CA  . PRO A 4   ? 0.6563 0.5725 0.8831 -0.0629 0.2140  -0.1328 79  PRO A CA  
25   C C   . PRO A 4   ? 0.6175 0.6073 0.9174 -0.0383 0.2104  -0.1368 79  PRO A C   
26   O O   . PRO A 4   ? 0.8873 0.9493 1.2423 -0.0459 0.2243  -0.1345 79  PRO A O   
27   C CB  . PRO A 4   ? 0.6787 0.5521 0.8689 -0.0905 0.1997  -0.1273 79  PRO A CB  
28   C CG  . PRO A 4   ? 0.6978 0.6096 0.8926 -0.1375 0.2065  -0.1279 79  PRO A CG  
29   C CD  . PRO A 4   ? 0.7526 0.6772 0.9495 -0.1376 0.2317  -0.1300 79  PRO A CD  
30   N N   . ARG A 5   ? 0.6110 0.5826 0.9160 -0.0054 0.1949  -0.1371 80  ARG A N   
31   C CA  . ARG A 5   ? 0.5347 0.5657 0.9084 0.0251  0.1925  -0.1348 80  ARG A CA  
32   C C   . ARG A 5   ? 0.5203 0.5338 0.8882 0.0328  0.1589  -0.1286 80  ARG A C   
33   O O   . ARG A 5   ? 0.5834 0.5261 0.9009 0.0458  0.1504  -0.1328 80  ARG A O   
34   C CB  . ARG A 5   ? 0.5297 0.5442 0.9054 0.0598  0.2196  -0.1464 80  ARG A CB  
35   C CG  . ARG A 5   ? 0.6968 0.7520 1.1379 0.0997  0.2259  -0.1413 80  ARG A CG  
36   C CD  . ARG A 5   ? 0.6916 0.6981 1.1051 0.1259  0.2585  -0.1579 80  ARG A CD  
37   N NE  . ARG A 5   ? 0.7383 0.7683 1.1752 0.1560  0.2533  -0.1397 80  ARG A NE  
38   C CZ  . ARG A 5   ? 0.5786 0.5913 0.9904 0.1710  0.2179  -0.1309 80  ARG A CZ  
39   N NH1 . ARG A 5   ? 0.6538 0.6271 1.0191 0.1609  0.1839  -0.1348 80  ARG A NH1 
40   N NH2 . ARG A 5   ? 0.6681 0.7024 1.0986 0.1968  0.2199  -0.1151 80  ARG A NH2 
41   N N   . ARG A 6   ? 0.5134 0.5959 0.9332 0.0214  0.1398  -0.1131 81  ARG A N   
42   C CA  . ARG A 6   ? 0.5128 0.5779 0.9166 0.0169  0.1066  -0.1067 81  ARG A CA  
43   C C   . ARG A 6   ? 0.4758 0.5301 0.9030 0.0702  0.1051  -0.1094 81  ARG A C   
44   O O   . ARG A 6   ? 0.6231 0.7297 1.1156 0.1048  0.1237  -0.1036 81  ARG A O   
45   C CB  . ARG A 6   ? 0.6644 0.8222 1.1168 -0.0205 0.0811  -0.0809 81  ARG A CB  
46   C CG  . ARG A 6   ? 0.7210 0.8551 1.1369 -0.0434 0.0447  -0.0742 81  ARG A CG  
47   C CD  . ARG A 6   ? 1.0580 1.2901 1.5058 -0.1027 0.0130  -0.0419 81  ARG A CD  
48   N NE  . ARG A 6   ? 1.2521 1.6050 1.8104 -0.0728 -0.0038 -0.0040 81  ARG A NE  
49   C CZ  . ARG A 6   ? 1.0840 1.5594 1.7547 -0.0533 0.0102  0.0298  81  ARG A CZ  
50   N NH1 . ARG A 6   ? 0.9313 1.4267 1.6160 -0.0636 0.0387  0.0253  81  ARG A NH1 
51   N NH2 . ARG A 6   ? 0.6574 1.2374 1.4323 -0.0204 0.0000  0.0737  81  ARG A NH2 
52   N N   . VAL A 7   ? 0.5170 0.4958 0.8882 0.0772  0.0897  -0.1169 82  VAL A N   
53   C CA  . VAL A 7   ? 0.5918 0.5562 0.9769 0.1211  0.0831  -0.1189 82  VAL A CA  
54   C C   . VAL A 7   ? 0.6273 0.6443 1.0511 0.1147  0.0530  -0.1012 82  VAL A C   
55   O O   . VAL A 7   ? 0.8663 0.8439 1.2401 0.0848  0.0300  -0.1003 82  VAL A O   
56   C CB  . VAL A 7   ? 0.5467 0.4166 0.8621 0.1319  0.0818  -0.1275 82  VAL A CB  
57   C CG1 . VAL A 7   ? 0.6363 0.5119 0.9062 0.1511  0.0623  -0.1092 82  VAL A CG1 
58   C CG2 . VAL A 7   ? 0.6532 0.4981 0.9224 0.1253  0.1006  -0.1255 82  VAL A CG2 
59   N N   . SER A 8   ? 0.8932 0.9963 1.4039 0.1412  0.0577  -0.0827 83  SER A N   
60   C CA  . SER A 8   ? 0.8474 1.0330 1.4139 0.1287  0.0265  -0.0502 83  SER A CA  
61   C C   . SER A 8   ? 0.7546 0.8976 1.2952 0.1459  0.0017  -0.0521 83  SER A C   
62   O O   . SER A 8   ? 0.6696 0.7578 1.1955 0.1904  0.0169  -0.0686 83  SER A O   
63   C CB  . SER A 8   ? 0.7148 1.0105 1.3986 0.1631  0.0484  -0.0173 83  SER A CB  
64   O OG  . SER A 8   ? 0.7686 1.1712 1.5219 0.1455  0.0144  0.0304  83  SER A OG  
65   N N   . PHE A 9   ? 0.4306 0.5972 0.9544 0.1017  -0.0371 -0.0339 84  PHE A N   
66   C CA  . PHE A 9   ? 0.7399 0.8738 1.2388 0.1100  -0.0629 -0.0318 84  PHE A CA  
67   C C   . PHE A 9   ? 0.7294 0.9411 1.2403 0.0517  -0.1065 0.0048  84  PHE A C   
68   O O   . PHE A 9   ? 0.8335 1.0615 1.3078 -0.0160 -0.1188 0.0108  84  PHE A O   
69   C CB  . PHE A 9   ? 0.5534 0.5491 0.9417 0.1037  -0.0566 -0.0675 84  PHE A CB  
70   C CG  . PHE A 9   ? 0.7498 0.6837 1.0496 0.0388  -0.0556 -0.0787 84  PHE A CG  
71   C CD1 . PHE A 9   ? 0.8814 0.7856 1.1596 0.0311  -0.0271 -0.0922 84  PHE A CD1 
72   C CD2 . PHE A 9   ? 0.8888 0.7836 1.1163 -0.0191 -0.0786 -0.0757 84  PHE A CD2 
73   C CE1 . PHE A 9   ? 0.6368 0.4708 0.8285 -0.0269 -0.0179 -0.1017 84  PHE A CE1 
74   C CE2 . PHE A 9   ? 0.7671 0.5813 0.8950 -0.0838 -0.0661 -0.0891 84  PHE A CE2 
75   C CZ  . PHE A 9   ? 0.7504 0.5329 0.8633 -0.0844 -0.0340 -0.1016 84  PHE A CZ  
76   N N   . ARG A 10  ? 0.7279 0.9882 1.2850 0.0719  -0.1307 0.0320  85  ARG A N   
77   C CA  . ARG A 10  ? 0.6534 0.9977 1.2196 0.0094  -0.1794 0.0756  85  ARG A CA  
78   C C   . ARG A 10  ? 0.7877 1.0238 1.2077 -0.0710 -0.1975 0.0472  85  ARG A C   
79   O O   . ARG A 10  ? 0.8133 0.9159 1.1465 -0.0544 -0.1808 0.0065  85  ARG A O   
80   C CB  . ARG A 10  ? 0.5861 0.9849 1.2191 0.0511  -0.1993 0.1092  85  ARG A CB  
81   C CG  . ARG A 10  ? 0.5581 1.0173 1.3145 0.1417  -0.1624 0.1289  85  ARG A CG  
82   C CD  . ARG A 10  ? 0.4051 0.9959 1.2426 0.1355  -0.1517 0.1798  85  ARG A CD  
83   N NE  . ARG A 10  ? 0.4416 1.1312 1.3075 0.0976  -0.1933 0.2377  85  ARG A NE  
84   C CZ  . ARG A 10  ? 0.4755 1.2805 1.4066 0.0783  -0.1960 0.2927  85  ARG A CZ  
85   N NH1 . ARG A 10  ? 0.4726 1.3145 1.4528 0.0943  -0.1602 0.2973  85  ARG A NH1 
86   N NH2 . ARG A 10  ? 0.5219 1.4038 1.4670 0.0407  -0.2342 0.3479  85  ARG A NH2 
87   N N   . GLY A 11  ? 0.7868 1.0766 1.1761 -0.1609 -0.2262 0.0715  86  GLY A N   
88   C CA  . GLY A 11  ? 0.8048 0.9805 1.0387 -0.2512 -0.2351 0.0458  86  GLY A CA  
89   C C   . GLY A 11  ? 0.9583 1.0377 1.1041 -0.2888 -0.1996 0.0092  86  GLY A C   
90   O O   . GLY A 11  ? 1.1040 1.0540 1.1054 -0.3574 -0.1895 -0.0178 86  GLY A O   
91   N N   . GLU A 12  ? 0.9791 1.1072 1.2000 -0.2476 -0.1746 0.0081  87  GLU A N   
92   C CA  . GLU A 12  ? 1.0662 1.1074 1.2082 -0.2818 -0.1407 -0.0222 87  GLU A CA  
93   C C   . GLU A 12  ? 1.1284 1.2183 1.2200 -0.3944 -0.1671 -0.0004 87  GLU A C   
94   O O   . GLU A 12  ? 1.0075 1.2559 1.1810 -0.4287 -0.2108 0.0509  87  GLU A O   
95   C CB  . GLU A 12  ? 0.9478 1.0292 1.1798 -0.2107 -0.1082 -0.0285 87  GLU A CB  
96   C CG  . GLU A 12  ? 0.9584 1.2160 1.3383 -0.1848 -0.1234 0.0157  87  GLU A CG  
97   C CD  . GLU A 12  ? 0.9886 1.2570 1.4303 -0.1231 -0.0812 0.0019  87  GLU A CD  
98   O OE1 . GLU A 12  ? 0.8879 1.0402 1.2573 -0.1099 -0.0495 -0.0374 87  GLU A OE1 
99   O OE2 . GLU A 12  ? 1.0376 1.4292 1.5992 -0.0891 -0.0760 0.0347  87  GLU A OE2 
100  N N   . ALA A 13  ? 1.1800 1.1327 1.1357 -0.4538 -0.1370 -0.0344 88  ALA A N   
101  C CA  . ALA A 13  ? 1.2454 1.2078 1.1142 -0.5770 -0.1560 -0.0222 88  ALA A CA  
102  C C   . ALA A 13  ? 1.2163 1.3153 1.1764 -0.5919 -0.1643 0.0053  88  ALA A C   
103  O O   . ALA A 13  ? 1.4651 1.6191 1.3805 -0.6985 -0.1923 0.0295  88  ALA A O   
104  C CB  . ALA A 13  ? 1.4188 1.1628 1.1002 -0.6322 -0.1060 -0.0702 88  ALA A CB  
105  N N   . SER A 14  ? 1.1654 1.3175 1.2432 -0.4959 -0.1394 0.0034  89  SER A N   
106  C CA  . SER A 14  ? 1.3036 1.5773 1.4684 -0.5045 -0.1383 0.0279  89  SER A CA  
107  C C   . SER A 14  ? 1.3657 1.7254 1.6823 -0.3904 -0.1191 0.0381  89  SER A C   
108  O O   . SER A 14  ? 1.3476 1.6081 1.6497 -0.3186 -0.0806 -0.0002 89  SER A O   
109  C CB  . SER A 14  ? 1.2417 1.3953 1.2997 -0.5457 -0.0986 -0.0095 89  SER A CB  
110  O OG  . SER A 14  ? 1.3052 1.5752 1.4463 -0.5540 -0.0965 0.0129  89  SER A OG  
111  N N   . GLU A 15  ? 1.5116 2.0526 1.9697 -0.3772 -0.1416 0.0941  90  GLU A N   
112  C CA  . GLU A 15  ? 1.4630 2.0783 2.0579 -0.2775 -0.1096 0.1061  90  GLU A CA  
113  C C   . GLU A 15  ? 1.4675 2.1082 2.0922 -0.2764 -0.0747 0.0997  90  GLU A C   
114  O O   . GLU A 15  ? 1.4423 2.1470 2.1749 -0.2061 -0.0410 0.1125  90  GLU A O   
115  C CB  . GLU A 15  ? 1.3411 2.1321 2.0836 -0.2521 -0.1354 0.1771  90  GLU A CB  
116  C CG  . GLU A 15  ? 1.3248 2.0903 2.0601 -0.2245 -0.1599 0.1820  90  GLU A CG  
117  C CD  . GLU A 15  ? 1.1871 2.1326 2.0751 -0.1990 -0.1837 0.2630  90  GLU A CD  
118  O OE1 . GLU A 15  ? 1.1329 2.2104 2.0805 -0.2414 -0.2018 0.3202  90  GLU A OE1 
119  O OE2 . GLU A 15  ? 1.1323 2.0666 2.0634 -0.1304 -0.1780 0.2678  90  GLU A OE2 
120  N N   . THR A 16  ? 1.4350 2.0167 1.9588 -0.3547 -0.0762 0.0796  91  THR A N   
121  C CA  . THR A 16  ? 1.3625 1.9492 1.8974 -0.3569 -0.0421 0.0679  91  THR A CA  
122  C C   . THR A 16  ? 1.3651 1.8001 1.8333 -0.3005 0.0028  0.0111  91  THR A C   
123  O O   . THR A 16  ? 1.3382 1.6373 1.7035 -0.3006 0.0050  -0.0222 91  THR A O   
124  C CB  . THR A 16  ? 1.3514 1.9340 1.7996 -0.4696 -0.0610 0.0724  91  THR A CB  
125  O OG1 . THR A 16  ? 1.5846 2.3072 2.0762 -0.5389 -0.1135 0.1310  91  THR A OG1 
126  C CG2 . THR A 16  ? 1.2922 1.9160 1.7770 -0.4737 -0.0304 0.0725  91  THR A CG2 
127  N N   . LEU A 17  ? 1.4236 1.8864 1.9524 -0.2542 0.0405  0.0058  92  LEU A N   
128  C CA  . LEU A 17  ? 1.5010 1.8423 1.9750 -0.2060 0.0782  -0.0373 92  LEU A CA  
129  C C   . LEU A 17  ? 1.4720 1.6879 1.8191 -0.2562 0.0865  -0.0656 92  LEU A C   
130  O O   . LEU A 17  ? 1.2672 1.3632 1.5443 -0.2290 0.1015  -0.0908 92  LEU A O   
131  C CB  . LEU A 17  ? 1.2996 1.6954 1.8501 -0.1626 0.1183  -0.0355 92  LEU A CB  
132  C CG  . LEU A 17  ? 1.0378 1.5177 1.7032 -0.0955 0.1361  -0.0131 92  LEU A CG  
133  C CD1 . LEU A 17  ? 0.8653 1.3967 1.5943 -0.0735 0.1851  -0.0076 92  LEU A CD1 
134  C CD2 . LEU A 17  ? 0.8346 1.2236 1.4664 -0.0384 0.1444  -0.0397 92  LEU A CD2 
135  N N   . GLN A 18  ? 1.4317 1.6734 1.7496 -0.3295 0.0808  -0.0566 93  GLN A N   
136  C CA  . GLN A 18  ? 1.5521 1.6683 1.7506 -0.3755 0.1014  -0.0813 93  GLN A CA  
137  C C   . GLN A 18  ? 1.7118 1.8259 1.8375 -0.4772 0.0785  -0.0715 93  GLN A C   
138  O O   . GLN A 18  ? 1.5924 1.8280 1.7723 -0.5172 0.0405  -0.0391 93  GLN A O   
139  C CB  . GLN A 18  ? 1.6254 1.7493 1.8422 -0.3636 0.1348  -0.0886 93  GLN A CB  
140  C CG  . GLN A 18  ? 1.6783 1.9237 1.9504 -0.4155 0.1282  -0.0654 93  GLN A CG  
141  C CD  . GLN A 18  ? 1.5512 1.9597 1.9681 -0.3787 0.1170  -0.0308 93  GLN A CD  
142  O OE1 . GLN A 18  ? 1.5912 2.0099 2.0632 -0.3085 0.1221  -0.0311 93  GLN A OE1 
143  N NE2 . GLN A 18  ? 1.3990 1.9355 1.8800 -0.4258 0.1063  0.0043  93  GLN A NE2 
144  N N   . SER A 19  ? 1.7351 1.7063 1.7319 -0.5233 0.1050  -0.0953 94  SER A N   
145  C CA  . SER A 19  ? 1.4678 1.3842 1.3511 -0.6315 0.1010  -0.0973 94  SER A CA  
146  C C   . SER A 19  ? 1.6406 1.6017 1.5302 -0.6753 0.1143  -0.0924 94  SER A C   
147  O O   . SER A 19  ? 1.6432 1.6108 1.5825 -0.6184 0.1419  -0.0990 94  SER A O   
148  C CB  . SER A 19  ? 1.5969 1.3003 1.3263 -0.6466 0.1409  -0.1273 94  SER A CB  
149  O OG  . SER A 19  ? 1.4593 1.0744 1.1838 -0.5793 0.1877  -0.1404 94  SER A OG  
150  N N   . PRO A 20  ? 1.7479 1.7430 1.5824 -0.7666 0.0919  -0.0778 95  PRO A N   
151  C CA  . PRO A 20  ? 1.7229 1.7700 1.5668 -0.7966 0.1004  -0.0695 95  PRO A CA  
152  C C   . PRO A 20  ? 1.7567 1.6507 1.5104 -0.7782 0.1542  -0.1012 95  PRO A C   
153  O O   . PRO A 20  ? 1.6467 1.5873 1.4394 -0.7794 0.1690  -0.0981 95  PRO A O   
154  C CB  . PRO A 20  ? 1.5994 1.6782 1.3641 -0.8792 0.0636  -0.0486 95  PRO A CB  
155  C CG  . PRO A 20  ? 1.4493 1.5817 1.2373 -0.8844 0.0224  -0.0282 95  PRO A CG  
156  C CD  . PRO A 20  ? 1.5770 1.5870 1.3471 -0.8224 0.0508  -0.0607 95  PRO A CD  
157  N N   . GLY A 21  ? 1.6778 1.3970 1.3183 -0.7546 0.1867  -0.1255 96  GLY A N   
158  C CA  . GLY A 21  ? 1.7428 1.3285 1.3117 -0.7245 0.2397  -0.1426 96  GLY A CA  
159  C C   . GLY A 21  ? 1.6496 1.2478 1.3097 -0.6550 0.2639  -0.1427 96  GLY A C   
160  O O   . GLY A 21  ? 1.5882 1.1053 1.2082 -0.6307 0.3023  -0.1460 96  GLY A O   
161  N N   . TYR A 22  ? 1.2886 0.9953 1.0680 -0.6116 0.2405  -0.1352 97  TYR A N   
162  C CA  . TYR A 22  ? 1.4270 1.1567 1.2819 -0.5222 0.2546  -0.1333 97  TYR A CA  
163  C C   . TYR A 22  ? 1.2664 1.1106 1.1972 -0.5256 0.2552  -0.1267 97  TYR A C   
164  O O   . TYR A 22  ? 1.2607 1.2427 1.2729 -0.5443 0.2290  -0.1136 97  TYR A O   
165  C CB  . TYR A 22  ? 1.2533 1.0395 1.1858 -0.4545 0.2297  -0.1294 97  TYR A CB  
166  C CG  . TYR A 22  ? 1.1422 0.9667 1.1471 -0.3785 0.2402  -0.1275 97  TYR A CG  
167  C CD1 . TYR A 22  ? 1.1700 0.9008 1.1320 -0.3453 0.2697  -0.1261 97  TYR A CD1 
168  C CD2 . TYR A 22  ? 0.8839 0.8354 0.9952 -0.3444 0.2244  -0.1221 97  TYR A CD2 
169  C CE1 . TYR A 22  ? 1.0405 0.8076 1.0526 -0.2929 0.2747  -0.1217 97  TYR A CE1 
170  C CE2 . TYR A 22  ? 0.8275 0.7943 0.9799 -0.2884 0.2400  -0.1249 97  TYR A CE2 
171  C CZ  . TYR A 22  ? 0.8466 0.7231 0.9435 -0.2691 0.2608  -0.1259 97  TYR A CZ  
172  O OH  . TYR A 22  ? 0.8852 0.7785 1.0078 -0.2297 0.2717  -0.1260 97  TYR A OH  
173  N N   . ASP A 23  ? 1.2919 1.0815 1.1990 -0.5072 0.2880  -0.1297 98  ASP A N   
174  C CA  . ASP A 23  ? 1.1054 0.9841 1.0727 -0.5066 0.2966  -0.1264 98  ASP A CA  
175  C C   . ASP A 23  ? 1.1772 1.0751 1.1986 -0.4321 0.3055  -0.1261 98  ASP A C   
176  O O   . ASP A 23  ? 1.2500 1.0583 1.2237 -0.4051 0.3241  -0.1228 98  ASP A O   
177  C CB  . ASP A 23  ? 1.3733 1.1760 1.2612 -0.5555 0.3266  -0.1287 98  ASP A CB  
178  C CG  . ASP A 23  ? 1.4252 1.3284 1.3689 -0.5745 0.3331  -0.1258 98  ASP A CG  
179  O OD1 . ASP A 23  ? 1.2148 1.2165 1.2507 -0.5307 0.3294  -0.1230 98  ASP A OD1 
180  O OD2 . ASP A 23  ? 1.4196 1.2944 1.3087 -0.6347 0.3478  -0.1267 98  ASP A OD2 
181  N N   . PRO A 24  ? 1.2284 1.2378 1.3444 -0.4006 0.2968  -0.1248 99  PRO A N   
182  C CA  . PRO A 24  ? 1.0342 1.0434 1.1781 -0.3414 0.3090  -0.1288 99  PRO A CA  
183  C C   . PRO A 24  ? 1.3083 1.2909 1.4213 -0.3474 0.3369  -0.1302 99  PRO A C   
184  O O   . PRO A 24  ? 1.0915 1.0625 1.2044 -0.3138 0.3459  -0.1318 99  PRO A O   
185  C CB  . PRO A 24  ? 0.8634 0.9875 1.1084 -0.3156 0.3066  -0.1263 99  PRO A CB  
186  C CG  . PRO A 24  ? 0.8283 1.0154 1.1054 -0.3505 0.2786  -0.1120 99  PRO A CG  
187  C CD  . PRO A 24  ? 1.0189 1.1549 1.2185 -0.4179 0.2781  -0.1131 99  PRO A CD  
188  N N   . SER A 25  ? 1.2604 1.2316 1.3394 -0.3960 0.3497  -0.1285 100 SER A N   
189  C CA  . SER A 25  ? 0.9922 0.9426 1.0411 -0.4062 0.3751  -0.1272 100 SER A CA  
190  C C   . SER A 25  ? 1.2374 1.0814 1.2115 -0.3987 0.3810  -0.1109 100 SER A C   
191  O O   . SER A 25  ? 1.1849 1.0147 1.1373 -0.3951 0.3940  -0.1004 100 SER A O   
192  C CB  . SER A 25  ? 1.0240 1.0118 1.0725 -0.4610 0.3883  -0.1288 100 SER A CB  
193  O OG  . SER A 25  ? 1.1569 1.2601 1.2908 -0.4666 0.3846  -0.1296 100 SER A OG  
194  N N   . ARG A 26  ? 1.1500 0.9189 1.0840 -0.3976 0.3754  -0.1030 101 ARG A N   
195  C CA  . ARG A 26  ? 1.1166 0.7841 0.9917 -0.3834 0.3921  -0.0762 101 ARG A CA  
196  C C   . ARG A 26  ? 1.3025 0.9758 1.1997 -0.3315 0.3802  -0.0570 101 ARG A C   
197  O O   . ARG A 26  ? 1.2007 0.9239 1.1417 -0.3055 0.3593  -0.0716 101 ARG A O   
198  C CB  . ARG A 26  ? 1.4384 1.0077 1.2573 -0.3965 0.4031  -0.0742 101 ARG A CB  
199  C CG  . ARG A 26  ? 1.3546 0.9297 1.1465 -0.4606 0.4031  -0.0971 101 ARG A CG  
200  C CD  . ARG A 26  ? 1.4565 0.9725 1.1839 -0.4980 0.4304  -0.0914 101 ARG A CD  
201  N NE  . ARG A 26  ? 1.6637 1.0507 1.3142 -0.4735 0.4537  -0.0754 101 ARG A NE  
202  C CZ  . ARG A 26  ? 1.7589 1.0768 1.3419 -0.4904 0.4760  -0.0728 101 ARG A CZ  
203  N NH1 . ARG A 26  ? 1.5890 0.9496 1.1651 -0.5357 0.4733  -0.0845 101 ARG A NH1 
204  N NH2 . ARG A 26  ? 1.8803 1.0857 1.4048 -0.4583 0.5055  -0.0578 101 ARG A NH2 
205  N N   . PRO A 27  ? 1.4260 1.0540 1.2951 -0.3183 0.3930  -0.0183 102 PRO A N   
206  C CA  . PRO A 27  ? 1.3381 0.9780 1.2252 -0.2779 0.3774  0.0107  102 PRO A CA  
207  C C   . PRO A 27  ? 1.3527 0.9371 1.2415 -0.2392 0.3758  0.0264  102 PRO A C   
208  O O   . PRO A 27  ? 1.4282 1.0305 1.3379 -0.2060 0.3600  0.0519  102 PRO A O   
209  C CB  . PRO A 27  ? 1.3284 0.9529 1.1903 -0.2855 0.3906  0.0607  102 PRO A CB  
210  C CG  . PRO A 27  ? 1.4398 0.9951 1.2630 -0.3094 0.4235  0.0649  102 PRO A CG  
211  C CD  . PRO A 27  ? 1.2512 0.8303 1.0765 -0.3436 0.4207  0.0074  102 PRO A CD  
212  N N   . GLU A 28  ? 1.4395 0.9535 1.2987 -0.2485 0.3935  0.0126  103 GLU A N   
213  C CA  . GLU A 28  ? 1.3684 0.8145 1.2172 -0.2159 0.4003  0.0237  103 GLU A CA  
214  C C   . GLU A 28  ? 1.2056 0.7076 1.0917 -0.2043 0.3653  -0.0114 103 GLU A C   
215  O O   . GLU A 28  ? 1.1565 0.7291 1.0681 -0.2293 0.3457  -0.0472 103 GLU A O   
216  C CB  . GLU A 28  ? 1.4911 0.8195 1.2701 -0.2413 0.4402  0.0189  103 GLU A CB  
217  C CG  . GLU A 28  ? 1.4150 0.6946 1.1651 -0.2179 0.4665  0.0574  103 GLU A CG  
218  C CD  . GLU A 28  ? 1.7684 1.0778 1.5101 -0.2559 0.4711  0.0579  103 GLU A CD  
219  O OE1 . GLU A 28  ? 1.5284 0.8837 1.2713 -0.3068 0.4601  0.0190  103 GLU A OE1 
220  O OE2 . GLU A 28  ? 1.8029 1.1004 1.5440 -0.2342 0.4843  0.1001  103 GLU A OE2 
221  N N   . SER A 29  ? 1.1119 0.5849 1.0074 -0.1632 0.3609  0.0055  104 SER A N   
222  C CA  . SER A 29  ? 0.9957 0.5150 0.9256 -0.1473 0.3291  -0.0221 104 SER A CA  
223  C C   . SER A 29  ? 1.0861 0.5730 0.9871 -0.1794 0.3284  -0.0546 104 SER A C   
224  O O   . SER A 29  ? 1.2465 0.6475 1.0838 -0.2125 0.3578  -0.0551 104 SER A O   
225  C CB  . SER A 29  ? 1.0064 0.5016 0.9504 -0.0976 0.3255  0.0084  104 SER A CB  
226  O OG  . SER A 29  ? 1.2767 0.6616 1.1777 -0.0850 0.3638  0.0351  104 SER A OG  
227  N N   . PHE A 30  ? 1.1759 0.5190 0.8929 -0.1871 0.4224  -0.0858 105 PHE A N   
228  C CA  . PHE A 30  ? 1.1411 0.5420 0.9247 -0.1797 0.4265  -0.0997 105 PHE A CA  
229  C C   . PHE A 30  ? 0.9974 0.3968 0.7956 -0.1557 0.4069  -0.0773 105 PHE A C   
230  O O   . PHE A 30  ? 1.1333 0.5450 0.9473 -0.1550 0.4183  -0.0858 105 PHE A O   
231  C CB  . PHE A 30  ? 1.0125 0.4854 0.8737 -0.1764 0.4207  -0.1161 105 PHE A CB  
232  C CG  . PHE A 30  ? 0.8460 0.3727 0.7722 -0.1656 0.4226  -0.1266 105 PHE A CG  
233  C CD1 . PHE A 30  ? 0.9986 0.5446 0.9395 -0.1814 0.4516  -0.1554 105 PHE A CD1 
234  C CD2 . PHE A 30  ? 0.8221 0.3782 0.7938 -0.1416 0.3987  -0.1102 105 PHE A CD2 
235  C CE1 . PHE A 30  ? 1.1509 0.7438 1.1509 -0.1746 0.4551  -0.1679 105 PHE A CE1 
236  C CE2 . PHE A 30  ? 0.8211 0.4194 0.8451 -0.1333 0.4033  -0.1197 105 PHE A CE2 
237  C CZ  . PHE A 30  ? 1.1115 0.7278 1.1502 -0.1505 0.4309  -0.1488 105 PHE A CZ  
238  N N   . PHE A 31  ? 1.1520 0.5357 0.9455 -0.1376 0.3803  -0.0511 106 PHE A N   
239  C CA  . PHE A 31  ? 1.1441 0.5218 0.9471 -0.1125 0.3637  -0.0289 106 PHE A CA  
240  C C   . PHE A 31  ? 1.1743 0.4858 0.9087 -0.1116 0.3801  -0.0191 106 PHE A C   
241  O O   . PHE A 31  ? 1.3987 0.7161 1.1463 -0.1038 0.3856  -0.0201 106 PHE A O   
242  C CB  . PHE A 31  ? 1.0676 0.4383 0.8783 -0.0942 0.3364  -0.0049 106 PHE A CB  
243  C CG  . PHE A 31  ? 0.9470 0.3127 0.7692 -0.0649 0.3201  0.0185  106 PHE A CG  
244  C CD1 . PHE A 31  ? 0.9245 0.3466 0.8106 -0.0527 0.3134  0.0135  106 PHE A CD1 
245  C CD2 . PHE A 31  ? 1.0386 0.3407 0.8027 -0.0460 0.3125  0.0471  106 PHE A CD2 
246  C CE1 . PHE A 31  ? 0.8685 0.2881 0.7646 -0.0266 0.3009  0.0326  106 PHE A CE1 
247  C CE2 . PHE A 31  ? 1.2327 0.5352 1.0118 -0.0147 0.2984  0.0678  106 PHE A CE2 
248  C CZ  . PHE A 31  ? 0.9388 0.3023 0.7864 -0.0075 0.2933  0.0584  106 PHE A CZ  
249  N N   . GLN A 32  ? 1.1371 0.3791 0.7913 -0.1200 0.3913  -0.0101 107 GLN A N   
250  C CA  . GLN A 32  ? 1.3210 0.4885 0.9000 -0.1152 0.4099  0.0024  107 GLN A CA  
251  C C   . GLN A 32  ? 1.2502 0.4192 0.8263 -0.1399 0.4463  -0.0277 107 GLN A C   
252  O O   . GLN A 32  ? 1.5744 0.6994 1.1149 -0.1361 0.4645  -0.0240 107 GLN A O   
253  C CB  . GLN A 32  ? 1.4876 0.5719 0.9689 -0.1145 0.4136  0.0230  107 GLN A CB  
254  C CG  . GLN A 32  ? 1.6479 0.7139 1.1138 -0.0852 0.3798  0.0581  107 GLN A CG  
255  C CD  . GLN A 32  ? 1.8259 0.8135 1.1859 -0.0870 0.3815  0.0778  107 GLN A CD  
256  O OE1 . GLN A 32  ? 1.8577 0.8050 1.1584 -0.1126 0.4095  0.0631  107 GLN A OE1 
257  N NE2 . GLN A 32  ? 1.8453 0.8096 1.1745 -0.0583 0.3515  0.1119  107 GLN A NE2 
258  N N   . GLN A 33  ? 1.2274 0.4452 0.8411 -0.1646 0.4598  -0.0586 108 GLN A N   
259  C CA  . GLN A 33  ? 1.3258 0.5467 0.9382 -0.1901 0.4976  -0.0903 108 GLN A CA  
260  C C   . GLN A 33  ? 1.1515 0.4385 0.8393 -0.1890 0.4972  -0.1073 108 GLN A C   
261  O O   . GLN A 33  ? 1.3724 0.6449 1.0500 -0.2032 0.5258  -0.1244 108 GLN A O   
262  C CB  . GLN A 33  ? 1.2325 0.4707 0.8448 -0.2163 0.5173  -0.1175 108 GLN A CB  
263  C CG  . GLN A 33  ? 1.3658 0.5277 0.8887 -0.2252 0.5276  -0.1071 108 GLN A CG  
264  C CD  . GLN A 33  ? 1.5318 0.7049 1.0493 -0.2548 0.5563  -0.1401 108 GLN A CD  
265  O OE1 . GLN A 33  ? 1.7007 0.9054 1.2501 -0.2731 0.5848  -0.1726 108 GLN A OE1 
266  N NE2 . GLN A 33  ? 1.4425 0.5895 0.9193 -0.2607 0.5508  -0.1341 108 GLN A NE2 
267  N N   . SER A 34  ? 1.1843 0.5386 0.9435 -0.1740 0.4686  -0.1044 109 SER A N   
268  C CA  . SER A 34  ? 1.2443 0.6590 1.0709 -0.1732 0.4694  -0.1215 109 SER A CA  
269  C C   . SER A 34  ? 1.1549 0.5669 0.9934 -0.1492 0.4497  -0.0998 109 SER A C   
270  O O   . SER A 34  ? 0.9620 0.4195 0.8525 -0.1466 0.4482  -0.1109 109 SER A O   
271  C CB  . SER A 34  ? 1.0437 0.5284 0.9387 -0.1704 0.4572  -0.1338 109 SER A CB  
272  O OG  . SER A 34  ? 1.3934 0.9308 1.3501 -0.1677 0.4585  -0.1488 109 SER A OG  
273  N N   . PHE A 35  ? 1.2398 0.5978 1.0307 -0.1311 0.4365  -0.0702 110 PHE A N   
274  C CA  . PHE A 35  ? 1.0955 0.4524 0.8995 -0.1053 0.4180  -0.0495 110 PHE A CA  
275  C C   . PHE A 35  ? 1.2793 0.5583 1.0140 -0.0947 0.4267  -0.0292 110 PHE A C   
276  O O   . PHE A 35  ? 1.4114 0.6403 1.0928 -0.0892 0.4236  -0.0116 110 PHE A O   
277  C CB  . PHE A 35  ? 0.9327 0.3254 0.7766 -0.0809 0.3820  -0.0290 110 PHE A CB  
278  C CG  . PHE A 35  ? 0.9450 0.4090 0.8581 -0.0830 0.3749  -0.0444 110 PHE A CG  
279  C CD1 . PHE A 35  ? 0.8913 0.3916 0.8472 -0.0755 0.3747  -0.0504 110 PHE A CD1 
280  C CD2 . PHE A 35  ? 0.9386 0.4280 0.8702 -0.0916 0.3712  -0.0525 110 PHE A CD2 
281  C CE1 . PHE A 35  ? 0.8574 0.4147 0.8718 -0.0741 0.3710  -0.0614 110 PHE A CE1 
282  C CE2 . PHE A 35  ? 0.8838 0.4322 0.8768 -0.0894 0.3682  -0.0647 110 PHE A CE2 
283  C CZ  . PHE A 35  ? 0.8841 0.4649 0.9179 -0.0796 0.3683  -0.0677 110 PHE A CZ  
284  N N   . GLN A 36  ? 1.2600 0.5248 0.9922 -0.0909 0.4393  -0.0315 111 GLN A N   
285  C CA  . GLN A 36  ? 1.4241 0.6188 1.0996 -0.0717 0.4451  -0.0086 111 GLN A CA  
286  C C   . GLN A 36  ? 1.3242 0.5405 1.0299 -0.0353 0.4094  0.0188  111 GLN A C   
287  O O   . GLN A 36  ? 1.1297 0.3927 0.8867 -0.0285 0.4003  0.0134  111 GLN A O   
288  C CB  . GLN A 36  ? 1.4876 0.6543 1.1464 -0.0872 0.4804  -0.0269 111 GLN A CB  
289  C CG  . GLN A 36  ? 1.6006 0.6849 1.1945 -0.0676 0.4943  -0.0051 111 GLN A CG  
290  C CD  . GLN A 36  ? 1.6134 0.6782 1.2041 -0.0803 0.5263  -0.0228 111 GLN A CD  
291  O OE1 . GLN A 36  ? 1.7158 0.8352 1.3623 -0.0852 0.5203  -0.0375 111 GLN A OE1 
292  N NE2 . GLN A 36  ? 1.9977 0.9789 1.5185 -0.0862 0.5634  -0.0219 111 GLN A NE2 
293  N N   . ARG A 37  ? 1.2641 0.4474 0.9376 -0.0122 0.3905  0.0472  112 ARG A N   
294  C CA  . ARG A 37  ? 1.1599 0.3636 0.8625 0.0232  0.3595  0.0722  112 ARG A CA  
295  C C   . ARG A 37  ? 1.2472 0.4214 0.9355 0.0434  0.3689  0.0811  112 ARG A C   
296  O O   . ARG A 37  ? 1.3807 0.4943 1.0151 0.0360  0.3987  0.0775  112 ARG A O   
297  C CB  . ARG A 37  ? 1.2058 0.3766 0.8721 0.0449  0.3395  0.1006  112 ARG A CB  
298  C CG  . ARG A 37  ? 1.2782 0.4889 0.9755 0.0319  0.3229  0.0952  112 ARG A CG  
299  C CD  . ARG A 37  ? 1.4345 0.6310 1.1199 0.0637  0.2955  0.1262  112 ARG A CD  
300  N NE  . ARG A 37  ? 1.5537 0.6964 1.1690 0.0571  0.2980  0.1367  112 ARG A NE  
301  C CZ  . ARG A 37  ? 1.6822 0.7840 1.2460 0.0904  0.2788  0.1698  112 ARG A CZ  
302  N NH1 . ARG A 37  ? 1.6825 0.7975 1.2657 0.1358  0.2554  0.1949  112 ARG A NH1 
303  N NH2 . ARG A 37  ? 1.6520 0.7016 1.1386 0.0810  0.2820  0.1784  112 ARG A NH2 
304  N N   . LEU A 38  ? 1.1501 0.3659 0.8866 0.0680  0.3468  0.0914  113 LEU A N   
305  C CA  . LEU A 38  ? 1.1884 0.3810 0.9164 0.0893  0.3546  0.0997  113 LEU A CA  
306  C C   . LEU A 38  ? 1.3320 0.5276 1.0687 0.1322  0.3270  0.1297  113 LEU A C   
307  O O   . LEU A 38  ? 1.7236 0.8619 1.4108 0.1582  0.3316  0.1506  113 LEU A O   
308  C CB  . LEU A 38  ? 1.1212 0.3623 0.8989 0.0772  0.3614  0.0785  113 LEU A CB  
309  C CG  . LEU A 38  ? 1.1096 0.3558 0.8875 0.0388  0.3892  0.0468  113 LEU A CG  
310  C CD1 . LEU A 38  ? 1.0649 0.3475 0.8823 0.0367  0.3940  0.0328  113 LEU A CD1 
311  C CD2 . LEU A 38  ? 1.3532 0.5240 1.0649 0.0227  0.4251  0.0399  113 LEU A CD2 
312  N N   . SER A 39  ? 1.1199 0.3821 0.9192 0.1416  0.3004  0.1318  114 SER A N   
313  C CA  . SER A 39  ? 1.1973 0.4752 1.0176 0.1819  0.2755  0.1558  114 SER A CA  
314  C C   . SER A 39  ? 1.1117 0.4511 0.9887 0.1821  0.2514  0.1559  114 SER A C   
315  O O   . SER A 39  ? 1.0286 0.4056 0.9373 0.1528  0.2551  0.1362  114 SER A O   
316  C CB  . SER A 39  ? 1.1818 0.4745 1.0272 0.1991  0.2802  0.1549  114 SER A CB  
317  O OG  . SER A 39  ? 1.1609 0.5089 1.0562 0.1778  0.2840  0.1337  114 SER A OG  
318  N N   . ARG A 40  ? 1.0713 0.4214 0.9619 0.2186  0.2284  0.1784  115 ARG A N   
319  C CA  . ARG A 40  ? 1.0113 0.4171 0.9599 0.2238  0.2094  0.1796  115 ARG A CA  
320  C C   . ARG A 40  ? 0.9469 0.4164 0.9655 0.2326  0.2061  0.1723  115 ARG A C   
321  O O   . ARG A 40  ? 1.0204 0.4943 1.0463 0.2636  0.2005  0.1831  115 ARG A O   
322  C CB  . ARG A 40  ? 1.0732 0.4652 1.0026 0.2635  0.1865  0.2077  115 ARG A CB  
323  C CG  . ARG A 40  ? 1.0934 0.5414 1.0870 0.2698  0.1714  0.2085  115 ARG A CG  
324  C CD  . ARG A 40  ? 1.3325 0.7633 1.2889 0.3089  0.1483  0.2368  115 ARG A CD  
325  N NE  . ARG A 40  ? 1.2781 0.7353 1.2366 0.3677  0.1221  0.2603  115 ARG A NE  
326  C CZ  . ARG A 40  ? 1.4990 0.9800 1.4243 0.4058  0.0861  0.2793  115 ARG A CZ  
327  N NH1 . ARG A 40  ? 1.5534 1.0450 1.4367 0.3770  0.0684  0.2690  115 ARG A NH1 
328  N NH2 . ARG A 40  ? 1.5662 1.0755 1.5008 0.4689  0.0633  0.3025  115 ARG A NH2 
329  N N   . LEU A 41  ? 0.9682 0.4850 1.0343 0.2057  0.2118  0.1544  116 LEU A N   
330  C CA  . LEU A 41  ? 0.8117 0.3845 0.9350 0.2092  0.2140  0.1481  116 LEU A CA  
331  C C   . LEU A 41  ? 0.9465 0.5688 1.1339 0.2317  0.2005  0.1572  116 LEU A C   
332  O O   . LEU A 41  ? 1.1492 0.8096 1.3773 0.2475  0.2006  0.1583  116 LEU A O   
333  C CB  . LEU A 41  ? 0.7544 0.3546 0.8940 0.1742  0.2282  0.1284  116 LEU A CB  
334  C CG  . LEU A 41  ? 0.7984 0.3684 0.8937 0.1546  0.2434  0.1155  116 LEU A CG  
335  C CD1 . LEU A 41  ? 0.8088 0.4130 0.9246 0.1286  0.2527  0.0988  116 LEU A CD1 
336  C CD2 . LEU A 41  ? 0.8040 0.3587 0.8847 0.1693  0.2515  0.1179  116 LEU A CD2 
337  N N   . GLY A 42  ? 0.8338 0.4589 1.0362 0.2331  0.1914  0.1622  117 GLY A N   
338  C CA  . GLY A 42  ? 0.9069 0.5906 1.1873 0.2569  0.1795  0.1686  117 GLY A CA  
339  C C   . GLY A 42  ? 0.8489 0.5256 1.1350 0.2575  0.1694  0.1739  117 GLY A C   
340  O O   . GLY A 42  ? 0.9328 0.5581 1.1634 0.2276  0.1775  0.1676  117 GLY A O   
341  N N   . HIS A 43  ? 1.0215 0.7830 1.3557 0.2700  0.1388  0.1691  118 HIS A N   
342  C CA  . HIS A 43  ? 0.9922 0.7925 1.3148 0.2454  0.1117  0.1535  118 HIS A CA  
343  C C   . HIS A 43  ? 0.8866 0.8012 1.3085 0.2358  0.0957  0.1303  118 HIS A C   
344  O O   . HIS A 43  ? 0.9817 0.9417 1.4777 0.2505  0.1067  0.1293  118 HIS A O   
345  C CB  . HIS A 43  ? 0.9990 0.7685 1.2348 0.2766  0.0817  0.1741  118 HIS A CB  
346  C CG  . HIS A 43  ? 1.1574 0.9862 1.4176 0.3323  0.0501  0.1898  118 HIS A CG  
347  N ND1 . HIS A 43  ? 1.2215 1.1717 1.5590 0.3354  0.0175  0.1703  118 HIS A ND1 
348  C CD2 . HIS A 43  ? 1.2274 1.0131 1.4464 0.3886  0.0468  0.2213  118 HIS A CD2 
349  C CE1 . HIS A 43  ? 1.2883 1.2773 1.6361 0.3940  -0.0076 0.1891  118 HIS A CE1 
350  N NE2 . HIS A 43  ? 1.2143 1.1001 1.4883 0.4296  0.0103  0.2224  118 HIS A NE2 
351  N N   . GLY A 44  ? 1.0756 1.0361 1.4980 0.2076  0.0728  0.1083  119 GLY A N   
352  C CA  . GLY A 44  ? 0.9644 1.0347 1.4798 0.1881  0.0595  0.0777  119 GLY A CA  
353  C C   . GLY A 44  ? 1.0319 1.1147 1.5356 0.1369  0.0547  0.0470  119 GLY A C   
354  O O   . GLY A 44  ? 1.0542 1.0759 1.4717 0.1274  0.0495  0.0523  119 GLY A O   
355  N N   . SER A 45  ? 0.9424 1.1021 1.5345 0.1024  0.0613  0.0127  120 SER A N   
356  C CA  . SER A 45  ? 0.9093 1.0764 1.4986 0.0492  0.0652  -0.0216 120 SER A CA  
357  C C   . SER A 45  ? 1.1103 1.1769 1.6578 0.0222  0.1064  -0.0167 120 SER A C   
358  O O   . SER A 45  ? 1.0260 1.0646 1.5286 -0.0091 0.1071  -0.0334 120 SER A O   
359  C CB  . SER A 45  ? 0.6762 0.9371 1.3732 0.0144  0.0732  -0.0617 120 SER A CB  
360  O OG  . SER A 45  ? 0.8702 1.1279 1.5637 -0.0394 0.0834  -0.0975 120 SER A OG  
361  N N   . TYR A 46  ? 1.1551 1.1708 1.7145 0.0365  0.1397  0.0050  121 TYR A N   
362  C CA  . TYR A 46  ? 1.0992 1.0332 1.6267 0.0175  0.1762  0.0092  121 TYR A CA  
363  C C   . TYR A 46  ? 1.1648 1.0261 1.5955 0.0272  0.1691  0.0263  121 TYR A C   
364  O O   . TYR A 46  ? 0.9880 0.7916 1.3908 0.0097  0.1950  0.0246  121 TYR A O   
365  C CB  . TYR A 46  ? 1.2716 1.1826 1.8366 0.0339  0.2096  0.0262  121 TYR A CB  
366  C CG  . TYR A 46  ? 1.2714 1.1671 1.8143 0.0796  0.2002  0.0560  121 TYR A CG  
367  C CD1 . TYR A 46  ? 1.1503 1.1082 1.7446 0.1066  0.1861  0.0608  121 TYR A CD1 
368  C CD2 . TYR A 46  ? 1.1334 0.9538 1.6076 0.0944  0.2086  0.0756  121 TYR A CD2 
369  C CE1 . TYR A 46  ? 1.1444 1.0817 1.7173 0.1505  0.1814  0.0872  121 TYR A CE1 
370  C CE2 . TYR A 46  ? 0.8853 0.6830 1.3368 0.1331  0.2051  0.0995  121 TYR A CE2 
371  C CZ  . TYR A 46  ? 0.9580 0.8103 1.4567 0.1628  0.1920  0.1065  121 TYR A CZ  
372  O OH  . TYR A 46  ? 1.0413 0.8649 1.5164 0.2035  0.1922  0.1295  121 TYR A OH  
373  N N   . GLY A 47  ? 1.1456 1.0076 1.5238 0.0558  0.1368  0.0426  122 GLY A N   
374  C CA  . GLY A 47  ? 1.0906 0.8768 1.3714 0.0630  0.1349  0.0592  122 GLY A CA  
375  C C   . GLY A 47  ? 1.1081 0.8525 1.3558 0.1073  0.1347  0.0922  122 GLY A C   
376  O O   . GLY A 47  ? 1.1071 0.8934 1.3799 0.1435  0.1138  0.1053  122 GLY A O   
377  N N   . GLU A 48  ? 0.8209 0.4842 1.0161 0.1036  0.1607  0.1024  123 GLU A N   
378  C CA  A GLU A 48  ? 0.8523 0.4602 1.0098 0.1378  0.1696  0.1285  123 GLU A CA  
379  C CA  B GLU A 48  ? 0.8546 0.4610 1.0102 0.1376  0.1696  0.1287  123 GLU A CA  
380  C C   . GLU A 48  ? 0.7756 0.3380 0.9388 0.1223  0.2063  0.1236  123 GLU A C   
381  O O   . GLU A 48  ? 0.8539 0.4063 1.0176 0.0881  0.2227  0.1051  123 GLU A O   
382  C CB  A GLU A 48  ? 0.9431 0.4871 0.9991 0.1525  0.1589  0.1469  123 GLU A CB  
383  C CB  B GLU A 48  ? 0.9465 0.4858 0.9989 0.1506  0.1606  0.1465  123 GLU A CB  
384  C CG  A GLU A 48  ? 1.0722 0.6614 1.1118 0.1835  0.1175  0.1584  123 GLU A CG  
385  C CG  B GLU A 48  ? 1.0429 0.6223 1.0665 0.1640  0.1213  0.1499  123 GLU A CG  
386  C CD  A GLU A 48  ? 1.1218 0.6385 1.0462 0.1986  0.1093  0.1792  123 GLU A CD  
387  C CD  B GLU A 48  ? 1.0204 0.6063 1.0170 0.1209  0.1181  0.1259  123 GLU A CD  
388  O OE1 A GLU A 48  ? 1.1739 0.6185 1.0370 0.1675  0.1352  0.1742  123 GLU A OE1 
389  O OE1 B GLU A 48  ? 1.0276 0.5447 0.9719 0.0934  0.1455  0.1211  123 GLU A OE1 
390  O OE2 A GLU A 48  ? 1.2097 0.7414 1.1038 0.2439  0.0787  0.2013  123 GLU A OE2 
391  O OE2 B GLU A 48  ? 1.0193 0.6825 1.0507 0.1125  0.0901  0.1082  123 GLU A OE2 
392  N N   . VAL A 49  ? 0.7698 0.3314 0.9318 0.1430  0.2103  0.1326  124 VAL A N   
393  C CA  . VAL A 49  ? 0.7284 0.3065 0.8792 0.1205  0.2223  0.1155  124 VAL A CA  
394  C C   . VAL A 49  ? 0.7794 0.3140 0.8662 0.1292  0.2234  0.1217  124 VAL A C   
395  O O   . VAL A 49  ? 0.8455 0.3719 0.9259 0.1591  0.2156  0.1373  124 VAL A O   
396  C CB  . VAL A 49  ? 0.6708 0.3072 0.8810 0.1251  0.2261  0.1119  124 VAL A CB  
397  C CG1 . VAL A 49  ? 0.6897 0.3406 0.8855 0.1065  0.2379  0.0977  124 VAL A CG1 
398  C CG2 . VAL A 49  ? 0.6341 0.3078 0.9128 0.1173  0.2296  0.1069  124 VAL A CG2 
399  N N   . PHE A 50  ? 0.7878 0.2976 0.8332 0.1035  0.2357  0.1076  125 PHE A N   
400  C CA  . PHE A 50  ? 0.8425 0.3060 0.8312 0.1044  0.2452  0.1091  125 PHE A CA  
401  C C   . PHE A 50  ? 0.8038 0.2916 0.8049 0.0895  0.2600  0.0904  125 PHE A C   
402  O O   . PHE A 50  ? 0.7673 0.2907 0.7951 0.0698  0.2661  0.0734  125 PHE A O   
403  C CB  . PHE A 50  ? 0.9082 0.3178 0.8366 0.0860  0.2545  0.1069  125 PHE A CB  
404  C CG  . PHE A 50  ? 1.0085 0.3797 0.9053 0.1024  0.2420  0.1287  125 PHE A CG  
405  C CD1 . PHE A 50  ? 1.1115 0.4303 0.9530 0.1342  0.2359  0.1550  125 PHE A CD1 
406  C CD2 . PHE A 50  ? 0.9365 0.3204 0.8539 0.0888  0.2377  0.1240  125 PHE A CD2 
407  C CE1 . PHE A 50  ? 1.2565 0.5389 1.0562 0.1584  0.2212  0.1802  125 PHE A CE1 
408  C CE2 . PHE A 50  ? 1.0628 0.4036 0.9419 0.1060  0.2277  0.1457  125 PHE A CE2 
409  C CZ  . PHE A 50  ? 1.1977 0.4889 1.0126 0.1449  0.2168  0.1764  125 PHE A CZ  
410  N N   . LYS A 51  ? 0.9092 0.3745 0.8893 0.1016  0.2672  0.0944  126 LYS A N   
411  C CA  . LYS A 51  ? 0.8817 0.3492 0.8573 0.0857  0.2869  0.0763  126 LYS A CA  
412  C C   . LYS A 51  ? 0.9321 0.3551 0.8606 0.0620  0.3064  0.0638  126 LYS A C   
413  O O   . LYS A 51  ? 1.1607 0.5263 1.0383 0.0678  0.3125  0.0747  126 LYS A O   
414  C CB  . LYS A 51  ? 0.8883 0.3405 0.8561 0.1044  0.2926  0.0829  126 LYS A CB  
415  C CG  . LYS A 51  ? 0.9306 0.3802 0.8936 0.0881  0.3154  0.0634  126 LYS A CG  
416  C CD  . LYS A 51  ? 1.0802 0.5210 1.0429 0.1068  0.3211  0.0691  126 LYS A CD  
417  C CE  . LYS A 51  ? 1.2795 0.6579 1.1960 0.1227  0.3288  0.0822  126 LYS A CE  
418  N NZ  . LYS A 51  ? 1.3264 0.6942 1.2436 0.1417  0.3371  0.0864  126 LYS A NZ  
419  N N   . VAL A 52  ? 0.8763 0.3241 0.8204 0.0366  0.3184  0.0415  127 VAL A N   
420  C CA  . VAL A 52  ? 0.8807 0.2959 0.7881 0.0102  0.3396  0.0252  127 VAL A CA  
421  C C   . VAL A 52  ? 0.9562 0.3820 0.8732 -0.0106 0.3640  -0.0007 127 VAL A C   
422  O O   . VAL A 52  ? 0.9534 0.4209 0.9117 -0.0069 0.3608  -0.0074 127 VAL A O   
423  C CB  . VAL A 52  ? 0.9591 0.3944 0.8772 -0.0041 0.3330  0.0192  127 VAL A CB  
424  C CG1 . VAL A 52  ? 0.8727 0.2900 0.7776 0.0125  0.3119  0.0426  127 VAL A CG1 
425  C CG2 . VAL A 52  ? 0.7723 0.2730 0.7506 -0.0079 0.3276  0.0067  127 VAL A CG2 
426  N N   . ARG A 53  ? 1.0094 0.3937 0.8857 -0.0336 0.3912  -0.0160 128 ARG A N   
427  C CA  . ARG A 53  ? 1.0292 0.4278 0.9183 -0.0631 0.4182  -0.0483 128 ARG A CA  
428  C C   . ARG A 53  ? 1.0867 0.4963 0.9745 -0.0881 0.4289  -0.0661 128 ARG A C   
429  O O   . ARG A 53  ? 1.0668 0.4322 0.9068 -0.0933 0.4364  -0.0595 128 ARG A O   
430  C CB  . ARG A 53  ? 1.1926 0.5375 1.0397 -0.0757 0.4491  -0.0581 128 ARG A CB  
431  C CG  . ARG A 53  ? 1.5025 0.8286 1.3449 -0.0512 0.4434  -0.0420 128 ARG A CG  
432  C CD  . ARG A 53  ? 1.4901 0.7822 1.3117 -0.0731 0.4790  -0.0644 128 ARG A CD  
433  N NE  . ARG A 53  ? 1.4516 0.7897 1.3198 -0.0818 0.4785  -0.0850 128 ARG A NE  
434  C CZ  . ARG A 53  ? 1.4664 0.8046 1.3399 -0.1150 0.5067  -0.1194 128 ARG A CZ  
435  N NH1 . ARG A 53  ? 1.5034 0.8015 1.3412 -0.1451 0.5421  -0.1378 128 ARG A NH1 
436  N NH2 . ARG A 53  ? 1.2166 0.5971 1.1323 -0.1192 0.4997  -0.1385 128 ARG A NH2 
437  N N   . SER A 54  ? 0.8779 0.3439 0.8168 -0.1019 0.4309  -0.0885 129 SER A N   
438  C CA  . SER A 54  ? 0.9398 0.4234 0.8847 -0.1252 0.4438  -0.1093 129 SER A CA  
439  C C   . SER A 54  ? 1.1258 0.5722 1.0303 -0.1562 0.4810  -0.1327 129 SER A C   
440  O O   . SER A 54  ? 1.1496 0.5890 1.0540 -0.1713 0.5021  -0.1501 129 SER A O   
441  C CB  . SER A 54  ? 0.9911 0.5434 1.0050 -0.1323 0.4423  -0.1314 129 SER A CB  
442  O OG  . SER A 54  ? 1.3238 0.8971 1.3485 -0.1569 0.4607  -0.1579 129 SER A OG  
443  N N   . LYS A 55  ? 1.2861 0.7841 1.0336 -0.3292 0.3569  -0.1961 130 LYS A N   
444  C CA  . LYS A 55  ? 1.1039 0.5697 0.8236 -0.3577 0.3957  -0.2135 130 LYS A CA  
445  C C   . LYS A 55  ? 1.0712 0.6224 0.8642 -0.3906 0.3865  -0.2372 130 LYS A C   
446  O O   . LYS A 55  ? 1.2565 0.7941 1.0405 -0.4158 0.4172  -0.2547 130 LYS A O   
447  C CB  . LYS A 55  ? 1.1517 0.5545 0.8241 -0.3382 0.4223  -0.1995 130 LYS A CB  
448  C CG  . LYS A 55  ? 1.3228 0.6346 0.9106 -0.3040 0.4354  -0.1759 130 LYS A CG  
449  C CD  . LYS A 55  ? 1.4374 0.6865 0.9708 -0.2843 0.4615  -0.1622 130 LYS A CD  
450  C CE  . LYS A 55  ? 1.5761 0.7398 1.0231 -0.2453 0.4701  -0.1365 130 LYS A CE  
451  N NZ  . LYS A 55  ? 1.4543 0.5623 0.8464 -0.2207 0.4887  -0.1203 130 LYS A NZ  
452  N N   . GLU A 56  ? 0.9863 0.6246 0.8493 -0.3889 0.3453  -0.2377 131 GLU A N   
453  C CA  . GLU A 56  ? 1.0193 0.7479 0.9541 -0.4136 0.3292  -0.2568 131 GLU A CA  
454  C C   . GLU A 56  ? 1.1031 0.8691 1.0514 -0.4371 0.3149  -0.2748 131 GLU A C   
455  O O   . GLU A 56  ? 1.3383 1.1328 1.3037 -0.4706 0.3263  -0.2995 131 GLU A O   
456  C CB  . GLU A 56  ? 0.9975 0.8004 0.9991 -0.3905 0.2930  -0.2418 131 GLU A CB  
457  C CG  . GLU A 56  ? 1.2141 1.1190 1.2905 -0.4058 0.2659  -0.2555 131 GLU A CG  
458  C CD  . GLU A 56  ? 1.3481 1.2994 1.4450 -0.3998 0.2302  -0.2541 131 GLU A CD  
459  O OE1 . GLU A 56  ? 1.4144 1.3477 1.4970 -0.3732 0.2147  -0.2353 131 GLU A OE1 
460  O OE2 . GLU A 56  ? 1.1042 1.1086 1.2292 -0.4222 0.2186  -0.2731 131 GLU A OE2 
461  N N   . ASP A 57  ? 0.9805 0.7471 0.9206 -0.4210 0.2906  -0.2643 132 ASP A N   
462  C CA  . ASP A 57  ? 1.0897 0.8864 1.0359 -0.4412 0.2760  -0.2803 132 ASP A CA  
463  C C   . ASP A 57  ? 1.0405 0.7545 0.9129 -0.4414 0.2949  -0.2783 132 ASP A C   
464  O O   . ASP A 57  ? 1.0496 0.7772 0.9170 -0.4592 0.2862  -0.2918 132 ASP A O   
465  C CB  . ASP A 57  ? 1.1182 0.9977 1.1225 -0.4243 0.2284  -0.2730 132 ASP A CB  
466  C CG  . ASP A 57  ? 1.2129 1.0676 1.2039 -0.3870 0.2128  -0.2477 132 ASP A CG  
467  O OD1 . ASP A 57  ? 1.3230 1.0960 1.2550 -0.3745 0.2336  -0.2372 132 ASP A OD1 
468  O OD2 . ASP A 57  ? 1.1021 1.0202 1.1411 -0.3688 0.1801  -0.2384 132 ASP A OD2 
469  N N   . GLY A 58  ? 1.0574 0.6859 0.8701 -0.4195 0.3192  -0.2606 133 GLY A N   
470  C CA  . GLY A 58  ? 1.2221 0.7694 0.9625 -0.4107 0.3359  -0.2532 133 GLY A CA  
471  C C   . GLY A 58  ? 1.1878 0.7511 0.9358 -0.3904 0.3040  -0.2434 133 GLY A C   
472  O O   . GLY A 58  ? 1.2867 0.7810 0.9747 -0.3779 0.3173  -0.2349 133 GLY A O   
473  N N   . ARG A 59  ? 1.2197 0.8684 1.0349 -0.3856 0.2646  -0.2441 134 ARG A N   
474  C CA  . ARG A 59  ? 1.0990 0.7614 0.9197 -0.3651 0.2361  -0.2355 134 ARG A CA  
475  C C   . ARG A 59  ? 0.9467 0.5552 0.7371 -0.3252 0.2388  -0.2115 134 ARG A C   
476  O O   . ARG A 59  ? 1.1506 0.7333 0.9329 -0.3101 0.2520  -0.1993 134 ARG A O   
477  C CB  . ARG A 59  ? 0.9892 0.7521 0.8842 -0.3639 0.1958  -0.2387 134 ARG A CB  
478  C CG  . ARG A 59  ? 1.1350 0.9601 1.0618 -0.3963 0.1843  -0.2617 134 ARG A CG  
479  C CD  . ARG A 59  ? 1.2471 1.1512 1.2227 -0.3849 0.1422  -0.2607 134 ARG A CD  
480  N NE  . ARG A 59  ? 1.5191 1.5055 1.5461 -0.4048 0.1245  -0.2769 134 ARG A NE  
481  C CZ  . ARG A 59  ? 1.3102 1.3557 1.3908 -0.3999 0.1158  -0.2738 134 ARG A CZ  
482  N NH1 . ARG A 59  ? 0.9704 1.0007 1.0593 -0.3790 0.1240  -0.2558 134 ARG A NH1 
483  N NH2 . ARG A 59  ? 1.2219 1.3428 1.3473 -0.4153 0.0985  -0.2891 134 ARG A NH2 
484  N N   . LEU A 60  ? 1.0474 0.6388 0.8194 -0.3070 0.2263  -0.2054 135 LEU A N   
485  C CA  . LEU A 60  ? 1.0098 0.5530 0.7532 -0.2667 0.2275  -0.1851 135 LEU A CA  
486  C C   . LEU A 60  ? 0.9671 0.5731 0.7671 -0.2475 0.1955  -0.1787 135 LEU A C   
487  O O   . LEU A 60  ? 1.0319 0.6926 0.8656 -0.2551 0.1712  -0.1870 135 LEU A O   
488  C CB  . LEU A 60  ? 1.1094 0.5953 0.7983 -0.2553 0.2365  -0.1829 135 LEU A CB  
489  C CG  . LEU A 60  ? 1.2098 0.6046 0.8239 -0.2492 0.2738  -0.1752 135 LEU A CG  
490  C CD1 . LEU A 60  ? 1.1008 0.4500 0.6663 -0.2502 0.2845  -0.1778 135 LEU A CD1 
491  C CD2 . LEU A 60  ? 1.0876 0.4434 0.6799 -0.2047 0.2782  -0.1523 135 LEU A CD2 
492  N N   . TYR A 61  ? 0.8114 0.4083 0.6182 -0.2229 0.1966  -0.1641 136 TYR A N   
493  C CA  . TYR A 61  ? 0.7085 0.3550 0.5625 -0.2032 0.1720  -0.1573 136 TYR A CA  
494  C C   . TYR A 61  ? 0.7570 0.3513 0.5783 -0.1606 0.1779  -0.1412 136 TYR A C   
495  O O   . TYR A 61  ? 0.8663 0.3924 0.6309 -0.1443 0.1987  -0.1324 136 TYR A O   
496  C CB  . TYR A 61  ? 0.7213 0.4288 0.6305 -0.2158 0.1636  -0.1569 136 TYR A CB  
497  C CG  . TYR A 61  ? 0.8206 0.5923 0.7686 -0.2484 0.1545  -0.1717 136 TYR A CG  
498  C CD1 . TYR A 61  ? 0.8246 0.6697 0.8180 -0.2517 0.1258  -0.1771 136 TYR A CD1 
499  C CD2 . TYR A 61  ? 0.6839 0.4429 0.6207 -0.2724 0.1747  -0.1807 136 TYR A CD2 
500  C CE1 . TYR A 61  ? 0.9251 0.8301 0.9515 -0.2743 0.1145  -0.1896 136 TYR A CE1 
501  C CE2 . TYR A 61  ? 0.8763 0.6975 0.8511 -0.2990 0.1654  -0.1962 136 TYR A CE2 
502  C CZ  . TYR A 61  ? 0.7942 0.6890 0.8139 -0.2981 0.1337  -0.1999 136 TYR A CZ  
503  O OH  . TYR A 61  ? 0.9013 0.8583 0.9565 -0.3195 0.1221  -0.2145 136 TYR A OH  
504  N N   . ALA A 62  ? 0.8070 0.4551 0.6698 -0.1348 0.1550  -0.1314 137 ALA A N   
505  C CA  . ALA A 62  ? 0.6331 0.2694 0.4850 -0.0887 0.1513  -0.1132 137 ALA A CA  
506  C C   . ALA A 62  ? 0.6063 0.2952 0.5029 -0.0823 0.1383  -0.1036 137 ALA A C   
507  O O   . ALA A 62  ? 0.7292 0.4897 0.6805 -0.0938 0.1201  -0.1053 137 ALA A O   
508  C CB  . ALA A 62  ? 0.6903 0.3535 0.5533 -0.0611 0.1363  -0.1092 137 ALA A CB  
509  N N   . VAL A 63  ? 0.6156 0.2643 0.4833 -0.0620 0.1483  -0.0930 138 VAL A N   
510  C CA  . VAL A 63  ? 0.5615 0.2473 0.4608 -0.0567 0.1395  -0.0842 138 VAL A CA  
511  C C   . VAL A 63  ? 0.6727 0.3659 0.5661 -0.0118 0.1265  -0.0710 138 VAL A C   
512  O O   . VAL A 63  ? 0.8337 0.4702 0.6751 0.0167  0.1353  -0.0655 138 VAL A O   
513  C CB  . VAL A 63  ? 0.7176 0.3512 0.5871 -0.0765 0.1635  -0.0856 138 VAL A CB  
514  C CG1 . VAL A 63  ? 0.6687 0.3323 0.5628 -0.0669 0.1560  -0.0752 138 VAL A CG1 
515  C CG2 . VAL A 63  ? 0.8194 0.4634 0.7082 -0.1252 0.1751  -0.1031 138 VAL A CG2 
516  N N   . LYS A 64  ? 0.7297 0.4931 0.6747 -0.0052 0.1062  -0.0669 139 LYS A N   
517  C CA  . LYS A 64  ? 0.6194 0.4054 0.5696 0.0305  0.0918  -0.0585 139 LYS A CA  
518  C C   . LYS A 64  ? 0.6337 0.4280 0.5904 0.0294  0.0900  -0.0520 139 LYS A C   
519  O O   . LYS A 64  ? 0.7311 0.5581 0.7233 0.0036  0.0899  -0.0536 139 LYS A O   
520  C CB  . LYS A 64  ? 0.4376 0.2928 0.4376 0.0364  0.0741  -0.0617 139 LYS A CB  
521  C CG  . LYS A 64  ? 0.6377 0.5341 0.6584 0.0623  0.0591  -0.0579 139 LYS A CG  
522  C CD  . LYS A 64  ? 0.5928 0.5440 0.6528 0.0694  0.0488  -0.0638 139 LYS A CD  
523  C CE  . LYS A 64  ? 0.6548 0.6415 0.7512 0.0410  0.0479  -0.0674 139 LYS A CE  
524  N NZ  . LYS A 64  ? 0.6607 0.6878 0.7858 0.0471  0.0433  -0.0734 139 LYS A NZ  
525  N N   . ARG A 65  ? 0.6766 0.4403 0.5961 0.0597  0.0885  -0.0445 140 ARG A N   
526  C CA  . ARG A 65  ? 0.6053 0.3723 0.5230 0.0623  0.0858  -0.0384 140 ARG A CA  
527  C C   . ARG A 65  ? 0.6014 0.4070 0.5273 0.0959  0.0639  -0.0362 140 ARG A C   
528  O O   . ARG A 65  ? 0.9063 0.7136 0.8199 0.1255  0.0556  -0.0371 140 ARG A O   
529  C CB  . ARG A 65  ? 0.7725 0.4549 0.6251 0.0633  0.1076  -0.0329 140 ARG A CB  
530  C CG  . ARG A 65  ? 0.9529 0.5761 0.7389 0.1050  0.1091  -0.0264 140 ARG A CG  
531  C CD  . ARG A 65  ? 0.8591 0.3860 0.5717 0.1036  0.1364  -0.0207 140 ARG A CD  
532  N NE  . ARG A 65  ? 1.2121 0.6771 0.8516 0.1493  0.1380  -0.0121 140 ARG A NE  
533  C CZ  . ARG A 65  ? 1.2261 0.6235 0.7989 0.1480  0.1588  -0.0032 140 ARG A CZ  
534  N NH1 . ARG A 65  ? 1.3882 0.7531 0.9514 0.1075  0.1854  -0.0055 140 ARG A NH1 
535  N NH2 . ARG A 65  ? 1.2754 0.6413 0.7899 0.1889  0.1541  0.0074  140 ARG A NH2 
536  N N   . SER A 66  ? 0.7365 0.5759 0.6850 0.0904  0.0554  -0.0348 141 SER A N   
537  C CA  . SER A 66  ? 0.7753 0.6575 0.7346 0.1158  0.0343  -0.0366 141 SER A CA  
538  C C   . SER A 66  ? 0.6658 0.4985 0.5621 0.1506  0.0308  -0.0301 141 SER A C   
539  O O   . SER A 66  ? 0.7822 0.5427 0.6255 0.1490  0.0483  -0.0224 141 SER A O   
540  C CB  . SER A 66  ? 0.7353 0.6627 0.7328 0.0954  0.0295  -0.0385 141 SER A CB  
541  O OG  . SER A 66  ? 0.6606 0.5469 0.6368 0.0773  0.0452  -0.0317 141 SER A OG  
542  N N   . MET A 67  ? 0.8167 0.6895 0.7179 0.1831  0.0087  -0.0343 142 MET A N   
543  C CA  . MET A 67  ? 0.7779 0.6096 0.6164 0.2259  0.0005  -0.0283 142 MET A CA  
544  C C   . MET A 67  ? 1.0444 0.8425 0.8440 0.2242  0.0011  -0.0223 142 MET A C   
545  O O   . MET A 67  ? 1.2061 0.9201 0.9349 0.2364  0.0164  -0.0119 142 MET A O   
546  C CB  . MET A 67  ? 1.1233 1.0244 0.9882 0.2608  -0.0266 -0.0374 142 MET A CB  
547  C CG  . MET A 67  ? 1.2664 1.1382 1.0688 0.3129  -0.0411 -0.0319 142 MET A CG  
548  S SD  . MET A 67  ? 1.7757 1.5515 1.5019 0.3488  -0.0212 -0.0188 142 MET A SD  
549  C CE  . MET A 67  ? 1.2551 1.1015 1.0472 0.3493  -0.0258 -0.0292 142 MET A CE  
550  N N   . SER A 68  ? 0.8768 0.7326 0.7162 0.2083  -0.0122 -0.0293 143 SER A N   
551  C CA  . SER A 68  ? 0.8915 0.7216 0.6949 0.2078  -0.0139 -0.0254 143 SER A CA  
552  C C   . SER A 68  ? 0.8219 0.6536 0.6561 0.1628  0.0042  -0.0245 143 SER A C   
553  O O   . SER A 68  ? 0.8205 0.6976 0.7148 0.1356  0.0090  -0.0297 143 SER A O   
554  C CB  . SER A 68  ? 1.0708 0.9657 0.8872 0.2294  -0.0455 -0.0362 143 SER A CB  
555  O OG  . SER A 68  ? 1.2623 1.2430 1.1566 0.2057  -0.0538 -0.0504 143 SER A OG  
556  N N   . PRO A 69  ? 0.9427 0.7230 0.7335 0.1567  0.0158  -0.0174 144 PRO A N   
557  C CA  . PRO A 69  ? 0.7644 0.5506 0.5858 0.1183  0.0333  -0.0165 144 PRO A CA  
558  C C   . PRO A 69  ? 0.8519 0.7162 0.7301 0.1044  0.0182  -0.0270 144 PRO A C   
559  O O   . PRO A 69  ? 0.9359 0.8487 0.8255 0.1217  -0.0062 -0.0371 144 PRO A O   
560  C CB  . PRO A 69  ? 0.7620 0.4764 0.5158 0.1235  0.0458  -0.0080 144 PRO A CB  
561  C CG  . PRO A 69  ? 0.8745 0.5222 0.5578 0.1572  0.0469  -0.0013 144 PRO A CG  
562  C CD  . PRO A 69  ? 0.8860 0.5883 0.5907 0.1862  0.0187  -0.0083 144 PRO A CD  
563  N N   . PHE A 70  ? 0.9427 0.8188 0.8565 0.0724  0.0353  -0.0258 145 PHE A N   
564  C CA  . PHE A 70  ? 0.5924 0.5311 0.5563 0.0558  0.0290  -0.0348 145 PHE A CA  
565  C C   . PHE A 70  ? 0.7378 0.6894 0.6800 0.0634  0.0137  -0.0426 145 PHE A C   
566  O O   . PHE A 70  ? 0.7123 0.6179 0.6085 0.0646  0.0201  -0.0370 145 PHE A O   
567  C CB  . PHE A 70  ? 0.6157 0.5514 0.6076 0.0267  0.0527  -0.0290 145 PHE A CB  
568  C CG  . PHE A 70  ? 0.6402 0.5839 0.6650 0.0162  0.0627  -0.0260 145 PHE A CG  
569  C CD1 . PHE A 70  ? 0.5298 0.5093 0.5817 0.0227  0.0503  -0.0324 145 PHE A CD1 
570  C CD2 . PHE A 70  ? 0.5324 0.4501 0.5612 -0.0008 0.0847  -0.0184 145 PHE A CD2 
571  C CE1 . PHE A 70  ? 0.4077 0.3925 0.4841 0.0124  0.0580  -0.0308 145 PHE A CE1 
572  C CE2 . PHE A 70  ? 0.5367 0.4685 0.5963 -0.0118 0.0908  -0.0186 145 PHE A CE2 
573  C CZ  . PHE A 70  ? 0.5271 0.4901 0.6074 -0.0052 0.0766  -0.0246 145 PHE A CZ  
574  N N   . ARG A 71  ? 0.7640 0.7793 0.7393 0.0666  -0.0056 -0.0576 146 ARG A N   
575  C CA  . ARG A 71  ? 0.6885 0.7300 0.6518 0.0683  -0.0218 -0.0705 146 ARG A CA  
576  C C   . ARG A 71  ? 0.8102 0.8432 0.7777 0.0380  -0.0033 -0.0710 146 ARG A C   
577  O O   . ARG A 71  ? 0.8097 0.8292 0.7423 0.0368  -0.0085 -0.0759 146 ARG A O   
578  C CB  . ARG A 71  ? 0.8262 0.9453 0.8334 0.0742  -0.0430 -0.0900 146 ARG A CB  
579  C CG  . ARG A 71  ? 0.8725 1.0353 0.8795 0.0692  -0.0605 -0.1098 146 ARG A CG  
580  C CD  . ARG A 71  ? 1.0454 1.2920 1.1060 0.0714  -0.0774 -0.1319 146 ARG A CD  
581  N NE  . ARG A 71  ? 1.1823 1.4516 1.2953 0.0461  -0.0567 -0.1346 146 ARG A NE  
582  C CZ  . ARG A 71  ? 1.1006 1.3973 1.2425 0.0137  -0.0428 -0.1486 146 ARG A CZ  
583  N NH1 . ARG A 71  ? 0.8869 1.1957 1.0153 -0.0019 -0.0468 -0.1632 146 ARG A NH1 
584  N NH2 . ARG A 71  ? 0.6920 0.9988 0.8713 -0.0033 -0.0229 -0.1484 146 ARG A NH2 
585  N N   . GLY A 72  ? 0.6230 0.6603 0.6275 0.0158  0.0186  -0.0658 147 GLY A N   
586  C CA  . GLY A 72  ? 0.4985 0.5243 0.5059 -0.0088 0.0397  -0.0644 147 GLY A CA  
587  C C   . GLY A 72  ? 0.5495 0.5858 0.5986 -0.0238 0.0601  -0.0575 147 GLY A C   
588  O O   . GLY A 72  ? 0.5468 0.5941 0.6191 -0.0172 0.0577  -0.0531 147 GLY A O   
589  N N   . PRO A 73  ? 0.5195 0.5494 0.5738 -0.0425 0.0807  -0.0563 148 PRO A N   
590  C CA  . PRO A 73  ? 0.3685 0.4074 0.4568 -0.0512 0.0993  -0.0485 148 PRO A CA  
591  C C   . PRO A 73  ? 0.3970 0.4801 0.5207 -0.0519 0.0917  -0.0585 148 PRO A C   
592  O O   . PRO A 73  ? 0.4609 0.5522 0.6079 -0.0484 0.0948  -0.0512 148 PRO A O   
593  C CB  . PRO A 73  ? 0.4316 0.4496 0.5068 -0.0664 0.1230  -0.0468 148 PRO A CB  
594  C CG  . PRO A 73  ? 0.3755 0.3593 0.4069 -0.0660 0.1206  -0.0476 148 PRO A CG  
595  C CD  . PRO A 73  ? 0.4605 0.4659 0.4821 -0.0537 0.0901  -0.0599 148 PRO A CD  
596  N N   . LYS A 74  ? 0.5519 0.6650 0.6805 -0.0579 0.0827  -0.0767 149 LYS A N   
597  C CA  . LYS A 74  ? 0.5019 0.6554 0.6641 -0.0597 0.0790  -0.0879 149 LYS A CA  
598  C C   . LYS A 74  ? 0.4208 0.5893 0.5953 -0.0403 0.0596  -0.0856 149 LYS A C   
599  O O   . LYS A 74  ? 0.4801 0.6607 0.6774 -0.0385 0.0629  -0.0835 149 LYS A O   
600  C CB  . LYS A 74  ? 0.5894 0.7772 0.7582 -0.0730 0.0748  -0.1117 149 LYS A CB  
601  C CG  . LYS A 74  ? 0.7331 0.9015 0.8875 -0.0970 0.0999  -0.1171 149 LYS A CG  
602  C CD  . LYS A 74  ? 1.1308 1.3252 1.2920 -0.1125 0.1001  -0.1403 149 LYS A CD  
603  C CE  . LYS A 74  ? 0.7953 1.0398 0.9655 -0.1205 0.0802  -0.1664 149 LYS A CE  
604  N NZ  . LYS A 74  ? 0.6705 0.9627 0.8663 -0.0975 0.0497  -0.1727 149 LYS A NZ  
605  N N   . ASP A 75  ? 0.5199 0.6814 0.6726 -0.0239 0.0408  -0.0856 150 ASP A N   
606  C CA  . ASP A 75  ? 0.4338 0.5981 0.5887 -0.0032 0.0262  -0.0822 150 ASP A CA  
607  C C   . ASP A 75  ? 0.4465 0.5779 0.6000 -0.0036 0.0382  -0.0654 150 ASP A C   
608  O O   . ASP A 75  ? 0.5873 0.7266 0.7556 0.0028  0.0352  -0.0645 150 ASP A O   
609  C CB  . ASP A 75  ? 0.6282 0.7805 0.7482 0.0185  0.0066  -0.0834 150 ASP A CB  
610  C CG  . ASP A 75  ? 0.6894 0.8355 0.8027 0.0435  -0.0051 -0.0792 150 ASP A CG  
611  O OD1 . ASP A 75  ? 0.9826 1.1708 1.1247 0.0517  -0.0146 -0.0899 150 ASP A OD1 
612  O OD2 . ASP A 75  ? 0.7841 0.8790 0.8608 0.0542  -0.0016 -0.0659 150 ASP A OD2 
613  N N   . ARG A 76  ? 0.4329 0.5293 0.5698 -0.0123 0.0527  -0.0538 151 ARG A N   
614  C CA  . ARG A 76  ? 0.3309 0.4063 0.4735 -0.0161 0.0645  -0.0415 151 ARG A CA  
615  C C   . ARG A 76  ? 0.3817 0.4844 0.5591 -0.0247 0.0718  -0.0414 151 ARG A C   
616  O O   . ARG A 76  ? 0.4720 0.5784 0.6616 -0.0228 0.0697  -0.0390 151 ARG A O   
617  C CB  . ARG A 76  ? 0.4498 0.4894 0.5732 -0.0240 0.0809  -0.0313 151 ARG A CB  
618  C CG  . ARG A 76  ? 0.4202 0.4515 0.5602 -0.0315 0.0946  -0.0220 151 ARG A CG  
619  C CD  . ARG A 76  ? 0.4895 0.4885 0.6142 -0.0389 0.1136  -0.0135 151 ARG A CD  
620  N NE  . ARG A 76  ? 0.6245 0.6252 0.7717 -0.0473 0.1263  -0.0081 151 ARG A NE  
621  C CZ  . ARG A 76  ? 0.5109 0.5325 0.6735 -0.0470 0.1239  -0.0046 151 ARG A CZ  
622  N NH1 . ARG A 76  ? 0.5892 0.6221 0.7486 -0.0423 0.1196  -0.0034 151 ARG A NH1 
623  N NH2 . ARG A 76  ? 0.6685 0.6967 0.8419 -0.0500 0.1236  -0.0034 151 ARG A NH2 
624  N N   . ALA A 77  ? 0.4175 0.5340 0.6049 -0.0340 0.0819  -0.0444 152 ALA A N   
625  C CA  . ALA A 77  ? 0.2995 0.4175 0.4843 -0.0336 0.0799  -0.0382 152 ALA A CA  
626  C C   . ALA A 77  ? 0.3873 0.5241 0.5808 -0.0286 0.0689  -0.0457 152 ALA A C   
627  O O   . ALA A 77  ? 0.4395 0.5740 0.6305 -0.0257 0.0663  -0.0399 152 ALA A O   
628  C CB  . ALA A 77  ? 0.3708 0.4782 0.5396 -0.0392 0.0888  -0.0372 152 ALA A CB  
629  N N   . ARG A 78  ? 0.3526 0.5113 0.5567 -0.0264 0.0623  -0.0601 153 ARG A N   
630  C CA  . ARG A 78  ? 0.3440 0.5185 0.5550 -0.0198 0.0529  -0.0667 153 ARG A CA  
631  C C   . ARG A 78  ? 0.4038 0.5757 0.6222 -0.0102 0.0474  -0.0636 153 ARG A C   
632  O O   . ARG A 78  ? 0.4073 0.5763 0.6236 -0.0086 0.0460  -0.0614 153 ARG A O   
633  C CB  . ARG A 78  ? 0.3755 0.5813 0.5976 -0.0164 0.0438  -0.0841 153 ARG A CB  
634  C CG  . ARG A 78  ? 0.5327 0.7535 0.7608 -0.0111 0.0377  -0.0911 153 ARG A CG  
635  C CD  . ARG A 78  ? 0.5879 0.8463 0.8283 -0.0069 0.0267  -0.1093 153 ARG A CD  
636  N NE  . ARG A 78  ? 0.6922 0.9578 0.9302 -0.0241 0.0335  -0.1194 153 ARG A NE  
637  C CZ  . ARG A 78  ? 0.6813 0.9659 0.9211 -0.0263 0.0275  -0.1290 153 ARG A CZ  
638  N NH1 . ARG A 78  ? 0.6293 0.9276 0.8716 -0.0080 0.0122  -0.1293 153 ARG A NH1 
639  N NH2 . ARG A 78  ? 0.6565 0.9436 0.8911 -0.0460 0.0372  -0.1399 153 ARG A NH2 
640  N N   . LYS A 79  ? 0.3928 0.5522 0.6063 -0.0037 0.0448  -0.0616 154 LYS A N   
641  C CA  . LYS A 79  ? 0.3192 0.4570 0.5220 0.0034  0.0412  -0.0566 154 LYS A CA  
642  C C   . LYS A 79  ? 0.3023 0.4327 0.5141 -0.0095 0.0507  -0.0492 154 LYS A C   
643  O O   . LYS A 79  ? 0.5089 0.6375 0.7233 -0.0096 0.0487  -0.0502 154 LYS A O   
644  C CB  . LYS A 79  ? 0.3486 0.4515 0.5177 0.0142  0.0369  -0.0520 154 LYS A CB  
645  C CG  . LYS A 79  ? 0.3810 0.4951 0.5375 0.0340  0.0224  -0.0595 154 LYS A CG  
646  C CD  . LYS A 79  ? 0.4718 0.5402 0.5825 0.0499  0.0191  -0.0528 154 LYS A CD  
647  C CE  . LYS A 79  ? 0.6777 0.7634 0.7738 0.0755  0.0004  -0.0603 154 LYS A CE  
648  N NZ  . LYS A 79  ? 0.8105 0.8424 0.8501 0.0972  -0.0024 -0.0521 154 LYS A NZ  
649  N N   . LEU A 80  ? 0.4128 0.5411 0.6291 -0.0195 0.0606  -0.0425 155 LEU A N   
650  C CA  . LEU A 80  ? 0.3316 0.4559 0.5467 -0.0265 0.0628  -0.0342 155 LEU A CA  
651  C C   . LEU A 80  ? 0.4020 0.5365 0.6106 -0.0234 0.0568  -0.0322 155 LEU A C   
652  O O   . LEU A 80  ? 0.3846 0.5244 0.5957 -0.0254 0.0550  -0.0286 155 LEU A O   
653  C CB  . LEU A 80  ? 0.3453 0.4590 0.5521 -0.0309 0.0707  -0.0254 155 LEU A CB  
654  C CG  . LEU A 80  ? 0.5059 0.5998 0.7143 -0.0372 0.0830  -0.0243 155 LEU A CG  
655  C CD1 . LEU A 80  ? 0.6225 0.7063 0.8201 -0.0394 0.0903  -0.0157 155 LEU A CD1 
656  C CD2 . LEU A 80  ? 0.4476 0.5331 0.6617 -0.0446 0.0852  -0.0266 155 LEU A CD2 
657  N N   . ALA A 81  ? 0.5228 0.6618 0.7255 -0.0197 0.0558  -0.0359 156 ALA A N   
658  C CA  . ALA A 81  ? 0.3049 0.4471 0.5015 -0.0179 0.0565  -0.0346 156 ALA A CA  
659  C C   . ALA A 81  ? 0.3775 0.5253 0.5816 -0.0160 0.0518  -0.0391 156 ALA A C   
660  O O   . ALA A 81  ? 0.4339 0.5857 0.6372 -0.0148 0.0532  -0.0373 156 ALA A O   
661  C CB  . ALA A 81  ? 0.3242 0.4669 0.5151 -0.0183 0.0604  -0.0407 156 ALA A CB  
662  N N   . GLU A 82  ? 0.3549 0.5037 0.5683 -0.0147 0.0479  -0.0468 157 GLU A N   
663  C CA  . GLU A 82  ? 0.3093 0.4611 0.5305 -0.0140 0.0458  -0.0537 157 GLU A CA  
664  C C   . GLU A 82  ? 0.3572 0.5114 0.5838 -0.0224 0.0443  -0.0512 157 GLU A C   
665  O O   . GLU A 82  ? 0.4748 0.6364 0.7054 -0.0243 0.0423  -0.0562 157 GLU A O   
666  C CB  . GLU A 82  ? 0.3614 0.5093 0.5886 -0.0073 0.0443  -0.0625 157 GLU A CB  
667  C CG  . GLU A 82  ? 0.5622 0.6940 0.7760 -0.0055 0.0419  -0.0667 157 GLU A CG  
668  C CD  . GLU A 82  ? 0.7376 0.8489 0.9340 0.0089  0.0398  -0.0699 157 GLU A CD  
669  O OE1 . GLU A 82  ? 0.6706 0.7880 0.8680 0.0201  0.0369  -0.0698 157 GLU A OE1 
670  O OE2 . GLU A 82  ? 0.5322 0.6198 0.7102 0.0106  0.0410  -0.0727 157 GLU A OE2 
671  N N   . VAL A 83  ? 0.4201 0.5715 0.6483 -0.0285 0.0456  -0.0452 158 VAL A N   
672  C CA  . VAL A 83  ? 0.2693 0.4307 0.5046 -0.0375 0.0430  -0.0438 158 VAL A CA  
673  C C   . VAL A 83  ? 0.3004 0.4798 0.5351 -0.0308 0.0401  -0.0370 158 VAL A C   
674  O O   . VAL A 83  ? 0.4220 0.6202 0.6662 -0.0333 0.0340  -0.0414 158 VAL A O   
675  C CB  . VAL A 83  ? 0.3587 0.5126 0.5963 -0.0453 0.0485  -0.0398 158 VAL A CB  
676  C CG1 . VAL A 83  ? 0.2486 0.4199 0.4967 -0.0558 0.0454  -0.0407 158 VAL A CG1 
677  C CG2 . VAL A 83  ? 0.4279 0.5592 0.6669 -0.0512 0.0568  -0.0472 158 VAL A CG2 
678  N N   . GLY A 84  ? 0.3886 0.5639 0.6133 -0.0226 0.0456  -0.0286 159 GLY A N   
679  C CA  . GLY A 84  ? 0.3521 0.5411 0.5774 -0.0138 0.0487  -0.0233 159 GLY A CA  
680  C C   . GLY A 84  ? 0.3110 0.5030 0.5359 -0.0091 0.0493  -0.0307 159 GLY A C   
681  O O   . GLY A 84  ? 0.4767 0.6880 0.7094 -0.0013 0.0492  -0.0314 159 GLY A O   
682  N N   . SER A 85  ? 0.4214 0.5979 0.6387 -0.0115 0.0507  -0.0381 160 SER A N   
683  C CA  . SER A 85  ? 0.2943 0.4714 0.5102 -0.0079 0.0548  -0.0473 160 SER A CA  
684  C C   . SER A 85  ? 0.4447 0.6304 0.6617 -0.0109 0.0430  -0.0535 160 SER A C   
685  O O   . SER A 85  ? 0.5669 0.7482 0.7652 -0.0045 0.0410  -0.0542 160 SER A O   
686  C CB  . SER A 85  ? 0.4014 0.5635 0.6101 -0.0088 0.0580  -0.0536 160 SER A CB  
687  O OG  . SER A 85  ? 0.5194 0.6722 0.7179 -0.0090 0.0633  -0.0489 160 SER A OG  
688  N N   . HIS A 86  ? 0.5144 0.7015 0.7397 -0.0213 0.0348  -0.0571 161 HIS A N   
689  C CA  . HIS A 86  ? 0.3547 0.5438 0.5721 -0.0295 0.0231  -0.0636 161 HIS A CA  
690  C C   . HIS A 86  ? 0.5049 0.7243 0.7296 -0.0271 0.0135  -0.0606 161 HIS A C   
691  O O   . HIS A 86  ? 0.4828 0.7080 0.6934 -0.0273 0.0022  -0.0662 161 HIS A O   
692  C CB  . HIS A 86  ? 0.5412 0.7200 0.7632 -0.0441 0.0222  -0.0686 161 HIS A CB  
693  C CG  . HIS A 86  ? 0.4170 0.5623 0.6170 -0.0447 0.0252  -0.0754 161 HIS A CG  
694  N ND1 . HIS A 86  ? 0.4396 0.5699 0.6193 -0.0531 0.0208  -0.0844 161 HIS A ND1 
695  C CD2 . HIS A 86  ? 0.3710 0.4955 0.5645 -0.0359 0.0323  -0.0747 161 HIS A CD2 
696  C CE1 . HIS A 86  ? 0.5538 0.6502 0.7137 -0.0484 0.0279  -0.0876 161 HIS A CE1 
697  N NE2 . HIS A 86  ? 0.6231 0.7189 0.7929 -0.0362 0.0337  -0.0816 161 HIS A NE2 
698  N N   . GLU A 87  ? 0.5332 0.7732 0.7785 -0.0230 0.0172  -0.0523 162 GLU A N   
699  C CA  . GLU A 87  ? 0.4883 0.7637 0.7445 -0.0149 0.0081  -0.0485 162 GLU A CA  
700  C C   . GLU A 87  ? 0.5873 0.8560 0.8160 0.0065  0.0078  -0.0426 162 GLU A C   
701  O O   . GLU A 87  ? 0.5527 0.8452 0.7752 0.0162  -0.0067 -0.0433 162 GLU A O   
702  C CB  . GLU A 87  ? 0.5758 0.8600 0.8504 -0.0124 0.0166  -0.0372 162 GLU A CB  
703  C CG  . GLU A 87  ? 0.6316 0.9483 0.9164 0.0064  0.0138  -0.0291 162 GLU A CG  
704  C CD  . GLU A 87  ? 0.9322 1.2339 1.2202 0.0125  0.0294  -0.0138 162 GLU A CD  
705  O OE1 . GLU A 87  ? 0.9888 1.2614 1.2574 0.0160  0.0442  -0.0083 162 GLU A OE1 
706  O OE2 . GLU A 87  ? 0.9948 1.3151 1.3026 0.0123  0.0272  -0.0091 162 GLU A OE2 
707  N N   . LYS A 88  ? 0.5470 0.7825 0.7562 0.0140  0.0244  -0.0381 163 LYS A N   
708  C CA  . LYS A 88  ? 0.4580 0.6742 0.6327 0.0329  0.0309  -0.0328 163 LYS A CA  
709  C C   . LYS A 88  ? 0.5416 0.7420 0.6885 0.0319  0.0221  -0.0414 163 LYS A C   
710  O O   . LYS A 88  ? 0.5800 0.7743 0.6955 0.0484  0.0170  -0.0384 163 LYS A O   
711  C CB  . LYS A 88  ? 0.4443 0.6293 0.6084 0.0351  0.0561  -0.0291 163 LYS A CB  
712  C CG  . LYS A 88  ? 0.5725 0.7644 0.7540 0.0366  0.0677  -0.0205 163 LYS A CG  
713  C CD  . LYS A 88  ? 0.7211 0.8842 0.8938 0.0308  0.0919  -0.0224 163 LYS A CD  
714  C CE  . LYS A 88  ? 0.7901 0.9534 0.9712 0.0275  0.0995  -0.0156 163 LYS A CE  
715  N NZ  . LYS A 88  ? 0.8556 0.9892 1.0154 0.0155  0.1080  -0.0195 163 LYS A NZ  
716  N N   . VAL A 89  ? 0.4209 0.6101 0.5733 0.0153  0.0212  -0.0516 164 VAL A N   
717  C CA  . VAL A 89  ? 0.4403 0.6098 0.5643 0.0129  0.0152  -0.0604 164 VAL A CA  
718  C C   . VAL A 89  ? 0.5305 0.7257 0.6498 0.0104  -0.0085 -0.0655 164 VAL A C   
719  O O   . VAL A 89  ? 0.6672 0.8510 0.7513 0.0187  -0.0165 -0.0683 164 VAL A O   
720  C CB  . VAL A 89  ? 0.3517 0.5030 0.4826 -0.0013 0.0212  -0.0692 164 VAL A CB  
721  C CG1 . VAL A 89  ? 0.4705 0.5990 0.5706 -0.0051 0.0158  -0.0786 164 VAL A CG1 
722  C CG2 . VAL A 89  ? 0.4132 0.5486 0.5496 0.0029  0.0418  -0.0678 164 VAL A CG2 
723  N N   . GLY A 90  ? 0.5030 0.7340 0.6567 -0.0021 -0.0194 -0.0683 165 GLY A N   
724  C CA  . GLY A 90  ? 0.3840 0.6501 0.5421 -0.0096 -0.0419 -0.0778 165 GLY A CA  
725  C C   . GLY A 90  ? 0.4917 0.7379 0.6330 -0.0313 -0.0472 -0.0934 165 GLY A C   
726  O O   . GLY A 90  ? 0.7824 0.9911 0.9166 -0.0407 -0.0330 -0.0958 165 GLY A O   
727  N N   . GLN A 91  ? 0.6302 0.9023 0.7627 -0.0381 -0.0681 -0.1050 166 GLN A N   
728  C CA  . GLN A 91  ? 0.6110 0.8633 0.7225 -0.0621 -0.0731 -0.1224 166 GLN A CA  
729  C C   . GLN A 91  ? 0.5446 0.7615 0.6024 -0.0499 -0.0766 -0.1240 166 GLN A C   
730  O O   . GLN A 91  ? 0.6448 0.8793 0.6830 -0.0301 -0.0913 -0.1205 166 GLN A O   
731  C CB  . GLN A 91  ? 0.5167 0.8215 0.6530 -0.0849 -0.0928 -0.1396 166 GLN A CB  
732  C CG  . GLN A 91  ? 0.6068 0.9342 0.7909 -0.1042 -0.0829 -0.1417 166 GLN A CG  
733  C CD  . GLN A 91  ? 1.0477 1.4290 1.2604 -0.1290 -0.0980 -0.1602 166 GLN A CD  
734  O OE1 . GLN A 91  ? 1.4058 1.8234 1.6123 -0.1226 -0.1203 -0.1663 166 GLN A OE1 
735  N NE2 . GLN A 91  ? 1.1135 1.4783 1.3439 -0.1497 -0.0804 -0.1608 166 GLN A NE2 
736  N N   . HIS A 92  ? 0.6124 0.7761 0.6428 -0.0591 -0.0616 -0.1289 167 HIS A N   
737  C CA  . HIS A 92  ? 0.5679 0.6881 0.5449 -0.0505 -0.0589 -0.1315 167 HIS A CA  
738  C C   . HIS A 92  ? 0.6139 0.6913 0.5713 -0.0725 -0.0481 -0.1442 167 HIS A C   
739  O O   . HIS A 92  ? 0.6108 0.6750 0.5903 -0.0804 -0.0327 -0.1425 167 HIS A O   
740  C CB  . HIS A 92  ? 0.6223 0.7114 0.5859 -0.0255 -0.0385 -0.1167 167 HIS A CB  
741  C CG  . HIS A 92  ? 0.5638 0.6075 0.4702 -0.0147 -0.0329 -0.1186 167 HIS A CG  
742  N ND1 . HIS A 92  ? 0.6494 0.6435 0.5311 -0.0208 -0.0145 -0.1245 167 HIS A ND1 
743  C CD2 . HIS A 92  ? 0.5813 0.6173 0.4459 0.0043  -0.0413 -0.1150 167 HIS A CD2 
744  C CE1 . HIS A 92  ? 0.6632 0.6206 0.4923 -0.0092 -0.0104 -0.1252 167 HIS A CE1 
745  N NE2 . HIS A 92  ? 0.7395 0.7188 0.5541 0.0064  -0.0267 -0.1193 167 HIS A NE2 
746  N N   . PRO A 93  ? 0.5887 0.6397 0.4996 -0.0809 -0.0549 -0.1566 168 PRO A N   
747  C CA  . PRO A 93  ? 0.6175 0.6205 0.5033 -0.1021 -0.0415 -0.1690 168 PRO A CA  
748  C C   . PRO A 93  ? 0.7780 0.7326 0.6585 -0.0887 -0.0129 -0.1597 168 PRO A C   
749  O O   . PRO A 93  ? 0.9310 0.8489 0.8008 -0.1010 0.0016  -0.1659 168 PRO A O   
750  C CB  . PRO A 93  ? 0.5921 0.5730 0.4216 -0.1080 -0.0537 -0.1821 168 PRO A CB  
751  C CG  . PRO A 93  ? 0.6195 0.6569 0.4564 -0.0972 -0.0824 -0.1811 168 PRO A CG  
752  C CD  . PRO A 93  ? 0.5633 0.6243 0.4371 -0.0708 -0.0754 -0.1604 168 PRO A CD  
753  N N   . CYS A 94  ? 0.6842 0.6376 0.5708 -0.0636 -0.0029 -0.1462 169 CYS A N   
754  C CA  . CYS A 94  ? 0.6859 0.6063 0.5748 -0.0503 0.0229  -0.1402 169 CYS A CA  
755  C C   . CYS A 94  ? 0.5875 0.5377 0.5279 -0.0421 0.0293  -0.1298 169 CYS A C   
756  O O   . CYS A 94  ? 0.5768 0.5174 0.5288 -0.0275 0.0471  -0.1249 169 CYS A O   
757  C CB  . CYS A 94  ? 0.6389 0.5336 0.4975 -0.0325 0.0352  -0.1366 169 CYS A CB  
758  S SG  . CYS A 94  ? 0.8614 0.7075 0.6477 -0.0395 0.0315  -0.1487 169 CYS A SG  
759  N N   . CYS A 95  ? 0.5789 0.5669 0.5509 -0.0519 0.0154  -0.1281 170 CYS A N   
760  C CA  . CYS A 95  ? 0.4415 0.4538 0.4564 -0.0458 0.0205  -0.1188 170 CYS A CA  
761  C C   . CYS A 95  ? 0.4617 0.4765 0.4898 -0.0635 0.0172  -0.1232 170 CYS A C   
762  O O   . CYS A 95  ? 0.6144 0.6412 0.6382 -0.0829 0.0048  -0.1321 170 CYS A O   
763  C CB  . CYS A 95  ? 0.5869 0.6393 0.6258 -0.0365 0.0127  -0.1093 170 CYS A CB  
764  S SG  . CYS A 95  ? 0.7243 0.7621 0.7397 -0.0162 0.0239  -0.1037 170 CYS A SG  
765  N N   . VAL A 96  ? 0.5288 0.5321 0.5710 -0.0567 0.0290  -0.1182 171 VAL A N   
766  C CA  . VAL A 96  ? 0.5256 0.5183 0.5713 -0.0710 0.0314  -0.1210 171 VAL A CA  
767  C C   . VAL A 96  ? 0.5165 0.5537 0.5946 -0.0836 0.0195  -0.1195 171 VAL A C   
768  O O   . VAL A 96  ? 0.5786 0.6478 0.6855 -0.0717 0.0166  -0.1094 171 VAL A O   
769  C CB  . VAL A 96  ? 0.5201 0.4935 0.5706 -0.0539 0.0442  -0.1137 171 VAL A CB  
770  C CG1 . VAL A 96  ? 0.6717 0.6245 0.7166 -0.0665 0.0495  -0.1149 171 VAL A CG1 
771  C CG2 . VAL A 96  ? 0.5813 0.5163 0.6036 -0.0383 0.0567  -0.1159 171 VAL A CG2 
772  N N   . ARG A 97  ? 0.5034 0.5428 0.5772 -0.1089 0.0147  -0.1311 172 ARG A N   
773  C CA  . ARG A 97  ? 0.4844 0.5732 0.5936 -0.1220 0.0041  -0.1326 172 ARG A CA  
774  C C   . ARG A 97  ? 0.5207 0.6040 0.6493 -0.1248 0.0162  -0.1264 172 ARG A C   
775  O O   . ARG A 97  ? 0.5878 0.6245 0.6934 -0.1327 0.0312  -0.1298 172 ARG A O   
776  C CB  . ARG A 97  ? 0.4742 0.5757 0.5767 -0.1516 -0.0050 -0.1516 172 ARG A CB  
777  C CG  . ARG A 97  ? 0.6821 0.8470 0.8285 -0.1647 -0.0170 -0.1562 172 ARG A CG  
778  C CD  . ARG A 97  ? 0.6044 0.7922 0.7489 -0.1967 -0.0278 -0.1798 172 ARG A CD  
779  N NE  . ARG A 97  ? 0.9375 1.0759 1.0595 -0.2210 -0.0075 -0.1882 172 ARG A NE  
780  C CZ  . ARG A 97  ? 1.0432 1.1246 1.1179 -0.2340 0.0026  -0.1990 172 ARG A CZ  
781  N NH1 . ARG A 97  ? 1.1756 1.2394 1.2191 -0.2251 -0.0057 -0.2025 172 ARG A NH1 
782  N NH2 . ARG A 97  ? 0.9005 0.9357 0.9527 -0.2531 0.0242  -0.2045 172 ARG A NH2 
783  N N   . LEU A 98  ? 0.4516 0.5760 0.6160 -0.1166 0.0116  -0.1168 173 LEU A N   
784  C CA  . LEU A 98  ? 0.4061 0.5274 0.5878 -0.1206 0.0226  -0.1113 173 LEU A CA  
785  C C   . LEU A 98  ? 0.6012 0.7516 0.8061 -0.1483 0.0219  -0.1231 173 LEU A C   
786  O O   . LEU A 98  ? 0.5629 0.7667 0.7943 -0.1489 0.0073  -0.1249 173 LEU A O   
787  C CB  . LEU A 98  ? 0.3915 0.5377 0.5971 -0.0993 0.0215  -0.0960 173 LEU A CB  
788  C CG  . LEU A 98  ? 0.3987 0.5382 0.6172 -0.1015 0.0330  -0.0895 173 LEU A CG  
789  C CD1 . LEU A 98  ? 0.5122 0.5976 0.6992 -0.0946 0.0447  -0.0873 173 LEU A CD1 
790  C CD2 . LEU A 98  ? 0.3417 0.5107 0.5838 -0.0851 0.0314  -0.0769 173 LEU A CD2 
791  N N   . GLU A 99  ? 0.5492 0.6622 0.7404 -0.1684 0.0389  -0.1304 174 GLU A N   
792  C CA  . GLU A 99  ? 0.5502 0.6812 0.7525 -0.1883 0.0415  -0.1372 174 GLU A CA  
793  C C   . GLU A 99  ? 0.5305 0.6837 0.7596 -0.1788 0.0457  -0.1242 174 GLU A C   
794  O O   . GLU A 99  ? 0.5535 0.7563 0.8112 -0.1757 0.0344  -0.1214 174 GLU A O   
795  C CB  . GLU A 99  ? 0.5470 0.6180 0.7113 -0.2112 0.0623  -0.1493 174 GLU A CB  
796  C CG  . GLU A 99  ? 0.7634 0.8124 0.8965 -0.2242 0.0588  -0.1636 174 GLU A CG  
797  C CD  . GLU A 99  ? 1.1058 1.2108 1.2593 -0.2374 0.0402  -0.1749 174 GLU A CD  
798  O OE1 . GLU A 99  ? 1.0154 1.1526 1.1943 -0.2486 0.0415  -0.1783 174 GLU A OE1 
799  O OE2 . GLU A 99  ? 1.0042 1.1199 1.1470 -0.2360 0.0245  -0.1813 174 GLU A OE2 
800  N N   . GLN A 100 ? 0.4736 0.5869 0.6905 -0.1731 0.0625  -0.1163 175 GLN A N   
801  C CA  . GLN A 100 ? 0.5092 0.6347 0.7435 -0.1641 0.0680  -0.1040 175 GLN A CA  
802  C C   . GLN A 100 ? 0.4769 0.5607 0.6947 -0.1514 0.0805  -0.0948 175 GLN A C   
803  O O   . GLN A 100 ? 0.5395 0.5728 0.7258 -0.1526 0.0899  -0.0986 175 GLN A O   
804  C CB  . GLN A 100 ? 0.5900 0.7102 0.8258 -0.1842 0.0816  -0.1117 175 GLN A CB  
805  C CG  . GLN A 100 ? 0.5406 0.5922 0.7355 -0.2010 0.1062  -0.1206 175 GLN A CG  
806  C CD  . GLN A 100 ? 0.8850 0.9327 1.0815 -0.2213 0.1227  -0.1300 175 GLN A CD  
807  O OE1 . GLN A 100 ? 0.9188 1.0206 1.1530 -0.2243 0.1141  -0.1313 175 GLN A OE1 
808  N NE2 . GLN A 100 ? 0.9435 0.9244 1.0965 -0.2340 0.1485  -0.1366 175 GLN A NE2 
809  N N   . ALA A 101 ? 0.4989 0.5991 0.7313 -0.1362 0.0798  -0.0815 176 ALA A N   
810  C CA  . ALA A 101 ? 0.3785 0.4464 0.5988 -0.1240 0.0900  -0.0730 176 ALA A CA  
811  C C   . ALA A 101 ? 0.4322 0.4884 0.6497 -0.1251 0.1026  -0.0660 176 ALA A C   
812  O O   . ALA A 101 ? 0.5378 0.6277 0.7743 -0.1266 0.0982  -0.0635 176 ALA A O   
813  C CB  . ALA A 101 ? 0.4499 0.5457 0.6828 -0.1008 0.0759  -0.0637 176 ALA A CB  
814  N N   . TRP A 102 ? 0.4237 0.4275 0.6138 -0.1230 0.1192  -0.0624 177 TRP A N   
815  C CA  . TRP A 102 ? 0.4841 0.4667 0.6634 -0.1233 0.1337  -0.0560 177 TRP A CA  
816  C C   . TRP A 102 ? 0.4542 0.3900 0.5947 -0.1035 0.1369  -0.0461 177 TRP A C   
817  O O   . TRP A 102 ? 0.5845 0.5090 0.7026 -0.0840 0.1230  -0.0444 177 TRP A O   
818  C CB  . TRP A 102 ? 0.5756 0.5271 0.7352 -0.1422 0.1514  -0.0650 177 TRP A CB  
819  C CG  . TRP A 102 ? 0.5706 0.4462 0.6768 -0.1474 0.1689  -0.0693 177 TRP A CG  
820  C CD1 . TRP A 102 ? 0.5255 0.3289 0.5785 -0.1391 0.1877  -0.0626 177 TRP A CD1 
821  C CD2 . TRP A 102 ? 0.5007 0.3563 0.5891 -0.1569 0.1688  -0.0796 177 TRP A CD2 
822  N NE1 . TRP A 102 ? 0.6337 0.3725 0.6336 -0.1381 0.1984  -0.0665 177 TRP A NE1 
823  C CE2 . TRP A 102 ? 0.5834 0.3515 0.6051 -0.1507 0.1885  -0.0775 177 TRP A CE2 
824  C CE3 . TRP A 102 ? 0.4455 0.3441 0.5601 -0.1667 0.1534  -0.0897 177 TRP A CE3 
825  C CZ2 . TRP A 102 ? 0.6937 0.4164 0.6752 -0.1534 0.1949  -0.0847 177 TRP A CZ2 
826  C CZ3 . TRP A 102 ? 0.6346 0.4884 0.7124 -0.1746 0.1602  -0.0988 177 TRP A CZ3 
827  C CH2 . TRP A 102 ? 0.6183 0.3840 0.6302 -0.1677 0.1818  -0.0960 177 TRP A CH2 
828  N N   . GLU A 103 ? 0.5626 0.4744 0.6910 -0.1042 0.1519  -0.0399 178 GLU A N   
829  C CA  . GLU A 103 ? 0.5939 0.4613 0.6756 -0.0819 0.1506  -0.0308 178 GLU A CA  
830  C C   . GLU A 103 ? 0.6545 0.4576 0.6959 -0.0909 0.1777  -0.0288 178 GLU A C   
831  O O   . GLU A 103 ? 0.6609 0.4798 0.7236 -0.1076 0.1910  -0.0328 178 GLU A O   
832  C CB  . GLU A 103 ? 0.5143 0.4205 0.6173 -0.0690 0.1378  -0.0238 178 GLU A CB  
833  C CG  . GLU A 103 ? 0.8686 0.8031 1.0078 -0.0831 0.1512  -0.0209 178 GLU A CG  
834  C CD  . GLU A 103 ? 0.8558 0.8167 1.0060 -0.0709 0.1428  -0.0144 178 GLU A CD  
835  O OE1 . GLU A 103 ? 0.9987 0.9626 1.1340 -0.0553 0.1257  -0.0147 178 GLU A OE1 
836  O OE2 . GLU A 103 ? 0.8660 0.8436 1.0266 -0.0701 0.1442  -0.0111 178 GLU A OE2 
837  N N   . GLU A 104 ? 0.6729 0.4121 0.6501 -0.0706 0.1791  -0.0237 179 GLU A N   
838  C CA  . GLU A 104 ? 0.6896 0.3524 0.6124 -0.0745 0.2066  -0.0204 179 GLU A CA  
839  C C   . GLU A 104 ? 0.8661 0.4807 0.7236 -0.0397 0.1952  -0.0112 179 GLU A C   
840  O O   . GLU A 104 ? 0.9044 0.5113 0.7378 -0.0161 0.1778  -0.0108 179 GLU A O   
841  C CB  . GLU A 104 ? 0.9451 0.5793 0.8448 -0.0883 0.2238  -0.0296 179 GLU A CB  
842  C CG  . GLU A 104 ? 1.0175 0.6010 0.8672 -0.0895 0.2487  -0.0295 179 GLU A CG  
843  C CD  . GLU A 104 ? 1.1344 0.6834 0.9557 -0.1038 0.2697  -0.0399 179 GLU A CD  
844  O OE1 . GLU A 104 ? 1.5294 1.0841 1.3582 -0.1084 0.2626  -0.0450 179 GLU A OE1 
845  O OE2 . GLU A 104 ? 1.2529 0.7663 1.0418 -0.1112 0.2954  -0.0443 179 GLU A OE2 
846  N N   . GLY A 105 ? 0.7896 0.3742 0.6186 -0.0351 0.2044  -0.0044 180 GLY A N   
847  C CA  . GLY A 105 ? 0.8082 0.3506 0.5723 -0.0012 0.1908  0.0031  180 GLY A CA  
848  C C   . GLY A 105 ? 0.8396 0.4467 0.6296 0.0214  0.1531  0.0019  180 GLY A C   
849  O O   . GLY A 105 ? 0.9416 0.5287 0.6858 0.0537  0.1348  0.0041  180 GLY A O   
850  N N   . GLY A 106 ? 0.8499 0.5344 0.7112 0.0062  0.1421  -0.0024 181 GLY A N   
851  C CA  . GLY A 106 ? 0.7744 0.5204 0.6644 0.0213  0.1121  -0.0064 181 GLY A CA  
852  C C   . GLY A 106 ? 0.6338 0.4108 0.5465 0.0299  0.0972  -0.0119 181 GLY A C   
853  O O   . GLY A 106 ? 0.8125 0.6468 0.7591 0.0375  0.0764  -0.0172 181 GLY A O   
854  N N   . ILE A 107 ? 0.7963 0.5338 0.6892 0.0269  0.1103  -0.0119 182 ILE A N   
855  C CA  . ILE A 107 ? 0.6724 0.4287 0.5791 0.0345  0.1000  -0.0170 182 ILE A CA  
856  C C   . ILE A 107 ? 0.6156 0.4181 0.5820 0.0051  0.1049  -0.0227 182 ILE A C   
857  O O   . ILE A 107 ? 0.7253 0.5175 0.7036 -0.0206 0.1242  -0.0234 182 ILE A O   
858  C CB  . ILE A 107 ? 0.7513 0.4306 0.5944 0.0479  0.1139  -0.0145 182 ILE A CB  
859  C CG1 . ILE A 107 ? 0.7544 0.3869 0.5310 0.0848  0.1063  -0.0074 182 ILE A CG1 
860  C CG2 . ILE A 107 ? 0.7176 0.4113 0.5726 0.0545  0.1067  -0.0198 182 ILE A CG2 
861  C CD1 . ILE A 107 ? 0.7803 0.4709 0.5743 0.1153  0.0732  -0.0103 182 ILE A CD1 
862  N N   . LEU A 108 ? 0.6290 0.4839 0.6322 0.0099  0.0876  -0.0276 183 LEU A N   
863  C CA  . LEU A 108 ? 0.5443 0.4414 0.5958 -0.0120 0.0884  -0.0329 183 LEU A CA  
864  C C   . LEU A 108 ? 0.4818 0.3557 0.5183 -0.0136 0.0917  -0.0383 183 LEU A C   
865  O O   . LEU A 108 ? 0.5659 0.4281 0.5805 0.0092  0.0829  -0.0389 183 LEU A O   
866  C CB  . LEU A 108 ? 0.5126 0.4727 0.6066 -0.0074 0.0720  -0.0351 183 LEU A CB  
867  C CG  . LEU A 108 ? 0.4415 0.4404 0.5750 -0.0227 0.0703  -0.0397 183 LEU A CG  
868  C CD1 . LEU A 108 ? 0.3625 0.3742 0.5202 -0.0446 0.0817  -0.0379 183 LEU A CD1 
869  C CD2 . LEU A 108 ? 0.3540 0.3987 0.5148 -0.0145 0.0583  -0.0421 183 LEU A CD2 
870  N N   . TYR A 109 ? 0.4468 0.3165 0.4957 -0.0406 0.1050  -0.0436 184 TYR A N   
871  C CA  . TYR A 109 ? 0.4275 0.2739 0.4612 -0.0493 0.1104  -0.0515 184 TYR A CA  
872  C C   . TYR A 109 ? 0.4270 0.3313 0.5085 -0.0654 0.0998  -0.0588 184 TYR A C   
873  O O   . TYR A 109 ? 0.5508 0.4986 0.6725 -0.0812 0.0987  -0.0597 184 TYR A O   
874  C CB  . TYR A 109 ? 0.5641 0.3528 0.5659 -0.0718 0.1366  -0.0562 184 TYR A CB  
875  C CG  . TYR A 109 ? 0.6517 0.3672 0.5922 -0.0550 0.1516  -0.0483 184 TYR A CG  
876  C CD1 . TYR A 109 ? 0.6957 0.4064 0.6345 -0.0542 0.1574  -0.0412 184 TYR A CD1 
877  C CD2 . TYR A 109 ? 0.6107 0.2557 0.4884 -0.0381 0.1617  -0.0473 184 TYR A CD2 
878  C CE1 . TYR A 109 ? 0.8699 0.5078 0.7441 -0.0369 0.1709  -0.0337 184 TYR A CE1 
879  C CE2 . TYR A 109 ? 0.7367 0.3082 0.5489 -0.0178 0.1755  -0.0388 184 TYR A CE2 
880  C CZ  . TYR A 109 ? 0.8527 0.4211 0.6626 -0.0176 0.1793  -0.0322 184 TYR A CZ  
881  O OH  . TYR A 109 ? 1.0710 0.5609 0.8076 0.0046  0.1927  -0.0234 184 TYR A OH  
882  N N   . LEU A 110 ? 0.5210 0.4238 0.5943 -0.0584 0.0926  -0.0636 185 LEU A N   
883  C CA  . LEU A 110 ? 0.5057 0.4516 0.6108 -0.0719 0.0830  -0.0711 185 LEU A CA  
884  C C   . LEU A 110 ? 0.5449 0.4520 0.6205 -0.0864 0.0922  -0.0818 185 LEU A C   
885  O O   . LEU A 110 ? 0.6480 0.5097 0.6839 -0.0698 0.0970  -0.0808 185 LEU A O   
886  C CB  . LEU A 110 ? 0.4682 0.4500 0.5907 -0.0510 0.0671  -0.0681 185 LEU A CB  
887  C CG  . LEU A 110 ? 0.5191 0.5439 0.6731 -0.0425 0.0594  -0.0611 185 LEU A CG  
888  C CD1 . LEU A 110 ? 0.6911 0.7008 0.8284 -0.0208 0.0582  -0.0555 185 LEU A CD1 
889  C CD2 . LEU A 110 ? 0.5984 0.6634 0.7764 -0.0386 0.0495  -0.0631 185 LEU A CD2 
890  N N   . GLN A 111 ? 0.3748 0.3015 0.4694 -0.1167 0.0949  -0.0928 186 GLN A N   
891  C CA  . GLN A 111 ? 0.4594 0.3518 0.5270 -0.1389 0.1051  -0.1071 186 GLN A CA  
892  C C   . GLN A 111 ? 0.5132 0.4479 0.6003 -0.1430 0.0873  -0.1144 186 GLN A C   
893  O O   . GLN A 111 ? 0.7056 0.7011 0.8346 -0.1535 0.0740  -0.1178 186 GLN A O   
894  C CB  . GLN A 111 ? 0.5773 0.4633 0.6518 -0.1748 0.1223  -0.1189 186 GLN A CB  
895  C CG  . GLN A 111 ? 0.5865 0.4420 0.6333 -0.2026 0.1339  -0.1363 186 GLN A CG  
896  C CD  . GLN A 111 ? 0.6941 0.5608 0.7476 -0.2246 0.1465  -0.1430 186 GLN A CD  
897  O OE1 . GLN A 111 ? 0.6692 0.5568 0.7460 -0.2218 0.1496  -0.1363 186 GLN A OE1 
898  N NE2 . GLN A 111 ? 0.8943 0.7458 0.9265 -0.2468 0.1556  -0.1575 186 GLN A NE2 
899  N N   . THR A 112 ? 0.6236 0.5240 0.6769 -0.1317 0.0878  -0.1163 187 THR A N   
900  C CA  . THR A 112 ? 0.5767 0.5036 0.6362 -0.1341 0.0738  -0.1232 187 THR A CA  
901  C C   . THR A 112 ? 0.6169 0.4976 0.6366 -0.1576 0.0851  -0.1391 187 THR A C   
902  O O   . THR A 112 ? 0.7948 0.6172 0.7789 -0.1696 0.1066  -0.1438 187 THR A O   
903  C CB  . THR A 112 ? 0.5671 0.4963 0.6228 -0.1007 0.0664  -0.1129 187 THR A CB  
904  O OG1 . THR A 112 ? 0.6854 0.5541 0.6981 -0.0838 0.0806  -0.1103 187 THR A OG1 
905  C CG2 . THR A 112 ? 0.5117 0.4817 0.6024 -0.0815 0.0582  -0.1000 187 THR A CG2 
906  N N   . GLU A 113 ? 0.5352 0.4363 0.5547 -0.1645 0.0726  -0.1479 188 GLU A N   
907  C CA  . GLU A 113 ? 0.6398 0.4913 0.6140 -0.1843 0.0834  -0.1633 188 GLU A CA  
908  C C   . GLU A 113 ? 0.6471 0.4274 0.5725 -0.1584 0.1009  -0.1549 188 GLU A C   
909  O O   . GLU A 113 ? 0.8375 0.6265 0.7717 -0.1235 0.0960  -0.1402 188 GLU A O   
910  C CB  . GLU A 113 ? 0.5677 0.4549 0.5467 -0.1920 0.0641  -0.1731 188 GLU A CB  
911  C CG  . GLU A 113 ? 0.8409 0.7461 0.8271 -0.1572 0.0525  -0.1590 188 GLU A CG  
912  C CD  . GLU A 113 ? 0.9560 0.8896 0.9388 -0.1622 0.0347  -0.1672 188 GLU A CD  
913  O OE1 . GLU A 113 ? 1.0410 0.9742 1.0085 -0.1917 0.0302  -0.1854 188 GLU A OE1 
914  O OE2 . GLU A 113 ? 0.9483 0.9028 0.9406 -0.1375 0.0261  -0.1567 188 GLU A OE2 
915  N N   . LEU A 114 ? 0.8028 0.7866 0.9390 -0.2020 0.0781  0.1201  189 LEU A N   
916  C CA  . LEU A 114 ? 0.6478 0.5661 0.7193 -0.1914 0.0660  0.1297  189 LEU A CA  
917  C C   . LEU A 114 ? 0.6449 0.5428 0.7120 -0.1713 0.0368  0.1165  189 LEU A C   
918  O O   . LEU A 114 ? 0.8333 0.7254 0.9249 -0.1830 0.0202  0.1104  189 LEU A O   
919  C CB  . LEU A 114 ? 0.7430 0.6121 0.7898 -0.2205 0.0690  0.1475  189 LEU A CB  
920  C CG  . LEU A 114 ? 0.7291 0.5241 0.7092 -0.2065 0.0529  0.1569  189 LEU A CG  
921  C CD1 . LEU A 114 ? 0.9065 0.6980 0.8435 -0.1835 0.0621  0.1622  189 LEU A CD1 
922  C CD2 . LEU A 114 ? 0.9122 0.6499 0.8656 -0.2370 0.0529  0.1751  189 LEU A CD2 
923  N N   . CYS A 115 ? 0.7167 0.6053 0.7526 -0.1427 0.0313  0.1110  190 CYS A N   
924  C CA  . CYS A 115 ? 0.6084 0.4774 0.6332 -0.1241 0.0095  0.0979  190 CYS A CA  
925  C C   . CYS A 115 ? 0.7484 0.5576 0.7265 -0.1153 -0.0012 0.1028  190 CYS A C   
926  O O   . CYS A 115 ? 0.7396 0.5174 0.6905 -0.1231 0.0047  0.1182  190 CYS A O   
927  C CB  . CYS A 115 ? 0.4974 0.3995 0.5250 -0.1002 0.0113  0.0860  190 CYS A CB  
928  S SG  . CYS A 115 ? 0.6749 0.6372 0.7557 -0.1048 0.0167  0.0773  190 CYS A SG  
929  N N   . GLY A 116 ? 0.7723 0.5626 0.7387 -0.0984 -0.0172 0.0889  191 GLY A N   
930  C CA  . GLY A 116 ? 0.7806 0.5181 0.7092 -0.0843 -0.0286 0.0881  191 GLY A CA  
931  C C   . GLY A 116 ? 0.6997 0.4430 0.6077 -0.0584 -0.0246 0.0877  191 GLY A C   
932  O O   . GLY A 116 ? 0.7154 0.4957 0.6307 -0.0562 -0.0116 0.0922  191 GLY A O   
933  N N   . PRO A 117 ? 0.7314 0.4390 0.6152 -0.0372 -0.0370 0.0802  192 PRO A N   
934  C CA  . PRO A 117 ? 0.8175 0.5361 0.6897 -0.0103 -0.0375 0.0762  192 PRO A CA  
935  C C   . PRO A 117 ? 0.6776 0.4521 0.5738 -0.0005 -0.0291 0.0609  192 PRO A C   
936  O O   . PRO A 117 ? 0.7696 0.5602 0.6818 -0.0068 -0.0279 0.0492  192 PRO A O   
937  C CB  . PRO A 117 ? 0.7871 0.4594 0.6399 0.0110  -0.0543 0.0660  192 PRO A CB  
938  C CG  . PRO A 117 ? 0.9322 0.5832 0.7895 -0.0019 -0.0592 0.0565  192 PRO A CG  
939  C CD  . PRO A 117 ? 0.7219 0.3785 0.5907 -0.0353 -0.0526 0.0723  192 PRO A CD  
940  N N   . SER A 118 ? 0.6596 0.4592 0.5538 0.0134  -0.0252 0.0616  193 SER A N   
941  C CA  . SER A 118 ? 0.5583 0.4057 0.4724 0.0214  -0.0182 0.0471  193 SER A CA  
942  C C   . SER A 118 ? 0.4692 0.3167 0.3882 0.0377  -0.0234 0.0264  193 SER A C   
943  O O   . SER A 118 ? 0.6600 0.4749 0.5678 0.0515  -0.0338 0.0215  193 SER A O   
944  C CB  . SER A 118 ? 0.4501 0.3207 0.3594 0.0321  -0.0155 0.0508  193 SER A CB  
945  O OG  . SER A 118 ? 0.6905 0.5485 0.5903 0.0556  -0.0285 0.0445  193 SER A OG  
946  N N   . LEU A 119 ? 0.6174 0.5003 0.5517 0.0358  -0.0152 0.0135  194 LEU A N   
947  C CA  . LEU A 119 ? 0.5599 0.4493 0.4980 0.0480  -0.0140 -0.0076 194 LEU A CA  
948  C C   . LEU A 119 ? 0.5154 0.4145 0.4601 0.0727  -0.0190 -0.0166 194 LEU A C   
949  O O   . LEU A 119 ? 0.7205 0.6151 0.6697 0.0880  -0.0204 -0.0344 194 LEU A O   
950  C CB  . LEU A 119 ? 0.5948 0.5173 0.5419 0.0375  -0.0029 -0.0167 194 LEU A CB  
951  C CG  . LEU A 119 ? 0.6993 0.6271 0.6439 0.0413  0.0043  -0.0379 194 LEU A CG  
952  C CD1 . LEU A 119 ? 0.7173 0.6038 0.6430 0.0390  -0.0013 -0.0430 194 LEU A CD1 
953  C CD2 . LEU A 119 ? 0.5620 0.5130 0.5058 0.0260  0.0143  -0.0417 194 LEU A CD2 
954  N N   . GLN A 120 ? 0.5791 0.4916 0.5248 0.0781  -0.0228 -0.0063 195 GLN A N   
955  C CA  . GLN A 120 ? 0.4875 0.4064 0.4397 0.1031  -0.0343 -0.0135 195 GLN A CA  
956  C C   . GLN A 120 ? 0.5485 0.4158 0.4820 0.1177  -0.0508 -0.0079 195 GLN A C   
957  O O   . GLN A 120 ? 0.7628 0.6263 0.7074 0.1416  -0.0603 -0.0242 195 GLN A O   
958  C CB  . GLN A 120 ? 0.5338 0.4731 0.4829 0.1033  -0.0373 -0.0030 195 GLN A CB  
959  C CG  . GLN A 120 ? 0.5733 0.5235 0.5309 0.1290  -0.0541 -0.0111 195 GLN A CG  
960  C CD  . GLN A 120 ? 0.6024 0.5673 0.5487 0.1272  -0.0590 -0.0009 195 GLN A CD  
961  O OE1 . GLN A 120 ? 0.6713 0.6234 0.5937 0.1099  -0.0512 0.0165  195 GLN A OE1 
962  N NE2 . GLN A 120 ? 0.6777 0.6717 0.6426 0.1451  -0.0719 -0.0137 195 GLN A NE2 
963  N N   . GLN A 121 ? 0.6520 0.4783 0.5581 0.1032  -0.0543 0.0143  196 GLN A N   
964  C CA  . GLN A 121 ? 0.5479 0.3141 0.4291 0.1126  -0.0710 0.0226  196 GLN A CA  
965  C C   . GLN A 121 ? 0.5651 0.3089 0.4515 0.1188  -0.0726 0.0051  196 GLN A C   
966  O O   . GLN A 121 ? 0.7721 0.4798 0.6511 0.1415  -0.0885 -0.0024 196 GLN A O   
967  C CB  . GLN A 121 ? 0.6054 0.3350 0.4573 0.0875  -0.0689 0.0497  196 GLN A CB  
968  C CG  . GLN A 121 ? 0.7699 0.5087 0.6040 0.0827  -0.0671 0.0675  196 GLN A CG  
969  C CD  . GLN A 121 ? 0.7662 0.4776 0.5757 0.0533  -0.0572 0.0917  196 GLN A CD  
970  O OE1 . GLN A 121 ? 0.8042 0.5258 0.6302 0.0307  -0.0441 0.0924  196 GLN A OE1 
971  N NE2 . GLN A 121 ? 0.9227 0.5994 0.6924 0.0525  -0.0637 0.1113  196 GLN A NE2 
972  N N   . HIS A 122 ? 0.6725 0.4334 0.5685 0.1001  -0.0581 -0.0025 197 HIS A N   
973  C CA  . HIS A 122 ? 0.6207 0.3568 0.5134 0.1036  -0.0589 -0.0201 197 HIS A CA  
974  C C   . HIS A 122 ? 0.5804 0.3388 0.4921 0.1326  -0.0577 -0.0479 197 HIS A C   
975  O O   . HIS A 122 ? 0.8489 0.5731 0.7539 0.1496  -0.0653 -0.0629 197 HIS A O   
976  C CB  . HIS A 122 ? 0.6315 0.3828 0.5259 0.0776  -0.0461 -0.0223 197 HIS A CB  
977  C CG  . HIS A 122 ? 0.7362 0.4546 0.6168 0.0767  -0.0482 -0.0386 197 HIS A CG  
978  N ND1 . HIS A 122 ? 0.9439 0.6848 0.8268 0.0785  -0.0360 -0.0609 197 HIS A ND1 
979  C CD2 . HIS A 122 ? 0.7104 0.3710 0.5696 0.0723  -0.0610 -0.0365 197 HIS A CD2 
980  C CE1 . HIS A 122 ? 0.7560 0.4549 0.6173 0.0769  -0.0410 -0.0728 197 HIS A CE1 
981  N NE2 . HIS A 122 ? 0.9187 0.5684 0.7673 0.0735  -0.0574 -0.0588 197 HIS A NE2 
982  N N   . CYS A 123 ? 0.6844 0.5011 0.6224 0.1385  -0.0477 -0.0569 198 CYS A N   
983  C CA  . CYS A 123 ? 0.6590 0.5079 0.6248 0.1641  -0.0440 -0.0851 198 CYS A CA  
984  C C   . CYS A 123 ? 0.6913 0.5228 0.6649 0.1968  -0.0667 -0.0872 198 CYS A C   
985  O O   . CYS A 123 ? 0.9121 0.7424 0.9029 0.2237  -0.0707 -0.1114 198 CYS A O   
986  C CB  . CYS A 123 ? 0.7202 0.6361 0.7136 0.1562  -0.0273 -0.0936 198 CYS A CB  
987  S SG  . CYS A 123 ? 0.9034 0.8338 0.8842 0.1228  -0.0035 -0.0957 198 CYS A SG  
988  N N   . GLU A 124 ? 0.6846 0.5014 0.6441 0.1963  -0.0823 -0.0632 199 GLU A N   
989  C CA  . GLU A 124 ? 0.7150 0.5025 0.6709 0.2270  -0.1096 -0.0612 199 GLU A CA  
990  C C   . GLU A 124 ? 0.8874 0.6035 0.8184 0.2393  -0.1242 -0.0622 199 GLU A C   
991  O O   . GLU A 124 ? 0.9082 0.6059 0.8496 0.2741  -0.1439 -0.0769 199 GLU A O   
992  C CB  . GLU A 124 ? 0.8174 0.5888 0.7456 0.2180  -0.1224 -0.0315 199 GLU A CB  
993  C CG  . GLU A 124 ? 0.9699 0.8041 0.9179 0.2084  -0.1121 -0.0311 199 GLU A CG  
994  C CD  . GLU A 124 ? 1.1053 0.9176 1.0163 0.1961  -0.1205 -0.0024 199 GLU A CD  
995  O OE1 . GLU A 124 ? 1.2187 0.9686 1.0900 0.1999  -0.1377 0.0166  199 GLU A OE1 
996  O OE2 . GLU A 124 ? 1.0733 0.9271 0.9910 0.1817  -0.1090 0.0008  199 GLU A OE2 
997  N N   . ALA A 125 ? 0.9485 0.6228 0.8486 0.2119  -0.1170 -0.0479 200 ALA A N   
998  C CA  . ALA A 125 ? 0.8362 0.4356 0.7083 0.2186  -0.1318 -0.0478 200 ALA A CA  
999  C C   . ALA A 125 ? 1.0051 0.6107 0.8983 0.2424  -0.1272 -0.0838 200 ALA A C   
1000 O O   . ALA A 125 ? 1.1067 0.6724 0.9964 0.2699  -0.1453 -0.0950 200 ALA A O   
1001 C CB  . ALA A 125 ? 0.8824 0.4456 0.7244 0.1796  -0.1242 -0.0268 200 ALA A CB  
1002 N N   . TRP A 126 ? 0.8572 0.5146 0.7705 0.2296  -0.1012 -0.1021 201 TRP A N   
1003 C CA  . TRP A 126 ? 1.0328 0.6992 0.9612 0.2487  -0.0906 -0.1380 201 TRP A CA  
1004 C C   . TRP A 126 ? 0.8986 0.6193 0.8748 0.2846  -0.0899 -0.1646 201 TRP A C   
1005 O O   . TRP A 126 ? 0.9222 0.6507 0.9146 0.3003  -0.0838 -0.1892 201 TRP A O   
1006 C CB  . TRP A 126 ? 0.8529 0.5482 0.7758 0.2194  -0.0631 -0.1466 201 TRP A CB  
1007 C CG  . TRP A 126 ? 0.9336 0.5735 0.8159 0.1899  -0.0678 -0.1290 201 TRP A CG  
1008 C CD1 . TRP A 126 ? 1.0755 0.7170 0.9460 0.1567  -0.0668 -0.1010 201 TRP A CD1 
1009 C CD2 . TRP A 126 ? 0.8889 0.4648 0.7409 0.1912  -0.0758 -0.1403 201 TRP A CD2 
1010 N NE1 . TRP A 126 ? 1.1011 0.6889 0.9413 0.1362  -0.0743 -0.0940 201 TRP A NE1 
1011 C CE2 . TRP A 126 ? 1.1927 0.7367 1.0181 0.1556  -0.0808 -0.1172 201 TRP A CE2 
1012 C CE3 . TRP A 126 ? 1.0014 0.5447 0.8483 0.2197  -0.0796 -0.1699 201 TRP A CE3 
1013 C CZ2 . TRP A 126 ? 1.2294 0.7090 1.0219 0.1451  -0.0914 -0.1216 201 TRP A CZ2 
1014 C CZ3 . TRP A 126 ? 1.1049 0.5869 0.9167 0.2074  -0.0875 -0.1721 201 TRP A CZ3 
1015 C CH2 . TRP A 126 ? 1.2738 0.7162 1.0551 0.1723  -0.0959 -0.1500 201 TRP A CH2 
1016 N N   . GLY A 127 ? 0.9610 0.7315 0.9629 0.2860  -0.0928 -0.1546 202 GLY A N   
1017 C CA  . GLY A 127 ? 1.0379 0.8643 1.0891 0.3121  -0.0970 -0.1732 202 GLY A CA  
1018 C C   . GLY A 127 ? 1.2214 1.1111 1.3120 0.3127  -0.0674 -0.2064 202 GLY A C   
1019 O O   . GLY A 127 ? 1.0847 1.0090 1.2144 0.3328  -0.0698 -0.2241 202 GLY A O   
1020 N N   . ALA A 128 ? 1.0743 0.9779 1.1525 0.2893  -0.0393 -0.2145 203 ALA A N   
1021 C CA  . ALA A 128 ? 0.9664 0.9245 1.0702 0.2820  -0.0065 -0.2419 203 ALA A CA  
1022 C C   . ALA A 128 ? 1.1508 1.1272 1.2341 0.2494  0.0185  -0.2398 203 ALA A C   
1023 O O   . ALA A 128 ? 0.9767 0.9336 1.0337 0.2267  0.0098  -0.2098 203 ALA A O   
1024 C CB  . ALA A 128 ? 0.8492 0.7721 0.9391 0.2932  -0.0002 -0.2609 203 ALA A CB  
1025 N N   . SER A 129 ? 1.1207 1.1326 1.2094 0.2344  0.0505  -0.2592 204 SER A N   
1026 C CA  . SER A 129 ? 0.7711 0.7941 0.8320 0.2003  0.0738  -0.2565 204 SER A CA  
1027 C C   . SER A 129 ? 0.8459 0.7975 0.8454 0.1829  0.0672  -0.2423 204 SER A C   
1028 O O   . SER A 129 ? 1.1200 1.0303 1.0980 0.1959  0.0664  -0.2591 204 SER A O   
1029 C CB  . SER A 129 ? 0.8812 0.9496 0.9533 0.1852  0.1084  -0.2745 204 SER A CB  
1030 O OG  . SER A 129 ? 1.1588 1.2908 1.2896 0.1950  0.1109  -0.2812 204 SER A OG  
1031 N N   . LEU A 130 ? 0.7470 0.6842 0.7208 0.1539  0.0607  -0.2123 205 LEU A N   
1032 C CA  . LEU A 130 ? 0.8765 0.7542 0.7990 0.1336  0.0527  -0.1983 205 LEU A CA  
1033 C C   . LEU A 130 ? 0.9933 0.8649 0.8819 0.1190  0.0765  -0.2194 205 LEU A C   
1034 O O   . LEU A 130 ? 0.9103 0.8246 0.8036 0.1046  0.1006  -0.2277 205 LEU A O   
1035 C CB  . LEU A 130 ? 0.7458 0.6208 0.6578 0.1073  0.0424  -0.1654 205 LEU A CB  
1036 C CG  . LEU A 130 ? 0.8365 0.6884 0.7562 0.1137  0.0171  -0.1400 205 LEU A CG  
1037 C CD1 . LEU A 130 ? 0.8223 0.6738 0.7316 0.0865  0.0122  -0.1127 205 LEU A CD1 
1038 C CD2 . LEU A 130 ? 0.8153 0.6052 0.7134 0.1248  0.0000  -0.1412 205 LEU A CD2 
1039 N N   . PRO A 131 ? 0.9693 0.7850 0.8187 0.1203  0.0706  -0.2285 206 PRO A N   
1040 C CA  . PRO A 131 ? 1.0366 0.8387 0.8415 0.1045  0.0922  -0.2481 206 PRO A CA  
1041 C C   . PRO A 131 ? 0.9136 0.7186 0.6880 0.0688  0.0961  -0.2279 206 PRO A C   
1042 O O   . PRO A 131 ? 0.8258 0.6202 0.6017 0.0556  0.0750  -0.1989 206 PRO A O   
1043 C CB  . PRO A 131 ? 0.9784 0.7087 0.7434 0.1104  0.0743  -0.2543 206 PRO A CB  
1044 C CG  . PRO A 131 ? 0.9543 0.6580 0.7363 0.1148  0.0420  -0.2266 206 PRO A CG  
1045 C CD  . PRO A 131 ? 0.9507 0.7070 0.7881 0.1328  0.0428  -0.2201 206 PRO A CD  
1046 N N   . GLU A 132 ? 1.0562 0.8749 0.8020 0.0533  0.1241  -0.2444 207 GLU A N   
1047 C CA  . GLU A 132 ? 0.8871 0.7065 0.6013 0.0206  0.1278  -0.2262 207 GLU A CA  
1048 C C   . GLU A 132 ? 0.9200 0.6808 0.5888 0.0032  0.0991  -0.2052 207 GLU A C   
1049 O O   . GLU A 132 ? 0.9304 0.6914 0.5899 -0.0171 0.0890  -0.1827 207 GLU A O   
1050 C CB  . GLU A 132 ? 0.9523 0.7924 0.6431 0.0074  0.1552  -0.2380 207 GLU A CB  
1051 C CG  . GLU A 132 ? 1.1141 1.0230 0.8593 0.0175  0.1800  -0.2491 207 GLU A CG  
1052 C CD  . GLU A 132 ? 1.2250 1.1542 0.9501 -0.0085 0.2028  -0.2453 207 GLU A CD  
1053 O OE1 . GLU A 132 ? 1.1713 1.0700 0.8512 -0.0357 0.1957  -0.2265 207 GLU A OE1 
1054 O OE2 . GLU A 132 ? 1.2669 1.2395 1.0217 -0.0024 0.2268  -0.2608 207 GLU A OE2 
1055 N N   . ALA A 133 ? 1.0027 0.7135 0.6457 0.0112  0.0840  -0.2137 208 ALA A N   
1056 C CA  . ALA A 133 ? 0.8673 0.5262 0.4744 -0.0061 0.0537  -0.1959 208 ALA A CA  
1057 C C   . ALA A 133 ? 1.0095 0.6839 0.6589 -0.0101 0.0302  -0.1650 208 ALA A C   
1058 O O   . ALA A 133 ? 1.0276 0.6973 0.6649 -0.0299 0.0168  -0.1463 208 ALA A O   
1059 C CB  . ALA A 133 ? 1.0181 0.6228 0.6000 0.0045  0.0397  -0.2112 208 ALA A CB  
1060 N N   . GLN A 134 ? 0.8646 0.5565 0.5622 0.0094  0.0250  -0.1600 209 GLN A N   
1061 C CA  . GLN A 134 ? 0.8247 0.5324 0.5588 0.0048  0.0076  -0.1323 209 GLN A CA  
1062 C C   . GLN A 134 ? 0.8042 0.5599 0.5585 -0.0031 0.0191  -0.1211 209 GLN A C   
1063 O O   . GLN A 134 ? 0.8069 0.5701 0.5753 -0.0144 0.0058  -0.0997 209 GLN A O   
1064 C CB  . GLN A 134 ? 0.8002 0.5097 0.5701 0.0265  0.0009  -0.1292 209 GLN A CB  
1065 C CG  . GLN A 134 ? 1.0228 0.6777 0.7730 0.0356  -0.0125 -0.1398 209 GLN A CG  
1066 C CD  . GLN A 134 ? 1.0891 0.7362 0.8681 0.0550  -0.0231 -0.1320 209 GLN A CD  
1067 O OE1 . GLN A 134 ? 1.0730 0.7519 0.8830 0.0571  -0.0239 -0.1140 209 GLN A OE1 
1068 N NE2 . GLN A 134 ? 1.4352 1.0342 1.1983 0.0693  -0.0325 -0.1455 209 GLN A NE2 
1069 N N   . VAL A 135 ? 0.8727 0.6620 0.6310 0.0021  0.0443  -0.1368 210 VAL A N   
1070 C CA  . VAL A 135 ? 0.6966 0.5300 0.4764 -0.0056 0.0548  -0.1275 210 VAL A CA  
1071 C C   . VAL A 135 ? 0.7739 0.5897 0.5201 -0.0306 0.0476  -0.1137 210 VAL A C   
1072 O O   . VAL A 135 ? 0.7323 0.5660 0.4976 -0.0372 0.0401  -0.0963 210 VAL A O   
1073 C CB  . VAL A 135 ? 0.8092 0.6827 0.6020 0.0013  0.0840  -0.1498 210 VAL A CB  
1074 C CG1 . VAL A 135 ? 0.7928 0.7052 0.6013 -0.0123 0.0942  -0.1410 210 VAL A CG1 
1075 C CG2 . VAL A 135 ? 0.7557 0.6510 0.5916 0.0308  0.0848  -0.1625 210 VAL A CG2 
1076 N N   . TRP A 136 ? 0.8500 0.6266 0.5427 -0.0436 0.0476  -0.1221 211 TRP A N   
1077 C CA  . TRP A 136 ? 0.8431 0.5944 0.4974 -0.0656 0.0350  -0.1088 211 TRP A CA  
1078 C C   . TRP A 136 ? 0.8865 0.6252 0.5608 -0.0674 0.0030  -0.0880 211 TRP A C   
1079 O O   . TRP A 136 ? 0.9946 0.7368 0.6714 -0.0772 -0.0086 -0.0729 211 TRP A O   
1080 C CB  . TRP A 136 ? 0.8990 0.6034 0.4835 -0.0785 0.0382  -0.1223 211 TRP A CB  
1081 C CG  . TRP A 136 ? 0.8351 0.5554 0.3964 -0.0833 0.0739  -0.1409 211 TRP A CG  
1082 C CD1 . TRP A 136 ? 0.9720 0.7011 0.5348 -0.0710 0.0941  -0.1631 211 TRP A CD1 
1083 C CD2 . TRP A 136 ? 0.9010 0.6435 0.4573 -0.0992 0.0904  -0.1332 211 TRP A CD2 
1084 N NE1 . TRP A 136 ? 0.9599 0.7205 0.5224 -0.0788 0.1229  -0.1698 211 TRP A NE1 
1085 C CE2 . TRP A 136 ? 0.8251 0.5918 0.3824 -0.0979 0.1212  -0.1508 211 TRP A CE2 
1086 C CE3 . TRP A 136 ? 0.8792 0.6208 0.4312 -0.1142 0.0808  -0.1136 211 TRP A CE3 
1087 C CZ2 . TRP A 136 ? 0.9029 0.6916 0.4571 -0.1149 0.1431  -0.1482 211 TRP A CZ2 
1088 C CZ3 . TRP A 136 ? 0.9016 0.6597 0.4468 -0.1298 0.1017  -0.1110 211 TRP A CZ3 
1089 C CH2 . TRP A 136 ? 0.9011 0.6823 0.4478 -0.1318 0.1327  -0.1277 211 TRP A CH2 
1090 N N   . GLY A 137 ? 0.8079 0.5317 0.4984 -0.0585 -0.0112 -0.0882 212 GLY A N   
1091 C CA  . GLY A 137 ? 0.6338 0.3525 0.3502 -0.0631 -0.0379 -0.0703 212 GLY A CA  
1092 C C   . GLY A 137 ? 0.6168 0.3792 0.3838 -0.0579 -0.0349 -0.0550 212 GLY A C   
1093 O O   . GLY A 137 ? 0.8380 0.6075 0.6189 -0.0656 -0.0491 -0.0418 212 GLY A O   
1094 N N   . TYR A 138 ? 0.7060 0.4973 0.5003 -0.0432 -0.0178 -0.0583 213 TYR A N   
1095 C CA  . TYR A 138 ? 0.6904 0.5201 0.5247 -0.0382 -0.0143 -0.0456 213 TYR A CA  
1096 C C   . TYR A 138 ? 0.7054 0.5539 0.5336 -0.0456 -0.0068 -0.0437 213 TYR A C   
1097 O O   . TYR A 138 ? 0.7807 0.6471 0.6313 -0.0473 -0.0126 -0.0317 213 TYR A O   
1098 C CB  . TYR A 138 ? 0.5870 0.4375 0.4446 -0.0202 -0.0020 -0.0505 213 TYR A CB  
1099 C CG  . TYR A 138 ? 0.7190 0.5425 0.5789 -0.0122 -0.0114 -0.0504 213 TYR A CG  
1100 C CD1 . TYR A 138 ? 0.7451 0.5459 0.6085 -0.0232 -0.0285 -0.0379 213 TYR A CD1 
1101 C CD2 . TYR A 138 ? 0.7556 0.5752 0.6162 0.0061  -0.0043 -0.0637 213 TYR A CD2 
1102 C CE1 . TYR A 138 ? 0.6057 0.3754 0.4676 -0.0199 -0.0374 -0.0367 213 TYR A CE1 
1103 C CE2 . TYR A 138 ? 0.7378 0.5228 0.5955 0.0138  -0.0155 -0.0631 213 TYR A CE2 
1104 C CZ  . TYR A 138 ? 0.7862 0.5436 0.6416 -0.0010 -0.0316 -0.0486 213 TYR A CZ  
1105 O OH  . TYR A 138 ? 0.8816 0.5988 0.7307 0.0027  -0.0430 -0.0468 213 TYR A OH  
1106 N N   . LEU A 139 ? 0.6998 0.5422 0.4957 -0.0511 0.0072  -0.0564 214 LEU A N   
1107 C CA  . LEU A 139 ? 0.6048 0.4555 0.3870 -0.0627 0.0140  -0.0537 214 LEU A CA  
1108 C C   . LEU A 139 ? 0.6316 0.4533 0.3932 -0.0747 -0.0088 -0.0411 214 LEU A C   
1109 O O   . LEU A 139 ? 0.7936 0.6256 0.5671 -0.0773 -0.0142 -0.0316 214 LEU A O   
1110 C CB  . LEU A 139 ? 0.7576 0.6045 0.5048 -0.0708 0.0367  -0.0700 214 LEU A CB  
1111 C CG  . LEU A 139 ? 0.6270 0.4716 0.3478 -0.0891 0.0453  -0.0669 214 LEU A CG  
1112 C CD1 . LEU A 139 ? 0.6111 0.4944 0.3741 -0.0847 0.0487  -0.0603 214 LEU A CD1 
1113 C CD2 . LEU A 139 ? 0.6982 0.5420 0.3850 -0.1004 0.0733  -0.0845 214 LEU A CD2 
1114 N N   . ARG A 140 ? 0.6738 0.4574 0.4050 -0.0807 -0.0251 -0.0424 215 ARG A N   
1115 C CA  . ARG A 140 ? 0.6646 0.4205 0.3793 -0.0899 -0.0526 -0.0317 215 ARG A CA  
1116 C C   . ARG A 140 ? 0.6515 0.4328 0.4224 -0.0820 -0.0689 -0.0198 215 ARG A C   
1117 O O   . ARG A 140 ? 0.8301 0.6136 0.6104 -0.0830 -0.0823 -0.0114 215 ARG A O   
1118 C CB  . ARG A 140 ? 0.6755 0.3855 0.3460 -0.0979 -0.0698 -0.0373 215 ARG A CB  
1119 C CG  . ARG A 140 ? 0.7763 0.4594 0.4370 -0.1048 -0.1054 -0.0269 215 ARG A CG  
1120 C CD  . ARG A 140 ? 0.8515 0.4843 0.4600 -0.1144 -0.1261 -0.0332 215 ARG A CD  
1121 N NE  . ARG A 140 ? 1.1491 0.7582 0.7491 -0.1189 -0.1628 -0.0227 215 ARG A NE  
1122 C CZ  . ARG A 140 ? 1.3041 0.9250 0.9519 -0.1153 -0.1917 -0.0175 215 ARG A CZ  
1123 N NH1 . ARG A 140 ? 1.2847 0.9353 0.9860 -0.1113 -0.1873 -0.0199 215 ARG A NH1 
1124 N NH2 . ARG A 140 ? 1.2019 0.8094 0.8507 -0.1137 -0.2215 -0.0077 215 ARG A NH2 
1125 N N   . ASP A 141 ? 0.7169 0.5157 0.5244 -0.0743 -0.0668 -0.0196 216 ASP A N   
1126 C CA  . ASP A 141 ? 0.6039 0.4287 0.4633 -0.0702 -0.0770 -0.0092 216 ASP A CA  
1127 C C   . ASP A 141 ? 0.5641 0.4240 0.4505 -0.0627 -0.0640 -0.0044 216 ASP A C   
1128 O O   . ASP A 141 ? 0.6758 0.5516 0.5924 -0.0608 -0.0743 0.0021  216 ASP A O   
1129 C CB  . ASP A 141 ? 0.6555 0.4856 0.5391 -0.0673 -0.0736 -0.0087 216 ASP A CB  
1130 C CG  . ASP A 141 ? 0.9942 0.7871 0.8564 -0.0761 -0.0915 -0.0135 216 ASP A CG  
1131 O OD1 . ASP A 141 ? 1.1412 0.9118 0.9832 -0.0846 -0.1128 -0.0142 216 ASP A OD1 
1132 O OD2 . ASP A 141 ? 1.0689 0.8505 0.9315 -0.0741 -0.0868 -0.0168 216 ASP A OD2 
1133 N N   . THR A 142 ? 0.5262 0.3998 0.4045 -0.0577 -0.0422 -0.0095 217 THR A N   
1134 C CA  . THR A 142 ? 0.5302 0.4340 0.4305 -0.0517 -0.0318 -0.0064 217 THR A CA  
1135 C C   . THR A 142 ? 0.7047 0.5957 0.5853 -0.0580 -0.0390 -0.0052 217 THR A C   
1136 O O   . THR A 142 ? 0.6639 0.5700 0.5663 -0.0533 -0.0421 -0.0010 217 THR A O   
1137 C CB  . THR A 142 ? 0.5972 0.5206 0.4981 -0.0449 -0.0110 -0.0135 217 THR A CB  
1138 O OG1 . THR A 142 ? 0.5496 0.4727 0.4606 -0.0376 -0.0087 -0.0146 217 THR A OG1 
1139 C CG2 . THR A 142 ? 0.5840 0.5377 0.5089 -0.0384 -0.0036 -0.0104 217 THR A CG2 
1140 N N   . LEU A 143 ? 0.5619 0.4202 0.3965 -0.0691 -0.0416 -0.0091 218 LEU A N   
1141 C CA  . LEU A 143 ? 0.5276 0.3601 0.3329 -0.0775 -0.0527 -0.0052 218 LEU A CA  
1142 C C   . LEU A 143 ? 0.5703 0.3899 0.3910 -0.0733 -0.0824 0.0023  218 LEU A C   
1143 O O   . LEU A 143 ? 0.8147 0.6276 0.6380 -0.0708 -0.0937 0.0064  218 LEU A O   
1144 C CB  . LEU A 143 ? 0.5335 0.3277 0.2769 -0.0932 -0.0480 -0.0099 218 LEU A CB  
1145 C CG  . LEU A 143 ? 0.5943 0.4053 0.3251 -0.1000 -0.0169 -0.0196 218 LEU A CG  
1146 C CD1 . LEU A 143 ? 0.5761 0.3518 0.2458 -0.1166 -0.0077 -0.0265 218 LEU A CD1 
1147 C CD2 . LEU A 143 ? 0.5319 0.3542 0.2695 -0.1043 -0.0105 -0.0164 218 LEU A CD2 
1148 N N   . LEU A 144 ? 0.5910 0.4071 0.4249 -0.0723 -0.0968 0.0027  219 LEU A N   
1149 C CA  . LEU A 144 ? 0.5449 0.3616 0.4097 -0.0674 -0.1252 0.0074  219 LEU A CA  
1150 C C   . LEU A 144 ? 0.5259 0.3862 0.4488 -0.0548 -0.1185 0.0091  219 LEU A C   
1151 O O   . LEU A 144 ? 0.6566 0.5179 0.5991 -0.0475 -0.1363 0.0105  219 LEU A O   
1152 C CB  . LEU A 144 ? 0.5279 0.3407 0.4050 -0.0714 -0.1388 0.0061  219 LEU A CB  
1153 C CG  . LEU A 144 ? 0.5823 0.3452 0.4004 -0.0829 -0.1550 0.0029  219 LEU A CG  
1154 C CD1 . LEU A 144 ? 0.6907 0.4520 0.5262 -0.0870 -0.1667 0.0000  219 LEU A CD1 
1155 C CD2 . LEU A 144 ? 0.6452 0.3719 0.4336 -0.0851 -0.1867 0.0072  219 LEU A CD2 
1156 N N   . ALA A 145 ? 0.5479 0.4419 0.4961 -0.0509 -0.0936 0.0082  220 ALA A N   
1157 C CA  . ALA A 145 ? 0.4668 0.3991 0.4600 -0.0404 -0.0834 0.0089  220 ALA A CA  
1158 C C   . ALA A 145 ? 0.5702 0.4980 0.5492 -0.0355 -0.0798 0.0070  220 ALA A C   
1159 O O   . ALA A 145 ? 0.6499 0.5893 0.6558 -0.0258 -0.0874 0.0057  220 ALA A O   
1160 C CB  . ALA A 145 ? 0.3969 0.3556 0.4057 -0.0388 -0.0597 0.0098  220 ALA A CB  
1161 N N   . LEU A 146 ? 0.5483 0.4601 0.4874 -0.0424 -0.0677 0.0052  221 LEU A N   
1162 C CA  . LEU A 146 ? 0.5295 0.4338 0.4532 -0.0421 -0.0640 0.0034  221 LEU A CA  
1163 C C   . LEU A 146 ? 0.4743 0.3419 0.3799 -0.0424 -0.0899 0.0062  221 LEU A C   
1164 O O   . LEU A 146 ? 0.6944 0.5612 0.6116 -0.0338 -0.0959 0.0047  221 LEU A O   
1165 C CB  . LEU A 146 ? 0.4620 0.3588 0.3501 -0.0538 -0.0460 -0.0001 221 LEU A CB  
1166 C CG  . LEU A 146 ? 0.5084 0.4416 0.4161 -0.0494 -0.0238 -0.0047 221 LEU A CG  
1167 C CD1 . LEU A 146 ? 0.4015 0.3335 0.2834 -0.0604 -0.0078 -0.0114 221 LEU A CD1 
1168 C CD2 . LEU A 146 ? 0.4085 0.3697 0.3475 -0.0378 -0.0191 -0.0052 221 LEU A CD2 
1169 N N   . ALA A 147 ? 0.5156 0.3480 0.3895 -0.0510 -0.1078 0.0096  222 ALA A N   
1170 C CA  . ALA A 147 ? 0.5363 0.3272 0.3891 -0.0496 -0.1389 0.0137  222 ALA A CA  
1171 C C   . ALA A 147 ? 0.5636 0.3792 0.4753 -0.0304 -0.1577 0.0115  222 ALA A C   
1172 O O   . ALA A 147 ? 0.7234 0.5162 0.6335 -0.0211 -0.1790 0.0117  222 ALA A O   
1173 C CB  . ALA A 147 ? 0.5872 0.3365 0.3938 -0.0617 -0.1572 0.0174  222 ALA A CB  
1174 N N   . HIS A 148 ? 0.5867 0.4479 0.5511 -0.0246 -0.1496 0.0087  223 HIS A N   
1175 C CA  . HIS A 148 ? 0.4987 0.3944 0.5273 -0.0082 -0.1603 0.0040  223 HIS A CA  
1176 C C   . HIS A 148 ? 0.5408 0.4618 0.5924 0.0041  -0.1415 -0.0018 223 HIS A C   
1177 O O   . HIS A 148 ? 0.6753 0.6009 0.7563 0.0202  -0.1558 -0.0078 223 HIS A O   
1178 C CB  . HIS A 148 ? 0.5076 0.4435 0.5822 -0.0113 -0.1527 0.0033  223 HIS A CB  
1179 C CG  . HIS A 148 ? 0.5131 0.4944 0.6603 0.0018  -0.1571 -0.0032 223 HIS A CG  
1180 N ND1 . HIS A 148 ? 0.6784 0.6573 0.8567 0.0118  -0.1909 -0.0075 223 HIS A ND1 
1181 C CD2 . HIS A 148 ? 0.5076 0.5392 0.7026 0.0064  -0.1311 -0.0074 223 HIS A CD2 
1182 C CE1 . HIS A 148 ? 0.5235 0.5561 0.7738 0.0225  -0.1834 -0.0160 223 HIS A CE1 
1183 N NE2 . HIS A 148 ? 0.5496 0.6135 0.8077 0.0180  -0.1452 -0.0156 223 HIS A NE2 
1184 N N   . LEU A 149 ? 0.5413 0.4781 0.5802 -0.0016 -0.1114 -0.0017 224 LEU A N   
1185 C CA  . LEU A 149 ? 0.4620 0.4183 0.5143 0.0086  -0.0947 -0.0081 224 LEU A CA  
1186 C C   . LEU A 149 ? 0.5111 0.4260 0.5285 0.0106  -0.1077 -0.0098 224 LEU A C   
1187 O O   . LEU A 149 ? 0.6283 0.5460 0.6659 0.0259  -0.1130 -0.0175 224 LEU A O   
1188 C CB  . LEU A 149 ? 0.4018 0.3794 0.4434 0.0016  -0.0654 -0.0072 224 LEU A CB  
1189 C CG  . LEU A 149 ? 0.3953 0.4156 0.4723 0.0043  -0.0461 -0.0069 224 LEU A CG  
1190 C CD1 . LEU A 149 ? 0.3876 0.4126 0.4821 -0.0029 -0.0538 -0.0015 224 LEU A CD1 
1191 C CD2 . LEU A 149 ? 0.4700 0.4983 0.5247 -0.0004 -0.0248 -0.0056 224 LEU A CD2 
1192 N N   . HIS A 150 ? 0.5536 0.4278 0.5168 -0.0057 -0.1118 -0.0036 225 HIS A N   
1193 C CA  . HIS A 150 ? 0.4752 0.3034 0.3974 -0.0099 -0.1221 -0.0030 225 HIS A CA  
1194 C C   . HIS A 150 ? 0.5841 0.3733 0.5036 0.0017  -0.1576 -0.0018 225 HIS A C   
1195 O O   . HIS A 150 ? 0.7510 0.5051 0.6504 0.0059  -0.1686 -0.0036 225 HIS A O   
1196 C CB  . HIS A 150 ? 0.5383 0.3358 0.4031 -0.0344 -0.1132 0.0032  225 HIS A CB  
1197 C CG  . HIS A 150 ? 0.6062 0.4415 0.4773 -0.0428 -0.0820 -0.0005 225 HIS A CG  
1198 N ND1 . HIS A 150 ? 0.4716 0.2976 0.3071 -0.0624 -0.0677 0.0009  225 HIS A ND1 
1199 C CD2 . HIS A 150 ? 0.4466 0.3283 0.3549 -0.0329 -0.0639 -0.0064 225 HIS A CD2 
1200 C CE1 . HIS A 150 ? 0.5936 0.4612 0.4507 -0.0618 -0.0448 -0.0048 225 HIS A CE1 
1201 N NE2 . HIS A 150 ? 0.5309 0.4290 0.4277 -0.0446 -0.0435 -0.0080 225 HIS A NE2 
1202 N N   . SER A 151 ? 0.6530 0.4446 0.5918 0.0073  -0.1787 0.0007  226 SER A N   
1203 C CA  . SER A 151 ? 0.6095 0.3682 0.5540 0.0226  -0.2177 0.0004  226 SER A CA  
1204 C C   . SER A 151 ? 0.5797 0.3702 0.5849 0.0496  -0.2205 -0.0127 226 SER A C   
1205 O O   . SER A 151 ? 0.8029 0.5609 0.8112 0.0666  -0.2524 -0.0158 226 SER A O   
1206 C CB  . SER A 151 ? 0.5661 0.3276 0.5252 0.0224  -0.2416 0.0039  226 SER A CB  
1207 O OG  . SER A 151 ? 0.7387 0.5678 0.7688 0.0301  -0.2267 -0.0033 226 SER A OG  
1208 N N   . GLN A 152 ? 0.6846 0.5348 0.7350 0.0547  -0.1884 -0.0211 227 GLN A N   
1209 C CA  . GLN A 152 ? 0.4579 0.3425 0.5625 0.0789  -0.1831 -0.0362 227 GLN A CA  
1210 C C   . GLN A 152 ? 0.5623 0.4381 0.6423 0.0792  -0.1619 -0.0422 227 GLN A C   
1211 O O   . GLN A 152 ? 0.6993 0.6100 0.8174 0.0960  -0.1466 -0.0561 227 GLN A O   
1212 C CB  . GLN A 152 ? 0.5278 0.4842 0.6981 0.0831  -0.1615 -0.0424 227 GLN A CB  
1213 C CG  . GLN A 152 ? 0.4614 0.4319 0.6623 0.0796  -0.1816 -0.0379 227 GLN A CG  
1214 C CD  . GLN A 152 ? 0.7005 0.7398 0.9638 0.0780  -0.1567 -0.0429 227 GLN A CD  
1215 O OE1 . GLN A 152 ? 0.7784 0.8283 1.0372 0.0598  -0.1485 -0.0340 227 GLN A OE1 
1216 N NE2 . GLN A 152 ? 0.7343 0.8179 1.0535 0.0960  -0.1432 -0.0579 227 GLN A NE2 
1217 N N   . GLY A 153 ? 0.7424 0.5738 0.7595 0.0595  -0.1597 -0.0333 228 GLY A N   
1218 C CA  . GLY A 153 ? 0.5447 0.3689 0.5400 0.0564  -0.1418 -0.0395 228 GLY A CA  
1219 C C   . GLY A 153 ? 0.6200 0.4987 0.6345 0.0525  -0.1069 -0.0439 228 GLY A C   
1220 O O   . GLY A 153 ? 0.6496 0.5345 0.6618 0.0576  -0.0937 -0.0538 228 GLY A O   
1221 N N   . LEU A 154 ? 0.6187 0.5316 0.6479 0.0436  -0.0941 -0.0367 229 LEU A N   
1222 C CA  . LEU A 154 ? 0.4663 0.4236 0.5079 0.0399  -0.0647 -0.0382 229 LEU A CA  
1223 C C   . LEU A 154 ? 0.5352 0.4832 0.5388 0.0188  -0.0547 -0.0299 229 LEU A C   
1224 O O   . LEU A 154 ? 0.6081 0.5349 0.5910 0.0062  -0.0638 -0.0213 229 LEU A O   
1225 C CB  . LEU A 154 ? 0.4418 0.4422 0.5280 0.0446  -0.0567 -0.0364 229 LEU A CB  
1226 C CG  . LEU A 154 ? 0.4248 0.4450 0.5623 0.0634  -0.0673 -0.0454 229 LEU A CG  
1227 C CD1 . LEU A 154 ? 0.3432 0.4060 0.5229 0.0595  -0.0580 -0.0418 229 LEU A CD1 
1228 C CD2 . LEU A 154 ? 0.4328 0.4682 0.5862 0.0808  -0.0546 -0.0610 229 LEU A CD2 
1229 N N   A VAL A 155 ? 0.4130 0.3780 0.4084 0.0160  -0.0365 -0.0343 230 VAL A N   
1230 N N   B VAL A 155 ? 0.4290 0.3936 0.4240 0.0157  -0.0367 -0.0342 230 VAL A N   
1231 C CA  A VAL A 155 ? 0.4675 0.4353 0.4390 -0.0004 -0.0259 -0.0303 230 VAL A CA  
1232 C CA  B VAL A 155 ? 0.4874 0.4544 0.4586 -0.0008 -0.0263 -0.0299 230 VAL A CA  
1233 C C   A VAL A 155 ? 0.5040 0.5113 0.4930 0.0041  -0.0084 -0.0295 230 VAL A C   
1234 C C   B VAL A 155 ? 0.5064 0.5130 0.4945 0.0036  -0.0085 -0.0295 230 VAL A C   
1235 O O   A VAL A 155 ? 0.4866 0.5122 0.4852 0.0142  0.0006  -0.0356 230 VAL A O   
1236 O O   B VAL A 155 ? 0.4870 0.5110 0.4837 0.0135  0.0002  -0.0358 230 VAL A O   
1237 C CB  A VAL A 155 ? 0.4825 0.4317 0.4277 -0.0095 -0.0254 -0.0366 230 VAL A CB  
1238 C CB  B VAL A 155 ? 0.4910 0.4367 0.4337 -0.0115 -0.0266 -0.0354 230 VAL A CB  
1239 C CG1 A VAL A 155 ? 0.5788 0.5370 0.5087 -0.0271 -0.0152 -0.0347 230 VAL A CG1 
1240 C CG1 B VAL A 155 ? 0.4635 0.4139 0.4129 0.0012  -0.0247 -0.0465 230 VAL A CG1 
1241 C CG2 A VAL A 155 ? 0.5415 0.4423 0.4648 -0.0131 -0.0441 -0.0364 230 VAL A CG2 
1242 C CG2 B VAL A 155 ? 0.5755 0.5389 0.5082 -0.0259 -0.0135 -0.0348 230 VAL A CG2 
1243 N N   . HIS A 156 ? 0.4667 0.4821 0.4545 -0.0034 -0.0042 -0.0223 231 HIS A N   
1244 C CA  . HIS A 156 ? 0.4511 0.4941 0.4506 0.0009  0.0087  -0.0192 231 HIS A CA  
1245 C C   . HIS A 156 ? 0.4492 0.5044 0.4363 0.0018  0.0167  -0.0244 231 HIS A C   
1246 O O   . HIS A 156 ? 0.5542 0.6253 0.5440 0.0097  0.0248  -0.0249 231 HIS A O   
1247 C CB  . HIS A 156 ? 0.4618 0.5023 0.4600 -0.0059 0.0081  -0.0120 231 HIS A CB  
1248 C CG  . HIS A 156 ? 0.4882 0.5464 0.4964 -0.0018 0.0173  -0.0064 231 HIS A CG  
1249 N ND1 . HIS A 156 ? 0.4535 0.5213 0.4514 0.0008  0.0240  -0.0068 231 HIS A ND1 
1250 C CD2 . HIS A 156 ? 0.4558 0.5203 0.4819 -0.0013 0.0192  0.0003  231 HIS A CD2 
1251 C CE1 . HIS A 156 ? 0.5055 0.5779 0.5078 0.0034  0.0290  0.0010  231 HIS A CE1 
1252 N NE2 . HIS A 156 ? 0.4483 0.5197 0.4681 0.0002  0.0281  0.0055  231 HIS A NE2 
1253 N N   . LEU A 157 ? 0.5890 0.6373 0.5614 -0.0079 0.0144  -0.0287 232 LEU A N   
1254 C CA  . LEU A 157 ? 0.4613 0.5237 0.4273 -0.0087 0.0174  -0.0358 232 LEU A CA  
1255 C C   . LEU A 157 ? 0.4929 0.5759 0.4637 -0.0020 0.0217  -0.0327 232 LEU A C   
1256 O O   . LEU A 157 ? 0.6023 0.6984 0.5691 0.0019  0.0205  -0.0379 232 LEU A O   
1257 C CB  . LEU A 157 ? 0.4678 0.5282 0.4281 -0.0023 0.0163  -0.0434 232 LEU A CB  
1258 C CG  . LEU A 157 ? 0.4444 0.4786 0.3945 -0.0088 0.0085  -0.0499 232 LEU A CG  
1259 C CD1 . LEU A 157 ? 0.4048 0.4364 0.3476 0.0002  0.0078  -0.0602 232 LEU A CD1 
1260 C CD2 . LEU A 157 ? 0.4523 0.4794 0.3921 -0.0276 0.0062  -0.0529 232 LEU A CD2 
1261 N N   . ASP A 158 ? 0.4894 0.5715 0.4665 -0.0001 0.0237  -0.0244 233 ASP A N   
1262 C CA  . ASP A 158 ? 0.4384 0.5309 0.4163 0.0071  0.0247  -0.0210 233 ASP A CA  
1263 C C   . ASP A 158 ? 0.4849 0.5688 0.4673 0.0051  0.0248  -0.0161 233 ASP A C   
1264 O O   . ASP A 158 ? 0.4902 0.5689 0.4727 0.0103  0.0252  -0.0077 233 ASP A O   
1265 C CB  . ASP A 158 ? 0.5434 0.6375 0.5145 0.0157  0.0281  -0.0140 233 ASP A CB  
1266 C CG  . ASP A 158 ? 0.7124 0.8101 0.6733 0.0242  0.0240  -0.0111 233 ASP A CG  
1267 O OD1 . ASP A 158 ? 0.8909 0.9967 0.8581 0.0265  0.0174  -0.0175 233 ASP A OD1 
1268 O OD2 . ASP A 158 ? 0.7714 0.8631 0.7172 0.0286  0.0274  -0.0026 233 ASP A OD2 
1269 N N   . VAL A 159 ? 0.4765 0.5545 0.4577 -0.0041 0.0250  -0.0215 234 VAL A N   
1270 C CA  . VAL A 159 ? 0.3805 0.4470 0.3600 -0.0064 0.0253  -0.0201 234 VAL A CA  
1271 C C   . VAL A 159 ? 0.5666 0.6475 0.5523 0.0016  0.0274  -0.0275 234 VAL A C   
1272 O O   . VAL A 159 ? 0.5815 0.6802 0.5732 -0.0016 0.0312  -0.0388 234 VAL A O   
1273 C CB  . VAL A 159 ? 0.4120 0.4615 0.3786 -0.0202 0.0254  -0.0232 234 VAL A CB  
1274 C CG1 . VAL A 159 ? 0.4834 0.5203 0.4417 -0.0224 0.0271  -0.0252 234 VAL A CG1 
1275 C CG2 . VAL A 159 ? 0.4488 0.4811 0.4127 -0.0235 0.0174  -0.0161 234 VAL A CG2 
1276 N N   . LYS A 160 ? 0.4805 0.5536 0.4671 0.0118  0.0241  -0.0219 235 LYS A N   
1277 C CA  . LYS A 160 ? 0.3639 0.4455 0.3580 0.0245  0.0219  -0.0294 235 LYS A CA  
1278 C C   . LYS A 160 ? 0.4327 0.4879 0.4194 0.0311  0.0171  -0.0212 235 LYS A C   
1279 O O   . LYS A 160 ? 0.4720 0.5094 0.4512 0.0245  0.0160  -0.0084 235 LYS A O   
1280 C CB  . LYS A 160 ? 0.4030 0.5043 0.4036 0.0357  0.0153  -0.0312 235 LYS A CB  
1281 C CG  . LYS A 160 ? 0.3452 0.4338 0.3306 0.0392  0.0109  -0.0167 235 LYS A CG  
1282 C CD  . LYS A 160 ? 0.4041 0.5073 0.3873 0.0500  0.0015  -0.0200 235 LYS A CD  
1283 C CE  . LYS A 160 ? 0.6696 0.7568 0.6275 0.0517  0.0001  -0.0060 235 LYS A CE  
1284 N NZ  . LYS A 160 ? 0.8422 0.9384 0.7893 0.0618  -0.0122 -0.0097 235 LYS A NZ  
1285 N N   . PRO A 161 ? 0.5266 0.5788 0.5179 0.0436  0.0140  -0.0296 236 PRO A N   
1286 C CA  . PRO A 161 ? 0.5643 0.5826 0.5446 0.0485  0.0079  -0.0227 236 PRO A CA  
1287 C C   . PRO A 161 ? 0.4844 0.4824 0.4524 0.0489  0.0012  -0.0038 236 PRO A C   
1288 O O   . PRO A 161 ? 0.6173 0.5864 0.5756 0.0419  -0.0009 0.0058  236 PRO A O   
1289 C CB  . PRO A 161 ? 0.4220 0.4444 0.4128 0.0679  0.0038  -0.0377 236 PRO A CB  
1290 C CG  . PRO A 161 ? 0.3878 0.4483 0.3969 0.0645  0.0149  -0.0557 236 PRO A CG  
1291 C CD  . PRO A 161 ? 0.4681 0.5477 0.4781 0.0528  0.0168  -0.0483 236 PRO A CD  
1292 N N   . ALA A 162 ? 0.4795 0.4905 0.4447 0.0546  -0.0017 0.0014  237 ALA A N   
1293 C CA  . ALA A 162 ? 0.3379 0.3275 0.2833 0.0523  -0.0043 0.0197  237 ALA A CA  
1294 C C   . ALA A 162 ? 0.5121 0.5037 0.4588 0.0337  0.0070  0.0291  237 ALA A C   
1295 O O   . ALA A 162 ? 0.5706 0.5446 0.5041 0.0264  0.0100  0.0437  237 ALA A O   
1296 C CB  . ALA A 162 ? 0.3912 0.3914 0.3256 0.0629  -0.0108 0.0215  237 ALA A CB  
1297 N N   . ASN A 163 ? 0.4763 0.4881 0.4387 0.0255  0.0131  0.0208  238 ASN A N   
1298 C CA  . ASN A 163 ? 0.4952 0.5127 0.4663 0.0120  0.0203  0.0264  238 ASN A CA  
1299 C C   . ASN A 163 ? 0.5148 0.5203 0.4956 0.0019  0.0172  0.0252  238 ASN A C   
1300 O O   . ASN A 163 ? 0.5077 0.5208 0.5023 -0.0074 0.0188  0.0270  238 ASN A O   
1301 C CB  . ASN A 163 ? 0.4872 0.5290 0.4650 0.0117  0.0247  0.0189  238 ASN A CB  
1302 C CG  . ASN A 163 ? 0.4790 0.5306 0.4441 0.0190  0.0271  0.0204  238 ASN A CG  
1303 O OD1 . ASN A 163 ? 0.5274 0.5665 0.4761 0.0218  0.0275  0.0304  238 ASN A OD1 
1304 N ND2 . ASN A 163 ? 0.4757 0.5443 0.4430 0.0206  0.0277  0.0107  238 ASN A ND2 
1305 N N   . ILE A 164 ? 0.5688 0.5551 0.5425 0.0049  0.0111  0.0204  239 ILE A N   
1306 C CA  . ILE A 164 ? 0.4368 0.4039 0.4112 -0.0049 0.0055  0.0189  239 ILE A CA  
1307 C C   . ILE A 164 ? 0.5630 0.5002 0.5299 -0.0063 0.0003  0.0270  239 ILE A C   
1308 O O   . ILE A 164 ? 0.5981 0.5204 0.5525 0.0061  -0.0024 0.0258  239 ILE A O   
1309 C CB  . ILE A 164 ? 0.5548 0.5183 0.5196 -0.0024 0.0046  0.0041  239 ILE A CB  
1310 C CG1 . ILE A 164 ? 0.5271 0.5138 0.4946 -0.0051 0.0099  -0.0019 239 ILE A CG1 
1311 C CG2 . ILE A 164 ? 0.4835 0.4207 0.4395 -0.0126 -0.0033 0.0020  239 ILE A CG2 
1312 C CD1 . ILE A 164 ? 0.5572 0.5424 0.5116 -0.0065 0.0142  -0.0159 239 ILE A CD1 
1313 N N   . PHE A 165 ? 0.4973 0.4245 0.4734 -0.0215 -0.0029 0.0347  240 PHE A N   
1314 C CA  . PHE A 165 ? 0.4577 0.3544 0.4272 -0.0289 -0.0069 0.0449  240 PHE A CA  
1315 C C   . PHE A 165 ? 0.5327 0.4033 0.5009 -0.0388 -0.0189 0.0394  240 PHE A C   
1316 O O   . PHE A 165 ? 0.5851 0.4678 0.5675 -0.0483 -0.0238 0.0353  240 PHE A O   
1317 C CB  . PHE A 165 ? 0.5355 0.4454 0.5194 -0.0431 0.0022  0.0594  240 PHE A CB  
1318 C CG  . PHE A 165 ? 0.4700 0.4011 0.4474 -0.0345 0.0142  0.0640  240 PHE A CG  
1319 C CD1 . PHE A 165 ? 0.4820 0.3906 0.4314 -0.0274 0.0146  0.0731  240 PHE A CD1 
1320 C CD2 . PHE A 165 ? 0.4967 0.4648 0.4915 -0.0327 0.0220  0.0587  240 PHE A CD2 
1321 C CE1 . PHE A 165 ? 0.5416 0.4659 0.4785 -0.0200 0.0227  0.0767  240 PHE A CE1 
1322 C CE2 . PHE A 165 ? 0.4638 0.4478 0.4483 -0.0252 0.0319  0.0608  240 PHE A CE2 
1323 C CZ  . PHE A 165 ? 0.5189 0.4818 0.4733 -0.0194 0.0323  0.0698  240 PHE A CZ  
1324 N N   . LEU A 166 ? 0.6104 0.4412 0.5590 -0.0354 -0.0263 0.0386  241 LEU A N   
1325 C CA  . LEU A 166 ? 0.6282 0.4272 0.5681 -0.0435 -0.0389 0.0306  241 LEU A CA  
1326 C C   . LEU A 166 ? 0.7112 0.5078 0.6713 -0.0681 -0.0455 0.0401  241 LEU A C   
1327 O O   . LEU A 166 ? 0.6781 0.4778 0.6503 -0.0798 -0.0394 0.0548  241 LEU A O   
1328 C CB  . LEU A 166 ? 0.6106 0.3635 0.5248 -0.0321 -0.0457 0.0264  241 LEU A CB  
1329 C CG  . LEU A 166 ? 0.7173 0.4666 0.6159 -0.0095 -0.0443 0.0066  241 LEU A CG  
1330 C CD1 . LEU A 166 ? 0.6950 0.4869 0.6045 0.0057  -0.0325 0.0043  241 LEU A CD1 
1331 C CD2 . LEU A 166 ? 0.8384 0.5390 0.7166 0.0038  -0.0535 0.0019  241 LEU A CD2 
1332 N N   . GLY A 167 ? 0.6808 0.4716 0.6436 -0.0772 -0.0583 0.0312  242 GLY A N   
1333 C CA  . GLY A 167 ? 0.4674 0.2566 0.4544 -0.1002 -0.0698 0.0366  242 GLY A CA  
1334 C C   . GLY A 167 ? 0.6819 0.4195 0.6462 -0.1086 -0.0870 0.0300  242 GLY A C   
1335 O O   . GLY A 167 ? 0.8176 0.5208 0.7462 -0.0941 -0.0885 0.0196  242 GLY A O   
1336 N N   . PRO A 168 ? 0.5404 0.2729 0.5275 -0.1322 -0.1005 0.0337  243 PRO A N   
1337 C CA  . PRO A 168 ? 0.6100 0.2890 0.5740 -0.1429 -0.1199 0.0263  243 PRO A CA  
1338 C C   . PRO A 168 ? 0.6625 0.3220 0.5941 -0.1333 -0.1340 0.0079  243 PRO A C   
1339 O O   . PRO A 168 ? 0.7135 0.4024 0.6509 -0.1289 -0.1361 0.0037  243 PRO A O   
1340 C CB  . PRO A 168 ? 0.6182 0.3112 0.6255 -0.1730 -0.1313 0.0339  243 PRO A CB  
1341 C CG  . PRO A 168 ? 0.5904 0.3376 0.6390 -0.1769 -0.1097 0.0480  243 PRO A CG  
1342 C CD  . PRO A 168 ? 0.6410 0.4177 0.6798 -0.1508 -0.0974 0.0438  243 PRO A CD  
1343 N N   . ARG A 169 ? 0.8296 0.4335 0.7216 -0.1305 -0.1436 -0.0035 244 ARG A N   
1344 C CA  . ARG A 169 ? 0.7801 0.3557 0.6300 -0.1235 -0.1547 -0.0230 244 ARG A CA  
1345 C C   . ARG A 169 ? 0.8162 0.4187 0.6492 -0.1025 -0.1367 -0.0303 244 ARG A C   
1346 O O   . ARG A 169 ? 0.7897 0.3951 0.6030 -0.1040 -0.1432 -0.0383 244 ARG A O   
1347 C CB  . ARG A 169 ? 0.7784 0.3560 0.6372 -0.1428 -0.1797 -0.0255 244 ARG A CB  
1348 C CG  . ARG A 169 ? 0.7347 0.2955 0.6061 -0.1582 -0.1930 -0.0231 244 ARG A CG  
1349 C CD  . ARG A 169 ? 0.8972 0.4691 0.7771 -0.1695 -0.2165 -0.0273 244 ARG A CD  
1350 N NE  . ARG A 169 ? 0.9520 0.5042 0.8407 -0.1851 -0.2301 -0.0277 244 ARG A NE  
1351 C CZ  . ARG A 169 ? 1.0999 0.6772 1.0401 -0.2046 -0.2309 -0.0164 244 ARG A CZ  
1352 N NH1 . ARG A 169 ? 1.0436 0.6682 1.0320 -0.2100 -0.2176 -0.0038 244 ARG A NH1 
1353 N NH2 . ARG A 169 ? 1.1075 0.6624 1.0507 -0.2202 -0.2435 -0.0186 244 ARG A NH2 
1354 N N   . GLY A 170 ? 0.7110 0.3307 0.5496 -0.0845 -0.1154 -0.0269 245 GLY A N   
1355 C CA  . GLY A 170 ? 0.6679 0.3108 0.4917 -0.0660 -0.0975 -0.0366 245 GLY A CA  
1356 C C   . GLY A 170 ? 0.7729 0.4642 0.6180 -0.0684 -0.0907 -0.0283 245 GLY A C   
1357 O O   . GLY A 170 ? 0.9501 0.6579 0.7803 -0.0580 -0.0769 -0.0364 245 GLY A O   
1358 N N   . ARG A 171 ? 0.8098 0.5247 0.6907 -0.0821 -0.0992 -0.0139 246 ARG A N   
1359 C CA  . ARG A 171 ? 0.6783 0.4364 0.5814 -0.0812 -0.0937 -0.0073 246 ARG A CA  
1360 C C   . ARG A 171 ? 0.7510 0.5426 0.6773 -0.0702 -0.0734 0.0018  246 ARG A C   
1361 O O   . ARG A 171 ? 0.7903 0.5708 0.7151 -0.0639 -0.0660 0.0049  246 ARG A O   
1362 C CB  . ARG A 171 ? 0.7073 0.4797 0.6435 -0.0973 -0.1126 0.0002  246 ARG A CB  
1363 C CG  . ARG A 171 ? 0.8240 0.5596 0.7404 -0.1104 -0.1393 -0.0076 246 ARG A CG  
1364 C CD  . ARG A 171 ? 0.9144 0.6263 0.7808 -0.1066 -0.1468 -0.0188 246 ARG A CD  
1365 N NE  . ARG A 171 ? 1.0176 0.7564 0.8895 -0.1017 -0.1450 -0.0147 246 ARG A NE  
1366 C CZ  . ARG A 171 ? 1.1566 0.9202 1.0658 -0.1059 -0.1612 -0.0076 246 ARG A CZ  
1367 N NH1 . ARG A 171 ? 0.9576 0.7349 0.9126 -0.1164 -0.1771 -0.0034 246 ARG A NH1 
1368 N NH2 . ARG A 171 ? 1.0069 0.7823 0.9099 -0.0994 -0.1614 -0.0056 246 ARG A NH2 
1369 N N   . CYS A 172 ? 0.6036 0.4316 0.5473 -0.0673 -0.0666 0.0058  247 CYS A N   
1370 C CA  . CYS A 172 ? 0.7316 0.5910 0.6943 -0.0581 -0.0494 0.0135  247 CYS A CA  
1371 C C   . CYS A 172 ? 0.5825 0.4768 0.5719 -0.0605 -0.0488 0.0180  247 CYS A C   
1372 O O   . CYS A 172 ? 0.6127 0.5046 0.6016 -0.0655 -0.0624 0.0143  247 CYS A O   
1373 C CB  . CYS A 172 ? 0.6241 0.4858 0.5656 -0.0418 -0.0360 0.0051  247 CYS A CB  
1374 S SG  . CYS A 172 ? 0.7717 0.6424 0.6931 -0.0405 -0.0324 -0.0063 247 CYS A SG  
1375 N N   . LYS A 173 ? 0.5444 0.4668 0.5536 -0.0558 -0.0347 0.0253  248 LYS A N   
1376 C CA  . LYS A 173 ? 0.5005 0.4565 0.5378 -0.0555 -0.0319 0.0277  248 LYS A CA  
1377 C C   . LYS A 173 ? 0.5211 0.4965 0.5518 -0.0432 -0.0159 0.0274  248 LYS A C   
1378 O O   . LYS A 173 ? 0.5249 0.4991 0.5465 -0.0384 -0.0055 0.0317  248 LYS A O   
1379 C CB  . LYS A 173 ? 0.4661 0.4417 0.5420 -0.0667 -0.0297 0.0357  248 LYS A CB  
1380 C CG  . LYS A 173 ? 0.5199 0.4769 0.6066 -0.0824 -0.0450 0.0370  248 LYS A CG  
1381 C CD  . LYS A 173 ? 0.5502 0.5382 0.6860 -0.0964 -0.0409 0.0427  248 LYS A CD  
1382 C CE  . LYS A 173 ? 0.8903 0.8556 1.0293 -0.1157 -0.0449 0.0490  248 LYS A CE  
1383 N NZ  . LYS A 173 ? 0.8897 0.8311 0.9967 -0.1150 -0.0286 0.0587  248 LYS A NZ  
1384 N N   . LEU A 174 ? 0.3770 0.3662 0.4102 -0.0385 -0.0170 0.0224  249 LEU A N   
1385 C CA  . LEU A 174 ? 0.3182 0.3263 0.3480 -0.0290 -0.0041 0.0209  249 LEU A CA  
1386 C C   . LEU A 174 ? 0.4372 0.4690 0.4898 -0.0285 0.0074  0.0272  249 LEU A C   
1387 O O   . LEU A 174 ? 0.4578 0.5025 0.5398 -0.0350 0.0058  0.0295  249 LEU A O   
1388 C CB  . LEU A 174 ? 0.3710 0.3804 0.3955 -0.0267 -0.0098 0.0142  249 LEU A CB  
1389 C CG  . LEU A 174 ? 0.4762 0.5003 0.4944 -0.0191 0.0005  0.0103  249 LEU A CG  
1390 C CD1 . LEU A 174 ? 0.4339 0.4556 0.4316 -0.0161 0.0078  0.0067  249 LEU A CD1 
1391 C CD2 . LEU A 174 ? 0.4137 0.4300 0.4258 -0.0199 -0.0081 0.0052  249 LEU A CD2 
1392 N N   . GLY A 175 ? 0.5140 0.5631 0.4498 -0.0828 0.0625  0.0986  250 GLY A N   
1393 C CA  . GLY A 175 ? 0.4572 0.5252 0.3875 -0.0897 0.0849  0.1035  250 GLY A CA  
1394 C C   . GLY A 175 ? 0.4297 0.4968 0.3359 -0.0686 0.0932  0.0963  250 GLY A C   
1395 O O   . GLY A 175 ? 0.5215 0.5797 0.4263 -0.0481 0.0810  0.0864  250 GLY A O   
1396 N N   . ASP A 176 ? 0.5573 0.6334 0.4411 -0.0772 0.1146  0.1010  251 ASP A N   
1397 C CA  . ASP A 176 ? 0.5204 0.5973 0.3732 -0.0617 0.1242  0.0926  251 ASP A CA  
1398 C C   . ASP A 176 ? 0.5539 0.6620 0.4445 -0.0386 0.1234  0.0708  251 ASP A C   
1399 O O   . ASP A 176 ? 0.5907 0.6790 0.4772 -0.0214 0.1051  0.0634  251 ASP A O   
1400 C CB  . ASP A 176 ? 0.8062 0.8315 0.6062 -0.0521 0.1060  0.0995  251 ASP A CB  
1401 C CG  . ASP A 176 ? 0.9125 0.9318 0.6627 -0.0467 0.1148  0.0975  251 ASP A CG  
1402 O OD1 . ASP A 176 ? 0.9036 0.9575 0.6641 -0.0404 0.1323  0.0809  251 ASP A OD1 
1403 O OD2 . ASP A 176 ? 0.9875 0.9692 0.6973 -0.0439 0.1001  0.1098  251 ASP A OD2 
1404 N N   . PHE A 177 ? 0.5330 0.6894 0.4634 -0.0383 0.1437  0.0599  252 PHE A N   
1405 C CA  . PHE A 177 ? 0.4457 0.6267 0.4156 -0.0142 0.1428  0.0384  252 PHE A CA  
1406 C C   . PHE A 177 ? 0.4255 0.6115 0.3656 -0.0026 0.1626  0.0203  252 PHE A C   
1407 O O   . PHE A 177 ? 0.4777 0.6944 0.4548 0.0140  0.1745  -0.0011 252 PHE A O   
1408 C CB  . PHE A 177 ? 0.3493 0.5816 0.3921 -0.0149 0.1481  0.0340  252 PHE A CB  
1409 C CG  . PHE A 177 ? 0.3156 0.5426 0.3819 -0.0292 0.1257  0.0501  252 PHE A CG  
1410 C CD1 . PHE A 177 ? 0.5202 0.7170 0.5855 -0.0195 0.0967  0.0527  252 PHE A CD1 
1411 C CD2 . PHE A 177 ? 0.5882 0.8395 0.6736 -0.0555 0.1344  0.0616  252 PHE A CD2 
1412 C CE1 . PHE A 177 ? 0.5004 0.6902 0.5774 -0.0340 0.0769  0.0647  252 PHE A CE1 
1413 C CE2 . PHE A 177 ? 0.5329 0.7760 0.6347 -0.0703 0.1116  0.0732  252 PHE A CE2 
1414 C CZ  . PHE A 177 ? 0.3602 0.5718 0.4548 -0.0586 0.0828  0.0738  252 PHE A CZ  
1415 N N   . GLY A 178 ? 0.4044 0.5580 0.2764 -0.0099 0.1641  0.0275  253 GLY A N   
1416 C CA  . GLY A 178 ? 0.4633 0.6172 0.2937 -0.0021 0.1802  0.0099  253 GLY A CA  
1417 C C   . GLY A 178 ? 0.4913 0.6281 0.3244 0.0217  0.1624  -0.0113 253 GLY A C   
1418 O O   . GLY A 178 ? 0.6550 0.7980 0.4700 0.0318  0.1764  -0.0348 253 GLY A O   
1419 N N   . LEU A 179 ? 0.3939 0.5076 0.2462 0.0282  0.1333  -0.0047 254 LEU A N   
1420 C CA  . LEU A 179 ? 0.5533 0.6492 0.4119 0.0452  0.1160  -0.0223 254 LEU A CA  
1421 C C   . LEU A 179 ? 0.4416 0.5486 0.3628 0.0577  0.1094  -0.0302 254 LEU A C   
1422 O O   . LEU A 179 ? 0.5419 0.6305 0.4710 0.0701  0.0969  -0.0448 254 LEU A O   
1423 C CB  . LEU A 179 ? 0.4869 0.5500 0.3217 0.0423  0.0888  -0.0109 254 LEU A CB  
1424 C CG  . LEU A 179 ? 0.6205 0.6639 0.3960 0.0348  0.0829  -0.0003 254 LEU A CG  
1425 C CD1 . LEU A 179 ? 0.7057 0.7283 0.4724 0.0412  0.0558  -0.0045 254 LEU A CD1 
1426 C CD2 . LEU A 179 ? 0.6865 0.7359 0.4146 0.0321  0.1026  -0.0102 254 LEU A CD2 
1427 N N   . LEU A 180 ? 0.6060 0.7395 0.5705 0.0532  0.1142  -0.0194 255 LEU A N   
1428 C CA  . LEU A 180 ? 0.4118 0.5540 0.4338 0.0657  0.1018  -0.0226 255 LEU A CA  
1429 C C   . LEU A 180 ? 0.4994 0.6495 0.5457 0.0884  0.1114  -0.0502 255 LEU A C   
1430 O O   . LEU A 180 ? 0.5218 0.6988 0.5654 0.0926  0.1388  -0.0671 255 LEU A O   
1431 C CB  . LEU A 180 ? 0.4358 0.6138 0.5011 0.0562  0.1049  -0.0088 255 LEU A CB  
1432 C CG  . LEU A 180 ? 0.2809 0.4751 0.4098 0.0694  0.0884  -0.0090 255 LEU A CG  
1433 C CD1 . LEU A 180 ? 0.3318 0.5377 0.4774 0.0508  0.0744  0.0129  255 LEU A CD1 
1434 C CD2 . LEU A 180 ? 0.4398 0.6793 0.6230 0.0882  0.1075  -0.0298 255 LEU A CD2 
1435 N N   . VAL A 181 ? 0.4941 0.6171 0.5611 0.1022  0.0901  -0.0554 256 VAL A N   
1436 C CA  . VAL A 181 ? 0.4166 0.5363 0.5129 0.1269  0.0941  -0.0820 256 VAL A CA  
1437 C C   . VAL A 181 ? 0.4919 0.6106 0.6476 0.1404  0.0722  -0.0732 256 VAL A C   
1438 O O   . VAL A 181 ? 0.4263 0.5311 0.5821 0.1279  0.0494  -0.0478 256 VAL A O   
1439 C CB  . VAL A 181 ? 0.4523 0.5253 0.5088 0.1308  0.0856  -0.0994 256 VAL A CB  
1440 C CG1 . VAL A 181 ? 0.7752 0.8452 0.7676 0.1147  0.0959  -0.1009 256 VAL A CG1 
1441 C CG2 . VAL A 181 ? 0.4328 0.4642 0.4918 0.1252  0.0546  -0.0835 256 VAL A CG2 
1442 N N   . GLU A 182 ? 0.4459 0.5790 0.6507 0.1671  0.0786  -0.0951 257 GLU A N   
1443 C CA  . GLU A 182 ? 0.4737 0.6027 0.7387 0.1859  0.0532  -0.0877 257 GLU A CA  
1444 C C   . GLU A 182 ? 0.5640 0.6294 0.8211 0.2015  0.0332  -0.0986 257 GLU A C   
1445 O O   . GLU A 182 ? 0.6621 0.7113 0.9062 0.2148  0.0487  -0.1295 257 GLU A O   
1446 C CB  . GLU A 182 ? 0.3836 0.5732 0.7221 0.2091  0.0703  -0.1052 257 GLU A CB  
1447 C CG  . GLU A 182 ? 0.5047 0.6964 0.9131 0.2311  0.0380  -0.0948 257 GLU A CG  
1448 C CD  . GLU A 182 ? 0.6296 0.8887 1.1099 0.2494  0.0543  -0.1080 257 GLU A CD  
1449 O OE1 . GLU A 182 ? 0.9118 1.2115 1.3856 0.2455  0.0949  -0.1277 257 GLU A OE1 
1450 O OE2 . GLU A 182 ? 0.7449 1.0116 1.2733 0.2620  0.0260  -0.0934 257 GLU A OE2 
1451 N N   . LEU A 183 ? 0.4887 0.5143 0.7478 0.1967  -0.0010 -0.0733 258 LEU A N   
1452 C CA  . LEU A 183 ? 0.6161 0.5732 0.8637 0.2047  -0.0223 -0.0775 258 LEU A CA  
1453 C C   . LEU A 183 ? 0.6864 0.6347 0.9945 0.2439  -0.0293 -0.0984 258 LEU A C   
1454 O O   . LEU A 183 ? 0.8125 0.7906 1.1739 0.2591  -0.0415 -0.0870 258 LEU A O   
1455 C CB  . LEU A 183 ? 0.6617 0.5792 0.8866 0.1832  -0.0539 -0.0410 258 LEU A CB  
1456 C CG  . LEU A 183 ? 0.5541 0.4782 0.7245 0.1479  -0.0464 -0.0243 258 LEU A CG  
1457 C CD1 . LEU A 183 ? 0.6883 0.5783 0.8370 0.1269  -0.0727 0.0084  258 LEU A CD1 
1458 C CD2 . LEU A 183 ? 0.5453 0.4501 0.6750 0.1384  -0.0314 -0.0448 258 LEU A CD2 
1459 N N   . GLY A 184 ? 0.7100 0.6177 1.0048 0.2568  -0.0219 -0.1281 259 GLY A N   
1460 C CA  . GLY A 184 ? 0.6427 0.5379 0.9705 0.2828  -0.0218 -0.1432 259 GLY A CA  
1461 C C   . GLY A 184 ? 0.9109 0.8365 1.2371 0.2962  0.0171  -0.1828 259 GLY A C   
1462 O O   . GLY A 184 ? 1.0570 1.0331 1.3666 0.2858  0.0465  -0.1933 259 GLY A O   
1463 N N   . GLU A 190 ? 1.1450 1.1489 0.9915 0.1501  0.1490  -0.2510 265 GLU A N   
1464 C CA  . GLU A 190 ? 1.0571 1.1022 0.9555 0.1534  0.1545  -0.2259 265 GLU A CA  
1465 C C   . GLU A 190 ? 0.9256 0.9652 0.8072 0.1305  0.1307  -0.1855 265 GLU A C   
1466 O O   . GLU A 190 ? 1.1534 1.2236 1.0442 0.1202  0.1390  -0.1594 265 GLU A O   
1467 C CB  . GLU A 190 ? 1.3086 1.3466 1.2855 0.1761  0.1436  -0.2292 265 GLU A CB  
1468 C CG  . GLU A 190 ? 1.4056 1.3852 1.3873 0.1763  0.1079  -0.2270 265 GLU A CG  
1469 C CD  . GLU A 190 ? 1.4015 1.3659 1.4529 0.1976  0.0932  -0.2238 265 GLU A CD  
1470 O OE1 . GLU A 190 ? 1.5316 1.5361 1.6348 0.2162  0.1089  -0.2267 265 GLU A OE1 
1471 O OE2 . GLU A 190 ? 1.2295 1.1424 1.2848 0.1947  0.0646  -0.2172 265 GLU A OE2 
1472 N N   . VAL A 191 ? 0.8229 0.8244 0.6828 0.1222  0.1021  -0.1829 266 VAL A N   
1473 C CA  . VAL A 191 ? 0.6661 0.6632 0.5172 0.1041  0.0799  -0.1507 266 VAL A CA  
1474 C C   . VAL A 191 ? 0.9420 0.9375 0.7272 0.0907  0.0763  -0.1497 266 VAL A C   
1475 O O   . VAL A 191 ? 1.0111 0.9888 0.7567 0.0912  0.0726  -0.1753 266 VAL A O   
1476 C CB  . VAL A 191 ? 0.8179 0.7818 0.6949 0.1011  0.0520  -0.1470 266 VAL A CB  
1477 C CG1 . VAL A 191 ? 0.9011 0.8669 0.7686 0.0831  0.0339  -0.1206 266 VAL A CG1 
1478 C CG2 . VAL A 191 ? 0.9498 0.9096 0.8845 0.1131  0.0502  -0.1401 266 VAL A CG2 
1479 N N   . GLN A 192 ? 0.7913 0.8012 0.5626 0.0792  0.0743  -0.1206 267 GLN A N   
1480 C CA  . GLN A 192 ? 0.7349 0.7403 0.4449 0.0686  0.0663  -0.1128 267 GLN A CA  
1481 C C   . GLN A 192 ? 0.8187 0.8146 0.5380 0.0617  0.0360  -0.0937 267 GLN A C   
1482 O O   . GLN A 192 ? 0.7180 0.7138 0.4857 0.0616  0.0275  -0.0845 267 GLN A O   
1483 C CB  . GLN A 192 ? 0.9162 0.9405 0.5986 0.0611  0.0892  -0.0945 267 GLN A CB  
1484 C CG  . GLN A 192 ? 0.9206 0.9671 0.6029 0.0661  0.1256  -0.1142 267 GLN A CG  
1485 C CD  . GLN A 192 ? 1.1302 1.1979 0.7952 0.0514  0.1501  -0.0925 267 GLN A CD  
1486 O OE1 . GLN A 192 ? 1.4660 1.5159 1.0717 0.0341  0.1519  -0.0820 267 GLN A OE1 
1487 N NE2 . GLN A 192 ? 1.1103 1.2070 0.8333 0.0526  0.1646  -0.0826 267 GLN A NE2 
1488 N N   . GLU A 193 ? 0.9962 0.9855 0.6674 0.0562  0.0196  -0.0883 268 GLU A N   
1489 C CA  . GLU A 193 ? 0.8257 0.8128 0.5106 0.0531  -0.0095 -0.0744 268 GLU A CA  
1490 C C   . GLU A 193 ? 0.6608 0.6548 0.3714 0.0521  -0.0054 -0.0461 268 GLU A C   
1491 O O   . GLU A 193 ? 0.9428 0.9347 0.6235 0.0494  0.0047  -0.0288 268 GLU A O   
1492 C CB  . GLU A 193 ? 1.0037 0.9830 0.6319 0.0509  -0.0320 -0.0745 268 GLU A CB  
1493 C CG  . GLU A 193 ? 1.3286 1.2978 0.9171 0.0491  -0.0371 -0.1051 268 GLU A CG  
1494 C CD  . GLU A 193 ? 1.2111 1.1786 0.8363 0.0462  -0.0611 -0.1245 268 GLU A CD  
1495 O OE1 . GLU A 193 ? 1.0475 1.0266 0.7259 0.0447  -0.0736 -0.1123 268 GLU A OE1 
1496 O OE2 . GLU A 193 ? 1.2122 1.1662 0.8116 0.0433  -0.0660 -0.1535 268 GLU A OE2 
1497 N N   . GLY A 194 ? 0.7938 0.7929 0.5553 0.0517  -0.0126 -0.0419 269 GLY A N   
1498 C CA  . GLY A 194 ? 0.6788 0.6812 0.4618 0.0504  -0.0109 -0.0203 269 GLY A CA  
1499 C C   . GLY A 194 ? 0.7266 0.7287 0.5083 0.0535  -0.0332 -0.0118 269 GLY A C   
1500 O O   . GLY A 194 ? 0.7946 0.7976 0.5595 0.0564  -0.0533 -0.0199 269 GLY A O   
1501 N N   . ASP A 195 ? 0.7750 0.7763 0.5771 0.0542  -0.0312 0.0029  270 ASP A N   
1502 C CA  . ASP A 195 ? 0.6659 0.6679 0.4774 0.0621  -0.0507 0.0087  270 ASP A CA  
1503 C C   . ASP A 195 ? 0.5861 0.6111 0.4462 0.0609  -0.0580 -0.0055 270 ASP A C   
1504 O O   . ASP A 195 ? 0.6413 0.6720 0.5295 0.0532  -0.0436 -0.0073 270 ASP A O   
1505 C CB  . ASP A 195 ? 0.5941 0.5810 0.4068 0.0637  -0.0438 0.0258  270 ASP A CB  
1506 C CG  . ASP A 195 ? 0.6387 0.6149 0.4488 0.0775  -0.0656 0.0337  270 ASP A CG  
1507 O OD1 . ASP A 195 ? 0.7554 0.7518 0.5939 0.0866  -0.0836 0.0226  270 ASP A OD1 
1508 O OD2 . ASP A 195 ? 0.7844 0.7317 0.5677 0.0793  -0.0659 0.0512  270 ASP A OD2 
1509 N N   . PRO A 196 ? 0.6534 0.6936 0.5240 0.0658  -0.0806 -0.0150 271 PRO A N   
1510 C CA  . PRO A 196 ? 0.5634 0.6323 0.4859 0.0596  -0.0843 -0.0292 271 PRO A CA  
1511 C C   . PRO A 196 ? 0.5815 0.6649 0.5435 0.0630  -0.0753 -0.0261 271 PRO A C   
1512 O O   . PRO A 196 ? 0.5823 0.6871 0.5817 0.0513  -0.0657 -0.0354 271 PRO A O   
1513 C CB  . PRO A 196 ? 0.6311 0.7173 0.5568 0.0647  -0.1144 -0.0393 271 PRO A CB  
1514 C CG  . PRO A 196 ? 0.6994 0.7643 0.5795 0.0796  -0.1296 -0.0243 271 PRO A CG  
1515 C CD  . PRO A 196 ? 0.6961 0.7299 0.5310 0.0747  -0.1054 -0.0125 271 PRO A CD  
1516 N N   . ARG A 197 ? 0.5827 0.6517 0.5342 0.0769  -0.0769 -0.0143 272 ARG A N   
1517 C CA  . ARG A 197 ? 0.4402 0.5195 0.4267 0.0822  -0.0668 -0.0167 272 ARG A CA  
1518 C C   . ARG A 197 ? 0.5079 0.5822 0.4955 0.0652  -0.0402 -0.0163 272 ARG A C   
1519 O O   . ARG A 197 ? 0.5431 0.6371 0.5619 0.0599  -0.0276 -0.0254 272 ARG A O   
1520 C CB  . ARG A 197 ? 0.5815 0.6327 0.5499 0.1005  -0.0753 -0.0043 272 ARG A CB  
1521 C CG  . ARG A 197 ? 0.7314 0.7845 0.7005 0.1205  -0.1074 -0.0017 272 ARG A CG  
1522 C CD  . ARG A 197 ? 0.6722 0.6814 0.6112 0.1362  -0.1177 0.0163  272 ARG A CD  
1523 N NE  . ARG A 197 ? 0.8110 0.7816 0.6885 0.1222  -0.1078 0.0347  272 ARG A NE  
1524 C CZ  . ARG A 197 ? 0.9418 0.8668 0.7803 0.1262  -0.1131 0.0548  272 ARG A CZ  
1525 N NH1 . ARG A 197 ? 1.0235 0.9261 0.8742 0.1473  -0.1315 0.0599  272 ARG A NH1 
1526 N NH2 . ARG A 197 ? 0.9885 0.8894 0.7774 0.1084  -0.0991 0.0696  272 ARG A NH2 
1527 N N   . TYR A 198 ? 0.6408 0.6911 0.5945 0.0562  -0.0316 -0.0062 273 TYR A N   
1528 C CA  . TYR A 198 ? 0.5318 0.5742 0.4831 0.0418  -0.0132 -0.0025 273 TYR A CA  
1529 C C   . TYR A 198 ? 0.5689 0.6139 0.5223 0.0286  -0.0103 -0.0056 273 TYR A C   
1530 O O   . TYR A 198 ? 0.6246 0.6587 0.5724 0.0185  -0.0008 0.0008  273 TYR A O   
1531 C CB  . TYR A 198 ? 0.5485 0.5648 0.4707 0.0423  -0.0075 0.0114  273 TYR A CB  
1532 C CG  . TYR A 198 ? 0.4471 0.4468 0.3602 0.0544  -0.0132 0.0167  273 TYR A CG  
1533 C CD1 . TYR A 198 ? 0.5037 0.4906 0.3955 0.0657  -0.0276 0.0242  273 TYR A CD1 
1534 C CD2 . TYR A 198 ? 0.5126 0.5031 0.4331 0.0541  -0.0055 0.0142  273 TYR A CD2 
1535 C CE1 . TYR A 198 ? 0.6276 0.5892 0.5086 0.0774  -0.0365 0.0323  273 TYR A CE1 
1536 C CE2 . TYR A 198 ? 0.6135 0.5795 0.5265 0.0670  -0.0124 0.0176  273 TYR A CE2 
1537 C CZ  . TYR A 198 ? 0.5386 0.4883 0.4334 0.0791  -0.0290 0.0283  273 TYR A CZ  
1538 O OH  . TYR A 198 ? 0.7910 0.7066 0.6759 0.0924  -0.0394 0.0350  273 TYR A OH  
1539 N N   . MET A 199 ? 0.6103 0.6660 0.5716 0.0287  -0.0216 -0.0155 274 MET A N   
1540 C CA  . MET A 199 ? 0.4242 0.4717 0.3842 0.0184  -0.0215 -0.0205 274 MET A CA  
1541 C C   . MET A 199 ? 0.6269 0.6793 0.6096 0.0000  -0.0141 -0.0217 274 MET A C   
1542 O O   . MET A 199 ? 0.5284 0.6056 0.5373 -0.0068 -0.0134 -0.0286 274 MET A O   
1543 C CB  . MET A 199 ? 0.4948 0.5478 0.4508 0.0220  -0.0379 -0.0336 274 MET A CB  
1544 C CG  . MET A 199 ? 0.6977 0.7346 0.6499 0.0131  -0.0395 -0.0435 274 MET A CG  
1545 S SD  . MET A 199 ? 0.8686 0.9049 0.7984 0.0186  -0.0591 -0.0615 274 MET A SD  
1546 C CE  . MET A 199 ? 0.7580 0.8318 0.7199 0.0175  -0.0781 -0.0655 274 MET A CE  
1547 N N   . ALA A 200 ? 0.5620 0.5920 0.5356 -0.0084 -0.0087 -0.0142 275 ALA A N   
1548 C CA  . ALA A 200 ? 0.4535 0.4773 0.4372 -0.0293 -0.0041 -0.0110 275 ALA A CA  
1549 C C   . ALA A 200 ? 0.5614 0.5894 0.5625 -0.0407 -0.0128 -0.0239 275 ALA A C   
1550 O O   . ALA A 200 ? 0.5946 0.6147 0.5906 -0.0318 -0.0243 -0.0347 275 ALA A O   
1551 C CB  . ALA A 200 ? 0.5835 0.5755 0.5522 -0.0324 -0.0043 0.0019  275 ALA A CB  
1552 N N   . PRO A 201 ? 0.4377 0.4783 0.4574 -0.0635 -0.0064 -0.0244 276 PRO A N   
1553 C CA  . PRO A 201 ? 0.4513 0.5030 0.4948 -0.0787 -0.0154 -0.0382 276 PRO A CA  
1554 C C   . PRO A 201 ? 0.5558 0.5639 0.5862 -0.0851 -0.0269 -0.0406 276 PRO A C   
1555 O O   . PRO A 201 ? 0.6237 0.6336 0.6644 -0.0891 -0.0405 -0.0571 276 PRO A O   
1556 C CB  . PRO A 201 ? 0.4097 0.4853 0.4750 -0.1064 0.0007  -0.0351 276 PRO A CB  
1557 C CG  . PRO A 201 ? 0.4517 0.5038 0.4871 -0.1104 0.0146  -0.0164 276 PRO A CG  
1558 C CD  . PRO A 201 ? 0.4985 0.5449 0.5158 -0.0803 0.0107  -0.0136 276 PRO A CD  
1559 N N   . GLU A 202 ? 0.5709 0.5379 0.5796 -0.0846 -0.0246 -0.0262 277 GLU A N   
1560 C CA  . GLU A 202 ? 0.5968 0.5163 0.5976 -0.0869 -0.0363 -0.0300 277 GLU A CA  
1561 C C   . GLU A 202 ? 0.6206 0.5310 0.6106 -0.0593 -0.0442 -0.0460 277 GLU A C   
1562 O O   . GLU A 202 ? 0.7593 0.6316 0.7447 -0.0573 -0.0533 -0.0570 277 GLU A O   
1563 C CB  . GLU A 202 ? 0.6032 0.4805 0.5887 -0.0931 -0.0355 -0.0079 277 GLU A CB  
1564 C CG  . GLU A 202 ? 0.7674 0.6427 0.7411 -0.0675 -0.0339 0.0021  277 GLU A CG  
1565 C CD  . GLU A 202 ? 0.7984 0.7079 0.7663 -0.0689 -0.0214 0.0134  277 GLU A CD  
1566 O OE1 . GLU A 202 ? 0.8340 0.7714 0.8090 -0.0858 -0.0116 0.0111  277 GLU A OE1 
1567 O OE2 . GLU A 202 ? 0.6588 0.5686 0.6184 -0.0534 -0.0210 0.0223  277 GLU A OE2 
1568 N N   . LEU A 203 ? 0.6165 0.5574 0.5993 -0.0393 -0.0397 -0.0483 278 LEU A N   
1569 C CA  . LEU A 203 ? 0.5178 0.4533 0.4832 -0.0179 -0.0431 -0.0636 278 LEU A CA  
1570 C C   . LEU A 203 ? 0.6175 0.5559 0.5794 -0.0234 -0.0568 -0.0865 278 LEU A C   
1571 O O   . LEU A 203 ? 0.7124 0.6317 0.6542 -0.0123 -0.0607 -0.1047 278 LEU A O   
1572 C CB  . LEU A 203 ? 0.5502 0.5126 0.5028 -0.0008 -0.0346 -0.0559 278 LEU A CB  
1573 C CG  . LEU A 203 ? 0.6908 0.6509 0.6446 0.0054  -0.0234 -0.0370 278 LEU A CG  
1574 C CD1 . LEU A 203 ? 0.6135 0.5918 0.5515 0.0203  -0.0156 -0.0336 278 LEU A CD1 
1575 C CD2 . LEU A 203 ? 0.6969 0.6259 0.6566 0.0104  -0.0245 -0.0367 278 LEU A CD2 
1576 N N   . LEU A 204 ? 0.6199 0.5850 0.6024 -0.0408 -0.0642 -0.0884 279 LEU A N   
1577 C CA  . LEU A 204 ? 0.5503 0.5204 0.5346 -0.0500 -0.0826 -0.1106 279 LEU A CA  
1578 C C   . LEU A 204 ? 0.5917 0.5164 0.5765 -0.0662 -0.0895 -0.1236 279 LEU A C   
1579 O O   . LEU A 204 ? 0.8649 0.7768 0.8372 -0.0692 -0.1048 -0.1475 279 LEU A O   
1580 C CB  . LEU A 204 ? 0.6721 0.6903 0.6923 -0.0649 -0.0897 -0.1101 279 LEU A CB  
1581 C CG  . LEU A 204 ? 0.7558 0.8140 0.7777 -0.0455 -0.0899 -0.1023 279 LEU A CG  
1582 C CD1 . LEU A 204 ? 0.6282 0.7367 0.6965 -0.0570 -0.1004 -0.1083 279 LEU A CD1 
1583 C CD2 . LEU A 204 ? 0.7970 0.8460 0.7767 -0.0244 -0.1016 -0.1096 279 LEU A CD2 
1584 N N   . GLN A 205 ? 0.6838 0.5787 0.6786 -0.0778 -0.0808 -0.1082 280 GLN A N   
1585 C CA  . GLN A 205 ? 0.7142 0.5523 0.7072 -0.0914 -0.0887 -0.1163 280 GLN A CA  
1586 C C   . GLN A 205 ? 0.6845 0.4788 0.6567 -0.0638 -0.0862 -0.1230 280 GLN A C   
1587 O O   . GLN A 205 ? 0.9836 0.7215 0.9559 -0.0683 -0.0929 -0.1272 280 GLN A O   
1588 C CB  . GLN A 205 ? 0.7813 0.6024 0.7908 -0.1199 -0.0832 -0.0929 280 GLN A CB  
1589 C CG  . GLN A 205 ? 0.8303 0.7094 0.8641 -0.1403 -0.0733 -0.0813 280 GLN A CG  
1590 C CD  . GLN A 205 ? 1.1516 1.0715 1.2115 -0.1567 -0.0848 -0.1022 280 GLN A CD  
1591 O OE1 . GLN A 205 ? 1.0036 0.8971 1.0627 -0.1686 -0.1014 -0.1219 280 GLN A OE1 
1592 N NE2 . GLN A 205 ? 1.0094 0.9939 1.0952 -0.1564 -0.0783 -0.0999 280 GLN A NE2 
1593 N N   . GLY A 206 ? 0.6767 0.4952 0.6342 -0.0358 -0.0763 -0.1241 281 GLY A N   
1594 C CA  . GLY A 206 ? 0.6920 0.4827 0.6388 -0.0089 -0.0697 -0.1340 281 GLY A CA  
1595 C C   . GLY A 206 ? 0.6587 0.4245 0.6223 -0.0015 -0.0660 -0.1115 281 GLY A C   
1596 O O   . GLY A 206 ? 0.8704 0.6000 0.8387 0.0176  -0.0671 -0.1219 281 GLY A O   
1597 N N   . SER A 207 ? 0.7008 0.4852 0.6733 -0.0151 -0.0630 -0.0824 282 SER A N   
1598 C CA  . SER A 207 ? 0.6210 0.3824 0.6024 -0.0120 -0.0644 -0.0573 282 SER A CA  
1599 C C   . SER A 207 ? 0.7405 0.5440 0.7232 0.0056  -0.0525 -0.0450 282 SER A C   
1600 O O   . SER A 207 ? 0.7002 0.5345 0.6789 -0.0064 -0.0463 -0.0286 282 SER A O   
1601 C CB  . SER A 207 ? 0.7963 0.5432 0.7768 -0.0453 -0.0688 -0.0341 282 SER A CB  
1602 O OG  . SER A 207 ? 0.9672 0.6866 0.9455 -0.0441 -0.0743 -0.0074 282 SER A OG  
1603 N N   . TYR A 208 ? 0.7806 0.5855 0.7714 0.0332  -0.0482 -0.0554 283 TYR A N   
1604 C CA  . TYR A 208 ? 0.6065 0.4523 0.6025 0.0473  -0.0364 -0.0462 283 TYR A CA  
1605 C C   . TYR A 208 ? 0.6082 0.4421 0.6234 0.0529  -0.0454 -0.0237 283 TYR A C   
1606 O O   . TYR A 208 ? 0.6607 0.4616 0.6947 0.0679  -0.0562 -0.0273 283 TYR A O   
1607 C CB  . TYR A 208 ? 0.7138 0.5786 0.7097 0.0702  -0.0228 -0.0708 283 TYR A CB  
1608 C CG  . TYR A 208 ? 0.8268 0.7003 0.7934 0.0644  -0.0184 -0.0916 283 TYR A CG  
1609 C CD1 . TYR A 208 ? 0.8189 0.7278 0.7655 0.0573  -0.0116 -0.0844 283 TYR A CD1 
1610 C CD2 . TYR A 208 ? 0.8972 0.7391 0.8542 0.0660  -0.0245 -0.1185 283 TYR A CD2 
1611 C CE1 . TYR A 208 ? 0.8949 0.8103 0.8127 0.0530  -0.0138 -0.1006 283 TYR A CE1 
1612 C CE2 . TYR A 208 ? 0.8668 0.7172 0.7930 0.0590  -0.0254 -0.1376 283 TYR A CE2 
1613 C CZ  . TYR A 208 ? 0.9351 0.8238 0.8419 0.0531  -0.0214 -0.1270 283 TYR A CZ  
1614 O OH  . TYR A 208 ? 1.2886 1.1845 1.1628 0.0473  -0.0283 -0.1432 283 TYR A OH  
1615 N N   . GLY A 209 ? 0.6512 0.5094 0.6611 0.0419  -0.0436 -0.0018 284 GLY A N   
1616 C CA  . GLY A 209 ? 0.5947 0.4451 0.6164 0.0442  -0.0561 0.0207  284 GLY A CA  
1617 C C   . GLY A 209 ? 0.5436 0.4320 0.5576 0.0360  -0.0487 0.0343  284 GLY A C   
1618 O O   . GLY A 209 ? 0.6767 0.5912 0.6764 0.0290  -0.0343 0.0280  284 GLY A O   
1619 N N   . THR A 210 ? 0.6526 0.5402 0.6760 0.0374  -0.0623 0.0530  285 THR A N   
1620 C CA  . THR A 210 ? 0.5194 0.4376 0.5342 0.0275  -0.0584 0.0644  285 THR A CA  
1621 C C   . THR A 210 ? 0.5210 0.4334 0.4982 0.0017  -0.0522 0.0722  285 THR A C   
1622 O O   . THR A 210 ? 0.7137 0.6495 0.6799 -0.0054 -0.0428 0.0729  285 THR A O   
1623 C CB  . THR A 210 ? 0.5437 0.4610 0.5753 0.0321  -0.0799 0.0822  285 THR A CB  
1624 O OG1 . THR A 210 ? 0.5711 0.4428 0.5811 0.0205  -0.1005 0.1011  285 THR A OG1 
1625 C CG2 . THR A 210 ? 0.4510 0.3854 0.5333 0.0613  -0.0835 0.0708  285 THR A CG2 
1626 N N   . ALA A 211 ? 0.6323 0.5141 0.5920 -0.0131 -0.0556 0.0765  286 ALA A N   
1627 C CA  . ALA A 211 ? 0.4867 0.3718 0.4178 -0.0376 -0.0445 0.0799  286 ALA A CA  
1628 C C   . ALA A 211 ? 0.5631 0.4803 0.4993 -0.0341 -0.0263 0.0613  286 ALA A C   
1629 O O   . ALA A 211 ? 0.6767 0.6089 0.5988 -0.0464 -0.0153 0.0607  286 ALA A O   
1630 C CB  . ALA A 211 ? 0.5619 0.4126 0.4792 -0.0574 -0.0485 0.0869  286 ALA A CB  
1631 N N   . ALA A 212 ? 0.5593 0.4852 0.5131 -0.0167 -0.0238 0.0454  287 ALA A N   
1632 C CA  . ALA A 212 ? 0.5764 0.5280 0.5297 -0.0125 -0.0124 0.0312  287 ALA A CA  
1633 C C   . ALA A 212 ? 0.5174 0.4892 0.4639 -0.0092 -0.0053 0.0355  287 ALA A C   
1634 O O   . ALA A 212 ? 0.6338 0.6192 0.5744 -0.0112 0.0017  0.0303  287 ALA A O   
1635 C CB  . ALA A 212 ? 0.5798 0.5327 0.5415 0.0038  -0.0128 0.0145  287 ALA A CB  
1636 N N   . ASP A 213 ? 0.5775 0.5509 0.5284 -0.0039 -0.0088 0.0442  288 ASP A N   
1637 C CA  . ASP A 213 ? 0.4574 0.4448 0.4014 -0.0055 -0.0034 0.0484  288 ASP A CA  
1638 C C   . ASP A 213 ? 0.4241 0.4053 0.3484 -0.0217 -0.0024 0.0540  288 ASP A C   
1639 O O   . ASP A 213 ? 0.6180 0.6043 0.5325 -0.0231 0.0049  0.0504  288 ASP A O   
1640 C CB  . ASP A 213 ? 0.5077 0.5047 0.4687 0.0000  -0.0086 0.0553  288 ASP A CB  
1641 C CG  . ASP A 213 ? 0.5574 0.5692 0.5368 0.0160  -0.0011 0.0454  288 ASP A CG  
1642 O OD1 . ASP A 213 ? 0.4903 0.5032 0.4573 0.0207  0.0078  0.0351  288 ASP A OD1 
1643 O OD2 . ASP A 213 ? 0.6090 0.6336 0.6152 0.0239  -0.0044 0.0469  288 ASP A OD2 
1644 N N   . VAL A 214 ? 0.5220 0.4878 0.4362 -0.0345 -0.0090 0.0624  289 VAL A N   
1645 C CA  . VAL A 214 ? 0.4437 0.4042 0.3311 -0.0525 -0.0040 0.0654  289 VAL A CA  
1646 C C   . VAL A 214 ? 0.5026 0.4756 0.3909 -0.0543 0.0123  0.0509  289 VAL A C   
1647 O O   . VAL A 214 ? 0.6588 0.6370 0.5343 -0.0591 0.0226  0.0440  289 VAL A O   
1648 C CB  . VAL A 214 ? 0.5529 0.4907 0.4204 -0.0689 -0.0148 0.0808  289 VAL A CB  
1649 C CG1 . VAL A 214 ? 0.5169 0.4497 0.3461 -0.0908 -0.0060 0.0823  289 VAL A CG1 
1650 C CG2 . VAL A 214 ? 0.5784 0.5076 0.4548 -0.0616 -0.0365 0.0947  289 VAL A CG2 
1651 N N   . PHE A 215 ? 0.5049 0.4843 0.4120 -0.0495 0.0136  0.0438  290 PHE A N   
1652 C CA  . PHE A 215 ? 0.4580 0.4580 0.3774 -0.0495 0.0251  0.0293  290 PHE A CA  
1653 C C   . PHE A 215 ? 0.4538 0.4654 0.3807 -0.0307 0.0263  0.0206  290 PHE A C   
1654 O O   . PHE A 215 ? 0.5275 0.5511 0.4587 -0.0282 0.0352  0.0107  290 PHE A O   
1655 C CB  . PHE A 215 ? 0.5322 0.5363 0.4711 -0.0518 0.0213  0.0236  290 PHE A CB  
1656 C CG  . PHE A 215 ? 0.4475 0.4800 0.4073 -0.0580 0.0313  0.0096  290 PHE A CG  
1657 C CD1 . PHE A 215 ? 0.5194 0.5750 0.5006 -0.0401 0.0280  -0.0035 290 PHE A CD1 
1658 C CD2 . PHE A 215 ? 0.4382 0.4767 0.3977 -0.0827 0.0432  0.0104  290 PHE A CD2 
1659 C CE1 . PHE A 215 ? 0.3546 0.4441 0.3664 -0.0430 0.0340  -0.0175 290 PHE A CE1 
1660 C CE2 . PHE A 215 ? 0.3053 0.3810 0.2951 -0.0892 0.0550  -0.0047 290 PHE A CE2 
1661 C CZ  . PHE A 215 ? 0.3288 0.4328 0.3498 -0.0675 0.0491  -0.0198 290 PHE A CZ  
1662 N N   . SER A 216 ? 0.4138 0.4200 0.3415 -0.0174 0.0181  0.0243  291 SER A N   
1663 C CA  . SER A 216 ? 0.3781 0.3868 0.3039 -0.0032 0.0178  0.0212  291 SER A CA  
1664 C C   . SER A 216 ? 0.4929 0.4914 0.4051 -0.0067 0.0227  0.0237  291 SER A C   
1665 O O   . SER A 216 ? 0.5524 0.5480 0.4645 0.0026  0.0242  0.0178  291 SER A O   
1666 C CB  . SER A 216 ? 0.4283 0.4334 0.3501 0.0057  0.0130  0.0261  291 SER A CB  
1667 O OG  . SER A 216 ? 0.6830 0.6926 0.6125 0.0097  0.0084  0.0191  291 SER A OG  
1668 N N   . LEU A 217 ? 0.5453 0.5346 0.4452 -0.0197 0.0222  0.0318  292 LEU A N   
1669 C CA  . LEU A 217 ? 0.5478 0.5243 0.4301 -0.0268 0.0250  0.0312  292 LEU A CA  
1670 C C   . LEU A 217 ? 0.4749 0.4532 0.3509 -0.0309 0.0366  0.0174  292 LEU A C   
1671 O O   . LEU A 217 ? 0.7140 0.6804 0.5811 -0.0276 0.0415  0.0082  292 LEU A O   
1672 C CB  . LEU A 217 ? 0.5014 0.4711 0.3722 -0.0410 0.0166  0.0428  292 LEU A CB  
1673 C CG  . LEU A 217 ? 0.4745 0.4292 0.3251 -0.0516 0.0148  0.0418  292 LEU A CG  
1674 C CD1 . LEU A 217 ? 0.4930 0.4393 0.3488 -0.0429 0.0166  0.0400  292 LEU A CD1 
1675 C CD2 . LEU A 217 ? 0.6733 0.6290 0.5209 -0.0643 0.0000  0.0547  292 LEU A CD2 
1676 N N   . GLY A 218 ? 0.6105 0.6025 0.4919 -0.0390 0.0430  0.0144  293 GLY A N   
1677 C CA  . GLY A 218 ? 0.4766 0.4805 0.3577 -0.0443 0.0600  -0.0013 293 GLY A CA  
1678 C C   . GLY A 218 ? 0.4280 0.4473 0.3391 -0.0229 0.0642  -0.0174 293 GLY A C   
1679 O O   . GLY A 218 ? 0.5900 0.6093 0.5012 -0.0174 0.0758  -0.0335 293 GLY A O   
1680 N N   . LEU A 219 ? 0.4370 0.4676 0.3727 -0.0091 0.0529  -0.0145 294 LEU A N   
1681 C CA  . LEU A 219 ? 0.4997 0.5406 0.4615 0.0139  0.0484  -0.0255 294 LEU A CA  
1682 C C   . LEU A 219 ? 0.5243 0.5326 0.4684 0.0268  0.0414  -0.0216 294 LEU A C   
1683 O O   . LEU A 219 ? 0.6315 0.6360 0.5896 0.0445  0.0413  -0.0334 294 LEU A O   
1684 C CB  . LEU A 219 ? 0.4809 0.5373 0.4623 0.0224  0.0335  -0.0218 294 LEU A CB  
1685 C CG  . LEU A 219 ? 0.4710 0.5579 0.4766 0.0090  0.0378  -0.0282 294 LEU A CG  
1686 C CD1 . LEU A 219 ? 0.5811 0.6740 0.5963 0.0155  0.0196  -0.0258 294 LEU A CD1 
1687 C CD2 . LEU A 219 ? 0.4049 0.5282 0.4476 0.0113  0.0509  -0.0473 294 LEU A CD2 
1688 N N   . THR A 220 ? 0.6061 0.5906 0.5235 0.0182  0.0350  -0.0056 295 THR A N   
1689 C CA  . THR A 220 ? 0.5187 0.4697 0.4175 0.0227  0.0298  -0.0001 295 THR A CA  
1690 C C   . THR A 220 ? 0.5491 0.4823 0.4375 0.0195  0.0396  -0.0147 295 THR A C   
1691 O O   . THR A 220 ? 0.6902 0.5970 0.5777 0.0332  0.0364  -0.0211 295 THR A O   
1692 C CB  . THR A 220 ? 0.5688 0.5098 0.4494 0.0084  0.0251  0.0174  295 THR A CB  
1693 O OG1 . THR A 220 ? 0.6835 0.6377 0.5705 0.0144  0.0190  0.0262  295 THR A OG1 
1694 C CG2 . THR A 220 ? 0.7715 0.6787 0.6335 0.0049  0.0217  0.0236  295 THR A CG2 
1695 N N   . ILE A 221 ? 0.6430 0.5848 0.5185 0.0012  0.0504  -0.0203 296 ILE A N   
1696 C CA  . ILE A 221 ? 0.5287 0.4549 0.3865 -0.0040 0.0625  -0.0387 296 ILE A CA  
1697 C C   . ILE A 221 ? 0.5580 0.5020 0.4448 0.0156  0.0757  -0.0624 296 ILE A C   
1698 O O   . ILE A 221 ? 0.8245 0.7459 0.7101 0.0281  0.0807  -0.0804 296 ILE A O   
1699 C CB  . ILE A 221 ? 0.5874 0.5192 0.4155 -0.0307 0.0695  -0.0368 296 ILE A CB  
1700 C CG1 . ILE A 221 ? 0.6012 0.5181 0.4104 -0.0459 0.0522  -0.0155 296 ILE A CG1 
1701 C CG2 . ILE A 221 ? 0.6409 0.5592 0.4428 -0.0377 0.0856  -0.0603 296 ILE A CG2 
1702 C CD1 . ILE A 221 ? 0.8207 0.7043 0.6167 -0.0471 0.0437  -0.0160 296 ILE A CD1 
1703 N N   . LEU A 222 ? 0.6649 0.6503 0.5828 0.0188  0.0811  -0.0646 297 LEU A N   
1704 C CA  . LEU A 222 ? 0.5336 0.5495 0.4928 0.0373  0.0935  -0.0884 297 LEU A CA  
1705 C C   . LEU A 222 ? 0.6033 0.6025 0.5882 0.0700  0.0767  -0.0916 297 LEU A C   
1706 O O   . LEU A 222 ? 0.6829 0.6882 0.6962 0.0913  0.0847  -0.1152 297 LEU A O   
1707 C CB  . LEU A 222 ? 0.5415 0.6069 0.5336 0.0301  0.0982  -0.0873 297 LEU A CB  
1708 C CG  . LEU A 222 ? 0.6294 0.7437 0.6761 0.0437  0.1135  -0.1129 297 LEU A CG  
1709 C CD1 . LEU A 222 ? 0.7362 0.8592 0.7708 0.0330  0.1459  -0.1371 297 LEU A CD1 
1710 C CD2 . LEU A 222 ? 0.6439 0.8034 0.7228 0.0307  0.1128  -0.1079 297 LEU A CD2 
1711 N N   . GLU A 223 ? 0.5754 0.5518 0.5492 0.0748  0.0535  -0.0683 298 GLU A N   
1712 C CA  . GLU A 223 ? 0.5970 0.5483 0.5835 0.1028  0.0337  -0.0649 298 GLU A CA  
1713 C C   . GLU A 223 ? 0.6224 0.5182 0.5843 0.1082  0.0337  -0.0703 298 GLU A C   
1714 O O   . GLU A 223 ? 0.7562 0.6341 0.7400 0.1356  0.0280  -0.0842 298 GLU A O   
1715 C CB  . GLU A 223 ? 0.5453 0.4865 0.5151 0.1008  0.0125  -0.0377 298 GLU A CB  
1716 C CG  . GLU A 223 ? 0.7539 0.6519 0.7132 0.1215  -0.0098 -0.0251 298 GLU A CG  
1717 C CD  . GLU A 223 ? 0.8944 0.7841 0.8268 0.1150  -0.0258 0.0009  298 GLU A CD  
1718 O OE1 . GLU A 223 ? 0.7365 0.6622 0.6733 0.1041  -0.0231 0.0031  298 GLU A OE1 
1719 O OE2 . GLU A 223 ? 1.0268 0.8707 0.9302 0.1194  -0.0397 0.0185  298 GLU A OE2 
1720 N N   . VAL A 224 ? 0.6129 0.4794 0.5324 0.0827  0.0378  -0.0607 299 VAL A N   
1721 C CA  . VAL A 224 ? 0.5110 0.3190 0.4040 0.0825  0.0346  -0.0647 299 VAL A CA  
1722 C C   . VAL A 224 ? 0.5767 0.3801 0.4707 0.0859  0.0543  -0.0985 299 VAL A C   
1723 O O   . VAL A 224 ? 0.8790 0.6347 0.7678 0.1000  0.0515  -0.1128 299 VAL A O   
1724 C CB  . VAL A 224 ? 0.7274 0.5121 0.5813 0.0517  0.0297  -0.0434 299 VAL A CB  
1725 C CG1 . VAL A 224 ? 0.6840 0.4744 0.5367 0.0500  0.0157  -0.0143 299 VAL A CG1 
1726 C CG2 . VAL A 224 ? 0.7969 0.6117 0.6369 0.0259  0.0430  -0.0478 299 VAL A CG2 
1727 N N   . ALA A 225 ? 0.6347 0.4829 0.5316 0.0723  0.0753  -0.1125 300 ALA A N   
1728 C CA  . ALA A 225 ? 0.7735 0.6208 0.6614 0.0708  0.0993  -0.1463 300 ALA A CA  
1729 C C   . ALA A 225 ? 0.5894 0.4670 0.5307 0.1036  0.1129  -0.1757 300 ALA A C   
1730 O O   . ALA A 225 ? 0.8403 0.7075 0.7794 0.1117  0.1329  -0.2094 300 ALA A O   
1731 C CB  . ALA A 225 ? 0.6970 0.5758 0.5552 0.0377  0.1172  -0.1464 300 ALA A CB  
1732 N N   . CYS A 226 ? 0.6758 0.5933 0.6671 0.1228  0.1024  -0.1664 301 CYS A N   
1733 C CA  . CYS A 226 ? 0.8374 0.7960 0.8933 0.1550  0.1117  -0.1938 301 CYS A CA  
1734 C C   . CYS A 226 ? 0.7862 0.7207 0.8784 0.1941  0.0805  -0.1864 301 CYS A C   
1735 O O   . CYS A 226 ? 0.9057 0.8707 1.0594 0.2276  0.0822  -0.2103 301 CYS A O   
1736 C CB  . CYS A 226 ? 0.9833 1.0200 1.0771 0.1433  0.1247  -0.1938 301 CYS A CB  
1737 S SG  . CYS A 226 ? 0.9071 0.9693 0.9556 0.0964  0.1601  -0.1986 301 CYS A SG  
1738 N N   . ASN A 227 ? 0.8423 0.7248 0.8989 0.1903  0.0519  -0.1536 302 ASN A N   
1739 C CA  . ASN A 227 ? 0.8640 0.7122 0.9385 0.2226  0.0184  -0.1391 302 ASN A CA  
1740 C C   . ASN A 227 ? 0.8845 0.7954 1.0190 0.2444  0.0043  -0.1383 302 ASN A C   
1741 O O   . ASN A 227 ? 1.0668 0.9766 1.2474 0.2830  -0.0151 -0.1470 302 ASN A O   
1742 C CB  . ASN A 227 ? 0.8814 0.6742 0.9659 0.2531  0.0156  -0.1619 302 ASN A CB  
1743 C CG  . ASN A 227 ? 0.9049 0.6239 0.9697 0.2709  -0.0217 -0.1341 302 ASN A CG  
1744 O OD1 . ASN A 227 ? 1.0335 0.7251 1.0517 0.2472  -0.0366 -0.0983 302 ASN A OD1 
1745 N ND2 . ASN A 227 ? 1.0017 0.7011 1.0992 0.2971  -0.0303 -0.1411 302 ASN A ND2 
1746 N N   . MET A 228 ? 0.9420 0.9065 1.0780 0.2196  0.0112  -0.1285 303 MET A N   
1747 C CA  . MET A 228 ? 0.9949 1.0206 1.1834 0.2318  -0.0033 -0.1278 303 MET A CA  
1748 C C   . MET A 228 ? 0.6834 0.6944 0.8351 0.2189  -0.0299 -0.0931 303 MET A C   
1749 O O   . MET A 228 ? 0.8186 0.7948 0.9124 0.1925  -0.0256 -0.0731 303 MET A O   
1750 C CB  . MET A 228 ? 0.9285 1.0294 1.1522 0.2114  0.0275  -0.1483 303 MET A CB  
1751 C CG  . MET A 228 ? 0.8382 0.9408 1.0128 0.1687  0.0408  -0.1307 303 MET A CG  
1752 S SD  . MET A 228 ? 1.2703 1.4540 1.4854 0.1429  0.0693  -0.1473 303 MET A SD  
1753 C CE  . MET A 228 ? 1.0591 1.2971 1.3453 0.1651  0.0390  -0.1482 303 MET A CE  
1754 N N   . GLU A 229 ? 0.7605 0.8017 0.9480 0.2378  -0.0577 -0.0883 304 GLU A N   
1755 C CA  . GLU A 229 ? 0.7803 0.8112 0.9312 0.2273  -0.0831 -0.0603 304 GLU A CA  
1756 C C   . GLU A 229 ? 0.6260 0.7174 0.7952 0.2030  -0.0726 -0.0662 304 GLU A C   
1757 O O   . GLU A 229 ? 0.7238 0.8768 0.9566 0.2092  -0.0693 -0.0871 304 GLU A O   
1758 C CB  . GLU A 229 ? 0.7800 0.7985 0.9462 0.2602  -0.1259 -0.0492 304 GLU A CB  
1759 C CG  . GLU A 229 ? 1.1785 1.1666 1.2835 0.2484  -0.1515 -0.0179 304 GLU A CG  
1760 C CD  . GLU A 229 ? 1.5076 1.4520 1.5944 0.2689  -0.1873 0.0029  304 GLU A CD  
1761 O OE1 . GLU A 229 ? 1.3107 1.2828 1.4509 0.2888  -0.2019 -0.0072 304 GLU A OE1 
1762 O OE2 . GLU A 229 ? 1.6680 1.5528 1.6852 0.2569  -0.1948 0.0306  304 GLU A OE2 
1763 N N   . LEU A 230 ? 0.5686 0.6424 0.6861 0.1751  -0.0669 -0.0490 305 LEU A N   
1764 C CA  . LEU A 230 ? 0.4794 0.5966 0.6081 0.1511  -0.0579 -0.0539 305 LEU A CA  
1765 C C   . LEU A 230 ? 0.5905 0.7304 0.7319 0.1589  -0.0899 -0.0500 305 LEU A C   
1766 O O   . LEU A 230 ? 0.6411 0.7454 0.7432 0.1694  -0.1151 -0.0319 305 LEU A O   
1767 C CB  . LEU A 230 ? 0.5478 0.6366 0.6222 0.1230  -0.0422 -0.0395 305 LEU A CB  
1768 C CG  . LEU A 230 ? 0.3925 0.4589 0.4481 0.1110  -0.0157 -0.0418 305 LEU A CG  
1769 C CD1 . LEU A 230 ? 0.4921 0.5385 0.5047 0.0860  -0.0069 -0.0269 305 LEU A CD1 
1770 C CD2 . LEU A 230 ? 0.5797 0.6863 0.6755 0.1051  0.0077  -0.0646 305 LEU A CD2 
1771 N N   . PRO A 231 ? 0.4958 0.6930 0.6872 0.1506  -0.0897 -0.0663 306 PRO A N   
1772 C CA  . PRO A 231 ? 0.4398 0.6620 0.6468 0.1566  -0.1241 -0.0662 306 PRO A CA  
1773 C C   . PRO A 231 ? 0.5590 0.7545 0.7063 0.1357  -0.1307 -0.0533 306 PRO A C   
1774 O O   . PRO A 231 ? 0.4783 0.6576 0.5970 0.1126  -0.1059 -0.0505 306 PRO A O   
1775 C CB  . PRO A 231 ? 0.3348 0.6298 0.6191 0.1470  -0.1152 -0.0902 306 PRO A CB  
1776 C CG  . PRO A 231 ? 0.3765 0.6705 0.6528 0.1206  -0.0723 -0.0952 306 PRO A CG  
1777 C CD  . PRO A 231 ? 0.3962 0.6377 0.6293 0.1316  -0.0580 -0.0852 306 PRO A CD  
1778 N N   . HIS A 232 ? 0.7150 0.9055 0.8432 0.1457  -0.1664 -0.0467 307 HIS A N   
1779 C CA  . HIS A 232 ? 0.5524 0.7210 0.6237 0.1280  -0.1731 -0.0405 307 HIS A CA  
1780 C C   . HIS A 232 ? 0.5531 0.7609 0.6565 0.1056  -0.1725 -0.0593 307 HIS A C   
1781 O O   . HIS A 232 ? 0.7532 0.9408 0.8203 0.0855  -0.1604 -0.0602 307 HIS A O   
1782 C CB  . HIS A 232 ? 0.7111 0.8555 0.7372 0.1436  -0.2114 -0.0269 307 HIS A CB  
1783 C CG  . HIS A 232 ? 0.9717 1.0593 0.9394 0.1542  -0.2089 -0.0027 307 HIS A CG  
1784 N ND1 . HIS A 232 ? 1.0453 1.0920 0.9367 0.1409  -0.2005 0.0117  307 HIS A ND1 
1785 C CD2 . HIS A 232 ? 0.9509 1.0147 0.9266 0.1751  -0.2126 0.0087  307 HIS A CD2 
1786 C CE1 . HIS A 232 ? 0.9936 0.9960 0.8485 0.1492  -0.1987 0.0332  307 HIS A CE1 
1787 N NE2 . HIS A 232 ? 0.9656 0.9724 0.8684 0.1702  -0.2076 0.0323  307 HIS A NE2 
1788 N N   . GLY A 233 ? 0.5609 0.8238 0.7349 0.1084  -0.1855 -0.0753 308 GLY A N   
1789 C CA  . GLY A 233 ? 0.4167 0.7166 0.6252 0.0824  -0.1857 -0.0928 308 GLY A CA  
1790 C C   . GLY A 233 ? 0.4909 0.8617 0.7923 0.0844  -0.1886 -0.1103 308 GLY A C   
1791 O O   . GLY A 233 ? 0.6053 0.9953 0.9460 0.1044  -0.1776 -0.1119 308 GLY A O   
1792 N N   . GLY A 234 ? 0.4964 0.9074 0.8356 0.0626  -0.2025 -0.1259 309 GLY A N   
1793 C CA  . GLY A 234 ? 0.5726 1.0484 0.9967 0.0594  -0.2001 -0.1391 309 GLY A CA  
1794 C C   . GLY A 234 ? 0.3502 0.8590 0.8206 0.0420  -0.1550 -0.1488 309 GLY A C   
1795 O O   . GLY A 234 ? 0.4527 0.9289 0.8848 0.0218  -0.1257 -0.1432 309 GLY A O   
1796 N N   . GLU A 235 ? 0.3558 0.9146 0.8929 0.0485  -0.1447 -0.1575 310 GLU A N   
1797 C CA  . GLU A 235 ? 0.4409 1.0337 1.0171 0.0269  -0.0991 -0.1673 310 GLU A CA  
1798 C C   . GLU A 235 ? 0.4352 1.0001 0.9815 0.0390  -0.0674 -0.1639 310 GLU A C   
1799 O O   . GLU A 235 ? 0.3985 0.9600 0.9309 0.0105  -0.0308 -0.1645 310 GLU A O   
1800 C CB  . GLU A 235 ? 0.5580 1.2119 1.2101 0.0349  -0.0960 -0.1791 310 GLU A CB  
1801 C CG  . GLU A 235 ? 0.7395 1.4322 1.4277 0.0065  -0.0488 -0.1893 310 GLU A CG  
1802 C CD  . GLU A 235 ? 1.0755 1.8376 1.8444 0.0093  -0.0489 -0.2024 310 GLU A CD  
1803 O OE1 . GLU A 235 ? 0.9811 1.7619 1.7804 0.0323  -0.0884 -0.2029 310 GLU A OE1 
1804 O OE2 . GLU A 235 ? 1.2841 2.0820 2.0836 -0.0123 -0.0097 -0.2112 310 GLU A OE2 
1805 N N   . GLY A 236 ? 0.2694 0.8076 0.7992 0.0786  -0.0816 -0.1583 311 GLY A N   
1806 C CA  . GLY A 236 ? 0.2473 0.7537 0.7456 0.0899  -0.0540 -0.1559 311 GLY A CA  
1807 C C   . GLY A 236 ? 0.3600 0.7980 0.7706 0.0652  -0.0414 -0.1354 311 GLY A C   
1808 O O   . GLY A 236 ? 0.3920 0.8052 0.7710 0.0538  -0.0087 -0.1318 311 GLY A O   
1809 N N   . TRP A 237 ? 0.3689 0.7763 0.7393 0.0576  -0.0681 -0.1235 312 TRP A N   
1810 C CA  . TRP A 237 ? 0.3805 0.7280 0.6777 0.0377  -0.0574 -0.1069 312 TRP A CA  
1811 C C   . TRP A 237 ? 0.2811 0.6387 0.5851 -0.0009 -0.0300 -0.1099 312 TRP A C   
1812 O O   . TRP A 237 ? 0.4911 0.8087 0.7496 -0.0144 -0.0084 -0.0979 312 TRP A O   
1813 C CB  . TRP A 237 ? 0.4112 0.7290 0.6684 0.0407  -0.0901 -0.0994 312 TRP A CB  
1814 C CG  . TRP A 237 ? 0.3300 0.5895 0.5188 0.0283  -0.0807 -0.0854 312 TRP A CG  
1815 C CD1 . TRP A 237 ? 0.3724 0.5849 0.5059 0.0428  -0.0798 -0.0700 312 TRP A CD1 
1816 C CD2 . TRP A 237 ? 0.3408 0.5841 0.5151 -0.0005 -0.0719 -0.0864 312 TRP A CD2 
1817 N NE1 . TRP A 237 ? 0.4043 0.5810 0.4968 0.0272  -0.0698 -0.0635 312 TRP A NE1 
1818 C CE2 . TRP A 237 ? 0.4334 0.6237 0.5485 0.0028  -0.0663 -0.0731 312 TRP A CE2 
1819 C CE3 . TRP A 237 ? 0.2966 0.5634 0.5047 -0.0295 -0.0684 -0.0971 312 TRP A CE3 
1820 C CZ2 . TRP A 237 ? 0.3102 0.4696 0.4021 -0.0162 -0.0596 -0.0714 312 TRP A CZ2 
1821 C CZ3 . TRP A 237 ? 0.3488 0.5755 0.5258 -0.0517 -0.0624 -0.0929 312 TRP A CZ3 
1822 C CH2 . TRP A 237 ? 0.3944 0.5676 0.5153 -0.0422 -0.0590 -0.0808 312 TRP A CH2 
1823 N N   . GLN A 238 ? 0.4555 0.8654 0.8159 -0.0209 -0.0327 -0.1243 313 GLN A N   
1824 C CA  . GLN A 238 ? 0.3206 0.7352 0.6848 -0.0626 -0.0075 -0.1242 313 GLN A CA  
1825 C C   . GLN A 238 ? 0.3275 0.7593 0.6994 -0.0725 0.0333  -0.1259 313 GLN A C   
1826 O O   . GLN A 238 ? 0.6049 1.0072 0.9397 -0.1022 0.0559  -0.1145 313 GLN A O   
1827 C CB  . GLN A 238 ? 0.2596 0.7297 0.6872 -0.0856 -0.0201 -0.1401 313 GLN A CB  
1828 C CG  . GLN A 238 ? 0.4212 0.8858 0.8472 -0.0738 -0.0646 -0.1447 313 GLN A CG  
1829 C CD  . GLN A 238 ? 0.4818 0.8778 0.8419 -0.0900 -0.0748 -0.1349 313 GLN A CD  
1830 O OE1 . GLN A 238 ? 0.5436 0.8976 0.8675 -0.1106 -0.0517 -0.1232 313 GLN A OE1 
1831 N NE2 . GLN A 238 ? 0.5738 0.9570 0.9169 -0.0796 -0.1107 -0.1407 313 GLN A NE2 
1832 N N   . GLN A 239 ? 0.4326 0.9081 0.8485 -0.0470 0.0419  -0.1405 314 GLN A N   
1833 C CA  . GLN A 239 ? 0.4049 0.9037 0.8304 -0.0570 0.0840  -0.1492 314 GLN A CA  
1834 C C   . GLN A 239 ? 0.4128 0.8446 0.7586 -0.0560 0.0990  -0.1328 314 GLN A C   
1835 O O   . GLN A 239 ? 0.5923 1.0220 0.9148 -0.0811 0.1325  -0.1319 314 GLN A O   
1836 C CB  . GLN A 239 ? 0.5879 1.1322 1.0712 -0.0233 0.0855  -0.1688 314 GLN A CB  
1837 C CG  . GLN A 239 ? 0.4791 1.0781 1.0301 -0.0255 0.0712  -0.1790 314 GLN A CG  
1838 C CD  . GLN A 239 ? 0.5386 1.1732 1.1417 0.0095  0.0719  -0.1949 314 GLN A CD  
1839 O OE1 . GLN A 239 ? 0.6517 1.2644 1.2376 0.0348  0.0840  -0.1995 314 GLN A OE1 
1840 N NE2 . GLN A 239 ? 0.4589 1.1465 1.1268 0.0107  0.0580  -0.2038 314 GLN A NE2 
1841 N N   . LEU A 240 ? 0.4037 0.7824 0.7055 -0.0301 0.0746  -0.1194 315 LEU A N   
1842 C CA  . LEU A 240 ? 0.4202 0.7389 0.6520 -0.0316 0.0842  -0.1034 315 LEU A CA  
1843 C C   . LEU A 240 ? 0.3937 0.6711 0.5771 -0.0619 0.0839  -0.0832 315 LEU A C   
1844 O O   . LEU A 240 ? 0.5456 0.7760 0.6750 -0.0639 0.0867  -0.0683 315 LEU A O   
1845 C CB  . LEU A 240 ? 0.3938 0.6733 0.5997 0.0024  0.0600  -0.0953 315 LEU A CB  
1846 C CG  . LEU A 240 ? 0.4009 0.6946 0.6359 0.0359  0.0592  -0.1100 315 LEU A CG  
1847 C CD1 . LEU A 240 ? 0.4776 0.7238 0.6793 0.0622  0.0320  -0.0958 315 LEU A CD1 
1848 C CD2 . LEU A 240 ? 0.4969 0.7881 0.7189 0.0302  0.0926  -0.1210 315 LEU A CD2 
1849 N N   . ARG A 241 ? 0.4388 0.7308 0.6430 -0.0852 0.0780  -0.0829 316 ARG A N   
1850 C CA  . ARG A 241 ? 0.3981 0.6428 0.5604 -0.1095 0.0724  -0.0646 316 ARG A CA  
1851 C C   . ARG A 241 ? 0.3807 0.6431 0.5584 -0.1513 0.0900  -0.0642 316 ARG A C   
1852 O O   . ARG A 241 ? 0.5006 0.7332 0.6666 -0.1717 0.0778  -0.0549 316 ARG A O   
1853 C CB  . ARG A 241 ? 0.4114 0.6326 0.5687 -0.0953 0.0407  -0.0624 316 ARG A CB  
1854 C CG  . ARG A 241 ? 0.4614 0.6539 0.5876 -0.0626 0.0277  -0.0561 316 ARG A CG  
1855 C CD  . ARG A 241 ? 0.3499 0.5374 0.4773 -0.0448 0.0000  -0.0605 316 ARG A CD  
1856 N NE  . ARG A 241 ? 0.4665 0.6233 0.5571 -0.0202 -0.0075 -0.0511 316 ARG A NE  
1857 C CZ  . ARG A 241 ? 0.4171 0.5826 0.5115 0.0032  -0.0115 -0.0522 316 ARG A CZ  
1858 N NH1 . ARG A 241 ? 0.3724 0.5783 0.5104 0.0114  -0.0104 -0.0646 316 ARG A NH1 
1859 N NH2 . ARG A 241 ? 0.4121 0.5449 0.4688 0.0185  -0.0168 -0.0410 316 ARG A NH2 
1860 N N   . GLN A 242 ? 0.6733 0.9424 0.5920 0.1508  0.0578  0.0825  317 GLN A N   
1861 C CA  . GLN A 242 ? 0.6035 0.9070 0.5602 0.1404  0.0822  0.0670  317 GLN A CA  
1862 C C   . GLN A 242 ? 0.5913 0.8958 0.5302 0.1336  0.1250  0.0561  317 GLN A C   
1863 O O   . GLN A 242 ? 0.6414 0.9649 0.5981 0.1206  0.1499  0.0427  317 GLN A O   
1864 C CB  . GLN A 242 ? 0.6206 0.9601 0.6711 0.1494  0.0715  0.0503  317 GLN A CB  
1865 C CG  . GLN A 242 ? 0.6420 0.9801 0.7145 0.1565  0.0255  0.0581  317 GLN A CG  
1866 C CD  . GLN A 242 ? 0.8637 1.1992 0.8978 0.1402  0.0185  0.0684  317 GLN A CD  
1867 O OE1 . GLN A 242 ? 0.9648 1.3256 1.0144 0.1257  0.0416  0.0572  317 GLN A OE1 
1868 N NE2 . GLN A 242 ? 0.9099 1.2117 0.8897 0.1404  -0.0126 0.0891  317 GLN A NE2 
1869 N N   . GLY A 243 ? 0.6527 0.9334 0.5536 0.1404  0.1343  0.0606  318 GLY A N   
1870 C CA  . GLY A 243 ? 0.5842 0.8591 0.4620 0.1357  0.1709  0.0510  318 GLY A CA  
1871 C C   . GLY A 243 ? 0.6996 0.9839 0.6214 0.1477  0.1861  0.0398  318 GLY A C   
1872 O O   . GLY A 243 ? 0.8083 1.0756 0.6970 0.1494  0.2070  0.0379  318 GLY A O   
1873 N N   . TYR A 244 ? 0.7771 1.0884 0.7751 0.1570  0.1744  0.0304  319 TYR A N   
1874 C CA  . TYR A 244 ? 0.7581 1.0806 0.8052 0.1701  0.1858  0.0173  319 TYR A CA  
1875 C C   . TYR A 244 ? 0.8078 1.1062 0.8475 0.1890  0.1540  0.0306  319 TYR A C   
1876 O O   . TYR A 244 ? 0.9775 1.2509 0.9758 0.1896  0.1240  0.0486  319 TYR A O   
1877 C CB  . TYR A 244 ? 0.5820 0.9489 0.7231 0.1705  0.1916  -0.0071 319 TYR A CB  
1878 C CG  . TYR A 244 ? 0.7381 1.1217 0.9281 0.1782  0.1515  -0.0066 319 TYR A CG  
1879 C CD1 . TYR A 244 ? 0.9383 1.3158 1.1653 0.2009  0.1131  -0.0043 319 TYR A CD1 
1880 C CD2 . TYR A 244 ? 0.8281 1.2293 1.0253 0.1631  0.1499  -0.0094 319 TYR A CD2 
1881 C CE1 . TYR A 244 ? 0.8812 1.2679 1.1500 0.2093  0.0717  -0.0049 319 TYR A CE1 
1882 C CE2 . TYR A 244 ? 0.8831 1.2993 1.1265 0.1708  0.1115  -0.0103 319 TYR A CE2 
1883 C CZ  . TYR A 244 ? 0.9157 1.3239 1.1947 0.1946  0.0714  -0.0082 319 TYR A CZ  
1884 O OH  . TYR A 244 ? 0.9044 1.3214 1.2261 0.2038  0.0285  -0.0098 319 TYR A OH  
1885 N N   . LEU A 245 ? 0.9155 1.2181 0.9922 0.2024  0.1616  0.0204  320 LEU A N   
1886 C CA  . LEU A 245 ? 0.8833 1.1573 0.9505 0.2195  0.1348  0.0308  320 LEU A CA  
1887 C C   . LEU A 245 ? 1.0529 1.3434 1.2012 0.2377  0.1031  0.0195  320 LEU A C   
1888 O O   . LEU A 245 ? 0.8902 1.2237 1.1148 0.2379  0.1120  -0.0029 320 LEU A O   
1889 C CB  . LEU A 245 ? 0.8930 1.1548 0.9398 0.2235  0.1634  0.0272  320 LEU A CB  
1890 C CG  . LEU A 245 ? 0.8434 1.0750 0.8022 0.2125  0.1799  0.0401  320 LEU A CG  
1891 C CD1 . LEU A 245 ? 0.8945 1.1224 0.8454 0.2157  0.2127  0.0311  320 LEU A CD1 
1892 C CD2 . LEU A 245 ? 0.8774 1.0700 0.7818 0.2141  0.1485  0.0594  320 LEU A CD2 
1893 N N   . PRO A 246 ? 1.3310 1.5854 1.4640 0.2523  0.0643  0.0320  321 PRO A N   
1894 C CA  . PRO A 246 ? 1.2886 1.5512 1.4977 0.2738  0.0275  0.0192  321 PRO A CA  
1895 C C   . PRO A 246 ? 1.2249 1.5140 1.5007 0.2867  0.0494  -0.0047 321 PRO A C   
1896 O O   . PRO A 246 ? 1.2292 1.4901 1.4749 0.2941  0.0548  0.0014  321 PRO A O   
1897 C CB  . PRO A 246 ? 1.3812 1.5805 1.5286 0.2820  -0.0172 0.0425  321 PRO A CB  
1898 C CG  . PRO A 246 ? 1.3873 1.5543 1.4436 0.2675  0.0101  0.0598  321 PRO A CG  
1899 C CD  . PRO A 246 ? 1.3137 1.5135 1.3552 0.2480  0.0500  0.0567  321 PRO A CD  
1900 N N   . PRO A 247 ? 1.0000 1.3440 1.3683 0.2883  0.0636  -0.0345 322 PRO A N   
1901 C CA  . PRO A 247 ? 0.8570 1.2307 1.2908 0.2970  0.0910  -0.0614 322 PRO A CA  
1902 C C   . PRO A 247 ? 0.9936 1.3425 1.4545 0.3245  0.0542  -0.0638 322 PRO A C   
1903 O O   . PRO A 247 ? 1.0355 1.3855 1.5084 0.3311  0.0765  -0.0731 322 PRO A O   
1904 C CB  . PRO A 247 ? 0.6372 1.0738 1.1692 0.2914  0.1048  -0.0960 322 PRO A CB  
1905 C CG  . PRO A 247 ? 0.8203 1.2539 1.3598 0.2945  0.0606  -0.0881 322 PRO A CG  
1906 C CD  . PRO A 247 ? 0.8946 1.2757 1.3188 0.2834  0.0509  -0.0483 322 PRO A CD  
1907 N N   . GLU A 248 ? 0.9884 1.3095 1.4544 0.3407  -0.0038 -0.0555 323 GLU A N   
1908 C CA  . GLU A 248 ? 1.0522 1.3361 1.5321 0.3673  -0.0466 -0.0559 323 GLU A CA  
1909 C C   . GLU A 248 ? 1.0977 1.3277 1.4856 0.3638  -0.0342 -0.0309 323 GLU A C   
1910 O O   . GLU A 248 ? 1.0778 1.3077 1.4892 0.3756  -0.0220 -0.0421 323 GLU A O   
1911 C CB  . GLU A 248 ? 1.2366 1.4828 1.7105 0.3809  -0.1141 -0.0455 323 GLU A CB  
1912 C CG  . GLU A 248 ? 1.3562 1.6544 1.9233 0.3860  -0.1326 -0.0715 323 GLU A CG  
1913 C CD  . GLU A 248 ? 1.3960 1.7155 1.9287 0.3591  -0.1084 -0.0599 323 GLU A CD  
1914 O OE1 . GLU A 248 ? 1.1179 1.4109 1.5551 0.3381  -0.0802 -0.0324 323 GLU A OE1 
1915 O OE2 . GLU A 248 ? 1.4744 1.8375 2.0781 0.3593  -0.1186 -0.0806 323 GLU A OE2 
1916 N N   . PHE A 249 ? 1.0439 1.2300 1.3287 0.3464  -0.0354 0.0003  324 PHE A N   
1917 C CA  . PHE A 249 ? 1.0548 1.1871 1.2498 0.3410  -0.0272 0.0220  324 PHE A CA  
1918 C C   . PHE A 249 ? 1.0420 1.1969 1.2092 0.3248  0.0332  0.0206  324 PHE A C   
1919 O O   . PHE A 249 ? 1.0627 1.1866 1.1831 0.3250  0.0458  0.0285  324 PHE A O   
1920 C CB  . PHE A 249 ? 1.1616 1.2344 1.2585 0.3275  -0.0561 0.0516  324 PHE A CB  
1921 C CG  . PHE A 249 ? 1.4093 1.4317 1.5034 0.3433  -0.1209 0.0584  324 PHE A CG  
1922 C CD1 . PHE A 249 ? 1.4677 1.5061 1.6080 0.3499  -0.1562 0.0523  324 PHE A CD1 
1923 C CD2 . PHE A 249 ? 1.3837 1.3377 1.4251 0.3512  -0.1484 0.0702  324 PHE A CD2 
1924 C CE1 . PHE A 249 ? 1.5592 1.5443 1.6929 0.3659  -0.2210 0.0579  324 PHE A CE1 
1925 C CE2 . PHE A 249 ? 1.4837 1.3793 1.5120 0.3654  -0.2125 0.0769  324 PHE A CE2 
1926 C CZ  . PHE A 249 ? 1.5492 1.4594 1.6237 0.3738  -0.2504 0.0707  324 PHE A CZ  
1927 N N   . THR A 250 ? 0.9901 1.1934 1.1814 0.3106  0.0691  0.0100  325 THR A N   
1928 C CA  . THR A 250 ? 0.9247 1.1398 1.0812 0.2958  0.1212  0.0087  325 THR A CA  
1929 C C   . THR A 250 ? 0.9452 1.1816 1.1525 0.3061  0.1489  -0.0118 325 THR A C   
1930 O O   . THR A 250 ? 1.0298 1.2659 1.2020 0.2963  0.1883  -0.0121 325 THR A O   
1931 C CB  . THR A 250 ? 0.9270 1.1774 1.0861 0.2767  0.1490  0.0029  325 THR A CB  
1932 O OG1 . THR A 250 ? 1.1742 1.4154 1.2705 0.2619  0.1876  0.0084  325 THR A OG1 
1933 C CG2 . THR A 250 ? 0.9724 1.2771 1.2271 0.2787  0.1675  -0.0269 325 THR A CG2 
1934 N N   . ALA A 251 ? 0.8389 1.0935 1.1290 0.3258  0.1284  -0.0309 326 ALA A N   
1935 C CA  . ALA A 251 ? 0.7048 0.9765 1.0428 0.3365  0.1520  -0.0511 326 ALA A CA  
1936 C C   . ALA A 251 ? 1.0291 1.2501 1.3001 0.3423  0.1489  -0.0329 326 ALA A C   
1937 O O   . ALA A 251 ? 1.1586 1.3292 1.3626 0.3425  0.1178  -0.0091 326 ALA A O   
1938 C CB  . ALA A 251 ? 0.6771 0.9776 1.1219 0.3589  0.1237  -0.0785 326 ALA A CB  
1939 N N   . GLY A 252 ? 0.7645 0.9974 1.0513 0.3447  0.1837  -0.0457 327 GLY A N   
1940 C CA  . GLY A 252 ? 0.8498 1.0400 1.0752 0.3479  0.1885  -0.0315 327 GLY A CA  
1941 C C   . GLY A 252 ? 0.9828 1.1506 1.1150 0.3276  0.2144  -0.0128 327 GLY A C   
1942 O O   . GLY A 252 ? 1.1152 1.2551 1.2006 0.3276  0.2273  -0.0061 327 GLY A O   
1943 N N   . LEU A 253 ? 0.7690 0.9483 0.8749 0.3110  0.2210  -0.0066 328 LEU A N   
1944 C CA  . LEU A 253 ? 0.8539 1.0166 0.8798 0.2933  0.2443  0.0054  328 LEU A CA  
1945 C C   . LEU A 253 ? 0.8421 1.0237 0.8766 0.2709  0.2774  -0.0110 328 LEU A C   
1946 O O   . LEU A 253 ? 0.8121 1.0260 0.9020 0.2626  0.2869  -0.0292 328 LEU A O   
1947 C CB  . LEU A 253 ? 0.8641 1.0231 0.8547 0.2799  0.2277  0.0180  328 LEU A CB  
1948 C CG  . LEU A 253 ? 0.8861 1.0086 0.8455 0.2822  0.1830  0.0358  328 LEU A CG  
1949 C CD1 . LEU A 253 ? 0.8196 0.9334 0.7210 0.2640  0.1791  0.0483  328 LEU A CD1 
1950 C CD2 . LEU A 253 ? 1.0252 1.1017 0.9407 0.2876  0.1728  0.0448  328 LEU A CD2 
1951 N N   . SER A 254 ? 0.6522 0.8035 0.6326 0.2456  0.2773  -0.0079 329 SER A N   
1952 C CA  . SER A 254 ? 0.6849 0.8387 0.6667 0.2119  0.2837  -0.0241 329 SER A CA  
1953 C C   . SER A 254 ? 0.8475 1.0108 0.8193 0.1922  0.2848  -0.0275 329 SER A C   
1954 O O   . SER A 254 ? 0.9415 1.0983 0.8846 0.1951  0.2764  -0.0140 329 SER A O   
1955 C CB  . SER A 254 ? 0.8099 0.9333 0.7460 0.1942  0.2744  -0.0206 329 SER A CB  
1956 O OG  . SER A 254 ? 0.8455 0.9496 0.7344 0.1852  0.2611  -0.0089 329 SER A OG  
1957 N N   . SER A 255 ? 1.2381 1.1037 0.8427 0.1006  0.1523  -0.3059 330 SER A N   
1958 C CA  . SER A 255 ? 0.9928 0.9166 0.5894 0.0947  0.1509  -0.2720 330 SER A CA  
1959 C C   . SER A 255 ? 1.0718 0.9591 0.6450 0.0653  0.1321  -0.2457 330 SER A C   
1960 O O   . SER A 255 ? 0.9753 0.8895 0.5619 0.0525  0.1347  -0.2126 330 SER A O   
1961 C CB  . SER A 255 ? 0.9954 0.9428 0.5434 0.1076  0.1614  -0.2763 330 SER A CB  
1962 O OG  . SER A 255 ? 1.1877 1.1014 0.6905 0.0929  0.1475  -0.3023 330 SER A OG  
1963 N N   . GLU A 256 ? 1.1183 0.9417 0.6646 0.0500  0.1120  -0.2579 331 GLU A N   
1964 C CA  . GLU A 256 ? 0.9623 0.7564 0.4987 0.0193  0.0909  -0.2323 331 GLU A CA  
1965 C C   . GLU A 256 ? 1.0538 0.8369 0.6295 0.0170  0.0919  -0.2069 331 GLU A C   
1966 O O   . GLU A 256 ? 1.1453 0.9425 0.7275 -0.0021 0.0849  -0.1782 331 GLU A O   
1967 C CB  . GLU A 256 ? 1.1872 0.9202 0.6932 0.0043  0.0654  -0.2554 331 GLU A CB  
1968 C CG  . GLU A 256 ? 1.3474 1.0945 0.8065 0.0054  0.0586  -0.2816 331 GLU A CG  
1969 C CD  . GLU A 256 ? 1.5008 1.2518 0.9535 0.0336  0.0755  -0.3216 331 GLU A CD  
1970 O OE1 . GLU A 256 ? 1.6518 1.3913 1.1406 0.0525  0.0908  -0.3285 331 GLU A OE1 
1971 O OE2 . GLU A 256 ? 1.5120 1.2807 0.9231 0.0380  0.0743  -0.3474 331 GLU A OE2 
1972 N N   . LEU A 257 ? 0.9896 0.7470 0.5898 0.0406  0.1005  -0.2164 332 LEU A N   
1973 C CA  . LEU A 257 ? 0.8685 0.6146 0.4981 0.0469  0.1029  -0.1910 332 LEU A CA  
1974 C C   . LEU A 257 ? 0.7890 0.6159 0.4567 0.0568  0.1164  -0.1746 332 LEU A C   
1975 O O   . LEU A 257 ? 0.9032 0.7428 0.5869 0.0493  0.1132  -0.1490 332 LEU A O   
1976 C CB  . LEU A 257 ? 0.9133 0.5990 0.5536 0.0757  0.1060  -0.1999 332 LEU A CB  
1977 C CG  . LEU A 257 ? 0.8666 0.5336 0.5306 0.0906  0.1080  -0.1690 332 LEU A CG  
1978 C CD1 . LEU A 257 ? 0.8063 0.4662 0.4847 0.0518  0.0880  -0.1387 332 LEU A CD1 
1979 C CD2 . LEU A 257 ? 0.9108 0.5139 0.5831 0.1245  0.1108  -0.1712 332 LEU A CD2 
1980 N N   . ARG A 258 ? 0.8309 0.7158 0.5157 0.0719  0.1306  -0.1922 333 ARG A N   
1981 C CA  . ARG A 258 ? 0.7632 0.7263 0.4896 0.0766  0.1401  -0.1820 333 ARG A CA  
1982 C C   . ARG A 258 ? 0.8974 0.8708 0.6067 0.0534  0.1354  -0.1524 333 ARG A C   
1983 O O   . ARG A 258 ? 0.8603 0.8561 0.5968 0.0500  0.1347  -0.1330 333 ARG A O   
1984 C CB  . ARG A 258 ? 0.7864 0.8017 0.5357 0.0893  0.1551  -0.2014 333 ARG A CB  
1985 C CG  . ARG A 258 ? 1.0576 1.0141 0.8130 0.1065  0.1826  -0.2193 333 ARG A CG  
1986 C CD  . ARG A 258 ? 1.0051 0.9767 0.7588 0.1255  0.2133  -0.2265 333 ARG A CD  
1987 N NE  . ARG A 258 ? 1.3979 1.3444 1.0968 0.1173  0.2269  -0.2362 333 ARG A NE  
1988 C CZ  . ARG A 258 ? 1.4431 1.4113 1.1049 0.1200  0.2329  -0.2157 333 ARG A CZ  
1989 N NH1 . ARG A 258 ? 1.4339 1.4585 1.1275 0.1100  0.2328  -0.1951 333 ARG A NH1 
1990 N NH2 . ARG A 258 ? 1.2420 1.1956 0.8495 0.1259  0.2400  -0.2268 333 ARG A NH2 
1991 N N   . SER A 259 ? 0.8007 0.7554 0.4691 0.0332  0.1329  -0.1516 334 SER A N   
1992 C CA  . SER A 259 ? 0.7973 0.7592 0.4565 0.0055  0.1298  -0.1260 334 SER A CA  
1993 C C   . SER A 259 ? 0.7644 0.7041 0.4341 -0.0097 0.1111  -0.1067 334 SER A C   
1994 O O   . SER A 259 ? 0.9215 0.8776 0.6084 -0.0213 0.1098  -0.0864 334 SER A O   
1995 C CB  . SER A 259 ? 0.9213 0.8674 0.5286 -0.0066 0.1277  -0.1293 334 SER A CB  
1996 O OG  . SER A 259 ? 1.0802 0.9822 0.6594 -0.0096 0.1081  -0.1446 334 SER A OG  
1997 N N   . VAL A 260 ? 0.7928 0.6890 0.4495 -0.0099 0.0982  -0.1134 335 VAL A N   
1998 C CA  . VAL A 260 ? 0.8315 0.7074 0.4940 -0.0208 0.0840  -0.0937 335 VAL A CA  
1999 C C   . VAL A 260 ? 0.7519 0.6543 0.4554 -0.0023 0.0928  -0.0848 335 VAL A C   
2000 O O   . VAL A 260 ? 0.7423 0.6579 0.4602 -0.0078 0.0857  -0.0649 335 VAL A O   
2001 C CB  . VAL A 260 ? 0.8406 0.6578 0.4792 -0.0283 0.0693  -0.1026 335 VAL A CB  
2002 C CG1 . VAL A 260 ? 0.7927 0.6148 0.4715 -0.0342 0.0519  -0.0729 335 VAL A CG1 
2003 C CG2 . VAL A 260 ? 0.9527 0.7519 0.5490 -0.0474 0.0536  -0.1156 335 VAL A CG2 
2004 N N   . LEU A 261 ? 0.8070 0.7218 0.5306 0.0244  0.1056  -0.1005 336 LEU A N   
2005 C CA  . LEU A 261 ? 0.7916 0.7416 0.5556 0.0470  0.1091  -0.0938 336 LEU A CA  
2006 C C   . LEU A 261 ? 0.6967 0.7065 0.4879 0.0379  0.1104  -0.0906 336 LEU A C   
2007 O O   . LEU A 261 ? 0.7641 0.7852 0.5758 0.0361  0.1070  -0.0804 336 LEU A O   
2008 C CB  . LEU A 261 ? 0.7383 0.6933 0.5220 0.0790  0.1176  -0.1108 336 LEU A CB  
2009 C CG  . LEU A 261 ? 0.7055 0.5917 0.4686 0.1044  0.1151  -0.1057 336 LEU A CG  
2010 C CD1 . LEU A 261 ? 0.7929 0.6898 0.5813 0.1410  0.1194  -0.1170 336 LEU A CD1 
2011 C CD2 . LEU A 261 ? 0.8084 0.6879 0.5873 0.1028  0.1020  -0.0721 336 LEU A CD2 
2012 N N   . VAL A 262 ? 0.7290 0.7484 0.5110 0.0300  0.1211  -0.0948 337 VAL A N   
2013 C CA  . VAL A 262 ? 0.7448 0.7963 0.5498 0.0130  0.1288  -0.0894 337 VAL A CA  
2014 C C   . VAL A 262 ? 0.7107 0.7463 0.5056 -0.0112 0.1163  -0.0712 337 VAL A C   
2015 O O   . VAL A 262 ? 0.6659 0.7218 0.4844 -0.0196 0.1159  -0.0693 337 VAL A O   
2016 C CB  . VAL A 262 ? 0.7624 0.8313 0.5589 0.0016  0.1483  -0.0973 337 VAL A CB  
2017 C CG1 . VAL A 262 ? 0.7117 0.8122 0.5307 -0.0271 0.1597  -0.0927 337 VAL A CG1 
2018 C CG2 . VAL A 262 ? 0.7115 0.7997 0.5237 0.0295  0.1623  -0.1160 337 VAL A CG2 
2019 N N   . MET A 263 ? 0.7903 0.7880 0.5502 -0.0222 0.1046  -0.0604 338 MET A N   
2020 C CA  . MET A 263 ? 0.6272 0.6045 0.3751 -0.0383 0.0904  -0.0404 338 MET A CA  
2021 C C   . MET A 263 ? 0.6009 0.5835 0.3690 -0.0251 0.0798  -0.0341 338 MET A C   
2022 O O   . MET A 263 ? 0.7680 0.7534 0.5420 -0.0307 0.0751  -0.0262 338 MET A O   
2023 C CB  . MET A 263 ? 0.6531 0.5959 0.3629 -0.0482 0.0764  -0.0320 338 MET A CB  
2024 C CG  . MET A 263 ? 0.6652 0.6025 0.3436 -0.0596 0.0849  -0.0339 338 MET A CG  
2025 S SD  . MET A 263 ? 0.9606 0.8653 0.5917 -0.0661 0.0631  -0.0313 338 MET A SD  
2026 C CE  . MET A 263 ? 1.1628 1.0572 0.8032 -0.0695 0.0381  -0.0062 338 MET A CE  
2027 N N   . MET A 264 ? 0.6834 0.6611 0.4548 -0.0070 0.0786  -0.0375 339 MET A N   
2028 C CA  . MET A 264 ? 0.5572 0.5449 0.3548 0.0123  0.0676  -0.0247 339 MET A CA  
2029 C C   . MET A 264 ? 0.5467 0.5762 0.3743 0.0307  0.0718  -0.0362 339 MET A C   
2030 O O   . MET A 264 ? 0.5987 0.6422 0.4408 0.0427  0.0614  -0.0288 339 MET A O   
2031 C CB  . MET A 264 ? 0.4961 0.4630 0.2963 0.0268  0.0657  -0.0182 339 MET A CB  
2032 C CG  . MET A 264 ? 0.6139 0.5428 0.3916 0.0052  0.0579  -0.0150 339 MET A CG  
2033 S SD  . MET A 264 ? 0.6825 0.5752 0.4703 0.0142  0.0580  -0.0089 339 MET A SD  
2034 C CE  . MET A 264 ? 0.7029 0.6202 0.5229 0.0260  0.0537  0.0230  339 MET A CE  
2035 N N   . LEU A 265 ? 0.6492 0.7019 0.4903 0.0334  0.0847  -0.0562 340 LEU A N   
2036 C CA  . LEU A 265 ? 0.6085 0.7048 0.4895 0.0484  0.0819  -0.0690 340 LEU A CA  
2037 C C   . LEU A 265 ? 0.6227 0.7465 0.5183 0.0241  0.0873  -0.0820 340 LEU A C   
2038 O O   . LEU A 265 ? 0.6775 0.8491 0.6111 0.0286  0.0879  -0.1012 340 LEU A O   
2039 C CB  . LEU A 265 ? 0.5534 0.6656 0.4522 0.0674  0.0887  -0.0811 340 LEU A CB  
2040 C CG  . LEU A 265 ? 0.5533 0.6402 0.4412 0.0950  0.0839  -0.0708 340 LEU A CG  
2041 C CD1 . LEU A 265 ? 0.6163 0.7196 0.5214 0.1190  0.0880  -0.0839 340 LEU A CD1 
2042 C CD2 . LEU A 265 ? 0.6198 0.7098 0.5097 0.1153  0.0683  -0.0521 340 LEU A CD2 
2043 N N   . GLU A 266 ? 0.7782 0.8726 0.6460 -0.0049 0.0904  -0.0720 341 GLU A N   
2044 C CA  . GLU A 266 ? 0.6123 0.7117 0.4933 -0.0345 0.0958  -0.0776 341 GLU A CA  
2045 C C   . GLU A 266 ? 0.5187 0.6402 0.4329 -0.0221 0.0779  -0.0899 341 GLU A C   
2046 O O   . GLU A 266 ? 0.6379 0.7386 0.5398 -0.0026 0.0601  -0.0783 341 GLU A O   
2047 C CB  . GLU A 266 ? 0.6162 0.6575 0.4544 -0.0598 0.0949  -0.0534 341 GLU A CB  
2048 C CG  . GLU A 266 ? 0.6846 0.7073 0.5306 -0.0874 0.0966  -0.0515 341 GLU A CG  
2049 C CD  . GLU A 266 ? 0.8202 0.8789 0.6955 -0.1164 0.1223  -0.0681 341 GLU A CD  
2050 O OE1 . GLU A 266 ? 0.9462 1.0265 0.8106 -0.1220 0.1447  -0.0707 341 GLU A OE1 
2051 O OE2 . GLU A 266 ? 0.9693 1.0375 0.8815 -0.1341 0.1206  -0.0811 341 GLU A OE2 
2052 N N   . PRO A 267 ? 0.4921 0.6612 0.4500 -0.0319 0.0815  -0.1160 342 PRO A N   
2053 C CA  . PRO A 267 ? 0.4957 0.6888 0.4821 -0.0173 0.0594  -0.1356 342 PRO A CA  
2054 C C   . PRO A 267 ? 0.7069 0.8441 0.6749 -0.0294 0.0463  -0.1263 342 PRO A C   
2055 O O   . PRO A 267 ? 0.6310 0.7669 0.5934 -0.0002 0.0261  -0.1304 342 PRO A O   
2056 C CB  . PRO A 267 ? 0.6035 0.8600 0.6467 -0.0379 0.0669  -0.1682 342 PRO A CB  
2057 C CG  . PRO A 267 ? 0.5570 0.8420 0.6037 -0.0417 0.0929  -0.1660 342 PRO A CG  
2058 C CD  . PRO A 267 ? 0.6459 0.8608 0.6337 -0.0532 0.1054  -0.1331 342 PRO A CD  
2059 N N   . ASP A 268 ? 0.6874 0.7765 0.6413 -0.0675 0.0583  -0.1129 343 ASP A N   
2060 C CA  . ASP A 268 ? 0.5991 0.6261 0.5347 -0.0751 0.0452  -0.1042 343 ASP A CA  
2061 C C   . ASP A 268 ? 0.6167 0.6060 0.5086 -0.0485 0.0349  -0.0751 343 ASP A C   
2062 O O   . ASP A 268 ? 0.6602 0.6274 0.5209 -0.0575 0.0450  -0.0505 343 ASP A O   
2063 C CB  . ASP A 268 ? 0.7575 0.7375 0.6868 -0.1229 0.0629  -0.0931 343 ASP A CB  
2064 C CG  . ASP A 268 ? 0.9063 0.8211 0.8310 -0.1323 0.0481  -0.0947 343 ASP A CG  
2065 O OD1 . ASP A 268 ? 1.0272 0.9131 0.9288 -0.0985 0.0271  -0.0887 343 ASP A OD1 
2066 O OD2 . ASP A 268 ? 1.1218 1.0135 1.0683 -0.1738 0.0592  -0.1026 343 ASP A OD2 
2067 N N   . PRO A 269 ? 0.6852 0.6726 0.5751 -0.0158 0.0152  -0.0792 344 PRO A N   
2068 C CA  . PRO A 269 ? 0.6746 0.6421 0.5356 0.0080  0.0079  -0.0521 344 PRO A CA  
2069 C C   . PRO A 269 ? 0.6876 0.5930 0.5179 -0.0078 0.0059  -0.0277 344 PRO A C   
2070 O O   . PRO A 269 ? 0.8455 0.7439 0.6548 0.0014  0.0021  -0.0039 344 PRO A O   
2071 C CB  . PRO A 269 ? 0.5760 0.5616 0.4448 0.0456  -0.0082 -0.0661 344 PRO A CB  
2072 C CG  . PRO A 269 ? 0.6251 0.6084 0.5151 0.0349  -0.0156 -0.1004 344 PRO A CG  
2073 C CD  . PRO A 269 ? 0.5337 0.5430 0.4479 0.0015  -0.0011 -0.1113 344 PRO A CD  
2074 N N   . LYS A 270 ? 0.8738 0.7325 0.7014 -0.0312 0.0067  -0.0323 345 LYS A N   
2075 C CA  . LYS A 270 ? 0.7604 0.5513 0.5498 -0.0429 0.0049  -0.0037 345 LYS A CA  
2076 C C   . LYS A 270 ? 0.7877 0.5774 0.5468 -0.0651 0.0203  0.0195  345 LYS A C   
2077 O O   . LYS A 270 ? 0.8805 0.6371 0.6004 -0.0594 0.0122  0.0466  345 LYS A O   
2078 C CB  . LYS A 270 ? 0.8761 0.6064 0.6676 -0.0683 0.0070  -0.0110 345 LYS A CB  
2079 C CG  . LYS A 270 ? 1.0744 0.8039 0.8952 -0.0494 -0.0097 -0.0450 345 LYS A CG  
2080 C CD  . LYS A 270 ? 1.1252 0.7857 0.9529 -0.0832 -0.0074 -0.0557 345 LYS A CD  
2081 C CE  . LYS A 270 ? 1.2084 0.8656 1.0631 -0.0644 -0.0279 -0.0985 345 LYS A CE  
2082 N NZ  . LYS A 270 ? 1.5351 1.1129 1.4000 -0.1020 -0.0275 -0.1119 345 LYS A NZ  
2083 N N   . LEU A 271 ? 0.9074 0.7371 0.6827 -0.0864 0.0408  0.0066  346 LEU A N   
2084 C CA  . LEU A 271 ? 0.7438 0.5757 0.4872 -0.1055 0.0588  0.0215  346 LEU A CA  
2085 C C   . LEU A 271 ? 0.8270 0.7009 0.5699 -0.0850 0.0552  0.0178  346 LEU A C   
2086 O O   . LEU A 271 ? 0.8286 0.7029 0.5410 -0.0958 0.0665  0.0244  346 LEU A O   
2087 C CB  . LEU A 271 ? 0.7550 0.6084 0.5183 -0.1401 0.0879  0.0081  346 LEU A CB  
2088 C CG  . LEU A 271 ? 0.7863 0.6028 0.5669 -0.1701 0.0951  0.0060  346 LEU A CG  
2089 C CD1 . LEU A 271 ? 0.7692 0.6302 0.5867 -0.2069 0.1262  -0.0105 346 LEU A CD1 
2090 C CD2 . LEU A 271 ? 0.8033 0.5345 0.5260 -0.1814 0.0942  0.0431  346 LEU A CD2 
2091 N N   . ARG A 272 ? 0.7828 0.6873 0.5551 -0.0562 0.0411  0.0075  347 ARG A N   
2092 C CA  . ARG A 272 ? 0.7216 0.6562 0.4974 -0.0401 0.0400  0.0063  347 ARG A CA  
2093 C C   . ARG A 272 ? 0.6757 0.5888 0.4235 -0.0359 0.0249  0.0275  347 ARG A C   
2094 O O   . ARG A 272 ? 0.8738 0.7689 0.6169 -0.0256 0.0083  0.0412  347 ARG A O   
2095 C CB  . ARG A 272 ? 0.5593 0.5314 0.3711 -0.0113 0.0335  -0.0058 347 ARG A CB  
2096 C CG  . ARG A 272 ? 0.6956 0.6898 0.5127 0.0038  0.0368  -0.0044 347 ARG A CG  
2097 C CD  . ARG A 272 ? 0.6826 0.7107 0.5253 0.0341  0.0335  -0.0115 347 ARG A CD  
2098 N NE  . ARG A 272 ? 0.4994 0.5544 0.3625 0.0360  0.0362  -0.0360 347 ARG A NE  
2099 C CZ  . ARG A 272 ? 0.4418 0.5213 0.3203 0.0582  0.0260  -0.0486 347 ARG A CZ  
2100 N NH1 . ARG A 272 ? 0.4886 0.5687 0.3602 0.0830  0.0171  -0.0366 347 ARG A NH1 
2101 N NH2 . ARG A 272 ? 0.5918 0.7017 0.4943 0.0555  0.0248  -0.0761 347 ARG A NH2 
2102 N N   . ALA A 273 ? 0.7547 0.6721 0.4864 -0.0420 0.0287  0.0267  348 ALA A N   
2103 C CA  . ALA A 273 ? 0.7490 0.6586 0.4689 -0.0400 0.0102  0.0395  348 ALA A CA  
2104 C C   . ALA A 273 ? 0.7568 0.6871 0.5062 -0.0212 -0.0034 0.0472  348 ALA A C   
2105 O O   . ALA A 273 ? 0.7913 0.7452 0.5718 -0.0066 0.0050  0.0408  348 ALA A O   
2106 C CB  . ALA A 273 ? 0.7384 0.6491 0.4464 -0.0492 0.0154  0.0282  348 ALA A CB  
2107 N N   . THR A 274 ? 0.8047 0.7346 0.5502 -0.0185 -0.0240 0.0615  349 THR A N   
2108 C CA  . THR A 274 ? 0.6231 0.5867 0.4094 -0.0024 -0.0337 0.0699  349 THR A CA  
2109 C C   . THR A 274 ? 0.7747 0.7510 0.5750 -0.0164 -0.0368 0.0680  349 THR A C   
2110 O O   . THR A 274 ? 0.7691 0.7238 0.5411 -0.0350 -0.0372 0.0573  349 THR A O   
2111 C CB  . THR A 274 ? 0.6691 0.6365 0.4560 0.0117  -0.0552 0.0843  349 THR A CB  
2112 O OG1 . THR A 274 ? 0.6560 0.6090 0.4125 -0.0012 -0.0725 0.0887  349 THR A OG1 
2113 C CG2 . THR A 274 ? 0.6611 0.6001 0.4336 0.0252  -0.0524 0.0844  349 THR A CG2 
2114 N N   . ALA A 275 ? 0.6283 0.6390 0.4729 -0.0082 -0.0374 0.0776  350 ALA A N   
2115 C CA  . ALA A 275 ? 0.4688 0.4870 0.3360 -0.0274 -0.0398 0.0772  350 ALA A CA  
2116 C C   . ALA A 275 ? 0.5635 0.5804 0.4174 -0.0469 -0.0667 0.0718  350 ALA A C   
2117 O O   . ALA A 275 ? 0.7205 0.7176 0.5640 -0.0692 -0.0714 0.0576  350 ALA A O   
2118 C CB  . ALA A 275 ? 0.4877 0.5487 0.4083 -0.0183 -0.0318 0.0941  350 ALA A CB  
2119 N N   . GLU A 276 ? 0.6064 0.6417 0.4566 -0.0353 -0.0873 0.0809  351 GLU A N   
2120 C CA  . GLU A 276 ? 0.5295 0.5696 0.3613 -0.0476 -0.1185 0.0764  351 GLU A CA  
2121 C C   . GLU A 276 ? 0.6841 0.6744 0.4428 -0.0583 -0.1194 0.0641  351 GLU A C   
2122 O O   . GLU A 276 ? 0.7399 0.7245 0.4746 -0.0758 -0.1378 0.0495  351 GLU A O   
2123 C CB  . GLU A 276 ? 0.6160 0.6870 0.4584 -0.0235 -0.1413 0.0919  351 GLU A CB  
2124 C CG  . GLU A 276 ? 0.9426 1.0838 0.8561 -0.0235 -0.1578 0.0966  351 GLU A CG  
2125 C CD  . GLU A 276 ? 1.2403 1.4176 1.1690 0.0108  -0.1781 0.1107  351 GLU A CD  
2126 O OE1 . GLU A 276 ? 1.0783 1.2132 0.9528 0.0287  -0.1899 0.1110  351 GLU A OE1 
2127 O OE2 . GLU A 276 ? 1.1505 1.3913 1.1461 0.0233  -0.1745 0.1179  351 GLU A OE2 
2128 N N   . ALA A 277 ? 0.7358 0.6935 0.4591 -0.0490 -0.0990 0.0679  352 ALA A N   
2129 C CA  . ALA A 277 ? 0.7713 0.6945 0.4443 -0.0564 -0.0870 0.0563  352 ALA A CA  
2130 C C   . ALA A 277 ? 0.6314 0.5397 0.2855 -0.0762 -0.0781 0.0343  352 ALA A C   
2131 O O   . ALA A 277 ? 0.8307 0.7263 0.4500 -0.0842 -0.0835 0.0193  352 ALA A O   
2132 C CB  . ALA A 277 ? 0.7024 0.6082 0.3733 -0.0466 -0.0606 0.0613  352 ALA A CB  
2133 N N   . LEU A 278 ? 0.7426 0.6568 0.4377 -0.0749 -0.0598 0.0293  353 LEU A N   
2134 C CA  . LEU A 278 ? 0.7614 0.6556 0.4527 -0.0851 -0.0482 0.0069  353 LEU A CA  
2135 C C   . LEU A 278 ? 0.6610 0.5535 0.3593 -0.1039 -0.0735 -0.0061 353 LEU A C   
2136 O O   . LEU A 278 ? 0.9053 0.7707 0.5636 -0.1150 -0.0779 -0.0312 353 LEU A O   
2137 C CB  . LEU A 278 ? 0.6946 0.5938 0.4302 -0.0729 -0.0258 0.0105  353 LEU A CB  
2138 C CG  . LEU A 278 ? 0.6351 0.5407 0.3675 -0.0558 -0.0035 0.0131  353 LEU A CG  
2139 C CD1 . LEU A 278 ? 0.6501 0.5710 0.4249 -0.0373 0.0096  0.0209  353 LEU A CD1 
2140 C CD2 . LEU A 278 ? 0.7694 0.6569 0.4630 -0.0589 0.0138  -0.0079 353 LEU A CD2 
2141 N N   . LEU A 279 ? 0.6286 0.5544 0.3802 -0.1084 -0.0906 0.0076  354 LEU A N   
2142 C CA  . LEU A 279 ? 0.5301 0.4636 0.3048 -0.1327 -0.1165 -0.0068 354 LEU A CA  
2143 C C   . LEU A 279 ? 0.6262 0.5578 0.3462 -0.1403 -0.1484 -0.0242 354 LEU A C   
2144 O O   . LEU A 279 ? 0.7164 0.6464 0.4417 -0.1626 -0.1728 -0.0483 354 LEU A O   
2145 C CB  . LEU A 279 ? 0.6636 0.6510 0.5134 -0.1358 -0.1262 0.0140  354 LEU A CB  
2146 C CG  . LEU A 279 ? 0.5967 0.5867 0.5013 -0.1355 -0.0971 0.0300  354 LEU A CG  
2147 C CD1 . LEU A 279 ? 0.4772 0.5328 0.4456 -0.1288 -0.0991 0.0553  354 LEU A CD1 
2148 C CD2 . LEU A 279 ? 0.5044 0.4574 0.4276 -0.1651 -0.0951 0.0132  354 LEU A CD2 
2149 N N   . ALA A 280 ? 0.8272 0.7561 0.4922 -0.1229 -0.1498 -0.0127 355 ALA A N   
2150 C CA  . ALA A 280 ? 0.7454 0.6719 0.3561 -0.1192 -0.1710 -0.0236 355 ALA A CA  
2151 C C   . ALA A 280 ? 0.7980 0.6880 0.3547 -0.1154 -0.1462 -0.0438 355 ALA A C   
2152 O O   . ALA A 280 ? 0.7817 0.6750 0.2969 -0.1058 -0.1547 -0.0511 355 ALA A O   
2153 C CB  . ALA A 280 ? 0.7822 0.7275 0.3861 -0.0918 -0.1743 0.0047  355 ALA A CB  
2154 N N   . LEU A 281 ? 0.9258 0.7884 0.4828 -0.1191 -0.1158 -0.0525 356 LEU A N   
2155 C CA  . LEU A 281 ? 0.8159 0.6567 0.3345 -0.1116 -0.0916 -0.0734 356 LEU A CA  
2156 C C   . LEU A 281 ? 0.9411 0.7649 0.4446 -0.1229 -0.1108 -0.1111 356 LEU A C   
2157 O O   . LEU A 281 ? 0.9998 0.8170 0.5372 -0.1435 -0.1339 -0.1233 356 LEU A O   
2158 C CB  . LEU A 281 ? 0.9432 0.7693 0.4772 -0.1058 -0.0555 -0.0743 356 LEU A CB  
2159 C CG  . LEU A 281 ? 0.9441 0.7895 0.4965 -0.0933 -0.0329 -0.0459 356 LEU A CG  
2160 C CD1 . LEU A 281 ? 0.9971 0.8403 0.5715 -0.0848 -0.0018 -0.0531 356 LEU A CD1 
2161 C CD2 . LEU A 281 ? 0.8558 0.7110 0.3783 -0.0855 -0.0257 -0.0352 356 LEU A CD2 
2162 N N   . PRO A 282 ? 0.9889 0.8080 0.4472 -0.1111 -0.1019 -0.1312 357 PRO A N   
2163 C CA  . PRO A 282 ? 0.9348 0.7374 0.3782 -0.1181 -0.1215 -0.1732 357 PRO A CA  
2164 C C   . PRO A 282 ? 0.9059 0.6655 0.3801 -0.1288 -0.1126 -0.1974 357 PRO A C   
2165 O O   . PRO A 282 ? 1.0929 0.8330 0.5843 -0.1459 -0.1372 -0.2265 357 PRO A O   
2166 C CB  . PRO A 282 ? 1.0841 0.8954 0.4684 -0.0972 -0.1048 -0.1860 357 PRO A CB  
2167 C CG  . PRO A 282 ? 0.9424 0.7788 0.3117 -0.0859 -0.0887 -0.1447 357 PRO A CG  
2168 C CD  . PRO A 282 ? 0.9899 0.8225 0.4110 -0.0924 -0.0758 -0.1170 357 PRO A CD  
2169 N N   . VAL A 283 ? 0.9894 0.7331 0.4753 -0.1182 -0.0784 -0.1866 358 VAL A N   
2170 C CA  . VAL A 283 ? 1.1112 0.8058 0.6209 -0.1204 -0.0671 -0.2067 358 VAL A CA  
2171 C C   . VAL A 283 ? 1.1478 0.8200 0.7068 -0.1488 -0.0853 -0.1962 358 VAL A C   
2172 O O   . VAL A 283 ? 1.2108 0.8310 0.7948 -0.1575 -0.0836 -0.2127 358 VAL A O   
2173 C CB  . VAL A 283 ? 1.0428 0.7379 0.5550 -0.0950 -0.0271 -0.1969 358 VAL A CB  
2174 C CG1 . VAL A 283 ? 1.2317 0.9592 0.7105 -0.0721 -0.0082 -0.2069 358 VAL A CG1 
2175 C CG2 . VAL A 283 ? 0.9301 0.6523 0.4650 -0.0969 -0.0178 -0.1586 358 VAL A CG2 
2176 N N   . LEU A 284 ? 1.1023 0.8163 0.6859 -0.1612 -0.1008 -0.1653 359 LEU A N   
2177 C CA  . LEU A 284 ? 0.9414 0.6715 0.6062 -0.1789 -0.1097 -0.1419 359 LEU A CA  
2178 C C   . LEU A 284 ? 1.2624 1.0220 0.9477 -0.2082 -0.1528 -0.1519 359 LEU A C   
2179 O O   . LEU A 284 ? 1.2482 1.0598 0.9905 -0.2160 -0.1640 -0.1241 359 LEU A O   
2180 C CB  . LEU A 284 ? 0.8534 0.6276 0.5540 -0.1607 -0.0905 -0.0977 359 LEU A CB  
2181 C CG  . LEU A 284 ? 0.6635 0.4186 0.3626 -0.1338 -0.0527 -0.0887 359 LEU A CG  
2182 C CD1 . LEU A 284 ? 0.6151 0.4161 0.3368 -0.1156 -0.0397 -0.0540 359 LEU A CD1 
2183 C CD2 . LEU A 284 ? 0.8695 0.5810 0.6072 -0.1372 -0.0408 -0.0891 359 LEU A CD2 
2184 N N   . ARG A 285 ? 1.3457 1.0868 0.9968 -0.2159 -0.1744 -0.1915 360 ARG A N   
2185 C CA  . ARG A 285 ? 1.4153 1.1994 1.0983 -0.2350 -0.2146 -0.2052 360 ARG A CA  
2186 C C   . ARG A 285 ? 1.5546 1.3315 1.3248 -0.2732 -0.2237 -0.2078 360 ARG A C   
2187 O O   . ARG A 285 ? 1.4054 1.1189 1.1919 -0.2829 -0.2036 -0.2179 360 ARG A O   
2188 C CB  . ARG A 285 ? 1.5289 1.3054 1.1612 -0.2236 -0.2292 -0.2485 360 ARG A CB  
2189 C CG  . ARG A 285 ? 1.6471 1.3561 1.2715 -0.2255 -0.2137 -0.2856 360 ARG A CG  
2190 C CD  . ARG A 285 ? 1.6839 1.3965 1.2831 -0.2266 -0.2393 -0.3368 360 ARG A CD  
2191 N NE  . ARG A 285 ? 1.7700 1.5008 1.2870 -0.1930 -0.2307 -0.3460 360 ARG A NE  
2192 C CZ  . ARG A 285 ? 1.8453 1.5830 1.3208 -0.1869 -0.2449 -0.3906 360 ARG A CZ  
2193 N NH1 . ARG A 285 ? 1.5648 1.2908 1.0721 -0.2134 -0.2703 -0.4354 360 ARG A NH1 
2194 N NH2 . ARG A 285 ? 1.8915 1.6517 1.2935 -0.1572 -0.2306 -0.3906 360 ARG A NH2 
2195 N N   . GLN A 286 ? 1.5808 1.4265 1.4118 -0.2915 -0.2512 -0.1958 361 GLN A N   
2196 C CA  . GLN A 286 ? 1.3759 1.2413 1.3064 -0.3308 -0.2593 -0.1958 361 GLN A CA  
2197 C C   . GLN A 286 ? 1.3086 1.0993 1.2734 -0.3504 -0.2268 -0.1915 361 GLN A C   
2198 O O   . GLN A 286 ? 1.3167 1.0837 1.3305 -0.3788 -0.2316 -0.2158 361 GLN A O   
2199 C CB  . GLN A 286 ? 1.0938 0.9897 1.0438 -0.3464 -0.2970 -0.2411 361 GLN A CB  
2200 C CG  . GLN A 286 ? 1.4933 1.3308 1.3718 -0.3344 -0.3010 -0.2896 361 GLN A CG  
2201 C CD  . GLN A 286 ? 1.6862 1.5667 1.5776 -0.3486 -0.3411 -0.3376 361 GLN A CD  
2202 O OE1 . GLN A 286 ? 1.8146 1.7737 1.7647 -0.3636 -0.3681 -0.3344 361 GLN A OE1 
2203 N NE2 . GLN A 286 ? 1.5889 1.4256 1.4261 -0.3429 -0.3442 -0.3851 361 GLN A NE2 
2204 N N   . ALA B 1   ? 1.1916 0.9708 1.1444 -0.2789 -0.3288 0.0088  76  ALA B N   
2205 C CA  . ALA B 1   ? 0.9666 0.7399 0.9417 -0.2627 -0.3071 -0.0063 76  ALA B CA  
2206 C C   . ALA B 1   ? 1.1226 0.9595 1.1644 -0.2365 -0.2869 -0.0019 76  ALA B C   
2207 O O   . ALA B 1   ? 1.0292 0.9360 1.1318 -0.2319 -0.2939 0.0264  76  ALA B O   
2208 C CB  . ALA B 1   ? 0.9984 0.7755 0.9981 -0.2785 -0.3223 0.0145  76  ALA B CB  
2209 N N   . LEU B 2   ? 1.1658 0.9775 1.1950 -0.2169 -0.2615 -0.0300 77  LEU B N   
2210 C CA  . LEU B 2   ? 0.8990 0.7685 0.9839 -0.1847 -0.2337 -0.0255 77  LEU B CA  
2211 C C   . LEU B 2   ? 1.0388 0.9632 1.1983 -0.1801 -0.2340 -0.0003 77  LEU B C   
2212 O O   . LEU B 2   ? 1.3437 1.2477 1.5068 -0.1981 -0.2468 0.0049  77  LEU B O   
2213 C CB  . LEU B 2   ? 0.8501 0.6907 0.9062 -0.1575 -0.1962 -0.0563 77  LEU B CB  
2214 C CG  . LEU B 2   ? 1.0397 0.8498 1.0317 -0.1554 -0.1835 -0.0795 77  LEU B CG  
2215 C CD1 . LEU B 2   ? 0.8909 0.6938 0.8726 -0.1269 -0.1445 -0.1045 77  LEU B CD1 
2216 C CD2 . LEU B 2   ? 0.9201 0.7698 0.9237 -0.1558 -0.1902 -0.0624 77  LEU B CD2 
2217 N N   . GLN B 3   ? 0.7888 0.7792 1.0018 -0.1568 -0.2203 0.0155  78  GLN B N   
2218 C CA  . GLN B 3   ? 0.6965 0.7487 0.9781 -0.1493 -0.2154 0.0395  78  GLN B CA  
2219 C C   . GLN B 3   ? 0.5458 0.6199 0.8479 -0.1128 -0.1799 0.0317  78  GLN B C   
2220 O O   . GLN B 3   ? 0.6164 0.6786 0.8940 -0.0942 -0.1657 0.0175  78  GLN B O   
2221 C CB  . GLN B 3   ? 0.8971 1.0164 1.2240 -0.1531 -0.2338 0.0706  78  GLN B CB  
2222 C CG  . GLN B 3   ? 0.8385 0.9441 1.1436 -0.1852 -0.2609 0.0852  78  GLN B CG  
2223 C CD  . GLN B 3   ? 1.0726 1.2458 1.4189 -0.1801 -0.2698 0.1143  78  GLN B CD  
2224 O OE1 . GLN B 3   ? 1.2538 1.4715 1.6319 -0.1497 -0.2573 0.1186  78  GLN B OE1 
2225 N NE2 . GLN B 3   ? 1.1727 1.3500 1.5160 -0.2081 -0.2917 0.1340  78  GLN B NE2 
2226 N N   . PRO B 4   ? 0.5969 0.7001 0.9387 -0.1062 -0.1676 0.0426  79  PRO B N   
2227 C CA  . PRO B 4   ? 0.4027 0.5250 0.7603 -0.0746 -0.1372 0.0375  79  PRO B CA  
2228 C C   . PRO B 4   ? 0.3987 0.5778 0.7893 -0.0525 -0.1319 0.0527  79  PRO B C   
2229 O O   . PRO B 4   ? 0.6281 0.8531 1.0506 -0.0583 -0.1474 0.0736  79  PRO B O   
2230 C CB  . PRO B 4   ? 0.3808 0.5117 0.7645 -0.0812 -0.1317 0.0475  79  PRO B CB  
2231 C CG  . PRO B 4   ? 0.5180 0.6748 0.9257 -0.1123 -0.1584 0.0713  79  PRO B CG  
2232 C CD  . PRO B 4   ? 0.6040 0.7205 0.9723 -0.1320 -0.1832 0.0621  79  PRO B CD  
2233 N N   . ARG B 5   ? 0.4346 0.6079 0.8138 -0.0256 -0.1103 0.0419  80  ARG B N   
2234 C CA  . ARG B 5   ? 0.2509 0.4610 0.6488 0.0019  -0.1033 0.0515  80  ARG B CA  
2235 C C   . ARG B 5   ? 0.2492 0.4696 0.6520 0.0209  -0.0766 0.0511  80  ARG B C   
2236 O O   . ARG B 5   ? 0.4174 0.6069 0.8024 0.0246  -0.0649 0.0377  80  ARG B O   
2237 C CB  . ARG B 5   ? 0.3741 0.5493 0.7301 0.0124  -0.1071 0.0392  80  ARG B CB  
2238 C CG  . ARG B 5   ? 0.5407 0.7347 0.9040 0.0448  -0.1018 0.0460  80  ARG B CG  
2239 C CD  . ARG B 5   ? 0.5121 0.6601 0.8257 0.0502  -0.1097 0.0361  80  ARG B CD  
2240 N NE  . ARG B 5   ? 0.6016 0.7534 0.9142 0.0836  -0.1083 0.0414  80  ARG B NE  
2241 C CZ  . ARG B 5   ? 0.4920 0.6263 0.7867 0.1021  -0.0908 0.0350  80  ARG B CZ  
2242 N NH1 . ARG B 5   ? 0.5856 0.7052 0.8689 0.0897  -0.0741 0.0257  80  ARG B NH1 
2243 N NH2 . ARG B 5   ? 0.7326 0.8603 1.0166 0.1344  -0.0917 0.0379  80  ARG B NH2 
2244 N N   . ARG B 6   ? 0.2547 0.5139 0.6674 0.0308  -0.0659 0.0635  81  ARG B N   
2245 C CA  . ARG B 6   ? 0.2104 0.4744 0.6129 0.0449  -0.0428 0.0617  81  ARG B CA  
2246 C C   . ARG B 6   ? 0.3025 0.5417 0.6731 0.0715  -0.0330 0.0498  81  ARG B C   
2247 O O   . ARG B 6   ? 0.5323 0.7760 0.8962 0.0907  -0.0386 0.0491  81  ARG B O   
2248 C CB  . ARG B 6   ? 0.3046 0.6209 0.7288 0.0482  -0.0358 0.0751  81  ARG B CB  
2249 C CG  . ARG B 6   ? 0.4046 0.7292 0.8181 0.0644  -0.0141 0.0727  81  ARG B CG  
2250 C CD  . ARG B 6   ? 0.7424 1.1249 1.1853 0.0639  -0.0068 0.0870  81  ARG B CD  
2251 N NE  . ARG B 6   ? 1.0199 1.4367 1.4831 0.0765  -0.0151 0.0905  81  ARG B NE  
2252 C CZ  . ARG B 6   ? 0.8443 1.2791 1.3089 0.1081  -0.0057 0.0846  81  ARG B CZ  
2253 N NH1 . ARG B 6   ? 0.6820 1.1017 1.1251 0.1289  0.0130  0.0751  81  ARG B NH1 
2254 N NH2 . ARG B 6   ? 0.3497 0.8157 0.8385 0.1193  -0.0167 0.0896  81  ARG B NH2 
2255 N N   . VAL B 7   ? 0.4394 0.6491 0.7893 0.0719  -0.0216 0.0419  82  VAL B N   
2256 C CA  . VAL B 7   ? 0.2991 0.4814 0.6154 0.0922  -0.0144 0.0334  82  VAL B CA  
2257 C C   . VAL B 7   ? 0.5287 0.7317 0.8408 0.1084  -0.0004 0.0358  82  VAL B C   
2258 O O   . VAL B 7   ? 0.5967 0.7970 0.9059 0.1022  0.0101  0.0377  82  VAL B O   
2259 C CB  . VAL B 7   ? 0.3243 0.4699 0.6246 0.0818  -0.0120 0.0251  82  VAL B CB  
2260 C CG1 . VAL B 7   ? 0.4114 0.5278 0.6789 0.0984  -0.0088 0.0206  82  VAL B CG1 
2261 C CG2 . VAL B 7   ? 0.3554 0.4881 0.6671 0.0676  -0.0247 0.0183  82  VAL B CG2 
2262 N N   . SER B 8   ? 0.8235 1.0469 1.1395 0.1299  -0.0014 0.0352  83  SER B N   
2263 C CA  . SER B 8   ? 0.6292 0.8787 0.9529 0.1447  0.0135  0.0367  83  SER B CA  
2264 C C   . SER B 8   ? 0.5571 0.7680 0.8447 0.1588  0.0244  0.0297  83  SER B C   
2265 O O   . SER B 8   ? 0.5598 0.7219 0.8155 0.1647  0.0165  0.0220  83  SER B O   
2266 C CB  . SER B 8   ? 0.6040 0.8798 0.9460 0.1666  0.0102  0.0371  83  SER B CB  
2267 O OG  . SER B 8   ? 0.8352 1.0665 1.1521 0.1863  -0.0016 0.0280  83  SER B OG  
2268 N N   . PHE B 9   ? 0.3703 0.6037 0.6608 0.1630  0.0428  0.0357  84  PHE B N   
2269 C CA  . PHE B 9   ? 0.7775 0.9782 1.0292 0.1777  0.0557  0.0326  84  PHE B CA  
2270 C C   . PHE B 9   ? 0.8127 1.0557 1.0710 0.1893  0.0783  0.0407  84  PHE B C   
2271 O O   . PHE B 9   ? 0.6879 0.9833 0.9842 0.1726  0.0834  0.0534  84  PHE B O   
2272 C CB  . PHE B 9   ? 0.4889 0.6613 0.7296 0.1580  0.0529  0.0355  84  PHE B CB  
2273 C CG  . PHE B 9   ? 0.6613 0.8688 0.9358 0.1329  0.0572  0.0490  84  PHE B CG  
2274 C CD1 . PHE B 9   ? 0.6492 0.8696 0.9519 0.1097  0.0443  0.0518  84  PHE B CD1 
2275 C CD2 . PHE B 9   ? 0.7431 0.9651 1.0158 0.1330  0.0736  0.0606  84  PHE B CD2 
2276 C CE1 . PHE B 9   ? 0.5757 0.8156 0.9042 0.0866  0.0446  0.0652  84  PHE B CE1 
2277 C CE2 . PHE B 9   ? 0.6993 0.9486 1.0033 0.1076  0.0740  0.0763  84  PHE B CE2 
2278 C CZ  . PHE B 9   ? 0.6147 0.8689 0.9458 0.0843  0.0578  0.0780  84  PHE B CZ  
2279 N N   . ARG B 10  ? 0.7769 0.9941 0.9915 0.2178  0.0916  0.0338  85  ARG B N   
2280 C CA  . ARG B 10  ? 0.7372 0.9930 0.9475 0.2324  0.1169  0.0399  85  ARG B CA  
2281 C C   . ARG B 10  ? 0.7523 1.0313 0.9743 0.2080  0.1271  0.0553  85  ARG B C   
2282 O O   . ARG B 10  ? 0.8073 1.0449 1.0049 0.2006  0.1238  0.0559  85  ARG B O   
2283 C CB  . ARG B 10  ? 0.7649 0.9704 0.9080 0.2683  0.1277  0.0260  85  ARG B CB  
2284 C CG  . ARG B 10  ? 0.8708 1.0550 1.0015 0.2958  0.1190  0.0136  85  ARG B CG  
2285 C CD  . ARG B 10  ? 1.2846 1.4136 1.3400 0.3312  0.1295  -0.0005 85  ARG B CD  
2286 N NE  . ARG B 10  ? 1.2509 1.3496 1.2889 0.3588  0.1185  -0.0115 85  ARG B NE  
2287 C CZ  . ARG B 10  ? 1.4735 1.5118 1.4412 0.3911  0.1208  -0.0257 85  ARG B CZ  
2288 N NH1 . ARG B 10  ? 1.5731 1.5715 1.4764 0.3997  0.1340  -0.0320 85  ARG B NH1 
2289 N NH2 . ARG B 10  ? 1.5150 1.5267 1.4719 0.4153  0.1080  -0.0335 85  ARG B NH2 
2290 N N   . GLY B 11  ? 0.6922 1.0373 0.9532 0.1941  0.1379  0.0706  86  GLY B N   
2291 C CA  . GLY B 11  ? 0.6265 0.9962 0.9015 0.1664  0.1449  0.0896  86  GLY B CA  
2292 C C   . GLY B 11  ? 0.7768 1.1611 1.0976 0.1281  0.1243  0.1021  86  GLY B C   
2293 O O   . GLY B 11  ? 0.6884 1.0785 1.0192 0.1019  0.1237  0.1186  86  GLY B O   
2294 N N   . GLU B 12  ? 0.8433 1.2283 1.1870 0.1239  0.1064  0.0952  87  GLU B N   
2295 C CA  . GLU B 12  ? 0.6803 1.0714 1.0559 0.0903  0.0871  0.1050  87  GLU B CA  
2296 C C   . GLU B 12  ? 0.7305 1.1819 1.1366 0.0696  0.0925  0.1270  87  GLU B C   
2297 O O   . GLU B 12  ? 0.7195 1.2192 1.1327 0.0842  0.1090  0.1315  87  GLU B O   
2298 C CB  . GLU B 12  ? 0.5659 0.9412 0.9495 0.0926  0.0683  0.0924  87  GLU B CB  
2299 C CG  . GLU B 12  ? 0.6243 1.0327 1.0188 0.1154  0.0725  0.0881  87  GLU B CG  
2300 C CD  . GLU B 12  ? 0.7800 1.1813 1.1885 0.1108  0.0514  0.0824  87  GLU B CD  
2301 O OE1 . GLU B 12  ? 0.7367 1.1120 1.1455 0.0881  0.0360  0.0827  87  GLU B OE1 
2302 O OE2 . GLU B 12  ? 0.9181 1.3392 1.3372 0.1311  0.0501  0.0786  87  GLU B OE2 
2303 N N   . ALA B 13  ? 0.6460 1.0919 1.0687 0.0350  0.0769  0.1412  88  ALA B N   
2304 C CA  . ALA B 13  ? 0.4646 0.9587 0.9092 0.0077  0.0776  0.1658  88  ALA B CA  
2305 C C   . ALA B 13  ? 0.6170 1.1547 1.0912 0.0018  0.0697  0.1724  88  ALA B C   
2306 O O   . ALA B 13  ? 0.7302 1.3247 1.2226 -0.0109 0.0769  0.1921  88  ALA B O   
2307 C CB  . ALA B 13  ? 0.5834 1.0441 1.0296 -0.0284 0.0584  0.1797  88  ALA B CB  
2308 N N   . SER B 14  ? 0.7262 1.2417 1.2055 0.0089  0.0543  0.1588  89  SER B N   
2309 C CA  . SER B 14  ? 0.9287 1.4836 1.4375 0.0001  0.0428  0.1682  89  SER B CA  
2310 C C   . SER B 14  ? 0.9102 1.4600 1.4184 0.0317  0.0421  0.1490  89  SER B C   
2311 O O   . SER B 14  ? 0.9041 1.4003 1.3895 0.0423  0.0345  0.1300  89  SER B O   
2312 C CB  . SER B 14  ? 0.9012 1.4300 1.4173 -0.0374 0.0147  0.1787  89  SER B CB  
2313 O OG  . SER B 14  ? 1.0407 1.6032 1.5818 -0.0472 0.0006  0.1886  89  SER B OG  
2314 N N   . GLU B 15  ? 1.1312 1.7384 1.6655 0.0461  0.0489  0.1558  90  GLU B N   
2315 C CA  . GLU B 15  ? 1.1106 1.7146 1.6485 0.0757  0.0442  0.1409  90  GLU B CA  
2316 C C   . GLU B 15  ? 1.0472 1.6332 1.5947 0.0566  0.0161  0.1422  90  GLU B C   
2317 O O   . GLU B 15  ? 0.9090 1.4677 1.4464 0.0755  0.0065  0.1271  90  GLU B O   
2318 C CB  . GLU B 15  ? 1.1757 1.8505 1.7449 0.0981  0.0586  0.1502  90  GLU B CB  
2319 C CG  . GLU B 15  ? 1.0945 1.7994 1.6552 0.1151  0.0890  0.1529  90  GLU B CG  
2320 C CD  . GLU B 15  ? 1.0269 1.7798 1.6046 0.0806  0.0949  0.1792  90  GLU B CD  
2321 O OE1 . GLU B 15  ? 1.0854 1.8059 1.6536 0.0452  0.0798  0.1867  90  GLU B OE1 
2322 O OE2 . GLU B 15  ? 0.7343 1.5571 1.3342 0.0890  0.1139  0.1931  90  GLU B OE2 
2323 N N   . THR B 16  ? 1.2132 1.8105 1.7759 0.0181  0.0009  0.1614  91  THR B N   
2324 C CA  . THR B 16  ? 1.1115 1.6893 1.6792 -0.0048 -0.0271 0.1654  91  THR B CA  
2325 C C   . THR B 16  ? 1.2146 1.7317 1.7577 -0.0321 -0.0394 0.1622  91  THR B C   
2326 O O   . THR B 16  ? 1.2472 1.7611 1.7870 -0.0510 -0.0353 0.1725  91  THR B O   
2327 C CB  . THR B 16  ? 1.0217 1.6582 1.6258 -0.0293 -0.0403 0.1927  91  THR B CB  
2328 O OG1 . THR B 16  ? 1.2840 1.9834 1.9178 -0.0002 -0.0274 0.1963  91  THR B OG1 
2329 C CG2 . THR B 16  ? 1.1139 1.7237 1.7167 -0.0544 -0.0721 0.1972  91  THR B CG2 
2330 N N   . LEU B 17  ? 1.0234 1.4925 1.5497 -0.0334 -0.0551 0.1487  92  LEU B N   
2331 C CA  . LEU B 17  ? 0.8228 1.2341 1.3307 -0.0584 -0.0700 0.1447  92  LEU B CA  
2332 C C   . LEU B 17  ? 0.9644 1.3778 1.4817 -0.0970 -0.0973 0.1635  92  LEU B C   
2333 O O   . LEU B 17  ? 0.7339 1.1412 1.2511 -0.1055 -0.1171 0.1637  92  LEU B O   
2334 C CB  . LEU B 17  ? 0.5303 0.8922 1.0165 -0.0443 -0.0746 0.1226  92  LEU B CB  
2335 C CG  . LEU B 17  ? 0.3983 0.7002 0.8673 -0.0568 -0.0806 0.1112  92  LEU B CG  
2336 C CD1 . LEU B 17  ? 0.4557 0.7513 0.9177 -0.0431 -0.0588 0.1079  92  LEU B CD1 
2337 C CD2 . LEU B 17  ? 0.3630 0.6260 0.8166 -0.0477 -0.0881 0.0914  92  LEU B CD2 
2338 N N   . GLN B 18  ? 0.9140 1.3318 1.4340 -0.1228 -0.1011 0.1807  93  GLN B N   
2339 C CA  . GLN B 18  ? 0.9011 1.3165 1.4221 -0.1624 -0.1290 0.2015  93  GLN B CA  
2340 C C   . GLN B 18  ? 0.6610 1.0337 1.1629 -0.1895 -0.1390 0.2093  93  GLN B C   
2341 O O   . GLN B 18  ? 0.6830 1.0460 1.1806 -0.1775 -0.1216 0.2036  93  GLN B O   
2342 C CB  . GLN B 18  ? 1.0785 1.5740 1.6327 -0.1670 -0.1262 0.2266  93  GLN B CB  
2343 C CG  . GLN B 18  ? 1.1372 1.6827 1.7069 -0.1633 -0.1033 0.2409  93  GLN B CG  
2344 C CD  . GLN B 18  ? 1.1675 1.7995 1.7744 -0.1656 -0.0987 0.2654  93  GLN B CD  
2345 O OE1 . GLN B 18  ? 0.8556 1.5227 1.4841 -0.1462 -0.0980 0.2628  93  GLN B OE1 
2346 N NE2 . GLN B 18  ? 1.2268 1.8953 1.8424 -0.1897 -0.0970 0.2909  93  GLN B NE2 
2347 N N   . SER B 19  ? 0.8953 1.2372 1.3810 -0.2269 -0.1700 0.2231  94  SER B N   
2348 C CA  . SER B 19  ? 0.9413 1.2297 1.4002 -0.2550 -0.1873 0.2312  94  SER B CA  
2349 C C   . SER B 19  ? 0.8507 1.1221 1.2918 -0.2965 -0.2224 0.2532  94  SER B C   
2350 O O   . SER B 19  ? 0.9758 1.2445 1.4128 -0.3039 -0.2386 0.2524  94  SER B O   
2351 C CB  . SER B 19  ? 0.8183 1.0194 1.2458 -0.2451 -0.1925 0.2023  94  SER B CB  
2352 O OG  . SER B 19  ? 0.9747 1.1131 1.3712 -0.2684 -0.2125 0.2079  94  SER B OG  
2353 N N   . PRO B 20  ? 1.0437 1.3013 1.4701 -0.3260 -0.2371 0.2749  95  PRO B N   
2354 C CA  . PRO B 20  ? 1.1551 1.3816 1.5536 -0.3680 -0.2756 0.2958  95  PRO B CA  
2355 C C   . PRO B 20  ? 1.1529 1.2694 1.4957 -0.3759 -0.3039 0.2718  95  PRO B C   
2356 O O   . PRO B 20  ? 1.0087 1.0946 1.3226 -0.4053 -0.3358 0.2830  95  PRO B O   
2357 C CB  . PRO B 20  ? 0.9616 1.1954 1.3533 -0.3942 -0.2829 0.3230  95  PRO B CB  
2358 C CG  . PRO B 20  ? 0.8180 1.0390 1.2133 -0.3668 -0.2569 0.3055  95  PRO B CG  
2359 C CD  . PRO B 20  ? 0.9932 1.2638 1.4241 -0.3246 -0.2218 0.2842  95  PRO B CD  
2360 N N   . GLY B 21  ? 1.0239 1.0798 1.3484 -0.3497 -0.2929 0.2388  96  GLY B N   
2361 C CA  . GLY B 21  ? 0.7413 0.6902 1.0085 -0.3508 -0.3148 0.2110  96  GLY B CA  
2362 C C   . GLY B 21  ? 1.1294 1.0684 1.3910 -0.3326 -0.3092 0.1847  96  GLY B C   
2363 O O   . GLY B 21  ? 1.2714 1.1279 1.4787 -0.3377 -0.3287 0.1636  96  GLY B O   
2364 N N   . TYR B 22  ? 1.1703 1.1892 1.4814 -0.3101 -0.2828 0.1850  97  TYR B N   
2365 C CA  . TYR B 22  ? 1.0637 1.0746 1.3690 -0.2923 -0.2779 0.1611  97  TYR B CA  
2366 C C   . TYR B 22  ? 0.9589 0.9843 1.2548 -0.3155 -0.3014 0.1762  97  TYR B C   
2367 O O   . TYR B 22  ? 0.9097 1.0119 1.2446 -0.3263 -0.3021 0.2070  97  TYR B O   
2368 C CB  . TYR B 22  ? 0.8737 0.9562 1.2291 -0.2575 -0.2441 0.1557  97  TYR B CB  
2369 C CG  . TYR B 22  ? 0.8312 0.9019 1.1768 -0.2405 -0.2417 0.1324  97  TYR B CG  
2370 C CD1 . TYR B 22  ? 0.9604 0.9466 1.2579 -0.2363 -0.2478 0.0999  97  TYR B CD1 
2371 C CD2 . TYR B 22  ? 0.4791 0.6195 0.8586 -0.2271 -0.2330 0.1418  97  TYR B CD2 
2372 C CE1 . TYR B 22  ? 0.9151 0.8896 1.1969 -0.2241 -0.2456 0.0791  97  TYR B CE1 
2373 C CE2 . TYR B 22  ? 0.6284 0.7538 0.9939 -0.2142 -0.2345 0.1227  97  TYR B CE2 
2374 C CZ  . TYR B 22  ? 0.6788 0.7228 0.9948 -0.2154 -0.2411 0.0922  97  TYR B CZ  
2375 O OH  . TYR B 22  ? 0.5986 0.6266 0.8935 -0.2061 -0.2425 0.0736  97  TYR B OH  
2376 N N   . ASP B 23  ? 1.0272 0.9787 1.2693 -0.3216 -0.3194 0.1541  98  ASP B N   
2377 C CA  . ASP B 23  ? 1.0070 0.9612 1.2316 -0.3425 -0.3432 0.1651  98  ASP B CA  
2378 C C   . ASP B 23  ? 0.9766 0.9222 1.1904 -0.3206 -0.3332 0.1386  98  ASP B C   
2379 O O   . ASP B 23  ? 1.1373 1.0062 1.3002 -0.3096 -0.3295 0.1039  98  ASP B O   
2380 C CB  . ASP B 23  ? 1.1130 0.9766 1.2667 -0.3743 -0.3778 0.1646  98  ASP B CB  
2381 C CG  . ASP B 23  ? 1.3291 1.1882 1.4579 -0.3985 -0.4050 0.1775  98  ASP B CG  
2382 O OD1 . ASP B 23  ? 1.4690 1.3988 1.6382 -0.4185 -0.4167 0.2151  98  ASP B OD1 
2383 O OD2 . ASP B 23  ? 1.3574 1.1427 1.4245 -0.3973 -0.4139 0.1505  98  ASP B OD2 
2384 N N   . PRO B 24  ? 1.0866 1.1063 1.3432 -0.3120 -0.3280 0.1528  99  PRO B N   
2385 C CA  . PRO B 24  ? 0.9510 0.9624 1.1956 -0.2914 -0.3199 0.1296  99  PRO B CA  
2386 C C   . PRO B 24  ? 1.1984 1.1264 1.3667 -0.3088 -0.3421 0.1105  99  PRO B C   
2387 O O   . PRO B 24  ? 1.0046 0.9140 1.1494 -0.2944 -0.3349 0.0883  99  PRO B O   
2388 C CB  . PRO B 24  ? 0.6534 0.7580 0.9570 -0.2816 -0.3168 0.1554  99  PRO B CB  
2389 C CG  . PRO B 24  ? 0.7856 0.9584 1.1423 -0.2829 -0.3062 0.1833  99  PRO B CG  
2390 C CD  . PRO B 24  ? 1.1207 1.2372 1.4397 -0.3157 -0.3258 0.1896  99  PRO B CD  
2391 N N   . SER B 25  ? 1.4064 1.2814 1.5296 -0.3392 -0.3685 0.1185  100 SER B N   
2392 C CA  . SER B 25  ? 1.4360 1.2265 1.4775 -0.3547 -0.3883 0.0999  100 SER B CA  
2393 C C   . SER B 25  ? 1.4424 1.1370 1.4180 -0.3430 -0.3778 0.0603  100 SER B C   
2394 O O   . SER B 25  ? 1.6814 1.3196 1.5975 -0.3348 -0.3725 0.0300  100 SER B O   
2395 C CB  . SER B 25  ? 1.3098 1.0882 1.3302 -0.3939 -0.4253 0.1311  100 SER B CB  
2396 O OG  . SER B 25  ? 1.5309 1.4017 1.6157 -0.4022 -0.4333 0.1684  100 SER B OG  
2397 N N   . ARG B 26  ? 1.3171 0.9928 1.3006 -0.3403 -0.3734 0.0603  101 ARG B N   
2398 C CA  . ARG B 26  ? 1.1948 0.7781 1.1187 -0.3242 -0.3639 0.0236  101 ARG B CA  
2399 C C   . ARG B 26  ? 1.2694 0.8538 1.1973 -0.2875 -0.3292 -0.0109 101 ARG B C   
2400 O O   . ARG B 26  ? 1.2670 0.9257 1.2589 -0.2733 -0.3115 -0.0019 101 ARG B O   
2401 C CB  . ARG B 26  ? 1.2349 0.8044 1.1746 -0.3263 -0.3672 0.0346  101 ARG B CB  
2402 C CG  . ARG B 26  ? 1.4114 0.9565 1.3262 -0.3647 -0.4044 0.0646  101 ARG B CG  
2403 C CD  . ARG B 26  ? 1.7009 1.2298 1.6263 -0.3676 -0.4086 0.0762  101 ARG B CD  
2404 N NE  . ARG B 26  ? 1.7131 1.1468 1.5843 -0.3421 -0.4003 0.0392  101 ARG B NE  
2405 C CZ  . ARG B 26  ? 1.8819 1.2172 1.6772 -0.3519 -0.4244 0.0289  101 ARG B CZ  
2406 N NH1 . ARG B 26  ? 1.6541 0.9666 1.4132 -0.3913 -0.4615 0.0538  101 ARG B NH1 
2407 N NH2 . ARG B 26  ? 1.6641 0.9216 1.4183 -0.3198 -0.4115 -0.0060 101 ARG B NH2 
2408 N N   . PRO B 27  ? 1.3977 0.9025 1.2567 -0.2704 -0.3181 -0.0499 102 PRO B N   
2409 C CA  . PRO B 27  ? 1.2208 0.7311 1.0793 -0.2376 -0.2848 -0.0812 102 PRO B CA  
2410 C C   . PRO B 27  ? 1.2008 0.7305 1.1075 -0.2087 -0.2609 -0.0877 102 PRO B C   
2411 O O   . PRO B 27  ? 1.0762 0.6303 1.0001 -0.1839 -0.2358 -0.1045 102 PRO B O   
2412 C CB  . PRO B 27  ? 1.4041 0.8258 1.1722 -0.2270 -0.2786 -0.1192 102 PRO B CB  
2413 C CG  . PRO B 27  ? 1.4496 0.8065 1.1811 -0.2412 -0.3028 -0.1135 102 PRO B CG  
2414 C CD  . PRO B 27  ? 1.4537 0.8617 1.2299 -0.2786 -0.3343 -0.0670 102 PRO B CD  
2415 N N   . GLU B 28  ? 1.2694 0.7880 1.1959 -0.2120 -0.2698 -0.0731 103 GLU B N   
2416 C CA  . GLU B 28  ? 1.1588 0.6939 1.1302 -0.1849 -0.2494 -0.0761 103 GLU B CA  
2417 C C   . GLU B 28  ? 0.9799 0.6095 1.0294 -0.1820 -0.2373 -0.0556 103 GLU B C   
2418 O O   . GLU B 28  ? 1.0099 0.7005 1.0907 -0.2041 -0.2492 -0.0286 103 GLU B O   
2419 C CB  . GLU B 28  ? 1.1880 0.6977 1.1639 -0.1960 -0.2662 -0.0574 103 GLU B CB  
2420 C CG  . GLU B 28  ? 1.1785 0.5873 1.0801 -0.1892 -0.2763 -0.0803 103 GLU B CG  
2421 C CD  . GLU B 28  ? 1.5983 0.9672 1.4437 -0.2224 -0.3059 -0.0741 103 GLU B CD  
2422 O OE1 . GLU B 28  ? 1.5590 0.9842 1.4290 -0.2519 -0.3204 -0.0476 103 GLU B OE1 
2423 O OE2 . GLU B 28  ? 1.6623 0.9440 1.4392 -0.2169 -0.3154 -0.0946 103 GLU B OE2 
2424 N N   . SER B 29  ? 1.0213 0.6673 1.1035 -0.1496 -0.2114 -0.0678 104 SER B N   
2425 C CA  . SER B 29  ? 0.8709 0.6132 1.0186 -0.1359 -0.1888 -0.0487 104 SER B CA  
2426 C C   . SER B 29  ? 0.6381 0.4291 0.8415 -0.1553 -0.2008 -0.0122 104 SER B C   
2427 O O   . SER B 29  ? 0.9048 0.6584 1.0975 -0.1752 -0.2212 -0.0010 104 SER B O   
2428 C CB  . SER B 29  ? 0.8494 0.6052 1.0082 -0.0937 -0.1522 -0.0679 104 SER B CB  
2429 O OG  . SER B 29  ? 0.7371 0.4624 0.9048 -0.0815 -0.1513 -0.0687 104 SER B OG  
2430 N N   . PHE B 30  ? 0.6958 0.5729 0.9522 -0.1470 -0.1852 0.0070  105 PHE B N   
2431 C CA  . PHE B 30  ? 0.5814 0.5176 0.8918 -0.1587 -0.1871 0.0398  105 PHE B CA  
2432 C C   . PHE B 30  ? 0.5511 0.4608 0.8652 -0.1473 -0.1777 0.0385  105 PHE B C   
2433 O O   . PHE B 30  ? 0.6742 0.5956 1.0063 -0.1691 -0.1899 0.0637  105 PHE B O   
2434 C CB  . PHE B 30  ? 0.3859 0.4092 0.7425 -0.1396 -0.1659 0.0528  105 PHE B CB  
2435 C CG  . PHE B 30  ? 0.3626 0.4518 0.7669 -0.1431 -0.1584 0.0826  105 PHE B CG  
2436 C CD1 . PHE B 30  ? 0.4347 0.5644 0.8464 -0.1633 -0.1690 0.1090  105 PHE B CD1 
2437 C CD2 . PHE B 30  ? 0.2861 0.3930 0.7094 -0.1205 -0.1342 0.0820  105 PHE B CD2 
2438 C CE1 . PHE B 30  ? 0.3782 0.5653 0.8162 -0.1609 -0.1540 0.1318  105 PHE B CE1 
2439 C CE2 . PHE B 30  ? 0.3515 0.5096 0.7946 -0.1198 -0.1214 0.1054  105 PHE B CE2 
2440 C CZ  . PHE B 30  ? 0.4799 0.6783 0.9294 -0.1394 -0.1299 0.1288  105 PHE B CZ  
2441 N N   . PHE B 31  ? 0.6191 0.4975 0.9149 -0.1138 -0.1563 0.0119  106 PHE B N   
2442 C CA  . PHE B 31  ? 0.4367 0.2893 0.7377 -0.0999 -0.1501 0.0111  106 PHE B CA  
2443 C C   . PHE B 31  ? 0.7985 0.5685 1.0645 -0.1195 -0.1796 0.0096  106 PHE B C   
2444 O O   . PHE B 31  ? 0.8664 0.6247 1.1442 -0.1310 -0.1906 0.0284  106 PHE B O   
2445 C CB  . PHE B 31  ? 0.5417 0.3862 0.8346 -0.0602 -0.1232 -0.0157 106 PHE B CB  
2446 C CG  . PHE B 31  ? 0.4982 0.3140 0.7970 -0.0421 -0.1197 -0.0178 106 PHE B CG  
2447 C CD1 . PHE B 31  ? 0.5846 0.4269 0.9140 -0.0516 -0.1225 0.0089  106 PHE B CD1 
2448 C CD2 . PHE B 31  ? 0.6713 0.4375 0.9452 -0.0139 -0.1130 -0.0457 106 PHE B CD2 
2449 C CE1 . PHE B 31  ? 0.6456 0.4586 0.9789 -0.0364 -0.1235 0.0095  106 PHE B CE1 
2450 C CE2 . PHE B 31  ? 0.6304 0.3730 0.9150 0.0063  -0.1126 -0.0458 106 PHE B CE2 
2451 C CZ  . PHE B 31  ? 0.5494 0.3124 0.8629 -0.0064 -0.1201 -0.0173 106 PHE B CZ  
2452 N N   . GLN B 32  ? 0.8770 0.5820 1.0925 -0.1254 -0.1948 -0.0121 107 GLN B N   
2453 C CA  . GLN B 32  ? 0.9308 0.5538 1.0919 -0.1341 -0.2168 -0.0176 107 GLN B CA  
2454 C C   . GLN B 32  ? 0.8918 0.5274 1.0477 -0.1775 -0.2441 0.0153  107 GLN B C   
2455 O O   . GLN B 32  ? 0.9681 0.5582 1.0986 -0.1883 -0.2620 0.0246  107 GLN B O   
2456 C CB  . GLN B 32  ? 1.0584 0.6129 1.1556 -0.1196 -0.2161 -0.0540 107 GLN B CB  
2457 C CG  . GLN B 32  ? 1.0222 0.5704 1.1206 -0.0731 -0.1856 -0.0873 107 GLN B CG  
2458 C CD  . GLN B 32  ? 1.3494 0.8580 1.3902 -0.0629 -0.1781 -0.1206 107 GLN B CD  
2459 O OE1 . GLN B 32  ? 1.1967 0.6739 1.1926 -0.0913 -0.1980 -0.1193 107 GLN B OE1 
2460 N NE2 . GLN B 32  ? 1.3498 0.8670 1.3917 -0.0231 -0.1480 -0.1488 107 GLN B NE2 
2461 N N   . GLN B 33  ? 0.7321 0.4327 0.9128 -0.2007 -0.2480 0.0346  108 GLN B N   
2462 C CA  . GLN B 33  ? 0.7328 0.4570 0.9126 -0.2390 -0.2719 0.0675  108 GLN B CA  
2463 C C   . GLN B 33  ? 0.7461 0.5427 0.9772 -0.2490 -0.2651 0.1020  108 GLN B C   
2464 O O   . GLN B 33  ? 1.0666 0.8708 1.2909 -0.2791 -0.2850 0.1293  108 GLN B O   
2465 C CB  . GLN B 33  ? 0.7355 0.5037 0.9207 -0.2553 -0.2787 0.0755  108 GLN B CB  
2466 C CG  . GLN B 33  ? 0.8995 0.5989 1.0250 -0.2515 -0.2869 0.0445  108 GLN B CG  
2467 C CD  . GLN B 33  ? 1.0573 0.8033 1.1901 -0.2678 -0.2957 0.0560  108 GLN B CD  
2468 O OE1 . GLN B 33  ? 1.0642 0.8664 1.2252 -0.2919 -0.3094 0.0897  108 GLN B OE1 
2469 N NE2 . GLN B 33  ? 0.9741 0.6988 1.0807 -0.2534 -0.2874 0.0289  108 GLN B NE2 
2470 N N   . SER B 34  ? 0.7704 0.6196 1.0479 -0.2251 -0.2374 0.1018  109 SER B N   
2471 C CA  . SER B 34  ? 0.5405 0.4696 0.8625 -0.2312 -0.2243 0.1327  109 SER B CA  
2472 C C   . SER B 34  ? 0.6381 0.5449 0.9620 -0.2225 -0.2183 0.1362  109 SER B C   
2473 O O   . SER B 34  ? 0.5413 0.5081 0.8923 -0.2282 -0.2064 0.1607  109 SER B O   
2474 C CB  . SER B 34  ? 0.6026 0.6179 0.9715 -0.2098 -0.1959 0.1339  109 SER B CB  
2475 O OG  . SER B 34  ? 0.7027 0.7358 1.0689 -0.2155 -0.2038 0.1310  109 SER B OG  
2476 N N   . PHE B 35  ? 0.6208 0.4433 0.9131 -0.2060 -0.2252 0.1121  110 PHE B N   
2477 C CA  . PHE B 35  ? 0.6992 0.4995 0.9943 -0.1932 -0.2210 0.1152  110 PHE B CA  
2478 C C   . PHE B 35  ? 0.8836 0.5844 1.1253 -0.1930 -0.2462 0.1031  110 PHE B C   
2479 O O   . PHE B 35  ? 0.8940 0.5325 1.0966 -0.1837 -0.2552 0.0771  110 PHE B O   
2480 C CB  . PHE B 35  ? 0.5684 0.3824 0.8925 -0.1554 -0.1940 0.0958  110 PHE B CB  
2481 C CG  . PHE B 35  ? 0.5802 0.4886 0.9526 -0.1513 -0.1679 0.1087  110 PHE B CG  
2482 C CD1 . PHE B 35  ? 0.5049 0.4636 0.8982 -0.1547 -0.1553 0.1325  110 PHE B CD1 
2483 C CD2 . PHE B 35  ? 0.4237 0.3681 0.8107 -0.1406 -0.1552 0.0953  110 PHE B CD2 
2484 C CE1 . PHE B 35  ? 0.4332 0.4728 0.8569 -0.1431 -0.1281 0.1398  110 PHE B CE1 
2485 C CE2 . PHE B 35  ? 0.4262 0.4528 0.8459 -0.1282 -0.1303 0.1044  110 PHE B CE2 
2486 C CZ  . PHE B 35  ? 0.3624 0.4343 0.7992 -0.1278 -0.1160 0.1253  110 PHE B CZ  
2487 N N   . GLN B 36  ? 0.8389 0.5249 1.0749 -0.2016 -0.2569 0.1215  111 GLN B N   
2488 C CA  . GLN B 36  ? 0.9069 0.5002 1.0956 -0.1942 -0.2795 0.1104  111 GLN B CA  
2489 C C   . GLN B 36  ? 0.9416 0.5137 1.1411 -0.1491 -0.2619 0.0880  111 GLN B C   
2490 O O   . GLN B 36  ? 0.9531 0.5597 1.1812 -0.1441 -0.2529 0.1034  111 GLN B O   
2491 C CB  . GLN B 36  ? 0.9280 0.5167 1.1035 -0.2281 -0.3036 0.1435  111 GLN B CB  
2492 C CG  . GLN B 36  ? 1.0115 0.6261 1.1764 -0.2730 -0.3230 0.1695  111 GLN B CG  
2493 C CD  . GLN B 36  ? 0.9296 0.5458 1.0819 -0.3069 -0.3455 0.2041  111 GLN B CD  
2494 O OE1 . GLN B 36  ? 1.0857 0.7230 1.2547 -0.3020 -0.3368 0.2162  111 GLN B OE1 
2495 N NE2 . GLN B 36  ? 1.0902 0.6825 1.2090 -0.3433 -0.3765 0.2214  111 GLN B NE2 
2496 N N   . ARG B 37  ? 0.9870 0.5079 1.1622 -0.1155 -0.2555 0.0526  112 ARG B N   
2497 C CA  . ARG B 37  ? 0.8952 0.4088 1.0836 -0.0688 -0.2360 0.0317  112 ARG B CA  
2498 C C   . ARG B 37  ? 0.9541 0.4128 1.1200 -0.0601 -0.2546 0.0368  112 ARG B C   
2499 O O   . ARG B 37  ? 1.1626 0.5464 1.2802 -0.0607 -0.2754 0.0268  112 ARG B O   
2500 C CB  . ARG B 37  ? 0.8848 0.3717 1.0523 -0.0347 -0.2192 -0.0067 112 ARG B CB  
2501 C CG  . ARG B 37  ? 1.0881 0.6003 1.2811 0.0130  -0.1914 -0.0252 112 ARG B CG  
2502 C CD  . ARG B 37  ? 1.0548 0.5503 1.2241 0.0449  -0.1710 -0.0616 112 ARG B CD  
2503 N NE  . ARG B 37  ? 0.9557 0.4796 1.1273 0.0268  -0.1641 -0.0674 112 ARG B NE  
2504 C CZ  . ARG B 37  ? 1.3095 0.8397 1.4679 0.0486  -0.1428 -0.0955 112 ARG B CZ  
2505 N NH1 . ARG B 37  ? 1.2633 0.7829 1.4087 0.0903  -0.1217 -0.1195 112 ARG B NH1 
2506 N NH2 . ARG B 37  ? 1.2522 0.8048 1.4111 0.0270  -0.1420 -0.0978 112 ARG B NH2 
2507 N N   . LEU B 38  ? 0.9485 0.4416 1.1467 -0.0522 -0.2487 0.0526  113 LEU B N   
2508 C CA  . LEU B 38  ? 0.9129 0.3597 1.0938 -0.0464 -0.2688 0.0612  113 LEU B CA  
2509 C C   . LEU B 38  ? 1.1005 0.5266 1.2843 0.0063  -0.2547 0.0355  113 LEU B C   
2510 O O   . LEU B 38  ? 1.3452 0.7014 1.4937 0.0249  -0.2687 0.0218  113 LEU B O   
2511 C CB  . LEU B 38  ? 0.8625 0.3573 1.0706 -0.0719 -0.2732 0.0958  113 LEU B CB  
2512 C CG  . LEU B 38  ? 0.8961 0.4244 1.1030 -0.1235 -0.2841 0.1266  113 LEU B CG  
2513 C CD1 . LEU B 38  ? 0.8813 0.4635 1.1124 -0.1411 -0.2796 0.1569  113 LEU B CD1 
2514 C CD2 . LEU B 38  ? 0.9569 0.4196 1.1151 -0.1518 -0.3189 0.1347  113 LEU B CD2 
2515 N N   . SER B 39  ? 0.9640 0.4541 1.1895 0.0308  -0.2267 0.0300  114 SER B N   
2516 C CA  . SER B 39  ? 1.0024 0.4947 1.2379 0.0790  -0.2097 0.0101  114 SER B CA  
2517 C C   . SER B 39  ? 0.8771 0.4513 1.1539 0.0939  -0.1778 0.0042  114 SER B C   
2518 O O   . SER B 39  ? 0.9054 0.5269 1.2034 0.0688  -0.1709 0.0162  114 SER B O   
2519 C CB  . SER B 39  ? 1.1724 0.6470 1.4132 0.0866  -0.2269 0.0266  114 SER B CB  
2520 O OG  . SER B 39  ? 1.1402 0.6703 1.4131 0.0635  -0.2274 0.0535  114 SER B OG  
2521 N N   . ARG B 40  ? 0.8753 0.4682 1.1629 0.1346  -0.1581 -0.0125 115 ARG B N   
2522 C CA  . ARG B 40  ? 0.6916 0.3633 1.0132 0.1475  -0.1295 -0.0168 115 ARG B CA  
2523 C C   . ARG B 40  ? 0.6539 0.3677 1.0071 0.1475  -0.1318 0.0047  115 ARG B C   
2524 O O   . ARG B 40  ? 0.7771 0.4615 1.1280 0.1598  -0.1474 0.0125  115 ARG B O   
2525 C CB  . ARG B 40  ? 0.6632 0.3421 0.9766 0.1873  -0.1050 -0.0442 115 ARG B CB  
2526 C CG  . ARG B 40  ? 0.6913 0.4506 1.0304 0.1918  -0.0769 -0.0485 115 ARG B CG  
2527 C CD  . ARG B 40  ? 0.8034 0.5651 1.1245 0.2198  -0.0529 -0.0760 115 ARG B CD  
2528 N NE  . ARG B 40  ? 0.9311 0.6894 1.2533 0.2619  -0.0426 -0.0834 115 ARG B NE  
2529 C CZ  . ARG B 40  ? 1.0905 0.8577 1.4014 0.2930  -0.0169 -0.1046 115 ARG B CZ  
2530 N NH1 . ARG B 40  ? 1.0842 0.8594 1.3762 0.2849  -0.0012 -0.1224 115 ARG B NH1 
2531 N NH2 . ARG B 40  ? 1.1328 0.9026 1.4537 0.3335  -0.0058 -0.1071 115 ARG B NH2 
2532 N N   . LEU B 41  ? 0.6144 0.3922 0.9933 0.1325  -0.1178 0.0146  116 LEU B N   
2533 C CA  . LEU B 41  ? 0.5813 0.3970 0.9837 0.1264  -0.1205 0.0355  116 LEU B CA  
2534 C C   . LEU B 41  ? 0.5347 0.4053 0.9556 0.1498  -0.1004 0.0286  116 LEU B C   
2535 O O   . LEU B 41  ? 0.5405 0.4244 0.9768 0.1600  -0.1076 0.0403  116 LEU B O   
2536 C CB  . LEU B 41  ? 0.4556 0.2982 0.8663 0.0915  -0.1204 0.0549  116 LEU B CB  
2537 C CG  . LEU B 41  ? 0.6531 0.4548 1.0499 0.0626  -0.1423 0.0720  116 LEU B CG  
2538 C CD1 . LEU B 41  ? 0.6556 0.4930 1.0617 0.0350  -0.1342 0.0891  116 LEU B CD1 
2539 C CD2 . LEU B 41  ? 0.7853 0.5542 1.1749 0.0571  -0.1673 0.0906  116 LEU B CD2 
2540 N N   . GLY B 42  ? 0.4756 0.3792 0.8947 0.1562  -0.0775 0.0121  117 GLY B N   
2541 C CA  . GLY B 42  ? 0.4986 0.4576 0.9322 0.1747  -0.0597 0.0078  117 GLY B CA  
2542 C C   . GLY B 42  ? 0.5070 0.4861 0.9290 0.1825  -0.0373 -0.0129 117 GLY B C   
2543 O O   . GLY B 42  ? 0.6674 0.6251 1.0733 0.1672  -0.0355 -0.0214 117 GLY B O   
2544 N N   . HIS B 43  ? 0.7813 0.8060 1.2141 0.2060  -0.0213 -0.0193 118 HIS B N   
2545 C CA  . HIS B 43  ? 0.6593 0.7094 1.0816 0.2141  0.0011  -0.0373 118 HIS B CA  
2546 C C   . HIS B 43  ? 0.7355 0.8619 1.1790 0.2185  0.0145  -0.0303 118 HIS B C   
2547 O O   . HIS B 43  ? 0.9228 1.0792 1.3904 0.2234  0.0061  -0.0152 118 HIS B O   
2548 C CB  . HIS B 43  ? 0.7494 0.7601 1.1533 0.2476  0.0096  -0.0597 118 HIS B CB  
2549 C CG  . HIS B 43  ? 0.7157 0.7307 1.1336 0.2866  0.0108  -0.0579 118 HIS B CG  
2550 N ND1 . HIS B 43  ? 0.9738 0.9525 1.3991 0.2914  -0.0117 -0.0450 118 HIS B ND1 
2551 C CD2 . HIS B 43  ? 0.8905 0.9438 1.3186 0.3242  0.0328  -0.0655 118 HIS B CD2 
2552 C CE1 . HIS B 43  ? 1.0065 0.9985 1.4463 0.3320  -0.0050 -0.0453 118 HIS B CE1 
2553 N NE2 . HIS B 43  ? 1.0931 1.1331 1.5367 0.3539  0.0236  -0.0570 118 HIS B NE2 
2554 N N   . GLY B 44  ? 0.6366 0.7948 1.0721 0.2142  0.0332  -0.0407 119 GLY B N   
2555 C CA  . GLY B 44  ? 0.5940 0.8290 1.0490 0.2128  0.0449  -0.0337 119 GLY B CA  
2556 C C   . GLY B 44  ? 0.7606 1.0162 1.2001 0.1995  0.0631  -0.0439 119 GLY B C   
2557 O O   . GLY B 44  ? 0.8167 1.0309 1.2329 0.2030  0.0706  -0.0617 119 GLY B O   
2558 N N   . SER B 45  ? 0.9840 1.3019 1.4366 0.1814  0.0676  -0.0330 120 SER B N   
2559 C CA  . SER B 45  ? 0.9475 1.2860 1.3861 0.1630  0.0828  -0.0381 120 SER B CA  
2560 C C   . SER B 45  ? 0.8455 1.1351 1.2603 0.1337  0.0715  -0.0361 120 SER B C   
2561 O O   . SER B 45  ? 0.8817 1.1650 1.2802 0.1233  0.0817  -0.0470 120 SER B O   
2562 C CB  . SER B 45  ? 1.0098 1.4324 1.4705 0.1474  0.0880  -0.0274 120 SER B CB  
2563 O OG  . SER B 45  ? 1.0697 1.4931 1.5427 0.1233  0.0665  -0.0116 120 SER B OG  
2564 N N   . TYR B 46  ? 0.7533 1.0108 1.1661 0.1214  0.0517  -0.0229 121 TYR B N   
2565 C CA  . TYR B 46  ? 0.7606 0.9753 1.1514 0.1005  0.0427  -0.0205 121 TYR B CA  
2566 C C   . TYR B 46  ? 0.7432 0.9109 1.1210 0.1084  0.0435  -0.0377 121 TYR B C   
2567 O O   . TYR B 46  ? 0.8636 1.0117 1.2270 0.0945  0.0419  -0.0417 121 TYR B O   
2568 C CB  . TYR B 46  ? 0.8499 1.0447 1.2406 0.0888  0.0256  -0.0023 121 TYR B CB  
2569 C CG  . TYR B 46  ? 0.8332 1.0050 1.2361 0.1034  0.0165  0.0001  121 TYR B CG  
2570 C CD1 . TYR B 46  ? 0.8668 0.9918 1.2616 0.1039  0.0095  -0.0043 121 TYR B CD1 
2571 C CD2 . TYR B 46  ? 0.8770 1.0770 1.3037 0.1153  0.0125  0.0084  121 TYR B CD2 
2572 C CE1 . TYR B 46  ? 0.7586 0.8596 1.1655 0.1145  -0.0015 -0.0004 121 TYR B CE1 
2573 C CE2 . TYR B 46  ? 0.9244 1.0998 1.3630 0.1295  0.0017  0.0117  121 TYR B CE2 
2574 C CZ  . TYR B 46  ? 0.8233 0.9462 1.2502 0.1283  -0.0055 0.0074  121 TYR B CZ  
2575 O OH  . TYR B 46  ? 0.9537 1.0482 1.3915 0.1398  -0.0192 0.0123  121 TYR B OH  
2576 N N   . GLY B 47  ? 0.6460 0.7941 1.0294 0.1310  0.0438  -0.0478 122 GLY B N   
2577 C CA  . GLY B 47  ? 0.5984 0.6951 0.9691 0.1366  0.0400  -0.0642 122 GLY B CA  
2578 C C   . GLY B 47  ? 0.7397 0.7980 1.1158 0.1498  0.0259  -0.0614 122 GLY B C   
2579 O O   . GLY B 47  ? 0.7884 0.8607 1.1767 0.1701  0.0270  -0.0579 122 GLY B O   
2580 N N   . GLU B 48  ? 0.5876 0.5996 0.9574 0.1381  0.0110  -0.0612 123 GLU B N   
2581 C CA  . GLU B 48  ? 0.5744 0.5421 0.9464 0.1454  -0.0063 -0.0570 123 GLU B CA  
2582 C C   . GLU B 48  ? 0.4271 0.3838 0.8086 0.1191  -0.0228 -0.0366 123 GLU B C   
2583 O O   . GLU B 48  ? 0.4397 0.4058 0.8214 0.1002  -0.0217 -0.0329 123 GLU B O   
2584 C CB  . GLU B 48  ? 0.5913 0.4989 0.9385 0.1588  -0.0114 -0.0790 123 GLU B CB  
2585 C CG  . GLU B 48  ? 0.8027 0.7143 1.1332 0.1892  0.0086  -0.1022 123 GLU B CG  
2586 C CD  . GLU B 48  ? 1.0832 1.0188 1.4021 0.1816  0.0260  -0.1180 123 GLU B CD  
2587 O OE1 . GLU B 48  ? 0.8211 0.7627 1.1443 0.1547  0.0199  -0.1119 123 GLU B OE1 
2588 O OE2 . GLU B 48  ? 1.1101 1.0595 1.4153 0.2037  0.0466  -0.1360 123 GLU B OE2 
2589 N N   . VAL B 49  ? 0.3815 0.3199 0.7717 0.1198  -0.0378 -0.0224 124 VAL B N   
2590 C CA  . VAL B 49  ? 0.3549 0.2822 0.7545 0.0960  -0.0535 -0.0010 124 VAL B CA  
2591 C C   . VAL B 49  ? 0.5965 0.4635 0.9871 0.0953  -0.0763 0.0010  124 VAL B C   
2592 O O   . VAL B 49  ? 0.6036 0.4471 0.9894 0.1130  -0.0842 -0.0006 124 VAL B O   
2593 C CB  . VAL B 49  ? 0.4122 0.3699 0.8239 0.0897  -0.0540 0.0192  124 VAL B CB  
2594 C CG1 . VAL B 49  ? 0.4339 0.3798 0.8525 0.0668  -0.0681 0.0422  124 VAL B CG1 
2595 C CG2 . VAL B 49  ? 0.4202 0.4240 0.8274 0.0864  -0.0359 0.0178  124 VAL B CG2 
2596 N N   . PHE B 50  ? 0.5631 0.4032 0.9486 0.0734  -0.0889 0.0069  125 PHE B N   
2597 C CA  . PHE B 50  ? 0.5767 0.3529 0.9407 0.0627  -0.1147 0.0115  125 PHE B CA  
2598 C C   . PHE B 50  ? 0.5782 0.3555 0.9513 0.0309  -0.1317 0.0437  125 PHE B C   
2599 O O   . PHE B 50  ? 0.5529 0.3741 0.9473 0.0147  -0.1222 0.0600  125 PHE B O   
2600 C CB  . PHE B 50  ? 0.7965 0.5344 1.1350 0.0534  -0.1209 -0.0040 125 PHE B CB  
2601 C CG  . PHE B 50  ? 0.6037 0.3362 0.9246 0.0821  -0.1032 -0.0359 125 PHE B CG  
2602 C CD1 . PHE B 50  ? 0.7400 0.4237 1.0307 0.1080  -0.1056 -0.0537 125 PHE B CD1 
2603 C CD2 . PHE B 50  ? 0.6840 0.4592 1.0154 0.0835  -0.0831 -0.0470 125 PHE B CD2 
2604 C CE1 . PHE B 50  ? 0.7836 0.4657 1.0553 0.1352  -0.0853 -0.0818 125 PHE B CE1 
2605 C CE2 . PHE B 50  ? 0.7672 0.5402 1.0783 0.1064  -0.0658 -0.0746 125 PHE B CE2 
2606 C CZ  . PHE B 50  ? 0.6781 0.4065 0.9594 0.1325  -0.0656 -0.0919 125 PHE B CZ  
2607 N N   . LYS B 51  ? 0.6790 0.4071 1.0311 0.0225  -0.1558 0.0536  126 LYS B N   
2608 C CA  . LYS B 51  ? 0.5850 0.3088 0.9328 -0.0147 -0.1744 0.0849  126 LYS B CA  
2609 C C   . LYS B 51  ? 0.6234 0.3186 0.9474 -0.0435 -0.1895 0.0875  126 LYS B C   
2610 O O   . LYS B 51  ? 0.8740 0.5109 1.1654 -0.0358 -0.2025 0.0694  126 LYS B O   
2611 C CB  . LYS B 51  ? 0.7001 0.3867 1.0326 -0.0133 -0.1954 0.0964  126 LYS B CB  
2612 C CG  . LYS B 51  ? 0.6111 0.2977 0.9325 -0.0540 -0.2138 0.1299  126 LYS B CG  
2613 C CD  . LYS B 51  ? 0.7269 0.3656 1.0275 -0.0527 -0.2390 0.1390  126 LYS B CD  
2614 C CE  . LYS B 51  ? 0.8742 0.5151 1.1571 -0.0963 -0.2573 0.1726  126 LYS B CE  
2615 N NZ  . LYS B 51  ? 0.9944 0.5833 1.2543 -0.0974 -0.2858 0.1822  126 LYS B NZ  
2616 N N   . VAL B 52  ? 0.6769 0.4173 1.0144 -0.0766 -0.1862 0.1103  127 VAL B N   
2617 C CA  . VAL B 52  ? 0.6146 0.3498 0.9356 -0.1070 -0.1982 0.1157  127 VAL B CA  
2618 C C   . VAL B 52  ? 0.6815 0.4569 1.0037 -0.1468 -0.2053 0.1516  127 VAL B C   
2619 O O   . VAL B 52  ? 0.7053 0.5189 1.0419 -0.1500 -0.1948 0.1699  127 VAL B O   
2620 C CB  . VAL B 52  ? 0.6781 0.4522 1.0197 -0.1026 -0.1796 0.1016  127 VAL B CB  
2621 C CG1 . VAL B 52  ? 0.6498 0.3883 0.9832 -0.0642 -0.1701 0.0650  127 VAL B CG1 
2622 C CG2 . VAL B 52  ? 0.4674 0.3224 0.8498 -0.1040 -0.1538 0.1165  127 VAL B CG2 
2623 N N   A ARG B 53  ? 0.8090 0.5783 1.1115 -0.1773 -0.2221 0.1615  128 ARG B N   
2624 N N   B ARG B 53  ? 0.8109 0.5781 1.1124 -0.1773 -0.2228 0.1615  128 ARG B N   
2625 C CA  A ARG B 53  ? 0.7876 0.6119 1.0935 -0.2145 -0.2245 0.1948  128 ARG B CA  
2626 C CA  B ARG B 53  ? 0.7869 0.6118 1.0933 -0.2141 -0.2241 0.1946  128 ARG B CA  
2627 C C   A ARG B 53  ? 0.7851 0.6642 1.1073 -0.2270 -0.2154 0.1967  128 ARG B C   
2628 C C   B ARG B 53  ? 0.7847 0.6637 1.1077 -0.2256 -0.2147 0.1957  128 ARG B C   
2629 O O   A ARG B 53  ? 0.7971 0.6368 1.0993 -0.2328 -0.2320 0.1840  128 ARG B O   
2630 O O   B ARG B 53  ? 0.7931 0.6323 1.0971 -0.2290 -0.2300 0.1812  128 ARG B O   
2631 C CB  A ARG B 53  ? 0.8442 0.6146 1.1104 -0.2430 -0.2587 0.2113  128 ARG B CB  
2632 C CB  B ARG B 53  ? 0.8422 0.6175 1.1100 -0.2440 -0.2576 0.2126  128 ARG B CB  
2633 C CG  A ARG B 53  ? 0.8376 0.6692 1.1066 -0.2823 -0.2610 0.2478  128 ARG B CG  
2634 C CG  B ARG B 53  ? 0.8387 0.6793 1.1122 -0.2799 -0.2563 0.2491  128 ARG B CG  
2635 C CD  A ARG B 53  ? 0.8060 0.5803 1.0338 -0.3116 -0.2979 0.2661  128 ARG B CD  
2636 C CD  B ARG B 53  ? 0.7957 0.5868 1.0292 -0.3137 -0.2933 0.2696  128 ARG B CD  
2637 N NE  A ARG B 53  ? 0.9016 0.6291 1.1152 -0.2978 -0.3062 0.2646  128 ARG B NE  
2638 N NE  B ARG B 53  ? 0.9059 0.6370 1.1170 -0.3049 -0.3090 0.2692  128 ARG B NE  
2639 C CZ  A ARG B 53  ? 0.8386 0.6047 1.0586 -0.3079 -0.2979 0.2863  128 ARG B CZ  
2640 C CZ  B ARG B 53  ? 0.9643 0.6012 1.1411 -0.2930 -0.3367 0.2524  128 ARG B CZ  
2641 N NH1 A ARG B 53  ? 0.8445 0.6982 1.0840 -0.3286 -0.2768 0.3090  128 ARG B NH1 
2642 N NH1 B ARG B 53  ? 0.9484 0.5332 1.1024 -0.2895 -0.3512 0.2333  128 ARG B NH1 
2643 N NH2 A ARG B 53  ? 0.8468 0.5637 1.0515 -0.2952 -0.3105 0.2842  128 ARG B NH2 
2644 N NH2 B ARG B 53  ? 0.9427 0.5357 1.1048 -0.2827 -0.3498 0.2540  128 ARG B NH2 
2645 N N   . SER B 54  ? 0.7943 0.7625 1.1485 -0.2284 -0.1891 0.2112  129 SER B N   
2646 C CA  . SER B 54  ? 0.5959 0.6248 0.9704 -0.2318 -0.1779 0.2120  129 SER B CA  
2647 C C   . SER B 54  ? 0.7628 0.8050 1.1241 -0.2692 -0.1993 0.2358  129 SER B C   
2648 O O   . SER B 54  ? 0.8967 0.9663 1.2545 -0.2915 -0.2024 0.2622  129 SER B O   
2649 C CB  . SER B 54  ? 0.7140 0.8301 1.1207 -0.2136 -0.1419 0.2169  129 SER B CB  
2650 O OG  . SER B 54  ? 0.8127 0.9901 1.2377 -0.2139 -0.1324 0.2198  129 SER B OG  
2651 N N   . LYS B 55  ? 0.8536 0.8767 1.2055 -0.2778 -0.2154 0.2279  130 LYS B N   
2652 C CA  . LYS B 55  ? 0.9291 0.9698 1.2708 -0.3142 -0.2375 0.2528  130 LYS B CA  
2653 C C   . LYS B 55  ? 0.6337 0.7848 1.0152 -0.3182 -0.2150 0.2753  130 LYS B C   
2654 O O   . LYS B 55  ? 0.9160 1.0995 1.2966 -0.3498 -0.2296 0.3036  130 LYS B O   
2655 C CB  . LYS B 55  ? 0.6610 0.6481 0.9769 -0.3216 -0.2615 0.2376  130 LYS B CB  
2656 C CG  . LYS B 55  ? 0.7104 0.5851 0.9810 -0.3104 -0.2801 0.2095  130 LYS B CG  
2657 C CD  . LYS B 55  ? 0.7560 0.5772 0.9927 -0.3153 -0.2998 0.1910  130 LYS B CD  
2658 C CE  . LYS B 55  ? 0.8122 0.5225 0.9994 -0.2952 -0.3116 0.1575  130 LYS B CE  
2659 N NZ  . LYS B 55  ? 0.8667 0.5201 1.0104 -0.2981 -0.3277 0.1362  130 LYS B NZ  
2660 N N   . GLU B 56  ? 0.7968 1.0046 1.2104 -0.2852 -0.1804 0.2632  131 GLU B N   
2661 C CA  . GLU B 56  ? 0.7711 1.0792 1.2187 -0.2803 -0.1564 0.2797  131 GLU B CA  
2662 C C   . GLU B 56  ? 0.7289 1.0775 1.1780 -0.2952 -0.1468 0.3047  131 GLU B C   
2663 O O   . GLU B 56  ? 0.8547 1.2754 1.3223 -0.3103 -0.1418 0.3288  131 GLU B O   
2664 C CB  . GLU B 56  ? 0.8368 1.1805 1.3071 -0.2370 -0.1242 0.2566  131 GLU B CB  
2665 C CG  . GLU B 56  ? 0.7424 1.1810 1.2438 -0.2225 -0.0985 0.2673  131 GLU B CG  
2666 C CD  . GLU B 56  ? 1.0386 1.5140 1.5577 -0.2355 -0.1129 0.2792  131 GLU B CD  
2667 O OE1 . GLU B 56  ? 1.1906 1.6284 1.7029 -0.2330 -0.1285 0.2644  131 GLU B OE1 
2668 O OE2 . GLU B 56  ? 1.1069 1.6508 1.6467 -0.2495 -0.1094 0.3046  131 GLU B OE2 
2669 N N   . ASP B 57  ? 0.6779 0.9832 1.1079 -0.2921 -0.1450 0.3005  132 ASP B N   
2670 C CA  . ASP B 57  ? 0.6924 1.0322 1.1182 -0.3073 -0.1363 0.3235  132 ASP B CA  
2671 C C   . ASP B 57  ? 0.7556 1.0182 1.1448 -0.3300 -0.1634 0.3314  132 ASP B C   
2672 O O   . ASP B 57  ? 0.8028 1.0873 1.1827 -0.3462 -0.1598 0.3517  132 ASP B O   
2673 C CB  . ASP B 57  ? 0.6209 1.0106 1.0621 -0.2735 -0.0961 0.3132  132 ASP B CB  
2674 C CG  . ASP B 57  ? 0.7950 1.1295 1.2292 -0.2424 -0.0889 0.2847  132 ASP B CG  
2675 O OD1 . ASP B 57  ? 0.8776 1.1340 1.2950 -0.2474 -0.1139 0.2743  132 ASP B OD1 
2676 O OD2 . ASP B 57  ? 0.8358 1.2042 1.2798 -0.2117 -0.0589 0.2726  132 ASP B OD2 
2677 N N   . GLY B 58  ? 0.7103 0.8819 1.0757 -0.3301 -0.1908 0.3154  133 GLY B N   
2678 C CA  . GLY B 58  ? 0.7301 0.8216 1.0581 -0.3469 -0.2201 0.3210  133 GLY B CA  
2679 C C   . GLY B 58  ? 0.8522 0.9188 1.1748 -0.3262 -0.2081 0.3127  133 GLY B C   
2680 O O   . GLY B 58  ? 1.0799 1.0870 1.3724 -0.3391 -0.2323 0.3204  133 GLY B O   
2681 N N   . ARG B 59  ? 0.5693 0.6763 0.9173 -0.2946 -0.1743 0.2979  134 ARG B N   
2682 C CA  . ARG B 59  ? 0.5780 0.6678 0.9205 -0.2769 -0.1629 0.2933  134 ARG B CA  
2683 C C   . ARG B 59  ? 0.6479 0.6704 0.9910 -0.2459 -0.1689 0.2646  134 ARG B C   
2684 O O   . ARG B 59  ? 0.5875 0.5884 0.9381 -0.2342 -0.1735 0.2450  134 ARG B O   
2685 C CB  . ARG B 59  ? 0.6951 0.8676 1.0579 -0.2617 -0.1231 0.2961  134 ARG B CB  
2686 C CG  . ARG B 59  ? 0.6024 0.8487 0.9663 -0.2865 -0.1118 0.3227  134 ARG B CG  
2687 C CD  . ARG B 59  ? 0.7418 1.0582 1.1179 -0.2642 -0.0710 0.3199  134 ARG B CD  
2688 N NE  . ARG B 59  ? 0.9502 1.3025 1.3089 -0.2859 -0.0625 0.3437  134 ARG B NE  
2689 C CZ  . ARG B 59  ? 1.1145 1.5028 1.4653 -0.2714 -0.0321 0.3430  134 ARG B CZ  
2690 N NH1 . ARG B 59  ? 0.8953 1.2874 1.2536 -0.2350 -0.0088 0.3211  134 ARG B NH1 
2691 N NH2 . ARG B 59  ? 0.9781 1.3968 1.3085 -0.2950 -0.0259 0.3650  134 ARG B NH2 
2692 N N   . LEU B 60  ? 0.7293 0.7211 1.0637 -0.2326 -0.1689 0.2626  135 LEU B N   
2693 C CA  . LEU B 60  ? 0.5752 0.5075 0.9124 -0.2011 -0.1752 0.2377  135 LEU B CA  
2694 C C   . LEU B 60  ? 0.5888 0.5622 0.9544 -0.1720 -0.1441 0.2229  135 LEU B C   
2695 O O   . LEU B 60  ? 0.6265 0.6510 0.9961 -0.1719 -0.1217 0.2340  135 LEU B O   
2696 C CB  . LEU B 60  ? 0.7390 0.6184 1.0540 -0.1994 -0.1950 0.2440  135 LEU B CB  
2697 C CG  . LEU B 60  ? 0.6483 0.4630 0.9310 -0.2193 -0.2318 0.2508  135 LEU B CG  
2698 C CD1 . LEU B 60  ? 0.6909 0.4532 0.9558 -0.2096 -0.2516 0.2528  135 LEU B CD1 
2699 C CD2 . LEU B 60  ? 0.7089 0.4758 0.9869 -0.2077 -0.2442 0.2270  135 LEU B CD2 
2700 N N   . TYR B 61  ? 0.5472 0.4951 0.9274 -0.1473 -0.1429 0.1970  136 TYR B N   
2701 C CA  . TYR B 61  ? 0.4257 0.4067 0.8313 -0.1206 -0.1167 0.1816  136 TYR B CA  
2702 C C   . TYR B 61  ? 0.4544 0.3827 0.8609 -0.0888 -0.1226 0.1550  136 TYR B C   
2703 O O   . TYR B 61  ? 0.5655 0.4338 0.9578 -0.0855 -0.1448 0.1456  136 TYR B O   
2704 C CB  . TYR B 61  ? 0.4759 0.5111 0.8991 -0.1202 -0.0997 0.1742  136 TYR B CB  
2705 C CG  . TYR B 61  ? 0.4031 0.5051 0.8239 -0.1381 -0.0866 0.1953  136 TYR B CG  
2706 C CD1 . TYR B 61  ? 0.5089 0.6644 0.9320 -0.1266 -0.0592 0.2007  136 TYR B CD1 
2707 C CD2 . TYR B 61  ? 0.4484 0.5589 0.8619 -0.1649 -0.1012 0.2085  136 TYR B CD2 
2708 C CE1 . TYR B 61  ? 0.7112 0.9292 1.1321 -0.1374 -0.0439 0.2167  136 TYR B CE1 
2709 C CE2 . TYR B 61  ? 0.4816 0.6602 0.8981 -0.1789 -0.0874 0.2275  136 TYR B CE2 
2710 C CZ  . TYR B 61  ? 0.5677 0.8011 0.9892 -0.1630 -0.0574 0.2303  136 TYR B CZ  
2711 O OH  . TYR B 61  ? 0.6316 0.9342 1.0571 -0.1721 -0.0413 0.2464  136 TYR B OH  
2712 N N   . ALA B 62  ? 0.5067 0.4639 0.9196 -0.0608 -0.1005 0.1396  137 ALA B N   
2713 C CA  . ALA B 62  ? 0.3988 0.3329 0.8155 -0.0284 -0.0978 0.1128  137 ALA B CA  
2714 C C   . ALA B 62  ? 0.3261 0.2944 0.7455 -0.0169 -0.0781 0.0927  137 ALA B C   
2715 O O   . ALA B 62  ? 0.5522 0.5675 0.9726 -0.0208 -0.0615 0.0985  137 ALA B O   
2716 C CB  . ALA B 62  ? 0.2911 0.2311 0.7123 -0.0112 -0.0934 0.1158  137 ALA B CB  
2717 N N   . VAL B 63  ? 0.3622 0.3035 0.7783 -0.0014 -0.0803 0.0689  138 VAL B N   
2718 C CA  . VAL B 63  ? 0.3324 0.2981 0.7452 0.0061  -0.0657 0.0506  138 VAL B CA  
2719 C C   . VAL B 63  ? 0.3359 0.2958 0.7487 0.0340  -0.0554 0.0279  138 VAL B C   
2720 O O   . VAL B 63  ? 0.4644 0.3852 0.8753 0.0487  -0.0637 0.0156  138 VAL B O   
2721 C CB  . VAL B 63  ? 0.4529 0.3965 0.8542 -0.0108 -0.0786 0.0456  138 VAL B CB  
2722 C CG1 . VAL B 63  ? 0.4597 0.4215 0.8529 -0.0022 -0.0664 0.0262  138 VAL B CG1 
2723 C CG2 . VAL B 63  ? 0.3181 0.2874 0.7275 -0.0416 -0.0869 0.0726  138 VAL B CG2 
2724 N N   . LYS B 64  ? 0.3645 0.3632 0.7780 0.0419  -0.0380 0.0231  139 LYS B N   
2725 C CA  . LYS B 64  ? 0.3797 0.3866 0.7761 0.0559  -0.0254 0.0051  139 LYS B CA  
2726 C C   . LYS B 64  ? 0.3270 0.3382 0.7149 0.0581  -0.0182 -0.0123 139 LYS B C   
2727 O O   . LYS B 64  ? 0.3477 0.3758 0.7360 0.0485  -0.0171 -0.0074 139 LYS B O   
2728 C CB  . LYS B 64  ? 0.3062 0.3408 0.6874 0.0536  -0.0158 0.0140  139 LYS B CB  
2729 C CG  . LYS B 64  ? 0.3958 0.4451 0.7671 0.0647  -0.0068 0.0030  139 LYS B CG  
2730 C CD  . LYS B 64  ? 0.4774 0.5466 0.8419 0.0603  -0.0055 0.0159  139 LYS B CD  
2731 C CE  . LYS B 64  ? 0.4411 0.5172 0.7861 0.0496  -0.0020 0.0213  139 LYS B CE  
2732 N NZ  . LYS B 64  ? 0.7207 0.8061 1.0622 0.0449  -0.0052 0.0352  139 LYS B NZ  
2733 N N   . ARG B 65  ? 0.4427 0.4413 0.8214 0.0721  -0.0129 -0.0323 140 ARG B N   
2734 C CA  . ARG B 65  ? 0.4888 0.4842 0.8548 0.0740  -0.0064 -0.0517 140 ARG B CA  
2735 C C   . ARG B 65  ? 0.5134 0.5385 0.8701 0.0851  0.0116  -0.0621 140 ARG B C   
2736 O O   . ARG B 65  ? 0.5064 0.5346 0.8630 0.1004  0.0171  -0.0659 140 ARG B O   
2737 C CB  . ARG B 65  ? 0.5286 0.4712 0.8734 0.0750  -0.0174 -0.0676 140 ARG B CB  
2738 C CG  . ARG B 65  ? 0.7598 0.6920 1.0718 0.0787  -0.0079 -0.0920 140 ARG B CG  
2739 C CD  . ARG B 65  ? 0.6372 0.5053 0.9156 0.0737  -0.0239 -0.1065 140 ARG B CD  
2740 N NE  . ARG B 65  ? 0.7493 0.5741 1.0259 0.0989  -0.0264 -0.1197 140 ARG B NE  
2741 C CZ  . ARG B 65  ? 0.7210 0.4728 0.9627 0.0983  -0.0442 -0.1328 140 ARG B CZ  
2742 N NH1 . ARG B 65  ? 0.8614 0.5796 1.0695 0.0688  -0.0627 -0.1318 140 ARG B NH1 
2743 N NH2 . ARG B 65  ? 0.7039 0.4218 0.9318 0.1236  -0.0441 -0.1405 140 ARG B NH2 
2744 N N   . SER B 66  ? 0.4509 0.5003 0.7999 0.0767  0.0193  -0.0640 141 SER B N   
2745 C CA  . SER B 66  ? 0.4200 0.5017 0.7635 0.0819  0.0356  -0.0718 141 SER B CA  
2746 C C   . SER B 66  ? 0.5568 0.6251 0.8853 0.0966  0.0468  -0.0973 141 SER B C   
2747 O O   . SER B 66  ? 0.7063 0.7316 1.0094 0.0939  0.0390  -0.1101 141 SER B O   
2748 C CB  . SER B 66  ? 0.4275 0.5243 0.7474 0.0629  0.0358  -0.0658 141 SER B CB  
2749 O OG  . SER B 66  ? 0.6296 0.6996 0.9230 0.0519  0.0272  -0.0723 141 SER B OG  
2750 N N   . MET B 67  ? 0.6009 0.7062 0.9373 0.1102  0.0641  -0.1023 142 MET B N   
2751 C CA  . MET B 67  ? 0.6111 0.7083 0.9325 0.1321  0.0796  -0.1273 142 MET B CA  
2752 C C   . MET B 67  ? 0.7256 0.8103 1.0024 0.1190  0.0877  -0.1462 142 MET B C   
2753 O O   . MET B 67  ? 0.8155 0.8453 1.0578 0.1203  0.0803  -0.1634 142 MET B O   
2754 C CB  . MET B 67  ? 0.7503 0.9021 1.0858 0.1477  0.0959  -0.1195 142 MET B CB  
2755 C CG  . MET B 67  ? 0.9743 1.1225 1.2919 0.1766  0.1159  -0.1434 142 MET B CG  
2756 S SD  . MET B 67  ? 1.4509 1.6826 1.7947 0.1950  0.1400  -0.1298 142 MET B SD  
2757 C CE  . MET B 67  ? 1.0615 1.2664 1.3743 0.2341  0.1651  -0.1610 142 MET B CE  
2758 N N   . SER B 68  ? 0.6540 0.7825 0.9202 0.1011  0.0982  -0.1390 143 SER B N   
2759 C CA  . SER B 68  ? 0.5952 0.7152 0.8097 0.0838  0.1045  -0.1513 143 SER B CA  
2760 C C   . SER B 68  ? 0.4220 0.5259 0.6158 0.0524  0.0833  -0.1340 143 SER B C   
2761 O O   . SER B 68  ? 0.6563 0.7720 0.8753 0.0450  0.0715  -0.1124 143 SER B O   
2762 C CB  . SER B 68  ? 0.7582 0.9411 0.9704 0.0838  0.1314  -0.1542 143 SER B CB  
2763 O OG  . SER B 68  ? 1.0626 1.2934 1.3026 0.0669  0.1278  -0.1274 143 SER B OG  
2764 N N   . PRO B 69  ? 0.5885 0.6624 0.7337 0.0353  0.0770  -0.1431 144 PRO B N   
2765 C CA  . PRO B 69  ? 0.4871 0.5475 0.6150 0.0099  0.0551  -0.1261 144 PRO B CA  
2766 C C   . PRO B 69  ? 0.6354 0.7323 0.7634 -0.0049 0.0572  -0.1078 144 PRO B C   
2767 O O   . PRO B 69  ? 0.8047 0.9435 0.9407 -0.0035 0.0761  -0.1073 144 PRO B O   
2768 C CB  . PRO B 69  ? 0.5753 0.6011 0.6472 -0.0053 0.0495  -0.1407 144 PRO B CB  
2769 C CG  . PRO B 69  ? 0.6064 0.6056 0.6680 0.0146  0.0610  -0.1663 144 PRO B CG  
2770 C CD  . PRO B 69  ? 0.5222 0.5639 0.6232 0.0410  0.0859  -0.1702 144 PRO B CD  
2771 N N   . PHE B 70  ? 0.7010 0.7807 0.8191 -0.0194 0.0356  -0.0914 145 PHE B N   
2772 C CA  . PHE B 70  ? 0.4437 0.5385 0.5513 -0.0347 0.0302  -0.0732 145 PHE B CA  
2773 C C   . PHE B 70  ? 0.6310 0.7414 0.6961 -0.0569 0.0395  -0.0756 145 PHE B C   
2774 O O   . PHE B 70  ? 0.6975 0.7858 0.7219 -0.0691 0.0351  -0.0843 145 PHE B O   
2775 C CB  . PHE B 70  ? 0.4442 0.5074 0.5410 -0.0398 0.0044  -0.0593 145 PHE B CB  
2776 C CG  . PHE B 70  ? 0.4873 0.5450 0.6242 -0.0205 -0.0019 -0.0542 145 PHE B CG  
2777 C CD1 . PHE B 70  ? 0.3894 0.4665 0.5623 -0.0070 0.0091  -0.0516 145 PHE B CD1 
2778 C CD2 . PHE B 70  ? 0.5874 0.6259 0.7269 -0.0174 -0.0194 -0.0496 145 PHE B CD2 
2779 C CE1 . PHE B 70  ? 0.4061 0.4787 0.6100 0.0069  0.0038  -0.0452 145 PHE B CE1 
2780 C CE2 . PHE B 70  ? 0.4655 0.5091 0.6423 -0.0023 -0.0224 -0.0427 145 PHE B CE2 
2781 C CZ  . PHE B 70  ? 0.4346 0.4929 0.6402 0.0088  -0.0102 -0.0408 145 PHE B CZ  
2782 N N   . ARG B 71  ? 0.6016 0.7528 0.6746 -0.0655 0.0513  -0.0655 146 ARG B N   
2783 C CA  . ARG B 71  ? 0.6077 0.7840 0.6413 -0.0923 0.0609  -0.0626 146 ARG B CA  
2784 C C   . ARG B 71  ? 0.6702 0.8088 0.6536 -0.1221 0.0335  -0.0453 146 ARG B C   
2785 O O   . ARG B 71  ? 0.7856 0.9229 0.7206 -0.1477 0.0338  -0.0448 146 ARG B O   
2786 C CB  . ARG B 71  ? 0.7940 1.0354 0.8574 -0.0963 0.0796  -0.0523 146 ARG B CB  
2787 C CG  . ARG B 71  ? 0.8170 1.1002 0.9306 -0.0628 0.1069  -0.0690 146 ARG B CG  
2788 C CD  . ARG B 71  ? 0.6479 1.0034 0.8024 -0.0660 0.1201  -0.0529 146 ARG B CD  
2789 N NE  . ARG B 71  ? 1.0653 1.4579 1.2738 -0.0279 0.1420  -0.0670 146 ARG B NE  
2790 C CZ  . ARG B 71  ? 1.0946 1.4686 1.3448 -0.0029 0.1325  -0.0666 146 ARG B CZ  
2791 N NH1 . ARG B 71  ? 0.9571 1.2820 1.2025 -0.0106 0.1059  -0.0543 146 ARG B NH1 
2792 N NH2 . ARG B 71  ? 0.9174 1.3223 1.2127 0.0321  0.1502  -0.0786 146 ARG B NH2 
2793 N N   . GLY B 72  ? 0.6347 0.7393 0.6246 -0.1179 0.0095  -0.0315 147 GLY B N   
2794 C CA  . GLY B 72  ? 0.5074 0.5670 0.4493 -0.1389 -0.0195 -0.0157 147 GLY B CA  
2795 C C   . GLY B 72  ? 0.5497 0.5713 0.5046 -0.1201 -0.0406 -0.0069 147 GLY B C   
2796 O O   . GLY B 72  ? 0.6023 0.6346 0.6032 -0.0939 -0.0322 -0.0125 147 GLY B O   
2797 N N   . PRO B 73  ? 0.5402 0.5137 0.4506 -0.1322 -0.0687 0.0069  148 PRO B N   
2798 C CA  . PRO B 73  ? 0.4114 0.3457 0.3268 -0.1093 -0.0868 0.0132  148 PRO B CA  
2799 C C   . PRO B 73  ? 0.5197 0.4650 0.4539 -0.1045 -0.0796 0.0192  148 PRO B C   
2800 O O   . PRO B 73  ? 0.6117 0.5546 0.5777 -0.0763 -0.0759 0.0152  148 PRO B O   
2801 C CB  . PRO B 73  ? 0.6218 0.4973 0.4739 -0.1260 -0.1191 0.0268  148 PRO B CB  
2802 C CG  . PRO B 73  ? 0.7105 0.5939 0.5349 -0.1516 -0.1198 0.0251  148 PRO B CG  
2803 C CD  . PRO B 73  ? 0.5147 0.4612 0.3641 -0.1640 -0.0865 0.0160  148 PRO B CD  
2804 N N   . LYS B 74  ? 0.6497 0.6090 0.5629 -0.1347 -0.0793 0.0311  149 LYS B N   
2805 C CA  . LYS B 74  ? 0.4897 0.4622 0.4202 -0.1354 -0.0761 0.0396  149 LYS B CA  
2806 C C   . LYS B 74  ? 0.5139 0.5409 0.5120 -0.1116 -0.0490 0.0279  149 LYS B C   
2807 O O   . LYS B 74  ? 0.6597 0.6811 0.6799 -0.0939 -0.0489 0.0292  149 LYS B O   
2808 C CB  . LYS B 74  ? 0.5901 0.5814 0.4919 -0.1785 -0.0817 0.0582  149 LYS B CB  
2809 C CG  . LYS B 74  ? 1.1693 1.1809 1.0889 -0.1871 -0.0824 0.0713  149 LYS B CG  
2810 C CD  . LYS B 74  ? 1.4126 1.3468 1.2913 -0.1793 -0.1092 0.0775  149 LYS B CD  
2811 C CE  . LYS B 74  ? 1.4543 1.3966 1.3287 -0.2030 -0.1191 0.0961  149 LYS B CE  
2812 N NZ  . LYS B 74  ? 1.2287 1.0954 1.0645 -0.1884 -0.1398 0.0969  149 LYS B NZ  
2813 N N   . ASP B 75  ? 0.5533 0.6268 0.5784 -0.1102 -0.0271 0.0159  150 ASP B N   
2814 C CA  . ASP B 75  ? 0.4299 0.5431 0.5134 -0.0849 -0.0049 0.0035  150 ASP B CA  
2815 C C   . ASP B 75  ? 0.4727 0.5562 0.5756 -0.0562 -0.0094 -0.0049 150 ASP B C   
2816 O O   . ASP B 75  ? 0.5416 0.6364 0.6818 -0.0385 -0.0031 -0.0054 150 ASP B O   
2817 C CB  . ASP B 75  ? 0.4735 0.6263 0.5680 -0.0850 0.0176  -0.0115 150 ASP B CB  
2818 C CG  . ASP B 75  ? 0.5231 0.7069 0.6715 -0.0566 0.0377  -0.0252 150 ASP B CG  
2819 O OD1 . ASP B 75  ? 0.8379 1.0300 1.0199 -0.0449 0.0360  -0.0175 150 ASP B OD1 
2820 O OD2 . ASP B 75  ? 0.6668 0.8596 0.8179 -0.0463 0.0531  -0.0437 150 ASP B OD2 
2821 N N   . ARG B 76  ? 0.4063 0.4557 0.4853 -0.0531 -0.0218 -0.0090 151 ARG B N   
2822 C CA  . ARG B 76  ? 0.4070 0.4401 0.5083 -0.0287 -0.0264 -0.0129 151 ARG B CA  
2823 C C   . ARG B 76  ? 0.4746 0.4853 0.5716 -0.0169 -0.0356 -0.0026 151 ARG B C   
2824 O O   . ARG B 76  ? 0.5052 0.5247 0.6344 0.0016  -0.0289 -0.0034 151 ARG B O   
2825 C CB  . ARG B 76  ? 0.4984 0.5085 0.5786 -0.0295 -0.0403 -0.0159 151 ARG B CB  
2826 C CG  . ARG B 76  ? 0.4467 0.4531 0.5554 -0.0068 -0.0461 -0.0157 151 ARG B CG  
2827 C CD  . ARG B 76  ? 0.4722 0.4644 0.5663 -0.0098 -0.0629 -0.0157 151 ARG B CD  
2828 N NE  . ARG B 76  ? 0.6044 0.6051 0.7312 0.0111  -0.0695 -0.0107 151 ARG B NE  
2829 C CZ  . ARG B 76  ? 0.6084 0.5968 0.7315 0.0304  -0.0800 -0.0018 151 ARG B CZ  
2830 N NH1 . ARG B 76  ? 0.8603 0.8128 0.9408 0.0305  -0.0893 0.0023  151 ARG B NH1 
2831 N NH2 . ARG B 76  ? 0.7063 0.7186 0.8672 0.0501  -0.0815 0.0036  151 ARG B NH2 
2832 N N   . ALA B 77  ? 0.5100 0.4858 0.5602 -0.0288 -0.0520 0.0072  152 ALA B N   
2833 C CA  . ALA B 77  ? 0.3480 0.2897 0.3798 -0.0158 -0.0615 0.0139  152 ALA B CA  
2834 C C   . ALA B 77  ? 0.4918 0.4542 0.5446 -0.0187 -0.0516 0.0187  152 ALA B C   
2835 O O   . ALA B 77  ? 0.5878 0.5352 0.6420 -0.0017 -0.0512 0.0202  152 ALA B O   
2836 C CB  . ALA B 77  ? 0.5094 0.3951 0.4755 -0.0303 -0.0857 0.0230  152 ALA B CB  
2837 N N   . ARG B 78  ? 0.5987 0.5990 0.6681 -0.0392 -0.0434 0.0219  153 ARG B N   
2838 C CA  . ARG B 78  ? 0.4353 0.4609 0.5305 -0.0421 -0.0374 0.0293  153 ARG B CA  
2839 C C   . ARG B 78  ? 0.5616 0.6120 0.7087 -0.0178 -0.0222 0.0214  153 ARG B C   
2840 O O   . ARG B 78  ? 0.5982 0.6420 0.7531 -0.0099 -0.0234 0.0272  153 ARG B O   
2841 C CB  . ARG B 78  ? 0.6081 0.6800 0.7155 -0.0674 -0.0319 0.0367  153 ARG B CB  
2842 C CG  . ARG B 78  ? 0.7872 0.8953 0.9301 -0.0701 -0.0283 0.0474  153 ARG B CG  
2843 C CD  . ARG B 78  ? 0.8819 1.0505 1.0443 -0.0932 -0.0216 0.0574  153 ARG B CD  
2844 N NE  . ARG B 78  ? 0.7867 0.9383 0.8989 -0.1306 -0.0412 0.0755  153 ARG B NE  
2845 C CZ  . ARG B 78  ? 0.6150 0.7692 0.6961 -0.1529 -0.0423 0.0770  153 ARG B CZ  
2846 N NH1 . ARG B 78  ? 0.5093 0.6825 0.6017 -0.1407 -0.0240 0.0599  153 ARG B NH1 
2847 N NH2 . ARG B 78  ? 0.9616 1.0941 0.9930 -0.1917 -0.0649 0.0974  153 ARG B NH2 
2848 N N   . LYS B 79  ? 0.4340 0.5068 0.6102 -0.0086 -0.0103 0.0089  154 LYS B N   
2849 C CA  . LYS B 79  ? 0.4914 0.5779 0.7100 0.0103  -0.0008 0.0031  154 LYS B CA  
2850 C C   . LYS B 79  ? 0.4332 0.4960 0.6468 0.0246  -0.0057 0.0053  154 LYS B C   
2851 O O   . LYS B 79  ? 0.4725 0.5405 0.7079 0.0337  -0.0021 0.0096  154 LYS B O   
2852 C CB  . LYS B 79  ? 0.4118 0.5139 0.6496 0.0144  0.0088  -0.0115 154 LYS B CB  
2853 C CG  . LYS B 79  ? 0.3798 0.5142 0.6265 0.0076  0.0207  -0.0172 154 LYS B CG  
2854 C CD  . LYS B 79  ? 0.5279 0.6654 0.7893 0.0190  0.0311  -0.0353 154 LYS B CD  
2855 C CE  . LYS B 79  ? 0.5931 0.7549 0.8412 0.0119  0.0447  -0.0459 154 LYS B CE  
2856 N NZ  . LYS B 79  ? 0.7567 0.9658 1.0332 0.0156  0.0577  -0.0413 154 LYS B NZ  
2857 N N   . LEU B 80  ? 0.4520 0.4923 0.6378 0.0276  -0.0138 0.0037  155 LEU B N   
2858 C CA  . LEU B 80  ? 0.3888 0.4187 0.5750 0.0460  -0.0154 0.0061  155 LEU B CA  
2859 C C   . LEU B 80  ? 0.5075 0.5144 0.6675 0.0528  -0.0172 0.0133  155 LEU B C   
2860 O O   . LEU B 80  ? 0.5323 0.5412 0.6984 0.0702  -0.0118 0.0153  155 LEU B O   
2861 C CB  . LEU B 80  ? 0.3515 0.3649 0.5167 0.0520  -0.0259 0.0037  155 LEU B CB  
2862 C CG  . LEU B 80  ? 0.4217 0.4538 0.6096 0.0478  -0.0273 -0.0019 155 LEU B CG  
2863 C CD1 . LEU B 80  ? 0.5349 0.5492 0.7005 0.0542  -0.0425 -0.0003 155 LEU B CD1 
2864 C CD2 . LEU B 80  ? 0.5046 0.5657 0.7375 0.0551  -0.0195 -0.0006 155 LEU B CD2 
2865 N N   . ALA B 81  ? 0.4752 0.4614 0.6032 0.0374  -0.0252 0.0182  156 ALA B N   
2866 C CA  . ALA B 81  ? 0.3901 0.3419 0.4799 0.0404  -0.0310 0.0245  156 ALA B CA  
2867 C C   . ALA B 81  ? 0.4942 0.4662 0.6118 0.0462  -0.0205 0.0291  156 ALA B C   
2868 O O   . ALA B 81  ? 0.6188 0.5650 0.7060 0.0559  -0.0204 0.0317  156 ALA B O   
2869 C CB  . ALA B 81  ? 0.4476 0.3758 0.4991 0.0141  -0.0461 0.0328  156 ALA B CB  
2870 N N   . GLU B 82  ? 0.4420 0.4543 0.6110 0.0410  -0.0127 0.0299  157 GLU B N   
2871 C CA  . GLU B 82  ? 0.3790 0.4057 0.5731 0.0445  -0.0067 0.0365  157 GLU B CA  
2872 C C   . GLU B 82  ? 0.4936 0.5255 0.6938 0.0616  0.0029  0.0356  157 GLU B C   
2873 O O   . GLU B 82  ? 0.5107 0.5413 0.7054 0.0644  0.0074  0.0430  157 GLU B O   
2874 C CB  . GLU B 82  ? 0.4223 0.4817 0.6666 0.0392  -0.0035 0.0364  157 GLU B CB  
2875 C CG  . GLU B 82  ? 0.6236 0.6909 0.8918 0.0400  -0.0029 0.0461  157 GLU B CG  
2876 C CD  . GLU B 82  ? 0.5674 0.6542 0.8740 0.0385  -0.0034 0.0445  157 GLU B CD  
2877 O OE1 . GLU B 82  ? 0.6044 0.7016 0.9146 0.0376  -0.0004 0.0342  157 GLU B OE1 
2878 O OE2 . GLU B 82  ? 0.5732 0.6571 0.8904 0.0374  -0.0066 0.0521  157 GLU B OE2 
2879 N N   . VAL B 83  ? 0.4436 0.4865 0.6553 0.0710  0.0057  0.0286  158 VAL B N   
2880 C CA  . VAL B 83  ? 0.3692 0.4304 0.5927 0.0869  0.0147  0.0309  158 VAL B CA  
2881 C C   . VAL B 83  ? 0.4461 0.4811 0.6231 0.1050  0.0182  0.0303  158 VAL B C   
2882 O O   . VAL B 83  ? 0.5897 0.6385 0.7659 0.1158  0.0303  0.0354  158 VAL B O   
2883 C CB  . VAL B 83  ? 0.4914 0.5712 0.7335 0.0890  0.0118  0.0254  158 VAL B CB  
2884 C CG1 . VAL B 83  ? 0.4231 0.5340 0.6766 0.0965  0.0188  0.0299  158 VAL B CG1 
2885 C CG2 . VAL B 83  ? 0.3321 0.4184 0.5939 0.0700  0.0073  0.0211  158 VAL B CG2 
2886 N N   . GLY B 84  ? 0.4913 0.4843 0.6229 0.1083  0.0073  0.0241  159 GLY B N   
2887 C CA  . GLY B 84  ? 0.3639 0.3147 0.4384 0.1280  0.0074  0.0206  159 GLY B CA  
2888 C C   . GLY B 84  ? 0.5010 0.4270 0.5412 0.1192  0.0087  0.0257  159 GLY B C   
2889 O O   . GLY B 84  ? 0.6817 0.5843 0.6808 0.1387  0.0169  0.0226  159 GLY B O   
2890 N N   . SER B 85  ? 0.4677 0.3991 0.5228 0.0915  0.0006  0.0335  160 SER B N   
2891 C CA  . SER B 85  ? 0.5078 0.4180 0.5336 0.0791  -0.0029 0.0418  160 SER B CA  
2892 C C   . SER B 85  ? 0.5788 0.5203 0.6270 0.0862  0.0140  0.0478  160 SER B C   
2893 O O   . SER B 85  ? 0.6815 0.5971 0.6839 0.0898  0.0180  0.0501  160 SER B O   
2894 C CB  . SER B 85  ? 0.6138 0.5335 0.6611 0.0500  -0.0173 0.0514  160 SER B CB  
2895 O OG  . SER B 85  ? 0.6333 0.5316 0.6585 0.0381  -0.0318 0.0492  160 SER B OG  
2896 N N   . HIS B 86  ? 0.6304 0.6235 0.7423 0.0851  0.0224  0.0512  161 HIS B N   
2897 C CA  . HIS B 86  ? 0.4405 0.4659 0.5727 0.0877  0.0370  0.0599  161 HIS B CA  
2898 C C   . HIS B 86  ? 0.6323 0.6634 0.7375 0.1145  0.0551  0.0546  161 HIS B C   
2899 O O   . HIS B 86  ? 0.7639 0.8046 0.8515 0.1175  0.0689  0.0612  161 HIS B O   
2900 C CB  . HIS B 86  ? 0.4781 0.5486 0.6765 0.0794  0.0379  0.0646  161 HIS B CB  
2901 C CG  . HIS B 86  ? 0.3560 0.4268 0.5811 0.0587  0.0265  0.0738  161 HIS B CG  
2902 N ND1 . HIS B 86  ? 0.3844 0.4635 0.6169 0.0471  0.0272  0.0886  161 HIS B ND1 
2903 C CD2 . HIS B 86  ? 0.2889 0.3539 0.5352 0.0500  0.0141  0.0707  161 HIS B CD2 
2904 C CE1 . HIS B 86  ? 0.4913 0.5638 0.7488 0.0344  0.0128  0.0940  161 HIS B CE1 
2905 N NE2 . HIS B 86  ? 0.4020 0.4698 0.6705 0.0382  0.0067  0.0824  161 HIS B NE2 
2906 N N   . GLU B 87  ? 0.6142 0.6419 0.7158 0.1356  0.0557  0.0433  162 GLU B N   
2907 C CA  . GLU B 87  ? 0.5673 0.6038 0.6479 0.1695  0.0730  0.0370  162 GLU B CA  
2908 C C   . GLU B 87  ? 0.7371 0.7141 0.7359 0.1829  0.0764  0.0295  162 GLU B C   
2909 O O   . GLU B 87  ? 0.8164 0.8075 0.7935 0.2064  0.0982  0.0275  162 GLU B O   
2910 C CB  . GLU B 87  ? 0.7399 0.7760 0.8318 0.1896  0.0661  0.0276  162 GLU B CB  
2911 C CG  . GLU B 87  ? 0.9812 1.0291 1.0580 0.2271  0.0799  0.0199  162 GLU B CG  
2912 C CD  . GLU B 87  ? 1.1423 1.1859 1.2317 0.2300  0.0631  0.0120  162 GLU B CD  
2913 O OE1 . GLU B 87  ? 1.1531 1.1823 1.2559 0.2112  0.0451  0.0126  162 GLU B OE1 
2914 O OE2 . GLU B 87  ? 1.0470 1.1028 1.1332 0.2526  0.0688  0.0067  162 GLU B OE2 
2915 N N   . LYS B 88  ? 0.7508 0.6617 0.7002 0.1669  0.0548  0.0259  163 LYS B N   
2916 C CA  . LYS B 88  ? 0.6919 0.5318 0.5518 0.1748  0.0518  0.0189  163 LYS B CA  
2917 C C   . LYS B 88  ? 0.6847 0.5282 0.5270 0.1562  0.0588  0.0297  163 LYS B C   
2918 O O   . LYS B 88  ? 0.9009 0.7039 0.6723 0.1703  0.0681  0.0233  163 LYS B O   
2919 C CB  . LYS B 88  ? 0.7024 0.4713 0.5138 0.1555  0.0215  0.0163  163 LYS B CB  
2920 C CG  . LYS B 88  ? 0.8044 0.5514 0.6114 0.1719  0.0106  0.0063  163 LYS B CG  
2921 C CD  . LYS B 88  ? 0.8574 0.5366 0.6129 0.1440  -0.0210 0.0085  163 LYS B CD  
2922 C CE  . LYS B 88  ? 0.9213 0.5711 0.6636 0.1567  -0.0350 0.0008  163 LYS B CE  
2923 N NZ  . LYS B 88  ? 1.3062 0.8924 0.9953 0.1229  -0.0673 0.0068  163 LYS B NZ  
2924 N N   . VAL B 89  ? 0.6272 0.5128 0.5271 0.1260  0.0533  0.0456  164 VAL B N   
2925 C CA  . VAL B 89  ? 0.7362 0.6217 0.6200 0.1051  0.0545  0.0593  164 VAL B CA  
2926 C C   . VAL B 89  ? 0.7718 0.7049 0.6646 0.1205  0.0844  0.0627  164 VAL B C   
2927 O O   . VAL B 89  ? 0.9470 0.8588 0.7816 0.1214  0.0950  0.0643  164 VAL B O   
2928 C CB  . VAL B 89  ? 0.6871 0.5986 0.6305 0.0724  0.0364  0.0756  164 VAL B CB  
2929 C CG1 . VAL B 89  ? 0.7256 0.6429 0.6611 0.0524  0.0364  0.0928  164 VAL B CG1 
2930 C CG2 . VAL B 89  ? 0.6203 0.4927 0.5485 0.0550  0.0094  0.0757  164 VAL B CG2 
2931 N N   . GLY B 90  ? 0.6948 0.6949 0.6574 0.1302  0.0979  0.0652  165 GLY B N   
2932 C CA  . GLY B 90  ? 0.7269 0.7867 0.7068 0.1403  0.1260  0.0728  165 GLY B CA  
2933 C C   . GLY B 90  ? 0.6571 0.7479 0.6679 0.1047  0.1227  0.0957  165 GLY B C   
2934 O O   . GLY B 90  ? 0.7705 0.8500 0.8130 0.0781  0.0991  0.1046  165 GLY B O   
2935 N N   . GLN B 91  ? 0.7030 0.8334 0.7023 0.1056  0.1470  0.1058  166 GLN B N   
2936 C CA  . GLN B 91  ? 0.7263 0.8870 0.7491 0.0699  0.1442  0.1309  166 GLN B CA  
2937 C C   . GLN B 91  ? 0.6017 0.7136 0.5492 0.0544  0.1417  0.1369  166 GLN B C   
2938 O O   . GLN B 91  ? 0.8718 0.9806 0.7585 0.0716  0.1667  0.1303  166 GLN B O   
2939 C CB  . GLN B 91  ? 0.5234 0.7712 0.5881 0.0715  0.1707  0.1444  166 GLN B CB  
2940 C CG  . GLN B 91  ? 0.7210 1.0188 0.8643 0.0758  0.1659  0.1452  166 GLN B CG  
2941 C CD  . GLN B 91  ? 1.0756 1.4661 1.2659 0.0668  0.1862  0.1658  166 GLN B CD  
2942 O OE1 . GLN B 91  ? 1.0406 1.4606 1.2852 0.0365  0.1704  0.1839  166 GLN B OE1 
2943 N NE2 . GLN B 91  ? 1.1276 1.5648 1.2951 0.0931  0.2209  0.1638  166 GLN B NE2 
2944 N N   . HIS B 92  ? 0.6979 0.7716 0.6479 0.0236  0.1113  0.1492  167 HIS B N   
2945 C CA  . HIS B 92  ? 0.6263 0.6568 0.5140 0.0002  0.1009  0.1617  167 HIS B CA  
2946 C C   . HIS B 92  ? 0.6346 0.6765 0.5663 -0.0364 0.0778  0.1885  167 HIS B C   
2947 O O   . HIS B 92  ? 0.7055 0.7561 0.7025 -0.0407 0.0589  0.1904  167 HIS B O   
2948 C CB  . HIS B 92  ? 0.6462 0.6016 0.4803 0.0016  0.0778  0.1500  167 HIS B CB  
2949 C CG  . HIS B 92  ? 0.6596 0.5650 0.4162 -0.0214 0.0663  0.1616  167 HIS B CG  
2950 N ND1 . HIS B 92  ? 0.7775 0.6590 0.5441 -0.0542 0.0319  0.1824  167 HIS B ND1 
2951 C CD2 . HIS B 92  ? 0.8989 0.7718 0.5633 -0.0154 0.0838  0.1552  167 HIS B CD2 
2952 C CE1 . HIS B 92  ? 0.8385 0.6749 0.5231 -0.0716 0.0257  0.1907  167 HIS B CE1 
2953 N NE2 . HIS B 92  ? 0.9439 0.7711 0.5609 -0.0493 0.0577  0.1733  167 HIS B NE2 
2954 N N   . PRO B 93  ? 0.6552 0.6927 0.5480 -0.0622 0.0780  0.2093  168 PRO B N   
2955 C CA  . PRO B 93  ? 0.6219 0.6642 0.5529 -0.0969 0.0529  0.2371  168 PRO B CA  
2956 C C   . PRO B 93  ? 0.6996 0.6977 0.6582 -0.1056 0.0126  0.2409  168 PRO B C   
2957 O O   . PRO B 93  ? 0.8077 0.8057 0.8077 -0.1254 -0.0105 0.2600  168 PRO B O   
2958 C CB  . PRO B 93  ? 0.6455 0.6785 0.5082 -0.1226 0.0595  0.2572  168 PRO B CB  
2959 C CG  . PRO B 93  ? 0.8844 0.9403 0.6948 -0.0967 0.1018  0.2393  168 PRO B CG  
2960 C CD  . PRO B 93  ? 0.6957 0.7255 0.5050 -0.0597 0.1034  0.2083  168 PRO B CD  
2961 N N   . CYS B 94  ? 0.5876 0.5494 0.5250 -0.0914 0.0024  0.2248  169 CYS B N   
2962 C CA  . CYS B 94  ? 0.5816 0.5152 0.5484 -0.0992 -0.0336 0.2311  169 CYS B CA  
2963 C C   . CYS B 94  ? 0.5519 0.4957 0.5664 -0.0759 -0.0345 0.2099  169 CYS B C   
2964 O O   . CYS B 94  ? 0.6364 0.5625 0.6647 -0.0778 -0.0581 0.2109  169 CYS B O   
2965 C CB  . CYS B 94  ? 0.5841 0.4681 0.4832 -0.1148 -0.0533 0.2395  169 CYS B CB  
2966 S SG  . CYS B 94  ? 0.8405 0.7038 0.6756 -0.1484 -0.0589 0.2677  169 CYS B SG  
2967 N N   . CYS B 95  ? 0.4868 0.4634 0.5269 -0.0558 -0.0101 0.1931  170 CYS B N   
2968 C CA  . CYS B 95  ? 0.4466 0.4325 0.5264 -0.0363 -0.0101 0.1738  170 CYS B CA  
2969 C C   . CYS B 95  ? 0.4299 0.4541 0.5728 -0.0312 -0.0031 0.1718  170 CYS B C   
2970 O O   . CYS B 95  ? 0.6497 0.7024 0.7952 -0.0347 0.0134  0.1781  170 CYS B O   
2971 C CB  . CYS B 95  ? 0.6282 0.6026 0.6631 -0.0153 0.0081  0.1527  170 CYS B CB  
2972 S SG  . CYS B 95  ? 0.7551 0.6664 0.7025 -0.0229 -0.0060 0.1515  170 CYS B SG  
2973 N N   . VAL B 96  ? 0.5947 0.6210 0.7857 -0.0248 -0.0160 0.1640  171 VAL B N   
2974 C CA  . VAL B 96  ? 0.5238 0.5738 0.7660 -0.0218 -0.0139 0.1605  171 VAL B CA  
2975 C C   . VAL B 96  ? 0.4880 0.5676 0.7292 -0.0080 0.0097  0.1474  171 VAL B C   
2976 O O   . VAL B 96  ? 0.5428 0.6187 0.7701 0.0090  0.0170  0.1305  171 VAL B O   
2977 C CB  . VAL B 96  ? 0.3553 0.3979 0.6385 -0.0131 -0.0290 0.1505  171 VAL B CB  
2978 C CG1 . VAL B 96  ? 0.4464 0.5030 0.7678 -0.0092 -0.0263 0.1424  171 VAL B CG1 
2979 C CG2 . VAL B 96  ? 0.3483 0.3698 0.6438 -0.0217 -0.0533 0.1658  171 VAL B CG2 
2980 N N   . ARG B 97  ? 0.4038 0.5142 0.6602 -0.0167 0.0192  0.1576  172 ARG B N   
2981 C CA  . ARG B 97  ? 0.4703 0.6213 0.7329 -0.0033 0.0411  0.1502  172 ARG B CA  
2982 C C   . ARG B 97  ? 0.5175 0.6801 0.8238 0.0023  0.0348  0.1390  172 ARG B C   
2983 O O   . ARG B 97  ? 0.4408 0.5979 0.7773 -0.0134 0.0191  0.1457  172 ARG B O   
2984 C CB  . ARG B 97  ? 0.4316 0.6245 0.6954 -0.0187 0.0547  0.1705  172 ARG B CB  
2985 C CG  . ARG B 97  ? 0.4438 0.6941 0.7243 -0.0025 0.0780  0.1664  172 ARG B CG  
2986 C CD  . ARG B 97  ? 0.6245 0.9306 0.9103 -0.0204 0.0939  0.1901  172 ARG B CD  
2987 N NE  . ARG B 97  ? 0.9370 1.2522 1.2594 -0.0557 0.0738  0.2112  172 ARG B NE  
2988 C CZ  . ARG B 97  ? 1.0561 1.3453 1.3644 -0.0862 0.0581  0.2313  172 ARG B CZ  
2989 N NH1 . ARG B 97  ? 0.9374 1.1959 1.1987 -0.0878 0.0605  0.2347  172 ARG B NH1 
2990 N NH2 . ARG B 97  ? 0.9792 1.2668 1.3162 -0.1174 0.0362  0.2496  172 ARG B NH2 
2991 N N   . LEU B 98  ? 0.4498 0.6210 0.7527 0.0241  0.0447  0.1219  173 LEU B N   
2992 C CA  . LEU B 98  ? 0.2856 0.4693 0.6221 0.0284  0.0395  0.1119  173 LEU B CA  
2993 C C   . LEU B 98  ? 0.4316 0.6694 0.7946 0.0255  0.0496  0.1226  173 LEU B C   
2994 O O   . LEU B 98  ? 0.4748 0.7450 0.8261 0.0415  0.0689  0.1242  173 LEU B O   
2995 C CB  . LEU B 98  ? 0.4004 0.5661 0.7185 0.0495  0.0412  0.0920  173 LEU B CB  
2996 C CG  . LEU B 98  ? 0.4405 0.6107 0.7737 0.0523  0.0349  0.0793  173 LEU B CG  
2997 C CD1 . LEU B 98  ? 0.2754 0.4211 0.6216 0.0380  0.0195  0.0738  173 LEU B CD1 
2998 C CD2 . LEU B 98  ? 0.4589 0.6107 0.7616 0.0705  0.0366  0.0636  173 LEU B CD2 
2999 N N   . GLU B 99  ? 0.3421 0.5870 0.7352 0.0057  0.0355  0.1292  174 GLU B N   
3000 C CA  . GLU B 99  ? 0.3595 0.6468 0.7642 -0.0038 0.0379  0.1385  174 GLU B CA  
3001 C C   . GLU B 99  ? 0.3229 0.6137 0.7263 0.0099  0.0347  0.1214  174 GLU B C   
3002 O O   . GLU B 99  ? 0.5147 0.8399 0.9146 0.0259  0.0469  0.1187  174 GLU B O   
3003 C CB  . GLU B 99  ? 0.3454 0.6270 0.7688 -0.0376 0.0188  0.1564  174 GLU B CB  
3004 C CG  . GLU B 99  ? 0.6091 0.8834 1.0283 -0.0572 0.0171  0.1771  174 GLU B CG  
3005 C CD  . GLU B 99  ? 0.7065 1.0346 1.1157 -0.0610 0.0383  0.1941  174 GLU B CD  
3006 O OE1 . GLU B 99  ? 0.6267 1.0013 1.0439 -0.0599 0.0462  0.1964  174 GLU B OE1 
3007 O OE2 . GLU B 99  ? 0.7739 1.0987 1.1662 -0.0653 0.0474  0.2055  174 GLU B OE2 
3008 N N   A GLN B 100 ? 0.3765 0.6317 0.7829 0.0045  0.0181  0.1100  175 GLN B N   
3009 N N   B GLN B 100 ? 0.3747 0.6307 0.7817 0.0040  0.0180  0.1104  175 GLN B N   
3010 C CA  A GLN B 100 ? 0.3011 0.5579 0.7065 0.0112  0.0119  0.0977  175 GLN B CA  
3011 C CA  B GLN B 100 ? 0.3016 0.5583 0.7064 0.0119  0.0123  0.0974  175 GLN B CA  
3012 C C   A GLN B 100 ? 0.2704 0.4802 0.6594 0.0192  0.0054  0.0782  175 GLN B C   
3013 C C   B GLN B 100 ? 0.2790 0.4888 0.6665 0.0204  0.0063  0.0779  175 GLN B C   
3014 O O   A GLN B 100 ? 0.3428 0.5217 0.7311 0.0155  0.0019  0.0751  175 GLN B O   
3015 O O   B GLN B 100 ? 0.3449 0.5241 0.7297 0.0178  0.0038  0.0746  175 GLN B O   
3016 C CB  A GLN B 100 ? 0.2966 0.5703 0.7273 -0.0135 -0.0041 0.1102  175 GLN B CB  
3017 C CB  B GLN B 100 ? 0.2977 0.5703 0.7273 -0.0119 -0.0039 0.1086  175 GLN B CB  
3018 C CG  A GLN B 100 ? 0.3150 0.6086 0.7509 -0.0089 -0.0101 0.1053  175 GLN B CG  
3019 C CG  B GLN B 100 ? 0.4424 0.7705 0.8881 -0.0225 0.0011  0.1284  175 GLN B CG  
3020 C CD  A GLN B 100 ? 0.4743 0.8223 0.9171 0.0047  0.0031  0.1120  175 GLN B CD  
3021 C CD  B GLN B 100 ? 0.3966 0.7330 0.8612 -0.0527 -0.0200 0.1426  175 GLN B CD  
3022 O OE1 A GLN B 100 ? 0.4239 0.8130 0.8856 -0.0100 0.0051  0.1305  175 GLN B OE1 
3023 O OE1 B GLN B 100 ? 0.5817 0.9667 1.0614 -0.0626 -0.0192 0.1583  175 GLN B OE1 
3024 N NE2 A GLN B 100 ? 0.5196 0.8667 0.9471 0.0329  0.0112  0.0972  175 GLN B NE2 
3025 N NE2 B GLN B 100 ? 0.2292 0.5161 0.6918 -0.0679 -0.0401 0.1370  175 GLN B NE2 
3026 N N   . ALA B 101 ? 0.3284 0.5367 0.7061 0.0300  0.0034  0.0663  176 ALA B N   
3027 C CA  . ALA B 101 ? 0.2450 0.4168 0.6063 0.0344  -0.0015 0.0498  176 ALA B CA  
3028 C C   . ALA B 101 ? 0.2302 0.4101 0.5987 0.0332  -0.0118 0.0458  176 ALA B C   
3029 O O   . ALA B 101 ? 0.3187 0.5270 0.6890 0.0417  -0.0110 0.0511  176 ALA B O   
3030 C CB  . ALA B 101 ? 0.1517 0.3062 0.4805 0.0507  0.0074  0.0413  176 ALA B CB  
3031 N N   . TRP B 102 ? 0.2612 0.4186 0.6376 0.0241  -0.0224 0.0360  177 TRP B N   
3032 C CA  . TRP B 102 ? 0.2746 0.4378 0.6609 0.0185  -0.0368 0.0330  177 TRP B CA  
3033 C C   . TRP B 102 ? 0.2740 0.3976 0.6341 0.0159  -0.0392 0.0129  177 TRP B C   
3034 O O   . TRP B 102 ? 0.3304 0.4337 0.6811 0.0198  -0.0299 0.0035  177 TRP B O   
3035 C CB  . TRP B 102 ? 0.4089 0.5900 0.8225 -0.0038 -0.0534 0.0461  177 TRP B CB  
3036 C CG  . TRP B 102 ? 0.2846 0.4272 0.6921 -0.0222 -0.0623 0.0403  177 TRP B CG  
3037 C CD1 . TRP B 102 ? 0.3223 0.4200 0.7026 -0.0341 -0.0751 0.0247  177 TRP B CD1 
3038 C CD2 . TRP B 102 ? 0.3326 0.4687 0.7514 -0.0289 -0.0602 0.0490  177 TRP B CD2 
3039 N NE1 . TRP B 102 ? 0.3045 0.3642 0.6781 -0.0435 -0.0810 0.0212  177 TRP B NE1 
3040 C CE2 . TRP B 102 ? 0.2972 0.3793 0.6958 -0.0419 -0.0739 0.0375  177 TRP B CE2 
3041 C CE3 . TRP B 102 ? 0.3369 0.5014 0.7720 -0.0250 -0.0485 0.0650  177 TRP B CE3 
3042 C CZ2 . TRP B 102 ? 0.3730 0.4271 0.7730 -0.0500 -0.0798 0.0430  177 TRP B CZ2 
3043 C CZ3 . TRP B 102 ? 0.2961 0.4391 0.7357 -0.0379 -0.0542 0.0727  177 TRP B CZ3 
3044 C CH2 . TRP B 102 ? 0.3058 0.3918 0.7278 -0.0496 -0.0711 0.0622  177 TRP B CH2 
3045 N N   . GLU B 103 ? 0.3710 0.4861 0.7143 0.0092  -0.0509 0.0073  178 GLU B N   
3046 C CA  . GLU B 103 ? 0.3936 0.4738 0.7005 0.0039  -0.0507 -0.0118 178 GLU B CA  
3047 C C   . GLU B 103 ? 0.3555 0.4183 0.6483 -0.0155 -0.0691 -0.0155 178 GLU B C   
3048 O O   . GLU B 103 ? 0.4928 0.5759 0.7992 -0.0232 -0.0853 -0.0016 178 GLU B O   
3049 C CB  . GLU B 103 ? 0.4027 0.4799 0.6834 0.0126  -0.0467 -0.0153 178 GLU B CB  
3050 C CG  . GLU B 103 ? 0.7524 0.8438 1.0347 0.0170  -0.0605 -0.0034 178 GLU B CG  
3051 C CD  . GLU B 103 ? 0.7454 0.8192 0.9929 0.0241  -0.0612 -0.0059 178 GLU B CD  
3052 O OE1 . GLU B 103 ? 0.9112 0.9669 1.1324 0.0183  -0.0519 -0.0159 178 GLU B OE1 
3053 O OE2 . GLU B 103 ? 0.7482 0.8268 0.9949 0.0354  -0.0726 0.0035  178 GLU B OE2 
3054 N N   . GLU B 104 ? 0.3940 0.4197 0.6584 -0.0223 -0.0673 -0.0341 179 GLU B N   
3055 C CA  . GLU B 104 ? 0.3139 0.3086 0.5485 -0.0423 -0.0853 -0.0417 179 GLU B CA  
3056 C C   . GLU B 104 ? 0.5584 0.5169 0.7472 -0.0392 -0.0726 -0.0679 179 GLU B C   
3057 O O   . GLU B 104 ? 0.6421 0.5923 0.8342 -0.0241 -0.0552 -0.0799 179 GLU B O   
3058 C CB  . GLU B 104 ? 0.4808 0.4609 0.7296 -0.0579 -0.1018 -0.0339 179 GLU B CB  
3059 C CG  . GLU B 104 ? 0.6793 0.6219 0.8925 -0.0840 -0.1271 -0.0384 179 GLU B CG  
3060 C CD  . GLU B 104 ? 0.8037 0.7243 1.0250 -0.1051 -0.1481 -0.0281 179 GLU B CD  
3061 O OE1 . GLU B 104 ? 0.9245 0.8605 1.1795 -0.0988 -0.1413 -0.0174 179 GLU B OE1 
3062 O OE2 . GLU B 104 ? 1.0019 0.8858 1.1907 -0.1315 -0.1739 -0.0291 179 GLU B OE2 
3063 N N   . GLY B 105 ? 0.5080 0.4492 0.6551 -0.0525 -0.0809 -0.0757 180 GLY B N   
3064 C CA  . GLY B 105 ? 0.4429 0.3570 0.5417 -0.0504 -0.0652 -0.1006 180 GLY B CA  
3065 C C   . GLY B 105 ? 0.4118 0.3552 0.5185 -0.0332 -0.0385 -0.1047 180 GLY B C   
3066 O O   . GLY B 105 ? 0.8073 0.7445 0.8985 -0.0217 -0.0179 -0.1238 180 GLY B O   
3067 N N   . GLY B 106 ? 0.5631 0.5383 0.6927 -0.0307 -0.0395 -0.0867 181 GLY B N   
3068 C CA  . GLY B 106 ? 0.4450 0.4451 0.5793 -0.0210 -0.0200 -0.0862 181 GLY B CA  
3069 C C   . GLY B 106 ? 0.4549 0.4714 0.6284 -0.0023 -0.0053 -0.0859 181 GLY B C   
3070 O O   . GLY B 106 ? 0.6199 0.6599 0.7998 0.0037  0.0095  -0.0845 181 GLY B O   
3071 N N   . ILE B 107 ? 0.5256 0.5301 0.7243 0.0034  -0.0121 -0.0844 182 ILE B N   
3072 C CA  . ILE B 107 ? 0.3826 0.3953 0.6157 0.0194  -0.0030 -0.0823 182 ILE B CA  
3073 C C   . ILE B 107 ? 0.4156 0.4460 0.6804 0.0195  -0.0114 -0.0603 182 ILE B C   
3074 O O   . ILE B 107 ? 0.5194 0.5487 0.7901 0.0100  -0.0262 -0.0502 182 ILE B O   
3075 C CB  . ILE B 107 ? 0.5137 0.4904 0.7434 0.0248  -0.0065 -0.0961 182 ILE B CB  
3076 C CG1 . ILE B 107 ? 0.5526 0.5080 0.7418 0.0294  0.0050  -0.1219 182 ILE B CG1 
3077 C CG2 . ILE B 107 ? 0.5435 0.5248 0.8075 0.0417  -0.0010 -0.0915 182 ILE B CG2 
3078 C CD1 . ILE B 107 ? 0.4908 0.4816 0.6868 0.0461  0.0306  -0.1297 182 ILE B CD1 
3079 N N   . LEU B 108 ? 0.3574 0.4075 0.6417 0.0296  -0.0018 -0.0522 183 LEU B N   
3080 C CA  . LEU B 108 ? 0.3761 0.4406 0.6825 0.0320  -0.0058 -0.0337 183 LEU B CA  
3081 C C   . LEU B 108 ? 0.3780 0.4364 0.7102 0.0355  -0.0076 -0.0284 183 LEU B C   
3082 O O   . LEU B 108 ? 0.3970 0.4481 0.7362 0.0443  -0.0018 -0.0353 183 LEU B O   
3083 C CB  . LEU B 108 ? 0.3300 0.4087 0.6303 0.0368  0.0014  -0.0268 183 LEU B CB  
3084 C CG  . LEU B 108 ? 0.2993 0.3862 0.6120 0.0423  0.0005  -0.0110 183 LEU B CG  
3085 C CD1 . LEU B 108 ? 0.2519 0.3452 0.5638 0.0435  -0.0063 -0.0036 183 LEU B CD1 
3086 C CD2 . LEU B 108 ? 0.3014 0.3894 0.5984 0.0440  0.0043  -0.0060 183 LEU B CD2 
3087 N N   . TYR B 109 ? 0.3982 0.4628 0.7457 0.0284  -0.0164 -0.0142 184 TYR B N   
3088 C CA  . TYR B 109 ? 0.1746 0.2323 0.5421 0.0250  -0.0217 -0.0038 184 TYR B CA  
3089 C C   . TYR B 109 ? 0.2849 0.3701 0.6661 0.0269  -0.0163 0.0150  184 TYR B C   
3090 O O   . TYR B 109 ? 0.3868 0.4915 0.7569 0.0261  -0.0137 0.0222  184 TYR B O   
3091 C CB  . TYR B 109 ? 0.3743 0.4175 0.7441 0.0075  -0.0382 0.0002  184 TYR B CB  
3092 C CG  . TYR B 109 ? 0.3249 0.3275 0.6693 0.0043  -0.0458 -0.0200 184 TYR B CG  
3093 C CD1 . TYR B 109 ? 0.3511 0.3536 0.6731 0.0005  -0.0466 -0.0309 184 TYR B CD1 
3094 C CD2 . TYR B 109 ? 0.2811 0.2389 0.6175 0.0057  -0.0538 -0.0286 184 TYR B CD2 
3095 C CE1 . TYR B 109 ? 0.4555 0.4173 0.7447 -0.0032 -0.0522 -0.0509 184 TYR B CE1 
3096 C CE2 . TYR B 109 ? 0.4101 0.3228 0.7136 0.0065  -0.0594 -0.0506 184 TYR B CE2 
3097 C CZ  . TYR B 109 ? 0.5241 0.4403 0.8026 0.0011  -0.0573 -0.0621 184 TYR B CZ  
3098 O OH  . TYR B 109 ? 0.7223 0.5901 0.9588 0.0010  -0.0615 -0.0854 184 TYR B OH  
3099 N N   . LEU B 110 ? 0.2961 0.3725 0.6790 0.0286  -0.0144 0.0218  185 LEU B N   
3100 C CA  . LEU B 110 ? 0.2404 0.3300 0.6131 0.0270  -0.0085 0.0376  185 LEU B CA  
3101 C C   . LEU B 110 ? 0.2088 0.2995 0.6142 0.0166  -0.0180 0.0544  185 LEU B C   
3102 O O   . LEU B 110 ? 0.3842 0.4479 0.7945 0.0178  -0.0259 0.0531  185 LEU B O   
3103 C CB  . LEU B 110 ? 0.3064 0.3879 0.6538 0.0341  -0.0019 0.0348  185 LEU B CB  
3104 C CG  . LEU B 110 ? 0.4130 0.4944 0.7344 0.0396  0.0029  0.0232  185 LEU B CG  
3105 C CD1 . LEU B 110 ? 0.5448 0.6243 0.8528 0.0418  0.0048  0.0274  185 LEU B CD1 
3106 C CD2 . LEU B 110 ? 0.4530 0.5459 0.7644 0.0426  0.0047  0.0236  185 LEU B CD2 
3107 N N   . GLN B 111 ? 0.3136 0.4316 0.7286 0.0045  -0.0178 0.0708  186 GLN B N   
3108 C CA  . GLN B 111 ? 0.2608 0.3770 0.6868 -0.0155 -0.0278 0.0906  186 GLN B CA  
3109 C C   . GLN B 111 ? 0.4587 0.5950 0.8779 -0.0147 -0.0163 0.1061  186 GLN B C   
3110 O O   . GLN B 111 ? 0.4303 0.6050 0.8451 -0.0091 -0.0010 0.1116  186 GLN B O   
3111 C CB  . GLN B 111 ? 0.2657 0.4083 0.7074 -0.0360 -0.0356 0.1032  186 GLN B CB  
3112 C CG  . GLN B 111 ? 0.3392 0.4840 0.7885 -0.0641 -0.0473 0.1285  186 GLN B CG  
3113 C CD  . GLN B 111 ? 0.3009 0.4784 0.7535 -0.0847 -0.0536 0.1426  186 GLN B CD  
3114 O OE1 . GLN B 111 ? 0.4222 0.6236 0.8764 -0.0761 -0.0490 0.1342  186 GLN B OE1 
3115 N NE2 . GLN B 111 ? 0.4663 0.6435 0.9148 -0.1126 -0.0659 0.1650  186 GLN B NE2 
3116 N N   . THR B 112 ? 0.3563 0.4631 0.7689 -0.0182 -0.0244 0.1124  187 THR B N   
3117 C CA  . THR B 112 ? 0.4915 0.6076 0.8888 -0.0213 -0.0172 0.1277  187 THR B CA  
3118 C C   . THR B 112 ? 0.3951 0.5000 0.7947 -0.0471 -0.0315 0.1512  187 THR B C   
3119 O O   . THR B 112 ? 0.4802 0.5606 0.8912 -0.0612 -0.0501 0.1546  187 THR B O   
3120 C CB  . THR B 112 ? 0.3016 0.3930 0.6846 -0.0066 -0.0183 0.1193  187 THR B CB  
3121 O OG1 . THR B 112 ? 0.5084 0.5640 0.9044 -0.0072 -0.0372 0.1186  187 THR B OG1 
3122 C CG2 . THR B 112 ? 0.3190 0.4160 0.6960 0.0125  -0.0084 0.0986  187 THR B CG2 
3123 N N   . GLU B 113 ? 0.3644 0.4808 0.7453 -0.0552 -0.0245 0.1681  188 GLU B N   
3124 C CA  . GLU B 113 ? 0.3029 0.4031 0.6782 -0.0827 -0.0404 0.1933  188 GLU B CA  
3125 C C   . GLU B 113 ? 0.5081 0.5483 0.8860 -0.0793 -0.0667 0.1906  188 GLU B C   
3126 O O   . GLU B 113 ? 0.6427 0.6669 1.0229 -0.0556 -0.0668 0.1737  188 GLU B O   
3127 C CB  . GLU B 113 ? 0.4244 0.5451 0.7701 -0.0906 -0.0264 0.2099  188 GLU B CB  
3128 C CG  . GLU B 113 ? 0.5911 0.6899 0.9119 -0.0703 -0.0225 0.1981  188 GLU B CG  
3129 C CD  . GLU B 113 ? 0.7525 0.8536 1.0323 -0.0827 -0.0153 0.2154  188 GLU B CD  
3130 O OE1 . GLU B 113 ? 0.6629 0.7727 0.9356 -0.1100 -0.0193 0.2395  188 GLU B OE1 
3131 O OE2 . GLU B 113 ? 0.7787 0.8695 1.0274 -0.0683 -0.0072 0.2058  188 GLU B OE2 
3132 N N   . LEU B 114 ? 0.5774 0.6484 0.8880 -0.0862 -0.1062 0.0036  189 LEU B N   
3133 C CA  . LEU B 114 ? 0.4402 0.4680 0.6860 -0.0870 -0.1046 -0.0009 189 LEU B CA  
3134 C C   . LEU B 114 ? 0.3483 0.3679 0.5678 -0.0817 -0.0674 0.0073  189 LEU B C   
3135 O O   . LEU B 114 ? 0.5453 0.5739 0.7965 -0.0926 -0.0436 0.0152  189 LEU B O   
3136 C CB  . LEU B 114 ? 0.6322 0.6414 0.8954 -0.1075 -0.1201 -0.0060 189 LEU B CB  
3137 C CG  . LEU B 114 ? 0.6161 0.5765 0.8156 -0.1068 -0.1200 -0.0120 189 LEU B CG  
3138 C CD1 . LEU B 114 ? 0.5936 0.5309 0.7356 -0.0935 -0.1446 -0.0243 189 LEU B CD1 
3139 C CD2 . LEU B 114 ? 0.6960 0.6356 0.9192 -0.1292 -0.1271 -0.0143 189 LEU B CD2 
3140 N N   . CYS B 115 ? 0.6598 0.6621 0.8214 -0.0657 -0.0627 0.0058  190 CYS B N   
3141 C CA  . CYS B 115 ? 0.5085 0.4973 0.6370 -0.0602 -0.0355 0.0122  190 CYS B CA  
3142 C C   . CYS B 115 ? 0.5928 0.5426 0.6767 -0.0602 -0.0414 0.0081  190 CYS B C   
3143 O O   . CYS B 115 ? 0.8108 0.7426 0.8845 -0.0633 -0.0639 -0.0014 190 CYS B O   
3144 C CB  . CYS B 115 ? 0.6283 0.6274 0.7320 -0.0429 -0.0265 0.0135  190 CYS B CB  
3145 S SG  . CYS B 115 ? 0.7560 0.7949 0.9097 -0.0386 -0.0223 0.0162  190 CYS B SG  
3146 N N   . GLY B 116 ? 0.5696 0.5034 0.6248 -0.0558 -0.0224 0.0148  191 GLY B N   
3147 C CA  . GLY B 116 ? 0.7450 0.6424 0.7625 -0.0524 -0.0270 0.0121  191 GLY B CA  
3148 C C   . GLY B 116 ? 0.5837 0.4742 0.5633 -0.0348 -0.0359 0.0034  191 GLY B C   
3149 O O   . GLY B 116 ? 0.5871 0.4950 0.5668 -0.0287 -0.0444 -0.0019 191 GLY B O   
3150 N N   . PRO B 117 ? 0.6213 0.4857 0.5694 -0.0261 -0.0331 0.0028  192 PRO B N   
3151 C CA  . PRO B 117 ? 0.5602 0.4211 0.4781 -0.0092 -0.0364 -0.0051 192 PRO B CA  
3152 C C   . PRO B 117 ? 0.5761 0.4632 0.4912 0.0000  -0.0252 0.0006  192 PRO B C   
3153 O O   . PRO B 117 ? 0.6367 0.5368 0.5635 -0.0040 -0.0137 0.0102  192 PRO B O   
3154 C CB  . PRO B 117 ? 0.4653 0.2945 0.3629 -0.0023 -0.0344 -0.0053 192 PRO B CB  
3155 C CG  . PRO B 117 ? 0.6174 0.4395 0.5262 -0.0125 -0.0251 0.0087  192 PRO B CG  
3156 C CD  . PRO B 117 ? 0.7327 0.5695 0.6737 -0.0307 -0.0258 0.0106  192 PRO B CD  
3157 N N   . SER B 118 ? 0.5616 0.4534 0.4586 0.0116  -0.0275 -0.0060 193 SER B N   
3158 C CA  . SER B 118 ? 0.4425 0.3558 0.3375 0.0191  -0.0182 -0.0013 193 SER B CA  
3159 C C   . SER B 118 ? 0.4274 0.3353 0.3143 0.0259  -0.0101 0.0044  193 SER B C   
3160 O O   . SER B 118 ? 0.6184 0.5049 0.4976 0.0292  -0.0123 0.0037  193 SER B O   
3161 C CB  . SER B 118 ? 0.4099 0.3281 0.2885 0.0276  -0.0209 -0.0082 193 SER B CB  
3162 O OG  . SER B 118 ? 0.6091 0.5125 0.4691 0.0377  -0.0180 -0.0144 193 SER B OG  
3163 N N   . LEU B 119 ? 0.5500 0.4753 0.4385 0.0282  -0.0029 0.0099  194 LEU B N   
3164 C CA  . LEU B 119 ? 0.4921 0.4138 0.3721 0.0346  -0.0003 0.0150  194 LEU B CA  
3165 C C   . LEU B 119 ? 0.5127 0.4322 0.3886 0.0473  -0.0031 0.0092  194 LEU B C   
3166 O O   . LEU B 119 ? 0.5879 0.4985 0.4620 0.0545  -0.0058 0.0125  194 LEU B O   
3167 C CB  . LEU B 119 ? 0.4768 0.4157 0.3572 0.0333  0.0056  0.0192  194 LEU B CB  
3168 C CG  . LEU B 119 ? 0.4990 0.4341 0.3684 0.0372  0.0041  0.0249  194 LEU B CG  
3169 C CD1 . LEU B 119 ? 0.5548 0.4670 0.4108 0.0325  0.0041  0.0332  194 LEU B CD1 
3170 C CD2 . LEU B 119 ? 0.4483 0.3972 0.3155 0.0346  0.0085  0.0254  194 LEU B CD2 
3171 N N   . GLN B 120 ? 0.4761 0.4030 0.3505 0.0509  -0.0017 0.0012  195 GLN B N   
3172 C CA  . GLN B 120 ? 0.4092 0.3340 0.2806 0.0631  0.0012  -0.0057 195 GLN B CA  
3173 C C   . GLN B 120 ? 0.5511 0.4487 0.4163 0.0681  -0.0028 -0.0113 195 GLN B C   
3174 O O   . GLN B 120 ? 0.7226 0.6149 0.5935 0.0802  -0.0014 -0.0127 195 GLN B O   
3175 C CB  . GLN B 120 ? 0.4132 0.3459 0.2750 0.0639  0.0065  -0.0122 195 GLN B CB  
3176 C CG  . GLN B 120 ? 0.4891 0.4212 0.3467 0.0759  0.0161  -0.0199 195 GLN B CG  
3177 C CD  . GLN B 120 ? 0.5825 0.5156 0.4198 0.0749  0.0231  -0.0247 195 GLN B CD  
3178 O OE1 . GLN B 120 ? 0.6501 0.5733 0.4701 0.0673  0.0148  -0.0258 195 GLN B OE1 
3179 N NE2 . GLN B 120 ? 0.7342 0.6792 0.5744 0.0821  0.0381  -0.0266 195 GLN B NE2 
3180 N N   . GLN B 121 ? 0.6541 0.5337 0.5111 0.0593  -0.0090 -0.0148 196 GLN B N   
3181 C CA  . GLN B 121 ? 0.4864 0.3343 0.3360 0.0621  -0.0140 -0.0213 196 GLN B CA  
3182 C C   . GLN B 121 ? 0.5087 0.3425 0.3658 0.0626  -0.0168 -0.0108 196 GLN B C   
3183 O O   . GLN B 121 ? 0.7558 0.5666 0.6109 0.0730  -0.0188 -0.0137 196 GLN B O   
3184 C CB  . GLN B 121 ? 0.4901 0.3226 0.3326 0.0492  -0.0232 -0.0274 196 GLN B CB  
3185 C CG  . GLN B 121 ? 0.5801 0.4169 0.4052 0.0495  -0.0253 -0.0378 196 GLN B CG  
3186 C CD  . GLN B 121 ? 0.6098 0.4327 0.4313 0.0357  -0.0407 -0.0433 196 GLN B CD  
3187 O OE1 . GLN B 121 ? 0.8381 0.6671 0.6827 0.0227  -0.0465 -0.0356 196 GLN B OE1 
3188 N NE2 . GLN B 121 ? 0.9536 0.7576 0.7463 0.0380  -0.0474 -0.0570 196 GLN B NE2 
3189 N N   . HIS B 122 ? 0.5816 0.4254 0.4445 0.0523  -0.0164 0.0016  197 HIS B N   
3190 C CA  . HIS B 122 ? 0.5839 0.4097 0.4441 0.0517  -0.0188 0.0138  197 HIS B CA  
3191 C C   . HIS B 122 ? 0.5792 0.4092 0.4411 0.0679  -0.0215 0.0171  197 HIS B C   
3192 O O   . HIS B 122 ? 0.7394 0.5447 0.5978 0.0750  -0.0281 0.0231  197 HIS B O   
3193 C CB  . HIS B 122 ? 0.5552 0.3903 0.4149 0.0374  -0.0136 0.0252  197 HIS B CB  
3194 C CG  . HIS B 122 ? 0.7231 0.5375 0.5690 0.0361  -0.0145 0.0395  197 HIS B CG  
3195 N ND1 . HIS B 122 ? 0.9122 0.6908 0.7505 0.0370  -0.0199 0.0446  197 HIS B ND1 
3196 C CD2 . HIS B 122 ? 0.7098 0.5290 0.5424 0.0339  -0.0115 0.0500  197 HIS B CD2 
3197 C CE1 . HIS B 122 ? 0.8018 0.5642 0.6216 0.0354  -0.0206 0.0598  197 HIS B CE1 
3198 N NE2 . HIS B 122 ? 0.7813 0.5677 0.5950 0.0334  -0.0157 0.0626  197 HIS B NE2 
3199 N N   . CYS B 123 ? 0.5764 0.4369 0.4469 0.0737  -0.0181 0.0142  198 CYS B N   
3200 C CA  . CYS B 123 ? 0.6306 0.5009 0.5127 0.0881  -0.0227 0.0167  198 CYS B CA  
3201 C C   . CYS B 123 ? 0.5803 0.4426 0.4742 0.1044  -0.0208 0.0063  198 CYS B C   
3202 O O   . CYS B 123 ? 0.7563 0.6099 0.6619 0.1181  -0.0282 0.0099  198 CYS B O   
3203 C CB  . CYS B 123 ? 0.6069 0.5119 0.4994 0.0868  -0.0189 0.0162  198 CYS B CB  
3204 S SG  . CYS B 123 ? 0.7859 0.6955 0.6627 0.0714  -0.0202 0.0264  198 CYS B SG  
3205 N N   . GLU B 124 ? 0.5792 0.4425 0.4685 0.1042  -0.0113 -0.0067 199 GLU B N   
3206 C CA  . GLU B 124 ? 0.4877 0.3373 0.3808 0.1197  -0.0055 -0.0193 199 GLU B CA  
3207 C C   . GLU B 124 ? 0.5628 0.3723 0.4504 0.1247  -0.0144 -0.0184 199 GLU B C   
3208 O O   . GLU B 124 ? 0.7316 0.5305 0.6333 0.1430  -0.0143 -0.0222 199 GLU B O   
3209 C CB  . GLU B 124 ? 0.6188 0.4664 0.4929 0.1153  0.0044  -0.0332 199 GLU B CB  
3210 C CG  . GLU B 124 ? 1.0229 0.8509 0.8903 0.1305  0.0143  -0.0494 199 GLU B CG  
3211 C CD  . GLU B 124 ? 1.3091 1.1329 1.1469 0.1253  0.0234  -0.0623 199 GLU B CD  
3212 O OE1 . GLU B 124 ? 1.3323 1.1802 1.1658 0.1154  0.0257  -0.0572 199 GLU B OE1 
3213 O OE2 . GLU B 124 ? 1.0942 0.8866 0.9093 0.1314  0.0269  -0.0775 199 GLU B OE2 
3214 N N   . ALA B 125 ? 0.8392 0.6258 0.7103 0.1089  -0.0214 -0.0128 200 ALA B N   
3215 C CA  . ALA B 125 ? 0.6772 0.4212 0.5421 0.1106  -0.0296 -0.0096 200 ALA B CA  
3216 C C   . ALA B 125 ? 0.7624 0.5001 0.6338 0.1173  -0.0392 0.0078  200 ALA B C   
3217 O O   . ALA B 125 ? 0.6772 0.3825 0.5504 0.1292  -0.0464 0.0103  200 ALA B O   
3218 C CB  . ALA B 125 ? 0.7859 0.5094 0.6365 0.0888  -0.0328 -0.0080 200 ALA B CB  
3219 N N   . TRP B 126 ? 0.6482 0.4120 0.5197 0.1102  -0.0412 0.0200  201 TRP B N   
3220 C CA  . TRP B 126 ? 0.6732 0.4281 0.5426 0.1161  -0.0538 0.0366  201 TRP B CA  
3221 C C   . TRP B 126 ? 0.5882 0.3558 0.4849 0.1399  -0.0608 0.0337  201 TRP B C   
3222 O O   . TRP B 126 ? 0.6845 0.4315 0.5832 0.1512  -0.0758 0.0451  201 TRP B O   
3223 C CB  . TRP B 126 ? 0.5918 0.3682 0.4487 0.1025  -0.0540 0.0472  201 TRP B CB  
3224 C CG  . TRP B 126 ? 0.6363 0.3947 0.4764 0.1048  -0.0686 0.0651  201 TRP B CG  
3225 C CD1 . TRP B 126 ? 0.7612 0.5384 0.6071 0.1133  -0.0815 0.0706  201 TRP B CD1 
3226 C CD2 . TRP B 126 ? 0.6879 0.4024 0.4991 0.0975  -0.0734 0.0806  201 TRP B CD2 
3227 N NE1 . TRP B 126 ? 0.8086 0.5546 0.6258 0.1128  -0.0965 0.0884  201 TRP B NE1 
3228 C CE2 . TRP B 126 ? 0.7253 0.4315 0.5190 0.1033  -0.0900 0.0957  201 TRP B CE2 
3229 C CE3 . TRP B 126 ? 0.6614 0.3415 0.4596 0.0853  -0.0660 0.0837  201 TRP B CE3 
3230 C CZ2 . TRP B 126 ? 0.8120 0.4735 0.5688 0.0980  -0.0977 0.1150  201 TRP B CZ2 
3231 C CZ3 . TRP B 126 ? 0.7036 0.3417 0.4717 0.0789  -0.0712 0.1030  201 TRP B CZ3 
3232 C CH2 . TRP B 126 ? 0.7968 0.4243 0.5411 0.0857  -0.0861 0.1191  201 TRP B CH2 
3233 N N   . GLY B 127 ? 0.6204 0.4214 0.5402 0.1478  -0.0500 0.0197  202 GLY B N   
3234 C CA  . GLY B 127 ? 0.5924 0.4096 0.5482 0.1707  -0.0517 0.0148  202 GLY B CA  
3235 C C   . GLY B 127 ? 0.5609 0.3978 0.5358 0.1770  -0.0698 0.0284  202 GLY B C   
3236 O O   . GLY B 127 ? 0.6842 0.5250 0.6922 0.1976  -0.0791 0.0293  202 GLY B O   
3237 N N   . ALA B 128 ? 0.5837 0.4322 0.5393 0.1603  -0.0762 0.0382  203 ALA B N   
3238 C CA  . ALA B 128 ? 0.7305 0.5925 0.6944 0.1633  -0.0972 0.0504  203 ALA B CA  
3239 C C   . ALA B 128 ? 0.7106 0.5854 0.6473 0.1423  -0.0954 0.0543  203 ALA B C   
3240 O O   . ALA B 128 ? 0.6132 0.4902 0.5330 0.1282  -0.0777 0.0480  203 ALA B O   
3241 C CB  . ALA B 128 ? 0.7640 0.5855 0.7105 0.1716  -0.1194 0.0663  203 ALA B CB  
3242 N N   . SER B 129 ? 0.7177 0.5995 0.6507 0.1413  -0.1154 0.0638  204 SER B N   
3243 C CA  . SER B 129 ? 0.5996 0.4852 0.5003 0.1228  -0.1147 0.0669  204 SER B CA  
3244 C C   . SER B 129 ? 0.6464 0.4924 0.4961 0.1098  -0.1079 0.0757  204 SER B C   
3245 O O   . SER B 129 ? 0.8632 0.6732 0.6918 0.1144  -0.1187 0.0877  204 SER B O   
3246 C CB  . SER B 129 ? 0.6630 0.5570 0.5642 0.1246  -0.1414 0.0743  204 SER B CB  
3247 O OG  . SER B 129 ? 0.8985 0.8321 0.8577 0.1362  -0.1485 0.0672  204 SER B OG  
3248 N N   . LEU B 130 ? 0.6334 0.4858 0.4665 0.0939  -0.0892 0.0707  205 LEU B N   
3249 C CA  . LEU B 130 ? 0.7320 0.5533 0.5251 0.0803  -0.0788 0.0787  205 LEU B CA  
3250 C C   . LEU B 130 ? 0.9161 0.7117 0.6648 0.0757  -0.0923 0.0927  205 LEU B C   
3251 O O   . LEU B 130 ? 0.8746 0.6842 0.6187 0.0762  -0.1052 0.0915  205 LEU B O   
3252 C CB  . LEU B 130 ? 0.6309 0.4697 0.4241 0.0662  -0.0571 0.0699  205 LEU B CB  
3253 C CG  . LEU B 130 ? 0.7219 0.5722 0.5419 0.0665  -0.0438 0.0590  205 LEU B CG  
3254 C CD1 . LEU B 130 ? 0.6913 0.5530 0.5082 0.0523  -0.0269 0.0544  205 LEU B CD1 
3255 C CD2 . LEU B 130 ? 0.7547 0.5738 0.5720 0.0695  -0.0454 0.0630  205 LEU B CD2 
3256 N N   . PRO B 131 ? 0.9360 0.6911 0.6484 0.0701  -0.0902 0.1062  206 PRO B N   
3257 C CA  . PRO B 131 ? 0.8544 0.5823 0.5153 0.0630  -0.0980 0.1190  206 PRO B CA  
3258 C C   . PRO B 131 ? 0.8347 0.5773 0.4754 0.0497  -0.0832 0.1117  206 PRO B C   
3259 O O   . PRO B 131 ? 0.9154 0.6716 0.5664 0.0412  -0.0599 0.1040  206 PRO B O   
3260 C CB  . PRO B 131 ? 0.9631 0.6541 0.6012 0.0543  -0.0856 0.1311  206 PRO B CB  
3261 C CG  . PRO B 131 ? 0.9090 0.5919 0.5787 0.0652  -0.0882 0.1298  206 PRO B CG  
3262 C CD  . PRO B 131 ? 0.8260 0.5571 0.5432 0.0685  -0.0798 0.1096  206 PRO B CD  
3263 N N   . GLU B 132 ? 0.8385 0.5830 0.4595 0.0476  -0.0964 0.1112  207 GLU B N   
3264 C CA  . GLU B 132 ? 0.7406 0.4986 0.3464 0.0378  -0.0855 0.1009  207 GLU B CA  
3265 C C   . GLU B 132 ? 0.7599 0.5043 0.3396 0.0238  -0.0538 0.1014  207 GLU B C   
3266 O O   . GLU B 132 ? 0.8793 0.6392 0.4620 0.0177  -0.0365 0.0910  207 GLU B O   
3267 C CB  . GLU B 132 ? 0.7589 0.5135 0.3436 0.0377  -0.1077 0.1001  207 GLU B CB  
3268 C CG  . GLU B 132 ? 0.9674 0.7338 0.5400 0.0294  -0.1007 0.0870  207 GLU B CG  
3269 C CD  . GLU B 132 ? 1.1292 0.8976 0.6936 0.0307  -0.1295 0.0835  207 GLU B CD  
3270 O OE1 . GLU B 132 ? 1.0485 0.8310 0.6446 0.0408  -0.1564 0.0866  207 GLU B OE1 
3271 O OE2 . GLU B 132 ? 1.2856 1.0417 0.8146 0.0220  -0.1252 0.0769  207 GLU B OE2 
3272 N N   . ALA B 133 ? 0.9351 0.6518 0.4937 0.0188  -0.0451 0.1135  208 ALA B N   
3273 C CA  . ALA B 133 ? 0.8466 0.5541 0.3891 0.0052  -0.0131 0.1148  208 ALA B CA  
3274 C C   . ALA B 133 ? 0.7868 0.5150 0.3643 0.0020  0.0072  0.1081  208 ALA B C   
3275 O O   . ALA B 133 ? 1.0116 0.7514 0.5913 -0.0061 0.0313  0.1011  208 ALA B O   
3276 C CB  . ALA B 133 ? 0.9519 0.6262 0.4714 -0.0001 -0.0082 0.1307  208 ALA B CB  
3277 N N   . GLN B 134 ? 0.8746 0.6067 0.4804 0.0095  -0.0026 0.1096  209 GLN B N   
3278 C CA  . GLN B 134 ? 0.7672 0.5294 0.4205 0.0068  0.0125  0.0986  209 GLN B CA  
3279 C C   . GLN B 134 ? 0.7756 0.5724 0.4487 0.0100  0.0135  0.0835  209 GLN B C   
3280 O O   . GLN B 134 ? 0.8993 0.7170 0.5966 0.0044  0.0317  0.0756  209 GLN B O   
3281 C CB  . GLN B 134 ? 0.8155 0.5832 0.5064 0.0151  -0.0004 0.0965  209 GLN B CB  
3282 C CG  . GLN B 134 ? 0.8624 0.5955 0.5441 0.0103  0.0013  0.1091  209 GLN B CG  
3283 C CD  . GLN B 134 ? 0.9897 0.7289 0.7112 0.0168  -0.0065 0.1016  209 GLN B CD  
3284 O OE1 . GLN B 134 ? 1.4014 1.1141 1.1187 0.0245  -0.0200 0.1082  209 GLN B OE1 
3285 N NE2 . GLN B 134 ? 0.9369 0.7075 0.6939 0.0145  0.0013  0.0875  209 GLN B NE2 
3286 N N   . VAL B 135 ? 0.7103 0.5131 0.3767 0.0186  -0.0072 0.0802  210 VAL B N   
3287 C CA  . VAL B 135 ? 0.6352 0.4685 0.3238 0.0208  -0.0080 0.0666  210 VAL B CA  
3288 C C   . VAL B 135 ? 0.6859 0.5150 0.3500 0.0120  0.0113  0.0618  210 VAL B C   
3289 O O   . VAL B 135 ? 0.8062 0.6583 0.4969 0.0109  0.0228  0.0516  210 VAL B O   
3290 C CB  . VAL B 135 ? 0.7698 0.6095 0.4597 0.0295  -0.0349 0.0651  210 VAL B CB  
3291 C CG1 . VAL B 135 ? 0.7994 0.6684 0.5148 0.0293  -0.0345 0.0522  210 VAL B CG1 
3292 C CG2 . VAL B 135 ? 0.6846 0.5291 0.4039 0.0407  -0.0502 0.0690  210 VAL B CG2 
3293 N N   . TRP B 136 ? 0.7167 0.5160 0.3320 0.0064  0.0158  0.0685  211 TRP B N   
3294 C CA  . TRP B 136 ? 0.8022 0.6011 0.4036 -0.0006 0.0364  0.0604  211 TRP B CA  
3295 C C   . TRP B 136 ? 0.8061 0.6159 0.4318 -0.0060 0.0669  0.0592  211 TRP B C   
3296 O O   . TRP B 136 ? 0.8923 0.7156 0.5305 -0.0067 0.0828  0.0487  211 TRP B O   
3297 C CB  . TRP B 136 ? 0.7941 0.5655 0.3515 -0.0052 0.0354  0.0657  211 TRP B CB  
3298 C CG  . TRP B 136 ? 0.8480 0.6107 0.3821 -0.0011 0.0059  0.0639  211 TRP B CG  
3299 C CD1 . TRP B 136 ? 0.7854 0.5326 0.3036 0.0027  -0.0189 0.0743  211 TRP B CD1 
3300 C CD2 . TRP B 136 ? 0.8277 0.5962 0.3550 -0.0009 -0.0032 0.0510  211 TRP B CD2 
3301 N NE1 . TRP B 136 ? 0.8587 0.6049 0.3634 0.0051  -0.0438 0.0687  211 TRP B NE1 
3302 C CE2 . TRP B 136 ? 0.8658 0.6237 0.3744 0.0019  -0.0347 0.0542  211 TRP B CE2 
3303 C CE3 . TRP B 136 ? 0.8698 0.6496 0.4064 -0.0027 0.0113  0.0371  211 TRP B CE3 
3304 C CZ2 . TRP B 136 ? 0.9010 0.6597 0.3998 0.0009  -0.0526 0.0436  211 TRP B CZ2 
3305 C CZ3 . TRP B 136 ? 0.9210 0.6979 0.4443 -0.0033 -0.0052 0.0266  211 TRP B CZ3 
3306 C CH2 . TRP B 136 ? 0.8677 0.6344 0.3723 -0.0024 -0.0372 0.0297  211 TRP B CH2 
3307 N N   . GLY B 137 ? 0.6734 0.4765 0.3091 -0.0099 0.0746  0.0699  212 GLY B N   
3308 C CA  . GLY B 137 ? 0.6034 0.4227 0.2752 -0.0165 0.1004  0.0685  212 GLY B CA  
3309 C C   . GLY B 137 ? 0.5629 0.4197 0.2908 -0.0106 0.0940  0.0570  212 GLY B C   
3310 O O   . GLY B 137 ? 0.8588 0.7346 0.6144 -0.0121 0.1112  0.0501  212 GLY B O   
3311 N N   . TYR B 138 ? 0.6024 0.4687 0.3466 -0.0032 0.0698  0.0552  213 TYR B N   
3312 C CA  . TYR B 138 ? 0.5836 0.4800 0.3708 0.0020  0.0637  0.0456  213 TYR B CA  
3313 C C   . TYR B 138 ? 0.6379 0.5447 0.4220 0.0060  0.0641  0.0365  213 TYR B C   
3314 O O   . TYR B 138 ? 0.7278 0.6546 0.5425 0.0078  0.0691  0.0300  213 TYR B O   
3315 C CB  . TYR B 138 ? 0.5776 0.4780 0.3776 0.0090  0.0425  0.0457  213 TYR B CB  
3316 C CG  . TYR B 138 ? 0.6266 0.5119 0.4302 0.0060  0.0401  0.0528  213 TYR B CG  
3317 C CD1 . TYR B 138 ? 0.6521 0.5335 0.4676 -0.0046 0.0554  0.0568  213 TYR B CD1 
3318 C CD2 . TYR B 138 ? 0.6481 0.5225 0.4473 0.0136  0.0232  0.0552  213 TYR B CD2 
3319 C CE1 . TYR B 138 ? 0.6987 0.5625 0.5181 -0.0096 0.0525  0.0632  213 TYR B CE1 
3320 C CE2 . TYR B 138 ? 0.6916 0.5463 0.4926 0.0113  0.0206  0.0609  213 TYR B CE2 
3321 C CZ  . TYR B 138 ? 0.7573 0.6051 0.5667 -0.0014 0.0347  0.0650  213 TYR B CZ  
3322 O OH  . TYR B 138 ? 0.7829 0.6078 0.5951 -0.0059 0.0316  0.0705  213 TYR B OH  
3323 N N   . LEU B 139 ? 0.6155 0.5060 0.3622 0.0071  0.0567  0.0362  214 LEU B N   
3324 C CA  . LEU B 139 ? 0.5897 0.4846 0.3309 0.0089  0.0564  0.0265  214 LEU B CA  
3325 C C   . LEU B 139 ? 0.6761 0.5674 0.4137 0.0058  0.0820  0.0212  214 LEU B C   
3326 O O   . LEU B 139 ? 0.7974 0.7021 0.5582 0.0089  0.0871  0.0129  214 LEU B O   
3327 C CB  . LEU B 139 ? 0.7837 0.6594 0.4846 0.0089  0.0391  0.0266  214 LEU B CB  
3328 C CG  . LEU B 139 ? 0.6286 0.4996 0.3140 0.0079  0.0370  0.0155  214 LEU B CG  
3329 C CD1 . LEU B 139 ? 0.5536 0.4507 0.2823 0.0110  0.0307  0.0092  214 LEU B CD1 
3330 C CD2 . LEU B 139 ? 0.7287 0.5785 0.3725 0.0062  0.0148  0.0164  214 LEU B CD2 
3331 N N   . ARG B 140 ? 0.6133 0.4851 0.3229 0.0003  0.1000  0.0265  215 ARG B N   
3332 C CA  . ARG B 140 ? 0.5872 0.4560 0.2948 -0.0016 0.1292  0.0205  215 ARG B CA  
3333 C C   . ARG B 140 ? 0.6330 0.5328 0.4031 0.0003  0.1411  0.0187  215 ARG B C   
3334 O O   . ARG B 140 ? 0.7627 0.6733 0.5547 0.0053  0.1516  0.0096  215 ARG B O   
3335 C CB  . ARG B 140 ? 0.5205 0.3703 0.2010 -0.0087 0.1419  0.0268  215 ARG B CB  
3336 C CG  . ARG B 140 ? 0.7935 0.6476 0.4872 -0.0098 0.1716  0.0203  215 ARG B CG  
3337 C CD  . ARG B 140 ? 0.8656 0.6966 0.5227 -0.0165 0.1852  0.0254  215 ARG B CD  
3338 N NE  . ARG B 140 ? 1.1387 0.9699 0.7997 -0.0151 0.2117  0.0158  215 ARG B NE  
3339 C CZ  . ARG B 140 ? 1.1379 0.9894 0.8438 -0.0161 0.2383  0.0156  215 ARG B CZ  
3340 N NH1 . ARG B 140 ? 1.1977 1.0706 0.9481 -0.0207 0.2419  0.0245  215 ARG B NH1 
3341 N NH2 . ARG B 140 ? 1.1112 0.9616 0.8200 -0.0126 0.2613  0.0058  215 ARG B NH2 
3342 N N   . ASP B 141 ? 0.6333 0.5456 0.4335 -0.0034 0.1371  0.0271  216 ASP B N   
3343 C CA  . ASP B 141 ? 0.7131 0.6541 0.5730 -0.0031 0.1441  0.0257  216 ASP B CA  
3344 C C   . ASP B 141 ? 0.6001 0.5605 0.4890 0.0056  0.1264  0.0189  216 ASP B C   
3345 O O   . ASP B 141 ? 0.7176 0.6964 0.6456 0.0097  0.1338  0.0146  216 ASP B O   
3346 C CB  . ASP B 141 ? 0.6494 0.5946 0.5304 -0.0108 0.1385  0.0348  216 ASP B CB  
3347 C CG  . ASP B 141 ? 0.9543 0.8861 0.8252 -0.0217 0.1641  0.0429  216 ASP B CG  
3348 O OD1 . ASP B 141 ? 1.2164 1.1388 1.0660 -0.0223 0.1893  0.0406  216 ASP B OD1 
3349 O OD2 . ASP B 141 ? 1.1056 1.0336 0.9878 -0.0301 0.1605  0.0513  216 ASP B OD2 
3350 N N   . THR B 142 ? 0.5693 0.5253 0.4412 0.0088  0.1038  0.0188  217 THR B N   
3351 C CA  . THR B 142 ? 0.5203 0.4900 0.4123 0.0156  0.0904  0.0139  217 THR B CA  
3352 C C   . THR B 142 ? 0.6849 0.6485 0.5683 0.0198  0.0990  0.0061  217 THR B C   
3353 O O   . THR B 142 ? 0.6263 0.6008 0.5364 0.0254  0.0967  0.0029  217 THR B O   
3354 C CB  . THR B 142 ? 0.5514 0.5190 0.4296 0.0172  0.0694  0.0156  217 THR B CB  
3355 O OG1 . THR B 142 ? 0.6154 0.5825 0.4975 0.0145  0.0628  0.0213  217 THR B OG1 
3356 C CG2 . THR B 142 ? 0.4413 0.4220 0.3399 0.0223  0.0590  0.0129  217 THR B CG2 
3357 N N   . LEU B 143 ? 0.5585 0.5006 0.4014 0.0174  0.1075  0.0027  218 LEU B N   
3358 C CA  . LEU B 143 ? 0.4359 0.3661 0.2666 0.0208  0.1178  -0.0073 218 LEU B CA  
3359 C C   . LEU B 143 ? 0.5529 0.4916 0.4140 0.0251  0.1425  -0.0110 218 LEU B C   
3360 O O   . LEU B 143 ? 0.6485 0.5879 0.5268 0.0323  0.1472  -0.0184 218 LEU B O   
3361 C CB  . LEU B 143 ? 0.5405 0.4411 0.3135 0.0163  0.1195  -0.0112 218 LEU B CB  
3362 C CG  . LEU B 143 ? 0.5513 0.4437 0.3007 0.0140  0.0931  -0.0115 218 LEU B CG  
3363 C CD1 . LEU B 143 ? 0.5240 0.3857 0.2142 0.0090  0.0909  -0.0139 218 LEU B CD1 
3364 C CD2 . LEU B 143 ? 0.4500 0.3460 0.2164 0.0166  0.0846  -0.0193 218 LEU B CD2 
3365 N N   . LEU B 144 ? 0.4979 0.4434 0.3703 0.0208  0.1591  -0.0056 219 LEU B N   
3366 C CA  . LEU B 144 ? 0.5213 0.4827 0.4367 0.0248  0.1834  -0.0084 219 LEU B CA  
3367 C C   . LEU B 144 ? 0.4933 0.4824 0.4681 0.0319  0.1687  -0.0072 219 LEU B C   
3368 O O   . LEU B 144 ? 0.6549 0.6541 0.6655 0.0409  0.1802  -0.0126 219 LEU B O   
3369 C CB  . LEU B 144 ? 0.5359 0.5019 0.4583 0.0157  0.2029  -0.0007 219 LEU B CB  
3370 C CG  . LEU B 144 ? 0.5710 0.5078 0.4368 0.0088  0.2204  -0.0005 219 LEU B CG  
3371 C CD1 . LEU B 144 ? 0.6300 0.5720 0.5086 -0.0020 0.2338  0.0102  219 LEU B CD1 
3372 C CD2 . LEU B 144 ? 0.6325 0.5603 0.4920 0.0146  0.2372  -0.0122 219 LEU B CD2 
3373 N N   . ALA B 145 ? 0.5359 0.5352 0.5195 0.0292  0.1428  -0.0002 220 ALA B N   
3374 C CA  . ALA B 145 ? 0.4862 0.5053 0.5132 0.0354  0.1249  0.0017  220 ALA B CA  
3375 C C   . ALA B 145 ? 0.5481 0.5568 0.5654 0.0439  0.1163  -0.0028 220 ALA B C   
3376 O O   . ALA B 145 ? 0.5826 0.6003 0.6353 0.0530  0.1147  -0.0038 220 ALA B O   
3377 C CB  . ALA B 145 ? 0.4504 0.4759 0.4773 0.0299  0.1016  0.0086  220 ALA B CB  
3378 N N   . LEU B 146 ? 0.5836 0.5729 0.5566 0.0408  0.1091  -0.0047 221 LEU B N   
3379 C CA  . LEU B 146 ? 0.4810 0.4577 0.4450 0.0457  0.1019  -0.0087 221 LEU B CA  
3380 C C   . LEU B 146 ? 0.5632 0.5278 0.5321 0.0529  0.1214  -0.0182 221 LEU B C   
3381 O O   . LEU B 146 ? 0.6866 0.6469 0.6737 0.0610  0.1178  -0.0200 221 LEU B O   
3382 C CB  . LEU B 146 ? 0.4745 0.4359 0.3971 0.0389  0.0913  -0.0098 221 LEU B CB  
3383 C CG  . LEU B 146 ? 0.4168 0.3885 0.3375 0.0349  0.0728  -0.0020 221 LEU B CG  
3384 C CD1 . LEU B 146 ? 0.4602 0.4209 0.3513 0.0295  0.0640  -0.0038 221 LEU B CD1 
3385 C CD2 . LEU B 146 ? 0.4026 0.3832 0.3469 0.0395  0.0616  0.0031  221 LEU B CD2 
3386 N N   . ALA B 147 ? 0.5211 0.4765 0.4709 0.0506  0.1435  -0.0244 222 ALA B N   
3387 C CA  . ALA B 147 ? 0.4341 0.3764 0.3874 0.0587  0.1671  -0.0356 222 ALA B CA  
3388 C C   . ALA B 147 ? 0.3684 0.3348 0.3860 0.0701  0.1748  -0.0339 222 ALA B C   
3389 O O   . ALA B 147 ? 0.6643 0.6218 0.6994 0.0816  0.1846  -0.0417 222 ALA B O   
3390 C CB  . ALA B 147 ? 0.5043 0.4309 0.4194 0.0534  0.1927  -0.0416 222 ALA B CB  
3391 N N   . HIS B 148 ? 0.5375 0.5331 0.5932 0.0673  0.1686  -0.0242 223 HIS B N   
3392 C CA  . HIS B 148 ? 0.5526 0.5750 0.6763 0.0774  0.1691  -0.0215 223 HIS B CA  
3393 C C   . HIS B 148 ? 0.4529 0.4746 0.5931 0.0858  0.1412  -0.0165 223 HIS B C   
3394 O O   . HIS B 148 ? 0.5294 0.5555 0.7102 0.0996  0.1428  -0.0183 223 HIS B O   
3395 C CB  . HIS B 148 ? 0.5687 0.6203 0.7270 0.0691  0.1663  -0.0131 223 HIS B CB  
3396 C CG  . HIS B 148 ? 0.4358 0.5193 0.6703 0.0777  0.1611  -0.0098 223 HIS B CG  
3397 N ND1 . HIS B 148 ? 0.4395 0.5383 0.7237 0.0871  0.1882  -0.0157 223 HIS B ND1 
3398 C CD2 . HIS B 148 ? 0.3882 0.4910 0.6583 0.0785  0.1306  -0.0014 223 HIS B CD2 
3399 C CE1 . HIS B 148 ? 0.3279 0.4579 0.6827 0.0938  0.1724  -0.0103 223 HIS B CE1 
3400 N NE2 . HIS B 148 ? 0.3938 0.5248 0.7377 0.0882  0.1357  -0.0016 223 HIS B NE2 
3401 N N   . LEU B 149 ? 0.5160 0.5306 0.6248 0.0784  0.1167  -0.0097 224 LEU B N   
3402 C CA  . LEU B 149 ? 0.4233 0.4320 0.5377 0.0845  0.0927  -0.0032 224 LEU B CA  
3403 C C   . LEU B 149 ? 0.4695 0.4501 0.5666 0.0912  0.0986  -0.0094 224 LEU B C   
3404 O O   . LEU B 149 ? 0.6283 0.6036 0.7508 0.1027  0.0902  -0.0063 224 LEU B O   
3405 C CB  . LEU B 149 ? 0.3186 0.3247 0.3997 0.0743  0.0718  0.0044  224 LEU B CB  
3406 C CG  . LEU B 149 ? 0.4956 0.5218 0.5956 0.0712  0.0531  0.0126  224 LEU B CG  
3407 C CD1 . LEU B 149 ? 0.4465 0.4923 0.5685 0.0651  0.0646  0.0104  224 LEU B CD1 
3408 C CD2 . LEU B 149 ? 0.5235 0.5401 0.5832 0.0634  0.0378  0.0173  224 LEU B CD2 
3409 N N   . HIS B 150 ? 0.5759 0.5352 0.6289 0.0840  0.1105  -0.0182 225 HIS B N   
3410 C CA  . HIS B 150 ? 0.4464 0.3745 0.4783 0.0871  0.1127  -0.0253 225 HIS B CA  
3411 C C   . HIS B 150 ? 0.5338 0.4522 0.5910 0.1015  0.1334  -0.0359 225 HIS B C   
3412 O O   . HIS B 150 ? 0.7903 0.6854 0.8511 0.1096  0.1303  -0.0386 225 HIS B O   
3413 C CB  . HIS B 150 ? 0.5010 0.4096 0.4801 0.0742  0.1152  -0.0326 225 HIS B CB  
3414 C CG  . HIS B 150 ? 0.5130 0.4302 0.4734 0.0625  0.0957  -0.0232 225 HIS B CG  
3415 N ND1 . HIS B 150 ? 0.4799 0.3891 0.4028 0.0512  0.0930  -0.0269 225 HIS B ND1 
3416 C CD2 . HIS B 150 ? 0.4331 0.3653 0.4073 0.0616  0.0786  -0.0108 225 HIS B CD2 
3417 C CE1 . HIS B 150 ? 0.6613 0.5833 0.5825 0.0448  0.0771  -0.0174 225 HIS B CE1 
3418 N NE2 . HIS B 150 ? 0.4972 0.4317 0.4454 0.0506  0.0698  -0.0082 225 HIS B NE2 
3419 N N   . SER B 151 ? 0.5620 0.4964 0.6385 0.1051  0.1563  -0.0418 226 SER B N   
3420 C CA  . SER B 151 ? 0.4913 0.4202 0.5991 0.1208  0.1805  -0.0527 226 SER B CA  
3421 C C   . SER B 151 ? 0.4796 0.4250 0.6515 0.1371  0.1677  -0.0446 226 SER B C   
3422 O O   . SER B 151 ? 0.6491 0.5896 0.8554 0.1535  0.1847  -0.0530 226 SER B O   
3423 C CB  . SER B 151 ? 0.4490 0.3947 0.5665 0.1197  0.2118  -0.0592 226 SER B CB  
3424 O OG  . SER B 151 ? 0.7433 0.7292 0.9063 0.1165  0.2043  -0.0470 226 SER B OG  
3425 N N   . GLN B 152 ? 0.5246 0.4875 0.7115 0.1336  0.1377  -0.0288 227 GLN B N   
3426 C CA  . GLN B 152 ? 0.5042 0.4776 0.7422 0.1481  0.1174  -0.0186 227 GLN B CA  
3427 C C   . GLN B 152 ? 0.4860 0.4311 0.6941 0.1470  0.0912  -0.0086 227 GLN B C   
3428 O O   . GLN B 152 ? 0.5614 0.5105 0.7979 0.1564  0.0678  0.0040  227 GLN B O   
3429 C CB  . GLN B 152 ? 0.5089 0.5230 0.7884 0.1452  0.1018  -0.0078 227 GLN B CB  
3430 C CG  . GLN B 152 ? 0.6037 0.6475 0.9158 0.1423  0.1282  -0.0149 227 GLN B CG  
3431 C CD  . GLN B 152 ? 0.5397 0.6225 0.9010 0.1385  0.1097  -0.0048 227 GLN B CD  
3432 O OE1 . GLN B 152 ? 0.6518 0.7571 1.0791 0.1515  0.0986  -0.0006 227 GLN B OE1 
3433 N NE2 . GLN B 152 ? 0.5434 0.6331 0.8747 0.1208  0.1040  -0.0012 227 GLN B NE2 
3434 N N   . GLY B 153 ? 0.5512 0.4676 0.7031 0.1350  0.0938  -0.0130 228 GLY B N   
3435 C CA  . GLY B 153 ? 0.5154 0.4052 0.6406 0.1312  0.0734  -0.0029 228 GLY B CA  
3436 C C   . GLY B 153 ? 0.5695 0.4740 0.6810 0.1214  0.0501  0.0128  228 GLY B C   
3437 O O   . GLY B 153 ? 0.6735 0.5613 0.7757 0.1225  0.0315  0.0258  228 GLY B O   
3438 N N   . LEU B 154 ? 0.5977 0.5292 0.7043 0.1118  0.0516  0.0120  229 LEU B N   
3439 C CA  . LEU B 154 ? 0.5260 0.4696 0.6165 0.1029  0.0321  0.0236  229 LEU B CA  
3440 C C   . LEU B 154 ? 0.5025 0.4404 0.5482 0.0869  0.0371  0.0205  229 LEU B C   
3441 O O   . LEU B 154 ? 0.5965 0.5348 0.6305 0.0816  0.0534  0.0094  229 LEU B O   
3442 C CB  . LEU B 154 ? 0.4192 0.3962 0.5424 0.1041  0.0271  0.0248  229 LEU B CB  
3443 C CG  . LEU B 154 ? 0.4559 0.4493 0.6390 0.1196  0.0237  0.0259  229 LEU B CG  
3444 C CD1 . LEU B 154 ? 0.3397 0.3677 0.5564 0.1158  0.0178  0.0269  229 LEU B CD1 
3445 C CD2 . LEU B 154 ? 0.3647 0.3419 0.5559 0.1308  -0.0007 0.0384  229 LEU B CD2 
3446 N N   . VAL B 155 ? 0.5464 0.4785 0.5667 0.0799  0.0233  0.0306  230 VAL B N   
3447 C CA  . VAL B 155 ? 0.5182 0.4503 0.5055 0.0663  0.0266  0.0290  230 VAL B CA  
3448 C C   . VAL B 155 ? 0.5874 0.5361 0.5670 0.0628  0.0156  0.0352  230 VAL B C   
3449 O O   . VAL B 155 ? 0.6067 0.5509 0.5825 0.0662  0.0013  0.0454  230 VAL B O   
3450 C CB  . VAL B 155 ? 0.5114 0.4196 0.4767 0.0598  0.0258  0.0336  230 VAL B CB  
3451 C CG1 . VAL B 155 ? 0.5786 0.4918 0.5229 0.0466  0.0314  0.0291  230 VAL B CG1 
3452 C CG2 . VAL B 155 ? 0.6306 0.5150 0.6054 0.0653  0.0323  0.0283  230 VAL B CG2 
3453 N N   . HIS B 156 ? 0.4161 0.3796 0.3892 0.0565  0.0213  0.0291  231 HIS B N   
3454 C CA  . HIS B 156 ? 0.3737 0.3491 0.3392 0.0536  0.0120  0.0325  231 HIS B CA  
3455 C C   . HIS B 156 ? 0.4748 0.4405 0.4107 0.0489  0.0076  0.0388  231 HIS B C   
3456 O O   . HIS B 156 ? 0.5730 0.5360 0.4970 0.0503  -0.0039 0.0449  231 HIS B O   
3457 C CB  . HIS B 156 ? 0.3848 0.3730 0.3501 0.0486  0.0200  0.0252  231 HIS B CB  
3458 C CG  . HIS B 156 ? 0.4189 0.4167 0.3826 0.0466  0.0107  0.0265  231 HIS B CG  
3459 N ND1 . HIS B 156 ? 0.4963 0.4904 0.4348 0.0430  0.0066  0.0278  231 HIS B ND1 
3460 C CD2 . HIS B 156 ? 0.5006 0.5100 0.4864 0.0471  0.0053  0.0257  231 HIS B CD2 
3461 C CE1 . HIS B 156 ? 0.4117 0.4106 0.3515 0.0421  -0.0018 0.0267  231 HIS B CE1 
3462 N NE2 . HIS B 156 ? 0.5932 0.6017 0.5625 0.0433  -0.0041 0.0258  231 HIS B NE2 
3463 N N   . LEU B 157 ? 0.5033 0.4633 0.4269 0.0425  0.0169  0.0371  232 LEU B N   
3464 C CA  . LEU B 157 ? 0.5343 0.4876 0.4371 0.0367  0.0189  0.0430  232 LEU B CA  
3465 C C   . LEU B 157 ? 0.4599 0.4237 0.3488 0.0350  0.0188  0.0419  232 LEU B C   
3466 O O   . LEU B 157 ? 0.6326 0.5918 0.5039 0.0316  0.0235  0.0466  232 LEU B O   
3467 C CB  . LEU B 157 ? 0.5038 0.4376 0.3948 0.0391  0.0128  0.0547  232 LEU B CB  
3468 C CG  . LEU B 157 ? 0.5100 0.4254 0.4102 0.0397  0.0150  0.0576  232 LEU B CG  
3469 C CD1 . LEU B 157 ? 0.5539 0.4460 0.4375 0.0425  0.0069  0.0723  232 LEU B CD1 
3470 C CD2 . LEU B 157 ? 0.4422 0.3556 0.3428 0.0289  0.0264  0.0531  232 LEU B CD2 
3471 N N   . ASP B 158 ? 0.4757 0.4513 0.3719 0.0372  0.0158  0.0356  233 ASP B N   
3472 C CA  . ASP B 158 ? 0.5432 0.5243 0.4268 0.0366  0.0159  0.0328  233 ASP B CA  
3473 C C   . ASP B 158 ? 0.5576 0.5489 0.4534 0.0365  0.0162  0.0258  233 ASP B C   
3474 O O   . ASP B 158 ? 0.6295 0.6219 0.5237 0.0378  0.0104  0.0233  233 ASP B O   
3475 C CB  . ASP B 158 ? 0.6224 0.5943 0.4873 0.0396  0.0056  0.0361  233 ASP B CB  
3476 C CG  . ASP B 158 ? 0.8587 0.8272 0.6990 0.0391  0.0110  0.0336  233 ASP B CG  
3477 O OD1 . ASP B 158 ? 0.9446 0.9142 0.7791 0.0367  0.0243  0.0354  233 ASP B OD1 
3478 O OD2 . ASP B 158 ? 0.9091 0.8732 0.7377 0.0411  0.0028  0.0291  233 ASP B OD2 
3479 N N   . VAL B 159 ? 0.4705 0.4654 0.3751 0.0341  0.0220  0.0228  234 VAL B N   
3480 C CA  . VAL B 159 ? 0.5300 0.5292 0.4382 0.0333  0.0232  0.0185  234 VAL B CA  
3481 C C   . VAL B 159 ? 0.4965 0.4995 0.3981 0.0333  0.0232  0.0170  234 VAL B C   
3482 O O   . VAL B 159 ? 0.7403 0.7472 0.6439 0.0313  0.0253  0.0167  234 VAL B O   
3483 C CB  . VAL B 159 ? 0.4489 0.4448 0.3601 0.0312  0.0286  0.0156  234 VAL B CB  
3484 C CG1 . VAL B 159 ? 0.5010 0.4960 0.4055 0.0295  0.0301  0.0132  234 VAL B CG1 
3485 C CG2 . VAL B 159 ? 0.4960 0.4891 0.4199 0.0340  0.0315  0.0156  234 VAL B CG2 
3486 N N   . LYS B 160 ? 0.6158 0.6178 0.5137 0.0358  0.0201  0.0157  235 LYS B N   
3487 C CA  . LYS B 160 ? 0.4317 0.4356 0.3267 0.0389  0.0205  0.0136  235 LYS B CA  
3488 C C   . LYS B 160 ? 0.5266 0.5226 0.4186 0.0403  0.0160  0.0116  235 LYS B C   
3489 O O   . LYS B 160 ? 0.5154 0.5071 0.4092 0.0375  0.0128  0.0119  235 LYS B O   
3490 C CB  . LYS B 160 ? 0.4314 0.4367 0.3197 0.0416  0.0253  0.0132  235 LYS B CB  
3491 C CG  . LYS B 160 ? 0.3742 0.3688 0.2459 0.0425  0.0220  0.0129  235 LYS B CG  
3492 C CD  . LYS B 160 ? 0.5741 0.5653 0.4293 0.0450  0.0306  0.0126  235 LYS B CD  
3493 C CE  . LYS B 160 ? 0.6429 0.6178 0.4708 0.0452  0.0242  0.0132  235 LYS B CE  
3494 N NZ  . LYS B 160 ? 0.8026 0.7693 0.6046 0.0468  0.0366  0.0140  235 LYS B NZ  
3495 N N   . PRO B 161 ? 0.5901 0.5837 0.4817 0.0446  0.0150  0.0100  236 PRO B N   
3496 C CA  . PRO B 161 ? 0.3901 0.3704 0.2779 0.0449  0.0106  0.0092  236 PRO B CA  
3497 C C   . PRO B 161 ? 0.4113 0.3824 0.2930 0.0439  0.0070  0.0050  236 PRO B C   
3498 O O   . PRO B 161 ? 0.5995 0.5604 0.4831 0.0396  0.0025  0.0049  236 PRO B O   
3499 C CB  . PRO B 161 ? 0.4709 0.4490 0.3609 0.0528  0.0094  0.0080  236 PRO B CB  
3500 C CG  . PRO B 161 ? 0.5405 0.5343 0.4405 0.0535  0.0105  0.0103  236 PRO B CG  
3501 C CD  . PRO B 161 ? 0.5650 0.5678 0.4649 0.0490  0.0166  0.0098  236 PRO B CD  
3502 N N   . ALA B 162 ? 0.4456 0.4177 0.3177 0.0464  0.0083  0.0018  237 ALA B N   
3503 C CA  . ALA B 162 ? 0.3807 0.3401 0.2397 0.0449  0.0006  -0.0030 237 ALA B CA  
3504 C C   . ALA B 162 ? 0.5745 0.5385 0.4449 0.0378  -0.0079 0.0007  237 ALA B C   
3505 O O   . ALA B 162 ? 0.6357 0.5907 0.5036 0.0343  -0.0195 -0.0028 237 ALA B O   
3506 C CB  . ALA B 162 ? 0.3926 0.3471 0.2286 0.0495  0.0050  -0.0065 237 ALA B CB  
3507 N N   . ASN B 163 ? 0.5791 0.5567 0.4646 0.0360  -0.0032 0.0066  238 ASN B N   
3508 C CA  . ASN B 163 ? 0.4849 0.4697 0.3888 0.0320  -0.0087 0.0097  238 ASN B CA  
3509 C C   . ASN B 163 ? 0.4213 0.4126 0.3467 0.0273  -0.0019 0.0120  238 ASN B C   
3510 O O   . ASN B 163 ? 0.5586 0.5598 0.5059 0.0255  -0.0006 0.0144  238 ASN B O   
3511 C CB  . ASN B 163 ? 0.4838 0.4741 0.3868 0.0349  -0.0067 0.0140  238 ASN B CB  
3512 C CG  . ASN B 163 ? 0.4607 0.4411 0.3375 0.0380  -0.0116 0.0141  238 ASN B CG  
3513 O OD1 . ASN B 163 ? 0.6870 0.6562 0.5464 0.0381  -0.0198 0.0097  238 ASN B OD1 
3514 N ND2 . ASN B 163 ? 0.6103 0.5910 0.4804 0.0396  -0.0058 0.0191  238 ASN B ND2 
3515 N N   . ILE B 164 ? 0.5092 0.4935 0.4282 0.0260  0.0035  0.0120  239 ILE B N   
3516 C CA  . ILE B 164 ? 0.3755 0.3591 0.3051 0.0201  0.0116  0.0155  239 ILE B CA  
3517 C C   . ILE B 164 ? 0.5044 0.4758 0.4369 0.0146  0.0063  0.0148  239 ILE B C   
3518 O O   . ILE B 164 ? 0.5705 0.5281 0.4866 0.0182  0.0009  0.0120  239 ILE B O   
3519 C CB  . ILE B 164 ? 0.4676 0.4466 0.3807 0.0222  0.0198  0.0181  239 ILE B CB  
3520 C CG1 . ILE B 164 ? 0.4649 0.4529 0.3769 0.0253  0.0240  0.0174  239 ILE B CG1 
3521 C CG2 . ILE B 164 ? 0.4709 0.4418 0.3827 0.0156  0.0294  0.0229  239 ILE B CG2 
3522 C CD1 . ILE B 164 ? 0.4779 0.4603 0.3726 0.0260  0.0273  0.0183  239 ILE B CD1 
3523 N N   . PHE B 165 ? 0.4625 0.4387 0.4192 0.0058  0.0088  0.0170  240 PHE B N   
3524 C CA  . PHE B 165 ? 0.4175 0.3820 0.3834 -0.0026 0.0019  0.0161  240 PHE B CA  
3525 C C   . PHE B 165 ? 0.4399 0.3984 0.4138 -0.0120 0.0166  0.0237  240 PHE B C   
3526 O O   . PHE B 165 ? 0.6761 0.6494 0.6699 -0.0161 0.0304  0.0274  240 PHE B O   
3527 C CB  . PHE B 165 ? 0.3464 0.3223 0.3398 -0.0076 -0.0122 0.0121  240 PHE B CB  
3528 C CG  . PHE B 165 ? 0.4820 0.4592 0.4590 0.0011  -0.0261 0.0067  240 PHE B CG  
3529 C CD1 . PHE B 165 ? 0.4796 0.4370 0.4274 0.0043  -0.0373 -0.0003 240 PHE B CD1 
3530 C CD2 . PHE B 165 ? 0.4758 0.4700 0.4630 0.0064  -0.0260 0.0090  240 PHE B CD2 
3531 C CE1 . PHE B 165 ? 0.4759 0.4308 0.4012 0.0114  -0.0465 -0.0042 240 PHE B CE1 
3532 C CE2 . PHE B 165 ? 0.4487 0.4392 0.4152 0.0133  -0.0378 0.0066  240 PHE B CE2 
3533 C CZ  . PHE B 165 ? 0.5098 0.4807 0.4432 0.0152  -0.0471 0.0004  240 PHE B CZ  
3534 N N   . LEU B 166 ? 0.5629 0.4971 0.5198 -0.0148 0.0152  0.0262  241 LEU B N   
3535 C CA  . LEU B 166 ? 0.7080 0.6284 0.6595 -0.0231 0.0298  0.0361  241 LEU B CA  
3536 C C   . LEU B 166 ? 0.6586 0.5833 0.6458 -0.0392 0.0355  0.0391  241 LEU B C   
3537 O O   . LEU B 166 ? 0.6202 0.5484 0.6314 -0.0447 0.0208  0.0328  241 LEU B O   
3538 C CB  . LEU B 166 ? 0.5761 0.4652 0.4971 -0.0192 0.0239  0.0396  241 LEU B CB  
3539 C CG  . LEU B 166 ? 0.4858 0.3734 0.3825 -0.0031 0.0157  0.0358  241 LEU B CG  
3540 C CD1 . LEU B 166 ? 0.6811 0.5387 0.5549 0.0015  0.0110  0.0418  241 LEU B CD1 
3541 C CD2 . LEU B 166 ? 0.4747 0.3801 0.3633 0.0017  0.0236  0.0373  241 LEU B CD2 
3542 N N   . GLY B 167 ? 0.8015 0.7252 0.7917 -0.0478 0.0573  0.0485  242 GLY B N   
3543 C CA  . GLY B 167 ? 0.7850 0.7146 0.8139 -0.0650 0.0684  0.0533  242 GLY B CA  
3544 C C   . GLY B 167 ? 0.8797 0.7772 0.8852 -0.0759 0.0831  0.0661  242 GLY B C   
3545 O O   . GLY B 167 ? 1.0030 0.8710 0.9621 -0.0686 0.0786  0.0708  242 GLY B O   
3546 N N   . PRO B 168 ? 0.7697 0.6719 0.8092 -0.0936 0.1007  0.0731  243 PRO B N   
3547 C CA  . PRO B 168 ? 0.8480 0.7154 0.8620 -0.1063 0.1177  0.0880  243 PRO B CA  
3548 C C   . PRO B 168 ? 0.8962 0.7520 0.8629 -0.1012 0.1415  0.0970  243 PRO B C   
3549 O O   . PRO B 168 ? 0.8085 0.6895 0.7802 -0.0942 0.1547  0.0918  243 PRO B O   
3550 C CB  . PRO B 168 ? 0.8893 0.7730 0.9632 -0.1283 0.1325  0.0920  243 PRO B CB  
3551 C CG  . PRO B 168 ? 0.7418 0.6748 0.8672 -0.1235 0.1341  0.0815  243 PRO B CG  
3552 C CD  . PRO B 168 ? 0.8774 0.8171 0.9841 -0.1036 0.1050  0.0687  243 PRO B CD  
3553 N N   . ARG B 169 ? 0.9742 0.7870 0.8911 -0.1043 0.1450  0.1105  244 ARG B N   
3554 C CA  . ARG B 169 ? 0.9594 0.7501 0.8195 -0.1024 0.1656  0.1213  244 ARG B CA  
3555 C C   . ARG B 169 ? 0.8795 0.6807 0.7086 -0.0828 0.1544  0.1117  244 ARG B C   
3556 O O   . ARG B 169 ? 0.8913 0.6978 0.6990 -0.0807 0.1741  0.1109  244 ARG B O   
3557 C CB  . ARG B 169 ? 0.8971 0.6998 0.7753 -0.1177 0.2054  0.1276  244 ARG B CB  
3558 C CG  . ARG B 169 ? 0.9857 0.7710 0.8810 -0.1384 0.2185  0.1410  244 ARG B CG  
3559 C CD  . ARG B 169 ? 1.1706 0.9975 1.1309 -0.1508 0.2437  0.1374  244 ARG B CD  
3560 N NE  . ARG B 169 ? 1.2853 1.1515 1.3182 -0.1522 0.2357  0.1252  244 ARG B NE  
3561 C CZ  . ARG B 169 ? 1.4771 1.3844 1.5845 -0.1625 0.2467  0.1208  244 ARG B CZ  
3562 N NH1 . ARG B 169 ? 1.5158 1.4302 1.6352 -0.1732 0.2708  0.1274  244 ARG B NH1 
3563 N NH2 . ARG B 169 ? 1.3558 1.3001 1.5254 -0.1594 0.2271  0.1082  244 ARG B NH2 
3564 N N   . GLY B 170 ? 0.8769 0.6796 0.7040 -0.0688 0.1238  0.1037  245 GLY B N   
3565 C CA  . GLY B 170 ? 0.6055 0.4154 0.4055 -0.0522 0.1110  0.0962  245 GLY B CA  
3566 C C   . GLY B 170 ? 0.7982 0.6463 0.6260 -0.0467 0.1172  0.0830  245 GLY B C   
3567 O O   . GLY B 170 ? 0.9277 0.7794 0.7317 -0.0358 0.1103  0.0774  245 GLY B O   
3568 N N   . ARG B 171 ? 0.7531 0.6288 0.6328 -0.0541 0.1281  0.0782  246 ARG B N   
3569 C CA  . ARG B 171 ? 0.5641 0.4741 0.4745 -0.0470 0.1308  0.0666  246 ARG B CA  
3570 C C   . ARG B 171 ? 0.6885 0.6147 0.6200 -0.0374 0.1029  0.0569  246 ARG B C   
3571 O O   . ARG B 171 ? 0.6689 0.5840 0.6011 -0.0381 0.0851  0.0571  246 ARG B O   
3572 C CB  . ARG B 171 ? 0.7186 0.6533 0.6812 -0.0573 0.1534  0.0664  246 ARG B CB  
3573 C CG  . ARG B 171 ? 0.7646 0.6827 0.7112 -0.0700 0.1866  0.0772  246 ARG B CG  
3574 C CD  . ARG B 171 ? 0.8005 0.7006 0.6900 -0.0630 0.2033  0.0769  246 ARG B CD  
3575 N NE  . ARG B 171 ? 0.9461 0.8729 0.8585 -0.0532 0.2128  0.0646  246 ARG B NE  
3576 C CZ  . ARG B 171 ? 1.2247 1.1670 1.1641 -0.0564 0.2458  0.0624  246 ARG B CZ  
3577 N NH1 . ARG B 171 ? 1.2908 1.2309 1.2416 -0.0685 0.2648  0.0695  246 ARG B NH1 
3578 N NH2 . ARG B 171 ? 1.0428 1.0055 1.0021 -0.0445 0.2507  0.0503  246 ARG B NH2 
3579 N N   . CYS B 172 ? 0.7003 0.6493 0.6455 -0.0283 0.1008  0.0482  247 CYS B N   
3580 C CA  . CYS B 172 ? 0.6996 0.6629 0.6612 -0.0202 0.0780  0.0402  247 CYS B CA  
3581 C C   . CYS B 172 ? 0.5786 0.5687 0.5726 -0.0154 0.0820  0.0343  247 CYS B C   
3582 O O   . CYS B 172 ? 0.6823 0.6793 0.6842 -0.0160 0.1028  0.0345  247 CYS B O   
3583 C CB  . CYS B 172 ? 0.5842 0.5349 0.5086 -0.0097 0.0636  0.0382  247 CYS B CB  
3584 S SG  . CYS B 172 ? 0.7074 0.6599 0.6058 -0.0018 0.0707  0.0352  247 CYS B SG  
3585 N N   . LYS B 173 ? 0.4790 0.4811 0.4893 -0.0098 0.0623  0.0290  248 LYS B N   
3586 C CA  . LYS B 173 ? 0.4452 0.4696 0.4877 -0.0042 0.0605  0.0252  248 LYS B CA  
3587 C C   . LYS B 173 ? 0.5254 0.5479 0.5492 0.0056  0.0427  0.0215  248 LYS B C   
3588 O O   . LYS B 173 ? 0.5076 0.5206 0.5143 0.0060  0.0272  0.0201  248 LYS B O   
3589 C CB  . LYS B 173 ? 0.4400 0.4832 0.5340 -0.0110 0.0526  0.0252  248 LYS B CB  
3590 C CG  . LYS B 173 ? 0.4978 0.5474 0.6216 -0.0232 0.0733  0.0298  248 LYS B CG  
3591 C CD  . LYS B 173 ? 0.4427 0.5162 0.6282 -0.0309 0.0622  0.0292  248 LYS B CD  
3592 C CE  . LYS B 173 ? 0.5443 0.6287 0.7680 -0.0442 0.0884  0.0345  248 LYS B CE  
3593 N NZ  . LYS B 173 ? 0.7966 0.9111 1.0937 -0.0524 0.0775  0.0338  248 LYS B NZ  
3594 N N   . LEU B 174 ? 0.4415 0.4705 0.4673 0.0133  0.0473  0.0197  249 LEU B N   
3595 C CA  . LEU B 174 ? 0.3143 0.3411 0.3259 0.0210  0.0332  0.0181  249 LEU B CA  
3596 C C   . LEU B 174 ? 0.3852 0.4221 0.4217 0.0225  0.0148  0.0185  249 LEU B C   
3597 O O   . LEU B 174 ? 0.4323 0.4849 0.5095 0.0217  0.0147  0.0193  249 LEU B O   
3598 C CB  . LEU B 174 ? 0.4187 0.4444 0.4252 0.0274  0.0433  0.0165  249 LEU B CB  
3599 C CG  . LEU B 174 ? 0.4840 0.5046 0.4756 0.0333  0.0321  0.0169  249 LEU B CG  
3600 C CD1 . LEU B 174 ? 0.3841 0.3951 0.3437 0.0315  0.0265  0.0168  249 LEU B CD1 
3601 C CD2 . LEU B 174 ? 0.5144 0.5300 0.5046 0.0379  0.0426  0.0146  249 LEU B CD2 
3602 N N   . GLY B 175 ? 0.4813 0.5087 0.4934 0.0247  -0.0010 0.0180  250 GLY B N   
3603 C CA  . GLY B 175 ? 0.3380 0.3681 0.3609 0.0258  -0.0222 0.0184  250 GLY B CA  
3604 C C   . GLY B 175 ? 0.4498 0.4676 0.4402 0.0320  -0.0324 0.0200  250 GLY B C   
3605 O O   . GLY B 175 ? 0.5577 0.5698 0.5281 0.0356  -0.0214 0.0213  250 GLY B O   
3606 N N   . ASP B 176 ? 0.5302 0.5423 0.5138 0.0321  -0.0539 0.0201  251 ASP B N   
3607 C CA  . ASP B 176 ? 0.4974 0.4933 0.4436 0.0370  -0.0639 0.0231  251 ASP B CA  
3608 C C   . ASP B 176 ? 0.5555 0.5527 0.5076 0.0437  -0.0586 0.0304  251 ASP B C   
3609 O O   . ASP B 176 ? 0.5859 0.5771 0.5190 0.0449  -0.0430 0.0317  251 ASP B O   
3610 C CB  . ASP B 176 ? 0.5573 0.5380 0.4609 0.0364  -0.0535 0.0192  251 ASP B CB  
3611 C CG  . ASP B 176 ? 0.8387 0.7992 0.6981 0.0391  -0.0630 0.0208  251 ASP B CG  
3612 O OD1 . ASP B 176 ? 0.7371 0.6924 0.5939 0.0415  -0.0796 0.0270  251 ASP B OD1 
3613 O OD2 . ASP B 176 ? 0.8849 0.8333 0.7114 0.0394  -0.0534 0.0163  251 ASP B OD2 
3614 N N   . PHE B 177 ? 0.5237 0.5285 0.5060 0.0481  -0.0728 0.0350  252 PHE B N   
3615 C CA  . PHE B 177 ? 0.4269 0.4291 0.4190 0.0562  -0.0701 0.0420  252 PHE B CA  
3616 C C   . PHE B 177 ? 0.4006 0.3802 0.3556 0.0602  -0.0870 0.0510  252 PHE B C   
3617 O O   . PHE B 177 ? 0.6046 0.5795 0.5735 0.0680  -0.0967 0.0591  252 PHE B O   
3618 C CB  . PHE B 177 ? 0.3504 0.3734 0.4017 0.0614  -0.0741 0.0425  252 PHE B CB  
3619 C CG  . PHE B 177 ? 0.3966 0.4386 0.4799 0.0569  -0.0523 0.0351  252 PHE B CG  
3620 C CD1 . PHE B 177 ? 0.4359 0.4719 0.4982 0.0541  -0.0281 0.0311  252 PHE B CD1 
3621 C CD2 . PHE B 177 ? 0.4918 0.5565 0.6251 0.0543  -0.0567 0.0330  252 PHE B CD2 
3622 C CE1 . PHE B 177 ? 0.4229 0.4704 0.5042 0.0497  -0.0085 0.0258  252 PHE B CE1 
3623 C CE2 . PHE B 177 ? 0.4911 0.5696 0.6483 0.0489  -0.0330 0.0280  252 PHE B CE2 
3624 C CZ  . PHE B 177 ? 0.3611 0.4285 0.4874 0.0469  -0.0089 0.0248  252 PHE B CZ  
3625 N N   . GLY B 178 ? 0.5536 0.5162 0.4594 0.0557  -0.0897 0.0501  253 GLY B N   
3626 C CA  . GLY B 178 ? 0.4528 0.3892 0.3136 0.0582  -0.1035 0.0594  253 GLY B CA  
3627 C C   . GLY B 178 ? 0.6307 0.5533 0.4754 0.0604  -0.0880 0.0685  253 GLY B C   
3628 O O   . GLY B 178 ? 0.8198 0.7212 0.6429 0.0646  -0.1006 0.0804  253 GLY B O   
3629 N N   . LEU B 179 ? 0.5341 0.4658 0.3881 0.0567  -0.0626 0.0637  254 LEU B N   
3630 C CA  . LEU B 179 ? 0.6472 0.5668 0.4923 0.0559  -0.0477 0.0706  254 LEU B CA  
3631 C C   . LEU B 179 ? 0.6263 0.5523 0.5125 0.0609  -0.0442 0.0705  254 LEU B C   
3632 O O   . LEU B 179 ? 0.6999 0.6136 0.5824 0.0594  -0.0329 0.0745  254 LEU B O   
3633 C CB  . LEU B 179 ? 0.5750 0.4997 0.4070 0.0483  -0.0248 0.0648  254 LEU B CB  
3634 C CG  . LEU B 179 ? 0.6354 0.5499 0.4245 0.0445  -0.0196 0.0649  254 LEU B CG  
3635 C CD1 . LEU B 179 ? 0.8639 0.7884 0.6551 0.0387  0.0037  0.0604  254 LEU B CD1 
3636 C CD2 . LEU B 179 ? 0.6481 0.5343 0.3961 0.0451  -0.0261 0.0781  254 LEU B CD2 
3637 N N   . LEU B 180 ? 0.6434 0.5873 0.5695 0.0663  -0.0519 0.0653  255 LEU B N   
3638 C CA  . LEU B 180 ? 0.4233 0.3733 0.3882 0.0723  -0.0434 0.0624  255 LEU B CA  
3639 C C   . LEU B 180 ? 0.5627 0.4914 0.5295 0.0810  -0.0538 0.0736  255 LEU B C   
3640 O O   . LEU B 180 ? 0.7218 0.6407 0.6798 0.0862  -0.0762 0.0837  255 LEU B O   
3641 C CB  . LEU B 180 ? 0.6041 0.5797 0.6144 0.0760  -0.0464 0.0553  255 LEU B CB  
3642 C CG  . LEU B 180 ? 0.5078 0.4927 0.5606 0.0832  -0.0320 0.0495  255 LEU B CG  
3643 C CD1 . LEU B 180 ? 0.4433 0.4530 0.5233 0.0790  -0.0199 0.0398  255 LEU B CD1 
3644 C CD2 . LEU B 180 ? 0.5234 0.5071 0.6118 0.0968  -0.0475 0.0564  255 LEU B CD2 
3645 N N   . VAL B 181 ? 0.5147 0.4321 0.4901 0.0828  -0.0393 0.0719  256 VAL B N   
3646 C CA  . VAL B 181 ? 0.5320 0.4247 0.5127 0.0920  -0.0472 0.0819  256 VAL B CA  
3647 C C   . VAL B 181 ? 0.5346 0.4326 0.5592 0.1017  -0.0358 0.0723  256 VAL B C   
3648 O O   . VAL B 181 ? 0.6461 0.5581 0.6805 0.0974  -0.0168 0.0585  256 VAL B O   
3649 C CB  . VAL B 181 ? 0.5486 0.4107 0.4894 0.0834  -0.0395 0.0905  256 VAL B CB  
3650 C CG1 . VAL B 181 ? 0.9270 0.7852 0.8230 0.0736  -0.0429 0.0979  256 VAL B CG1 
3651 C CG2 . VAL B 181 ? 0.6542 0.5169 0.5988 0.0750  -0.0170 0.0785  256 VAL B CG2 
3652 N N   . GLU B 182 ? 0.5506 0.4345 0.5990 0.1159  -0.0474 0.0796  257 GLU B N   
3653 C CA  . GLU B 182 ? 0.5863 0.4694 0.6758 0.1280  -0.0344 0.0701  257 GLU B CA  
3654 C C   . GLU B 182 ? 0.5795 0.4226 0.6486 0.1280  -0.0273 0.0728  257 GLU B C   
3655 O O   . GLU B 182 ? 0.6785 0.4934 0.7269 0.1296  -0.0427 0.0890  257 GLU B O   
3656 C CB  . GLU B 182 ? 0.5686 0.4656 0.7114 0.1466  -0.0515 0.0748  257 GLU B CB  
3657 C CG  . GLU B 182 ? 0.5194 0.4173 0.7102 0.1617  -0.0336 0.0633  257 GLU B CG  
3658 C CD  . GLU B 182 ? 0.9455 0.8615 1.2004 0.1820  -0.0508 0.0685  257 GLU B CD  
3659 O OE1 . GLU B 182 ? 1.0956 1.0113 1.3496 0.1853  -0.0830 0.0842  257 GLU B OE1 
3660 O OE2 . GLU B 182 ? 0.9675 0.8978 1.2737 0.1948  -0.0322 0.0566  257 GLU B OE2 
3661 N N   . LEU B 183 ? 0.5972 0.4339 0.6681 0.1250  -0.0046 0.0573  258 LEU B N   
3662 C CA  . LEU B 183 ? 0.6519 0.4483 0.7040 0.1222  0.0022  0.0569  258 LEU B CA  
3663 C C   . LEU B 183 ? 0.7693 0.5418 0.8521 0.1425  -0.0057 0.0623  258 LEU B C   
3664 O O   . LEU B 183 ? 0.9729 0.7492 1.0918 0.1567  0.0064  0.0490  258 LEU B O   
3665 C CB  . LEU B 183 ? 0.7567 0.5507 0.7997 0.1136  0.0249  0.0366  258 LEU B CB  
3666 C CG  . LEU B 183 ? 0.7015 0.5165 0.7159 0.0949  0.0297  0.0326  258 LEU B CG  
3667 C CD1 . LEU B 183 ? 0.7557 0.5629 0.7562 0.0866  0.0467  0.0138  258 LEU B CD1 
3668 C CD2 . LEU B 183 ? 0.6267 0.4309 0.6111 0.0814  0.0197  0.0477  258 LEU B CD2 
3669 N N   . GLY B 184 ? 1.0515 0.7973 1.1189 0.1447  -0.0252 0.0825  259 GLY B N   
3670 C CA  . GLY B 184 ? 0.8389 0.5565 0.9327 0.1649  -0.0373 0.0913  259 GLY B CA  
3671 C C   . GLY B 184 ? 1.3467 1.0152 1.4019 0.1585  -0.0482 0.1108  259 GLY B C   
3672 O O   . GLY B 184 ? 1.4246 1.0902 1.4399 0.1454  -0.0584 0.1266  259 GLY B O   
3673 N N   . THR B 185 ? 1.4892 1.1162 1.5540 0.1674  -0.0439 0.1096  260 THR B N   
3674 C CA  . THR B 185 ? 1.3959 0.9696 1.4253 0.1597  -0.0512 0.1284  260 THR B CA  
3675 C C   . THR B 185 ? 1.4135 0.9821 1.4282 0.1667  -0.0758 0.1547  260 THR B C   
3676 O O   . THR B 185 ? 1.2344 0.8070 1.2091 0.1521  -0.0834 0.1693  260 THR B O   
3677 C CB  . THR B 185 ? 1.4820 1.0116 1.5272 0.1698  -0.0421 0.1194  260 THR B CB  
3678 O OG1 . THR B 185 ? 1.3577 0.8938 1.4094 0.1615  -0.0177 0.0922  260 THR B OG1 
3679 C CG2 . THR B 185 ? 1.6093 1.0901 1.6187 0.1561  -0.0437 0.1386  260 THR B CG2 
3680 N N   . GLU B 190 ? 1.2485 0.9249 0.9736 0.0673  -0.0686 0.1883  265 GLU B N   
3681 C CA  . GLU B 190 ? 1.1675 0.8788 0.9158 0.0771  -0.0853 0.1753  265 GLU B CA  
3682 C C   . GLU B 190 ? 1.2484 0.9986 1.0075 0.0672  -0.0652 0.1557  265 GLU B C   
3683 O O   . GLU B 190 ? 1.1594 0.9342 0.9240 0.0705  -0.0753 0.1462  265 GLU B O   
3684 C CB  . GLU B 190 ? 1.2842 1.0076 1.0928 0.0938  -0.0996 0.1689  265 GLU B CB  
3685 C CG  . GLU B 190 ? 1.3418 1.0691 1.1890 0.0920  -0.0777 0.1569  265 GLU B CG  
3686 C CD  . GLU B 190 ? 1.5368 1.2735 1.4410 0.1103  -0.0872 0.1495  265 GLU B CD  
3687 O OE1 . GLU B 190 ? 1.7209 1.4732 1.6470 0.1232  -0.1098 0.1514  265 GLU B OE1 
3688 O OE2 . GLU B 190 ? 1.4326 1.1609 1.3614 0.1117  -0.0719 0.1408  265 GLU B OE2 
3689 N N   . VAL B 191 ? 1.1610 0.9151 0.9249 0.0548  -0.0389 0.1501  266 VAL B N   
3690 C CA  . VAL B 191 ? 0.8189 0.6068 0.5931 0.0461  -0.0213 0.1336  266 VAL B CA  
3691 C C   . VAL B 191 ? 1.0319 0.8157 0.7588 0.0377  -0.0122 0.1387  266 VAL B C   
3692 O O   . VAL B 191 ? 1.0862 0.8397 0.7731 0.0317  -0.0063 0.1547  266 VAL B O   
3693 C CB  . VAL B 191 ? 0.7993 0.5932 0.6004 0.0366  -0.0013 0.1253  266 VAL B CB  
3694 C CG1 . VAL B 191 ? 0.9442 0.7708 0.7543 0.0281  0.0138  0.1109  266 VAL B CG1 
3695 C CG2 . VAL B 191 ? 0.8220 0.6167 0.6633 0.0462  -0.0076 0.1168  266 VAL B CG2 
3696 N N   . GLN B 192 ? 1.0326 0.8440 0.7620 0.0373  -0.0093 0.1252  267 GLN B N   
3697 C CA  . GLN B 192 ? 0.9296 0.7382 0.6164 0.0318  0.0013  0.1257  267 GLN B CA  
3698 C C   . GLN B 192 ? 0.9929 0.8281 0.6997 0.0232  0.0267  0.1141  267 GLN B C   
3699 O O   . GLN B 192 ? 0.8310 0.6876 0.5811 0.0215  0.0310  0.1046  267 GLN B O   
3700 C CB  . GLN B 192 ? 0.8711 0.6843 0.5413 0.0397  -0.0192 0.1191  267 GLN B CB  
3701 C CG  . GLN B 192 ? 1.0528 0.8489 0.7196 0.0496  -0.0508 0.1283  267 GLN B CG  
3702 C CD  . GLN B 192 ? 1.1659 0.9675 0.8200 0.0544  -0.0736 0.1207  267 GLN B CD  
3703 O OE1 . GLN B 192 ? 1.3793 1.1783 0.9998 0.0486  -0.0679 0.1150  267 GLN B OE1 
3704 N NE2 . GLN B 192 ? 1.1040 0.9229 0.8023 0.0623  -0.0959 0.1161  267 GLN B NE2 
3705 N N   . GLU B 193 ? 1.0550 0.8872 0.7282 0.0184  0.0433  0.1149  268 GLU B N   
3706 C CA  . GLU B 193 ? 1.0027 0.8611 0.6982 0.0118  0.0673  0.1051  268 GLU B CA  
3707 C C   . GLU B 193 ? 0.9640 0.8521 0.6916 0.0181  0.0593  0.0877  268 GLU B C   
3708 O O   . GLU B 193 ? 0.9362 0.8228 0.6462 0.0252  0.0469  0.0815  268 GLU B O   
3709 C CB  . GLU B 193 ? 0.8574 0.7087 0.5155 0.0078  0.0870  0.1071  268 GLU B CB  
3710 C CG  . GLU B 193 ? 1.0808 0.9106 0.7182 -0.0016 0.0971  0.1223  268 GLU B CG  
3711 C CD  . GLU B 193 ? 1.2342 1.0723 0.9043 -0.0140 0.1192  0.1285  268 GLU B CD  
3712 O OE1 . GLU B 193 ? 1.0433 0.9097 0.7501 -0.0161 0.1327  0.1190  268 GLU B OE1 
3713 O OE2 . GLU B 193 ? 1.3709 1.1867 1.0321 -0.0220 0.1218  0.1432  268 GLU B OE2 
3714 N N   . GLY B 194 ? 0.9350 0.8469 0.7068 0.0143  0.0652  0.0804  269 GLY B N   
3715 C CA  . GLY B 194 ? 0.7412 0.6775 0.5394 0.0191  0.0596  0.0663  269 GLY B CA  
3716 C C   . GLY B 194 ? 0.7372 0.6919 0.5422 0.0183  0.0760  0.0591  269 GLY B C   
3717 O O   . GLY B 194 ? 0.8184 0.7705 0.6106 0.0141  0.0949  0.0637  269 GLY B O   
3718 N N   . ASP B 195 ? 0.7266 0.6992 0.5532 0.0230  0.0698  0.0481  270 ASP B N   
3719 C CA  . ASP B 195 ? 0.5829 0.5740 0.4240 0.0251  0.0823  0.0407  270 ASP B CA  
3720 C C   . ASP B 195 ? 0.6241 0.6350 0.5035 0.0174  0.0908  0.0419  270 ASP B C   
3721 O O   . ASP B 195 ? 0.5712 0.5881 0.4722 0.0144  0.0789  0.0398  270 ASP B O   
3722 C CB  . ASP B 195 ? 0.5907 0.5892 0.4405 0.0327  0.0702  0.0307  270 ASP B CB  
3723 C CG  . ASP B 195 ? 0.6684 0.6761 0.5219 0.0392  0.0812  0.0231  270 ASP B CG  
3724 O OD1 . ASP B 195 ? 0.6360 0.6585 0.5085 0.0375  0.0979  0.0238  270 ASP B OD1 
3725 O OD2 . ASP B 195 ? 0.7213 0.7213 0.5626 0.0460  0.0735  0.0160  270 ASP B OD2 
3726 N N   . PRO B 196 ? 0.5230 0.5441 0.4121 0.0132  0.1112  0.0445  271 PRO B N   
3727 C CA  . PRO B 196 ? 0.4169 0.4592 0.3500 0.0033  0.1165  0.0459  271 PRO B CA  
3728 C C   . PRO B 196 ? 0.4534 0.5200 0.4241 0.0073  0.1044  0.0367  271 PRO B C   
3729 O O   . PRO B 196 ? 0.4835 0.5626 0.4863 -0.0013 0.0971  0.0365  271 PRO B O   
3730 C CB  . PRO B 196 ? 0.4595 0.5098 0.3971 -0.0009 0.1448  0.0508  271 PRO B CB  
3731 C CG  . PRO B 196 ? 0.5685 0.6080 0.4694 0.0113  0.1534  0.0461  271 PRO B CG  
3732 C CD  . PRO B 196 ? 0.6663 0.6794 0.5271 0.0165  0.1316  0.0459  271 PRO B CD  
3733 N N   . ARG B 197 ? 0.4581 0.5283 0.4234 0.0196  0.1001  0.0294  272 ARG B N   
3734 C CA  . ARG B 197 ? 0.3165 0.4046 0.3123 0.0244  0.0863  0.0231  272 ARG B CA  
3735 C C   . ARG B 197 ? 0.4221 0.5010 0.4135 0.0199  0.0653  0.0225  272 ARG B C   
3736 O O   . ARG B 197 ? 0.5278 0.6191 0.5441 0.0170  0.0530  0.0200  272 ARG B O   
3737 C CB  . ARG B 197 ? 0.4280 0.5132 0.4129 0.0385  0.0857  0.0166  272 ARG B CB  
3738 C CG  . ARG B 197 ? 0.5709 0.6638 0.5601 0.0452  0.1088  0.0139  272 ARG B CG  
3739 C CD  . ARG B 197 ? 0.5688 0.6484 0.5375 0.0590  0.1075  0.0058  272 ARG B CD  
3740 N NE  . ARG B 197 ? 0.7386 0.7892 0.6596 0.0581  0.0992  0.0057  272 ARG B NE  
3741 C CZ  . ARG B 197 ? 0.8122 0.8435 0.7043 0.0663  0.0993  -0.0014 272 ARG B CZ  
3742 N NH1 . ARG B 197 ? 0.7892 0.8232 0.6905 0.0776  0.1098  -0.0097 272 ARG B NH1 
3743 N NH2 . ARG B 197 ? 0.7454 0.7537 0.6013 0.0633  0.0875  -0.0008 272 ARG B NH2 
3744 N N   . TYR B 198 ? 0.4339 0.4906 0.3937 0.0197  0.0607  0.0242  273 TYR B N   
3745 C CA  . TYR B 198 ? 0.4933 0.5395 0.4462 0.0175  0.0461  0.0223  273 TYR B CA  
3746 C C   . TYR B 198 ? 0.4504 0.4845 0.4006 0.0084  0.0466  0.0258  273 TYR B C   
3747 O O   . TYR B 198 ? 0.6671 0.6876 0.6068 0.0082  0.0390  0.0236  273 TYR B O   
3748 C CB  . TYR B 198 ? 0.5491 0.5822 0.4788 0.0249  0.0409  0.0207  273 TYR B CB  
3749 C CG  . TYR B 198 ? 0.4585 0.4964 0.3875 0.0335  0.0403  0.0171  273 TYR B CG  
3750 C CD1 . TYR B 198 ? 0.3755 0.4103 0.2927 0.0386  0.0493  0.0165  273 TYR B CD1 
3751 C CD2 . TYR B 198 ? 0.4401 0.4804 0.3755 0.0366  0.0304  0.0143  273 TYR B CD2 
3752 C CE1 . TYR B 198 ? 0.4836 0.5180 0.3993 0.0471  0.0491  0.0114  273 TYR B CE1 
3753 C CE2 . TYR B 198 ? 0.5889 0.6288 0.5242 0.0450  0.0292  0.0117  273 TYR B CE2 
3754 C CZ  . TYR B 198 ? 0.5576 0.5947 0.4851 0.0504  0.0388  0.0094  273 TYR B CZ  
3755 O OH  . TYR B 198 ? 0.7921 0.8242 0.7187 0.0595  0.0380  0.0050  273 TYR B OH  
3756 N N   . MET B 199 ? 0.5258 0.5626 0.4859 0.0008  0.0574  0.0312  274 MET B N   
3757 C CA  . MET B 199 ? 0.3852 0.4044 0.3405 -0.0078 0.0588  0.0361  274 MET B CA  
3758 C C   . MET B 199 ? 0.4834 0.5038 0.4586 -0.0174 0.0491  0.0308  274 MET B C   
3759 O O   . MET B 199 ? 0.5341 0.5748 0.5371 -0.0230 0.0465  0.0279  274 MET B O   
3760 C CB  . MET B 199 ? 0.4673 0.4846 0.4215 -0.0140 0.0758  0.0458  274 MET B CB  
3761 C CG  . MET B 199 ? 0.6427 0.6371 0.5912 -0.0236 0.0778  0.0535  274 MET B CG  
3762 S SD  . MET B 199 ? 0.9337 0.9205 0.8706 -0.0313 0.1009  0.0681  274 MET B SD  
3763 C CE  . MET B 199 ? 0.8977 0.8725 0.7889 -0.0162 0.1015  0.0705  274 MET B CE  
3764 N N   . ALA B 200 ? 0.5287 0.5265 0.4905 -0.0188 0.0427  0.0285  275 ALA B N   
3765 C CA  . ALA B 200 ? 0.5206 0.5104 0.4927 -0.0292 0.0338  0.0219  275 ALA B CA  
3766 C C   . ALA B 200 ? 0.5655 0.5543 0.5584 -0.0438 0.0407  0.0281  275 ALA B C   
3767 O O   . ALA B 200 ? 0.6408 0.6217 0.6275 -0.0446 0.0539  0.0389  275 ALA B O   
3768 C CB  . ALA B 200 ? 0.5240 0.4858 0.4746 -0.0252 0.0297  0.0166  275 ALA B CB  
3769 N N   . PRO B 201 ? 0.5278 0.5225 0.5443 -0.0566 0.0312  0.0221  276 PRO B N   
3770 C CA  . PRO B 201 ? 0.5158 0.5133 0.5607 -0.0734 0.0391  0.0286  276 PRO B CA  
3771 C C   . PRO B 201 ? 0.5879 0.5492 0.6160 -0.0793 0.0460  0.0351  276 PRO B C   
3772 O O   . PRO B 201 ? 0.5982 0.5569 0.6366 -0.0890 0.0609  0.0472  276 PRO B O   
3773 C CB  . PRO B 201 ? 0.4868 0.4956 0.5599 -0.0859 0.0203  0.0182  276 PRO B CB  
3774 C CG  . PRO B 201 ? 0.4863 0.4785 0.5270 -0.0766 0.0032  0.0060  276 PRO B CG  
3775 C CD  . PRO B 201 ? 0.4116 0.4087 0.4283 -0.0578 0.0118  0.0097  276 PRO B CD  
3776 N N   . GLU B 202 ? 0.6066 0.5379 0.6089 -0.0731 0.0373  0.0280  277 GLU B N   
3777 C CA  . GLU B 202 ? 0.5678 0.4613 0.5581 -0.0770 0.0416  0.0334  277 GLU B CA  
3778 C C   . GLU B 202 ? 0.5672 0.4510 0.5378 -0.0666 0.0538  0.0488  277 GLU B C   
3779 O O   . GLU B 202 ? 0.7148 0.5674 0.6767 -0.0701 0.0582  0.0584  277 GLU B O   
3780 C CB  . GLU B 202 ? 0.5501 0.4143 0.5211 -0.0707 0.0309  0.0195  277 GLU B CB  
3781 C CG  . GLU B 202 ? 0.6487 0.5138 0.5974 -0.0500 0.0317  0.0166  277 GLU B CG  
3782 C CD  . GLU B 202 ? 0.7712 0.6626 0.7172 -0.0449 0.0250  0.0072  277 GLU B CD  
3783 O OE1 . GLU B 202 ? 0.8179 0.7298 0.7802 -0.0550 0.0181  0.0044  277 GLU B OE1 
3784 O OE2 . GLU B 202 ? 0.6198 0.5111 0.5498 -0.0308 0.0262  0.0034  277 GLU B OE2 
3785 N N   . LEU B 203 ? 0.5662 0.4721 0.5270 -0.0540 0.0572  0.0514  278 LEU B N   
3786 C CA  . LEU B 203 ? 0.5109 0.4059 0.4482 -0.0450 0.0649  0.0652  278 LEU B CA  
3787 C C   . LEU B 203 ? 0.7034 0.5935 0.6411 -0.0578 0.0806  0.0804  278 LEU B C   
3788 O O   . LEU B 203 ? 0.8540 0.7160 0.7674 -0.0563 0.0849  0.0945  278 LEU B O   
3789 C CB  . LEU B 203 ? 0.5753 0.4933 0.5019 -0.0313 0.0638  0.0625  278 LEU B CB  
3790 C CG  . LEU B 203 ? 0.5658 0.4850 0.4871 -0.0179 0.0521  0.0519  278 LEU B CG  
3791 C CD1 . LEU B 203 ? 0.6768 0.6117 0.5857 -0.0068 0.0515  0.0530  278 LEU B CD1 
3792 C CD2 . LEU B 203 ? 0.7781 0.6677 0.6917 -0.0117 0.0468  0.0535  278 LEU B CD2 
3793 N N   . LEU B 204 ? 0.6573 0.5742 0.6234 -0.0703 0.0896  0.0787  279 LEU B N   
3794 C CA  . LEU B 204 ? 0.6535 0.5678 0.6258 -0.0850 0.1097  0.0932  279 LEU B CA  
3795 C C   . LEU B 204 ? 0.7058 0.5839 0.6796 -0.0992 0.1094  0.1011  279 LEU B C   
3796 O O   . LEU B 204 ? 0.8738 0.7310 0.8331 -0.1080 0.1254  0.1184  279 LEU B O   
3797 C CB  . LEU B 204 ? 0.8078 0.7634 0.8243 -0.0956 0.1191  0.0881  279 LEU B CB  
3798 C CG  . LEU B 204 ? 0.7751 0.7643 0.7933 -0.0822 0.1245  0.0825  279 LEU B CG  
3799 C CD1 . LEU B 204 ? 0.6970 0.7257 0.7677 -0.0927 0.1358  0.0799  279 LEU B CD1 
3800 C CD2 . LEU B 204 ? 0.8700 0.8441 0.8435 -0.0727 0.1402  0.0934  279 LEU B CD2 
3801 N N   . GLN B 205 ? 0.8684 0.7342 0.8552 -0.1019 0.0924  0.0888  280 GLN B N   
3802 C CA  . GLN B 205 ? 0.7002 0.5260 0.6883 -0.1143 0.0896  0.0929  280 GLN B CA  
3803 C C   . GLN B 205 ? 0.7007 0.4847 0.6531 -0.0990 0.0832  0.0992  280 GLN B C   
3804 O O   . GLN B 205 ? 0.9985 0.7445 0.9505 -0.1039 0.0772  0.0987  280 GLN B O   
3805 C CB  . GLN B 205 ? 0.7706 0.5983 0.7857 -0.1244 0.0735  0.0740  280 GLN B CB  
3806 C CG  . GLN B 205 ? 0.8524 0.7248 0.9089 -0.1375 0.0729  0.0669  280 GLN B CG  
3807 C CD  . GLN B 205 ? 1.0109 0.8970 1.0949 -0.1559 0.0943  0.0827  280 GLN B CD  
3808 O OE1 . GLN B 205 ? 0.8669 0.7901 0.9648 -0.1532 0.1084  0.0874  280 GLN B OE1 
3809 N NE2 . GLN B 205 ? 1.0853 0.9395 1.1773 -0.1750 0.0990  0.0910  280 GLN B NE2 
3810 N N   . GLY B 206 ? 0.7455 0.5347 0.6709 -0.0802 0.0826  0.1044  281 GLY B N   
3811 C CA  . GLY B 206 ? 1.0375 0.7920 0.9367 -0.0645 0.0737  0.1116  281 GLY B CA  
3812 C C   . GLY B 206 ? 0.8653 0.6100 0.7725 -0.0520 0.0593  0.0947  281 GLY B C   
3813 O O   . GLY B 206 ? 0.9571 0.6684 0.8545 -0.0408 0.0526  0.0995  281 GLY B O   
3814 N N   . SER B 207 ? 0.6820 0.4533 0.6058 -0.0527 0.0552  0.0755  282 SER B N   
3815 C CA  . SER B 207 ? 0.6066 0.3682 0.5323 -0.0415 0.0461  0.0580  282 SER B CA  
3816 C C   . SER B 207 ? 0.6499 0.4400 0.5705 -0.0242 0.0433  0.0528  282 SER B C   
3817 O O   . SER B 207 ? 0.8356 0.6579 0.7608 -0.0265 0.0434  0.0453  282 SER B O   
3818 C CB  . SER B 207 ? 0.6246 0.3881 0.5634 -0.0557 0.0420  0.0406  282 SER B CB  
3819 O OG  . SER B 207 ? 0.9648 0.7201 0.8961 -0.0442 0.0365  0.0225  282 SER B OG  
3820 N N   . TYR B 208 ? 0.8291 0.6069 0.7436 -0.0069 0.0397  0.0575  283 TYR B N   
3821 C CA  . TYR B 208 ? 0.6561 0.4593 0.5707 0.0081  0.0364  0.0544  283 TYR B CA  
3822 C C   . TYR B 208 ? 0.7885 0.5858 0.7133 0.0201  0.0361  0.0391  283 TYR B C   
3823 O O   . TYR B 208 ? 0.7143 0.4830 0.6447 0.0287  0.0352  0.0392  283 TYR B O   
3824 C CB  . TYR B 208 ? 0.6798 0.4782 0.5842 0.0181  0.0306  0.0715  283 TYR B CB  
3825 C CG  . TYR B 208 ? 0.8080 0.6075 0.6932 0.0070  0.0352  0.0865  283 TYR B CG  
3826 C CD1 . TYR B 208 ? 0.7896 0.5588 0.6645 -0.0034 0.0398  0.1001  283 TYR B CD1 
3827 C CD2 . TYR B 208 ? 0.9026 0.7306 0.7786 0.0065  0.0374  0.0867  283 TYR B CD2 
3828 C CE1 . TYR B 208 ? 0.9341 0.7037 0.7895 -0.0143 0.0493  0.1142  283 TYR B CE1 
3829 C CE2 . TYR B 208 ? 0.8405 0.6681 0.6966 -0.0026 0.0462  0.0987  283 TYR B CE2 
3830 C CZ  . TYR B 208 ? 0.9393 0.7387 0.7848 -0.0132 0.0535  0.1127  283 TYR B CZ  
3831 O OH  . TYR B 208 ? 1.2571 1.0554 1.0810 -0.0229 0.0672  0.1250  283 TYR B OH  
3832 N N   . GLY B 209 ? 0.7190 0.5406 0.6450 0.0212  0.0386  0.0264  284 GLY B N   
3833 C CA  . GLY B 209 ? 0.6447 0.4614 0.5758 0.0315  0.0435  0.0117  284 GLY B CA  
3834 C C   . GLY B 209 ? 0.6110 0.4582 0.5410 0.0341  0.0462  0.0054  284 GLY B C   
3835 O O   . GLY B 209 ? 0.6503 0.5207 0.5766 0.0286  0.0424  0.0114  284 GLY B O   
3836 N N   . THR B 210 ? 0.7206 0.5648 0.6531 0.0426  0.0550  -0.0069 285 THR B N   
3837 C CA  . THR B 210 ? 0.4610 0.3292 0.3906 0.0440  0.0600  -0.0118 285 THR B CA  
3838 C C   . THR B 210 ? 0.5370 0.4112 0.4440 0.0307  0.0560  -0.0163 285 THR B C   
3839 O O   . THR B 210 ? 0.6091 0.5043 0.5125 0.0297  0.0554  -0.0146 285 THR B O   
3840 C CB  . THR B 210 ? 0.4990 0.3590 0.4328 0.0542  0.0753  -0.0242 285 THR B CB  
3841 O OG1 . THR B 210 ? 0.6778 0.5062 0.5896 0.0502  0.0805  -0.0380 285 THR B OG1 
3842 C CG2 . THR B 210 ? 0.5727 0.4345 0.5409 0.0698  0.0776  -0.0190 285 THR B CG2 
3843 N N   . ALA B 211 ? 0.6276 0.4830 0.5223 0.0203  0.0513  -0.0217 286 ALA B N   
3844 C CA  . ALA B 211 ? 0.5037 0.3665 0.3834 0.0079  0.0428  -0.0256 286 ALA B CA  
3845 C C   . ALA B 211 ? 0.6053 0.4969 0.4976 0.0039  0.0362  -0.0133 286 ALA B C   
3846 O O   . ALA B 211 ? 0.5846 0.4902 0.4711 -0.0014 0.0296  -0.0150 286 ALA B O   
3847 C CB  . ALA B 211 ? 0.5585 0.3967 0.4308 -0.0042 0.0358  -0.0334 286 ALA B CB  
3848 N N   . ALA B 212 ? 0.5862 0.4840 0.4929 0.0074  0.0375  -0.0013 287 ALA B N   
3849 C CA  . ALA B 212 ? 0.5111 0.4321 0.4245 0.0044  0.0348  0.0085  287 ALA B CA  
3850 C C   . ALA B 212 ? 0.4767 0.4176 0.3870 0.0109  0.0345  0.0080  287 ALA B C   
3851 O O   . ALA B 212 ? 0.6717 0.6298 0.5842 0.0080  0.0316  0.0103  287 ALA B O   
3852 C CB  . ALA B 212 ? 0.5167 0.4327 0.4345 0.0071  0.0368  0.0213  287 ALA B CB  
3853 N N   . ASP B 213 ? 0.6999 0.6383 0.6089 0.0196  0.0386  0.0049  288 ASP B N   
3854 C CA  . ASP B 213 ? 0.4729 0.4271 0.3807 0.0236  0.0390  0.0053  288 ASP B CA  
3855 C C   . ASP B 213 ? 0.5293 0.4835 0.4217 0.0192  0.0377  -0.0013 288 ASP B C   
3856 O O   . ASP B 213 ? 0.6308 0.5972 0.5209 0.0191  0.0339  0.0013  288 ASP B O   
3857 C CB  . ASP B 213 ? 0.5877 0.5420 0.5066 0.0324  0.0449  0.0050  288 ASP B CB  
3858 C CG  . ASP B 213 ? 0.7052 0.6619 0.6387 0.0380  0.0396  0.0136  288 ASP B CG  
3859 O OD1 . ASP B 213 ? 0.5510 0.5108 0.4781 0.0352  0.0333  0.0206  288 ASP B OD1 
3860 O OD2 . ASP B 213 ? 0.7717 0.7264 0.7224 0.0459  0.0417  0.0136  288 ASP B OD2 
3861 N N   . VAL B 214 ? 0.5632 0.4997 0.4413 0.0159  0.0396  -0.0100 289 VAL B N   
3862 C CA  . VAL B 214 ? 0.4813 0.4120 0.3358 0.0113  0.0348  -0.0157 289 VAL B CA  
3863 C C   . VAL B 214 ? 0.5247 0.4688 0.3855 0.0052  0.0202  -0.0122 289 VAL B C   
3864 O O   . VAL B 214 ? 0.6141 0.5633 0.4649 0.0050  0.0128  -0.0110 289 VAL B O   
3865 C CB  . VAL B 214 ? 0.6140 0.5175 0.4452 0.0083  0.0380  -0.0276 289 VAL B CB  
3866 C CG1 . VAL B 214 ? 0.5555 0.4483 0.3539 0.0025  0.0282  -0.0328 289 VAL B CG1 
3867 C CG2 . VAL B 214 ? 0.6067 0.5000 0.4366 0.0169  0.0567  -0.0319 289 VAL B CG2 
3868 N N   . PHE B 215 ? 0.5307 0.4805 0.4110 0.0003  0.0168  -0.0096 290 PHE B N   
3869 C CA  . PHE B 215 ? 0.4699 0.4380 0.3669 -0.0051 0.0065  -0.0063 290 PHE B CA  
3870 C C   . PHE B 215 ? 0.4759 0.4643 0.3837 0.0021  0.0093  0.0011  290 PHE B C   
3871 O O   . PHE B 215 ? 0.6016 0.6022 0.5146 0.0032  0.0009  0.0019  290 PHE B O   
3872 C CB  . PHE B 215 ? 0.5254 0.4946 0.4431 -0.0138 0.0072  -0.0043 290 PHE B CB  
3873 C CG  . PHE B 215 ? 0.5139 0.5037 0.4568 -0.0216 -0.0022 -0.0029 290 PHE B CG  
3874 C CD1 . PHE B 215 ? 0.5590 0.5734 0.5244 -0.0182 0.0041  0.0048  290 PHE B CD1 
3875 C CD2 . PHE B 215 ? 0.4597 0.4444 0.4058 -0.0321 -0.0175 -0.0101 290 PHE B CD2 
3876 C CE1 . PHE B 215 ? 0.3714 0.4091 0.3693 -0.0241 -0.0018 0.0058  290 PHE B CE1 
3877 C CE2 . PHE B 215 ? 0.4561 0.4648 0.4360 -0.0394 -0.0280 -0.0085 290 PHE B CE2 
3878 C CZ  . PHE B 215 ? 0.4569 0.4943 0.4665 -0.0348 -0.0188 -0.0003 290 PHE B CZ  
3879 N N   . SER B 216 ? 0.4198 0.4095 0.3303 0.0077  0.0192  0.0061  291 SER B N   
3880 C CA  . SER B 216 ? 0.3208 0.3238 0.2356 0.0141  0.0213  0.0107  291 SER B CA  
3881 C C   . SER B 216 ? 0.4801 0.4817 0.3835 0.0185  0.0173  0.0091  291 SER B C   
3882 O O   . SER B 216 ? 0.4848 0.4955 0.3928 0.0225  0.0144  0.0110  291 SER B O   
3883 C CB  . SER B 216 ? 0.4062 0.4052 0.3191 0.0183  0.0279  0.0152  291 SER B CB  
3884 O OG  . SER B 216 ? 0.6023 0.5974 0.5201 0.0140  0.0318  0.0194  291 SER B OG  
3885 N N   . LEU B 217 ? 0.4845 0.4724 0.3722 0.0180  0.0192  0.0057  292 LEU B N   
3886 C CA  . LEU B 217 ? 0.4384 0.4208 0.3109 0.0200  0.0178  0.0061  292 LEU B CA  
3887 C C   . LEU B 217 ? 0.4543 0.4349 0.3174 0.0179  0.0047  0.0056  292 LEU B C   
3888 O O   . LEU B 217 ? 0.6885 0.6671 0.5437 0.0211  -0.0005 0.0093  292 LEU B O   
3889 C CB  . LEU B 217 ? 0.4492 0.4170 0.3065 0.0194  0.0281  0.0029  292 LEU B CB  
3890 C CG  . LEU B 217 ? 0.5024 0.4625 0.3435 0.0199  0.0322  0.0057  292 LEU B CG  
3891 C CD1 . LEU B 217 ? 0.5870 0.5582 0.4453 0.0230  0.0314  0.0112  292 LEU B CD1 
3892 C CD2 . LEU B 217 ? 0.6299 0.5784 0.4609 0.0191  0.0485  0.0022  292 LEU B CD2 
3893 N N   . GLY B 218 ? 0.5214 0.5014 0.3868 0.0122  -0.0032 0.0015  293 GLY B N   
3894 C CA  . GLY B 218 ? 0.3939 0.3750 0.2560 0.0100  -0.0211 0.0011  293 GLY B CA  
3895 C C   . GLY B 218 ? 0.5143 0.5182 0.4067 0.0153  -0.0274 0.0062  293 GLY B C   
3896 O O   . GLY B 218 ? 0.5544 0.5581 0.4437 0.0196  -0.0404 0.0092  293 GLY B O   
3897 N N   . LEU B 219 ? 0.4686 0.4897 0.3887 0.0160  -0.0175 0.0073  294 LEU B N   
3898 C CA  . LEU B 219 ? 0.4610 0.5024 0.4086 0.0228  -0.0172 0.0104  294 LEU B CA  
3899 C C   . LEU B 219 ? 0.4319 0.4663 0.3674 0.0322  -0.0125 0.0129  294 LEU B C   
3900 O O   . LEU B 219 ? 0.5048 0.5464 0.4535 0.0401  -0.0177 0.0145  294 LEU B O   
3901 C CB  . LEU B 219 ? 0.4000 0.4564 0.3713 0.0200  -0.0037 0.0110  294 LEU B CB  
3902 C CG  . LEU B 219 ? 0.4531 0.5177 0.4448 0.0087  -0.0075 0.0095  294 LEU B CG  
3903 C CD1 . LEU B 219 ? 0.5281 0.6031 0.5377 0.0053  0.0102  0.0129  294 LEU B CD1 
3904 C CD2 . LEU B 219 ? 0.3210 0.4030 0.3405 0.0079  -0.0250 0.0084  294 LEU B CD2 
3905 N N   . THR B 220 ? 0.5111 0.5315 0.4259 0.0315  -0.0033 0.0130  295 THR B N   
3906 C CA  . THR B 220 ? 0.5033 0.5145 0.4077 0.0372  -0.0008 0.0150  295 THR B CA  
3907 C C   . THR B 220 ? 0.5308 0.5297 0.4212 0.0394  -0.0119 0.0183  295 THR B C   
3908 O O   . THR B 220 ? 0.6527 0.6490 0.5474 0.0465  -0.0159 0.0206  295 THR B O   
3909 C CB  . THR B 220 ? 0.5397 0.5413 0.4319 0.0339  0.0084  0.0147  295 THR B CB  
3910 O OG1 . THR B 220 ? 0.5514 0.5604 0.4530 0.0337  0.0151  0.0138  295 THR B OG1 
3911 C CG2 . THR B 220 ? 0.4846 0.4759 0.3691 0.0363  0.0093  0.0168  295 THR B CG2 
3912 N N   . ILE B 221 ? 0.5654 0.5521 0.4344 0.0336  -0.0170 0.0185  296 ILE B N   
3913 C CA  . ILE B 221 ? 0.4610 0.4302 0.3066 0.0349  -0.0290 0.0234  296 ILE B CA  
3914 C C   . ILE B 221 ? 0.5104 0.4909 0.3757 0.0411  -0.0476 0.0253  296 ILE B C   
3915 O O   . ILE B 221 ? 0.6761 0.6471 0.5374 0.0482  -0.0577 0.0313  296 ILE B O   
3916 C CB  . ILE B 221 ? 0.5864 0.5365 0.3967 0.0270  -0.0290 0.0217  296 ILE B CB  
3917 C CG1 . ILE B 221 ? 0.6961 0.6373 0.4945 0.0233  -0.0079 0.0204  296 ILE B CG1 
3918 C CG2 . ILE B 221 ? 0.6415 0.5697 0.4190 0.0277  -0.0447 0.0279  296 ILE B CG2 
3919 C CD1 . ILE B 221 ? 0.7122 0.6459 0.5086 0.0251  -0.0004 0.0269  296 ILE B CD1 
3920 N N   . LEU B 222 ? 0.6284 0.6293 0.5196 0.0385  -0.0528 0.0209  297 LEU B N   
3921 C CA  . LEU B 222 ? 0.5288 0.5474 0.4514 0.0443  -0.0704 0.0223  297 LEU B CA  
3922 C C   . LEU B 222 ? 0.6414 0.6739 0.5946 0.0566  -0.0632 0.0236  297 LEU B C   
3923 O O   . LEU B 222 ? 0.6871 0.7265 0.6617 0.0663  -0.0776 0.0267  297 LEU B O   
3924 C CB  . LEU B 222 ? 0.5359 0.5757 0.4869 0.0361  -0.0742 0.0171  297 LEU B CB  
3925 C CG  . LEU B 222 ? 0.5374 0.6008 0.5301 0.0390  -0.0950 0.0179  297 LEU B CG  
3926 C CD1 . LEU B 222 ? 0.4982 0.5425 0.4647 0.0415  -0.1235 0.0224  297 LEU B CD1 
3927 C CD2 . LEU B 222 ? 0.5610 0.6433 0.5823 0.0265  -0.0964 0.0126  297 LEU B CD2 
3928 N N   . GLU B 223 ? 0.7191 0.7534 0.6734 0.0572  -0.0423 0.0207  298 GLU B N   
3929 C CA  . GLU B 223 ? 0.6238 0.6648 0.5982 0.0689  -0.0338 0.0193  298 GLU B CA  
3930 C C   . GLU B 223 ? 0.5705 0.5869 0.5257 0.0766  -0.0404 0.0235  298 GLU B C   
3931 O O   . GLU B 223 ? 0.6624 0.6806 0.6376 0.0892  -0.0452 0.0239  298 GLU B O   
3932 C CB  . GLU B 223 ? 0.5906 0.6343 0.5614 0.0662  -0.0128 0.0147  298 GLU B CB  
3933 C CG  . GLU B 223 ? 0.6201 0.6611 0.5973 0.0774  -0.0027 0.0108  298 GLU B CG  
3934 C CD  . GLU B 223 ? 0.8242 0.8623 0.7873 0.0739  0.0140  0.0065  298 GLU B CD  
3935 O OE1 . GLU B 223 ? 0.7452 0.7865 0.7003 0.0640  0.0178  0.0080  298 GLU B OE1 
3936 O OE2 . GLU B 223 ? 0.9865 1.0157 0.9438 0.0816  0.0220  0.0014  298 GLU B OE2 
3937 N N   . VAL B 224 ? 0.5983 0.5909 0.5177 0.0692  -0.0391 0.0268  299 VAL B N   
3938 C CA  . VAL B 224 ? 0.4742 0.4402 0.3746 0.0734  -0.0425 0.0321  299 VAL B CA  
3939 C C   . VAL B 224 ? 0.4698 0.4183 0.3528 0.0755  -0.0619 0.0415  299 VAL B C   
3940 O O   . VAL B 224 ? 0.7123 0.6391 0.5875 0.0826  -0.0687 0.0478  299 VAL B O   
3941 C CB  . VAL B 224 ? 0.4972 0.4472 0.3731 0.0633  -0.0297 0.0324  299 VAL B CB  
3942 C CG1 . VAL B 224 ? 0.4717 0.4373 0.3604 0.0607  -0.0161 0.0243  299 VAL B CG1 
3943 C CG2 . VAL B 224 ? 0.5714 0.5119 0.4201 0.0528  -0.0299 0.0366  299 VAL B CG2 
3944 N N   . ALA B 225 ? 0.5348 0.4877 0.4073 0.0693  -0.0727 0.0428  300 ALA B N   
3945 C CA  . ALA B 225 ? 0.4959 0.4288 0.3443 0.0712  -0.0952 0.0520  300 ALA B CA  
3946 C C   . ALA B 225 ? 0.4790 0.4280 0.3650 0.0846  -0.1169 0.0539  300 ALA B C   
3947 O O   . ALA B 225 ? 0.6363 0.5652 0.5062 0.0907  -0.1392 0.0637  300 ALA B O   
3948 C CB  . ALA B 225 ? 0.6489 0.5752 0.4654 0.0592  -0.1007 0.0507  300 ALA B CB  
3949 N N   . CYS B 226 ? 0.6295 0.6139 0.5660 0.0896  -0.1107 0.0457  301 CYS B N   
3950 C CA  . CYS B 226 ? 0.5651 0.5726 0.5506 0.1030  -0.1276 0.0464  301 CYS B CA  
3951 C C   . CYS B 226 ? 0.6008 0.6220 0.6250 0.1172  -0.1105 0.0410  301 CYS B C   
3952 O O   . CYS B 226 ? 0.8007 0.8419 0.8722 0.1315  -0.1202 0.0408  301 CYS B O   
3953 C CB  . CYS B 226 ? 0.7365 0.7774 0.7550 0.0954  -0.1357 0.0411  301 CYS B CB  
3954 S SG  . CYS B 226 ? 0.8566 0.8773 0.8239 0.0775  -0.1533 0.0425  301 CYS B SG  
3955 N N   . ASN B 227 ? 0.5441 0.5542 0.5499 0.1140  -0.0862 0.0358  302 ASN B N   
3956 C CA  . ASN B 227 ? 0.6137 0.6285 0.6431 0.1263  -0.0685 0.0283  302 ASN B CA  
3957 C C   . ASN B 227 ? 0.6669 0.7224 0.7488 0.1318  -0.0582 0.0209  302 ASN B C   
3958 O O   . ASN B 227 ? 0.6587 0.7252 0.7777 0.1483  -0.0533 0.0169  302 ASN B O   
3959 C CB  . ASN B 227 ? 0.6359 0.6258 0.6670 0.1425  -0.0797 0.0329  302 ASN B CB  
3960 C CG  . ASN B 227 ? 0.6898 0.6707 0.7281 0.1530  -0.0596 0.0229  302 ASN B CG  
3961 O OD1 . ASN B 227 ? 0.6921 0.6738 0.7149 0.1446  -0.0396 0.0147  302 ASN B OD1 
3962 N ND2 . ASN B 227 ? 0.6494 0.6189 0.7093 0.1721  -0.0663 0.0231  302 ASN B ND2 
3963 N N   . MET B 228 ? 0.5545 0.6313 0.6413 0.1179  -0.0529 0.0192  303 MET B N   
3964 C CA  . MET B 228 ? 0.7511 0.8661 0.8872 0.1188  -0.0400 0.0139  303 MET B CA  
3965 C C   . MET B 228 ? 0.6382 0.7535 0.7565 0.1105  -0.0113 0.0078  303 MET B C   
3966 O O   . MET B 228 ? 0.5920 0.6851 0.6659 0.1003  -0.0081 0.0085  303 MET B O   
3967 C CB  . MET B 228 ? 0.7291 0.8674 0.8900 0.1080  -0.0584 0.0174  303 MET B CB  
3968 C CG  . MET B 228 ? 0.6866 0.8170 0.8136 0.0881  -0.0546 0.0172  303 MET B CG  
3969 S SD  . MET B 228 ? 0.8938 1.0532 1.0590 0.0744  -0.0717 0.0174  303 MET B SD  
3970 C CE  . MET B 228 ? 0.7413 0.9468 0.9830 0.0813  -0.0510 0.0139  303 MET B CE  
3971 N N   . GLU B 229 ? 0.5980 0.7383 0.7521 0.1156  0.0099  0.0025  304 GLU B N   
3972 C CA  . GLU B 229 ? 0.4588 0.5978 0.5931 0.1081  0.0370  -0.0018 304 GLU B CA  
3973 C C   . GLU B 229 ? 0.6887 0.8474 0.8362 0.0911  0.0394  0.0021  304 GLU B C   
3974 O O   . GLU B 229 ? 0.6029 0.7898 0.7973 0.0883  0.0304  0.0043  304 GLU B O   
3975 C CB  . GLU B 229 ? 0.5861 0.7359 0.7428 0.1217  0.0635  -0.0096 304 GLU B CB  
3976 C CG  . GLU B 229 ? 1.1330 1.2781 1.2624 0.1138  0.0921  -0.0127 304 GLU B CG  
3977 C CD  . GLU B 229 ? 1.3251 1.4809 1.4743 0.1267  0.1227  -0.0211 304 GLU B CD  
3978 O OE1 . GLU B 229 ? 1.5117 1.6605 1.6720 0.1447  0.1230  -0.0281 304 GLU B OE1 
3979 O OE2 . GLU B 229 ? 1.2835 1.4521 1.4357 0.1190  0.1481  -0.0204 304 GLU B OE2 
3980 N N   . LEU B 230 ? 0.6152 0.7574 0.7233 0.0795  0.0494  0.0030  305 LEU B N   
3981 C CA  . LEU B 230 ? 0.3402 0.4933 0.4558 0.0632  0.0519  0.0071  305 LEU B CA  
3982 C C   . LEU B 230 ? 0.5845 0.7539 0.7185 0.0605  0.0810  0.0069  305 LEU B C   
3983 O O   . LEU B 230 ? 0.6153 0.7705 0.7209 0.0665  0.1007  0.0040  305 LEU B O   
3984 C CB  . LEU B 230 ? 0.4180 0.5437 0.4852 0.0533  0.0468  0.0095  305 LEU B CB  
3985 C CG  . LEU B 230 ? 0.2940 0.4036 0.3417 0.0524  0.0231  0.0104  305 LEU B CG  
3986 C CD1 . LEU B 230 ? 0.4052 0.4932 0.4157 0.0433  0.0230  0.0120  305 LEU B CD1 
3987 C CD2 . LEU B 230 ? 0.3514 0.4770 0.4292 0.0481  0.0042  0.0116  305 LEU B CD2 
3988 N N   . PRO B 231 ? 0.3692 0.5660 0.5478 0.0504  0.0848  0.0100  306 PRO B N   
3989 C CA  . PRO B 231 ? 0.4088 0.6215 0.6071 0.0462  0.1169  0.0115  306 PRO B CA  
3990 C C   . PRO B 231 ? 0.3841 0.5710 0.5337 0.0338  0.1306  0.0170  306 PRO B C   
3991 O O   . PRO B 231 ? 0.4320 0.5998 0.5552 0.0244  0.1137  0.0204  306 PRO B O   
3992 C CB  . PRO B 231 ? 0.3355 0.5859 0.6030 0.0362  0.1112  0.0140  306 PRO B CB  
3993 C CG  . PRO B 231 ? 0.4218 0.6617 0.6799 0.0280  0.0757  0.0150  306 PRO B CG  
3994 C CD  . PRO B 231 ? 0.4083 0.6217 0.6222 0.0417  0.0593  0.0119  306 PRO B CD  
3995 N N   . HIS B 232 ? 0.6026 0.7866 0.7385 0.0351  0.1621  0.0179  307 HIS B N   
3996 C CA  . HIS B 232 ? 0.5065 0.6634 0.5937 0.0243  0.1753  0.0255  307 HIS B CA  
3997 C C   . HIS B 232 ? 0.5584 0.7277 0.6755 0.0051  0.1840  0.0348  307 HIS B C   
3998 O O   . HIS B 232 ? 0.5335 0.6771 0.6150 -0.0059 0.1837  0.0430  307 HIS B O   
3999 C CB  . HIS B 232 ? 0.7014 0.8432 0.7506 0.0322  0.2054  0.0234  307 HIS B CB  
4000 C CG  . HIS B 232 ? 0.8505 0.9684 0.8568 0.0477  0.1957  0.0142  307 HIS B CG  
4001 N ND1 . HIS B 232 ? 0.9091 1.0360 0.9314 0.0641  0.2038  0.0032  307 HIS B ND1 
4002 C CD2 . HIS B 232 ? 0.7779 0.8626 0.7294 0.0488  0.1781  0.0140  307 HIS B CD2 
4003 C CE1 . HIS B 232 ? 0.8929 0.9901 0.8686 0.0730  0.1912  -0.0035 307 HIS B CE1 
4004 N NE2 . HIS B 232 ? 0.9012 0.9749 0.8360 0.0633  0.1752  0.0030  307 HIS B NE2 
4005 N N   . GLY B 233 ? 0.4895 0.6970 0.6743 0.0008  0.1905  0.0341  308 GLY B N   
4006 C CA  . GLY B 233 ? 0.4549 0.6752 0.6744 -0.0198 0.1997  0.0426  308 GLY B CA  
4007 C C   . GLY B 233 ? 0.4454 0.7144 0.7515 -0.0229 0.1992  0.0395  308 GLY B C   
4008 O O   . GLY B 233 ? 0.6135 0.9031 0.9503 -0.0086 0.1820  0.0314  308 GLY B O   
4009 N N   . GLY B 234 ? 0.3543 0.6408 0.7019 -0.0422 0.2167  0.0470  309 GLY B N   
4010 C CA  . GLY B 234 ? 0.5174 0.8555 0.9581 -0.0471 0.2166  0.0447  309 GLY B CA  
4011 C C   . GLY B 234 ? 0.3963 0.7451 0.8699 -0.0525 0.1700  0.0398  309 GLY B C   
4012 O O   . GLY B 234 ? 0.4251 0.7399 0.8509 -0.0577 0.1436  0.0392  309 GLY B O   
4013 N N   . GLU B 235 ? 0.3572 0.7536 0.9139 -0.0503 0.1601  0.0357  310 GLU B N   
4014 C CA  . GLU B 235 ? 0.3775 0.7855 0.9688 -0.0577 0.1139  0.0314  310 GLU B CA  
4015 C C   . GLU B 235 ? 0.3774 0.7563 0.9122 -0.0408 0.0795  0.0252  310 GLU B C   
4016 O O   . GLU B 235 ? 0.4991 0.8555 1.0070 -0.0500 0.0464  0.0229  310 GLU B O   
4017 C CB  . GLU B 235 ? 0.3671 0.8265 1.0471 -0.0561 0.1054  0.0283  310 GLU B CB  
4018 C CG  . GLU B 235 ? 0.7706 1.2458 1.4933 -0.0820 0.1093  0.0319  310 GLU B CG  
4019 C CD  . GLU B 235 ? 1.0038 1.4601 1.7215 -0.1051 0.0760  0.0317  310 GLU B CD  
4020 O OE1 . GLU B 235 ? 1.0005 1.4455 1.7030 -0.0996 0.0379  0.0264  310 GLU B OE1 
4021 O OE2 . GLU B 235 ? 0.9417 1.3904 1.6661 -0.1289 0.0873  0.0364  310 GLU B OE2 
4022 N N   . GLY B 236 ? 0.2889 0.6653 0.8035 -0.0168 0.0882  0.0222  311 GLY B N   
4023 C CA  . GLY B 236 ? 0.3271 0.6742 0.7886 -0.0023 0.0591  0.0181  311 GLY B CA  
4024 C C   . GLY B 236 ? 0.3313 0.6305 0.7128 -0.0105 0.0534  0.0193  311 GLY B C   
4025 O O   . GLY B 236 ? 0.4748 0.7517 0.8222 -0.0090 0.0235  0.0166  311 GLY B O   
4026 N N   . TRP B 237 ? 0.4324 0.7143 0.7830 -0.0185 0.0826  0.0240  312 TRP B N   
4027 C CA  . TRP B 237 ? 0.3995 0.6389 0.6847 -0.0261 0.0774  0.0260  312 TRP B CA  
4028 C C   . TRP B 237 ? 0.3860 0.6192 0.6824 -0.0449 0.0540  0.0252  312 TRP B C   
4029 O O   . TRP B 237 ? 0.4135 0.6156 0.6647 -0.0458 0.0349  0.0221  312 TRP B O   
4030 C CB  . TRP B 237 ? 0.4143 0.6369 0.6685 -0.0303 0.1113  0.0331  312 TRP B CB  
4031 C CG  . TRP B 237 ? 0.3027 0.4822 0.4908 -0.0323 0.1066  0.0358  312 TRP B CG  
4032 C CD1 . TRP B 237 ? 0.3822 0.5370 0.5172 -0.0186 0.1057  0.0343  312 TRP B CD1 
4033 C CD2 . TRP B 237 ? 0.2838 0.4404 0.4576 -0.0485 0.1016  0.0403  312 TRP B CD2 
4034 N NE1 . TRP B 237 ? 0.3237 0.4459 0.4171 -0.0243 0.1001  0.0380  312 TRP B NE1 
4035 C CE2 . TRP B 237 ? 0.3852 0.5060 0.4997 -0.0415 0.0980  0.0416  312 TRP B CE2 
4036 C CE3 . TRP B 237 ? 0.3623 0.5241 0.5708 -0.0684 0.0987  0.0429  312 TRP B CE3 
4037 C CZ2 . TRP B 237 ? 0.3385 0.4288 0.4282 -0.0510 0.0930  0.0455  312 TRP B CZ2 
4038 C CZ3 . TRP B 237 ? 0.3103 0.4371 0.4886 -0.0793 0.0937  0.0463  312 TRP B CZ3 
4039 C CH2 . TRP B 237 ? 0.4078 0.4994 0.5276 -0.0692 0.0914  0.0476  312 TRP B CH2 
4040 N N   . GLN B 238 ? 0.3983 0.6602 0.7563 -0.0604 0.0561  0.0270  313 GLN B N   
4041 C CA  . GLN B 238 ? 0.3317 0.5846 0.7013 -0.0806 0.0330  0.0246  313 GLN B CA  
4042 C C   . GLN B 238 ? 0.3973 0.6505 0.7673 -0.0765 -0.0082 0.0159  313 GLN B C   
4043 O O   . GLN B 238 ? 0.4929 0.7136 0.8233 -0.0839 -0.0293 0.0107  313 GLN B O   
4044 C CB  . GLN B 238 ? 0.3753 0.6612 0.8176 -0.1004 0.0455  0.0289  313 GLN B CB  
4045 C CG  . GLN B 238 ? 0.3077 0.5929 0.7484 -0.1058 0.0899  0.0396  313 GLN B CG  
4046 C CD  . GLN B 238 ? 0.4945 0.7322 0.8794 -0.1181 0.0974  0.0455  313 GLN B CD  
4047 O OE1 . GLN B 238 ? 0.5406 0.7483 0.8950 -0.1231 0.0713  0.0401  313 GLN B OE1 
4048 N NE2 . GLN B 238 ? 0.6833 0.9113 1.0525 -0.1221 0.1336  0.0568  313 GLN B NE2 
4049 N N   . GLN B 239 ? 0.3573 0.6437 0.7689 -0.0637 -0.0199 0.0142  314 GLN B N   
4050 C CA  . GLN B 239 ? 0.4454 0.7311 0.8573 -0.0602 -0.0620 0.0082  314 GLN B CA  
4051 C C   . GLN B 239 ? 0.3801 0.6205 0.7090 -0.0502 -0.0743 0.0051  314 GLN B C   
4052 O O   . GLN B 239 ? 0.5905 0.8109 0.8932 -0.0553 -0.1059 -0.0003 314 GLN B O   
4053 C CB  . GLN B 239 ? 0.3880 0.7150 0.8588 -0.0443 -0.0705 0.0093  314 GLN B CB  
4054 C CG  . GLN B 239 ? 0.4783 0.8572 1.0447 -0.0541 -0.0603 0.0114  314 GLN B CG  
4055 C CD  . GLN B 239 ? 0.6850 1.1058 1.3146 -0.0342 -0.0658 0.0120  314 GLN B CD  
4056 O OE1 . GLN B 239 ? 0.6235 1.0306 1.2200 -0.0120 -0.0705 0.0118  314 GLN B OE1 
4057 N NE2 . GLN B 239 ? 0.7406 1.2092 1.4590 -0.0417 -0.0642 0.0127  314 GLN B NE2 
4058 N N   . LEU B 240 ? 0.4352 0.6584 0.7215 -0.0371 -0.0495 0.0082  315 LEU B N   
4059 C CA  . LEU B 240 ? 0.3717 0.5550 0.5864 -0.0295 -0.0564 0.0060  315 LEU B CA  
4060 C C   . LEU B 240 ? 0.5232 0.6727 0.6973 -0.0430 -0.0552 0.0028  315 LEU B C   
4061 O O   . LEU B 240 ? 0.5606 0.6784 0.6800 -0.0377 -0.0585 0.0002  315 LEU B O   
4062 C CB  . LEU B 240 ? 0.3351 0.5117 0.5234 -0.0132 -0.0324 0.0097  315 LEU B CB  
4063 C CG  . LEU B 240 ? 0.2871 0.4809 0.4941 0.0050  -0.0358 0.0107  315 LEU B CG  
4064 C CD1 . LEU B 240 ? 0.3375 0.5183 0.5135 0.0175  -0.0114 0.0123  315 LEU B CD1 
4065 C CD2 . LEU B 240 ? 0.4810 0.6598 0.6652 0.0104  -0.0677 0.0095  315 LEU B CD2 
4066 N N   . ARG B 241 ? 0.4556 0.6099 0.6573 -0.0601 -0.0489 0.0031  316 ARG B N   
4067 C CA  . ARG B 241 ? 0.3881 0.5069 0.5545 -0.0717 -0.0456 0.0003  316 ARG B CA  
4068 C C   . ARG B 241 ? 0.4471 0.5643 0.6397 -0.0922 -0.0659 -0.0059 316 ARG B C   
4069 O O   . ARG B 241 ? 0.5233 0.6220 0.7147 -0.1063 -0.0569 -0.0057 316 ARG B O   
4070 C CB  . ARG B 241 ? 0.3569 0.4692 0.5174 -0.0723 -0.0137 0.0087  316 ARG B CB  
4071 C CG  . ARG B 241 ? 0.4273 0.5307 0.5499 -0.0538 0.0010  0.0123  316 ARG B CG  
4072 C CD  . ARG B 241 ? 0.3876 0.4948 0.5121 -0.0523 0.0298  0.0218  316 ARG B CD  
4073 N NE  . ARG B 241 ? 0.3875 0.4833 0.4737 -0.0360 0.0382  0.0234  316 ARG B NE  
4074 C CZ  . ARG B 241 ? 0.3811 0.4934 0.4716 -0.0227 0.0410  0.0226  316 ARG B CZ  
4075 N NH1 . ARG B 241 ? 0.4187 0.5611 0.5516 -0.0210 0.0366  0.0206  316 ARG B NH1 
4076 N NH2 . ARG B 241 ? 0.4128 0.5106 0.4677 -0.0108 0.0470  0.0233  316 ARG B NH2 
4077 N N   . GLN B 242 ? 0.6596 0.7937 0.8761 -0.0945 -0.0959 -0.0112 317 GLN B N   
4078 C CA  . GLN B 242 ? 0.5460 0.6763 0.7843 -0.1148 -0.1229 -0.0192 317 GLN B CA  
4079 C C   . GLN B 242 ? 0.4608 0.5512 0.6382 -0.1150 -0.1518 -0.0310 317 GLN B C   
4080 O O   . GLN B 242 ? 0.6456 0.7232 0.8273 -0.1321 -0.1776 -0.0406 317 GLN B O   
4081 C CB  . GLN B 242 ? 0.6434 0.8233 0.9595 -0.1198 -0.1407 -0.0171 317 GLN B CB  
4082 C CG  . GLN B 242 ? 0.6388 0.8610 1.0189 -0.1194 -0.1085 -0.0065 317 GLN B CG  
4083 C CD  . GLN B 242 ? 0.6084 0.8267 1.0138 -0.1417 -0.0887 -0.0034 317 GLN B CD  
4084 O OE1 . GLN B 242 ? 0.7642 1.0026 1.2274 -0.1620 -0.1030 -0.0056 317 GLN B OE1 
4085 N NE2 . GLN B 242 ? 0.7387 0.9297 1.1021 -0.1389 -0.0572 0.0025  317 GLN B NE2 
4086 N N   . GLY B 243 ? 0.5269 0.5957 0.6464 -0.0975 -0.1475 -0.0310 318 GLY B N   
4087 C CA  . GLY B 243 ? 0.7993 0.8282 0.8540 -0.0965 -0.1689 -0.0413 318 GLY B CA  
4088 C C   . GLY B 243 ? 0.8928 0.9290 0.9359 -0.0868 -0.1969 -0.0399 318 GLY B C   
4089 O O   . GLY B 243 ? 1.1018 1.1010 1.0796 -0.0839 -0.2106 -0.0462 318 GLY B O   
4090 N N   . TYR B 244 ? 0.9050 0.9850 1.0075 -0.0809 -0.2045 -0.0314 319 TYR B N   
4091 C CA  . TYR B 244 ? 0.7928 0.8797 0.8902 -0.0694 -0.2332 -0.0277 319 TYR B CA  
4092 C C   . TYR B 244 ? 0.8745 0.9784 0.9792 -0.0484 -0.2116 -0.0167 319 TYR B C   
4093 O O   . TYR B 244 ? 0.9390 1.0637 1.0746 -0.0442 -0.1793 -0.0120 319 TYR B O   
4094 C CB  . TYR B 244 ? 0.6418 0.7651 0.8088 -0.0782 -0.2678 -0.0281 319 TYR B CB  
4095 C CG  . TYR B 244 ? 0.8694 1.0464 1.1298 -0.0808 -0.2482 -0.0222 319 TYR B CG  
4096 C CD1 . TYR B 244 ? 0.9201 1.1299 1.2184 -0.0622 -0.2286 -0.0126 319 TYR B CD1 
4097 C CD2 . TYR B 244 ? 0.8777 1.0702 1.1876 -0.1027 -0.2482 -0.0267 319 TYR B CD2 
4098 C CE1 . TYR B 244 ? 0.8281 1.0849 1.2072 -0.0641 -0.2061 -0.0081 319 TYR B CE1 
4099 C CE2 . TYR B 244 ? 0.9867 1.2277 1.3809 -0.1064 -0.2259 -0.0203 319 TYR B CE2 
4100 C CZ  . TYR B 244 ? 1.0405 1.3139 1.4675 -0.0865 -0.2036 -0.0113 319 TYR B CZ  
4101 O OH  . TYR B 244 ? 0.9433 1.2628 1.4497 -0.0898 -0.1767 -0.0057 319 TYR B OH  
4102 N N   . LEU B 245 ? 0.8552 0.9453 0.9260 -0.0358 -0.2307 -0.0125 320 LEU B N   
4103 C CA  . LEU B 245 ? 0.9029 1.0059 0.9833 -0.0161 -0.2168 -0.0026 320 LEU B CA  
4104 C C   . LEU B 245 ? 0.9716 1.1184 1.1280 -0.0084 -0.2358 0.0025  320 LEU B C   
4105 O O   . LEU B 245 ? 0.9944 1.1454 1.1642 -0.0121 -0.2753 0.0018  320 LEU B O   
4106 C CB  . LEU B 245 ? 0.9424 1.0053 0.9495 -0.0067 -0.2258 0.0013  320 LEU B CB  
4107 C CG  . LEU B 245 ? 0.9179 0.9372 0.8499 -0.0126 -0.2076 -0.0040 320 LEU B CG  
4108 C CD1 . LEU B 245 ? 0.9086 0.8894 0.7714 -0.0059 -0.2204 0.0008  320 LEU B CD1 
4109 C CD2 . LEU B 245 ? 0.8432 0.8686 0.7817 -0.0081 -0.1670 -0.0027 320 LEU B CD2 
4110 N N   . PRO B 246 ? 1.1554 1.3346 1.3629 0.0027  -0.2097 0.0070  321 PRO B N   
4111 C CA  . PRO B 246 ? 1.2144 1.4358 1.4977 0.0141  -0.2238 0.0113  321 PRO B CA  
4112 C C   . PRO B 246 ? 1.1917 1.3960 1.4511 0.0294  -0.2573 0.0178  321 PRO B C   
4113 O O   . PRO B 246 ? 1.0994 1.2766 1.3122 0.0428  -0.2461 0.0228  321 PRO B O   
4114 C CB  . PRO B 246 ? 1.1020 1.3444 1.4154 0.0260  -0.1813 0.0134  321 PRO B CB  
4115 C CG  . PRO B 246 ? 0.9752 1.2006 1.2535 0.0125  -0.1503 0.0097  321 PRO B CG  
4116 C CD  . PRO B 246 ? 1.0134 1.1928 1.2144 0.0044  -0.1659 0.0071  321 PRO B CD  
4117 N N   . PRO B 247 ? 0.9320 1.1486 1.2204 0.0269  -0.2989 0.0185  322 PRO B N   
4118 C CA  . PRO B 247 ? 0.8372 1.0224 1.0778 0.0382  -0.3227 0.0255  322 PRO B CA  
4119 C C   . PRO B 247 ? 0.9238 1.1205 1.1934 0.0624  -0.3147 0.0341  322 PRO B C   
4120 O O   . PRO B 247 ? 0.9550 1.1205 1.1806 0.0722  -0.3305 0.0419  322 PRO B O   
4121 C CB  . PRO B 247 ? 0.8709 1.0675 1.1364 0.0276  -0.3540 0.0225  322 PRO B CB  
4122 C CG  . PRO B 247 ? 0.8804 1.1305 1.2377 0.0192  -0.3410 0.0171  322 PRO B CG  
4123 C CD  . PRO B 247 ? 0.8556 1.1071 1.2079 0.0118  -0.3086 0.0130  322 PRO B CD  
4124 N N   . GLU B 248 ? 0.9104 1.1474 1.2498 0.0719  -0.2882 0.0327  323 GLU B N   
4125 C CA  . GLU B 248 ? 0.8980 1.1430 1.2652 0.0958  -0.2780 0.0383  323 GLU B CA  
4126 C C   . GLU B 248 ? 1.1211 1.3214 1.4197 0.1067  -0.2684 0.0435  323 GLU B C   
4127 O O   . GLU B 248 ? 1.0881 1.2602 1.3551 0.1183  -0.2822 0.0517  323 GLU B O   
4128 C CB  . GLU B 248 ? 0.9123 1.2068 1.3622 0.1022  -0.2446 0.0331  323 GLU B CB  
4129 C CG  . GLU B 248 ? 0.8051 1.1099 1.2570 0.0877  -0.2140 0.0265  323 GLU B CG  
4130 C CD  . GLU B 248 ? 1.0691 1.4140 1.5873 0.0946  -0.1729 0.0223  323 GLU B CD  
4131 O OE1 . GLU B 248 ? 1.0651 1.4336 1.6334 0.1106  -0.1697 0.0230  323 GLU B OE1 
4132 O OE2 . GLU B 248 ? 1.1762 1.5187 1.6756 0.0822  -0.1374 0.0182  323 GLU B OE2 
4133 N N   . PHE B 249 ? 1.1189 1.3077 1.3859 0.0998  -0.2373 0.0387  324 PHE B N   
4134 C CA  . PHE B 249 ? 0.9886 1.1360 1.1912 0.1064  -0.2184 0.0420  324 PHE B CA  
4135 C C   . PHE B 249 ? 1.0058 1.1051 1.1218 0.0949  -0.2325 0.0462  324 PHE B C   
4136 O O   . PHE B 249 ? 0.9950 1.0579 1.0608 0.1009  -0.2256 0.0522  324 PHE B O   
4137 C CB  . PHE B 249 ? 0.8938 1.0476 1.0950 0.1024  -0.1731 0.0345  324 PHE B CB  
4138 C CG  . PHE B 249 ? 1.0008 1.1912 1.2703 0.1160  -0.1510 0.0302  324 PHE B CG  
4139 C CD1 . PHE B 249 ? 0.9796 1.1604 1.2564 0.1368  -0.1439 0.0316  324 PHE B CD1 
4140 C CD2 . PHE B 249 ? 0.9651 1.1963 1.2894 0.1075  -0.1348 0.0244  324 PHE B CD2 
4141 C CE1 . PHE B 249 ? 0.9486 1.1598 1.2843 0.1507  -0.1201 0.0255  324 PHE B CE1 
4142 C CE2 . PHE B 249 ? 0.9808 1.2444 1.3646 0.1200  -0.1093 0.0202  324 PHE B CE2 
4143 C CZ  . PHE B 249 ? 0.9281 1.1817 1.3165 0.1424  -0.1013 0.0198  324 PHE B CZ  
4144 N N   . THR B 250 ? 1.0294 1.1256 1.1264 0.0781  -0.2501 0.0426  325 THR B N   
4145 C CA  . THR B 250 ? 1.0733 1.1225 1.0848 0.0670  -0.2590 0.0443  325 THR B CA  
4146 C C   . THR B 250 ? 1.0206 1.0434 0.9984 0.0704  -0.2899 0.0530  325 THR B C   
4147 O O   . THR B 250 ? 1.1538 1.1409 1.0645 0.0586  -0.2951 0.0523  325 THR B O   
4148 C CB  . THR B 250 ? 0.9794 1.0306 0.9785 0.0467  -0.2566 0.0336  325 THR B CB  
4149 O OG1 . THR B 250 ? 1.1651 1.2468 1.2182 0.0415  -0.2871 0.0303  325 THR B OG1 
4150 C CG2 . THR B 250 ? 1.0669 1.1351 1.0856 0.0411  -0.2152 0.0264  325 THR B CG2 
4151 N N   . ALA B 251 ? 0.9812 1.0197 1.0031 0.0855  -0.3023 0.0598  326 ALA B N   
4152 C CA  . ALA B 251 ? 1.1659 1.1812 1.1600 0.0878  -0.3283 0.0679  326 ALA B CA  
4153 C C   . ALA B 251 ? 1.1696 1.1316 1.0818 0.0876  -0.3196 0.0771  326 ALA B C   
4154 O O   . ALA B 251 ? 1.2678 1.1967 1.1191 0.0775  -0.3305 0.0788  326 ALA B O   
4155 C CB  . ALA B 251 ? 0.9847 1.0293 1.0486 0.1058  -0.3415 0.0733  326 ALA B CB  
4156 N N   . GLY B 252 ? 1.1236 1.0759 1.0342 0.0981  -0.2982 0.0824  327 GLY B N   
4157 C CA  . GLY B 252 ? 1.1405 1.0450 0.9835 0.0968  -0.2877 0.0922  327 GLY B CA  
4158 C C   . GLY B 252 ? 1.0784 0.9556 0.8560 0.0803  -0.2662 0.0882  327 GLY B C   
4159 O O   . GLY B 252 ? 1.1659 1.0053 0.8893 0.0766  -0.2546 0.0961  327 GLY B O   
4160 N N   . LEU B 253 ? 1.0332 0.9286 0.8177 0.0701  -0.2591 0.0762  328 LEU B N   
4161 C CA  . LEU B 253 ? 0.8758 0.7469 0.6031 0.0558  -0.2362 0.0708  328 LEU B CA  
4162 C C   . LEU B 253 ? 1.0458 0.8858 0.7156 0.0456  -0.2471 0.0708  328 LEU B C   
4163 O O   . LEU B 253 ? 0.9630 0.8097 0.6428 0.0444  -0.2757 0.0687  328 LEU B O   
4164 C CB  . LEU B 253 ? 1.0250 0.9221 0.7772 0.0489  -0.2274 0.0577  328 LEU B CB  
4165 C CG  . LEU B 253 ? 0.9496 0.8807 0.7613 0.0579  -0.2116 0.0552  328 LEU B CG  
4166 C CD1 . LEU B 253 ? 0.8974 0.8534 0.7334 0.0465  -0.1921 0.0417  328 LEU B CD1 
4167 C CD2 . LEU B 253 ? 0.9908 0.9040 0.7845 0.0631  -0.1848 0.0611  328 LEU B CD2 
4168 N N   . SER B 254 ? 0.8790 0.6852 0.4904 0.0383  -0.2234 0.0729  329 SER B N   
4169 C CA  . SER B 254 ? 1.0110 0.7845 0.5626 0.0292  -0.2288 0.0717  329 SER B CA  
4170 C C   . SER B 254 ? 1.0199 0.7996 0.5655 0.0188  -0.2328 0.0559  329 SER B C   
4171 O O   . SER B 254 ? 0.9427 0.7484 0.5236 0.0167  -0.2247 0.0463  329 SER B O   
4172 C CB  . SER B 254 ? 1.0785 0.8188 0.5769 0.0236  -0.1972 0.0767  329 SER B CB  
4173 O OG  . SER B 254 ? 0.9611 0.7087 0.4595 0.0169  -0.1661 0.0663  329 SER B OG  
4174 N N   . SER B 255 ? 1.0338 0.7854 0.5305 0.0121  -0.2460 0.0531  330 SER B N   
4175 C CA  . SER B 255 ? 1.0699 0.8199 0.5546 0.0016  -0.2510 0.0371  330 SER B CA  
4176 C C   . SER B 255 ? 1.0092 0.7532 0.4765 -0.0046 -0.2129 0.0268  330 SER B C   
4177 O O   . SER B 255 ? 1.0944 0.8502 0.5779 -0.0107 -0.2116 0.0132  330 SER B O   
4178 C CB  . SER B 255 ? 0.9930 0.7074 0.4203 -0.0038 -0.2716 0.0361  330 SER B CB  
4179 O OG  . SER B 255 ? 1.2708 0.9799 0.6853 -0.0141 -0.2775 0.0195  330 SER B OG  
4180 N N   . GLU B 256 ? 1.1963 0.9225 0.6346 -0.0033 -0.1819 0.0332  331 GLU B N   
4181 C CA  . GLU B 256 ? 0.8995 0.6225 0.3277 -0.0079 -0.1448 0.0239  331 GLU B CA  
4182 C C   . GLU B 256 ? 0.9049 0.6623 0.3881 -0.0048 -0.1333 0.0209  331 GLU B C   
4183 O O   . GLU B 256 ? 1.0482 0.8109 0.5378 -0.0089 -0.1178 0.0085  331 GLU B O   
4184 C CB  . GLU B 256 ? 0.9828 0.6819 0.3743 -0.0083 -0.1151 0.0324  331 GLU B CB  
4185 C CG  . GLU B 256 ? 1.1302 0.7891 0.4554 -0.0131 -0.1176 0.0331  331 GLU B CG  
4186 C CD  . GLU B 256 ? 1.4477 1.0924 0.7557 -0.0096 -0.1508 0.0462  331 GLU B CD  
4187 O OE1 . GLU B 256 ? 1.2921 0.9569 0.6406 -0.0023 -0.1651 0.0568  331 GLU B OE1 
4188 O OE2 . GLU B 256 ? 1.7072 1.3189 0.9603 -0.0135 -0.1628 0.0458  331 GLU B OE2 
4189 N N   . LEU B 257 ? 0.8596 0.6375 0.3805 0.0032  -0.1406 0.0320  332 LEU B N   
4190 C CA  . LEU B 257 ? 0.7629 0.5702 0.3304 0.0069  -0.1301 0.0297  332 LEU B CA  
4191 C C   . LEU B 257 ? 0.7899 0.6204 0.3916 0.0045  -0.1516 0.0199  332 LEU B C   
4192 O O   . LEU B 257 ? 0.8220 0.6648 0.4411 0.0019  -0.1380 0.0116  332 LEU B O   
4193 C CB  . LEU B 257 ? 0.7745 0.5935 0.3706 0.0170  -0.1328 0.0431  332 LEU B CB  
4194 C CG  . LEU B 257 ? 0.8035 0.6480 0.4409 0.0223  -0.1203 0.0416  332 LEU B CG  
4195 C CD1 . LEU B 257 ? 0.6955 0.5359 0.3224 0.0165  -0.0843 0.0358  332 LEU B CD1 
4196 C CD2 . LEU B 257 ? 0.8285 0.6817 0.4960 0.0333  -0.1229 0.0527  332 LEU B CD2 
4197 N N   . ARG B 258 ? 0.7495 0.5866 0.3648 0.0048  -0.1855 0.0210  333 ARG B N   
4198 C CA  . ARG B 258 ? 0.7719 0.6335 0.4273 -0.0005 -0.2070 0.0115  333 ARG B CA  
4199 C C   . ARG B 258 ? 0.8108 0.6548 0.4375 -0.0128 -0.1965 -0.0040 333 ARG B C   
4200 O O   . ARG B 258 ? 0.9150 0.7770 0.5750 -0.0184 -0.1935 -0.0126 333 ARG B O   
4201 C CB  . ARG B 258 ? 0.8911 0.7619 0.5672 0.0005  -0.2444 0.0148  333 ARG B CB  
4202 C CG  . ARG B 258 ? 0.9728 0.8769 0.7096 0.0133  -0.2596 0.0256  333 ARG B CG  
4203 C CD  . ARG B 258 ? 0.9530 0.8793 0.7327 0.0116  -0.2953 0.0240  333 ARG B CD  
4204 N NE  . ARG B 258 ? 1.1584 1.1030 0.9787 0.0263  -0.3108 0.0360  333 ARG B NE  
4205 C CZ  . ARG B 258 ? 1.3998 1.3193 1.1864 0.0322  -0.3248 0.0455  333 ARG B CZ  
4206 N NH1 . ARG B 258 ? 1.3741 1.2502 1.0855 0.0245  -0.3240 0.0450  333 ARG B NH1 
4207 N NH2 . ARG B 258 ? 1.3311 1.2683 1.1612 0.0467  -0.3387 0.0555  333 ARG B NH2 
4208 N N   . SER B 259 ? 0.8921 0.7007 0.4612 -0.0169 -0.1881 -0.0077 334 SER B N   
4209 C CA  . SER B 259 ? 0.7284 0.5158 0.2685 -0.0263 -0.1766 -0.0236 334 SER B CA  
4210 C C   . SER B 259 ? 0.8280 0.6195 0.3766 -0.0254 -0.1424 -0.0289 334 SER B C   
4211 O O   . SER B 259 ? 0.8899 0.6775 0.4434 -0.0323 -0.1383 -0.0421 334 SER B O   
4212 C CB  . SER B 259 ? 0.8122 0.5606 0.2881 -0.0282 -0.1698 -0.0253 334 SER B CB  
4213 O OG  . SER B 259 ? 1.3122 1.0383 0.7601 -0.0347 -0.1536 -0.0412 334 SER B OG  
4214 N N   . VAL B 260 ? 0.7680 0.5658 0.3202 -0.0174 -0.1184 -0.0186 335 VAL B N   
4215 C CA  . VAL B 260 ? 0.7837 0.5871 0.3477 -0.0154 -0.0861 -0.0225 335 VAL B CA  
4216 C C   . VAL B 260 ? 0.6999 0.5443 0.3366 -0.0141 -0.0880 -0.0218 335 VAL B C   
4217 O O   . VAL B 260 ? 0.8006 0.6521 0.4602 -0.0160 -0.0711 -0.0292 335 VAL B O   
4218 C CB  . VAL B 260 ? 0.7756 0.5790 0.3351 -0.0087 -0.0597 -0.0113 335 VAL B CB  
4219 C CG1 . VAL B 260 ? 0.8698 0.6873 0.4571 -0.0057 -0.0294 -0.0140 335 VAL B CG1 
4220 C CG2 . VAL B 260 ? 0.9012 0.6763 0.4154 -0.0110 -0.0479 -0.0112 335 VAL B CG2 
4221 N N   . LEU B 261 ? 0.9590 0.8302 0.6346 -0.0099 -0.1069 -0.0124 336 LEU B N   
4222 C CA  . LEU B 261 ? 0.6544 0.5649 0.3983 -0.0086 -0.1044 -0.0113 336 LEU B CA  
4223 C C   . LEU B 261 ? 0.7933 0.7095 0.5585 -0.0195 -0.1163 -0.0213 336 LEU B C   
4224 O O   . LEU B 261 ? 0.8334 0.7689 0.6385 -0.0216 -0.1020 -0.0228 336 LEU B O   
4225 C CB  . LEU B 261 ? 0.7023 0.6381 0.4826 -0.0005 -0.1203 -0.0009 336 LEU B CB  
4226 C CG  . LEU B 261 ? 0.6572 0.5870 0.4244 0.0098  -0.1091 0.0095  336 LEU B CG  
4227 C CD1 . LEU B 261 ? 0.8651 0.8151 0.6682 0.0194  -0.1273 0.0180  336 LEU B CD1 
4228 C CD2 . LEU B 261 ? 0.5554 0.4944 0.3384 0.0122  -0.0779 0.0091  336 LEU B CD2 
4229 N N   . VAL B 262 ? 0.7710 0.6681 0.5083 -0.0275 -0.1436 -0.0278 337 VAL B N   
4230 C CA  . VAL B 262 ? 0.6485 0.5473 0.4062 -0.0405 -0.1568 -0.0386 337 VAL B CA  
4231 C C   . VAL B 262 ? 0.7801 0.6565 0.5188 -0.0447 -0.1313 -0.0488 337 VAL B C   
4232 O O   . VAL B 262 ? 0.7961 0.6851 0.5741 -0.0513 -0.1246 -0.0520 337 VAL B O   
4233 C CB  . VAL B 262 ? 0.6902 0.5675 0.4145 -0.0489 -0.1953 -0.0450 337 VAL B CB  
4234 C CG1 . VAL B 262 ? 0.8368 0.7035 0.5685 -0.0650 -0.2075 -0.0596 337 VAL B CG1 
4235 C CG2 . VAL B 262 ? 0.8532 0.7617 0.6193 -0.0443 -0.2246 -0.0344 337 VAL B CG2 
4236 N N   . MET B 263 ? 0.7935 0.6359 0.4737 -0.0404 -0.1149 -0.0533 338 MET B N   
4237 C CA  . MET B 263 ? 0.6762 0.4976 0.3426 -0.0410 -0.0891 -0.0633 338 MET B CA  
4238 C C   . MET B 263 ? 0.6909 0.5406 0.4082 -0.0344 -0.0649 -0.0554 338 MET B C   
4239 O O   . MET B 263 ? 0.8002 0.6457 0.5360 -0.0377 -0.0549 -0.0607 338 MET B O   
4240 C CB  . MET B 263 ? 0.7456 0.5309 0.3467 -0.0356 -0.0712 -0.0684 338 MET B CB  
4241 C CG  . MET B 263 ? 0.9230 0.6722 0.4582 -0.0417 -0.0940 -0.0756 338 MET B CG  
4242 S SD  . MET B 263 ? 1.1868 0.9098 0.6740 -0.0338 -0.0602 -0.0762 338 MET B SD  
4243 C CE  . MET B 263 ? 1.1648 0.8670 0.6511 -0.0336 -0.0338 -0.0945 338 MET B CE  
4244 N N   . MET B 264 ? 0.6259 0.5004 0.3627 -0.0253 -0.0569 -0.0425 339 MET B N   
4245 C CA  . MET B 264 ? 0.6089 0.5063 0.3854 -0.0190 -0.0367 -0.0353 339 MET B CA  
4246 C C   . MET B 264 ? 0.5982 0.5225 0.4247 -0.0242 -0.0439 -0.0311 339 MET B C   
4247 O O   . MET B 264 ? 0.7044 0.6348 0.5535 -0.0233 -0.0292 -0.0284 339 MET B O   
4248 C CB  . MET B 264 ? 0.5337 0.4449 0.3120 -0.0092 -0.0277 -0.0247 339 MET B CB  
4249 C CG  . MET B 264 ? 0.7008 0.5874 0.4332 -0.0059 -0.0167 -0.0263 339 MET B CG  
4250 S SD  . MET B 264 ? 0.6657 0.5656 0.4047 0.0025  -0.0060 -0.0134 339 MET B SD  
4251 C CE  . MET B 264 ? 0.6133 0.5332 0.3944 0.0074  0.0139  -0.0120 339 MET B CE  
4252 N N   . LEU B 265 ? 0.8020 0.7421 0.6471 -0.0294 -0.0658 -0.0295 340 LEU B N   
4253 C CA  . LEU B 265 ? 0.5671 0.5368 0.4653 -0.0350 -0.0691 -0.0250 340 LEU B CA  
4254 C C   . LEU B 265 ? 0.5943 0.5543 0.5040 -0.0505 -0.0800 -0.0331 340 LEU B C   
4255 O O   . LEU B 265 ? 0.8315 0.8168 0.7878 -0.0588 -0.0871 -0.0300 340 LEU B O   
4256 C CB  . LEU B 265 ? 0.5037 0.5018 0.4299 -0.0310 -0.0850 -0.0186 340 LEU B CB  
4257 C CG  . LEU B 265 ? 0.4176 0.4245 0.3390 -0.0163 -0.0744 -0.0103 340 LEU B CG  
4258 C CD1 . LEU B 265 ? 0.4029 0.4383 0.3613 -0.0106 -0.0882 -0.0046 340 LEU B CD1 
4259 C CD2 . LEU B 265 ? 0.4959 0.5083 0.4264 -0.0116 -0.0480 -0.0063 340 LEU B CD2 
4260 N N   . GLU B 266 ? 0.7968 0.7204 0.6673 -0.0549 -0.0799 -0.0441 341 GLU B N   
4261 C CA  . GLU B 266 ? 0.5929 0.4997 0.4709 -0.0702 -0.0892 -0.0534 341 GLU B CA  
4262 C C   . GLU B 266 ? 0.5891 0.5082 0.5080 -0.0743 -0.0713 -0.0458 341 GLU B C   
4263 O O   . GLU B 266 ? 0.6577 0.5696 0.5682 -0.0646 -0.0491 -0.0410 341 GLU B O   
4264 C CB  . GLU B 266 ? 0.5905 0.4502 0.4133 -0.0706 -0.0865 -0.0680 341 GLU B CB  
4265 C CG  . GLU B 266 ? 0.8463 0.6799 0.6742 -0.0843 -0.0894 -0.0783 341 GLU B CG  
4266 C CD  . GLU B 266 ? 0.8970 0.7338 0.7435 -0.1030 -0.1206 -0.0849 341 GLU B CD  
4267 O OE1 . GLU B 266 ? 1.0617 0.9097 0.8999 -0.1038 -0.1443 -0.0855 341 GLU B OE1 
4268 O OE2 . GLU B 266 ? 1.0759 0.9030 0.9475 -0.1174 -0.1232 -0.0887 341 GLU B OE2 
4269 N N   . PRO B 267 ? 0.6579 0.5950 0.6215 -0.0888 -0.0804 -0.0435 342 PRO B N   
4270 C CA  . PRO B 267 ? 0.5861 0.5339 0.5844 -0.0932 -0.0602 -0.0329 342 PRO B CA  
4271 C C   . PRO B 267 ? 0.7486 0.6571 0.7260 -0.0962 -0.0483 -0.0365 342 PRO B C   
4272 O O   . PRO B 267 ? 0.7011 0.6097 0.6881 -0.0926 -0.0286 -0.0253 342 PRO B O   
4273 C CB  . PRO B 267 ? 0.5629 0.5380 0.6154 -0.1108 -0.0733 -0.0310 342 PRO B CB  
4274 C CG  . PRO B 267 ? 0.6022 0.5925 0.6559 -0.1099 -0.1012 -0.0375 342 PRO B CG  
4275 C CD  . PRO B 267 ? 0.5666 0.5181 0.5546 -0.1020 -0.1094 -0.0486 342 PRO B CD  
4276 N N   . ASP B 268 ? 0.7070 0.5785 0.6536 -0.1019 -0.0603 -0.0517 343 ASP B N   
4277 C CA  . ASP B 268 ? 0.5875 0.4179 0.5179 -0.1037 -0.0497 -0.0566 343 ASP B CA  
4278 C C   . ASP B 268 ? 0.7667 0.5784 0.6596 -0.0833 -0.0334 -0.0592 343 ASP B C   
4279 O O   . ASP B 268 ? 0.7719 0.5706 0.6279 -0.0768 -0.0382 -0.0708 343 ASP B O   
4280 C CB  . ASP B 268 ? 0.6342 0.4298 0.5498 -0.1198 -0.0692 -0.0743 343 ASP B CB  
4281 C CG  . ASP B 268 ? 0.8095 0.5647 0.7249 -0.1264 -0.0599 -0.0772 343 ASP B CG  
4282 O OD1 . ASP B 268 ? 0.9827 0.7223 0.8860 -0.1113 -0.0395 -0.0718 343 ASP B OD1 
4283 O OD2 . ASP B 268 ? 1.1192 0.8573 1.0494 -0.1470 -0.0748 -0.0844 343 ASP B OD2 
4284 N N   . PRO B 269 ? 0.8222 0.6315 0.7233 -0.0733 -0.0145 -0.0482 344 PRO B N   
4285 C CA  . PRO B 269 ? 0.7758 0.5730 0.6524 -0.0538 -0.0003 -0.0505 344 PRO B CA  
4286 C C   . PRO B 269 ? 0.7130 0.4665 0.5575 -0.0511 0.0015  -0.0689 344 PRO B C   
4287 O O   . PRO B 269 ? 0.9385 0.6855 0.7599 -0.0368 0.0125  -0.0754 344 PRO B O   
4288 C CB  . PRO B 269 ? 0.7773 0.5780 0.6743 -0.0466 0.0130  -0.0343 344 PRO B CB  
4289 C CG  . PRO B 269 ? 0.6077 0.4009 0.5267 -0.0641 0.0089  -0.0278 344 PRO B CG  
4290 C CD  . PRO B 269 ? 0.6360 0.4523 0.5682 -0.0795 -0.0058 -0.0324 344 PRO B CD  
4291 N N   . LYS B 270 ? 0.8242 0.5460 0.6673 -0.0648 -0.0072 -0.0782 345 LYS B N   
4292 C CA  . LYS B 270 ? 1.0302 0.7050 0.8367 -0.0624 -0.0057 -0.0993 345 LYS B CA  
4293 C C   . LYS B 270 ? 0.9734 0.6449 0.7385 -0.0633 -0.0148 -0.1139 345 LYS B C   
4294 O O   . LYS B 270 ? 1.0651 0.7057 0.7905 -0.0536 -0.0039 -0.1293 345 LYS B O   
4295 C CB  . LYS B 270 ? 0.9628 0.6013 0.7750 -0.0800 -0.0169 -0.1074 345 LYS B CB  
4296 C CG  . LYS B 270 ? 0.9764 0.6093 0.8236 -0.0819 -0.0087 -0.0912 345 LYS B CG  
4297 C CD  . LYS B 270 ? 1.1766 0.7606 1.0218 -0.0978 -0.0170 -0.1026 345 LYS B CD  
4298 C CE  . LYS B 270 ? 1.5281 1.1067 1.4084 -0.1058 -0.0117 -0.0827 345 LYS B CE  
4299 N NZ  . LYS B 270 ? 1.6209 1.2432 1.5366 -0.1238 -0.0182 -0.0662 345 LYS B NZ  
4300 N N   . LEU B 271 ? 0.8321 0.5336 0.6049 -0.0741 -0.0339 -0.1088 346 LEU B N   
4301 C CA  . LEU B 271 ? 0.9198 0.6153 0.6506 -0.0765 -0.0486 -0.1200 346 LEU B CA  
4302 C C   . LEU B 271 ? 0.7942 0.5212 0.5186 -0.0633 -0.0405 -0.1088 346 LEU B C   
4303 O O   . LEU B 271 ? 0.9759 0.6963 0.6610 -0.0636 -0.0511 -0.1146 346 LEU B O   
4304 C CB  . LEU B 271 ? 0.8808 0.5854 0.6261 -0.0972 -0.0811 -0.1223 346 LEU B CB  
4305 C CG  . LEU B 271 ? 0.8539 0.5336 0.6186 -0.1156 -0.0925 -0.1306 346 LEU B CG  
4306 C CD1 . LEU B 271 ? 0.8603 0.5583 0.6502 -0.1368 -0.1263 -0.1320 346 LEU B CD1 
4307 C CD2 . LEU B 271 ? 0.8491 0.4677 0.5618 -0.1144 -0.0879 -0.1532 346 LEU B CD2 
4308 N N   . ARG B 272 ? 0.8539 0.6111 0.6124 -0.0523 -0.0234 -0.0928 347 ARG B N   
4309 C CA  . ARG B 272 ? 0.8196 0.6063 0.5774 -0.0417 -0.0171 -0.0820 347 ARG B CA  
4310 C C   . ARG B 272 ? 0.7526 0.5202 0.4741 -0.0286 0.0037  -0.0887 347 ARG B C   
4311 O O   . ARG B 272 ? 0.9882 0.7331 0.7061 -0.0215 0.0211  -0.0963 347 ARG B O   
4312 C CB  . ARG B 272 ? 0.6062 0.4286 0.4105 -0.0363 -0.0083 -0.0642 347 ARG B CB  
4313 C CG  . ARG B 272 ? 0.5858 0.4389 0.3948 -0.0279 -0.0058 -0.0532 347 ARG B CG  
4314 C CD  . ARG B 272 ? 0.6119 0.4942 0.4608 -0.0249 0.0001  -0.0385 347 ARG B CD  
4315 N NE  . ARG B 272 ? 0.5587 0.4502 0.4355 -0.0375 -0.0101 -0.0353 347 ARG B NE  
4316 C CZ  . ARG B 272 ? 0.4863 0.3889 0.3909 -0.0389 -0.0021 -0.0247 347 ARG B CZ  
4317 N NH1 . ARG B 272 ? 0.5487 0.4532 0.4547 -0.0279 0.0117  -0.0166 347 ARG B NH1 
4318 N NH2 . ARG B 272 ? 0.5395 0.4505 0.4706 -0.0525 -0.0085 -0.0217 347 ARG B NH2 
4319 N N   . ALA B 273 ? 0.8723 0.6485 0.5693 -0.0251 0.0030  -0.0854 348 ALA B N   
4320 C CA  . ALA B 273 ? 0.7454 0.5065 0.4102 -0.0146 0.0262  -0.0899 348 ALA B CA  
4321 C C   . ALA B 273 ? 0.8178 0.6045 0.5229 -0.0024 0.0476  -0.0790 348 ALA B C   
4322 O O   . ALA B 273 ? 0.8496 0.6673 0.5949 -0.0017 0.0414  -0.0656 348 ALA B O   
4323 C CB  . ALA B 273 ? 0.6910 0.4508 0.3162 -0.0164 0.0188  -0.0866 348 ALA B CB  
4324 N N   . THR B 274 ? 0.8429 0.6158 0.5371 0.0075  0.0728  -0.0856 349 THR B N   
4325 C CA  . THR B 274 ? 0.6848 0.4821 0.4195 0.0191  0.0911  -0.0766 349 THR B CA  
4326 C C   . THR B 274 ? 0.7198 0.5325 0.4452 0.0210  0.1016  -0.0691 349 THR B C   
4327 O O   . THR B 274 ? 0.8028 0.5999 0.4827 0.0154  0.0997  -0.0718 349 THR B O   
4328 C CB  . THR B 274 ? 0.7087 0.4864 0.4516 0.0300  0.1132  -0.0877 349 THR B CB  
4329 O OG1 . THR B 274 ? 0.8590 0.6056 0.5527 0.0307  0.1305  -0.1029 349 THR B OG1 
4330 C CG2 . THR B 274 ? 0.7250 0.4838 0.4799 0.0281  0.1023  -0.0929 349 THR B CG2 
4331 N N   . ALA B 275 ? 0.6976 0.5387 0.4655 0.0283  0.1110  -0.0588 350 ALA B N   
4332 C CA  . ALA B 275 ? 0.5193 0.3749 0.2856 0.0285  0.1217  -0.0510 350 ALA B CA  
4333 C C   . ALA B 275 ? 0.7922 0.6255 0.5250 0.0304  0.1490  -0.0604 350 ALA B C   
4334 O O   . ALA B 275 ? 0.8193 0.6473 0.5214 0.0244  0.1515  -0.0558 350 ALA B O   
4335 C CB  . ALA B 275 ? 0.5878 0.4759 0.4092 0.0348  0.1247  -0.0405 350 ALA B CB  
4336 N N   . GLU B 276 ? 0.7017 0.5223 0.4434 0.0388  0.1685  -0.0722 351 GLU B N   
4337 C CA  . GLU B 276 ? 0.6765 0.4856 0.4015 0.0392  0.1883  -0.0784 351 GLU B CA  
4338 C C   . GLU B 276 ? 0.6992 0.4771 0.3604 0.0296  0.1764  -0.0844 351 GLU B C   
4339 O O   . GLU B 276 ? 0.8688 0.6388 0.5022 0.0257  0.1864  -0.0825 351 GLU B O   
4340 C CB  . GLU B 276 ? 0.6617 0.4655 0.4158 0.0511  0.2059  -0.0896 351 GLU B CB  
4341 C CG  . GLU B 276 ? 1.0189 0.8124 0.7597 0.0533  0.2302  -0.0970 351 GLU B CG  
4342 C CD  . GLU B 276 ? 1.3097 1.0939 1.0759 0.0661  0.2446  -0.1098 351 GLU B CD  
4343 O OE1 . GLU B 276 ? 1.3025 1.0833 1.0922 0.0725  0.2331  -0.1125 351 GLU B OE1 
4344 O OE2 . GLU B 276 ? 1.2082 0.9866 0.9705 0.0703  0.2679  -0.1167 351 GLU B OE2 
4345 N N   . ALA B 277 ? 0.7462 0.5053 0.3843 0.0250  0.1538  -0.0912 352 ALA B N   
4346 C CA  . ALA B 277 ? 0.8267 0.5576 0.4086 0.0155  0.1371  -0.0971 352 ALA B CA  
4347 C C   . ALA B 277 ? 0.8026 0.5424 0.3642 0.0081  0.1213  -0.0833 352 ALA B C   
4348 O O   . ALA B 277 ? 0.8796 0.6018 0.3997 0.0036  0.1202  -0.0828 352 ALA B O   
4349 C CB  . ALA B 277 ? 0.8691 0.5803 0.4401 0.0104  0.1141  -0.1078 352 ALA B CB  
4350 N N   . LEU B 278 ? 0.7377 0.5024 0.3269 0.0075  0.1089  -0.0718 353 LEU B N   
4351 C CA  . LEU B 278 ? 0.7515 0.5243 0.3271 0.0025  0.0933  -0.0582 353 LEU B CA  
4352 C C   . LEU B 278 ? 0.7932 0.5695 0.3656 0.0034  0.1147  -0.0496 353 LEU B C   
4353 O O   . LEU B 278 ? 0.9472 0.7098 0.4844 -0.0014 0.1070  -0.0433 353 LEU B O   
4354 C CB  . LEU B 278 ? 0.6542 0.4526 0.2628 0.0034  0.0795  -0.0486 353 LEU B CB  
4355 C CG  . LEU B 278 ? 0.6564 0.4594 0.2807 -0.0001 0.0540  -0.0530 353 LEU B CG  
4356 C CD1 . LEU B 278 ? 0.8549 0.6963 0.5370 0.0025  0.0452  -0.0410 353 LEU B CD1 
4357 C CD2 . LEU B 278 ? 0.8598 0.6437 0.4420 -0.0082 0.0262  -0.0552 353 LEU B CD2 
4358 N N   . LEU B 279 ? 0.7676 0.5611 0.3780 0.0092  0.1409  -0.0489 354 LEU B N   
4359 C CA  . LEU B 279 ? 0.7404 0.5379 0.3529 0.0081  0.1634  -0.0416 354 LEU B CA  
4360 C C   . LEU B 279 ? 0.8115 0.5796 0.3773 0.0057  0.1763  -0.0485 354 LEU B C   
4361 O O   . LEU B 279 ? 1.0283 0.7915 0.5795 0.0021  0.1910  -0.0409 354 LEU B O   
4362 C CB  . LEU B 279 ? 0.6760 0.5000 0.3458 0.0147  0.1874  -0.0415 354 LEU B CB  
4363 C CG  . LEU B 279 ? 0.6209 0.4737 0.3349 0.0164  0.1782  -0.0321 354 LEU B CG  
4364 C CD1 . LEU B 279 ? 0.5849 0.4622 0.3579 0.0249  0.1963  -0.0349 354 LEU B CD1 
4365 C CD2 . LEU B 279 ? 0.5984 0.4568 0.3081 0.0093  0.1757  -0.0178 354 LEU B CD2 
4366 N N   . ALA B 280 ? 0.9436 0.6894 0.4833 0.0071  0.1718  -0.0628 355 ALA B N   
4367 C CA  . ALA B 280 ? 0.9928 0.7062 0.4808 0.0049  0.1825  -0.0710 355 ALA B CA  
4368 C C   . ALA B 280 ? 1.0299 0.7177 0.4604 -0.0030 0.1555  -0.0676 355 ALA B C   
4369 O O   . ALA B 280 ? 1.0650 0.7225 0.4441 -0.0058 0.1624  -0.0724 355 ALA B O   
4370 C CB  . ALA B 280 ? 1.0945 0.7922 0.5805 0.0105  0.1910  -0.0895 355 ALA B CB  
4371 N N   . LEU B 281 ? 0.9990 0.6977 0.4373 -0.0062 0.1249  -0.0597 356 LEU B N   
4372 C CA  . LEU B 281 ? 0.9509 0.6297 0.3440 -0.0124 0.0957  -0.0552 356 LEU B CA  
4373 C C   . LEU B 281 ? 1.0731 0.7421 0.4389 -0.0150 0.1046  -0.0413 356 LEU B C   
4374 O O   . LEU B 281 ? 1.2616 0.9480 0.6558 -0.0135 0.1266  -0.0323 356 LEU B O   
4375 C CB  . LEU B 281 ? 0.9257 0.6240 0.3447 -0.0136 0.0629  -0.0494 356 LEU B CB  
4376 C CG  . LEU B 281 ? 0.8713 0.5709 0.3051 -0.0144 0.0477  -0.0629 356 LEU B CG  
4377 C CD1 . LEU B 281 ? 1.0304 0.7500 0.4892 -0.0166 0.0159  -0.0562 356 LEU B CD1 
4378 C CD2 . LEU B 281 ? 0.9620 0.6270 0.3484 -0.0190 0.0388  -0.0773 356 LEU B CD2 
4379 N N   . PRO B 282 ? 1.1940 0.8332 0.5040 -0.0196 0.0870  -0.0393 357 PRO B N   
4380 C CA  . PRO B 282 ? 1.1066 0.7295 0.3832 -0.0225 0.0969  -0.0258 357 PRO B CA  
4381 C C   . PRO B 282 ? 1.1198 0.7647 0.4292 -0.0221 0.0899  -0.0080 357 PRO B C   
4382 O O   . PRO B 282 ? 1.2858 0.9281 0.5923 -0.0240 0.1115  0.0026  357 PRO B O   
4383 C CB  . PRO B 282 ? 1.2534 0.8399 0.4653 -0.0267 0.0700  -0.0273 357 PRO B CB  
4384 C CG  . PRO B 282 ? 1.1680 0.7465 0.3736 -0.0268 0.0595  -0.0463 357 PRO B CG  
4385 C CD  . PRO B 282 ? 1.1903 0.8060 0.4628 -0.0230 0.0583  -0.0498 357 PRO B CD  
4386 N N   . VAL B 283 ? 1.1942 0.8600 0.5355 -0.0200 0.0612  -0.0046 358 VAL B N   
4387 C CA  . VAL B 283 ? 1.0629 0.7451 0.4309 -0.0187 0.0520  0.0116  358 VAL B CA  
4388 C C   . VAL B 283 ? 1.0653 0.7763 0.4857 -0.0167 0.0767  0.0147  358 VAL B C   
4389 O O   . VAL B 283 ? 1.0636 0.7848 0.5042 -0.0164 0.0729  0.0276  358 VAL B O   
4390 C CB  . VAL B 283 ? 1.0771 0.7726 0.4635 -0.0159 0.0135  0.0136  358 VAL B CB  
4391 C CG1 . VAL B 283 ? 1.2036 0.8724 0.5432 -0.0183 -0.0157 0.0131  358 VAL B CG1 
4392 C CG2 . VAL B 283 ? 1.0672 0.7860 0.4919 -0.0139 0.0112  0.0010  358 VAL B CG2 
4393 N N   . LEU B 284 ? 1.2040 0.9267 0.6473 -0.0151 0.1007  0.0032  359 LEU B N   
4394 C CA  . LEU B 284 ? 1.1037 0.8561 0.6017 -0.0128 0.1205  0.0051  359 LEU B CA  
4395 C C   . LEU B 284 ? 1.1258 0.8786 0.6319 -0.0140 0.1579  0.0026  359 LEU B C   
4396 O O   . LEU B 284 ? 1.1647 0.9437 0.7209 -0.0120 0.1747  0.0028  359 LEU B O   
4397 C CB  . LEU B 284 ? 0.8199 0.5938 0.3546 -0.0077 0.1123  -0.0050 359 LEU B CB  
4398 C CG  . LEU B 284 ? 0.7335 0.5188 0.2807 -0.0062 0.0810  -0.0002 359 LEU B CG  
4399 C CD1 . LEU B 284 ? 0.7266 0.5245 0.2968 -0.0030 0.0737  -0.0115 359 LEU B CD1 
4400 C CD2 . LEU B 284 ? 0.7158 0.5187 0.2936 -0.0054 0.0825  0.0128  359 LEU B CD2 
4401 N N   . ARG B 285 ? 1.4049 1.1302 0.8651 -0.0170 0.1714  0.0000  360 ARG B N   
4402 C CA  . ARG B 285 ? 1.4566 1.1831 0.9261 -0.0180 0.2091  -0.0021 360 ARG B CA  
4403 C C   . ARG B 285 ? 1.4891 1.2173 0.9642 -0.0248 0.2224  0.0141  360 ARG B C   
4404 O O   . ARG B 285 ? 1.6471 1.3579 1.0904 -0.0291 0.2050  0.0262  360 ARG B O   
4405 C CB  . ARG B 285 ? 1.4411 1.1344 0.8550 -0.0185 0.2214  -0.0122 360 ARG B CB  
4406 C CG  . ARG B 285 ? 1.4069 1.0965 0.8199 -0.0124 0.2175  -0.0305 360 ARG B CG  
4407 C CD  . ARG B 285 ? 1.5868 1.2436 0.9490 -0.0125 0.2382  -0.0414 360 ARG B CD  
4408 N NE  . ARG B 285 ? 1.6683 1.3148 1.0232 -0.0074 0.2325  -0.0596 360 ARG B NE  
4409 C CZ  . ARG B 285 ? 1.6973 1.3580 1.0919 0.0003  0.2535  -0.0714 360 ARG B CZ  
4410 N NH1 . ARG B 285 ? 1.6938 1.3834 1.1430 0.0040  0.2804  -0.0670 360 ARG B NH1 
4411 N NH2 . ARG B 285 ? 1.4891 1.1338 0.8703 0.0043  0.2461  -0.0878 360 ARG B NH2 
4412 N N   . GLN B 286 ? 1.5020 1.2512 1.0212 -0.0257 0.2530  0.0144  361 GLN B N   
4413 C CA  . GLN B 286 ? 1.4490 1.2000 0.9781 -0.0342 0.2706  0.0288  361 GLN B CA  
4414 C C   . GLN B 286 ? 1.4465 1.1879 0.9638 -0.0374 0.3085  0.0261  361 GLN B C   
4415 O O   . GLN B 286 ? 1.6024 1.3091 1.0566 -0.0405 0.3137  0.0272  361 GLN B O   
4416 C CB  . GLN B 286 ? 1.1980 0.9860 0.7986 -0.0352 0.2726  0.0340  361 GLN B CB  
4417 C CG  . GLN B 286 ? 1.3059 1.0958 0.9096 -0.0362 0.2414  0.0436  361 GLN B CG  
4418 C CD  . GLN B 286 ? 1.2734 1.0434 0.8533 -0.0456 0.2398  0.0608  361 GLN B CD  
4419 O OE1 . GLN B 286 ? 1.3064 1.0522 0.8470 -0.0511 0.2551  0.0660  361 GLN B OE1 
4420 N NE2 . GLN B 286 ? 1.2183 0.9954 0.8201 -0.0473 0.2220  0.0699  361 GLN B NE2 
# 
