data_9H8E
# 
_entry.id   9H8E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9H8E         pdb_00009h8e 10.2210/pdb9h8e/pdb 
WWPDB D_1292134174 ?            ?                   
# 
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 2025-02-19 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
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'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H8E 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              MARIANNE.SCHIMPL@ASTRAZENECA.COM 
_pdbx_contact_author.name_first         MARIANNE 
_pdbx_contact_author.name_last          SCHIMPL 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2284-5250 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Schimpl, M.' 1 0000-0003-2284-5250 
'Pflug, A.'   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                4582 
_citation.page_last                 4595 
_citation.title                     'Discovery and Optimization of Pyrazine Carboxamide AZ3246, a Selective HPK1 Inhibitor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02631 
_citation.pdbx_database_id_PubMed   39928839 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Shields, J.D.'      1  0000-0002-9015-8594 
primary 'Baker, D.'          2  ?                   
primary 'Balazs, A.Y.S.'     3  0000-0002-5556-6795 
primary 'Bommakanti, G.'     4  ?                   
primary 'Casella, R.'        5  ?                   
primary 'Cao, S.'            6  ?                   
primary 'Cook, S.'           7  ?                   
primary 'Escobar, R.A.'      8  0000-0001-7476-7747 
primary 'Fawell, S.'         9  ?                   
primary 'Gibbons, F.D.'      10 ?                   
primary 'Giblin, K.A.'       11 ?                   
primary 'Goldberg, F.W.'     12 0000-0002-4874-1700 
primary 'Gosselin, E.'       13 ?                   
primary 'Grebe, T.'          14 ?                   
primary 'Hariparsad, N.'     15 0000-0002-6290-5329 
primary 'Hatoum-Mokdad, H.'  16 ?                   
primary 'Howells, R.'        17 ?                   
primary 'Hughes, S.J.'       18 ?                   
primary 'Jackson, A.'        19 ?                   
primary 'Karapa Reddy, I.'   20 ?                   
primary 'Kettle, J.G.'       21 0000-0001-7373-0758 
primary 'Lamont, G.M.'       22 ?                   
primary 'Lamont, S.'         23 ?                   
primary 'Li, M.'             24 ?                   
primary 'Lill, S.O.N.'       25 ?                   
primary 'Mele, D.A.'         26 ?                   
primary 'Metrano, A.J.'      27 0000-0002-2599-8917 
primary 'Mfuh, A.M.'         28 0000-0002-8619-1455 
primary 'Morrill, L.A.'      29 ?                   
primary 'Peng, B.'           30 ?                   
primary 'Pflug, A.'          31 ?                   
primary 'Proia, T.A.'        32 ?                   
primary 'Rezaei, H.'         33 ?                   
primary 'Richards, R.'       34 ?                   
primary 'Richter, M.'        35 ?                   
primary 'Robbins, K.J.'      36 0009-0007-1292-4525 
primary 'San Martin, M.'     37 ?                   
primary 'Schimpl, M.'        38 0000-0003-2284-5250 
primary 'Schuller, A.G.'     39 0000-0001-9163-5885 
primary 'Sha, L.'            40 ?                   
primary 'Shen, M.'           41 ?                   
primary 'Sheppeck 2nd, J.E.' 42 0009-0006-3373-8791 
primary 'Singh, M.'          43 ?                   
primary 'Stokes, S.'         44 ?                   
primary 'Song, K.'           45 0000-0001-9409-1991 
primary 'Sun, Y.'            46 ?                   
primary 'Tang, H.'           47 ?                   
primary 'Wagner, D.J.'       48 0000-0002-5805-930X 
primary 'Wang, J.'           49 ?                   
primary 'Wang, Y.'           50 ?                   
primary 'Wilson, D.M.'       51 ?                   
primary 'Wu, A.'             52 ?                   
primary 'Wu, C.'             53 ?                   
primary 'Wu, D.'             54 ?                   
primary 'Wu, Y.'             55 ?                   
primary 'Xu, K.'             56 ?                   
primary 'Yang, Y.'           57 ?                   
primary 'Yao, T.'            58 ?                   
primary 'Ye, M.'             59 ?                   
primary 'Zhang, A.X.'        60 0000-0003-0406-2404 
primary 'Zhang, H.'          61 ?                   
primary 'Zhai, X.'           62 ?                   
primary 'Zhou, Y.'           63 ?                   
primary 'Ziegler, R.E.'      64 0000-0001-9574-8780 
primary 'Grimster, N.P.'     65 0000-0003-0088-1250 
# 
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 'Mitogen-activated protein kinase kinase kinase kinase 1'                                                        
32948.223 1   2.7.11.1 'T165E, S171E' ? ? 
2 non-polymer syn '5-(methylamino)-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[(4-morpholin-4-ylphenyl)amino]pyrazine-2-carboxamide' 
459.504   1   ?        ?              ? ? 
3 water       nat water                                                                                                            
18.015    131 ?        ?              ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Hematopoietic progenitor kinase,MAPK/ERK kinase kinase kinase 1,MEK kinase kinase 1,MEKKK 1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHG
SYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGIS
AQIGAELARRLEFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKE
KGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHG
SYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGIS
AQIGAELARRLEFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKE
KGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '5-(methylamino)-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[(4-morpholin-4-ylphenyl)amino]pyrazine-2-carboxamide' A1ITA 
3 water                                                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ASP n 
1 4   VAL n 
1 5   VAL n 
1 6   ASP n 
1 7   PRO n 
1 8   ASP n 
1 9   ILE n 
1 10  PHE n 
1 11  ASN n 
1 12  ARG n 
1 13  ASP n 
1 14  PRO n 
1 15  ARG n 
1 16  ASP n 
1 17  HIS n 
1 18  TYR n 
1 19  ASP n 
1 20  LEU n 
1 21  LEU n 
1 22  GLN n 
1 23  ARG n 
1 24  LEU n 
1 25  GLY n 
1 26  GLY n 
1 27  GLY n 
1 28  THR n 
1 29  TYR n 
1 30  GLY n 
1 31  GLU n 
1 32  VAL n 
1 33  PHE n 
1 34  LYS n 
1 35  ALA n 
1 36  ARG n 
1 37  ASP n 
1 38  LYS n 
1 39  VAL n 
1 40  SER n 
1 41  GLY n 
1 42  ASP n 
1 43  LEU n 
1 44  VAL n 
1 45  ALA n 
1 46  LEU n 
1 47  LYS n 
1 48  MET n 
1 49  VAL n 
1 50  LYS n 
1 51  MET n 
1 52  GLU n 
1 53  PRO n 
1 54  ASP n 
1 55  ASP n 
1 56  ASP n 
1 57  VAL n 
1 58  SER n 
1 59  THR n 
1 60  LEU n 
1 61  GLN n 
1 62  LYS n 
1 63  GLU n 
1 64  ILE n 
1 65  LEU n 
1 66  ILE n 
1 67  LEU n 
1 68  LYS n 
1 69  THR n 
1 70  CYS n 
1 71  ARG n 
1 72  HIS n 
1 73  ALA n 
1 74  ASN n 
1 75  ILE n 
1 76  VAL n 
1 77  ALA n 
1 78  TYR n 
1 79  HIS n 
1 80  GLY n 
1 81  SER n 
1 82  TYR n 
1 83  LEU n 
1 84  TRP n 
1 85  LEU n 
1 86  GLN n 
1 87  LYS n 
1 88  LEU n 
1 89  TRP n 
1 90  ILE n 
1 91  CYS n 
1 92  MET n 
1 93  GLU n 
1 94  PHE n 
1 95  CYS n 
1 96  GLY n 
1 97  ALA n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 GLN n 
1 102 ASP n 
1 103 ILE n 
1 104 TYR n 
1 105 GLN n 
1 106 VAL n 
1 107 THR n 
1 108 GLY n 
1 109 SER n 
1 110 LEU n 
1 111 SER n 
1 112 GLU n 
1 113 LEU n 
1 114 GLN n 
1 115 ILE n 
1 116 SER n 
1 117 TYR n 
1 118 VAL n 
1 119 CYS n 
1 120 ARG n 
1 121 GLU n 
1 122 VAL n 
1 123 LEU n 
1 124 GLN n 
1 125 GLY n 
1 126 LEU n 
1 127 ALA n 
1 128 TYR n 
1 129 LEU n 
1 130 HIS n 
1 131 SER n 
1 132 GLN n 
1 133 LYS n 
1 134 LYS n 
1 135 ILE n 
1 136 HIS n 
1 137 ARG n 
1 138 ASP n 
1 139 ILE n 
1 140 LYS n 
1 141 GLY n 
1 142 ALA n 
1 143 ASN n 
1 144 ILE n 
1 145 LEU n 
1 146 ILE n 
1 147 ASN n 
1 148 ASP n 
1 149 ALA n 
1 150 GLY n 
1 151 GLU n 
1 152 VAL n 
1 153 ARG n 
1 154 LEU n 
1 155 ALA n 
1 156 ASP n 
1 157 PHE n 
1 158 GLY n 
1 159 ILE n 
1 160 SER n 
1 161 ALA n 
1 162 GLN n 
1 163 ILE n 
1 164 GLY n 
1 165 ALA n 
1 166 GLU n 
1 167 LEU n 
1 168 ALA n 
1 169 ARG n 
1 170 ARG n 
1 171 LEU n 
1 172 GLU n 
1 173 PHE n 
1 174 ILE n 
1 175 GLY n 
1 176 THR n 
1 177 PRO n 
1 178 TYR n 
1 179 TRP n 
1 180 MET n 
1 181 ALA n 
1 182 PRO n 
1 183 GLU n 
1 184 VAL n 
1 185 ALA n 
1 186 ALA n 
1 187 VAL n 
1 188 ALA n 
1 189 LEU n 
1 190 LYS n 
1 191 GLY n 
1 192 GLY n 
1 193 TYR n 
1 194 ASN n 
1 195 GLU n 
1 196 LEU n 
1 197 CYS n 
1 198 ASP n 
1 199 ILE n 
1 200 TRP n 
1 201 SER n 
1 202 LEU n 
1 203 GLY n 
1 204 ILE n 
1 205 THR n 
1 206 ALA n 
1 207 ILE n 
1 208 GLU n 
1 209 LEU n 
1 210 ALA n 
1 211 GLU n 
1 212 LEU n 
1 213 GLN n 
1 214 PRO n 
1 215 PRO n 
1 216 LEU n 
1 217 PHE n 
1 218 ASP n 
1 219 VAL n 
1 220 HIS n 
1 221 PRO n 
1 222 LEU n 
1 223 ARG n 
1 224 VAL n 
1 225 LEU n 
1 226 PHE n 
1 227 LEU n 
1 228 MET n 
1 229 THR n 
1 230 LYS n 
1 231 SER n 
1 232 GLY n 
1 233 TYR n 
1 234 GLN n 
1 235 PRO n 
1 236 PRO n 
1 237 ARG n 
1 238 LEU n 
1 239 LYS n 
1 240 GLU n 
1 241 LYS n 
1 242 GLY n 
1 243 LYS n 
1 244 TRP n 
1 245 SER n 
1 246 ALA n 
1 247 ALA n 
1 248 PHE n 
1 249 HIS n 
1 250 ASN n 
1 251 PHE n 
1 252 ILE n 
1 253 LYS n 
1 254 VAL n 
1 255 THR n 
1 256 LEU n 
1 257 THR n 
1 258 LYS n 
1 259 SER n 
1 260 PRO n 
1 261 LYS n 
1 262 LYS n 
1 263 ARG n 
1 264 PRO n 
1 265 SER n 
1 266 ALA n 
1 267 THR n 
1 268 LYS n 
1 269 MET n 
1 270 LEU n 
1 271 SER n 
1 272 HIS n 
1 273 GLN n 
1 274 LEU n 
1 275 VAL n 
1 276 SER n 
1 277 GLN n 
1 278 PRO n 
1 279 GLY n 
1 280 LEU n 
1 281 ASN n 
1 282 ARG n 
1 283 GLY n 
1 284 LEU n 
1 285 ILE n 
1 286 LEU n 
1 287 ASP n 
1 288 LEU n 
1 289 LEU n 
1 290 ASP n 
1 291 LYS n 
1 292 LEU n 
1 293 LYS n 
1 294 ASN 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                   294 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MAP4K1, HPK1' 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1ITA non-polymer         . 
'5-(methylamino)-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[(4-morpholin-4-ylphenyl)amino]pyrazine-2-carboxamide' ? 'C23 H25 N9 O2' 
459.504 
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 
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   GLY 1   0   ?   ?   ?   A . n 
A 1 2   SER 2   1   ?   ?   ?   A . n 
A 1 3   ASP 3   2   ?   ?   ?   A . n 
A 1 4   VAL 4   3   ?   ?   ?   A . n 
A 1 5   VAL 5   4   ?   ?   ?   A . n 
A 1 6   ASP 6   5   ?   ?   ?   A . n 
A 1 7   PRO 7   6   ?   ?   ?   A . n 
A 1 8   ASP 8   7   7   ASP ASP A . n 
A 1 9   ILE 9   8   8   ILE ILE A . n 
A 1 10  PHE 10  9   9   PHE PHE A . n 
A 1 11  ASN 11  10  10  ASN ASN A . n 
A 1 12  ARG 12  11  11  ARG ARG A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  ASP 16  15  15  ASP ASP A . n 
A 1 17  HIS 17  16  16  HIS HIS A . n 
A 1 18  TYR 18  17  17  TYR TYR A . n 
A 1 19  ASP 19  18  18  ASP ASP A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  LEU 21  20  20  LEU LEU A . n 
A 1 22  GLN 22  21  21  GLN GLN A . n 
A 1 23  ARG 23  22  22  ARG ARG A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  THR 28  27  27  THR THR A . n 
A 1 29  TYR 29  28  28  TYR TYR A . n 
A 1 30  GLY 30  29  29  GLY GLY A . n 
A 1 31  GLU 31  30  30  GLU GLU A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  PHE 33  32  32  PHE PHE A . n 
A 1 34  LYS 34  33  33  LYS LYS A . n 
A 1 35  ALA 35  34  34  ALA ALA A . n 
A 1 36  ARG 36  35  35  ARG ARG A . n 
A 1 37  ASP 37  36  36  ASP ASP A . n 
A 1 38  LYS 38  37  37  LYS LYS A . n 
A 1 39  VAL 39  38  38  VAL VAL A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  ASP 42  41  41  ASP ASP A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  VAL 44  43  43  VAL VAL A . n 
A 1 45  ALA 45  44  44  ALA ALA A . n 
A 1 46  LEU 46  45  45  LEU LEU A . n 
A 1 47  LYS 47  46  46  LYS LYS A . n 
A 1 48  MET 48  47  47  MET MET A . n 
A 1 49  VAL 49  48  48  VAL VAL A . n 
A 1 50  LYS 50  49  49  LYS LYS A . n 
A 1 51  MET 51  50  50  MET MET A . n 
A 1 52  GLU 52  51  51  GLU GLU A . n 
A 1 53  PRO 53  52  52  PRO PRO A . n 
A 1 54  ASP 54  53  53  ASP ASP A . n 
A 1 55  ASP 55  54  54  ASP ASP A . n 
A 1 56  ASP 56  55  55  ASP ASP A . n 
A 1 57  VAL 57  56  56  VAL VAL A . n 
A 1 58  SER 58  57  57  SER SER A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  LEU 60  59  59  LEU LEU A . n 
A 1 61  GLN 61  60  60  GLN GLN A . n 
A 1 62  LYS 62  61  61  LYS LYS A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  ILE 64  63  63  ILE ILE A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  ILE 66  65  65  ILE ILE A . n 
A 1 67  LEU 67  66  66  LEU LEU A . n 
A 1 68  LYS 68  67  67  LYS LYS A . n 
A 1 69  THR 69  68  68  THR THR A . n 
A 1 70  CYS 70  69  69  CYS CYS A . n 
A 1 71  ARG 71  70  70  ARG ARG A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  ALA 73  72  72  ALA ALA A . n 
A 1 74  ASN 74  73  73  ASN ASN A . n 
A 1 75  ILE 75  74  74  ILE ILE A . n 
A 1 76  VAL 76  75  75  VAL VAL A . n 
A 1 77  ALA 77  76  76  ALA ALA A . n 
A 1 78  TYR 78  77  77  TYR TYR A . n 
A 1 79  HIS 79  78  78  HIS HIS A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  SER 81  80  80  SER SER A . n 
A 1 82  TYR 82  81  81  TYR TYR A . n 
A 1 83  LEU 83  82  82  LEU LEU A . n 
A 1 84  TRP 84  83  83  TRP TRP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLN 86  85  85  GLN GLN A . n 
A 1 87  LYS 87  86  86  LYS LYS A . n 
A 1 88  LEU 88  87  87  LEU LEU A . n 
A 1 89  TRP 89  88  88  TRP TRP A . n 
A 1 90  ILE 90  89  89  ILE ILE A . n 
A 1 91  CYS 91  90  90  CYS CYS A . n 
A 1 92  MET 92  91  91  MET MET A . n 
A 1 93  GLU 93  92  92  GLU GLU A . n 
A 1 94  PHE 94  93  93  PHE PHE A . n 
A 1 95  CYS 95  94  94  CYS CYS A . n 
A 1 96  GLY 96  95  95  GLY GLY A . n 
A 1 97  ALA 97  96  96  ALA ALA A . n 
A 1 98  GLY 98  97  97  GLY GLY A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 LEU 100 99  99  LEU LEU A . n 
A 1 101 GLN 101 100 100 GLN GLN A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 ILE 103 102 102 ILE ILE A . n 
A 1 104 TYR 104 103 103 TYR TYR A . n 
A 1 105 GLN 105 104 104 GLN GLN A . n 
A 1 106 VAL 106 105 105 VAL VAL A . n 
A 1 107 THR 107 106 106 THR THR A . n 
A 1 108 GLY 108 107 107 GLY GLY A . n 
A 1 109 SER 109 108 108 SER SER A . n 
A 1 110 LEU 110 109 109 LEU LEU A . n 
A 1 111 SER 111 110 110 SER SER A . n 
A 1 112 GLU 112 111 111 GLU GLU A . n 
A 1 113 LEU 113 112 112 LEU LEU A . n 
A 1 114 GLN 114 113 113 GLN GLN A . n 
A 1 115 ILE 115 114 114 ILE ILE A . n 
A 1 116 SER 116 115 115 SER SER A . n 
A 1 117 TYR 117 116 116 TYR TYR A . n 
A 1 118 VAL 118 117 117 VAL VAL A . n 
A 1 119 CYS 119 118 118 CYS CYS A . n 
A 1 120 ARG 120 119 119 ARG ARG A . n 
A 1 121 GLU 121 120 120 GLU GLU A . n 
A 1 122 VAL 122 121 121 VAL VAL A . n 
A 1 123 LEU 123 122 122 LEU LEU A . n 
A 1 124 GLN 124 123 123 GLN GLN A . n 
A 1 125 GLY 125 124 124 GLY GLY A . n 
A 1 126 LEU 126 125 125 LEU LEU A . n 
A 1 127 ALA 127 126 126 ALA ALA A . n 
A 1 128 TYR 128 127 127 TYR TYR A . n 
A 1 129 LEU 129 128 128 LEU LEU A . n 
A 1 130 HIS 130 129 129 HIS HIS A . n 
A 1 131 SER 131 130 130 SER SER A . n 
A 1 132 GLN 132 131 131 GLN GLN A . n 
A 1 133 LYS 133 132 132 LYS LYS A . n 
A 1 134 LYS 134 133 133 LYS LYS A . n 
A 1 135 ILE 135 134 134 ILE ILE A . n 
A 1 136 HIS 136 135 135 HIS HIS A . n 
A 1 137 ARG 137 136 136 ARG ARG A . n 
A 1 138 ASP 138 137 137 ASP ASP A . n 
A 1 139 ILE 139 138 138 ILE ILE A . n 
A 1 140 LYS 140 139 139 LYS LYS A . n 
A 1 141 GLY 141 140 140 GLY GLY A . n 
A 1 142 ALA 142 141 141 ALA ALA A . n 
A 1 143 ASN 143 142 142 ASN ASN A . n 
A 1 144 ILE 144 143 143 ILE ILE A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ILE 146 145 145 ILE ILE A . n 
A 1 147 ASN 147 146 146 ASN ASN A . n 
A 1 148 ASP 148 147 147 ASP ASP A . n 
A 1 149 ALA 149 148 148 ALA ALA A . n 
A 1 150 GLY 150 149 149 GLY GLY A . n 
A 1 151 GLU 151 150 150 GLU GLU A . n 
A 1 152 VAL 152 151 151 VAL VAL A . n 
A 1 153 ARG 153 152 152 ARG ARG A . n 
A 1 154 LEU 154 153 153 LEU LEU A . n 
A 1 155 ALA 155 154 154 ALA ALA A . n 
A 1 156 ASP 156 155 155 ASP ASP A . n 
A 1 157 PHE 157 156 156 PHE PHE A . n 
A 1 158 GLY 158 157 157 GLY GLY A . n 
A 1 159 ILE 159 158 158 ILE ILE A . n 
A 1 160 SER 160 159 159 SER SER A . n 
A 1 161 ALA 161 160 160 ALA ALA A . n 
A 1 162 GLN 162 161 161 GLN GLN A . n 
A 1 163 ILE 163 162 162 ILE ILE A . n 
A 1 164 GLY 164 163 163 GLY GLY A . n 
A 1 165 ALA 165 164 164 ALA ALA A . n 
A 1 166 GLU 166 165 165 GLU GLU A . n 
A 1 167 LEU 167 166 166 LEU LEU A . n 
A 1 168 ALA 168 167 167 ALA ALA A . n 
A 1 169 ARG 169 168 168 ARG ARG A . n 
A 1 170 ARG 170 169 169 ARG ARG A . n 
A 1 171 LEU 171 170 170 LEU LEU A . n 
A 1 172 GLU 172 171 171 GLU GLU A . n 
A 1 173 PHE 173 172 172 PHE PHE A . n 
A 1 174 ILE 174 173 173 ILE ILE A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 THR 176 175 175 THR THR A . n 
A 1 177 PRO 177 176 176 PRO PRO A . n 
A 1 178 TYR 178 177 177 TYR TYR A . n 
A 1 179 TRP 179 178 178 TRP TRP A . n 
A 1 180 MET 180 179 179 MET MET A . n 
A 1 181 ALA 181 180 180 ALA ALA A . n 
A 1 182 PRO 182 181 181 PRO PRO A . n 
A 1 183 GLU 183 182 182 GLU GLU A . n 
A 1 184 VAL 184 183 183 VAL VAL A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 ALA 186 185 185 ALA ALA A . n 
A 1 187 VAL 187 186 186 VAL VAL A . n 
A 1 188 ALA 188 187 187 ALA ALA A . n 
A 1 189 LEU 189 188 188 LEU LEU A . n 
A 1 190 LYS 190 189 189 LYS LYS A . n 
A 1 191 GLY 191 190 190 GLY GLY A . n 
A 1 192 GLY 192 191 191 GLY GLY A . n 
A 1 193 TYR 193 192 192 TYR TYR A . n 
A 1 194 ASN 194 193 193 ASN ASN A . n 
A 1 195 GLU 195 194 194 GLU GLU A . n 
A 1 196 LEU 196 195 195 LEU LEU A . n 
A 1 197 CYS 197 196 196 CYS CYS A . n 
A 1 198 ASP 198 197 197 ASP ASP A . n 
A 1 199 ILE 199 198 198 ILE ILE A . n 
A 1 200 TRP 200 199 199 TRP TRP A . n 
A 1 201 SER 201 200 200 SER SER A . n 
A 1 202 LEU 202 201 201 LEU LEU A . n 
A 1 203 GLY 203 202 202 GLY GLY A . n 
A 1 204 ILE 204 203 203 ILE ILE A . n 
A 1 205 THR 205 204 204 THR THR A . n 
A 1 206 ALA 206 205 205 ALA ALA A . n 
A 1 207 ILE 207 206 206 ILE ILE A . n 
A 1 208 GLU 208 207 207 GLU GLU A . n 
A 1 209 LEU 209 208 208 LEU LEU A . n 
A 1 210 ALA 210 209 209 ALA ALA A . n 
A 1 211 GLU 211 210 210 GLU GLU A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 GLN 213 212 212 GLN GLN A . n 
A 1 214 PRO 214 213 213 PRO PRO A . n 
A 1 215 PRO 215 214 214 PRO PRO A . n 
A 1 216 LEU 216 215 215 LEU LEU A . n 
A 1 217 PHE 217 216 216 PHE PHE A . n 
A 1 218 ASP 218 217 217 ASP ASP A . n 
A 1 219 VAL 219 218 218 VAL VAL A . n 
A 1 220 HIS 220 219 219 HIS HIS A . n 
A 1 221 PRO 221 220 220 PRO PRO A . n 
A 1 222 LEU 222 221 221 LEU LEU A . n 
A 1 223 ARG 223 222 222 ARG ARG A . n 
A 1 224 VAL 224 223 223 VAL VAL A . n 
A 1 225 LEU 225 224 224 LEU LEU A . n 
A 1 226 PHE 226 225 225 PHE PHE A . n 
A 1 227 LEU 227 226 226 LEU LEU A . n 
A 1 228 MET 228 227 227 MET MET A . n 
A 1 229 THR 229 228 228 THR THR A . n 
A 1 230 LYS 230 229 229 LYS LYS A . n 
A 1 231 SER 231 230 230 SER SER A . n 
A 1 232 GLY 232 231 231 GLY GLY A . n 
A 1 233 TYR 233 232 232 TYR TYR A . n 
A 1 234 GLN 234 233 233 GLN GLN A . n 
A 1 235 PRO 235 234 234 PRO PRO A . n 
A 1 236 PRO 236 235 235 PRO PRO A . n 
A 1 237 ARG 237 236 236 ARG ARG A . n 
A 1 238 LEU 238 237 237 LEU LEU A . n 
A 1 239 LYS 239 238 238 LYS LYS A . n 
A 1 240 GLU 240 239 239 GLU GLU A . n 
A 1 241 LYS 241 240 240 LYS LYS A . n 
A 1 242 GLY 242 241 241 GLY GLY A . n 
A 1 243 LYS 243 242 242 LYS LYS A . n 
A 1 244 TRP 244 243 243 TRP TRP A . n 
A 1 245 SER 245 244 244 SER SER A . n 
A 1 246 ALA 246 245 245 ALA ALA A . n 
A 1 247 ALA 247 246 246 ALA ALA A . n 
A 1 248 PHE 248 247 247 PHE PHE A . n 
A 1 249 HIS 249 248 248 HIS HIS A . n 
A 1 250 ASN 250 249 249 ASN ASN A . n 
A 1 251 PHE 251 250 250 PHE PHE A . n 
A 1 252 ILE 252 251 251 ILE ILE A . n 
A 1 253 LYS 253 252 252 LYS LYS A . n 
A 1 254 VAL 254 253 253 VAL VAL A . n 
A 1 255 THR 255 254 254 THR THR A . n 
A 1 256 LEU 256 255 255 LEU LEU A . n 
A 1 257 THR 257 256 256 THR THR A . n 
A 1 258 LYS 258 257 257 LYS LYS A . n 
A 1 259 SER 259 258 258 SER SER A . n 
A 1 260 PRO 260 259 259 PRO PRO A . n 
A 1 261 LYS 261 260 260 LYS LYS A . n 
A 1 262 LYS 262 261 261 LYS LYS A . n 
A 1 263 ARG 263 262 262 ARG ARG A . n 
A 1 264 PRO 264 263 263 PRO PRO A . n 
A 1 265 SER 265 264 264 SER SER A . n 
A 1 266 ALA 266 265 265 ALA ALA A . n 
A 1 267 THR 267 266 266 THR THR A . n 
A 1 268 LYS 268 267 267 LYS LYS A . n 
A 1 269 MET 269 268 268 MET MET A . n 
A 1 270 LEU 270 269 269 LEU LEU A . n 
A 1 271 SER 271 270 270 SER SER A . n 
A 1 272 HIS 272 271 271 HIS HIS A . n 
A 1 273 GLN 273 272 272 GLN GLN A . n 
A 1 274 LEU 274 273 273 LEU LEU A . n 
A 1 275 VAL 275 274 274 VAL VAL A . n 
A 1 276 SER 276 275 275 SER SER A . n 
A 1 277 GLN 277 276 276 GLN GLN A . n 
A 1 278 PRO 278 277 277 PRO PRO A . n 
A 1 279 GLY 279 278 278 GLY GLY A . n 
A 1 280 LEU 280 279 279 LEU LEU A . n 
A 1 281 ASN 281 280 280 ASN ASN A . n 
A 1 282 ARG 282 281 281 ARG ARG A . n 
A 1 283 GLY 283 282 282 GLY GLY A . n 
A 1 284 LEU 284 283 283 LEU LEU A . n 
A 1 285 ILE 285 284 284 ILE ILE A . n 
A 1 286 LEU 286 285 285 LEU LEU A . n 
A 1 287 ASP 287 286 286 ASP ASP A . n 
A 1 288 LEU 288 287 287 LEU LEU A . n 
A 1 289 LEU 289 288 288 LEU LEU A . n 
A 1 290 ASP 290 289 289 ASP ASP A . n 
A 1 291 LYS 291 290 290 LYS LYS A . n 
A 1 292 LEU 292 291 291 LEU LEU A . n 
A 1 293 LYS 293 292 292 LYS LYS A . n 
A 1 294 ASN 294 293 293 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ITA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITA 
_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 
B 2 A1ITA 1   301 301 A1ITA INH A . 
C 3 HOH   1   401 59  HOH   HOH A . 
C 3 HOH   2   402 90  HOH   HOH A . 
C 3 HOH   3   403 72  HOH   HOH A . 
C 3 HOH   4   404 130 HOH   HOH A . 
C 3 HOH   5   405 87  HOH   HOH A . 
C 3 HOH   6   406 49  HOH   HOH A . 
C 3 HOH   7   407 123 HOH   HOH A . 
C 3 HOH   8   408 62  HOH   HOH A . 
C 3 HOH   9   409 18  HOH   HOH A . 
C 3 HOH   10  410 30  HOH   HOH A . 
C 3 HOH   11  411 111 HOH   HOH A . 
C 3 HOH   12  412 65  HOH   HOH A . 
C 3 HOH   13  413 21  HOH   HOH A . 
C 3 HOH   14  414 7   HOH   HOH A . 
C 3 HOH   15  415 64  HOH   HOH A . 
C 3 HOH   16  416 40  HOH   HOH A . 
C 3 HOH   17  417 80  HOH   HOH A . 
C 3 HOH   18  418 68  HOH   HOH A . 
C 3 HOH   19  419 107 HOH   HOH A . 
C 3 HOH   20  420 78  HOH   HOH A . 
C 3 HOH   21  421 2   HOH   HOH A . 
C 3 HOH   22  422 79  HOH   HOH A . 
C 3 HOH   23  423 48  HOH   HOH A . 
C 3 HOH   24  424 58  HOH   HOH A . 
C 3 HOH   25  425 129 HOH   HOH A . 
C 3 HOH   26  426 43  HOH   HOH A . 
C 3 HOH   27  427 31  HOH   HOH A . 
C 3 HOH   28  428 11  HOH   HOH A . 
C 3 HOH   29  429 82  HOH   HOH A . 
C 3 HOH   30  430 39  HOH   HOH A . 
C 3 HOH   31  431 60  HOH   HOH A . 
C 3 HOH   32  432 4   HOH   HOH A . 
C 3 HOH   33  433 114 HOH   HOH A . 
C 3 HOH   34  434 5   HOH   HOH A . 
C 3 HOH   35  435 34  HOH   HOH A . 
C 3 HOH   36  436 97  HOH   HOH A . 
C 3 HOH   37  437 77  HOH   HOH A . 
C 3 HOH   38  438 131 HOH   HOH A . 
C 3 HOH   39  439 27  HOH   HOH A . 
C 3 HOH   40  440 74  HOH   HOH A . 
C 3 HOH   41  441 70  HOH   HOH A . 
C 3 HOH   42  442 14  HOH   HOH A . 
C 3 HOH   43  443 22  HOH   HOH A . 
C 3 HOH   44  444 24  HOH   HOH A . 
C 3 HOH   45  445 12  HOH   HOH A . 
C 3 HOH   46  446 47  HOH   HOH A . 
C 3 HOH   47  447 37  HOH   HOH A . 
C 3 HOH   48  448 55  HOH   HOH A . 
C 3 HOH   49  449 54  HOH   HOH A . 
C 3 HOH   50  450 124 HOH   HOH A . 
C 3 HOH   51  451 10  HOH   HOH A . 
C 3 HOH   52  452 19  HOH   HOH A . 
C 3 HOH   53  453 15  HOH   HOH A . 
C 3 HOH   54  454 76  HOH   HOH A . 
C 3 HOH   55  455 33  HOH   HOH A . 
C 3 HOH   56  456 17  HOH   HOH A . 
C 3 HOH   57  457 126 HOH   HOH A . 
C 3 HOH   58  458 1   HOH   HOH A . 
C 3 HOH   59  459 26  HOH   HOH A . 
C 3 HOH   60  460 36  HOH   HOH A . 
C 3 HOH   61  461 91  HOH   HOH A . 
C 3 HOH   62  462 92  HOH   HOH A . 
C 3 HOH   63  463 69  HOH   HOH A . 
C 3 HOH   64  464 100 HOH   HOH A . 
C 3 HOH   65  465 46  HOH   HOH A . 
C 3 HOH   66  466 93  HOH   HOH A . 
C 3 HOH   67  467 85  HOH   HOH A . 
C 3 HOH   68  468 52  HOH   HOH A . 
C 3 HOH   69  469 86  HOH   HOH A . 
C 3 HOH   70  470 44  HOH   HOH A . 
C 3 HOH   71  471 8   HOH   HOH A . 
C 3 HOH   72  472 104 HOH   HOH A . 
C 3 HOH   73  473 108 HOH   HOH A . 
C 3 HOH   74  474 45  HOH   HOH A . 
C 3 HOH   75  475 32  HOH   HOH A . 
C 3 HOH   76  476 112 HOH   HOH A . 
C 3 HOH   77  477 25  HOH   HOH A . 
C 3 HOH   78  478 118 HOH   HOH A . 
C 3 HOH   79  479 109 HOH   HOH A . 
C 3 HOH   80  480 75  HOH   HOH A . 
C 3 HOH   81  481 28  HOH   HOH A . 
C 3 HOH   82  482 51  HOH   HOH A . 
C 3 HOH   83  483 103 HOH   HOH A . 
C 3 HOH   84  484 113 HOH   HOH A . 
C 3 HOH   85  485 117 HOH   HOH A . 
C 3 HOH   86  486 57  HOH   HOH A . 
C 3 HOH   87  487 23  HOH   HOH A . 
C 3 HOH   88  488 16  HOH   HOH A . 
C 3 HOH   89  489 101 HOH   HOH A . 
C 3 HOH   90  490 38  HOH   HOH A . 
C 3 HOH   91  491 41  HOH   HOH A . 
C 3 HOH   92  492 6   HOH   HOH A . 
C 3 HOH   93  493 3   HOH   HOH A . 
C 3 HOH   94  494 35  HOH   HOH A . 
C 3 HOH   95  495 20  HOH   HOH A . 
C 3 HOH   96  496 125 HOH   HOH A . 
C 3 HOH   97  497 89  HOH   HOH A . 
C 3 HOH   98  498 13  HOH   HOH A . 
C 3 HOH   99  499 98  HOH   HOH A . 
C 3 HOH   100 500 81  HOH   HOH A . 
C 3 HOH   101 501 116 HOH   HOH A . 
C 3 HOH   102 502 110 HOH   HOH A . 
C 3 HOH   103 503 29  HOH   HOH A . 
C 3 HOH   104 504 73  HOH   HOH A . 
C 3 HOH   105 505 96  HOH   HOH A . 
C 3 HOH   106 506 94  HOH   HOH A . 
C 3 HOH   107 507 95  HOH   HOH A . 
C 3 HOH   108 508 88  HOH   HOH A . 
C 3 HOH   109 509 9   HOH   HOH A . 
C 3 HOH   110 510 53  HOH   HOH A . 
C 3 HOH   111 511 128 HOH   HOH A . 
C 3 HOH   112 512 63  HOH   HOH A . 
C 3 HOH   113 513 121 HOH   HOH A . 
C 3 HOH   114 514 67  HOH   HOH A . 
C 3 HOH   115 515 102 HOH   HOH A . 
C 3 HOH   116 516 56  HOH   HOH A . 
C 3 HOH   117 517 127 HOH   HOH A . 
C 3 HOH   118 518 115 HOH   HOH A . 
C 3 HOH   119 519 42  HOH   HOH A . 
C 3 HOH   120 520 120 HOH   HOH A . 
C 3 HOH   121 521 99  HOH   HOH A . 
C 3 HOH   122 522 50  HOH   HOH A . 
C 3 HOH   123 523 106 HOH   HOH A . 
C 3 HOH   124 524 61  HOH   HOH A . 
C 3 HOH   125 525 122 HOH   HOH A . 
C 3 HOH   126 526 83  HOH   HOH A . 
C 3 HOH   127 527 71  HOH   HOH A . 
C 3 HOH   128 528 132 HOH   HOH A . 
C 3 HOH   129 529 119 HOH   HOH A . 
C 3 HOH   130 530 84  HOH   HOH A . 
C 3 HOH   131 531 66  HOH   HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? '2.11.8 (26-JUL-2023)' 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .                      3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                      4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                      5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.01 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H8E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.113 
_cell.length_a_esd                 ? 
_cell.length_b                     67.196 
_cell.length_b_esd                 ? 
_cell.length_c                     59.628 
_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                         9H8E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9H8E 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.92 
_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              8.5 
_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    
'24 % PEG400, 0.1 M PCTP pH 8.5, co-crystallised with 1 mM inhibitor, cryoprotected with 20 % ethylene glyco' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 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         2022-10-05 
_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   0.9795 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.631 
_reflns.d_resolution_low                               59.300 
_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                                     23396 
_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                           61.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.0 
_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                                0.044 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       79663 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.037 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.631 
_reflns_shell.d_res_low                                     1.782 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           3769 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1170 
_reflns_shell.percent_possible_obs                          13.2 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               0.886 
_reflns_shell.pdbx_Rpim_I_all                               0.481 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.741 
_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]                            -2.50960 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.96030 
_refine.aniso_B[2][2]                            -0.92460 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            3.43420 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.11 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_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                                 9H8E 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.631 
_refine.ls_d_res_low                             59.30 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     23394 
_refine.ls_number_reflns_R_free                  1159 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    61.1 
_refine.ls_percent_reflns_R_free                 4.950 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1945 
_refine.ls_R_factor_R_free                       0.2185 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1933 
_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                    ? 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.135 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.134 
_refine.pdbx_overall_SU_R_Blow_DPI               0.155 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.156 
_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_analyze.entry_id                        9H8E 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.631 
_refine_hist.d_res_low                        59.30 
_refine_hist.number_atoms_solvent             131 
_refine_hist.number_atoms_total               2434 
_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        2269 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_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' ? 0.009 ? 2355 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.93  ? 3185 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 838  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 388  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2355 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.23  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.22 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 294  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2093 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.631 
_refine_ls_shell.d_res_low                        1.73 
_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             445 
_refine_ls_shell.percent_reflns_obs               7.55 
_refine_ls_shell.percent_reflns_R_free            4.91 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2824 
_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                  0.3108 
# 
_struct.entry_id                     9H8E 
_struct.title                        'Crystal structure of HPK1 T165E/S171E in complex with compound 13' 
_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        9H8E 
_struct_keywords.text            'TRANSFERASE, Kinase, type 1 inhibitor, structure-based drug design' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    M4K1_HUMAN 
_struct_ref.pdbx_db_accession          Q92918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSY
LWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQ
IGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKG
KWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKN
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H8E 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 294 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q92918 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  293 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       293 
# 
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 9H8E GLY A 1   ? UNP Q92918 ?   ?   'expression tag'      0   1 
1 9H8E SER A 2   ? UNP Q92918 ?   ?   'expression tag'      1   2 
1 9H8E GLU A 166 ? UNP Q92918 THR 165 'engineered mutation' 165 3 
1 9H8E GLU A 172 ? UNP Q92918 SER 171 'engineered mutation' 171 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     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)' 870   ? 
1 MORE         1     ? 
1 'SSA (A^2)'  13770 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 13  ? ASP A 16  ? ASP A 12  ASP A 15  5 ? 4  
HELX_P HELX_P2  AA2 ASP A 56  ? CYS A 70  ? ASP A 55  CYS A 69  1 ? 15 
HELX_P HELX_P3  AA3 SER A 99  ? GLY A 108 ? SER A 98  GLY A 107 1 ? 10 
HELX_P HELX_P4  AA4 SER A 111 ? GLN A 132 ? SER A 110 GLN A 131 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 140 ? ALA A 142 ? LYS A 139 ALA A 141 5 ? 3  
HELX_P HELX_P6  AA6 ALA A 165 ? GLU A 172 ? ALA A 164 GLU A 171 1 ? 8  
HELX_P HELX_P7  AA7 PHE A 173 ? THR A 176 ? PHE A 172 THR A 175 5 ? 4  
HELX_P HELX_P8  AA8 ALA A 181 ? ALA A 186 ? ALA A 180 ALA A 185 1 ? 6  
HELX_P HELX_P9  AA9 LEU A 196 ? LEU A 212 ? LEU A 195 LEU A 211 1 ? 17 
HELX_P HELX_P10 AB1 HIS A 220 ? THR A 229 ? HIS A 219 THR A 228 1 ? 10 
HELX_P HELX_P11 AB2 SER A 245 ? LEU A 256 ? SER A 244 LEU A 255 1 ? 12 
HELX_P HELX_P12 AB3 SER A 265 ? LEU A 270 ? SER A 264 LEU A 269 1 ? 6  
HELX_P HELX_P13 AB4 ARG A 282 ? LYS A 291 ? ARG A 281 LYS A 290 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 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 ? 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 
# 
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 ILE A 9   ? PHE A 10  ? ILE A 8   PHE A 9   
AA1 2 TYR A 78  ? TRP A 84  ? TYR A 77  TRP A 83  
AA1 3 LYS A 87  ? GLU A 93  ? LYS A 86  GLU A 92  
AA1 4 LEU A 43  ? LYS A 50  ? LEU A 42  LYS A 49  
AA1 5 GLY A 30  ? ASP A 37  ? GLY A 29  ASP A 36  
AA1 6 TYR A 18  ? GLY A 27  ? TYR A 17  GLY A 26  
AA2 1 ILE A 144 ? ILE A 146 ? ILE A 143 ILE A 145 
AA2 2 VAL A 152 ? LEU A 154 ? VAL A 151 LEU A 153 
# 
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 PHE A 10  ? N PHE A 9   O SER A 81  ? O SER A 80  
AA1 2 3 N TYR A 82  ? N TYR A 81  O TRP A 89  ? O TRP A 88  
AA1 3 4 O LEU A 88  ? O LEU A 87  N VAL A 49  ? N VAL A 48  
AA1 4 5 O LEU A 46  ? O LEU A 45  N PHE A 33  ? N PHE A 32  
AA1 5 6 O LYS A 34  ? O LYS A 33  N GLN A 22  ? N GLN A 21  
AA2 1 2 N LEU A 145 ? N LEU A 144 O ARG A 153 ? O ARG A 152 
# 
_pdbx_entry_details.entry_id                   9H8E 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 20  ? ? -93.93  -147.54 
2 1 VAL A 105 ? ? -120.06 -59.14  
3 1 ASP A 137 ? ? -147.40 32.68   
4 1 THR A 175 ? ? -151.93 70.96   
5 1 ALA A 185 ? ? -81.95  42.99   
6 1 THR A 228 ? ? -92.72  30.24   
7 1 LYS A 242 ? ? -141.11 -40.91  
8 1 LEU A 255 ? ? -92.31  40.11   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 467 ? C HOH . 
2 1 A HOH 524 ? C HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         16.8535 
_pdbx_refine_tls.origin_y         0.0261 
_pdbx_refine_tls.origin_z         11.1035 
_pdbx_refine_tls.T[1][1]          -0.0947 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0168 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0107 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0806 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0040 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0254 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.6767 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.1163 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4469 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          3.0195 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0723 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.2627 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0656 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.3575 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1052 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3786 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0142 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0140 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1171 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0925 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0513 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   '{ A|* }' 
# 
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 GLY 0 ? A GLY 1 
2 1 Y 1 A SER 1 ? A SER 2 
3 1 Y 1 A ASP 2 ? A ASP 3 
4 1 Y 1 A VAL 3 ? A VAL 4 
5 1 Y 1 A VAL 4 ? A VAL 5 
6 1 Y 1 A ASP 5 ? A ASP 6 
7 1 Y 1 A PRO 6 ? A PRO 7 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ITA C1   C Y N 1   
A1ITA C2   C Y N 2   
A1ITA C3   C Y N 3   
A1ITA N6   N Y N 4   
A1ITA C7   C Y N 5   
A1ITA C8   C Y N 6   
A1ITA C9   C Y N 7   
A1ITA C10  C Y N 8   
A1ITA C11  C N N 9   
A1ITA C12  C N N 10  
A1ITA C13  C N N 11  
A1ITA C14  C N N 12  
A1ITA C15  C N N 13  
A1ITA C16  C Y N 14  
A1ITA C19  C Y N 15  
A1ITA C20  C Y N 16  
A1ITA C21  C Y N 17  
A1ITA C22  C N N 18  
A1ITA O1   O N N 19  
A1ITA N5   N N N 20  
A1ITA N1   N Y N 21  
A1ITA N7   N Y N 22  
A1ITA N8   N Y N 23  
A1ITA C18  C Y N 24  
A1ITA C17  C Y N 25  
A1ITA C4   C Y N 26  
A1ITA N2   N Y N 27  
A1ITA N    N N N 28  
A1ITA C    C N N 29  
A1ITA N3   N N N 30  
A1ITA C5   C Y N 31  
A1ITA C6   C Y N 32  
A1ITA N4   N N N 33  
A1ITA O    O N N 34  
A1ITA H1   H N N 35  
A1ITA H2   H N N 36  
A1ITA H3   H N N 37  
A1ITA H4   H N N 38  
A1ITA H5   H N N 39  
A1ITA H6   H N N 40  
A1ITA H7   H N N 41  
A1ITA H8   H N N 42  
A1ITA H9   H N N 43  
A1ITA H10  H N N 44  
A1ITA H11  H N N 45  
A1ITA H12  H N N 46  
A1ITA H13  H N N 47  
A1ITA H14  H N N 48  
A1ITA H15  H N N 49  
A1ITA H16  H N N 50  
A1ITA H17  H N N 51  
A1ITA H18  H N N 52  
A1ITA H19  H N N 53  
A1ITA H20  H N N 54  
A1ITA H21  H N N 55  
A1ITA H22  H N N 56  
A1ITA H23  H N N 57  
A1ITA H24  H N N 58  
A1ITA H25  H N N 59  
ALA   N    N N N 60  
ALA   CA   C N S 61  
ALA   C    C N N 62  
ALA   O    O N N 63  
ALA   CB   C N N 64  
ALA   OXT  O N N 65  
ALA   H    H N N 66  
ALA   H2   H N N 67  
ALA   HA   H N N 68  
ALA   HB1  H N N 69  
ALA   HB2  H N N 70  
ALA   HB3  H N N 71  
ALA   HXT  H N N 72  
ARG   N    N N N 73  
ARG   CA   C N S 74  
ARG   C    C N N 75  
ARG   O    O N N 76  
ARG   CB   C N N 77  
ARG   CG   C N N 78  
ARG   CD   C N N 79  
ARG   NE   N N N 80  
ARG   CZ   C N N 81  
ARG   NH1  N N N 82  
ARG   NH2  N N N 83  
ARG   OXT  O N N 84  
ARG   H    H N N 85  
ARG   H2   H N N 86  
ARG   HA   H N N 87  
ARG   HB2  H N N 88  
ARG   HB3  H N N 89  
ARG   HG2  H N N 90  
ARG   HG3  H N N 91  
ARG   HD2  H N N 92  
ARG   HD3  H N N 93  
ARG   HE   H N N 94  
ARG   HH11 H N N 95  
ARG   HH12 H N N 96  
ARG   HH21 H N N 97  
ARG   HH22 H N N 98  
ARG   HXT  H N N 99  
ASN   N    N N N 100 
ASN   CA   C N S 101 
ASN   C    C N N 102 
ASN   O    O N N 103 
ASN   CB   C N N 104 
ASN   CG   C N N 105 
ASN   OD1  O N N 106 
ASN   ND2  N N N 107 
ASN   OXT  O N N 108 
ASN   H    H N N 109 
ASN   H2   H N N 110 
ASN   HA   H N N 111 
ASN   HB2  H N N 112 
ASN   HB3  H N N 113 
ASN   HD21 H N N 114 
ASN   HD22 H N N 115 
ASN   HXT  H N N 116 
ASP   N    N N N 117 
ASP   CA   C N S 118 
ASP   C    C N N 119 
ASP   O    O N N 120 
ASP   CB   C N N 121 
ASP   CG   C N N 122 
ASP   OD1  O N N 123 
ASP   OD2  O N N 124 
ASP   OXT  O N N 125 
ASP   H    H N N 126 
ASP   H2   H N N 127 
ASP   HA   H N N 128 
ASP   HB2  H N N 129 
ASP   HB3  H N N 130 
ASP   HD2  H N N 131 
ASP   HXT  H N N 132 
CYS   N    N N N 133 
CYS   CA   C N R 134 
CYS   C    C N N 135 
CYS   O    O N N 136 
CYS   CB   C N N 137 
CYS   SG   S N N 138 
CYS   OXT  O N N 139 
CYS   H    H N N 140 
CYS   H2   H N N 141 
CYS   HA   H N N 142 
CYS   HB2  H N N 143 
CYS   HB3  H N N 144 
CYS   HG   H N N 145 
CYS   HXT  H N N 146 
GLN   N    N N N 147 
GLN   CA   C N S 148 
GLN   C    C N N 149 
GLN   O    O N N 150 
GLN   CB   C N N 151 
GLN   CG   C N N 152 
GLN   CD   C N N 153 
GLN   OE1  O N N 154 
GLN   NE2  N N N 155 
GLN   OXT  O N N 156 
GLN   H    H N N 157 
GLN   H2   H N N 158 
GLN   HA   H N N 159 
GLN   HB2  H N N 160 
GLN   HB3  H N N 161 
GLN   HG2  H N N 162 
GLN   HG3  H N N 163 
GLN   HE21 H N N 164 
GLN   HE22 H N N 165 
GLN   HXT  H N N 166 
GLU   N    N N N 167 
GLU   CA   C N S 168 
GLU   C    C N N 169 
GLU   O    O N N 170 
GLU   CB   C N N 171 
GLU   CG   C N N 172 
GLU   CD   C N N 173 
GLU   OE1  O N N 174 
GLU   OE2  O N N 175 
GLU   OXT  O N N 176 
GLU   H    H N N 177 
GLU   H2   H N N 178 
GLU   HA   H N N 179 
GLU   HB2  H N N 180 
GLU   HB3  H N N 181 
GLU   HG2  H N N 182 
GLU   HG3  H N N 183 
GLU   HE2  H N N 184 
GLU   HXT  H N N 185 
GLY   N    N N N 186 
GLY   CA   C N N 187 
GLY   C    C N N 188 
GLY   O    O N N 189 
GLY   OXT  O N N 190 
GLY   H    H N N 191 
GLY   H2   H N N 192 
GLY   HA2  H N N 193 
GLY   HA3  H N N 194 
GLY   HXT  H N N 195 
HIS   N    N N N 196 
HIS   CA   C N S 197 
HIS   C    C N N 198 
HIS   O    O N N 199 
HIS   CB   C N N 200 
HIS   CG   C Y N 201 
HIS   ND1  N Y N 202 
HIS   CD2  C Y N 203 
HIS   CE1  C Y N 204 
HIS   NE2  N Y N 205 
HIS   OXT  O N N 206 
HIS   H    H N N 207 
HIS   H2   H N N 208 
HIS   HA   H N N 209 
HIS   HB2  H N N 210 
HIS   HB3  H N N 211 
HIS   HD1  H N N 212 
HIS   HD2  H N N 213 
HIS   HE1  H N N 214 
HIS   HE2  H N N 215 
HIS   HXT  H N N 216 
HOH   O    O N N 217 
HOH   H1   H N N 218 
HOH   H2   H N N 219 
ILE   N    N N N 220 
ILE   CA   C N S 221 
ILE   C    C N N 222 
ILE   O    O N N 223 
ILE   CB   C N S 224 
ILE   CG1  C N N 225 
ILE   CG2  C N N 226 
ILE   CD1  C N N 227 
ILE   OXT  O N N 228 
ILE   H    H N N 229 
ILE   H2   H N N 230 
ILE   HA   H N N 231 
ILE   HB   H N N 232 
ILE   HG12 H N N 233 
ILE   HG13 H N N 234 
ILE   HG21 H N N 235 
ILE   HG22 H N N 236 
ILE   HG23 H N N 237 
ILE   HD11 H N N 238 
ILE   HD12 H N N 239 
ILE   HD13 H N N 240 
ILE   HXT  H N N 241 
LEU   N    N N N 242 
LEU   CA   C N S 243 
LEU   C    C N N 244 
LEU   O    O N N 245 
LEU   CB   C N N 246 
LEU   CG   C N N 247 
LEU   CD1  C N N 248 
LEU   CD2  C N N 249 
LEU   OXT  O N N 250 
LEU   H    H N N 251 
LEU   H2   H N N 252 
LEU   HA   H N N 253 
LEU   HB2  H N N 254 
LEU   HB3  H N N 255 
LEU   HG   H N N 256 
LEU   HD11 H N N 257 
LEU   HD12 H N N 258 
LEU   HD13 H N N 259 
LEU   HD21 H N N 260 
LEU   HD22 H N N 261 
LEU   HD23 H N N 262 
LEU   HXT  H N N 263 
LYS   N    N N N 264 
LYS   CA   C N S 265 
LYS   C    C N N 266 
LYS   O    O N N 267 
LYS   CB   C N N 268 
LYS   CG   C N N 269 
LYS   CD   C N N 270 
LYS   CE   C N N 271 
LYS   NZ   N N N 272 
LYS   OXT  O N N 273 
LYS   H    H N N 274 
LYS   H2   H N N 275 
LYS   HA   H N N 276 
LYS   HB2  H N N 277 
LYS   HB3  H N N 278 
LYS   HG2  H N N 279 
LYS   HG3  H N N 280 
LYS   HD2  H N N 281 
LYS   HD3  H N N 282 
LYS   HE2  H N N 283 
LYS   HE3  H N N 284 
LYS   HZ1  H N N 285 
LYS   HZ2  H N N 286 
LYS   HZ3  H N N 287 
LYS   HXT  H N N 288 
MET   N    N N N 289 
MET   CA   C N S 290 
MET   C    C N N 291 
MET   O    O N N 292 
MET   CB   C N N 293 
MET   CG   C N N 294 
MET   SD   S N N 295 
MET   CE   C N N 296 
MET   OXT  O N N 297 
MET   H    H N N 298 
MET   H2   H N N 299 
MET   HA   H N N 300 
MET   HB2  H N N 301 
MET   HB3  H N N 302 
MET   HG2  H N N 303 
MET   HG3  H N N 304 
MET   HE1  H N N 305 
MET   HE2  H N N 306 
MET   HE3  H N N 307 
MET   HXT  H N N 308 
PHE   N    N N N 309 
PHE   CA   C N S 310 
PHE   C    C N N 311 
PHE   O    O N N 312 
PHE   CB   C N N 313 
PHE   CG   C Y N 314 
PHE   CD1  C Y N 315 
PHE   CD2  C Y N 316 
PHE   CE1  C Y N 317 
PHE   CE2  C Y N 318 
PHE   CZ   C Y N 319 
PHE   OXT  O N N 320 
PHE   H    H N N 321 
PHE   H2   H N N 322 
PHE   HA   H N N 323 
PHE   HB2  H N N 324 
PHE   HB3  H N N 325 
PHE   HD1  H N N 326 
PHE   HD2  H N N 327 
PHE   HE1  H N N 328 
PHE   HE2  H N N 329 
PHE   HZ   H N N 330 
PHE   HXT  H N N 331 
PRO   N    N N N 332 
PRO   CA   C N S 333 
PRO   C    C N N 334 
PRO   O    O N N 335 
PRO   CB   C N N 336 
PRO   CG   C N N 337 
PRO   CD   C N N 338 
PRO   OXT  O N N 339 
PRO   H    H N N 340 
PRO   HA   H N N 341 
PRO   HB2  H N N 342 
PRO   HB3  H N N 343 
PRO   HG2  H N N 344 
PRO   HG3  H N N 345 
PRO   HD2  H N N 346 
PRO   HD3  H N N 347 
PRO   HXT  H N N 348 
SER   N    N N N 349 
SER   CA   C N S 350 
SER   C    C N N 351 
SER   O    O N N 352 
SER   CB   C N N 353 
SER   OG   O N N 354 
SER   OXT  O N N 355 
SER   H    H N N 356 
SER   H2   H N N 357 
SER   HA   H N N 358 
SER   HB2  H N N 359 
SER   HB3  H N N 360 
SER   HG   H N N 361 
SER   HXT  H N N 362 
THR   N    N N N 363 
THR   CA   C N S 364 
THR   C    C N N 365 
THR   O    O N N 366 
THR   CB   C N R 367 
THR   OG1  O N N 368 
THR   CG2  C N N 369 
THR   OXT  O N N 370 
THR   H    H N N 371 
THR   H2   H N N 372 
THR   HA   H N N 373 
THR   HB   H N N 374 
THR   HG1  H N N 375 
THR   HG21 H N N 376 
THR   HG22 H N N 377 
THR   HG23 H N N 378 
THR   HXT  H N N 379 
TRP   N    N N N 380 
TRP   CA   C N S 381 
TRP   C    C N N 382 
TRP   O    O N N 383 
TRP   CB   C N N 384 
TRP   CG   C Y N 385 
TRP   CD1  C Y N 386 
TRP   CD2  C Y N 387 
TRP   NE1  N Y N 388 
TRP   CE2  C Y N 389 
TRP   CE3  C Y N 390 
TRP   CZ2  C Y N 391 
TRP   CZ3  C Y N 392 
TRP   CH2  C Y N 393 
TRP   OXT  O N N 394 
TRP   H    H N N 395 
TRP   H2   H N N 396 
TRP   HA   H N N 397 
TRP   HB2  H N N 398 
TRP   HB3  H N N 399 
TRP   HD1  H N N 400 
TRP   HE1  H N N 401 
TRP   HE3  H N N 402 
TRP   HZ2  H N N 403 
TRP   HZ3  H N N 404 
TRP   HH2  H N N 405 
TRP   HXT  H N N 406 
TYR   N    N N N 407 
TYR   CA   C N S 408 
TYR   C    C N N 409 
TYR   O    O N N 410 
TYR   CB   C N N 411 
TYR   CG   C Y N 412 
TYR   CD1  C Y N 413 
TYR   CD2  C Y N 414 
TYR   CE1  C Y N 415 
TYR   CE2  C Y N 416 
TYR   CZ   C Y N 417 
TYR   OH   O N N 418 
TYR   OXT  O N N 419 
TYR   H    H N N 420 
TYR   H2   H N N 421 
TYR   HA   H N N 422 
TYR   HB2  H N N 423 
TYR   HB3  H N N 424 
TYR   HD1  H N N 425 
TYR   HD2  H N N 426 
TYR   HE1  H N N 427 
TYR   HE2  H N N 428 
TYR   HH   H N N 429 
TYR   HXT  H N N 430 
VAL   N    N N N 431 
VAL   CA   C N S 432 
VAL   C    C N N 433 
VAL   O    O N N 434 
VAL   CB   C N N 435 
VAL   CG1  C N N 436 
VAL   CG2  C N N 437 
VAL   OXT  O N N 438 
VAL   H    H N N 439 
VAL   H2   H N N 440 
VAL   HA   H N N 441 
VAL   HB   H N N 442 
VAL   HG11 H N N 443 
VAL   HG12 H N N 444 
VAL   HG13 H N N 445 
VAL   HG21 H N N 446 
VAL   HG22 H N N 447 
VAL   HG23 H N N 448 
VAL   HXT  H N N 449 
# 
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 
A1ITA C22 N8   sing N N 1   
A1ITA C21 N8   sing Y N 2   
A1ITA C21 N7   doub Y N 3   
A1ITA N8  C19  sing Y N 4   
A1ITA N7  C20  sing Y N 5   
A1ITA C13 C14  sing N N 6   
A1ITA C13 O    sing N N 7   
A1ITA C14 N4   sing N N 8   
A1ITA C19 C20  doub Y N 9   
A1ITA C19 C18  sing Y N 10  
A1ITA O   C12  sing N N 11  
A1ITA C   N    sing N N 12  
A1ITA C20 C16  sing Y N 13  
A1ITA N   C1   sing N N 14  
A1ITA C18 N6   doub Y N 15  
A1ITA C7  C6   doub Y N 16  
A1ITA C7  C8   sing Y N 17  
A1ITA N4  C8   sing N N 18  
A1ITA N4  C11  sing N N 19  
A1ITA C12 C11  sing N N 20  
A1ITA C1  N2   doub Y N 21  
A1ITA C1  C2   sing Y N 22  
A1ITA C16 C2   sing N N 23  
A1ITA C16 C17  doub Y N 24  
A1ITA C6  C5   sing Y N 25  
A1ITA C8  C9   doub Y N 26  
A1ITA N2  C4   sing Y N 27  
A1ITA C2  N1   doub Y N 28  
A1ITA N6  C17  sing Y N 29  
A1ITA C5  N3   sing N N 30  
A1ITA C5  C10  doub Y N 31  
A1ITA C9  C10  sing Y N 32  
A1ITA C4  N3   sing N N 33  
A1ITA C4  C3   doub Y N 34  
A1ITA N1  C3   sing Y N 35  
A1ITA C3  C15  sing N N 36  
A1ITA C15 O1   doub N N 37  
A1ITA C15 N5   sing N N 38  
A1ITA C7  H1   sing N N 39  
A1ITA C9  H2   sing N N 40  
A1ITA C10 H3   sing N N 41  
A1ITA C11 H4   sing N N 42  
A1ITA C11 H5   sing N N 43  
A1ITA C12 H6   sing N N 44  
A1ITA C12 H7   sing N N 45  
A1ITA C13 H8   sing N N 46  
A1ITA C13 H9   sing N N 47  
A1ITA C14 H10  sing N N 48  
A1ITA C14 H11  sing N N 49  
A1ITA C21 H12  sing N N 50  
A1ITA C22 H13  sing N N 51  
A1ITA C22 H14  sing N N 52  
A1ITA C22 H15  sing N N 53  
A1ITA N5  H16  sing N N 54  
A1ITA N5  H17  sing N N 55  
A1ITA C18 H18  sing N N 56  
A1ITA C17 H19  sing N N 57  
A1ITA N   H20  sing N N 58  
A1ITA C   H21  sing N N 59  
A1ITA C   H22  sing N N 60  
A1ITA C   H23  sing N N 61  
A1ITA N3  H24  sing N N 62  
A1ITA C6  H25  sing N N 63  
ALA   N   CA   sing N N 64  
ALA   N   H    sing N N 65  
ALA   N   H2   sing N N 66  
ALA   CA  C    sing N N 67  
ALA   CA  CB   sing N N 68  
ALA   CA  HA   sing N N 69  
ALA   C   O    doub N N 70  
ALA   C   OXT  sing N N 71  
ALA   CB  HB1  sing N N 72  
ALA   CB  HB2  sing N N 73  
ALA   CB  HB3  sing N N 74  
ALA   OXT HXT  sing N N 75  
ARG   N   CA   sing N N 76  
ARG   N   H    sing N N 77  
ARG   N   H2   sing N N 78  
ARG   CA  C    sing N N 79  
ARG   CA  CB   sing N N 80  
ARG   CA  HA   sing N N 81  
ARG   C   O    doub N N 82  
ARG   C   OXT  sing N N 83  
ARG   CB  CG   sing N N 84  
ARG   CB  HB2  sing N N 85  
ARG   CB  HB3  sing N N 86  
ARG   CG  CD   sing N N 87  
ARG   CG  HG2  sing N N 88  
ARG   CG  HG3  sing N N 89  
ARG   CD  NE   sing N N 90  
ARG   CD  HD2  sing N N 91  
ARG   CD  HD3  sing N N 92  
ARG   NE  CZ   sing N N 93  
ARG   NE  HE   sing N N 94  
ARG   CZ  NH1  sing N N 95  
ARG   CZ  NH2  doub N N 96  
ARG   NH1 HH11 sing N N 97  
ARG   NH1 HH12 sing N N 98  
ARG   NH2 HH21 sing N N 99  
ARG   NH2 HH22 sing N N 100 
ARG   OXT HXT  sing N N 101 
ASN   N   CA   sing N N 102 
ASN   N   H    sing N N 103 
ASN   N   H2   sing N N 104 
ASN   CA  C    sing N N 105 
ASN   CA  CB   sing N N 106 
ASN   CA  HA   sing N N 107 
ASN   C   O    doub N N 108 
ASN   C   OXT  sing N N 109 
ASN   CB  CG   sing N N 110 
ASN   CB  HB2  sing N N 111 
ASN   CB  HB3  sing N N 112 
ASN   CG  OD1  doub N N 113 
ASN   CG  ND2  sing N N 114 
ASN   ND2 HD21 sing N N 115 
ASN   ND2 HD22 sing N N 116 
ASN   OXT HXT  sing N N 117 
ASP   N   CA   sing N N 118 
ASP   N   H    sing N N 119 
ASP   N   H2   sing N N 120 
ASP   CA  C    sing N N 121 
ASP   CA  CB   sing N N 122 
ASP   CA  HA   sing N N 123 
ASP   C   O    doub N N 124 
ASP   C   OXT  sing N N 125 
ASP   CB  CG   sing N N 126 
ASP   CB  HB2  sing N N 127 
ASP   CB  HB3  sing N N 128 
ASP   CG  OD1  doub N N 129 
ASP   CG  OD2  sing N N 130 
ASP   OD2 HD2  sing N N 131 
ASP   OXT HXT  sing N N 132 
CYS   N   CA   sing N N 133 
CYS   N   H    sing N N 134 
CYS   N   H2   sing N N 135 
CYS   CA  C    sing N N 136 
CYS   CA  CB   sing N N 137 
CYS   CA  HA   sing N N 138 
CYS   C   O    doub N N 139 
CYS   C   OXT  sing N N 140 
CYS   CB  SG   sing N N 141 
CYS   CB  HB2  sing N N 142 
CYS   CB  HB3  sing N N 143 
CYS   SG  HG   sing N N 144 
CYS   OXT HXT  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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                    9H8E 
_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]   0.012802 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001348 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014882 
_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]   0.016863 
_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 
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   . ASP   A 1 8   ? 5.093   -0.690  34.303  1.00 80.88 ? 7   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 8   ? 5.652   -0.755  32.948  1.00 81.67 ? 7   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 8   ? 5.477   0.570   32.205  1.00 81.43 ? 7   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 8   ? 6.383   0.992   31.482  1.00 81.59 ? 7   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 8   ? 5.009   -1.893  32.126  1.00 84.02 ? 7   ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 8   ? 5.250   -3.292  32.667  1.00 89.66 ? 7   ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 8   ? 5.268   -3.456  33.910  1.00 90.44 ? 7   ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 8   ? 5.404   -4.228  31.846  1.00 92.26 ? 7   ASP   A OD2 1 
ATOM   9    N N   . ILE   A 1 9   ? 4.288   1.195   32.348  1.00 80.75 ? 8   ILE   A N   1 
ATOM   10   C CA  . ILE   A 1 9   ? 3.925   2.466   31.719  1.00 80.58 ? 8   ILE   A CA  1 
ATOM   11   C C   . ILE   A 1 9   ? 3.535   3.422   32.823  1.00 81.14 ? 8   ILE   A C   1 
ATOM   12   O O   . ILE   A 1 9   ? 2.381   3.429   33.255  1.00 81.39 ? 8   ILE   A O   1 
ATOM   13   C CB  . ILE   A 1 9   ? 2.760   2.287   30.713  1.00 80.65 ? 8   ILE   A CB  1 
ATOM   14   C CG1 . ILE   A 1 9   ? 3.035   1.129   29.733  1.00 81.39 ? 8   ILE   A CG1 1 
ATOM   15   C CG2 . ILE   A 1 9   ? 2.449   3.602   29.990  1.00 80.89 ? 8   ILE   A CG2 1 
ATOM   16   C CD1 . ILE   A 1 9   ? 1.949   0.839   28.736  1.00 82.75 ? 8   ILE   A CD1 1 
ATOM   17   N N   . PHE   A 1 10  ? 4.498   4.201   33.315  1.00 81.26 ? 9   PHE   A N   1 
ATOM   18   C CA  . PHE   A 1 10  ? 4.237   5.125   34.411  1.00 81.99 ? 9   PHE   A CA  1 
ATOM   19   C C   . PHE   A 1 10  ? 3.380   6.302   33.994  1.00 81.26 ? 9   PHE   A C   1 
ATOM   20   O O   . PHE   A 1 10  ? 3.707   7.002   33.043  1.00 81.01 ? 9   PHE   A O   1 
ATOM   21   C CB  . PHE   A 1 10  ? 5.547   5.600   35.041  1.00 82.80 ? 9   PHE   A CB  1 
ATOM   22   C CG  . PHE   A 1 10  ? 6.346   4.477   35.656  1.00 84.54 ? 9   PHE   A CG  1 
ATOM   23   C CD1 . PHE   A 1 10  ? 5.960   3.907   36.858  1.00 85.94 ? 9   PHE   A CD1 1 
ATOM   24   C CD2 . PHE   A 1 10  ? 7.492   4.003   35.043  1.00 85.61 ? 9   PHE   A CD2 1 
ATOM   25   C CE1 . PHE   A 1 10  ? 6.698   2.878   37.428  1.00 86.75 ? 9   PHE   A CE1 1 
ATOM   26   C CE2 . PHE   A 1 10  ? 8.231   2.980   35.618  1.00 86.62 ? 9   PHE   A CE2 1 
ATOM   27   C CZ  . PHE   A 1 10  ? 7.835   2.431   36.814  1.00 86.50 ? 9   PHE   A CZ  1 
ATOM   28   N N   . ASN   A 1 11  ? 2.275   6.514   34.697  1.00 80.92 ? 10  ASN   A N   1 
ATOM   29   C CA  . ASN   A 1 11  ? 1.375   7.637   34.440  1.00 81.23 ? 10  ASN   A CA  1 
ATOM   30   C C   . ASN   A 1 11  ? 1.944   8.911   35.083  1.00 79.93 ? 10  ASN   A C   1 
ATOM   31   O O   . ASN   A 1 11  ? 1.353   9.470   36.010  1.00 79.50 ? 10  ASN   A O   1 
ATOM   32   C CB  . ASN   A 1 11  ? -0.034  7.350   34.990  1.00 83.45 ? 10  ASN   A CB  1 
ATOM   33   C CG  . ASN   A 1 11  ? -1.120  8.083   34.243  1.00 88.52 ? 10  ASN   A CG  1 
ATOM   34   O OD1 . ASN   A 1 11  ? -1.113  8.176   32.999  1.00 90.59 ? 10  ASN   A OD1 1 
ATOM   35   N ND2 . ASN   A 1 11  ? -2.076  8.615   34.982  1.00 90.09 ? 10  ASN   A ND2 1 
ATOM   36   N N   . ARG   A 1 12  ? 3.106   9.351   34.588  1.00 78.98 ? 11  ARG   A N   1 
ATOM   37   C CA  . ARG   A 1 12  ? 3.785   10.549  35.047  1.00 79.02 ? 11  ARG   A CA  1 
ATOM   38   C C   . ARG   A 1 12  ? 4.715   11.144  33.983  1.00 78.43 ? 11  ARG   A C   1 
ATOM   39   O O   . ARG   A 1 12  ? 4.961   10.533  32.945  1.00 77.90 ? 11  ARG   A O   1 
ATOM   40   C CB  . ARG   A 1 12  ? 4.501   10.324  36.384  1.00 81.18 ? 11  ARG   A CB  1 
ATOM   41   C CG  . ARG   A 1 12  ? 5.772   9.504   36.312  1.00 83.97 ? 11  ARG   A CG  1 
ATOM   42   C CD  . ARG   A 1 12  ? 6.579   9.670   37.593  1.00 87.49 ? 11  ARG   A CD  1 
ATOM   43   N NE  . ARG   A 1 12  ? 5.787   9.409   38.799  1.00 90.79 ? 11  ARG   A NE  1 
ATOM   44   C CZ  . ARG   A 1 12  ? 6.214   9.616   40.039  1.00 93.17 ? 11  ARG   A CZ  1 
ATOM   45   N NH1 . ARG   A 1 12  ? 5.426   9.348   41.068  1.00 93.91 ? 11  ARG   A NH1 1 
ATOM   46   N NH2 . ARG   A 1 12  ? 7.433   10.092  40.259  1.00 93.06 ? 11  ARG   A NH2 1 
ATOM   47   N N   . ASP   A 1 13  ? 5.157   12.379  34.212  1.00 78.15 ? 12  ASP   A N   1 
ATOM   48   C CA  . ASP   A 1 13  ? 6.037   13.109  33.317  1.00 78.25 ? 12  ASP   A CA  1 
ATOM   49   C C   . ASP   A 1 13  ? 7.411   12.480  33.439  1.00 77.88 ? 12  ASP   A C   1 
ATOM   50   O O   . ASP   A 1 13  ? 7.929   12.403  34.553  1.00 78.44 ? 12  ASP   A O   1 
ATOM   51   C CB  . ASP   A 1 13  ? 6.100   14.572  33.804  1.00 80.13 ? 12  ASP   A CB  1 
ATOM   52   C CG  . ASP   A 1 13  ? 6.747   15.566  32.861  1.00 85.31 ? 12  ASP   A CG  1 
ATOM   53   O OD1 . ASP   A 1 13  ? 7.304   15.136  31.835  1.00 85.85 ? 12  ASP   A OD1 1 
ATOM   54   O OD2 . ASP   A 1 13  ? 6.695   16.778  33.155  1.00 88.71 ? 12  ASP   A OD2 1 
ATOM   55   N N   . PRO   A 1 14  ? 8.044   12.046  32.333  1.00 77.01 ? 13  PRO   A N   1 
ATOM   56   C CA  . PRO   A 1 14  ? 9.399   11.481  32.450  1.00 76.53 ? 13  PRO   A CA  1 
ATOM   57   C C   . PRO   A 1 14  ? 10.422  12.488  32.987  1.00 76.44 ? 13  PRO   A C   1 
ATOM   58   O O   . PRO   A 1 14  ? 11.469  12.068  33.462  1.00 76.43 ? 13  PRO   A O   1 
ATOM   59   C CB  . PRO   A 1 14  ? 9.724   11.030  31.027  1.00 76.86 ? 13  PRO   A CB  1 
ATOM   60   C CG  . PRO   A 1 14  ? 8.861   11.862  30.170  1.00 77.54 ? 13  PRO   A CG  1 
ATOM   61   C CD  . PRO   A 1 14  ? 7.586   12.055  30.932  1.00 76.19 ? 13  PRO   A CD  1 
ATOM   62   N N   . ARG   A 1 15  ? 10.113  13.806  32.948  1.00 76.20 ? 14  ARG   A N   1 
ATOM   63   C CA  . ARG   A 1 15  ? 10.972  14.854  33.503  1.00 77.07 ? 14  ARG   A CA  1 
ATOM   64   C C   . ARG   A 1 15  ? 11.161  14.721  35.018  1.00 77.76 ? 14  ARG   A C   1 
ATOM   65   O O   . ARG   A 1 15  ? 12.087  15.315  35.557  1.00 78.31 ? 14  ARG   A O   1 
ATOM   66   C CB  . ARG   A 1 15  ? 10.452  16.254  33.145  1.00 78.67 ? 14  ARG   A CB  1 
ATOM   67   C CG  . ARG   A 1 15  ? 10.768  16.627  31.703  1.00 82.94 ? 14  ARG   A CG  1 
ATOM   68   C CD  . ARG   A 1 15  ? 9.947   17.805  31.212  1.00 86.39 ? 14  ARG   A CD  1 
ATOM   69   N NE  . ARG   A 1 15  ? 9.892   17.822  29.746  1.00 89.20 ? 14  ARG   A NE  1 
ATOM   70   C CZ  . ARG   A 1 15  ? 8.951   17.222  29.023  1.00 90.88 ? 14  ARG   A CZ  1 
ATOM   71   N NH1 . ARG   A 1 15  ? 7.967   16.558  29.618  1.00 90.41 ? 14  ARG   A NH1 1 
ATOM   72   N NH2 . ARG   A 1 15  ? 8.979   17.289  27.698  1.00 90.55 ? 14  ARG   A NH2 1 
ATOM   73   N N   . ASP   A 1 16  ? 10.295  13.953  35.707  1.00 77.62 ? 15  ASP   A N   1 
ATOM   74   C CA  . ASP   A 1 16  ? 10.439  13.694  37.137  1.00 78.07 ? 15  ASP   A CA  1 
ATOM   75   C C   . ASP   A 1 16  ? 11.712  12.871  37.396  1.00 77.71 ? 15  ASP   A C   1 
ATOM   76   O O   . ASP   A 1 16  ? 12.353  13.051  38.425  1.00 78.24 ? 15  ASP   A O   1 
ATOM   77   C CB  . ASP   A 1 16  ? 9.227   12.910  37.668  1.00 80.58 ? 15  ASP   A CB  1 
ATOM   78   C CG  . ASP   A 1 16  ? 7.942   13.706  37.757  1.00 87.37 ? 15  ASP   A CG  1 
ATOM   79   O OD1 . ASP   A 1 16  ? 8.012   14.909  38.072  1.00 88.91 ? 15  ASP   A OD1 1 
ATOM   80   O OD2 . ASP   A 1 16  ? 6.865   13.119  37.532  1.00 90.52 ? 15  ASP   A OD2 1 
ATOM   81   N N   . HIS   A 1 17  ? 12.071  11.965  36.473  1.00 76.86 ? 16  HIS   A N   1 
ATOM   82   C CA  . HIS   A 1 17  ? 13.242  11.109  36.636  1.00 76.74 ? 16  HIS   A CA  1 
ATOM   83   C C   . HIS   A 1 17  ? 14.389  11.455  35.676  1.00 75.57 ? 16  HIS   A C   1 
ATOM   84   O O   . HIS   A 1 17  ? 15.524  11.057  35.926  1.00 76.27 ? 16  HIS   A O   1 
ATOM   85   C CB  . HIS   A 1 17  ? 12.846  9.631   36.439  1.00 78.19 ? 16  HIS   A CB  1 
ATOM   86   C CG  . HIS   A 1 17  ? 11.662  9.206   37.251  1.00 81.08 ? 16  HIS   A CG  1 
ATOM   87   N ND1 . HIS   A 1 17  ? 11.485  9.643   38.552  1.00 83.19 ? 16  HIS   A ND1 1 
ATOM   88   C CD2 . HIS   A 1 17  ? 10.639  8.384   36.924  1.00 82.40 ? 16  HIS   A CD2 1 
ATOM   89   C CE1 . HIS   A 1 17  ? 10.362  9.084   38.971  1.00 83.74 ? 16  HIS   A CE1 1 
ATOM   90   N NE2 . HIS   A 1 17  ? 9.820   8.312   38.030  1.00 83.52 ? 16  HIS   A NE2 1 
ATOM   91   N N   . TYR   A 1 18  ? 14.099  12.143  34.561  1.00 73.54 ? 17  TYR   A N   1 
ATOM   92   C CA  . TYR   A 1 18  ? 15.123  12.455  33.571  1.00 71.77 ? 17  TYR   A CA  1 
ATOM   93   C C   . TYR   A 1 18  ? 15.316  13.934  33.275  1.00 71.65 ? 17  TYR   A C   1 
ATOM   94   O O   . TYR   A 1 18  ? 14.362  14.709  33.196  1.00 71.67 ? 17  TYR   A O   1 
ATOM   95   C CB  . TYR   A 1 18  ? 14.863  11.692  32.262  1.00 70.32 ? 17  TYR   A CB  1 
ATOM   96   C CG  . TYR   A 1 18  ? 14.945  10.193  32.438  1.00 69.21 ? 17  TYR   A CG  1 
ATOM   97   C CD1 . TYR   A 1 18  ? 16.166  9.541   32.445  1.00 69.17 ? 17  TYR   A CD1 1 
ATOM   98   C CD2 . TYR   A 1 18  ? 13.802  9.434   32.628  1.00 69.38 ? 17  TYR   A CD2 1 
ATOM   99   C CE1 . TYR   A 1 18  ? 16.251  8.173   32.669  1.00 69.78 ? 17  TYR   A CE1 1 
ATOM   100  C CE2 . TYR   A 1 18  ? 13.871  8.062   32.819  1.00 69.72 ? 17  TYR   A CE2 1 
ATOM   101  C CZ  . TYR   A 1 18  ? 15.098  7.433   32.846  1.00 70.44 ? 17  TYR   A CZ  1 
ATOM   102  O OH  . TYR   A 1 18  ? 15.160  6.069   33.008  1.00 71.68 ? 17  TYR   A OH  1 
ATOM   103  N N   . ASP   A 1 19  ? 16.578  14.313  33.102  1.00 71.30 ? 18  ASP   A N   1 
ATOM   104  C CA  . ASP   A 1 19  ? 16.968  15.649  32.705  1.00 71.50 ? 18  ASP   A CA  1 
ATOM   105  C C   . ASP   A 1 19  ? 17.049  15.605  31.176  1.00 70.87 ? 18  ASP   A C   1 
ATOM   106  O O   . ASP   A 1 19  ? 17.917  14.916  30.628  1.00 71.25 ? 18  ASP   A O   1 
ATOM   107  C CB  . ASP   A 1 19  ? 18.335  15.985  33.294  1.00 74.17 ? 18  ASP   A CB  1 
ATOM   108  C CG  . ASP   A 1 19  ? 18.305  16.111  34.802  1.00 80.98 ? 18  ASP   A CG  1 
ATOM   109  O OD1 . ASP   A 1 19  ? 17.439  16.852  35.316  1.00 82.01 ? 18  ASP   A OD1 1 
ATOM   110  O OD2 . ASP   A 1 19  ? 19.147  15.463  35.472  1.00 84.07 ? 18  ASP   A OD2 1 
ATOM   111  N N   . LEU   A 1 20  ? 16.105  16.255  30.490  1.00 69.73 ? 19  LEU   A N   1 
ATOM   112  C CA  . LEU   A 1 20  ? 16.088  16.252  29.032  1.00 69.37 ? 19  LEU   A CA  1 
ATOM   113  C C   . LEU   A 1 20  ? 17.197  17.116  28.475  1.00 68.45 ? 19  LEU   A C   1 
ATOM   114  O O   . LEU   A 1 20  ? 17.220  18.320  28.697  1.00 68.85 ? 19  LEU   A O   1 
ATOM   115  C CB  . LEU   A 1 20  ? 14.741  16.736  28.467  1.00 69.82 ? 19  LEU   A CB  1 
ATOM   116  C CG  . LEU   A 1 20  ? 13.629  15.711  28.266  1.00 72.05 ? 19  LEU   A CG  1 
ATOM   117  C CD1 . LEU   A 1 20  ? 12.462  16.335  27.516  1.00 73.05 ? 19  LEU   A CD1 1 
ATOM   118  C CD2 . LEU   A 1 20  ? 14.110  14.505  27.491  1.00 72.54 ? 19  LEU   A CD2 1 
ATOM   119  N N   . LEU   A 1 21  ? 18.113  16.502  27.749  1.00 67.23 ? 20  LEU   A N   1 
ATOM   120  C CA  . LEU   A 1 21  ? 19.196  17.226  27.099  1.00 66.38 ? 20  LEU   A CA  1 
ATOM   121  C C   . LEU   A 1 21  ? 18.776  17.565  25.635  1.00 65.51 ? 20  LEU   A C   1 
ATOM   122  O O   . LEU   A 1 21  ? 17.588  17.818  25.403  1.00 66.60 ? 20  LEU   A O   1 
ATOM   123  C CB  . LEU   A 1 21  ? 20.540  16.464  27.227  1.00 65.99 ? 20  LEU   A CB  1 
ATOM   124  C CG  . LEU   A 1 21  ? 20.968  16.064  28.639  1.00 66.44 ? 20  LEU   A CG  1 
ATOM   125  C CD1 . LEU   A 1 21  ? 22.346  15.475  28.624  1.00 67.19 ? 20  LEU   A CD1 1 
ATOM   126  C CD2 . LEU   A 1 21  ? 20.960  17.239  29.577  1.00 66.34 ? 20  LEU   A CD2 1 
ATOM   127  N N   . GLN   A 1 22  ? 19.706  17.611  24.674  1.00 63.19 ? 21  GLN   A N   1 
ATOM   128  C CA  . GLN   A 1 22  ? 19.385  18.008  23.315  1.00 61.40 ? 21  GLN   A CA  1 
ATOM   129  C C   . GLN   A 1 22  ? 18.560  16.985  22.527  1.00 59.04 ? 21  GLN   A C   1 
ATOM   130  O O   . GLN   A 1 22  ? 18.500  15.799  22.865  1.00 58.79 ? 21  GLN   A O   1 
ATOM   131  C CB  . GLN   A 1 22  ? 20.671  18.386  22.553  1.00 63.67 ? 21  GLN   A CB  1 
ATOM   132  C CG  . GLN   A 1 22  ? 21.497  17.193  22.069  1.00 67.89 ? 21  GLN   A CG  1 
ATOM   133  C CD  . GLN   A 1 22  ? 22.618  16.831  23.009  1.00 74.17 ? 21  GLN   A CD  1 
ATOM   134  O OE1 . GLN   A 1 22  ? 22.652  17.229  24.181  1.00 75.80 ? 21  GLN   A OE1 1 
ATOM   135  N NE2 . GLN   A 1 22  ? 23.569  16.059  22.511  1.00 75.98 ? 21  GLN   A NE2 1 
ATOM   136  N N   . ARG   A 1 23  ? 17.910  17.474  21.472  1.00 56.57 ? 22  ARG   A N   1 
ATOM   137  C CA  . ARG   A 1 23  ? 17.174  16.654  20.550  1.00 54.32 ? 22  ARG   A CA  1 
ATOM   138  C C   . ARG   A 1 23  ? 18.207  15.956  19.676  1.00 52.30 ? 22  ARG   A C   1 
ATOM   139  O O   . ARG   A 1 23  ? 19.131  16.595  19.178  1.00 53.02 ? 22  ARG   A O   1 
ATOM   140  C CB  . ARG   A 1 23  ? 16.260  17.527  19.691  1.00 54.54 ? 22  ARG   A CB  1 
ATOM   141  C CG  . ARG   A 1 23  ? 15.409  16.728  18.721  1.00 54.92 ? 22  ARG   A CG  1 
ATOM   142  C CD  . ARG   A 1 23  ? 14.546  17.644  17.902  1.00 55.73 ? 22  ARG   A CD  1 
ATOM   143  N NE  . ARG   A 1 23  ? 13.717  16.915  16.944  1.00 56.40 ? 22  ARG   A NE  1 
ATOM   144  C CZ  . ARG   A 1 23  ? 14.089  16.619  15.702  1.00 57.13 ? 22  ARG   A CZ  1 
ATOM   145  N NH1 . ARG   A 1 23  ? 13.263  15.973  14.895  1.00 56.44 ? 22  ARG   A NH1 1 
ATOM   146  N NH2 . ARG   A 1 23  ? 15.286  16.975  15.257  1.00 56.39 ? 22  ARG   A NH2 1 
ATOM   147  N N   . LEU   A 1 24  ? 18.086  14.642  19.528  1.00 49.27 ? 23  LEU   A N   1 
ATOM   148  C CA  . LEU   A 1 24  ? 18.993  13.861  18.700  1.00 47.34 ? 23  LEU   A CA  1 
ATOM   149  C C   . LEU   A 1 24  ? 18.492  13.714  17.255  1.00 45.50 ? 23  LEU   A C   1 
ATOM   150  O O   . LEU   A 1 24  ? 19.292  13.515  16.353  1.00 44.68 ? 23  LEU   A O   1 
ATOM   151  C CB  . LEU   A 1 24  ? 19.203  12.482  19.320  1.00 46.96 ? 23  LEU   A CB  1 
ATOM   152  C CG  . LEU   A 1 24  ? 19.753  12.505  20.735  1.00 48.04 ? 23  LEU   A CG  1 
ATOM   153  C CD1 . LEU   A 1 24  ? 19.677  11.119  21.378  1.00 48.47 ? 23  LEU   A CD1 1 
ATOM   154  C CD2 . LEU   A 1 24  ? 21.162  13.051  20.751  1.00 48.52 ? 23  LEU   A CD2 1 
ATOM   155  N N   . GLY   A 1 25  ? 17.179  13.822  17.056  1.00 44.11 ? 24  GLY   A N   1 
ATOM   156  C CA  . GLY   A 1 25  ? 16.530  13.705  15.760  1.00 43.10 ? 24  GLY   A CA  1 
ATOM   157  C C   . GLY   A 1 25  ? 15.135  13.133  15.887  1.00 42.19 ? 24  GLY   A C   1 
ATOM   158  O O   . GLY   A 1 25  ? 14.584  13.073  16.987  1.00 41.82 ? 24  GLY   A O   1 
ATOM   159  N N   . GLY   A 1 26  ? 14.563  12.707  14.772  1.00 41.46 ? 25  GLY   A N   1 
ATOM   160  C CA  . GLY   A 1 26  ? 13.216  12.163  14.774  1.00 41.24 ? 25  GLY   A CA  1 
ATOM   161  C C   . GLY   A 1 26  ? 12.682  11.828  13.398  1.00 41.43 ? 25  GLY   A C   1 
ATOM   162  O O   . GLY   A 1 26  ? 13.396  11.921  12.397  1.00 41.08 ? 25  GLY   A O   1 
ATOM   163  N N   . GLY   A 1 27  ? 11.438  11.370  13.368  1.00 40.78 ? 26  GLY   A N   1 
ATOM   164  C CA  . GLY   A 1 27  ? 10.757  11.020  12.129  1.00 40.44 ? 26  GLY   A CA  1 
ATOM   165  C C   . GLY   A 1 27  ? 9.365   10.492  12.384  1.00 39.75 ? 26  GLY   A C   1 
ATOM   166  O O   . GLY   A 1 27  ? 8.790   10.755  13.445  1.00 39.36 ? 26  GLY   A O   1 
ATOM   167  N N   . THR   A 1 28  ? 8.840   9.666   11.465  1.00 39.89 ? 27  THR   A N   1 
ATOM   168  C CA  . THR   A 1 28  ? 7.503   9.067   11.673  1.00 40.88 ? 27  THR   A CA  1 
ATOM   169  C C   . THR   A 1 28  ? 7.406   8.235   12.968  1.00 41.43 ? 27  THR   A C   1 
ATOM   170  O O   . THR   A 1 28  ? 6.322   8.053   13.500  1.00 41.81 ? 27  THR   A O   1 
ATOM   171  C CB  . THR   A 1 28  ? 7.119   8.195   10.502  1.00 41.01 ? 27  THR   A CB  1 
ATOM   172  O OG1 . THR   A 1 28  ? 8.076   7.127   10.390  1.00 41.52 ? 27  THR   A OG1 1 
ATOM   173  C CG2 . THR   A 1 28  ? 6.927   9.004   9.215   1.00 40.39 ? 27  THR   A CG2 1 
ATOM   174  N N   . TYR   A 1 29  ? 8.542   7.750   13.468  1.00 41.28 ? 28  TYR   A N   1 
ATOM   175  C CA  . TYR   A 1 29  ? 8.640   6.947   14.679  1.00 41.02 ? 28  TYR   A CA  1 
ATOM   176  C C   . TYR   A 1 29  ? 8.657   7.755   15.987  1.00 42.03 ? 28  TYR   A C   1 
ATOM   177  O O   . TYR   A 1 29  ? 8.722   7.147   17.063  1.00 43.00 ? 28  TYR   A O   1 
ATOM   178  C CB  . TYR   A 1 29  ? 9.900   6.084   14.616  1.00 39.40 ? 28  TYR   A CB  1 
ATOM   179  C CG  . TYR   A 1 29  ? 11.182  6.884   14.530  1.00 37.98 ? 28  TYR   A CG  1 
ATOM   180  C CD1 . TYR   A 1 29  ? 11.785  7.394   15.670  1.00 38.25 ? 28  TYR   A CD1 1 
ATOM   181  C CD2 . TYR   A 1 29  ? 11.798  7.124   13.305  1.00 37.69 ? 28  TYR   A CD2 1 
ATOM   182  C CE1 . TYR   A 1 29  ? 12.922  8.184   15.594  1.00 38.72 ? 28  TYR   A CE1 1 
ATOM   183  C CE2 . TYR   A 1 29  ? 12.972  7.866   13.222  1.00 37.80 ? 28  TYR   A CE2 1 
ATOM   184  C CZ  . TYR   A 1 29  ? 13.530  8.395   14.371  1.00 39.29 ? 28  TYR   A CZ  1 
ATOM   185  O OH  . TYR   A 1 29  ? 14.695  9.124   14.318  1.00 40.95 ? 28  TYR   A OH  1 
ATOM   186  N N   . GLY   A 1 30  ? 8.687   9.081   15.908  1.00 42.09 ? 29  GLY   A N   1 
ATOM   187  C CA  . GLY   A 1 30  ? 8.711   9.902   17.111  1.00 42.91 ? 29  GLY   A CA  1 
ATOM   188  C C   . GLY   A 1 30  ? 9.869   10.867  17.190  1.00 44.29 ? 29  GLY   A C   1 
ATOM   189  O O   . GLY   A 1 30  ? 10.618  10.999  16.225  1.00 45.00 ? 29  GLY   A O   1 
ATOM   190  N N   . GLU   A 1 31  ? 10.000  11.581  18.329  1.00 44.76 ? 30  GLU   A N   1 
ATOM   191  C CA  . GLU   A 1 31  ? 11.085  12.542  18.581  1.00 45.91 ? 30  GLU   A CA  1 
ATOM   192  C C   . GLU   A 1 31  ? 12.057  11.991  19.616  1.00 46.55 ? 30  GLU   A C   1 
ATOM   193  O O   . GLU   A 1 31  ? 11.639  11.652  20.717  1.00 47.32 ? 30  GLU   A O   1 
ATOM   194  C CB  . GLU   A 1 31  ? 10.507  13.862  19.104  1.00 47.92 ? 30  GLU   A CB  1 
ATOM   195  C CG  . GLU   A 1 31  ? 9.665   14.563  18.070  1.00 54.54 ? 30  GLU   A CG  1 
ATOM   196  C CD  . GLU   A 1 31  ? 10.502  15.261  17.023  1.00 63.08 ? 30  GLU   A CD  1 
ATOM   197  O OE1 . GLU   A 1 31  ? 11.005  16.365  17.329  1.00 67.16 ? 30  GLU   A OE1 1 
ATOM   198  O OE2 . GLU   A 1 31  ? 10.662  14.711  15.908  1.00 63.36 ? 30  GLU   A OE2 1 
ATOM   199  N N   . VAL   A 1 32  ? 13.342  11.920  19.289  1.00 46.53 ? 31  VAL   A N   1 
ATOM   200  C CA  . VAL   A 1 32  ? 14.337  11.345  20.185  1.00 46.89 ? 31  VAL   A CA  1 
ATOM   201  C C   . VAL   A 1 32  ? 15.206  12.400  20.830  1.00 48.19 ? 31  VAL   A C   1 
ATOM   202  O O   . VAL   A 1 32  ? 15.709  13.282  20.144  1.00 48.03 ? 31  VAL   A O   1 
ATOM   203  C CB  . VAL   A 1 32  ? 15.167  10.252  19.496  1.00 47.12 ? 31  VAL   A CB  1 
ATOM   204  C CG1 . VAL   A 1 32  ? 16.110  9.576   20.485  1.00 47.60 ? 31  VAL   A CG1 1 
ATOM   205  C CG2 . VAL   A 1 32  ? 14.258  9.225   18.828  1.00 47.13 ? 31  VAL   A CG2 1 
ATOM   206  N N   . PHE   A 1 33  ? 15.337  12.334  22.174  1.00 48.82 ? 32  PHE   A N   1 
ATOM   207  C CA  . PHE   A 1 33  ? 16.122  13.266  22.960  1.00 50.22 ? 32  PHE   A CA  1 
ATOM   208  C C   . PHE   A 1 33  ? 17.168  12.524  23.774  1.00 51.41 ? 32  PHE   A C   1 
ATOM   209  O O   . PHE   A 1 33  ? 16.929  11.419  24.256  1.00 50.93 ? 32  PHE   A O   1 
ATOM   210  C CB  . PHE   A 1 33  ? 15.213  14.071  23.918  1.00 50.42 ? 32  PHE   A CB  1 
ATOM   211  C CG  . PHE   A 1 33  ? 14.176  14.913  23.210  1.00 51.52 ? 32  PHE   A CG  1 
ATOM   212  C CD1 . PHE   A 1 33  ? 12.949  14.378  22.850  1.00 52.15 ? 32  PHE   A CD1 1 
ATOM   213  C CD2 . PHE   A 1 33  ? 14.420  16.247  22.923  1.00 52.38 ? 32  PHE   A CD2 1 
ATOM   214  C CE1 . PHE   A 1 33  ? 11.999  15.156  22.194  1.00 52.49 ? 32  PHE   A CE1 1 
ATOM   215  C CE2 . PHE   A 1 33  ? 13.468  17.018  22.257  1.00 52.50 ? 32  PHE   A CE2 1 
ATOM   216  C CZ  . PHE   A 1 33  ? 12.277  16.459  21.879  1.00 51.99 ? 32  PHE   A CZ  1 
ATOM   217  N N   . LYS   A 1 34  ? 18.335  13.138  23.926  1.00 52.55 ? 33  LYS   A N   1 
ATOM   218  C CA  . LYS   A 1 34  ? 19.373  12.611  24.787  1.00 54.42 ? 33  LYS   A CA  1 
ATOM   219  C C   . LYS   A 1 34  ? 18.931  13.012  26.188  1.00 56.74 ? 33  LYS   A C   1 
ATOM   220  O O   . LYS   A 1 34  ? 18.406  14.113  26.361  1.00 56.50 ? 33  LYS   A O   1 
ATOM   221  C CB  . LYS   A 1 34  ? 20.712  13.267  24.453  1.00 56.00 ? 33  LYS   A CB  1 
ATOM   222  C CG  . LYS   A 1 34  ? 21.885  12.664  25.205  1.00 59.67 ? 33  LYS   A CG  1 
ATOM   223  C CD  . LYS   A 1 34  ? 23.168  13.401  24.858  1.00 63.54 ? 33  LYS   A CD  1 
ATOM   224  C CE  . LYS   A 1 34  ? 24.362  12.914  25.628  1.00 66.54 ? 33  LYS   A CE  1 
ATOM   225  N NZ  . LYS   A 1 34  ? 25.606  13.570  25.155  1.00 68.39 ? 33  LYS   A NZ  1 
ATOM   226  N N   . ALA   A 1 35  ? 19.060  12.120  27.176  1.00 58.65 ? 34  ALA   A N   1 
ATOM   227  C CA  . ALA   A 1 35  ? 18.619  12.444  28.542  1.00 60.50 ? 34  ALA   A CA  1 
ATOM   228  C C   . ALA   A 1 35  ? 19.515  11.826  29.594  1.00 62.98 ? 34  ALA   A C   1 
ATOM   229  O O   . ALA   A 1 35  ? 20.171  10.819  29.333  1.00 62.85 ? 34  ALA   A O   1 
ATOM   230  C CB  . ALA   A 1 35  ? 17.177  12.001  28.751  1.00 60.46 ? 34  ALA   A CB  1 
ATOM   231  N N   . ARG   A 1 36  ? 19.538  12.418  30.793  1.00 65.04 ? 35  ARG   A N   1 
ATOM   232  C CA  . ARG   A 1 36  ? 20.352  11.907  31.875  1.00 67.73 ? 35  ARG   A CA  1 
ATOM   233  C C   . ARG   A 1 36  ? 19.472  11.548  33.063  1.00 70.00 ? 35  ARG   A C   1 
ATOM   234  O O   . ARG   A 1 36  ? 18.657  12.364  33.493  1.00 70.14 ? 35  ARG   A O   1 
ATOM   235  C CB  . ARG   A 1 36  ? 21.390  12.964  32.287  1.00 70.12 ? 35  ARG   A CB  1 
ATOM   236  C CG  . ARG   A 1 36  ? 22.491  12.403  33.180  1.00 75.47 ? 35  ARG   A CG  1 
ATOM   237  C CD  . ARG   A 1 36  ? 23.522  13.447  33.568  1.00 80.75 ? 35  ARG   A CD  1 
ATOM   238  N NE  . ARG   A 1 36  ? 24.251  13.964  32.406  1.00 85.14 ? 35  ARG   A NE  1 
ATOM   239  C CZ  . ARG   A 1 36  ? 24.498  15.255  32.192  1.00 87.84 ? 35  ARG   A CZ  1 
ATOM   240  N NH1 . ARG   A 1 36  ? 24.072  16.174  33.054  1.00 86.76 ? 35  ARG   A NH1 1 
ATOM   241  N NH2 . ARG   A 1 36  ? 25.168  15.638  31.113  1.00 88.27 ? 35  ARG   A NH2 1 
ATOM   242  N N   . ASP   A 1 37  ? 19.652  10.347  33.626  1.00 71.42 ? 36  ASP   A N   1 
ATOM   243  C CA  . ASP   A 1 37  ? 18.902  9.938   34.817  1.00 73.43 ? 36  ASP   A CA  1 
ATOM   244  C C   . ASP   A 1 37  ? 19.377  10.812  35.983  1.00 75.49 ? 36  ASP   A C   1 
ATOM   245  O O   . ASP   A 1 37  ? 20.581  10.951  36.184  1.00 75.71 ? 36  ASP   A O   1 
ATOM   246  C CB  . ASP   A 1 37  ? 19.148  8.443   35.106  1.00 75.00 ? 36  ASP   A CB  1 
ATOM   247  C CG  . ASP   A 1 37  ? 18.284  7.818   36.190  1.00 78.75 ? 36  ASP   A CG  1 
ATOM   248  O OD1 . ASP   A 1 37  ? 18.271  8.349   37.319  1.00 78.90 ? 36  ASP   A OD1 1 
ATOM   249  O OD2 . ASP   A 1 37  ? 17.658  6.771   35.921  1.00 80.80 ? 36  ASP   A OD2 1 
ATOM   250  N N   . LYS   A 1 38  ? 18.438  11.450  36.700  1.00 76.92 ? 37  LYS   A N   1 
ATOM   251  C CA  . LYS   A 1 38  ? 18.736  12.341  37.823  1.00 78.63 ? 37  LYS   A CA  1 
ATOM   252  C C   . LYS   A 1 38  ? 19.363  11.637  39.028  1.00 80.18 ? 37  LYS   A C   1 
ATOM   253  O O   . LYS   A 1 38  ? 19.899  12.313  39.916  1.00 80.81 ? 37  LYS   A O   1 
ATOM   254  C CB  . LYS   A 1 38  ? 17.447  13.013  38.321  1.00 81.09 ? 37  LYS   A CB  1 
ATOM   255  C CG  . LYS   A 1 38  ? 16.702  13.859  37.308  1.00 85.55 ? 37  LYS   A CG  1 
ATOM   256  C CD  . LYS   A 1 38  ? 15.490  14.466  38.001  1.00 89.67 ? 37  LYS   A CD  1 
ATOM   257  C CE  . LYS   A 1 38  ? 14.867  15.608  37.247  1.00 93.32 ? 37  LYS   A CE  1 
ATOM   258  N NZ  . LYS   A 1 38  ? 13.788  16.246  38.051  1.00 96.08 ? 37  LYS   A NZ  1 
ATOM   259  N N   . VAL   A 1 39  ? 19.215  10.310  39.126  1.00 80.65 ? 38  VAL   A N   1 
ATOM   260  C CA  . VAL   A 1 39  ? 19.722  9.583   40.283  1.00 81.87 ? 38  VAL   A CA  1 
ATOM   261  C C   . VAL   A 1 39  ? 21.056  8.900   39.980  1.00 81.79 ? 38  VAL   A C   1 
ATOM   262  O O   . VAL   A 1 39  ? 22.036  9.128   40.693  1.00 82.24 ? 38  VAL   A O   1 
ATOM   263  C CB  . VAL   A 1 39  ? 18.639  8.617   40.847  1.00 83.39 ? 38  VAL   A CB  1 
ATOM   264  C CG1 . VAL   A 1 39  ? 19.244  7.514   41.716  1.00 84.61 ? 38  VAL   A CG1 1 
ATOM   265  C CG2 . VAL   A 1 39  ? 17.586  9.401   41.630  1.00 83.69 ? 38  VAL   A CG2 1 
ATOM   266  N N   . SER   A 1 40  ? 21.097  8.081   38.933  1.00 80.98 ? 39  SER   A N   1 
ATOM   267  C CA  . SER   A 1 40  ? 22.307  7.346   38.589  1.00 80.66 ? 39  SER   A CA  1 
ATOM   268  C C   . SER   A 1 40  ? 23.320  8.144   37.762  1.00 80.03 ? 39  SER   A C   1 
ATOM   269  O O   . SER   A 1 40  ? 24.500  7.800   37.745  1.00 80.23 ? 39  SER   A O   1 
ATOM   270  C CB  . SER   A 1 40  ? 21.940  6.063   37.861  1.00 81.80 ? 39  SER   A CB  1 
ATOM   271  O OG  . SER   A 1 40  ? 21.359  6.385   36.608  1.00 84.64 ? 39  SER   A OG  1 
ATOM   272  N N   . GLY   A 1 41  ? 22.858  9.178   37.066  1.00 78.97 ? 40  GLY   A N   1 
ATOM   273  C CA  . GLY   A 1 41  ? 23.720  9.982   36.204  1.00 77.89 ? 40  GLY   A CA  1 
ATOM   274  C C   . GLY   A 1 41  ? 23.962  9.375   34.830  1.00 76.12 ? 40  GLY   A C   1 
ATOM   275  O O   . GLY   A 1 41  ? 24.630  9.988   33.995  1.00 76.46 ? 40  GLY   A O   1 
ATOM   276  N N   . ASP   A 1 42  ? 23.418  8.173   34.576  1.00 74.13 ? 41  ASP   A N   1 
ATOM   277  C CA  . ASP   A 1 42  ? 23.588  7.466   33.312  1.00 72.76 ? 41  ASP   A CA  1 
ATOM   278  C C   . ASP   A 1 42  ? 22.861  8.161   32.161  1.00 70.48 ? 41  ASP   A C   1 
ATOM   279  O O   . ASP   A 1 42  ? 21.819  8.784   32.369  1.00 70.57 ? 41  ASP   A O   1 
ATOM   280  C CB  . ASP   A 1 42  ? 23.084  6.015   33.433  1.00 74.80 ? 41  ASP   A CB  1 
ATOM   281  C CG  . ASP   A 1 42  ? 23.725  5.189   34.531  1.00 79.60 ? 41  ASP   A CG  1 
ATOM   282  O OD1 . ASP   A 1 42  ? 24.603  5.723   35.242  1.00 80.90 ? 41  ASP   A OD1 1 
ATOM   283  O OD2 . ASP   A 1 42  ? 23.336  4.007   34.689  1.00 81.44 ? 41  ASP   A OD2 1 
ATOM   284  N N   . LEU   A 1 43  ? 23.403  8.034   30.942  1.00 68.09 ? 42  LEU   A N   1 
ATOM   285  C CA  . LEU   A 1 43  ? 22.789  8.616   29.756  1.00 66.13 ? 42  LEU   A CA  1 
ATOM   286  C C   . LEU   A 1 43  ? 21.853  7.610   29.107  1.00 63.47 ? 42  LEU   A C   1 
ATOM   287  O O   . LEU   A 1 43  ? 22.175  6.427   29.023  1.00 63.69 ? 42  LEU   A O   1 
ATOM   288  C CB  . LEU   A 1 43  ? 23.848  9.063   28.742  1.00 66.57 ? 42  LEU   A CB  1 
ATOM   289  C CG  . LEU   A 1 43  ? 24.707  10.257  29.143  1.00 68.62 ? 42  LEU   A CG  1 
ATOM   290  C CD1 . LEU   A 1 43  ? 25.781  10.518  28.098  1.00 69.51 ? 42  LEU   A CD1 1 
ATOM   291  C CD2 . LEU   A 1 43  ? 23.861  11.500  29.374  1.00 68.96 ? 42  LEU   A CD2 1 
ATOM   292  N N   . VAL   A 1 44  ? 20.676  8.081   28.677  1.00 60.79 ? 43  VAL   A N   1 
ATOM   293  C CA  . VAL   A 1 44  ? 19.639  7.283   28.018  1.00 58.70 ? 43  VAL   A CA  1 
ATOM   294  C C   . VAL   A 1 44  ? 19.074  8.067   26.809  1.00 56.24 ? 43  VAL   A C   1 
ATOM   295  O O   . VAL   A 1 44  ? 19.319  9.270   26.669  1.00 55.43 ? 43  VAL   A O   1 
ATOM   296  C CB  . VAL   A 1 44  ? 18.482  6.941   29.013  1.00 59.62 ? 43  VAL   A CB  1 
ATOM   297  C CG1 . VAL   A 1 44  ? 18.991  6.281   30.292  1.00 60.11 ? 43  VAL   A CG1 1 
ATOM   298  C CG2 . VAL   A 1 44  ? 17.656  8.190   29.343  1.00 60.43 ? 43  VAL   A CG2 1 
ATOM   299  N N   . ALA   A 1 45  ? 18.291  7.393   25.951  1.00 54.74 ? 44  ALA   A N   1 
ATOM   300  C CA  . ALA   A 1 45  ? 17.570  8.073   24.887  1.00 54.14 ? 44  ALA   A CA  1 
ATOM   301  C C   . ALA   A 1 45  ? 16.074  8.074   25.272  1.00 53.80 ? 44  ALA   A C   1 
ATOM   302  O O   . ALA   A 1 45  ? 15.575  7.083   25.807  1.00 54.31 ? 44  ALA   A O   1 
ATOM   303  C CB  . ALA   A 1 45  ? 17.782  7.374   23.554  1.00 53.87 ? 44  ALA   A CB  1 
ATOM   304  N N   . LEU   A 1 46  ? 15.378  9.190   25.058  1.00 52.90 ? 45  LEU   A N   1 
ATOM   305  C CA  . LEU   A 1 46  ? 13.954  9.269   25.346  1.00 53.02 ? 45  LEU   A CA  1 
ATOM   306  C C   . LEU   A 1 46  ? 13.219  9.564   24.061  1.00 53.32 ? 45  LEU   A C   1 
ATOM   307  O O   . LEU   A 1 46  ? 13.418  10.626  23.476  1.00 54.12 ? 45  LEU   A O   1 
ATOM   308  C CB  . LEU   A 1 46  ? 13.646  10.361  26.382  1.00 53.39 ? 45  LEU   A CB  1 
ATOM   309  C CG  . LEU   A 1 46  ? 14.000  10.064  27.858  1.00 54.78 ? 45  LEU   A CG  1 
ATOM   310  C CD1 . LEU   A 1 46  ? 13.456  11.151  28.784  1.00 54.27 ? 45  LEU   A CD1 1 
ATOM   311  C CD2 . LEU   A 1 46  ? 13.434  8.730   28.317  1.00 55.61 ? 45  LEU   A CD2 1 
ATOM   312  N N   . LYS   A 1 47  ? 12.369  8.636   23.614  1.00 52.25 ? 46  LYS   A N   1 
ATOM   313  C CA  . LYS   A 1 47  ? 11.592  8.806   22.398  1.00 51.65 ? 46  LYS   A CA  1 
ATOM   314  C C   . LYS   A 1 47  ? 10.136  9.161   22.725  1.00 52.22 ? 46  LYS   A C   1 
ATOM   315  O O   . LYS   A 1 47  ? 9.456   8.396   23.384  1.00 51.40 ? 46  LYS   A O   1 
ATOM   316  C CB  . LYS   A 1 47  ? 11.666  7.523   21.556  1.00 51.32 ? 46  LYS   A CB  1 
ATOM   317  C CG  . LYS   A 1 47  ? 10.823  7.524   20.284  1.00 51.82 ? 46  LYS   A CG  1 
ATOM   318  C CD  . LYS   A 1 47  ? 11.158  6.317   19.393  1.00 54.05 ? 46  LYS   A CD  1 
ATOM   319  C CE  . LYS   A 1 47  ? 10.979  4.970   20.080  1.00 56.38 ? 46  LYS   A CE  1 
ATOM   320  N NZ  . LYS   A 1 47  ? 11.802  3.886   19.455  1.00 57.30 ? 46  LYS   A NZ  1 
ATOM   321  N N   . MET   A 1 48  ? 9.667   10.320  22.258  1.00 53.16 ? 47  MET   A N   1 
ATOM   322  C CA  . MET   A 1 48  ? 8.297   10.780  22.438  1.00 54.41 ? 47  MET   A CA  1 
ATOM   323  C C   . MET   A 1 48  ? 7.457   10.412  21.203  1.00 55.71 ? 47  MET   A C   1 
ATOM   324  O O   . MET   A 1 48  ? 7.717   10.874  20.096  1.00 55.20 ? 47  MET   A O   1 
ATOM   325  C CB  . MET   A 1 48  ? 8.286   12.301  22.629  1.00 55.51 ? 47  MET   A CB  1 
ATOM   326  C CG  . MET   A 1 48  ? 6.887   12.906  22.634  1.00 60.72 ? 47  MET   A CG  1 
ATOM   327  S SD  . MET   A 1 48  ? 6.951   14.706  22.438  1.00 74.66 ? 47  MET   A SD  1 
ATOM   328  C CE  . MET   A 1 48  ? 6.875   14.817  20.644  1.00 71.35 ? 47  MET   A CE  1 
ATOM   329  N N   . VAL   A 1 49  ? 6.419   9.622   21.416  1.00 57.34 ? 48  VAL   A N   1 
ATOM   330  C CA  . VAL   A 1 49  ? 5.495   9.202   20.377  1.00 59.20 ? 48  VAL   A CA  1 
ATOM   331  C C   . VAL   A 1 49  ? 4.145   9.839   20.714  1.00 62.40 ? 48  VAL   A C   1 
ATOM   332  O O   . VAL   A 1 49  ? 3.601   9.554   21.779  1.00 63.38 ? 48  VAL   A O   1 
ATOM   333  C CB  . VAL   A 1 49  ? 5.366   7.662   20.340  1.00 59.05 ? 48  VAL   A CB  1 
ATOM   334  C CG1 . VAL   A 1 49  ? 4.531   7.223   19.151  1.00 59.67 ? 48  VAL   A CG1 1 
ATOM   335  C CG2 . VAL   A 1 49  ? 6.731   6.978   20.324  1.00 58.97 ? 48  VAL   A CG2 1 
ATOM   336  N N   . LYS   A 1 50  ? 3.609   10.711  19.849  1.00 64.18 ? 49  LYS   A N   1 
ATOM   337  C CA  . LYS   A 1 50  ? 2.305   11.335  20.102  1.00 66.62 ? 49  LYS   A CA  1 
ATOM   338  C C   . LYS   A 1 50  ? 1.163   10.342  19.879  1.00 68.52 ? 49  LYS   A C   1 
ATOM   339  O O   . LYS   A 1 50  ? 1.108   9.678   18.848  1.00 68.34 ? 49  LYS   A O   1 
ATOM   340  C CB  . LYS   A 1 50  ? 2.112   12.593  19.250  1.00 69.12 ? 49  LYS   A CB  1 
ATOM   341  C CG  . LYS   A 1 50  ? 2.852   13.810  19.801  1.00 74.02 ? 49  LYS   A CG  1 
ATOM   342  C CD  . LYS   A 1 50  ? 3.691   14.504  18.739  1.00 78.96 ? 49  LYS   A CD  1 
ATOM   343  C CE  . LYS   A 1 50  ? 2.853   15.078  17.628  1.00 82.92 ? 49  LYS   A CE  1 
ATOM   344  N NZ  . LYS   A 1 50  ? 1.862   16.057  18.143  1.00 84.90 ? 49  LYS   A NZ  1 
ATOM   345  N N   . MET   A 1 51  ? 0.271   10.220  20.860  1.00 70.20 ? 50  MET   A N   1 
ATOM   346  C CA  . MET   A 1 51  ? -0.848  9.285   20.795  1.00 72.15 ? 50  MET   A CA  1 
ATOM   347  C C   . MET   A 1 51  ? -1.972  9.771   19.888  1.00 73.23 ? 50  MET   A C   1 
ATOM   348  O O   . MET   A 1 51  ? -2.365  10.933  19.953  1.00 72.95 ? 50  MET   A O   1 
ATOM   349  C CB  . MET   A 1 51  ? -1.384  8.993   22.210  1.00 73.65 ? 50  MET   A CB  1 
ATOM   350  C CG  . MET   A 1 51  ? -0.334  8.426   23.145  1.00 76.48 ? 50  MET   A CG  1 
ATOM   351  S SD  . MET   A 1 51  ? -0.257  6.629   23.074  1.00 82.32 ? 50  MET   A SD  1 
ATOM   352  C CE  . MET   A 1 51  ? 1.025   6.377   21.793  1.00 81.16 ? 50  MET   A CE  1 
ATOM   353  N N   . GLU   A 1 52  ? -2.494  8.866   19.059  1.00 74.46 ? 51  GLU   A N   1 
ATOM   354  C CA  . GLU   A 1 52  ? -3.582  9.127   18.116  1.00 76.51 ? 51  GLU   A CA  1 
ATOM   355  C C   . GLU   A 1 52  ? -4.958  9.049   18.800  1.00 78.05 ? 51  GLU   A C   1 
ATOM   356  O O   . GLU   A 1 52  ? -5.102  8.413   19.844  1.00 78.17 ? 51  GLU   A O   1 
ATOM   357  C CB  . GLU   A 1 52  ? -3.502  8.138   16.932  1.00 79.49 ? 51  GLU   A CB  1 
ATOM   358  C CG  . GLU   A 1 52  ? -2.233  8.272   16.110  1.00 85.45 ? 51  GLU   A CG  1 
ATOM   359  C CD  . GLU   A 1 52  ? -2.016  9.618   15.450  1.00 92.42 ? 51  GLU   A CD  1 
ATOM   360  O OE1 . GLU   A 1 52  ? -2.727  9.915   14.464  1.00 94.71 ? 51  GLU   A OE1 1 
ATOM   361  O OE2 . GLU   A 1 52  ? -1.128  10.371  15.909  1.00 94.19 ? 51  GLU   A OE2 1 
ATOM   362  N N   . PRO   A 1 53  ? -5.996  9.669   18.211  1.00 79.12 ? 52  PRO   A N   1 
ATOM   363  C CA  . PRO   A 1 53  ? -7.323  9.638   18.835  1.00 79.77 ? 52  PRO   A CA  1 
ATOM   364  C C   . PRO   A 1 53  ? -7.921  8.254   19.081  1.00 81.04 ? 52  PRO   A C   1 
ATOM   365  O O   . PRO   A 1 53  ? -8.843  8.123   19.882  1.00 82.09 ? 52  PRO   A O   1 
ATOM   366  C CB  . PRO   A 1 53  ? -8.179  10.447  17.861  1.00 80.42 ? 52  PRO   A CB  1 
ATOM   367  C CG  . PRO   A 1 53  ? -7.219  11.311  17.129  1.00 80.51 ? 52  PRO   A CG  1 
ATOM   368  C CD  . PRO   A 1 53  ? -5.999  10.481  16.980  1.00 78.93 ? 52  PRO   A CD  1 
ATOM   369  N N   . ASP   A 1 54  ? -7.434  7.237   18.389  1.00 81.38 ? 53  ASP   A N   1 
ATOM   370  C CA  . ASP   A 1 54  ? -7.934  5.873   18.541  1.00 82.32 ? 53  ASP   A CA  1 
ATOM   371  C C   . ASP   A 1 54  ? -6.913  4.923   19.197  1.00 82.32 ? 53  ASP   A C   1 
ATOM   372  O O   . ASP   A 1 54  ? -7.048  3.708   19.065  1.00 82.69 ? 53  ASP   A O   1 
ATOM   373  C CB  . ASP   A 1 54  ? -8.358  5.305   17.178  1.00 84.83 ? 53  ASP   A CB  1 
ATOM   374  C CG  . ASP   A 1 54  ? -9.644  5.870   16.611  1.00 90.79 ? 53  ASP   A CG  1 
ATOM   375  O OD1 . ASP   A 1 54  ? -10.321 6.639   17.319  1.00 92.31 ? 53  ASP   A OD1 1 
ATOM   376  O OD2 . ASP   A 1 54  ? -9.985  5.524   15.469  1.00 93.34 ? 53  ASP   A OD2 1 
ATOM   377  N N   . ASP   A 1 55  ? -5.912  5.461   19.907  1.00 81.65 ? 54  ASP   A N   1 
ATOM   378  C CA  . ASP   A 1 55  ? -4.911  4.641   20.580  1.00 81.30 ? 54  ASP   A CA  1 
ATOM   379  C C   . ASP   A 1 55  ? -5.345  4.246   22.003  1.00 81.28 ? 54  ASP   A C   1 
ATOM   380  O O   . ASP   A 1 55  ? -4.853  4.819   22.979  1.00 81.62 ? 54  ASP   A O   1 
ATOM   381  C CB  . ASP   A 1 55  ? -3.573  5.383   20.629  1.00 82.58 ? 54  ASP   A CB  1 
ATOM   382  C CG  . ASP   A 1 55  ? -2.741  5.253   19.379  1.00 86.76 ? 54  ASP   A CG  1 
ATOM   383  O OD1 . ASP   A 1 55  ? -2.984  4.304   18.599  1.00 87.51 ? 54  ASP   A OD1 1 
ATOM   384  O OD2 . ASP   A 1 55  ? -1.845  6.096   19.180  1.00 88.64 ? 54  ASP   A OD2 1 
ATOM   385  N N   . ASP   A 1 56  ? -6.259  3.265   22.126  1.00 80.37 ? 55  ASP   A N   1 
ATOM   386  C CA  . ASP   A 1 56  ? -6.727  2.793   23.433  1.00 79.72 ? 55  ASP   A CA  1 
ATOM   387  C C   . ASP   A 1 56  ? -5.558  2.231   24.269  1.00 78.55 ? 55  ASP   A C   1 
ATOM   388  O O   . ASP   A 1 56  ? -4.600  1.676   23.705  1.00 78.36 ? 55  ASP   A O   1 
ATOM   389  C CB  . ASP   A 1 56  ? -7.832  1.741   23.261  1.00 81.46 ? 55  ASP   A CB  1 
ATOM   390  C CG  . ASP   A 1 56  ? -7.366  0.520   22.509  1.00 86.86 ? 55  ASP   A CG  1 
ATOM   391  O OD1 . ASP   A 1 56  ? -6.961  0.665   21.337  1.00 88.52 ? 55  ASP   A OD1 1 
ATOM   392  O OD2 . ASP   A 1 56  ? -7.383  -0.578  23.096  1.00 88.95 ? 55  ASP   A OD2 1 
ATOM   393  N N   . VAL   A 1 57  ? -5.617  2.402   25.604  1.00 77.27 ? 56  VAL   A N   1 
ATOM   394  C CA  . VAL   A 1 57  ? -4.532  1.969   26.493  1.00 77.22 ? 56  VAL   A CA  1 
ATOM   395  C C   . VAL   A 1 57  ? -4.436  0.422   26.589  1.00 77.07 ? 56  VAL   A C   1 
ATOM   396  O O   . VAL   A 1 57  ? -3.386  -0.087  26.968  1.00 77.16 ? 56  VAL   A O   1 
ATOM   397  C CB  . VAL   A 1 57  ? -4.497  2.658   27.901  1.00 78.36 ? 56  VAL   A CB  1 
ATOM   398  C CG1 . VAL   A 1 57  ? -5.152  4.044   27.891  1.00 79.11 ? 56  VAL   A CG1 1 
ATOM   399  C CG2 . VAL   A 1 57  ? -5.095  1.784   29.000  1.00 78.91 ? 56  VAL   A CG2 1 
ATOM   400  N N   . SER   A 1 58  ? -5.481  -0.313  26.202  1.00 77.08 ? 57  SER   A N   1 
ATOM   401  C CA  . SER   A 1 58  ? -5.450  -1.772  26.231  1.00 77.61 ? 57  SER   A CA  1 
ATOM   402  C C   . SER   A 1 58  ? -4.539  -2.304  25.140  1.00 78.02 ? 57  SER   A C   1 
ATOM   403  O O   . SER   A 1 58  ? -3.791  -3.248  25.381  1.00 79.02 ? 57  SER   A O   1 
ATOM   404  C CB  . SER   A 1 58  ? -6.856  -2.345  26.083  1.00 79.14 ? 57  SER   A CB  1 
ATOM   405  O OG  . SER   A 1 58  ? -7.687  -1.928  27.153  1.00 82.22 ? 57  SER   A OG  1 
ATOM   406  N N   . THR   A 1 59  ? -4.572  -1.690  23.945  1.00 76.95 ? 58  THR   A N   1 
ATOM   407  C CA  . THR   A 1 59  ? -3.698  -2.083  22.839  1.00 76.07 ? 58  THR   A CA  1 
ATOM   408  C C   . THR   A 1 59  ? -2.262  -1.593  23.113  1.00 75.22 ? 58  THR   A C   1 
ATOM   409  O O   . THR   A 1 59  ? -1.292  -2.312  22.850  1.00 75.22 ? 58  THR   A O   1 
ATOM   410  C CB  . THR   A 1 59  ? -4.254  -1.554  21.510  1.00 77.20 ? 58  THR   A CB  1 
ATOM   411  O OG1 . THR   A 1 59  ? -5.543  -2.132  21.288  1.00 78.26 ? 58  THR   A OG1 1 
ATOM   412  C CG2 . THR   A 1 59  ? -3.332  -1.854  20.320  1.00 77.55 ? 58  THR   A CG2 1 
ATOM   413  N N   . LEU   A 1 60  ? -2.143  -0.378  23.685  1.00 73.89 ? 59  LEU   A N   1 
ATOM   414  C CA  . LEU   A 1 60  ? -0.897  0.259   24.096  1.00 72.75 ? 59  LEU   A CA  1 
ATOM   415  C C   . LEU   A 1 60  ? -0.168  -0.660  25.087  1.00 71.90 ? 59  LEU   A C   1 
ATOM   416  O O   . LEU   A 1 60  ? 1.035   -0.853  24.952  1.00 71.91 ? 59  LEU   A O   1 
ATOM   417  C CB  . LEU   A 1 60  ? -1.244  1.600   24.766  1.00 72.55 ? 59  LEU   A CB  1 
ATOM   418  C CG  . LEU   A 1 60  ? -0.094  2.511   25.152  1.00 73.24 ? 59  LEU   A CG  1 
ATOM   419  C CD1 . LEU   A 1 60  ? 0.697   2.913   23.938  1.00 73.11 ? 59  LEU   A CD1 1 
ATOM   420  C CD2 . LEU   A 1 60  ? -0.613  3.766   25.859  1.00 73.47 ? 59  LEU   A CD2 1 
ATOM   421  N N   . GLN   A 1 61  ? -0.913  -1.278  26.035  1.00 70.99 ? 60  GLN   A N   1 
ATOM   422  C CA  . GLN   A 1 61  ? -0.361  -2.218  27.011  1.00 70.80 ? 60  GLN   A CA  1 
ATOM   423  C C   . GLN   A 1 61  ? 0.213   -3.476  26.325  1.00 70.20 ? 60  GLN   A C   1 
ATOM   424  O O   . GLN   A 1 61  ? 1.307   -3.920  26.679  1.00 70.07 ? 60  GLN   A O   1 
ATOM   425  C CB  . GLN   A 1 61  ? -1.406  -2.555  28.102  1.00 72.77 ? 60  GLN   A CB  1 
ATOM   426  C CG  . GLN   A 1 61  ? -1.250  -3.903  28.818  1.00 77.60 ? 60  GLN   A CG  1 
ATOM   427  C CD  . GLN   A 1 61  ? -0.082  -3.976  29.775  1.00 84.00 ? 60  GLN   A CD  1 
ATOM   428  O OE1 . GLN   A 1 61  ? 0.936   -3.290  29.627  1.00 86.42 ? 60  GLN   A OE1 1 
ATOM   429  N NE2 . GLN   A 1 61  ? -0.196  -4.838  30.778  1.00 85.42 ? 60  GLN   A NE2 1 
ATOM   430  N N   . LYS   A 1 62  ? -0.502  -4.026  25.326  1.00 69.55 ? 61  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -0.029  -5.188  24.570  1.00 69.09 ? 61  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? 1.274   -4.860  23.865  1.00 68.06 ? 61  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? 2.176   -5.694  23.843  1.00 68.34 ? 61  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -1.059  -5.633  23.517  1.00 71.63 ? 61  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -2.385  -6.099  24.087  1.00 77.30 ? 61  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -3.314  -6.581  22.976  1.00 82.38 ? 61  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -4.774  -6.416  23.340  1.00 85.49 ? 61  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -5.217  -4.996  23.236  1.00 87.40 ? 61  LYS   A NZ  1 
ATOM   439  N N   . GLU   A 1 63  ? 1.378   -3.644  23.291  1.00 66.52 ? 62  GLU   A N   1 
ATOM   440  C CA  . GLU   A 1 63  ? 2.575   -3.208  22.573  1.00 65.12 ? 62  GLU   A CA  1 
ATOM   441  C C   . GLU   A 1 63  ? 3.755   -3.063  23.507  1.00 63.84 ? 62  GLU   A C   1 
ATOM   442  O O   . GLU   A 1 63  ? 4.842   -3.522  23.170  1.00 63.86 ? 62  GLU   A O   1 
ATOM   443  C CB  . GLU   A 1 63  ? 2.340   -1.877  21.831  1.00 66.67 ? 62  GLU   A CB  1 
ATOM   444  C CG  . GLU   A 1 63  ? 1.181   -1.886  20.851  1.00 70.40 ? 62  GLU   A CG  1 
ATOM   445  C CD  . GLU   A 1 63  ? 1.182   -3.020  19.847  1.00 74.79 ? 62  GLU   A CD  1 
ATOM   446  O OE1 . GLU   A 1 63  ? 0.116   -3.654  19.672  1.00 75.65 ? 62  GLU   A OE1 1 
ATOM   447  O OE2 . GLU   A 1 63  ? 2.244   -3.267  19.230  1.00 75.05 ? 62  GLU   A OE2 1 
ATOM   448  N N   . ILE   A 1 64  ? 3.551   -2.465  24.694  1.00 62.64 ? 63  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 64  ? 4.652   -2.289  25.643  1.00 61.97 ? 63  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 64  ? 5.163   -3.660  26.123  1.00 61.88 ? 63  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 64  ? 6.370   -3.834  26.275  1.00 62.02 ? 63  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 64  ? 4.302   -1.276  26.776  1.00 61.76 ? 63  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 64  ? 4.831   0.112   26.420  1.00 62.24 ? 63  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 64  ? 4.831   -1.679  28.151  1.00 62.13 ? 63  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 64  ? 4.012   0.838   25.498  1.00 63.48 ? 63  ILE   A CD1 1 
ATOM   456  N N   . LEU   A 1 65  ? 4.271   -4.648  26.258  1.00 61.66 ? 64  LEU   A N   1 
ATOM   457  C CA  . LEU   A 1 65  ? 4.644   -6.013  26.629  1.00 62.18 ? 64  LEU   A CA  1 
ATOM   458  C C   . LEU   A 1 65  ? 5.549   -6.615  25.527  1.00 61.85 ? 64  LEU   A C   1 
ATOM   459  O O   . LEU   A 1 65  ? 6.545   -7.269  25.837  1.00 61.74 ? 64  LEU   A O   1 
ATOM   460  C CB  . LEU   A 1 65  ? 3.370   -6.854  26.782  1.00 62.83 ? 64  LEU   A CB  1 
ATOM   461  C CG  . LEU   A 1 65  ? 3.430   -8.020  27.739  1.00 65.47 ? 64  LEU   A CG  1 
ATOM   462  C CD1 . LEU   A 1 65  ? 3.284   -7.545  29.186  1.00 65.77 ? 64  LEU   A CD1 1 
ATOM   463  C CD2 . LEU   A 1 65  ? 2.312   -9.010  27.437  1.00 66.86 ? 64  LEU   A CD2 1 
ATOM   464  N N   . ILE   A 1 66  ? 5.219   -6.355  24.249  1.00 61.50 ? 65  ILE   A N   1 
ATOM   465  C CA  . ILE   A 1 66  ? 5.991   -6.825  23.107  1.00 62.03 ? 65  ILE   A CA  1 
ATOM   466  C C   . ILE   A 1 66  ? 7.360   -6.132  23.073  1.00 62.81 ? 65  ILE   A C   1 
ATOM   467  O O   . ILE   A 1 66  ? 8.358   -6.775  22.775  1.00 63.31 ? 65  ILE   A O   1 
ATOM   468  C CB  . ILE   A 1 66  ? 5.203   -6.618  21.792  1.00 62.62 ? 65  ILE   A CB  1 
ATOM   469  C CG1 . ILE   A 1 66  ? 3.894   -7.420  21.785  1.00 63.52 ? 65  ILE   A CG1 1 
ATOM   470  C CG2 . ILE   A 1 66  ? 6.047   -6.977  20.574  1.00 62.97 ? 65  ILE   A CG2 1 
ATOM   471  C CD1 . ILE   A 1 66  ? 2.943   -7.005  20.662  1.00 64.58 ? 65  ILE   A CD1 1 
ATOM   472  N N   . LEU   A 1 67  ? 7.413   -4.831  23.410  1.00 62.51 ? 66  LEU   A N   1 
ATOM   473  C CA  . LEU   A 1 67  ? 8.663   -4.057  23.481  1.00 62.63 ? 66  LEU   A CA  1 
ATOM   474  C C   . LEU   A 1 67  ? 9.607   -4.574  24.579  1.00 62.87 ? 66  LEU   A C   1 
ATOM   475  O O   . LEU   A 1 67  ? 10.821  -4.426  24.478  1.00 63.30 ? 66  LEU   A O   1 
ATOM   476  C CB  . LEU   A 1 67  ? 8.340   -2.595  23.803  1.00 62.61 ? 66  LEU   A CB  1 
ATOM   477  C CG  . LEU   A 1 67  ? 8.354   -1.605  22.666  1.00 63.86 ? 66  LEU   A CG  1 
ATOM   478  C CD1 . LEU   A 1 67  ? 7.958   -0.225  23.172  1.00 64.20 ? 66  LEU   A CD1 1 
ATOM   479  C CD2 . LEU   A 1 67  ? 9.721   -1.551  22.012  1.00 64.35 ? 66  LEU   A CD2 1 
ATOM   480  N N   . LYS   A 1 68  ? 9.051   -5.117  25.646  1.00 62.74 ? 67  LYS   A N   1 
ATOM   481  C CA  . LYS   A 1 68  ? 9.822   -5.599  26.776  1.00 63.62 ? 67  LYS   A CA  1 
ATOM   482  C C   . LYS   A 1 68  ? 10.293  -7.042  26.583  1.00 64.02 ? 67  LYS   A C   1 
ATOM   483  O O   . LYS   A 1 68  ? 11.312  -7.429  27.158  1.00 64.78 ? 67  LYS   A O   1 
ATOM   484  C CB  . LYS   A 1 68  ? 8.979   -5.468  28.064  1.00 65.78 ? 67  LYS   A CB  1 
ATOM   485  C CG  . LYS   A 1 68  ? 9.793   -5.404  29.349  1.00 70.60 ? 67  LYS   A CG  1 
ATOM   486  C CD  . LYS   A 1 68  ? 8.989   -4.784  30.497  1.00 76.30 ? 67  LYS   A CD  1 
ATOM   487  C CE  . LYS   A 1 68  ? 9.837   -4.570  31.731  1.00 80.83 ? 67  LYS   A CE  1 
ATOM   488  N NZ  . LYS   A 1 68  ? 9.613   -3.227  32.336  1.00 83.17 ? 67  LYS   A NZ  1 
ATOM   489  N N   . THR   A 1 69  ? 9.551   -7.847  25.812  1.00 63.38 ? 68  THR   A N   1 
ATOM   490  C CA  . THR   A 1 69  ? 9.914   -9.249  25.618  1.00 63.13 ? 68  THR   A CA  1 
ATOM   491  C C   . THR   A 1 69  ? 10.694  -9.465  24.310  1.00 61.85 ? 68  THR   A C   1 
ATOM   492  O O   . THR   A 1 69  ? 11.500  -10.389 24.243  1.00 62.53 ? 68  THR   A O   1 
ATOM   493  C CB  . THR   A 1 69  ? 8.685   -10.161 25.763  1.00 64.48 ? 68  THR   A CB  1 
ATOM   494  O OG1 . THR   A 1 69  ? 7.684   -9.759  24.828  1.00 65.72 ? 68  THR   A OG1 1 
ATOM   495  C CG2 . THR   A 1 69  ? 8.109   -10.125 27.167  1.00 64.92 ? 68  THR   A CG2 1 
ATOM   496  N N   . CYS   A 1 70  ? 10.487  -8.624  23.296  1.00 60.08 ? 69  CYS   A N   1 
ATOM   497  C CA  . CYS   A 1 70  ? 11.234  -8.751  22.035  1.00 58.99 ? 69  CYS   A CA  1 
ATOM   498  C C   . CYS   A 1 70  ? 12.617  -8.139  22.247  1.00 56.80 ? 69  CYS   A C   1 
ATOM   499  O O   . CYS   A 1 70  ? 12.817  -6.980  21.918  1.00 57.46 ? 69  CYS   A O   1 
ATOM   500  C CB  . CYS   A 1 70  ? 10.490  -8.066  20.892  1.00 60.27 ? 69  CYS   A CB  1 
ATOM   501  S SG  . CYS   A 1 70  ? 11.090  -8.502  19.236  1.00 63.22 ? 69  CYS   A SG  1 
ATOM   502  N N   . ARG   A 1 71  ? 13.550  -8.903  22.836  1.00 54.42 ? 70  ARG   A N   1 
ATOM   503  C CA  . ARG   A 1 71  ? 14.888  -8.438  23.189  1.00 52.74 ? 70  ARG   A CA  1 
ATOM   504  C C   . ARG   A 1 71  ? 16.035  -9.199  22.515  1.00 48.58 ? 70  ARG   A C   1 
ATOM   505  O O   . ARG   A 1 71  ? 16.058  -10.437 22.515  1.00 48.86 ? 70  ARG   A O   1 
ATOM   506  C CB  . ARG   A 1 71  ? 15.094  -8.549  24.707  1.00 55.80 ? 70  ARG   A CB  1 
ATOM   507  C CG  . ARG   A 1 71  ? 14.349  -7.510  25.512  1.00 62.76 ? 70  ARG   A CG  1 
ATOM   508  C CD  . ARG   A 1 71  ? 14.934  -7.389  26.911  1.00 68.40 ? 70  ARG   A CD  1 
ATOM   509  N NE  . ARG   A 1 71  ? 14.170  -8.132  27.915  1.00 74.47 ? 70  ARG   A NE  1 
ATOM   510  C CZ  . ARG   A 1 71  ? 14.520  -9.319  28.404  1.00 78.15 ? 70  ARG   A CZ  1 
ATOM   511  N NH1 . ARG   A 1 71  ? 13.774  -9.908  29.331  1.00 77.44 ? 70  ARG   A NH1 1 
ATOM   512  N NH2 . ARG   A 1 71  ? 15.622  -9.923  27.975  1.00 79.19 ? 70  ARG   A NH2 1 
ATOM   513  N N   . HIS   A 1 72  ? 17.053  -8.465  22.083  1.00 44.48 ? 71  HIS   A N   1 
ATOM   514  C CA  . HIS   A 1 72  ? 18.225  -9.085  21.470  1.00 41.21 ? 71  HIS   A CA  1 
ATOM   515  C C   . HIS   A 1 72  ? 19.432  -8.147  21.558  1.00 39.75 ? 71  HIS   A C   1 
ATOM   516  O O   . HIS   A 1 72  ? 19.262  -6.926  21.434  1.00 39.84 ? 71  HIS   A O   1 
ATOM   517  C CB  . HIS   A 1 72  ? 17.921  -9.419  20.006  1.00 39.44 ? 71  HIS   A CB  1 
ATOM   518  C CG  . HIS   A 1 72  ? 18.979  -10.245 19.357  1.00 38.97 ? 71  HIS   A CG  1 
ATOM   519  N ND1 . HIS   A 1 72  ? 20.017  -9.665  18.656  1.00 40.02 ? 71  HIS   A ND1 1 
ATOM   520  C CD2 . HIS   A 1 72  ? 19.133  -11.587 19.330  1.00 39.54 ? 71  HIS   A CD2 1 
ATOM   521  C CE1 . HIS   A 1 72  ? 20.763  -10.664 18.230  1.00 40.15 ? 71  HIS   A CE1 1 
ATOM   522  N NE2 . HIS   A 1 72  ? 20.269  -11.840 18.604  1.00 39.78 ? 71  HIS   A NE2 1 
ATOM   523  N N   . ALA   A 1 73  ? 20.655  -8.699  21.701  1.00 37.77 ? 72  ALA   A N   1 
ATOM   524  C CA  . ALA   A 1 73  ? 21.855  -7.850  21.756  1.00 37.20 ? 72  ALA   A CA  1 
ATOM   525  C C   . ALA   A 1 73  ? 21.994  -6.881  20.572  1.00 36.55 ? 72  ALA   A C   1 
ATOM   526  O O   . ALA   A 1 73  ? 22.598  -5.834  20.742  1.00 37.50 ? 72  ALA   A O   1 
ATOM   527  C CB  . ALA   A 1 73  ? 23.120  -8.691  21.888  1.00 36.86 ? 72  ALA   A CB  1 
ATOM   528  N N   . ASN   A 1 74  ? 21.488  -7.238  19.380  1.00 34.61 ? 73  ASN   A N   1 
ATOM   529  C CA  . ASN   A 1 74  ? 21.578  -6.373  18.202  1.00 33.91 ? 73  ASN   A CA  1 
ATOM   530  C C   . ASN   A 1 74  ? 20.351  -5.483  17.986  1.00 34.32 ? 73  ASN   A C   1 
ATOM   531  O O   . ASN   A 1 74  ? 20.112  -5.048  16.858  1.00 34.51 ? 73  ASN   A O   1 
ATOM   532  C CB  . ASN   A 1 74  ? 21.902  -7.169  16.927  1.00 33.59 ? 73  ASN   A CB  1 
ATOM   533  C CG  . ASN   A 1 74  ? 23.256  -7.825  16.998  1.00 34.82 ? 73  ASN   A CG  1 
ATOM   534  O OD1 . ASN   A 1 74  ? 23.383  -9.048  17.034  1.00 35.72 ? 73  ASN   A OD1 1 
ATOM   535  N ND2 . ASN   A 1 74  ? 24.303  -7.030  17.069  1.00 34.65 ? 73  ASN   A ND2 1 
ATOM   536  N N   . ILE   A 1 75  ? 19.560  -5.244  19.036  1.00 34.25 ? 74  ILE   A N   1 
ATOM   537  C CA  . ILE   A 1 75  ? 18.410  -4.332  19.026  1.00 34.77 ? 74  ILE   A CA  1 
ATOM   538  C C   . ILE   A 1 75  ? 18.573  -3.440  20.262  1.00 36.42 ? 74  ILE   A C   1 
ATOM   539  O O   . ILE   A 1 75  ? 18.834  -3.959  21.349  1.00 35.85 ? 74  ILE   A O   1 
ATOM   540  C CB  . ILE   A 1 75  ? 17.051  -5.061  19.100  1.00 34.76 ? 74  ILE   A CB  1 
ATOM   541  C CG1 . ILE   A 1 75  ? 16.837  -6.008  17.909  1.00 34.45 ? 74  ILE   A CG1 1 
ATOM   542  C CG2 . ILE   A 1 75  ? 15.885  -4.039  19.204  1.00 35.27 ? 74  ILE   A CG2 1 
ATOM   543  C CD1 . ILE   A 1 75  ? 15.646  -6.895  18.097  1.00 34.70 ? 74  ILE   A CD1 1 
ATOM   544  N N   . VAL   A 1 76  ? 18.417  -2.103  20.114  1.00 37.48 ? 75  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 76  ? 18.516  -1.158  21.227  1.00 39.82 ? 75  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 76  ? 17.575  -1.578  22.384  1.00 41.50 ? 75  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 76  ? 16.416  -1.926  22.145  1.00 41.50 ? 75  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 76  ? 18.252  0.289   20.726  1.00 41.05 ? 75  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 76  ? 18.153  1.273   21.887  1.00 42.17 ? 75  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 76  ? 19.335  0.720   19.750  1.00 41.46 ? 75  VAL   A CG2 1 
ATOM   551  N N   . ALA   A 1 77  ? 18.126  -1.707  23.591  1.00 42.96 ? 76  ALA   A N   1 
ATOM   552  C CA  . ALA   A 1 77  ? 17.360  -2.187  24.738  1.00 45.23 ? 76  ALA   A CA  1 
ATOM   553  C C   . ALA   A 1 77  ? 16.283  -1.217  25.164  1.00 46.84 ? 76  ALA   A C   1 
ATOM   554  O O   . ALA   A 1 77  ? 16.502  -0.012  25.165  1.00 47.06 ? 76  ALA   A O   1 
ATOM   555  C CB  . ALA   A 1 77  ? 18.295  -2.461  25.913  1.00 45.50 ? 76  ALA   A CB  1 
ATOM   556  N N   . TYR   A 1 78  ? 15.115  -1.741  25.511  1.00 47.66 ? 77  TYR   A N   1 
ATOM   557  C CA  . TYR   A 1 78  ? 14.014  -0.942  26.010  1.00 48.98 ? 77  TYR   A CA  1 
ATOM   558  C C   . TYR   A 1 78  ? 14.149  -0.941  27.538  1.00 50.50 ? 77  TYR   A C   1 
ATOM   559  O O   . TYR   A 1 78  ? 14.335  -2.004  28.134  1.00 50.64 ? 77  TYR   A O   1 
ATOM   560  C CB  . TYR   A 1 78  ? 12.683  -1.574  25.563  1.00 49.11 ? 77  TYR   A CB  1 
ATOM   561  C CG  . TYR   A 1 78  ? 11.462  -1.114  26.331  1.00 50.29 ? 77  TYR   A CG  1 
ATOM   562  C CD1 . TYR   A 1 78  ? 10.779  0.038   25.965  1.00 51.20 ? 77  TYR   A CD1 1 
ATOM   563  C CD2 . TYR   A 1 78  ? 10.971  -1.850  27.401  1.00 51.17 ? 77  TYR   A CD2 1 
ATOM   564  C CE1 . TYR   A 1 78  ? 9.652   0.457   26.662  1.00 51.99 ? 77  TYR   A CE1 1 
ATOM   565  C CE2 . TYR   A 1 78  ? 9.842   -1.444  28.099  1.00 52.15 ? 77  TYR   A CE2 1 
ATOM   566  C CZ  . TYR   A 1 78  ? 9.169   -0.304  27.708  1.00 53.11 ? 77  TYR   A CZ  1 
ATOM   567  O OH  . TYR   A 1 78  ? 8.070   0.101   28.424  1.00 55.11 ? 77  TYR   A OH  1 
ATOM   568  N N   . HIS   A 1 79  ? 14.053  0.236   28.176  1.00 51.76 ? 78  HIS   A N   1 
ATOM   569  C CA  . HIS   A 1 79  ? 14.171  0.342   29.634  1.00 53.70 ? 78  HIS   A CA  1 
ATOM   570  C C   . HIS   A 1 79  ? 12.824  0.516   30.320  1.00 55.14 ? 78  HIS   A C   1 
ATOM   571  O O   . HIS   A 1 79  ? 12.652  0.064   31.449  1.00 56.11 ? 78  HIS   A O   1 
ATOM   572  C CB  . HIS   A 1 79  ? 15.071  1.522   30.036  1.00 55.27 ? 78  HIS   A CB  1 
ATOM   573  C CG  . HIS   A 1 79  ? 16.484  1.413   29.566  1.00 59.13 ? 78  HIS   A CG  1 
ATOM   574  N ND1 . HIS   A 1 79  ? 17.145  0.196   29.532  1.00 61.58 ? 78  HIS   A ND1 1 
ATOM   575  C CD2 . HIS   A 1 79  ? 17.334  2.385   29.156  1.00 60.62 ? 78  HIS   A CD2 1 
ATOM   576  C CE1 . HIS   A 1 79  ? 18.361  0.459   29.084  1.00 62.19 ? 78  HIS   A CE1 1 
ATOM   577  N NE2 . HIS   A 1 79  ? 18.527  1.765   28.856  1.00 61.97 ? 78  HIS   A NE2 1 
ATOM   578  N N   . GLY   A 1 80  ? 11.920  1.253   29.693  1.00 55.05 ? 79  GLY   A N   1 
ATOM   579  C CA  . GLY   A 1 80  ? 10.622  1.537   30.287  1.00 55.82 ? 79  GLY   A CA  1 
ATOM   580  C C   . GLY   A 1 80  ? 9.846   2.604   29.547  1.00 56.96 ? 79  GLY   A C   1 
ATOM   581  O O   . GLY   A 1 80  ? 10.323  3.126   28.541  1.00 56.87 ? 79  GLY   A O   1 
ATOM   582  N N   . SER   A 1 81  ? 8.628   2.906   30.005  1.00 58.00 ? 80  SER   A N   1 
ATOM   583  C CA  . SER   A 1 81  ? 7.804   3.898   29.329  1.00 59.74 ? 80  SER   A CA  1 
ATOM   584  C C   . SER   A 1 81  ? 6.941   4.740   30.273  1.00 61.29 ? 80  SER   A C   1 
ATOM   585  O O   . SER   A 1 81  ? 6.734   4.396   31.437  1.00 60.93 ? 80  SER   A O   1 
ATOM   586  C CB  . SER   A 1 81  ? 6.965   3.254   28.226  1.00 61.08 ? 80  SER   A CB  1 
ATOM   587  O OG  . SER   A 1 81  ? 5.875   2.540   28.787  1.00 63.71 ? 80  SER   A OG  1 
ATOM   588  N N   . TYR   A 1 82  ? 6.511   5.901   29.776  1.00 62.96 ? 81  TYR   A N   1 
ATOM   589  C CA  . TYR   A 1 82  ? 5.699   6.844   30.523  1.00 65.30 ? 81  TYR   A CA  1 
ATOM   590  C C   . TYR   A 1 82  ? 4.557   7.320   29.638  1.00 67.33 ? 81  TYR   A C   1 
ATOM   591  O O   . TYR   A 1 82  ? 4.790   7.642   28.476  1.00 67.58 ? 81  TYR   A O   1 
ATOM   592  C CB  . TYR   A 1 82  ? 6.534   8.075   30.938  1.00 65.65 ? 81  TYR   A CB  1 
ATOM   593  C CG  . TYR   A 1 82  ? 7.755   7.756   31.771  1.00 66.82 ? 81  TYR   A CG  1 
ATOM   594  C CD1 . TYR   A 1 82  ? 8.893   7.212   31.192  1.00 67.81 ? 81  TYR   A CD1 1 
ATOM   595  C CD2 . TYR   A 1 82  ? 7.798   8.064   33.123  1.00 68.23 ? 81  TYR   A CD2 1 
ATOM   596  C CE1 . TYR   A 1 82  ? 10.002  6.884   31.954  1.00 68.81 ? 81  TYR   A CE1 1 
ATOM   597  C CE2 . TYR   A 1 82  ? 8.917   7.774   33.890  1.00 69.27 ? 81  TYR   A CE2 1 
ATOM   598  C CZ  . TYR   A 1 82  ? 10.018  7.182   33.299  1.00 70.00 ? 81  TYR   A CZ  1 
ATOM   599  O OH  . TYR   A 1 82  ? 11.127  6.875   34.040  1.00 72.07 ? 81  TYR   A OH  1 
ATOM   600  N N   . LEU   A 1 83  ? 3.332   7.380   30.170  1.00 68.46 ? 82  LEU   A N   1 
ATOM   601  C CA  . LEU   A 1 83  ? 2.211   7.937   29.422  1.00 70.14 ? 82  LEU   A CA  1 
ATOM   602  C C   . LEU   A 1 83  ? 1.881   9.250   30.103  1.00 71.85 ? 82  LEU   A C   1 
ATOM   603  O O   . LEU   A 1 83  ? 1.561   9.262   31.291  1.00 71.93 ? 82  LEU   A O   1 
ATOM   604  C CB  . LEU   A 1 83  ? 0.994   7.015   29.399  1.00 70.72 ? 82  LEU   A CB  1 
ATOM   605  C CG  . LEU   A 1 83  ? -0.237  7.618   28.723  1.00 72.71 ? 82  LEU   A CG  1 
ATOM   606  C CD1 . LEU   A 1 83  ? 0.027   7.921   27.244  1.00 73.30 ? 82  LEU   A CD1 1 
ATOM   607  C CD2 . LEU   A 1 83  ? -1.425  6.720   28.872  1.00 73.76 ? 82  LEU   A CD2 1 
ATOM   608  N N   . TRP   A 1 84  ? 2.010   10.363  29.376  1.00 73.00 ? 83  TRP   A N   1 
ATOM   609  C CA  . TRP   A 1 84  ? 1.787   11.676  29.960  1.00 74.37 ? 83  TRP   A CA  1 
ATOM   610  C C   . TRP   A 1 84  ? 1.308   12.678  28.928  1.00 74.93 ? 83  TRP   A C   1 
ATOM   611  O O   . TRP   A 1 84  ? 1.946   12.822  27.889  1.00 75.12 ? 83  TRP   A O   1 
ATOM   612  C CB  . TRP   A 1 84  ? 3.107   12.161  30.573  1.00 75.18 ? 83  TRP   A CB  1 
ATOM   613  C CG  . TRP   A 1 84  ? 3.042   13.498  31.242  1.00 76.71 ? 83  TRP   A CG  1 
ATOM   614  C CD1 . TRP   A 1 84  ? 3.584   14.666  30.797  1.00 77.89 ? 83  TRP   A CD1 1 
ATOM   615  C CD2 . TRP   A 1 84  ? 2.455   13.786  32.515  1.00 77.80 ? 83  TRP   A CD2 1 
ATOM   616  N NE1 . TRP   A 1 84  ? 3.339   15.675  31.701  1.00 78.84 ? 83  TRP   A NE1 1 
ATOM   617  C CE2 . TRP   A 1 84  ? 2.657   15.157  32.771  1.00 78.82 ? 83  TRP   A CE2 1 
ATOM   618  C CE3 . TRP   A 1 84  ? 1.753   13.023  33.453  1.00 78.68 ? 83  TRP   A CE3 1 
ATOM   619  C CZ2 . TRP   A 1 84  ? 2.194   15.771  33.922  1.00 80.31 ? 83  TRP   A CZ2 1 
ATOM   620  C CZ3 . TRP   A 1 84  ? 1.329   13.623  34.609  1.00 80.07 ? 83  TRP   A CZ3 1 
ATOM   621  C CH2 . TRP   A 1 84  ? 1.520   14.989  34.828  1.00 80.70 ? 83  TRP   A CH2 1 
ATOM   622  N N   . LEU   A 1 85  ? 0.191   13.377  29.218  1.00 75.29 ? 84  LEU   A N   1 
ATOM   623  C CA  . LEU   A 1 85  ? -0.409  14.426  28.380  1.00 75.96 ? 84  LEU   A CA  1 
ATOM   624  C C   . LEU   A 1 85  ? -0.544  14.055  26.892  1.00 75.17 ? 84  LEU   A C   1 
ATOM   625  O O   . LEU   A 1 85  ? -0.150  14.834  26.021  1.00 75.55 ? 84  LEU   A O   1 
ATOM   626  C CB  . LEU   A 1 85  ? 0.357   15.751  28.548  1.00 76.97 ? 84  LEU   A CB  1 
ATOM   627  C CG  . LEU   A 1 85  ? 0.447   16.286  29.968  1.00 79.68 ? 84  LEU   A CG  1 
ATOM   628  C CD1 . LEU   A 1 85  ? 1.317   17.526  30.021  1.00 80.94 ? 84  LEU   A CD1 1 
ATOM   629  C CD2 . LEU   A 1 85  ? -0.937  16.585  30.542  1.00 80.56 ? 84  LEU   A CD2 1 
ATOM   630  N N   . GLN   A 1 86  ? -1.083  12.855  26.613  1.00 73.96 ? 85  GLN   A N   1 
ATOM   631  C CA  . GLN   A 1 86  ? -1.273  12.315  25.260  1.00 73.20 ? 85  GLN   A CA  1 
ATOM   632  C C   . GLN   A 1 86  ? 0.031   11.953  24.530  1.00 71.57 ? 85  GLN   A C   1 
ATOM   633  O O   . GLN   A 1 86  ? 0.012   11.676  23.330  1.00 71.74 ? 85  GLN   A O   1 
ATOM   634  C CB  . GLN   A 1 86  ? -2.137  13.246  24.388  1.00 75.64 ? 85  GLN   A CB  1 
ATOM   635  C CG  . GLN   A 1 86  ? -3.542  13.475  24.924  1.00 80.76 ? 85  GLN   A CG  1 
ATOM   636  C CD  . GLN   A 1 86  ? -4.321  12.186  25.048  1.00 86.81 ? 85  GLN   A CD  1 
ATOM   637  O OE1 . GLN   A 1 86  ? -4.950  11.910  26.090  1.00 88.98 ? 85  GLN   A OE1 1 
ATOM   638  N NE2 . GLN   A 1 86  ? -4.288  11.366  23.992  1.00 87.02 ? 85  GLN   A NE2 1 
ATOM   639  N N   . LYS   A 1 87  ? 1.161   11.957  25.238  1.00 69.53 ? 86  LYS   A N   1 
ATOM   640  C CA  . LYS   A 1 87  ? 2.443   11.616  24.648  1.00 67.52 ? 86  LYS   A CA  1 
ATOM   641  C C   . LYS   A 1 87  ? 3.033   10.411  25.378  1.00 65.26 ? 86  LYS   A C   1 
ATOM   642  O O   . LYS   A 1 87  ? 3.054   10.380  26.610  1.00 65.84 ? 86  LYS   A O   1 
ATOM   643  C CB  . LYS   A 1 87  ? 3.388   12.829  24.651  1.00 69.15 ? 86  LYS   A CB  1 
ATOM   644  C CG  . LYS   A 1 87  ? 2.840   13.969  23.803  1.00 73.50 ? 86  LYS   A CG  1 
ATOM   645  C CD  . LYS   A 1 87  ? 3.745   15.185  23.712  1.00 78.40 ? 86  LYS   A CD  1 
ATOM   646  C CE  . LYS   A 1 87  ? 4.033   15.834  25.042  1.00 83.34 ? 86  LYS   A CE  1 
ATOM   647  N NZ  . LYS   A 1 87  ? 4.607   17.202  24.885  1.00 85.76 ? 86  LYS   A NZ  1 
ATOM   648  N N   . LEU   A 1 88  ? 3.444   9.390   24.615  1.00 62.41 ? 87  LEU   A N   1 
ATOM   649  C CA  . LEU   A 1 88  ? 4.038   8.185   25.162  1.00 60.16 ? 87  LEU   A CA  1 
ATOM   650  C C   . LEU   A 1 88  ? 5.547   8.331   25.032  1.00 59.09 ? 87  LEU   A C   1 
ATOM   651  O O   . LEU   A 1 88  ? 6.056   8.632   23.956  1.00 58.89 ? 87  LEU   A O   1 
ATOM   652  C CB  . LEU   A 1 88  ? 3.531   6.953   24.413  1.00 59.46 ? 87  LEU   A CB  1 
ATOM   653  C CG  . LEU   A 1 88  ? 4.250   5.649   24.716  1.00 60.00 ? 87  LEU   A CG  1 
ATOM   654  C CD1 . LEU   A 1 88  ? 3.941   5.171   26.105  1.00 60.23 ? 87  LEU   A CD1 1 
ATOM   655  C CD2 . LEU   A 1 88  ? 3.950   4.601   23.668  1.00 59.96 ? 87  LEU   A CD2 1 
ATOM   656  N N   . TRP   A 1 89  ? 6.256   8.148   26.131  1.00 57.85 ? 88  TRP   A N   1 
ATOM   657  C CA  . TRP   A 1 89  ? 7.689   8.312   26.162  1.00 57.10 ? 88  TRP   A CA  1 
ATOM   658  C C   . TRP   A 1 89  ? 8.331   6.981   26.404  1.00 55.50 ? 88  TRP   A C   1 
ATOM   659  O O   . TRP   A 1 89  ? 8.028   6.346   27.395  1.00 55.70 ? 88  TRP   A O   1 
ATOM   660  C CB  . TRP   A 1 89  ? 8.067   9.287   27.281  1.00 57.73 ? 88  TRP   A CB  1 
ATOM   661  C CG  . TRP   A 1 89  ? 7.676   10.714  27.029  1.00 58.89 ? 88  TRP   A CG  1 
ATOM   662  C CD1 . TRP   A 1 89  ? 6.483   11.306  27.319  1.00 60.32 ? 88  TRP   A CD1 1 
ATOM   663  C CD2 . TRP   A 1 89  ? 8.530   11.752  26.533  1.00 59.33 ? 88  TRP   A CD2 1 
ATOM   664  N NE1 . TRP   A 1 89  ? 6.545   12.657  27.051  1.00 60.68 ? 88  TRP   A NE1 1 
ATOM   665  C CE2 . TRP   A 1 89  ? 7.790   12.951  26.549  1.00 60.39 ? 88  TRP   A CE2 1 
ATOM   666  C CE3 . TRP   A 1 89  ? 9.848   11.779  26.061  1.00 59.71 ? 88  TRP   A CE3 1 
ATOM   667  C CZ2 . TRP   A 1 89  ? 8.325   14.161  26.113  1.00 60.81 ? 88  TRP   A CZ2 1 
ATOM   668  C CZ3 . TRP   A 1 89  ? 10.376  12.980  25.637  1.00 60.48 ? 88  TRP   A CZ3 1 
ATOM   669  C CH2 . TRP   A 1 89  ? 9.618   14.152  25.661  1.00 60.65 ? 88  TRP   A CH2 1 
ATOM   670  N N   . ILE   A 1 90  ? 9.200   6.545   25.497  1.00 53.38 ? 89  ILE   A N   1 
ATOM   671  C CA  . ILE   A 1 90  ? 9.927   5.295   25.621  1.00 52.40 ? 89  ILE   A CA  1 
ATOM   672  C C   . ILE   A 1 90  ? 11.392  5.577   25.971  1.00 51.54 ? 89  ILE   A C   1 
ATOM   673  O O   . ILE   A 1 90  ? 12.082  6.308   25.268  1.00 51.69 ? 89  ILE   A O   1 
ATOM   674  C CB  . ILE   A 1 90  ? 9.785   4.458   24.332  1.00 52.65 ? 89  ILE   A CB  1 
ATOM   675  C CG1 . ILE   A 1 90  ? 8.354   3.928   24.200  1.00 53.35 ? 89  ILE   A CG1 1 
ATOM   676  C CG2 . ILE   A 1 90  ? 10.819  3.314   24.265  1.00 52.72 ? 89  ILE   A CG2 1 
ATOM   677  C CD1 . ILE   A 1 90  ? 8.034   3.507   22.836  1.00 54.76 ? 89  ILE   A CD1 1 
ATOM   678  N N   . CYS   A 1 91  ? 11.854  4.994   27.057  1.00 50.33 ? 90  CYS   A N   1 
ATOM   679  C CA  . CYS   A 1 91  ? 13.225  5.123   27.495  1.00 49.98 ? 90  CYS   A CA  1 
ATOM   680  C C   . CYS   A 1 91  ? 13.991  3.948   26.931  1.00 48.50 ? 90  CYS   A C   1 
ATOM   681  O O   . CYS   A 1 91  ? 13.546  2.801   27.047  1.00 48.12 ? 90  CYS   A O   1 
ATOM   682  C CB  . CYS   A 1 91  ? 13.299  5.162   29.020  1.00 51.87 ? 90  CYS   A CB  1 
ATOM   683  S SG  . CYS   A 1 91  ? 14.962  5.451   29.670  1.00 56.03 ? 90  CYS   A SG  1 
ATOM   684  N N   . MET   A 1 92  ? 15.133  4.227   26.292  1.00 47.16 ? 91  MET   A N   1 
ATOM   685  C CA  . MET   A 1 92  ? 15.936  3.183   25.697  1.00 46.42 ? 91  MET   A CA  1 
ATOM   686  C C   . MET   A 1 92  ? 17.445  3.453   25.835  1.00 46.29 ? 91  MET   A C   1 
ATOM   687  O O   . MET   A 1 92  ? 17.841  4.572   26.148  1.00 46.23 ? 91  MET   A O   1 
ATOM   688  C CB  . MET   A 1 92  ? 15.514  3.007   24.226  1.00 46.46 ? 91  MET   A CB  1 
ATOM   689  C CG  . MET   A 1 92  ? 15.776  4.216   23.392  1.00 48.05 ? 91  MET   A CG  1 
ATOM   690  S SD  . MET   A 1 92  ? 14.848  4.303   21.829  1.00 51.17 ? 91  MET   A SD  1 
ATOM   691  C CE  . MET   A 1 92  ? 14.885  6.052   21.608  1.00 57.97 ? 91  MET   A CE  1 
ATOM   692  N N   . GLU   A 1 93  ? 18.292  2.433   25.595  1.00 45.93 ? 92  GLU   A N   1 
ATOM   693  C CA  . GLU   A 1 93  ? 19.750  2.592   25.662  1.00 46.20 ? 92  GLU   A CA  1 
ATOM   694  C C   . GLU   A 1 93  ? 20.243  3.680   24.701  1.00 45.43 ? 92  GLU   A C   1 
ATOM   695  O O   . GLU   A 1 93  ? 19.770  3.790   23.563  1.00 45.91 ? 92  GLU   A O   1 
ATOM   696  C CB  . GLU   A 1 93  ? 20.463  1.265   25.338  1.00 50.36 ? 92  GLU   A CB  1 
ATOM   697  C CG  . GLU   A 1 93  ? 21.982  1.330   25.451  1.00 58.73 ? 92  GLU   A CG  1 
ATOM   698  C CD  . GLU   A 1 93  ? 22.759  0.606   24.360  1.00 70.01 ? 92  GLU   A CD  1 
ATOM   699  O OE1 . GLU   A 1 93  ? 23.985  0.849   24.250  1.00 71.41 ? 92  GLU   A OE1 1 
ATOM   700  O OE2 . GLU   A 1 93  ? 22.149  -0.203  23.618  1.00 73.23 ? 92  GLU   A OE2 1 
ATOM   701  N N   . PHE   A 1 94  ? 21.195  4.478   25.154  1.00 44.39 ? 93  PHE   A N   1 
ATOM   702  C CA  . PHE   A 1 94  ? 21.760  5.553   24.360  1.00 44.55 ? 93  PHE   A CA  1 
ATOM   703  C C   . PHE   A 1 94  ? 22.895  5.022   23.490  1.00 44.11 ? 93  PHE   A C   1 
ATOM   704  O O   . PHE   A 1 94  ? 23.792  4.353   23.986  1.00 45.18 ? 93  PHE   A O   1 
ATOM   705  C CB  . PHE   A 1 94  ? 22.270  6.667   25.286  1.00 44.88 ? 93  PHE   A CB  1 
ATOM   706  C CG  . PHE   A 1 94  ? 22.944  7.820   24.588  1.00 46.17 ? 93  PHE   A CG  1 
ATOM   707  C CD1 . PHE   A 1 94  ? 22.250  8.604   23.682  1.00 47.31 ? 93  PHE   A CD1 1 
ATOM   708  C CD2 . PHE   A 1 94  ? 24.239  8.185   24.912  1.00 47.16 ? 93  PHE   A CD2 1 
ATOM   709  C CE1 . PHE   A 1 94  ? 22.861  9.685   23.060  1.00 48.06 ? 93  PHE   A CE1 1 
ATOM   710  C CE2 . PHE   A 1 94  ? 24.844  9.276   24.296  1.00 48.11 ? 93  PHE   A CE2 1 
ATOM   711  C CZ  . PHE   A 1 94  ? 24.152  10.017  23.374  1.00 47.88 ? 93  PHE   A CZ  1 
ATOM   712  N N   . CYS   A 1 95  ? 22.827  5.279   22.193  1.00 42.59 ? 94  CYS   A N   1 
ATOM   713  C CA  . CYS   A 1 95  ? 23.842  4.857   21.246  1.00 42.01 ? 94  CYS   A CA  1 
ATOM   714  C C   . CYS   A 1 95  ? 24.552  6.118   20.807  1.00 41.91 ? 94  CYS   A C   1 
ATOM   715  O O   . CYS   A 1 95  ? 24.091  6.775   19.879  1.00 41.59 ? 94  CYS   A O   1 
ATOM   716  C CB  . CYS   A 1 95  ? 23.201  4.132   20.069  1.00 41.50 ? 94  CYS   A CB  1 
ATOM   717  S SG  . CYS   A 1 95  ? 22.542  2.499   20.491  1.00 42.75 ? 94  CYS   A SG  1 
ATOM   718  N N   . GLY   A 1 96  ? 25.635  6.452   21.523  1.00 42.03 ? 95  GLY   A N   1 
ATOM   719  C CA  . GLY   A 1 96  ? 26.405  7.689   21.406  1.00 42.43 ? 95  GLY   A CA  1 
ATOM   720  C C   . GLY   A 1 96  ? 26.856  8.154   20.037  1.00 42.96 ? 95  GLY   A C   1 
ATOM   721  O O   . GLY   A 1 96  ? 26.905  9.364   19.800  1.00 43.42 ? 95  GLY   A O   1 
ATOM   722  N N   . ALA   A 1 97  ? 27.193  7.217   19.119  1.00 42.15 ? 96  ALA   A N   1 
ATOM   723  C CA  . ALA   A 1 97  ? 27.669  7.630   17.800  1.00 41.65 ? 96  ALA   A CA  1 
ATOM   724  C C   . ALA   A 1 97  ? 26.567  7.870   16.771  1.00 40.79 ? 96  ALA   A C   1 
ATOM   725  O O   . ALA   A 1 97  ? 26.869  8.288   15.650  1.00 41.09 ? 96  ALA   A O   1 
ATOM   726  C CB  . ALA   A 1 97  ? 28.704  6.641   17.270  1.00 41.68 ? 96  ALA   A CB  1 
ATOM   727  N N   . GLY   A 1 98  ? 25.304  7.661   17.161  1.00 39.19 ? 97  GLY   A N   1 
ATOM   728  C CA  . GLY   A 1 98  ? 24.164  7.865   16.287  1.00 36.96 ? 97  GLY   A CA  1 
ATOM   729  C C   . GLY   A 1 98  ? 24.038  6.753   15.277  1.00 35.57 ? 97  GLY   A C   1 
ATOM   730  O O   . GLY   A 1 98  ? 24.498  5.621   15.511  1.00 36.02 ? 97  GLY   A O   1 
ATOM   731  N N   . SER   A 1 99  ? 23.436  7.065   14.139  1.00 33.24 ? 98  SER   A N   1 
ATOM   732  C CA  . SER   A 1 99  ? 23.238  6.064   13.098  1.00 32.19 ? 98  SER   A CA  1 
ATOM   733  C C   . SER   A 1 99  ? 24.446  5.916   12.171  1.00 31.80 ? 98  SER   A C   1 
ATOM   734  O O   . SER   A 1 99  ? 25.321  6.794   12.117  1.00 32.52 ? 98  SER   A O   1 
ATOM   735  C CB  . SER   A 1 99  ? 21.991  6.402   12.288  1.00 31.58 ? 98  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 99  ? 22.205  7.465   11.379  1.00 32.46 ? 98  SER   A OG  1 
ATOM   737  N N   . LEU   A 1 100 ? 24.442  4.854   11.359  1.00 31.40 ? 99  LEU   A N   1 
ATOM   738  C CA  . LEU   A 1 100 ? 25.453  4.676   10.337  1.00 31.42 ? 99  LEU   A CA  1 
ATOM   739  C C   . LEU   A 1 100 ? 25.386  5.800   9.313   1.00 31.30 ? 99  LEU   A C   1 
ATOM   740  O O   . LEU   A 1 100 ? 26.414  6.152   8.788   1.00 32.59 ? 99  LEU   A O   1 
ATOM   741  C CB  . LEU   A 1 100 ? 25.308  3.311   9.665   1.00 31.50 ? 99  LEU   A CB  1 
ATOM   742  C CG  . LEU   A 1 100 ? 25.833  2.156   10.537  1.00 33.37 ? 99  LEU   A CG  1 
ATOM   743  C CD1 . LEU   A 1 100 ? 25.467  0.828   9.915   1.00 33.94 ? 99  LEU   A CD1 1 
ATOM   744  C CD2 . LEU   A 1 100 ? 27.357  2.249   10.706  1.00 35.04 ? 99  LEU   A CD2 1 
ATOM   745  N N   . GLN   A 1 101 ? 24.199  6.390   9.043   1.00 31.08 ? 100 GLN   A N   1 
ATOM   746  C CA  . GLN   A 1 101 ? 24.109  7.553   8.146   1.00 30.28 ? 100 GLN   A CA  1 
ATOM   747  C C   . GLN   A 1 101 ? 24.808  8.767   8.794   1.00 31.23 ? 100 GLN   A C   1 
ATOM   748  O O   . GLN   A 1 101 ? 25.581  9.449   8.141   1.00 32.37 ? 100 GLN   A O   1 
ATOM   749  C CB  . GLN   A 1 101 ? 22.668  7.943   7.799   1.00 29.33 ? 100 GLN   A CB  1 
ATOM   750  C CG  . GLN   A 1 101 ? 22.654  9.095   6.768   1.00 30.77 ? 100 GLN   A CG  1 
ATOM   751  C CD  . GLN   A 1 101 ? 21.262  9.536   6.342   1.00 32.14 ? 100 GLN   A CD  1 
ATOM   752  O OE1 . GLN   A 1 101 ? 20.945  10.737  6.267   1.00 34.44 ? 100 GLN   A OE1 1 
ATOM   753  N NE2 . GLN   A 1 101 ? 20.438  8.592   6.052   1.00 29.49 ? 100 GLN   A NE2 1 
ATOM   754  N N   . ASP   A 1 102 ? 24.561  9.025   10.096  1.00 31.90 ? 101 ASP   A N   1 
ATOM   755  C CA  . ASP   A 1 102 ? 25.237  10.117  10.808  1.00 32.54 ? 101 ASP   A CA  1 
ATOM   756  C C   . ASP   A 1 102 ? 26.764  9.944   10.740  1.00 33.03 ? 101 ASP   A C   1 
ATOM   757  O O   . ASP   A 1 102 ? 27.495  10.929  10.662  1.00 33.71 ? 101 ASP   A O   1 
ATOM   758  C CB  . ASP   A 1 102 ? 24.821  10.149  12.286  1.00 33.78 ? 101 ASP   A CB  1 
ATOM   759  C CG  . ASP   A 1 102 ? 23.346  10.353  12.507  1.00 38.60 ? 101 ASP   A CG  1 
ATOM   760  O OD1 . ASP   A 1 102 ? 22.718  11.075  11.690  1.00 38.89 ? 101 ASP   A OD1 1 
ATOM   761  O OD2 . ASP   A 1 102 ? 22.810  9.792   13.506  1.00 38.85 ? 101 ASP   A OD2 1 
ATOM   762  N N   . ILE   A 1 103 ? 27.236  8.687   10.717  1.00 32.83 ? 102 ILE   A N   1 
ATOM   763  C CA  . ILE   A 1 103 ? 28.646  8.403   10.646  1.00 31.72 ? 102 ILE   A CA  1 
ATOM   764  C C   . ILE   A 1 103 ? 29.209  8.514   9.237   1.00 31.50 ? 102 ILE   A C   1 
ATOM   765  O O   . ILE   A 1 103 ? 30.169  9.273   9.052   1.00 31.38 ? 102 ILE   A O   1 
ATOM   766  C CB  . ILE   A 1 103 ? 28.936  7.030   11.285  1.00 32.11 ? 102 ILE   A CB  1 
ATOM   767  C CG1 . ILE   A 1 103 ? 28.586  7.048   12.782  1.00 31.98 ? 102 ILE   A CG1 1 
ATOM   768  C CG2 . ILE   A 1 103 ? 30.393  6.590   11.049  1.00 32.54 ? 102 ILE   A CG2 1 
ATOM   769  C CD1 . ILE   A 1 103 ? 28.561  5.664   13.387  1.00 32.54 ? 102 ILE   A CD1 1 
ATOM   770  N N   . TYR   A 1 104 ? 28.629  7.808   8.239   1.00 31.04 ? 103 TYR   A N   1 
ATOM   771  C CA  . TYR   A 1 104 ? 29.193  7.873   6.896   1.00 31.62 ? 103 TYR   A CA  1 
ATOM   772  C C   . TYR   A 1 104 ? 29.083  9.283   6.263   1.00 33.35 ? 103 TYR   A C   1 
ATOM   773  O O   . TYR   A 1 104 ? 29.878  9.578   5.387   1.00 34.93 ? 103 TYR   A O   1 
ATOM   774  C CB  . TYR   A 1 104 ? 28.721  6.756   5.945   1.00 30.43 ? 103 TYR   A CB  1 
ATOM   775  C CG  . TYR   A 1 104 ? 27.290  6.789   5.473   1.00 30.75 ? 103 TYR   A CG  1 
ATOM   776  C CD1 . TYR   A 1 104 ? 26.826  7.821   4.657   1.00 30.55 ? 103 TYR   A CD1 1 
ATOM   777  C CD2 . TYR   A 1 104 ? 26.439  5.710   5.702   1.00 29.42 ? 103 TYR   A CD2 1 
ATOM   778  C CE1 . TYR   A 1 104 ? 25.507  7.838   4.206   1.00 31.03 ? 103 TYR   A CE1 1 
ATOM   779  C CE2 . TYR   A 1 104 ? 25.125  5.723   5.272   1.00 30.68 ? 103 TYR   A CE2 1 
ATOM   780  C CZ  . TYR   A 1 104 ? 24.666  6.780   4.509   1.00 31.21 ? 103 TYR   A CZ  1 
ATOM   781  O OH  . TYR   A 1 104 ? 23.380  6.751   4.060   1.00 32.92 ? 103 TYR   A OH  1 
ATOM   782  N N   . GLN   A 1 105 ? 28.151  10.144  6.719   1.00 32.61 ? 104 GLN   A N   1 
ATOM   783  C CA  . GLN   A 1 105 ? 28.062  11.513  6.201   1.00 33.97 ? 104 GLN   A CA  1 
ATOM   784  C C   . GLN   A 1 105 ? 29.079  12.475  6.888   1.00 35.12 ? 104 GLN   A C   1 
ATOM   785  O O   . GLN   A 1 105 ? 29.000  13.699  6.751   1.00 36.29 ? 104 GLN   A O   1 
ATOM   786  C CB  . GLN   A 1 105 ? 26.619  12.042  6.246   1.00 35.33 ? 104 GLN   A CB  1 
ATOM   787  C CG  . GLN   A 1 105 ? 25.688  11.265  5.307   1.00 37.27 ? 104 GLN   A CG  1 
ATOM   788  C CD  . GLN   A 1 105 ? 24.304  11.874  5.210   1.00 38.45 ? 104 GLN   A CD  1 
ATOM   789  O OE1 . GLN   A 1 105 ? 23.724  12.286  6.212   1.00 39.44 ? 104 GLN   A OE1 1 
ATOM   790  N NE2 . GLN   A 1 105 ? 23.730  11.901  4.005   1.00 35.44 ? 104 GLN   A NE2 1 
ATOM   791  N N   . VAL   A 1 106 ? 30.019  11.908  7.640   1.00 36.02 ? 105 VAL   A N   1 
ATOM   792  C CA  . VAL   A 1 106 ? 31.189  12.553  8.186   1.00 37.38 ? 105 VAL   A CA  1 
ATOM   793  C C   . VAL   A 1 106 ? 32.399  11.822  7.624   1.00 37.76 ? 105 VAL   A C   1 
ATOM   794  O O   . VAL   A 1 106 ? 33.202  12.448  6.948   1.00 39.15 ? 105 VAL   A O   1 
ATOM   795  C CB  . VAL   A 1 106 ? 31.256  12.677  9.729   1.00 39.23 ? 105 VAL   A CB  1 
ATOM   796  C CG1 . VAL   A 1 106 ? 32.628  13.235  10.163  1.00 40.17 ? 105 VAL   A CG1 1 
ATOM   797  C CG2 . VAL   A 1 106 ? 30.124  13.549  10.256  1.00 39.78 ? 105 VAL   A CG2 1 
ATOM   798  N N   . THR   A 1 107 ? 32.524  10.499  7.871   1.00 37.31 ? 106 THR   A N   1 
ATOM   799  C CA  . THR   A 1 107 ? 33.698  9.689   7.479   1.00 38.31 ? 106 THR   A CA  1 
ATOM   800  C C   . THR   A 1 107 ? 33.864  9.347   5.983   1.00 39.87 ? 106 THR   A C   1 
ATOM   801  O O   . THR   A 1 107 ? 34.952  8.988   5.571   1.00 39.79 ? 106 THR   A O   1 
ATOM   802  C CB  . THR   A 1 107 ? 33.637  8.297   8.181   1.00 37.79 ? 106 THR   A CB  1 
ATOM   803  O OG1 . THR   A 1 107 ? 32.547  7.522   7.658   1.00 36.29 ? 106 THR   A OG1 1 
ATOM   804  C CG2 . THR   A 1 107 ? 33.564  8.382   9.692   1.00 37.77 ? 106 THR   A CG2 1 
ATOM   805  N N   . GLY   A 1 108 ? 32.768  9.326   5.225   1.00 40.14 ? 107 GLY   A N   1 
ATOM   806  C CA  . GLY   A 1 108 ? 32.813  8.794   3.863   1.00 39.90 ? 107 GLY   A CA  1 
ATOM   807  C C   . GLY   A 1 108 ? 32.558  7.284   3.888   1.00 38.37 ? 107 GLY   A C   1 
ATOM   808  O O   . GLY   A 1 108 ? 32.269  6.708   4.943   1.00 37.43 ? 107 GLY   A O   1 
ATOM   809  N N   . SER   A 1 109 ? 32.692  6.622   2.731   1.00 37.16 ? 108 SER   A N   1 
ATOM   810  C CA  . SER   A 1 109 ? 32.352  5.223   2.567   1.00 37.07 ? 108 SER   A CA  1 
ATOM   811  C C   . SER   A 1 109 ? 33.068  4.251   3.512   1.00 36.26 ? 108 SER   A C   1 
ATOM   812  O O   . SER   A 1 109 ? 34.268  4.389   3.766   1.00 36.36 ? 108 SER   A O   1 
ATOM   813  C CB  . SER   A 1 109 ? 32.555  4.799   1.117   1.00 38.45 ? 108 SER   A CB  1 
ATOM   814  O OG  . SER   A 1 109 ? 33.933  4.604   0.875   1.00 43.01 ? 108 SER   A OG  1 
ATOM   815  N N   . LEU   A 1 110 ? 32.320  3.274   4.015   1.00 35.48 ? 109 LEU   A N   1 
ATOM   816  C CA  . LEU   A 1 110 ? 32.869  2.243   4.886   1.00 34.28 ? 109 LEU   A CA  1 
ATOM   817  C C   . LEU   A 1 110 ? 33.729  1.273   4.062   1.00 35.24 ? 109 LEU   A C   1 
ATOM   818  O O   . LEU   A 1 110 ? 33.537  1.112   2.850   1.00 35.28 ? 109 LEU   A O   1 
ATOM   819  C CB  . LEU   A 1 110 ? 31.741  1.471   5.599   1.00 32.69 ? 109 LEU   A CB  1 
ATOM   820  C CG  . LEU   A 1 110 ? 31.286  2.041   6.940   1.00 33.61 ? 109 LEU   A CG  1 
ATOM   821  C CD1 . LEU   A 1 110 ? 30.594  3.396   6.761   1.00 33.93 ? 109 LEU   A CD1 1 
ATOM   822  C CD2 . LEU   A 1 110 ? 30.393  1.071   7.707   1.00 34.14 ? 109 LEU   A CD2 1 
ATOM   823  N N   . SER   A 1 111 ? 34.688  0.625   4.728   1.00 35.05 ? 110 SER   A N   1 
ATOM   824  C CA  . SER   A 1 111 ? 35.521  -0.365  4.079   1.00 35.17 ? 110 SER   A CA  1 
ATOM   825  C C   . SER   A 1 111 ? 34.712  -1.643  3.915   1.00 35.29 ? 110 SER   A C   1 
ATOM   826  O O   . SER   A 1 111 ? 33.694  -1.825  4.601   1.00 34.95 ? 110 SER   A O   1 
ATOM   827  C CB  . SER   A 1 111 ? 36.776  -0.625  4.915   1.00 35.52 ? 110 SER   A CB  1 
ATOM   828  O OG  . SER   A 1 111 ? 36.439  -1.450  6.022   1.00 37.87 ? 110 SER   A OG  1 
ATOM   829  N N   . GLU   A 1 112 ? 35.197  -2.576  3.082   1.00 35.75 ? 111 GLU   A N   1 
ATOM   830  C CA  . GLU   A 1 112 ? 34.468  -3.827  2.902   1.00 36.39 ? 111 GLU   A CA  1 
ATOM   831  C C   . GLU   A 1 112 ? 34.356  -4.625  4.216   1.00 37.06 ? 111 GLU   A C   1 
ATOM   832  O O   . GLU   A 1 112 ? 33.309  -5.230  4.503   1.00 36.88 ? 111 GLU   A O   1 
ATOM   833  C CB  . GLU   A 1 112 ? 35.052  -4.655  1.779   1.00 37.26 ? 111 GLU   A CB  1 
ATOM   834  C CG  . GLU   A 1 112 ? 34.255  -5.924  1.533   1.00 38.26 ? 111 GLU   A CG  1 
ATOM   835  C CD  . GLU   A 1 112 ? 34.799  -6.711  0.368   1.00 41.94 ? 111 GLU   A CD  1 
ATOM   836  O OE1 . GLU   A 1 112 ? 35.109  -6.075  -0.666  1.00 41.79 ? 111 GLU   A OE1 1 
ATOM   837  O OE2 . GLU   A 1 112 ? 34.909  -7.958  0.478   1.00 42.97 ? 111 GLU   A OE2 1 
ATOM   838  N N   . LEU   A 1 113 ? 35.393  -4.555  5.039   1.00 36.35 ? 112 LEU   A N   1 
ATOM   839  C CA  . LEU   A 1 113 ? 35.401  -5.265  6.323   1.00 36.34 ? 112 LEU   A CA  1 
ATOM   840  C C   . LEU   A 1 113 ? 34.425  -4.665  7.299   1.00 35.20 ? 112 LEU   A C   1 
ATOM   841  O O   . LEU   A 1 113 ? 33.695  -5.401  7.946   1.00 35.39 ? 112 LEU   A O   1 
ATOM   842  C CB  . LEU   A 1 113 ? 36.827  -5.273  6.914   1.00 36.57 ? 112 LEU   A CB  1 
ATOM   843  C CG  . LEU   A 1 113 ? 37.707  -6.364  6.331   1.00 40.02 ? 112 LEU   A CG  1 
ATOM   844  C CD1 . LEU   A 1 113 ? 39.177  -6.158  6.734   1.00 40.55 ? 112 LEU   A CD1 1 
ATOM   845  C CD2 . LEU   A 1 113 ? 37.204  -7.752  6.742   1.00 41.67 ? 112 LEU   A CD2 1 
ATOM   846  N N   . GLN   A 1 114 ? 34.338  -3.338  7.342   1.00 33.69 ? 113 GLN   A N   1 
ATOM   847  C CA  . GLN   A 1 114 ? 33.372  -2.640  8.190   1.00 32.39 ? 113 GLN   A CA  1 
ATOM   848  C C   . GLN   A 1 114 ? 31.936  -2.974  7.783   1.00 32.04 ? 113 GLN   A C   1 
ATOM   849  O O   . GLN   A 1 114 ? 31.104  -3.317  8.627   1.00 32.43 ? 113 GLN   A O   1 
ATOM   850  C CB  . GLN   A 1 114 ? 33.613  -1.133  8.097   1.00 31.70 ? 113 GLN   A CB  1 
ATOM   851  C CG  . GLN   A 1 114 ? 34.919  -0.776  8.798   1.00 33.88 ? 113 GLN   A CG  1 
ATOM   852  C CD  . GLN   A 1 114 ? 35.411  0.611   8.500   1.00 35.41 ? 113 GLN   A CD  1 
ATOM   853  O OE1 . GLN   A 1 114 ? 35.028  1.238   7.502   1.00 33.69 ? 113 GLN   A OE1 1 
ATOM   854  N NE2 . GLN   A 1 114 ? 36.320  1.079   9.332   1.00 33.57 ? 113 GLN   A NE2 1 
ATOM   855  N N   . ILE   A 1 115 ? 31.643  -2.932  6.471   1.00 31.53 ? 114 ILE   A N   1 
ATOM   856  C CA  . ILE   A 1 115 ? 30.307  -3.283  5.980   1.00 30.70 ? 114 ILE   A CA  1 
ATOM   857  C C   . ILE   A 1 115 ? 29.991  -4.738  6.311   1.00 30.88 ? 114 ILE   A C   1 
ATOM   858  O O   . ILE   A 1 115 ? 28.914  -5.037  6.802   1.00 31.25 ? 114 ILE   A O   1 
ATOM   859  C CB  . ILE   A 1 115 ? 30.228  -3.035  4.464   1.00 30.92 ? 114 ILE   A CB  1 
ATOM   860  C CG1 . ILE   A 1 115 ? 30.446  -1.552  4.171   1.00 31.34 ? 114 ILE   A CG1 1 
ATOM   861  C CG2 . ILE   A 1 115 ? 28.871  -3.537  3.886   1.00 30.05 ? 114 ILE   A CG2 1 
ATOM   862  C CD1 . ILE   A 1 115 ? 30.577  -1.241  2.675   1.00 33.28 ? 114 ILE   A CD1 1 
ATOM   863  N N   . SER   A 1 116 ? 30.972  -5.626  6.164   1.00 30.38 ? 115 SER   A N   1 
ATOM   864  C CA  . SER   A 1 116 ? 30.787  -7.046  6.486   1.00 30.36 ? 115 SER   A CA  1 
ATOM   865  C C   . SER   A 1 116 ? 30.351  -7.240  7.952   1.00 29.29 ? 115 SER   A C   1 
ATOM   866  O O   . SER   A 1 116 ? 29.403  -7.974  8.213   1.00 29.32 ? 115 SER   A O   1 
ATOM   867  C CB  . SER   A 1 116 ? 32.094  -7.808  6.245   1.00 32.15 ? 115 SER   A CB  1 
ATOM   868  O OG  . SER   A 1 116 ? 32.436  -7.823  4.871   1.00 35.54 ? 115 SER   A OG  1 
ATOM   869  N N   . TYR   A 1 117 ? 31.065  -6.594  8.904   1.00 28.91 ? 116 TYR   A N   1 
ATOM   870  C CA  . TYR   A 1 117 ? 30.718  -6.675  10.319  1.00 30.21 ? 116 TYR   A CA  1 
ATOM   871  C C   . TYR   A 1 117 ? 29.313  -6.104  10.553  1.00 29.96 ? 116 TYR   A C   1 
ATOM   872  O O   . TYR   A 1 117 ? 28.489  -6.792  11.140  1.00 29.39 ? 116 TYR   A O   1 
ATOM   873  C CB  . TYR   A 1 117 ? 31.753  -5.921  11.171  1.00 31.74 ? 116 TYR   A CB  1 
ATOM   874  C CG  . TYR   A 1 117 ? 31.345  -5.713  12.617  1.00 33.99 ? 116 TYR   A CG  1 
ATOM   875  C CD1 . TYR   A 1 117 ? 31.338  -6.773  13.523  1.00 35.71 ? 116 TYR   A CD1 1 
ATOM   876  C CD2 . TYR   A 1 117 ? 31.085  -4.443  13.107  1.00 35.94 ? 116 TYR   A CD2 1 
ATOM   877  C CE1 . TYR   A 1 117 ? 31.006  -6.573  14.866  1.00 37.27 ? 116 TYR   A CE1 1 
ATOM   878  C CE2 . TYR   A 1 117 ? 30.746  -4.235  14.438  1.00 37.46 ? 116 TYR   A CE2 1 
ATOM   879  C CZ  . TYR   A 1 117 ? 30.734  -5.293  15.318  1.00 39.19 ? 116 TYR   A CZ  1 
ATOM   880  O OH  . TYR   A 1 117 ? 30.380  -5.029  16.615  1.00 42.79 ? 116 TYR   A OH  1 
ATOM   881  N N   . VAL   A 1 118 ? 29.002  -4.867  10.055  1.00 29.55 ? 117 VAL   A N   1 
ATOM   882  C CA  . VAL   A 1 118 ? 27.646  -4.331  10.229  1.00 29.78 ? 117 VAL   A CA  1 
ATOM   883  C C   . VAL   A 1 118 ? 26.569  -5.319  9.686   1.00 30.01 ? 117 VAL   A C   1 
ATOM   884  O O   . VAL   A 1 118 ? 25.559  -5.543  10.376  1.00 29.76 ? 117 VAL   A O   1 
ATOM   885  C CB  . VAL   A 1 118 ? 27.521  -2.942  9.559   1.00 30.13 ? 117 VAL   A CB  1 
ATOM   886  C CG1 . VAL   A 1 118 ? 26.064  -2.555  9.386   1.00 30.30 ? 117 VAL   A CG1 1 
ATOM   887  C CG2 . VAL   A 1 118 ? 28.318  -1.880  10.337  1.00 29.93 ? 117 VAL   A CG2 1 
ATOM   888  N N   . CYS   A 1 119 ? 26.762  -5.851  8.457   1.00 28.78 ? 118 CYS   A N   1 
ATOM   889  C CA  . CYS   A 1 119 ? 25.803  -6.801  7.863   1.00 28.47 ? 118 CYS   A CA  1 
ATOM   890  C C   . CYS   A 1 119 ? 25.659  -8.054  8.726   1.00 28.67 ? 118 CYS   A C   1 
ATOM   891  O O   . CYS   A 1 119 ? 24.559  -8.539  8.850   1.00 30.05 ? 118 CYS   A O   1 
ATOM   892  C CB  . CYS   A 1 119 ? 26.179  -7.173  6.423   1.00 28.66 ? 118 CYS   A CB  1 
ATOM   893  S SG  . CYS   A 1 119 ? 25.945  -5.838  5.234   1.00 32.13 ? 118 CYS   A SG  1 
ATOM   894  N N   . ARG   A 1 120 ? 26.743  -8.573  9.320   1.00 28.95 ? 119 ARG   A N   1 
ATOM   895  C CA  . ARG   A 1 120 ? 26.627  -9.739  10.200  1.00 29.57 ? 119 ARG   A CA  1 
ATOM   896  C C   . ARG   A 1 120 ? 25.753  -9.400  11.444  1.00 29.75 ? 119 ARG   A C   1 
ATOM   897  O O   . ARG   A 1 120 ? 24.869  -10.174 11.823  1.00 30.38 ? 119 ARG   A O   1 
ATOM   898  C CB  . ARG   A 1 120 ? 28.010  -10.259 10.669  1.00 30.30 ? 119 ARG   A CB  1 
ATOM   899  C CG  . ARG   A 1 120 ? 27.869  -11.585 11.381  1.00 30.65 ? 119 ARG   A CG  1 
ATOM   900  C CD  . ARG   A 1 120 ? 29.106  -11.965 12.180  1.00 33.18 ? 119 ARG   A CD  1 
ATOM   901  N NE  . ARG   A 1 120 ? 29.355  -11.017 13.259  1.00 35.45 ? 119 ARG   A NE  1 
ATOM   902  C CZ  . ARG   A 1 120 ? 30.479  -10.952 13.967  1.00 38.17 ? 119 ARG   A CZ  1 
ATOM   903  N NH1 . ARG   A 1 120 ? 31.483  -11.789 13.715  1.00 36.69 ? 119 ARG   A NH1 1 
ATOM   904  N NH2 . ARG   A 1 120 ? 30.615  -10.039 14.919  1.00 39.13 ? 119 ARG   A NH2 1 
ATOM   905  N N   . GLU   A 1 121 ? 26.033  -8.278  12.091  1.00 29.84 ? 120 GLU   A N   1 
ATOM   906  C CA  . GLU   A 1 121 ? 25.320  -7.894  13.313  1.00 29.85 ? 120 GLU   A CA  1 
ATOM   907  C C   . GLU   A 1 121 ? 23.850  -7.632  13.020  1.00 29.81 ? 120 GLU   A C   1 
ATOM   908  O O   . GLU   A 1 121 ? 23.000  -8.070  13.783  1.00 29.92 ? 120 GLU   A O   1 
ATOM   909  C CB  . GLU   A 1 121 ? 25.990  -6.663  13.949  1.00 31.03 ? 120 GLU   A CB  1 
ATOM   910  C CG  . GLU   A 1 121 ? 27.436  -6.989  14.311  1.00 30.12 ? 120 GLU   A CG  1 
ATOM   911  C CD  . GLU   A 1 121 ? 27.531  -8.030  15.414  1.00 33.68 ? 120 GLU   A CD  1 
ATOM   912  O OE1 . GLU   A 1 121 ? 27.094  -7.732  16.549  1.00 35.39 ? 120 GLU   A OE1 1 
ATOM   913  O OE2 . GLU   A 1 121 ? 28.012  -9.151  15.150  1.00 35.40 ? 120 GLU   A OE2 1 
ATOM   914  N N   . VAL   A 1 122 ? 23.548  -7.013  11.869  1.00 28.80 ? 121 VAL   A N   1 
ATOM   915  C CA  . VAL   A 1 122 ? 22.156  -6.745  11.488  1.00 27.68 ? 121 VAL   A CA  1 
ATOM   916  C C   . VAL   A 1 122 ? 21.447  -8.055  11.181  1.00 28.87 ? 121 VAL   A C   1 
ATOM   917  O O   . VAL   A 1 122 ? 20.276  -8.214  11.578  1.00 28.63 ? 121 VAL   A O   1 
ATOM   918  C CB  . VAL   A 1 122 ? 22.040  -5.744  10.309  1.00 28.06 ? 121 VAL   A CB  1 
ATOM   919  C CG1 . VAL   A 1 122 ? 20.602  -5.671  9.773   1.00 27.74 ? 121 VAL   A CG1 1 
ATOM   920  C CG2 . VAL   A 1 122 ? 22.513  -4.351  10.736  1.00 28.59 ? 121 VAL   A CG2 1 
ATOM   921  N N   . LEU   A 1 123 ? 22.121  -8.987  10.495  1.00 29.24 ? 122 LEU   A N   1 
ATOM   922  C CA  . LEU   A 1 123 ? 21.505  -10.301 10.181  1.00 29.18 ? 122 LEU   A CA  1 
ATOM   923  C C   . LEU   A 1 123 ? 21.189  -11.050 11.464  1.00 29.65 ? 122 LEU   A C   1 
ATOM   924  O O   . LEU   A 1 123 ? 20.190  -11.767 11.512  1.00 30.00 ? 122 LEU   A O   1 
ATOM   925  C CB  . LEU   A 1 123 ? 22.408  -11.176 9.261   1.00 29.02 ? 122 LEU   A CB  1 
ATOM   926  C CG  . LEU   A 1 123 ? 22.485  -10.736 7.771   1.00 29.04 ? 122 LEU   A CG  1 
ATOM   927  C CD1 . LEU   A 1 123 ? 23.667  -11.423 7.066   1.00 27.93 ? 122 LEU   A CD1 1 
ATOM   928  C CD2 . LEU   A 1 123 ? 21.154  -11.057 7.007   1.00 29.19 ? 122 LEU   A CD2 1 
ATOM   929  N N   . GLN   A 1 124 ? 22.026  -10.902 12.510  1.00 29.71 ? 123 GLN   A N   1 
ATOM   930  C CA  . GLN   A 1 124 ? 21.747  -11.582 13.798  1.00 29.66 ? 123 GLN   A CA  1 
ATOM   931  C C   . GLN   A 1 124 ? 20.450  -11.053 14.399  1.00 30.27 ? 123 GLN   A C   1 
ATOM   932  O O   . GLN   A 1 124 ? 19.662  -11.829 14.921  1.00 30.67 ? 123 GLN   A O   1 
ATOM   933  C CB  . GLN   A 1 124 ? 22.914  -11.384 14.772  1.00 29.43 ? 123 GLN   A CB  1 
ATOM   934  C CG  . GLN   A 1 124 ? 24.139  -12.170 14.314  1.00 29.45 ? 123 GLN   A CG  1 
ATOM   935  C CD  . GLN   A 1 124 ? 25.427  -11.718 14.932  1.00 36.83 ? 123 GLN   A CD  1 
ATOM   936  O OE1 . GLN   A 1 124 ? 25.492  -10.805 15.765  1.00 39.70 ? 123 GLN   A OE1 1 
ATOM   937  N NE2 . GLN   A 1 124 ? 26.489  -12.364 14.537  1.00 36.74 ? 123 GLN   A NE2 1 
ATOM   938  N N   . GLY   A 1 125 ? 20.263  -9.737  14.337  1.00 30.25 ? 124 GLY   A N   1 
ATOM   939  C CA  . GLY   A 1 125 ? 19.043  -9.093  14.808  1.00 30.21 ? 124 GLY   A CA  1 
ATOM   940  C C   . GLY   A 1 125 ? 17.843  -9.492  13.966  1.00 29.53 ? 124 GLY   A C   1 
ATOM   941  O O   . GLY   A 1 125 ? 16.768  -9.735  14.501  1.00 29.01 ? 124 GLY   A O   1 
ATOM   942  N N   . LEU   A 1 126 ? 18.005  -9.553  12.622  1.00 28.92 ? 125 LEU   A N   1 
ATOM   943  C CA  . LEU   A 1 126 ? 16.898  -9.924  11.726  1.00 28.23 ? 125 LEU   A CA  1 
ATOM   944  C C   . LEU   A 1 126 ? 16.504  -11.363 11.902  1.00 28.67 ? 125 LEU   A C   1 
ATOM   945  O O   . LEU   A 1 126 ? 15.310  -11.669 11.915  1.00 28.45 ? 125 LEU   A O   1 
ATOM   946  C CB  . LEU   A 1 126 ? 17.291  -9.690  10.257  1.00 28.06 ? 125 LEU   A CB  1 
ATOM   947  C CG  . LEU   A 1 126 ? 17.267  -8.248  9.795   1.00 28.02 ? 125 LEU   A CG  1 
ATOM   948  C CD1 . LEU   A 1 126 ? 17.751  -8.151  8.349   1.00 29.18 ? 125 LEU   A CD1 1 
ATOM   949  C CD2 . LEU   A 1 126 ? 15.854  -7.641  9.952   1.00 28.20 ? 125 LEU   A CD2 1 
ATOM   950  N N   . ALA   A 1 127 ? 17.486  -12.258 12.080  1.00 28.53 ? 126 ALA   A N   1 
ATOM   951  C CA  . ALA   A 1 127 ? 17.179  -13.673 12.309  1.00 29.61 ? 126 ALA   A CA  1 
ATOM   952  C C   . ALA   A 1 127 ? 16.384  -13.835 13.600  1.00 30.98 ? 126 ALA   A C   1 
ATOM   953  O O   . ALA   A 1 127 ? 15.485  -14.688 13.666  1.00 31.36 ? 126 ALA   A O   1 
ATOM   954  C CB  . ALA   A 1 127 ? 18.473  -14.493 12.382  1.00 28.98 ? 126 ALA   A CB  1 
ATOM   955  N N   . TYR   A 1 128 ? 16.692  -13.014 14.624  1.00 31.74 ? 127 TYR   A N   1 
ATOM   956  C CA  . TYR   A 1 128 ? 15.950  -13.092 15.887  1.00 32.96 ? 127 TYR   A CA  1 
ATOM   957  C C   . TYR   A 1 128 ? 14.523  -12.571 15.615  1.00 32.23 ? 127 TYR   A C   1 
ATOM   958  O O   . TYR   A 1 128 ? 13.573  -13.271 15.917  1.00 32.48 ? 127 TYR   A O   1 
ATOM   959  C CB  . TYR   A 1 128 ? 16.616  -12.238 16.992  1.00 33.76 ? 127 TYR   A CB  1 
ATOM   960  C CG  . TYR   A 1 128 ? 15.697  -12.073 18.187  1.00 35.99 ? 127 TYR   A CG  1 
ATOM   961  C CD1 . TYR   A 1 128 ? 15.475  -13.125 19.068  1.00 37.60 ? 127 TYR   A CD1 1 
ATOM   962  C CD2 . TYR   A 1 128 ? 14.974  -10.902 18.375  1.00 37.44 ? 127 TYR   A CD2 1 
ATOM   963  C CE1 . TYR   A 1 128 ? 14.609  -12.992 20.145  1.00 39.16 ? 127 TYR   A CE1 1 
ATOM   964  C CE2 . TYR   A 1 128 ? 14.091  -10.763 19.438  1.00 38.96 ? 127 TYR   A CE2 1 
ATOM   965  C CZ  . TYR   A 1 128 ? 13.905  -11.811 20.315  1.00 40.94 ? 127 TYR   A CZ  1 
ATOM   966  O OH  . TYR   A 1 128 ? 13.034  -11.650 21.364  1.00 43.86 ? 127 TYR   A OH  1 
ATOM   967  N N   . LEU   A 1 129 ? 14.379  -11.377 15.016  1.00 31.86 ? 128 LEU   A N   1 
ATOM   968  C CA  . LEU   A 1 129 ? 13.059  -10.824 14.700  1.00 31.71 ? 128 LEU   A CA  1 
ATOM   969  C C   . LEU   A 1 129 ? 12.200  -11.775 13.885  1.00 32.16 ? 128 LEU   A C   1 
ATOM   970  O O   . LEU   A 1 129 ? 11.056  -12.003 14.246  1.00 33.15 ? 128 LEU   A O   1 
ATOM   971  C CB  . LEU   A 1 129 ? 13.174  -9.464  13.998  1.00 32.31 ? 128 LEU   A CB  1 
ATOM   972  C CG  . LEU   A 1 129 ? 13.725  -8.341  14.891  1.00 34.39 ? 128 LEU   A CG  1 
ATOM   973  C CD1 . LEU   A 1 129 ? 13.858  -7.055  14.131  1.00 33.74 ? 128 LEU   A CD1 1 
ATOM   974  C CD2 . LEU   A 1 129 ? 12.842  -8.134  16.127  1.00 36.66 ? 128 LEU   A CD2 1 
ATOM   975  N N   . HIS   A 1 130 ? 12.765  -12.416 12.878  1.00 31.74 ? 129 HIS   A N   1 
ATOM   976  C CA  . HIS   A 1 130 ? 12.021  -13.380 12.053  1.00 31.98 ? 129 HIS   A CA  1 
ATOM   977  C C   . HIS   A 1 130 ? 11.608  -14.636 12.876  1.00 33.43 ? 129 HIS   A C   1 
ATOM   978  O O   . HIS   A 1 130 ? 10.492  -15.139 12.702  1.00 33.07 ? 129 HIS   A O   1 
ATOM   979  C CB  . HIS   A 1 130 ? 12.855  -13.725 10.797  1.00 30.61 ? 129 HIS   A CB  1 
ATOM   980  C CG  . HIS   A 1 130 ? 13.099  -12.549 9.888   1.00 31.35 ? 129 HIS   A CG  1 
ATOM   981  N ND1 . HIS   A 1 130 ? 14.023  -12.622 8.838   1.00 31.22 ? 129 HIS   A ND1 1 
ATOM   982  C CD2 . HIS   A 1 130 ? 12.588  -11.291 9.914   1.00 31.15 ? 129 HIS   A CD2 1 
ATOM   983  C CE1 . HIS   A 1 130 ? 13.983  -11.451 8.241   1.00 30.43 ? 129 HIS   A CE1 1 
ATOM   984  N NE2 . HIS   A 1 130 ? 13.156  -10.612 8.854   1.00 31.28 ? 129 HIS   A NE2 1 
ATOM   985  N N   . SER   A 1 131 ? 12.443  -15.078 13.837  1.00 35.06 ? 130 SER   A N   1 
ATOM   986  C CA  . SER   A 1 131 ? 12.058  -16.205 14.707  1.00 37.02 ? 130 SER   A CA  1 
ATOM   987  C C   . SER   A 1 131 ? 10.853  -15.824 15.606  1.00 38.85 ? 130 SER   A C   1 
ATOM   988  O O   . SER   A 1 131 ? 10.074  -16.700 16.007  1.00 39.24 ? 130 SER   A O   1 
ATOM   989  C CB  . SER   A 1 131 ? 13.246  -16.696 15.538  1.00 38.17 ? 130 SER   A CB  1 
ATOM   990  O OG  . SER   A 1 131 ? 13.624  -15.738 16.509  1.00 40.08 ? 130 SER   A OG  1 
ATOM   991  N N   . GLN   A 1 132 ? 10.676  -14.529 15.888  1.00 38.74 ? 131 GLN   A N   1 
ATOM   992  C CA  . GLN   A 1 132 ? 9.520   -14.047 16.647  1.00 39.91 ? 131 GLN   A CA  1 
ATOM   993  C C   . GLN   A 1 132 ? 8.339   -13.693 15.724  1.00 39.00 ? 131 GLN   A C   1 
ATOM   994  O O   . GLN   A 1 132 ? 7.414   -13.023 16.183  1.00 39.50 ? 131 GLN   A O   1 
ATOM   995  C CB  . GLN   A 1 132 ? 9.921   -12.798 17.463  1.00 43.44 ? 131 GLN   A CB  1 
ATOM   996  C CG  . GLN   A 1 132 ? 11.162  -13.013 18.329  1.00 48.21 ? 131 GLN   A CG  1 
ATOM   997  C CD  . GLN   A 1 132 ? 10.846  -14.043 19.379  1.00 54.42 ? 131 GLN   A CD  1 
ATOM   998  O OE1 . GLN   A 1 132 ? 10.081  -13.780 20.305  1.00 57.31 ? 131 GLN   A OE1 1 
ATOM   999  N NE2 . GLN   A 1 132 ? 11.376  -15.252 19.223  1.00 54.61 ? 131 GLN   A NE2 1 
ATOM   1000 N N   . LYS   A 1 133 ? 8.387   -14.090 14.424  1.00 37.61 ? 132 LYS   A N   1 
ATOM   1001 C CA  . LYS   A 1 133 ? 7.345   -13.842 13.428  1.00 38.18 ? 132 LYS   A CA  1 
ATOM   1002 C C   . LYS   A 1 133 ? 7.080   -12.344 13.227  1.00 37.66 ? 132 LYS   A C   1 
ATOM   1003 O O   . LYS   A 1 133 ? 5.952   -11.924 12.992  1.00 38.48 ? 132 LYS   A O   1 
ATOM   1004 C CB  . LYS   A 1 133 ? 6.037   -14.638 13.737  1.00 41.90 ? 132 LYS   A CB  1 
ATOM   1005 C CG  . LYS   A 1 133 ? 6.232   -16.154 13.861  1.00 46.87 ? 132 LYS   A CG  1 
ATOM   1006 C CD  . LYS   A 1 133 ? 4.872   -16.856 13.847  1.00 55.04 ? 132 LYS   A CD  1 
ATOM   1007 C CE  . LYS   A 1 133 ? 4.959   -18.368 13.971  1.00 61.94 ? 132 LYS   A CE  1 
ATOM   1008 N NZ  . LYS   A 1 133 ? 5.422   -18.792 15.321  1.00 65.60 ? 132 LYS   A NZ  1 
ATOM   1009 N N   . LYS   A 1 134 ? 8.131   -11.552 13.335  1.00 36.48 ? 133 LYS   A N   1 
ATOM   1010 C CA  . LYS   A 1 134 ? 8.109   -10.121 13.062  1.00 35.88 ? 133 LYS   A CA  1 
ATOM   1011 C C   . LYS   A 1 134 ? 8.877   -9.829  11.780  1.00 33.83 ? 133 LYS   A C   1 
ATOM   1012 O O   . LYS   A 1 134 ? 9.875   -10.496 11.496  1.00 34.80 ? 133 LYS   A O   1 
ATOM   1013 C CB  . LYS   A 1 134 ? 8.752   -9.325  14.203  1.00 38.53 ? 133 LYS   A CB  1 
ATOM   1014 C CG  . LYS   A 1 134 ? 7.866   -9.259  15.442  1.00 43.59 ? 133 LYS   A CG  1 
ATOM   1015 C CD  . LYS   A 1 134 ? 8.189   -8.011  16.196  1.00 49.85 ? 133 LYS   A CD  1 
ATOM   1016 C CE  . LYS   A 1 134 ? 7.488   -7.989  17.511  1.00 54.59 ? 133 LYS   A CE  1 
ATOM   1017 N NZ  . LYS   A 1 134 ? 7.871   -9.163  18.340  1.00 58.44 ? 133 LYS   A NZ  1 
ATOM   1018 N N   . ILE   A 1 135 ? 8.422   -8.827  11.010  1.00 31.17 ? 134 ILE   A N   1 
ATOM   1019 C CA  . ILE   A 1 135 ? 9.132   -8.370  9.828   1.00 29.29 ? 134 ILE   A CA  1 
ATOM   1020 C C   . ILE   A 1 135 ? 9.568   -6.951  10.161  1.00 28.45 ? 134 ILE   A C   1 
ATOM   1021 O O   . ILE   A 1 135 ? 8.739   -6.172  10.630  1.00 29.43 ? 134 ILE   A O   1 
ATOM   1022 C CB  . ILE   A 1 135 ? 8.240   -8.401  8.578   1.00 28.64 ? 134 ILE   A CB  1 
ATOM   1023 C CG1 . ILE   A 1 135 ? 7.736   -9.832  8.272   1.00 28.84 ? 134 ILE   A CG1 1 
ATOM   1024 C CG2 . ILE   A 1 135 ? 8.975   -7.779  7.393   1.00 28.39 ? 134 ILE   A CG2 1 
ATOM   1025 C CD1 . ILE   A 1 135 ? 6.683   -9.859  7.122   1.00 30.26 ? 134 ILE   A CD1 1 
ATOM   1026 N N   . HIS   A 1 136 ? 10.857  -6.634  10.046  1.00 27.55 ? 135 HIS   A N   1 
ATOM   1027 C CA  . HIS   A 1 136 ? 11.353  -5.303  10.400  1.00 26.96 ? 135 HIS   A CA  1 
ATOM   1028 C C   . HIS   A 1 136 ? 10.745  -4.248  9.445   1.00 27.99 ? 135 HIS   A C   1 
ATOM   1029 O O   . HIS   A 1 136 ? 10.069  -3.319  9.901   1.00 28.96 ? 135 HIS   A O   1 
ATOM   1030 C CB  . HIS   A 1 136 ? 12.899  -5.277  10.401  1.00 26.85 ? 135 HIS   A CB  1 
ATOM   1031 C CG  . HIS   A 1 136 ? 13.471  -4.042  11.029  1.00 29.19 ? 135 HIS   A CG  1 
ATOM   1032 N ND1 . HIS   A 1 136 ? 13.516  -2.833  10.341  1.00 30.52 ? 135 HIS   A ND1 1 
ATOM   1033 C CD2 . HIS   A 1 136 ? 13.931  -3.841  12.294  1.00 29.74 ? 135 HIS   A CD2 1 
ATOM   1034 C CE1 . HIS   A 1 136 ? 14.026  -1.954  11.196  1.00 31.07 ? 135 HIS   A CE1 1 
ATOM   1035 N NE2 . HIS   A 1 136 ? 14.329  -2.517  12.368  1.00 30.18 ? 135 HIS   A NE2 1 
ATOM   1036 N N   . ARG   A 1 137 ? 10.999  -4.376  8.114   1.00 26.45 ? 136 ARG   A N   1 
ATOM   1037 C CA  . ARG   A 1 137 ? 10.405  -3.514  7.085   1.00 25.89 ? 136 ARG   A CA  1 
ATOM   1038 C C   . ARG   A 1 137 ? 10.894  -2.052  7.123   1.00 26.87 ? 136 ARG   A C   1 
ATOM   1039 O O   . ARG   A 1 137 ? 10.333  -1.204  6.444   1.00 28.40 ? 136 ARG   A O   1 
ATOM   1040 C CB  . ARG   A 1 137 ? 8.879   -3.589  7.109   1.00 25.74 ? 136 ARG   A CB  1 
ATOM   1041 C CG  . ARG   A 1 137 ? 8.306   -4.433  5.984   1.00 27.58 ? 136 ARG   A CG  1 
ATOM   1042 C CD  . ARG   A 1 137 ? 8.156   -3.603  4.740   1.00 28.00 ? 136 ARG   A CD  1 
ATOM   1043 N NE  . ARG   A 1 137 ? 6.850   -2.935  4.731   1.00 30.61 ? 136 ARG   A NE  1 
ATOM   1044 C CZ  . ARG   A 1 137 ? 6.652   -1.624  4.816   1.00 32.63 ? 136 ARG   A CZ  1 
ATOM   1045 N NH1 . ARG   A 1 137 ? 7.685   -0.792  4.939   1.00 31.59 ? 136 ARG   A NH1 1 
ATOM   1046 N NH2 . ARG   A 1 137 ? 5.422   -1.132  4.789   1.00 30.83 ? 136 ARG   A NH2 1 
ATOM   1047 N N   . ASP   A 1 138 ? 12.003  -1.781  7.830   1.00 26.74 ? 137 ASP   A N   1 
ATOM   1048 C CA  . ASP   A 1 138 ? 12.542  -0.429  7.951   1.00 26.80 ? 137 ASP   A CA  1 
ATOM   1049 C C   . ASP   A 1 138 ? 14.076  -0.456  8.055   1.00 26.79 ? 137 ASP   A C   1 
ATOM   1050 O O   . ASP   A 1 138 ? 14.665  0.411   8.726   1.00 26.40 ? 137 ASP   A O   1 
ATOM   1051 C CB  . ASP   A 1 138 ? 11.951  0.216   9.196   1.00 29.14 ? 137 ASP   A CB  1 
ATOM   1052 C CG  . ASP   A 1 138 ? 11.982  1.720   9.193   1.00 34.55 ? 137 ASP   A CG  1 
ATOM   1053 O OD1 . ASP   A 1 138 ? 11.993  2.319   8.074   1.00 35.14 ? 137 ASP   A OD1 1 
ATOM   1054 O OD2 . ASP   A 1 138 ? 12.028  2.310   10.306  1.00 34.79 ? 137 ASP   A OD2 1 
ATOM   1055 N N   . ILE   A 1 139 ? 14.743  -1.448  7.380   1.00 25.55 ? 138 ILE   A N   1 
ATOM   1056 C CA  . ILE   A 1 139 ? 16.207  -1.557  7.392   1.00 26.18 ? 138 ILE   A CA  1 
ATOM   1057 C C   . ILE   A 1 139 ? 16.845  -0.551  6.434   1.00 25.63 ? 138 ILE   A C   1 
ATOM   1058 O O   . ILE   A 1 139 ? 16.520  -0.533  5.241   1.00 25.86 ? 138 ILE   A O   1 
ATOM   1059 C CB  . ILE   A 1 139 ? 16.681  -3.003  7.024   1.00 25.86 ? 138 ILE   A CB  1 
ATOM   1060 C CG1 . ILE   A 1 139 ? 16.062  -4.050  7.962   1.00 26.99 ? 138 ILE   A CG1 1 
ATOM   1061 C CG2 . ILE   A 1 139 ? 18.211  -3.076  6.959   1.00 25.14 ? 138 ILE   A CG2 1 
ATOM   1062 C CD1 . ILE   A 1 139 ? 16.514  -3.937  9.525   1.00 28.03 ? 138 ILE   A CD1 1 
ATOM   1063 N N   . LYS   A 1 140 ? 17.719  0.296   6.974   1.00 24.66 ? 139 LYS   A N   1 
ATOM   1064 C CA  . LYS   A 1 140 ? 18.485  1.344   6.266   1.00 24.08 ? 139 LYS   A CA  1 
ATOM   1065 C C   . LYS   A 1 140 ? 19.506  1.886   7.269   1.00 25.56 ? 139 LYS   A C   1 
ATOM   1066 O O   . LYS   A 1 140 ? 19.333  1.727   8.492   1.00 25.54 ? 139 LYS   A O   1 
ATOM   1067 C CB  . LYS   A 1 140 ? 17.599  2.482   5.742   1.00 25.66 ? 139 LYS   A CB  1 
ATOM   1068 C CG  . LYS   A 1 140 ? 16.977  3.326   6.848   1.00 26.40 ? 139 LYS   A CG  1 
ATOM   1069 C CD  . LYS   A 1 140 ? 15.765  4.121   6.361   1.00 30.97 ? 139 LYS   A CD  1 
ATOM   1070 C CE  . LYS   A 1 140 ? 16.028  4.883   5.115   1.00 35.69 ? 139 LYS   A CE  1 
ATOM   1071 N NZ  . LYS   A 1 140 ? 16.662  6.184   5.405   1.00 41.32 ? 139 LYS   A NZ  1 
ATOM   1072 N N   . GLY   A 1 141 ? 20.559  2.520   6.754   1.00 25.61 ? 140 GLY   A N   1 
ATOM   1073 C CA  . GLY   A 1 141 ? 21.623  3.056   7.586   1.00 27.64 ? 140 GLY   A CA  1 
ATOM   1074 C C   . GLY   A 1 141 ? 21.167  3.956   8.722   1.00 29.23 ? 140 GLY   A C   1 
ATOM   1075 O O   . GLY   A 1 141 ? 21.706  3.831   9.827   1.00 30.05 ? 140 GLY   A O   1 
ATOM   1076 N N   . ALA   A 1 142 ? 20.148  4.855   8.467   1.00 29.23 ? 141 ALA   A N   1 
ATOM   1077 C CA  . ALA   A 1 142 ? 19.640  5.778   9.486   1.00 29.88 ? 141 ALA   A CA  1 
ATOM   1078 C C   . ALA   A 1 142 ? 18.983  5.043   10.657  1.00 30.09 ? 141 ALA   A C   1 
ATOM   1079 O O   . ALA   A 1 142 ? 18.836  5.610   11.720  1.00 30.09 ? 141 ALA   A O   1 
ATOM   1080 C CB  . ALA   A 1 142 ? 18.651  6.771   8.868   1.00 30.43 ? 141 ALA   A CB  1 
ATOM   1081 N N   . ASN   A 1 143 ? 18.587  3.763   10.467  1.00 30.00 ? 142 ASN   A N   1 
ATOM   1082 C CA  . ASN   A 1 143 ? 17.910  3.005   11.509  1.00 29.58 ? 142 ASN   A CA  1 
ATOM   1083 C C   . ASN   A 1 143 ? 18.803  1.955   12.168  1.00 29.43 ? 142 ASN   A C   1 
ATOM   1084 O O   . ASN   A 1 143 ? 18.297  1.089   12.866  1.00 29.60 ? 142 ASN   A O   1 
ATOM   1085 C CB  . ASN   A 1 143 ? 16.629  2.389   10.933  1.00 29.18 ? 142 ASN   A CB  1 
ATOM   1086 C CG  . ASN   A 1 143 ? 15.698  3.454   10.391  1.00 30.00 ? 142 ASN   A CG  1 
ATOM   1087 O OD1 . ASN   A 1 143 ? 15.774  4.640   10.772  1.00 30.41 ? 142 ASN   A OD1 1 
ATOM   1088 N ND2 . ASN   A 1 143 ? 14.812  3.081   9.473   1.00 27.65 ? 142 ASN   A ND2 1 
ATOM   1089 N N   . ILE   A 1 144 ? 20.121  2.025   11.921  1.00 28.38 ? 143 ILE   A N   1 
ATOM   1090 C CA  . ILE   A 1 144 ? 21.098  1.165   12.532  1.00 29.15 ? 143 ILE   A CA  1 
ATOM   1091 C C   . ILE   A 1 144 ? 22.004  2.087   13.308  1.00 30.55 ? 143 ILE   A C   1 
ATOM   1092 O O   . ILE   A 1 144 ? 22.670  2.955   12.725  1.00 30.00 ? 143 ILE   A O   1 
ATOM   1093 C CB  . ILE   A 1 144 ? 21.878  0.330   11.481  1.00 29.38 ? 143 ILE   A CB  1 
ATOM   1094 C CG1 . ILE   A 1 144 ? 20.918  -0.603  10.696  1.00 29.48 ? 143 ILE   A CG1 1 
ATOM   1095 C CG2 . ILE   A 1 144 ? 23.030  -0.469  12.166  1.00 29.90 ? 143 ILE   A CG2 1 
ATOM   1096 C CD1 . ILE   A 1 144 ? 21.375  -0.907  9.305   1.00 30.80 ? 143 ILE   A CD1 1 
ATOM   1097 N N   . LEU   A 1 145 ? 22.012  1.923   14.631  1.00 31.34 ? 144 LEU   A N   1 
ATOM   1098 C CA  . LEU   A 1 145 ? 22.783  2.789   15.527  1.00 32.37 ? 144 LEU   A CA  1 
ATOM   1099 C C   . LEU   A 1 145 ? 24.071  2.126   16.005  1.00 32.90 ? 144 LEU   A C   1 
ATOM   1100 O O   . LEU   A 1 145 ? 24.162  0.900   16.071  1.00 31.56 ? 144 LEU   A O   1 
ATOM   1101 C CB  . LEU   A 1 145 ? 21.925  3.148   16.743  1.00 32.78 ? 144 LEU   A CB  1 
ATOM   1102 C CG  . LEU   A 1 145 ? 20.490  3.657   16.422  1.00 34.98 ? 144 LEU   A CG  1 
ATOM   1103 C CD1 . LEU   A 1 145 ? 19.719  3.928   17.685  1.00 34.92 ? 144 LEU   A CD1 1 
ATOM   1104 C CD2 . LEU   A 1 145 ? 20.510  4.874   15.468  1.00 35.12 ? 144 LEU   A CD2 1 
ATOM   1105 N N   . ILE   A 1 146 ? 25.048  2.962   16.389  1.00 33.93 ? 145 ILE   A N   1 
ATOM   1106 C CA  . ILE   A 1 146 ? 26.346  2.548   16.870  1.00 36.37 ? 145 ILE   A CA  1 
ATOM   1107 C C   . ILE   A 1 146 ? 26.606  3.191   18.219  1.00 38.41 ? 145 ILE   A C   1 
ATOM   1108 O O   . ILE   A 1 146 ? 26.441  4.397   18.332  1.00 38.85 ? 145 ILE   A O   1 
ATOM   1109 C CB  . ILE   A 1 146 ? 27.411  3.034   15.865  1.00 36.77 ? 145 ILE   A CB  1 
ATOM   1110 C CG1 . ILE   A 1 146 ? 27.139  2.534   14.419  1.00 37.64 ? 145 ILE   A CG1 1 
ATOM   1111 C CG2 . ILE   A 1 146 ? 28.813  2.682   16.344  1.00 36.94 ? 145 ILE   A CG2 1 
ATOM   1112 C CD1 . ILE   A 1 146 ? 27.348  1.055   14.184  1.00 38.96 ? 145 ILE   A CD1 1 
ATOM   1113 N N   . ASN   A 1 147 ? 27.008  2.416   19.237  1.00 39.89 ? 146 ASN   A N   1 
ATOM   1114 C CA  . ASN   A 1 147 ? 27.358  2.999   20.538  1.00 42.25 ? 146 ASN   A CA  1 
ATOM   1115 C C   . ASN   A 1 147 ? 28.869  3.308   20.557  1.00 45.19 ? 146 ASN   A C   1 
ATOM   1116 O O   . ASN   A 1 147 ? 29.589  2.916   19.619  1.00 45.84 ? 146 ASN   A O   1 
ATOM   1117 C CB  . ASN   A 1 147 ? 26.913  2.094   21.710  1.00 43.05 ? 146 ASN   A CB  1 
ATOM   1118 C CG  . ASN   A 1 147 ? 27.589  0.747   21.818  1.00 45.65 ? 146 ASN   A CG  1 
ATOM   1119 O OD1 . ASN   A 1 147 ? 28.590  0.448   21.141  1.00 45.97 ? 146 ASN   A OD1 1 
ATOM   1120 N ND2 . ASN   A 1 147 ? 27.077  -0.088  22.724  1.00 45.44 ? 146 ASN   A ND2 1 
ATOM   1121 N N   . ASP   A 1 148 ? 29.373  4.000   21.602  1.00 46.36 ? 147 ASP   A N   1 
ATOM   1122 C CA  . ASP   A 1 148 ? 30.788  4.355   21.645  1.00 48.19 ? 147 ASP   A CA  1 
ATOM   1123 C C   . ASP   A 1 148 ? 31.742  3.138   21.736  1.00 48.61 ? 147 ASP   A C   1 
ATOM   1124 O O   . ASP   A 1 148 ? 32.940  3.283   21.499  1.00 49.16 ? 147 ASP   A O   1 
ATOM   1125 C CB  . ASP   A 1 148 ? 31.058  5.393   22.747  1.00 52.13 ? 147 ASP   A CB  1 
ATOM   1126 C CG  . ASP   A 1 148 ? 30.448  6.765   22.422  1.00 59.61 ? 147 ASP   A CG  1 
ATOM   1127 O OD1 . ASP   A 1 148 ? 30.067  6.992   21.241  1.00 60.24 ? 147 ASP   A OD1 1 
ATOM   1128 O OD2 . ASP   A 1 148 ? 30.363  7.612   23.340  1.00 63.54 ? 147 ASP   A OD2 1 
ATOM   1129 N N   . ALA   A 1 149 ? 31.207  1.939   21.980  1.00 48.07 ? 148 ALA   A N   1 
ATOM   1130 C CA  . ALA   A 1 149 ? 32.009  0.714   22.003  1.00 47.73 ? 148 ALA   A CA  1 
ATOM   1131 C C   . ALA   A 1 149 ? 32.066  0.011   20.609  1.00 47.45 ? 148 ALA   A C   1 
ATOM   1132 O O   . ALA   A 1 149 ? 32.647  -1.074  20.511  1.00 48.36 ? 148 ALA   A O   1 
ATOM   1133 C CB  . ALA   A 1 149 ? 31.450  -0.246  23.035  1.00 47.71 ? 148 ALA   A CB  1 
ATOM   1134 N N   . GLY   A 1 150 ? 31.469  0.614   19.568  1.00 45.14 ? 149 GLY   A N   1 
ATOM   1135 C CA  . GLY   A 1 150 ? 31.476  0.038   18.229  1.00 43.68 ? 149 GLY   A CA  1 
ATOM   1136 C C   . GLY   A 1 150 ? 30.485  -1.093  18.008  1.00 42.27 ? 149 GLY   A C   1 
ATOM   1137 O O   . GLY   A 1 150 ? 30.554  -1.796  16.995  1.00 42.72 ? 149 GLY   A O   1 
ATOM   1138 N N   . GLU   A 1 151 ? 29.567  -1.300  18.962  1.00 40.26 ? 150 GLU   A N   1 
ATOM   1139 C CA  . GLU   A 1 151 ? 28.527  -2.301  18.828  1.00 38.88 ? 150 GLU   A CA  1 
ATOM   1140 C C   . GLU   A 1 151 ? 27.467  -1.836  17.853  1.00 37.33 ? 150 GLU   A C   1 
ATOM   1141 O O   . GLU   A 1 151 ? 27.255  -0.624  17.683  1.00 36.83 ? 150 GLU   A O   1 
ATOM   1142 C CB  . GLU   A 1 151 ? 27.927  -2.637  20.195  1.00 40.79 ? 150 GLU   A CB  1 
ATOM   1143 C CG  . GLU   A 1 151 ? 28.922  -3.409  21.041  1.00 45.62 ? 150 GLU   A CG  1 
ATOM   1144 C CD  . GLU   A 1 151 ? 28.549  -3.533  22.498  1.00 50.26 ? 150 GLU   A CD  1 
ATOM   1145 O OE1 . GLU   A 1 151 ? 27.965  -2.568  23.037  1.00 50.29 ? 150 GLU   A OE1 1 
ATOM   1146 O OE2 . GLU   A 1 151 ? 28.820  -4.600  23.096  1.00 54.60 ? 150 GLU   A OE2 1 
ATOM   1147 N N   . VAL   A 1 152 ? 26.806  -2.793  17.190  1.00 35.57 ? 151 VAL   A N   1 
ATOM   1148 C CA  . VAL   A 1 152 ? 25.795  -2.479  16.173  1.00 34.41 ? 151 VAL   A CA  1 
ATOM   1149 C C   . VAL   A 1 152 ? 24.414  -2.905  16.650  1.00 34.65 ? 151 VAL   A C   1 
ATOM   1150 O O   . VAL   A 1 152 ? 24.210  -4.064  17.055  1.00 33.97 ? 151 VAL   A O   1 
ATOM   1151 C CB  . VAL   A 1 152 ? 26.163  -3.159  14.821  1.00 33.88 ? 151 VAL   A CB  1 
ATOM   1152 C CG1 . VAL   A 1 152 ? 25.065  -3.000  13.773  1.00 33.52 ? 151 VAL   A CG1 1 
ATOM   1153 C CG2 . VAL   A 1 152 ? 27.482  -2.654  14.299  1.00 33.36 ? 151 VAL   A CG2 1 
ATOM   1154 N N   . ARG   A 1 153 ? 23.444  -1.957  16.618  1.00 34.67 ? 152 ARG   A N   1 
ATOM   1155 C CA  . ARG   A 1 153 ? 22.092  -2.282  17.062  1.00 35.36 ? 152 ARG   A CA  1 
ATOM   1156 C C   . ARG   A 1 153 ? 21.063  -1.670  16.164  1.00 34.12 ? 152 ARG   A C   1 
ATOM   1157 O O   . ARG   A 1 153 ? 21.172  -0.491  15.803  1.00 34.06 ? 152 ARG   A O   1 
ATOM   1158 C CB  . ARG   A 1 153 ? 21.828  -1.786  18.504  1.00 38.88 ? 152 ARG   A CB  1 
ATOM   1159 C CG  . ARG   A 1 153 ? 23.076  -1.709  19.382  1.00 45.23 ? 152 ARG   A CG  1 
ATOM   1160 C CD  . ARG   A 1 153 ? 22.852  -2.118  20.808  1.00 49.85 ? 152 ARG   A CD  1 
ATOM   1161 N NE  . ARG   A 1 153 ? 23.793  -3.161  21.184  1.00 55.49 ? 152 ARG   A NE  1 
ATOM   1162 C CZ  . ARG   A 1 153 ? 24.471  -3.196  22.325  1.00 61.94 ? 152 ARG   A CZ  1 
ATOM   1163 N NH1 . ARG   A 1 153 ? 24.319  -2.232  23.226  1.00 63.62 ? 152 ARG   A NH1 1 
ATOM   1164 N NH2 . ARG   A 1 153 ? 25.291  -4.206  22.587  1.00 62.58 ? 152 ARG   A NH2 1 
ATOM   1165 N N   . LEU   A 1 154 ? 19.997  -2.421  15.875  1.00 32.25 ? 153 LEU   A N   1 
ATOM   1166 C CA  . LEU   A 1 154 ? 18.859  -1.876  15.174  1.00 31.70 ? 153 LEU   A CA  1 
ATOM   1167 C C   . LEU   A 1 154 ? 18.157  -0.923  16.170  1.00 33.47 ? 153 LEU   A C   1 
ATOM   1168 O O   . LEU   A 1 154 ? 17.977  -1.294  17.331  1.00 33.55 ? 153 LEU   A O   1 
ATOM   1169 C CB  . LEU   A 1 154 ? 17.912  -3.017  14.776  1.00 31.60 ? 153 LEU   A CB  1 
ATOM   1170 C CG  . LEU   A 1 154 ? 18.481  -3.997  13.734  1.00 32.92 ? 153 LEU   A CG  1 
ATOM   1171 C CD1 . LEU   A 1 154 ? 17.541  -5.181  13.523  1.00 32.98 ? 153 LEU   A CD1 1 
ATOM   1172 C CD2 . LEU   A 1 154 ? 18.777  -3.269  12.414  1.00 33.04 ? 153 LEU   A CD2 1 
ATOM   1173 N N   . ALA   A 1 155 ? 17.801  0.303   15.736  1.00 34.27 ? 154 ALA   A N   1 
ATOM   1174 C CA  . ALA   A 1 155 ? 17.139  1.287   16.617  1.00 34.95 ? 154 ALA   A CA  1 
ATOM   1175 C C   . ALA   A 1 155 ? 15.876  0.740   17.260  1.00 35.69 ? 154 ALA   A C   1 
ATOM   1176 O O   . ALA   A 1 155 ? 15.575  1.035   18.423  1.00 36.21 ? 154 ALA   A O   1 
ATOM   1177 C CB  . ALA   A 1 155 ? 16.812  2.564   15.849  1.00 35.31 ? 154 ALA   A CB  1 
ATOM   1178 N N   . ASP   A 1 156 ? 15.133  -0.063  16.516  1.00 35.16 ? 155 ASP   A N   1 
ATOM   1179 C CA  . ASP   A 1 156 ? 13.904  -0.666  17.050  1.00 35.05 ? 155 ASP   A CA  1 
ATOM   1180 C C   . ASP   A 1 156 ? 13.629  -1.979  16.305  1.00 35.81 ? 155 ASP   A C   1 
ATOM   1181 O O   . ASP   A 1 156 ? 14.433  -2.359  15.431  1.00 34.94 ? 155 ASP   A O   1 
ATOM   1182 C CB  . ASP   A 1 156 ? 12.728  0.341   17.003  1.00 35.14 ? 155 ASP   A CB  1 
ATOM   1183 C CG  . ASP   A 1 156 ? 12.319  0.812   15.632  1.00 36.55 ? 155 ASP   A CG  1 
ATOM   1184 O OD1 . ASP   A 1 156 ? 12.621  0.120   14.649  1.00 37.48 ? 155 ASP   A OD1 1 
ATOM   1185 O OD2 . ASP   A 1 156 ? 11.706  1.867   15.539  1.00 39.18 ? 155 ASP   A OD2 1 
ATOM   1186 N N   . PHE   A 1 157 ? 12.523  -2.662  16.626  1.00 36.81 ? 156 PHE   A N   1 
ATOM   1187 C CA  . PHE   A 1 157 ? 12.232  -3.902  15.917  1.00 38.75 ? 156 PHE   A CA  1 
ATOM   1188 C C   . PHE   A 1 157 ? 11.446  -3.689  14.602  1.00 38.03 ? 156 PHE   A C   1 
ATOM   1189 O O   . PHE   A 1 157 ? 10.942  -4.651  14.034  1.00 38.34 ? 156 PHE   A O   1 
ATOM   1190 C CB  . PHE   A 1 157 ? 11.570  -4.941  16.829  1.00 39.87 ? 156 PHE   A CB  1 
ATOM   1191 C CG  . PHE   A 1 157 ? 10.289  -4.509  17.481  1.00 42.08 ? 156 PHE   A CG  1 
ATOM   1192 C CD1 . PHE   A 1 157 ? 9.227   -4.042  16.722  1.00 44.31 ? 156 PHE   A CD1 1 
ATOM   1193 C CD2 . PHE   A 1 157 ? 10.122  -4.616  18.850  1.00 43.56 ? 156 PHE   A CD2 1 
ATOM   1194 C CE1 . PHE   A 1 157 ? 8.035   -3.645  17.330  1.00 45.51 ? 156 PHE   A CE1 1 
ATOM   1195 C CE2 . PHE   A 1 157 ? 8.918   -4.265  19.446  1.00 45.75 ? 156 PHE   A CE2 1 
ATOM   1196 C CZ  . PHE   A 1 157 ? 7.879   -3.785  18.681  1.00 45.87 ? 156 PHE   A CZ  1 
ATOM   1197 N N   . GLY   A 1 158 ? 11.366  -2.463  14.127  1.00 37.55 ? 157 GLY   A N   1 
ATOM   1198 C CA  . GLY   A 1 158 ? 10.704  -2.160  12.872  1.00 37.57 ? 157 GLY   A CA  1 
ATOM   1199 C C   . GLY   A 1 158 ? 9.411   -1.388  12.987  1.00 38.48 ? 157 GLY   A C   1 
ATOM   1200 O O   . GLY   A 1 158 ? 9.100   -0.789  14.025  1.00 38.96 ? 157 GLY   A O   1 
ATOM   1201 N N   . ILE   A 1 159 ? 8.642   -1.424  11.907  1.00 38.73 ? 158 ILE   A N   1 
ATOM   1202 C CA  . ILE   A 1 159 ? 7.393   -0.691  11.809  1.00 41.00 ? 158 ILE   A CA  1 
ATOM   1203 C C   . ILE   A 1 159 ? 6.213   -1.326  12.525  1.00 43.65 ? 158 ILE   A C   1 
ATOM   1204 O O   . ILE   A 1 159 ? 5.198   -0.651  12.657  1.00 44.78 ? 158 ILE   A O   1 
ATOM   1205 C CB  . ILE   A 1 159 ? 7.043   -0.475  10.309  1.00 40.73 ? 158 ILE   A CB  1 
ATOM   1206 C CG1 . ILE   A 1 159 ? 6.672   -1.814  9.635   1.00 41.65 ? 158 ILE   A CG1 1 
ATOM   1207 C CG2 . ILE   A 1 159 ? 8.173   0.249   9.574   1.00 40.02 ? 158 ILE   A CG2 1 
ATOM   1208 C CD1 . ILE   A 1 159 ? 5.804   -1.735  8.367   1.00 43.05 ? 158 ILE   A CD1 1 
ATOM   1209 N N   . SER   A 1 160 ? 6.294   -2.602  12.935  1.00 45.13 ? 159 SER   A N   1 
ATOM   1210 C CA  . SER   A 1 160 ? 5.146   -3.325  13.506  1.00 47.82 ? 159 SER   A CA  1 
ATOM   1211 C C   . SER   A 1 160 ? 4.551   -2.799  14.824  1.00 51.19 ? 159 SER   A C   1 
ATOM   1212 O O   . SER   A 1 160 ? 3.518   -3.326  15.225  1.00 52.31 ? 159 SER   A O   1 
ATOM   1213 C CB  . SER   A 1 160 ? 5.438   -4.814  13.678  1.00 47.83 ? 159 SER   A CB  1 
ATOM   1214 O OG  . SER   A 1 160 ? 6.462   -5.044  14.632  1.00 49.39 ? 159 SER   A OG  1 
ATOM   1215 N N   . ALA   A 1 161 ? 5.183   -1.844  15.508  1.00 53.23 ? 160 ALA   A N   1 
ATOM   1216 C CA  . ALA   A 1 161 ? 4.622   -1.318  16.754  1.00 56.08 ? 160 ALA   A CA  1 
ATOM   1217 C C   . ALA   A 1 161 ? 3.337   -0.498  16.487  1.00 58.61 ? 160 ALA   A C   1 
ATOM   1218 O O   . ALA   A 1 161 ? 3.376   0.552   15.848  1.00 58.85 ? 160 ALA   A O   1 
ATOM   1219 C CB  . ALA   A 1 161 ? 5.651   -0.463  17.477  1.00 56.52 ? 160 ALA   A CB  1 
ATOM   1220 N N   . GLN   A 1 162 ? 2.208   -0.971  16.994  1.00 60.49 ? 161 GLN   A N   1 
ATOM   1221 C CA  . GLN   A 1 162 ? 0.927   -0.284  16.840  1.00 62.15 ? 161 GLN   A CA  1 
ATOM   1222 C C   . GLN   A 1 162 ? 0.783   0.833   17.891  1.00 63.43 ? 161 GLN   A C   1 
ATOM   1223 O O   . GLN   A 1 162 ? -0.103  0.775   18.749  1.00 63.36 ? 161 GLN   A O   1 
ATOM   1224 C CB  . GLN   A 1 162 ? -0.226  -1.289  16.936  1.00 64.46 ? 161 GLN   A CB  1 
ATOM   1225 C CG  . GLN   A 1 162 ? -0.079  -2.515  16.027  1.00 68.98 ? 161 GLN   A CG  1 
ATOM   1226 C CD  . GLN   A 1 162 ? -1.041  -3.634  16.407  1.00 75.63 ? 161 GLN   A CD  1 
ATOM   1227 O OE1 . GLN   A 1 162 ? -1.587  -3.678  17.521  1.00 78.49 ? 161 GLN   A OE1 1 
ATOM   1228 N NE2 . GLN   A 1 162 ? -1.264  -4.583  15.501  1.00 75.95 ? 161 GLN   A NE2 1 
ATOM   1229 N N   . ILE   A 1 163 ? 1.681   1.840   17.836  1.00 64.15 ? 162 ILE   A N   1 
ATOM   1230 C CA  . ILE   A 1 163 ? 1.701   2.991   18.755  1.00 64.92 ? 162 ILE   A CA  1 
ATOM   1231 C C   . ILE   A 1 163 ? 1.895   4.270   17.945  1.00 65.13 ? 162 ILE   A C   1 
ATOM   1232 O O   . ILE   A 1 163 ? 2.720   4.301   17.035  1.00 66.01 ? 162 ILE   A O   1 
ATOM   1233 C CB  . ILE   A 1 163 ? 2.834   2.863   19.825  1.00 65.68 ? 162 ILE   A CB  1 
ATOM   1234 C CG1 . ILE   A 1 163 ? 4.177   2.473   19.174  1.00 66.93 ? 162 ILE   A CG1 1 
ATOM   1235 C CG2 . ILE   A 1 163 ? 2.455   1.882   20.934  1.00 66.24 ? 162 ILE   A CG2 1 
ATOM   1236 C CD1 . ILE   A 1 163 ? 5.426   2.729   20.024  1.00 68.30 ? 162 ILE   A CD1 1 
ATOM   1237 N N   . GLY   A 1 164 ? 1.157   5.313   18.285  1.00 64.39 ? 163 GLY   A N   1 
ATOM   1238 C CA  . GLY   A 1 164 ? 1.270   6.594   17.606  1.00 63.90 ? 163 GLY   A CA  1 
ATOM   1239 C C   . GLY   A 1 164 ? 1.035   6.592   16.106  1.00 63.01 ? 163 GLY   A C   1 
ATOM   1240 O O   . GLY   A 1 164 ? 0.009   6.103   15.622  1.00 63.48 ? 163 GLY   A O   1 
ATOM   1241 N N   . ALA   A 1 165 ? 1.988   7.164   15.358  1.00 61.48 ? 164 ALA   A N   1 
ATOM   1242 C CA  . ALA   A 1 165 ? 1.901   7.300   13.904  1.00 59.92 ? 164 ALA   A CA  1 
ATOM   1243 C C   . ALA   A 1 165 ? 2.256   6.014   13.135  1.00 56.66 ? 164 ALA   A C   1 
ATOM   1244 O O   . ALA   A 1 165 ? 3.061   6.046   12.206  1.00 56.71 ? 164 ALA   A O   1 
ATOM   1245 C CB  . ALA   A 1 165 ? 2.769   8.469   13.438  1.00 60.60 ? 164 ALA   A CB  1 
ATOM   1246 N N   . GLU   A 1 166 ? 1.624   4.895   13.494  1.00 53.63 ? 165 GLU   A N   1 
ATOM   1247 C CA  . GLU   A 1 166 ? 1.879   3.621   12.831  1.00 51.14 ? 165 GLU   A CA  1 
ATOM   1248 C C   . GLU   A 1 166 ? 1.608   3.675   11.321  1.00 48.31 ? 165 GLU   A C   1 
ATOM   1249 O O   . GLU   A 1 166 ? 2.385   3.114   10.566  1.00 48.08 ? 165 GLU   A O   1 
ATOM   1250 C CB  . GLU   A 1 166 ? 1.061   2.493   13.495  1.00 52.56 ? 165 GLU   A CB  1 
ATOM   1251 C CG  . GLU   A 1 166 ? 1.316   1.099   12.933  1.00 55.21 ? 165 GLU   A CG  1 
ATOM   1252 C CD  . GLU   A 1 166 ? 0.524   0.740   11.687  1.00 56.06 ? 165 GLU   A CD  1 
ATOM   1253 O OE1 . GLU   A 1 166 ? -0.615  1.246   11.549  1.00 53.36 ? 165 GLU   A OE1 1 
ATOM   1254 O OE2 . GLU   A 1 166 ? 1.061   0.005   10.824  1.00 54.75 ? 165 GLU   A OE2 1 
ATOM   1255 N N   . LEU   A 1 167 ? 0.498   4.317   10.878  1.00 46.04 ? 166 LEU   A N   1 
ATOM   1256 C CA  . LEU   A 1 167 ? 0.168   4.335   9.454   1.00 44.48 ? 166 LEU   A CA  1 
ATOM   1257 C C   . LEU   A 1 167 ? 1.189   5.107   8.604   1.00 42.95 ? 166 LEU   A C   1 
ATOM   1258 O O   . LEU   A 1 167 ? 1.629   4.622   7.552   1.00 41.98 ? 166 LEU   A O   1 
ATOM   1259 C CB  . LEU   A 1 167 ? -1.273  4.855   9.220   1.00 45.16 ? 166 LEU   A CB  1 
ATOM   1260 C CG  . LEU   A 1 167 ? -1.730  4.715   7.771   1.00 47.71 ? 166 LEU   A CG  1 
ATOM   1261 C CD1 . LEU   A 1 167 ? -1.765  3.242   7.326   1.00 48.62 ? 166 LEU   A CD1 1 
ATOM   1262 C CD2 . LEU   A 1 167 ? -3.025  5.438   7.510   1.00 48.59 ? 166 LEU   A CD2 1 
ATOM   1263 N N   . ALA   A 1 168 ? 1.570   6.305   9.047   1.00 42.48 ? 167 ALA   A N   1 
ATOM   1264 C CA  . ALA   A 1 168 ? 2.549   7.119   8.308   1.00 41.68 ? 167 ALA   A CA  1 
ATOM   1265 C C   . ALA   A 1 168 ? 3.915   6.424   8.243   1.00 40.24 ? 167 ALA   A C   1 
ATOM   1266 O O   . ALA   A 1 168 ? 4.625   6.517   7.241   1.00 40.18 ? 167 ALA   A O   1 
ATOM   1267 C CB  . ALA   A 1 168 ? 2.673   8.495   8.955   1.00 42.38 ? 167 ALA   A CB  1 
ATOM   1268 N N   . ARG   A 1 169 ? 4.280   5.716   9.306   1.00 38.72 ? 168 ARG   A N   1 
ATOM   1269 C CA  . ARG   A 1 169 ? 5.513   4.971   9.357   1.00 38.87 ? 168 ARG   A CA  1 
ATOM   1270 C C   . ARG   A 1 169 ? 5.424   3.758   8.404   1.00 37.55 ? 168 ARG   A C   1 
ATOM   1271 O O   . ARG   A 1 169 ? 6.370   3.450   7.698   1.00 38.13 ? 168 ARG   A O   1 
ATOM   1272 C CB  . ARG   A 1 169 ? 5.763   4.556   10.812  1.00 40.55 ? 168 ARG   A CB  1 
ATOM   1273 C CG  . ARG   A 1 169 ? 6.838   3.549   10.965  1.00 44.37 ? 168 ARG   A CG  1 
ATOM   1274 C CD  . ARG   A 1 169 ? 7.509   3.679   12.291  1.00 45.98 ? 168 ARG   A CD  1 
ATOM   1275 N NE  . ARG   A 1 169 ? 8.844   3.122   12.168  1.00 46.43 ? 168 ARG   A NE  1 
ATOM   1276 C CZ  . ARG   A 1 169 ? 9.532   2.590   13.165  1.00 46.60 ? 168 ARG   A CZ  1 
ATOM   1277 N NH1 . ARG   A 1 169 ? 9.015   2.543   14.391  1.00 45.52 ? 168 ARG   A NH1 1 
ATOM   1278 N NH2 . ARG   A 1 169 ? 10.744  2.102   12.949  1.00 46.09 ? 168 ARG   A NH2 1 
ATOM   1279 N N   . ARG   A 1 170 ? 4.269   3.090   8.363   1.00 35.98 ? 169 ARG   A N   1 
ATOM   1280 C CA  . ARG   A 1 170 ? 4.065   1.931   7.502   1.00 34.71 ? 169 ARG   A CA  1 
ATOM   1281 C C   . ARG   A 1 170 ? 4.119   2.333   6.006   1.00 34.55 ? 169 ARG   A C   1 
ATOM   1282 O O   . ARG   A 1 170 ? 4.598   1.578   5.159   1.00 33.67 ? 169 ARG   A O   1 
ATOM   1283 C CB  . ARG   A 1 170 ? 2.685   1.333   7.822   1.00 35.68 ? 169 ARG   A CB  1 
ATOM   1284 C CG  . ARG   A 1 170 ? 2.461   -0.026  7.223   1.00 37.64 ? 169 ARG   A CG  1 
ATOM   1285 C CD  . ARG   A 1 170 ? 1.002   -0.248  6.908   1.00 40.54 ? 169 ARG   A CD  1 
ATOM   1286 N NE  . ARG   A 1 170 ? 0.128   -0.168  8.086   1.00 42.23 ? 169 ARG   A NE  1 
ATOM   1287 C CZ  . ARG   A 1 170 ? -1.193  -0.292  8.046   1.00 45.03 ? 169 ARG   A CZ  1 
ATOM   1288 N NH1 . ARG   A 1 170 ? -1.909  -0.204  9.161   1.00 43.99 ? 169 ARG   A NH1 1 
ATOM   1289 N NH2 . ARG   A 1 170 ? -1.817  -0.472  6.884   1.00 43.82 ? 169 ARG   A NH2 1 
ATOM   1290 N N   . LEU   A 1 171 ? 3.577   3.519   5.691   1.00 35.19 ? 170 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 171 ? 3.483   4.014   4.322   1.00 35.93 ? 170 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 171 ? 4.596   4.945   3.881   1.00 35.81 ? 170 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 171 ? 4.608   5.381   2.724   1.00 36.33 ? 170 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 171 ? 2.150   4.748   4.151   1.00 36.31 ? 170 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 171 ? 0.897   3.926   4.236   1.00 38.51 ? 170 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 171 ? -0.312  4.796   3.955   1.00 39.34 ? 170 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 171 ? 0.939   2.743   3.257   1.00 38.94 ? 170 LEU   A CD2 1 
ATOM   1298 N N   . GLU   A 1 172 ? 5.493   5.296   4.788   1.00 34.77 ? 171 GLU   A N   1 
ATOM   1299 C CA  . GLU   A 1 172 ? 6.583   6.230   4.504   1.00 34.39 ? 171 GLU   A CA  1 
ATOM   1300 C C   . GLU   A 1 172 ? 7.436   5.826   3.276   1.00 33.09 ? 171 GLU   A C   1 
ATOM   1301 O O   . GLU   A 1 172 ? 7.873   6.699   2.534   1.00 33.04 ? 171 GLU   A O   1 
ATOM   1302 C CB  . GLU   A 1 172 ? 7.481   6.376   5.740   1.00 35.15 ? 171 GLU   A CB  1 
ATOM   1303 C CG  . GLU   A 1 172 ? 8.466   7.532   5.634   1.00 40.69 ? 171 GLU   A CG  1 
ATOM   1304 C CD  . GLU   A 1 172 ? 9.311   7.729   6.878   1.00 47.92 ? 171 GLU   A CD  1 
ATOM   1305 O OE1 . GLU   A 1 172 ? 9.868   8.840   7.041   1.00 49.21 ? 171 GLU   A OE1 1 
ATOM   1306 O OE2 . GLU   A 1 172 ? 9.423   6.778   7.688   1.00 47.46 ? 171 GLU   A OE2 1 
ATOM   1307 N N   . PHE   A 1 173 ? 7.682   4.515   3.067   1.00 30.92 ? 172 PHE   A N   1 
ATOM   1308 C CA  . PHE   A 1 173 ? 8.493   4.062   1.944   1.00 29.81 ? 172 PHE   A CA  1 
ATOM   1309 C C   . PHE   A 1 173 ? 7.933   4.523   0.596   1.00 31.49 ? 172 PHE   A C   1 
ATOM   1310 O O   . PHE   A 1 173 ? 8.691   4.634   -0.337  1.00 32.71 ? 172 PHE   A O   1 
ATOM   1311 C CB  . PHE   A 1 173 ? 8.692   2.521   1.962   1.00 28.73 ? 172 PHE   A CB  1 
ATOM   1312 C CG  . PHE   A 1 173 ? 7.495   1.744   1.443   1.00 29.56 ? 172 PHE   A CG  1 
ATOM   1313 C CD1 . PHE   A 1 173 ? 6.408   1.491   2.260   1.00 30.59 ? 172 PHE   A CD1 1 
ATOM   1314 C CD2 . PHE   A 1 173 ? 7.416   1.361   0.111   1.00 30.21 ? 172 PHE   A CD2 1 
ATOM   1315 C CE1 . PHE   A 1 173 ? 5.276   0.831   1.769   1.00 30.80 ? 172 PHE   A CE1 1 
ATOM   1316 C CE2 . PHE   A 1 173 ? 6.280   0.691   -0.375  1.00 31.33 ? 172 PHE   A CE2 1 
ATOM   1317 C CZ  . PHE   A 1 173 ? 5.241   0.414   0.466   1.00 30.79 ? 172 PHE   A CZ  1 
ATOM   1318 N N   . ILE   A 1 174 ? 6.630   4.780   0.466   1.00 32.11 ? 173 ILE   A N   1 
ATOM   1319 C CA  . ILE   A 1 174 ? 6.053   5.229   -0.801  1.00 33.93 ? 173 ILE   A CA  1 
ATOM   1320 C C   . ILE   A 1 174 ? 6.750   6.536   -1.304  1.00 35.82 ? 173 ILE   A C   1 
ATOM   1321 O O   . ILE   A 1 174 ? 6.956   6.709   -2.514  1.00 37.11 ? 173 ILE   A O   1 
ATOM   1322 C CB  . ILE   A 1 174 ? 4.546   5.383   -0.597  1.00 34.13 ? 173 ILE   A CB  1 
ATOM   1323 C CG1 . ILE   A 1 174 ? 3.900   4.006   -0.433  1.00 33.90 ? 173 ILE   A CG1 1 
ATOM   1324 C CG2 . ILE   A 1 174 ? 3.884   6.198   -1.714  1.00 36.73 ? 173 ILE   A CG2 1 
ATOM   1325 C CD1 . ILE   A 1 174 ? 2.292   4.067   -0.195  1.00 33.97 ? 173 ILE   A CD1 1 
ATOM   1326 N N   . GLY   A 1 175 ? 7.142   7.398   -0.357  1.00 34.40 ? 174 GLY   A N   1 
ATOM   1327 C CA  . GLY   A 1 175 ? 7.859   8.636   -0.662  1.00 34.24 ? 174 GLY   A CA  1 
ATOM   1328 C C   . GLY   A 1 175 ? 9.371   8.444   -0.675  1.00 33.44 ? 174 GLY   A C   1 
ATOM   1329 O O   . GLY   A 1 175 ? 10.095  9.328   -1.104  1.00 33.93 ? 174 GLY   A O   1 
ATOM   1330 N N   . THR   A 1 176 ? 9.874   7.309   -0.183  1.00 33.67 ? 175 THR   A N   1 
ATOM   1331 C CA  . THR   A 1 176 ? 11.317  7.008   -0.136  1.00 33.53 ? 175 THR   A CA  1 
ATOM   1332 C C   . THR   A 1 176 ? 11.481  5.466   -0.202  1.00 31.86 ? 175 THR   A C   1 
ATOM   1333 O O   . THR   A 1 176 ? 11.735  4.820   0.808   1.00 31.53 ? 175 THR   A O   1 
ATOM   1334 C CB  . THR   A 1 176 ? 11.951  7.679   1.107   1.00 37.02 ? 175 THR   A CB  1 
ATOM   1335 O OG1 . THR   A 1 176 ? 13.295  7.219   1.254   1.00 38.94 ? 175 THR   A OG1 1 
ATOM   1336 C CG2 . THR   A 1 176 ? 11.158  7.456   2.392   1.00 36.86 ? 175 THR   A CG2 1 
ATOM   1337 N N   . PRO   A 1 177 ? 11.199  4.874   -1.397  1.00 30.58 ? 176 PRO   A N   1 
ATOM   1338 C CA  . PRO   A 1 177 ? 11.140  3.399   -1.516  1.00 29.30 ? 176 PRO   A CA  1 
ATOM   1339 C C   . PRO   A 1 177 ? 12.441  2.691   -1.771  1.00 27.95 ? 176 PRO   A C   1 
ATOM   1340 O O   . PRO   A 1 177 ? 12.448  1.489   -2.015  1.00 28.85 ? 176 PRO   A O   1 
ATOM   1341 C CB  . PRO   A 1 177 ? 10.269  3.204   -2.758  1.00 30.14 ? 176 PRO   A CB  1 
ATOM   1342 C CG  . PRO   A 1 177 ? 10.649  4.392   -3.640  1.00 31.88 ? 176 PRO   A CG  1 
ATOM   1343 C CD  . PRO   A 1 177 ? 10.847  5.540   -2.673  1.00 30.20 ? 176 PRO   A CD  1 
ATOM   1344 N N   . TYR   A 1 178 ? 13.531  3.426   -1.734  1.00 26.05 ? 177 TYR   A N   1 
ATOM   1345 C CA  . TYR   A 1 178 ? 14.852  2.972   -2.169  1.00 26.23 ? 177 TYR   A CA  1 
ATOM   1346 C C   . TYR   A 1 178 ? 15.369  1.699   -1.511  1.00 26.36 ? 177 TYR   A C   1 
ATOM   1347 O O   . TYR   A 1 178 ? 16.137  0.968   -2.127  1.00 26.36 ? 177 TYR   A O   1 
ATOM   1348 C CB  . TYR   A 1 178 ? 15.874  4.114   -2.012  1.00 26.06 ? 177 TYR   A CB  1 
ATOM   1349 C CG  . TYR   A 1 178 ? 15.363  5.407   -2.630  1.00 25.52 ? 177 TYR   A CG  1 
ATOM   1350 C CD1 . TYR   A 1 178 ? 15.328  5.576   -4.010  1.00 26.11 ? 177 TYR   A CD1 1 
ATOM   1351 C CD2 . TYR   A 1 178 ? 14.825  6.413   -1.844  1.00 26.23 ? 177 TYR   A CD2 1 
ATOM   1352 C CE1 . TYR   A 1 178 ? 14.797  6.719   -4.584  1.00 25.72 ? 177 TYR   A CE1 1 
ATOM   1353 C CE2 . TYR   A 1 178 ? 14.327  7.585   -2.409  1.00 24.89 ? 177 TYR   A CE2 1 
ATOM   1354 C CZ  . TYR   A 1 178 ? 14.304  7.723   -3.783  1.00 25.70 ? 177 TYR   A CZ  1 
ATOM   1355 O OH  . TYR   A 1 178 ? 13.815  8.857   -4.375  1.00 28.34 ? 177 TYR   A OH  1 
ATOM   1356 N N   . TRP   A 1 179 ? 14.985  1.459   -0.268  1.00 25.55 ? 178 TRP   A N   1 
ATOM   1357 C CA  . TRP   A 1 179 ? 15.459  0.299   0.461   1.00 25.62 ? 178 TRP   A CA  1 
ATOM   1358 C C   . TRP   A 1 179 ? 14.466  -0.888  0.425   1.00 26.69 ? 178 TRP   A C   1 
ATOM   1359 O O   . TRP   A 1 179 ? 14.769  -1.935  0.998   1.00 27.33 ? 178 TRP   A O   1 
ATOM   1360 C CB  . TRP   A 1 179 ? 15.690  0.705   1.918   1.00 24.46 ? 178 TRP   A CB  1 
ATOM   1361 C CG  . TRP   A 1 179 ? 16.896  1.568   2.121   1.00 23.86 ? 178 TRP   A CG  1 
ATOM   1362 C CD1 . TRP   A 1 179 ? 18.127  1.151   2.513   1.00 24.64 ? 178 TRP   A CD1 1 
ATOM   1363 C CD2 . TRP   A 1 179 ? 16.965  3.012   2.029   1.00 23.27 ? 178 TRP   A CD2 1 
ATOM   1364 N NE1 . TRP   A 1 179 ? 18.981  2.242   2.623   1.00 24.56 ? 178 TRP   A NE1 1 
ATOM   1365 C CE2 . TRP   A 1 179 ? 18.288  3.388   2.337   1.00 24.11 ? 178 TRP   A CE2 1 
ATOM   1366 C CE3 . TRP   A 1 179 ? 16.056  4.015   1.648   1.00 24.27 ? 178 TRP   A CE3 1 
ATOM   1367 C CZ2 . TRP   A 1 179 ? 18.703  4.724   2.364   1.00 24.89 ? 178 TRP   A CZ2 1 
ATOM   1368 C CZ3 . TRP   A 1 179 ? 16.465  5.352   1.696   1.00 24.95 ? 178 TRP   A CZ3 1 
ATOM   1369 C CH2 . TRP   A 1 179 ? 17.785  5.686   2.007   1.00 24.84 ? 178 TRP   A CH2 1 
ATOM   1370 N N   . MET   A 1 180 ? 13.265  -0.707  -0.136  1.00 26.71 ? 179 MET   A N   1 
ATOM   1371 C CA  . MET   A 1 180 ? 12.261  -1.770  -0.119  1.00 26.17 ? 179 MET   A CA  1 
ATOM   1372 C C   . MET   A 1 180 ? 12.405  -2.784  -1.249  1.00 27.38 ? 179 MET   A C   1 
ATOM   1373 O O   . MET   A 1 180 ? 12.799  -2.437  -2.369  1.00 27.71 ? 179 MET   A O   1 
ATOM   1374 C CB  . MET   A 1 180 ? 10.831  -1.175  -0.063  1.00 25.78 ? 179 MET   A CB  1 
ATOM   1375 C CG  . MET   A 1 180 ? 10.549  -0.453  1.276   1.00 29.15 ? 179 MET   A CG  1 
ATOM   1376 S SD  . MET   A 1 180 ? 10.723  -1.523  2.756   1.00 31.67 ? 179 MET   A SD  1 
ATOM   1377 C CE  . MET   A 1 180 ? 12.326  -0.896  3.477   1.00 29.75 ? 179 MET   A CE  1 
ATOM   1378 N N   . ALA   A 1 181 ? 12.026  -4.035  -0.959  1.00 27.17 ? 180 ALA   A N   1 
ATOM   1379 C CA  . ALA   A 1 181 ? 12.115  -5.126  -1.932  1.00 27.64 ? 180 ALA   A CA  1 
ATOM   1380 C C   . ALA   A 1 181 ? 11.054  -4.936  -2.997  1.00 27.91 ? 180 ALA   A C   1 
ATOM   1381 O O   . ALA   A 1 181 ? 10.032  -4.310  -2.708  1.00 26.47 ? 180 ALA   A O   1 
ATOM   1382 C CB  . ALA   A 1 181 ? 11.908  -6.464  -1.223  1.00 27.38 ? 180 ALA   A CB  1 
ATOM   1383 N N   . PRO   A 1 182 ? 11.224  -5.489  -4.221  1.00 28.73 ? 181 PRO   A N   1 
ATOM   1384 C CA  . PRO   A 1 182 ? 10.195  -5.264  -5.264  1.00 29.13 ? 181 PRO   A CA  1 
ATOM   1385 C C   . PRO   A 1 182 ? 8.817   -5.749  -4.845  1.00 29.16 ? 181 PRO   A C   1 
ATOM   1386 O O   . PRO   A 1 182 ? 7.831   -5.124  -5.211  1.00 30.78 ? 181 PRO   A O   1 
ATOM   1387 C CB  . PRO   A 1 182 ? 10.690  -6.120  -6.471  1.00 29.90 ? 181 PRO   A CB  1 
ATOM   1388 C CG  . PRO   A 1 182 ? 12.177  -6.299  -6.246  1.00 30.84 ? 181 PRO   A CG  1 
ATOM   1389 C CD  . PRO   A 1 182 ? 12.371  -6.272  -4.731  1.00 28.83 ? 181 PRO   A CD  1 
ATOM   1390 N N   . GLU   A 1 183 ? 8.728   -6.866  -4.096  1.00 28.66 ? 182 GLU   A N   1 
ATOM   1391 C CA  . GLU   A 1 183 ? 7.388   -7.384  -3.695  1.00 29.14 ? 182 GLU   A CA  1 
ATOM   1392 C C   . GLU   A 1 183 ? 6.702   -6.423  -2.693  1.00 29.45 ? 182 GLU   A C   1 
ATOM   1393 O O   . GLU   A 1 183 ? 5.478   -6.370  -2.666  1.00 30.35 ? 182 GLU   A O   1 
ATOM   1394 C CB  . GLU   A 1 183 ? 7.469   -8.834  -3.156  1.00 28.77 ? 182 GLU   A CB  1 
ATOM   1395 C CG  . GLU   A 1 183 ? 8.237   -8.910  -1.842  1.00 27.82 ? 182 GLU   A CG  1 
ATOM   1396 C CD  . GLU   A 1 183 ? 9.744   -9.107  -1.939  1.00 28.88 ? 182 GLU   A CD  1 
ATOM   1397 O OE1 . GLU   A 1 183 ? 10.327  -8.862  -3.022  1.00 25.21 ? 182 GLU   A OE1 1 
ATOM   1398 O OE2 . GLU   A 1 183 ? 10.347  -9.463  -0.904  1.00 28.43 ? 182 GLU   A OE2 1 
ATOM   1399 N N   . VAL   A 1 184 ? 7.469   -5.604  -1.961  1.00 28.85 ? 183 VAL   A N   1 
ATOM   1400 C CA  . VAL   A 1 184 ? 6.939   -4.567  -1.043  1.00 29.32 ? 183 VAL   A CA  1 
ATOM   1401 C C   . VAL   A 1 184 ? 6.581   -3.311  -1.865  1.00 30.38 ? 183 VAL   A C   1 
ATOM   1402 O O   . VAL   A 1 184 ? 5.502   -2.723  -1.692  1.00 30.66 ? 183 VAL   A O   1 
ATOM   1403 C CB  . VAL   A 1 184 ? 7.989   -4.212  0.035   1.00 29.15 ? 183 VAL   A CB  1 
ATOM   1404 C CG1 . VAL   A 1 184 ? 7.518   -3.040  0.884   1.00 30.53 ? 183 VAL   A CG1 1 
ATOM   1405 C CG2 . VAL   A 1 184 ? 8.311   -5.417  0.908   1.00 29.14 ? 183 VAL   A CG2 1 
ATOM   1406 N N   . ALA   A 1 185 ? 7.486   -2.885  -2.776  1.00 30.52 ? 184 ALA   A N   1 
ATOM   1407 C CA  . ALA   A 1 185 ? 7.248   -1.769  -3.711  1.00 30.79 ? 184 ALA   A CA  1 
ATOM   1408 C C   . ALA   A 1 185 ? 5.963   -1.994  -4.558  1.00 31.45 ? 184 ALA   A C   1 
ATOM   1409 O O   . ALA   A 1 185 ? 5.339   -1.022  -5.012  1.00 32.29 ? 184 ALA   A O   1 
ATOM   1410 C CB  . ALA   A 1 185 ? 8.466   -1.593  -4.609  1.00 30.73 ? 184 ALA   A CB  1 
ATOM   1411 N N   . ALA   A 1 186 ? 5.493   -3.266  -4.666  1.00 30.55 ? 185 ALA   A N   1 
ATOM   1412 C CA  . ALA   A 1 186 ? 4.214   -3.618  -5.345  1.00 31.28 ? 185 ALA   A CA  1 
ATOM   1413 C C   . ALA   A 1 186 ? 3.037   -3.380  -4.351  1.00 32.83 ? 185 ALA   A C   1 
ATOM   1414 O O   . ALA   A 1 186 ? 2.103   -4.188  -4.235  1.00 31.82 ? 185 ALA   A O   1 
ATOM   1415 C CB  . ALA   A 1 186 ? 4.241   -5.077  -5.810  1.00 30.64 ? 185 ALA   A CB  1 
ATOM   1416 N N   . VAL   A 1 187 ? 3.111   -2.233  -3.628  1.00 34.06 ? 186 VAL   A N   1 
ATOM   1417 C CA  . VAL   A 1 187 ? 2.145   -1.807  -2.619  1.00 34.46 ? 186 VAL   A CA  1 
ATOM   1418 C C   . VAL   A 1 187 ? 0.747   -1.703  -3.217  1.00 33.87 ? 186 VAL   A C   1 
ATOM   1419 O O   . VAL   A 1 187 ? 0.557   -1.261  -4.353  1.00 34.11 ? 186 VAL   A O   1 
ATOM   1420 C CB  . VAL   A 1 187 ? 2.598   -0.479  -1.966  1.00 35.82 ? 186 VAL   A CB  1 
ATOM   1421 C CG1 . VAL   A 1 187 ? 2.732   0.617   -3.007  1.00 36.97 ? 186 VAL   A CG1 1 
ATOM   1422 C CG2 . VAL   A 1 187 ? 1.679   -0.059  -0.826  1.00 36.23 ? 186 VAL   A CG2 1 
ATOM   1423 N N   . ALA   A 1 188 ? -0.224  -2.195  -2.469  1.00 33.43 ? 187 ALA   A N   1 
ATOM   1424 C CA  . ALA   A 1 188 ? -1.641  -2.207  -2.841  1.00 33.94 ? 187 ALA   A CA  1 
ATOM   1425 C C   . ALA   A 1 188 ? -1.958  -3.112  -4.023  1.00 35.27 ? 187 ALA   A C   1 
ATOM   1426 O O   . ALA   A 1 188 ? -3.064  -3.056  -4.546  1.00 36.33 ? 187 ALA   A O   1 
ATOM   1427 C CB  . ALA   A 1 188 ? -2.178  -0.798  -3.056  1.00 34.65 ? 187 ALA   A CB  1 
ATOM   1428 N N   . LEU   A 1 189 ? -1.039  -4.024  -4.387  1.00 35.73 ? 188 LEU   A N   1 
ATOM   1429 C CA  . LEU   A 1 189 ? -1.341  -5.055  -5.391  1.00 36.51 ? 188 LEU   A CA  1 
ATOM   1430 C C   . LEU   A 1 189 ? -1.608  -6.371  -4.629  1.00 36.49 ? 188 LEU   A C   1 
ATOM   1431 O O   . LEU   A 1 189 ? -1.272  -6.482  -3.446  1.00 36.24 ? 188 LEU   A O   1 
ATOM   1432 C CB  . LEU   A 1 189 ? -0.206  -5.192  -6.431  1.00 36.95 ? 188 LEU   A CB  1 
ATOM   1433 C CG  . LEU   A 1 189 ? -0.032  -4.011  -7.389  1.00 37.70 ? 188 LEU   A CG  1 
ATOM   1434 C CD1 . LEU   A 1 189 ? 1.156   -4.233  -8.362  1.00 37.85 ? 188 LEU   A CD1 1 
ATOM   1435 C CD2 . LEU   A 1 189 ? -1.334  -3.707  -8.156  1.00 37.23 ? 188 LEU   A CD2 1 
ATOM   1436 N N   . LYS   A 1 190 ? -2.170  -7.376  -5.296  1.00 36.59 ? 189 LYS   A N   1 
ATOM   1437 C CA  . LYS   A 1 190 ? -2.559  -8.618  -4.652  1.00 37.53 ? 189 LYS   A CA  1 
ATOM   1438 C C   . LYS   A 1 190 ? -1.459  -9.428  -3.933  1.00 37.97 ? 189 LYS   A C   1 
ATOM   1439 O O   . LYS   A 1 190 ? -1.786  -10.187 -3.016  1.00 37.44 ? 189 LYS   A O   1 
ATOM   1440 C CB  . LYS   A 1 190 ? -3.281  -9.536  -5.650  1.00 38.80 ? 189 LYS   A CB  1 
ATOM   1441 C CG  . LYS   A 1 190 ? -2.363  -10.198 -6.665  1.00 42.39 ? 189 LYS   A CG  1 
ATOM   1442 C CD  . LYS   A 1 190 ? -3.168  -11.041 -7.666  1.00 45.57 ? 189 LYS   A CD  1 
ATOM   1443 C CE  . LYS   A 1 190 ? -2.228  -11.648 -8.670  1.00 50.62 ? 189 LYS   A CE  1 
ATOM   1444 N NZ  . LYS   A 1 190 ? -2.872  -11.843 -9.997  1.00 52.73 ? 189 LYS   A NZ  1 
ATOM   1445 N N   . GLY   A 1 191 ? -0.210  -9.332  -4.378  1.00 38.49 ? 190 GLY   A N   1 
ATOM   1446 C CA  . GLY   A 1 191 ? 0.835   -10.158 -3.797  1.00 40.53 ? 190 GLY   A CA  1 
ATOM   1447 C C   . GLY   A 1 191 ? 1.271   -9.584  -2.478  1.00 42.13 ? 190 GLY   A C   1 
ATOM   1448 O O   . GLY   A 1 191 ? 1.504   -8.370  -2.387  1.00 43.53 ? 190 GLY   A O   1 
ATOM   1449 N N   . GLY   A 1 192 ? 1.358   -10.431 -1.463  1.00 40.86 ? 191 GLY   A N   1 
ATOM   1450 C CA  . GLY   A 1 192 ? 1.836   -9.928  -0.184  1.00 39.95 ? 191 GLY   A CA  1 
ATOM   1451 C C   . GLY   A 1 192 ? 3.345   -9.983  -0.185  1.00 38.82 ? 191 GLY   A C   1 
ATOM   1452 O O   . GLY   A 1 192 ? 3.995   -9.969  -1.245  1.00 39.11 ? 191 GLY   A O   1 
ATOM   1453 N N   . TYR   A 1 193 ? 3.908   -9.991  1.011   1.00 36.02 ? 192 TYR   A N   1 
ATOM   1454 C CA  . TYR   A 1 193 ? 5.339   -10.149 1.167   1.00 32.85 ? 192 TYR   A CA  1 
ATOM   1455 C C   . TYR   A 1 193 ? 5.572   -10.923 2.452   1.00 33.15 ? 192 TYR   A C   1 
ATOM   1456 O O   . TYR   A 1 193 ? 4.624   -11.256 3.183   1.00 34.33 ? 192 TYR   A O   1 
ATOM   1457 C CB  . TYR   A 1 193 ? 6.091   -8.786  1.089   1.00 31.12 ? 192 TYR   A CB  1 
ATOM   1458 C CG  . TYR   A 1 193 ? 5.757   -7.779  2.160   1.00 30.41 ? 192 TYR   A CG  1 
ATOM   1459 C CD1 . TYR   A 1 193 ? 6.265   -7.903  3.447   1.00 29.79 ? 192 TYR   A CD1 1 
ATOM   1460 C CD2 . TYR   A 1 193 ? 4.891   -6.723  1.903   1.00 29.80 ? 192 TYR   A CD2 1 
ATOM   1461 C CE1 . TYR   A 1 193 ? 5.950   -6.983  4.438   1.00 30.11 ? 192 TYR   A CE1 1 
ATOM   1462 C CE2 . TYR   A 1 193 ? 4.631   -5.762  2.861   1.00 30.84 ? 192 TYR   A CE2 1 
ATOM   1463 C CZ  . TYR   A 1 193 ? 5.153   -5.896  4.136   1.00 31.47 ? 192 TYR   A CZ  1 
ATOM   1464 O OH  . TYR   A 1 193 ? 4.856   -4.946  5.094   1.00 32.99 ? 192 TYR   A OH  1 
ATOM   1465 N N   . ASN   A 1 194 ? 6.822   -11.267 2.712   1.00 32.68 ? 193 ASN   A N   1 
ATOM   1466 C CA  . ASN   A 1 194 ? 7.173   -11.993 3.899   1.00 32.43 ? 193 ASN   A CA  1 
ATOM   1467 C C   . ASN   A 1 194 ? 8.502   -11.416 4.429   1.00 31.21 ? 193 ASN   A C   1 
ATOM   1468 O O   . ASN   A 1 194 ? 9.006   -10.414 3.905   1.00 30.37 ? 193 ASN   A O   1 
ATOM   1469 C CB  . ASN   A 1 194 ? 7.175   -13.521 3.630   1.00 33.93 ? 193 ASN   A CB  1 
ATOM   1470 C CG  . ASN   A 1 194 ? 8.241   -13.994 2.649   1.00 36.02 ? 193 ASN   A CG  1 
ATOM   1471 O OD1 . ASN   A 1 194 ? 9.201   -13.285 2.328   1.00 35.85 ? 193 ASN   A OD1 1 
ATOM   1472 N ND2 . ASN   A 1 194 ? 8.091   -15.205 2.142   1.00 36.38 ? 193 ASN   A ND2 1 
ATOM   1473 N N   . GLU   A 1 195 ? 9.046   -12.027 5.478   1.00 29.72 ? 194 GLU   A N   1 
ATOM   1474 C CA  . GLU   A 1 195 ? 10.244  -11.550 6.151   1.00 29.08 ? 194 GLU   A CA  1 
ATOM   1475 C C   . GLU   A 1 195 ? 11.475  -11.441 5.237   1.00 29.25 ? 194 GLU   A C   1 
ATOM   1476 O O   . GLU   A 1 195 ? 12.419  -10.732 5.567   1.00 28.20 ? 194 GLU   A O   1 
ATOM   1477 C CB  . GLU   A 1 195 ? 10.509  -12.457 7.374   1.00 29.61 ? 194 GLU   A CB  1 
ATOM   1478 C CG  . GLU   A 1 195 ? 11.044  -13.827 7.028   1.00 29.80 ? 194 GLU   A CG  1 
ATOM   1479 C CD  . GLU   A 1 195 ? 10.033  -14.893 6.615   1.00 36.64 ? 194 GLU   A CD  1 
ATOM   1480 O OE1 . GLU   A 1 195 ? 10.475  -16.049 6.428   1.00 36.58 ? 194 GLU   A OE1 1 
ATOM   1481 O OE2 . GLU   A 1 195 ? 8.820   -14.594 6.468   1.00 38.62 ? 194 GLU   A OE2 1 
ATOM   1482 N N   . LEU   A 1 196 ? 11.467  -12.125 4.080   1.00 28.99 ? 195 LEU   A N   1 
ATOM   1483 C CA  . LEU   A 1 196 ? 12.593  -12.047 3.159   1.00 26.70 ? 195 LEU   A CA  1 
ATOM   1484 C C   . LEU   A 1 196 ? 12.793  -10.647 2.572   1.00 25.73 ? 195 LEU   A C   1 
ATOM   1485 O O   . LEU   A 1 196 ? 13.903  -10.348 2.107   1.00 26.55 ? 195 LEU   A O   1 
ATOM   1486 C CB  . LEU   A 1 196 ? 12.512  -13.098 2.078   1.00 26.10 ? 195 LEU   A CB  1 
ATOM   1487 C CG  . LEU   A 1 196 ? 12.618  -14.520 2.676   1.00 27.99 ? 195 LEU   A CG  1 
ATOM   1488 C CD1 . LEU   A 1 196 ? 12.339  -15.581 1.625   1.00 30.58 ? 195 LEU   A CD1 1 
ATOM   1489 C CD2 . LEU   A 1 196 ? 14.022  -14.732 3.255   1.00 26.92 ? 195 LEU   A CD2 1 
ATOM   1490 N N   . CYS   A 1 197 ? 11.768  -9.744  2.651   1.00 24.58 ? 196 CYS   A N   1 
ATOM   1491 C CA  . CYS   A 1 197 ? 11.942  -8.369  2.197   1.00 24.24 ? 196 CYS   A CA  1 
ATOM   1492 C C   . CYS   A 1 197 ? 13.068  -7.687  3.015   1.00 24.69 ? 196 CYS   A C   1 
ATOM   1493 O O   . CYS   A 1 197 ? 13.756  -6.830  2.478   1.00 25.47 ? 196 CYS   A O   1 
ATOM   1494 C CB  . CYS   A 1 197 ? 10.627  -7.586  2.303   1.00 25.60 ? 196 CYS   A CB  1 
ATOM   1495 S SG  . CYS   A 1 197 ? 10.068  -7.301  4.007   1.00 27.43 ? 196 CYS   A SG  1 
ATOM   1496 N N   . ASP   A 1 198 ? 13.257  -8.065  4.304   1.00 23.99 ? 197 ASP   A N   1 
ATOM   1497 C CA  . ASP   A 1 198 ? 14.337  -7.486  5.123   1.00 24.12 ? 197 ASP   A CA  1 
ATOM   1498 C C   . ASP   A 1 198 ? 15.725  -7.854  4.606   1.00 24.01 ? 197 ASP   A C   1 
ATOM   1499 O O   . ASP   A 1 198 ? 16.669  -7.059  4.774   1.00 23.37 ? 197 ASP   A O   1 
ATOM   1500 C CB  . ASP   A 1 198 ? 14.222  -7.951  6.592   1.00 24.47 ? 197 ASP   A CB  1 
ATOM   1501 C CG  . ASP   A 1 198 ? 13.078  -7.311  7.319   1.00 27.33 ? 197 ASP   A CG  1 
ATOM   1502 O OD1 . ASP   A 1 198 ? 12.665  -6.198  6.918   1.00 28.46 ? 197 ASP   A OD1 1 
ATOM   1503 O OD2 . ASP   A 1 198 ? 12.563  -7.929  8.280   1.00 29.86 ? 197 ASP   A OD2 1 
ATOM   1504 N N   . ILE   A 1 199 ? 15.862  -9.025  3.981   1.00 23.67 ? 198 ILE   A N   1 
ATOM   1505 C CA  . ILE   A 1 199 ? 17.133  -9.477  3.404   1.00 24.78 ? 198 ILE   A CA  1 
ATOM   1506 C C   . ILE   A 1 199 ? 17.499  -8.578  2.245   1.00 25.21 ? 198 ILE   A C   1 
ATOM   1507 O O   . ILE   A 1 199 ? 18.650  -8.121  2.164   1.00 25.41 ? 198 ILE   A O   1 
ATOM   1508 C CB  . ILE   A 1 199 ? 17.065  -10.967 3.013   1.00 26.20 ? 198 ILE   A CB  1 
ATOM   1509 C CG1 . ILE   A 1 199 ? 16.660  -11.797 4.253   1.00 27.72 ? 198 ILE   A CG1 1 
ATOM   1510 C CG2 . ILE   A 1 199 ? 18.406  -11.438 2.383   1.00 26.39 ? 198 ILE   A CG2 1 
ATOM   1511 C CD1 . ILE   A 1 199 ? 17.603  -11.588 5.393   1.00 28.73 ? 198 ILE   A CD1 1 
ATOM   1512 N N   . TRP   A 1 200 ? 16.517  -8.257  1.382   1.00 24.49 ? 199 TRP   A N   1 
ATOM   1513 C CA  . TRP   A 1 200 ? 16.757  -7.315  0.264   1.00 25.03 ? 199 TRP   A CA  1 
ATOM   1514 C C   . TRP   A 1 200 ? 17.193  -5.938  0.833   1.00 26.17 ? 199 TRP   A C   1 
ATOM   1515 O O   . TRP   A 1 200 ? 18.164  -5.351  0.353   1.00 25.82 ? 199 TRP   A O   1 
ATOM   1516 C CB  . TRP   A 1 200 ? 15.445  -7.128  -0.554  1.00 24.06 ? 199 TRP   A CB  1 
ATOM   1517 C CG  . TRP   A 1 200 ? 15.537  -6.073  -1.628  1.00 23.56 ? 199 TRP   A CG  1 
ATOM   1518 C CD1 . TRP   A 1 200 ? 15.547  -4.721  -1.445  1.00 23.85 ? 199 TRP   A CD1 1 
ATOM   1519 C CD2 . TRP   A 1 200 ? 15.685  -6.291  -3.056  1.00 22.84 ? 199 TRP   A CD2 1 
ATOM   1520 N NE1 . TRP   A 1 200 ? 15.691  -4.082  -2.664  1.00 24.69 ? 199 TRP   A NE1 1 
ATOM   1521 C CE2 . TRP   A 1 200 ? 15.729  -5.020  -3.669  1.00 23.53 ? 199 TRP   A CE2 1 
ATOM   1522 C CE3 . TRP   A 1 200 ? 15.737  -7.434  -3.864  1.00 23.59 ? 199 TRP   A CE3 1 
ATOM   1523 C CZ2 . TRP   A 1 200 ? 15.870  -4.859  -5.046  1.00 24.36 ? 199 TRP   A CZ2 1 
ATOM   1524 C CZ3 . TRP   A 1 200 ? 15.843  -7.280  -5.237  1.00 24.82 ? 199 TRP   A CZ3 1 
ATOM   1525 C CH2 . TRP   A 1 200 ? 15.978  -6.009  -5.813  1.00 24.92 ? 199 TRP   A CH2 1 
ATOM   1526 N N   . SER   A 1 201 ? 16.468  -5.434  1.845   1.00 25.35 ? 200 SER   A N   1 
ATOM   1527 C CA  . SER   A 1 201 ? 16.753  -4.096  2.432   1.00 25.01 ? 200 SER   A CA  1 
ATOM   1528 C C   . SER   A 1 201 ? 18.183  -4.063  3.015   1.00 24.53 ? 200 SER   A C   1 
ATOM   1529 O O   . SER   A 1 201 ? 18.830  -3.014  3.002   1.00 25.02 ? 200 SER   A O   1 
ATOM   1530 C CB  . SER   A 1 201 ? 15.719  -3.777  3.519   1.00 25.76 ? 200 SER   A CB  1 
ATOM   1531 O OG  . SER   A 1 201 ? 14.399  -3.656  2.995   1.00 24.15 ? 200 SER   A OG  1 
ATOM   1532 N N   . LEU   A 1 202 ? 18.663  -5.204  3.532   1.00 23.05 ? 201 LEU   A N   1 
ATOM   1533 C CA  . LEU   A 1 202 ? 20.023  -5.267  4.071   1.00 24.74 ? 201 LEU   A CA  1 
ATOM   1534 C C   . LEU   A 1 202 ? 21.064  -5.207  2.916   1.00 24.45 ? 201 LEU   A C   1 
ATOM   1535 O O   . LEU   A 1 202 ? 22.048  -4.500  3.031   1.00 23.92 ? 201 LEU   A O   1 
ATOM   1536 C CB  . LEU   A 1 202 ? 20.243  -6.500  4.962   1.00 26.20 ? 201 LEU   A CB  1 
ATOM   1537 C CG  . LEU   A 1 202 ? 21.700  -6.611  5.476   1.00 29.04 ? 201 LEU   A CG  1 
ATOM   1538 C CD1 . LEU   A 1 202 ? 22.137  -5.372  6.294   1.00 28.14 ? 201 LEU   A CD1 1 
ATOM   1539 C CD2 . LEU   A 1 202 ? 21.894  -7.832  6.199   1.00 31.52 ? 201 LEU   A CD2 1 
ATOM   1540 N N   . GLY   A 1 203 ? 20.779  -5.834  1.779   1.00 24.84 ? 202 GLY   A N   1 
ATOM   1541 C CA  . GLY   A 1 203 ? 21.646  -5.738  0.598   1.00 24.01 ? 202 GLY   A CA  1 
ATOM   1542 C C   . GLY   A 1 203 ? 21.727  -4.296  0.101   1.00 24.38 ? 202 GLY   A C   1 
ATOM   1543 O O   . GLY   A 1 203 ? 22.804  -3.770  -0.159  1.00 24.95 ? 202 GLY   A O   1 
ATOM   1544 N N   . ILE   A 1 204 ? 20.591  -3.598  0.041   1.00 24.92 ? 203 ILE   A N   1 
ATOM   1545 C CA  . ILE   A 1 204 ? 20.604  -2.160  -0.340  1.00 24.63 ? 203 ILE   A CA  1 
ATOM   1546 C C   . ILE   A 1 204 ? 21.392  -1.345  0.689   1.00 25.39 ? 203 ILE   A C   1 
ATOM   1547 O O   . ILE   A 1 204 ? 22.153  -0.468  0.312   1.00 26.90 ? 203 ILE   A O   1 
ATOM   1548 C CB  . ILE   A 1 204 ? 19.172  -1.596  -0.427  1.00 23.30 ? 203 ILE   A CB  1 
ATOM   1549 C CG1 . ILE   A 1 204 ? 18.388  -2.384  -1.459  1.00 24.23 ? 203 ILE   A CG1 1 
ATOM   1550 C CG2 . ILE   A 1 204 ? 19.219  -0.048  -0.720  1.00 24.16 ? 203 ILE   A CG2 1 
ATOM   1551 C CD1 . ILE   A 1 204 ? 18.797  -2.066  -3.009  1.00 24.58 ? 203 ILE   A CD1 1 
ATOM   1552 N N   . THR   A 1 205 ? 21.207  -1.622  2.000   1.00 24.17 ? 204 THR   A N   1 
ATOM   1553 C CA  . THR   A 1 205 ? 21.938  -0.924  3.054   1.00 24.56 ? 204 THR   A CA  1 
ATOM   1554 C C   . THR   A 1 205 ? 23.448  -1.106  2.867   1.00 25.59 ? 204 THR   A C   1 
ATOM   1555 O O   . THR   A 1 205 ? 24.196  -0.144  3.016   1.00 25.02 ? 204 THR   A O   1 
ATOM   1556 C CB  . THR   A 1 205 ? 21.488  -1.433  4.443   1.00 25.34 ? 204 THR   A CB  1 
ATOM   1557 O OG1 . THR   A 1 205 ? 20.128  -1.052  4.579   1.00 25.32 ? 204 THR   A OG1 1 
ATOM   1558 C CG2 . THR   A 1 205 ? 22.281  -0.768  5.584   1.00 26.64 ? 204 THR   A CG2 1 
ATOM   1559 N N   . ALA   A 1 206 ? 23.874  -2.299  2.463   1.00 26.08 ? 205 ALA   A N   1 
ATOM   1560 C CA  . ALA   A 1 206 ? 25.300  -2.547  2.249   1.00 26.54 ? 205 ALA   A CA  1 
ATOM   1561 C C   . ALA   A 1 206 ? 25.826  -1.680  1.084   1.00 27.64 ? 205 ALA   A C   1 
ATOM   1562 O O   . ALA   A 1 206 ? 26.935  -1.167  1.181   1.00 28.32 ? 205 ALA   A O   1 
ATOM   1563 C CB  . ALA   A 1 206 ? 25.542  -4.040  1.991   1.00 27.09 ? 205 ALA   A CB  1 
ATOM   1564 N N   . ILE   A 1 207 ? 25.057  -1.503  0.004   1.00 27.48 ? 206 ILE   A N   1 
ATOM   1565 C CA  . ILE   A 1 207 ? 25.448  -0.602  -1.098  1.00 28.12 ? 206 ILE   A CA  1 
ATOM   1566 C C   . ILE   A 1 207 ? 25.437  0.850   -0.570  1.00 28.46 ? 206 ILE   A C   1 
ATOM   1567 O O   . ILE   A 1 207 ? 26.322  1.635   -0.877  1.00 28.95 ? 206 ILE   A O   1 
ATOM   1568 C CB  . ILE   A 1 207 ? 24.459  -0.742  -2.294  1.00 29.24 ? 206 ILE   A CB  1 
ATOM   1569 C CG1 . ILE   A 1 207 ? 24.590  -2.123  -2.946  1.00 30.10 ? 206 ILE   A CG1 1 
ATOM   1570 C CG2 . ILE   A 1 207 ? 24.721  0.364   -3.333  1.00 30.44 ? 206 ILE   A CG2 1 
ATOM   1571 C CD1 . ILE   A 1 207 ? 23.507  -2.423  -4.064  1.00 32.00 ? 206 ILE   A CD1 1 
ATOM   1572 N N   . GLU   A 1 208 ? 24.470  1.200   0.273   1.00 27.65 ? 207 GLU   A N   1 
ATOM   1573 C CA  . GLU   A 1 208 ? 24.393  2.531   0.895   1.00 27.41 ? 207 GLU   A CA  1 
ATOM   1574 C C   . GLU   A 1 208 ? 25.680  2.830   1.696   1.00 28.84 ? 207 GLU   A C   1 
ATOM   1575 O O   . GLU   A 1 208 ? 26.188  3.964   1.639   1.00 28.91 ? 207 GLU   A O   1 
ATOM   1576 C CB  . GLU   A 1 208 ? 23.169  2.554   1.807   1.00 28.39 ? 207 GLU   A CB  1 
ATOM   1577 C CG  . GLU   A 1 208 ? 23.008  3.826   2.606   1.00 27.79 ? 207 GLU   A CG  1 
ATOM   1578 C CD  . GLU   A 1 208 ? 22.072  3.702   3.792   1.00 29.80 ? 207 GLU   A CD  1 
ATOM   1579 O OE1 . GLU   A 1 208 ? 21.417  2.645   3.965   1.00 29.27 ? 207 GLU   A OE1 1 
ATOM   1580 O OE2 . GLU   A 1 208 ? 22.021  4.673   4.574   1.00 30.10 ? 207 GLU   A OE2 1 
ATOM   1581 N N   . LEU   A 1 209 ? 26.151  1.878   2.494   1.00 28.94 ? 208 LEU   A N   1 
ATOM   1582 C CA  . LEU   A 1 209 ? 27.396  2.114   3.290   1.00 29.06 ? 208 LEU   A CA  1 
ATOM   1583 C C   . LEU   A 1 209 ? 28.627  2.219   2.432   1.00 29.85 ? 208 LEU   A C   1 
ATOM   1584 O O   . LEU   A 1 209 ? 29.564  2.963   2.761   1.00 29.33 ? 208 LEU   A O   1 
ATOM   1585 C CB  . LEU   A 1 209 ? 27.592  0.996   4.304   1.00 28.43 ? 208 LEU   A CB  1 
ATOM   1586 C CG  . LEU   A 1 209 ? 26.449  0.789   5.267   1.00 28.41 ? 208 LEU   A CG  1 
ATOM   1587 C CD1 . LEU   A 1 209 ? 26.688  -0.538  6.102   1.00 28.87 ? 208 LEU   A CD1 1 
ATOM   1588 C CD2 . LEU   A 1 209 ? 26.235  2.029   6.131   1.00 28.18 ? 208 LEU   A CD2 1 
ATOM   1589 N N   . ALA   A 1 210 ? 28.608  1.530   1.291   1.00 30.36 ? 209 ALA   A N   1 
ATOM   1590 C CA  . ALA   A 1 210 ? 29.692  1.580   0.309   1.00 31.04 ? 209 ALA   A CA  1 
ATOM   1591 C C   . ALA   A 1 210 ? 29.639  2.865   -0.545  1.00 31.98 ? 209 ALA   A C   1 
ATOM   1592 O O   . ALA   A 1 210 ? 30.685  3.351   -0.985  1.00 32.91 ? 209 ALA   A O   1 
ATOM   1593 C CB  . ALA   A 1 210 ? 29.555  0.375   -0.616  1.00 30.94 ? 209 ALA   A CB  1 
ATOM   1594 N N   . GLU   A 1 211 ? 28.419  3.370   -0.868  1.00 30.64 ? 210 GLU   A N   1 
ATOM   1595 C CA  . GLU   A 1 211 ? 28.294  4.452   -1.845  1.00 32.04 ? 210 GLU   A CA  1 
ATOM   1596 C C   . GLU   A 1 211 ? 27.703  5.769   -1.358  1.00 33.24 ? 210 GLU   A C   1 
ATOM   1597 O O   . GLU   A 1 211 ? 27.668  6.748   -2.142  1.00 34.92 ? 210 GLU   A O   1 
ATOM   1598 C CB  . GLU   A 1 211 ? 27.473  3.956   -3.048  1.00 34.57 ? 210 GLU   A CB  1 
ATOM   1599 C CG  . GLU   A 1 211 ? 28.016  2.671   -3.625  1.00 35.64 ? 210 GLU   A CG  1 
ATOM   1600 C CD  . GLU   A 1 211 ? 27.415  2.135   -4.909  1.00 37.28 ? 210 GLU   A CD  1 
ATOM   1601 O OE1 . GLU   A 1 211 ? 26.377  2.646   -5.385  1.00 35.56 ? 210 GLU   A OE1 1 
ATOM   1602 O OE2 . GLU   A 1 211 ? 28.024  1.188   -5.450  1.00 36.94 ? 210 GLU   A OE2 1 
ATOM   1603 N N   . LEU   A 1 212 ? 27.311  5.816   -0.070  1.00 31.59 ? 211 LEU   A N   1 
ATOM   1604 C CA  . LEU   A 1 212 ? 26.738  6.991   0.636   1.00 31.16 ? 211 LEU   A CA  1 
ATOM   1605 C C   . LEU   A 1 212 ? 25.298  7.328   0.272   1.00 31.05 ? 211 LEU   A C   1 
ATOM   1606 O O   . LEU   A 1 212 ? 24.762  8.375   0.661   1.00 32.18 ? 211 LEU   A O   1 
ATOM   1607 C CB  . LEU   A 1 212 ? 27.614  8.233   0.476   1.00 30.23 ? 211 LEU   A CB  1 
ATOM   1608 C CG  . LEU   A 1 212 ? 29.100  8.050   0.751   1.00 32.19 ? 211 LEU   A CG  1 
ATOM   1609 C CD1 . LEU   A 1 212 ? 29.845  9.378   0.627   1.00 32.99 ? 211 LEU   A CD1 1 
ATOM   1610 C CD2 . LEU   A 1 212 ? 29.365  7.322   2.106   1.00 32.80 ? 211 LEU   A CD2 1 
ATOM   1611 N N   . GLN   A 1 213 ? 24.670  6.447   -0.471  1.00 30.57 ? 212 GLN   A N   1 
ATOM   1612 C CA  . GLN   A 1 213 ? 23.288  6.570   -0.880  1.00 29.80 ? 212 GLN   A CA  1 
ATOM   1613 C C   . GLN   A 1 213 ? 22.874  5.198   -1.443  1.00 30.13 ? 212 GLN   A C   1 
ATOM   1614 O O   . GLN   A 1 213 ? 23.703  4.460   -2.018  1.00 31.13 ? 212 GLN   A O   1 
ATOM   1615 C CB  . GLN   A 1 213 ? 23.104  7.712   -1.921  1.00 31.05 ? 212 GLN   A CB  1 
ATOM   1616 C CG  . GLN   A 1 213 ? 23.454  7.391   -3.371  1.00 35.05 ? 212 GLN   A CG  1 
ATOM   1617 C CD  . GLN   A 1 213 ? 23.126  8.560   -4.298  1.00 40.96 ? 212 GLN   A CD  1 
ATOM   1618 O OE1 . GLN   A 1 213 ? 23.118  9.713   -3.890  1.00 40.63 ? 212 GLN   A OE1 1 
ATOM   1619 N NE2 . GLN   A 1 213 ? 22.808  8.283   -5.565  1.00 41.83 ? 212 GLN   A NE2 1 
ATOM   1620 N N   . PRO   A 1 214 ? 21.590  4.850   -1.311  1.00 28.92 ? 213 PRO   A N   1 
ATOM   1621 C CA  . PRO   A 1 214 ? 21.117  3.614   -1.932  1.00 29.24 ? 213 PRO   A CA  1 
ATOM   1622 C C   . PRO   A 1 214 ? 21.021  3.794   -3.464  1.00 30.76 ? 213 PRO   A C   1 
ATOM   1623 O O   . PRO   A 1 214 ? 20.979  4.931   -3.965  1.00 30.50 ? 213 PRO   A O   1 
ATOM   1624 C CB  . PRO   A 1 214 ? 19.718  3.446   -1.326  1.00 28.48 ? 213 PRO   A CB  1 
ATOM   1625 C CG  . PRO   A 1 214 ? 19.240  4.862   -1.189  1.00 28.78 ? 213 PRO   A CG  1 
ATOM   1626 C CD  . PRO   A 1 214 ? 20.487  5.581   -0.663  1.00 28.08 ? 213 PRO   A CD  1 
ATOM   1627 N N   . PRO   A 1 215 ? 20.933  2.691   -4.223  1.00 31.18 ? 214 PRO   A N   1 
ATOM   1628 C CA  . PRO   A 1 215 ? 20.784  2.827   -5.689  1.00 32.01 ? 214 PRO   A CA  1 
ATOM   1629 C C   . PRO   A 1 215 ? 19.538  3.602   -6.082  1.00 31.91 ? 214 PRO   A C   1 
ATOM   1630 O O   . PRO   A 1 215 ? 18.511  3.547   -5.396  1.00 31.26 ? 214 PRO   A O   1 
ATOM   1631 C CB  . PRO   A 1 215 ? 20.696  1.365   -6.190  1.00 33.17 ? 214 PRO   A CB  1 
ATOM   1632 C CG  . PRO   A 1 215 ? 21.257  0.540   -5.080  1.00 33.21 ? 214 PRO   A CG  1 
ATOM   1633 C CD  . PRO   A 1 215 ? 21.030  1.284   -3.796  1.00 31.31 ? 214 PRO   A CD  1 
ATOM   1634 N N   . LEU   A 1 216 ? 19.620  4.331   -7.173  1.00 32.35 ? 215 LEU   A N   1 
ATOM   1635 C CA  . LEU   A 1 216 ? 18.489  5.113   -7.691  1.00 34.04 ? 215 LEU   A CA  1 
ATOM   1636 C C   . LEU   A 1 216 ? 17.982  6.234   -6.763  1.00 34.01 ? 215 LEU   A C   1 
ATOM   1637 O O   . LEU   A 1 216 ? 16.898  6.756   -7.030  1.00 33.44 ? 215 LEU   A O   1 
ATOM   1638 C CB  . LEU   A 1 216 ? 17.297  4.191   -8.095  1.00 35.56 ? 215 LEU   A CB  1 
ATOM   1639 C CG  . LEU   A 1 216 ? 17.597  3.077   -9.130  1.00 38.59 ? 215 LEU   A CG  1 
ATOM   1640 C CD1 . LEU   A 1 216 ? 16.341  2.298   -9.466  1.00 39.69 ? 215 LEU   A CD1 1 
ATOM   1641 C CD2 . LEU   A 1 216 ? 18.198  3.657   -10.406 1.00 40.35 ? 215 LEU   A CD2 1 
ATOM   1642 N N   . PHE   A 1 217 ? 18.740  6.609   -5.703  1.00 33.91 ? 216 PHE   A N   1 
ATOM   1643 C CA  . PHE   A 1 217 ? 18.341  7.649   -4.721  1.00 34.21 ? 216 PHE   A CA  1 
ATOM   1644 C C   . PHE   A 1 217 ? 17.888  8.997   -5.329  1.00 35.12 ? 216 PHE   A C   1 
ATOM   1645 O O   . PHE   A 1 217 ? 17.037  9.694   -4.759  1.00 35.23 ? 216 PHE   A O   1 
ATOM   1646 C CB  . PHE   A 1 217 ? 19.478  7.883   -3.718  1.00 33.39 ? 216 PHE   A CB  1 
ATOM   1647 C CG  . PHE   A 1 217 ? 19.068  8.643   -2.474  1.00 33.72 ? 216 PHE   A CG  1 
ATOM   1648 C CD1 . PHE   A 1 217 ? 18.012  8.206   -1.691  1.00 33.92 ? 216 PHE   A CD1 1 
ATOM   1649 C CD2 . PHE   A 1 217 ? 19.765  9.770   -2.067  1.00 34.22 ? 216 PHE   A CD2 1 
ATOM   1650 C CE1 . PHE   A 1 217 ? 17.672  8.872   -0.521  1.00 34.07 ? 216 PHE   A CE1 1 
ATOM   1651 C CE2 . PHE   A 1 217 ? 19.428  10.429  -0.888  1.00 34.67 ? 216 PHE   A CE2 1 
ATOM   1652 C CZ  . PHE   A 1 217 ? 18.389  9.975   -0.124  1.00 34.04 ? 216 PHE   A CZ  1 
ATOM   1653 N N   . ASP   A 1 218 ? 18.469  9.362   -6.468  1.00 36.13 ? 217 ASP   A N   1 
ATOM   1654 C CA  . ASP   A 1 218 ? 18.198  10.600  -7.192  1.00 38.36 ? 217 ASP   A CA  1 
ATOM   1655 C C   . ASP   A 1 218 ? 16.981  10.521  -8.118  1.00 38.37 ? 217 ASP   A C   1 
ATOM   1656 O O   . ASP   A 1 218 ? 16.667  11.517  -8.782  1.00 37.49 ? 217 ASP   A O   1 
ATOM   1657 C CB  . ASP   A 1 218 ? 19.405  10.982  -8.064  1.00 42.35 ? 217 ASP   A CB  1 
ATOM   1658 C CG  . ASP   A 1 218 ? 20.654  11.162  -7.258  1.00 54.13 ? 217 ASP   A CG  1 
ATOM   1659 O OD1 . ASP   A 1 218 ? 20.547  11.639  -6.090  1.00 55.25 ? 217 ASP   A OD1 1 
ATOM   1660 O OD2 . ASP   A 1 218 ? 21.749  10.803  -7.771  1.00 58.72 ? 217 ASP   A OD2 1 
ATOM   1661 N N   . VAL   A 1 219 ? 16.371  9.340   -8.236  1.00 37.66 ? 218 VAL   A N   1 
ATOM   1662 C CA  . VAL   A 1 219 ? 15.203  9.148   -9.070  1.00 38.64 ? 218 VAL   A CA  1 
ATOM   1663 C C   . VAL   A 1 219 ? 13.976  9.434   -8.198  1.00 38.17 ? 218 VAL   A C   1 
ATOM   1664 O O   . VAL   A 1 219 ? 13.953  9.062   -7.017  1.00 37.77 ? 218 VAL   A O   1 
ATOM   1665 C CB  . VAL   A 1 219 ? 15.198  7.708   -9.615  1.00 39.97 ? 218 VAL   A CB  1 
ATOM   1666 C CG1 . VAL   A 1 219 ? 13.955  7.424   -10.447 1.00 40.44 ? 218 VAL   A CG1 1 
ATOM   1667 C CG2 . VAL   A 1 219 ? 16.481  7.422   -10.405 1.00 40.89 ? 218 VAL   A CG2 1 
ATOM   1668 N N   . HIS   A 1 220 ? 12.948  10.096  -8.775  1.00 37.80 ? 219 HIS   A N   1 
ATOM   1669 C CA  . HIS   A 1 220 ? 11.703  10.430  -8.101  1.00 38.58 ? 219 HIS   A CA  1 
ATOM   1670 C C   . HIS   A 1 220 ? 11.081  9.157   -7.536  1.00 40.16 ? 219 HIS   A C   1 
ATOM   1671 O O   . HIS   A 1 220 ? 11.060  8.135   -8.230  1.00 40.38 ? 219 HIS   A O   1 
ATOM   1672 C CB  . HIS   A 1 220 ? 10.734  11.097  -9.091  1.00 39.39 ? 219 HIS   A CB  1 
ATOM   1673 C CG  . HIS   A 1 220 ? 9.487   11.627  -8.465  1.00 41.84 ? 219 HIS   A CG  1 
ATOM   1674 N ND1 . HIS   A 1 220 ? 8.482   10.780  -8.012  1.00 43.89 ? 219 HIS   A ND1 1 
ATOM   1675 C CD2 . HIS   A 1 220 ? 9.082   12.912  -8.313  1.00 43.23 ? 219 HIS   A CD2 1 
ATOM   1676 C CE1 . HIS   A 1 220 ? 7.519   11.575  -7.567  1.00 44.84 ? 219 HIS   A CE1 1 
ATOM   1677 N NE2 . HIS   A 1 220 ? 7.842   12.871  -7.718  1.00 44.85 ? 219 HIS   A NE2 1 
ATOM   1678 N N   . PRO   A 1 221 ? 10.709  9.178   -6.244  1.00 40.45 ? 220 PRO   A N   1 
ATOM   1679 C CA  . PRO   A 1 221 ? 10.191  7.960   -5.600  1.00 40.68 ? 220 PRO   A CA  1 
ATOM   1680 C C   . PRO   A 1 221 ? 9.112   7.189   -6.370  1.00 40.56 ? 220 PRO   A C   1 
ATOM   1681 O O   . PRO   A 1 221 ? 9.164   5.971   -6.440  1.00 39.07 ? 220 PRO   A O   1 
ATOM   1682 C CB  . PRO   A 1 221 ? 9.670   8.465   -4.253  1.00 41.94 ? 220 PRO   A CB  1 
ATOM   1683 C CG  . PRO   A 1 221 ? 9.664   9.982   -4.349  1.00 42.52 ? 220 PRO   A CG  1 
ATOM   1684 C CD  . PRO   A 1 221 ? 10.750  10.316  -5.308  1.00 40.34 ? 220 PRO   A CD  1 
ATOM   1685 N N   . LEU   A 1 222 ? 8.179   7.895   -6.994  1.00 41.85 ? 221 LEU   A N   1 
ATOM   1686 C CA  . LEU   A 1 222 ? 7.124   7.252   -7.778  1.00 43.43 ? 221 LEU   A CA  1 
ATOM   1687 C C   . LEU   A 1 222 ? 7.679   6.598   -9.051  1.00 44.03 ? 221 LEU   A C   1 
ATOM   1688 O O   . LEU   A 1 222 ? 7.145   5.582   -9.490  1.00 45.06 ? 221 LEU   A O   1 
ATOM   1689 C CB  . LEU   A 1 222 ? 5.976   8.229   -8.076  1.00 44.30 ? 221 LEU   A CB  1 
ATOM   1690 C CG  . LEU   A 1 222 ? 5.420   8.947   -6.843  1.00 47.59 ? 221 LEU   A CG  1 
ATOM   1691 C CD1 . LEU   A 1 222 ? 4.299   9.874   -7.217  1.00 48.19 ? 221 LEU   A CD1 1 
ATOM   1692 C CD2 . LEU   A 1 222 ? 4.930   7.955   -5.768  1.00 49.60 ? 221 LEU   A CD2 1 
ATOM   1693 N N   . ARG   A 1 223 ? 8.760   7.135   -9.614  1.00 43.84 ? 222 ARG   A N   1 
ATOM   1694 C CA  . ARG   A 1 223 ? 9.401   6.509   -10.768 1.00 44.41 ? 222 ARG   A CA  1 
ATOM   1695 C C   . ARG   A 1 223 ? 10.083  5.205   -10.321 1.00 43.08 ? 222 ARG   A C   1 
ATOM   1696 O O   . ARG   A 1 223 ? 9.965   4.205   -11.028 1.00 43.87 ? 222 ARG   A O   1 
ATOM   1697 C CB  . ARG   A 1 223 ? 10.381  7.456   -11.472 1.00 47.67 ? 222 ARG   A CB  1 
ATOM   1698 C CG  . ARG   A 1 223 ? 11.075  6.820   -12.676 1.00 54.33 ? 222 ARG   A CG  1 
ATOM   1699 C CD  . ARG   A 1 223 ? 11.582  7.831   -13.706 1.00 60.88 ? 222 ARG   A CD  1 
ATOM   1700 N NE  . ARG   A 1 223 ? 13.031  7.709   -13.872 1.00 67.77 ? 222 ARG   A NE  1 
ATOM   1701 C CZ  . ARG   A 1 223 ? 13.629  6.897   -14.741 1.00 72.27 ? 222 ARG   A CZ  1 
ATOM   1702 N NH1 . ARG   A 1 223 ? 12.906  6.146   -15.566 1.00 72.61 ? 222 ARG   A NH1 1 
ATOM   1703 N NH2 . ARG   A 1 223 ? 14.954  6.834   -14.797 1.00 72.77 ? 222 ARG   A NH2 1 
ATOM   1704 N N   . VAL   A 1 224 ? 10.725  5.191   -9.125  1.00 40.31 ? 223 VAL   A N   1 
ATOM   1705 C CA  . VAL   A 1 224 ? 11.396  3.989   -8.606  1.00 38.57 ? 223 VAL   A CA  1 
ATOM   1706 C C   . VAL   A 1 224 ? 10.370  2.874   -8.366  1.00 39.24 ? 223 VAL   A C   1 
ATOM   1707 O O   . VAL   A 1 224 ? 10.644  1.719   -8.687  1.00 38.27 ? 223 VAL   A O   1 
ATOM   1708 C CB  . VAL   A 1 224 ? 12.223  4.273   -7.318  1.00 37.23 ? 223 VAL   A CB  1 
ATOM   1709 C CG1 . VAL   A 1 224 ? 12.709  2.981   -6.670  1.00 36.98 ? 223 VAL   A CG1 1 
ATOM   1710 C CG2 . VAL   A 1 224 ? 13.411  5.192   -7.616  1.00 36.91 ? 223 VAL   A CG2 1 
ATOM   1711 N N   . LEU   A 1 225 ? 9.190   3.220   -7.807  1.00 40.39 ? 224 LEU   A N   1 
ATOM   1712 C CA  . LEU   A 1 225 ? 8.122   2.249   -7.564  1.00 42.10 ? 224 LEU   A CA  1 
ATOM   1713 C C   . LEU   A 1 225 ? 7.703   1.615   -8.884  1.00 44.40 ? 224 LEU   A C   1 
ATOM   1714 O O   . LEU   A 1 225 ? 7.600   0.405   -8.966  1.00 43.88 ? 224 LEU   A O   1 
ATOM   1715 C CB  . LEU   A 1 225 ? 6.904   2.915   -6.895  1.00 41.38 ? 224 LEU   A CB  1 
ATOM   1716 C CG  . LEU   A 1 225 ? 7.039   3.218   -5.412  1.00 41.52 ? 224 LEU   A CG  1 
ATOM   1717 C CD1 . LEU   A 1 225 ? 5.871   3.994   -4.933  1.00 42.07 ? 224 LEU   A CD1 1 
ATOM   1718 C CD2 . LEU   A 1 225 ? 7.205   1.958   -4.589  1.00 41.36 ? 224 LEU   A CD2 1 
ATOM   1719 N N   . PHE   A 1 226 ? 7.542   2.438   -9.932  1.00 46.68 ? 225 PHE   A N   1 
ATOM   1720 C CA  . PHE   A 1 226 ? 7.175   1.972   -11.269 1.00 49.18 ? 225 PHE   A CA  1 
ATOM   1721 C C   . PHE   A 1 226 ? 8.190   0.993   -11.803 1.00 49.77 ? 225 PHE   A C   1 
ATOM   1722 O O   . PHE   A 1 226 ? 7.817   -0.120  -12.180 1.00 50.40 ? 225 PHE   A O   1 
ATOM   1723 C CB  . PHE   A 1 226 ? 7.029   3.157   -12.243 1.00 50.74 ? 225 PHE   A CB  1 
ATOM   1724 C CG  . PHE   A 1 226 ? 6.677   2.768   -13.663 1.00 53.63 ? 225 PHE   A CG  1 
ATOM   1725 C CD1 . PHE   A 1 226 ? 7.668   2.474   -14.587 1.00 55.32 ? 225 PHE   A CD1 1 
ATOM   1726 C CD2 . PHE   A 1 226 ? 5.359   2.719   -14.076 1.00 55.35 ? 225 PHE   A CD2 1 
ATOM   1727 C CE1 . PHE   A 1 226 ? 7.343   2.123   -15.892 1.00 56.75 ? 225 PHE   A CE1 1 
ATOM   1728 C CE2 . PHE   A 1 226 ? 5.035   2.395   -15.388 1.00 56.76 ? 225 PHE   A CE2 1 
ATOM   1729 C CZ  . PHE   A 1 226 ? 6.028   2.099   -16.289 1.00 56.90 ? 225 PHE   A CZ  1 
ATOM   1730 N N   . LEU   A 1 227 ? 9.482   1.390   -11.818 1.00 49.53 ? 226 LEU   A N   1 
ATOM   1731 C CA  . LEU   A 1 227 ? 10.543  0.559   -12.353 1.00 50.48 ? 226 LEU   A CA  1 
ATOM   1732 C C   . LEU   A 1 227 ? 10.646  -0.758  -11.631 1.00 51.53 ? 226 LEU   A C   1 
ATOM   1733 O O   . LEU   A 1 227 ? 10.841  -1.777  -12.274 1.00 50.74 ? 226 LEU   A O   1 
ATOM   1734 C CB  . LEU   A 1 227 ? 11.902  1.280   -12.324 1.00 50.62 ? 226 LEU   A CB  1 
ATOM   1735 C CG  . LEU   A 1 227 ? 11.966  2.655   -13.001 1.00 52.37 ? 226 LEU   A CG  1 
ATOM   1736 C CD1 . LEU   A 1 227 ? 13.366  3.258   -12.874 1.00 53.13 ? 226 LEU   A CD1 1 
ATOM   1737 C CD2 . LEU   A 1 227 ? 11.514  2.586   -14.455 1.00 52.85 ? 226 LEU   A CD2 1 
ATOM   1738 N N   . MET   A 1 228 ? 10.499  -0.737  -10.300 1.00 53.45 ? 227 MET   A N   1 
ATOM   1739 C CA  . MET   A 1 228 ? 10.637  -1.933  -9.468  1.00 55.65 ? 227 MET   A CA  1 
ATOM   1740 C C   . MET   A 1 228 ? 9.579   -2.984  -9.721  1.00 57.72 ? 227 MET   A C   1 
ATOM   1741 O O   . MET   A 1 228 ? 9.886   -4.164  -9.613  1.00 58.39 ? 227 MET   A O   1 
ATOM   1742 C CB  . MET   A 1 228 ? 10.712  -1.581  -7.977  1.00 56.38 ? 227 MET   A CB  1 
ATOM   1743 C CG  . MET   A 1 228 ? 12.115  -1.303  -7.531  1.00 59.02 ? 227 MET   A CG  1 
ATOM   1744 S SD  . MET   A 1 228 ? 12.332  -1.501  -5.747  1.00 61.38 ? 227 MET   A SD  1 
ATOM   1745 C CE  . MET   A 1 228 ? 11.658  -0.059  -5.247  1.00 47.43 ? 227 MET   A CE  1 
ATOM   1746 N N   . THR   A 1 229 ? 8.354   -2.584  -10.078 1.00 59.15 ? 228 THR   A N   1 
ATOM   1747 C CA  . THR   A 1 229 ? 7.299   -3.547  -10.362 1.00 61.42 ? 228 THR   A CA  1 
ATOM   1748 C C   . THR   A 1 229 ? 7.225   -3.908  -11.867 1.00 63.08 ? 228 THR   A C   1 
ATOM   1749 O O   . THR   A 1 229 ? 6.150   -4.235  -12.384 1.00 63.42 ? 228 THR   A O   1 
ATOM   1750 C CB  . THR   A 1 229 ? 5.974   -3.081  -9.770  1.00 64.08 ? 228 THR   A CB  1 
ATOM   1751 O OG1 . THR   A 1 229 ? 5.483   -1.940  -10.473 1.00 65.61 ? 228 THR   A OG1 1 
ATOM   1752 C CG2 . THR   A 1 229 ? 6.100   -2.764  -8.296  1.00 64.97 ? 228 THR   A CG2 1 
ATOM   1753 N N   . LYS   A 1 230 ? 8.378   -3.862  -12.566 1.00 63.48 ? 229 LYS   A N   1 
ATOM   1754 C CA  . LYS   A 1 230 ? 8.453   -4.249  -13.973 1.00 63.94 ? 229 LYS   A CA  1 
ATOM   1755 C C   . LYS   A 1 230 ? 9.122   -5.612  -14.050 1.00 64.69 ? 229 LYS   A C   1 
ATOM   1756 O O   . LYS   A 1 230 ? 10.019  -5.918  -13.255 1.00 65.20 ? 229 LYS   A O   1 
ATOM   1757 C CB  . LYS   A 1 230 ? 9.239   -3.234  -14.803 1.00 65.30 ? 229 LYS   A CB  1 
ATOM   1758 C CG  . LYS   A 1 230 ? 8.374   -2.153  -15.421 1.00 69.32 ? 229 LYS   A CG  1 
ATOM   1759 C CD  . LYS   A 1 230 ? 9.201   -1.182  -16.270 1.00 74.06 ? 229 LYS   A CD  1 
ATOM   1760 C CE  . LYS   A 1 230 ? 9.834   -1.819  -17.496 1.00 76.97 ? 229 LYS   A CE  1 
ATOM   1761 N NZ  . LYS   A 1 230 ? 11.302  -2.036  -17.321 1.00 78.49 ? 229 LYS   A NZ  1 
ATOM   1762 N N   . SER   A 1 231 ? 8.679   -6.444  -14.993 1.00 64.63 ? 230 SER   A N   1 
ATOM   1763 C CA  . SER   A 1 231 ? 9.233   -7.792  -15.158 1.00 64.95 ? 230 SER   A CA  1 
ATOM   1764 C C   . SER   A 1 231 ? 10.726  -7.757  -15.488 1.00 63.56 ? 230 SER   A C   1 
ATOM   1765 O O   . SER   A 1 231 ? 11.496  -8.582  -14.994 1.00 63.94 ? 230 SER   A O   1 
ATOM   1766 C CB  . SER   A 1 231 ? 8.470   -8.551  -16.243 1.00 67.40 ? 230 SER   A CB  1 
ATOM   1767 O OG  . SER   A 1 231 ? 7.070   -8.445  -16.033 1.00 70.73 ? 230 SER   A OG  1 
ATOM   1768 N N   . GLY   A 1 232 ? 11.128  -6.775  -16.281 1.00 61.71 ? 231 GLY   A N   1 
ATOM   1769 C CA  . GLY   A 1 232 ? 12.520  -6.622  -16.662 1.00 60.35 ? 231 GLY   A CA  1 
ATOM   1770 C C   . GLY   A 1 232 ? 13.379  -5.844  -15.690 1.00 58.50 ? 231 GLY   A C   1 
ATOM   1771 O O   . GLY   A 1 232 ? 14.485  -5.444  -16.065 1.00 59.10 ? 231 GLY   A O   1 
ATOM   1772 N N   . TYR   A 1 233 ? 12.903  -5.605  -14.441 1.00 56.32 ? 232 TYR   A N   1 
ATOM   1773 C CA  . TYR   A 1 233 ? 13.711  -4.870  -13.450 1.00 54.64 ? 232 TYR   A CA  1 
ATOM   1774 C C   . TYR   A 1 233 ? 14.919  -5.674  -13.102 1.00 53.17 ? 232 TYR   A C   1 
ATOM   1775 O O   . TYR   A 1 233 ? 14.803  -6.854  -12.774 1.00 53.81 ? 232 TYR   A O   1 
ATOM   1776 C CB  . TYR   A 1 233 ? 12.957  -4.547  -12.135 1.00 54.39 ? 232 TYR   A CB  1 
ATOM   1777 C CG  . TYR   A 1 233 ? 13.786  -3.700  -11.176 1.00 55.15 ? 232 TYR   A CG  1 
ATOM   1778 C CD1 . TYR   A 1 233 ? 14.196  -2.421  -11.523 1.00 55.81 ? 232 TYR   A CD1 1 
ATOM   1779 C CD2 . TYR   A 1 233 ? 14.175  -4.192  -9.933  1.00 55.38 ? 232 TYR   A CD2 1 
ATOM   1780 C CE1 . TYR   A 1 233 ? 14.963  -1.644  -10.661 1.00 56.29 ? 232 TYR   A CE1 1 
ATOM   1781 C CE2 . TYR   A 1 233 ? 14.939  -3.420  -9.056  1.00 55.63 ? 232 TYR   A CE2 1 
ATOM   1782 C CZ  . TYR   A 1 233 ? 15.331  -2.143  -9.425  1.00 56.99 ? 232 TYR   A CZ  1 
ATOM   1783 O OH  . TYR   A 1 233 ? 16.091  -1.342  -8.585  1.00 57.95 ? 232 TYR   A OH  1 
ATOM   1784 N N   . GLN   A 1 234 ? 16.075  -5.066  -13.221 1.00 51.46 ? 233 GLN   A N   1 
ATOM   1785 C CA  . GLN   A 1 234 ? 17.306  -5.731  -12.857 1.00 50.42 ? 233 GLN   A CA  1 
ATOM   1786 C C   . GLN   A 1 234 ? 17.687  -5.206  -11.484 1.00 47.60 ? 233 GLN   A C   1 
ATOM   1787 O O   . GLN   A 1 234 ? 17.747  -3.992  -11.281 1.00 47.66 ? 233 GLN   A O   1 
ATOM   1788 C CB  . GLN   A 1 234 ? 18.397  -5.482  -13.912 1.00 53.59 ? 233 GLN   A CB  1 
ATOM   1789 C CG  . GLN   A 1 234 ? 18.071  -6.118  -15.285 1.00 59.68 ? 233 GLN   A CG  1 
ATOM   1790 C CD  . GLN   A 1 234 ? 17.674  -7.592  -15.207 1.00 66.97 ? 233 GLN   A CD  1 
ATOM   1791 O OE1 . GLN   A 1 234 ? 16.545  -7.978  -15.551 1.00 69.82 ? 233 GLN   A OE1 1 
ATOM   1792 N NE2 . GLN   A 1 234 ? 18.580  -8.446  -14.733 1.00 67.19 ? 233 GLN   A NE2 1 
ATOM   1793 N N   . PRO   A 1 235 ? 17.855  -6.102  -10.499 1.00 44.57 ? 234 PRO   A N   1 
ATOM   1794 C CA  . PRO   A 1 235 ? 18.276  -5.651  -9.166  1.00 42.40 ? 234 PRO   A CA  1 
ATOM   1795 C C   . PRO   A 1 235 ? 19.570  -4.844  -9.218  1.00 40.85 ? 234 PRO   A C   1 
ATOM   1796 O O   . PRO   A 1 235 ? 20.400  -5.060  -10.087 1.00 40.80 ? 234 PRO   A O   1 
ATOM   1797 C CB  . PRO   A 1 235 ? 18.506  -6.960  -8.407  1.00 43.00 ? 234 PRO   A CB  1 
ATOM   1798 C CG  . PRO   A 1 235 ? 17.726  -8.001  -9.156  1.00 44.26 ? 234 PRO   A CG  1 
ATOM   1799 C CD  . PRO   A 1 235 ? 17.779  -7.580  -10.584 1.00 43.53 ? 234 PRO   A CD  1 
ATOM   1800 N N   . PRO   A 1 236 ? 19.749  -3.894  -8.301  1.00 39.46 ? 235 PRO   A N   1 
ATOM   1801 C CA  . PRO   A 1 236 ? 20.982  -3.089  -8.296  1.00 38.92 ? 235 PRO   A CA  1 
ATOM   1802 C C   . PRO   A 1 236 ? 22.290  -3.850  -8.088  1.00 38.37 ? 235 PRO   A C   1 
ATOM   1803 O O   . PRO   A 1 236 ? 22.328  -5.002  -7.671  1.00 38.42 ? 235 PRO   A O   1 
ATOM   1804 C CB  . PRO   A 1 236 ? 20.755  -2.151  -7.100  1.00 39.77 ? 235 PRO   A CB  1 
ATOM   1805 C CG  . PRO   A 1 236 ? 19.319  -2.090  -6.917  1.00 39.73 ? 235 PRO   A CG  1 
ATOM   1806 C CD  . PRO   A 1 236 ? 18.834  -3.462  -7.233  1.00 38.03 ? 235 PRO   A CD  1 
ATOM   1807 N N   . ARG   A 1 237 ? 23.390  -3.170  -8.374  1.00 37.89 ? 236 ARG   A N   1 
ATOM   1808 C CA  . ARG   A 1 237 ? 24.721  -3.695  -8.172  1.00 37.85 ? 236 ARG   A CA  1 
ATOM   1809 C C   . ARG   A 1 237 ? 25.615  -2.556  -7.676  1.00 36.99 ? 236 ARG   A C   1 
ATOM   1810 O O   . ARG   A 1 237 ? 25.316  -1.374  -7.899  1.00 36.72 ? 236 ARG   A O   1 
ATOM   1811 C CB  . ARG   A 1 237 ? 25.307  -4.225  -9.504  1.00 40.42 ? 236 ARG   A CB  1 
ATOM   1812 C CG  . ARG   A 1 237 ? 24.494  -5.280  -10.219 1.00 45.52 ? 236 ARG   A CG  1 
ATOM   1813 C CD  . ARG   A 1 237 ? 24.996  -5.446  -11.643 1.00 52.35 ? 236 ARG   A CD  1 
ATOM   1814 N NE  . ARG   A 1 237 ? 24.447  -6.659  -12.255 1.00 60.07 ? 236 ARG   A NE  1 
ATOM   1815 C CZ  . ARG   A 1 237 ? 24.703  -7.058  -13.497 1.00 64.66 ? 236 ARG   A CZ  1 
ATOM   1816 N NH1 . ARG   A 1 237 ? 24.159  -8.173  -13.966 1.00 64.48 ? 236 ARG   A NH1 1 
ATOM   1817 N NH2 . ARG   A 1 237 ? 25.523  -6.357  -14.273 1.00 66.38 ? 236 ARG   A NH2 1 
ATOM   1818 N N   . LEU   A 1 238 ? 26.748  -2.909  -7.070  1.00 36.10 ? 237 LEU   A N   1 
ATOM   1819 C CA  . LEU   A 1 238 ? 27.762  -1.933  -6.674  1.00 36.49 ? 237 LEU   A CA  1 
ATOM   1820 C C   . LEU   A 1 238 ? 28.302  -1.228  -7.955  1.00 40.33 ? 237 LEU   A C   1 
ATOM   1821 O O   . LEU   A 1 238 ? 28.450  -1.864  -8.998  1.00 39.45 ? 237 LEU   A O   1 
ATOM   1822 C CB  . LEU   A 1 238 ? 28.900  -2.641  -5.929  1.00 34.62 ? 237 LEU   A CB  1 
ATOM   1823 C CG  . LEU   A 1 238 ? 28.507  -3.209  -4.543  1.00 34.00 ? 237 LEU   A CG  1 
ATOM   1824 C CD1 . LEU   A 1 238 ? 29.381  -4.396  -4.179  1.00 34.33 ? 237 LEU   A CD1 1 
ATOM   1825 C CD2 . LEU   A 1 238 ? 28.473  -2.093  -3.464  1.00 32.29 ? 237 LEU   A CD2 1 
ATOM   1826 N N   . LYS   A 1 239 ? 28.531  0.085   -7.878  1.00 43.63 ? 238 LYS   A N   1 
ATOM   1827 C CA  . LYS   A 1 239 ? 28.956  0.885   -9.016  1.00 47.82 ? 238 LYS   A CA  1 
ATOM   1828 C C   . LYS   A 1 239 ? 30.418  0.683   -9.391  1.00 51.71 ? 238 LYS   A C   1 
ATOM   1829 O O   . LYS   A 1 239 ? 30.744  0.708   -10.575 1.00 52.38 ? 238 LYS   A O   1 
ATOM   1830 C CB  . LYS   A 1 239 ? 28.630  2.370   -8.780  1.00 52.03 ? 238 LYS   A CB  1 
ATOM   1831 C CG  . LYS   A 1 239 ? 28.722  3.197   -10.060 1.00 59.67 ? 238 LYS   A CG  1 
ATOM   1832 C CD  . LYS   A 1 239 ? 29.380  4.565   -9.854  1.00 65.67 ? 238 LYS   A CD  1 
ATOM   1833 C CE  . LYS   A 1 239 ? 29.602  5.256   -11.181 1.00 70.10 ? 238 LYS   A CE  1 
ATOM   1834 N NZ  . LYS   A 1 239 ? 29.698  6.733   -11.023 1.00 73.46 ? 238 LYS   A NZ  1 
ATOM   1835 N N   . GLU   A 1 240 ? 31.297  0.410   -8.416  1.00 54.22 ? 239 GLU   A N   1 
ATOM   1836 C CA  . GLU   A 1 240 ? 32.734  0.218   -8.704  1.00 55.82 ? 239 GLU   A CA  1 
ATOM   1837 C C   . GLU   A 1 240 ? 33.239  -1.218  -8.497  1.00 57.56 ? 239 GLU   A C   1 
ATOM   1838 O O   . GLU   A 1 240 ? 33.822  -1.529  -7.453  1.00 58.27 ? 239 GLU   A O   1 
ATOM   1839 C CB  . GLU   A 1 240 ? 33.557  1.173   -7.846  1.00 59.58 ? 239 GLU   A CB  1 
ATOM   1840 C CG  . GLU   A 1 240 ? 33.215  2.629   -8.059  1.00 66.84 ? 239 GLU   A CG  1 
ATOM   1841 C CD  . GLU   A 1 240 ? 34.297  3.583   -7.593  1.00 73.97 ? 239 GLU   A CD  1 
ATOM   1842 O OE1 . GLU   A 1 240 ? 34.845  3.366   -6.487  1.00 74.56 ? 239 GLU   A OE1 1 
ATOM   1843 O OE2 . GLU   A 1 240 ? 34.587  4.555   -8.329  1.00 77.62 ? 239 GLU   A OE2 1 
ATOM   1844 N N   . LYS   A 1 241 ? 33.098  -2.080  -9.516  1.00 58.39 ? 240 LYS   A N   1 
ATOM   1845 C CA  . LYS   A 1 241 ? 33.479  -3.505  -9.445  1.00 58.76 ? 240 LYS   A CA  1 
ATOM   1846 C C   . LYS   A 1 241 ? 34.938  -3.778  -9.007  1.00 58.89 ? 240 LYS   A C   1 
ATOM   1847 O O   . LYS   A 1 241 ? 35.176  -4.744  -8.259  1.00 57.83 ? 240 LYS   A O   1 
ATOM   1848 C CB  . LYS   A 1 241 ? 33.176  -4.213  -10.777 1.00 60.86 ? 240 LYS   A CB  1 
ATOM   1849 C CG  . LYS   A 1 241 ? 33.216  -5.742  -10.667 1.00 65.94 ? 240 LYS   A CG  1 
ATOM   1850 C CD  . LYS   A 1 241 ? 33.039  -6.446  -11.986 1.00 72.11 ? 240 LYS   A CD  1 
ATOM   1851 C CE  . LYS   A 1 241 ? 33.055  -7.942  -11.790 1.00 77.89 ? 240 LYS   A CE  1 
ATOM   1852 N NZ  . LYS   A 1 241 ? 31.981  -8.387  -10.853 1.00 80.81 ? 240 LYS   A NZ  1 
ATOM   1853 N N   . GLY   A 1 242 ? 35.875  -2.927  -9.490  1.00 58.90 ? 241 GLY   A N   1 
ATOM   1854 C CA  . GLY   A 1 242 ? 37.317  -2.980  -9.231  1.00 58.93 ? 241 GLY   A CA  1 
ATOM   1855 C C   . GLY   A 1 242 ? 37.839  -2.322  -7.958  1.00 57.64 ? 241 GLY   A C   1 
ATOM   1856 O O   . GLY   A 1 242 ? 38.957  -1.767  -7.928  1.00 59.23 ? 241 GLY   A O   1 
ATOM   1857 N N   . LYS   A 1 243 ? 37.049  -2.456  -6.896  1.00 54.77 ? 242 LYS   A N   1 
ATOM   1858 C CA  . LYS   A 1 243 ? 37.275  -2.000  -5.520  1.00 52.79 ? 242 LYS   A CA  1 
ATOM   1859 C C   . LYS   A 1 243 ? 36.737  -3.098  -4.553  1.00 49.72 ? 242 LYS   A C   1 
ATOM   1860 O O   . LYS   A 1 243 ? 37.384  -3.445  -3.571  1.00 51.39 ? 242 LYS   A O   1 
ATOM   1861 C CB  . LYS   A 1 243 ? 36.527  -0.664  -5.258  1.00 54.79 ? 242 LYS   A CB  1 
ATOM   1862 C CG  . LYS   A 1 243 ? 36.444  -0.267  -3.781  1.00 58.80 ? 242 LYS   A CG  1 
ATOM   1863 C CD  . LYS   A 1 243 ? 35.833  1.123   -3.545  1.00 62.33 ? 242 LYS   A CD  1 
ATOM   1864 C CE  . LYS   A 1 243 ? 36.106  1.600   -2.133  1.00 64.50 ? 242 LYS   A CE  1 
ATOM   1865 N NZ  . LYS   A 1 243 ? 35.615  2.977   -1.897  1.00 65.24 ? 242 LYS   A NZ  1 
ATOM   1866 N N   . TRP   A 1 244 ? 35.604  -3.674  -4.870  1.00 45.30 ? 243 TRP   A N   1 
ATOM   1867 C CA  . TRP   A 1 244 ? 34.941  -4.657  -4.015  1.00 41.98 ? 243 TRP   A CA  1 
ATOM   1868 C C   . TRP   A 1 244 ? 35.271  -6.063  -4.399  1.00 41.35 ? 243 TRP   A C   1 
ATOM   1869 O O   . TRP   A 1 244 ? 35.511  -6.333  -5.584  1.00 42.69 ? 243 TRP   A O   1 
ATOM   1870 C CB  . TRP   A 1 244 ? 33.425  -4.440  -4.044  1.00 39.47 ? 243 TRP   A CB  1 
ATOM   1871 C CG  . TRP   A 1 244 ? 33.025  -3.013  -3.794  1.00 36.46 ? 243 TRP   A CG  1 
ATOM   1872 C CD1 . TRP   A 1 244 ? 32.467  -2.154  -4.691  1.00 35.50 ? 243 TRP   A CD1 1 
ATOM   1873 C CD2 . TRP   A 1 244 ? 33.260  -2.253  -2.596  1.00 35.43 ? 243 TRP   A CD2 1 
ATOM   1874 N NE1 . TRP   A 1 244 ? 32.289  -0.920  -4.109  1.00 35.65 ? 243 TRP   A NE1 1 
ATOM   1875 C CE2 . TRP   A 1 244 ? 32.777  -0.952  -2.825  1.00 35.91 ? 243 TRP   A CE2 1 
ATOM   1876 C CE3 . TRP   A 1 244 ? 33.799  -2.557  -1.342  1.00 35.25 ? 243 TRP   A CE3 1 
ATOM   1877 C CZ2 . TRP   A 1 244 ? 32.821  0.045   -1.843  1.00 36.78 ? 243 TRP   A CZ2 1 
ATOM   1878 C CZ3 . TRP   A 1 244 ? 33.785  -1.593  -0.354  1.00 35.73 ? 243 TRP   A CZ3 1 
ATOM   1879 C CH2 . TRP   A 1 244 ? 33.333  -0.294  -0.618  1.00 36.37 ? 243 TRP   A CH2 1 
ATOM   1880 N N   . SER   A 1 245 ? 35.360  -6.948  -3.415  1.00 39.98 ? 244 SER   A N   1 
ATOM   1881 C CA  . SER   A 1 245 ? 35.744  -8.338  -3.716  1.00 40.48 ? 244 SER   A CA  1 
ATOM   1882 C C   . SER   A 1 245 ? 34.613  -9.109  -4.382  1.00 39.90 ? 244 SER   A C   1 
ATOM   1883 O O   . SER   A 1 245 ? 33.441  -8.687  -4.325  1.00 40.12 ? 244 SER   A O   1 
ATOM   1884 C CB  . SER   A 1 245 ? 36.185  -9.073  -2.447  1.00 42.52 ? 244 SER   A CB  1 
ATOM   1885 O OG  . SER   A 1 245 ? 35.033  -9.398  -1.678  1.00 44.49 ? 244 SER   A OG  1 
ATOM   1886 N N   . ALA   A 1 246 ? 34.963  -10.293 -4.919  1.00 39.19 ? 245 ALA   A N   1 
ATOM   1887 C CA  . ALA   A 1 246 ? 34.006  -11.258 -5.468  1.00 38.97 ? 245 ALA   A CA  1 
ATOM   1888 C C   . ALA   A 1 246 ? 33.010  -11.675 -4.409  1.00 38.87 ? 245 ALA   A C   1 
ATOM   1889 O O   . ALA   A 1 246 ? 31.823  -11.812 -4.727  1.00 38.79 ? 245 ALA   A O   1 
ATOM   1890 C CB  . ALA   A 1 246 ? 34.738  -12.485 -6.020  1.00 38.09 ? 245 ALA   A CB  1 
ATOM   1891 N N   . ALA   A 1 247 ? 33.452  -11.833 -3.142  1.00 37.68 ? 246 ALA   A N   1 
ATOM   1892 C CA  . ALA   A 1 247 ? 32.531  -12.187 -2.044  1.00 36.33 ? 246 ALA   A CA  1 
ATOM   1893 C C   . ALA   A 1 247 ? 31.464  -11.084 -1.821  1.00 35.00 ? 246 ALA   A C   1 
ATOM   1894 O O   . ALA   A 1 247 ? 30.274  -11.383 -1.590  1.00 35.08 ? 246 ALA   A O   1 
ATOM   1895 C CB  . ALA   A 1 247 ? 33.331  -12.417 -0.761  1.00 36.04 ? 246 ALA   A CB  1 
ATOM   1896 N N   . PHE   A 1 248 ? 31.896  -9.803  -1.832  1.00 32.79 ? 247 PHE   A N   1 
ATOM   1897 C CA  . PHE   A 1 248 ? 30.951  -8.700  -1.631  1.00 32.07 ? 247 PHE   A CA  1 
ATOM   1898 C C   . PHE   A 1 248 ? 29.958  -8.613  -2.803  1.00 32.60 ? 247 PHE   A C   1 
ATOM   1899 O O   . PHE   A 1 248 ? 28.755  -8.533  -2.573  1.00 32.75 ? 247 PHE   A O   1 
ATOM   1900 C CB  . PHE   A 1 248 ? 31.683  -7.390  -1.347  1.00 31.53 ? 247 PHE   A CB  1 
ATOM   1901 C CG  . PHE   A 1 248 ? 30.853  -6.197  -0.922  1.00 31.82 ? 247 PHE   A CG  1 
ATOM   1902 C CD1 . PHE   A 1 248 ? 29.571  -6.360  -0.415  1.00 32.48 ? 247 PHE   A CD1 1 
ATOM   1903 C CD2 . PHE   A 1 248 ? 31.387  -4.920  -0.948  1.00 32.51 ? 247 PHE   A CD2 1 
ATOM   1904 C CE1 . PHE   A 1 248 ? 28.801  -5.255  -0.047  1.00 33.35 ? 247 PHE   A CE1 1 
ATOM   1905 C CE2 . PHE   A 1 248 ? 30.639  -3.823  -0.524  1.00 32.82 ? 247 PHE   A CE2 1 
ATOM   1906 C CZ  . PHE   A 1 248 ? 29.345  -3.993  -0.105  1.00 33.16 ? 247 PHE   A CZ  1 
ATOM   1907 N N   . HIS   A 1 249 ? 30.430  -8.745  -4.049  1.00 33.39 ? 248 HIS   A N   1 
ATOM   1908 C CA  . HIS   A 1 249 ? 29.545  -8.758  -5.218  1.00 34.41 ? 248 HIS   A CA  1 
ATOM   1909 C C   . HIS   A 1 249 ? 28.489  -9.873  -5.110  1.00 33.86 ? 248 HIS   A C   1 
ATOM   1910 O O   . HIS   A 1 249 ? 27.328  -9.653  -5.443  1.00 32.56 ? 248 HIS   A O   1 
ATOM   1911 C CB  . HIS   A 1 249 ? 30.353  -8.911  -6.530  1.00 35.59 ? 248 HIS   A CB  1 
ATOM   1912 C CG  . HIS   A 1 249 ? 30.949  -7.609  -6.975  1.00 40.29 ? 248 HIS   A CG  1 
ATOM   1913 N ND1 . HIS   A 1 249 ? 32.315  -7.413  -7.000  1.00 43.29 ? 248 HIS   A ND1 1 
ATOM   1914 C CD2 . HIS   A 1 249 ? 30.332  -6.445  -7.281  1.00 41.03 ? 248 HIS   A CD2 1 
ATOM   1915 C CE1 . HIS   A 1 249 ? 32.489  -6.151  -7.361  1.00 44.12 ? 248 HIS   A CE1 1 
ATOM   1916 N NE2 . HIS   A 1 249 ? 31.310  -5.528  -7.530  1.00 44.05 ? 248 HIS   A NE2 1 
ATOM   1917 N N   . ASN   A 1 250 ? 28.910  -11.073 -4.663  1.00 33.46 ? 249 ASN   A N   1 
ATOM   1918 C CA  . ASN   A 1 250 ? 28.012  -12.197 -4.538  1.00 33.13 ? 249 ASN   A CA  1 
ATOM   1919 C C   . ASN   A 1 250 ? 27.007  -11.978 -3.415  1.00 32.78 ? 249 ASN   A C   1 
ATOM   1920 O O   . ASN   A 1 250 ? 25.822  -12.263 -3.574  1.00 32.17 ? 249 ASN   A O   1 
ATOM   1921 C CB  . ASN   A 1 250 ? 28.790  -13.510 -4.332  1.00 33.69 ? 249 ASN   A CB  1 
ATOM   1922 C CG  . ASN   A 1 250 ? 27.842  -14.684 -4.244  1.00 37.41 ? 249 ASN   A CG  1 
ATOM   1923 O OD1 . ASN   A 1 250 ? 27.487  -15.135 -3.151  1.00 37.35 ? 249 ASN   A OD1 1 
ATOM   1924 N ND2 . ASN   A 1 250 ? 27.348  -15.137 -5.393  1.00 38.64 ? 249 ASN   A ND2 1 
ATOM   1925 N N   . PHE   A 1 251 ? 27.451  -11.392 -2.299  1.00 32.55 ? 250 PHE   A N   1 
ATOM   1926 C CA  . PHE   A 1 251 ? 26.537  -11.074 -1.191  1.00 31.27 ? 250 PHE   A CA  1 
ATOM   1927 C C   . PHE   A 1 251 ? 25.429  -10.112 -1.692  1.00 30.79 ? 250 PHE   A C   1 
ATOM   1928 O O   . PHE   A 1 251 ? 24.270  -10.313 -1.391  1.00 31.11 ? 250 PHE   A O   1 
ATOM   1929 C CB  . PHE   A 1 251 ? 27.338  -10.403 -0.047  1.00 31.02 ? 250 PHE   A CB  1 
ATOM   1930 C CG  . PHE   A 1 251 ? 26.478  -9.967  1.122   1.00 30.82 ? 250 PHE   A CG  1 
ATOM   1931 C CD1 . PHE   A 1 251 ? 26.271  -10.808 2.201   1.00 30.72 ? 250 PHE   A CD1 1 
ATOM   1932 C CD2 . PHE   A 1 251 ? 25.954  -8.681  1.180   1.00 31.98 ? 250 PHE   A CD2 1 
ATOM   1933 C CE1 . PHE   A 1 251 ? 25.495  -10.402 3.287   1.00 30.32 ? 250 PHE   A CE1 1 
ATOM   1934 C CE2 . PHE   A 1 251 ? 25.174  -8.279  2.258   1.00 32.00 ? 250 PHE   A CE2 1 
ATOM   1935 C CZ  . PHE   A 1 251 ? 24.943  -9.140  3.303   1.00 30.92 ? 250 PHE   A CZ  1 
ATOM   1936 N N   . ILE   A 1 252 ? 25.778  -9.129  -2.509  1.00 30.35 ? 251 ILE   A N   1 
ATOM   1937 C CA  . ILE   A 1 252 ? 24.810  -8.203  -3.092  1.00 30.45 ? 251 ILE   A CA  1 
ATOM   1938 C C   . ILE   A 1 252 ? 23.907  -8.967  -4.060  1.00 32.01 ? 251 ILE   A C   1 
ATOM   1939 O O   . ILE   A 1 252 ? 22.684  -8.814  -4.031  1.00 31.67 ? 251 ILE   A O   1 
ATOM   1940 C CB  . ILE   A 1 252 ? 25.564  -7.030  -3.790  1.00 30.61 ? 251 ILE   A CB  1 
ATOM   1941 C CG1 . ILE   A 1 252 ? 26.275  -6.118  -2.753  1.00 31.83 ? 251 ILE   A CG1 1 
ATOM   1942 C CG2 . ILE   A 1 252 ? 24.642  -6.195  -4.702  1.00 29.92 ? 251 ILE   A CG2 1 
ATOM   1943 C CD1 . ILE   A 1 252 ? 25.432  -5.573  -1.657  1.00 31.34 ? 251 ILE   A CD1 1 
ATOM   1944 N N   . LYS   A 1 253 ? 24.497  -9.821  -4.890  1.00 33.71 ? 252 LYS   A N   1 
ATOM   1945 C CA  . LYS   A 1 253 ? 23.744  -10.630 -5.839  1.00 34.78 ? 252 LYS   A CA  1 
ATOM   1946 C C   . LYS   A 1 253 ? 22.669  -11.500 -5.164  1.00 34.63 ? 252 LYS   A C   1 
ATOM   1947 O O   . LYS   A 1 253 ? 21.511  -11.497 -5.613  1.00 35.71 ? 252 LYS   A O   1 
ATOM   1948 C CB  . LYS   A 1 253 ? 24.701  -11.513 -6.676  1.00 37.17 ? 252 LYS   A CB  1 
ATOM   1949 C CG  . LYS   A 1 253 ? 23.990  -12.287 -7.786  1.00 42.00 ? 252 LYS   A CG  1 
ATOM   1950 C CD  . LYS   A 1 253 ? 24.998  -13.177 -8.542  1.00 48.35 ? 252 LYS   A CD  1 
ATOM   1951 C CE  . LYS   A 1 253 ? 24.379  -14.074 -9.588  1.00 52.80 ? 252 LYS   A CE  1 
ATOM   1952 N NZ  . LYS   A 1 253 ? 25.373  -15.083 -10.094 1.00 56.30 ? 252 LYS   A NZ  1 
ATOM   1953 N N   . VAL   A 1 254 ? 23.021  -12.200 -4.067  1.00 32.69 ? 253 VAL   A N   1 
ATOM   1954 C CA  . VAL   A 1 254 ? 22.050  -13.098 -3.421  1.00 32.04 ? 253 VAL   A CA  1 
ATOM   1955 C C   . VAL   A 1 254 ? 21.042  -12.332 -2.534  1.00 31.07 ? 253 VAL   A C   1 
ATOM   1956 O O   . VAL   A 1 254 ? 19.858  -12.697 -2.564  1.00 30.23 ? 253 VAL   A O   1 
ATOM   1957 C CB  . VAL   A 1 254 ? 22.700  -14.313 -2.696  1.00 33.01 ? 253 VAL   A CB  1 
ATOM   1958 C CG1 . VAL   A 1 254 ? 23.667  -15.021 -3.639  1.00 33.43 ? 253 VAL   A CG1 1 
ATOM   1959 C CG2 . VAL   A 1 254 ? 23.442  -13.882 -1.429  1.00 33.61 ? 253 VAL   A CG2 1 
ATOM   1960 N N   . THR   A 1 255 ? 21.476  -11.305 -1.756  1.00 30.38 ? 254 THR   A N   1 
ATOM   1961 C CA  . THR   A 1 255 ? 20.511  -10.528 -0.965  1.00 30.36 ? 254 THR   A CA  1 
ATOM   1962 C C   . THR   A 1 255 ? 19.513  -9.794  -1.884  1.00 30.67 ? 254 THR   A C   1 
ATOM   1963 O O   . THR   A 1 255 ? 18.315  -9.714  -1.562  1.00 31.11 ? 254 THR   A O   1 
ATOM   1964 C CB  . THR   A 1 255 ? 21.204  -9.544  -0.024  1.00 31.46 ? 254 THR   A CB  1 
ATOM   1965 O OG1 . THR   A 1 255 ? 22.018  -8.636  -0.784  1.00 31.33 ? 254 THR   A OG1 1 
ATOM   1966 C CG2 . THR   A 1 255 ? 21.990  -10.250 1.075   1.00 31.39 ? 254 THR   A CG2 1 
ATOM   1967 N N   . LEU   A 1 256 ? 19.985  -9.320  -3.047  1.00 29.95 ? 255 LEU   A N   1 
ATOM   1968 C CA  . LEU   A 1 256 ? 19.105  -8.657  -4.000  1.00 29.75 ? 255 LEU   A CA  1 
ATOM   1969 C C   . LEU   A 1 256 ? 18.527  -9.609  -5.028  1.00 30.53 ? 255 LEU   A C   1 
ATOM   1970 O O   . LEU   A 1 256 ? 18.460  -9.272  -6.206  1.00 31.86 ? 255 LEU   A O   1 
ATOM   1971 C CB  . LEU   A 1 256 ? 19.770  -7.427  -4.675  1.00 29.24 ? 255 LEU   A CB  1 
ATOM   1972 C CG  . LEU   A 1 256 ? 20.396  -6.404  -3.714  1.00 29.23 ? 255 LEU   A CG  1 
ATOM   1973 C CD1 . LEU   A 1 256 ? 20.802  -5.141  -4.463  1.00 29.09 ? 255 LEU   A CD1 1 
ATOM   1974 C CD2 . LEU   A 1 256 ? 19.411  -5.999  -2.588  1.00 28.63 ? 255 LEU   A CD2 1 
ATOM   1975 N N   . THR   A 1 257 ? 18.139  -10.829 -4.605  1.00 29.19 ? 256 THR   A N   1 
ATOM   1976 C CA  . THR   A 1 257 ? 17.457  -11.750 -5.501  1.00 28.79 ? 256 THR   A CA  1 
ATOM   1977 C C   . THR   A 1 257 ? 16.039  -11.190 -5.704  1.00 29.97 ? 256 THR   A C   1 
ATOM   1978 O O   . THR   A 1 257 ? 15.365  -10.830 -4.720  1.00 29.24 ? 256 THR   A O   1 
ATOM   1979 C CB  . THR   A 1 257 ? 17.401  -13.151 -4.897  1.00 31.06 ? 256 THR   A CB  1 
ATOM   1980 O OG1 . THR   A 1 257 ? 18.758  -13.633 -4.767  1.00 32.74 ? 256 THR   A OG1 1 
ATOM   1981 C CG2 . THR   A 1 257 ? 16.660  -14.115 -5.807  1.00 31.08 ? 256 THR   A CG2 1 
ATOM   1982 N N   . LYS   A 1 258 ? 15.624  -11.015 -6.962  1.00 30.76 ? 257 LYS   A N   1 
ATOM   1983 C CA  . LYS   A 1 258 ? 14.313  -10.424 -7.279  1.00 32.39 ? 257 LYS   A CA  1 
ATOM   1984 C C   . LYS   A 1 258 ? 13.125  -11.228 -6.679  1.00 32.38 ? 257 LYS   A C   1 
ATOM   1985 O O   . LYS   A 1 258 ? 12.271  -10.642 -6.023  1.00 32.57 ? 257 LYS   A O   1 
ATOM   1986 C CB  . LYS   A 1 258 ? 14.168  -10.262 -8.799  1.00 35.54 ? 257 LYS   A CB  1 
ATOM   1987 C CG  . LYS   A 1 258 ? 12.824  -9.782  -9.264  1.00 43.10 ? 257 LYS   A CG  1 
ATOM   1988 C CD  . LYS   A 1 258 ? 12.649  -10.119 -10.732 1.00 50.43 ? 257 LYS   A CD  1 
ATOM   1989 C CE  . LYS   A 1 258 ? 12.996  -8.950  -11.601 1.00 56.13 ? 257 LYS   A CE  1 
ATOM   1990 N NZ  . LYS   A 1 258 ? 13.253  -9.363  -13.004 1.00 59.91 ? 257 LYS   A NZ  1 
ATOM   1991 N N   . SER   A 1 259 ? 13.093  -12.550 -6.870  1.00 32.85 ? 258 SER   A N   1 
ATOM   1992 C CA  . SER   A 1 259 ? 12.014  -13.373 -6.333  1.00 33.58 ? 258 SER   A CA  1 
ATOM   1993 C C   . SER   A 1 259 ? 12.266  -13.673 -4.870  1.00 34.24 ? 258 SER   A C   1 
ATOM   1994 O O   . SER   A 1 259 ? 13.282  -14.294 -4.547  1.00 34.23 ? 258 SER   A O   1 
ATOM   1995 C CB  . SER   A 1 259 ? 11.944  -14.702 -7.081  1.00 34.76 ? 258 SER   A CB  1 
ATOM   1996 O OG  . SER   A 1 259 ? 10.950  -15.521 -6.484  1.00 37.52 ? 258 SER   A OG  1 
ATOM   1997 N N   . PRO   A 1 260 ? 11.316  -13.345 -3.990  1.00 34.45 ? 259 PRO   A N   1 
ATOM   1998 C CA  . PRO   A 1 260 ? 11.481  -13.723 -2.575  1.00 34.24 ? 259 PRO   A CA  1 
ATOM   1999 C C   . PRO   A 1 260 ? 11.491  -15.252 -2.387  1.00 34.33 ? 259 PRO   A C   1 
ATOM   2000 O O   . PRO   A 1 260 ? 12.005  -15.715 -1.374  1.00 34.53 ? 259 PRO   A O   1 
ATOM   2001 C CB  . PRO   A 1 260 ? 10.274  -13.097 -1.871  1.00 35.34 ? 259 PRO   A CB  1 
ATOM   2002 C CG  . PRO   A 1 260 ? 9.311   -12.714 -2.949  1.00 35.90 ? 259 PRO   A CG  1 
ATOM   2003 C CD  . PRO   A 1 260 ? 10.034  -12.647 -4.250  1.00 34.37 ? 259 PRO   A CD  1 
ATOM   2004 N N   . LYS   A 1 261 ? 10.967  -16.033 -3.355  1.00 33.60 ? 260 LYS   A N   1 
ATOM   2005 C CA  . LYS   A 1 261 ? 11.013  -17.492 -3.204  1.00 34.22 ? 260 LYS   A CA  1 
ATOM   2006 C C   . LYS   A 1 261 ? 12.438  -18.052 -3.443  1.00 34.65 ? 260 LYS   A C   1 
ATOM   2007 O O   . LYS   A 1 261 ? 12.686  -19.228 -3.187  1.00 34.62 ? 260 LYS   A O   1 
ATOM   2008 C CB  . LYS   A 1 261 ? 9.981   -18.169 -4.090  1.00 36.32 ? 260 LYS   A CB  1 
ATOM   2009 C CG  . LYS   A 1 261 ? 8.533   -17.822 -3.707  1.00 40.86 ? 260 LYS   A CG  1 
ATOM   2010 C CD  . LYS   A 1 261 ? 7.600   -18.453 -4.692  1.00 45.92 ? 260 LYS   A CD  1 
ATOM   2011 C CE  . LYS   A 1 261 ? 6.168   -18.017 -4.535  1.00 51.75 ? 260 LYS   A CE  1 
ATOM   2012 N NZ  . LYS   A 1 261 ? 5.298   -18.722 -5.532  1.00 55.02 ? 260 LYS   A NZ  1 
ATOM   2013 N N   . LYS   A 1 262 ? 13.352  -17.218 -3.961  1.00 34.00 ? 261 LYS   A N   1 
ATOM   2014 C CA  . LYS   A 1 262 ? 14.738  -17.612 -4.216  1.00 33.42 ? 261 LYS   A CA  1 
ATOM   2015 C C   . LYS   A 1 262 ? 15.736  -16.886 -3.302  1.00 33.12 ? 261 LYS   A C   1 
ATOM   2016 O O   . LYS   A 1 262 ? 16.919  -17.198 -3.335  1.00 33.34 ? 261 LYS   A O   1 
ATOM   2017 C CB  . LYS   A 1 262 ? 15.084  -17.361 -5.697  1.00 33.46 ? 261 LYS   A CB  1 
ATOM   2018 C CG  . LYS   A 1 262 ? 14.204  -18.169 -6.646  1.00 36.14 ? 261 LYS   A CG  1 
ATOM   2019 C CD  . LYS   A 1 262 ? 14.513  -17.938 -8.124  1.00 42.24 ? 261 LYS   A CD  1 
ATOM   2020 C CE  . LYS   A 1 262 ? 15.669  -18.804 -8.588  1.00 48.94 ? 261 LYS   A CE  1 
ATOM   2021 N NZ  . LYS   A 1 262 ? 15.288  -20.247 -8.754  1.00 52.58 ? 261 LYS   A NZ  1 
ATOM   2022 N N   . ARG   A 1 263 ? 15.273  -15.917 -2.509  1.00 32.13 ? 262 ARG   A N   1 
ATOM   2023 C CA  . ARG   A 1 263 ? 16.146  -15.105 -1.681  1.00 30.81 ? 262 ARG   A CA  1 
ATOM   2024 C C   . ARG   A 1 263 ? 16.451  -15.836 -0.383  1.00 30.94 ? 262 ARG   A C   1 
ATOM   2025 O O   . ARG   A 1 263 ? 15.550  -16.397 0.227   1.00 30.47 ? 262 ARG   A O   1 
ATOM   2026 C CB  . ARG   A 1 263 ? 15.444  -13.752 -1.403  1.00 29.98 ? 262 ARG   A CB  1 
ATOM   2027 C CG  . ARG   A 1 263 ? 16.360  -12.659 -0.839  1.00 29.36 ? 262 ARG   A CG  1 
ATOM   2028 C CD  . ARG   A 1 263 ? 15.629  -11.314 -0.724  1.00 30.80 ? 262 ARG   A CD  1 
ATOM   2029 N NE  . ARG   A 1 263 ? 14.893  -10.940 -1.935  1.00 29.45 ? 262 ARG   A NE  1 
ATOM   2030 C CZ  . ARG   A 1 263 ? 13.667  -10.405 -1.933  1.00 29.34 ? 262 ARG   A CZ  1 
ATOM   2031 N NH1 . ARG   A 1 263 ? 13.039  -10.159 -0.783  1.00 26.65 ? 262 ARG   A NH1 1 
ATOM   2032 N NH2 . ARG   A 1 263 ? 13.047  -10.145 -3.083  1.00 27.46 ? 262 ARG   A NH2 1 
ATOM   2033 N N   . PRO   A 1 264 ? 17.711  -15.832 0.065   1.00 30.91 ? 263 PRO   A N   1 
ATOM   2034 C CA  . PRO   A 1 264 ? 18.057  -16.579 1.286   1.00 30.45 ? 263 PRO   A CA  1 
ATOM   2035 C C   . PRO   A 1 264 ? 17.554  -15.931 2.557   1.00 29.31 ? 263 PRO   A C   1 
ATOM   2036 O O   . PRO   A 1 264 ? 17.387  -14.727 2.607   1.00 28.84 ? 263 PRO   A O   1 
ATOM   2037 C CB  . PRO   A 1 264 ? 19.598  -16.584 1.266   1.00 31.34 ? 263 PRO   A CB  1 
ATOM   2038 C CG  . PRO   A 1 264 ? 19.974  -16.228 -0.128  1.00 32.00 ? 263 PRO   A CG  1 
ATOM   2039 C CD  . PRO   A 1 264 ? 18.917  -15.286 -0.577  1.00 30.64 ? 263 PRO   A CD  1 
ATOM   2040 N N   . SER   A 1 265 ? 17.306  -16.754 3.579   1.00 29.72 ? 264 SER   A N   1 
ATOM   2041 C CA  . SER   A 1 265 ? 16.862  -16.310 4.902   1.00 29.34 ? 264 SER   A CA  1 
ATOM   2042 C C   . SER   A 1 265 ? 17.978  -15.592 5.636   1.00 29.65 ? 264 SER   A C   1 
ATOM   2043 O O   . SER   A 1 265 ? 19.152  -15.659 5.221   1.00 28.93 ? 264 SER   A O   1 
ATOM   2044 C CB  . SER   A 1 265 ? 16.372  -17.508 5.729   1.00 29.90 ? 264 SER   A CB  1 
ATOM   2045 O OG  . SER   A 1 265 ? 17.466  -18.334 6.093   1.00 30.75 ? 264 SER   A OG  1 
ATOM   2046 N N   . ALA   A 1 266 ? 17.643  -14.897 6.762   1.00 30.14 ? 265 ALA   A N   1 
ATOM   2047 C CA  . ALA   A 1 266 ? 18.693  -14.224 7.545   1.00 30.65 ? 265 ALA   A CA  1 
ATOM   2048 C C   . ALA   A 1 266 ? 19.665  -15.276 8.118   1.00 30.34 ? 265 ALA   A C   1 
ATOM   2049 O O   . ALA   A 1 266 ? 20.881  -15.072 8.097   1.00 30.12 ? 265 ALA   A O   1 
ATOM   2050 C CB  . ALA   A 1 266 ? 18.070  -13.412 8.677   1.00 31.43 ? 265 ALA   A CB  1 
ATOM   2051 N N   . THR   A 1 267 ? 19.135  -16.393 8.613   1.00 30.96 ? 266 THR   A N   1 
ATOM   2052 C CA  . THR   A 1 267 ? 19.979  -17.462 9.171   1.00 32.57 ? 266 THR   A CA  1 
ATOM   2053 C C   . THR   A 1 267 ? 20.904  -18.016 8.085   1.00 32.17 ? 266 THR   A C   1 
ATOM   2054 O O   . THR   A 1 267 ? 22.111  -18.125 8.315   1.00 32.60 ? 266 THR   A O   1 
ATOM   2055 C CB  . THR   A 1 267 ? 19.144  -18.553 9.841   1.00 36.78 ? 266 THR   A CB  1 
ATOM   2056 O OG1 . THR   A 1 267 ? 18.408  -17.976 10.923  1.00 39.71 ? 266 THR   A OG1 1 
ATOM   2057 C CG2 . THR   A 1 267 ? 20.006  -19.697 10.362  1.00 37.23 ? 266 THR   A CG2 1 
ATOM   2058 N N   . LYS   A 1 268 ? 20.376  -18.243 6.870   1.00 31.70 ? 267 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 268 ? 21.234  -18.725 5.758   1.00 31.94 ? 267 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 268 ? 22.336  -17.729 5.428   1.00 31.65 ? 267 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 268 ? 23.482  -18.120 5.254   1.00 32.29 ? 267 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 268 ? 20.391  -19.039 4.501   1.00 32.92 ? 267 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 268 ? 21.195  -19.514 3.291   1.00 32.66 ? 267 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 268 ? 22.035  -20.784 3.592   1.00 34.75 ? 267 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 268 ? 22.520  -21.454 2.330   1.00 37.02 ? 267 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 268 ? 23.309  -22.694 2.614   1.00 36.34 ? 267 LYS   A NZ  1 
ATOM   2067 N N   . MET   A 1 269 ? 22.000  -16.437 5.348   1.00 31.30 ? 268 MET   A N   1 
ATOM   2068 C CA  . MET   A 1 269 ? 22.971  -15.386 5.062   1.00 30.55 ? 268 MET   A CA  1 
ATOM   2069 C C   . MET   A 1 269 ? 24.062  -15.338 6.118   1.00 31.94 ? 268 MET   A C   1 
ATOM   2070 O O   . MET   A 1 269 ? 25.169  -14.961 5.761   1.00 32.67 ? 268 MET   A O   1 
ATOM   2071 C CB  . MET   A 1 269 ? 22.313  -13.979 4.961   1.00 29.92 ? 268 MET   A CB  1 
ATOM   2072 C CG  . MET   A 1 269 ? 21.423  -13.756 3.727   1.00 30.83 ? 268 MET   A CG  1 
ATOM   2073 S SD  . MET   A 1 269 ? 22.192  -14.219 2.154   1.00 35.86 ? 268 MET   A SD  1 
ATOM   2074 C CE  . MET   A 1 269 ? 23.733  -13.269 2.231   1.00 34.57 ? 268 MET   A CE  1 
ATOM   2075 N N   . LEU   A 1 270 ? 23.789  -15.715 7.400   1.00 31.26 ? 269 LEU   A N   1 
ATOM   2076 C CA  . LEU   A 1 270 ? 24.867  -15.665 8.400   1.00 32.77 ? 269 LEU   A CA  1 
ATOM   2077 C C   . LEU   A 1 270 ? 26.062  -16.608 8.064   1.00 34.88 ? 269 LEU   A C   1 
ATOM   2078 O O   . LEU   A 1 270 ? 27.158  -16.391 8.578   1.00 36.08 ? 269 LEU   A O   1 
ATOM   2079 C CB  . LEU   A 1 270 ? 24.352  -15.884 9.834   1.00 33.35 ? 269 LEU   A CB  1 
ATOM   2080 C CG  . LEU   A 1 270 ? 23.608  -14.655 10.411  1.00 35.87 ? 269 LEU   A CG  1 
ATOM   2081 C CD1 . LEU   A 1 270 ? 22.683  -15.065 11.571  1.00 36.80 ? 269 LEU   A CD1 1 
ATOM   2082 C CD2 . LEU   A 1 270 ? 24.609  -13.574 10.850  1.00 36.23 ? 269 LEU   A CD2 1 
ATOM   2083 N N   . SER   A 1 271 ? 25.867  -17.618 7.197   1.00 34.61 ? 270 SER   A N   1 
ATOM   2084 C CA  . SER   A 1 271 ? 26.998  -18.480 6.784   1.00 35.94 ? 270 SER   A CA  1 
ATOM   2085 C C   . SER   A 1 271 ? 27.560  -18.074 5.439   1.00 36.96 ? 270 SER   A C   1 
ATOM   2086 O O   . SER   A 1 271 ? 28.467  -18.728 4.950   1.00 38.47 ? 270 SER   A O   1 
ATOM   2087 C CB  . SER   A 1 271 ? 26.632  -19.957 6.789   1.00 37.41 ? 270 SER   A CB  1 
ATOM   2088 O OG  . SER   A 1 271 ? 25.452  -20.128 6.023   1.00 41.32 ? 270 SER   A OG  1 
ATOM   2089 N N   . HIS   A 1 272 ? 27.118  -16.933 4.856   1.00 35.75 ? 271 HIS   A N   1 
ATOM   2090 C CA  . HIS   A 1 272 ? 27.701  -16.433 3.607   1.00 35.27 ? 271 HIS   A CA  1 
ATOM   2091 C C   . HIS   A 1 272 ? 29.154  -16.066 3.905   1.00 36.94 ? 271 HIS   A C   1 
ATOM   2092 O O   . HIS   A 1 272 ? 29.403  -15.464 4.958   1.00 37.99 ? 271 HIS   A O   1 
ATOM   2093 C CB  . HIS   A 1 272 ? 26.964  -15.158 3.122   1.00 34.42 ? 271 HIS   A CB  1 
ATOM   2094 C CG  . HIS   A 1 272 ? 27.379  -14.767 1.737   1.00 34.29 ? 271 HIS   A CG  1 
ATOM   2095 N ND1 . HIS   A 1 272 ? 28.562  -14.046 1.494   1.00 34.98 ? 271 HIS   A ND1 1 
ATOM   2096 C CD2 . HIS   A 1 272 ? 26.837  -15.137 0.549   1.00 33.74 ? 271 HIS   A CD2 1 
ATOM   2097 C CE1 . HIS   A 1 272 ? 28.666  -13.988 0.176   1.00 34.86 ? 271 HIS   A CE1 1 
ATOM   2098 N NE2 . HIS   A 1 272 ? 27.650  -14.637 -0.430  1.00 35.04 ? 271 HIS   A NE2 1 
ATOM   2099 N N   . GLN   A 1 273 ? 30.099  -16.397 2.981   1.00 36.87 ? 272 GLN   A N   1 
ATOM   2100 C CA  . GLN   A 1 273 ? 31.528  -16.101 3.121   1.00 38.22 ? 272 GLN   A CA  1 
ATOM   2101 C C   . GLN   A 1 273 ? 31.805  -14.661 3.569   1.00 37.76 ? 272 GLN   A C   1 
ATOM   2102 O O   . GLN   A 1 273 ? 32.755  -14.445 4.308   1.00 39.22 ? 272 GLN   A O   1 
ATOM   2103 C CB  . GLN   A 1 273 ? 32.271  -16.343 1.782   1.00 42.38 ? 272 GLN   A CB  1 
ATOM   2104 C CG  . GLN   A 1 273 ? 33.822  -16.272 1.891   1.00 49.19 ? 272 GLN   A CG  1 
ATOM   2105 C CD  . GLN   A 1 273 ? 34.566  -16.106 0.568   1.00 57.04 ? 272 GLN   A CD  1 
ATOM   2106 O OE1 . GLN   A 1 273 ? 34.089  -16.475 -0.516  1.00 60.78 ? 272 GLN   A OE1 1 
ATOM   2107 N NE2 . GLN   A 1 273 ? 35.761  -15.541 0.630   1.00 57.32 ? 272 GLN   A NE2 1 
ATOM   2108 N N   . LEU   A 1 274 ? 31.009  -13.675 3.128   1.00 36.03 ? 273 LEU   A N   1 
ATOM   2109 C CA  . LEU   A 1 274 ? 31.297  -12.269 3.475   1.00 34.51 ? 273 LEU   A CA  1 
ATOM   2110 C C   . LEU   A 1 274 ? 31.134  -11.972 4.966   1.00 35.21 ? 273 LEU   A C   1 
ATOM   2111 O O   . LEU   A 1 274 ? 31.940  -11.236 5.541   1.00 35.76 ? 273 LEU   A O   1 
ATOM   2112 C CB  . LEU   A 1 274 ? 30.413  -11.298 2.677   1.00 33.63 ? 273 LEU   A CB  1 
ATOM   2113 C CG  . LEU   A 1 274 ? 30.821  -9.819  2.879   1.00 33.48 ? 273 LEU   A CG  1 
ATOM   2114 C CD1 . LEU   A 1 274 ? 32.145  -9.523  2.157   1.00 34.93 ? 273 LEU   A CD1 1 
ATOM   2115 C CD2 . LEU   A 1 274 ? 29.722  -8.865  2.414   1.00 32.44 ? 273 LEU   A CD2 1 
ATOM   2116 N N   . VAL   A 1 275 ? 30.083  -12.515 5.589   1.00 35.07 ? 274 VAL   A N   1 
ATOM   2117 C CA  . VAL   A 1 275 ? 29.817  -12.205 6.990   1.00 35.78 ? 274 VAL   A CA  1 
ATOM   2118 C C   . VAL   A 1 275 ? 30.255  -13.249 7.968   1.00 38.23 ? 274 VAL   A C   1 
ATOM   2119 O O   . VAL   A 1 275 ? 30.118  -13.040 9.171   1.00 39.03 ? 274 VAL   A O   1 
ATOM   2120 C CB  . VAL   A 1 275 ? 28.345  -11.878 7.164   1.00 36.09 ? 274 VAL   A CB  1 
ATOM   2121 C CG1 . VAL   A 1 275 ? 27.982  -10.645 6.318   1.00 36.12 ? 274 VAL   A CG1 1 
ATOM   2122 C CG2 . VAL   A 1 275 ? 27.508  -13.103 6.773   1.00 36.17 ? 274 VAL   A CG2 1 
ATOM   2123 N N   . SER   A 1 276 ? 30.724  -14.402 7.486   1.00 39.40 ? 275 SER   A N   1 
ATOM   2124 C CA  . SER   A 1 276 ? 31.245  -15.457 8.346   1.00 40.69 ? 275 SER   A CA  1 
ATOM   2125 C C   . SER   A 1 276 ? 32.780  -15.482 8.354   1.00 41.44 ? 275 SER   A C   1 
ATOM   2126 O O   . SER   A 1 276 ? 33.358  -16.369 8.968   1.00 42.96 ? 275 SER   A O   1 
ATOM   2127 C CB  . SER   A 1 276 ? 30.675  -16.812 7.937   1.00 42.28 ? 275 SER   A CB  1 
ATOM   2128 O OG  . SER   A 1 276 ? 31.244  -17.234 6.710   1.00 44.76 ? 275 SER   A OG  1 
ATOM   2129 N N   . GLN   A 1 277 ? 33.450  -14.529 7.673   1.00 40.77 ? 276 GLN   A N   1 
ATOM   2130 C CA  . GLN   A 1 277 ? 34.905  -14.457 7.607   1.00 41.26 ? 276 GLN   A CA  1 
ATOM   2131 C C   . GLN   A 1 277 ? 35.528  -14.081 8.961   1.00 42.26 ? 276 GLN   A C   1 
ATOM   2132 O O   . GLN   A 1 277 ? 34.873  -13.439 9.788   1.00 41.88 ? 276 GLN   A O   1 
ATOM   2133 C CB  . GLN   A 1 277 ? 35.357  -13.499 6.476   1.00 40.41 ? 276 GLN   A CB  1 
ATOM   2134 C CG  . GLN   A 1 277 ? 34.970  -12.048 6.674   1.00 39.28 ? 276 GLN   A CG  1 
ATOM   2135 C CD  . GLN   A 1 277 ? 35.455  -11.183 5.529   1.00 40.84 ? 276 GLN   A CD  1 
ATOM   2136 O OE1 . GLN   A 1 277 ? 34.684  -10.447 4.893   1.00 41.64 ? 276 GLN   A OE1 1 
ATOM   2137 N NE2 . GLN   A 1 277 ? 36.742  -11.215 5.251   1.00 36.06 ? 276 GLN   A NE2 1 
ATOM   2138 N N   . PRO   A 1 278 ? 36.764  -14.536 9.234   1.00 43.56 ? 277 PRO   A N   1 
ATOM   2139 C CA  . PRO   A 1 278 ? 37.425  -14.129 10.492  1.00 44.30 ? 277 PRO   A CA  1 
ATOM   2140 C C   . PRO   A 1 278 ? 37.759  -12.624 10.581  1.00 44.59 ? 277 PRO   A C   1 
ATOM   2141 O O   . PRO   A 1 278 ? 37.866  -11.901 9.570   1.00 44.16 ? 277 PRO   A O   1 
ATOM   2142 C CB  . PRO   A 1 278 ? 38.742  -14.949 10.506  1.00 45.15 ? 277 PRO   A CB  1 
ATOM   2143 C CG  . PRO   A 1 278 ? 38.698  -15.855 9.304   1.00 45.58 ? 277 PRO   A CG  1 
ATOM   2144 C CD  . PRO   A 1 278 ? 37.681  -15.296 8.354   1.00 43.86 ? 277 PRO   A CD  1 
ATOM   2145 N N   . GLY   A 1 279 ? 37.977  -12.176 11.810  1.00 44.50 ? 278 GLY   A N   1 
ATOM   2146 C CA  . GLY   A 1 279 ? 38.378  -10.809 12.092  1.00 43.90 ? 278 GLY   A CA  1 
ATOM   2147 C C   . GLY   A 1 279 ? 37.280  -9.772  12.040  1.00 43.40 ? 278 GLY   A C   1 
ATOM   2148 O O   . GLY   A 1 279 ? 37.585  -8.582  11.983  1.00 43.79 ? 278 GLY   A O   1 
ATOM   2149 N N   . LEU   A 1 280 ? 35.999  -10.195 12.068  1.00 41.88 ? 279 LEU   A N   1 
ATOM   2150 C CA  . LEU   A 1 280 ? 34.893  -9.227  12.073  1.00 41.56 ? 279 LEU   A CA  1 
ATOM   2151 C C   . LEU   A 1 280 ? 34.528  -9.005  13.545  1.00 42.55 ? 279 LEU   A C   1 
ATOM   2152 O O   . LEU   A 1 280 ? 34.169  -9.957  14.242  1.00 43.13 ? 279 LEU   A O   1 
ATOM   2153 C CB  . LEU   A 1 280 ? 33.672  -9.761  11.296  1.00 39.73 ? 279 LEU   A CB  1 
ATOM   2154 C CG  . LEU   A 1 280 ? 33.842  -10.046 9.800   1.00 39.48 ? 279 LEU   A CG  1 
ATOM   2155 C CD1 . LEU   A 1 280 ? 32.482  -10.236 9.119   1.00 38.42 ? 279 LEU   A CD1 1 
ATOM   2156 C CD2 . LEU   A 1 280 ? 34.506  -8.899  9.071   1.00 39.70 ? 279 LEU   A CD2 1 
ATOM   2157 N N   . ASN   A 1 281 ? 34.723  -7.793  14.041  1.00 41.79 ? 280 ASN   A N   1 
ATOM   2158 C CA  . ASN   A 1 281 ? 34.468  -7.452  15.443  1.00 41.91 ? 280 ASN   A CA  1 
ATOM   2159 C C   . ASN   A 1 281 ? 34.315  -5.936  15.604  1.00 42.02 ? 280 ASN   A C   1 
ATOM   2160 O O   . ASN   A 1 281 ? 34.609  -5.192  14.671  1.00 41.90 ? 280 ASN   A O   1 
ATOM   2161 C CB  . ASN   A 1 281 ? 35.548  -8.032  16.379  1.00 43.44 ? 280 ASN   A CB  1 
ATOM   2162 C CG  . ASN   A 1 281 ? 36.951  -7.560  16.062  1.00 47.49 ? 280 ASN   A CG  1 
ATOM   2163 O OD1 . ASN   A 1 281 ? 37.269  -6.364  16.136  1.00 48.37 ? 280 ASN   A OD1 1 
ATOM   2164 N ND2 . ASN   A 1 281 ? 37.823  -8.496  15.712  1.00 47.98 ? 280 ASN   A ND2 1 
ATOM   2165 N N   . ARG   A 1 282 ? 33.848  -5.473  16.774  1.00 41.90 ? 281 ARG   A N   1 
ATOM   2166 C CA  . ARG   A 1 282 ? 33.616  -4.051  17.044  1.00 41.82 ? 281 ARG   A CA  1 
ATOM   2167 C C   . ARG   A 1 282 ? 34.821  -3.142  16.821  1.00 41.79 ? 281 ARG   A C   1 
ATOM   2168 O O   . ARG   A 1 282 ? 34.639  -1.934  16.622  1.00 41.44 ? 281 ARG   A O   1 
ATOM   2169 C CB  . ARG   A 1 282 ? 33.062  -3.850  18.458  1.00 43.35 ? 281 ARG   A CB  1 
ATOM   2170 C CG  . ARG   A 1 282 ? 34.004  -4.350  19.546  1.00 45.50 ? 281 ARG   A CG  1 
ATOM   2171 C CD  . ARG   A 1 282 ? 33.345  -4.294  20.904  1.00 47.31 ? 281 ARG   A CD  1 
ATOM   2172 N NE  . ARG   A 1 282 ? 34.342  -4.435  21.961  1.00 51.15 ? 281 ARG   A NE  1 
ATOM   2173 C CZ  . ARG   A 1 282 ? 34.995  -3.423  22.520  1.00 54.06 ? 281 ARG   A CZ  1 
ATOM   2174 N NH1 . ARG   A 1 282 ? 35.908  -3.652  23.460  1.00 54.70 ? 281 ARG   A NH1 1 
ATOM   2175 N NH2 . ARG   A 1 282 ? 34.754  -2.174  22.134  1.00 54.22 ? 281 ARG   A NH2 1 
ATOM   2176 N N   . GLY   A 1 283 ? 36.031  -3.718  16.830  1.00 41.90 ? 282 GLY   A N   1 
ATOM   2177 C CA  . GLY   A 1 283 ? 37.267  -2.969  16.591  1.00 42.31 ? 282 GLY   A CA  1 
ATOM   2178 C C   . GLY   A 1 283 ? 37.255  -2.284  15.237  1.00 41.67 ? 282 GLY   A C   1 
ATOM   2179 O O   . GLY   A 1 283 ? 37.817  -1.205  15.094  1.00 41.39 ? 282 GLY   A O   1 
ATOM   2180 N N   . LEU   A 1 284 ? 36.588  -2.892  14.241  1.00 40.94 ? 283 LEU   A N   1 
ATOM   2181 C CA  . LEU   A 1 284 ? 36.440  -2.324  12.897  1.00 40.74 ? 283 LEU   A CA  1 
ATOM   2182 C C   . LEU   A 1 284 ? 35.645  -1.007  12.969  1.00 40.97 ? 283 LEU   A C   1 
ATOM   2183 O O   . LEU   A 1 284 ? 35.978  -0.041  12.283  1.00 41.24 ? 283 LEU   A O   1 
ATOM   2184 C CB  . LEU   A 1 284 ? 35.688  -3.321  11.977  1.00 39.58 ? 283 LEU   A CB  1 
ATOM   2185 C CG  . LEU   A 1 284 ? 36.413  -4.623  11.682  1.00 40.22 ? 283 LEU   A CG  1 
ATOM   2186 C CD1 . LEU   A 1 284 ? 35.511  -5.593  10.942  1.00 38.81 ? 283 LEU   A CD1 1 
ATOM   2187 C CD2 . LEU   A 1 284 ? 37.699  -4.358  10.905  1.00 42.00 ? 283 LEU   A CD2 1 
ATOM   2188 N N   . ILE   A 1 285 ? 34.615  -0.967  13.816  1.00 40.92 ? 284 ILE   A N   1 
ATOM   2189 C CA  . ILE   A 1 285 ? 33.790  0.227   13.995  1.00 40.76 ? 284 ILE   A CA  1 
ATOM   2190 C C   . ILE   A 1 285 ? 34.490  1.230   14.895  1.00 41.39 ? 284 ILE   A C   1 
ATOM   2191 O O   . ILE   A 1 285 ? 34.372  2.421   14.644  1.00 41.13 ? 284 ILE   A O   1 
ATOM   2192 C CB  . ILE   A 1 285 ? 32.340  -0.104  14.426  1.00 41.53 ? 284 ILE   A CB  1 
ATOM   2193 C CG1 . ILE   A 1 285 ? 31.702  -1.038  13.378  1.00 41.96 ? 284 ILE   A CG1 1 
ATOM   2194 C CG2 . ILE   A 1 285 ? 31.502  1.178   14.556  1.00 41.99 ? 284 ILE   A CG2 1 
ATOM   2195 C CD1 . ILE   A 1 285 ? 31.616  -0.415  11.918  1.00 42.99 ? 284 ILE   A CD1 1 
ATOM   2196 N N   . LEU   A 1 286 ? 35.331  0.783   15.847  1.00 42.48 ? 285 LEU   A N   1 
ATOM   2197 C CA  . LEU   A 1 286 ? 36.151  1.692   16.657  1.00 44.56 ? 285 LEU   A CA  1 
ATOM   2198 C C   . LEU   A 1 286 ? 37.117  2.450   15.716  1.00 46.02 ? 285 LEU   A C   1 
ATOM   2199 O O   . LEU   A 1 286 ? 37.253  3.665   15.850  1.00 46.44 ? 285 LEU   A O   1 
ATOM   2200 C CB  . LEU   A 1 286 ? 36.952  0.911   17.721  1.00 45.19 ? 285 LEU   A CB  1 
ATOM   2201 C CG  . LEU   A 1 286 ? 36.122  0.342   18.888  1.00 47.80 ? 285 LEU   A CG  1 
ATOM   2202 C CD1 . LEU   A 1 286 ? 37.013  -0.414  19.888  1.00 48.65 ? 285 LEU   A CD1 1 
ATOM   2203 C CD2 . LEU   A 1 286 ? 35.401  1.457   19.631  1.00 48.86 ? 285 LEU   A CD2 1 
ATOM   2204 N N   . ASP   A 1 287 ? 37.695  1.747   14.698  1.00 46.12 ? 286 ASP   A N   1 
ATOM   2205 C CA  . ASP   A 1 287 ? 38.563  2.394   13.704  1.00 46.94 ? 286 ASP   A CA  1 
ATOM   2206 C C   . ASP   A 1 287 ? 37.752  3.405   12.895  1.00 47.02 ? 286 ASP   A C   1 
ATOM   2207 O O   . ASP   A 1 287 ? 38.218  4.523   12.661  1.00 48.46 ? 286 ASP   A O   1 
ATOM   2208 C CB  . ASP   A 1 287 ? 39.192  1.375   12.747  1.00 49.18 ? 286 ASP   A CB  1 
ATOM   2209 C CG  . ASP   A 1 287 ? 39.905  0.233   13.441  1.00 54.47 ? 286 ASP   A CG  1 
ATOM   2210 O OD1 . ASP   A 1 287 ? 40.546  0.478   14.475  1.00 54.82 ? 286 ASP   A OD1 1 
ATOM   2211 O OD2 . ASP   A 1 287 ? 39.786  -0.925  12.961  1.00 57.93 ? 286 ASP   A OD2 1 
ATOM   2212 N N   . LEU   A 1 288 ? 36.520  3.040   12.510  1.00 45.17 ? 287 LEU   A N   1 
ATOM   2213 C CA  . LEU   A 1 288 ? 35.647  3.954   11.774  1.00 44.30 ? 287 LEU   A CA  1 
ATOM   2214 C C   . LEU   A 1 288 ? 35.334  5.223   12.603  1.00 45.00 ? 287 LEU   A C   1 
ATOM   2215 O O   . LEU   A 1 288 ? 35.385  6.329   12.061  1.00 45.67 ? 287 LEU   A O   1 
ATOM   2216 C CB  . LEU   A 1 288 ? 34.344  3.225   11.383  1.00 43.06 ? 287 LEU   A CB  1 
ATOM   2217 C CG  . LEU   A 1 288 ? 33.343  4.053   10.596  1.00 43.30 ? 287 LEU   A CG  1 
ATOM   2218 C CD1 . LEU   A 1 288 ? 33.905  4.470   9.255   1.00 43.67 ? 287 LEU   A CD1 1 
ATOM   2219 C CD2 . LEU   A 1 288 ? 32.008  3.312   10.443  1.00 42.14 ? 287 LEU   A CD2 1 
ATOM   2220 N N   . LEU   A 1 289 ? 35.058  5.072   13.916  1.00 45.38 ? 288 LEU   A N   1 
ATOM   2221 C CA  . LEU   A 1 289 ? 34.741  6.204   14.799  1.00 47.37 ? 288 LEU   A CA  1 
ATOM   2222 C C   . LEU   A 1 289 ? 35.945  7.092   15.035  1.00 50.92 ? 288 LEU   A C   1 
ATOM   2223 O O   . LEU   A 1 289 ? 35.774  8.287   15.291  1.00 52.04 ? 288 LEU   A O   1 
ATOM   2224 C CB  . LEU   A 1 289 ? 34.144  5.748   16.141  1.00 46.88 ? 288 LEU   A CB  1 
ATOM   2225 C CG  . LEU   A 1 289 ? 32.859  4.907   16.042  1.00 47.81 ? 288 LEU   A CG  1 
ATOM   2226 C CD1 . LEU   A 1 289 ? 32.500  4.296   17.384  1.00 48.54 ? 288 LEU   A CD1 1 
ATOM   2227 C CD2 . LEU   A 1 289 ? 31.708  5.711   15.483  1.00 47.57 ? 288 LEU   A CD2 1 
ATOM   2228 N N   . ASP   A 1 290 ? 37.167  6.535   14.938  1.00 52.80 ? 289 ASP   A N   1 
ATOM   2229 C CA  . ASP   A 1 290 ? 38.394  7.320   15.061  1.00 55.26 ? 289 ASP   A CA  1 
ATOM   2230 C C   . ASP   A 1 290 ? 38.472  8.345   13.917  1.00 56.65 ? 289 ASP   A C   1 
ATOM   2231 O O   . ASP   A 1 290 ? 38.984  9.429   14.128  1.00 56.90 ? 289 ASP   A O   1 
ATOM   2232 C CB  . ASP   A 1 290 ? 39.623  6.394   15.044  1.00 59.19 ? 289 ASP   A CB  1 
ATOM   2233 C CG  . ASP   A 1 290 ? 40.065  5.913   16.413  1.00 68.02 ? 289 ASP   A CG  1 
ATOM   2234 O OD1 . ASP   A 1 290 ? 39.978  6.706   17.377  1.00 69.72 ? 289 ASP   A OD1 1 
ATOM   2235 O OD2 . ASP   A 1 290 ? 40.529  4.750   16.515  1.00 71.98 ? 289 ASP   A OD2 1 
ATOM   2236 N N   . LYS   A 1 291 ? 37.943  8.026   12.720  1.00 58.14 ? 290 LYS   A N   1 
ATOM   2237 C CA  . LYS   A 1 291 ? 37.903  8.961   11.593  1.00 60.77 ? 290 LYS   A CA  1 
ATOM   2238 C C   . LYS   A 1 291 ? 37.050  10.198  11.868  1.00 64.27 ? 290 LYS   A C   1 
ATOM   2239 O O   . LYS   A 1 291 ? 37.182  11.193  11.149  1.00 64.46 ? 290 LYS   A O   1 
ATOM   2240 C CB  . LYS   A 1 291 ? 37.363  8.295   10.332  1.00 62.21 ? 290 LYS   A CB  1 
ATOM   2241 C CG  . LYS   A 1 291 ? 38.314  7.336   9.661   1.00 66.06 ? 290 LYS   A CG  1 
ATOM   2242 C CD  . LYS   A 1 291 ? 37.753  6.920   8.312   1.00 70.23 ? 290 LYS   A CD  1 
ATOM   2243 C CE  . LYS   A 1 291 ? 37.743  8.076   7.343   1.00 74.33 ? 290 LYS   A CE  1 
ATOM   2244 N NZ  . LYS   A 1 291 ? 37.335  7.650   5.985   1.00 77.63 ? 290 LYS   A NZ  1 
ATOM   2245 N N   . LEU   A 1 292 ? 36.131  10.135  12.849  1.00 66.60 ? 291 LEU   A N   1 
ATOM   2246 C CA  . LEU   A 1 292 ? 35.308  11.302  13.201  1.00 69.33 ? 291 LEU   A CA  1 
ATOM   2247 C C   . LEU   A 1 292 ? 36.155  12.418  13.810  1.00 73.09 ? 291 LEU   A C   1 
ATOM   2248 O O   . LEU   A 1 292 ? 35.778  13.585  13.696  1.00 73.81 ? 291 LEU   A O   1 
ATOM   2249 C CB  . LEU   A 1 292 ? 34.198  10.909  14.172  1.00 69.04 ? 291 LEU   A CB  1 
ATOM   2250 C CG  . LEU   A 1 292 ? 33.258  9.841   13.645  1.00 69.42 ? 291 LEU   A CG  1 
ATOM   2251 C CD1 . LEU   A 1 292 ? 32.359  9.323   14.737  1.00 69.82 ? 291 LEU   A CD1 1 
ATOM   2252 C CD2 . LEU   A 1 292 ? 32.435  10.379  12.504  1.00 69.86 ? 291 LEU   A CD2 1 
ATOM   2253 N N   . LYS   A 1 293 ? 37.294  12.062  14.460  1.00 75.28 ? 292 LYS   A N   1 
ATOM   2254 C CA  . LYS   A 1 293 ? 38.226  13.012  15.058  1.00 78.10 ? 292 LYS   A CA  1 
ATOM   2255 C C   . LYS   A 1 293 ? 38.970  13.796  13.976  1.00 80.81 ? 292 LYS   A C   1 
ATOM   2256 O O   . LYS   A 1 293 ? 39.282  14.971  14.180  1.00 81.64 ? 292 LYS   A O   1 
ATOM   2257 C CB  . LYS   A 1 293 ? 39.231  12.285  15.960  1.00 80.40 ? 292 LYS   A CB  1 
ATOM   2258 C CG  . LYS   A 1 293 ? 38.576  11.365  16.988  1.00 85.12 ? 292 LYS   A CG  1 
ATOM   2259 C CD  . LYS   A 1 293 ? 39.627  10.602  17.781  1.00 89.59 ? 292 LYS   A CD  1 
ATOM   2260 C CE  . LYS   A 1 293 ? 39.032  9.666   18.805  1.00 93.28 ? 292 LYS   A CE  1 
ATOM   2261 N NZ  . LYS   A 1 293 ? 40.088  8.873   19.493  1.00 95.60 ? 292 LYS   A NZ  1 
ATOM   2262 N N   . ASN   A 1 294 ? 39.270  13.153  12.829  1.00 82.03 ? 293 ASN   A N   1 
ATOM   2263 C CA  . ASN   A 1 294 ? 39.955  13.836  11.735  1.00 83.67 ? 293 ASN   A CA  1 
ATOM   2264 C C   . ASN   A 1 294 ? 38.967  14.437  10.726  1.00 84.76 ? 293 ASN   A C   1 
ATOM   2265 O O   . ASN   A 1 294 ? 38.910  15.656  10.566  1.00 85.34 ? 293 ASN   A O   1 
ATOM   2266 C CB  . ASN   A 1 294 ? 41.016  12.940  11.062  1.00 85.14 ? 293 ASN   A CB  1 
ATOM   2267 C CG  . ASN   A 1 294 ? 40.512  11.668  10.407  1.00 88.33 ? 293 ASN   A CG  1 
ATOM   2268 O OD1 . ASN   A 1 294 ? 41.032  10.568  10.649  1.00 89.35 ? 293 ASN   A OD1 1 
ATOM   2269 N ND2 . ASN   A 1 294 ? 39.515  11.780  9.540   1.00 88.79 ? 293 ASN   A ND2 1 
HETATM 2270 C C1  . A1ITA B 2 .   ? 17.605  8.028   17.242  1.00 39.35 ? 301 A1ITA A C1  1 
HETATM 2271 C C2  . A1ITA B 2 .   ? 17.090  6.835   17.829  1.00 38.47 ? 301 A1ITA A C2  1 
HETATM 2272 C C3  . A1ITA B 2 .   ? 18.843  6.817   19.297  1.00 41.10 ? 301 A1ITA A C3  1 
HETATM 2273 N N6  . A1ITA B 2 .   ? 13.882  4.822   17.906  1.00 37.08 ? 301 A1ITA A N6  1 
HETATM 2274 C C7  . A1ITA B 2 .   ? 22.116  10.928  16.849  1.00 46.50 ? 301 A1ITA A C7  1 
HETATM 2275 C C8  . A1ITA B 2 .   ? 23.328  11.170  17.487  1.00 47.87 ? 301 A1ITA A C8  1 
HETATM 2276 C C9  . A1ITA B 2 .   ? 23.579  10.530  18.697  1.00 46.53 ? 301 A1ITA A C9  1 
HETATM 2277 C C10 . A1ITA B 2 .   ? 22.646  9.675   19.254  1.00 45.46 ? 301 A1ITA A C10 1 
HETATM 2278 C C11 . A1ITA B 2 .   ? 25.336  12.635  17.745  1.00 52.47 ? 301 A1ITA A C11 1 
HETATM 2279 C C12 . A1ITA B 2 .   ? 25.859  13.903  17.090  1.00 53.58 ? 301 A1ITA A C12 1 
HETATM 2280 C C13 . A1ITA B 2 .   ? 25.141  13.191  14.958  1.00 52.62 ? 301 A1ITA A C13 1 
HETATM 2281 C C14 . A1ITA B 2 .   ? 24.631  11.880  15.507  1.00 51.78 ? 301 A1ITA A C14 1 
HETATM 2282 C C15 . A1ITA B 2 .   ? 19.518  6.133   20.462  1.00 41.14 ? 301 A1ITA A C15 1 
HETATM 2283 C C16 . A1ITA B 2 .   ? 15.880  6.094   17.366  1.00 36.57 ? 301 A1ITA A C16 1 
HETATM 2284 C C19 . A1ITA B 2 .   ? 14.528  5.094   15.647  1.00 35.88 ? 301 A1ITA A C19 1 
HETATM 2285 C C20 . A1ITA B 2 .   ? 15.656  5.836   15.995  1.00 35.39 ? 301 A1ITA A C20 1 
HETATM 2286 C C21 . A1ITA B 2 .   ? 15.661  5.703   13.876  1.00 34.45 ? 301 A1ITA A C21 1 
HETATM 2287 C C22 . A1ITA B 2 .   ? 13.574  4.341   13.432  1.00 34.89 ? 301 A1ITA A C22 1 
HETATM 2288 O O1  . A1ITA B 2 .   ? 20.581  6.573   20.941  1.00 41.43 ? 301 A1ITA A O1  1 
HETATM 2289 N N5  . A1ITA B 2 .   ? 18.902  5.054   20.945  1.00 40.93 ? 301 A1ITA A N5  1 
HETATM 2290 N N1  . A1ITA B 2 .   ? 17.723  6.230   18.844  1.00 39.76 ? 301 A1ITA A N1  1 
HETATM 2291 N N7  . A1ITA B 2 .   ? 16.361  6.213   14.859  1.00 34.02 ? 301 A1ITA A N7  1 
HETATM 2292 N N8  . A1ITA B 2 .   ? 14.553  5.022   14.271  1.00 35.72 ? 301 A1ITA A N8  1 
HETATM 2293 C C18 . A1ITA B 2 .   ? 13.666  4.605   16.603  1.00 36.42 ? 301 A1ITA A C18 1 
HETATM 2294 C C17 . A1ITA B 2 .   ? 14.963  5.536   18.257  1.00 36.93 ? 301 A1ITA A C17 1 
HETATM 2295 C C4  . A1ITA B 2 .   ? 19.342  8.008   18.718  1.00 41.83 ? 301 A1ITA A C4  1 
HETATM 2296 N N2  . A1ITA B 2 .   ? 18.723  8.614   17.693  1.00 40.71 ? 301 A1ITA A N2  1 
HETATM 2297 N N   . A1ITA B 2 .   ? 16.979  8.625   16.220  1.00 39.07 ? 301 A1ITA A N   1 
HETATM 2298 C C   . A1ITA B 2 .   ? 17.061  10.053  15.981  1.00 39.05 ? 301 A1ITA A C   1 
HETATM 2299 N N3  . A1ITA B 2 .   ? 20.494  8.557   19.211  1.00 43.45 ? 301 A1ITA A N3  1 
HETATM 2300 C C5  . A1ITA B 2 .   ? 21.438  9.435   18.612  1.00 44.71 ? 301 A1ITA A C5  1 
HETATM 2301 C C6  . A1ITA B 2 .   ? 21.183  10.071  17.402  1.00 45.47 ? 301 A1ITA A C6  1 
HETATM 2302 N N4  . A1ITA B 2 .   ? 24.273  12.041  16.919  1.00 50.70 ? 301 A1ITA A N4  1 
HETATM 2303 O O   . A1ITA B 2 .   ? 26.249  13.668  15.724  1.00 53.92 ? 301 A1ITA A O   1 
HETATM 2304 O O   . HOH   C 3 .   ? 21.955  12.084  -4.339  1.00 44.18 ? 401 HOH   A O   1 
HETATM 2305 O O   . HOH   C 3 .   ? 15.188  13.300  -8.243  1.00 35.91 ? 402 HOH   A O   1 
HETATM 2306 O O   . HOH   C 3 .   ? 38.733  -12.040 7.324   1.00 46.63 ? 403 HOH   A O   1 
HETATM 2307 O O   . HOH   C 3 .   ? 40.828  -3.121  13.255  1.00 58.33 ? 404 HOH   A O   1 
HETATM 2308 O O   . HOH   C 3 .   ? 21.950  11.575  9.386   1.00 61.60 ? 405 HOH   A O   1 
HETATM 2309 O O   . HOH   C 3 .   ? 12.858  -16.741 6.629   1.00 32.23 ? 406 HOH   A O   1 
HETATM 2310 O O   . HOH   C 3 .   ? 4.868   1.552   14.112  1.00 57.12 ? 407 HOH   A O   1 
HETATM 2311 O O   . HOH   C 3 .   ? 9.107   4.299   8.016   1.00 35.06 ? 408 HOH   A O   1 
HETATM 2312 O O   . HOH   C 3 .   ? 27.700  -5.516  17.650  1.00 34.71 ? 409 HOH   A O   1 
HETATM 2313 O O   . HOH   C 3 .   ? 30.575  1.117   -5.312  1.00 35.19 ? 410 HOH   A O   1 
HETATM 2314 O O   . HOH   C 3 .   ? 28.225  -9.343  18.213  1.00 48.52 ? 411 HOH   A O   1 
HETATM 2315 O O   . HOH   C 3 .   ? 26.410  -8.206  -7.375  1.00 36.07 ? 412 HOH   A O   1 
HETATM 2316 O O   . HOH   C 3 .   ? 8.873   -11.285 0.720   1.00 28.63 ? 413 HOH   A O   1 
HETATM 2317 O O   . HOH   C 3 .   ? 14.802  6.920   10.015  1.00 31.68 ? 414 HOH   A O   1 
HETATM 2318 O O   . HOH   C 3 .   ? 10.928  9.211   9.380   1.00 36.25 ? 415 HOH   A O   1 
HETATM 2319 O O   . HOH   C 3 .   ? 31.071  -12.469 -7.127  1.00 40.90 ? 416 HOH   A O   1 
HETATM 2320 O O   . HOH   C 3 .   ? 1.876   -6.949  -4.537  1.00 38.30 ? 417 HOH   A O   1 
HETATM 2321 O O   . HOH   C 3 .   ? 12.292  -4.441  22.222  1.00 45.13 ? 418 HOH   A O   1 
HETATM 2322 O O   . HOH   C 3 .   ? 24.559  -10.751 18.648  1.00 54.48 ? 419 HOH   A O   1 
HETATM 2323 O O   . HOH   C 3 .   ? 12.437  -13.709 22.898  1.00 58.39 ? 420 HOH   A O   1 
HETATM 2324 O O   . HOH   C 3 .   ? 12.655  2.417   1.396   1.00 26.44 ? 421 HOH   A O   1 
HETATM 2325 O O   . HOH   C 3 .   ? 10.178  -17.466 -8.094  1.00 46.35 ? 422 HOH   A O   1 
HETATM 2326 O O   . HOH   C 3 .   ? 10.016  2.737   17.386  1.00 44.53 ? 423 HOH   A O   1 
HETATM 2327 O O   . HOH   C 3 .   ? 15.182  -16.701 11.945  1.00 30.38 ? 424 HOH   A O   1 
HETATM 2328 O O   . HOH   C 3 .   ? 35.326  2.359   1.246   1.00 53.27 ? 425 HOH   A O   1 
HETATM 2329 O O   . HOH   C 3 .   ? 26.901  -14.813 13.558  1.00 43.73 ? 426 HOH   A O   1 
HETATM 2330 O O   . HOH   C 3 .   ? 24.809  1.121   -7.085  1.00 34.03 ? 427 HOH   A O   1 
HETATM 2331 O O   . HOH   C 3 .   ? 24.208  4.045   -4.610  1.00 35.46 ? 428 HOH   A O   1 
HETATM 2332 O O   . HOH   C 3 .   ? 25.964  -21.174 3.616   1.00 42.91 ? 429 HOH   A O   1 
HETATM 2333 O O   . HOH   C 3 .   ? 20.388  9.289   10.641  1.00 39.35 ? 430 HOH   A O   1 
HETATM 2334 O O   . HOH   C 3 .   ? 17.346  1.121   -4.517  1.00 36.74 ? 431 HOH   A O   1 
HETATM 2335 O O   . HOH   C 3 .   ? 14.839  -14.904 7.683   1.00 24.51 ? 432 HOH   A O   1 
HETATM 2336 O O   . HOH   C 3 .   ? 30.375  -6.721  18.704  1.00 50.15 ? 433 HOH   A O   1 
HETATM 2337 O O   . HOH   C 3 .   ? 15.136  -1.398  -3.203  1.00 25.21 ? 434 HOH   A O   1 
HETATM 2338 O O   . HOH   C 3 .   ? 8.472   -4.701  12.875  1.00 36.79 ? 435 HOH   A O   1 
HETATM 2339 O O   . HOH   C 3 .   ? 0.151   -5.843  -1.246  1.00 46.32 ? 436 HOH   A O   1 
HETATM 2340 O O   . HOH   C 3 .   ? 20.389  -10.400 -7.807  1.00 48.37 ? 437 HOH   A O   1 
HETATM 2341 O O   . HOH   C 3 .   ? 21.338  13.287  12.399  1.00 44.20 ? 438 HOH   A O   1 
HETATM 2342 O O   . HOH   C 3 .   ? 19.276  12.355  13.904  1.00 34.27 ? 439 HOH   A O   1 
HETATM 2343 O O   . HOH   C 3 .   ? 4.801   4.365   -10.110 1.00 57.39 ? 440 HOH   A O   1 
HETATM 2344 O O   . HOH   C 3 .   ? 28.025  -15.190 10.851  1.00 40.08 ? 441 HOH   A O   1 
HETATM 2345 O O   . HOH   C 3 .   ? 13.682  1.023   12.317  1.00 38.83 ? 442 HOH   A O   1 
HETATM 2346 O O   . HOH   C 3 .   ? 12.710  4.937   7.880   1.00 35.37 ? 443 HOH   A O   1 
HETATM 2347 O O   . HOH   C 3 .   ? 20.098  9.909   13.703  1.00 33.73 ? 444 HOH   A O   1 
HETATM 2348 O O   . HOH   C 3 .   ? 18.418  7.560   13.582  1.00 33.67 ? 445 HOH   A O   1 
HETATM 2349 O O   . HOH   C 3 .   ? 40.039  -4.077  -3.627  1.00 41.04 ? 446 HOH   A O   1 
HETATM 2350 O O   . HOH   C 3 .   ? 20.050  -14.335 15.935  1.00 35.75 ? 447 HOH   A O   1 
HETATM 2351 O O   . HOH   C 3 .   ? 35.804  -8.518  3.015   1.00 42.65 ? 448 HOH   A O   1 
HETATM 2352 O O   . HOH   C 3 .   ? 23.262  -7.593  -7.633  1.00 42.62 ? 449 HOH   A O   1 
HETATM 2353 O O   . HOH   C 3 .   ? 14.461  -0.226  20.619  1.00 48.84 ? 450 HOH   A O   1 
HETATM 2354 O O   . HOH   C 3 .   ? 32.002  -13.577 11.136  1.00 33.66 ? 451 HOH   A O   1 
HETATM 2355 O O   . HOH   C 3 .   ? 10.291  4.472   10.159  1.00 40.92 ? 452 HOH   A O   1 
HETATM 2356 O O   . HOH   C 3 .   ? 10.208  1.693   6.035   1.00 33.95 ? 453 HOH   A O   1 
HETATM 2357 O O   . HOH   C 3 .   ? 4.515   -0.101  -7.508  1.00 46.18 ? 454 HOH   A O   1 
HETATM 2358 O O   . HOH   C 3 .   ? 3.310   -13.283 4.570   1.00 40.69 ? 455 HOH   A O   1 
HETATM 2359 O O   . HOH   C 3 .   ? 6.696   -16.391 6.303   1.00 47.14 ? 456 HOH   A O   1 
HETATM 2360 O O   . HOH   C 3 .   ? 28.595  -12.896 16.292  1.00 63.63 ? 457 HOH   A O   1 
HETATM 2361 O O   . HOH   C 3 .   ? 19.722  5.754   5.748   1.00 26.45 ? 458 HOH   A O   1 
HETATM 2362 O O   . HOH   C 3 .   ? 3.596   -3.262  0.287   1.00 38.28 ? 459 HOH   A O   1 
HETATM 2363 O O   . HOH   C 3 .   ? 25.463  10.828  1.816   1.00 37.84 ? 460 HOH   A O   1 
HETATM 2364 O O   . HOH   C 3 .   ? 15.977  -20.165 7.611   1.00 53.21 ? 461 HOH   A O   1 
HETATM 2365 O O   . HOH   C 3 .   ? 23.360  5.739   -6.613  1.00 51.18 ? 462 HOH   A O   1 
HETATM 2366 O O   . HOH   C 3 .   ? 17.030  -5.603  22.740  1.00 41.92 ? 463 HOH   A O   1 
HETATM 2367 O O   . HOH   C 3 .   ? 15.318  7.661   7.382   1.00 36.22 ? 464 HOH   A O   1 
HETATM 2368 O O   . HOH   C 3 .   ? 37.255  -4.246  -0.784  1.00 36.07 ? 465 HOH   A O   1 
HETATM 2369 O O   . HOH   C 3 .   ? 24.289  -22.919 -0.030  1.00 38.66 ? 466 HOH   A O   1 
HETATM 2370 O O   . HOH   C 3 .   ? -0.000  -3.560  0.000   0.50 58.56 ? 467 HOH   A O   1 
HETATM 2371 O O   . HOH   C 3 .   ? -2.834  -7.006  -8.025  1.00 34.90 ? 468 HOH   A O   1 
HETATM 2372 O O   . HOH   C 3 .   ? 11.231  -21.407 -2.100  1.00 35.22 ? 469 HOH   A O   1 
HETATM 2373 O O   . HOH   C 3 .   ? 13.358  -3.705  5.634   1.00 24.79 ? 470 HOH   A O   1 
HETATM 2374 O O   . HOH   C 3 .   ? 15.714  -0.026  13.379  1.00 33.33 ? 471 HOH   A O   1 
HETATM 2375 O O   . HOH   C 3 .   ? 21.664  -7.178  -11.536 1.00 53.06 ? 472 HOH   A O   1 
HETATM 2376 O O   . HOH   C 3 .   ? 18.472  -0.725  -10.055 1.00 54.30 ? 473 HOH   A O   1 
HETATM 2377 O O   . HOH   C 3 .   ? 14.578  -18.403 2.036   1.00 40.77 ? 474 HOH   A O   1 
HETATM 2378 O O   . HOH   C 3 .   ? 12.622  -1.739  -14.528 1.00 48.43 ? 475 HOH   A O   1 
HETATM 2379 O O   . HOH   C 3 .   ? 25.278  5.985   30.154  1.00 76.02 ? 476 HOH   A O   1 
HETATM 2380 O O   . HOH   C 3 .   ? -2.014  4.042   15.810  1.00 53.61 ? 477 HOH   A O   1 
HETATM 2381 O O   . HOH   C 3 .   ? 25.709  -5.553  20.058  1.00 67.22 ? 478 HOH   A O   1 
HETATM 2382 O O   . HOH   C 3 .   ? 22.949  -1.118  -10.374 1.00 48.51 ? 479 HOH   A O   1 
HETATM 2383 O O   . HOH   C 3 .   ? 8.586   -18.078 5.548   1.00 67.19 ? 480 HOH   A O   1 
HETATM 2384 O O   . HOH   C 3 .   ? 27.232  5.126   23.563  1.00 47.19 ? 481 HOH   A O   1 
HETATM 2385 O O   . HOH   C 3 .   ? 21.181  -11.557 21.928  1.00 45.38 ? 482 HOH   A O   1 
HETATM 2386 O O   . HOH   C 3 .   ? 29.420  -17.613 0.415   1.00 46.55 ? 483 HOH   A O   1 
HETATM 2387 O O   . HOH   C 3 .   ? 21.971  14.648  16.612  1.00 52.82 ? 484 HOH   A O   1 
HETATM 2388 O O   . HOH   C 3 .   ? 21.260  -4.217  22.958  1.00 57.71 ? 485 HOH   A O   1 
HETATM 2389 O O   . HOH   C 3 .   ? 16.553  12.258  12.679  1.00 44.73 ? 486 HOH   A O   1 
HETATM 2390 O O   . HOH   C 3 .   ? 37.375  -2.380  1.141   1.00 32.94 ? 487 HOH   A O   1 
HETATM 2391 O O   . HOH   C 3 .   ? 16.402  -0.855  -5.716  1.00 39.00 ? 488 HOH   A O   1 
HETATM 2392 O O   . HOH   C 3 .   ? 13.258  11.086  9.590   1.00 49.45 ? 489 HOH   A O   1 
HETATM 2393 O O   . HOH   C 3 .   ? 27.598  -5.718  -7.345  1.00 32.27 ? 490 HOH   A O   1 
HETATM 2394 O O   . HOH   C 3 .   ? 5.639   -8.053  11.630  1.00 33.26 ? 491 HOH   A O   1 
HETATM 2395 O O   . HOH   C 3 .   ? 11.756  -4.511  1.962   1.00 23.79 ? 492 HOH   A O   1 
HETATM 2396 O O   . HOH   C 3 .   ? 7.699   2.152   5.378   1.00 27.95 ? 493 HOH   A O   1 
HETATM 2397 O O   . HOH   C 3 .   ? 17.201  -19.659 2.899   1.00 29.06 ? 494 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? 38.218  3.367   9.012   1.00 40.97 ? 495 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? 32.742  -10.130 17.043  1.00 51.06 ? 496 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? 1.445   -8.339  -6.690  1.00 47.80 ? 497 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? 14.891  -13.831 -8.935  1.00 34.48 ? 498 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? 3.973   -8.553  -4.122  1.00 54.68 ? 499 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? 5.696   -16.546 3.417   1.00 55.74 ? 500 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? 36.212  -12.728 -2.276  1.00 40.64 ? 501 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? 32.776  -7.703  18.524  1.00 54.15 ? 502 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? 17.305  -11.817 -9.364  1.00 43.07 ? 503 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? 33.710  7.943   0.169   1.00 41.30 ? 504 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? 3.084   -5.635  -0.869  1.00 50.33 ? 505 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? -0.131  7.857   11.097  1.00 47.15 ? 506 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? -1.596  5.868   12.612  1.00 53.99 ? 507 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? 38.562  -9.447  3.301   1.00 39.29 ? 508 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? 15.958  -16.595 9.388   1.00 32.42 ? 509 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? 13.610  10.998  -11.778 1.00 44.77 ? 510 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? 6.573   12.747  17.729  1.00 57.53 ? 511 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? 11.786  6.763   9.923   1.00 42.92 ? 512 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? 17.329  9.433   6.878   1.00 56.16 ? 513 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? 31.947  3.630   -4.738  1.00 42.01 ? 514 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? 15.847  8.936   11.100  1.00 51.42 ? 515 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? 28.369  -12.938 -7.923  1.00 45.02 ? 516 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 12.615  -17.652 11.130  1.00 49.24 ? 517 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 25.031  12.649  -5.028  1.00 44.32 ? 518 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? 12.276  2.807   3.862   1.00 40.07 ? 519 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? 18.709  10.458  9.270   1.00 49.00 ? 520 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 11.939  5.161   5.281   1.00 52.47 ? 521 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? 25.812  11.339  -1.559  1.00 69.70 ? 522 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 19.758  -12.581 -8.907  1.00 55.96 ? 523 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? 39.057  -6.222  0.000   0.50 70.51 ? 524 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 22.355  -8.936  -9.691  1.00 55.34 ? 525 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? 13.178  -18.372 4.540   1.00 46.23 ? 526 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 38.315  -7.122  2.658   1.00 43.89 ? 527 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? 25.370  -19.761 10.711  1.00 45.67 ? 528 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? 32.535  7.100   -2.166  1.00 53.42 ? 529 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? 23.516  2.322   -8.705  1.00 47.57 ? 530 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 30.296  5.335   -5.873  1.00 48.81 ? 531 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 8   ? 1.1911 1.3009 0.5811 0.0534  0.3343  -0.0417 7   ASP   A N   
2    C CA  . ASP   A 8   ? 1.1825 1.2855 0.6350 0.0516  0.3051  -0.0373 7   ASP   A CA  
3    C C   . ASP   A 8   ? 1.1661 1.2673 0.6605 0.0637  0.3009  -0.0694 7   ASP   A C   
4    O O   . ASP   A 8   ? 1.1671 1.2518 0.6810 0.0646  0.2700  -0.0768 7   ASP   A O   
5    C CB  . ASP   A 8   ? 1.1870 1.3077 0.6978 0.0427  0.3144  -0.0080 7   ASP   A CB  
6    C CG  . ASP   A 8   ? 1.2686 1.3882 0.7499 0.0296  0.3141  0.0272  7   ASP   A CG  
7    O OD1 . ASP   A 8   ? 1.3015 1.4187 0.7162 0.0277  0.3266  0.0321  7   ASP   A OD1 
8    O OD2 . ASP   A 8   ? 1.2870 1.4072 0.8112 0.0214  0.3015  0.0500  7   ASP   A OD2 
9    N N   . ILE   A 9   ? 1.1455 1.2645 0.6581 0.0728  0.3327  -0.0867 8   ILE   A N   
10   C CA  . ILE   A 9   ? 1.1293 1.2481 0.6844 0.0856  0.3329  -0.1165 8   ILE   A CA  
11   C C   . ILE   A 9   ? 1.1523 1.2696 0.6610 0.0968  0.3545  -0.1463 8   ILE   A C   
12   O O   . ILE   A 9   ? 1.1461 1.2856 0.6609 0.1016  0.3910  -0.1503 8   ILE   A O   
13   C CB  . ILE   A 9   ? 1.0956 1.2391 0.7294 0.0873  0.3502  -0.1092 8   ILE   A CB  
14   C CG1 . ILE   A 9   ? 1.0910 1.2375 0.7641 0.0748  0.3330  -0.0778 8   ILE   A CG1 
15   C CG2 . ILE   A 9   ? 1.0842 1.2250 0.7643 0.1006  0.3460  -0.1375 8   ILE   A CG2 
16   C CD1 . ILE   A 9   ? 1.0756 1.2452 0.8232 0.0745  0.3456  -0.0689 8   ILE   A CD1 
17   N N   . PHE   A 10  ? 1.1780 1.2698 0.6398 0.1007  0.3328  -0.1678 9   PHE   A N   
18   C CA  . PHE   A 10  ? 1.2062 1.2924 0.6165 0.1113  0.3504  -0.1993 9   PHE   A CA  
19   C C   . PHE   A 10  ? 1.1785 1.2712 0.6377 0.1266  0.3665  -0.2294 9   PHE   A C   
20   O O   . PHE   A 10  ? 1.1631 1.2445 0.6703 0.1308  0.3441  -0.2399 9   PHE   A O   
21   C CB  . PHE   A 10  ? 1.2476 1.3031 0.5953 0.1102  0.3189  -0.2141 9   PHE   A CB  
22   C CG  . PHE   A 10  ? 1.2904 1.3395 0.5822 0.0968  0.3045  -0.1858 9   PHE   A CG  
23   C CD1 . PHE   A 10  ? 1.3273 1.3844 0.5535 0.0937  0.3290  -0.1771 9   PHE   A CD1 
24   C CD2 . PHE   A 10  ? 1.3041 1.3392 0.6093 0.0875  0.2667  -0.1675 9   PHE   A CD2 
25   C CE1 . PHE   A 10  ? 1.3571 1.4068 0.5322 0.0815  0.3138  -0.1490 9   PHE   A CE1 
26   C CE2 . PHE   A 10  ? 1.3350 1.3637 0.5924 0.0763  0.2521  -0.1414 9   PHE   A CE2 
27   C CZ  . PHE   A 10  ? 1.3533 1.3883 0.5452 0.0733  0.2744  -0.1318 9   PHE   A CZ  
28   N N   . ASN   A 11  ? 1.1713 1.2829 0.6203 0.1349  0.4061  -0.2424 10  ASN   A N   
29   C CA  . ASN   A 11  ? 1.1574 1.2768 0.6522 0.1513  0.4249  -0.2727 10  ASN   A CA  
30   C C   . ASN   A 11  ? 1.1649 1.2562 0.6159 0.1624  0.4137  -0.3126 10  ASN   A C   
31   O O   . ASN   A 11  ? 1.1691 1.2644 0.5871 0.1733  0.4422  -0.3389 10  ASN   A O   
32   C CB  . ASN   A 11  ? 1.1715 1.3242 0.6752 0.1563  0.4740  -0.2719 10  ASN   A CB  
33   C CG  . ASN   A 11  ? 1.2026 1.3729 0.7878 0.1700  0.4907  -0.2879 10  ASN   A CG  
34   O OD1 . ASN   A 11  ? 1.2059 1.3761 0.8600 0.1695  0.4696  -0.2793 10  ASN   A OD1 
35   N ND2 . ASN   A 11  ? 1.2193 1.4054 0.7984 0.1828  0.5287  -0.3114 10  ASN   A ND2 
36   N N   . ARG   A 12  ? 1.1622 1.2252 0.6137 0.1592  0.3724  -0.3174 11  ARG   A N   
37   C CA  . ARG   A 12  ? 1.1837 1.2167 0.6019 0.1676  0.3544  -0.3536 11  ARG   A CA  
38   C C   . ARG   A 12  ? 1.1694 1.1792 0.6313 0.1655  0.3131  -0.3556 11  ARG   A C   
39   O O   . ARG   A 12  ? 1.1453 1.1615 0.6531 0.1565  0.2971  -0.3275 11  ARG   A O   
40   C CB  . ARG   A 12  ? 1.2487 1.2667 0.5693 0.1625  0.3499  -0.3601 11  ARG   A CB  
41   C CG  . ARG   A 12  ? 1.2985 1.3029 0.5892 0.1464  0.3140  -0.3330 11  ARG   A CG  
42   C CD  . ARG   A 12  ? 1.3812 1.3640 0.5790 0.1442  0.3013  -0.3486 11  ARG   A CD  
43   N NE  . ARG   A 12  ? 1.4394 1.4357 0.5744 0.1480  0.3393  -0.3548 11  ARG   A NE  
44   C CZ  . ARG   A 12  ? 1.5044 1.4848 0.5508 0.1484  0.3371  -0.3724 11  ARG   A CZ  
45   N NH1 . ARG   A 12  ? 1.5275 1.5223 0.5182 0.1516  0.3752  -0.3761 11  ARG   A NH1 
46   N NH2 . ARG   A 12  ? 1.5245 1.4746 0.5369 0.1452  0.2966  -0.3864 11  ARG   A NH2 
47   N N   . ASP   A 13  ? 1.1782 1.1617 0.6293 0.1743  0.2982  -0.3901 12  ASP   A N   
48   C CA  . ASP   A 13  ? 1.1747 1.1342 0.6645 0.1727  0.2611  -0.3956 12  ASP   A CA  
49   C C   . ASP   A 13  ? 1.1879 1.1328 0.6383 0.1573  0.2275  -0.3772 12  ASP   A C   
50   O O   . ASP   A 13  ? 1.2228 1.1563 0.6011 0.1548  0.2230  -0.3875 12  ASP   A O   
51   C CB  . ASP   A 13  ? 1.2108 1.1447 0.6891 0.1861  0.2573  -0.4401 12  ASP   A CB  
52   C CG  . ASP   A 13  ? 1.2676 1.1767 0.7970 0.1873  0.2252  -0.4501 12  ASP   A CG  
53   O OD1 . ASP   A 13  ? 1.2612 1.1716 0.8292 0.1768  0.2031  -0.4226 12  ASP   A OD1 
54   O OD2 . ASP   A 13  ? 1.3174 1.2052 0.8480 0.1987  0.2229  -0.4857 12  ASP   A OD2 
55   N N   . PRO   A 14  ? 1.1622 1.1069 0.6570 0.1474  0.2029  -0.3511 13  PRO   A N   
56   C CA  . PRO   A 14  ? 1.1713 1.1028 0.6339 0.1337  0.1704  -0.3349 13  PRO   A CA  
57   C C   . PRO   A 14  ? 1.1913 1.0917 0.6213 0.1346  0.1421  -0.3634 13  PRO   A C   
58   O O   . PRO   A 14  ? 1.2086 1.0985 0.5970 0.1248  0.1181  -0.3556 13  PRO   A O   
59   C CB  . PRO   A 14  ? 1.1515 1.0896 0.6791 0.1259  0.1542  -0.3072 13  PRO   A CB  
60   C CG  . PRO   A 14  ? 1.1381 1.0800 0.7281 0.1363  0.1659  -0.3188 13  PRO   A CG  
61   C CD  . PRO   A 14  ? 1.1213 1.0774 0.6961 0.1482  0.2028  -0.3358 13  PRO   A CD  
62   N N   . ARG   A 15  ? 1.1869 1.0718 0.6365 0.1462  0.1440  -0.3968 14  ARG   A N   
63   C CA  . ARG   A 15  ? 1.2179 1.0715 0.6388 0.1478  0.1187  -0.4281 14  ARG   A CA  
64   C C   . ARG   A 15  ? 1.2589 1.1050 0.5905 0.1482  0.1225  -0.4453 14  ARG   A C   
65   O O   . ARG   A 15  ? 1.2856 1.1062 0.5834 0.1456  0.0952  -0.4659 14  ARG   A O   
66   C CB  . ARG   A 15  ? 1.2289 1.0675 0.6929 0.1613  0.1234  -0.4598 14  ARG   A CB  
67   C CG  . ARG   A 15  ? 1.2586 1.0924 0.8003 0.1578  0.1041  -0.4456 14  ARG   A CG  
68   C CD  . ARG   A 15  ? 1.2877 1.1132 0.8816 0.1722  0.1151  -0.4684 14  ARG   A CD  
69   N NE  . ARG   A 15  ? 1.2967 1.1281 0.9643 0.1690  0.1065  -0.4446 14  ARG   A NE  
70   C CZ  . ARG   A 15  ? 1.2960 1.1539 1.0031 0.1716  0.1274  -0.4228 14  ARG   A CZ  
71   N NH1 . ARG   A 15  ? 1.2892 1.1715 0.9746 0.1772  0.1595  -0.4209 14  ARG   A NH1 
72   N NH2 . ARG   A 15  ? 1.2707 1.1309 1.0389 0.1683  0.1163  -0.4028 14  ARG   A NH2 
73   N N   . ASP   A 16  ? 1.2628 1.1307 0.5557 0.1508  0.1557  -0.4369 15  ASP   A N   
74   C CA  . ASP   A 16  ? 1.3005 1.1633 0.5025 0.1500  0.1614  -0.4483 15  ASP   A CA  
75   C C   . ASP   A 16  ? 1.3113 1.1666 0.4748 0.1344  0.1272  -0.4242 15  ASP   A C   
76   O O   . ASP   A 16  ? 1.3468 1.1845 0.4413 0.1322  0.1109  -0.4403 15  ASP   A O   
77   C CB  . ASP   A 16  ? 1.3311 1.2225 0.5081 0.1540  0.2063  -0.4365 15  ASP   A CB  
78   C CG  . ASP   A 16  ? 1.4064 1.3068 0.6064 0.1708  0.2437  -0.4646 15  ASP   A CG  
79   O OD1 . ASP   A 16  ? 1.4359 1.3140 0.6284 0.1812  0.2384  -0.5040 15  ASP   A OD1 
80   O OD2 . ASP   A 16  ? 1.4275 1.3571 0.6547 0.1736  0.2781  -0.4478 15  ASP   A OD2 
81   N N   . HIS   A 17  ? 1.2812 1.1498 0.4892 0.1242  0.1159  -0.3867 16  HIS   A N   
82   C CA  . HIS   A 17  ? 1.2902 1.1542 0.4714 0.1104  0.0847  -0.3615 16  HIS   A CA  
83   C C   . HIS   A 17  ? 1.2621 1.1125 0.4968 0.1034  0.0461  -0.3568 16  HIS   A C   
84   O O   . HIS   A 17  ? 1.2813 1.1229 0.4937 0.0936  0.0147  -0.3455 16  HIS   A O   
85   C CB  . HIS   A 17  ? 1.2988 1.1885 0.4834 0.1031  0.1016  -0.3200 16  HIS   A CB  
86   C CG  . HIS   A 17  ? 1.3437 1.2508 0.4862 0.1084  0.1427  -0.3191 16  HIS   A CG  
87   N ND1 . HIS   A 17  ? 1.3995 1.2967 0.4647 0.1138  0.1532  -0.3448 16  HIS   A ND1 
88   C CD2 . HIS   A 17  ? 1.3430 1.2765 0.5111 0.1082  0.1752  -0.2955 16  HIS   A CD2 
89   C CE1 . HIS   A 17  ? 1.4052 1.3244 0.4521 0.1169  0.1937  -0.3352 16  HIS   A CE1 
90   N NE2 . HIS   A 17  ? 1.3742 1.3160 0.4833 0.1133  0.2077  -0.3052 16  HIS   A NE2 
91   N N   . TYR   A 18  ? 1.2124 1.0627 0.5193 0.1081  0.0486  -0.3629 17  TYR   A N   
92   C CA  . TYR   A 18  ? 1.1755 1.0152 0.5361 0.1009  0.0164  -0.3559 17  TYR   A CA  
93   C C   . TYR   A 18  ? 1.1715 0.9883 0.5625 0.1068  0.0035  -0.3880 17  TYR   A C   
94   O O   . TYR   A 18  ? 1.1666 0.9818 0.5746 0.1185  0.0255  -0.4090 17  TYR   A O   
95   C CB  . TYR   A 18  ? 1.1289 0.9892 0.5539 0.0967  0.0244  -0.3228 17  TYR   A CB  
96   C CG  . TYR   A 18  ? 1.1160 0.9946 0.5191 0.0886  0.0288  -0.2888 17  TYR   A CG  
97   C CD1 . TYR   A 18  ? 1.1196 0.9941 0.5146 0.0776  -0.0009 -0.2700 17  TYR   A CD1 
98   C CD2 . TYR   A 18  ? 1.1146 1.0143 0.5074 0.0918  0.0626  -0.2754 17  TYR   A CD2 
99   C CE1 . TYR   A 18  ? 1.1295 1.0182 0.5039 0.0708  0.0020  -0.2393 17  TYR   A CE1 
100  C CE2 . TYR   A 18  ? 1.1204 1.0346 0.4940 0.0837  0.0662  -0.2436 17  TYR   A CE2 
101  C CZ  . TYR   A 18  ? 1.1351 1.0426 0.4985 0.0736  0.0355  -0.2257 17  TYR   A CZ  
102  O OH  . TYR   A 18  ? 1.1517 1.0717 0.5000 0.0662  0.0382  -0.1936 17  TYR   A OH  
103  N N   . ASP   A 19  ? 1.1693 0.9685 0.5712 0.0983  -0.0330 -0.3907 18  ASP   A N   
104  C CA  . ASP   A 19  ? 1.1675 0.9434 0.6060 0.1005  -0.0508 -0.4159 18  ASP   A CA  
105  C C   . ASP   A 19  ? 1.1300 0.9148 0.6478 0.0965  -0.0529 -0.3924 18  ASP   A C   
106  O O   . ASP   A 19  ? 1.1256 0.9180 0.6634 0.0853  -0.0708 -0.3662 18  ASP   A O   
107  C CB  . ASP   A 19  ? 1.2172 0.9719 0.6289 0.0914  -0.0900 -0.4278 18  ASP   A CB  
108  C CG  . ASP   A 19  ? 1.3352 1.0779 0.6637 0.0950  -0.0914 -0.4534 18  ASP   A CG  
109  O OD1 . ASP   A 19  ? 1.3584 1.0923 0.6653 0.1071  -0.0707 -0.4835 18  ASP   A OD1 
110  O OD2 . ASP   A 19  ? 1.3893 1.1315 0.6735 0.0863  -0.1133 -0.4435 18  ASP   A OD2 
111  N N   . LEU   A 20  ? 1.1008 0.8864 0.6622 0.1060  -0.0333 -0.4001 19  LEU   A N   
112  C CA  . LEU   A 20  ? 1.0702 0.8635 0.7019 0.1028  -0.0344 -0.3781 19  LEU   A CA  
113  C C   . LEU   A 20  ? 1.0537 0.8255 0.7214 0.0952  -0.0656 -0.3835 19  LEU   A C   
114  O O   . LEU   A 20  ? 1.0645 0.8127 0.7387 0.1002  -0.0736 -0.4116 19  LEU   A O   
115  C CB  . LEU   A 20  ? 1.0615 0.8613 0.7302 0.1155  -0.0069 -0.3842 19  LEU   A CB  
116  C CG  . LEU   A 20  ? 1.0790 0.9085 0.7500 0.1195  0.0238  -0.3636 19  LEU   A CG  
117  C CD1 . LEU   A 20  ? 1.0732 0.9075 0.7949 0.1309  0.0435  -0.3688 19  LEU   A CD1 
118  C CD2 . LEU   A 20  ? 1.0735 0.9212 0.7616 0.1076  0.0173  -0.3266 19  LEU   A CD2 
119  N N   . LEU   A 21  ? 1.0272 0.8071 0.7203 0.0831  -0.0823 -0.3567 20  LEU   A N   
120  C CA  . LEU   A 21  ? 1.0082 0.7719 0.7423 0.0741  -0.1097 -0.3566 20  LEU   A CA  
121  C C   . LEU   A 21  ? 0.9741 0.7419 0.7731 0.0750  -0.1007 -0.3410 20  LEU   A C   
122  O O   . LEU   A 21  ? 0.9829 0.7546 0.7929 0.0860  -0.0779 -0.3459 20  LEU   A O   
123  C CB  . LEU   A 21  ? 1.0043 0.7738 0.7293 0.0605  -0.1345 -0.3393 20  LEU   A CB  
124  C CG  . LEU   A 21  ? 1.0332 0.7989 0.6925 0.0591  -0.1463 -0.3511 20  LEU   A CG  
125  C CD1 . LEU   A 21  ? 1.0396 0.8095 0.7039 0.0461  -0.1746 -0.3342 20  LEU   A CD1 
126  C CD2 . LEU   A 21  ? 1.0504 0.7894 0.6807 0.0642  -0.1565 -0.3894 20  LEU   A CD2 
127  N N   . GLN   A 22  ? 0.9309 0.6978 0.7722 0.0640  -0.1178 -0.3230 21  GLN   A N   
128  C CA  . GLN   A 22  ? 0.8895 0.6573 0.7863 0.0640  -0.1114 -0.3086 21  GLN   A CA  
129  C C   . GLN   A 22  ? 0.8471 0.6409 0.7552 0.0667  -0.0889 -0.2830 21  GLN   A C   
130  O O   . GLN   A 22  ? 0.8467 0.6597 0.7272 0.0652  -0.0809 -0.2700 21  GLN   A O   
131  C CB  . GLN   A 22  ? 0.9079 0.6673 0.8439 0.0506  -0.1350 -0.2971 21  GLN   A CB  
132  C CG  . GLN   A 22  ? 0.9522 0.7333 0.8939 0.0398  -0.1398 -0.2686 21  GLN   A CG  
133  C CD  . GLN   A 22  ? 1.0415 0.8214 0.9551 0.0321  -0.1613 -0.2739 21  GLN   A CD  
134  O OE1 . GLN   A 22  ? 1.0793 0.8454 0.9555 0.0354  -0.1702 -0.2982 21  GLN   A OE1 
135  N NE2 . GLN   A 22  ? 1.0536 0.8482 0.9851 0.0220  -0.1705 -0.2515 21  GLN   A NE2 
136  N N   . ARG   A 23  ? 0.8024 0.5952 0.7519 0.0707  -0.0800 -0.2759 22  ARG   A N   
137  C CA  . ARG   A 23  ? 0.7607 0.5754 0.7280 0.0722  -0.0626 -0.2522 22  ARG   A CA  
138  C C   . ARG   A 23  ? 0.7256 0.5501 0.7114 0.0591  -0.0737 -0.2263 22  ARG   A C   
139  O O   . ARG   A 23  ? 0.7305 0.5423 0.7419 0.0511  -0.0904 -0.2239 22  ARG   A O   
140  C CB  . ARG   A 23  ? 0.7527 0.5602 0.7593 0.0802  -0.0546 -0.2536 22  ARG   A CB  
141  C CG  . ARG   A 23  ? 0.7438 0.5735 0.7694 0.0821  -0.0385 -0.2305 22  ARG   A CG  
142  C CD  . ARG   A 23  ? 0.7438 0.5652 0.8084 0.0900  -0.0343 -0.2315 22  ARG   A CD  
143  N NE  . ARG   A 23  ? 0.7391 0.5812 0.8226 0.0915  -0.0218 -0.2102 22  ARG   A NE  
144  C CZ  . ARG   A 23  ? 0.7393 0.5860 0.8456 0.0832  -0.0281 -0.1865 22  ARG   A CZ  
145  N NH1 . ARG   A 23  ? 0.7199 0.5843 0.8403 0.0852  -0.0177 -0.1701 22  ARG   A NH1 
146  N NH2 . ARG   A 23  ? 0.7310 0.5651 0.8465 0.0724  -0.0446 -0.1796 22  ARG   A NH2 
147  N N   . LEU   A 24  ? 0.6838 0.5307 0.6576 0.0567  -0.0640 -0.2075 23  LEU   A N   
148  C CA  . LEU   A 24  ? 0.6499 0.5079 0.6408 0.0458  -0.0714 -0.1839 23  LEU   A CA  
149  C C   . LEU   A 24  ? 0.6119 0.4788 0.6380 0.0454  -0.0618 -0.1649 23  LEU   A C   
150  O O   . LEU   A 24  ? 0.5931 0.4631 0.6416 0.0366  -0.0690 -0.1489 23  LEU   A O   
151  C CB  . LEU   A 24  ? 0.6498 0.5249 0.6096 0.0434  -0.0681 -0.1740 23  LEU   A CB  
152  C CG  . LEU   A 24  ? 0.6793 0.5467 0.5991 0.0429  -0.0797 -0.1896 23  LEU   A CG  
153  C CD1 . LEU   A 24  ? 0.6906 0.5744 0.5767 0.0423  -0.0732 -0.1778 23  LEU   A CD1 
154  C CD2 . LEU   A 24  ? 0.6850 0.5401 0.6185 0.0337  -0.1048 -0.1931 23  LEU   A CD2 
155  N N   . GLY   A 25  ? 0.5914 0.4627 0.6219 0.0548  -0.0459 -0.1671 24  GLY   A N   
156  C CA  . GLY   A 25  ? 0.5661 0.4453 0.6261 0.0556  -0.0380 -0.1507 24  GLY   A CA  
157  C C   . GLY   A 25  ? 0.5514 0.4461 0.6056 0.0646  -0.0190 -0.1501 24  GLY   A C   
158  O O   . GLY   A 25  ? 0.5540 0.4509 0.5839 0.0716  -0.0099 -0.1647 24  GLY   A O   
159  N N   . GLY   A 26  ? 0.5311 0.4371 0.6072 0.0642  -0.0128 -0.1334 25  GLY   A N   
160  C CA  . GLY   A 26  ? 0.5221 0.4443 0.6004 0.0718  0.0038  -0.1314 25  GLY   A CA  
161  C C   . GLY   A 26  ? 0.5123 0.4439 0.6178 0.0702  0.0055  -0.1133 25  GLY   A C   
162  O O   . GLY   A 26  ? 0.5054 0.4317 0.6236 0.0628  -0.0047 -0.1009 25  GLY   A O   
163  N N   . GLY   A 27  ? 0.4965 0.4435 0.6094 0.0765  0.0188  -0.1116 26  GLY   A N   
164  C CA  . GLY   A 27  ? 0.4806 0.4375 0.6183 0.0758  0.0195  -0.0963 26  GLY   A CA  
165  C C   . GLY   A 27  ? 0.4627 0.4385 0.6092 0.0829  0.0346  -0.0973 26  GLY   A C   
166  O O   . GLY   A 27  ? 0.4592 0.4379 0.5985 0.0908  0.0460  -0.1121 26  GLY   A O   
167  N N   . THR   A 28  ? 0.4549 0.4448 0.6158 0.0795  0.0358  -0.0822 27  THR   A N   
168  C CA  . THR   A 28  ? 0.4561 0.4664 0.6307 0.0846  0.0497  -0.0816 27  THR   A CA  
169  C C   . THR   A 28  ? 0.4677 0.4895 0.6171 0.0841  0.0652  -0.0865 27  THR   A C   
170  O O   . THR   A 28  ? 0.4643 0.5012 0.6231 0.0900  0.0803  -0.0909 27  THR   A O   
171  C CB  . THR   A 28  ? 0.4486 0.4705 0.6391 0.0788  0.0456  -0.0648 27  THR   A CB  
172  O OG1 . THR   A 28  ? 0.4623 0.4849 0.6305 0.0683  0.0430  -0.0552 27  THR   A OG1 
173  C CG2 . THR   A 28  ? 0.4357 0.4487 0.6504 0.0804  0.0316  -0.0585 27  THR   A CG2 
174  N N   . TYR   A 29  ? 0.4782 0.4934 0.5968 0.0769  0.0613  -0.0848 28  TYR   A N   
175  C CA  . TYR   A 29  ? 0.4822 0.5050 0.5712 0.0751  0.0726  -0.0866 28  TYR   A CA  
176  C C   . TYR   A 29  ? 0.5054 0.5203 0.5713 0.0823  0.0793  -0.1059 28  TYR   A C   
177  O O   . TYR   A 29  ? 0.5260 0.5463 0.5617 0.0810  0.0888  -0.1074 28  TYR   A O   
178  C CB  . TYR   A 29  ? 0.4704 0.4884 0.5383 0.0648  0.0626  -0.0757 28  TYR   A CB  
179  C CG  . TYR   A 29  ? 0.4616 0.4608 0.5208 0.0624  0.0465  -0.0812 28  TYR   A CG  
180  C CD1 . TYR   A 29  ? 0.4774 0.4660 0.5098 0.0641  0.0439  -0.0945 28  TYR   A CD1 
181  C CD2 . TYR   A 29  ? 0.4542 0.4463 0.5316 0.0576  0.0338  -0.0731 28  TYR   A CD2 
182  C CE1 . TYR   A 29  ? 0.4900 0.4616 0.5197 0.0612  0.0281  -0.1003 28  TYR   A CE1 
183  C CE2 . TYR   A 29  ? 0.4621 0.4383 0.5359 0.0543  0.0203  -0.0770 28  TYR   A CE2 
184  C CZ  . TYR   A 29  ? 0.4915 0.4576 0.5438 0.0559  0.0168  -0.0907 28  TYR   A CZ  
185  O OH  . TYR   A 29  ? 0.5175 0.4684 0.5699 0.0517  0.0022  -0.0948 28  TYR   A OH  
186  N N   . GLY   A 30  ? 0.5073 0.5077 0.5841 0.0892  0.0731  -0.1201 29  GLY   A N   
187  C CA  . GLY   A 30  ? 0.5284 0.5190 0.5831 0.0965  0.0785  -0.1416 29  GLY   A CA  
188  C C   . GLY   A 30  ? 0.5573 0.5235 0.6020 0.0947  0.0603  -0.1519 29  GLY   A C   
189  O O   . GLY   A 30  ? 0.5640 0.5218 0.6238 0.0881  0.0447  -0.1413 29  GLY   A O   
190  N N   . GLU   A 31  ? 0.5752 0.5299 0.5955 0.1006  0.0627  -0.1734 30  GLU   A N   
191  C CA  . GLU   A 31  ? 0.6013 0.5317 0.6114 0.0986  0.0447  -0.1865 30  GLU   A CA  
192  C C   . GLU   A 31  ? 0.6254 0.5526 0.5906 0.0920  0.0388  -0.1892 30  GLU   A C   
193  O O   . GLU   A 31  ? 0.6439 0.5777 0.5763 0.0959  0.0521  -0.1982 30  GLU   A O   
194  C CB  . GLU   A 31  ? 0.6293 0.5455 0.6459 0.1109  0.0489  -0.2123 30  GLU   A CB  
195  C CG  . GLU   A 31  ? 0.6975 0.6129 0.7619 0.1180  0.0500  -0.2096 30  GLU   A CG  
196  C CD  . GLU   A 31  ? 0.8035 0.7003 0.8928 0.1117  0.0285  -0.2013 30  GLU   A CD  
197  O OE1 . GLU   A 31  ? 0.8626 0.7361 0.9530 0.1138  0.0174  -0.2177 30  GLU   A OE1 
198  O OE2 . GLU   A 31  ? 0.7986 0.7034 0.9055 0.1042  0.0230  -0.1786 30  GLU   A OE2 
199  N N   . VAL   A 32  ? 0.6289 0.5466 0.5926 0.0821  0.0192  -0.1813 31  VAL   A N   
200  C CA  . VAL   A 32  ? 0.6468 0.5623 0.5727 0.0753  0.0099  -0.1813 31  VAL   A CA  
201  C C   . VAL   A 32  ? 0.6752 0.5682 0.5875 0.0749  -0.0074 -0.2016 31  VAL   A C   
202  O O   . VAL   A 32  ? 0.6683 0.5472 0.6095 0.0726  -0.0208 -0.2042 31  VAL   A O   
203  C CB  . VAL   A 32  ? 0.6439 0.5690 0.5775 0.0645  0.0011  -0.1571 31  VAL   A CB  
204  C CG1 . VAL   A 32  ? 0.6626 0.5870 0.5591 0.0587  -0.0089 -0.1556 31  VAL   A CG1 
205  C CG2 . VAL   A 32  ? 0.6323 0.5777 0.5806 0.0648  0.0172  -0.1390 31  VAL   A CG2 
206  N N   . PHE   A 33  ? 0.6996 0.5885 0.5666 0.0769  -0.0070 -0.2163 32  PHE   A N   
207  C CA  . PHE   A 33  ? 0.7313 0.5985 0.5785 0.0764  -0.0245 -0.2385 32  PHE   A CA  
208  C C   . PHE   A 33  ? 0.7588 0.6266 0.5680 0.0682  -0.0394 -0.2335 32  PHE   A C   
209  O O   . PHE   A 33  ? 0.7571 0.6399 0.5381 0.0672  -0.0296 -0.2212 32  PHE   A O   
210  C CB  . PHE   A 33  ? 0.7446 0.6029 0.5680 0.0886  -0.0109 -0.2668 32  PHE   A CB  
211  C CG  . PHE   A 33  ? 0.7459 0.6019 0.6098 0.0985  0.0019  -0.2743 32  PHE   A CG  
212  C CD1 . PHE   A 33  ? 0.7421 0.6187 0.6205 0.1049  0.0257  -0.2641 32  PHE   A CD1 
213  C CD2 . PHE   A 33  ? 0.7559 0.5887 0.6456 0.1013  -0.0109 -0.2911 32  PHE   A CD2 
214  C CE1 . PHE   A 33  ? 0.7335 0.6086 0.6524 0.1145  0.0351  -0.2702 32  PHE   A CE1 
215  C CE2 . PHE   A 33  ? 0.7453 0.5749 0.6746 0.1110  -0.0010 -0.2962 32  PHE   A CE2 
216  C CZ  . PHE   A 33  ? 0.7266 0.5781 0.6707 0.1176  0.0213  -0.2853 32  PHE   A CZ  
217  N N   . LYS   A 34  ? 0.7781 0.6293 0.5893 0.0619  -0.0644 -0.2422 33  LYS   A N   
218  C CA  . LYS   A 34  ? 0.8139 0.6633 0.5904 0.0548  -0.0829 -0.2408 33  LYS   A CA  
219  C C   . LYS   A 34  ? 0.8648 0.7039 0.5871 0.0620  -0.0787 -0.2662 33  LYS   A C   
220  O O   . LYS   A 34  ? 0.8657 0.6903 0.5908 0.0696  -0.0738 -0.2903 33  LYS   A O   
221  C CB  . LYS   A 34  ? 0.8298 0.6652 0.6328 0.0458  -0.1113 -0.2438 33  LYS   A CB  
222  C CG  . LYS   A 34  ? 0.8848 0.7209 0.6616 0.0377  -0.1340 -0.2393 33  LYS   A CG  
223  C CD  . LYS   A 34  ? 0.9266 0.7505 0.7373 0.0285  -0.1613 -0.2432 33  LYS   A CD  
224  C CE  . LYS   A 34  ? 0.9712 0.7955 0.7614 0.0208  -0.1873 -0.2405 33  LYS   A CE  
225  N NZ  . LYS   A 34  ? 0.9827 0.7992 0.8164 0.0109  -0.2122 -0.2416 33  LYS   A NZ  
226  N N   . ALA   A 35  ? 0.9034 0.7495 0.5757 0.0604  -0.0788 -0.2611 34  ALA   A N   
227  C CA  . ALA   A 35  ? 0.9496 0.7866 0.5626 0.0671  -0.0727 -0.2848 34  ALA   A CA  
228  C C   . ALA   A 35  ? 0.9992 0.8333 0.5606 0.0606  -0.0927 -0.2816 34  ALA   A C   
229  O O   . ALA   A 35  ? 0.9913 0.8367 0.5601 0.0527  -0.1030 -0.2559 34  ALA   A O   
230  C CB  . ALA   A 35  ? 0.9492 0.8018 0.5463 0.0761  -0.0376 -0.2825 34  ALA   A CB  
231  N N   . ARG   A 36  ? 1.0482 0.8666 0.5564 0.0642  -0.0988 -0.3082 35  ARG   A N   
232  C CA  . ARG   A 36  ? 1.1023 0.9160 0.5551 0.0584  -0.1200 -0.3067 35  ARG   A CA  
233  C C   . ARG   A 36  ? 1.1535 0.9703 0.5357 0.0651  -0.0982 -0.3145 35  ARG   A C   
234  O O   . ARG   A 36  ? 1.1645 0.9731 0.5274 0.0745  -0.0805 -0.3416 35  ARG   A O   
235  C CB  . ARG   A 36  ? 1.1423 0.9317 0.5903 0.0546  -0.1537 -0.3323 35  ARG   A CB  
236  C CG  . ARG   A 36  ? 1.2257 1.0112 0.6307 0.0463  -0.1845 -0.3262 35  ARG   A CG  
237  C CD  . ARG   A 36  ? 1.3004 1.0626 0.7052 0.0415  -0.2199 -0.3520 35  ARG   A CD  
238  N NE  . ARG   A 36  ? 1.3309 1.0914 0.8128 0.0350  -0.2350 -0.3466 35  ARG   A NE  
239  C CZ  . ARG   A 36  ? 1.3623 1.1027 0.8726 0.0347  -0.2471 -0.3718 35  ARG   A CZ  
240  N NH1 . ARG   A 36  ? 1.3693 1.0886 0.8385 0.0415  -0.2466 -0.4068 35  ARG   A NH1 
241  N NH2 . ARG   A 36  ? 1.3444 1.0851 0.9243 0.0276  -0.2591 -0.3624 35  ARG   A NH2 
242  N N   . ASP   A 37  ? 1.1809 1.0089 0.5238 0.0602  -0.0993 -0.2911 36  ASP   A N   
243  C CA  . ASP   A 37  ? 1.2296 1.0607 0.4996 0.0648  -0.0791 -0.2951 36  ASP   A CA  
244  C C   . ASP   A 37  ? 1.2835 1.0912 0.4936 0.0664  -0.0988 -0.3280 36  ASP   A C   
245  O O   . ASP   A 37  ? 1.2919 1.0871 0.4975 0.0590  -0.1358 -0.3301 36  ASP   A O   
246  C CB  . ASP   A 37  ? 1.2531 1.0985 0.4980 0.0575  -0.0811 -0.2591 36  ASP   A CB  
247  C CG  . ASP   A 37  ? 1.3215 1.1740 0.4966 0.0606  -0.0553 -0.2544 36  ASP   A CG  
248  O OD1 . ASP   A 37  ? 1.3498 1.1887 0.4592 0.0638  -0.0581 -0.2782 36  ASP   A OD1 
249  O OD2 . ASP   A 37  ? 1.3379 1.2092 0.5228 0.0590  -0.0332 -0.2262 36  ASP   A OD2 
250  N N   . LYS   A 38  ? 1.3173 1.1192 0.4860 0.0763  -0.0744 -0.3556 37  LYS   A N   
251  C CA  . LYS   A 38  ? 1.3672 1.1456 0.4748 0.0795  -0.0890 -0.3919 37  LYS   A CA  
252  C C   . LYS   A 38  ? 1.4153 1.1891 0.4421 0.0730  -0.1083 -0.3838 37  LYS   A C   
253  O O   . LYS   A 38  ? 1.4472 1.1995 0.4238 0.0729  -0.1311 -0.4118 37  LYS   A O   
254  C CB  . LYS   A 38  ? 1.4080 1.1852 0.4880 0.0930  -0.0517 -0.4211 37  LYS   A CB  
255  C CG  . LYS   A 38  ? 1.4399 1.2186 0.5923 0.1018  -0.0324 -0.4343 37  LYS   A CG  
256  C CD  . LYS   A 38  ? 1.5039 1.2815 0.6218 0.1159  0.0032  -0.4648 37  LYS   A CD  
257  C CE  . LYS   A 38  ? 1.5315 1.3021 0.7121 0.1266  0.0154  -0.4885 37  LYS   A CE  
258  N NZ  . LYS   A 38  ? 1.5797 1.3474 0.7233 0.1414  0.0478  -0.5225 37  LYS   A NZ  
259  N N   . VAL   A 39  ? 1.4207 1.2133 0.4305 0.0682  -0.0983 -0.3473 38  VAL   A N   
260  C CA  . VAL   A 39  ? 1.4639 1.2523 0.3945 0.0623  -0.1150 -0.3358 38  VAL   A CA  
261  C C   . VAL   A 39  ? 1.4547 1.2428 0.4101 0.0510  -0.1563 -0.3088 38  VAL   A C   
262  O O   . VAL   A 39  ? 1.4787 1.2505 0.3957 0.0462  -0.1932 -0.3189 38  VAL   A O   
263  C CB  . VAL   A 39  ? 1.4933 1.2995 0.3757 0.0648  -0.0761 -0.3153 38  VAL   A CB  
264  C CG1 . VAL   A 39  ? 1.5299 1.3359 0.3488 0.0561  -0.0951 -0.2871 38  VAL   A CG1 
265  C CG2 . VAL   A 39  ? 1.5159 1.3173 0.3467 0.0757  -0.0432 -0.3496 38  VAL   A CG2 
266  N N   . SER   A 40  ? 1.4168 1.2229 0.4370 0.0472  -0.1509 -0.2761 39  SER   A N   
267  C CA  . SER   A 40  ? 1.4021 1.2107 0.4517 0.0377  -0.1859 -0.2492 39  SER   A CA  
268  C C   . SER   A 40  ? 1.3746 1.1751 0.4912 0.0341  -0.2161 -0.2617 39  SER   A C   
269  O O   . SER   A 40  ? 1.3728 1.1714 0.5042 0.0265  -0.2518 -0.2487 39  SER   A O   
270  C CB  . SER   A 40  ? 1.3968 1.2271 0.4842 0.0352  -0.1669 -0.2096 39  SER   A CB  
271  O OG  . SER   A 40  ? 1.4049 1.2456 0.5653 0.0388  -0.1444 -0.2115 39  SER   A OG  
272  N N   . GLY   A 41  ? 1.3480 1.1445 0.5081 0.0393  -0.2016 -0.2849 40  GLY   A N   
273  C CA  . GLY   A 41  ? 1.3144 1.1034 0.5418 0.0354  -0.2258 -0.2951 40  GLY   A CA  
274  C C   . GLY   A 41  ? 1.2595 1.0663 0.5666 0.0313  -0.2218 -0.2661 40  GLY   A C   
275  O O   . GLY   A 41  ? 1.2449 1.0481 0.6121 0.0276  -0.2376 -0.2709 40  GLY   A O   
276  N N   . ASP   A 42  ? 1.2276 1.0531 0.5358 0.0317  -0.2002 -0.2360 41  ASP   A N   
277  C CA  . ASP   A 42  ? 1.1817 1.0239 0.5588 0.0284  -0.1948 -0.2085 41  ASP   A CA  
278  C C   . ASP   A 42  ? 1.1328 0.9789 0.5663 0.0330  -0.1711 -0.2174 41  ASP   A C   
279  O O   . ASP   A 42  ? 1.1411 0.9835 0.5567 0.0407  -0.1471 -0.2362 41  ASP   A O   
280  C CB  . ASP   A 42  ? 1.2083 1.0666 0.5670 0.0279  -0.1771 -0.1766 41  ASP   A CB  
281  C CG  . ASP   A 42  ? 1.2887 1.1438 0.5921 0.0235  -0.1992 -0.1618 41  ASP   A CG  
282  O OD1 . ASP   A 42  ? 1.3191 1.1599 0.5949 0.0207  -0.2307 -0.1771 41  ASP   A OD1 
283  O OD2 . ASP   A 42  ? 1.3137 1.1795 0.6011 0.0225  -0.1862 -0.1346 41  ASP   A OD2 
284  N N   . LEU   A 43  ? 1.0772 0.9312 0.5787 0.0286  -0.1775 -0.2031 42  LEU   A N   
285  C CA  . LEU   A 43  ? 1.0330 0.8908 0.5889 0.0319  -0.1579 -0.2070 42  LEU   A CA  
286  C C   . LEU   A 43  ? 0.9877 0.8645 0.5595 0.0344  -0.1289 -0.1836 42  LEU   A C   
287  O O   . LEU   A 43  ? 0.9860 0.8741 0.5599 0.0302  -0.1320 -0.1583 42  LEU   A O   
288  C CB  . LEU   A 43  ? 1.0183 0.8741 0.6368 0.0253  -0.1786 -0.2042 42  LEU   A CB  
289  C CG  . LEU   A 43  ? 1.0505 0.8869 0.6698 0.0219  -0.2063 -0.2290 42  LEU   A CG  
290  C CD1 . LEU   A 43  ? 1.0389 0.8778 0.7245 0.0138  -0.2240 -0.2204 42  LEU   A CD1 
291  C CD2 . LEU   A 43  ? 1.0644 0.8848 0.6708 0.0293  -0.1936 -0.2590 42  LEU   A CD2 
292  N N   . VAL   A 44  ? 0.9485 0.8283 0.5329 0.0414  -0.1016 -0.1926 43  VAL   A N   
293  C CA  . VAL   A 44  ? 0.9096 0.8072 0.5136 0.0441  -0.0733 -0.1740 43  VAL   A CA  
294  C C   . VAL   A 44  ? 0.8601 0.7587 0.5182 0.0479  -0.0611 -0.1808 43  VAL   A C   
295  O O   . VAL   A 44  ? 0.8498 0.7340 0.5225 0.0497  -0.0708 -0.2013 43  VAL   A O   
296  C CB  . VAL   A 44  ? 0.9366 0.8397 0.4889 0.0500  -0.0478 -0.1774 43  VAL   A CB  
297  C CG1 . VAL   A 44  ? 0.9647 0.8640 0.4551 0.0464  -0.0600 -0.1713 43  VAL   A CG1 
298  C CG2 . VAL   A 44  ? 0.9536 0.8476 0.4950 0.0593  -0.0332 -0.2079 43  VAL   A CG2 
299  N N   . ALA   A 45  ? 0.8259 0.7406 0.5135 0.0489  -0.0408 -0.1633 44  ALA   A N   
300  C CA  . ALA   A 45  ? 0.8027 0.7192 0.5351 0.0534  -0.0280 -0.1684 44  ALA   A CA  
301  C C   . ALA   A 45  ? 0.8003 0.7259 0.5179 0.0621  0.0014  -0.1750 44  ALA   A C   
302  O O   . ALA   A 45  ? 0.8113 0.7493 0.5031 0.0616  0.0155  -0.1623 44  ALA   A O   
303  C CB  . ALA   A 45  ? 0.7799 0.7079 0.5590 0.0481  -0.0284 -0.1454 44  ALA   A CB  
304  N N   . LEU   A 46  ? 0.7854 0.7046 0.5200 0.0702  0.0106  -0.1947 45  LEU   A N   
305  C CA  . LEU   A 46  ? 0.7850 0.7148 0.5148 0.0794  0.0391  -0.2020 45  LEU   A CA  
306  C C   . LEU   A 46  ? 0.7676 0.7048 0.5538 0.0829  0.0482  -0.1966 45  LEU   A C   
307  O O   . LEU   A 46  ? 0.7725 0.6965 0.5875 0.0855  0.0380  -0.2083 45  LEU   A O   
308  C CB  . LEU   A 46  ? 0.8051 0.7209 0.5027 0.0883  0.0439  -0.2335 45  LEU   A CB  
309  C CG  . LEU   A 46  ? 0.8470 0.7576 0.4766 0.0872  0.0418  -0.2419 45  LEU   A CG  
310  C CD1 . LEU   A 46  ? 0.8546 0.7530 0.4543 0.0978  0.0522  -0.2756 45  LEU   A CD1 
311  C CD2 . LEU   A 46  ? 0.8598 0.7905 0.4627 0.0844  0.0611  -0.2202 45  LEU   A CD2 
312  N N   . LYS   A 47  ? 0.7417 0.6993 0.5443 0.0825  0.0659  -0.1783 46  LYS   A N   
313  C CA  . LYS   A 47  ? 0.7141 0.6805 0.5681 0.0855  0.0735  -0.1716 46  LYS   A CA  
314  C C   . LYS   A 47  ? 0.7150 0.6927 0.5766 0.0964  0.0992  -0.1835 46  LYS   A C   
315  O O   . LYS   A 47  ? 0.7060 0.6993 0.5478 0.0970  0.1186  -0.1779 46  LYS   A O   
316  C CB  . LYS   A 47  ? 0.6985 0.6796 0.5718 0.0770  0.0730  -0.1439 46  LYS   A CB  
317  C CG  . LYS   A 47  ? 0.6849 0.6767 0.6072 0.0790  0.0797  -0.1350 46  LYS   A CG  
318  C CD  . LYS   A 47  ? 0.7047 0.7060 0.6429 0.0696  0.0741  -0.1106 46  LYS   A CD  
319  C CE  . LYS   A 47  ? 0.7381 0.7521 0.6520 0.0648  0.0845  -0.0965 46  LYS   A CE  
320  N NZ  . LYS   A 47  ? 0.7471 0.7624 0.6676 0.0553  0.0724  -0.0766 46  LYS   A NZ  
321  N N   . MET   A 48  ? 0.7190 0.6888 0.6119 0.1050  0.0994  -0.1989 47  MET   A N   
322  C CA  . MET   A 48  ? 0.7252 0.7059 0.6363 0.1170  0.1223  -0.2113 47  MET   A CA  
323  C C   . MET   A 48  ? 0.7187 0.7162 0.6817 0.1171  0.1275  -0.1938 47  MET   A C   
324  O O   . MET   A 48  ? 0.7037 0.6927 0.7009 0.1158  0.1119  -0.1883 47  MET   A O   
325  C CB  . MET   A 48  ? 0.7433 0.7034 0.6626 0.1273  0.1170  -0.2389 47  MET   A CB  
326  C CG  . MET   A 48  ? 0.7956 0.7660 0.7455 0.1414  0.1386  -0.2525 47  MET   A CG  
327  S SD  . MET   A 48  ? 0.9727 0.9150 0.9492 0.1530  0.1263  -0.2802 47  MET   A SD  
328  C CE  . MET   A 48  ? 0.9098 0.8529 0.9483 0.1491  0.1100  -0.2567 47  MET   A CE  
329  N N   . VAL   A 49  ? 0.7296 0.7508 0.6981 0.1185  0.1497  -0.1854 48  VAL   A N   
330  C CA  . VAL   A 49  ? 0.7311 0.7707 0.7478 0.1187  0.1555  -0.1702 48  VAL   A CA  
331  C C   . VAL   A 49  ? 0.7590 0.8114 0.8006 0.1322  0.1776  -0.1859 48  VAL   A C   
332  O O   . VAL   A 49  ? 0.7751 0.8400 0.7931 0.1356  0.2004  -0.1930 48  VAL   A O   
333  C CB  . VAL   A 49  ? 0.7253 0.7836 0.7347 0.1081  0.1628  -0.1465 48  VAL   A CB  
334  C CG1 . VAL   A 49  ? 0.7108 0.7855 0.7707 0.1067  0.1637  -0.1313 48  VAL   A CG1 
335  C CG2 . VAL   A 49  ? 0.7386 0.7846 0.7172 0.0964  0.1441  -0.1339 48  VAL   A CG2 
336  N N   . LYS   A 50  ? 0.7666 0.8164 0.8554 0.1402  0.1717  -0.1910 49  LYS   A N   
337  C CA  . LYS   A 50  ? 0.7824 0.8456 0.9034 0.1544  0.1918  -0.2059 49  LYS   A CA  
338  C C   . LYS   A 50  ? 0.7859 0.8813 0.9361 0.1525  0.2101  -0.1899 49  LYS   A C   
339  O O   . LYS   A 50  ? 0.7727 0.8757 0.9482 0.1444  0.1986  -0.1691 49  LYS   A O   
340  C CB  . LYS   A 50  ? 0.8044 0.8528 0.9691 0.1640  0.1771  -0.2151 49  LYS   A CB  
341  C CG  . LYS   A 50  ? 0.8836 0.9025 1.0264 0.1703  0.1677  -0.2391 49  LYS   A CG  
342  C CD  . LYS   A 50  ? 0.9484 0.9427 1.1090 0.1662  0.1383  -0.2328 49  LYS   A CD  
343  C CE  . LYS   A 50  ? 0.9780 0.9754 1.1973 0.1737  0.1322  -0.2267 49  LYS   A CE  
344  N NZ  . LYS   A 50  ? 0.9937 0.9919 1.2400 0.1915  0.1468  -0.2502 49  LYS   A NZ  
345  N N   . MET   A 51  ? 0.8024 0.9167 0.9481 0.1594  0.2390  -0.2000 50  MET   A N   
346  C CA  . MET   A 51  ? 0.8065 0.9533 0.9816 0.1571  0.2593  -0.1857 50  MET   A CA  
347  C C   . MET   A 51  ? 0.7920 0.9535 1.0370 0.1663  0.2593  -0.1860 50  MET   A C   
348  O O   . MET   A 51  ? 0.7828 0.9380 1.0508 0.1807  0.2615  -0.2059 50  MET   A O   
349  C CB  . MET   A 51  ? 0.8304 0.9935 0.9746 0.1606  0.2927  -0.1955 50  MET   A CB  
350  C CG  . MET   A 51  ? 0.8944 1.0441 0.9672 0.1510  0.2918  -0.1927 50  MET   A CG  
351  S SD  . MET   A 51  ? 0.9668 1.1336 1.0276 0.1327  0.2952  -0.1590 50  MET   A SD  
352  C CE  . MET   A 51  ? 0.9586 1.1020 1.0230 0.1218  0.2545  -0.1431 50  MET   A CE  
353  N N   . GLU   A 52  ? 0.7896 0.9703 1.0694 0.1582  0.2557  -0.1642 51  GLU   A N   
354  C CA  . GLU   A 52  ? 0.7873 0.9848 1.1350 0.1646  0.2523  -0.1602 51  GLU   A CA  
355  C C   . GLU   A 52  ? 0.7844 1.0145 1.1666 0.1734  0.2846  -0.1675 51  GLU   A C   
356  O O   . GLU   A 52  ? 0.7912 1.0349 1.1440 0.1696  0.3100  -0.1676 51  GLU   A O   
357  C CB  . GLU   A 52  ? 0.8168 1.0199 1.1835 0.1509  0.2327  -0.1347 51  GLU   A CB  
358  C CG  . GLU   A 52  ? 0.9106 1.0844 1.2515 0.1434  0.2023  -0.1275 51  GLU   A CG  
359  C CD  . GLU   A 52  ? 0.9998 1.1525 1.3591 0.1533  0.1831  -0.1378 51  GLU   A CD  
360  O OE1 . GLU   A 52  ? 1.0105 1.1700 1.4182 0.1574  0.1717  -0.1319 51  GLU   A OE1 
361  O OE2 . GLU   A 52  ? 1.0416 1.1700 1.3674 0.1563  0.1780  -0.1509 51  GLU   A OE2 
362  N N   . PRO   A 53  ? 0.7717 1.0160 1.2184 0.1848  0.2843  -0.1722 52  PRO   A N   
363  C CA  . PRO   A 53  ? 0.7554 1.0333 1.2423 0.1939  0.3161  -0.1799 52  PRO   A CA  
364  C C   . PRO   A 53  ? 0.7584 1.0673 1.2536 0.1812  0.3350  -0.1608 52  PRO   A C   
365  O O   . PRO   A 53  ? 0.7560 1.0927 1.2704 0.1865  0.3674  -0.1670 52  PRO   A O   
366  C CB  . PRO   A 53  ? 0.7370 1.0218 1.2969 0.2063  0.3024  -0.1830 52  PRO   A CB  
367  C CG  . PRO   A 53  ? 0.7558 1.0037 1.2996 0.2083  0.2699  -0.1861 52  PRO   A CG  
368  C CD  . PRO   A 53  ? 0.7610 0.9909 1.2471 0.1906  0.2551  -0.1708 52  PRO   A CD  
369  N N   . ASP   A 54  ? 0.7676 1.0725 1.2518 0.1647  0.3161  -0.1381 53  ASP   A N   
370  C CA  . ASP   A 54  ? 0.7678 1.0983 1.2615 0.1510  0.3304  -0.1184 53  ASP   A CA  
371  C C   . ASP   A 54  ? 0.7955 1.1122 1.2203 0.1365  0.3334  -0.1073 53  ASP   A C   
372  O O   . ASP   A 54  ? 0.7948 1.1236 1.2235 0.1224  0.3353  -0.0871 53  ASP   A O   
373  C CB  . ASP   A 54  ? 0.7795 1.1191 1.3246 0.1429  0.3062  -0.1001 53  ASP   A CB  
374  C CG  . ASP   A 54  ? 0.8208 1.1847 1.4440 0.1541  0.3068  -0.1048 53  ASP   A CG  
375  O OD1 . ASP   A 54  ? 0.8282 1.2064 1.4728 0.1685  0.3307  -0.1218 53  ASP   A OD1 
376  O OD2 . ASP   A 54  ? 0.8381 1.2070 1.5014 0.1487  0.2833  -0.0919 53  ASP   A OD2 
377  N N   . ASP   A 55  ? 0.8156 1.1069 1.1798 0.1401  0.3327  -0.1204 54  ASP   A N   
378  C CA  . ASP   A 55  ? 0.8376 1.1149 1.1364 0.1278  0.3334  -0.1105 54  ASP   A CA  
379  C C   . ASP   A 55  ? 0.8416 1.1362 1.1103 0.1275  0.3699  -0.1127 54  ASP   A C   
380  O O   . ASP   A 55  ? 0.8675 1.1485 1.0852 0.1338  0.3796  -0.1291 54  ASP   A O   
381  C CB  . ASP   A 55  ? 0.8822 1.1240 1.1315 0.1305  0.3116  -0.1224 54  ASP   A CB  
382  C CG  . ASP   A 55  ? 0.9396 1.1618 1.1952 0.1232  0.2767  -0.1110 54  ASP   A CG  
383  O OD1 . ASP   A 55  ? 0.9368 1.1695 1.2185 0.1130  0.2685  -0.0917 54  ASP   A OD1 
384  O OD2 . ASP   A 55  ? 0.9792 1.1754 1.2135 0.1274  0.2580  -0.1219 54  ASP   A OD2 
385  N N   . ASP   A 56  ? 0.8104 1.1343 1.1091 0.1195  0.3899  -0.0961 55  ASP   A N   
386  C CA  . ASP   A 56  ? 0.8050 1.1475 1.0766 0.1173  0.4268  -0.0940 55  ASP   A CA  
387  C C   . ASP   A 56  ? 0.8248 1.1448 1.0150 0.1078  0.4238  -0.0863 55  ASP   A C   
388  O O   . ASP   A 56  ? 0.8355 1.1349 1.0070 0.0976  0.3958  -0.0726 55  ASP   A O   
389  C CB  . ASP   A 56  ? 0.7984 1.1748 1.1219 0.1074  0.4446  -0.0730 55  ASP   A CB  
390  C CG  . ASP   A 56  ? 0.8683 1.2369 1.1951 0.0897  0.4213  -0.0468 55  ASP   A CG  
391  O OD1 . ASP   A 56  ? 0.8872 1.2410 1.2354 0.0891  0.3888  -0.0458 55  ASP   A OD1 
392  O OD2 . ASP   A 56  ? 0.8991 1.2752 1.2055 0.0767  0.4357  -0.0274 55  ASP   A OD2 
393  N N   . VAL   A 57  ? 0.8237 1.1472 0.9650 0.1117  0.4520  -0.0959 56  VAL   A N   
394  C CA  . VAL   A 57  ? 0.8572 1.1591 0.9179 0.1040  0.4484  -0.0900 56  VAL   A CA  
395  C C   . VAL   A 57  ? 0.8563 1.1649 0.9072 0.0853  0.4503  -0.0566 56  VAL   A C   
396  O O   . VAL   A 57  ? 0.8832 1.1702 0.8784 0.0771  0.4358  -0.0462 56  VAL   A O   
397  C CB  . VAL   A 57  ? 0.8927 1.1915 0.8933 0.1136  0.4740  -0.1115 56  VAL   A CB  
398  C CG1 . VAL   A 57  ? 0.8899 1.1945 0.9213 0.1330  0.4857  -0.1437 56  VAL   A CG1 
399  C CG2 . VAL   A 57  ? 0.9015 1.2225 0.8743 0.1058  0.5106  -0.0963 56  VAL   A CG2 
400  N N   . SER   A 58  ? 0.8280 1.1646 0.9359 0.0787  0.4651  -0.0399 57  SER   A N   
401  C CA  . SER   A 58  ? 0.8336 1.1753 0.9398 0.0607  0.4660  -0.0084 57  SER   A CA  
402  C C   . SER   A 58  ? 0.8437 1.1627 0.9581 0.0523  0.4265  0.0038  57  SER   A C   
403  O O   . SER   A 58  ? 0.8732 1.1776 0.9516 0.0404  0.4167  0.0231  57  SER   A O   
404  C CB  . SER   A 58  ? 0.8191 1.1973 0.9906 0.0557  0.4919  0.0043  57  SER   A CB  
405  O OG  . SER   A 58  ? 0.8533 1.2547 1.0160 0.0629  0.5325  -0.0058 57  SER   A OG  
406  N N   . THR   A 59  ? 0.8161 1.1311 0.9763 0.0587  0.4037  -0.0074 58  THR   A N   
407  C CA  . THR   A 59  ? 0.8100 1.1036 0.9768 0.0521  0.3674  0.0012  58  THR   A CA  
408  C C   . THR   A 59  ? 0.8305 1.0920 0.9356 0.0553  0.3469  -0.0083 58  THR   A C   
409  O O   . THR   A 59  ? 0.8441 1.0872 0.9267 0.0461  0.3260  0.0052  58  THR   A O   
410  C CB  . THR   A 59  ? 0.8002 1.1010 1.0319 0.0577  0.3513  -0.0069 58  THR   A CB  
411  O OG1 . THR   A 59  ? 0.7840 1.1152 1.0743 0.0530  0.3680  0.0037  58  THR   A OG1 
412  C CG2 . THR   A 59  ? 0.8112 1.0893 1.0458 0.0519  0.3149  -0.0005 58  THR   A CG2 
413  N N   . LEU   A 60  ? 0.8241 1.0795 0.9041 0.0684  0.3535  -0.0322 59  LEU   A N   
414  C CA  . LEU   A 60  ? 0.8378 1.0649 0.8613 0.0726  0.3367  -0.0451 59  LEU   A CA  
415  C C   . LEU   A 60  ? 0.8505 1.0682 0.8134 0.0624  0.3394  -0.0291 59  LEU   A C   
416  O O   . LEU   A 60  ? 0.8683 1.0630 0.8009 0.0580  0.3143  -0.0247 59  LEU   A O   
417  C CB  . LEU   A 60  ? 0.8392 1.0672 0.8502 0.0880  0.3522  -0.0736 59  LEU   A CB  
418  C CG  . LEU   A 60  ? 0.8742 1.0733 0.8351 0.0941  0.3345  -0.0926 59  LEU   A CG  
419  C CD1 . LEU   A 60  ? 0.8712 1.0511 0.8555 0.0940  0.3004  -0.0942 59  LEU   A CD1 
420  C CD2 . LEU   A 60  ? 0.8793 1.0806 0.8318 0.1096  0.3534  -0.1220 59  LEU   A CD2 
421  N N   . GLN   A 61  ? 0.8373 1.0737 0.7864 0.0581  0.3697  -0.0182 60  GLN   A N   
422  C CA  . GLN   A 61  ? 0.8563 1.0852 0.7487 0.0478  0.3742  0.0008  60  GLN   A CA  
423  C C   . GLN   A 61  ? 0.8470 1.0668 0.7535 0.0340  0.3522  0.0277  60  GLN   A C   
424  O O   . GLN   A 61  ? 0.8671 1.0664 0.7289 0.0286  0.3348  0.0372  60  GLN   A O   
425  C CB  . GLN   A 61  ? 0.8777 1.1307 0.7567 0.0461  0.4144  0.0076  60  GLN   A CB  
426  C CG  . GLN   A 61  ? 0.9500 1.2033 0.7953 0.0312  0.4228  0.0385  60  GLN   A CG  
427  C CD  . GLN   A 61  ? 1.0662 1.2948 0.8306 0.0293  0.4108  0.0410  60  GLN   A CD  
428  O OE1 . GLN   A 61  ? 1.1129 1.3186 0.8520 0.0354  0.3844  0.0248  60  GLN   A OE1 
429  N NE2 . GLN   A 61  ? 1.0968 1.3292 0.8195 0.0199  0.4286  0.0629  60  GLN   A NE2 
430  N N   . LYS   A 62  ? 0.8126 1.0470 0.7828 0.0288  0.3514  0.0384  61  LYS   A N   
431  C CA  . LYS   A 62  ? 0.8036 1.0288 0.7927 0.0167  0.3305  0.0603  61  LYS   A CA  
432  C C   . LYS   A 62  ? 0.8036 1.0026 0.7798 0.0193  0.2962  0.0525  61  LYS   A C   
433  O O   . LYS   A 62  ? 0.8191 1.0020 0.7755 0.0114  0.2793  0.0677  61  LYS   A O   
434  C CB  . LYS   A 62  ? 0.8050 1.0495 0.8669 0.0124  0.3329  0.0672  61  LYS   A CB  
435  C CG  . LYS   A 62  ? 0.8587 1.1322 0.9462 0.0076  0.3663  0.0781  61  LYS   A CG  
436  C CD  . LYS   A 62  ? 0.8922 1.1831 1.0547 0.0022  0.3630  0.0849  61  LYS   A CD  
437  C CE  . LYS   A 62  ? 0.9065 1.2315 1.1103 0.0038  0.3954  0.0838  61  LYS   A CE  
438  N NZ  . LYS   A 62  ? 0.9225 1.2571 1.1412 0.0205  0.4017  0.0566  61  LYS   A NZ  
439  N N   . GLU   A 63  ? 0.7810 0.9759 0.7706 0.0304  0.2862  0.0293  62  GLU   A N   
440  C CA  . GLU   A 63  ? 0.7736 0.9455 0.7551 0.0328  0.2557  0.0210  62  GLU   A CA  
441  C C   . GLU   A 63  ? 0.7846 0.9367 0.7041 0.0331  0.2464  0.0188  62  GLU   A C   
442  O O   . GLU   A 63  ? 0.7942 0.9295 0.7028 0.0282  0.2235  0.0270  62  GLU   A O   
443  C CB  . GLU   A 63  ? 0.7840 0.9557 0.7936 0.0442  0.2493  -0.0017 62  GLU   A CB  
444  C CG  . GLU   A 63  ? 0.8038 0.9947 0.8762 0.0452  0.2545  -0.0009 62  GLU   A CG  
445  C CD  . GLU   A 63  ? 0.8483 1.0404 0.9530 0.0344  0.2411  0.0175  62  GLU   A CD  
446  O OE1 . GLU   A 63  ? 0.8400 1.0522 0.9824 0.0295  0.2543  0.0276  62  GLU   A OE1 
447  O OE2 . GLU   A 63  ? 0.8613 1.0346 0.9555 0.0307  0.2177  0.0210  62  GLU   A OE2 
448  N N   . ILE   A 64  ? 0.7822 0.9365 0.6612 0.0389  0.2638  0.0076  63  ILE   A N   
449  C CA  . ILE   A 64  ? 0.8011 0.9362 0.6175 0.0391  0.2530  0.0041  63  ILE   A CA  
450  C C   . ILE   A 64  ? 0.8105 0.9403 0.6005 0.0274  0.2485  0.0317  63  ILE   A C   
451  O O   . ILE   A 64  ? 0.8283 0.9392 0.5891 0.0249  0.2254  0.0355  63  ILE   A O   
452  C CB  . ILE   A 64  ? 0.8112 0.9483 0.5872 0.0487  0.2720  -0.0174 63  ILE   A CB  
453  C CG1 . ILE   A 64  ? 0.8214 0.9438 0.5996 0.0591  0.2555  -0.0450 63  ILE   A CG1 
454  C CG2 . ILE   A 64  ? 0.8422 0.9707 0.5478 0.0447  0.2760  -0.0100 63  ILE   A CG2 
455  C CD1 . ILE   A 64  ? 0.8149 0.9479 0.6492 0.0667  0.2608  -0.0577 63  ILE   A CD1 
456  N N   . LEU   A 65  ? 0.7964 0.9426 0.6039 0.0198  0.2683  0.0517  64  LEU   A N   
457  C CA  . LEU   A 65  ? 0.8105 0.9511 0.6011 0.0081  0.2643  0.0803  64  LEU   A CA  
458  C C   . LEU   A 65  ? 0.8013 0.9275 0.6211 0.0035  0.2343  0.0889  64  LEU   A C   
459  O O   . LEU   A 65  ? 0.8144 0.9245 0.6070 -0.0013 0.2171  0.1025  64  LEU   A O   
460  C CB  . LEU   A 65  ? 0.8022 0.9648 0.6203 0.0006  0.2921  0.0984  64  LEU   A CB  
461  C CG  . LEU   A 65  ? 0.8478 1.0081 0.6314 -0.0103 0.3012  0.1268  64  LEU   A CG  
462  C CD1 . LEU   A 65  ? 0.8723 1.0354 0.5914 -0.0069 0.3223  0.1221  64  LEU   A CD1 
463  C CD2 . LEU   A 65  ? 0.8432 1.0223 0.6749 -0.0202 0.3202  0.1474  64  LEU   A CD2 
464  N N   . ILE   A 66  ? 0.7770 0.9088 0.6510 0.0058  0.2279  0.0802  65  ILE   A N   
465  C CA  . ILE   A 66  ? 0.7782 0.8979 0.6808 0.0025  0.2025  0.0848  65  ILE   A CA  
466  C C   . ILE   A 66  ? 0.8035 0.9039 0.6789 0.0078  0.1785  0.0723  65  ILE   A C   
467  O O   . ILE   A 66  ? 0.8150 0.9019 0.6887 0.0037  0.1587  0.0822  65  ILE   A O   
468  C CB  . ILE   A 66  ? 0.7622 0.8934 0.7235 0.0040  0.2029  0.0772  65  ILE   A CB  
469  C CG1 . ILE   A 66  ? 0.7559 0.9069 0.7507 -0.0028 0.2237  0.0912  65  ILE   A CG1 
470  C CG2 . ILE   A 66  ? 0.7631 0.8812 0.7484 0.0017  0.1775  0.0785  65  ILE   A CG2 
471  C CD1 . ILE   A 66  ? 0.7459 0.9116 0.7961 0.0001  0.2256  0.0809  65  ILE   A CD1 
472  N N   . LEU   A 67  ? 0.8066 0.9056 0.6628 0.0168  0.1805  0.0504  66  LEU   A N   
473  C CA  . LEU   A 67  ? 0.8224 0.9037 0.6536 0.0212  0.1585  0.0371  66  LEU   A CA  
474  C C   . LEU   A 67  ? 0.8465 0.9153 0.6269 0.0173  0.1487  0.0480  66  LEU   A C   
475  O O   . LEU   A 67  ? 0.8604 0.9146 0.6301 0.0175  0.1252  0.0455  66  LEU   A O   
476  C CB  . LEU   A 67  ? 0.8258 0.9080 0.6453 0.0311  0.1660  0.0115  66  LEU   A CB  
477  C CG  . LEU   A 67  ? 0.8297 0.9097 0.6871 0.0371  0.1564  -0.0052 66  LEU   A CG  
478  C CD1 . LEU   A 67  ? 0.8384 0.9179 0.6828 0.0473  0.1656  -0.0297 66  LEU   A CD1 
479  C CD2 . LEU   A 67  ? 0.8402 0.9039 0.7010 0.0348  0.1287  -0.0049 66  LEU   A CD2 
480  N N   . LYS   A 68  ? 0.8533 0.9283 0.6021 0.0140  0.1664  0.0601  67  LYS   A N   
481  C CA  . LYS   A 68  ? 0.8861 0.9495 0.5815 0.0104  0.1578  0.0722  67  LYS   A CA  
482  C C   . LYS   A 68  ? 0.8894 0.9470 0.5960 0.0013  0.1464  0.1003  67  LYS   A C   
483  O O   . LYS   A 68  ? 0.9142 0.9579 0.5892 -0.0010 0.1277  0.1102  67  LYS   A O   
484  C CB  . LYS   A 68  ? 0.9257 0.9978 0.5757 0.0110  0.1842  0.0725  67  LYS   A CB  
485  C CG  . LYS   A 68  ? 1.0145 1.0726 0.5955 0.0106  0.1739  0.0742  67  LYS   A CG  
486  C CD  . LYS   A 68  ? 1.0999 1.1659 0.6332 0.0149  0.2005  0.0623  67  LYS   A CD  
487  C CE  . LYS   A 68  ? 1.1870 1.2372 0.6470 0.0152  0.1872  0.0598  67  LYS   A CE  
488  N NZ  . LYS   A 68  ? 1.2286 1.2776 0.6541 0.0248  0.1969  0.0279  67  LYS   A NZ  
489  N N   . THR   A 69  ? 0.8628 0.9302 0.6151 -0.0037 0.1563  0.1130  68  THR   A N   
490  C CA  . THR   A 69  ? 0.8571 0.9176 0.6239 -0.0122 0.1466  0.1387  68  THR   A CA  
491  C C   . THR   A 69  ? 0.8291 0.8815 0.6393 -0.0116 0.1243  0.1351  68  THR   A C   
492  O O   . THR   A 69  ? 0.8405 0.8812 0.6542 -0.0155 0.1079  0.1508  68  THR   A O   
493  C CB  . THR   A 69  ? 0.8637 0.9374 0.6487 -0.0199 0.1707  0.1576  68  THR   A CB  
494  O OG1 . THR   A 69  ? 0.8583 0.9479 0.6910 -0.0179 0.1837  0.1450  68  THR   A OG1 
495  C CG2 . THR   A 69  ? 0.8836 0.9639 0.6191 -0.0218 0.1927  0.1658  68  THR   A CG2 
496  N N   . CYS   A 70  ? 0.7942 0.8522 0.6362 -0.0063 0.1236  0.1151  69  CYS   A N   
497  C CA  . CYS   A 70  ? 0.7706 0.8216 0.6493 -0.0056 0.1045  0.1105  69  CYS   A CA  
498  C C   . CYS   A 70  ? 0.7548 0.7929 0.6106 -0.0013 0.0830  0.1013  69  CYS   A C   
499  O O   . CYS   A 70  ? 0.7626 0.8008 0.6197 0.0044  0.0792  0.0817  69  CYS   A O   
500  C CB  . CYS   A 70  ? 0.7705 0.8318 0.6877 -0.0023 0.1113  0.0947  69  CYS   A CB  
501  S SG  . CYS   A 70  ? 0.7946 0.8499 0.7576 -0.0036 0.0938  0.0929  69  CYS   A SG  
502  N N   . ARG   A 71  ? 0.7348 0.7617 0.5714 -0.0042 0.0683  0.1163  70  ARG   A N   
503  C CA  . ARG   A 71  ? 0.7242 0.7400 0.5398 -0.0010 0.0461  0.1102  70  ARG   A CA  
504  C C   . ARG   A 71  ? 0.6650 0.6722 0.5086 -0.0022 0.0253  0.1185  70  ARG   A C   
505  O O   . ARG   A 71  ? 0.6659 0.6693 0.5213 -0.0065 0.0237  0.1379  70  ARG   A O   
506  C CB  . ARG   A 71  ? 0.7832 0.7932 0.5439 -0.0023 0.0440  0.1197  70  ARG   A CB  
507  C CG  . ARG   A 71  ? 0.8817 0.8975 0.6052 0.0012  0.0602  0.1048  70  ARG   A CG  
508  C CD  . ARG   A 71  ? 0.9761 0.9827 0.6400 0.0011  0.0505  0.1085  70  ARG   A CD  
509  N NE  . ARG   A 71  ? 1.0635 1.0732 0.6926 -0.0036 0.0680  0.1276  70  ARG   A NE  
510  C CZ  . ARG   A 71  ? 1.1169 1.1193 0.7332 -0.0096 0.0600  0.1545  70  ARG   A CZ  
511  N NH1 . ARG   A 71  ? 1.1181 1.1236 0.7007 -0.0146 0.0779  0.1725  70  ARG   A NH1 
512  N NH2 . ARG   A 71  ? 1.1260 1.1182 0.7647 -0.0105 0.0344  0.1641  70  ARG   A NH2 
513  N N   . HIS   A 72  ? 0.6115 0.6148 0.4638 0.0016  0.0089  0.1048  71  HIS   A N   
514  C CA  . HIS   A 72  ? 0.5628 0.5599 0.4433 0.0015  -0.0097 0.1106  71  HIS   A CA  
515  C C   . HIS   A 72  ? 0.5471 0.5405 0.4226 0.0048  -0.0286 0.0974  71  HIS   A C   
516  O O   . HIS   A 72  ? 0.5495 0.5455 0.4187 0.0073  -0.0252 0.0792  71  HIS   A O   
517  C CB  . HIS   A 72  ? 0.5232 0.5248 0.4503 0.0011  -0.0029 0.1068  71  HIS   A CB  
518  C CG  . HIS   A 72  ? 0.5089 0.5050 0.4667 0.0014  -0.0175 0.1131  71  HIS   A CG  
519  N ND1 . HIS   A 72  ? 0.5155 0.5119 0.4933 0.0044  -0.0289 0.1011  71  HIS   A ND1 
520  C CD2 . HIS   A 72  ? 0.5129 0.5032 0.4861 -0.0008 -0.0212 0.1299  71  HIS   A CD2 
521  C CE1 . HIS   A 72  ? 0.5096 0.5019 0.5141 0.0047  -0.0380 0.1098  71  HIS   A CE1 
522  N NE2 . HIS   A 72  ? 0.5070 0.4944 0.5102 0.0020  -0.0346 0.1266  71  HIS   A NE2 
523  N N   . ALA   A 73  ? 0.5213 0.5086 0.4053 0.0049  -0.0492 0.1060  72  ALA   A N   
524  C CA  . ALA   A 73  ? 0.5140 0.4994 0.4001 0.0072  -0.0684 0.0943  72  ALA   A CA  
525  C C   . ALA   A 73  ? 0.4936 0.4844 0.4109 0.0088  -0.0642 0.0758  72  ALA   A C   
526  O O   . ALA   A 73  ? 0.5078 0.4974 0.4194 0.0097  -0.0744 0.0627  72  ALA   A O   
527  C CB  . ALA   A 73  ? 0.5053 0.4863 0.4087 0.0075  -0.0901 0.1071  72  ALA   A CB  
528  N N   . ASN   A 74  ? 0.4565 0.4522 0.4062 0.0086  -0.0509 0.0754  73  ASN   A N   
529  C CA  . ASN   A 74  ? 0.4373 0.4375 0.4137 0.0096  -0.0465 0.0605  73  ASN   A CA  
530  C C   . ASN   A 74  ? 0.4448 0.4482 0.4110 0.0103  -0.0300 0.0494  73  ASN   A C   
531  O O   . ASN   A 74  ? 0.4381 0.4451 0.4279 0.0107  -0.0233 0.0416  73  ASN   A O   
532  C CB  . ASN   A 74  ? 0.4188 0.4218 0.4356 0.0093  -0.0441 0.0643  73  ASN   A CB  
533  C CG  . ASN   A 74  ? 0.4286 0.4299 0.4644 0.0102  -0.0606 0.0714  73  ASN   A CG  
534  O OD1 . ASN   A 74  ? 0.4373 0.4359 0.4842 0.0104  -0.0628 0.0840  73  ASN   A OD1 
535  N ND2 . ASN   A 74  ? 0.4238 0.4265 0.4661 0.0107  -0.0735 0.0638  73  ASN   A ND2 
536  N N   . ILE   A 75  ? 0.4557 0.4583 0.3874 0.0108  -0.0230 0.0491  74  ILE   A N   
537  C CA  . ILE   A 75  ? 0.4643 0.4705 0.3861 0.0130  -0.0076 0.0374  74  ILE   A CA  
538  C C   . ILE   A 75  ? 0.4999 0.5008 0.3830 0.0150  -0.0129 0.0276  74  ILE   A C   
539  O O   . ILE   A 75  ? 0.5041 0.5012 0.3568 0.0138  -0.0189 0.0363  74  ILE   A O   
540  C CB  . ILE   A 75  ? 0.4626 0.4757 0.3826 0.0118  0.0114  0.0463  74  ILE   A CB  
541  C CG1 . ILE   A 75  ? 0.4452 0.4620 0.4020 0.0093  0.0152  0.0546  74  ILE   A CG1 
542  C CG2 . ILE   A 75  ? 0.4699 0.4885 0.3819 0.0153  0.0271  0.0330  74  ILE   A CG2 
543  C CD1 . ILE   A 75  ? 0.4461 0.4686 0.4039 0.0064  0.0304  0.0658  74  ILE   A CD1 
544  N N   . VAL   A 76  ? 0.5142 0.5130 0.3967 0.0181  -0.0117 0.0095  75  VAL   A N   
545  C CA  . VAL   A 76  ? 0.5582 0.5501 0.4046 0.0207  -0.0164 -0.0040 75  VAL   A CA  
546  C C   . VAL   A 76  ? 0.5919 0.5864 0.3986 0.0217  -0.0020 0.0006  75  VAL   A C   
547  O O   . VAL   A 76  ? 0.5863 0.5897 0.4009 0.0224  0.0180  0.0051  75  VAL   A O   
548  C CB  . VAL   A 76  ? 0.5706 0.5592 0.4297 0.0243  -0.0138 -0.0240 75  VAL   A CB  
549  C CG1 . VAL   A 76  ? 0.6002 0.5805 0.4216 0.0279  -0.0158 -0.0410 75  VAL   A CG1 
550  C CG2 . VAL   A 76  ? 0.5659 0.5510 0.4585 0.0219  -0.0288 -0.0264 75  VAL   A CG2 
551  N N   . ALA   A 77  ? 0.6261 0.6138 0.3923 0.0208  -0.0130 0.0026  76  ALA   A N   
552  C CA  . ALA   A 77  ? 0.6686 0.6583 0.3917 0.0207  0.0005  0.0098  76  ALA   A CA  
553  C C   . ALA   A 77  ? 0.6945 0.6870 0.3982 0.0260  0.0201  -0.0084 76  ALA   A C   
554  O O   . ALA   A 77  ? 0.7002 0.6860 0.4019 0.0300  0.0141  -0.0296 76  ALA   A O   
555  C CB  . ALA   A 77  ? 0.6895 0.6696 0.3697 0.0185  -0.0190 0.0157  76  ALA   A CB  
556  N N   . TYR   A 78  ? 0.7051 0.7076 0.3980 0.0261  0.0439  -0.0003 77  TYR   A N   
557  C CA  . TYR   A 78  ? 0.7259 0.7338 0.4011 0.0318  0.0660  -0.0164 77  TYR   A CA  
558  C C   . TYR   A 78  ? 0.7688 0.7706 0.3792 0.0318  0.0666  -0.0180 77  TYR   A C   
559  O O   . TYR   A 78  ? 0.7787 0.7805 0.3647 0.0263  0.0649  0.0034  77  TYR   A O   
560  C CB  . TYR   A 78  ? 0.7130 0.7378 0.4151 0.0310  0.0921  -0.0053 77  TYR   A CB  
561  C CG  . TYR   A 78  ? 0.7320 0.7665 0.4122 0.0360  0.1195  -0.0156 77  TYR   A CG  
562  C CD1 . TYR   A 78  ? 0.7354 0.7738 0.4361 0.0441  0.1302  -0.0379 77  TYR   A CD1 
563  C CD2 . TYR   A 78  ? 0.7541 0.7945 0.3955 0.0327  0.1358  -0.0023 77  TYR   A CD2 
564  C CE1 . TYR   A 78  ? 0.7471 0.7960 0.4322 0.0498  0.1569  -0.0487 77  TYR   A CE1 
565  C CE2 . TYR   A 78  ? 0.7690 0.8207 0.3918 0.0374  0.1641  -0.0119 77  TYR   A CE2 
566  C CZ  . TYR   A 78  ? 0.7713 0.8282 0.4184 0.0464  0.1752  -0.0358 77  TYR   A CZ  
567  O OH  . TYR   A 78  ? 0.7978 0.8670 0.4291 0.0521  0.2044  -0.0468 77  TYR   A OH  
568  N N   . HIS   A 79  ? 0.7968 0.7919 0.3779 0.0380  0.0686  -0.0430 78  HIS   A N   
569  C CA  . HIS   A 79  ? 0.8463 0.8342 0.3598 0.0386  0.0691  -0.0482 78  HIS   A CA  
570  C C   . HIS   A 79  ? 0.8692 0.8684 0.3574 0.0432  0.1032  -0.0553 78  HIS   A C   
571  O O   . HIS   A 79  ? 0.8995 0.8990 0.3335 0.0411  0.1121  -0.0474 78  HIS   A O   
572  C CB  . HIS   A 79  ? 0.8795 0.8502 0.3703 0.0421  0.0465  -0.0739 78  HIS   A CB  
573  C CG  . HIS   A 79  ? 0.9251 0.8855 0.4360 0.0372  0.0127  -0.0680 78  HIS   A CG  
574  N ND1 . HIS   A 79  ? 0.9547 0.9166 0.4683 0.0304  -0.0009 -0.0411 78  HIS   A ND1 
575  C CD2 . HIS   A 79  ? 0.9410 0.8903 0.4719 0.0383  -0.0090 -0.0859 78  HIS   A CD2 
576  C CE1 . HIS   A 79  ? 0.9576 0.9111 0.4944 0.0282  -0.0293 -0.0441 78  HIS   A CE1 
577  N NE2 . HIS   A 79  ? 0.9537 0.8998 0.5010 0.0321  -0.0350 -0.0701 78  HIS   A NE2 
578  N N   . GLY   A 80  ? 0.8530 0.8609 0.3780 0.0499  0.1213  -0.0713 79  GLY   A N   
579  C CA  . GLY   A 80  ? 0.8636 0.8843 0.3730 0.0558  0.1549  -0.0811 79  GLY   A CA  
580  C C   . GLY   A 80  ? 0.8608 0.8873 0.4160 0.0651  0.1673  -0.1033 79  GLY   A C   
581  O O   . GLY   A 80  ? 0.8482 0.8675 0.4452 0.0663  0.1491  -0.1095 79  GLY   A O   
582  N N   . SER   A 81  ? 0.8709 0.9113 0.4214 0.0718  0.1989  -0.1137 80  SER   A N   
583  C CA  . SER   A 81  ? 0.8750 0.9219 0.4729 0.0818  0.2111  -0.1339 80  SER   A CA  
584  C C   . SER   A 81  ? 0.9023 0.9537 0.4727 0.0928  0.2379  -0.1597 80  SER   A C   
585  O O   . SER   A 81  ? 0.9150 0.9700 0.4302 0.0918  0.2545  -0.1587 80  SER   A O   
586  C CB  . SER   A 81  ? 0.8642 0.9311 0.5256 0.0792  0.2222  -0.1153 80  SER   A CB  
587  O OG  . SER   A 81  ? 0.8923 0.9807 0.5476 0.0777  0.2536  -0.1035 80  SER   A OG  
588  N N   . TYR   A 82  ? 0.9120 0.9610 0.5190 0.1036  0.2407  -0.1839 81  TYR   A N   
589  C CA  . TYR   A 82  ? 0.9460 0.9977 0.5374 0.1163  0.2651  -0.2127 81  TYR   A CA  
590  C C   . TYR   A 82  ? 0.9428 1.0110 0.6044 0.1252  0.2817  -0.2188 81  TYR   A C   
591  O O   . TYR   A 82  ? 0.9309 0.9934 0.6433 0.1252  0.2622  -0.2160 81  TYR   A O   
592  C CB  . TYR   A 82  ? 0.9697 0.9932 0.5313 0.1227  0.2445  -0.2437 81  TYR   A CB  
593  C CG  . TYR   A 82  ? 1.0128 1.0179 0.5082 0.1144  0.2220  -0.2408 81  TYR   A CG  
594  C CD1 . TYR   A 82  ? 1.0258 1.0210 0.5298 0.1035  0.1901  -0.2207 81  TYR   A CD1 
595  C CD2 . TYR   A 82  ? 1.0568 1.0537 0.4820 0.1182  0.2312  -0.2599 81  TYR   A CD2 
596  C CE1 . TYR   A 82  ? 1.0621 1.0421 0.5102 0.0961  0.1680  -0.2166 81  TYR   A CE1 
597  C CE2 . TYR   A 82  ? 1.0961 1.0758 0.4600 0.1105  0.2075  -0.2567 81  TYR   A CE2 
598  C CZ  . TYR   A 82  ? 1.1034 1.0751 0.4814 0.0995  0.1751  -0.2344 81  TYR   A CZ  
599  O OH  . TYR   A 82  ? 1.1531 1.1092 0.4759 0.0922  0.1498  -0.2300 81  TYR   A OH  
600  N N   . LEU   A 83  ? 0.9487 1.0380 0.6143 0.1329  0.3173  -0.2266 82  LEU   A N   
601  C CA  . LEU   A 83  ? 0.9417 1.0473 0.6758 0.1432  0.3327  -0.2352 82  LEU   A CA  
602  C C   . LEU   A 83  ? 0.9713 1.0675 0.6912 0.1591  0.3454  -0.2730 82  LEU   A C   
603  O O   . LEU   A 83  ? 0.9874 1.0885 0.6572 0.1631  0.3698  -0.2857 82  LEU   A O   
604  C CB  . LEU   A 83  ? 0.9280 1.0676 0.6915 0.1405  0.3640  -0.2156 82  LEU   A CB  
605  C CG  . LEU   A 83  ? 0.9225 1.0817 0.7586 0.1522  0.3806  -0.2258 82  LEU   A CG  
606  C CD1 . LEU   A 83  ? 0.9130 1.0633 0.8088 0.1516  0.3507  -0.2193 82  LEU   A CD1 
607  C CD2 . LEU   A 83  ? 0.9155 1.1096 0.7776 0.1489  0.4130  -0.2081 82  LEU   A CD2 
608  N N   . TRP   A 84  ? 0.9775 1.0582 0.7380 0.1681  0.3281  -0.2913 83  TRP   A N   
609  C CA  . TRP   A 84  ? 1.0026 1.0694 0.7535 0.1837  0.3362  -0.3291 83  TRP   A CA  
610  C C   . TRP   A 84  ? 0.9866 1.0497 0.8106 0.1950  0.3285  -0.3409 83  TRP   A C   
611  O O   . TRP   A 84  ? 0.9833 1.0326 0.8381 0.1894  0.2986  -0.3294 83  TRP   A O   
612  C CB  . TRP   A 84  ? 1.0443 1.0778 0.7345 0.1803  0.3101  -0.3451 83  TRP   A CB  
613  C CG  . TRP   A 84  ? 1.0760 1.0899 0.7487 0.1950  0.3144  -0.3862 83  TRP   A CG  
614  C CD1 . TRP   A 84  ? 1.0927 1.0786 0.7881 0.2010  0.2894  -0.4070 83  TRP   A CD1 
615  C CD2 . TRP   A 84  ? 1.1041 1.1227 0.7293 0.2051  0.3451  -0.4121 83  TRP   A CD2 
616  N NE1 . TRP   A 84  ? 1.1184 1.0905 0.7866 0.2147  0.3019  -0.4457 83  TRP   A NE1 
617  C CE2 . TRP   A 84  ? 1.1267 1.1186 0.7493 0.2178  0.3364  -0.4505 83  TRP   A CE2 
618  C CE3 . TRP   A 84  ? 1.1204 1.1634 0.7057 0.2045  0.3805  -0.4064 83  TRP   A CE3 
619  C CZ2 . TRP   A 84  ? 1.1608 1.1494 0.7410 0.2306  0.3616  -0.4852 83  TRP   A CZ2 
620  C CZ3 . TRP   A 84  ? 1.1542 1.1947 0.6936 0.2163  0.4063  -0.4391 83  TRP   A CZ3 
621  C CH2 . TRP   A 84  ? 1.1716 1.1855 0.7093 0.2299  0.3974  -0.4793 83  TRP   A CH2 
622  N N   . LEU   A 85  ? 0.9779 1.0533 0.8295 0.2111  0.3558  -0.3634 84  LEU   A N   
623  C CA  . LEU   A 85  ? 0.9639 1.0361 0.8861 0.2248  0.3514  -0.3775 84  LEU   A CA  
624  C C   . LEU   A 85  ? 0.9292 1.0102 0.9169 0.2182  0.3321  -0.3487 84  LEU   A C   
625  O O   . LEU   A 85  ? 0.9296 0.9899 0.9510 0.2208  0.3059  -0.3518 84  LEU   A O   
626  C CB  . LEU   A 85  ? 0.9942 1.0285 0.9016 0.2328  0.3298  -0.4081 84  LEU   A CB  
627  C CG  . LEU   A 85  ? 1.0535 1.0757 0.8984 0.2414  0.3467  -0.4422 84  LEU   A CG  
628  C CD1 . LEU   A 85  ? 1.0865 1.0685 0.9204 0.2465  0.3193  -0.4700 84  LEU   A CD1 
629  C CD2 . LEU   A 85  ? 1.0497 1.0961 0.9150 0.2583  0.3883  -0.4624 84  LEU   A CD2 
630  N N   . GLN   A 86  ? 0.8988 1.0092 0.9022 0.2089  0.3448  -0.3205 85  GLN   A N   
631  C CA  . GLN   A 86  ? 0.8668 0.9884 0.9261 0.2013  0.3285  -0.2925 85  GLN   A CA  
632  C C   . GLN   A 86  ? 0.8593 0.9589 0.9009 0.1866  0.2928  -0.2736 85  GLN   A C   
633  O O   . GLN   A 86  ? 0.8463 0.9493 0.9304 0.1811  0.2756  -0.2540 85  GLN   A O   
634  C CB  . GLN   A 86  ? 0.8715 0.9972 1.0052 0.2152  0.3260  -0.3016 85  GLN   A CB  
635  C CG  . GLN   A 86  ? 0.9158 1.0697 1.0831 0.2296  0.3619  -0.3162 85  GLN   A CG  
636  C CD  . GLN   A 86  ? 0.9766 1.1674 1.1545 0.2208  0.3855  -0.2931 85  GLN   A CD  
637  O OE1 . GLN   A 86  ? 1.0039 1.2151 1.1617 0.2244  0.4201  -0.3013 85  GLN   A OE1 
638  N NE2 . GLN   A 86  ? 0.9661 1.1656 1.1748 0.2085  0.3676  -0.2637 85  GLN   A NE2 
639  N N   . LYS   A 87  ? 0.8615 0.9392 0.8412 0.1805  0.2813  -0.2800 86  LYS   A N   
640  C CA  . LYS   A 87  ? 0.8478 0.9064 0.8112 0.1672  0.2495  -0.2636 86  LYS   A CA  
641  C C   . LYS   A 87  ? 0.8360 0.8996 0.7438 0.1542  0.2525  -0.2472 86  LYS   A C   
642  O O   . LYS   A 87  ? 0.8607 0.9237 0.7171 0.1563  0.2680  -0.2598 86  LYS   A O   
643  C CB  . LYS   A 87  ? 0.8836 0.9085 0.8351 0.1712  0.2256  -0.2848 86  LYS   A CB  
644  C CG  . LYS   A 87  ? 0.9214 0.9389 0.9323 0.1830  0.2193  -0.2962 86  LYS   A CG  
645  C CD  . LYS   A 87  ? 0.9965 0.9793 1.0028 0.1859  0.1950  -0.3151 86  LYS   A CD  
646  C CE  . LYS   A 87  ? 1.0810 1.0473 1.0383 0.1929  0.2022  -0.3465 86  LYS   A CE  
647  N NZ  . LYS   A 87  ? 1.1187 1.0518 1.0879 0.1988  0.1811  -0.3686 86  LYS   A NZ  
648  N N   . LEU   A 88  ? 0.7944 0.8637 0.7131 0.1411  0.2389  -0.2187 87  LEU   A N   
649  C CA  . LEU   A 88  ? 0.7797 0.8523 0.6537 0.1285  0.2383  -0.1996 87  LEU   A CA  
650  C C   . LEU   A 88  ? 0.7840 0.8305 0.6306 0.1211  0.2067  -0.1987 87  LEU   A C   
651  O O   . LEU   A 88  ? 0.7739 0.8102 0.6534 0.1187  0.1848  -0.1936 87  LEU   A O   
652  C CB  . LEU   A 88  ? 0.7524 0.8470 0.6598 0.1194  0.2433  -0.1705 87  LEU   A CB  
653  C CG  . LEU   A 88  ? 0.7710 0.8658 0.6428 0.1055  0.2370  -0.1470 87  LEU   A CG  
654  C CD1 . LEU   A 88  ? 0.7878 0.8913 0.6093 0.1047  0.2607  -0.1473 87  LEU   A CD1 
655  C CD2 . LEU   A 88  ? 0.7520 0.8609 0.6655 0.0965  0.2333  -0.1210 87  LEU   A CD2 
656  N N   . TRP   A 89  ? 0.7916 0.8279 0.5785 0.1177  0.2042  -0.2036 88  TRP   A N   
657  C CA  . TRP   A 89  ? 0.7987 0.8116 0.5592 0.1110  0.1743  -0.2045 88  TRP   A CA  
658  C C   . TRP   A 89  ? 0.7864 0.8040 0.5182 0.0986  0.1674  -0.1790 88  TRP   A C   
659  O O   . TRP   A 89  ? 0.7997 0.8259 0.4909 0.0969  0.1837  -0.1741 88  TRP   A O   
660  C CB  . TRP   A 89  ? 0.8285 0.8227 0.5422 0.1178  0.1721  -0.2339 88  TRP   A CB  
661  C CG  . TRP   A 89  ? 0.8374 0.8200 0.5800 0.1301  0.1728  -0.2615 88  TRP   A CG  
662  C CD1 . TRP   A 89  ? 0.8474 0.8397 0.6047 0.1431  0.1987  -0.2797 88  TRP   A CD1 
663  C CD2 . TRP   A 89  ? 0.8459 0.8035 0.6051 0.1308  0.1460  -0.2748 88  TRP   A CD2 
664  N NE1 . TRP   A 89  ? 0.8506 0.8234 0.6316 0.1526  0.1886  -0.3044 88  TRP   A NE1 
665  C CE2 . TRP   A 89  ? 0.8536 0.8045 0.6365 0.1445  0.1561  -0.3008 88  TRP   A CE2 
666  C CE3 . TRP   A 89  ? 0.8559 0.7967 0.6159 0.1209  0.1150  -0.2667 88  TRP   A CE3 
667  C CZ2 . TRP   A 89  ? 0.8597 0.7855 0.6654 0.1480  0.1352  -0.3177 88  TRP   A CZ2 
668  C CZ3 . TRP   A 89  ? 0.8658 0.7840 0.6484 0.1237  0.0958  -0.2832 88  TRP   A CZ3 
669  C CH2 . TRP   A 89  ? 0.8634 0.7732 0.6680 0.1368  0.1054  -0.3078 88  TRP   A CH2 
670  N N   . ILE   A 90  ? 0.7542 0.7662 0.5079 0.0900  0.1443  -0.1621 89  ILE   A N   
671  C CA  . ILE   A 90  ? 0.7479 0.7619 0.4811 0.0788  0.1344  -0.1380 89  ILE   A CA  
672  C C   . ILE   A 90  ? 0.7539 0.7470 0.4576 0.0744  0.1059  -0.1432 89  ILE   A C   
673  O O   . ILE   A 90  ? 0.7516 0.7321 0.4804 0.0744  0.0866  -0.1508 89  ILE   A O   
674  C CB  . ILE   A 90  ? 0.7310 0.7563 0.5131 0.0727  0.1312  -0.1149 89  ILE   A CB  
675  C CG1 . ILE   A 90  ? 0.7244 0.7724 0.5301 0.0748  0.1586  -0.1065 89  ILE   A CG1 
676  C CG2 . ILE   A 90  ? 0.7374 0.7594 0.5065 0.0619  0.1143  -0.0926 89  ILE   A CG2 
677  C CD1 . ILE   A 90  ? 0.7216 0.7786 0.5805 0.0715  0.1547  -0.0925 89  ILE   A CD1 
678  N N   . CYS   A 91  ? 0.7569 0.7468 0.4086 0.0703  0.1031  -0.1379 90  CYS   A N   
679  C CA  . CYS   A 91  ? 0.7680 0.7405 0.3907 0.0655  0.0748  -0.1408 90  CYS   A CA  
680  C C   . CYS   A 91  ? 0.7425 0.7188 0.3814 0.0559  0.0598  -0.1130 90  CYS   A C   
681  O O   . CYS   A 91  ? 0.7351 0.7239 0.3692 0.0519  0.0722  -0.0917 90  CYS   A O   
682  C CB  . CYS   A 91  ? 0.8171 0.7830 0.3708 0.0668  0.0779  -0.1508 90  CYS   A CB  
683  S SG  . CYS   A 91  ? 0.8898 0.8333 0.4059 0.0615  0.0396  -0.1579 90  CYS   A SG  
684  N N   . MET   A 92  ? 0.7214 0.6873 0.3832 0.0521  0.0339  -0.1131 91  MET   A N   
685  C CA  . MET   A 92  ? 0.7042 0.6735 0.3862 0.0442  0.0194  -0.0895 91  MET   A CA  
686  C C   . MET   A 92  ? 0.7087 0.6644 0.3856 0.0398  -0.0117 -0.0926 91  MET   A C   
687  O O   . MET   A 92  ? 0.7154 0.6584 0.3828 0.0423  -0.0229 -0.1140 91  MET   A O   
688  C CB  . MET   A 92  ? 0.6823 0.6612 0.4219 0.0437  0.0267  -0.0806 91  MET   A CB  
689  C CG  . MET   A 92  ? 0.6942 0.6648 0.4665 0.0465  0.0179  -0.0965 91  MET   A CG  
690  S SD  . MET   A 92  ? 0.7112 0.6927 0.5404 0.0486  0.0317  -0.0910 91  MET   A SD  
691  C CE  . MET   A 92  ? 0.7977 0.7646 0.6405 0.0548  0.0253  -0.1160 91  MET   A CE  
692  N N   . GLU   A 93  ? 0.6999 0.6583 0.3868 0.0334  -0.0261 -0.0719 92  GLU   A N   
693  C CA  . GLU   A 93  ? 0.7052 0.6542 0.3958 0.0290  -0.0558 -0.0726 92  GLU   A CA  
694  C C   . GLU   A 93  ? 0.6833 0.6268 0.4162 0.0291  -0.0652 -0.0865 92  GLU   A C   
695  O O   . GLU   A 93  ? 0.6740 0.6238 0.4468 0.0301  -0.0533 -0.0837 92  GLU   A O   
696  C CB  . GLU   A 93  ? 0.7502 0.7055 0.4577 0.0236  -0.0661 -0.0472 92  GLU   A CB  
697  C CG  . GLU   A 93  ? 0.8556 0.8043 0.5715 0.0194  -0.0968 -0.0463 92  GLU   A CG  
698  C CD  . GLU   A 93  ? 0.9790 0.9352 0.7458 0.0159  -0.1046 -0.0304 92  GLU   A CD  
699  O OE1 . GLU   A 93  ? 0.9914 0.9446 0.7774 0.0128  -0.1274 -0.0322 92  GLU   A OE1 
700  O OE2 . GLU   A 93  ? 1.0096 0.9748 0.7981 0.0161  -0.0879 -0.0170 92  GLU   A OE2 
701  N N   . PHE   A 94  ? 0.6771 0.6083 0.4011 0.0274  -0.0876 -0.1006 93  PHE   A N   
702  C CA  . PHE   A 94  ? 0.6686 0.5927 0.4313 0.0260  -0.0983 -0.1129 93  PHE   A CA  
703  C C   . PHE   A 94  ? 0.6469 0.5772 0.4517 0.0195  -0.1132 -0.0970 93  PHE   A C   
704  O O   . PHE   A 94  ? 0.6631 0.5947 0.4589 0.0157  -0.1307 -0.0874 93  PHE   A O   
705  C CB  . PHE   A 94  ? 0.6874 0.5947 0.4233 0.0263  -0.1163 -0.1366 93  PHE   A CB  
706  C CG  . PHE   A 94  ? 0.6937 0.5912 0.4695 0.0235  -0.1299 -0.1490 93  PHE   A CG  
707  C CD1 . PHE   A 94  ? 0.6983 0.5938 0.5053 0.0269  -0.1152 -0.1558 93  PHE   A CD1 
708  C CD2 . PHE   A 94  ? 0.7070 0.5965 0.4883 0.0172  -0.1583 -0.1543 93  PHE   A CD2 
709  C CE1 . PHE   A 94  ? 0.6994 0.5842 0.5423 0.0235  -0.1276 -0.1652 93  PHE   A CE1 
710  C CE2 . PHE   A 94  ? 0.7093 0.5895 0.5293 0.0134  -0.1701 -0.1650 93  PHE   A CE2 
711  C CZ  . PHE   A 94  ? 0.6974 0.5747 0.5470 0.0164  -0.1541 -0.1698 93  PHE   A CZ  
712  N N   . CYS   A 95  ? 0.6110 0.5458 0.4613 0.0185  -0.1055 -0.0934 94  CYS   A N   
713  C CA  . CYS   A 95  ? 0.5873 0.5292 0.4797 0.0129  -0.1153 -0.0800 94  CYS   A CA  
714  C C   . CYS   A 95  ? 0.5798 0.5127 0.5000 0.0094  -0.1277 -0.0927 94  CYS   A C   
715  O O   . CYS   A 95  ? 0.5679 0.4993 0.5129 0.0102  -0.1167 -0.0958 94  CYS   A O   
716  C CB  . CYS   A 95  ? 0.5680 0.5217 0.4871 0.0138  -0.0958 -0.0655 94  CYS   A CB  
717  S SG  . CYS   A 95  ? 0.5881 0.5521 0.4843 0.0156  -0.0837 -0.0474 94  CYS   A SG  
718  N N   . GLY   A 96  ? 0.5852 0.5115 0.5002 0.0053  -0.1517 -0.0996 95  GLY   A N   
719  C CA  . GLY   A 96  ? 0.5865 0.5019 0.5239 0.0006  -0.1679 -0.1136 95  GLY   A CA  
720  C C   . GLY   A 96  ? 0.5741 0.4932 0.5649 -0.0043 -0.1646 -0.1075 95  GLY   A C   
721  O O   . GLY   A 96  ? 0.5789 0.4859 0.5850 -0.0062 -0.1684 -0.1199 95  GLY   A O   
722  N N   . ALA   A 97  ? 0.5492 0.4839 0.5683 -0.0065 -0.1571 -0.0885 96  ALA   A N   
723  C CA  . ALA   A 97  ? 0.5258 0.4650 0.5918 -0.0116 -0.1524 -0.0820 96  ALA   A CA  
724  C C   . ALA   A 97  ? 0.5129 0.4517 0.5852 -0.0081 -0.1300 -0.0789 96  ALA   A C   
725  O O   . ALA   A 97  ? 0.5049 0.4456 0.6107 -0.0125 -0.1251 -0.0729 96  ALA   A O   
726  C CB  . ALA   A 97  ? 0.5105 0.4662 0.6070 -0.0158 -0.1561 -0.0659 96  ALA   A CB  
727  N N   . GLY   A 98  ? 0.5040 0.4403 0.5446 -0.0007 -0.1170 -0.0829 97  GLY   A N   
728  C CA  . GLY   A 98  ? 0.4739 0.4105 0.5201 0.0034  -0.0979 -0.0805 97  GLY   A CA  
729  C C   . GLY   A 98  ? 0.4463 0.3978 0.5075 0.0027  -0.0853 -0.0631 97  GLY   A C   
730  O O   . GLY   A 98  ? 0.4497 0.4112 0.5076 0.0018  -0.0876 -0.0539 97  GLY   A O   
731  N N   . SER   A 99  ? 0.4110 0.3631 0.4890 0.0032  -0.0733 -0.0587 98  SER   A N   
732  C CA  . SER   A 99  ? 0.3896 0.3541 0.4794 0.0026  -0.0614 -0.0445 98  SER   A CA  
733  C C   . SER   A 99  ? 0.3726 0.3435 0.4924 -0.0043 -0.0647 -0.0353 98  SER   A C   
734  O O   . SER   A 99  ? 0.3775 0.3430 0.5150 -0.0095 -0.0744 -0.0386 98  SER   A O   
735  C CB  . SER   A 99  ? 0.3819 0.3448 0.4732 0.0065  -0.0481 -0.0436 98  SER   A CB  
736  O OG  . SER   A 99  ? 0.3885 0.3439 0.5008 0.0031  -0.0496 -0.0431 98  SER   A OG  
737  N N   . LEU   A 100 ? 0.3610 0.3432 0.4889 -0.0046 -0.0550 -0.0244 99  LEU   A N   
738  C CA  . LEU   A 100 ? 0.3493 0.3392 0.5051 -0.0101 -0.0533 -0.0163 99  LEU   A CA  
739  C C   . LEU   A 100 ? 0.3452 0.3288 0.5152 -0.0140 -0.0490 -0.0151 99  LEU   A C   
740  O O   . LEU   A 100 ? 0.3526 0.3393 0.5464 -0.0203 -0.0510 -0.0111 99  LEU   A O   
741  C CB  . LEU   A 100 ? 0.3460 0.3470 0.5038 -0.0084 -0.0426 -0.0076 99  LEU   A CB  
742  C CG  . LEU   A 100 ? 0.3686 0.3760 0.5234 -0.0064 -0.0492 -0.0053 99  LEU   A CG  
743  C CD1 . LEU   A 100 ? 0.3730 0.3878 0.5286 -0.0038 -0.0384 0.0017  99  LEU   A CD1 
744  C CD2 . LEU   A 100 ? 0.3793 0.3923 0.5599 -0.0107 -0.0605 -0.0042 99  LEU   A CD2 
745  N N   . GLN   A 101 ? 0.3493 0.3245 0.5072 -0.0104 -0.0434 -0.0175 100 GLN   A N   
746  C CA  . GLN   A 101 ? 0.3378 0.3042 0.5084 -0.0139 -0.0418 -0.0149 100 GLN   A CA  
747  C C   . GLN   A 101 ? 0.3500 0.3046 0.5321 -0.0179 -0.0549 -0.0225 100 GLN   A C   
748  O O   . GLN   A 101 ? 0.3579 0.3099 0.5622 -0.0251 -0.0566 -0.0170 100 GLN   A O   
749  C CB  . GLN   A 101 ? 0.3322 0.2916 0.4906 -0.0082 -0.0359 -0.0160 100 GLN   A CB  
750  C CG  . GLN   A 101 ? 0.3491 0.2984 0.5217 -0.0122 -0.0357 -0.0099 100 GLN   A CG  
751  C CD  . GLN   A 101 ? 0.3711 0.3136 0.5365 -0.0061 -0.0322 -0.0095 100 GLN   A CD  
752  O OE1 . GLN   A 101 ? 0.4024 0.3306 0.5756 -0.0053 -0.0372 -0.0115 100 GLN   A OE1 
753  N NE2 . GLN   A 101 ? 0.3381 0.2902 0.4920 -0.0020 -0.0248 -0.0068 100 GLN   A NE2 
754  N N   . ASP   A 102 ? 0.3661 0.3133 0.5327 -0.0136 -0.0641 -0.0355 101 ASP   A N   
755  C CA  . ASP   A 102 ? 0.3754 0.3100 0.5510 -0.0174 -0.0787 -0.0456 101 ASP   A CA  
756  C C   . ASP   A 102 ? 0.3706 0.3135 0.5711 -0.0262 -0.0873 -0.0405 101 ASP   A C   
757  O O   . ASP   A 102 ? 0.3744 0.3091 0.5972 -0.0331 -0.0964 -0.0424 101 ASP   A O   
758  C CB  . ASP   A 102 ? 0.4024 0.3303 0.5507 -0.0112 -0.0869 -0.0613 101 ASP   A CB  
759  C CG  . ASP   A 102 ? 0.4725 0.3943 0.5996 -0.0020 -0.0775 -0.0683 101 ASP   A CG  
760  O OD1 . ASP   A 102 ? 0.4748 0.3894 0.6136 -0.0007 -0.0717 -0.0658 101 ASP   A OD1 
761  O OD2 . ASP   A 102 ? 0.4840 0.4086 0.5836 0.0040  -0.0758 -0.0755 101 ASP   A OD2 
762  N N   . ILE   A 103 ? 0.3624 0.3217 0.5634 -0.0260 -0.0841 -0.0334 102 ILE   A N   
763  C CA  . ILE   A 103 ? 0.3355 0.3057 0.5642 -0.0329 -0.0911 -0.0284 102 ILE   A CA  
764  C C   . ILE   A 103 ? 0.3201 0.2986 0.5781 -0.0395 -0.0793 -0.0158 102 ILE   A C   
765  O O   . ILE   A 103 ? 0.3090 0.2869 0.5962 -0.0479 -0.0856 -0.0142 102 ILE   A O   
766  C CB  . ILE   A 103 ? 0.3393 0.3222 0.5585 -0.0288 -0.0940 -0.0265 102 ILE   A CB  
767  C CG1 . ILE   A 103 ? 0.3507 0.3247 0.5395 -0.0242 -0.1078 -0.0380 102 ILE   A CG1 
768  C CG2 . ILE   A 103 ? 0.3279 0.3256 0.5828 -0.0346 -0.0994 -0.0198 102 ILE   A CG2 
769  C CD1 . ILE   A 103 ? 0.3602 0.3438 0.5324 -0.0193 -0.1086 -0.0334 102 ILE   A CD1 
770  N N   . TYR   A 104 ? 0.3145 0.3002 0.5647 -0.0366 -0.0623 -0.0072 103 TYR   A N   
771  C CA  . TYR   A 104 ? 0.3117 0.3056 0.5843 -0.0429 -0.0497 0.0043  103 TYR   A CA  
772  C C   . TYR   A 104 ? 0.3348 0.3153 0.6171 -0.0492 -0.0491 0.0081  103 TYR   A C   
773  O O   . TYR   A 104 ? 0.3448 0.3314 0.6510 -0.0572 -0.0421 0.0179  103 TYR   A O   
774  C CB  . TYR   A 104 ? 0.2971 0.3013 0.5580 -0.0389 -0.0330 0.0112  103 TYR   A CB  
775  C CG  . TYR   A 104 ? 0.3131 0.3086 0.5465 -0.0337 -0.0258 0.0118  103 TYR   A CG  
776  C CD1 . TYR   A 104 ? 0.3145 0.2994 0.5467 -0.0368 -0.0221 0.0171  103 TYR   A CD1 
777  C CD2 . TYR   A 104 ? 0.3021 0.3013 0.5142 -0.0262 -0.0220 0.0092  103 TYR   A CD2 
778  C CE1 . TYR   A 104 ? 0.3302 0.3084 0.5406 -0.0316 -0.0175 0.0181  103 TYR   A CE1 
779  C CE2 . TYR   A 104 ? 0.3270 0.3202 0.5187 -0.0219 -0.0164 0.0098  103 TYR   A CE2 
780  C CZ  . TYR   A 104 ? 0.3370 0.3205 0.5285 -0.0243 -0.0146 0.0140  103 TYR   A CZ  
781  O OH  . TYR   A 104 ? 0.3656 0.3447 0.5404 -0.0196 -0.0109 0.0151  103 TYR   A OH  
782  N N   . GLN   A 105 ? 0.3367 0.2993 0.6030 -0.0457 -0.0560 0.0010  104 GLN   A N   
783  C CA  . GLN   A 105 ? 0.3551 0.3021 0.6336 -0.0513 -0.0578 0.0048  104 GLN   A CA  
784  C C   . GLN   A 105 ? 0.3634 0.3026 0.6686 -0.0592 -0.0733 -0.0010 104 GLN   A C   
785  O O   . GLN   A 105 ? 0.3800 0.3021 0.6968 -0.0635 -0.0789 -0.0009 104 GLN   A O   
786  C CB  . GLN   A 105 ? 0.3851 0.3163 0.6409 -0.0435 -0.0578 0.0002  104 GLN   A CB  
787  C CG  . GLN   A 105 ? 0.4136 0.3521 0.6503 -0.0384 -0.0438 0.0087  104 GLN   A CG  
788  C CD  . GLN   A 105 ? 0.4380 0.3626 0.6602 -0.0313 -0.0444 0.0062  104 GLN   A CD  
789  O OE1 . GLN   A 105 ? 0.4562 0.3712 0.6712 -0.0250 -0.0521 -0.0070 104 GLN   A OE1 
790  N NE2 . GLN   A 105 ? 0.4017 0.3259 0.6190 -0.0316 -0.0363 0.0184  104 GLN   A NE2 
791  N N   . VAL   A 106 ? 0.3671 0.3180 0.6836 -0.0610 -0.0818 -0.0062 105 VAL   A N   
792  C CA  . VAL   A 106 ? 0.3744 0.3240 0.7217 -0.0698 -0.0970 -0.0103 105 VAL   A CA  
793  C C   . VAL   A 106 ? 0.3613 0.3342 0.7391 -0.0762 -0.0899 0.0006  105 VAL   A C   
794  O O   . VAL   A 106 ? 0.3667 0.3427 0.7781 -0.0866 -0.0866 0.0098  105 VAL   A O   
795  C CB  . VAL   A 106 ? 0.4048 0.3459 0.7399 -0.0662 -0.1182 -0.0283 105 VAL   A CB  
796  C CG1 . VAL   A 106 ? 0.4035 0.3465 0.7764 -0.0770 -0.1354 -0.0311 105 VAL   A CG1 
797  C CG2 . VAL   A 106 ? 0.4282 0.3457 0.7374 -0.0601 -0.1233 -0.0410 105 VAL   A CG2 
798  N N   . THR   A 107 ? 0.3531 0.3426 0.7218 -0.0698 -0.0866 0.0003  106 THR   A N   
799  C CA  . THR   A 107 ? 0.3474 0.3602 0.7479 -0.0736 -0.0808 0.0080  106 THR   A CA  
800  C C   . THR   A 107 ? 0.3591 0.3848 0.7708 -0.0766 -0.0564 0.0220  106 THR   A C   
801  O O   . THR   A 107 ? 0.3406 0.3849 0.7865 -0.0815 -0.0500 0.0280  106 THR   A O   
802  C CB  . THR   A 107 ? 0.3425 0.3663 0.7272 -0.0642 -0.0845 0.0037  106 THR   A CB  
803  O OG1 . THR   A 107 ? 0.3345 0.3576 0.6867 -0.0560 -0.0689 0.0063  106 THR   A OG1 
804  C CG2 . THR   A 107 ? 0.3508 0.3650 0.7192 -0.0607 -0.1077 -0.0088 106 THR   A CG2 
805  N N   . GLY   A 108 ? 0.3755 0.3929 0.7568 -0.0725 -0.0429 0.0260  107 GLY   A N   
806  C CA  . GLY   A 108 ? 0.3685 0.3977 0.7498 -0.0736 -0.0204 0.0372  107 GLY   A CA  
807  C C   . GLY   A 108 ? 0.3505 0.3918 0.7157 -0.0640 -0.0134 0.0337  107 GLY   A C   
808  O O   . GLY   A 108 ? 0.3433 0.3827 0.6962 -0.0570 -0.0257 0.0250  107 GLY   A O   
809  N N   . SER   A 109 ? 0.3312 0.3843 0.6962 -0.0639 0.0064  0.0405  108 SER   A N   
810  C CA  . SER   A 109 ? 0.3325 0.3939 0.6819 -0.0551 0.0145  0.0370  108 SER   A CA  
811  C C   . SER   A 109 ? 0.3120 0.3851 0.6808 -0.0502 0.0050  0.0309  108 SER   A C   
812  O O   . SER   A 109 ? 0.2966 0.3818 0.7032 -0.0547 0.0007  0.0321  108 SER   A O   
813  C CB  . SER   A 109 ? 0.3469 0.4185 0.6955 -0.0569 0.0375  0.0436  108 SER   A CB  
814  O OG  . SER   A 109 ? 0.3850 0.4756 0.7736 -0.0613 0.0455  0.0463  108 SER   A OG  
815  N N   . LEU   A 110 ? 0.3111 0.3807 0.6561 -0.0413 0.0011  0.0257  109 LEU   A N   
816  C CA  . LEU   A 110 ? 0.2885 0.3668 0.6474 -0.0358 -0.0085 0.0221  109 LEU   A CA  
817  C C   . LEU   A 110 ? 0.2856 0.3817 0.6715 -0.0340 0.0067  0.0241  109 LEU   A C   
818  O O   . LEU   A 110 ? 0.2874 0.3865 0.6664 -0.0347 0.0261  0.0262  109 LEU   A O   
819  C CB  . LEU   A 110 ? 0.2832 0.3512 0.6075 -0.0276 -0.0149 0.0181  109 LEU   A CB  
820  C CG  . LEU   A 110 ? 0.3051 0.3608 0.6112 -0.0269 -0.0339 0.0136  109 LEU   A CG  
821  C CD1 . LEU   A 110 ? 0.3189 0.3611 0.6094 -0.0311 -0.0341 0.0121  109 LEU   A CD1 
822  C CD2 . LEU   A 110 ? 0.3230 0.3731 0.6010 -0.0193 -0.0383 0.0117  109 LEU   A CD2 
823  N N   . SER   A 111 ? 0.2691 0.3769 0.6859 -0.0312 -0.0026 0.0230  110 SER   A N   
824  C CA  . SER   A 111 ? 0.2548 0.3797 0.7018 -0.0275 0.0107  0.0232  110 SER   A CA  
825  C C   . SER   A 111 ? 0.2665 0.3855 0.6887 -0.0184 0.0166  0.0198  110 SER   A C   
826  O O   . SER   A 111 ? 0.2780 0.3826 0.6673 -0.0152 0.0061  0.0187  110 SER   A O   
827  C CB  . SER   A 111 ? 0.2397 0.3785 0.7315 -0.0267 -0.0043 0.0236  110 SER   A CB  
828  O OG  . SER   A 111 ? 0.2764 0.4078 0.7548 -0.0193 -0.0223 0.0220  110 SER   A OG  
829  N N   . GLU   A 112 ? 0.2623 0.3929 0.7033 -0.0140 0.0330  0.0175  111 GLU   A N   
830  C CA  . GLU   A 112 ? 0.2794 0.4029 0.7005 -0.0057 0.0377  0.0132  111 GLU   A CA  
831  C C   . GLU   A 112 ? 0.2894 0.4069 0.7119 0.0005  0.0171  0.0142  111 GLU   A C   
832  O O   . GLU   A 112 ? 0.3017 0.4059 0.6937 0.0043  0.0137  0.0136  111 GLU   A O   
833  C CB  . GLU   A 112 ? 0.2796 0.4150 0.7210 -0.0016 0.0588  0.0082  111 GLU   A CB  
834  C CG  . GLU   A 112 ? 0.3026 0.4278 0.7235 0.0062  0.0629  0.0022  111 GLU   A CG  
835  C CD  . GLU   A 112 ? 0.3401 0.4753 0.7780 0.0108  0.0848  -0.0058 111 GLU   A CD  
836  O OE1 . GLU   A 112 ? 0.3360 0.4795 0.7723 0.0056  0.1030  -0.0065 111 GLU   A OE1 
837  O OE2 . GLU   A 112 ? 0.3491 0.4828 0.8009 0.0194  0.0842  -0.0114 111 GLU   A OE2 
838  N N   . LEU   A 113 ? 0.2658 0.3928 0.7223 0.0006  0.0025  0.0170  112 LEU   A N   
839  C CA  . LEU   A 113 ? 0.2675 0.3889 0.7245 0.0060  -0.0191 0.0202  112 LEU   A CA  
840  C C   . LEU   A 113 ? 0.2722 0.3777 0.6875 0.0031  -0.0339 0.0222  112 LEU   A C   
841  O O   . LEU   A 113 ? 0.2862 0.3808 0.6778 0.0075  -0.0412 0.0245  112 LEU   A O   
842  C CB  . LEU   A 113 ? 0.2489 0.3858 0.7549 0.0065  -0.0332 0.0230  112 LEU   A CB  
843  C CG  . LEU   A 113 ? 0.2731 0.4243 0.8231 0.0140  -0.0229 0.0211  112 LEU   A CG  
844  C CD1 . LEU   A 113 ? 0.2544 0.4252 0.8609 0.0133  -0.0346 0.0237  112 LEU   A CD1 
845  C CD2 . LEU   A 113 ? 0.3012 0.4413 0.8406 0.0233  -0.0287 0.0224  112 LEU   A CD2 
846  N N   . GLN   A 114 ? 0.2571 0.3603 0.6627 -0.0044 -0.0363 0.0213  113 GLN   A N   
847  C CA  . GLN   A 114 ? 0.2589 0.3467 0.6249 -0.0066 -0.0477 0.0206  113 GLN   A CA  
848  C C   . GLN   A 114 ? 0.2713 0.3474 0.5988 -0.0041 -0.0358 0.0195  113 GLN   A C   
849  O O   . GLN   A 114 ? 0.2889 0.3548 0.5883 -0.0012 -0.0438 0.0206  113 GLN   A O   
850  C CB  . GLN   A 114 ? 0.2493 0.3363 0.6189 -0.0148 -0.0502 0.0185  113 GLN   A CB  
851  C CG  . GLN   A 114 ? 0.2618 0.3584 0.6671 -0.0181 -0.0679 0.0191  113 GLN   A CG  
852  C CD  . GLN   A 114 ? 0.2749 0.3733 0.6973 -0.0274 -0.0684 0.0177  113 GLN   A CD  
853  O OE1 . GLN   A 114 ? 0.2559 0.3521 0.6723 -0.0315 -0.0516 0.0183  113 GLN   A OE1 
854  N NE2 . GLN   A 114 ? 0.2421 0.3447 0.6886 -0.0313 -0.0886 0.0167  113 GLN   A NE2 
855  N N   . ILE   A 115 ? 0.2643 0.3427 0.5910 -0.0053 -0.0166 0.0178  114 ILE   A N   
856  C CA  . ILE   A 115 ? 0.2679 0.3364 0.5622 -0.0032 -0.0067 0.0164  114 ILE   A CA  
857  C C   . ILE   A 115 ? 0.2719 0.3378 0.5637 0.0033  -0.0082 0.0174  114 ILE   A C   
858  O O   . ILE   A 115 ? 0.2886 0.3449 0.5539 0.0049  -0.0113 0.0186  114 ILE   A O   
859  C CB  . ILE   A 115 ? 0.2693 0.3414 0.5642 -0.0058 0.0122  0.0146  114 ILE   A CB  
860  C CG1 . ILE   A 115 ? 0.2742 0.3462 0.5703 -0.0131 0.0131  0.0162  114 ILE   A CG1 
861  C CG2 . ILE   A 115 ? 0.2715 0.3344 0.5360 -0.0035 0.0203  0.0125  114 ILE   A CG2 
862  C CD1 . ILE   A 115 ? 0.2969 0.3734 0.5942 -0.0169 0.0317  0.0172  114 ILE   A CD1 
863  N N   . SER   A 116 ? 0.2523 0.3270 0.5752 0.0071  -0.0073 0.0177  115 SER   A N   
864  C CA  . SER   A 116 ? 0.2523 0.3229 0.5784 0.0134  -0.0101 0.0195  115 SER   A CA  
865  C C   . SER   A 116 ? 0.2478 0.3096 0.5555 0.0145  -0.0280 0.0263  115 SER   A C   
866  O O   . SER   A 116 ? 0.2580 0.3103 0.5458 0.0164  -0.0275 0.0290  115 SER   A O   
867  C CB  . SER   A 116 ? 0.2567 0.3389 0.6261 0.0181  -0.0091 0.0188  115 SER   A CB  
868  O OG  . SER   A 116 ? 0.2923 0.3826 0.6755 0.0180  0.0107  0.0118  115 SER   A OG  
869  N N   . TYR   A 117 ? 0.2396 0.3047 0.5540 0.0126  -0.0438 0.0292  116 TYR   A N   
870  C CA  . TYR   A 117 ? 0.2667 0.3233 0.5579 0.0132  -0.0609 0.0351  116 TYR   A CA  
871  C C   . TYR   A 117 ? 0.2809 0.3271 0.5301 0.0106  -0.0560 0.0333  116 TYR   A C   
872  O O   . TYR   A 117 ? 0.2835 0.3219 0.5111 0.0125  -0.0573 0.0384  116 TYR   A O   
873  C CB  . TYR   A 117 ? 0.2802 0.3419 0.5841 0.0108  -0.0794 0.0358  116 TYR   A CB  
874  C CG  . TYR   A 117 ? 0.3231 0.3750 0.5934 0.0102  -0.0968 0.0395  116 TYR   A CG  
875  C CD1 . TYR   A 117 ? 0.3492 0.3960 0.6117 0.0142  -0.1087 0.0492  116 TYR   A CD1 
876  C CD2 . TYR   A 117 ? 0.3568 0.4041 0.6045 0.0057  -0.1026 0.0335  116 TYR   A CD2 
877  C CE1 . TYR   A 117 ? 0.3837 0.4217 0.6107 0.0133  -0.1240 0.0532  116 TYR   A CE1 
878  C CE2 . TYR   A 117 ? 0.3904 0.4287 0.6042 0.0055  -0.1175 0.0348  116 TYR   A CE2 
879  C CZ  . TYR   A 117 ? 0.4176 0.4519 0.6196 0.0091  -0.1280 0.0450  116 TYR   A CZ  
880  O OH  . TYR   A 117 ? 0.4793 0.5046 0.6420 0.0084  -0.1413 0.0462  116 TYR   A OH  
881  N N   . VAL   A 118 ? 0.2788 0.3251 0.5190 0.0064  -0.0494 0.0268  117 VAL   A N   
882  C CA  . VAL   A 118 ? 0.2961 0.3336 0.5018 0.0052  -0.0442 0.0245  117 VAL   A CA  
883  C C   . VAL   A 118 ? 0.3035 0.3376 0.4992 0.0075  -0.0320 0.0265  117 VAL   A C   
884  O O   . VAL   A 118 ? 0.3104 0.3384 0.4818 0.0083  -0.0325 0.0292  117 VAL   A O   
885  C CB  . VAL   A 118 ? 0.3011 0.3384 0.5056 0.0011  -0.0385 0.0181  117 VAL   A CB  
886  C CG1 . VAL   A 118 ? 0.3147 0.3447 0.4920 0.0014  -0.0302 0.0156  117 VAL   A CG1 
887  C CG2 . VAL   A 118 ? 0.2970 0.3338 0.5063 -0.0020 -0.0528 0.0151  117 VAL   A CG2 
888  N N   . CYS   A 119 ? 0.2805 0.3187 0.4943 0.0082  -0.0209 0.0245  118 CYS   A N   
889  C CA  . CYS   A 119 ? 0.2803 0.3144 0.4871 0.0097  -0.0112 0.0247  118 CYS   A CA  
890  C C   . CYS   A 119 ? 0.2844 0.3137 0.4912 0.0126  -0.0178 0.0320  118 CYS   A C   
891  O O   . CYS   A 119 ? 0.3087 0.3325 0.5005 0.0123  -0.0140 0.0345  118 CYS   A O   
892  C CB  . CYS   A 119 ? 0.2755 0.3139 0.4997 0.0101  0.0007  0.0193  118 CYS   A CB  
893  S SG  . CYS   A 119 ? 0.3215 0.3625 0.5367 0.0057  0.0108  0.0138  118 CYS   A SG  
894  N N   . ARG   A 120 ? 0.2810 0.3125 0.5065 0.0152  -0.0281 0.0367  119 ARG   A N   
895  C CA  . ARG   A 120 ? 0.2912 0.3163 0.5159 0.0178  -0.0362 0.0465  119 ARG   A CA  
896  C C   . ARG   A 120 ? 0.3069 0.3261 0.4971 0.0156  -0.0421 0.0530  119 ARG   A C   
897  O O   . ARG   A 120 ? 0.3214 0.3341 0.4989 0.0152  -0.0396 0.0600  119 ARG   A O   
898  C CB  . ARG   A 120 ? 0.2900 0.3187 0.5426 0.0216  -0.0492 0.0514  119 ARG   A CB  
899  C CG  . ARG   A 120 ? 0.2967 0.3165 0.5513 0.0246  -0.0569 0.0630  119 ARG   A CG  
900  C CD  . ARG   A 120 ? 0.3209 0.3429 0.5969 0.0283  -0.0750 0.0710  119 ARG   A CD  
901  N NE  . ARG   A 120 ? 0.3563 0.3800 0.6107 0.0255  -0.0891 0.0740  119 ARG   A NE  
902  C CZ  . ARG   A 120 ? 0.3843 0.4120 0.6541 0.0273  -0.1077 0.0788  119 ARG   A CZ  
903  N NH1 . ARG   A 120 ? 0.3502 0.3823 0.6615 0.0326  -0.1139 0.0821  119 ARG   A NH1 
904  N NH2 . ARG   A 120 ? 0.4044 0.4321 0.6501 0.0241  -0.1210 0.0792  119 ARG   A NH2 
905  N N   . GLU   A 121 ? 0.3120 0.3333 0.4883 0.0139  -0.0496 0.0504  120 GLU   A N   
906  C CA  . GLU   A 121 ? 0.3255 0.3416 0.4671 0.0126  -0.0545 0.0542  120 GLU   A CA  
907  C C   . GLU   A 121 ? 0.3321 0.3464 0.4541 0.0109  -0.0400 0.0510  120 GLU   A C   
908  O O   . GLU   A 121 ? 0.3418 0.3521 0.4429 0.0104  -0.0378 0.0579  120 GLU   A O   
909  C CB  . GLU   A 121 ? 0.3428 0.3604 0.4756 0.0113  -0.0660 0.0483  120 GLU   A CB  
910  C CG  . GLU   A 121 ? 0.3224 0.3434 0.4784 0.0126  -0.0828 0.0526  120 GLU   A CG  
911  C CD  . GLU   A 121 ? 0.3733 0.3886 0.5176 0.0146  -0.0949 0.0660  120 GLU   A CD  
912  O OE1 . GLU   A 121 ? 0.4090 0.4185 0.5172 0.0134  -0.1017 0.0689  120 GLU   A OE1 
913  O OE2 . GLU   A 121 ? 0.3865 0.4022 0.5562 0.0175  -0.0973 0.0737  120 GLU   A OE2 
914  N N   . VAL   A 122 ? 0.3152 0.3328 0.4462 0.0100  -0.0300 0.0419  121 VAL   A N   
915  C CA  . VAL   A 122 ? 0.3057 0.3227 0.4234 0.0089  -0.0180 0.0389  121 VAL   A CA  
916  C C   . VAL   A 122 ? 0.3192 0.3343 0.4433 0.0086  -0.0116 0.0451  121 VAL   A C   
917  O O   . VAL   A 122 ? 0.3211 0.3355 0.4312 0.0074  -0.0055 0.0484  121 VAL   A O   
918  C CB  . VAL   A 122 ? 0.3071 0.3270 0.4322 0.0079  -0.0115 0.0294  121 VAL   A CB  
919  C CG1 . VAL   A 122 ? 0.3055 0.3255 0.4231 0.0073  -0.0012 0.0274  121 VAL   A CG1 
920  C CG2 . VAL   A 122 ? 0.3164 0.3357 0.4343 0.0074  -0.0178 0.0236  121 VAL   A CG2 
921  N N   . LEU   A 123 ? 0.3166 0.3309 0.4636 0.0097  -0.0124 0.0463  122 LEU   A N   
922  C CA  . LEU   A 123 ? 0.3143 0.3242 0.4704 0.0091  -0.0079 0.0511  122 LEU   A CA  
923  C C   . LEU   A 123 ? 0.3256 0.3304 0.4704 0.0084  -0.0127 0.0644  122 LEU   A C   
924  O O   . LEU   A 123 ? 0.3316 0.3334 0.4750 0.0059  -0.0069 0.0698  122 LEU   A O   
925  C CB  . LEU   A 123 ? 0.3034 0.3118 0.4873 0.0116  -0.0083 0.0479  122 LEU   A CB  
926  C CG  . LEU   A 123 ? 0.2996 0.3119 0.4917 0.0114  0.0004  0.0354  122 LEU   A CG  
927  C CD1 . LEU   A 123 ? 0.2767 0.2896 0.4950 0.0150  0.0008  0.0310  122 LEU   A CD1 
928  C CD2 . LEU   A 123 ? 0.3045 0.3139 0.4904 0.0087  0.0080  0.0317  122 LEU   A CD2 
929  N N   . GLN   A 124 ? 0.3294 0.3333 0.4661 0.0099  -0.0238 0.0706  123 GLN   A N   
930  C CA  . GLN   A 124 ? 0.3364 0.3345 0.4561 0.0088  -0.0289 0.0854  123 GLN   A CA  
931  C C   . GLN   A 124 ? 0.3528 0.3531 0.4442 0.0058  -0.0193 0.0864  123 GLN   A C   
932  O O   . GLN   A 124 ? 0.3615 0.3587 0.4454 0.0031  -0.0145 0.0976  123 GLN   A O   
933  C CB  . GLN   A 124 ? 0.3362 0.3331 0.4490 0.0110  -0.0451 0.0906  123 GLN   A CB  
934  C CG  . GLN   A 124 ? 0.3254 0.3210 0.4724 0.0146  -0.0545 0.0927  123 GLN   A CG  
935  C CD  . GLN   A 124 ? 0.4169 0.4152 0.5673 0.0170  -0.0713 0.0935  123 GLN   A CD  
936  O OE1 . GLN   A 124 ? 0.4615 0.4611 0.5859 0.0155  -0.0782 0.0921  123 GLN   A OE1 
937  N NE2 . GLN   A 124 ? 0.4039 0.4033 0.5886 0.0208  -0.0788 0.0948  123 GLN   A NE2 
938  N N   . GLY   A 125 ? 0.3552 0.3609 0.4334 0.0064  -0.0162 0.0750  124 GLY   A N   
939  C CA  . GLY   A 125 ? 0.3609 0.3702 0.4167 0.0051  -0.0056 0.0727  124 GLY   A CA  
940  C C   . GLY   A 125 ? 0.3463 0.3591 0.4165 0.0029  0.0072  0.0718  124 GLY   A C   
941  O O   . GLY   A 125 ? 0.3422 0.3577 0.4025 0.0007  0.0164  0.0777  124 GLY   A O   
942  N N   . LEU   A 126 ? 0.3305 0.3440 0.4243 0.0032  0.0079  0.0641  125 LEU   A N   
943  C CA  . LEU   A 126 ? 0.3161 0.3324 0.4239 0.0008  0.0168  0.0619  125 LEU   A CA  
944  C C   . LEU   A 126 ? 0.3197 0.3314 0.4385 -0.0026 0.0182  0.0733  125 LEU   A C   
945  O O   . LEU   A 126 ? 0.3144 0.3297 0.4367 -0.0061 0.0264  0.0766  125 LEU   A O   
946  C CB  . LEU   A 126 ? 0.3083 0.3247 0.4331 0.0017  0.0157  0.0511  125 LEU   A CB  
947  C CG  . LEU   A 126 ? 0.3086 0.3293 0.4266 0.0035  0.0168  0.0409  125 LEU   A CG  
948  C CD1 . LEU   A 126 ? 0.3190 0.3391 0.4506 0.0036  0.0162  0.0332  125 LEU   A CD1 
949  C CD2 . LEU   A 126 ? 0.3113 0.3377 0.4226 0.0030  0.0243  0.0391  125 LEU   A CD2 
950  N N   . ALA   A 127 ? 0.3176 0.3215 0.4450 -0.0017 0.0100  0.0800  126 ALA   A N   
951  C CA  . ALA   A 127 ? 0.3296 0.3261 0.4695 -0.0050 0.0098  0.0923  126 ALA   A CA  
952  C C   . ALA   A 127 ? 0.3531 0.3508 0.4732 -0.0086 0.0150  0.1066  126 ALA   A C   
953  O O   . ALA   A 127 ? 0.3551 0.3512 0.4852 -0.0137 0.0211  0.1156  126 ALA   A O   
954  C CB  . ALA   A 127 ? 0.3201 0.3074 0.4737 -0.0018 -0.0014 0.0973  126 ALA   A CB  
955  N N   . TYR   A 128 ? 0.3711 0.3718 0.4629 -0.0066 0.0132  0.1085  127 TYR   A N   
956  C CA  . TYR   A 128 ? 0.3942 0.3970 0.4611 -0.0097 0.0203  0.1211  127 TYR   A CA  
957  C C   . TYR   A 128 ? 0.3805 0.3946 0.4494 -0.0121 0.0361  0.1149  127 TYR   A C   
958  O O   . TYR   A 128 ? 0.3813 0.3976 0.4554 -0.0173 0.0456  0.1258  127 TYR   A O   
959  C CB  . TYR   A 128 ? 0.4159 0.4186 0.4483 -0.0065 0.0140  0.1208  127 TYR   A CB  
960  C CG  . TYR   A 128 ? 0.4531 0.4601 0.4542 -0.0092 0.0255  0.1292  127 TYR   A CG  
961  C CD1 . TYR   A 128 ? 0.4790 0.4806 0.4691 -0.0138 0.0271  0.1500  127 TYR   A CD1 
962  C CD2 . TYR   A 128 ? 0.4737 0.4902 0.4586 -0.0072 0.0367  0.1168  127 TYR   A CD2 
963  C CE1 . TYR   A 128 ? 0.5071 0.5139 0.4668 -0.0168 0.0407  0.1585  127 TYR   A CE1 
964  C CE2 . TYR   A 128 ? 0.5002 0.5223 0.4576 -0.0091 0.0504  0.1229  127 TYR   A CE2 
965  C CZ  . TYR   A 128 ? 0.5312 0.5492 0.4750 -0.0142 0.0534  0.1439  127 TYR   A CZ  
966  O OH  . TYR   A 128 ? 0.5759 0.6006 0.4900 -0.0163 0.0695  0.1502  127 TYR   A OH  
967  N N   . LEU   A 129 ? 0.3735 0.3947 0.4422 -0.0084 0.0383  0.0983  128 LEU   A N   
968  C CA  . LEU   A 129 ? 0.3657 0.3981 0.4410 -0.0093 0.0513  0.0919  128 LEU   A CA  
969  C C   . LEU   A 129 ? 0.3607 0.3949 0.4662 -0.0145 0.0554  0.0957  128 LEU   A C   
970  O O   . LEU   A 129 ? 0.3687 0.4112 0.4795 -0.0184 0.0669  0.1020  128 LEU   A O   
971  C CB  . LEU   A 129 ? 0.3719 0.4083 0.4474 -0.0043 0.0495  0.0746  128 LEU   A CB  
972  C CG  . LEU   A 129 ? 0.4082 0.4437 0.4549 0.0003  0.0471  0.0684  128 LEU   A CG  
973  C CD1 . LEU   A 129 ? 0.3978 0.4348 0.4495 0.0044  0.0444  0.0529  128 LEU   A CD1 
974  C CD2 . LEU   A 129 ? 0.4423 0.4842 0.4664 0.0002  0.0598  0.0726  128 LEU   A CD2 
975  N N   . HIS   A 130 ? 0.3514 0.3777 0.4770 -0.0150 0.0463  0.0927  129 HIS   A N   
976  C CA  . HIS   A 130 ? 0.3452 0.3705 0.4992 -0.0203 0.0476  0.0943  129 HIS   A CA  
977  C C   . HIS   A 130 ? 0.3630 0.3839 0.5231 -0.0268 0.0515  0.1127  129 HIS   A C   
978  O O   . HIS   A 130 ? 0.3503 0.3764 0.5298 -0.0328 0.0583  0.1170  129 HIS   A O   
979  C CB  . HIS   A 130 ? 0.3259 0.3422 0.4950 -0.0183 0.0373  0.0842  129 HIS   A CB  
980  C CG  . HIS   A 130 ? 0.3352 0.3562 0.4997 -0.0138 0.0352  0.0687  129 HIS   A CG  
981  N ND1 . HIS   A 130 ? 0.3336 0.3482 0.5044 -0.0112 0.0283  0.0591  129 HIS   A ND1 
982  C CD2 . HIS   A 130 ? 0.3329 0.3635 0.4872 -0.0114 0.0396  0.0622  129 HIS   A CD2 
983  C CE1 . HIS   A 130 ? 0.3241 0.3444 0.4876 -0.0086 0.0287  0.0491  129 HIS   A CE1 
984  N NE2 . HIS   A 130 ? 0.3350 0.3640 0.4895 -0.0082 0.0343  0.0505  129 HIS   A NE2 
985  N N   . SER   A 131 ? 0.3921 0.4042 0.5358 -0.0261 0.0470  0.1251  130 SER   A N   
986  C CA  . SER   A 131 ? 0.4180 0.4247 0.5638 -0.0326 0.0508  0.1457  130 SER   A CA  
987  C C   . SER   A 131 ? 0.4411 0.4615 0.5736 -0.0367 0.0676  0.1537  130 SER   A C   
988  O O   . SER   A 131 ? 0.4419 0.4628 0.5863 -0.0445 0.0754  0.1690  130 SER   A O   
989  C CB  . SER   A 131 ? 0.4424 0.4362 0.5716 -0.0303 0.0402  0.1582  130 SER   A CB  
990  O OG  . SER   A 131 ? 0.4771 0.4759 0.5698 -0.0264 0.0409  0.1583  130 SER   A OG  
991  N N   . GLN   A 132 ? 0.4430 0.4749 0.5542 -0.0317 0.0739  0.1428  131 GLN   A N   
992  C CA  . GLN   A 132 ? 0.4562 0.5032 0.5572 -0.0338 0.0919  0.1462  131 GLN   A CA  
993  C C   . GLN   A 132 ? 0.4294 0.4904 0.5619 -0.0350 0.0995  0.1353  131 GLN   A C   
994  O O   . GLN   A 132 ? 0.4319 0.5081 0.5607 -0.0342 0.1143  0.1330  131 GLN   A O   
995  C CB  . GLN   A 132 ? 0.5125 0.5633 0.5749 -0.0267 0.0944  0.1379  131 GLN   A CB  
996  C CG  . GLN   A 132 ? 0.5880 0.6254 0.6184 -0.0250 0.0828  0.1466  131 GLN   A CG  
997  C CD  . GLN   A 132 ? 0.6720 0.7062 0.6895 -0.0319 0.0899  0.1702  131 GLN   A CD  
998  O OE1 . GLN   A 132 ? 0.7128 0.7564 0.7083 -0.0338 0.1062  0.1760  131 GLN   A OE1 
999  N NE2 . GLN   A 132 ? 0.6739 0.6946 0.7065 -0.0359 0.0790  0.1846  131 GLN   A NE2 
1000 N N   . LYS   A 133 ? 0.4035 0.4597 0.5659 -0.0363 0.0891  0.1276  132 LYS   A N   
1001 C CA  . LYS   A 133 ? 0.3968 0.4643 0.5897 -0.0378 0.0914  0.1176  132 LYS   A CA  
1002 C C   . LYS   A 133 ? 0.3894 0.4683 0.5733 -0.0301 0.0947  0.1022  132 LYS   A C   
1003 O O   . LYS   A 133 ? 0.3884 0.4821 0.5917 -0.0305 0.1025  0.0981  132 LYS   A O   
1004 C CB  . LYS   A 133 ? 0.4315 0.5096 0.6511 -0.0471 0.1036  0.1303  132 LYS   A CB  
1005 C CG  . LYS   A 133 ? 0.4943 0.5586 0.7280 -0.0556 0.0991  0.1462  132 LYS   A CG  
1006 C CD  . LYS   A 133 ? 0.5820 0.6574 0.8518 -0.0658 0.1089  0.1558  132 LYS   A CD  
1007 C CE  . LYS   A 133 ? 0.6683 0.7287 0.9565 -0.0755 0.1046  0.1724  132 LYS   A CE  
1008 N NZ  . LYS   A 133 ? 0.7261 0.7797 0.9865 -0.0775 0.1121  0.1933  132 LYS   A NZ  
1009 N N   . LYS   A 134 ? 0.3857 0.4572 0.5432 -0.0231 0.0879  0.0943  133 LYS   A N   
1010 C CA  . LYS   A 134 ? 0.3790 0.4563 0.5282 -0.0156 0.0878  0.0794  133 LYS   A CA  
1011 C C   . LYS   A 134 ? 0.3539 0.4223 0.5091 -0.0130 0.0731  0.0684  133 LYS   A C   
1012 O O   . LYS   A 134 ? 0.3712 0.4276 0.5236 -0.0142 0.0639  0.0707  133 LYS   A O   
1013 C CB  . LYS   A 134 ? 0.4252 0.5001 0.5386 -0.0104 0.0911  0.0779  133 LYS   A CB  
1014 C CG  . LYS   A 134 ? 0.4895 0.5757 0.5910 -0.0113 0.1089  0.0848  133 LYS   A CG  
1015 C CD  . LYS   A 134 ? 0.5790 0.6653 0.6500 -0.0038 0.1119  0.0742  133 LYS   A CD  
1016 C CE  . LYS   A 134 ? 0.6425 0.7382 0.6933 -0.0041 0.1303  0.0801  133 LYS   A CE  
1017 N NZ  . LYS   A 134 ? 0.6998 0.7886 0.7322 -0.0109 0.1310  0.0992  133 LYS   A NZ  
1018 N N   . ILE   A 135 ? 0.3154 0.3899 0.4793 -0.0091 0.0715  0.0570  134 ILE   A N   
1019 C CA  . ILE   A 135 ? 0.2939 0.3606 0.4584 -0.0066 0.0595  0.0475  134 ILE   A CA  
1020 C C   . ILE   A 135 ? 0.2895 0.3558 0.4357 0.0002  0.0595  0.0395  134 ILE   A C   
1021 O O   . ILE   A 135 ? 0.2985 0.3738 0.4458 0.0036  0.0673  0.0363  134 ILE   A O   
1022 C CB  . ILE   A 135 ? 0.2758 0.3476 0.4646 -0.0085 0.0549  0.0425  134 ILE   A CB  
1023 C CG1 . ILE   A 135 ? 0.2716 0.3430 0.4813 -0.0161 0.0538  0.0490  134 ILE   A CG1 
1024 C CG2 . ILE   A 135 ? 0.2774 0.3413 0.4601 -0.0058 0.0440  0.0335  134 ILE   A CG2 
1025 C CD1 . ILE   A 135 ? 0.2790 0.3570 0.5138 -0.0187 0.0476  0.0436  134 ILE   A CD1 
1026 N N   . HIS   A 136 ? 0.2865 0.3425 0.4176 0.0022  0.0516  0.0363  135 HIS   A N   
1027 C CA  . HIS   A 136 ? 0.2851 0.3386 0.4005 0.0075  0.0501  0.0287  135 HIS   A CA  
1028 C C   . HIS   A 136 ? 0.2932 0.3496 0.4207 0.0106  0.0480  0.0207  135 HIS   A C   
1029 O O   . HIS   A 136 ? 0.3039 0.3653 0.4312 0.0151  0.0532  0.0157  135 HIS   A O   
1030 C CB  . HIS   A 136 ? 0.2912 0.3345 0.3945 0.0077  0.0411  0.0280  135 HIS   A CB  
1031 C CG  . HIS   A 136 ? 0.3276 0.3672 0.4145 0.0117  0.0386  0.0212  135 HIS   A CG  
1032 N ND1 . HIS   A 136 ? 0.3436 0.3810 0.4350 0.0144  0.0352  0.0129  135 HIS   A ND1 
1033 C CD2 . HIS   A 136 ? 0.3423 0.3792 0.4084 0.0132  0.0384  0.0213  135 HIS   A CD2 
1034 C CE1 . HIS   A 136 ? 0.3572 0.3900 0.4333 0.0173  0.0330  0.0074  135 HIS   A CE1 
1035 N NE2 . HIS   A 136 ? 0.3516 0.3841 0.4109 0.0167  0.0340  0.0114  135 HIS   A NE2 
1036 N N   . ARG   A 137 ? 0.2718 0.3244 0.4089 0.0086  0.0402  0.0193  136 ARG   A N   
1037 C CA  . ARG   A 137 ? 0.2608 0.3149 0.4080 0.0106  0.0360  0.0146  136 ARG   A CA  
1038 C C   . ARG   A 137 ? 0.2781 0.3263 0.4166 0.0153  0.0329  0.0089  136 ARG   A C   
1039 O O   . ARG   A 137 ? 0.2945 0.3430 0.4416 0.0179  0.0293  0.0064  136 ARG   A O   
1040 C CB  . ARG   A 137 ? 0.2486 0.3146 0.4150 0.0113  0.0405  0.0154  136 ARG   A CB  
1041 C CG  . ARG   A 137 ? 0.2656 0.3340 0.4481 0.0065  0.0345  0.0174  136 ARG   A CG  
1042 C CD  . ARG   A 137 ? 0.2711 0.3364 0.4564 0.0082  0.0245  0.0137  136 ARG   A CD  
1043 N NE  . ARG   A 137 ? 0.2940 0.3698 0.4994 0.0119  0.0246  0.0128  136 ARG   A NE  
1044 C CZ  . ARG   A 137 ? 0.3191 0.3944 0.5261 0.0183  0.0236  0.0096  136 ARG   A CZ  
1045 N NH1 . ARG   A 137 ? 0.3159 0.3799 0.5044 0.0208  0.0224  0.0072  136 ARG   A NH1 
1046 N NH2 . ARG   A 137 ? 0.2850 0.3710 0.5155 0.0224  0.0235  0.0086  136 ARG   A NH2 
1047 N N   . ASP   A 138 ? 0.2837 0.3253 0.4069 0.0159  0.0322  0.0075  137 ASP   A N   
1048 C CA  . ASP   A 138 ? 0.2890 0.3234 0.4058 0.0192  0.0284  0.0018  137 ASP   A CA  
1049 C C   . ASP   A 138 ? 0.2948 0.3215 0.4017 0.0166  0.0230  0.0022  137 ASP   A C   
1050 O O   . ASP   A 138 ? 0.2944 0.3155 0.3933 0.0184  0.0201  -0.0026 137 ASP   A O   
1051 C CB  . ASP   A 138 ? 0.3199 0.3567 0.4308 0.0244  0.0346  -0.0039 137 ASP   A CB  
1052 C CG  . ASP   A 138 ? 0.3904 0.4199 0.5023 0.0292  0.0310  -0.0119 137 ASP   A CG  
1053 O OD1 . ASP   A 138 ? 0.3958 0.4208 0.5184 0.0289  0.0246  -0.0108 137 ASP   A OD1 
1054 O OD2 . ASP   A 138 ? 0.3981 0.4249 0.4986 0.0331  0.0340  -0.0193 137 ASP   A OD2 
1055 N N   . ILE   A 139 ? 0.2781 0.3048 0.3880 0.0124  0.0212  0.0069  138 ILE   A N   
1056 C CA  . ILE   A 139 ? 0.2885 0.3107 0.3957 0.0102  0.0167  0.0077  138 ILE   A CA  
1057 C C   . ILE   A 139 ? 0.2817 0.2990 0.3929 0.0089  0.0131  0.0059  138 ILE   A C   
1058 O O   . ILE   A 139 ? 0.2833 0.3007 0.3986 0.0075  0.0137  0.0074  138 ILE   A O   
1059 C CB  . ILE   A 139 ? 0.2821 0.3061 0.3945 0.0074  0.0175  0.0123  138 ILE   A CB  
1060 C CG1 . ILE   A 139 ? 0.2961 0.3232 0.4060 0.0075  0.0208  0.0167  138 ILE   A CG1 
1061 C CG2 . ILE   A 139 ? 0.2726 0.2942 0.3884 0.0061  0.0135  0.0126  138 ILE   A CG2 
1062 C CD1 . ILE   A 139 ? 0.3145 0.3403 0.4103 0.0091  0.0190  0.0185  138 ILE   A CD1 
1063 N N   . LYS   A 140 ? 0.2717 0.2844 0.3810 0.0089  0.0087  0.0032  139 LYS   A N   
1064 C CA  . LYS   A 140 ? 0.2641 0.2714 0.3793 0.0065  0.0052  0.0029  139 LYS   A CA  
1065 C C   . LYS   A 140 ? 0.2843 0.2879 0.3991 0.0058  -0.0012 -0.0006 139 LYS   A C   
1066 O O   . LYS   A 140 ? 0.2874 0.2909 0.3922 0.0085  -0.0032 -0.0042 139 LYS   A O   
1067 C CB  . LYS   A 140 ? 0.2854 0.2875 0.4020 0.0083  0.0044  0.0018  139 LYS   A CB  
1068 C CG  . LYS   A 140 ? 0.2974 0.2953 0.4102 0.0132  0.0027  -0.0053 139 LYS   A CG  
1069 C CD  . LYS   A 140 ? 0.3543 0.3497 0.4728 0.0171  0.0031  -0.0062 139 LYS   A CD  
1070 C CE  . LYS   A 140 ? 0.4141 0.4027 0.5394 0.0141  -0.0010 -0.0005 139 LYS   A CE  
1071 N NZ  . LYS   A 140 ? 0.4877 0.4646 0.6177 0.0136  -0.0066 -0.0036 139 LYS   A NZ  
1072 N N   . GLY   A 141 ? 0.2823 0.2831 0.4075 0.0018  -0.0044 0.0006  140 GLY   A N   
1073 C CA  . GLY   A 141 ? 0.3076 0.3054 0.4374 -0.0001 -0.0127 -0.0028 140 GLY   A CA  
1074 C C   . GLY   A 141 ? 0.3340 0.3236 0.4530 0.0032  -0.0186 -0.0114 140 GLY   A C   
1075 O O   . GLY   A 141 ? 0.3468 0.3358 0.4590 0.0035  -0.0257 -0.0155 140 GLY   A O   
1076 N N   . ALA   A 142 ? 0.3369 0.3200 0.4537 0.0062  -0.0163 -0.0147 141 ALA   A N   
1077 C CA  . ALA   A 142 ? 0.3510 0.3253 0.4589 0.0107  -0.0201 -0.0254 141 ALA   A CA  
1078 C C   . ALA   A 142 ? 0.3585 0.3379 0.4468 0.0155  -0.0164 -0.0298 141 ALA   A C   
1079 O O   . ALA   A 142 ? 0.3647 0.3381 0.4403 0.0187  -0.0194 -0.0399 141 ALA   A O   
1080 C CB  . ALA   A 142 ? 0.3581 0.3254 0.4728 0.0141  -0.0177 -0.0270 141 ALA   A CB  
1081 N N   . ASN   A 143 ? 0.3551 0.3448 0.4401 0.0156  -0.0094 -0.0222 142 ASN   A N   
1082 C CA  . ASN   A 143 ? 0.3537 0.3487 0.4214 0.0189  -0.0041 -0.0232 142 ASN   A CA  
1083 C C   . ASN   A 143 ? 0.3536 0.3519 0.4126 0.0161  -0.0088 -0.0178 142 ASN   A C   
1084 O O   . ASN   A 143 ? 0.3587 0.3617 0.4043 0.0175  -0.0039 -0.0142 142 ASN   A O   
1085 C CB  . ASN   A 143 ? 0.3442 0.3473 0.4171 0.0209  0.0066  -0.0184 142 ASN   A CB  
1086 C CG  . ASN   A 143 ? 0.3523 0.3524 0.4352 0.0248  0.0091  -0.0234 142 ASN   A CG  
1087 O OD1 . ASN   A 143 ? 0.3609 0.3520 0.4427 0.0276  0.0053  -0.0323 142 ASN   A OD1 
1088 N ND2 . ASN   A 143 ? 0.3165 0.3229 0.4111 0.0251  0.0140  -0.0180 142 ASN   A ND2 
1089 N N   . ILE   A 144 ? 0.3374 0.3338 0.4070 0.0121  -0.0183 -0.0160 143 ILE   A N   
1090 C CA  . ILE   A 144 ? 0.3471 0.3463 0.4140 0.0101  -0.0258 -0.0111 143 ILE   A CA  
1091 C C   . ILE   A 144 ? 0.3686 0.3608 0.4313 0.0087  -0.0392 -0.0189 143 ILE   A C   
1092 O O   . ILE   A 144 ? 0.3569 0.3456 0.4374 0.0057  -0.0441 -0.0220 143 ILE   A O   
1093 C CB  . ILE   A 144 ? 0.3404 0.3458 0.4300 0.0069  -0.0250 -0.0026 143 ILE   A CB  
1094 C CG1 . ILE   A 144 ? 0.3392 0.3496 0.4315 0.0079  -0.0133 0.0030  143 ILE   A CG1 
1095 C CG2 . ILE   A 144 ? 0.3450 0.3531 0.4378 0.0057  -0.0354 0.0022  143 ILE   A CG2 
1096 C CD1 . ILE   A 144 ? 0.3481 0.3620 0.4602 0.0054  -0.0093 0.0063  143 ILE   A CD1 
1097 N N   . LEU   A 145 ? 0.3879 0.3772 0.4259 0.0105  -0.0453 -0.0219 144 LEU   A N   
1098 C CA  . LEU   A 145 ? 0.4067 0.3880 0.4352 0.0093  -0.0603 -0.0316 144 LEU   A CA  
1099 C C   . LEU   A 145 ? 0.4109 0.3952 0.4442 0.0062  -0.0756 -0.0254 144 LEU   A C   
1100 O O   . LEU   A 145 ? 0.3917 0.3826 0.4247 0.0066  -0.0741 -0.0141 144 LEU   A O   
1101 C CB  . LEU   A 145 ? 0.4259 0.4009 0.4186 0.0138  -0.0579 -0.0412 144 LEU   A CB  
1102 C CG  . LEU   A 145 ? 0.4551 0.4296 0.4445 0.0187  -0.0413 -0.0471 144 LEU   A CG  
1103 C CD1 . LEU   A 145 ? 0.4673 0.4378 0.4218 0.0236  -0.0366 -0.0572 144 LEU   A CD1 
1104 C CD2 . LEU   A 145 ? 0.4508 0.4187 0.4648 0.0182  -0.0421 -0.0540 144 LEU   A CD2 
1105 N N   . ILE   A 146 ? 0.4236 0.4024 0.4632 0.0030  -0.0917 -0.0331 145 ILE   A N   
1106 C CA  . ILE   A 146 ? 0.4501 0.4322 0.4996 -0.0002 -0.1098 -0.0289 145 ILE   A CA  
1107 C C   . ILE   A 146 ? 0.4888 0.4608 0.5097 -0.0003 -0.1270 -0.0401 145 ILE   A C   
1108 O O   . ILE   A 146 ? 0.4989 0.4612 0.5161 -0.0009 -0.1295 -0.0539 145 ILE   A O   
1109 C CB  . ILE   A 146 ? 0.4391 0.4259 0.5321 -0.0055 -0.1140 -0.0278 145 ILE   A CB  
1110 C CG1 . ILE   A 146 ? 0.4391 0.4347 0.5563 -0.0055 -0.0957 -0.0188 145 ILE   A CG1 
1111 C CG2 . ILE   A 146 ? 0.4332 0.4257 0.5445 -0.0088 -0.1338 -0.0242 145 ILE   A CG2 
1112 C CD1 . ILE   A 146 ? 0.4498 0.4555 0.5751 -0.0035 -0.0915 -0.0068 145 ILE   A CD1 
1113 N N   . ASN   A 147 ? 0.5144 0.4872 0.5141 0.0003  -0.1398 -0.0346 146 ASN   A N   
1114 C CA  . ASN   A 147 ? 0.5581 0.5207 0.5267 -0.0003 -0.1591 -0.0458 146 ASN   A CA  
1115 C C   . ASN   A 147 ? 0.5841 0.5488 0.5842 -0.0060 -0.1834 -0.0468 146 ASN   A C   
1116 O O   . ASN   A 147 ? 0.5738 0.5497 0.6180 -0.0085 -0.1822 -0.0370 146 ASN   A O   
1117 C CB  . ASN   A 147 ? 0.5842 0.5451 0.5065 0.0029  -0.1610 -0.0389 146 ASN   A CB  
1118 C CG  . ASN   A 147 ? 0.6110 0.5801 0.5436 0.0024  -0.1701 -0.0199 146 ASN   A CG  
1119 O OD1 . ASN   A 147 ? 0.5979 0.5751 0.5738 -0.0001 -0.1784 -0.0130 146 ASN   A OD1 
1120 N ND2 . ASN   A 147 ? 0.6222 0.5890 0.5153 0.0047  -0.1687 -0.0106 146 ASN   A ND2 
1121 N N   . ASP   A 148 ? 0.6091 0.5639 0.5886 -0.0081 -0.2053 -0.0591 147 ASP   A N   
1122 C CA  . ASP   A 148 ? 0.6201 0.5776 0.6333 -0.0142 -0.2301 -0.0609 147 ASP   A CA  
1123 C C   . ASP   A 148 ? 0.6141 0.5847 0.6483 -0.0146 -0.2433 -0.0434 147 ASP   A C   
1124 O O   . ASP   A 148 ? 0.6043 0.5826 0.6808 -0.0194 -0.2599 -0.0418 147 ASP   A O   
1125 C CB  . ASP   A 148 ? 0.6844 0.6267 0.6696 -0.0167 -0.2524 -0.0799 147 ASP   A CB  
1126 C CG  . ASP   A 148 ? 0.7834 0.7127 0.7689 -0.0172 -0.2427 -0.0982 147 ASP   A CG  
1127 O OD1 . ASP   A 148 ? 0.7796 0.7132 0.7958 -0.0173 -0.2227 -0.0940 147 ASP   A OD1 
1128 O OD2 . ASP   A 148 ? 0.8486 0.7624 0.8032 -0.0173 -0.2559 -0.1169 147 ASP   A OD2 
1129 N N   . ALA   A 149 ? 0.6137 0.5877 0.6249 -0.0097 -0.2346 -0.0298 148 ALA   A N   
1130 C CA  . ALA   A 149 ? 0.5984 0.5831 0.6318 -0.0088 -0.2454 -0.0123 148 ALA   A CA  
1131 C C   . ALA   A 149 ? 0.5746 0.5728 0.6554 -0.0074 -0.2251 -0.0012 148 ALA   A C   
1132 O O   . ALA   A 149 ? 0.5758 0.5826 0.6789 -0.0053 -0.2304 0.0127  148 ALA   A O   
1133 C CB  . ALA   A 149 ? 0.6165 0.5955 0.6008 -0.0047 -0.2483 -0.0018 148 ALA   A CB  
1134 N N   . GLY   A 150 ? 0.5406 0.5395 0.6350 -0.0083 -0.2030 -0.0076 149 GLY   A N   
1135 C CA  . GLY   A 150 ? 0.5057 0.5159 0.6381 -0.0073 -0.1836 0.0007  149 GLY   A CA  
1136 C C   . GLY   A 150 ? 0.4938 0.5041 0.6083 -0.0023 -0.1655 0.0108  149 GLY   A C   
1137 O O   . GLY   A 150 ? 0.4870 0.5058 0.6305 -0.0009 -0.1520 0.0177  149 GLY   A O   
1138 N N   . GLU   A 151 ? 0.4873 0.4883 0.5540 0.0002  -0.1647 0.0114  150 GLU   A N   
1139 C CA  . GLU   A 151 ? 0.4758 0.4763 0.5252 0.0038  -0.1473 0.0210  150 GLU   A CA  
1140 C C   . GLU   A 151 ? 0.4555 0.4562 0.5067 0.0042  -0.1237 0.0146  150 GLU   A C   
1141 O O   . GLU   A 151 ? 0.4514 0.4482 0.4996 0.0026  -0.1213 0.0020  150 GLU   A O   
1142 C CB  . GLU   A 151 ? 0.5197 0.5116 0.5184 0.0054  -0.1531 0.0250  150 GLU   A CB  
1143 C CG  . GLU   A 151 ? 0.5812 0.5730 0.5792 0.0055  -0.1767 0.0366  150 GLU   A CG  
1144 C CD  . GLU   A 151 ? 0.6616 0.6438 0.6042 0.0059  -0.1870 0.0400  150 GLU   A CD  
1145 O OE1 . GLU   A 151 ? 0.6762 0.6515 0.5832 0.0054  -0.1837 0.0262  150 GLU   A OE1 
1146 O OE2 . GLU   A 151 ? 0.7200 0.7007 0.6538 0.0070  -0.1976 0.0565  150 GLU   A OE2 
1147 N N   . VAL   A 152 ? 0.4296 0.4340 0.4878 0.0061  -0.1076 0.0233  151 VAL   A N   
1148 C CA  . VAL   A 152 ? 0.4132 0.4187 0.4757 0.0065  -0.0870 0.0187  151 VAL   A CA  
1149 C C   . VAL   A 152 ? 0.4276 0.4299 0.4589 0.0086  -0.0745 0.0219  151 VAL   A C   
1150 O O   . VAL   A 152 ? 0.4215 0.4240 0.4453 0.0094  -0.0737 0.0338  151 VAL   A O   
1151 C CB  . VAL   A 152 ? 0.3913 0.4046 0.4914 0.0063  -0.0782 0.0238  151 VAL   A CB  
1152 C CG1 . VAL   A 152 ? 0.3863 0.4003 0.4871 0.0065  -0.0592 0.0208  151 VAL   A CG1 
1153 C CG2 . VAL   A 152 ? 0.3717 0.3908 0.5052 0.0038  -0.0867 0.0205  151 VAL   A CG2 
1154 N N   . ARG   A 153 ? 0.4341 0.4335 0.4496 0.0094  -0.0642 0.0118  152 ARG   A N   
1155 C CA  . ARG   A 153 ? 0.4513 0.4504 0.4417 0.0114  -0.0503 0.0141  152 ARG   A CA  
1156 C C   . ARG   A 153 ? 0.4316 0.4329 0.4317 0.0127  -0.0350 0.0071  152 ARG   A C   
1157 O O   . ARG   A 153 ? 0.4298 0.4279 0.4366 0.0129  -0.0366 -0.0038 152 ARG   A O   
1158 C CB  . ARG   A 153 ? 0.5115 0.5045 0.4611 0.0129  -0.0549 0.0085  152 ARG   A CB  
1159 C CG  . ARG   A 153 ? 0.5972 0.5853 0.5361 0.0114  -0.0770 0.0085  152 ARG   A CG  
1160 C CD  . ARG   A 153 ? 0.6718 0.6555 0.5670 0.0120  -0.0816 0.0135  152 ARG   A CD  
1161 N NE  . ARG   A 153 ? 0.7420 0.7256 0.6410 0.0105  -0.0975 0.0286  152 ARG   A NE  
1162 C CZ  . ARG   A 153 ? 0.8347 0.8126 0.7062 0.0098  -0.1166 0.0308  152 ARG   A CZ  
1163 N NH1 . ARG   A 153 ? 0.8707 0.8416 0.7051 0.0103  -0.1215 0.0171  152 ARG   A NH1 
1164 N NH2 . ARG   A 153 ? 0.8398 0.8180 0.7198 0.0090  -0.1317 0.0465  152 ARG   A NH2 
1165 N N   . LEU   A 154 ? 0.4063 0.4123 0.4068 0.0133  -0.0211 0.0137  153 LEU   A N   
1166 C CA  . LEU   A 154 ? 0.3959 0.4048 0.4037 0.0149  -0.0078 0.0078  153 LEU   A CA  
1167 C C   . LEU   A 154 ? 0.4279 0.4340 0.4099 0.0184  -0.0035 -0.0026 153 LEU   A C   
1168 O O   . LEU   A 154 ? 0.4382 0.4437 0.3929 0.0189  -0.0025 0.0003  153 LEU   A O   
1169 C CB  . LEU   A 154 ? 0.3899 0.4051 0.4056 0.0139  0.0039  0.0177  153 LEU   A CB  
1170 C CG  . LEU   A 154 ? 0.3977 0.4144 0.4386 0.0113  0.0012  0.0253  153 LEU   A CG  
1171 C CD1 . LEU   A 154 ? 0.3951 0.4157 0.4424 0.0097  0.0107  0.0343  153 LEU   A CD1 
1172 C CD2 . LEU   A 154 ? 0.3924 0.4093 0.4537 0.0111  0.0006  0.0182  153 LEU   A CD2 
1173 N N   . ALA   A 155 ? 0.4365 0.4398 0.4259 0.0209  -0.0012 -0.0145 154 ALA   A N   
1174 C CA  . ALA   A 155 ? 0.4533 0.4528 0.4219 0.0256  0.0035  -0.0274 154 ALA   A CA  
1175 C C   . ALA   A 155 ? 0.4651 0.4726 0.4184 0.0281  0.0198  -0.0243 154 ALA   A C   
1176 O O   . ALA   A 155 ? 0.4821 0.4877 0.4061 0.0310  0.0241  -0.0311 154 ALA   A O   
1177 C CB  . ALA   A 155 ? 0.4532 0.4482 0.4403 0.0284  0.0044  -0.0385 154 ALA   A CB  
1178 N N   . ASP   A 156 ? 0.4488 0.4655 0.4216 0.0267  0.0295  -0.0144 155 ASP   A N   
1179 C CA  . ASP   A 156 ? 0.4467 0.4732 0.4120 0.0277  0.0460  -0.0094 155 ASP   A CA  
1180 C C   . ASP   A 156 ? 0.4469 0.4804 0.4332 0.0229  0.0492  0.0058  155 ASP   A C   
1181 O O   . ASP   A 156 ? 0.4317 0.4615 0.4343 0.0198  0.0389  0.0103  155 ASP   A O   
1182 C CB  . ASP   A 156 ? 0.4437 0.4749 0.4166 0.0340  0.0583  -0.0217 155 ASP   A CB  
1183 C CG  . ASP   A 156 ? 0.4494 0.4826 0.4568 0.0352  0.0570  -0.0239 155 ASP   A CG  
1184 O OD1 . ASP   A 156 ? 0.4548 0.4892 0.4801 0.0306  0.0514  -0.0144 155 ASP   A OD1 
1185 O OD2 . ASP   A 156 ? 0.4802 0.5129 0.4957 0.0410  0.0610  -0.0352 155 ASP   A OD2 
1186 N N   . PHE   A 157 ? 0.4559 0.4992 0.4433 0.0219  0.0637  0.0130  156 PHE   A N   
1187 C CA  . PHE   A 157 ? 0.4714 0.5197 0.4811 0.0167  0.0654  0.0262  156 PHE   A CA  
1188 C C   . PHE   A 157 ? 0.4492 0.5038 0.4920 0.0172  0.0678  0.0225  156 PHE   A C   
1189 O O   . PHE   A 157 ? 0.4451 0.5046 0.5071 0.0129  0.0704  0.0310  156 PHE   A O   
1190 C CB  . PHE   A 157 ? 0.4873 0.5418 0.4859 0.0130  0.0772  0.0393  156 PHE   A CB  
1191 C CG  . PHE   A 157 ? 0.5129 0.5791 0.5069 0.0158  0.0958  0.0354  156 PHE   A CG  
1192 C CD1 . PHE   A 157 ? 0.5279 0.6045 0.5513 0.0184  0.1037  0.0287  156 PHE   A CD1 
1193 C CD2 . PHE   A 157 ? 0.5422 0.6099 0.5029 0.0159  0.1058  0.0391  156 PHE   A CD2 
1194 C CE1 . PHE   A 157 ? 0.5383 0.6279 0.5629 0.0218  0.1221  0.0246  156 PHE   A CE1 
1195 C CE2 . PHE   A 157 ? 0.5665 0.6471 0.5245 0.0187  0.1262  0.0352  156 PHE   A CE2 
1196 C CZ  . PHE   A 157 ? 0.5526 0.6448 0.5454 0.0218  0.1347  0.0276  156 PHE   A CZ  
1197 N N   . GLY   A 158 ? 0.4417 0.4945 0.4907 0.0219  0.0651  0.0104  157 GLY   A N   
1198 C CA  . GLY   A 158 ? 0.4311 0.4881 0.5081 0.0227  0.0642  0.0078  157 GLY   A CA  
1199 C C   . GLY   A 158 ? 0.4354 0.5020 0.5247 0.0281  0.0745  0.0008  157 GLY   A C   
1200 O O   . GLY   A 158 ? 0.4457 0.5142 0.5204 0.0328  0.0833  -0.0060 157 GLY   A O   
1201 N N   . ILE   A 159 ? 0.4273 0.5001 0.5442 0.0277  0.0732  0.0020  158 ILE   A N   
1202 C CA  . ILE   A 159 ? 0.4458 0.5288 0.5831 0.0333  0.0804  -0.0039 158 ILE   A CA  
1203 C C   . ILE   A 159 ? 0.4702 0.5700 0.6183 0.0328  0.0967  0.0004  158 ILE   A C   
1204 O O   . ILE   A 159 ? 0.4752 0.5853 0.6410 0.0388  0.1051  -0.0059 158 ILE   A O   
1205 C CB  . ILE   A 159 ? 0.4338 0.5169 0.5967 0.0328  0.0694  -0.0031 158 ILE   A CB  
1206 C CG1 . ILE   A 159 ? 0.4383 0.5280 0.6161 0.0253  0.0675  0.0067  158 ILE   A CG1 
1207 C CG2 . ILE   A 159 ? 0.4336 0.5010 0.5861 0.0331  0.0558  -0.0061 158 ILE   A CG2 
1208 C CD1 . ILE   A 159 ? 0.4447 0.5403 0.6507 0.0249  0.0595  0.0073  158 ILE   A CD1 
1209 N N   . SER   A 160 ? 0.4900 0.5929 0.6317 0.0256  0.1015  0.0116  159 SER   A N   
1210 C CA  . SER   A 160 ? 0.5136 0.6332 0.6700 0.0229  0.1175  0.0188  159 SER   A CA  
1211 C C   . SER   A 160 ? 0.5575 0.6868 0.7006 0.0282  0.1367  0.0138  159 SER   A C   
1212 O O   . SER   A 160 ? 0.5608 0.7064 0.7204 0.0258  0.1522  0.0200  159 SER   A O   
1213 C CB  . SER   A 160 ? 0.5158 0.6336 0.6679 0.0133  0.1176  0.0335  159 SER   A CB  
1214 O OG  . SER   A 160 ? 0.5514 0.6583 0.6669 0.0124  0.1173  0.0371  159 SER   A OG  
1215 N N   . ALA   A 161 ? 0.5963 0.7159 0.7102 0.0347  0.1366  0.0028  160 ALA   A N   
1216 C CA  . ALA   A 161 ? 0.6354 0.7629 0.7326 0.0405  0.1556  -0.0047 160 ALA   A CA  
1217 C C   . ALA   A 161 ? 0.6505 0.7934 0.7832 0.0485  0.1664  -0.0147 160 ALA   A C   
1218 O O   . ALA   A 161 ? 0.6510 0.7876 0.7974 0.0554  0.1566  -0.0260 160 ALA   A O   
1219 C CB  . ALA   A 161 ? 0.6596 0.7706 0.7172 0.0453  0.1495  -0.0165 160 ALA   A CB  
1220 N N   . GLN   A 162 ? 0.6619 0.8252 0.8114 0.0475  0.1867  -0.0097 161 GLN   A N   
1221 C CA  . GLN   A 162 ? 0.6638 0.8453 0.8523 0.0555  0.1990  -0.0185 161 GLN   A CA  
1222 C C   . GLN   A 162 ? 0.6871 0.8684 0.8544 0.0668  0.2143  -0.0363 161 GLN   A C   
1223 O O   . GLN   A 162 ? 0.6790 0.8784 0.8500 0.0697  0.2390  -0.0384 161 GLN   A O   
1224 C CB  . GLN   A 162 ? 0.6742 0.8800 0.8949 0.0489  0.2155  -0.0054 161 GLN   A CB  
1225 C CG  . GLN   A 162 ? 0.7261 0.9302 0.9648 0.0368  0.2010  0.0112  161 GLN   A CG  
1226 C CD  . GLN   A 162 ? 0.7954 1.0202 1.0581 0.0281  0.2185  0.0259  161 GLN   A CD  
1227 O OE1 . GLN   A 162 ? 0.8298 1.0684 1.0839 0.0291  0.2432  0.0273  161 GLN   A OE1 
1228 N NE2 . GLN   A 162 ? 0.7886 1.0156 1.0814 0.0187  0.2066  0.0371  161 GLN   A NE2 
1229 N N   . ILE   A 163 ? 0.7106 0.8711 0.8557 0.0730  0.2001  -0.0498 162 ILE   A N   
1230 C CA  . ILE   A 163 ? 0.7298 0.8844 0.8526 0.0840  0.2101  -0.0701 162 ILE   A CA  
1231 C C   . ILE   A 163 ? 0.7301 0.8709 0.8737 0.0927  0.1932  -0.0838 162 ILE   A C   
1232 O O   . ILE   A 163 ? 0.7459 0.8716 0.8906 0.0881  0.1707  -0.0782 162 ILE   A O   
1233 C CB  . ILE   A 163 ? 0.7651 0.9032 0.8271 0.0808  0.2085  -0.0724 162 ILE   A CB  
1234 C CG1 . ILE   A 163 ? 0.7923 0.9111 0.8397 0.0724  0.1821  -0.0627 162 ILE   A CG1 
1235 C CG2 . ILE   A 163 ? 0.7764 0.9281 0.8123 0.0753  0.2306  -0.0620 162 ILE   A CG2 
1236 C CD1 . ILE   A 163 ? 0.8332 0.9324 0.8294 0.0714  0.1727  -0.0692 162 ILE   A CD1 
1237 N N   . GLY   A 164 ? 0.7137 0.8591 0.8736 0.1051  0.2049  -0.1012 163 GLY   A N   
1238 C CA  . GLY   A 164 ? 0.7052 0.8360 0.8866 0.1142  0.1898  -0.1141 163 GLY   A CA  
1239 C C   . GLY   A 164 ? 0.6793 0.8110 0.9036 0.1120  0.1710  -0.1027 163 GLY   A C   
1240 O O   . GLY   A 164 ? 0.6654 0.8180 0.9284 0.1114  0.1767  -0.0940 163 GLY   A O   
1241 N N   . ALA   A 165 ? 0.6698 0.7789 0.8872 0.1103  0.1480  -0.1026 164 ALA   A N   
1242 C CA  . ALA   A 165 ? 0.6403 0.7462 0.8901 0.1082  0.1284  -0.0922 164 ALA   A CA  
1243 C C   . ALA   A 165 ? 0.5988 0.7093 0.8447 0.0948  0.1192  -0.0728 164 ALA   A C   
1244 O O   . ALA   A 165 ? 0.6062 0.7023 0.8464 0.0893  0.1004  -0.0656 164 ALA   A O   
1245 C CB  . ALA   A 165 ? 0.6597 0.7395 0.9033 0.1113  0.1098  -0.0992 164 ALA   A CB  
1246 N N   . GLU   A 166 ? 0.5521 0.6825 0.8031 0.0897  0.1331  -0.0644 165 GLU   A N   
1247 C CA  . GLU   A 166 ? 0.5195 0.6537 0.7697 0.0776  0.1253  -0.0477 165 GLU   A CA  
1248 C C   . GLU   A 166 ? 0.4738 0.6072 0.7546 0.0757  0.1064  -0.0403 165 GLU   A C   
1249 O O   . GLU   A 166 ? 0.4787 0.6019 0.7463 0.0674  0.0926  -0.0316 165 GLU   A O   
1250 C CB  . GLU   A 166 ? 0.5276 0.6838 0.7856 0.0727  0.1444  -0.0400 165 GLU   A CB  
1251 C CG  . GLU   A 166 ? 0.5607 0.7188 0.8182 0.0600  0.1371  -0.0237 165 GLU   A CG  
1252 C CD  . GLU   A 166 ? 0.5542 0.7226 0.8534 0.0568  0.1260  -0.0165 165 GLU   A CD  
1253 O OE1 . GLU   A 166 ? 0.5021 0.6862 0.8390 0.0634  0.1311  -0.0207 165 GLU   A OE1 
1254 O OE2 . GLU   A 166 ? 0.5419 0.7020 0.8365 0.0484  0.1111  -0.0079 165 GLU   A OE2 
1255 N N   . LEU   A 167 ? 0.4279 0.5723 0.7493 0.0836  0.1057  -0.0438 166 LEU   A N   
1256 C CA  . LEU   A 167 ? 0.3993 0.5433 0.7474 0.0815  0.0861  -0.0356 166 LEU   A CA  
1257 C C   . LEU   A 167 ? 0.3942 0.5136 0.7239 0.0813  0.0662  -0.0350 166 LEU   A C   
1258 O O   . LEU   A 167 ? 0.3863 0.4991 0.7095 0.0734  0.0512  -0.0253 166 LEU   A O   
1259 C CB  . LEU   A 167 ? 0.3848 0.5472 0.7837 0.0906  0.0881  -0.0386 166 LEU   A CB  
1260 C CG  . LEU   A 167 ? 0.4074 0.5718 0.8336 0.0874  0.0662  -0.0286 166 LEU   A CG  
1261 C CD1 . LEU   A 167 ? 0.4167 0.5899 0.8406 0.0741  0.0630  -0.0174 166 LEU   A CD1 
1262 C CD2 . LEU   A 167 ? 0.3963 0.5760 0.8740 0.0979  0.0640  -0.0318 166 LEU   A CD2 
1263 N N   . ALA   A 168 ? 0.3957 0.5012 0.7173 0.0896  0.0667  -0.0457 167 ALA   A N   
1264 C CA  . ALA   A 168 ? 0.3984 0.4801 0.7053 0.0887  0.0493  -0.0442 167 ALA   A CA  
1265 C C   . ALA   A 168 ? 0.3967 0.4669 0.6654 0.0778  0.0454  -0.0385 167 ALA   A C   
1266 O O   . ALA   A 168 ? 0.4029 0.4607 0.6631 0.0724  0.0309  -0.0308 167 ALA   A O   
1267 C CB  . ALA   A 168 ? 0.4113 0.4798 0.7193 0.0993  0.0518  -0.0582 167 ALA   A CB  
1268 N N   . ARG   A 169 ? 0.3833 0.4583 0.6296 0.0746  0.0586  -0.0415 168 ARG   A N   
1269 C CA  . ARG   A 169 ? 0.3985 0.4649 0.6135 0.0653  0.0553  -0.0361 168 ARG   A CA  
1270 C C   . ARG   A 169 ? 0.3775 0.4513 0.5981 0.0565  0.0495  -0.0234 168 ARG   A C   
1271 O O   . ARG   A 169 ? 0.3929 0.4566 0.5991 0.0500  0.0397  -0.0176 168 ARG   A O   
1272 C CB  . ARG   A 169 ? 0.4264 0.4966 0.6177 0.0654  0.0701  -0.0419 168 ARG   A CB  
1273 C CG  . ARG   A 169 ? 0.4852 0.5507 0.6500 0.0562  0.0675  -0.0344 168 ARG   A CG  
1274 C CD  . ARG   A 169 ? 0.5176 0.5772 0.6521 0.0573  0.0740  -0.0417 168 ARG   A CD  
1275 N NE  . ARG   A 169 ? 0.5337 0.5832 0.6474 0.0497  0.0642  -0.0355 168 ARG   A NE  
1276 C CZ  . ARG   A 169 ? 0.5455 0.5927 0.6322 0.0468  0.0669  -0.0348 168 ARG   A CZ  
1277 N NH1 . ARG   A 169 ? 0.5349 0.5883 0.6062 0.0503  0.0801  -0.0399 168 ARG   A NH1 
1278 N NH2 . ARG   A 169 ? 0.5457 0.5849 0.6205 0.0407  0.0566  -0.0288 168 ARG   A NH2 
1279 N N   . ARG   A 170 ? 0.3438 0.4354 0.5877 0.0562  0.0558  -0.0200 169 ARG   A N   
1280 C CA  . ARG   A 170 ? 0.3229 0.4210 0.5748 0.0479  0.0496  -0.0101 169 ARG   A CA  
1281 C C   . ARG   A 170 ? 0.3211 0.4110 0.5807 0.0467  0.0312  -0.0059 169 ARG   A C   
1282 O O   . ARG   A 170 ? 0.3148 0.4001 0.5643 0.0392  0.0227  0.0001  169 ARG   A O   
1283 C CB  . ARG   A 170 ? 0.3180 0.4378 0.6000 0.0484  0.0597  -0.0083 169 ARG   A CB  
1284 C CG  . ARG   A 170 ? 0.3378 0.4643 0.6280 0.0387  0.0555  0.0006  169 ARG   A CG  
1285 C CD  . ARG   A 170 ? 0.3543 0.5003 0.6859 0.0393  0.0558  0.0026  169 ARG   A CD  
1286 N NE  . ARG   A 170 ? 0.3637 0.5276 0.7134 0.0438  0.0759  -0.0002 169 ARG   A NE  
1287 C CZ  . ARG   A 170 ? 0.3781 0.5632 0.7696 0.0452  0.0805  0.0010  169 ARG   A CZ  
1288 N NH1 . ARG   A 170 ? 0.3544 0.5565 0.7603 0.0495  0.1020  -0.0019 169 ARG   A NH1 
1289 N NH2 . ARG   A 170 ? 0.3517 0.5417 0.7714 0.0426  0.0635  0.0047  169 ARG   A NH2 
1290 N N   . LEU   A 171 ? 0.3239 0.4118 0.6012 0.0546  0.0252  -0.0090 170 LEU   A N   
1291 C CA  . LEU   A 171 ? 0.3334 0.4136 0.6180 0.0543  0.0072  -0.0032 170 LEU   A CA  
1292 C C   . LEU   A 171 ? 0.3460 0.4053 0.6091 0.0542  -0.0012 -0.0022 170 LEU   A C   
1293 O O   . LEU   A 171 ? 0.3550 0.4062 0.6191 0.0531  -0.0157 0.0046  170 LEU   A O   
1294 C CB  . LEU   A 171 ? 0.3222 0.4127 0.6445 0.0630  0.0032  -0.0046 170 LEU   A CB  
1295 C CG  . LEU   A 171 ? 0.3322 0.4454 0.6857 0.0623  0.0074  -0.0033 170 LEU   A CG  
1296 C CD1 . LEU   A 171 ? 0.3259 0.4485 0.7204 0.0719  0.0008  -0.0044 170 LEU   A CD1 
1297 C CD2 . LEU   A 171 ? 0.3390 0.4541 0.6865 0.0515  -0.0034 0.0046  170 LEU   A CD2 
1298 N N   . GLU   A 172 ? 0.3419 0.3925 0.5866 0.0552  0.0069  -0.0083 171 GLU   A N   
1299 C CA  . GLU   A 172 ? 0.3489 0.3802 0.5777 0.0545  -0.0001 -0.0079 171 GLU   A CA  
1300 C C   . GLU   A 172 ? 0.3410 0.3642 0.5523 0.0455  -0.0098 0.0022  171 GLU   A C   
1301 O O   . GLU   A 172 ? 0.3458 0.3557 0.5537 0.0449  -0.0190 0.0072  171 GLU   A O   
1302 C CB  . GLU   A 172 ? 0.3666 0.3920 0.5770 0.0548  0.0094  -0.0165 171 GLU   A CB  
1303 C CG  . GLU   A 172 ? 0.4460 0.4520 0.6481 0.0550  0.0022  -0.0182 171 GLU   A CG  
1304 C CD  . GLU   A 172 ? 0.5451 0.5451 0.7304 0.0553  0.0086  -0.0282 171 GLU   A CD  
1305 O OE1 . GLU   A 172 ? 0.5667 0.5513 0.7517 0.0572  0.0033  -0.0332 171 GLU   A OE1 
1306 O OE2 . GLU   A 172 ? 0.5405 0.5501 0.7127 0.0533  0.0176  -0.0306 171 GLU   A OE2 
1307 N N   . PHE   A 173 ? 0.3147 0.3453 0.5150 0.0386  -0.0068 0.0050  172 PHE   A N   
1308 C CA  . PHE   A 173 ? 0.3087 0.3326 0.4914 0.0309  -0.0133 0.0120  172 PHE   A CA  
1309 C C   . PHE   A 173 ? 0.3298 0.3499 0.5170 0.0306  -0.0267 0.0195  172 PHE   A C   
1310 O O   . PHE   A 173 ? 0.3541 0.3648 0.5238 0.0256  -0.0318 0.0255  172 PHE   A O   
1311 C CB  . PHE   A 173 ? 0.2950 0.3271 0.4696 0.0249  -0.0081 0.0118  172 PHE   A CB  
1312 C CG  . PHE   A 173 ? 0.2968 0.3401 0.4863 0.0238  -0.0124 0.0134  172 PHE   A CG  
1313 C CD1 . PHE   A 173 ? 0.2980 0.3547 0.5095 0.0275  -0.0065 0.0104  172 PHE   A CD1 
1314 C CD2 . PHE   A 173 ? 0.3083 0.3488 0.4907 0.0192  -0.0229 0.0176  172 PHE   A CD2 
1315 C CE1 . PHE   A 173 ? 0.2903 0.3585 0.5214 0.0258  -0.0117 0.0122  172 PHE   A CE1 
1316 C CE2 . PHE   A 173 ? 0.3140 0.3643 0.5122 0.0177  -0.0298 0.0180  172 PHE   A CE2 
1317 C CZ  . PHE   A 173 ? 0.2936 0.3580 0.5182 0.0207  -0.0244 0.0156  172 PHE   A CZ  
1318 N N   . ILE   A 174 ? 0.3273 0.3550 0.5376 0.0359  -0.0327 0.0199  173 ILE   A N   
1319 C CA  . ILE   A 174 ? 0.3503 0.3741 0.5648 0.0360  -0.0485 0.0283  173 ILE   A CA  
1320 C C   . ILE   A 174 ? 0.3837 0.3893 0.5881 0.0367  -0.0553 0.0351  173 ILE   A C   
1321 O O   . ILE   A 174 ? 0.4079 0.4051 0.5971 0.0323  -0.0660 0.0449  173 ILE   A O   
1322 C CB  . ILE   A 174 ? 0.3370 0.3740 0.5859 0.0431  -0.0532 0.0266  173 ILE   A CB  
1323 C CG1 . ILE   A 174 ? 0.3253 0.3793 0.5836 0.0392  -0.0491 0.0233  173 ILE   A CG1 
1324 C CG2 . ILE   A 174 ? 0.3685 0.3998 0.6275 0.0459  -0.0723 0.0358  173 ILE   A CG2 
1325 C CD1 . ILE   A 174 ? 0.3060 0.3781 0.6067 0.0456  -0.0524 0.0217  173 ILE   A CD1 
1326 N N   . GLY   A 175 ? 0.3657 0.3645 0.5768 0.0415  -0.0485 0.0298  174 GLY   A N   
1327 C CA  . GLY   A 175 ? 0.3716 0.3520 0.5773 0.0414  -0.0539 0.0356  174 GLY   A CA  
1328 C C   . GLY   A 175 ? 0.3723 0.3449 0.5533 0.0331  -0.0470 0.0368  174 GLY   A C   
1329 O O   . GLY   A 175 ? 0.3854 0.3434 0.5605 0.0302  -0.0509 0.0439  174 GLY   A O   
1330 N N   . THR   A 176 ? 0.3758 0.3581 0.5454 0.0292  -0.0367 0.0307  175 THR   A N   
1331 C CA  . THR   A 176 ? 0.3815 0.3595 0.5329 0.0220  -0.0300 0.0310  175 THR   A CA  
1332 C C   . THR   A 176 ? 0.3601 0.3501 0.5004 0.0178  -0.0236 0.0282  175 THR   A C   
1333 O O   . THR   A 176 ? 0.3534 0.3499 0.4946 0.0184  -0.0155 0.0210  175 THR   A O   
1334 C CB  . THR   A 176 ? 0.4257 0.3980 0.5829 0.0246  -0.0250 0.0229  175 THR   A CB  
1335 O OG1 . THR   A 176 ? 0.4544 0.4263 0.5987 0.0179  -0.0192 0.0226  175 THR   A OG1 
1336 C CG2 . THR   A 176 ? 0.4171 0.3982 0.5852 0.0319  -0.0192 0.0114  175 THR   A CG2 
1337 N N   . PRO   A 177 ? 0.3466 0.3386 0.4767 0.0139  -0.0285 0.0339  176 PRO   A N   
1338 C CA  . PRO   A 177 ? 0.3294 0.3311 0.4529 0.0107  -0.0243 0.0297  176 PRO   A CA  
1339 C C   . PRO   A 177 ? 0.3183 0.3186 0.4252 0.0049  -0.0166 0.0289  176 PRO   A C   
1340 O O   . PRO   A 177 ? 0.3295 0.3352 0.4312 0.0024  -0.0139 0.0253  176 PRO   A O   
1341 C CB  . PRO   A 177 ? 0.3414 0.3436 0.4602 0.0093  -0.0353 0.0346  176 PRO   A CB  
1342 C CG  . PRO   A 177 ? 0.3713 0.3610 0.4790 0.0079  -0.0420 0.0447  176 PRO   A CG  
1343 C CD  . PRO   A 177 ? 0.3466 0.3308 0.4701 0.0126  -0.0397 0.0441  176 PRO   A CD  
1344 N N   . TYR   A 178 ? 0.2981 0.2913 0.4003 0.0028  -0.0132 0.0319  177 TYR   A N   
1345 C CA  . TYR   A 178 ? 0.3047 0.2972 0.3947 -0.0028 -0.0057 0.0327  177 TYR   A CA  
1346 C C   . TYR   A 178 ? 0.3030 0.3032 0.3955 -0.0030 0.0019  0.0253  177 TYR   A C   
1347 O O   . TYR   A 178 ? 0.3053 0.3070 0.3891 -0.0065 0.0075  0.0243  177 TYR   A O   
1348 C CB  . TYR   A 178 ? 0.3041 0.2891 0.3971 -0.0051 -0.0039 0.0375  177 TYR   A CB  
1349 C CG  . TYR   A 178 ? 0.3008 0.2755 0.3935 -0.0047 -0.0123 0.0466  177 TYR   A CG  
1350 C CD1 . TYR   A 178 ? 0.3155 0.2855 0.3910 -0.0090 -0.0150 0.0562  177 TYR   A CD1 
1351 C CD2 . TYR   A 178 ? 0.3064 0.2753 0.4149 0.0004  -0.0181 0.0452  177 TYR   A CD2 
1352 C CE1 . TYR   A 178 ? 0.3143 0.2736 0.3895 -0.0085 -0.0247 0.0666  177 TYR   A CE1 
1353 C CE2 . TYR   A 178 ? 0.2920 0.2499 0.4039 0.0015  -0.0271 0.0540  177 TYR   A CE2 
1354 C CZ  . TYR   A 178 ? 0.3092 0.2623 0.4049 -0.0031 -0.0311 0.0658  177 TYR   A CZ  
1355 O OH  . TYR   A 178 ? 0.3459 0.2867 0.4442 -0.0021 -0.0416 0.0769  177 TYR   A OH  
1356 N N   . TRP   A 179 ? 0.2874 0.2919 0.3915 0.0008  0.0026  0.0204  178 TRP   A N   
1357 C CA  . TRP   A 179 ? 0.2855 0.2957 0.3924 0.0006  0.0082  0.0158  178 TRP   A CA  
1358 C C   . TRP   A 179 ? 0.2961 0.3121 0.4059 0.0012  0.0077  0.0131  178 TRP   A C   
1359 O O   . TRP   A 179 ? 0.3020 0.3211 0.4152 0.0008  0.0117  0.0106  178 TRP   A O   
1360 C CB  . TRP   A 179 ? 0.2683 0.2789 0.3823 0.0037  0.0091  0.0132  178 TRP   A CB  
1361 C CG  . TRP   A 179 ? 0.2621 0.2676 0.3768 0.0019  0.0090  0.0141  178 TRP   A CG  
1362 C CD1 . TRP   A 179 ? 0.2704 0.2779 0.3879 -0.0002 0.0116  0.0132  178 TRP   A CD1 
1363 C CD2 . TRP   A 179 ? 0.2565 0.2541 0.3738 0.0020  0.0048  0.0161  178 TRP   A CD2 
1364 N NE1 . TRP   A 179 ? 0.2695 0.2719 0.3916 -0.0023 0.0093  0.0145  178 TRP   A NE1 
1365 C CE2 . TRP   A 179 ? 0.2664 0.2617 0.3879 -0.0013 0.0054  0.0163  178 TRP   A CE2 
1366 C CE3 . TRP   A 179 ? 0.2704 0.2620 0.3896 0.0044  -0.0002 0.0185  178 TRP   A CE3 
1367 C CZ2 . TRP   A 179 ? 0.2773 0.2637 0.4046 -0.0029 0.0012  0.0180  178 TRP   A CZ2 
1368 C CZ3 . TRP   A 179 ? 0.2807 0.2623 0.4052 0.0038  -0.0043 0.0204  178 TRP   A CZ3 
1369 C CH2 . TRP   A 179 ? 0.2791 0.2577 0.4071 -0.0005 -0.0033 0.0204  178 TRP   A CH2 
1370 N N   . MET   A 180 ? 0.2953 0.3124 0.4070 0.0020  0.0017  0.0142  179 MET   A N   
1371 C CA  . MET   A 180 ? 0.2838 0.3070 0.4033 0.0016  0.0001  0.0118  179 MET   A CA  
1372 C C   . MET   A 180 ? 0.3029 0.3240 0.4133 -0.0026 -0.0018 0.0091  179 MET   A C   
1373 O O   . MET   A 180 ? 0.3140 0.3298 0.4090 -0.0047 -0.0043 0.0100  179 MET   A O   
1374 C CB  . MET   A 180 ? 0.2730 0.3011 0.4056 0.0047  -0.0060 0.0133  179 MET   A CB  
1375 C CG  . MET   A 180 ? 0.3107 0.3424 0.4544 0.0099  -0.0012 0.0125  179 MET   A CG  
1376 S SD  . MET   A 180 ? 0.3393 0.3773 0.4868 0.0097  0.0093  0.0104  179 MET   A SD  
1377 C CE  . MET   A 180 ? 0.3224 0.3522 0.4557 0.0105  0.0127  0.0093  179 MET   A CE  
1378 N N   . ALA   A 181 ? 0.2962 0.3207 0.4153 -0.0040 -0.0007 0.0056  180 ALA   A N   
1379 C CA  . ALA   A 181 ? 0.3057 0.3265 0.4181 -0.0077 -0.0029 0.0002  180 ALA   A CA  
1380 C C   . ALA   A 181 ? 0.3105 0.3312 0.4188 -0.0094 -0.0141 -0.0005 180 ALA   A C   
1381 O O   . ALA   A 181 ? 0.2861 0.3125 0.4071 -0.0076 -0.0198 0.0035  180 ALA   A O   
1382 C CB  . ALA   A 181 ? 0.2967 0.3195 0.4242 -0.0090 0.0000  -0.0023 180 ALA   A CB  
1383 N N   . PRO   A 182 ? 0.3284 0.3431 0.4200 -0.0126 -0.0183 -0.0061 181 PRO   A N   
1384 C CA  . PRO   A 182 ? 0.3360 0.3500 0.4207 -0.0146 -0.0322 -0.0063 181 PRO   A CA  
1385 C C   . PRO   A 182 ? 0.3251 0.3469 0.4361 -0.0155 -0.0407 -0.0068 181 PRO   A C   
1386 O O   . PRO   A 182 ? 0.3422 0.3679 0.4593 -0.0149 -0.0522 -0.0030 181 PRO   A O   
1387 C CB  . PRO   A 182 ? 0.3566 0.3621 0.4173 -0.0182 -0.0335 -0.0157 181 PRO   A CB  
1388 C CG  . PRO   A 182 ? 0.3723 0.3747 0.4248 -0.0169 -0.0180 -0.0179 181 PRO   A CG  
1389 C CD  . PRO   A 182 ? 0.3365 0.3450 0.4140 -0.0140 -0.0107 -0.0131 181 PRO   A CD  
1390 N N   . GLU   A 183 ? 0.3118 0.3362 0.4410 -0.0171 -0.0354 -0.0104 182 GLU   A N   
1391 C CA  . GLU   A 183 ? 0.3053 0.3386 0.4634 -0.0194 -0.0420 -0.0097 182 GLU   A CA  
1392 C C   . GLU   A 183 ? 0.2986 0.3436 0.4770 -0.0150 -0.0385 -0.0015 182 GLU   A C   
1393 O O   . GLU   A 183 ? 0.2990 0.3538 0.5006 -0.0157 -0.0458 0.0003  182 GLU   A O   
1394 C CB  . GLU   A 183 ? 0.2962 0.3277 0.4693 -0.0232 -0.0369 -0.0137 182 GLU   A CB  
1395 C CG  . GLU   A 183 ? 0.2821 0.3149 0.4599 -0.0204 -0.0220 -0.0084 182 GLU   A CG  
1396 C CD  . GLU   A 183 ? 0.3054 0.3284 0.4635 -0.0185 -0.0144 -0.0116 182 GLU   A CD  
1397 O OE1 . GLU   A 183 ? 0.2684 0.2847 0.4049 -0.0182 -0.0170 -0.0171 182 GLU   A OE1 
1398 O OE2 . GLU   A 183 ? 0.2976 0.3205 0.4620 -0.0171 -0.0055 -0.0078 182 GLU   A OE2 
1399 N N   . VAL   A 184 ? 0.2939 0.3381 0.4642 -0.0104 -0.0283 0.0025  183 VAL   A N   
1400 C CA  . VAL   A 184 ? 0.2921 0.3449 0.4770 -0.0051 -0.0241 0.0076  183 VAL   A CA  
1401 C C   . VAL   A 184 ? 0.3078 0.3587 0.4876 -0.0019 -0.0347 0.0104  183 VAL   A C   
1402 O O   . VAL   A 184 ? 0.3013 0.3610 0.5026 0.0015  -0.0396 0.0128  183 VAL   A O   
1403 C CB  . VAL   A 184 ? 0.2940 0.3439 0.4696 -0.0019 -0.0112 0.0091  183 VAL   A CB  
1404 C CG1 . VAL   A 184 ? 0.3061 0.3620 0.4919 0.0041  -0.0074 0.0114  183 VAL   A CG1 
1405 C CG2 . VAL   A 184 ? 0.2918 0.3428 0.4725 -0.0047 -0.0025 0.0089  183 VAL   A CG2 
1406 N N   . ALA   A 185 ? 0.3224 0.3619 0.4751 -0.0028 -0.0380 0.0108  184 ALA   A N   
1407 C CA  . ALA   A 185 ? 0.3307 0.3654 0.4737 -0.0011 -0.0493 0.0159  184 ALA   A CA  
1408 C C   . ALA   A 185 ? 0.3338 0.3734 0.4878 -0.0027 -0.0662 0.0161  184 ALA   A C   
1409 O O   . ALA   A 185 ? 0.3428 0.3823 0.5017 0.0005  -0.0776 0.0220  184 ALA   A O   
1410 C CB  . ALA   A 185 ? 0.3450 0.3675 0.4550 -0.0040 -0.0477 0.0168  184 ALA   A CB  
1411 N N   . ALA   A 186 ? 0.3178 0.3620 0.4810 -0.0074 -0.0689 0.0100  185 ALA   A N   
1412 C CA  . ALA   A 186 ? 0.3193 0.3699 0.4992 -0.0099 -0.0862 0.0090  185 ALA   A CA  
1413 C C   . ALA   A 186 ? 0.3188 0.3863 0.5422 -0.0061 -0.0844 0.0119  185 ALA   A C   
1414 O O   . ALA   A 186 ? 0.2935 0.3715 0.5442 -0.0097 -0.0890 0.0094  185 ALA   A O   
1415 C CB  . ALA   A 186 ? 0.3139 0.3614 0.4888 -0.0171 -0.0895 0.0001  185 ALA   A CB  
1416 N N   . VAL   A 187 ? 0.3311 0.4010 0.5619 0.0011  -0.0767 0.0166  186 VAL   A N   
1417 C CA  . VAL   A 187 ? 0.3185 0.4038 0.5869 0.0067  -0.0708 0.0181  186 VAL   A CA  
1418 C C   . VAL   A 187 ? 0.2968 0.3938 0.5964 0.0072  -0.0882 0.0201  186 VAL   A C   
1419 O O   . VAL   A 187 ? 0.3056 0.3959 0.5945 0.0070  -0.1069 0.0232  186 VAL   A O   
1420 C CB  . VAL   A 187 ? 0.3386 0.4196 0.6030 0.0149  -0.0622 0.0205  186 VAL   A CB  
1421 C CG1 . VAL   A 187 ? 0.3618 0.4313 0.6118 0.0176  -0.0772 0.0261  186 VAL   A CG1 
1422 C CG2 . VAL   A 187 ? 0.3266 0.4231 0.6269 0.0217  -0.0525 0.0194  186 VAL   A CG2 
1423 N N   . ALA   A 188 ? 0.2724 0.3873 0.6106 0.0070  -0.0823 0.0189  187 ALA   A N   
1424 C CA  . ALA   A 188 ? 0.2599 0.3908 0.6389 0.0073  -0.0969 0.0204  187 ALA   A CA  
1425 C C   . ALA   A 188 ? 0.2794 0.4070 0.6537 -0.0016 -0.1176 0.0183  187 ALA   A C   
1426 O O   . ALA   A 188 ? 0.2788 0.4177 0.6838 -0.0019 -0.1352 0.0198  187 ALA   A O   
1427 C CB  . ALA   A 188 ? 0.2627 0.3962 0.6575 0.0171  -0.1063 0.0249  187 ALA   A CB  
1428 N N   . LEU   A 189 ? 0.3016 0.4148 0.6414 -0.0087 -0.1156 0.0136  188 LEU   A N   
1429 C CA  . LEU   A 189 ? 0.3141 0.4233 0.6497 -0.0176 -0.1333 0.0083  188 LEU   A CA  
1430 C C   . LEU   A 189 ? 0.3026 0.4199 0.6640 -0.0247 -0.1222 0.0046  188 LEU   A C   
1431 O O   . LEU   A 189 ? 0.2955 0.4174 0.6641 -0.0228 -0.1003 0.0070  188 LEU   A O   
1432 C CB  . LEU   A 189 ? 0.3452 0.4324 0.6262 -0.0205 -0.1392 0.0042  188 LEU   A CB  
1433 C CG  . LEU   A 189 ? 0.3669 0.4449 0.6205 -0.0160 -0.1533 0.0099  188 LEU   A CG  
1434 C CD1 . LEU   A 189 ? 0.3941 0.4519 0.5923 -0.0197 -0.1542 0.0059  188 LEU   A CD1 
1435 C CD2 . LEU   A 189 ? 0.3502 0.4369 0.6276 -0.0161 -0.1798 0.0132  188 LEU   A CD2 
1436 N N   . LYS   A 190 ? 0.2997 0.4173 0.6733 -0.0332 -0.1377 -0.0009 189 LYS   A N   
1437 C CA  . LYS   A 190 ? 0.2991 0.4237 0.7033 -0.0410 -0.1299 -0.0028 189 LYS   A CA  
1438 C C   . LYS   A 190 ? 0.3155 0.4282 0.6989 -0.0434 -0.1096 -0.0045 189 LYS   A C   
1439 O O   . LYS   A 190 ? 0.2965 0.4174 0.7087 -0.0478 -0.0973 -0.0012 189 LYS   A O   
1440 C CB  . LYS   A 190 ? 0.3111 0.4340 0.7292 -0.0505 -0.1540 -0.0102 189 LYS   A CB  
1441 C CG  . LYS   A 190 ? 0.3801 0.4790 0.7515 -0.0548 -0.1633 -0.0212 189 LYS   A CG  
1442 C CD  . LYS   A 190 ? 0.4168 0.5132 0.8013 -0.0640 -0.1898 -0.0306 189 LYS   A CD  
1443 C CE  . LYS   A 190 ? 0.5058 0.5776 0.8398 -0.0671 -0.1970 -0.0438 189 LYS   A CE  
1444 N NZ  . LYS   A 190 ? 0.5374 0.6038 0.8623 -0.0724 -0.2279 -0.0531 189 LYS   A NZ  
1445 N N   . GLY   A 191 ? 0.3440 0.4377 0.6807 -0.0410 -0.1070 -0.0089 190 GLY   A N   
1446 C CA  . GLY   A 191 ? 0.3790 0.4612 0.6997 -0.0429 -0.0910 -0.0110 190 GLY   A CA  
1447 C C   . GLY   A 191 ? 0.3966 0.4854 0.7187 -0.0369 -0.0694 -0.0025 190 GLY   A C   
1448 O O   . GLY   A 191 ? 0.4180 0.5089 0.7270 -0.0294 -0.0664 0.0009  190 GLY   A O   
1449 N N   . GLY   A 192 ? 0.3747 0.4656 0.7121 -0.0403 -0.0555 0.0013  191 GLY   A N   
1450 C CA  . GLY   A 192 ? 0.3632 0.4589 0.6958 -0.0348 -0.0358 0.0087  191 GLY   A CA  
1451 C C   . GLY   A 192 ? 0.3671 0.4458 0.6623 -0.0320 -0.0298 0.0061  191 GLY   A C   
1452 O O   . GLY   A 192 ? 0.3831 0.4491 0.6537 -0.0318 -0.0391 -0.0012 191 GLY   A O   
1453 N N   . TYR   A 193 ? 0.3329 0.4123 0.6234 -0.0296 -0.0140 0.0121  192 TYR   A N   
1454 C CA  . TYR   A 193 ? 0.3069 0.3722 0.5690 -0.0273 -0.0084 0.0107  192 TYR   A CA  
1455 C C   . TYR   A 193 ? 0.3081 0.3739 0.5777 -0.0293 0.0042  0.0187  192 TYR   A C   
1456 O O   . TYR   A 193 ? 0.3112 0.3884 0.6049 -0.0328 0.0101  0.0256  192 TYR   A O   
1457 C CB  . TYR   A 193 ? 0.2941 0.3572 0.5312 -0.0198 -0.0064 0.0097  192 TYR   A CB  
1458 C CG  . TYR   A 193 ? 0.2799 0.3537 0.5219 -0.0145 0.0031  0.0150  192 TYR   A CG  
1459 C CD1 . TYR   A 193 ? 0.2738 0.3481 0.5100 -0.0130 0.0159  0.0199  192 TYR   A CD1 
1460 C CD2 . TYR   A 193 ? 0.2655 0.3485 0.5182 -0.0105 -0.0013 0.0146  192 TYR   A CD2 
1461 C CE1 . TYR   A 193 ? 0.2746 0.3577 0.5117 -0.0078 0.0251  0.0224  192 TYR   A CE1 
1462 C CE2 . TYR   A 193 ? 0.2746 0.3658 0.5314 -0.0044 0.0082  0.0169  192 TYR   A CE2 
1463 C CZ  . TYR   A 193 ? 0.2856 0.3768 0.5333 -0.0031 0.0220  0.0198  192 TYR   A CZ  
1464 O OH  . TYR   A 193 ? 0.3019 0.4006 0.5511 0.0031  0.0317  0.0197  192 TYR   A OH  
1465 N N   . ASN   A 194 ? 0.3125 0.3664 0.5629 -0.0277 0.0081  0.0187  193 ASN   A N   
1466 C CA  . ASN   A 194 ? 0.3089 0.3609 0.5623 -0.0292 0.0176  0.0277  193 ASN   A CA  
1467 C C   . ASN   A 194 ? 0.3041 0.3501 0.5317 -0.0231 0.0224  0.0285  193 ASN   A C   
1468 O O   . ASN   A 194 ? 0.2991 0.3441 0.5108 -0.0184 0.0197  0.0225  193 ASN   A O   
1469 C CB  . ASN   A 194 ? 0.3262 0.3678 0.5951 -0.0360 0.0133  0.0279  193 ASN   A CB  
1470 C CG  . ASN   A 194 ? 0.3622 0.3880 0.6182 -0.0345 0.0061  0.0174  193 ASN   A CG  
1471 O OD1 . ASN   A 194 ? 0.3685 0.3911 0.6025 -0.0288 0.0066  0.0125  193 ASN   A OD1 
1472 N ND2 . ASN   A 194 ? 0.3652 0.3810 0.6361 -0.0397 -0.0001 0.0130  193 ASN   A ND2 
1473 N N   . GLU   A 195 ? 0.2876 0.3295 0.5123 -0.0236 0.0284  0.0369  194 GLU   A N   
1474 C CA  . GLU   A 195 ? 0.2879 0.3255 0.4916 -0.0186 0.0312  0.0388  194 GLU   A CA  
1475 C C   . GLU   A 195 ? 0.2967 0.3247 0.4899 -0.0154 0.0252  0.0301  194 GLU   A C   
1476 O O   . GLU   A 195 ? 0.2886 0.3156 0.4671 -0.0111 0.0260  0.0296  194 GLU   A O   
1477 C CB  . GLU   A 195 ? 0.2956 0.3294 0.4999 -0.0208 0.0359  0.0511  194 GLU   A CB  
1478 C CG  . GLU   A 195 ? 0.2984 0.3193 0.5147 -0.0238 0.0306  0.0526  194 GLU   A CG  
1479 C CD  . GLU   A 195 ? 0.3772 0.3964 0.6186 -0.0311 0.0289  0.0542  194 GLU   A CD  
1480 O OE1 . GLU   A 195 ? 0.3770 0.3833 0.6297 -0.0333 0.0245  0.0552  194 GLU   A OE1 
1481 O OE2 . GLU   A 195 ? 0.3947 0.4251 0.6477 -0.0344 0.0312  0.0540  194 GLU   A OE2 
1482 N N   . LEU   A 196 ? 0.2931 0.3145 0.4941 -0.0178 0.0195  0.0225  195 LEU   A N   
1483 C CA  . LEU   A 196 ? 0.2699 0.2838 0.4607 -0.0148 0.0167  0.0135  195 LEU   A CA  
1484 C C   . LEU   A 196 ? 0.2615 0.2800 0.4362 -0.0117 0.0163  0.0088  195 LEU   A C   
1485 O O   . LEU   A 196 ? 0.2765 0.2912 0.4412 -0.0090 0.0171  0.0045  195 LEU   A O   
1486 C CB  . LEU   A 196 ? 0.2625 0.2674 0.4617 -0.0177 0.0118  0.0046  195 LEU   A CB  
1487 C CG  . LEU   A 196 ? 0.2834 0.2797 0.5005 -0.0201 0.0118  0.0095  195 LEU   A CG  
1488 C CD1 . LEU   A 196 ? 0.3159 0.3019 0.5442 -0.0235 0.0059  -0.0013 195 LEU   A CD1 
1489 C CD2 . LEU   A 196 ? 0.2726 0.2636 0.4868 -0.0152 0.0145  0.0128  195 LEU   A CD2 
1490 N N   . CYS   A 197 ? 0.2441 0.2711 0.4187 -0.0117 0.0156  0.0107  196 CYS   A N   
1491 C CA  . CYS   A 197 ? 0.2434 0.2728 0.4048 -0.0086 0.0144  0.0082  196 CYS   A CA  
1492 C C   . CYS   A 197 ? 0.2528 0.2813 0.4041 -0.0050 0.0187  0.0110  196 CYS   A C   
1493 O O   . CYS   A 197 ? 0.2668 0.2932 0.4079 -0.0033 0.0179  0.0084  196 CYS   A O   
1494 C CB  . CYS   A 197 ? 0.2552 0.2936 0.4240 -0.0081 0.0126  0.0102  196 CYS   A CB  
1495 S SG  . CYS   A 197 ? 0.2728 0.3203 0.4489 -0.0060 0.0214  0.0174  196 CYS   A SG  
1496 N N   . ASP   A 198 ? 0.2428 0.2724 0.3966 -0.0043 0.0225  0.0168  197 ASP   A N   
1497 C CA  . ASP   A 198 ? 0.2481 0.2763 0.3922 -0.0013 0.0238  0.0188  197 ASP   A CA  
1498 C C   . ASP   A 198 ? 0.2485 0.2711 0.3926 -0.0008 0.0222  0.0161  197 ASP   A C   
1499 O O   . ASP   A 198 ? 0.2423 0.2648 0.3808 0.0010  0.0216  0.0153  197 ASP   A O   
1500 C CB  . ASP   A 198 ? 0.2524 0.2821 0.3953 -0.0012 0.0267  0.0264  197 ASP   A CB  
1501 C CG  . ASP   A 198 ? 0.2870 0.3241 0.4275 -0.0004 0.0314  0.0282  197 ASP   A CG  
1502 O OD1 . ASP   A 198 ? 0.3007 0.3409 0.4396 0.0019  0.0310  0.0231  197 ASP   A OD1 
1503 O OD2 . ASP   A 198 ? 0.3177 0.3578 0.4591 -0.0019 0.0362  0.0351  197 ASP   A OD2 
1504 N N   . ILE   A 199 ? 0.2428 0.2611 0.3955 -0.0024 0.0219  0.0138  198 ILE   A N   
1505 C CA  . ILE   A 199 ? 0.2569 0.2710 0.4134 -0.0010 0.0225  0.0095  198 ILE   A CA  
1506 C C   . ILE   A 199 ? 0.2650 0.2803 0.4124 -0.0009 0.0242  0.0032  198 ILE   A C   
1507 O O   . ILE   A 199 ? 0.2671 0.2838 0.4147 0.0005  0.0263  0.0025  198 ILE   A O   
1508 C CB  . ILE   A 199 ? 0.2730 0.2805 0.4421 -0.0020 0.0220  0.0067  198 ILE   A CB  
1509 C CG1 . ILE   A 199 ? 0.2899 0.2954 0.4679 -0.0030 0.0203  0.0165  198 ILE   A CG1 
1510 C CG2 . ILE   A 199 ? 0.2743 0.2783 0.4501 0.0010  0.0245  0.0002  198 ILE   A CG2 
1511 C CD1 . ILE   A 199 ? 0.3029 0.3094 0.4792 -0.0002 0.0189  0.0240  198 ILE   A CD1 
1512 N N   . TRP   A 200 ? 0.2583 0.2738 0.3983 -0.0030 0.0226  0.0001  199 TRP   A N   
1513 C CA  . TRP   A 200 ? 0.2695 0.2850 0.3966 -0.0036 0.0235  -0.0032 199 TRP   A CA  
1514 C C   . TRP   A 200 ? 0.2841 0.3026 0.4076 -0.0024 0.0237  0.0019  199 TRP   A C   
1515 O O   . TRP   A 200 ? 0.2809 0.2993 0.4008 -0.0028 0.0269  0.0015  199 TRP   A O   
1516 C CB  . TRP   A 200 ? 0.2596 0.2748 0.3797 -0.0059 0.0181  -0.0049 199 TRP   A CB  
1517 C CG  . TRP   A 200 ? 0.2590 0.2730 0.3630 -0.0068 0.0170  -0.0051 199 TRP   A CG  
1518 C CD1 . TRP   A 200 ? 0.2636 0.2790 0.3634 -0.0059 0.0159  0.0006  199 TRP   A CD1 
1519 C CD2 . TRP   A 200 ? 0.2567 0.2665 0.3447 -0.0089 0.0171  -0.0107 199 TRP   A CD2 
1520 N NE1 . TRP   A 200 ? 0.2808 0.2929 0.3645 -0.0079 0.0150  0.0012  199 TRP   A NE1 
1521 C CE2 . TRP   A 200 ? 0.2703 0.2796 0.3441 -0.0098 0.0158  -0.0056 199 TRP   A CE2 
1522 C CE3 . TRP   A 200 ? 0.2693 0.2747 0.3525 -0.0102 0.0178  -0.0200 199 TRP   A CE3 
1523 C CZ2 . TRP   A 200 ? 0.2896 0.2948 0.3413 -0.0123 0.0160  -0.0077 199 TRP   A CZ2 
1524 C CZ3 . TRP   A 200 ? 0.2938 0.2952 0.3541 -0.0121 0.0179  -0.0249 199 TRP   A CZ3 
1525 C CH2 . TRP   A 200 ? 0.3006 0.3024 0.3438 -0.0134 0.0179  -0.0179 199 TRP   A CH2 
1526 N N   . SER   A 201 ? 0.2723 0.2931 0.3977 -0.0012 0.0211  0.0060  200 SER   A N   
1527 C CA  . SER   A 201 ? 0.2690 0.2903 0.3911 0.0003  0.0200  0.0085  200 SER   A CA  
1528 C C   . SER   A 201 ? 0.2616 0.2829 0.3877 0.0007  0.0211  0.0091  200 SER   A C   
1529 O O   . SER   A 201 ? 0.2683 0.2888 0.3935 0.0002  0.0203  0.0097  200 SER   A O   
1530 C CB  . SER   A 201 ? 0.2770 0.3011 0.4005 0.0024  0.0188  0.0103  200 SER   A CB  
1531 O OG  . SER   A 201 ? 0.2551 0.2816 0.3808 0.0024  0.0171  0.0099  200 SER   A OG  
1532 N N   . LEU   A 202 ? 0.2402 0.2621 0.3736 0.0014  0.0217  0.0097  201 LEU   A N   
1533 C CA  . LEU   A 202 ? 0.2586 0.2816 0.4000 0.0022  0.0207  0.0107  201 LEU   A CA  
1534 C C   . LEU   A 202 ? 0.2521 0.2768 0.4000 0.0010  0.0255  0.0076  201 LEU   A C   
1535 O O   . LEU   A 202 ? 0.2425 0.2697 0.3967 0.0002  0.0252  0.0085  201 LEU   A O   
1536 C CB  . LEU   A 202 ? 0.2748 0.2971 0.4237 0.0038  0.0184  0.0140  201 LEU   A CB  
1537 C CG  . LEU   A 202 ? 0.3061 0.3303 0.4670 0.0052  0.0147  0.0156  201 LEU   A CG  
1538 C CD1 . LEU   A 202 ? 0.2961 0.3216 0.4516 0.0048  0.0089  0.0166  201 LEU   A CD1 
1539 C CD2 . LEU   A 202 ? 0.3356 0.3576 0.5044 0.0071  0.0112  0.0201  201 LEU   A CD2 
1540 N N   . GLY   A 203 ? 0.2585 0.2819 0.4036 0.0003  0.0304  0.0035  202 GLY   A N   
1541 C CA  . GLY   A 203 ? 0.2469 0.2724 0.3930 -0.0009 0.0379  -0.0001 202 GLY   A CA  
1542 C C   . GLY   A 203 ? 0.2546 0.2804 0.3914 -0.0040 0.0389  0.0033  202 GLY   A C   
1543 O O   . GLY   A 203 ? 0.2580 0.2878 0.4024 -0.0057 0.0436  0.0046  202 GLY   A O   
1544 N N   . ILE   A 204 ? 0.2670 0.2889 0.3910 -0.0049 0.0341  0.0056  203 ILE   A N   
1545 C CA  . ILE   A 204 ? 0.2662 0.2860 0.3835 -0.0075 0.0331  0.0103  203 ILE   A CA  
1546 C C   . ILE   A 204 ? 0.2715 0.2922 0.4010 -0.0077 0.0299  0.0129  203 ILE   A C   
1547 O O   . ILE   A 204 ? 0.2893 0.3101 0.4228 -0.0110 0.0322  0.0162  203 ILE   A O   
1548 C CB  . ILE   A 204 ? 0.2544 0.2697 0.3611 -0.0068 0.0265  0.0122  203 ILE   A CB  
1549 C CG1 . ILE   A 204 ? 0.2703 0.2846 0.3658 -0.0074 0.0267  0.0092  203 ILE   A CG1 
1550 C CG2 . ILE   A 204 ? 0.2681 0.2786 0.3713 -0.0088 0.0239  0.0180  203 ILE   A CG2 
1551 C CD1 . ILE   A 204 ? 0.2811 0.2929 0.3598 -0.0111 0.0314  0.0107  203 ILE   A CD1 
1552 N N   . THR   A 205 ? 0.2542 0.2753 0.3888 -0.0047 0.0243  0.0116  204 THR   A N   
1553 C CA  . THR   A 205 ? 0.2563 0.2773 0.3994 -0.0049 0.0189  0.0122  204 THR   A CA  
1554 C C   . THR   A 205 ? 0.2617 0.2887 0.4218 -0.0071 0.0217  0.0128  204 THR   A C   
1555 O O   . THR   A 205 ? 0.2515 0.2784 0.4207 -0.0101 0.0192  0.0144  204 THR   A O   
1556 C CB  . THR   A 205 ? 0.2674 0.2881 0.4075 -0.0013 0.0133  0.0108  204 THR   A CB  
1557 O OG1 . THR   A 205 ? 0.2720 0.2894 0.4007 0.0005  0.0127  0.0100  204 THR   A OG1 
1558 C CG2 . THR   A 205 ? 0.2826 0.3023 0.4272 -0.0015 0.0055  0.0100  204 THR   A CG2 
1559 N N   . ALA   A 206 ? 0.2640 0.2959 0.4311 -0.0057 0.0273  0.0112  205 ALA   A N   
1560 C CA  . ALA   A 206 ? 0.2601 0.3000 0.4485 -0.0067 0.0315  0.0111  205 ALA   A CA  
1561 C C   . ALA   A 206 ? 0.2726 0.3151 0.4627 -0.0117 0.0406  0.0134  205 ALA   A C   
1562 O O   . ALA   A 206 ? 0.2726 0.3212 0.4823 -0.0146 0.0414  0.0155  205 ALA   A O   
1563 C CB  . ALA   A 206 ? 0.2631 0.3064 0.4599 -0.0028 0.0365  0.0075  205 ALA   A CB  
1564 N N   . ILE   A 207 ? 0.2785 0.3166 0.4489 -0.0132 0.0466  0.0139  206 ILE   A N   
1565 C CA  . ILE   A 207 ? 0.2879 0.3266 0.4541 -0.0187 0.0550  0.0188  206 ILE   A CA  
1566 C C   . ILE   A 207 ? 0.2927 0.3258 0.4628 -0.0224 0.0467  0.0247  206 ILE   A C   
1567 O O   . ILE   A 207 ? 0.2938 0.3297 0.4766 -0.0278 0.0508  0.0298  206 ILE   A O   
1568 C CB  . ILE   A 207 ? 0.3131 0.3461 0.4518 -0.0191 0.0594  0.0187  206 ILE   A CB  
1569 C CG1 . ILE   A 207 ? 0.3239 0.3609 0.4589 -0.0162 0.0682  0.0107  206 ILE   A CG1 
1570 C CG2 . ILE   A 207 ? 0.3321 0.3632 0.4613 -0.0255 0.0658  0.0271  206 ILE   A CG2 
1571 C CD1 . ILE   A 207 ? 0.3601 0.3903 0.4654 -0.0165 0.0691  0.0083  206 ILE   A CD1 
1572 N N   . GLU   A 208 ? 0.2879 0.3130 0.4495 -0.0195 0.0357  0.0234  207 GLU   A N   
1573 C CA  . GLU   A 208 ? 0.2860 0.3037 0.4518 -0.0216 0.0269  0.0259  207 GLU   A CA  
1574 C C   . GLU   A 208 ? 0.2945 0.3170 0.4843 -0.0243 0.0228  0.0251  207 GLU   A C   
1575 O O   . GLU   A 208 ? 0.2930 0.3116 0.4937 -0.0296 0.0203  0.0290  207 GLU   A O   
1576 C CB  . GLU   A 208 ? 0.3045 0.3155 0.4585 -0.0161 0.0180  0.0214  207 GLU   A CB  
1577 C CG  . GLU   A 208 ? 0.2988 0.3009 0.4563 -0.0163 0.0088  0.0203  207 GLU   A CG  
1578 C CD  . GLU   A 208 ? 0.3284 0.3272 0.4768 -0.0102 0.0024  0.0136  207 GLU   A CD  
1579 O OE1 . GLU   A 208 ? 0.3229 0.3265 0.4629 -0.0065 0.0051  0.0119  207 GLU   A OE1 
1580 O OE2 . GLU   A 208 ? 0.3340 0.3252 0.4844 -0.0095 -0.0048 0.0097  207 GLU   A OE2 
1581 N N   . LEU   A 209 ? 0.2904 0.3198 0.4895 -0.0209 0.0198  0.0206  208 LEU   A N   
1582 C CA  . LEU   A 209 ? 0.2817 0.3167 0.5057 -0.0233 0.0128  0.0199  208 LEU   A CA  
1583 C C   . LEU   A 209 ? 0.2801 0.3258 0.5283 -0.0288 0.0226  0.0243  208 LEU   A C   
1584 O O   . LEU   A 209 ? 0.2649 0.3135 0.5362 -0.0339 0.0174  0.0260  208 LEU   A O   
1585 C CB  . LEU   A 209 ? 0.2710 0.3107 0.4985 -0.0180 0.0060  0.0161  208 LEU   A CB  
1586 C CG  . LEU   A 209 ? 0.2813 0.3126 0.4854 -0.0132 -0.0017 0.0128  208 LEU   A CG  
1587 C CD1 . LEU   A 209 ? 0.2848 0.3208 0.4916 -0.0085 -0.0064 0.0124  208 LEU   A CD1 
1588 C CD2 . LEU   A 209 ? 0.2836 0.3057 0.4814 -0.0145 -0.0126 0.0096  208 LEU   A CD2 
1589 N N   . ALA   A 210 ? 0.2864 0.3378 0.5294 -0.0282 0.0372  0.0256  209 ALA   A N   
1590 C CA  . ALA   A 210 ? 0.2847 0.3477 0.5472 -0.0330 0.0514  0.0295  209 ALA   A CA  
1591 C C   . ALA   A 210 ? 0.3006 0.3579 0.5567 -0.0410 0.0572  0.0381  209 ALA   A C   
1592 O O   . ALA   A 210 ? 0.3017 0.3677 0.5809 -0.0476 0.0653  0.0437  209 ALA   A O   
1593 C CB  . ALA   A 210 ? 0.2849 0.3535 0.5372 -0.0288 0.0655  0.0257  209 ALA   A CB  
1594 N N   . GLU   A 211 ? 0.2980 0.3415 0.5248 -0.0405 0.0539  0.0405  210 GLU   A N   
1595 C CA  . GLU   A 211 ? 0.3210 0.3576 0.5386 -0.0475 0.0597  0.0508  210 GLU   A CA  
1596 C C   . GLU   A 211 ? 0.3422 0.3632 0.5574 -0.0497 0.0463  0.0546  210 GLU   A C   
1597 O O   . GLU   A 211 ? 0.3673 0.3809 0.5786 -0.0561 0.0496  0.0653  210 GLU   A O   
1598 C CB  . GLU   A 211 ? 0.3647 0.3986 0.5502 -0.0457 0.0692  0.0525  210 GLU   A CB  
1599 C CG  . GLU   A 211 ? 0.3737 0.4208 0.5597 -0.0430 0.0834  0.0464  210 GLU   A CG  
1600 C CD  . GLU   A 211 ? 0.4059 0.4509 0.5596 -0.0422 0.0938  0.0461  210 GLU   A CD  
1601 O OE1 . GLU   A 211 ? 0.3969 0.4300 0.5241 -0.0431 0.0878  0.0511  210 GLU   A OE1 
1602 O OE2 . GLU   A 211 ? 0.3973 0.4527 0.5535 -0.0405 0.1075  0.0400  210 GLU   A OE2 
1603 N N   . LEU   A 212 ? 0.3221 0.3377 0.5406 -0.0448 0.0318  0.0463  211 LEU   A N   
1604 C CA  . LEU   A 212 ? 0.3220 0.3222 0.5399 -0.0448 0.0182  0.0454  211 LEU   A CA  
1605 C C   . LEU   A 212 ? 0.3328 0.3208 0.5261 -0.0404 0.0153  0.0469  211 LEU   A C   
1606 O O   . LEU   A 212 ? 0.3514 0.3257 0.5455 -0.0398 0.0059  0.0466  211 LEU   A O   
1607 C CB  . LEU   A 212 ? 0.3041 0.2994 0.5449 -0.0541 0.0164  0.0528  211 LEU   A CB  
1608 C CG  . LEU   A 212 ? 0.3138 0.3231 0.5864 -0.0598 0.0187  0.0527  211 LEU   A CG  
1609 C CD1 . LEU   A 212 ? 0.3176 0.3204 0.6155 -0.0702 0.0155  0.0606  211 LEU   A CD1 
1610 C CD2 . LEU   A 212 ? 0.3169 0.3321 0.5971 -0.0540 0.0073  0.0404  211 LEU   A CD2 
1611 N N   . GLN   A 213 ? 0.3317 0.3243 0.5055 -0.0371 0.0226  0.0477  212 GLN   A N   
1612 C CA  . GLN   A 213 ? 0.3317 0.3159 0.4846 -0.0328 0.0192  0.0491  212 GLN   A CA  
1613 C C   . GLN   A 213 ? 0.3383 0.3316 0.4749 -0.0294 0.0263  0.0459  212 GLN   A C   
1614 O O   . GLN   A 213 ? 0.3474 0.3503 0.4852 -0.0321 0.0369  0.0462  212 GLN   A O   
1615 C CB  . GLN   A 213 ? 0.3530 0.3262 0.5006 -0.0381 0.0192  0.0621  212 GLN   A CB  
1616 C CG  . GLN   A 213 ? 0.4070 0.3851 0.5397 -0.0435 0.0313  0.0719  212 GLN   A CG  
1617 C CD  . GLN   A 213 ? 0.4894 0.4541 0.6130 -0.0485 0.0288  0.0869  212 GLN   A CD  
1618 O OE1 . GLN   A 213 ? 0.4842 0.4370 0.6225 -0.0503 0.0204  0.0913  212 GLN   A OE1 
1619 N NE2 . GLN   A 213 ? 0.5089 0.4737 0.6069 -0.0506 0.0347  0.0950  212 GLN   A NE2 
1620 N N   . PRO   A 214 ? 0.3283 0.3187 0.4518 -0.0235 0.0209  0.0420  213 PRO   A N   
1621 C CA  . PRO   A 214 ? 0.3351 0.3318 0.4441 -0.0214 0.0258  0.0389  213 PRO   A CA  
1622 C C   . PRO   A 214 ? 0.3614 0.3553 0.4519 -0.0257 0.0307  0.0470  213 PRO   A C   
1623 O O   . PRO   A 214 ? 0.3620 0.3475 0.4494 -0.0293 0.0280  0.0569  213 PRO   A O   
1624 C CB  . PRO   A 214 ? 0.3276 0.3217 0.4328 -0.0151 0.0173  0.0342  213 PRO   A CB  
1625 C CG  . PRO   A 214 ? 0.3336 0.3172 0.4426 -0.0147 0.0095  0.0390  213 PRO   A CG  
1626 C CD  . PRO   A 214 ? 0.3205 0.3020 0.4442 -0.0187 0.0106  0.0401  213 PRO   A CD  
1627 N N   . PRO   A 215 ? 0.3698 0.3690 0.4458 -0.0253 0.0369  0.0430  214 PRO   A N   
1628 C CA  . PRO   A 215 ? 0.3897 0.3854 0.4411 -0.0293 0.0408  0.0497  214 PRO   A CA  
1629 C C   . PRO   A 215 ? 0.3960 0.3816 0.4347 -0.0284 0.0282  0.0569  214 PRO   A C   
1630 O O   . PRO   A 215 ? 0.3857 0.3700 0.4319 -0.0231 0.0179  0.0526  214 PRO   A O   
1631 C CB  . PRO   A 215 ? 0.4066 0.4083 0.4456 -0.0273 0.0468  0.0394  214 PRO   A CB  
1632 C CG  . PRO   A 215 ? 0.3967 0.4061 0.4590 -0.0237 0.0497  0.0303  214 PRO   A CG  
1633 C CD  . PRO   A 215 ? 0.3674 0.3744 0.4480 -0.0216 0.0404  0.0323  214 PRO   A CD  
1634 N N   . LEU   A 216 ? 0.4097 0.3888 0.4305 -0.0334 0.0290  0.0686  215 LEU   A N   
1635 C CA  . LEU   A 216 ? 0.4388 0.4073 0.4474 -0.0326 0.0153  0.0778  215 LEU   A CA  
1636 C C   . LEU   A 216 ? 0.4332 0.3940 0.4650 -0.0291 0.0041  0.0815  215 LEU   A C   
1637 O O   . LEU   A 216 ? 0.4295 0.3830 0.4579 -0.0261 -0.0087 0.0868  215 LEU   A O   
1638 C CB  . LEU   A 216 ? 0.4623 0.4328 0.4558 -0.0286 0.0066  0.0706  215 LEU   A CB  
1639 C CG  . LEU   A 216 ? 0.5084 0.4831 0.4747 -0.0315 0.0149  0.0647  215 LEU   A CG  
1640 C CD1 . LEU   A 216 ? 0.5260 0.5006 0.4814 -0.0283 0.0025  0.0575  215 LEU   A CD1 
1641 C CD2 . LEU   A 216 ? 0.5421 0.5114 0.4797 -0.0384 0.0216  0.0771  215 LEU   A CD2 
1642 N N   . PHE   A 217 ? 0.4235 0.3856 0.4792 -0.0290 0.0080  0.0778  216 PHE   A N   
1643 C CA  . PHE   A 217 ? 0.4229 0.3767 0.5001 -0.0252 -0.0016 0.0775  216 PHE   A CA  
1644 C C   . PHE   A 217 ? 0.4399 0.3784 0.5162 -0.0266 -0.0112 0.0917  216 PHE   A C   
1645 O O   . PHE   A 217 ? 0.4391 0.3700 0.5296 -0.0205 -0.0219 0.0900  216 PHE   A O   
1646 C CB  . PHE   A 217 ? 0.4049 0.3610 0.5026 -0.0273 0.0037  0.0724  216 PHE   A CB  
1647 C CG  . PHE   A 217 ? 0.4051 0.3542 0.5221 -0.0219 -0.0052 0.0656  216 PHE   A CG  
1648 C CD1 . PHE   A 217 ? 0.4057 0.3583 0.5247 -0.0136 -0.0099 0.0553  216 PHE   A CD1 
1649 C CD2 . PHE   A 217 ? 0.4091 0.3484 0.5426 -0.0255 -0.0080 0.0685  216 PHE   A CD2 
1650 C CE1 . PHE   A 217 ? 0.4047 0.3517 0.5383 -0.0082 -0.0156 0.0471  216 PHE   A CE1 
1651 C CE2 . PHE   A 217 ? 0.4123 0.3441 0.5610 -0.0201 -0.0159 0.0591  216 PHE   A CE2 
1652 C CZ  . PHE   A 217 ? 0.4034 0.3394 0.5504 -0.0111 -0.0189 0.0481  216 PHE   A CZ  
1653 N N   . ASP   A 218 ? 0.4595 0.3933 0.5200 -0.0344 -0.0066 0.1059  217 ASP   A N   
1654 C CA  . ASP   A 218 ? 0.4944 0.4122 0.5511 -0.0375 -0.0150 0.1233  217 ASP   A CA  
1655 C C   . ASP   A 218 ? 0.5030 0.4165 0.5384 -0.0344 -0.0268 0.1304  217 ASP   A C   
1656 O O   . ASP   A 218 ? 0.4982 0.3975 0.5288 -0.0364 -0.0361 0.1468  217 ASP   A O   
1657 C CB  . ASP   A 218 ? 0.5490 0.4647 0.5954 -0.0488 -0.0032 0.1379  217 ASP   A CB  
1658 C CG  . ASP   A 218 ? 0.6881 0.6085 0.7599 -0.0531 0.0065  0.1330  217 ASP   A CG  
1659 O OD1 . ASP   A 218 ? 0.6952 0.6111 0.7931 -0.0487 -0.0011 0.1241  217 ASP   A OD1 
1660 O OD2 . ASP   A 218 ? 0.7451 0.6746 0.8115 -0.0607 0.0218  0.1369  217 ASP   A OD2 
1661 N N   . VAL   A 219 ? 0.4945 0.4193 0.5171 -0.0304 -0.0271 0.1196  218 VAL   A N   
1662 C CA  . VAL   A 219 ? 0.5137 0.4362 0.5182 -0.0277 -0.0402 0.1242  218 VAL   A CA  
1663 C C   . VAL   A 219 ? 0.4987 0.4208 0.5307 -0.0178 -0.0537 0.1173  218 VAL   A C   
1664 O O   . VAL   A 219 ? 0.4837 0.4139 0.5373 -0.0130 -0.0488 0.1029  218 VAL   A O   
1665 C CB  . VAL   A 219 ? 0.5348 0.4691 0.5148 -0.0291 -0.0339 0.1143  218 VAL   A CB  
1666 C CG1 . VAL   A 219 ? 0.5472 0.4799 0.5094 -0.0267 -0.0500 0.1170  218 VAL   A CG1 
1667 C CG2 . VAL   A 219 ? 0.5539 0.4902 0.5095 -0.0377 -0.0170 0.1187  218 VAL   A CG2 
1668 N N   . HIS   A 220 ? 0.4970 0.4104 0.5287 -0.0145 -0.0706 0.1280  219 HIS   A N   
1669 C CA  . HIS   A 220 ? 0.4970 0.4112 0.5576 -0.0045 -0.0834 0.1226  219 HIS   A CA  
1670 C C   . HIS   A 220 ? 0.5090 0.4407 0.5762 -0.0002 -0.0804 0.1056  219 HIS   A C   
1671 O O   . HIS   A 220 ? 0.5171 0.4559 0.5613 -0.0042 -0.0793 0.1032  219 HIS   A O   
1672 C CB  . HIS   A 220 ? 0.5123 0.4166 0.5676 -0.0025 -0.1033 0.1382  219 HIS   A CB  
1673 C CG  . HIS   A 220 ? 0.5313 0.4360 0.6225 0.0085  -0.1166 0.1344  219 HIS   A CG  
1674 N ND1 . HIS   A 220 ? 0.5465 0.4676 0.6535 0.0148  -0.1195 0.1210  219 HIS   A ND1 
1675 C CD2 . HIS   A 220 ? 0.5456 0.4363 0.6607 0.0142  -0.1275 0.1431  219 HIS   A CD2 
1676 C CE1 . HIS   A 220 ? 0.5482 0.4668 0.6889 0.0244  -0.1303 0.1213  219 HIS   A CE1 
1677 N NE2 . HIS   A 220 ? 0.5524 0.4523 0.6995 0.0250  -0.1358 0.1336  219 HIS   A NE2 
1678 N N   . PRO   A 221 ? 0.5008 0.4388 0.5974 0.0069  -0.0770 0.0931  220 PRO   A N   
1679 C CA  . PRO   A 221 ? 0.4956 0.4502 0.5999 0.0099  -0.0719 0.0786  220 PRO   A CA  
1680 C C   . PRO   A 221 ? 0.4931 0.4558 0.5923 0.0103  -0.0831 0.0789  220 PRO   A C   
1681 O O   . PRO   A 221 ? 0.4743 0.4467 0.5636 0.0072  -0.0779 0.0710  220 PRO   A O   
1682 C CB  . PRO   A 221 ? 0.4998 0.4573 0.6363 0.0186  -0.0698 0.0693  220 PRO   A CB  
1683 C CG  . PRO   A 221 ? 0.5087 0.4499 0.6570 0.0217  -0.0779 0.0783  220 PRO   A CG  
1684 C CD  . PRO   A 221 ? 0.4935 0.4229 0.6164 0.0124  -0.0771 0.0914  220 PRO   A CD  
1685 N N   . LEU   A 222 ? 0.5086 0.4662 0.6153 0.0138  -0.1000 0.0885  221 LEU   A N   
1686 C CA  . LEU   A 222 ? 0.5272 0.4921 0.6309 0.0138  -0.1145 0.0895  221 LEU   A CA  
1687 C C   . LEU   A 222 ? 0.5506 0.5110 0.6115 0.0047  -0.1165 0.0942  221 LEU   A C   
1688 O O   . LEU   A 222 ? 0.5634 0.5320 0.6166 0.0026  -0.1224 0.0879  221 LEU   A O   
1689 C CB  . LEU   A 222 ? 0.5318 0.4928 0.6585 0.0208  -0.1341 0.0991  221 LEU   A CB  
1690 C CG  . LEU   A 222 ? 0.5579 0.5228 0.7276 0.0310  -0.1306 0.0926  221 LEU   A CG  
1691 C CD1 . LEU   A 222 ? 0.5579 0.5193 0.7538 0.0388  -0.1504 0.1019  221 LEU   A CD1 
1692 C CD2 . LEU   A 222 ? 0.5695 0.5540 0.7612 0.0341  -0.1189 0.0762  221 LEU   A CD2 
1693 N N   . ARG   A 223 ? 0.5613 0.5094 0.5952 -0.0009 -0.1103 0.1040  222 ARG   A N   
1694 C CA  . ARG   A 223 ? 0.5839 0.5287 0.5748 -0.0093 -0.1075 0.1068  222 ARG   A CA  
1695 C C   . ARG   A 223 ? 0.5653 0.5205 0.5512 -0.0120 -0.0901 0.0904  222 ARG   A C   
1696 O O   . ARG   A 223 ? 0.5817 0.5401 0.5451 -0.0155 -0.0921 0.0840  222 ARG   A O   
1697 C CB  . ARG   A 223 ? 0.6383 0.5687 0.6041 -0.0151 -0.1029 0.1231  222 ARG   A CB  
1698 C CG  . ARG   A 223 ? 0.7392 0.6674 0.6575 -0.0235 -0.0966 0.1254  222 ARG   A CG  
1699 C CD  . ARG   A 223 ? 0.8372 0.7505 0.7256 -0.0296 -0.0989 0.1469  222 ARG   A CD  
1700 N NE  . ARG   A 223 ? 0.9305 0.8441 0.8004 -0.0368 -0.0756 0.1475  222 ARG   A NE  
1701 C CZ  . ARG   A 223 ? 0.9993 0.9159 0.8306 -0.0427 -0.0646 0.1434  222 ARG   A CZ  
1702 N NH1 . ARG   A 223 ? 1.0131 0.9303 0.8155 -0.0429 -0.0764 0.1380  222 ARG   A NH1 
1703 N NH2 . ARG   A 223 ? 1.0076 0.9268 0.8303 -0.0483 -0.0418 0.1436  222 ARG   A NH2 
1704 N N   . VAL   A 224 ? 0.5213 0.4812 0.5293 -0.0098 -0.0751 0.0830  223 VAL   A N   
1705 C CA  . VAL   A 224 ? 0.4964 0.4654 0.5037 -0.0116 -0.0599 0.0691  223 VAL   A CA  
1706 C C   . VAL   A 224 ? 0.4975 0.4766 0.5170 -0.0092 -0.0663 0.0578  223 VAL   A C   
1707 O O   . VAL   A 224 ? 0.4886 0.4712 0.4944 -0.0125 -0.0613 0.0488  223 VAL   A O   
1708 C CB  . VAL   A 224 ? 0.4715 0.4428 0.5004 -0.0096 -0.0461 0.0649  223 VAL   A CB  
1709 C CG1 . VAL   A 224 ? 0.4637 0.4446 0.4967 -0.0100 -0.0341 0.0516  223 VAL   A CG1 
1710 C CG2 . VAL   A 224 ? 0.4739 0.4361 0.4923 -0.0141 -0.0385 0.0748  223 VAL   A CG2 
1711 N N   . LEU   A 225 ? 0.5009 0.4850 0.5489 -0.0034 -0.0769 0.0581  224 LEU   A N   
1712 C CA  . LEU   A 225 ? 0.5128 0.5081 0.5785 -0.0019 -0.0832 0.0493  224 LEU   A CA  
1713 C C   . LEU   A 225 ? 0.5509 0.5438 0.5923 -0.0067 -0.0966 0.0491  224 LEU   A C   
1714 O O   . LEU   A 225 ? 0.5435 0.5412 0.5824 -0.0097 -0.0951 0.0386  224 LEU   A O   
1715 C CB  . LEU   A 225 ? 0.4893 0.4914 0.5914 0.0052  -0.0921 0.0515  224 LEU   A CB  
1716 C CG  . LEU   A 225 ? 0.4807 0.4883 0.6087 0.0106  -0.0786 0.0466  224 LEU   A CG  
1717 C CD1 . LEU   A 225 ? 0.4746 0.4880 0.6359 0.0184  -0.0863 0.0483  224 LEU   A CD1 
1718 C CD2 . LEU   A 225 ? 0.4731 0.4907 0.6076 0.0087  -0.0661 0.0360  224 LEU   A CD2 
1719 N N   . PHE   A 226 ? 0.5897 0.5732 0.6105 -0.0079 -0.1098 0.0607  225 PHE   A N   
1720 C CA  . PHE   A 226 ? 0.6332 0.6122 0.6232 -0.0127 -0.1246 0.0613  225 PHE   A CA  
1721 C C   . PHE   A 226 ? 0.6533 0.6288 0.6090 -0.0186 -0.1116 0.0520  225 PHE   A C   
1722 O O   . PHE   A 226 ? 0.6627 0.6409 0.6114 -0.0213 -0.1170 0.0404  225 PHE   A O   
1723 C CB  . PHE   A 226 ? 0.6639 0.6312 0.6326 -0.0131 -0.1393 0.0785  225 PHE   A CB  
1724 C CG  . PHE   A 226 ? 0.7156 0.6768 0.6453 -0.0183 -0.1562 0.0804  225 PHE   A CG  
1725 C CD1 . PHE   A 226 ? 0.7564 0.7087 0.6371 -0.0248 -0.1469 0.0803  225 PHE   A CD1 
1726 C CD2 . PHE   A 226 ? 0.7322 0.6968 0.6741 -0.0166 -0.1816 0.0821  225 PHE   A CD2 
1727 C CE1 . PHE   A 226 ? 0.7905 0.7361 0.6296 -0.0295 -0.1624 0.0807  225 PHE   A CE1 
1728 C CE2 . PHE   A 226 ? 0.7654 0.7232 0.6681 -0.0217 -0.1999 0.0836  225 PHE   A CE2 
1729 C CZ  . PHE   A 226 ? 0.7886 0.7361 0.6373 -0.0281 -0.1902 0.0826  225 PHE   A CZ  
1730 N N   . LEU   A 227 ? 0.6581 0.6279 0.5958 -0.0206 -0.0943 0.0561  226 LEU   A N   
1731 C CA  . LEU   A 227 ? 0.6810 0.6485 0.5885 -0.0253 -0.0795 0.0475  226 LEU   A CA  
1732 C C   . LEU   A 227 ? 0.6854 0.6608 0.6116 -0.0244 -0.0705 0.0305  226 LEU   A C   
1733 O O   . LEU   A 227 ? 0.6831 0.6565 0.5884 -0.0273 -0.0687 0.0191  226 LEU   A O   
1734 C CB  . LEU   A 227 ? 0.6880 0.6513 0.5840 -0.0273 -0.0612 0.0557  226 LEU   A CB  
1735 C CG  . LEU   A 227 ? 0.7193 0.6726 0.5980 -0.0294 -0.0677 0.0752  226 LEU   A CG  
1736 C CD1 . LEU   A 227 ? 0.7311 0.6821 0.6054 -0.0327 -0.0478 0.0824  226 LEU   A CD1 
1737 C CD2 . LEU   A 227 ? 0.7423 0.6879 0.5780 -0.0336 -0.0815 0.0805  226 LEU   A CD2 
1738 N N   . MET   A 228 ? 0.6945 0.6776 0.6588 -0.0202 -0.0652 0.0289  227 MET   A N   
1739 C CA  . MET   A 228 ? 0.7135 0.7033 0.6977 -0.0194 -0.0562 0.0161  227 MET   A CA  
1740 C C   . MET   A 228 ? 0.7363 0.7290 0.7278 -0.0208 -0.0688 0.0066  227 MET   A C   
1741 O O   . MET   A 228 ? 0.7443 0.7371 0.7371 -0.0224 -0.0624 -0.0051 227 MET   A O   
1742 C CB  . MET   A 228 ? 0.7092 0.7059 0.7271 -0.0150 -0.0480 0.0183  227 MET   A CB  
1743 C CG  . MET   A 228 ? 0.7444 0.7394 0.7587 -0.0150 -0.0314 0.0196  227 MET   A CG  
1744 S SD  . MET   A 228 ? 0.7606 0.7634 0.8081 -0.0108 -0.0217 0.0165  227 MET   A SD  
1745 C CE  . MET   A 228 ? 0.5793 0.5818 0.6412 -0.0068 -0.0288 0.0256  227 MET   A CE  
1746 N N   . THR   A 229 ? 0.7514 0.7459 0.7502 -0.0205 -0.0877 0.0115  228 THR   A N   
1747 C CA  . THR   A 229 ? 0.7754 0.7735 0.7850 -0.0229 -0.1020 0.0028  228 THR   A CA  
1748 C C   . THR   A 229 ? 0.8129 0.8014 0.7826 -0.0278 -0.1152 -0.0023 228 THR   A C   
1749 O O   . THR   A 229 ? 0.8151 0.8050 0.7894 -0.0300 -0.1353 -0.0052 228 THR   A O   
1750 C CB  . THR   A 229 ? 0.7926 0.8014 0.8407 -0.0197 -0.1146 0.0089  228 THR   A CB  
1751 O OG1 . THR   A 229 ? 0.8163 0.8219 0.8547 -0.0180 -0.1301 0.0204  228 THR   A OG1 
1752 C CG2 . THR   A 229 ? 0.7901 0.8076 0.8707 -0.0149 -0.0996 0.0119  228 THR   A CG2 
1753 N N   . LYS   A 230 ? 0.8340 0.8134 0.7645 -0.0296 -0.1036 -0.0038 229 LYS   A N   
1754 C CA  . LYS   A 230 ? 0.8582 0.8276 0.7437 -0.0340 -0.1121 -0.0103 229 LYS   A CA  
1755 C C   . LYS   A 230 ? 0.8714 0.8374 0.7491 -0.0357 -0.0996 -0.0292 229 LYS   A C   
1756 O O   . LYS   A 230 ? 0.8716 0.8406 0.7651 -0.0334 -0.0797 -0.0323 229 LYS   A O   
1757 C CB  . LYS   A 230 ? 0.8916 0.8533 0.7360 -0.0352 -0.1064 0.0017  229 LYS   A CB  
1758 C CG  . LYS   A 230 ? 0.9472 0.9057 0.7811 -0.0355 -0.1282 0.0177  229 LYS   A CG  
1759 C CD  . LYS   A 230 ? 1.0246 0.9736 0.8156 -0.0379 -0.1215 0.0318  229 LYS   A CD  
1760 C CE  . LYS   A 230 ? 1.0827 1.0232 0.8186 -0.0429 -0.1157 0.0223  229 LYS   A CE  
1761 N NZ  . LYS   A 230 ? 1.1046 1.0462 0.8313 -0.0433 -0.0854 0.0174  229 LYS   A NZ  
1762 N N   . SER   A 231 ? 0.8805 0.8396 0.7354 -0.0395 -0.1127 -0.0425 230 SER   A N   
1763 C CA  . SER   A 231 ? 0.8889 0.8420 0.7369 -0.0407 -0.1030 -0.0629 230 SER   A CA  
1764 C C   . SER   A 231 ? 0.8824 0.8314 0.7012 -0.0391 -0.0782 -0.0663 230 SER   A C   
1765 O O   . SER   A 231 ? 0.8821 0.8313 0.7161 -0.0369 -0.0616 -0.0771 230 SER   A O   
1766 C CB  . SER   A 231 ? 0.9312 0.8754 0.7544 -0.0453 -0.1238 -0.0775 230 SER   A CB  
1767 O OG  . SER   A 231 ? 0.9617 0.9118 0.8138 -0.0472 -0.1484 -0.0723 230 SER   A OG  
1768 N N   . GLY   A 232 ? 0.8727 0.8187 0.6533 -0.0403 -0.0756 -0.0553 231 GLY   A N   
1769 C CA  . GLY   A 232 ? 0.8648 0.8093 0.6188 -0.0397 -0.0511 -0.0563 231 GLY   A CA  
1770 C C   . GLY   A 232 ? 0.8294 0.7825 0.6108 -0.0369 -0.0330 -0.0423 231 GLY   A C   
1771 O O   . GLY   A 232 ? 0.8437 0.7972 0.6047 -0.0374 -0.0142 -0.0384 231 GLY   A O   
1772 N N   . TYR   A 233 ? 0.7841 0.7446 0.6114 -0.0342 -0.0380 -0.0349 232 TYR   A N   
1773 C CA  . TYR   A 233 ? 0.7519 0.7195 0.6047 -0.0315 -0.0228 -0.0234 232 TYR   A CA  
1774 C C   . TYR   A 233 ? 0.7293 0.6996 0.5915 -0.0295 -0.0018 -0.0346 232 TYR   A C   
1775 O O   . TYR   A 233 ? 0.7321 0.7018 0.6105 -0.0278 -0.0018 -0.0488 232 TYR   A O   
1776 C CB  . TYR   A 233 ? 0.7319 0.7063 0.6285 -0.0285 -0.0313 -0.0161 232 TYR   A CB  
1777 C CG  . TYR   A 233 ? 0.7328 0.7125 0.6501 -0.0262 -0.0180 -0.0054 232 TYR   A CG  
1778 C CD1 . TYR   A 233 ? 0.7466 0.7240 0.6499 -0.0277 -0.0155 0.0091  232 TYR   A CD1 
1779 C CD2 . TYR   A 233 ? 0.7227 0.7086 0.6730 -0.0231 -0.0092 -0.0095 232 TYR   A CD2 
1780 C CE1 . TYR   A 233 ? 0.7448 0.7257 0.6684 -0.0263 -0.0051 0.0174  232 TYR   A CE1 
1781 C CE2 . TYR   A 233 ? 0.7188 0.7087 0.6861 -0.0213 0.0005  -0.0011 232 TYR   A CE2 
1782 C CZ  . TYR   A 233 ? 0.7410 0.7285 0.6960 -0.0231 0.0023  0.0115  232 TYR   A CZ  
1783 O OH  . TYR   A 233 ? 0.7461 0.7364 0.7193 -0.0221 0.0103  0.0188  232 TYR   A OH  
1784 N N   . GLN   A 234 ? 0.7093 0.6824 0.5635 -0.0298 0.0155  -0.0279 233 GLN   A N   
1785 C CA  . GLN   A 234 ? 0.6896 0.6676 0.5587 -0.0272 0.0357  -0.0370 233 GLN   A CA  
1786 C C   . GLN   A 234 ? 0.6380 0.6237 0.5467 -0.0247 0.0392  -0.0270 233 GLN   A C   
1787 O O   . GLN   A 234 ? 0.6377 0.6250 0.5481 -0.0264 0.0379  -0.0118 233 GLN   A O   
1788 C CB  . GLN   A 234 ? 0.7402 0.7185 0.5774 -0.0294 0.0543  -0.0376 233 GLN   A CB  
1789 C CG  . GLN   A 234 ? 0.8355 0.8050 0.6272 -0.0314 0.0520  -0.0508 233 GLN   A CG  
1790 C CD  . GLN   A 234 ? 0.9264 0.8909 0.7274 -0.0282 0.0465  -0.0727 233 GLN   A CD  
1791 O OE1 . GLN   A 234 ? 0.9688 0.9257 0.7582 -0.0299 0.0268  -0.0786 233 GLN   A OE1 
1792 N NE2 . GLN   A 234 ? 0.9194 0.8878 0.7457 -0.0237 0.0622  -0.0845 233 GLN   A NE2 
1793 N N   . PRO   A 235 ? 0.5880 0.5770 0.5283 -0.0209 0.0415  -0.0350 234 PRO   A N   
1794 C CA  . PRO   A 235 ? 0.5472 0.5430 0.5207 -0.0187 0.0442  -0.0264 234 PRO   A CA  
1795 C C   . PRO   A 235 ? 0.5253 0.5267 0.5003 -0.0198 0.0590  -0.0189 234 PRO   A C   
1796 O O   . PRO   A 235 ? 0.5294 0.5320 0.4888 -0.0209 0.0727  -0.0239 234 PRO   A O   
1797 C CB  . PRO   A 235 ? 0.5459 0.5428 0.5450 -0.0149 0.0469  -0.0374 234 PRO   A CB  
1798 C CG  . PRO   A 235 ? 0.5691 0.5583 0.5541 -0.0155 0.0397  -0.0504 234 PRO   A CG  
1799 C CD  . PRO   A 235 ? 0.5743 0.5595 0.5201 -0.0187 0.0421  -0.0523 234 PRO   A CD  
1800 N N   . PRO   A 236 ? 0.5000 0.5049 0.4942 -0.0199 0.0569  -0.0075 235 PRO   A N   
1801 C CA  . PRO   A 236 ? 0.4891 0.4995 0.4901 -0.0221 0.0693  0.0002  235 PRO   A CA  
1802 C C   . PRO   A 236 ? 0.4730 0.4917 0.4933 -0.0199 0.0844  -0.0077 235 PRO   A C   
1803 O O   . PRO   A 236 ? 0.4687 0.4882 0.5029 -0.0155 0.0844  -0.0184 235 PRO   A O   
1804 C CB  . PRO   A 236 ? 0.4925 0.5032 0.5153 -0.0216 0.0601  0.0098  235 PRO   A CB  
1805 C CG  . PRO   A 236 ? 0.4959 0.5009 0.5128 -0.0201 0.0449  0.0106  235 PRO   A CG  
1806 C CD  . PRO   A 236 ? 0.4765 0.4807 0.4878 -0.0182 0.0434  -0.0016 235 PRO   A CD  
1807 N N   . ARG   A 237 ? 0.4633 0.4884 0.4880 -0.0230 0.0972  -0.0013 236 ARG   A N   
1808 C CA  . ARG   A 237 ? 0.4509 0.4868 0.5004 -0.0210 0.1118  -0.0068 236 ARG   A CA  
1809 C C   . ARG   A 237 ? 0.4304 0.4733 0.5017 -0.0250 0.1153  0.0054  236 ARG   A C   
1810 O O   . ARG   A 237 ? 0.4326 0.4706 0.4920 -0.0303 0.1111  0.0176  236 ARG   A O   
1811 C CB  . ARG   A 237 ? 0.4893 0.5283 0.5182 -0.0216 0.1303  -0.0151 236 ARG   A CB  
1812 C CG  . ARG   A 237 ? 0.5655 0.5958 0.5682 -0.0186 0.1272  -0.0291 236 ARG   A CG  
1813 C CD  . ARG   A 237 ? 0.6619 0.6936 0.6337 -0.0206 0.1453  -0.0355 236 ARG   A CD  
1814 N NE  . ARG   A 237 ? 0.7691 0.7925 0.7207 -0.0167 0.1436  -0.0538 236 ARG   A NE  
1815 C CZ  . ARG   A 237 ? 0.8386 0.8604 0.7577 -0.0171 0.1575  -0.0648 236 ARG   A CZ  
1816 N NH1 . ARG   A 237 ? 0.8450 0.8572 0.7477 -0.0135 0.1532  -0.0832 236 ARG   A NH1 
1817 N NH2 . ARG   A 237 ? 0.8634 0.8929 0.7660 -0.0212 0.1764  -0.0578 236 ARG   A NH2 
1818 N N   . LEU   A 238 ? 0.4042 0.4581 0.5093 -0.0228 0.1225  0.0024  237 LEU   A N   
1819 C CA  . LEU   A 238 ? 0.3978 0.4602 0.5285 -0.0274 0.1265  0.0123  237 LEU   A CA  
1820 C C   . LEU   A 238 ? 0.4505 0.5169 0.5648 -0.0345 0.1439  0.0199  237 LEU   A C   
1821 O O   . LEU   A 238 ? 0.4450 0.5141 0.5400 -0.0336 0.1587  0.0128  237 LEU   A O   
1822 C CB  . LEU   A 238 ? 0.3563 0.4315 0.5276 -0.0231 0.1308  0.0061  237 LEU   A CB  
1823 C CG  . LEU   A 238 ? 0.3443 0.4155 0.5320 -0.0173 0.1131  0.0025  237 LEU   A CG  
1824 C CD1 . LEU   A 238 ? 0.3353 0.4157 0.5533 -0.0108 0.1178  -0.0063 237 LEU   A CD1 
1825 C CD2 . LEU   A 238 ? 0.3196 0.3883 0.5192 -0.0208 0.0986  0.0119  237 LEU   A CD2 
1826 N N   . LYS   A 239 ? 0.4910 0.5562 0.6107 -0.0417 0.1419  0.0341  238 LYS   A N   
1827 C CA  . LYS   A 239 ? 0.5488 0.6159 0.6521 -0.0499 0.1570  0.0454  238 LYS   A CA  
1828 C C   . LYS   A 239 ? 0.5832 0.6688 0.7127 -0.0525 0.1797  0.0446  238 LYS   A C   
1829 O O   . LYS   A 239 ? 0.5975 0.6874 0.7052 -0.0564 0.1990  0.0474  238 LYS   A O   
1830 C CB  . LYS   A 239 ? 0.6058 0.6625 0.7086 -0.0570 0.1454  0.0620  238 LYS   A CB  
1831 C CG  . LYS   A 239 ? 0.7128 0.7661 0.7884 -0.0658 0.1577  0.0768  238 LYS   A CG  
1832 C CD  . LYS   A 239 ? 0.7811 0.8335 0.8807 -0.0753 0.1577  0.0937  238 LYS   A CD  
1833 C CE  . LYS   A 239 ? 0.8467 0.8971 0.9197 -0.0848 0.1731  0.1102  238 LYS   A CE  
1834 N NZ  . LYS   A 239 ? 0.8882 0.9283 0.9747 -0.0939 0.1653  0.1294  238 LYS   A NZ  
1835 N N   . GLU   A 240 ? 0.5957 0.6933 0.7712 -0.0498 0.1782  0.0402  239 GLU   A N   
1836 C CA  . GLU   A 240 ? 0.5975 0.7159 0.8073 -0.0516 0.1993  0.0393  239 GLU   A CA  
1837 C C   . GLU   A 240 ? 0.6088 0.7383 0.8401 -0.0414 0.2063  0.0222  239 GLU   A C   
1838 O O   . GLU   A 240 ? 0.6012 0.7387 0.8742 -0.0374 0.1971  0.0188  239 GLU   A O   
1839 C CB  . GLU   A 240 ? 0.6280 0.7538 0.8819 -0.0580 0.1924  0.0497  239 GLU   A CB  
1840 C CG  . GLU   A 240 ? 0.7285 0.8428 0.9685 -0.0685 0.1868  0.0668  239 GLU   A CG  
1841 C CD  . GLU   A 240 ? 0.8001 0.9244 1.0859 -0.0773 0.1873  0.0772  239 GLU   A CD  
1842 O OE1 . GLU   A 240 ? 0.7918 0.9238 1.1173 -0.0742 0.1755  0.0710  239 GLU   A OE1 
1843 O OE2 . GLU   A 240 ? 0.8478 0.9717 1.1298 -0.0879 0.1983  0.0923  239 GLU   A OE2 
1844 N N   . LYS   A 241 ? 0.6279 0.7580 0.8326 -0.0372 0.2226  0.0114  240 LYS   A N   
1845 C CA  . LYS   A 241 ? 0.6243 0.7614 0.8468 -0.0266 0.2295  -0.0067 240 LYS   A CA  
1846 C C   . LYS   A 241 ? 0.5986 0.7582 0.8806 -0.0238 0.2406  -0.0091 240 LYS   A C   
1847 O O   . LYS   A 241 ? 0.5744 0.7366 0.8863 -0.0147 0.2324  -0.0192 240 LYS   A O   
1848 C CB  . LYS   A 241 ? 0.6659 0.7993 0.8473 -0.0238 0.2478  -0.0187 240 LYS   A CB  
1849 C CG  . LYS   A 241 ? 0.7264 0.8593 0.9196 -0.0119 0.2494  -0.0394 240 LYS   A CG  
1850 C CD  . LYS   A 241 ? 0.8187 0.9480 0.9732 -0.0090 0.2682  -0.0543 240 LYS   A CD  
1851 C CE  . LYS   A 241 ? 0.8876 1.0135 1.0586 0.0030  0.2673  -0.0754 240 LYS   A CE  
1852 N NZ  . LYS   A 241 ? 0.9312 1.0396 1.0998 0.0060  0.2385  -0.0761 240 LYS   A NZ  
1853 N N   . GLY   A 242 ? 0.5877 0.7630 0.8874 -0.0321 0.2586  0.0014  241 GLY   A N   
1854 C CA  . GLY   A 242 ? 0.5598 0.7600 0.9194 -0.0318 0.2716  0.0016  241 GLY   A CA  
1855 C C   . GLY   A 242 ? 0.5257 0.7318 0.9328 -0.0355 0.2513  0.0115  241 GLY   A C   
1856 O O   . GLY   A 242 ? 0.5245 0.7503 0.9756 -0.0415 0.2615  0.0191  241 GLY   A O   
1857 N N   . LYS   A 243 ? 0.4972 0.6871 0.8967 -0.0317 0.2229  0.0104  242 LYS   A N   
1858 C CA  . LYS   A 243 ? 0.4612 0.6507 0.8937 -0.0332 0.1978  0.0164  242 LYS   A CA  
1859 C C   . LYS   A 243 ? 0.4259 0.6054 0.8579 -0.0220 0.1776  0.0064  242 LYS   A C   
1860 O O   . LYS   A 243 ? 0.4309 0.6184 0.9033 -0.0179 0.1645  0.0052  242 LYS   A O   
1861 C CB  . LYS   A 243 ? 0.5008 0.6741 0.9068 -0.0430 0.1828  0.0291  242 LYS   A CB  
1862 C CG  . LYS   A 243 ? 0.5474 0.7140 0.9726 -0.0431 0.1540  0.0316  242 LYS   A CG  
1863 C CD  . LYS   A 243 ? 0.6039 0.7551 1.0094 -0.0524 0.1413  0.0423  242 LYS   A CD  
1864 C CE  . LYS   A 243 ? 0.6231 0.7718 1.0557 -0.0536 0.1162  0.0432  242 LYS   A CE  
1865 N NZ  . LYS   A 243 ? 0.6421 0.7756 1.0611 -0.0621 0.1045  0.0515  242 LYS   A NZ  
1866 N N   . TRP   A 244 ? 0.3902 0.5528 0.7782 -0.0175 0.1755  0.0000  243 TRP   A N   
1867 C CA  . TRP   A 244 ? 0.3538 0.5045 0.7367 -0.0087 0.1573  -0.0071 243 TRP   A CA  
1868 C C   . TRP   A 244 ? 0.3396 0.4952 0.7361 0.0014  0.1686  -0.0205 243 TRP   A C   
1869 O O   . TRP   A 244 ? 0.3579 0.5193 0.7449 0.0022  0.1917  -0.0277 243 TRP   A O   
1870 C CB  . TRP   A 244 ? 0.3461 0.4754 0.6780 -0.0103 0.1462  -0.0057 243 TRP   A CB  
1871 C CG  . TRP   A 244 ? 0.3152 0.4378 0.6324 -0.0194 0.1367  0.0064  243 TRP   A CG  
1872 C CD1 . TRP   A 244 ? 0.3163 0.4319 0.6006 -0.0263 0.1440  0.0126  243 TRP   A CD1 
1873 C CD2 . TRP   A 244 ? 0.2953 0.4175 0.6331 -0.0226 0.1182  0.0134  243 TRP   A CD2 
1874 N NE1 . TRP   A 244 ? 0.3199 0.4295 0.6052 -0.0329 0.1310  0.0230  243 TRP   A NE1 
1875 C CE2 . TRP   A 244 ? 0.3113 0.4248 0.6285 -0.0309 0.1156  0.0224  243 TRP   A CE2 
1876 C CE3 . TRP   A 244 ? 0.2810 0.4078 0.6504 -0.0190 0.1022  0.0126  243 TRP   A CE3 
1877 C CZ2 . TRP   A 244 ? 0.3201 0.4288 0.6485 -0.0354 0.0984  0.0285  243 TRP   A CZ2 
1878 C CZ3 . TRP   A 244 ? 0.2869 0.4089 0.6618 -0.0237 0.0843  0.0186  243 TRP   A CZ3 
1879 C CH2 . TRP   A 244 ? 0.3043 0.4175 0.6603 -0.0318 0.0832  0.0255  243 TRP   A CH2 
1880 N N   . SER   A 245 ? 0.3154 0.4685 0.7353 0.0093  0.1531  -0.0240 244 SER   A N   
1881 C CA  . SER   A 245 ? 0.3140 0.4703 0.7540 0.0200  0.1624  -0.0370 244 SER   A CA  
1882 C C   . SER   A 245 ? 0.3269 0.4651 0.7241 0.0234  0.1659  -0.0473 244 SER   A C   
1883 O O   . SER   A 245 ? 0.3484 0.4714 0.7046 0.0184  0.1556  -0.0429 244 SER   A O   
1884 C CB  . SER   A 245 ? 0.3264 0.4837 0.8055 0.0274  0.1427  -0.0354 244 SER   A CB  
1885 O OG  . SER   A 245 ? 0.3679 0.5049 0.8177 0.0282  0.1226  -0.0325 244 SER   A OG  
1886 N N   . ALA   A 246 ? 0.3126 0.4522 0.7242 0.0324  0.1783  -0.0618 245 ALA   A N   
1887 C CA  . ALA   A 246 ? 0.3264 0.4480 0.7062 0.0368  0.1794  -0.0745 245 ALA   A CA  
1888 C C   . ALA   A 246 ? 0.3343 0.4382 0.7045 0.0376  0.1541  -0.0689 245 ALA   A C   
1889 O O   . ALA   A 246 ? 0.3516 0.4397 0.6827 0.0350  0.1493  -0.0718 245 ALA   A O   
1890 C CB  . ALA   A 246 ? 0.3044 0.4306 0.7124 0.0477  0.1951  -0.0919 245 ALA   A CB  
1891 N N   . ALA   A 247 ? 0.3067 0.4137 0.7111 0.0406  0.1373  -0.0600 246 ALA   A N   
1892 C CA  . ALA   A 247 ? 0.2986 0.3897 0.6922 0.0406  0.1144  -0.0524 246 ALA   A CA  
1893 C C   . ALA   A 247 ? 0.2976 0.3817 0.6506 0.0312  0.1055  -0.0427 246 ALA   A C   
1894 O O   . ALA   A 247 ? 0.3124 0.3815 0.6388 0.0299  0.0959  -0.0418 246 ALA   A O   
1895 C CB  . ALA   A 247 ? 0.2793 0.3766 0.7136 0.0447  0.0986  -0.0432 246 ALA   A CB  
1896 N N   . PHE   A 248 ? 0.2662 0.3611 0.6186 0.0247  0.1081  -0.0349 247 PHE   A N   
1897 C CA  . PHE   A 248 ? 0.2708 0.3585 0.5892 0.0168  0.0999  -0.0264 247 PHE   A CA  
1898 C C   . PHE   A 248 ? 0.2939 0.3727 0.5720 0.0137  0.1093  -0.0322 247 PHE   A C   
1899 O O   . PHE   A 248 ? 0.3088 0.3754 0.5601 0.0117  0.0990  -0.0298 247 PHE   A O   
1900 C CB  . PHE   A 248 ? 0.2559 0.3550 0.5872 0.0106  0.0990  -0.0173 247 PHE   A CB  
1901 C CG  . PHE   A 248 ? 0.2712 0.3622 0.5757 0.0036  0.0880  -0.0086 247 PHE   A CG  
1902 C CD1 . PHE   A 248 ? 0.2933 0.3701 0.5705 0.0042  0.0761  -0.0075 247 PHE   A CD1 
1903 C CD2 . PHE   A 248 ? 0.2754 0.3733 0.5868 -0.0032 0.0892  -0.0016 247 PHE   A CD2 
1904 C CE1 . PHE   A 248 ? 0.3138 0.3839 0.5693 -0.0009 0.0675  -0.0011 247 PHE   A CE1 
1905 C CE2 . PHE   A 248 ? 0.2894 0.3782 0.5794 -0.0086 0.0785  0.0050  247 PHE   A CE2 
1906 C CZ  . PHE   A 248 ? 0.3077 0.3829 0.5695 -0.0068 0.0684  0.0046  247 PHE   A CZ  
1907 N N   . HIS   A 249 ? 0.3034 0.3880 0.5774 0.0140  0.1286  -0.0405 248 HIS   A N   
1908 C CA  . HIS   A 249 ? 0.3330 0.4085 0.5659 0.0114  0.1363  -0.0469 248 HIS   A CA  
1909 C C   . HIS   A 249 ? 0.3357 0.3958 0.5552 0.0154  0.1264  -0.0552 248 HIS   A C   
1910 O O   . HIS   A 249 ? 0.3335 0.3832 0.5202 0.0116  0.1199  -0.0546 248 HIS   A O   
1911 C CB  . HIS   A 249 ? 0.3457 0.4304 0.5761 0.0123  0.1604  -0.0565 248 HIS   A CB  
1912 C CG  . HIS   A 249 ? 0.4026 0.4987 0.6297 0.0047  0.1712  -0.0459 248 HIS   A CG  
1913 N ND1 . HIS   A 249 ? 0.4222 0.5367 0.6859 0.0050  0.1853  -0.0445 248 HIS   A ND1 
1914 C CD2 . HIS   A 249 ? 0.4238 0.5149 0.6204 -0.0036 0.1677  -0.0349 248 HIS   A CD2 
1915 C CE1 . HIS   A 249 ? 0.4346 0.5542 0.6874 -0.0040 0.1910  -0.0324 248 HIS   A CE1 
1916 N NE2 . HIS   A 249 ? 0.4523 0.5570 0.6642 -0.0091 0.1801  -0.0261 248 HIS   A NE2 
1917 N N   . ASN   A 250 ? 0.3215 0.3802 0.5696 0.0229  0.1248  -0.0625 249 ASN   A N   
1918 C CA  . ASN   A 250 ? 0.3246 0.3680 0.5662 0.0261  0.1157  -0.0698 249 ASN   A CA  
1919 C C   . ASN   A 250 ? 0.3249 0.3606 0.5600 0.0228  0.0965  -0.0576 249 ASN   A C   
1920 O O   . ASN   A 250 ? 0.3281 0.3525 0.5416 0.0204  0.0895  -0.0596 249 ASN   A O   
1921 C CB  . ASN   A 250 ? 0.3199 0.3624 0.5976 0.0352  0.1188  -0.0793 249 ASN   A CB  
1922 C CG  . ASN   A 250 ? 0.3748 0.3993 0.6475 0.0375  0.1091  -0.0864 249 ASN   A CG  
1923 O OD1 . ASN   A 250 ? 0.3714 0.3891 0.6585 0.0382  0.0942  -0.0774 249 ASN   A OD1 
1924 N ND2 . ASN   A 250 ? 0.4010 0.4168 0.6502 0.0373  0.1167  -0.1018 249 ASN   A ND2 
1925 N N   . PHE   A 251 ? 0.3139 0.3565 0.5663 0.0221  0.0883  -0.0452 250 PHE   A N   
1926 C CA  . PHE   A 251 ? 0.3029 0.3394 0.5459 0.0191  0.0723  -0.0340 250 PHE   A CA  
1927 C C   . PHE   A 251 ? 0.3095 0.3425 0.5181 0.0128  0.0713  -0.0316 250 PHE   A C   
1928 O O   . PHE   A 251 ? 0.3207 0.3455 0.5159 0.0111  0.0628  -0.0296 250 PHE   A O   
1929 C CB  . PHE   A 251 ? 0.2904 0.3356 0.5528 0.0190  0.0647  -0.0231 250 PHE   A CB  
1930 C CG  . PHE   A 251 ? 0.2941 0.3338 0.5432 0.0162  0.0504  -0.0129 250 PHE   A CG  
1931 C CD1 . PHE   A 251 ? 0.2917 0.3254 0.5500 0.0190  0.0396  -0.0076 250 PHE   A CD1 
1932 C CD2 . PHE   A 251 ? 0.3153 0.3560 0.5439 0.0110  0.0483  -0.0082 250 PHE   A CD2 
1933 C CE1 . PHE   A 251 ? 0.2929 0.3227 0.5362 0.0164  0.0290  0.0015  250 PHE   A CE1 
1934 C CE2 . PHE   A 251 ? 0.3209 0.3573 0.5377 0.0094  0.0373  -0.0010 250 PHE   A CE2 
1935 C CZ  . PHE   A 251 ? 0.3069 0.3385 0.5295 0.0120  0.0286  0.0035  250 PHE   A CZ  
1936 N N   . ILE   A 252 ? 0.3058 0.3450 0.5023 0.0093  0.0803  -0.0314 251 ILE   A N   
1937 C CA  . ILE   A 252 ? 0.3187 0.3540 0.4844 0.0039  0.0786  -0.0282 251 ILE   A CA  
1938 C C   . ILE   A 252 ? 0.3485 0.3748 0.4929 0.0039  0.0797  -0.0380 251 ILE   A C   
1939 O O   . ILE   A 252 ? 0.3520 0.3716 0.4797 0.0013  0.0703  -0.0358 251 ILE   A O   
1940 C CB  . ILE   A 252 ? 0.3198 0.3631 0.4801 -0.0002 0.0888  -0.0240 251 ILE   A CB  
1941 C CG1 . ILE   A 252 ? 0.3259 0.3762 0.5072 -0.0018 0.0836  -0.0141 251 ILE   A CG1 
1942 C CG2 . ILE   A 252 ? 0.3243 0.3618 0.4507 -0.0053 0.0883  -0.0210 251 ILE   A CG2 
1943 C CD1 . ILE   A 252 ? 0.3233 0.3679 0.4996 -0.0027 0.0686  -0.0072 251 ILE   A CD1 
1944 N N   . LYS   A 253 ? 0.3692 0.3954 0.5163 0.0070  0.0907  -0.0500 252 LYS   A N   
1945 C CA  . LYS   A 253 ? 0.3929 0.4091 0.5196 0.0071  0.0910  -0.0623 252 LYS   A CA  
1946 C C   . LYS   A 253 ? 0.3921 0.3982 0.5254 0.0076  0.0768  -0.0631 252 LYS   A C   
1947 O O   . LYS   A 253 ? 0.4150 0.4142 0.5277 0.0040  0.0691  -0.0651 252 LYS   A O   
1948 C CB  . LYS   A 253 ? 0.4205 0.4379 0.5540 0.0119  0.1062  -0.0775 252 LYS   A CB  
1949 C CG  . LYS   A 253 ? 0.4942 0.4999 0.6015 0.0117  0.1069  -0.0932 252 LYS   A CG  
1950 C CD  . LYS   A 253 ? 0.5718 0.5782 0.6873 0.0179  0.1237  -0.1107 252 LYS   A CD  
1951 C CE  . LYS   A 253 ? 0.6408 0.6335 0.7317 0.0186  0.1236  -0.1298 252 LYS   A CE  
1952 N NZ  . LYS   A 253 ? 0.6801 0.6721 0.7870 0.0266  0.1395  -0.1488 252 LYS   A NZ  
1953 N N   . VAL   A 254 ? 0.3578 0.3635 0.5206 0.0114  0.0725  -0.0599 253 VAL   A N   
1954 C CA  . VAL   A 254 ? 0.3503 0.3461 0.5209 0.0111  0.0609  -0.0589 253 VAL   A CA  
1955 C C   . VAL   A 254 ? 0.3396 0.3373 0.5034 0.0068  0.0504  -0.0453 253 VAL   A C   
1956 O O   . VAL   A 254 ? 0.3331 0.3247 0.4910 0.0037  0.0429  -0.0459 253 VAL   A O   
1957 C CB  . VAL   A 254 ? 0.3535 0.3448 0.5560 0.0166  0.0598  -0.0603 253 VAL   A CB  
1958 C CG1 . VAL   A 254 ? 0.3563 0.3463 0.5677 0.0221  0.0717  -0.0761 253 VAL   A CG1 
1959 C CG2 . VAL   A 254 ? 0.3520 0.3515 0.5735 0.0186  0.0565  -0.0466 253 VAL   A CG2 
1960 N N   . THR   A 255 ? 0.3272 0.3334 0.4936 0.0065  0.0499  -0.0343 254 THR   A N   
1961 C CA  . THR   A 255 ? 0.3291 0.3369 0.4876 0.0034  0.0418  -0.0240 254 THR   A CA  
1962 C C   . THR   A 255 ? 0.3410 0.3479 0.4764 -0.0004 0.0401  -0.0258 254 THR   A C   
1963 O O   . THR   A 255 ? 0.3481 0.3537 0.4804 -0.0026 0.0328  -0.0222 254 THR   A O   
1964 C CB  . THR   A 255 ? 0.3388 0.3537 0.5026 0.0041  0.0410  -0.0149 254 THR   A CB  
1965 O OG1 . THR   A 255 ? 0.3374 0.3577 0.4954 0.0032  0.0480  -0.0165 254 THR   A OG1 
1966 C CG2 . THR   A 255 ? 0.3307 0.3461 0.5159 0.0076  0.0380  -0.0107 254 THR   A CG2 
1967 N N   . LEU   A 256 ? 0.3364 0.3445 0.4569 -0.0013 0.0467  -0.0309 255 LEU   A N   
1968 C CA  . LEU   A 256 ? 0.3426 0.3486 0.4392 -0.0049 0.0433  -0.0314 255 LEU   A CA  
1969 C C   . LEU   A 256 ? 0.3589 0.3575 0.4437 -0.0060 0.0413  -0.0431 255 LEU   A C   
1970 O O   . LEU   A 256 ? 0.3845 0.3810 0.4451 -0.0080 0.0432  -0.0474 255 LEU   A O   
1971 C CB  . LEU   A 256 ? 0.3398 0.3498 0.4213 -0.0066 0.0499  -0.0270 255 LEU   A CB  
1972 C CG  . LEU   A 256 ? 0.3335 0.3493 0.4278 -0.0064 0.0506  -0.0168 255 LEU   A CG  
1973 C CD1 . LEU   A 256 ? 0.3360 0.3535 0.4159 -0.0098 0.0552  -0.0109 255 LEU   A CD1 
1974 C CD2 . LEU   A 256 ? 0.3239 0.3393 0.4245 -0.0060 0.0400  -0.0101 255 LEU   A CD2 
1975 N N   . THR   A 257 ? 0.3383 0.3317 0.4391 -0.0050 0.0371  -0.0483 256 THR   A N   
1976 C CA  . THR   A 257 ? 0.3391 0.3236 0.4313 -0.0068 0.0322  -0.0605 256 THR   A CA  
1977 C C   . THR   A 257 ? 0.3573 0.3425 0.4390 -0.0113 0.0198  -0.0557 256 THR   A C   
1978 O O   . THR   A 257 ? 0.3416 0.3319 0.4376 -0.0120 0.0146  -0.0452 256 THR   A O   
1979 C CB  . THR   A 257 ? 0.3618 0.3393 0.4790 -0.0053 0.0299  -0.0653 256 THR   A CB  
1980 O OG1 . THR   A 257 ? 0.3789 0.3563 0.5087 0.0000  0.0405  -0.0698 256 THR   A OG1 
1981 C CG2 . THR   A 257 ? 0.3678 0.3345 0.4787 -0.0079 0.0232  -0.0794 256 THR   A CG2 
1982 N N   . LYS   A 258 ? 0.3772 0.3584 0.4332 -0.0138 0.0155  -0.0628 257 LYS   A N   
1983 C CA  . LYS   A 258 ? 0.4003 0.3827 0.4475 -0.0176 0.0017  -0.0580 257 LYS   A CA  
1984 C C   . LYS   A 258 ? 0.3922 0.3741 0.4640 -0.0201 -0.0094 -0.0584 257 LYS   A C   
1985 O O   . LYS   A 258 ? 0.3878 0.3771 0.4726 -0.0210 -0.0154 -0.0481 257 LYS   A O   
1986 C CB  . LYS   A 258 ? 0.4538 0.4304 0.4660 -0.0201 -0.0027 -0.0662 257 LYS   A CB  
1987 C CG  . LYS   A 258 ? 0.5523 0.5292 0.5561 -0.0237 -0.0201 -0.0623 257 LYS   A CG  
1988 C CD  . LYS   A 258 ? 0.6597 0.6275 0.6290 -0.0266 -0.0271 -0.0745 257 LYS   A CD  
1989 C CE  . LYS   A 258 ? 0.7436 0.7115 0.6777 -0.0273 -0.0253 -0.0668 257 LYS   A CE  
1990 N NZ  . LYS   A 258 ? 0.8082 0.7668 0.7013 -0.0293 -0.0249 -0.0800 257 LYS   A NZ  
1991 N N   . SER   A 259 ? 0.3981 0.3713 0.4789 -0.0213 -0.0111 -0.0702 258 SER   A N   
1992 C CA  . SER   A 259 ? 0.3989 0.3710 0.5061 -0.0250 -0.0209 -0.0698 258 SER   A CA  
1993 C C   . SER   A 259 ? 0.3965 0.3728 0.5317 -0.0233 -0.0137 -0.0590 258 SER   A C   
1994 O O   . SER   A 259 ? 0.3960 0.3670 0.5376 -0.0199 -0.0052 -0.0618 258 SER   A O   
1995 C CB  . SER   A 259 ? 0.4181 0.3767 0.5259 -0.0274 -0.0261 -0.0868 258 SER   A CB  
1996 O OG  . SER   A 259 ? 0.4433 0.4006 0.5817 -0.0321 -0.0350 -0.0846 258 SER   A OG  
1997 N N   . PRO   A 260 ? 0.3902 0.3754 0.5433 -0.0255 -0.0174 -0.0473 259 PRO   A N   
1998 C CA  . PRO   A 260 ? 0.3791 0.3672 0.5545 -0.0246 -0.0107 -0.0367 259 PRO   A CA  
1999 C C   . PRO   A 260 ? 0.3770 0.3542 0.5730 -0.0272 -0.0122 -0.0411 259 PRO   A C   
2000 O O   . PRO   A 260 ? 0.3756 0.3512 0.5851 -0.0256 -0.0062 -0.0332 259 PRO   A O   
2001 C CB  . PRO   A 260 ? 0.3846 0.3851 0.5731 -0.0269 -0.0137 -0.0257 259 PRO   A CB  
2002 C CG  . PRO   A 260 ? 0.3928 0.3957 0.5754 -0.0299 -0.0254 -0.0316 259 PRO   A CG  
2003 C CD  . PRO   A 260 ? 0.3859 0.3795 0.5404 -0.0286 -0.0278 -0.0434 259 PRO   A CD  
2004 N N   . LYS   A 261 ? 0.3702 0.3385 0.5681 -0.0313 -0.0214 -0.0538 260 LYS   A N   
2005 C CA  . LYS   A 261 ? 0.3752 0.3301 0.5949 -0.0338 -0.0235 -0.0590 260 LYS   A CA  
2006 C C   . LYS   A 261 ? 0.3864 0.3299 0.6001 -0.0275 -0.0157 -0.0682 260 LYS   A C   
2007 O O   . LYS   A 261 ? 0.3834 0.3146 0.6175 -0.0277 -0.0162 -0.0712 260 LYS   A O   
2008 C CB  . LYS   A 261 ? 0.4018 0.3496 0.6286 -0.0407 -0.0371 -0.0708 260 LYS   A CB  
2009 C CG  . LYS   A 261 ? 0.4489 0.4096 0.6941 -0.0473 -0.0449 -0.0604 260 LYS   A CG  
2010 C CD  . LYS   A 261 ? 0.5128 0.4667 0.7652 -0.0543 -0.0610 -0.0735 260 LYS   A CD  
2011 C CE  . LYS   A 261 ? 0.5749 0.5439 0.8474 -0.0604 -0.0703 -0.0650 260 LYS   A CE  
2012 N NZ  . LYS   A 261 ? 0.6155 0.5770 0.8978 -0.0680 -0.0889 -0.0788 260 LYS   A NZ  
2013 N N   . LYS   A 262 ? 0.3851 0.3328 0.5738 -0.0220 -0.0084 -0.0725 261 LYS   A N   
2014 C CA  . LYS   A 262 ? 0.3810 0.3221 0.5667 -0.0153 0.0010  -0.0812 261 LYS   A CA  
2015 C C   . LYS   A 262 ? 0.3733 0.3243 0.5609 -0.0101 0.0106  -0.0683 261 LYS   A C   
2016 O O   . LYS   A 262 ? 0.3754 0.3236 0.5678 -0.0044 0.0183  -0.0730 261 LYS   A O   
2017 C CB  . LYS   A 262 ? 0.3925 0.3302 0.5486 -0.0138 0.0032  -0.0987 261 LYS   A CB  
2018 C CG  . LYS   A 262 ? 0.4320 0.3575 0.5837 -0.0187 -0.0083 -0.1146 261 LYS   A CG  
2019 C CD  . LYS   A 262 ? 0.5228 0.4439 0.6382 -0.0175 -0.0065 -0.1324 261 LYS   A CD  
2020 C CE  . LYS   A 262 ? 0.6110 0.5212 0.7272 -0.0110 0.0046  -0.1496 261 LYS   A CE  
2021 N NZ  . LYS   A 262 ? 0.6567 0.5487 0.7926 -0.0126 -0.0038 -0.1649 261 LYS   A NZ  
2022 N N   . ARG   A 263 ? 0.3577 0.3204 0.5427 -0.0119 0.0097  -0.0533 262 ARG   A N   
2023 C CA  . ARG   A 263 ? 0.3385 0.3101 0.5221 -0.0078 0.0165  -0.0426 262 ARG   A CA  
2024 C C   . ARG   A 263 ? 0.3335 0.3024 0.5397 -0.0065 0.0163  -0.0318 262 ARG   A C   
2025 O O   . ARG   A 263 ? 0.3243 0.2905 0.5430 -0.0107 0.0116  -0.0247 262 ARG   A O   
2026 C CB  . ARG   A 263 ? 0.3286 0.3117 0.4990 -0.0100 0.0148  -0.0332 262 ARG   A CB  
2027 C CG  . ARG   A 263 ? 0.3203 0.3116 0.4837 -0.0063 0.0207  -0.0257 262 ARG   A CG  
2028 C CD  . ARG   A 263 ? 0.3399 0.3396 0.4908 -0.0079 0.0184  -0.0193 262 ARG   A CD  
2029 N NE  . ARG   A 263 ? 0.3279 0.3268 0.4642 -0.0105 0.0139  -0.0256 262 ARG   A NE  
2030 C CZ  . ARG   A 263 ? 0.3251 0.3286 0.4610 -0.0129 0.0073  -0.0218 262 ARG   A CZ  
2031 N NH1 . ARG   A 263 ? 0.2847 0.2947 0.4334 -0.0129 0.0072  -0.0126 262 ARG   A NH1 
2032 N NH2 . ARG   A 263 ? 0.3062 0.3082 0.4290 -0.0152 0.0006  -0.0272 262 ARG   A NH2 
2033 N N   . PRO   A 264 ? 0.3307 0.3006 0.5430 -0.0010 0.0211  -0.0292 263 PRO   A N   
2034 C CA  . PRO   A 264 ? 0.3197 0.2854 0.5519 0.0005  0.0186  -0.0177 263 PRO   A CA  
2035 C C   . PRO   A 264 ? 0.3044 0.2779 0.5313 -0.0019 0.0166  -0.0013 263 PRO   A C   
2036 O O   . PRO   A 264 ? 0.3006 0.2840 0.5112 -0.0024 0.0185  0.0005  263 PRO   A O   
2037 C CB  . PRO   A 264 ? 0.3278 0.2949 0.5681 0.0076  0.0229  -0.0208 263 PRO   A CB  
2038 C CG  . PRO   A 264 ? 0.3395 0.3086 0.5678 0.0092  0.0299  -0.0368 263 PRO   A CG  
2039 C CD  . PRO   A 264 ? 0.3283 0.3027 0.5331 0.0037  0.0285  -0.0366 263 PRO   A CD  
2040 N N   . SER   A 265 ? 0.3071 0.2750 0.5474 -0.0036 0.0132  0.0106  264 SER   A N   
2041 C CA  . SER   A 265 ? 0.3024 0.2767 0.5356 -0.0058 0.0128  0.0266  264 SER   A CA  
2042 C C   . SER   A 265 ? 0.3073 0.2870 0.5321 -0.0009 0.0123  0.0320  264 SER   A C   
2043 O O   . SER   A 265 ? 0.2961 0.2746 0.5283 0.0040  0.0120  0.0256  264 SER   A O   
2044 C CB  . SER   A 265 ? 0.3074 0.2725 0.5562 -0.0096 0.0099  0.0393  264 SER   A CB  
2045 O OG  . SER   A 265 ? 0.3168 0.2722 0.5795 -0.0051 0.0058  0.0435  264 SER   A OG  
2046 N N   . ALA   A 266 ? 0.3162 0.3026 0.5266 -0.0023 0.0124  0.0430  265 ALA   A N   
2047 C CA  . ALA   A 266 ? 0.3242 0.3146 0.5259 0.0017  0.0092  0.0475  265 ALA   A CA  
2048 C C   . ALA   A 266 ? 0.3178 0.2998 0.5352 0.0048  0.0025  0.0555  265 ALA   A C   
2049 O O   . ALA   A 266 ? 0.3121 0.2959 0.5364 0.0095  -0.0013 0.0529  265 ALA   A O   
2050 C CB  . ALA   A 266 ? 0.3388 0.3355 0.5198 -0.0002 0.0103  0.0561  265 ALA   A CB  
2051 N N   . THR   A 267 ? 0.3258 0.2988 0.5520 0.0020  0.0005  0.0659  266 THR   A N   
2052 C CA  . THR   A 267 ? 0.3438 0.3066 0.5871 0.0050  -0.0075 0.0756  266 THR   A CA  
2053 C C   . THR   A 267 ? 0.3320 0.2900 0.6003 0.0106  -0.0080 0.0623  266 THR   A C   
2054 O O   . THR   A 267 ? 0.3332 0.2914 0.6141 0.0164  -0.0138 0.0636  266 THR   A O   
2055 C CB  . THR   A 267 ? 0.3987 0.3511 0.6476 -0.0001 -0.0088 0.0907  266 THR   A CB  
2056 O OG1 . THR   A 267 ? 0.4420 0.4010 0.6657 -0.0046 -0.0059 0.1031  266 THR   A OG1 
2057 C CG2 . THR   A 267 ? 0.4021 0.3413 0.6710 0.0033  -0.0186 0.1021  266 THR   A CG2 
2058 N N   . LYS   A 268 ? 0.3248 0.2805 0.5992 0.0091  -0.0018 0.0479  267 LYS   A N   
2059 C CA  . LYS   A 268 ? 0.3226 0.2742 0.6167 0.0148  0.0003  0.0323  267 LYS   A CA  
2060 C C   . LYS   A 268 ? 0.3159 0.2800 0.6065 0.0197  0.0035  0.0249  267 LYS   A C   
2061 O O   . LYS   A 268 ? 0.3171 0.2807 0.6291 0.0261  0.0026  0.0209  267 LYS   A O   
2062 C CB  . LYS   A 268 ? 0.3369 0.2836 0.6303 0.0116  0.0058  0.0170  267 LYS   A CB  
2063 C CG  . LYS   A 268 ? 0.3304 0.2725 0.6381 0.0174  0.0103  -0.0018 267 LYS   A CG  
2064 C CD  . LYS   A 268 ? 0.3503 0.2797 0.6901 0.0237  0.0055  0.0001  267 LYS   A CD  
2065 C CE  . LYS   A 268 ? 0.3766 0.2987 0.7313 0.0291  0.0115  -0.0215 267 LYS   A CE  
2066 N NZ  . LYS   A 268 ? 0.3605 0.2692 0.7509 0.0364  0.0067  -0.0208 267 LYS   A NZ  
2067 N N   . MET   A 269 ? 0.3155 0.2908 0.5827 0.0166  0.0072  0.0234  268 MET   A N   
2068 C CA  . MET   A 269 ? 0.3031 0.2900 0.5674 0.0194  0.0102  0.0180  268 MET   A CA  
2069 C C   . MET   A 269 ? 0.3158 0.3060 0.5920 0.0232  0.0017  0.0280  268 MET   A C   
2070 O O   . MET   A 269 ? 0.3178 0.3159 0.6074 0.0269  0.0035  0.0224  268 MET   A O   
2071 C CB  . MET   A 269 ? 0.3011 0.2967 0.5389 0.0149  0.0136  0.0171  268 MET   A CB  
2072 C CG  . MET   A 269 ? 0.3169 0.3119 0.5426 0.0118  0.0206  0.0063  268 MET   A CG  
2073 S SD  . MET   A 269 ? 0.3778 0.3713 0.6136 0.0152  0.0292  -0.0106 268 MET   A SD  
2074 C CE  . MET   A 269 ? 0.3545 0.3606 0.5985 0.0187  0.0328  -0.0101 268 MET   A CE  
2075 N N   . LEU   A 270 ? 0.3104 0.2952 0.5821 0.0220  -0.0078 0.0432  269 LEU   A N   
2076 C CA  . LEU   A 270 ? 0.3255 0.3131 0.6064 0.0256  -0.0189 0.0530  269 LEU   A CA  
2077 C C   . LEU   A 270 ? 0.3406 0.3257 0.6588 0.0329  -0.0222 0.0501  269 LEU   A C   
2078 O O   . LEU   A 270 ? 0.3489 0.3404 0.6815 0.0367  -0.0308 0.0542  269 LEU   A O   
2079 C CB  . LEU   A 270 ? 0.3407 0.3223 0.6039 0.0228  -0.0285 0.0706  269 LEU   A CB  
2080 C CG  . LEU   A 270 ? 0.3820 0.3702 0.6108 0.0179  -0.0263 0.0723  269 LEU   A CG  
2081 C CD1 . LEU   A 270 ? 0.4029 0.3844 0.6108 0.0139  -0.0290 0.0877  269 LEU   A CD1 
2082 C CD2 . LEU   A 270 ? 0.3850 0.3821 0.6093 0.0197  -0.0337 0.0704  269 LEU   A CD2 
2083 N N   . SER   A 271 ? 0.3344 0.3108 0.6701 0.0352  -0.0160 0.0418  270 SER   A N   
2084 C CA  . SER   A 271 ? 0.3391 0.3135 0.7130 0.0435  -0.0169 0.0359  270 SER   A CA  
2085 C C   . SER   A 271 ? 0.3456 0.3300 0.7288 0.0464  -0.0026 0.0166  270 SER   A C   
2086 O O   . SER   A 271 ? 0.3539 0.3386 0.7691 0.0539  0.0005  0.0084  270 SER   A O   
2087 C CB  . SER   A 271 ? 0.3576 0.3139 0.7499 0.0457  -0.0203 0.0386  270 SER   A CB  
2088 O OG  . SER   A 271 ? 0.4149 0.3642 0.7910 0.0402  -0.0114 0.0296  270 SER   A OG  
2089 N N   . HIS   A 272 ? 0.3362 0.3296 0.6926 0.0411  0.0064  0.0099  271 HIS   A N   
2090 C CA  . HIS   A 272 ? 0.3252 0.3289 0.6861 0.0428  0.0207  -0.0058 271 HIS   A CA  
2091 C C   . HIS   A 272 ? 0.3323 0.3499 0.7214 0.0476  0.0187  -0.0037 271 HIS   A C   
2092 O O   . HIS   A 272 ? 0.3449 0.3674 0.7311 0.0456  0.0068  0.0086  271 HIS   A O   
2093 C CB  . HIS   A 272 ? 0.3239 0.3338 0.6501 0.0355  0.0274  -0.0084 271 HIS   A CB  
2094 C CG  . HIS   A 272 ? 0.3202 0.3376 0.6449 0.0361  0.0429  -0.0230 271 HIS   A CG  
2095 N ND1 . HIS   A 272 ? 0.3189 0.3513 0.6590 0.0377  0.0494  -0.0247 271 HIS   A ND1 
2096 C CD2 . HIS   A 272 ? 0.3196 0.3310 0.6314 0.0355  0.0529  -0.0362 271 HIS   A CD2 
2097 C CE1 . HIS   A 272 ? 0.3187 0.3539 0.6520 0.0379  0.0650  -0.0378 271 HIS   A CE1 
2098 N NE2 . HIS   A 272 ? 0.3317 0.3539 0.6459 0.0369  0.0668  -0.0457 271 HIS   A NE2 
2099 N N   . GLN   A 273 ? 0.3200 0.3446 0.7363 0.0537  0.0305  -0.0164 272 GLN   A N   
2100 C CA  . GLN   A 273 ? 0.3201 0.3609 0.7713 0.0585  0.0307  -0.0158 272 GLN   A CA  
2101 C C   . GLN   A 273 ? 0.3137 0.3679 0.7530 0.0520  0.0267  -0.0081 272 GLN   A C   
2102 O O   . GLN   A 273 ? 0.3205 0.3842 0.7856 0.0541  0.0162  -0.0007 272 GLN   A O   
2103 C CB  . GLN   A 273 ? 0.3628 0.4124 0.8349 0.0637  0.0511  -0.0334 272 GLN   A CB  
2104 C CG  . GLN   A 273 ? 0.4268 0.4950 0.9471 0.0702  0.0530  -0.0336 272 GLN   A CG  
2105 C CD  . GLN   A 273 ? 0.5165 0.5992 1.0517 0.0731  0.0775  -0.0497 272 GLN   A CD  
2106 O OE1 . GLN   A 273 ? 0.5724 0.6482 1.0887 0.0738  0.0933  -0.0641 272 GLN   A OE1 
2107 N NE2 . GLN   A 273 ? 0.5017 0.6055 1.0709 0.0742  0.0814  -0.0475 272 GLN   A NE2 
2108 N N   . LEU   A 274 ? 0.3039 0.3582 0.7067 0.0443  0.0335  -0.0098 273 LEU   A N   
2109 C CA  . LEU   A 274 ? 0.2839 0.3491 0.6781 0.0382  0.0302  -0.0039 273 LEU   A CA  
2110 C C   . LEU   A 274 ? 0.2968 0.3581 0.6830 0.0362  0.0097  0.0093  273 LEU   A C   
2111 O O   . LEU   A 274 ? 0.2960 0.3671 0.6957 0.0346  0.0013  0.0140  273 LEU   A O   
2112 C CB  . LEU   A 274 ? 0.2855 0.3491 0.6432 0.0311  0.0407  -0.0078 273 LEU   A CB  
2113 C CG  . LEU   A 274 ? 0.2814 0.3550 0.6355 0.0249  0.0390  -0.0030 273 LEU   A CG  
2114 C CD1 . LEU   A 274 ? 0.2835 0.3738 0.6698 0.0256  0.0512  -0.0074 273 LEU   A CD1 
2115 C CD2 . LEU   A 274 ? 0.2830 0.3507 0.5988 0.0183  0.0434  -0.0032 273 LEU   A CD2 
2116 N N   . VAL   A 275 ? 0.3073 0.3544 0.6707 0.0355  0.0020  0.0152  274 VAL   A N   
2117 C CA  . VAL   A 275 ? 0.3230 0.3659 0.6706 0.0332  -0.0150 0.0274  274 VAL   A CA  
2118 C C   . VAL   A 275 ? 0.3499 0.3871 0.7155 0.0382  -0.0300 0.0375  274 VAL   A C   
2119 O O   . VAL   A 275 ? 0.3665 0.4000 0.7163 0.0364  -0.0448 0.0484  274 VAL   A O   
2120 C CB  . VAL   A 275 ? 0.3433 0.3767 0.6511 0.0280  -0.0130 0.0294  274 VAL   A CB  
2121 C CG1 . VAL   A 275 ? 0.3477 0.3866 0.6381 0.0231  -0.0020 0.0216  274 VAL   A CG1 
2122 C CG2 . VAL   A 275 ? 0.3488 0.3707 0.6549 0.0296  -0.0078 0.0282  274 VAL   A CG2 
2123 N N   . SER   A 276 ? 0.3553 0.3902 0.7517 0.0448  -0.0266 0.0343  275 SER   A N   
2124 C CA  . SER   A 276 ? 0.3658 0.3943 0.7858 0.0506  -0.0418 0.0449  275 SER   A CA  
2125 C C   . SER   A 276 ? 0.3556 0.3979 0.8211 0.0568  -0.0477 0.0437  275 SER   A C   
2126 O O   . SER   A 276 ? 0.3672 0.4056 0.8596 0.0630  -0.0612 0.0521  275 SER   A O   
2127 C CB  . SER   A 276 ? 0.3884 0.4019 0.8161 0.0543  -0.0368 0.0433  275 SER   A CB  
2128 O OG  . SER   A 276 ? 0.4085 0.4267 0.8656 0.0600  -0.0224 0.0278  275 SER   A OG  
2129 N N   . GLN   A 277 ? 0.3375 0.3965 0.8151 0.0551  -0.0377 0.0342  276 GLN   A N   
2130 C CA  . GLN   A 277 ? 0.3220 0.3979 0.8476 0.0600  -0.0411 0.0325  276 GLN   A CA  
2131 C C   . GLN   A 277 ? 0.3313 0.4109 0.8636 0.0590  -0.0667 0.0457  276 GLN   A C   
2132 O O   . GLN   A 277 ? 0.3420 0.4145 0.8348 0.0526  -0.0774 0.0529  276 GLN   A O   
2133 C CB  . GLN   A 277 ? 0.3028 0.3955 0.8371 0.0566  -0.0213 0.0202  276 GLN   A CB  
2134 C CG  . GLN   A 277 ? 0.2984 0.3942 0.8000 0.0466  -0.0226 0.0222  276 GLN   A CG  
2135 C CD  . GLN   A 277 ? 0.3095 0.4203 0.8220 0.0428  -0.0029 0.0128  276 GLN   A CD  
2136 O OE1 . GLN   A 277 ? 0.3320 0.4392 0.8110 0.0365  0.0091  0.0089  276 GLN   A OE1 
2137 N NE2 . GLN   A 277 ? 0.2269 0.3557 0.7876 0.0461  0.0008  0.0102  276 GLN   A NE2 
2138 N N   . PRO   A 278 ? 0.3277 0.4178 0.9096 0.0659  -0.0779 0.0488  277 PRO   A N   
2139 C CA  . PRO   A 278 ? 0.3333 0.4279 0.9220 0.0644  -0.1051 0.0609  277 PRO   A CA  
2140 C C   . PRO   A 278 ? 0.3352 0.4430 0.9161 0.0557  -0.1072 0.0572  277 PRO   A C   
2141 O O   . PRO   A 278 ? 0.3240 0.4429 0.9110 0.0519  -0.0870 0.0464  277 PRO   A O   
2142 C CB  . PRO   A 278 ? 0.3185 0.4246 0.9723 0.0746  -0.1141 0.0628  277 PRO   A CB  
2143 C CG  . PRO   A 278 ? 0.3161 0.4214 0.9943 0.0821  -0.0903 0.0511  277 PRO   A CG  
2144 C CD  . PRO   A 278 ? 0.3098 0.4108 0.9460 0.0751  -0.0657 0.0398  277 PRO   A CD  
2145 N N   . GLY   A 279 ? 0.3389 0.4447 0.9070 0.0525  -0.1328 0.0668  278 GLY   A N   
2146 C CA  . GLY   A 279 ? 0.3294 0.4451 0.8935 0.0444  -0.1404 0.0636  278 GLY   A CA  
2147 C C   . GLY   A 279 ? 0.3443 0.4504 0.8542 0.0358  -0.1311 0.0587  278 GLY   A C   
2148 O O   . GLY   A 279 ? 0.3465 0.4602 0.8573 0.0289  -0.1321 0.0535  278 GLY   A O   
2149 N N   . LEU   A 280 ? 0.3454 0.4348 0.8111 0.0360  -0.1225 0.0605  279 LEU   A N   
2150 C CA  . LEU   A 280 ? 0.3606 0.4412 0.7772 0.0289  -0.1143 0.0560  279 LEU   A CA  
2151 C C   . LEU   A 280 ? 0.3896 0.4590 0.7681 0.0267  -0.1363 0.0639  279 LEU   A C   
2152 O O   . LEU   A 280 ? 0.4054 0.4645 0.7688 0.0303  -0.1449 0.0742  279 LEU   A O   
2153 C CB  . LEU   A 280 ? 0.3488 0.4196 0.7410 0.0298  -0.0930 0.0530  279 LEU   A CB  
2154 C CG  . LEU   A 280 ? 0.3344 0.4130 0.7526 0.0320  -0.0699 0.0438  279 LEU   A CG  
2155 C CD1 . LEU   A 280 ? 0.3359 0.4035 0.7204 0.0305  -0.0527 0.0396  279 LEU   A CD1 
2156 C CD2 . LEU   A 280 ? 0.3264 0.4192 0.7627 0.0272  -0.0610 0.0362  279 LEU   A CD2 
2157 N N   . ASN   A 281 ? 0.3837 0.4549 0.7491 0.0208  -0.1465 0.0595  280 ASN   A N   
2158 C CA  . ASN   A 281 ? 0.4016 0.4627 0.7282 0.0186  -0.1676 0.0641  280 ASN   A CA  
2159 C C   . ASN   A 281 ? 0.4100 0.4700 0.7166 0.0116  -0.1694 0.0534  280 ASN   A C   
2160 O O   . ASN   A 281 ? 0.3977 0.4662 0.7283 0.0083  -0.1575 0.0452  280 ASN   A O   
2161 C CB  . ASN   A 281 ? 0.4126 0.4769 0.7611 0.0219  -0.1953 0.0740  280 ASN   A CB  
2162 C CG  . ASN   A 281 ? 0.4399 0.5216 0.8428 0.0208  -0.2052 0.0695  280 ASN   A CG  
2163 O OD1 . ASN   A 281 ? 0.4493 0.5353 0.8531 0.0143  -0.2105 0.0610  280 ASN   A OD1 
2164 N ND2 . ASN   A 281 ? 0.4260 0.5182 0.8789 0.0270  -0.2078 0.0750  280 ASN   A ND2 
2165 N N   . ARG   A 282 ? 0.4271 0.4758 0.6891 0.0095  -0.1835 0.0533  281 ARG   A N   
2166 C CA  . ARG   A 282 ? 0.4350 0.4791 0.6747 0.0037  -0.1864 0.0415  281 ARG   A CA  
2167 C C   . ARG   A 282 ? 0.4178 0.4723 0.6976 -0.0011 -0.1982 0.0346  281 ARG   A C   
2168 O O   . ARG   A 282 ? 0.4167 0.4679 0.6899 -0.0064 -0.1946 0.0241  281 ARG   A O   
2169 C CB  . ARG   A 282 ? 0.4770 0.5075 0.6627 0.0034  -0.2016 0.0419  281 ARG   A CB  
2170 C CG  . ARG   A 282 ? 0.5033 0.5342 0.6915 0.0045  -0.2312 0.0504  281 ARG   A CG  
2171 C CD  . ARG   A 282 ? 0.5516 0.5681 0.6781 0.0044  -0.2430 0.0521  281 ARG   A CD  
2172 N NE  . ARG   A 282 ? 0.6007 0.6167 0.7261 0.0040  -0.2758 0.0575  281 ARG   A NE  
2173 C CZ  . ARG   A 282 ? 0.6387 0.6536 0.7616 -0.0005 -0.2971 0.0465  281 ARG   A CZ  
2174 N NH1 . ARG   A 282 ? 0.6468 0.6617 0.7700 -0.0008 -0.3292 0.0524  281 ARG   A NH1 
2175 N NH2 . ARG   A 282 ? 0.6416 0.6548 0.7636 -0.0048 -0.2881 0.0295  281 ARG   A NH2 
2176 N N   . GLY   A 283 ? 0.4001 0.4670 0.7249 0.0006  -0.2118 0.0409  282 GLY   A N   
2177 C CA  . GLY   A 283 ? 0.3849 0.4652 0.7575 -0.0044 -0.2228 0.0360  282 GLY   A CA  
2178 C C   . GLY   A 283 ? 0.3654 0.4537 0.7642 -0.0085 -0.1979 0.0295  282 GLY   A C   
2179 O O   . GLY   A 283 ? 0.3535 0.4462 0.7732 -0.0157 -0.2029 0.0230  282 GLY   A O   
2180 N N   . LEU   A 284 ? 0.3568 0.4458 0.7528 -0.0047 -0.1716 0.0316  283 LEU   A N   
2181 C CA  . LEU   A 284 ? 0.3470 0.4418 0.7590 -0.0083 -0.1465 0.0269  283 LEU   A CA  
2182 C C   . LEU   A 284 ? 0.3657 0.4475 0.7435 -0.0144 -0.1438 0.0191  283 LEU   A C   
2183 O O   . LEU   A 284 ? 0.3608 0.4469 0.7592 -0.0209 -0.1365 0.0154  283 LEU   A O   
2184 C CB  . LEU   A 284 ? 0.3355 0.4295 0.7389 -0.0025 -0.1225 0.0297  283 LEU   A CB  
2185 C CG  . LEU   A 284 ? 0.3274 0.4327 0.7681 0.0044  -0.1207 0.0352  283 LEU   A CG  
2186 C CD1 . LEU   A 284 ? 0.3170 0.4164 0.7412 0.0099  -0.1003 0.0360  283 LEU   A CD1 
2187 C CD2 . LEU   A 284 ? 0.3239 0.4496 0.8223 0.0022  -0.1149 0.0335  283 LEU   A CD2 
2188 N N   . ILE   A 285 ? 0.3871 0.4530 0.7148 -0.0123 -0.1494 0.0171  284 ILE   A N   
2189 C CA  . ILE   A 285 ? 0.4004 0.4529 0.6955 -0.0161 -0.1474 0.0084  284 ILE   A CA  
2190 C C   . ILE   A 285 ? 0.4083 0.4569 0.7074 -0.0216 -0.1712 0.0013  284 ILE   A C   
2191 O O   . ILE   A 285 ? 0.4067 0.4491 0.7068 -0.0271 -0.1692 -0.0063 284 ILE   A O   
2192 C CB  . ILE   A 285 ? 0.4317 0.4709 0.6752 -0.0113 -0.1395 0.0079  284 ILE   A CB  
2193 C CG1 . ILE   A 285 ? 0.4348 0.4782 0.6813 -0.0073 -0.1168 0.0139  284 ILE   A CG1 
2194 C CG2 . ILE   A 285 ? 0.4510 0.4773 0.6670 -0.0140 -0.1362 -0.0025 284 ILE   A CG2 
2195 C CD1 . ILE   A 285 ? 0.4397 0.4876 0.7060 -0.0108 -0.0971 0.0114  284 ILE   A CD1 
2196 N N   . LEU   A 286 ? 0.4180 0.4705 0.7256 -0.0208 -0.1949 0.0041  285 LEU   A N   
2197 C CA  . LEU   A 286 ? 0.4419 0.4921 0.7592 -0.0268 -0.2209 -0.0033 285 LEU   A CA  
2198 C C   . LEU   A 286 ? 0.4373 0.5001 0.8111 -0.0345 -0.2167 -0.0046 285 LEU   A C   
2199 O O   . LEU   A 286 ? 0.4442 0.4994 0.8209 -0.0416 -0.2245 -0.0136 285 LEU   A O   
2200 C CB  . LEU   A 286 ? 0.4471 0.5017 0.7682 -0.0242 -0.2481 0.0026  285 LEU   A CB  
2201 C CG  . LEU   A 286 ? 0.5051 0.5453 0.7658 -0.0187 -0.2570 0.0045  285 LEU   A CG  
2202 C CD1 . LEU   A 286 ? 0.5126 0.5569 0.7791 -0.0166 -0.2865 0.0128  285 LEU   A CD1 
2203 C CD2 . LEU   A 286 ? 0.5405 0.5628 0.7532 -0.0215 -0.2626 -0.0097 285 LEU   A CD2 
2204 N N   . ASP   A 287 ? 0.4180 0.4990 0.8354 -0.0331 -0.2013 0.0042  286 ASP   A N   
2205 C CA  . ASP   A 287 ? 0.4061 0.5012 0.8764 -0.0406 -0.1918 0.0048  286 ASP   A CA  
2206 C C   . ASP   A 287 ? 0.4165 0.5007 0.8693 -0.0453 -0.1720 0.0008  286 ASP   A C   
2207 O O   . ASP   A 287 ? 0.4270 0.5107 0.9035 -0.0543 -0.1751 -0.0025 286 ASP   A O   
2208 C CB  . ASP   A 287 ? 0.4132 0.5292 0.9261 -0.0366 -0.1747 0.0136  286 ASP   A CB  
2209 C CG  . ASP   A 287 ? 0.4702 0.5963 1.0031 -0.0299 -0.1923 0.0192  286 ASP   A CG  
2210 O OD1 . ASP   A 287 ? 0.4720 0.5980 1.0131 -0.0323 -0.2213 0.0177  286 ASP   A OD1 
2211 O OD2 . ASP   A 287 ? 0.5099 0.6424 1.0489 -0.0220 -0.1783 0.0249  286 ASP   A OD2 
2212 N N   . LEU   A 288 ? 0.4098 0.4843 0.8222 -0.0395 -0.1535 0.0014  287 LEU   A N   
2213 C CA  . LEU   A 288 ? 0.4088 0.4719 0.8025 -0.0427 -0.1369 -0.0015 287 LEU   A CA  
2214 C C   . LEU   A 288 ? 0.4306 0.4755 0.8036 -0.0471 -0.1534 -0.0120 287 LEU   A C   
2215 O O   . LEU   A 288 ? 0.4362 0.4757 0.8232 -0.0542 -0.1490 -0.0139 287 LEU   A O   
2216 C CB  . LEU   A 288 ? 0.4083 0.4649 0.7627 -0.0349 -0.1186 0.0006  287 LEU   A CB  
2217 C CG  . LEU   A 288 ? 0.4218 0.4671 0.7563 -0.0368 -0.1025 -0.0012 287 LEU   A CG  
2218 C CD1 . LEU   A 288 ? 0.4121 0.4671 0.7800 -0.0431 -0.0863 0.0050  287 LEU   A CD1 
2219 C CD2 . LEU   A 288 ? 0.4220 0.4610 0.7180 -0.0291 -0.0895 -0.0003 287 LEU   A CD2 
2220 N N   . LEU   A 289 ? 0.4496 0.4845 0.7900 -0.0432 -0.1726 -0.0188 288 LEU   A N   
2221 C CA  . LEU   A 289 ? 0.4891 0.5054 0.8052 -0.0460 -0.1886 -0.0319 288 LEU   A CA  
2222 C C   . LEU   A 289 ? 0.5203 0.5386 0.8757 -0.0557 -0.2086 -0.0366 288 LEU   A C   
2223 O O   . LEU   A 289 ? 0.5417 0.5443 0.8913 -0.0605 -0.2166 -0.0473 288 LEU   A O   
2224 C CB  . LEU   A 289 ? 0.5031 0.5090 0.7694 -0.0393 -0.2020 -0.0381 288 LEU   A CB  
2225 C CG  . LEU   A 289 ? 0.5289 0.5320 0.7557 -0.0306 -0.1829 -0.0337 288 LEU   A CG  
2226 C CD1 . LEU   A 289 ? 0.5548 0.5514 0.7380 -0.0252 -0.1962 -0.0359 288 LEU   A CD1 
2227 C CD2 . LEU   A 289 ? 0.5360 0.5272 0.7444 -0.0295 -0.1653 -0.0396 288 LEU   A CD2 
2228 N N   . ASP   A 290 ? 0.5230 0.5605 0.9226 -0.0586 -0.2171 -0.0290 289 ASP   A N   
2229 C CA  . ASP   A 290 ? 0.5363 0.5799 0.9836 -0.0689 -0.2356 -0.0318 289 ASP   A CA  
2230 C C   . ASP   A 290 ? 0.5439 0.5868 1.0218 -0.0777 -0.2183 -0.0293 289 ASP   A C   
2231 O O   . ASP   A 290 ? 0.5417 0.5777 1.0424 -0.0871 -0.2327 -0.0356 289 ASP   A O   
2232 C CB  . ASP   A 290 ? 0.5621 0.6303 1.0564 -0.0689 -0.2440 -0.0224 289 ASP   A CB  
2233 C CG  . ASP   A 290 ? 0.6786 0.7457 1.1600 -0.0658 -0.2759 -0.0261 289 ASP   A CG  
2234 O OD1 . ASP   A 290 ? 0.7139 0.7644 1.1708 -0.0693 -0.2986 -0.0385 289 ASP   A OD1 
2235 O OD2 . ASP   A 290 ? 0.7188 0.8010 1.2151 -0.0598 -0.2791 -0.0169 289 ASP   A OD2 
2236 N N   . LYS   A 291 ? 0.5614 0.6097 1.0379 -0.0751 -0.1887 -0.0199 290 LYS   A N   
2237 C CA  . LYS   A 291 ? 0.5886 0.6344 1.0861 -0.0831 -0.1710 -0.0149 290 LYS   A CA  
2238 C C   . LYS   A 291 ? 0.6513 0.6704 1.1203 -0.0853 -0.1762 -0.0247 290 LYS   A C   
2239 O O   . LYS   A 291 ? 0.6480 0.6614 1.1397 -0.0940 -0.1693 -0.0210 290 LYS   A O   
2240 C CB  . LYS   A 291 ? 0.6063 0.6610 1.0965 -0.0786 -0.1402 -0.0039 290 LYS   A CB  
2241 C CG  . LYS   A 291 ? 0.6329 0.7141 1.1628 -0.0785 -0.1283 0.0059  290 LYS   A CG  
2242 C CD  . LYS   A 291 ? 0.6876 0.7738 1.2070 -0.0757 -0.0975 0.0145  290 LYS   A CD  
2243 C CE  . LYS   A 291 ? 0.7373 0.8180 1.2689 -0.0857 -0.0842 0.0206  290 LYS   A CE  
2244 N NZ  . LYS   A 291 ? 0.7804 0.8675 1.3015 -0.0838 -0.0552 0.0296  290 LYS   A NZ  
2245 N N   . LEU   A 292 ? 0.7028 0.7053 1.1225 -0.0773 -0.1863 -0.0364 291 LEU   A N   
2246 C CA  . LEU   A 292 ? 0.7545 0.7313 1.1485 -0.0776 -0.1914 -0.0484 291 LEU   A CA  
2247 C C   . LEU   A 292 ? 0.7963 0.7632 1.2177 -0.0877 -0.2158 -0.0586 291 LEU   A C   
2248 O O   . LEU   A 292 ? 0.8121 0.7590 1.2332 -0.0916 -0.2172 -0.0653 291 LEU   A O   
2249 C CB  . LEU   A 292 ? 0.7739 0.7384 1.1108 -0.0664 -0.1949 -0.0594 291 LEU   A CB  
2250 C CG  . LEU   A 292 ? 0.7850 0.7574 1.0951 -0.0570 -0.1725 -0.0504 291 LEU   A CG  
2251 C CD1 . LEU   A 292 ? 0.8097 0.7740 1.0691 -0.0474 -0.1773 -0.0594 291 LEU   A CD1 
2252 C CD2 . LEU   A 292 ? 0.7930 0.7588 1.1026 -0.0570 -0.1515 -0.0449 291 LEU   A CD2 
2253 N N   . LYS   A 293 ? 0.8112 0.7909 1.2583 -0.0919 -0.2366 -0.0599 292 LYS   A N   
2254 C CA  . LYS   A 293 ? 0.8386 0.8116 1.3172 -0.1026 -0.2630 -0.0695 292 LYS   A CA  
2255 C C   . LYS   A 293 ? 0.8514 0.8308 1.3884 -0.1156 -0.2537 -0.0587 292 LYS   A C   
2256 O O   . LYS   A 293 ? 0.8602 0.8241 1.4178 -0.1252 -0.2682 -0.0668 292 LYS   A O   
2257 C CB  . LYS   A 293 ? 0.8580 0.8462 1.3506 -0.1031 -0.2877 -0.0713 292 LYS   A CB  
2258 C CG  . LYS   A 293 ? 0.9384 0.9224 1.3732 -0.0909 -0.2956 -0.0775 292 LYS   A CG  
2259 C CD  . LYS   A 293 ? 0.9840 0.9838 1.4361 -0.0914 -0.3209 -0.0755 292 LYS   A CD  
2260 C CE  . LYS   A 293 ? 1.0518 1.0467 1.4459 -0.0803 -0.3293 -0.0785 292 LYS   A CE  
2261 N NZ  . LYS   A 293 ? 1.0693 1.0799 1.4833 -0.0805 -0.3547 -0.0732 292 LYS   A NZ  
2262 N N   . ASN   A 294 ? 0.8503 0.8522 1.4142 -0.1165 -0.2293 -0.0406 293 ASN   A N   
2263 C CA  . ASN   A 294 ? 0.8510 0.8609 1.4671 -0.1292 -0.2164 -0.0278 293 ASN   A CA  
2264 C C   . ASN   A 294 ? 0.8767 0.8714 1.4722 -0.1287 -0.1924 -0.0206 293 ASN   A C   
2265 O O   . ASN   A 294 ? 0.8853 0.8619 1.4951 -0.1374 -0.1964 -0.0217 293 ASN   A O   
2266 C CB  . ASN   A 294 ? 0.8426 0.8865 1.5059 -0.1320 -0.2040 -0.0132 293 ASN   A CB  
2267 C CG  . ASN   A 294 ? 0.8862 0.9447 1.5253 -0.1205 -0.1790 -0.0043 293 ASN   A CG  
2268 O OD1 . ASN   A 294 ? 0.8886 0.9671 1.5393 -0.1148 -0.1815 -0.0023 293 ASN   A OD1 
2269 N ND2 . ASN   A 294 ? 0.9057 0.9543 1.5137 -0.1171 -0.1554 0.0015  293 ASN   A ND2 
2270 C C1  . A1ITA B .   ? 0.5255 0.4682 0.5016 0.0396  -0.0235 -0.1038 301 A1ITA A C1  
2271 C C2  . A1ITA B .   ? 0.5174 0.4730 0.4714 0.0406  -0.0126 -0.0958 301 A1ITA A C2  
2272 C C3  . A1ITA B .   ? 0.5668 0.5105 0.4843 0.0347  -0.0379 -0.1030 301 A1ITA A C3  
2273 N N6  . A1ITA B .   ? 0.4884 0.4812 0.4393 0.0488  0.0358  -0.0774 301 A1ITA A N6  
2274 C C7  . A1ITA B .   ? 0.6123 0.5111 0.6432 0.0162  -0.0908 -0.1208 301 A1ITA A C7  
2275 C C8  . A1ITA B .   ? 0.6321 0.5247 0.6619 0.0100  -0.1104 -0.1269 301 A1ITA A C8  
2276 C C9  . A1ITA B .   ? 0.6257 0.5210 0.6211 0.0111  -0.1177 -0.1318 301 A1ITA A C9  
2277 C C10 . A1ITA B .   ? 0.6202 0.5240 0.5831 0.0177  -0.1038 -0.1296 301 A1ITA A C10 
2278 C C11 . A1ITA B .   ? 0.6857 0.5589 0.7490 -0.0035 -0.1455 -0.1395 301 A1ITA A C11 
2279 C C12 . A1ITA B .   ? 0.6920 0.5509 0.7929 -0.0101 -0.1542 -0.1428 301 A1ITA A C12 
2280 C C13 . A1ITA B .   ? 0.6635 0.5414 0.7946 -0.0098 -0.1254 -0.1117 301 A1ITA A C13 
2281 C C14 . A1ITA B .   ? 0.6584 0.5512 0.7578 -0.0037 -0.1168 -0.1085 301 A1ITA A C14 
2282 C C15 . A1ITA B .   ? 0.5790 0.5225 0.4617 0.0321  -0.0480 -0.1009 301 A1ITA A C15 
2283 C C16 . A1ITA B .   ? 0.4855 0.4554 0.4484 0.0435  0.0053  -0.0860 301 A1ITA A C16 
2284 C C19 . A1ITA B .   ? 0.4570 0.4464 0.4598 0.0432  0.0219  -0.0662 301 A1ITA A C19 
2285 C C20 . A1ITA B .   ? 0.4580 0.4340 0.4527 0.0412  0.0075  -0.0743 301 A1ITA A C20 
2286 C C21 . A1ITA B .   ? 0.4304 0.4106 0.4680 0.0368  0.0057  -0.0592 301 A1ITA A C21 
2287 C C22 . A1ITA B .   ? 0.4246 0.4279 0.4732 0.0405  0.0281  -0.0475 301 A1ITA A C22 
2288 O O1  . A1ITA B .   ? 0.5881 0.5221 0.4641 0.0286  -0.0675 -0.1081 301 A1ITA A O1  
2289 N N5  . A1ITA B .   ? 0.5802 0.5339 0.4411 0.0333  -0.0360 -0.0903 301 A1ITA A N5  
2290 N N1  . A1ITA B .   ? 0.5436 0.4991 0.4681 0.0380  -0.0195 -0.0946 301 A1ITA A N1  
2291 N N7  . A1ITA B .   ? 0.4339 0.4049 0.4537 0.0369  -0.0022 -0.0693 301 A1ITA A N7  
2292 N N8  . A1ITA B .   ? 0.4451 0.4365 0.4758 0.0403  0.0190  -0.0571 301 A1ITA A N8  
2293 C C18 . A1ITA B .   ? 0.4674 0.4654 0.4511 0.0467  0.0355  -0.0677 301 A1ITA A C18 
2294 C C17 . A1ITA B .   ? 0.4949 0.4735 0.4347 0.0473  0.0201  -0.0867 301 A1ITA A C17 
2295 C C4  . A1ITA B .   ? 0.5718 0.5036 0.5141 0.0333  -0.0483 -0.1123 301 A1ITA A C4  
2296 N N2  . A1ITA B .   ? 0.5484 0.4791 0.5194 0.0357  -0.0405 -0.1120 301 A1ITA A N2  
2297 N N   . A1ITA B .   ? 0.5130 0.4545 0.5170 0.0421  -0.0181 -0.1027 301 A1ITA A N   
2298 C C   . A1ITA B .   ? 0.5128 0.4381 0.5327 0.0443  -0.0252 -0.1150 301 A1ITA A C   
2299 N N3  . A1ITA B .   ? 0.5974 0.5180 0.5356 0.0289  -0.0681 -0.1206 301 A1ITA A N3  
2300 C C5  . A1ITA B .   ? 0.6067 0.5176 0.5745 0.0233  -0.0828 -0.1236 301 A1ITA A C5  
2301 C C6  . A1ITA B .   ? 0.6057 0.5141 0.6080 0.0228  -0.0775 -0.1198 301 A1ITA A C6  
2302 N N4  . A1ITA B .   ? 0.6597 0.5437 0.7231 0.0022  -0.1231 -0.1270 301 A1ITA A N4  
2303 O O   . A1ITA B .   ? 0.6806 0.5507 0.8176 -0.0164 -0.1462 -0.1220 301 A1ITA A O   
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