data_9H8F
# 
_entry.id   9H8F 
# 
_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   9H8F         pdb_00009h8f 10.2210/pdb9h8f/pdb 
WWPDB D_1292134168 ?            ?                   
# 
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                        9H8F 
_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-cyclopropyl-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[[3-methyl-1-[2,2,2-tris(fluoranyl)ethyl]pyrazol-4-yl]amino]pyrazine-2-carboxamide
;
471.438   1   ?        ?              ? ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?        ?              ? ? 
4 water       nat water 18.015    274 ?        ?              ? ? 
# 
_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-cyclopropyl-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[[3-methyl-1-[2,2,2-tris(fluoranyl)ethyl]pyrazol-4-yl]amino]pyrazine-2-carboxamide
;
A1ITB 
3 1,2-ETHANEDIOL EDO   
4 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 
A1ITB non-polymer         . 
;5-cyclopropyl-6-(3-methylimidazo[4,5-c]pyridin-7-yl)-3-[[3-methyl-1-[2,2,2-tris(fluoranyl)ethyl]pyrazol-4-yl]amino]pyrazine-2-carboxamide
;
?                 'C21 H20 F3 N9 O' 471.438 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
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        A1ITB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITB 
_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 A1ITB 1   301 301 A1ITB INH A . 
C 3 EDO   1   302 301 EDO   EDO A . 
D 3 EDO   1   303 302 EDO   EDO A . 
E 4 HOH   1   401 160 HOH   HOH A . 
E 4 HOH   2   402 37  HOH   HOH A . 
E 4 HOH   3   403 188 HOH   HOH A . 
E 4 HOH   4   404 270 HOH   HOH A . 
E 4 HOH   5   405 261 HOH   HOH A . 
E 4 HOH   6   406 187 HOH   HOH A . 
E 4 HOH   7   407 76  HOH   HOH A . 
E 4 HOH   8   408 27  HOH   HOH A . 
E 4 HOH   9   409 72  HOH   HOH A . 
E 4 HOH   10  410 101 HOH   HOH A . 
E 4 HOH   11  411 214 HOH   HOH A . 
E 4 HOH   12  412 167 HOH   HOH A . 
E 4 HOH   13  413 86  HOH   HOH A . 
E 4 HOH   14  414 251 HOH   HOH A . 
E 4 HOH   15  415 99  HOH   HOH A . 
E 4 HOH   16  416 126 HOH   HOH A . 
E 4 HOH   17  417 59  HOH   HOH A . 
E 4 HOH   18  418 269 HOH   HOH A . 
E 4 HOH   19  419 164 HOH   HOH A . 
E 4 HOH   20  420 211 HOH   HOH A . 
E 4 HOH   21  421 257 HOH   HOH A . 
E 4 HOH   22  422 35  HOH   HOH A . 
E 4 HOH   23  423 68  HOH   HOH A . 
E 4 HOH   24  424 66  HOH   HOH A . 
E 4 HOH   25  425 56  HOH   HOH A . 
E 4 HOH   26  426 82  HOH   HOH A . 
E 4 HOH   27  427 253 HOH   HOH A . 
E 4 HOH   28  428 43  HOH   HOH A . 
E 4 HOH   29  429 115 HOH   HOH A . 
E 4 HOH   30  430 38  HOH   HOH A . 
E 4 HOH   31  431 16  HOH   HOH A . 
E 4 HOH   32  432 25  HOH   HOH A . 
E 4 HOH   33  433 24  HOH   HOH A . 
E 4 HOH   34  434 1   HOH   HOH A . 
E 4 HOH   35  435 52  HOH   HOH A . 
E 4 HOH   36  436 32  HOH   HOH A . 
E 4 HOH   37  437 60  HOH   HOH A . 
E 4 HOH   38  438 259 HOH   HOH A . 
E 4 HOH   39  439 250 HOH   HOH A . 
E 4 HOH   40  440 161 HOH   HOH A . 
E 4 HOH   41  441 189 HOH   HOH A . 
E 4 HOH   42  442 134 HOH   HOH A . 
E 4 HOH   43  443 203 HOH   HOH A . 
E 4 HOH   44  444 40  HOH   HOH A . 
E 4 HOH   45  445 85  HOH   HOH A . 
E 4 HOH   46  446 215 HOH   HOH A . 
E 4 HOH   47  447 196 HOH   HOH A . 
E 4 HOH   48  448 26  HOH   HOH A . 
E 4 HOH   49  449 129 HOH   HOH A . 
E 4 HOH   50  450 42  HOH   HOH A . 
E 4 HOH   51  451 182 HOH   HOH A . 
E 4 HOH   52  452 225 HOH   HOH A . 
E 4 HOH   53  453 147 HOH   HOH A . 
E 4 HOH   54  454 14  HOH   HOH A . 
E 4 HOH   55  455 113 HOH   HOH A . 
E 4 HOH   56  456 11  HOH   HOH A . 
E 4 HOH   57  457 10  HOH   HOH A . 
E 4 HOH   58  458 191 HOH   HOH A . 
E 4 HOH   59  459 112 HOH   HOH A . 
E 4 HOH   60  460 17  HOH   HOH A . 
E 4 HOH   61  461 71  HOH   HOH A . 
E 4 HOH   62  462 159 HOH   HOH A . 
E 4 HOH   63  463 119 HOH   HOH A . 
E 4 HOH   64  464 33  HOH   HOH A . 
E 4 HOH   65  465 125 HOH   HOH A . 
E 4 HOH   66  466 31  HOH   HOH A . 
E 4 HOH   67  467 184 HOH   HOH A . 
E 4 HOH   68  468 117 HOH   HOH A . 
E 4 HOH   69  469 172 HOH   HOH A . 
E 4 HOH   70  470 55  HOH   HOH A . 
E 4 HOH   71  471 81  HOH   HOH A . 
E 4 HOH   72  472 47  HOH   HOH A . 
E 4 HOH   73  473 194 HOH   HOH A . 
E 4 HOH   74  474 3   HOH   HOH A . 
E 4 HOH   75  475 51  HOH   HOH A . 
E 4 HOH   76  476 258 HOH   HOH A . 
E 4 HOH   77  477 139 HOH   HOH A . 
E 4 HOH   78  478 8   HOH   HOH A . 
E 4 HOH   79  479 162 HOH   HOH A . 
E 4 HOH   80  480 104 HOH   HOH A . 
E 4 HOH   81  481 255 HOH   HOH A . 
E 4 HOH   82  482 19  HOH   HOH A . 
E 4 HOH   83  483 186 HOH   HOH A . 
E 4 HOH   84  484 49  HOH   HOH A . 
E 4 HOH   85  485 155 HOH   HOH A . 
E 4 HOH   86  486 181 HOH   HOH A . 
E 4 HOH   87  487 96  HOH   HOH A . 
E 4 HOH   88  488 80  HOH   HOH A . 
E 4 HOH   89  489 18  HOH   HOH A . 
E 4 HOH   90  490 212 HOH   HOH A . 
E 4 HOH   91  491 169 HOH   HOH A . 
E 4 HOH   92  492 123 HOH   HOH A . 
E 4 HOH   93  493 77  HOH   HOH A . 
E 4 HOH   94  494 207 HOH   HOH A . 
E 4 HOH   95  495 217 HOH   HOH A . 
E 4 HOH   96  496 21  HOH   HOH A . 
E 4 HOH   97  497 128 HOH   HOH A . 
E 4 HOH   98  498 91  HOH   HOH A . 
E 4 HOH   99  499 44  HOH   HOH A . 
E 4 HOH   100 500 63  HOH   HOH A . 
E 4 HOH   101 501 20  HOH   HOH A . 
E 4 HOH   102 502 157 HOH   HOH A . 
E 4 HOH   103 503 36  HOH   HOH A . 
E 4 HOH   104 504 249 HOH   HOH A . 
E 4 HOH   105 505 93  HOH   HOH A . 
E 4 HOH   106 506 223 HOH   HOH A . 
E 4 HOH   107 507 15  HOH   HOH A . 
E 4 HOH   108 508 156 HOH   HOH A . 
E 4 HOH   109 509 58  HOH   HOH A . 
E 4 HOH   110 510 46  HOH   HOH A . 
E 4 HOH   111 511 69  HOH   HOH A . 
E 4 HOH   112 512 98  HOH   HOH A . 
E 4 HOH   113 513 64  HOH   HOH A . 
E 4 HOH   114 514 12  HOH   HOH A . 
E 4 HOH   115 515 94  HOH   HOH A . 
E 4 HOH   116 516 268 HOH   HOH A . 
E 4 HOH   117 517 23  HOH   HOH A . 
E 4 HOH   118 518 190 HOH   HOH A . 
E 4 HOH   119 519 78  HOH   HOH A . 
E 4 HOH   120 520 67  HOH   HOH A . 
E 4 HOH   121 521 262 HOH   HOH A . 
E 4 HOH   122 522 124 HOH   HOH A . 
E 4 HOH   123 523 219 HOH   HOH A . 
E 4 HOH   124 524 28  HOH   HOH A . 
E 4 HOH   125 525 83  HOH   HOH A . 
E 4 HOH   126 526 140 HOH   HOH A . 
E 4 HOH   127 527 13  HOH   HOH A . 
E 4 HOH   128 528 103 HOH   HOH A . 
E 4 HOH   129 529 132 HOH   HOH A . 
E 4 HOH   130 530 107 HOH   HOH A . 
E 4 HOH   131 531 220 HOH   HOH A . 
E 4 HOH   132 532 9   HOH   HOH A . 
E 4 HOH   133 533 218 HOH   HOH A . 
E 4 HOH   134 534 150 HOH   HOH A . 
E 4 HOH   135 535 213 HOH   HOH A . 
E 4 HOH   136 536 53  HOH   HOH A . 
E 4 HOH   137 537 271 HOH   HOH A . 
E 4 HOH   138 538 7   HOH   HOH A . 
E 4 HOH   139 539 158 HOH   HOH A . 
E 4 HOH   140 540 54  HOH   HOH A . 
E 4 HOH   141 541 204 HOH   HOH A . 
E 4 HOH   142 542 154 HOH   HOH A . 
E 4 HOH   143 543 165 HOH   HOH A . 
E 4 HOH   144 544 170 HOH   HOH A . 
E 4 HOH   145 545 171 HOH   HOH A . 
E 4 HOH   146 546 29  HOH   HOH A . 
E 4 HOH   147 547 222 HOH   HOH A . 
E 4 HOH   148 548 90  HOH   HOH A . 
E 4 HOH   149 549 41  HOH   HOH A . 
E 4 HOH   150 550 105 HOH   HOH A . 
E 4 HOH   151 551 50  HOH   HOH A . 
E 4 HOH   152 552 100 HOH   HOH A . 
E 4 HOH   153 553 138 HOH   HOH A . 
E 4 HOH   154 554 65  HOH   HOH A . 
E 4 HOH   155 555 224 HOH   HOH A . 
E 4 HOH   156 556 106 HOH   HOH A . 
E 4 HOH   157 557 136 HOH   HOH A . 
E 4 HOH   158 558 87  HOH   HOH A . 
E 4 HOH   159 559 45  HOH   HOH A . 
E 4 HOH   160 560 39  HOH   HOH A . 
E 4 HOH   161 561 120 HOH   HOH A . 
E 4 HOH   162 562 57  HOH   HOH A . 
E 4 HOH   163 563 133 HOH   HOH A . 
E 4 HOH   164 564 34  HOH   HOH A . 
E 4 HOH   165 565 109 HOH   HOH A . 
E 4 HOH   166 566 102 HOH   HOH A . 
E 4 HOH   167 567 108 HOH   HOH A . 
E 4 HOH   168 568 266 HOH   HOH A . 
E 4 HOH   169 569 121 HOH   HOH A . 
E 4 HOH   170 570 180 HOH   HOH A . 
E 4 HOH   171 571 48  HOH   HOH A . 
E 4 HOH   172 572 79  HOH   HOH A . 
E 4 HOH   173 573 95  HOH   HOH A . 
E 4 HOH   174 574 193 HOH   HOH A . 
E 4 HOH   175 575 221 HOH   HOH A . 
E 4 HOH   176 576 131 HOH   HOH A . 
E 4 HOH   177 577 5   HOH   HOH A . 
E 4 HOH   178 578 247 HOH   HOH A . 
E 4 HOH   179 579 6   HOH   HOH A . 
E 4 HOH   180 580 260 HOH   HOH A . 
E 4 HOH   181 581 61  HOH   HOH A . 
E 4 HOH   182 582 130 HOH   HOH A . 
E 4 HOH   183 583 4   HOH   HOH A . 
E 4 HOH   184 584 2   HOH   HOH A . 
E 4 HOH   185 585 143 HOH   HOH A . 
E 4 HOH   186 586 141 HOH   HOH A . 
E 4 HOH   187 587 201 HOH   HOH A . 
E 4 HOH   188 588 202 HOH   HOH A . 
E 4 HOH   189 589 62  HOH   HOH A . 
E 4 HOH   190 590 192 HOH   HOH A . 
E 4 HOH   191 591 89  HOH   HOH A . 
E 4 HOH   192 592 127 HOH   HOH A . 
E 4 HOH   193 593 200 HOH   HOH A . 
E 4 HOH   194 594 142 HOH   HOH A . 
E 4 HOH   195 595 216 HOH   HOH A . 
E 4 HOH   196 596 209 HOH   HOH A . 
E 4 HOH   197 597 252 HOH   HOH A . 
E 4 HOH   198 598 246 HOH   HOH A . 
E 4 HOH   199 599 227 HOH   HOH A . 
E 4 HOH   200 600 88  HOH   HOH A . 
E 4 HOH   201 601 263 HOH   HOH A . 
E 4 HOH   202 602 151 HOH   HOH A . 
E 4 HOH   203 603 148 HOH   HOH A . 
E 4 HOH   204 604 153 HOH   HOH A . 
E 4 HOH   205 605 97  HOH   HOH A . 
E 4 HOH   206 606 137 HOH   HOH A . 
E 4 HOH   207 607 228 HOH   HOH A . 
E 4 HOH   208 608 229 HOH   HOH A . 
E 4 HOH   209 609 233 HOH   HOH A . 
E 4 HOH   210 610 256 HOH   HOH A . 
E 4 HOH   211 611 70  HOH   HOH A . 
E 4 HOH   212 612 144 HOH   HOH A . 
E 4 HOH   213 613 74  HOH   HOH A . 
E 4 HOH   214 614 208 HOH   HOH A . 
E 4 HOH   215 615 163 HOH   HOH A . 
E 4 HOH   216 616 179 HOH   HOH A . 
E 4 HOH   217 617 242 HOH   HOH A . 
E 4 HOH   218 618 199 HOH   HOH A . 
E 4 HOH   219 619 149 HOH   HOH A . 
E 4 HOH   220 620 238 HOH   HOH A . 
E 4 HOH   221 621 22  HOH   HOH A . 
E 4 HOH   222 622 272 HOH   HOH A . 
E 4 HOH   223 623 92  HOH   HOH A . 
E 4 HOH   224 624 114 HOH   HOH A . 
E 4 HOH   225 625 264 HOH   HOH A . 
E 4 HOH   226 626 226 HOH   HOH A . 
E 4 HOH   227 627 254 HOH   HOH A . 
E 4 HOH   228 628 183 HOH   HOH A . 
E 4 HOH   229 629 145 HOH   HOH A . 
E 4 HOH   230 630 84  HOH   HOH A . 
E 4 HOH   231 631 30  HOH   HOH A . 
E 4 HOH   232 632 168 HOH   HOH A . 
E 4 HOH   233 633 236 HOH   HOH A . 
E 4 HOH   234 634 118 HOH   HOH A . 
E 4 HOH   235 635 73  HOH   HOH A . 
E 4 HOH   236 636 244 HOH   HOH A . 
E 4 HOH   237 637 116 HOH   HOH A . 
E 4 HOH   238 638 110 HOH   HOH A . 
E 4 HOH   239 639 122 HOH   HOH A . 
E 4 HOH   240 640 178 HOH   HOH A . 
E 4 HOH   241 641 241 HOH   HOH A . 
E 4 HOH   242 642 239 HOH   HOH A . 
E 4 HOH   243 643 206 HOH   HOH A . 
E 4 HOH   244 644 240 HOH   HOH A . 
E 4 HOH   245 645 273 HOH   HOH A . 
E 4 HOH   246 646 234 HOH   HOH A . 
E 4 HOH   247 647 248 HOH   HOH A . 
E 4 HOH   248 648 210 HOH   HOH A . 
E 4 HOH   249 649 135 HOH   HOH A . 
E 4 HOH   250 650 152 HOH   HOH A . 
E 4 HOH   251 651 230 HOH   HOH A . 
E 4 HOH   252 652 166 HOH   HOH A . 
E 4 HOH   253 653 75  HOH   HOH A . 
E 4 HOH   254 654 267 HOH   HOH A . 
E 4 HOH   255 655 111 HOH   HOH A . 
E 4 HOH   256 656 231 HOH   HOH A . 
E 4 HOH   257 657 197 HOH   HOH A . 
E 4 HOH   258 658 173 HOH   HOH A . 
E 4 HOH   259 659 232 HOH   HOH A . 
E 4 HOH   260 660 174 HOH   HOH A . 
E 4 HOH   261 661 245 HOH   HOH A . 
E 4 HOH   262 662 175 HOH   HOH A . 
E 4 HOH   263 663 265 HOH   HOH A . 
E 4 HOH   264 664 185 HOH   HOH A . 
E 4 HOH   265 665 146 HOH   HOH A . 
E 4 HOH   266 666 198 HOH   HOH A . 
E 4 HOH   267 667 237 HOH   HOH A . 
E 4 HOH   268 668 274 HOH   HOH A . 
E 4 HOH   269 669 195 HOH   HOH A . 
E 4 HOH   270 670 177 HOH   HOH A . 
E 4 HOH   271 671 176 HOH   HOH A . 
E 4 HOH   272 672 205 HOH   HOH A . 
E 4 HOH   273 673 235 HOH   HOH A . 
E 4 HOH   274 674 243 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 (24-FEB-2021)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AMoRE     ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.87 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H8F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.611 
_cell.length_a_esd                 ? 
_cell.length_b                     67.868 
_cell.length_b_esd                 ? 
_cell.length_c                     63.669 
_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                         9H8F 
_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                   9H8F 
_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             2.57 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.10 
_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    
'6.5 % PEG8000, 0.1 M PCTP pH 8.5, co-crystallised with 1 mM inhibitor, cryoprotected with 20 % ethylene glycol' 
_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                                       9H8F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.393 
_reflns.d_resolution_low                               63.44 
_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                                     39592 
_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                           59.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_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                                0.045 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.038 
_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                                    1.393 
_reflns_shell.d_res_low                                     1.542 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6834 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1980 
_reflns_shell.percent_possible_obs                          11.4 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.661 
_reflns_shell.pdbx_Rpim_I_all                               0.349 
_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                                  0.560 
_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]                            -0.79710 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.22540 
_refine.aniso_B[2][2]                            -0.29810 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            1.09520 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.05 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.695 
_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                                 9H8F 
_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                            1.393 
_refine.ls_d_res_low                             63.44 
_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                     39578 
_refine.ls_number_reflns_R_free                  1953 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    59.5 
_refine.ls_percent_reflns_R_free                 4.930 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2033 
_refine.ls_R_factor_R_free                       0.2463 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2011 
_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   0.104 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.106 
_refine.pdbx_overall_SU_R_Blow_DPI               0.102 
_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             0.099 
_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                        9H8F 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.21 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.393 
_refine_hist.d_res_low                        63.44 
_refine_hist.number_atoms_solvent             274 
_refine_hist.number_atoms_total               2585 
_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         42 
_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' ? 0.008 ? 2361 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.90  ? 3193 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 831  ? 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' ? ?     ? 2361 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.43  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.98 ? ?    ? 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' ? ?     ? 2354 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.393 
_refine_ls_shell.d_res_low                        1.49 
_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             742 
_refine_ls_shell.percent_reflns_obs               6.61 
_refine_ls_shell.percent_reflns_R_free            6.31 
_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                  0.2544 
_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                  0.2412 
# 
_struct.entry_id                     9H8F 
_struct.title                        
'Crystal structure of HPK1 T165E/S171E in complex with pyrazine carboxamide inhibitor AZ3246 (compound 24)' 
_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        9H8F 
_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 ? 
D N N 3 ? 
E N N 4 ? 
# 
_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              9H8F 
_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 9H8F GLY A 1   ? UNP Q92918 ?   ?   'expression tag'      0   1 
1 9H8F SER A 2   ? UNP Q92918 ?   ?   'expression tag'      1   2 
1 9H8F GLU A 166 ? UNP Q92918 THR 165 'engineered mutation' 165 3 
1 9H8F 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)' 1240  ? 
1 MORE         4     ? 
1 'SSA (A^2)'  13890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 GLU A 240 ? TRP A 244 ? GLU A 239 TRP A 243 5 ? 5  
HELX_P HELX_P12 AB3 SER A 245 ? LEU A 256 ? SER A 244 LEU A 255 1 ? 12 
HELX_P HELX_P13 AB4 SER A 259 ? ARG A 263 ? SER A 258 ARG A 262 5 ? 5  
HELX_P HELX_P14 AB5 SER A 265 ? LEU A 270 ? SER A 264 LEU A 269 1 ? 6  
HELX_P HELX_P15 AB6 HIS A 272 ? GLN A 277 ? HIS A 271 GLN A 276 1 ? 6  
HELX_P HELX_P16 AB7 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 GLY A 80  ? N GLY A 79  O CYS A 91  ? O CYS A 90  
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                   9H8F 
_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 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     530 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     530 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              1.26 
# 
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  ? ? -110.37 -161.74 
2 1 VAL A 105 ? ? -121.88 -51.80  
3 1 ASP A 137 ? ? -145.97 31.02   
4 1 GLN A 161 ? ? -84.77  44.10   
5 1 THR A 175 ? ? -161.32 73.17   
6 1 ALA A 185 ? ? -79.37  44.62   
7 1 LEU A 255 ? ? -95.09  38.01   
# 
_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         16.7982 
_pdbx_refine_tls.origin_y         -0.0579 
_pdbx_refine_tls.origin_z         11.4767 
_pdbx_refine_tls.T[1][1]          -0.0257 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0244 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0071 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0297 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0076 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0054 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.9605 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0348 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2780 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.2180 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0230 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.8502 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0630 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1246 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0093 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1723 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0540 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0366 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0748 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0663 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0089 
_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 
A1ITB C1   C Y N 1   
A1ITB C2   C Y N 2   
A1ITB C3   C Y N 3   
A1ITB N6   N Y N 4   
A1ITB C7   C Y N 5   
A1ITB C8   C Y N 6   
A1ITB C9   C Y N 7   
A1ITB C10  C N N 8   
A1ITB C11  C N N 9   
A1ITB C12  C N N 10  
A1ITB C13  C Y N 11  
A1ITB C14  C Y N 12  
A1ITB C15  C Y N 13  
A1ITB C16  C Y N 14  
A1ITB C19  C N N 15  
A1ITB C20  C N N 16  
A1ITB O    O N N 17  
A1ITB N8   N N N 18  
A1ITB N3   N Y N 19  
A1ITB C17  C Y N 20  
A1ITB C18  C Y N 21  
A1ITB N7   N Y N 22  
A1ITB N5   N Y N 23  
A1ITB N4   N Y N 24  
A1ITB C6   C Y N 25  
A1ITB N2   N N N 26  
A1ITB N    N Y N 27  
A1ITB C4   C N N 28  
A1ITB C5   C N N 29  
A1ITB F2   F N N 30  
A1ITB F1   F N N 31  
A1ITB F    F N N 32  
A1ITB N1   N Y N 33  
A1ITB C    C N N 34  
A1ITB H1   H N N 35  
A1ITB H2   H N N 36  
A1ITB H3   H N N 37  
A1ITB H4   H N N 38  
A1ITB H5   H N N 39  
A1ITB H6   H N N 40  
A1ITB H7   H N N 41  
A1ITB H8   H N N 42  
A1ITB H9   H N N 43  
A1ITB H10  H N N 44  
A1ITB H11  H N N 45  
A1ITB H12  H N N 46  
A1ITB H13  H N N 47  
A1ITB H14  H N N 48  
A1ITB H15  H N N 49  
A1ITB H16  H N N 50  
A1ITB H17  H N N 51  
A1ITB H18  H N N 52  
A1ITB H19  H N N 53  
A1ITB H20  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
EDO   C1   C N N 142 
EDO   O1   O N N 143 
EDO   C2   C N N 144 
EDO   O2   O N N 145 
EDO   H11  H N N 146 
EDO   H12  H N N 147 
EDO   HO1  H N N 148 
EDO   H21  H N N 149 
EDO   H22  H N N 150 
EDO   HO2  H N N 151 
GLN   N    N N N 152 
GLN   CA   C N S 153 
GLN   C    C N N 154 
GLN   O    O N N 155 
GLN   CB   C N N 156 
GLN   CG   C N N 157 
GLN   CD   C N N 158 
GLN   OE1  O N N 159 
GLN   NE2  N N N 160 
GLN   OXT  O N N 161 
GLN   H    H N N 162 
GLN   H2   H N N 163 
GLN   HA   H N N 164 
GLN   HB2  H N N 165 
GLN   HB3  H N N 166 
GLN   HG2  H N N 167 
GLN   HG3  H N N 168 
GLN   HE21 H N N 169 
GLN   HE22 H N N 170 
GLN   HXT  H N N 171 
GLU   N    N N N 172 
GLU   CA   C N S 173 
GLU   C    C N N 174 
GLU   O    O N N 175 
GLU   CB   C N N 176 
GLU   CG   C N N 177 
GLU   CD   C N N 178 
GLU   OE1  O N N 179 
GLU   OE2  O N N 180 
GLU   OXT  O N N 181 
GLU   H    H N N 182 
GLU   H2   H N N 183 
GLU   HA   H N N 184 
GLU   HB2  H N N 185 
GLU   HB3  H N N 186 
GLU   HG2  H N N 187 
GLU   HG3  H N N 188 
GLU   HE2  H N N 189 
GLU   HXT  H N N 190 
GLY   N    N N N 191 
GLY   CA   C N N 192 
GLY   C    C N N 193 
GLY   O    O N N 194 
GLY   OXT  O N N 195 
GLY   H    H N N 196 
GLY   H2   H N N 197 
GLY   HA2  H N N 198 
GLY   HA3  H N N 199 
GLY   HXT  H N N 200 
HIS   N    N N N 201 
HIS   CA   C N S 202 
HIS   C    C N N 203 
HIS   O    O N N 204 
HIS   CB   C N N 205 
HIS   CG   C Y N 206 
HIS   ND1  N Y N 207 
HIS   CD2  C Y N 208 
HIS   CE1  C Y N 209 
HIS   NE2  N Y N 210 
HIS   OXT  O N N 211 
HIS   H    H N N 212 
HIS   H2   H N N 213 
HIS   HA   H N N 214 
HIS   HB2  H N N 215 
HIS   HB3  H N N 216 
HIS   HD1  H N N 217 
HIS   HD2  H N N 218 
HIS   HE1  H N N 219 
HIS   HE2  H N N 220 
HIS   HXT  H N N 221 
HOH   O    O N N 222 
HOH   H1   H N N 223 
HOH   H2   H N N 224 
ILE   N    N N N 225 
ILE   CA   C N S 226 
ILE   C    C N N 227 
ILE   O    O N N 228 
ILE   CB   C N S 229 
ILE   CG1  C N N 230 
ILE   CG2  C N N 231 
ILE   CD1  C N N 232 
ILE   OXT  O N N 233 
ILE   H    H N N 234 
ILE   H2   H N N 235 
ILE   HA   H N N 236 
ILE   HB   H N N 237 
ILE   HG12 H N N 238 
ILE   HG13 H N N 239 
ILE   HG21 H N N 240 
ILE   HG22 H N N 241 
ILE   HG23 H N N 242 
ILE   HD11 H N N 243 
ILE   HD12 H N N 244 
ILE   HD13 H N N 245 
ILE   HXT  H N N 246 
LEU   N    N N N 247 
LEU   CA   C N S 248 
LEU   C    C N N 249 
LEU   O    O N N 250 
LEU   CB   C N N 251 
LEU   CG   C N N 252 
LEU   CD1  C N N 253 
LEU   CD2  C N N 254 
LEU   OXT  O N N 255 
LEU   H    H N N 256 
LEU   H2   H N N 257 
LEU   HA   H N N 258 
LEU   HB2  H N N 259 
LEU   HB3  H N N 260 
LEU   HG   H N N 261 
LEU   HD11 H N N 262 
LEU   HD12 H N N 263 
LEU   HD13 H N N 264 
LEU   HD21 H N N 265 
LEU   HD22 H N N 266 
LEU   HD23 H N N 267 
LEU   HXT  H N N 268 
LYS   N    N N N 269 
LYS   CA   C N S 270 
LYS   C    C N N 271 
LYS   O    O N N 272 
LYS   CB   C N N 273 
LYS   CG   C N N 274 
LYS   CD   C N N 275 
LYS   CE   C N N 276 
LYS   NZ   N N N 277 
LYS   OXT  O N N 278 
LYS   H    H N N 279 
LYS   H2   H N N 280 
LYS   HA   H N N 281 
LYS   HB2  H N N 282 
LYS   HB3  H N N 283 
LYS   HG2  H N N 284 
LYS   HG3  H N N 285 
LYS   HD2  H N N 286 
LYS   HD3  H N N 287 
LYS   HE2  H N N 288 
LYS   HE3  H N N 289 
LYS   HZ1  H N N 290 
LYS   HZ2  H N N 291 
LYS   HZ3  H N N 292 
LYS   HXT  H N N 293 
MET   N    N N N 294 
MET   CA   C N S 295 
MET   C    C N N 296 
MET   O    O N N 297 
MET   CB   C N N 298 
MET   CG   C N N 299 
MET   SD   S N N 300 
MET   CE   C N N 301 
MET   OXT  O N N 302 
MET   H    H N N 303 
MET   H2   H N N 304 
MET   HA   H N N 305 
MET   HB2  H N N 306 
MET   HB3  H N N 307 
MET   HG2  H N N 308 
MET   HG3  H N N 309 
MET   HE1  H N N 310 
MET   HE2  H N N 311 
MET   HE3  H N N 312 
MET   HXT  H N N 313 
PHE   N    N N N 314 
PHE   CA   C N S 315 
PHE   C    C N N 316 
PHE   O    O N N 317 
PHE   CB   C N N 318 
PHE   CG   C Y N 319 
PHE   CD1  C Y N 320 
PHE   CD2  C Y N 321 
PHE   CE1  C Y N 322 
PHE   CE2  C Y N 323 
PHE   CZ   C Y N 324 
PHE   OXT  O N N 325 
PHE   H    H N N 326 
PHE   H2   H N N 327 
PHE   HA   H N N 328 
PHE   HB2  H N N 329 
PHE   HB3  H N N 330 
PHE   HD1  H N N 331 
PHE   HD2  H N N 332 
PHE   HE1  H N N 333 
PHE   HE2  H N N 334 
PHE   HZ   H N N 335 
PHE   HXT  H N N 336 
PRO   N    N N N 337 
PRO   CA   C N S 338 
PRO   C    C N N 339 
PRO   O    O N N 340 
PRO   CB   C N N 341 
PRO   CG   C N N 342 
PRO   CD   C N N 343 
PRO   OXT  O N N 344 
PRO   H    H N N 345 
PRO   HA   H N N 346 
PRO   HB2  H N N 347 
PRO   HB3  H N N 348 
PRO   HG2  H N N 349 
PRO   HG3  H N N 350 
PRO   HD2  H N N 351 
PRO   HD3  H N N 352 
PRO   HXT  H N N 353 
SER   N    N N N 354 
SER   CA   C N S 355 
SER   C    C N N 356 
SER   O    O N N 357 
SER   CB   C N N 358 
SER   OG   O N N 359 
SER   OXT  O N N 360 
SER   H    H N N 361 
SER   H2   H N N 362 
SER   HA   H N N 363 
SER   HB2  H N N 364 
SER   HB3  H N N 365 
SER   HG   H N N 366 
SER   HXT  H N N 367 
THR   N    N N N 368 
THR   CA   C N S 369 
THR   C    C N N 370 
THR   O    O N N 371 
THR   CB   C N R 372 
THR   OG1  O N N 373 
THR   CG2  C N N 374 
THR   OXT  O N N 375 
THR   H    H N N 376 
THR   H2   H N N 377 
THR   HA   H N N 378 
THR   HB   H N N 379 
THR   HG1  H N N 380 
THR   HG21 H N N 381 
THR   HG22 H N N 382 
THR   HG23 H N N 383 
THR   HXT  H N N 384 
TRP   N    N N N 385 
TRP   CA   C N S 386 
TRP   C    C N N 387 
TRP   O    O N N 388 
TRP   CB   C N N 389 
TRP   CG   C Y N 390 
TRP   CD1  C Y N 391 
TRP   CD2  C Y N 392 
TRP   NE1  N Y N 393 
TRP   CE2  C Y N 394 
TRP   CE3  C Y N 395 
TRP   CZ2  C Y N 396 
TRP   CZ3  C Y N 397 
TRP   CH2  C Y N 398 
TRP   OXT  O N N 399 
TRP   H    H N N 400 
TRP   H2   H N N 401 
TRP   HA   H N N 402 
TRP   HB2  H N N 403 
TRP   HB3  H N N 404 
TRP   HD1  H N N 405 
TRP   HE1  H N N 406 
TRP   HE3  H N N 407 
TRP   HZ2  H N N 408 
TRP   HZ3  H N N 409 
TRP   HH2  H N N 410 
TRP   HXT  H N N 411 
TYR   N    N N N 412 
TYR   CA   C N S 413 
TYR   C    C N N 414 
TYR   O    O N N 415 
TYR   CB   C N N 416 
TYR   CG   C Y N 417 
TYR   CD1  C Y N 418 
TYR   CD2  C Y N 419 
TYR   CE1  C Y N 420 
TYR   CE2  C Y N 421 
TYR   CZ   C Y N 422 
TYR   OH   O N N 423 
TYR   OXT  O N N 424 
TYR   H    H N N 425 
TYR   H2   H N N 426 
TYR   HA   H N N 427 
TYR   HB2  H N N 428 
TYR   HB3  H N N 429 
TYR   HD1  H N N 430 
TYR   HD2  H N N 431 
TYR   HE1  H N N 432 
TYR   HE2  H N N 433 
TYR   HH   H N N 434 
TYR   HXT  H N N 435 
VAL   N    N N N 436 
VAL   CA   C N S 437 
VAL   C    C N N 438 
VAL   O    O N N 439 
VAL   CB   C N N 440 
VAL   CG1  C N N 441 
VAL   CG2  C N N 442 
VAL   OXT  O N N 443 
VAL   H    H N N 444 
VAL   H2   H N N 445 
VAL   HA   H N N 446 
VAL   HB   H N N 447 
VAL   HG11 H N N 448 
VAL   HG12 H N N 449 
VAL   HG13 H N N 450 
VAL   HG21 H N N 451 
VAL   HG22 H N N 452 
VAL   HG23 H N N 453 
VAL   HXT  H N N 454 
# 
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 
A1ITB C19 N7   sing N N 1   
A1ITB C18 N7   sing Y N 2   
A1ITB C18 N6   doub Y N 3   
A1ITB N7  C16  sing Y N 4   
A1ITB F1  C5   sing N N 5   
A1ITB N6  C17  sing Y N 6   
A1ITB C12 C10  sing N N 7   
A1ITB C12 C11  sing N N 8   
A1ITB C16 C17  doub Y N 9   
A1ITB C16 C15  sing Y N 10  
A1ITB F2  C5   sing N N 11  
A1ITB C4  C5   sing N N 12  
A1ITB C4  N    sing N N 13  
A1ITB C5  F    sing N N 14  
A1ITB C17 C13  sing Y N 15  
A1ITB C10 C11  sing N N 16  
A1ITB C10 C9   sing N N 17  
A1ITB C15 N5   doub Y N 18  
A1ITB N   C3   sing Y N 19  
A1ITB N   N1   sing Y N 20  
A1ITB C3  C2   doub Y N 21  
A1ITB C9  N4   doub Y N 22  
A1ITB C9  C8   sing Y N 23  
A1ITB C13 C8   sing N N 24  
A1ITB C13 C14  doub Y N 25  
A1ITB N4  C6   sing Y N 26  
A1ITB C8  N3   doub Y N 27  
A1ITB N5  C14  sing Y N 28  
A1ITB N1  C1   doub Y N 29  
A1ITB C2  C1   sing Y N 30  
A1ITB C2  N2   sing N N 31  
A1ITB C6  N2   sing N N 32  
A1ITB C6  C7   doub Y N 33  
A1ITB N3  C7   sing Y N 34  
A1ITB C1  C    sing N N 35  
A1ITB C7  C20  sing N N 36  
A1ITB C20 N8   sing N N 37  
A1ITB C20 O    doub N N 38  
A1ITB C3  H1   sing N N 39  
A1ITB C10 H2   sing N N 40  
A1ITB C11 H3   sing N N 41  
A1ITB C11 H4   sing N N 42  
A1ITB C12 H5   sing N N 43  
A1ITB C12 H6   sing N N 44  
A1ITB C14 H7   sing N N 45  
A1ITB C15 H8   sing N N 46  
A1ITB C19 H9   sing N N 47  
A1ITB C19 H10  sing N N 48  
A1ITB C19 H11  sing N N 49  
A1ITB N8  H12  sing N N 50  
A1ITB N8  H13  sing N N 51  
A1ITB C18 H14  sing N N 52  
A1ITB N2  H15  sing N N 53  
A1ITB C4  H16  sing N N 54  
A1ITB C4  H17  sing N N 55  
A1ITB C   H18  sing N N 56  
A1ITB C   H19  sing N N 57  
A1ITB C   H20  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
EDO   C1  O1   sing N N 141 
EDO   C1  C2   sing N N 142 
EDO   C1  H11  sing N N 143 
EDO   C1  H12  sing N N 144 
EDO   O1  HO1  sing N N 145 
EDO   C2  O2   sing N N 146 
EDO   C2  H21  sing N N 147 
EDO   C2  H22  sing N N 148 
EDO   O2  HO2  sing N N 149 
GLN   N   CA   sing N N 150 
GLN   N   H    sing N N 151 
GLN   N   H2   sing N N 152 
GLN   CA  C    sing N N 153 
GLN   CA  CB   sing N N 154 
GLN   CA  HA   sing N N 155 
GLN   C   O    doub N N 156 
GLN   C   OXT  sing N N 157 
GLN   CB  CG   sing N N 158 
GLN   CB  HB2  sing N N 159 
GLN   CB  HB3  sing N N 160 
GLN   CG  CD   sing N N 161 
GLN   CG  HG2  sing N N 162 
GLN   CG  HG3  sing N N 163 
GLN   CD  OE1  doub N N 164 
GLN   CD  NE2  sing N N 165 
GLN   NE2 HE21 sing N N 166 
GLN   NE2 HE22 sing N N 167 
GLN   OXT HXT  sing N N 168 
GLU   N   CA   sing N N 169 
GLU   N   H    sing N N 170 
GLU   N   H2   sing N N 171 
GLU   CA  C    sing N N 172 
GLU   CA  CB   sing N N 173 
GLU   CA  HA   sing N N 174 
GLU   C   O    doub N N 175 
GLU   C   OXT  sing N N 176 
GLU   CB  CG   sing N N 177 
GLU   CB  HB2  sing N N 178 
GLU   CB  HB3  sing N N 179 
GLU   CG  CD   sing N N 180 
GLU   CG  HG2  sing N N 181 
GLU   CG  HG3  sing N N 182 
GLU   CD  OE1  doub N N 183 
GLU   CD  OE2  sing N N 184 
GLU   OE2 HE2  sing N N 185 
GLU   OXT HXT  sing N N 186 
GLY   N   CA   sing N N 187 
GLY   N   H    sing N N 188 
GLY   N   H2   sing N N 189 
GLY   CA  C    sing N N 190 
GLY   CA  HA2  sing N N 191 
GLY   CA  HA3  sing N N 192 
GLY   C   O    doub N N 193 
GLY   C   OXT  sing N N 194 
GLY   OXT HXT  sing N N 195 
HIS   N   CA   sing N N 196 
HIS   N   H    sing N N 197 
HIS   N   H2   sing N N 198 
HIS   CA  C    sing N N 199 
HIS   CA  CB   sing N N 200 
HIS   CA  HA   sing N N 201 
HIS   C   O    doub N N 202 
HIS   C   OXT  sing N N 203 
HIS   CB  CG   sing N N 204 
HIS   CB  HB2  sing N N 205 
HIS   CB  HB3  sing N N 206 
HIS   CG  ND1  sing Y N 207 
HIS   CG  CD2  doub Y N 208 
HIS   ND1 CE1  doub Y N 209 
HIS   ND1 HD1  sing N N 210 
HIS   CD2 NE2  sing Y N 211 
HIS   CD2 HD2  sing N N 212 
HIS   CE1 NE2  sing Y N 213 
HIS   CE1 HE1  sing N N 214 
HIS   NE2 HE2  sing N N 215 
HIS   OXT HXT  sing N N 216 
HOH   O   H1   sing N N 217 
HOH   O   H2   sing N N 218 
ILE   N   CA   sing N N 219 
ILE   N   H    sing N N 220 
ILE   N   H2   sing N N 221 
ILE   CA  C    sing N N 222 
ILE   CA  CB   sing N N 223 
ILE   CA  HA   sing N N 224 
ILE   C   O    doub N N 225 
ILE   C   OXT  sing N N 226 
ILE   CB  CG1  sing N N 227 
ILE   CB  CG2  sing N N 228 
ILE   CB  HB   sing N N 229 
ILE   CG1 CD1  sing N N 230 
ILE   CG1 HG12 sing N N 231 
ILE   CG1 HG13 sing N N 232 
ILE   CG2 HG21 sing N N 233 
ILE   CG2 HG22 sing N N 234 
ILE   CG2 HG23 sing N N 235 
ILE   CD1 HD11 sing N N 236 
ILE   CD1 HD12 sing N N 237 
ILE   CD1 HD13 sing N N 238 
ILE   OXT HXT  sing N N 239 
LEU   N   CA   sing N N 240 
LEU   N   H    sing N N 241 
LEU   N   H2   sing N N 242 
LEU   CA  C    sing N N 243 
LEU   CA  CB   sing N N 244 
LEU   CA  HA   sing N N 245 
LEU   C   O    doub N N 246 
LEU   C   OXT  sing N N 247 
LEU   CB  CG   sing N N 248 
LEU   CB  HB2  sing N N 249 
LEU   CB  HB3  sing N N 250 
LEU   CG  CD1  sing N N 251 
LEU   CG  CD2  sing N N 252 
LEU   CG  HG   sing N N 253 
LEU   CD1 HD11 sing N N 254 
LEU   CD1 HD12 sing N N 255 
LEU   CD1 HD13 sing N N 256 
LEU   CD2 HD21 sing N N 257 
LEU   CD2 HD22 sing N N 258 
LEU   CD2 HD23 sing N N 259 
LEU   OXT HXT  sing N N 260 
LYS   N   CA   sing N N 261 
LYS   N   H    sing N N 262 
LYS   N   H2   sing N N 263 
LYS   CA  C    sing N N 264 
LYS   CA  CB   sing N N 265 
LYS   CA  HA   sing N N 266 
LYS   C   O    doub N N 267 
LYS   C   OXT  sing N N 268 
LYS   CB  CG   sing N N 269 
LYS   CB  HB2  sing N N 270 
LYS   CB  HB3  sing N N 271 
LYS   CG  CD   sing N N 272 
LYS   CG  HG2  sing N N 273 
LYS   CG  HG3  sing N N 274 
LYS   CD  CE   sing N N 275 
LYS   CD  HD2  sing N N 276 
LYS   CD  HD3  sing N N 277 
LYS   CE  NZ   sing N N 278 
LYS   CE  HE2  sing N N 279 
LYS   CE  HE3  sing N N 280 
LYS   NZ  HZ1  sing N N 281 
LYS   NZ  HZ2  sing N N 282 
LYS   NZ  HZ3  sing N N 283 
LYS   OXT HXT  sing N N 284 
MET   N   CA   sing N N 285 
MET   N   H    sing N N 286 
MET   N   H2   sing N N 287 
MET   CA  C    sing N N 288 
MET   CA  CB   sing N N 289 
MET   CA  HA   sing N N 290 
MET   C   O    doub N N 291 
MET   C   OXT  sing N N 292 
MET   CB  CG   sing N N 293 
MET   CB  HB2  sing N N 294 
MET   CB  HB3  sing N N 295 
MET   CG  SD   sing N N 296 
MET   CG  HG2  sing N N 297 
MET   CG  HG3  sing N N 298 
MET   SD  CE   sing N N 299 
MET   CE  HE1  sing N N 300 
MET   CE  HE2  sing N N 301 
MET   CE  HE3  sing N N 302 
MET   OXT HXT  sing N N 303 
PHE   N   CA   sing N N 304 
PHE   N   H    sing N N 305 
PHE   N   H2   sing N N 306 
PHE   CA  C    sing N N 307 
PHE   CA  CB   sing N N 308 
PHE   CA  HA   sing N N 309 
PHE   C   O    doub N N 310 
PHE   C   OXT  sing N N 311 
PHE   CB  CG   sing N N 312 
PHE   CB  HB2  sing N N 313 
PHE   CB  HB3  sing N N 314 
PHE   CG  CD1  doub Y N 315 
PHE   CG  CD2  sing Y N 316 
PHE   CD1 CE1  sing Y N 317 
PHE   CD1 HD1  sing N N 318 
PHE   CD2 CE2  doub Y N 319 
PHE   CD2 HD2  sing N N 320 
PHE   CE1 CZ   doub Y N 321 
PHE   CE1 HE1  sing N N 322 
PHE   CE2 CZ   sing Y N 323 
PHE   CE2 HE2  sing N N 324 
PHE   CZ  HZ   sing N N 325 
PHE   OXT HXT  sing N N 326 
PRO   N   CA   sing N N 327 
PRO   N   CD   sing N N 328 
PRO   N   H    sing N N 329 
PRO   CA  C    sing N N 330 
PRO   CA  CB   sing N N 331 
PRO   CA  HA   sing N N 332 
PRO   C   O    doub N N 333 
PRO   C   OXT  sing N N 334 
PRO   CB  CG   sing N N 335 
PRO   CB  HB2  sing N N 336 
PRO   CB  HB3  sing N N 337 
PRO   CG  CD   sing N N 338 
PRO   CG  HG2  sing N N 339 
PRO   CG  HG3  sing N N 340 
PRO   CD  HD2  sing N N 341 
PRO   CD  HD3  sing N N 342 
PRO   OXT HXT  sing N N 343 
SER   N   CA   sing N N 344 
SER   N   H    sing N N 345 
SER   N   H2   sing N N 346 
SER   CA  C    sing N N 347 
SER   CA  CB   sing N N 348 
SER   CA  HA   sing N N 349 
SER   C   O    doub N N 350 
SER   C   OXT  sing N N 351 
SER   CB  OG   sing N N 352 
SER   CB  HB2  sing N N 353 
SER   CB  HB3  sing N N 354 
SER   OG  HG   sing N N 355 
SER   OXT HXT  sing N N 356 
THR   N   CA   sing N N 357 
THR   N   H    sing N N 358 
THR   N   H2   sing N N 359 
THR   CA  C    sing N N 360 
THR   CA  CB   sing N N 361 
THR   CA  HA   sing N N 362 
THR   C   O    doub N N 363 
THR   C   OXT  sing N N 364 
THR   CB  OG1  sing N N 365 
THR   CB  CG2  sing N N 366 
THR   CB  HB   sing N N 367 
THR   OG1 HG1  sing N N 368 
THR   CG2 HG21 sing N N 369 
THR   CG2 HG22 sing N N 370 
THR   CG2 HG23 sing N N 371 
THR   OXT HXT  sing N N 372 
TRP   N   CA   sing N N 373 
TRP   N   H    sing N N 374 
TRP   N   H2   sing N N 375 
TRP   CA  C    sing N N 376 
TRP   CA  CB   sing N N 377 
TRP   CA  HA   sing N N 378 
TRP   C   O    doub N N 379 
TRP   C   OXT  sing N N 380 
TRP   CB  CG   sing N N 381 
TRP   CB  HB2  sing N N 382 
TRP   CB  HB3  sing N N 383 
TRP   CG  CD1  doub Y N 384 
TRP   CG  CD2  sing Y N 385 
TRP   CD1 NE1  sing Y N 386 
TRP   CD1 HD1  sing N N 387 
TRP   CD2 CE2  doub Y N 388 
TRP   CD2 CE3  sing Y N 389 
TRP   NE1 CE2  sing Y N 390 
TRP   NE1 HE1  sing N N 391 
TRP   CE2 CZ2  sing Y N 392 
TRP   CE3 CZ3  doub Y N 393 
TRP   CE3 HE3  sing N N 394 
TRP   CZ2 CH2  doub Y N 395 
TRP   CZ2 HZ2  sing N N 396 
TRP   CZ3 CH2  sing Y N 397 
TRP   CZ3 HZ3  sing N N 398 
TRP   CH2 HH2  sing N N 399 
TRP   OXT HXT  sing N N 400 
TYR   N   CA   sing N N 401 
TYR   N   H    sing N N 402 
TYR   N   H2   sing N N 403 
TYR   CA  C    sing N N 404 
TYR   CA  CB   sing N N 405 
TYR   CA  HA   sing N N 406 
TYR   C   O    doub N N 407 
TYR   C   OXT  sing N N 408 
TYR   CB  CG   sing N N 409 
TYR   CB  HB2  sing N N 410 
TYR   CB  HB3  sing N N 411 
TYR   CG  CD1  doub Y N 412 
TYR   CG  CD2  sing Y N 413 
TYR   CD1 CE1  sing Y N 414 
TYR   CD1 HD1  sing N N 415 
TYR   CD2 CE2  doub Y N 416 
TYR   CD2 HD2  sing N N 417 
TYR   CE1 CZ   doub Y N 418 
TYR   CE1 HE1  sing N N 419 
TYR   CE2 CZ   sing Y N 420 
TYR   CE2 HE2  sing N N 421 
TYR   CZ  OH   sing N N 422 
TYR   OH  HH   sing N N 423 
TYR   OXT HXT  sing N N 424 
VAL   N   CA   sing N N 425 
VAL   N   H    sing N N 426 
VAL   N   H2   sing N N 427 
VAL   CA  C    sing N N 428 
VAL   CA  CB   sing N N 429 
VAL   CA  HA   sing N N 430 
VAL   C   O    doub N N 431 
VAL   C   OXT  sing N N 432 
VAL   CB  CG1  sing N N 433 
VAL   CB  CG2  sing N N 434 
VAL   CB  HB   sing N N 435 
VAL   CG1 HG11 sing N N 436 
VAL   CG1 HG12 sing N N 437 
VAL   CG1 HG13 sing N N 438 
VAL   CG2 HG21 sing N N 439 
VAL   CG2 HG22 sing N N 440 
VAL   CG2 HG23 sing N N 441 
VAL   OXT HXT  sing N N 442 
# 
_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                    9H8F 
_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]   0.012721 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001084 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014734 
_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]   0.015763 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 8   ? 5.216   -2.915  34.829  1.00 50.18 ? 7   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 8   ? 5.797   -2.802  33.497  1.00 50.83 ? 7   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 8   ? 5.692   -1.364  32.972  1.00 50.07 ? 7   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 8   ? 6.661   -0.832  32.430  1.00 50.70 ? 7   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 8   ? 5.116   -3.785  32.527  1.00 53.87 ? 7   ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 8   ? 5.253   -5.239  32.930  1.00 60.36 ? 7   ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 8   ? 4.818   -5.589  34.051  1.00 61.63 ? 7   ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 8   ? 5.789   -6.030  32.123  1.00 63.32 ? 7   ASP   A OD2 1 
ATOM   9    N N   . ILE   A 1 9   ? 4.517   -0.739  33.123  1.00 48.47 ? 8   ILE   A N   1 
ATOM   10   C CA  . ILE   A 1 9   ? 4.300   0.634   32.671  1.00 47.18 ? 8   ILE   A CA  1 
ATOM   11   C C   . ILE   A 1 9   ? 3.993   1.487   33.888  1.00 45.69 ? 8   ILE   A C   1 
ATOM   12   O O   . ILE   A 1 9   ? 3.087   1.144   34.648  1.00 45.18 ? 8   ILE   A O   1 
ATOM   13   C CB  . ILE   A 1 9   ? 3.130   0.724   31.659  1.00 47.73 ? 8   ILE   A CB  1 
ATOM   14   C CG1 . ILE   A 1 9   ? 3.229   -0.340  30.557  1.00 48.93 ? 8   ILE   A CG1 1 
ATOM   15   C CG2 . ILE   A 1 9   ? 3.009   2.137   31.085  1.00 48.28 ? 8   ILE   A CG2 1 
ATOM   16   C CD1 . ILE   A 1 9   ? 2.004   -0.407  29.649  1.00 50.45 ? 8   ILE   A CD1 1 
ATOM   17   N N   . PHE   A 1 10  ? 4.720   2.597   34.075  1.00 44.28 ? 9   PHE   A N   1 
ATOM   18   C CA  . PHE   A 1 10  ? 4.471   3.474   35.215  1.00 43.56 ? 9   PHE   A CA  1 
ATOM   19   C C   . PHE   A 1 10  ? 3.413   4.517   34.871  1.00 41.90 ? 9   PHE   A C   1 
ATOM   20   O O   . PHE   A 1 10  ? 3.522   5.179   33.840  1.00 41.65 ? 9   PHE   A O   1 
ATOM   21   C CB  . PHE   A 1 10  ? 5.763   4.190   35.648  1.00 44.08 ? 9   PHE   A CB  1 
ATOM   22   C CG  . PHE   A 1 10  ? 6.859   3.320   36.220  1.00 45.35 ? 9   PHE   A CG  1 
ATOM   23   C CD1 . PHE   A 1 10  ? 6.810   2.891   37.534  1.00 46.56 ? 9   PHE   A CD1 1 
ATOM   24   C CD2 . PHE   A 1 10  ? 7.977   3.005   35.471  1.00 46.38 ? 9   PHE   A CD2 1 
ATOM   25   C CE1 . PHE   A 1 10  ? 7.834   2.120   38.068  1.00 47.31 ? 9   PHE   A CE1 1 
ATOM   26   C CE2 . PHE   A 1 10  ? 9.001   2.238   36.010  1.00 47.21 ? 9   PHE   A CE2 1 
ATOM   27   C CZ  . PHE   A 1 10  ? 8.921   1.800   37.303  1.00 47.09 ? 9   PHE   A CZ  1 
ATOM   28   N N   . ASN   A 1 11  ? 2.413   4.700   35.739  1.00 40.46 ? 10  ASN   A N   1 
ATOM   29   C CA  . ASN   A 1 11  ? 1.381   5.718   35.549  1.00 40.28 ? 10  ASN   A CA  1 
ATOM   30   C C   . ASN   A 1 11  ? 1.900   7.024   36.187  1.00 39.23 ? 10  ASN   A C   1 
ATOM   31   O O   . ASN   A 1 11  ? 1.363   7.488   37.198  1.00 38.02 ? 10  ASN   A O   1 
ATOM   32   C CB  . ASN   A 1 11  ? 0.053   5.288   36.223  1.00 42.20 ? 10  ASN   A CB  1 
ATOM   33   C CG  . ASN   A 1 11  ? -1.120  6.186   35.891  1.00 46.78 ? 10  ASN   A CG  1 
ATOM   34   O OD1 . ASN   A 1 11  ? -1.285  6.627   34.749  1.00 48.97 ? 10  ASN   A OD1 1 
ATOM   35   N ND2 . ASN   A 1 11  ? -1.965  6.477   36.878  1.00 47.65 ? 10  ASN   A ND2 1 
ATOM   36   N N   . ARG   A 1 12  ? 2.983   7.584   35.627  1.00 38.74 ? 11  ARG   A N   1 
ATOM   37   C CA  . ARG   A 1 12  ? 3.584   8.801   36.161  1.00 39.10 ? 11  ARG   A CA  1 
ATOM   38   C C   . ARG   A 1 12  ? 4.494   9.510   35.157  1.00 38.44 ? 11  ARG   A C   1 
ATOM   39   O O   . ARG   A 1 12  ? 4.793   8.979   34.080  1.00 37.56 ? 11  ARG   A O   1 
ATOM   40   C CB  . ARG   A 1 12  ? 4.332   8.511   37.484  1.00 41.92 ? 11  ARG   A CB  1 
ATOM   41   C CG  . ARG   A 1 12  ? 5.675   7.821   37.311  1.00 46.15 ? 11  ARG   A CG  1 
ATOM   42   C CD  . ARG   A 1 12  ? 6.606   8.173   38.457  1.00 50.40 ? 11  ARG   A CD  1 
ATOM   43   N NE  . ARG   A 1 12  ? 6.390   7.322   39.624  1.00 53.82 ? 11  ARG   A NE  1 
ATOM   44   C CZ  . ARG   A 1 12  ? 6.302   7.761   40.875  1.00 56.13 ? 11  ARG   A CZ  1 
ATOM   45   N NH1 . ARG   A 1 12  ? 6.117   6.907   41.869  1.00 55.82 ? 11  ARG   A NH1 1 
ATOM   46   N NH2 . ARG   A 1 12  ? 6.399   9.058   41.142  1.00 56.27 ? 11  ARG   A NH2 1 
ATOM   47   N N   . ASP   A 1 13  ? 4.925   10.724  35.509  1.00 37.92 ? 12  ASP   A N   1 
ATOM   48   C CA  . ASP   A 1 13  ? 5.796   11.534  34.673  1.00 37.44 ? 12  ASP   A CA  1 
ATOM   49   C C   . ASP   A 1 13  ? 7.175   10.900  34.612  1.00 37.43 ? 12  ASP   A C   1 
ATOM   50   O O   . ASP   A 1 13  ? 7.764   10.640  35.661  1.00 37.75 ? 12  ASP   A O   1 
ATOM   51   C CB  . ASP   A 1 13  ? 5.906   12.930  35.314  1.00 38.16 ? 12  ASP   A CB  1 
ATOM   52   C CG  . ASP   A 1 13  ? 6.435   14.024  34.416  1.00 40.96 ? 12  ASP   A CG  1 
ATOM   53   O OD1 . ASP   A 1 13  ? 7.011   13.699  33.359  1.00 40.03 ? 12  ASP   A OD1 1 
ATOM   54   O OD2 . ASP   A 1 13  ? 6.274   15.207  34.771  1.00 42.91 ? 12  ASP   A OD2 1 
ATOM   55   N N   . PRO   A 1 14  ? 7.743   10.688  33.406  1.00 36.64 ? 13  PRO   A N   1 
ATOM   56   C CA  . PRO   A 1 14  ? 9.110   10.149  33.337  1.00 36.63 ? 13  PRO   A CA  1 
ATOM   57   C C   . PRO   A 1 14  ? 10.127  11.064  34.027  1.00 37.19 ? 13  PRO   A C   1 
ATOM   58   O O   . PRO   A 1 14  ? 11.131  10.581  34.542  1.00 37.01 ? 13  PRO   A O   1 
ATOM   59   C CB  . PRO   A 1 14  ? 9.380   10.037  31.827  1.00 36.85 ? 13  PRO   A CB  1 
ATOM   60   C CG  . PRO   A 1 14  ? 8.424   10.979  31.192  1.00 37.29 ? 13  PRO   A CG  1 
ATOM   61   C CD  . PRO   A 1 14  ? 7.196   10.956  32.063  1.00 35.93 ? 13  PRO   A CD  1 
ATOM   62   N N   . ARG   A 1 15  ? 9.852   12.379  34.059  1.00 38.09 ? 14  ARG   A N   1 
ATOM   63   C CA  . ARG   A 1 15  ? 10.686  13.384  34.712  1.00 39.54 ? 14  ARG   A CA  1 
ATOM   64   C C   . ARG   A 1 15  ? 10.814  13.151  36.244  1.00 40.44 ? 14  ARG   A C   1 
ATOM   65   O O   . ARG   A 1 15  ? 11.688  13.746  36.874  1.00 40.65 ? 14  ARG   A O   1 
ATOM   66   C CB  . ARG   A 1 15  ? 10.153  14.794  34.403  1.00 41.47 ? 14  ARG   A CB  1 
ATOM   67   C CG  . ARG   A 1 15  ? 10.101  15.118  32.906  1.00 44.80 ? 14  ARG   A CG  1 
ATOM   68   C CD  . ARG   A 1 15  ? 9.108   16.241  32.616  1.00 48.29 ? 14  ARG   A CD  1 
ATOM   69   N NE  . ARG   A 1 15  ? 9.044   16.597  31.195  1.00 50.82 ? 14  ARG   A NE  1 
ATOM   70   C CZ  . ARG   A 1 15  ? 8.151   16.118  30.334  1.00 52.70 ? 14  ARG   A CZ  1 
ATOM   71   N NH1 . ARG   A 1 15  ? 8.159   16.518  29.071  1.00 52.42 ? 14  ARG   A NH1 1 
ATOM   72   N NH2 . ARG   A 1 15  ? 7.245   15.233  30.731  1.00 52.46 ? 14  ARG   A NH2 1 
ATOM   73   N N   . ASP   A 1 16  ? 9.970   12.279  36.841  1.00 40.42 ? 15  ASP   A N   1 
ATOM   74   C CA  . ASP   A 1 16  ? 10.112  11.935  38.270  1.00 40.86 ? 15  ASP   A CA  1 
ATOM   75   C C   . ASP   A 1 16  ? 11.334  11.012  38.491  1.00 40.75 ? 15  ASP   A C   1 
ATOM   76   O O   . ASP   A 1 16  ? 11.847  10.930  39.605  1.00 41.08 ? 15  ASP   A O   1 
ATOM   77   C CB  . ASP   A 1 16  ? 8.858   11.217  38.793  1.00 42.95 ? 15  ASP   A CB  1 
ATOM   78   C CG  . ASP   A 1 16  ? 7.612   12.075  38.860  1.00 48.54 ? 15  ASP   A CG  1 
ATOM   79   O OD1 . ASP   A 1 16  ? 7.728   13.308  38.683  1.00 49.51 ? 15  ASP   A OD1 1 
ATOM   80   O OD2 . ASP   A 1 16  ? 6.516   11.512  39.095  1.00 51.01 ? 15  ASP   A OD2 1 
ATOM   81   N N   . HIS   A 1 17  ? 11.771  10.292  37.448  1.00 39.80 ? 16  HIS   A N   1 
ATOM   82   C CA  . HIS   A 1 17  ? 12.912  9.390   37.536  1.00 39.71 ? 16  HIS   A CA  1 
ATOM   83   C C   . HIS   A 1 17  ? 14.080  9.806   36.623  1.00 39.50 ? 16  HIS   A C   1 
ATOM   84   O O   . HIS   A 1 17  ? 15.173  9.273   36.776  1.00 40.09 ? 16  HIS   A O   1 
ATOM   85   C CB  . HIS   A 1 17  ? 12.483  7.947   37.201  1.00 40.47 ? 16  HIS   A CB  1 
ATOM   86   C CG  . HIS   A 1 17  ? 11.489  7.350   38.153  1.00 42.66 ? 16  HIS   A CG  1 
ATOM   87   N ND1 . HIS   A 1 17  ? 11.334  7.834   39.443  1.00 44.42 ? 16  HIS   A ND1 1 
ATOM   88   C CD2 . HIS   A 1 17  ? 10.659  6.295   37.983  1.00 43.77 ? 16  HIS   A CD2 1 
ATOM   89   C CE1 . HIS   A 1 17  ? 10.399  7.081   39.999  1.00 44.82 ? 16  HIS   A CE1 1 
ATOM   90   N NE2 . HIS   A 1 17  ? 9.968   6.138   39.165  1.00 44.88 ? 16  HIS   A NE2 1 
ATOM   91   N N   . TYR   A 1 18  ? 13.857  10.727  35.674  1.00 38.55 ? 17  TYR   A N   1 
ATOM   92   C CA  . TYR   A 1 18  ? 14.904  11.147  34.745  1.00 38.04 ? 17  TYR   A CA  1 
ATOM   93   C C   . TYR   A 1 18  ? 14.983  12.665  34.591  1.00 38.53 ? 17  TYR   A C   1 
ATOM   94   O O   . TYR   A 1 18  ? 13.970  13.362  34.674  1.00 38.48 ? 17  TYR   A O   1 
ATOM   95   C CB  . TYR   A 1 18  ? 14.656  10.541  33.347  1.00 36.77 ? 17  TYR   A CB  1 
ATOM   96   C CG  . TYR   A 1 18  ? 14.667  9.030   33.315  1.00 36.24 ? 17  TYR   A CG  1 
ATOM   97   C CD1 . TYR   A 1 18  ? 15.850  8.326   33.156  1.00 36.59 ? 17  TYR   A CD1 1 
ATOM   98   C CD2 . TYR   A 1 18  ? 13.492  8.304   33.435  1.00 36.95 ? 17  TYR   A CD2 1 
ATOM   99   C CE1 . TYR   A 1 18  ? 15.871  6.938   33.160  1.00 37.39 ? 17  TYR   A CE1 1 
ATOM   100  C CE2 . TYR   A 1 18  ? 13.497  6.915   33.423  1.00 37.71 ? 17  TYR   A CE2 1 
ATOM   101  C CZ  . TYR   A 1 18  ? 14.690  6.234   33.290  1.00 38.46 ? 17  TYR   A CZ  1 
ATOM   102  O OH  . TYR   A 1 18  ? 14.693  4.855   33.275  1.00 39.54 ? 17  TYR   A OH  1 
ATOM   103  N N   . ASP   A 1 19  ? 16.180  13.170  34.283  1.00 38.85 ? 18  ASP   A N   1 
ATOM   104  C CA  . ASP   A 1 19  ? 16.356  14.581  33.976  1.00 39.74 ? 18  ASP   A CA  1 
ATOM   105  C C   . ASP   A 1 19  ? 16.307  14.659  32.445  1.00 40.26 ? 18  ASP   A C   1 
ATOM   106  O O   . ASP   A 1 19  ? 17.091  13.980  31.780  1.00 40.28 ? 18  ASP   A O   1 
ATOM   107  C CB  . ASP   A 1 19  ? 17.705  15.084  34.503  1.00 42.01 ? 18  ASP   A CB  1 
ATOM   108  C CG  . ASP   A 1 19  ? 17.744  15.219  36.014  1.00 47.27 ? 18  ASP   A CG  1 
ATOM   109  O OD1 . ASP   A 1 19  ? 16.827  15.856  36.578  1.00 47.74 ? 18  ASP   A OD1 1 
ATOM   110  O OD2 . ASP   A 1 19  ? 18.694  14.693  36.632  1.00 50.39 ? 18  ASP   A OD2 1 
ATOM   111  N N   . LEU   A 1 20  ? 15.346  15.403  31.882  1.00 40.33 ? 19  LEU   A N   1 
ATOM   112  C CA  . LEU   A 1 20  ? 15.222  15.511  30.427  1.00 41.09 ? 19  LEU   A CA  1 
ATOM   113  C C   . LEU   A 1 20  ? 16.271  16.457  29.865  1.00 41.42 ? 19  LEU   A C   1 
ATOM   114  O O   . LEU   A 1 20  ? 16.351  17.607  30.280  1.00 41.98 ? 19  LEU   A O   1 
ATOM   115  C CB  . LEU   A 1 20  ? 13.830  16.022  30.018  1.00 41.66 ? 19  LEU   A CB  1 
ATOM   116  C CG  . LEU   A 1 20  ? 12.872  15.046  29.319  1.00 43.43 ? 19  LEU   A CG  1 
ATOM   117  C CD1 . LEU   A 1 20  ? 11.643  15.780  28.800  1.00 44.07 ? 19  LEU   A CD1 1 
ATOM   118  C CD2 . LEU   A 1 20  ? 13.532  14.336  28.158  1.00 44.04 ? 19  LEU   A CD2 1 
ATOM   119  N N   . LEU   A 1 21  ? 17.053  15.988  28.905  1.00 41.07 ? 20  LEU   A N   1 
ATOM   120  C CA  . LEU   A 1 21  ? 18.060  16.818  28.252  1.00 41.12 ? 20  LEU   A CA  1 
ATOM   121  C C   . LEU   A 1 21  ? 17.633  17.107  26.777  1.00 40.91 ? 20  LEU   A C   1 
ATOM   122  O O   . LEU   A 1 21  ? 16.451  16.981  26.451  1.00 41.75 ? 20  LEU   A O   1 
ATOM   123  C CB  . LEU   A 1 21  ? 19.459  16.169  28.376  1.00 41.27 ? 20  LEU   A CB  1 
ATOM   124  C CG  . LEU   A 1 21  ? 19.901  15.808  29.792  1.00 43.12 ? 20  LEU   A CG  1 
ATOM   125  C CD1 . LEU   A 1 21  ? 21.235  15.078  29.780  1.00 43.83 ? 20  LEU   A CD1 1 
ATOM   126  C CD2 . LEU   A 1 21  ? 19.958  17.044  30.687  1.00 43.69 ? 20  LEU   A CD2 1 
ATOM   127  N N   . GLN   A 1 22  ? 18.569  17.523  25.914  1.00 39.16 ? 21  GLN   A N   1 
ATOM   128  C CA  . GLN   A 1 22  ? 18.319  17.903  24.534  1.00 37.92 ? 21  GLN   A CA  1 
ATOM   129  C C   . GLN   A 1 22  ? 17.499  16.925  23.705  1.00 35.30 ? 21  GLN   A C   1 
ATOM   130  O O   . GLN   A 1 22  ? 17.590  15.711  23.879  1.00 34.69 ? 21  GLN   A O   1 
ATOM   131  C CB  . GLN   A 1 22  ? 19.654  18.174  23.816  1.00 40.80 ? 21  GLN   A CB  1 
ATOM   132  C CG  . GLN   A 1 22  ? 20.674  17.051  24.005  1.00 46.68 ? 21  GLN   A CG  1 
ATOM   133  C CD  . GLN   A 1 22  ? 21.897  17.209  23.140  1.00 53.40 ? 21  GLN   A CD  1 
ATOM   134  O OE1 . GLN   A 1 22  ? 23.036  17.180  23.623  1.00 54.87 ? 21  GLN   A OE1 1 
ATOM   135  N NE2 . GLN   A 1 22  ? 21.689  17.371  21.838  1.00 55.08 ? 21  GLN   A NE2 1 
ATOM   136  N N   . ARG   A 1 23  ? 16.712  17.470  22.777  1.00 33.19 ? 22  ARG   A N   1 
ATOM   137  C CA  . ARG   A 1 23  ? 15.989  16.649  21.822  1.00 31.58 ? 22  ARG   A CA  1 
ATOM   138  C C   . ARG   A 1 23  ? 17.041  16.210  20.801  1.00 30.38 ? 22  ARG   A C   1 
ATOM   139  O O   . ARG   A 1 23  ? 17.803  17.044  20.316  1.00 30.86 ? 22  ARG   A O   1 
ATOM   140  C CB  . ARG   A 1 23  ? 14.900  17.472  21.133  1.00 31.42 ? 22  ARG   A CB  1 
ATOM   141  C CG  . ARG   A 1 23  ? 14.163  16.729  20.030  1.00 30.87 ? 22  ARG   A CG  1 
ATOM   142  C CD  . ARG   A 1 23  ? 13.270  17.684  19.266  1.00 31.08 ? 22  ARG   A CD  1 
ATOM   143  N NE  . ARG   A 1 23  ? 12.478  17.006  18.241  1.00 31.58 ? 22  ARG   A NE  1 
ATOM   144  C CZ  . ARG   A 1 23  ? 12.870  16.842  16.979  1.00 33.28 ? 22  ARG   A CZ  1 
ATOM   145  N NH1 . ARG   A 1 23  ? 12.084  16.223  16.110  1.00 33.12 ? 22  ARG   A NH1 1 
ATOM   146  N NH2 . ARG   A 1 23  ? 14.049  17.302  16.577  1.00 31.74 ? 22  ARG   A NH2 1 
ATOM   147  N N   . LEU   A 1 24  ? 17.131  14.910  20.518  1.00 28.40 ? 23  LEU   A N   1 
ATOM   148  C CA  . LEU   A 1 24  ? 18.093  14.400  19.553  1.00 27.14 ? 23  LEU   A CA  1 
ATOM   149  C C   . LEU   A 1 24  ? 17.484  14.437  18.133  1.00 26.27 ? 23  LEU   A C   1 
ATOM   150  O O   . LEU   A 1 24  ? 18.113  14.910  17.191  1.00 25.90 ? 23  LEU   A O   1 
ATOM   151  C CB  . LEU   A 1 24  ? 18.512  12.965  19.934  1.00 26.81 ? 23  LEU   A CB  1 
ATOM   152  C CG  . LEU   A 1 24  ? 19.277  12.837  21.253  1.00 27.96 ? 23  LEU   A CG  1 
ATOM   153  C CD1 . LEU   A 1 24  ? 19.287  11.404  21.763  1.00 27.72 ? 23  LEU   A CD1 1 
ATOM   154  C CD2 . LEU   A 1 24  ? 20.690  13.382  21.126  1.00 28.85 ? 23  LEU   A CD2 1 
ATOM   155  N N   . GLY   A 1 25  ? 16.261  13.948  18.005  1.00 25.58 ? 24  GLY   A N   1 
ATOM   156  C CA  . GLY   A 1 25  ? 15.581  13.905  16.723  1.00 25.46 ? 24  GLY   A CA  1 
ATOM   157  C C   . GLY   A 1 25  ? 14.180  13.360  16.844  1.00 25.63 ? 24  GLY   A C   1 
ATOM   158  O O   . GLY   A 1 25  ? 13.656  13.221  17.951  1.00 25.37 ? 24  GLY   A O   1 
ATOM   159  N N   . GLY   A 1 26  ? 13.563  13.086  15.710  1.00 25.32 ? 25  GLY   A N   1 
ATOM   160  C CA  . GLY   A 1 26  ? 12.195  12.589  15.706  1.00 25.66 ? 25  GLY   A CA  1 
ATOM   161  C C   . GLY   A 1 26  ? 11.678  12.244  14.336  1.00 25.39 ? 25  GLY   A C   1 
ATOM   162  O O   . GLY   A 1 26  ? 12.189  12.729  13.324  1.00 25.27 ? 25  GLY   A O   1 
ATOM   163  N N   . GLY   A 1 27  ? 10.665  11.393  14.328  1.00 24.58 ? 26  GLY   A N   1 
ATOM   164  C CA  . GLY   A 1 27  ? 10.016  10.946  13.111  1.00 24.92 ? 26  GLY   A CA  1 
ATOM   165  C C   . GLY   A 1 27  ? 8.720   10.237  13.414  1.00 24.84 ? 26  GLY   A C   1 
ATOM   166  O O   . GLY   A 1 27  ? 8.100   10.484  14.457  1.00 24.45 ? 26  GLY   A O   1 
ATOM   167  N N   . THR   A 1 28  ? 8.315   9.316   12.516  1.00 24.44 ? 27  THR   A N   1 
ATOM   168  C CA  . THR   A 1 28  ? 7.088   8.531   12.702  1.00 24.80 ? 27  THR   A CA  1 
ATOM   169  C C   . THR   A 1 28  ? 7.152   7.617   13.942  1.00 24.90 ? 27  THR   A C   1 
ATOM   170  O O   . THR   A 1 28  ? 6.103   7.233   14.476  1.00 25.87 ? 27  THR   A O   1 
ATOM   171  C CB  . THR   A 1 28  ? 6.807   7.720   11.431  1.00 25.39 ? 27  THR   A CB  1 
ATOM   172  O OG1 . THR   A 1 28  ? 7.962   6.949   11.109  1.00 23.73 ? 27  THR   A OG1 1 
ATOM   173  C CG2 . THR   A 1 28  ? 6.445   8.615   10.245  1.00 26.21 ? 27  THR   A CG2 1 
ATOM   174  N N   . TYR   A 1 29  ? 8.366   7.280   14.400  1.00 23.57 ? 28  TYR   A N   1 
ATOM   175  C CA  . TYR   A 1 29  ? 8.598   6.445   15.587  1.00 23.41 ? 28  TYR   A CA  1 
ATOM   176  C C   . TYR   A 1 29  ? 8.460   7.232   16.919  1.00 24.35 ? 28  TYR   A C   1 
ATOM   177  O O   . TYR   A 1 29  ? 8.471   6.619   17.983  1.00 24.76 ? 28  TYR   A O   1 
ATOM   178  C CB  . TYR   A 1 29  ? 9.984   5.771   15.519  1.00 22.14 ? 28  TYR   A CB  1 
ATOM   179  C CG  . TYR   A 1 29  ? 11.078  6.788   15.294  1.00 20.35 ? 28  TYR   A CG  1 
ATOM   180  C CD1 . TYR   A 1 29  ? 11.649  7.467   16.357  1.00 20.78 ? 28  TYR   A CD1 1 
ATOM   181  C CD2 . TYR   A 1 29  ? 11.481  7.134   14.009  1.00 20.21 ? 28  TYR   A CD2 1 
ATOM   182  C CE1 . TYR   A 1 29  ? 12.580  8.468   16.154  1.00 21.58 ? 28  TYR   A CE1 1 
ATOM   183  C CE2 . TYR   A 1 29  ? 12.431  8.120   13.796  1.00 20.29 ? 28  TYR   A CE2 1 
ATOM   184  C CZ  . TYR   A 1 29  ? 12.997  8.768   14.874  1.00 21.80 ? 28  TYR   A CZ  1 
ATOM   185  O OH  . TYR   A 1 29  ? 13.921  9.765   14.691  1.00 23.55 ? 28  TYR   A OH  1 
ATOM   186  N N   . GLY   A 1 30  ? 8.378   8.563   16.861  1.00 24.45 ? 29  GLY   A N   1 
ATOM   187  C CA  . GLY   A 1 30  ? 8.271   9.370   18.068  1.00 24.85 ? 29  GLY   A CA  1 
ATOM   188  C C   . GLY   A 1 30  ? 9.309   10.473  18.146  1.00 25.14 ? 29  GLY   A C   1 
ATOM   189  O O   . GLY   A 1 30  ? 10.001  10.758  17.161  1.00 25.37 ? 29  GLY   A O   1 
ATOM   190  N N   . GLU   A 1 31  ? 9.407   11.120  19.308  1.00 23.99 ? 30  GLU   A N   1 
ATOM   191  C CA  . GLU   A 1 31  ? 10.368  12.204  19.527  1.00 24.22 ? 30  GLU   A CA  1 
ATOM   192  C C   . GLU   A 1 31  ? 11.388  11.683  20.513  1.00 23.95 ? 30  GLU   A C   1 
ATOM   193  O O   . GLU   A 1 31  ? 11.004  11.206  21.576  1.00 24.66 ? 30  GLU   A O   1 
ATOM   194  C CB  . GLU   A 1 31  ? 9.662   13.438  20.101  1.00 26.15 ? 30  GLU   A CB  1 
ATOM   195  C CG  . GLU   A 1 31  ? 8.672   14.056  19.134  1.00 31.47 ? 30  GLU   A CG  1 
ATOM   196  C CD  . GLU   A 1 31  ? 9.344   14.828  18.018  1.00 38.06 ? 30  GLU   A CD  1 
ATOM   197  O OE1 . GLU   A 1 31  ? 9.786   15.970  18.278  1.00 40.50 ? 30  GLU   A OE1 1 
ATOM   198  O OE2 . GLU   A 1 31  ? 9.427   14.298  16.886  1.00 38.83 ? 30  GLU   A OE2 1 
ATOM   199  N N   . VAL   A 1 32  ? 12.670  11.748  20.178  1.00 23.10 ? 31  VAL   A N   1 
ATOM   200  C CA  . VAL   A 1 32  ? 13.711  11.155  21.007  1.00 23.11 ? 31  VAL   A CA  1 
ATOM   201  C C   . VAL   A 1 32  ? 14.577  12.181  21.683  1.00 24.96 ? 31  VAL   A C   1 
ATOM   202  O O   . VAL   A 1 32  ? 15.096  13.079  21.033  1.00 25.39 ? 31  VAL   A O   1 
ATOM   203  C CB  . VAL   A 1 32  ? 14.553  10.136  20.203  1.00 22.45 ? 31  VAL   A CB  1 
ATOM   204  C CG1 . VAL   A 1 32  ? 15.666  9.549   21.072  1.00 22.29 ? 31  VAL   A CG1 1 
ATOM   205  C CG2 . VAL   A 1 32  ? 13.665  9.031   19.632  1.00 22.25 ? 31  VAL   A CG2 1 
ATOM   206  N N   . PHE   A 1 33  ? 14.731  12.054  23.006  1.00 26.13 ? 32  PHE   A N   1 
ATOM   207  C CA  . PHE   A 1 33  ? 15.532  12.974  23.794  1.00 27.35 ? 32  PHE   A CA  1 
ATOM   208  C C   . PHE   A 1 33  ? 16.662  12.258  24.517  1.00 28.04 ? 32  PHE   A C   1 
ATOM   209  O O   . PHE   A 1 33  ? 16.516  11.111  24.935  1.00 28.25 ? 32  PHE   A O   1 
ATOM   210  C CB  . PHE   A 1 33  ? 14.647  13.618  24.875  1.00 27.83 ? 32  PHE   A CB  1 
ATOM   211  C CG  . PHE   A 1 33  ? 13.477  14.408  24.343  1.00 28.99 ? 32  PHE   A CG  1 
ATOM   212  C CD1 . PHE   A 1 33  ? 12.307  13.774  23.962  1.00 29.90 ? 32  PHE   A CD1 1 
ATOM   213  C CD2 . PHE   A 1 33  ? 13.525  15.789  24.278  1.00 30.37 ? 32  PHE   A CD2 1 
ATOM   214  C CE1 . PHE   A 1 33  ? 11.238  14.503  23.460  1.00 30.69 ? 32  PHE   A CE1 1 
ATOM   215  C CE2 . PHE   A 1 33  ? 12.456  16.511  23.774  1.00 31.12 ? 32  PHE   A CE2 1 
ATOM   216  C CZ  . PHE   A 1 33  ? 11.325  15.860  23.356  1.00 30.88 ? 32  PHE   A CZ  1 
ATOM   217  N N   . LYS   A 1 34  ? 17.759  12.970  24.742  1.00 28.29 ? 33  LYS   A N   1 
ATOM   218  C CA  . LYS   A 1 34  ? 18.818  12.493  25.616  1.00 30.11 ? 33  LYS   A CA  1 
ATOM   219  C C   . LYS   A 1 34  ? 18.275  12.706  27.063  1.00 31.66 ? 33  LYS   A C   1 
ATOM   220  O O   . LYS   A 1 34  ? 17.556  13.677  27.314  1.00 31.57 ? 33  LYS   A O   1 
ATOM   221  C CB  . LYS   A 1 34  ? 20.080  13.350  25.427  1.00 31.54 ? 33  LYS   A CB  1 
ATOM   222  C CG  . LYS   A 1 34  ? 21.300  12.810  26.136  1.00 35.42 ? 33  LYS   A CG  1 
ATOM   223  C CD  . LYS   A 1 34  ? 22.508  13.658  25.793  1.00 40.16 ? 33  LYS   A CD  1 
ATOM   224  C CE  . LYS   A 1 34  ? 23.796  13.064  26.299  1.00 44.50 ? 33  LYS   A CE  1 
ATOM   225  N NZ  . LYS   A 1 34  ? 24.971  13.864  25.859  1.00 46.81 ? 33  LYS   A NZ  1 
ATOM   226  N N   . ALA   A 1 35  ? 18.600  11.809  27.991  1.00 33.39 ? 34  ALA   A N   1 
ATOM   227  C CA  . ALA   A 1 35  ? 18.140  11.924  29.380  1.00 35.50 ? 34  ALA   A CA  1 
ATOM   228  C C   . ALA   A 1 35  ? 19.119  11.223  30.334  1.00 37.27 ? 34  ALA   A C   1 
ATOM   229  O O   . ALA   A 1 35  ? 19.940  10.416  29.894  1.00 37.23 ? 34  ALA   A O   1 
ATOM   230  C CB  . ALA   A 1 35  ? 16.735  11.334  29.524  1.00 35.95 ? 34  ALA   A CB  1 
ATOM   231  N N   . ARG   A 1 36  ? 19.059  11.549  31.634  1.00 38.50 ? 35  ARG   A N   1 
ATOM   232  C CA  . ARG   A 1 36  ? 19.962  10.961  32.610  1.00 40.37 ? 35  ARG   A CA  1 
ATOM   233  C C   . ARG   A 1 36  ? 19.164  10.399  33.783  1.00 41.54 ? 35  ARG   A C   1 
ATOM   234  O O   . ARG   A 1 36  ? 18.287  11.086  34.299  1.00 41.27 ? 35  ARG   A O   1 
ATOM   235  C CB  . ARG   A 1 36  ? 20.938  12.037  33.098  1.00 42.49 ? 35  ARG   A CB  1 
ATOM   236  C CG  . ARG   A 1 36  ? 22.109  11.502  33.907  1.00 47.09 ? 35  ARG   A CG  1 
ATOM   237  C CD  . ARG   A 1 36  ? 22.999  12.613  34.450  1.00 51.82 ? 35  ARG   A CD  1 
ATOM   238  N NE  . ARG   A 1 36  ? 23.506  13.496  33.396  1.00 56.63 ? 35  ARG   A NE  1 
ATOM   239  C CZ  . ARG   A 1 36  ? 23.195  14.786  33.285  1.00 59.91 ? 35  ARG   A CZ  1 
ATOM   240  N NH1 . ARG   A 1 36  ? 22.387  15.361  34.170  1.00 59.66 ? 35  ARG   A NH1 1 
ATOM   241  N NH2 . ARG   A 1 36  ? 23.699  15.515  32.297  1.00 60.15 ? 35  ARG   A NH2 1 
ATOM   242  N N   . ASP   A 1 37  ? 19.455  9.150   34.191  1.00 42.57 ? 36  ASP   A N   1 
ATOM   243  C CA  . ASP   A 1 37  ? 18.781  8.504   35.318  1.00 44.22 ? 36  ASP   A CA  1 
ATOM   244  C C   . ASP   A 1 37  ? 19.136  9.266   36.588  1.00 45.86 ? 36  ASP   A C   1 
ATOM   245  O O   . ASP   A 1 37  ? 20.314  9.468   36.864  1.00 46.09 ? 36  ASP   A O   1 
ATOM   246  C CB  . ASP   A 1 37  ? 19.220  7.031   35.428  1.00 46.08 ? 36  ASP   A CB  1 
ATOM   247  C CG  . ASP   A 1 37  ? 18.358  6.167   36.332  1.00 51.04 ? 36  ASP   A CG  1 
ATOM   248  O OD1 . ASP   A 1 37  ? 18.334  6.425   37.556  1.00 51.82 ? 36  ASP   A OD1 1 
ATOM   249  O OD2 . ASP   A 1 37  ? 17.722  5.219   35.818  1.00 53.16 ? 36  ASP   A OD2 1 
ATOM   250  N N   . LYS   A 1 38  ? 18.124  9.727   37.336  1.00 46.79 ? 37  LYS   A N   1 
ATOM   251  C CA  . LYS   A 1 38  ? 18.327  10.510  38.554  1.00 48.11 ? 37  LYS   A CA  1 
ATOM   252  C C   . LYS   A 1 38  ? 19.157  9.824   39.628  1.00 49.54 ? 37  LYS   A C   1 
ATOM   253  O O   . LYS   A 1 38  ? 19.901  10.503  40.333  1.00 49.80 ? 37  LYS   A O   1 
ATOM   254  C CB  . LYS   A 1 38  ? 16.989  10.960  39.148  1.00 49.41 ? 37  LYS   A CB  1 
ATOM   255  C CG  . LYS   A 1 38  ? 16.410  12.195  38.485  1.00 52.87 ? 37  LYS   A CG  1 
ATOM   256  C CD  . LYS   A 1 38  ? 15.137  12.627  39.189  1.00 57.13 ? 37  LYS   A CD  1 
ATOM   257  C CE  . LYS   A 1 38  ? 14.525  13.841  38.546  1.00 61.04 ? 37  LYS   A CE  1 
ATOM   258  N NZ  . LYS   A 1 38  ? 13.218  14.183  39.165  1.00 63.28 ? 37  LYS   A NZ  1 
ATOM   259  N N   . VAL   A 1 39  ? 19.035  8.497   39.769  1.00 50.28 ? 38  VAL   A N   1 
ATOM   260  C CA  . VAL   A 1 39  ? 19.772  7.786   40.815  1.00 51.44 ? 38  VAL   A CA  1 
ATOM   261  C C   . VAL   A 1 39  ? 21.154  7.313   40.345  1.00 51.81 ? 38  VAL   A C   1 
ATOM   262  O O   . VAL   A 1 39  ? 22.158  7.686   40.951  1.00 52.30 ? 38  VAL   A O   1 
ATOM   263  C CB  . VAL   A 1 39  ? 18.936  6.640   41.435  1.00 52.49 ? 38  VAL   A CB  1 
ATOM   264  C CG1 . VAL   A 1 39  ? 19.759  5.841   42.440  1.00 53.18 ? 38  VAL   A CG1 1 
ATOM   265  C CG2 . VAL   A 1 39  ? 17.670  7.187   42.087  1.00 52.86 ? 38  VAL   A CG2 1 
ATOM   266  N N   . SER   A 1 40  ? 21.218  6.529   39.261  1.00 51.27 ? 39  SER   A N   1 
ATOM   267  C CA  . SER   A 1 40  ? 22.491  6.003   38.768  1.00 51.21 ? 39  SER   A CA  1 
ATOM   268  C C   . SER   A 1 40  ? 23.375  7.011   38.029  1.00 50.44 ? 39  SER   A C   1 
ATOM   269  O O   . SER   A 1 40  ? 24.584  6.819   37.961  1.00 50.87 ? 39  SER   A O   1 
ATOM   270  C CB  . SER   A 1 40  ? 22.258  4.784   37.882  1.00 52.97 ? 39  SER   A CB  1 
ATOM   271  O OG  . SER   A 1 40  ? 21.738  5.161   36.617  1.00 55.31 ? 39  SER   A OG  1 
ATOM   272  N N   . GLY   A 1 41  ? 22.774  8.038   37.444  1.00 49.12 ? 40  GLY   A N   1 
ATOM   273  C CA  . GLY   A 1 41  ? 23.518  9.028   36.671  1.00 48.15 ? 40  GLY   A CA  1 
ATOM   274  C C   . GLY   A 1 41  ? 23.835  8.594   35.246  1.00 46.99 ? 40  GLY   A C   1 
ATOM   275  O O   . GLY   A 1 41  ? 24.490  9.331   34.505  1.00 47.37 ? 40  GLY   A O   1 
ATOM   276  N N   . ASP   A 1 42  ? 23.380  7.399   34.843  1.00 45.31 ? 41  ASP   A N   1 
ATOM   277  C CA  . ASP   A 1 42  ? 23.636  6.862   33.512  1.00 44.28 ? 41  ASP   A CA  1 
ATOM   278  C C   . ASP   A 1 42  ? 22.823  7.570   32.434  1.00 42.36 ? 41  ASP   A C   1 
ATOM   279  O O   . ASP   A 1 42  ? 21.693  7.992   32.678  1.00 42.62 ? 41  ASP   A O   1 
ATOM   280  C CB  . ASP   A 1 42  ? 23.336  5.350   33.476  1.00 46.36 ? 41  ASP   A CB  1 
ATOM   281  C CG  . ASP   A 1 42  ? 24.165  4.506   34.429  1.00 51.63 ? 41  ASP   A CG  1 
ATOM   282  O OD1 . ASP   A 1 42  ? 25.049  5.071   35.112  1.00 52.33 ? 41  ASP   A OD1 1 
ATOM   283  O OD2 . ASP   A 1 42  ? 23.918  3.282   34.504  1.00 54.14 ? 41  ASP   A OD2 1 
ATOM   284  N N   . LEU   A 1 43  ? 23.392  7.688   31.236  1.00 40.31 ? 42  LEU   A N   1 
ATOM   285  C CA  . LEU   A 1 43  ? 22.694  8.311   30.115  1.00 38.60 ? 42  LEU   A CA  1 
ATOM   286  C C   . LEU   A 1 43  ? 21.744  7.308   29.492  1.00 35.74 ? 42  LEU   A C   1 
ATOM   287  O O   . LEU   A 1 43  ? 22.073  6.132   29.379  1.00 35.78 ? 42  LEU   A O   1 
ATOM   288  C CB  . LEU   A 1 43  ? 23.696  8.794   29.054  1.00 39.12 ? 42  LEU   A CB  1 
ATOM   289  C CG  . LEU   A 1 43  ? 24.446  10.067  29.400  1.00 40.64 ? 42  LEU   A CG  1 
ATOM   290  C CD1 . LEU   A 1 43  ? 25.522  10.354  28.379  1.00 41.35 ? 42  LEU   A CD1 1 
ATOM   291  C CD2 . LEU   A 1 43  ? 23.498  11.241  29.501  1.00 40.90 ? 42  LEU   A CD2 1 
ATOM   292  N N   . VAL   A 1 44  ? 20.550  7.775   29.101  1.00 33.40 ? 43  VAL   A N   1 
ATOM   293  C CA  . VAL   A 1 44  ? 19.513  6.983   28.445  1.00 31.79 ? 43  VAL   A CA  1 
ATOM   294  C C   . VAL   A 1 44  ? 18.875  7.824   27.311  1.00 30.51 ? 43  VAL   A C   1 
ATOM   295  O O   . VAL   A 1 44  ? 19.125  9.029   27.201  1.00 30.38 ? 43  VAL   A O   1 
ATOM   296  C CB  . VAL   A 1 44  ? 18.407  6.513   29.445  1.00 32.24 ? 43  VAL   A CB  1 
ATOM   297  C CG1 . VAL   A 1 44  ? 18.964  5.644   30.565  1.00 32.69 ? 43  VAL   A CG1 1 
ATOM   298  C CG2 . VAL   A 1 44  ? 17.612  7.700   29.984  1.00 32.65 ? 43  VAL   A CG2 1 
ATOM   299  N N   . ALA   A 1 45  ? 18.044  7.189   26.478  1.00 29.29 ? 44  ALA   A N   1 
ATOM   300  C CA  . ALA   A 1 45  ? 17.284  7.893   25.469  1.00 28.86 ? 44  ALA   A CA  1 
ATOM   301  C C   . ALA   A 1 45  ? 15.811  7.727   25.852  1.00 28.53 ? 44  ALA   A C   1 
ATOM   302  O O   . ALA   A 1 45  ? 15.374  6.611   26.129  1.00 28.78 ? 44  ALA   A O   1 
ATOM   303  C CB  . ALA   A 1 45  ? 17.549  7.290   24.101  1.00 28.89 ? 44  ALA   A CB  1 
ATOM   304  N N   . LEU   A 1 46  ? 15.058  8.826   25.918  1.00 27.83 ? 45  LEU   A N   1 
ATOM   305  C CA  . LEU   A 1 46  ? 13.626  8.752   26.214  1.00 27.86 ? 45  LEU   A CA  1 
ATOM   306  C C   . LEU   A 1 46  ? 12.909  9.056   24.927  1.00 27.16 ? 45  LEU   A C   1 
ATOM   307  O O   . LEU   A 1 46  ? 13.194  10.062  24.302  1.00 27.51 ? 45  LEU   A O   1 
ATOM   308  C CB  . LEU   A 1 46  ? 13.198  9.752   27.297  1.00 28.25 ? 45  LEU   A CB  1 
ATOM   309  C CG  . LEU   A 1 46  ? 13.473  9.345   28.739  1.00 31.38 ? 45  LEU   A CG  1 
ATOM   310  C CD1 . LEU   A 1 46  ? 13.154  10.482  29.683  1.00 32.59 ? 45  LEU   A CD1 1 
ATOM   311  C CD2 . LEU   A 1 46  ? 12.655  8.131   29.123  1.00 32.52 ? 45  LEU   A CD2 1 
ATOM   312  N N   . LYS   A 1 47  ? 11.974  8.205   24.534  1.00 26.58 ? 46  LYS   A N   1 
ATOM   313  C CA  . LYS   A 1 47  ? 11.240  8.383   23.298  1.00 26.22 ? 46  LYS   A CA  1 
ATOM   314  C C   . LYS   A 1 47  ? 9.774   8.592   23.596  1.00 27.32 ? 46  LYS   A C   1 
ATOM   315  O O   . LYS   A 1 47  ? 9.135   7.700   24.124  1.00 28.03 ? 46  LYS   A O   1 
ATOM   316  C CB  . LYS   A 1 47  ? 11.445  7.149   22.409  1.00 25.60 ? 46  LYS   A CB  1 
ATOM   317  C CG  . LYS   A 1 47  ? 10.650  7.159   21.111  1.00 26.24 ? 46  LYS   A CG  1 
ATOM   318  C CD  . LYS   A 1 47  ? 11.097  5.985   20.191  1.00 28.06 ? 46  LYS   A CD  1 
ATOM   319  C CE  . LYS   A 1 47  ? 11.008  4.627   20.853  1.00 30.43 ? 46  LYS   A CE  1 
ATOM   320  N NZ  . LYS   A 1 47  ? 11.710  3.572   20.060  1.00 32.66 ? 46  LYS   A NZ  1 
ATOM   321  N N   . MET   A 1 48  ? 9.243   9.758   23.251  1.00 27.54 ? 47  MET   A N   1 
ATOM   322  C CA  . MET   A 1 48  ? 7.847   10.114  23.466  1.00 28.53 ? 47  MET   A CA  1 
ATOM   323  C C   . MET   A 1 48  ? 7.012   9.709   22.243  1.00 29.39 ? 47  MET   A C   1 
ATOM   324  O O   . MET   A 1 48  ? 7.302   10.127  21.125  1.00 29.03 ? 47  MET   A O   1 
ATOM   325  C CB  . MET   A 1 48  ? 7.746   11.626  23.729  1.00 29.68 ? 47  MET   A CB  1 
ATOM   326  C CG  . MET   A 1 48  ? 6.357   12.083  24.104  1.00 32.67 ? 47  MET   A CG  1 
ATOM   327  S SD  . MET   A 1 48  ? 6.256   13.881  24.175  1.00 44.20 ? 47  MET   A SD  1 
ATOM   328  C CE  . MET   A 1 48  ? 6.508   14.265  22.421  1.00 41.77 ? 47  MET   A CE  1 
ATOM   329  N N   . VAL   A 1 49  ? 6.004   8.849   22.453  1.00 30.18 ? 48  VAL   A N   1 
ATOM   330  C CA  . VAL   A 1 49  ? 5.118   8.357   21.402  1.00 31.12 ? 48  VAL   A CA  1 
ATOM   331  C C   . VAL   A 1 49  ? 3.680   8.791   21.701  1.00 32.94 ? 48  VAL   A C   1 
ATOM   332  O O   . VAL   A 1 49  ? 3.156   8.494   22.780  1.00 32.21 ? 48  VAL   A O   1 
ATOM   333  C CB  . VAL   A 1 49  ? 5.210   6.820   21.257  1.00 31.32 ? 48  VAL   A CB  1 
ATOM   334  C CG1 . VAL   A 1 49  ? 4.415   6.342   20.052  1.00 31.66 ? 48  VAL   A CG1 1 
ATOM   335  C CG2 . VAL   A 1 49  ? 6.662   6.364   21.141  1.00 31.48 ? 48  VAL   A CG2 1 
ATOM   336  N N   . LYS   A 1 50  ? 3.050   9.521   20.775  1.00 34.52 ? 49  LYS   A N   1 
ATOM   337  C CA  . LYS   A 1 50  ? 1.671   9.965   20.979  1.00 36.16 ? 49  LYS   A CA  1 
ATOM   338  C C   . LYS   A 1 50  ? 0.745   8.772   20.805  1.00 37.45 ? 49  LYS   A C   1 
ATOM   339  O O   . LYS   A 1 50  ? 0.926   7.986   19.879  1.00 37.96 ? 49  LYS   A O   1 
ATOM   340  C CB  . LYS   A 1 50  ? 1.297   11.090  20.010  1.00 39.51 ? 49  LYS   A CB  1 
ATOM   341  C CG  . LYS   A 1 50  ? 1.862   12.455  20.406  1.00 45.71 ? 49  LYS   A CG  1 
ATOM   342  C CD  . LYS   A 1 50  ? 1.641   13.514  19.316  1.00 51.01 ? 49  LYS   A CD  1 
ATOM   343  C CE  . LYS   A 1 50  ? 0.179   13.735  18.990  1.00 55.52 ? 49  LYS   A CE  1 
ATOM   344  N NZ  . LYS   A 1 50  ? -0.523  14.487  20.065  1.00 58.18 ? 49  LYS   A NZ  1 
ATOM   345  N N   . MET   A 1 51  ? -0.238  8.623   21.700  1.00 38.21 ? 50  MET   A N   1 
ATOM   346  C CA  . MET   A 1 51  ? -1.151  7.486   21.639  1.00 38.91 ? 50  MET   A CA  1 
ATOM   347  C C   . MET   A 1 51  ? -2.459  7.760   20.918  1.00 39.14 ? 50  MET   A C   1 
ATOM   348  O O   . MET   A 1 51  ? -2.954  8.885   20.931  1.00 39.66 ? 50  MET   A O   1 
ATOM   349  C CB  . MET   A 1 51  ? -1.436  6.975   23.059  1.00 39.34 ? 50  MET   A CB  1 
ATOM   350  C CG  . MET   A 1 51  ? -0.192  6.476   23.774  1.00 40.42 ? 50  MET   A CG  1 
ATOM   351  S SD  . MET   A 1 51  ? 0.266   4.814   23.227  1.00 41.87 ? 50  MET   A SD  1 
ATOM   352  C CE  . MET   A 1 51  ? 1.607   5.197   22.115  1.00 39.34 ? 50  MET   A CE  1 
ATOM   353  N N   . GLU   A 1 52  ? -3.036  6.716   20.310  1.00 39.15 ? 51  GLU   A N   1 
ATOM   354  C CA  . GLU   A 1 52  ? -4.357  6.806   19.693  1.00 40.04 ? 51  GLU   A CA  1 
ATOM   355  C C   . GLU   A 1 52  ? -5.360  6.606   20.835  1.00 40.47 ? 51  GLU   A C   1 
ATOM   356  O O   . GLU   A 1 52  ? -5.266  5.616   21.563  1.00 40.49 ? 51  GLU   A O   1 
ATOM   357  C CB  . GLU   A 1 52  ? -4.557  5.694   18.648  1.00 42.73 ? 51  GLU   A CB  1 
ATOM   358  C CG  . GLU   A 1 52  ? -3.860  5.944   17.320  1.00 46.86 ? 51  GLU   A CG  1 
ATOM   359  C CD  . GLU   A 1 52  ? -4.571  6.933   16.416  1.00 52.59 ? 51  GLU   A CD  1 
ATOM   360  O OE1 . GLU   A 1 52  ? -5.787  7.165   16.616  1.00 52.75 ? 51  GLU   A OE1 1 
ATOM   361  O OE2 . GLU   A 1 52  ? -3.910  7.477   15.502  1.00 54.81 ? 51  GLU   A OE2 1 
ATOM   362  N N   . PRO   A 1 53  ? -6.324  7.524   21.000  1.00 40.34 ? 52  PRO   A N   1 
ATOM   363  C CA  . PRO   A 1 53  ? -7.301  7.386   22.098  1.00 40.58 ? 52  PRO   A CA  1 
ATOM   364  C C   . PRO   A 1 53  ? -8.106  6.087   22.092  1.00 41.14 ? 52  PRO   A C   1 
ATOM   365  O O   . PRO   A 1 53  ? -8.594  5.681   23.145  1.00 41.28 ? 52  PRO   A O   1 
ATOM   366  C CB  . PRO   A 1 53  ? -8.214  8.606   21.924  1.00 41.34 ? 52  PRO   A CB  1 
ATOM   367  C CG  . PRO   A 1 53  ? -7.415  9.579   21.133  1.00 41.92 ? 52  PRO   A CG  1 
ATOM   368  C CD  . PRO   A 1 53  ? -6.532  8.768   20.236  1.00 40.09 ? 52  PRO   A CD  1 
ATOM   369  N N   . ASP   A 1 54  ? -8.239  5.429   20.926  1.00 41.71 ? 53  ASP   A N   1 
ATOM   370  C CA  . ASP   A 1 54  ? -8.996  4.175   20.813  1.00 42.79 ? 53  ASP   A CA  1 
ATOM   371  C C   . ASP   A 1 54  ? -8.273  2.968   21.405  1.00 43.22 ? 53  ASP   A C   1 
ATOM   372  O O   . ASP   A 1 54  ? -8.932  2.003   21.795  1.00 43.91 ? 53  ASP   A O   1 
ATOM   373  C CB  . ASP   A 1 54  ? -9.381  3.883   19.353  1.00 44.37 ? 53  ASP   A CB  1 
ATOM   374  C CG  . ASP   A 1 54  ? -10.566 4.671   18.827  1.00 47.78 ? 53  ASP   A CG  1 
ATOM   375  O OD1 . ASP   A 1 54  ? -11.168 5.442   19.611  1.00 48.66 ? 53  ASP   A OD1 1 
ATOM   376  O OD2 . ASP   A 1 54  ? -10.893 4.518   17.637  1.00 49.12 ? 53  ASP   A OD2 1 
ATOM   377  N N   . ASP   A 1 55  ? -6.940  3.010   21.462  1.00 43.04 ? 54  ASP   A N   1 
ATOM   378  C CA  . ASP   A 1 55  ? -6.133  1.919   22.011  1.00 43.28 ? 54  ASP   A CA  1 
ATOM   379  C C   . ASP   A 1 55  ? -6.244  1.883   23.546  1.00 43.66 ? 54  ASP   A C   1 
ATOM   380  O O   . ASP   A 1 55  ? -5.660  2.733   24.229  1.00 43.72 ? 54  ASP   A O   1 
ATOM   381  C CB  . ASP   A 1 55  ? -4.669  2.068   21.576  1.00 44.83 ? 54  ASP   A CB  1 
ATOM   382  C CG  . ASP   A 1 55  ? -4.446  1.895   20.081  1.00 48.70 ? 54  ASP   A CG  1 
ATOM   383  O OD1 . ASP   A 1 55  ? -5.338  1.323   19.405  1.00 49.32 ? 54  ASP   A OD1 1 
ATOM   384  O OD2 . ASP   A 1 55  ? -3.382  2.329   19.586  1.00 50.16 ? 54  ASP   A OD2 1 
ATOM   385  N N   . ASP   A 1 56  ? -7.004  0.911   24.087  1.00 43.19 ? 55  ASP   A N   1 
ATOM   386  C CA  . ASP   A 1 56  ? -7.173  0.793   25.535  1.00 43.60 ? 55  ASP   A CA  1 
ATOM   387  C C   . ASP   A 1 56  ? -5.864  0.379   26.241  1.00 42.92 ? 55  ASP   A C   1 
ATOM   388  O O   . ASP   A 1 56  ? -4.916  -0.038  25.568  1.00 42.70 ? 55  ASP   A O   1 
ATOM   389  C CB  . ASP   A 1 56  ? -8.364  -0.122  25.897  1.00 46.27 ? 55  ASP   A CB  1 
ATOM   390  C CG  . ASP   A 1 56  ? -8.309  -1.558  25.408  1.00 52.00 ? 55  ASP   A CG  1 
ATOM   391  O OD1 . ASP   A 1 56  ? -7.199  -2.103  25.291  1.00 52.20 ? 55  ASP   A OD1 1 
ATOM   392  O OD2 . ASP   A 1 56  ? -9.389  -2.146  25.173  1.00 56.03 ? 55  ASP   A OD2 1 
ATOM   393  N N   . VAL   A 1 57  ? -5.802  0.499   27.584  1.00 42.42 ? 56  VAL   A N   1 
ATOM   394  C CA  . VAL   A 1 57  ? -4.575  0.168   28.305  1.00 42.40 ? 56  VAL   A CA  1 
ATOM   395  C C   . VAL   A 1 57  ? -4.213  -1.318  28.134  1.00 42.47 ? 56  VAL   A C   1 
ATOM   396  O O   . VAL   A 1 57  ? -3.041  -1.633  28.233  1.00 42.71 ? 56  VAL   A O   1 
ATOM   397  C CB  . VAL   A 1 57  ? -4.506  0.642   29.792  1.00 43.20 ? 56  VAL   A CB  1 
ATOM   398  C CG1 . VAL   A 1 57  ? -5.264  1.945   30.015  1.00 43.37 ? 56  VAL   A CG1 1 
ATOM   399  C CG2 . VAL   A 1 57  ? -4.965  -0.425  30.760  1.00 43.89 ? 56  VAL   A CG2 1 
ATOM   400  N N   . SER   A 1 58  ? -5.180  -2.217  27.838  1.00 42.42 ? 57  SER   A N   1 
ATOM   401  C CA  . SER   A 1 58  ? -4.858  -3.629  27.589  1.00 42.98 ? 57  SER   A CA  1 
ATOM   402  C C   . SER   A 1 58  ? -4.065  -3.758  26.281  1.00 43.23 ? 57  SER   A C   1 
ATOM   403  O O   . SER   A 1 58  ? -3.107  -4.527  26.207  1.00 43.27 ? 57  SER   A O   1 
ATOM   404  C CB  . SER   A 1 58  ? -6.124  -4.476  27.503  1.00 45.05 ? 57  SER   A CB  1 
ATOM   405  O OG  . SER   A 1 58  ? -6.638  -4.808  28.783  1.00 48.85 ? 57  SER   A OG  1 
ATOM   406  N N   . THR   A 1 59  ? -4.462  -2.988  25.257  1.00 43.03 ? 58  THR   A N   1 
ATOM   407  C CA  . THR   A 1 59  ? -3.797  -2.958  23.958  1.00 43.50 ? 58  THR   A CA  1 
ATOM   408  C C   . THR   A 1 59  ? -2.378  -2.414  24.138  1.00 43.02 ? 58  THR   A C   1 
ATOM   409  O O   . THR   A 1 59  ? -1.420  -2.988  23.616  1.00 43.34 ? 58  THR   A O   1 
ATOM   410  C CB  . THR   A 1 59  ? -4.625  -2.112  22.983  1.00 45.43 ? 58  THR   A CB  1 
ATOM   411  O OG1 . THR   A 1 59  ? -5.965  -2.619  22.947  1.00 46.76 ? 58  THR   A OG1 1 
ATOM   412  C CG2 . THR   A 1 59  ? -4.036  -2.084  21.589  1.00 45.98 ? 58  THR   A CG2 1 
ATOM   413  N N   . LEU   A 1 60  ? -2.239  -1.335  24.922  1.00 42.01 ? 59  LEU   A N   1 
ATOM   414  C CA  . LEU   A 1 60  ? -0.945  -0.729  25.226  1.00 41.52 ? 59  LEU   A CA  1 
ATOM   415  C C   . LEU   A 1 60  ? -0.050  -1.700  26.014  1.00 40.58 ? 59  LEU   A C   1 
ATOM   416  O O   . LEU   A 1 60  ? 1.127   -1.833  25.700  1.00 40.40 ? 59  LEU   A O   1 
ATOM   417  C CB  . LEU   A 1 60  ? -1.143  0.578   26.021  1.00 42.03 ? 59  LEU   A CB  1 
ATOM   418  C CG  . LEU   A 1 60  ? 0.132   1.344   26.346  1.00 44.24 ? 59  LEU   A CG  1 
ATOM   419  C CD1 . LEU   A 1 60  ? 0.834   1.797   25.076  1.00 45.29 ? 59  LEU   A CD1 1 
ATOM   420  C CD2 . LEU   A 1 60  ? -0.159  2.544   27.203  1.00 45.19 ? 59  LEU   A CD2 1 
ATOM   421  N N   . GLN   A 1 61  ? -0.609  -2.394  27.019  1.00 39.55 ? 60  GLN   A N   1 
ATOM   422  C CA  . GLN   A 1 61  ? 0.149   -3.363  27.815  1.00 39.33 ? 60  GLN   A CA  1 
ATOM   423  C C   . GLN   A 1 61  ? 0.649   -4.519  26.967  1.00 38.63 ? 60  GLN   A C   1 
ATOM   424  O O   . GLN   A 1 61  ? 1.747   -5.015  27.206  1.00 38.00 ? 60  GLN   A O   1 
ATOM   425  C CB  . GLN   A 1 61  ? -0.708  -3.917  28.959  1.00 41.43 ? 60  GLN   A CB  1 
ATOM   426  C CG  . GLN   A 1 61  ? -0.753  -2.997  30.155  1.00 46.34 ? 60  GLN   A CG  1 
ATOM   427  C CD  . GLN   A 1 61  ? -0.074  -3.616  31.346  1.00 52.98 ? 60  GLN   A CD  1 
ATOM   428  O OE1 . GLN   A 1 61  ? 1.155   -3.763  31.385  1.00 55.25 ? 60  GLN   A OE1 1 
ATOM   429  N NE2 . GLN   A 1 61  ? -0.866  -3.969  32.355  1.00 53.41 ? 60  GLN   A NE2 1 
ATOM   430  N N   . LYS   A 1 62  ? -0.162  -4.976  26.006  1.00 38.70 ? 61  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? 0.246   -6.070  25.123  1.00 39.73 ? 61  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? 1.462   -5.680  24.284  1.00 39.63 ? 61  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? 2.326   -6.515  24.017  1.00 39.15 ? 61  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -0.913  -6.487  24.204  1.00 42.82 ? 61  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -1.923  -7.400  24.885  1.00 48.26 ? 61  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -3.119  -7.689  23.987  1.00 53.80 ? 61  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -4.232  -8.369  24.744  1.00 58.02 ? 61  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -5.416  -8.604  23.880  1.00 60.81 ? 61  LYS   A NZ  1 
ATOM   439  N N   . GLU   A 1 63  ? 1.532   -4.402  23.879  1.00 39.58 ? 62  GLU   A N   1 
ATOM   440  C CA  . GLU   A 1 63  ? 2.629   -3.891  23.075  1.00 39.86 ? 62  GLU   A CA  1 
ATOM   441  C C   . GLU   A 1 63  ? 3.880   -3.625  23.907  1.00 40.01 ? 62  GLU   A C   1 
ATOM   442  O O   . GLU   A 1 63  ? 4.975   -3.928  23.447  1.00 40.11 ? 62  GLU   A O   1 
ATOM   443  C CB  . GLU   A 1 63  ? 2.174   -2.669  22.272  1.00 41.97 ? 62  GLU   A CB  1 
ATOM   444  C CG  . GLU   A 1 63  ? 1.002   -3.000  21.362  1.00 46.34 ? 62  GLU   A CG  1 
ATOM   445  C CD  . GLU   A 1 63  ? 1.284   -4.068  20.325  1.00 53.33 ? 62  GLU   A CD  1 
ATOM   446  O OE1 . GLU   A 1 63  ? 0.517   -5.057  20.255  1.00 55.38 ? 62  GLU   A OE1 1 
ATOM   447  O OE2 . GLU   A 1 63  ? 2.272   -3.911  19.573  1.00 54.92 ? 62  GLU   A OE2 1 
ATOM   448  N N   . ILE   A 1 64  ? 3.729   -3.153  25.160  1.00 39.59 ? 63  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 64  ? 4.887   -2.949  26.042  1.00 39.78 ? 63  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 64  ? 5.489   -4.308  26.442  1.00 39.34 ? 63  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 64  ? 6.718   -4.436  26.530  1.00 39.99 ? 63  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 64  ? 4.579   -2.007  27.252  1.00 41.07 ? 63  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 64  ? 4.827   -0.544  26.880  1.00 42.66 ? 63  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 64  ? 5.408   -2.351  28.499  1.00 41.68 ? 63  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 64  ? 3.908   -0.004  25.870  1.00 44.48 ? 63  ILE   A CD1 1 
ATOM   456  N N   . LEU   A 1 65  ? 4.643   -5.345  26.612  1.00 37.90 ? 64  LEU   A N   1 
ATOM   457  C CA  . LEU   A 1 65  ? 5.139   -6.682  26.922  1.00 37.42 ? 64  LEU   A CA  1 
ATOM   458  C C   . LEU   A 1 65  ? 5.992   -7.198  25.751  1.00 37.18 ? 64  LEU   A C   1 
ATOM   459  O O   . LEU   A 1 65  ? 7.060   -7.759  25.979  1.00 37.03 ? 64  LEU   A O   1 
ATOM   460  C CB  . LEU   A 1 65  ? 3.994   -7.654  27.211  1.00 37.61 ? 64  LEU   A CB  1 
ATOM   461  C CG  . LEU   A 1 65  ? 4.439   -9.090  27.507  1.00 39.23 ? 64  LEU   A CG  1 
ATOM   462  C CD1 . LEU   A 1 65  ? 5.294   -9.158  28.769  1.00 39.76 ? 64  LEU   A CD1 1 
ATOM   463  C CD2 . LEU   A 1 65  ? 3.254   -10.021 27.601  1.00 40.01 ? 64  LEU   A CD2 1 
ATOM   464  N N   . ILE   A 1 66  ? 5.554   -6.945  24.507  1.00 36.74 ? 65  ILE   A N   1 
ATOM   465  C CA  . ILE   A 1 66  ? 6.318   -7.324  23.319  1.00 37.27 ? 65  ILE   A CA  1 
ATOM   466  C C   . ILE   A 1 66  ? 7.631   -6.541  23.303  1.00 38.37 ? 65  ILE   A C   1 
ATOM   467  O O   . ILE   A 1 66  ? 8.688   -7.147  23.177  1.00 38.97 ? 65  ILE   A O   1 
ATOM   468  C CB  . ILE   A 1 66  ? 5.484   -7.108  22.034  1.00 37.65 ? 65  ILE   A CB  1 
ATOM   469  C CG1 . ILE   A 1 66  ? 4.380   -8.163  21.913  1.00 38.23 ? 65  ILE   A CG1 1 
ATOM   470  C CG2 . ILE   A 1 66  ? 6.359   -7.107  20.781  1.00 38.42 ? 65  ILE   A CG2 1 
ATOM   471  C CD1 . ILE   A 1 66  ? 3.301   -7.773  20.914  1.00 39.38 ? 65  ILE   A CD1 1 
ATOM   472  N N   . LEU   A 1 67  ? 7.577   -5.219  23.525  1.00 38.64 ? 66  LEU   A N   1 
ATOM   473  C CA  . LEU   A 1 67  ? 8.763   -4.353  23.577  1.00 39.78 ? 66  LEU   A CA  1 
ATOM   474  C C   . LEU   A 1 67  ? 9.824   -4.875  24.549  1.00 39.88 ? 66  LEU   A C   1 
ATOM   475  O O   . LEU   A 1 67  ? 11.021  -4.790  24.271  1.00 40.39 ? 66  LEU   A O   1 
ATOM   476  C CB  . LEU   A 1 67  ? 8.360   -2.929  23.992  1.00 40.48 ? 66  LEU   A CB  1 
ATOM   477  C CG  . LEU   A 1 67  ? 8.447   -1.863  22.920  1.00 42.83 ? 66  LEU   A CG  1 
ATOM   478  C CD1 . LEU   A 1 67  ? 7.947   -0.533  23.443  1.00 43.43 ? 66  LEU   A CD1 1 
ATOM   479  C CD2 . LEU   A 1 67  ? 9.872   -1.709  22.418  1.00 43.90 ? 66  LEU   A CD2 1 
ATOM   480  N N   . LYS   A 1 68  ? 9.371   -5.452  25.664  1.00 39.28 ? 67  LYS   A N   1 
ATOM   481  C CA  . LYS   A 1 68  ? 10.196  -6.005  26.729  1.00 38.94 ? 67  LYS   A CA  1 
ATOM   482  C C   . LYS   A 1 68  ? 10.709  -7.419  26.440  1.00 38.14 ? 67  LYS   A C   1 
ATOM   483  O O   . LYS   A 1 68  ? 11.839  -7.739  26.819  1.00 38.30 ? 67  LYS   A O   1 
ATOM   484  C CB  . LYS   A 1 68  ? 9.385   -6.018  28.033  1.00 41.38 ? 67  LYS   A CB  1 
ATOM   485  C CG  . LYS   A 1 68  ? 10.217  -6.129  29.298  1.00 46.00 ? 67  LYS   A CG  1 
ATOM   486  C CD  . LYS   A 1 68  ? 9.324   -6.296  30.516  1.00 50.64 ? 67  LYS   A CD  1 
ATOM   487  C CE  . LYS   A 1 68  ? 10.120  -6.532  31.772  1.00 54.74 ? 67  LYS   A CE  1 
ATOM   488  N NZ  . LYS   A 1 68  ? 9.245   -6.916  32.914  1.00 56.68 ? 67  LYS   A NZ  1 
ATOM   489  N N   . THR   A 1 69  ? 9.881   -8.282  25.821  1.00 36.88 ? 68  THR   A N   1 
ATOM   490  C CA  . THR   A 1 69  ? 10.296  -9.668  25.582  1.00 36.71 ? 68  THR   A CA  1 
ATOM   491  C C   . THR   A 1 69  ? 11.041  -9.853  24.249  1.00 35.61 ? 68  THR   A C   1 
ATOM   492  O O   . THR   A 1 69  ? 11.839  -10.774 24.134  1.00 36.07 ? 68  THR   A O   1 
ATOM   493  C CB  . THR   A 1 69  ? 9.116   -10.642 25.728  1.00 38.30 ? 68  THR   A CB  1 
ATOM   494  O OG1 . THR   A 1 69  ? 8.099   -10.291 24.793  1.00 39.81 ? 68  THR   A OG1 1 
ATOM   495  C CG2 . THR   A 1 69  ? 8.539   -10.659 27.140  1.00 38.63 ? 68  THR   A CG2 1 
ATOM   496  N N   . CYS   A 1 70  ? 10.788  -9.001  23.254  1.00 34.11 ? 69  CYS   A N   1 
ATOM   497  C CA  . CYS   A 1 70  ? 11.473  -9.090  21.961  1.00 33.42 ? 69  CYS   A CA  1 
ATOM   498  C C   . CYS   A 1 70  ? 12.826  -8.405  22.189  1.00 32.74 ? 69  CYS   A C   1 
ATOM   499  O O   . CYS   A 1 70  ? 12.951  -7.219  21.927  1.00 33.18 ? 69  CYS   A O   1 
ATOM   500  C CB  . CYS   A 1 70  ? 10.653  -8.383  20.884  1.00 34.04 ? 69  CYS   A CB  1 
ATOM   501  S SG  . CYS   A 1 70  ? 11.160  -8.751  19.180  1.00 36.46 ? 69  CYS   A SG  1 
ATOM   502  N N   . ARG   A 1 71  ? 13.806  -9.151  22.754  1.00 31.74 ? 70  ARG   A N   1 
ATOM   503  C CA  . ARG   A 1 71  ? 15.123  -8.677  23.206  1.00 31.41 ? 70  ARG   A CA  1 
ATOM   504  C C   . ARG   A 1 71  ? 16.295  -9.378  22.521  1.00 28.50 ? 70  ARG   A C   1 
ATOM   505  O O   . ARG   A 1 71  ? 16.344  -10.599 22.516  1.00 28.74 ? 70  ARG   A O   1 
ATOM   506  C CB  . ARG   A 1 71  ? 15.271  -9.005  24.707  1.00 34.51 ? 70  ARG   A CB  1 
ATOM   507  C CG  . ARG   A 1 71  ? 15.069  -7.838  25.649  1.00 40.30 ? 70  ARG   A CG  1 
ATOM   508  C CD  . ARG   A 1 71  ? 15.638  -8.142  27.027  1.00 46.24 ? 70  ARG   A CD  1 
ATOM   509  N NE  . ARG   A 1 71  ? 14.838  -9.122  27.763  1.00 51.57 ? 70  ARG   A NE  1 
ATOM   510  C CZ  . ARG   A 1 71  ? 15.227  -10.363 28.037  1.00 55.31 ? 70  ARG   A CZ  1 
ATOM   511  N NH1 . ARG   A 1 71  ? 14.429  -11.182 28.709  1.00 56.03 ? 70  ARG   A NH1 1 
ATOM   512  N NH2 . ARG   A 1 71  ? 16.415  -10.797 27.636  1.00 55.86 ? 70  ARG   A NH2 1 
ATOM   513  N N   . HIS   A 1 72  ? 17.316  -8.618  22.106  1.00 25.77 ? 71  HIS   A N   1 
ATOM   514  C CA  . HIS   A 1 72  ? 18.494  -9.201  21.483  1.00 23.07 ? 71  HIS   A CA  1 
ATOM   515  C C   . HIS   A 1 72  ? 19.651  -8.223  21.598  1.00 21.68 ? 71  HIS   A C   1 
ATOM   516  O O   . HIS   A 1 72  ? 19.430  -7.013  21.577  1.00 21.17 ? 71  HIS   A O   1 
ATOM   517  C CB  . HIS   A 1 72  ? 18.215  -9.524  20.005  1.00 22.51 ? 71  HIS   A CB  1 
ATOM   518  C CG  . HIS   A 1 72  ? 19.312  -10.315 19.357  1.00 22.15 ? 71  HIS   A CG  1 
ATOM   519  N ND1 . HIS   A 1 72  ? 20.382  -9.693  18.737  1.00 22.55 ? 71  HIS   A ND1 1 
ATOM   520  C CD2 . HIS   A 1 72  ? 19.482  -11.656 19.281  1.00 22.17 ? 71  HIS   A CD2 1 
ATOM   521  C CE1 . HIS   A 1 72  ? 21.179  -10.669 18.332  1.00 22.66 ? 71  HIS   A CE1 1 
ATOM   522  N NE2 . HIS   A 1 72  ? 20.654  -11.868 18.591  1.00 22.42 ? 71  HIS   A NE2 1 
ATOM   523  N N   . ALA   A 1 73  ? 20.884  -8.731  21.693  1.00 20.50 ? 72  ALA   A N   1 
ATOM   524  C CA  . ALA   A 1 73  ? 22.058  -7.856  21.798  1.00 20.36 ? 72  ALA   A CA  1 
ATOM   525  C C   . ALA   A 1 73  ? 22.192  -6.859  20.634  1.00 20.18 ? 72  ALA   A C   1 
ATOM   526  O O   . ALA   A 1 73  ? 22.804  -5.817  20.816  1.00 21.82 ? 72  ALA   A O   1 
ATOM   527  C CB  . ALA   A 1 73  ? 23.328  -8.688  21.898  1.00 20.71 ? 72  ALA   A CB  1 
ATOM   528  N N   . ASN   A 1 74  ? 21.667  -7.176  19.451  1.00 17.90 ? 73  ASN   A N   1 
ATOM   529  C CA  . ASN   A 1 74  ? 21.748  -6.287  18.289  1.00 17.01 ? 73  ASN   A CA  1 
ATOM   530  C C   . ASN   A 1 74  ? 20.508  -5.417  18.069  1.00 17.61 ? 73  ASN   A C   1 
ATOM   531  O O   . ASN   A 1 74  ? 20.276  -4.967  16.952  1.00 16.86 ? 73  ASN   A O   1 
ATOM   532  C CB  . ASN   A 1 74  ? 22.093  -7.060  17.009  1.00 16.66 ? 73  ASN   A CB  1 
ATOM   533  C CG  . ASN   A 1 74  ? 23.472  -7.651  17.103  1.00 18.05 ? 73  ASN   A CG  1 
ATOM   534  O OD1 . ASN   A 1 74  ? 23.658  -8.885  17.122  1.00 18.48 ? 73  ASN   A OD1 1 
ATOM   535  N ND2 . ASN   A 1 74  ? 24.471  -6.764  17.199  1.00 17.79 ? 73  ASN   A ND2 1 
ATOM   536  N N   . ILE   A 1 75  ? 19.684  -5.237  19.100  1.00 18.18 ? 74  ILE   A N   1 
ATOM   537  C CA  . ILE   A 1 75  ? 18.519  -4.343  19.064  1.00 19.89 ? 74  ILE   A CA  1 
ATOM   538  C C   . ILE   A 1 75  ? 18.655  -3.468  20.301  1.00 21.59 ? 74  ILE   A C   1 
ATOM   539  O O   . ILE   A 1 75  ? 18.934  -3.988  21.390  1.00 22.07 ? 74  ILE   A O   1 
ATOM   540  C CB  . ILE   A 1 75  ? 17.169  -5.108  19.056  1.00 20.97 ? 74  ILE   A CB  1 
ATOM   541  C CG1 . ILE   A 1 75  ? 17.062  -6.024  17.830  1.00 22.20 ? 74  ILE   A CG1 1 
ATOM   542  C CG2 . ILE   A 1 75  ? 15.952  -4.154  19.138  1.00 22.35 ? 74  ILE   A CG2 1 
ATOM   543  C CD1 . ILE   A 1 75  ? 15.941  -7.014  17.947  1.00 23.73 ? 74  ILE   A CD1 1 
ATOM   544  N N   . VAL   A 1 76  ? 18.443  -2.132  20.166  1.00 21.70 ? 75  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 76  ? 18.557  -1.210  21.302  1.00 23.90 ? 75  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 76  ? 17.648  -1.662  22.444  1.00 25.25 ? 75  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 76  ? 16.472  -1.931  22.211  1.00 25.54 ? 75  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 76  ? 18.245  0.239   20.868  1.00 25.45 ? 75  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 76  ? 18.165  1.161   22.077  1.00 26.94 ? 75  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 76  ? 19.294  0.738   19.887  1.00 25.90 ? 75  VAL   A CG2 1 
ATOM   551  N N   . ALA   A 1 77  ? 18.230  -1.862  23.618  1.00 26.58 ? 76  ALA   A N   1 
ATOM   552  C CA  . ALA   A 1 77  ? 17.517  -2.380  24.779  1.00 28.44 ? 76  ALA   A CA  1 
ATOM   553  C C   . ALA   A 1 77  ? 16.430  -1.453  25.303  1.00 29.81 ? 76  ALA   A C   1 
ATOM   554  O O   . ALA   A 1 77  ? 16.594  -0.241  25.312  1.00 29.58 ? 76  ALA   A O   1 
ATOM   555  C CB  . ALA   A 1 77  ? 18.502  -2.699  25.890  1.00 29.11 ? 76  ALA   A CB  1 
ATOM   556  N N   . TYR   A 1 78  ? 15.329  -2.051  25.745  1.00 30.81 ? 77  TYR   A N   1 
ATOM   557  C CA  . TYR   A 1 78  ? 14.203  -1.371  26.363  1.00 32.30 ? 77  TYR   A CA  1 
ATOM   558  C C   . TYR   A 1 78  ? 14.437  -1.397  27.891  1.00 32.85 ? 77  TYR   A C   1 
ATOM   559  O O   . TYR   A 1 78  ? 14.828  -2.429  28.437  1.00 32.53 ? 77  TYR   A O   1 
ATOM   560  C CB  . TYR   A 1 78  ? 12.903  -2.094  25.974  1.00 33.02 ? 77  TYR   A CB  1 
ATOM   561  C CG  . TYR   A 1 78  ? 11.711  -1.761  26.836  1.00 34.30 ? 77  TYR   A CG  1 
ATOM   562  C CD1 . TYR   A 1 78  ? 10.950  -0.627  26.596  1.00 35.65 ? 77  TYR   A CD1 1 
ATOM   563  C CD2 . TYR   A 1 78  ? 11.320  -2.600  27.871  1.00 35.39 ? 77  TYR   A CD2 1 
ATOM   564  C CE1 . TYR   A 1 78  ? 9.842   -0.324  27.377  1.00 36.62 ? 77  TYR   A CE1 1 
ATOM   565  C CE2 . TYR   A 1 78  ? 10.231  -2.294  28.675  1.00 36.44 ? 77  TYR   A CE2 1 
ATOM   566  C CZ  . TYR   A 1 78  ? 9.485   -1.162  28.414  1.00 37.81 ? 77  TYR   A CZ  1 
ATOM   567  O OH  . TYR   A 1 78  ? 8.397   -0.867  29.197  1.00 39.73 ? 77  TYR   A OH  1 
ATOM   568  N N   . HIS   A 1 79  ? 14.207  -0.274  28.574  1.00 33.30 ? 78  HIS   A N   1 
ATOM   569  C CA  . HIS   A 1 79  ? 14.441  -0.186  30.019  1.00 34.73 ? 78  HIS   A CA  1 
ATOM   570  C C   . HIS   A 1 79  ? 13.169  -0.047  30.837  1.00 34.99 ? 78  HIS   A C   1 
ATOM   571  O O   . HIS   A 1 79  ? 13.099  -0.545  31.955  1.00 35.94 ? 78  HIS   A O   1 
ATOM   572  C CB  . HIS   A 1 79  ? 15.386  0.981   30.355  1.00 36.43 ? 78  HIS   A CB  1 
ATOM   573  C CG  . HIS   A 1 79  ? 16.776  0.816   29.831  1.00 40.60 ? 78  HIS   A CG  1 
ATOM   574  N ND1 . HIS   A 1 79  ? 17.335  -0.438  29.648  1.00 43.19 ? 78  HIS   A ND1 1 
ATOM   575  C CD2 . HIS   A 1 79  ? 17.692  1.757   29.502  1.00 42.26 ? 78  HIS   A CD2 1 
ATOM   576  C CE1 . HIS   A 1 79  ? 18.559  -0.222  29.192  1.00 44.09 ? 78  HIS   A CE1 1 
ATOM   577  N NE2 . HIS   A 1 79  ? 18.819  1.084   29.086  1.00 43.91 ? 78  HIS   A NE2 1 
ATOM   578  N N   . GLY   A 1 80  ? 12.191  0.655   30.299  1.00 34.26 ? 79  GLY   A N   1 
ATOM   579  C CA  . GLY   A 1 80  ? 10.936  0.898   31.002  1.00 34.04 ? 79  GLY   A CA  1 
ATOM   580  C C   . GLY   A 1 80  ? 10.028  1.857   30.259  1.00 33.74 ? 79  GLY   A C   1 
ATOM   581  O O   . GLY   A 1 80  ? 10.433  2.438   29.250  1.00 32.81 ? 79  GLY   A O   1 
ATOM   582  N N   . SER   A 1 81  ? 8.777   2.010   30.724  1.00 34.05 ? 80  SER   A N   1 
ATOM   583  C CA  . SER   A 1 81  ? 7.833   2.917   30.059  1.00 34.62 ? 80  SER   A CA  1 
ATOM   584  C C   . SER   A 1 81  ? 6.958   3.697   31.021  1.00 34.86 ? 80  SER   A C   1 
ATOM   585  O O   . SER   A 1 81  ? 6.765   3.294   32.164  1.00 35.42 ? 80  SER   A O   1 
ATOM   586  C CB  . SER   A 1 81  ? 6.984   2.194   29.019  1.00 36.68 ? 80  SER   A CB  1 
ATOM   587  O OG  . SER   A 1 81  ? 6.177   1.191   29.613  1.00 40.21 ? 80  SER   A OG  1 
ATOM   588  N N   . TYR   A 1 82  ? 6.485   4.858   30.567  1.00 34.51 ? 81  TYR   A N   1 
ATOM   589  C CA  . TYR   A 1 82  ? 5.663   5.759   31.360  1.00 35.23 ? 81  TYR   A CA  1 
ATOM   590  C C   . TYR   A 1 82  ? 4.470   6.193   30.549  1.00 36.57 ? 81  TYR   A C   1 
ATOM   591  O O   . TYR   A 1 82  ? 4.614   6.559   29.385  1.00 36.47 ? 81  TYR   A O   1 
ATOM   592  C CB  . TYR   A 1 82  ? 6.474   7.013   31.746  1.00 34.90 ? 81  TYR   A CB  1 
ATOM   593  C CG  . TYR   A 1 82  ? 7.659   6.680   32.617  1.00 35.31 ? 81  TYR   A CG  1 
ATOM   594  C CD1 . TYR   A 1 82  ? 8.830   6.173   32.069  1.00 35.97 ? 81  TYR   A CD1 1 
ATOM   595  C CD2 . TYR   A 1 82  ? 7.601   6.841   33.994  1.00 36.10 ? 81  TYR   A CD2 1 
ATOM   596  C CE1 . TYR   A 1 82  ? 9.892   5.787   32.873  1.00 36.91 ? 81  TYR   A CE1 1 
ATOM   597  C CE2 . TYR   A 1 82  ? 8.670   6.491   34.804  1.00 36.84 ? 81  TYR   A CE2 1 
ATOM   598  C CZ  . TYR   A 1 82  ? 9.811   5.956   34.240  1.00 37.79 ? 81  TYR   A CZ  1 
ATOM   599  O OH  . TYR   A 1 82  ? 10.869  5.592   35.031  1.00 39.72 ? 81  TYR   A OH  1 
ATOM   600  N N   . LEU   A 1 83  ? 3.298   6.182   31.163  1.00 37.15 ? 82  LEU   A N   1 
ATOM   601  C CA  . LEU   A 1 83  ? 2.096   6.673   30.521  1.00 38.64 ? 82  LEU   A CA  1 
ATOM   602  C C   . LEU   A 1 83  ? 1.852   8.029   31.156  1.00 40.15 ? 82  LEU   A C   1 
ATOM   603  O O   . LEU   A 1 83  ? 1.602   8.106   32.363  1.00 39.95 ? 82  LEU   A O   1 
ATOM   604  C CB  . LEU   A 1 83  ? 0.909   5.734   30.775  1.00 39.32 ? 82  LEU   A CB  1 
ATOM   605  C CG  . LEU   A 1 83  ? -0.395  6.109   30.078  1.00 41.50 ? 82  LEU   A CG  1 
ATOM   606  C CD1 . LEU   A 1 83  ? -0.205  6.241   28.562  1.00 42.00 ? 82  LEU   A CD1 1 
ATOM   607  C CD2 . LEU   A 1 83  ? -1.465  5.079   30.365  1.00 42.78 ? 82  LEU   A CD2 1 
ATOM   608  N N   . TRP   A 1 84  ? 1.988   9.107   30.371  1.00 40.98 ? 83  TRP   A N   1 
ATOM   609  C CA  . TRP   A 1 84  ? 1.823   10.452  30.912  1.00 42.35 ? 83  TRP   A CA  1 
ATOM   610  C C   . TRP   A 1 84  ? 1.203   11.392  29.890  1.00 42.78 ? 83  TRP   A C   1 
ATOM   611  O O   . TRP   A 1 84  ? 1.745   11.544  28.795  1.00 42.58 ? 83  TRP   A O   1 
ATOM   612  C CB  . TRP   A 1 84  ? 3.183   10.987  31.388  1.00 42.77 ? 83  TRP   A CB  1 
ATOM   613  C CG  . TRP   A 1 84  ? 3.137   12.356  31.996  1.00 43.79 ? 83  TRP   A CG  1 
ATOM   614  C CD1 . TRP   A 1 84  ? 3.587   13.515  31.438  1.00 44.97 ? 83  TRP   A CD1 1 
ATOM   615  C CD2 . TRP   A 1 84  ? 2.647   12.700  33.298  1.00 44.27 ? 83  TRP   A CD2 1 
ATOM   616  N NE1 . TRP   A 1 84  ? 3.398   14.564  32.309  1.00 45.48 ? 83  TRP   A NE1 1 
ATOM   617  C CE2 . TRP   A 1 84  ? 2.823   14.090  33.459  1.00 45.17 ? 83  TRP   A CE2 1 
ATOM   618  C CE3 . TRP   A 1 84  ? 2.054   11.973  34.336  1.00 44.85 ? 83  TRP   A CE3 1 
ATOM   619  C CZ2 . TRP   A 1 84  ? 2.454   14.758  34.625  1.00 45.86 ? 83  TRP   A CZ2 1 
ATOM   620  C CZ3 . TRP   A 1 84  ? 1.711   12.635  35.497  1.00 45.81 ? 83  TRP   A CZ3 1 
ATOM   621  C CH2 . TRP   A 1 84  ? 1.899   14.012  35.629  1.00 46.03 ? 83  TRP   A CH2 1 
ATOM   622  N N   . LEU   A 1 85  ? 0.062   12.011  30.250  1.00 42.96 ? 84  LEU   A N   1 
ATOM   623  C CA  . LEU   A 1 85  ? -0.669  12.962  29.410  1.00 43.85 ? 84  LEU   A CA  1 
ATOM   624  C C   . LEU   A 1 85  ? -0.993  12.403  28.013  1.00 44.01 ? 84  LEU   A C   1 
ATOM   625  O O   . LEU   A 1 85  ? -0.702  13.056  27.009  1.00 44.13 ? 84  LEU   A O   1 
ATOM   626  C CB  . LEU   A 1 85  ? 0.093   14.300  29.311  1.00 44.41 ? 84  LEU   A CB  1 
ATOM   627  C CG  . LEU   A 1 85  ? 0.501   14.944  30.634  1.00 46.38 ? 84  LEU   A CG  1 
ATOM   628  C CD1 . LEU   A 1 85  ? 1.319   16.201  30.394  1.00 46.86 ? 84  LEU   A CD1 1 
ATOM   629  C CD2 . LEU   A 1 85  ? -0.715  15.266  31.489  1.00 47.17 ? 84  LEU   A CD2 1 
ATOM   630  N N   . GLN   A 1 86  ? -1.596  11.193  27.951  1.00 43.95 ? 85  GLN   A N   1 
ATOM   631  C CA  . GLN   A 1 86  ? -1.951  10.528  26.683  1.00 44.22 ? 85  GLN   A CA  1 
ATOM   632  C C   . GLN   A 1 86  ? -0.738  10.203  25.802  1.00 43.40 ? 85  GLN   A C   1 
ATOM   633  O O   . GLN   A 1 86  ? -0.881  10.025  24.593  1.00 43.93 ? 85  GLN   A O   1 
ATOM   634  C CB  . GLN   A 1 86  ? -2.961  11.362  25.876  1.00 47.07 ? 85  GLN   A CB  1 
ATOM   635  C CG  . GLN   A 1 86  ? -4.414  11.103  26.212  1.00 52.66 ? 85  GLN   A CG  1 
ATOM   636  C CD  . GLN   A 1 86  ? -5.037  10.194  25.187  1.00 58.30 ? 85  GLN   A CD  1 
ATOM   637  O OE1 . GLN   A 1 86  ? -4.477  9.154   24.826  1.00 60.65 ? 85  GLN   A OE1 1 
ATOM   638  N NE2 . GLN   A 1 86  ? -6.212  10.564  24.695  1.00 58.50 ? 85  GLN   A NE2 1 
ATOM   639  N N   . LYS   A 1 87  ? 0.455   10.166  26.391  1.00 41.88 ? 86  LYS   A N   1 
ATOM   640  C CA  . LYS   A 1 87  ? 1.676   9.869   25.661  1.00 40.92 ? 86  LYS   A CA  1 
ATOM   641  C C   . LYS   A 1 87  ? 2.408   8.730   26.342  1.00 39.43 ? 86  LYS   A C   1 
ATOM   642  O O   . LYS   A 1 87  ? 2.362   8.593   27.568  1.00 39.56 ? 86  LYS   A O   1 
ATOM   643  C CB  . LYS   A 1 87  ? 2.579   11.110  25.557  1.00 42.87 ? 86  LYS   A CB  1 
ATOM   644  C CG  . LYS   A 1 87  ? 1.997   12.199  24.654  1.00 47.79 ? 86  LYS   A CG  1 
ATOM   645  C CD  . LYS   A 1 87  ? 2.704   13.539  24.814  1.00 52.98 ? 86  LYS   A CD  1 
ATOM   646  C CE  . LYS   A 1 87  ? 2.596   14.087  26.219  1.00 56.95 ? 86  LYS   A CE  1 
ATOM   647  N NZ  . LYS   A 1 87  ? 2.970   15.524  26.292  1.00 58.73 ? 86  LYS   A NZ  1 
ATOM   648  N N   . LEU   A 1 88  ? 3.053   7.897   25.545  1.00 37.48 ? 87  LEU   A N   1 
ATOM   649  C CA  . LEU   A 1 88  ? 3.814   6.779   26.062  1.00 36.49 ? 87  LEU   A CA  1 
ATOM   650  C C   . LEU   A 1 88  ? 5.272   7.144   25.929  1.00 35.67 ? 87  LEU   A C   1 
ATOM   651  O O   . LEU   A 1 88  ? 5.744   7.363   24.816  1.00 36.62 ? 87  LEU   A O   1 
ATOM   652  C CB  . LEU   A 1 88  ? 3.536   5.520   25.242  1.00 36.53 ? 87  LEU   A CB  1 
ATOM   653  C CG  . LEU   A 1 88  ? 4.313   4.292   25.678  1.00 38.39 ? 87  LEU   A CG  1 
ATOM   654  C CD1 . LEU   A 1 88  ? 3.701   3.677   26.940  1.00 39.12 ? 87  LEU   A CD1 1 
ATOM   655  C CD2 . LEU   A 1 88  ? 4.373   3.287   24.565  1.00 39.15 ? 87  LEU   A CD2 1 
ATOM   656  N N   . TRP   A 1 89  ? 5.987   7.216   27.041  1.00 33.72 ? 88  TRP   A N   1 
ATOM   657  C CA  . TRP   A 1 89  ? 7.409   7.509   27.026  1.00 32.83 ? 88  TRP   A CA  1 
ATOM   658  C C   . TRP   A 1 89  ? 8.161   6.208   27.202  1.00 31.60 ? 88  TRP   A C   1 
ATOM   659  O O   . TRP   A 1 89  ? 7.949   5.502   28.181  1.00 31.39 ? 88  TRP   A O   1 
ATOM   660  C CB  . TRP   A 1 89  ? 7.778   8.455   28.159  1.00 32.74 ? 88  TRP   A CB  1 
ATOM   661  C CG  . TRP   A 1 89  ? 7.366   9.871   27.932  1.00 33.47 ? 88  TRP   A CG  1 
ATOM   662  C CD1 . TRP   A 1 89  ? 6.146   10.424  28.188  1.00 34.41 ? 88  TRP   A CD1 1 
ATOM   663  C CD2 . TRP   A 1 89  ? 8.214   10.943  27.509  1.00 33.58 ? 88  TRP   A CD2 1 
ATOM   664  N NE1 . TRP   A 1 89  ? 6.168   11.767  27.901  1.00 34.73 ? 88  TRP   A NE1 1 
ATOM   665  C CE2 . TRP   A 1 89  ? 7.434   12.117  27.503  1.00 34.34 ? 88  TRP   A CE2 1 
ATOM   666  C CE3 . TRP   A 1 89  ? 9.557   11.026  27.125  1.00 33.96 ? 88  TRP   A CE3 1 
ATOM   667  C CZ2 . TRP   A 1 89  ? 7.955   13.353  27.127  1.00 34.87 ? 88  TRP   A CZ2 1 
ATOM   668  C CZ3 . TRP   A 1 89  ? 10.066  12.249  26.742  1.00 34.55 ? 88  TRP   A CZ3 1 
ATOM   669  C CH2 . TRP   A 1 89  ? 9.272   13.397  26.755  1.00 34.78 ? 88  TRP   A CH2 1 
ATOM   670  N N   . ILE   A 1 90  ? 9.031   5.888   26.262  1.00 30.17 ? 89  ILE   A N   1 
ATOM   671  C CA  . ILE   A 1 90  ? 9.816   4.663   26.303  1.00 30.06 ? 89  ILE   A CA  1 
ATOM   672  C C   . ILE   A 1 90  ? 11.265  4.970   26.640  1.00 29.39 ? 89  ILE   A C   1 
ATOM   673  O O   . ILE   A 1 90  ? 11.902  5.769   25.962  1.00 28.92 ? 89  ILE   A O   1 
ATOM   674  C CB  . ILE   A 1 90  ? 9.694   3.928   24.951  1.00 31.34 ? 89  ILE   A CB  1 
ATOM   675  C CG1 . ILE   A 1 90  ? 8.236   3.506   24.706  1.00 33.40 ? 89  ILE   A CG1 1 
ATOM   676  C CG2 . ILE   A 1 90  ? 10.644  2.724   24.880  1.00 32.13 ? 89  ILE   A CG2 1 
ATOM   677  C CD1 . ILE   A 1 90  ? 7.904   3.201   23.281  1.00 35.60 ? 89  ILE   A CD1 1 
ATOM   678  N N   . CYS   A 1 91  ? 11.798  4.318   27.670  1.00 29.04 ? 90  CYS   A N   1 
ATOM   679  C CA  . CYS   A 1 91  ? 13.192  4.484   28.037  1.00 28.72 ? 90  CYS   A CA  1 
ATOM   680  C C   . CYS   A 1 91  ? 14.004  3.423   27.328  1.00 28.18 ? 90  CYS   A C   1 
ATOM   681  O O   . CYS   A 1 91  ? 13.675  2.239   27.397  1.00 27.71 ? 90  CYS   A O   1 
ATOM   682  C CB  . CYS   A 1 91  ? 13.390  4.415   29.543  1.00 30.03 ? 90  CYS   A CB  1 
ATOM   683  S SG  . CYS   A 1 91  ? 15.097  4.705   30.055  1.00 34.67 ? 90  CYS   A SG  1 
ATOM   684  N N   . MET   A 1 92  ? 15.056  3.845   26.644  1.00 27.52 ? 91  MET   A N   1 
ATOM   685  C CA  . MET   A 1 92  ? 15.876  2.917   25.880  1.00 27.84 ? 91  MET   A CA  1 
ATOM   686  C C   . MET   A 1 92  ? 17.364  3.179   26.039  1.00 27.77 ? 91  MET   A C   1 
ATOM   687  O O   . MET   A 1 92  ? 17.774  4.238   26.519  1.00 27.47 ? 91  MET   A O   1 
ATOM   688  C CB  . MET   A 1 92  ? 15.439  2.892   24.396  1.00 28.45 ? 91  MET   A CB  1 
ATOM   689  C CG  . MET   A 1 92  ? 15.691  4.167   23.637  1.00 29.89 ? 91  MET   A CG  1 
ATOM   690  S SD  . MET   A 1 92  ? 14.671  4.347   22.131  1.00 31.77 ? 91  MET   A SD  1 
ATOM   691  C CE  . MET   A 1 92  ? 15.190  2.925   21.222  1.00 34.81 ? 91  MET   A CE  1 
ATOM   692  N N   . GLU   A 1 93  ? 18.178  2.186   25.655  1.00 28.02 ? 92  GLU   A N   1 
ATOM   693  C CA  . GLU   A 1 93  ? 19.623  2.251   25.705  1.00 28.68 ? 92  GLU   A CA  1 
ATOM   694  C C   . GLU   A 1 93  ? 20.128  3.437   24.851  1.00 29.16 ? 92  GLU   A C   1 
ATOM   695  O O   . GLU   A 1 93  ? 19.645  3.664   23.736  1.00 29.47 ? 92  GLU   A O   1 
ATOM   696  C CB  . GLU   A 1 93  ? 20.173  0.878   25.229  1.00 30.89 ? 92  GLU   A CB  1 
ATOM   697  C CG  . GLU   A 1 93  ? 21.586  0.819   24.688  1.00 35.44 ? 92  GLU   A CG  1 
ATOM   698  C CD  . GLU   A 1 93  ? 21.988  -0.557  24.170  1.00 40.24 ? 92  GLU   A CD  1 
ATOM   699  O OE1 . GLU   A 1 93  ? 23.206  -0.784  23.997  1.00 44.32 ? 92  GLU   A OE1 1 
ATOM   700  O OE2 . GLU   A 1 93  ? 21.096  -1.407  23.934  1.00 37.67 ? 92  GLU   A OE2 1 
ATOM   701  N N   . PHE   A 1 94  ? 21.021  4.240   25.419  1.00 28.53 ? 93  PHE   A N   1 
ATOM   702  C CA  . PHE   A 1 94  ? 21.594  5.399   24.754  1.00 28.68 ? 93  PHE   A CA  1 
ATOM   703  C C   . PHE   A 1 94  ? 22.713  4.963   23.811  1.00 28.38 ? 93  PHE   A C   1 
ATOM   704  O O   . PHE   A 1 94  ? 23.657  4.321   24.251  1.00 28.96 ? 93  PHE   A O   1 
ATOM   705  C CB  . PHE   A 1 94  ? 22.162  6.363   25.792  1.00 29.08 ? 93  PHE   A CB  1 
ATOM   706  C CG  . PHE   A 1 94  ? 22.679  7.658   25.220  1.00 29.44 ? 93  PHE   A CG  1 
ATOM   707  C CD1 . PHE   A 1 94  ? 21.808  8.611   24.725  1.00 30.40 ? 93  PHE   A CD1 1 
ATOM   708  C CD2 . PHE   A 1 94  ? 24.033  7.943   25.221  1.00 30.52 ? 93  PHE   A CD2 1 
ATOM   709  C CE1 . PHE   A 1 94  ? 22.281  9.820   24.227  1.00 31.18 ? 93  PHE   A CE1 1 
ATOM   710  C CE2 . PHE   A 1 94  ? 24.506  9.154   24.723  1.00 31.27 ? 93  PHE   A CE2 1 
ATOM   711  C CZ  . PHE   A 1 94  ? 23.629  10.080  24.223  1.00 31.08 ? 93  PHE   A CZ  1 
ATOM   712  N N   . CYS   A 1 95  ? 22.609  5.305   22.524  1.00 26.92 ? 94  CYS   A N   1 
ATOM   713  C CA  . CYS   A 1 95  ? 23.639  4.956   21.548  1.00 26.10 ? 94  CYS   A CA  1 
ATOM   714  C C   . CYS   A 1 95  ? 24.351  6.240   21.172  1.00 25.14 ? 94  CYS   A C   1 
ATOM   715  O O   . CYS   A 1 95  ? 23.896  6.971   20.301  1.00 25.19 ? 94  CYS   A O   1 
ATOM   716  C CB  . CYS   A 1 95  ? 23.016  4.275   20.337  1.00 25.80 ? 94  CYS   A CB  1 
ATOM   717  S SG  . CYS   A 1 95  ? 22.334  2.636   20.698  1.00 27.07 ? 94  CYS   A SG  1 
ATOM   718  N N   . GLY   A 1 96  ? 25.451  6.503   21.862  1.00 24.68 ? 95  GLY   A N   1 
ATOM   719  C CA  . GLY   A 1 96  ? 26.209  7.752   21.772  1.00 24.85 ? 95  GLY   A CA  1 
ATOM   720  C C   . GLY   A 1 96  ? 26.647  8.297   20.425  1.00 24.48 ? 95  GLY   A C   1 
ATOM   721  O O   . GLY   A 1 96  ? 26.808  9.507   20.295  1.00 25.01 ? 95  GLY   A O   1 
ATOM   722  N N   . ALA   A 1 97  ? 26.922  7.430   19.435  1.00 23.73 ? 96  ALA   A N   1 
ATOM   723  C CA  . ALA   A 1 97  ? 27.379  7.908   18.125  1.00 22.82 ? 96  ALA   A CA  1 
ATOM   724  C C   . ALA   A 1 97  ? 26.268  8.118   17.099  1.00 22.72 ? 96  ALA   A C   1 
ATOM   725  O O   . ALA   A 1 97  ? 26.562  8.433   15.945  1.00 22.71 ? 96  ALA   A O   1 
ATOM   726  C CB  . ALA   A 1 97  ? 28.451  6.985   17.564  1.00 22.77 ? 96  ALA   A CB  1 
ATOM   727  N N   . GLY   A 1 98  ? 25.010  7.963   17.511  1.00 22.03 ? 97  GLY   A N   1 
ATOM   728  C CA  . GLY   A 1 98  ? 23.894  8.153   16.602  1.00 21.44 ? 97  GLY   A CA  1 
ATOM   729  C C   . GLY   A 1 98  ? 23.798  7.038   15.586  1.00 20.44 ? 97  GLY   A C   1 
ATOM   730  O O   . GLY   A 1 98  ? 24.239  5.921   15.841  1.00 20.35 ? 97  GLY   A O   1 
ATOM   731  N N   . SER   A 1 99  ? 23.179  7.318   14.440  1.00 19.02 ? 98  SER   A N   1 
ATOM   732  C CA  . SER   A 1 99  ? 22.995  6.312   13.402  1.00 18.07 ? 98  SER   A CA  1 
ATOM   733  C C   . SER   A 1 99  ? 24.229  6.199   12.495  1.00 17.90 ? 98  SER   A C   1 
ATOM   734  O O   . SER   A 1 99  ? 25.081  7.085   12.472  1.00 18.39 ? 98  SER   A O   1 
ATOM   735  C CB  . SER   A 1 99  ? 21.765  6.671   12.563  1.00 18.49 ? 98  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 99  ? 22.066  7.640   11.567  1.00 19.67 ? 98  SER   A OG  1 
ATOM   737  N N   . LEU   A 1 100 ? 24.274  5.141   11.681  1.00 16.93 ? 99  LEU   A N   1 
ATOM   738  C CA  . LEU   A 1 100 ? 25.302  4.995   10.667  1.00 16.12 ? 99  LEU   A CA  1 
ATOM   739  C C   . LEU   A 1 100 ? 25.224  6.123   9.644   1.00 15.31 ? 99  LEU   A C   1 
ATOM   740  O O   . LEU   A 1 100 ? 26.272  6.548   9.188   1.00 16.01 ? 99  LEU   A O   1 
ATOM   741  C CB  . LEU   A 1 100 ? 25.238  3.629   9.986   1.00 15.41 ? 99  LEU   A CB  1 
ATOM   742  C CG  . LEU   A 1 100 ? 25.910  2.511   10.806  1.00 17.16 ? 99  LEU   A CG  1 
ATOM   743  C CD1 . LEU   A 1 100 ? 25.638  1.190   10.184  1.00 18.02 ? 99  LEU   A CD1 1 
ATOM   744  C CD2 . LEU   A 1 100 ? 27.413  2.746   10.932  1.00 17.43 ? 99  LEU   A CD2 1 
ATOM   745  N N   . GLN   A 1 101 ? 24.027  6.675   9.367   1.00 15.42 ? 100 GLN   A N   1 
ATOM   746  C CA  . GLN   A 1 101 ? 23.902  7.825   8.453   1.00 15.23 ? 100 GLN   A CA  1 
ATOM   747  C C   . GLN   A 1 101 ? 24.549  9.056   9.054   1.00 15.11 ? 100 GLN   A C   1 
ATOM   748  O O   . GLN   A 1 101 ? 25.276  9.776   8.370   1.00 15.70 ? 100 GLN   A O   1 
ATOM   749  C CB  . GLN   A 1 101 ? 22.449  8.117   8.081   1.00 16.27 ? 100 GLN   A CB  1 
ATOM   750  C CG  . GLN   A 1 101 ? 22.347  9.265   7.058   1.00 16.62 ? 100 GLN   A CG  1 
ATOM   751  C CD  . GLN   A 1 101 ? 20.954  9.689   6.734   1.00 18.05 ? 100 GLN   A CD  1 
ATOM   752  O OE1 . GLN   A 1 101 ? 20.671  10.896  6.623   1.00 22.88 ? 100 GLN   A OE1 1 
ATOM   753  N NE2 . GLN   A 1 101 ? 20.051  8.745   6.545   1.00 14.39 ? 100 GLN   A NE2 1 
ATOM   754  N N   . ASP   A 1 102 ? 24.345  9.272   10.355  1.00 15.25 ? 101 ASP   A N   1 
ATOM   755  C CA  . ASP   A 1 102 ? 24.967  10.400  11.056  1.00 16.56 ? 101 ASP   A CA  1 
ATOM   756  C C   . ASP   A 1 102 ? 26.488  10.309  10.983  1.00 18.49 ? 101 ASP   A C   1 
ATOM   757  O O   . ASP   A 1 102 ? 27.173  11.321  10.797  1.00 19.22 ? 101 ASP   A O   1 
ATOM   758  C CB  . ASP   A 1 102 ? 24.514  10.437  12.522  1.00 17.85 ? 101 ASP   A CB  1 
ATOM   759  C CG  . ASP   A 1 102 ? 23.021  10.612  12.664  1.00 20.53 ? 101 ASP   A CG  1 
ATOM   760  O OD1 . ASP   A 1 102 ? 22.429  11.358  11.849  1.00 21.52 ? 101 ASP   A OD1 1 
ATOM   761  O OD2 . ASP   A 1 102 ? 22.441  10.003  13.583  1.00 20.98 ? 101 ASP   A OD2 1 
ATOM   762  N N   . ILE   A 1 103 ? 27.018  9.082   11.075  1.00 18.53 ? 102 ILE   A N   1 
ATOM   763  C CA  . ILE   A 1 103 ? 28.442  8.861   10.998  1.00 18.43 ? 102 ILE   A CA  1 
ATOM   764  C C   . ILE   A 1 103 ? 28.977  9.054   9.580   1.00 17.97 ? 102 ILE   A C   1 
ATOM   765  O O   . ILE   A 1 103 ? 29.910  9.834   9.408   1.00 18.75 ? 102 ILE   A O   1 
ATOM   766  C CB  . ILE   A 1 103 ? 28.783  7.467   11.581  1.00 18.57 ? 102 ILE   A CB  1 
ATOM   767  C CG1 . ILE   A 1 103 ? 28.421  7.420   13.102  1.00 18.97 ? 102 ILE   A CG1 1 
ATOM   768  C CG2 . ILE   A 1 103 ? 30.272  7.113   11.355  1.00 19.59 ? 102 ILE   A CG2 1 
ATOM   769  C CD1 . ILE   A 1 103 ? 28.306  6.009   13.680  1.00 18.87 ? 102 ILE   A CD1 1 
ATOM   770  N N   . TYR   A 1 104 ? 28.406  8.374   8.574   1.00 17.10 ? 103 TYR   A N   1 
ATOM   771  C CA  . TYR   A 1 104 ? 28.960  8.452   7.209   1.00 16.66 ? 103 TYR   A CA  1 
ATOM   772  C C   . TYR   A 1 104 ? 28.794  9.846   6.594   1.00 16.78 ? 103 TYR   A C   1 
ATOM   773  O O   . TYR   A 1 104 ? 29.581  10.188  5.710   1.00 16.96 ? 103 TYR   A O   1 
ATOM   774  C CB  . TYR   A 1 104 ? 28.529  7.317   6.245   1.00 15.62 ? 103 TYR   A CB  1 
ATOM   775  C CG  . TYR   A 1 104 ? 27.084  7.278   5.762   1.00 14.64 ? 103 TYR   A CG  1 
ATOM   776  C CD1 . TYR   A 1 104 ? 26.563  8.298   4.979   1.00 14.99 ? 103 TYR   A CD1 1 
ATOM   777  C CD2 . TYR   A 1 104 ? 26.285  6.161   5.980   1.00 14.60 ? 103 TYR   A CD2 1 
ATOM   778  C CE1 . TYR   A 1 104 ? 25.259  8.257   4.506   1.00 14.39 ? 103 TYR   A CE1 1 
ATOM   779  C CE2 . TYR   A 1 104 ? 24.982  6.097   5.492   1.00 14.71 ? 103 TYR   A CE2 1 
ATOM   780  C CZ  . TYR   A 1 104 ? 24.467  7.154   4.767   1.00 14.78 ? 103 TYR   A CZ  1 
ATOM   781  O OH  . TYR   A 1 104 ? 23.188  7.119   4.264   1.00 15.14 ? 103 TYR   A OH  1 
ATOM   782  N N   . GLN   A 1 105 ? 27.812  10.652  7.076   1.00 16.16 ? 104 GLN   A N   1 
ATOM   783  C CA  . GLN   A 1 105 ? 27.671  12.017  6.588   1.00 16.37 ? 104 GLN   A CA  1 
ATOM   784  C C   . GLN   A 1 105 ? 28.726  12.971  7.197   1.00 17.52 ? 104 GLN   A C   1 
ATOM   785  O O   . GLN   A 1 105 ? 28.670  14.179  6.973   1.00 18.04 ? 104 GLN   A O   1 
ATOM   786  C CB  . GLN   A 1 105 ? 26.254  12.533  6.746   1.00 16.94 ? 104 GLN   A CB  1 
ATOM   787  C CG  . GLN   A 1 105 ? 25.325  11.718  5.851   1.00 18.69 ? 104 GLN   A CG  1 
ATOM   788  C CD  . GLN   A 1 105 ? 23.933  12.274  5.798   1.00 20.74 ? 104 GLN   A CD  1 
ATOM   789  O OE1 . GLN   A 1 105 ? 23.310  12.504  6.837   1.00 19.34 ? 104 GLN   A OE1 1 
ATOM   790  N NE2 . GLN   A 1 105 ? 23.420  12.445  4.583   1.00 20.93 ? 104 GLN   A NE2 1 
ATOM   791  N N   . VAL   A 1 106 ? 29.702  12.412  7.936   1.00 17.62 ? 105 VAL   A N   1 
ATOM   792  C CA  . VAL   A 1 106 ? 30.852  13.131  8.452   1.00 18.84 ? 105 VAL   A CA  1 
ATOM   793  C C   . VAL   A 1 106 ? 32.081  12.411  7.883   1.00 19.88 ? 105 VAL   A C   1 
ATOM   794  O O   . VAL   A 1 106 ? 32.952  13.051  7.288   1.00 21.14 ? 105 VAL   A O   1 
ATOM   795  C CB  . VAL   A 1 106 ? 30.921  13.159  9.999   1.00 20.87 ? 105 VAL   A CB  1 
ATOM   796  C CG1 . VAL   A 1 106 ? 32.265  13.737  10.469  1.00 21.34 ? 105 VAL   A CG1 1 
ATOM   797  C CG2 . VAL   A 1 106 ? 29.764  13.951  10.583  1.00 22.76 ? 105 VAL   A CG2 1 
ATOM   798  N N   . THR   A 1 107 ? 32.155  11.069  8.053   1.00 19.85 ? 106 THR   A N   1 
ATOM   799  C CA  . THR   A 1 107 ? 33.353  10.324  7.681   1.00 19.91 ? 106 THR   A CA  1 
ATOM   800  C C   . THR   A 1 107 ? 33.537  9.984   6.206   1.00 20.78 ? 106 THR   A C   1 
ATOM   801  O O   . THR   A 1 107 ? 34.648  9.638   5.812   1.00 21.43 ? 106 THR   A O   1 
ATOM   802  C CB  . THR   A 1 107 ? 33.397  8.983   8.450   1.00 20.84 ? 106 THR   A CB  1 
ATOM   803  O OG1 . THR   A 1 107 ? 32.337  8.139   7.980   1.00 20.30 ? 106 THR   A OG1 1 
ATOM   804  C CG2 . THR   A 1 107 ? 33.303  9.156   9.960   1.00 21.62 ? 106 THR   A CG2 1 
ATOM   805  N N   . GLY   A 1 108 ? 32.444  9.915   5.453   1.00 19.98 ? 107 GLY   A N   1 
ATOM   806  C CA  . GLY   A 1 108 ? 32.511  9.380   4.100   1.00 19.57 ? 107 GLY   A CA  1 
ATOM   807  C C   . GLY   A 1 108 ? 32.290  7.868   4.131   1.00 19.29 ? 107 GLY   A C   1 
ATOM   808  O O   . GLY   A 1 108 ? 32.012  7.284   5.194   1.00 19.42 ? 107 GLY   A O   1 
ATOM   809  N N   . SER   A 1 109 ? 32.438  7.222   2.973   1.00 18.35 ? 108 SER   A N   1 
ATOM   810  C CA  . SER   A 1 109 ? 32.173  5.801   2.786   1.00 19.84 ? 108 SER   A CA  1 
ATOM   811  C C   . SER   A 1 109 ? 32.887  4.893   3.773   1.00 17.93 ? 108 SER   A C   1 
ATOM   812  O O   . SER   A 1 109 ? 34.036  5.132   4.150   1.00 17.71 ? 108 SER   A O   1 
ATOM   813  C CB  . SER   A 1 109 ? 32.473  5.370   1.350   1.00 23.52 ? 108 SER   A CB  1 
ATOM   814  O OG  . SER   A 1 109 ? 33.853  5.500   1.051   1.00 29.77 ? 108 SER   A OG  1 
ATOM   815  N N   . LEU   A 1 110 ? 32.146  3.910   4.281   1.00 17.44 ? 109 LEU   A N   1 
ATOM   816  C CA  . LEU   A 1 110 ? 32.718  2.934   5.201   1.00 17.20 ? 109 LEU   A CA  1 
ATOM   817  C C   . LEU   A 1 110 ? 33.626  2.010   4.407   1.00 18.26 ? 109 LEU   A C   1 
ATOM   818  O O   . LEU   A 1 110 ? 33.479  1.865   3.179   1.00 19.31 ? 109 LEU   A O   1 
ATOM   819  C CB  . LEU   A 1 110 ? 31.590  2.096   5.844   1.00 16.63 ? 109 LEU   A CB  1 
ATOM   820  C CG  . LEU   A 1 110 ? 31.078  2.612   7.182   1.00 17.94 ? 109 LEU   A CG  1 
ATOM   821  C CD1 . LEU   A 1 110 ? 30.382  3.971   7.002   1.00 18.65 ? 109 LEU   A CD1 1 
ATOM   822  C CD2 . LEU   A 1 110 ? 30.129  1.604   7.846   1.00 18.45 ? 109 LEU   A CD2 1 
ATOM   823  N N   . SER   A 1 111 ? 34.589  1.402   5.098   1.00 17.58 ? 110 SER   A N   1 
ATOM   824  C CA  . SER   A 1 111 ? 35.470  0.443   4.464   1.00 17.25 ? 110 SER   A CA  1 
ATOM   825  C C   . SER   A 1 111 ? 34.671  -0.855  4.235   1.00 16.93 ? 110 SER   A C   1 
ATOM   826  O O   . SER   A 1 111 ? 33.621  -1.078  4.878   1.00 17.00 ? 110 SER   A O   1 
ATOM   827  C CB  . SER   A 1 111 ? 36.661  0.145   5.362   1.00 18.69 ? 110 SER   A CB  1 
ATOM   828  O OG  . SER   A 1 111 ? 36.239  -0.598  6.495   1.00 19.92 ? 110 SER   A OG  1 
ATOM   829  N N   . GLU   A 1 112 ? 35.181  -1.729  3.366   1.00 16.34 ? 111 GLU   A N   1 
ATOM   830  C CA  . GLU   A 1 112 ? 34.487  -3.009  3.139   1.00 16.20 ? 111 GLU   A CA  1 
ATOM   831  C C   . GLU   A 1 112 ? 34.421  -3.859  4.450   1.00 16.68 ? 111 GLU   A C   1 
ATOM   832  O O   . GLU   A 1 112 ? 33.414  -4.524  4.679   1.00 16.73 ? 111 GLU   A O   1 
ATOM   833  C CB  . GLU   A 1 112 ? 35.191  -3.797  2.032   1.00 17.18 ? 111 GLU   A CB  1 
ATOM   834  C CG  . GLU   A 1 112 ? 34.536  -5.133  1.763   1.00 17.71 ? 111 GLU   A CG  1 
ATOM   835  C CD  . GLU   A 1 112 ? 35.011  -5.853  0.524   1.00 18.21 ? 111 GLU   A CD  1 
ATOM   836  O OE1 . GLU   A 1 112 ? 35.410  -5.192  -0.465  1.00 18.58 ? 111 GLU   A OE1 1 
ATOM   837  O OE2 . GLU   A 1 112 ? 35.004  -7.101  0.556   1.00 21.22 ? 111 GLU   A OE2 1 
ATOM   838  N N   . LEU   A 1 113 ? 35.505  -3.866  5.279   1.00 16.69 ? 112 LEU   A N   1 
ATOM   839  C CA  . LEU   A 1 113 ? 35.457  -4.634  6.525   1.00 17.45 ? 112 LEU   A CA  1 
ATOM   840  C C   . LEU   A 1 113 ? 34.455  -4.019  7.501   1.00 17.27 ? 112 LEU   A C   1 
ATOM   841  O O   . LEU   A 1 113 ? 33.746  -4.760  8.193   1.00 18.12 ? 112 LEU   A O   1 
ATOM   842  C CB  . LEU   A 1 113 ? 36.829  -4.803  7.174   1.00 17.61 ? 112 LEU   A CB  1 
ATOM   843  C CG  . LEU   A 1 113 ? 37.756  -5.703  6.390   1.00 19.57 ? 112 LEU   A CG  1 
ATOM   844  C CD1 . LEU   A 1 113 ? 39.183  -5.631  6.942   1.00 18.71 ? 112 LEU   A CD1 1 
ATOM   845  C CD2 . LEU   A 1 113 ? 37.310  -7.156  6.484   1.00 21.69 ? 112 LEU   A CD2 1 
ATOM   846  N N   . GLN   A 1 114 ? 34.332  -2.684  7.518   1.00 16.11 ? 113 GLN   A N   1 
ATOM   847  C CA  . GLN   A 1 114 ? 33.356  -2.048  8.412   1.00 15.00 ? 113 GLN   A CA  1 
ATOM   848  C C   . GLN   A 1 114 ? 31.929  -2.429  7.994   1.00 14.97 ? 113 GLN   A C   1 
ATOM   849  O O   . GLN   A 1 114 ? 31.108  -2.715  8.862   1.00 15.07 ? 113 GLN   A O   1 
ATOM   850  C CB  . GLN   A 1 114 ? 33.537  -0.529  8.421   1.00 15.49 ? 113 GLN   A CB  1 
ATOM   851  C CG  . GLN   A 1 114 ? 34.724  -0.111  9.277   1.00 16.94 ? 113 GLN   A CG  1 
ATOM   852  C CD  . GLN   A 1 114 ? 35.288  1.252   8.911   1.00 18.34 ? 113 GLN   A CD  1 
ATOM   853  O OE1 . GLN   A 1 114 ? 34.855  1.916   7.955   1.00 18.60 ? 113 GLN   A OE1 1 
ATOM   854  N NE2 . GLN   A 1 114 ? 36.311  1.671   9.644   1.00 19.43 ? 113 GLN   A NE2 1 
ATOM   855  N N   . ILE   A 1 115 ? 31.653  -2.429  6.673   1.00 13.81 ? 114 ILE   A N   1 
ATOM   856  C CA  . ILE   A 1 115 ? 30.338  -2.792  6.135   1.00 13.89 ? 114 ILE   A CA  1 
ATOM   857  C C   . ILE   A 1 115 ? 30.077  -4.255  6.450   1.00 14.48 ? 114 ILE   A C   1 
ATOM   858  O O   . ILE   A 1 115 ? 28.994  -4.580  6.907   1.00 13.79 ? 114 ILE   A O   1 
ATOM   859  C CB  . ILE   A 1 115 ? 30.328  -2.523  4.614   1.00 14.27 ? 114 ILE   A CB  1 
ATOM   860  C CG1 . ILE   A 1 115 ? 30.378  -0.992  4.343   1.00 15.46 ? 114 ILE   A CG1 1 
ATOM   861  C CG2 . ILE   A 1 115 ? 29.076  -3.143  3.957   1.00 14.04 ? 114 ILE   A CG2 1 
ATOM   862  C CD1 . ILE   A 1 115 ? 30.552  -0.628  2.883   1.00 16.75 ? 114 ILE   A CD1 1 
ATOM   863  N N   . SER   A 1 116 ? 31.092  -5.130  6.303   1.00 13.92 ? 115 SER   A N   1 
ATOM   864  C CA  . SER   A 1 116 ? 30.922  -6.557  6.612   1.00 14.39 ? 115 SER   A CA  1 
ATOM   865  C C   . SER   A 1 116 ? 30.476  -6.766  8.079   1.00 14.98 ? 115 SER   A C   1 
ATOM   866  O O   . SER   A 1 116 ? 29.580  -7.557  8.334   1.00 15.51 ? 115 SER   A O   1 
ATOM   867  C CB  . SER   A 1 116 ? 32.227  -7.311  6.369   1.00 15.08 ? 115 SER   A CB  1 
ATOM   868  O OG  . SER   A 1 116 ? 32.680  -7.143  5.030   1.00 16.41 ? 115 SER   A OG  1 
ATOM   869  N N   . TYR   A 1 117 ? 31.137  -6.097  9.034   1.00 14.25 ? 116 TYR   A N   1 
ATOM   870  C CA  . TYR   A 1 117 ? 30.802  -6.184  10.460  1.00 14.62 ? 116 TYR   A CA  1 
ATOM   871  C C   . TYR   A 1 117 ? 29.392  -5.667  10.710  1.00 15.06 ? 116 TYR   A C   1 
ATOM   872  O O   . TYR   A 1 117 ? 28.583  -6.325  11.382  1.00 14.75 ? 116 TYR   A O   1 
ATOM   873  C CB  . TYR   A 1 117 ? 31.847  -5.397  11.295  1.00 15.46 ? 116 TYR   A CB  1 
ATOM   874  C CG  . TYR   A 1 117 ? 31.507  -5.256  12.758  1.00 17.34 ? 116 TYR   A CG  1 
ATOM   875  C CD1 . TYR   A 1 117 ? 31.552  -6.350  13.614  1.00 19.82 ? 116 TYR   A CD1 1 
ATOM   876  C CD2 . TYR   A 1 117 ? 31.115  -4.040  13.283  1.00 18.56 ? 116 TYR   A CD2 1 
ATOM   877  C CE1 . TYR   A 1 117 ? 31.204  -6.226  14.960  1.00 21.25 ? 116 TYR   A CE1 1 
ATOM   878  C CE2 . TYR   A 1 117 ? 30.805  -3.899  14.629  1.00 20.06 ? 116 TYR   A CE2 1 
ATOM   879  C CZ  . TYR   A 1 117 ? 30.852  -4.991  15.461  1.00 22.25 ? 116 TYR   A CZ  1 
ATOM   880  O OH  . TYR   A 1 117 ? 30.514  -4.821  16.775  1.00 26.11 ? 116 TYR   A OH  1 
ATOM   881  N N   . VAL   A 1 118 ? 29.056  -4.501  10.130  1.00 14.50 ? 117 VAL   A N   1 
ATOM   882  C CA  . VAL   A 1 118 ? 27.700  -3.949  10.277  1.00 14.06 ? 117 VAL   A CA  1 
ATOM   883  C C   . VAL   A 1 118 ? 26.662  -4.969  9.775   1.00 13.94 ? 117 VAL   A C   1 
ATOM   884  O O   . VAL   A 1 118 ? 25.696  -5.276  10.466  1.00 14.27 ? 117 VAL   A O   1 
ATOM   885  C CB  . VAL   A 1 118 ? 27.548  -2.592  9.547   1.00 14.26 ? 117 VAL   A CB  1 
ATOM   886  C CG1 . VAL   A 1 118 ? 26.076  -2.186  9.417   1.00 15.26 ? 117 VAL   A CG1 1 
ATOM   887  C CG2 . VAL   A 1 118 ? 28.339  -1.514  10.270  1.00 14.26 ? 117 VAL   A CG2 1 
ATOM   888  N N   . CYS   A 1 119 ? 26.906  -5.506  8.578   1.00 14.41 ? 118 CYS   A N   1 
ATOM   889  C CA  . CYS   A 1 119 ? 25.997  -6.485  7.994   1.00 14.40 ? 118 CYS   A CA  1 
ATOM   890  C C   . CYS   A 1 119 ? 25.849  -7.733  8.836   1.00 13.57 ? 118 CYS   A C   1 
ATOM   891  O O   . CYS   A 1 119 ? 24.733  -8.243  8.943   1.00 14.45 ? 118 CYS   A O   1 
ATOM   892  C CB  . CYS   A 1 119 ? 26.412  -6.835  6.571   1.00 15.59 ? 118 CYS   A CB  1 
ATOM   893  S SG  . CYS   A 1 119 ? 26.118  -5.509  5.391   1.00 17.20 ? 118 CYS   A SG  1 
ATOM   894  N N   . ARG   A 1 120 ? 26.932  -8.254  9.406   1.00 13.08 ? 119 ARG   A N   1 
ATOM   895  C CA  . ARG   A 1 120 ? 26.833  -9.453  10.248  1.00 13.14 ? 119 ARG   A CA  1 
ATOM   896  C C   . ARG   A 1 120 ? 25.993  -9.157  11.483  1.00 14.36 ? 119 ARG   A C   1 
ATOM   897  O O   . ARG   A 1 120 ? 25.088  -9.932  11.839  1.00 15.28 ? 119 ARG   A O   1 
ATOM   898  C CB  . ARG   A 1 120 ? 28.233  -9.904  10.706  1.00 13.99 ? 119 ARG   A CB  1 
ATOM   899  C CG  . ARG   A 1 120 ? 28.164  -11.196 11.487  1.00 15.95 ? 119 ARG   A CG  1 
ATOM   900  C CD  . ARG   A 1 120 ? 29.483  -11.502 12.184  1.00 17.54 ? 119 ARG   A CD  1 
ATOM   901  N NE  . ARG   A 1 120 ? 29.706  -10.633 13.342  1.00 20.17 ? 119 ARG   A NE  1 
ATOM   902  C CZ  . ARG   A 1 120 ? 30.840  -10.585 14.031  1.00 22.48 ? 119 ARG   A CZ  1 
ATOM   903  N NH1 . ARG   A 1 120 ? 31.883  -11.325 13.663  1.00 22.74 ? 119 ARG   A NH1 1 
ATOM   904  N NH2 . ARG   A 1 120 ? 30.949  -9.788  15.082  1.00 21.98 ? 119 ARG   A NH2 1 
ATOM   905  N N   . GLU   A 1 121 ? 26.237  -7.992  12.097  1.00 13.55 ? 120 GLU   A N   1 
ATOM   906  C CA  . GLU   A 1 121 ? 25.515  -7.628  13.309  1.00 13.80 ? 120 GLU   A CA  1 
ATOM   907  C C   . GLU   A 1 121 ? 24.021  -7.404  13.036  1.00 14.60 ? 120 GLU   A C   1 
ATOM   908  O O   . GLU   A 1 121 ? 23.190  -7.866  13.810  1.00 15.27 ? 120 GLU   A O   1 
ATOM   909  C CB  . GLU   A 1 121 ? 26.160  -6.388  13.932  1.00 13.72 ? 120 GLU   A CB  1 
ATOM   910  C CG  . GLU   A 1 121 ? 27.592  -6.644  14.409  1.00 14.41 ? 120 GLU   A CG  1 
ATOM   911  C CD  . GLU   A 1 121 ? 27.718  -7.728  15.468  1.00 17.81 ? 120 GLU   A CD  1 
ATOM   912  O OE1 . GLU   A 1 121 ? 27.278  -7.489  16.622  1.00 18.27 ? 120 GLU   A OE1 1 
ATOM   913  O OE2 . GLU   A 1 121 ? 28.274  -8.807  15.156  1.00 18.92 ? 120 GLU   A OE2 1 
ATOM   914  N N   . VAL   A 1 122 ? 23.686  -6.706  11.946  1.00 13.98 ? 121 VAL   A N   1 
ATOM   915  C CA  . VAL   A 1 122 ? 22.291  -6.490  11.568  1.00 13.90 ? 121 VAL   A CA  1 
ATOM   916  C C   . VAL   A 1 122 ? 21.636  -7.843  11.222  1.00 13.36 ? 121 VAL   A C   1 
ATOM   917  O O   . VAL   A 1 122 ? 20.478  -8.067  11.580  1.00 13.86 ? 121 VAL   A O   1 
ATOM   918  C CB  . VAL   A 1 122 ? 22.179  -5.481  10.414  1.00 15.44 ? 121 VAL   A CB  1 
ATOM   919  C CG1 . VAL   A 1 122 ? 20.749  -5.408  9.870   1.00 15.48 ? 121 VAL   A CG1 1 
ATOM   920  C CG2 . VAL   A 1 122 ? 22.647  -4.095  10.879  1.00 16.17 ? 121 VAL   A CG2 1 
ATOM   921  N N   . LEU   A 1 123 ? 22.365  -8.747  10.543  1.00 12.83 ? 122 LEU   A N   1 
ATOM   922  C CA  . LEU   A 1 123 ? 21.802  -10.078 10.209  1.00 12.97 ? 122 LEU   A CA  1 
ATOM   923  C C   . LEU   A 1 123 ? 21.506  -10.867 11.471  1.00 13.30 ? 122 LEU   A C   1 
ATOM   924  O O   . LEU   A 1 123 ? 20.519  -11.601 11.517  1.00 14.33 ? 122 LEU   A O   1 
ATOM   925  C CB  . LEU   A 1 123 ? 22.750  -10.879 9.326   1.00 13.67 ? 122 LEU   A CB  1 
ATOM   926  C CG  . LEU   A 1 123 ? 22.710  -10.498 7.853   1.00 15.41 ? 122 LEU   A CG  1 
ATOM   927  C CD1 . LEU   A 1 123 ? 23.922  -11.058 7.111   1.00 14.56 ? 122 LEU   A CD1 1 
ATOM   928  C CD2 . LEU   A 1 123 ? 21.402  -10.944 7.202   1.00 16.32 ? 122 LEU   A CD2 1 
ATOM   929  N N   . GLN   A 1 124 ? 22.360  -10.740 12.511  1.00 13.36 ? 123 GLN   A N   1 
ATOM   930  C CA  . GLN   A 1 124 ? 22.069  -11.401 13.789  1.00 14.08 ? 123 GLN   A CA  1 
ATOM   931  C C   . GLN   A 1 124 ? 20.739  -10.883 14.368  1.00 15.20 ? 123 GLN   A C   1 
ATOM   932  O O   . GLN   A 1 124 ? 19.907  -11.685 14.786  1.00 16.03 ? 123 GLN   A O   1 
ATOM   933  C CB  . GLN   A 1 124 ? 23.221  -11.217 14.784  1.00 15.66 ? 123 GLN   A CB  1 
ATOM   934  C CG  . GLN   A 1 124 ? 24.466  -12.012 14.362  1.00 14.96 ? 123 GLN   A CG  1 
ATOM   935  C CD  . GLN   A 1 124 ? 25.748  -11.484 14.975  1.00 20.39 ? 123 GLN   A CD  1 
ATOM   936  O OE1 . GLN   A 1 124 ? 25.756  -10.515 15.751  1.00 23.42 ? 123 GLN   A OE1 1 
ATOM   937  N NE2 . GLN   A 1 124 ? 26.862  -12.116 14.655  1.00 17.54 ? 123 GLN   A NE2 1 
ATOM   938  N N   . GLY   A 1 125 ? 20.546  -9.575  14.343  1.00 15.09 ? 124 GLY   A N   1 
ATOM   939  C CA  . GLY   A 1 125 ? 19.304  -8.967  14.819  1.00 16.08 ? 124 GLY   A CA  1 
ATOM   940  C C   . GLY   A 1 125 ? 18.093  -9.380  13.998  1.00 14.91 ? 124 GLY   A C   1 
ATOM   941  O O   . GLY   A 1 125 ? 17.061  -9.721  14.566  1.00 14.83 ? 124 GLY   A O   1 
ATOM   942  N N   . LEU   A 1 126 ? 18.223  -9.407  12.657  1.00 13.97 ? 125 LEU   A N   1 
ATOM   943  C CA  . LEU   A 1 126 ? 17.112  -9.795  11.771  1.00 14.15 ? 125 LEU   A CA  1 
ATOM   944  C C   . LEU   A 1 126 ? 16.772  -11.270 11.931  1.00 14.12 ? 125 LEU   A C   1 
ATOM   945  O O   . LEU   A 1 126 ? 15.588  -11.647 11.933  1.00 14.31 ? 125 LEU   A O   1 
ATOM   946  C CB  . LEU   A 1 126 ? 17.468  -9.529  10.303  1.00 14.67 ? 125 LEU   A CB  1 
ATOM   947  C CG  . LEU   A 1 126 ? 17.504  -8.072  9.831   1.00 14.68 ? 125 LEU   A CG  1 
ATOM   948  C CD1 . LEU   A 1 126 ? 17.966  -8.011  8.355   1.00 14.47 ? 125 LEU   A CD1 1 
ATOM   949  C CD2 . LEU   A 1 126 ? 16.133  -7.376  10.052  1.00 14.74 ? 125 LEU   A CD2 1 
ATOM   950  N N   . ALA   A 1 127 ? 17.808  -12.144 12.098  1.00 13.93 ? 126 ALA   A N   1 
ATOM   951  C CA  . ALA   A 1 127 ? 17.531  -13.571 12.289  1.00 14.97 ? 126 ALA   A CA  1 
ATOM   952  C C   . ALA   A 1 127 ? 16.715  -13.751 13.592  1.00 16.40 ? 126 ALA   A C   1 
ATOM   953  O O   . ALA   A 1 127 ? 15.755  -14.510 13.600  1.00 17.71 ? 126 ALA   A O   1 
ATOM   954  C CB  . ALA   A 1 127 ? 18.840  -14.374 12.369  1.00 15.51 ? 126 ALA   A CB  1 
ATOM   955  N N   . TYR   A 1 128 ? 17.034  -12.967 14.636  1.00 16.34 ? 127 TYR   A N   1 
ATOM   956  C CA  . TYR   A 1 128 ? 16.272  -13.030 15.885  1.00 17.38 ? 127 TYR   A CA  1 
ATOM   957  C C   . TYR   A 1 128 ? 14.820  -12.560 15.631  1.00 18.33 ? 127 TYR   A C   1 
ATOM   958  O O   . TYR   A 1 128 ? 13.885  -13.276 15.987  1.00 19.08 ? 127 TYR   A O   1 
ATOM   959  C CB  . TYR   A 1 128 ? 16.943  -12.174 16.981  1.00 18.12 ? 127 TYR   A CB  1 
ATOM   960  C CG  . TYR   A 1 128 ? 16.071  -12.069 18.215  1.00 19.60 ? 127 TYR   A CG  1 
ATOM   961  C CD1 . TYR   A 1 128 ? 15.956  -13.132 19.102  1.00 21.07 ? 127 TYR   A CD1 1 
ATOM   962  C CD2 . TYR   A 1 128 ? 15.249  -10.964 18.415  1.00 20.42 ? 127 TYR   A CD2 1 
ATOM   963  C CE1 . TYR   A 1 128 ? 15.083  -13.076 20.188  1.00 22.46 ? 127 TYR   A CE1 1 
ATOM   964  C CE2 . TYR   A 1 128 ? 14.381  -10.894 19.493  1.00 21.96 ? 127 TYR   A CE2 1 
ATOM   965  C CZ  . TYR   A 1 128 ? 14.281  -11.960 20.364  1.00 24.08 ? 127 TYR   A CZ  1 
ATOM   966  O OH  . TYR   A 1 128 ? 13.439  -11.834 21.445  1.00 26.08 ? 127 TYR   A OH  1 
ATOM   967  N N   . LEU   A 1 129 ? 14.630  -11.369 15.041  1.00 16.77 ? 128 LEU   A N   1 
ATOM   968  C CA  . LEU   A 1 129 ? 13.271  -10.864 14.780  1.00 17.86 ? 128 LEU   A CA  1 
ATOM   969  C C   . LEU   A 1 129 ? 12.458  -11.794 13.917  1.00 17.82 ? 128 LEU   A C   1 
ATOM   970  O O   . LEU   A 1 129 ? 11.274  -12.023 14.214  1.00 18.20 ? 128 LEU   A O   1 
ATOM   971  C CB  . LEU   A 1 129 ? 13.336  -9.466  14.134  1.00 18.48 ? 128 LEU   A CB  1 
ATOM   972  C CG  . LEU   A 1 129 ? 13.922  -8.383  15.002  1.00 21.54 ? 128 LEU   A CG  1 
ATOM   973  C CD1 . LEU   A 1 129 ? 14.079  -7.082  14.216  1.00 21.18 ? 128 LEU   A CD1 1 
ATOM   974  C CD2 . LEU   A 1 129 ? 13.059  -8.164  16.250  1.00 23.27 ? 128 LEU   A CD2 1 
ATOM   975  N N   . HIS   A 1 130 ? 13.081  -12.411 12.893  1.00 16.29 ? 129 HIS   A N   1 
ATOM   976  C CA  . HIS   A 1 130 ? 12.346  -13.345 12.041  1.00 17.36 ? 129 HIS   A CA  1 
ATOM   977  C C   . HIS   A 1 130 ? 11.944  -14.602 12.811  1.00 19.42 ? 129 HIS   A C   1 
ATOM   978  O O   . HIS   A 1 130 ? 10.857  -15.144 12.580  1.00 20.50 ? 129 HIS   A O   1 
ATOM   979  C CB  . HIS   A 1 130 ? 13.167  -13.674 10.774  1.00 15.91 ? 129 HIS   A CB  1 
ATOM   980  C CG  . HIS   A 1 130 ? 13.394  -12.483 9.875   1.00 15.10 ? 129 HIS   A CG  1 
ATOM   981  N ND1 . HIS   A 1 130 ? 14.183  -12.586 8.731   1.00 15.17 ? 129 HIS   A ND1 1 
ATOM   982  C CD2 . HIS   A 1 130 ? 12.895  -11.214 9.946   1.00 16.28 ? 129 HIS   A CD2 1 
ATOM   983  C CE1 . HIS   A 1 130 ? 14.152  -11.393 8.167   1.00 16.26 ? 129 HIS   A CE1 1 
ATOM   984  N NE2 . HIS   A 1 130 ? 13.372  -10.537 8.852   1.00 16.12 ? 129 HIS   A NE2 1 
ATOM   985  N N   . SER   A 1 131 ? 12.785  -15.044 13.752  1.00 19.95 ? 130 SER   A N   1 
ATOM   986  C CA  . SER   A 1 131 ? 12.436  -16.213 14.582  1.00 21.21 ? 130 SER   A CA  1 
ATOM   987  C C   . SER   A 1 131 ? 11.228  -15.912 15.492  1.00 22.77 ? 130 SER   A C   1 
ATOM   988  O O   . SER   A 1 131 ? 10.498  -16.832 15.872  1.00 23.33 ? 130 SER   A O   1 
ATOM   989  C CB  . SER   A 1 131 ? 13.641  -16.677 15.398  1.00 21.87 ? 130 SER   A CB  1 
ATOM   990  O OG  . SER   A 1 131 ? 13.848  -15.875 16.546  1.00 24.22 ? 130 SER   A OG  1 
ATOM   991  N N   . GLN   A 1 132 ? 11.038  -14.632 15.849  1.00 22.93 ? 131 GLN   A N   1 
ATOM   992  C CA  . GLN   A 1 132 ? 9.909   -14.126 16.641  1.00 23.72 ? 131 GLN   A CA  1 
ATOM   993  C C   . GLN   A 1 132 ? 8.678   -13.754 15.772  1.00 23.91 ? 131 GLN   A C   1 
ATOM   994  O O   . GLN   A 1 132 ? 7.720   -13.174 16.284  1.00 24.13 ? 131 GLN   A O   1 
ATOM   995  C CB  . GLN   A 1 132 ? 10.369  -12.920 17.476  1.00 26.10 ? 131 GLN   A CB  1 
ATOM   996  C CG  . GLN   A 1 132 ? 11.544  -13.244 18.394  1.00 29.31 ? 131 GLN   A CG  1 
ATOM   997  C CD  . GLN   A 1 132 ? 11.232  -14.348 19.371  1.00 35.51 ? 131 GLN   A CD  1 
ATOM   998  O OE1 . GLN   A 1 132 ? 10.394  -14.198 20.252  1.00 37.28 ? 131 GLN   A OE1 1 
ATOM   999  N NE2 . GLN   A 1 132 ? 11.901  -15.488 19.233  1.00 36.49 ? 131 GLN   A NE2 1 
ATOM   1000 N N   . LYS   A 1 133 ? 8.712   -14.093 14.467  1.00 23.17 ? 132 LYS   A N   1 
ATOM   1001 C CA  . LYS   A 1 133 ? 7.642   -13.871 13.499  1.00 23.31 ? 132 LYS   A CA  1 
ATOM   1002 C C   . LYS   A 1 133 ? 7.332   -12.392 13.263  1.00 22.64 ? 132 LYS   A C   1 
ATOM   1003 O O   . LYS   A 1 133 ? 6.187   -12.010 12.990  1.00 23.18 ? 132 LYS   A O   1 
ATOM   1004 C CB  . LYS   A 1 133 ? 6.379   -14.675 13.845  1.00 26.27 ? 132 LYS   A CB  1 
ATOM   1005 C CG  . LYS   A 1 133 ? 6.662   -16.168 13.929  1.00 31.44 ? 132 LYS   A CG  1 
ATOM   1006 C CD  . LYS   A 1 133 ? 5.364   -16.963 14.029  1.00 39.05 ? 132 LYS   A CD  1 
ATOM   1007 C CE  . LYS   A 1 133 ? 5.581   -18.302 14.686  1.00 45.64 ? 132 LYS   A CE  1 
ATOM   1008 N NZ  . LYS   A 1 133 ? 6.025   -18.152 16.100  1.00 49.57 ? 132 LYS   A NZ  1 
ATOM   1009 N N   . LYS   A 1 134 ? 8.371   -11.569 13.319  1.00 21.20 ? 133 LYS   A N   1 
ATOM   1010 C CA  . LYS   A 1 134 ? 8.252   -10.166 13.005  1.00 20.75 ? 133 LYS   A CA  1 
ATOM   1011 C C   . LYS   A 1 134 ? 8.993   -9.878  11.700  1.00 19.11 ? 133 LYS   A C   1 
ATOM   1012 O O   . LYS   A 1 134 ? 9.961   -10.556 11.353  1.00 19.80 ? 133 LYS   A O   1 
ATOM   1013 C CB  . LYS   A 1 134 ? 8.858   -9.281  14.104  1.00 23.49 ? 133 LYS   A CB  1 
ATOM   1014 C CG  . LYS   A 1 134 ? 8.102   -9.279  15.424  1.00 27.92 ? 133 LYS   A CG  1 
ATOM   1015 C CD  . LYS   A 1 134 ? 8.538   -8.087  16.251  1.00 32.51 ? 133 LYS   A CD  1 
ATOM   1016 C CE  . LYS   A 1 134 ? 7.757   -7.944  17.532  1.00 38.07 ? 133 LYS   A CE  1 
ATOM   1017 N NZ  . LYS   A 1 134 ? 7.828   -9.189  18.355  1.00 40.51 ? 133 LYS   A NZ  1 
ATOM   1018 N N   . ILE   A 1 135 ? 8.555   -8.844  11.008  1.00 17.55 ? 134 ILE   A N   1 
ATOM   1019 C CA  . ILE   A 1 135 ? 9.250   -8.317  9.837   1.00 16.85 ? 134 ILE   A CA  1 
ATOM   1020 C C   . ILE   A 1 135 ? 9.624   -6.903  10.237  1.00 16.11 ? 134 ILE   A C   1 
ATOM   1021 O O   . ILE   A 1 135 ? 8.763   -6.128  10.681  1.00 16.91 ? 134 ILE   A O   1 
ATOM   1022 C CB  . ILE   A 1 135 ? 8.397   -8.328  8.560   1.00 16.97 ? 134 ILE   A CB  1 
ATOM   1023 C CG1 . ILE   A 1 135 ? 7.899   -9.745  8.233   1.00 19.13 ? 134 ILE   A CG1 1 
ATOM   1024 C CG2 . ILE   A 1 135 ? 9.185   -7.703  7.400   1.00 16.96 ? 134 ILE   A CG2 1 
ATOM   1025 C CD1 . ILE   A 1 135 ? 6.886   -9.770  7.061   1.00 19.96 ? 134 ILE   A CD1 1 
ATOM   1026 N N   . HIS   A 1 136 ? 10.909  -6.554  10.123  1.00 15.06 ? 135 HIS   A N   1 
ATOM   1027 C CA  . HIS   A 1 136 ? 11.354  -5.218  10.518  1.00 14.32 ? 135 HIS   A CA  1 
ATOM   1028 C C   . HIS   A 1 136 ? 10.770  -4.163  9.566   1.00 14.14 ? 135 HIS   A C   1 
ATOM   1029 O O   . HIS   A 1 136 ? 10.091  -3.225  10.010  1.00 14.93 ? 135 HIS   A O   1 
ATOM   1030 C CB  . HIS   A 1 136 ? 12.883  -5.192  10.541  1.00 14.64 ? 135 HIS   A CB  1 
ATOM   1031 C CG  . HIS   A 1 136 ? 13.438  -3.951  11.143  1.00 14.20 ? 135 HIS   A CG  1 
ATOM   1032 N ND1 . HIS   A 1 136 ? 13.483  -2.769  10.436  1.00 15.04 ? 135 HIS   A ND1 1 
ATOM   1033 C CD2 . HIS   A 1 136 ? 14.021  -3.769  12.353  1.00 15.89 ? 135 HIS   A CD2 1 
ATOM   1034 C CE1 . HIS   A 1 136 ? 14.124  -1.907  11.215  1.00 15.18 ? 135 HIS   A CE1 1 
ATOM   1035 N NE2 . HIS   A 1 136 ? 14.423  -2.462  12.407  1.00 15.14 ? 135 HIS   A NE2 1 
ATOM   1036 N N   . ARG   A 1 137 ? 11.001  -4.322  8.257   1.00 13.83 ? 136 ARG   A N   1 
ATOM   1037 C CA  . ARG   A 1 137 ? 10.413  -3.460  7.239   1.00 13.81 ? 136 ARG   A CA  1 
ATOM   1038 C C   . ARG   A 1 137 ? 10.861  -2.008  7.331   1.00 13.42 ? 136 ARG   A C   1 
ATOM   1039 O O   . ARG   A 1 137 ? 10.259  -1.168  6.676   1.00 14.34 ? 136 ARG   A O   1 
ATOM   1040 C CB  . ARG   A 1 137 ? 8.863   -3.572  7.238   1.00 15.05 ? 136 ARG   A CB  1 
ATOM   1041 C CG  . ARG   A 1 137 ? 8.306   -4.359  6.072   1.00 16.34 ? 136 ARG   A CG  1 
ATOM   1042 C CD  . ARG   A 1 137 ? 8.131   -3.450  4.864   1.00 16.50 ? 136 ARG   A CD  1 
ATOM   1043 N NE  . ARG   A 1 137 ? 6.808   -2.814  4.863   1.00 16.02 ? 136 ARG   A NE  1 
ATOM   1044 C CZ  . ARG   A 1 137 ? 6.565   -1.520  5.069   1.00 16.70 ? 136 ARG   A CZ  1 
ATOM   1045 N NH1 . ARG   A 1 137 ? 7.570   -0.671  5.298   1.00 15.28 ? 136 ARG   A NH1 1 
ATOM   1046 N NH2 . ARG   A 1 137 ? 5.323   -1.060  5.028   1.00 15.93 ? 136 ARG   A NH2 1 
ATOM   1047 N N   . ASP   A 1 138 ? 11.980  -1.719  8.041   1.00 12.19 ? 137 ASP   A N   1 
ATOM   1048 C CA  . ASP   A 1 138 ? 12.477  -0.343  8.181   1.00 13.54 ? 137 ASP   A CA  1 
ATOM   1049 C C   . ASP   A 1 138 ? 14.004  -0.343  8.231   1.00 14.16 ? 137 ASP   A C   1 
ATOM   1050 O O   . ASP   A 1 138 ? 14.586  0.526   8.876   1.00 14.55 ? 137 ASP   A O   1 
ATOM   1051 C CB  . ASP   A 1 138 ? 11.878  0.287   9.461   1.00 14.41 ? 137 ASP   A CB  1 
ATOM   1052 C CG  . ASP   A 1 138 ? 11.923  1.789   9.500   1.00 19.27 ? 137 ASP   A CG  1 
ATOM   1053 O OD1 . ASP   A 1 138 ? 11.977  2.404   8.415   1.00 16.16 ? 137 ASP   A OD1 1 
ATOM   1054 O OD2 . ASP   A 1 138 ? 11.916  2.355   10.626  1.00 22.43 ? 137 ASP   A OD2 1 
ATOM   1055 N N   . ILE   A 1 139 ? 14.667  -1.307  7.548   1.00 13.57 ? 138 ILE   A N   1 
ATOM   1056 C CA  . ILE   A 1 139 ? 16.132  -1.350  7.573   1.00 13.36 ? 138 ILE   A CA  1 
ATOM   1057 C C   . ILE   A 1 139 ? 16.714  -0.303  6.637   1.00 14.48 ? 138 ILE   A C   1 
ATOM   1058 O O   . ILE   A 1 139 ? 16.386  -0.261  5.442   1.00 14.76 ? 138 ILE   A O   1 
ATOM   1059 C CB  . ILE   A 1 139 ? 16.631  -2.753  7.179   1.00 13.96 ? 138 ILE   A CB  1 
ATOM   1060 C CG1 . ILE   A 1 139 ? 16.136  -3.823  8.171   1.00 14.41 ? 138 ILE   A CG1 1 
ATOM   1061 C CG2 . ILE   A 1 139 ? 18.164  -2.782  7.025   1.00 14.73 ? 138 ILE   A CG2 1 
ATOM   1062 C CD1 . ILE   A 1 139 ? 16.804  -3.718  9.581   1.00 15.73 ? 138 ILE   A CD1 1 
ATOM   1063 N N   . LYS   A 1 140 ? 17.592  0.542   7.195   1.00 13.44 ? 139 LYS   A N   1 
ATOM   1064 C CA  . LYS   A 1 140 ? 18.365  1.575   6.485   1.00 13.01 ? 139 LYS   A CA  1 
ATOM   1065 C C   . LYS   A 1 140 ? 19.455  2.079   7.441   1.00 13.55 ? 139 LYS   A C   1 
ATOM   1066 O O   . LYS   A 1 140 ? 19.354  1.854   8.652   1.00 14.21 ? 139 LYS   A O   1 
ATOM   1067 C CB  . LYS   A 1 140 ? 17.478  2.744   5.968   1.00 13.94 ? 139 LYS   A CB  1 
ATOM   1068 C CG  . LYS   A 1 140 ? 16.858  3.557   7.100   1.00 14.09 ? 139 LYS   A CG  1 
ATOM   1069 C CD  . LYS   A 1 140 ? 15.857  4.578   6.570   1.00 15.92 ? 139 LYS   A CD  1 
ATOM   1070 C CE  . LYS   A 1 140 ? 16.507  5.639   5.726   1.00 17.76 ? 139 LYS   A CE  1 
ATOM   1071 N NZ  . LYS   A 1 140 ? 15.523  6.738   5.405   1.00 19.20 ? 139 LYS   A NZ  1 
ATOM   1072 N N   . GLY   A 1 141 ? 20.469  2.772   6.918   1.00 13.12 ? 140 GLY   A N   1 
ATOM   1073 C CA  . GLY   A 1 141 ? 21.561  3.309   7.729   1.00 13.89 ? 140 GLY   A CA  1 
ATOM   1074 C C   . GLY   A 1 141 ? 21.089  4.167   8.905   1.00 14.40 ? 140 GLY   A C   1 
ATOM   1075 O O   . GLY   A 1 141 ? 21.581  3.994   10.021  1.00 15.15 ? 140 GLY   A O   1 
ATOM   1076 N N   . ALA   A 1 142 ? 20.070  5.038   8.696   1.00 13.86 ? 141 ALA   A N   1 
ATOM   1077 C CA  . ALA   A 1 142 ? 19.561  5.895   9.770   1.00 14.24 ? 141 ALA   A CA  1 
ATOM   1078 C C   . ALA   A 1 142 ? 18.945  5.119   10.927  1.00 15.33 ? 141 ALA   A C   1 
ATOM   1079 O O   . ALA   A 1 142 ? 18.743  5.688   12.017  1.00 16.68 ? 141 ALA   A O   1 
ATOM   1080 C CB  . ALA   A 1 142 ? 18.549  6.875   9.207   1.00 15.27 ? 141 ALA   A CB  1 
ATOM   1081 N N   . ASN   A 1 143 ? 18.566  3.835   10.682  1.00 14.24 ? 142 ASN   A N   1 
ATOM   1082 C CA  . ASN   A 1 143 ? 17.889  3.030   11.709  1.00 14.09 ? 142 ASN   A CA  1 
ATOM   1083 C C   . ASN   A 1 143 ? 18.793  1.953   12.340  1.00 15.22 ? 142 ASN   A C   1 
ATOM   1084 O O   . ASN   A 1 143 ? 18.295  1.044   13.009  1.00 16.40 ? 142 ASN   A O   1 
ATOM   1085 C CB  . ASN   A 1 143 ? 16.587  2.432   11.147  1.00 13.92 ? 142 ASN   A CB  1 
ATOM   1086 C CG  . ASN   A 1 143 ? 15.629  3.525   10.712  1.00 15.46 ? 142 ASN   A CG  1 
ATOM   1087 O OD1 . ASN   A 1 143 ? 15.685  4.670   11.189  1.00 16.57 ? 142 ASN   A OD1 1 
ATOM   1088 N ND2 . ASN   A 1 143 ? 14.781  3.202   9.747   1.00 15.84 ? 142 ASN   A ND2 1 
ATOM   1089 N N   . ILE   A 1 144 ? 20.098  2.075   12.152  1.00 14.27 ? 143 ILE   A N   1 
ATOM   1090 C CA  . ILE   A 1 144 ? 21.114  1.212   12.748  1.00 14.62 ? 143 ILE   A CA  1 
ATOM   1091 C C   . ILE   A 1 144 ? 21.965  2.179   13.563  1.00 15.94 ? 143 ILE   A C   1 
ATOM   1092 O O   . ILE   A 1 144 ? 22.604  3.074   12.994  1.00 15.73 ? 143 ILE   A O   1 
ATOM   1093 C CB  . ILE   A 1 144 ? 21.969  0.524   11.655  1.00 15.14 ? 143 ILE   A CB  1 
ATOM   1094 C CG1 . ILE   A 1 144 ? 21.093  -0.355  10.761  1.00 15.29 ? 143 ILE   A CG1 1 
ATOM   1095 C CG2 . ILE   A 1 144 ? 23.081  -0.305  12.303  1.00 15.36 ? 143 ILE   A CG2 1 
ATOM   1096 C CD1 . ILE   A 1 144 ? 21.711  -0.699  9.382   1.00 16.04 ? 143 ILE   A CD1 1 
ATOM   1097 N N   . LEU   A 1 145 ? 21.949  2.026   14.889  1.00 16.20 ? 144 LEU   A N   1 
ATOM   1098 C CA  . LEU   A 1 145 ? 22.624  2.926   15.803  1.00 17.29 ? 144 LEU   A CA  1 
ATOM   1099 C C   . LEU   A 1 145 ? 23.919  2.360   16.330  1.00 18.19 ? 144 LEU   A C   1 
ATOM   1100 O O   . LEU   A 1 145 ? 24.084  1.138   16.458  1.00 18.15 ? 144 LEU   A O   1 
ATOM   1101 C CB  . LEU   A 1 145 ? 21.697  3.260   16.980  1.00 17.88 ? 144 LEU   A CB  1 
ATOM   1102 C CG  . LEU   A 1 145 ? 20.275  3.767   16.625  1.00 19.77 ? 144 LEU   A CG  1 
ATOM   1103 C CD1 . LEU   A 1 145 ? 19.560  4.215   17.872  1.00 20.25 ? 144 LEU   A CD1 1 
ATOM   1104 C CD2 . LEU   A 1 145 ? 20.300  4.940   15.640  1.00 20.57 ? 144 LEU   A CD2 1 
ATOM   1105 N N   . ILE   A 1 146 ? 24.849  3.259   16.629  1.00 18.03 ? 145 ILE   A N   1 
ATOM   1106 C CA  . ILE   A 1 146 ? 26.185  2.880   17.100  1.00 19.25 ? 145 ILE   A CA  1 
ATOM   1107 C C   . ILE   A 1 146 ? 26.445  3.488   18.463  1.00 20.30 ? 145 ILE   A C   1 
ATOM   1108 O O   . ILE   A 1 146 ? 26.239  4.696   18.648  1.00 20.59 ? 145 ILE   A O   1 
ATOM   1109 C CB  . ILE   A 1 146 ? 27.250  3.359   16.078  1.00 20.21 ? 145 ILE   A CB  1 
ATOM   1110 C CG1 . ILE   A 1 146 ? 26.979  2.829   14.648  1.00 20.78 ? 145 ILE   A CG1 1 
ATOM   1111 C CG2 . ILE   A 1 146 ? 28.687  3.051   16.538  1.00 21.07 ? 145 ILE   A CG2 1 
ATOM   1112 C CD1 . ILE   A 1 146 ? 26.950  1.281   14.492  1.00 22.36 ? 145 ILE   A CD1 1 
ATOM   1113 N N   . ASN   A 1 147 ? 26.895  2.669   19.429  1.00 21.08 ? 146 ASN   A N   1 
ATOM   1114 C CA  . ASN   A 1 147 ? 27.227  3.206   20.748  1.00 22.43 ? 146 ASN   A CA  1 
ATOM   1115 C C   . ASN   A 1 147 ? 28.735  3.589   20.808  1.00 24.13 ? 146 ASN   A C   1 
ATOM   1116 O O   . ASN   A 1 147 ? 29.488  3.357   19.843  1.00 23.71 ? 146 ASN   A O   1 
ATOM   1117 C CB  . ASN   A 1 147 ? 26.754  2.277   21.887  1.00 23.45 ? 146 ASN   A CB  1 
ATOM   1118 C CG  . ASN   A 1 147 ? 27.510  0.977   22.004  1.00 25.26 ? 146 ASN   A CG  1 
ATOM   1119 O OD1 . ASN   A 1 147 ? 28.561  0.784   21.390  1.00 25.30 ? 146 ASN   A OD1 1 
ATOM   1120 N ND2 . ASN   A 1 147 ? 27.001  0.051   22.817  1.00 26.38 ? 146 ASN   A ND2 1 
ATOM   1121 N N   . ASP   A 1 148 ? 29.177  4.173   21.923  1.00 25.13 ? 147 ASP   A N   1 
ATOM   1122 C CA  . ASP   A 1 148 ? 30.567  4.595   22.047  1.00 26.31 ? 147 ASP   A CA  1 
ATOM   1123 C C   . ASP   A 1 148 ? 31.557  3.417   22.010  1.00 26.18 ? 147 ASP   A C   1 
ATOM   1124 O O   . ASP   A 1 148 ? 32.732  3.620   21.703  1.00 26.63 ? 147 ASP   A O   1 
ATOM   1125 C CB  . ASP   A 1 148 ? 30.756  5.489   23.274  1.00 29.79 ? 147 ASP   A CB  1 
ATOM   1126 C CG  . ASP   A 1 148 ? 29.998  6.801   23.144  1.00 37.94 ? 147 ASP   A CG  1 
ATOM   1127 O OD1 . ASP   A 1 148 ? 29.807  7.269   21.997  1.00 38.60 ? 147 ASP   A OD1 1 
ATOM   1128 O OD2 . ASP   A 1 148 ? 29.602  7.361   24.187  1.00 42.88 ? 147 ASP   A OD2 1 
ATOM   1129 N N   . ALA   A 1 149 ? 31.087  2.191   22.274  1.00 25.32 ? 148 ALA   A N   1 
ATOM   1130 C CA  . ALA   A 1 149 ? 31.949  1.017   22.205  1.00 25.50 ? 148 ALA   A CA  1 
ATOM   1131 C C   . ALA   A 1 149 ? 32.100  0.452   20.776  1.00 25.31 ? 148 ALA   A C   1 
ATOM   1132 O O   . ALA   A 1 149 ? 32.825  -0.515  20.597  1.00 25.59 ? 148 ALA   A O   1 
ATOM   1133 C CB  . ALA   A 1 149 ? 31.418  -0.064  23.132  1.00 25.98 ? 148 ALA   A CB  1 
ATOM   1134 N N   . GLY   A 1 150 ? 31.404  1.016   19.784  1.00 24.58 ? 149 GLY   A N   1 
ATOM   1135 C CA  . GLY   A 1 150 ? 31.467  0.497   18.417  1.00 24.22 ? 149 GLY   A CA  1 
ATOM   1136 C C   . GLY   A 1 150 ? 30.463  -0.617  18.152  1.00 23.65 ? 149 GLY   A C   1 
ATOM   1137 O O   . GLY   A 1 150 ? 30.516  -1.280  17.106  1.00 24.05 ? 149 GLY   A O   1 
ATOM   1138 N N   . GLU   A 1 151 ? 29.547  -0.861  19.107  1.00 22.35 ? 150 GLU   A N   1 
ATOM   1139 C CA  . GLU   A 1 151 ? 28.549  -1.910  18.957  1.00 21.94 ? 150 GLU   A CA  1 
ATOM   1140 C C   . GLU   A 1 151 ? 27.429  -1.460  18.046  1.00 20.59 ? 150 GLU   A C   1 
ATOM   1141 O O   . GLU   A 1 151 ? 27.100  -0.274  17.995  1.00 20.17 ? 150 GLU   A O   1 
ATOM   1142 C CB  . GLU   A 1 151 ? 28.041  -2.373  20.321  1.00 24.46 ? 150 GLU   A CB  1 
ATOM   1143 C CG  . GLU   A 1 151 ? 29.179  -2.983  21.124  1.00 28.90 ? 150 GLU   A CG  1 
ATOM   1144 C CD  . GLU   A 1 151 ? 28.829  -3.352  22.547  1.00 38.55 ? 150 GLU   A CD  1 
ATOM   1145 O OE1 . GLU   A 1 151 ? 28.045  -2.608  23.179  1.00 38.71 ? 150 GLU   A OE1 1 
ATOM   1146 O OE2 . GLU   A 1 151 ? 29.336  -4.390  23.031  1.00 43.05 ? 150 GLU   A OE2 1 
ATOM   1147 N N   . VAL   A 1 152 ? 26.865  -2.413  17.307  1.00 19.15 ? 151 VAL   A N   1 
ATOM   1148 C CA  . VAL   A 1 152 ? 25.847  -2.183  16.296  1.00 19.23 ? 151 VAL   A CA  1 
ATOM   1149 C C   . VAL   A 1 152 ? 24.488  -2.640  16.768  1.00 19.99 ? 151 VAL   A C   1 
ATOM   1150 O O   . VAL   A 1 152 ? 24.337  -3.789  17.175  1.00 21.35 ? 151 VAL   A O   1 
ATOM   1151 C CB  . VAL   A 1 152 ? 26.274  -2.872  14.980  1.00 19.91 ? 151 VAL   A CB  1 
ATOM   1152 C CG1 . VAL   A 1 152 ? 25.165  -2.791  13.927  1.00 20.76 ? 151 VAL   A CG1 1 
ATOM   1153 C CG2 . VAL   A 1 152 ? 27.576  -2.276  14.464  1.00 20.57 ? 151 VAL   A CG2 1 
ATOM   1154 N N   . ARG   A 1 153 ? 23.507  -1.722  16.779  1.00 19.34 ? 152 ARG   A N   1 
ATOM   1155 C CA  . ARG   A 1 153 ? 22.180  -2.066  17.256  1.00 19.41 ? 152 ARG   A CA  1 
ATOM   1156 C C   . ARG   A 1 153 ? 21.123  -1.513  16.339  1.00 18.42 ? 152 ARG   A C   1 
ATOM   1157 O O   . ARG   A 1 153 ? 21.140  -0.316  16.074  1.00 18.85 ? 152 ARG   A O   1 
ATOM   1158 C CB  . ARG   A 1 153 ? 21.928  -1.405  18.623  1.00 23.33 ? 152 ARG   A CB  1 
ATOM   1159 C CG  . ARG   A 1 153 ? 23.037  -1.508  19.654  1.00 29.58 ? 152 ARG   A CG  1 
ATOM   1160 C CD  . ARG   A 1 153 ? 22.677  -2.586  20.634  1.00 33.59 ? 152 ARG   A CD  1 
ATOM   1161 N NE  . ARG   A 1 153 ? 23.648  -2.738  21.720  1.00 36.53 ? 152 ARG   A NE  1 
ATOM   1162 C CZ  . ARG   A 1 153 ? 24.731  -3.506  21.661  1.00 39.05 ? 152 ARG   A CZ  1 
ATOM   1163 N NH1 . ARG   A 1 153 ? 25.522  -3.631  22.719  1.00 38.35 ? 152 ARG   A NH1 1 
ATOM   1164 N NH2 . ARG   A 1 153 ? 25.021  -4.172  20.549  1.00 38.89 ? 152 ARG   A NH2 1 
ATOM   1165 N N   . LEU   A 1 154 ? 20.112  -2.316  15.992  1.00 16.06 ? 153 LEU   A N   1 
ATOM   1166 C CA  . LEU   A 1 154 ? 18.936  -1.792  15.281  1.00 16.26 ? 153 LEU   A CA  1 
ATOM   1167 C C   . LEU   A 1 154 ? 18.205  -0.866  16.259  1.00 17.96 ? 153 LEU   A C   1 
ATOM   1168 O O   . LEU   A 1 154 ? 18.037  -1.230  17.428  1.00 18.24 ? 153 LEU   A O   1 
ATOM   1169 C CB  . LEU   A 1 154 ? 18.005  -2.959  14.932  1.00 16.66 ? 153 LEU   A CB  1 
ATOM   1170 C CG  . LEU   A 1 154 ? 18.529  -3.944  13.900  1.00 16.67 ? 153 LEU   A CG  1 
ATOM   1171 C CD1 . LEU   A 1 154 ? 17.569  -5.133  13.727  1.00 16.99 ? 153 LEU   A CD1 1 
ATOM   1172 C CD2 . LEU   A 1 154 ? 18.732  -3.255  12.559  1.00 18.04 ? 153 LEU   A CD2 1 
ATOM   1173 N N   . ALA   A 1 155 ? 17.805  0.330   15.811  1.00 17.99 ? 154 ALA   A N   1 
ATOM   1174 C CA  . ALA   A 1 155 ? 17.104  1.290   16.681  1.00 19.34 ? 154 ALA   A CA  1 
ATOM   1175 C C   . ALA   A 1 155 ? 15.878  0.683   17.376  1.00 20.66 ? 154 ALA   A C   1 
ATOM   1176 O O   . ALA   A 1 155 ? 15.607  0.967   18.544  1.00 21.82 ? 154 ALA   A O   1 
ATOM   1177 C CB  . ALA   A 1 155 ? 16.686  2.506   15.868  1.00 19.25 ? 154 ALA   A CB  1 
ATOM   1178 N N   . ASP   A 1 156 ? 15.124  -0.129  16.648  1.00 20.65 ? 155 ASP   A N   1 
ATOM   1179 C CA  . ASP   A 1 156 ? 13.937  -0.800  17.181  1.00 20.76 ? 155 ASP   A CA  1 
ATOM   1180 C C   . ASP   A 1 156 ? 13.673  -2.085  16.373  1.00 21.48 ? 155 ASP   A C   1 
ATOM   1181 O O   . ASP   A 1 156 ? 14.446  -2.414  15.459  1.00 20.94 ? 155 ASP   A O   1 
ATOM   1182 C CB  . ASP   A 1 156 ? 12.706  0.155   17.205  1.00 21.75 ? 155 ASP   A CB  1 
ATOM   1183 C CG  . ASP   A 1 156 ? 12.286  0.722   15.864  1.00 24.33 ? 155 ASP   A CG  1 
ATOM   1184 O OD1 . ASP   A 1 156 ? 12.564  0.078   14.828  1.00 23.26 ? 155 ASP   A OD1 1 
ATOM   1185 O OD2 . ASP   A 1 156 ? 11.673  1.810   15.845  1.00 26.32 ? 155 ASP   A OD2 1 
ATOM   1186 N N   . PHE   A 1 157 ? 12.591  -2.819  16.689  1.00 22.63 ? 156 PHE   A N   1 
ATOM   1187 C CA  . PHE   A 1 157 ? 12.278  -4.034  15.946  1.00 23.04 ? 156 PHE   A CA  1 
ATOM   1188 C C   . PHE   A 1 157 ? 11.516  -3.778  14.639  1.00 21.25 ? 156 PHE   A C   1 
ATOM   1189 O O   . PHE   A 1 157 ? 11.011  -4.730  14.049  1.00 21.02 ? 156 PHE   A O   1 
ATOM   1190 C CB  . PHE   A 1 157 ? 11.553  -5.069  16.826  1.00 24.84 ? 156 PHE   A CB  1 
ATOM   1191 C CG  . PHE   A 1 157 ? 10.338  -4.594  17.575  1.00 27.05 ? 156 PHE   A CG  1 
ATOM   1192 C CD1 . PHE   A 1 157 ? 9.225   -4.121  16.898  1.00 28.93 ? 156 PHE   A CD1 1 
ATOM   1193 C CD2 . PHE   A 1 157 ? 10.252  -4.743  18.952  1.00 28.71 ? 156 PHE   A CD2 1 
ATOM   1194 C CE1 . PHE   A 1 157 ? 8.076   -3.741  17.590  1.00 30.17 ? 156 PHE   A CE1 1 
ATOM   1195 C CE2 . PHE   A 1 157 ? 9.112   -4.356  19.640  1.00 29.83 ? 156 PHE   A CE2 1 
ATOM   1196 C CZ  . PHE   A 1 157 ? 8.031   -3.857  18.956  1.00 29.86 ? 156 PHE   A CZ  1 
ATOM   1197 N N   . GLY   A 1 158 ? 11.415  -2.510  14.208  1.00 21.08 ? 157 GLY   A N   1 
ATOM   1198 C CA  . GLY   A 1 158 ? 10.760  -2.170  12.961  1.00 20.53 ? 157 GLY   A CA  1 
ATOM   1199 C C   . GLY   A 1 158 ? 9.395   -1.526  13.083  1.00 21.19 ? 157 GLY   A C   1 
ATOM   1200 O O   . GLY   A 1 158 ? 9.044   -0.979  14.132  1.00 21.55 ? 157 GLY   A O   1 
ATOM   1201 N N   . ILE   A 1 159 ? 8.597   -1.642  12.031  1.00 20.36 ? 158 ILE   A N   1 
ATOM   1202 C CA  . ILE   A 1 159 ? 7.276   -0.989  12.008  1.00 21.10 ? 158 ILE   A CA  1 
ATOM   1203 C C   . ILE   A 1 159 ? 6.128   -1.699  12.718  1.00 23.79 ? 158 ILE   A C   1 
ATOM   1204 O O   . ILE   A 1 159 ? 5.042   -1.123  12.745  1.00 25.05 ? 158 ILE   A O   1 
ATOM   1205 C CB  . ILE   A 1 159 ? 6.870   -0.760  10.534  1.00 20.28 ? 158 ILE   A CB  1 
ATOM   1206 C CG1 . ILE   A 1 159 ? 6.551   -2.091  9.814   1.00 21.01 ? 158 ILE   A CG1 1 
ATOM   1207 C CG2 . ILE   A 1 159 ? 7.899   0.082   9.778   1.00 20.13 ? 158 ILE   A CG2 1 
ATOM   1208 C CD1 . ILE   A 1 159 ? 5.790   -1.874  8.512   1.00 22.31 ? 158 ILE   A CD1 1 
ATOM   1209 N N   . SER   A 1 160 ? 6.291   -2.936  13.191  1.00 24.55 ? 159 SER   A N   1 
ATOM   1210 C CA  . SER   A 1 160 ? 5.169   -3.731  13.685  1.00 26.47 ? 159 SER   A CA  1 
ATOM   1211 C C   . SER   A 1 160 ? 4.519   -3.328  15.021  1.00 29.78 ? 159 SER   A C   1 
ATOM   1212 O O   . SER   A 1 160 ? 3.494   -3.936  15.356  1.00 30.48 ? 159 SER   A O   1 
ATOM   1213 C CB  . SER   A 1 160 ? 5.518   -5.207  13.746  1.00 26.22 ? 159 SER   A CB  1 
ATOM   1214 O OG  . SER   A 1 160 ? 6.552   -5.467  14.676  1.00 25.83 ? 159 SER   A OG  1 
ATOM   1215 N N   . ALA   A 1 161 ? 5.041   -2.325  15.750  1.00 31.13 ? 160 ALA   A N   1 
ATOM   1216 C CA  . ALA   A 1 161 ? 4.393   -1.906  17.006  1.00 33.22 ? 160 ALA   A CA  1 
ATOM   1217 C C   . ALA   A 1 161 ? 2.960   -1.403  16.736  1.00 35.64 ? 160 ALA   A C   1 
ATOM   1218 O O   . ALA   A 1 161 ? 2.776   -0.448  15.979  1.00 35.73 ? 160 ALA   A O   1 
ATOM   1219 C CB  . ALA   A 1 161 ? 5.208   -0.820  17.689  1.00 33.21 ? 160 ALA   A CB  1 
ATOM   1220 N N   . GLN   A 1 162 ? 1.953   -2.086  17.317  1.00 37.04 ? 161 GLN   A N   1 
ATOM   1221 C CA  . GLN   A 1 162 ? 0.543   -1.746  17.140  1.00 38.94 ? 161 GLN   A CA  1 
ATOM   1222 C C   . GLN   A 1 162 ? 0.115   -0.662  18.120  1.00 39.95 ? 161 GLN   A C   1 
ATOM   1223 O O   . GLN   A 1 162 ? -0.939  -0.754  18.750  1.00 40.75 ? 161 GLN   A O   1 
ATOM   1224 C CB  . GLN   A 1 162 ? -0.339  -2.992  17.272  1.00 41.62 ? 161 GLN   A CB  1 
ATOM   1225 C CG  . GLN   A 1 162 ? -0.019  -4.075  16.250  1.00 46.68 ? 161 GLN   A CG  1 
ATOM   1226 C CD  . GLN   A 1 162 ? -1.216  -4.959  16.022  1.00 54.33 ? 161 GLN   A CD  1 
ATOM   1227 O OE1 . GLN   A 1 162 ? -2.189  -4.565  15.363  1.00 57.19 ? 161 GLN   A OE1 1 
ATOM   1228 N NE2 . GLN   A 1 162 ? -1.184  -6.171  16.573  1.00 55.64 ? 161 GLN   A NE2 1 
ATOM   1229 N N   . ILE   A 1 163 ? 0.960   0.357   18.262  1.00 39.94 ? 162 ILE   A N   1 
ATOM   1230 C CA  . ILE   A 1 163 ? 0.748   1.529   19.115  1.00 40.45 ? 162 ILE   A CA  1 
ATOM   1231 C C   . ILE   A 1 163 ? 1.304   2.763   18.401  1.00 39.84 ? 162 ILE   A C   1 
ATOM   1232 O O   . ILE   A 1 163 ? 2.125   2.637   17.495  1.00 40.42 ? 162 ILE   A O   1 
ATOM   1233 C CB  . ILE   A 1 163 ? 1.380   1.380   20.530  1.00 41.72 ? 162 ILE   A CB  1 
ATOM   1234 C CG1 . ILE   A 1 163 ? 2.774   0.737   20.482  1.00 43.19 ? 162 ILE   A CG1 1 
ATOM   1235 C CG2 . ILE   A 1 163 ? 0.451   0.657   21.495  1.00 42.44 ? 162 ILE   A CG2 1 
ATOM   1236 C CD1 . ILE   A 1 163 ? 3.537   0.833   21.799  1.00 45.03 ? 162 ILE   A CD1 1 
ATOM   1237 N N   . GLY   A 1 164 ? 0.857   3.940   18.802  1.00 39.01 ? 163 GLY   A N   1 
ATOM   1238 C CA  . GLY   A 1 164 ? 1.336   5.185   18.220  1.00 38.50 ? 163 GLY   A CA  1 
ATOM   1239 C C   . GLY   A 1 164 ? 0.922   5.414   16.781  1.00 37.63 ? 163 GLY   A C   1 
ATOM   1240 O O   . GLY   A 1 164 ? -0.150  4.974   16.355  1.00 37.25 ? 163 GLY   A O   1 
ATOM   1241 N N   . ALA   A 1 165 ? 1.782   6.093   16.013  1.00 36.63 ? 164 ALA   A N   1 
ATOM   1242 C CA  . ALA   A 1 165 ? 1.494   6.420   14.620  1.00 35.67 ? 164 ALA   A CA  1 
ATOM   1243 C C   . ALA   A 1 165 ? 1.847   5.262   13.683  1.00 33.96 ? 164 ALA   A C   1 
ATOM   1244 O O   . ALA   A 1 165 ? 2.603   5.436   12.719  1.00 34.23 ? 164 ALA   A O   1 
ATOM   1245 C CB  . ALA   A 1 165 ? 2.239   7.694   14.222  1.00 35.88 ? 164 ALA   A CB  1 
ATOM   1246 N N   . GLU   A 1 166 ? 1.283   4.070   13.960  1.00 31.67 ? 165 GLU   A N   1 
ATOM   1247 C CA  . GLU   A 1 166 ? 1.508   2.863   13.178  1.00 29.58 ? 165 GLU   A CA  1 
ATOM   1248 C C   . GLU   A 1 166 ? 1.237   3.080   11.696  1.00 27.38 ? 165 GLU   A C   1 
ATOM   1249 O O   . GLU   A 1 166 ? 2.083   2.723   10.891  1.00 27.40 ? 165 GLU   A O   1 
ATOM   1250 C CB  . GLU   A 1 166 ? 0.655   1.691   13.720  1.00 31.35 ? 165 GLU   A CB  1 
ATOM   1251 C CG  . GLU   A 1 166 ? 0.948   0.343   13.075  1.00 33.94 ? 165 GLU   A CG  1 
ATOM   1252 C CD  . GLU   A 1 166 ? 0.284   0.068   11.739  1.00 36.70 ? 165 GLU   A CD  1 
ATOM   1253 O OE1 . GLU   A 1 166 ? -0.841  0.571   11.507  1.00 36.46 ? 165 GLU   A OE1 1 
ATOM   1254 O OE2 . GLU   A 1 166 ? 0.904   -0.631  10.906  1.00 36.85 ? 165 GLU   A OE2 1 
ATOM   1255 N N   . LEU   A 1 167 ? 0.090   3.696   11.328  1.00 25.89 ? 166 LEU   A N   1 
ATOM   1256 C CA  . LEU   A 1 167 ? -0.231  3.861   9.912   1.00 25.10 ? 166 LEU   A CA  1 
ATOM   1257 C C   . LEU   A 1 167 ? 0.765   4.753   9.191   1.00 24.62 ? 166 LEU   A C   1 
ATOM   1258 O O   . LEU   A 1 167 ? 1.202   4.418   8.094   1.00 24.33 ? 166 LEU   A O   1 
ATOM   1259 C CB  . LEU   A 1 167 ? -1.668  4.363   9.724   1.00 25.76 ? 166 LEU   A CB  1 
ATOM   1260 C CG  . LEU   A 1 167 ? -2.107  4.471   8.268   1.00 27.45 ? 166 LEU   A CG  1 
ATOM   1261 C CD1 . LEU   A 1 167 ? -2.119  3.092   7.590   1.00 27.66 ? 166 LEU   A CD1 1 
ATOM   1262 C CD2 . LEU   A 1 167 ? -3.461  5.109   8.183   1.00 28.04 ? 166 LEU   A CD2 1 
ATOM   1263 N N   . ALA   A 1 168 ? 1.147   5.884   9.800   1.00 25.00 ? 167 ALA   A N   1 
ATOM   1264 C CA  . ALA   A 1 168 ? 2.136   6.782   9.187   1.00 25.34 ? 167 ALA   A CA  1 
ATOM   1265 C C   . ALA   A 1 168 ? 3.493   6.059   9.022   1.00 24.65 ? 167 ALA   A C   1 
ATOM   1266 O O   . ALA   A 1 168 ? 4.186   6.225   8.015   1.00 24.16 ? 167 ALA   A O   1 
ATOM   1267 C CB  . ALA   A 1 168 ? 2.319   8.018   10.050  1.00 26.21 ? 167 ALA   A CB  1 
ATOM   1268 N N   . ARG   A 1 169 ? 3.858   5.246   10.011  1.00 23.73 ? 168 ARG   A N   1 
ATOM   1269 C CA  . ARG   A 1 169 ? 5.104   4.489   9.954   1.00 23.58 ? 168 ARG   A CA  1 
ATOM   1270 C C   . ARG   A 1 169 ? 5.081   3.448   8.851   1.00 22.43 ? 168 ARG   A C   1 
ATOM   1271 O O   . ARG   A 1 169 ? 6.052   3.265   8.126   1.00 22.23 ? 168 ARG   A O   1 
ATOM   1272 C CB  . ARG   A 1 169 ? 5.367   3.819   11.294  1.00 25.66 ? 168 ARG   A CB  1 
ATOM   1273 C CG  . ARG   A 1 169 ? 6.700   4.239   11.788  1.00 29.31 ? 168 ARG   A CG  1 
ATOM   1274 C CD  . ARG   A 1 169 ? 7.146   3.476   12.974  1.00 29.94 ? 168 ARG   A CD  1 
ATOM   1275 N NE  . ARG   A 1 169 ? 8.522   3.070   12.747  1.00 29.65 ? 168 ARG   A NE  1 
ATOM   1276 C CZ  . ARG   A 1 169 ? 9.298   2.509   13.656  1.00 30.35 ? 168 ARG   A CZ  1 
ATOM   1277 N NH1 . ARG   A 1 169 ? 10.544  2.177   13.354  1.00 29.39 ? 168 ARG   A NH1 1 
ATOM   1278 N NH2 . ARG   A 1 169 ? 8.837   2.274   14.881  1.00 29.85 ? 168 ARG   A NH2 1 
ATOM   1279 N N   . ARG   A 1 170 ? 3.956   2.763   8.723   1.00 21.15 ? 169 ARG   A N   1 
ATOM   1280 C CA  . ARG   A 1 170 ? 3.786   1.706   7.743   1.00 20.23 ? 169 ARG   A CA  1 
ATOM   1281 C C   . ARG   A 1 170 ? 3.828   2.239   6.297   1.00 19.66 ? 169 ARG   A C   1 
ATOM   1282 O O   . ARG   A 1 170 ? 4.357   1.588   5.410   1.00 18.97 ? 169 ARG   A O   1 
ATOM   1283 C CB  . ARG   A 1 170 ? 2.421   1.084   8.013   1.00 22.04 ? 169 ARG   A CB  1 
ATOM   1284 C CG  . ARG   A 1 170 ? 2.214   -0.234  7.327   1.00 23.48 ? 169 ARG   A CG  1 
ATOM   1285 C CD  . ARG   A 1 170 ? 0.766   -0.391  6.985   1.00 22.98 ? 169 ARG   A CD  1 
ATOM   1286 N NE  . ARG   A 1 170 ? -0.111  -0.334  8.165   1.00 23.91 ? 169 ARG   A NE  1 
ATOM   1287 C CZ  . ARG   A 1 170 ? -1.438  -0.399  8.100   1.00 24.98 ? 169 ARG   A CZ  1 
ATOM   1288 N NH1 . ARG   A 1 170 ? -2.171  -0.300  9.205   1.00 26.07 ? 169 ARG   A NH1 1 
ATOM   1289 N NH2 . ARG   A 1 170 ? -2.047  -0.539  6.927   1.00 23.31 ? 169 ARG   A NH2 1 
ATOM   1290 N N   . LEU   A 1 171 ? 3.189   3.412   6.047   1.00 19.58 ? 170 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 171 ? 3.115   3.980   4.696   1.00 19.72 ? 170 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 171 ? 4.268   4.908   4.323   1.00 19.21 ? 170 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 171 ? 4.332   5.376   3.177   1.00 18.73 ? 170 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 171 ? 1.804   4.780   4.558   1.00 20.02 ? 170 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 171 ? 0.498   4.049   4.880   1.00 23.39 ? 170 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 171 ? -0.732  5.003   4.704   1.00 23.29 ? 170 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 171 ? 0.353   2.805   4.014   1.00 25.68 ? 170 LEU   A CD2 1 
ATOM   1298 N N   . GLU   A 1 172 ? 5.152   5.210   5.278   1.00 19.28 ? 171 GLU   A N   1 
ATOM   1299 C CA  . GLU   A 1 172 ? 6.266   6.126   5.072   1.00 19.05 ? 171 GLU   A CA  1 
ATOM   1300 C C   . GLU   A 1 172 ? 7.129   5.796   3.863   1.00 18.30 ? 171 GLU   A C   1 
ATOM   1301 O O   . GLU   A 1 172 ? 7.504   6.709   3.142   1.00 19.19 ? 171 GLU   A O   1 
ATOM   1302 C CB  . GLU   A 1 172 ? 7.102   6.215   6.328   1.00 21.10 ? 171 GLU   A CB  1 
ATOM   1303 C CG  . GLU   A 1 172 ? 8.155   7.302   6.292   1.00 25.40 ? 171 GLU   A CG  1 
ATOM   1304 C CD  . GLU   A 1 172 ? 8.688   7.653   7.663   1.00 28.62 ? 171 GLU   A CD  1 
ATOM   1305 O OE1 . GLU   A 1 172 ? 9.181   8.792   7.842   1.00 28.86 ? 171 GLU   A OE1 1 
ATOM   1306 O OE2 . GLU   A 1 172 ? 8.597   6.795   8.567   1.00 28.38 ? 171 GLU   A OE2 1 
ATOM   1307 N N   . PHE   A 1 173 ? 7.434   4.500   3.620   1.00 16.32 ? 172 PHE   A N   1 
ATOM   1308 C CA  . PHE   A 1 173 ? 8.245   4.129   2.461   1.00 15.48 ? 172 PHE   A CA  1 
ATOM   1309 C C   . PHE   A 1 173 ? 7.664   4.583   1.124   1.00 15.40 ? 172 PHE   A C   1 
ATOM   1310 O O   . PHE   A 1 173 ? 8.427   4.716   0.175   1.00 14.87 ? 172 PHE   A O   1 
ATOM   1311 C CB  . PHE   A 1 173 ? 8.512   2.614   2.433   1.00 15.04 ? 172 PHE   A CB  1 
ATOM   1312 C CG  . PHE   A 1 173 ? 7.376   1.835   1.819   1.00 15.34 ? 172 PHE   A CG  1 
ATOM   1313 C CD1 . PHE   A 1 173 ? 6.270   1.501   2.565   1.00 16.86 ? 172 PHE   A CD1 1 
ATOM   1314 C CD2 . PHE   A 1 173 ? 7.389   1.498   0.473   1.00 16.15 ? 172 PHE   A CD2 1 
ATOM   1315 C CE1 . PHE   A 1 173 ? 5.195   0.842   1.988   1.00 18.31 ? 172 PHE   A CE1 1 
ATOM   1316 C CE2 . PHE   A 1 173 ? 6.316   0.818   -0.098  1.00 17.23 ? 172 PHE   A CE2 1 
ATOM   1317 C CZ  . PHE   A 1 173 ? 5.235   0.490   0.668   1.00 18.15 ? 172 PHE   A CZ  1 
ATOM   1318 N N   . ILE   A 1 174 ? 6.331   4.807   1.004   1.00 17.43 ? 173 ILE   A N   1 
ATOM   1319 C CA  . ILE   A 1 174 ? 5.772   5.255   -0.271  1.00 18.39 ? 173 ILE   A CA  1 
ATOM   1320 C C   . ILE   A 1 174 ? 6.413   6.592   -0.740  1.00 19.86 ? 173 ILE   A C   1 
ATOM   1321 O O   . ILE   A 1 174 ? 6.670   6.776   -1.930  1.00 21.26 ? 173 ILE   A O   1 
ATOM   1322 C CB  . ILE   A 1 174 ? 4.247   5.304   -0.172  1.00 19.00 ? 173 ILE   A CB  1 
ATOM   1323 C CG1 . ILE   A 1 174 ? 3.696   3.871   -0.041  1.00 19.26 ? 173 ILE   A CG1 1 
ATOM   1324 C CG2 . ILE   A 1 174 ? 3.641   6.022   -1.380  1.00 20.53 ? 173 ILE   A CG2 1 
ATOM   1325 C CD1 . ILE   A 1 174 ? 2.144   3.822   0.308   1.00 21.06 ? 173 ILE   A CD1 1 
ATOM   1326 N N   . GLY   A 1 175 ? 6.749   7.458   0.211   1.00 19.11 ? 174 GLY   A N   1 
ATOM   1327 C CA  . GLY   A 1 175 ? 7.438   8.710   -0.093  1.00 19.46 ? 174 GLY   A CA  1 
ATOM   1328 C C   . GLY   A 1 175 ? 8.961   8.606   -0.090  1.00 18.81 ? 174 GLY   A C   1 
ATOM   1329 O O   . GLY   A 1 175 ? 9.649   9.591   -0.372  1.00 19.05 ? 174 GLY   A O   1 
ATOM   1330 N N   . THR   A 1 176 ? 9.517   7.413   0.223   1.00 18.05 ? 175 THR   A N   1 
ATOM   1331 C CA  . THR   A 1 176 ? 10.977  7.170   0.302   1.00 17.08 ? 175 THR   A CA  1 
ATOM   1332 C C   . THR   A 1 176 ? 11.227  5.638   0.211   1.00 16.65 ? 175 THR   A C   1 
ATOM   1333 O O   . THR   A 1 176 ? 11.411  4.974   1.223   1.00 16.42 ? 175 THR   A O   1 
ATOM   1334 C CB  . THR   A 1 176 ? 11.571  7.813   1.558   1.00 18.40 ? 175 THR   A CB  1 
ATOM   1335 O OG1 . THR   A 1 176 ? 12.923  7.366   1.707   1.00 19.72 ? 175 THR   A OG1 1 
ATOM   1336 C CG2 . THR   A 1 176 ? 10.788  7.503   2.828   1.00 18.31 ? 175 THR   A CG2 1 
ATOM   1337 N N   . PRO   A 1 177 ? 11.056  5.070   -0.998  1.00 15.82 ? 176 PRO   A N   1 
ATOM   1338 C CA  . PRO   A 1 177 ? 11.011  3.605   -1.134  1.00 14.60 ? 176 PRO   A CA  1 
ATOM   1339 C C   . PRO   A 1 177 ? 12.316  2.940   -1.467  1.00 14.10 ? 176 PRO   A C   1 
ATOM   1340 O O   . PRO   A 1 177 ? 12.341  1.765   -1.768  1.00 14.67 ? 176 PRO   A O   1 
ATOM   1341 C CB  . PRO   A 1 177 ? 10.066  3.419   -2.311  1.00 16.04 ? 176 PRO   A CB  1 
ATOM   1342 C CG  . PRO   A 1 177 ? 10.417  4.593   -3.216  1.00 17.69 ? 176 PRO   A CG  1 
ATOM   1343 C CD  . PRO   A 1 177 ? 10.735  5.743   -2.275  1.00 15.72 ? 176 PRO   A CD  1 
ATOM   1344 N N   . TYR   A 1 178 ? 13.402  3.709   -1.439  1.00 13.41 ? 177 TYR   A N   1 
ATOM   1345 C CA  . TYR   A 1 178 ? 14.714  3.256   -1.920  1.00 12.37 ? 177 TYR   A CA  1 
ATOM   1346 C C   . TYR   A 1 178 ? 15.257  2.008   -1.248  1.00 13.23 ? 177 TYR   A C   1 
ATOM   1347 O O   . TYR   A 1 178 ? 16.036  1.296   -1.866  1.00 13.55 ? 177 TYR   A O   1 
ATOM   1348 C CB  . TYR   A 1 178 ? 15.742  4.398   -1.830  1.00 12.03 ? 177 TYR   A CB  1 
ATOM   1349 C CG  . TYR   A 1 178 ? 15.169  5.710   -2.321  1.00 12.79 ? 177 TYR   A CG  1 
ATOM   1350 C CD1 . TYR   A 1 178 ? 15.113  6.005   -3.677  1.00 13.55 ? 177 TYR   A CD1 1 
ATOM   1351 C CD2 . TYR   A 1 178 ? 14.662  6.645   -1.432  1.00 12.85 ? 177 TYR   A CD2 1 
ATOM   1352 C CE1 . TYR   A 1 178 ? 14.552  7.193   -4.130  1.00 13.61 ? 177 TYR   A CE1 1 
ATOM   1353 C CE2 . TYR   A 1 178 ? 14.058  7.819   -1.880  1.00 13.85 ? 177 TYR   A CE2 1 
ATOM   1354 C CZ  . TYR   A 1 178 ? 14.037  8.101   -3.227  1.00 14.50 ? 177 TYR   A CZ  1 
ATOM   1355 O OH  . TYR   A 1 178 ? 13.547  9.301   -3.673  1.00 16.71 ? 177 TYR   A OH  1 
ATOM   1356 N N   . TRP   A 1 179 ? 14.870  1.755   0.017   1.00 11.84 ? 178 TRP   A N   1 
ATOM   1357 C CA  . TRP   A 1 179 ? 15.393  0.586   0.731   1.00 11.90 ? 178 TRP   A CA  1 
ATOM   1358 C C   . TRP   A 1 179 ? 14.424  -0.619  0.727   1.00 10.98 ? 178 TRP   A C   1 
ATOM   1359 O O   . TRP   A 1 179 ? 14.780  -1.681  1.264   1.00 12.24 ? 178 TRP   A O   1 
ATOM   1360 C CB  . TRP   A 1 179 ? 15.661  0.958   2.193   1.00 12.03 ? 178 TRP   A CB  1 
ATOM   1361 C CG  . TRP   A 1 179 ? 16.870  1.829   2.382   1.00 12.24 ? 178 TRP   A CG  1 
ATOM   1362 C CD1 . TRP   A 1 179 ? 18.127  1.420   2.716   1.00 13.18 ? 178 TRP   A CD1 1 
ATOM   1363 C CD2 . TRP   A 1 179 ? 16.910  3.269   2.346   1.00 12.35 ? 178 TRP   A CD2 1 
ATOM   1364 N NE1 . TRP   A 1 179 ? 18.964  2.507   2.834   1.00 13.29 ? 178 TRP   A NE1 1 
ATOM   1365 C CE2 . TRP   A 1 179 ? 18.235  3.655   2.634   1.00 13.38 ? 178 TRP   A CE2 1 
ATOM   1366 C CE3 . TRP   A 1 179 ? 15.968  4.263   2.049   1.00 13.86 ? 178 TRP   A CE3 1 
ATOM   1367 C CZ2 . TRP   A 1 179 ? 18.625  4.992   2.688   1.00 13.77 ? 178 TRP   A CZ2 1 
ATOM   1368 C CZ3 . TRP   A 1 179 ? 16.364  5.592   2.095   1.00 14.60 ? 178 TRP   A CZ3 1 
ATOM   1369 C CH2 . TRP   A 1 179 ? 17.678  5.944   2.401   1.00 14.47 ? 178 TRP   A CH2 1 
ATOM   1370 N N   . MET   A 1 180 ? 13.236  -0.501  0.089   1.00 10.76 ? 179 MET   A N   1 
ATOM   1371 C CA  . MET   A 1 180 ? 12.294  -1.632  0.113   1.00 10.59 ? 179 MET   A CA  1 
ATOM   1372 C C   . MET   A 1 180 ? 12.442  -2.583  -1.045  1.00 11.46 ? 179 MET   A C   1 
ATOM   1373 O O   . MET   A 1 180 ? 12.736  -2.173  -2.176  1.00 11.08 ? 179 MET   A O   1 
ATOM   1374 C CB  . MET   A 1 180 ? 10.872  -1.116  0.220   1.00 11.55 ? 179 MET   A CB  1 
ATOM   1375 C CG  . MET   A 1 180 ? 10.613  -0.354  1.493   1.00 15.13 ? 179 MET   A CG  1 
ATOM   1376 S SD  . MET   A 1 180 ? 10.694  -1.319  3.021   1.00 15.95 ? 179 MET   A SD  1 
ATOM   1377 C CE  . MET   A 1 180 ? 12.144  -0.588  3.790   1.00 20.17 ? 179 MET   A CE  1 
ATOM   1378 N N   . ALA   A 1 181 ? 12.145  -3.858  -0.775  1.00 11.98 ? 180 ALA   A N   1 
ATOM   1379 C CA  . ALA   A 1 181 ? 12.215  -4.908  -1.770  1.00 13.65 ? 180 ALA   A CA  1 
ATOM   1380 C C   . ALA   A 1 181 ? 11.119  -4.725  -2.828  1.00 15.16 ? 180 ALA   A C   1 
ATOM   1381 O O   . ALA   A 1 181 ? 10.095  -4.080  -2.567  1.00 14.43 ? 180 ALA   A O   1 
ATOM   1382 C CB  . ALA   A 1 181 ? 12.054  -6.238  -1.057  1.00 13.33 ? 180 ALA   A CB  1 
ATOM   1383 N N   . PRO   A 1 182 ? 11.337  -5.217  -4.060  1.00 16.10 ? 181 PRO   A N   1 
ATOM   1384 C CA  . PRO   A 1 182 ? 10.330  -4.999  -5.111  1.00 15.68 ? 181 PRO   A CA  1 
ATOM   1385 C C   . PRO   A 1 182 ? 8.943   -5.565  -4.735  1.00 15.89 ? 181 PRO   A C   1 
ATOM   1386 O O   . PRO   A 1 182 ? 7.939   -4.930  -5.058  1.00 16.54 ? 181 PRO   A O   1 
ATOM   1387 C CB  . PRO   A 1 182 ? 10.947  -5.677  -6.353  1.00 17.14 ? 181 PRO   A CB  1 
ATOM   1388 C CG  . PRO   A 1 182 ? 12.442  -5.809  -6.038  1.00 18.29 ? 181 PRO   A CG  1 
ATOM   1389 C CD  . PRO   A 1 182 ? 12.522  -5.959  -4.552  1.00 16.45 ? 181 PRO   A CD  1 
ATOM   1390 N N   . GLU   A 1 183 ? 8.885   -6.655  -3.944  1.00 15.14 ? 182 GLU   A N   1 
ATOM   1391 C CA  . GLU   A 1 183 ? 7.569   -7.185  -3.526  1.00 15.45 ? 182 GLU   A CA  1 
ATOM   1392 C C   . GLU   A 1 183 ? 6.850   -6.261  -2.512  1.00 15.56 ? 182 GLU   A C   1 
ATOM   1393 O O   . GLU   A 1 183 ? 5.610   -6.305  -2.416  1.00 15.82 ? 182 GLU   A O   1 
ATOM   1394 C CB  . GLU   A 1 183 ? 7.667   -8.619  -3.031  1.00 16.73 ? 182 GLU   A CB  1 
ATOM   1395 C CG  . GLU   A 1 183 ? 8.430   -8.759  -1.730  1.00 18.61 ? 182 GLU   A CG  1 
ATOM   1396 C CD  . GLU   A 1 183 ? 9.932   -8.954  -1.808  1.00 16.68 ? 182 GLU   A CD  1 
ATOM   1397 O OE1 . GLU   A 1 183 ? 10.534  -8.723  -2.886  1.00 14.72 ? 182 GLU   A OE1 1 
ATOM   1398 O OE2 . GLU   A 1 183 ? 10.504  -9.374  -0.777  1.00 15.56 ? 182 GLU   A OE2 1 
ATOM   1399 N N   . VAL   A 1 184 ? 7.612   -5.392  -1.802  1.00 15.44 ? 183 VAL   A N   1 
ATOM   1400 C CA  . VAL   A 1 184 ? 7.047   -4.384  -0.886  1.00 15.52 ? 183 VAL   A CA  1 
ATOM   1401 C C   . VAL   A 1 184 ? 6.660   -3.114  -1.701  1.00 16.65 ? 183 VAL   A C   1 
ATOM   1402 O O   . VAL   A 1 184 ? 5.604   -2.499  -1.463  1.00 16.50 ? 183 VAL   A O   1 
ATOM   1403 C CB  . VAL   A 1 184 ? 8.045   -4.038  0.238   1.00 15.91 ? 183 VAL   A CB  1 
ATOM   1404 C CG1 . VAL   A 1 184 ? 7.542   -2.866  1.076   1.00 16.82 ? 183 VAL   A CG1 1 
ATOM   1405 C CG2 . VAL   A 1 184 ? 8.307   -5.258  1.101   1.00 15.58 ? 183 VAL   A CG2 1 
ATOM   1406 N N   . ALA   A 1 185 ? 7.520   -2.734  -2.680  1.00 16.17 ? 184 ALA   A N   1 
ATOM   1407 C CA  . ALA   A 1 185 ? 7.246   -1.640  -3.608  1.00 17.46 ? 184 ALA   A CA  1 
ATOM   1408 C C   . ALA   A 1 185 ? 5.989   -1.889  -4.431  1.00 16.83 ? 184 ALA   A C   1 
ATOM   1409 O O   . ALA   A 1 185 ? 5.382   -0.933  -4.911  1.00 16.81 ? 184 ALA   A O   1 
ATOM   1410 C CB  . ALA   A 1 185 ? 8.452   -1.402  -4.531  1.00 18.34 ? 184 ALA   A CB  1 
ATOM   1411 N N   . ALA   A 1 186 ? 5.591   -3.159  -4.600  1.00 16.27 ? 185 ALA   A N   1 
ATOM   1412 C CA  . ALA   A 1 186 ? 4.337   -3.531  -5.273  1.00 16.97 ? 185 ALA   A CA  1 
ATOM   1413 C C   . ALA   A 1 186 ? 3.158   -3.351  -4.290  1.00 18.21 ? 185 ALA   A C   1 
ATOM   1414 O O   . ALA   A 1 186 ? 2.209   -4.142  -4.234  1.00 18.06 ? 185 ALA   A O   1 
ATOM   1415 C CB  . ALA   A 1 186 ? 4.413   -4.961  -5.771  1.00 17.55 ? 185 ALA   A CB  1 
ATOM   1416 N N   . VAL   A 1 187 ? 3.184   -2.212  -3.586  1.00 19.03 ? 186 VAL   A N   1 
ATOM   1417 C CA  . VAL   A 1 187 ? 2.191   -1.820  -2.604  1.00 18.90 ? 186 VAL   A CA  1 
ATOM   1418 C C   . VAL   A 1 187 ? 0.813   -1.703  -3.228  1.00 17.83 ? 186 VAL   A C   1 
ATOM   1419 O O   . VAL   A 1 187 ? 0.656   -1.233  -4.353  1.00 18.10 ? 186 VAL   A O   1 
ATOM   1420 C CB  . VAL   A 1 187 ? 2.652   -0.515  -1.917  1.00 19.75 ? 186 VAL   A CB  1 
ATOM   1421 C CG1 . VAL   A 1 187 ? 2.783   0.611   -2.928  1.00 19.94 ? 186 VAL   A CG1 1 
ATOM   1422 C CG2 . VAL   A 1 187 ? 1.754   -0.138  -0.745  1.00 20.46 ? 186 VAL   A CG2 1 
ATOM   1423 N N   . ALA   A 1 188 ? -0.200  -2.170  -2.502  1.00 17.26 ? 187 ALA   A N   1 
ATOM   1424 C CA  . ALA   A 1 188 ? -1.619  -2.146  -2.934  1.00 17.64 ? 187 ALA   A CA  1 
ATOM   1425 C C   . ALA   A 1 188 ? -1.952  -3.090  -4.097  1.00 17.75 ? 187 ALA   A C   1 
ATOM   1426 O O   . ALA   A 1 188 ? -3.077  -3.053  -4.605  1.00 19.05 ? 187 ALA   A O   1 
ATOM   1427 C CB  . ALA   A 1 188 ? -2.097  -0.730  -3.233  1.00 18.01 ? 187 ALA   A CB  1 
ATOM   1428 N N   . LEU   A 1 189 ? -0.988  -3.946  -4.500  1.00 18.82 ? 188 LEU   A N   1 
ATOM   1429 C CA  . LEU   A 1 189 ? -1.262  -5.021  -5.454  1.00 19.83 ? 188 LEU   A CA  1 
ATOM   1430 C C   . LEU   A 1 189 ? -1.551  -6.288  -4.640  1.00 19.30 ? 188 LEU   A C   1 
ATOM   1431 O O   . LEU   A 1 189 ? -1.331  -6.315  -3.430  1.00 19.19 ? 188 LEU   A O   1 
ATOM   1432 C CB  . LEU   A 1 189 ? -0.122  -5.204  -6.474  1.00 20.38 ? 188 LEU   A CB  1 
ATOM   1433 C CG  . LEU   A 1 189 ? 0.031   -3.996  -7.427  1.00 21.50 ? 188 LEU   A CG  1 
ATOM   1434 C CD1 . LEU   A 1 189 ? 1.311   -4.126  -8.273  1.00 23.15 ? 188 LEU   A CD1 1 
ATOM   1435 C CD2 . LEU   A 1 189 ? -1.190  -3.827  -8.317  1.00 21.58 ? 188 LEU   A CD2 1 
ATOM   1436 N N   . LYS   A 1 190 ? -2.055  -7.335  -5.286  1.00 18.89 ? 189 LYS   A N   1 
ATOM   1437 C CA  . LYS   A 1 190 ? -2.510  -8.532  -4.589  1.00 18.82 ? 189 LYS   A CA  1 
ATOM   1438 C C   . LYS   A 1 190 ? -1.450  -9.307  -3.855  1.00 19.34 ? 189 LYS   A C   1 
ATOM   1439 O O   . LYS   A 1 190 ? -1.776  -10.010 -2.896  1.00 19.16 ? 189 LYS   A O   1 
ATOM   1440 C CB  . LYS   A 1 190 ? -3.260  -9.477  -5.554  1.00 19.09 ? 189 LYS   A CB  1 
ATOM   1441 C CG  . LYS   A 1 190 ? -2.327  -10.041 -6.638  1.00 21.44 ? 189 LYS   A CG  1 
ATOM   1442 C CD  . LYS   A 1 190 ? -3.069  -10.857 -7.706  1.00 25.66 ? 189 LYS   A CD  1 
ATOM   1443 C CE  . LYS   A 1 190 ? -2.063  -11.389 -8.719  1.00 31.31 ? 189 LYS   A CE  1 
ATOM   1444 N NZ  . LYS   A 1 190 ? -2.720  -12.064 -9.866  1.00 36.15 ? 189 LYS   A NZ  1 
ATOM   1445 N N   . GLY   A 1 191 ? -0.217  -9.263  -4.337  1.00 19.68 ? 190 GLY   A N   1 
ATOM   1446 C CA  . GLY   A 1 191 ? 0.824   -10.075 -3.736  1.00 21.71 ? 190 GLY   A CA  1 
ATOM   1447 C C   . GLY   A 1 191 ? 1.256   -9.431  -2.449  1.00 24.28 ? 190 GLY   A C   1 
ATOM   1448 O O   . GLY   A 1 191 ? 1.410   -8.201  -2.397  1.00 26.65 ? 190 GLY   A O   1 
ATOM   1449 N N   . GLY   A 1 192 ? 1.420   -10.246 -1.423  1.00 23.23 ? 191 GLY   A N   1 
ATOM   1450 C CA  . GLY   A 1 192 ? 1.933   -9.702  -0.176  1.00 21.19 ? 191 GLY   A CA  1 
ATOM   1451 C C   . GLY   A 1 192 ? 3.437   -9.839  -0.172  1.00 19.59 ? 191 GLY   A C   1 
ATOM   1452 O O   . GLY   A 1 192 ? 4.093   -9.772  -1.228  1.00 19.54 ? 191 GLY   A O   1 
ATOM   1453 N N   . TYR   A 1 193 ? 3.972   -9.935  1.016   1.00 17.01 ? 192 TYR   A N   1 
ATOM   1454 C CA  . TYR   A 1 193 ? 5.416   -10.089 1.180   1.00 16.41 ? 192 TYR   A CA  1 
ATOM   1455 C C   . TYR   A 1 193 ? 5.700   -10.889 2.453   1.00 17.35 ? 192 TYR   A C   1 
ATOM   1456 O O   . TYR   A 1 193 ? 4.779   -11.265 3.183   1.00 17.80 ? 192 TYR   A O   1 
ATOM   1457 C CB  . TYR   A 1 193 ? 6.164   -8.728  1.116   1.00 15.73 ? 192 TYR   A CB  1 
ATOM   1458 C CG  . TYR   A 1 193 ? 5.785   -7.754  2.213   1.00 15.99 ? 192 TYR   A CG  1 
ATOM   1459 C CD1 . TYR   A 1 193 ? 6.397   -7.805  3.458   1.00 16.82 ? 192 TYR   A CD1 1 
ATOM   1460 C CD2 . TYR   A 1 193 ? 4.858   -6.744  1.987   1.00 16.15 ? 192 TYR   A CD2 1 
ATOM   1461 C CE1 . TYR   A 1 193 ? 6.094   -6.884  4.451   1.00 16.73 ? 192 TYR   A CE1 1 
ATOM   1462 C CE2 . TYR   A 1 193 ? 4.578   -5.793  2.962   1.00 16.53 ? 192 TYR   A CE2 1 
ATOM   1463 C CZ  . TYR   A 1 193 ? 5.154   -5.897  4.214   1.00 17.02 ? 192 TYR   A CZ  1 
ATOM   1464 O OH  . TYR   A 1 193 ? 4.808   -5.028  5.229   1.00 16.83 ? 192 TYR   A OH  1 
ATOM   1465 N N   . ASN   A 1 194 ? 6.976   -11.228 2.674   1.00 16.09 ? 193 ASN   A N   1 
ATOM   1466 C CA  . ASN   A 1 194 ? 7.351   -11.959 3.865   1.00 14.80 ? 193 ASN   A CA  1 
ATOM   1467 C C   . ASN   A 1 194 ? 8.659   -11.326 4.426   1.00 14.58 ? 193 ASN   A C   1 
ATOM   1468 O O   . ASN   A 1 194 ? 9.136   -10.288 3.938   1.00 15.45 ? 193 ASN   A O   1 
ATOM   1469 C CB  . ASN   A 1 194 ? 7.428   -13.470 3.586   1.00 15.73 ? 193 ASN   A CB  1 
ATOM   1470 C CG  . ASN   A 1 194 ? 8.513   -13.841 2.610   1.00 17.73 ? 193 ASN   A CG  1 
ATOM   1471 O OD1 . ASN   A 1 194 ? 9.491   -13.105 2.419   1.00 15.68 ? 193 ASN   A OD1 1 
ATOM   1472 N ND2 . ASN   A 1 194 ? 8.363   -14.984 1.964   1.00 20.04 ? 193 ASN   A ND2 1 
ATOM   1473 N N   . GLU   A 1 195 ? 9.235   -11.964 5.433   1.00 14.43 ? 194 GLU   A N   1 
ATOM   1474 C CA  . GLU   A 1 195 ? 10.404  -11.435 6.120   1.00 13.80 ? 194 GLU   A CA  1 
ATOM   1475 C C   . GLU   A 1 195 ? 11.649  -11.303 5.236   1.00 14.31 ? 194 GLU   A C   1 
ATOM   1476 O O   . GLU   A 1 195 ? 12.597  -10.572 5.597   1.00 14.65 ? 194 GLU   A O   1 
ATOM   1477 C CB  . GLU   A 1 195 ? 10.709  -12.309 7.345   1.00 16.20 ? 194 GLU   A CB  1 
ATOM   1478 C CG  . GLU   A 1 195 ? 11.251  -13.682 7.015   1.00 17.94 ? 194 GLU   A CG  1 
ATOM   1479 C CD  . GLU   A 1 195 ? 10.282  -14.768 6.581   1.00 21.92 ? 194 GLU   A CD  1 
ATOM   1480 O OE1 . GLU   A 1 195 ? 10.782  -15.872 6.286   1.00 23.04 ? 194 GLU   A OE1 1 
ATOM   1481 O OE2 . GLU   A 1 195 ? 9.049   -14.536 6.516   1.00 23.11 ? 194 GLU   A OE2 1 
ATOM   1482 N N   . LEU   A 1 196 ? 11.655  -11.980 4.079   1.00 14.09 ? 195 LEU   A N   1 
ATOM   1483 C CA  . LEU   A 1 196 ? 12.795  -11.865 3.173   1.00 14.79 ? 195 LEU   A CA  1 
ATOM   1484 C C   . LEU   A 1 196 ? 12.947  -10.458 2.589   1.00 13.13 ? 195 LEU   A C   1 
ATOM   1485 O O   . LEU   A 1 196 ? 14.025  -10.128 2.078   1.00 13.87 ? 195 LEU   A O   1 
ATOM   1486 C CB  . LEU   A 1 196 ? 12.779  -12.937 2.099   1.00 15.28 ? 195 LEU   A CB  1 
ATOM   1487 C CG  . LEU   A 1 196 ? 12.867  -14.350 2.709   1.00 16.44 ? 195 LEU   A CG  1 
ATOM   1488 C CD1 . LEU   A 1 196 ? 12.588  -15.407 1.687   1.00 19.23 ? 195 LEU   A CD1 1 
ATOM   1489 C CD2 . LEU   A 1 196 ? 14.220  -14.574 3.383   1.00 16.50 ? 195 LEU   A CD2 1 
ATOM   1490 N N   . CYS   A 1 197 ? 11.910  -9.591  2.695   1.00 12.67 ? 196 CYS   A N   1 
ATOM   1491 C CA  . CYS   A 1 197 ? 12.060  -8.193  2.261   1.00 12.82 ? 196 CYS   A CA  1 
ATOM   1492 C C   . CYS   A 1 197 ? 13.172  -7.513  3.098   1.00 14.00 ? 196 CYS   A C   1 
ATOM   1493 O O   . CYS   A 1 197 ? 13.845  -6.637  2.576   1.00 15.09 ? 196 CYS   A O   1 
ATOM   1494 C CB  . CYS   A 1 197 ? 10.738  -7.431  2.353   1.00 12.97 ? 196 CYS   A CB  1 
ATOM   1495 S SG  . CYS   A 1 197 ? 10.164  -7.152  4.052   1.00 15.61 ? 196 CYS   A SG  1 
ATOM   1496 N N   . ASP   A 1 198 ? 13.401  -7.938  4.367   1.00 12.93 ? 197 ASP   A N   1 
ATOM   1497 C CA  . ASP   A 1 198 ? 14.481  -7.336  5.182   1.00 13.17 ? 197 ASP   A CA  1 
ATOM   1498 C C   . ASP   A 1 198 ? 15.867  -7.625  4.643   1.00 12.62 ? 197 ASP   A C   1 
ATOM   1499 O O   . ASP   A 1 198 ? 16.772  -6.802  4.793   1.00 12.67 ? 197 ASP   A O   1 
ATOM   1500 C CB  . ASP   A 1 198 ? 14.413  -7.812  6.638   1.00 14.44 ? 197 ASP   A CB  1 
ATOM   1501 C CG  . ASP   A 1 198 ? 13.213  -7.243  7.374   1.00 14.80 ? 197 ASP   A CG  1 
ATOM   1502 O OD1 . ASP   A 1 198 ? 12.792  -6.090  7.042   1.00 15.45 ? 197 ASP   A OD1 1 
ATOM   1503 O OD2 . ASP   A 1 198 ? 12.728  -7.908  8.334   1.00 14.97 ? 197 ASP   A OD2 1 
ATOM   1504 N N   . ILE   A 1 199 ? 16.044  -8.809  4.058   1.00 12.24 ? 198 ILE   A N   1 
ATOM   1505 C CA  . ILE   A 1 199 ? 17.342  -9.189  3.488   1.00 12.73 ? 198 ILE   A CA  1 
ATOM   1506 C C   . ILE   A 1 199 ? 17.687  -8.277  2.309   1.00 13.14 ? 198 ILE   A C   1 
ATOM   1507 O O   . ILE   A 1 199 ? 18.798  -7.747  2.241   1.00 12.91 ? 198 ILE   A O   1 
ATOM   1508 C CB  . ILE   A 1 199 ? 17.284  -10.680 3.104   1.00 13.65 ? 198 ILE   A CB  1 
ATOM   1509 C CG1 . ILE   A 1 199 ? 16.995  -11.532 4.379   1.00 14.81 ? 198 ILE   A CG1 1 
ATOM   1510 C CG2 . ILE   A 1 199 ? 18.573  -11.122 2.412   1.00 14.87 ? 198 ILE   A CG2 1 
ATOM   1511 C CD1 . ILE   A 1 199 ? 17.994  -11.403 5.425   1.00 15.66 ? 198 ILE   A CD1 1 
ATOM   1512 N N   . TRP   A 1 200 ? 16.686  -7.940  1.482   1.00 12.85 ? 199 TRP   A N   1 
ATOM   1513 C CA  . TRP   A 1 200 ? 16.903  -6.998  0.372   1.00 11.81 ? 199 TRP   A CA  1 
ATOM   1514 C C   . TRP   A 1 200 ? 17.276  -5.613  0.952   1.00 12.03 ? 199 TRP   A C   1 
ATOM   1515 O O   . TRP   A 1 200 ? 18.272  -4.991  0.539   1.00 12.98 ? 199 TRP   A O   1 
ATOM   1516 C CB  . TRP   A 1 200 ? 15.590  -6.882  -0.472  1.00 11.19 ? 199 TRP   A CB  1 
ATOM   1517 C CG  . TRP   A 1 200 ? 15.640  -5.814  -1.519  1.00 11.59 ? 199 TRP   A CG  1 
ATOM   1518 C CD1 . TRP   A 1 200 ? 15.536  -4.467  -1.324  1.00 12.07 ? 199 TRP   A CD1 1 
ATOM   1519 C CD2 . TRP   A 1 200 ? 15.798  -6.004  -2.935  1.00 11.27 ? 199 TRP   A CD2 1 
ATOM   1520 N NE1 . TRP   A 1 200 ? 15.681  -3.804  -2.517  1.00 13.14 ? 199 TRP   A NE1 1 
ATOM   1521 C CE2 . TRP   A 1 200 ? 15.800  -4.723  -3.529  1.00 12.09 ? 199 TRP   A CE2 1 
ATOM   1522 C CE3 . TRP   A 1 200 ? 15.883  -7.126  -3.759  1.00 11.80 ? 199 TRP   A CE3 1 
ATOM   1523 C CZ2 . TRP   A 1 200 ? 15.950  -4.536  -4.904  1.00 12.30 ? 199 TRP   A CZ2 1 
ATOM   1524 C CZ3 . TRP   A 1 200 ? 16.019  -6.937  -5.126  1.00 12.95 ? 199 TRP   A CZ3 1 
ATOM   1525 C CH2 . TRP   A 1 200 ? 16.059  -5.649  -5.680  1.00 12.69 ? 199 TRP   A CH2 1 
ATOM   1526 N N   . SER   A 1 201 ? 16.514  -5.153  1.997   1.00 12.32 ? 200 SER   A N   1 
ATOM   1527 C CA  . SER   A 1 201 ? 16.803  -3.849  2.623   1.00 11.34 ? 200 SER   A CA  1 
ATOM   1528 C C   . SER   A 1 201 ? 18.218  -3.814  3.168   1.00 11.53 ? 200 SER   A C   1 
ATOM   1529 O O   . SER   A 1 201 ? 18.866  -2.761  3.086   1.00 11.90 ? 200 SER   A O   1 
ATOM   1530 C CB  . SER   A 1 201 ? 15.821  -3.555  3.758   1.00 12.07 ? 200 SER   A CB  1 
ATOM   1531 O OG  . SER   A 1 201 ? 14.485  -3.474  3.254   1.00 13.78 ? 200 SER   A OG  1 
ATOM   1532 N N   . LEU   A 1 202 ? 18.719  -4.970  3.673   1.00 10.63 ? 201 LEU   A N   1 
ATOM   1533 C CA  . LEU   A 1 202 ? 20.105  -4.993  4.160   1.00 11.93 ? 201 LEU   A CA  1 
ATOM   1534 C C   . LEU   A 1 202 ? 21.122  -4.869  3.023   1.00 12.04 ? 201 LEU   A C   1 
ATOM   1535 O O   . LEU   A 1 202 ? 22.094  -4.126  3.179   1.00 12.61 ? 201 LEU   A O   1 
ATOM   1536 C CB  . LEU   A 1 202 ? 20.400  -6.193  5.032   1.00 13.44 ? 201 LEU   A CB  1 
ATOM   1537 C CG  . LEU   A 1 202 ? 21.840  -6.235  5.573   1.00 16.49 ? 201 LEU   A CG  1 
ATOM   1538 C CD1 . LEU   A 1 202 ? 22.127  -5.045  6.487   1.00 17.74 ? 201 LEU   A CD1 1 
ATOM   1539 C CD2 . LEU   A 1 202 ? 22.129  -7.531  6.219   1.00 18.04 ? 201 LEU   A CD2 1 
ATOM   1540 N N   . GLY   A 1 203 ? 20.844  -5.491  1.889   1.00 11.48 ? 202 GLY   A N   1 
ATOM   1541 C CA  . GLY   A 1 203 ? 21.678  -5.345  0.692   1.00 11.63 ? 202 GLY   A CA  1 
ATOM   1542 C C   . GLY   A 1 203 ? 21.747  -3.893  0.239   1.00 12.39 ? 202 GLY   A C   1 
ATOM   1543 O O   . GLY   A 1 203 ? 22.820  -3.358  -0.011  1.00 12.25 ? 202 GLY   A O   1 
ATOM   1544 N N   . ILE   A 1 204 ? 20.579  -3.208  0.205   1.00 10.84 ? 203 ILE   A N   1 
ATOM   1545 C CA  . ILE   A 1 204 ? 20.579  -1.782  -0.164  1.00 10.67 ? 203 ILE   A CA  1 
ATOM   1546 C C   . ILE   A 1 204 ? 21.373  -0.971  0.866   1.00 11.53 ? 203 ILE   A C   1 
ATOM   1547 O O   . ILE   A 1 204 ? 22.064  -0.040  0.498   1.00 12.77 ? 203 ILE   A O   1 
ATOM   1548 C CB  . ILE   A 1 204 ? 19.128  -1.246  -0.275  1.00 10.40 ? 203 ILE   A CB  1 
ATOM   1549 C CG1 . ILE   A 1 204 ? 18.322  -1.939  -1.371  1.00 10.85 ? 203 ILE   A CG1 1 
ATOM   1550 C CG2 . ILE   A 1 204 ? 19.121  0.286   -0.469  1.00 11.00 ? 203 ILE   A CG2 1 
ATOM   1551 C CD1 . ILE   A 1 204 ? 18.849  -1.788  -2.840  1.00 12.35 ? 203 ILE   A CD1 1 
ATOM   1552 N N   . THR   A 1 205 ? 21.198  -1.270  2.182   1.00 11.48 ? 204 THR   A N   1 
ATOM   1553 C CA  . THR   A 1 205 ? 21.928  -0.561  3.244   1.00 11.75 ? 204 THR   A CA  1 
ATOM   1554 C C   . THR   A 1 205 ? 23.438  -0.748  3.060   1.00 12.58 ? 204 THR   A C   1 
ATOM   1555 O O   . THR   A 1 205 ? 24.183  0.211   3.234   1.00 12.59 ? 204 THR   A O   1 
ATOM   1556 C CB  . THR   A 1 205 ? 21.433  -1.082  4.618   1.00 12.29 ? 204 THR   A CB  1 
ATOM   1557 O OG1 . THR   A 1 205 ? 20.045  -0.758  4.728   1.00 13.32 ? 204 THR   A OG1 1 
ATOM   1558 C CG2 . THR   A 1 205 ? 22.143  -0.406  5.791   1.00 12.17 ? 204 THR   A CG2 1 
ATOM   1559 N N   . ALA   A 1 206 ? 23.885  -1.950  2.629   1.00 12.26 ? 205 ALA   A N   1 
ATOM   1560 C CA  . ALA   A 1 206 ? 25.331  -2.137  2.392   1.00 12.85 ? 205 ALA   A CA  1 
ATOM   1561 C C   . ALA   A 1 206 ? 25.849  -1.201  1.258   1.00 13.77 ? 205 ALA   A C   1 
ATOM   1562 O O   . ALA   A 1 206 ? 26.924  -0.604  1.399   1.00 14.77 ? 205 ALA   A O   1 
ATOM   1563 C CB  . ALA   A 1 206 ? 25.592  -3.600  2.047   1.00 13.09 ? 205 ALA   A CB  1 
ATOM   1564 N N   . ILE   A 1 207 ? 25.026  -0.996  0.197   1.00 14.04 ? 206 ILE   A N   1 
ATOM   1565 C CA  . ILE   A 1 207 ? 25.360  -0.078  -0.905  1.00 14.13 ? 206 ILE   A CA  1 
ATOM   1566 C C   . ILE   A 1 207 ? 25.358  1.362   -0.361  1.00 12.84 ? 206 ILE   A C   1 
ATOM   1567 O O   . ILE   A 1 207 ? 26.293  2.136   -0.595  1.00 13.66 ? 206 ILE   A O   1 
ATOM   1568 C CB  . ILE   A 1 207 ? 24.417  -0.220  -2.122  1.00 14.21 ? 206 ILE   A CB  1 
ATOM   1569 C CG1 . ILE   A 1 207 ? 24.532  -1.642  -2.743  1.00 14.95 ? 206 ILE   A CG1 1 
ATOM   1570 C CG2 . ILE   A 1 207 ? 24.759  0.897   -3.170  1.00 15.54 ? 206 ILE   A CG2 1 
ATOM   1571 C CD1 . ILE   A 1 207 ? 23.562  -1.913  -3.901  1.00 16.08 ? 206 ILE   A CD1 1 
ATOM   1572 N N   . GLU   A 1 208 ? 24.350  1.705   0.451   1.00 12.30 ? 207 GLU   A N   1 
ATOM   1573 C CA  . GLU   A 1 208 ? 24.262  3.018   1.115   1.00 12.36 ? 207 GLU   A CA  1 
ATOM   1574 C C   . GLU   A 1 208 ? 25.525  3.314   1.942   1.00 12.77 ? 207 GLU   A C   1 
ATOM   1575 O O   . GLU   A 1 208 ? 26.078  4.415   1.842   1.00 13.81 ? 207 GLU   A O   1 
ATOM   1576 C CB  . GLU   A 1 208 ? 23.023  3.037   2.027   1.00 14.71 ? 207 GLU   A CB  1 
ATOM   1577 C CG  . GLU   A 1 208 ? 22.869  4.275   2.873   1.00 14.47 ? 207 GLU   A CG  1 
ATOM   1578 C CD  . GLU   A 1 208 ? 22.003  4.077   4.099   1.00 15.30 ? 207 GLU   A CD  1 
ATOM   1579 O OE1 . GLU   A 1 208 ? 21.307  3.037   4.209   1.00 13.49 ? 207 GLU   A OE1 1 
ATOM   1580 O OE2 . GLU   A 1 208 ? 21.969  5.004   4.934   1.00 16.29 ? 207 GLU   A OE2 1 
ATOM   1581 N N   . LEU   A 1 209 ? 26.015  2.347   2.722   1.00 12.75 ? 208 LEU   A N   1 
ATOM   1582 C CA  . LEU   A 1 209 ? 27.216  2.559   3.542   1.00 14.06 ? 208 LEU   A CA  1 
ATOM   1583 C C   . LEU   A 1 209 ? 28.456  2.736   2.668   1.00 15.18 ? 208 LEU   A C   1 
ATOM   1584 O O   . LEU   A 1 209 ? 29.371  3.464   3.033   1.00 14.93 ? 208 LEU   A O   1 
ATOM   1585 C CB  . LEU   A 1 209 ? 27.396  1.377   4.498   1.00 14.45 ? 208 LEU   A CB  1 
ATOM   1586 C CG  . LEU   A 1 209 ? 26.284  1.207   5.544   1.00 15.21 ? 208 LEU   A CG  1 
ATOM   1587 C CD1 . LEU   A 1 209 ? 26.511  -0.086  6.349   1.00 15.55 ? 208 LEU   A CD1 1 
ATOM   1588 C CD2 . LEU   A 1 209 ? 26.119  2.452   6.416   1.00 15.65 ? 208 LEU   A CD2 1 
ATOM   1589 N N   . ALA   A 1 210 ? 28.475  2.086   1.513   1.00 15.81 ? 209 ALA   A N   1 
ATOM   1590 C CA  . ALA   A 1 210 ? 29.577  2.167   0.560   1.00 16.07 ? 209 ALA   A CA  1 
ATOM   1591 C C   . ALA   A 1 210 ? 29.559  3.438   -0.286  1.00 16.12 ? 209 ALA   A C   1 
ATOM   1592 O O   . ALA   A 1 210 ? 30.607  3.872   -0.777  1.00 17.48 ? 209 ALA   A O   1 
ATOM   1593 C CB  . ALA   A 1 210 ? 29.488  0.978   -0.376  1.00 16.00 ? 209 ALA   A CB  1 
ATOM   1594 N N   . GLU   A 1 211 ? 28.352  3.962   -0.582  1.00 15.12 ? 210 GLU   A N   1 
ATOM   1595 C CA  . GLU   A 1 211 ? 28.189  5.036   -1.556  1.00 15.41 ? 210 GLU   A CA  1 
ATOM   1596 C C   . GLU   A 1 211 ? 27.525  6.307   -1.050  1.00 15.20 ? 210 GLU   A C   1 
ATOM   1597 O O   . GLU   A 1 211 ? 27.409  7.255   -1.819  1.00 15.74 ? 210 GLU   A O   1 
ATOM   1598 C CB  . GLU   A 1 211 ? 27.417  4.494   -2.775  1.00 16.71 ? 210 GLU   A CB  1 
ATOM   1599 C CG  . GLU   A 1 211 ? 28.152  3.336   -3.436  1.00 17.91 ? 210 GLU   A CG  1 
ATOM   1600 C CD  . GLU   A 1 211 ? 27.511  2.705   -4.654  1.00 19.38 ? 210 GLU   A CD  1 
ATOM   1601 O OE1 . GLU   A 1 211 ? 26.430  3.168   -5.085  1.00 18.49 ? 210 GLU   A OE1 1 
ATOM   1602 O OE2 . GLU   A 1 211 ? 28.102  1.737   -5.184  1.00 20.83 ? 210 GLU   A OE2 1 
ATOM   1603 N N   . LEU   A 1 212 ? 27.144  6.356   0.243   1.00 14.22 ? 211 LEU   A N   1 
ATOM   1604 C CA  . LEU   A 1 212 ? 26.548  7.527   0.912   1.00 15.50 ? 211 LEU   A CA  1 
ATOM   1605 C C   . LEU   A 1 212 ? 25.099  7.804   0.548   1.00 15.76 ? 211 LEU   A C   1 
ATOM   1606 O O   . LEU   A 1 212 ? 24.520  8.780   1.040   1.00 16.35 ? 211 LEU   A O   1 
ATOM   1607 C CB  . LEU   A 1 212 ? 27.392  8.799   0.734   1.00 15.40 ? 211 LEU   A CB  1 
ATOM   1608 C CG  . LEU   A 1 212 ? 28.883  8.614   1.057   1.00 16.17 ? 211 LEU   A CG  1 
ATOM   1609 C CD1 . LEU   A 1 212 ? 29.652  9.932   0.897   1.00 15.80 ? 211 LEU   A CD1 1 
ATOM   1610 C CD2 . LEU   A 1 212 ? 29.071  8.078   2.476   1.00 17.96 ? 211 LEU   A CD2 1 
ATOM   1611 N N   . GLN   A 1 213 ? 24.498  6.955   -0.265  1.00 15.37 ? 212 GLN   A N   1 
ATOM   1612 C CA  . GLN   A 1 213 ? 23.084  7.019   -0.624  1.00 14.64 ? 212 GLN   A CA  1 
ATOM   1613 C C   . GLN   A 1 213 ? 22.696  5.673   -1.211  1.00 15.07 ? 212 GLN   A C   1 
ATOM   1614 O O   . GLN   A 1 213 ? 23.547  4.949   -1.757  1.00 14.17 ? 212 GLN   A O   1 
ATOM   1615 C CB  . GLN   A 1 213 ? 22.786  8.157   -1.614  1.00 15.69 ? 212 GLN   A CB  1 
ATOM   1616 C CG  . GLN   A 1 213 ? 23.328  7.974   -3.019  1.00 19.04 ? 212 GLN   A CG  1 
ATOM   1617 C CD  . GLN   A 1 213 ? 22.975  9.156   -3.892  1.00 23.36 ? 212 GLN   A CD  1 
ATOM   1618 O OE1 . GLN   A 1 213 ? 22.800  10.290  -3.426  1.00 24.89 ? 212 GLN   A OE1 1 
ATOM   1619 N NE2 . GLN   A 1 213 ? 22.864  8.916   -5.176  1.00 24.55 ? 212 GLN   A NE2 1 
ATOM   1620 N N   . PRO   A 1 214 ? 21.412  5.291   -1.076  1.00 14.00 ? 213 PRO   A N   1 
ATOM   1621 C CA  . PRO   A 1 214 ? 20.985  4.021   -1.700  1.00 14.28 ? 213 PRO   A CA  1 
ATOM   1622 C C   . PRO   A 1 214 ? 20.865  4.231   -3.219  1.00 15.40 ? 213 PRO   A C   1 
ATOM   1623 O O   . PRO   A 1 214 ? 20.795  5.387   -3.715  1.00 14.23 ? 213 PRO   A O   1 
ATOM   1624 C CB  . PRO   A 1 214 ? 19.623  3.768   -1.063  1.00 14.42 ? 213 PRO   A CB  1 
ATOM   1625 C CG  . PRO   A 1 214 ? 19.056  5.179   -0.845  1.00 14.33 ? 213 PRO   A CG  1 
ATOM   1626 C CD  . PRO   A 1 214 ? 20.290  6.000   -0.429  1.00 13.24 ? 213 PRO   A CD  1 
ATOM   1627 N N   . PRO   A 1 215 ? 20.806  3.137   -4.004  1.00 15.17 ? 214 PRO   A N   1 
ATOM   1628 C CA  . PRO   A 1 215 ? 20.606  3.296   -5.456  1.00 15.61 ? 214 PRO   A CA  1 
ATOM   1629 C C   . PRO   A 1 215 ? 19.306  4.072   -5.781  1.00 16.97 ? 214 PRO   A C   1 
ATOM   1630 O O   . PRO   A 1 215 ? 18.354  4.034   -5.006  1.00 16.58 ? 214 PRO   A O   1 
ATOM   1631 C CB  . PRO   A 1 215 ? 20.487  1.848   -5.942  1.00 16.83 ? 214 PRO   A CB  1 
ATOM   1632 C CG  . PRO   A 1 215 ? 21.304  1.047   -4.917  1.00 16.74 ? 214 PRO   A CG  1 
ATOM   1633 C CD  . PRO   A 1 215 ? 20.910  1.706   -3.619  1.00 14.47 ? 214 PRO   A CD  1 
ATOM   1634 N N   . LEU   A 1 216 ? 19.286  4.807   -6.892  1.00 17.90 ? 215 LEU   A N   1 
ATOM   1635 C CA  . LEU   A 1 216 ? 18.101  5.588   -7.323  1.00 18.48 ? 215 LEU   A CA  1 
ATOM   1636 C C   . LEU   A 1 216 ? 17.676  6.695   -6.318  1.00 17.13 ? 215 LEU   A C   1 
ATOM   1637 O O   . LEU   A 1 216 ? 16.598  7.227   -6.475  1.00 16.30 ? 215 LEU   A O   1 
ATOM   1638 C CB  . LEU   A 1 216 ? 16.879  4.703   -7.695  1.00 20.47 ? 215 LEU   A CB  1 
ATOM   1639 C CG  . LEU   A 1 216 ? 17.086  3.526   -8.674  1.00 24.24 ? 215 LEU   A CG  1 
ATOM   1640 C CD1 . LEU   A 1 216 ? 15.760  2.802   -8.966  1.00 25.29 ? 215 LEU   A CD1 1 
ATOM   1641 C CD2 . LEU   A 1 216 ? 17.737  3.995   -9.954  1.00 25.84 ? 215 LEU   A CD2 1 
ATOM   1642 N N   . PHE   A 1 217 ? 18.530  7.096   -5.359  1.00 16.22 ? 216 PHE   A N   1 
ATOM   1643 C CA  . PHE   A 1 217 ? 18.161  8.133   -4.369  1.00 16.42 ? 216 PHE   A CA  1 
ATOM   1644 C C   . PHE   A 1 217 ? 17.727  9.443   -4.993  1.00 16.89 ? 216 PHE   A C   1 
ATOM   1645 O O   . PHE   A 1 217 ? 16.859  10.121  -4.449  1.00 17.40 ? 216 PHE   A O   1 
ATOM   1646 C CB  . PHE   A 1 217 ? 19.276  8.373   -3.334  1.00 15.93 ? 216 PHE   A CB  1 
ATOM   1647 C CG  . PHE   A 1 217 ? 18.816  9.082   -2.081  1.00 17.16 ? 216 PHE   A CG  1 
ATOM   1648 C CD1 . PHE   A 1 217 ? 17.797  8.560   -1.306  1.00 18.41 ? 216 PHE   A CD1 1 
ATOM   1649 C CD2 . PHE   A 1 217 ? 19.423  10.266  -1.668  1.00 18.19 ? 216 PHE   A CD2 1 
ATOM   1650 C CE1 . PHE   A 1 217 ? 17.405  9.183   -0.123  1.00 19.92 ? 216 PHE   A CE1 1 
ATOM   1651 C CE2 . PHE   A 1 217 ? 19.002  10.909  -0.507  1.00 19.73 ? 216 PHE   A CE2 1 
ATOM   1652 C CZ  . PHE   A 1 217 ? 17.989  10.370  0.251   1.00 19.95 ? 216 PHE   A CZ  1 
ATOM   1653 N N   . ASP   A 1 218 ? 18.285  9.761   -6.159  1.00 17.45 ? 217 ASP   A N   1 
ATOM   1654 C CA  . ASP   A 1 218 ? 18.012  10.976  -6.934  1.00 18.50 ? 217 ASP   A CA  1 
ATOM   1655 C C   . ASP   A 1 218 ? 16.746  10.951  -7.741  1.00 17.47 ? 217 ASP   A C   1 
ATOM   1656 O O   . ASP   A 1 218 ? 16.480  11.915  -8.466  1.00 16.54 ? 217 ASP   A O   1 
ATOM   1657 C CB  . ASP   A 1 218 ? 19.125  11.158  -7.975  1.00 22.68 ? 217 ASP   A CB  1 
ATOM   1658 C CG  . ASP   A 1 218 ? 20.425  11.641  -7.423  1.00 30.89 ? 217 ASP   A CG  1 
ATOM   1659 O OD1 . ASP   A 1 218 ? 20.468  12.007  -6.215  1.00 33.72 ? 217 ASP   A OD1 1 
ATOM   1660 O OD2 . ASP   A 1 218 ? 21.400  11.681  -8.186  1.00 32.63 ? 217 ASP   A OD2 1 
ATOM   1661 N N   . VAL   A 1 219 ? 16.056  9.803   -7.753  1.00 16.87 ? 218 VAL   A N   1 
ATOM   1662 C CA  . VAL   A 1 219 ? 14.840  9.625   -8.514  1.00 17.36 ? 218 VAL   A CA  1 
ATOM   1663 C C   . VAL   A 1 219 ? 13.649  9.887   -7.622  1.00 16.62 ? 218 VAL   A C   1 
ATOM   1664 O O   . VAL   A 1 219 ? 13.655  9.498   -6.444  1.00 16.33 ? 218 VAL   A O   1 
ATOM   1665 C CB  . VAL   A 1 219 ? 14.827  8.198   -9.104  1.00 19.01 ? 218 VAL   A CB  1 
ATOM   1666 C CG1 . VAL   A 1 219 ? 13.543  7.936   -9.872  1.00 19.04 ? 218 VAL   A CG1 1 
ATOM   1667 C CG2 . VAL   A 1 219 ? 16.046  7.989   -10.002 1.00 20.68 ? 218 VAL   A CG2 1 
ATOM   1668 N N   . HIS   A 1 220 ? 12.589  10.482  -8.193  1.00 15.93 ? 219 HIS   A N   1 
ATOM   1669 C CA  . HIS   A 1 220 ? 11.356  10.774  -7.457  1.00 16.51 ? 219 HIS   A CA  1 
ATOM   1670 C C   . HIS   A 1 220 ? 10.786  9.459   -6.912  1.00 17.06 ? 219 HIS   A C   1 
ATOM   1671 O O   . HIS   A 1 220 ? 10.784  8.464   -7.634  1.00 17.49 ? 219 HIS   A O   1 
ATOM   1672 C CB  . HIS   A 1 220 ? 10.317  11.415  -8.376  1.00 16.93 ? 219 HIS   A CB  1 
ATOM   1673 C CG  . HIS   A 1 220 ? 9.126   11.948  -7.654  1.00 19.93 ? 219 HIS   A CG  1 
ATOM   1674 N ND1 . HIS   A 1 220 ? 8.096   11.112  -7.232  1.00 20.83 ? 219 HIS   A ND1 1 
ATOM   1675 C CD2 . HIS   A 1 220 ? 8.817   13.224  -7.328  1.00 20.71 ? 219 HIS   A CD2 1 
ATOM   1676 C CE1 . HIS   A 1 220 ? 7.210   11.904  -6.646  1.00 22.33 ? 219 HIS   A CE1 1 
ATOM   1677 N NE2 . HIS   A 1 220 ? 7.594   13.188  -6.689  1.00 22.19 ? 219 HIS   A NE2 1 
ATOM   1678 N N   . PRO   A 1 221 ? 10.374  9.437   -5.635  1.00 18.38 ? 220 PRO   A N   1 
ATOM   1679 C CA  . PRO   A 1 221 ? 9.852   8.190   -5.049  1.00 18.50 ? 220 PRO   A CA  1 
ATOM   1680 C C   . PRO   A 1 221 ? 8.752   7.477   -5.851  1.00 18.90 ? 220 PRO   A C   1 
ATOM   1681 O O   . PRO   A 1 221 ? 8.776   6.250   -5.907  1.00 19.78 ? 220 PRO   A O   1 
ATOM   1682 C CB  . PRO   A 1 221 ? 9.352   8.594   -3.654  1.00 20.17 ? 220 PRO   A CB  1 
ATOM   1683 C CG  . PRO   A 1 221 ? 9.672   10.013  -3.475  1.00 21.13 ? 220 PRO   A CG  1 
ATOM   1684 C CD  . PRO   A 1 221 ? 10.365  10.563  -4.678  1.00 19.19 ? 220 PRO   A CD  1 
ATOM   1685 N N   . LEU   A 1 222 ? 7.820   8.209   -6.486  1.00 18.63 ? 221 LEU   A N   1 
ATOM   1686 C CA  . LEU   A 1 222 ? 6.773   7.567   -7.293  1.00 19.72 ? 221 LEU   A CA  1 
ATOM   1687 C C   . LEU   A 1 222 ? 7.343   6.952   -8.578  1.00 20.78 ? 221 LEU   A C   1 
ATOM   1688 O O   . LEU   A 1 222 ? 6.850   5.915   -9.044  1.00 21.62 ? 221 LEU   A O   1 
ATOM   1689 C CB  . LEU   A 1 222 ? 5.626   8.541   -7.611  1.00 20.77 ? 221 LEU   A CB  1 
ATOM   1690 C CG  . LEU   A 1 222 ? 4.875   9.094   -6.393  1.00 25.02 ? 221 LEU   A CG  1 
ATOM   1691 C CD1 . LEU   A 1 222 ? 3.838   10.112  -6.812  1.00 26.02 ? 221 LEU   A CD1 1 
ATOM   1692 C CD2 . LEU   A 1 222 ? 4.238   7.973   -5.572  1.00 27.15 ? 221 LEU   A CD2 1 
ATOM   1693 N N   . ARG   A 1 223 ? 8.432   7.531   -9.114  1.00 18.90 ? 222 ARG   A N   1 
ATOM   1694 C CA  . ARG   A 1 223 ? 9.096   6.962   -10.276 1.00 19.40 ? 222 ARG   A CA  1 
ATOM   1695 C C   . ARG   A 1 223 ? 9.849   5.690   -9.860  1.00 19.30 ? 222 ARG   A C   1 
ATOM   1696 O O   . ARG   A 1 223 ? 9.824   4.706   -10.603 1.00 19.89 ? 222 ARG   A O   1 
ATOM   1697 C CB  . ARG   A 1 223 ? 10.060  7.969   -10.933 1.00 21.80 ? 222 ARG   A CB  1 
ATOM   1698 C CG  . ARG   A 1 223 ? 10.810  7.335   -12.122 1.00 24.58 ? 222 ARG   A CG  1 
ATOM   1699 C CD  . ARG   A 1 223 ? 11.189  8.284   -13.253 1.00 27.74 ? 222 ARG   A CD  1 
ATOM   1700 N NE  . ARG   A 1 223 ? 12.037  7.594   -14.236 1.00 31.24 ? 222 ARG   A NE  1 
ATOM   1701 C CZ  . ARG   A 1 223 ? 11.579  6.849   -15.238 1.00 33.52 ? 222 ARG   A CZ  1 
ATOM   1702 N NH1 . ARG   A 1 223 ? 10.273  6.699   -15.419 1.00 34.34 ? 222 ARG   A NH1 1 
ATOM   1703 N NH2 . ARG   A 1 223 ? 12.423  6.251   -16.070 1.00 32.98 ? 222 ARG   A NH2 1 
ATOM   1704 N N   . VAL   A 1 224 ? 10.457  5.655   -8.649  1.00 18.03 ? 223 VAL   A N   1 
ATOM   1705 C CA  . VAL   A 1 224 ? 11.122  4.425   -8.173  1.00 18.29 ? 223 VAL   A CA  1 
ATOM   1706 C C   . VAL   A 1 224 ? 10.055  3.315   -8.019  1.00 19.06 ? 223 VAL   A C   1 
ATOM   1707 O O   . VAL   A 1 224 ? 10.299  2.177   -8.419  1.00 20.08 ? 223 VAL   A O   1 
ATOM   1708 C CB  . VAL   A 1 224 ? 11.875  4.665   -6.849  1.00 18.34 ? 223 VAL   A CB  1 
ATOM   1709 C CG1 . VAL   A 1 224 ? 12.457  3.367   -6.279  1.00 18.88 ? 223 VAL   A CG1 1 
ATOM   1710 C CG2 . VAL   A 1 224 ? 12.974  5.695   -7.051  1.00 18.55 ? 223 VAL   A CG2 1 
ATOM   1711 N N   . LEU   A 1 225 ? 8.877   3.658   -7.492  1.00 19.32 ? 224 LEU   A N   1 
ATOM   1712 C CA  . LEU   A 1 225 ? 7.788   2.660   -7.358  1.00 19.90 ? 224 LEU   A CA  1 
ATOM   1713 C C   . LEU   A 1 225 ? 7.355   2.139   -8.719  1.00 21.57 ? 224 LEU   A C   1 
ATOM   1714 O O   . LEU   A 1 225 ? 7.136   0.923   -8.879  1.00 22.68 ? 224 LEU   A O   1 
ATOM   1715 C CB  . LEU   A 1 225 ? 6.588   3.236   -6.606  1.00 20.10 ? 224 LEU   A CB  1 
ATOM   1716 C CG  . LEU   A 1 225 ? 6.789   3.506   -5.104  1.00 20.88 ? 224 LEU   A CG  1 
ATOM   1717 C CD1 . LEU   A 1 225 ? 5.487   4.040   -4.482  1.00 21.50 ? 224 LEU   A CD1 1 
ATOM   1718 C CD2 . LEU   A 1 225 ? 7.261   2.247   -4.372  1.00 21.25 ? 224 LEU   A CD2 1 
ATOM   1719 N N   . PHE   A 1 226 ? 7.256   3.028   -9.711  1.00 21.09 ? 225 PHE   A N   1 
ATOM   1720 C CA  . PHE   A 1 226 ? 6.925   2.642   -11.083 1.00 22.23 ? 225 PHE   A CA  1 
ATOM   1721 C C   . PHE   A 1 226 ? 7.973   1.680   -11.642 1.00 22.37 ? 225 PHE   A C   1 
ATOM   1722 O O   . PHE   A 1 226 ? 7.609   0.638   -12.169 1.00 23.65 ? 225 PHE   A O   1 
ATOM   1723 C CB  . PHE   A 1 226 ? 6.805   3.880   -11.999 1.00 23.00 ? 225 PHE   A CB  1 
ATOM   1724 C CG  . PHE   A 1 226 ? 6.785   3.578   -13.481 1.00 24.96 ? 225 PHE   A CG  1 
ATOM   1725 C CD1 . PHE   A 1 226 ? 5.637   3.109   -14.093 1.00 26.64 ? 225 PHE   A CD1 1 
ATOM   1726 C CD2 . PHE   A 1 226 ? 7.907   3.786   -14.264 1.00 26.35 ? 225 PHE   A CD2 1 
ATOM   1727 C CE1 . PHE   A 1 226 ? 5.611   2.857   -15.458 1.00 28.21 ? 225 PHE   A CE1 1 
ATOM   1728 C CE2 . PHE   A 1 226 ? 7.886   3.512   -15.626 1.00 27.73 ? 225 PHE   A CE2 1 
ATOM   1729 C CZ  . PHE   A 1 226 ? 6.735   3.062   -16.217 1.00 27.91 ? 225 PHE   A CZ  1 
ATOM   1730 N N   . LEU   A 1 227 ? 9.270   2.018   -11.526 1.00 21.80 ? 226 LEU   A N   1 
ATOM   1731 C CA  . LEU   A 1 227 ? 10.340  1.190   -12.058 1.00 21.46 ? 226 LEU   A CA  1 
ATOM   1732 C C   . LEU   A 1 227 ? 10.430  -0.198  -11.406 1.00 22.51 ? 226 LEU   A C   1 
ATOM   1733 O O   . LEU   A 1 227 ? 10.711  -1.188  -12.096 1.00 21.27 ? 226 LEU   A O   1 
ATOM   1734 C CB  . LEU   A 1 227 ? 11.672  1.925   -11.876 1.00 21.13 ? 226 LEU   A CB  1 
ATOM   1735 C CG  . LEU   A 1 227 ? 11.820  3.208   -12.703 1.00 22.09 ? 226 LEU   A CG  1 
ATOM   1736 C CD1 . LEU   A 1 227 ? 13.046  4.014   -12.241 1.00 22.41 ? 226 LEU   A CD1 1 
ATOM   1737 C CD2 . LEU   A 1 227 ? 11.934  2.881   -14.180 1.00 22.40 ? 226 LEU   A CD2 1 
ATOM   1738 N N   . MET   A 1 228 ? 10.225  -0.271  -10.078 1.00 24.20 ? 227 MET   A N   1 
ATOM   1739 C CA  . MET   A 1 228 ? 10.378  -1.538  -9.355  1.00 26.93 ? 227 MET   A CA  1 
ATOM   1740 C C   . MET   A 1 228 ? 9.277   -2.553  -9.637  1.00 30.49 ? 227 MET   A C   1 
ATOM   1741 O O   . MET   A 1 228 ? 9.491   -3.747  -9.404  1.00 31.68 ? 227 MET   A O   1 
ATOM   1742 C CB  . MET   A 1 228 ? 10.536  -1.303  -7.843  1.00 27.59 ? 227 MET   A CB  1 
ATOM   1743 C CG  . MET   A 1 228 ? 11.785  -0.516  -7.489  1.00 30.95 ? 227 MET   A CG  1 
ATOM   1744 S SD  . MET   A 1 228 ? 11.989  -0.374  -5.691  1.00 37.30 ? 227 MET   A SD  1 
ATOM   1745 C CE  . MET   A 1 228 ? 12.702  -1.933  -5.370  1.00 23.12 ? 227 MET   A CE  1 
ATOM   1746 N N   . THR   A 1 229 ? 8.115   -2.108  -10.136 1.00 32.20 ? 228 THR   A N   1 
ATOM   1747 C CA  . THR   A 1 229 ? 7.047   -3.050  -10.475 1.00 34.83 ? 228 THR   A CA  1 
ATOM   1748 C C   . THR   A 1 229 ? 7.028   -3.403  -11.976 1.00 36.77 ? 228 THR   A C   1 
ATOM   1749 O O   . THR   A 1 229 ? 6.177   -4.186  -12.387 1.00 37.27 ? 228 THR   A O   1 
ATOM   1750 C CB  . THR   A 1 229 ? 5.691   -2.596  -9.948  1.00 37.46 ? 228 THR   A CB  1 
ATOM   1751 O OG1 . THR   A 1 229 ? 5.378   -1.280  -10.411 1.00 39.04 ? 228 THR   A OG1 1 
ATOM   1752 C CG2 . THR   A 1 229 ? 5.634   -2.649  -8.448  1.00 37.85 ? 228 THR   A CG2 1 
ATOM   1753 N N   . LYS   A 1 230 ? 7.967   -2.863  -12.782 1.00 37.58 ? 229 LYS   A N   1 
ATOM   1754 C CA  . LYS   A 1 230 ? 8.081   -3.208  -14.196 1.00 38.88 ? 229 LYS   A CA  1 
ATOM   1755 C C   . LYS   A 1 230 ? 8.704   -4.601  -14.262 1.00 40.49 ? 229 LYS   A C   1 
ATOM   1756 O O   . LYS   A 1 230 ? 9.535   -4.957  -13.421 1.00 40.84 ? 229 LYS   A O   1 
ATOM   1757 C CB  . LYS   A 1 230 ? 8.974   -2.204  -14.937 1.00 40.67 ? 229 LYS   A CB  1 
ATOM   1758 C CG  . LYS   A 1 230 ? 8.236   -1.229  -15.845 1.00 45.06 ? 229 LYS   A CG  1 
ATOM   1759 C CD  . LYS   A 1 230 ? 9.219   -0.256  -16.509 1.00 50.01 ? 229 LYS   A CD  1 
ATOM   1760 C CE  . LYS   A 1 230 ? 8.686   0.408   -17.761 1.00 54.11 ? 229 LYS   A CE  1 
ATOM   1761 N NZ  . LYS   A 1 230 ? 8.881   -0.431  -18.977 1.00 56.43 ? 229 LYS   A NZ  1 
ATOM   1762 N N   . SER   A 1 231 ? 8.269   -5.405  -15.235 1.00 41.05 ? 230 SER   A N   1 
ATOM   1763 C CA  . SER   A 1 231 ? 8.711   -6.785  -15.404 1.00 41.65 ? 230 SER   A CA  1 
ATOM   1764 C C   . SER   A 1 231 ? 10.214  -6.958  -15.553 1.00 41.23 ? 230 SER   A C   1 
ATOM   1765 O O   . SER   A 1 231 ? 10.774  -7.875  -14.957 1.00 42.42 ? 230 SER   A O   1 
ATOM   1766 C CB  . SER   A 1 231 ? 7.994   -7.434  -16.586 1.00 44.08 ? 230 SER   A CB  1 
ATOM   1767 O OG  . SER   A 1 231 ? 6.594   -7.218  -16.511 1.00 47.69 ? 230 SER   A OG  1 
ATOM   1768 N N   . GLY   A 1 232 ? 10.853  -6.093  -16.335 1.00 39.24 ? 231 GLY   A N   1 
ATOM   1769 C CA  . GLY   A 1 232 ? 12.285  -6.186  -16.587 1.00 37.67 ? 231 GLY   A CA  1 
ATOM   1770 C C   . GLY   A 1 232 ? 13.180  -5.467  -15.596 1.00 35.51 ? 231 GLY   A C   1 
ATOM   1771 O O   . GLY   A 1 232 ? 14.364  -5.271  -15.866 1.00 35.86 ? 231 GLY   A O   1 
ATOM   1772 N N   . TYR   A 1 233 ? 12.638  -5.075  -14.433 1.00 33.34 ? 232 TYR   A N   1 
ATOM   1773 C CA  . TYR   A 1 233 ? 13.415  -4.390  -13.392 1.00 31.57 ? 232 TYR   A CA  1 
ATOM   1774 C C   . TYR   A 1 233 ? 14.616  -5.235  -12.964 1.00 30.56 ? 232 TYR   A C   1 
ATOM   1775 O O   . TYR   A 1 233 ? 14.453  -6.414  -12.648 1.00 30.65 ? 232 TYR   A O   1 
ATOM   1776 C CB  . TYR   A 1 233 ? 12.517  -4.089  -12.170 1.00 31.06 ? 232 TYR   A CB  1 
ATOM   1777 C CG  . TYR   A 1 233 ? 13.288  -3.684  -10.937 1.00 31.32 ? 232 TYR   A CG  1 
ATOM   1778 C CD1 . TYR   A 1 233 ? 13.867  -2.431  -10.839 1.00 31.71 ? 232 TYR   A CD1 1 
ATOM   1779 C CD2 . TYR   A 1 233 ? 13.517  -4.589  -9.909  1.00 32.06 ? 232 TYR   A CD2 1 
ATOM   1780 C CE1 . TYR   A 1 233 ? 14.633  -2.075  -9.738  1.00 32.38 ? 232 TYR   A CE1 1 
ATOM   1781 C CE2 . TYR   A 1 233 ? 14.275  -4.243  -8.801  1.00 32.28 ? 232 TYR   A CE2 1 
ATOM   1782 C CZ  . TYR   A 1 233 ? 14.833  -2.985  -8.720  1.00 32.44 ? 232 TYR   A CZ  1 
ATOM   1783 O OH  . TYR   A 1 233 ? 15.547  -2.625  -7.610  1.00 32.66 ? 232 TYR   A OH  1 
ATOM   1784 N N   . GLN   A 1 234 ? 15.806  -4.636  -12.956 1.00 29.00 ? 233 GLN   A N   1 
ATOM   1785 C CA  . GLN   A 1 234 ? 17.004  -5.357  -12.542 1.00 28.02 ? 233 GLN   A CA  1 
ATOM   1786 C C   . GLN   A 1 234 ? 17.476  -4.849  -11.184 1.00 26.01 ? 233 GLN   A C   1 
ATOM   1787 O O   . GLN   A 1 234 ? 17.581  -3.642  -10.963 1.00 25.72 ? 233 GLN   A O   1 
ATOM   1788 C CB  . GLN   A 1 234 ? 18.121  -5.183  -13.581 1.00 30.13 ? 233 GLN   A CB  1 
ATOM   1789 C CG  . GLN   A 1 234 ? 17.762  -5.695  -14.976 1.00 34.54 ? 233 GLN   A CG  1 
ATOM   1790 C CD  . GLN   A 1 234 ? 17.557  -7.186  -15.015 1.00 39.88 ? 233 GLN   A CD  1 
ATOM   1791 O OE1 . GLN   A 1 234 ? 16.510  -7.687  -15.440 1.00 42.34 ? 233 GLN   A OE1 1 
ATOM   1792 N NE2 . GLN   A 1 234 ? 18.554  -7.932  -14.579 1.00 40.39 ? 233 GLN   A NE2 1 
ATOM   1793 N N   . PRO   A 1 235 ? 17.849  -5.759  -10.280 1.00 24.16 ? 234 PRO   A N   1 
ATOM   1794 C CA  . PRO   A 1 235 ? 18.392  -5.328  -8.986  1.00 22.83 ? 234 PRO   A CA  1 
ATOM   1795 C C   . PRO   A 1 235 ? 19.629  -4.439  -9.132  1.00 21.49 ? 234 PRO   A C   1 
ATOM   1796 O O   . PRO   A 1 235 ? 20.439  -4.615  -10.060 1.00 21.64 ? 234 PRO   A O   1 
ATOM   1797 C CB  . PRO   A 1 235 ? 18.772  -6.653  -8.325  1.00 23.97 ? 234 PRO   A CB  1 
ATOM   1798 C CG  . PRO   A 1 235 ? 17.803  -7.654  -8.942  1.00 24.77 ? 234 PRO   A CG  1 
ATOM   1799 C CD  . PRO   A 1 235 ? 17.812  -7.233  -10.386 1.00 23.62 ? 234 PRO   A CD  1 
ATOM   1800 N N   . PRO   A 1 236 ? 19.807  -3.491  -8.209  1.00 19.57 ? 235 PRO   A N   1 
ATOM   1801 C CA  . PRO   A 1 236 ? 20.988  -2.617  -8.301  1.00 19.41 ? 235 PRO   A CA  1 
ATOM   1802 C C   . PRO   A 1 236 ? 22.300  -3.313  -7.922  1.00 19.11 ? 235 PRO   A C   1 
ATOM   1803 O O   . PRO   A 1 236 ? 22.318  -4.462  -7.463  1.00 19.17 ? 235 PRO   A O   1 
ATOM   1804 C CB  . PRO   A 1 236 ? 20.627  -1.451  -7.392  1.00 20.56 ? 235 PRO   A CB  1 
ATOM   1805 C CG  . PRO   A 1 236 ? 19.697  -2.018  -6.375  1.00 20.99 ? 235 PRO   A CG  1 
ATOM   1806 C CD  . PRO   A 1 236 ? 18.953  -3.145  -7.055  1.00 18.93 ? 235 PRO   A CD  1 
ATOM   1807 N N   . ARG   A 1 237 ? 23.410  -2.653  -8.224  1.00 18.06 ? 236 ARG   A N   1 
ATOM   1808 C CA  . ARG   A 1 237 ? 24.742  -3.188  -7.928  1.00 18.20 ? 236 ARG   A CA  1 
ATOM   1809 C C   . ARG   A 1 237 ? 25.630  -2.057  -7.418  1.00 17.44 ? 236 ARG   A C   1 
ATOM   1810 O O   . ARG   A 1 237 ? 25.299  -0.878  -7.571  1.00 18.11 ? 236 ARG   A O   1 
ATOM   1811 C CB  . ARG   A 1 237 ? 25.400  -3.746  -9.224  1.00 20.88 ? 236 ARG   A CB  1 
ATOM   1812 C CG  . ARG   A 1 237 ? 24.577  -4.738  -10.026 1.00 27.35 ? 236 ARG   A CG  1 
ATOM   1813 C CD  . ARG   A 1 237 ? 25.133  -4.864  -11.439 1.00 33.17 ? 236 ARG   A CD  1 
ATOM   1814 N NE  . ARG   A 1 237 ? 24.573  -6.018  -12.142 1.00 40.28 ? 236 ARG   A NE  1 
ATOM   1815 C CZ  . ARG   A 1 237 ? 24.893  -6.367  -13.386 1.00 45.29 ? 236 ARG   A CZ  1 
ATOM   1816 N NH1 . ARG   A 1 237 ? 24.336  -7.433  -13.946 1.00 46.27 ? 236 ARG   A NH1 1 
ATOM   1817 N NH2 . ARG   A 1 237 ? 25.778  -5.657  -14.077 1.00 45.36 ? 236 ARG   A NH2 1 
ATOM   1818 N N   . LEU   A 1 238 ? 26.789  -2.410  -6.846  1.00 15.85 ? 237 LEU   A N   1 
ATOM   1819 C CA  . LEU   A 1 238 ? 27.780  -1.379  -6.466  1.00 16.01 ? 237 LEU   A CA  1 
ATOM   1820 C C   . LEU   A 1 238 ? 28.287  -0.667  -7.754  1.00 19.16 ? 237 LEU   A C   1 
ATOM   1821 O O   . LEU   A 1 238 ? 28.499  -1.316  -8.779  1.00 20.47 ? 237 LEU   A O   1 
ATOM   1822 C CB  . LEU   A 1 238 ? 28.928  -2.020  -5.675  1.00 15.78 ? 237 LEU   A CB  1 
ATOM   1823 C CG  . LEU   A 1 238 ? 28.536  -2.535  -4.283  1.00 15.71 ? 237 LEU   A CG  1 
ATOM   1824 C CD1 . LEU   A 1 238 ? 29.490  -3.647  -3.807  1.00 15.70 ? 237 LEU   A CD1 1 
ATOM   1825 C CD2 . LEU   A 1 238 ? 28.466  -1.417  -3.281  1.00 16.78 ? 237 LEU   A CD2 1 
ATOM   1826 N N   . LYS   A 1 239 ? 28.475  0.660   -7.692  1.00 19.37 ? 238 LYS   A N   1 
ATOM   1827 C CA  . LYS   A 1 239 ? 28.905  1.487   -8.818  1.00 21.96 ? 238 LYS   A CA  1 
ATOM   1828 C C   . LYS   A 1 239 ? 30.353  1.222   -9.268  1.00 24.26 ? 238 LYS   A C   1 
ATOM   1829 O O   . LYS   A 1 239 ? 30.616  1.073   -10.469 1.00 25.81 ? 238 LYS   A O   1 
ATOM   1830 C CB  . LYS   A 1 239 ? 28.702  2.977   -8.433  1.00 25.76 ? 238 LYS   A CB  1 
ATOM   1831 C CG  . LYS   A 1 239 ? 29.334  3.991   -9.376  1.00 33.54 ? 238 LYS   A CG  1 
ATOM   1832 C CD  . LYS   A 1 239 ? 29.403  5.382   -8.749  1.00 40.63 ? 238 LYS   A CD  1 
ATOM   1833 C CE  . LYS   A 1 239 ? 30.055  6.379   -9.677  1.00 45.90 ? 238 LYS   A CE  1 
ATOM   1834 N NZ  . LYS   A 1 239 ? 29.892  7.776   -9.178  1.00 49.51 ? 238 LYS   A NZ  1 
ATOM   1835 N N   . GLU   A 1 240 ? 31.294  1.205   -8.325  1.00 24.49 ? 239 GLU   A N   1 
ATOM   1836 C CA  . GLU   A 1 240 ? 32.723  1.048   -8.686  1.00 25.40 ? 239 GLU   A CA  1 
ATOM   1837 C C   . GLU   A 1 240 ? 33.184  -0.365  -8.465  1.00 26.20 ? 239 GLU   A C   1 
ATOM   1838 O O   . GLU   A 1 240 ? 33.532  -0.719  -7.344  1.00 26.14 ? 239 GLU   A O   1 
ATOM   1839 C CB  . GLU   A 1 240 ? 33.575  1.984   -7.849  1.00 27.73 ? 239 GLU   A CB  1 
ATOM   1840 C CG  . GLU   A 1 240 ? 33.266  3.440   -8.091  1.00 32.32 ? 239 GLU   A CG  1 
ATOM   1841 C CD  . GLU   A 1 240 ? 34.290  4.311   -7.403  1.00 36.99 ? 239 GLU   A CD  1 
ATOM   1842 O OE1 . GLU   A 1 240 ? 33.918  5.016   -6.437  1.00 34.32 ? 239 GLU   A OE1 1 
ATOM   1843 O OE2 . GLU   A 1 240 ? 35.478  4.250   -7.802  1.00 41.93 ? 239 GLU   A OE2 1 
ATOM   1844 N N   . LYS   A 1 241 ? 33.178  -1.180  -9.529  1.00 26.58 ? 240 LYS   A N   1 
ATOM   1845 C CA  . LYS   A 1 241 ? 33.515  -2.599  -9.463  1.00 26.77 ? 240 LYS   A CA  1 
ATOM   1846 C C   . LYS   A 1 241 ? 34.865  -2.887  -8.822  1.00 25.94 ? 240 LYS   A C   1 
ATOM   1847 O O   . LYS   A 1 241 ? 34.970  -3.747  -7.950  1.00 26.10 ? 240 LYS   A O   1 
ATOM   1848 C CB  . LYS   A 1 241 ? 33.419  -3.242  -10.860 1.00 29.86 ? 240 LYS   A CB  1 
ATOM   1849 C CG  . LYS   A 1 241 ? 33.562  -4.766  -10.844 1.00 35.33 ? 240 LYS   A CG  1 
ATOM   1850 C CD  . LYS   A 1 241 ? 33.253  -5.375  -12.201 1.00 40.54 ? 240 LYS   A CD  1 
ATOM   1851 C CE  . LYS   A 1 241 ? 33.977  -6.685  -12.420 1.00 45.12 ? 240 LYS   A CE  1 
ATOM   1852 N NZ  . LYS   A 1 241 ? 33.053  -7.844  -12.356 1.00 47.81 ? 240 LYS   A NZ  1 
ATOM   1853 N N   . GLY   A 1 242 ? 35.886  -2.141  -9.229  1.00 24.82 ? 241 GLY   A N   1 
ATOM   1854 C CA  . GLY   A 1 242 ? 37.230  -2.341  -8.724  1.00 24.22 ? 241 GLY   A CA  1 
ATOM   1855 C C   . GLY   A 1 242 ? 37.473  -1.900  -7.298  1.00 23.23 ? 241 GLY   A C   1 
ATOM   1856 O O   . GLY   A 1 242 ? 38.550  -2.168  -6.754  1.00 23.16 ? 241 GLY   A O   1 
ATOM   1857 N N   . LYS   A 1 243 ? 36.512  -1.215  -6.685  1.00 21.78 ? 242 LYS   A N   1 
ATOM   1858 C CA  . LYS   A 1 243 ? 36.679  -0.762  -5.309  1.00 21.19 ? 242 LYS   A CA  1 
ATOM   1859 C C   . LYS   A 1 243 ? 36.351  -1.840  -4.283  1.00 21.40 ? 242 LYS   A C   1 
ATOM   1860 O O   . LYS   A 1 243 ? 36.756  -1.716  -3.128  1.00 22.68 ? 242 LYS   A O   1 
ATOM   1861 C CB  . LYS   A 1 243 ? 35.842  0.507   -5.066  1.00 21.75 ? 242 LYS   A CB  1 
ATOM   1862 C CG  . LYS   A 1 243 ? 36.026  1.167   -3.706  1.00 23.57 ? 242 LYS   A CG  1 
ATOM   1863 C CD  . LYS   A 1 243 ? 35.378  2.563   -3.666  1.00 27.46 ? 242 LYS   A CD  1 
ATOM   1864 C CE  . LYS   A 1 243 ? 35.569  3.251   -2.327  1.00 29.49 ? 242 LYS   A CE  1 
ATOM   1865 N NZ  . LYS   A 1 243 ? 35.101  4.672   -2.350  1.00 31.04 ? 242 LYS   A NZ  1 
ATOM   1866 N N   . TRP   A 1 244 ? 35.614  -2.888  -4.692  1.00 19.61 ? 243 TRP   A N   1 
ATOM   1867 C CA  . TRP   A 1 244 ? 35.105  -3.902  -3.783  1.00 19.45 ? 243 TRP   A CA  1 
ATOM   1868 C C   . TRP   A 1 244 ? 35.468  -5.313  -4.185  1.00 19.51 ? 243 TRP   A C   1 
ATOM   1869 O O   . TRP   A 1 244 ? 35.682  -5.601  -5.373  1.00 20.14 ? 243 TRP   A O   1 
ATOM   1870 C CB  . TRP   A 1 244 ? 33.570  -3.747  -3.670  1.00 19.08 ? 243 TRP   A CB  1 
ATOM   1871 C CG  . TRP   A 1 244 ? 33.131  -2.318  -3.497  1.00 18.91 ? 243 TRP   A CG  1 
ATOM   1872 C CD1 . TRP   A 1 244 ? 32.591  -1.510  -4.449  1.00 19.30 ? 243 TRP   A CD1 1 
ATOM   1873 C CD2 . TRP   A 1 244 ? 33.312  -1.499  -2.331  1.00 19.39 ? 243 TRP   A CD2 1 
ATOM   1874 N NE1 . TRP   A 1 244 ? 32.340  -0.261  -3.919  1.00 19.87 ? 243 TRP   A NE1 1 
ATOM   1875 C CE2 . TRP   A 1 244 ? 32.755  -0.236  -2.614  1.00 19.69 ? 243 TRP   A CE2 1 
ATOM   1876 C CE3 . TRP   A 1 244 ? 33.844  -1.728  -1.055  1.00 20.35 ? 243 TRP   A CE3 1 
ATOM   1877 C CZ2 . TRP   A 1 244 ? 32.738  0.800   -1.679  1.00 20.28 ? 243 TRP   A CZ2 1 
ATOM   1878 C CZ3 . TRP   A 1 244 ? 33.820  -0.704  -0.126  1.00 20.34 ? 243 TRP   A CZ3 1 
ATOM   1879 C CH2 . TRP   A 1 244 ? 33.272  0.542   -0.439  1.00 19.99 ? 243 TRP   A CH2 1 
ATOM   1880 N N   . SER   A 1 245 ? 35.553  -6.205  -3.196  1.00 18.74 ? 244 SER   A N   1 
ATOM   1881 C CA  . SER   A 1 245 ? 35.948  -7.590  -3.482  1.00 19.04 ? 244 SER   A CA  1 
ATOM   1882 C C   . SER   A 1 245 ? 34.834  -8.386  -4.140  1.00 19.99 ? 244 SER   A C   1 
ATOM   1883 O O   . SER   A 1 245 ? 33.648  -8.031  -4.017  1.00 19.39 ? 244 SER   A O   1 
ATOM   1884 C CB  . SER   A 1 245 ? 36.394  -8.314  -2.207  1.00 19.78 ? 244 SER   A CB  1 
ATOM   1885 O OG  . SER   A 1 245 ? 35.274  -8.692  -1.408  1.00 20.74 ? 244 SER   A OG  1 
ATOM   1886 N N   . ALA   A 1 246 ? 35.196  -9.533  -4.743  1.00 20.92 ? 245 ALA   A N   1 
ATOM   1887 C CA  . ALA   A 1 246 ? 34.200  -10.454 -5.324  1.00 21.62 ? 245 ALA   A CA  1 
ATOM   1888 C C   . ALA   A 1 246 ? 33.204  -10.906 -4.244  1.00 20.91 ? 245 ALA   A C   1 
ATOM   1889 O O   . ALA   A 1 246 ? 32.007  -10.972 -4.520  1.00 20.01 ? 245 ALA   A O   1 
ATOM   1890 C CB  . ALA   A 1 246 ? 34.896  -11.673 -5.928  1.00 23.19 ? 245 ALA   A CB  1 
ATOM   1891 N N   . ALA   A 1 247 ? 33.681  -11.116 -2.997  1.00 19.97 ? 246 ALA   A N   1 
ATOM   1892 C CA  . ALA   A 1 247 ? 32.784  -11.506 -1.893  1.00 19.32 ? 246 ALA   A CA  1 
ATOM   1893 C C   . ALA   A 1 247 ? 31.711  -10.430 -1.616  1.00 18.23 ? 246 ALA   A C   1 
ATOM   1894 O O   . ALA   A 1 247 ? 30.548  -10.767 -1.380  1.00 18.33 ? 246 ALA   A O   1 
ATOM   1895 C CB  . ALA   A 1 247 ? 33.593  -11.747 -0.632  1.00 19.99 ? 246 ALA   A CB  1 
ATOM   1896 N N   . PHE   A 1 248 ? 32.099  -9.141  -1.642  1.00 16.76 ? 247 PHE   A N   1 
ATOM   1897 C CA  . PHE   A 1 248 ? 31.115  -8.063  -1.404  1.00 16.64 ? 247 PHE   A CA  1 
ATOM   1898 C C   . PHE   A 1 248 ? 30.158  -7.972  -2.584  1.00 16.63 ? 247 PHE   A C   1 
ATOM   1899 O O   . PHE   A 1 248 ? 28.953  -7.930  -2.373  1.00 16.87 ? 247 PHE   A O   1 
ATOM   1900 C CB  . PHE   A 1 248 ? 31.834  -6.741  -1.094  1.00 15.78 ? 247 PHE   A CB  1 
ATOM   1901 C CG  . PHE   A 1 248 ? 30.984  -5.570  -0.646  1.00 15.86 ? 247 PHE   A CG  1 
ATOM   1902 C CD1 . PHE   A 1 248 ? 29.672  -5.752  -0.222  1.00 15.94 ? 247 PHE   A CD1 1 
ATOM   1903 C CD2 . PHE   A 1 248 ? 31.517  -4.297  -0.592  1.00 16.87 ? 247 PHE   A CD2 1 
ATOM   1904 C CE1 . PHE   A 1 248 ? 28.886  -4.656  0.166   1.00 16.02 ? 247 PHE   A CE1 1 
ATOM   1905 C CE2 . PHE   A 1 248 ? 30.747  -3.212  -0.185  1.00 16.90 ? 247 PHE   A CE2 1 
ATOM   1906 C CZ  . PHE   A 1 248 ? 29.438  -3.401  0.189   1.00 15.93 ? 247 PHE   A CZ  1 
ATOM   1907 N N   . HIS   A 1 249 ? 30.674  -8.069  -3.834  1.00 15.68 ? 248 HIS   A N   1 
ATOM   1908 C CA  . HIS   A 1 249 ? 29.764  -8.075  -4.992  1.00 15.74 ? 248 HIS   A CA  1 
ATOM   1909 C C   . HIS   A 1 249 ? 28.769  -9.254  -4.935  1.00 15.47 ? 248 HIS   A C   1 
ATOM   1910 O O   . HIS   A 1 249 ? 27.589  -9.095  -5.261  1.00 15.96 ? 248 HIS   A O   1 
ATOM   1911 C CB  . HIS   A 1 249 ? 30.585  -8.126  -6.289  1.00 16.85 ? 248 HIS   A CB  1 
ATOM   1912 C CG  . HIS   A 1 249 ? 31.180  -6.799  -6.633  1.00 19.05 ? 248 HIS   A CG  1 
ATOM   1913 N ND1 . HIS   A 1 249 ? 32.558  -6.615  -6.755  1.00 21.73 ? 248 HIS   A ND1 1 
ATOM   1914 C CD2 . HIS   A 1 249 ? 30.561  -5.617  -6.852  1.00 18.74 ? 248 HIS   A CD2 1 
ATOM   1915 C CE1 . HIS   A 1 249 ? 32.717  -5.345  -7.077  1.00 20.56 ? 248 HIS   A CE1 1 
ATOM   1916 N NE2 . HIS   A 1 249 ? 31.538  -4.705  -7.145  1.00 21.45 ? 248 HIS   A NE2 1 
ATOM   1917 N N   . ASN   A 1 250 ? 29.240  -10.434 -4.491  1.00 14.84 ? 249 ASN   A N   1 
ATOM   1918 C CA  . ASN   A 1 250 ? 28.347  -11.598 -4.398  1.00 14.55 ? 249 ASN   A CA  1 
ATOM   1919 C C   . ASN   A 1 250 ? 27.329  -11.402 -3.276  1.00 15.41 ? 249 ASN   A C   1 
ATOM   1920 O O   . ASN   A 1 250 ? 26.166  -11.778 -3.441  1.00 15.93 ? 249 ASN   A O   1 
ATOM   1921 C CB  . ASN   A 1 250 ? 29.121  -12.872 -4.136  1.00 16.15 ? 249 ASN   A CB  1 
ATOM   1922 C CG  . ASN   A 1 250 ? 28.222  -14.051 -4.191  1.00 18.29 ? 249 ASN   A CG  1 
ATOM   1923 O OD1 . ASN   A 1 250 ? 27.793  -14.584 -3.153  1.00 17.59 ? 249 ASN   A OD1 1 
ATOM   1924 N ND2 . ASN   A 1 250 ? 27.854  -14.425 -5.409  1.00 21.03 ? 249 ASN   A ND2 1 
ATOM   1925 N N   . PHE   A 1 251 ? 27.749  -10.797 -2.157  1.00 15.03 ? 250 PHE   A N   1 
ATOM   1926 C CA  . PHE   A 1 251 ? 26.812  -10.504 -1.051  1.00 14.45 ? 250 PHE   A CA  1 
ATOM   1927 C C   . PHE   A 1 251 ? 25.677  -9.600  -1.526  1.00 14.25 ? 250 PHE   A C   1 
ATOM   1928 O O   . PHE   A 1 251 ? 24.510  -9.843  -1.205  1.00 14.76 ? 250 PHE   A O   1 
ATOM   1929 C CB  . PHE   A 1 251 ? 27.555  -9.811  0.101   1.00 14.95 ? 250 PHE   A CB  1 
ATOM   1930 C CG  . PHE   A 1 251 ? 26.690  -9.513  1.312   1.00 14.99 ? 250 PHE   A CG  1 
ATOM   1931 C CD1 . PHE   A 1 251 ? 26.065  -8.278  1.453   1.00 15.05 ? 250 PHE   A CD1 1 
ATOM   1932 C CD2 . PHE   A 1 251 ? 26.569  -10.435 2.340   1.00 14.60 ? 250 PHE   A CD2 1 
ATOM   1933 C CE1 . PHE   A 1 251 ? 25.309  -7.985  2.592   1.00 15.87 ? 250 PHE   A CE1 1 
ATOM   1934 C CE2 . PHE   A 1 251 ? 25.810  -10.136 3.479   1.00 15.37 ? 250 PHE   A CE2 1 
ATOM   1935 C CZ  . PHE   A 1 251 ? 25.185  -8.916  3.589   1.00 16.00 ? 250 PHE   A CZ  1 
ATOM   1936 N N   . ILE   A 1 252 ? 26.022  -8.580  -2.322  1.00 14.15 ? 251 ILE   A N   1 
ATOM   1937 C CA  . ILE   A 1 252 ? 25.002  -7.680  -2.871  1.00 14.55 ? 251 ILE   A CA  1 
ATOM   1938 C C   . ILE   A 1 252 ? 24.113  -8.466  -3.848  1.00 15.33 ? 251 ILE   A C   1 
ATOM   1939 O O   . ILE   A 1 252 ? 22.867  -8.339  -3.841  1.00 15.79 ? 251 ILE   A O   1 
ATOM   1940 C CB  . ILE   A 1 252 ? 25.712  -6.506  -3.584  1.00 14.59 ? 251 ILE   A CB  1 
ATOM   1941 C CG1 . ILE   A 1 252 ? 26.407  -5.608  -2.557  1.00 14.90 ? 251 ILE   A CG1 1 
ATOM   1942 C CG2 . ILE   A 1 252 ? 24.697  -5.701  -4.426  1.00 15.09 ? 251 ILE   A CG2 1 
ATOM   1943 C CD1 . ILE   A 1 252 ? 25.491  -5.017  -1.494  1.00 14.50 ? 251 ILE   A CD1 1 
ATOM   1944 N N   . LYS   A 1 253 ? 24.751  -9.308  -4.690  1.00 15.41 ? 252 LYS   A N   1 
ATOM   1945 C CA  . LYS   A 1 253 ? 23.993  -10.071 -5.674  1.00 15.65 ? 252 LYS   A CA  1 
ATOM   1946 C C   . LYS   A 1 253 ? 22.950  -10.971 -5.015  1.00 15.69 ? 252 LYS   A C   1 
ATOM   1947 O O   . LYS   A 1 253 ? 21.797  -10.990 -5.460  1.00 15.57 ? 252 LYS   A O   1 
ATOM   1948 C CB  . LYS   A 1 253 ? 24.909  -10.907 -6.583  1.00 17.76 ? 252 LYS   A CB  1 
ATOM   1949 C CG  . LYS   A 1 253 ? 24.119  -11.693 -7.642  1.00 22.78 ? 252 LYS   A CG  1 
ATOM   1950 C CD  . LYS   A 1 253 ? 25.006  -12.551 -8.538  1.00 29.36 ? 252 LYS   A CD  1 
ATOM   1951 C CE  . LYS   A 1 253 ? 24.147  -13.234 -9.589  1.00 34.35 ? 252 LYS   A CE  1 
ATOM   1952 N NZ  . LYS   A 1 253 ? 24.941  -14.113 -10.481 1.00 38.16 ? 252 LYS   A NZ  1 
ATOM   1953 N N   . VAL   A 1 254 ? 23.325  -11.664 -3.927  1.00 15.46 ? 253 VAL   A N   1 
ATOM   1954 C CA  . VAL   A 1 254 ? 22.363  -12.618 -3.331  1.00 15.60 ? 253 VAL   A CA  1 
ATOM   1955 C C   . VAL   A 1 254 ? 21.343  -11.953 -2.405  1.00 15.49 ? 253 VAL   A C   1 
ATOM   1956 O O   . VAL   A 1 254 ? 20.181  -12.396 -2.368  1.00 16.21 ? 253 VAL   A O   1 
ATOM   1957 C CB  . VAL   A 1 254 ? 23.041  -13.837 -2.669  1.00 17.15 ? 253 VAL   A CB  1 
ATOM   1958 C CG1 . VAL   A 1 254 ? 23.952  -14.538 -3.669  1.00 18.31 ? 253 VAL   A CG1 1 
ATOM   1959 C CG2 . VAL   A 1 254 ? 23.811  -13.439 -1.428  1.00 18.25 ? 253 VAL   A CG2 1 
ATOM   1960 N N   . THR   A 1 255 ? 21.740  -10.906 -1.684  1.00 14.91 ? 254 THR   A N   1 
ATOM   1961 C CA  . THR   A 1 255 ? 20.770  -10.192 -0.839  1.00 14.11 ? 254 THR   A CA  1 
ATOM   1962 C C   . THR   A 1 255 ? 19.754  -9.471  -1.730  1.00 13.67 ? 254 THR   A C   1 
ATOM   1963 O O   . THR   A 1 255 ? 18.591  -9.329  -1.358  1.00 14.70 ? 254 THR   A O   1 
ATOM   1964 C CB  . THR   A 1 255 ? 21.441  -9.241  0.132   1.00 14.16 ? 254 THR   A CB  1 
ATOM   1965 O OG1 . THR   A 1 255 ? 22.240  -8.279  -0.584  1.00 12.90 ? 254 THR   A OG1 1 
ATOM   1966 C CG2 . THR   A 1 255 ? 22.193  -9.959  1.195   1.00 14.92 ? 254 THR   A CG2 1 
ATOM   1967 N N   . LEU   A 1 256 ? 20.195  -8.994  -2.920  1.00 13.54 ? 255 LEU   A N   1 
ATOM   1968 C CA  . LEU   A 1 256 ? 19.272  -8.316  -3.829  1.00 13.85 ? 255 LEU   A CA  1 
ATOM   1969 C C   . LEU   A 1 256 ? 18.702  -9.253  -4.864  1.00 15.82 ? 255 LEU   A C   1 
ATOM   1970 O O   . LEU   A 1 256 ? 18.556  -8.864  -6.028  1.00 17.63 ? 255 LEU   A O   1 
ATOM   1971 C CB  . LEU   A 1 256 ? 19.901  -7.053  -4.467  1.00 12.75 ? 255 LEU   A CB  1 
ATOM   1972 C CG  . LEU   A 1 256 ? 20.495  -6.073  -3.455  1.00 13.99 ? 255 LEU   A CG  1 
ATOM   1973 C CD1 . LEU   A 1 256 ? 21.095  -4.852  -4.141  1.00 13.80 ? 255 LEU   A CD1 1 
ATOM   1974 C CD2 . LEU   A 1 256 ? 19.471  -5.672  -2.390  1.00 15.31 ? 255 LEU   A CD2 1 
ATOM   1975 N N   . THR   A 1 257 ? 18.402  -10.506 -4.479  1.00 15.32 ? 256 THR   A N   1 
ATOM   1976 C CA  . THR   A 1 257 ? 17.766  -11.448 -5.411  1.00 14.51 ? 256 THR   A CA  1 
ATOM   1977 C C   . THR   A 1 257 ? 16.325  -10.960 -5.632  1.00 14.95 ? 256 THR   A C   1 
ATOM   1978 O O   . THR   A 1 257 ? 15.600  -10.699 -4.652  1.00 13.84 ? 256 THR   A O   1 
ATOM   1979 C CB  . THR   A 1 257 ? 17.775  -12.863 -4.855  1.00 15.64 ? 256 THR   A CB  1 
ATOM   1980 O OG1 . THR   A 1 257 ? 19.121  -13.302 -4.703  1.00 16.74 ? 256 THR   A OG1 1 
ATOM   1981 C CG2 . THR   A 1 257 ? 17.078  -13.852 -5.794  1.00 16.46 ? 256 THR   A CG2 1 
ATOM   1982 N N   . LYS   A 1 258 ? 15.936  -10.762 -6.890  1.00 14.61 ? 257 LYS   A N   1 
ATOM   1983 C CA  . LYS   A 1 258 ? 14.629  -10.190 -7.213  1.00 16.28 ? 257 LYS   A CA  1 
ATOM   1984 C C   . LYS   A 1 258 ? 13.459  -11.006 -6.650  1.00 15.84 ? 257 LYS   A C   1 
ATOM   1985 O O   . LYS   A 1 258 ? 12.566  -10.457 -6.002  1.00 17.09 ? 257 LYS   A O   1 
ATOM   1986 C CB  . LYS   A 1 258 ? 14.503  -10.038 -8.730  1.00 19.97 ? 257 LYS   A CB  1 
ATOM   1987 C CG  . LYS   A 1 258 ? 13.237  -9.358  -9.177  1.00 25.04 ? 257 LYS   A CG  1 
ATOM   1988 C CD  . LYS   A 1 258 ? 13.197  -9.374  -10.698 1.00 31.30 ? 257 LYS   A CD  1 
ATOM   1989 C CE  . LYS   A 1 258 ? 12.159  -8.457  -11.284 1.00 35.72 ? 257 LYS   A CE  1 
ATOM   1990 N NZ  . LYS   A 1 258 ? 12.390  -8.284  -12.744 1.00 38.13 ? 257 LYS   A NZ  1 
ATOM   1991 N N   . SER   A 1 259 ? 13.491  -12.325 -6.857  1.00 15.52 ? 258 SER   A N   1 
ATOM   1992 C CA  . SER   A 1 259 ? 12.436  -13.191 -6.345  1.00 16.26 ? 258 SER   A CA  1 
ATOM   1993 C C   . SER   A 1 259 ? 12.664  -13.537 -4.883  1.00 16.92 ? 258 SER   A C   1 
ATOM   1994 O O   . SER   A 1 259 ? 13.690  -14.149 -4.542  1.00 17.72 ? 258 SER   A O   1 
ATOM   1995 C CB  . SER   A 1 259 ? 12.350  -14.476 -7.162  1.00 19.08 ? 258 SER   A CB  1 
ATOM   1996 O OG  . SER   A 1 259 ? 11.405  -15.365 -6.578  1.00 21.91 ? 258 SER   A OG  1 
ATOM   1997 N N   . PRO   A 1 260 ? 11.677  -13.267 -4.013  1.00 16.13 ? 259 PRO   A N   1 
ATOM   1998 C CA  . PRO   A 1 260 ? 11.837  -13.655 -2.607  1.00 16.89 ? 259 PRO   A CA  1 
ATOM   1999 C C   . PRO   A 1 260 ? 11.918  -15.176 -2.442  1.00 17.64 ? 259 PRO   A C   1 
ATOM   2000 O O   . PRO   A 1 260 ? 12.581  -15.623 -1.513  1.00 19.76 ? 259 PRO   A O   1 
ATOM   2001 C CB  . PRO   A 1 260 ? 10.637  -13.059 -1.884  1.00 18.17 ? 259 PRO   A CB  1 
ATOM   2002 C CG  . PRO   A 1 260 ? 9.750   -12.538 -2.919  1.00 18.91 ? 259 PRO   A CG  1 
ATOM   2003 C CD  . PRO   A 1 260 ? 10.413  -12.551 -4.267  1.00 16.16 ? 259 PRO   A CD  1 
ATOM   2004 N N   . LYS   A 1 261 ? 11.352  -15.953 -3.377  1.00 16.27 ? 260 LYS   A N   1 
ATOM   2005 C CA  . LYS   A 1 261 ? 11.443  -17.417 -3.302  1.00 16.40 ? 260 LYS   A CA  1 
ATOM   2006 C C   . LYS   A 1 261 ? 12.885  -17.925 -3.538  1.00 17.20 ? 260 LYS   A C   1 
ATOM   2007 O O   . LYS   A 1 261 ? 13.161  -19.106 -3.331  1.00 18.26 ? 260 LYS   A O   1 
ATOM   2008 C CB  . LYS   A 1 261 ? 10.505  -18.065 -4.315  1.00 18.76 ? 260 LYS   A CB  1 
ATOM   2009 C CG  . LYS   A 1 261 ? 9.035   -17.758 -4.106  1.00 22.72 ? 260 LYS   A CG  1 
ATOM   2010 C CD  . LYS   A 1 261 ? 8.187   -18.368 -5.222  1.00 26.51 ? 260 LYS   A CD  1 
ATOM   2011 C CE  . LYS   A 1 261 ? 6.734   -17.926 -5.190  1.00 31.36 ? 260 LYS   A CE  1 
ATOM   2012 N NZ  . LYS   A 1 261 ? 6.011   -18.259 -6.471  1.00 33.58 ? 260 LYS   A NZ  1 
ATOM   2013 N N   . LYS   A 1 262 ? 13.793  -17.044 -3.994  1.00 16.71 ? 261 LYS   A N   1 
ATOM   2014 C CA  . LYS   A 1 262 ? 15.200  -17.416 -4.209  1.00 16.93 ? 261 LYS   A CA  1 
ATOM   2015 C C   . LYS   A 1 262 ? 16.165  -16.649 -3.305  1.00 16.84 ? 261 LYS   A C   1 
ATOM   2016 O O   . LYS   A 1 262 ? 17.358  -16.933 -3.340  1.00 18.37 ? 261 LYS   A O   1 
ATOM   2017 C CB  . LYS   A 1 262 ? 15.579  -17.126 -5.664  1.00 18.33 ? 261 LYS   A CB  1 
ATOM   2018 C CG  . LYS   A 1 262 ? 14.862  -18.047 -6.626  1.00 21.22 ? 261 LYS   A CG  1 
ATOM   2019 C CD  . LYS   A 1 262 ? 14.796  -17.462 -7.992  1.00 28.29 ? 261 LYS   A CD  1 
ATOM   2020 C CE  . LYS   A 1 262 ? 15.766  -18.087 -8.926  1.00 33.89 ? 261 LYS   A CE  1 
ATOM   2021 N NZ  . LYS   A 1 262 ? 15.099  -18.450 -10.206 1.00 37.50 ? 261 LYS   A NZ  1 
ATOM   2022 N N   . ARG   A 1 263 ? 15.667  -15.684 -2.527  1.00 15.55 ? 262 ARG   A N   1 
ATOM   2023 C CA  . ARG   A 1 263 ? 16.475  -14.826 -1.684  1.00 15.13 ? 262 ARG   A CA  1 
ATOM   2024 C C   . ARG   A 1 263 ? 16.792  -15.533 -0.384  1.00 16.04 ? 262 ARG   A C   1 
ATOM   2025 O O   . ARG   A 1 263 ? 15.873  -16.046 0.268   1.00 16.62 ? 262 ARG   A O   1 
ATOM   2026 C CB  . ARG   A 1 263 ? 15.722  -13.500 -1.430  1.00 13.99 ? 262 ARG   A CB  1 
ATOM   2027 C CG  . ARG   A 1 263 ? 16.614  -12.405 -0.859  1.00 12.71 ? 262 ARG   A CG  1 
ATOM   2028 C CD  . ARG   A 1 263 ? 15.874  -11.089 -0.671  1.00 14.63 ? 262 ARG   A CD  1 
ATOM   2029 N NE  . ARG   A 1 263 ? 15.140  -10.692 -1.875  1.00 13.67 ? 262 ARG   A NE  1 
ATOM   2030 C CZ  . ARG   A 1 263 ? 13.910  -10.176 -1.868  1.00 14.42 ? 262 ARG   A CZ  1 
ATOM   2031 N NH1 . ARG   A 1 263 ? 13.254  -10.019 -0.724  1.00 13.60 ? 262 ARG   A NH1 1 
ATOM   2032 N NH2 . ARG   A 1 263 ? 13.291  -9.904  -3.013  1.00 13.88 ? 262 ARG   A NH2 1 
ATOM   2033 N N   . PRO   A 1 264 ? 18.076  -15.574 0.026   1.00 15.79 ? 263 PRO   A N   1 
ATOM   2034 C CA  . PRO   A 1 264 ? 18.407  -16.273 1.269   1.00 16.13 ? 263 PRO   A CA  1 
ATOM   2035 C C   . PRO   A 1 264 ? 17.873  -15.629 2.532   1.00 15.68 ? 263 PRO   A C   1 
ATOM   2036 O O   . PRO   A 1 264 ? 17.694  -14.410 2.600   1.00 16.44 ? 263 PRO   A O   1 
ATOM   2037 C CB  . PRO   A 1 264 ? 19.945  -16.269 1.300   1.00 17.37 ? 263 PRO   A CB  1 
ATOM   2038 C CG  . PRO   A 1 264 ? 20.375  -15.954 -0.148  1.00 18.20 ? 263 PRO   A CG  1 
ATOM   2039 C CD  . PRO   A 1 264 ? 19.290  -15.014 -0.617  1.00 16.10 ? 263 PRO   A CD  1 
ATOM   2040 N N   . SER   A 1 265 ? 17.653  -16.464 3.545   1.00 15.40 ? 264 SER   A N   1 
ATOM   2041 C CA  . SER   A 1 265 ? 17.209  -16.046 4.864   1.00 15.08 ? 264 SER   A CA  1 
ATOM   2042 C C   . SER   A 1 265 ? 18.321  -15.342 5.641   1.00 15.75 ? 264 SER   A C   1 
ATOM   2043 O O   . SER   A 1 265 ? 19.501  -15.473 5.289   1.00 16.26 ? 264 SER   A O   1 
ATOM   2044 C CB  . SER   A 1 265 ? 16.750  -17.259 5.655   1.00 15.36 ? 264 SER   A CB  1 
ATOM   2045 O OG  . SER   A 1 265 ? 17.849  -18.090 6.006   1.00 16.39 ? 264 SER   A OG  1 
ATOM   2046 N N   . ALA   A 1 266 ? 17.979  -14.674 6.763   1.00 15.37 ? 265 ALA   A N   1 
ATOM   2047 C CA  . ALA   A 1 266 ? 19.005  -14.027 7.598   1.00 15.87 ? 265 ALA   A CA  1 
ATOM   2048 C C   . ALA   A 1 266 ? 19.982  -15.069 8.145   1.00 16.44 ? 265 ALA   A C   1 
ATOM   2049 O O   . ALA   A 1 266 ? 21.192  -14.854 8.106   1.00 16.88 ? 265 ALA   A O   1 
ATOM   2050 C CB  . ALA   A 1 266 ? 18.346  -13.245 8.727   1.00 17.06 ? 265 ALA   A CB  1 
ATOM   2051 N N   . THR   A 1 267 ? 19.463  -16.211 8.598   1.00 15.87 ? 266 THR   A N   1 
ATOM   2052 C CA  . THR   A 1 267 ? 20.348  -17.279 9.094   1.00 16.53 ? 266 THR   A CA  1 
ATOM   2053 C C   . THR   A 1 267 ? 21.292  -17.793 7.990   1.00 16.64 ? 266 THR   A C   1 
ATOM   2054 O O   . THR   A 1 267 ? 22.486  -17.936 8.230   1.00 17.40 ? 266 THR   A O   1 
ATOM   2055 C CB  . THR   A 1 267 ? 19.548  -18.413 9.726   1.00 20.03 ? 266 THR   A CB  1 
ATOM   2056 O OG1 . THR   A 1 267 ? 18.950  -17.935 10.932  1.00 21.64 ? 266 THR   A OG1 1 
ATOM   2057 C CG2 . THR   A 1 267 ? 20.415  -19.604 10.067  1.00 21.39 ? 266 THR   A CG2 1 
ATOM   2058 N N   . LYS   A 1 268 ? 20.766  -18.002 6.781   1.00 15.79 ? 267 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 268 ? 21.597  -18.495 5.671   1.00 15.12 ? 267 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 268 ? 22.698  -17.472 5.332   1.00 15.37 ? 267 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 268 ? 23.870  -17.827 5.120   1.00 15.85 ? 267 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 268 ? 20.720  -18.787 4.441   1.00 15.52 ? 267 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 268 ? 21.505  -19.295 3.233   1.00 15.50 ? 267 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 268 ? 22.225  -20.617 3.503   1.00 16.04 ? 267 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 268 ? 22.885  -21.119 2.227   1.00 19.24 ? 267 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 268 ? 23.721  -22.340 2.460   1.00 18.90 ? 267 LYS   A NZ  1 
ATOM   2067 N N   . MET   A 1 269 ? 22.295  -16.185 5.280   1.00 14.64 ? 268 MET   A N   1 
ATOM   2068 C CA  . MET   A 1 269 ? 23.236  -15.124 4.996   1.00 13.85 ? 268 MET   A CA  1 
ATOM   2069 C C   . MET   A 1 269 ? 24.377  -15.054 5.979   1.00 15.44 ? 268 MET   A C   1 
ATOM   2070 O O   . MET   A 1 269 ? 25.463  -14.652 5.595   1.00 16.13 ? 268 MET   A O   1 
ATOM   2071 C CB  . MET   A 1 269 ? 22.510  -13.767 4.910   1.00 12.79 ? 268 MET   A CB  1 
ATOM   2072 C CG  . MET   A 1 269 ? 21.706  -13.638 3.689   1.00 14.48 ? 268 MET   A CG  1 
ATOM   2073 S SD  . MET   A 1 269 ? 22.572  -13.858 2.104   1.00 17.32 ? 268 MET   A SD  1 
ATOM   2074 C CE  . MET   A 1 269 ? 24.035  -12.886 2.352   1.00 16.42 ? 268 MET   A CE  1 
ATOM   2075 N N   . LEU   A 1 270 ? 24.145  -15.458 7.240   1.00 16.10 ? 269 LEU   A N   1 
ATOM   2076 C CA  . LEU   A 1 270 ? 25.215  -15.410 8.235   1.00 16.82 ? 269 LEU   A CA  1 
ATOM   2077 C C   . LEU   A 1 270 ? 26.422  -16.320 7.908   1.00 17.64 ? 269 LEU   A C   1 
ATOM   2078 O O   . LEU   A 1 270 ? 27.523  -16.121 8.464   1.00 18.48 ? 269 LEU   A O   1 
ATOM   2079 C CB  . LEU   A 1 270 ? 24.671  -15.684 9.640   1.00 17.54 ? 269 LEU   A CB  1 
ATOM   2080 C CG  . LEU   A 1 270 ? 23.924  -14.498 10.243  1.00 20.29 ? 269 LEU   A CG  1 
ATOM   2081 C CD1 . LEU   A 1 270 ? 23.156  -14.930 11.463  1.00 21.92 ? 269 LEU   A CD1 1 
ATOM   2082 C CD2 . LEU   A 1 270 ? 24.893  -13.388 10.622  1.00 20.92 ? 269 LEU   A CD2 1 
ATOM   2083 N N   . SER   A 1 271 ? 26.245  -17.287 6.998   1.00 17.90 ? 270 SER   A N   1 
ATOM   2084 C CA  . SER   A 1 271 ? 27.405  -18.121 6.616   1.00 18.51 ? 270 SER   A CA  1 
ATOM   2085 C C   . SER   A 1 271 ? 28.056  -17.632 5.295   1.00 18.85 ? 270 SER   A C   1 
ATOM   2086 O O   . SER   A 1 271 ? 29.058  -18.202 4.853   1.00 19.75 ? 270 SER   A O   1 
ATOM   2087 C CB  . SER   A 1 271 ? 27.095  -19.615 6.623   1.00 20.78 ? 270 SER   A CB  1 
ATOM   2088 O OG  . SER   A 1 271 ? 25.952  -19.920 5.862   1.00 24.04 ? 270 SER   A OG  1 
ATOM   2089 N N   . HIS   A 1 272 ? 27.561  -16.487 4.726   1.00 17.64 ? 271 HIS   A N   1 
ATOM   2090 C CA  . HIS   A 1 272 ? 28.151  -15.926 3.515   1.00 16.91 ? 271 HIS   A CA  1 
ATOM   2091 C C   . HIS   A 1 272 ? 29.580  -15.479 3.862   1.00 17.95 ? 271 HIS   A C   1 
ATOM   2092 O O   . HIS   A 1 272 ? 29.823  -14.952 4.954   1.00 17.93 ? 271 HIS   A O   1 
ATOM   2093 C CB  . HIS   A 1 272 ? 27.324  -14.731 2.965   1.00 15.79 ? 271 HIS   A CB  1 
ATOM   2094 C CG  . HIS   A 1 272 ? 27.789  -14.309 1.611   1.00 15.19 ? 271 HIS   A CG  1 
ATOM   2095 N ND1 . HIS   A 1 272 ? 28.873  -13.470 1.454   1.00 17.03 ? 271 HIS   A ND1 1 
ATOM   2096 C CD2 . HIS   A 1 272 ? 27.297  -14.626 0.394   1.00 15.47 ? 271 HIS   A CD2 1 
ATOM   2097 C CE1 . HIS   A 1 272 ? 29.023  -13.320 0.145   1.00 17.35 ? 271 HIS   A CE1 1 
ATOM   2098 N NE2 . HIS   A 1 272 ? 28.069  -13.974 -0.529  1.00 16.42 ? 271 HIS   A NE2 1 
ATOM   2099 N N   . GLN   A 1 273 ? 30.496  -15.652 2.931   1.00 18.73 ? 272 GLN   A N   1 
ATOM   2100 C CA  . GLN   A 1 273 ? 31.911  -15.306 3.116   1.00 19.42 ? 272 GLN   A CA  1 
ATOM   2101 C C   . GLN   A 1 273 ? 32.129  -13.876 3.620   1.00 18.71 ? 272 GLN   A C   1 
ATOM   2102 O O   . GLN   A 1 273 ? 33.023  -13.627 4.441   1.00 19.66 ? 272 GLN   A O   1 
ATOM   2103 C CB  . GLN   A 1 273 ? 32.645  -15.497 1.772   1.00 23.53 ? 272 GLN   A CB  1 
ATOM   2104 C CG  . GLN   A 1 273 ? 34.139  -15.166 1.809   1.00 29.55 ? 272 GLN   A CG  1 
ATOM   2105 C CD  . GLN   A 1 273 ? 34.812  -15.291 0.457   1.00 36.12 ? 272 GLN   A CD  1 
ATOM   2106 O OE1 . GLN   A 1 273 ? 34.193  -15.612 -0.567  1.00 37.62 ? 272 GLN   A OE1 1 
ATOM   2107 N NE2 . GLN   A 1 273 ? 36.105  -15.016 0.426   1.00 38.01 ? 272 GLN   A NE2 1 
ATOM   2108 N N   . LEU   A 1 274 ? 31.301  -12.921 3.149   1.00 17.72 ? 273 LEU   A N   1 
ATOM   2109 C CA  . LEU   A 1 274 ? 31.537  -11.536 3.540   1.00 17.16 ? 273 LEU   A CA  1 
ATOM   2110 C C   . LEU   A 1 274 ? 31.360  -11.339 5.057   1.00 17.84 ? 273 LEU   A C   1 
ATOM   2111 O O   . LEU   A 1 274 ? 32.143  -10.631 5.666   1.00 18.70 ? 273 LEU   A O   1 
ATOM   2112 C CB  . LEU   A 1 274 ? 30.610  -10.601 2.769   1.00 16.35 ? 273 LEU   A CB  1 
ATOM   2113 C CG  . LEU   A 1 274 ? 31.005  -9.128  2.901   1.00 16.82 ? 273 LEU   A CG  1 
ATOM   2114 C CD1 . LEU   A 1 274 ? 32.228  -8.823  2.059   1.00 18.04 ? 273 LEU   A CD1 1 
ATOM   2115 C CD2 . LEU   A 1 274 ? 29.866  -8.219  2.496   1.00 16.78 ? 273 LEU   A CD2 1 
ATOM   2116 N N   . VAL   A 1 275 ? 30.374  -12.003 5.660   1.00 16.96 ? 274 VAL   A N   1 
ATOM   2117 C CA  . VAL   A 1 275 ? 30.056  -11.789 7.081   1.00 16.67 ? 274 VAL   A CA  1 
ATOM   2118 C C   . VAL   A 1 275 ? 30.534  -12.878 8.010   1.00 18.53 ? 274 VAL   A C   1 
ATOM   2119 O O   . VAL   A 1 275 ? 30.381  -12.734 9.233   1.00 19.76 ? 274 VAL   A O   1 
ATOM   2120 C CB  . VAL   A 1 275 ? 28.542  -11.527 7.281   1.00 16.62 ? 274 VAL   A CB  1 
ATOM   2121 C CG1 . VAL   A 1 275 ? 28.136  -10.270 6.538   1.00 16.19 ? 274 VAL   A CG1 1 
ATOM   2122 C CG2 . VAL   A 1 275 ? 27.713  -12.728 6.833   1.00 17.59 ? 274 VAL   A CG2 1 
ATOM   2123 N N   . SER   A 1 276 ? 31.017  -14.001 7.463   1.00 19.03 ? 275 SER   A N   1 
ATOM   2124 C CA  . SER   A 1 276 ? 31.549  -15.081 8.298   1.00 20.02 ? 275 SER   A CA  1 
ATOM   2125 C C   . SER   A 1 276 ? 33.081  -15.027 8.367   1.00 21.76 ? 275 SER   A C   1 
ATOM   2126 O O   . SER   A 1 276 ? 33.678  -15.823 9.083   1.00 22.76 ? 275 SER   A O   1 
ATOM   2127 C CB  . SER   A 1 276 ? 31.064  -16.451 7.806   1.00 21.60 ? 275 SER   A CB  1 
ATOM   2128 O OG  . SER   A 1 276 ? 31.532  -16.703 6.492   1.00 24.57 ? 275 SER   A OG  1 
ATOM   2129 N N   . GLN   A 1 277 ? 33.730  -14.107 7.622   1.00 21.54 ? 276 GLN   A N   1 
ATOM   2130 C CA  . GLN   A 1 277 ? 35.184  -14.001 7.611   1.00 21.96 ? 276 GLN   A CA  1 
ATOM   2131 C C   . GLN   A 1 277 ? 35.725  -13.572 8.968   1.00 22.78 ? 276 GLN   A C   1 
ATOM   2132 O O   . GLN   A 1 277 ? 35.046  -12.889 9.743   1.00 22.69 ? 276 GLN   A O   1 
ATOM   2133 C CB  . GLN   A 1 277 ? 35.645  -13.033 6.507   1.00 22.66 ? 276 GLN   A CB  1 
ATOM   2134 C CG  . GLN   A 1 277 ? 35.199  -11.598 6.732   1.00 23.42 ? 276 GLN   A CG  1 
ATOM   2135 C CD  . GLN   A 1 277 ? 35.654  -10.677 5.618   1.00 23.62 ? 276 GLN   A CD  1 
ATOM   2136 O OE1 . GLN   A 1 277 ? 34.860  -9.911  5.031   1.00 23.45 ? 276 GLN   A OE1 1 
ATOM   2137 N NE2 . GLN   A 1 277 ? 36.934  -10.692 5.329   1.00 21.71 ? 276 GLN   A NE2 1 
ATOM   2138 N N   . PRO   A 1 278 ? 36.945  -14.023 9.303   1.00 24.68 ? 277 PRO   A N   1 
ATOM   2139 C CA  . PRO   A 1 278 ? 37.529  -13.600 10.583  1.00 25.66 ? 277 PRO   A CA  1 
ATOM   2140 C C   . PRO   A 1 278 ? 37.914  -12.119 10.585  1.00 26.81 ? 277 PRO   A C   1 
ATOM   2141 O O   . PRO   A 1 278 ? 38.072  -11.484 9.526   1.00 27.15 ? 277 PRO   A O   1 
ATOM   2142 C CB  . PRO   A 1 278 ? 38.748  -14.516 10.746  1.00 26.16 ? 277 PRO   A CB  1 
ATOM   2143 C CG  . PRO   A 1 278 ? 39.113  -14.947 9.356   1.00 26.31 ? 277 PRO   A CG  1 
ATOM   2144 C CD  . PRO   A 1 278 ? 37.867  -14.855 8.505   1.00 24.84 ? 277 PRO   A CD  1 
ATOM   2145 N N   . GLY   A 1 279 ? 38.074  -11.574 11.780  1.00 26.54 ? 278 GLY   A N   1 
ATOM   2146 C CA  . GLY   A 1 279 ? 38.515  -10.197 11.948  1.00 26.79 ? 278 GLY   A CA  1 
ATOM   2147 C C   . GLY   A 1 279 ? 37.424  -9.152  11.898  1.00 26.40 ? 278 GLY   A C   1 
ATOM   2148 O O   . GLY   A 1 279 ? 37.711  -7.966  11.702  1.00 27.41 ? 278 GLY   A O   1 
ATOM   2149 N N   . LEU   A 1 280 ? 36.167  -9.571  12.073  1.00 24.40 ? 279 LEU   A N   1 
ATOM   2150 C CA  . LEU   A 1 280 ? 35.059  -8.623  12.088  1.00 23.51 ? 279 LEU   A CA  1 
ATOM   2151 C C   . LEU   A 1 280 ? 34.669  -8.372  13.537  1.00 25.18 ? 279 LEU   A C   1 
ATOM   2152 O O   . LEU   A 1 280 ? 34.127  -9.252  14.200  1.00 26.22 ? 279 LEU   A O   1 
ATOM   2153 C CB  . LEU   A 1 280 ? 33.867  -9.146  11.284  1.00 20.74 ? 279 LEU   A CB  1 
ATOM   2154 C CG  . LEU   A 1 280 ? 34.111  -9.501  9.814   1.00 19.75 ? 279 LEU   A CG  1 
ATOM   2155 C CD1 . LEU   A 1 280 ? 32.783  -9.884  9.135   1.00 19.14 ? 279 LEU   A CD1 1 
ATOM   2156 C CD2 . LEU   A 1 280 ? 34.734  -8.343  9.045   1.00 19.83 ? 279 LEU   A CD2 1 
ATOM   2157 N N   . ASN   A 1 281 ? 34.983  -7.183  14.042  1.00 25.59 ? 280 ASN   A N   1 
ATOM   2158 C CA  . ASN   A 1 281 ? 34.713  -6.837  15.435  1.00 25.05 ? 280 ASN   A CA  1 
ATOM   2159 C C   . ASN   A 1 281 ? 34.519  -5.330  15.596  1.00 23.95 ? 280 ASN   A C   1 
ATOM   2160 O O   . ASN   A 1 281 ? 34.775  -4.583  14.650  1.00 23.32 ? 280 ASN   A O   1 
ATOM   2161 C CB  . ASN   A 1 281 ? 35.848  -7.349  16.323  1.00 25.86 ? 280 ASN   A CB  1 
ATOM   2162 C CG  . ASN   A 1 281 ? 37.198  -6.819  15.901  1.00 30.11 ? 280 ASN   A CG  1 
ATOM   2163 O OD1 . ASN   A 1 281 ? 37.448  -5.597  15.847  1.00 31.66 ? 280 ASN   A OD1 1 
ATOM   2164 N ND2 . ASN   A 1 281 ? 38.110  -7.724  15.610  1.00 30.20 ? 280 ASN   A ND2 1 
ATOM   2165 N N   . ARG   A 1 282 ? 34.048  -4.892  16.791  1.00 23.04 ? 281 ARG   A N   1 
ATOM   2166 C CA  . ARG   A 1 282 ? 33.750  -3.508  17.103  1.00 23.76 ? 281 ARG   A CA  1 
ATOM   2167 C C   . ARG   A 1 282 ? 34.928  -2.559  16.937  1.00 23.33 ? 281 ARG   A C   1 
ATOM   2168 O O   . ARG   A 1 282 ? 34.709  -1.378  16.736  1.00 23.14 ? 281 ARG   A O   1 
ATOM   2169 C CB  . ARG   A 1 282 ? 33.129  -3.374  18.508  1.00 25.25 ? 281 ARG   A CB  1 
ATOM   2170 C CG  . ARG   A 1 282 ? 34.083  -3.738  19.641  1.00 26.46 ? 281 ARG   A CG  1 
ATOM   2171 C CD  . ARG   A 1 282 ? 33.345  -3.773  20.971  1.00 29.75 ? 281 ARG   A CD  1 
ATOM   2172 N NE  . ARG   A 1 282 ? 34.258  -3.937  22.103  1.00 33.26 ? 281 ARG   A NE  1 
ATOM   2173 C CZ  . ARG   A 1 282 ? 34.811  -2.930  22.773  1.00 35.40 ? 281 ARG   A CZ  1 
ATOM   2174 N NH1 . ARG   A 1 282 ? 35.643  -3.174  23.780  1.00 35.99 ? 281 ARG   A NH1 1 
ATOM   2175 N NH2 . ARG   A 1 282 ? 34.550  -1.672  22.433  1.00 33.73 ? 281 ARG   A NH2 1 
ATOM   2176 N N   . GLY   A 1 283 ? 36.150  -3.072  16.960  1.00 23.79 ? 282 GLY   A N   1 
ATOM   2177 C CA  . GLY   A 1 283 ? 37.338  -2.264  16.730  1.00 23.58 ? 282 GLY   A CA  1 
ATOM   2178 C C   . GLY   A 1 283 ? 37.338  -1.629  15.351  1.00 23.16 ? 282 GLY   A C   1 
ATOM   2179 O O   . GLY   A 1 283 ? 37.849  -0.521  15.189  1.00 23.74 ? 282 GLY   A O   1 
ATOM   2180 N N   . LEU   A 1 284 ? 36.714  -2.288  14.348  1.00 21.36 ? 283 LEU   A N   1 
ATOM   2181 C CA  . LEU   A 1 284 ? 36.594  -1.682  13.008  1.00 21.09 ? 283 LEU   A CA  1 
ATOM   2182 C C   . LEU   A 1 284 ? 35.736  -0.415  13.077  1.00 21.36 ? 283 LEU   A C   1 
ATOM   2183 O O   . LEU   A 1 284 ? 36.010  0.560   12.366  1.00 21.17 ? 283 LEU   A O   1 
ATOM   2184 C CB  . LEU   A 1 284 ? 35.924  -2.647  12.030  1.00 21.06 ? 283 LEU   A CB  1 
ATOM   2185 C CG  . LEU   A 1 284 ? 36.730  -3.882  11.720  1.00 22.11 ? 283 LEU   A CG  1 
ATOM   2186 C CD1 . LEU   A 1 284 ? 35.857  -4.913  10.988  1.00 21.98 ? 283 LEU   A CD1 1 
ATOM   2187 C CD2 . LEU   A 1 284 ? 38.002  -3.527  10.926  1.00 23.41 ? 283 LEU   A CD2 1 
ATOM   2188 N N   . ILE   A 1 285 ? 34.693  -0.437  13.917  1.00 21.12 ? 284 ILE   A N   1 
ATOM   2189 C CA  . ILE   A 1 285 ? 33.820  0.725   14.088  1.00 20.72 ? 284 ILE   A CA  1 
ATOM   2190 C C   . ILE   A 1 285 ? 34.463  1.775   14.990  1.00 22.42 ? 284 ILE   A C   1 
ATOM   2191 O O   . ILE   A 1 285 ? 34.269  2.967   14.753  1.00 23.31 ? 284 ILE   A O   1 
ATOM   2192 C CB  . ILE   A 1 285 ? 32.405  0.319   14.545  1.00 20.51 ? 284 ILE   A CB  1 
ATOM   2193 C CG1 . ILE   A 1 285 ? 31.790  -0.666  13.521  1.00 21.81 ? 284 ILE   A CG1 1 
ATOM   2194 C CG2 . ILE   A 1 285 ? 31.515  1.560   14.732  1.00 19.91 ? 284 ILE   A CG2 1 
ATOM   2195 C CD1 . ILE   A 1 285 ? 31.685  -0.106  12.074  1.00 23.79 ? 284 ILE   A CD1 1 
ATOM   2196 N N   . LEU   A 1 286 ? 35.299  1.354   15.956  1.00 22.62 ? 285 LEU   A N   1 
ATOM   2197 C CA  . LEU   A 1 286 ? 36.069  2.291   16.778  1.00 23.72 ? 285 LEU   A CA  1 
ATOM   2198 C C   . LEU   A 1 286 ? 37.020  3.099   15.880  1.00 23.90 ? 285 LEU   A C   1 
ATOM   2199 O O   . LEU   A 1 286 ? 37.121  4.324   16.053  1.00 24.34 ? 285 LEU   A O   1 
ATOM   2200 C CB  . LEU   A 1 286 ? 36.840  1.550   17.879  1.00 24.16 ? 285 LEU   A CB  1 
ATOM   2201 C CG  . LEU   A 1 286 ? 35.995  1.004   19.018  1.00 26.57 ? 285 LEU   A CG  1 
ATOM   2202 C CD1 . LEU   A 1 286 ? 36.857  0.288   20.036  1.00 27.72 ? 285 LEU   A CD1 1 
ATOM   2203 C CD2 . LEU   A 1 286 ? 35.188  2.107   19.695  1.00 27.69 ? 285 LEU   A CD2 1 
ATOM   2204 N N   . ASP   A 1 287 ? 37.601  2.449   14.845  1.00 23.73 ? 286 ASP   A N   1 
ATOM   2205 C CA  . ASP   A 1 287 ? 38.454  3.128   13.858  1.00 24.23 ? 286 ASP   A CA  1 
ATOM   2206 C C   . ASP   A 1 287 ? 37.600  4.154   13.100  1.00 23.84 ? 286 ASP   A C   1 
ATOM   2207 O O   . ASP   A 1 287 ? 38.049  5.262   12.848  1.00 24.75 ? 286 ASP   A O   1 
ATOM   2208 C CB  . ASP   A 1 287 ? 39.053  2.136   12.829  1.00 27.12 ? 286 ASP   A CB  1 
ATOM   2209 C CG  . ASP   A 1 287 ? 40.030  1.122   13.387  1.00 33.21 ? 286 ASP   A CG  1 
ATOM   2210 O OD1 . ASP   A 1 287 ? 40.602  1.382   14.463  1.00 33.45 ? 286 ASP   A OD1 1 
ATOM   2211 O OD2 . ASP   A 1 287 ? 40.223  0.057   12.740  1.00 35.49 ? 286 ASP   A OD2 1 
ATOM   2212 N N   . LEU   A 1 288 ? 36.376  3.765   12.711  1.00 23.07 ? 287 LEU   A N   1 
ATOM   2213 C CA  . LEU   A 1 288 ? 35.451  4.645   12.012  1.00 22.23 ? 287 LEU   A CA  1 
ATOM   2214 C C   . LEU   A 1 288 ? 35.099  5.859   12.894  1.00 23.17 ? 287 LEU   A C   1 
ATOM   2215 O O   . LEU   A 1 288 ? 35.156  6.976   12.420  1.00 23.20 ? 287 LEU   A O   1 
ATOM   2216 C CB  . LEU   A 1 288 ? 34.177  3.869   11.616  1.00 21.81 ? 287 LEU   A CB  1 
ATOM   2217 C CG  . LEU   A 1 288 ? 33.124  4.644   10.816  1.00 22.17 ? 287 LEU   A CG  1 
ATOM   2218 C CD1 . LEU   A 1 288 ? 33.644  4.992   9.424   1.00 22.97 ? 287 LEU   A CD1 1 
ATOM   2219 C CD2 . LEU   A 1 288 ? 31.859  3.835   10.694  1.00 21.64 ? 287 LEU   A CD2 1 
ATOM   2220 N N   . LEU   A 1 289 ? 34.813  5.653   14.179  1.00 24.00 ? 288 LEU   A N   1 
ATOM   2221 C CA  . LEU   A 1 289 ? 34.503  6.747   15.102  1.00 25.70 ? 288 LEU   A CA  1 
ATOM   2222 C C   . LEU   A 1 289 ? 35.696  7.668   15.346  1.00 28.33 ? 288 LEU   A C   1 
ATOM   2223 O O   . LEU   A 1 289 ? 35.506  8.862   15.589  1.00 28.50 ? 288 LEU   A O   1 
ATOM   2224 C CB  . LEU   A 1 289 ? 33.967  6.204   16.425  1.00 25.72 ? 288 LEU   A CB  1 
ATOM   2225 C CG  . LEU   A 1 289 ? 32.655  5.410   16.312  1.00 26.82 ? 288 LEU   A CG  1 
ATOM   2226 C CD1 . LEU   A 1 289 ? 32.248  4.855   17.668  1.00 28.08 ? 288 LEU   A CD1 1 
ATOM   2227 C CD2 . LEU   A 1 289 ? 31.540  6.259   15.701  1.00 26.67 ? 288 LEU   A CD2 1 
ATOM   2228 N N   . ASP   A 1 290 ? 36.924  7.129   15.241  1.00 29.66 ? 289 ASP   A N   1 
ATOM   2229 C CA  . ASP   A 1 290 ? 38.128  7.949   15.360  1.00 31.77 ? 289 ASP   A CA  1 
ATOM   2230 C C   . ASP   A 1 290 ? 38.182  8.966   14.213  1.00 33.55 ? 289 ASP   A C   1 
ATOM   2231 O O   . ASP   A 1 290 ? 38.662  10.071  14.429  1.00 33.46 ? 289 ASP   A O   1 
ATOM   2232 C CB  . ASP   A 1 290 ? 39.396  7.082   15.371  1.00 34.21 ? 289 ASP   A CB  1 
ATOM   2233 C CG  . ASP   A 1 290 ? 39.736  6.478   16.718  1.00 42.23 ? 289 ASP   A CG  1 
ATOM   2234 O OD1 . ASP   A 1 290 ? 39.148  6.917   17.735  1.00 44.30 ? 289 ASP   A OD1 1 
ATOM   2235 O OD2 . ASP   A 1 290 ? 40.605  5.577   16.763  1.00 45.34 ? 289 ASP   A OD2 1 
ATOM   2236 N N   . LYS   A 1 291 ? 37.646  8.625   13.016  1.00 34.78 ? 290 LYS   A N   1 
ATOM   2237 C CA  . LYS   A 1 291 ? 37.609  9.544   11.878  1.00 36.78 ? 290 LYS   A CA  1 
ATOM   2238 C C   . LYS   A 1 291 ? 36.741  10.788  12.138  1.00 39.14 ? 290 LYS   A C   1 
ATOM   2239 O O   . LYS   A 1 291 ? 36.925  11.797  11.458  1.00 39.48 ? 290 LYS   A O   1 
ATOM   2240 C CB  . LYS   A 1 291 ? 37.109  8.848   10.606  1.00 38.05 ? 290 LYS   A CB  1 
ATOM   2241 C CG  . LYS   A 1 291 ? 38.062  7.836   10.005  1.00 40.11 ? 290 LYS   A CG  1 
ATOM   2242 C CD  . LYS   A 1 291 ? 37.571  7.399   8.624   1.00 42.60 ? 290 LYS   A CD  1 
ATOM   2243 C CE  . LYS   A 1 291 ? 37.616  8.526   7.620   1.00 45.59 ? 290 LYS   A CE  1 
ATOM   2244 N NZ  . LYS   A 1 291 ? 37.182  8.091   6.266   1.00 47.53 ? 290 LYS   A NZ  1 
ATOM   2245 N N   . LEU   A 1 292 ? 35.795  10.719  13.099  1.00 40.48 ? 291 LEU   A N   1 
ATOM   2246 C CA  . LEU   A 1 292 ? 34.935  11.861  13.436  1.00 42.02 ? 291 LEU   A CA  1 
ATOM   2247 C C   . LEU   A 1 292 ? 35.731  13.023  14.015  1.00 44.87 ? 291 LEU   A C   1 
ATOM   2248 O O   . LEU   A 1 292 ? 35.337  14.174  13.839  1.00 45.19 ? 291 LEU   A O   1 
ATOM   2249 C CB  . LEU   A 1 292 ? 33.863  11.456  14.450  1.00 41.48 ? 291 LEU   A CB  1 
ATOM   2250 C CG  . LEU   A 1 292 ? 32.837  10.445  13.975  1.00 41.23 ? 291 LEU   A CG  1 
ATOM   2251 C CD1 . LEU   A 1 292 ? 31.947  10.020  15.115  1.00 41.69 ? 291 LEU   A CD1 1 
ATOM   2252 C CD2 . LEU   A 1 292 ? 31.987  11.031  12.881  1.00 41.12 ? 291 LEU   A CD2 1 
ATOM   2253 N N   . LYS   A 1 293 ? 36.820  12.719  14.743  1.00 46.73 ? 292 LYS   A N   1 
ATOM   2254 C CA  . LYS   A 1 293 ? 37.673  13.722  15.374  1.00 49.17 ? 292 LYS   A CA  1 
ATOM   2255 C C   . LYS   A 1 293 ? 38.395  14.577  14.339  1.00 51.28 ? 292 LYS   A C   1 
ATOM   2256 O O   . LYS   A 1 293 ? 38.550  15.778  14.544  1.00 52.05 ? 292 LYS   A O   1 
ATOM   2257 C CB  . LYS   A 1 293 ? 38.656  13.051  16.341  1.00 51.21 ? 292 LYS   A CB  1 
ATOM   2258 C CG  . LYS   A 1 293 ? 37.938  12.238  17.413  1.00 55.42 ? 292 LYS   A CG  1 
ATOM   2259 C CD  . LYS   A 1 293 ? 38.878  11.327  18.194  1.00 59.72 ? 292 LYS   A CD  1 
ATOM   2260 C CE  . LYS   A 1 293 ? 38.115  10.484  19.190  1.00 63.44 ? 292 LYS   A CE  1 
ATOM   2261 N NZ  . LYS   A 1 293 ? 38.991  9.501   19.881  1.00 65.85 ? 292 LYS   A NZ  1 
ATOM   2262 N N   . ASN   A 1 294 ? 38.801  13.975  13.215  1.00 52.14 ? 293 ASN   A N   1 
ATOM   2263 C CA  . ASN   A 1 294 ? 39.464  14.707  12.140  1.00 53.33 ? 293 ASN   A CA  1 
ATOM   2264 C C   . ASN   A 1 294 ? 38.466  15.100  11.056  1.00 53.88 ? 293 ASN   A C   1 
ATOM   2265 O O   . ASN   A 1 294 ? 38.011  16.242  11.027  1.00 54.10 ? 293 ASN   A O   1 
ATOM   2266 C CB  . ASN   A 1 294 ? 40.618  13.898  11.544  1.00 55.01 ? 293 ASN   A CB  1 
ATOM   2267 C CG  . ASN   A 1 294 ? 40.270  12.474  11.204  1.00 58.89 ? 293 ASN   A CG  1 
ATOM   2268 O OD1 . ASN   A 1 294 ? 40.327  11.583  12.053  1.00 60.60 ? 293 ASN   A OD1 1 
ATOM   2269 N ND2 . ASN   A 1 294 ? 39.910  12.222  9.951   1.00 59.57 ? 293 ASN   A ND2 1 
HETATM 2270 C C1  . A1ITB B 2 .   ? 22.116  10.192  19.394  1.00 24.77 ? 301 A1ITB A C1  1 
HETATM 2271 C C2  . A1ITB B 2 .   ? 20.951  9.558   18.925  1.00 24.19 ? 301 A1ITB A C2  1 
HETATM 2272 C C3  . A1ITB B 2 .   ? 20.751  10.077  17.671  1.00 24.47 ? 301 A1ITB A C3  1 
HETATM 2273 N N6  . A1ITB B 2 .   ? 16.148  6.254   15.319  1.00 17.68 ? 301 A1ITB A N6  1 
HETATM 2274 C C7  . A1ITB B 2 .   ? 18.598  6.861   19.702  1.00 21.12 ? 301 A1ITB A C7  1 
HETATM 2275 C C8  . A1ITB B 2 .   ? 16.815  6.894   18.260  1.00 19.26 ? 301 A1ITB A C8  1 
HETATM 2276 C C9  . A1ITB B 2 .   ? 17.296  8.126   17.680  1.00 20.27 ? 301 A1ITB A C9  1 
HETATM 2277 C C10 . A1ITB B 2 .   ? 16.637  8.914   16.585  1.00 20.33 ? 301 A1ITB A C10 1 
HETATM 2278 C C11 . A1ITB B 2 .   ? 16.296  10.351  16.873  1.00 20.58 ? 301 A1ITB A C11 1 
HETATM 2279 C C12 . A1ITB B 2 .   ? 17.384  10.041  15.924  1.00 20.53 ? 301 A1ITB A C12 1 
HETATM 2280 C C13 . A1ITB B 2 .   ? 15.626  6.111   17.825  1.00 18.20 ? 301 A1ITB A C13 1 
HETATM 2281 C C14 . A1ITB B 2 .   ? 14.736  5.519   18.717  1.00 18.32 ? 301 A1ITB A C14 1 
HETATM 2282 C C15 . A1ITB B 2 .   ? 13.504  4.550   17.048  1.00 18.68 ? 301 A1ITB A C15 1 
HETATM 2283 C C16 . A1ITB B 2 .   ? 14.350  5.070   16.096  1.00 18.28 ? 301 A1ITB A C16 1 
HETATM 2284 C C19 . A1ITB B 2 .   ? 13.443  4.281   13.875  1.00 18.58 ? 301 A1ITB A C19 1 
HETATM 2285 C C20 . A1ITB B 2 .   ? 19.300  6.142   20.832  1.00 22.16 ? 301 A1ITB A C20 1 
HETATM 2286 O O   . A1ITB B 2 .   ? 20.356  6.574   21.299  1.00 23.35 ? 301 A1ITB A O   1 
HETATM 2287 N N8  . A1ITB B 2 .   ? 18.705  5.042   21.291  1.00 22.00 ? 301 A1ITB A N8  1 
HETATM 2288 N N3  . A1ITB B 2 .   ? 17.483  6.278   19.246  1.00 20.62 ? 301 A1ITB A N3  1 
HETATM 2289 C C17 . A1ITB B 2 .   ? 15.449  5.852   16.450  1.00 17.90 ? 301 A1ITB A C17 1 
HETATM 2290 C C18 . A1ITB B 2 .   ? 15.474  5.715   14.331  1.00 17.07 ? 301 A1ITB A C18 1 
HETATM 2291 N N7  . A1ITB B 2 .   ? 14.390  4.994   14.720  1.00 17.86 ? 301 A1ITB A N7  1 
HETATM 2292 N N5  . A1ITB B 2 .   ? 13.688  4.774   18.353  1.00 19.07 ? 301 A1ITB A N5  1 
HETATM 2293 N N4  . A1ITB B 2 .   ? 18.413  8.678   18.172  1.00 20.59 ? 301 A1ITB A N4  1 
HETATM 2294 C C6  . A1ITB B 2 .   ? 19.056  8.055   19.165  1.00 21.64 ? 301 A1ITB A C6  1 
HETATM 2295 N N2  . A1ITB B 2 .   ? 20.227  8.634   19.652  1.00 22.88 ? 301 A1ITB A N2  1 
HETATM 2296 N N   . A1ITB B 2 .   ? 21.747  10.949  17.445  1.00 25.33 ? 301 A1ITB A N   1 
HETATM 2297 C C4  . A1ITB B 2 .   ? 21.966  11.767  16.263  1.00 26.59 ? 301 A1ITB A C4  1 
HETATM 2298 C C5  . A1ITB B 2 .   ? 21.092  12.994  16.296  1.00 28.06 ? 301 A1ITB A C5  1 
HETATM 2299 F F2  . A1ITB B 2 .   ? 19.787  12.696  16.238  1.00 28.32 ? 301 A1ITB A F2  1 
HETATM 2300 F F1  . A1ITB B 2 .   ? 21.324  13.829  15.287  1.00 28.98 ? 301 A1ITB A F1  1 
HETATM 2301 F F   . A1ITB B 2 .   ? 21.261  13.694  17.425  1.00 27.95 ? 301 A1ITB A F   1 
HETATM 2302 N N1  . A1ITB B 2 .   ? 22.591  11.033  18.498  1.00 24.96 ? 301 A1ITB A N1  1 
HETATM 2303 C C   . A1ITB B 2 .   ? 22.815  10.023  20.700  1.00 25.35 ? 301 A1ITB A C   1 
HETATM 2304 C C1  . EDO   C 3 .   ? 21.342  9.830   2.652   1.00 21.69 ? 302 EDO   A C1  1 
HETATM 2305 O O1  . EDO   C 3 .   ? 22.065  10.057  1.454   1.00 22.58 ? 302 EDO   A O1  1 
HETATM 2306 C C2  . EDO   C 3 .   ? 20.539  8.520   2.462   1.00 20.67 ? 302 EDO   A C2  1 
HETATM 2307 O O2  . EDO   C 3 .   ? 21.464  7.419   2.501   1.00 20.90 ? 302 EDO   A O2  1 
HETATM 2308 C C1  . EDO   D 3 .   ? -4.480  -6.858  -8.095  1.00 27.09 ? 303 EDO   A C1  1 
HETATM 2309 O O1  . EDO   D 3 .   ? -3.034  -6.875  -8.078  1.00 26.24 ? 303 EDO   A O1  1 
HETATM 2310 C C2  . EDO   D 3 .   ? -5.025  -5.764  -9.039  1.00 27.87 ? 303 EDO   A C2  1 
HETATM 2311 O O2  . EDO   D 3 .   ? -4.622  -6.043  -10.384 1.00 28.57 ? 303 EDO   A O2  1 
HETATM 2312 O O   . HOH   E 4 .   ? 22.766  12.578  9.197   1.00 29.77 ? 401 HOH   A O   1 
HETATM 2313 O O   . HOH   E 4 .   ? 22.028  12.656  -4.437  1.00 28.63 ? 402 HOH   A O   1 
HETATM 2314 O O   . HOH   E 4 .   ? 3.094   -1.747  10.821  1.00 35.90 ? 403 HOH   A O   1 
HETATM 2315 O O   . HOH   E 4 .   ? -4.165  4.685   23.989  1.00 37.97 ? 404 HOH   A O   1 
HETATM 2316 O O   . HOH   E 4 .   ? 38.853  -11.454 7.169   1.00 23.59 ? 405 HOH   A O   1 
HETATM 2317 O O   . HOH   E 4 .   ? 8.152   4.161   18.470  1.00 31.92 ? 406 HOH   A O   1 
HETATM 2318 O O   . HOH   E 4 .   ? 2.020   -6.866  -4.457  1.00 26.54 ? 407 HOH   A O   1 
HETATM 2319 O O   . HOH   E 4 .   ? 15.051  13.976  -8.042  1.00 18.48 ? 408 HOH   A O   1 
HETATM 2320 O O   . HOH   E 4 .   ? 28.548  16.466  8.109   1.00 24.96 ? 409 HOH   A O   1 
HETATM 2321 O O   . HOH   E 4 .   ? 4.286   1.004   14.506  1.00 29.41 ? 410 HOH   A O   1 
HETATM 2322 O O   . HOH   E 4 .   ? -9.007  3.833   24.874  1.00 36.56 ? 411 HOH   A O   1 
HETATM 2323 O O   . HOH   E 4 .   ? 30.018  -2.956  -10.041 1.00 39.89 ? 412 HOH   A O   1 
HETATM 2324 O O   . HOH   E 4 .   ? 10.304  4.353   10.747  1.00 30.03 ? 413 HOH   A O   1 
HETATM 2325 O O   . HOH   E 4 .   ? 12.109  -1.175  -14.255 1.00 27.79 ? 414 HOH   A O   1 
HETATM 2326 O O   . HOH   E 4 .   ? 35.031  6.430   6.150   1.00 31.33 ? 415 HOH   A O   1 
HETATM 2327 O O   . HOH   E 4 .   ? 35.899  6.708   3.294   1.00 32.82 ? 416 HOH   A O   1 
HETATM 2328 O O   . HOH   E 4 .   ? 32.351  4.875   -2.404  1.00 23.49 ? 417 HOH   A O   1 
HETATM 2329 O O   . HOH   E 4 .   ? 7.722   12.792  15.653  1.00 28.84 ? 418 HOH   A O   1 
HETATM 2330 O O   . HOH   E 4 .   ? 12.470  -4.593  22.132  1.00 37.80 ? 419 HOH   A O   1 
HETATM 2331 O O   . HOH   E 4 .   ? 28.898  -5.943  25.073  1.00 49.87 ? 420 HOH   A O   1 
HETATM 2332 O O   . HOH   E 4 .   ? -2.882  1.405   12.899  1.00 37.47 ? 421 HOH   A O   1 
HETATM 2333 O O   . HOH   E 4 .   ? 38.080  -1.060  8.286   1.00 24.56 ? 422 HOH   A O   1 
HETATM 2334 O O   . HOH   E 4 .   ? 8.574   -4.897  12.977  1.00 19.26 ? 423 HOH   A O   1 
HETATM 2335 O O   . HOH   E 4 .   ? 7.029   -16.192 6.426   1.00 30.51 ? 424 HOH   A O   1 
HETATM 2336 O O   . HOH   E 4 .   ? 10.224  2.545   17.893  1.00 30.74 ? 425 HOH   A O   1 
HETATM 2337 O O   . HOH   E 4 .   ? 3.292   -6.247  -1.195  1.00 25.84 ? 426 HOH   A O   1 
HETATM 2338 O O   . HOH   E 4 .   ? 16.673  -20.240 6.936   1.00 30.70 ? 427 HOH   A O   1 
HETATM 2339 O O   . HOH   E 4 .   ? 10.230  -9.265  -6.045  1.00 32.62 ? 428 HOH   A O   1 
HETATM 2340 O O   . HOH   E 4 .   ? 24.975  1.754   -6.749  1.00 22.40 ? 429 HOH   A O   1 
HETATM 2341 O O   . HOH   E 4 .   ? 13.303  -16.568 6.509   1.00 18.32 ? 430 HOH   A O   1 
HETATM 2342 O O   . HOH   E 4 .   ? 13.518  1.020   12.571  1.00 18.72 ? 431 HOH   A O   1 
HETATM 2343 O O   . HOH   E 4 .   ? 24.102  4.511   -4.289  1.00 20.59 ? 432 HOH   A O   1 
HETATM 2344 O O   . HOH   E 4 .   ? 21.306  -6.803  -11.233 1.00 29.88 ? 433 HOH   A O   1 
HETATM 2345 O O   . HOH   E 4 .   ? 36.235  -7.067  -7.490  1.00 31.98 ? 434 HOH   A O   1 
HETATM 2346 O O   . HOH   E 4 .   ? 20.415  9.533   10.761  1.00 21.65 ? 435 HOH   A O   1 
HETATM 2347 O O   . HOH   E 4 .   ? 14.498  10.694  12.289  1.00 22.94 ? 436 HOH   A O   1 
HETATM 2348 O O   . HOH   E 4 .   ? 29.960  -19.991 3.134   1.00 39.62 ? 437 HOH   A O   1 
HETATM 2349 O O   . HOH   E 4 .   ? -1.699  4.115   20.565  1.00 38.73 ? 438 HOH   A O   1 
HETATM 2350 O O   . HOH   E 4 .   ? -1.452  -7.590  -10.072 1.00 39.24 ? 439 HOH   A O   1 
HETATM 2351 O O   . HOH   E 4 .   ? 25.958  -21.668 3.877   1.00 30.37 ? 440 HOH   A O   1 
HETATM 2352 O O   . HOH   E 4 .   ? 11.595  13.125  10.773  1.00 35.21 ? 441 HOH   A O   1 
HETATM 2353 O O   . HOH   E 4 .   ? -7.944  6.609   18.053  1.00 35.07 ? 442 HOH   A O   1 
HETATM 2354 O O   . HOH   E 4 .   ? 11.945  10.921  -0.389  1.00 33.86 ? 443 HOH   A O   1 
HETATM 2355 O O   . HOH   E 4 .   ? 28.397  -9.072  18.434  1.00 35.01 ? 444 HOH   A O   1 
HETATM 2356 O O   . HOH   E 4 .   ? 19.813  9.992   13.981  1.00 23.95 ? 445 HOH   A O   1 
HETATM 2357 O O   . HOH   E 4 .   ? 36.142  12.259  8.957   1.00 45.04 ? 446 HOH   A O   1 
HETATM 2358 O O   . HOH   E 4 .   ? 18.024  14.751  14.536  1.00 36.48 ? 447 HOH   A O   1 
HETATM 2359 O O   . HOH   E 4 .   ? 8.708   4.133   8.469   1.00 23.51 ? 448 HOH   A O   1 
HETATM 2360 O O   . HOH   E 4 .   ? 0.100   -5.722  -1.259  1.00 29.78 ? 449 HOH   A O   1 
HETATM 2361 O O   . HOH   E 4 .   ? 18.025  7.714   13.598  1.00 18.91 ? 450 HOH   A O   1 
HETATM 2362 O O   . HOH   E 4 .   ? 39.672  -4.443  14.924  1.00 47.03 ? 451 HOH   A O   1 
HETATM 2363 O O   . HOH   E 4 .   ? 13.385  -13.936 23.094  1.00 38.82 ? 452 HOH   A O   1 
HETATM 2364 O O   . HOH   E 4 .   ? 28.278  10.401  15.348  1.00 34.36 ? 453 HOH   A O   1 
HETATM 2365 O O   . HOH   E 4 .   ? 9.044   -11.124 0.632   1.00 13.70 ? 454 HOH   A O   1 
HETATM 2366 O O   . HOH   E 4 .   ? 20.121  16.681  17.303  1.00 28.89 ? 455 HOH   A O   1 
HETATM 2367 O O   . HOH   E 4 .   ? 14.662  6.980   10.292  1.00 17.09 ? 456 HOH   A O   1 
HETATM 2368 O O   . HOH   E 4 .   ? 27.730  -5.160  17.874  1.00 19.10 ? 457 HOH   A O   1 
HETATM 2369 O O   . HOH   E 4 .   ? 13.230  -20.123 -11.162 1.00 26.89 ? 458 HOH   A O   1 
HETATM 2370 O O   . HOH   E 4 .   ? 4.146   -10.730 -3.736  1.00 28.33 ? 459 HOH   A O   1 
HETATM 2371 O O   . HOH   E 4 .   ? 19.736  5.970   6.076   1.00 14.15 ? 460 HOH   A O   1 
HETATM 2372 O O   . HOH   E 4 .   ? 4.765   0.152   -7.293  1.00 22.59 ? 461 HOH   A O   1 
HETATM 2373 O O   . HOH   E 4 .   ? 33.348  -18.549 5.757   1.00 34.01 ? 462 HOH   A O   1 
HETATM 2374 O O   . HOH   E 4 .   ? 4.760   6.088   16.516  1.00 33.65 ? 463 HOH   A O   1 
HETATM 2375 O O   . HOH   E 4 .   ? 26.573  -7.611  -7.272  1.00 19.29 ? 464 HOH   A O   1 
HETATM 2376 O O   . HOH   E 4 .   ? 16.800  11.771  -11.141 1.00 25.46 ? 465 HOH   A O   1 
HETATM 2377 O O   . HOH   E 4 .   ? 30.796  1.682   -5.344  1.00 18.07 ? 466 HOH   A O   1 
HETATM 2378 O O   . HOH   E 4 .   ? 40.557  2.876   16.837  1.00 52.70 ? 467 HOH   A O   1 
HETATM 2379 O O   . HOH   E 4 .   ? -8.186  -1.346  22.079  1.00 40.99 ? 468 HOH   A O   1 
HETATM 2380 O O   . HOH   E 4 .   ? 3.001   7.622   2.470   1.00 26.78 ? 469 HOH   A O   1 
HETATM 2381 O O   . HOH   E 4 .   ? 17.354  1.569   -4.213  1.00 27.93 ? 470 HOH   A O   1 
HETATM 2382 O O   . HOH   E 4 .   ? 21.575  11.412  -10.873 1.00 31.37 ? 471 HOH   A O   1 
HETATM 2383 O O   . HOH   E 4 .   ? 15.583  -16.570 11.850  1.00 19.52 ? 472 HOH   A O   1 
HETATM 2384 O O   . HOH   E 4 .   ? 7.485   9.415   3.318   1.00 31.05 ? 473 HOH   A O   1 
HETATM 2385 O O   . HOH   E 4 .   ? 12.605  2.571   1.616   1.00 12.59 ? 474 HOH   A O   1 
HETATM 2386 O O   . HOH   E 4 .   ? -5.720  -8.139  -11.710 1.00 21.39 ? 475 HOH   A O   1 
HETATM 2387 O O   . HOH   E 4 .   ? 14.690  7.753   -13.688 1.00 37.80 ? 476 HOH   A O   1 
HETATM 2388 O O   . HOH   E 4 .   ? 31.719  4.239   -5.042  1.00 30.56 ? 477 HOH   A O   1 
HETATM 2389 O O   . HOH   E 4 .   ? 15.207  -14.828 7.584   1.00 12.89 ? 478 HOH   A O   1 
HETATM 2390 O O   . HOH   E 4 .   ? 40.708  5.656   12.438  1.00 41.35 ? 479 HOH   A O   1 
HETATM 2391 O O   . HOH   E 4 .   ? 14.698  -0.536  20.693  1.00 33.46 ? 480 HOH   A O   1 
HETATM 2392 O O   . HOH   E 4 .   ? 9.953   -15.379 10.025  1.00 35.96 ? 481 HOH   A O   1 
HETATM 2393 O O   . HOH   E 4 .   ? 35.875  -8.523  2.706   1.00 21.69 ? 482 HOH   A O   1 
HETATM 2394 O O   . HOH   E 4 .   ? 5.021   -0.186  -12.880 1.00 33.26 ? 483 HOH   A O   1 
HETATM 2395 O O   . HOH   E 4 .   ? 23.366  -6.970  -7.644  1.00 28.42 ? 484 HOH   A O   1 
HETATM 2396 O O   . HOH   E 4 .   ? 35.336  3.090   1.604   1.00 26.86 ? 485 HOH   A O   1 
HETATM 2397 O O   . HOH   E 4 .   ? 37.003  5.449   18.557  1.00 37.98 ? 486 HOH   A O   1 
HETATM 2398 O O   . HOH   E 4 .   ? 17.577  9.600   7.313   1.00 26.13 ? 487 HOH   A O   1 
HETATM 2399 O O   . HOH   E 4 .   ? 37.291  -3.241  -0.778  1.00 21.84 ? 488 HOH   A O   1 
HETATM 2400 O O   . HOH   E 4 .   ? 20.793  -9.512  -7.528  1.00 21.47 ? 489 HOH   A O   1 
HETATM 2401 O O   . HOH   E 4 .   ? 12.040  1.158   21.306  1.00 49.79 ? 490 HOH   A O   1 
HETATM 2402 O O   . HOH   E 4 .   ? 3.897   8.496   6.513   1.00 29.25 ? 491 HOH   A O   1 
HETATM 2403 O O   . HOH   E 4 .   ? 38.921  -0.098  10.335  1.00 26.14 ? 492 HOH   A O   1 
HETATM 2404 O O   . HOH   E 4 .   ? 28.959  -12.455 16.386  1.00 29.84 ? 493 HOH   A O   1 
HETATM 2405 O O   . HOH   E 4 .   ? 39.179  -0.474  -2.814  1.00 30.26 ? 494 HOH   A O   1 
HETATM 2406 O O   . HOH   E 4 .   ? 33.744  -10.366 -13.204 1.00 61.18 ? 495 HOH   A O   1 
HETATM 2407 O O   . HOH   E 4 .   ? 11.790  -21.366 -2.576  1.00 18.79 ? 496 HOH   A O   1 
HETATM 2408 O O   . HOH   E 4 .   ? 11.441  9.064   6.296   1.00 26.95 ? 497 HOH   A O   1 
HETATM 2409 O O   . HOH   E 4 .   ? 14.490  9.551   2.293   1.00 27.39 ? 498 HOH   A O   1 
HETATM 2410 O O   . HOH   E 4 .   ? 12.592  5.087   8.476   1.00 18.46 ? 499 HOH   A O   1 
HETATM 2411 O O   . HOH   E 4 .   ? 14.981  -18.085 1.889   1.00 24.13 ? 500 HOH   A O   1 
HETATM 2412 O O   . HOH   E 4 .   ? 20.439  -14.153 15.905  1.00 21.58 ? 501 HOH   A O   1 
HETATM 2413 O O   . HOH   E 4 .   ? 35.731  6.084   -4.648  1.00 41.15 ? 502 HOH   A O   1 
HETATM 2414 O O   . HOH   E 4 .   ? 3.762   -13.297 4.753   1.00 33.49 ? 503 HOH   A O   1 
HETATM 2415 O O   . HOH   E 4 .   ? 3.626   -3.226  0.327   1.00 20.05 ? 504 HOH   A O   1 
HETATM 2416 O O   . HOH   E 4 .   ? 27.296  -14.460 13.240  1.00 23.57 ? 505 HOH   A O   1 
HETATM 2417 O O   . HOH   E 4 .   ? 1.816   -9.236  24.237  1.00 35.64 ? 506 HOH   A O   1 
HETATM 2418 O O   . HOH   E 4 .   ? 15.214  7.856   7.931   1.00 20.22 ? 507 HOH   A O   1 
HETATM 2419 O O   . HOH   E 4 .   ? 42.631  -0.273  11.388  1.00 35.63 ? 508 HOH   A O   1 
HETATM 2420 O O   . HOH   E 4 .   ? 36.067  4.147   6.819   1.00 24.84 ? 509 HOH   A O   1 
HETATM 2421 O O   . HOH   E 4 .   ? 32.340  -13.029 11.188  1.00 20.82 ? 510 HOH   A O   1 
HETATM 2422 O O   . HOH   E 4 .   ? 25.058  -10.461 18.943  1.00 29.95 ? 511 HOH   A O   1 
HETATM 2423 O O   . HOH   E 4 .   ? -5.151  -10.925 -10.613 1.00 29.61 ? 512 HOH   A O   1 
HETATM 2424 O O   . HOH   E 4 .   ? 10.453  9.005   10.315  1.00 22.34 ? 513 HOH   A O   1 
HETATM 2425 O O   . HOH   E 4 .   ? 13.456  -3.654  5.847   1.00 12.80 ? 514 HOH   A O   1 
HETATM 2426 O O   . HOH   E 4 .   ? 22.238  -14.098 18.001  1.00 33.20 ? 515 HOH   A O   1 
HETATM 2427 O O   . HOH   E 4 .   ? 6.569   -13.342 7.039   1.00 35.54 ? 516 HOH   A O   1 
HETATM 2428 O O   . HOH   E 4 .   ? 15.130  -1.060  -3.118  1.00 12.94 ? 517 HOH   A O   1 
HETATM 2429 O O   . HOH   E 4 .   ? 13.383  5.619   3.981   1.00 21.72 ? 518 HOH   A O   1 
HETATM 2430 O O   . HOH   E 4 .   ? 31.334  -11.738 -7.132  1.00 25.23 ? 519 HOH   A O   1 
HETATM 2431 O O   . HOH   E 4 .   ? 29.946  12.188  3.771   1.00 17.31 ? 520 HOH   A O   1 
HETATM 2432 O O   . HOH   E 4 .   ? 39.000  -9.500  3.836   1.00 29.45 ? 521 HOH   A O   1 
HETATM 2433 O O   . HOH   E 4 .   ? 29.780  8.144   -3.048  1.00 32.81 ? 522 HOH   A O   1 
HETATM 2434 O O   . HOH   E 4 .   ? 32.778  -9.589  17.214  1.00 33.38 ? 523 HOH   A O   1 
HETATM 2435 O O   . HOH   E 4 .   ? 27.223  -5.931  20.587  1.00 52.44 ? 524 HOH   A O   1 
HETATM 2436 O O   . HOH   E 4 .   ? 17.179  -5.638  22.876  1.00 24.00 ? 525 HOH   A O   1 
HETATM 2437 O O   . HOH   E 4 .   ? 28.366  -14.654 10.737  1.00 25.23 ? 526 HOH   A O   1 
HETATM 2438 O O   . HOH   E 4 .   ? 15.781  -0.172  13.507  1.00 17.21 ? 527 HOH   A O   1 
HETATM 2439 O O   . HOH   E 4 .   ? 21.339  -2.817  -12.073 1.00 44.91 ? 528 HOH   A O   1 
HETATM 2440 O O   . HOH   E 4 .   ? 35.666  0.592   23.750  1.00 38.58 ? 529 HOH   A O   1 
HETATM 2441 O O   . HOH   E 4 .   ? 0.602   -3.610  -0.178  1.00 32.88 ? 530 HOH   A O   1 
HETATM 2442 O O   . HOH   E 4 .   ? 8.269   12.091  -0.470  1.00 40.67 ? 531 HOH   A O   1 
HETATM 2443 O O   . HOH   E 4 .   ? 25.148  11.244  2.347   1.00 19.05 ? 532 HOH   A O   1 
HETATM 2444 O O   . HOH   E 4 .   ? 5.513   11.530  19.380  1.00 36.92 ? 533 HOH   A O   1 
HETATM 2445 O O   . HOH   E 4 .   ? 20.706  -17.797 13.198  1.00 34.61 ? 534 HOH   A O   1 
HETATM 2446 O O   . HOH   E 4 .   ? 12.396  15.599  13.316  1.00 48.92 ? 535 HOH   A O   1 
HETATM 2447 O O   . HOH   E 4 .   ? 38.049  3.907   9.112   1.00 33.14 ? 536 HOH   A O   1 
HETATM 2448 O O   . HOH   E 4 .   ? 30.285  -10.633 17.769  1.00 41.41 ? 537 HOH   A O   1 
HETATM 2449 O O   . HOH   E 4 .   ? 11.845  -4.305  2.070   1.00 11.91 ? 538 HOH   A O   1 
HETATM 2450 O O   . HOH   E 4 .   ? 9.963   1.704   6.431   1.00 20.47 ? 539 HOH   A O   1 
HETATM 2451 O O   . HOH   E 4 .   ? 40.262  -2.892  -4.523  1.00 17.83 ? 540 HOH   A O   1 
HETATM 2452 O O   . HOH   E 4 .   ? 16.145  20.304  23.069  1.00 41.17 ? 541 HOH   A O   1 
HETATM 2453 O O   . HOH   E 4 .   ? 21.500  4.486   -8.745  1.00 38.01 ? 542 HOH   A O   1 
HETATM 2454 O O   . HOH   E 4 .   ? 36.552  5.723   -0.011  1.00 43.62 ? 543 HOH   A O   1 
HETATM 2455 O O   . HOH   E 4 .   ? 7.712   7.680   -14.446 1.00 40.29 ? 544 HOH   A O   1 
HETATM 2456 O O   . HOH   E 4 .   ? -11.806 8.183   18.867  1.00 39.53 ? 545 HOH   A O   1 
HETATM 2457 O O   . HOH   E 4 .   ? 26.979  5.065   23.885  1.00 28.84 ? 546 HOH   A O   1 
HETATM 2458 O O   . HOH   E 4 .   ? 37.822  -13.088 14.258  1.00 49.85 ? 547 HOH   A O   1 
HETATM 2459 O O   . HOH   E 4 .   ? 21.437  -11.550 22.189  1.00 27.74 ? 548 HOH   A O   1 
HETATM 2460 O O   . HOH   E 4 .   ? 27.787  -5.142  -7.069  1.00 18.87 ? 549 HOH   A O   1 
HETATM 2461 O O   . HOH   E 4 .   ? 24.829  -22.740 -0.211  1.00 24.22 ? 550 HOH   A O   1 
HETATM 2462 O O   . HOH   E 4 .   ? 25.295  -18.040 2.574   1.00 29.28 ? 551 HOH   A O   1 
HETATM 2463 O O   . HOH   E 4 .   ? 16.500  8.896   3.687   1.00 24.63 ? 552 HOH   A O   1 
HETATM 2464 O O   . HOH   E 4 .   ? 16.419  18.562  17.747  1.00 40.33 ? 553 HOH   A O   1 
HETATM 2465 O O   . HOH   E 4 .   ? 17.606  -11.688 -9.111  1.00 21.65 ? 554 HOH   A O   1 
HETATM 2466 O O   . HOH   E 4 .   ? 5.735   -16.259 2.225   1.00 32.45 ? 555 HOH   A O   1 
HETATM 2467 O O   . HOH   E 4 .   ? 9.735   -16.493 -0.148  1.00 30.85 ? 556 HOH   A O   1 
HETATM 2468 O O   . HOH   E 4 .   ? 37.966  -9.543  -5.723  1.00 32.28 ? 557 HOH   A O   1 
HETATM 2469 O O   . HOH   E 4 .   ? 34.982  -12.193 12.675  1.00 29.39 ? 558 HOH   A O   1 
HETATM 2470 O O   . HOH   E 4 .   ? 12.606  11.542  -10.940 1.00 22.54 ? 559 HOH   A O   1 
HETATM 2471 O O   . HOH   E 4 .   ? 7.433   2.245   5.725   1.00 16.07 ? 560 HOH   A O   1 
HETATM 2472 O O   . HOH   E 4 .   ? 37.382  -1.203  1.463   1.00 22.31 ? 561 HOH   A O   1 
HETATM 2473 O O   . HOH   E 4 .   ? 25.702  -16.234 -6.354  1.00 31.94 ? 562 HOH   A O   1 
HETATM 2474 O O   . HOH   E 4 .   ? 22.876  -0.248  -9.880  1.00 26.34 ? 563 HOH   A O   1 
HETATM 2475 O O   . HOH   E 4 .   ? 33.265  8.716   0.544   1.00 26.87 ? 564 HOH   A O   1 
HETATM 2476 O O   . HOH   E 4 .   ? 36.503  -11.958 -2.618  1.00 23.45 ? 565 HOH   A O   1 
HETATM 2477 O O   . HOH   E 4 .   ? -0.740  7.149   11.748  1.00 26.63 ? 566 HOH   A O   1 
HETATM 2478 O O   . HOH   E 4 .   ? 21.510  -4.288  23.238  1.00 28.75 ? 567 HOH   A O   1 
HETATM 2479 O O   . HOH   E 4 .   ? 16.227  -1.899  -14.098 1.00 35.62 ? 568 HOH   A O   1 
HETATM 2480 O O   . HOH   E 4 .   ? 23.574  6.226   -6.288  1.00 33.92 ? 569 HOH   A O   1 
HETATM 2481 O O   . HOH   E 4 .   ? -2.343  2.770   16.799  1.00 43.44 ? 570 HOH   A O   1 
HETATM 2482 O O   . HOH   E 4 .   ? 20.822  -13.843 -7.126  1.00 33.18 ? 571 HOH   A O   1 
HETATM 2483 O O   . HOH   E 4 .   ? 29.959  -17.353 0.506   1.00 29.87 ? 572 HOH   A O   1 
HETATM 2484 O O   . HOH   E 4 .   ? 37.742  -5.128  18.807  1.00 41.77 ? 573 HOH   A O   1 
HETATM 2485 O O   . HOH   E 4 .   ? -2.223  4.008   13.233  1.00 33.50 ? 574 HOH   A O   1 
HETATM 2486 O O   . HOH   E 4 .   ? -3.950  -0.737  17.693  1.00 43.61 ? 575 HOH   A O   1 
HETATM 2487 O O   . HOH   E 4 .   ? 16.823  -20.055 11.240  1.00 43.39 ? 576 HOH   A O   1 
HETATM 2488 O O   . HOH   E 4 .   ? 8.817   -13.088 10.171  1.00 25.33 ? 577 HOH   A O   1 
HETATM 2489 O O   . HOH   E 4 .   ? 8.437   -14.747 -6.512  1.00 39.69 ? 578 HOH   A O   1 
HETATM 2490 O O   . HOH   E 4 .   ? 1.263   -8.563  -6.893  1.00 30.51 ? 579 HOH   A O   1 
HETATM 2491 O O   . HOH   E 4 .   ? 16.309  -0.547  -5.531  1.00 44.22 ? 580 HOH   A O   1 
HETATM 2492 O O   . HOH   E 4 .   ? 15.315  -13.724 -8.878  1.00 19.09 ? 581 HOH   A O   1 
HETATM 2493 O O   . HOH   E 4 .   ? 28.673  -18.626 9.846   1.00 28.31 ? 582 HOH   A O   1 
HETATM 2494 O O   . HOH   E 4 .   ? 17.638  -19.411 2.632   1.00 20.14 ? 583 HOH   A O   1 
HETATM 2495 O O   . HOH   E 4 .   ? 16.484  -16.473 9.391   1.00 16.16 ? 584 HOH   A O   1 
HETATM 2496 O O   . HOH   E 4 .   ? 13.735  -18.272 -0.150  1.00 32.41 ? 585 HOH   A O   1 
HETATM 2497 O O   . HOH   E 4 .   ? 14.026  1.762   5.772   1.00 27.08 ? 586 HOH   A O   1 
HETATM 2498 O O   . HOH   E 4 .   ? 4.946   6.954   -11.306 1.00 40.33 ? 587 HOH   A O   1 
HETATM 2499 O O   . HOH   E 4 .   ? 33.020  -7.241  18.601  1.00 31.14 ? 588 HOH   A O   1 
HETATM 2500 O O   . HOH   E 4 .   ? 15.593  13.047  13.304  1.00 28.66 ? 589 HOH   A O   1 
HETATM 2501 O O   . HOH   E 4 .   ? 31.545  -15.047 -2.185  1.00 44.93 ? 590 HOH   A O   1 
HETATM 2502 O O   . HOH   E 4 .   ? 4.125   -8.282  -4.431  1.00 29.85 ? 591 HOH   A O   1 
HETATM 2503 O O   . HOH   E 4 .   ? 36.922  3.692   4.057   1.00 38.11 ? 592 HOH   A O   1 
HETATM 2504 O O   . HOH   E 4 .   ? 32.052  -17.691 11.163  1.00 48.56 ? 593 HOH   A O   1 
HETATM 2505 O O   . HOH   E 4 .   ? 36.920  -13.667 3.258   1.00 58.87 ? 594 HOH   A O   1 
HETATM 2506 O O   . HOH   E 4 .   ? 8.018   -16.541 -8.391  1.00 37.07 ? 595 HOH   A O   1 
HETATM 2507 O O   . HOH   E 4 .   ? 2.035   -6.779  17.866  1.00 44.68 ? 596 HOH   A O   1 
HETATM 2508 O O   . HOH   E 4 .   ? 10.271  4.558   5.413   1.00 27.33 ? 597 HOH   A O   1 
HETATM 2509 O O   . HOH   E 4 .   ? 37.127  -10.934 15.855  1.00 55.87 ? 598 HOH   A O   1 
HETATM 2510 O O   . HOH   E 4 .   ? 28.693  -12.082 -7.693  1.00 26.61 ? 599 HOH   A O   1 
HETATM 2511 O O   . HOH   E 4 .   ? 12.890  -17.406 11.100  1.00 28.11 ? 600 HOH   A O   1 
HETATM 2512 O O   . HOH   E 4 .   ? 20.267  7.949   -8.236  1.00 35.72 ? 601 HOH   A O   1 
HETATM 2513 O O   . HOH   E 4 .   ? 35.745  -11.497 2.089   1.00 34.55 ? 602 HOH   A O   1 
HETATM 2514 O O   . HOH   E 4 .   ? 12.507  -2.279  20.130  1.00 37.82 ? 603 HOH   A O   1 
HETATM 2515 O O   . HOH   E 4 .   ? 25.968  11.867  15.615  1.00 49.40 ? 604 HOH   A O   1 
HETATM 2516 O O   . HOH   E 4 .   ? 37.090  -5.590  -10.139 1.00 35.55 ? 605 HOH   A O   1 
HETATM 2517 O O   . HOH   E 4 .   ? 12.590  10.757  10.381  1.00 24.00 ? 606 HOH   A O   1 
HETATM 2518 O O   . HOH   E 4 .   ? 18.318  -15.725 16.510  1.00 31.83 ? 607 HOH   A O   1 
HETATM 2519 O O   . HOH   E 4 .   ? 12.033  6.287   6.085   1.00 24.15 ? 608 HOH   A O   1 
HETATM 2520 O O   . HOH   E 4 .   ? 4.833   -13.777 0.609   1.00 34.69 ? 609 HOH   A O   1 
HETATM 2521 O O   . HOH   E 4 .   ? 34.620  -8.932  -8.655  1.00 37.71 ? 610 HOH   A O   1 
HETATM 2522 O O   . HOH   E 4 .   ? 7.066   -12.640 -0.684  1.00 20.07 ? 611 HOH   A O   1 
HETATM 2523 O O   . HOH   E 4 .   ? -6.240  -12.891 -9.350  1.00 29.37 ? 612 HOH   A O   1 
HETATM 2524 O O   . HOH   E 4 .   ? 30.215  -8.269  -10.053 1.00 42.12 ? 613 HOH   A O   1 
HETATM 2525 O O   . HOH   E 4 .   ? 13.635  0.265   23.168  1.00 45.33 ? 614 HOH   A O   1 
HETATM 2526 O O   . HOH   E 4 .   ? 4.515   -8.523  14.264  1.00 38.37 ? 615 HOH   A O   1 
HETATM 2527 O O   . HOH   E 4 .   ? 1.026   -11.509 -7.000  1.00 36.82 ? 616 HOH   A O   1 
HETATM 2528 O O   . HOH   E 4 .   ? 32.266  -14.668 -4.697  1.00 50.54 ? 617 HOH   A O   1 
HETATM 2529 O O   . HOH   E 4 .   ? 11.682  -16.997 -10.524 1.00 45.65 ? 618 HOH   A O   1 
HETATM 2530 O O   . HOH   E 4 .   ? 18.205  11.746  3.959   1.00 29.67 ? 619 HOH   A O   1 
HETATM 2531 O O   . HOH   E 4 .   ? 7.513   -15.303 -1.658  1.00 28.55 ? 620 HOH   A O   1 
HETATM 2532 O O   . HOH   E 4 .   ? 12.336  2.983   4.259   1.00 23.12 ? 621 HOH   A O   1 
HETATM 2533 O O   . HOH   E 4 .   ? 9.733   10.463  4.494   1.00 48.11 ? 622 HOH   A O   1 
HETATM 2534 O O   . HOH   E 4 .   ? 27.675  -9.389  -9.068  1.00 37.35 ? 623 HOH   A O   1 
HETATM 2535 O O   . HOH   E 4 .   ? 31.073  -15.295 11.988  1.00 42.23 ? 624 HOH   A O   1 
HETATM 2536 O O   . HOH   E 4 .   ? 32.307  12.653  2.753   1.00 27.82 ? 625 HOH   A O   1 
HETATM 2537 O O   . HOH   E 4 .   ? 11.875  6.657   10.604  1.00 22.57 ? 626 HOH   A O   1 
HETATM 2538 O O   . HOH   E 4 .   ? 23.764  14.641  -8.943  1.00 35.54 ? 627 HOH   A O   1 
HETATM 2539 O O   . HOH   E 4 .   ? 24.969  13.126  -4.978  1.00 36.85 ? 628 HOH   A O   1 
HETATM 2540 O O   . HOH   E 4 .   ? 20.186  -11.991 -8.884  1.00 39.78 ? 629 HOH   A O   1 
HETATM 2541 O O   . HOH   E 4 .   ? 28.880  -5.441  -9.954  1.00 39.35 ? 630 HOH   A O   1 
HETATM 2542 O O   . HOH   E 4 .   ? 16.356  8.854   11.700  1.00 20.35 ? 631 HOH   A O   1 
HETATM 2543 O O   . HOH   E 4 .   ? 23.901  -12.204 20.867  1.00 43.11 ? 632 HOH   A O   1 
HETATM 2544 O O   . HOH   E 4 .   ? 26.407  -10.461 -11.090 1.00 61.55 ? 633 HOH   A O   1 
HETATM 2545 O O   . HOH   E 4 .   ? 13.087  -18.248 8.591   1.00 30.13 ? 634 HOH   A O   1 
HETATM 2546 O O   . HOH   E 4 .   ? 39.406  -4.995  -2.750  1.00 29.47 ? 635 HOH   A O   1 
HETATM 2547 O O   . HOH   E 4 .   ? 13.823  -19.850 -13.810 1.00 42.22 ? 636 HOH   A O   1 
HETATM 2548 O O   . HOH   E 4 .   ? 32.247  7.732   -1.964  1.00 36.51 ? 637 HOH   A O   1 
HETATM 2549 O O   . HOH   E 4 .   ? 12.359  10.696  4.000   1.00 33.98 ? 638 HOH   A O   1 
HETATM 2550 O O   . HOH   E 4 .   ? 32.230  -10.066 -9.031  1.00 34.77 ? 639 HOH   A O   1 
HETATM 2551 O O   . HOH   E 4 .   ? 27.805  -20.986 2.120   1.00 49.35 ? 640 HOH   A O   1 
HETATM 2552 O O   . HOH   E 4 .   ? 34.680  -7.732  20.592  1.00 45.27 ? 641 HOH   A O   1 
HETATM 2553 O O   . HOH   E 4 .   ? 26.158  -19.758 10.284  1.00 22.70 ? 642 HOH   A O   1 
HETATM 2554 O O   . HOH   E 4 .   ? 6.523   -11.996 -3.691  1.00 33.68 ? 643 HOH   A O   1 
HETATM 2555 O O   . HOH   E 4 .   ? 29.470  11.429  17.768  1.00 37.44 ? 644 HOH   A O   1 
HETATM 2556 O O   . HOH   E 4 .   ? 23.113  2.587   -8.198  1.00 35.89 ? 645 HOH   A O   1 
HETATM 2557 O O   . HOH   E 4 .   ? 38.623  -7.613  2.530   1.00 32.68 ? 646 HOH   A O   1 
HETATM 2558 O O   . HOH   E 4 .   ? 10.951  -18.905 3.448   1.00 39.44 ? 647 HOH   A O   1 
HETATM 2559 O O   . HOH   E 4 .   ? 38.467  -3.138  20.417  1.00 42.90 ? 648 HOH   A O   1 
HETATM 2560 O O   . HOH   E 4 .   ? 13.484  -13.532 -10.861 1.00 41.15 ? 649 HOH   A O   1 
HETATM 2561 O O   . HOH   E 4 .   ? 22.555  -8.581  -9.473  1.00 30.52 ? 650 HOH   A O   1 
HETATM 2562 O O   . HOH   E 4 .   ? 13.541  -18.335 4.170   1.00 20.48 ? 651 HOH   A O   1 
HETATM 2563 O O   . HOH   E 4 .   ? 18.454  12.333  13.183  1.00 30.79 ? 652 HOH   A O   1 
HETATM 2564 O O   . HOH   E 4 .   ? 18.815  -19.817 0.312   1.00 27.21 ? 653 HOH   A O   1 
HETATM 2565 O O   . HOH   E 4 .   ? 0.902   -8.150  -9.349  1.00 41.28 ? 654 HOH   A O   1 
HETATM 2566 O O   . HOH   E 4 .   ? 17.890  10.309  9.964   1.00 25.66 ? 655 HOH   A O   1 
HETATM 2567 O O   . HOH   E 4 .   ? 7.027   -14.614 -4.346  1.00 27.60 ? 656 HOH   A O   1 
HETATM 2568 O O   . HOH   E 4 .   ? 19.180  10.614  -11.817 1.00 37.33 ? 657 HOH   A O   1 
HETATM 2569 O O   . HOH   E 4 .   ? 22.779  -15.591 -6.956  1.00 29.33 ? 658 HOH   A O   1 
HETATM 2570 O O   . HOH   E 4 .   ? 24.028  -16.900 0.827   1.00 32.81 ? 659 HOH   A O   1 
HETATM 2571 O O   . HOH   E 4 .   ? 14.761  10.677  -12.509 1.00 29.28 ? 660 HOH   A O   1 
HETATM 2572 O O   . HOH   E 4 .   ? 31.354  9.873   18.624  1.00 46.19 ? 661 HOH   A O   1 
HETATM 2573 O O   . HOH   E 4 .   ? 13.523  10.104  7.811   1.00 25.64 ? 662 HOH   A O   1 
HETATM 2574 O O   . HOH   E 4 .   ? 14.650  0.129   -14.048 1.00 30.37 ? 663 HOH   A O   1 
HETATM 2575 O O   . HOH   E 4 .   ? 37.060  1.414   0.286   1.00 32.38 ? 664 HOH   A O   1 
HETATM 2576 O O   . HOH   E 4 .   ? 7.779   -10.785 -5.978  1.00 32.17 ? 665 HOH   A O   1 
HETATM 2577 O O   . HOH   E 4 .   ? 20.867  1.538   -9.780  1.00 38.42 ? 666 HOH   A O   1 
HETATM 2578 O O   . HOH   E 4 .   ? 38.912  2.057   3.425   1.00 31.28 ? 667 HOH   A O   1 
HETATM 2579 O O   . HOH   E 4 .   ? 18.204  12.927  10.579  1.00 30.90 ? 668 HOH   A O   1 
HETATM 2580 O O   . HOH   E 4 .   ? 0.301   7.081   1.449   1.00 32.97 ? 669 HOH   A O   1 
HETATM 2581 O O   . HOH   E 4 .   ? 21.916  -15.925 14.424  1.00 39.68 ? 670 HOH   A O   1 
HETATM 2582 O O   . HOH   E 4 .   ? 11.346  -20.267 7.961   1.00 42.76 ? 671 HOH   A O   1 
HETATM 2583 O O   . HOH   E 4 .   ? 10.178  11.555  -12.158 1.00 36.01 ? 672 HOH   A O   1 
HETATM 2584 O O   . HOH   E 4 .   ? 3.180   -12.819 -5.371  1.00 36.50 ? 673 HOH   A O   1 
HETATM 2585 O O   . HOH   E 4 .   ? 31.005  13.365  16.949  1.00 46.55 ? 674 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   ? 0.7051 0.7332 0.4684 0.0773  0.1464  0.0529  7   ASP   A N   
2    C CA  . ASP   A 8   ? 0.7061 0.7314 0.4937 0.0744  0.1332  0.0495  7   ASP   A CA  
3    C C   . ASP   A 8   ? 0.6940 0.7195 0.4890 0.0817  0.1303  0.0355  7   ASP   A C   
4    O O   . ASP   A 8   ? 0.7052 0.7201 0.5010 0.0823  0.1166  0.0290  7   ASP   A O   
5    C CB  . ASP   A 8   ? 0.7300 0.7676 0.5492 0.0668  0.1368  0.0585  7   ASP   A CB  
6    C CG  . ASP   A 8   ? 0.8144 0.8500 0.6290 0.0590  0.1383  0.0726  7   ASP   A CG  
7    O OD1 . ASP   A 8   ? 0.8362 0.8738 0.6318 0.0592  0.1490  0.0787  7   ASP   A OD1 
8    O OD2 . ASP   A 8   ? 0.8481 0.8799 0.6780 0.0526  0.1289  0.0775  7   ASP   A OD2 
9    N N   . ILE   A 9   ? 0.6676 0.7053 0.4688 0.0872  0.1432  0.0312  8   ILE   A N   
10   C CA  . ILE   A 9   ? 0.6488 0.6865 0.4573 0.0949  0.1413  0.0183  8   ILE   A CA  
11   C C   . ILE   A 9   ? 0.6398 0.6747 0.4216 0.1040  0.1498  0.0103  8   ILE   A C   
12   O O   . ILE   A 9   ? 0.6317 0.6775 0.4074 0.1055  0.1650  0.0147  8   ILE   A O   
13   C CB  . ILE   A 9   ? 0.6386 0.6935 0.4813 0.0947  0.1481  0.0186  8   ILE   A CB  
14   C CG1 . ILE   A 9   ? 0.6439 0.7034 0.5119 0.0850  0.1423  0.0279  8   ILE   A CG1 
15   C CG2 . ILE   A 9   ? 0.6435 0.6961 0.4946 0.1024  0.1438  0.0059  8   ILE   A CG2 
16   C CD1 . ILE   A 9   ? 0.6463 0.7236 0.5469 0.0839  0.1492  0.0296  8   ILE   A CD1 
17   N N   . PHE   A 10  ? 0.6318 0.6526 0.3980 0.1101  0.1406  -0.0013 9   PHE   A N   
18   C CA  . PHE   A 10  ? 0.6331 0.6493 0.3725 0.1194  0.1476  -0.0106 9   PHE   A CA  
19   C C   . PHE   A 10  ? 0.6035 0.6293 0.3590 0.1278  0.1561  -0.0199 9   PHE   A C   
20   O O   . PHE   A 10  ? 0.5943 0.6181 0.3702 0.1287  0.1476  -0.0255 9   PHE   A O   
21   C CB  . PHE   A 10  ? 0.6553 0.6503 0.3692 0.1219  0.1329  -0.0193 9   PHE   A CB  
22   C CG  . PHE   A 10  ? 0.6819 0.6661 0.3750 0.1158  0.1240  -0.0119 9   PHE   A CG  
23   C CD1 . PHE   A 10  ? 0.7085 0.6900 0.3707 0.1172  0.1311  -0.0082 9   PHE   A CD1 
24   C CD2 . PHE   A 10  ? 0.6943 0.6703 0.3975 0.1092  0.1081  -0.0092 9   PHE   A CD2 
25   C CE1 . PHE   A 10  ? 0.7281 0.6987 0.3708 0.1120  0.1217  -0.0012 9   PHE   A CE1 
26   C CE2 . PHE   A 10  ? 0.7142 0.6803 0.3993 0.1044  0.0992  -0.0028 9   PHE   A CE2 
27   C CZ  . PHE   A 10  ? 0.7237 0.6868 0.3788 0.1059  0.1056  0.0013  9   PHE   A CZ  
28   N N   . ASN   A 11  ? 0.5853 0.6210 0.3311 0.1344  0.1725  -0.0219 10  ASN   A N   
29   C CA  . ASN   A 11  ? 0.5753 0.6203 0.3349 0.1439  0.1814  -0.0315 10  ASN   A CA  
30   C C   . ASN   A 11  ? 0.5766 0.6040 0.3101 0.1537  0.1758  -0.0467 10  ASN   A C   
31   O O   . ASN   A 11  ? 0.5674 0.5962 0.2810 0.1622  0.1875  -0.0532 10  ASN   A O   
32   C CB  . ASN   A 11  ? 0.5921 0.6573 0.3541 0.1467  0.2029  -0.0268 10  ASN   A CB  
33   C CG  . ASN   A 11  ? 0.6383 0.7172 0.4219 0.1561  0.2127  -0.0351 10  ASN   A CG  
34   O OD1 . ASN   A 11  ? 0.6559 0.7373 0.4676 0.1564  0.2053  -0.0379 10  ASN   A OD1 
35   N ND2 . ASN   A 11  ? 0.6505 0.7385 0.4213 0.1643  0.2297  -0.0392 10  ASN   A ND2 
36   N N   . ARG   A 12  ? 0.5763 0.5867 0.3090 0.1521  0.1579  -0.0523 11  ARG   A N   
37   C CA  . ARG   A 12  ? 0.5949 0.5866 0.3043 0.1599  0.1502  -0.0665 11  ARG   A CA  
38   C C   . ARG   A 12  ? 0.5870 0.5648 0.3088 0.1575  0.1318  -0.0718 11  ARG   A C   
39   O O   . ARG   A 12  ? 0.5666 0.5484 0.3121 0.1494  0.1245  -0.0640 11  ARG   A O   
40   C CB  . ARG   A 12  ? 0.6481 0.6274 0.3174 0.1596  0.1487  -0.0667 11  ARG   A CB  
41   C CG  . ARG   A 12  ? 0.7078 0.6754 0.3703 0.1498  0.1328  -0.0596 11  ARG   A CG  
42   C CD  . ARG   A 12  ? 0.7809 0.7298 0.4044 0.1525  0.1250  -0.0663 11  ARG   A CD  
43   N NE  . ARG   A 12  ? 0.8318 0.7844 0.4288 0.1519  0.1354  -0.0591 11  ARG   A NE  
44   C CZ  . ARG   A 12  ? 0.8752 0.8202 0.4373 0.1592  0.1409  -0.0665 11  ARG   A CZ  
45   N NH1 . ARG   A 12  ? 0.8781 0.8266 0.4163 0.1577  0.1503  -0.0582 11  ARG   A NH1 
46   N NH2 . ARG   A 12  ? 0.8851 0.8179 0.4349 0.1680  0.1369  -0.0823 11  ARG   A NH2 
47   N N   . ASP   A 13  ? 0.5913 0.5525 0.2969 0.1647  0.1246  -0.0852 12  ASP   A N   
48   C CA  . ASP   A 13  ? 0.5870 0.5335 0.3020 0.1628  0.1076  -0.0911 12  ASP   A CA  
49   C C   . ASP   A 13  ? 0.5932 0.5295 0.2994 0.1529  0.0934  -0.0850 12  ASP   A C   
50   O O   . ASP   A 13  ? 0.6098 0.5376 0.2871 0.1526  0.0914  -0.0856 12  ASP   A O   
51   C CB  . ASP   A 13  ? 0.6084 0.5382 0.3034 0.1730  0.1044  -0.1072 12  ASP   A CB  
52   C CG  . ASP   A 13  ? 0.6439 0.5599 0.3526 0.1735  0.0901  -0.1147 12  ASP   A CG  
53   O OD1 . ASP   A 13  ? 0.6252 0.5418 0.3539 0.1647  0.0802  -0.1076 12  ASP   A OD1 
54   O OD2 . ASP   A 13  ? 0.6758 0.5798 0.3746 0.1825  0.0889  -0.1278 12  ASP   A OD2 
55   N N   . PRO   A 14  ? 0.5753 0.5117 0.3051 0.1451  0.0828  -0.0796 13  PRO   A N   
56   C CA  . PRO   A 14  ? 0.5806 0.5076 0.3035 0.1363  0.0689  -0.0747 13  PRO   A CA  
57   C C   . PRO   A 14  ? 0.6027 0.5092 0.3010 0.1389  0.0566  -0.0854 13  PRO   A C   
58   O O   . PRO   A 14  ? 0.6084 0.5074 0.2905 0.1341  0.0481  -0.0826 13  PRO   A O   
59   C CB  . PRO   A 14  ? 0.5716 0.5027 0.3259 0.1295  0.0613  -0.0697 13  PRO   A CB  
60   C CG  . PRO   A 14  ? 0.5700 0.5049 0.3418 0.1360  0.0661  -0.0758 13  PRO   A CG  
61   C CD  . PRO   A 14  ? 0.5525 0.4973 0.3154 0.1442  0.0826  -0.0780 13  PRO   A CD  
62   N N   . ARG   A 15  ? 0.6180 0.5152 0.3138 0.1466  0.0554  -0.0978 14  ARG   A N   
63   C CA  . ARG   A 15  ? 0.6508 0.5275 0.3240 0.1498  0.0439  -0.1096 14  ARG   A CA  
64   C C   . ARG   A 15  ? 0.6765 0.5473 0.3129 0.1538  0.0475  -0.1130 14  ARG   A C   
65   O O   . ARG   A 15  ? 0.6921 0.5456 0.3069 0.1546  0.0360  -0.1212 14  ARG   A O   
66   C CB  . ARG   A 15  ? 0.6757 0.5443 0.3557 0.1581  0.0438  -0.1218 14  ARG   A CB  
67   C CG  . ARG   A 15  ? 0.7056 0.5776 0.4191 0.1542  0.0387  -0.1186 14  ARG   A CG  
68   C CD  . ARG   A 15  ? 0.7470 0.6172 0.4705 0.1640  0.0441  -0.1276 14  ARG   A CD  
69   N NE  . ARG   A 15  ? 0.7684 0.6406 0.5219 0.1605  0.0386  -0.1243 14  ARG   A NE  
70   C CZ  . ARG   A 15  ? 0.7781 0.6675 0.5567 0.1599  0.0467  -0.1165 14  ARG   A CZ  
71   N NH1 . ARG   A 15  ? 0.7667 0.6557 0.5693 0.1569  0.0404  -0.1141 14  ARG   A NH1 
72   N NH2 . ARG   A 15  ? 0.7688 0.6760 0.5484 0.1619  0.0611  -0.1109 14  ARG   A NH2 
73   N N   . ASP   A 16  ? 0.6742 0.5588 0.3028 0.1557  0.0628  -0.1062 15  ASP   A N   
74   C CA  . ASP   A 16  ? 0.6936 0.5731 0.2858 0.1585  0.0665  -0.1074 15  ASP   A CA  
75   C C   . ASP   A 16  ? 0.6973 0.5716 0.2793 0.1493  0.0544  -0.0986 15  ASP   A C   
76   O O   . ASP   A 16  ? 0.7155 0.5798 0.2656 0.1506  0.0506  -0.1012 15  ASP   A O   
77   C CB  . ASP   A 16  ? 0.7156 0.6124 0.3040 0.1623  0.0872  -0.1012 15  ASP   A CB  
78   C CG  . ASP   A 16  ? 0.7825 0.6855 0.3761 0.1730  0.1009  -0.1105 15  ASP   A CG  
79   O OD1 . ASP   A 16  ? 0.7988 0.6893 0.3929 0.1790  0.0942  -0.1234 15  ASP   A OD1 
80   O OD2 . ASP   A 16  ? 0.8067 0.7268 0.4045 0.1755  0.1184  -0.1048 15  ASP   A OD2 
81   N N   . HIS   A 17  ? 0.6739 0.5556 0.2827 0.1403  0.0485  -0.0882 16  HIS   A N   
82   C CA  . HIS   A 17  ? 0.6755 0.5537 0.2795 0.1319  0.0371  -0.0796 16  HIS   A CA  
83   C C   . HIS   A 17  ? 0.6697 0.5397 0.2915 0.1258  0.0195  -0.0817 16  HIS   A C   
84   O O   . HIS   A 17  ? 0.6806 0.5455 0.2970 0.1199  0.0078  -0.0772 16  HIS   A O   
85   C CB  . HIS   A 17  ? 0.6749 0.5695 0.2932 0.1260  0.0461  -0.0641 16  HIS   A CB  
86   C CG  . HIS   A 17  ? 0.7058 0.6089 0.3061 0.1298  0.0627  -0.0595 16  HIS   A CG  
87   N ND1 . HIS   A 17  ? 0.7425 0.6371 0.3082 0.1370  0.0667  -0.0671 16  HIS   A ND1 
88   C CD2 . HIS   A 17  ? 0.7105 0.6295 0.3229 0.1269  0.0758  -0.0477 16  HIS   A CD2 
89   C CE1 . HIS   A 17  ? 0.7462 0.6526 0.3042 0.1382  0.0830  -0.0595 16  HIS   A CE1 
90   N NE2 . HIS   A 17  ? 0.7327 0.6539 0.3186 0.1320  0.0888  -0.0475 16  HIS   A NE2 
91   N N   . TYR   A 18  ? 0.6509 0.5199 0.2941 0.1271  0.0177  -0.0878 17  TYR   A N   
92   C CA  . TYR   A 18  ? 0.6406 0.5028 0.3019 0.1210  0.0025  -0.0891 17  TYR   A CA  
93   C C   . TYR   A 18  ? 0.6515 0.5001 0.3124 0.1255  -0.0039 -0.1024 17  TYR   A C   
94   O O   . TYR   A 18  ? 0.6511 0.5000 0.3111 0.1333  0.0054  -0.1091 17  TYR   A O   
95   C CB  . TYR   A 18  ? 0.6085 0.4847 0.3040 0.1150  0.0056  -0.0794 17  TYR   A CB  
96   C CG  . TYR   A 18  ? 0.5961 0.4845 0.2962 0.1095  0.0102  -0.0661 17  TYR   A CG  
97   C CD1 . TYR   A 18  ? 0.6003 0.4867 0.3033 0.1022  -0.0011 -0.0600 17  TYR   A CD1 
98   C CD2 . TYR   A 18  ? 0.5996 0.5015 0.3026 0.1116  0.0257  -0.0596 17  TYR   A CD2 
99   C CE1 . TYR   A 18  ? 0.6060 0.5018 0.3127 0.0976  0.0026  -0.0481 17  TYR   A CE1 
100  C CE2 . TYR   A 18  ? 0.6047 0.5163 0.3119 0.1061  0.0294  -0.0473 17  TYR   A CE2 
101  C CZ  . TYR   A 18  ? 0.6151 0.5228 0.3235 0.0994  0.0177  -0.0416 17  TYR   A CZ  
102  O OH  . TYR   A 18  ? 0.6246 0.5403 0.3373 0.0944  0.0210  -0.0296 17  TYR   A OH  
103  N N   . ASP   A 19  ? 0.6582 0.4953 0.3227 0.1203  -0.0200 -0.1057 18  ASP   A N   
104  C CA  . ASP   A 19  ? 0.6728 0.4961 0.3409 0.1228  -0.0277 -0.1170 18  ASP   A CA  
105  C C   . ASP   A 19  ? 0.6656 0.4963 0.3677 0.1176  -0.0284 -0.1114 18  ASP   A C   
106  O O   . ASP   A 19  ? 0.6588 0.4954 0.3761 0.1091  -0.0346 -0.1029 18  ASP   A O   
107  C CB  . ASP   A 19  ? 0.7118 0.5187 0.3656 0.1191  -0.0451 -0.1233 18  ASP   A CB  
108  C CG  . ASP   A 19  ? 0.7941 0.5906 0.4115 0.1251  -0.0460 -0.1310 18  ASP   A CG  
109  O OD1 . ASP   A 19  ? 0.8065 0.5984 0.4090 0.1343  -0.0371 -0.1397 18  ASP   A OD1 
110  O OD2 . ASP   A 19  ? 0.8393 0.6323 0.4429 0.1208  -0.0556 -0.1285 18  ASP   A OD2 
111  N N   . LEU   A 20  ? 0.6621 0.4938 0.3764 0.1230  -0.0215 -0.1154 19  LEU   A N   
112  C CA  . LEU   A 20  ? 0.6595 0.4976 0.4041 0.1185  -0.0222 -0.1100 19  LEU   A CA  
113  C C   . LEU   A 20  ? 0.6660 0.4898 0.4180 0.1134  -0.0371 -0.1144 19  LEU   A C   
114  O O   . LEU   A 20  ? 0.6820 0.4899 0.4232 0.1178  -0.0427 -0.1252 19  LEU   A O   
115  C CB  . LEU   A 20  ? 0.6613 0.5049 0.4167 0.1264  -0.0108 -0.1127 19  LEU   A CB  
116  C CG  . LEU   A 20  ? 0.6705 0.5345 0.4452 0.1255  0.0014  -0.1023 19  LEU   A CG  
117  C CD1 . LEU   A 20  ? 0.6729 0.5403 0.4612 0.1330  0.0091  -0.1060 19  LEU   A CD1 
118  C CD2 . LEU   A 20  ? 0.6687 0.5400 0.4647 0.1152  -0.0043 -0.0920 19  LEU   A CD2 
119  N N   . LEU   A 21  ? 0.6534 0.4828 0.4244 0.1040  -0.0433 -0.1062 20  LEU   A N   
120  C CA  . LEU   A 21  ? 0.6543 0.4724 0.4356 0.0978  -0.0565 -0.1086 20  LEU   A CA  
121  C C   . LEU   A 21  ? 0.6411 0.4646 0.4486 0.0953  -0.0539 -0.1036 20  LEU   A C   
122  O O   . LEU   A 21  ? 0.6466 0.4786 0.4610 0.1007  -0.0432 -0.1018 20  LEU   A O   
123  C CB  . LEU   A 21  ? 0.6560 0.4752 0.4370 0.0890  -0.0668 -0.1040 20  LEU   A CB  
124  C CG  . LEU   A 21  ? 0.6898 0.5040 0.4447 0.0911  -0.0704 -0.1078 20  LEU   A CG  
125  C CD1 . LEU   A 21  ? 0.6962 0.5138 0.4553 0.0826  -0.0807 -0.1019 20  LEU   A CD1 
126  C CD2 . LEU   A 21  ? 0.7101 0.5052 0.4446 0.0966  -0.0769 -0.1211 20  LEU   A CD2 
127  N N   . GLN   A 22  ? 0.6159 0.4344 0.4376 0.0874  -0.0638 -0.1016 21  GLN   A N   
128  C CA  . GLN   A 22  ? 0.5921 0.4130 0.4357 0.0843  -0.0632 -0.0970 21  GLN   A CA  
129  C C   . GLN   A 22  ? 0.5479 0.3870 0.4064 0.0841  -0.0526 -0.0877 21  GLN   A C   
130  O O   . GLN   A 22  ? 0.5360 0.3877 0.3943 0.0818  -0.0482 -0.0815 21  GLN   A O   
131  C CB  . GLN   A 22  ? 0.6263 0.4425 0.4816 0.0739  -0.0746 -0.0940 21  GLN   A CB  
132  C CG  . GLN   A 22  ? 0.6971 0.5232 0.5532 0.0670  -0.0778 -0.0881 21  GLN   A CG  
133  C CD  . GLN   A 22  ? 0.7771 0.6028 0.6490 0.0568  -0.0867 -0.0840 21  GLN   A CD  
134  O OE1 . GLN   A 22  ? 0.7981 0.6202 0.6665 0.0519  -0.0960 -0.0855 21  GLN   A OE1 
135  N NE2 . GLN   A 22  ? 0.7909 0.6210 0.6808 0.0533  -0.0841 -0.0784 21  GLN   A NE2 
136  N N   . ARG   A 23  ? 0.5166 0.3561 0.3885 0.0864  -0.0493 -0.0867 22  ARG   A N   
137  C CA  . ARG   A 23  ? 0.4854 0.3410 0.3735 0.0852  -0.0413 -0.0780 22  ARG   A CA  
138  C C   . ARG   A 23  ? 0.4644 0.3241 0.3660 0.0747  -0.0471 -0.0705 22  ARG   A C   
139  O O   . ARG   A 23  ? 0.4724 0.3216 0.3784 0.0701  -0.0557 -0.0718 22  ARG   A O   
140  C CB  . ARG   A 23  ? 0.4809 0.3342 0.3788 0.0910  -0.0380 -0.0796 22  ARG   A CB  
141  C CG  . ARG   A 23  ? 0.4628 0.3318 0.3785 0.0893  -0.0315 -0.0709 22  ARG   A CG  
142  C CD  . ARG   A 23  ? 0.4634 0.3280 0.3895 0.0942  -0.0312 -0.0723 22  ARG   A CD  
143  N NE  . ARG   A 23  ? 0.4593 0.3387 0.4017 0.0932  -0.0257 -0.0646 22  ARG   A NE  
144  C CZ  . ARG   A 23  ? 0.4759 0.3578 0.4307 0.0859  -0.0296 -0.0577 22  ARG   A CZ  
145  N NH1 . ARG   A 23  ? 0.4652 0.3600 0.4332 0.0855  -0.0250 -0.0515 22  ARG   A NH1 
146  N NH2 . ARG   A 23  ? 0.4601 0.3317 0.4141 0.0787  -0.0383 -0.0569 22  ARG   A NH2 
147  N N   . LEU   A 24  ? 0.4323 0.3066 0.3401 0.0708  -0.0426 -0.0629 23  LEU   A N   
148  C CA  . LEU   A 24  ? 0.4103 0.2899 0.3309 0.0616  -0.0469 -0.0562 23  LEU   A CA  
149  C C   . LEU   A 24  ? 0.3917 0.2773 0.3290 0.0599  -0.0437 -0.0508 23  LEU   A C   
150  O O   . LEU   A 24  ? 0.3853 0.2671 0.3316 0.0541  -0.0490 -0.0485 23  LEU   A O   
151  C CB  . LEU   A 24  ? 0.4029 0.2941 0.3219 0.0587  -0.0442 -0.0512 23  LEU   A CB  
152  C CG  . LEU   A 24  ? 0.4248 0.3103 0.3274 0.0593  -0.0491 -0.0552 23  LEU   A CG  
153  C CD1 . LEU   A 24  ? 0.4193 0.3158 0.3181 0.0590  -0.0444 -0.0499 23  LEU   A CD1 
154  C CD2 . LEU   A 24  ? 0.4379 0.3154 0.3429 0.0528  -0.0604 -0.0569 23  LEU   A CD2 
155  N N   . GLY   A 25  ? 0.3787 0.2738 0.3195 0.0648  -0.0351 -0.0487 24  GLY   A N   
156  C CA  . GLY   A 25  ? 0.3701 0.2715 0.3257 0.0638  -0.0324 -0.0437 24  GLY   A CA  
157  C C   . GLY   A 25  ? 0.3675 0.2799 0.3264 0.0699  -0.0232 -0.0425 24  GLY   A C   
158  O O   . GLY   A 25  ? 0.3670 0.2808 0.3162 0.0758  -0.0182 -0.0462 24  GLY   A O   
159  N N   . GLY   A 26  ? 0.3564 0.2767 0.3289 0.0685  -0.0210 -0.0374 25  GLY   A N   
160  C CA  . GLY   A 26  ? 0.3546 0.2865 0.3336 0.0736  -0.0129 -0.0358 25  GLY   A CA  
161  C C   . GLY   A 26  ? 0.3435 0.2835 0.3378 0.0706  -0.0126 -0.0299 25  GLY   A C   
162  O O   . GLY   A 26  ? 0.3423 0.2766 0.3412 0.0664  -0.0186 -0.0279 25  GLY   A O   
163  N N   . GLY   A 27  ? 0.3264 0.2796 0.3280 0.0726  -0.0056 -0.0271 26  GLY   A N   
164  C CA  . GLY   A 27  ? 0.3229 0.2851 0.3388 0.0703  -0.0053 -0.0219 26  GLY   A CA  
165  C C   . GLY   A 27  ? 0.3146 0.2908 0.3385 0.0742  0.0027  -0.0204 26  GLY   A C   
166  O O   . GLY   A 27  ? 0.3106 0.2884 0.3301 0.0807  0.0083  -0.0241 26  GLY   A O   
167  N N   . THR   A 28  ? 0.3021 0.2888 0.3377 0.0699  0.0036  -0.0149 27  THR   A N   
168  C CA  . THR   A 28  ? 0.2985 0.2996 0.3444 0.0721  0.0108  -0.0126 27  THR   A CA  
169  C C   . THR   A 28  ? 0.3004 0.3068 0.3389 0.0719  0.0180  -0.0120 27  THR   A C   
170  O O   . THR   A 28  ? 0.3073 0.3243 0.3515 0.0753  0.0256  -0.0112 27  THR   A O   
171  C CB  . THR   A 28  ? 0.2990 0.3081 0.3577 0.0664  0.0084  -0.0072 27  THR   A CB  
172  O OG1 . THR   A 28  ? 0.2809 0.2867 0.3342 0.0591  0.0056  -0.0047 27  THR   A OG1 
173  C CG2 . THR   A 28  ? 0.3080 0.3136 0.3743 0.0677  0.0020  -0.0072 27  THR   A CG2 
174  N N   . TYR   A 29  ? 0.2900 0.2892 0.3162 0.0680  0.0157  -0.0120 28  TYR   A N   
175  C CA  . TYR   A 29  ? 0.2905 0.2922 0.3069 0.0675  0.0211  -0.0109 28  TYR   A CA  
176  C C   . TYR   A 29  ? 0.3088 0.3052 0.3112 0.0746  0.0247  -0.0166 28  TYR   A C   
177  O O   . TYR   A 29  ? 0.3164 0.3152 0.3092 0.0752  0.0300  -0.0157 28  TYR   A O   
178  C CB  . TYR   A 29  ? 0.2785 0.2747 0.2880 0.0609  0.0161  -0.0087 28  TYR   A CB  
179  C CG  . TYR   A 29  ? 0.2624 0.2460 0.2649 0.0602  0.0081  -0.0127 28  TYR   A CG  
180  C CD1 . TYR   A 29  ? 0.2759 0.2502 0.2637 0.0634  0.0065  -0.0175 28  TYR   A CD1 
181  C CD2 . TYR   A 29  ? 0.2589 0.2397 0.2692 0.0564  0.0022  -0.0117 28  TYR   A CD2 
182  C CE1 . TYR   A 29  ? 0.2914 0.2540 0.2743 0.0624  -0.0011 -0.0212 28  TYR   A CE1 
183  C CE2 . TYR   A 29  ? 0.2654 0.2350 0.2704 0.0553  -0.0046 -0.0147 28  TYR   A CE2 
184  C CZ  . TYR   A 29  ? 0.2918 0.2524 0.2840 0.0580  -0.0064 -0.0194 28  TYR   A CZ  
185  O OH  . TYR   A 29  ? 0.3191 0.2683 0.3072 0.0563  -0.0136 -0.0224 28  TYR   A OH  
186  N N   . GLY   A 30  ? 0.3136 0.3016 0.3136 0.0797  0.0214  -0.0224 29  GLY   A N   
187  C CA  . GLY   A 30  ? 0.3256 0.3069 0.3115 0.0868  0.0242  -0.0290 29  GLY   A CA  
188  C C   . GLY   A 30  ? 0.3385 0.3031 0.3136 0.0872  0.0154  -0.0346 29  GLY   A C   
189  O O   . GLY   A 30  ? 0.3416 0.3005 0.3221 0.0823  0.0077  -0.0331 29  GLY   A O   
190  N N   . GLU   A 31  ? 0.3319 0.2884 0.2913 0.0928  0.0167  -0.0412 30  GLU   A N   
191  C CA  . GLU   A 31  ? 0.3441 0.2837 0.2923 0.0933  0.0080  -0.0474 30  GLU   A CA  
192  C C   . GLU   A 31  ? 0.3478 0.2830 0.2794 0.0901  0.0060  -0.0479 30  GLU   A C   
193  O O   . GLU   A 31  ? 0.3589 0.2983 0.2795 0.0936  0.0129  -0.0486 30  GLU   A O   
194  C CB  . GLU   A 31  ? 0.3731 0.3050 0.3155 0.1030  0.0098  -0.0559 30  GLU   A CB  
195  C CG  . GLU   A 31  ? 0.4337 0.3689 0.3932 0.1069  0.0104  -0.0557 30  GLU   A CG  
196  C CD  . GLU   A 31  ? 0.5187 0.4428 0.4848 0.1025  -0.0001 -0.0548 30  GLU   A CD  
197  O OE1 . GLU   A 31  ? 0.5575 0.4658 0.5154 0.1051  -0.0062 -0.0612 30  GLU   A OE1 
198  O OE2 . GLU   A 31  ? 0.5220 0.4527 0.5007 0.0963  -0.0022 -0.0478 30  GLU   A OE2 
199  N N   . VAL   A 32  ? 0.3402 0.2675 0.2700 0.0836  -0.0031 -0.0471 31  VAL   A N   
200  C CA  . VAL   A 32  ? 0.3457 0.2700 0.2623 0.0800  -0.0064 -0.0466 31  VAL   A CA  
201  C C   . VAL   A 32  ? 0.3791 0.2877 0.2816 0.0812  -0.0146 -0.0542 31  VAL   A C   
202  O O   . VAL   A 32  ? 0.3857 0.2854 0.2937 0.0788  -0.0221 -0.0565 31  VAL   A O   
203  C CB  . VAL   A 32  ? 0.3318 0.2624 0.2588 0.0713  -0.0099 -0.0391 31  VAL   A CB  
204  C CG1 . VAL   A 32  ? 0.3350 0.2624 0.2495 0.0683  -0.0143 -0.0386 31  VAL   A CG1 
205  C CG2 . VAL   A 32  ? 0.3202 0.2654 0.2597 0.0702  -0.0020 -0.0321 31  VAL   A CG2 
206  N N   . PHE   A 33  ? 0.4015 0.3063 0.2851 0.0845  -0.0136 -0.0579 32  PHE   A N   
207  C CA  . PHE   A 33  ? 0.4274 0.3168 0.2952 0.0859  -0.0219 -0.0659 32  PHE   A CA  
208  C C   . PHE   A 33  ? 0.4403 0.3283 0.2968 0.0813  -0.0277 -0.0641 32  PHE   A C   
209  O O   . PHE   A 33  ? 0.4412 0.3384 0.2938 0.0806  -0.0224 -0.0585 32  PHE   A O   
210  C CB  . PHE   A 33  ? 0.4407 0.3247 0.2920 0.0956  -0.0161 -0.0740 32  PHE   A CB  
211  C CG  . PHE   A 33  ? 0.4517 0.3366 0.3133 0.1020  -0.0105 -0.0771 32  PHE   A CG  
212  C CD1 . PHE   A 33  ? 0.4542 0.3542 0.3276 0.1045  0.0002  -0.0720 32  PHE   A CD1 
213  C CD2 . PHE   A 33  ? 0.4748 0.3449 0.3342 0.1058  -0.0165 -0.0854 32  PHE   A CD2 
214  C CE1 . PHE   A 33  ? 0.4599 0.3615 0.3445 0.1107  0.0045  -0.0747 32  PHE   A CE1 
215  C CE2 . PHE   A 33  ? 0.4808 0.3513 0.3506 0.1122  -0.0121 -0.0880 32  PHE   A CE2 
216  C CZ  . PHE   A 33  ? 0.4679 0.3547 0.3506 0.1147  -0.0017 -0.0826 32  PHE   A CZ  
217  N N   . LYS   A 34  ? 0.4496 0.3252 0.3000 0.0785  -0.0389 -0.0690 33  LYS   A N   
218  C CA  . LYS   A 34  ? 0.4782 0.3505 0.3155 0.0755  -0.0459 -0.0690 33  LYS   A CA  
219  C C   . LYS   A 34  ? 0.5084 0.3744 0.3202 0.0834  -0.0421 -0.0756 33  LYS   A C   
220  O O   . LYS   A 34  ? 0.5119 0.3705 0.3171 0.0899  -0.0393 -0.0832 33  LYS   A O   
221  C CB  . LYS   A 34  ? 0.4992 0.3600 0.3390 0.0703  -0.0593 -0.0733 33  LYS   A CB  
222  C CG  . LYS   A 34  ? 0.5517 0.4110 0.3831 0.0661  -0.0683 -0.0724 33  LYS   A CG  
223  C CD  . LYS   A 34  ? 0.6123 0.4625 0.4511 0.0600  -0.0812 -0.0758 33  LYS   A CD  
224  C CE  . LYS   A 34  ? 0.6677 0.5191 0.5039 0.0550  -0.0909 -0.0739 33  LYS   A CE  
225  N NZ  . LYS   A 34  ? 0.6954 0.5403 0.5428 0.0481  -0.1029 -0.0765 33  LYS   A NZ  
226  N N   . ALA   A 35  ? 0.5343 0.4029 0.3314 0.0832  -0.0420 -0.0727 34  ALA   A N   
227  C CA  . ALA   A 35  ? 0.5718 0.4347 0.3422 0.0903  -0.0381 -0.0782 34  ALA   A CA  
228  C C   . ALA   A 35  ? 0.6009 0.4609 0.3545 0.0876  -0.0456 -0.0761 34  ALA   A C   
229  O O   . ALA   A 35  ? 0.5945 0.4603 0.3596 0.0810  -0.0509 -0.0688 34  ALA   A O   
230  C CB  . ALA   A 35  ? 0.5738 0.4484 0.3436 0.0956  -0.0224 -0.0744 34  ALA   A CB  
231  N N   . ARG   A 36  ? 0.6289 0.4794 0.3547 0.0930  -0.0466 -0.0828 35  ARG   A N   
232  C CA  . ARG   A 36  ? 0.6601 0.5064 0.3673 0.0911  -0.0547 -0.0812 35  ARG   A CA  
233  C C   . ARG   A 36  ? 0.6829 0.5309 0.3645 0.0972  -0.0445 -0.0800 35  ARG   A C   
234  O O   . ARG   A 36  ? 0.6855 0.5292 0.3532 0.1045  -0.0369 -0.0875 35  ARG   A O   
235  C CB  . ARG   A 36  ? 0.6964 0.5263 0.3918 0.0906  -0.0696 -0.0916 35  ARG   A CB  
236  C CG  . ARG   A 36  ? 0.7607 0.5863 0.4422 0.0872  -0.0819 -0.0898 35  ARG   A CG  
237  C CD  . ARG   A 36  ? 0.8301 0.6392 0.4994 0.0867  -0.0970 -0.1008 35  ARG   A CD  
238  N NE  . ARG   A 36  ? 0.8841 0.6901 0.5774 0.0817  -0.1042 -0.1040 35  ARG   A NE  
239  C CZ  . ARG   A 36  ? 0.9301 0.7243 0.6219 0.0846  -0.1055 -0.1140 35  ARG   A CZ  
240  N NH1 . ARG   A 36  ? 0.9381 0.7230 0.6058 0.0932  -0.1002 -0.1228 35  ARG   A NH1 
241  N NH2 . ARG   A 36  ? 0.9266 0.7180 0.6407 0.0791  -0.1121 -0.1152 35  ARG   A NH2 
242  N N   . ASP   A 37  ? 0.6959 0.5501 0.3716 0.0944  -0.0441 -0.0705 36  ASP   A N   
243  C CA  . ASP   A 37  ? 0.7245 0.5805 0.3751 0.0990  -0.0346 -0.0675 36  ASP   A CA  
244  C C   . ASP   A 37  ? 0.7613 0.6020 0.3792 0.1038  -0.0416 -0.0777 36  ASP   A C   
245  O O   . ASP   A 37  ? 0.7693 0.6007 0.3811 0.1007  -0.0570 -0.0805 36  ASP   A O   
246  C CB  . ASP   A 37  ? 0.7450 0.6084 0.3972 0.0939  -0.0357 -0.0546 36  ASP   A CB  
247  C CG  . ASP   A 37  ? 0.8128 0.6810 0.4452 0.0972  -0.0231 -0.0480 36  ASP   A CG  
248  O OD1 . ASP   A 37  ? 0.8362 0.6956 0.4373 0.1018  -0.0234 -0.0525 36  ASP   A OD1 
249  O OD2 . ASP   A 37  ? 0.8305 0.7110 0.4783 0.0947  -0.0130 -0.0380 36  ASP   A OD2 
250  N N   . LYS   A 38  ? 0.7806 0.6189 0.3783 0.1117  -0.0304 -0.0838 37  LYS   A N   
251  C CA  . LYS   A 38  ? 0.8135 0.6365 0.3777 0.1174  -0.0356 -0.0949 37  LYS   A CA  
252  C C   . LYS   A 38  ? 0.8426 0.6593 0.3803 0.1157  -0.0446 -0.0912 37  LYS   A C   
253  O O   . LYS   A 38  ? 0.8576 0.6597 0.3750 0.1170  -0.0574 -0.1004 37  LYS   A O   
254  C CB  . LYS   A 38  ? 0.8352 0.6593 0.3831 0.1267  -0.0193 -0.1011 37  LYS   A CB  
255  C CG  . LYS   A 38  ? 0.8750 0.6961 0.4379 0.1313  -0.0163 -0.1114 37  LYS   A CG  
256  C CD  . LYS   A 38  ? 0.9342 0.7566 0.4797 0.1415  -0.0004 -0.1183 37  LYS   A CD  
257  C CE  . LYS   A 38  ? 0.9797 0.7987 0.5407 0.1470  0.0023  -0.1285 37  LYS   A CE  
258  N NZ  . LYS   A 38  ? 1.0111 0.8342 0.5590 0.1575  0.0193  -0.1346 37  LYS   A NZ  
259  N N   . VAL   A 39  ? 0.8487 0.6756 0.3860 0.1127  -0.0388 -0.0780 38  VAL   A N   
260  C CA  . VAL   A 39  ? 0.8742 0.6949 0.3853 0.1114  -0.0473 -0.0732 38  VAL   A CA  
261  C C   . VAL   A 39  ? 0.8737 0.6936 0.4014 0.1038  -0.0647 -0.0679 38  VAL   A C   
262  O O   . VAL   A 39  ? 0.8889 0.6971 0.4012 0.1032  -0.0805 -0.0734 38  VAL   A O   
263  C CB  . VAL   A 39  ? 0.8897 0.7189 0.3859 0.1128  -0.0326 -0.0619 38  VAL   A CB  
264  C CG1 . VAL   A 39  ? 0.9094 0.7316 0.3797 0.1110  -0.0426 -0.0554 38  VAL   A CG1 
265  C CG2 . VAL   A 39  ? 0.9009 0.7306 0.3770 0.1210  -0.0160 -0.0684 38  VAL   A CG2 
266  N N   . SER   A 40  ? 0.8521 0.6844 0.4115 0.0982  -0.0623 -0.0579 39  SER   A N   
267  C CA  . SER   A 40  ? 0.8451 0.6785 0.4223 0.0916  -0.0771 -0.0525 39  SER   A CA  
268  C C   . SER   A 40  ? 0.8303 0.6592 0.4270 0.0883  -0.0901 -0.0612 39  SER   A C   
269  O O   . SER   A 40  ? 0.8340 0.6608 0.4379 0.0838  -0.1051 -0.0597 39  SER   A O   
270  C CB  . SER   A 40  ? 0.8541 0.7016 0.4571 0.0871  -0.0698 -0.0394 39  SER   A CB  
271  O OG  . SER   A 40  ? 0.8711 0.7270 0.5035 0.0856  -0.0624 -0.0409 39  SER   A OG  
272  N N   . GLY   A 41  ? 0.8106 0.6385 0.4174 0.0903  -0.0843 -0.0693 40  GLY   A N   
273  C CA  . GLY   A 41  ? 0.7932 0.6167 0.4197 0.0867  -0.0953 -0.0766 40  GLY   A CA  
274  C C   . GLY   A 41  ? 0.7621 0.5977 0.4256 0.0802  -0.0949 -0.0693 40  GLY   A C   
275  O O   . GLY   A 41  ? 0.7615 0.5948 0.4434 0.0762  -0.1033 -0.0737 40  GLY   A O   
276  N N   . ASP   A 42  ? 0.7331 0.5810 0.4073 0.0789  -0.0852 -0.0581 41  ASP   A N   
277  C CA  . ASP   A 42  ? 0.7052 0.5647 0.4124 0.0732  -0.0841 -0.0511 41  ASP   A CA  
278  C C   . ASP   A 42  ? 0.6733 0.5369 0.3995 0.0736  -0.0751 -0.0543 41  ASP   A C   
279  O O   . ASP   A 42  ? 0.6801 0.5427 0.3966 0.0789  -0.0644 -0.0578 41  ASP   A O   
280  C CB  . ASP   A 42  ? 0.7270 0.5967 0.4380 0.0721  -0.0768 -0.0388 41  ASP   A CB  
281  C CG  . ASP   A 42  ? 0.8002 0.6663 0.4951 0.0715  -0.0861 -0.0336 41  ASP   A CG  
282  O OD1 . ASP   A 42  ? 0.8168 0.6733 0.4982 0.0717  -0.0994 -0.0397 41  ASP   A OD1 
283  O OD2 . ASP   A 42  ? 0.8298 0.7020 0.5253 0.0708  -0.0807 -0.0234 41  ASP   A OD2 
284  N N   . LEU   A 43  ? 0.6366 0.5051 0.3899 0.0680  -0.0794 -0.0527 42  LEU   A N   
285  C CA  . LEU   A 43  ? 0.6074 0.4797 0.3795 0.0678  -0.0721 -0.0546 42  LEU   A CA  
286  C C   . LEU   A 43  ? 0.5628 0.4481 0.3470 0.0679  -0.0590 -0.0459 42  LEU   A C   
287  O O   . LEU   A 43  ? 0.5589 0.4514 0.3493 0.0649  -0.0589 -0.0375 42  LEU   A O   
288  C CB  . LEU   A 43  ? 0.6061 0.4789 0.4015 0.0613  -0.0814 -0.0555 42  LEU   A CB  
289  C CG  . LEU   A 43  ? 0.6318 0.4915 0.4207 0.0605  -0.0934 -0.0651 42  LEU   A CG  
290  C CD1 . LEU   A 43  ? 0.6319 0.4942 0.4450 0.0529  -0.1020 -0.0640 42  LEU   A CD1 
291  C CD2 . LEU   A 43  ? 0.6411 0.4919 0.4212 0.0658  -0.0882 -0.0734 42  LEU   A CD2 
292  N N   . VAL   A 44  ? 0.5311 0.4189 0.3192 0.0714  -0.0483 -0.0480 43  VAL   A N   
293  C CA  . VAL   A 44  ? 0.5022 0.4023 0.3034 0.0715  -0.0359 -0.0408 43  VAL   A CA  
294  C C   . VAL   A 44  ? 0.4792 0.3815 0.2985 0.0719  -0.0320 -0.0440 43  VAL   A C   
295  O O   . VAL   A 44  ? 0.4809 0.3741 0.2993 0.0730  -0.0377 -0.0518 43  VAL   A O   
296  C CB  . VAL   A 44  ? 0.5131 0.4160 0.2960 0.0771  -0.0244 -0.0390 43  VAL   A CB  
297  C CG1 . VAL   A 44  ? 0.5262 0.4263 0.2894 0.0767  -0.0279 -0.0346 43  VAL   A CG1 
298  C CG2 . VAL   A 44  ? 0.5250 0.4212 0.2943 0.0841  -0.0197 -0.0485 43  VAL   A CG2 
299  N N   . ALA   A 45  ? 0.4545 0.3682 0.2900 0.0709  -0.0229 -0.0379 44  ALA   A N   
300  C CA  . ALA   A 45  ? 0.4430 0.3594 0.2940 0.0720  -0.0187 -0.0401 44  ALA   A CA  
301  C C   . ALA   A 45  ? 0.4379 0.3612 0.2850 0.0778  -0.0057 -0.0395 44  ALA   A C   
302  O O   . ALA   A 45  ? 0.4385 0.3704 0.2847 0.0770  0.0012  -0.0326 44  ALA   A O   
303  C CB  . ALA   A 45  ? 0.4328 0.3577 0.3072 0.0657  -0.0196 -0.0337 44  ALA   A CB  
304  N N   . LEU   A 46  ? 0.4311 0.3504 0.2758 0.0837  -0.0024 -0.0466 45  LEU   A N   
305  C CA  . LEU   A 46  ? 0.4291 0.3565 0.2731 0.0897  0.0104  -0.0465 45  LEU   A CA  
306  C C   . LEU   A 46  ? 0.4101 0.3444 0.2774 0.0893  0.0131  -0.0452 45  LEU   A C   
307  O O   . LEU   A 46  ? 0.4150 0.3416 0.2885 0.0895  0.0066  -0.0500 45  LEU   A O   
308  C CB  . LEU   A 46  ? 0.4435 0.3622 0.2675 0.0981  0.0131  -0.0560 45  LEU   A CB  
309  C CG  . LEU   A 46  ? 0.4934 0.4079 0.2909 0.1003  0.0145  -0.0569 45  LEU   A CG  
310  C CD1 . LEU   A 46  ? 0.5189 0.4228 0.2964 0.1087  0.0157  -0.0681 45  LEU   A CD1 
311  C CD2 . LEU   A 46  ? 0.5037 0.4317 0.3004 0.1002  0.0266  -0.0483 45  LEU   A CD2 
312  N N   . LYS   A 47  ? 0.3940 0.3420 0.2738 0.0886  0.0221  -0.0386 46  LYS   A N   
313  C CA  . LYS   A 47  ? 0.3796 0.3351 0.2815 0.0881  0.0242  -0.0367 46  LYS   A CA  
314  C C   . LYS   A 47  ? 0.3895 0.3539 0.2948 0.0951  0.0355  -0.0383 46  LYS   A C   
315  O O   . LYS   A 47  ? 0.3956 0.3702 0.2994 0.0953  0.0446  -0.0335 46  LYS   A O   
316  C CB  . LYS   A 47  ? 0.3636 0.3285 0.2808 0.0804  0.0237  -0.0276 46  LYS   A CB  
317  C CG  . LYS   A 47  ? 0.3615 0.3350 0.3007 0.0792  0.0257  -0.0249 46  LYS   A CG  
318  C CD  . LYS   A 47  ? 0.3782 0.3578 0.3301 0.0712  0.0231  -0.0172 46  LYS   A CD  
319  C CE  . LYS   A 47  ? 0.4074 0.3937 0.3552 0.0686  0.0285  -0.0108 46  LYS   A CE  
320  N NZ  . LYS   A 47  ? 0.4316 0.4202 0.3889 0.0613  0.0240  -0.0049 46  LYS   A NZ  
321  N N   . MET   A 48  ? 0.3916 0.3523 0.3025 0.1008  0.0350  -0.0446 47  MET   A N   
322  C CA  . MET   A 48  ? 0.3993 0.3687 0.3161 0.1085  0.0451  -0.0472 47  MET   A CA  
323  C C   . MET   A 48  ? 0.3972 0.3799 0.3396 0.1061  0.0475  -0.0413 47  MET   A C   
324  O O   . MET   A 48  ? 0.3900 0.3687 0.3442 0.1033  0.0397  -0.0408 47  MET   A O   
325  C CB  . MET   A 48  ? 0.4203 0.3773 0.3300 0.1166  0.0421  -0.0578 47  MET   A CB  
326  C CG  . MET   A 48  ? 0.4539 0.4192 0.3682 0.1263  0.0529  -0.0620 47  MET   A CG  
327  S SD  . MET   A 48  ? 0.6069 0.5559 0.5165 0.1359  0.0476  -0.0744 47  MET   A SD  
328  C CE  . MET   A 48  ? 0.5694 0.5154 0.5022 0.1303  0.0367  -0.0701 47  MET   A CE  
329  N N   . VAL   A 49  ? 0.3993 0.3977 0.3498 0.1065  0.0581  -0.0362 48  VAL   A N   
330  C CA  . VAL   A 49  ? 0.3984 0.4107 0.3732 0.1040  0.0607  -0.0305 48  VAL   A CA  
331  C C   . VAL   A 49  ? 0.4145 0.4383 0.3988 0.1124  0.0708  -0.0333 48  VAL   A C   
332  O O   . VAL   A 49  ? 0.4058 0.4363 0.3815 0.1160  0.0813  -0.0336 48  VAL   A O   
333  C CB  . VAL   A 49  ? 0.3959 0.4178 0.3761 0.0956  0.0633  -0.0209 48  VAL   A CB  
334  C CG1 . VAL   A 49  ? 0.3878 0.4221 0.3929 0.0922  0.0635  -0.0158 48  VAL   A CG1 
335  C CG2 . VAL   A 49  ? 0.4051 0.4161 0.3748 0.0886  0.0542  -0.0187 48  VAL   A CG2 
336  N N   . LYS   A 50  ? 0.4278 0.4540 0.4295 0.1159  0.0678  -0.0354 49  LYS   A N   
337  C CA  . LYS   A 50  ? 0.4405 0.4788 0.4546 0.1245  0.0768  -0.0383 49  LYS   A CA  
338  C C   . LYS   A 50  ? 0.4444 0.5030 0.4757 0.1203  0.0852  -0.0302 49  LYS   A C   
339  O O   . LYS   A 50  ? 0.4456 0.5081 0.4886 0.1121  0.0801  -0.0234 49  LYS   A O   
340  C CB  . LYS   A 50  ? 0.4796 0.5137 0.5078 0.1295  0.0698  -0.0424 49  LYS   A CB  
341  C CG  . LYS   A 50  ? 0.5697 0.5847 0.5823 0.1363  0.0642  -0.0520 49  LYS   A CG  
342  C CD  . LYS   A 50  ? 0.6346 0.6428 0.6608 0.1397  0.0553  -0.0544 49  LYS   A CD  
343  C CE  . LYS   A 50  ? 0.6793 0.7028 0.7275 0.1470  0.0611  -0.0546 49  LYS   A CE  
344  N NZ  . LYS   A 50  ? 0.7145 0.7389 0.7573 0.1590  0.0699  -0.0632 49  LYS   A NZ  
345  N N   . MET   A 51  ? 0.4491 0.5206 0.4820 0.1257  0.0981  -0.0308 50  MET   A N   
346  C CA  . MET   A 51  ? 0.4457 0.5371 0.4956 0.1213  0.1069  -0.0227 50  MET   A CA  
347  C C   . MET   A 51  ? 0.4338 0.5413 0.5121 0.1253  0.1096  -0.0225 50  MET   A C   
348  O O   . MET   A 51  ? 0.4394 0.5458 0.5219 0.1350  0.1100  -0.0298 50  MET   A O   
349  C CB  . MET   A 51  ? 0.4538 0.5518 0.4892 0.1230  0.1205  -0.0216 50  MET   A CB  
350  C CG  . MET   A 51  ? 0.4810 0.5650 0.4896 0.1179  0.1175  -0.0199 50  MET   A CG  
351  S SD  . MET   A 51  ? 0.4958 0.5837 0.5115 0.1041  0.1140  -0.0077 50  MET   A SD  
352  C CE  . MET   A 51  ? 0.4705 0.5406 0.4837 0.0998  0.0964  -0.0099 50  MET   A CE  
353  N N   . GLU   A 52  ? 0.4224 0.5447 0.5207 0.1181  0.1111  -0.0144 51  GLU   A N   
354  C CA  . GLU   A 52  ? 0.4179 0.5584 0.5452 0.1211  0.1141  -0.0132 51  GLU   A CA  
355  C C   . GLU   A 52  ? 0.4165 0.5739 0.5471 0.1260  0.1307  -0.0131 51  GLU   A C   
356  O O   . GLU   A 52  ? 0.4179 0.5801 0.5404 0.1203  0.1387  -0.0073 51  GLU   A O   
357  C CB  . GLU   A 52  ? 0.4426 0.5920 0.5890 0.1105  0.1089  -0.0046 51  GLU   A CB  
358  C CG  . GLU   A 52  ? 0.4984 0.6354 0.6469 0.1065  0.0935  -0.0047 51  GLU   A CG  
359  C CD  . GLU   A 52  ? 0.5638 0.7040 0.7304 0.1131  0.0873  -0.0084 51  GLU   A CD  
360  O OE1 . GLU   A 52  ? 0.5542 0.7108 0.7392 0.1192  0.0945  -0.0094 51  GLU   A OE1 
361  O OE2 . GLU   A 52  ? 0.5979 0.7243 0.7604 0.1121  0.0752  -0.0100 51  GLU   A OE2 
362  N N   . PRO   A 53  ? 0.4076 0.5743 0.5506 0.1368  0.1363  -0.0190 52  PRO   A N   
363  C CA  . PRO   A 53  ? 0.4037 0.5879 0.5504 0.1423  0.1535  -0.0194 52  PRO   A CA  
364  C C   . PRO   A 53  ? 0.3969 0.6028 0.5634 0.1339  0.1621  -0.0093 52  PRO   A C   
365  O O   . PRO   A 53  ? 0.3962 0.6137 0.5585 0.1349  0.1770  -0.0073 52  PRO   A O   
366  C CB  . PRO   A 53  ? 0.4056 0.5965 0.5686 0.1552  0.1551  -0.0276 52  PRO   A CB  
367  C CG  . PRO   A 53  ? 0.4226 0.5922 0.5780 0.1578  0.1393  -0.0331 52  PRO   A CG  
368  C CD  . PRO   A 53  ? 0.4032 0.5640 0.5562 0.1451  0.1274  -0.0259 52  PRO   A CD  
369  N N   . ASP   A 54  ? 0.3957 0.6065 0.5826 0.1253  0.1530  -0.0030 53  ASP   A N   
370  C CA  . ASP   A 54  ? 0.3959 0.6262 0.6036 0.1163  0.1593  0.0066  53  ASP   A CA  
371  C C   . ASP   A 54  ? 0.4095 0.6336 0.5989 0.1059  0.1626  0.0142  53  ASP   A C   
372  O O   . ASP   A 54  ? 0.4093 0.6490 0.6100 0.1000  0.1726  0.0218  53  ASP   A O   
373  C CB  . ASP   A 54  ? 0.4049 0.6413 0.6397 0.1107  0.1473  0.0101  53  ASP   A CB  
374  C CG  . ASP   A 54  ? 0.4333 0.6856 0.6966 0.1190  0.1472  0.0063  53  ASP   A CG  
375  O OD1 . ASP   A 54  ? 0.4413 0.7017 0.7059 0.1298  0.1578  0.0007  53  ASP   A OD1 
376  O OD2 . ASP   A 54  ? 0.4418 0.6985 0.7259 0.1152  0.1365  0.0086  53  ASP   A OD2 
377  N N   . ASP   A 55  ? 0.4236 0.6254 0.5864 0.1035  0.1542  0.0126  54  ASP   A N   
378  C CA  . ASP   A 55  ? 0.4357 0.6292 0.5797 0.0945  0.1555  0.0194  54  ASP   A CA  
379  C C   . ASP   A 55  ? 0.4462 0.6424 0.5703 0.0984  0.1704  0.0195  54  ASP   A C   
380  O O   . ASP   A 55  ? 0.4592 0.6427 0.5594 0.1060  0.1708  0.0121  54  ASP   A O   
381  C CB  . ASP   A 55  ? 0.4699 0.6399 0.5935 0.0917  0.1414  0.0169  54  ASP   A CB  
382  C CG  . ASP   A 55  ? 0.5147 0.6813 0.6544 0.0862  0.1275  0.0181  54  ASP   A CG  
383  O OD1 . ASP   A 55  ? 0.5090 0.6906 0.6744 0.0818  0.1279  0.0228  54  ASP   A OD1 
384  O OD2 . ASP   A 55  ? 0.5433 0.6927 0.6700 0.0860  0.1162  0.0145  54  ASP   A OD2 
385  N N   . ASP   A 56  ? 0.4318 0.6441 0.5652 0.0931  0.1826  0.0279  55  ASP   A N   
386  C CA  . ASP   A 56  ? 0.4422 0.6582 0.5562 0.0961  0.1979  0.0293  55  ASP   A CA  
387  C C   . ASP   A 56  ? 0.4520 0.6473 0.5314 0.0924  0.1941  0.0313  55  ASP   A C   
388  O O   . ASP   A 56  ? 0.4553 0.6365 0.5306 0.0859  0.1807  0.0334  55  ASP   A O   
389  C CB  . ASP   A 56  ? 0.4613 0.7010 0.5959 0.0909  0.2125  0.0386  55  ASP   A CB  
390  C CG  . ASP   A 56  ? 0.5289 0.7709 0.6759 0.0769  0.2088  0.0503  55  ASP   A CG  
391  O OD1 . ASP   A 56  ? 0.5435 0.7672 0.6727 0.0708  0.1991  0.0532  55  ASP   A OD1 
392  O OD2 . ASP   A 56  ? 0.5638 0.8262 0.7390 0.0721  0.2156  0.0565  55  ASP   A OD2 
393  N N   . VAL   A 57  ? 0.4547 0.6482 0.5090 0.0967  0.2055  0.0305  56  VAL   A N   
394  C CA  . VAL   A 57  ? 0.4721 0.6460 0.4929 0.0940  0.2011  0.0321  56  VAL   A CA  
395  C C   . VAL   A 57  ? 0.4728 0.6448 0.4961 0.0811  0.1981  0.0448  56  VAL   A C   
396  O O   . VAL   A 57  ? 0.4885 0.6426 0.4917 0.0777  0.1884  0.0460  56  VAL   A O   
397  C CB  . VAL   A 57  ? 0.4939 0.6640 0.4835 0.1016  0.2125  0.0281  56  VAL   A CB  
398  C CG1 . VAL   A 57  ? 0.4920 0.6699 0.4857 0.1145  0.2199  0.0168  56  VAL   A CG1 
399  C CG2 . VAL   A 57  ? 0.5019 0.6819 0.4839 0.0960  0.2269  0.0392  56  VAL   A CG2 
400  N N   . SER   A 58  ? 0.4578 0.6474 0.5064 0.0741  0.2052  0.0538  57  SER   A N   
401  C CA  . SER   A 58  ? 0.4646 0.6510 0.5175 0.0617  0.2013  0.0654  57  SER   A CA  
402  C C   . SER   A 58  ? 0.4685 0.6429 0.5311 0.0574  0.1832  0.0634  57  SER   A C   
403  O O   . SER   A 58  ? 0.4776 0.6379 0.5287 0.0510  0.1750  0.0681  57  SER   A O   
404  C CB  . SER   A 58  ? 0.4745 0.6825 0.5549 0.0550  0.2123  0.0747  57  SER   A CB  
405  O OG  . SER   A 58  ? 0.5238 0.7405 0.5916 0.0550  0.2291  0.0808  57  SER   A OG  
406  N N   . THR   A 59  ? 0.4571 0.6373 0.5405 0.0614  0.1773  0.0563  58  THR   A N   
407  C CA  . THR   A 59  ? 0.4635 0.6335 0.5559 0.0583  0.1611  0.0535  58  THR   A CA  
408  C C   . THR   A 59  ? 0.4737 0.6220 0.5386 0.0617  0.1512  0.0476  58  THR   A C   
409  O O   . THR   A 59  ? 0.4835 0.6193 0.5439 0.0558  0.1405  0.0499  58  THR   A O   
410  C CB  . THR   A 59  ? 0.4756 0.6570 0.5935 0.0632  0.1583  0.0473  58  THR   A CB  
411  O OG1 . THR   A 59  ? 0.4765 0.6797 0.6205 0.0602  0.1681  0.0529  58  THR   A OG1 
412  C CG2 . THR   A 59  ? 0.4826 0.6547 0.6099 0.0598  0.1423  0.0449  58  THR   A CG2 
413  N N   . LEU   A 60  ? 0.4686 0.6125 0.5151 0.0712  0.1552  0.0399  59  LEU   A N   
414  C CA  . LEU   A 60  ? 0.4778 0.6018 0.4979 0.0747  0.1464  0.0338  59  LEU   A CA  
415  C C   . LEU   A 60  ? 0.4769 0.5901 0.4748 0.0689  0.1456  0.0407  59  LEU   A C   
416  O O   . LEU   A 60  ? 0.4830 0.5813 0.4709 0.0662  0.1339  0.0399  59  LEU   A O   
417  C CB  . LEU   A 60  ? 0.4897 0.6121 0.4950 0.0860  0.1521  0.0240  59  LEU   A CB  
418  C CG  . LEU   A 60  ? 0.5332 0.6353 0.5124 0.0900  0.1425  0.0166  59  LEU   A CG  
419  C CD1 . LEU   A 60  ? 0.5463 0.6388 0.5356 0.0884  0.1275  0.0125  59  LEU   A CD1 
420  C CD2 . LEU   A 60  ? 0.5508 0.6511 0.5149 0.1010  0.1489  0.0070  59  LEU   A CD2 
421  N N   . GLN   A 61  ? 0.4636 0.5846 0.4547 0.0670  0.1582  0.0480  60  GLN   A N   
422  C CA  . GLN   A 61  ? 0.4711 0.5821 0.4411 0.0616  0.1578  0.0558  60  GLN   A CA  
423  C C   . GLN   A 61  ? 0.4596 0.5659 0.4422 0.0517  0.1483  0.0633  60  GLN   A C   
424  O O   . GLN   A 61  ? 0.4619 0.5537 0.4280 0.0488  0.1405  0.0660  60  GLN   A O   
425  C CB  . GLN   A 61  ? 0.4965 0.6184 0.4594 0.0606  0.1741  0.0635  60  GLN   A CB  
426  C CG  . GLN   A 61  ? 0.5680 0.6878 0.5049 0.0700  0.1824  0.0569  60  GLN   A CG  
427  C CD  . GLN   A 61  ? 0.6662 0.7749 0.5717 0.0679  0.1845  0.0632  60  GLN   A CD  
428  O OE1 . GLN   A 61  ? 0.7064 0.7978 0.5952 0.0663  0.1721  0.0627  60  GLN   A OE1 
429  N NE2 . GLN   A 61  ? 0.6713 0.7900 0.5681 0.0679  0.2002  0.0692  60  GLN   A NE2 
430  N N   . LYS   A 62  ? 0.4468 0.5652 0.4586 0.0468  0.1489  0.0666  61  LYS   A N   
431  C CA  . LYS   A 62  ? 0.4569 0.5707 0.4818 0.0377  0.1399  0.0727  61  LYS   A CA  
432  C C   . LYS   A 62  ? 0.4621 0.5612 0.4826 0.0387  0.1246  0.0661  61  LYS   A C   
433  O O   . LYS   A 62  ? 0.4606 0.5492 0.4777 0.0333  0.1166  0.0701  61  LYS   A O   
434  C CB  . LYS   A 62  ? 0.4800 0.6098 0.5373 0.0329  0.1426  0.0757  61  LYS   A CB  
435  C CG  . LYS   A 62  ? 0.5418 0.6847 0.6073 0.0274  0.1556  0.0860  61  LYS   A CG  
436  C CD  . LYS   A 62  ? 0.5948 0.7551 0.6942 0.0231  0.1579  0.0881  61  LYS   A CD  
437  C CE  . LYS   A 62  ? 0.6398 0.8159 0.7488 0.0185  0.1727  0.0975  61  LYS   A CE  
438  N NZ  . LYS   A 62  ? 0.6574 0.8516 0.8014 0.0143  0.1743  0.0990  61  LYS   A NZ  
439  N N   . GLU   A 63  ? 0.4615 0.5599 0.4825 0.0458  0.1210  0.0561  62  GLU   A N   
440  C CA  . GLU   A 63  ? 0.4704 0.5560 0.4879 0.0469  0.1076  0.0497  62  GLU   A CA  
441  C C   . GLU   A 63  ? 0.4867 0.5569 0.4766 0.0496  0.1028  0.0473  62  GLU   A C   
442  O O   . GLU   A 63  ? 0.4927 0.5520 0.4791 0.0466  0.0924  0.0471  62  GLU   A O   
443  C CB  . GLU   A 63  ? 0.4914 0.5818 0.5215 0.0526  0.1051  0.0412  62  GLU   A CB  
444  C CG  . GLU   A 63  ? 0.5322 0.6377 0.5907 0.0494  0.1076  0.0439  62  GLU   A CG  
445  C CD  . GLU   A 63  ? 0.6169 0.7204 0.6890 0.0407  0.0997  0.0488  62  GLU   A CD  
446  O OE1 . GLU   A 63  ? 0.6348 0.7479 0.7215 0.0348  0.1045  0.0558  62  GLU   A OE1 
447  O OE2 . GLU   A 63  ? 0.6421 0.7344 0.7104 0.0398  0.0889  0.0453  62  GLU   A OE2 
448  N N   . ILE   A 64  ? 0.4881 0.5577 0.4584 0.0550  0.1105  0.0458  63  ILE   A N   
449  C CA  . ILE   A 64  ? 0.5046 0.5595 0.4474 0.0573  0.1055  0.0437  63  ILE   A CA  
450  C C   . ILE   A 64  ? 0.5037 0.5526 0.4386 0.0505  0.1034  0.0535  63  ILE   A C   
451  O O   . ILE   A 64  ? 0.5203 0.5563 0.4428 0.0497  0.0934  0.0528  63  ILE   A O   
452  C CB  . ILE   A 64  ? 0.5281 0.5826 0.4498 0.0655  0.1136  0.0381  63  ILE   A CB  
453  C CG1 . ILE   A 64  ? 0.5503 0.5995 0.4709 0.0726  0.1078  0.0262  63  ILE   A CG1 
454  C CG2 . ILE   A 64  ? 0.5496 0.5926 0.4416 0.0657  0.1127  0.0409  63  ILE   A CG2 
455  C CD1 . ILE   A 64  ? 0.5615 0.6215 0.5071 0.0744  0.1096  0.0228  63  ILE   A CD1 
456  N N   . LEU   A 65  ? 0.4791 0.5373 0.4235 0.0453  0.1121  0.0630  64  LEU   A N   
457  C CA  . LEU   A 65  ? 0.4771 0.5288 0.4161 0.0386  0.1098  0.0730  64  LEU   A CA  
458  C C   . LEU   A 65  ? 0.4718 0.5164 0.4244 0.0340  0.0970  0.0728  64  LEU   A C   
459  O O   . LEU   A 65  ? 0.4776 0.5104 0.4189 0.0321  0.0892  0.0756  64  LEU   A O   
460  C CB  . LEU   A 65  ? 0.4721 0.5353 0.4218 0.0332  0.1215  0.0832  64  LEU   A CB  
461  C CG  . LEU   A 65  ? 0.4965 0.5520 0.4420 0.0257  0.1190  0.0946  64  LEU   A CG  
462  C CD1 . LEU   A 65  ? 0.5180 0.5610 0.4319 0.0283  0.1177  0.0972  64  LEU   A CD1 
463  C CD2 . LEU   A 65  ? 0.4974 0.5647 0.4581 0.0192  0.1299  0.1046  64  LEU   A CD2 
464  N N   . ILE   A 66  ? 0.4563 0.5079 0.4320 0.0329  0.0945  0.0688  65  ILE   A N   
465  C CA  . ILE   A 66  ? 0.4608 0.5064 0.4487 0.0292  0.0831  0.0673  65  ILE   A CA  
466  C C   . ILE   A 66  ? 0.4834 0.5173 0.4571 0.0334  0.0733  0.0601  65  ILE   A C   
467  O O   . ILE   A 66  ? 0.4956 0.5200 0.4652 0.0309  0.0651  0.0619  65  ILE   A O   
468  C CB  . ILE   A 66  ? 0.4538 0.5097 0.4671 0.0276  0.0829  0.0643  65  ILE   A CB  
469  C CG1 . ILE   A 66  ? 0.4520 0.5182 0.4823 0.0214  0.0898  0.0724  65  ILE   A CG1 
470  C CG2 . ILE   A 66  ? 0.4630 0.5121 0.4846 0.0258  0.0711  0.0599  65  ILE   A CG2 
471  C CD1 . ILE   A 66  ? 0.4543 0.5335 0.5084 0.0210  0.0915  0.0693  65  ILE   A CD1 
472  N N   . LEU   A 67  ? 0.4893 0.5235 0.4553 0.0398  0.0741  0.0520  66  LEU   A N   
473  C CA  . LEU   A 67  ? 0.5117 0.5351 0.4647 0.0435  0.0650  0.0448  66  LEU   A CA  
474  C C   . LEU   A 67  ? 0.5233 0.5359 0.4559 0.0430  0.0606  0.0483  66  LEU   A C   
475  O O   . LEU   A 67  ? 0.5338 0.5377 0.4631 0.0426  0.0504  0.0456  66  LEU   A O   
476  C CB  . LEU   A 67  ? 0.5229 0.5476 0.4676 0.0507  0.0686  0.0367  66  LEU   A CB  
477  C CG  . LEU   A 67  ? 0.5489 0.5734 0.5052 0.0530  0.0629  0.0288  66  LEU   A CG  
478  C CD1 . LEU   A 67  ? 0.5590 0.5839 0.5070 0.0605  0.0671  0.0212  66  LEU   A CD1 
479  C CD2 . LEU   A 67  ? 0.5672 0.5808 0.5201 0.0512  0.0508  0.0258  66  LEU   A CD2 
480  N N   . LYS   A 68  ? 0.5197 0.5333 0.4395 0.0428  0.0683  0.0548  67  LYS   A N   
481  C CA  . LYS   A 68  ? 0.5259 0.5296 0.4243 0.0426  0.0650  0.0594  67  LYS   A CA  
482  C C   . LYS   A 68  ? 0.5148 0.5142 0.4203 0.0364  0.0601  0.0681  67  LYS   A C   
483  O O   . LYS   A 68  ? 0.5240 0.5132 0.4179 0.0365  0.0515  0.0694  67  LYS   A O   
484  C CB  . LYS   A 68  ? 0.5615 0.5684 0.4422 0.0449  0.0765  0.0634  67  LYS   A CB  
485  C CG  . LYS   A 68  ? 0.6334 0.6290 0.4854 0.0470  0.0730  0.0655  67  LYS   A CG  
486  C CD  . LYS   A 68  ? 0.6965 0.6962 0.5312 0.0485  0.0858  0.0708  67  LYS   A CD  
487  C CE  . LYS   A 68  ? 0.7624 0.7503 0.5670 0.0500  0.0819  0.0742  67  LYS   A CE  
488  N NZ  . LYS   A 68  ? 0.7915 0.7833 0.5789 0.0502  0.0953  0.0815  67  LYS   A NZ  
489  N N   . THR   A 69  ? 0.4900 0.4969 0.4144 0.0313  0.0652  0.0740  68  THR   A N   
490  C CA  . THR   A 69  ? 0.4874 0.4890 0.4184 0.0256  0.0608  0.0821  68  THR   A CA  
491  C C   . THR   A 69  ? 0.4686 0.4675 0.4170 0.0237  0.0508  0.0779  68  THR   A C   
492  O O   . THR   A 69  ? 0.4767 0.4678 0.4261 0.0212  0.0440  0.0819  68  THR   A O   
493  C CB  . THR   A 69  ? 0.5020 0.5108 0.4425 0.0203  0.0706  0.0916  68  THR   A CB  
494  O OG1 . THR   A 69  ? 0.5100 0.5309 0.4719 0.0192  0.0754  0.0880  68  THR   A OG1 
495  C CG2 . THR   A 69  ? 0.5122 0.5225 0.4331 0.0216  0.0807  0.0976  68  THR   A CG2 
496  N N   . CYS   A 70  ? 0.4433 0.4482 0.4047 0.0251  0.0500  0.0701  69  CYS   A N   
497  C CA  . CYS   A 70  ? 0.4302 0.4331 0.4064 0.0234  0.0414  0.0657  69  CYS   A CA  
498  C C   . CYS   A 70  ? 0.4285 0.4232 0.3923 0.0271  0.0328  0.0602  69  CYS   A C   
499  O O   . CYS   A 70  ? 0.4340 0.4302 0.3966 0.0304  0.0313  0.0527  69  CYS   A O   
500  C CB  . CYS   A 70  ? 0.4296 0.4418 0.4221 0.0234  0.0439  0.0602  69  CYS   A CB  
501  S SG  . CYS   A 70  ? 0.4541 0.4654 0.4659 0.0200  0.0358  0.0566  69  CYS   A SG  
502  N N   . ARG   A 71  ? 0.4217 0.4078 0.3765 0.0266  0.0269  0.0643  70  ARG   A N   
503  C CA  . ARG   A 71  ? 0.4242 0.4026 0.3665 0.0298  0.0182  0.0606  70  ARG   A CA  
504  C C   . ARG   A 71  ? 0.3858 0.3593 0.3378 0.0282  0.0089  0.0606  70  ARG   A C   
505  O O   . ARG   A 71  ? 0.3883 0.3588 0.3449 0.0255  0.0082  0.0672  70  ARG   A O   
506  C CB  . ARG   A 71  ? 0.4730 0.4451 0.3933 0.0315  0.0191  0.0664  70  ARG   A CB  
507  C CG  . ARG   A 71  ? 0.5527 0.5245 0.4541 0.0360  0.0220  0.0619  70  ARG   A CG  
508  C CD  . ARG   A 71  ? 0.6386 0.6019 0.5164 0.0379  0.0189  0.0664  70  ARG   A CD  
509  N NE  . ARG   A 71  ? 0.7084 0.6720 0.5789 0.0356  0.0269  0.0766  70  ARG   A NE  
510  C CZ  . ARG   A 71  ? 0.7583 0.7157 0.6275 0.0328  0.0235  0.0855  70  ARG   A CZ  
511  N NH1 . ARG   A 71  ? 0.7696 0.7272 0.6321 0.0301  0.0315  0.0953  70  ARG   A NH1 
512  N NH2 . ARG   A 71  ? 0.7653 0.7165 0.6408 0.0325  0.0122  0.0851  70  ARG   A NH2 
513  N N   . HIS   A 72  ? 0.3512 0.3232 0.3046 0.0301  0.0016  0.0537  71  HIS   A N   
514  C CA  . HIS   A 72  ? 0.3148 0.2838 0.2781 0.0292  -0.0066 0.0531  71  HIS   A CA  
515  C C   . HIS   A 72  ? 0.2995 0.2665 0.2580 0.0318  -0.0143 0.0467  71  HIS   A C   
516  O O   . HIS   A 72  ? 0.2937 0.2628 0.2481 0.0332  -0.0129 0.0411  71  HIS   A O   
517  C CB  . HIS   A 72  ? 0.2992 0.2732 0.2827 0.0263  -0.0051 0.0508  71  HIS   A CB  
518  C CG  . HIS   A 72  ? 0.2921 0.2633 0.2862 0.0257  -0.0119 0.0505  71  HIS   A CG  
519  N ND1 . HIS   A 72  ? 0.2949 0.2674 0.2946 0.0268  -0.0177 0.0443  71  HIS   A ND1 
520  C CD2 . HIS   A 72  ? 0.2918 0.2589 0.2918 0.0243  -0.0136 0.0557  71  HIS   A CD2 
521  C CE1 . HIS   A 72  ? 0.2939 0.2642 0.3029 0.0265  -0.0221 0.0455  71  HIS   A CE1 
522  N NE2 . HIS   A 72  ? 0.2919 0.2583 0.3016 0.0252  -0.0201 0.0520  71  HIS   A NE2 
523  N N   . ALA   A 73  ? 0.2851 0.2481 0.2455 0.0324  -0.0226 0.0475  72  ALA   A N   
524  C CA  . ALA   A 73  ? 0.2844 0.2464 0.2427 0.0341  -0.0307 0.0418  72  ALA   A CA  
525  C C   . ALA   A 73  ? 0.2763 0.2439 0.2468 0.0329  -0.0302 0.0344  72  ALA   A C   
526  O O   . ALA   A 73  ? 0.2986 0.2654 0.2650 0.0339  -0.0348 0.0294  72  ALA   A O   
527  C CB  . ALA   A 73  ? 0.2881 0.2472 0.2517 0.0348  -0.0394 0.0441  72  ALA   A CB  
528  N N   . ASN   A 74  ? 0.2410 0.2134 0.2258 0.0306  -0.0255 0.0340  73  ASN   A N   
529  C CA  . ASN   A 74  ? 0.2247 0.2018 0.2199 0.0293  -0.0249 0.0280  73  ASN   A CA  
530  C C   . ASN   A 74  ? 0.2324 0.2119 0.2249 0.0292  -0.0183 0.0259  73  ASN   A C   
531  O O   . ASN   A 74  ? 0.2183 0.2017 0.2206 0.0277  -0.0166 0.0227  73  ASN   A O   
532  C CB  . ASN   A 74  ? 0.2134 0.1940 0.2255 0.0271  -0.0250 0.0277  73  ASN   A CB  
533  C CG  . ASN   A 74  ? 0.2297 0.2091 0.2470 0.0279  -0.0320 0.0279  73  ASN   A CG  
534  O OD1 . ASN   A 74  ? 0.2343 0.2117 0.2562 0.0283  -0.0330 0.0317  73  ASN   A OD1 
535  N ND2 . ASN   A 74  ? 0.2261 0.2065 0.2433 0.0284  -0.0374 0.0239  73  ASN   A ND2 
536  N N   . ILE   A 75  ? 0.2446 0.2223 0.2240 0.0312  -0.0143 0.0279  74  ILE   A N   
537  C CA  . ILE   A 75  ? 0.2663 0.2466 0.2428 0.0323  -0.0080 0.0256  74  ILE   A CA  
538  C C   . ILE   A 75  ? 0.2954 0.2708 0.2542 0.0358  -0.0095 0.0231  74  ILE   A C   
539  O O   . ILE   A 75  ? 0.3069 0.2782 0.2533 0.0371  -0.0109 0.0266  74  ILE   A O   
540  C CB  . ILE   A 75  ? 0.2773 0.2620 0.2572 0.0314  0.0002  0.0305  74  ILE   A CB  
541  C CG1 . ILE   A 75  ? 0.2861 0.2744 0.2829 0.0277  0.0005  0.0323  74  ILE   A CG1 
542  C CG2 . ILE   A 75  ? 0.2943 0.2830 0.2720 0.0335  0.0068  0.0280  74  ILE   A CG2 
543  C CD1 . ILE   A 75  ? 0.3031 0.2945 0.3039 0.0258  0.0068  0.0382  74  ILE   A CD1 
544  N N   . VAL   A 76  ? 0.2979 0.2726 0.2540 0.0376  -0.0093 0.0171  75  VAL   A N   
545  C CA  . VAL   A 76  ? 0.3335 0.3023 0.2722 0.0413  -0.0110 0.0133  75  VAL   A CA  
546  C C   . VAL   A 76  ? 0.3553 0.3240 0.2800 0.0439  -0.0041 0.0171  75  VAL   A C   
547  O O   . VAL   A 76  ? 0.3551 0.3299 0.2853 0.0439  0.0043  0.0197  75  VAL   A O   
548  C CB  . VAL   A 76  ? 0.3532 0.3208 0.2931 0.0430  -0.0109 0.0064  75  VAL   A CB  
549  C CG1 . VAL   A 76  ? 0.3806 0.3413 0.3016 0.0474  -0.0116 0.0018  75  VAL   A CG1 
550  C CG2 . VAL   A 76  ? 0.3555 0.3220 0.3066 0.0399  -0.0181 0.0033  75  VAL   A CG2 
551  N N   . ALA   A 77  ? 0.3798 0.3425 0.2878 0.0455  -0.0078 0.0184  76  ALA   A N   
552  C CA  . ALA   A 77  ? 0.4089 0.3709 0.3010 0.0475  -0.0015 0.0231  76  ALA   A CA  
553  C C   . ALA   A 77  ? 0.4292 0.3924 0.3112 0.0518  0.0065  0.0189  76  ALA   A C   
554  O O   . ALA   A 77  ? 0.4288 0.3883 0.3066 0.0545  0.0037  0.0112  76  ALA   A O   
555  C CB  . ALA   A 77  ? 0.4258 0.3799 0.3005 0.0485  -0.0090 0.0249  76  ALA   A CB  
556  N N   . TYR   A 78  ? 0.4412 0.4096 0.3200 0.0523  0.0167  0.0242  77  TYR   A N   
557  C CA  . TYR   A 78  ? 0.4621 0.4336 0.3315 0.0567  0.0263  0.0214  77  TYR   A CA  
558  C C   . TYR   A 78  ? 0.4806 0.4450 0.3225 0.0599  0.0266  0.0222  77  TYR   A C   
559  O O   . TYR   A 78  ? 0.4801 0.4419 0.3142 0.0575  0.0250  0.0296  77  TYR   A O   
560  C CB  . TYR   A 78  ? 0.4629 0.4456 0.3462 0.0548  0.0373  0.0275  77  TYR   A CB  
561  C CG  . TYR   A 78  ? 0.4808 0.4686 0.3538 0.0590  0.0491  0.0272  77  TYR   A CG  
562  C CD1 . TYR   A 78  ? 0.4951 0.4870 0.3726 0.0637  0.0537  0.0199  77  TYR   A CD1 
563  C CD2 . TYR   A 78  ? 0.4987 0.4876 0.3582 0.0584  0.0562  0.0346  77  TYR   A CD2 
564  C CE1 . TYR   A 78  ? 0.5080 0.5058 0.3774 0.0682  0.0654  0.0192  77  TYR   A CE1 
565  C CE2 . TYR   A 78  ? 0.5132 0.5081 0.3632 0.0623  0.0682  0.0344  77  TYR   A CE2 
566  C CZ  . TYR   A 78  ? 0.5270 0.5269 0.3827 0.0675  0.0731  0.0264  77  TYR   A CZ  
567  O OH  . TYR   A 78  ? 0.5516 0.5587 0.3993 0.0720  0.0858  0.0257  77  TYR   A OH  
568  N N   . HIS   A 79  ? 0.4928 0.4533 0.3191 0.0654  0.0284  0.0145  78  HIS   A N   
569  C CA  . HIS   A 79  ? 0.5231 0.4760 0.3206 0.0688  0.0283  0.0140  78  HIS   A CA  
570  C C   . HIS   A 79  ? 0.5288 0.4869 0.3138 0.0732  0.0423  0.0143  78  HIS   A C   
571  O O   . HIS   A 79  ? 0.5488 0.5042 0.3126 0.0741  0.0459  0.0189  78  HIS   A O   
572  C CB  . HIS   A 79  ? 0.5527 0.4944 0.3372 0.0720  0.0175  0.0040  78  HIS   A CB  
573  C CG  . HIS   A 79  ? 0.6044 0.5409 0.3974 0.0678  0.0035  0.0040  78  HIS   A CG  
574  N ND1 . HIS   A 79  ? 0.6343 0.5725 0.4343 0.0632  -0.0001 0.0129  78  HIS   A ND1 
575  C CD2 . HIS   A 79  ? 0.6266 0.5566 0.4223 0.0678  -0.0071 -0.0037 78  HIS   A CD2 
576  C CE1 . HIS   A 79  ? 0.6446 0.5784 0.4521 0.0610  -0.0124 0.0100  78  HIS   A CE1 
577  N NE2 . HIS   A 79  ? 0.6445 0.5737 0.4501 0.0632  -0.0169 0.0004  78  HIS   A NE2 
578  N N   . GLY   A 80  ? 0.5128 0.4783 0.3106 0.0760  0.0499  0.0096  79  GLY   A N   
579  C CA  . GLY   A 80  ? 0.5105 0.4830 0.2998 0.0809  0.0641  0.0088  79  GLY   A CA  
580  C C   . GLY   A 80  ? 0.4985 0.4783 0.3051 0.0848  0.0695  0.0019  79  GLY   A C   
581  O O   . GLY   A 80  ? 0.4824 0.4597 0.3045 0.0839  0.0614  -0.0028 79  GLY   A O   
582  N N   . SER   A 81  ? 0.4997 0.4890 0.3050 0.0892  0.0834  0.0016  80  SER   A N   
583  C CA  . SER   A 81  ? 0.4985 0.4955 0.3213 0.0939  0.0887  -0.0049 80  SER   A CA  
584  C C   . SER   A 81  ? 0.5056 0.5051 0.3136 0.1027  0.0999  -0.0115 80  SER   A C   
585  O O   . SER   A 81  ? 0.5196 0.5195 0.3066 0.1042  0.1077  -0.0087 80  SER   A O   
586  C CB  . SER   A 81  ? 0.5099 0.5217 0.3622 0.0892  0.0940  0.0024  80  SER   A CB  
587  O OG  . SER   A 81  ? 0.5513 0.5739 0.4026 0.0869  0.1061  0.0113  80  SER   A OG  
588  N N   . TYR   A 82  ? 0.4978 0.4978 0.3155 0.1088  0.1003  -0.0208 81  TYR   A N   
589  C CA  . TYR   A 82  ? 0.5102 0.5120 0.3164 0.1186  0.1103  -0.0292 81  TYR   A CA  
590  C C   . TYR   A 82  ? 0.5136 0.5290 0.3469 0.1222  0.1175  -0.0310 81  TYR   A C   
591  O O   . TYR   A 82  ? 0.5058 0.5202 0.3595 0.1204  0.1092  -0.0324 81  TYR   A O   
592  C CB  . TYR   A 82  ? 0.5185 0.5022 0.3054 0.1243  0.1004  -0.0415 81  TYR   A CB  
593  C CG  . TYR   A 82  ? 0.5375 0.5074 0.2967 0.1214  0.0922  -0.0407 81  TYR   A CG  
594  C CD1 . TYR   A 82  ? 0.5466 0.5097 0.3105 0.1134  0.0788  -0.0359 81  TYR   A CD1 
595  C CD2 . TYR   A 82  ? 0.5595 0.5241 0.2881 0.1268  0.0979  -0.0445 81  TYR   A CD2 
596  C CE1 . TYR   A 82  ? 0.5700 0.5220 0.3104 0.1108  0.0709  -0.0343 81  TYR   A CE1 
597  C CE2 . TYR   A 82  ? 0.5816 0.5338 0.2844 0.1240  0.0895  -0.0432 81  TYR   A CE2 
598  C CZ  . TYR   A 82  ? 0.5932 0.5395 0.3030 0.1160  0.0757  -0.0378 81  TYR   A CZ  
599  O OH  . TYR   A 82  ? 0.6294 0.5643 0.3155 0.1136  0.0667  -0.0362 81  TYR   A OH  
600  N N   . LEU   A 83  ? 0.5166 0.5449 0.3499 0.1276  0.1329  -0.0311 82  LEU   A N   
601  C CA  . LEU   A 83  ? 0.5224 0.5646 0.3813 0.1325  0.1402  -0.0338 82  LEU   A CA  
602  C C   . LEU   A 83  ? 0.5486 0.5836 0.3934 0.1444  0.1430  -0.0471 82  LEU   A C   
603  O O   . LEU   A 83  ? 0.5537 0.5885 0.3757 0.1497  0.1529  -0.0502 82  LEU   A O   
604  C CB  . LEU   A 83  ? 0.5197 0.5831 0.3911 0.1306  0.1562  -0.0248 82  LEU   A CB  
605  C CG  . LEU   A 83  ? 0.5314 0.6123 0.4332 0.1350  0.1637  -0.0263 82  LEU   A CG  
606  C CD1 . LEU   A 83  ? 0.5292 0.6092 0.4574 0.1307  0.1511  -0.0254 82  LEU   A CD1 
607  C CD2 . LEU   A 83  ? 0.5361 0.6383 0.4509 0.1314  0.1789  -0.0165 82  LEU   A CD2 
608  N N   . TRP   A 84  ? 0.5581 0.5851 0.4141 0.1485  0.1338  -0.0553 83  TRP   A N   
609  C CA  . TRP   A 84  ? 0.5829 0.6001 0.4260 0.1599  0.1347  -0.0687 83  TRP   A CA  
610  C C   . TRP   A 84  ? 0.5789 0.5987 0.4477 0.1653  0.1317  -0.0741 83  TRP   A C   
611  O O   . TRP   A 84  ? 0.5739 0.5873 0.4568 0.1601  0.1191  -0.0722 83  TRP   A O   
612  C CB  . TRP   A 84  ? 0.6051 0.5989 0.4210 0.1593  0.1217  -0.0754 83  TRP   A CB  
613  C CG  . TRP   A 84  ? 0.6278 0.6082 0.4276 0.1704  0.1210  -0.0899 83  TRP   A CG  
614  C CD1 . TRP   A 84  ? 0.6466 0.6117 0.4503 0.1736  0.1090  -0.0987 83  TRP   A CD1 
615  C CD2 . TRP   A 84  ? 0.6421 0.6220 0.4179 0.1797  0.1325  -0.0975 83  TRP   A CD2 
616  N NE1 . TRP   A 84  ? 0.6631 0.6175 0.4475 0.1844  0.1118  -0.1118 83  TRP   A NE1 
617  C CE2 . TRP   A 84  ? 0.6620 0.6254 0.4286 0.1887  0.1263  -0.1117 83  TRP   A CE2 
618  C CE3 . TRP   A 84  ? 0.6504 0.6422 0.4116 0.1814  0.1479  -0.0936 83  TRP   A CE3 
619  C CZ2 . TRP   A 84  ? 0.6807 0.6386 0.4231 0.1996  0.1347  -0.1229 83  TRP   A CZ2 
620  C CZ3 . TRP   A 84  ? 0.6725 0.6595 0.4087 0.1919  0.1566  -0.1042 83  TRP   A CZ3 
621  C CH2 . TRP   A 84  ? 0.6840 0.6542 0.4109 0.2012  0.1501  -0.1191 83  TRP   A CH2 
622  N N   . LEU   A 85  ? 0.5760 0.6053 0.4508 0.1760  0.1434  -0.0805 84  LEU   A N   
623  C CA  . LEU   A 85  ? 0.5783 0.6107 0.4772 0.1831  0.1415  -0.0862 84  LEU   A CA  
624  C C   . LEU   A 85  ? 0.5655 0.6099 0.4969 0.1756  0.1367  -0.0765 84  LEU   A C   
625  O O   . LEU   A 85  ? 0.5659 0.6014 0.5096 0.1752  0.1247  -0.0786 84  LEU   A O   
626  C CB  . LEU   A 85  ? 0.5974 0.6058 0.4842 0.1885  0.1286  -0.0977 84  LEU   A CB  
627  C CG  . LEU   A 85  ? 0.6385 0.6318 0.4919 0.1959  0.1308  -0.1087 84  LEU   A CG  
628  C CD1 . LEU   A 85  ? 0.6557 0.6245 0.5004 0.1991  0.1159  -0.1190 84  LEU   A CD1 
629  C CD2 . LEU   A 85  ? 0.6451 0.6507 0.4963 0.2080  0.1479  -0.1152 84  LEU   A CD2 
630  N N   . GLN   A 86  ? 0.5537 0.6179 0.4983 0.1694  0.1458  -0.0659 85  GLN   A N   
631  C CA  . GLN   A 86  ? 0.5430 0.6195 0.5175 0.1616  0.1417  -0.0566 85  GLN   A CA  
632  C C   . GLN   A 86  ? 0.5378 0.6007 0.5107 0.1514  0.1259  -0.0520 85  GLN   A C   
633  O O   . GLN   A 86  ? 0.5355 0.6029 0.5307 0.1467  0.1191  -0.0474 85  GLN   A O   
634  C CB  . GLN   A 86  ? 0.5673 0.6523 0.5687 0.1693  0.1416  -0.0608 85  GLN   A CB  
635  C CG  . GLN   A 86  ? 0.6238 0.7332 0.6438 0.1748  0.1575  -0.0593 85  GLN   A CG  
636  C CD  . GLN   A 86  ? 0.6792 0.8065 0.7296 0.1667  0.1568  -0.0489 85  GLN   A CD  
637  O OE1 . GLN   A 86  ? 0.7093 0.8361 0.7590 0.1552  0.1523  -0.0399 85  GLN   A OE1 
638  N NE2 . GLN   A 86  ? 0.6671 0.8104 0.7451 0.1729  0.1607  -0.0501 85  GLN   A NE2 
639  N N   . LYS   A 87  ? 0.5328 0.5790 0.4795 0.1483  0.1199  -0.0537 86  LYS   A N   
640  C CA  . LYS   A 87  ? 0.5255 0.5594 0.4699 0.1390  0.1058  -0.0498 86  LYS   A CA  
641  C C   . LYS   A 87  ? 0.5128 0.5452 0.4400 0.1314  0.1070  -0.0430 86  LYS   A C   
642  O O   . LYS   A 87  ? 0.5217 0.5534 0.4282 0.1346  0.1150  -0.0446 86  LYS   A O   
643  C CB  . LYS   A 87  ? 0.5614 0.5740 0.4933 0.1426  0.0938  -0.0591 86  LYS   A CB  
644  C CG  . LYS   A 87  ? 0.6180 0.6294 0.5686 0.1487  0.0897  -0.0643 86  LYS   A CG  
645  C CD  . LYS   A 87  ? 0.6956 0.6855 0.6319 0.1539  0.0803  -0.0746 86  LYS   A CD  
646  C CE  . LYS   A 87  ? 0.7559 0.7393 0.6687 0.1628  0.0872  -0.0840 86  LYS   A CE  
647  N NZ  . LYS   A 87  ? 0.7880 0.7516 0.6919 0.1698  0.0789  -0.0952 86  LYS   A NZ  
648  N N   . LEU   A 88  ? 0.4856 0.5175 0.4212 0.1215  0.0992  -0.0352 87  LEU   A N   
649  C CA  . LEU   A 88  ? 0.4783 0.5079 0.4001 0.1141  0.0986  -0.0282 87  LEU   A CA  
650  C C   . LEU   A 88  ? 0.4786 0.4899 0.3867 0.1110  0.0847  -0.0314 87  LEU   A C   
651  O O   . LEU   A 88  ? 0.4877 0.4948 0.4090 0.1072  0.0749  -0.0312 87  LEU   A O   
652  C CB  . LEU   A 88  ? 0.4681 0.5098 0.4103 0.1052  0.0994  -0.0174 87  LEU   A CB  
653  C CG  . LEU   A 88  ? 0.4964 0.5352 0.4269 0.0974  0.0980  -0.0094 87  LEU   A CG  
654  C CD1 . LEU   A 88  ? 0.5075 0.5539 0.4249 0.0989  0.1112  -0.0054 87  LEU   A CD1 
655  C CD2 . LEU   A 88  ? 0.4972 0.5421 0.4483 0.0886  0.0936  -0.0013 87  LEU   A CD2 
656  N N   . TRP   A 89  ? 0.4662 0.4669 0.3482 0.1124  0.0835  -0.0344 88  TRP   A N   
657  C CA  . TRP   A 89  ? 0.4647 0.4490 0.3338 0.1091  0.0702  -0.0372 88  TRP   A CA  
658  C C   . TRP   A 89  ? 0.4507 0.4356 0.3145 0.1010  0.0675  -0.0281 88  TRP   A C   
659  O O   . TRP   A 89  ? 0.4515 0.4398 0.3013 0.1011  0.0748  -0.0241 88  TRP   A O   
660  C CB  . TRP   A 89  ? 0.4767 0.4476 0.3198 0.1160  0.0687  -0.0470 88  TRP   A CB  
661  C CG  . TRP   A 89  ? 0.4867 0.4516 0.3334 0.1238  0.0675  -0.0574 88  TRP   A CG  
662  C CD1 . TRP   A 89  ? 0.4948 0.4671 0.3456 0.1325  0.0781  -0.0621 88  TRP   A CD1 
663  C CD2 . TRP   A 89  ? 0.4940 0.4429 0.3389 0.1241  0.0548  -0.0646 88  TRP   A CD2 
664  N NE1 . TRP   A 89  ? 0.5020 0.4632 0.3544 0.1386  0.0723  -0.0719 88  TRP   A NE1 
665  C CE2 . TRP   A 89  ? 0.5035 0.4496 0.3515 0.1333  0.0579  -0.0734 88  TRP   A CE2 
666  C CE3 . TRP   A 89  ? 0.5036 0.4408 0.3460 0.1175  0.0411  -0.0642 88  TRP   A CE3 
667  C CZ2 . TRP   A 89  ? 0.5156 0.4460 0.3633 0.1355  0.0474  -0.0815 88  TRP   A CZ2 
668  C CZ3 . TRP   A 89  ? 0.5156 0.4387 0.3585 0.1191  0.0314  -0.0719 88  TRP   A CZ3 
669  C CH2 . TRP   A 89  ? 0.5192 0.4382 0.3641 0.1279  0.0343  -0.0803 88  TRP   A CH2 
670  N N   . ILE   A 90  ? 0.4300 0.4115 0.3049 0.0941  0.0573  -0.0248 89  ILE   A N   
671  C CA  . ILE   A 90  ? 0.4294 0.4108 0.3020 0.0868  0.0535  -0.0166 89  ILE   A CA  
672  C C   . ILE   A 90  ? 0.4307 0.3977 0.2882 0.0851  0.0413  -0.0201 89  ILE   A C   
673  O O   . ILE   A 90  ? 0.4251 0.3849 0.2886 0.0844  0.0323  -0.0251 89  ILE   A O   
674  C CB  . ILE   A 90  ? 0.4343 0.4241 0.3322 0.0803  0.0517  -0.0100 89  ILE   A CB  
675  C CG1 . ILE   A 90  ? 0.4502 0.4553 0.3636 0.0813  0.0633  -0.0059 89  ILE   A CG1 
676  C CG2 . ILE   A 90  ? 0.4453 0.4332 0.3422 0.0731  0.0462  -0.0026 89  ILE   A CG2 
677  C CD1 . ILE   A 90  ? 0.4671 0.4796 0.4059 0.0769  0.0610  -0.0026 89  ILE   A CD1 
678  N N   . CYS   A 91  ? 0.4340 0.3969 0.2724 0.0841  0.0406  -0.0169 90  CYS   A N   
679  C CA  . CYS   A 91  ? 0.4385 0.3890 0.2637 0.0821  0.0284  -0.0194 90  CYS   A CA  
680  C C   . CYS   A 91  ? 0.4264 0.3794 0.2647 0.0746  0.0220  -0.0116 90  CYS   A C   
681  O O   . CYS   A 91  ? 0.4170 0.3770 0.2587 0.0716  0.0273  -0.0031 90  CYS   A O   
682  C CB  . CYS   A 91  ? 0.4670 0.4107 0.2632 0.0856  0.0295  -0.0207 90  CYS   A CB  
683  S SG  . CYS   A 91  ? 0.5363 0.4648 0.3163 0.0835  0.0129  -0.0246 90  CYS   A SG  
684  N N   . MET   A 92  ? 0.4175 0.3646 0.2636 0.0715  0.0109  -0.0146 91  MET   A N   
685  C CA  . MET   A 92  ? 0.4161 0.3658 0.2760 0.0651  0.0049  -0.0084 91  MET   A CA  
686  C C   . MET   A 92  ? 0.4199 0.3607 0.2744 0.0628  -0.0080 -0.0112 91  MET   A C   
687  O O   . MET   A 92  ? 0.4229 0.3548 0.2659 0.0655  -0.0135 -0.0188 91  MET   A O   
688  C CB  . MET   A 92  ? 0.4128 0.3704 0.2978 0.0621  0.0070  -0.0069 91  MET   A CB  
689  C CG  . MET   A 92  ? 0.4300 0.3831 0.3225 0.0628  0.0017  -0.0140 91  MET   A CG  
690  S SD  . MET   A 92  ? 0.4430 0.4051 0.3592 0.0618  0.0069  -0.0128 91  MET   A SD  
691  C CE  . MET   A 92  ? 0.4742 0.4431 0.4055 0.0547  0.0050  -0.0047 91  MET   A CE  
692  N N   . GLU   A 93  ? 0.4194 0.3624 0.2828 0.0580  -0.0130 -0.0053 92  GLU   A N   
693  C CA  . GLU   A 93  ? 0.4298 0.3671 0.2927 0.0554  -0.0251 -0.0068 92  GLU   A CA  
694  C C   . GLU   A 93  ? 0.4332 0.3676 0.3071 0.0539  -0.0311 -0.0135 92  GLU   A C   
695  O O   . GLU   A 93  ? 0.4300 0.3695 0.3201 0.0525  -0.0272 -0.0135 92  GLU   A O   
696  C CB  . GLU   A 93  ? 0.4519 0.3947 0.3272 0.0511  -0.0271 0.0012  92  GLU   A CB  
697  C CG  . GLU   A 93  ? 0.5061 0.4479 0.3927 0.0474  -0.0378 0.0005  92  GLU   A CG  
698  C CD  . GLU   A 93  ? 0.5606 0.5080 0.4604 0.0443  -0.0383 0.0078  92  GLU   A CD  
699  O OE1 . GLU   A 93  ? 0.6100 0.5570 0.5169 0.0423  -0.0471 0.0079  92  GLU   A OE1 
700  O OE2 . GLU   A 93  ? 0.5251 0.4772 0.4292 0.0440  -0.0302 0.0132  92  GLU   A OE2 
701  N N   . PHE   A 94  ? 0.4315 0.3571 0.2954 0.0543  -0.0404 -0.0193 93  PHE   A N   
702  C CA  . PHE   A 94  ? 0.4319 0.3531 0.3047 0.0523  -0.0470 -0.0254 93  PHE   A CA  
703  C C   . PHE   A 94  ? 0.4201 0.3462 0.3119 0.0463  -0.0534 -0.0221 93  PHE   A C   
704  O O   . PHE   A 94  ? 0.4280 0.3542 0.3181 0.0447  -0.0600 -0.0197 93  PHE   A O   
705  C CB  . PHE   A 94  ? 0.4469 0.3564 0.3017 0.0545  -0.0553 -0.0328 93  PHE   A CB  
706  C CG  . PHE   A 94  ? 0.4510 0.3540 0.3136 0.0524  -0.0621 -0.0394 93  PHE   A CG  
707  C CD1 . PHE   A 94  ? 0.4631 0.3633 0.3288 0.0548  -0.0571 -0.0435 93  PHE   A CD1 
708  C CD2 . PHE   A 94  ? 0.4644 0.3637 0.3313 0.0479  -0.0740 -0.0412 93  PHE   A CD2 
709  C CE1 . PHE   A 94  ? 0.4734 0.3659 0.3453 0.0526  -0.0637 -0.0489 93  PHE   A CE1 
710  C CE2 . PHE   A 94  ? 0.4738 0.3665 0.3479 0.0451  -0.0802 -0.0467 93  PHE   A CE2 
711  C CZ  . PHE   A 94  ? 0.4720 0.3607 0.3482 0.0473  -0.0750 -0.0503 93  PHE   A CZ  
712  N N   . CYS   A 95  ? 0.3943 0.3245 0.3039 0.0434  -0.0513 -0.0220 94  CYS   A N   
713  C CA  . CYS   A 95  ? 0.3761 0.3118 0.3038 0.0378  -0.0560 -0.0193 94  CYS   A CA  
714  C C   . CYS   A 95  ? 0.3643 0.2941 0.2967 0.0349  -0.0630 -0.0247 94  CYS   A C   
715  O O   . CYS   A 95  ? 0.3626 0.2918 0.3026 0.0340  -0.0600 -0.0261 94  CYS   A O   
716  C CB  . CYS   A 95  ? 0.3642 0.3090 0.3073 0.0361  -0.0482 -0.0145 94  CYS   A CB  
717  S SG  . CYS   A 95  ? 0.3789 0.3301 0.3195 0.0379  -0.0411 -0.0074 94  CYS   A SG  
718  N N   . GLY   A 96  ? 0.3615 0.2867 0.2893 0.0335  -0.0728 -0.0273 95  GLY   A N   
719  C CA  . GLY   A 96  ? 0.3653 0.2833 0.2956 0.0304  -0.0811 -0.0328 95  GLY   A CA  
720  C C   . GLY   A 96  ? 0.3531 0.2744 0.3026 0.0247  -0.0814 -0.0320 95  GLY   A C   
721  O O   . GLY   A 96  ? 0.3625 0.2758 0.3120 0.0230  -0.0856 -0.0364 95  GLY   A O   
722  N N   . ALA   A 97  ? 0.3346 0.2670 0.3001 0.0216  -0.0776 -0.0265 96  ALA   A N   
723  C CA  . ALA   A 97  ? 0.3162 0.2523 0.2987 0.0160  -0.0773 -0.0253 96  ALA   A CA  
724  C C   . ALA   A 97  ? 0.3134 0.2506 0.2994 0.0168  -0.0687 -0.0235 96  ALA   A C   
725  O O   . ALA   A 97  ? 0.3080 0.2484 0.3064 0.0123  -0.0675 -0.0217 96  ALA   A O   
726  C CB  . ALA   A 97  ? 0.3065 0.2538 0.3049 0.0120  -0.0786 -0.0213 96  ALA   A CB  
727  N N   . GLY   A 98  ? 0.3090 0.2439 0.2841 0.0224  -0.0628 -0.0240 97  GLY   A N   
728  C CA  . GLY   A 98  ? 0.2998 0.2362 0.2788 0.0236  -0.0555 -0.0224 97  GLY   A CA  
729  C C   . GLY   A 98  ? 0.2794 0.2270 0.2703 0.0214  -0.0500 -0.0169 97  GLY   A C   
730  O O   . GLY   A 98  ? 0.2755 0.2292 0.2685 0.0212  -0.0498 -0.0144 97  GLY   A O   
731  N N   . SER   A 99  ? 0.2585 0.2078 0.2563 0.0203  -0.0458 -0.0153 98  SER   A N   
732  C CA  . SER   A 99  ? 0.2400 0.1988 0.2478 0.0184  -0.0407 -0.0109 98  SER   A CA  
733  C C   . SER   A 99  ? 0.2324 0.1959 0.2518 0.0125  -0.0431 -0.0093 98  SER   A C   
734  O O   . SER   A 99  ? 0.2392 0.1987 0.2607 0.0091  -0.0482 -0.0110 98  SER   A O   
735  C CB  . SER   A 99  ? 0.2449 0.2036 0.2542 0.0199  -0.0359 -0.0100 98  SER   A CB  
736  O OG  . SER   A 99  ? 0.2592 0.2146 0.2736 0.0162  -0.0380 -0.0098 98  SER   A OG  
737  N N   . LEU   A 100 ? 0.2146 0.1866 0.2421 0.0111  -0.0391 -0.0062 99  LEU   A N   
738  C CA  . LEU   A 100 ? 0.1986 0.1764 0.2373 0.0061  -0.0394 -0.0048 99  LEU   A CA  
739  C C   . LEU   A 100 ? 0.1888 0.1632 0.2296 0.0025  -0.0391 -0.0044 99  LEU   A C   
740  O O   . LEU   A 100 ? 0.1948 0.1709 0.2426 -0.0023 -0.0412 -0.0040 99  LEU   A O   
741  C CB  . LEU   A 100 ? 0.1846 0.1710 0.2299 0.0062  -0.0347 -0.0024 99  LEU   A CB  
742  C CG  . LEU   A 100 ? 0.2048 0.1950 0.2521 0.0079  -0.0366 -0.0021 99  LEU   A CG  
743  C CD1 . LEU   A 100 ? 0.2120 0.2081 0.2646 0.0088  -0.0320 -0.0002 99  LEU   A CD1 
744  C CD2 . LEU   A 100 ? 0.2046 0.1978 0.2598 0.0049  -0.0416 -0.0031 99  LEU   A CD2 
745  N N   . GLN   A 101 ? 0.1938 0.1632 0.2290 0.0048  -0.0370 -0.0043 100 GLN   A N   
746  C CA  . GLN   A 101 ? 0.1928 0.1571 0.2289 0.0018  -0.0377 -0.0033 100 GLN   A CA  
747  C C   . GLN   A 101 ? 0.1950 0.1504 0.2287 -0.0001 -0.0437 -0.0056 100 GLN   A C   
748  O O   . GLN   A 101 ? 0.2014 0.1550 0.2400 -0.0055 -0.0456 -0.0042 100 GLN   A O   
749  C CB  . GLN   A 101 ? 0.2085 0.1695 0.2400 0.0055  -0.0351 -0.0027 100 GLN   A CB  
750  C CG  . GLN   A 101 ? 0.2148 0.1697 0.2468 0.0024  -0.0365 -0.0008 100 GLN   A CG  
751  C CD  . GLN   A 101 ? 0.2355 0.1865 0.2640 0.0065  -0.0354 -0.0003 100 GLN   A CD  
752  O OE1 . GLN   A 101 ? 0.3007 0.2422 0.3264 0.0070  -0.0385 -0.0006 100 GLN   A OE1 
753  N NE2 . GLN   A 101 ? 0.1865 0.1443 0.2160 0.0095  -0.0314 0.0005  100 GLN   A NE2 
754  N N   . ASP   A 102 ? 0.2012 0.1510 0.2273 0.0040  -0.0468 -0.0093 101 ASP   A N   
755  C CA  . ASP   A 102 ? 0.2221 0.1623 0.2449 0.0025  -0.0536 -0.0126 101 ASP   A CA  
756  C C   . ASP   A 102 ? 0.2420 0.1867 0.2738 -0.0037 -0.0575 -0.0119 101 ASP   A C   
757  O O   . ASP   A 102 ? 0.2520 0.1910 0.2872 -0.0085 -0.0621 -0.0123 101 ASP   A O   
758  C CB  . ASP   A 102 ? 0.2443 0.1786 0.2554 0.0085  -0.0558 -0.0171 101 ASP   A CB  
759  C CG  . ASP   A 102 ? 0.2819 0.2127 0.2855 0.0149  -0.0514 -0.0182 101 ASP   A CG  
760  O OD1 . ASP   A 102 ? 0.2952 0.2218 0.3007 0.0147  -0.0504 -0.0172 101 ASP   A OD1 
761  O OD2 . ASP   A 102 ? 0.2894 0.2220 0.2856 0.0200  -0.0489 -0.0197 101 ASP   A OD2 
762  N N   . ILE   A 103 ? 0.2372 0.1926 0.2744 -0.0037 -0.0557 -0.0106 102 ILE   A N   
763  C CA  . ILE   A 103 ? 0.2301 0.1922 0.2782 -0.0087 -0.0589 -0.0100 102 ILE   A CA  
764  C C   . ILE   A 103 ? 0.2185 0.1865 0.2778 -0.0148 -0.0554 -0.0064 102 ILE   A C   
765  O O   . ILE   A 103 ? 0.2263 0.1934 0.2926 -0.0206 -0.0592 -0.0061 102 ILE   A O   
766  C CB  . ILE   A 103 ? 0.2282 0.1990 0.2784 -0.0056 -0.0584 -0.0098 102 ILE   A CB  
767  C CG1 . ILE   A 103 ? 0.2399 0.2038 0.2772 -0.0004 -0.0629 -0.0130 102 ILE   A CG1 
768  C CG2 . ILE   A 103 ? 0.2331 0.2135 0.2979 -0.0102 -0.0611 -0.0089 102 ILE   A CG2 
769  C CD1 . ILE   A 103 ? 0.2373 0.2071 0.2725 0.0038  -0.0610 -0.0116 102 ILE   A CD1 
770  N N   . TYR   A 104 ? 0.2051 0.1790 0.2658 -0.0140 -0.0484 -0.0036 103 TYR   A N   
771  C CA  . TYR   A 104 ? 0.1944 0.1746 0.2639 -0.0197 -0.0443 -0.0002 103 TYR   A CA  
772  C C   . TYR   A 104 ? 0.1998 0.1709 0.2669 -0.0240 -0.0456 0.0017  103 TYR   A C   
773  O O   . TYR   A 104 ? 0.1982 0.1733 0.2730 -0.0303 -0.0439 0.0046  103 TYR   A O   
774  C CB  . TYR   A 104 ? 0.1779 0.1666 0.2490 -0.0180 -0.0370 0.0017  103 TYR   A CB  
775  C CG  . TYR   A 104 ? 0.1701 0.1541 0.2321 -0.0145 -0.0337 0.0027  103 TYR   A CG  
776  C CD1 . TYR   A 104 ? 0.1782 0.1555 0.2359 -0.0168 -0.0334 0.0048  103 TYR   A CD1 
777  C CD2 . TYR   A 104 ? 0.1695 0.1567 0.2285 -0.0095 -0.0309 0.0019  103 TYR   A CD2 
778  C CE1 . TYR   A 104 ? 0.1740 0.1480 0.2250 -0.0135 -0.0313 0.0058  103 TYR   A CE1 
779  C CE2 . TYR   A 104 ? 0.1738 0.1584 0.2269 -0.0068 -0.0282 0.0028  103 TYR   A CE2 
780  C CZ  . TYR   A 104 ? 0.1780 0.1563 0.2272 -0.0086 -0.0287 0.0046  103 TYR   A CZ  
781  O OH  . TYR   A 104 ? 0.1848 0.1610 0.2294 -0.0058 -0.0269 0.0056  103 TYR   A OH  
782  N N   . GLN   A 105 ? 0.1994 0.1584 0.2563 -0.0206 -0.0485 0.0001  104 GLN   A N   
783  C CA  . GLN   A 105 ? 0.2063 0.1546 0.2610 -0.0242 -0.0510 0.0018  104 GLN   A CA  
784  C C   . GLN   A 105 ? 0.2214 0.1638 0.2805 -0.0293 -0.0580 0.0002  104 GLN   A C   
785  O O   . GLN   A 105 ? 0.2324 0.1636 0.2896 -0.0324 -0.0613 0.0012  104 GLN   A O   
786  C CB  . GLN   A 105 ? 0.2206 0.1585 0.2646 -0.0184 -0.0514 0.0006  104 GLN   A CB  
787  C CG  . GLN   A 105 ? 0.2411 0.1855 0.2835 -0.0155 -0.0450 0.0033  104 GLN   A CG  
788  C CD  . GLN   A 105 ? 0.2724 0.2083 0.3072 -0.0103 -0.0454 0.0030  104 GLN   A CD  
789  O OE1 . GLN   A 105 ? 0.2584 0.1887 0.2879 -0.0047 -0.0475 -0.0010 104 GLN   A OE1 
790  N NE2 . GLN   A 105 ? 0.2751 0.2107 0.3093 -0.0118 -0.0430 0.0071  104 GLN   A NE2 
791  N N   . VAL   A 106 ? 0.2180 0.1678 0.2837 -0.0302 -0.0607 -0.0020 105 VAL   A N   
792  C CA  . VAL   A 106 ? 0.2319 0.1791 0.3047 -0.0358 -0.0677 -0.0034 105 VAL   A CA  
793  C C   . VAL   A 106 ? 0.2346 0.1978 0.3229 -0.0411 -0.0646 -0.0007 105 VAL   A C   
794  O O   . VAL   A 106 ? 0.2464 0.2117 0.3449 -0.0489 -0.0651 0.0022  105 VAL   A O   
795  C CB  . VAL   A 106 ? 0.2618 0.2031 0.3282 -0.0316 -0.0752 -0.0093 105 VAL   A CB  
796  C CG1 . VAL   A 106 ? 0.2644 0.2057 0.3408 -0.0382 -0.0832 -0.0108 105 VAL   A CG1 
797  C CG2 . VAL   A 106 ? 0.2958 0.2215 0.3473 -0.0261 -0.0777 -0.0129 105 VAL   A CG2 
798  N N   . THR   A 107 ? 0.2296 0.2043 0.3205 -0.0368 -0.0612 -0.0014 106 THR   A N   
799  C CA  . THR   A 107 ? 0.2200 0.2101 0.3265 -0.0402 -0.0589 0.0001  106 THR   A CA  
800  C C   . THR   A 107 ? 0.2255 0.2253 0.3388 -0.0437 -0.0498 0.0044  106 THR   A C   
801  O O   . THR   A 107 ? 0.2247 0.2371 0.3525 -0.0477 -0.0476 0.0056  106 THR   A O   
802  C CB  . THR   A 107 ? 0.2292 0.2266 0.3359 -0.0337 -0.0593 -0.0024 106 THR   A CB  
803  O OG1 . THR   A 107 ? 0.2247 0.2230 0.3234 -0.0285 -0.0524 -0.0016 106 THR   A OG1 
804  C CG2 . THR   A 107 ? 0.2446 0.2337 0.3432 -0.0299 -0.0681 -0.0065 106 THR   A CG2 
805  N N   . GLY   A 108 ? 0.2202 0.2156 0.3232 -0.0412 -0.0444 0.0061  107 GLY   A N   
806  C CA  . GLY   A 108 ? 0.2110 0.2155 0.3172 -0.0432 -0.0357 0.0094  107 GLY   A CA  
807  C C   . GLY   A 108 ? 0.2042 0.2177 0.3110 -0.0370 -0.0316 0.0073  107 GLY   A C   
808  O O   . GLY   A 108 ? 0.2073 0.2192 0.3113 -0.0315 -0.0355 0.0042  107 GLY   A O   
809  N N   . SER   A 109 ? 0.1883 0.2106 0.2982 -0.0380 -0.0240 0.0090  108 SER   A N   
810  C CA  . SER   A 109 ? 0.2048 0.2342 0.3148 -0.0325 -0.0196 0.0069  108 SER   A CA  
811  C C   . SER   A 109 ? 0.1751 0.2114 0.2946 -0.0290 -0.0228 0.0040  108 SER   A C   
812  O O   . SER   A 109 ? 0.1663 0.2088 0.2979 -0.0320 -0.0258 0.0037  108 SER   A O   
813  C CB  . SER   A 109 ? 0.2476 0.2856 0.3603 -0.0350 -0.0111 0.0085  108 SER   A CB  
814  O OG  . SER   A 109 ? 0.3182 0.3674 0.4454 -0.0398 -0.0087 0.0093  108 SER   A OG  
815  N N   . LEU   A 110 ? 0.1717 0.2058 0.2853 -0.0226 -0.0233 0.0021  109 LEU   A N   
816  C CA  . LEU   A 110 ? 0.1645 0.2038 0.2853 -0.0186 -0.0265 -0.0001 109 LEU   A CA  
817  C C   . LEU   A 110 ? 0.1693 0.2214 0.3030 -0.0185 -0.0211 -0.0008 109 LEU   A C   
818  O O   . LEU   A 110 ? 0.1818 0.2374 0.3146 -0.0201 -0.0140 -0.0002 109 LEU   A O   
819  C CB  . LEU   A 110 ? 0.1630 0.1958 0.2732 -0.0123 -0.0274 -0.0010 109 LEU   A CB  
820  C CG  . LEU   A 110 ? 0.1859 0.2091 0.2868 -0.0102 -0.0341 -0.0015 109 LEU   A CG  
821  C CD1 . LEU   A 110 ? 0.2009 0.2150 0.2928 -0.0129 -0.0349 -0.0007 109 LEU   A CD1 
822  C CD2 . LEU   A 110 ? 0.1963 0.2157 0.2890 -0.0043 -0.0339 -0.0017 109 LEU   A CD2 
823  N N   . SER   A 111 ? 0.1543 0.2136 0.2999 -0.0165 -0.0246 -0.0023 110 SER   A N   
824  C CA  . SER   A 111 ? 0.1415 0.2132 0.3008 -0.0150 -0.0198 -0.0037 110 SER   A CA  
825  C C   . SER   A 111 ? 0.1405 0.2096 0.2934 -0.0090 -0.0164 -0.0052 110 SER   A C   
826  O O   . SER   A 111 ? 0.1487 0.2078 0.2895 -0.0060 -0.0195 -0.0047 110 SER   A O   
827  C CB  . SER   A 111 ? 0.1521 0.2316 0.3266 -0.0137 -0.0259 -0.0047 110 SER   A CB  
828  O OG  . SER   A 111 ? 0.1718 0.2447 0.3404 -0.0079 -0.0321 -0.0053 110 SER   A OG  
829  N N   . GLU   A 112 ? 0.1270 0.2051 0.2886 -0.0073 -0.0103 -0.0072 111 GLU   A N   
830  C CA  . GLU   A 112 ? 0.1281 0.2027 0.2846 -0.0018 -0.0078 -0.0091 111 GLU   A CA  
831  C C   . GLU   A 112 ? 0.1353 0.2056 0.2929 0.0036  -0.0149 -0.0091 111 GLU   A C   
832  O O   . GLU   A 112 ? 0.1419 0.2039 0.2898 0.0067  -0.0154 -0.0089 111 GLU   A O   
833  C CB  . GLU   A 112 ? 0.1338 0.2187 0.3002 -0.0003 -0.0004 -0.0122 111 GLU   A CB  
834  C CG  . GLU   A 112 ? 0.1435 0.2239 0.3054 0.0052  0.0016  -0.0149 111 GLU   A CG  
835  C CD  . GLU   A 112 ? 0.1455 0.2334 0.3128 0.0069  0.0097  -0.0190 111 GLU   A CD  
836  O OE1 . GLU   A 112 ? 0.1478 0.2426 0.3157 0.0028  0.0160  -0.0191 111 GLU   A OE1 
837  O OE2 . GLU   A 112 ? 0.1829 0.2697 0.3538 0.0125  0.0097  -0.0221 111 GLU   A OE2 
838  N N   . LEU   A 113 ? 0.1294 0.2055 0.2993 0.0046  -0.0205 -0.0091 112 LEU   A N   
839  C CA  . LEU   A 113 ? 0.1409 0.2121 0.3100 0.0096  -0.0277 -0.0084 112 LEU   A CA  
840  C C   . LEU   A 113 ? 0.1481 0.2073 0.3009 0.0087  -0.0327 -0.0059 112 LEU   A C   
841  O O   . LEU   A 113 ? 0.1642 0.2157 0.3086 0.0126  -0.0351 -0.0047 112 LEU   A O   
842  C CB  . LEU   A 113 ? 0.1343 0.2145 0.3202 0.0111  -0.0336 -0.0088 112 LEU   A CB  
843  C CG  . LEU   A 113 ? 0.1496 0.2415 0.3527 0.0142  -0.0289 -0.0116 112 LEU   A CG  
844  C CD1 . LEU   A 113 ? 0.1284 0.2317 0.3509 0.0148  -0.0347 -0.0120 112 LEU   A CD1 
845  C CD2 . LEU   A 113 ? 0.1790 0.2652 0.3798 0.0209  -0.0287 -0.0126 112 LEU   A CD2 
846  N N   . GLN   A 114 ? 0.1358 0.1929 0.2834 0.0038  -0.0337 -0.0052 113 GLN   A N   
847  C CA  . GLN   A 114 ? 0.1308 0.1766 0.2627 0.0037  -0.0377 -0.0037 113 GLN   A CA  
848  C C   . GLN   A 114 ? 0.1368 0.1755 0.2563 0.0053  -0.0326 -0.0030 113 GLN   A C   
849  O O   . GLN   A 114 ? 0.1441 0.1752 0.2533 0.0081  -0.0350 -0.0017 113 GLN   A O   
850  C CB  . GLN   A 114 ? 0.1382 0.1822 0.2680 -0.0016 -0.0398 -0.0036 113 GLN   A CB  
851  C CG  . GLN   A 114 ? 0.1523 0.2002 0.2913 -0.0030 -0.0477 -0.0042 113 GLN   A CG  
852  C CD  . GLN   A 114 ? 0.1677 0.2174 0.3118 -0.0096 -0.0486 -0.0043 113 GLN   A CD  
853  O OE1 . GLN   A 114 ? 0.1726 0.2208 0.3134 -0.0133 -0.0430 -0.0035 113 GLN   A OE1 
854  N NE2 . GLN   A 114 ? 0.1773 0.2304 0.3304 -0.0116 -0.0563 -0.0050 113 GLN   A NE2 
855  N N   . ILE   A 115 ? 0.1208 0.1624 0.2414 0.0033  -0.0257 -0.0037 114 ILE   A N   
856  C CA  . ILE   A 115 ? 0.1269 0.1630 0.2376 0.0043  -0.0215 -0.0033 114 ILE   A CA  
857  C C   . ILE   A 115 ? 0.1345 0.1693 0.2464 0.0089  -0.0215 -0.0035 114 ILE   A C   
858  O O   . ILE   A 115 ? 0.1310 0.1590 0.2340 0.0105  -0.0219 -0.0020 114 ILE   A O   
859  C CB  . ILE   A 115 ? 0.1299 0.1701 0.2420 0.0011  -0.0151 -0.0043 114 ILE   A CB  
860  C CG1 . ILE   A 115 ? 0.1466 0.1854 0.2553 -0.0039 -0.0154 -0.0029 114 ILE   A CG1 
861  C CG2 . ILE   A 115 ? 0.1314 0.1670 0.2352 0.0025  -0.0115 -0.0045 114 ILE   A CG2 
862  C CD1 . ILE   A 115 ? 0.1613 0.2044 0.2708 -0.0077 -0.0094 -0.0029 114 ILE   A CD1 
863  N N   . SER   A 116 ? 0.1213 0.1625 0.2451 0.0111  -0.0215 -0.0050 115 SER   A N   
864  C CA  . SER   A 116 ? 0.1275 0.1660 0.2532 0.0157  -0.0223 -0.0051 115 SER   A CA  
865  C C   . SER   A 116 ? 0.1399 0.1710 0.2581 0.0180  -0.0281 -0.0018 115 SER   A C   
866  O O   . SER   A 116 ? 0.1508 0.1756 0.2631 0.0198  -0.0275 -0.0001 115 SER   A O   
867  C CB  . SER   A 116 ? 0.1285 0.1751 0.2694 0.0184  -0.0225 -0.0074 115 SER   A CB  
868  O OG  . SER   A 116 ? 0.1406 0.1949 0.2879 0.0165  -0.0160 -0.0106 115 SER   A OG  
869  N N   . TYR   A 117 ? 0.1304 0.1622 0.2489 0.0177  -0.0338 -0.0008 116 TYR   A N   
870  C CA  . TYR   A 117 ? 0.1405 0.1652 0.2496 0.0198  -0.0395 0.0022  116 TYR   A CA  
871  C C   . TYR   A 117 ? 0.1536 0.1709 0.2478 0.0186  -0.0370 0.0037  116 TYR   A C   
872  O O   . TYR   A 117 ? 0.1543 0.1656 0.2407 0.0207  -0.0371 0.0065  116 TYR   A O   
873  C CB  . TYR   A 117 ? 0.1494 0.1766 0.2613 0.0191  -0.0466 0.0019  116 TYR   A CB  
874  C CG  . TYR   A 117 ? 0.1803 0.1995 0.2792 0.0209  -0.0526 0.0043  116 TYR   A CG  
875  C CD1 . TYR   A 117 ? 0.2137 0.2291 0.3102 0.0249  -0.0564 0.0073  116 TYR   A CD1 
876  C CD2 . TYR   A 117 ? 0.2009 0.2156 0.2888 0.0188  -0.0544 0.0037  116 TYR   A CD2 
877  C CE1 . TYR   A 117 ? 0.2391 0.2469 0.3212 0.0265  -0.0614 0.0099  116 TYR   A CE1 
878  C CE2 . TYR   A 117 ? 0.2268 0.2341 0.3010 0.0208  -0.0595 0.0053  116 TYR   A CE2 
879  C CZ  . TYR   A 117 ? 0.2568 0.2609 0.3275 0.0245  -0.0627 0.0086  116 TYR   A CZ  
880  O OH  . TYR   A 117 ? 0.3135 0.3101 0.3683 0.0264  -0.0671 0.0104  116 TYR   A OH  
881  N N   . VAL   A 118 ? 0.1474 0.1653 0.2385 0.0152  -0.0344 0.0023  117 VAL   A N   
882  C CA  . VAL   A 118 ? 0.1478 0.1597 0.2268 0.0147  -0.0319 0.0033  117 VAL   A CA  
883  C C   . VAL   A 118 ? 0.1471 0.1574 0.2250 0.0158  -0.0272 0.0046  117 VAL   A C   
884  O O   . VAL   A 118 ? 0.1555 0.1611 0.2256 0.0172  -0.0266 0.0070  117 VAL   A O   
885  C CB  . VAL   A 118 ? 0.1507 0.1631 0.2282 0.0111  -0.0302 0.0016  117 VAL   A CB  
886  C CG1 . VAL   A 118 ? 0.1681 0.1756 0.2360 0.0113  -0.0268 0.0025  117 VAL   A CG1 
887  C CG2 . VAL   A 118 ? 0.1513 0.1626 0.2278 0.0098  -0.0356 0.0006  117 VAL   A CG2 
888  N N   . CYS   A 119 ? 0.1490 0.1636 0.2350 0.0149  -0.0239 0.0028  118 CYS   A N   
889  C CA  . CYS   A 119 ? 0.1495 0.1622 0.2354 0.0154  -0.0203 0.0032  118 CYS   A CA  
890  C C   . CYS   A 119 ? 0.1403 0.1490 0.2263 0.0182  -0.0222 0.0058  118 CYS   A C   
891  O O   . CYS   A 119 ? 0.1541 0.1590 0.2360 0.0182  -0.0203 0.0078  118 CYS   A O   
892  C CB  . CYS   A 119 ? 0.1606 0.1779 0.2539 0.0142  -0.0169 -0.0001 118 CYS   A CB  
893  S SG  . CYS   A 119 ? 0.1812 0.2011 0.2710 0.0102  -0.0136 -0.0017 118 CYS   A SG  
894  N N   . ARG   A 120 ? 0.1319 0.1416 0.2234 0.0206  -0.0261 0.0061  119 ARG   A N   
895  C CA  . ARG   A 120 ? 0.1347 0.1391 0.2256 0.0234  -0.0286 0.0094  119 ARG   A CA  
896  C C   . ARG   A 120 ? 0.1560 0.1550 0.2345 0.0235  -0.0297 0.0137  119 ARG   A C   
897  O O   . ARG   A 120 ? 0.1706 0.1648 0.2450 0.0237  -0.0281 0.0172  119 ARG   A O   
898  C CB  . ARG   A 120 ? 0.1420 0.1487 0.2411 0.0264  -0.0338 0.0092  119 ARG   A CB  
899  C CG  . ARG   A 120 ? 0.1691 0.1692 0.2678 0.0294  -0.0369 0.0131  119 ARG   A CG  
900  C CD  . ARG   A 120 ? 0.1865 0.1882 0.2917 0.0329  -0.0437 0.0137  119 ARG   A CD  
901  N NE  . ARG   A 120 ? 0.2232 0.2240 0.3194 0.0326  -0.0487 0.0159  119 ARG   A NE  
902  C CZ  . ARG   A 120 ? 0.2502 0.2532 0.3507 0.0349  -0.0558 0.0162  119 ARG   A CZ  
903  N NH1 . ARG   A 120 ? 0.2471 0.2545 0.3626 0.0379  -0.0584 0.0147  119 ARG   A NH1 
904  N NH2 . ARG   A 120 ? 0.2480 0.2489 0.3382 0.0345  -0.0607 0.0177  119 ARG   A NH2 
905  N N   . GLU   A 121 ? 0.1476 0.1473 0.2198 0.0231  -0.0320 0.0132  120 GLU   A N   
906  C CA  . GLU   A 121 ? 0.1570 0.1516 0.2158 0.0238  -0.0328 0.0163  120 GLU   A CA  
907  C C   . GLU   A 121 ? 0.1692 0.1628 0.2226 0.0224  -0.0268 0.0173  120 GLU   A C   
908  O O   . GLU   A 121 ? 0.1814 0.1713 0.2276 0.0231  -0.0252 0.0212  120 GLU   A O   
909  C CB  . GLU   A 121 ? 0.1576 0.1526 0.2111 0.0238  -0.0371 0.0143  120 GLU   A CB  
910  C CG  . GLU   A 121 ? 0.1639 0.1605 0.2232 0.0253  -0.0441 0.0140  120 GLU   A CG  
911  C CD  . GLU   A 121 ? 0.2101 0.2017 0.2648 0.0284  -0.0480 0.0186  120 GLU   A CD  
912  O OE1 . GLU   A 121 ? 0.2225 0.2086 0.2628 0.0294  -0.0497 0.0211  120 GLU   A OE1 
913  O OE2 . GLU   A 121 ? 0.2204 0.2131 0.2852 0.0299  -0.0494 0.0196  120 GLU   A OE2 
914  N N   . VAL   A 122 ? 0.1590 0.1561 0.2161 0.0202  -0.0237 0.0141  121 VAL   A N   
915  C CA  . VAL   A 122 ? 0.1589 0.1559 0.2132 0.0191  -0.0189 0.0147  121 VAL   A CA  
916  C C   . VAL   A 122 ? 0.1507 0.1469 0.2100 0.0185  -0.0164 0.0171  121 VAL   A C   
917  O O   . VAL   A 122 ? 0.1585 0.1537 0.2144 0.0181  -0.0134 0.0200  121 VAL   A O   
918  C CB  . VAL   A 122 ? 0.1765 0.1767 0.2337 0.0170  -0.0174 0.0111  121 VAL   A CB  
919  C CG1 . VAL   A 122 ? 0.1769 0.1778 0.2336 0.0160  -0.0133 0.0117  121 VAL   A CG1 
920  C CG2 . VAL   A 122 ? 0.1878 0.1870 0.2395 0.0172  -0.0199 0.0093  121 VAL   A CG2 
921  N N   . LEU   A 123 ? 0.1411 0.1377 0.2088 0.0184  -0.0177 0.0158  122 LEU   A N   
922  C CA  . LEU   A 123 ? 0.1420 0.1360 0.2147 0.0178  -0.0163 0.0175  122 LEU   A CA  
923  C C   . LEU   A 123 ? 0.1495 0.1384 0.2174 0.0189  -0.0172 0.0232  122 LEU   A C   
924  O O   . LEU   A 123 ? 0.1630 0.1496 0.2318 0.0173  -0.0148 0.0264  122 LEU   A O   
925  C CB  . LEU   A 123 ? 0.1477 0.1421 0.2296 0.0185  -0.0177 0.0142  122 LEU   A CB  
926  C CG  . LEU   A 123 ? 0.1669 0.1655 0.2529 0.0167  -0.0153 0.0092  122 LEU   A CG  
927  C CD1 . LEU   A 123 ? 0.1529 0.1533 0.2469 0.0182  -0.0161 0.0052  122 LEU   A CD1 
928  C CD2 . LEU   A 123 ? 0.1790 0.1760 0.2653 0.0143  -0.0129 0.0095  122 LEU   A CD2 
929  N N   . GLN   A 124 ? 0.1526 0.1395 0.2155 0.0213  -0.0210 0.0250  123 GLN   A N   
930  C CA  . GLN   A 124 ? 0.1660 0.1473 0.2215 0.0223  -0.0219 0.0312  123 GLN   A CA  
931  C C   . GLN   A 124 ? 0.1830 0.1649 0.2296 0.0210  -0.0170 0.0340  123 GLN   A C   
932  O O   . GLN   A 124 ? 0.1949 0.1740 0.2401 0.0198  -0.0143 0.0391  123 GLN   A O   
933  C CB  . GLN   A 124 ? 0.1885 0.1679 0.2388 0.0252  -0.0278 0.0322  123 GLN   A CB  
934  C CG  . GLN   A 124 ? 0.1761 0.1551 0.2373 0.0272  -0.0326 0.0305  123 GLN   A CG  
935  C CD  . GLN   A 124 ? 0.2446 0.2252 0.3048 0.0296  -0.0390 0.0293  123 GLN   A CD  
936  O OE1 . GLN   A 124 ? 0.2864 0.2671 0.3364 0.0297  -0.0405 0.0293  123 GLN   A OE1 
937  N NE2 . GLN   A 124 ? 0.2044 0.1863 0.2757 0.0318  -0.0431 0.0277  123 GLN   A NE2 
938  N N   . GLY   A 125 ? 0.1820 0.1676 0.2239 0.0213  -0.0157 0.0308  124 GLY   A N   
939  C CA  . GLY   A 125 ? 0.1963 0.1835 0.2311 0.0209  -0.0107 0.0323  124 GLY   A CA  
940  C C   . GLY   A 125 ? 0.1777 0.1681 0.2206 0.0182  -0.0059 0.0331  124 GLY   A C   
941  O O   . GLY   A 125 ? 0.1773 0.1682 0.2178 0.0174  -0.0016 0.0374  124 GLY   A O   
942  N N   . LEU   A 126 ? 0.1617 0.1546 0.2144 0.0166  -0.0067 0.0291  125 LEU   A N   
943  C CA  . LEU   A 126 ? 0.1604 0.1562 0.2211 0.0139  -0.0036 0.0292  125 LEU   A CA  
944  C C   . LEU   A 126 ? 0.1595 0.1517 0.2251 0.0119  -0.0032 0.0336  125 LEU   A C   
945  O O   . LEU   A 126 ? 0.1601 0.1543 0.2294 0.0094  0.0002  0.0366  125 LEU   A O   
946  C CB  . LEU   A 126 ? 0.1640 0.1619 0.2315 0.0128  -0.0053 0.0237  125 LEU   A CB  
947  C CG  . LEU   A 126 ? 0.1639 0.1653 0.2286 0.0134  -0.0053 0.0199  125 LEU   A CG  
948  C CD1 . LEU   A 126 ? 0.1589 0.1617 0.2291 0.0119  -0.0068 0.0155  125 LEU   A CD1 
949  C CD2 . LEU   A 126 ? 0.1640 0.1689 0.2272 0.0135  -0.0018 0.0212  125 LEU   A CD2 
950  N N   . ALA   A 127 ? 0.1587 0.1453 0.2253 0.0129  -0.0070 0.0344  126 ALA   A N   
951  C CA  . ALA   A 127 ? 0.1722 0.1534 0.2432 0.0111  -0.0073 0.0389  126 ALA   A CA  
952  C C   . ALA   A 127 ? 0.1931 0.1731 0.2569 0.0103  -0.0038 0.0464  126 ALA   A C   
953  O O   . ALA   A 127 ? 0.2083 0.1876 0.2769 0.0069  -0.0011 0.0505  126 ALA   A O   
954  C CB  . ALA   A 127 ? 0.1804 0.1554 0.2533 0.0134  -0.0124 0.0385  126 ALA   A CB  
955  N N   . TYR   A 128 ? 0.1960 0.1765 0.2482 0.0130  -0.0035 0.0477  127 TYR   A N   
956  C CA  . TYR   A 128 ? 0.2125 0.1925 0.2554 0.0127  0.0008  0.0543  127 TYR   A CA  
957  C C   . TYR   A 128 ? 0.2206 0.2083 0.2675 0.0104  0.0074  0.0544  127 TYR   A C   
958  O O   . TYR   A 128 ? 0.2290 0.2173 0.2787 0.0074  0.0116  0.0603  127 TYR   A O   
959  C CB  . TYR   A 128 ? 0.2273 0.2059 0.2553 0.0165  -0.0008 0.0541  127 TYR   A CB  
960  C CG  . TYR   A 128 ? 0.2497 0.2288 0.2661 0.0166  0.0049  0.0599  127 TYR   A CG  
961  C CD1 . TYR   A 128 ? 0.2721 0.2454 0.2829 0.0153  0.0056  0.0681  127 TYR   A CD1 
962  C CD2 . TYR   A 128 ? 0.2595 0.2450 0.2714 0.0178  0.0103  0.0574  127 TYR   A CD2 
963  C CE1 . TYR   A 128 ? 0.2930 0.2676 0.2929 0.0149  0.0122  0.0739  127 TYR   A CE1 
964  C CE2 . TYR   A 128 ? 0.2818 0.2690 0.2837 0.0180  0.0169  0.0623  127 TYR   A CE2 
965  C CZ  . TYR   A 128 ? 0.3123 0.2945 0.3081 0.0163  0.0183  0.0707  127 TYR   A CZ  
966  O OH  . TYR   A 128 ? 0.3407 0.3252 0.3252 0.0166  0.0258  0.0756  127 TYR   A OH  
967  N N   . LEU   A 129 ? 0.1985 0.1921 0.2465 0.0118  0.0082  0.0485  128 LEU   A N   
968  C CA  . LEU   A 129 ? 0.2079 0.2095 0.2612 0.0105  0.0137  0.0483  128 LEU   A CA  
969  C C   . LEU   A 129 ? 0.2020 0.2056 0.2693 0.0060  0.0145  0.0499  128 LEU   A C   
970  O O   . LEU   A 129 ? 0.2035 0.2124 0.2756 0.0036  0.0197  0.0540  128 LEU   A O   
971  C CB  . LEU   A 129 ? 0.2145 0.2203 0.2675 0.0130  0.0128  0.0415  128 LEU   A CB  
972  C CG  . LEU   A 129 ? 0.2582 0.2621 0.2979 0.0172  0.0123  0.0393  128 LEU   A CG  
973  C CD1 . LEU   A 129 ? 0.2524 0.2587 0.2935 0.0190  0.0103  0.0328  128 LEU   A CD1 
974  C CD2 . LEU   A 129 ? 0.2822 0.2885 0.3133 0.0189  0.0186  0.0431  128 LEU   A CD2 
975  N N   . HIS   A 130 ? 0.1816 0.1813 0.2560 0.0045  0.0094  0.0468  129 HIS   A N   
976  C CA  . HIS   A 130 ? 0.1909 0.1909 0.2778 0.0000  0.0090  0.0475  129 HIS   A CA  
977  C C   . HIS   A 130 ? 0.2177 0.2134 0.3067 -0.0032 0.0108  0.0552  129 HIS   A C   
978  O O   . HIS   A 130 ? 0.2270 0.2259 0.3258 -0.0076 0.0131  0.0580  129 HIS   A O   
979  C CB  . HIS   A 130 ? 0.1722 0.1682 0.2640 -0.0001 0.0034  0.0414  129 HIS   A CB  
980  C CG  . HIS   A 130 ? 0.1607 0.1614 0.2515 0.0019  0.0021  0.0348  129 HIS   A CG  
981  N ND1 . HIS   A 130 ? 0.1617 0.1600 0.2547 0.0021  -0.0018 0.0291  129 HIS   A ND1 
982  C CD2 . HIS   A 130 ? 0.1746 0.1817 0.2624 0.0036  0.0044  0.0334  129 HIS   A CD2 
983  C CE1 . HIS   A 130 ? 0.1748 0.1778 0.2654 0.0034  -0.0017 0.0253  129 HIS   A CE1 
984  N NE2 . HIS   A 130 ? 0.1722 0.1801 0.2601 0.0044  0.0015  0.0276  129 HIS   A NE2 
985  N N   . SER   A 131 ? 0.2300 0.2183 0.3099 -0.0014 0.0096  0.0590  130 SER   A N   
986  C CA  . SER   A 131 ? 0.2477 0.2305 0.3276 -0.0046 0.0113  0.0676  130 SER   A CA  
987  C C   . SER   A 131 ? 0.2659 0.2559 0.3433 -0.0064 0.0192  0.0737  130 SER   A C   
988  O O   . SER   A 131 ? 0.2718 0.2606 0.3541 -0.0111 0.0222  0.0808  130 SER   A O   
989  C CB  . SER   A 131 ? 0.2628 0.2359 0.3324 -0.0016 0.0073  0.0706  130 SER   A CB  
990  O OG  . SER   A 131 ? 0.2968 0.2716 0.3518 0.0018  0.0098  0.0728  130 SER   A OG  
991  N N   . GLN   A 132 ? 0.2679 0.2654 0.3379 -0.0028 0.0228  0.0708  131 GLN   A N   
992  C CA  . GLN   A 132 ? 0.2758 0.2820 0.3434 -0.0031 0.0311  0.0746  131 GLN   A CA  
993  C C   . GLN   A 132 ? 0.2694 0.2866 0.3523 -0.0054 0.0342  0.0719  131 GLN   A C   
994  O O   . GLN   A 132 ? 0.2689 0.2955 0.3524 -0.0048 0.0412  0.0736  131 GLN   A O   
995  C CB  . GLN   A 132 ? 0.3111 0.3183 0.3624 0.0028  0.0328  0.0719  131 GLN   A CB  
996  C CG  . GLN   A 132 ? 0.3602 0.3571 0.3962 0.0052  0.0289  0.0747  131 GLN   A CG  
997  C CD  . GLN   A 132 ? 0.4419 0.4343 0.4731 0.0020  0.0323  0.0848  131 GLN   A CD  
998  O OE1 . GLN   A 132 ? 0.4648 0.4620 0.4899 0.0015  0.0401  0.0897  131 GLN   A OE1 
999  N NE2 . GLN   A 132 ? 0.4566 0.4394 0.4905 -0.0001 0.0266  0.0883  131 GLN   A NE2 
1000 N N   . LYS   A 133 ? 0.2563 0.2726 0.3515 -0.0079 0.0287  0.0676  132 LYS   A N   
1001 C CA  . LYS   A 133 ? 0.2500 0.2755 0.3603 -0.0105 0.0292  0.0648  132 LYS   A CA  
1002 C C   . LYS   A 133 ? 0.2392 0.2732 0.3479 -0.0058 0.0308  0.0593  132 LYS   A C   
1003 O O   . LYS   A 133 ? 0.2391 0.2834 0.3584 -0.0067 0.0340  0.0592  132 LYS   A O   
1004 C CB  . LYS   A 133 ? 0.2815 0.3129 0.4037 -0.0162 0.0345  0.0720  132 LYS   A CB  
1005 C CG  . LYS   A 133 ? 0.3494 0.3706 0.4747 -0.0214 0.0317  0.0774  132 LYS   A CG  
1006 C CD  . LYS   A 133 ? 0.4386 0.4660 0.5791 -0.0285 0.0359  0.0840  132 LYS   A CD  
1007 C CE  . LYS   A 133 ? 0.5261 0.5430 0.6651 -0.0332 0.0359  0.0923  132 LYS   A CE  
1008 N NZ  . LYS   A 133 ? 0.5827 0.5965 0.7044 -0.0301 0.0413  0.0985  132 LYS   A NZ  
1009 N N   . LYS   A 134 ? 0.2266 0.2559 0.3231 -0.0009 0.0280  0.0546  133 LYS   A N   
1010 C CA  . LYS   A 134 ? 0.2200 0.2544 0.3142 0.0034  0.0280  0.0490  133 LYS   A CA  
1011 C C   . LYS   A 134 ? 0.1999 0.2304 0.2959 0.0036  0.0208  0.0427  133 LYS   A C   
1012 O O   . LYS   A 134 ? 0.2117 0.2347 0.3057 0.0024  0.0164  0.0418  133 LYS   A O   
1013 C CB  . LYS   A 134 ? 0.2609 0.2927 0.3390 0.0086  0.0303  0.0483  133 LYS   A CB  
1014 C CG  . LYS   A 134 ? 0.3171 0.3535 0.3900 0.0097  0.0385  0.0535  133 LYS   A CG  
1015 C CD  . LYS   A 134 ? 0.3810 0.4157 0.4385 0.0157  0.0400  0.0501  133 LYS   A CD  
1016 C CE  . LYS   A 134 ? 0.4522 0.4918 0.5026 0.0177  0.0489  0.0540  133 LYS   A CE  
1017 N NZ  . LYS   A 134 ? 0.4858 0.5219 0.5315 0.0140  0.0517  0.0622  133 LYS   A NZ  
1018 N N   . ILE   A 135 ? 0.1772 0.2130 0.2767 0.0056  0.0199  0.0385  134 ILE   A N   
1019 C CA  . ILE   A 135 ? 0.1698 0.2022 0.2682 0.0063  0.0140  0.0328  134 ILE   A CA  
1020 C C   . ILE   A 135 ? 0.1637 0.1958 0.2526 0.0113  0.0146  0.0299  134 ILE   A C   
1021 O O   . ILE   A 135 ? 0.1715 0.2094 0.2614 0.0140  0.0183  0.0301  134 ILE   A O   
1022 C CB  . ILE   A 135 ? 0.1658 0.2031 0.2759 0.0038  0.0111  0.0308  134 ILE   A CB  
1023 C CG1 . ILE   A 135 ? 0.1896 0.2271 0.3101 -0.0016 0.0102  0.0335  134 ILE   A CG1 
1024 C CG2 . ILE   A 135 ? 0.1684 0.2017 0.2743 0.0047  0.0056  0.0254  134 ILE   A CG2 
1025 C CD1 . ILE   A 135 ? 0.1941 0.2373 0.3268 -0.0043 0.0067  0.0316  134 ILE   A CD1 
1026 N N   . HIS   A 136 ? 0.1556 0.1810 0.2357 0.0126  0.0110  0.0270  135 HIS   A N   
1027 C CA  . HIS   A 136 ? 0.1499 0.1734 0.2209 0.0167  0.0107  0.0240  135 HIS   A CA  
1028 C C   . HIS   A 136 ? 0.1450 0.1717 0.2205 0.0178  0.0090  0.0209  135 HIS   A C   
1029 O O   . HIS   A 136 ? 0.1544 0.1839 0.2288 0.0213  0.0114  0.0202  135 HIS   A O   
1030 C CB  . HIS   A 136 ? 0.1588 0.1753 0.2222 0.0168  0.0068  0.0221  135 HIS   A CB  
1031 C CG  . HIS   A 136 ? 0.1574 0.1708 0.2112 0.0203  0.0059  0.0195  135 HIS   A CG  
1032 N ND1 . HIS   A 136 ? 0.1684 0.1812 0.2220 0.0214  0.0036  0.0159  135 HIS   A ND1 
1033 C CD2 . HIS   A 136 ? 0.1835 0.1931 0.2271 0.0226  0.0062  0.0199  135 HIS   A CD2 
1034 C CE1 . HIS   A 136 ? 0.1746 0.1830 0.2190 0.0240  0.0025  0.0140  135 HIS   A CE1 
1035 N NE2 . HIS   A 136 ? 0.1770 0.1836 0.2147 0.0250  0.0040  0.0161  135 HIS   A NE2 
1036 N N   . ARG   A 137 ? 0.1400 0.1658 0.2199 0.0152  0.0049  0.0190  136 ARG   A N   
1037 C CA  . ARG   A 137 ? 0.1376 0.1658 0.2215 0.0157  0.0024  0.0170  136 ARG   A CA  
1038 C C   . ARG   A 137 ? 0.1364 0.1608 0.2127 0.0191  0.0010  0.0144  136 ARG   A C   
1039 O O   . ARG   A 137 ? 0.1468 0.1724 0.2258 0.0204  -0.0009 0.0134  136 ARG   A O   
1040 C CB  . ARG   A 137 ? 0.1469 0.1834 0.2414 0.0160  0.0046  0.0189  136 ARG   A CB  
1041 C CG  . ARG   A 137 ? 0.1592 0.1986 0.2632 0.0120  0.0013  0.0191  136 ARG   A CG  
1042 C CD  . ARG   A 137 ? 0.1613 0.2003 0.2655 0.0126  -0.0036 0.0166  136 ARG   A CD  
1043 N NE  . ARG   A 137 ? 0.1498 0.1962 0.2629 0.0152  -0.0033 0.0174  136 ARG   A NE  
1044 C CZ  . ARG   A 137 ? 0.1591 0.2055 0.2700 0.0199  -0.0033 0.0164  136 ARG   A CZ  
1045 N NH1 . ARG   A 137 ? 0.1475 0.1861 0.2469 0.0220  -0.0038 0.0146  136 ARG   A NH1 
1046 N NH2 . ARG   A 137 ? 0.1435 0.1974 0.2646 0.0225  -0.0031 0.0170  136 ARG   A NH2 
1047 N N   . ASP   A 138 ? 0.1257 0.1445 0.1929 0.0202  0.0008  0.0134  137 ASP   A N   
1048 C CA  . ASP   A 138 ? 0.1468 0.1607 0.2071 0.0228  -0.0011 0.0109  137 ASP   A CA  
1049 C C   . ASP   A 138 ? 0.1586 0.1669 0.2126 0.0210  -0.0038 0.0097  137 ASP   A C   
1050 O O   . ASP   A 138 ? 0.1673 0.1710 0.2145 0.0229  -0.0049 0.0080  137 ASP   A O   
1051 C CB  . ASP   A 138 ? 0.1592 0.1733 0.2151 0.0275  0.0023  0.0105  137 ASP   A CB  
1052 C CG  . ASP   A 138 ? 0.2240 0.2332 0.2751 0.0309  0.0003  0.0075  137 ASP   A CG  
1053 O OD1 . ASP   A 138 ? 0.1844 0.1916 0.2380 0.0297  -0.0034 0.0068  137 ASP   A OD1 
1054 O OD2 . ASP   A 138 ? 0.2673 0.2737 0.3112 0.0347  0.0021  0.0058  137 ASP   A OD2 
1055 N N   . ILE   A 139 ? 0.1498 0.1587 0.2070 0.0175  -0.0049 0.0101  138 ILE   A N   
1056 C CA  . ILE   A 139 ? 0.1495 0.1550 0.2033 0.0161  -0.0071 0.0089  138 ILE   A CA  
1057 C C   . ILE   A 139 ? 0.1650 0.1680 0.2173 0.0147  -0.0098 0.0071  138 ILE   A C   
1058 O O   . ILE   A 139 ? 0.1671 0.1715 0.2222 0.0128  -0.0104 0.0070  138 ILE   A O   
1059 C CB  . ILE   A 139 ? 0.1549 0.1620 0.2133 0.0138  -0.0069 0.0095  138 ILE   A CB  
1060 C CG1 . ILE   A 139 ? 0.1600 0.1680 0.2194 0.0147  -0.0046 0.0123  138 ILE   A CG1 
1061 C CG2 . ILE   A 139 ? 0.1657 0.1710 0.2232 0.0126  -0.0091 0.0079  138 ILE   A CG2 
1062 C CD1 . ILE   A 139 ? 0.1802 0.1851 0.2325 0.0169  -0.0049 0.0132  138 ILE   A CD1 
1063 N N   . LYS   A 140 ? 0.1547 0.1537 0.2023 0.0152  -0.0117 0.0058  139 LYS   A N   
1064 C CA  . LYS   A 140 ? 0.1507 0.1466 0.1970 0.0130  -0.0143 0.0047  139 LYS   A CA  
1065 C C   . LYS   A 140 ? 0.1600 0.1523 0.2027 0.0132  -0.0167 0.0034  139 LYS   A C   
1066 O O   . LYS   A 140 ? 0.1699 0.1612 0.2089 0.0159  -0.0166 0.0031  139 LYS   A O   
1067 C CB  . LYS   A 140 ? 0.1640 0.1569 0.2086 0.0140  -0.0153 0.0048  139 LYS   A CB  
1068 C CG  . LYS   A 140 ? 0.1686 0.1577 0.2089 0.0184  -0.0154 0.0036  139 LYS   A CG  
1069 C CD  . LYS   A 140 ? 0.1926 0.1792 0.2332 0.0204  -0.0164 0.0037  139 LYS   A CD  
1070 C CE  . LYS   A 140 ? 0.2185 0.1992 0.2572 0.0176  -0.0200 0.0039  139 LYS   A CE  
1071 N NZ  . LYS   A 140 ? 0.2384 0.2146 0.2766 0.0206  -0.0219 0.0041  139 LYS   A NZ  
1072 N N   . GLY   A 141 ? 0.1548 0.1454 0.1983 0.0101  -0.0190 0.0027  140 GLY   A N   
1073 C CA  . GLY   A 141 ? 0.1661 0.1536 0.2079 0.0095  -0.0223 0.0013  140 GLY   A CA  
1074 C C   . GLY   A 141 ? 0.1772 0.1583 0.2115 0.0130  -0.0243 -0.0004 140 GLY   A C   
1075 O O   . GLY   A 141 ? 0.1884 0.1680 0.2190 0.0144  -0.0263 -0.0016 140 GLY   A O   
1076 N N   . ALA   A 142 ? 0.1728 0.1498 0.2040 0.0150  -0.0239 -0.0008 141 ALA   A N   
1077 C CA  . ALA   A 142 ? 0.1823 0.1528 0.2061 0.0191  -0.0252 -0.0033 141 ALA   A CA  
1078 C C   . ALA   A 142 ? 0.1968 0.1697 0.2160 0.0234  -0.0223 -0.0036 141 ALA   A C   
1079 O O   . ALA   A 142 ? 0.2183 0.1862 0.2294 0.0270  -0.0231 -0.0063 141 ALA   A O   
1080 C CB  . ALA   A 142 ? 0.1967 0.1632 0.2202 0.0211  -0.0250 -0.0035 141 ALA   A CB  
1081 N N   . ASN   A 143 ? 0.1790 0.1592 0.2028 0.0229  -0.0186 -0.0009 142 ASN   A N   
1082 C CA  . ASN   A 143 ? 0.1775 0.1604 0.1976 0.0262  -0.0150 0.0002  142 ASN   A CA  
1083 C C   . ASN   A 143 ? 0.1917 0.1761 0.2106 0.0250  -0.0161 0.0016  142 ASN   A C   
1084 O O   . ASN   A 143 ? 0.2066 0.1934 0.2233 0.0266  -0.0130 0.0039  142 ASN   A O   
1085 C CB  . ASN   A 143 ? 0.1712 0.1602 0.1974 0.0270  -0.0103 0.0025  142 ASN   A CB  
1086 C CG  . ASN   A 143 ? 0.1908 0.1784 0.2182 0.0294  -0.0099 0.0011  142 ASN   A CG  
1087 O OD1 . ASN   A 143 ? 0.2090 0.1902 0.2304 0.0320  -0.0118 -0.0019 142 ASN   A OD1 
1088 N ND2 . ASN   A 143 ? 0.1914 0.1840 0.2266 0.0285  -0.0083 0.0029  142 ASN   A ND2 
1089 N N   . ILE   A 144 ? 0.1795 0.1624 0.2002 0.0222  -0.0205 0.0007  143 ILE   A N   
1090 C CA  . ILE   A 144 ? 0.1836 0.1676 0.2043 0.0215  -0.0231 0.0017  143 ILE   A CA  
1091 C C   . ILE   A 144 ? 0.2045 0.1827 0.2186 0.0219  -0.0286 -0.0013 143 ILE   A C   
1092 O O   . ILE   A 144 ? 0.2013 0.1776 0.2190 0.0192  -0.0318 -0.0032 143 ILE   A O   
1093 C CB  . ILE   A 144 ? 0.1848 0.1738 0.2165 0.0179  -0.0236 0.0027  143 ILE   A CB  
1094 C CG1 . ILE   A 144 ? 0.1834 0.1767 0.2208 0.0174  -0.0189 0.0047  143 ILE   A CG1 
1095 C CG2 . ILE   A 144 ? 0.1867 0.1768 0.2199 0.0179  -0.0270 0.0035  143 ILE   A CG2 
1096 C CD1 . ILE   A 144 ? 0.1884 0.1858 0.2350 0.0140  -0.0186 0.0044  143 ILE   A CD1 
1097 N N   . LEU   A 145 ? 0.2123 0.1871 0.2160 0.0249  -0.0300 -0.0016 144 LEU   A N   
1098 C CA  . LEU   A 145 ? 0.2313 0.1994 0.2263 0.0257  -0.0359 -0.0051 144 LEU   A CA  
1099 C C   . LEU   A 145 ? 0.2420 0.2109 0.2382 0.0243  -0.0420 -0.0045 144 LEU   A C   
1100 O O   . LEU   A 145 ? 0.2392 0.2121 0.2381 0.0247  -0.0410 -0.0009 144 LEU   A O   
1101 C CB  . LEU   A 145 ? 0.2453 0.2084 0.2255 0.0305  -0.0337 -0.0067 144 LEU   A CB  
1102 C CG  . LEU   A 145 ? 0.2694 0.2328 0.2490 0.0332  -0.0272 -0.0074 144 LEU   A CG  
1103 C CD1 . LEU   A 145 ? 0.2820 0.2405 0.2467 0.0383  -0.0251 -0.0099 144 LEU   A CD1 
1104 C CD2 . LEU   A 145 ? 0.2784 0.2389 0.2643 0.0314  -0.0291 -0.0100 144 LEU   A CD2 
1105 N N   . ILE   A 146 ? 0.2418 0.2066 0.2368 0.0228  -0.0488 -0.0078 145 ILE   A N   
1106 C CA  . ILE   A 146 ? 0.2557 0.2219 0.2539 0.0212  -0.0561 -0.0077 145 ILE   A CA  
1107 C C   . ILE   A 146 ? 0.2765 0.2346 0.2601 0.0234  -0.0626 -0.0110 145 ILE   A C   
1108 O O   . ILE   A 146 ? 0.2846 0.2357 0.2618 0.0235  -0.0646 -0.0153 145 ILE   A O   
1109 C CB  . ILE   A 146 ? 0.2612 0.2317 0.2748 0.0161  -0.0591 -0.0086 145 ILE   A CB  
1110 C CG1 . ILE   A 146 ? 0.2618 0.2398 0.2879 0.0140  -0.0523 -0.0060 145 ILE   A CG1 
1111 C CG2 . ILE   A 146 ? 0.2689 0.2425 0.2891 0.0144  -0.0671 -0.0088 145 ILE   A CG2 
1112 C CD1 . ILE   A 146 ? 0.2780 0.2623 0.3093 0.0155  -0.0490 -0.0024 145 ILE   A CD1 
1113 N N   . ASN   A 147 ? 0.2886 0.2465 0.2658 0.0254  -0.0666 -0.0091 146 ASN   A N   
1114 C CA  . ASN   A 147 ? 0.3136 0.2634 0.2751 0.0275  -0.0739 -0.0124 146 ASN   A CA  
1115 C C   . ASN   A 147 ? 0.3319 0.2826 0.3024 0.0238  -0.0847 -0.0146 146 ASN   A C   
1116 O O   . ASN   A 147 ? 0.3177 0.2763 0.3069 0.0201  -0.0852 -0.0131 146 ASN   A O   
1117 C CB  . ASN   A 147 ? 0.3326 0.2800 0.2784 0.0318  -0.0726 -0.0092 146 ASN   A CB  
1118 C CG  . ASN   A 147 ? 0.3516 0.3041 0.3042 0.0315  -0.0760 -0.0040 146 ASN   A CG  
1119 O OD1 . ASN   A 147 ? 0.3447 0.3029 0.3137 0.0286  -0.0806 -0.0037 146 ASN   A OD1 
1120 N ND2 . ASN   A 147 ? 0.3705 0.3210 0.3109 0.0347  -0.0736 0.0004  146 ASN   A ND2 
1121 N N   . ASP   A 148 ? 0.3514 0.2944 0.3089 0.0249  -0.0933 -0.0184 147 ASP   A N   
1122 C CA  . ASP   A 148 ? 0.3630 0.3068 0.3296 0.0211  -0.1044 -0.0208 147 ASP   A CA  
1123 C C   . ASP   A 148 ? 0.3542 0.3071 0.3335 0.0206  -0.1085 -0.0163 147 ASP   A C   
1124 O O   . ASP   A 148 ? 0.3528 0.3112 0.3478 0.0167  -0.1155 -0.0172 147 ASP   A O   
1125 C CB  . ASP   A 148 ? 0.4170 0.3493 0.3654 0.0225  -0.1134 -0.0265 147 ASP   A CB  
1126 C CG  . ASP   A 148 ? 0.5260 0.4492 0.4665 0.0226  -0.1105 -0.0319 147 ASP   A CG  
1127 O OD1 . ASP   A 148 ? 0.5287 0.4549 0.4829 0.0194  -0.1055 -0.0316 147 ASP   A OD1 
1128 O OD2 . ASP   A 148 ? 0.5989 0.5114 0.5189 0.0262  -0.1135 -0.0366 147 ASP   A OD2 
1129 N N   . ALA   A 149 ? 0.3442 0.2993 0.3186 0.0243  -0.1041 -0.0114 148 ALA   A N   
1130 C CA  . ALA   A 149 ? 0.3399 0.3026 0.3266 0.0246  -0.1078 -0.0070 148 ALA   A CA  
1131 C C   . ALA   A 149 ? 0.3264 0.2998 0.3354 0.0223  -0.1007 -0.0046 148 ALA   A C   
1132 O O   . ALA   A 149 ? 0.3235 0.3037 0.3450 0.0230  -0.1030 -0.0017 148 ALA   A O   
1133 C CB  . ALA   A 149 ? 0.3524 0.3110 0.3236 0.0294  -0.1068 -0.0023 148 ALA   A CB  
1134 N N   . GLY   A 150 ? 0.3155 0.2899 0.3286 0.0201  -0.0924 -0.0059 149 GLY   A N   
1135 C CA  . GLY   A 150 ? 0.3019 0.2855 0.3330 0.0181  -0.0853 -0.0040 149 GLY   A CA  
1136 C C   . GLY   A 150 ? 0.2955 0.2796 0.3233 0.0210  -0.0770 -0.0001 149 GLY   A C   
1137 O O   . GLY   A 150 ? 0.2939 0.2849 0.3351 0.0201  -0.0718 0.0015  149 GLY   A O   
1138 N N   . GLU   A 151 ? 0.2875 0.2644 0.2974 0.0245  -0.0755 0.0016  150 GLU   A N   
1139 C CA  . GLU   A 151 ? 0.2833 0.2603 0.2902 0.0266  -0.0679 0.0059  150 GLU   A CA  
1140 C C   . GLU   A 151 ? 0.2655 0.2434 0.2735 0.0253  -0.0590 0.0048  150 GLU   A C   
1141 O O   . GLU   A 151 ? 0.2630 0.2377 0.2659 0.0244  -0.0585 0.0013  150 GLU   A O   
1142 C CB  . GLU   A 151 ? 0.3238 0.2938 0.3119 0.0302  -0.0693 0.0089  150 GLU   A CB  
1143 C CG  . GLU   A 151 ? 0.3802 0.3495 0.3683 0.0317  -0.0790 0.0108  150 GLU   A CG  
1144 C CD  . GLU   A 151 ? 0.5121 0.4734 0.4792 0.0350  -0.0817 0.0140  150 GLU   A CD  
1145 O OE1 . GLU   A 151 ? 0.5217 0.4773 0.4717 0.0361  -0.0791 0.0120  150 GLU   A OE1 
1146 O OE2 . GLU   A 151 ? 0.5692 0.5298 0.5365 0.0368  -0.0864 0.0187  150 GLU   A OE2 
1147 N N   . VAL   A 152 ? 0.2436 0.2252 0.2586 0.0253  -0.0526 0.0079  151 VAL   A N   
1148 C CA  . VAL   A 152 ? 0.2429 0.2265 0.2613 0.0240  -0.0449 0.0074  151 VAL   A CA  
1149 C C   . VAL   A 152 ? 0.2567 0.2376 0.2653 0.0262  -0.0390 0.0103  151 VAL   A C   
1150 O O   . VAL   A 152 ? 0.2745 0.2549 0.2819 0.0274  -0.0381 0.0145  151 VAL   A O   
1151 C CB  . VAL   A 152 ? 0.2437 0.2341 0.2786 0.0219  -0.0425 0.0077  151 VAL   A CB  
1152 C CG1 . VAL   A 152 ? 0.2531 0.2452 0.2905 0.0206  -0.0353 0.0077  151 VAL   A CG1 
1153 C CG2 . VAL   A 152 ? 0.2472 0.2418 0.2926 0.0193  -0.0469 0.0048  151 VAL   A CG2 
1154 N N   . ARG   A 153 ? 0.2514 0.2302 0.2531 0.0267  -0.0350 0.0084  152 ARG   A N   
1155 C CA  . ARG   A 153 ? 0.2553 0.2332 0.2491 0.0288  -0.0287 0.0110  152 ARG   A CA  
1156 C C   . ARG   A 153 ? 0.2401 0.2208 0.2389 0.0281  -0.0230 0.0096  152 ARG   A C   
1157 O O   . ARG   A 153 ? 0.2465 0.2253 0.2443 0.0281  -0.0243 0.0057  152 ARG   A O   
1158 C CB  . ARG   A 153 ? 0.3127 0.2848 0.2891 0.0320  -0.0299 0.0097  152 ARG   A CB  
1159 C CG  . ARG   A 153 ? 0.3961 0.3637 0.3640 0.0329  -0.0377 0.0096  152 ARG   A CG  
1160 C CD  . ARG   A 153 ? 0.4509 0.4166 0.4088 0.0349  -0.0359 0.0152  152 ARG   A CD  
1161 N NE  . ARG   A 153 ? 0.4933 0.4540 0.4407 0.0363  -0.0440 0.0158  152 ARG   A NE  
1162 C CZ  . ARG   A 153 ? 0.5223 0.4840 0.4774 0.0355  -0.0505 0.0181  152 ARG   A CZ  
1163 N NH1 . ARG   A 153 ? 0.5186 0.4755 0.4631 0.0371  -0.0585 0.0189  152 ARG   A NH1 
1164 N NH2 . ARG   A 153 ? 0.5125 0.4797 0.4855 0.0334  -0.0493 0.0193  152 ARG   A NH2 
1165 N N   . LEU   A 154 ? 0.2076 0.1919 0.2106 0.0279  -0.0171 0.0129  153 LEU   A N   
1166 C CA  . LEU   A 154 ? 0.2079 0.1952 0.2149 0.0279  -0.0121 0.0119  153 LEU   A CA  
1167 C C   . LEU   A 154 ? 0.2342 0.2186 0.2295 0.0315  -0.0097 0.0100  153 LEU   A C   
1168 O O   . LEU   A 154 ? 0.2419 0.2244 0.2266 0.0337  -0.0083 0.0120  153 LEU   A O   
1169 C CB  . LEU   A 154 ? 0.2091 0.2009 0.2229 0.0267  -0.0070 0.0161  153 LEU   A CB  
1170 C CG  . LEU   A 154 ? 0.2048 0.1988 0.2299 0.0236  -0.0085 0.0173  153 LEU   A CG  
1171 C CD1 . LEU   A 154 ? 0.2060 0.2027 0.2368 0.0222  -0.0043 0.0214  153 LEU   A CD1 
1172 C CD2 . LEU   A 154 ? 0.2188 0.2149 0.2516 0.0217  -0.0097 0.0137  153 LEU   A CD2 
1173 N N   . ALA   A 155 ? 0.2347 0.2182 0.2307 0.0326  -0.0095 0.0062  154 ALA   A N   
1174 C CA  . ALA   A 155 ? 0.2564 0.2367 0.2419 0.0369  -0.0072 0.0033  154 ALA   A CA  
1175 C C   . ALA   A 155 ? 0.2728 0.2575 0.2548 0.0394  0.0005  0.0064  154 ALA   A C   
1176 O O   . ALA   A 155 ? 0.2927 0.2746 0.2617 0.0431  0.0027  0.0053  154 ALA   A O   
1177 C CB  . ALA   A 155 ? 0.2541 0.2331 0.2443 0.0377  -0.0076 -0.0005 154 ALA   A CB  
1178 N N   . ASP   A 156 ? 0.2665 0.2581 0.2600 0.0373  0.0046  0.0101  155 ASP   A N   
1179 C CA  . ASP   A 156 ? 0.2659 0.2633 0.2596 0.0385  0.0121  0.0140  155 ASP   A CA  
1180 C C   . ASP   A 156 ? 0.2689 0.2717 0.2757 0.0340  0.0134  0.0189  155 ASP   A C   
1181 O O   . ASP   A 156 ? 0.2602 0.2617 0.2739 0.0309  0.0086  0.0186  155 ASP   A O   
1182 C CB  . ASP   A 156 ? 0.2767 0.2778 0.2719 0.0425  0.0173  0.0112  155 ASP   A CB  
1183 C CG  . ASP   A 156 ? 0.3039 0.3080 0.3124 0.0417  0.0156  0.0092  155 ASP   A CG  
1184 O OD1 . ASP   A 156 ? 0.2865 0.2926 0.3049 0.0373  0.0129  0.0113  155 ASP   A OD1 
1185 O OD2 . ASP   A 156 ? 0.3292 0.3331 0.3376 0.0457  0.0168  0.0055  155 ASP   A OD2 
1186 N N   . PHE   A 157 ? 0.2802 0.2890 0.2907 0.0335  0.0199  0.0233  156 PHE   A N   
1187 C CA  . PHE   A 157 ? 0.2799 0.2927 0.3029 0.0290  0.0206  0.0276  156 PHE   A CA  
1188 C C   . PHE   A 157 ? 0.2505 0.2691 0.2879 0.0276  0.0205  0.0258  156 PHE   A C   
1189 O O   . PHE   A 157 ? 0.2426 0.2652 0.2908 0.0239  0.0215  0.0289  156 PHE   A O   
1190 C CB  . PHE   A 157 ? 0.3020 0.3179 0.3238 0.0278  0.0268  0.0341  156 PHE   A CB  
1191 C CG  . PHE   A 157 ? 0.3286 0.3510 0.3480 0.0308  0.0349  0.0348  156 PHE   A CG  
1192 C CD1 . PHE   A 157 ? 0.3455 0.3762 0.3775 0.0314  0.0381  0.0332  156 PHE   A CD1 
1193 C CD2 . PHE   A 157 ? 0.3549 0.3757 0.3602 0.0328  0.0397  0.0378  156 PHE   A CD2 
1194 C CE1 . PHE   A 157 ? 0.3586 0.3969 0.3907 0.0345  0.0463  0.0339  156 PHE   A CE1 
1195 C CE2 . PHE   A 157 ? 0.3673 0.3952 0.3708 0.0357  0.0485  0.0385  156 PHE   A CE2 
1196 C CZ  . PHE   A 157 ? 0.3598 0.3969 0.3777 0.0367  0.0520  0.0363  156 PHE   A CZ  
1197 N N   . GLY   A 158 ? 0.2484 0.2667 0.2857 0.0304  0.0189  0.0211  157 GLY   A N   
1198 C CA  . GLY   A 158 ? 0.2360 0.2588 0.2853 0.0294  0.0176  0.0195  157 GLY   A CA  
1199 C C   . GLY   A 158 ? 0.2401 0.2700 0.2951 0.0327  0.0222  0.0190  157 GLY   A C   
1200 O O   . GLY   A 158 ? 0.2469 0.2772 0.2946 0.0370  0.0267  0.0181  157 GLY   A O   
1201 N N   . ILE   A 159 ? 0.2232 0.2591 0.2914 0.0310  0.0213  0.0195  158 ILE   A N   
1202 C CA  . ILE   A 159 ? 0.2271 0.2708 0.3036 0.0345  0.0248  0.0188  158 ILE   A CA  
1203 C C   . ILE   A 159 ? 0.2553 0.3092 0.3395 0.0344  0.0325  0.0228  158 ILE   A C   
1204 O O   . ILE   A 159 ? 0.2657 0.3276 0.3584 0.0379  0.0358  0.0220  158 ILE   A O   
1205 C CB  . ILE   A 159 ? 0.2121 0.2583 0.3000 0.0328  0.0195  0.0178  158 ILE   A CB  
1206 C CG1 . ILE   A 159 ? 0.2162 0.2671 0.3149 0.0268  0.0184  0.0211  158 ILE   A CG1 
1207 C CG2 . ILE   A 159 ? 0.2158 0.2527 0.2964 0.0329  0.0128  0.0144  158 ILE   A CG2 
1208 C CD1 . ILE   A 159 ? 0.2273 0.2827 0.3378 0.0258  0.0138  0.0203  158 ILE   A CD1 
1209 N N   . SER   A 160 ? 0.2649 0.3193 0.3485 0.0302  0.0351  0.0274  159 SER   A N   
1210 C CA  . SER   A 160 ? 0.2826 0.3472 0.3759 0.0283  0.0421  0.0323  159 SER   A CA  
1211 C C   . SER   A 160 ? 0.3246 0.3946 0.4123 0.0329  0.0513  0.0333  159 SER   A C   
1212 O O   . SER   A 160 ? 0.3266 0.4069 0.4247 0.0311  0.0580  0.0377  159 SER   A O   
1213 C CB  . SER   A 160 ? 0.2798 0.3419 0.3744 0.0220  0.0417  0.0375  159 SER   A CB  
1214 O OG  . SER   A 160 ? 0.2833 0.3365 0.3617 0.0226  0.0421  0.0388  159 SER   A OG  
1215 N N   . ALA   A 161 ? 0.3488 0.4126 0.4213 0.0387  0.0520  0.0291  160 ALA   A N   
1216 C CA  . ALA   A 161 ? 0.3759 0.4447 0.4415 0.0437  0.0612  0.0290  160 ALA   A CA  
1217 C C   . ALA   A 161 ? 0.3965 0.4788 0.4790 0.0470  0.0664  0.0280  160 ALA   A C   
1218 O O   . ALA   A 161 ? 0.3956 0.4777 0.4843 0.0505  0.0618  0.0232  160 ALA   A O   
1219 C CB  . ALA   A 161 ? 0.3856 0.4440 0.4321 0.0496  0.0594  0.0232  160 ALA   A CB  
1220 N N   . GLN   A 162 ? 0.4075 0.5017 0.4984 0.0455  0.0756  0.0331  161 GLN   A N   
1221 C CA  . GLN   A 162 ? 0.4201 0.5297 0.5298 0.0483  0.0814  0.0329  161 GLN   A CA  
1222 C C   . GLN   A 162 ? 0.4346 0.5472 0.5360 0.0573  0.0892  0.0283  161 GLN   A C   
1223 O O   . GLN   A 162 ? 0.4376 0.5635 0.5471 0.0594  0.0996  0.0304  161 GLN   A O   
1224 C CB  . GLN   A 162 ? 0.4449 0.5669 0.5697 0.0418  0.0878  0.0407  161 GLN   A CB  
1225 C CG  . GLN   A 162 ? 0.5068 0.6255 0.6412 0.0331  0.0797  0.0445  161 GLN   A CG  
1226 C CD  . GLN   A 162 ? 0.5914 0.7247 0.7482 0.0275  0.0841  0.0503  161 GLN   A CD  
1227 O OE1 . GLN   A 162 ? 0.6174 0.7622 0.7935 0.0289  0.0833  0.0486  161 GLN   A OE1 
1228 N NE2 . GLN   A 162 ? 0.6084 0.7416 0.7641 0.0210  0.0883  0.0575  161 GLN   A NE2 
1229 N N   . ILE   A 163 ? 0.4441 0.5440 0.5293 0.0626  0.0842  0.0218  162 ILE   A N   
1230 C CA  . ILE   A 163 ? 0.4547 0.5531 0.5290 0.0719  0.0894  0.0154  162 ILE   A CA  
1231 C C   . ILE   A 163 ? 0.4517 0.5390 0.5231 0.0763  0.0796  0.0082  162 ILE   A C   
1232 O O   . ILE   A 163 ? 0.4619 0.5406 0.5333 0.0716  0.0698  0.0086  162 ILE   A O   
1233 C CB  . ILE   A 163 ? 0.4816 0.5726 0.5309 0.0734  0.0949  0.0155  162 ILE   A CB  
1234 C CG1 . ILE   A 163 ? 0.5096 0.5868 0.5447 0.0673  0.0867  0.0180  162 ILE   A CG1 
1235 C CG2 . ILE   A 163 ? 0.4857 0.5899 0.5369 0.0729  0.1083  0.0211  162 ILE   A CG2 
1236 C CD1 . ILE   A 163 ? 0.5450 0.6123 0.5537 0.0697  0.0890  0.0168  162 ILE   A CD1 
1237 N N   . GLY   A 164 ? 0.4421 0.5292 0.5109 0.0852  0.0826  0.0017  163 GLY   A N   
1238 C CA  . GLY   A 164 ? 0.4407 0.5161 0.5062 0.0896  0.0737  -0.0050 163 GLY   A CA  
1239 C C   . GLY   A 164 ? 0.4218 0.5007 0.5071 0.0881  0.0662  -0.0041 163 GLY   A C   
1240 O O   . GLY   A 164 ? 0.4055 0.4992 0.5106 0.0873  0.0696  -0.0007 163 GLY   A O   
1241 N N   . ALA   A 165 ? 0.4155 0.4809 0.4954 0.0874  0.0557  -0.0069 164 ALA   A N   
1242 C CA  . ALA   A 165 ? 0.3980 0.4642 0.4930 0.0861  0.0476  -0.0061 164 ALA   A CA  
1243 C C   . ALA   A 165 ? 0.3733 0.4421 0.4749 0.0765  0.0429  -0.0001 164 ALA   A C   
1244 O O   . ALA   A 165 ? 0.3806 0.4403 0.4797 0.0728  0.0340  0.0000  164 ALA   A O   
1245 C CB  . ALA   A 165 ? 0.4092 0.4594 0.4948 0.0894  0.0390  -0.0112 164 ALA   A CB  
1246 N N   . GLU   A 166 ? 0.3375 0.4184 0.4475 0.0723  0.0492  0.0049  165 GLU   A N   
1247 C CA  . GLU   A 166 ? 0.3079 0.3913 0.4246 0.0634  0.0455  0.0102  165 GLU   A CA  
1248 C C   . GLU   A 166 ? 0.2755 0.3597 0.4050 0.0615  0.0367  0.0105  165 GLU   A C   
1249 O O   . GLU   A 166 ? 0.2799 0.3564 0.4048 0.0560  0.0298  0.0115  165 GLU   A O   
1250 C CB  . GLU   A 166 ? 0.3221 0.4197 0.4495 0.0600  0.0540  0.0155  165 GLU   A CB  
1251 C CG  . GLU   A 166 ? 0.3529 0.4511 0.4856 0.0507  0.0505  0.0208  165 GLU   A CG  
1252 C CD  . GLU   A 166 ? 0.3794 0.4843 0.5307 0.0472  0.0442  0.0221  165 GLU   A CD  
1253 O OE1 . GLU   A 166 ? 0.3676 0.4834 0.5344 0.0511  0.0454  0.0214  165 GLU   A OE1 
1254 O OE2 . GLU   A 166 ? 0.3836 0.4827 0.5339 0.0409  0.0376  0.0236  165 GLU   A OE2 
1255 N N   . LEU   A 167 ? 0.2484 0.3419 0.3935 0.0664  0.0367  0.0093  166 LEU   A N   
1256 C CA  . LEU   A 167 ? 0.2343 0.3286 0.3909 0.0646  0.0276  0.0101  166 LEU   A CA  
1257 C C   . LEU   A 167 ? 0.2376 0.3162 0.3815 0.0651  0.0188  0.0075  166 LEU   A C   
1258 O O   . LEU   A 167 ? 0.2354 0.3098 0.3791 0.0596  0.0114  0.0093  166 LEU   A O   
1259 C CB  . LEU   A 167 ? 0.2314 0.3393 0.4081 0.0703  0.0288  0.0096  166 LEU   A CB  
1260 C CG  . LEU   A 167 ? 0.2481 0.3578 0.4372 0.0684  0.0186  0.0110  166 LEU   A CG  
1261 C CD1 . LEU   A 167 ? 0.2468 0.3615 0.4426 0.0588  0.0158  0.0153  166 LEU   A CD1 
1262 C CD2 . LEU   A 167 ? 0.2447 0.3672 0.4535 0.0754  0.0192  0.0101  166 LEU   A CD2 
1263 N N   . ALA   A 168 ? 0.2492 0.3186 0.3821 0.0714  0.0195  0.0032  167 ALA   A N   
1264 C CA  . ALA   A 168 ? 0.2627 0.3163 0.3837 0.0713  0.0114  0.0011  167 ALA   A CA  
1265 C C   . ALA   A 168 ? 0.2611 0.3064 0.3692 0.0635  0.0091  0.0028  167 ALA   A C   
1266 O O   . ALA   A 168 ? 0.2587 0.2963 0.3629 0.0596  0.0020  0.0036  167 ALA   A O   
1267 C CB  . ALA   A 168 ? 0.2799 0.3247 0.3912 0.0789  0.0132  -0.0041 167 ALA   A CB  
1268 N N   . ARG   A 169 ? 0.2508 0.2983 0.3526 0.0614  0.0154  0.0034  168 ARG   A N   
1269 C CA  . ARG   A 169 ? 0.2546 0.2953 0.3460 0.0549  0.0135  0.0050  168 ARG   A CA  
1270 C C   . ARG   A 169 ? 0.2359 0.2810 0.3355 0.0481  0.0100  0.0086  168 ARG   A C   
1271 O O   . ARG   A 169 ? 0.2376 0.2757 0.3313 0.0436  0.0050  0.0089  168 ARG   A O   
1272 C CB  . ARG   A 169 ? 0.2831 0.3254 0.3665 0.0548  0.0206  0.0055  168 ARG   A CB  
1273 C CG  . ARG   A 169 ? 0.3389 0.3688 0.4059 0.0547  0.0180  0.0029  168 ARG   A CG  
1274 C CD  . ARG   A 169 ? 0.3501 0.3799 0.4075 0.0536  0.0230  0.0041  168 ARG   A CD  
1275 N NE  . ARG   A 169 ? 0.3519 0.3736 0.4012 0.0486  0.0179  0.0048  168 ARG   A NE  
1276 C CZ  . ARG   A 169 ? 0.3654 0.3836 0.4043 0.0472  0.0192  0.0056  168 ARG   A CZ  
1277 N NH1 . ARG   A 169 ? 0.3567 0.3688 0.3910 0.0431  0.0141  0.0060  168 ARG   A NH1 
1278 N NH2 . ARG   A 169 ? 0.3600 0.3813 0.3928 0.0502  0.0258  0.0062  168 ARG   A NH2 
1279 N N   . ARG   A 170 ? 0.2109 0.2681 0.3246 0.0474  0.0128  0.0111  169 ARG   A N   
1280 C CA  . ARG   A 170 ? 0.1949 0.2565 0.3172 0.0410  0.0094  0.0141  169 ARG   A CA  
1281 C C   . ARG   A 170 ? 0.1884 0.2460 0.3127 0.0399  0.0007  0.0134  169 ARG   A C   
1282 O O   . ARG   A 170 ? 0.1813 0.2359 0.3036 0.0345  -0.0036 0.0143  169 ARG   A O   
1283 C CB  . ARG   A 170 ? 0.2075 0.2835 0.3464 0.0411  0.0141  0.0166  169 ARG   A CB  
1284 C CG  . ARG   A 170 ? 0.2212 0.3019 0.3690 0.0339  0.0119  0.0196  169 ARG   A CG  
1285 C CD  . ARG   A 170 ? 0.2038 0.2981 0.3714 0.0342  0.0119  0.0213  169 ARG   A CD  
1286 N NE  . ARG   A 170 ? 0.2092 0.3144 0.3848 0.0380  0.0212  0.0225  169 ARG   A NE  
1287 C CZ  . ARG   A 170 ? 0.2116 0.3311 0.4066 0.0391  0.0231  0.0240  169 ARG   A CZ  
1288 N NH1 . ARG   A 170 ? 0.2197 0.3496 0.4211 0.0429  0.0328  0.0250  169 ARG   A NH1 
1289 N NH2 . ARG   A 170 ? 0.1844 0.3087 0.3926 0.0366  0.0154  0.0244  169 ARG   A NH2 
1290 N N   . LEU   A 171 ? 0.1859 0.2437 0.3143 0.0455  -0.0019 0.0119  170 LEU   A N   
1291 C CA  . LEU   A 171 ? 0.1885 0.2424 0.3182 0.0449  -0.0104 0.0121  170 LEU   A CA  
1292 C C   . LEU   A 171 ? 0.1919 0.2315 0.3067 0.0449  -0.0147 0.0108  170 LEU   A C   
1293 O O   . LEU   A 171 ? 0.1878 0.2227 0.3011 0.0438  -0.0216 0.0117  170 LEU   A O   
1294 C CB  . LEU   A 171 ? 0.1855 0.2465 0.3286 0.0512  -0.0121 0.0119  170 LEU   A CB  
1295 C CG  . LEU   A 171 ? 0.2167 0.2940 0.3782 0.0517  -0.0080 0.0134  170 LEU   A CG  
1296 C CD1 . LEU   A 171 ? 0.2082 0.2926 0.3840 0.0590  -0.0103 0.0127  170 LEU   A CD1 
1297 C CD2 . LEU   A 171 ? 0.2419 0.3240 0.4097 0.0440  -0.0117 0.0160  170 LEU   A CD2 
1298 N N   . GLU   A 172 ? 0.1986 0.2314 0.3026 0.0461  -0.0110 0.0088  171 GLU   A N   
1299 C CA  . GLU   A 172 ? 0.2043 0.2240 0.2956 0.0457  -0.0146 0.0075  171 GLU   A CA  
1300 C C   . GLU   A 172 ? 0.1982 0.2130 0.2840 0.0392  -0.0195 0.0094  171 GLU   A C   
1301 O O   . GLU   A 172 ? 0.2141 0.2206 0.2946 0.0391  -0.0245 0.0098  171 GLU   A O   
1302 C CB  . GLU   A 172 ? 0.2351 0.2499 0.3167 0.0468  -0.0102 0.0052  171 GLU   A CB  
1303 C CG  . GLU   A 172 ? 0.2977 0.2994 0.3682 0.0468  -0.0140 0.0034  171 GLU   A CG  
1304 C CD  . GLU   A 172 ? 0.3429 0.3397 0.4048 0.0498  -0.0106 0.0000  171 GLU   A CD  
1305 O OE1 . GLU   A 172 ? 0.3519 0.3380 0.4069 0.0519  -0.0137 -0.0024 171 GLU   A OE1 
1306 O OE2 . GLU   A 172 ? 0.3380 0.3409 0.3995 0.0499  -0.0051 0.0000  171 GLU   A OE2 
1307 N N   . PHE   A 173 ? 0.1712 0.1907 0.2581 0.0340  -0.0180 0.0105  172 PHE   A N   
1308 C CA  . PHE   A 173 ? 0.1639 0.1793 0.2452 0.0284  -0.0218 0.0115  172 PHE   A CA  
1309 C C   . PHE   A 173 ? 0.1625 0.1771 0.2456 0.0279  -0.0281 0.0131  172 PHE   A C   
1310 O O   . PHE   A 173 ? 0.1604 0.1692 0.2355 0.0242  -0.0313 0.0139  172 PHE   A O   
1311 C CB  . PHE   A 173 ? 0.1558 0.1763 0.2393 0.0239  -0.0193 0.0117  172 PHE   A CB  
1312 C CG  . PHE   A 173 ? 0.1534 0.1820 0.2474 0.0226  -0.0210 0.0128  172 PHE   A CG  
1313 C CD1 . PHE   A 173 ? 0.1660 0.2034 0.2712 0.0250  -0.0178 0.0135  172 PHE   A CD1 
1314 C CD2 . PHE   A 173 ? 0.1644 0.1921 0.2571 0.0189  -0.0261 0.0131  172 PHE   A CD2 
1315 C CE1 . PHE   A 173 ? 0.1778 0.2233 0.2946 0.0234  -0.0201 0.0146  172 PHE   A CE1 
1316 C CE2 . PHE   A 173 ? 0.1725 0.2072 0.2751 0.0176  -0.0289 0.0137  172 PHE   A CE2 
1317 C CZ  . PHE   A 173 ? 0.1768 0.2205 0.2923 0.0196  -0.0262 0.0146  172 PHE   A CZ  
1318 N N   . ILE   A 174 ? 0.1826 0.2034 0.2762 0.0316  -0.0302 0.0138  173 ILE   A N   
1319 C CA  . ILE   A 174 ? 0.1948 0.2144 0.2896 0.0314  -0.0375 0.0156  173 ILE   A CA  
1320 C C   . ILE   A 174 ? 0.2210 0.2285 0.3051 0.0324  -0.0415 0.0167  173 ILE   A C   
1321 O O   . ILE   A 174 ? 0.2425 0.2452 0.3199 0.0293  -0.0466 0.0188  173 ILE   A O   
1322 C CB  . ILE   A 174 ? 0.1942 0.2236 0.3042 0.0358  -0.0390 0.0161  173 ILE   A CB  
1323 C CG1 . ILE   A 174 ? 0.1904 0.2309 0.3106 0.0324  -0.0364 0.0160  173 ILE   A CG1 
1324 C CG2 . ILE   A 174 ? 0.2140 0.2408 0.3250 0.0370  -0.0478 0.0182  173 ILE   A CG2 
1325 C CD1 . ILE   A 174 ? 0.2027 0.2560 0.3416 0.0365  -0.0362 0.0165  173 ILE   A CD1 
1326 N N   . GLY   A 175 ? 0.2142 0.2162 0.2956 0.0362  -0.0388 0.0152  174 GLY   A N   
1327 C CA  . GLY   A 175 ? 0.2260 0.2155 0.2980 0.0365  -0.0423 0.0162  174 GLY   A CA  
1328 C C   . GLY   A 175 ? 0.2236 0.2065 0.2845 0.0309  -0.0402 0.0161  174 GLY   A C   
1329 O O   . GLY   A 175 ? 0.2327 0.2052 0.2860 0.0298  -0.0429 0.0174  174 GLY   A O   
1330 N N   . THR   A 176 ? 0.2121 0.2009 0.2728 0.0273  -0.0356 0.0148  175 THR   A N   
1331 C CA  . THR   A 176 ? 0.2038 0.1886 0.2566 0.0225  -0.0332 0.0143  175 THR   A CA  
1332 C C   . THR   A 176 ? 0.1950 0.1878 0.2500 0.0190  -0.0298 0.0134  175 THR   A C   
1333 O O   . THR   A 176 ? 0.1899 0.1865 0.2476 0.0197  -0.0256 0.0117  175 THR   A O   
1334 C CB  . THR   A 176 ? 0.2230 0.2027 0.2733 0.0248  -0.0309 0.0120  175 THR   A CB  
1335 O OG1 . THR   A 176 ? 0.2417 0.2204 0.2872 0.0202  -0.0287 0.0114  175 THR   A OG1 
1336 C CG2 . THR   A 176 ? 0.2181 0.2035 0.2742 0.0300  -0.0271 0.0095  175 THR   A CG2 
1337 N N   . PRO   A 177 ? 0.1841 0.1791 0.2381 0.0157  -0.0321 0.0146  176 PRO   A N   
1338 C CA  . PRO   A 177 ? 0.1650 0.1669 0.2227 0.0132  -0.0299 0.0133  176 PRO   A CA  
1339 C C   . PRO   A 177 ? 0.1611 0.1617 0.2128 0.0089  -0.0274 0.0122  176 PRO   A C   
1340 O O   . PRO   A 177 ? 0.1663 0.1709 0.2200 0.0068  -0.0263 0.0109  176 PRO   A O   
1341 C CB  . PRO   A 177 ? 0.1820 0.1862 0.2413 0.0124  -0.0348 0.0145  176 PRO   A CB  
1342 C CG  . PRO   A 177 ? 0.2086 0.2048 0.2586 0.0116  -0.0388 0.0169  176 PRO   A CG  
1343 C CD  . PRO   A 177 ? 0.1857 0.1765 0.2352 0.0147  -0.0376 0.0173  176 PRO   A CD  
1344 N N   . TYR   A 178 ? 0.1564 0.1515 0.2018 0.0075  -0.0267 0.0128  177 TYR   A N   
1345 C CA  . TYR   A 178 ? 0.1449 0.1395 0.1854 0.0033  -0.0243 0.0120  177 TYR   A CA  
1346 C C   . TYR   A 178 ? 0.1528 0.1521 0.1976 0.0030  -0.0205 0.0095  177 TYR   A C   
1347 O O   . TYR   A 178 ? 0.1571 0.1579 0.2000 0.0003  -0.0187 0.0082  177 TYR   A O   
1348 C CB  . TYR   A 178 ? 0.1443 0.1330 0.1798 0.0017  -0.0242 0.0134  177 TYR   A CB  
1349 C CG  . TYR   A 178 ? 0.1574 0.1396 0.1890 0.0026  -0.0285 0.0164  177 TYR   A CG  
1350 C CD1 . TYR   A 178 ? 0.1702 0.1498 0.1950 -0.0002 -0.0308 0.0190  177 TYR   A CD1 
1351 C CD2 . TYR   A 178 ? 0.1588 0.1368 0.1928 0.0065  -0.0303 0.0165  177 TYR   A CD2 
1352 C CE1 . TYR   A 178 ? 0.1745 0.1471 0.1956 0.0008  -0.0355 0.0225  177 TYR   A CE1 
1353 C CE2 . TYR   A 178 ? 0.1745 0.1457 0.2060 0.0081  -0.0348 0.0191  177 TYR   A CE2 
1354 C CZ  . TYR   A 178 ? 0.1859 0.1541 0.2110 0.0051  -0.0377 0.0225  177 TYR   A CZ  
1355 O OH  . TYR   A 178 ? 0.2176 0.1777 0.2396 0.0065  -0.0427 0.0258  177 TYR   A OH  
1356 N N   . TRP   A 179 ? 0.1328 0.1340 0.1829 0.0060  -0.0191 0.0089  178 TRP   A N   
1357 C CA  . TRP   A 179 ? 0.1313 0.1357 0.1850 0.0058  -0.0161 0.0074  178 TRP   A CA  
1358 C C   . TRP   A 179 ? 0.1163 0.1251 0.1759 0.0061  -0.0157 0.0071  178 TRP   A C   
1359 O O   . TRP   A 179 ? 0.1306 0.1411 0.1932 0.0058  -0.0136 0.0063  178 TRP   A O   
1360 C CB  . TRP   A 179 ? 0.1333 0.1364 0.1874 0.0084  -0.0147 0.0073  178 TRP   A CB  
1361 C CG  . TRP   A 179 ? 0.1388 0.1378 0.1886 0.0073  -0.0153 0.0070  178 TRP   A CG  
1362 C CD1 . TRP   A 179 ? 0.1503 0.1500 0.2005 0.0058  -0.0143 0.0060  178 TRP   A CD1 
1363 C CD2 . TRP   A 179 ? 0.1432 0.1368 0.1892 0.0077  -0.0176 0.0077  178 TRP   A CD2 
1364 N NE1 . TRP   A 179 ? 0.1538 0.1497 0.2013 0.0045  -0.0157 0.0061  178 TRP   A NE1 
1365 C CE2 . TRP   A 179 ? 0.1575 0.1487 0.2019 0.0055  -0.0178 0.0072  178 TRP   A CE2 
1366 C CE3 . TRP   A 179 ? 0.1640 0.1541 0.2086 0.0096  -0.0200 0.0089  178 TRP   A CE3 
1367 C CZ2 . TRP   A 179 ? 0.1658 0.1506 0.2069 0.0047  -0.0203 0.0077  178 TRP   A CZ2 
1368 C CZ3 . TRP   A 179 ? 0.1770 0.1599 0.2177 0.0094  -0.0225 0.0094  178 TRP   A CZ3 
1369 C CH2 . TRP   A 179 ? 0.1770 0.1570 0.2158 0.0066  -0.0226 0.0089  178 TRP   A CH2 
1370 N N   . MET   A 180 ? 0.1121 0.1227 0.1741 0.0064  -0.0182 0.0078  179 MET   A N   
1371 C CA  . MET   A 180 ? 0.1059 0.1210 0.1754 0.0059  -0.0182 0.0077  179 MET   A CA  
1372 C C   . MET   A 180 ? 0.1174 0.1323 0.1857 0.0027  -0.0200 0.0057  179 MET   A C   
1373 O O   . MET   A 180 ? 0.1157 0.1281 0.1772 0.0012  -0.0222 0.0050  179 MET   A O   
1374 C CB  . MET   A 180 ? 0.1148 0.1335 0.1903 0.0082  -0.0201 0.0093  179 MET   A CB  
1375 C CG  . MET   A 180 ? 0.1594 0.1788 0.2366 0.0121  -0.0174 0.0104  179 MET   A CG  
1376 S SD  . MET   A 180 ? 0.1677 0.1900 0.2485 0.0129  -0.0120 0.0110  179 MET   A SD  
1377 C CE  . MET   A 180 ? 0.2266 0.2424 0.2975 0.0142  -0.0107 0.0100  179 MET   A CE  
1378 N N   . ALA   A 181 ? 0.1213 0.1382 0.1958 0.0016  -0.0191 0.0050  180 ALA   A N   
1379 C CA  . ALA   A 181 ? 0.1430 0.1588 0.2169 -0.0012 -0.0210 0.0022  180 ALA   A CA  
1380 C C   . ALA   A 181 ? 0.1615 0.1787 0.2360 -0.0024 -0.0261 0.0020  180 ALA   A C   
1381 O O   . ALA   A 181 ? 0.1493 0.1700 0.2290 -0.0010 -0.0279 0.0044  180 ALA   A O   
1382 C CB  . ALA   A 181 ? 0.1361 0.1527 0.2177 -0.0019 -0.0194 0.0021  180 ALA   A CB  
1383 N N   . PRO   A 182 ? 0.1762 0.1907 0.2448 -0.0047 -0.0289 -0.0012 181 PRO   A N   
1384 C CA  . PRO   A 182 ? 0.1710 0.1862 0.2385 -0.0059 -0.0350 -0.0014 181 PRO   A CA  
1385 C C   . PRO   A 182 ? 0.1675 0.1878 0.2484 -0.0066 -0.0379 -0.0002 181 PRO   A C   
1386 O O   . PRO   A 182 ? 0.1734 0.1970 0.2579 -0.0059 -0.0424 0.0016  181 PRO   A O   
1387 C CB  . PRO   A 182 ? 0.1943 0.2050 0.2518 -0.0083 -0.0365 -0.0059 181 PRO   A CB  
1388 C CG  . PRO   A 182 ? 0.2114 0.2197 0.2637 -0.0076 -0.0303 -0.0073 181 PRO   A CG  
1389 C CD  . PRO   A 182 ? 0.1840 0.1947 0.2462 -0.0059 -0.0266 -0.0049 181 PRO   A CD  
1390 N N   . GLU   A 183 ? 0.1548 0.1763 0.2443 -0.0076 -0.0352 -0.0005 182 GLU   A N   
1391 C CA  . GLU   A 183 ? 0.1520 0.1794 0.2558 -0.0090 -0.0372 0.0013  182 GLU   A CA  
1392 C C   . GLU   A 183 ? 0.1485 0.1826 0.2602 -0.0059 -0.0345 0.0057  182 GLU   A C   
1393 O O   . GLU   A 183 ? 0.1454 0.1865 0.2692 -0.0064 -0.0368 0.0075  182 GLU   A O   
1394 C CB  . GLU   A 183 ? 0.1666 0.1922 0.2770 -0.0116 -0.0353 0.0005  182 GLU   A CB  
1395 C CG  . GLU   A 183 ? 0.1907 0.2154 0.3012 -0.0098 -0.0286 0.0028  182 GLU   A CG  
1396 C CD  . GLU   A 183 ? 0.1718 0.1899 0.2720 -0.0086 -0.0260 0.0001  182 GLU   A CD  
1397 O OE1 . GLU   A 183 ? 0.1512 0.1659 0.2421 -0.0087 -0.0280 -0.0035 182 GLU   A OE1 
1398 O OE2 . GLU   A 183 ? 0.1575 0.1743 0.2593 -0.0077 -0.0219 0.0018  182 GLU   A OE2 
1399 N N   . VAL   A 184 ? 0.1496 0.1820 0.2549 -0.0026 -0.0300 0.0070  183 VAL   A N   
1400 C CA  . VAL   A 184 ? 0.1475 0.1847 0.2575 0.0013  -0.0274 0.0100  183 VAL   A CA  
1401 C C   . VAL   A 184 ? 0.1631 0.2000 0.2695 0.0035  -0.0322 0.0102  183 VAL   A C   
1402 O O   . VAL   A 184 ? 0.1563 0.1991 0.2715 0.0061  -0.0334 0.0120  183 VAL   A O   
1403 C CB  . VAL   A 184 ? 0.1556 0.1896 0.2594 0.0037  -0.0215 0.0107  183 VAL   A CB  
1404 C CG1 . VAL   A 184 ? 0.1654 0.2025 0.2712 0.0082  -0.0192 0.0125  183 VAL   A CG1 
1405 C CG2 . VAL   A 184 ? 0.1502 0.1843 0.2577 0.0019  -0.0175 0.0114  183 VAL   A CG2 
1406 N N   . ALA   A 185 ? 0.1636 0.1936 0.2574 0.0025  -0.0348 0.0087  184 ALA   A N   
1407 C CA  . ALA   A 185 ? 0.1824 0.2103 0.2706 0.0037  -0.0400 0.0095  184 ALA   A CA  
1408 C C   . ALA   A 185 ? 0.1705 0.2029 0.2661 0.0027  -0.0469 0.0097  184 ALA   A C   
1409 O O   . ALA   A 185 ? 0.1702 0.2029 0.2658 0.0050  -0.0518 0.0114  184 ALA   A O   
1410 C CB  . ALA   A 185 ? 0.2013 0.2214 0.2740 0.0017  -0.0405 0.0082  184 ALA   A CB  
1411 N N   . ALA   A 186 ? 0.1602 0.1956 0.2625 -0.0007 -0.0482 0.0079  185 ALA   A N   
1412 C CA  . ALA   A 186 ? 0.1640 0.2048 0.2760 -0.0023 -0.0553 0.0078  185 ALA   A CA  
1413 C C   . ALA   A 186 ? 0.1700 0.2213 0.3004 0.0001  -0.0536 0.0106  185 ALA   A C   
1414 O O   . ALA   A 186 ? 0.1611 0.2195 0.3056 -0.0023 -0.0556 0.0107  185 ALA   A O   
1415 C CB  . ALA   A 186 ? 0.1717 0.2108 0.2842 -0.0072 -0.0573 0.0044  185 ALA   A CB  
1416 N N   . VAL   A 187 ? 0.1802 0.2323 0.3105 0.0050  -0.0501 0.0127  186 VAL   A N   
1417 C CA  . VAL   A 187 ? 0.1703 0.2319 0.3158 0.0088  -0.0469 0.0149  186 VAL   A CA  
1418 C C   . VAL   A 187 ? 0.1492 0.2194 0.3089 0.0092  -0.0542 0.0158  186 VAL   A C   
1419 O O   . VAL   A 187 ? 0.1556 0.2224 0.3099 0.0093  -0.0624 0.0156  186 VAL   A O   
1420 C CB  . VAL   A 187 ? 0.1846 0.2424 0.3234 0.0144  -0.0429 0.0157  186 VAL   A CB  
1421 C CG1 . VAL   A 187 ? 0.1923 0.2435 0.3218 0.0165  -0.0497 0.0161  186 VAL   A CG1 
1422 C CG2 . VAL   A 187 ? 0.1858 0.2531 0.3385 0.0191  -0.0378 0.0171  186 VAL   A CG2 
1423 N N   . ALA   A 188 ? 0.1319 0.2138 0.3102 0.0092  -0.0513 0.0172  187 ALA   A N   
1424 C CA  . ALA   A 188 ? 0.1267 0.2199 0.3235 0.0095  -0.0577 0.0183  187 ALA   A CA  
1425 C C   . ALA   A 188 ? 0.1275 0.2204 0.3264 0.0034  -0.0668 0.0168  187 ALA   A C   
1426 O O   . ALA   A 188 ? 0.1362 0.2378 0.3497 0.0032  -0.0741 0.0175  187 ALA   A O   
1427 C CB  . ALA   A 188 ? 0.1307 0.2249 0.3287 0.0161  -0.0622 0.0193  187 ALA   A CB  
1428 N N   . LEU   A 189 ? 0.1490 0.2321 0.3341 -0.0014 -0.0668 0.0143  188 LEU   A N   
1429 C CA  . LEU   A 189 ? 0.1617 0.2434 0.3485 -0.0075 -0.0744 0.0119  188 LEU   A CA  
1430 C C   . LEU   A 189 ? 0.1486 0.2355 0.3492 -0.0122 -0.0692 0.0125  188 LEU   A C   
1431 O O   . LEU   A 189 ? 0.1451 0.2348 0.3493 -0.0106 -0.0596 0.0148  188 LEU   A O   
1432 C CB  . LEU   A 189 ? 0.1809 0.2488 0.3448 -0.0096 -0.0777 0.0083  188 LEU   A CB  
1433 C CG  . LEU   A 189 ? 0.2013 0.2640 0.3517 -0.0061 -0.0839 0.0087  188 LEU   A CG  
1434 C CD1 . LEU   A 189 ? 0.2343 0.2841 0.3610 -0.0079 -0.0842 0.0057  188 LEU   A CD1 
1435 C CD2 . LEU   A 189 ? 0.1972 0.2658 0.3569 -0.0065 -0.0955 0.0091  188 LEU   A CD2 
1436 N N   . LYS   A 190 ? 0.1406 0.2283 0.3486 -0.0181 -0.0759 0.0106  189 LYS   A N   
1437 C CA  . LYS   A 190 ? 0.1328 0.2258 0.3566 -0.0233 -0.0724 0.0120  189 LYS   A CA  
1438 C C   . LYS   A 190 ? 0.1453 0.2296 0.3599 -0.0250 -0.0641 0.0117  189 LYS   A C   
1439 O O   . LYS   A 190 ? 0.1373 0.2265 0.3643 -0.0277 -0.0581 0.0149  189 LYS   A O   
1440 C CB  . LYS   A 190 ? 0.1327 0.2266 0.3659 -0.0298 -0.0831 0.0094  189 LYS   A CB  
1441 C CG  . LYS   A 190 ? 0.1745 0.2530 0.3871 -0.0323 -0.0888 0.0036  189 LYS   A CG  
1442 C CD  . LYS   A 190 ? 0.2261 0.3040 0.4451 -0.0381 -0.1010 -0.0001 189 LYS   A CD  
1443 C CE  . LYS   A 190 ? 0.3104 0.3725 0.5066 -0.0397 -0.1051 -0.0066 189 LYS   A CE  
1444 N NZ  . LYS   A 190 ? 0.3719 0.4315 0.5700 -0.0447 -0.1181 -0.0113 189 LYS   A NZ  
1445 N N   . GLY   A 191 ? 0.1608 0.2325 0.3546 -0.0238 -0.0641 0.0083  190 GLY   A N   
1446 C CA  . GLY   A 191 ? 0.1920 0.2552 0.3778 -0.0252 -0.0576 0.0077  190 GLY   A CA  
1447 C C   . GLY   A 191 ? 0.2241 0.2900 0.4083 -0.0207 -0.0476 0.0115  190 GLY   A C   
1448 O O   . GLY   A 191 ? 0.2557 0.3231 0.4336 -0.0156 -0.0463 0.0121  190 GLY   A O   
1449 N N   . GLY   A 192 ? 0.2093 0.2749 0.3985 -0.0227 -0.0412 0.0141  191 GLY   A N   
1450 C CA  . GLY   A 192 ? 0.1846 0.2513 0.3694 -0.0185 -0.0320 0.0173  191 GLY   A CA  
1451 C C   . GLY   A 192 ? 0.1741 0.2289 0.3413 -0.0171 -0.0300 0.0148  191 GLY   A C   
1452 O O   . GLY   A 192 ? 0.1795 0.2272 0.3359 -0.0171 -0.0348 0.0104  191 GLY   A O   
1453 N N   . TYR   A 193 ? 0.1428 0.1964 0.3072 -0.0155 -0.0228 0.0177  192 TYR   A N   
1454 C CA  . TYR   A 193 ? 0.1433 0.1869 0.2934 -0.0139 -0.0207 0.0158  192 TYR   A CA  
1455 C C   . TYR   A 193 ? 0.1551 0.1970 0.3071 -0.0148 -0.0148 0.0198  192 TYR   A C   
1456 O O   . TYR   A 193 ? 0.1550 0.2033 0.3181 -0.0168 -0.0117 0.0243  192 TYR   A O   
1457 C CB  . TYR   A 193 ? 0.1392 0.1813 0.2771 -0.0088 -0.0197 0.0143  192 TYR   A CB  
1458 C CG  . TYR   A 193 ? 0.1400 0.1881 0.2794 -0.0048 -0.0144 0.0176  192 TYR   A CG  
1459 C CD1 . TYR   A 193 ? 0.1527 0.1989 0.2873 -0.0029 -0.0084 0.0199  192 TYR   A CD1 
1460 C CD2 . TYR   A 193 ? 0.1378 0.1930 0.2827 -0.0023 -0.0159 0.0180  192 TYR   A CD2 
1461 C CE1 . TYR   A 193 ? 0.1504 0.2011 0.2841 0.0013  -0.0037 0.0219  192 TYR   A CE1 
1462 C CE2 . TYR   A 193 ? 0.1410 0.2007 0.2862 0.0024  -0.0110 0.0199  192 TYR   A CE2 
1463 C CZ  . TYR   A 193 ? 0.1499 0.2075 0.2894 0.0040  -0.0046 0.0217  192 TYR   A CZ  
1464 O OH  . TYR   A 193 ? 0.1462 0.2081 0.2853 0.0086  0.0006  0.0230  192 TYR   A OH  
1465 N N   . ASN   A 194 ? 0.1455 0.1787 0.2871 -0.0136 -0.0136 0.0185  193 ASN   A N   
1466 C CA  . ASN   A 194 ? 0.1303 0.1604 0.2717 -0.0139 -0.0090 0.0226  193 ASN   A CA  
1467 C C   . ASN   A 194 ? 0.1334 0.1590 0.2616 -0.0093 -0.0065 0.0217  193 ASN   A C   
1468 O O   . ASN   A 194 ? 0.1467 0.1726 0.2678 -0.0064 -0.0077 0.0185  193 ASN   A O   
1469 C CB  . ASN   A 194 ? 0.1426 0.1658 0.2893 -0.0185 -0.0118 0.0224  193 ASN   A CB  
1470 C CG  . ASN   A 194 ? 0.1735 0.1878 0.3124 -0.0178 -0.0160 0.0163  193 ASN   A CG  
1471 O OD1 . ASN   A 194 ? 0.1515 0.1641 0.2802 -0.0139 -0.0154 0.0134  193 ASN   A OD1 
1472 N ND2 . ASN   A 194 ? 0.2029 0.2114 0.3469 -0.0215 -0.0201 0.0139  193 ASN   A ND2 
1473 N N   . GLU   A 195 ? 0.1338 0.1551 0.2593 -0.0090 -0.0036 0.0250  194 GLU   A N   
1474 C CA  . GLU   A 195 ? 0.1307 0.1484 0.2452 -0.0050 -0.0018 0.0248  194 GLU   A CA  
1475 C C   . GLU   A 195 ? 0.1411 0.1535 0.2492 -0.0035 -0.0052 0.0193  194 GLU   A C   
1476 O O   . GLU   A 195 ? 0.1484 0.1596 0.2486 -0.0003 -0.0045 0.0183  194 GLU   A O   
1477 C CB  . GLU   A 195 ? 0.1630 0.1765 0.2761 -0.0053 0.0009  0.0299  194 GLU   A CB  
1478 C CG  . GLU   A 195 ? 0.1868 0.1920 0.3029 -0.0076 -0.0022 0.0294  194 GLU   A CG  
1479 C CD  . GLU   A 195 ? 0.2338 0.2382 0.3610 -0.0128 -0.0037 0.0309  194 GLU   A CD  
1480 O OE1 . GLU   A 195 ? 0.2501 0.2461 0.3793 -0.0143 -0.0067 0.0299  194 GLU   A OE1 
1481 O OE2 . GLU   A 195 ? 0.2437 0.2557 0.3787 -0.0154 -0.0023 0.0329  194 GLU   A OE2 
1482 N N   . LEU   A 196 ? 0.1381 0.1476 0.2497 -0.0059 -0.0089 0.0155  195 LEU   A N   
1483 C CA  . LEU   A 196 ? 0.1502 0.1559 0.2557 -0.0044 -0.0110 0.0102  195 LEU   A CA  
1484 C C   . LEU   A 196 ? 0.1299 0.1394 0.2294 -0.0027 -0.0112 0.0079  195 LEU   A C   
1485 O O   . LEU   A 196 ? 0.1420 0.1495 0.2355 -0.0013 -0.0115 0.0046  195 LEU   A O   
1486 C CB  . LEU   A 196 ? 0.1570 0.1578 0.2658 -0.0069 -0.0145 0.0060  195 LEU   A CB  
1487 C CG  . LEU   A 196 ? 0.1719 0.1664 0.2862 -0.0083 -0.0147 0.0082  195 LEU   A CG  
1488 C CD1 . LEU   A 196 ? 0.2076 0.1968 0.3263 -0.0112 -0.0187 0.0039  195 LEU   A CD1 
1489 C CD2 . LEU   A 196 ? 0.1756 0.1658 0.2857 -0.0048 -0.0134 0.0085  195 LEU   A CD2 
1490 N N   . CYS   A 197 ? 0.1217 0.1368 0.2230 -0.0027 -0.0108 0.0099  196 CYS   A N   
1491 C CA  . CYS   A 197 ? 0.1249 0.1421 0.2202 -0.0007 -0.0114 0.0085  196 CYS   A CA  
1492 C C   . CYS   A 197 ? 0.1427 0.1581 0.2311 0.0022  -0.0090 0.0091  196 CYS   A C   
1493 O O   . CYS   A 197 ? 0.1588 0.1733 0.2414 0.0030  -0.0098 0.0071  196 CYS   A O   
1494 C CB  . CYS   A 197 ? 0.1232 0.1463 0.2231 -0.0002 -0.0116 0.0107  196 CYS   A CB  
1495 S SG  . CYS   A 197 ? 0.1542 0.1815 0.2572 0.0022  -0.0064 0.0154  196 CYS   A SG  
1496 N N   . ASP   A 198 ? 0.1294 0.1438 0.2182 0.0034  -0.0065 0.0120  197 ASP   A N   
1497 C CA  . ASP   A 198 ? 0.1353 0.1477 0.2174 0.0060  -0.0055 0.0121  197 ASP   A CA  
1498 C C   . ASP   A 198 ? 0.1300 0.1393 0.2100 0.0059  -0.0069 0.0091  197 ASP   A C   
1499 O O   . ASP   A 198 ? 0.1323 0.1412 0.2078 0.0072  -0.0072 0.0080  197 ASP   A O   
1500 C CB  . ASP   A 198 ? 0.1520 0.1634 0.2333 0.0072  -0.0032 0.0161  197 ASP   A CB  
1501 C CG  . ASP   A 198 ? 0.1549 0.1706 0.2368 0.0083  -0.0002 0.0189  197 ASP   A CG  
1502 O OD1 . ASP   A 198 ? 0.1627 0.1810 0.2434 0.0097  -0.0004 0.0173  197 ASP   A OD1 
1503 O OD2 . ASP   A 198 ? 0.1565 0.1727 0.2396 0.0080  0.0026  0.0228  197 ASP   A OD2 
1504 N N   . ILE   A 199 ? 0.1247 0.1318 0.2087 0.0044  -0.0079 0.0075  198 ILE   A N   
1505 C CA  . ILE   A 199 ? 0.1317 0.1369 0.2151 0.0050  -0.0085 0.0040  198 ILE   A CA  
1506 C C   . ILE   A 199 ? 0.1376 0.1448 0.2170 0.0042  -0.0087 0.0007  198 ILE   A C   
1507 O O   . ILE   A 199 ? 0.1351 0.1432 0.2123 0.0051  -0.0081 -0.0006 198 ILE   A O   
1508 C CB  . ILE   A 199 ? 0.1429 0.1444 0.2315 0.0040  -0.0095 0.0026  198 ILE   A CB  
1509 C CG1 . ILE   A 199 ? 0.1574 0.1559 0.2493 0.0044  -0.0093 0.0072  198 ILE   A CG1 
1510 C CG2 . ILE   A 199 ? 0.1588 0.1587 0.2476 0.0053  -0.0096 -0.0020 198 ILE   A CG2 
1511 C CD1 . ILE   A 199 ? 0.1694 0.1668 0.2587 0.0071  -0.0091 0.0092  198 ILE   A CD1 
1512 N N   . TRP   A 200 ? 0.1338 0.1422 0.2123 0.0025  -0.0097 0.0002  199 TRP   A N   
1513 C CA  . TRP   A 200 ? 0.1221 0.1316 0.1951 0.0016  -0.0102 -0.0018 199 TRP   A CA  
1514 C C   . TRP   A 200 ? 0.1259 0.1363 0.1951 0.0027  -0.0096 0.0003  199 TRP   A C   
1515 O O   . TRP   A 200 ? 0.1389 0.1496 0.2048 0.0023  -0.0089 -0.0008 199 TRP   A O   
1516 C CB  . TRP   A 200 ? 0.1141 0.1242 0.1868 -0.0001 -0.0127 -0.0018 199 TRP   A CB  
1517 C CG  . TRP   A 200 ? 0.1214 0.1318 0.1871 -0.0010 -0.0139 -0.0025 199 TRP   A CG  
1518 C CD1 . TRP   A 200 ? 0.1285 0.1393 0.1910 -0.0002 -0.0142 -0.0001 199 TRP   A CD1 
1519 C CD2 . TRP   A 200 ? 0.1197 0.1288 0.1797 -0.0028 -0.0151 -0.0057 199 TRP   A CD2 
1520 N NE1 . TRP   A 200 ? 0.1447 0.1544 0.2001 -0.0017 -0.0155 -0.0008 199 TRP   A NE1 
1521 C CE2 . TRP   A 200 ? 0.1324 0.1414 0.1855 -0.0033 -0.0160 -0.0041 199 TRP   A CE2 
1522 C CE3 . TRP   A 200 ? 0.1273 0.1346 0.1865 -0.0039 -0.0158 -0.0099 199 TRP   A CE3 
1523 C CZ2 . TRP   A 200 ? 0.1385 0.1461 0.1829 -0.0052 -0.0170 -0.0059 199 TRP   A CZ2 
1524 C CZ3 . TRP   A 200 ? 0.1453 0.1513 0.1955 -0.0053 -0.0167 -0.0126 199 TRP   A CZ3 
1525 C CH2 . TRP   A 200 ? 0.1444 0.1508 0.1869 -0.0061 -0.0172 -0.0103 199 TRP   A CH2 
1526 N N   . SER   A 201 ? 0.1289 0.1399 0.1993 0.0042  -0.0096 0.0033  200 SER   A N   
1527 C CA  . SER   A 201 ? 0.1180 0.1284 0.1844 0.0056  -0.0095 0.0046  200 SER   A CA  
1528 C C   . SER   A 201 ? 0.1210 0.1305 0.1864 0.0061  -0.0090 0.0039  200 SER   A C   
1529 O O   . SER   A 201 ? 0.1271 0.1357 0.1893 0.0057  -0.0096 0.0036  200 SER   A O   
1530 C CB  . SER   A 201 ? 0.1266 0.1377 0.1941 0.0078  -0.0088 0.0070  200 SER   A CB  
1531 O OG  . SER   A 201 ? 0.1465 0.1599 0.2171 0.0076  -0.0095 0.0078  200 SER   A OG  
1532 N N   . LEU   A 202 ? 0.1086 0.1180 0.1775 0.0067  -0.0085 0.0037  201 LEU   A N   
1533 C CA  . LEU   A 202 ? 0.1248 0.1342 0.1944 0.0074  -0.0088 0.0029  201 LEU   A CA  
1534 C C   . LEU   A 202 ? 0.1251 0.1366 0.1958 0.0058  -0.0081 0.0001  201 LEU   A C   
1535 O O   . LEU   A 202 ? 0.1319 0.1446 0.2026 0.0053  -0.0085 -0.0001 201 LEU   A O   
1536 C CB  . LEU   A 202 ? 0.1431 0.1513 0.2161 0.0091  -0.0092 0.0040  201 LEU   A CB  
1537 C CG  . LEU   A 202 ? 0.1809 0.1897 0.2559 0.0103  -0.0106 0.0033  201 LEU   A CG  
1538 C CD1 . LEU   A 202 ? 0.1986 0.2068 0.2688 0.0109  -0.0123 0.0044  201 LEU   A CD1 
1539 C CD2 . LEU   A 202 ? 0.1999 0.2069 0.2786 0.0122  -0.0115 0.0044  201 LEU   A CD2 
1540 N N   . GLY   A 203 ? 0.1175 0.1296 0.1889 0.0046  -0.0070 -0.0019 202 GLY   A N   
1541 C CA  . GLY   A 203 ? 0.1189 0.1333 0.1895 0.0030  -0.0053 -0.0046 202 GLY   A CA  
1542 C C   . GLY   A 203 ? 0.1302 0.1450 0.1956 0.0008  -0.0052 -0.0032 202 GLY   A C   
1543 O O   . GLY   A 203 ? 0.1273 0.1446 0.1935 -0.0005 -0.0039 -0.0036 202 GLY   A O   
1544 N N   . ILE   A 204 ? 0.1128 0.1250 0.1739 0.0005  -0.0070 -0.0012 203 ILE   A N   
1545 C CA  . ILE   A 204 ? 0.1129 0.1236 0.1690 -0.0012 -0.0078 0.0006  203 ILE   A CA  
1546 C C   . ILE   A 204 ? 0.1235 0.1335 0.1811 -0.0009 -0.0086 0.0017  203 ILE   A C   
1547 O O   . ILE   A 204 ? 0.1398 0.1494 0.1958 -0.0032 -0.0085 0.0025  203 ILE   A O   
1548 C CB  . ILE   A 204 ? 0.1114 0.1194 0.1643 -0.0005 -0.0102 0.0025  203 ILE   A CB  
1549 C CG1 . ILE   A 204 ? 0.1174 0.1260 0.1687 -0.0013 -0.0108 0.0013  203 ILE   A CG1 
1550 C CG2 . ILE   A 204 ? 0.1217 0.1263 0.1699 -0.0015 -0.0118 0.0047  203 ILE   A CG2 
1551 C CD1 . ILE   A 204 ? 0.1386 0.1472 0.1835 -0.0041 -0.0098 0.0002  203 ILE   A CD1 
1552 N N   . THR   A 205 ? 0.1224 0.1316 0.1823 0.0018  -0.0097 0.0021  204 THR   A N   
1553 C CA  . THR   A 205 ? 0.1262 0.1340 0.1863 0.0023  -0.0115 0.0025  204 THR   A CA  
1554 C C   . THR   A 205 ? 0.1337 0.1454 0.1989 0.0006  -0.0109 0.0013  204 THR   A C   
1555 O O   . THR   A 205 ? 0.1339 0.1450 0.1995 -0.0013 -0.0123 0.0017  204 THR   A O   
1556 C CB  . THR   A 205 ? 0.1336 0.1399 0.1934 0.0057  -0.0124 0.0031  204 THR   A CB  
1557 O OG1 . THR   A 205 ? 0.1484 0.1527 0.2049 0.0072  -0.0122 0.0042  204 THR   A OG1 
1558 C CG2 . THR   A 205 ? 0.1335 0.1375 0.1916 0.0066  -0.0151 0.0030  204 THR   A CG2 
1559 N N   . ALA   A 206 ? 0.1267 0.1423 0.1967 0.0010  -0.0088 -0.0003 205 ALA   A N   
1560 C CA  . ALA   A 206 ? 0.1301 0.1511 0.2070 -0.0001 -0.0076 -0.0018 205 ALA   A CA  
1561 C C   . ALA   A 206 ? 0.1414 0.1647 0.2171 -0.0042 -0.0052 -0.0014 205 ALA   A C   
1562 O O   . ALA   A 206 ? 0.1513 0.1779 0.2319 -0.0063 -0.0055 -0.0011 205 ALA   A O   
1563 C CB  . ALA   A 206 ? 0.1304 0.1545 0.2125 0.0020  -0.0055 -0.0041 205 ALA   A CB  
1564 N N   . ILE   A 207 ? 0.1478 0.1690 0.2167 -0.0056 -0.0035 -0.0010 206 ILE   A N   
1565 C CA  . ILE   A 207 ? 0.1500 0.1718 0.2150 -0.0097 -0.0014 0.0005  206 ILE   A CA  
1566 C C   . ILE   A 207 ? 0.1360 0.1531 0.1990 -0.0117 -0.0046 0.0034  206 ILE   A C   
1567 O O   . ILE   A 207 ? 0.1449 0.1638 0.2104 -0.0154 -0.0038 0.0048  206 ILE   A O   
1568 C CB  . ILE   A 207 ? 0.1546 0.1741 0.2111 -0.0103 0.0000  0.0005  206 ILE   A CB  
1569 C CG1 . ILE   A 207 ? 0.1623 0.1855 0.2204 -0.0086 0.0030  -0.0034 206 ILE   A CG1 
1570 C CG2 . ILE   A 207 ? 0.1737 0.1925 0.2243 -0.0149 0.0017  0.0033  206 ILE   A CG2 
1571 C CD1 . ILE   A 207 ? 0.1805 0.2010 0.2296 -0.0091 0.0032  -0.0042 206 ILE   A CD1 
1572 N N   . GLU   A 208 ? 0.1323 0.1435 0.1917 -0.0092 -0.0083 0.0041  207 GLU   A N   
1573 C CA  . GLU   A 208 ? 0.1359 0.1410 0.1928 -0.0099 -0.0119 0.0058  207 GLU   A CA  
1574 C C   . GLU   A 208 ? 0.1383 0.1454 0.2017 -0.0114 -0.0136 0.0052  207 GLU   A C   
1575 O O   . GLU   A 208 ? 0.1521 0.1566 0.2159 -0.0150 -0.0151 0.0067  207 GLU   A O   
1576 C CB  . GLU   A 208 ? 0.1685 0.1687 0.2218 -0.0056 -0.0145 0.0055  207 GLU   A CB  
1577 C CG  . GLU   A 208 ? 0.1687 0.1620 0.2190 -0.0049 -0.0183 0.0060  207 GLU   A CG  
1578 C CD  . GLU   A 208 ? 0.1809 0.1716 0.2289 0.0000  -0.0196 0.0047  207 GLU   A CD  
1579 O OE1 . GLU   A 208 ? 0.1565 0.1506 0.2054 0.0025  -0.0177 0.0044  207 GLU   A OE1 
1580 O OE2 . GLU   A 208 ? 0.1964 0.1813 0.2413 0.0013  -0.0226 0.0039  207 GLU   A OE2 
1581 N N   . LEU   A 209 ? 0.1346 0.1461 0.2036 -0.0089 -0.0139 0.0032  208 LEU   A N   
1582 C CA  . LEU   A 209 ? 0.1481 0.1621 0.2239 -0.0100 -0.0166 0.0024  208 LEU   A CA  
1583 C C   . LEU   A 209 ? 0.1572 0.1785 0.2412 -0.0146 -0.0138 0.0029  208 LEU   A C   
1584 O O   . LEU   A 209 ? 0.1518 0.1741 0.2413 -0.0177 -0.0164 0.0034  208 LEU   A O   
1585 C CB  . LEU   A 209 ? 0.1509 0.1677 0.2304 -0.0058 -0.0179 0.0008  208 LEU   A CB  
1586 C CG  . LEU   A 209 ? 0.1653 0.1757 0.2370 -0.0016 -0.0202 0.0009  208 LEU   A CG  
1587 C CD1 . LEU   A 209 ? 0.1677 0.1806 0.2425 0.0019  -0.0210 0.0003  208 LEU   A CD1 
1588 C CD2 . LEU   A 209 ? 0.1751 0.1785 0.2410 -0.0017 -0.0245 0.0008  208 LEU   A CD2 
1589 N N   . ALA   A 210 ? 0.1633 0.1896 0.2479 -0.0151 -0.0084 0.0027  209 ALA   A N   
1590 C CA  . ALA   A 210 ? 0.1616 0.1960 0.2530 -0.0192 -0.0039 0.0031  209 ALA   A CA  
1591 C C   . ALA   A 210 ? 0.1650 0.1961 0.2513 -0.0248 -0.0026 0.0066  209 ALA   A C   
1592 O O   . ALA   A 210 ? 0.1779 0.2151 0.2710 -0.0295 0.0003  0.0080  209 ALA   A O   
1593 C CB  . ALA   A 210 ? 0.1589 0.1987 0.2502 -0.0171 0.0016  0.0009  209 ALA   A CB  
1594 N N   . GLU   A 211 ? 0.1592 0.1813 0.2341 -0.0243 -0.0040 0.0083  210 GLU   A N   
1595 C CA  . GLU   A 211 ? 0.1665 0.1842 0.2347 -0.0290 -0.0029 0.0123  210 GLU   A CA  
1596 C C   . GLU   A 211 ? 0.1696 0.1759 0.2321 -0.0296 -0.0085 0.0146  210 GLU   A C   
1597 O O   . GLU   A 211 ? 0.1799 0.1811 0.2369 -0.0336 -0.0083 0.0185  210 GLU   A O   
1598 C CB  . GLU   A 211 ? 0.1860 0.2038 0.2450 -0.0281 0.0009  0.0125  210 GLU   A CB  
1599 C CG  . GLU   A 211 ? 0.1963 0.2244 0.2599 -0.0277 0.0071  0.0096  210 GLU   A CG  
1600 C CD  . GLU   A 211 ? 0.2181 0.2462 0.2720 -0.0268 0.0107  0.0087  210 GLU   A CD  
1601 O OE1 . GLU   A 211 ? 0.2129 0.2334 0.2563 -0.0268 0.0080  0.0109  210 GLU   A OE1 
1602 O OE2 . GLU   A 211 ? 0.2329 0.2687 0.2899 -0.0258 0.0158  0.0055  210 GLU   A OE2 
1603 N N   . LEU   A 212 ? 0.1583 0.1603 0.2217 -0.0258 -0.0135 0.0124  211 LEU   A N   
1604 C CA  . LEU   A 212 ? 0.1800 0.1708 0.2384 -0.0252 -0.0190 0.0132  211 LEU   A CA  
1605 C C   . LEU   A 212 ? 0.1888 0.1723 0.2378 -0.0219 -0.0200 0.0143  211 LEU   A C   
1606 O O   . LEU   A 212 ? 0.2007 0.1748 0.2458 -0.0205 -0.0243 0.0146  211 LEU   A O   
1607 C CB  . LEU   A 212 ? 0.1792 0.1658 0.2402 -0.0315 -0.0210 0.0160  211 LEU   A CB  
1608 C CG  . LEU   A 212 ? 0.1821 0.1773 0.2549 -0.0354 -0.0204 0.0152  211 LEU   A CG  
1609 C CD1 . LEU   A 212 ? 0.1778 0.1683 0.2541 -0.0425 -0.0228 0.0184  211 LEU   A CD1 
1610 C CD2 . LEU   A 212 ? 0.2030 0.1996 0.2798 -0.0310 -0.0245 0.0109  211 LEU   A CD2 
1611 N N   . GLN   A 213 ? 0.1834 0.1711 0.2295 -0.0204 -0.0167 0.0144  212 GLN   A N   
1612 C CA  . GLN   A 213 ? 0.1780 0.1611 0.2173 -0.0170 -0.0180 0.0152  212 GLN   A CA  
1613 C C   . GLN   A 213 ? 0.1811 0.1713 0.2202 -0.0153 -0.0146 0.0136  212 GLN   A C   
1614 O O   . GLN   A 213 ? 0.1665 0.1636 0.2084 -0.0175 -0.0106 0.0128  212 GLN   A O   
1615 C CB  . GLN   A 213 ? 0.1959 0.1716 0.2285 -0.0201 -0.0196 0.0196  212 GLN   A CB  
1616 C CG  . GLN   A 213 ? 0.2383 0.2179 0.2674 -0.0250 -0.0155 0.0224  212 GLN   A CG  
1617 C CD  . GLN   A 213 ? 0.2986 0.2693 0.3198 -0.0279 -0.0179 0.0277  212 GLN   A CD  
1618 O OE1 . GLN   A 213 ? 0.3212 0.2827 0.3420 -0.0281 -0.0223 0.0295  212 GLN   A OE1 
1619 N NE2 . GLN   A 213 ? 0.3155 0.2880 0.3294 -0.0302 -0.0153 0.0303  212 GLN   A NE2 
1620 N N   . PRO   A 214 ? 0.1687 0.1575 0.2056 -0.0111 -0.0161 0.0128  213 PRO   A N   
1621 C CA  . PRO   A 214 ? 0.1704 0.1648 0.2072 -0.0100 -0.0137 0.0112  213 PRO   A CA  
1622 C C   . PRO   A 214 ? 0.1873 0.1808 0.2169 -0.0131 -0.0129 0.0134  213 PRO   A C   
1623 O O   . PRO   A 214 ? 0.1763 0.1640 0.2006 -0.0153 -0.0149 0.0169  213 PRO   A O   
1624 C CB  . PRO   A 214 ? 0.1724 0.1654 0.2101 -0.0054 -0.0160 0.0104  213 PRO   A CB  
1625 C CG  . PRO   A 214 ? 0.1748 0.1604 0.2094 -0.0044 -0.0197 0.0126  213 PRO   A CG  
1626 C CD  . PRO   A 214 ? 0.1618 0.1443 0.1969 -0.0073 -0.0198 0.0132  213 PRO   A CD  
1627 N N   . PRO   A 215 ? 0.1834 0.1816 0.2115 -0.0133 -0.0104 0.0113  214 PRO   A N   
1628 C CA  . PRO   A 215 ? 0.1926 0.1893 0.2113 -0.0159 -0.0101 0.0130  214 PRO   A CA  
1629 C C   . PRO   A 215 ? 0.2137 0.2041 0.2269 -0.0146 -0.0155 0.0161  214 PRO   A C   
1630 O O   . PRO   A 215 ? 0.2074 0.1969 0.2254 -0.0109 -0.0186 0.0154  214 PRO   A O   
1631 C CB  . PRO   A 215 ? 0.2063 0.2080 0.2251 -0.0148 -0.0078 0.0088  214 PRO   A CB  
1632 C CG  . PRO   A 215 ? 0.2001 0.2068 0.2290 -0.0131 -0.0050 0.0056  214 PRO   A CG  
1633 C CD  . PRO   A 215 ? 0.1707 0.1744 0.2046 -0.0110 -0.0083 0.0073  214 PRO   A CD  
1634 N N   . LEU   A 216 ? 0.2301 0.2163 0.2337 -0.0175 -0.0166 0.0198  215 LEU   A N   
1635 C CA  . LEU   A 216 ? 0.2414 0.2211 0.2396 -0.0161 -0.0226 0.0232  215 LEU   A CA  
1636 C C   . LEU   A 216 ? 0.2245 0.1984 0.2279 -0.0135 -0.0264 0.0252  215 LEU   A C   
1637 O O   . LEU   A 216 ? 0.2160 0.1856 0.2179 -0.0109 -0.0315 0.0271  215 LEU   A O   
1638 C CB  . LEU   A 216 ? 0.2659 0.2481 0.2639 -0.0133 -0.0259 0.0208  215 LEU   A CB  
1639 C CG  . LEU   A 216 ? 0.3141 0.3006 0.3064 -0.0150 -0.0235 0.0176  215 LEU   A CG  
1640 C CD1 . LEU   A 216 ? 0.3267 0.3143 0.3201 -0.0126 -0.0285 0.0155  215 LEU   A CD1 
1641 C CD2 . LEU   A 216 ? 0.3398 0.3234 0.3185 -0.0192 -0.0217 0.0205  215 LEU   A CD2 
1642 N N   . PHE   A 217 ? 0.2115 0.1848 0.2202 -0.0142 -0.0243 0.0246  216 PHE   A N   
1643 C CA  . PHE   A 217 ? 0.2149 0.1817 0.2274 -0.0113 -0.0279 0.0253  216 PHE   A CA  
1644 C C   . PHE   A 217 ? 0.2263 0.1831 0.2324 -0.0120 -0.0327 0.0302  216 PHE   A C   
1645 O O   . PHE   A 217 ? 0.2337 0.1853 0.2423 -0.0076 -0.0369 0.0303  216 PHE   A O   
1646 C CB  . PHE   A 217 ? 0.2069 0.1738 0.2246 -0.0127 -0.0258 0.0236  216 PHE   A CB  
1647 C CG  . PHE   A 217 ? 0.2230 0.1845 0.2445 -0.0085 -0.0290 0.0221  216 PHE   A CG  
1648 C CD1 . PHE   A 217 ? 0.2366 0.2010 0.2619 -0.0028 -0.0295 0.0191  216 PHE   A CD1 
1649 C CD2 . PHE   A 217 ? 0.2389 0.1922 0.2600 -0.0104 -0.0313 0.0234  216 PHE   A CD2 
1650 C CE1 . PHE   A 217 ? 0.2564 0.2164 0.2841 0.0016  -0.0314 0.0171  216 PHE   A CE1 
1651 C CE2 . PHE   A 217 ? 0.2597 0.2072 0.2828 -0.0059 -0.0343 0.0209  216 PHE   A CE2 
1652 C CZ  . PHE   A 217 ? 0.2604 0.2114 0.2863 0.0003  -0.0340 0.0176  216 PHE   A CZ  
1653 N N   . ASP   A 218 ? 0.2369 0.1914 0.2348 -0.0172 -0.0318 0.0344  217 ASP   A N   
1654 C CA  . ASP   A 218 ? 0.2564 0.2004 0.2463 -0.0189 -0.0363 0.0405  217 ASP   A CA  
1655 C C   . ASP   A 218 ? 0.2458 0.1876 0.2302 -0.0159 -0.0414 0.0424  217 ASP   A C   
1656 O O   . ASP   A 218 ? 0.2396 0.1723 0.2164 -0.0171 -0.0458 0.0480  217 ASP   A O   
1657 C CB  . ASP   A 218 ? 0.3121 0.2558 0.2938 -0.0263 -0.0323 0.0448  217 ASP   A CB  
1658 C CG  . ASP   A 218 ? 0.4146 0.3579 0.4014 -0.0308 -0.0288 0.0454  217 ASP   A CG  
1659 O OD1 . ASP   A 218 ? 0.4485 0.3893 0.4436 -0.0283 -0.0308 0.0426  217 ASP   A OD1 
1660 O OD2 . ASP   A 218 ? 0.4373 0.3828 0.4197 -0.0370 -0.0242 0.0485  217 ASP   A OD2 
1661 N N   . VAL   A 219 ? 0.2344 0.1846 0.2219 -0.0128 -0.0410 0.0383  218 VAL   A N   
1662 C CA  . VAL   A 219 ? 0.2418 0.1918 0.2258 -0.0102 -0.0464 0.0395  218 VAL   A CA  
1663 C C   . VAL   A 219 ? 0.2290 0.1790 0.2234 -0.0035 -0.0507 0.0377  218 VAL   A C   
1664 O O   . VAL   A 219 ? 0.2205 0.1754 0.2247 -0.0007 -0.0477 0.0334  218 VAL   A O   
1665 C CB  . VAL   A 219 ? 0.2606 0.2195 0.2424 -0.0115 -0.0435 0.0358  218 VAL   A CB  
1666 C CG1 . VAL   A 219 ? 0.2617 0.2211 0.2408 -0.0091 -0.0501 0.0364  218 VAL   A CG1 
1667 C CG2 . VAL   A 219 ? 0.2851 0.2445 0.2562 -0.0174 -0.0382 0.0371  218 VAL   A CG2 
1668 N N   . HIS   A 220 ? 0.2225 0.1679 0.2151 -0.0006 -0.0578 0.0409  219 HIS   A N   
1669 C CA  . HIS   A 220 ? 0.2257 0.1722 0.2294 0.0064  -0.0620 0.0394  219 HIS   A CA  
1670 C C   . HIS   A 220 ? 0.2252 0.1841 0.2389 0.0085  -0.0591 0.0341  219 HIS   A C   
1671 O O   . HIS   A 220 ? 0.2300 0.1942 0.2402 0.0056  -0.0586 0.0330  219 HIS   A O   
1672 C CB  . HIS   A 220 ? 0.2337 0.1752 0.2342 0.0089  -0.0706 0.0438  219 HIS   A CB  
1673 C CG  . HIS   A 220 ? 0.2675 0.2094 0.2804 0.0165  -0.0749 0.0427  219 HIS   A CG  
1674 N ND1 . HIS   A 220 ? 0.2709 0.2243 0.2961 0.0205  -0.0749 0.0388  219 HIS   A ND1 
1675 C CD2 . HIS   A 220 ? 0.2798 0.2122 0.2949 0.0208  -0.0790 0.0449  219 HIS   A CD2 
1676 C CE1 . HIS   A 220 ? 0.2872 0.2390 0.3221 0.0274  -0.0783 0.0387  219 HIS   A CE1 
1677 N NE2 . HIS   A 220 ? 0.2918 0.2305 0.3207 0.0282  -0.0811 0.0420  219 HIS   A NE2 
1678 N N   . PRO   A 221 ? 0.2369 0.1995 0.2619 0.0132  -0.0569 0.0307  220 PRO   A N   
1679 C CA  . PRO   A 221 ? 0.2314 0.2055 0.2661 0.0147  -0.0536 0.0266  220 PRO   A CA  
1680 C C   . PRO   A 221 ? 0.2329 0.2135 0.2715 0.0151  -0.0581 0.0268  220 PRO   A C   
1681 O O   . PRO   A 221 ? 0.2410 0.2287 0.2820 0.0127  -0.0555 0.0241  220 PRO   A O   
1682 C CB  . PRO   A 221 ? 0.2486 0.2242 0.2934 0.0205  -0.0515 0.0242  220 PRO   A CB  
1683 C CG  . PRO   A 221 ? 0.2659 0.2305 0.3063 0.0223  -0.0538 0.0261  220 PRO   A CG  
1684 C CD  . PRO   A 221 ? 0.2483 0.2042 0.2768 0.0173  -0.0572 0.0305  220 PRO   A CD  
1685 N N   . LEU   A 222 ? 0.2302 0.2080 0.2695 0.0179  -0.0654 0.0298  221 LEU   A N   
1686 C CA  . LEU   A 222 ? 0.2406 0.2247 0.2839 0.0181  -0.0712 0.0300  221 LEU   A CA  
1687 C C   . LEU   A 222 ? 0.2594 0.2412 0.2888 0.0121  -0.0728 0.0307  221 LEU   A C   
1688 O O   . LEU   A 222 ? 0.2671 0.2553 0.2989 0.0104  -0.0748 0.0285  221 LEU   A O   
1689 C CB  . LEU   A 222 ? 0.2528 0.2348 0.3016 0.0233  -0.0794 0.0331  221 LEU   A CB  
1690 C CG  . LEU   A 222 ? 0.3003 0.2861 0.3643 0.0304  -0.0778 0.0315  221 LEU   A CG  
1691 C CD1 . LEU   A 222 ? 0.3122 0.2951 0.3815 0.0360  -0.0863 0.0346  221 LEU   A CD1 
1692 C CD2 . LEU   A 222 ? 0.3178 0.3173 0.3965 0.0314  -0.0730 0.0276  221 LEU   A CD2 
1693 N N   . ARG   A 223 ? 0.2435 0.2164 0.2583 0.0086  -0.0713 0.0333  222 ARG   A N   
1694 C CA  . ARG   A 223 ? 0.2553 0.2263 0.2555 0.0031  -0.0709 0.0336  222 ARG   A CA  
1695 C C   . ARG   A 223 ? 0.2511 0.2287 0.2536 0.0003  -0.0632 0.0284  222 ARG   A C   
1696 O O   . ARG   A 223 ? 0.2592 0.2396 0.2568 -0.0023 -0.0639 0.0258  222 ARG   A O   
1697 C CB  . ARG   A 223 ? 0.2942 0.2549 0.2792 -0.0002 -0.0704 0.0386  222 ARG   A CB  
1698 C CG  . ARG   A 223 ? 0.3350 0.2948 0.3040 -0.0058 -0.0683 0.0385  222 ARG   A CG  
1699 C CD  . ARG   A 223 ? 0.3841 0.3341 0.3356 -0.0090 -0.0713 0.0450  222 ARG   A CD  
1700 N NE  . ARG   A 223 ? 0.4332 0.3840 0.3696 -0.0141 -0.0668 0.0439  222 ARG   A NE  
1701 C CZ  . ARG   A 223 ? 0.4649 0.4172 0.3918 -0.0150 -0.0707 0.0420  222 ARG   A CZ  
1702 N NH1 . ARG   A 223 ? 0.4731 0.4267 0.4050 -0.0117 -0.0798 0.0416  222 ARG   A NH1 
1703 N NH2 . ARG   A 223 ? 0.4626 0.4154 0.3752 -0.0192 -0.0655 0.0402  222 ARG   A NH2 
1704 N N   . VAL   A 224 ? 0.2318 0.2113 0.2419 0.0012  -0.0567 0.0264  223 VAL   A N   
1705 C CA  . VAL   A 224 ? 0.2320 0.2174 0.2454 -0.0007 -0.0501 0.0218  223 VAL   A CA  
1706 C C   . VAL   A 224 ? 0.2358 0.2289 0.2596 0.0007  -0.0523 0.0186  223 VAL   A C   
1707 O O   . VAL   A 224 ? 0.2484 0.2441 0.2702 -0.0019 -0.0508 0.0153  223 VAL   A O   
1708 C CB  . VAL   A 224 ? 0.2304 0.2162 0.2501 0.0005  -0.0442 0.0208  223 VAL   A CB  
1709 C CG1 . VAL   A 224 ? 0.2338 0.2255 0.2582 -0.0007 -0.0385 0.0165  223 VAL   A CG1 
1710 C CG2 . VAL   A 224 ? 0.2385 0.2170 0.2492 -0.0020 -0.0424 0.0238  223 VAL   A CG2 
1711 N N   . LEU   A 225 ? 0.2342 0.2305 0.2693 0.0047  -0.0560 0.0196  224 LEU   A N   
1712 C CA  . LEU   A 225 ? 0.2349 0.2394 0.2818 0.0054  -0.0583 0.0174  224 LEU   A CA  
1713 C C   . LEU   A 225 ? 0.2584 0.2624 0.2987 0.0026  -0.0649 0.0168  224 LEU   A C   
1714 O O   . LEU   A 225 ? 0.2698 0.2780 0.3139 0.0004  -0.0650 0.0134  224 LEU   A O   
1715 C CB  . LEU   A 225 ? 0.2311 0.2404 0.2921 0.0105  -0.0606 0.0189  224 LEU   A CB  
1716 C CG  . LEU   A 225 ? 0.2378 0.2491 0.3066 0.0137  -0.0538 0.0182  224 LEU   A CG  
1717 C CD1 . LEU   A 225 ? 0.2389 0.2562 0.3219 0.0192  -0.0558 0.0192  224 LEU   A CD1 
1718 C CD2 . LEU   A 225 ? 0.2396 0.2555 0.3122 0.0114  -0.0474 0.0154  224 LEU   A CD2 
1719 N N   . PHE   A 226 ? 0.2579 0.2559 0.2874 0.0026  -0.0707 0.0201  225 PHE   A N   
1720 C CA  . PHE   A 226 ? 0.2765 0.2725 0.2958 -0.0001 -0.0776 0.0197  225 PHE   A CA  
1721 C C   . PHE   A 226 ? 0.2829 0.2768 0.2902 -0.0045 -0.0729 0.0158  225 PHE   A C   
1722 O O   . PHE   A 226 ? 0.2984 0.2946 0.3054 -0.0064 -0.0758 0.0120  225 PHE   A O   
1723 C CB  . PHE   A 226 ? 0.2929 0.2811 0.2999 0.0006  -0.0840 0.0250  225 PHE   A CB  
1724 C CG  . PHE   A 226 ? 0.3247 0.3086 0.3150 -0.0027 -0.0901 0.0250  225 PHE   A CG  
1725 C CD1 . PHE   A 226 ? 0.3435 0.3309 0.3377 -0.0023 -0.0994 0.0239  225 PHE   A CD1 
1726 C CD2 . PHE   A 226 ? 0.3513 0.3281 0.3220 -0.0062 -0.0865 0.0262  225 PHE   A CD2 
1727 C CE1 . PHE   A 226 ? 0.3708 0.3534 0.3476 -0.0052 -0.1057 0.0236  225 PHE   A CE1 
1728 C CE2 . PHE   A 226 ? 0.3760 0.3486 0.3291 -0.0090 -0.0915 0.0261  225 PHE   A CE2 
1729 C CZ  . PHE   A 226 ? 0.3767 0.3516 0.3320 -0.0084 -0.1015 0.0246  225 PHE   A CZ  
1730 N N   . LEU   A 227 ? 0.2801 0.2699 0.2783 -0.0059 -0.0657 0.0165  226 LEU   A N   
1731 C CA  . LEU   A 227 ? 0.2798 0.2684 0.2673 -0.0094 -0.0604 0.0127  226 LEU   A CA  
1732 C C   . LEU   A 227 ? 0.2878 0.2817 0.2858 -0.0096 -0.0565 0.0071  226 LEU   A C   
1733 O O   . LEU   A 227 ? 0.2744 0.2678 0.2658 -0.0117 -0.0561 0.0025  226 LEU   A O   
1734 C CB  . LEU   A 227 ? 0.2792 0.2643 0.2595 -0.0106 -0.0532 0.0151  226 LEU   A CB  
1735 C CG  . LEU   A 227 ? 0.2982 0.2760 0.2649 -0.0118 -0.0562 0.0211  226 LEU   A CG  
1736 C CD1 . LEU   A 227 ? 0.3039 0.2790 0.2686 -0.0133 -0.0493 0.0240  226 LEU   A CD1 
1737 C CD2 . LEU   A 227 ? 0.3093 0.2839 0.2580 -0.0148 -0.0586 0.0206  226 LEU   A CD2 
1738 N N   . MET   A 228 ? 0.3026 0.3010 0.3160 -0.0073 -0.0534 0.0073  227 MET   A N   
1739 C CA  . MET   A 228 ? 0.3325 0.3350 0.3556 -0.0077 -0.0494 0.0031  227 MET   A CA  
1740 C C   . MET   A 228 ? 0.3741 0.3797 0.4046 -0.0086 -0.0549 0.0004  227 MET   A C   
1741 O O   . MET   A 228 ? 0.3874 0.3939 0.4222 -0.0099 -0.0526 -0.0035 227 MET   A O   
1742 C CB  . MET   A 228 ? 0.3359 0.3416 0.3709 -0.0052 -0.0443 0.0047  227 MET   A CB  
1743 C CG  . MET   A 228 ? 0.3816 0.3841 0.4103 -0.0050 -0.0389 0.0063  227 MET   A CG  
1744 S SD  . MET   A 228 ? 0.4570 0.4625 0.4977 -0.0021 -0.0339 0.0071  227 MET   A SD  
1745 C CE  . MET   A 228 ? 0.2757 0.2832 0.3196 -0.0036 -0.0294 0.0030  227 MET   A CE  
1746 N N   . THR   A 229 ? 0.3946 0.4015 0.4274 -0.0080 -0.0628 0.0025  228 THR   A N   
1747 C CA  . THR   A 229 ? 0.4241 0.4344 0.4649 -0.0095 -0.0691 -0.0001 228 THR   A CA  
1748 C C   . THR   A 229 ? 0.4553 0.4606 0.4811 -0.0122 -0.0755 -0.0032 228 THR   A C   
1749 O O   . THR   A 229 ? 0.4594 0.4664 0.4904 -0.0140 -0.0820 -0.0059 228 THR   A O   
1750 C CB  . THR   A 229 ? 0.4497 0.4670 0.5068 -0.0073 -0.0738 0.0032  228 THR   A CB  
1751 O OG1 . THR   A 229 ? 0.4721 0.4874 0.5237 -0.0048 -0.0784 0.0073  228 THR   A OG1 
1752 C CG2 . THR   A 229 ? 0.4478 0.4707 0.5197 -0.0052 -0.0668 0.0046  228 THR   A CG2 
1753 N N   . LYS   A 230 ? 0.4739 0.4729 0.4809 -0.0128 -0.0735 -0.0028 229 LYS   A N   
1754 C CA  . LYS   A 230 ? 0.4981 0.4917 0.4874 -0.0151 -0.0782 -0.0060 229 LYS   A CA  
1755 C C   . LYS   A 230 ? 0.5193 0.5116 0.5073 -0.0169 -0.0740 -0.0132 229 LYS   A C   
1756 O O   . LYS   A 230 ? 0.5213 0.5149 0.5153 -0.0162 -0.0656 -0.0143 229 LYS   A O   
1757 C CB  . LYS   A 230 ? 0.5292 0.5171 0.4990 -0.0154 -0.0755 -0.0028 229 LYS   A CB  
1758 C CG  . LYS   A 230 ? 0.5892 0.5737 0.5491 -0.0152 -0.0846 0.0020  229 LYS   A CG  
1759 C CD  . LYS   A 230 ? 0.6605 0.6387 0.6010 -0.0162 -0.0806 0.0061  229 LYS   A CD  
1760 C CE  . LYS   A 230 ? 0.7201 0.6923 0.6434 -0.0170 -0.0897 0.0098  229 LYS   A CE  
1761 N NZ  . LYS   A 230 ? 0.7570 0.7256 0.6616 -0.0195 -0.0917 0.0045  229 LYS   A NZ  
1762 N N   . SER   A 231 ? 0.5300 0.5191 0.5105 -0.0190 -0.0805 -0.0182 230 SER   A N   
1763 C CA  . SER   A 231 ? 0.5390 0.5254 0.5183 -0.0204 -0.0782 -0.0259 230 SER   A CA  
1764 C C   . SER   A 231 ? 0.5387 0.5219 0.5061 -0.0197 -0.0682 -0.0289 230 SER   A C   
1765 O O   . SER   A 231 ? 0.5511 0.5344 0.5262 -0.0192 -0.0628 -0.0329 230 SER   A O   
1766 C CB  . SER   A 231 ? 0.5744 0.5563 0.5441 -0.0226 -0.0882 -0.0311 230 SER   A CB  
1767 O OG  . SER   A 231 ? 0.6146 0.6007 0.5966 -0.0234 -0.0982 -0.0281 230 SER   A OG  
1768 N N   . GLY   A 232 ? 0.5202 0.5008 0.4697 -0.0197 -0.0658 -0.0267 231 GLY   A N   
1769 C CA  . GLY   A 232 ? 0.5046 0.4838 0.4431 -0.0192 -0.0559 -0.0292 231 GLY   A CA  
1770 C C   . GLY   A 232 ? 0.4731 0.4564 0.4198 -0.0180 -0.0472 -0.0243 231 GLY   A C   
1771 O O   . GLY   A 232 ? 0.4804 0.4638 0.4184 -0.0181 -0.0393 -0.0249 231 GLY   A O   
1772 N N   . TYR   A 233 ? 0.4386 0.4258 0.4024 -0.0169 -0.0484 -0.0197 232 TYR   A N   
1773 C CA  . TYR   A 233 ? 0.4124 0.4028 0.3843 -0.0157 -0.0414 -0.0155 232 TYR   A CA  
1774 C C   . TYR   A 233 ? 0.3978 0.3898 0.3735 -0.0149 -0.0331 -0.0200 232 TYR   A C   
1775 O O   . TYR   A 233 ? 0.3964 0.3883 0.3799 -0.0143 -0.0336 -0.0248 232 TYR   A O   
1776 C CB  . TYR   A 233 ? 0.3988 0.3929 0.3884 -0.0141 -0.0443 -0.0115 232 TYR   A CB  
1777 C CG  . TYR   A 233 ? 0.3981 0.3950 0.3969 -0.0126 -0.0375 -0.0088 232 TYR   A CG  
1778 C CD1 . TYR   A 233 ? 0.4049 0.4010 0.3990 -0.0126 -0.0349 -0.0041 232 TYR   A CD1 
1779 C CD2 . TYR   A 233 ? 0.4025 0.4020 0.4137 -0.0115 -0.0341 -0.0112 232 TYR   A CD2 
1780 C CE1 . TYR   A 233 ? 0.4101 0.4083 0.4119 -0.0115 -0.0294 -0.0024 232 TYR   A CE1 
1781 C CE2 . TYR   A 233 ? 0.4022 0.4039 0.4203 -0.0101 -0.0286 -0.0090 232 TYR   A CE2 
1782 C CZ  . TYR   A 233 ? 0.4060 0.4072 0.4194 -0.0101 -0.0265 -0.0050 232 TYR   A CZ  
1783 O OH  . TYR   A 233 ? 0.4060 0.4088 0.4261 -0.0089 -0.0222 -0.0032 232 TYR   A OH  
1784 N N   . GLN   A 234 ? 0.3791 0.3725 0.3501 -0.0150 -0.0259 -0.0182 233 GLN   A N   
1785 C CA  . GLN   A 234 ? 0.3642 0.3602 0.3402 -0.0138 -0.0183 -0.0222 233 GLN   A CA  
1786 C C   . GLN   A 234 ? 0.3331 0.3328 0.3225 -0.0127 -0.0149 -0.0181 233 GLN   A C   
1787 O O   . GLN   A 234 ? 0.3296 0.3297 0.3178 -0.0136 -0.0147 -0.0124 233 GLN   A O   
1788 C CB  . GLN   A 234 ? 0.3955 0.3918 0.3573 -0.0149 -0.0118 -0.0241 233 GLN   A CB  
1789 C CG  . GLN   A 234 ? 0.4584 0.4503 0.4035 -0.0158 -0.0145 -0.0290 233 GLN   A CG  
1790 C CD  . GLN   A 234 ? 0.5255 0.5152 0.4747 -0.0140 -0.0161 -0.0373 233 GLN   A CD  
1791 O OE1 . GLN   A 234 ? 0.5591 0.5445 0.5052 -0.0146 -0.0238 -0.0399 233 GLN   A OE1 
1792 N NE2 . GLN   A 234 ? 0.5284 0.5207 0.4853 -0.0118 -0.0095 -0.0416 233 GLN   A NE2 
1793 N N   . PRO   A 235 ? 0.3050 0.3066 0.3064 -0.0108 -0.0125 -0.0209 234 PRO   A N   
1794 C CA  . PRO   A 235 ? 0.2834 0.2882 0.2958 -0.0096 -0.0096 -0.0174 234 PRO   A CA  
1795 C C   . PRO   A 235 ? 0.2666 0.2743 0.2755 -0.0107 -0.0041 -0.0152 234 PRO   A C   
1796 O O   . PRO   A 235 ? 0.2706 0.2796 0.2718 -0.0115 0.0004  -0.0180 234 PRO   A O   
1797 C CB  . PRO   A 235 ? 0.2942 0.2997 0.3166 -0.0074 -0.0078 -0.0217 234 PRO   A CB  
1798 C CG  . PRO   A 235 ? 0.3065 0.3080 0.3267 -0.0077 -0.0125 -0.0258 234 PRO   A CG  
1799 C CD  . PRO   A 235 ? 0.2976 0.2974 0.3024 -0.0095 -0.0128 -0.0274 234 PRO   A CD  
1800 N N   . PRO   A 236 ? 0.2400 0.2488 0.2546 -0.0108 -0.0040 -0.0105 235 PRO   A N   
1801 C CA  . PRO   A 236 ? 0.2377 0.2492 0.2506 -0.0126 0.0007  -0.0081 235 PRO   A CA  
1802 C C   . PRO   A 236 ? 0.2294 0.2463 0.2505 -0.0114 0.0062  -0.0114 235 PRO   A C   
1803 O O   . PRO   A 236 ? 0.2276 0.2452 0.2557 -0.0087 0.0062  -0.0154 235 PRO   A O   
1804 C CB  . PRO   A 236 ? 0.2517 0.2612 0.2684 -0.0129 -0.0025 -0.0027 235 PRO   A CB  
1805 C CG  . PRO   A 236 ? 0.2547 0.2633 0.2796 -0.0099 -0.0062 -0.0034 235 PRO   A CG  
1806 C CD  . PRO   A 236 ? 0.2296 0.2374 0.2522 -0.0093 -0.0080 -0.0072 235 PRO   A CD  
1807 N N   . ARG   A 237 ? 0.2151 0.2359 0.2353 -0.0137 0.0111  -0.0099 236 ARG   A N   
1808 C CA  . ARG   A 237 ? 0.2114 0.2391 0.2409 -0.0126 0.0165  -0.0128 236 ARG   A CA  
1809 C C   . ARG   A 237 ? 0.1987 0.2299 0.2338 -0.0153 0.0181  -0.0083 236 ARG   A C   
1810 O O   . ARG   A 237 ? 0.2105 0.2380 0.2396 -0.0184 0.0161  -0.0033 236 ARG   A O   
1811 C CB  . ARG   A 237 ? 0.2464 0.2778 0.2691 -0.0129 0.0228  -0.0171 236 ARG   A CB  
1812 C CG  . ARG   A 237 ? 0.3329 0.3596 0.3466 -0.0111 0.0211  -0.0222 236 ARG   A CG  
1813 C CD  . ARG   A 237 ? 0.4098 0.4390 0.4116 -0.0122 0.0273  -0.0253 236 ARG   A CD  
1814 N NE  . ARG   A 237 ? 0.5037 0.5285 0.4982 -0.0098 0.0259  -0.0321 236 ARG   A NE  
1815 C CZ  . ARG   A 237 ? 0.5712 0.5965 0.5531 -0.0098 0.0306  -0.0367 236 ARG   A CZ  
1816 N NH1 . ARG   A 237 ? 0.5875 0.6075 0.5629 -0.0074 0.0282  -0.0436 236 ARG   A NH1 
1817 N NH2 . ARG   A 237 ? 0.5723 0.6032 0.5478 -0.0123 0.0380  -0.0346 236 ARG   A NH2 
1818 N N   . LEU   A 238 ? 0.1724 0.2104 0.2194 -0.0142 0.0213  -0.0101 237 LEU   A N   
1819 C CA  . LEU   A 238 ? 0.1707 0.2133 0.2244 -0.0176 0.0229  -0.0063 237 LEU   A CA  
1820 C C   . LEU   A 238 ? 0.2124 0.2578 0.2578 -0.0223 0.0287  -0.0040 237 LEU   A C   
1821 O O   . LEU   A 238 ? 0.2298 0.2784 0.2695 -0.0217 0.0340  -0.0074 237 LEU   A O   
1822 C CB  . LEU   A 238 ? 0.1599 0.2104 0.2291 -0.0151 0.0246  -0.0091 237 LEU   A CB  
1823 C CG  . LEU   A 238 ? 0.1579 0.2049 0.2341 -0.0112 0.0186  -0.0098 237 LEU   A CG  
1824 C CD1 . LEU   A 238 ? 0.1512 0.2048 0.2404 -0.0073 0.0201  -0.0138 237 LEU   A CD1 
1825 C CD2 . LEU   A 238 ? 0.1719 0.2156 0.2500 -0.0132 0.0138  -0.0055 237 LEU   A CD2 
1826 N N   . LYS   A 239 ? 0.2162 0.2597 0.2602 -0.0270 0.0278  0.0018  238 LYS   A N   
1827 C CA  . LYS   A 239 ? 0.2512 0.2961 0.2869 -0.0325 0.0328  0.0058  238 LYS   A CA  
1828 C C   . LYS   A 239 ? 0.2735 0.3308 0.3176 -0.0344 0.0417  0.0043  238 LYS   A C   
1829 O O   . LYS   A 239 ? 0.2950 0.3557 0.3301 -0.0361 0.0485  0.0038  238 LYS   A O   
1830 C CB  . LYS   A 239 ? 0.3022 0.3402 0.3365 -0.0369 0.0282  0.0126  238 LYS   A CB  
1831 C CG  . LYS   A 239 ? 0.4023 0.4413 0.4308 -0.0437 0.0330  0.0184  238 LYS   A CG  
1832 C CD  . LYS   A 239 ? 0.4932 0.5256 0.5250 -0.0480 0.0280  0.0244  238 LYS   A CD  
1833 C CE  . LYS   A 239 ? 0.5615 0.5943 0.5882 -0.0556 0.0328  0.0310  238 LYS   A CE  
1834 N NZ  . LYS   A 239 ? 0.6105 0.6331 0.6376 -0.0596 0.0266  0.0370  238 LYS   A NZ  
1835 N N   . GLU   A 240 ? 0.2682 0.3326 0.3296 -0.0342 0.0416  0.0036  239 GLU   A N   
1836 C CA  . GLU   A 240 ? 0.2713 0.3494 0.3442 -0.0362 0.0499  0.0026  239 GLU   A CA  
1837 C C   . GLU   A 240 ? 0.2755 0.3613 0.3585 -0.0298 0.0525  -0.0047 239 GLU   A C   
1838 O O   . GLU   A 240 ? 0.2693 0.3575 0.3663 -0.0268 0.0482  -0.0065 239 GLU   A O   
1839 C CB  . GLU   A 240 ? 0.2948 0.3769 0.3821 -0.0406 0.0477  0.0067  239 GLU   A CB  
1840 C CG  . GLU   A 240 ? 0.3585 0.4325 0.4372 -0.0474 0.0454  0.0141  239 GLU   A CG  
1841 C CD  . GLU   A 240 ? 0.4107 0.4897 0.5049 -0.0526 0.0440  0.0175  239 GLU   A CD  
1842 O OE1 . GLU   A 240 ? 0.3793 0.4496 0.4751 -0.0533 0.0356  0.0194  239 GLU   A OE1 
1843 O OE2 . GLU   A 240 ? 0.4651 0.5574 0.5708 -0.0558 0.0514  0.0178  239 GLU   A OE2 
1844 N N   . LYS   A 241 ? 0.2822 0.3707 0.3572 -0.0273 0.0591  -0.0092 240 LYS   A N   
1845 C CA  . LYS   A 241 ? 0.2802 0.3739 0.3630 -0.0205 0.0615  -0.0169 240 LYS   A CA  
1846 C C   . LYS   A 241 ? 0.2579 0.3648 0.3630 -0.0189 0.0643  -0.0187 240 LYS   A C   
1847 O O   . LYS   A 241 ? 0.2562 0.3633 0.3723 -0.0134 0.0601  -0.0224 240 LYS   A O   
1848 C CB  . LYS   A 241 ? 0.3235 0.4183 0.3927 -0.0190 0.0692  -0.0216 240 LYS   A CB  
1849 C CG  . LYS   A 241 ? 0.3903 0.4869 0.4651 -0.0113 0.0706  -0.0305 240 LYS   A CG  
1850 C CD  . LYS   A 241 ? 0.4627 0.5571 0.5206 -0.0096 0.0765  -0.0359 240 LYS   A CD  
1851 C CE  . LYS   A 241 ? 0.5156 0.6165 0.5823 -0.0027 0.0820  -0.0450 240 LYS   A CE  
1852 N NZ  . LYS   A 241 ? 0.5554 0.6449 0.6162 0.0027  0.0759  -0.0511 240 LYS   A NZ  
1853 N N   . GLY   A 242 ? 0.2377 0.3554 0.3499 -0.0240 0.0710  -0.0155 241 GLY   A N   
1854 C CA  . GLY   A 242 ? 0.2175 0.3498 0.3528 -0.0230 0.0740  -0.0169 241 GLY   A CA  
1855 C C   . GLY   A 242 ? 0.2004 0.3321 0.3501 -0.0238 0.0647  -0.0140 241 GLY   A C   
1856 O O   . GLY   A 242 ? 0.1888 0.3323 0.3589 -0.0222 0.0652  -0.0155 241 GLY   A O   
1857 N N   . LYS   A 243 ? 0.1897 0.3082 0.3294 -0.0261 0.0562  -0.0099 242 LYS   A N   
1858 C CA  . LYS   A 243 ? 0.1795 0.2958 0.3299 -0.0267 0.0471  -0.0076 242 LYS   A CA  
1859 C C   . LYS   A 243 ? 0.1820 0.2942 0.3369 -0.0192 0.0403  -0.0117 242 LYS   A C   
1860 O O   . LYS   A 243 ? 0.1941 0.3073 0.3602 -0.0185 0.0335  -0.0109 242 LYS   A O   
1861 C CB  . LYS   A 243 ? 0.1948 0.2987 0.3329 -0.0321 0.0413  -0.0018 242 LYS   A CB  
1862 C CG  . LYS   A 243 ? 0.2161 0.3167 0.3628 -0.0335 0.0321  0.0005  242 LYS   A CG  
1863 C CD  . LYS   A 243 ? 0.2728 0.3621 0.4084 -0.0393 0.0280  0.0060  242 LYS   A CD  
1864 C CE  . LYS   A 243 ? 0.2976 0.3826 0.4404 -0.0406 0.0188  0.0072  242 LYS   A CE  
1865 N NZ  . LYS   A 243 ? 0.3238 0.3979 0.4577 -0.0464 0.0152  0.0122  242 LYS   A NZ  
1866 N N   . TRP   A 244 ? 0.1643 0.2711 0.3098 -0.0139 0.0417  -0.0159 243 TRP   A N   
1867 C CA  . TRP   A 244 ? 0.1639 0.2642 0.3109 -0.0075 0.0352  -0.0187 243 TRP   A CA  
1868 C C   . TRP   A 244 ? 0.1611 0.2660 0.3141 -0.0010 0.0393  -0.0251 243 TRP   A C   
1869 O O   . TRP   A 244 ? 0.1688 0.2784 0.3179 -0.0008 0.0475  -0.0283 243 TRP   A O   
1870 C CB  . TRP   A 244 ? 0.1700 0.2557 0.2993 -0.0077 0.0304  -0.0170 243 TRP   A CB  
1871 C CG  . TRP   A 244 ? 0.1722 0.2524 0.2939 -0.0136 0.0273  -0.0113 243 TRP   A CG  
1872 C CD1 . TRP   A 244 ? 0.1828 0.2590 0.2915 -0.0181 0.0301  -0.0085 243 TRP   A CD1 
1873 C CD2 . TRP   A 244 ? 0.1772 0.2552 0.3042 -0.0156 0.0206  -0.0080 243 TRP   A CD2 
1874 N NE1 . TRP   A 244 ? 0.1927 0.2634 0.2988 -0.0223 0.0254  -0.0036 243 TRP   A NE1 
1875 C CE2 . TRP   A 244 ? 0.1867 0.2582 0.3034 -0.0208 0.0196  -0.0037 243 TRP   A CE2 
1876 C CE3 . TRP   A 244 ? 0.1850 0.2649 0.3234 -0.0131 0.0148  -0.0084 243 TRP   A CE3 
1877 C CZ2 . TRP   A 244 ? 0.1954 0.2620 0.3133 -0.0235 0.0133  -0.0005 243 TRP   A CZ2 
1878 C CZ3 . TRP   A 244 ? 0.1863 0.2617 0.3246 -0.0160 0.0084  -0.0053 243 TRP   A CZ3 
1879 C CH2 . TRP   A 244 ? 0.1875 0.2561 0.3158 -0.0210 0.0078  -0.0017 243 TRP   A CH2 
1880 N N   . SER   A 245 ? 0.1492 0.2521 0.3109 0.0045  0.0336  -0.0269 244 SER   A N   
1881 C CA  . SER   A 245 ? 0.1495 0.2555 0.3186 0.0114  0.0365  -0.0331 244 SER   A CA  
1882 C C   . SER   A 245 ? 0.1702 0.2653 0.3242 0.0138  0.0375  -0.0365 244 SER   A C   
1883 O O   . SER   A 245 ? 0.1708 0.2552 0.3109 0.0111  0.0335  -0.0336 244 SER   A O   
1884 C CB  . SER   A 245 ? 0.1542 0.2602 0.3372 0.0166  0.0293  -0.0333 244 SER   A CB  
1885 O OG  . SER   A 245 ? 0.1743 0.2664 0.3473 0.0181  0.0219  -0.0314 244 SER   A OG  
1886 N N   . ALA   A 246 ? 0.1797 0.2771 0.3379 0.0193  0.0418  -0.0431 245 ALA   A N   
1887 C CA  . ALA   A 246 ? 0.1966 0.2829 0.3421 0.0220  0.0416  -0.0474 245 ALA   A CA  
1888 C C   . ALA   A 246 ? 0.1927 0.2665 0.3353 0.0233  0.0323  -0.0446 245 ALA   A C   
1889 O O   . ALA   A 246 ? 0.1892 0.2529 0.3181 0.0214  0.0302  -0.0442 245 ALA   A O   
1890 C CB  . ALA   A 246 ? 0.2126 0.3027 0.3658 0.0287  0.0467  -0.0555 245 ALA   A CB  
1891 N N   . ALA   A 247 ? 0.1763 0.2512 0.3314 0.0258  0.0267  -0.0420 246 ALA   A N   
1892 C CA  . ALA   A 247 ? 0.1729 0.2364 0.3246 0.0267  0.0185  -0.0385 246 ALA   A CA  
1893 C C   . ALA   A 247 ? 0.1654 0.2232 0.3040 0.0209  0.0157  -0.0329 246 ALA   A C   
1894 O O   . ALA   A 247 ? 0.1729 0.2208 0.3029 0.0206  0.0123  -0.0316 246 ALA   A O   
1895 C CB  . ALA   A 247 ? 0.1758 0.2423 0.3413 0.0300  0.0131  -0.0361 246 ALA   A CB  
1896 N N   . PHE   A 248 ? 0.1447 0.2089 0.2830 0.0164  0.0171  -0.0297 247 PHE   A N   
1897 C CA  . PHE   A 248 ? 0.1490 0.2075 0.2756 0.0116  0.0144  -0.0248 247 PHE   A CA  
1898 C C   . PHE   A 248 ? 0.1549 0.2089 0.2680 0.0093  0.0177  -0.0263 247 PHE   A C   
1899 O O   . PHE   A 248 ? 0.1637 0.2094 0.2679 0.0084  0.0141  -0.0243 247 PHE   A O   
1900 C CB  . PHE   A 248 ? 0.1346 0.1997 0.2653 0.0075  0.0142  -0.0212 247 PHE   A CB  
1901 C CG  . PHE   A 248 ? 0.1410 0.1997 0.2617 0.0034  0.0105  -0.0165 247 PHE   A CG  
1902 C CD1 . PHE   A 248 ? 0.1485 0.1975 0.2596 0.0042  0.0068  -0.0150 247 PHE   A CD1 
1903 C CD2 . PHE   A 248 ? 0.1520 0.2146 0.2743 -0.0011 0.0106  -0.0136 247 PHE   A CD2 
1904 C CE1 . PHE   A 248 ? 0.1540 0.1977 0.2568 0.0013  0.0039  -0.0112 247 PHE   A CE1 
1905 C CE2 . PHE   A 248 ? 0.1577 0.2133 0.2711 -0.0042 0.0069  -0.0098 247 PHE   A CE2 
1906 C CZ  . PHE   A 248 ? 0.1517 0.1982 0.2554 -0.0025 0.0038  -0.0089 247 PHE   A CZ  
1907 N N   . HIS   A 249 ? 0.1415 0.2010 0.2531 0.0089  0.0243  -0.0301 248 HIS   A N   
1908 C CA  . HIS   A 249 ? 0.1489 0.2033 0.2460 0.0070  0.0266  -0.0318 248 HIS   A CA  
1909 C C   . HIS   A 249 ? 0.1499 0.1948 0.2431 0.0101  0.0229  -0.0349 248 HIS   A C   
1910 O O   . HIS   A 249 ? 0.1620 0.2001 0.2444 0.0080  0.0203  -0.0337 248 HIS   A O   
1911 C CB  . HIS   A 249 ? 0.1609 0.2228 0.2563 0.0068  0.0349  -0.0360 248 HIS   A CB  
1912 C CG  . HIS   A 249 ? 0.1869 0.2559 0.2812 0.0016  0.0387  -0.0317 248 HIS   A CG  
1913 N ND1 . HIS   A 249 ? 0.2127 0.2939 0.3190 0.0014  0.0445  -0.0324 248 HIS   A ND1 
1914 C CD2 . HIS   A 249 ? 0.1876 0.2529 0.2714 -0.0037 0.0372  -0.0264 248 HIS   A CD2 
1915 C CE1 . HIS   A 249 ? 0.1984 0.2824 0.3004 -0.0046 0.0466  -0.0274 248 HIS   A CE1 
1916 N NE2 . HIS   A 249 ? 0.2178 0.2916 0.3057 -0.0076 0.0421  -0.0236 248 HIS   A NE2 
1917 N N   . ASN   A 250 ? 0.1387 0.1832 0.2418 0.0151  0.0221  -0.0384 249 ASN   A N   
1918 C CA  . ASN   A 250 ? 0.1391 0.1737 0.2399 0.0175  0.0183  -0.0410 249 ASN   A CA  
1919 C C   . ASN   A 250 ? 0.1526 0.1807 0.2521 0.0159  0.0119  -0.0351 249 ASN   A C   
1920 O O   . ASN   A 250 ? 0.1638 0.1845 0.2569 0.0147  0.0091  -0.0351 249 ASN   A O   
1921 C CB  . ASN   A 250 ? 0.1557 0.1901 0.2679 0.0234  0.0185  -0.0456 249 ASN   A CB  
1922 C CG  . ASN   A 250 ? 0.1874 0.2107 0.2968 0.0251  0.0148  -0.0484 249 ASN   A CG  
1923 O OD1 . ASN   A 250 ? 0.1792 0.1962 0.2931 0.0261  0.0094  -0.0450 249 ASN   A OD1 
1924 N ND2 . ASN   A 250 ? 0.2261 0.2463 0.3267 0.0249  0.0173  -0.0542 249 ASN   A ND2 
1925 N N   . PHE   A 251 ? 0.1448 0.1761 0.2503 0.0157  0.0097  -0.0302 250 PHE   A N   
1926 C CA  . PHE   A 251 ? 0.1401 0.1660 0.2431 0.0144  0.0046  -0.0247 250 PHE   A CA  
1927 C C   . PHE   A 251 ? 0.1420 0.1655 0.2341 0.0102  0.0043  -0.0224 250 PHE   A C   
1928 O O   . PHE   A 251 ? 0.1516 0.1693 0.2401 0.0095  0.0013  -0.0205 250 PHE   A O   
1929 C CB  . PHE   A 251 ? 0.1431 0.1730 0.2519 0.0146  0.0025  -0.0207 250 PHE   A CB  
1930 C CG  . PHE   A 251 ? 0.1466 0.1712 0.2517 0.0139  -0.0021 -0.0156 250 PHE   A CG  
1931 C CD1 . PHE   A 251 ? 0.1500 0.1742 0.2478 0.0107  -0.0026 -0.0124 250 PHE   A CD1 
1932 C CD2 . PHE   A 251 ? 0.1421 0.1620 0.2508 0.0168  -0.0056 -0.0137 250 PHE   A CD2 
1933 C CE1 . PHE   A 251 ? 0.1629 0.1829 0.2572 0.0108  -0.0059 -0.0083 250 PHE   A CE1 
1934 C CE2 . PHE   A 251 ? 0.1548 0.1704 0.2589 0.0162  -0.0087 -0.0088 250 PHE   A CE2 
1935 C CZ  . PHE   A 251 ? 0.1650 0.1811 0.2620 0.0134  -0.0085 -0.0066 250 PHE   A CZ  
1936 N N   . ILE   A 252 ? 0.1406 0.1688 0.2281 0.0075  0.0075  -0.0225 251 ILE   A N   
1937 C CA  . ILE   A 252 ? 0.1501 0.1756 0.2271 0.0040  0.0067  -0.0202 251 ILE   A CA  
1938 C C   . ILE   A 252 ? 0.1636 0.1845 0.2342 0.0039  0.0064  -0.0237 251 ILE   A C   
1939 O O   . ILE   A 252 ? 0.1725 0.1890 0.2384 0.0025  0.0030  -0.0218 251 ILE   A O   
1940 C CB  . ILE   A 252 ? 0.1501 0.1809 0.2235 0.0010  0.0103  -0.0191 251 ILE   A CB  
1941 C CG1 . ILE   A 252 ? 0.1509 0.1849 0.2305 0.0002  0.0090  -0.0154 251 ILE   A CG1 
1942 C CG2 . ILE   A 252 ? 0.1616 0.1886 0.2230 -0.0022 0.0094  -0.0172 251 ILE   A CG2 
1943 C CD1 . ILE   A 252 ? 0.1483 0.1770 0.2255 0.0000  0.0041  -0.0113 251 ILE   A CD1 
1944 N N   . LYS   A 253 ? 0.1641 0.1863 0.2352 0.0057  0.0097  -0.0293 252 LYS   A N   
1945 C CA  . LYS   A 253 ? 0.1712 0.1882 0.2352 0.0056  0.0089  -0.0337 252 LYS   A CA  
1946 C C   . LYS   A 253 ? 0.1728 0.1829 0.2405 0.0063  0.0037  -0.0332 252 LYS   A C   
1947 O O   . LYS   A 253 ? 0.1745 0.1805 0.2363 0.0041  0.0005  -0.0330 252 LYS   A O   
1948 C CB  . LYS   A 253 ? 0.1973 0.2160 0.2613 0.0082  0.0135  -0.0409 252 LYS   A CB  
1949 C CG  . LYS   A 253 ? 0.2662 0.2783 0.3211 0.0081  0.0120  -0.0464 252 LYS   A CG  
1950 C CD  . LYS   A 253 ? 0.3497 0.3626 0.4034 0.0115  0.0169  -0.0546 252 LYS   A CD  
1951 C CE  . LYS   A 253 ? 0.4192 0.4243 0.4616 0.0109  0.0144  -0.0604 252 LYS   A CE  
1952 N NZ  . LYS   A 253 ? 0.4685 0.4731 0.5082 0.0148  0.0192  -0.0694 252 LYS   A NZ  
1953 N N   . VAL   A 254 ? 0.1669 0.1759 0.2446 0.0090  0.0026  -0.0321 253 VAL   A N   
1954 C CA  . VAL   A 254 ? 0.1698 0.1718 0.2511 0.0091  -0.0018 -0.0311 253 VAL   A CA  
1955 C C   . VAL   A 254 ? 0.1685 0.1702 0.2497 0.0068  -0.0046 -0.0244 253 VAL   A C   
1956 O O   . VAL   A 254 ? 0.1790 0.1766 0.2603 0.0051  -0.0076 -0.0234 253 VAL   A O   
1957 C CB  . VAL   A 254 ? 0.1874 0.1860 0.2781 0.0129  -0.0024 -0.0327 253 VAL   A CB  
1958 C CG1 . VAL   A 254 ? 0.2018 0.2006 0.2931 0.0159  0.0008  -0.0404 253 VAL   A CG1 
1959 C CG2 . VAL   A 254 ? 0.1980 0.2004 0.2951 0.0147  -0.0024 -0.0281 253 VAL   A CG2 
1960 N N   . THR   A 255 ? 0.1597 0.1658 0.2411 0.0068  -0.0037 -0.0203 254 THR   A N   
1961 C CA  . THR   A 255 ? 0.1499 0.1559 0.2302 0.0053  -0.0057 -0.0148 254 THR   A CA  
1962 C C   . THR   A 255 ? 0.1465 0.1528 0.2201 0.0025  -0.0067 -0.0147 254 THR   A C   
1963 O O   . THR   A 255 ? 0.1597 0.1651 0.2339 0.0014  -0.0089 -0.0117 254 THR   A O   
1964 C CB  . THR   A 255 ? 0.1492 0.1585 0.2303 0.0061  -0.0052 -0.0113 254 THR   A CB  
1965 O OG1 . THR   A 255 ? 0.1330 0.1465 0.2108 0.0051  -0.0029 -0.0127 254 THR   A OG1 
1966 C CG2 . THR   A 255 ? 0.1570 0.1654 0.2445 0.0089  -0.0059 -0.0103 254 THR   A CG2 
1967 N N   . LEU   A 256 ? 0.1464 0.1545 0.2137 0.0015  -0.0050 -0.0176 255 LEU   A N   
1968 C CA  . LEU   A 256 ? 0.1530 0.1606 0.2127 -0.0009 -0.0068 -0.0171 255 LEU   A CA  
1969 C C   . LEU   A 256 ? 0.1801 0.1843 0.2367 -0.0018 -0.0088 -0.0216 255 LEU   A C   
1970 O O   . LEU   A 256 ? 0.2061 0.2100 0.2537 -0.0033 -0.0092 -0.0235 255 LEU   A O   
1971 C CB  . LEU   A 256 ? 0.1406 0.1510 0.1930 -0.0022 -0.0046 -0.0161 255 LEU   A CB  
1972 C CG  . LEU   A 256 ? 0.1544 0.1672 0.2101 -0.0018 -0.0036 -0.0121 255 LEU   A CG  
1973 C CD1 . LEU   A 256 ? 0.1534 0.1681 0.2028 -0.0039 -0.0016 -0.0107 255 LEU   A CD1 
1974 C CD2 . LEU   A 256 ? 0.1705 0.1820 0.2291 -0.0011 -0.0066 -0.0081 255 LEU   A CD2 
1975 N N   . THR   A 257 ? 0.1727 0.1734 0.2359 -0.0010 -0.0104 -0.0234 256 THR   A N   
1976 C CA  . THR   A 257 ? 0.1648 0.1608 0.2257 -0.0023 -0.0133 -0.0282 256 THR   A CA  
1977 C C   . THR   A 257 ? 0.1706 0.1671 0.2303 -0.0050 -0.0180 -0.0253 256 THR   A C   
1978 O O   . THR   A 257 ? 0.1536 0.1521 0.2202 -0.0054 -0.0191 -0.0203 256 THR   A O   
1979 C CB  . THR   A 257 ? 0.1779 0.1690 0.2473 -0.0012 -0.0145 -0.0300 256 THR   A CB  
1980 O OG1 . THR   A 257 ? 0.1912 0.1822 0.2627 0.0021  -0.0107 -0.0329 256 THR   A OG1 
1981 C CG2 . THR   A 257 ? 0.1910 0.1760 0.2585 -0.0028 -0.0184 -0.0354 256 THR   A CG2 
1982 N N   . LYS   A 258 ? 0.1697 0.1650 0.2203 -0.0067 -0.0205 -0.0283 257 LYS   A N   
1983 C CA  . LYS   A 258 ? 0.1909 0.1873 0.2404 -0.0089 -0.0257 -0.0256 257 LYS   A CA  
1984 C C   . LYS   A 258 ? 0.1817 0.1774 0.2426 -0.0105 -0.0298 -0.0244 257 LYS   A C   
1985 O O   . LYS   A 258 ? 0.1940 0.1937 0.2615 -0.0111 -0.0313 -0.0194 257 LYS   A O   
1986 C CB  . LYS   A 258 ? 0.2428 0.2367 0.2791 -0.0103 -0.0285 -0.0297 257 LYS   A CB  
1987 C CG  . LYS   A 258 ? 0.3072 0.3024 0.3417 -0.0122 -0.0348 -0.0268 257 LYS   A CG  
1988 C CD  . LYS   A 258 ? 0.3927 0.3843 0.4123 -0.0135 -0.0381 -0.0313 257 LYS   A CD  
1989 C CE  . LYS   A 258 ? 0.4499 0.4426 0.4648 -0.0149 -0.0446 -0.0278 257 LYS   A CE  
1990 N NZ  . LYS   A 258 ? 0.4879 0.4767 0.4843 -0.0159 -0.0467 -0.0312 257 LYS   A NZ  
1991 N N   . SER   A 259 ? 0.1785 0.1689 0.2423 -0.0112 -0.0313 -0.0290 258 SER   A N   
1992 C CA  . SER   A 259 ? 0.1844 0.1734 0.2598 -0.0137 -0.0352 -0.0276 258 SER   A CA  
1993 C C   . SER   A 259 ? 0.1892 0.1791 0.2748 -0.0126 -0.0314 -0.0229 258 SER   A C   
1994 O O   . SER   A 259 ? 0.2005 0.1866 0.2861 -0.0104 -0.0282 -0.0247 258 SER   A O   
1995 C CB  . SER   A 259 ? 0.2231 0.2044 0.2973 -0.0153 -0.0391 -0.0345 258 SER   A CB  
1996 O OG  . SER   A 259 ? 0.2552 0.2347 0.3424 -0.0184 -0.0426 -0.0325 258 SER   A OG  
1997 N N   . PRO   A 260 ? 0.1745 0.1692 0.2692 -0.0140 -0.0318 -0.0170 259 PRO   A N   
1998 C CA  . PRO   A 260 ? 0.1814 0.1764 0.2840 -0.0133 -0.0282 -0.0121 259 PRO   A CA  
1999 C C   . PRO   A 260 ? 0.1914 0.1787 0.3001 -0.0149 -0.0296 -0.0138 259 PRO   A C   
2000 O O   . PRO   A 260 ? 0.2183 0.2030 0.3294 -0.0131 -0.0266 -0.0114 259 PRO   A O   
2001 C CB  . PRO   A 260 ? 0.1927 0.1949 0.3030 -0.0146 -0.0280 -0.0061 259 PRO   A CB  
2002 C CG  . PRO   A 260 ? 0.2011 0.2067 0.3106 -0.0163 -0.0328 -0.0079 259 PRO   A CG  
2003 C CD  . PRO   A 260 ? 0.1718 0.1724 0.2698 -0.0160 -0.0354 -0.0143 259 PRO   A CD  
2004 N N   . LYS   A 261 ? 0.1750 0.1579 0.2853 -0.0179 -0.0347 -0.0184 260 LYS   A N   
2005 C CA  . LYS   A 261 ? 0.1778 0.1515 0.2937 -0.0195 -0.0369 -0.0207 260 LYS   A CA  
2006 C C   . LYS   A 261 ? 0.1925 0.1592 0.3019 -0.0153 -0.0346 -0.0260 260 LYS   A C   
2007 O O   . LYS   A 261 ? 0.2072 0.1653 0.3212 -0.0153 -0.0359 -0.0277 260 LYS   A O   
2008 C CB  . LYS   A 261 ? 0.2081 0.1780 0.3266 -0.0238 -0.0438 -0.0252 260 LYS   A CB  
2009 C CG  . LYS   A 261 ? 0.2525 0.2298 0.3811 -0.0283 -0.0467 -0.0203 260 LYS   A CG  
2010 C CD  . LYS   A 261 ? 0.3010 0.2745 0.4317 -0.0327 -0.0549 -0.0256 260 LYS   A CD  
2011 C CE  . LYS   A 261 ? 0.3557 0.3387 0.4972 -0.0368 -0.0587 -0.0213 260 LYS   A CE  
2012 N NZ  . LYS   A 261 ? 0.3850 0.3652 0.5257 -0.0404 -0.0680 -0.0274 260 LYS   A NZ  
2013 N N   . LYS   A 262 ? 0.1883 0.1588 0.2879 -0.0117 -0.0314 -0.0286 261 LYS   A N   
2014 C CA  . LYS   A 262 ? 0.1939 0.1604 0.2889 -0.0073 -0.0284 -0.0335 261 LYS   A CA  
2015 C C   . LYS   A 262 ? 0.1910 0.1632 0.2857 -0.0039 -0.0232 -0.0292 261 LYS   A C   
2016 O O   . LYS   A 262 ? 0.2113 0.1818 0.3049 -0.0001 -0.0207 -0.0324 261 LYS   A O   
2017 C CB  . LYS   A 262 ? 0.2155 0.1818 0.2991 -0.0064 -0.0286 -0.0411 261 LYS   A CB  
2018 C CG  . LYS   A 262 ? 0.2551 0.2137 0.3373 -0.0091 -0.0343 -0.0474 261 LYS   A CG  
2019 C CD  . LYS   A 262 ? 0.3486 0.3087 0.4175 -0.0095 -0.0356 -0.0527 261 LYS   A CD  
2020 C CE  . LYS   A 262 ? 0.4244 0.3787 0.4847 -0.0062 -0.0337 -0.0620 261 LYS   A CE  
2021 N NZ  . LYS   A 262 ? 0.4751 0.4237 0.5259 -0.0086 -0.0395 -0.0690 261 LYS   A NZ  
2022 N N   . ARG   A 263 ? 0.1720 0.1508 0.2679 -0.0049 -0.0220 -0.0225 262 ARG   A N   
2023 C CA  . ARG   A 263 ? 0.1655 0.1493 0.2600 -0.0021 -0.0181 -0.0187 262 ARG   A CA  
2024 C C   . ARG   A 263 ? 0.1758 0.1564 0.2770 -0.0007 -0.0175 -0.0144 262 ARG   A C   
2025 O O   . ARG   A 263 ? 0.1820 0.1605 0.2888 -0.0032 -0.0189 -0.0100 262 ARG   A O   
2026 C CB  . ARG   A 263 ? 0.1495 0.1404 0.2417 -0.0035 -0.0176 -0.0141 262 ARG   A CB  
2027 C CG  . ARG   A 263 ? 0.1330 0.1284 0.2214 -0.0009 -0.0143 -0.0118 262 ARG   A CG  
2028 C CD  . ARG   A 263 ? 0.1565 0.1571 0.2423 -0.0018 -0.0142 -0.0081 262 ARG   A CD  
2029 N NE  . ARG   A 263 ? 0.1453 0.1469 0.2271 -0.0038 -0.0167 -0.0104 262 ARG   A NE  
2030 C CZ  . ARG   A 263 ? 0.1531 0.1578 0.2371 -0.0053 -0.0188 -0.0077 262 ARG   A CZ  
2031 N NH1 . ARG   A 263 ? 0.1398 0.1473 0.2299 -0.0050 -0.0177 -0.0029 262 ARG   A NH1 
2032 N NH2 . ARG   A 263 ? 0.1474 0.1524 0.2277 -0.0070 -0.0222 -0.0099 262 ARG   A NH2 
2033 N N   . PRO   A 264 ? 0.1728 0.1533 0.2739 0.0031  -0.0155 -0.0150 263 PRO   A N   
2034 C CA  . PRO   A 264 ? 0.1767 0.1532 0.2830 0.0047  -0.0158 -0.0105 263 PRO   A CA  
2035 C C   . PRO   A 264 ? 0.1699 0.1500 0.2758 0.0037  -0.0148 -0.0029 263 PRO   A C   
2036 O O   . PRO   A 264 ? 0.1790 0.1655 0.2804 0.0035  -0.0132 -0.0016 263 PRO   A O   
2037 C CB  . PRO   A 264 ? 0.1919 0.1695 0.2985 0.0092  -0.0145 -0.0134 263 PRO   A CB  
2038 C CG  . PRO   A 264 ? 0.2028 0.1832 0.3053 0.0097  -0.0128 -0.0209 263 PRO   A CG  
2039 C CD  . PRO   A 264 ? 0.1769 0.1612 0.2737 0.0059  -0.0129 -0.0195 263 PRO   A CD  
2040 N N   . SER   A 265 ? 0.1668 0.1418 0.2766 0.0035  -0.0157 0.0021  264 SER   A N   
2041 C CA  . SER   A 265 ? 0.1625 0.1398 0.2706 0.0030  -0.0142 0.0095  264 SER   A CA  
2042 C C   . SER   A 265 ? 0.1717 0.1515 0.2752 0.0068  -0.0135 0.0107  264 SER   A C   
2043 O O   . SER   A 265 ? 0.1781 0.1573 0.2825 0.0098  -0.0144 0.0068  264 SER   A O   
2044 C CB  . SER   A 265 ? 0.1670 0.1370 0.2797 0.0013  -0.0153 0.0149  264 SER   A CB  
2045 O OG  . SER   A 265 ? 0.1819 0.1450 0.2960 0.0046  -0.0174 0.0147  264 SER   A OG  
2046 N N   . ALA   A 266 ? 0.1674 0.1500 0.2664 0.0069  -0.0119 0.0161  265 ALA   A N   
2047 C CA  . ALA   A 266 ? 0.1749 0.1591 0.2690 0.0102  -0.0124 0.0173  265 ALA   A CA  
2048 C C   . ALA   A 266 ? 0.1833 0.1613 0.2800 0.0129  -0.0153 0.0187  265 ALA   A C   
2049 O O   . ALA   A 266 ? 0.1882 0.1676 0.2857 0.0159  -0.0170 0.0160  265 ALA   A O   
2050 C CB  . ALA   A 266 ? 0.1914 0.1781 0.2788 0.0100  -0.0103 0.0223  265 ALA   A CB  
2051 N N   . THR   A 267 ? 0.1776 0.1487 0.2768 0.0116  -0.0161 0.0230  266 THR   A N   
2052 C CA  . THR   A 267 ? 0.1874 0.1511 0.2896 0.0144  -0.0196 0.0249  266 THR   A CA  
2053 C C   . THR   A 267 ? 0.1868 0.1492 0.2963 0.0170  -0.0215 0.0175  266 THR   A C   
2054 O O   . THR   A 267 ? 0.1958 0.1578 0.3075 0.0211  -0.0239 0.0163  266 THR   A O   
2055 C CB  . THR   A 267 ? 0.2340 0.1894 0.3375 0.0118  -0.0202 0.0315  266 THR   A CB  
2056 O OG1 . THR   A 267 ? 0.2565 0.2137 0.3521 0.0106  -0.0179 0.0386  266 THR   A OG1 
2057 C CG2 . THR   A 267 ? 0.2531 0.1990 0.3606 0.0148  -0.0246 0.0331  266 THR   A CG2 
2058 N N   . LYS   A 268 ? 0.1749 0.1374 0.2877 0.0148  -0.0202 0.0124  267 LYS   A N   
2059 C CA  . LYS   A 268 ? 0.1650 0.1262 0.2831 0.0175  -0.0210 0.0046  267 LYS   A CA  
2060 C C   . LYS   A 268 ? 0.1655 0.1357 0.2826 0.0203  -0.0195 0.0005  267 LYS   A C   
2061 O O   . LYS   A 268 ? 0.1697 0.1404 0.2921 0.0245  -0.0205 -0.0032 267 LYS   A O   
2062 C CB  . LYS   A 268 ? 0.1703 0.1300 0.2895 0.0141  -0.0202 -0.0003 267 LYS   A CB  
2063 C CG  . LYS   A 268 ? 0.1694 0.1275 0.2919 0.0170  -0.0203 -0.0091 267 LYS   A CG  
2064 C CD  . LYS   A 268 ? 0.1771 0.1258 0.3065 0.0210  -0.0234 -0.0100 267 LYS   A CD  
2065 C CE  . LYS   A 268 ? 0.2172 0.1644 0.3495 0.0242  -0.0227 -0.0199 267 LYS   A CE  
2066 N NZ  . LYS   A 268 ? 0.2132 0.1517 0.3534 0.0294  -0.0256 -0.0217 267 LYS   A NZ  
2067 N N   . MET   A 269 ? 0.1559 0.1335 0.2670 0.0180  -0.0171 0.0012  268 MET   A N   
2068 C CA  . MET   A 269 ? 0.1435 0.1291 0.2536 0.0194  -0.0158 -0.0018 268 MET   A CA  
2069 C C   . MET   A 269 ? 0.1623 0.1493 0.2749 0.0229  -0.0182 0.0005  268 MET   A C   
2070 O O   . MET   A 269 ? 0.1677 0.1606 0.2843 0.0249  -0.0177 -0.0032 268 MET   A O   
2071 C CB  . MET   A 269 ? 0.1306 0.1217 0.2337 0.0163  -0.0136 -0.0005 268 MET   A CB  
2072 C CG  . MET   A 269 ? 0.1524 0.1442 0.2537 0.0135  -0.0119 -0.0040 268 MET   A CG  
2073 S SD  . MET   A 269 ? 0.1868 0.1810 0.2902 0.0146  -0.0100 -0.0122 268 MET   A SD  
2074 C CE  . MET   A 269 ? 0.1724 0.1743 0.2773 0.0168  -0.0086 -0.0127 268 MET   A CE  
2075 N N   . LEU   A 270 ? 0.1731 0.1549 0.2836 0.0235  -0.0210 0.0067  269 LEU   A N   
2076 C CA  . LEU   A 270 ? 0.1817 0.1641 0.2935 0.0270  -0.0246 0.0091  269 LEU   A CA  
2077 C C   . LEU   A 270 ? 0.1887 0.1704 0.3112 0.0315  -0.0271 0.0056  269 LEU   A C   
2078 O O   . LEU   A 270 ? 0.1968 0.1820 0.3232 0.0347  -0.0303 0.0060  269 LEU   A O   
2079 C CB  . LEU   A 270 ? 0.1951 0.1714 0.3000 0.0267  -0.0271 0.0169  269 LEU   A CB  
2080 C CG  . LEU   A 270 ? 0.2322 0.2117 0.3269 0.0241  -0.0250 0.0197  269 LEU   A CG  
2081 C CD1 . LEU   A 270 ? 0.2575 0.2309 0.3447 0.0233  -0.0256 0.0272  269 LEU   A CD1 
2082 C CD2 . LEU   A 270 ? 0.2389 0.2244 0.3316 0.0256  -0.0271 0.0182  269 LEU   A CD2 
2083 N N   . SER   A 271 ? 0.1917 0.1691 0.3194 0.0322  -0.0258 0.0016  270 SER   A N   
2084 C CA  . SER   A 271 ? 0.1959 0.1729 0.3344 0.0374  -0.0275 -0.0028 270 SER   A CA  
2085 C C   . SER   A 271 ? 0.1957 0.1820 0.3387 0.0380  -0.0229 -0.0110 270 SER   A C   
2086 O O   . SER   A 271 ? 0.2030 0.1914 0.3558 0.0427  -0.0229 -0.0157 270 SER   A O   
2087 C CB  . SER   A 271 ? 0.2274 0.1925 0.3699 0.0392  -0.0300 -0.0023 270 SER   A CB  
2088 O OG  . SER   A 271 ? 0.2714 0.2317 0.4102 0.0352  -0.0275 -0.0042 270 SER   A OG  
2089 N N   . HIS   A 272 ? 0.1805 0.1731 0.3166 0.0337  -0.0190 -0.0121 271 HIS   A N   
2090 C CA  . HIS   A 272 ? 0.1676 0.1688 0.3059 0.0336  -0.0143 -0.0185 271 HIS   A CA  
2091 C C   . HIS   A 272 ? 0.1748 0.1852 0.3219 0.0366  -0.0149 -0.0190 271 HIS   A C   
2092 O O   . HIS   A 272 ? 0.1742 0.1861 0.3208 0.0363  -0.0187 -0.0141 271 HIS   A O   
2093 C CB  . HIS   A 272 ? 0.1555 0.1604 0.2839 0.0282  -0.0110 -0.0180 271 HIS   A CB  
2094 C CG  . HIS   A 272 ? 0.1456 0.1573 0.2742 0.0277  -0.0059 -0.0241 271 HIS   A CG  
2095 N ND1 . HIS   A 272 ? 0.1641 0.1859 0.2971 0.0279  -0.0036 -0.0251 271 HIS   A ND1 
2096 C CD2 . HIS   A 272 ? 0.1513 0.1610 0.2754 0.0266  -0.0029 -0.0290 271 HIS   A CD2 
2097 C CE1 . HIS   A 272 ? 0.1675 0.1932 0.2983 0.0270  0.0016  -0.0302 271 HIS   A CE1 
2098 N NE2 . HIS   A 272 ? 0.1603 0.1787 0.2847 0.0263  0.0020  -0.0328 271 HIS   A NE2 
2099 N N   . GLN   A 273 ? 0.1797 0.1969 0.3349 0.0392  -0.0112 -0.0252 272 GLN   A N   
2100 C CA  . GLN   A 273 ? 0.1810 0.2089 0.3479 0.0420  -0.0113 -0.0264 272 GLN   A CA  
2101 C C   . GLN   A 273 ? 0.1705 0.2057 0.3346 0.0379  -0.0120 -0.0225 272 GLN   A C   
2102 O O   . GLN   A 273 ? 0.1782 0.2184 0.3502 0.0395  -0.0160 -0.0203 272 GLN   A O   
2103 C CB  . GLN   A 273 ? 0.2282 0.2639 0.4018 0.0441  -0.0046 -0.0340 272 GLN   A CB  
2104 C CG  . GLN   A 273 ? 0.2950 0.3443 0.4835 0.0469  -0.0033 -0.0358 272 GLN   A CG  
2105 C CD  . GLN   A 273 ? 0.3733 0.4315 0.5675 0.0487  0.0050  -0.0432 272 GLN   A CD  
2106 O OE1 . GLN   A 273 ? 0.3968 0.4505 0.5821 0.0480  0.0096  -0.0476 272 GLN   A OE1 
2107 N NE2 . GLN   A 273 ? 0.3879 0.4596 0.5968 0.0509  0.0071  -0.0448 272 GLN   A NE2 
2108 N N   . LEU   A 274 ? 0.1618 0.1968 0.3147 0.0325  -0.0089 -0.0216 273 LEU   A N   
2109 C CA  . LEU   A 274 ? 0.1535 0.1943 0.3040 0.0287  -0.0096 -0.0185 273 LEU   A CA  
2110 C C   . LEU   A 274 ? 0.1648 0.2008 0.3122 0.0290  -0.0165 -0.0130 273 LEU   A C   
2111 O O   . LEU   A 274 ? 0.1724 0.2138 0.3242 0.0285  -0.0196 -0.0115 273 LEU   A O   
2112 C CB  . LEU   A 274 ? 0.1475 0.1874 0.2864 0.0235  -0.0057 -0.0183 273 LEU   A CB  
2113 C CG  . LEU   A 274 ? 0.1519 0.1978 0.2896 0.0194  -0.0056 -0.0162 273 LEU   A CG  
2114 C CD1 . LEU   A 274 ? 0.1601 0.2173 0.3079 0.0188  -0.0010 -0.0194 273 LEU   A CD1 
2115 C CD2 . LEU   A 274 ? 0.1571 0.1986 0.2819 0.0150  -0.0040 -0.0144 273 LEU   A CD2 
2116 N N   . VAL   A 275 ? 0.1595 0.1855 0.2996 0.0297  -0.0190 -0.0100 274 VAL   A N   
2117 C CA  . VAL   A 275 ? 0.1595 0.1804 0.2933 0.0298  -0.0245 -0.0044 274 VAL   A CA  
2118 C C   . VAL   A 275 ? 0.1830 0.1993 0.3218 0.0344  -0.0300 -0.0020 274 VAL   A C   
2119 O O   . VAL   A 275 ? 0.2022 0.2142 0.3346 0.0347  -0.0348 0.0028  274 VAL   A O   
2120 C CB  . VAL   A 275 ? 0.1657 0.1795 0.2863 0.0267  -0.0231 -0.0014 274 VAL   A CB  
2121 C CG1 . VAL   A 275 ? 0.1606 0.1785 0.2760 0.0226  -0.0193 -0.0030 274 VAL   A CG1 
2122 C CG2 . VAL   A 275 ? 0.1804 0.1873 0.3005 0.0274  -0.0214 -0.0017 274 VAL   A CG2 
2123 N N   . SER   A 276 ? 0.1861 0.2020 0.3348 0.0381  -0.0294 -0.0050 275 SER   A N   
2124 C CA  . SER   A 276 ? 0.1984 0.2092 0.3531 0.0431  -0.0353 -0.0026 275 SER   A CA  
2125 C C   . SER   A 276 ? 0.2123 0.2327 0.3818 0.0470  -0.0382 -0.0050 275 SER   A C   
2126 O O   . SER   A 276 ? 0.2238 0.2412 0.3998 0.0517  -0.0442 -0.0029 275 SER   A O   
2127 C CB  . SER   A 276 ? 0.2207 0.2227 0.3775 0.0455  -0.0341 -0.0040 275 SER   A CB  
2128 O OG  . SER   A 276 ? 0.2536 0.2611 0.4190 0.0470  -0.0291 -0.0113 275 SER   A OG  
2129 N N   . GLN   A 277 ? 0.2036 0.2358 0.3792 0.0449  -0.0342 -0.0091 276 GLN   A N   
2130 C CA  . GLN   A 277 ? 0.1995 0.2431 0.3916 0.0480  -0.0362 -0.0115 276 GLN   A CA  
2131 C C   . GLN   A 277 ? 0.2095 0.2538 0.4021 0.0484  -0.0451 -0.0069 276 GLN   A C   
2132 O O   . GLN   A 277 ? 0.2150 0.2536 0.3937 0.0449  -0.0478 -0.0028 276 GLN   A O   
2133 C CB  . GLN   A 277 ? 0.2026 0.2586 0.3999 0.0443  -0.0291 -0.0159 276 GLN   A CB  
2134 C CG  . GLN   A 277 ? 0.2154 0.2723 0.4020 0.0378  -0.0289 -0.0133 276 GLN   A CG  
2135 C CD  . GLN   A 277 ? 0.2127 0.2806 0.4041 0.0338  -0.0220 -0.0166 276 GLN   A CD  
2136 O OE1 . GLN   A 277 ? 0.2151 0.2807 0.3951 0.0290  -0.0176 -0.0164 276 GLN   A OE1 
2137 N NE2 . GLN   A 277 ? 0.1788 0.2590 0.3872 0.0355  -0.0211 -0.0192 276 GLN   A NE2 
2138 N N   . PRO   A 278 ? 0.2261 0.2768 0.4346 0.0533  -0.0501 -0.0076 277 PRO   A N   
2139 C CA  . PRO   A 278 ? 0.2381 0.2898 0.4472 0.0537  -0.0598 -0.0035 277 PRO   A CA  
2140 C C   . PRO   A 278 ? 0.2494 0.3103 0.4588 0.0480  -0.0597 -0.0043 277 PRO   A C   
2141 O O   . PRO   A 278 ? 0.2490 0.3187 0.4637 0.0446  -0.0522 -0.0081 277 PRO   A O   
2142 C CB  . PRO   A 278 ? 0.2360 0.2934 0.4647 0.0607  -0.0650 -0.0048 277 PRO   A CB  
2143 C CG  . PRO   A 278 ? 0.2307 0.2963 0.4729 0.0628  -0.0561 -0.0113 277 PRO   A CG  
2144 C CD  . PRO   A 278 ? 0.2195 0.2779 0.4466 0.0587  -0.0474 -0.0128 277 PRO   A CD  
2145 N N   . GLY   A 279 ? 0.2491 0.3073 0.4522 0.0470  -0.0683 -0.0007 278 GLY   A N   
2146 C CA  . GLY   A 279 ? 0.2495 0.3148 0.4536 0.0418  -0.0703 -0.0014 278 GLY   A CA  
2147 C C   . GLY   A 279 ? 0.2530 0.3117 0.4386 0.0360  -0.0663 -0.0006 278 GLY   A C   
2148 O O   . GLY   A 279 ? 0.2633 0.3275 0.4505 0.0310  -0.0658 -0.0021 278 GLY   A O   
2149 N N   . LEU   A 280 ? 0.2370 0.2839 0.4060 0.0365  -0.0636 0.0017  279 LEU   A N   
2150 C CA  . LEU   A 280 ? 0.2335 0.2741 0.3856 0.0319  -0.0601 0.0025  279 LEU   A CA  
2151 C C   . LEU   A 280 ? 0.2629 0.2943 0.3996 0.0325  -0.0674 0.0062  279 LEU   A C   
2152 O O   . LEU   A 280 ? 0.2817 0.3047 0.4098 0.0356  -0.0692 0.0098  279 LEU   A O   
2153 C CB  . LEU   A 280 ? 0.2027 0.2379 0.3475 0.0315  -0.0518 0.0023  279 LEU   A CB  
2154 C CG  . LEU   A 280 ? 0.1840 0.2264 0.3402 0.0314  -0.0442 -0.0018 279 LEU   A CG  
2155 C CD1 . LEU   A 280 ? 0.1820 0.2173 0.3280 0.0303  -0.0377 -0.0018 279 LEU   A CD1 
2156 C CD2 . LEU   A 280 ? 0.1793 0.2317 0.3425 0.0270  -0.0410 -0.0046 279 LEU   A CD2 
2157 N N   . ASN   A 281 ? 0.2689 0.3015 0.4018 0.0294  -0.0717 0.0054  280 ASN   A N   
2158 C CA  . ASN   A 281 ? 0.2702 0.2942 0.3872 0.0301  -0.0790 0.0080  280 ASN   A CA  
2159 C C   . ASN   A 281 ? 0.2596 0.2822 0.3682 0.0256  -0.0797 0.0057  280 ASN   A C   
2160 O O   . ASN   A 281 ? 0.2464 0.2755 0.3641 0.0217  -0.0756 0.0028  280 ASN   A O   
2161 C CB  . ASN   A 281 ? 0.2773 0.3035 0.4016 0.0335  -0.0895 0.0094  280 ASN   A CB  
2162 C CG  . ASN   A 281 ? 0.3203 0.3589 0.4647 0.0317  -0.0932 0.0060  280 ASN   A CG  
2163 O OD1 . ASN   A 281 ? 0.3389 0.3804 0.4837 0.0271  -0.0945 0.0036  280 ASN   A OD1 
2164 N ND2 . ASN   A 281 ? 0.3128 0.3592 0.4755 0.0353  -0.0951 0.0059  280 ASN   A ND2 
2165 N N   . ARG   A 282 ? 0.2570 0.2705 0.3477 0.0262  -0.0846 0.0070  281 ARG   A N   
2166 C CA  . ARG   A 282 ? 0.2711 0.2805 0.3511 0.0229  -0.0859 0.0044  281 ARG   A CA  
2167 C C   . ARG   A 282 ? 0.2592 0.2753 0.3520 0.0192  -0.0918 0.0011  281 ARG   A C   
2168 O O   . ARG   A 282 ? 0.2588 0.2727 0.3477 0.0154  -0.0908 -0.0015 281 ARG   A O   
2169 C CB  . ARG   A 282 ? 0.3010 0.2994 0.3589 0.0254  -0.0905 0.0060  281 ARG   A CB  
2170 C CG  . ARG   A 282 ? 0.3172 0.3144 0.3736 0.0279  -0.1020 0.0073  281 ARG   A CG  
2171 C CD  . ARG   A 282 ? 0.3711 0.3568 0.4027 0.0306  -0.1048 0.0096  281 ARG   A CD  
2172 N NE  . ARG   A 282 ? 0.4177 0.4011 0.4449 0.0327  -0.1171 0.0105  281 ARG   A NE  
2173 C CZ  . ARG   A 282 ? 0.4476 0.4285 0.4689 0.0312  -0.1259 0.0067  281 ARG   A CZ  
2174 N NH1 . ARG   A 282 ? 0.4571 0.4360 0.4745 0.0332  -0.1380 0.0078  281 ARG   A NH1 
2175 N NH2 . ARG   A 282 ? 0.4274 0.4072 0.4469 0.0275  -0.1234 0.0018  281 ARG   A NH2 
2176 N N   . GLY   A 283 ? 0.2567 0.2812 0.3661 0.0201  -0.0975 0.0012  282 GLY   A N   
2177 C CA  . GLY   A 283 ? 0.2458 0.2790 0.3712 0.0160  -0.1027 -0.0015 282 GLY   A CA  
2178 C C   . GLY   A 283 ? 0.2344 0.2745 0.3710 0.0111  -0.0938 -0.0033 282 GLY   A C   
2179 O O   . GLY   A 283 ? 0.2390 0.2817 0.3814 0.0059  -0.0964 -0.0054 282 GLY   A O   
2180 N N   . LEU   A 284 ? 0.2103 0.2525 0.3487 0.0123  -0.0836 -0.0025 283 LEU   A N   
2181 C CA  . LEU   A 284 ? 0.2029 0.2503 0.3482 0.0077  -0.0748 -0.0038 283 LEU   A CA  
2182 C C   . LEU   A 284 ? 0.2144 0.2524 0.3447 0.0040  -0.0738 -0.0045 283 LEU   A C   
2183 O O   . LEU   A 284 ? 0.2090 0.2500 0.3453 -0.0013 -0.0715 -0.0055 283 LEU   A O   
2184 C CB  . LEU   A 284 ? 0.2019 0.2507 0.3477 0.0102  -0.0651 -0.0030 283 LEU   A CB  
2185 C CG  . LEU   A 284 ? 0.2068 0.2646 0.3686 0.0141  -0.0646 -0.0032 283 LEU   A CG  
2186 C CD1 . LEU   A 284 ? 0.2076 0.2625 0.3650 0.0171  -0.0565 -0.0028 283 LEU   A CD1 
2187 C CD2 . LEU   A 284 ? 0.2114 0.2836 0.3945 0.0109  -0.0630 -0.0051 283 LEU   A CD2 
2188 N N   . ILE   A 285 ? 0.2215 0.2481 0.3327 0.0070  -0.0750 -0.0038 284 ILE   A N   
2189 C CA  . ILE   A 285 ? 0.2245 0.2416 0.3212 0.0049  -0.0742 -0.0050 284 ILE   A CA  
2190 C C   . ILE   A 285 ? 0.2484 0.2612 0.3423 0.0025  -0.0839 -0.0073 284 ILE   A C   
2191 O O   . ILE   A 285 ? 0.2622 0.2705 0.3530 -0.0014 -0.0838 -0.0091 284 ILE   A O   
2192 C CB  . ILE   A 285 ? 0.2309 0.2389 0.3095 0.0091  -0.0704 -0.0036 284 ILE   A CB  
2193 C CG1 . ILE   A 285 ? 0.2444 0.2566 0.3276 0.0104  -0.0614 -0.0017 284 ILE   A CG1 
2194 C CG2 . ILE   A 285 ? 0.2310 0.2297 0.2959 0.0078  -0.0695 -0.0055 284 ILE   A CG2 
2195 C CD1 . ILE   A 285 ? 0.2656 0.2821 0.3563 0.0062  -0.0547 -0.0025 284 ILE   A CD1 
2196 N N   . LEU   A 286 ? 0.2495 0.2639 0.3459 0.0044  -0.0928 -0.0074 285 LEU   A N   
2197 C CA  . LEU   A 286 ? 0.2645 0.2761 0.3606 0.0017  -0.1034 -0.0101 285 LEU   A CA  
2198 C C   . LEU   A 286 ? 0.2574 0.2776 0.3729 -0.0051 -0.1035 -0.0112 285 LEU   A C   
2199 O O   . LEU   A 286 ? 0.2660 0.2802 0.3785 -0.0095 -0.1077 -0.0136 285 LEU   A O   
2200 C CB  . LEU   A 286 ? 0.2694 0.2824 0.3661 0.0052  -0.1134 -0.0094 285 LEU   A CB  
2201 C CG  . LEU   A 286 ? 0.3110 0.3133 0.3851 0.0109  -0.1153 -0.0081 285 LEU   A CG  
2202 C CD1 . LEU   A 286 ? 0.3247 0.3285 0.4000 0.0141  -0.1262 -0.0068 285 LEU   A CD1 
2203 C CD2 . LEU   A 286 ? 0.3365 0.3259 0.3896 0.0105  -0.1168 -0.0113 285 LEU   A CD2 
2204 N N   . ASP   A 287 ? 0.2447 0.2779 0.3791 -0.0061 -0.0976 -0.0094 286 ASP   A N   
2205 C CA  . ASP   A 287 ? 0.2414 0.2845 0.3947 -0.0129 -0.0952 -0.0096 286 ASP   A CA  
2206 C C   . ASP   A 287 ? 0.2420 0.2776 0.3863 -0.0169 -0.0886 -0.0096 286 ASP   A C   
2207 O O   . ASP   A 287 ? 0.2517 0.2868 0.4019 -0.0232 -0.0909 -0.0102 286 ASP   A O   
2208 C CB  . ASP   A 287 ? 0.2666 0.3248 0.4389 -0.0119 -0.0878 -0.0080 286 ASP   A CB  
2209 C CG  . ASP   A 287 ? 0.3361 0.4037 0.5221 -0.0078 -0.0940 -0.0080 286 ASP   A CG  
2210 O OD1 . ASP   A 287 ? 0.3397 0.4053 0.5258 -0.0078 -0.1054 -0.0089 286 ASP   A OD1 
2211 O OD2 . ASP   A 287 ? 0.3586 0.4350 0.5549 -0.0044 -0.0879 -0.0072 286 ASP   A OD2 
2212 N N   . LEU   A 288 ? 0.2385 0.2684 0.3696 -0.0134 -0.0807 -0.0085 287 LEU   A N   
2213 C CA  . LEU   A 288 ? 0.2335 0.2558 0.3553 -0.0160 -0.0749 -0.0082 287 LEU   A CA  
2214 C C   . LEU   A 288 ? 0.2542 0.2631 0.3629 -0.0173 -0.0821 -0.0106 287 LEU   A C   
2215 O O   . LEU   A 288 ? 0.2554 0.2604 0.3658 -0.0225 -0.0821 -0.0108 287 LEU   A O   
2216 C CB  . LEU   A 288 ? 0.2330 0.2521 0.3435 -0.0111 -0.0669 -0.0069 287 LEU   A CB  
2217 C CG  . LEU   A 288 ? 0.2428 0.2550 0.3444 -0.0129 -0.0609 -0.0062 287 LEU   A CG  
2218 C CD1 . LEU   A 288 ? 0.2464 0.2662 0.3600 -0.0186 -0.0552 -0.0044 287 LEU   A CD1 
2219 C CD2 . LEU   A 288 ? 0.2407 0.2499 0.3316 -0.0077 -0.0550 -0.0053 287 LEU   A CD2 
2220 N N   . LEU   A 289 ? 0.2715 0.2730 0.3673 -0.0126 -0.0884 -0.0126 288 LEU   A N   
2221 C CA  . LEU   A 289 ? 0.3021 0.2903 0.3840 -0.0129 -0.0954 -0.0160 288 LEU   A CA  
2222 C C   . LEU   A 289 ? 0.3317 0.3204 0.4243 -0.0191 -0.1047 -0.0181 288 LEU   A C   
2223 O O   . LEU   A 289 ? 0.3399 0.3177 0.4255 -0.0218 -0.1087 -0.0208 288 LEU   A O   
2224 C CB  . LEU   A 289 ? 0.3106 0.2917 0.3750 -0.0062 -0.0993 -0.0175 288 LEU   A CB  
2225 C CG  . LEU   A 289 ? 0.3290 0.3082 0.3818 -0.0006 -0.0904 -0.0154 288 LEU   A CG  
2226 C CD1 . LEU   A 289 ? 0.3526 0.3257 0.3886 0.0052  -0.0941 -0.0160 288 LEU   A CD1 
2227 C CD2 . LEU   A 289 ? 0.3321 0.3041 0.3774 -0.0010 -0.0840 -0.0161 288 LEU   A CD2 
2228 N N   . ASP   A 290 ? 0.3381 0.3397 0.4492 -0.0214 -0.1080 -0.0169 289 ASP   A N   
2229 C CA  . ASP   A 290 ? 0.3589 0.3637 0.4844 -0.0283 -0.1165 -0.0183 289 ASP   A CA  
2230 C C   . ASP   A 290 ? 0.3785 0.3834 0.5127 -0.0357 -0.1112 -0.0167 289 ASP   A C   
2231 O O   . ASP   A 290 ? 0.3781 0.3774 0.5157 -0.0416 -0.1182 -0.0185 289 ASP   A O   
2232 C CB  . ASP   A 290 ? 0.3774 0.3985 0.5238 -0.0288 -0.1199 -0.0169 289 ASP   A CB  
2233 C CG  . ASP   A 290 ? 0.4816 0.5010 0.6219 -0.0238 -0.1305 -0.0187 289 ASP   A CG  
2234 O OD1 . ASP   A 290 ? 0.5195 0.5246 0.6391 -0.0212 -0.1366 -0.0217 289 ASP   A OD1 
2235 O OD2 . ASP   A 290 ? 0.5116 0.5436 0.6673 -0.0222 -0.1330 -0.0172 289 ASP   A OD2 
2236 N N   . LYS   A 291 ? 0.3918 0.4015 0.5281 -0.0356 -0.0994 -0.0133 290 LYS   A N   
2237 C CA  . LYS   A 291 ? 0.4156 0.4245 0.5574 -0.0423 -0.0938 -0.0108 290 LYS   A CA  
2238 C C   . LYS   A 291 ? 0.4570 0.4476 0.5827 -0.0432 -0.0967 -0.0127 290 LYS   A C   
2239 O O   . LYS   A 291 ? 0.4608 0.4478 0.5916 -0.0500 -0.0959 -0.0109 290 LYS   A O   
2240 C CB  . LYS   A 291 ? 0.4285 0.4450 0.5721 -0.0410 -0.0812 -0.0072 290 LYS   A CB  
2241 C CG  . LYS   A 291 ? 0.4423 0.4772 0.6047 -0.0415 -0.0766 -0.0054 290 LYS   A CG  
2242 C CD  . LYS   A 291 ? 0.4720 0.5123 0.6344 -0.0413 -0.0643 -0.0024 290 LYS   A CD  
2243 C CE  . LYS   A 291 ? 0.5099 0.5478 0.6744 -0.0491 -0.0603 0.0006  290 LYS   A CE  
2244 N NZ  . LYS   A 291 ? 0.5332 0.5763 0.6962 -0.0490 -0.0489 0.0035  290 LYS   A NZ  
2245 N N   . LEU   A 292 ? 0.4842 0.4631 0.5906 -0.0364 -0.0996 -0.0161 291 LEU   A N   
2246 C CA  . LEU   A 292 ? 0.5148 0.4762 0.6056 -0.0357 -0.1023 -0.0189 291 LEU   A CA  
2247 C C   . LEU   A 292 ? 0.5524 0.5056 0.6468 -0.0416 -0.1132 -0.0221 291 LEU   A C   
2248 O O   . LEU   A 292 ? 0.5627 0.5029 0.6515 -0.0443 -0.1148 -0.0231 291 LEU   A O   
2249 C CB  . LEU   A 292 ? 0.5176 0.4704 0.5881 -0.0267 -0.1028 -0.0223 291 LEU   A CB  
2250 C CG  . LEU   A 292 ? 0.5147 0.4724 0.5795 -0.0209 -0.0926 -0.0195 291 LEU   A CG  
2251 C CD1 . LEU   A 292 ? 0.5289 0.4797 0.5756 -0.0130 -0.0935 -0.0224 291 LEU   A CD1 
2252 C CD2 . LEU   A 292 ? 0.5153 0.4688 0.5784 -0.0222 -0.0855 -0.0171 291 LEU   A CD2 
2253 N N   . LYS   A 293 ? 0.5707 0.5306 0.6742 -0.0433 -0.1216 -0.0238 292 LYS   A N   
2254 C CA  . LYS   A 293 ? 0.6022 0.5554 0.7105 -0.0493 -0.1335 -0.0273 292 LYS   A CA  
2255 C C   . LYS   A 293 ? 0.6217 0.5783 0.7483 -0.0597 -0.1323 -0.0236 292 LYS   A C   
2256 O O   . LYS   A 293 ? 0.6361 0.5802 0.7616 -0.0649 -0.1393 -0.0259 292 LYS   A O   
2257 C CB  . LYS   A 293 ? 0.6231 0.5846 0.7380 -0.0483 -0.1429 -0.0295 292 LYS   A CB  
2258 C CG  . LYS   A 293 ? 0.6849 0.6415 0.7795 -0.0385 -0.1443 -0.0323 292 LYS   A CG  
2259 C CD  . LYS   A 293 ? 0.7334 0.7004 0.8352 -0.0367 -0.1521 -0.0327 292 LYS   A CD  
2260 C CE  . LYS   A 293 ? 0.7895 0.7511 0.8699 -0.0273 -0.1524 -0.0342 292 LYS   A CE  
2261 N NZ  . LYS   A 293 ? 0.8145 0.7858 0.9016 -0.0251 -0.1598 -0.0334 292 LYS   A NZ  
2262 N N   . ASN   A 294 ? 0.6218 0.5947 0.7645 -0.0627 -0.1231 -0.0180 293 ASN   A N   
2263 C CA  . ASN   A 294 ? 0.6297 0.6075 0.7892 -0.0727 -0.1199 -0.0133 293 ASN   A CA  
2264 C C   . ASN   A 294 ? 0.6420 0.6127 0.7924 -0.0727 -0.1099 -0.0094 293 ASN   A C   
2265 O O   . ASN   A 294 ? 0.6530 0.6076 0.7951 -0.0754 -0.1130 -0.0099 293 ASN   A O   
2266 C CB  . ASN   A 294 ? 0.6354 0.6359 0.8188 -0.0764 -0.1156 -0.0096 293 ASN   A CB  
2267 C CG  . ASN   A 294 ? 0.6810 0.6935 0.8629 -0.0687 -0.1065 -0.0083 293 ASN   A CG  
2268 O OD1 . ASN   A 294 ? 0.7025 0.7185 0.8814 -0.0621 -0.1106 -0.0112 293 ASN   A OD1 
2269 N ND2 . ASN   A 294 ? 0.6872 0.7055 0.8706 -0.0695 -0.0945 -0.0039 293 ASN   A ND2 
2270 C C1  . A1ITB B .   ? 0.3644 0.2751 0.3018 0.0386  -0.0566 -0.0370 301 A1ITB A C1  
2271 C C2  . A1ITB B .   ? 0.3529 0.2717 0.2944 0.0414  -0.0472 -0.0331 301 A1ITB A C2  
2272 C C3  . A1ITB B .   ? 0.3521 0.2716 0.3061 0.0388  -0.0465 -0.0317 301 A1ITB A C3  
2273 N N6  . A1ITB B .   ? 0.2408 0.2042 0.2267 0.0437  -0.0133 -0.0124 301 A1ITB A N6  
2274 C C7  . A1ITB B .   ? 0.3087 0.2487 0.2449 0.0491  -0.0261 -0.0232 301 A1ITB A C7  
2275 C C8  . A1ITB B .   ? 0.2760 0.2258 0.2298 0.0507  -0.0162 -0.0202 301 A1ITB A C8  
2276 C C9  . A1ITB B .   ? 0.2907 0.2323 0.2472 0.0495  -0.0223 -0.0241 301 A1ITB A C9  
2277 C C10 . A1ITB B .   ? 0.2882 0.2293 0.2549 0.0500  -0.0216 -0.0245 301 A1ITB A C10 
2278 C C11 . A1ITB B .   ? 0.2970 0.2274 0.2577 0.0546  -0.0239 -0.0306 301 A1ITB A C11 
2279 C C12 . A1ITB B .   ? 0.2928 0.2248 0.2625 0.0469  -0.0288 -0.0268 301 A1ITB A C12 
2280 C C13 . A1ITB B .   ? 0.2563 0.2164 0.2187 0.0517  -0.0081 -0.0158 301 A1ITB A C13 
2281 C C14 . A1ITB B .   ? 0.2583 0.2234 0.2145 0.0554  -0.0007 -0.0143 301 A1ITB A C14 
2282 C C15 . A1ITB B .   ? 0.2497 0.2297 0.2305 0.0520  0.0055  -0.0074 301 A1ITB A C15 
2283 C C16 . A1ITB B .   ? 0.2444 0.2197 0.2304 0.0485  -0.0014 -0.0087 301 A1ITB A C16 
2284 C C19 . A1ITB B .   ? 0.2361 0.2234 0.2465 0.0435  0.0005  -0.0029 301 A1ITB A C19 
2285 C C20 . A1ITB B .   ? 0.3265 0.2650 0.2506 0.0491  -0.0291 -0.0222 301 A1ITB A C20 
2286 O O   . A1ITB B .   ? 0.3458 0.2775 0.2638 0.0477  -0.0374 -0.0254 301 A1ITB A O   
2287 N N8  . A1ITB B .   ? 0.3235 0.2682 0.2442 0.0504  -0.0227 -0.0174 301 A1ITB A N8  
2288 N N3  . A1ITB B .   ? 0.2972 0.2456 0.2407 0.0503  -0.0181 -0.0195 301 A1ITB A N3  
2289 C C17 . A1ITB B .   ? 0.2456 0.2113 0.2233 0.0480  -0.0080 -0.0126 301 A1ITB A C17 
2290 C C18 . A1ITB B .   ? 0.2269 0.1978 0.2240 0.0421  -0.0101 -0.0089 301 A1ITB A C18 
2291 N N7  . A1ITB B .   ? 0.2340 0.2122 0.2325 0.0447  -0.0035 -0.0067 301 A1ITB A N7  
2292 N N5  . A1ITB B .   ? 0.2613 0.2364 0.2269 0.0554  0.0063  -0.0100 301 A1ITB A N5  
2293 N N4  . A1ITB B .   ? 0.2999 0.2330 0.2494 0.0478  -0.0298 -0.0276 301 A1ITB A N4  
2294 C C6  . A1ITB B .   ? 0.3166 0.2493 0.2565 0.0476  -0.0319 -0.0274 301 A1ITB A C6  
2295 N N2  . A1ITB B .   ? 0.3370 0.2613 0.2708 0.0455  -0.0408 -0.0311 301 A1ITB A N2  
2296 N N   . A1ITB B .   ? 0.3645 0.2767 0.3213 0.0345  -0.0542 -0.0340 301 A1ITB A N   
2297 C C4  . A1ITB B .   ? 0.3778 0.2870 0.3454 0.0301  -0.0564 -0.0329 301 A1ITB A C4  
2298 C C5  . A1ITB B .   ? 0.4018 0.3002 0.3643 0.0346  -0.0565 -0.0371 301 A1ITB A C5  
2299 F F2  . A1ITB B .   ? 0.4039 0.3069 0.3654 0.0404  -0.0490 -0.0363 301 A1ITB A F2  
2300 F F1  . A1ITB B .   ? 0.4122 0.3057 0.3831 0.0306  -0.0594 -0.0357 301 A1ITB A F1  
2301 F F   . A1ITB B .   ? 0.4081 0.2957 0.3581 0.0379  -0.0611 -0.0437 301 A1ITB A F   
2302 N N1  . A1ITB B .   ? 0.3646 0.2716 0.3121 0.0342  -0.0607 -0.0375 301 A1ITB A N1  
2303 C C   . A1ITB B .   ? 0.3778 0.2839 0.3014 0.0397  -0.0625 -0.0399 301 A1ITB A C   
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